data_8R1R
# 
_entry.id   8R1R 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8R1R         pdb_00008r1r 10.2210/pdb8r1r/pdb 
WWPDB D_1292134177 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8R1R 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              paul.race1@newcastle.ac.uk 
_pdbx_contact_author.name_first         Paul 
_pdbx_contact_author.name_last          Race 
_pdbx_contact_author.name_mi            R 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0184-5630 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Back, C.R.' 1 0000-0002-9835-9171 
'Race, P.R.' 2 0000-0003-0184-5630 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;The Diels-Alderase TedJ: Structure, Function and as a Biocatalyst for the Total Synthesis of the Antibiotic (-)-13-Deoxytetrodecamycin
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Russell, J.'        1 ?                   
primary 'Back, C.R.'         2 0000-0002-9835-9171 
primary 'Perry, C.'          3 ?                   
primary 'Cheung, K.'         4 ?                   
primary 'Hayes, M.A.'        5 ?                   
primary 'van der Kamp, M.W.' 6 ?                   
primary 'Race, P.R.'         7 ?                   
primary 'Willis, C.L.'       8 ?                   
# 
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 'Short-chain dehydrogenase/reductase' 53012.633 1   ? ? ? 'Complexed with FAD' 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'         785.550   1   ? ? ? ?                    
3 water       nat water                                 18.015    171 ? ? ? ?                    
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Diels Aldrease TedJ' 
# 
_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       
;MAHHHHHHSSGLEVLFQGPMTDPVIVVGAGPTGLMLACELGLAGAPVVVLDRRDAPDPHAPGQAVNAGVVALLEQRGLAD
ALRASGLPLPGAHFSLLWLRPEEITADRPEVGTGLLVAQPRLTEVLEQRARELGVDVRRGHEVTELRQSPGHVTLKLRTS
AGDSTLRGSYVVAADGAGSTVRRLAGIDFPGSGWTVSGIVGDVTVDFSELAVHHLGAHYLPAGGVYSGAPAGPGVLRVIT
TVFGATPPAPSGPVAAEELQGEVEHLTGQPLPAREVLWARRFTSHSGNAERYRSGRVFLAGDAAHSFYPLGGLRLSTCLQ
DAVNLGWKLAADLAGWAPPGLLDTYHAERHPEGERARLALDAQLALMHPAARTAGARSLVADLARFEDVNRYLVELVTGV
DPRYRVGTDGASGSVVPDPALGGRVPGAAPLLHGGGGLLLLGAADGDGERGEGGAHARTAAAWADRVGVAPALAADATRS
VLLRPDGHVAWAEGSGSLETALKNWFGTPR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHHHHHSSGLEVLFQGPMTDPVIVVGAGPTGLMLACELGLAGAPVVVLDRRDAPDPHAPGQAVNAGVVALLEQRGLAD
ALRASGLPLPGAHFSLLWLRPEEITADRPEVGTGLLVAQPRLTEVLEQRARELGVDVRRGHEVTELRQSPGHVTLKLRTS
AGDSTLRGSYVVAADGAGSTVRRLAGIDFPGSGWTVSGIVGDVTVDFSELAVHHLGAHYLPAGGVYSGAPAGPGVLRVIT
TVFGATPPAPSGPVAAEELQGEVEHLTGQPLPAREVLWARRFTSHSGNAERYRSGRVFLAGDAAHSFYPLGGLRLSTCLQ
DAVNLGWKLAADLAGWAPPGLLDTYHAERHPEGERARLALDAQLALMHPAARTAGARSLVADLARFEDVNRYLVELVTGV
DPRYRVGTDGASGSVVPDPALGGRVPGAAPLLHGGGGLLLLGAADGDGERGEGGAHARTAAAWADRVGVAPALAADATRS
VLLRPDGHVAWAEGSGSLETALKNWFGTPR
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   SER n 
1 10  SER n 
1 11  GLY n 
1 12  LEU n 
1 13  GLU n 
1 14  VAL n 
1 15  LEU n 
1 16  PHE n 
1 17  GLN n 
1 18  GLY n 
1 19  PRO n 
1 20  MET n 
1 21  THR n 
1 22  ASP n 
1 23  PRO n 
1 24  VAL n 
1 25  ILE n 
1 26  VAL n 
1 27  VAL n 
1 28  GLY n 
1 29  ALA n 
1 30  GLY n 
1 31  PRO n 
1 32  THR n 
1 33  GLY n 
1 34  LEU n 
1 35  MET n 
1 36  LEU n 
1 37  ALA n 
1 38  CYS n 
1 39  GLU n 
1 40  LEU n 
1 41  GLY n 
1 42  LEU n 
1 43  ALA n 
1 44  GLY n 
1 45  ALA n 
1 46  PRO n 
1 47  VAL n 
1 48  VAL n 
1 49  VAL n 
1 50  LEU n 
1 51  ASP n 
1 52  ARG n 
1 53  ARG n 
1 54  ASP n 
1 55  ALA n 
1 56  PRO n 
1 57  ASP n 
1 58  PRO n 
1 59  HIS n 
1 60  ALA n 
1 61  PRO n 
1 62  GLY n 
1 63  GLN n 
1 64  ALA n 
1 65  VAL n 
1 66  ASN n 
1 67  ALA n 
1 68  GLY n 
1 69  VAL n 
1 70  VAL n 
1 71  ALA n 
1 72  LEU n 
1 73  LEU n 
1 74  GLU n 
1 75  GLN n 
1 76  ARG n 
1 77  GLY n 
1 78  LEU n 
1 79  ALA n 
1 80  ASP n 
1 81  ALA n 
1 82  LEU n 
1 83  ARG n 
1 84  ALA n 
1 85  SER n 
1 86  GLY n 
1 87  LEU n 
1 88  PRO n 
1 89  LEU n 
1 90  PRO n 
1 91  GLY n 
1 92  ALA n 
1 93  HIS n 
1 94  PHE n 
1 95  SER n 
1 96  LEU n 
1 97  LEU n 
1 98  TRP n 
1 99  LEU n 
1 100 ARG n 
1 101 PRO n 
1 102 GLU n 
1 103 GLU n 
1 104 ILE n 
1 105 THR n 
1 106 ALA n 
1 107 ASP n 
1 108 ARG n 
1 109 PRO n 
1 110 GLU n 
1 111 VAL n 
1 112 GLY n 
1 113 THR n 
1 114 GLY n 
1 115 LEU n 
1 116 LEU n 
1 117 VAL n 
1 118 ALA n 
1 119 GLN n 
1 120 PRO n 
1 121 ARG n 
1 122 LEU n 
1 123 THR n 
1 124 GLU n 
1 125 VAL n 
1 126 LEU n 
1 127 GLU n 
1 128 GLN n 
1 129 ARG n 
1 130 ALA n 
1 131 ARG n 
1 132 GLU n 
1 133 LEU n 
1 134 GLY n 
1 135 VAL n 
1 136 ASP n 
1 137 VAL n 
1 138 ARG n 
1 139 ARG n 
1 140 GLY n 
1 141 HIS n 
1 142 GLU n 
1 143 VAL n 
1 144 THR n 
1 145 GLU n 
1 146 LEU n 
1 147 ARG n 
1 148 GLN n 
1 149 SER n 
1 150 PRO n 
1 151 GLY n 
1 152 HIS n 
1 153 VAL n 
1 154 THR n 
1 155 LEU n 
1 156 LYS n 
1 157 LEU n 
1 158 ARG n 
1 159 THR n 
1 160 SER n 
1 161 ALA n 
1 162 GLY n 
1 163 ASP n 
1 164 SER n 
1 165 THR n 
1 166 LEU n 
1 167 ARG n 
1 168 GLY n 
1 169 SER n 
1 170 TYR n 
1 171 VAL n 
1 172 VAL n 
1 173 ALA n 
1 174 ALA n 
1 175 ASP n 
1 176 GLY n 
1 177 ALA n 
1 178 GLY n 
1 179 SER n 
1 180 THR n 
1 181 VAL n 
1 182 ARG n 
1 183 ARG n 
1 184 LEU n 
1 185 ALA n 
1 186 GLY n 
1 187 ILE n 
1 188 ASP n 
1 189 PHE n 
1 190 PRO n 
1 191 GLY n 
1 192 SER n 
1 193 GLY n 
1 194 TRP n 
1 195 THR n 
1 196 VAL n 
1 197 SER n 
1 198 GLY n 
1 199 ILE n 
1 200 VAL n 
1 201 GLY n 
1 202 ASP n 
1 203 VAL n 
1 204 THR n 
1 205 VAL n 
1 206 ASP n 
1 207 PHE n 
1 208 SER n 
1 209 GLU n 
1 210 LEU n 
1 211 ALA n 
1 212 VAL n 
1 213 HIS n 
1 214 HIS n 
1 215 LEU n 
1 216 GLY n 
1 217 ALA n 
1 218 HIS n 
1 219 TYR n 
1 220 LEU n 
1 221 PRO n 
1 222 ALA n 
1 223 GLY n 
1 224 GLY n 
1 225 VAL n 
1 226 TYR n 
1 227 SER n 
1 228 GLY n 
1 229 ALA n 
1 230 PRO n 
1 231 ALA n 
1 232 GLY n 
1 233 PRO n 
1 234 GLY n 
1 235 VAL n 
1 236 LEU n 
1 237 ARG n 
1 238 VAL n 
1 239 ILE n 
1 240 THR n 
1 241 THR n 
1 242 VAL n 
1 243 PHE n 
1 244 GLY n 
1 245 ALA n 
1 246 THR n 
1 247 PRO n 
1 248 PRO n 
1 249 ALA n 
1 250 PRO n 
1 251 SER n 
1 252 GLY n 
1 253 PRO n 
1 254 VAL n 
1 255 ALA n 
1 256 ALA n 
1 257 GLU n 
1 258 GLU n 
1 259 LEU n 
1 260 GLN n 
1 261 GLY n 
1 262 GLU n 
1 263 VAL n 
1 264 GLU n 
1 265 HIS n 
1 266 LEU n 
1 267 THR n 
1 268 GLY n 
1 269 GLN n 
1 270 PRO n 
1 271 LEU n 
1 272 PRO n 
1 273 ALA n 
1 274 ARG n 
1 275 GLU n 
1 276 VAL n 
1 277 LEU n 
1 278 TRP n 
1 279 ALA n 
1 280 ARG n 
1 281 ARG n 
1 282 PHE n 
1 283 THR n 
1 284 SER n 
1 285 HIS n 
1 286 SER n 
1 287 GLY n 
1 288 ASN n 
1 289 ALA n 
1 290 GLU n 
1 291 ARG n 
1 292 TYR n 
1 293 ARG n 
1 294 SER n 
1 295 GLY n 
1 296 ARG n 
1 297 VAL n 
1 298 PHE n 
1 299 LEU n 
1 300 ALA n 
1 301 GLY n 
1 302 ASP n 
1 303 ALA n 
1 304 ALA n 
1 305 HIS n 
1 306 SER n 
1 307 PHE n 
1 308 TYR n 
1 309 PRO n 
1 310 LEU n 
1 311 GLY n 
1 312 GLY n 
1 313 LEU n 
1 314 ARG n 
1 315 LEU n 
1 316 SER n 
1 317 THR n 
1 318 CYS n 
1 319 LEU n 
1 320 GLN n 
1 321 ASP n 
1 322 ALA n 
1 323 VAL n 
1 324 ASN n 
1 325 LEU n 
1 326 GLY n 
1 327 TRP n 
1 328 LYS n 
1 329 LEU n 
1 330 ALA n 
1 331 ALA n 
1 332 ASP n 
1 333 LEU n 
1 334 ALA n 
1 335 GLY n 
1 336 TRP n 
1 337 ALA n 
1 338 PRO n 
1 339 PRO n 
1 340 GLY n 
1 341 LEU n 
1 342 LEU n 
1 343 ASP n 
1 344 THR n 
1 345 TYR n 
1 346 HIS n 
1 347 ALA n 
1 348 GLU n 
1 349 ARG n 
1 350 HIS n 
1 351 PRO n 
1 352 GLU n 
1 353 GLY n 
1 354 GLU n 
1 355 ARG n 
1 356 ALA n 
1 357 ARG n 
1 358 LEU n 
1 359 ALA n 
1 360 LEU n 
1 361 ASP n 
1 362 ALA n 
1 363 GLN n 
1 364 LEU n 
1 365 ALA n 
1 366 LEU n 
1 367 MET n 
1 368 HIS n 
1 369 PRO n 
1 370 ALA n 
1 371 ALA n 
1 372 ARG n 
1 373 THR n 
1 374 ALA n 
1 375 GLY n 
1 376 ALA n 
1 377 ARG n 
1 378 SER n 
1 379 LEU n 
1 380 VAL n 
1 381 ALA n 
1 382 ASP n 
1 383 LEU n 
1 384 ALA n 
1 385 ARG n 
1 386 PHE n 
1 387 GLU n 
1 388 ASP n 
1 389 VAL n 
1 390 ASN n 
1 391 ARG n 
1 392 TYR n 
1 393 LEU n 
1 394 VAL n 
1 395 GLU n 
1 396 LEU n 
1 397 VAL n 
1 398 THR n 
1 399 GLY n 
1 400 VAL n 
1 401 ASP n 
1 402 PRO n 
1 403 ARG n 
1 404 TYR n 
1 405 ARG n 
1 406 VAL n 
1 407 GLY n 
1 408 THR n 
1 409 ASP n 
1 410 GLY n 
1 411 ALA n 
1 412 SER n 
1 413 GLY n 
1 414 SER n 
1 415 VAL n 
1 416 VAL n 
1 417 PRO n 
1 418 ASP n 
1 419 PRO n 
1 420 ALA n 
1 421 LEU n 
1 422 GLY n 
1 423 GLY n 
1 424 ARG n 
1 425 VAL n 
1 426 PRO n 
1 427 GLY n 
1 428 ALA n 
1 429 ALA n 
1 430 PRO n 
1 431 LEU n 
1 432 LEU n 
1 433 HIS n 
1 434 GLY n 
1 435 GLY n 
1 436 GLY n 
1 437 GLY n 
1 438 LEU n 
1 439 LEU n 
1 440 LEU n 
1 441 LEU n 
1 442 GLY n 
1 443 ALA n 
1 444 ALA n 
1 445 ASP n 
1 446 GLY n 
1 447 ASP n 
1 448 GLY n 
1 449 GLU n 
1 450 ARG n 
1 451 GLY n 
1 452 GLU n 
1 453 GLY n 
1 454 GLY n 
1 455 ALA n 
1 456 HIS n 
1 457 ALA n 
1 458 ARG n 
1 459 THR n 
1 460 ALA n 
1 461 ALA n 
1 462 ALA n 
1 463 TRP n 
1 464 ALA n 
1 465 ASP n 
1 466 ARG n 
1 467 VAL n 
1 468 GLY n 
1 469 VAL n 
1 470 ALA n 
1 471 PRO n 
1 472 ALA n 
1 473 LEU n 
1 474 ALA n 
1 475 ALA n 
1 476 ASP n 
1 477 ALA n 
1 478 THR n 
1 479 ARG n 
1 480 SER n 
1 481 VAL n 
1 482 LEU n 
1 483 LEU n 
1 484 ARG n 
1 485 PRO n 
1 486 ASP n 
1 487 GLY n 
1 488 HIS n 
1 489 VAL n 
1 490 ALA n 
1 491 TRP n 
1 492 ALA n 
1 493 GLU n 
1 494 GLY n 
1 495 SER n 
1 496 GLY n 
1 497 SER n 
1 498 LEU n 
1 499 GLU n 
1 500 THR n 
1 501 ALA n 
1 502 LEU n 
1 503 LYS n 
1 504 ASN n 
1 505 TRP n 
1 506 PHE n 
1 507 GLY n 
1 508 THR n 
1 509 PRO n 
1 510 ARG 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                   510 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 tedJ 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    WAC04657 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   'Synthetic gene' 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      Streptomyces 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1883 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_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                       pOPINF 
_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 
CYS 'L-peptide linking' y CYSTEINE                      ? 'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking' y GLUTAMINE                     ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                       ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                     ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                         ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ? 'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE                 ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ? 'C3 H7 N O3'        105.093 
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   -18 ?   ?   ?   A . n 
A 1 2   ALA 2   -17 ?   ?   ?   A . n 
A 1 3   HIS 3   -16 ?   ?   ?   A . n 
A 1 4   HIS 4   -15 ?   ?   ?   A . n 
A 1 5   HIS 5   -14 ?   ?   ?   A . n 
A 1 6   HIS 6   -13 ?   ?   ?   A . n 
A 1 7   HIS 7   -12 ?   ?   ?   A . n 
A 1 8   HIS 8   -11 ?   ?   ?   A . n 
A 1 9   SER 9   -10 ?   ?   ?   A . n 
A 1 10  SER 10  -9  ?   ?   ?   A . n 
A 1 11  GLY 11  -8  -8  GLY GLY A . n 
A 1 12  LEU 12  -7  -7  LEU LEU A . n 
A 1 13  GLU 13  -6  -6  GLU GLU A . n 
A 1 14  VAL 14  -5  -5  VAL VAL A . n 
A 1 15  LEU 15  -4  -4  LEU LEU A . n 
A 1 16  PHE 16  -3  -3  PHE PHE A . n 
A 1 17  GLN 17  -2  -2  GLN GLN A . n 
A 1 18  GLY 18  -1  -1  GLY GLY A . n 
A 1 19  PRO 19  0   0   PRO PRO A . n 
A 1 20  MET 20  1   1   MET MET A . n 
A 1 21  THR 21  2   2   THR THR A . n 
A 1 22  ASP 22  3   3   ASP ASP A . n 
A 1 23  PRO 23  4   4   PRO PRO A . n 
A 1 24  VAL 24  5   5   VAL VAL A . n 
A 1 25  ILE 25  6   6   ILE ILE A . n 
A 1 26  VAL 26  7   7   VAL VAL A . n 
A 1 27  VAL 27  8   8   VAL VAL A . n 
A 1 28  GLY 28  9   9   GLY GLY A . n 
A 1 29  ALA 29  10  10  ALA ALA A . n 
A 1 30  GLY 30  11  11  GLY GLY A . n 
A 1 31  PRO 31  12  12  PRO PRO A . n 
A 1 32  THR 32  13  13  THR THR A . n 
A 1 33  GLY 33  14  14  GLY GLY A . n 
A 1 34  LEU 34  15  15  LEU LEU A . n 
A 1 35  MET 35  16  16  MET MET A . n 
A 1 36  LEU 36  17  17  LEU LEU A . n 
A 1 37  ALA 37  18  18  ALA ALA A . n 
A 1 38  CYS 38  19  19  CYS CYS A . n 
A 1 39  GLU 39  20  20  GLU GLU A . n 
A 1 40  LEU 40  21  21  LEU LEU A . n 
A 1 41  GLY 41  22  22  GLY GLY A . n 
A 1 42  LEU 42  23  23  LEU LEU A . n 
A 1 43  ALA 43  24  24  ALA ALA A . n 
A 1 44  GLY 44  25  25  GLY GLY A . n 
A 1 45  ALA 45  26  26  ALA ALA A . n 
A 1 46  PRO 46  27  27  PRO PRO A . n 
A 1 47  VAL 47  28  28  VAL VAL A . n 
A 1 48  VAL 48  29  29  VAL VAL A . n 
A 1 49  VAL 49  30  30  VAL VAL A . n 
A 1 50  LEU 50  31  31  LEU LEU A . n 
A 1 51  ASP 51  32  32  ASP ASP A . n 
A 1 52  ARG 52  33  33  ARG ARG A . n 
A 1 53  ARG 53  34  34  ARG ARG A . n 
A 1 54  ASP 54  35  35  ASP ASP A . n 
A 1 55  ALA 55  36  36  ALA ALA A . n 
A 1 56  PRO 56  37  37  PRO PRO A . n 
A 1 57  ASP 57  38  38  ASP ASP A . n 
A 1 58  PRO 58  39  39  PRO PRO A . n 
A 1 59  HIS 59  40  40  HIS HIS A . n 
A 1 60  ALA 60  41  41  ALA ALA A . n 
A 1 61  PRO 61  42  42  PRO PRO A . n 
A 1 62  GLY 62  43  43  GLY GLY A . n 
A 1 63  GLN 63  44  44  GLN GLN A . n 
A 1 64  ALA 64  45  45  ALA ALA A . n 
A 1 65  VAL 65  46  46  VAL VAL A . n 
A 1 66  ASN 66  47  47  ASN ASN A . n 
A 1 67  ALA 67  48  48  ALA ALA A . n 
A 1 68  GLY 68  49  49  GLY GLY A . n 
A 1 69  VAL 69  50  50  VAL VAL A . n 
A 1 70  VAL 70  51  51  VAL VAL A . n 
A 1 71  ALA 71  52  52  ALA ALA A . n 
A 1 72  LEU 72  53  53  LEU LEU A . n 
A 1 73  LEU 73  54  54  LEU LEU A . n 
A 1 74  GLU 74  55  55  GLU GLU A . n 
A 1 75  GLN 75  56  56  GLN GLN A . n 
A 1 76  ARG 76  57  57  ARG ARG A . n 
A 1 77  GLY 77  58  58  GLY GLY A . n 
A 1 78  LEU 78  59  59  LEU LEU A . n 
A 1 79  ALA 79  60  60  ALA ALA A . n 
A 1 80  ASP 80  61  61  ASP ASP A . n 
A 1 81  ALA 81  62  62  ALA ALA A . n 
A 1 82  LEU 82  63  63  LEU LEU A . n 
A 1 83  ARG 83  64  64  ARG ARG A . n 
A 1 84  ALA 84  65  65  ALA ALA A . n 
A 1 85  SER 85  66  66  SER SER A . n 
A 1 86  GLY 86  67  67  GLY GLY A . n 
A 1 87  LEU 87  68  68  LEU LEU A . n 
A 1 88  PRO 88  69  69  PRO PRO A . n 
A 1 89  LEU 89  70  70  LEU LEU A . n 
A 1 90  PRO 90  71  71  PRO PRO A . n 
A 1 91  GLY 91  72  72  GLY GLY A . n 
A 1 92  ALA 92  73  73  ALA ALA A . n 
A 1 93  HIS 93  74  74  HIS HIS A . n 
A 1 94  PHE 94  75  75  PHE PHE A . n 
A 1 95  SER 95  76  76  SER SER A . n 
A 1 96  LEU 96  77  77  LEU LEU A . n 
A 1 97  LEU 97  78  78  LEU LEU A . n 
A 1 98  TRP 98  79  79  TRP TRP A . n 
A 1 99  LEU 99  80  80  LEU LEU A . n 
A 1 100 ARG 100 81  81  ARG ARG A . n 
A 1 101 PRO 101 82  82  PRO PRO A . n 
A 1 102 GLU 102 83  83  GLU GLU A . n 
A 1 103 GLU 103 84  84  GLU GLU A . n 
A 1 104 ILE 104 85  85  ILE ILE A . n 
A 1 105 THR 105 86  86  THR THR A . n 
A 1 106 ALA 106 87  87  ALA ALA A . n 
A 1 107 ASP 107 88  88  ASP ASP A . n 
A 1 108 ARG 108 89  89  ARG ARG A . n 
A 1 109 PRO 109 90  90  PRO PRO A . n 
A 1 110 GLU 110 91  91  GLU GLU A . n 
A 1 111 VAL 111 92  92  VAL VAL A . n 
A 1 112 GLY 112 93  93  GLY GLY A . n 
A 1 113 THR 113 94  94  THR THR A . n 
A 1 114 GLY 114 95  95  GLY GLY A . n 
A 1 115 LEU 115 96  96  LEU LEU A . n 
A 1 116 LEU 116 97  97  LEU LEU A . n 
A 1 117 VAL 117 98  98  VAL VAL A . n 
A 1 118 ALA 118 99  99  ALA ALA A . n 
A 1 119 GLN 119 100 100 GLN GLN A . n 
A 1 120 PRO 120 101 101 PRO PRO A . n 
A 1 121 ARG 121 102 102 ARG ARG A . n 
A 1 122 LEU 122 103 103 LEU LEU A . n 
A 1 123 THR 123 104 104 THR THR A . n 
A 1 124 GLU 124 105 105 GLU GLU A . n 
A 1 125 VAL 125 106 106 VAL VAL A . n 
A 1 126 LEU 126 107 107 LEU LEU A . n 
A 1 127 GLU 127 108 108 GLU GLU A . n 
A 1 128 GLN 128 109 109 GLN GLN A . n 
A 1 129 ARG 129 110 110 ARG ARG A . n 
A 1 130 ALA 130 111 111 ALA ALA A . n 
A 1 131 ARG 131 112 112 ARG ARG A . n 
A 1 132 GLU 132 113 113 GLU GLU A . n 
A 1 133 LEU 133 114 114 LEU LEU A . n 
A 1 134 GLY 134 115 115 GLY GLY A . n 
A 1 135 VAL 135 116 116 VAL VAL A . n 
A 1 136 ASP 136 117 117 ASP ASP A . n 
A 1 137 VAL 137 118 118 VAL VAL A . n 
A 1 138 ARG 138 119 119 ARG ARG A . n 
A 1 139 ARG 139 120 120 ARG ARG A . n 
A 1 140 GLY 140 121 121 GLY GLY A . n 
A 1 141 HIS 141 122 122 HIS HIS A . n 
A 1 142 GLU 142 123 123 GLU GLU A . n 
A 1 143 VAL 143 124 124 VAL VAL A . n 
A 1 144 THR 144 125 125 THR THR A . n 
A 1 145 GLU 145 126 126 GLU GLU A . n 
A 1 146 LEU 146 127 127 LEU LEU A . n 
A 1 147 ARG 147 128 128 ARG ARG A . n 
A 1 148 GLN 148 129 129 GLN GLN A . n 
A 1 149 SER 149 130 130 SER SER A . n 
A 1 150 PRO 150 131 131 PRO PRO A . n 
A 1 151 GLY 151 132 132 GLY GLY A . n 
A 1 152 HIS 152 133 133 HIS HIS A . n 
A 1 153 VAL 153 134 134 VAL VAL A . n 
A 1 154 THR 154 135 135 THR THR A . n 
A 1 155 LEU 155 136 136 LEU LEU A . n 
A 1 156 LYS 156 137 137 LYS LYS A . n 
A 1 157 LEU 157 138 138 LEU LEU A . n 
A 1 158 ARG 158 139 139 ARG ARG A . n 
A 1 159 THR 159 140 140 THR THR A . n 
A 1 160 SER 160 141 141 SER SER A . n 
A 1 161 ALA 161 142 142 ALA ALA A . n 
A 1 162 GLY 162 143 143 GLY GLY A . n 
A 1 163 ASP 163 144 144 ASP ASP A . n 
A 1 164 SER 164 145 145 SER SER A . n 
A 1 165 THR 165 146 146 THR THR A . n 
A 1 166 LEU 166 147 147 LEU LEU A . n 
A 1 167 ARG 167 148 148 ARG ARG A . n 
A 1 168 GLY 168 149 149 GLY GLY A . n 
A 1 169 SER 169 150 150 SER SER A . n 
A 1 170 TYR 170 151 151 TYR TYR A . n 
A 1 171 VAL 171 152 152 VAL VAL A . n 
A 1 172 VAL 172 153 153 VAL VAL A . n 
A 1 173 ALA 173 154 154 ALA ALA A . n 
A 1 174 ALA 174 155 155 ALA ALA A . n 
A 1 175 ASP 175 156 156 ASP ASP A . n 
A 1 176 GLY 176 157 157 GLY GLY A . n 
A 1 177 ALA 177 158 158 ALA ALA A . n 
A 1 178 GLY 178 159 159 GLY GLY A . n 
A 1 179 SER 179 160 160 SER SER A . n 
A 1 180 THR 180 161 161 THR THR A . n 
A 1 181 VAL 181 162 162 VAL VAL A . n 
A 1 182 ARG 182 163 163 ARG ARG A . n 
A 1 183 ARG 183 164 164 ARG ARG A . n 
A 1 184 LEU 184 165 165 LEU LEU A . n 
A 1 185 ALA 185 166 166 ALA ALA A . n 
A 1 186 GLY 186 167 167 GLY GLY A . n 
A 1 187 ILE 187 168 168 ILE ILE A . n 
A 1 188 ASP 188 169 169 ASP ASP A . n 
A 1 189 PHE 189 170 170 PHE PHE A . n 
A 1 190 PRO 190 171 171 PRO PRO A . n 
A 1 191 GLY 191 172 172 GLY GLY A . n 
A 1 192 SER 192 173 173 SER SER A . n 
A 1 193 GLY 193 174 174 GLY GLY A . n 
A 1 194 TRP 194 175 175 TRP TRP A . n 
A 1 195 THR 195 176 176 THR THR A . n 
A 1 196 VAL 196 177 177 VAL VAL A . n 
A 1 197 SER 197 178 178 SER SER A . n 
A 1 198 GLY 198 179 179 GLY GLY A . n 
A 1 199 ILE 199 180 180 ILE ILE A . n 
A 1 200 VAL 200 181 181 VAL VAL A . n 
A 1 201 GLY 201 182 182 GLY GLY A . n 
A 1 202 ASP 202 183 183 ASP ASP A . n 
A 1 203 VAL 203 184 184 VAL VAL A . n 
A 1 204 THR 204 185 185 THR THR A . n 
A 1 205 VAL 205 186 186 VAL VAL A . n 
A 1 206 ASP 206 187 187 ASP ASP A . n 
A 1 207 PHE 207 188 188 PHE PHE A . n 
A 1 208 SER 208 189 189 SER SER A . n 
A 1 209 GLU 209 190 190 GLU GLU A . n 
A 1 210 LEU 210 191 191 LEU LEU A . n 
A 1 211 ALA 211 192 192 ALA ALA A . n 
A 1 212 VAL 212 193 193 VAL VAL A . n 
A 1 213 HIS 213 194 194 HIS HIS A . n 
A 1 214 HIS 214 195 195 HIS HIS A . n 
A 1 215 LEU 215 196 196 LEU LEU A . n 
A 1 216 GLY 216 197 197 GLY GLY A . n 
A 1 217 ALA 217 198 198 ALA ALA A . n 
A 1 218 HIS 218 199 199 HIS HIS A . n 
A 1 219 TYR 219 200 200 TYR TYR A . n 
A 1 220 LEU 220 201 201 LEU LEU A . n 
A 1 221 PRO 221 202 202 PRO PRO A . n 
A 1 222 ALA 222 203 203 ALA ALA A . n 
A 1 223 GLY 223 204 204 GLY GLY A . n 
A 1 224 GLY 224 205 205 GLY GLY A . n 
A 1 225 VAL 225 206 206 VAL VAL A . n 
A 1 226 TYR 226 207 207 TYR TYR A . n 
A 1 227 SER 227 208 208 SER SER A . n 
A 1 228 GLY 228 209 209 GLY GLY A . n 
A 1 229 ALA 229 210 210 ALA ALA A . n 
A 1 230 PRO 230 211 211 PRO PRO A . n 
A 1 231 ALA 231 212 212 ALA ALA A . n 
A 1 232 GLY 232 213 213 GLY GLY A . n 
A 1 233 PRO 233 214 214 PRO PRO A . n 
A 1 234 GLY 234 215 215 GLY GLY A . n 
A 1 235 VAL 235 216 216 VAL VAL A . n 
A 1 236 LEU 236 217 217 LEU LEU A . n 
A 1 237 ARG 237 218 218 ARG ARG A . n 
A 1 238 VAL 238 219 219 VAL VAL A . n 
A 1 239 ILE 239 220 220 ILE ILE A . n 
A 1 240 THR 240 221 221 THR THR A . n 
A 1 241 THR 241 222 222 THR THR A . n 
A 1 242 VAL 242 223 223 VAL VAL A . n 
A 1 243 PHE 243 224 224 PHE PHE A . n 
A 1 244 GLY 244 225 225 GLY GLY A . n 
A 1 245 ALA 245 226 226 ALA ALA A . n 
A 1 246 THR 246 227 227 THR THR A . n 
A 1 247 PRO 247 228 228 PRO PRO A . n 
A 1 248 PRO 248 229 229 PRO PRO A . n 
A 1 249 ALA 249 230 230 ALA ALA A . n 
A 1 250 PRO 250 231 231 PRO PRO A . n 
A 1 251 SER 251 232 232 SER SER A . n 
A 1 252 GLY 252 233 233 GLY GLY A . n 
A 1 253 PRO 253 234 234 PRO PRO A . n 
A 1 254 VAL 254 235 235 VAL VAL A . n 
A 1 255 ALA 255 236 236 ALA ALA A . n 
A 1 256 ALA 256 237 237 ALA ALA A . n 
A 1 257 GLU 257 238 238 GLU GLU A . n 
A 1 258 GLU 258 239 239 GLU GLU A . n 
A 1 259 LEU 259 240 240 LEU LEU A . n 
A 1 260 GLN 260 241 241 GLN GLN A . n 
A 1 261 GLY 261 242 242 GLY GLY A . n 
A 1 262 GLU 262 243 243 GLU GLU A . n 
A 1 263 VAL 263 244 244 VAL VAL A . n 
A 1 264 GLU 264 245 245 GLU GLU A . n 
A 1 265 HIS 265 246 246 HIS HIS A . n 
A 1 266 LEU 266 247 247 LEU LEU A . n 
A 1 267 THR 267 248 248 THR THR A . n 
A 1 268 GLY 268 249 249 GLY GLY A . n 
A 1 269 GLN 269 250 250 GLN GLN A . n 
A 1 270 PRO 270 251 251 PRO PRO A . n 
A 1 271 LEU 271 252 252 LEU LEU A . n 
A 1 272 PRO 272 253 253 PRO PRO A . n 
A 1 273 ALA 273 254 254 ALA ALA A . n 
A 1 274 ARG 274 255 255 ARG ARG A . n 
A 1 275 GLU 275 256 256 GLU GLU A . n 
A 1 276 VAL 276 257 257 VAL VAL A . n 
A 1 277 LEU 277 258 258 LEU LEU A . n 
A 1 278 TRP 278 259 259 TRP TRP A . n 
A 1 279 ALA 279 260 260 ALA ALA A . n 
A 1 280 ARG 280 261 261 ARG ARG A . n 
A 1 281 ARG 281 262 262 ARG ARG A . n 
A 1 282 PHE 282 263 263 PHE PHE A . n 
A 1 283 THR 283 264 264 THR THR A . n 
A 1 284 SER 284 265 265 SER SER A . n 
A 1 285 HIS 285 266 266 HIS HIS A . n 
A 1 286 SER 286 267 267 SER SER A . n 
A 1 287 GLY 287 268 268 GLY GLY A . n 
A 1 288 ASN 288 269 269 ASN ASN A . n 
A 1 289 ALA 289 270 270 ALA ALA A . n 
A 1 290 GLU 290 271 271 GLU GLU A . n 
A 1 291 ARG 291 272 272 ARG ARG A . n 
A 1 292 TYR 292 273 273 TYR TYR A . n 
A 1 293 ARG 293 274 274 ARG ARG A . n 
A 1 294 SER 294 275 275 SER SER A . n 
A 1 295 GLY 295 276 276 GLY GLY A . n 
A 1 296 ARG 296 277 277 ARG ARG A . n 
A 1 297 VAL 297 278 278 VAL VAL A . n 
A 1 298 PHE 298 279 279 PHE PHE A . n 
A 1 299 LEU 299 280 280 LEU LEU A . n 
A 1 300 ALA 300 281 281 ALA ALA A . n 
A 1 301 GLY 301 282 282 GLY GLY A . n 
A 1 302 ASP 302 283 283 ASP ASP A . n 
A 1 303 ALA 303 284 284 ALA ALA A . n 
A 1 304 ALA 304 285 285 ALA ALA A . n 
A 1 305 HIS 305 286 286 HIS HIS A . n 
A 1 306 SER 306 287 287 SER SER A . n 
A 1 307 PHE 307 288 288 PHE PHE A . n 
A 1 308 TYR 308 289 289 TYR TYR A . n 
A 1 309 PRO 309 290 290 PRO PRO A . n 
A 1 310 LEU 310 291 291 LEU LEU A . n 
A 1 311 GLY 311 292 292 GLY GLY A . n 
A 1 312 GLY 312 293 293 GLY GLY A . n 
A 1 313 LEU 313 294 294 LEU LEU A . n 
A 1 314 ARG 314 295 295 ARG ARG A . n 
A 1 315 LEU 315 296 296 LEU LEU A . n 
A 1 316 SER 316 297 297 SER SER A . n 
A 1 317 THR 317 298 298 THR THR A . n 
A 1 318 CYS 318 299 299 CYS CYS A . n 
A 1 319 LEU 319 300 300 LEU LEU A . n 
A 1 320 GLN 320 301 301 GLN GLN A . n 
A 1 321 ASP 321 302 302 ASP ASP A . n 
A 1 322 ALA 322 303 303 ALA ALA A . n 
A 1 323 VAL 323 304 304 VAL VAL A . n 
A 1 324 ASN 324 305 305 ASN ASN A . n 
A 1 325 LEU 325 306 306 LEU LEU A . n 
A 1 326 GLY 326 307 307 GLY GLY A . n 
A 1 327 TRP 327 308 308 TRP TRP A . n 
A 1 328 LYS 328 309 309 LYS LYS A . n 
A 1 329 LEU 329 310 310 LEU LEU A . n 
A 1 330 ALA 330 311 311 ALA ALA A . n 
A 1 331 ALA 331 312 312 ALA ALA A . n 
A 1 332 ASP 332 313 313 ASP ASP A . n 
A 1 333 LEU 333 314 314 LEU LEU A . n 
A 1 334 ALA 334 315 315 ALA ALA A . n 
A 1 335 GLY 335 316 316 GLY GLY A . n 
A 1 336 TRP 336 317 317 TRP TRP A . n 
A 1 337 ALA 337 318 318 ALA ALA A . n 
A 1 338 PRO 338 319 319 PRO PRO A . n 
A 1 339 PRO 339 320 320 PRO PRO A . n 
A 1 340 GLY 340 321 321 GLY GLY A . n 
A 1 341 LEU 341 322 322 LEU LEU A . n 
A 1 342 LEU 342 323 323 LEU LEU A . n 
A 1 343 ASP 343 324 324 ASP ASP A . n 
A 1 344 THR 344 325 325 THR THR A . n 
A 1 345 TYR 345 326 326 TYR TYR A . n 
A 1 346 HIS 346 327 327 HIS HIS A . n 
A 1 347 ALA 347 328 328 ALA ALA A . n 
A 1 348 GLU 348 329 329 GLU GLU A . n 
A 1 349 ARG 349 330 330 ARG ARG A . n 
A 1 350 HIS 350 331 331 HIS HIS A . n 
A 1 351 PRO 351 332 332 PRO PRO A . n 
A 1 352 GLU 352 333 333 GLU GLU A . n 
A 1 353 GLY 353 334 334 GLY GLY A . n 
A 1 354 GLU 354 335 335 GLU GLU A . n 
A 1 355 ARG 355 336 336 ARG ARG A . n 
A 1 356 ALA 356 337 337 ALA ALA A . n 
A 1 357 ARG 357 338 338 ARG ARG A . n 
A 1 358 LEU 358 339 339 LEU LEU A . n 
A 1 359 ALA 359 340 340 ALA ALA A . n 
A 1 360 LEU 360 341 341 LEU LEU A . n 
A 1 361 ASP 361 342 342 ASP ASP A . n 
A 1 362 ALA 362 343 343 ALA ALA A . n 
A 1 363 GLN 363 344 344 GLN GLN A . n 
A 1 364 LEU 364 345 345 LEU LEU A . n 
A 1 365 ALA 365 346 346 ALA ALA A . n 
A 1 366 LEU 366 347 347 LEU LEU A . n 
A 1 367 MET 367 348 348 MET MET A . n 
A 1 368 HIS 368 349 349 HIS HIS A . n 
A 1 369 PRO 369 350 350 PRO PRO A . n 
A 1 370 ALA 370 351 351 ALA ALA A . n 
A 1 371 ALA 371 352 352 ALA ALA A . n 
A 1 372 ARG 372 353 353 ARG ARG A . n 
A 1 373 THR 373 354 354 THR THR A . n 
A 1 374 ALA 374 355 355 ALA ALA A . n 
A 1 375 GLY 375 356 356 GLY GLY A . n 
A 1 376 ALA 376 357 357 ALA ALA A . n 
A 1 377 ARG 377 358 358 ARG ARG A . n 
A 1 378 SER 378 359 359 SER SER A . n 
A 1 379 LEU 379 360 360 LEU LEU A . n 
A 1 380 VAL 380 361 361 VAL VAL A . n 
A 1 381 ALA 381 362 362 ALA ALA A . n 
A 1 382 ASP 382 363 363 ASP ASP A . n 
A 1 383 LEU 383 364 364 LEU LEU A . n 
A 1 384 ALA 384 365 365 ALA ALA A . n 
A 1 385 ARG 385 366 366 ARG ARG A . n 
A 1 386 PHE 386 367 367 PHE PHE A . n 
A 1 387 GLU 387 368 368 GLU GLU A . n 
A 1 388 ASP 388 369 369 ASP ASP A . n 
A 1 389 VAL 389 370 370 VAL VAL A . n 
A 1 390 ASN 390 371 371 ASN ASN A . n 
A 1 391 ARG 391 372 372 ARG ARG A . n 
A 1 392 TYR 392 373 373 TYR TYR A . n 
A 1 393 LEU 393 374 374 LEU LEU A . n 
A 1 394 VAL 394 375 375 VAL VAL A . n 
A 1 395 GLU 395 376 376 GLU GLU A . n 
A 1 396 LEU 396 377 377 LEU LEU A . n 
A 1 397 VAL 397 378 378 VAL VAL A . n 
A 1 398 THR 398 379 379 THR THR A . n 
A 1 399 GLY 399 380 380 GLY GLY A . n 
A 1 400 VAL 400 381 381 VAL VAL A . n 
A 1 401 ASP 401 382 382 ASP ASP A . n 
A 1 402 PRO 402 383 383 PRO PRO A . n 
A 1 403 ARG 403 384 384 ARG ARG A . n 
A 1 404 TYR 404 385 385 TYR TYR A . n 
A 1 405 ARG 405 386 386 ARG ARG A . n 
A 1 406 VAL 406 387 387 VAL VAL A . n 
A 1 407 GLY 407 388 388 GLY GLY A . n 
A 1 408 THR 408 389 389 THR THR A . n 
A 1 409 ASP 409 390 390 ASP ASP A . n 
A 1 410 GLY 410 391 391 GLY GLY A . n 
A 1 411 ALA 411 392 392 ALA ALA A . n 
A 1 412 SER 412 393 393 SER SER A . n 
A 1 413 GLY 413 394 394 GLY GLY A . n 
A 1 414 SER 414 395 395 SER SER A . n 
A 1 415 VAL 415 396 396 VAL VAL A . n 
A 1 416 VAL 416 397 397 VAL VAL A . n 
A 1 417 PRO 417 398 398 PRO PRO A . n 
A 1 418 ASP 418 399 399 ASP ASP A . n 
A 1 419 PRO 419 400 400 PRO PRO A . n 
A 1 420 ALA 420 401 401 ALA ALA A . n 
A 1 421 LEU 421 402 402 LEU LEU A . n 
A 1 422 GLY 422 403 403 GLY GLY A . n 
A 1 423 GLY 423 404 404 GLY GLY A . n 
A 1 424 ARG 424 405 405 ARG ARG A . n 
A 1 425 VAL 425 406 406 VAL VAL A . n 
A 1 426 PRO 426 407 407 PRO PRO A . n 
A 1 427 GLY 427 408 408 GLY GLY A . n 
A 1 428 ALA 428 409 409 ALA ALA A . n 
A 1 429 ALA 429 410 410 ALA ALA A . n 
A 1 430 PRO 430 411 411 PRO PRO A . n 
A 1 431 LEU 431 412 412 LEU LEU A . n 
A 1 432 LEU 432 413 413 LEU LEU A . n 
A 1 433 HIS 433 414 414 HIS HIS A . n 
A 1 434 GLY 434 415 415 GLY GLY A . n 
A 1 435 GLY 435 416 416 GLY GLY A . n 
A 1 436 GLY 436 417 417 GLY GLY A . n 
A 1 437 GLY 437 418 418 GLY GLY A . n 
A 1 438 LEU 438 419 419 LEU LEU A . n 
A 1 439 LEU 439 420 420 LEU LEU A . n 
A 1 440 LEU 440 421 421 LEU LEU A . n 
A 1 441 LEU 441 422 422 LEU LEU A . n 
A 1 442 GLY 442 423 423 GLY GLY A . n 
A 1 443 ALA 443 424 424 ALA ALA A . n 
A 1 444 ALA 444 425 425 ALA ALA A . n 
A 1 445 ASP 445 426 426 ASP ASP A . n 
A 1 446 GLY 446 427 ?   ?   ?   A . n 
A 1 447 ASP 447 428 ?   ?   ?   A . n 
A 1 448 GLY 448 429 ?   ?   ?   A . n 
A 1 449 GLU 449 430 ?   ?   ?   A . n 
A 1 450 ARG 450 431 ?   ?   ?   A . n 
A 1 451 GLY 451 432 ?   ?   ?   A . n 
A 1 452 GLU 452 433 ?   ?   ?   A . n 
A 1 453 GLY 453 434 ?   ?   ?   A . n 
A 1 454 GLY 454 435 435 GLY GLY A . n 
A 1 455 ALA 455 436 436 ALA ALA A . n 
A 1 456 HIS 456 437 437 HIS HIS A . n 
A 1 457 ALA 457 438 438 ALA ALA A . n 
A 1 458 ARG 458 439 439 ARG ARG A . n 
A 1 459 THR 459 440 440 THR THR A . n 
A 1 460 ALA 460 441 441 ALA ALA A . n 
A 1 461 ALA 461 442 442 ALA ALA A . n 
A 1 462 ALA 462 443 443 ALA ALA A . n 
A 1 463 TRP 463 444 444 TRP TRP A . n 
A 1 464 ALA 464 445 445 ALA ALA A . n 
A 1 465 ASP 465 446 446 ASP ASP A . n 
A 1 466 ARG 466 447 447 ARG ARG A . n 
A 1 467 VAL 467 448 448 VAL VAL A . n 
A 1 468 GLY 468 449 449 GLY GLY A . n 
A 1 469 VAL 469 450 450 VAL VAL A . n 
A 1 470 ALA 470 451 451 ALA ALA A . n 
A 1 471 PRO 471 452 452 PRO PRO A . n 
A 1 472 ALA 472 453 453 ALA ALA A . n 
A 1 473 LEU 473 454 454 LEU LEU A . n 
A 1 474 ALA 474 455 455 ALA ALA A . n 
A 1 475 ALA 475 456 456 ALA ALA A . n 
A 1 476 ASP 476 457 457 ASP ASP A . n 
A 1 477 ALA 477 458 458 ALA ALA A . n 
A 1 478 THR 478 459 459 THR THR A . n 
A 1 479 ARG 479 460 460 ARG ARG A . n 
A 1 480 SER 480 461 461 SER SER A . n 
A 1 481 VAL 481 462 462 VAL VAL A . n 
A 1 482 LEU 482 463 463 LEU LEU A . n 
A 1 483 LEU 483 464 464 LEU LEU A . n 
A 1 484 ARG 484 465 465 ARG ARG A . n 
A 1 485 PRO 485 466 466 PRO PRO A . n 
A 1 486 ASP 486 467 467 ASP ASP A . n 
A 1 487 GLY 487 468 468 GLY GLY A . n 
A 1 488 HIS 488 469 469 HIS HIS A . n 
A 1 489 VAL 489 470 470 VAL VAL A . n 
A 1 490 ALA 490 471 471 ALA ALA A . n 
A 1 491 TRP 491 472 472 TRP TRP A . n 
A 1 492 ALA 492 473 473 ALA ALA A . n 
A 1 493 GLU 493 474 474 GLU GLU A . n 
A 1 494 GLY 494 475 475 GLY GLY A . n 
A 1 495 SER 495 476 476 SER SER A . n 
A 1 496 GLY 496 477 477 GLY GLY A . n 
A 1 497 SER 497 478 478 SER SER A . n 
A 1 498 LEU 498 479 479 LEU LEU A . n 
A 1 499 GLU 499 480 480 GLU GLU A . n 
A 1 500 THR 500 481 481 THR THR A . n 
A 1 501 ALA 501 482 482 ALA ALA A . n 
A 1 502 LEU 502 483 483 LEU LEU A . n 
A 1 503 LYS 503 484 484 LYS LYS A . n 
A 1 504 ASN 504 485 485 ASN ASN A . n 
A 1 505 TRP 505 486 486 TRP TRP A . n 
A 1 506 PHE 506 487 487 PHE PHE A . n 
A 1 507 GLY 507 488 488 GLY GLY A . n 
A 1 508 THR 508 489 489 THR THR A . n 
A 1 509 PRO 509 490 490 PRO PRO A . n 
A 1 510 ARG 510 491 491 ARG ARG A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FAD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FAD 1   501 582 FAD FAD A . 
C 3 HOH 1   601 157 HOH HOH A . 
C 3 HOH 2   602 151 HOH HOH A . 
C 3 HOH 3   603 130 HOH HOH A . 
C 3 HOH 4   604 71  HOH HOH A . 
C 3 HOH 5   605 122 HOH HOH A . 
C 3 HOH 6   606 120 HOH HOH A . 
C 3 HOH 7   607 67  HOH HOH A . 
C 3 HOH 8   608 59  HOH HOH A . 
C 3 HOH 9   609 62  HOH HOH A . 
C 3 HOH 10  610 108 HOH HOH A . 
C 3 HOH 11  611 128 HOH HOH A . 
C 3 HOH 12  612 79  HOH HOH A . 
C 3 HOH 13  613 81  HOH HOH A . 
C 3 HOH 14  614 150 HOH HOH A . 
C 3 HOH 15  615 7   HOH HOH A . 
C 3 HOH 16  616 166 HOH HOH A . 
C 3 HOH 17  617 63  HOH HOH A . 
C 3 HOH 18  618 36  HOH HOH A . 
C 3 HOH 19  619 92  HOH HOH A . 
C 3 HOH 20  620 127 HOH HOH A . 
C 3 HOH 21  621 70  HOH HOH A . 
C 3 HOH 22  622 27  HOH HOH A . 
C 3 HOH 23  623 118 HOH HOH A . 
C 3 HOH 24  624 158 HOH HOH A . 
C 3 HOH 25  625 21  HOH HOH A . 
C 3 HOH 26  626 115 HOH HOH A . 
C 3 HOH 27  627 9   HOH HOH A . 
C 3 HOH 28  628 22  HOH HOH A . 
C 3 HOH 29  629 25  HOH HOH A . 
C 3 HOH 30  630 133 HOH HOH A . 
C 3 HOH 31  631 60  HOH HOH A . 
C 3 HOH 32  632 113 HOH HOH A . 
C 3 HOH 33  633 72  HOH HOH A . 
C 3 HOH 34  634 173 HOH HOH A . 
C 3 HOH 35  635 31  HOH HOH A . 
C 3 HOH 36  636 142 HOH HOH A . 
C 3 HOH 37  637 16  HOH HOH A . 
C 3 HOH 38  638 144 HOH HOH A . 
C 3 HOH 39  639 14  HOH HOH A . 
C 3 HOH 40  640 101 HOH HOH A . 
C 3 HOH 41  641 42  HOH HOH A . 
C 3 HOH 42  642 65  HOH HOH A . 
C 3 HOH 43  643 117 HOH HOH A . 
C 3 HOH 44  644 13  HOH HOH A . 
C 3 HOH 45  645 5   HOH HOH A . 
C 3 HOH 46  646 50  HOH HOH A . 
C 3 HOH 47  647 170 HOH HOH A . 
C 3 HOH 48  648 12  HOH HOH A . 
C 3 HOH 49  649 29  HOH HOH A . 
C 3 HOH 50  650 68  HOH HOH A . 
C 3 HOH 51  651 11  HOH HOH A . 
C 3 HOH 52  652 123 HOH HOH A . 
C 3 HOH 53  653 114 HOH HOH A . 
C 3 HOH 54  654 110 HOH HOH A . 
C 3 HOH 55  655 91  HOH HOH A . 
C 3 HOH 56  656 167 HOH HOH A . 
C 3 HOH 57  657 52  HOH HOH A . 
C 3 HOH 58  658 39  HOH HOH A . 
C 3 HOH 59  659 163 HOH HOH A . 
C 3 HOH 60  660 10  HOH HOH A . 
C 3 HOH 61  661 6   HOH HOH A . 
C 3 HOH 62  662 66  HOH HOH A . 
C 3 HOH 63  663 141 HOH HOH A . 
C 3 HOH 64  664 44  HOH HOH A . 
C 3 HOH 65  665 73  HOH HOH A . 
C 3 HOH 66  666 119 HOH HOH A . 
C 3 HOH 67  667 139 HOH HOH A . 
C 3 HOH 68  668 95  HOH HOH A . 
C 3 HOH 69  669 40  HOH HOH A . 
C 3 HOH 70  670 89  HOH HOH A . 
C 3 HOH 71  671 41  HOH HOH A . 
C 3 HOH 72  672 111 HOH HOH A . 
C 3 HOH 73  673 69  HOH HOH A . 
C 3 HOH 74  674 53  HOH HOH A . 
C 3 HOH 75  675 30  HOH HOH A . 
C 3 HOH 76  676 121 HOH HOH A . 
C 3 HOH 77  677 107 HOH HOH A . 
C 3 HOH 78  678 48  HOH HOH A . 
C 3 HOH 79  679 15  HOH HOH A . 
C 3 HOH 80  680 136 HOH HOH A . 
C 3 HOH 81  681 35  HOH HOH A . 
C 3 HOH 82  682 3   HOH HOH A . 
C 3 HOH 83  683 32  HOH HOH A . 
C 3 HOH 84  684 82  HOH HOH A . 
C 3 HOH 85  685 47  HOH HOH A . 
C 3 HOH 86  686 64  HOH HOH A . 
C 3 HOH 87  687 148 HOH HOH A . 
C 3 HOH 88  688 83  HOH HOH A . 
C 3 HOH 89  689 28  HOH HOH A . 
C 3 HOH 90  690 78  HOH HOH A . 
C 3 HOH 91  691 33  HOH HOH A . 
C 3 HOH 92  692 34  HOH HOH A . 
C 3 HOH 93  693 77  HOH HOH A . 
C 3 HOH 94  694 125 HOH HOH A . 
C 3 HOH 95  695 4   HOH HOH A . 
C 3 HOH 96  696 43  HOH HOH A . 
C 3 HOH 97  697 103 HOH HOH A . 
C 3 HOH 98  698 2   HOH HOH A . 
C 3 HOH 99  699 58  HOH HOH A . 
C 3 HOH 100 700 8   HOH HOH A . 
C 3 HOH 101 701 156 HOH HOH A . 
C 3 HOH 102 702 171 HOH HOH A . 
C 3 HOH 103 703 102 HOH HOH A . 
C 3 HOH 104 704 76  HOH HOH A . 
C 3 HOH 105 705 140 HOH HOH A . 
C 3 HOH 106 706 19  HOH HOH A . 
C 3 HOH 107 707 26  HOH HOH A . 
C 3 HOH 108 708 96  HOH HOH A . 
C 3 HOH 109 709 56  HOH HOH A . 
C 3 HOH 110 710 90  HOH HOH A . 
C 3 HOH 111 711 74  HOH HOH A . 
C 3 HOH 112 712 165 HOH HOH A . 
C 3 HOH 113 713 87  HOH HOH A . 
C 3 HOH 114 714 131 HOH HOH A . 
C 3 HOH 115 715 46  HOH HOH A . 
C 3 HOH 116 716 116 HOH HOH A . 
C 3 HOH 117 717 37  HOH HOH A . 
C 3 HOH 118 718 99  HOH HOH A . 
C 3 HOH 119 719 24  HOH HOH A . 
C 3 HOH 120 720 93  HOH HOH A . 
C 3 HOH 121 721 126 HOH HOH A . 
C 3 HOH 122 722 129 HOH HOH A . 
C 3 HOH 123 723 18  HOH HOH A . 
C 3 HOH 124 724 38  HOH HOH A . 
C 3 HOH 125 725 51  HOH HOH A . 
C 3 HOH 126 726 104 HOH HOH A . 
C 3 HOH 127 727 169 HOH HOH A . 
C 3 HOH 128 728 23  HOH HOH A . 
C 3 HOH 129 729 49  HOH HOH A . 
C 3 HOH 130 730 97  HOH HOH A . 
C 3 HOH 131 731 55  HOH HOH A . 
C 3 HOH 132 732 20  HOH HOH A . 
C 3 HOH 133 733 80  HOH HOH A . 
C 3 HOH 134 734 85  HOH HOH A . 
C 3 HOH 135 735 88  HOH HOH A . 
C 3 HOH 136 736 17  HOH HOH A . 
C 3 HOH 137 737 98  HOH HOH A . 
C 3 HOH 138 738 106 HOH HOH A . 
C 3 HOH 139 739 155 HOH HOH A . 
C 3 HOH 140 740 138 HOH HOH A . 
C 3 HOH 141 741 84  HOH HOH A . 
C 3 HOH 142 742 154 HOH HOH A . 
C 3 HOH 143 743 134 HOH HOH A . 
C 3 HOH 144 744 86  HOH HOH A . 
C 3 HOH 145 745 100 HOH HOH A . 
C 3 HOH 146 746 135 HOH HOH A . 
C 3 HOH 147 747 57  HOH HOH A . 
C 3 HOH 148 748 149 HOH HOH A . 
C 3 HOH 149 749 164 HOH HOH A . 
C 3 HOH 150 750 146 HOH HOH A . 
C 3 HOH 151 751 124 HOH HOH A . 
C 3 HOH 152 752 54  HOH HOH A . 
C 3 HOH 153 753 1   HOH HOH A . 
C 3 HOH 154 754 109 HOH HOH A . 
C 3 HOH 155 755 174 HOH HOH A . 
C 3 HOH 156 756 137 HOH HOH A . 
C 3 HOH 157 757 147 HOH HOH A . 
C 3 HOH 158 758 162 HOH HOH A . 
C 3 HOH 159 759 172 HOH HOH A . 
C 3 HOH 160 760 145 HOH HOH A . 
C 3 HOH 161 761 161 HOH HOH A . 
C 3 HOH 162 762 105 HOH HOH A . 
C 3 HOH 163 763 159 HOH HOH A . 
C 3 HOH 164 764 94  HOH HOH A . 
C 3 HOH 165 765 168 HOH HOH A . 
C 3 HOH 166 766 160 HOH HOH A . 
C 3 HOH 167 767 112 HOH HOH A . 
C 3 HOH 168 768 132 HOH HOH A . 
C 3 HOH 169 769 152 HOH HOH A . 
C 3 HOH 170 770 153 HOH HOH A . 
C 3 HOH 171 771 175 HOH HOH A . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     THR 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      2 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     CG2 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    A 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    THR 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     21 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    CG2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0411 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8R1R 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     70.250 
_cell.length_a_esd                 ? 
_cell.length_b                     70.250 
_cell.length_b_esd                 ? 
_cell.length_c                     203.700 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8R1R 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8R1R 
_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             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.11 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    '1.4 M sodium acetate trihydrate, 0.1 M sodium cacodylate, pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 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         2023-07-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.99987 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.99987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8R1R 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.59 
_reflns.d_resolution_low                               101.85 
_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                                     69717 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                25.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.27 
_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                              0.153 
_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                                    1.59 
_reflns_shell.d_res_low                                     1.62 
_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                             3433 
_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                               21.46 
_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                                  0.385 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_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]                            1.25 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            1.25 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -2.50 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               34.056 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8R1R 
_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                            1.59 
_refine.ls_d_res_low                             66.50 
_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                     65939 
_refine.ls_number_reflns_R_free                  3662 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20877 
_refine.ls_R_factor_R_free                       0.24410 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20686 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.092 
_refine.pdbx_overall_ESU_R_Free                  0.095 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.805 
_refine.overall_SU_ML                            0.089 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.59 
_refine_hist.d_res_low                        66.50 
_refine_hist.number_atoms_solvent             171 
_refine_hist.number_atoms_total               3825 
_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        3601 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         53 
_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' ? 0.008  0.012  3743 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3535 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.534  1.647  5124 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.514  1.567  8099 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.492  5.000  490  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 7.153  5.000  39   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.206 10.000 516  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.081  0.200  578  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  4528 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  847  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.823  3.339  1966 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.823  3.339  1966 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.794  5.983  2454 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.795  5.985  2455 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.085  3.763  1777 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.088  3.765  1774 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.148  6.689  2671 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.140  32.31  4091 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.145  32.29  4068 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.590 
_refine_ls_shell.d_res_low                        1.631 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             274 
_refine_ls_shell.number_reflns_R_work             4804 
_refine_ls_shell.percent_reflns_obs               100.00 
_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                  0.414 
_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   20 
_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                  0.430 
# 
_struct.entry_id                     8R1R 
_struct.title                        'Structure of the Diels Alderase TedJ, in complex with cofactor FAD' 
_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        8R1R 
_struct_keywords.text            'Diels Alderase, decalin cyclase, tetradecamycin, class II spirotetronate, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A150VPP7_9ACTN 
_struct_ref.pdbx_db_accession          A0A150VPP7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTDPVIVVGAGPTGLMLACELGLAGAPVVVLDRRDAPDPHAPGQAVNAGVVALLEQRGLADALRASGLPLPGAHFSLLWL
RPEEITADRPEVGTGLLVAQPRLTEVLEQRARELGVDVRRGHEVTELRQSPGHVTLKLRTSAGDSTLRGSYVVAADGAGS
TVRRLAGIDFPGSGWTVSGIVGDVTVDFSELAVHHLGAHYLPAGGVYSGAPAGPGVLRVITTVFGATPPAPSGPVAAEEL
QGEVEHLTGQPLPAREVLWARRFTSHSGNAERYRSGRVFLAGDAAHSFYPLGGLRLSTCLQDAVNLGWKLAADLAGWAPP
GLLDTYHAERHPEGERARLALDAQLALMHPAARTAGARSLVADLARFEDVNRYLVELVTGVDPRYRVGTDGASGSVVPDP
ALGGRVPGAAPLLHGGGGLLLLGAADGDGERGEGGAHARTAAAWADRVGVAPALAADATRSVLLRPDGHVAWAEGSGSLE
TALKNWFGTPR
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8R1R 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 20 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 510 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A150VPP7 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  491 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       491 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8R1R MET A 1  ? UNP A0A150VPP7 ? ? 'initiating methionine' -18 1  
1 8R1R ALA A 2  ? UNP A0A150VPP7 ? ? 'expression tag'        -17 2  
1 8R1R HIS A 3  ? UNP A0A150VPP7 ? ? 'expression tag'        -16 3  
1 8R1R HIS A 4  ? UNP A0A150VPP7 ? ? 'expression tag'        -15 4  
1 8R1R HIS A 5  ? UNP A0A150VPP7 ? ? 'expression tag'        -14 5  
1 8R1R HIS A 6  ? UNP A0A150VPP7 ? ? 'expression tag'        -13 6  
1 8R1R HIS A 7  ? UNP A0A150VPP7 ? ? 'expression tag'        -12 7  
1 8R1R HIS A 8  ? UNP A0A150VPP7 ? ? 'expression tag'        -11 8  
1 8R1R SER A 9  ? UNP A0A150VPP7 ? ? 'expression tag'        -10 9  
1 8R1R SER A 10 ? UNP A0A150VPP7 ? ? 'expression tag'        -9  10 
1 8R1R GLY A 11 ? UNP A0A150VPP7 ? ? 'expression tag'        -8  11 
1 8R1R LEU A 12 ? UNP A0A150VPP7 ? ? 'expression tag'        -7  12 
1 8R1R GLU A 13 ? UNP A0A150VPP7 ? ? 'expression tag'        -6  13 
1 8R1R VAL A 14 ? UNP A0A150VPP7 ? ? 'expression tag'        -5  14 
1 8R1R LEU A 15 ? UNP A0A150VPP7 ? ? 'expression tag'        -4  15 
1 8R1R PHE A 16 ? UNP A0A150VPP7 ? ? 'expression tag'        -3  16 
1 8R1R GLN A 17 ? UNP A0A150VPP7 ? ? 'expression tag'        -2  17 
1 8R1R GLY A 18 ? UNP A0A150VPP7 ? ? 'expression tag'        -1  18 
1 8R1R PRO A 19 ? UNP A0A150VPP7 ? ? 'expression tag'        0   19 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4980  ? 
1 MORE         -28   ? 
1 'SSA (A^2)'  38490 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z        1.0000000000 0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000    
2 'crystal symmetry operation' 8_554 -y,-x,-z-1/2 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -101.8500000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 11  ? LEU A 15  ? GLY A -8  LEU A -4  5 ? 5  
HELX_P HELX_P2  AA2 GLY A 30  ? ALA A 43  ? GLY A 11  ALA A 24  1 ? 14 
HELX_P HELX_P3  AA3 ASN A 66  ? GLN A 75  ? ASN A 47  GLN A 56  1 ? 10 
HELX_P HELX_P4  AA4 LEU A 78  ? ALA A 84  ? LEU A 59  ALA A 65  1 ? 7  
HELX_P HELX_P5  AA5 ARG A 100 ? ILE A 104 ? ARG A 81  ILE A 85  5 ? 5  
HELX_P HELX_P6  AA6 ARG A 108 ? THR A 113 ? ARG A 89  THR A 94  5 ? 6  
HELX_P HELX_P7  AA7 ALA A 118 ? LEU A 133 ? ALA A 99  LEU A 114 1 ? 16 
HELX_P HELX_P8  AA8 SER A 179 ? ALA A 185 ? SER A 160 ALA A 166 1 ? 7  
HELX_P HELX_P9  AA9 ASP A 206 ? LEU A 210 ? ASP A 187 LEU A 191 5 ? 5  
HELX_P HELX_P10 AB1 ALA A 211 ? LEU A 215 ? ALA A 192 LEU A 196 5 ? 5  
HELX_P HELX_P11 AB2 ALA A 255 ? GLY A 268 ? ALA A 236 GLY A 249 1 ? 14 
HELX_P HELX_P12 AB3 GLY A 301 ? ALA A 303 ? GLY A 282 ALA A 284 5 ? 3  
HELX_P HELX_P13 AB4 GLY A 312 ? ALA A 334 ? GLY A 293 ALA A 315 1 ? 23 
HELX_P HELX_P14 AB5 LEU A 342 ? ALA A 365 ? LEU A 323 ALA A 346 1 ? 24 
HELX_P HELX_P15 AB6 PRO A 369 ? ALA A 384 ? PRO A 350 ALA A 365 1 ? 16 
HELX_P HELX_P16 AB7 PHE A 386 ? THR A 398 ? PHE A 367 THR A 379 1 ? 13 
HELX_P HELX_P17 AB8 GLY A 407 ? ALA A 411 ? GLY A 388 ALA A 392 5 ? 5  
HELX_P HELX_P18 AB9 VAL A 425 ? HIS A 433 ? VAL A 406 HIS A 414 5 ? 9  
HELX_P HELX_P19 AC1 ALA A 455 ? ALA A 462 ? ALA A 436 ALA A 443 1 ? 8  
HELX_P HELX_P20 AC2 LEU A 473 ? ASP A 476 ? LEU A 454 ASP A 457 5 ? 4  
HELX_P HELX_P21 AC3 SER A 497 ? GLY A 507 ? SER A 478 GLY A 488 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          HIS 
_struct_mon_prot_cis.label_seq_id           368 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           HIS 
_struct_mon_prot_cis.auth_seq_id            349 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    369 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     350 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -4.36 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 6 ? 
AA6 ? 2 ? 
AA7 ? 4 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? 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 ASP A 136 ? ARG A 138 ? ASP A 117 ARG A 119 
AA1 2 VAL A 47  ? LEU A 50  ? VAL A 28  LEU A 31  
AA1 3 VAL A 24  ? VAL A 27  ? VAL A 5   VAL A 8   
AA1 4 TYR A 170 ? ALA A 173 ? TYR A 151 ALA A 154 
AA1 5 VAL A 297 ? LEU A 299 ? VAL A 278 LEU A 280 
AA1 6 ARG A 293 ? SER A 294 ? ARG A 274 SER A 275 
AA2 1 ALA A 64  ? VAL A 65  ? ALA A 45  VAL A 46  
AA2 2 LEU A 115 ? LEU A 116 ? LEU A 96  LEU A 97  
AA2 3 LEU A 87  ? PRO A 88  ? LEU A 68  PRO A 69  
AA3 1 HIS A 93  ? PHE A 94  ? HIS A 74  PHE A 75  
AA3 2 LEU A 97  ? TRP A 98  ? LEU A 78  TRP A 79  
AA4 1 GLU A 142 ? GLN A 148 ? GLU A 123 GLN A 129 
AA4 2 VAL A 153 ? ARG A 158 ? VAL A 134 ARG A 139 
AA4 3 ASP A 163 ? GLY A 168 ? ASP A 144 GLY A 149 
AA5 1 GLY A 216 ? LEU A 220 ? GLY A 197 LEU A 201 
AA5 2 GLY A 224 ? GLY A 232 ? GLY A 205 GLY A 213 
AA5 3 VAL A 235 ? VAL A 242 ? VAL A 216 VAL A 223 
AA5 4 THR A 195 ? THR A 204 ? THR A 176 THR A 185 
AA5 5 GLU A 275 ? HIS A 285 ? GLU A 256 HIS A 266 
AA5 6 GLY A 252 ? PRO A 253 ? GLY A 233 PRO A 234 
AA6 1 GLY A 287 ? ASN A 288 ? GLY A 268 ASN A 269 
AA6 2 HIS A 305 ? SER A 306 ? HIS A 286 SER A 287 
AA7 1 VAL A 467 ? PRO A 471 ? VAL A 448 PRO A 452 
AA7 2 GLY A 437 ? LEU A 441 ? GLY A 418 LEU A 422 
AA7 3 VAL A 481 ? LEU A 483 ? VAL A 462 LEU A 464 
AA7 4 VAL A 489 ? ALA A 492 ? VAL A 470 ALA A 473 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ARG A 138 ? O ARG A 119 N VAL A 49  ? N VAL A 30  
AA1 2 3 O VAL A 48  ? O VAL A 29  N VAL A 26  ? N VAL A 7   
AA1 3 4 N ILE A 25  ? N ILE A 6   O TYR A 170 ? O TYR A 151 
AA1 4 5 N ALA A 173 ? N ALA A 154 O PHE A 298 ? O PHE A 279 
AA1 5 6 O VAL A 297 ? O VAL A 278 N SER A 294 ? N SER A 275 
AA2 1 2 N VAL A 65  ? N VAL A 46  O LEU A 115 ? O LEU A 96  
AA2 2 3 O LEU A 116 ? O LEU A 97  N LEU A 87  ? N LEU A 68  
AA3 1 2 N PHE A 94  ? N PHE A 75  O LEU A 97  ? O LEU A 78  
AA4 1 2 N THR A 144 ? N THR A 125 O LYS A 156 ? O LYS A 137 
AA4 2 3 N VAL A 153 ? N VAL A 134 O GLY A 168 ? O GLY A 149 
AA5 1 2 N HIS A 218 ? N HIS A 199 O TYR A 226 ? O TYR A 207 
AA5 2 3 N ALA A 229 ? N ALA A 210 O ARG A 237 ? O ARG A 218 
AA5 3 4 O LEU A 236 ? O LEU A 217 N VAL A 203 ? N VAL A 184 
AA5 4 5 N VAL A 200 ? N VAL A 181 O ARG A 280 ? O ARG A 261 
AA5 5 6 O ARG A 281 ? O ARG A 262 N GLY A 252 ? N GLY A 233 
AA6 1 2 N GLY A 287 ? N GLY A 268 O SER A 306 ? O SER A 287 
AA7 1 2 O GLY A 468 ? O GLY A 449 N LEU A 439 ? N LEU A 420 
AA7 2 3 N LEU A 438 ? N LEU A 419 O LEU A 483 ? O LEU A 464 
AA7 3 4 N LEU A 482 ? N LEU A 463 O TRP A 491 ? O TRP A 472 
# 
_pdbx_entry_details.entry_id                   8R1R 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU A 70  ? ? -117.93 72.25  
2 1 SER A 160 ? ? -19.38  114.01 
3 1 VAL A 397 ? ? -119.25 70.19  
4 1 SER A 476 ? ? -107.64 42.28  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     34 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.075 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     681 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 -18 ? A MET 1   
2  1 Y 1 A ALA -17 ? A ALA 2   
3  1 Y 1 A HIS -16 ? A HIS 3   
4  1 Y 1 A HIS -15 ? A HIS 4   
5  1 Y 1 A HIS -14 ? A HIS 5   
6  1 Y 1 A HIS -13 ? A HIS 6   
7  1 Y 1 A HIS -12 ? A HIS 7   
8  1 Y 1 A HIS -11 ? A HIS 8   
9  1 Y 1 A SER -10 ? A SER 9   
10 1 Y 1 A SER -9  ? A SER 10  
11 1 Y 1 A GLY 427 ? A GLY 446 
12 1 Y 1 A ASP 428 ? A ASP 447 
13 1 Y 1 A GLY 429 ? A GLY 448 
14 1 Y 1 A GLU 430 ? A GLU 449 
15 1 Y 1 A ARG 431 ? A ARG 450 
16 1 Y 1 A GLY 432 ? A GLY 451 
17 1 Y 1 A GLU 433 ? A GLU 452 
18 1 Y 1 A GLY 434 ? A GLY 453 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
GLN N      N N N 174 
GLN CA     C N S 175 
GLN C      C N N 176 
GLN O      O N N 177 
GLN CB     C N N 178 
GLN CG     C N N 179 
GLN CD     C N N 180 
GLN OE1    O N N 181 
GLN NE2    N N N 182 
GLN OXT    O N N 183 
GLN H      H N N 184 
GLN H2     H N N 185 
GLN HA     H N N 186 
GLN HB2    H N N 187 
GLN HB3    H N N 188 
GLN HG2    H N N 189 
GLN HG3    H N N 190 
GLN HE21   H N N 191 
GLN HE22   H N N 192 
GLN HXT    H N N 193 
GLU N      N N N 194 
GLU CA     C N S 195 
GLU C      C N N 196 
GLU O      O N N 197 
GLU CB     C N N 198 
GLU CG     C N N 199 
GLU CD     C N N 200 
GLU OE1    O N N 201 
GLU OE2    O N N 202 
GLU OXT    O N N 203 
GLU H      H N N 204 
GLU H2     H N N 205 
GLU HA     H N N 206 
GLU HB2    H N N 207 
GLU HB3    H N N 208 
GLU HG2    H N N 209 
GLU HG3    H N N 210 
GLU HE2    H N N 211 
GLU HXT    H N N 212 
GLY N      N N N 213 
GLY CA     C N N 214 
GLY C      C N N 215 
GLY O      O N N 216 
GLY OXT    O N N 217 
GLY H      H N N 218 
GLY H2     H N N 219 
GLY HA2    H N N 220 
GLY HA3    H N N 221 
GLY HXT    H N N 222 
HIS N      N N N 223 
HIS CA     C N S 224 
HIS C      C N N 225 
HIS O      O N N 226 
HIS CB     C N N 227 
HIS CG     C Y N 228 
HIS ND1    N Y N 229 
HIS CD2    C Y N 230 
HIS CE1    C Y N 231 
HIS NE2    N Y N 232 
HIS OXT    O N N 233 
HIS H      H N N 234 
HIS H2     H N N 235 
HIS HA     H N N 236 
HIS HB2    H N N 237 
HIS HB3    H N N 238 
HIS HD1    H N N 239 
HIS HD2    H N N 240 
HIS HE1    H N N 241 
HIS HE2    H N N 242 
HIS HXT    H N N 243 
HOH O      O N N 244 
HOH H1     H N N 245 
HOH H2     H N N 246 
ILE N      N N N 247 
ILE CA     C N S 248 
ILE C      C N N 249 
ILE O      O N N 250 
ILE CB     C N S 251 
ILE CG1    C N N 252 
ILE CG2    C N N 253 
ILE CD1    C N N 254 
ILE OXT    O N N 255 
ILE H      H N N 256 
ILE H2     H N N 257 
ILE HA     H N N 258 
ILE HB     H N N 259 
ILE HG12   H N N 260 
ILE HG13   H N N 261 
ILE HG21   H N N 262 
ILE HG22   H N N 263 
ILE HG23   H N N 264 
ILE HD11   H N N 265 
ILE HD12   H N N 266 
ILE HD13   H N N 267 
ILE HXT    H N N 268 
LEU N      N N N 269 
LEU CA     C N S 270 
LEU C      C N N 271 
LEU O      O N N 272 
LEU CB     C N N 273 
LEU CG     C N N 274 
LEU CD1    C N N 275 
LEU CD2    C N N 276 
LEU OXT    O N N 277 
LEU H      H N N 278 
LEU H2     H N N 279 
LEU HA     H N N 280 
LEU HB2    H N N 281 
LEU HB3    H N N 282 
LEU HG     H N N 283 
LEU HD11   H N N 284 
LEU HD12   H N N 285 
LEU HD13   H N N 286 
LEU HD21   H N N 287 
LEU HD22   H N N 288 
LEU HD23   H N N 289 
LEU HXT    H N N 290 
LYS N      N N N 291 
LYS CA     C N S 292 
LYS C      C N N 293 
LYS O      O N N 294 
LYS CB     C N N 295 
LYS CG     C N N 296 
LYS CD     C N N 297 
LYS CE     C N N 298 
LYS NZ     N N N 299 
LYS OXT    O N N 300 
LYS H      H N N 301 
LYS H2     H N N 302 
LYS HA     H N N 303 
LYS HB2    H N N 304 
LYS HB3    H N N 305 
LYS HG2    H N N 306 
LYS HG3    H N N 307 
LYS HD2    H N N 308 
LYS HD3    H N N 309 
LYS HE2    H N N 310 
LYS HE3    H N N 311 
LYS HZ1    H N N 312 
LYS HZ2    H N N 313 
LYS HZ3    H N N 314 
LYS HXT    H N N 315 
MET N      N N N 316 
MET CA     C N S 317 
MET C      C N N 318 
MET O      O N N 319 
MET CB     C N N 320 
MET CG     C N N 321 
MET SD     S N N 322 
MET CE     C N N 323 
MET OXT    O N N 324 
MET H      H N N 325 
MET H2     H N N 326 
MET HA     H N N 327 
MET HB2    H N N 328 
MET HB3    H N N 329 
MET HG2    H N N 330 
MET HG3    H N N 331 
MET HE1    H N N 332 
MET HE2    H N N 333 
MET HE3    H N N 334 
MET HXT    H N N 335 
PHE N      N N N 336 
PHE CA     C N S 337 
PHE C      C N N 338 
PHE O      O N N 339 
PHE CB     C N N 340 
PHE CG     C Y N 341 
PHE CD1    C Y N 342 
PHE CD2    C Y N 343 
PHE CE1    C Y N 344 
PHE CE2    C Y N 345 
PHE CZ     C Y N 346 
PHE OXT    O N N 347 
PHE H      H N N 348 
PHE H2     H N N 349 
PHE HA     H N N 350 
PHE HB2    H N N 351 
PHE HB3    H N N 352 
PHE HD1    H N N 353 
PHE HD2    H N N 354 
PHE HE1    H N N 355 
PHE HE2    H N N 356 
PHE HZ     H N N 357 
PHE HXT    H N N 358 
PRO N      N N N 359 
PRO CA     C N S 360 
PRO C      C N N 361 
PRO O      O N N 362 
PRO CB     C N N 363 
PRO CG     C N N 364 
PRO CD     C N N 365 
PRO OXT    O N N 366 
PRO H      H N N 367 
PRO HA     H N N 368 
PRO HB2    H N N 369 
PRO HB3    H N N 370 
PRO HG2    H N N 371 
PRO HG3    H N N 372 
PRO HD2    H N N 373 
PRO HD3    H N N 374 
PRO HXT    H N N 375 
SER N      N N N 376 
SER CA     C N S 377 
SER C      C N N 378 
SER O      O N N 379 
SER CB     C N N 380 
SER OG     O N N 381 
SER OXT    O N N 382 
SER H      H N N 383 
SER H2     H N N 384 
SER HA     H N N 385 
SER HB2    H N N 386 
SER HB3    H N N 387 
SER HG     H N N 388 
SER HXT    H N N 389 
THR N      N N N 390 
THR CA     C N S 391 
THR C      C N N 392 
THR O      O N N 393 
THR CB     C N R 394 
THR OG1    O N N 395 
THR CG2    C N N 396 
THR OXT    O N N 397 
THR H      H N N 398 
THR H2     H N N 399 
THR HA     H N N 400 
THR HB     H N N 401 
THR HG1    H N N 402 
THR HG21   H N N 403 
THR HG22   H N N 404 
THR HG23   H N N 405 
THR HXT    H N N 406 
TRP N      N N N 407 
TRP CA     C N S 408 
TRP C      C N N 409 
TRP O      O N N 410 
TRP CB     C N N 411 
TRP CG     C Y N 412 
TRP CD1    C Y N 413 
TRP CD2    C Y N 414 
TRP NE1    N Y N 415 
TRP CE2    C Y N 416 
TRP CE3    C Y N 417 
TRP CZ2    C Y N 418 
TRP CZ3    C Y N 419 
TRP CH2    C Y N 420 
TRP OXT    O N N 421 
TRP H      H N N 422 
TRP H2     H N N 423 
TRP HA     H N N 424 
TRP HB2    H N N 425 
TRP HB3    H N N 426 
TRP HD1    H N N 427 
TRP HE1    H N N 428 
TRP HE3    H N N 429 
TRP HZ2    H N N 430 
TRP HZ3    H N N 431 
TRP HH2    H N N 432 
TRP HXT    H N N 433 
TYR N      N N N 434 
TYR CA     C N S 435 
TYR C      C N N 436 
TYR O      O N N 437 
TYR CB     C N N 438 
TYR CG     C Y N 439 
TYR CD1    C Y N 440 
TYR CD2    C Y N 441 
TYR CE1    C Y N 442 
TYR CE2    C Y N 443 
TYR CZ     C Y N 444 
TYR OH     O N N 445 
TYR OXT    O N N 446 
TYR H      H N N 447 
TYR H2     H N N 448 
TYR HA     H N N 449 
TYR HB2    H N N 450 
TYR HB3    H N N 451 
TYR HD1    H N N 452 
TYR HD2    H N N 453 
TYR HE1    H N N 454 
TYR HE2    H N N 455 
TYR HH     H N N 456 
TYR HXT    H N N 457 
VAL N      N N N 458 
VAL CA     C N S 459 
VAL C      C N N 460 
VAL O      O N N 461 
VAL CB     C N N 462 
VAL CG1    C N N 463 
VAL CG2    C N N 464 
VAL OXT    O N N 465 
VAL H      H N N 466 
VAL H2     H N N 467 
VAL HA     H N N 468 
VAL HB     H N N 469 
VAL HG11   H N N 470 
VAL HG12   H N N 471 
VAL HG13   H N N 472 
VAL HG21   H N N 473 
VAL HG22   H N N 474 
VAL HG23   H N N 475 
VAL HXT    H N N 476 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
HIS N     CA     sing N N 220 
HIS N     H      sing N N 221 
HIS N     H2     sing N N 222 
HIS CA    C      sing N N 223 
HIS CA    CB     sing N N 224 
HIS CA    HA     sing N N 225 
HIS C     O      doub N N 226 
HIS C     OXT    sing N N 227 
HIS CB    CG     sing N N 228 
HIS CB    HB2    sing N N 229 
HIS CB    HB3    sing N N 230 
HIS CG    ND1    sing Y N 231 
HIS CG    CD2    doub Y N 232 
HIS ND1   CE1    doub Y N 233 
HIS ND1   HD1    sing N N 234 
HIS CD2   NE2    sing Y N 235 
HIS CD2   HD2    sing N N 236 
HIS CE1   NE2    sing Y N 237 
HIS CE1   HE1    sing N N 238 
HIS NE2   HE2    sing N N 239 
HIS OXT   HXT    sing N N 240 
HOH O     H1     sing N N 241 
HOH O     H2     sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Biotechnology and Biological Sciences Research Council (BBSRC)' 'United Kingdom' BB/T001968/1 1 
'Biotechnology and Biological Sciences Research Council (BBSRC)' 'United Kingdom' BB/M012107/1 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   5XGV 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8R1R 
_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]   0.014235 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014235 
_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]   0.004909 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . GLY A 1 11  ? -21.951 17.501  8.564   1.00 54.77  ? -8  GLY A N     1 
ATOM   2    C CA    . GLY A 1 11  ? -20.684 17.243  9.278   1.00 59.56  ? -8  GLY A CA    1 
ATOM   3    C C     . GLY A 1 11  ? -20.523 15.778  9.688   1.00 61.12  ? -8  GLY A C     1 
ATOM   4    O O     . GLY A 1 11  ? -19.426 15.228  9.575   1.00 59.36  ? -8  GLY A O     1 
ATOM   5    N N     . LEU A 1 12  ? -21.631 15.154  10.132  1.00 57.72  ? -7  LEU A N     1 
ATOM   6    C CA    . LEU A 1 12  ? -21.621 13.812  10.711  1.00 57.18  ? -7  LEU A CA    1 
ATOM   7    C C     . LEU A 1 12  ? -21.107 12.776  9.708   1.00 62.00  ? -7  LEU A C     1 
ATOM   8    O O     . LEU A 1 12  ? -20.600 11.727  10.125  1.00 56.57  ? -7  LEU A O     1 
ATOM   9    C CB    . LEU A 1 12  ? -23.029 13.434  11.193  1.00 57.09  ? -7  LEU A CB    1 
ATOM   10   C CG    . LEU A 1 12  ? -23.700 14.433  12.137  1.00 58.95  ? -7  LEU A CG    1 
ATOM   11   C CD1   . LEU A 1 12  ? -25.074 13.945  12.586  1.00 55.78  ? -7  LEU A CD1   1 
ATOM   12   C CD2   . LEU A 1 12  ? -22.812 14.713  13.334  1.00 55.36  ? -7  LEU A CD2   1 
ATOM   13   N N     . GLU A 1 13  ? -21.216 13.087  8.402   1.00 55.81  ? -6  GLU A N     1 
ATOM   14   C CA    . GLU A 1 13  ? -20.828 12.169  7.339   1.00 65.96  ? -6  GLU A CA    1 
ATOM   15   C C     . GLU A 1 13  ? -19.322 11.888  7.403   1.00 65.32  ? -6  GLU A C     1 
ATOM   16   O O     . GLU A 1 13  ? -18.895 10.808  6.990   1.00 61.83  ? -6  GLU A O     1 
ATOM   17   C CB    . GLU A 1 13  ? -21.154 12.689  5.926   1.00 71.64  ? -6  GLU A CB    1 
ATOM   18   C CG    . GLU A 1 13  ? -22.177 13.819  5.837   1.00 74.80  ? -6  GLU A CG    1 
ATOM   19   C CD    . GLU A 1 13  ? -21.623 15.241  5.877   1.00 83.10  ? -6  GLU A CD    1 
ATOM   20   O OE1   . GLU A 1 13  ? -22.443 16.182  5.882   1.00 98.16  ? -6  GLU A OE1   1 
ATOM   21   O OE2   . GLU A 1 13  ? -20.381 15.423  5.890   1.00 82.84  ? -6  GLU A OE2   1 
ATOM   22   N N     . VAL A 1 14  ? -18.536 12.864  7.901   1.00 61.26  ? -5  VAL A N     1 
ATOM   23   C CA    . VAL A 1 14  ? -17.078 12.776  7.954   1.00 64.87  ? -5  VAL A CA    1 
ATOM   24   C C     . VAL A 1 14  ? -16.625 11.789  9.036   1.00 64.11  ? -5  VAL A C     1 
ATOM   25   O O     . VAL A 1 14  ? -15.506 11.275  8.995   1.00 62.13  ? -5  VAL A O     1 
ATOM   26   C CB    . VAL A 1 14  ? -16.450 14.163  8.201   1.00 66.82  ? -5  VAL A CB    1 
ATOM   27   C CG1   . VAL A 1 14  ? -14.926 14.095  8.271   1.00 63.59  ? -5  VAL A CG1   1 
ATOM   28   C CG2   . VAL A 1 14  ? -16.907 15.170  7.151   1.00 71.27  ? -5  VAL A CG2   1 
ATOM   29   N N     . LEU A 1 15  ? -17.495 11.533  10.021  1.00 59.03  ? -4  LEU A N     1 
ATOM   30   C CA    . LEU A 1 15  ? -17.120 10.760  11.188  1.00 51.83  ? -4  LEU A CA    1 
ATOM   31   C C     . LEU A 1 15  ? -17.086 9.279   10.832  1.00 48.07  ? -4  LEU A C     1 
ATOM   32   O O     . LEU A 1 15  ? -17.789 8.827   9.929   1.00 49.93  ? -4  LEU A O     1 
ATOM   33   C CB    . LEU A 1 15  ? -18.117 11.079  12.299  1.00 57.86  ? -4  LEU A CB    1 
ATOM   34   C CG    . LEU A 1 15  ? -18.302 12.578  12.560  1.00 69.85  ? -4  LEU A CG    1 
ATOM   35   C CD1   . LEU A 1 15  ? -18.918 12.822  13.915  1.00 73.99  ? -4  LEU A CD1   1 
ATOM   36   C CD2   . LEU A 1 15  ? -16.987 13.342  12.450  1.00 74.68  ? -4  LEU A CD2   1 
ATOM   37   N N     . PHE A 1 16  ? -16.169 8.563   11.484  1.00 44.91  ? -3  PHE A N     1 
ATOM   38   C CA    . PHE A 1 16  ? -16.134 7.106   11.510  1.00 46.04  ? -3  PHE A CA    1 
ATOM   39   C C     . PHE A 1 16  ? -15.551 6.488   10.240  1.00 45.12  ? -3  PHE A C     1 
ATOM   40   O O     . PHE A 1 16  ? -15.596 5.262   10.090  1.00 51.32  ? -3  PHE A O     1 
ATOM   41   C CB    . PHE A 1 16  ? -17.545 6.541   11.680  1.00 45.39  ? -3  PHE A CB    1 
ATOM   42   C CG    . PHE A 1 16  ? -18.262 7.008   12.914  1.00 42.32  ? -3  PHE A CG    1 
ATOM   43   C CD1   . PHE A 1 16  ? -17.751 6.728   14.167  1.00 36.00  ? -3  PHE A CD1   1 
ATOM   44   C CD2   . PHE A 1 16  ? -19.455 7.708   12.821  1.00 44.49  ? -3  PHE A CD2   1 
ATOM   45   C CE1   . PHE A 1 16  ? -18.432 7.113   15.304  1.00 35.92  ? -3  PHE A CE1   1 
ATOM   46   C CE2   . PHE A 1 16  ? -20.114 8.121   13.967  1.00 42.79  ? -3  PHE A CE2   1 
ATOM   47   C CZ    . PHE A 1 16  ? -19.620 7.794   15.197  1.00 39.60  ? -3  PHE A CZ    1 
ATOM   48   N N     . GLN A 1 17  ? -15.049 7.316   9.318   1.00 43.96  ? -2  GLN A N     1 
ATOM   49   C CA    . GLN A 1 17  ? -14.631 6.810   8.011   1.00 54.57  ? -2  GLN A CA    1 
ATOM   50   C C     . GLN A 1 17  ? -13.167 6.358   8.033   1.00 53.18  ? -2  GLN A C     1 
ATOM   51   O O     . GLN A 1 17  ? -12.738 5.584   7.176   1.00 45.88  ? -2  GLN A O     1 
ATOM   52   C CB    . GLN A 1 17  ? -14.880 7.841   6.904   1.00 54.24  ? -2  GLN A CB    1 
ATOM   53   C CG    . GLN A 1 17  ? -16.355 8.192   6.724   1.00 55.76  ? -2  GLN A CG    1 
ATOM   54   C CD    . GLN A 1 17  ? -17.258 6.979   6.753   1.00 55.79  ? -2  GLN A CD    1 
ATOM   55   O OE1   . GLN A 1 17  ? -18.183 6.891   7.556   1.00 51.36  ? -2  GLN A OE1   1 
ATOM   56   N NE2   . GLN A 1 17  ? -17.000 6.032   5.868   1.00 56.65  ? -2  GLN A NE2   1 
ATOM   57   N N     . GLY A 1 18  ? -12.396 6.829   9.010   1.00 45.41  ? -1  GLY A N     1 
ATOM   58   C CA    . GLY A 1 18  ? -11.041 6.338   9.177   1.00 39.41  ? -1  GLY A CA    1 
ATOM   59   C C     . GLY A 1 18  ? -10.070 7.134   8.325   1.00 38.40  ? -1  GLY A C     1 
ATOM   60   O O     . GLY A 1 18  ? -10.453 8.068   7.646   1.00 40.19  ? -1  GLY A O     1 
ATOM   61   N N     . PRO A 1 19  ? -8.786  6.750   8.290   1.00 34.43  ? 0   PRO A N     1 
ATOM   62   C CA    . PRO A 1 19  ? -7.810  7.464   7.466   1.00 32.23  ? 0   PRO A CA    1 
ATOM   63   C C     . PRO A 1 19  ? -8.128  7.340   5.973   1.00 37.51  ? 0   PRO A C     1 
ATOM   64   O O     . PRO A 1 19  ? -8.667  6.340   5.526   1.00 32.86  ? 0   PRO A O     1 
ATOM   65   C CB    . PRO A 1 19  ? -6.482  6.764   7.794   1.00 34.78  ? 0   PRO A CB    1 
ATOM   66   C CG    . PRO A 1 19  ? -6.745  6.026   9.100   1.00 33.07  ? 0   PRO A CG    1 
ATOM   67   C CD    . PRO A 1 19  ? -8.205  5.613   9.018   1.00 37.40  ? 0   PRO A CD    1 
ATOM   68   N N     . MET A 1 20  ? -7.782  8.353   5.178   1.00 34.73  ? 1   MET A N     1 
ATOM   69   C CA    . MET A 1 20  ? -8.058  8.278   3.744   1.00 40.22  ? 1   MET A CA    1 
ATOM   70   C C     . MET A 1 20  ? -7.007  9.057   2.975   1.00 37.62  ? 1   MET A C     1 
ATOM   71   O O     . MET A 1 20  ? -6.763  10.197  3.318   1.00 32.89  ? 1   MET A O     1 
ATOM   72   C CB    . MET A 1 20  ? -9.435  8.873   3.422   1.00 48.39  ? 1   MET A CB    1 
ATOM   73   C CG    . MET A 1 20  ? -10.478 7.838   3.094   1.00 65.44  ? 1   MET A CG    1 
ATOM   74   S SD    . MET A 1 20  ? -11.705 8.533   1.958   1.00 91.72  ? 1   MET A SD    1 
ATOM   75   C CE    . MET A 1 20  ? -10.906 8.283   0.369   1.00 88.22  ? 1   MET A CE    1 
ATOM   76   N N     . THR A 1 21  ? -6.370  8.438   1.967   1.00 40.20  ? 2   THR A N     1 
ATOM   77   C CA    . THR A 1 21  ? -5.472  9.185   1.086   1.00 47.09  ? 2   THR A CA    1 
ATOM   78   C C     . THR A 1 21  ? -6.304  9.737   -0.077  1.00 43.92  ? 2   THR A C     1 
ATOM   79   O O     . THR A 1 21  ? -7.366  9.205   -0.401  1.00 37.29  ? 2   THR A O     1 
ATOM   80   C CB    . THR A 1 21  ? -4.257  8.344   0.679   1.00 47.79  ? 2   THR A CB    1 
ATOM   81   O OG1   . THR A 1 21  ? -4.815  7.318   -0.135  1.00 58.51  ? 2   THR A OG1   1 
ATOM   82   N N     . ASP A 1 22  ? -5.843  10.869  -0.623  1.00 39.08  ? 3   ASP A N     1 
ATOM   83   C CA    . ASP A 1 22  ? -6.482  11.589  -1.723  1.00 36.69  ? 3   ASP A CA    1 
ATOM   84   C C     . ASP A 1 22  ? -6.531  10.685  -2.953  1.00 33.17  ? 3   ASP A C     1 
ATOM   85   O O     . ASP A 1 22  ? -5.483  10.291  -3.454  1.00 31.30  ? 3   ASP A O     1 
ATOM   86   C CB    . ASP A 1 22  ? -5.685  12.855  -2.065  1.00 38.51  ? 3   ASP A CB    1 
ATOM   87   C CG    . ASP A 1 22  ? -5.850  13.964  -1.040  1.00 46.52  ? 3   ASP A CG    1 
ATOM   88   O OD1   . ASP A 1 22  ? -6.878  13.932  -0.302  1.00 47.87  ? 3   ASP A OD1   1 
ATOM   89   O OD2   . ASP A 1 22  ? -4.972  14.861  -1.009  1.00 44.15  ? 3   ASP A OD2   1 
ATOM   90   N N     . PRO A 1 23  ? -7.720  10.279  -3.433  1.00 30.06  ? 4   PRO A N     1 
ATOM   91   C CA    . PRO A 1 23  ? -7.793  9.298   -4.510  1.00 27.86  ? 4   PRO A CA    1 
ATOM   92   C C     . PRO A 1 23  ? -7.574  9.930   -5.880  1.00 27.35  ? 4   PRO A C     1 
ATOM   93   O O     . PRO A 1 23  ? -7.688  11.152  -6.050  1.00 28.14  ? 4   PRO A O     1 
ATOM   94   C CB    . PRO A 1 23  ? -9.239  8.808   -4.386  1.00 28.30  ? 4   PRO A CB    1 
ATOM   95   C CG    . PRO A 1 23  ? -9.997  10.055  -3.967  1.00 31.40  ? 4   PRO A CG    1 
ATOM   96   C CD    . PRO A 1 23  ? -9.039  10.820  -3.082  1.00 29.58  ? 4   PRO A CD    1 
ATOM   97   N N     . VAL A 1 24  ? -7.220  9.078   -6.849  1.00 28.91  ? 5   VAL A N     1 
ATOM   98   C CA    . VAL A 1 24  ? -7.427  9.411   -8.246  1.00 26.49  ? 5   VAL A CA    1 
ATOM   99   C C     . VAL A 1 24  ? -8.920  9.368   -8.484  1.00 26.15  ? 5   VAL A C     1 
ATOM   100  O O     . VAL A 1 24  ? -9.550  8.351   -8.193  1.00 28.63  ? 5   VAL A O     1 
ATOM   101  C CB    . VAL A 1 24  ? -6.691  8.429   -9.173  1.00 27.37  ? 5   VAL A CB    1 
ATOM   102  C CG1   . VAL A 1 24  ? -7.001  8.761   -10.613 1.00 27.13  ? 5   VAL A CG1   1 
ATOM   103  C CG2   . VAL A 1 24  ? -5.192  8.427   -8.902  1.00 27.14  ? 5   VAL A CG2   1 
ATOM   104  N N     . ILE A 1 25  ? -9.500  10.492  -8.924  1.00 22.90  ? 6   ILE A N     1 
ATOM   105  C CA    . ILE A 1 25  ? -10.908 10.506  -9.298  1.00 23.56  ? 6   ILE A CA    1 
ATOM   106  C C     . ILE A 1 25  ? -11.047 10.262  -10.812 1.00 25.63  ? 6   ILE A C     1 
ATOM   107  O O     . ILE A 1 25  ? -10.635 11.082  -11.621 1.00 26.21  ? 6   ILE A O     1 
ATOM   108  C CB    . ILE A 1 25  ? -11.559 11.844  -8.907  1.00 24.56  ? 6   ILE A CB    1 
ATOM   109  C CG1   . ILE A 1 25  ? -11.301 12.186  -7.437  1.00 28.01  ? 6   ILE A CG1   1 
ATOM   110  C CG2   . ILE A 1 25  ? -13.052 11.814  -9.222  1.00 27.91  ? 6   ILE A CG2   1 
ATOM   111  C CD1   . ILE A 1 25  ? -11.805 13.578  -7.052  1.00 30.05  ? 6   ILE A CD1   1 
ATOM   112  N N     . VAL A 1 26  ? -11.713 9.160   -11.165 1.00 25.38  ? 7   VAL A N     1 
ATOM   113  C CA    . VAL A 1 26  ? -12.018 8.785   -12.531 1.00 23.87  ? 7   VAL A CA    1 
ATOM   114  C C     . VAL A 1 26  ? -13.445 9.208   -12.800 1.00 25.87  ? 7   VAL A C     1 
ATOM   115  O O     . VAL A 1 26  ? -14.392 8.679   -12.187 1.00 30.01  ? 7   VAL A O     1 
ATOM   116  C CB    . VAL A 1 26  ? -11.822 7.270   -12.730 1.00 23.94  ? 7   VAL A CB    1 
ATOM   117  C CG1   . VAL A 1 26  ? -12.139 6.840   -14.152 1.00 27.86  ? 7   VAL A CG1   1 
ATOM   118  C CG2   . VAL A 1 26  ? -10.433 6.852   -12.359 1.00 24.87  ? 7   VAL A CG2   1 
ATOM   119  N N     . VAL A 1 27  ? -13.589 10.146  -13.741 1.00 26.09  ? 8   VAL A N     1 
ATOM   120  C CA    . VAL A 1 27  ? -14.911 10.612  -14.108 1.00 26.44  ? 8   VAL A CA    1 
ATOM   121  C C     . VAL A 1 27  ? -15.384 9.842   -15.324 1.00 30.21  ? 8   VAL A C     1 
ATOM   122  O O     . VAL A 1 27  ? -14.935 10.112  -16.438 1.00 28.18  ? 8   VAL A O     1 
ATOM   123  C CB    . VAL A 1 27  ? -14.940 12.121  -14.362 1.00 28.54  ? 8   VAL A CB    1 
ATOM   124  C CG1   . VAL A 1 27  ? -16.360 12.582  -14.667 1.00 28.65  ? 8   VAL A CG1   1 
ATOM   125  C CG2   . VAL A 1 27  ? -14.293 12.862  -13.219 1.00 29.57  ? 8   VAL A CG2   1 
ATOM   126  N N     . GLY A 1 28  ? -16.316 8.920   -15.071 1.00 26.15  ? 9   GLY A N     1 
ATOM   127  C CA    . GLY A 1 28  ? -16.921 8.098   -16.086 1.00 28.42  ? 9   GLY A CA    1 
ATOM   128  C C     . GLY A 1 28  ? -16.671 6.621   -15.801 1.00 25.52  ? 9   GLY A C     1 
ATOM   129  O O     . GLY A 1 28  ? -15.547 6.245   -15.519 1.00 27.66  ? 9   GLY A O     1 
ATOM   130  N N     . ALA A 1 29  ? -17.745 5.825   -15.815 1.00 26.23  ? 10  ALA A N     1 
ATOM   131  C CA    . ALA A 1 29  ? -17.669 4.380   -15.602 1.00 28.96  ? 10  ALA A CA    1 
ATOM   132  C C     . ALA A 1 29  ? -18.004 3.601   -16.880 1.00 28.55  ? 10  ALA A C     1 
ATOM   133  O O     . ALA A 1 29  ? -18.612 2.527   -16.848 1.00 31.04  ? 10  ALA A O     1 
ATOM   134  C CB    . ALA A 1 29  ? -18.626 3.987   -14.499 1.00 29.98  ? 10  ALA A CB    1 
ATOM   135  N N     . GLY A 1 30  ? -17.586 4.136   -18.024 1.00 27.26  ? 11  GLY A N     1 
ATOM   136  C CA    . GLY A 1 30  ? -17.557 3.376   -19.256 1.00 28.08  ? 11  GLY A CA    1 
ATOM   137  C C     . GLY A 1 30  ? -16.315 2.491   -19.277 1.00 26.08  ? 11  GLY A C     1 
ATOM   138  O O     . GLY A 1 30  ? -15.617 2.378   -18.264 1.00 26.09  ? 11  GLY A O     1 
ATOM   139  N N     . PRO A 1 31  ? -16.033 1.865   -20.439 1.00 26.34  ? 12  PRO A N     1 
ATOM   140  C CA    . PRO A 1 31  ? -14.876 0.981   -20.604 1.00 23.23  ? 12  PRO A CA    1 
ATOM   141  C C     . PRO A 1 31  ? -13.564 1.652   -20.236 1.00 23.30  ? 12  PRO A C     1 
ATOM   142  O O     . PRO A 1 31  ? -12.786 1.047   -19.527 1.00 21.90  ? 12  PRO A O     1 
ATOM   143  C CB    . PRO A 1 31  ? -14.884 0.640   -22.085 1.00 23.87  ? 12  PRO A CB    1 
ATOM   144  C CG    . PRO A 1 31  ? -16.326 0.800   -22.497 1.00 28.90  ? 12  PRO A CG    1 
ATOM   145  C CD    . PRO A 1 31  ? -16.882 1.920   -21.645 1.00 26.12  ? 12  PRO A CD    1 
ATOM   146  N N     . THR A 1 32  ? -13.391 2.928   -20.597 1.00 22.22  ? 13  THR A N     1 
ATOM   147  C CA    . THR A 1 32  ? -12.120 3.559   -20.298 1.00 23.56  ? 13  THR A CA    1 
ATOM   148  C C     . THR A 1 32  ? -11.942 3.693   -18.785 1.00 23.46  ? 13  THR A C     1 
ATOM   149  O O     . THR A 1 32  ? -10.902 3.342   -18.228 1.00 22.84  ? 13  THR A O     1 
ATOM   150  C CB    . THR A 1 32  ? -12.034 4.932   -20.977 1.00 23.04  ? 13  THR A CB    1 
ATOM   151  O OG1   . THR A 1 32  ? -12.156 4.861   -22.406 1.00 23.94  ? 13  THR A OG1   1 
ATOM   152  C CG2   . THR A 1 32  ? -10.742 5.625   -20.631 1.00 25.19  ? 13  THR A CG2   1 
ATOM   153  N N     . GLY A 1 33  ? -12.954 4.288   -18.114 1.00 22.98  ? 14  GLY A N     1 
ATOM   154  C CA    . GLY A 1 33  ? -12.904 4.568   -16.693 1.00 22.93  ? 14  GLY A CA    1 
ATOM   155  C C     . GLY A 1 33  ? -12.685 3.324   -15.861 1.00 22.76  ? 14  GLY A C     1 
ATOM   156  O O     . GLY A 1 33  ? -11.883 3.331   -14.941 1.00 26.22  ? 14  GLY A O     1 
ATOM   157  N N     . LEU A 1 34  ? -13.450 2.277   -16.172 1.00 23.12  ? 15  LEU A N     1 
ATOM   158  C CA    . LEU A 1 34  ? -13.378 1.052   -15.401 1.00 25.10  ? 15  LEU A CA    1 
ATOM   159  C C     . LEU A 1 34  ? -12.069 0.333   -15.669 1.00 24.49  ? 15  LEU A C     1 
ATOM   160  O O     . LEU A 1 34  ? -11.550 -0.258  -14.751 1.00 26.08  ? 15  LEU A O     1 
ATOM   161  C CB    . LEU A 1 34  ? -14.587 0.184   -15.727 1.00 25.09  ? 15  LEU A CB    1 
ATOM   162  C CG    . LEU A 1 34  ? -15.909 0.781   -15.240 1.00 26.92  ? 15  LEU A CG    1 
ATOM   163  C CD1   . LEU A 1 34  ? -17.040 -0.187  -15.530 1.00 31.68  ? 15  LEU A CD1   1 
ATOM   164  C CD2   . LEU A 1 34  ? -15.823 1.065   -13.752 1.00 32.75  ? 15  LEU A CD2   1 
ATOM   165  N N     . MET A 1 35  ? -11.543 0.342   -16.902 1.00 23.40  ? 16  MET A N     1 
ATOM   166  C CA    . MET A 1 35  ? -10.257 -0.303  -17.133 1.00 23.08  ? 16  MET A CA    1 
ATOM   167  C C     . MET A 1 35  ? -9.194  0.432   -16.296 1.00 23.03  ? 16  MET A C     1 
ATOM   168  O O     . MET A 1 35  ? -8.283  -0.164  -15.720 1.00 23.87  ? 16  MET A O     1 
ATOM   169  C CB    . MET A 1 35  ? -9.875  -0.281  -18.620 1.00 22.61  ? 16  MET A CB    1 
ATOM   170  C CG    . MET A 1 35  ? -8.566  -0.989  -18.925 1.00 26.94  ? 16  MET A CG    1 
ATOM   171  S SD    . MET A 1 35  ? -8.857  -2.774  -18.619 1.00 30.61  ? 16  MET A SD    1 
ATOM   172  C CE    . MET A 1 35  ? -7.282  -3.502  -19.079 1.00 32.06  ? 16  MET A CE    1 
ATOM   173  N N     . LEU A 1 36  ? -9.264  1.756   -16.290 1.00 21.82  ? 17  LEU A N     1 
ATOM   174  C CA    . LEU A 1 36  ? -8.268  2.543   -15.586 1.00 22.92  ? 17  LEU A CA    1 
ATOM   175  C C     . LEU A 1 36  ? -8.385  2.282   -14.085 1.00 22.30  ? 17  LEU A C     1 
ATOM   176  O O     . LEU A 1 36  ? -7.405  2.075   -13.383 1.00 23.94  ? 17  LEU A O     1 
ATOM   177  C CB    . LEU A 1 36  ? -8.522  4.012   -15.922 1.00 24.08  ? 17  LEU A CB    1 
ATOM   178  C CG    . LEU A 1 36  ? -7.698  5.016   -15.123 1.00 27.18  ? 17  LEU A CG    1 
ATOM   179  C CD1   . LEU A 1 36  ? -6.204  4.777   -15.296 1.00 23.73  ? 17  LEU A CD1   1 
ATOM   180  C CD2   . LEU A 1 36  ? -8.030  6.432   -15.538 1.00 28.70  ? 17  LEU A CD2   1 
ATOM   181  N N     . ALA A 1 37  ? -9.618  2.240   -13.586 1.00 23.61  ? 18  ALA A N     1 
ATOM   182  C CA    . ALA A 1 37  ? -9.831  1.914   -12.183 1.00 27.22  ? 18  ALA A CA    1 
ATOM   183  C C     . ALA A 1 37  ? -9.287  0.522   -11.841 1.00 26.41  ? 18  ALA A C     1 
ATOM   184  O O     . ALA A 1 37  ? -8.735  0.364   -10.763 1.00 27.37  ? 18  ALA A O     1 
ATOM   185  C CB    . ALA A 1 37  ? -11.286 2.004   -11.828 1.00 29.19  ? 18  ALA A CB    1 
ATOM   186  N N     . CYS A 1 38  ? -9.438  -0.467  -12.734 1.00 27.40  ? 19  CYS A N     1 
ATOM   187  C CA    . CYS A 1 38  ? -8.838  -1.786  -12.497 1.00 25.35  ? 19  CYS A CA    1 
ATOM   188  C C     . CYS A 1 38  ? -7.313  -1.705  -12.454 1.00 26.62  ? 19  CYS A C     1 
ATOM   189  O O     . CYS A 1 38  ? -6.661  -2.400  -11.680 1.00 28.50  ? 19  CYS A O     1 
ATOM   190  C CB    . CYS A 1 38  ? -9.286  -2.835  -13.494 1.00 28.87  ? 19  CYS A CB    1 
ATOM   191  S SG    . CYS A 1 38  ? -11.052 -3.223  -13.396 1.00 30.85  ? 19  CYS A SG    1 
ATOM   192  N N     . GLU A 1 39  ? -6.700  -0.890  -13.310 1.00 25.01  ? 20  GLU A N     1 
ATOM   193  C CA    . GLU A 1 39  ? -5.253  -0.793  -13.342 1.00 26.05  ? 20  GLU A CA    1 
ATOM   194  C C     . GLU A 1 39  ? -4.755  -0.123  -12.062 1.00 29.01  ? 20  GLU A C     1 
ATOM   195  O O     . GLU A 1 39  ? -3.771  -0.560  -11.483 1.00 27.33  ? 20  GLU A O     1 
ATOM   196  C CB    . GLU A 1 39  ? -4.798  0.016   -14.560 1.00 25.68  ? 20  GLU A CB    1 
ATOM   197  C CG    . GLU A 1 39  ? -5.011  -0.760  -15.853 1.00 27.51  ? 20  GLU A CG    1 
ATOM   198  C CD    . GLU A 1 39  ? -4.108  -1.978  -15.990 1.00 31.32  ? 20  GLU A CD    1 
ATOM   199  O OE1   . GLU A 1 39  ? -2.897  -1.826  -15.696 1.00 29.19  ? 20  GLU A OE1   1 
ATOM   200  O OE2   . GLU A 1 39  ? -4.607  -3.052  -16.431 1.00 29.47  ? 20  GLU A OE2   1 
ATOM   201  N N     . LEU A 1 40  ? -5.416  0.968   -11.661 1.00 26.84  ? 21  LEU A N     1 
ATOM   202  C CA    . LEU A 1 40  ? -5.097  1.651   -10.413 1.00 26.91  ? 21  LEU A CA    1 
ATOM   203  C C     . LEU A 1 40  ? -5.287  0.750   -9.196  1.00 30.23  ? 21  LEU A C     1 
ATOM   204  O O     . LEU A 1 40  ? -4.394  0.663   -8.356  1.00 31.35  ? 21  LEU A O     1 
ATOM   205  C CB    . LEU A 1 40  ? -5.975  2.896   -10.315 1.00 28.42  ? 21  LEU A CB    1 
ATOM   206  C CG    . LEU A 1 40  ? -5.552  4.024   -11.260 1.00 28.74  ? 21  LEU A CG    1 
ATOM   207  C CD1   . LEU A 1 40  ? -6.634  5.079   -11.337 1.00 27.26  ? 21  LEU A CD1   1 
ATOM   208  C CD2   . LEU A 1 40  ? -4.233  4.619   -10.824 1.00 28.79  ? 21  LEU A CD2   1 
ATOM   209  N N     . GLY A 1 41  ? -6.431  0.068   -9.127  1.00 28.28  ? 22  GLY A N     1 
ATOM   210  C CA    . GLY A 1 41  ? -6.707  -0.903  -8.085  1.00 33.17  ? 22  GLY A CA    1 
ATOM   211  C C     . GLY A 1 41  ? -5.638  -1.983  -7.972  1.00 32.68  ? 22  GLY A C     1 
ATOM   212  O O     . GLY A 1 41  ? -5.165  -2.277  -6.874  1.00 29.14  ? 22  GLY A O     1 
ATOM   213  N N     . LEU A 1 42  ? -5.254  -2.573  -9.109  1.00 30.79  ? 23  LEU A N     1 
ATOM   214  C CA    . LEU A 1 42  ? -4.281  -3.651  -9.116  1.00 29.68  ? 23  LEU A CA    1 
ATOM   215  C C     . LEU A 1 42  ? -2.952  -3.129  -8.614  1.00 30.64  ? 23  LEU A C     1 
ATOM   216  O O     . LEU A 1 42  ? -2.226  -3.819  -7.918  1.00 32.16  ? 23  LEU A O     1 
ATOM   217  C CB    . LEU A 1 42  ? -4.142  -4.190  -10.542 1.00 30.49  ? 23  LEU A CB    1 
ATOM   218  C CG    . LEU A 1 42  ? -3.106  -5.294  -10.762 1.00 33.01  ? 23  LEU A CG    1 
ATOM   219  C CD1   . LEU A 1 42  ? -3.479  -6.540  -9.970  1.00 33.79  ? 23  LEU A CD1   1 
ATOM   220  C CD2   . LEU A 1 42  ? -3.025  -5.592  -12.252 1.00 32.28  ? 23  LEU A CD2   1 
ATOM   221  N N     . ALA A 1 43  ? -2.628  -1.894  -8.973  1.00 31.60  ? 24  ALA A N     1 
ATOM   222  C CA    . ALA A 1 43  ? -1.330  -1.331  -8.637  1.00 35.58  ? 24  ALA A CA    1 
ATOM   223  C C     . ALA A 1 43  ? -1.321  -0.786  -7.207  1.00 35.06  ? 24  ALA A C     1 
ATOM   224  O O     . ALA A 1 43  ? -0.283  -0.320  -6.741  1.00 38.11  ? 24  ALA A O     1 
ATOM   225  C CB    . ALA A 1 43  ? -0.995  -0.261  -9.643  1.00 36.78  ? 24  ALA A CB    1 
ATOM   226  N N     . GLY A 1 44  ? -2.476  -0.806  -6.530  1.00 36.90  ? 25  GLY A N     1 
ATOM   227  C CA    . GLY A 1 44  ? -2.578  -0.416  -5.126  1.00 35.14  ? 25  GLY A CA    1 
ATOM   228  C C     . GLY A 1 44  ? -2.731  1.094   -4.922  1.00 38.23  ? 25  GLY A C     1 
ATOM   229  O O     . GLY A 1 44  ? -2.492  1.600   -3.826  1.00 35.70  ? 25  GLY A O     1 
ATOM   230  N N     . ALA A 1 45  ? -3.173  1.827   -5.944  1.00 31.91  ? 26  ALA A N     1 
ATOM   231  C CA    . ALA A 1 45  ? -3.381  3.262   -5.800  1.00 33.19  ? 26  ALA A CA    1 
ATOM   232  C C     . ALA A 1 45  ? -4.813  3.508   -5.338  1.00 30.37  ? 26  ALA A C     1 
ATOM   233  O O     . ALA A 1 45  ? -5.737  2.812   -5.763  1.00 30.74  ? 26  ALA A O     1 
ATOM   234  C CB    . ALA A 1 45  ? -3.091  3.968   -7.095  1.00 30.33  ? 26  ALA A CB    1 
ATOM   235  N N     . PRO A 1 46  ? -5.077  4.559   -4.526  1.00 32.44  ? 27  PRO A N     1 
ATOM   236  C CA    . PRO A 1 46  ? -6.455  4.914   -4.184  1.00 33.24  ? 27  PRO A CA    1 
ATOM   237  C C     . PRO A 1 46  ? -7.259  5.442   -5.375  1.00 30.80  ? 27  PRO A C     1 
ATOM   238  O O     . PRO A 1 46  ? -6.769  6.301   -6.095  1.00 31.98  ? 27  PRO A O     1 
ATOM   239  C CB    . PRO A 1 46  ? -6.258  6.052   -3.164  1.00 35.15  ? 27  PRO A CB    1 
ATOM   240  C CG    . PRO A 1 46  ? -4.923  6.680   -3.565  1.00 34.03  ? 27  PRO A CG    1 
ATOM   241  C CD    . PRO A 1 46  ? -4.076  5.496   -3.971  1.00 35.15  ? 27  PRO A CD    1 
ATOM   242  N N     . VAL A 1 47  ? -8.501  4.983   -5.560  1.00 28.29  ? 28  VAL A N     1 
ATOM   243  C CA    . VAL A 1 47  ? -9.286  5.418   -6.703  1.00 31.65  ? 28  VAL A CA    1 
ATOM   244  C C     . VAL A 1 47  ? -10.760 5.441   -6.336  1.00 32.56  ? 28  VAL A C     1 
ATOM   245  O O     . VAL A 1 47  ? -11.221 4.607   -5.560  1.00 33.69  ? 28  VAL A O     1 
ATOM   246  C CB    . VAL A 1 47  ? -8.999  4.532   -7.937  1.00 33.28  ? 28  VAL A CB    1 
ATOM   247  C CG1   . VAL A 1 47  ? -9.044  3.049   -7.589  1.00 32.95  ? 28  VAL A CG1   1 
ATOM   248  C CG2   . VAL A 1 47  ? -9.893  4.889   -9.125  1.00 30.74  ? 28  VAL A CG2   1 
ATOM   249  N N     . VAL A 1 48  ? -11.437 6.463   -6.849  1.00 30.03  ? 29  VAL A N     1 
ATOM   250  C CA    . VAL A 1 48  ? -12.882 6.590   -6.870  1.00 28.90  ? 29  VAL A CA    1 
ATOM   251  C C     . VAL A 1 48  ? -13.354 6.802   -8.305  1.00 28.72  ? 29  VAL A C     1 
ATOM   252  O O     . VAL A 1 48  ? -12.830 7.682   -8.989  1.00 27.01  ? 29  VAL A O     1 
ATOM   253  C CB    . VAL A 1 48  ? -13.336 7.811   -6.032  1.00 30.49  ? 29  VAL A CB    1 
ATOM   254  C CG1   . VAL A 1 48  ? -14.833 8.017   -6.124  1.00 34.24  ? 29  VAL A CG1   1 
ATOM   255  C CG2   . VAL A 1 48  ? -12.883 7.735   -4.579  1.00 33.97  ? 29  VAL A CG2   1 
ATOM   256  N N     . VAL A 1 49  ? -14.451 6.131   -8.694  1.00 25.28  ? 30  VAL A N     1 
ATOM   257  C CA    . VAL A 1 49  ? -15.075 6.267   -9.998  1.00 28.29  ? 30  VAL A CA    1 
ATOM   258  C C     . VAL A 1 49  ? -16.448 6.911   -9.806  1.00 29.48  ? 30  VAL A C     1 
ATOM   259  O O     . VAL A 1 49  ? -17.234 6.446   -8.973  1.00 31.40  ? 30  VAL A O     1 
ATOM   260  C CB    . VAL A 1 49  ? -15.228 4.898   -10.695 1.00 29.92  ? 30  VAL A CB    1 
ATOM   261  C CG1   . VAL A 1 49  ? -15.978 5.055   -12.000 1.00 31.28  ? 30  VAL A CG1   1 
ATOM   262  C CG2   . VAL A 1 49  ? -13.874 4.210   -10.877 1.00 31.85  ? 30  VAL A CG2   1 
ATOM   263  N N     . LEU A 1 50  ? -16.687 7.999   -10.531 1.00 28.22  ? 31  LEU A N     1 
ATOM   264  C CA    . LEU A 1 50  ? -17.970 8.686   -10.560 1.00 30.53  ? 31  LEU A CA    1 
ATOM   265  C C     . LEU A 1 50  ? -18.637 8.449   -11.908 1.00 32.86  ? 31  LEU A C     1 
ATOM   266  O O     . LEU A 1 50  ? -17.972 8.329   -12.940 1.00 33.21  ? 31  LEU A O     1 
ATOM   267  C CB    . LEU A 1 50  ? -17.780 10.189  -10.362 1.00 31.39  ? 31  LEU A CB    1 
ATOM   268  C CG    . LEU A 1 50  ? -16.915 10.625  -9.182  1.00 32.03  ? 31  LEU A CG    1 
ATOM   269  C CD1   . LEU A 1 50  ? -16.664 12.122  -9.268  1.00 31.42  ? 31  LEU A CD1   1 
ATOM   270  C CD2   . LEU A 1 50  ? -17.538 10.231  -7.840  1.00 31.75  ? 31  LEU A CD2   1 
ATOM   271  N N     . ASP A 1 51  ? -19.970 8.438   -11.917 1.00 30.07  ? 32  ASP A N     1 
ATOM   272  C CA    . ASP A 1 51  ? -20.695 8.429   -13.166 1.00 30.56  ? 32  ASP A CA    1 
ATOM   273  C C     . ASP A 1 51  ? -22.082 9.019   -12.945 1.00 32.08  ? 32  ASP A C     1 
ATOM   274  O O     . ASP A 1 51  ? -22.723 8.722   -11.928 1.00 33.70  ? 32  ASP A O     1 
ATOM   275  C CB    . ASP A 1 51  ? -20.848 7.016   -13.728 1.00 32.19  ? 32  ASP A CB    1 
ATOM   276  C CG    . ASP A 1 51  ? -21.216 7.015   -15.209 1.00 36.34  ? 32  ASP A CG    1 
ATOM   277  O OD1   . ASP A 1 51  ? -22.405 7.241   -15.543 1.00 35.96  ? 32  ASP A OD1   1 
ATOM   278  O OD2   . ASP A 1 51  ? -20.316 6.746   -16.039 1.00 32.54  ? 32  ASP A OD2   1 
ATOM   279  N N     . ARG A 1 52  ? -22.492 9.854   -13.900 1.00 35.07  ? 33  ARG A N     1 
ATOM   280  C CA    . ARG A 1 52  ? -23.734 10.610  -13.843 1.00 39.08  ? 33  ARG A CA    1 
ATOM   281  C C     . ARG A 1 52  ? -24.934 9.685   -14.020 1.00 38.48  ? 33  ARG A C     1 
ATOM   282  O O     . ARG A 1 52  ? -26.022 10.037  -13.598 1.00 36.64  ? 33  ARG A O     1 
ATOM   283  C CB    . ARG A 1 52  ? -23.733 11.703  -14.915 1.00 44.92  ? 33  ARG A CB    1 
ATOM   284  C CG    . ARG A 1 52  ? -24.336 11.252  -16.239 1.00 49.46  ? 33  ARG A CG    1 
ATOM   285  C CD    . ARG A 1 52  ? -23.776 11.795  -17.533 1.00 56.86  ? 33  ARG A CD    1 
ATOM   286  N NE    . ARG A 1 52  ? -23.465 13.199  -17.522 1.00 57.60  ? 33  ARG A NE    1 
ATOM   287  C CZ    . ARG A 1 52  ? -23.139 13.884  -18.609 1.00 55.69  ? 33  ARG A CZ    1 
ATOM   288  N NH1   . ARG A 1 52  ? -23.229 13.315  -19.799 1.00 53.64  ? 33  ARG A NH1   1 
ATOM   289  N NH2   . ARG A 1 52  ? -22.750 15.142  -18.497 1.00 53.16  ? 33  ARG A NH2   1 
ATOM   290  N N     . ARG A 1 53  ? -24.766 8.501   -14.628 1.00 36.01  ? 34  ARG A N     1 
ATOM   291  C CA    . ARG A 1 53  ? -25.897 7.600   -14.829 1.00 37.85  ? 34  ARG A CA    1 
ATOM   292  C C     . ARG A 1 53  ? -26.249 6.866   -13.536 1.00 37.31  ? 34  ARG A C     1 
ATOM   293  O O     . ARG A 1 53  ? -25.410 6.677   -12.666 1.00 33.10  ? 34  ARG A O     1 
ATOM   294  C CB    . ARG A 1 53  ? -25.611 6.549   -15.909 1.00 39.78  ? 34  ARG A CB    1 
ATOM   295  C CG    . ARG A 1 53  ? -25.462 7.123   -17.312 1.00 40.14  ? 34  ARG A CG    1 
ATOM   296  C CD    . ARG A 1 53  ? -24.996 6.028   -18.256 1.00 44.25  ? 34  ARG A CD    1 
ATOM   297  N NE    . ARG A 1 53  ? -26.029 5.010   -18.326 1.00 45.11  ? 34  ARG A NE    1 
ATOM   298  C CZ    . ARG A 1 53  ? -27.121 5.110   -19.073 1.00 45.96  ? 34  ARG A CZ    1 
ATOM   299  N NH1   . ARG A 1 53  ? -27.179 6.006   -20.041 1.00 45.15  ? 34  ARG A NH1   1 
ATOM   300  N NH2   . ARG A 1 53  ? -28.136 4.294   -18.864 1.00 49.43  ? 34  ARG A NH2   1 
ATOM   301  N N     . ASP A 1 54  ? -27.515 6.448   -13.415 1.00 41.48  ? 35  ASP A N     1 
ATOM   302  C CA    . ASP A 1 54  ? -27.958 5.708   -12.245 1.00 40.98  ? 35  ASP A CA    1 
ATOM   303  C C     . ASP A 1 54  ? -27.538 4.246   -12.335 1.00 38.48  ? 35  ASP A C     1 
ATOM   304  O O     . ASP A 1 54  ? -27.383 3.587   -11.313 1.00 37.57  ? 35  ASP A O     1 
ATOM   305  C CB    . ASP A 1 54  ? -29.475 5.836   -12.054 1.00 48.81  ? 35  ASP A CB    1 
ATOM   306  C CG    . ASP A 1 54  ? -29.898 7.250   -11.673 1.00 53.65  ? 35  ASP A CG    1 
ATOM   307  O OD1   . ASP A 1 54  ? -29.189 7.879   -10.842 1.00 53.22  ? 35  ASP A OD1   1 
ATOM   308  O OD2   . ASP A 1 54  ? -30.928 7.720   -12.206 1.00 56.01  ? 35  ASP A OD2   1 
ATOM   309  N N     . ALA A 1 55  ? -27.393 3.728   -13.559 1.00 37.87  ? 36  ALA A N     1 
ATOM   310  C CA    . ALA A 1 55  ? -27.000 2.344   -13.760 1.00 37.06  ? 36  ALA A CA    1 
ATOM   311  C C     . ALA A 1 55  ? -26.220 2.223   -15.071 1.00 35.13  ? 36  ALA A C     1 
ATOM   312  O O     . ALA A 1 55  ? -26.214 3.157   -15.890 1.00 34.19  ? 36  ALA A O     1 
ATOM   313  C CB    . ALA A 1 55  ? -28.249 1.485   -13.792 1.00 37.76  ? 36  ALA A CB    1 
ATOM   314  N N     . PRO A 1 56  ? -25.571 1.067   -15.330 1.00 37.39  ? 37  PRO A N     1 
ATOM   315  C CA    . PRO A 1 56  ? -24.898 0.832   -16.611 1.00 39.34  ? 37  PRO A CA    1 
ATOM   316  C C     . PRO A 1 56  ? -25.862 1.011   -17.780 1.00 39.78  ? 37  PRO A C     1 
ATOM   317  O O     . PRO A 1 56  ? -27.075 0.788   -17.656 1.00 35.87  ? 37  PRO A O     1 
ATOM   318  C CB    . PRO A 1 56  ? -24.416 -0.629  -16.523 1.00 35.94  ? 37  PRO A CB    1 
ATOM   319  C CG    . PRO A 1 56  ? -24.324 -0.901  -15.067 1.00 36.41  ? 37  PRO A CG    1 
ATOM   320  C CD    . PRO A 1 56  ? -25.415 -0.076  -14.422 1.00 38.10  ? 37  PRO A CD    1 
ATOM   321  N N     . ASP A 1 57  ? -25.299 1.440   -18.912 1.00 35.90  ? 38  ASP A N     1 
ATOM   322  C CA    . ASP A 1 57  ? -26.065 1.655   -20.124 1.00 36.91  ? 38  ASP A CA    1 
ATOM   323  C C     . ASP A 1 57  ? -26.303 0.316   -20.829 1.00 37.80  ? 38  ASP A C     1 
ATOM   324  O O     . ASP A 1 57  ? -25.365 -0.300  -21.342 1.00 34.27  ? 38  ASP A O     1 
ATOM   325  C CB    . ASP A 1 57  ? -25.326 2.669   -20.986 1.00 38.99  ? 38  ASP A CB    1 
ATOM   326  C CG    . ASP A 1 57  ? -26.107 3.076   -22.209 1.00 43.73  ? 38  ASP A CG    1 
ATOM   327  O OD1   . ASP A 1 57  ? -27.195 2.485   -22.449 1.00 38.25  ? 38  ASP A OD1   1 
ATOM   328  O OD2   . ASP A 1 57  ? -25.613 3.970   -22.898 1.00 46.78  ? 38  ASP A OD2   1 
ATOM   329  N N     . PRO A 1 58  ? -27.560 -0.173  -20.934 1.00 34.86  ? 39  PRO A N     1 
ATOM   330  C CA    . PRO A 1 58  ? -27.821 -1.428  -21.648 1.00 37.01  ? 39  PRO A CA    1 
ATOM   331  C C     . PRO A 1 58  ? -27.685 -1.290  -23.168 1.00 32.79  ? 39  PRO A C     1 
ATOM   332  O O     . PRO A 1 58  ? -27.616 -2.276  -23.899 1.00 35.69  ? 39  PRO A O     1 
ATOM   333  C CB    . PRO A 1 58  ? -29.271 -1.722  -21.229 1.00 39.00  ? 39  PRO A CB    1 
ATOM   334  C CG    . PRO A 1 58  ? -29.879 -0.350  -21.115 1.00 36.45  ? 39  PRO A CG    1 
ATOM   335  C CD    . PRO A 1 58  ? -28.794 0.497   -20.477 1.00 38.44  ? 39  PRO A CD    1 
ATOM   336  N N     . HIS A 1 59  ? -27.646 -0.047  -23.651 1.00 32.02  ? 40  HIS A N     1 
ATOM   337  C CA    . HIS A 1 59  ? -27.626 0.257   -25.072 1.00 35.27  ? 40  HIS A CA    1 
ATOM   338  C C     . HIS A 1 59  ? -26.231 0.657   -25.536 1.00 34.93  ? 40  HIS A C     1 
ATOM   339  O O     . HIS A 1 59  ? -26.084 1.167   -26.648 1.00 36.28  ? 40  HIS A O     1 
ATOM   340  C CB    . HIS A 1 59  ? -28.531 1.459   -25.397 1.00 40.50  ? 40  HIS A CB    1 
ATOM   341  C CG    . HIS A 1 59  ? -29.981 1.172   -25.146 1.00 45.80  ? 40  HIS A CG    1 
ATOM   342  N ND1   . HIS A 1 59  ? -30.981 2.132   -25.190 1.00 47.44  ? 40  HIS A ND1   1 
ATOM   343  C CD2   . HIS A 1 59  ? -30.573 0.002   -24.850 1.00 39.80  ? 40  HIS A CD2   1 
ATOM   344  C CE1   . HIS A 1 59  ? -32.138 1.547   -24.917 1.00 46.43  ? 40  HIS A CE1   1 
ATOM   345  N NE2   . HIS A 1 59  ? -31.923 0.259   -24.703 1.00 43.88  ? 40  HIS A NE2   1 
ATOM   346  N N     . ALA A 1 60  ? -25.208 0.499   -24.685 1.00 32.84  ? 41  ALA A N     1 
ATOM   347  C CA    . ALA A 1 60  ? -23.871 0.859   -25.142 1.00 31.42  ? 41  ALA A CA    1 
ATOM   348  C C     . ALA A 1 60  ? -23.660 0.117   -26.476 1.00 29.99  ? 41  ALA A C     1 
ATOM   349  O O     . ALA A 1 60  ? -23.995 -1.058  -26.629 1.00 28.20  ? 41  ALA A O     1 
ATOM   350  C CB    . ALA A 1 60  ? -22.823 0.555   -24.107 1.00 32.90  ? 41  ALA A CB    1 
ATOM   351  N N     . PRO A 1 61  ? -23.248 0.836   -27.532 1.00 28.46  ? 42  PRO A N     1 
ATOM   352  C CA    . PRO A 1 61  ? -23.454 0.348   -28.891 1.00 27.08  ? 42  PRO A CA    1 
ATOM   353  C C     . PRO A 1 61  ? -22.401 -0.556  -29.523 1.00 28.61  ? 42  PRO A C     1 
ATOM   354  O O     . PRO A 1 61  ? -22.664 -1.120  -30.574 1.00 30.27  ? 42  PRO A O     1 
ATOM   355  C CB    . PRO A 1 61  ? -23.567 1.657   -29.656 1.00 27.24  ? 42  PRO A CB    1 
ATOM   356  C CG    . PRO A 1 61  ? -22.634 2.588   -28.927 1.00 31.59  ? 42  PRO A CG    1 
ATOM   357  C CD    . PRO A 1 61  ? -22.799 2.226   -27.474 1.00 28.95  ? 42  PRO A CD    1 
ATOM   358  N N     . GLY A 1 62  ? -21.214 -0.651  -28.931 1.00 31.00  ? 43  GLY A N     1 
ATOM   359  C CA    . GLY A 1 62  ? -20.124 -1.317  -29.619 1.00 29.50  ? 43  GLY A CA    1 
ATOM   360  C C     . GLY A 1 62  ? -20.353 -2.824  -29.652 1.00 28.49  ? 43  GLY A C     1 
ATOM   361  O O     . GLY A 1 62  ? -21.031 -3.371  -28.788 1.00 30.95  ? 43  GLY A O     1 
ATOM   362  N N     . GLN A 1 63  ? -19.829 -3.469  -30.683 1.00 28.15  ? 44  GLN A N     1 
ATOM   363  C CA    . GLN A 1 63  ? -19.749 -4.921  -30.712 1.00 31.72  ? 44  GLN A CA    1 
ATOM   364  C C     . GLN A 1 63  ? -18.397 -5.448  -31.183 1.00 28.82  ? 44  GLN A C     1 
ATOM   365  O O     . GLN A 1 63  ? -18.170 -6.639  -31.063 1.00 35.10  ? 44  GLN A O     1 
ATOM   366  C CB    . GLN A 1 63  ? -20.820 -5.502  -31.626 1.00 37.72  ? 44  GLN A CB    1 
ATOM   367  C CG    . GLN A 1 63  ? -22.143 -5.731  -30.914 1.00 40.63  ? 44  GLN A CG    1 
ATOM   368  C CD    . GLN A 1 63  ? -23.092 -6.531  -31.771 1.00 45.59  ? 44  GLN A CD    1 
ATOM   369  O OE1   . GLN A 1 63  ? -23.385 -6.163  -32.903 1.00 40.95  ? 44  GLN A OE1   1 
ATOM   370  N NE2   . GLN A 1 63  ? -23.576 -7.636  -31.237 1.00 54.52  ? 44  GLN A NE2   1 
ATOM   371  N N     . ALA A 1 64  ? -17.592 -4.635  -31.855 1.00 26.36  ? 45  ALA A N     1 
ATOM   372  C CA    . ALA A 1 64  ? -16.322 -5.108  -32.378 1.00 30.73  ? 45  ALA A CA    1 
ATOM   373  C C     . ALA A 1 64  ? -15.237 -4.806  -31.346 1.00 30.88  ? 45  ALA A C     1 
ATOM   374  O O     . ALA A 1 64  ? -14.944 -3.634  -31.086 1.00 30.96  ? 45  ALA A O     1 
ATOM   375  C CB    . ALA A 1 64  ? -15.999 -4.452  -33.704 1.00 30.81  ? 45  ALA A CB    1 
ATOM   376  N N     . VAL A 1 65  ? -14.663 -5.878  -30.785 1.00 26.61  ? 46  VAL A N     1 
ATOM   377  C CA    . VAL A 1 65  ? -13.588 -5.798  -29.809 1.00 28.24  ? 46  VAL A CA    1 
ATOM   378  C C     . VAL A 1 65  ? -12.358 -6.433  -30.451 1.00 29.55  ? 46  VAL A C     1 
ATOM   379  O O     . VAL A 1 65  ? -12.280 -7.652  -30.609 1.00 31.34  ? 46  VAL A O     1 
ATOM   380  C CB    . VAL A 1 65  ? -14.009 -6.495  -28.496 1.00 30.31  ? 46  VAL A CB    1 
ATOM   381  C CG1   . VAL A 1 65  ? -12.899 -6.620  -27.502 1.00 28.42  ? 46  VAL A CG1   1 
ATOM   382  C CG2   . VAL A 1 65  ? -15.200 -5.802  -27.844 1.00 32.76  ? 46  VAL A CG2   1 
ATOM   383  N N     . ASN A 1 66  ? -11.376 -5.614  -30.804 1.00 26.92  ? 47  ASN A N     1 
ATOM   384  C CA    . ASN A 1 66  ? -10.278 -6.093  -31.624 1.00 26.53  ? 47  ASN A CA    1 
ATOM   385  C C     . ASN A 1 66  ? -9.198  -6.734  -30.756 1.00 24.24  ? 47  ASN A C     1 
ATOM   386  O O     . ASN A 1 66  ? -9.252  -6.687  -29.535 1.00 23.82  ? 47  ASN A O     1 
ATOM   387  C CB    . ASN A 1 66  ? -9.779  -4.981  -32.544 1.00 25.23  ? 47  ASN A CB    1 
ATOM   388  C CG    . ASN A 1 66  ? -9.059  -3.838  -31.849 1.00 23.25  ? 47  ASN A CG    1 
ATOM   389  O OD1   . ASN A 1 66  ? -8.734  -3.924  -30.675 1.00 23.38  ? 47  ASN A OD1   1 
ATOM   390  N ND2   . ASN A 1 66  ? -8.782  -2.780  -32.590 1.00 25.56  ? 47  ASN A ND2   1 
ATOM   391  N N     . ALA A 1 67  ? -8.173  -7.278  -31.431 1.00 23.20  ? 48  ALA A N     1 
ATOM   392  C CA    . ALA A 1 67  ? -7.023  -7.898  -30.792 1.00 23.19  ? 48  ALA A CA    1 
ATOM   393  C C     . ALA A 1 67  ? -6.259  -6.973  -29.856 1.00 23.44  ? 48  ALA A C     1 
ATOM   394  O O     . ALA A 1 67  ? -5.757  -7.440  -28.834 1.00 24.67  ? 48  ALA A O     1 
ATOM   395  C CB    . ALA A 1 67  ? -6.110  -8.465  -31.842 1.00 23.54  ? 48  ALA A CB    1 
ATOM   396  N N     . GLY A 1 68  ? -6.226  -5.670  -30.158 1.00 22.89  ? 49  GLY A N     1 
ATOM   397  C CA    . GLY A 1 68  ? -5.603  -4.727  -29.244 1.00 24.10  ? 49  GLY A CA    1 
ATOM   398  C C     . GLY A 1 68  ? -6.284  -4.703  -27.884 1.00 22.47  ? 49  GLY A C     1 
ATOM   399  O O     . GLY A 1 68  ? -5.628  -4.634  -26.862 1.00 23.82  ? 49  GLY A O     1 
ATOM   400  N N     . VAL A 1 69  ? -7.626  -4.740  -27.869 1.00 22.46  ? 50  VAL A N     1 
ATOM   401  C CA    . VAL A 1 69  ? -8.357  -4.778  -26.630 1.00 25.83  ? 50  VAL A CA    1 
ATOM   402  C C     . VAL A 1 69  ? -8.109  -6.107  -25.925 1.00 23.75  ? 50  VAL A C     1 
ATOM   403  O O     . VAL A 1 69  ? -7.903  -6.136  -24.719 1.00 22.67  ? 50  VAL A O     1 
ATOM   404  C CB    . VAL A 1 69  ? -9.868  -4.593  -26.847 1.00 22.96  ? 50  VAL A CB    1 
ATOM   405  C CG1   . VAL A 1 69  ? -10.624 -4.864  -25.557 1.00 24.51  ? 50  VAL A CG1   1 
ATOM   406  C CG2   . VAL A 1 69  ? -10.199 -3.196  -27.378 1.00 26.57  ? 50  VAL A CG2   1 
ATOM   407  N N     . VAL A 1 70  ? -8.200  -7.201  -26.676 1.00 24.20  ? 51  VAL A N     1 
ATOM   408  C CA    . VAL A 1 70  ? -8.124  -8.509  -26.049 1.00 24.59  ? 51  VAL A CA    1 
ATOM   409  C C     . VAL A 1 70  ? -6.770  -8.682  -25.371 1.00 23.80  ? 51  VAL A C     1 
ATOM   410  O O     . VAL A 1 70  ? -6.690  -9.225  -24.282 1.00 23.95  ? 51  VAL A O     1 
ATOM   411  C CB    . VAL A 1 70  ? -8.406  -9.615  -27.078 1.00 24.76  ? 51  VAL A CB    1 
ATOM   412  C CG1   . VAL A 1 70  ? -8.106  -10.997 -26.514 1.00 28.69  ? 51  VAL A CG1   1 
ATOM   413  C CG2   . VAL A 1 70  ? -9.851  -9.487  -27.536 1.00 27.12  ? 51  VAL A CG2   1 
ATOM   414  N N     . ALA A 1 71  ? -5.707  -8.127  -25.977 1.00 25.16  ? 52  ALA A N     1 
ATOM   415  C CA    . ALA A 1 71  ? -4.367  -8.270  -25.433 1.00 25.57  ? 52  ALA A CA    1 
ATOM   416  C C     . ALA A 1 71  ? -4.281  -7.664  -24.028 1.00 24.66  ? 52  ALA A C     1 
ATOM   417  O O     . ALA A 1 71  ? -3.567  -8.165  -23.159 1.00 24.58  ? 52  ALA A O     1 
ATOM   418  C CB    . ALA A 1 71  ? -3.348  -7.634  -26.359 1.00 29.15  ? 52  ALA A CB    1 
ATOM   419  N N     . LEU A 1 72  ? -4.948  -6.520  -23.822 1.00 22.42  ? 53  LEU A N     1 
ATOM   420  C CA    . LEU A 1 72  ? -4.900  -5.852  -22.546 1.00 22.19  ? 53  LEU A CA    1 
ATOM   421  C C     . LEU A 1 72  ? -5.727  -6.598  -21.516 1.00 21.78  ? 53  LEU A C     1 
ATOM   422  O O     . LEU A 1 72  ? -5.419  -6.590  -20.321 1.00 23.67  ? 53  LEU A O     1 
ATOM   423  C CB    . LEU A 1 72  ? -5.393  -4.418  -22.753 1.00 21.99  ? 53  LEU A CB    1 
ATOM   424  C CG    . LEU A 1 72  ? -4.478  -3.601  -23.653 1.00 23.92  ? 53  LEU A CG    1 
ATOM   425  C CD1   . LEU A 1 72  ? -5.049  -2.188  -23.855 1.00 28.08  ? 53  LEU A CD1   1 
ATOM   426  C CD2   . LEU A 1 72  ? -3.063  -3.519  -23.104 1.00 25.69  ? 53  LEU A CD2   1 
ATOM   427  N N     . LEU A 1 73  ? -6.856  -7.137  -21.967 1.00 22.20  ? 54  LEU A N     1 
ATOM   428  C CA    . LEU A 1 73  ? -7.670  -7.969  -21.099 1.00 24.01  ? 54  LEU A CA    1 
ATOM   429  C C     . LEU A 1 73  ? -6.890  -9.235  -20.703 1.00 24.89  ? 54  LEU A C     1 
ATOM   430  O O     . LEU A 1 73  ? -6.893  -9.619  -19.526 1.00 23.24  ? 54  LEU A O     1 
ATOM   431  C CB    . LEU A 1 73  ? -8.948  -8.272  -21.869 1.00 24.11  ? 54  LEU A CB    1 
ATOM   432  C CG    . LEU A 1 73  ? -10.185 -7.420  -21.631 1.00 34.22  ? 54  LEU A CG    1 
ATOM   433  C CD1   . LEU A 1 73  ? -9.904  -6.002  -21.291 1.00 34.40  ? 54  LEU A CD1   1 
ATOM   434  C CD2   . LEU A 1 73  ? -11.122 -7.535  -22.814 1.00 32.14  ? 54  LEU A CD2   1 
ATOM   435  N N     . GLU A 1 74  ? -6.194  -9.839  -21.653 1.00 25.76  ? 55  GLU A N     1 
ATOM   436  C CA    . GLU A 1 74  ? -5.492  -11.093 -21.403 1.00 26.38  ? 55  GLU A CA    1 
ATOM   437  C C     . GLU A 1 74  ? -4.408  -10.920 -20.350 1.00 27.20  ? 55  GLU A C     1 
ATOM   438  O O     . GLU A 1 74  ? -4.149  -11.832 -19.550 1.00 28.48  ? 55  GLU A O     1 
ATOM   439  C CB    . GLU A 1 74  ? -4.842  -11.594 -22.696 1.00 28.95  ? 55  GLU A CB    1 
ATOM   440  C CG    . GLU A 1 74  ? -4.491  -13.065 -22.672 1.00 35.90  ? 55  GLU A CG    1 
ATOM   441  C CD    . GLU A 1 74  ? -5.703  -13.993 -22.722 1.00 41.33  ? 55  GLU A CD    1 
ATOM   442  O OE1   . GLU A 1 74  ? -6.255  -14.235 -23.832 1.00 44.92  ? 55  GLU A OE1   1 
ATOM   443  O OE2   . GLU A 1 74  ? -6.107  -14.463 -21.649 1.00 49.58  ? 55  GLU A OE2   1 
ATOM   444  N N     . GLN A 1 75  ? -3.731  -9.765  -20.332 1.00 24.97  ? 56  GLN A N     1 
ATOM   445  C CA    . GLN A 1 75  ? -2.634  -9.606  -19.398 1.00 24.97  ? 56  GLN A CA    1 
ATOM   446  C C     . GLN A 1 75  ? -3.146  -9.346  -17.975 1.00 24.56  ? 56  GLN A C     1 
ATOM   447  O O     . GLN A 1 75  ? -2.350  -9.261  -17.039 1.00 25.45  ? 56  GLN A O     1 
ATOM   448  C CB    . GLN A 1 75  ? -1.654  -8.575  -19.966 1.00 27.15  ? 56  GLN A CB    1 
ATOM   449  C CG    . GLN A 1 75  ? -2.074  -7.141  -19.815 1.00 26.02  ? 56  GLN A CG    1 
ATOM   450  C CD    . GLN A 1 75  ? -1.025  -6.186  -20.327 1.00 28.14  ? 56  GLN A CD    1 
ATOM   451  O OE1   . GLN A 1 75  ? -0.015  -6.580  -20.899 1.00 29.35  ? 56  GLN A OE1   1 
ATOM   452  N NE2   . GLN A 1 75  ? -1.307  -4.900  -20.182 1.00 28.43  ? 56  GLN A NE2   1 
ATOM   453  N N     . ARG A 1 76  ? -4.472  -9.264  -17.793 1.00 24.82  ? 57  ARG A N     1 
ATOM   454  C CA    . ARG A 1 76  ? -5.079  -9.185  -16.475 1.00 25.40  ? 57  ARG A CA    1 
ATOM   455  C C     . ARG A 1 76  ? -6.013  -10.365 -16.202 1.00 26.13  ? 57  ARG A C     1 
ATOM   456  O O     . ARG A 1 76  ? -6.731  -10.340 -15.202 1.00 28.76  ? 57  ARG A O     1 
ATOM   457  C CB    . ARG A 1 76  ? -5.882  -7.881  -16.329 1.00 25.94  ? 57  ARG A CB    1 
ATOM   458  C CG    . ARG A 1 76  ? -5.029  -6.638  -16.537 1.00 26.09  ? 57  ARG A CG    1 
ATOM   459  C CD    . ARG A 1 76  ? -3.900  -6.493  -15.542 1.00 28.35  ? 57  ARG A CD    1 
ATOM   460  N NE    . ARG A 1 76  ? -3.141  -5.283  -15.854 1.00 27.05  ? 57  ARG A NE    1 
ATOM   461  C CZ    . ARG A 1 76  ? -1.818  -5.226  -15.966 1.00 29.66  ? 57  ARG A CZ    1 
ATOM   462  N NH1   . ARG A 1 76  ? -1.076  -6.322  -15.901 1.00 28.31  ? 57  ARG A NH1   1 
ATOM   463  N NH2   . ARG A 1 76  ? -1.233  -4.053  -16.158 1.00 27.67  ? 57  ARG A NH2   1 
ATOM   464  N N     . GLY A 1 77  ? -6.047  -11.347 -17.101 1.00 26.11  ? 58  GLY A N     1 
ATOM   465  C CA    . GLY A 1 77  ? -6.907  -12.521 -16.977 1.00 27.68  ? 58  GLY A CA    1 
ATOM   466  C C     . GLY A 1 77  ? -8.395  -12.195 -17.108 1.00 27.33  ? 58  GLY A C     1 
ATOM   467  O O     . GLY A 1 77  ? -9.221  -12.862 -16.493 1.00 30.25  ? 58  GLY A O     1 
ATOM   468  N N     . LEU A 1 78  ? -8.747  -11.157 -17.865 1.00 24.34  ? 59  LEU A N     1 
ATOM   469  C CA    . LEU A 1 78  ? -10.138 -10.729 -18.025 1.00 26.24  ? 59  LEU A CA    1 
ATOM   470  C C     . LEU A 1 78  ? -10.729 -11.211 -19.351 1.00 26.31  ? 59  LEU A C     1 
ATOM   471  O O     . LEU A 1 78  ? -11.923 -11.034 -19.628 1.00 25.77  ? 59  LEU A O     1 
ATOM   472  C CB    . LEU A 1 78  ? -10.161 -9.196  -17.981 1.00 27.21  ? 59  LEU A CB    1 
ATOM   473  C CG    . LEU A 1 78  ? -9.841  -8.563  -16.625 1.00 30.72  ? 59  LEU A CG    1 
ATOM   474  C CD1   . LEU A 1 78  ? -9.533  -7.076  -16.779 1.00 29.88  ? 59  LEU A CD1   1 
ATOM   475  C CD2   . LEU A 1 78  ? -10.997 -8.758  -15.669 1.00 38.19  ? 59  LEU A CD2   1 
ATOM   476  N N     . ALA A 1 79  ? -9.887  -11.733 -20.243 1.00 25.98  ? 60  ALA A N     1 
ATOM   477  C CA    . ALA A 1 79  ? -10.311 -12.085 -21.596 1.00 28.51  ? 60  ALA A CA    1 
ATOM   478  C C     . ALA A 1 79  ? -11.278 -13.292 -21.604 1.00 30.75  ? 60  ALA A C     1 
ATOM   479  O O     . ALA A 1 79  ? -12.273 -13.258 -22.330 1.00 27.81  ? 60  ALA A O     1 
ATOM   480  C CB    . ALA A 1 79  ? -9.130  -12.291 -22.488 1.00 27.76  ? 60  ALA A CB    1 
ATOM   481  N N     . ASP A 1 80  ? -11.064 -14.285 -20.740 1.00 28.78  ? 61  ASP A N     1 
ATOM   482  C CA    . ASP A 1 80  ? -11.943 -15.459 -20.673 1.00 31.39  ? 61  ASP A CA    1 
ATOM   483  C C     . ASP A 1 80  ? -13.387 -15.062 -20.336 1.00 30.97  ? 61  ASP A C     1 
ATOM   484  O O     . ASP A 1 80  ? -14.304 -15.512 -21.003 1.00 31.94  ? 61  ASP A O     1 
ATOM   485  C CB    . ASP A 1 80  ? -11.446 -16.498 -19.680 1.00 32.83  ? 61  ASP A CB    1 
ATOM   486  C CG    . ASP A 1 80  ? -10.235 -17.307 -20.140 1.00 38.93  ? 61  ASP A CG    1 
ATOM   487  O OD1   . ASP A 1 80  ? -9.893  -17.316 -21.365 1.00 40.80  ? 61  ASP A OD1   1 
ATOM   488  O OD2   . ASP A 1 80  ? -9.628  -17.926 -19.263 1.00 48.17  ? 61  ASP A OD2   1 
ATOM   489  N N     . ALA A 1 81  ? -13.590 -14.172 -19.365 1.00 30.96  ? 62  ALA A N     1 
ATOM   490  C CA    . ALA A 1 81  ? -14.926 -13.720 -19.009 1.00 32.40  ? 62  ALA A CA    1 
ATOM   491  C C     . ALA A 1 81  ? -15.610 -13.037 -20.191 1.00 33.83  ? 62  ALA A C     1 
ATOM   492  O O     . ALA A 1 81  ? -16.829 -13.104 -20.334 1.00 31.46  ? 62  ALA A O     1 
ATOM   493  C CB    . ALA A 1 81  ? -14.891 -12.811 -17.806 1.00 30.81  ? 62  ALA A CB    1 
ATOM   494  N N     . LEU A 1 82  ? -14.866 -12.268 -20.993 1.00 31.18  ? 63  LEU A N     1 
ATOM   495  C CA    . LEU A 1 82  ? -15.488 -11.596 -22.138 1.00 30.60  ? 63  LEU A CA    1 
ATOM   496  C C     . LEU A 1 82  ? -15.836 -12.611 -23.228 1.00 27.91  ? 63  LEU A C     1 
ATOM   497  O O     . LEU A 1 82  ? -16.900 -12.521 -23.840 1.00 29.61  ? 63  LEU A O     1 
ATOM   498  C CB    . LEU A 1 82  ? -14.537 -10.543 -22.698 1.00 31.15  ? 63  LEU A CB    1 
ATOM   499  C CG    . LEU A 1 82  ? -15.081 -9.174  -23.121 1.00 36.24  ? 63  LEU A CG    1 
ATOM   500  C CD1   . LEU A 1 82  ? -14.364 -8.712  -24.360 1.00 31.95  ? 63  LEU A CD1   1 
ATOM   501  C CD2   . LEU A 1 82  ? -16.599 -9.004  -23.230 1.00 31.08  ? 63  LEU A CD2   1 
ATOM   502  N N     . ARG A 1 83  ? -14.922 -13.573 -23.456 1.00 28.40  ? 64  ARG A N     1 
ATOM   503  C CA    . ARG A 1 83  ? -15.049 -14.564 -24.518 1.00 28.18  ? 64  ARG A CA    1 
ATOM   504  C C     . ARG A 1 83  ? -16.298 -15.429 -24.319 1.00 29.21  ? 64  ARG A C     1 
ATOM   505  O O     . ARG A 1 83  ? -16.876 -15.872 -25.304 1.00 32.43  ? 64  ARG A O     1 
ATOM   506  C CB    . ARG A 1 83  ? -13.796 -15.433 -24.612 1.00 29.20  ? 64  ARG A CB    1 
ATOM   507  C CG    . ARG A 1 83  ? -12.696 -14.763 -25.421 1.00 30.27  ? 64  ARG A CG    1 
ATOM   508  C CD    . ARG A 1 83  ? -11.575 -15.687 -25.861 1.00 37.56  ? 64  ARG A CD    1 
ATOM   509  N NE    . ARG A 1 83  ? -10.667 -15.931 -24.782 1.00 38.58  ? 64  ARG A NE    1 
ATOM   510  C CZ    . ARG A 1 83  ? -9.447  -15.397 -24.660 1.00 40.54  ? 64  ARG A CZ    1 
ATOM   511  N NH1   . ARG A 1 83  ? -8.978  -14.545 -25.551 1.00 36.22  ? 64  ARG A NH1   1 
ATOM   512  N NH2   . ARG A 1 83  ? -8.697  -15.722 -23.627 1.00 41.66  ? 64  ARG A NH2   1 
ATOM   513  N N     . ALA A 1 84  ? -16.715 -15.597 -23.062 1.00 31.32  ? 65  ALA A N     1 
ATOM   514  C CA    . ALA A 1 84  ? -17.919 -16.344 -22.742 1.00 31.41  ? 65  ALA A CA    1 
ATOM   515  C C     . ALA A 1 84  ? -19.139 -15.719 -23.427 1.00 34.99  ? 65  ALA A C     1 
ATOM   516  O O     . ALA A 1 84  ? -20.105 -16.435 -23.677 1.00 35.45  ? 65  ALA A O     1 
ATOM   517  C CB    . ALA A 1 84  ? -18.089 -16.391 -21.249 1.00 31.91  ? 65  ALA A CB    1 
ATOM   518  N N     . SER A 1 85  ? -19.109 -14.409 -23.741 1.00 30.28  ? 66  SER A N     1 
ATOM   519  C CA    . SER A 1 85  ? -20.271 -13.731 -24.328 1.00 30.48  ? 66  SER A CA    1 
ATOM   520  C C     . SER A 1 85  ? -20.074 -13.414 -25.819 1.00 32.63  ? 66  SER A C     1 
ATOM   521  O O     . SER A 1 85  ? -20.901 -12.714 -26.432 1.00 33.35  ? 66  SER A O     1 
ATOM   522  C CB    . SER A 1 85  ? -20.563 -12.446 -23.599 1.00 33.25  ? 66  SER A CB    1 
ATOM   523  O OG    . SER A 1 85  ? -20.789 -12.660 -22.212 1.00 33.69  ? 66  SER A OG    1 
ATOM   524  N N     . GLY A 1 86  ? -18.940 -13.865 -26.378 1.00 30.07  ? 67  GLY A N     1 
ATOM   525  C CA    . GLY A 1 86  ? -18.505 -13.441 -27.696 1.00 28.31  ? 67  GLY A CA    1 
ATOM   526  C C     . GLY A 1 86  ? -18.387 -14.552 -28.744 1.00 28.91  ? 67  GLY A C     1 
ATOM   527  O O     . GLY A 1 86  ? -18.293 -15.749 -28.426 1.00 31.28  ? 67  GLY A O     1 
ATOM   528  N N     . LEU A 1 87  ? -18.364 -14.096 -30.004 1.00 27.97  ? 68  LEU A N     1 
ATOM   529  C CA    . LEU A 1 87  ? -18.079 -14.895 -31.191 1.00 30.16  ? 68  LEU A CA    1 
ATOM   530  C C     . LEU A 1 87  ? -16.704 -14.489 -31.744 1.00 29.82  ? 68  LEU A C     1 
ATOM   531  O O     . LEU A 1 87  ? -16.375 -13.290 -31.779 1.00 28.31  ? 68  LEU A O     1 
ATOM   532  C CB    . LEU A 1 87  ? -19.218 -14.650 -32.188 1.00 29.54  ? 68  LEU A CB    1 
ATOM   533  C CG    . LEU A 1 87  ? -19.047 -15.261 -33.571 1.00 33.14  ? 68  LEU A CG    1 
ATOM   534  C CD1   . LEU A 1 87  ? -19.252 -16.773 -33.533 1.00 37.41  ? 68  LEU A CD1   1 
ATOM   535  C CD2   . LEU A 1 87  ? -19.984 -14.587 -34.560 1.00 37.17  ? 68  LEU A CD2   1 
ATOM   536  N N     . PRO A 1 88  ? -15.804 -15.435 -32.121 1.00 31.74  ? 69  PRO A N     1 
ATOM   537  C CA    . PRO A 1 88  ? -14.542 -15.071 -32.756 1.00 33.43  ? 69  PRO A CA    1 
ATOM   538  C C     . PRO A 1 88  ? -14.889 -14.305 -34.023 1.00 36.22  ? 69  PRO A C     1 
ATOM   539  O O     . PRO A 1 88  ? -15.802 -14.683 -34.743 1.00 37.53  ? 69  PRO A O     1 
ATOM   540  C CB    . PRO A 1 88  ? -13.825 -16.388 -33.086 1.00 35.95  ? 69  PRO A CB    1 
ATOM   541  C CG    . PRO A 1 88  ? -14.506 -17.389 -32.213 1.00 35.01  ? 69  PRO A CG    1 
ATOM   542  C CD    . PRO A 1 88  ? -15.933 -16.896 -32.021 1.00 34.61  ? 69  PRO A CD    1 
ATOM   543  N N     . LEU A 1 89  ? -14.206 -13.177 -34.210 1.00 38.64  ? 70  LEU A N     1 
ATOM   544  C CA    . LEU A 1 89  ? -14.325 -12.356 -35.396 1.00 42.78  ? 70  LEU A CA    1 
ATOM   545  C C     . LEU A 1 89  ? -12.960 -12.326 -36.071 1.00 42.97  ? 70  LEU A C     1 
ATOM   546  O O     . LEU A 1 89  ? -12.221 -11.353 -35.899 1.00 44.78  ? 70  LEU A O     1 
ATOM   547  C CB    . LEU A 1 89  ? -14.726 -10.970 -34.900 1.00 47.27  ? 70  LEU A CB    1 
ATOM   548  C CG    . LEU A 1 89  ? -15.351 -10.051 -35.938 1.00 58.08  ? 70  LEU A CG    1 
ATOM   549  C CD1   . LEU A 1 89  ? -16.498 -10.763 -36.669 1.00 57.30  ? 70  LEU A CD1   1 
ATOM   550  C CD2   . LEU A 1 89  ? -15.827 -8.776  -35.245 1.00 54.79  ? 70  LEU A CD2   1 
ATOM   551  N N     . PRO A 1 90  ? -12.502 -13.427 -36.709 1.00 48.30  ? 71  PRO A N     1 
ATOM   552  C CA    . PRO A 1 90  ? -11.127 -13.480 -37.218 1.00 58.09  ? 71  PRO A CA    1 
ATOM   553  C C     . PRO A 1 90  ? -10.846 -12.582 -38.434 1.00 54.07  ? 71  PRO A C     1 
ATOM   554  O O     . PRO A 1 90  ? -9.686  -12.219 -38.616 1.00 52.02  ? 71  PRO A O     1 
ATOM   555  C CB    . PRO A 1 90  ? -10.885 -14.970 -37.536 1.00 59.05  ? 71  PRO A CB    1 
ATOM   556  C CG    . PRO A 1 90  ? -12.275 -15.576 -37.694 1.00 59.74  ? 71  PRO A CG    1 
ATOM   557  C CD    . PRO A 1 90  ? -13.232 -14.693 -36.915 1.00 59.90  ? 71  PRO A CD    1 
ATOM   558  N N     . GLY A 1 91  ? -11.895 -12.201 -39.211 1.00 49.19  ? 72  GLY A N     1 
ATOM   559  C CA    . GLY A 1 91  ? -11.768 -11.336 -40.388 1.00 41.51  ? 72  GLY A CA    1 
ATOM   560  C C     . GLY A 1 91  ? -11.294 -9.930  -40.014 1.00 39.83  ? 72  GLY A C     1 
ATOM   561  O O     . GLY A 1 91  ? -11.443 -9.535  -38.874 1.00 36.34  ? 72  GLY A O     1 
ATOM   562  N N     . ALA A 1 92  ? -10.758 -9.167  -40.986 1.00 33.05  ? 73  ALA A N     1 
ATOM   563  C CA    . ALA A 1 92  ? -10.349 -7.789  -40.738 1.00 31.05  ? 73  ALA A CA    1 
ATOM   564  C C     . ALA A 1 92  ? -10.611 -6.981  -42.003 1.00 27.61  ? 73  ALA A C     1 
ATOM   565  O O     . ALA A 1 92  ? -10.483 -7.512  -43.102 1.00 29.08  ? 73  ALA A O     1 
ATOM   566  C CB    . ALA A 1 92  ? -8.884  -7.763  -40.354 1.00 30.60  ? 73  ALA A CB    1 
ATOM   567  N N     . HIS A 1 93  ? -11.000 -5.702  -41.858 1.00 28.07  ? 74  HIS A N     1 
ATOM   568  C CA    . HIS A 1 93  ? -11.231 -4.876  -43.023 1.00 26.27  ? 74  HIS A CA    1 
ATOM   569  C C     . HIS A 1 93  ? -10.623 -3.495  -42.809 1.00 26.25  ? 74  HIS A C     1 
ATOM   570  O O     . HIS A 1 93  ? -10.417 -3.057  -41.673 1.00 26.19  ? 74  HIS A O     1 
ATOM   571  C CB    . HIS A 1 93  ? -12.727 -4.717  -43.294 1.00 30.74  ? 74  HIS A CB    1 
ATOM   572  C CG    . HIS A 1 93  ? -13.435 -3.847  -42.305 1.00 31.79  ? 74  HIS A CG    1 
ATOM   573  N ND1   . HIS A 1 93  ? -13.470 -2.462  -42.376 1.00 31.13  ? 74  HIS A ND1   1 
ATOM   574  C CD2   . HIS A 1 93  ? -14.208 -4.196  -41.258 1.00 31.88  ? 74  HIS A CD2   1 
ATOM   575  C CE1   . HIS A 1 93  ? -14.219 -1.998  -41.373 1.00 33.38  ? 74  HIS A CE1   1 
ATOM   576  N NE2   . HIS A 1 93  ? -14.683 -3.032  -40.670 1.00 33.34  ? 74  HIS A NE2   1 
ATOM   577  N N     . PHE A 1 94  ? -10.431 -2.818  -43.927 1.00 24.73  ? 75  PHE A N     1 
ATOM   578  C CA    . PHE A 1 94  ? -10.065 -1.413  -43.949 1.00 24.58  ? 75  PHE A CA    1 
ATOM   579  C C     . PHE A 1 94  ? -10.993 -0.701  -44.920 1.00 27.23  ? 75  PHE A C     1 
ATOM   580  O O     . PHE A 1 94  ? -11.063 -1.049  -46.094 1.00 25.80  ? 75  PHE A O     1 
ATOM   581  C CB    . PHE A 1 94  ? -8.592  -1.283  -44.315 1.00 24.19  ? 75  PHE A CB    1 
ATOM   582  C CG    . PHE A 1 94  ? -8.088  0.136   -44.352 1.00 23.18  ? 75  PHE A CG    1 
ATOM   583  C CD1   . PHE A 1 94  ? -8.192  0.878   -45.507 1.00 25.95  ? 75  PHE A CD1   1 
ATOM   584  C CD2   . PHE A 1 94  ? -7.564  0.736   -43.221 1.00 25.26  ? 75  PHE A CD2   1 
ATOM   585  C CE1   . PHE A 1 94  ? -7.708  2.176   -45.555 1.00 22.55  ? 75  PHE A CE1   1 
ATOM   586  C CE2   . PHE A 1 94  ? -7.113  2.053   -43.264 1.00 24.11  ? 75  PHE A CE2   1 
ATOM   587  C CZ    . PHE A 1 94  ? -7.160  2.746   -44.444 1.00 24.50  ? 75  PHE A CZ    1 
ATOM   588  N N     . SER A 1 95  ? -11.753 0.279   -44.415 1.00 26.52  ? 76  SER A N     1 
ATOM   589  C CA    . SER A 1 95  ? -12.773 0.920   -45.226 1.00 25.72  ? 76  SER A CA    1 
ATOM   590  C C     . SER A 1 95  ? -13.745 -0.102  -45.810 1.00 24.58  ? 76  SER A C     1 
ATOM   591  O O     . SER A 1 95  ? -14.237 0.071   -46.921 1.00 27.49  ? 76  SER A O     1 
ATOM   592  C CB    . SER A 1 95  ? -12.172 1.762   -46.313 1.00 28.56  ? 76  SER A CB    1 
ATOM   593  O OG    . SER A 1 95  ? -13.123 2.701   -46.772 1.00 28.35  ? 76  SER A OG    1 
ATOM   594  N N     . LEU A 1 96  ? -14.007 -1.147  -45.052 1.00 25.90  ? 77  LEU A N     1 
ATOM   595  C CA    . LEU A 1 96  ? -14.855 -2.272  -45.444 1.00 27.51  ? 77  LEU A CA    1 
ATOM   596  C C     . LEU A 1 96  ? -14.347 -2.985  -46.707 1.00 28.08  ? 77  LEU A C     1 
ATOM   597  O O     . LEU A 1 96  ? -15.139 -3.607  -47.408 1.00 31.49  ? 77  LEU A O     1 
ATOM   598  C CB    . LEU A 1 96  ? -16.296 -1.776  -45.659 1.00 29.01  ? 77  LEU A CB    1 
ATOM   599  C CG    . LEU A 1 96  ? -17.330 -1.940  -44.538 1.00 37.96  ? 77  LEU A CG    1 
ATOM   600  C CD1   . LEU A 1 96  ? -16.862 -2.725  -43.335 1.00 38.20  ? 77  LEU A CD1   1 
ATOM   601  C CD2   . LEU A 1 96  ? -17.933 -0.619  -44.126 1.00 40.10  ? 77  LEU A CD2   1 
ATOM   602  N N     . LEU A 1 97  ? -13.058 -2.846  -47.038 1.00 29.39  ? 78  LEU A N     1 
ATOM   603  C CA    . LEU A 1 97  ? -12.381 -3.748  -47.971 1.00 29.61  ? 78  LEU A CA    1 
ATOM   604  C C     . LEU A 1 97  ? -11.823 -4.903  -47.143 1.00 28.67  ? 78  LEU A C     1 
ATOM   605  O O     . LEU A 1 97  ? -11.069 -4.688  -46.208 1.00 30.39  ? 78  LEU A O     1 
ATOM   606  C CB    . LEU A 1 97  ? -11.224 -3.019  -48.669 1.00 27.75  ? 78  LEU A CB    1 
ATOM   607  C CG    . LEU A 1 97  ? -11.593 -1.799  -49.512 1.00 28.05  ? 78  LEU A CG    1 
ATOM   608  C CD1   . LEU A 1 97  ? -10.369 -0.991  -49.859 1.00 28.05  ? 78  LEU A CD1   1 
ATOM   609  C CD2   . LEU A 1 97  ? -12.342 -2.191  -50.773 1.00 32.91  ? 78  LEU A CD2   1 
ATOM   610  N N     . TRP A 1 98  ? -12.154 -6.135  -47.497 1.00 29.13  ? 79  TRP A N     1 
ATOM   611  C CA    . TRP A 1 98  ? -11.748 -7.271  -46.676 1.00 29.00  ? 79  TRP A CA    1 
ATOM   612  C C     . TRP A 1 98  ? -10.261 -7.576  -46.877 1.00 27.46  ? 79  TRP A C     1 
ATOM   613  O O     . TRP A 1 98  ? -9.786  -7.540  -47.985 1.00 28.27  ? 79  TRP A O     1 
ATOM   614  C CB    . TRP A 1 98  ? -12.697 -8.457  -46.939 1.00 34.36  ? 79  TRP A CB    1 
ATOM   615  C CG    . TRP A 1 98  ? -14.017 -8.057  -46.373 1.00 39.16  ? 79  TRP A CG    1 
ATOM   616  C CD1   . TRP A 1 98  ? -15.054 -7.499  -47.060 1.00 41.28  ? 79  TRP A CD1   1 
ATOM   617  C CD2   . TRP A 1 98  ? -14.354 -7.963  -44.968 1.00 41.88  ? 79  TRP A CD2   1 
ATOM   618  N NE1   . TRP A 1 98  ? -16.025 -7.097  -46.184 1.00 44.74  ? 79  TRP A NE1   1 
ATOM   619  C CE2   . TRP A 1 98  ? -15.633 -7.374  -44.899 1.00 43.70  ? 79  TRP A CE2   1 
ATOM   620  C CE3   . TRP A 1 98  ? -13.708 -8.321  -43.777 1.00 42.91  ? 79  TRP A CE3   1 
ATOM   621  C CZ2   . TRP A 1 98  ? -16.282 -7.150  -43.688 1.00 41.55  ? 79  TRP A CZ2   1 
ATOM   622  C CZ3   . TRP A 1 98  ? -14.348 -8.105  -42.577 1.00 45.46  ? 79  TRP A CZ3   1 
ATOM   623  C CH2   . TRP A 1 98  ? -15.622 -7.524  -42.539 1.00 45.54  ? 79  TRP A CH2   1 
ATOM   624  N N     . LEU A 1 99  ? -9.544  -7.858  -45.777 1.00 26.73  ? 80  LEU A N     1 
ATOM   625  C CA    . LEU A 1 99  ? -8.110  -8.074  -45.765 1.00 26.27  ? 80  LEU A CA    1 
ATOM   626  C C     . LEU A 1 99  ? -7.885  -9.557  -45.572 1.00 27.54  ? 80  LEU A C     1 
ATOM   627  O O     . LEU A 1 99  ? -8.851  -10.323 -45.488 1.00 27.61  ? 80  LEU A O     1 
ATOM   628  C CB    . LEU A 1 99  ? -7.462  -7.253  -44.644 1.00 27.63  ? 80  LEU A CB    1 
ATOM   629  C CG    . LEU A 1 99  ? -7.735  -5.748  -44.694 1.00 27.14  ? 80  LEU A CG    1 
ATOM   630  C CD1   . LEU A 1 99  ? -7.222  -5.070  -43.435 1.00 26.32  ? 80  LEU A CD1   1 
ATOM   631  C CD2   . LEU A 1 99  ? -7.097  -5.107  -45.898 1.00 29.18  ? 80  LEU A CD2   1 
ATOM   632  N N     . ARG A 1 100 ? -6.615  -9.925  -45.479 1.00 26.03  ? 81  ARG A N     1 
ATOM   633  C CA    . ARG A 1 100 ? -6.220  -11.333 -45.342 1.00 26.82  ? 81  ARG A CA    1 
ATOM   634  C C     . ARG A 1 100 ? -5.414  -11.553 -44.068 1.00 26.03  ? 81  ARG A C     1 
ATOM   635  O O     . ARG A 1 100 ? -4.207  -11.778 -44.120 1.00 28.10  ? 81  ARG A O     1 
ATOM   636  C CB    . ARG A 1 100 ? -5.418  -11.757 -46.575 1.00 30.30  ? 81  ARG A CB    1 
ATOM   637  C CG    . ARG A 1 100 ? -6.144  -11.612 -47.901 1.00 32.15  ? 81  ARG A CG    1 
ATOM   638  C CD    . ARG A 1 100 ? -5.383  -12.138 -49.101 1.00 31.52  ? 81  ARG A CD    1 
ATOM   639  N NE    . ARG A 1 100 ? -4.023  -11.627 -49.266 1.00 35.14  ? 81  ARG A NE    1 
ATOM   640  C CZ    . ARG A 1 100 ? -3.734  -10.387 -49.614 1.00 32.54  ? 81  ARG A CZ    1 
ATOM   641  N NH1   . ARG A 1 100 ? -2.490  -9.967  -49.588 1.00 33.81  ? 81  ARG A NH1   1 
ATOM   642  N NH2   . ARG A 1 100 ? -4.707  -9.559  -49.922 1.00 34.48  ? 81  ARG A NH2   1 
ATOM   643  N N     . PRO A 1 101 ? -6.038  -11.507 -42.862 1.00 29.00  ? 82  PRO A N     1 
ATOM   644  C CA    . PRO A 1 101 ? -5.294  -11.626 -41.605 1.00 30.69  ? 82  PRO A CA    1 
ATOM   645  C C     . PRO A 1 101 ? -4.650  -13.016 -41.468 1.00 31.47  ? 82  PRO A C     1 
ATOM   646  O O     . PRO A 1 101 ? -3.595  -13.131 -40.860 1.00 29.50  ? 82  PRO A O     1 
ATOM   647  C CB    . PRO A 1 101 ? -6.351  -11.342 -40.530 1.00 32.38  ? 82  PRO A CB    1 
ATOM   648  C CG    . PRO A 1 101 ? -7.653  -11.727 -41.166 1.00 32.95  ? 82  PRO A CG    1 
ATOM   649  C CD    . PRO A 1 101 ? -7.493  -11.391 -42.644 1.00 31.11  ? 82  PRO A CD    1 
ATOM   650  N N     . GLU A 1 102 ? -5.232  -14.019 -42.138 1.00 33.38  ? 83  GLU A N     1 
ATOM   651  C CA    . GLU A 1 102 ? -4.710  -15.382 -42.118 1.00 35.61  ? 83  GLU A CA    1 
ATOM   652  C C     . GLU A 1 102 ? -3.289  -15.469 -42.672 1.00 36.88  ? 83  GLU A C     1 
ATOM   653  O O     . GLU A 1 102 ? -2.569  -16.413 -42.355 1.00 35.41  ? 83  GLU A O     1 
ATOM   654  C CB    . GLU A 1 102 ? -5.623  -16.339 -42.889 1.00 39.00  ? 83  GLU A CB    1 
ATOM   655  C CG    . GLU A 1 102 ? -5.756  -16.038 -44.382 1.00 44.77  ? 83  GLU A CG    1 
ATOM   656  C CD    . GLU A 1 102 ? -6.858  -15.076 -44.833 1.00 50.72  ? 83  GLU A CD    1 
ATOM   657  O OE1   . GLU A 1 102 ? -7.379  -14.269 -44.009 1.00 40.43  ? 83  GLU A OE1   1 
ATOM   658  O OE2   . GLU A 1 102 ? -7.224  -15.158 -46.026 1.00 59.91  ? 83  GLU A OE2   1 
ATOM   659  N N     . GLU A 1 103 ? -2.881  -14.499 -43.502 1.00 38.44  ? 84  GLU A N     1 
ATOM   660  C CA    . GLU A 1 103 ? -1.545  -14.478 -44.079 1.00 41.91  ? 84  GLU A CA    1 
ATOM   661  C C     . GLU A 1 103 ? -0.483  -14.142 -43.045 1.00 38.13  ? 84  GLU A C     1 
ATOM   662  O O     . GLU A 1 103 ? 0.676   -14.416 -43.315 1.00 39.70  ? 84  GLU A O     1 
ATOM   663  C CB    . GLU A 1 103 ? -1.375  -13.443 -45.197 1.00 42.36  ? 84  GLU A CB    1 
ATOM   664  C CG    . GLU A 1 103 ? -1.817  -13.943 -46.533 1.00 46.18  ? 84  GLU A CG    1 
ATOM   665  C CD    . GLU A 1 103 ? -1.575  -13.059 -47.744 1.00 46.26  ? 84  GLU A CD    1 
ATOM   666  O OE1   . GLU A 1 103 ? -0.935  -11.956 -47.659 1.00 42.36  ? 84  GLU A OE1   1 
ATOM   667  O OE2   . GLU A 1 103 ? -2.040  -13.487 -48.793 1.00 50.39  ? 84  GLU A OE2   1 
ATOM   668  N N     . ILE A 1 104 ? -0.843  -13.519 -41.911 1.00 38.00  ? 85  ILE A N     1 
ATOM   669  C CA    . ILE A 1 104 ? 0.175   -13.170 -40.929 1.00 38.80  ? 85  ILE A CA    1 
ATOM   670  C C     . ILE A 1 104 ? -0.066  -13.823 -39.564 1.00 37.50  ? 85  ILE A C     1 
ATOM   671  O O     . ILE A 1 104 ? 0.757   -13.634 -38.686 1.00 38.88  ? 85  ILE A O     1 
ATOM   672  C CB    . ILE A 1 104 ? 0.309   -11.642 -40.787 1.00 37.67  ? 85  ILE A CB    1 
ATOM   673  C CG1   . ILE A 1 104 ? -0.925  -10.992 -40.163 1.00 36.58  ? 85  ILE A CG1   1 
ATOM   674  C CG2   . ILE A 1 104 ? 0.628   -10.998 -42.134 1.00 43.99  ? 85  ILE A CG2   1 
ATOM   675  C CD1   . ILE A 1 104 ? -0.692  -9.545  -39.782 1.00 37.81  ? 85  ILE A CD1   1 
ATOM   676  N N     . THR A 1 105 ? -1.164  -14.565 -39.353 1.00 38.31  ? 86  THR A N     1 
ATOM   677  C CA    . THR A 1 105 ? -1.447  -15.129 -38.035 1.00 42.72  ? 86  THR A CA    1 
ATOM   678  C C     . THR A 1 105 ? -0.441  -16.207 -37.624 1.00 48.24  ? 86  THR A C     1 
ATOM   679  O O     . THR A 1 105 ? -0.181  -16.379 -36.437 1.00 44.72  ? 86  THR A O     1 
ATOM   680  C CB    . THR A 1 105 ? -2.848  -15.736 -37.925 1.00 46.37  ? 86  THR A CB    1 
ATOM   681  O OG1   . THR A 1 105 ? -2.971  -16.701 -38.964 1.00 47.45  ? 86  THR A OG1   1 
ATOM   682  C CG2   . THR A 1 105 ? -3.960  -14.715 -38.014 1.00 43.51  ? 86  THR A CG2   1 
ATOM   683  N N     . ALA A 1 106 ? 0.144   -16.924 -38.585 1.00 47.78  ? 87  ALA A N     1 
ATOM   684  C CA    . ALA A 1 106 ? 1.276   -17.791 -38.279 1.00 52.81  ? 87  ALA A CA    1 
ATOM   685  C C     . ALA A 1 106 ? 2.382   -16.999 -37.575 1.00 49.98  ? 87  ALA A C     1 
ATOM   686  O O     . ALA A 1 106 ? 2.915   -17.422 -36.558 1.00 52.50  ? 87  ALA A O     1 
ATOM   687  C CB    . ALA A 1 106 ? 1.775   -18.450 -39.545 1.00 53.13  ? 87  ALA A CB    1 
ATOM   688  N N     . ASP A 1 107 ? 2.724   -15.825 -38.097 1.00 52.74  ? 88  ASP A N     1 
ATOM   689  C CA    . ASP A 1 107 ? 3.784   -15.018 -37.512 1.00 53.34  ? 88  ASP A CA    1 
ATOM   690  C C     . ASP A 1 107 ? 3.268   -14.203 -36.315 1.00 53.36  ? 88  ASP A C     1 
ATOM   691  O O     . ASP A 1 107 ? 4.025   -13.880 -35.400 1.00 47.43  ? 88  ASP A O     1 
ATOM   692  C CB    . ASP A 1 107 ? 4.400   -14.118 -38.590 1.00 65.73  ? 88  ASP A CB    1 
ATOM   693  C CG    . ASP A 1 107 ? 5.187   -12.946 -38.030 1.00 69.73  ? 88  ASP A CG    1 
ATOM   694  O OD1   . ASP A 1 107 ? 6.220   -13.196 -37.377 1.00 75.35  ? 88  ASP A OD1   1 
ATOM   695  O OD2   . ASP A 1 107 ? 4.740   -11.799 -38.225 1.00 64.31  ? 88  ASP A OD2   1 
ATOM   696  N N     . ARG A 1 108 ? 1.994   -13.788 -36.335 1.00 48.67  ? 89  ARG A N     1 
ATOM   697  C CA    . ARG A 1 108 ? 1.444   -12.992 -35.245 1.00 48.24  ? 89  ARG A CA    1 
ATOM   698  C C     . ARG A 1 108 ? 0.047   -13.492 -34.876 1.00 42.24  ? 89  ARG A C     1 
ATOM   699  O O     . ARG A 1 108 ? -0.956  -12.899 -35.289 1.00 37.84  ? 89  ARG A O     1 
ATOM   700  C CB    . ARG A 1 108 ? 1.422   -11.519 -35.637 1.00 48.51  ? 89  ARG A CB    1 
ATOM   701  C CG    . ARG A 1 108 ? 2.813   -10.917 -35.722 1.00 56.54  ? 89  ARG A CG    1 
ATOM   702  C CD    . ARG A 1 108 ? 2.759   -9.423  -35.836 1.00 55.64  ? 89  ARG A CD    1 
ATOM   703  N NE    . ARG A 1 108 ? 2.393   -8.742  -34.601 1.00 54.45  ? 89  ARG A NE    1 
ATOM   704  C CZ    . ARG A 1 108 ? 2.543   -7.431  -34.436 1.00 51.13  ? 89  ARG A CZ    1 
ATOM   705  N NH1   . ARG A 1 108 ? 3.119   -6.730  -35.395 1.00 50.47  ? 89  ARG A NH1   1 
ATOM   706  N NH2   . ARG A 1 108 ? 2.147   -6.825  -33.332 1.00 42.51  ? 89  ARG A NH2   1 
ATOM   707  N N     . PRO A 1 109 ? -0.046  -14.578 -34.075 1.00 46.12  ? 90  PRO A N     1 
ATOM   708  C CA    . PRO A 1 109 ? -1.329  -15.166 -33.680 1.00 43.67  ? 90  PRO A CA    1 
ATOM   709  C C     . PRO A 1 109 ? -2.327  -14.179 -33.066 1.00 41.62  ? 90  PRO A C     1 
ATOM   710  O O     . PRO A 1 109 ? -3.519  -14.285 -33.329 1.00 43.58  ? 90  PRO A O     1 
ATOM   711  C CB    . PRO A 1 109 ? -0.949  -16.246 -32.658 1.00 45.93  ? 90  PRO A CB    1 
ATOM   712  C CG    . PRO A 1 109 ? 0.498   -16.566 -32.957 1.00 48.74  ? 90  PRO A CG    1 
ATOM   713  C CD    . PRO A 1 109 ? 1.107   -15.287 -33.488 1.00 49.03  ? 90  PRO A CD    1 
ATOM   714  N N     . GLU A 1 110 ? -1.818  -13.225 -32.277 1.00 39.41  ? 91  GLU A N     1 
ATOM   715  C CA    . GLU A 1 110 ? -2.565  -12.090 -31.724 1.00 41.26  ? 91  GLU A CA    1 
ATOM   716  C C     . GLU A 1 110 ? -3.601  -11.531 -32.699 1.00 36.23  ? 91  GLU A C     1 
ATOM   717  O O     . GLU A 1 110 ? -4.724  -11.174 -32.316 1.00 38.83  ? 91  GLU A O     1 
ATOM   718  C CB    . GLU A 1 110 ? -1.587  -10.984 -31.310 1.00 44.53  ? 91  GLU A CB    1 
ATOM   719  C CG    . GLU A 1 110 ? -0.190  -11.193 -31.918 1.00 53.82  ? 91  GLU A CG    1 
ATOM   720  C CD    . GLU A 1 110 ? 0.768   -10.016 -31.926 1.00 56.49  ? 91  GLU A CD    1 
ATOM   721  O OE1   . GLU A 1 110 ? 1.878   -10.195 -32.453 1.00 61.23  ? 91  GLU A OE1   1 
ATOM   722  O OE2   . GLU A 1 110 ? 0.416   -8.938  -31.396 1.00 66.98  ? 91  GLU A OE2   1 
ATOM   723  N N     . VAL A 1 111 ? -3.236  -11.436 -33.971 1.00 33.49  ? 92  VAL A N     1 
ATOM   724  C CA    . VAL A 1 111 ? -4.055  -10.748 -34.949 1.00 36.28  ? 92  VAL A CA    1 
ATOM   725  C C     . VAL A 1 111 ? -5.409  -11.440 -35.116 1.00 34.86  ? 92  VAL A C     1 
ATOM   726  O O     . VAL A 1 111 ? -6.339  -10.809 -35.575 1.00 33.96  ? 92  VAL A O     1 
ATOM   727  C CB    . VAL A 1 111 ? -3.244  -10.632 -36.255 1.00 42.99  ? 92  VAL A CB    1 
ATOM   728  C CG1   . VAL A 1 111 ? -4.055  -10.856 -37.516 1.00 41.76  ? 92  VAL A CG1   1 
ATOM   729  C CG2   . VAL A 1 111 ? -2.465  -9.326  -36.278 1.00 41.97  ? 92  VAL A CG2   1 
ATOM   730  N N     . GLY A 1 112 ? -5.518  -12.726 -34.746 1.00 33.20  ? 93  GLY A N     1 
ATOM   731  C CA    . GLY A 1 112 ? -6.769  -13.466 -34.903 1.00 32.12  ? 93  GLY A CA    1 
ATOM   732  C C     . GLY A 1 112 ? -7.616  -13.603 -33.637 1.00 34.12  ? 93  GLY A C     1 
ATOM   733  O O     . GLY A 1 112 ? -8.532  -14.441 -33.620 1.00 38.82  ? 93  GLY A O     1 
ATOM   734  N N     . THR A 1 113 ? -7.438  -12.707 -32.643 1.00 30.55  ? 94  THR A N     1 
ATOM   735  C CA    . THR A 1 113 ? -8.099  -12.860 -31.353 1.00 31.19  ? 94  THR A CA    1 
ATOM   736  C C     . THR A 1 113 ? -9.261  -11.885 -31.165 1.00 27.66  ? 94  THR A C     1 
ATOM   737  O O     . THR A 1 113 ? -9.815  -11.851 -30.084 1.00 28.82  ? 94  THR A O     1 
ATOM   738  C CB    . THR A 1 113 ? -7.090  -12.710 -30.207 1.00 32.92  ? 94  THR A CB    1 
ATOM   739  O OG1   . THR A 1 113 ? -6.465  -11.423 -30.351 1.00 31.87  ? 94  THR A OG1   1 
ATOM   740  C CG2   . THR A 1 113 ? -6.078  -13.839 -30.190 1.00 33.11  ? 94  THR A CG2   1 
ATOM   741  N N     . GLY A 1 114 ? -9.675  -11.165 -32.200 1.00 28.01  ? 95  GLY A N     1 
ATOM   742  C CA    . GLY A 1 114 ? -10.762 -10.205 -32.068 1.00 30.23  ? 95  GLY A CA    1 
ATOM   743  C C     . GLY A 1 114 ? -12.106 -10.895 -31.858 1.00 32.07  ? 95  GLY A C     1 
ATOM   744  O O     . GLY A 1 114 ? -12.226 -12.087 -32.178 1.00 27.03  ? 95  GLY A O     1 
ATOM   745  N N     . LEU A 1 115 ? -13.086 -10.144 -31.317 1.00 27.77  ? 96  LEU A N     1 
ATOM   746  C CA    . LEU A 1 115 ? -14.368 -10.700 -30.906 1.00 29.02  ? 96  LEU A CA    1 
ATOM   747  C C     . LEU A 1 115 ? -15.533 -9.827  -31.376 1.00 28.30  ? 96  LEU A C     1 
ATOM   748  O O     . LEU A 1 115 ? -15.428 -8.611  -31.486 1.00 28.33  ? 96  LEU A O     1 
ATOM   749  C CB    . LEU A 1 115 ? -14.433 -10.766 -29.377 1.00 30.89  ? 96  LEU A CB    1 
ATOM   750  C CG    . LEU A 1 115 ? -13.401 -11.625 -28.663 1.00 30.15  ? 96  LEU A CG    1 
ATOM   751  C CD1   . LEU A 1 115 ? -13.543 -11.444 -27.179 1.00 31.40  ? 96  LEU A CD1   1 
ATOM   752  C CD2   . LEU A 1 115 ? -13.570 -13.109 -29.029 1.00 31.49  ? 96  LEU A CD2   1 
ATOM   753  N N     . LEU A 1 116 ? -16.646 -10.497 -31.676 1.00 27.34  ? 97  LEU A N     1 
ATOM   754  C CA    . LEU A 1 116 ? -17.947 -9.843  -31.716 1.00 28.70  ? 97  LEU A CA    1 
ATOM   755  C C     . LEU A 1 116 ? -18.576 -10.075 -30.350 1.00 31.63  ? 97  LEU A C     1 
ATOM   756  O O     . LEU A 1 116 ? -18.838 -11.221 -29.980 1.00 29.95  ? 97  LEU A O     1 
ATOM   757  C CB    . LEU A 1 116 ? -18.783 -10.459 -32.840 1.00 31.08  ? 97  LEU A CB    1 
ATOM   758  C CG    . LEU A 1 116 ? -20.103 -9.763  -33.187 1.00 40.45  ? 97  LEU A CG    1 
ATOM   759  C CD1   . LEU A 1 116 ? -20.936 -9.473  -31.955 1.00 48.95  ? 97  LEU A CD1   1 
ATOM   760  C CD2   . LEU A 1 116 ? -19.852 -8.478  -33.957 1.00 39.31  ? 97  LEU A CD2   1 
ATOM   761  N N     . VAL A 1 117 ? -18.750 -8.990  -29.587 1.00 29.48  ? 98  VAL A N     1 
ATOM   762  C CA    . VAL A 1 117 ? -19.292 -9.084  -28.238 1.00 29.88  ? 98  VAL A CA    1 
ATOM   763  C C     . VAL A 1 117 ? -19.867 -7.727  -27.846 1.00 31.78  ? 98  VAL A C     1 
ATOM   764  O O     . VAL A 1 117 ? -19.276 -6.676  -28.092 1.00 29.74  ? 98  VAL A O     1 
ATOM   765  C CB    . VAL A 1 117 ? -18.238 -9.592  -27.234 1.00 31.75  ? 98  VAL A CB    1 
ATOM   766  C CG1   . VAL A 1 117 ? -17.063 -8.635  -27.131 1.00 30.83  ? 98  VAL A CG1   1 
ATOM   767  C CG2   . VAL A 1 117 ? -18.832 -9.851  -25.859 1.00 30.58  ? 98  VAL A CG2   1 
ATOM   768  N N     . ALA A 1 118 ? -21.045 -7.746  -27.220 1.00 33.76  ? 99  ALA A N     1 
ATOM   769  C CA    . ALA A 1 118 ? -21.746 -6.495  -26.937 1.00 34.65  ? 99  ALA A CA    1 
ATOM   770  C C     . ALA A 1 118 ? -20.969 -5.699  -25.891 1.00 26.60  ? 99  ALA A C     1 
ATOM   771  O O     . ALA A 1 118 ? -20.481 -6.237  -24.901 1.00 28.50  ? 99  ALA A O     1 
ATOM   772  C CB    . ALA A 1 118 ? -23.171 -6.776  -26.504 1.00 36.75  ? 99  ALA A CB    1 
ATOM   773  N N     . GLN A 1 119 ? -20.823 -4.395  -26.152 1.00 29.75  ? 100 GLN A N     1 
ATOM   774  C CA    . GLN A 1 119 ? -20.055 -3.496  -25.295 1.00 27.38  ? 100 GLN A CA    1 
ATOM   775  C C     . GLN A 1 119 ? -20.489 -3.586  -23.831 1.00 26.00  ? 100 GLN A C     1 
ATOM   776  O O     . GLN A 1 119 ? -19.631 -3.572  -22.962 1.00 26.93  ? 100 GLN A O     1 
ATOM   777  C CB    . GLN A 1 119 ? -20.167 -2.057  -25.813 1.00 28.00  ? 100 GLN A CB    1 
ATOM   778  C CG    . GLN A 1 119 ? -19.382 -1.059  -24.982 1.00 26.13  ? 100 GLN A CG    1 
ATOM   779  C CD    . GLN A 1 119 ? -19.348 0.291   -25.634 1.00 26.40  ? 100 GLN A CD    1 
ATOM   780  O OE1   . GLN A 1 119 ? -19.496 0.452   -26.849 1.00 27.75  ? 100 GLN A OE1   1 
ATOM   781  N NE2   . GLN A 1 119 ? -19.151 1.297   -24.799 1.00 27.65  ? 100 GLN A NE2   1 
ATOM   782  N N     . PRO A 1 120 ? -21.793 -3.685  -23.443 1.00 25.19  ? 101 PRO A N     1 
ATOM   783  C CA    . PRO A 1 120 ? -22.130 -3.816  -22.022 1.00 27.91  ? 101 PRO A CA    1 
ATOM   784  C C     . PRO A 1 120 ? -21.517 -5.020  -21.320 1.00 26.80  ? 101 PRO A C     1 
ATOM   785  O O     . PRO A 1 120 ? -21.306 -4.980  -20.111 1.00 29.43  ? 101 PRO A O     1 
ATOM   786  C CB    . PRO A 1 120 ? -23.670 -3.883  -22.014 1.00 29.78  ? 101 PRO A CB    1 
ATOM   787  C CG    . PRO A 1 120 ? -24.071 -3.173  -23.273 1.00 30.60  ? 101 PRO A CG    1 
ATOM   788  C CD    . PRO A 1 120 ? -23.001 -3.567  -24.280 1.00 28.81  ? 101 PRO A CD    1 
ATOM   789  N N     . ARG A 1 121 ? -21.181 -6.059  -22.082 1.00 29.42  ? 102 ARG A N     1 
ATOM   790  C CA    . ARG A 1 121 ? -20.518 -7.236  -21.533 1.00 28.11  ? 102 ARG A CA    1 
ATOM   791  C C     . ARG A 1 121 ? -19.073 -6.907  -21.144 1.00 27.11  ? 102 ARG A C     1 
ATOM   792  O O     . ARG A 1 121 ? -18.606 -7.340  -20.100 1.00 30.33  ? 102 ARG A O     1 
ATOM   793  C CB    . ARG A 1 121 ? -20.504 -8.400  -22.525 1.00 29.19  ? 102 ARG A CB    1 
ATOM   794  C CG    . ARG A 1 121 ? -21.856 -8.842  -23.052 1.00 35.67  ? 102 ARG A CG    1 
ATOM   795  C CD    . ARG A 1 121 ? -22.713 -9.603  -22.049 1.00 37.65  ? 102 ARG A CD    1 
ATOM   796  N NE    . ARG A 1 121 ? -23.485 -8.696  -21.235 1.00 43.50  ? 102 ARG A NE    1 
ATOM   797  C CZ    . ARG A 1 121 ? -24.463 -7.920  -21.694 1.00 44.97  ? 102 ARG A CZ    1 
ATOM   798  N NH1   . ARG A 1 121 ? -24.898 -8.051  -22.938 1.00 44.32  ? 102 ARG A NH1   1 
ATOM   799  N NH2   . ARG A 1 121 ? -25.008 -7.020  -20.899 1.00 39.70  ? 102 ARG A NH2   1 
ATOM   800  N N     . LEU A 1 122 ? -18.384 -6.111  -21.956 1.00 29.79  ? 103 LEU A N     1 
ATOM   801  C CA    . LEU A 1 122 ? -17.043 -5.649  -21.599 1.00 26.82  ? 103 LEU A CA    1 
ATOM   802  C C     . LEU A 1 122 ? -17.110 -4.813  -20.330 1.00 24.72  ? 103 LEU A C     1 
ATOM   803  O O     . LEU A 1 122 ? -16.341 -5.008  -19.403 1.00 26.26  ? 103 LEU A O     1 
ATOM   804  C CB    . LEU A 1 122 ? -16.468 -4.853  -22.775 1.00 30.71  ? 103 LEU A CB    1 
ATOM   805  C CG    . LEU A 1 122 ? -15.203 -4.036  -22.506 1.00 29.80  ? 103 LEU A CG    1 
ATOM   806  C CD1   . LEU A 1 122 ? -14.038 -4.953  -22.149 1.00 30.38  ? 103 LEU A CD1   1 
ATOM   807  C CD2   . LEU A 1 122 ? -14.849 -3.197  -23.725 1.00 30.69  ? 103 LEU A CD2   1 
ATOM   808  N N     . THR A 1 123 ? -18.025 -3.823  -20.314 1.00 27.03  ? 104 THR A N     1 
ATOM   809  C CA    . THR A 1 123 ? -18.162 -2.946  -19.183 1.00 29.12  ? 104 THR A CA    1 
ATOM   810  C C     . THR A 1 123 ? -18.504 -3.745  -17.923 1.00 29.64  ? 104 THR A C     1 
ATOM   811  O O     . THR A 1 123 ? -17.942 -3.460  -16.897 1.00 30.97  ? 104 THR A O     1 
ATOM   812  C CB    . THR A 1 123 ? -19.154 -1.828  -19.520 1.00 29.09  ? 104 THR A CB    1 
ATOM   813  O OG1   . THR A 1 123 ? -18.603 -1.106  -20.625 1.00 30.87  ? 104 THR A OG1   1 
ATOM   814  C CG2   . THR A 1 123 ? -19.382 -0.911  -18.349 1.00 35.89  ? 104 THR A CG2   1 
ATOM   815  N N     . GLU A 1 124 ? -19.360 -4.770  -18.018 1.00 31.54  ? 105 GLU A N     1 
ATOM   816  C CA    . GLU A 1 124 ? -19.699 -5.634  -16.893 1.00 33.04  ? 105 GLU A CA    1 
ATOM   817  C C     . GLU A 1 124 ? -18.473 -6.398  -16.377 1.00 30.05  ? 105 GLU A C     1 
ATOM   818  O O     . GLU A 1 124 ? -18.307 -6.558  -15.176 1.00 30.02  ? 105 GLU A O     1 
ATOM   819  C CB    . GLU A 1 124 ? -20.706 -6.721  -17.293 1.00 38.37  ? 105 GLU A CB    1 
ATOM   820  C CG    . GLU A 1 124 ? -22.161 -6.298  -17.310 1.00 46.80  ? 105 GLU A CG    1 
ATOM   821  C CD    . GLU A 1 124 ? -23.080 -7.188  -18.150 1.00 53.90  ? 105 GLU A CD    1 
ATOM   822  O OE1   . GLU A 1 124 ? -22.683 -8.337  -18.527 1.00 48.47  ? 105 GLU A OE1   1 
ATOM   823  O OE2   . GLU A 1 124 ? -24.188 -6.717  -18.475 1.00 61.98  ? 105 GLU A OE2   1 
ATOM   824  N N     . VAL A 1 125 ? -17.648 -6.925  -17.285 1.00 31.69  ? 106 VAL A N     1 
ATOM   825  C CA    . VAL A 1 125 ? -16.438 -7.642  -16.893 1.00 29.77  ? 106 VAL A CA    1 
ATOM   826  C C     . VAL A 1 125 ? -15.509 -6.717  -16.103 1.00 28.00  ? 106 VAL A C     1 
ATOM   827  O O     . VAL A 1 125 ? -14.989 -7.081  -15.065 1.00 28.50  ? 106 VAL A O     1 
ATOM   828  C CB    . VAL A 1 125 ? -15.735 -8.274  -18.109 1.00 30.15  ? 106 VAL A CB    1 
ATOM   829  C CG1   . VAL A 1 125 ? -14.284 -8.651  -17.834 1.00 30.38  ? 106 VAL A CG1   1 
ATOM   830  C CG2   . VAL A 1 125 ? -16.534 -9.490  -18.602 1.00 33.45  ? 106 VAL A CG2   1 
ATOM   831  N N     . LEU A 1 126 ? -15.338 -5.484  -16.576 1.00 27.69  ? 107 LEU A N     1 
ATOM   832  C CA    . LEU A 1 126 ? -14.427 -4.560  -15.927 1.00 24.77  ? 107 LEU A CA    1 
ATOM   833  C C     . LEU A 1 126 ? -15.019 -4.119  -14.583 1.00 27.47  ? 107 LEU A C     1 
ATOM   834  O O     . LEU A 1 126 ? -14.310 -3.996  -13.589 1.00 27.29  ? 107 LEU A O     1 
ATOM   835  C CB    . LEU A 1 126 ? -14.199 -3.377  -16.864 1.00 23.59  ? 107 LEU A CB    1 
ATOM   836  C CG    . LEU A 1 126 ? -13.490 -3.694  -18.176 1.00 29.28  ? 107 LEU A CG    1 
ATOM   837  C CD1   . LEU A 1 126 ? -13.449 -2.468  -19.103 1.00 29.17  ? 107 LEU A CD1   1 
ATOM   838  C CD2   . LEU A 1 126 ? -12.091 -4.193  -17.896 1.00 28.59  ? 107 LEU A CD2   1 
ATOM   839  N N     . GLU A 1 127 ? -16.340 -3.874  -14.565 1.00 28.12  ? 108 GLU A N     1 
ATOM   840  C CA    . GLU A 1 127 ? -16.975 -3.446  -13.336 1.00 31.80  ? 108 GLU A CA    1 
ATOM   841  C C     . GLU A 1 127 ? -16.868 -4.526  -12.253 1.00 32.29  ? 108 GLU A C     1 
ATOM   842  O O     . GLU A 1 127 ? -16.591 -4.203  -11.092 1.00 32.12  ? 108 GLU A O     1 
ATOM   843  C CB    . GLU A 1 127 ? -18.438 -3.039  -13.550 1.00 34.94  ? 108 GLU A CB    1 
ATOM   844  C CG    . GLU A 1 127 ? -18.999 -2.335  -12.319 1.00 40.47  ? 108 GLU A CG    1 
ATOM   845  C CD    . GLU A 1 127 ? -20.284 -1.553  -12.548 1.00 49.55  ? 108 GLU A CD    1 
ATOM   846  O OE1   . GLU A 1 127 ? -20.869 -1.067  -11.546 1.00 50.46  ? 108 GLU A OE1   1 
ATOM   847  O OE2   . GLU A 1 127 ? -20.700 -1.437  -13.725 1.00 47.54  ? 108 GLU A OE2   1 
ATOM   848  N N     . GLN A 1 128 ? -17.110 -5.796  -12.604 1.00 32.85  ? 109 GLN A N     1 
ATOM   849  C CA    . GLN A 1 128 ? -16.953 -6.863  -11.628 1.00 36.14  ? 109 GLN A CA    1 
ATOM   850  C C     . GLN A 1 128 ? -15.521 -6.917  -11.098 1.00 31.11  ? 109 GLN A C     1 
ATOM   851  O O     . GLN A 1 128 ? -15.297 -7.046  -9.902  1.00 31.15  ? 109 GLN A O     1 
ATOM   852  C CB    . GLN A 1 128 ? -17.367 -8.198  -12.226 1.00 39.45  ? 109 GLN A CB    1 
ATOM   853  C CG    . GLN A 1 128 ? -17.241 -9.344  -11.241 1.00 51.87  ? 109 GLN A CG    1 
ATOM   854  C CD    . GLN A 1 128 ? -17.483 -10.666 -11.924 1.00 63.13  ? 109 GLN A CD    1 
ATOM   855  O OE1   . GLN A 1 128 ? -16.684 -11.594 -11.826 1.00 76.99  ? 109 GLN A OE1   1 
ATOM   856  N NE2   . GLN A 1 128 ? -18.595 -10.759 -12.634 1.00 68.99  ? 109 GLN A NE2   1 
ATOM   857  N N     . ARG A 1 129 ? -14.525 -6.815  -11.974 1.00 29.73  ? 110 ARG A N     1 
ATOM   858  C CA    . ARG A 1 129 ? -13.153 -6.819  -11.507 1.00 27.97  ? 110 ARG A CA    1 
ATOM   859  C C     . ARG A 1 129 ? -12.873 -5.611  -10.609 1.00 27.58  ? 110 ARG A C     1 
ATOM   860  O O     . ARG A 1 129 ? -12.245 -5.756  -9.574  1.00 29.58  ? 110 ARG A O     1 
ATOM   861  C CB    . ARG A 1 129 ? -12.175 -6.910  -12.685 1.00 28.90  ? 110 ARG A CB    1 
ATOM   862  C CG    . ARG A 1 129 ? -10.716 -6.779  -12.281 1.00 28.28  ? 110 ARG A CG    1 
ATOM   863  C CD    . ARG A 1 129 ? -10.150 -7.905  -11.422 1.00 33.54  ? 110 ARG A CD    1 
ATOM   864  N NE    . ARG A 1 129 ? -10.296 -9.202  -12.079 1.00 39.51  ? 110 ARG A NE    1 
ATOM   865  C CZ    . ARG A 1 129 ? -9.341  -9.772  -12.829 1.00 48.65  ? 110 ARG A CZ    1 
ATOM   866  N NH1   . ARG A 1 129 ? -9.570  -10.892 -13.494 1.00 53.16  ? 110 ARG A NH1   1 
ATOM   867  N NH2   . ARG A 1 129 ? -8.158  -9.198  -12.947 1.00 46.78  ? 110 ARG A NH2   1 
ATOM   868  N N     . ALA A 1 130 ? -13.367 -4.419  -10.958 1.00 30.47  ? 111 ALA A N     1 
ATOM   869  C CA    . ALA A 1 130 ? -13.157 -3.244  -10.114 1.00 31.15  ? 111 ALA A CA    1 
ATOM   870  C C     . ALA A 1 130 ? -13.745 -3.481  -8.706  1.00 32.50  ? 111 ALA A C     1 
ATOM   871  O O     . ALA A 1 130 ? -13.097 -3.159  -7.708  1.00 35.95  ? 111 ALA A O     1 
ATOM   872  C CB    . ALA A 1 130 ? -13.773 -2.023  -10.767 1.00 29.71  ? 111 ALA A CB    1 
ATOM   873  N N     . ARG A 1 131 ? -14.950 -4.086  -8.633  1.00 34.35  ? 112 ARG A N     1 
ATOM   874  C CA    . ARG A 1 131 ? -15.581 -4.392  -7.351  1.00 40.67  ? 112 ARG A CA    1 
ATOM   875  C C     . ARG A 1 131 ? -14.714 -5.356  -6.541  1.00 40.00  ? 112 ARG A C     1 
ATOM   876  O O     . ARG A 1 131 ? -14.527 -5.151  -5.346  1.00 39.91  ? 112 ARG A O     1 
ATOM   877  C CB    . ARG A 1 131 ? -17.002 -4.941  -7.528  1.00 46.01  ? 112 ARG A CB    1 
ATOM   878  C CG    . ARG A 1 131 ? -17.917 -4.009  -8.310  1.00 54.45  ? 112 ARG A CG    1 
ATOM   879  C CD    . ARG A 1 131 ? -19.393 -4.050  -7.955  1.00 66.12  ? 112 ARG A CD    1 
ATOM   880  N NE    . ARG A 1 131 ? -19.839 -2.865  -7.220  1.00 76.98  ? 112 ARG A NE    1 
ATOM   881  C CZ    . ARG A 1 131 ? -20.028 -1.646  -7.734  1.00 74.94  ? 112 ARG A CZ    1 
ATOM   882  N NH1   . ARG A 1 131 ? -19.804 -1.394  -9.014  1.00 68.13  ? 112 ARG A NH1   1 
ATOM   883  N NH2   . ARG A 1 131 ? -20.447 -0.667  -6.952  1.00 78.79  ? 112 ARG A NH2   1 
ATOM   884  N N     . GLU A 1 132 ? -14.137 -6.384  -7.177  1.00 39.17  ? 113 GLU A N     1 
ATOM   885  C CA    . GLU A 1 132 ? -13.238 -7.289  -6.470  1.00 40.88  ? 113 GLU A CA    1 
ATOM   886  C C     . GLU A 1 132 ? -11.985 -6.586  -5.955  1.00 39.02  ? 113 GLU A C     1 
ATOM   887  O O     . GLU A 1 132 ? -11.432 -6.998  -4.944  1.00 36.59  ? 113 GLU A O     1 
ATOM   888  C CB    . GLU A 1 132 ? -12.810 -8.468  -7.340  1.00 44.36  ? 113 GLU A CB    1 
ATOM   889  C CG    . GLU A 1 132 ? -13.934 -9.459  -7.582  1.00 57.45  ? 113 GLU A CG    1 
ATOM   890  C CD    . GLU A 1 132 ? -13.808 -10.321 -8.831  1.00 63.78  ? 113 GLU A CD    1 
ATOM   891  O OE1   . GLU A 1 132 ? -12.673 -10.480 -9.336  1.00 67.57  ? 113 GLU A OE1   1 
ATOM   892  O OE2   . GLU A 1 132 ? -14.862 -10.798 -9.321  1.00 64.26  ? 113 GLU A OE2   1 
ATOM   893  N N     . LEU A 1 133 ? -11.523 -5.529  -6.624  1.00 32.41  ? 114 LEU A N     1 
ATOM   894  C CA    . LEU A 1 133 ? -10.328 -4.819  -6.176  1.00 34.10  ? 114 LEU A CA    1 
ATOM   895  C C     . LEU A 1 133 ? -10.694 -3.722  -5.171  1.00 36.59  ? 114 LEU A C     1 
ATOM   896  O O     . LEU A 1 133 ? -9.867  -2.883  -4.819  1.00 37.62  ? 114 LEU A O     1 
ATOM   897  C CB    . LEU A 1 133 ? -9.649  -4.214  -7.403  1.00 32.95  ? 114 LEU A CB    1 
ATOM   898  C CG    . LEU A 1 133 ? -8.881  -5.188  -8.294  1.00 33.81  ? 114 LEU A CG    1 
ATOM   899  C CD1   . LEU A 1 133 ? -8.490  -4.497  -9.603  1.00 37.06  ? 114 LEU A CD1   1 
ATOM   900  C CD2   . LEU A 1 133 ? -7.660  -5.730  -7.596  1.00 36.52  ? 114 LEU A CD2   1 
ATOM   901  N N     . GLY A 1 134 ? -11.974 -3.650  -4.816  1.00 35.69  ? 115 GLY A N     1 
ATOM   902  C CA    . GLY A 1 134 ? -12.429 -2.749  -3.770  1.00 37.93  ? 115 GLY A CA    1 
ATOM   903  C C     . GLY A 1 134 ? -12.740 -1.340  -4.270  1.00 41.38  ? 115 GLY A C     1 
ATOM   904  O O     . GLY A 1 134 ? -12.780 -0.398  -3.476  1.00 41.28  ? 115 GLY A O     1 
ATOM   905  N N     . VAL A 1 135 ? -12.965 -1.166  -5.583  1.00 38.83  ? 116 VAL A N     1 
ATOM   906  C CA    . VAL A 1 135 ? -13.094 0.183   -6.109  1.00 40.32  ? 116 VAL A CA    1 
ATOM   907  C C     . VAL A 1 135 ? -14.506 0.688   -5.853  1.00 39.99  ? 116 VAL A C     1 
ATOM   908  O O     . VAL A 1 135 ? -15.474 0.027   -6.206  1.00 42.36  ? 116 VAL A O     1 
ATOM   909  C CB    . VAL A 1 135 ? -12.741 0.223   -7.607  1.00 39.47  ? 116 VAL A CB    1 
ATOM   910  C CG1   . VAL A 1 135 ? -13.133 1.534   -8.243  1.00 36.20  ? 116 VAL A CG1   1 
ATOM   911  C CG2   . VAL A 1 135 ? -11.265 -0.070  -7.800  1.00 41.60  ? 116 VAL A CG2   1 
ATOM   912  N N     . ASP A 1 136 ? -14.622 1.898   -5.297  1.00 46.57  ? 117 ASP A N     1 
ATOM   913  C CA    . ASP A 1 136 ? -15.935 2.485   -5.066  1.00 53.71  ? 117 ASP A CA    1 
ATOM   914  C C     . ASP A 1 136 ? -16.368 3.240   -6.319  1.00 45.72  ? 117 ASP A C     1 
ATOM   915  O O     . ASP A 1 136 ? -15.681 4.188   -6.751  1.00 36.99  ? 117 ASP A O     1 
ATOM   916  C CB    . ASP A 1 136 ? -16.011 3.376   -3.817  1.00 61.56  ? 117 ASP A CB    1 
ATOM   917  C CG    . ASP A 1 136 ? -14.847 4.336   -3.623  1.00 68.17  ? 117 ASP A CG    1 
ATOM   918  O OD1   . ASP A 1 136 ? -13.797 4.149   -4.304  1.00 66.95  ? 117 ASP A OD1   1 
ATOM   919  O OD2   . ASP A 1 136 ? -15.000 5.272   -2.794  1.00 73.79  ? 117 ASP A OD2   1 
ATOM   920  N N     . VAL A 1 137 ? -17.519 2.785   -6.842  1.00 42.46  ? 118 VAL A N     1 
ATOM   921  C CA    . VAL A 1 137 ? -18.172 3.305   -8.038  1.00 46.57  ? 118 VAL A CA    1 
ATOM   922  C C     . VAL A 1 137 ? -19.459 4.030   -7.654  1.00 41.12  ? 118 VAL A C     1 
ATOM   923  O O     . VAL A 1 137 ? -20.456 3.407   -7.320  1.00 46.53  ? 118 VAL A O     1 
ATOM   924  C CB    . VAL A 1 137 ? -18.498 2.175   -9.028  1.00 49.38  ? 118 VAL A CB    1 
ATOM   925  C CG1   . VAL A 1 137 ? -19.120 2.709   -10.321 1.00 42.73  ? 118 VAL A CG1   1 
ATOM   926  C CG2   . VAL A 1 137 ? -17.265 1.338   -9.327  1.00 55.26  ? 118 VAL A CG2   1 
ATOM   927  N N     . ARG A 1 138 ? -19.449 5.339   -7.841  1.00 37.43  ? 119 ARG A N     1 
ATOM   928  C CA    . ARG A 1 138 ? -20.463 6.214   -7.306  1.00 37.31  ? 119 ARG A CA    1 
ATOM   929  C C     . ARG A 1 138 ? -21.321 6.709   -8.454  1.00 37.90  ? 119 ARG A C     1 
ATOM   930  O O     . ARG A 1 138 ? -20.948 7.659   -9.141  1.00 35.48  ? 119 ARG A O     1 
ATOM   931  C CB    . ARG A 1 138 ? -19.777 7.352   -6.548  1.00 39.05  ? 119 ARG A CB    1 
ATOM   932  C CG    . ARG A 1 138 ? -18.946 6.871   -5.376  1.00 39.85  ? 119 ARG A CG    1 
ATOM   933  C CD    . ARG A 1 138 ? -18.533 8.046   -4.523  1.00 43.16  ? 119 ARG A CD    1 
ATOM   934  N NE    . ARG A 1 138 ? -17.603 7.605   -3.502  1.00 45.93  ? 119 ARG A NE    1 
ATOM   935  C CZ    . ARG A 1 138 ? -16.937 8.428   -2.697  1.00 42.18  ? 119 ARG A CZ    1 
ATOM   936  N NH1   . ARG A 1 138 ? -17.251 9.711   -2.660  1.00 41.72  ? 119 ARG A NH1   1 
ATOM   937  N NH2   . ARG A 1 138 ? -15.955 7.958   -1.952  1.00 45.32  ? 119 ARG A NH2   1 
ATOM   938  N N     . ARG A 1 139 ? -22.450 6.034   -8.658  1.00 34.47  ? 120 ARG A N     1 
ATOM   939  C CA    . ARG A 1 139 ? -23.381 6.374   -9.720  1.00 36.53  ? 120 ARG A CA    1 
ATOM   940  C C     . ARG A 1 139 ? -24.298 7.491   -9.231  1.00 35.48  ? 120 ARG A C     1 
ATOM   941  O O     . ARG A 1 139 ? -24.294 7.775   -8.042  1.00 37.92  ? 120 ARG A O     1 
ATOM   942  C CB    . ARG A 1 139 ? -24.150 5.125   -10.169 1.00 40.87  ? 120 ARG A CB    1 
ATOM   943  C CG    . ARG A 1 139 ? -23.294 4.178   -11.007 1.00 42.21  ? 120 ARG A CG    1 
ATOM   944  C CD    . ARG A 1 139 ? -24.062 3.456   -12.093 1.00 44.71  ? 120 ARG A CD    1 
ATOM   945  N NE    . ARG A 1 139 ? -23.185 2.863   -13.105 1.00 46.26  ? 120 ARG A NE    1 
ATOM   946  C CZ    . ARG A 1 139 ? -22.440 1.780   -12.913 1.00 42.12  ? 120 ARG A CZ    1 
ATOM   947  N NH1   . ARG A 1 139 ? -22.517 1.117   -11.774 1.00 43.04  ? 120 ARG A NH1   1 
ATOM   948  N NH2   . ARG A 1 139 ? -21.648 1.344   -13.873 1.00 39.13  ? 120 ARG A NH2   1 
ATOM   949  N N     . GLY A 1 140 ? -25.024 8.120   -10.162 1.00 35.60  ? 121 GLY A N     1 
ATOM   950  C CA    . GLY A 1 140 ? -25.829 9.302   -9.886  1.00 38.02  ? 121 GLY A CA    1 
ATOM   951  C C     . GLY A 1 140 ? -24.972 10.497  -9.450  1.00 37.56  ? 121 GLY A C     1 
ATOM   952  O O     . GLY A 1 140 ? -25.467 11.406  -8.795  1.00 43.81  ? 121 GLY A O     1 
ATOM   953  N N     . HIS A 1 141 ? -23.691 10.517  -9.831  1.00 33.27  ? 122 HIS A N     1 
ATOM   954  C CA    . HIS A 1 141 ? -22.799 11.609  -9.471  1.00 31.90  ? 122 HIS A CA    1 
ATOM   955  C C     . HIS A 1 141 ? -22.312 12.330  -10.733 1.00 36.03  ? 122 HIS A C     1 
ATOM   956  O O     . HIS A 1 141 ? -21.532 11.785  -11.501 1.00 36.13  ? 122 HIS A O     1 
ATOM   957  C CB    . HIS A 1 141 ? -21.627 11.069  -8.663  1.00 36.32  ? 122 HIS A CB    1 
ATOM   958  C CG    . HIS A 1 141 ? -21.915 10.666  -7.252  1.00 34.03  ? 122 HIS A CG    1 
ATOM   959  N ND1   . HIS A 1 141 ? -22.834 9.701   -6.894  1.00 37.29  ? 122 HIS A ND1   1 
ATOM   960  C CD2   . HIS A 1 141 ? -21.334 11.071  -6.118  1.00 39.33  ? 122 HIS A CD2   1 
ATOM   961  C CE1   . HIS A 1 141 ? -22.815 9.555   -5.570  1.00 38.69  ? 122 HIS A CE1   1 
ATOM   962  N NE2   . HIS A 1 141 ? -21.906 10.379  -5.079  1.00 41.58  ? 122 HIS A NE2   1 
ATOM   963  N N     . GLU A 1 142 ? -22.752 13.573  -10.948 1.00 34.10  ? 123 GLU A N     1 
ATOM   964  C CA    . GLU A 1 142 ? -22.389 14.343  -12.130 1.00 37.12  ? 123 GLU A CA    1 
ATOM   965  C C     . GLU A 1 142 ? -21.365 15.413  -11.762 1.00 40.97  ? 123 GLU A C     1 
ATOM   966  O O     . GLU A 1 142 ? -21.616 16.271  -10.919 1.00 40.74  ? 123 GLU A O     1 
ATOM   967  C CB    . GLU A 1 142 ? -23.614 14.990  -12.780 1.00 39.31  ? 123 GLU A CB    1 
ATOM   968  C CG    . GLU A 1 142 ? -23.287 15.778  -14.038 1.00 42.04  ? 123 GLU A CG    1 
ATOM   969  C CD    . GLU A 1 142 ? -24.472 16.148  -14.909 1.00 47.45  ? 123 GLU A CD    1 
ATOM   970  O OE1   . GLU A 1 142 ? -24.240 16.590  -16.042 1.00 48.71  ? 123 GLU A OE1   1 
ATOM   971  O OE2   . GLU A 1 142 ? -25.615 15.985  -14.460 1.00 55.07  ? 123 GLU A OE2   1 
ATOM   972  N N     . VAL A 1 143 ? -20.224 15.408  -12.452 1.00 31.69  ? 124 VAL A N     1 
ATOM   973  C CA    . VAL A 1 143 ? -19.242 16.455  -12.269 1.00 33.57  ? 124 VAL A CA    1 
ATOM   974  C C     . VAL A 1 143 ? -19.713 17.715  -12.999 1.00 37.25  ? 124 VAL A C     1 
ATOM   975  O O     . VAL A 1 143 ? -20.030 17.651  -14.194 1.00 36.32  ? 124 VAL A O     1 
ATOM   976  C CB    . VAL A 1 143 ? -17.855 15.991  -12.742 1.00 31.53  ? 124 VAL A CB    1 
ATOM   977  C CG1   . VAL A 1 143 ? -16.824 17.093  -12.638 1.00 31.88  ? 124 VAL A CG1   1 
ATOM   978  C CG2   . VAL A 1 143 ? -17.405 14.764  -11.984 1.00 31.52  ? 124 VAL A CG2   1 
ATOM   979  N N     . THR A 1 144 ? -19.746 18.857  -12.271 1.00 35.03  ? 125 THR A N     1 
ATOM   980  C CA    . THR A 1 144 ? -20.177 20.127  -12.853 1.00 35.25  ? 125 THR A CA    1 
ATOM   981  C C     . THR A 1 144 ? -19.072 21.193  -12.868 1.00 32.11  ? 125 THR A C     1 
ATOM   982  O O     . THR A 1 144 ? -19.118 22.103  -13.694 1.00 39.37  ? 125 THR A O     1 
ATOM   983  C CB    . THR A 1 144 ? -21.455 20.668  -12.179 1.00 37.40  ? 125 THR A CB    1 
ATOM   984  O OG1   . THR A 1 144 ? -21.145 20.870  -10.809 1.00 39.89  ? 125 THR A OG1   1 
ATOM   985  C CG2   . THR A 1 144 ? -22.655 19.757  -12.319 1.00 38.87  ? 125 THR A CG2   1 
ATOM   986  N N     . GLU A 1 145 ? -18.068 21.117  -11.996 1.00 36.32  ? 126 GLU A N     1 
ATOM   987  C CA    . GLU A 1 145 ? -16.997 22.103  -12.000 1.00 37.24  ? 126 GLU A CA    1 
ATOM   988  C C     . GLU A 1 145 ? -15.738 21.419  -11.511 1.00 35.61  ? 126 GLU A C     1 
ATOM   989  O O     . GLU A 1 145 ? -15.822 20.369  -10.876 1.00 35.37  ? 126 GLU A O     1 
ATOM   990  C CB    . GLU A 1 145 ? -17.316 23.305  -11.083 1.00 46.55  ? 126 GLU A CB    1 
ATOM   991  C CG    . GLU A 1 145 ? -18.702 23.915  -11.318 1.00 58.80  ? 126 GLU A CG    1 
ATOM   992  C CD    . GLU A 1 145 ? -19.180 24.996  -10.350 1.00 65.79  ? 126 GLU A CD    1 
ATOM   993  O OE1   . GLU A 1 145 ? -18.637 26.124  -10.386 1.00 66.17  ? 126 GLU A OE1   1 
ATOM   994  O OE2   . GLU A 1 145 ? -20.116 24.711  -9.564  1.00 69.37  ? 126 GLU A OE2   1 
ATOM   995  N N     . LEU A 1 146 ? -14.593 22.068  -11.770 1.00 32.89  ? 127 LEU A N     1 
ATOM   996  C CA    . LEU A 1 146 ? -13.287 21.553  -11.403 1.00 38.44  ? 127 LEU A CA    1 
ATOM   997  C C     . LEU A 1 146 ? -12.381 22.721  -11.020 1.00 37.63  ? 127 LEU A C     1 
ATOM   998  O O     . LEU A 1 146 ? -12.320 23.702  -11.749 1.00 40.88  ? 127 LEU A O     1 
ATOM   999  C CB    . LEU A 1 146 ? -12.745 20.795  -12.627 1.00 41.57  ? 127 LEU A CB    1 
ATOM   1000 C CG    . LEU A 1 146 ? -11.232 20.792  -12.803 1.00 47.24  ? 127 LEU A CG    1 
ATOM   1001 C CD1   . LEU A 1 146 ? -10.652 19.524  -12.235 1.00 56.89  ? 127 LEU A CD1   1 
ATOM   1002 C CD2   . LEU A 1 146 ? -10.846 20.935  -14.263 1.00 58.06  ? 127 LEU A CD2   1 
ATOM   1003 N N     . ARG A 1 147 ? -11.637 22.579  -9.920  1.00 36.95  ? 128 ARG A N     1 
ATOM   1004 C CA    . ARG A 1 147 ? -10.648 23.564  -9.531  1.00 36.48  ? 128 ARG A CA    1 
ATOM   1005 C C     . ARG A 1 147 ? -9.373  22.849  -9.113  1.00 36.58  ? 128 ARG A C     1 
ATOM   1006 O O     . ARG A 1 147 ? -9.390  22.011  -8.207  1.00 38.02  ? 128 ARG A O     1 
ATOM   1007 C CB    . ARG A 1 147 ? -11.199 24.443  -8.394  1.00 43.54  ? 128 ARG A CB    1 
ATOM   1008 C CG    . ARG A 1 147 ? -10.163 25.376  -7.773  1.00 44.81  ? 128 ARG A CG    1 
ATOM   1009 C CD    . ARG A 1 147 ? -10.798 26.306  -6.740  1.00 49.76  ? 128 ARG A CD    1 
ATOM   1010 N NE    . ARG A 1 147 ? -11.370 25.541  -5.630  1.00 49.82  ? 128 ARG A NE    1 
ATOM   1011 C CZ    . ARG A 1 147 ? -10.678 25.094  -4.589  1.00 46.56  ? 128 ARG A CZ    1 
ATOM   1012 N NH1   . ARG A 1 147 ? -11.243 24.300  -3.694  1.00 49.08  ? 128 ARG A NH1   1 
ATOM   1013 N NH2   . ARG A 1 147 ? -9.409  25.437  -4.455  1.00 48.26  ? 128 ARG A NH2   1 
ATOM   1014 N N     . GLN A 1 148 ? -8.264  23.224  -9.764  1.00 34.35  ? 129 GLN A N     1 
ATOM   1015 C CA    . GLN A 1 148 ? -6.953  22.706  -9.416  1.00 37.24  ? 129 GLN A CA    1 
ATOM   1016 C C     . GLN A 1 148 ? -6.296  23.565  -8.339  1.00 39.42  ? 129 GLN A C     1 
ATOM   1017 O O     . GLN A 1 148 ? -6.367  24.793  -8.355  1.00 39.43  ? 129 GLN A O     1 
ATOM   1018 C CB    . GLN A 1 148 ? -6.047  22.672  -10.644 1.00 40.44  ? 129 GLN A CB    1 
ATOM   1019 C CG    . GLN A 1 148 ? -6.604  21.821  -11.779 1.00 41.81  ? 129 GLN A CG    1 
ATOM   1020 C CD    . GLN A 1 148 ? -5.513  21.240  -12.650 1.00 35.78  ? 129 GLN A CD    1 
ATOM   1021 O OE1   . GLN A 1 148 ? -4.473  20.757  -12.175 1.00 32.50  ? 129 GLN A OE1   1 
ATOM   1022 N NE2   . GLN A 1 148 ? -5.777  21.282  -13.949 1.00 37.54  ? 129 GLN A NE2   1 
ATOM   1023 N N     . SER A 1 149 ? -5.589  22.889  -7.446  1.00 36.82  ? 130 SER A N     1 
ATOM   1024 C CA    . SER A 1 149 ? -4.672  23.506  -6.512  1.00 38.21  ? 130 SER A CA    1 
ATOM   1025 C C     . SER A 1 149 ? -3.308  22.877  -6.759  1.00 37.70  ? 130 SER A C     1 
ATOM   1026 O O     . SER A 1 149 ? -3.210  21.876  -7.470  1.00 40.74  ? 130 SER A O     1 
ATOM   1027 C CB    . SER A 1 149 ? -5.119  23.315  -5.085  1.00 37.82  ? 130 SER A CB    1 
ATOM   1028 O OG    . SER A 1 149 ? -6.443  23.775  -4.892  1.00 38.55  ? 130 SER A OG    1 
ATOM   1029 N N     . PRO A 1 150 ? -2.212  23.431  -6.214  1.00 40.17  ? 131 PRO A N     1 
ATOM   1030 C CA    . PRO A 1 150 ? -0.880  22.863  -6.458  1.00 40.09  ? 131 PRO A CA    1 
ATOM   1031 C C     . PRO A 1 150 ? -0.744  21.374  -6.111  1.00 40.81  ? 131 PRO A C     1 
ATOM   1032 O O     . PRO A 1 150 ? -0.092  20.631  -6.861  1.00 36.72  ? 131 PRO A O     1 
ATOM   1033 C CB    . PRO A 1 150 ? 0.036   23.802  -5.660  1.00 43.86  ? 131 PRO A CB    1 
ATOM   1034 C CG    . PRO A 1 150 ? -0.739  25.130  -5.647  1.00 38.87  ? 131 PRO A CG    1 
ATOM   1035 C CD    . PRO A 1 150 ? -2.177  24.702  -5.463  1.00 40.27  ? 131 PRO A CD    1 
ATOM   1036 N N     . GLY A 1 151 ? -1.467  20.924  -5.069  1.00 34.81  ? 132 GLY A N     1 
ATOM   1037 C CA    . GLY A 1 151 ? -1.267  19.596  -4.508  1.00 36.78  ? 132 GLY A CA    1 
ATOM   1038 C C     . GLY A 1 151 ? -2.479  18.666  -4.627  1.00 34.01  ? 132 GLY A C     1 
ATOM   1039 O O     . GLY A 1 151 ? -2.393  17.523  -4.192  1.00 36.50  ? 132 GLY A O     1 
ATOM   1040 N N     . HIS A 1 152 ? -3.600  19.157  -5.148  1.00 33.23  ? 133 HIS A N     1 
ATOM   1041 C CA    . HIS A 1 152 ? -4.804  18.347  -5.274  1.00 34.32  ? 133 HIS A CA    1 
ATOM   1042 C C     . HIS A 1 152 ? -5.760  19.019  -6.240  1.00 31.52  ? 133 HIS A C     1 
ATOM   1043 O O     . HIS A 1 152 ? -5.544  20.140  -6.718  1.00 34.45  ? 133 HIS A O     1 
ATOM   1044 C CB    . HIS A 1 152 ? -5.493  18.143  -3.914  1.00 36.95  ? 133 HIS A CB    1 
ATOM   1045 C CG    . HIS A 1 152 ? -5.979  19.413  -3.298  1.00 37.49  ? 133 HIS A CG    1 
ATOM   1046 N ND1   . HIS A 1 152 ? -7.284  19.859  -3.357  1.00 40.53  ? 133 HIS A ND1   1 
ATOM   1047 C CD2   . HIS A 1 152 ? -5.282  20.341  -2.627  1.00 34.42  ? 133 HIS A CD2   1 
ATOM   1048 C CE1   . HIS A 1 152 ? -7.362  21.023  -2.729  1.00 38.70  ? 133 HIS A CE1   1 
ATOM   1049 N NE2   . HIS A 1 152 ? -6.152  21.337  -2.298  1.00 40.73  ? 133 HIS A NE2   1 
ATOM   1050 N N     . VAL A 1 153 ? -6.860  18.327  -6.518  1.00 31.37  ? 134 VAL A N     1 
ATOM   1051 C CA    . VAL A 1 153 ? -7.926  18.848  -7.334  1.00 31.31  ? 134 VAL A CA    1 
ATOM   1052 C C     . VAL A 1 153 ? -9.218  18.688  -6.560  1.00 34.56  ? 134 VAL A C     1 
ATOM   1053 O O     . VAL A 1 153 ? -9.356  17.704  -5.843  1.00 37.04  ? 134 VAL A O     1 
ATOM   1054 C CB    . VAL A 1 153 ? -8.013  18.086  -8.677  1.00 33.20  ? 134 VAL A CB    1 
ATOM   1055 C CG1   . VAL A 1 153 ? -8.984  18.739  -9.633  1.00 39.11  ? 134 VAL A CG1   1 
ATOM   1056 C CG2   . VAL A 1 153 ? -6.652  17.986  -9.305  1.00 34.41  ? 134 VAL A CG2   1 
ATOM   1057 N N     . THR A 1 154 ? -10.159 19.612  -6.793  1.00 32.25  ? 135 THR A N     1 
ATOM   1058 C CA    . THR A 1 154 ? -11.481 19.604  -6.196  1.00 36.29  ? 135 THR A CA    1 
ATOM   1059 C C     . THR A 1 154 ? -12.556 19.666  -7.269  1.00 32.95  ? 135 THR A C     1 
ATOM   1060 O O     . THR A 1 154 ? -12.572 20.563  -8.118  1.00 38.86  ? 135 THR A O     1 
ATOM   1061 C CB    . THR A 1 154 ? -11.661 20.804  -5.247  1.00 37.99  ? 135 THR A CB    1 
ATOM   1062 O OG1   . THR A 1 154 ? -10.580 20.788  -4.329  1.00 39.73  ? 135 THR A OG1   1 
ATOM   1063 C CG2   . THR A 1 154 ? -12.957 20.803  -4.477  1.00 39.77  ? 135 THR A CG2   1 
ATOM   1064 N N     . LEU A 1 155 ? -13.496 18.712  -7.215  1.00 33.61  ? 136 LEU A N     1 
ATOM   1065 C CA    . LEU A 1 155 ? -14.615 18.663  -8.142  1.00 32.29  ? 136 LEU A CA    1 
ATOM   1066 C C     . LEU A 1 155 ? -15.884 19.107  -7.438  1.00 35.19  ? 136 LEU A C     1 
ATOM   1067 O O     . LEU A 1 155 ? -16.072 18.775  -6.280  1.00 38.69  ? 136 LEU A O     1 
ATOM   1068 C CB    . LEU A 1 155 ? -14.819 17.217  -8.604  1.00 36.37  ? 136 LEU A CB    1 
ATOM   1069 C CG    . LEU A 1 155 ? -13.612 16.617  -9.311  1.00 38.78  ? 136 LEU A CG    1 
ATOM   1070 C CD1   . LEU A 1 155 ? -13.986 15.287  -9.913  1.00 37.37  ? 136 LEU A CD1   1 
ATOM   1071 C CD2   . LEU A 1 155 ? -13.094 17.565  -10.377 1.00 40.64  ? 136 LEU A CD2   1 
ATOM   1072 N N     . LYS A 1 156 ? -16.757 19.814  -8.152  1.00 37.91  ? 137 LYS A N     1 
ATOM   1073 C CA    . LYS A 1 156 ? -18.121 20.032  -7.693  1.00 40.43  ? 137 LYS A CA    1 
ATOM   1074 C C     . LYS A 1 156 ? -19.016 18.963  -8.320  1.00 39.59  ? 137 LYS A C     1 
ATOM   1075 O O     . LYS A 1 156 ? -18.923 18.730  -9.527  1.00 39.78  ? 137 LYS A O     1 
ATOM   1076 C CB    . LYS A 1 156 ? -18.506 21.467  -8.074  1.00 47.05  ? 137 LYS A CB    1 
ATOM   1077 C CG    . LYS A 1 156 ? -19.640 22.108  -7.288  1.00 58.82  ? 137 LYS A CG    1 
ATOM   1078 C CD    . LYS A 1 156 ? -21.025 21.693  -7.755  1.00 66.65  ? 137 LYS A CD    1 
ATOM   1079 C CE    . LYS A 1 156 ? -22.028 22.832  -7.777  1.00 70.11  ? 137 LYS A CE    1 
ATOM   1080 N NZ    . LYS A 1 156 ? -22.034 23.599  -6.510  1.00 73.01  ? 137 LYS A NZ    1 
ATOM   1081 N N     . LEU A 1 157 ? -19.870 18.317  -7.515  1.00 36.90  ? 138 LEU A N     1 
ATOM   1082 C CA    . LEU A 1 157 ? -20.716 17.222  -7.961  1.00 40.10  ? 138 LEU A CA    1 
ATOM   1083 C C     . LEU A 1 157 ? -22.183 17.565  -7.738  1.00 44.46  ? 138 LEU A C     1 
ATOM   1084 O O     . LEU A 1 157 ? -22.508 18.335  -6.840  1.00 45.96  ? 138 LEU A O     1 
ATOM   1085 C CB    . LEU A 1 157 ? -20.409 15.936  -7.180  1.00 39.44  ? 138 LEU A CB    1 
ATOM   1086 C CG    . LEU A 1 157 ? -18.947 15.552  -6.980  1.00 50.29  ? 138 LEU A CG    1 
ATOM   1087 C CD1   . LEU A 1 157 ? -18.845 14.166  -6.353  1.00 49.73  ? 138 LEU A CD1   1 
ATOM   1088 C CD2   . LEU A 1 157 ? -18.160 15.592  -8.282  1.00 51.43  ? 138 LEU A CD2   1 
ATOM   1089 N N     . ARG A 1 158 ? -23.048 16.905  -8.512  1.00 44.00  ? 139 ARG A N     1 
ATOM   1090 C CA    . ARG A 1 158 ? -24.491 16.919  -8.335  1.00 48.88  ? 139 ARG A CA    1 
ATOM   1091 C C     . ARG A 1 158 ? -24.997 15.486  -8.196  1.00 48.95  ? 139 ARG A C     1 
ATOM   1092 O O     . ARG A 1 158 ? -24.697 14.638  -9.033  1.00 42.13  ? 139 ARG A O     1 
ATOM   1093 C CB    . ARG A 1 158 ? -25.217 17.537  -9.529  1.00 53.23  ? 139 ARG A CB    1 
ATOM   1094 C CG    . ARG A 1 158 ? -25.271 19.057  -9.532  1.00 77.57  ? 139 ARG A CG    1 
ATOM   1095 C CD    . ARG A 1 158 ? -26.669 19.551  -9.873  1.00 88.01  ? 139 ARG A CD    1 
ATOM   1096 N NE    . ARG A 1 158 ? -27.598 19.190  -8.801  1.00 107.97 ? 139 ARG A NE    1 
ATOM   1097 C CZ    . ARG A 1 158 ? -28.510 19.994  -8.260  1.00 111.96 ? 139 ARG A CZ    1 
ATOM   1098 N NH1   . ARG A 1 158 ? -28.780 21.165  -8.811  1.00 116.48 ? 139 ARG A NH1   1 
ATOM   1099 N NH2   . ARG A 1 158 ? -29.181 19.600  -7.189  1.00 108.93 ? 139 ARG A NH2   1 
ATOM   1100 N N     . THR A 1 159 ? -25.789 15.246  -7.142  1.00 42.21  ? 140 THR A N     1 
ATOM   1101 C CA    . THR A 1 159 ? -26.531 14.007  -6.938  1.00 47.42  ? 140 THR A CA    1 
ATOM   1102 C C     . THR A 1 159 ? -27.995 14.371  -6.698  1.00 50.55  ? 140 THR A C     1 
ATOM   1103 O O     . THR A 1 159 ? -28.328 15.555  -6.672  1.00 45.98  ? 140 THR A O     1 
ATOM   1104 C CB    . THR A 1 159 ? -25.959 13.213  -5.757  1.00 52.12  ? 140 THR A CB    1 
ATOM   1105 O OG1   . THR A 1 159 ? -26.293 13.933  -4.566  1.00 55.13  ? 140 THR A OG1   1 
ATOM   1106 C CG2   . THR A 1 159 ? -24.459 13.006  -5.832  1.00 48.09  ? 140 THR A CG2   1 
ATOM   1107 N N     . SER A 1 160 ? -28.864 13.369  -6.520  1.00 49.61  ? 141 SER A N     1 
ATOM   1108 C CA    . SER A 1 160 ? -30.266 13.647  -6.230  1.00 61.75  ? 141 SER A CA    1 
ATOM   1109 C C     . SER A 1 160 ? -30.427 14.213  -4.812  1.00 69.67  ? 141 SER A C     1 
ATOM   1110 O O     . SER A 1 160 ? -31.442 14.842  -4.511  1.00 76.10  ? 141 SER A O     1 
ATOM   1111 C CB    . SER A 1 160 ? -31.157 12.441  -6.465  1.00 57.77  ? 141 SER A CB    1 
ATOM   1112 O OG    . SER A 1 160 ? -30.691 11.313  -5.746  1.00 60.29  ? 141 SER A OG    1 
ATOM   1113 N N     . ALA A 1 161 ? -29.436 14.001  -3.934  1.00 68.57  ? 142 ALA A N     1 
ATOM   1114 C CA    . ALA A 1 161 ? -29.382 14.771  -2.701  1.00 66.94  ? 142 ALA A CA    1 
ATOM   1115 C C     . ALA A 1 161 ? -29.192 16.242  -3.063  1.00 72.22  ? 142 ALA A C     1 
ATOM   1116 O O     . ALA A 1 161 ? -30.098 17.043  -2.861  1.00 85.57  ? 142 ALA A O     1 
ATOM   1117 C CB    . ALA A 1 161 ? -28.304 14.263  -1.779  1.00 61.07  ? 142 ALA A CB    1 
ATOM   1118 N N     . GLY A 1 162 ? -28.044 16.578  -3.659  1.00 64.22  ? 143 GLY A N     1 
ATOM   1119 C CA    . GLY A 1 162 ? -27.747 17.943  -4.061  1.00 60.92  ? 143 GLY A CA    1 
ATOM   1120 C C     . GLY A 1 162 ? -26.255 18.121  -4.334  1.00 63.61  ? 143 GLY A C     1 
ATOM   1121 O O     . GLY A 1 162 ? -25.553 17.151  -4.603  1.00 61.63  ? 143 GLY A O     1 
ATOM   1122 N N     . ASP A 1 163 ? -25.776 19.364  -4.229  1.00 56.00  ? 144 ASP A N     1 
ATOM   1123 C CA    . ASP A 1 163 ? -24.418 19.717  -4.610  1.00 56.36  ? 144 ASP A CA    1 
ATOM   1124 C C     . ASP A 1 163 ? -23.439 19.282  -3.519  1.00 58.50  ? 144 ASP A C     1 
ATOM   1125 O O     . ASP A 1 163 ? -23.792 19.228  -2.345  1.00 58.92  ? 144 ASP A O     1 
ATOM   1126 C CB    . ASP A 1 163 ? -24.334 21.212  -4.940  1.00 61.11  ? 144 ASP A CB    1 
ATOM   1127 C CG    . ASP A 1 163 ? -25.234 21.632  -6.100  1.00 75.28  ? 144 ASP A CG    1 
ATOM   1128 O OD1   . ASP A 1 163 ? -26.011 20.776  -6.601  1.00 76.41  ? 144 ASP A OD1   1 
ATOM   1129 O OD2   . ASP A 1 163 ? -25.152 22.812  -6.512  1.00 81.27  ? 144 ASP A OD2   1 
ATOM   1130 N N     . SER A 1 164 ? -22.213 18.925  -3.924  1.00 45.07  ? 145 SER A N     1 
ATOM   1131 C CA    . SER A 1 164 ? -21.156 18.569  -2.996  1.00 41.76  ? 145 SER A CA    1 
ATOM   1132 C C     . SER A 1 164 ? -19.786 18.718  -3.657  1.00 42.00  ? 145 SER A C     1 
ATOM   1133 O O     . SER A 1 164 ? -19.688 19.101  -4.821  1.00 41.97  ? 145 SER A O     1 
ATOM   1134 C CB    . SER A 1 164 ? -21.351 17.177  -2.440  1.00 46.71  ? 145 SER A CB    1 
ATOM   1135 O OG    . SER A 1 164 ? -21.158 16.190  -3.431  1.00 48.36  ? 145 SER A OG    1 
ATOM   1136 N N     . THR A 1 165 ? -18.742 18.379  -2.894  1.00 39.17  ? 146 THR A N     1 
ATOM   1137 C CA    . THR A 1 165 ? -17.362 18.573  -3.297  1.00 43.52  ? 146 THR A CA    1 
ATOM   1138 C C     . THR A 1 165 ? -16.627 17.258  -3.083  1.00 41.99  ? 146 THR A C     1 
ATOM   1139 O O     . THR A 1 165 ? -17.000 16.500  -2.191  1.00 41.75  ? 146 THR A O     1 
ATOM   1140 C CB    . THR A 1 165 ? -16.802 19.770  -2.513  1.00 48.40  ? 146 THR A CB    1 
ATOM   1141 O OG1   . THR A 1 165 ? -17.239 20.958  -3.174  1.00 56.33  ? 146 THR A OG1   1 
ATOM   1142 C CG2   . THR A 1 165 ? -15.299 19.797  -2.414  1.00 55.40  ? 146 THR A CG2   1 
ATOM   1143 N N     . LEU A 1 166 ? -15.575 17.002  -3.882  1.00 37.87  ? 147 LEU A N     1 
ATOM   1144 C CA    . LEU A 1 166 ? -14.729 15.835  -3.702  1.00 36.50  ? 147 LEU A CA    1 
ATOM   1145 C C     . LEU A 1 166 ? -13.299 16.222  -4.063  1.00 33.46  ? 147 LEU A C     1 
ATOM   1146 O O     . LEU A 1 166 ? -13.055 16.797  -5.117  1.00 40.00  ? 147 LEU A O     1 
ATOM   1147 C CB    . LEU A 1 166 ? -15.252 14.703  -4.598  1.00 43.50  ? 147 LEU A CB    1 
ATOM   1148 C CG    . LEU A 1 166 ? -15.031 13.268  -4.119  1.00 56.19  ? 147 LEU A CG    1 
ATOM   1149 C CD1   . LEU A 1 166 ? -13.657 13.072  -3.516  1.00 61.56  ? 147 LEU A CD1   1 
ATOM   1150 C CD2   . LEU A 1 166 ? -16.104 12.847  -3.115  1.00 58.91  ? 147 LEU A CD2   1 
ATOM   1151 N N     . ARG A 1 167 ? -12.371 15.870  -3.188  1.00 32.48  ? 148 ARG A N     1 
ATOM   1152 C CA    . ARG A 1 167 ? -10.967 16.196  -3.326  1.00 36.70  ? 148 ARG A CA    1 
ATOM   1153 C C     . ARG A 1 167 ? -10.246 14.946  -3.861  1.00 34.35  ? 148 ARG A C     1 
ATOM   1154 O O     . ARG A 1 167 ? -10.514 13.852  -3.383  1.00 32.12  ? 148 ARG A O     1 
ATOM   1155 C CB    . ARG A 1 167 ? -10.448 16.623  -1.947  1.00 41.03  ? 148 ARG A CB    1 
ATOM   1156 C CG    . ARG A 1 167 ? -8.935  16.686  -1.796  1.00 42.21  ? 148 ARG A CG    1 
ATOM   1157 C CD    . ARG A 1 167 ? -8.511  17.022  -0.370  1.00 43.58  ? 148 ARG A CD    1 
ATOM   1158 N NE    . ARG A 1 167 ? -7.075  16.859  -0.175  1.00 42.59  ? 148 ARG A NE    1 
ATOM   1159 C CZ    . ARG A 1 167 ? -6.216  17.862  0.009   1.00 42.11  ? 148 ARG A CZ    1 
ATOM   1160 N NH1   . ARG A 1 167 ? -4.919  17.640  -0.092  1.00 39.36  ? 148 ARG A NH1   1 
ATOM   1161 N NH2   . ARG A 1 167 ? -6.663  19.088  0.233   1.00 39.70  ? 148 ARG A NH2   1 
ATOM   1162 N N     . GLY A 1 168 ? -9.385  15.105  -4.876  1.00 31.78  ? 149 GLY A N     1 
ATOM   1163 C CA    . GLY A 1 168 ? -8.499  14.031  -5.326  1.00 30.88  ? 149 GLY A CA    1 
ATOM   1164 C C     . GLY A 1 168 ? -7.068  14.514  -5.535  1.00 29.12  ? 149 GLY A C     1 
ATOM   1165 O O     . GLY A 1 168 ? -6.793  15.719  -5.578  1.00 34.08  ? 149 GLY A O     1 
ATOM   1166 N N     . SER A 1 169 ? -6.139  13.563  -5.634  1.00 27.25  ? 150 SER A N     1 
ATOM   1167 C CA    . SER A 1 169 ? -4.768  13.845  -6.034  1.00 28.90  ? 150 SER A CA    1 
ATOM   1168 C C     . SER A 1 169 ? -4.720  14.192  -7.539  1.00 29.76  ? 150 SER A C     1 
ATOM   1169 O O     . SER A 1 169 ? -4.039  15.122  -7.962  1.00 29.91  ? 150 SER A O     1 
ATOM   1170 C CB    . SER A 1 169 ? -3.911  12.651  -5.718  1.00 29.88  ? 150 SER A CB    1 
ATOM   1171 O OG    . SER A 1 169 ? -4.545  11.459  -6.211  1.00 29.97  ? 150 SER A OG    1 
ATOM   1172 N N     . TYR A 1 170 ? -5.470  13.427  -8.338  1.00 27.47  ? 151 TYR A N     1 
ATOM   1173 C CA    . TYR A 1 170 ? -5.543  13.591  -9.793  1.00 27.64  ? 151 TYR A CA    1 
ATOM   1174 C C     . TYR A 1 170 ? -6.982  13.392  -10.223 1.00 26.71  ? 151 TYR A C     1 
ATOM   1175 O O     . TYR A 1 170 ? -7.762  12.668  -9.598  1.00 27.40  ? 151 TYR A O     1 
ATOM   1176 C CB    . TYR A 1 170 ? -4.633  12.577  -10.496 1.00 26.39  ? 151 TYR A CB    1 
ATOM   1177 C CG    . TYR A 1 170 ? -3.163  12.821  -10.294 1.00 26.63  ? 151 TYR A CG    1 
ATOM   1178 C CD1   . TYR A 1 170 ? -2.513  13.856  -10.945 1.00 29.78  ? 151 TYR A CD1   1 
ATOM   1179 C CD2   . TYR A 1 170 ? -2.425  12.075  -9.398  1.00 27.83  ? 151 TYR A CD2   1 
ATOM   1180 C CE1   . TYR A 1 170 ? -1.158  14.097  -10.759 1.00 31.21  ? 151 TYR A CE1   1 
ATOM   1181 C CE2   . TYR A 1 170 ? -1.070  12.305  -9.195  1.00 31.19  ? 151 TYR A CE2   1 
ATOM   1182 C CZ    . TYR A 1 170 ? -0.433  13.329  -9.874  1.00 32.27  ? 151 TYR A CZ    1 
ATOM   1183 O OH    . TYR A 1 170 ? 0.928   13.570  -9.695  1.00 33.80  ? 151 TYR A OH    1 
ATOM   1184 N N     . VAL A 1 171 ? -7.323  13.957  -11.374 1.00 26.12  ? 152 VAL A N     1 
ATOM   1185 C CA    . VAL A 1 171 ? -8.610  13.700  -11.968 1.00 27.64  ? 152 VAL A CA    1 
ATOM   1186 C C     . VAL A 1 171 ? -8.353  13.229  -13.397 1.00 26.77  ? 152 VAL A C     1 
ATOM   1187 O O     . VAL A 1 171 ? -7.530  13.828  -14.092 1.00 27.61  ? 152 VAL A O     1 
ATOM   1188 C CB    . VAL A 1 171 ? -9.483  14.964  -11.973 1.00 30.35  ? 152 VAL A CB    1 
ATOM   1189 C CG1   . VAL A 1 171 ? -10.767 14.747  -12.756 1.00 32.63  ? 152 VAL A CG1   1 
ATOM   1190 C CG2   . VAL A 1 171 ? -9.772  15.407  -10.548 1.00 36.56  ? 152 VAL A CG2   1 
ATOM   1191 N N     . VAL A 1 172 ? -9.003  12.127  -13.763 1.00 26.44  ? 153 VAL A N     1 
ATOM   1192 C CA    . VAL A 1 172 ? -8.941  11.630  -15.138 1.00 23.91  ? 153 VAL A CA    1 
ATOM   1193 C C     . VAL A 1 172 ? -10.321 11.708  -15.758 1.00 24.46  ? 153 VAL A C     1 
ATOM   1194 O O     . VAL A 1 172 ? -11.275 11.106  -15.266 1.00 27.05  ? 153 VAL A O     1 
ATOM   1195 C CB    . VAL A 1 172 ? -8.397  10.196  -15.202 1.00 24.02  ? 153 VAL A CB    1 
ATOM   1196 C CG1   . VAL A 1 172 ? -8.316  9.743   -16.657 1.00 27.44  ? 153 VAL A CG1   1 
ATOM   1197 C CG2   . VAL A 1 172 ? -7.043  10.073  -14.527 1.00 25.64  ? 153 VAL A CG2   1 
ATOM   1198 N N     . ALA A 1 173 ? -10.401 12.440  -16.873 1.00 25.45  ? 154 ALA A N     1 
ATOM   1199 C CA    . ALA A 1 173 ? -11.582 12.487  -17.706 1.00 24.75  ? 154 ALA A CA    1 
ATOM   1200 C C     . ALA A 1 173 ? -11.704 11.175  -18.482 1.00 27.49  ? 154 ALA A C     1 
ATOM   1201 O O     . ALA A 1 173 ? -10.938 10.932  -19.398 1.00 30.33  ? 154 ALA A O     1 
ATOM   1202 C CB    . ALA A 1 173 ? -11.471 13.633  -18.665 1.00 29.11  ? 154 ALA A CB    1 
ATOM   1203 N N     . ALA A 1 174 ? -12.687 10.366  -18.118 1.00 24.91  ? 155 ALA A N     1 
ATOM   1204 C CA    . ALA A 1 174 ? -13.077 9.200   -18.885 1.00 25.01  ? 155 ALA A CA    1 
ATOM   1205 C C     . ALA A 1 174 ? -14.554 9.330   -19.191 1.00 22.92  ? 155 ALA A C     1 
ATOM   1206 O O     . ALA A 1 174 ? -15.316 8.346   -19.175 1.00 26.80  ? 155 ALA A O     1 
ATOM   1207 C CB    . ALA A 1 174 ? -12.776 7.951   -18.114 1.00 25.38  ? 155 ALA A CB    1 
ATOM   1208 N N     . ASP A 1 175 ? -14.935 10.568  -19.512 1.00 26.98  ? 156 ASP A N     1 
ATOM   1209 C CA    . ASP A 1 175 ? -16.345 10.903  -19.575 1.00 30.11  ? 156 ASP A CA    1 
ATOM   1210 C C     . ASP A 1 175 ? -16.851 11.019  -21.012 1.00 30.76  ? 156 ASP A C     1 
ATOM   1211 O O     . ASP A 1 175 ? -17.831 11.706  -21.255 1.00 30.27  ? 156 ASP A O     1 
ATOM   1212 C CB    . ASP A 1 175 ? -16.651 12.167  -18.762 1.00 32.56  ? 156 ASP A CB    1 
ATOM   1213 C CG    . ASP A 1 175 ? -15.817 13.406  -19.054 1.00 40.53  ? 156 ASP A CG    1 
ATOM   1214 O OD1   . ASP A 1 175 ? -14.795 13.300  -19.775 1.00 34.33  ? 156 ASP A OD1   1 
ATOM   1215 O OD2   . ASP A 1 175 ? -16.208 14.497  -18.544 1.00 41.03  ? 156 ASP A OD2   1 
ATOM   1216 N N     . GLY A 1 176 ? -16.200 10.350  -21.975 1.00 26.54  ? 157 GLY A N     1 
ATOM   1217 C CA    . GLY A 1 176 ? -16.759 10.254  -23.306 1.00 27.51  ? 157 GLY A CA    1 
ATOM   1218 C C     . GLY A 1 176 ? -16.458 11.437  -24.221 1.00 27.56  ? 157 GLY A C     1 
ATOM   1219 O O     . GLY A 1 176 ? -15.727 12.379  -23.883 1.00 28.54  ? 157 GLY A O     1 
ATOM   1220 N N     . ALA A 1 177 ? -16.999 11.305  -25.438 1.00 28.96  ? 158 ALA A N     1 
ATOM   1221 C CA    . ALA A 1 177 ? -16.584 12.105  -26.573 1.00 30.55  ? 158 ALA A CA    1 
ATOM   1222 C C     . ALA A 1 177 ? -16.969 13.574  -26.375 1.00 35.41  ? 158 ALA A C     1 
ATOM   1223 O O     . ALA A 1 177 ? -16.273 14.462  -26.865 1.00 35.83  ? 158 ALA A O     1 
ATOM   1224 C CB    . ALA A 1 177 ? -17.197 11.519  -27.826 1.00 36.10  ? 158 ALA A CB    1 
ATOM   1225 N N     . GLY A 1 178 ? -18.058 13.818  -25.635 1.00 34.62  ? 159 GLY A N     1 
ATOM   1226 C CA    . GLY A 1 178 ? -18.463 15.189  -25.342 1.00 39.71  ? 159 GLY A CA    1 
ATOM   1227 C C     . GLY A 1 178 ? -17.894 15.702  -24.019 1.00 40.60  ? 159 GLY A C     1 
ATOM   1228 O O     . GLY A 1 178 ? -18.346 16.736  -23.539 1.00 40.63  ? 159 GLY A O     1 
ATOM   1229 N N     . SER A 1 179 ? -16.849 15.033  -23.492 1.00 35.78  ? 160 SER A N     1 
ATOM   1230 C CA    . SER A 1 179 ? -16.253 15.245  -22.173 1.00 36.70  ? 160 SER A CA    1 
ATOM   1231 C C     . SER A 1 179 ? -16.552 16.598  -21.501 1.00 36.00  ? 160 SER A C     1 
ATOM   1232 O O     . SER A 1 179 ? -16.024 17.631  -21.915 1.00 32.33  ? 160 SER A O     1 
ATOM   1233 C CB    . SER A 1 179 ? -14.771 15.091  -22.252 1.00 35.94  ? 160 SER A CB    1 
ATOM   1234 O OG    . SER A 1 179 ? -14.192 15.299  -20.979 1.00 33.44  ? 160 SER A OG    1 
ATOM   1235 N N     . THR A 1 180 ? -17.294 16.548  -20.379 1.00 37.06  ? 161 THR A N     1 
ATOM   1236 C CA    . THR A 1 180 ? -17.438 17.686  -19.468 1.00 33.85  ? 161 THR A CA    1 
ATOM   1237 C C     . THR A 1 180 ? -16.072 18.195  -19.002 1.00 34.53  ? 161 THR A C     1 
ATOM   1238 O O     . THR A 1 180 ? -15.780 19.394  -19.056 1.00 34.32  ? 161 THR A O     1 
ATOM   1239 C CB    . THR A 1 180 ? -18.288 17.291  -18.255 1.00 34.48  ? 161 THR A CB    1 
ATOM   1240 O OG1   . THR A 1 180 ? -19.532 16.738  -18.680 1.00 34.68  ? 161 THR A OG1   1 
ATOM   1241 C CG2   . THR A 1 180 ? -18.560 18.448  -17.321 1.00 39.07  ? 161 THR A CG2   1 
ATOM   1242 N N     . VAL A 1 181 ? -15.217 17.262  -18.550 1.00 29.76  ? 162 VAL A N     1 
ATOM   1243 C CA    . VAL A 1 181 ? -13.934 17.603  -17.980 1.00 32.27  ? 162 VAL A CA    1 
ATOM   1244 C C     . VAL A 1 181 ? -13.029 18.259  -19.001 1.00 33.33  ? 162 VAL A C     1 
ATOM   1245 O O     . VAL A 1 181 ? -12.275 19.149  -18.634 1.00 32.84  ? 162 VAL A O     1 
ATOM   1246 C CB    . VAL A 1 181 ? -13.269 16.373  -17.331 1.00 33.11  ? 162 VAL A CB    1 
ATOM   1247 C CG1   . VAL A 1 181 ? -11.863 16.662  -16.840 1.00 32.93  ? 162 VAL A CG1   1 
ATOM   1248 C CG2   . VAL A 1 181 ? -14.120 15.836  -16.200 1.00 36.91  ? 162 VAL A CG2   1 
ATOM   1249 N N     . ARG A 1 182 ? -13.013 17.770  -20.253 1.00 32.12  ? 163 ARG A N     1 
ATOM   1250 C CA    . ARG A 1 182 ? -12.134 18.370  -21.238 1.00 31.04  ? 163 ARG A CA    1 
ATOM   1251 C C     . ARG A 1 182 ? -12.534 19.839  -21.426 1.00 27.40  ? 163 ARG A C     1 
ATOM   1252 O O     . ARG A 1 182 ? -11.669 20.696  -21.523 1.00 30.42  ? 163 ARG A O     1 
ATOM   1253 C CB    . ARG A 1 182 ? -12.236 17.632  -22.582 1.00 30.88  ? 163 ARG A CB    1 
ATOM   1254 C CG    . ARG A 1 182 ? -11.322 18.158  -23.678 1.00 31.04  ? 163 ARG A CG    1 
ATOM   1255 C CD    . ARG A 1 182 ? -11.544 17.493  -25.039 1.00 30.97  ? 163 ARG A CD    1 
ATOM   1256 N NE    . ARG A 1 182 ? -12.897 17.650  -25.573 1.00 30.33  ? 163 ARG A NE    1 
ATOM   1257 C CZ    . ARG A 1 182 ? -13.739 16.681  -25.933 1.00 32.79  ? 163 ARG A CZ    1 
ATOM   1258 N NH1   . ARG A 1 182 ? -13.432 15.401  -25.801 1.00 33.94  ? 163 ARG A NH1   1 
ATOM   1259 N NH2   . ARG A 1 182 ? -14.931 16.993  -26.407 1.00 34.16  ? 163 ARG A NH2   1 
ATOM   1260 N N     . ARG A 1 183 ? -13.839 20.088  -21.466 1.00 32.62  ? 164 ARG A N     1 
ATOM   1261 C CA    . ARG A 1 183 ? -14.350 21.445  -21.610 1.00 33.59  ? 164 ARG A CA    1 
ATOM   1262 C C     . ARG A 1 183 ? -14.000 22.286  -20.372 1.00 38.66  ? 164 ARG A C     1 
ATOM   1263 O O     . ARG A 1 183 ? -13.514 23.407  -20.521 1.00 37.96  ? 164 ARG A O     1 
ATOM   1264 C CB    . ARG A 1 183 ? -15.840 21.383  -21.950 1.00 36.29  ? 164 ARG A CB    1 
ATOM   1265 C CG    . ARG A 1 183 ? -16.101 20.833  -23.350 1.00 41.83  ? 164 ARG A CG    1 
ATOM   1266 C CD    . ARG A 1 183 ? -17.566 20.765  -23.712 1.00 42.70  ? 164 ARG A CD    1 
ATOM   1267 N NE    . ARG A 1 183 ? -18.196 19.587  -23.150 1.00 42.71  ? 164 ARG A NE    1 
ATOM   1268 C CZ    . ARG A 1 183 ? -19.444 19.518  -22.700 1.00 47.28  ? 164 ARG A CZ    1 
ATOM   1269 N NH1   . ARG A 1 183 ? -19.856 18.436  -22.068 1.00 42.82  ? 164 ARG A NH1   1 
ATOM   1270 N NH2   . ARG A 1 183 ? -20.280 20.531  -22.861 1.00 53.57  ? 164 ARG A NH2   1 
ATOM   1271 N N     . LEU A 1 184 ? -14.154 21.733  -19.155 1.00 38.55  ? 165 LEU A N     1 
ATOM   1272 C CA    . LEU A 1 184 ? -13.850 22.491  -17.942 1.00 36.78  ? 165 LEU A CA    1 
ATOM   1273 C C     . LEU A 1 184 ? -12.366 22.829  -17.880 1.00 38.87  ? 165 LEU A C     1 
ATOM   1274 O O     . LEU A 1 184 ? -12.001 23.846  -17.312 1.00 37.63  ? 165 LEU A O     1 
ATOM   1275 C CB    . LEU A 1 184 ? -14.252 21.728  -16.676 1.00 33.71  ? 165 LEU A CB    1 
ATOM   1276 C CG    . LEU A 1 184 ? -15.742 21.496  -16.455 1.00 40.45  ? 165 LEU A CG    1 
ATOM   1277 C CD1   . LEU A 1 184 ? -15.954 20.435  -15.386 1.00 39.57  ? 165 LEU A CD1   1 
ATOM   1278 C CD2   . LEU A 1 184 ? -16.471 22.780  -16.057 1.00 41.68  ? 165 LEU A CD2   1 
ATOM   1279 N N     . ALA A 1 185 ? -11.505 21.987  -18.469 1.00 37.63  ? 166 ALA A N     1 
ATOM   1280 C CA    . ALA A 1 185 ? -10.070 22.230  -18.468 1.00 35.47  ? 166 ALA A CA    1 
ATOM   1281 C C     . ALA A 1 185 ? -9.639  23.149  -19.604 1.00 32.00  ? 166 ALA A C     1 
ATOM   1282 O O     . ALA A 1 185 ? -8.445  23.415  -19.735 1.00 35.96  ? 166 ALA A O     1 
ATOM   1283 C CB    . ALA A 1 185 ? -9.333  20.918  -18.552 1.00 36.56  ? 166 ALA A CB    1 
ATOM   1284 N N     . GLY A 1 186 ? -10.598 23.547  -20.449 1.00 34.88  ? 167 GLY A N     1 
ATOM   1285 C CA    . GLY A 1 186 ? -10.380 24.426  -21.586 1.00 37.41  ? 167 GLY A CA    1 
ATOM   1286 C C     . GLY A 1 186 ? -9.464  23.794  -22.636 1.00 40.69  ? 167 GLY A C     1 
ATOM   1287 O O     . GLY A 1 186 ? -8.629  24.481  -23.204 1.00 38.43  ? 167 GLY A O     1 
ATOM   1288 N N     . ILE A 1 187 ? -9.553  22.466  -22.842 1.00 36.85  ? 168 ILE A N     1 
ATOM   1289 C CA    . ILE A 1 187 ? -8.670  21.813  -23.799 1.00 34.84  ? 168 ILE A CA    1 
ATOM   1290 C C     . ILE A 1 187 ? -9.414  21.686  -25.136 1.00 31.95  ? 168 ILE A C     1 
ATOM   1291 O O     . ILE A 1 187 ? -10.530 21.178  -25.209 1.00 36.38  ? 168 ILE A O     1 
ATOM   1292 C CB    . ILE A 1 187 ? -8.155  20.456  -23.258 1.00 33.13  ? 168 ILE A CB    1 
ATOM   1293 C CG1   . ILE A 1 187 ? -7.194  20.646  -22.080 1.00 36.88  ? 168 ILE A CG1   1 
ATOM   1294 C CG2   . ILE A 1 187 ? -7.525  19.664  -24.389 1.00 32.71  ? 168 ILE A CG2   1 
ATOM   1295 C CD1   . ILE A 1 187 ? -6.803  19.372  -21.356 1.00 35.74  ? 168 ILE A CD1   1 
ATOM   1296 N N     . ASP A 1 188 ? -8.766  22.144  -26.208 1.00 30.79  ? 169 ASP A N     1 
ATOM   1297 C CA    . ASP A 1 188 ? -9.353  22.125  -27.535 1.00 33.51  ? 169 ASP A CA    1 
ATOM   1298 C C     . ASP A 1 188 ? -9.282  20.705  -28.095 1.00 33.30  ? 169 ASP A C     1 
ATOM   1299 O O     . ASP A 1 188 ? -8.385  19.929  -27.741 1.00 32.50  ? 169 ASP A O     1 
ATOM   1300 C CB    . ASP A 1 188 ? -8.681  23.116  -28.488 1.00 36.54  ? 169 ASP A CB    1 
ATOM   1301 C CG    . ASP A 1 188 ? -8.862  24.580  -28.091 1.00 45.21  ? 169 ASP A CG    1 
ATOM   1302 O OD1   . ASP A 1 188 ? -9.966  24.934  -27.593 1.00 46.12  ? 169 ASP A OD1   1 
ATOM   1303 O OD2   . ASP A 1 188 ? -7.932  25.365  -28.347 1.00 52.05  ? 169 ASP A OD2   1 
ATOM   1304 N N     . PHE A 1 189 ? -10.211 20.433  -29.006 1.00 30.75  ? 170 PHE A N     1 
ATOM   1305 C CA    . PHE A 1 189 ? -10.400 19.111  -29.594 1.00 30.11  ? 170 PHE A CA    1 
ATOM   1306 C C     . PHE A 1 189 ? -10.387 19.232  -31.119 1.00 30.53  ? 170 PHE A C     1 
ATOM   1307 O O     . PHE A 1 189 ? -11.416 19.093  -31.749 1.00 29.65  ? 170 PHE A O     1 
ATOM   1308 C CB    . PHE A 1 189 ? -11.721 18.585  -29.058 1.00 30.74  ? 170 PHE A CB    1 
ATOM   1309 C CG    . PHE A 1 189 ? -11.966 17.102  -29.151 1.00 31.24  ? 170 PHE A CG    1 
ATOM   1310 C CD1   . PHE A 1 189 ? -11.084 16.203  -28.589 1.00 31.05  ? 170 PHE A CD1   1 
ATOM   1311 C CD2   . PHE A 1 189 ? -13.138 16.623  -29.697 1.00 31.70  ? 170 PHE A CD2   1 
ATOM   1312 C CE1   . PHE A 1 189 ? -11.360 14.841  -28.597 1.00 30.54  ? 170 PHE A CE1   1 
ATOM   1313 C CE2   . PHE A 1 189 ? -13.399 15.260  -29.735 1.00 33.55  ? 170 PHE A CE2   1 
ATOM   1314 C CZ    . PHE A 1 189 ? -12.516 14.375  -29.170 1.00 31.57  ? 170 PHE A CZ    1 
ATOM   1315 N N     . PRO A 1 190 ? -9.254  19.560  -31.761 1.00 28.11  ? 171 PRO A N     1 
ATOM   1316 C CA    . PRO A 1 190 ? -9.253  19.738  -33.218 1.00 32.96  ? 171 PRO A CA    1 
ATOM   1317 C C     . PRO A 1 190 ? -9.361  18.428  -34.014 1.00 34.01  ? 171 PRO A C     1 
ATOM   1318 O O     . PRO A 1 190 ? -8.921  17.385  -33.540 1.00 28.31  ? 171 PRO A O     1 
ATOM   1319 C CB    . PRO A 1 190 ? -7.875  20.347  -33.449 1.00 33.10  ? 171 PRO A CB    1 
ATOM   1320 C CG    . PRO A 1 190 ? -7.017  19.749  -32.345 1.00 34.05  ? 171 PRO A CG    1 
ATOM   1321 C CD    . PRO A 1 190 ? -7.928  19.726  -31.148 1.00 32.26  ? 171 PRO A CD    1 
ATOM   1322 N N     . GLY A 1 191 ? -9.827  18.522  -35.271 1.00 33.25  ? 172 GLY A N     1 
ATOM   1323 C CA    . GLY A 1 191 ? -9.804  17.408  -36.208 1.00 32.18  ? 172 GLY A CA    1 
ATOM   1324 C C     . GLY A 1 191 ? -10.047 17.889  -37.636 1.00 32.64  ? 172 GLY A C     1 
ATOM   1325 O O     . GLY A 1 191 ? -9.877  19.057  -37.935 1.00 31.43  ? 172 GLY A O     1 
ATOM   1326 N N     . SER A 1 192 ? -10.540 16.986  -38.484 1.00 29.56  ? 173 SER A N     1 
ATOM   1327 C CA    . SER A 1 192 ? -10.481 17.139  -39.932 1.00 30.36  ? 173 SER A CA    1 
ATOM   1328 C C     . SER A 1 192 ? -11.768 17.735  -40.495 1.00 33.65  ? 173 SER A C     1 
ATOM   1329 O O     . SER A 1 192 ? -11.851 18.062  -41.696 1.00 33.01  ? 173 SER A O     1 
ATOM   1330 C CB    . SER A 1 192 ? -10.255 15.772  -40.532 1.00 29.99  ? 173 SER A CB    1 
ATOM   1331 O OG    . SER A 1 192 ? -11.293 14.893  -40.064 1.00 29.93  ? 173 SER A OG    1 
ATOM   1332 N N     . GLY A 1 193 ? -12.802 17.759  -39.658 1.00 33.86  ? 174 GLY A N     1 
ATOM   1333 C CA    . GLY A 1 193 ? -14.120 18.141  -40.116 1.00 35.04  ? 174 GLY A CA    1 
ATOM   1334 C C     . GLY A 1 193 ? -14.978 16.956  -40.530 1.00 35.58  ? 174 GLY A C     1 
ATOM   1335 O O     . GLY A 1 193 ? -16.136 17.144  -40.854 1.00 33.58  ? 174 GLY A O     1 
ATOM   1336 N N     . TRP A 1 194 ? -14.438 15.726  -40.563 1.00 30.08  ? 175 TRP A N     1 
ATOM   1337 C CA    . TRP A 1 194 ? -15.318 14.602  -40.774 1.00 29.87  ? 175 TRP A CA    1 
ATOM   1338 C C     . TRP A 1 194 ? -16.314 14.532  -39.624 1.00 31.91  ? 175 TRP A C     1 
ATOM   1339 O O     . TRP A 1 194 ? -15.946 14.397  -38.476 1.00 34.05  ? 175 TRP A O     1 
ATOM   1340 C CB    . TRP A 1 194 ? -14.530 13.292  -40.942 1.00 28.42  ? 175 TRP A CB    1 
ATOM   1341 C CG    . TRP A 1 194 ? -13.997 13.071  -42.326 1.00 26.66  ? 175 TRP A CG    1 
ATOM   1342 C CD1   . TRP A 1 194 ? -12.705 13.243  -42.730 1.00 29.04  ? 175 TRP A CD1   1 
ATOM   1343 C CD2   . TRP A 1 194 ? -14.705 12.541  -43.456 1.00 26.99  ? 175 TRP A CD2   1 
ATOM   1344 N NE1   . TRP A 1 194 ? -12.577 12.910  -44.056 1.00 29.30  ? 175 TRP A NE1   1 
ATOM   1345 C CE2   . TRP A 1 194 ? -13.793 12.481  -44.522 1.00 28.02  ? 175 TRP A CE2   1 
ATOM   1346 C CE3   . TRP A 1 194 ? -16.034 12.157  -43.685 1.00 27.78  ? 175 TRP A CE3   1 
ATOM   1347 C CZ2   . TRP A 1 194 ? -14.165 12.055  -45.794 1.00 27.89  ? 175 TRP A CZ2   1 
ATOM   1348 C CZ3   . TRP A 1 194 ? -16.399 11.723  -44.937 1.00 30.08  ? 175 TRP A CZ3   1 
ATOM   1349 C CH2   . TRP A 1 194 ? -15.461 11.652  -45.968 1.00 29.60  ? 175 TRP A CH2   1 
ATOM   1350 N N     . THR A 1 195 ? -17.578 14.723  -39.957 1.00 31.79  ? 176 THR A N     1 
ATOM   1351 C CA    . THR A 1 195 ? -18.662 14.559  -39.021 1.00 33.12  ? 176 THR A CA    1 
ATOM   1352 C C     . THR A 1 195 ? -19.599 13.596  -39.731 1.00 36.01  ? 176 THR A C     1 
ATOM   1353 O O     . THR A 1 195 ? -20.011 13.848  -40.858 1.00 43.29  ? 176 THR A O     1 
ATOM   1354 C CB    . THR A 1 195 ? -19.292 15.924  -38.696 1.00 36.30  ? 176 THR A CB    1 
ATOM   1355 O OG1   . THR A 1 195 ? -18.248 16.760  -38.179 1.00 37.48  ? 176 THR A OG1   1 
ATOM   1356 C CG2   . THR A 1 195 ? -20.426 15.866  -37.700 1.00 43.94  ? 176 THR A CG2   1 
ATOM   1357 N N     . VAL A 1 196 ? -19.855 12.452  -39.125 1.00 32.63  ? 177 VAL A N     1 
ATOM   1358 C CA    . VAL A 1 196 ? -20.600 11.430  -39.830 1.00 33.11  ? 177 VAL A CA    1 
ATOM   1359 C C     . VAL A 1 196 ? -21.720 10.957  -38.923 1.00 35.12  ? 177 VAL A C     1 
ATOM   1360 O O     . VAL A 1 196 ? -21.445 10.510  -37.810 1.00 34.21  ? 177 VAL A O     1 
ATOM   1361 C CB    . VAL A 1 196 ? -19.705 10.242  -40.226 1.00 34.24  ? 177 VAL A CB    1 
ATOM   1362 C CG1   . VAL A 1 196 ? -20.541 9.156   -40.882 1.00 32.97  ? 177 VAL A CG1   1 
ATOM   1363 C CG2   . VAL A 1 196 ? -18.548 10.692  -41.101 1.00 36.00  ? 177 VAL A CG2   1 
ATOM   1364 N N     . SER A 1 197 ? -22.927 10.920  -39.493 1.00 31.74  ? 178 SER A N     1 
ATOM   1365 C CA    . SER A 1 197 ? -24.134 10.630  -38.752 1.00 35.20  ? 178 SER A CA    1 
ATOM   1366 C C     . SER A 1 197 ? -24.643 9.238   -39.125 1.00 31.64  ? 178 SER A C     1 
ATOM   1367 O O     . SER A 1 197 ? -24.411 8.750   -40.226 1.00 35.96  ? 178 SER A O     1 
ATOM   1368 C CB    . SER A 1 197 ? -25.142 11.723  -39.025 1.00 40.74  ? 178 SER A CB    1 
ATOM   1369 O OG    . SER A 1 197 ? -26.402 11.362  -38.500 1.00 56.18  ? 178 SER A OG    1 
ATOM   1370 N N     . GLY A 1 198 ? -25.335 8.601   -38.195 1.00 30.73  ? 179 GLY A N     1 
ATOM   1371 C CA    . GLY A 1 198 ? -25.924 7.299   -38.434 1.00 28.81  ? 179 GLY A CA    1 
ATOM   1372 C C     . GLY A 1 198 ? -27.082 7.018   -37.494 1.00 30.66  ? 179 GLY A C     1 
ATOM   1373 O O     . GLY A 1 198 ? -27.429 7.824   -36.620 1.00 31.62  ? 179 GLY A O     1 
ATOM   1374 N N     . ILE A 1 199 ? -27.675 5.840   -37.688 1.00 26.11  ? 180 ILE A N     1 
ATOM   1375 C CA    . ILE A 1 199 ? -28.626 5.298   -36.748 1.00 27.89  ? 180 ILE A CA    1 
ATOM   1376 C C     . ILE A 1 199 ? -28.060 3.996   -36.203 1.00 29.30  ? 180 ILE A C     1 
ATOM   1377 O O     . ILE A 1 199 ? -27.568 3.184   -36.979 1.00 28.75  ? 180 ILE A O     1 
ATOM   1378 C CB    . ILE A 1 199 ? -29.986 5.012   -37.407 1.00 31.29  ? 180 ILE A CB    1 
ATOM   1379 C CG1   . ILE A 1 199 ? -30.622 6.281   -37.974 1.00 38.87  ? 180 ILE A CG1   1 
ATOM   1380 C CG2   . ILE A 1 199 ? -30.928 4.325   -36.440 1.00 33.10  ? 180 ILE A CG2   1 
ATOM   1381 C CD1   . ILE A 1 199 ? -31.772 5.998   -38.923 1.00 40.13  ? 180 ILE A CD1   1 
ATOM   1382 N N     . VAL A 1 200 ? -28.180 3.816   -34.895 1.00 27.87  ? 181 VAL A N     1 
ATOM   1383 C CA    . VAL A 1 200 ? -27.910 2.538   -34.255 1.00 30.04  ? 181 VAL A CA    1 
ATOM   1384 C C     . VAL A 1 200 ? -29.177 2.121   -33.518 1.00 34.94  ? 181 VAL A C     1 
ATOM   1385 O O     . VAL A 1 200 ? -29.895 2.978   -32.980 1.00 31.65  ? 181 VAL A O     1 
ATOM   1386 C CB    . VAL A 1 200 ? -26.694 2.600   -33.307 1.00 29.72  ? 181 VAL A CB    1 
ATOM   1387 C CG1   . VAL A 1 200 ? -26.877 3.555   -32.133 1.00 30.41  ? 181 VAL A CG1   1 
ATOM   1388 C CG2   . VAL A 1 200 ? -26.336 1.222   -32.770 1.00 27.99  ? 181 VAL A CG2   1 
ATOM   1389 N N     . GLY A 1 201 ? -29.434 0.813   -33.529 1.00 30.61  ? 182 GLY A N     1 
ATOM   1390 C CA    . GLY A 1 201 ? -30.541 0.238   -32.788 1.00 32.49  ? 182 GLY A CA    1 
ATOM   1391 C C     . GLY A 1 201 ? -30.507 -1.288  -32.793 1.00 32.64  ? 182 GLY A C     1 
ATOM   1392 O O     . GLY A 1 201 ? -29.646 -1.895  -33.406 1.00 29.00  ? 182 GLY A O     1 
ATOM   1393 N N     . ASP A 1 202 ? -31.467 -1.870  -32.071 1.00 32.45  ? 183 ASP A N     1 
ATOM   1394 C CA    . ASP A 1 202 ? -31.626 -3.301  -31.903 1.00 31.95  ? 183 ASP A CA    1 
ATOM   1395 C C     . ASP A 1 202 ? -33.025 -3.618  -32.400 1.00 35.84  ? 183 ASP A C     1 
ATOM   1396 O O     . ASP A 1 202 ? -33.965 -2.883  -32.072 1.00 33.28  ? 183 ASP A O     1 
ATOM   1397 C CB    . ASP A 1 202 ? -31.511 -3.738  -30.439 1.00 34.18  ? 183 ASP A CB    1 
ATOM   1398 C CG    . ASP A 1 202 ? -30.097 -3.820  -29.891 1.00 37.94  ? 183 ASP A CG    1 
ATOM   1399 O OD1   . ASP A 1 202 ? -29.149 -3.788  -30.686 1.00 38.37  ? 183 ASP A OD1   1 
ATOM   1400 O OD2   . ASP A 1 202 ? -29.970 -3.961  -28.680 1.00 43.27  ? 183 ASP A OD2   1 
ATOM   1401 N N     . VAL A 1 203 ? -33.108 -4.673  -33.216 1.00 30.18  ? 184 VAL A N     1 
ATOM   1402 C CA    . VAL A 1 203 ? -34.331 -5.083  -33.863 1.00 34.68  ? 184 VAL A CA    1 
ATOM   1403 C C     . VAL A 1 203 ? -34.562 -6.555  -33.542 1.00 36.32  ? 184 VAL A C     1 
ATOM   1404 O O     . VAL A 1 203 ? -33.640 -7.350  -33.640 1.00 30.00  ? 184 VAL A O     1 
ATOM   1405 C CB    . VAL A 1 203 ? -34.227 -4.884  -35.383 1.00 35.14  ? 184 VAL A CB    1 
ATOM   1406 C CG1   . VAL A 1 203 ? -35.509 -5.288  -36.090 1.00 42.03  ? 184 VAL A CG1   1 
ATOM   1407 C CG2   . VAL A 1 203 ? -33.852 -3.457  -35.736 1.00 36.02  ? 184 VAL A CG2   1 
ATOM   1408 N N     . THR A 1 204 ? -35.810 -6.902  -33.217 1.00 38.70  ? 185 THR A N     1 
ATOM   1409 C CA    . THR A 1 204 ? -36.214 -8.292  -33.040 1.00 39.86  ? 185 THR A CA    1 
ATOM   1410 C C     . THR A 1 204 ? -36.404 -8.926  -34.411 1.00 39.25  ? 185 THR A C     1 
ATOM   1411 O O     . THR A 1 204 ? -37.140 -8.376  -35.244 1.00 37.17  ? 185 THR A O     1 
ATOM   1412 C CB    . THR A 1 204 ? -37.500 -8.394  -32.204 1.00 40.86  ? 185 THR A CB    1 
ATOM   1413 O OG1   . THR A 1 204 ? -37.280 -7.769  -30.943 1.00 43.42  ? 185 THR A OG1   1 
ATOM   1414 C CG2   . THR A 1 204 ? -37.927 -9.825  -31.953 1.00 49.11  ? 185 THR A CG2   1 
ATOM   1415 N N     . VAL A 1 205 ? -35.732 -10.073 -34.640 1.00 33.35  ? 186 VAL A N     1 
ATOM   1416 C CA    . VAL A 1 205 ? -35.782 -10.751 -35.918 1.00 36.79  ? 186 VAL A CA    1 
ATOM   1417 C C     . VAL A 1 205 ? -35.826 -12.256 -35.677 1.00 39.45  ? 186 VAL A C     1 
ATOM   1418 O O     . VAL A 1 205 ? -35.449 -12.727 -34.609 1.00 38.20  ? 186 VAL A O     1 
ATOM   1419 C CB    . VAL A 1 205 ? -34.578 -10.397 -36.805 1.00 35.89  ? 186 VAL A CB    1 
ATOM   1420 C CG1   . VAL A 1 205 ? -34.637 -8.962  -37.300 1.00 42.64  ? 186 VAL A CG1   1 
ATOM   1421 C CG2   . VAL A 1 205 ? -33.264 -10.664 -36.084 1.00 40.87  ? 186 VAL A CG2   1 
ATOM   1422 N N     . ASP A 1 206 ? -36.321 -12.977 -36.680 1.00 41.63  ? 187 ASP A N     1 
ATOM   1423 C CA    . ASP A 1 206 ? -36.015 -14.393 -36.858 1.00 41.85  ? 187 ASP A CA    1 
ATOM   1424 C C     . ASP A 1 206 ? -34.768 -14.466 -37.734 1.00 36.30  ? 187 ASP A C     1 
ATOM   1425 O O     . ASP A 1 206 ? -34.826 -14.138 -38.916 1.00 40.00  ? 187 ASP A O     1 
ATOM   1426 C CB    . ASP A 1 206 ? -37.218 -15.105 -37.485 1.00 42.96  ? 187 ASP A CB    1 
ATOM   1427 C CG    . ASP A 1 206 ? -36.977 -16.497 -38.058 1.00 53.30  ? 187 ASP A CG    1 
ATOM   1428 O OD1   . ASP A 1 206 ? -35.806 -16.961 -38.099 1.00 53.37  ? 187 ASP A OD1   1 
ATOM   1429 O OD2   . ASP A 1 206 ? -37.974 -17.109 -38.479 1.00 50.40  ? 187 ASP A OD2   1 
ATOM   1430 N N     . PHE A 1 207 ? -33.617 -14.872 -37.176 1.00 38.75  ? 188 PHE A N     1 
ATOM   1431 C CA    . PHE A 1 207 ? -32.379 -14.814 -37.954 1.00 39.62  ? 188 PHE A CA    1 
ATOM   1432 C C     . PHE A 1 207 ? -32.439 -15.620 -39.264 1.00 45.13  ? 188 PHE A C     1 
ATOM   1433 O O     . PHE A 1 207 ? -31.753 -15.275 -40.235 1.00 40.64  ? 188 PHE A O     1 
ATOM   1434 C CB    . PHE A 1 207 ? -31.188 -15.304 -37.128 1.00 41.51  ? 188 PHE A CB    1 
ATOM   1435 C CG    . PHE A 1 207 ? -30.823 -14.425 -35.957 1.00 36.07  ? 188 PHE A CG    1 
ATOM   1436 C CD1   . PHE A 1 207 ? -30.362 -13.129 -36.166 1.00 36.02  ? 188 PHE A CD1   1 
ATOM   1437 C CD2   . PHE A 1 207 ? -30.922 -14.889 -34.657 1.00 33.02  ? 188 PHE A CD2   1 
ATOM   1438 C CE1   . PHE A 1 207 ? -30.026 -12.312 -35.100 1.00 33.21  ? 188 PHE A CE1   1 
ATOM   1439 C CE2   . PHE A 1 207 ? -30.589 -14.074 -33.589 1.00 33.36  ? 188 PHE A CE2   1 
ATOM   1440 C CZ    . PHE A 1 207 ? -30.153 -12.780 -33.807 1.00 34.07  ? 188 PHE A CZ    1 
ATOM   1441 N N     . SER A 1 208 ? -33.227 -16.710 -39.304 1.00 47.06  ? 189 SER A N     1 
ATOM   1442 C CA    . SER A 1 208 ? -33.336 -17.526 -40.513 1.00 50.31  ? 189 SER A CA    1 
ATOM   1443 C C     . SER A 1 208 ? -33.987 -16.749 -41.665 1.00 50.85  ? 189 SER A C     1 
ATOM   1444 O O     . SER A 1 208 ? -33.729 -17.028 -42.838 1.00 47.32  ? 189 SER A O     1 
ATOM   1445 C CB    . SER A 1 208 ? -34.089 -18.812 -40.226 1.00 52.06  ? 189 SER A CB    1 
ATOM   1446 O OG    . SER A 1 208 ? -35.485 -18.563 -40.102 1.00 54.68  ? 189 SER A OG    1 
ATOM   1447 N N     . GLU A 1 209 ? -34.823 -15.760 -41.340 1.00 51.44  ? 190 GLU A N     1 
ATOM   1448 C CA    . GLU A 1 209 ? -35.521 -14.977 -42.352 1.00 53.75  ? 190 GLU A CA    1 
ATOM   1449 C C     . GLU A 1 209 ? -34.605 -13.961 -43.039 1.00 52.33  ? 190 GLU A C     1 
ATOM   1450 O O     . GLU A 1 209 ? -34.976 -13.424 -44.076 1.00 52.50  ? 190 GLU A O     1 
ATOM   1451 C CB    . GLU A 1 209 ? -36.687 -14.203 -41.737 1.00 59.65  ? 190 GLU A CB    1 
ATOM   1452 C CG    . GLU A 1 209 ? -37.916 -15.049 -41.473 1.00 69.82  ? 190 GLU A CG    1 
ATOM   1453 C CD    . GLU A 1 209 ? -39.120 -14.251 -40.993 1.00 79.99  ? 190 GLU A CD    1 
ATOM   1454 O OE1   . GLU A 1 209 ? -39.011 -13.003 -40.883 1.00 75.75  ? 190 GLU A OE1   1 
ATOM   1455 O OE2   . GLU A 1 209 ? -40.167 -14.877 -40.725 1.00 88.39  ? 190 GLU A OE2   1 
ATOM   1456 N N     . LEU A 1 210 ? -33.435 -13.660 -42.461 1.00 47.43  ? 191 LEU A N     1 
ATOM   1457 C CA    . LEU A 1 210 ? -32.617 -12.575 -42.966 1.00 43.79  ? 191 LEU A CA    1 
ATOM   1458 C C     . LEU A 1 210 ? -31.989 -12.971 -44.294 1.00 46.66  ? 191 LEU A C     1 
ATOM   1459 O O     . LEU A 1 210 ? -31.372 -14.020 -44.408 1.00 45.53  ? 191 LEU A O     1 
ATOM   1460 C CB    . LEU A 1 210 ? -31.506 -12.266 -41.959 1.00 44.43  ? 191 LEU A CB    1 
ATOM   1461 C CG    . LEU A 1 210 ? -31.927 -11.559 -40.675 1.00 38.77  ? 191 LEU A CG    1 
ATOM   1462 C CD1   . LEU A 1 210 ? -30.745 -11.472 -39.730 1.00 38.45  ? 191 LEU A CD1   1 
ATOM   1463 C CD2   . LEU A 1 210 ? -32.490 -10.165 -40.955 1.00 40.11  ? 191 LEU A CD2   1 
ATOM   1464 N N     . ALA A 1 211 ? -32.080 -12.084 -45.282 1.00 44.92  ? 192 ALA A N     1 
ATOM   1465 C CA    . ALA A 1 211 ? -31.287 -12.271 -46.474 1.00 46.73  ? 192 ALA A CA    1 
ATOM   1466 C C     . ALA A 1 211 ? -29.834 -11.968 -46.108 1.00 50.50  ? 192 ALA A C     1 
ATOM   1467 O O     . ALA A 1 211 ? -29.569 -11.155 -45.217 1.00 43.81  ? 192 ALA A O     1 
ATOM   1468 C CB    . ALA A 1 211 ? -31.825 -11.396 -47.585 1.00 49.87  ? 192 ALA A CB    1 
ATOM   1469 N N     . VAL A 1 212 ? -28.904 -12.637 -46.799 1.00 49.94  ? 193 VAL A N     1 
ATOM   1470 C CA    . VAL A 1 212 ? -27.482 -12.557 -46.500 1.00 54.53  ? 193 VAL A CA    1 
ATOM   1471 C C     . VAL A 1 212 ? -27.014 -11.097 -46.442 1.00 49.74  ? 193 VAL A C     1 
ATOM   1472 O O     . VAL A 1 212 ? -26.146 -10.770 -45.638 1.00 45.15  ? 193 VAL A O     1 
ATOM   1473 C CB    . VAL A 1 212 ? -26.666 -13.400 -47.507 1.00 61.74  ? 193 VAL A CB    1 
ATOM   1474 C CG1   . VAL A 1 212 ? -25.417 -12.683 -48.013 1.00 63.43  ? 193 VAL A CG1   1 
ATOM   1475 C CG2   . VAL A 1 212 ? -26.321 -14.769 -46.930 1.00 63.71  ? 193 VAL A CG2   1 
ATOM   1476 N N     . HIS A 1 213 ? -27.603 -10.218 -47.259 1.00 51.26  ? 194 HIS A N     1 
ATOM   1477 C CA    . HIS A 1 213 ? -27.186 -8.824  -47.301 1.00 53.87  ? 194 HIS A CA    1 
ATOM   1478 C C     . HIS A 1 213 ? -27.600 -8.061  -46.040 1.00 47.45  ? 194 HIS A C     1 
ATOM   1479 O O     . HIS A 1 213 ? -27.238 -6.897  -45.890 1.00 43.33  ? 194 HIS A O     1 
ATOM   1480 C CB    . HIS A 1 213 ? -27.706 -8.123  -48.564 1.00 62.73  ? 194 HIS A CB    1 
ATOM   1481 C CG    . HIS A 1 213 ? -29.192 -7.940  -48.649 1.00 68.63  ? 194 HIS A CG    1 
ATOM   1482 N ND1   . HIS A 1 213 ? -29.744 -7.030  -49.525 1.00 73.24  ? 194 HIS A ND1   1 
ATOM   1483 C CD2   . HIS A 1 213 ? -30.226 -8.487  -47.993 1.00 67.50  ? 194 HIS A CD2   1 
ATOM   1484 C CE1   . HIS A 1 213 ? -31.066 -7.055  -49.413 1.00 74.82  ? 194 HIS A CE1   1 
ATOM   1485 N NE2   . HIS A 1 213 ? -31.385 -7.936  -48.488 1.00 65.73  ? 194 HIS A NE2   1 
ATOM   1486 N N     . HIS A 1 214 ? -28.378 -8.688  -45.149 1.00 42.25  ? 195 HIS A N     1 
ATOM   1487 C CA    . HIS A 1 214 ? -28.747 -8.064  -43.885 1.00 37.09  ? 195 HIS A CA    1 
ATOM   1488 C C     . HIS A 1 214 ? -27.840 -8.498  -42.736 1.00 32.77  ? 195 HIS A C     1 
ATOM   1489 O O     . HIS A 1 214 ? -27.964 -7.984  -41.641 1.00 35.67  ? 195 HIS A O     1 
ATOM   1490 C CB    . HIS A 1 214 ? -30.230 -8.309  -43.594 1.00 36.57  ? 195 HIS A CB    1 
ATOM   1491 C CG    . HIS A 1 214 ? -31.146 -7.418  -44.351 1.00 41.54  ? 195 HIS A CG    1 
ATOM   1492 N ND1   . HIS A 1 214 ? -30.754 -6.232  -44.928 1.00 45.59  ? 195 HIS A ND1   1 
ATOM   1493 C CD2   . HIS A 1 214 ? -32.454 -7.529  -44.588 1.00 37.30  ? 195 HIS A CD2   1 
ATOM   1494 C CE1   . HIS A 1 214 ? -31.806 -5.668  -45.509 1.00 42.93  ? 195 HIS A CE1   1 
ATOM   1495 N NE2   . HIS A 1 214 ? -32.849 -6.419  -45.284 1.00 42.80  ? 195 HIS A NE2   1 
ATOM   1496 N N     . LEU A 1 215 ? -26.899 -9.418  -42.993 1.00 33.92  ? 196 LEU A N     1 
ATOM   1497 C CA    . LEU A 1 215 ? -25.874 -9.801  -42.042 1.00 33.34  ? 196 LEU A CA    1 
ATOM   1498 C C     . LEU A 1 215 ? -24.494 -9.296  -42.454 1.00 31.68  ? 196 LEU A C     1 
ATOM   1499 O O     . LEU A 1 215 ? -24.118 -9.355  -43.630 1.00 35.40  ? 196 LEU A O     1 
ATOM   1500 C CB    . LEU A 1 215 ? -25.858 -11.336 -41.981 1.00 36.84  ? 196 LEU A CB    1 
ATOM   1501 C CG    . LEU A 1 215 ? -27.037 -11.970 -41.244 1.00 42.02  ? 196 LEU A CG    1 
ATOM   1502 C CD1   . LEU A 1 215 ? -27.095 -13.471 -41.520 1.00 46.21  ? 196 LEU A CD1   1 
ATOM   1503 C CD2   . LEU A 1 215 ? -26.928 -11.709 -39.752 1.00 44.05  ? 196 LEU A CD2   1 
ATOM   1504 N N     . GLY A 1 216 ? -23.701 -8.941  -41.442 1.00 29.47  ? 197 GLY A N     1 
ATOM   1505 C CA    . GLY A 1 216 ? -22.353 -8.431  -41.634 1.00 30.61  ? 197 GLY A CA    1 
ATOM   1506 C C     . GLY A 1 216 ? -22.372 -6.932  -41.926 1.00 32.00  ? 197 GLY A C     1 
ATOM   1507 O O     . GLY A 1 216 ? -23.432 -6.308  -41.910 1.00 34.27  ? 197 GLY A O     1 
ATOM   1508 N N     . ALA A 1 217 ? -21.177 -6.406  -42.218 1.00 31.69  ? 198 ALA A N     1 
ATOM   1509 C CA    . ALA A 1 217 ? -20.943 -4.994  -42.491 1.00 32.37  ? 198 ALA A CA    1 
ATOM   1510 C C     . ALA A 1 217 ? -20.611 -4.801  -43.968 1.00 32.84  ? 198 ALA A C     1 
ATOM   1511 O O     . ALA A 1 217 ? -19.731 -5.492  -44.482 1.00 31.50  ? 198 ALA A O     1 
ATOM   1512 C CB    . ALA A 1 217 ? -19.797 -4.524  -41.635 1.00 34.34  ? 198 ALA A CB    1 
ATOM   1513 N N     . HIS A 1 218 ? -21.280 -3.832  -44.620 1.00 28.67  ? 199 HIS A N     1 
ATOM   1514 C CA    . HIS A 1 218 ? -21.226 -3.653  -46.064 1.00 31.58  ? 199 HIS A CA    1 
ATOM   1515 C C     . HIS A 1 218 ? -21.101 -2.174  -46.396 1.00 31.55  ? 199 HIS A C     1 
ATOM   1516 O O     . HIS A 1 218 ? -21.855 -1.363  -45.851 1.00 30.87  ? 199 HIS A O     1 
ATOM   1517 C CB    . HIS A 1 218 ? -22.502 -4.168  -46.739 1.00 34.18  ? 199 HIS A CB    1 
ATOM   1518 C CG    . HIS A 1 218 ? -22.727 -5.586  -46.383 1.00 38.73  ? 199 HIS A CG    1 
ATOM   1519 N ND1   . HIS A 1 218 ? -22.108 -6.597  -47.082 1.00 40.63  ? 199 HIS A ND1   1 
ATOM   1520 C CD2   . HIS A 1 218 ? -23.316 -6.164  -45.328 1.00 42.37  ? 199 HIS A CD2   1 
ATOM   1521 C CE1   . HIS A 1 218 ? -22.410 -7.762  -46.517 1.00 49.16  ? 199 HIS A CE1   1 
ATOM   1522 N NE2   . HIS A 1 218 ? -23.131 -7.519  -45.433 1.00 42.76  ? 199 HIS A NE2   1 
ATOM   1523 N N     . TYR A 1 219 ? -20.181 -1.852  -47.306 1.00 29.99  ? 200 TYR A N     1 
ATOM   1524 C CA    . TYR A 1 219 ? -20.169 -0.547  -47.953 1.00 30.63  ? 200 TYR A CA    1 
ATOM   1525 C C     . TYR A 1 219 ? -21.010 -0.616  -49.217 1.00 32.27  ? 200 TYR A C     1 
ATOM   1526 O O     . TYR A 1 219 ? -20.770 -1.464  -50.068 1.00 33.05  ? 200 TYR A O     1 
ATOM   1527 C CB    . TYR A 1 219 ? -18.740 -0.114  -48.300 1.00 29.55  ? 200 TYR A CB    1 
ATOM   1528 C CG    . TYR A 1 219 ? -18.654 1.123   -49.164 1.00 30.55  ? 200 TYR A CG    1 
ATOM   1529 C CD1   . TYR A 1 219 ? -19.130 2.329   -48.697 1.00 31.14  ? 200 TYR A CD1   1 
ATOM   1530 C CD2   . TYR A 1 219 ? -18.181 1.076   -50.468 1.00 29.22  ? 200 TYR A CD2   1 
ATOM   1531 C CE1   . TYR A 1 219 ? -19.080 3.478   -49.462 1.00 29.38  ? 200 TYR A CE1   1 
ATOM   1532 C CE2   . TYR A 1 219 ? -18.117 2.217   -51.247 1.00 27.34  ? 200 TYR A CE2   1 
ATOM   1533 C CZ    . TYR A 1 219 ? -18.571 3.417   -50.743 1.00 28.51  ? 200 TYR A CZ    1 
ATOM   1534 O OH    . TYR A 1 219 ? -18.539 4.580   -51.441 1.00 30.40  ? 200 TYR A OH    1 
ATOM   1535 N N     . LEU A 1 220 ? -22.020 0.261   -49.310 1.00 33.35  ? 201 LEU A N     1 
ATOM   1536 C CA    . LEU A 1 220 ? -22.907 0.294   -50.457 1.00 35.58  ? 201 LEU A CA    1 
ATOM   1537 C C     . LEU A 1 220 ? -22.320 1.305   -51.438 1.00 40.63  ? 201 LEU A C     1 
ATOM   1538 O O     . LEU A 1 220 ? -22.075 2.447   -51.069 1.00 38.76  ? 201 LEU A O     1 
ATOM   1539 C CB    . LEU A 1 220 ? -24.327 0.665   -50.011 1.00 38.29  ? 201 LEU A CB    1 
ATOM   1540 C CG    . LEU A 1 220 ? -25.111 -0.429  -49.277 1.00 43.40  ? 201 LEU A CG    1 
ATOM   1541 C CD1   . LEU A 1 220 ? -24.932 -1.817  -49.905 1.00 43.68  ? 201 LEU A CD1   1 
ATOM   1542 C CD2   . LEU A 1 220 ? -24.728 -0.474  -47.806 1.00 52.78  ? 201 LEU A CD2   1 
ATOM   1543 N N     . PRO A 1 221 ? -21.951 0.881   -52.670 1.00 43.76  ? 202 PRO A N     1 
ATOM   1544 C CA    . PRO A 1 221 ? -21.276 1.761   -53.622 1.00 44.44  ? 202 PRO A CA    1 
ATOM   1545 C C     . PRO A 1 221 ? -21.982 3.095   -53.850 1.00 48.27  ? 202 PRO A C     1 
ATOM   1546 O O     . PRO A 1 221 ? -21.327 4.052   -54.244 1.00 47.41  ? 202 PRO A O     1 
ATOM   1547 C CB    . PRO A 1 221 ? -21.261 0.939   -54.921 1.00 46.69  ? 202 PRO A CB    1 
ATOM   1548 C CG    . PRO A 1 221 ? -21.252 -0.494  -54.438 1.00 50.22  ? 202 PRO A CG    1 
ATOM   1549 C CD    . PRO A 1 221 ? -22.122 -0.487  -53.191 1.00 43.65  ? 202 PRO A CD    1 
ATOM   1550 N N     . ALA A 1 222 ? -23.306 3.148   -53.625 1.00 43.59  ? 203 ALA A N     1 
ATOM   1551 C CA    . ALA A 1 222 ? -24.061 4.389   -53.714 1.00 45.74  ? 203 ALA A CA    1 
ATOM   1552 C C     . ALA A 1 222 ? -23.498 5.446   -52.763 1.00 52.75  ? 203 ALA A C     1 
ATOM   1553 O O     . ALA A 1 222 ? -23.642 6.641   -53.022 1.00 47.76  ? 203 ALA A O     1 
ATOM   1554 C CB    . ALA A 1 222 ? -25.524 4.134   -53.412 1.00 45.56  ? 203 ALA A CB    1 
ATOM   1555 N N     . GLY A 1 223 ? -22.934 5.004   -51.626 1.00 50.14  ? 204 GLY A N     1 
ATOM   1556 C CA    . GLY A 1 223 ? -22.417 5.911   -50.609 1.00 46.37  ? 204 GLY A CA    1 
ATOM   1557 C C     . GLY A 1 223 ? -23.120 5.726   -49.262 1.00 47.46  ? 204 GLY A C     1 
ATOM   1558 O O     . GLY A 1 223 ? -23.855 6.602   -48.805 1.00 45.26  ? 204 GLY A O     1 
ATOM   1559 N N     . GLY A 1 224 ? -22.876 4.578   -48.615 1.00 36.45  ? 205 GLY A N     1 
ATOM   1560 C CA    . GLY A 1 224 ? -23.308 4.389   -47.241 1.00 33.44  ? 205 GLY A CA    1 
ATOM   1561 C C     . GLY A 1 224 ? -22.789 3.080   -46.656 1.00 33.86  ? 205 GLY A C     1 
ATOM   1562 O O     . GLY A 1 224 ? -22.173 2.279   -47.370 1.00 32.44  ? 205 GLY A O     1 
ATOM   1563 N N     . VAL A 1 225 ? -23.071 2.885   -45.366 1.00 30.40  ? 206 VAL A N     1 
ATOM   1564 C CA    . VAL A 1 225 ? -22.670 1.684   -44.668 1.00 30.21  ? 206 VAL A CA    1 
ATOM   1565 C C     . VAL A 1 225 ? -23.885 1.071   -43.999 1.00 32.28  ? 206 VAL A C     1 
ATOM   1566 O O     . VAL A 1 225 ? -24.681 1.781   -43.397 1.00 32.93  ? 206 VAL A O     1 
ATOM   1567 C CB    . VAL A 1 225 ? -21.598 2.013   -43.633 1.00 35.24  ? 206 VAL A CB    1 
ATOM   1568 C CG1   . VAL A 1 225 ? -21.287 0.789   -42.778 1.00 40.49  ? 206 VAL A CG1   1 
ATOM   1569 C CG2   . VAL A 1 225 ? -20.359 2.570   -44.290 1.00 32.63  ? 206 VAL A CG2   1 
ATOM   1570 N N     . TYR A 1 226 ? -24.015 -0.251  -44.119 1.00 29.55  ? 207 TYR A N     1 
ATOM   1571 C CA    . TYR A 1 226 ? -25.000 -0.995  -43.358 1.00 29.13  ? 207 TYR A CA    1 
ATOM   1572 C C     . TYR A 1 226 ? -24.261 -2.080  -42.590 1.00 30.98  ? 207 TYR A C     1 
ATOM   1573 O O     . TYR A 1 226 ? -23.385 -2.716  -43.156 1.00 32.27  ? 207 TYR A O     1 
ATOM   1574 C CB    . TYR A 1 226 ? -26.069 -1.641  -44.241 1.00 29.17  ? 207 TYR A CB    1 
ATOM   1575 C CG    . TYR A 1 226 ? -26.852 -2.686  -43.501 1.00 32.31  ? 207 TYR A CG    1 
ATOM   1576 C CD1   . TYR A 1 226 ? -26.395 -3.995  -43.432 1.00 32.20  ? 207 TYR A CD1   1 
ATOM   1577 C CD2   . TYR A 1 226 ? -27.995 -2.356  -42.786 1.00 32.70  ? 207 TYR A CD2   1 
ATOM   1578 C CE1   . TYR A 1 226 ? -27.077 -4.952  -42.698 1.00 33.92  ? 207 TYR A CE1   1 
ATOM   1579 C CE2   . TYR A 1 226 ? -28.711 -3.309  -42.083 1.00 32.35  ? 207 TYR A CE2   1 
ATOM   1580 C CZ    . TYR A 1 226 ? -28.249 -4.614  -42.040 1.00 33.42  ? 207 TYR A CZ    1 
ATOM   1581 O OH    . TYR A 1 226 ? -28.937 -5.546  -41.299 1.00 30.55  ? 207 TYR A OH    1 
ATOM   1582 N N     . SER A 1 227 ? -24.629 -2.267  -41.315 1.00 28.41  ? 208 SER A N     1 
ATOM   1583 C CA    . SER A 1 227 ? -24.091 -3.347  -40.505 1.00 30.67  ? 208 SER A CA    1 
ATOM   1584 C C     . SER A 1 227 ? -25.225 -4.001  -39.725 1.00 30.03  ? 208 SER A C     1 
ATOM   1585 O O     . SER A 1 227 ? -26.055 -3.335  -39.096 1.00 31.07  ? 208 SER A O     1 
ATOM   1586 C CB    . SER A 1 227 ? -22.984 -2.865  -39.615 1.00 30.83  ? 208 SER A CB    1 
ATOM   1587 O OG    . SER A 1 227 ? -22.686 -3.814  -38.607 1.00 40.88  ? 208 SER A OG    1 
ATOM   1588 N N     . GLY A 1 228 ? -25.262 -5.329  -39.804 1.00 29.24  ? 209 GLY A N     1 
ATOM   1589 C CA    . GLY A 1 228 ? -26.203 -6.139  -39.052 1.00 32.14  ? 209 GLY A CA    1 
ATOM   1590 C C     . GLY A 1 228 ? -25.412 -7.240  -38.341 1.00 30.00  ? 209 GLY A C     1 
ATOM   1591 O O     . GLY A 1 228 ? -24.684 -7.973  -38.990 1.00 31.89  ? 209 GLY A O     1 
ATOM   1592 N N     . ALA A 1 229 ? -25.477 -7.289  -37.015 1.00 27.19  ? 210 ALA A N     1 
ATOM   1593 C CA    . ALA A 1 229 ? -24.797 -8.350  -36.307 1.00 33.91  ? 210 ALA A CA    1 
ATOM   1594 C C     . ALA A 1 229 ? -25.664 -8.835  -35.149 1.00 32.77  ? 210 ALA A C     1 
ATOM   1595 O O     . ALA A 1 229 ? -26.301 -8.057  -34.443 1.00 31.03  ? 210 ALA A O     1 
ATOM   1596 C CB    . ALA A 1 229 ? -23.432 -7.868  -35.857 1.00 31.74  ? 210 ALA A CB    1 
ATOM   1597 N N     . PRO A 1 230 ? -25.688 -10.159 -34.890 1.00 30.66  ? 211 PRO A N     1 
ATOM   1598 C CA    . PRO A 1 230 ? -26.470 -10.674 -33.775 1.00 30.85  ? 211 PRO A CA    1 
ATOM   1599 C C     . PRO A 1 230 ? -25.930 -10.138 -32.450 1.00 31.97  ? 211 PRO A C     1 
ATOM   1600 O O     . PRO A 1 230 ? -24.722 -10.141 -32.211 1.00 33.25  ? 211 PRO A O     1 
ATOM   1601 C CB    . PRO A 1 230 ? -26.329 -12.205 -33.896 1.00 31.58  ? 211 PRO A CB    1 
ATOM   1602 C CG    . PRO A 1 230 ? -25.021 -12.393 -34.643 1.00 32.06  ? 211 PRO A CG    1 
ATOM   1603 C CD    . PRO A 1 230 ? -24.891 -11.198 -35.565 1.00 32.46  ? 211 PRO A CD    1 
ATOM   1604 N N     . ALA A 1 231 ? -26.851 -9.703  -31.575 1.00 33.73  ? 212 ALA A N     1 
ATOM   1605 C CA    . ALA A 1 231 ? -26.476 -9.128  -30.296 1.00 34.71  ? 212 ALA A CA    1 
ATOM   1606 C C     . ALA A 1 231 ? -26.934 -10.022 -29.142 1.00 35.54  ? 212 ALA A C     1 
ATOM   1607 O O     . ALA A 1 231 ? -26.549 -9.810  -28.001 1.00 35.48  ? 212 ALA A O     1 
ATOM   1608 C CB    . ALA A 1 231 ? -27.035 -7.723  -30.199 1.00 39.33  ? 212 ALA A CB    1 
ATOM   1609 N N     . GLY A 1 232 ? -27.780 -11.006 -29.438 1.00 35.45  ? 213 GLY A N     1 
ATOM   1610 C CA    . GLY A 1 232 ? -28.425 -11.815 -28.421 1.00 33.84  ? 213 GLY A CA    1 
ATOM   1611 C C     . GLY A 1 232 ? -29.545 -12.610 -29.072 1.00 34.92  ? 213 GLY A C     1 
ATOM   1612 O O     . GLY A 1 232 ? -29.783 -12.480 -30.280 1.00 34.56  ? 213 GLY A O     1 
ATOM   1613 N N     . PRO A 1 233 ? -30.247 -13.481 -28.320 1.00 41.10  ? 214 PRO A N     1 
ATOM   1614 C CA    . PRO A 1 233 ? -31.351 -14.259 -28.890 1.00 36.86  ? 214 PRO A CA    1 
ATOM   1615 C C     . PRO A 1 233 ? -32.422 -13.399 -29.562 1.00 34.05  ? 214 PRO A C     1 
ATOM   1616 O O     . PRO A 1 233 ? -33.041 -12.561 -28.918 1.00 35.78  ? 214 PRO A O     1 
ATOM   1617 C CB    . PRO A 1 233 ? -31.935 -15.008 -27.675 1.00 39.61  ? 214 PRO A CB    1 
ATOM   1618 C CG    . PRO A 1 233 ? -30.797 -15.042 -26.664 1.00 41.09  ? 214 PRO A CG    1 
ATOM   1619 C CD    . PRO A 1 233 ? -29.992 -13.781 -26.900 1.00 41.20  ? 214 PRO A CD    1 
ATOM   1620 N N     . GLY A 1 234 ? -32.636 -13.652 -30.852 1.00 33.37  ? 215 GLY A N     1 
ATOM   1621 C CA    . GLY A 1 234 ? -33.585 -12.937 -31.694 1.00 36.30  ? 215 GLY A CA    1 
ATOM   1622 C C     . GLY A 1 234 ? -33.360 -11.420 -31.732 1.00 34.55  ? 215 GLY A C     1 
ATOM   1623 O O     . GLY A 1 234 ? -34.316 -10.696 -32.017 1.00 35.70  ? 215 GLY A O     1 
ATOM   1624 N N     . VAL A 1 235 ? -32.126 -10.946 -31.476 1.00 34.82  ? 216 VAL A N     1 
ATOM   1625 C CA    . VAL A 1 235 ? -31.856 -9.503  -31.525 1.00 34.36  ? 216 VAL A CA    1 
ATOM   1626 C C     . VAL A 1 235 ? -30.744 -9.228  -32.526 1.00 33.92  ? 216 VAL A C     1 
ATOM   1627 O O     . VAL A 1 235 ? -29.658 -9.805  -32.399 1.00 31.08  ? 216 VAL A O     1 
ATOM   1628 C CB    . VAL A 1 235 ? -31.513 -8.907  -30.144 1.00 36.18  ? 216 VAL A CB    1 
ATOM   1629 C CG1   . VAL A 1 235 ? -31.253 -7.398  -30.226 1.00 35.37  ? 216 VAL A CG1   1 
ATOM   1630 C CG2   . VAL A 1 235 ? -32.610 -9.185  -29.141 1.00 39.23  ? 216 VAL A CG2   1 
ATOM   1631 N N     . LEU A 1 236 ? -31.048 -8.386  -33.536 1.00 30.44  ? 217 LEU A N     1 
ATOM   1632 C CA    . LEU A 1 236 ? -30.046 -7.919  -34.482 1.00 27.72  ? 217 LEU A CA    1 
ATOM   1633 C C     . LEU A 1 236 ? -29.683 -6.468  -34.165 1.00 32.41  ? 217 LEU A C     1 
ATOM   1634 O O     . LEU A 1 236 ? -30.562 -5.592  -34.099 1.00 31.61  ? 217 LEU A O     1 
ATOM   1635 C CB    . LEU A 1 236 ? -30.593 -8.052  -35.905 1.00 29.17  ? 217 LEU A CB    1 
ATOM   1636 C CG    . LEU A 1 236 ? -29.622 -7.742  -37.050 1.00 31.84  ? 217 LEU A CG    1 
ATOM   1637 C CD1   . LEU A 1 236 ? -28.606 -8.880  -37.254 1.00 32.50  ? 217 LEU A CD1   1 
ATOM   1638 C CD2   . LEU A 1 236 ? -30.398 -7.488  -38.335 1.00 33.24  ? 217 LEU A CD2   1 
ATOM   1639 N N     . ARG A 1 237 ? -28.387 -6.215  -33.994 1.00 30.92  ? 218 ARG A N     1 
ATOM   1640 C CA    . ARG A 1 237 ? -27.877 -4.854  -33.869 1.00 33.44  ? 218 ARG A CA    1 
ATOM   1641 C C     . ARG A 1 237 ? -27.621 -4.307  -35.274 1.00 31.22  ? 218 ARG A C     1 
ATOM   1642 O O     . ARG A 1 237 ? -26.911 -4.904  -36.075 1.00 29.03  ? 218 ARG A O     1 
ATOM   1643 C CB    . ARG A 1 237 ? -26.618 -4.857  -32.994 1.00 33.15  ? 218 ARG A CB    1 
ATOM   1644 C CG    . ARG A 1 237 ? -25.808 -3.562  -33.032 1.00 36.66  ? 218 ARG A CG    1 
ATOM   1645 C CD    . ARG A 1 237 ? -26.150 -2.490  -32.019 1.00 47.09  ? 218 ARG A CD    1 
ATOM   1646 N NE    . ARG A 1 237 ? -26.720 -2.954  -30.752 1.00 41.97  ? 218 ARG A NE    1 
ATOM   1647 C CZ    . ARG A 1 237 ? -26.086 -3.140  -29.600 1.00 40.86  ? 218 ARG A CZ    1 
ATOM   1648 N NH1   . ARG A 1 237 ? -26.807 -3.464  -28.549 1.00 42.68  ? 218 ARG A NH1   1 
ATOM   1649 N NH2   . ARG A 1 237 ? -24.779 -2.982  -29.463 1.00 47.11  ? 218 ARG A NH2   1 
ATOM   1650 N N     . VAL A 1 238 ? -28.153 -3.115  -35.547 1.00 28.46  ? 219 VAL A N     1 
ATOM   1651 C CA    . VAL A 1 238 ? -28.139 -2.561  -36.873 1.00 28.19  ? 219 VAL A CA    1 
ATOM   1652 C C     . VAL A 1 238 ? -27.543 -1.163  -36.757 1.00 27.85  ? 219 VAL A C     1 
ATOM   1653 O O     . VAL A 1 238 ? -27.820 -0.460  -35.791 1.00 29.66  ? 219 VAL A O     1 
ATOM   1654 C CB    . VAL A 1 238 ? -29.562 -2.514  -37.462 1.00 32.52  ? 219 VAL A CB    1 
ATOM   1655 C CG1   . VAL A 1 238 ? -29.612 -1.708  -38.745 1.00 32.58  ? 219 VAL A CG1   1 
ATOM   1656 C CG2   . VAL A 1 238 ? -30.127 -3.910  -37.672 1.00 38.01  ? 219 VAL A CG2   1 
ATOM   1657 N N     . ILE A 1 239 ? -26.616 -0.862  -37.660 1.00 28.09  ? 220 ILE A N     1 
ATOM   1658 C CA    . ILE A 1 239 ? -26.091 0.485   -37.843 1.00 30.26  ? 220 ILE A CA    1 
ATOM   1659 C C     . ILE A 1 239 ? -26.287 0.825   -39.314 1.00 30.28  ? 220 ILE A C     1 
ATOM   1660 O O     . ILE A 1 239 ? -25.978 0.026   -40.185 1.00 27.97  ? 220 ILE A O     1 
ATOM   1661 C CB    . ILE A 1 239 ? -24.604 0.575   -37.448 1.00 34.90  ? 220 ILE A CB    1 
ATOM   1662 C CG1   . ILE A 1 239 ? -24.361 0.182   -35.992 1.00 40.42  ? 220 ILE A CG1   1 
ATOM   1663 C CG2   . ILE A 1 239 ? -24.059 1.969   -37.762 1.00 35.83  ? 220 ILE A CG2   1 
ATOM   1664 C CD1   . ILE A 1 239 ? -22.905 0.010   -35.638 1.00 45.41  ? 220 ILE A CD1   1 
ATOM   1665 N N     . THR A 1 240 ? -26.822 2.017   -39.593 1.00 29.06  ? 221 THR A N     1 
ATOM   1666 C CA    . THR A 1 240 ? -26.924 2.539   -40.936 1.00 29.81  ? 221 THR A CA    1 
ATOM   1667 C C     . THR A 1 240 ? -26.283 3.926   -40.973 1.00 32.07  ? 221 THR A C     1 
ATOM   1668 O O     . THR A 1 240 ? -26.486 4.705   -40.050 1.00 31.26  ? 221 THR A O     1 
ATOM   1669 C CB    . THR A 1 240 ? -28.395 2.625   -41.362 1.00 35.44  ? 221 THR A CB    1 
ATOM   1670 O OG1   . THR A 1 240 ? -29.038 3.602   -40.540 1.00 34.20  ? 221 THR A OG1   1 
ATOM   1671 C CG2   . THR A 1 240 ? -29.134 1.312   -41.239 1.00 36.24  ? 221 THR A CG2   1 
ATOM   1672 N N     . THR A 1 241 ? -25.466 4.199   -41.989 1.00 28.90  ? 222 THR A N     1 
ATOM   1673 C CA    . THR A 1 241 ? -25.138 5.586   -42.295 1.00 35.16  ? 222 THR A CA    1 
ATOM   1674 C C     . THR A 1 241 ? -25.300 5.819   -43.785 1.00 33.54  ? 222 THR A C     1 
ATOM   1675 O O     . THR A 1 241 ? -24.853 5.025   -44.619 1.00 33.55  ? 222 THR A O     1 
ATOM   1676 C CB    . THR A 1 241 ? -23.802 6.111   -41.743 1.00 44.41  ? 222 THR A CB    1 
ATOM   1677 O OG1   . THR A 1 241 ? -22.809 6.220   -42.760 1.00 55.65  ? 222 THR A OG1   1 
ATOM   1678 C CG2   . THR A 1 241 ? -23.325 5.365   -40.520 1.00 39.52  ? 222 THR A CG2   1 
ATOM   1679 N N     . VAL A 1 242 ? -26.019 6.904   -44.086 1.00 33.62  ? 223 VAL A N     1 
ATOM   1680 C CA    . VAL A 1 242 ? -26.155 7.362   -45.452 1.00 36.12  ? 223 VAL A CA    1 
ATOM   1681 C C     . VAL A 1 242 ? -25.309 8.623   -45.568 1.00 38.27  ? 223 VAL A C     1 
ATOM   1682 O O     . VAL A 1 242 ? -25.584 9.611   -44.910 1.00 38.90  ? 223 VAL A O     1 
ATOM   1683 C CB    . VAL A 1 242 ? -27.637 7.572   -45.799 1.00 41.22  ? 223 VAL A CB    1 
ATOM   1684 C CG1   . VAL A 1 242 ? -27.816 7.974   -47.251 1.00 44.22  ? 223 VAL A CG1   1 
ATOM   1685 C CG2   . VAL A 1 242 ? -28.447 6.321   -45.478 1.00 44.96  ? 223 VAL A CG2   1 
ATOM   1686 N N     . PHE A 1 243 ? -24.225 8.544   -46.338 1.00 40.72  ? 224 PHE A N     1 
ATOM   1687 C CA    . PHE A 1 243 ? -23.266 9.632   -46.430 1.00 39.82  ? 224 PHE A CA    1 
ATOM   1688 C C     . PHE A 1 243 ? -23.838 10.809  -47.223 1.00 46.45  ? 224 PHE A C     1 
ATOM   1689 O O     . PHE A 1 243 ? -24.592 10.614  -48.172 1.00 51.20  ? 224 PHE A O     1 
ATOM   1690 C CB    . PHE A 1 243 ? -22.001 9.150   -47.137 1.00 41.78  ? 224 PHE A CB    1 
ATOM   1691 C CG    . PHE A 1 243 ? -21.154 8.194   -46.353 1.00 39.86  ? 224 PHE A CG    1 
ATOM   1692 C CD1   . PHE A 1 243 ? -20.546 8.595   -45.175 1.00 40.32  ? 224 PHE A CD1   1 
ATOM   1693 C CD2   . PHE A 1 243 ? -20.915 6.915   -46.829 1.00 36.67  ? 224 PHE A CD2   1 
ATOM   1694 C CE1   . PHE A 1 243 ? -19.768 7.708   -44.453 1.00 40.60  ? 224 PHE A CE1   1 
ATOM   1695 C CE2   . PHE A 1 243 ? -20.158 6.028   -46.099 1.00 34.90  ? 224 PHE A CE2   1 
ATOM   1696 C CZ    . PHE A 1 243 ? -19.587 6.421   -44.911 1.00 39.85  ? 224 PHE A CZ    1 
ATOM   1697 N N     . GLY A 1 244 ? -23.499 12.036  -46.805 1.00 56.92  ? 225 GLY A N     1 
ATOM   1698 C CA    . GLY A 1 244 ? -23.888 13.226  -47.549 1.00 69.17  ? 225 GLY A CA    1 
ATOM   1699 C C     . GLY A 1 244 ? -25.387 13.525  -47.479 1.00 73.27  ? 225 GLY A C     1 
ATOM   1700 O O     . GLY A 1 244 ? -25.828 14.565  -47.962 1.00 73.18  ? 225 GLY A O     1 
ATOM   1701 N N     . ALA A 1 245 ? -26.169 12.595  -46.913 1.00 75.79  ? 226 ALA A N     1 
ATOM   1702 C CA    . ALA A 1 245 ? -27.549 12.864  -46.548 1.00 70.74  ? 226 ALA A CA    1 
ATOM   1703 C C     . ALA A 1 245 ? -27.544 13.602  -45.215 1.00 70.54  ? 226 ALA A C     1 
ATOM   1704 O O     . ALA A 1 245 ? -27.084 13.059  -44.213 1.00 70.83  ? 226 ALA A O     1 
ATOM   1705 C CB    . ALA A 1 245 ? -28.337 11.575  -46.460 1.00 67.27  ? 226 ALA A CB    1 
ATOM   1706 N N     . THR A 1 246 ? -28.015 14.855  -45.219 1.00 70.60  ? 227 THR A N     1 
ATOM   1707 C CA    . THR A 1 246 ? -28.220 15.587  -43.979 1.00 68.25  ? 227 THR A CA    1 
ATOM   1708 C C     . THR A 1 246 ? -29.374 14.917  -43.238 1.00 65.33  ? 227 THR A C     1 
ATOM   1709 O O     . THR A 1 246 ? -30.477 14.850  -43.772 1.00 59.15  ? 227 THR A O     1 
ATOM   1710 C CB    . THR A 1 246 ? -28.508 17.076  -44.231 1.00 67.24  ? 227 THR A CB    1 
ATOM   1711 O OG1   . THR A 1 246 ? -27.569 17.563  -45.193 1.00 65.64  ? 227 THR A OG1   1 
ATOM   1712 C CG2   . THR A 1 246 ? -28.441 17.907  -42.966 1.00 61.84  ? 227 THR A CG2   1 
ATOM   1713 N N     . PRO A 1 247 ? -29.179 14.373  -42.011 1.00 60.48  ? 228 PRO A N     1 
ATOM   1714 C CA    . PRO A 1 247 ? -30.258 13.647  -41.339 1.00 61.55  ? 228 PRO A CA    1 
ATOM   1715 C C     . PRO A 1 247 ? -31.388 14.606  -40.962 1.00 57.02  ? 228 PRO A C     1 
ATOM   1716 O O     . PRO A 1 247 ? -31.178 15.821  -40.922 1.00 49.63  ? 228 PRO A O     1 
ATOM   1717 C CB    . PRO A 1 247 ? -29.557 13.037  -40.116 1.00 61.46  ? 228 PRO A CB    1 
ATOM   1718 C CG    . PRO A 1 247 ? -28.430 14.017  -39.825 1.00 66.00  ? 228 PRO A CG    1 
ATOM   1719 C CD    . PRO A 1 247 ? -27.956 14.466  -41.193 1.00 64.40  ? 228 PRO A CD    1 
ATOM   1720 N N     . PRO A 1 248 ? -32.620 14.103  -40.694 1.00 62.63  ? 229 PRO A N     1 
ATOM   1721 C CA    . PRO A 1 248 ? -33.711 14.958  -40.203 1.00 59.34  ? 229 PRO A CA    1 
ATOM   1722 C C     . PRO A 1 248 ? -33.328 15.799  -38.978 1.00 57.01  ? 229 PRO A C     1 
ATOM   1723 O O     . PRO A 1 248 ? -33.790 16.933  -38.843 1.00 47.61  ? 229 PRO A O     1 
ATOM   1724 C CB    . PRO A 1 248 ? -34.829 13.962  -39.848 1.00 60.98  ? 229 PRO A CB    1 
ATOM   1725 C CG    . PRO A 1 248 ? -34.538 12.735  -40.707 1.00 61.60  ? 229 PRO A CG    1 
ATOM   1726 C CD    . PRO A 1 248 ? -33.030 12.699  -40.871 1.00 61.87  ? 229 PRO A CD    1 
ATOM   1727 N N     . ALA A 1 249 ? -32.496 15.209  -38.096 1.00 52.52  ? 230 ALA A N     1 
ATOM   1728 C CA    . ALA A 1 249 ? -31.898 15.863  -36.940 1.00 45.97  ? 230 ALA A CA    1 
ATOM   1729 C C     . ALA A 1 249 ? -30.545 15.209  -36.651 1.00 44.69  ? 230 ALA A C     1 
ATOM   1730 O O     . ALA A 1 249 ? -30.320 14.056  -37.038 1.00 49.58  ? 230 ALA A O     1 
ATOM   1731 C CB    . ALA A 1 249 ? -32.804 15.739  -35.735 1.00 45.29  ? 230 ALA A CB    1 
ATOM   1732 N N     . PRO A 1 250 ? -29.616 15.884  -35.941 1.00 51.76  ? 231 PRO A N     1 
ATOM   1733 C CA    . PRO A 1 250 ? -28.302 15.306  -35.635 1.00 52.68  ? 231 PRO A CA    1 
ATOM   1734 C C     . PRO A 1 250 ? -28.281 14.288  -34.491 1.00 51.76  ? 231 PRO A C     1 
ATOM   1735 O O     . PRO A 1 250 ? -27.305 13.554  -34.345 1.00 56.84  ? 231 PRO A O     1 
ATOM   1736 C CB    . PRO A 1 250 ? -27.418 16.499  -35.210 1.00 56.48  ? 231 PRO A CB    1 
ATOM   1737 C CG    . PRO A 1 250 ? -28.295 17.743  -35.399 1.00 57.89  ? 231 PRO A CG    1 
ATOM   1738 C CD    . PRO A 1 250 ? -29.738 17.257  -35.423 1.00 53.43  ? 231 PRO A CD    1 
ATOM   1739 N N     . SER A 1 251 ? -29.319 14.263  -33.652 1.00 45.75  ? 232 SER A N     1 
ATOM   1740 C CA    . SER A 1 251 ? -29.393 13.258  -32.596 1.00 47.91  ? 232 SER A CA    1 
ATOM   1741 C C     . SER A 1 251 ? -30.837 12.997  -32.195 1.00 48.29  ? 232 SER A C     1 
ATOM   1742 O O     . SER A 1 251 ? -31.769 13.535  -32.795 1.00 41.60  ? 232 SER A O     1 
ATOM   1743 C CB    . SER A 1 251 ? -28.586 13.660  -31.392 1.00 55.88  ? 232 SER A CB    1 
ATOM   1744 O OG    . SER A 1 251 ? -29.282 14.639  -30.635 1.00 60.44  ? 232 SER A OG    1 
ATOM   1745 N N     . GLY A 1 252 ? -30.990 12.108  -31.205 1.00 50.28  ? 233 GLY A N     1 
ATOM   1746 C CA    . GLY A 1 252 ? -32.278 11.818  -30.608 1.00 48.15  ? 233 GLY A CA    1 
ATOM   1747 C C     . GLY A 1 252 ? -32.779 10.423  -30.967 1.00 49.77  ? 233 GLY A C     1 
ATOM   1748 O O     . GLY A 1 252 ? -32.221 9.745   -31.839 1.00 42.96  ? 233 GLY A O     1 
ATOM   1749 N N     . PRO A 1 253 ? -33.882 9.981   -30.323 1.00 50.62  ? 234 PRO A N     1 
ATOM   1750 C CA    . PRO A 1 253 ? -34.497 8.694   -30.634 1.00 46.26  ? 234 PRO A CA    1 
ATOM   1751 C C     . PRO A 1 253 ? -35.047 8.680   -32.051 1.00 47.23  ? 234 PRO A C     1 
ATOM   1752 O O     . PRO A 1 253 ? -35.291 9.726   -32.638 1.00 45.49  ? 234 PRO A O     1 
ATOM   1753 C CB    . PRO A 1 253 ? -35.622 8.542   -29.603 1.00 51.93  ? 234 PRO A CB    1 
ATOM   1754 C CG    . PRO A 1 253 ? -35.887 9.957   -29.123 1.00 54.75  ? 234 PRO A CG    1 
ATOM   1755 C CD    . PRO A 1 253 ? -34.570 10.690  -29.232 1.00 51.94  ? 234 PRO A CD    1 
ATOM   1756 N N     . VAL A 1 254 ? -35.227 7.468   -32.581 1.00 44.56  ? 235 VAL A N     1 
ATOM   1757 C CA    . VAL A 1 254 ? -35.558 7.241   -33.970 1.00 44.32  ? 235 VAL A CA    1 
ATOM   1758 C C     . VAL A 1 254 ? -36.606 6.132   -34.007 1.00 47.37  ? 235 VAL A C     1 
ATOM   1759 O O     . VAL A 1 254 ? -36.470 5.151   -33.289 1.00 44.56  ? 235 VAL A O     1 
ATOM   1760 C CB    . VAL A 1 254 ? -34.275 6.871   -34.738 1.00 49.21  ? 235 VAL A CB    1 
ATOM   1761 C CG1   . VAL A 1 254 ? -34.554 6.030   -35.973 1.00 46.75  ? 235 VAL A CG1   1 
ATOM   1762 C CG2   . VAL A 1 254 ? -33.475 8.114   -35.088 1.00 54.12  ? 235 VAL A CG2   1 
ATOM   1763 N N     . ALA A 1 255 ? -37.638 6.284   -34.840 1.00 50.90  ? 236 ALA A N     1 
ATOM   1764 C CA    . ALA A 1 255 ? -38.718 5.307   -34.901 1.00 52.42  ? 236 ALA A CA    1 
ATOM   1765 C C     . ALA A 1 255 ? -38.411 4.254   -35.966 1.00 49.30  ? 236 ALA A C     1 
ATOM   1766 O O     . ALA A 1 255 ? -37.582 4.475   -36.851 1.00 46.42  ? 236 ALA A O     1 
ATOM   1767 C CB    . ALA A 1 255 ? -40.019 6.022   -35.190 1.00 55.88  ? 236 ALA A CB    1 
ATOM   1768 N N     . ALA A 1 256 ? -39.140 3.131   -35.905 1.00 45.04  ? 237 ALA A N     1 
ATOM   1769 C CA    . ALA A 1 256 ? -38.980 2.017   -36.830 1.00 46.54  ? 237 ALA A CA    1 
ATOM   1770 C C     . ALA A 1 256 ? -38.957 2.473   -38.294 1.00 57.19  ? 237 ALA A C     1 
ATOM   1771 O O     . ALA A 1 256 ? -38.085 2.077   -39.072 1.00 49.95  ? 237 ALA A O     1 
ATOM   1772 C CB    . ALA A 1 256 ? -40.089 1.015   -36.604 1.00 49.05  ? 237 ALA A CB    1 
ATOM   1773 N N     . GLU A 1 257 ? -39.924 3.325   -38.658 1.00 57.33  ? 238 GLU A N     1 
ATOM   1774 C CA    . GLU A 1 257 ? -40.069 3.816   -40.018 1.00 57.77  ? 238 GLU A CA    1 
ATOM   1775 C C     . GLU A 1 257 ? -38.762 4.436   -40.519 1.00 47.95  ? 238 GLU A C     1 
ATOM   1776 O O     . GLU A 1 257 ? -38.384 4.215   -41.671 1.00 48.71  ? 238 GLU A O     1 
ATOM   1777 C CB    . GLU A 1 257 ? -41.184 4.866   -40.088 1.00 65.77  ? 238 GLU A CB    1 
ATOM   1778 C CG    . GLU A 1 257 ? -42.507 4.406   -39.496 1.00 78.80  ? 238 GLU A CG    1 
ATOM   1779 C CD    . GLU A 1 257 ? -43.371 5.528   -38.941 1.00 90.73  ? 238 GLU A CD    1 
ATOM   1780 O OE1   . GLU A 1 257 ? -43.199 6.690   -39.368 1.00 88.60  ? 238 GLU A OE1   1 
ATOM   1781 O OE2   . GLU A 1 257 ? -44.195 5.240   -38.058 1.00 102.60 ? 238 GLU A OE2   1 
ATOM   1782 N N     . GLU A 1 258 ? -38.106 5.244   -39.673 1.00 42.53  ? 239 GLU A N     1 
ATOM   1783 C CA    . GLU A 1 258 ? -36.907 5.961   -40.086 1.00 44.20  ? 239 GLU A CA    1 
ATOM   1784 C C     . GLU A 1 258 ? -35.770 4.957   -40.271 1.00 42.35  ? 239 GLU A C     1 
ATOM   1785 O O     . GLU A 1 258 ? -35.064 4.992   -41.275 1.00 39.71  ? 239 GLU A O     1 
ATOM   1786 C CB    . GLU A 1 258 ? -36.538 7.072   -39.097 1.00 46.84  ? 239 GLU A CB    1 
ATOM   1787 C CG    . GLU A 1 258 ? -35.284 7.863   -39.489 1.00 54.26  ? 239 GLU A CG    1 
ATOM   1788 C CD    . GLU A 1 258 ? -35.007 9.123   -38.670 1.00 60.82  ? 239 GLU A CD    1 
ATOM   1789 O OE1   . GLU A 1 258 ? -33.849 9.622   -38.694 1.00 58.42  ? 239 GLU A OE1   1 
ATOM   1790 O OE2   . GLU A 1 258 ? -35.947 9.624   -38.011 1.00 58.98  ? 239 GLU A OE2   1 
ATOM   1791 N N     . LEU A 1 259 ? -35.642 4.023   -39.327 1.00 42.04  ? 240 LEU A N     1 
ATOM   1792 C CA    . LEU A 1 259 ? -34.586 3.029   -39.438 1.00 42.21  ? 240 LEU A CA    1 
ATOM   1793 C C     . LEU A 1 259 ? -34.854 2.148   -40.662 1.00 39.92  ? 240 LEU A C     1 
ATOM   1794 O O     . LEU A 1 259 ? -33.984 2.004   -41.527 1.00 37.91  ? 240 LEU A O     1 
ATOM   1795 C CB    . LEU A 1 259 ? -34.480 2.237   -38.131 1.00 40.08  ? 240 LEU A CB    1 
ATOM   1796 C CG    . LEU A 1 259 ? -33.492 1.073   -38.189 1.00 46.47  ? 240 LEU A CG    1 
ATOM   1797 C CD1   . LEU A 1 259 ? -32.121 1.558   -38.654 1.00 48.91  ? 240 LEU A CD1   1 
ATOM   1798 C CD2   . LEU A 1 259 ? -33.380 0.379   -36.843 1.00 47.90  ? 240 LEU A CD2   1 
ATOM   1799 N N     . GLN A 1 260 ? -36.083 1.629   -40.796 1.00 37.82  ? 241 GLN A N     1 
ATOM   1800 C CA    . GLN A 1 260 ? -36.417 0.802   -41.949 1.00 38.36  ? 241 GLN A CA    1 
ATOM   1801 C C     . GLN A 1 260 ? -36.216 1.576   -43.248 1.00 43.85  ? 241 GLN A C     1 
ATOM   1802 O O     . GLN A 1 260 ? -35.817 0.987   -44.253 1.00 41.68  ? 241 GLN A O     1 
ATOM   1803 C CB    . GLN A 1 260 ? -37.858 0.291   -41.870 1.00 45.27  ? 241 GLN A CB    1 
ATOM   1804 C CG    . GLN A 1 260 ? -38.050 -0.719  -40.751 1.00 43.19  ? 241 GLN A CG    1 
ATOM   1805 C CD    . GLN A 1 260 ? -37.492 -2.061  -41.161 1.00 47.58  ? 241 GLN A CD    1 
ATOM   1806 O OE1   . GLN A 1 260 ? -36.356 -2.175  -41.622 1.00 44.20  ? 241 GLN A OE1   1 
ATOM   1807 N NE2   . GLN A 1 260 ? -38.312 -3.092  -41.045 1.00 47.60  ? 241 GLN A NE2   1 
ATOM   1808 N N     . GLY A 1 261 ? -36.469 2.897   -43.204 1.00 40.43  ? 242 GLY A N     1 
ATOM   1809 C CA    . GLY A 1 261 ? -36.214 3.767   -44.341 1.00 42.54  ? 242 GLY A CA    1 
ATOM   1810 C C     . GLY A 1 261 ? -34.765 3.696   -44.824 1.00 39.27  ? 242 GLY A C     1 
ATOM   1811 O O     . GLY A 1 261 ? -34.517 3.488   -46.018 1.00 35.77  ? 242 GLY A O     1 
ATOM   1812 N N     . GLU A 1 262 ? -33.826 3.826   -43.872 1.00 38.93  ? 243 GLU A N     1 
ATOM   1813 C CA    . GLU A 1 262 ? -32.398 3.820   -44.181 1.00 40.19  ? 243 GLU A CA    1 
ATOM   1814 C C     . GLU A 1 262 ? -31.939 2.426   -44.600 1.00 36.92  ? 243 GLU A C     1 
ATOM   1815 O O     . GLU A 1 262 ? -31.244 2.285   -45.608 1.00 36.27  ? 243 GLU A O     1 
ATOM   1816 C CB    . GLU A 1 262 ? -31.568 4.335   -43.004 1.00 38.27  ? 243 GLU A CB    1 
ATOM   1817 C CG    . GLU A 1 262 ? -31.779 5.821   -42.771 1.00 43.46  ? 243 GLU A CG    1 
ATOM   1818 C CD    . GLU A 1 262 ? -30.607 6.602   -42.194 1.00 48.91  ? 243 GLU A CD    1 
ATOM   1819 O OE1   . GLU A 1 262 ? -29.563 5.991   -41.817 1.00 45.72  ? 243 GLU A OE1   1 
ATOM   1820 O OE2   . GLU A 1 262 ? -30.745 7.826   -42.105 1.00 45.56  ? 243 GLU A OE2   1 
ATOM   1821 N N     . VAL A 1 263 ? -32.367 1.389   -43.865 1.00 37.54  ? 244 VAL A N     1 
ATOM   1822 C CA    . VAL A 1 263 ? -32.021 0.039   -44.271 1.00 35.80  ? 244 VAL A CA    1 
ATOM   1823 C C     . VAL A 1 263 ? -32.443 -0.206  -45.721 1.00 38.91  ? 244 VAL A C     1 
ATOM   1824 O O     . VAL A 1 263 ? -31.665 -0.738  -46.515 1.00 39.84  ? 244 VAL A O     1 
ATOM   1825 C CB    . VAL A 1 263 ? -32.625 -1.023  -43.335 1.00 37.19  ? 244 VAL A CB    1 
ATOM   1826 C CG1   . VAL A 1 263 ? -32.384 -2.430  -43.864 1.00 38.09  ? 244 VAL A CG1   1 
ATOM   1827 C CG2   . VAL A 1 263 ? -32.090 -0.894  -41.923 1.00 38.87  ? 244 VAL A CG2   1 
ATOM   1828 N N     . GLU A 1 264 ? -33.690 0.130   -46.066 1.00 40.04  ? 245 GLU A N     1 
ATOM   1829 C CA    . GLU A 1 264 ? -34.176 -0.146  -47.416 1.00 46.72  ? 245 GLU A CA    1 
ATOM   1830 C C     . GLU A 1 264 ? -33.451 0.721   -48.452 1.00 43.72  ? 245 GLU A C     1 
ATOM   1831 O O     . GLU A 1 264 ? -33.060 0.232   -49.513 1.00 44.86  ? 245 GLU A O     1 
ATOM   1832 C CB    . GLU A 1 264 ? -35.681 0.087   -47.518 1.00 51.67  ? 245 GLU A CB    1 
ATOM   1833 C CG    . GLU A 1 264 ? -36.272 -0.582  -48.742 1.00 57.89  ? 245 GLU A CG    1 
ATOM   1834 C CD    . GLU A 1 264 ? -37.720 -0.211  -48.997 1.00 69.12  ? 245 GLU A CD    1 
ATOM   1835 O OE1   . GLU A 1 264 ? -38.018 0.197   -50.137 1.00 73.30  ? 245 GLU A OE1   1 
ATOM   1836 O OE2   . GLU A 1 264 ? -38.542 -0.319  -48.050 1.00 72.64  ? 245 GLU A OE2   1 
ATOM   1837 N N     . HIS A 1 265 ? -33.246 2.003   -48.126 1.00 42.70  ? 246 HIS A N     1 
ATOM   1838 C CA    . HIS A 1 265 ? -32.488 2.901   -48.983 1.00 45.16  ? 246 HIS A CA    1 
ATOM   1839 C C     . HIS A 1 265 ? -31.125 2.306   -49.320 1.00 44.08  ? 246 HIS A C     1 
ATOM   1840 O O     . HIS A 1 265 ? -30.686 2.397   -50.455 1.00 46.77  ? 246 HIS A O     1 
ATOM   1841 C CB    . HIS A 1 265 ? -32.334 4.301   -48.372 1.00 48.85  ? 246 HIS A CB    1 
ATOM   1842 C CG    . HIS A 1 265 ? -31.494 5.192   -49.231 1.00 57.96  ? 246 HIS A CG    1 
ATOM   1843 N ND1   . HIS A 1 265 ? -30.371 5.860   -48.787 1.00 63.94  ? 246 HIS A ND1   1 
ATOM   1844 C CD2   . HIS A 1 265 ? -31.606 5.483   -50.532 1.00 59.34  ? 246 HIS A CD2   1 
ATOM   1845 C CE1   . HIS A 1 265 ? -29.834 6.543   -49.791 1.00 57.68  ? 246 HIS A CE1   1 
ATOM   1846 N NE2   . HIS A 1 265 ? -30.566 6.324   -50.860 1.00 62.72  ? 246 HIS A NE2   1 
ATOM   1847 N N     . LEU A 1 266 ? -30.454 1.698   -48.344 1.00 43.59  ? 247 LEU A N     1 
ATOM   1848 C CA    . LEU A 1 266 ? -29.085 1.246   -48.542 1.00 43.20  ? 247 LEU A CA    1 
ATOM   1849 C C     . LEU A 1 266 ? -29.060 -0.111  -49.224 1.00 42.41  ? 247 LEU A C     1 
ATOM   1850 O O     . LEU A 1 266 ? -28.298 -0.303  -50.173 1.00 38.14  ? 247 LEU A O     1 
ATOM   1851 C CB    . LEU A 1 266 ? -28.365 1.139   -47.195 1.00 45.42  ? 247 LEU A CB    1 
ATOM   1852 C CG    . LEU A 1 266 ? -27.951 2.460   -46.556 1.00 44.91  ? 247 LEU A CG    1 
ATOM   1853 C CD1   . LEU A 1 266 ? -27.563 2.240   -45.106 1.00 41.70  ? 247 LEU A CD1   1 
ATOM   1854 C CD2   . LEU A 1 266 ? -26.804 3.092   -47.327 1.00 47.81  ? 247 LEU A CD2   1 
ATOM   1855 N N     . THR A 1 267 ? -29.820 -1.058  -48.666 1.00 41.29  ? 248 THR A N     1 
ATOM   1856 C CA    . THR A 1 267 ? -29.710 -2.461  -49.042 1.00 45.08  ? 248 THR A CA    1 
ATOM   1857 C C     . THR A 1 267 ? -30.795 -2.882  -50.036 1.00 44.89  ? 248 THR A C     1 
ATOM   1858 O O     . THR A 1 267 ? -30.775 -4.009  -50.502 1.00 47.69  ? 248 THR A O     1 
ATOM   1859 C CB    . THR A 1 267 ? -29.867 -3.359  -47.815 1.00 45.25  ? 248 THR A CB    1 
ATOM   1860 O OG1   . THR A 1 267 ? -31.229 -3.236  -47.377 1.00 40.45  ? 248 THR A OG1   1 
ATOM   1861 C CG2   . THR A 1 267 ? -28.913 -2.993  -46.698 1.00 46.50  ? 248 THR A CG2   1 
ATOM   1862 N N     . GLY A 1 268 ? -31.766 -2.007  -50.315 1.00 48.29  ? 249 GLY A N     1 
ATOM   1863 C CA    . GLY A 1 268 ? -32.815 -2.306  -51.282 1.00 51.76  ? 249 GLY A CA    1 
ATOM   1864 C C     . GLY A 1 268 ? -34.045 -2.962  -50.650 1.00 57.49  ? 249 GLY A C     1 
ATOM   1865 O O     . GLY A 1 268 ? -35.064 -3.143  -51.312 1.00 52.25  ? 249 GLY A O     1 
ATOM   1866 N N     . GLN A 1 269 ? -33.970 -3.287  -49.355 1.00 54.23  ? 250 GLN A N     1 
ATOM   1867 C CA    . GLN A 1 269 ? -34.974 -4.128  -48.722 1.00 57.21  ? 250 GLN A CA    1 
ATOM   1868 C C     . GLN A 1 269 ? -35.031 -3.784  -47.232 1.00 55.03  ? 250 GLN A C     1 
ATOM   1869 O O     . GLN A 1 269 ? -33.986 -3.667  -46.592 1.00 48.18  ? 250 GLN A O     1 
ATOM   1870 C CB    . GLN A 1 269 ? -34.596 -5.572  -49.072 1.00 64.12  ? 250 GLN A CB    1 
ATOM   1871 C CG    . GLN A 1 269 ? -35.206 -6.665  -48.212 1.00 71.21  ? 250 GLN A CG    1 
ATOM   1872 C CD    . GLN A 1 269 ? -34.704 -8.036  -48.620 1.00 78.86  ? 250 GLN A CD    1 
ATOM   1873 O OE1   . GLN A 1 269 ? -34.880 -9.026  -47.914 1.00 79.44  ? 250 GLN A OE1   1 
ATOM   1874 N NE2   . GLN A 1 269 ? -34.046 -8.113  -49.765 1.00 83.39  ? 250 GLN A NE2   1 
ATOM   1875 N N     . PRO A 1 270 ? -36.235 -3.609  -46.631 1.00 49.65  ? 251 PRO A N     1 
ATOM   1876 C CA    . PRO A 1 270 ? -36.354 -3.396  -45.187 1.00 45.21  ? 251 PRO A CA    1 
ATOM   1877 C C     . PRO A 1 270 ? -36.069 -4.717  -44.472 1.00 41.62  ? 251 PRO A C     1 
ATOM   1878 O O     . PRO A 1 270 ? -36.045 -5.769  -45.102 1.00 38.26  ? 251 PRO A O     1 
ATOM   1879 C CB    . PRO A 1 270 ? -37.825 -2.989  -44.992 1.00 49.63  ? 251 PRO A CB    1 
ATOM   1880 C CG    . PRO A 1 270 ? -38.549 -3.727  -46.114 1.00 50.83  ? 251 PRO A CG    1 
ATOM   1881 C CD    . PRO A 1 270 ? -37.561 -3.734  -47.270 1.00 53.59  ? 251 PRO A CD    1 
ATOM   1882 N N     . LEU A 1 271 ? -35.865 -4.649  -43.156 1.00 42.06  ? 252 LEU A N     1 
ATOM   1883 C CA    . LEU A 1 271 ? -35.595 -5.845  -42.368 1.00 42.68  ? 252 LEU A CA    1 
ATOM   1884 C C     . LEU A 1 271 ? -36.911 -6.554  -42.106 1.00 42.11  ? 252 LEU A C     1 
ATOM   1885 O O     . LEU A 1 271 ? -37.936 -5.879  -41.970 1.00 41.80  ? 252 LEU A O     1 
ATOM   1886 C CB    . LEU A 1 271 ? -34.955 -5.451  -41.038 1.00 42.06  ? 252 LEU A CB    1 
ATOM   1887 C CG    . LEU A 1 271 ? -33.524 -4.936  -41.120 1.00 44.68  ? 252 LEU A CG    1 
ATOM   1888 C CD1   . LEU A 1 271 ? -33.174 -4.180  -39.854 1.00 46.39  ? 252 LEU A CD1   1 
ATOM   1889 C CD2   . LEU A 1 271 ? -32.550 -6.077  -41.347 1.00 47.26  ? 252 LEU A CD2   1 
ATOM   1890 N N     . PRO A 1 272 ? -36.898 -7.900  -41.997 1.00 45.16  ? 253 PRO A N     1 
ATOM   1891 C CA    . PRO A 1 272 ? -38.052 -8.651  -41.494 1.00 47.81  ? 253 PRO A CA    1 
ATOM   1892 C C     . PRO A 1 272 ? -38.204 -8.481  -39.981 1.00 49.11  ? 253 PRO A C     1 
ATOM   1893 O O     . PRO A 1 272 ? -37.921 -9.372  -39.190 1.00 60.25  ? 253 PRO A O     1 
ATOM   1894 C CB    . PRO A 1 272 ? -37.764 -10.118 -41.886 1.00 50.03  ? 253 PRO A CB    1 
ATOM   1895 C CG    . PRO A 1 272 ? -36.279 -10.192 -42.229 1.00 46.90  ? 253 PRO A CG    1 
ATOM   1896 C CD    . PRO A 1 272 ? -35.752 -8.770  -42.311 1.00 46.11  ? 253 PRO A CD    1 
ATOM   1897 N N     . ALA A 1 273 ? -38.643 -7.304  -39.560 1.00 50.00  ? 254 ALA A N     1 
ATOM   1898 C CA    . ALA A 1 273 ? -38.540 -6.932  -38.163 1.00 46.06  ? 254 ALA A CA    1 
ATOM   1899 C C     . ALA A 1 273 ? -39.881 -7.133  -37.471 1.00 52.81  ? 254 ALA A C     1 
ATOM   1900 O O     . ALA A 1 273 ? -40.888 -6.617  -37.945 1.00 52.97  ? 254 ALA A O     1 
ATOM   1901 C CB    . ALA A 1 273 ? -38.097 -5.492  -38.063 1.00 48.46  ? 254 ALA A CB    1 
ATOM   1902 N N     . ARG A 1 274 ? -39.855 -7.820  -36.319 1.00 52.86  ? 255 ARG A N     1 
ATOM   1903 C CA    . ARG A 1 274 ? -41.011 -7.921  -35.434 1.00 55.58  ? 255 ARG A CA    1 
ATOM   1904 C C     . ARG A 1 274 ? -41.236 -6.582  -34.733 1.00 56.38  ? 255 ARG A C     1 
ATOM   1905 O O     . ARG A 1 274 ? -42.368 -6.100  -34.656 1.00 56.73  ? 255 ARG A O     1 
ATOM   1906 C CB    . ARG A 1 274 ? -40.832 -9.025  -34.379 1.00 62.70  ? 255 ARG A CB    1 
ATOM   1907 C CG    . ARG A 1 274 ? -40.111 -10.264 -34.892 1.00 71.73  ? 255 ARG A CG    1 
ATOM   1908 C CD    . ARG A 1 274 ? -40.487 -11.590 -34.248 1.00 73.65  ? 255 ARG A CD    1 
ATOM   1909 N NE    . ARG A 1 274 ? -40.071 -12.682 -35.121 1.00 79.88  ? 255 ARG A NE    1 
ATOM   1910 C CZ    . ARG A 1 274 ? -40.526 -12.883 -36.360 1.00 85.80  ? 255 ARG A CZ    1 
ATOM   1911 N NH1   . ARG A 1 274 ? -39.923 -13.747 -37.154 1.00 88.41  ? 255 ARG A NH1   1 
ATOM   1912 N NH2   . ARG A 1 274 ? -41.542 -12.180 -36.833 1.00 87.44  ? 255 ARG A NH2   1 
ATOM   1913 N N     . GLU A 1 275 ? -40.142 -6.003  -34.215 1.00 52.41  ? 256 GLU A N     1 
ATOM   1914 C CA    . GLU A 1 275 ? -40.176 -4.800  -33.405 1.00 48.28  ? 256 GLU A CA    1 
ATOM   1915 C C     . GLU A 1 275 ? -38.789 -4.163  -33.406 1.00 46.94  ? 256 GLU A C     1 
ATOM   1916 O O     . GLU A 1 275 ? -37.775 -4.858  -33.360 1.00 42.86  ? 256 GLU A O     1 
ATOM   1917 C CB    . GLU A 1 275 ? -40.582 -5.166  -31.978 1.00 49.97  ? 256 GLU A CB    1 
ATOM   1918 C CG    . GLU A 1 275 ? -40.484 -4.025  -30.987 1.00 61.72  ? 256 GLU A CG    1 
ATOM   1919 C CD    . GLU A 1 275 ? -40.951 -4.375  -29.583 1.00 69.57  ? 256 GLU A CD    1 
ATOM   1920 O OE1   . GLU A 1 275 ? -41.422 -5.515  -29.391 1.00 70.72  ? 256 GLU A OE1   1 
ATOM   1921 O OE2   . GLU A 1 275 ? -40.839 -3.510  -28.684 1.00 76.87  ? 256 GLU A OE2   1 
ATOM   1922 N N     . VAL A 1 276 ? -38.756 -2.830  -33.430 1.00 45.36  ? 257 VAL A N     1 
ATOM   1923 C CA    . VAL A 1 276 ? -37.535 -2.110  -33.129 1.00 42.86  ? 257 VAL A CA    1 
ATOM   1924 C C     . VAL A 1 276 ? -37.532 -1.861  -31.630 1.00 44.13  ? 257 VAL A C     1 
ATOM   1925 O O     . VAL A 1 276 ? -38.331 -1.067  -31.147 1.00 52.25  ? 257 VAL A O     1 
ATOM   1926 C CB    . VAL A 1 276 ? -37.447 -0.800  -33.928 1.00 42.84  ? 257 VAL A CB    1 
ATOM   1927 C CG1   . VAL A 1 276 ? -36.227 0.016   -33.515 1.00 43.88  ? 257 VAL A CG1   1 
ATOM   1928 C CG2   . VAL A 1 276 ? -37.458 -1.068  -35.426 1.00 44.03  ? 257 VAL A CG2   1 
ATOM   1929 N N     . LEU A 1 277 ? -36.640 -2.545  -30.904 1.00 39.31  ? 258 LEU A N     1 
ATOM   1930 C CA    . LEU A 1 277 ? -36.555 -2.402  -29.459 1.00 40.38  ? 258 LEU A CA    1 
ATOM   1931 C C     . LEU A 1 277 ? -36.155 -0.984  -29.067 1.00 42.87  ? 258 LEU A C     1 
ATOM   1932 O O     . LEU A 1 277 ? -36.761 -0.410  -28.188 1.00 42.73  ? 258 LEU A O     1 
ATOM   1933 C CB    . LEU A 1 277 ? -35.539 -3.393  -28.895 1.00 41.45  ? 258 LEU A CB    1 
ATOM   1934 C CG    . LEU A 1 277 ? -35.869 -4.859  -29.121 1.00 43.84  ? 258 LEU A CG    1 
ATOM   1935 C CD1   . LEU A 1 277 ? -34.761 -5.724  -28.542 1.00 45.05  ? 258 LEU A CD1   1 
ATOM   1936 C CD2   . LEU A 1 277 ? -37.220 -5.213  -28.506 1.00 46.15  ? 258 LEU A CD2   1 
ATOM   1937 N N     . TRP A 1 278 ? -35.074 -0.476  -29.652 1.00 37.77  ? 259 TRP A N     1 
ATOM   1938 C CA    . TRP A 1 278 ? -34.633 0.896   -29.462 1.00 38.24  ? 259 TRP A CA    1 
ATOM   1939 C C     . TRP A 1 278 ? -33.810 1.281   -30.693 1.00 38.67  ? 259 TRP A C     1 
ATOM   1940 O O     . TRP A 1 278 ? -33.255 0.409   -31.371 1.00 33.65  ? 259 TRP A O     1 
ATOM   1941 C CB    . TRP A 1 278 ? -33.819 1.055   -28.178 1.00 36.96  ? 259 TRP A CB    1 
ATOM   1942 C CG    . TRP A 1 278 ? -32.539 0.272   -28.189 1.00 36.99  ? 259 TRP A CG    1 
ATOM   1943 C CD1   . TRP A 1 278 ? -32.360 -1.048  -27.876 1.00 37.92  ? 259 TRP A CD1   1 
ATOM   1944 C CD2   . TRP A 1 278 ? -31.248 0.762   -28.594 1.00 37.21  ? 259 TRP A CD2   1 
ATOM   1945 N NE1   . TRP A 1 278 ? -31.044 -1.408  -28.036 1.00 35.77  ? 259 TRP A NE1   1 
ATOM   1946 C CE2   . TRP A 1 278 ? -30.340 -0.321  -28.487 1.00 37.80  ? 259 TRP A CE2   1 
ATOM   1947 C CE3   . TRP A 1 278 ? -30.779 1.993   -29.058 1.00 39.26  ? 259 TRP A CE3   1 
ATOM   1948 C CZ2   . TRP A 1 278 ? -28.990 -0.194  -28.807 1.00 37.49  ? 259 TRP A CZ2   1 
ATOM   1949 C CZ3   . TRP A 1 278 ? -29.440 2.123   -29.360 1.00 39.24  ? 259 TRP A CZ3   1 
ATOM   1950 C CH2   . TRP A 1 278 ? -28.560 1.036   -29.243 1.00 36.62  ? 259 TRP A CH2   1 
ATOM   1951 N N     . ALA A 1 279 ? -33.751 2.582   -30.982 1.00 36.61  ? 260 ALA A N     1 
ATOM   1952 C CA    . ALA A 1 279 ? -32.948 3.112   -32.070 1.00 35.41  ? 260 ALA A CA    1 
ATOM   1953 C C     . ALA A 1 279 ? -32.695 4.602   -31.839 1.00 40.34  ? 260 ALA A C     1 
ATOM   1954 O O     . ALA A 1 279 ? -33.618 5.333   -31.447 1.00 36.92  ? 260 ALA A O     1 
ATOM   1955 C CB    . ALA A 1 279 ? -33.636 2.870   -33.383 1.00 38.72  ? 260 ALA A CB    1 
ATOM   1956 N N     . ARG A 1 280 ? -31.456 5.042   -32.095 1.00 35.32  ? 261 ARG A N     1 
ATOM   1957 C CA    . ARG A 1 280 ? -31.091 6.435   -31.904 1.00 39.25  ? 261 ARG A CA    1 
ATOM   1958 C C     . ARG A 1 280 ? -30.180 6.924   -33.032 1.00 42.19  ? 261 ARG A C     1 
ATOM   1959 O O     . ARG A 1 280 ? -29.440 6.179   -33.676 1.00 31.71  ? 261 ARG A O     1 
ATOM   1960 C CB    . ARG A 1 280 ? -30.483 6.635   -30.513 1.00 47.67  ? 261 ARG A CB    1 
ATOM   1961 C CG    . ARG A 1 280 ? -29.034 6.206   -30.395 1.00 50.15  ? 261 ARG A CG    1 
ATOM   1962 C CD    . ARG A 1 280 ? -28.410 6.319   -29.015 1.00 61.29  ? 261 ARG A CD    1 
ATOM   1963 N NE    . ARG A 1 280 ? -26.947 6.340   -29.165 1.00 66.59  ? 261 ARG A NE    1 
ATOM   1964 C CZ    . ARG A 1 280 ? -26.113 5.345   -28.845 1.00 66.37  ? 261 ARG A CZ    1 
ATOM   1965 N NH1   . ARG A 1 280 ? -26.539 4.261   -28.210 1.00 71.88  ? 261 ARG A NH1   1 
ATOM   1966 N NH2   . ARG A 1 280 ? -24.830 5.456   -29.140 1.00 56.88  ? 261 ARG A NH2   1 
ATOM   1967 N N     . ARG A 1 281 ? -30.253 8.229   -33.266 1.00 34.26  ? 262 ARG A N     1 
ATOM   1968 C CA    . ARG A 1 281 ? -29.413 8.905   -34.228 1.00 35.86  ? 262 ARG A CA    1 
ATOM   1969 C C     . ARG A 1 281 ? -28.133 9.274   -33.493 1.00 37.96  ? 262 ARG A C     1 
ATOM   1970 O O     . ARG A 1 281 ? -28.197 9.763   -32.378 1.00 41.74  ? 262 ARG A O     1 
ATOM   1971 C CB    . ARG A 1 281 ? -30.227 10.089  -34.780 1.00 45.91  ? 262 ARG A CB    1 
ATOM   1972 C CG    . ARG A 1 281 ? -29.430 11.163  -35.509 1.00 51.27  ? 262 ARG A CG    1 
ATOM   1973 C CD    . ARG A 1 281 ? -29.082 10.771  -36.929 1.00 50.24  ? 262 ARG A CD    1 
ATOM   1974 N NE    . ARG A 1 281 ? -30.244 10.474  -37.748 1.00 49.15  ? 262 ARG A NE    1 
ATOM   1975 C CZ    . ARG A 1 281 ? -30.173 9.865   -38.925 1.00 52.83  ? 262 ARG A CZ    1 
ATOM   1976 N NH1   . ARG A 1 281 ? -31.278 9.507   -39.547 1.00 54.96  ? 262 ARG A NH1   1 
ATOM   1977 N NH2   . ARG A 1 281 ? -28.991 9.584   -39.459 1.00 53.41  ? 262 ARG A NH2   1 
ATOM   1978 N N     . PHE A 1 282 ? -26.968 8.979   -34.077 1.00 32.97  ? 263 PHE A N     1 
ATOM   1979 C CA    . PHE A 1 282 ? -25.697 9.362   -33.490 1.00 33.43  ? 263 PHE A CA    1 
ATOM   1980 C C     . PHE A 1 282 ? -24.971 10.257  -34.487 1.00 31.61  ? 263 PHE A C     1 
ATOM   1981 O O     . PHE A 1 282 ? -25.213 10.181  -35.687 1.00 30.58  ? 263 PHE A O     1 
ATOM   1982 C CB    . PHE A 1 282 ? -24.903 8.130   -33.068 1.00 33.77  ? 263 PHE A CB    1 
ATOM   1983 C CG    . PHE A 1 282 ? -24.372 7.324   -34.223 1.00 31.80  ? 263 PHE A CG    1 
ATOM   1984 C CD1   . PHE A 1 282 ? -25.110 6.282   -34.756 1.00 31.02  ? 263 PHE A CD1   1 
ATOM   1985 C CD2   . PHE A 1 282 ? -23.112 7.580   -34.742 1.00 32.30  ? 263 PHE A CD2   1 
ATOM   1986 C CE1   . PHE A 1 282 ? -24.640 5.568   -35.845 1.00 33.35  ? 263 PHE A CE1   1 
ATOM   1987 C CE2   . PHE A 1 282 ? -22.635 6.851   -35.828 1.00 34.74  ? 263 PHE A CE2   1 
ATOM   1988 C CZ    . PHE A 1 282 ? -23.400 5.851   -36.377 1.00 32.51  ? 263 PHE A CZ    1 
ATOM   1989 N N     . THR A 1 283 ? -24.116 11.153  -33.981 1.00 31.85  ? 264 THR A N     1 
ATOM   1990 C CA    . THR A 1 283 ? -23.265 11.954  -34.836 1.00 33.53  ? 264 THR A CA    1 
ATOM   1991 C C     . THR A 1 283 ? -21.846 11.855  -34.303 1.00 34.21  ? 264 THR A C     1 
ATOM   1992 O O     . THR A 1 283 ? -21.619 12.228  -33.171 1.00 32.25  ? 264 THR A O     1 
ATOM   1993 C CB    . THR A 1 283 ? -23.714 13.419  -34.887 1.00 37.98  ? 264 THR A CB    1 
ATOM   1994 O OG1   . THR A 1 283 ? -24.953 13.466  -35.583 1.00 42.23  ? 264 THR A OG1   1 
ATOM   1995 C CG2   . THR A 1 283 ? -22.735 14.321  -35.603 1.00 37.93  ? 264 THR A CG2   1 
ATOM   1996 N N     . SER A 1 284 ? -20.898 11.332  -35.097 1.00 31.07  ? 265 SER A N     1 
ATOM   1997 C CA    . SER A 1 284 ? -19.534 11.163  -34.619 1.00 30.84  ? 265 SER A CA    1 
ATOM   1998 C C     . SER A 1 284 ? -18.706 12.369  -35.034 1.00 31.96  ? 265 SER A C     1 
ATOM   1999 O O     . SER A 1 284 ? -18.718 12.759  -36.193 1.00 38.56  ? 265 SER A O     1 
ATOM   2000 C CB    . SER A 1 284 ? -18.888 9.917   -35.176 1.00 34.44  ? 265 SER A CB    1 
ATOM   2001 O OG    . SER A 1 284 ? -19.652 8.747   -34.890 1.00 38.47  ? 265 SER A OG    1 
ATOM   2002 N N     . HIS A 1 285 ? -17.948 12.917  -34.094 1.00 30.31  ? 266 HIS A N     1 
ATOM   2003 C CA    . HIS A 1 285 ? -17.049 14.002  -34.393 1.00 32.24  ? 266 HIS A CA    1 
ATOM   2004 C C     . HIS A 1 285 ? -15.657 13.402  -34.467 1.00 33.42  ? 266 HIS A C     1 
ATOM   2005 O O     . HIS A 1 285 ? -15.386 12.390  -33.834 1.00 32.63  ? 266 HIS A O     1 
ATOM   2006 C CB    . HIS A 1 285 ? -17.219 15.151  -33.391 1.00 35.39  ? 266 HIS A CB    1 
ATOM   2007 C CG    . HIS A 1 285 ? -18.611 15.716  -33.455 1.00 41.18  ? 266 HIS A CG    1 
ATOM   2008 N ND1   . HIS A 1 285 ? -18.956 16.687  -34.380 1.00 45.47  ? 266 HIS A ND1   1 
ATOM   2009 C CD2   . HIS A 1 285 ? -19.760 15.372  -32.824 1.00 41.12  ? 266 HIS A CD2   1 
ATOM   2010 C CE1   . HIS A 1 285 ? -20.257 16.966  -34.259 1.00 43.63  ? 266 HIS A CE1   1 
ATOM   2011 N NE2   . HIS A 1 285 ? -20.761 16.187  -33.315 1.00 43.00  ? 266 HIS A NE2   1 
ATOM   2012 N N     . SER A 1 286 ? -14.832 13.999  -35.321 1.00 28.78  ? 267 SER A N     1 
ATOM   2013 C CA    . SER A 1 286 ? -13.435 13.629  -35.413 1.00 27.99  ? 267 SER A CA    1 
ATOM   2014 C C     . SER A 1 286 ? -12.621 14.611  -34.597 1.00 28.67  ? 267 SER A C     1 
ATOM   2015 O O     . SER A 1 286 ? -12.616 15.803  -34.893 1.00 27.75  ? 267 SER A O     1 
ATOM   2016 C CB    . SER A 1 286 ? -13.012 13.633  -36.863 1.00 31.82  ? 267 SER A CB    1 
ATOM   2017 O OG    . SER A 1 286 ? -11.642 13.273  -37.000 1.00 27.89  ? 267 SER A OG    1 
ATOM   2018 N N     . GLY A 1 287 ? -11.901 14.112  -33.599 1.00 26.42  ? 268 GLY A N     1 
ATOM   2019 C CA    . GLY A 1 287 ? -11.090 14.979  -32.775 1.00 29.77  ? 268 GLY A CA    1 
ATOM   2020 C C     . GLY A 1 287 ? -9.992  14.227  -32.042 1.00 27.59  ? 268 GLY A C     1 
ATOM   2021 O O     . GLY A 1 287 ? -10.113 13.025  -31.781 1.00 26.51  ? 268 GLY A O     1 
ATOM   2022 N N     . ASN A 1 288 ? -8.904  14.960  -31.780 1.00 25.69  ? 269 ASN A N     1 
ATOM   2023 C CA    . ASN A 1 288 ? -7.865  14.516  -30.875 1.00 25.23  ? 269 ASN A CA    1 
ATOM   2024 C C     . ASN A 1 288 ? -7.568  15.706  -29.967 1.00 26.22  ? 269 ASN A C     1 
ATOM   2025 O O     . ASN A 1 288 ? -7.194  16.758  -30.481 1.00 26.32  ? 269 ASN A O     1 
ATOM   2026 C CB    . ASN A 1 288 ? -6.641  14.049  -31.651 1.00 24.82  ? 269 ASN A CB    1 
ATOM   2027 C CG    . ASN A 1 288 ? -5.597  13.326  -30.825 1.00 25.93  ? 269 ASN A CG    1 
ATOM   2028 O OD1   . ASN A 1 288 ? -4.381  13.529  -30.965 1.00 29.17  ? 269 ASN A OD1   1 
ATOM   2029 N ND2   . ASN A 1 288 ? -6.062  12.418  -30.008 1.00 24.93  ? 269 ASN A ND2   1 
ATOM   2030 N N     . ALA A 1 289 ? -7.606  15.517  -28.641 1.00 27.04  ? 270 ALA A N     1 
ATOM   2031 C CA    . ALA A 1 289 ? -7.389  16.627  -27.716 1.00 28.09  ? 270 ALA A CA    1 
ATOM   2032 C C     . ALA A 1 289 ? -5.968  17.180  -27.862 1.00 28.67  ? 270 ALA A C     1 
ATOM   2033 O O     . ALA A 1 289 ? -4.997  16.458  -28.047 1.00 25.91  ? 270 ALA A O     1 
ATOM   2034 C CB    . ALA A 1 289 ? -7.695  16.181  -26.303 1.00 27.23  ? 270 ALA A CB    1 
ATOM   2035 N N     . GLU A 1 290 ? -5.833  18.514  -27.830 1.00 28.73  ? 271 GLU A N     1 
ATOM   2036 C CA    . GLU A 1 290 ? -4.535  19.139  -28.071 1.00 31.19  ? 271 GLU A CA    1 
ATOM   2037 C C     . GLU A 1 290 ? -3.519  18.751  -27.017 1.00 26.44  ? 271 GLU A C     1 
ATOM   2038 O O     . GLU A 1 290 ? -2.334  18.683  -27.294 1.00 30.45  ? 271 GLU A O     1 
ATOM   2039 C CB    . GLU A 1 290 ? -4.618  20.671  -28.053 1.00 39.17  ? 271 GLU A CB    1 
ATOM   2040 C CG    . GLU A 1 290 ? -5.302  21.229  -29.277 1.00 55.34  ? 271 GLU A CG    1 
ATOM   2041 C CD    . GLU A 1 290 ? -5.033  22.698  -29.570 1.00 65.19  ? 271 GLU A CD    1 
ATOM   2042 O OE1   . GLU A 1 290 ? -4.622  23.416  -28.625 1.00 54.34  ? 271 GLU A OE1   1 
ATOM   2043 O OE2   . GLU A 1 290 ? -5.226  23.106  -30.752 1.00 64.73  ? 271 GLU A OE2   1 
ATOM   2044 N N     . ARG A 1 291 ? -3.954  18.592  -25.767 1.00 29.40  ? 272 ARG A N     1 
ATOM   2045 C CA    . ARG A 1 291 ? -3.128  17.910  -24.788 1.00 33.63  ? 272 ARG A CA    1 
ATOM   2046 C C     . ARG A 1 291 ? -3.959  16.972  -23.917 1.00 27.38  ? 272 ARG A C     1 
ATOM   2047 O O     . ARG A 1 291 ? -5.159  17.154  -23.696 1.00 30.51  ? 272 ARG A O     1 
ATOM   2048 C CB    . ARG A 1 291 ? -2.285  18.863  -23.952 1.00 42.64  ? 272 ARG A CB    1 
ATOM   2049 C CG    . ARG A 1 291 ? -3.010  20.092  -23.460 1.00 48.91  ? 272 ARG A CG    1 
ATOM   2050 C CD    . ARG A 1 291 ? -1.936  21.088  -23.047 1.00 57.12  ? 272 ARG A CD    1 
ATOM   2051 N NE    . ARG A 1 291 ? -2.355  21.786  -21.848 1.00 60.57  ? 272 ARG A NE    1 
ATOM   2052 C CZ    . ARG A 1 291 ? -3.387  22.619  -21.796 1.00 61.11  ? 272 ARG A CZ    1 
ATOM   2053 N NH1   . ARG A 1 291 ? -4.030  22.957  -22.902 1.00 61.04  ? 272 ARG A NH1   1 
ATOM   2054 N NH2   . ARG A 1 291 ? -3.752  23.123  -20.633 1.00 54.10  ? 272 ARG A NH2   1 
ATOM   2055 N N     . TYR A 1 292 ? -3.266  15.913  -23.495 1.00 26.50  ? 273 TYR A N     1 
ATOM   2056 C CA    . TYR A 1 292 ? -3.891  14.844  -22.731 1.00 24.72  ? 273 TYR A CA    1 
ATOM   2057 C C     . TYR A 1 292 ? -3.698  15.092  -21.227 1.00 27.86  ? 273 TYR A C     1 
ATOM   2058 O O     . TYR A 1 292 ? -4.269  14.369  -20.410 1.00 26.24  ? 273 TYR A O     1 
ATOM   2059 C CB    . TYR A 1 292 ? -3.295  13.495  -23.139 1.00 25.44  ? 273 TYR A CB    1 
ATOM   2060 C CG    . TYR A 1 292 ? -3.810  12.889  -24.423 1.00 24.83  ? 273 TYR A CG    1 
ATOM   2061 C CD1   . TYR A 1 292 ? -4.347  13.639  -25.458 1.00 24.68  ? 273 TYR A CD1   1 
ATOM   2062 C CD2   . TYR A 1 292 ? -3.762  11.511  -24.590 1.00 27.45  ? 273 TYR A CD2   1 
ATOM   2063 C CE1   . TYR A 1 292 ? -4.816  13.037  -26.632 1.00 24.71  ? 273 TYR A CE1   1 
ATOM   2064 C CE2   . TYR A 1 292 ? -4.197  10.897  -25.755 1.00 24.48  ? 273 TYR A CE2   1 
ATOM   2065 C CZ    . TYR A 1 292 ? -4.745  11.649  -26.769 1.00 24.46  ? 273 TYR A CZ    1 
ATOM   2066 O OH    . TYR A 1 292 ? -5.119  11.055  -27.936 1.00 23.59  ? 273 TYR A OH    1 
ATOM   2067 N N     . ARG A 1 293 ? -2.864  16.086  -20.852 1.00 27.81  ? 274 ARG A N     1 
ATOM   2068 C CA    . ARG A 1 293 ? -2.617  16.407  -19.442 1.00 26.58  ? 274 ARG A CA    1 
ATOM   2069 C C     . ARG A 1 293 ? -2.673  17.927  -19.265 1.00 28.73  ? 274 ARG A C     1 
ATOM   2070 O O     . ARG A 1 293 ? -2.167  18.656  -20.104 1.00 28.45  ? 274 ARG A O     1 
ATOM   2071 C CB    . ARG A 1 293 ? -1.253  15.889  -18.997 1.00 25.75  ? 274 ARG A CB    1 
ATOM   2072 C CG    . ARG A 1 293 ? -0.894  16.260  -17.556 1.00 27.40  ? 274 ARG A CG    1 
ATOM   2073 C CD    . ARG A 1 293 ? 0.550   15.984  -17.201 1.00 29.94  ? 274 ARG A CD    1 
ATOM   2074 N NE    . ARG A 1 293 ? 0.772   16.106  -15.759 1.00 31.42  ? 274 ARG A NE    1 
ATOM   2075 C CZ    . ARG A 1 293 ? 1.885   15.763  -15.135 1.00 31.58  ? 274 ARG A CZ    1 
ATOM   2076 N NH1   . ARG A 1 293 ? 2.940   15.398  -15.834 1.00 36.32  ? 274 ARG A NH1   1 
ATOM   2077 N NH2   . ARG A 1 293 ? 1.953   15.868  -13.820 1.00 35.72  ? 274 ARG A NH2   1 
ATOM   2078 N N     . SER A 1 294 ? -3.330  18.388  -18.199 1.00 31.43  ? 275 SER A N     1 
ATOM   2079 C CA    . SER A 1 294 ? -3.259  19.781  -17.772 1.00 31.37  ? 275 SER A CA    1 
ATOM   2080 C C     . SER A 1 294 ? -3.142  19.800  -16.245 1.00 28.54  ? 275 SER A C     1 
ATOM   2081 O O     . SER A 1 294 ? -4.124  19.604  -15.555 1.00 32.38  ? 275 SER A O     1 
ATOM   2082 C CB    . SER A 1 294 ? -4.445  20.553  -18.267 1.00 34.96  ? 275 SER A CB    1 
ATOM   2083 O OG    . SER A 1 294 ? -4.314  21.928  -17.931 1.00 35.54  ? 275 SER A OG    1 
ATOM   2084 N N     . GLY A 1 295 ? -1.917  19.963  -15.768 1.00 31.44  ? 276 GLY A N     1 
ATOM   2085 C CA    . GLY A 1 295 ? -1.591  19.924  -14.357 1.00 30.88  ? 276 GLY A CA    1 
ATOM   2086 C C     . GLY A 1 295 ? -1.871  18.532  -13.798 1.00 31.64  ? 276 GLY A C     1 
ATOM   2087 O O     . GLY A 1 295 ? -1.202  17.566  -14.168 1.00 30.76  ? 276 GLY A O     1 
ATOM   2088 N N     . ARG A 1 296 ? -2.900  18.459  -12.952 1.00 28.46  ? 277 ARG A N     1 
ATOM   2089 C CA    . ARG A 1 296 ? -3.264  17.219  -12.300 1.00 28.90  ? 277 ARG A CA    1 
ATOM   2090 C C     . ARG A 1 296 ? -4.511  16.634  -12.959 1.00 25.25  ? 277 ARG A C     1 
ATOM   2091 O O     . ARG A 1 296 ? -5.116  15.737  -12.379 1.00 30.16  ? 277 ARG A O     1 
ATOM   2092 C CB    . ARG A 1 296 ? -3.499  17.468  -10.797 1.00 30.25  ? 277 ARG A CB    1 
ATOM   2093 C CG    . ARG A 1 296 ? -2.226  17.668  -9.989  1.00 29.90  ? 277 ARG A CG    1 
ATOM   2094 C CD    . ARG A 1 296 ? -2.574  18.078  -8.540  1.00 32.85  ? 277 ARG A CD    1 
ATOM   2095 N NE    . ARG A 1 296 ? -1.386  18.069  -7.697  1.00 32.24  ? 277 ARG A NE    1 
ATOM   2096 C CZ    . ARG A 1 296 ? -0.794  16.977  -7.237  1.00 34.71  ? 277 ARG A CZ    1 
ATOM   2097 N NH1   . ARG A 1 296 ? -1.394  15.800  -7.297  1.00 34.68  ? 277 ARG A NH1   1 
ATOM   2098 N NH2   . ARG A 1 296 ? 0.393   17.062  -6.677  1.00 35.56  ? 277 ARG A NH2   1 
ATOM   2099 N N     . VAL A 1 297 ? -4.888  17.121  -14.152 1.00 26.30  ? 278 VAL A N     1 
ATOM   2100 C CA    . VAL A 1 297 ? -6.034  16.631  -14.909 1.00 27.80  ? 278 VAL A CA    1 
ATOM   2101 C C     . VAL A 1 297 ? -5.541  15.903  -16.167 1.00 27.62  ? 278 VAL A C     1 
ATOM   2102 O O     . VAL A 1 297 ? -4.703  16.413  -16.913 1.00 25.66  ? 278 VAL A O     1 
ATOM   2103 C CB    . VAL A 1 297 ? -7.002  17.768  -15.272 1.00 32.52  ? 278 VAL A CB    1 
ATOM   2104 C CG1   . VAL A 1 297 ? -8.148  17.304  -16.157 1.00 33.10  ? 278 VAL A CG1   1 
ATOM   2105 C CG2   . VAL A 1 297 ? -7.558  18.439  -14.025 1.00 35.20  ? 278 VAL A CG2   1 
ATOM   2106 N N     . PHE A 1 298 ? -6.084  14.699  -16.399 1.00 26.88  ? 279 PHE A N     1 
ATOM   2107 C CA    . PHE A 1 298 ? -5.719  13.896  -17.559 1.00 24.49  ? 279 PHE A CA    1 
ATOM   2108 C C     . PHE A 1 298 ? -6.976  13.556  -18.342 1.00 25.40  ? 279 PHE A C     1 
ATOM   2109 O O     . PHE A 1 298 ? -8.082  13.478  -17.790 1.00 27.66  ? 279 PHE A O     1 
ATOM   2110 C CB    . PHE A 1 298 ? -5.010  12.585  -17.154 1.00 25.19  ? 279 PHE A CB    1 
ATOM   2111 C CG    . PHE A 1 298 ? -3.638  12.750  -16.548 1.00 25.16  ? 279 PHE A CG    1 
ATOM   2112 C CD1   . PHE A 1 298 ? -3.483  13.120  -15.209 1.00 26.35  ? 279 PHE A CD1   1 
ATOM   2113 C CD2   . PHE A 1 298 ? -2.501  12.576  -17.303 1.00 27.68  ? 279 PHE A CD2   1 
ATOM   2114 C CE1   . PHE A 1 298 ? -2.224  13.276  -14.664 1.00 28.58  ? 279 PHE A CE1   1 
ATOM   2115 C CE2   . PHE A 1 298 ? -1.239  12.739  -16.750 1.00 29.86  ? 279 PHE A CE2   1 
ATOM   2116 C CZ    . PHE A 1 298 ? -1.104  13.095  -15.422 1.00 30.62  ? 279 PHE A CZ    1 
ATOM   2117 N N     . LEU A 1 299 ? -6.816  13.384  -19.675 1.00 24.72  ? 280 LEU A N     1 
ATOM   2118 C CA    . LEU A 1 299 ? -7.893  12.883  -20.521 1.00 25.58  ? 280 LEU A CA    1 
ATOM   2119 C C     . LEU A 1 299 ? -7.542  11.468  -20.997 1.00 25.32  ? 280 LEU A C     1 
ATOM   2120 O O     . LEU A 1 299 ? -6.384  11.204  -21.291 1.00 24.59  ? 280 LEU A O     1 
ATOM   2121 C CB    . LEU A 1 299 ? -8.055  13.768  -21.744 1.00 27.07  ? 280 LEU A CB    1 
ATOM   2122 C CG    . LEU A 1 299 ? -8.201  15.272  -21.483 1.00 26.00  ? 280 LEU A CG    1 
ATOM   2123 C CD1   . LEU A 1 299 ? -8.266  15.998  -22.821 1.00 26.63  ? 280 LEU A CD1   1 
ATOM   2124 C CD2   . LEU A 1 299 ? -9.449  15.542  -20.649 1.00 26.77  ? 280 LEU A CD2   1 
ATOM   2125 N N     . ALA A 1 300 ? -8.557  10.614  -21.084 1.00 24.56  ? 281 ALA A N     1 
ATOM   2126 C CA    . ALA A 1 300 ? -8.406  9.267   -21.623 1.00 25.49  ? 281 ALA A CA    1 
ATOM   2127 C C     . ALA A 1 300 ? -9.674  8.808   -22.335 1.00 25.17  ? 281 ALA A C     1 
ATOM   2128 O O     . ALA A 1 300 ? -10.783 9.223   -22.013 1.00 26.94  ? 281 ALA A O     1 
ATOM   2129 C CB    . ALA A 1 300 ? -8.050  8.315   -20.514 1.00 24.59  ? 281 ALA A CB    1 
ATOM   2130 N N     . GLY A 1 301 ? -9.482  7.890   -23.300 1.00 24.41  ? 282 GLY A N     1 
ATOM   2131 C CA    . GLY A 1 301 ? -10.567 7.332   -24.088 1.00 22.88  ? 282 GLY A CA    1 
ATOM   2132 C C     . GLY A 1 301 ? -11.202 8.389   -24.986 1.00 22.92  ? 282 GLY A C     1 
ATOM   2133 O O     . GLY A 1 301 ? -10.506 9.226   -25.564 1.00 23.89  ? 282 GLY A O     1 
ATOM   2134 N N     . ASP A 1 302 ? -12.522 8.296   -25.144 1.00 23.71  ? 283 ASP A N     1 
ATOM   2135 C CA    . ASP A 1 302 ? -13.235 9.138   -26.078 1.00 24.77  ? 283 ASP A CA    1 
ATOM   2136 C C     . ASP A 1 302 ? -13.067 10.605  -25.695 1.00 24.44  ? 283 ASP A C     1 
ATOM   2137 O O     . ASP A 1 302 ? -13.234 11.461  -26.556 1.00 26.21  ? 283 ASP A O     1 
ATOM   2138 C CB    . ASP A 1 302 ? -14.713 8.785   -26.155 1.00 26.40  ? 283 ASP A CB    1 
ATOM   2139 C CG    . ASP A 1 302 ? -15.093 7.595   -27.028 1.00 29.08  ? 283 ASP A CG    1 
ATOM   2140 O OD1   . ASP A 1 302 ? -14.195 6.930   -27.617 1.00 28.25  ? 283 ASP A OD1   1 
ATOM   2141 O OD2   . ASP A 1 302 ? -16.308 7.320   -27.112 1.00 28.78  ? 283 ASP A OD2   1 
ATOM   2142 N N     . ALA A 1 303 ? -12.799 10.887  -24.414 1.00 26.83  ? 284 ALA A N     1 
ATOM   2143 C CA    . ALA A 1 303 ? -12.612 12.277  -24.006 1.00 24.96  ? 284 ALA A CA    1 
ATOM   2144 C C     . ALA A 1 303 ? -11.360 12.831  -24.668 1.00 25.25  ? 284 ALA A C     1 
ATOM   2145 O O     . ALA A 1 303 ? -11.244 14.032  -24.829 1.00 25.26  ? 284 ALA A O     1 
ATOM   2146 C CB    . ALA A 1 303 ? -12.516 12.381  -22.508 1.00 28.22  ? 284 ALA A CB    1 
ATOM   2147 N N     . ALA A 1 304 ? -10.375 11.963  -24.979 1.00 24.97  ? 285 ALA A N     1 
ATOM   2148 C CA    . ALA A 1 304 ? -9.128  12.372  -25.600 1.00 23.04  ? 285 ALA A CA    1 
ATOM   2149 C C     . ALA A 1 304 ? -9.149  12.293  -27.139 1.00 24.75  ? 285 ALA A C     1 
ATOM   2150 O O     . ALA A 1 304 ? -8.348  12.948  -27.797 1.00 25.80  ? 285 ALA A O     1 
ATOM   2151 C CB    . ALA A 1 304 ? -7.999  11.512  -25.097 1.00 24.61  ? 285 ALA A CB    1 
ATOM   2152 N N     . HIS A 1 305 ? -9.975  11.422  -27.713 1.00 22.99  ? 286 HIS A N     1 
ATOM   2153 C CA    . HIS A 1 305 ? -9.994  11.207  -29.154 1.00 21.26  ? 286 HIS A CA    1 
ATOM   2154 C C     . HIS A 1 305 ? -11.349 10.613  -29.547 1.00 23.64  ? 286 HIS A C     1 
ATOM   2155 O O     . HIS A 1 305 ? -11.880 9.737   -28.869 1.00 25.97  ? 286 HIS A O     1 
ATOM   2156 C CB    . HIS A 1 305 ? -8.817  10.332  -29.601 1.00 23.23  ? 286 HIS A CB    1 
ATOM   2157 C CG    . HIS A 1 305 ? -8.601  9.162   -28.698 1.00 24.98  ? 286 HIS A CG    1 
ATOM   2158 N ND1   . HIS A 1 305 ? -9.472  8.088   -28.584 1.00 25.26  ? 286 HIS A ND1   1 
ATOM   2159 C CD2   . HIS A 1 305 ? -7.632  8.967   -27.811 1.00 27.63  ? 286 HIS A CD2   1 
ATOM   2160 C CE1   . HIS A 1 305 ? -9.020  7.285   -27.618 1.00 23.75  ? 286 HIS A CE1   1 
ATOM   2161 N NE2   . HIS A 1 305 ? -7.878  7.778   -27.172 1.00 25.71  ? 286 HIS A NE2   1 
ATOM   2162 N N     . SER A 1 306 ? -11.836 11.033  -30.712 1.00 23.95  ? 287 SER A N     1 
ATOM   2163 C CA    . SER A 1 306 ? -13.074 10.537  -31.258 1.00 26.84  ? 287 SER A CA    1 
ATOM   2164 C C     . SER A 1 306 ? -12.974 10.477  -32.779 1.00 22.33  ? 287 SER A C     1 
ATOM   2165 O O     . SER A 1 306 ? -12.258 11.250  -33.375 1.00 23.29  ? 287 SER A O     1 
ATOM   2166 C CB    . SER A 1 306 ? -14.198 11.452  -30.855 1.00 29.86  ? 287 SER A CB    1 
ATOM   2167 O OG    . SER A 1 306 ? -15.433 10.938  -31.302 1.00 39.89  ? 287 SER A OG    1 
ATOM   2168 N N     . PHE A 1 307 ? -13.766 9.589   -33.353 1.00 21.73  ? 288 PHE A N     1 
ATOM   2169 C CA    . PHE A 1 307 ? -13.828 9.343   -34.775 1.00 23.53  ? 288 PHE A CA    1 
ATOM   2170 C C     . PHE A 1 307 ? -14.945 8.334   -35.037 1.00 24.13  ? 288 PHE A C     1 
ATOM   2171 O O     . PHE A 1 307 ? -15.372 7.641   -34.132 1.00 27.28  ? 288 PHE A O     1 
ATOM   2172 C CB    . PHE A 1 307 ? -12.452 8.918   -35.294 1.00 22.76  ? 288 PHE A CB    1 
ATOM   2173 C CG    . PHE A 1 307 ? -11.723 7.883   -34.490 1.00 23.43  ? 288 PHE A CG    1 
ATOM   2174 C CD1   . PHE A 1 307 ? -12.083 6.545   -34.552 1.00 25.60  ? 288 PHE A CD1   1 
ATOM   2175 C CD2   . PHE A 1 307 ? -10.717 8.254   -33.607 1.00 25.79  ? 288 PHE A CD2   1 
ATOM   2176 C CE1   . PHE A 1 307 ? -11.389 5.614   -33.812 1.00 25.17  ? 288 PHE A CE1   1 
ATOM   2177 C CE2   . PHE A 1 307 ? -10.046 7.312   -32.854 1.00 24.52  ? 288 PHE A CE2   1 
ATOM   2178 C CZ    . PHE A 1 307 ? -10.407 5.997   -32.946 1.00 23.14  ? 288 PHE A CZ    1 
ATOM   2179 N N     . TYR A 1 308 ? -15.405 8.260   -36.282 1.00 24.01  ? 289 TYR A N     1 
ATOM   2180 C CA    . TYR A 1 308 ? -16.487 7.374   -36.635 1.00 24.46  ? 289 TYR A CA    1 
ATOM   2181 C C     . TYR A 1 308 ? -16.101 5.938   -36.316 1.00 25.27  ? 289 TYR A C     1 
ATOM   2182 O O     . TYR A 1 308 ? -14.988 5.521   -36.634 1.00 26.71  ? 289 TYR A O     1 
ATOM   2183 C CB    . TYR A 1 308 ? -16.780 7.515   -38.124 1.00 27.14  ? 289 TYR A CB    1 
ATOM   2184 C CG    . TYR A 1 308 ? -17.927 6.649   -38.547 1.00 27.39  ? 289 TYR A CG    1 
ATOM   2185 C CD1   . TYR A 1 308 ? -19.234 7.033   -38.307 1.00 28.59  ? 289 TYR A CD1   1 
ATOM   2186 C CD2   . TYR A 1 308 ? -17.701 5.412   -39.118 1.00 32.52  ? 289 TYR A CD2   1 
ATOM   2187 C CE1   . TYR A 1 308 ? -20.296 6.234   -38.680 1.00 32.31  ? 289 TYR A CE1   1 
ATOM   2188 C CE2   . TYR A 1 308 ? -18.753 4.588   -39.473 1.00 36.01  ? 289 TYR A CE2   1 
ATOM   2189 C CZ    . TYR A 1 308 ? -20.051 5.007   -39.268 1.00 35.62  ? 289 TYR A CZ    1 
ATOM   2190 O OH    . TYR A 1 308 ? -21.081 4.197   -39.645 1.00 37.49  ? 289 TYR A OH    1 
ATOM   2191 N N     . PRO A 1 309 ? -16.971 5.159   -35.643 1.00 25.75  ? 290 PRO A N     1 
ATOM   2192 C CA    . PRO A 1 309 ? -16.642 3.784   -35.259 1.00 27.03  ? 290 PRO A CA    1 
ATOM   2193 C C     . PRO A 1 309 ? -16.872 2.734   -36.344 1.00 28.27  ? 290 PRO A C     1 
ATOM   2194 O O     . PRO A 1 309 ? -17.792 1.925   -36.301 1.00 31.89  ? 290 PRO A O     1 
ATOM   2195 C CB    . PRO A 1 309 ? -17.591 3.560   -34.094 1.00 27.64  ? 290 PRO A CB    1 
ATOM   2196 C CG    . PRO A 1 309 ? -18.832 4.264   -34.547 1.00 27.81  ? 290 PRO A CG    1 
ATOM   2197 C CD    . PRO A 1 309 ? -18.303 5.547   -35.164 1.00 26.60  ? 290 PRO A CD    1 
ATOM   2198 N N     . LEU A 1 310 ? -16.001 2.735   -37.346 1.00 31.60  ? 291 LEU A N     1 
ATOM   2199 C CA    . LEU A 1 310 ? -16.185 1.814   -38.458 1.00 31.68  ? 291 LEU A CA    1 
ATOM   2200 C C     . LEU A 1 310 ? -15.756 0.400   -38.073 1.00 34.42  ? 291 LEU A C     1 
ATOM   2201 O O     . LEU A 1 310 ? -16.345 -0.566  -38.554 1.00 36.24  ? 291 LEU A O     1 
ATOM   2202 C CB    . LEU A 1 310 ? -15.379 2.313   -39.651 1.00 31.58  ? 291 LEU A CB    1 
ATOM   2203 C CG    . LEU A 1 310 ? -15.700 1.642   -40.978 1.00 34.72  ? 291 LEU A CG    1 
ATOM   2204 C CD1   . LEU A 1 310 ? -17.147 1.914   -41.417 1.00 37.64  ? 291 LEU A CD1   1 
ATOM   2205 C CD2   . LEU A 1 310 ? -14.712 2.133   -42.015 1.00 32.72  ? 291 LEU A CD2   1 
ATOM   2206 N N     . GLY A 1 311 ? -14.678 0.307   -37.292 1.00 30.25  ? 292 GLY A N     1 
ATOM   2207 C CA    . GLY A 1 311 ? -14.101 -0.949  -36.821 1.00 27.70  ? 292 GLY A CA    1 
ATOM   2208 C C     . GLY A 1 311 ? -14.001 -0.965  -35.283 1.00 28.40  ? 292 GLY A C     1 
ATOM   2209 O O     . GLY A 1 311 ? -14.982 -0.643  -34.599 1.00 31.92  ? 292 GLY A O     1 
ATOM   2210 N N     . GLY A 1 312 ? -12.830 -1.347  -34.747 1.00 27.82  ? 293 GLY A N     1 
ATOM   2211 C CA    . GLY A 1 312 ? -12.597 -1.485  -33.311 1.00 24.72  ? 293 GLY A CA    1 
ATOM   2212 C C     . GLY A 1 312 ? -11.534 -0.540  -32.733 1.00 21.06  ? 293 GLY A C     1 
ATOM   2213 O O     . GLY A 1 312 ? -11.162 -0.709  -31.559 1.00 22.09  ? 293 GLY A O     1 
ATOM   2214 N N     . LEU A 1 313 ? -11.081 0.467   -33.493 1.00 24.00  ? 294 LEU A N     1 
ATOM   2215 C CA    . LEU A 1 313 ? -10.021 1.336   -32.971 1.00 23.06  ? 294 LEU A CA    1 
ATOM   2216 C C     . LEU A 1 313 ? -10.524 2.268   -31.855 1.00 24.00  ? 294 LEU A C     1 
ATOM   2217 O O     . LEU A 1 313 ? -9.723  2.778   -31.090 1.00 20.78  ? 294 LEU A O     1 
ATOM   2218 C CB    . LEU A 1 313 ? -9.373  2.146   -34.099 1.00 24.09  ? 294 LEU A CB    1 
ATOM   2219 C CG    . LEU A 1 313 ? -8.581  1.318   -35.122 1.00 27.05  ? 294 LEU A CG    1 
ATOM   2220 C CD1   . LEU A 1 313 ? -7.940  2.252   -36.136 1.00 29.52  ? 294 LEU A CD1   1 
ATOM   2221 C CD2   . LEU A 1 313 ? -7.510  0.463   -34.432 1.00 26.50  ? 294 LEU A CD2   1 
ATOM   2222 N N     . ARG A 1 314 ? -11.823 2.534   -31.753 1.00 24.19  ? 295 ARG A N     1 
ATOM   2223 C CA    . ARG A 1 314 ? -12.282 3.373   -30.647 1.00 25.06  ? 295 ARG A CA    1 
ATOM   2224 C C     . ARG A 1 314 ? -11.975 2.717   -29.307 1.00 24.20  ? 295 ARG A C     1 
ATOM   2225 O O     . ARG A 1 314 ? -11.268 3.274   -28.466 1.00 23.24  ? 295 ARG A O     1 
ATOM   2226 C CB    . ARG A 1 314 ? -13.777 3.691   -30.734 1.00 25.12  ? 295 ARG A CB    1 
ATOM   2227 C CG    . ARG A 1 314 ? -14.160 4.591   -31.898 1.00 25.32  ? 295 ARG A CG    1 
ATOM   2228 C CD    . ARG A 1 314 ? -14.007 6.062   -31.545 1.00 26.82  ? 295 ARG A CD    1 
ATOM   2229 N NE    . ARG A 1 314 ? -14.971 6.510   -30.542 1.00 26.71  ? 295 ARG A NE    1 
ATOM   2230 C CZ    . ARG A 1 314 ? -16.268 6.762   -30.736 1.00 27.76  ? 295 ARG A CZ    1 
ATOM   2231 N NH1   . ARG A 1 314 ? -16.837 6.687   -31.929 1.00 28.33  ? 295 ARG A NH1   1 
ATOM   2232 N NH2   . ARG A 1 314 ? -17.020 7.108   -29.713 1.00 27.47  ? 295 ARG A NH2   1 
ATOM   2233 N N     . LEU A 1 315 ? -12.440 1.479   -29.120 1.00 22.47  ? 296 LEU A N     1 
ATOM   2234 C CA    . LEU A 1 315 ? -12.209 0.817   -27.850 1.00 20.94  ? 296 LEU A CA    1 
ATOM   2235 C C     . LEU A 1 315 ? -10.729 0.468   -27.645 1.00 21.87  ? 296 LEU A C     1 
ATOM   2236 O O     . LEU A 1 315 ? -10.287 0.466   -26.501 1.00 21.73  ? 296 LEU A O     1 
ATOM   2237 C CB    . LEU A 1 315 ? -13.097 -0.425  -27.677 1.00 21.76  ? 296 LEU A CB    1 
ATOM   2238 C CG    . LEU A 1 315 ? -14.576 -0.170  -27.419 1.00 26.05  ? 296 LEU A CG    1 
ATOM   2239 C CD1   . LEU A 1 315 ? -15.370 -1.472  -27.574 1.00 26.59  ? 296 LEU A CD1   1 
ATOM   2240 C CD2   . LEU A 1 315 ? -14.778 0.416   -26.042 1.00 31.09  ? 296 LEU A CD2   1 
ATOM   2241 N N     . SER A 1 316 ? -9.965  0.122   -28.704 1.00 21.15  ? 297 SER A N     1 
ATOM   2242 C CA    . SER A 1 316 ? -8.586  -0.213  -28.469 1.00 22.74  ? 297 SER A CA    1 
ATOM   2243 C C     . SER A 1 316 ? -7.800  1.029   -28.065 1.00 21.91  ? 297 SER A C     1 
ATOM   2244 O O     . SER A 1 316 ? -7.035  0.925   -27.094 1.00 23.32  ? 297 SER A O     1 
ATOM   2245 C CB    . SER A 1 316 ? -7.898  -0.980  -29.586 1.00 22.73  ? 297 SER A CB    1 
ATOM   2246 O OG    . SER A 1 316 ? -7.904  -0.289  -30.807 1.00 24.16  ? 297 SER A OG    1 
ATOM   2247 N N     . THR A 1 317 ? -8.030  2.194   -28.693 1.00 23.77  ? 298 THR A N     1 
ATOM   2248 C CA    . THR A 1 317 ? -7.305  3.372   -28.212 1.00 23.82  ? 298 THR A CA    1 
ATOM   2249 C C     . THR A 1 317 ? -7.731  3.738   -26.786 1.00 23.92  ? 298 THR A C     1 
ATOM   2250 O O     . THR A 1 317 ? -6.891  4.149   -25.984 1.00 25.02  ? 298 THR A O     1 
ATOM   2251 C CB    . THR A 1 317 ? -7.397  4.577   -29.157 1.00 23.65  ? 298 THR A CB    1 
ATOM   2252 O OG1   . THR A 1 317 ? -8.758  4.930   -29.397 1.00 26.05  ? 298 THR A OG1   1 
ATOM   2253 C CG2   . THR A 1 317 ? -6.708  4.288   -30.462 1.00 27.11  ? 298 THR A CG2   1 
ATOM   2254 N N     . CYS A 1 318 ? -9.022  3.583   -26.457 1.00 20.77  ? 299 CYS A N     1 
ATOM   2255 C CA    . CYS A 1 318 ? -9.541  3.806   -25.111 1.00 22.42  ? 299 CYS A CA    1 
ATOM   2256 C C     . CYS A 1 318 ? -8.786  3.000   -24.056 1.00 22.61  ? 299 CYS A C     1 
ATOM   2257 O O     . CYS A 1 318 ? -8.278  3.538   -23.061 1.00 21.00  ? 299 CYS A O     1 
ATOM   2258 C CB    . CYS A 1 318 ? -11.030 3.469   -24.993 1.00 24.16  ? 299 CYS A CB    1 
ATOM   2259 S SG    . CYS A 1 318 ? -12.131 4.736   -25.687 1.00 27.24  ? 299 CYS A SG    1 
ATOM   2260 N N     . LEU A 1 319 ? -8.752  1.659   -24.212 1.00 23.42  ? 300 LEU A N     1 
ATOM   2261 C CA    . LEU A 1 319 ? -8.155  0.834   -23.198 1.00 22.54  ? 300 LEU A CA    1 
ATOM   2262 C C     . LEU A 1 319 ? -6.635  0.956   -23.224 1.00 21.52  ? 300 LEU A C     1 
ATOM   2263 O O     . LEU A 1 319 ? -6.043  0.841   -22.159 1.00 20.91  ? 300 LEU A O     1 
ATOM   2264 C CB    . LEU A 1 319 ? -8.580  -0.638  -23.313 1.00 25.70  ? 300 LEU A CB    1 
ATOM   2265 C CG    . LEU A 1 319 ? -10.089 -0.965  -23.281 1.00 35.71  ? 300 LEU A CG    1 
ATOM   2266 C CD1   . LEU A 1 319 ? -10.349 -2.307  -22.603 1.00 37.04  ? 300 LEU A CD1   1 
ATOM   2267 C CD2   . LEU A 1 319 ? -10.968 0.114   -22.689 1.00 35.13  ? 300 LEU A CD2   1 
ATOM   2268 N N     . GLN A 1 320 ? -6.036  1.283   -24.382 1.00 21.67  ? 301 GLN A N     1 
ATOM   2269 C CA    . GLN A 1 320 ? -4.594  1.524   -24.424 1.00 22.19  ? 301 GLN A CA    1 
ATOM   2270 C C     . GLN A 1 320 ? -4.223  2.779   -23.631 1.00 20.69  ? 301 GLN A C     1 
ATOM   2271 O O     . GLN A 1 320 ? -3.209  2.789   -22.952 1.00 21.07  ? 301 GLN A O     1 
ATOM   2272 C CB    . GLN A 1 320 ? -4.076  1.599   -25.860 1.00 23.17  ? 301 GLN A CB    1 
ATOM   2273 C CG    . GLN A 1 320 ? -4.103  0.211   -26.554 1.00 24.59  ? 301 GLN A CG    1 
ATOM   2274 C CD    . GLN A 1 320 ? -4.003  0.201   -28.064 1.00 26.28  ? 301 GLN A CD    1 
ATOM   2275 O OE1   . GLN A 1 320 ? -3.856  -0.846  -28.688 1.00 31.49  ? 301 GLN A OE1   1 
ATOM   2276 N NE2   . GLN A 1 320 ? -4.157  1.341   -28.679 1.00 21.87  ? 301 GLN A NE2   1 
ATOM   2277 N N     . ASP A 1 321 ? -5.053  3.816   -23.685 1.00 22.28  ? 302 ASP A N     1 
ATOM   2278 C CA    . ASP A 1 321 ? -4.831  4.983   -22.838 1.00 23.36  ? 302 ASP A CA    1 
ATOM   2279 C C     . ASP A 1 321 ? -4.917  4.609   -21.356 1.00 23.42  ? 302 ASP A C     1 
ATOM   2280 O O     . ASP A 1 321 ? -4.069  4.994   -20.554 1.00 21.91  ? 302 ASP A O     1 
ATOM   2281 C CB    . ASP A 1 321 ? -5.914  6.044   -23.029 1.00 22.56  ? 302 ASP A CB    1 
ATOM   2282 C CG    . ASP A 1 321 ? -5.934  6.769   -24.368 1.00 24.50  ? 302 ASP A CG    1 
ATOM   2283 O OD1   . ASP A 1 321 ? -4.881  6.775   -25.094 1.00 24.04  ? 302 ASP A OD1   1 
ATOM   2284 O OD2   . ASP A 1 321 ? -6.996  7.406   -24.627 1.00 25.39  ? 302 ASP A OD2   1 
ATOM   2285 N N     . ALA A 1 322 ? -5.951  3.842   -20.979 1.00 18.46  ? 303 ALA A N     1 
ATOM   2286 C CA    . ALA A 1 322 ? -6.185  3.508   -19.587 1.00 20.12  ? 303 ALA A CA    1 
ATOM   2287 C C     . ALA A 1 322 ? -4.988  2.735   -19.048 1.00 21.61  ? 303 ALA A C     1 
ATOM   2288 O O     . ALA A 1 322 ? -4.563  2.938   -17.909 1.00 22.45  ? 303 ALA A O     1 
ATOM   2289 C CB    . ALA A 1 322 ? -7.466  2.687   -19.445 1.00 23.10  ? 303 ALA A CB    1 
ATOM   2290 N N     . VAL A 1 323 ? -4.503  1.772   -19.826 1.00 22.29  ? 304 VAL A N     1 
ATOM   2291 C CA    . VAL A 1 323 ? -3.442  0.924   -19.312 1.00 21.43  ? 304 VAL A CA    1 
ATOM   2292 C C     . VAL A 1 323 ? -2.100  1.675   -19.338 1.00 23.51  ? 304 VAL A C     1 
ATOM   2293 O O     . VAL A 1 323 ? -1.214  1.380   -18.529 1.00 23.62  ? 304 VAL A O     1 
ATOM   2294 C CB    . VAL A 1 323 ? -3.417  -0.413  -20.061 1.00 23.16  ? 304 VAL A CB    1 
ATOM   2295 C CG1   . VAL A 1 323 ? -2.249  -1.283  -19.661 1.00 26.29  ? 304 VAL A CG1   1 
ATOM   2296 C CG2   . VAL A 1 323 ? -4.734  -1.158  -19.886 1.00 24.03  ? 304 VAL A CG2   1 
ATOM   2297 N N     . ASN A 1 324 ? -1.920  2.641   -20.245 1.00 22.77  ? 305 ASN A N     1 
ATOM   2298 C CA    . ASN A 1 324 ? -0.691  3.436   -20.255 1.00 23.47  ? 305 ASN A CA    1 
ATOM   2299 C C     . ASN A 1 324 ? -0.656  4.272   -18.963 1.00 22.63  ? 305 ASN A C     1 
ATOM   2300 O O     . ASN A 1 324 ? 0.338   4.380   -18.269 1.00 23.97  ? 305 ASN A O     1 
ATOM   2301 C CB    . ASN A 1 324 ? -0.622  4.290   -21.534 1.00 22.65  ? 305 ASN A CB    1 
ATOM   2302 C CG    . ASN A 1 324 ? 0.681   5.052   -21.725 1.00 24.10  ? 305 ASN A CG    1 
ATOM   2303 O OD1   . ASN A 1 324 ? 0.977   6.003   -21.006 1.00 24.44  ? 305 ASN A OD1   1 
ATOM   2304 N ND2   . ASN A 1 324 ? 1.468   4.608   -22.678 1.00 25.07  ? 305 ASN A ND2   1 
ATOM   2305 N N     . LEU A 1 325 ? -1.791  4.854   -18.614 1.00 21.62  ? 306 LEU A N     1 
ATOM   2306 C CA    . LEU A 1 325 ? -1.861  5.847   -17.550 1.00 23.88  ? 306 LEU A CA    1 
ATOM   2307 C C     . LEU A 1 325 ? -1.875  5.241   -16.142 1.00 24.11  ? 306 LEU A C     1 
ATOM   2308 O O     . LEU A 1 325 ? -1.228  5.761   -15.245 1.00 24.93  ? 306 LEU A O     1 
ATOM   2309 C CB    . LEU A 1 325 ? -3.121  6.665   -17.750 1.00 23.74  ? 306 LEU A CB    1 
ATOM   2310 C CG    . LEU A 1 325 ? -3.306  7.822   -16.769 1.00 27.07  ? 306 LEU A CG    1 
ATOM   2311 C CD1   . LEU A 1 325 ? -2.111  8.754   -16.759 1.00 26.89  ? 306 LEU A CD1   1 
ATOM   2312 C CD2   . LEU A 1 325 ? -4.578  8.561   -17.076 1.00 27.44  ? 306 LEU A CD2   1 
ATOM   2313 N N     . GLY A 1 326 ? -2.605  4.152   -15.917 1.00 21.63  ? 307 GLY A N     1 
ATOM   2314 C CA    . GLY A 1 326 ? -2.839  3.692   -14.566 1.00 23.28  ? 307 GLY A CA    1 
ATOM   2315 C C     . GLY A 1 326 ? -1.548  3.418   -13.795 1.00 23.98  ? 307 GLY A C     1 
ATOM   2316 O O     . GLY A 1 326 ? -1.380  3.891   -12.678 1.00 24.72  ? 307 GLY A O     1 
ATOM   2317 N N     . TRP A 1 327 ? -0.644  2.614   -14.337 1.00 23.61  ? 308 TRP A N     1 
ATOM   2318 C CA    . TRP A 1 327 ? 0.529   2.239   -13.590 1.00 22.53  ? 308 TRP A CA    1 
ATOM   2319 C C     . TRP A 1 327 ? 1.396   3.467   -13.340 1.00 24.94  ? 308 TRP A C     1 
ATOM   2320 O O     . TRP A 1 327 ? 2.122   3.506   -12.344 1.00 23.49  ? 308 TRP A O     1 
ATOM   2321 C CB    . TRP A 1 327 ? 1.319   1.128   -14.271 1.00 25.51  ? 308 TRP A CB    1 
ATOM   2322 C CG    . TRP A 1 327 ? 2.119   1.515   -15.478 1.00 24.33  ? 308 TRP A CG    1 
ATOM   2323 C CD1   . TRP A 1 327 ? 1.676   1.557   -16.768 1.00 24.26  ? 308 TRP A CD1   1 
ATOM   2324 C CD2   . TRP A 1 327 ? 3.501   1.903   -15.523 1.00 24.13  ? 308 TRP A CD2   1 
ATOM   2325 N NE1   . TRP A 1 327 ? 2.684   1.910   -17.613 1.00 25.24  ? 308 TRP A NE1   1 
ATOM   2326 C CE2   . TRP A 1 327 ? 3.810   2.145   -16.874 1.00 25.10  ? 308 TRP A CE2   1 
ATOM   2327 C CE3   . TRP A 1 327 ? 4.510   2.071   -14.572 1.00 27.21  ? 308 TRP A CE3   1 
ATOM   2328 C CZ2   . TRP A 1 327 ? 5.086   2.506   -17.290 1.00 24.70  ? 308 TRP A CZ2   1 
ATOM   2329 C CZ3   . TRP A 1 327 ? 5.766   2.456   -14.988 1.00 28.62  ? 308 TRP A CZ3   1 
ATOM   2330 C CH2   . TRP A 1 327 ? 6.053   2.650   -16.328 1.00 27.56  ? 308 TRP A CH2   1 
ATOM   2331 N N     . LYS A 1 328 ? 1.368   4.407   -14.291 1.00 25.15  ? 309 LYS A N     1 
ATOM   2332 C CA    . LYS A 1 328 ? 2.174   5.619   -14.156 1.00 25.52  ? 309 LYS A CA    1 
ATOM   2333 C C     . LYS A 1 328 ? 1.659   6.523   -13.022 1.00 25.36  ? 309 LYS A C     1 
ATOM   2334 O O     . LYS A 1 328 ? 2.474   7.058   -12.254 1.00 27.65  ? 309 LYS A O     1 
ATOM   2335 C CB    . LYS A 1 328 ? 2.268   6.341   -15.499 1.00 24.55  ? 309 LYS A CB    1 
ATOM   2336 C CG    . LYS A 1 328 ? 2.983   5.579   -16.586 1.00 24.02  ? 309 LYS A CG    1 
ATOM   2337 C CD    . LYS A 1 328 ? 2.918   6.261   -17.940 1.00 26.20  ? 309 LYS A CD    1 
ATOM   2338 C CE    . LYS A 1 328 ? 3.542   5.476   -19.072 1.00 26.79  ? 309 LYS A CE    1 
ATOM   2339 N NZ    . LYS A 1 328 ? 3.529   6.257   -20.330 1.00 26.66  ? 309 LYS A NZ    1 
ATOM   2340 N N     . LEU A 1 329 ? 0.338   6.732   -12.954 1.00 25.43  ? 310 LEU A N     1 
ATOM   2341 C CA    . LEU A 1 329 ? -0.297  7.446   -11.839 1.00 28.96  ? 310 LEU A CA    1 
ATOM   2342 C C     . LEU A 1 329 ? 0.068   6.757   -10.523 1.00 29.69  ? 310 LEU A C     1 
ATOM   2343 O O     . LEU A 1 329 ? 0.443   7.381   -9.526  1.00 28.30  ? 310 LEU A O     1 
ATOM   2344 C CB    . LEU A 1 329 ? -1.815  7.412   -11.984 1.00 29.70  ? 310 LEU A CB    1 
ATOM   2345 C CG    . LEU A 1 329 ? -2.631  8.680   -12.268 1.00 38.27  ? 310 LEU A CG    1 
ATOM   2346 C CD1   . LEU A 1 329 ? -1.829  9.914   -12.652 1.00 35.66  ? 310 LEU A CD1   1 
ATOM   2347 C CD2   . LEU A 1 329 ? -3.755  8.403   -13.239 1.00 32.20  ? 310 LEU A CD2   1 
ATOM   2348 N N     . ALA A 1 330 ? -0.038  5.420   -10.499 1.00 26.45  ? 311 ALA A N     1 
ATOM   2349 C CA    . ALA A 1 330 ? 0.229   4.703   -9.265  1.00 27.55  ? 311 ALA A CA    1 
ATOM   2350 C C     . ALA A 1 330 ? 1.695   4.841   -8.854  1.00 26.32  ? 311 ALA A C     1 
ATOM   2351 O O     . ALA A 1 330 ? 1.980   4.942   -7.663  1.00 27.54  ? 311 ALA A O     1 
ATOM   2352 C CB    . ALA A 1 330 ? -0.214  3.252   -9.399  1.00 23.95  ? 311 ALA A CB    1 
ATOM   2353 N N     . ALA A 1 331 ? 2.624   4.855   -9.803  1.00 24.79  ? 312 ALA A N     1 
ATOM   2354 C CA    . ALA A 1 331 ? 4.037   4.929   -9.469  1.00 26.60  ? 312 ALA A CA    1 
ATOM   2355 C C     . ALA A 1 331 ? 4.355   6.321   -8.927  1.00 30.90  ? 312 ALA A C     1 
ATOM   2356 O O     . ALA A 1 331 ? 5.212   6.516   -8.050  1.00 29.59  ? 312 ALA A O     1 
ATOM   2357 C CB    . ALA A 1 331 ? 4.851   4.618   -10.673 1.00 26.68  ? 312 ALA A CB    1 
ATOM   2358 N N     . ASP A 1 332 ? 3.657   7.293   -9.480  1.00 27.46  ? 313 ASP A N     1 
ATOM   2359 C CA    . ASP A 1 332 ? 3.832   8.667   -9.064  1.00 32.07  ? 313 ASP A CA    1 
ATOM   2360 C C     . ASP A 1 332 ? 3.354   8.834   -7.622  1.00 30.98  ? 313 ASP A C     1 
ATOM   2361 O O     . ASP A 1 332 ? 4.087   9.329   -6.785  1.00 30.44  ? 313 ASP A O     1 
ATOM   2362 C CB    . ASP A 1 332 ? 3.077   9.640   -9.960  1.00 32.54  ? 313 ASP A CB    1 
ATOM   2363 C CG    . ASP A 1 332 ? 3.375   11.070  -9.545  1.00 38.46  ? 313 ASP A CG    1 
ATOM   2364 O OD1   . ASP A 1 332 ? 4.509   11.548  -9.846  1.00 41.28  ? 313 ASP A OD1   1 
ATOM   2365 O OD2   . ASP A 1 332 ? 2.502   11.647  -8.876  1.00 40.04  ? 313 ASP A OD2   1 
ATOM   2366 N N     . LEU A 1 333 ? 2.128   8.406   -7.329  1.00 29.66  ? 314 LEU A N     1 
ATOM   2367 C CA    . LEU A 1 333 ? 1.592   8.450   -5.975  1.00 33.99  ? 314 LEU A CA    1 
ATOM   2368 C C     . LEU A 1 333 ? 2.415   7.610   -4.989  1.00 34.41  ? 314 LEU A C     1 
ATOM   2369 O O     . LEU A 1 333 ? 2.613   8.041   -3.855  1.00 32.52  ? 314 LEU A O     1 
ATOM   2370 C CB    . LEU A 1 333 ? 0.133   7.992   -5.994  1.00 31.56  ? 314 LEU A CB    1 
ATOM   2371 C CG    . LEU A 1 333 ? -0.847  8.959   -6.639  1.00 35.08  ? 314 LEU A CG    1 
ATOM   2372 C CD1   . LEU A 1 333 ? -2.200  8.290   -6.803  1.00 39.68  ? 314 LEU A CD1   1 
ATOM   2373 C CD2   . LEU A 1 333 ? -1.008  10.240  -5.835  1.00 38.38  ? 314 LEU A CD2   1 
ATOM   2374 N N     . ALA A 1 334 ? 2.969   6.460   -5.404  1.00 29.32  ? 315 ALA A N     1 
ATOM   2375 C CA    . ALA A 1 334 ? 3.663   5.598   -4.472  1.00 34.35  ? 315 ALA A CA    1 
ATOM   2376 C C     . ALA A 1 334 ? 5.038   6.179   -4.171  1.00 35.46  ? 315 ALA A C     1 
ATOM   2377 O O     . ALA A 1 334 ? 5.673   5.717   -3.237  1.00 36.45  ? 315 ALA A O     1 
ATOM   2378 C CB    . ALA A 1 334 ? 3.758   4.166   -4.985  1.00 31.63  ? 315 ALA A CB    1 
ATOM   2379 N N     . GLY A 1 335 ? 5.509   7.096   -5.023  1.00 34.37  ? 316 GLY A N     1 
ATOM   2380 C CA    . GLY A 1 335 ? 6.704   7.867   -4.789  1.00 36.03  ? 316 GLY A CA    1 
ATOM   2381 C C     . GLY A 1 335 ? 7.929   7.335   -5.526  1.00 37.92  ? 316 GLY A C     1 
ATOM   2382 O O     . GLY A 1 335 ? 9.001   7.892   -5.323  1.00 38.13  ? 316 GLY A O     1 
ATOM   2383 N N     . TRP A 1 336 ? 7.804   6.296   -6.383  1.00 33.44  ? 317 TRP A N     1 
ATOM   2384 C CA    . TRP A 1 336 ? 8.969   5.706   -7.026  1.00 29.55  ? 317 TRP A CA    1 
ATOM   2385 C C     . TRP A 1 336 ? 9.087   6.054   -8.513  1.00 32.13  ? 317 TRP A C     1 
ATOM   2386 O O     . TRP A 1 336 ? 10.102  5.706   -9.117  1.00 33.29  ? 317 TRP A O     1 
ATOM   2387 C CB    . TRP A 1 336 ? 9.027   4.189   -6.825  1.00 31.90  ? 317 TRP A CB    1 
ATOM   2388 C CG    . TRP A 1 336 ? 7.864   3.385   -7.338  1.00 32.88  ? 317 TRP A CG    1 
ATOM   2389 C CD1   . TRP A 1 336 ? 6.845   2.897   -6.569  1.00 36.06  ? 317 TRP A CD1   1 
ATOM   2390 C CD2   . TRP A 1 336 ? 7.622   2.880   -8.674  1.00 34.75  ? 317 TRP A CD2   1 
ATOM   2391 N NE1   . TRP A 1 336 ? 5.968   2.171   -7.323  1.00 32.52  ? 317 TRP A NE1   1 
ATOM   2392 C CE2   . TRP A 1 336 ? 6.422   2.112   -8.614  1.00 31.91  ? 317 TRP A CE2   1 
ATOM   2393 C CE3   . TRP A 1 336 ? 8.306   2.933   -9.893  1.00 35.35  ? 317 TRP A CE3   1 
ATOM   2394 C CZ2   . TRP A 1 336 ? 5.884   1.449   -9.722  1.00 30.52  ? 317 TRP A CZ2   1 
ATOM   2395 C CZ3   . TRP A 1 336 ? 7.762   2.293   -11.001 1.00 34.40  ? 317 TRP A CZ3   1 
ATOM   2396 C CH2   . TRP A 1 336 ? 6.570   1.551   -10.908 1.00 33.04  ? 317 TRP A CH2   1 
ATOM   2397 N N     . ALA A 1 337 ? 8.099   6.753   -9.096  1.00 29.29  ? 318 ALA A N     1 
ATOM   2398 C CA    . ALA A 1 337 ? 8.127   7.064   -10.519 1.00 31.48  ? 318 ALA A CA    1 
ATOM   2399 C C     . ALA A 1 337 ? 9.423   7.804   -10.850 1.00 36.61  ? 318 ALA A C     1 
ATOM   2400 O O     . ALA A 1 337 ? 9.827   8.688   -10.098 1.00 32.88  ? 318 ALA A O     1 
ATOM   2401 C CB    . ALA A 1 337 ? 6.947   7.925   -10.917 1.00 28.81  ? 318 ALA A CB    1 
ATOM   2402 N N     . PRO A 1 338 ? 10.112  7.484   -11.965 1.00 33.24  ? 319 PRO A N     1 
ATOM   2403 C CA    . PRO A 1 338 ? 11.244  8.308   -12.390 1.00 32.99  ? 319 PRO A CA    1 
ATOM   2404 C C     . PRO A 1 338 ? 10.716  9.675   -12.779 1.00 34.13  ? 319 PRO A C     1 
ATOM   2405 O O     . PRO A 1 338 ? 9.534   9.870   -13.068 1.00 30.75  ? 319 PRO A O     1 
ATOM   2406 C CB    . PRO A 1 338 ? 11.893  7.571   -13.568 1.00 36.38  ? 319 PRO A CB    1 
ATOM   2407 C CG    . PRO A 1 338 ? 10.865  6.508   -13.983 1.00 36.94  ? 319 PRO A CG    1 
ATOM   2408 C CD    . PRO A 1 338 ? 9.899   6.319   -12.835 1.00 31.77  ? 319 PRO A CD    1 
ATOM   2409 N N     . PRO A 1 339 ? 11.575  10.710  -12.789 1.00 43.14  ? 320 PRO A N     1 
ATOM   2410 C CA    . PRO A 1 339 ? 11.102  12.046  -13.141 1.00 42.17  ? 320 PRO A CA    1 
ATOM   2411 C C     . PRO A 1 339 ? 10.597  12.078  -14.591 1.00 36.28  ? 320 PRO A C     1 
ATOM   2412 O O     . PRO A 1 339 ? 11.139  11.428  -15.477 1.00 37.40  ? 320 PRO A O     1 
ATOM   2413 C CB    . PRO A 1 339 ? 12.339  12.958  -12.959 1.00 49.02  ? 320 PRO A CB    1 
ATOM   2414 C CG    . PRO A 1 339 ? 13.420  12.094  -12.313 1.00 47.62  ? 320 PRO A CG    1 
ATOM   2415 C CD    . PRO A 1 339 ? 13.024  10.644  -12.545 1.00 47.99  ? 320 PRO A CD    1 
ATOM   2416 N N     . GLY A 1 340 ? 9.518   12.816  -14.817 1.00 33.96  ? 321 GLY A N     1 
ATOM   2417 C CA    . GLY A 1 340 ? 8.913   12.891  -16.129 1.00 37.86  ? 321 GLY A CA    1 
ATOM   2418 C C     . GLY A 1 340 ? 7.974   11.719  -16.484 1.00 32.77  ? 321 GLY A C     1 
ATOM   2419 O O     . GLY A 1 340 ? 7.503   11.668  -17.617 1.00 32.78  ? 321 GLY A O     1 
ATOM   2420 N N     . LEU A 1 341 ? 7.707   10.771  -15.575 1.00 33.00  ? 322 LEU A N     1 
ATOM   2421 C CA    . LEU A 1 341 ? 7.006   9.557   -15.998 1.00 30.21  ? 322 LEU A CA    1 
ATOM   2422 C C     . LEU A 1 341 ? 5.602   9.912   -16.461 1.00 29.99  ? 322 LEU A C     1 
ATOM   2423 O O     . LEU A 1 341 ? 5.154   9.431   -17.506 1.00 29.30  ? 322 LEU A O     1 
ATOM   2424 C CB    . LEU A 1 341 ? 6.919   8.496   -14.900 1.00 29.69  ? 322 LEU A CB    1 
ATOM   2425 C CG    . LEU A 1 341 ? 6.214   7.197   -15.330 1.00 29.91  ? 322 LEU A CG    1 
ATOM   2426 C CD1   . LEU A 1 341 ? 7.000   6.476   -16.422 1.00 31.89  ? 322 LEU A CD1   1 
ATOM   2427 C CD2   . LEU A 1 341 ? 6.004   6.259   -14.139 1.00 30.82  ? 322 LEU A CD2   1 
ATOM   2428 N N     . LEU A 1 342 ? 4.932   10.752  -15.691 1.00 28.62  ? 323 LEU A N     1 
ATOM   2429 C CA    . LEU A 1 342 ? 3.586   11.147  -16.028 1.00 30.41  ? 323 LEU A CA    1 
ATOM   2430 C C     . LEU A 1 342 ? 3.537   11.898  -17.358 1.00 31.76  ? 323 LEU A C     1 
ATOM   2431 O O     . LEU A 1 342 ? 2.497   11.876  -18.008 1.00 27.97  ? 323 LEU A O     1 
ATOM   2432 C CB    . LEU A 1 342 ? 3.042   12.001  -14.885 1.00 34.79  ? 323 LEU A CB    1 
ATOM   2433 C CG    . LEU A 1 342 ? 1.815   11.480  -14.140 1.00 38.48  ? 323 LEU A CG    1 
ATOM   2434 C CD1   . LEU A 1 342 ? 1.599   9.986   -14.266 1.00 36.34  ? 323 LEU A CD1   1 
ATOM   2435 C CD2   . LEU A 1 342 ? 1.855   11.902  -12.690 1.00 34.02  ? 323 LEU A CD2   1 
ATOM   2436 N N     . ASP A 1 343 ? 4.617   12.596  -17.734 1.00 31.41  ? 324 ASP A N     1 
ATOM   2437 C CA    . ASP A 1 343 ? 4.602   13.349  -18.982 1.00 31.89  ? 324 ASP A CA    1 
ATOM   2438 C C     . ASP A 1 343 ? 4.663   12.397  -20.184 1.00 31.07  ? 324 ASP A C     1 
ATOM   2439 O O     . ASP A 1 343 ? 4.360   12.806  -21.310 1.00 29.52  ? 324 ASP A O     1 
ATOM   2440 C CB    . ASP A 1 343 ? 5.705   14.419  -19.019 1.00 37.04  ? 324 ASP A CB    1 
ATOM   2441 C CG    . ASP A 1 343 ? 5.221   15.826  -18.644 1.00 46.39  ? 324 ASP A CG    1 
ATOM   2442 O OD1   . ASP A 1 343 ? 4.011   15.995  -18.295 1.00 42.74  ? 324 ASP A OD1   1 
ATOM   2443 O OD2   . ASP A 1 343 ? 6.041   16.775  -18.756 1.00 52.81  ? 324 ASP A OD2   1 
ATOM   2444 N N     . THR A 1 344 ? 5.136   11.162  -19.971 1.00 29.80  ? 325 THR A N     1 
ATOM   2445 C CA    . THR A 1 344 ? 5.213   10.213  -21.070 1.00 27.80  ? 325 THR A CA    1 
ATOM   2446 C C     . THR A 1 344 ? 3.812   9.740   -21.468 1.00 26.14  ? 325 THR A C     1 
ATOM   2447 O O     . THR A 1 344 ? 3.686   9.105   -22.528 1.00 26.11  ? 325 THR A O     1 
ATOM   2448 C CB    . THR A 1 344 ? 6.093   8.986   -20.779 1.00 28.58  ? 325 THR A CB    1 
ATOM   2449 O OG1   . THR A 1 344 ? 5.525   8.061   -19.826 1.00 27.48  ? 325 THR A OG1   1 
ATOM   2450 C CG2   . THR A 1 344 ? 7.485   9.370   -20.330 1.00 29.52  ? 325 THR A CG2   1 
ATOM   2451 N N     . TYR A 1 345 ? 2.787   9.980   -20.644 1.00 25.12  ? 326 TYR A N     1 
ATOM   2452 C CA    . TYR A 1 345 ? 1.436   9.592   -21.035 1.00 26.10  ? 326 TYR A CA    1 
ATOM   2453 C C     . TYR A 1 345 ? 1.005   10.370  -22.275 1.00 26.23  ? 326 TYR A C     1 
ATOM   2454 O O     . TYR A 1 345 ? 0.690   9.792   -23.303 1.00 24.15  ? 326 TYR A O     1 
ATOM   2455 C CB    . TYR A 1 345 ? 0.415   9.806   -19.925 1.00 24.48  ? 326 TYR A CB    1 
ATOM   2456 C CG    . TYR A 1 345 ? -1.010  9.602   -20.334 1.00 22.97  ? 326 TYR A CG    1 
ATOM   2457 C CD1   . TYR A 1 345 ? -1.469  8.350   -20.678 1.00 23.74  ? 326 TYR A CD1   1 
ATOM   2458 C CD2   . TYR A 1 345 ? -1.902  10.661  -20.426 1.00 24.64  ? 326 TYR A CD2   1 
ATOM   2459 C CE1   . TYR A 1 345 ? -2.789  8.139   -21.005 1.00 23.25  ? 326 TYR A CE1   1 
ATOM   2460 C CE2   . TYR A 1 345 ? -3.229  10.467  -20.765 1.00 24.69  ? 326 TYR A CE2   1 
ATOM   2461 C CZ    . TYR A 1 345 ? -3.661  9.200   -21.090 1.00 24.15  ? 326 TYR A CZ    1 
ATOM   2462 O OH    . TYR A 1 345 ? -4.944  9.033   -21.429 1.00 23.11  ? 326 TYR A OH    1 
ATOM   2463 N N     . HIS A 1 346 ? 1.040   11.712  -22.202 1.00 26.15  ? 327 HIS A N     1 
ATOM   2464 C CA    . HIS A 1 346 ? 0.765   12.510  -23.375 1.00 26.76  ? 327 HIS A CA    1 
ATOM   2465 C C     . HIS A 1 346 ? 1.727   12.163  -24.503 1.00 21.48  ? 327 HIS A C     1 
ATOM   2466 O O     . HIS A 1 346 ? 1.316   12.050  -25.666 1.00 23.46  ? 327 HIS A O     1 
ATOM   2467 C CB    . HIS A 1 346 ? 0.800   14.020  -23.068 1.00 25.60  ? 327 HIS A CB    1 
ATOM   2468 C CG    . HIS A 1 346 ? 0.661   14.855  -24.283 1.00 25.50  ? 327 HIS A CG    1 
ATOM   2469 N ND1   . HIS A 1 346 ? -0.534  15.358  -24.746 1.00 25.86  ? 327 HIS A ND1   1 
ATOM   2470 C CD2   . HIS A 1 346 ? 1.614   15.295  -25.131 1.00 30.36  ? 327 HIS A CD2   1 
ATOM   2471 C CE1   . HIS A 1 346 ? -0.305  16.039  -25.868 1.00 33.34  ? 327 HIS A CE1   1 
ATOM   2472 N NE2   . HIS A 1 346 ? 0.994   16.009  -26.126 1.00 32.94  ? 327 HIS A NE2   1 
ATOM   2473 N N     . ALA A 1 347 ? 3.034   12.027  -24.200 1.00 26.95  ? 328 ALA A N     1 
ATOM   2474 C CA    . ALA A 1 347 ? 4.034   11.850  -25.250 1.00 29.14  ? 328 ALA A CA    1 
ATOM   2475 C C     . ALA A 1 347 ? 3.777   10.589  -26.072 1.00 26.88  ? 328 ALA A C     1 
ATOM   2476 O O     . ALA A 1 347 ? 3.999   10.612  -27.283 1.00 24.01  ? 328 ALA A O     1 
ATOM   2477 C CB    . ALA A 1 347 ? 5.439   11.751  -24.725 1.00 26.07  ? 328 ALA A CB    1 
ATOM   2478 N N     . GLU A 1 348 ? 3.300   9.529   -25.397 1.00 25.97  ? 329 GLU A N     1 
ATOM   2479 C CA    . GLU A 1 348 ? 3.064   8.237   -26.017 1.00 24.72  ? 329 GLU A CA    1 
ATOM   2480 C C     . GLU A 1 348 ? 1.656   8.116   -26.588 1.00 24.31  ? 329 GLU A C     1 
ATOM   2481 O O     . GLU A 1 348 ? 1.514   7.595   -27.709 1.00 23.67  ? 329 GLU A O     1 
ATOM   2482 C CB    . GLU A 1 348 ? 3.334   7.105   -25.032 1.00 26.13  ? 329 GLU A CB    1 
ATOM   2483 C CG    . GLU A 1 348 ? 4.790   6.929   -24.704 1.00 24.17  ? 329 GLU A CG    1 
ATOM   2484 C CD    . GLU A 1 348 ? 5.119   5.830   -23.697 1.00 29.97  ? 329 GLU A CD    1 
ATOM   2485 O OE1   . GLU A 1 348 ? 4.168   5.348   -22.980 1.00 26.04  ? 329 GLU A OE1   1 
ATOM   2486 O OE2   . GLU A 1 348 ? 6.316   5.416   -23.664 1.00 26.23  ? 329 GLU A OE2   1 
ATOM   2487 N N     . ARG A 1 349 ? 0.639   8.636   -25.887 1.00 22.37  ? 330 ARG A N     1 
ATOM   2488 C CA    . ARG A 1 349 ? -0.742  8.380   -26.295 1.00 22.43  ? 330 ARG A CA    1 
ATOM   2489 C C     . ARG A 1 349 ? -1.288  9.448   -27.249 1.00 23.41  ? 330 ARG A C     1 
ATOM   2490 O O     . ARG A 1 349 ? -2.119  9.141   -28.083 1.00 22.26  ? 330 ARG A O     1 
ATOM   2491 C CB    . ARG A 1 349 ? -1.652  8.218   -25.079 1.00 22.16  ? 330 ARG A CB    1 
ATOM   2492 C CG    . ARG A 1 349 ? -1.338  7.005   -24.226 1.00 23.77  ? 330 ARG A CG    1 
ATOM   2493 C CD    . ARG A 1 349 ? -1.225  5.712   -24.991 1.00 21.96  ? 330 ARG A CD    1 
ATOM   2494 N NE    . ARG A 1 349 ? -2.421  5.507   -25.779 1.00 23.06  ? 330 ARG A NE    1 
ATOM   2495 C CZ    . ARG A 1 349 ? -2.517  4.696   -26.841 1.00 24.58  ? 330 ARG A CZ    1 
ATOM   2496 N NH1   . ARG A 1 349 ? -1.565  3.830   -27.135 1.00 22.48  ? 330 ARG A NH1   1 
ATOM   2497 N NH2   . ARG A 1 349 ? -3.608  4.704   -27.574 1.00 23.36  ? 330 ARG A NH2   1 
ATOM   2498 N N     . HIS A 1 350 ? -0.819  10.702  -27.179 1.00 25.10  ? 331 HIS A N     1 
ATOM   2499 C CA    . HIS A 1 350 ? -1.357  11.749  -28.034 1.00 24.51  ? 331 HIS A CA    1 
ATOM   2500 C C     . HIS A 1 350 ? -1.143  11.391  -29.503 1.00 22.56  ? 331 HIS A C     1 
ATOM   2501 O O     . HIS A 1 350 ? -2.075  11.404  -30.284 1.00 24.46  ? 331 HIS A O     1 
ATOM   2502 C CB    . HIS A 1 350 ? -0.799  13.139  -27.672 1.00 25.70  ? 331 HIS A CB    1 
ATOM   2503 C CG    . HIS A 1 350 ? -1.330  14.219  -28.542 1.00 28.61  ? 331 HIS A CG    1 
ATOM   2504 N ND1   . HIS A 1 350 ? -0.645  14.625  -29.667 1.00 30.79  ? 331 HIS A ND1   1 
ATOM   2505 C CD2   . HIS A 1 350 ? -2.461  14.924  -28.514 1.00 27.09  ? 331 HIS A CD2   1 
ATOM   2506 C CE1   . HIS A 1 350 ? -1.342  15.567  -30.280 1.00 29.39  ? 331 HIS A CE1   1 
ATOM   2507 N NE2   . HIS A 1 350 ? -2.453  15.752  -29.610 1.00 30.66  ? 331 HIS A NE2   1 
ATOM   2508 N N     . PRO A 1 351 ? 0.061   10.998  -29.945 1.00 24.80  ? 332 PRO A N     1 
ATOM   2509 C CA    . PRO A 1 351 ? 0.274   10.653  -31.359 1.00 24.34  ? 332 PRO A CA    1 
ATOM   2510 C C     . PRO A 1 351 ? -0.507  9.387   -31.754 1.00 23.24  ? 332 PRO A C     1 
ATOM   2511 O O     . PRO A 1 351 ? -0.893  9.243   -32.887 1.00 23.50  ? 332 PRO A O     1 
ATOM   2512 C CB    . PRO A 1 351 ? 1.784   10.433  -31.503 1.00 27.94  ? 332 PRO A CB    1 
ATOM   2513 C CG    . PRO A 1 351 ? 2.364   10.593  -30.127 1.00 30.91  ? 332 PRO A CG    1 
ATOM   2514 C CD    . PRO A 1 351 ? 1.292   11.049  -29.168 1.00 27.35  ? 332 PRO A CD    1 
ATOM   2515 N N     . GLU A 1 352 ? -0.804  8.516   -30.801 1.00 24.59  ? 333 GLU A N     1 
ATOM   2516 C CA    . GLU A 1 352 ? -1.532  7.298   -31.105 1.00 25.23  ? 333 GLU A CA    1 
ATOM   2517 C C     . GLU A 1 352 ? -3.009  7.611   -31.320 1.00 24.13  ? 333 GLU A C     1 
ATOM   2518 O O     . GLU A 1 352 ? -3.647  7.038   -32.214 1.00 22.51  ? 333 GLU A O     1 
ATOM   2519 C CB    . GLU A 1 352 ? -1.263  6.271   -30.009 1.00 25.97  ? 333 GLU A CB    1 
ATOM   2520 C CG    . GLU A 1 352 ? 0.010   5.480   -30.203 1.00 25.48  ? 333 GLU A CG    1 
ATOM   2521 C CD    . GLU A 1 352 ? 0.082   4.743   -31.538 1.00 31.00  ? 333 GLU A CD    1 
ATOM   2522 O OE1   . GLU A 1 352 ? 0.933   5.118   -32.320 1.00 35.42  ? 333 GLU A OE1   1 
ATOM   2523 O OE2   . GLU A 1 352 ? -0.739  3.785   -31.802 1.00 32.01  ? 333 GLU A OE2   1 
ATOM   2524 N N     . GLY A 1 353 ? -3.552  8.562   -30.548 1.00 25.75  ? 334 GLY A N     1 
ATOM   2525 C CA    . GLY A 1 353 ? -4.912  9.020   -30.773 1.00 24.58  ? 334 GLY A CA    1 
ATOM   2526 C C     . GLY A 1 353 ? -5.058  9.660   -32.158 1.00 23.92  ? 334 GLY A C     1 
ATOM   2527 O O     . GLY A 1 353 ? -6.050  9.483   -32.883 1.00 24.41  ? 334 GLY A O     1 
ATOM   2528 N N     . GLU A 1 354 ? -4.050  10.464  -32.501 1.00 24.35  ? 335 GLU A N     1 
ATOM   2529 C CA    . GLU A 1 354 ? -4.022  11.115  -33.793 1.00 26.80  ? 335 GLU A CA    1 
ATOM   2530 C C     . GLU A 1 354 ? -3.890  10.067  -34.899 1.00 22.92  ? 335 GLU A C     1 
ATOM   2531 O O     . GLU A 1 354 ? -4.560  10.197  -35.906 1.00 22.58  ? 335 GLU A O     1 
ATOM   2532 C CB    . GLU A 1 354 ? -2.933  12.187  -33.836 1.00 25.45  ? 335 GLU A CB    1 
ATOM   2533 C CG    . GLU A 1 354 ? -2.848  12.882  -35.194 1.00 30.00  ? 335 GLU A CG    1 
ATOM   2534 C CD    . GLU A 1 354 ? -4.091  13.592  -35.710 1.00 32.53  ? 335 GLU A CD    1 
ATOM   2535 O OE1   . GLU A 1 354 ? -4.949  13.942  -34.889 1.00 29.74  ? 335 GLU A OE1   1 
ATOM   2536 O OE2   . GLU A 1 354 ? -4.199  13.783  -36.965 1.00 36.28  ? 335 GLU A OE2   1 
ATOM   2537 N N     . ARG A 1 355 ? -3.031  9.041   -34.736 1.00 23.65  ? 336 ARG A N     1 
ATOM   2538 C CA    . ARG A 1 355 ? -2.829  8.065   -35.789 1.00 24.08  ? 336 ARG A CA    1 
ATOM   2539 C C     . ARG A 1 355 ? -4.134  7.298   -36.055 1.00 24.59  ? 336 ARG A C     1 
ATOM   2540 O O     . ARG A 1 355 ? -4.472  7.037   -37.221 1.00 23.39  ? 336 ARG A O     1 
ATOM   2541 C CB    . ARG A 1 355 ? -1.648  7.146   -35.438 1.00 26.38  ? 336 ARG A CB    1 
ATOM   2542 C CG    . ARG A 1 355 ? -1.160  6.259   -36.578 1.00 29.32  ? 336 ARG A CG    1 
ATOM   2543 C CD    . ARG A 1 355 ? 0.196   5.623   -36.244 1.00 32.03  ? 336 ARG A CD    1 
ATOM   2544 N NE    . ARG A 1 355 ? 0.081   4.624   -35.198 1.00 30.17  ? 336 ARG A NE    1 
ATOM   2545 C CZ    . ARG A 1 355 ? -0.299  3.347   -35.366 1.00 32.23  ? 336 ARG A CZ    1 
ATOM   2546 N NH1   . ARG A 1 355 ? -0.455  2.844   -36.578 1.00 31.29  ? 336 ARG A NH1   1 
ATOM   2547 N NH2   . ARG A 1 355 ? -0.439  2.549   -34.314 1.00 30.19  ? 336 ARG A NH2   1 
ATOM   2548 N N     . ALA A 1 356 ? -4.880  6.958   -34.998 1.00 23.10  ? 337 ALA A N     1 
ATOM   2549 C CA    . ALA A 1 356 ? -6.176  6.297   -35.162 1.00 21.21  ? 337 ALA A CA    1 
ATOM   2550 C C     . ALA A 1 356 ? -7.201  7.212   -35.821 1.00 25.32  ? 337 ALA A C     1 
ATOM   2551 O O     . ALA A 1 356 ? -7.951  6.796   -36.715 1.00 24.31  ? 337 ALA A O     1 
ATOM   2552 C CB    . ALA A 1 356 ? -6.664  5.850   -33.816 1.00 23.30  ? 337 ALA A CB    1 
ATOM   2553 N N     . ARG A 1 357 ? -7.262  8.471   -35.353 1.00 23.33  ? 338 ARG A N     1 
ATOM   2554 C CA    . ARG A 1 357 ? -8.212  9.445   -35.888 1.00 22.84  ? 338 ARG A CA    1 
ATOM   2555 C C     . ARG A 1 357 ? -7.955  9.623   -37.389 1.00 21.98  ? 338 ARG A C     1 
ATOM   2556 O O     . ARG A 1 357 ? -8.880  9.618   -38.198 1.00 22.33  ? 338 ARG A O     1 
ATOM   2557 C CB    . ARG A 1 357 ? -8.082  10.794  -35.167 1.00 22.02  ? 338 ARG A CB    1 
ATOM   2558 C CG    . ARG A 1 357 ? -9.187  11.773  -35.540 1.00 24.51  ? 338 ARG A CG    1 
ATOM   2559 C CD    . ARG A 1 357 ? -8.760  13.191  -35.186 1.00 25.11  ? 338 ARG A CD    1 
ATOM   2560 N NE    . ARG A 1 357 ? -7.685  13.660  -36.042 1.00 25.77  ? 338 ARG A NE    1 
ATOM   2561 C CZ    . ARG A 1 357 ? -7.790  13.892  -37.361 1.00 27.91  ? 338 ARG A CZ    1 
ATOM   2562 N NH1   . ARG A 1 357 ? -6.701  14.119  -38.073 1.00 28.43  ? 338 ARG A NH1   1 
ATOM   2563 N NH2   . ARG A 1 357 ? -8.969  13.891  -37.963 1.00 27.60  ? 338 ARG A NH2   1 
ATOM   2564 N N     . LEU A 1 358 ? -6.680  9.683   -37.774 1.00 22.47  ? 339 LEU A N     1 
ATOM   2565 C CA    . LEU A 1 358 ? -6.256  9.900   -39.149 1.00 22.99  ? 339 LEU A CA    1 
ATOM   2566 C C     . LEU A 1 358 ? -6.547  8.665   -40.008 1.00 22.90  ? 339 LEU A C     1 
ATOM   2567 O O     . LEU A 1 358 ? -6.840  8.792   -41.199 1.00 22.81  ? 339 LEU A O     1 
ATOM   2568 C CB    . LEU A 1 358 ? -4.751  10.158  -39.105 1.00 26.37  ? 339 LEU A CB    1 
ATOM   2569 C CG    . LEU A 1 358 ? -4.106  11.303  -39.876 1.00 38.09  ? 339 LEU A CG    1 
ATOM   2570 C CD1   . LEU A 1 358 ? -2.920  10.804  -40.665 1.00 36.33  ? 339 LEU A CD1   1 
ATOM   2571 C CD2   . LEU A 1 358 ? -5.048  12.147  -40.715 1.00 32.15  ? 339 LEU A CD2   1 
ATOM   2572 N N     . ALA A 1 359 ? -6.483  7.478   -39.403 1.00 24.33  ? 340 ALA A N     1 
ATOM   2573 C CA    . ALA A 1 359 ? -6.803  6.235   -40.073 1.00 24.41  ? 340 ALA A CA    1 
ATOM   2574 C C     . ALA A 1 359 ? -8.292  6.173   -40.389 1.00 24.25  ? 340 ALA A C     1 
ATOM   2575 O O     . ALA A 1 359 ? -8.637  5.685   -41.442 1.00 22.44  ? 340 ALA A O     1 
ATOM   2576 C CB    . ALA A 1 359 ? -6.388  5.046   -39.253 1.00 23.80  ? 340 ALA A CB    1 
ATOM   2577 N N     . LEU A 1 360 ? -9.146  6.731   -39.539 1.00 23.48  ? 341 LEU A N     1 
ATOM   2578 C CA    . LEU A 1 360 ? -10.554 6.778   -39.871 1.00 23.99  ? 341 LEU A CA    1 
ATOM   2579 C C     . LEU A 1 360 ? -10.812 7.831   -40.947 1.00 26.30  ? 341 LEU A C     1 
ATOM   2580 O O     . LEU A 1 360 ? -11.573 7.574   -41.867 1.00 26.65  ? 341 LEU A O     1 
ATOM   2581 C CB    . LEU A 1 360 ? -11.414 6.951   -38.609 1.00 25.22  ? 341 LEU A CB    1 
ATOM   2582 C CG    . LEU A 1 360 ? -11.823 5.644   -37.930 1.00 29.07  ? 341 LEU A CG    1 
ATOM   2583 C CD1   . LEU A 1 360 ? -12.706 4.775   -38.827 1.00 31.87  ? 341 LEU A CD1   1 
ATOM   2584 C CD2   . LEU A 1 360 ? -10.602 4.848   -37.455 1.00 31.80  ? 341 LEU A CD2   1 
ATOM   2585 N N     . ASP A 1 361 ? -10.145 8.983   -40.902 1.00 24.77  ? 342 ASP A N     1 
ATOM   2586 C CA    . ASP A 1 361 ? -10.232 9.900   -42.025 1.00 26.87  ? 342 ASP A CA    1 
ATOM   2587 C C     . ASP A 1 361 ? -9.877  9.188   -43.340 1.00 25.13  ? 342 ASP A C     1 
ATOM   2588 O O     . ASP A 1 361 ? -10.536 9.376   -44.361 1.00 24.24  ? 342 ASP A O     1 
ATOM   2589 C CB    . ASP A 1 361 ? -9.250  11.063  -41.882 1.00 25.34  ? 342 ASP A CB    1 
ATOM   2590 C CG    . ASP A 1 361 ? -9.600  12.183  -40.914 1.00 28.57  ? 342 ASP A CG    1 
ATOM   2591 O OD1   . ASP A 1 361 ? -10.703 12.192  -40.380 1.00 25.52  ? 342 ASP A OD1   1 
ATOM   2592 O OD2   . ASP A 1 361 ? -8.730  13.063  -40.734 1.00 28.53  ? 342 ASP A OD2   1 
ATOM   2593 N N     . ALA A 1 362 ? -8.805  8.388   -43.334 1.00 25.46  ? 343 ALA A N     1 
ATOM   2594 C CA    . ALA A 1 362 ? -8.379  7.696   -44.533 1.00 22.04  ? 343 ALA A CA    1 
ATOM   2595 C C     . ALA A 1 362 ? -9.485  6.777   -45.037 1.00 22.38  ? 343 ALA A C     1 
ATOM   2596 O O     . ALA A 1 362 ? -9.769  6.794   -46.238 1.00 24.38  ? 343 ALA A O     1 
ATOM   2597 C CB    . ALA A 1 362 ? -7.120  6.910   -44.292 1.00 22.43  ? 343 ALA A CB    1 
ATOM   2598 N N     . GLN A 1 363 ? -10.059 5.961   -44.146 1.00 23.86  ? 344 GLN A N     1 
ATOM   2599 C CA    . GLN A 1 363 ? -11.094 5.023   -44.526 1.00 23.22  ? 344 GLN A CA    1 
ATOM   2600 C C     . GLN A 1 363 ? -12.349 5.734   -45.039 1.00 26.84  ? 344 GLN A C     1 
ATOM   2601 O O     . GLN A 1 363 ? -12.997 5.229   -45.970 1.00 24.93  ? 344 GLN A O     1 
ATOM   2602 C CB    . GLN A 1 363 ? -11.422 4.110   -43.354 1.00 23.77  ? 344 GLN A CB    1 
ATOM   2603 C CG    . GLN A 1 363 ? -10.259 3.194   -42.961 1.00 24.53  ? 344 GLN A CG    1 
ATOM   2604 C CD    . GLN A 1 363 ? -10.590 2.313   -41.784 1.00 24.42  ? 344 GLN A CD    1 
ATOM   2605 O OE1   . GLN A 1 363 ? -11.329 1.330   -41.896 1.00 24.89  ? 344 GLN A OE1   1 
ATOM   2606 N NE2   . GLN A 1 363 ? -9.985  2.626   -40.654 1.00 25.99  ? 344 GLN A NE2   1 
ATOM   2607 N N     . LEU A 1 364 ? -12.700 6.879   -44.433 1.00 24.37  ? 345 LEU A N     1 
ATOM   2608 C CA    . LEU A 1 364 ? -13.896 7.591   -44.876 1.00 27.38  ? 345 LEU A CA    1 
ATOM   2609 C C     . LEU A 1 364 ? -13.682 8.213   -46.259 1.00 27.01  ? 345 LEU A C     1 
ATOM   2610 O O     . LEU A 1 364 ? -14.595 8.274   -47.067 1.00 24.80  ? 345 LEU A O     1 
ATOM   2611 C CB    . LEU A 1 364 ? -14.297 8.661   -43.864 1.00 23.86  ? 345 LEU A CB    1 
ATOM   2612 C CG    . LEU A 1 364 ? -14.834 8.133   -42.531 1.00 27.68  ? 345 LEU A CG    1 
ATOM   2613 C CD1   . LEU A 1 364 ? -14.858 9.254   -41.483 1.00 27.64  ? 345 LEU A CD1   1 
ATOM   2614 C CD2   . LEU A 1 364 ? -16.208 7.509   -42.690 1.00 28.93  ? 345 LEU A CD2   1 
ATOM   2615 N N     . ALA A 1 365 ? -12.483 8.714   -46.522 1.00 25.12  ? 346 ALA A N     1 
ATOM   2616 C CA    . ALA A 1 365 ? -12.153 9.327   -47.795 1.00 26.75  ? 346 ALA A CA    1 
ATOM   2617 C C     . ALA A 1 365 ? -12.117 8.325   -48.958 1.00 25.38  ? 346 ALA A C     1 
ATOM   2618 O O     . ALA A 1 365 ? -11.960 8.743   -50.109 1.00 27.42  ? 346 ALA A O     1 
ATOM   2619 C CB    . ALA A 1 365 ? -10.830 10.039  -47.647 1.00 25.61  ? 346 ALA A CB    1 
ATOM   2620 N N     . LEU A 1 366 ? -12.211 7.024   -48.670 1.00 24.92  ? 347 LEU A N     1 
ATOM   2621 C CA    . LEU A 1 366 ? -12.427 6.009   -49.679 1.00 26.20  ? 347 LEU A CA    1 
ATOM   2622 C C     . LEU A 1 366 ? -13.894 5.612   -49.806 1.00 29.02  ? 347 LEU A C     1 
ATOM   2623 O O     . LEU A 1 366 ? -14.181 4.646   -50.522 1.00 28.25  ? 347 LEU A O     1 
ATOM   2624 C CB    . LEU A 1 366 ? -11.628 4.742   -49.322 1.00 26.10  ? 347 LEU A CB    1 
ATOM   2625 C CG    . LEU A 1 366 ? -10.141 4.948   -49.088 1.00 27.29  ? 347 LEU A CG    1 
ATOM   2626 C CD1   . LEU A 1 366 ? -9.476  3.620   -48.777 1.00 28.48  ? 347 LEU A CD1   1 
ATOM   2627 C CD2   . LEU A 1 366 ? -9.469  5.612   -50.267 1.00 29.32  ? 347 LEU A CD2   1 
ATOM   2628 N N     . MET A 1 367 ? -14.808 6.350   -49.161 1.00 25.92  ? 348 MET A N     1 
ATOM   2629 C CA    . MET A 1 367 ? -16.208 5.975   -49.182 1.00 25.78  ? 348 MET A CA    1 
ATOM   2630 C C     . MET A 1 367 ? -17.114 7.125   -49.608 1.00 27.55  ? 348 MET A C     1 
ATOM   2631 O O     . MET A 1 367 ? -18.159 6.846   -50.174 1.00 27.45  ? 348 MET A O     1 
ATOM   2632 C CB    . MET A 1 367 ? -16.649 5.568   -47.776 1.00 29.12  ? 348 MET A CB    1 
ATOM   2633 C CG    . MET A 1 367 ? -16.086 4.263   -47.327 1.00 29.46  ? 348 MET A CG    1 
ATOM   2634 S SD    . MET A 1 367 ? -16.738 3.816   -45.654 1.00 37.51  ? 348 MET A SD    1 
ATOM   2635 C CE    . MET A 1 367 ? -16.767 2.047   -45.828 1.00 37.34  ? 348 MET A CE    1 
ATOM   2636 N N     . HIS A 1 368 ? -16.744 8.369   -49.285 1.00 26.86  ? 349 HIS A N     1 
ATOM   2637 C CA    . HIS A 1 368 ? -17.644 9.498   -49.518 1.00 27.36  ? 349 HIS A CA    1 
ATOM   2638 C C     . HIS A 1 368 ? -16.827 10.694  -49.975 1.00 29.61  ? 349 HIS A C     1 
ATOM   2639 O O     . HIS A 1 368 ? -15.805 10.992  -49.373 1.00 28.52  ? 349 HIS A O     1 
ATOM   2640 C CB    . HIS A 1 368 ? -18.380 9.916   -48.233 1.00 29.47  ? 349 HIS A CB    1 
ATOM   2641 C CG    . HIS A 1 368 ? -19.238 11.130  -48.390 1.00 33.16  ? 349 HIS A CG    1 
ATOM   2642 N ND1   . HIS A 1 368 ? -18.893 12.377  -47.909 1.00 41.90  ? 349 HIS A ND1   1 
ATOM   2643 C CD2   . HIS A 1 368 ? -20.399 11.300  -49.065 1.00 32.16  ? 349 HIS A CD2   1 
ATOM   2644 C CE1   . HIS A 1 368 ? -19.839 13.258  -48.259 1.00 35.83  ? 349 HIS A CE1   1 
ATOM   2645 N NE2   . HIS A 1 368 ? -20.762 12.616  -48.948 1.00 36.69  ? 349 HIS A NE2   1 
ATOM   2646 N N     . PRO A 1 369 ? -17.256 11.453  -51.019 1.00 28.65  ? 350 PRO A N     1 
ATOM   2647 C CA    . PRO A 1 369 ? -18.454 11.141  -51.831 1.00 28.89  ? 350 PRO A CA    1 
ATOM   2648 C C     . PRO A 1 369 ? -18.236 9.974   -52.791 1.00 28.72  ? 350 PRO A C     1 
ATOM   2649 O O     . PRO A 1 369 ? -17.211 9.912   -53.473 1.00 30.38  ? 350 PRO A O     1 
ATOM   2650 C CB    . PRO A 1 369 ? -18.723 12.444  -52.617 1.00 31.35  ? 350 PRO A CB    1 
ATOM   2651 C CG    . PRO A 1 369 ? -17.840 13.505  -51.965 1.00 33.26  ? 350 PRO A CG    1 
ATOM   2652 C CD    . PRO A 1 369 ? -16.663 12.754  -51.372 1.00 31.32  ? 350 PRO A CD    1 
ATOM   2653 N N     . ALA A 1 370 ? -19.170 9.028   -52.830 1.00 29.83  ? 351 ALA A N     1 
ATOM   2654 C CA    . ALA A 1 370 ? -18.937 7.711   -53.418 1.00 27.78  ? 351 ALA A CA    1 
ATOM   2655 C C     . ALA A 1 370 ? -18.433 7.779   -54.859 1.00 30.23  ? 351 ALA A C     1 
ATOM   2656 O O     . ALA A 1 370 ? -17.475 7.089   -55.212 1.00 29.51  ? 351 ALA A O     1 
ATOM   2657 C CB    . ALA A 1 370 ? -20.183 6.856   -53.370 1.00 33.05  ? 351 ALA A CB    1 
ATOM   2658 N N     . ALA A 1 371 ? -19.071 8.609   -55.700 1.00 28.15  ? 352 ALA A N     1 
ATOM   2659 C CA    . ALA A 1 371 ? -18.726 8.690   -57.105 1.00 30.31  ? 352 ALA A CA    1 
ATOM   2660 C C     . ALA A 1 371 ? -17.290 9.191   -57.261 1.00 27.87  ? 352 ALA A C     1 
ATOM   2661 O O     . ALA A 1 371 ? -16.569 8.764   -58.163 1.00 30.38  ? 352 ALA A O     1 
ATOM   2662 C CB    . ALA A 1 371 ? -19.681 9.626   -57.822 1.00 30.19  ? 352 ALA A CB    1 
ATOM   2663 N N     . ARG A 1 372 ? -16.914 10.146  -56.400 1.00 27.25  ? 353 ARG A N     1 
ATOM   2664 C CA    . ARG A 1 372 ? -15.620 10.804  -56.482 1.00 27.95  ? 353 ARG A CA    1 
ATOM   2665 C C     . ARG A 1 372 ? -14.507 9.965   -55.856 1.00 27.35  ? 353 ARG A C     1 
ATOM   2666 O O     . ARG A 1 372 ? -13.331 10.186  -56.157 1.00 26.85  ? 353 ARG A O     1 
ATOM   2667 C CB    . ARG A 1 372 ? -15.714 12.189  -55.851 1.00 31.52  ? 353 ARG A CB    1 
ATOM   2668 C CG    . ARG A 1 372 ? -16.748 13.049  -56.573 1.00 38.24  ? 353 ARG A CG    1 
ATOM   2669 C CD    . ARG A 1 372 ? -17.155 14.285  -55.829 1.00 44.82  ? 353 ARG A CD    1 
ATOM   2670 N NE    . ARG A 1 372 ? -15.984 15.139  -55.737 1.00 50.29  ? 353 ARG A NE    1 
ATOM   2671 C CZ    . ARG A 1 372 ? -15.769 16.179  -56.517 1.00 54.76  ? 353 ARG A CZ    1 
ATOM   2672 N NH1   . ARG A 1 372 ? -14.725 16.952  -56.279 1.00 50.48  ? 353 ARG A NH1   1 
ATOM   2673 N NH2   . ARG A 1 372 ? -16.622 16.442  -57.502 1.00 47.37  ? 353 ARG A NH2   1 
ATOM   2674 N N     . THR A 1 373 ? -14.851 9.057   -54.947 1.00 26.57  ? 354 THR A N     1 
ATOM   2675 C CA    . THR A 1 373 ? -13.835 8.326   -54.195 1.00 26.63  ? 354 THR A CA    1 
ATOM   2676 C C     . THR A 1 373 ? -13.650 6.928   -54.756 1.00 25.81  ? 354 THR A C     1 
ATOM   2677 O O     . THR A 1 373 ? -12.706 6.255   -54.333 1.00 26.80  ? 354 THR A O     1 
ATOM   2678 C CB    . THR A 1 373 ? -14.149 8.272   -52.691 1.00 27.05  ? 354 THR A CB    1 
ATOM   2679 O OG1   . THR A 1 373 ? -15.371 7.562   -52.489 1.00 25.24  ? 354 THR A OG1   1 
ATOM   2680 C CG2   . THR A 1 373 ? -14.272 9.660   -52.098 1.00 26.47  ? 354 THR A CG2   1 
ATOM   2681 N N     . ALA A 1 374 ? -14.450 6.518   -55.756 1.00 25.97  ? 355 ALA A N     1 
ATOM   2682 C CA    . ALA A 1 374 ? -14.386 5.150   -56.270 1.00 27.20  ? 355 ALA A CA    1 
ATOM   2683 C C     . ALA A 1 374 ? -12.981 4.791   -56.751 1.00 26.87  ? 355 ALA A C     1 
ATOM   2684 O O     . ALA A 1 374 ? -12.550 3.646   -56.614 1.00 26.91  ? 355 ALA A O     1 
ATOM   2685 C CB    . ALA A 1 374 ? -15.392 4.925   -57.382 1.00 31.94  ? 355 ALA A CB    1 
ATOM   2686 N N     . GLY A 1 375 ? -12.298 5.743   -57.376 1.00 27.18  ? 356 GLY A N     1 
ATOM   2687 C CA    . GLY A 1 375 ? -10.972 5.473   -57.936 1.00 27.96  ? 356 GLY A CA    1 
ATOM   2688 C C     . GLY A 1 375 ? -9.917  5.203   -56.862 1.00 26.64  ? 356 GLY A C     1 
ATOM   2689 O O     . GLY A 1 375 ? -9.118  4.251   -56.987 1.00 25.23  ? 356 GLY A O     1 
ATOM   2690 N N     . ALA A 1 376 ? -9.923  6.046   -55.816 1.00 26.74  ? 357 ALA A N     1 
ATOM   2691 C CA    . ALA A 1 376 ? -9.060  5.856   -54.646 1.00 25.25  ? 357 ALA A CA    1 
ATOM   2692 C C     . ALA A 1 376 ? -9.363  4.555   -53.926 1.00 24.86  ? 357 ALA A C     1 
ATOM   2693 O O     . ALA A 1 376 ? -8.457  3.832   -53.541 1.00 24.14  ? 357 ALA A O     1 
ATOM   2694 C CB    . ALA A 1 376 ? -9.130  7.019   -53.715 1.00 27.12  ? 357 ALA A CB    1 
ATOM   2695 N N     . ARG A 1 377 ? -10.642 4.212   -53.788 1.00 24.87  ? 358 ARG A N     1 
ATOM   2696 C CA    . ARG A 1 377 ? -11.013 2.945   -53.200 1.00 24.92  ? 358 ARG A CA    1 
ATOM   2697 C C     . ARG A 1 377 ? -10.471 1.774   -54.014 1.00 27.01  ? 358 ARG A C     1 
ATOM   2698 O O     . ARG A 1 377 ? -9.977  0.815   -53.428 1.00 26.60  ? 358 ARG A O     1 
ATOM   2699 C CB    . ARG A 1 377 ? -12.534 2.887   -53.043 1.00 25.91  ? 358 ARG A CB    1 
ATOM   2700 C CG    . ARG A 1 377 ? -13.052 1.619   -52.380 1.00 27.42  ? 358 ARG A CG    1 
ATOM   2701 C CD    . ARG A 1 377 ? -14.553 1.733   -52.221 1.00 25.88  ? 358 ARG A CD    1 
ATOM   2702 N NE    . ARG A 1 377 ? -15.061 0.656   -51.399 1.00 25.79  ? 358 ARG A NE    1 
ATOM   2703 C CZ    . ARG A 1 377 ? -14.886 0.575   -50.092 1.00 24.81  ? 358 ARG A CZ    1 
ATOM   2704 N NH1   . ARG A 1 377 ? -14.451 1.630   -49.416 1.00 25.41  ? 358 ARG A NH1   1 
ATOM   2705 N NH2   . ARG A 1 377 ? -15.163 -0.565  -49.483 1.00 27.29  ? 358 ARG A NH2   1 
ATOM   2706 N N     . SER A 1 378 ? -10.599 1.826   -55.344 1.00 23.75  ? 359 SER A N     1 
ATOM   2707 C CA    . SER A 1 378 ? -10.125 0.764   -56.214 1.00 25.53  ? 359 SER A CA    1 
ATOM   2708 C C     . SER A 1 378 ? -8.607  0.649   -56.157 1.00 26.00  ? 359 SER A C     1 
ATOM   2709 O O     . SER A 1 378 ? -8.080  -0.451  -56.131 1.00 26.55  ? 359 SER A O     1 
ATOM   2710 C CB    . SER A 1 378 ? -10.609 1.027   -57.630 1.00 28.95  ? 359 SER A CB    1 
ATOM   2711 O OG    . SER A 1 378 ? -10.179 0.014   -58.501 1.00 31.98  ? 359 SER A OG    1 
ATOM   2712 N N     . LEU A 1 379 ? -7.927  1.792   -56.072 1.00 25.69  ? 360 LEU A N     1 
ATOM   2713 C CA    . LEU A 1 379 ? -6.479  1.808   -55.916 1.00 27.40  ? 360 LEU A CA    1 
ATOM   2714 C C     . LEU A 1 379 ? -6.056  1.050   -54.658 1.00 25.74  ? 360 LEU A C     1 
ATOM   2715 O O     . LEU A 1 379 ? -5.197  0.173   -54.733 1.00 24.95  ? 360 LEU A O     1 
ATOM   2716 C CB    . LEU A 1 379 ? -5.978  3.250   -55.852 1.00 28.88  ? 360 LEU A CB    1 
ATOM   2717 C CG    . LEU A 1 379 ? -4.536  3.425   -55.358 1.00 32.62  ? 360 LEU A CG    1 
ATOM   2718 C CD1   . LEU A 1 379 ? -3.578  2.972   -56.432 1.00 30.46  ? 360 LEU A CD1   1 
ATOM   2719 C CD2   . LEU A 1 379 ? -4.269  4.875   -54.947 1.00 33.16  ? 360 LEU A CD2   1 
ATOM   2720 N N     . VAL A 1 380 ? -6.685  1.372   -53.519 1.00 26.34  ? 361 VAL A N     1 
ATOM   2721 C CA    . VAL A 1 380 ? -6.290  0.780   -52.244 1.00 26.14  ? 361 VAL A CA    1 
ATOM   2722 C C     . VAL A 1 380 ? -6.611  -0.717  -52.218 1.00 25.45  ? 361 VAL A C     1 
ATOM   2723 O O     . VAL A 1 380 ? -5.788  -1.508  -51.769 1.00 25.93  ? 361 VAL A O     1 
ATOM   2724 C CB    . VAL A 1 380 ? -6.872  1.552   -51.050 1.00 26.63  ? 361 VAL A CB    1 
ATOM   2725 C CG1   . VAL A 1 380 ? -6.648  0.798   -49.747 1.00 27.45  ? 361 VAL A CG1   1 
ATOM   2726 C CG2   . VAL A 1 380 ? -6.313  2.968   -50.995 1.00 27.55  ? 361 VAL A CG2   1 
ATOM   2727 N N     . ALA A 1 381 ? -7.750  -1.108  -52.791 1.00 25.98  ? 362 ALA A N     1 
ATOM   2728 C CA    . ALA A 1 381 ? -8.102  -2.503  -52.985 1.00 26.94  ? 362 ALA A CA    1 
ATOM   2729 C C     . ALA A 1 381 ? -7.022  -3.227  -53.791 1.00 31.17  ? 362 ALA A C     1 
ATOM   2730 O O     . ALA A 1 381 ? -6.690  -4.349  -53.433 1.00 27.40  ? 362 ALA A O     1 
ATOM   2731 C CB    . ALA A 1 381 ? -9.449  -2.628  -53.642 1.00 28.97  ? 362 ALA A CB    1 
ATOM   2732 N N     . ASP A 1 382 ? -6.512  -2.594  -54.864 1.00 31.12  ? 363 ASP A N     1 
ATOM   2733 C CA    . ASP A 1 382 ? -5.433  -3.159  -55.668 1.00 33.21  ? 363 ASP A CA    1 
ATOM   2734 C C     . ASP A 1 382 ? -4.170  -3.282  -54.831 1.00 29.93  ? 363 ASP A C     1 
ATOM   2735 O O     . ASP A 1 382 ? -3.497  -4.313  -54.876 1.00 27.64  ? 363 ASP A O     1 
ATOM   2736 C CB    . ASP A 1 382 ? -5.045  -2.305  -56.887 1.00 36.87  ? 363 ASP A CB    1 
ATOM   2737 C CG    . ASP A 1 382 ? -6.042  -2.231  -58.040 1.00 46.27  ? 363 ASP A CG    1 
ATOM   2738 O OD1   . ASP A 1 382 ? -6.954  -3.084  -58.095 1.00 44.72  ? 363 ASP A OD1   1 
ATOM   2739 O OD2   . ASP A 1 382 ? -5.862  -1.326  -58.923 1.00 45.03  ? 363 ASP A OD2   1 
ATOM   2740 N N     . LEU A 1 383 ? -3.753  -2.181  -54.188 1.00 26.81  ? 364 LEU A N     1 
ATOM   2741 C CA    . LEU A 1 383 ? -2.536  -2.238  -53.379 1.00 28.12  ? 364 LEU A CA    1 
ATOM   2742 C C     . LEU A 1 383 ? -2.619  -3.313  -52.286 1.00 29.29  ? 364 LEU A C     1 
ATOM   2743 O O     . LEU A 1 383 ? -1.595  -3.917  -51.969 1.00 25.34  ? 364 LEU A O     1 
ATOM   2744 C CB    . LEU A 1 383 ? -2.240  -0.871  -52.782 1.00 27.24  ? 364 LEU A CB    1 
ATOM   2745 C CG    . LEU A 1 383 ? -2.004  0.250   -53.781 1.00 28.60  ? 364 LEU A CG    1 
ATOM   2746 C CD1   . LEU A 1 383 ? -1.687  1.544   -53.058 1.00 29.31  ? 364 LEU A CD1   1 
ATOM   2747 C CD2   . LEU A 1 383 ? -0.904  -0.128  -54.733 1.00 29.22  ? 364 LEU A CD2   1 
ATOM   2748 N N     . ALA A 1 384 ? -3.826  -3.594  -51.766 1.00 27.09  ? 365 ALA A N     1 
ATOM   2749 C CA    . ALA A 1 384 ? -4.015  -4.514  -50.654 1.00 27.98  ? 365 ALA A CA    1 
ATOM   2750 C C     . ALA A 1 384 ? -3.790  -5.969  -51.080 1.00 29.16  ? 365 ALA A C     1 
ATOM   2751 O O     . ALA A 1 384 ? -3.702  -6.858  -50.246 1.00 28.92  ? 365 ALA A O     1 
ATOM   2752 C CB    . ALA A 1 384 ? -5.397  -4.312  -50.055 1.00 28.93  ? 365 ALA A CB    1 
ATOM   2753 N N     . ARG A 1 385 ? -3.666  -6.219  -52.382 1.00 32.10  ? 366 ARG A N     1 
ATOM   2754 C CA    . ARG A 1 385 ? -3.228  -7.529  -52.855 1.00 33.00  ? 366 ARG A CA    1 
ATOM   2755 C C     . ARG A 1 385 ? -1.774  -7.825  -52.490 1.00 27.61  ? 366 ARG A C     1 
ATOM   2756 O O     . ARG A 1 385 ? -1.411  -8.992  -52.297 1.00 29.80  ? 366 ARG A O     1 
ATOM   2757 C CB    . ARG A 1 385 ? -3.430  -7.638  -54.372 1.00 37.98  ? 366 ARG A CB    1 
ATOM   2758 C CG    . ARG A 1 385 ? -4.908  -7.680  -54.741 1.00 52.09  ? 366 ARG A CG    1 
ATOM   2759 C CD    . ARG A 1 385 ? -5.236  -7.646  -56.234 1.00 64.34  ? 366 ARG A CD    1 
ATOM   2760 N NE    . ARG A 1 385 ? -6.688  -7.681  -56.405 1.00 83.96  ? 366 ARG A NE    1 
ATOM   2761 C CZ    . ARG A 1 385 ? -7.446  -6.681  -56.857 1.00 91.89  ? 366 ARG A CZ    1 
ATOM   2762 N NH1   . ARG A 1 385 ? -6.904  -5.622  -57.430 1.00 90.52  ? 366 ARG A NH1   1 
ATOM   2763 N NH2   . ARG A 1 385 ? -8.762  -6.765  -56.765 1.00 93.13  ? 366 ARG A NH2   1 
ATOM   2764 N N     . PHE A 1 386 ? -0.927  -6.801  -52.351 1.00 24.77  ? 367 PHE A N     1 
ATOM   2765 C CA    . PHE A 1 386 ? 0.445   -7.074  -51.965 1.00 26.49  ? 367 PHE A CA    1 
ATOM   2766 C C     . PHE A 1 386 ? 0.525   -7.493  -50.484 1.00 29.24  ? 367 PHE A C     1 
ATOM   2767 O O     . PHE A 1 386 ? -0.219  -7.021  -49.629 1.00 26.24  ? 367 PHE A O     1 
ATOM   2768 C CB    . PHE A 1 386 ? 1.319   -5.848  -52.188 1.00 25.62  ? 367 PHE A CB    1 
ATOM   2769 C CG    . PHE A 1 386 ? 1.396   -5.356  -53.610 1.00 27.16  ? 367 PHE A CG    1 
ATOM   2770 C CD1   . PHE A 1 386 ? 1.884   -6.189  -54.613 1.00 30.85  ? 367 PHE A CD1   1 
ATOM   2771 C CD2   . PHE A 1 386 ? 1.063   -4.037  -53.930 1.00 28.28  ? 367 PHE A CD2   1 
ATOM   2772 C CE1   . PHE A 1 386 ? 2.011   -5.717  -55.917 1.00 31.71  ? 367 PHE A CE1   1 
ATOM   2773 C CE2   . PHE A 1 386 ? 1.166   -3.572  -55.233 1.00 30.25  ? 367 PHE A CE2   1 
ATOM   2774 C CZ    . PHE A 1 386 ? 1.635   -4.417  -56.225 1.00 32.67  ? 367 PHE A CZ    1 
ATOM   2775 N N     . GLU A 1 387 ? 1.480   -8.368  -50.162 1.00 28.97  ? 368 GLU A N     1 
ATOM   2776 C CA    . GLU A 1 387 ? 1.608   -8.909  -48.818 1.00 28.57  ? 368 GLU A CA    1 
ATOM   2777 C C     . GLU A 1 387 ? 1.964   -7.808  -47.824 1.00 26.60  ? 368 GLU A C     1 
ATOM   2778 O O     . GLU A 1 387 ? 1.421   -7.784  -46.727 1.00 26.21  ? 368 GLU A O     1 
ATOM   2779 C CB    . GLU A 1 387 ? 2.610   -10.069 -48.804 1.00 32.65  ? 368 GLU A CB    1 
ATOM   2780 C CG    . GLU A 1 387 ? 2.058   -11.316 -49.479 1.00 39.38  ? 368 GLU A CG    1 
ATOM   2781 C CD    . GLU A 1 387 ? 2.942   -12.555 -49.357 1.00 52.17  ? 368 GLU A CD    1 
ATOM   2782 O OE1   . GLU A 1 387 ? 4.079   -12.441 -48.811 1.00 50.92  ? 368 GLU A OE1   1 
ATOM   2783 O OE2   . GLU A 1 387 ? 2.502   -13.640 -49.817 1.00 56.35  ? 368 GLU A OE2   1 
ATOM   2784 N N     . ASP A 1 388 ? 2.897   -6.910  -48.159 1.00 25.45  ? 369 ASP A N     1 
ATOM   2785 C CA    . ASP A 1 388 ? 3.307   -5.930  -47.178 1.00 26.74  ? 369 ASP A CA    1 
ATOM   2786 C C     . ASP A 1 388 ? 2.215   -4.899  -46.910 1.00 25.99  ? 369 ASP A C     1 
ATOM   2787 O O     . ASP A 1 388 ? 2.095   -4.431  -45.774 1.00 26.28  ? 369 ASP A O     1 
ATOM   2788 C CB    . ASP A 1 388 ? 4.619   -5.259  -47.555 1.00 29.67  ? 369 ASP A CB    1 
ATOM   2789 C CG    . ASP A 1 388 ? 4.820   -4.867  -49.011 1.00 36.31  ? 369 ASP A CG    1 
ATOM   2790 O OD1   . ASP A 1 388 ? 3.810   -4.660  -49.758 1.00 33.63  ? 369 ASP A OD1   1 
ATOM   2791 O OD2   . ASP A 1 388 ? 6.002   -4.760  -49.396 1.00 34.92  ? 369 ASP A OD2   1 
ATOM   2792 N N     . VAL A 1 389 ? 1.459   -4.540  -47.941 1.00 23.85  ? 370 VAL A N     1 
ATOM   2793 C CA    . VAL A 1 389 ? 0.282   -3.693  -47.737 1.00 23.63  ? 370 VAL A CA    1 
ATOM   2794 C C     . VAL A 1 389 ? -0.758  -4.400  -46.870 1.00 24.34  ? 370 VAL A C     1 
ATOM   2795 O O     . VAL A 1 389 ? -1.234  -3.810  -45.904 1.00 25.26  ? 370 VAL A O     1 
ATOM   2796 C CB    . VAL A 1 389 ? -0.323  -3.200  -49.051 1.00 25.17  ? 370 VAL A CB    1 
ATOM   2797 C CG1   . VAL A 1 389 ? -1.600  -2.389  -48.813 1.00 24.66  ? 370 VAL A CG1   1 
ATOM   2798 C CG2   . VAL A 1 389 ? 0.678   -2.387  -49.817 1.00 26.09  ? 370 VAL A CG2   1 
ATOM   2799 N N     . ASN A 1 390 ? -1.037  -5.684  -47.126 1.00 22.82  ? 371 ASN A N     1 
ATOM   2800 C CA    . ASN A 1 390 ? -2.016  -6.413  -46.353 1.00 24.52  ? 371 ASN A CA    1 
ATOM   2801 C C     . ASN A 1 390 ? -1.623  -6.422  -44.871 1.00 24.21  ? 371 ASN A C     1 
ATOM   2802 O O     . ASN A 1 390 ? -2.444  -6.180  -43.986 1.00 23.23  ? 371 ASN A O     1 
ATOM   2803 C CB    . ASN A 1 390 ? -2.224  -7.825  -46.899 1.00 24.63  ? 371 ASN A CB    1 
ATOM   2804 C CG    . ASN A 1 390 ? -3.183  -8.654  -46.076 1.00 26.64  ? 371 ASN A CG    1 
ATOM   2805 O OD1   . ASN A 1 390 ? -4.394  -8.408  -46.032 1.00 25.44  ? 371 ASN A OD1   1 
ATOM   2806 N ND2   . ASN A 1 390 ? -2.633  -9.641  -45.386 1.00 28.86  ? 371 ASN A ND2   1 
ATOM   2807 N N     . ARG A 1 391 ? -0.336  -6.692  -44.587 1.00 25.27  ? 372 ARG A N     1 
ATOM   2808 C CA    . ARG A 1 391 ? 0.149   -6.739  -43.227 1.00 26.41  ? 372 ARG A CA    1 
ATOM   2809 C C     . ARG A 1 391 ? 0.003   -5.365  -42.563 1.00 25.10  ? 372 ARG A C     1 
ATOM   2810 O O     . ARG A 1 391 ? -0.361  -5.287  -41.401 1.00 24.69  ? 372 ARG A O     1 
ATOM   2811 C CB    . ARG A 1 391 ? 1.617   -7.178  -43.207 1.00 29.55  ? 372 ARG A CB    1 
ATOM   2812 C CG    . ARG A 1 391 ? 2.246   -7.162  -41.819 1.00 28.82  ? 372 ARG A CG    1 
ATOM   2813 C CD    . ARG A 1 391 ? 3.714   -7.527  -41.792 1.00 30.81  ? 372 ARG A CD    1 
ATOM   2814 N NE    . ARG A 1 391 ? 3.933   -8.934  -42.128 1.00 37.01  ? 372 ARG A NE    1 
ATOM   2815 C CZ    . ARG A 1 391 ? 3.878   -9.939  -41.266 1.00 44.19  ? 372 ARG A CZ    1 
ATOM   2816 N NH1   . ARG A 1 391 ? 4.071   -11.177 -41.685 1.00 44.52  ? 372 ARG A NH1   1 
ATOM   2817 N NH2   . ARG A 1 391 ? 3.637   -9.707  -39.985 1.00 41.76  ? 372 ARG A NH2   1 
ATOM   2818 N N     . TYR A 1 392 ? 0.364   -4.298  -43.268 1.00 23.71  ? 373 TYR A N     1 
ATOM   2819 C CA    . TYR A 1 392 ? 0.283   -2.962  -42.719 1.00 28.05  ? 373 TYR A CA    1 
ATOM   2820 C C     . TYR A 1 392 ? -1.158  -2.660  -42.315 1.00 26.40  ? 373 TYR A C     1 
ATOM   2821 O O     . TYR A 1 392 ? -1.421  -2.253  -41.191 1.00 27.76  ? 373 TYR A O     1 
ATOM   2822 C CB    . TYR A 1 392 ? 0.833   -1.942  -43.708 1.00 28.77  ? 373 TYR A CB    1 
ATOM   2823 C CG    . TYR A 1 392 ? 0.656   -0.502  -43.307 1.00 34.33  ? 373 TYR A CG    1 
ATOM   2824 C CD1   . TYR A 1 392 ? -0.559  0.128   -43.490 1.00 32.97  ? 373 TYR A CD1   1 
ATOM   2825 C CD2   . TYR A 1 392 ? 1.693   0.217   -42.746 1.00 39.53  ? 373 TYR A CD2   1 
ATOM   2826 C CE1   . TYR A 1 392 ? -0.739  1.455   -43.145 1.00 39.78  ? 373 TYR A CE1   1 
ATOM   2827 C CE2   . TYR A 1 392 ? 1.524   1.544   -42.384 1.00 45.84  ? 373 TYR A CE2   1 
ATOM   2828 C CZ    . TYR A 1 392 ? 0.306   2.160   -42.581 1.00 46.78  ? 373 TYR A CZ    1 
ATOM   2829 O OH    . TYR A 1 392 ? 0.088   3.476   -42.242 1.00 65.13  ? 373 TYR A OH    1 
ATOM   2830 N N     . LEU A 1 393 ? -2.101  -2.939  -43.199 1.00 24.72  ? 374 LEU A N     1 
ATOM   2831 C CA    . LEU A 1 393 ? -3.491  -2.615  -42.905 1.00 25.08  ? 374 LEU A CA    1 
ATOM   2832 C C     . LEU A 1 393 ? -4.073  -3.511  -41.806 1.00 25.27  ? 374 LEU A C     1 
ATOM   2833 O O     . LEU A 1 393 ? -4.827  -3.061  -40.939 1.00 25.39  ? 374 LEU A O     1 
ATOM   2834 C CB    . LEU A 1 393 ? -4.266  -2.741  -44.214 1.00 25.99  ? 374 LEU A CB    1 
ATOM   2835 C CG    . LEU A 1 393 ? -3.983  -1.706  -45.300 1.00 27.21  ? 374 LEU A CG    1 
ATOM   2836 C CD1   . LEU A 1 393 ? -4.840  -2.001  -46.515 1.00 28.20  ? 374 LEU A CD1   1 
ATOM   2837 C CD2   . LEU A 1 393 ? -4.238  -0.292  -44.832 1.00 28.73  ? 374 LEU A CD2   1 
ATOM   2838 N N     . VAL A 1 394 ? -3.800  -4.814  -41.850 1.00 22.66  ? 375 VAL A N     1 
ATOM   2839 C CA    . VAL A 1 394 ? -4.275  -5.727  -40.835 1.00 23.26  ? 375 VAL A CA    1 
ATOM   2840 C C     . VAL A 1 394 ? -3.756  -5.307  -39.460 1.00 22.96  ? 375 VAL A C     1 
ATOM   2841 O O     . VAL A 1 394 ? -4.497  -5.303  -38.481 1.00 22.11  ? 375 VAL A O     1 
ATOM   2842 C CB    . VAL A 1 394 ? -3.886  -7.188  -41.133 1.00 23.46  ? 375 VAL A CB    1 
ATOM   2843 C CG1   . VAL A 1 394 ? -4.065  -8.092  -39.915 1.00 25.06  ? 375 VAL A CG1   1 
ATOM   2844 C CG2   . VAL A 1 394 ? -4.662  -7.727  -42.314 1.00 24.82  ? 375 VAL A CG2   1 
ATOM   2845 N N     . GLU A 1 395 ? -2.450  -5.026  -39.350 1.00 21.82  ? 376 GLU A N     1 
ATOM   2846 C CA    . GLU A 1 395 ? -1.871  -4.684  -38.057 1.00 23.37  ? 376 GLU A CA    1 
ATOM   2847 C C     . GLU A 1 395 ? -2.450  -3.370  -37.534 1.00 23.36  ? 376 GLU A C     1 
ATOM   2848 O O     . GLU A 1 395 ? -2.586  -3.201  -36.321 1.00 24.47  ? 376 GLU A O     1 
ATOM   2849 C CB    . GLU A 1 395 ? -0.358  -4.641  -38.142 1.00 23.89  ? 376 GLU A CB    1 
ATOM   2850 C CG    . GLU A 1 395 ? 0.236   -6.043  -38.295 1.00 23.45  ? 376 GLU A CG    1 
ATOM   2851 C CD    . GLU A 1 395 ? 1.749   -6.125  -38.428 1.00 28.72  ? 376 GLU A CD    1 
ATOM   2852 O OE1   . GLU A 1 395 ? 2.395   -5.063  -38.502 1.00 36.40  ? 376 GLU A OE1   1 
ATOM   2853 O OE2   . GLU A 1 395 ? 2.290   -7.266  -38.499 1.00 36.82  ? 376 GLU A OE2   1 
ATOM   2854 N N     . LEU A 1 396 ? -2.791  -2.480  -38.450 1.00 25.30  ? 377 LEU A N     1 
ATOM   2855 C CA    . LEU A 1 396 ? -3.416  -1.197  -38.086 1.00 26.68  ? 377 LEU A CA    1 
ATOM   2856 C C     . LEU A 1 396 ? -4.813  -1.431  -37.520 1.00 25.03  ? 377 LEU A C     1 
ATOM   2857 O O     . LEU A 1 396 ? -5.096  -1.073  -36.357 1.00 24.16  ? 377 LEU A O     1 
ATOM   2858 C CB    . LEU A 1 396 ? -3.427  -0.298  -39.318 1.00 25.53  ? 377 LEU A CB    1 
ATOM   2859 C CG    . LEU A 1 396 ? -4.271  0.984   -39.213 1.00 28.23  ? 377 LEU A CG    1 
ATOM   2860 C CD1   . LEU A 1 396 ? -3.697  1.909   -38.168 1.00 32.38  ? 377 LEU A CD1   1 
ATOM   2861 C CD2   . LEU A 1 396 ? -4.341  1.683   -40.558 1.00 33.46  ? 377 LEU A CD2   1 
ATOM   2862 N N     . VAL A 1 397 ? -5.663  -2.103  -38.286 1.00 24.57  ? 378 VAL A N     1 
ATOM   2863 C CA    . VAL A 1 397 ? -7.072  -2.154  -37.936 1.00 27.43  ? 378 VAL A CA    1 
ATOM   2864 C C     . VAL A 1 397 ? -7.330  -3.070  -36.735 1.00 27.42  ? 378 VAL A C     1 
ATOM   2865 O O     . VAL A 1 397 ? -8.344  -2.906  -36.063 1.00 26.57  ? 378 VAL A O     1 
ATOM   2866 C CB    . VAL A 1 397 ? -7.993  -2.506  -39.113 1.00 28.25  ? 378 VAL A CB    1 
ATOM   2867 C CG1   . VAL A 1 397 ? -7.868  -1.478  -40.212 1.00 24.69  ? 378 VAL A CG1   1 
ATOM   2868 C CG2   . VAL A 1 397 ? -7.802  -3.938  -39.635 1.00 29.14  ? 378 VAL A CG2   1 
ATOM   2869 N N     . THR A 1 398 ? -6.459  -4.049  -36.481 1.00 22.87  ? 379 THR A N     1 
ATOM   2870 C CA    . THR A 1 398 ? -6.621  -4.944  -35.354 1.00 24.92  ? 379 THR A CA    1 
ATOM   2871 C C     . THR A 1 398 ? -6.058  -4.321  -34.072 1.00 23.51  ? 379 THR A C     1 
ATOM   2872 O O     . THR A 1 398 ? -6.265  -4.890  -33.021 1.00 26.61  ? 379 THR A O     1 
ATOM   2873 C CB    . THR A 1 398 ? -5.973  -6.315  -35.624 1.00 23.34  ? 379 THR A CB    1 
ATOM   2874 O OG1   . THR A 1 398 ? -4.553  -6.131  -35.823 1.00 25.77  ? 379 THR A OG1   1 
ATOM   2875 C CG2   . THR A 1 398 ? -6.610  -7.065  -36.763 1.00 22.77  ? 379 THR A CG2   1 
ATOM   2876 N N     . GLY A 1 399 ? -5.372  -3.148  -34.116 1.00 24.89  ? 380 GLY A N     1 
ATOM   2877 C CA    . GLY A 1 399 ? -4.903  -2.488  -32.897 1.00 25.90  ? 380 GLY A CA    1 
ATOM   2878 C C     . GLY A 1 399 ? -3.587  -3.055  -32.351 1.00 24.28  ? 380 GLY A C     1 
ATOM   2879 O O     . GLY A 1 399 ? -3.256  -2.882  -31.172 1.00 23.15  ? 380 GLY A O     1 
ATOM   2880 N N     . VAL A 1 400 ? -2.881  -3.774  -33.210 1.00 25.41  ? 381 VAL A N     1 
ATOM   2881 C CA    . VAL A 1 400 ? -1.715  -4.545  -32.836 1.00 27.74  ? 381 VAL A CA    1 
ATOM   2882 C C     . VAL A 1 400 ? -0.409  -3.835  -33.213 1.00 31.28  ? 381 VAL A C     1 
ATOM   2883 O O     . VAL A 1 400 ? 0.657   -4.227  -32.754 1.00 28.37  ? 381 VAL A O     1 
ATOM   2884 C CB    . VAL A 1 400 ? -1.951  -5.887  -33.546 1.00 35.64  ? 381 VAL A CB    1 
ATOM   2885 C CG1   . VAL A 1 400 ? -0.806  -6.417  -34.361 1.00 38.93  ? 381 VAL A CG1   1 
ATOM   2886 C CG2   . VAL A 1 400 ? -2.577  -6.891  -32.601 1.00 34.21  ? 381 VAL A CG2   1 
ATOM   2887 N N     . ASP A 1 401 ? -0.456  -2.802  -34.055 1.00 28.17  ? 382 ASP A N     1 
ATOM   2888 C CA    . ASP A 1 401 ? 0.789   -2.175  -34.496 1.00 28.66  ? 382 ASP A CA    1 
ATOM   2889 C C     . ASP A 1 401 ? 1.308   -1.034  -33.621 1.00 28.58  ? 382 ASP A C     1 
ATOM   2890 O O     . ASP A 1 401 ? 2.388   -0.539  -33.962 1.00 28.32  ? 382 ASP A O     1 
ATOM   2891 C CB    . ASP A 1 401 ? 0.671   -1.587  -35.897 1.00 30.81  ? 382 ASP A CB    1 
ATOM   2892 C CG    . ASP A 1 401 ? -0.329  -0.441  -36.007 1.00 31.10  ? 382 ASP A CG    1 
ATOM   2893 O OD1   . ASP A 1 401 ? -0.989  -0.140  -34.988 1.00 32.56  ? 382 ASP A OD1   1 
ATOM   2894 O OD2   . ASP A 1 401 ? -0.450  0.096   -37.124 1.00 32.24  ? 382 ASP A OD2   1 
ATOM   2895 N N     . PRO A 1 402 ? 0.667   -0.526  -32.521 1.00 27.78  ? 383 PRO A N     1 
ATOM   2896 C CA    . PRO A 1 402 ? 1.281   0.579   -31.769 1.00 28.00  ? 383 PRO A CA    1 
ATOM   2897 C C     . PRO A 1 402 ? 2.670   0.214   -31.270 1.00 29.26  ? 383 PRO A C     1 
ATOM   2898 O O     . PRO A 1 402 ? 2.891   -0.867  -30.735 1.00 27.20  ? 383 PRO A O     1 
ATOM   2899 C CB    . PRO A 1 402 ? 0.351   0.842   -30.561 1.00 29.91  ? 383 PRO A CB    1 
ATOM   2900 C CG    . PRO A 1 402 ? -1.001  0.309   -31.046 1.00 32.68  ? 383 PRO A CG    1 
ATOM   2901 C CD    . PRO A 1 402 ? -0.648  -0.882  -31.952 1.00 32.87  ? 383 PRO A CD    1 
ATOM   2902 N N     . ARG A 1 403 ? 3.601   1.150   -31.423 1.00 24.18  ? 384 ARG A N     1 
ATOM   2903 C CA    . ARG A 1 403 ? 4.931   0.972   -30.900 1.00 25.87  ? 384 ARG A CA    1 
ATOM   2904 C C     . ARG A 1 403 ? 5.353   2.323   -30.337 1.00 25.05  ? 384 ARG A C     1 
ATOM   2905 O O     . ARG A 1 403 ? 5.455   3.273   -31.083 1.00 24.49  ? 384 ARG A O     1 
ATOM   2906 C CB    . ARG A 1 403 ? 5.892   0.528   -31.993 1.00 26.76  ? 384 ARG A CB    1 
ATOM   2907 C CG    . ARG A 1 403 ? 7.316   0.329   -31.499 1.00 29.55  ? 384 ARG A CG    1 
ATOM   2908 C CD    . ARG A 1 403 ? 8.293   0.006   -32.603 1.00 29.60  ? 384 ARG A CD    1 
ATOM   2909 N NE    . ARG A 1 403 ? 7.954   -1.269  -33.207 1.00 27.44  ? 384 ARG A NE    1 
ATOM   2910 C CZ    . ARG A 1 403 ? 8.143   -2.452  -32.638 1.00 32.50  ? 384 ARG A CZ    1 
ATOM   2911 N NH1   . ARG A 1 403 ? 7.619   -3.526  -33.192 1.00 36.25  ? 384 ARG A NH1   1 
ATOM   2912 N NH2   . ARG A 1 403 ? 8.793   -2.564  -31.496 1.00 31.20  ? 384 ARG A NH2   1 
ATOM   2913 N N     . TYR A 1 404 ? 5.633   2.377   -29.046 1.00 23.51  ? 385 TYR A N     1 
ATOM   2914 C CA    . TYR A 1 404 ? 6.168   3.610   -28.494 1.00 23.66  ? 385 TYR A CA    1 
ATOM   2915 C C     . TYR A 1 404 ? 7.618   3.824   -28.910 1.00 25.04  ? 385 TYR A C     1 
ATOM   2916 O O     . TYR A 1 404 ? 8.406   2.897   -29.103 1.00 25.09  ? 385 TYR A O     1 
ATOM   2917 C CB    . TYR A 1 404 ? 5.950   3.622   -26.989 1.00 23.58  ? 385 TYR A CB    1 
ATOM   2918 C CG    . TYR A 1 404 ? 4.520   3.388   -26.562 1.00 25.86  ? 385 TYR A CG    1 
ATOM   2919 C CD1   . TYR A 1 404 ? 3.478   4.086   -27.142 1.00 24.62  ? 385 TYR A CD1   1 
ATOM   2920 C CD2   . TYR A 1 404 ? 4.212   2.487   -25.548 1.00 26.37  ? 385 TYR A CD2   1 
ATOM   2921 C CE1   . TYR A 1 404 ? 2.170   3.910   -26.729 1.00 26.87  ? 385 TYR A CE1   1 
ATOM   2922 C CE2   . TYR A 1 404 ? 2.902   2.274   -25.136 1.00 23.74  ? 385 TYR A CE2   1 
ATOM   2923 C CZ    . TYR A 1 404 ? 1.886   2.992   -25.733 1.00 27.23  ? 385 TYR A CZ    1 
ATOM   2924 O OH    . TYR A 1 404 ? 0.599   2.816   -25.363 1.00 27.43  ? 385 TYR A OH    1 
ATOM   2925 N N     . ARG A 1 405 ? 7.993   5.111   -28.943 1.00 26.33  ? 386 ARG A N     1 
ATOM   2926 C CA    . ARG A 1 405 ? 9.347   5.538   -29.234 1.00 31.27  ? 386 ARG A CA    1 
ATOM   2927 C C     . ARG A 1 405 ? 10.224  5.425   -27.989 1.00 28.48  ? 386 ARG A C     1 
ATOM   2928 O O     . ARG A 1 405 ? 10.152  6.221   -27.059 1.00 29.74  ? 386 ARG A O     1 
ATOM   2929 C CB    . ARG A 1 405 ? 9.316   6.988   -29.735 1.00 36.02  ? 386 ARG A CB    1 
ATOM   2930 C CG    . ARG A 1 405 ? 8.339   7.241   -30.877 1.00 47.22  ? 386 ARG A CG    1 
ATOM   2931 C CD    . ARG A 1 405 ? 8.938   7.043   -32.255 1.00 62.05  ? 386 ARG A CD    1 
ATOM   2932 N NE    . ARG A 1 405 ? 9.984   8.018   -32.540 1.00 72.68  ? 386 ARG A NE    1 
ATOM   2933 C CZ    . ARG A 1 405 ? 9.806   9.327   -32.557 1.00 71.20  ? 386 ARG A CZ    1 
ATOM   2934 N NH1   . ARG A 1 405 ? 10.854  10.128  -32.639 1.00 69.86  ? 386 ARG A NH1   1 
ATOM   2935 N NH2   . ARG A 1 405 ? 8.588   9.823   -32.432 1.00 75.86  ? 386 ARG A NH2   1 
ATOM   2936 N N     . VAL A 1 406 ? 11.103  4.446   -28.009 1.00 27.16  ? 387 VAL A N     1 
ATOM   2937 C CA    . VAL A 1 406 ? 11.983  4.145   -26.911 1.00 30.00  ? 387 VAL A CA    1 
ATOM   2938 C C     . VAL A 1 406 ? 13.362  3.924   -27.522 1.00 32.00  ? 387 VAL A C     1 
ATOM   2939 O O     . VAL A 1 406 ? 13.529  3.097   -28.424 1.00 29.23  ? 387 VAL A O     1 
ATOM   2940 C CB    . VAL A 1 406 ? 11.509  2.870   -26.174 1.00 29.18  ? 387 VAL A CB    1 
ATOM   2941 C CG1   . VAL A 1 406 ? 12.451  2.563   -25.033 1.00 26.24  ? 387 VAL A CG1   1 
ATOM   2942 C CG2   . VAL A 1 406 ? 10.053  2.966   -25.727 1.00 30.83  ? 387 VAL A CG2   1 
ATOM   2943 N N     . GLY A 1 407 ? 14.353  4.685   -27.050 1.00 33.84  ? 388 GLY A N     1 
ATOM   2944 C CA    . GLY A 1 407 ? 15.689  4.563   -27.609 1.00 31.74  ? 388 GLY A CA    1 
ATOM   2945 C C     . GLY A 1 407 ? 16.539  3.524   -26.890 1.00 33.45  ? 388 GLY A C     1 
ATOM   2946 O O     . GLY A 1 407 ? 16.092  2.876   -25.952 1.00 30.68  ? 388 GLY A O     1 
ATOM   2947 N N     . THR A 1 408 ? 17.795  3.412   -27.334 1.00 31.07  ? 389 THR A N     1 
ATOM   2948 C CA    . THR A 1 408 ? 18.812  2.617   -26.676 1.00 35.33  ? 389 THR A CA    1 
ATOM   2949 C C     . THR A 1 408 ? 18.809  2.912   -25.175 1.00 33.95  ? 389 THR A C     1 
ATOM   2950 O O     . THR A 1 408 ? 18.571  4.047   -24.767 1.00 33.02  ? 389 THR A O     1 
ATOM   2951 C CB    . THR A 1 408 ? 20.191  2.943   -27.272 1.00 41.72  ? 389 THR A CB    1 
ATOM   2952 O OG1   . THR A 1 408 ? 20.090  2.743   -28.686 1.00 45.27  ? 389 THR A OG1   1 
ATOM   2953 C CG2   . THR A 1 408 ? 21.301  2.090   -26.699 1.00 40.91  ? 389 THR A CG2   1 
ATOM   2954 N N     . ASP A 1 409 ? 19.046  1.872   -24.362 1.00 35.59  ? 390 ASP A N     1 
ATOM   2955 C CA    . ASP A 1 409 ? 19.082  2.015   -22.909 1.00 38.29  ? 390 ASP A CA    1 
ATOM   2956 C C     . ASP A 1 409 ? 17.684  2.341   -22.370 1.00 37.65  ? 390 ASP A C     1 
ATOM   2957 O O     . ASP A 1 409 ? 17.559  2.779   -21.229 1.00 36.57  ? 390 ASP A O     1 
ATOM   2958 C CB    . ASP A 1 409 ? 20.034  3.136   -22.455 1.00 38.16  ? 390 ASP A CB    1 
ATOM   2959 C CG    . ASP A 1 409 ? 21.529  2.971   -22.731 1.00 40.43  ? 390 ASP A CG    1 
ATOM   2960 O OD1   . ASP A 1 409 ? 22.005  1.834   -22.942 1.00 39.16  ? 390 ASP A OD1   1 
ATOM   2961 O OD2   . ASP A 1 409 ? 22.212  3.999   -22.739 1.00 46.27  ? 390 ASP A OD2   1 
ATOM   2962 N N     . GLY A 1 410 ? 16.628  2.128   -23.168 1.00 35.90  ? 391 GLY A N     1 
ATOM   2963 C CA    . GLY A 1 410 ? 15.259  2.382   -22.726 1.00 33.00  ? 391 GLY A CA    1 
ATOM   2964 C C     . GLY A 1 410 ? 14.886  3.862   -22.628 1.00 32.63  ? 391 GLY A C     1 
ATOM   2965 O O     . GLY A 1 410 ? 13.910  4.214   -21.973 1.00 33.12  ? 391 GLY A O     1 
ATOM   2966 N N     . ALA A 1 411 ? 15.615  4.753   -23.306 1.00 32.41  ? 392 ALA A N     1 
ATOM   2967 C CA    . ALA A 1 411 ? 15.361  6.181   -23.183 1.00 36.24  ? 392 ALA A CA    1 
ATOM   2968 C C     . ALA A 1 411 ? 14.003  6.544   -23.790 1.00 36.18  ? 392 ALA A C     1 
ATOM   2969 O O     . ALA A 1 411 ? 13.735  6.216   -24.934 1.00 35.01  ? 392 ALA A O     1 
ATOM   2970 C CB    . ALA A 1 411 ? 16.471  6.969   -23.853 1.00 40.28  ? 392 ALA A CB    1 
ATOM   2971 N N     . SER A 1 412 ? 13.185  7.297   -23.053 1.00 39.14  ? 393 SER A N     1 
ATOM   2972 C CA    . SER A 1 412 ? 11.865  7.692   -23.522 1.00 41.19  ? 393 SER A CA    1 
ATOM   2973 C C     . SER A 1 412 ? 11.959  8.814   -24.552 1.00 51.65  ? 393 SER A C     1 
ATOM   2974 O O     . SER A 1 412 ? 12.842  9.668   -24.461 1.00 42.25  ? 393 SER A O     1 
ATOM   2975 C CB    . SER A 1 412 ? 10.972  8.118   -22.393 1.00 42.93  ? 393 SER A CB    1 
ATOM   2976 O OG    . SER A 1 412 ? 11.340  9.392   -21.863 1.00 46.59  ? 393 SER A OG    1 
ATOM   2977 N N     . GLY A 1 413 ? 11.032  8.786   -25.525 1.00 54.66  ? 394 GLY A N     1 
ATOM   2978 C CA    . GLY A 1 413 ? 10.831  9.878   -26.467 1.00 60.62  ? 394 GLY A CA    1 
ATOM   2979 C C     . GLY A 1 413 ? 12.081  10.193  -27.287 1.00 64.54  ? 394 GLY A C     1 
ATOM   2980 O O     . GLY A 1 413 ? 12.344  11.351  -27.588 1.00 66.10  ? 394 GLY A O     1 
ATOM   2981 N N     . SER A 1 414 ? 12.831  9.146   -27.648 1.00 65.21  ? 395 SER A N     1 
ATOM   2982 C CA    . SER A 1 414 ? 14.105  9.287   -28.333 1.00 62.56  ? 395 SER A CA    1 
ATOM   2983 C C     . SER A 1 414 ? 13.894  9.945   -29.693 1.00 57.13  ? 395 SER A C     1 
ATOM   2984 O O     . SER A 1 414 ? 12.834  9.769   -30.301 1.00 55.86  ? 395 SER A O     1 
ATOM   2985 C CB    . SER A 1 414 ? 14.747  7.930   -28.492 1.00 61.87  ? 395 SER A CB    1 
ATOM   2986 O OG    . SER A 1 414 ? 16.110  8.051   -28.845 1.00 67.83  ? 395 SER A OG    1 
ATOM   2987 N N     . VAL A 1 415 ? 14.925  10.654  -30.177 1.00 45.88  ? 396 VAL A N     1 
ATOM   2988 C CA    . VAL A 1 415 ? 14.977  11.102  -31.565 1.00 46.37  ? 396 VAL A CA    1 
ATOM   2989 C C     . VAL A 1 415 ? 15.447  9.938   -32.436 1.00 43.15  ? 396 VAL A C     1 
ATOM   2990 O O     . VAL A 1 415 ? 15.251  9.963   -33.636 1.00 46.34  ? 396 VAL A O     1 
ATOM   2991 C CB    . VAL A 1 415 ? 15.932  12.293  -31.799 1.00 55.28  ? 396 VAL A CB    1 
ATOM   2992 C CG1   . VAL A 1 415 ? 15.546  13.056  -33.059 1.00 57.31  ? 396 VAL A CG1   1 
ATOM   2993 C CG2   . VAL A 1 415 ? 16.012  13.233  -30.612 1.00 58.39  ? 396 VAL A CG2   1 
ATOM   2994 N N     . VAL A 1 416 ? 16.145  8.973   -31.826 1.00 40.49  ? 397 VAL A N     1 
ATOM   2995 C CA    . VAL A 1 416 ? 16.684  7.814   -32.516 1.00 51.88  ? 397 VAL A CA    1 
ATOM   2996 C C     . VAL A 1 416 ? 16.040  6.579   -31.885 1.00 42.03  ? 397 VAL A C     1 
ATOM   2997 O O     . VAL A 1 416 ? 16.679  5.856   -31.125 1.00 40.87  ? 397 VAL A O     1 
ATOM   2998 C CB    . VAL A 1 416 ? 18.228  7.786   -32.441 1.00 54.84  ? 397 VAL A CB    1 
ATOM   2999 C CG1   . VAL A 1 416 ? 18.856  8.284   -33.734 1.00 60.23  ? 397 VAL A CG1   1 
ATOM   3000 C CG2   . VAL A 1 416 ? 18.774  8.570   -31.244 1.00 57.67  ? 397 VAL A CG2   1 
ATOM   3001 N N     . PRO A 1 417 ? 14.733  6.352   -32.111 1.00 37.83  ? 398 PRO A N     1 
ATOM   3002 C CA    . PRO A 1 417 ? 14.048  5.215   -31.497 1.00 37.25  ? 398 PRO A CA    1 
ATOM   3003 C C     . PRO A 1 417 ? 14.676  3.910   -31.951 1.00 36.02  ? 398 PRO A C     1 
ATOM   3004 O O     . PRO A 1 417 ? 15.067  3.787   -33.100 1.00 34.45  ? 398 PRO A O     1 
ATOM   3005 C CB    . PRO A 1 417 ? 12.616  5.328   -32.022 1.00 41.90  ? 398 PRO A CB    1 
ATOM   3006 C CG    . PRO A 1 417 ? 12.747  6.189   -33.254 1.00 45.74  ? 398 PRO A CG    1 
ATOM   3007 C CD    . PRO A 1 417 ? 13.832  7.183   -32.909 1.00 39.76  ? 398 PRO A CD    1 
ATOM   3008 N N     . ASP A 1 418 ? 14.703  2.915   -31.059 1.00 32.55  ? 399 ASP A N     1 
ATOM   3009 C CA    . ASP A 1 418 ? 15.194  1.593   -31.386 1.00 29.54  ? 399 ASP A CA    1 
ATOM   3010 C C     . ASP A 1 418 ? 13.984  0.776   -31.853 1.00 29.23  ? 399 ASP A C     1 
ATOM   3011 O O     . ASP A 1 418 ? 13.030  0.585   -31.110 1.00 29.66  ? 399 ASP A O     1 
ATOM   3012 C CB    . ASP A 1 418 ? 15.890  1.001   -30.165 1.00 31.27  ? 399 ASP A CB    1 
ATOM   3013 C CG    . ASP A 1 418 ? 16.402  -0.415  -30.349 1.00 35.12  ? 399 ASP A CG    1 
ATOM   3014 O OD1   . ASP A 1 418 ? 15.888  -1.123  -31.250 1.00 35.76  ? 399 ASP A OD1   1 
ATOM   3015 O OD2   . ASP A 1 418 ? 17.343  -0.790  -29.603 1.00 37.45  ? 399 ASP A OD2   1 
ATOM   3016 N N     . PRO A 1 419 ? 13.962  0.303   -33.104 1.00 32.16  ? 400 PRO A N     1 
ATOM   3017 C CA    . PRO A 1 419 ? 12.786  -0.384  -33.636 1.00 34.02  ? 400 PRO A CA    1 
ATOM   3018 C C     . PRO A 1 419 ? 12.483  -1.728  -32.966 1.00 33.84  ? 400 PRO A C     1 
ATOM   3019 O O     . PRO A 1 419 ? 11.364  -2.222  -33.120 1.00 31.52  ? 400 PRO A O     1 
ATOM   3020 C CB    . PRO A 1 419 ? 13.164  -0.510  -35.121 1.00 37.40  ? 400 PRO A CB    1 
ATOM   3021 C CG    . PRO A 1 419 ? 14.651  -0.731  -35.052 1.00 38.49  ? 400 PRO A CG    1 
ATOM   3022 C CD    . PRO A 1 419 ? 15.085  0.335   -34.070 1.00 37.14  ? 400 PRO A CD    1 
ATOM   3023 N N     . ALA A 1 420 ? 13.428  -2.281  -32.176 1.00 33.27  ? 401 ALA A N     1 
ATOM   3024 C CA    . ALA A 1 420 ? 13.130  -3.476  -31.388 1.00 34.97  ? 401 ALA A CA    1 
ATOM   3025 C C     . ALA A 1 420 ? 12.337  -3.177  -30.105 1.00 30.09  ? 401 ALA A C     1 
ATOM   3026 O O     . ALA A 1 420 ? 11.934  -4.119  -29.409 1.00 29.32  ? 401 ALA A O     1 
ATOM   3027 C CB    . ALA A 1 420 ? 14.389  -4.215  -31.027 1.00 36.84  ? 401 ALA A CB    1 
ATOM   3028 N N     . LEU A 1 421 ? 12.141  -1.895  -29.743 1.00 27.86  ? 402 LEU A N     1 
ATOM   3029 C CA    . LEU A 1 421 ? 11.580  -1.547  -28.449 1.00 24.45  ? 402 LEU A CA    1 
ATOM   3030 C C     . LEU A 1 421 ? 10.222  -0.891  -28.655 1.00 24.78  ? 402 LEU A C     1 
ATOM   3031 O O     . LEU A 1 421 ? 9.874   -0.462  -29.748 1.00 26.45  ? 402 LEU A O     1 
ATOM   3032 C CB    . LEU A 1 421 ? 12.520  -0.600  -27.694 1.00 26.63  ? 402 LEU A CB    1 
ATOM   3033 C CG    . LEU A 1 421 ? 13.965  -1.083  -27.490 1.00 25.78  ? 402 LEU A CG    1 
ATOM   3034 C CD1   . LEU A 1 421 ? 14.710  -0.098  -26.636 1.00 29.52  ? 402 LEU A CD1   1 
ATOM   3035 C CD2   . LEU A 1 421 ? 14.023  -2.468  -26.867 1.00 29.86  ? 402 LEU A CD2   1 
ATOM   3036 N N     . GLY A 1 422 ? 9.482   -0.788  -27.555 1.00 26.18  ? 403 GLY A N     1 
ATOM   3037 C CA    . GLY A 1 422 ? 8.232   -0.043  -27.509 1.00 21.83  ? 403 GLY A CA    1 
ATOM   3038 C C     . GLY A 1 422 ? 7.015   -0.867  -27.896 1.00 21.64  ? 403 GLY A C     1 
ATOM   3039 O O     . GLY A 1 422 ? 5.911   -0.353  -27.786 1.00 24.45  ? 403 GLY A O     1 
ATOM   3040 N N     . GLY A 1 423 ? 7.199   -2.115  -28.334 1.00 22.12  ? 404 GLY A N     1 
ATOM   3041 C CA    . GLY A 1 423 ? 6.069   -2.935  -28.756 1.00 21.15  ? 404 GLY A CA    1 
ATOM   3042 C C     . GLY A 1 423 ? 5.702   -3.886  -27.631 1.00 21.87  ? 404 GLY A C     1 
ATOM   3043 O O     . GLY A 1 423 ? 5.911   -3.555  -26.476 1.00 23.01  ? 404 GLY A O     1 
ATOM   3044 N N     . ARG A 1 424 ? 5.196   -5.072  -27.983 1.00 24.33  ? 405 ARG A N     1 
ATOM   3045 C CA    . ARG A 1 424 ? 4.657   -5.983  -26.993 1.00 23.89  ? 405 ARG A CA    1 
ATOM   3046 C C     . ARG A 1 424 ? 5.254   -7.374  -27.179 1.00 26.34  ? 405 ARG A C     1 
ATOM   3047 O O     . ARG A 1 424 ? 5.885   -7.652  -28.201 1.00 26.47  ? 405 ARG A O     1 
ATOM   3048 C CB    . ARG A 1 424 ? 3.132   -5.995  -27.078 1.00 23.80  ? 405 ARG A CB    1 
ATOM   3049 C CG    . ARG A 1 424 ? 2.523   -4.666  -26.660 1.00 24.97  ? 405 ARG A CG    1 
ATOM   3050 C CD    . ARG A 1 424 ? 1.012   -4.640  -26.816 1.00 25.95  ? 405 ARG A CD    1 
ATOM   3051 N NE    . ARG A 1 424 ? 0.406   -5.520  -25.850 1.00 27.17  ? 405 ARG A NE    1 
ATOM   3052 C CZ    . ARG A 1 424 ? 0.344   -5.287  -24.535 1.00 29.43  ? 405 ARG A CZ    1 
ATOM   3053 N NH1   . ARG A 1 424 ? -0.064  -6.246  -23.728 1.00 34.86  ? 405 ARG A NH1   1 
ATOM   3054 N NH2   . ARG A 1 424 ? 0.689   -4.105  -24.035 1.00 28.10  ? 405 ARG A NH2   1 
ATOM   3055 N N     . VAL A 1 425 ? 5.056   -8.196  -26.143 1.00 27.38  ? 406 VAL A N     1 
ATOM   3056 C CA    . VAL A 1 425 ? 5.378   -9.620  -26.139 1.00 26.40  ? 406 VAL A CA    1 
ATOM   3057 C C     . VAL A 1 425 ? 4.072   -10.344 -25.783 1.00 26.17  ? 406 VAL A C     1 
ATOM   3058 O O     . VAL A 1 425 ? 3.725   -10.533 -24.612 1.00 28.03  ? 406 VAL A O     1 
ATOM   3059 C CB    . VAL A 1 425 ? 6.524   -9.972  -25.169 1.00 27.58  ? 406 VAL A CB    1 
ATOM   3060 C CG1   . VAL A 1 425 ? 6.906   -11.452 -25.225 1.00 27.65  ? 406 VAL A CG1   1 
ATOM   3061 C CG2   . VAL A 1 425 ? 7.766   -9.141  -25.425 1.00 27.56  ? 406 VAL A CG2   1 
ATOM   3062 N N     . PRO A 1 426 ? 3.277   -10.722 -26.796 1.00 28.91  ? 407 PRO A N     1 
ATOM   3063 C CA    . PRO A 1 426 ? 1.927   -11.246 -26.567 1.00 32.68  ? 407 PRO A CA    1 
ATOM   3064 C C     . PRO A 1 426 ? 1.870   -12.499 -25.703 1.00 36.35  ? 407 PRO A C     1 
ATOM   3065 O O     . PRO A 1 426 ? 0.951   -12.658 -24.896 1.00 30.80  ? 407 PRO A O     1 
ATOM   3066 C CB    . PRO A 1 426 ? 1.452   -11.613 -27.976 1.00 36.73  ? 407 PRO A CB    1 
ATOM   3067 C CG    . PRO A 1 426 ? 2.256   -10.739 -28.880 1.00 37.20  ? 407 PRO A CG    1 
ATOM   3068 C CD    . PRO A 1 426 ? 3.604   -10.586 -28.220 1.00 33.90  ? 407 PRO A CD    1 
ATOM   3069 N N     . GLY A 1 427 ? 2.917   -13.326 -25.838 1.00 31.93  ? 408 GLY A N     1 
ATOM   3070 C CA    . GLY A 1 427 ? 3.029   -14.558 -25.069 1.00 31.89  ? 408 GLY A CA    1 
ATOM   3071 C C     . GLY A 1 427 ? 3.216   -14.317 -23.580 1.00 32.81  ? 408 GLY A C     1 
ATOM   3072 O O     . GLY A 1 427 ? 2.993   -15.224 -22.798 1.00 31.65  ? 408 GLY A O     1 
ATOM   3073 N N     . ALA A 1 428 ? 3.609   -13.096 -23.164 1.00 27.28  ? 409 ALA A N     1 
ATOM   3074 C CA    . ALA A 1 428 ? 3.821   -12.779 -21.766 1.00 27.22  ? 409 ALA A CA    1 
ATOM   3075 C C     . ALA A 1 428 ? 2.531   -12.501 -20.980 1.00 25.74  ? 409 ALA A C     1 
ATOM   3076 O O     . ALA A 1 428 ? 2.572   -12.471 -19.753 1.00 27.21  ? 409 ALA A O     1 
ATOM   3077 C CB    . ALA A 1 428 ? 4.768   -11.602 -21.644 1.00 28.49  ? 409 ALA A CB    1 
ATOM   3078 N N     . ALA A 1 429 ? 1.387   -12.342 -21.659 1.00 29.43  ? 410 ALA A N     1 
ATOM   3079 C CA    . ALA A 1 429 ? 0.174   -11.900 -20.992 1.00 28.37  ? 410 ALA A CA    1 
ATOM   3080 C C     . ALA A 1 429 ? -0.133  -12.724 -19.750 1.00 25.95  ? 410 ALA A C     1 
ATOM   3081 O O     . ALA A 1 429 ? -0.410  -12.143 -18.708 1.00 27.75  ? 410 ALA A O     1 
ATOM   3082 C CB    . ALA A 1 429 ? -0.992  -11.859 -21.939 1.00 28.46  ? 410 ALA A CB    1 
ATOM   3083 N N     . PRO A 1 430 ? -0.107  -14.076 -19.773 1.00 29.65  ? 411 PRO A N     1 
ATOM   3084 C CA    . PRO A 1 430 ? -0.433  -14.825 -18.558 1.00 33.99  ? 411 PRO A CA    1 
ATOM   3085 C C     . PRO A 1 430 ? 0.486   -14.552 -17.363 1.00 35.31  ? 411 PRO A C     1 
ATOM   3086 O O     . PRO A 1 430 ? 0.098   -14.801 -16.218 1.00 38.11  ? 411 PRO A O     1 
ATOM   3087 C CB    . PRO A 1 430 ? -0.362  -16.295 -19.024 1.00 35.27  ? 411 PRO A CB    1 
ATOM   3088 C CG    . PRO A 1 430 ? -0.614  -16.225 -20.521 1.00 35.30  ? 411 PRO A CG    1 
ATOM   3089 C CD    . PRO A 1 430 ? 0.112   -14.953 -20.935 1.00 33.92  ? 411 PRO A CD    1 
ATOM   3090 N N     . LEU A 1 431 ? 1.685   -13.998 -17.616 1.00 29.48  ? 412 LEU A N     1 
ATOM   3091 C CA    . LEU A 1 431 ? 2.670   -13.779 -16.577 1.00 29.70  ? 412 LEU A CA    1 
ATOM   3092 C C     . LEU A 1 431 ? 2.454   -12.425 -15.892 1.00 31.16  ? 412 LEU A C     1 
ATOM   3093 O O     . LEU A 1 431 ? 3.105   -12.124 -14.899 1.00 29.47  ? 412 LEU A O     1 
ATOM   3094 C CB    . LEU A 1 431 ? 4.066   -13.821 -17.198 1.00 31.08  ? 412 LEU A CB    1 
ATOM   3095 C CG    . LEU A 1 431 ? 4.442   -15.099 -17.955 1.00 35.43  ? 412 LEU A CG    1 
ATOM   3096 C CD1   . LEU A 1 431 ? 5.845   -14.990 -18.526 1.00 32.82  ? 412 LEU A CD1   1 
ATOM   3097 C CD2   . LEU A 1 431 ? 4.324   -16.335 -17.075 1.00 37.92  ? 412 LEU A CD2   1 
ATOM   3098 N N     . LEU A 1 432 ? 1.528   -11.610 -16.395 1.00 29.74  ? 413 LEU A N     1 
ATOM   3099 C CA    . LEU A 1 432 ? 1.423   -10.231 -15.938 1.00 30.04  ? 413 LEU A CA    1 
ATOM   3100 C C     . LEU A 1 432 ? 0.181   -9.978  -15.093 1.00 29.67  ? 413 LEU A C     1 
ATOM   3101 O O     . LEU A 1 432 ? -0.080  -8.834  -14.746 1.00 26.15  ? 413 LEU A O     1 
ATOM   3102 C CB    . LEU A 1 432 ? 1.411   -9.315  -17.179 1.00 29.58  ? 413 LEU A CB    1 
ATOM   3103 C CG    . LEU A 1 432 ? 2.772   -9.097  -17.849 1.00 29.46  ? 413 LEU A CG    1 
ATOM   3104 C CD1   . LEU A 1 432 ? 2.610   -8.416  -19.191 1.00 31.12  ? 413 LEU A CD1   1 
ATOM   3105 C CD2   . LEU A 1 432 ? 3.716   -8.293  -16.993 1.00 32.59  ? 413 LEU A CD2   1 
ATOM   3106 N N     . HIS A 1 433 ? -0.579  -11.022 -14.735 1.00 27.46  ? 414 HIS A N     1 
ATOM   3107 C CA    . HIS A 1 433 ? -1.861  -10.819 -14.063 1.00 29.51  ? 414 HIS A CA    1 
ATOM   3108 C C     . HIS A 1 433 ? -1.717  -10.062 -12.739 1.00 30.66  ? 414 HIS A C     1 
ATOM   3109 O O     . HIS A 1 433 ? -2.624  -9.365  -12.299 1.00 29.96  ? 414 HIS A O     1 
ATOM   3110 C CB    . HIS A 1 433 ? -2.502  -12.172 -13.763 1.00 30.53  ? 414 HIS A CB    1 
ATOM   3111 C CG    . HIS A 1 433 ? -2.990  -12.914 -14.947 1.00 31.64  ? 414 HIS A CG    1 
ATOM   3112 N ND1   . HIS A 1 433 ? -2.871  -12.587 -16.284 1.00 34.01  ? 414 HIS A ND1   1 
ATOM   3113 C CD2   . HIS A 1 433 ? -3.728  -14.041 -14.895 1.00 30.69  ? 414 HIS A CD2   1 
ATOM   3114 C CE1   . HIS A 1 433 ? -3.476  -13.534 -17.008 1.00 30.16  ? 414 HIS A CE1   1 
ATOM   3115 N NE2   . HIS A 1 433 ? -3.993  -14.426 -16.174 1.00 36.28  ? 414 HIS A NE2   1 
ATOM   3116 N N     . GLY A 1 434 ? -0.566  -10.244 -12.099 1.00 30.11  ? 415 GLY A N     1 
ATOM   3117 C CA    . GLY A 1 434 ? -0.303  -9.674  -10.799 1.00 35.84  ? 415 GLY A CA    1 
ATOM   3118 C C     . GLY A 1 434 ? 0.058   -8.201  -10.891 1.00 32.94  ? 415 GLY A C     1 
ATOM   3119 O O     . GLY A 1 434 ? 0.196   -7.556  -9.867  1.00 34.10  ? 415 GLY A O     1 
ATOM   3120 N N     . GLY A 1 435 ? 0.266   -7.692  -12.107 1.00 31.61  ? 416 GLY A N     1 
ATOM   3121 C CA    . GLY A 1 435 ? 0.789   -6.348  -12.251 1.00 30.44  ? 416 GLY A CA    1 
ATOM   3122 C C     . GLY A 1 435 ? 2.309   -6.302  -12.084 1.00 32.59  ? 416 GLY A C     1 
ATOM   3123 O O     . GLY A 1 435 ? 3.019   -7.309  -11.933 1.00 30.94  ? 416 GLY A O     1 
ATOM   3124 N N     . GLY A 1 436 ? 2.812   -5.076  -12.093 1.00 28.16  ? 417 GLY A N     1 
ATOM   3125 C CA    . GLY A 1 436 ? 4.246   -4.818  -11.973 1.00 29.04  ? 417 GLY A CA    1 
ATOM   3126 C C     . GLY A 1 436 ? 4.979   -4.993  -13.309 1.00 27.57  ? 417 GLY A C     1 
ATOM   3127 O O     . GLY A 1 436 ? 4.437   -5.419  -14.320 1.00 25.14  ? 417 GLY A O     1 
ATOM   3128 N N     . GLY A 1 437 ? 6.250   -4.606  -13.295 1.00 26.68  ? 418 GLY A N     1 
ATOM   3129 C CA    . GLY A 1 437 ? 7.129   -4.828  -14.406 1.00 26.18  ? 418 GLY A CA    1 
ATOM   3130 C C     . GLY A 1 437 ? 7.564   -6.293  -14.444 1.00 27.34  ? 418 GLY A C     1 
ATOM   3131 O O     . GLY A 1 437 ? 7.375   -7.046  -13.489 1.00 25.83  ? 418 GLY A O     1 
ATOM   3132 N N     . LEU A 1 438 ? 8.176   -6.672  -15.558 1.00 23.47  ? 419 LEU A N     1 
ATOM   3133 C CA    . LEU A 1 438 ? 8.577   -8.063  -15.725 1.00 25.57  ? 419 LEU A CA    1 
ATOM   3134 C C     . LEU A 1 438 ? 9.816   -8.117  -16.582 1.00 22.09  ? 419 LEU A C     1 
ATOM   3135 O O     . LEU A 1 438 ? 9.807   -7.638  -17.713 1.00 24.64  ? 419 LEU A O     1 
ATOM   3136 C CB    . LEU A 1 438 ? 7.446   -8.831  -16.412 1.00 26.00  ? 419 LEU A CB    1 
ATOM   3137 C CG    . LEU A 1 438 ? 7.231   -10.308 -16.082 1.00 33.32  ? 419 LEU A CG    1 
ATOM   3138 C CD1   . LEU A 1 438 ? 6.813   -11.067 -17.303 1.00 29.02  ? 419 LEU A CD1   1 
ATOM   3139 C CD2   . LEU A 1 438 ? 8.360   -10.999 -15.338 1.00 32.80  ? 419 LEU A CD2   1 
ATOM   3140 N N     . LEU A 1 439 ? 10.851  -8.765  -16.055 1.00 26.34  ? 420 LEU A N     1 
ATOM   3141 C CA    . LEU A 1 439 ? 12.047  -9.059  -16.798 1.00 24.68  ? 420 LEU A CA    1 
ATOM   3142 C C     . LEU A 1 439 ? 12.001  -10.515 -17.214 1.00 27.38  ? 420 LEU A C     1 
ATOM   3143 O O     . LEU A 1 439 ? 11.972  -11.380 -16.349 1.00 28.08  ? 420 LEU A O     1 
ATOM   3144 C CB    . LEU A 1 439 ? 13.271  -8.785  -15.928 1.00 28.73  ? 420 LEU A CB    1 
ATOM   3145 C CG    . LEU A 1 439 ? 14.581  -9.239  -16.558 1.00 30.57  ? 420 LEU A CG    1 
ATOM   3146 C CD1   . LEU A 1 439 ? 14.863  -8.483  -17.834 1.00 35.11  ? 420 LEU A CD1   1 
ATOM   3147 C CD2   . LEU A 1 439 ? 15.722  -9.056  -15.572 1.00 32.49  ? 420 LEU A CD2   1 
ATOM   3148 N N     . LEU A 1 440 ? 11.932  -10.724 -18.530 1.00 25.34  ? 421 LEU A N     1 
ATOM   3149 C CA    . LEU A 1 440 ? 11.955  -12.038 -19.145 1.00 26.62  ? 421 LEU A CA    1 
ATOM   3150 C C     . LEU A 1 440 ? 13.413  -12.388 -19.383 1.00 28.40  ? 421 LEU A C     1 
ATOM   3151 O O     . LEU A 1 440 ? 14.114  -11.606 -20.004 1.00 29.21  ? 421 LEU A O     1 
ATOM   3152 C CB    . LEU A 1 440 ? 11.185  -12.047 -20.462 1.00 27.57  ? 421 LEU A CB    1 
ATOM   3153 C CG    . LEU A 1 440 ? 9.685   -11.792 -20.326 1.00 32.42  ? 421 LEU A CG    1 
ATOM   3154 C CD1   . LEU A 1 440 ? 9.008   -11.711 -21.665 1.00 31.64  ? 421 LEU A CD1   1 
ATOM   3155 C CD2   . LEU A 1 440 ? 9.049   -12.886 -19.512 1.00 33.04  ? 421 LEU A CD2   1 
ATOM   3156 N N     . LEU A 1 441 ? 13.829  -13.553 -18.883 1.00 27.78  ? 422 LEU A N     1 
ATOM   3157 C CA    . LEU A 1 441 ? 15.238  -13.947 -18.894 1.00 30.92  ? 422 LEU A CA    1 
ATOM   3158 C C     . LEU A 1 441 ? 15.426  -15.024 -19.939 1.00 27.23  ? 422 LEU A C     1 
ATOM   3159 O O     . LEU A 1 441 ? 14.703  -16.038 -19.899 1.00 32.70  ? 422 LEU A O     1 
ATOM   3160 C CB    . LEU A 1 441 ? 15.643  -14.514 -17.535 1.00 33.35  ? 422 LEU A CB    1 
ATOM   3161 C CG    . LEU A 1 441 ? 15.669  -13.541 -16.364 1.00 37.66  ? 422 LEU A CG    1 
ATOM   3162 C CD1   . LEU A 1 441 ? 16.103  -14.299 -15.110 1.00 48.16  ? 422 LEU A CD1   1 
ATOM   3163 C CD2   . LEU A 1 441 ? 16.609  -12.386 -16.640 1.00 39.40  ? 422 LEU A CD2   1 
ATOM   3164 N N     . GLY A 1 442 ? 16.322  -14.745 -20.896 1.00 29.46  ? 423 GLY A N     1 
ATOM   3165 C CA    . GLY A 1 442 ? 16.711  -15.705 -21.921 1.00 31.30  ? 423 GLY A CA    1 
ATOM   3166 C C     . GLY A 1 442 ? 18.229  -15.909 -21.954 1.00 32.70  ? 423 GLY A C     1 
ATOM   3167 O O     . GLY A 1 442 ? 18.987  -15.058 -21.517 1.00 29.94  ? 423 GLY A O     1 
ATOM   3168 N N     . ALA A 1 443 ? 18.668  -17.054 -22.487 1.00 31.58  ? 424 ALA A N     1 
ATOM   3169 C CA    . ALA A 1 443 ? 20.083  -17.383 -22.566 1.00 32.84  ? 424 ALA A CA    1 
ATOM   3170 C C     . ALA A 1 443 ? 20.784  -16.697 -23.736 1.00 36.38  ? 424 ALA A C     1 
ATOM   3171 O O     . ALA A 1 443 ? 22.004  -16.718 -23.807 1.00 40.93  ? 424 ALA A O     1 
ATOM   3172 C CB    . ALA A 1 443 ? 20.231  -18.885 -22.657 1.00 33.37  ? 424 ALA A CB    1 
ATOM   3173 N N     . ALA A 1 444 ? 20.040  -16.120 -24.681 1.00 37.30  ? 425 ALA A N     1 
ATOM   3174 C CA    . ALA A 1 444 ? 20.660  -15.512 -25.858 1.00 43.04  ? 425 ALA A CA    1 
ATOM   3175 C C     . ALA A 1 444 ? 21.615  -14.399 -25.431 1.00 46.67  ? 425 ALA A C     1 
ATOM   3176 O O     . ALA A 1 444 ? 21.286  -13.626 -24.532 1.00 45.18  ? 425 ALA A O     1 
ATOM   3177 C CB    . ALA A 1 444 ? 19.595  -14.978 -26.785 1.00 44.28  ? 425 ALA A CB    1 
ATOM   3178 N N     . ASP A 1 445 ? 22.784  -14.312 -26.085 1.00 52.74  ? 426 ASP A N     1 
ATOM   3179 C CA    . ASP A 1 445 ? 23.875  -13.456 -25.627 1.00 64.81  ? 426 ASP A CA    1 
ATOM   3180 C C     . ASP A 1 445 ? 23.940  -12.170 -26.466 1.00 66.77  ? 426 ASP A C     1 
ATOM   3181 O O     . ASP A 1 445 ? 23.390  -12.186 -27.586 1.00 61.74  ? 426 ASP A O     1 
ATOM   3182 C CB    . ASP A 1 445 ? 25.221  -14.195 -25.640 1.00 74.58  ? 426 ASP A CB    1 
ATOM   3183 C CG    . ASP A 1 445 ? 25.694  -14.673 -27.008 1.00 85.17  ? 426 ASP A CG    1 
ATOM   3184 O OD1   . ASP A 1 445 ? 25.202  -15.725 -27.474 1.00 84.08  ? 426 ASP A OD1   1 
ATOM   3185 O OD2   . ASP A 1 445 ? 26.559  -13.992 -27.605 1.00 95.43  ? 426 ASP A OD2   1 
ATOM   3186 N N     . GLY A 1 454 ? 23.193  -15.336 -15.377 1.00 75.79  ? 435 GLY A N     1 
ATOM   3187 C CA    . GLY A 1 454 ? 23.864  -14.615 -14.274 1.00 73.74  ? 435 GLY A CA    1 
ATOM   3188 C C     . GLY A 1 454 ? 23.420  -13.156 -14.144 1.00 68.25  ? 435 GLY A C     1 
ATOM   3189 O O     . GLY A 1 454 ? 22.556  -12.833 -13.329 1.00 71.16  ? 435 GLY A O     1 
ATOM   3190 N N     . ALA A 1 455 ? 24.011  -12.285 -14.974 1.00 58.94  ? 436 ALA A N     1 
ATOM   3191 C CA    . ALA A 1 455 ? 24.122  -10.866 -14.676 1.00 56.19  ? 436 ALA A CA    1 
ATOM   3192 C C     . ALA A 1 455 ? 22.781  -10.127 -14.756 1.00 53.06  ? 436 ALA A C     1 
ATOM   3193 O O     . ALA A 1 455 ? 22.648  -9.082  -14.125 1.00 49.16  ? 436 ALA A O     1 
ATOM   3194 C CB    . ALA A 1 455 ? 25.126  -10.234 -15.603 1.00 52.59  ? 436 ALA A CB    1 
ATOM   3195 N N     . HIS A 1 456 ? 21.816  -10.597 -15.561 1.00 50.56  ? 437 HIS A N     1 
ATOM   3196 C CA    . HIS A 1 456 ? 20.608  -9.797  -15.766 1.00 49.60  ? 437 HIS A CA    1 
ATOM   3197 C C     . HIS A 1 456 ? 19.757  -9.838  -14.499 1.00 42.96  ? 437 HIS A C     1 
ATOM   3198 O O     . HIS A 1 456 ? 19.334  -8.794  -13.998 1.00 39.73  ? 437 HIS A O     1 
ATOM   3199 C CB    . HIS A 1 456 ? 19.805  -10.216 -17.003 1.00 45.97  ? 437 HIS A CB    1 
ATOM   3200 C CG    . HIS A 1 456 ? 20.424  -9.791  -18.299 1.00 45.73  ? 437 HIS A CG    1 
ATOM   3201 N ND1   . HIS A 1 456 ? 21.182  -8.646  -18.456 1.00 43.15  ? 437 HIS A ND1   1 
ATOM   3202 C CD2   . HIS A 1 456 ? 20.385  -10.389 -19.492 1.00 41.80  ? 437 HIS A CD2   1 
ATOM   3203 C CE1   . HIS A 1 456 ? 21.602  -8.573  -19.705 1.00 43.35  ? 437 HIS A CE1   1 
ATOM   3204 N NE2   . HIS A 1 456 ? 21.125  -9.620  -20.350 1.00 42.67  ? 437 HIS A NE2   1 
ATOM   3205 N N     . ALA A 1 457 ? 19.529  -11.060 -13.999 1.00 46.17  ? 438 ALA A N     1 
ATOM   3206 C CA    . ALA A 1 457 ? 18.827  -11.280 -12.741 1.00 46.94  ? 438 ALA A CA    1 
ATOM   3207 C C     . ALA A 1 457 ? 19.463  -10.451 -11.633 1.00 51.39  ? 438 ALA A C     1 
ATOM   3208 O O     . ALA A 1 457 ? 18.750  -9.822  -10.852 1.00 48.28  ? 438 ALA A O     1 
ATOM   3209 C CB    . ALA A 1 457 ? 18.817  -12.752 -12.402 1.00 50.17  ? 438 ALA A CB    1 
ATOM   3210 N N     . ARG A 1 458 ? 20.807  -10.434 -11.597 1.00 51.51  ? 439 ARG A N     1 
ATOM   3211 C CA    . ARG A 1 458 ? 21.546  -9.721  -10.563 1.00 49.77  ? 439 ARG A CA    1 
ATOM   3212 C C     . ARG A 1 458 ? 21.256  -8.225  -10.623 1.00 46.24  ? 439 ARG A C     1 
ATOM   3213 O O     . ARG A 1 458 ? 20.948  -7.625  -9.607  1.00 50.88  ? 439 ARG A O     1 
ATOM   3214 C CB    . ARG A 1 458 ? 23.052  -9.983  -10.689 1.00 56.09  ? 439 ARG A CB    1 
ATOM   3215 C CG    . ARG A 1 458 ? 23.845  -9.629  -9.436  1.00 65.48  ? 439 ARG A CG    1 
ATOM   3216 C CD    . ARG A 1 458 ? 25.281  -10.136 -9.463  1.00 71.26  ? 439 ARG A CD    1 
ATOM   3217 N NE    . ARG A 1 458 ? 25.370  -11.469 -10.058 1.00 73.33  ? 439 ARG A NE    1 
ATOM   3218 C CZ    . ARG A 1 458 ? 26.028  -11.756 -11.177 1.00 70.06  ? 439 ARG A CZ    1 
ATOM   3219 N NH1   . ARG A 1 458 ? 25.815  -12.899 -11.807 1.00 73.89  ? 439 ARG A NH1   1 
ATOM   3220 N NH2   . ARG A 1 458 ? 26.841  -10.859 -11.706 1.00 77.54  ? 439 ARG A NH2   1 
ATOM   3221 N N     . THR A 1 459 ? 21.380  -7.622  -11.812 1.00 43.10  ? 440 THR A N     1 
ATOM   3222 C CA    . THR A 1 459 ? 21.058  -6.216  -12.050 1.00 43.05  ? 440 THR A CA    1 
ATOM   3223 C C     . THR A 1 459 ? 19.626  -5.875  -11.605 1.00 39.25  ? 440 THR A C     1 
ATOM   3224 O O     . THR A 1 459 ? 19.373  -4.838  -11.004 1.00 40.86  ? 440 THR A O     1 
ATOM   3225 C CB    . THR A 1 459 ? 21.195  -5.925  -13.555 1.00 44.11  ? 440 THR A CB    1 
ATOM   3226 O OG1   . THR A 1 459 ? 22.413  -6.517  -14.008 1.00 48.38  ? 440 THR A OG1   1 
ATOM   3227 C CG2   . THR A 1 459 ? 21.170  -4.452  -13.900 1.00 45.99  ? 440 THR A CG2   1 
ATOM   3228 N N     . ALA A 1 460 ? 18.677  -6.741  -11.977 1.00 40.35  ? 441 ALA A N     1 
ATOM   3229 C CA    . ALA A 1 460 ? 17.258  -6.498  -11.786 1.00 41.14  ? 441 ALA A CA    1 
ATOM   3230 C C     . ALA A 1 460 ? 16.868  -6.619  -10.313 1.00 40.13  ? 441 ALA A C     1 
ATOM   3231 O O     . ALA A 1 460 ? 15.828  -6.110  -9.926  1.00 35.06  ? 441 ALA A O     1 
ATOM   3232 C CB    . ALA A 1 460 ? 16.443  -7.464  -12.611 1.00 41.81  ? 441 ALA A CB    1 
ATOM   3233 N N     . ALA A 1 461 ? 17.688  -7.305  -9.511  1.00 40.44  ? 442 ALA A N     1 
ATOM   3234 C CA    . ALA A 1 461 ? 17.409  -7.518  -8.090  1.00 40.64  ? 442 ALA A CA    1 
ATOM   3235 C C     . ALA A 1 461 ? 17.193  -6.206  -7.337  1.00 37.73  ? 442 ALA A C     1 
ATOM   3236 O O     . ALA A 1 461 ? 16.324  -6.118  -6.464  1.00 38.85  ? 442 ALA A O     1 
ATOM   3237 C CB    . ALA A 1 461 ? 18.532  -8.321  -7.471  1.00 44.29  ? 442 ALA A CB    1 
ATOM   3238 N N     . ALA A 1 462 ? 17.951  -5.169  -7.687  1.00 35.95  ? 443 ALA A N     1 
ATOM   3239 C CA    . ALA A 1 462 ? 17.809  -3.881  -7.049  1.00 35.46  ? 443 ALA A CA    1 
ATOM   3240 C C     . ALA A 1 462 ? 16.441  -3.250  -7.326  1.00 38.66  ? 443 ALA A C     1 
ATOM   3241 O O     . ALA A 1 462 ? 16.088  -2.252  -6.711  1.00 33.87  ? 443 ALA A O     1 
ATOM   3242 C CB    . ALA A 1 462 ? 18.936  -2.993  -7.499  1.00 43.63  ? 443 ALA A CB    1 
ATOM   3243 N N     . TRP A 1 463 ? 15.668  -3.798  -8.271  1.00 35.00  ? 444 TRP A N     1 
ATOM   3244 C CA    . TRP A 1 463 ? 14.336  -3.272  -8.563  1.00 32.15  ? 444 TRP A CA    1 
ATOM   3245 C C     . TRP A 1 463 ? 13.290  -4.353  -8.315  1.00 32.59  ? 444 TRP A C     1 
ATOM   3246 O O     . TRP A 1 463 ? 12.169  -4.209  -8.812  1.00 28.63  ? 444 TRP A O     1 
ATOM   3247 C CB    . TRP A 1 463 ? 14.269  -2.772  -10.024 1.00 29.29  ? 444 TRP A CB    1 
ATOM   3248 C CG    . TRP A 1 463 ? 14.998  -1.491  -10.283 1.00 27.72  ? 444 TRP A CG    1 
ATOM   3249 C CD1   . TRP A 1 463 ? 14.447  -0.248  -10.330 1.00 31.45  ? 444 TRP A CD1   1 
ATOM   3250 C CD2   . TRP A 1 463 ? 16.388  -1.320  -10.599 1.00 28.65  ? 444 TRP A CD2   1 
ATOM   3251 N NE1   . TRP A 1 463 ? 15.402  0.680   -10.639 1.00 31.63  ? 444 TRP A NE1   1 
ATOM   3252 C CE2   . TRP A 1 463 ? 16.597  0.049   -10.812 1.00 30.57  ? 444 TRP A CE2   1 
ATOM   3253 C CE3   . TRP A 1 463 ? 17.470  -2.199  -10.772 1.00 32.91  ? 444 TRP A CE3   1 
ATOM   3254 C CZ2   . TRP A 1 463 ? 17.846  0.576   -11.124 1.00 35.19  ? 444 TRP A CZ2   1 
ATOM   3255 C CZ3   . TRP A 1 463 ? 18.707  -1.678  -11.086 1.00 36.05  ? 444 TRP A CZ3   1 
ATOM   3256 C CH2   . TRP A 1 463 ? 18.889  -0.309  -11.249 1.00 35.67  ? 444 TRP A CH2   1 
ATOM   3257 N N     . ALA A 1 464 ? 13.632  -5.372  -7.501  1.00 31.40  ? 445 ALA A N     1 
ATOM   3258 C CA    . ALA A 1 464 ? 12.728  -6.509  -7.268  1.00 32.58  ? 445 ALA A CA    1 
ATOM   3259 C C     . ALA A 1 464 ? 11.414  -6.075  -6.616  1.00 30.60  ? 445 ALA A C     1 
ATOM   3260 O O     . ALA A 1 464 ? 10.425  -6.813  -6.642  1.00 31.09  ? 445 ALA A O     1 
ATOM   3261 C CB    . ALA A 1 464 ? 13.407  -7.572  -6.450  1.00 35.67  ? 445 ALA A CB    1 
ATOM   3262 N N     . ASP A 1 465 ? 11.360  -4.875  -6.025  1.00 27.32  ? 446 ASP A N     1 
ATOM   3263 C CA    . ASP A 1 465 ? 10.119  -4.388  -5.443  1.00 28.59  ? 446 ASP A CA    1 
ATOM   3264 C C     . ASP A 1 465 ? 9.146   -3.866  -6.507  1.00 29.92  ? 446 ASP A C     1 
ATOM   3265 O O     . ASP A 1 465 ? 7.984   -3.632  -6.194  1.00 28.29  ? 446 ASP A O     1 
ATOM   3266 C CB    . ASP A 1 465 ? 10.392  -3.307  -4.387  1.00 33.21  ? 446 ASP A CB    1 
ATOM   3267 C CG    . ASP A 1 465 ? 11.208  -2.116  -4.861  1.00 37.23  ? 446 ASP A CG    1 
ATOM   3268 O OD1   . ASP A 1 465 ? 11.888  -2.230  -5.909  1.00 35.91  ? 446 ASP A OD1   1 
ATOM   3269 O OD2   . ASP A 1 465 ? 11.138  -1.061  -4.190  1.00 42.16  ? 446 ASP A OD2   1 
ATOM   3270 N N     . ARG A 1 466 ? 9.613   -3.680  -7.753  1.00 29.71  ? 447 ARG A N     1 
ATOM   3271 C CA    . ARG A 1 466 ? 8.820   -3.125  -8.836  1.00 27.88  ? 447 ARG A CA    1 
ATOM   3272 C C     . ARG A 1 466 ? 8.798   -4.038  -10.074 1.00 26.26  ? 447 ARG A C     1 
ATOM   3273 O O     . ARG A 1 466 ? 7.894   -3.895  -10.909 1.00 27.42  ? 447 ARG A O     1 
ATOM   3274 C CB    . ARG A 1 466 ? 9.384   -1.750  -9.202  1.00 27.77  ? 447 ARG A CB    1 
ATOM   3275 C CG    . ARG A 1 466 ? 9.043   -0.632  -8.228  1.00 29.41  ? 447 ARG A CG    1 
ATOM   3276 C CD    . ARG A 1 466 ? 10.074  0.497   -8.240  1.00 30.91  ? 447 ARG A CD    1 
ATOM   3277 N NE    . ARG A 1 466 ? 11.309  0.026   -7.646  1.00 31.04  ? 447 ARG A NE    1 
ATOM   3278 C CZ    . ARG A 1 466 ? 12.402  0.758   -7.438  1.00 35.08  ? 447 ARG A CZ    1 
ATOM   3279 N NH1   . ARG A 1 466 ? 13.395  0.254   -6.727  1.00 38.12  ? 447 ARG A NH1   1 
ATOM   3280 N NH2   . ARG A 1 466 ? 12.507  1.981   -7.917  1.00 32.34  ? 447 ARG A NH2   1 
ATOM   3281 N N     . VAL A 1 467 ? 9.774   -4.956  -10.209 1.00 25.23  ? 448 VAL A N     1 
ATOM   3282 C CA    . VAL A 1 467 ? 9.962   -5.761  -11.404 1.00 27.51  ? 448 VAL A CA    1 
ATOM   3283 C C     . VAL A 1 467 ? 10.104  -7.228  -11.007 1.00 29.67  ? 448 VAL A C     1 
ATOM   3284 O O     . VAL A 1 467 ? 11.020  -7.551  -10.272 1.00 28.92  ? 448 VAL A O     1 
ATOM   3285 C CB    . VAL A 1 467 ? 11.226  -5.266  -12.126 1.00 28.08  ? 448 VAL A CB    1 
ATOM   3286 C CG1   . VAL A 1 467 ? 11.571  -6.104  -13.342 1.00 31.55  ? 448 VAL A CG1   1 
ATOM   3287 C CG2   . VAL A 1 467 ? 11.096  -3.793  -12.467 1.00 28.50  ? 448 VAL A CG2   1 
ATOM   3288 N N     . GLY A 1 468 ? 9.194   -8.095  -11.451 1.00 26.80  ? 449 GLY A N     1 
ATOM   3289 C CA    . GLY A 1 468 ? 9.368   -9.533  -11.304 1.00 26.73  ? 449 GLY A CA    1 
ATOM   3290 C C     . GLY A 1 468 ? 10.246  -10.147 -12.388 1.00 27.93  ? 449 GLY A C     1 
ATOM   3291 O O     . GLY A 1 468 ? 10.603  -9.497  -13.355 1.00 26.15  ? 449 GLY A O     1 
ATOM   3292 N N     . VAL A 1 469 ? 10.498  -11.466 -12.283 1.00 27.39  ? 450 VAL A N     1 
ATOM   3293 C CA    . VAL A 1 469 ? 11.310  -12.175 -13.231 1.00 26.71  ? 450 VAL A CA    1 
ATOM   3294 C C     . VAL A 1 469 ? 10.567  -13.442 -13.650 1.00 31.41  ? 450 VAL A C     1 
ATOM   3295 O O     . VAL A 1 469 ? 9.893   -14.082 -12.835 1.00 36.78  ? 450 VAL A O     1 
ATOM   3296 C CB    . VAL A 1 469 ? 12.693  -12.494 -12.634 1.00 32.81  ? 450 VAL A CB    1 
ATOM   3297 C CG1   . VAL A 1 469 ? 13.411  -13.546 -13.434 1.00 44.22  ? 450 VAL A CG1   1 
ATOM   3298 C CG2   . VAL A 1 469 ? 13.579  -11.264 -12.523 1.00 35.53  ? 450 VAL A CG2   1 
ATOM   3299 N N     . ALA A 1 470 ? 10.707  -13.779 -14.930 1.00 28.52  ? 451 ALA A N     1 
ATOM   3300 C CA    . ALA A 1 470 ? 10.244  -15.042 -15.480 1.00 29.22  ? 451 ALA A CA    1 
ATOM   3301 C C     . ALA A 1 470 ? 11.142  -15.425 -16.648 1.00 33.53  ? 451 ALA A C     1 
ATOM   3302 O O     . ALA A 1 470 ? 11.905  -14.598 -17.179 1.00 29.07  ? 451 ALA A O     1 
ATOM   3303 C CB    . ALA A 1 470 ? 8.794   -14.980 -15.891 1.00 30.98  ? 451 ALA A CB    1 
ATOM   3304 N N     . PRO A 1 471 ? 11.103  -16.705 -17.080 1.00 31.25  ? 452 PRO A N     1 
ATOM   3305 C CA    . PRO A 1 471 ? 11.895  -17.143 -18.231 1.00 30.73  ? 452 PRO A CA    1 
ATOM   3306 C C     . PRO A 1 471 ? 11.259  -16.629 -19.517 1.00 28.95  ? 452 PRO A C     1 
ATOM   3307 O O     . PRO A 1 471 ? 10.048  -16.805 -19.728 1.00 28.67  ? 452 PRO A O     1 
ATOM   3308 C CB    . PRO A 1 471 ? 11.804  -18.680 -18.212 1.00 33.21  ? 452 PRO A CB    1 
ATOM   3309 C CG    . PRO A 1 471 ? 11.070  -19.023 -16.945 1.00 34.01  ? 452 PRO A CG    1 
ATOM   3310 C CD    . PRO A 1 471 ? 10.279  -17.788 -16.530 1.00 35.25  ? 452 PRO A CD    1 
ATOM   3311 N N     . ALA A 1 472 ? 12.085  -16.090 -20.424 1.00 27.62  ? 453 ALA A N     1 
ATOM   3312 C CA    . ALA A 1 472 ? 11.635  -15.705 -21.751 1.00 31.86  ? 453 ALA A CA    1 
ATOM   3313 C C     . ALA A 1 472 ? 10.909  -16.862 -22.437 1.00 32.68  ? 453 ALA A C     1 
ATOM   3314 O O     . ALA A 1 472 ? 9.925   -16.645 -23.135 1.00 30.30  ? 453 ALA A O     1 
ATOM   3315 C CB    . ALA A 1 472 ? 12.795  -15.200 -22.564 1.00 32.51  ? 453 ALA A CB    1 
ATOM   3316 N N     . LEU A 1 473 ? 11.350  -18.111 -22.212 1.00 29.61  ? 454 LEU A N     1 
ATOM   3317 C CA    . LEU A 1 473 ? 10.720  -19.224 -22.895 1.00 29.92  ? 454 LEU A CA    1 
ATOM   3318 C C     . LEU A 1 473 ? 9.275   -19.457 -22.427 1.00 30.92  ? 454 LEU A C     1 
ATOM   3319 O O     . LEU A 1 473 ? 8.527   -20.137 -23.129 1.00 32.98  ? 454 LEU A O     1 
ATOM   3320 C CB    . LEU A 1 473 ? 11.569  -20.501 -22.753 1.00 32.74  ? 454 LEU A CB    1 
ATOM   3321 C CG    . LEU A 1 473 ? 11.573  -21.167 -21.377 1.00 34.88  ? 454 LEU A CG    1 
ATOM   3322 C CD1   . LEU A 1 473 ? 10.400  -22.131 -21.213 1.00 38.97  ? 454 LEU A CD1   1 
ATOM   3323 C CD2   . LEU A 1 473 ? 12.887  -21.907 -21.133 1.00 34.95  ? 454 LEU A CD2   1 
ATOM   3324 N N     . ALA A 1 474 ? 8.898   -18.973 -21.243 1.00 29.59  ? 455 ALA A N     1 
ATOM   3325 C CA    . ALA A 1 474 ? 7.527   -19.109 -20.764 1.00 31.18  ? 455 ALA A CA    1 
ATOM   3326 C C     . ALA A 1 474 ? 6.613   -18.080 -21.437 1.00 34.59  ? 455 ALA A C     1 
ATOM   3327 O O     . ALA A 1 474 ? 5.404   -18.140 -21.224 1.00 34.09  ? 455 ALA A O     1 
ATOM   3328 C CB    . ALA A 1 474 ? 7.481   -18.995 -19.262 1.00 33.34  ? 455 ALA A CB    1 
ATOM   3329 N N     . ALA A 1 475 ? 7.190   -17.158 -22.224 1.00 31.16  ? 456 ALA A N     1 
ATOM   3330 C CA    . ALA A 1 475 ? 6.458   -16.116 -22.929 1.00 35.25  ? 456 ALA A CA    1 
ATOM   3331 C C     . ALA A 1 475 ? 6.608   -16.212 -24.444 1.00 37.61  ? 456 ALA A C     1 
ATOM   3332 O O     . ALA A 1 475 ? 6.176   -15.306 -25.159 1.00 33.61  ? 456 ALA A O     1 
ATOM   3333 C CB    . ALA A 1 475 ? 6.959   -14.772 -22.461 1.00 34.88  ? 456 ALA A CB    1 
ATOM   3334 N N     . ASP A 1 476 ? 7.277   -17.273 -24.922 1.00 40.70  ? 457 ASP A N     1 
ATOM   3335 C CA    . ASP A 1 476 ? 7.670   -17.415 -26.316 1.00 41.22  ? 457 ASP A CA    1 
ATOM   3336 C C     . ASP A 1 476 ? 8.510   -16.229 -26.788 1.00 37.39  ? 457 ASP A C     1 
ATOM   3337 O O     . ASP A 1 476 ? 8.399   -15.806 -27.936 1.00 38.06  ? 457 ASP A O     1 
ATOM   3338 C CB    . ASP A 1 476 ? 6.456   -17.655 -27.222 1.00 46.74  ? 457 ASP A CB    1 
ATOM   3339 C CG    . ASP A 1 476 ? 6.303   -19.122 -27.592 1.00 67.10  ? 457 ASP A CG    1 
ATOM   3340 O OD1   . ASP A 1 476 ? 7.193   -19.636 -28.311 1.00 76.01  ? 457 ASP A OD1   1 
ATOM   3341 O OD2   . ASP A 1 476 ? 5.322   -19.754 -27.132 1.00 74.87  ? 457 ASP A OD2   1 
ATOM   3342 N N     . ALA A 1 477 ? 9.371   -15.704 -25.918 1.00 36.31  ? 458 ALA A N     1 
ATOM   3343 C CA    . ALA A 1 477 ? 10.374  -14.736 -26.349 1.00 33.77  ? 458 ALA A CA    1 
ATOM   3344 C C     . ALA A 1 477 ? 11.719  -15.457 -26.472 1.00 38.15  ? 458 ALA A C     1 
ATOM   3345 O O     . ALA A 1 477 ? 11.934  -16.441 -25.778 1.00 35.36  ? 458 ALA A O     1 
ATOM   3346 C CB    . ALA A 1 477 ? 10.445  -13.602 -25.375 1.00 31.11  ? 458 ALA A CB    1 
ATOM   3347 N N     . THR A 1 478 ? 12.609  -14.950 -27.329 1.00 36.03  ? 459 THR A N     1 
ATOM   3348 C CA    . THR A 1 478 ? 13.834  -15.675 -27.676 1.00 39.17  ? 459 THR A CA    1 
ATOM   3349 C C     . THR A 1 478 ? 15.075  -14.911 -27.226 1.00 37.70  ? 459 THR A C     1 
ATOM   3350 O O     . THR A 1 478 ? 16.194  -15.311 -27.554 1.00 34.76  ? 459 THR A O     1 
ATOM   3351 C CB    . THR A 1 478 ? 13.870  -15.989 -29.175 1.00 39.92  ? 459 THR A CB    1 
ATOM   3352 O OG1   . THR A 1 478 ? 13.859  -14.746 -29.874 1.00 39.72  ? 459 THR A OG1   1 
ATOM   3353 C CG2   . THR A 1 478 ? 12.697  -16.849 -29.598 1.00 39.04  ? 459 THR A CG2   1 
ATOM   3354 N N     . ARG A 1 479 ? 14.859  -13.843 -26.454 1.00 31.42  ? 460 ARG A N     1 
ATOM   3355 C CA    . ARG A 1 479 ? 15.932  -13.160 -25.756 1.00 35.26  ? 460 ARG A CA    1 
ATOM   3356 C C     . ARG A 1 479 ? 15.355  -12.433 -24.538 1.00 33.00  ? 460 ARG A C     1 
ATOM   3357 O O     . ARG A 1 479 ? 14.122  -12.356 -24.375 1.00 31.85  ? 460 ARG A O     1 
ATOM   3358 C CB    . ARG A 1 479 ? 16.630  -12.179 -26.700 1.00 36.72  ? 460 ARG A CB    1 
ATOM   3359 C CG    . ARG A 1 479 ? 15.794  -10.949 -27.033 1.00 37.62  ? 460 ARG A CG    1 
ATOM   3360 C CD    . ARG A 1 479 ? 16.481  -9.937  -27.940 1.00 46.22  ? 460 ARG A CD    1 
ATOM   3361 N NE    . ARG A 1 479 ? 16.711  -10.451 -29.283 1.00 56.27  ? 460 ARG A NE    1 
ATOM   3362 C CZ    . ARG A 1 479 ? 17.792  -10.213 -30.034 1.00 65.72  ? 460 ARG A CZ    1 
ATOM   3363 N NH1   . ARG A 1 479 ? 17.960  -10.862 -31.173 1.00 65.34  ? 460 ARG A NH1   1 
ATOM   3364 N NH2   . ARG A 1 479 ? 18.722  -9.356  -29.643 1.00 62.32  ? 460 ARG A NH2   1 
ATOM   3365 N N     . SER A 1 480 ? 16.265  -11.926 -23.690 1.00 29.60  ? 461 SER A N     1 
ATOM   3366 C CA    . SER A 1 480 ? 15.902  -11.173 -22.501 1.00 29.85  ? 461 SER A CA    1 
ATOM   3367 C C     . SER A 1 480 ? 15.204  -9.873  -22.921 1.00 29.17  ? 461 SER A C     1 
ATOM   3368 O O     . SER A 1 480 ? 15.657  -9.169  -23.825 1.00 28.63  ? 461 SER A O     1 
ATOM   3369 C CB    . SER A 1 480 ? 17.095  -10.894 -21.628 1.00 29.22  ? 461 SER A CB    1 
ATOM   3370 O OG    . SER A 1 480 ? 17.596  -12.113 -21.064 1.00 30.85  ? 461 SER A OG    1 
ATOM   3371 N N     . VAL A 1 481 ? 14.094  -9.572  -22.244 1.00 27.56  ? 462 VAL A N     1 
ATOM   3372 C CA    . VAL A 1 481 ? 13.309  -8.369  -22.516 1.00 28.46  ? 462 VAL A CA    1 
ATOM   3373 C C     . VAL A 1 481 ? 12.766  -7.823  -21.195 1.00 27.38  ? 462 VAL A C     1 
ATOM   3374 O O     . VAL A 1 481 ? 12.366  -8.596  -20.331 1.00 26.62  ? 462 VAL A O     1 
ATOM   3375 C CB    . VAL A 1 481 ? 12.180  -8.695  -23.507 1.00 32.78  ? 462 VAL A CB    1 
ATOM   3376 C CG1   . VAL A 1 481 ? 11.472  -9.937  -23.082 1.00 42.52  ? 462 VAL A CG1   1 
ATOM   3377 C CG2   . VAL A 1 481 ? 11.164  -7.579  -23.701 1.00 32.79  ? 462 VAL A CG2   1 
ATOM   3378 N N     . LEU A 1 482 ? 12.682  -6.486  -21.065 1.00 27.20  ? 463 LEU A N     1 
ATOM   3379 C CA    . LEU A 1 482 ? 12.074  -5.851  -19.917 1.00 23.80  ? 463 LEU A CA    1 
ATOM   3380 C C     . LEU A 1 482 ? 10.736  -5.232  -20.327 1.00 25.01  ? 463 LEU A C     1 
ATOM   3381 O O     . LEU A 1 482 ? 10.666  -4.414  -21.263 1.00 25.46  ? 463 LEU A O     1 
ATOM   3382 C CB    . LEU A 1 482 ? 13.008  -4.740  -19.410 1.00 24.67  ? 463 LEU A CB    1 
ATOM   3383 C CG    . LEU A 1 482 ? 12.458  -3.885  -18.261 1.00 27.73  ? 463 LEU A CG    1 
ATOM   3384 C CD1   . LEU A 1 482 ? 12.319  -4.683  -16.985 1.00 28.94  ? 463 LEU A CD1   1 
ATOM   3385 C CD2   . LEU A 1 482 ? 13.370  -2.696  -17.993 1.00 28.34  ? 463 LEU A CD2   1 
ATOM   3386 N N     . LEU A 1 483 ? 9.683   -5.671  -19.641 1.00 24.43  ? 464 LEU A N     1 
ATOM   3387 C CA    . LEU A 1 483 ? 8.342   -5.156  -19.861 1.00 22.71  ? 464 LEU A CA    1 
ATOM   3388 C C     . LEU A 1 483 ? 7.968   -4.179  -18.767 1.00 23.10  ? 464 LEU A C     1 
ATOM   3389 O O     . LEU A 1 483 ? 8.106   -4.440  -17.578 1.00 23.54  ? 464 LEU A O     1 
ATOM   3390 C CB    . LEU A 1 483 ? 7.369   -6.328  -19.848 1.00 22.41  ? 464 LEU A CB    1 
ATOM   3391 C CG    . LEU A 1 483 ? 7.563   -7.384  -20.936 1.00 27.41  ? 464 LEU A CG    1 
ATOM   3392 C CD1   . LEU A 1 483 ? 6.445   -8.417  -20.845 1.00 28.67  ? 464 LEU A CD1   1 
ATOM   3393 C CD2   . LEU A 1 483 ? 7.593   -6.775  -22.321 1.00 28.92  ? 464 LEU A CD2   1 
ATOM   3394 N N     . ARG A 1 484 ? 7.496   -3.008  -19.187 1.00 24.89  ? 465 ARG A N     1 
ATOM   3395 C CA    . ARG A 1 484 ? 6.775   -2.124  -18.318 1.00 25.48  ? 465 ARG A CA    1 
ATOM   3396 C C     . ARG A 1 484 ? 5.507   -2.803  -17.826 1.00 25.60  ? 465 ARG A C     1 
ATOM   3397 O O     . ARG A 1 484 ? 5.054   -3.751  -18.442 1.00 25.38  ? 465 ARG A O     1 
ATOM   3398 C CB    . ARG A 1 484 ? 6.435   -0.860  -19.105 1.00 24.86  ? 465 ARG A CB    1 
ATOM   3399 C CG    . ARG A 1 484 ? 7.650   0.000   -19.424 1.00 26.95  ? 465 ARG A CG    1 
ATOM   3400 C CD    . ARG A 1 484 ? 7.505   0.779   -20.720 1.00 28.07  ? 465 ARG A CD    1 
ATOM   3401 N NE    . ARG A 1 484 ? 6.162   1.313   -20.983 1.00 26.75  ? 465 ARG A NE    1 
ATOM   3402 C CZ    . ARG A 1 484 ? 5.887   2.340   -21.794 1.00 28.92  ? 465 ARG A CZ    1 
ATOM   3403 N NH1   . ARG A 1 484 ? 6.841   3.012   -22.389 1.00 31.41  ? 465 ARG A NH1   1 
ATOM   3404 N NH2   . ARG A 1 484 ? 4.644   2.747   -21.964 1.00 24.48  ? 465 ARG A NH2   1 
ATOM   3405 N N     . PRO A 1 485 ? 4.854   -2.271  -16.765 1.00 25.76  ? 466 PRO A N     1 
ATOM   3406 C CA    . PRO A 1 485 ? 3.608   -2.850  -16.271 1.00 25.61  ? 466 PRO A CA    1 
ATOM   3407 C C     . PRO A 1 485 ? 2.462   -2.796  -17.280 1.00 25.42  ? 466 PRO A C     1 
ATOM   3408 O O     . PRO A 1 485 ? 1.480   -3.557  -17.188 1.00 25.45  ? 466 PRO A O     1 
ATOM   3409 C CB    . PRO A 1 485 ? 3.301   -1.978  -15.038 1.00 24.36  ? 466 PRO A CB    1 
ATOM   3410 C CG    . PRO A 1 485 ? 4.673   -1.469  -14.619 1.00 24.22  ? 466 PRO A CG    1 
ATOM   3411 C CD    . PRO A 1 485 ? 5.298   -1.139  -15.938 1.00 23.03  ? 466 PRO A CD    1 
ATOM   3412 N N     . ASP A 1 486 ? 2.570   -1.921  -18.284 1.00 22.35  ? 467 ASP A N     1 
ATOM   3413 C CA    . ASP A 1 486 ? 1.567   -1.904  -19.348 1.00 23.93  ? 467 ASP A CA    1 
ATOM   3414 C C     . ASP A 1 486 ? 1.783   -2.952  -20.452 1.00 21.96  ? 467 ASP A C     1 
ATOM   3415 O O     . ASP A 1 486 ? 0.966   -3.066  -21.368 1.00 22.94  ? 467 ASP A O     1 
ATOM   3416 C CB    . ASP A 1 486 ? 1.405   -0.532  -20.015 1.00 23.50  ? 467 ASP A CB    1 
ATOM   3417 C CG    . ASP A 1 486 ? 2.669   0.116   -20.523 1.00 27.73  ? 467 ASP A CG    1 
ATOM   3418 O OD1   . ASP A 1 486 ? 3.660   -0.596  -20.729 1.00 25.55  ? 467 ASP A OD1   1 
ATOM   3419 O OD2   . ASP A 1 486 ? 2.610   1.357   -20.686 1.00 28.61  ? 467 ASP A OD2   1 
ATOM   3420 N N     . GLY A 1 487 ? 2.821   -3.793  -20.311 1.00 21.78  ? 468 GLY A N     1 
ATOM   3421 C CA    . GLY A 1 487 ? 3.143   -4.806  -21.286 1.00 24.74  ? 468 GLY A CA    1 
ATOM   3422 C C     . GLY A 1 487 ? 4.060   -4.365  -22.426 1.00 24.47  ? 468 GLY A C     1 
ATOM   3423 O O     . GLY A 1 487 ? 4.386   -5.182  -23.281 1.00 27.18  ? 468 GLY A O     1 
ATOM   3424 N N     . HIS A 1 488 ? 4.487   -3.091  -22.463 1.00 22.02  ? 469 HIS A N     1 
ATOM   3425 C CA    . HIS A 1 488 ? 5.327   -2.598  -23.541 1.00 24.24  ? 469 HIS A CA    1 
ATOM   3426 C C     . HIS A 1 488 ? 6.805   -2.732  -23.179 1.00 23.54  ? 469 HIS A C     1 
ATOM   3427 O O     . HIS A 1 488 ? 7.225   -2.569  -22.010 1.00 23.49  ? 469 HIS A O     1 
ATOM   3428 C CB    . HIS A 1 488 ? 4.979   -1.147  -23.928 1.00 25.42  ? 469 HIS A CB    1 
ATOM   3429 C CG    . HIS A 1 488 ? 3.718   -1.106  -24.706 1.00 23.50  ? 469 HIS A CG    1 
ATOM   3430 N ND1   . HIS A 1 488 ? 3.659   -1.035  -26.085 1.00 23.56  ? 469 HIS A ND1   1 
ATOM   3431 C CD2   . HIS A 1 488 ? 2.454   -1.254  -24.274 1.00 26.01  ? 469 HIS A CD2   1 
ATOM   3432 C CE1   . HIS A 1 488 ? 2.374   -1.111  -26.444 1.00 25.58  ? 469 HIS A CE1   1 
ATOM   3433 N NE2   . HIS A 1 488 ? 1.640   -1.231  -25.361 1.00 26.10  ? 469 HIS A NE2   1 
ATOM   3434 N N     . VAL A 1 489 ? 7.584   -2.973  -24.228 1.00 25.22  ? 470 VAL A N     1 
ATOM   3435 C CA    . VAL A 1 489 ? 8.994   -3.297  -24.110 1.00 23.24  ? 470 VAL A CA    1 
ATOM   3436 C C     . VAL A 1 489 ? 9.818   -2.032  -23.894 1.00 24.50  ? 470 VAL A C     1 
ATOM   3437 O O     . VAL A 1 489 ? 9.822   -1.157  -24.722 1.00 29.00  ? 470 VAL A O     1 
ATOM   3438 C CB    . VAL A 1 489 ? 9.484   -4.057  -25.350 1.00 23.17  ? 470 VAL A CB    1 
ATOM   3439 C CG1   . VAL A 1 489 ? 11.000  -4.238  -25.300 1.00 24.26  ? 470 VAL A CG1   1 
ATOM   3440 C CG2   . VAL A 1 489 ? 8.762   -5.394  -25.499 1.00 24.33  ? 470 VAL A CG2   1 
ATOM   3441 N N     . ALA A 1 490 ? 10.542  -1.975  -22.776 1.00 23.93  ? 471 ALA A N     1 
ATOM   3442 C CA    . ALA A 1 490 ? 11.429  -0.878  -22.437 1.00 24.40  ? 471 ALA A CA    1 
ATOM   3443 C C     . ALA A 1 490 ? 12.892  -1.203  -22.761 1.00 27.50  ? 471 ALA A C     1 
ATOM   3444 O O     . ALA A 1 490 ? 13.691  -0.291  -22.843 1.00 27.83  ? 471 ALA A O     1 
ATOM   3445 C CB    . ALA A 1 490 ? 11.275  -0.627  -20.964 1.00 25.88  ? 471 ALA A CB    1 
ATOM   3446 N N     . TRP A 1 491 ? 13.236  -2.497  -22.877 1.00 26.42  ? 472 TRP A N     1 
ATOM   3447 C CA    . TRP A 1 491 ? 14.597  -2.934  -23.164 1.00 25.60  ? 472 TRP A CA    1 
ATOM   3448 C C     . TRP A 1 491 ? 14.554  -4.373  -23.664 1.00 28.00  ? 472 TRP A C     1 
ATOM   3449 O O     . TRP A 1 491 ? 13.633  -5.116  -23.306 1.00 25.80  ? 472 TRP A O     1 
ATOM   3450 C CB    . TRP A 1 491 ? 15.492  -2.801  -21.924 1.00 27.98  ? 472 TRP A CB    1 
ATOM   3451 C CG    . TRP A 1 491 ? 16.851  -3.436  -22.018 1.00 28.42  ? 472 TRP A CG    1 
ATOM   3452 C CD1   . TRP A 1 491 ? 18.019  -2.815  -22.356 1.00 34.50  ? 472 TRP A CD1   1 
ATOM   3453 C CD2   . TRP A 1 491 ? 17.204  -4.807  -21.748 1.00 29.22  ? 472 TRP A CD2   1 
ATOM   3454 N NE1   . TRP A 1 491 ? 19.061  -3.708  -22.326 1.00 31.18  ? 472 TRP A NE1   1 
ATOM   3455 C CE2   . TRP A 1 491 ? 18.596  -4.929  -21.923 1.00 31.19  ? 472 TRP A CE2   1 
ATOM   3456 C CE3   . TRP A 1 491 ? 16.482  -5.933  -21.350 1.00 30.31  ? 472 TRP A CE3   1 
ATOM   3457 C CZ2   . TRP A 1 491 ? 19.267  -6.140  -21.751 1.00 33.66  ? 472 TRP A CZ2   1 
ATOM   3458 C CZ3   . TRP A 1 491 ? 17.140  -7.120  -21.164 1.00 31.72  ? 472 TRP A CZ3   1 
ATOM   3459 C CH2   . TRP A 1 491 ? 18.522  -7.222  -21.353 1.00 35.02  ? 472 TRP A CH2   1 
ATOM   3460 N N     . ALA A 1 492 ? 15.544  -4.741  -24.494 1.00 27.28  ? 473 ALA A N     1 
ATOM   3461 C CA    . ALA A 1 492 ? 15.797  -6.135  -24.818 1.00 30.06  ? 473 ALA A CA    1 
ATOM   3462 C C     . ALA A 1 492 ? 17.292  -6.320  -25.025 1.00 31.02  ? 473 ALA A C     1 
ATOM   3463 O O     . ALA A 1 492 ? 17.983  -5.352  -25.315 1.00 29.71  ? 473 ALA A O     1 
ATOM   3464 C CB    . ALA A 1 492 ? 15.032  -6.554  -26.039 1.00 29.03  ? 473 ALA A CB    1 
ATOM   3465 N N     . GLU A 1 493 ? 17.750  -7.565  -24.856 1.00 30.25  ? 474 GLU A N     1 
ATOM   3466 C CA    . GLU A 1 493 ? 19.127  -7.923  -25.132 1.00 31.56  ? 474 GLU A CA    1 
ATOM   3467 C C     . GLU A 1 493 ? 19.556  -7.321  -26.465 1.00 33.58  ? 474 GLU A C     1 
ATOM   3468 O O     . GLU A 1 493 ? 18.892  -7.526  -27.479 1.00 32.31  ? 474 GLU A O     1 
ATOM   3469 C CB    . GLU A 1 493 ? 19.252  -9.449  -25.187 1.00 35.52  ? 474 GLU A CB    1 
ATOM   3470 C CG    . GLU A 1 493 ? 20.686  -9.936  -25.261 1.00 41.03  ? 474 GLU A CG    1 
ATOM   3471 C CD    . GLU A 1 493 ? 21.462  -9.583  -24.011 1.00 46.31  ? 474 GLU A CD    1 
ATOM   3472 O OE1   . GLU A 1 493 ? 21.058  -10.065 -22.936 1.00 50.75  ? 474 GLU A OE1   1 
ATOM   3473 O OE2   . GLU A 1 493 ? 22.417  -8.788  -24.100 1.00 49.31  ? 474 GLU A OE2   1 
ATOM   3474 N N     . GLY A 1 494 ? 20.652  -6.548  -26.433 1.00 36.22  ? 475 GLY A N     1 
ATOM   3475 C CA    . GLY A 1 494 ? 21.193  -5.905  -27.621 1.00 40.56  ? 475 GLY A CA    1 
ATOM   3476 C C     . GLY A 1 494 ? 20.782  -4.440  -27.781 1.00 37.69  ? 475 GLY A C     1 
ATOM   3477 O O     . GLY A 1 494 ? 21.283  -3.775  -28.670 1.00 40.02  ? 475 GLY A O     1 
ATOM   3478 N N     . SER A 1 495 ? 19.903  -3.914  -26.922 1.00 33.58  ? 476 SER A N     1 
ATOM   3479 C CA    . SER A 1 495 ? 19.473  -2.524  -27.018 1.00 35.07  ? 476 SER A CA    1 
ATOM   3480 C C     . SER A 1 495 ? 20.071  -1.667  -25.895 1.00 38.53  ? 476 SER A C     1 
ATOM   3481 O O     . SER A 1 495 ? 19.405  -0.790  -25.332 1.00 40.33  ? 476 SER A O     1 
ATOM   3482 C CB    . SER A 1 495 ? 17.945  -2.436  -27.029 1.00 34.07  ? 476 SER A CB    1 
ATOM   3483 O OG    . SER A 1 495 ? 17.406  -3.078  -28.171 1.00 33.51  ? 476 SER A OG    1 
ATOM   3484 N N     . GLY A 1 496 ? 21.357  -1.863  -25.585 1.00 38.32  ? 477 GLY A N     1 
ATOM   3485 C CA    . GLY A 1 496 ? 21.996  -1.037  -24.569 1.00 36.72  ? 477 GLY A CA    1 
ATOM   3486 C C     . GLY A 1 496 ? 21.888  -1.642  -23.166 1.00 38.16  ? 477 GLY A C     1 
ATOM   3487 O O     . GLY A 1 496 ? 21.781  -2.859  -23.006 1.00 36.16  ? 477 GLY A O     1 
ATOM   3488 N N     . SER A 1 497 ? 21.937  -0.774  -22.149 1.00 36.27  ? 478 SER A N     1 
ATOM   3489 C CA    . SER A 1 497 ? 22.084  -1.187  -20.755 1.00 36.85  ? 478 SER A CA    1 
ATOM   3490 C C     . SER A 1 497 ? 20.736  -1.512  -20.099 1.00 35.14  ? 478 SER A C     1 
ATOM   3491 O O     . SER A 1 497 ? 19.883  -0.644  -20.031 1.00 32.92  ? 478 SER A O     1 
ATOM   3492 C CB    . SER A 1 497 ? 22.741  -0.079  -19.980 1.00 36.47  ? 478 SER A CB    1 
ATOM   3493 O OG    . SER A 1 497 ? 22.650  -0.323  -18.597 1.00 37.24  ? 478 SER A OG    1 
ATOM   3494 N N     . LEU A 1 498 ? 20.580  -2.722  -19.541 1.00 35.98  ? 479 LEU A N     1 
ATOM   3495 C CA    . LEU A 1 498 ? 19.372  -3.048  -18.784 1.00 36.63  ? 479 LEU A CA    1 
ATOM   3496 C C     . LEU A 1 498 ? 19.265  -2.161  -17.544 1.00 34.87  ? 479 LEU A C     1 
ATOM   3497 O O     . LEU A 1 498 ? 18.196  -1.680  -17.174 1.00 30.60  ? 479 LEU A O     1 
ATOM   3498 C CB    . LEU A 1 498 ? 19.388  -4.536  -18.419 1.00 33.08  ? 479 LEU A CB    1 
ATOM   3499 C CG    . LEU A 1 498 ? 18.352  -4.967  -17.387 1.00 33.68  ? 479 LEU A CG    1 
ATOM   3500 C CD1   . LEU A 1 498 ? 16.921  -4.657  -17.854 1.00 31.46  ? 479 LEU A CD1   1 
ATOM   3501 C CD2   . LEU A 1 498 ? 18.538  -6.446  -17.070 1.00 35.55  ? 479 LEU A CD2   1 
ATOM   3502 N N     . GLU A 1 499 ? 20.399  -1.906  -16.903 1.00 38.67  ? 480 GLU A N     1 
ATOM   3503 C CA    . GLU A 1 499 ? 20.388  -1.099  -15.695 1.00 36.34  ? 480 GLU A CA    1 
ATOM   3504 C C     . GLU A 1 499 ? 19.871  0.311   -15.984 1.00 31.53  ? 480 GLU A C     1 
ATOM   3505 O O     . GLU A 1 499 ? 19.112  0.860   -15.201 1.00 36.62  ? 480 GLU A O     1 
ATOM   3506 C CB    . GLU A 1 499 ? 21.789  -1.098  -15.076 1.00 43.53  ? 480 GLU A CB    1 
ATOM   3507 C CG    . GLU A 1 499 ? 21.970  -0.113  -13.949 1.00 47.21  ? 480 GLU A CG    1 
ATOM   3508 C CD    . GLU A 1 499 ? 23.378  -0.142  -13.367 1.00 53.05  ? 480 GLU A CD    1 
ATOM   3509 O OE1   . GLU A 1 499 ? 24.254  -0.817  -13.960 1.00 60.40  ? 480 GLU A OE1   1 
ATOM   3510 O OE2   . GLU A 1 499 ? 23.592  0.519   -12.344 1.00 55.45  ? 480 GLU A OE2   1 
ATOM   3511 N N     . THR A 1 500 ? 20.260  0.916   -17.108 1.00 33.01  ? 481 THR A N     1 
ATOM   3512 C CA    . THR A 1 500 ? 19.811  2.267   -17.427 1.00 33.72  ? 481 THR A CA    1 
ATOM   3513 C C     . THR A 1 500 ? 18.314  2.252   -17.769 1.00 30.40  ? 481 THR A C     1 
ATOM   3514 O O     . THR A 1 500 ? 17.591  3.193   -17.503 1.00 30.86  ? 481 THR A O     1 
ATOM   3515 C CB    . THR A 1 500 ? 20.660  2.833   -18.580 1.00 39.01  ? 481 THR A CB    1 
ATOM   3516 O OG1   . THR A 1 500 ? 22.033  2.830   -18.163 1.00 40.22  ? 481 THR A OG1   1 
ATOM   3517 C CG2   . THR A 1 500 ? 20.255  4.227   -18.997 1.00 39.68  ? 481 THR A CG2   1 
ATOM   3518 N N     . ALA A 1 501 ? 17.855  1.182   -18.425 1.00 31.69  ? 482 ALA A N     1 
ATOM   3519 C CA    . ALA A 1 501 ? 16.448  1.061   -18.770 1.00 30.95  ? 482 ALA A CA    1 
ATOM   3520 C C     . ALA A 1 501 ? 15.586  0.895   -17.523 1.00 27.37  ? 482 ALA A C     1 
ATOM   3521 O O     . ALA A 1 501 ? 14.501  1.488   -17.450 1.00 29.09  ? 482 ALA A O     1 
ATOM   3522 C CB    . ALA A 1 501 ? 16.267  -0.096  -19.729 1.00 29.75  ? 482 ALA A CB    1 
ATOM   3523 N N     . LEU A 1 502 ? 16.053  0.106   -16.546 1.00 31.43  ? 483 LEU A N     1 
ATOM   3524 C CA    . LEU A 1 502 ? 15.369  -0.006  -15.255 1.00 30.82  ? 483 LEU A CA    1 
ATOM   3525 C C     . LEU A 1 502 ? 15.266  1.367   -14.578 1.00 34.02  ? 483 LEU A C     1 
ATOM   3526 O O     . LEU A 1 502 ? 14.193  1.776   -14.113 1.00 30.95  ? 483 LEU A O     1 
ATOM   3527 C CB    . LEU A 1 502 ? 16.089  -1.038  -14.381 1.00 30.10  ? 483 LEU A CB    1 
ATOM   3528 C CG    . LEU A 1 502 ? 15.948  -2.482  -14.824 1.00 30.28  ? 483 LEU A CG    1 
ATOM   3529 C CD1   . LEU A 1 502 ? 17.060  -3.356  -14.264 1.00 34.71  ? 483 LEU A CD1   1 
ATOM   3530 C CD2   . LEU A 1 502 ? 14.599  -3.018  -14.406 1.00 31.20  ? 483 LEU A CD2   1 
ATOM   3531 N N     . LYS A 1 503 ? 16.369  2.135   -14.566 1.00 33.67  ? 484 LYS A N     1 
ATOM   3532 C CA    . LYS A 1 503 ? 16.291  3.489   -14.043 1.00 34.17  ? 484 LYS A CA    1 
ATOM   3533 C C     . LYS A 1 503 ? 15.277  4.342   -14.804 1.00 29.95  ? 484 LYS A C     1 
ATOM   3534 O O     . LYS A 1 503 ? 14.560  5.098   -14.177 1.00 33.29  ? 484 LYS A O     1 
ATOM   3535 C CB    . LYS A 1 503 ? 17.656  4.181   -14.014 1.00 42.96  ? 484 LYS A CB    1 
ATOM   3536 C CG    . LYS A 1 503 ? 18.722  3.466   -13.200 1.00 59.16  ? 484 LYS A CG    1 
ATOM   3537 C CD    . LYS A 1 503 ? 19.974  4.296   -12.890 1.00 71.15  ? 484 LYS A CD    1 
ATOM   3538 C CE    . LYS A 1 503 ? 19.805  5.193   -11.677 1.00 82.97  ? 484 LYS A CE    1 
ATOM   3539 N NZ    . LYS A 1 503 ? 18.940  6.367   -11.955 1.00 85.72  ? 484 LYS A NZ    1 
ATOM   3540 N N     . ASN A 1 504 ? 15.238  4.279   -16.147 1.00 29.50  ? 485 ASN A N     1 
ATOM   3541 C CA    . ASN A 1 504 ? 14.415  5.189   -16.938 1.00 32.32  ? 485 ASN A CA    1 
ATOM   3542 C C     . ASN A 1 504 ? 12.925  4.970   -16.702 1.00 30.23  ? 485 ASN A C     1 
ATOM   3543 O O     . ASN A 1 504 ? 12.175  5.916   -16.831 1.00 31.43  ? 485 ASN A O     1 
ATOM   3544 C CB    . ASN A 1 504 ? 14.717  5.101   -18.447 1.00 35.61  ? 485 ASN A CB    1 
ATOM   3545 C CG    . ASN A 1 504 ? 16.013  5.820   -18.814 1.00 39.85  ? 485 ASN A CG    1 
ATOM   3546 O OD1   . ASN A 1 504 ? 16.372  6.800   -18.166 1.00 45.22  ? 485 ASN A OD1   1 
ATOM   3547 N ND2   . ASN A 1 504 ? 16.745  5.326   -19.802 1.00 38.09  ? 485 ASN A ND2   1 
ATOM   3548 N N     . TRP A 1 505 ? 12.502  3.733   -16.418 1.00 28.40  ? 486 TRP A N     1 
ATOM   3549 C CA    . TRP A 1 505 ? 11.072  3.419   -16.304 1.00 28.07  ? 486 TRP A CA    1 
ATOM   3550 C C     . TRP A 1 505 ? 10.658  3.093   -14.871 1.00 28.67  ? 486 TRP A C     1 
ATOM   3551 O O     . TRP A 1 505 ? 9.481   3.204   -14.554 1.00 27.92  ? 486 TRP A O     1 
ATOM   3552 C CB    . TRP A 1 505 ? 10.672  2.293   -17.272 1.00 27.77  ? 486 TRP A CB    1 
ATOM   3553 C CG    . TRP A 1 505 ? 10.798  2.759   -18.681 1.00 26.77  ? 486 TRP A CG    1 
ATOM   3554 C CD1   . TRP A 1 505 ? 11.851  2.541   -19.515 1.00 27.22  ? 486 TRP A CD1   1 
ATOM   3555 C CD2   . TRP A 1 505 ? 9.901   3.641   -19.369 1.00 27.03  ? 486 TRP A CD2   1 
ATOM   3556 N NE1   . TRP A 1 505 ? 11.651  3.202   -20.691 1.00 26.39  ? 486 TRP A NE1   1 
ATOM   3557 C CE2   . TRP A 1 505 ? 10.496  3.921   -20.619 1.00 27.20  ? 486 TRP A CE2   1 
ATOM   3558 C CE3   . TRP A 1 505 ? 8.705   4.295   -19.028 1.00 28.62  ? 486 TRP A CE3   1 
ATOM   3559 C CZ2   . TRP A 1 505 ? 9.898   4.761   -21.548 1.00 28.06  ? 486 TRP A CZ2   1 
ATOM   3560 C CZ3   . TRP A 1 505 ? 8.112   5.118   -19.954 1.00 30.70  ? 486 TRP A CZ3   1 
ATOM   3561 C CH2   . TRP A 1 505 ? 8.699   5.335   -21.208 1.00 29.40  ? 486 TRP A CH2   1 
ATOM   3562 N N     . PHE A 1 506 ? 11.589  2.663   -14.010 1.00 27.74  ? 487 PHE A N     1 
ATOM   3563 C CA    . PHE A 1 506 ? 11.200  2.196   -12.683 1.00 27.74  ? 487 PHE A CA    1 
ATOM   3564 C C     . PHE A 1 506 ? 11.876  2.978   -11.566 1.00 28.50  ? 487 PHE A C     1 
ATOM   3565 O O     . PHE A 1 506 ? 11.556  2.743   -10.423 1.00 30.88  ? 487 PHE A O     1 
ATOM   3566 C CB    . PHE A 1 506 ? 11.492  0.702   -12.569 1.00 28.40  ? 487 PHE A CB    1 
ATOM   3567 C CG    . PHE A 1 506 ? 10.659  -0.164  -13.471 1.00 25.03  ? 487 PHE A CG    1 
ATOM   3568 C CD1   . PHE A 1 506 ? 9.379   -0.528  -13.122 1.00 28.49  ? 487 PHE A CD1   1 
ATOM   3569 C CD2   . PHE A 1 506 ? 11.147  -0.586  -14.699 1.00 26.33  ? 487 PHE A CD2   1 
ATOM   3570 C CE1   . PHE A 1 506 ? 8.618   -1.346  -13.945 1.00 27.20  ? 487 PHE A CE1   1 
ATOM   3571 C CE2   . PHE A 1 506 ? 10.398  -1.420  -15.511 1.00 29.72  ? 487 PHE A CE2   1 
ATOM   3572 C CZ    . PHE A 1 506 ? 9.119   -1.797  -15.134 1.00 26.69  ? 487 PHE A CZ    1 
ATOM   3573 N N     . GLY A 1 507 ? 12.768  3.918   -11.891 1.00 32.51  ? 488 GLY A N     1 
ATOM   3574 C CA    . GLY A 1 507 ? 13.295  4.857   -10.904 1.00 36.18  ? 488 GLY A CA    1 
ATOM   3575 C C     . GLY A 1 507 ? 14.571  4.360   -10.220 1.00 34.76  ? 488 GLY A C     1 
ATOM   3576 O O     . GLY A 1 507 ? 15.329  3.558   -10.756 1.00 34.72  ? 488 GLY A O     1 
ATOM   3577 N N     . THR A 1 508 ? 14.776  4.801   -8.976  1.00 36.04  ? 489 THR A N     1 
ATOM   3578 C CA    . THR A 1 508 ? 16.033  4.576   -8.274  1.00 43.07  ? 489 THR A CA    1 
ATOM   3579 C C     . THR A 1 508 ? 16.085  3.177   -7.646  1.00 39.21  ? 489 THR A C     1 
ATOM   3580 O O     . THR A 1 508 ? 15.097  2.646   -7.119  1.00 35.57  ? 489 THR A O     1 
ATOM   3581 C CB    . THR A 1 508 ? 16.241  5.718   -7.272  1.00 45.04  ? 489 THR A CB    1 
ATOM   3582 O OG1   . THR A 1 508 ? 15.225  5.594   -6.293  1.00 49.09  ? 489 THR A OG1   1 
ATOM   3583 C CG2   . THR A 1 508 ? 16.091  7.080   -7.908  1.00 47.15  ? 489 THR A CG2   1 
ATOM   3584 N N     . PRO A 1 509 ? 17.261  2.519   -7.722  1.00 37.02  ? 490 PRO A N     1 
ATOM   3585 C CA    . PRO A 1 509 ? 17.468  1.199   -7.128  1.00 39.40  ? 490 PRO A CA    1 
ATOM   3586 C C     . PRO A 1 509 ? 17.131  1.230   -5.637  1.00 42.04  ? 490 PRO A C     1 
ATOM   3587 O O     . PRO A 1 509 ? 17.170  2.283   -5.018  1.00 44.54  ? 490 PRO A O     1 
ATOM   3588 C CB    . PRO A 1 509 ? 18.942  0.844   -7.394  1.00 44.80  ? 490 PRO A CB    1 
ATOM   3589 C CG    . PRO A 1 509 ? 19.567  2.068   -8.043  1.00 40.60  ? 490 PRO A CG    1 
ATOM   3590 C CD    . PRO A 1 509 ? 18.459  3.033   -8.405  1.00 39.50  ? 490 PRO A CD    1 
ATOM   3591 N N     . ARG A 1 510 ? 16.682  0.096   -5.097  1.00 46.91  ? 491 ARG A N     1 
ATOM   3592 C CA    . ARG A 1 510 ? 16.147  0.056   -3.742  1.00 53.18  ? 491 ARG A CA    1 
ATOM   3593 C C     . ARG A 1 510 ? 17.234  0.472   -2.733  1.00 57.56  ? 491 ARG A C     1 
ATOM   3594 O O     . ARG A 1 510 ? 18.432  0.300   -3.069  1.00 60.25  ? 491 ARG A O     1 
ATOM   3595 C CB    . ARG A 1 510 ? 15.576  -1.335  -3.428  1.00 51.12  ? 491 ARG A CB    1 
ATOM   3596 C CG    . ARG A 1 510 ? 16.593  -2.472  -3.425  1.00 51.86  ? 491 ARG A CG    1 
ATOM   3597 C CD    . ARG A 1 510 ? 15.972  -3.844  -3.158  1.00 52.71  ? 491 ARG A CD    1 
ATOM   3598 N NE    . ARG A 1 510 ? 16.936  -4.935  -3.346  1.00 47.19  ? 491 ARG A NE    1 
ATOM   3599 C CZ    . ARG A 1 510 ? 16.628  -6.230  -3.338  1.00 51.70  ? 491 ARG A CZ    1 
ATOM   3600 N NH1   . ARG A 1 510 ? 17.569  -7.138  -3.554  1.00 46.02  ? 491 ARG A NH1   1 
ATOM   3601 N NH2   . ARG A 1 510 ? 15.377  -6.616  -3.121  1.00 52.65  ? 491 ARG A NH2   1 
HETATM 3602 P PA    . FAD B 2 .   ? -18.337 6.310   -22.665 1.00 26.58  ? 501 FAD A PA    1 
HETATM 3603 O O1A   . FAD B 2 .   ? -18.608 4.848   -22.888 1.00 25.81  ? 501 FAD A O1A   1 
HETATM 3604 O O2A   . FAD B 2 .   ? -19.041 7.401   -23.362 1.00 27.02  ? 501 FAD A O2A   1 
HETATM 3605 O O5B   . FAD B 2 .   ? -18.552 6.516   -21.079 1.00 29.49  ? 501 FAD A O5B   1 
HETATM 3606 C C5B   . FAD B 2 .   ? -18.424 7.846   -20.497 1.00 27.31  ? 501 FAD A C5B   1 
HETATM 3607 C C4B   . FAD B 2 .   ? -19.118 7.832   -19.160 1.00 28.45  ? 501 FAD A C4B   1 
HETATM 3608 O O4B   . FAD B 2 .   ? -18.948 9.143   -18.546 1.00 30.53  ? 501 FAD A O4B   1 
HETATM 3609 C C3B   . FAD B 2 .   ? -20.625 7.567   -19.260 1.00 29.37  ? 501 FAD A C3B   1 
HETATM 3610 O O3B   . FAD B 2 .   ? -21.024 6.445   -18.480 1.00 32.74  ? 501 FAD A O3B   1 
HETATM 3611 C C2B   . FAD B 2 .   ? -21.269 8.883   -18.793 1.00 30.89  ? 501 FAD A C2B   1 
HETATM 3612 O O2B   . FAD B 2 .   ? -22.451 8.601   -18.071 1.00 31.53  ? 501 FAD A O2B   1 
HETATM 3613 C C1B   . FAD B 2 .   ? -20.180 9.492   -17.931 1.00 32.17  ? 501 FAD A C1B   1 
HETATM 3614 N N9A   . FAD B 2 .   ? -20.209 10.938  -17.805 1.00 31.89  ? 501 FAD A N9A   1 
HETATM 3615 C C8A   . FAD B 2 .   ? -20.258 11.846  -18.820 1.00 33.27  ? 501 FAD A C8A   1 
HETATM 3616 N N7A   . FAD B 2 .   ? -20.209 13.084  -18.389 1.00 32.58  ? 501 FAD A N7A   1 
HETATM 3617 C C5A   . FAD B 2 .   ? -20.132 12.966  -16.999 1.00 31.84  ? 501 FAD A C5A   1 
HETATM 3618 C C6A   . FAD B 2 .   ? -20.103 13.911  -15.955 1.00 32.80  ? 501 FAD A C6A   1 
HETATM 3619 N N6A   . FAD B 2 .   ? -20.095 15.225  -16.150 1.00 35.91  ? 501 FAD A N6A   1 
HETATM 3620 N N1A   . FAD B 2 .   ? -19.978 13.452  -14.690 1.00 28.40  ? 501 FAD A N1A   1 
HETATM 3621 C C2A   . FAD B 2 .   ? -19.995 12.125  -14.489 1.00 31.95  ? 501 FAD A C2A   1 
HETATM 3622 N N3A   . FAD B 2 .   ? -20.072 11.144  -15.385 1.00 28.46  ? 501 FAD A N3A   1 
HETATM 3623 C C4A   . FAD B 2 .   ? -20.129 11.641  -16.633 1.00 30.73  ? 501 FAD A C4A   1 
HETATM 3624 N N1    . FAD B 2 .   ? -16.125 1.110   -30.553 1.00 24.42  ? 501 FAD A N1    1 
HETATM 3625 C C2    . FAD B 2 .   ? -15.529 -0.089  -30.805 1.00 26.66  ? 501 FAD A C2    1 
HETATM 3626 O O2    . FAD B 2 .   ? -14.338 -0.262  -30.540 1.00 24.22  ? 501 FAD A O2    1 
HETATM 3627 N N3    . FAD B 2 .   ? -16.177 -1.085  -31.429 1.00 24.31  ? 501 FAD A N3    1 
HETATM 3628 C C4    . FAD B 2 .   ? -17.436 -0.933  -31.959 1.00 27.21  ? 501 FAD A C4    1 
HETATM 3629 O O4    . FAD B 2 .   ? -17.982 -1.877  -32.520 1.00 27.86  ? 501 FAD A O4    1 
HETATM 3630 C C4X   . FAD B 2 .   ? -18.064 0.321   -31.799 1.00 23.96  ? 501 FAD A C4X   1 
HETATM 3631 N N5    . FAD B 2 .   ? -19.304 0.494   -32.260 1.00 25.06  ? 501 FAD A N5    1 
HETATM 3632 C C5X   . FAD B 2 .   ? -19.880 1.724   -32.012 1.00 26.19  ? 501 FAD A C5X   1 
HETATM 3633 C C6    . FAD B 2 .   ? -21.146 1.999   -32.549 1.00 26.38  ? 501 FAD A C6    1 
HETATM 3634 C C7    . FAD B 2 .   ? -21.764 3.211   -32.343 1.00 25.89  ? 501 FAD A C7    1 
HETATM 3635 C C7M   . FAD B 2 .   ? -23.151 3.412   -32.918 1.00 28.11  ? 501 FAD A C7M   1 
HETATM 3636 C C8    . FAD B 2 .   ? -21.139 4.191   -31.554 1.00 26.20  ? 501 FAD A C8    1 
HETATM 3637 C C8M   . FAD B 2 .   ? -21.763 5.537   -31.291 1.00 27.84  ? 501 FAD A C8M   1 
HETATM 3638 C C9    . FAD B 2 .   ? -19.888 3.958   -31.039 1.00 25.91  ? 501 FAD A C9    1 
HETATM 3639 C C9A   . FAD B 2 .   ? -19.254 2.722   -31.237 1.00 25.17  ? 501 FAD A C9A   1 
HETATM 3640 N N10   . FAD B 2 .   ? -17.979 2.466   -30.744 1.00 24.32  ? 501 FAD A N10   1 
HETATM 3641 C C10   . FAD B 2 .   ? -17.359 1.263   -30.988 1.00 22.64  ? 501 FAD A C10   1 
HETATM 3642 C "C1'" . FAD B 2 .   ? -17.290 3.443   -29.904 1.00 25.36  ? 501 FAD A "C1'" 1 
HETATM 3643 C "C2'" . FAD B 2 .   ? -17.497 3.064   -28.390 1.00 27.56  ? 501 FAD A "C2'" 1 
HETATM 3644 O "O2'" . FAD B 2 .   ? -18.878 2.911   -27.988 1.00 24.32  ? 501 FAD A "O2'" 1 
HETATM 3645 C "C3'" . FAD B 2 .   ? -16.872 4.133   -27.497 1.00 27.77  ? 501 FAD A "C3'" 1 
HETATM 3646 O "O3'" . FAD B 2 .   ? -15.486 4.322   -27.892 1.00 27.47  ? 501 FAD A "O3'" 1 
HETATM 3647 C "C4'" . FAD B 2 .   ? -16.845 3.846   -25.992 1.00 26.43  ? 501 FAD A "C4'" 1 
HETATM 3648 O "O4'" . FAD B 2 .   ? -18.148 3.913   -25.389 1.00 26.22  ? 501 FAD A "O4'" 1 
HETATM 3649 C "C5'" . FAD B 2 .   ? -15.938 4.818   -25.277 1.00 24.44  ? 501 FAD A "C5'" 1 
HETATM 3650 O "O5'" . FAD B 2 .   ? -15.878 4.481   -23.896 1.00 26.85  ? 501 FAD A "O5'" 1 
HETATM 3651 P P     . FAD B 2 .   ? -15.499 5.580   -22.814 1.00 25.28  ? 501 FAD A P     1 
HETATM 3652 O O1P   . FAD B 2 .   ? -15.416 4.863   -21.527 1.00 25.04  ? 501 FAD A O1P   1 
HETATM 3653 O O2P   . FAD B 2 .   ? -14.339 6.434   -23.202 1.00 22.89  ? 501 FAD A O2P   1 
HETATM 3654 O O3P   . FAD B 2 .   ? -16.770 6.596   -22.847 1.00 23.14  ? 501 FAD A O3P   1 
HETATM 3655 O O     . HOH C 3 .   ? -37.745 -11.707 -38.687 1.00 47.68  ? 601 HOH A O     1 
HETATM 3656 O O     . HOH C 3 .   ? -22.613 -4.226  -34.138 1.00 40.92  ? 602 HOH A O     1 
HETATM 3657 O O     . HOH C 3 .   ? -7.497  -3.697  -60.402 1.00 54.83  ? 603 HOH A O     1 
HETATM 3658 O O     . HOH C 3 .   ? 7.456   -4.652  -51.408 1.00 33.07  ? 604 HOH A O     1 
HETATM 3659 O O     . HOH C 3 .   ? 4.073   15.398  -12.592 1.00 40.85  ? 605 HOH A O     1 
HETATM 3660 O O     . HOH C 3 .   ? 19.604  0.245   -29.243 1.00 38.97  ? 606 HOH A O     1 
HETATM 3661 O O     . HOH C 3 .   ? -3.434  0.256   -34.538 1.00 32.32  ? 607 HOH A O     1 
HETATM 3662 O O     . HOH C 3 .   ? -19.121 -11.458 -20.749 1.00 38.28  ? 608 HOH A O     1 
HETATM 3663 O O     . HOH C 3 .   ? -20.809 10.612  -2.816  1.00 51.50  ? 609 HOH A O     1 
HETATM 3664 O O     . HOH C 3 .   ? -2.832  21.375  -10.339 1.00 41.51  ? 610 HOH A O     1 
HETATM 3665 O O     . HOH C 3 .   ? 17.347  -2.716  -32.599 1.00 41.30  ? 611 HOH A O     1 
HETATM 3666 O O     . HOH C 3 .   ? -5.075  -9.080  -12.966 1.00 32.56  ? 612 HOH A O     1 
HETATM 3667 O O     . HOH C 3 .   ? 17.274  -5.508  -29.002 1.00 33.38  ? 613 HOH A O     1 
HETATM 3668 O O     . HOH C 3 .   ? -14.208 1.694   -56.293 1.00 31.72  ? 614 HOH A O     1 
HETATM 3669 O O     . HOH C 3 .   ? 8.117   -6.637  -29.012 1.00 28.78  ? 615 HOH A O     1 
HETATM 3670 O O     . HOH C 3 .   ? -21.122 2.088   -16.427 1.00 39.43  ? 616 HOH A O     1 
HETATM 3671 O O     . HOH C 3 .   ? 8.389   6.539   -24.722 1.00 32.19  ? 617 HOH A O     1 
HETATM 3672 O O     . HOH C 3 .   ? 19.137  -12.564 -23.555 1.00 33.83  ? 618 HOH A O     1 
HETATM 3673 O O     . HOH C 3 .   ? -24.195 -3.914  -36.501 1.00 34.52  ? 619 HOH A O     1 
HETATM 3674 O O     . HOH C 3 .   ? 2.512   -2.653  -39.475 1.00 34.89  ? 620 HOH A O     1 
HETATM 3675 O O     . HOH C 3 .   ? 1.562   -2.801  -29.601 1.00 38.93  ? 621 HOH A O     1 
HETATM 3676 O O     . HOH C 3 .   ? -5.504  0.712   -31.087 1.00 26.54  ? 622 HOH A O     1 
HETATM 3677 O O     . HOH C 3 .   ? -17.491 -0.915  -35.313 1.00 40.49  ? 623 HOH A O     1 
HETATM 3678 O O     . HOH C 3 .   ? -14.402 -18.002 -21.823 1.00 42.85  ? 624 HOH A O     1 
HETATM 3679 O O     . HOH C 3 .   ? 3.399   6.968   -29.430 1.00 29.04  ? 625 HOH A O     1 
HETATM 3680 O O     . HOH C 3 .   ? -33.665 -10.017 -44.922 1.00 42.12  ? 626 HOH A O     1 
HETATM 3681 O O     . HOH C 3 .   ? -15.345 5.722   -18.972 1.00 27.35  ? 627 HOH A O     1 
HETATM 3682 O O     . HOH C 3 .   ? -8.644  22.449  -5.471  1.00 39.26  ? 628 HOH A O     1 
HETATM 3683 O O     . HOH C 3 .   ? -20.378 3.126   -21.964 1.00 31.84  ? 629 HOH A O     1 
HETATM 3684 O O     . HOH C 3 .   ? 4.543   12.912  -28.459 1.00 35.31  ? 630 HOH A O     1 
HETATM 3685 O O     . HOH C 3 .   ? 1.185   13.306  -19.801 1.00 28.81  ? 631 HOH A O     1 
HETATM 3686 O O     . HOH C 3 .   ? -1.793  -3.952  -29.240 1.00 31.62  ? 632 HOH A O     1 
HETATM 3687 O O     . HOH C 3 .   ? -3.088  4.454   -32.831 1.00 33.30  ? 633 HOH A O     1 
HETATM 3688 O O     . HOH C 3 .   ? -32.593 11.543  -37.108 1.00 50.64  ? 634 HOH A O     1 
HETATM 3689 O O     . HOH C 3 .   ? -18.229 8.602   -25.778 1.00 28.42  ? 635 HOH A O     1 
HETATM 3690 O O     . HOH C 3 .   ? -13.061 -10.519 -11.977 1.00 44.75  ? 636 HOH A O     1 
HETATM 3691 O O     . HOH C 3 .   ? 5.455   -8.733  -12.713 1.00 34.16  ? 637 HOH A O     1 
HETATM 3692 O O     . HOH C 3 .   ? 1.000   1.788   -5.716  1.00 33.22  ? 638 HOH A O     1 
HETATM 3693 O O     . HOH C 3 .   ? 3.432   -7.604  -23.910 1.00 29.89  ? 639 HOH A O     1 
HETATM 3694 O O     . HOH C 3 .   ? -25.006 1.077   -53.537 1.00 42.84  ? 640 HOH A O     1 
HETATM 3695 O O     . HOH C 3 .   ? -7.793  14.009  -43.063 1.00 28.92  ? 641 HOH A O     1 
HETATM 3696 O O     . HOH C 3 .   ? -8.945  -10.484 -35.019 1.00 34.56  ? 642 HOH A O     1 
HETATM 3697 O O     . HOH C 3 .   ? -32.710 -11.592 -26.433 1.00 42.89  ? 643 HOH A O     1 
HETATM 3698 O O     . HOH C 3 .   ? -1.811  0.635   -16.016 1.00 24.52  ? 644 HOH A O     1 
HETATM 3699 O O     . HOH C 3 .   ? -11.189 8.582   -56.414 1.00 24.12  ? 645 HOH A O     1 
HETATM 3700 O O     . HOH C 3 .   ? -13.246 17.393  -36.968 1.00 34.98  ? 646 HOH A O     1 
HETATM 3701 O O     . HOH C 3 .   ? -14.840 14.829  -53.321 1.00 38.78  ? 647 HOH A O     1 
HETATM 3702 O O     . HOH C 3 .   ? -11.031 -14.487 -32.609 1.00 32.40  ? 648 HOH A O     1 
HETATM 3703 O O     . HOH C 3 .   ? -4.613  7.492   -27.684 1.00 26.99  ? 649 HOH A O     1 
HETATM 3704 O O     . HOH C 3 .   ? -18.610 15.282  -42.669 1.00 43.94  ? 650 HOH A O     1 
HETATM 3705 O O     . HOH C 3 .   ? -11.543 10.828  -38.203 1.00 27.13  ? 651 HOH A O     1 
HETATM 3706 O O     . HOH C 3 .   ? -1.132  -9.112  -23.855 1.00 30.53  ? 652 HOH A O     1 
HETATM 3707 O O     . HOH C 3 .   ? -4.849  -10.022 -28.681 1.00 31.31  ? 653 HOH A O     1 
HETATM 3708 O O     . HOH C 3 .   ? 13.090  -5.217  -2.656  1.00 47.93  ? 654 HOH A O     1 
HETATM 3709 O O     . HOH C 3 .   ? 7.108   3.914   -33.150 1.00 37.98  ? 655 HOH A O     1 
HETATM 3710 O O     . HOH C 3 .   ? -14.520 -12.869 -38.904 1.00 50.92  ? 656 HOH A O     1 
HETATM 3711 O O     . HOH C 3 .   ? -20.433 0.505   -21.845 1.00 31.79  ? 657 HOH A O     1 
HETATM 3712 O O     . HOH C 3 .   ? 0.453   10.376  -34.971 1.00 27.98  ? 658 HOH A O     1 
HETATM 3713 O O     . HOH C 3 .   ? -12.756 9.454   9.658   1.00 47.38  ? 659 HOH A O     1 
HETATM 3714 O O     . HOH C 3 .   ? -13.658 8.876   -22.193 1.00 24.71  ? 660 HOH A O     1 
HETATM 3715 O O     . HOH C 3 .   ? -12.183 -2.900  -30.291 1.00 24.53  ? 661 HOH A O     1 
HETATM 3716 O O     . HOH C 3 .   ? 2.974   3.439   -33.020 1.00 31.76  ? 662 HOH A O     1 
HETATM 3717 O O     . HOH C 3 .   ? -23.440 12.057  -41.928 1.00 41.06  ? 663 HOH A O     1 
HETATM 3718 O O     . HOH C 3 .   ? 4.232   15.235  -22.570 1.00 39.21  ? 664 HOH A O     1 
HETATM 3719 O O     . HOH C 3 .   ? 1.735   -5.368  -30.505 1.00 40.29  ? 665 HOH A O     1 
HETATM 3720 O O     . HOH C 3 .   ? -10.517 -1.381  -36.752 1.00 31.71  ? 666 HOH A O     1 
HETATM 3721 O O     . HOH C 3 .   ? -1.501  -17.007 -15.863 1.00 45.56  ? 667 HOH A O     1 
HETATM 3722 O O     . HOH C 3 .   ? -25.928 -3.068  -25.918 1.00 42.23  ? 668 HOH A O     1 
HETATM 3723 O O     . HOH C 3 .   ? 12.356  5.497   -7.558  1.00 35.51  ? 669 HOH A O     1 
HETATM 3724 O O     . HOH C 3 .   ? -3.216  15.063  -3.280  1.00 38.71  ? 670 HOH A O     1 
HETATM 3725 O O     . HOH C 3 .   ? -16.038 5.019   -53.295 1.00 39.03  ? 671 HOH A O     1 
HETATM 3726 O O     . HOH C 3 .   ? -0.598  -8.472  -7.396  1.00 48.53  ? 672 HOH A O     1 
HETATM 3727 O O     . HOH C 3 .   ? -15.969 16.408  -36.593 1.00 36.85  ? 673 HOH A O     1 
HETATM 3728 O O     . HOH C 3 .   ? -14.202 1.733   -33.426 1.00 28.99  ? 674 HOH A O     1 
HETATM 3729 O O     . HOH C 3 .   ? 0.449   -1.094  -39.449 1.00 28.48  ? 675 HOH A O     1 
HETATM 3730 O O     . HOH C 3 .   ? -7.630  22.871  -15.243 1.00 42.51  ? 676 HOH A O     1 
HETATM 3731 O O     . HOH C 3 .   ? -15.049 24.439  -13.122 1.00 41.61  ? 677 HOH A O     1 
HETATM 3732 O O     . HOH C 3 .   ? -13.520 12.562  -49.271 1.00 29.98  ? 678 HOH A O     1 
HETATM 3733 O O     . HOH C 3 .   ? -20.399 5.201   -27.601 1.00 31.62  ? 679 HOH A O     1 
HETATM 3734 O O     . HOH C 3 .   ? -21.592 -1.957  -32.996 1.00 37.46  ? 680 HOH A O     1 
HETATM 3735 O O     . HOH C 3 .   ? -11.320 11.320  -50.925 0.50 25.65  ? 681 HOH A O     1 
HETATM 3736 O O     . HOH C 3 .   ? 9.202   -4.028  -28.890 1.00 25.74  ? 682 HOH A O     1 
HETATM 3737 O O     . HOH C 3 .   ? 6.042   7.030   -28.426 1.00 32.43  ? 683 HOH A O     1 
HETATM 3738 O O     . HOH C 3 .   ? -3.618  15.470  -32.973 1.00 33.85  ? 684 HOH A O     1 
HETATM 3739 O O     . HOH C 3 .   ? -11.744 6.351   -28.833 1.00 28.07  ? 685 HOH A O     1 
HETATM 3740 O O     . HOH C 3 .   ? -20.398 -16.854 -26.951 1.00 37.85  ? 686 HOH A O     1 
HETATM 3741 O O     . HOH C 3 .   ? 8.967   12.785  -19.724 1.00 39.21  ? 687 HOH A O     1 
HETATM 3742 O O     . HOH C 3 .   ? -19.138 14.213  -20.721 1.00 41.08  ? 688 HOH A O     1 
HETATM 3743 O O     . HOH C 3 .   ? 14.055  -18.488 -21.100 1.00 32.28  ? 689 HOH A O     1 
HETATM 3744 O O     . HOH C 3 .   ? -1.522  0.547   -23.050 1.00 38.08  ? 690 HOH A O     1 
HETATM 3745 O O     . HOH C 3 .   ? -14.601 -9.769  -14.349 1.00 29.88  ? 691 HOH A O     1 
HETATM 3746 O O     . HOH C 3 .   ? -22.702 -0.603  -20.499 1.00 30.73  ? 692 HOH A O     1 
HETATM 3747 O O     . HOH C 3 .   ? 2.608   1.324   -10.639 1.00 29.22  ? 693 HOH A O     1 
HETATM 3748 O O     . HOH C 3 .   ? 22.079  -5.339  -24.302 1.00 40.44  ? 694 HOH A O     1 
HETATM 3749 O O     . HOH C 3 .   ? 10.879  2.395   -30.356 1.00 25.80  ? 695 HOH A O     1 
HETATM 3750 O O     . HOH C 3 .   ? 3.170   1.880   -35.187 1.00 41.47  ? 696 HOH A O     1 
HETATM 3751 O O     . HOH C 3 .   ? -7.603  3.494   -59.245 1.00 30.04  ? 697 HOH A O     1 
HETATM 3752 O O     . HOH C 3 .   ? -8.067  -14.033 -19.662 1.00 29.89  ? 698 HOH A O     1 
HETATM 3753 O O     . HOH C 3 .   ? 1.699   -5.713  -15.376 1.00 30.33  ? 699 HOH A O     1 
HETATM 3754 O O     . HOH C 3 .   ? -19.471 8.231   -32.118 1.00 28.71  ? 700 HOH A O     1 
HETATM 3755 O O     . HOH C 3 .   ? -24.778 -3.965  -18.225 1.00 49.94  ? 701 HOH A O     1 
HETATM 3756 O O     . HOH C 3 .   ? 2.756   -9.648  -52.336 1.00 34.65  ? 702 HOH A O     1 
HETATM 3757 O O     . HOH C 3 .   ? 11.671  -12.704 -28.771 1.00 44.22  ? 703 HOH A O     1 
HETATM 3758 O O     . HOH C 3 .   ? -22.295 -10.299 -26.921 1.00 37.97  ? 704 HOH A O     1 
HETATM 3759 O O     . HOH C 3 .   ? -27.428 7.850   -41.788 1.00 46.41  ? 705 HOH A O     1 
HETATM 3760 O O     . HOH C 3 .   ? -9.991  -14.042 -28.298 1.00 31.16  ? 706 HOH A O     1 
HETATM 3761 O O     . HOH C 3 .   ? -11.873 -13.598 -17.163 1.00 33.09  ? 707 HOH A O     1 
HETATM 3762 O O     . HOH C 3 .   ? -10.751 -10.777 -43.426 1.00 33.81  ? 708 HOH A O     1 
HETATM 3763 O O     . HOH C 3 .   ? -3.933  -4.476  -19.139 1.00 24.28  ? 709 HOH A O     1 
HETATM 3764 O O     . HOH C 3 .   ? -22.040 4.249   -19.974 1.00 35.93  ? 710 HOH A O     1 
HETATM 3765 O O     . HOH C 3 .   ? -16.228 -2.636  -51.116 1.00 41.85  ? 711 HOH A O     1 
HETATM 3766 O O     . HOH C 3 .   ? -22.488 1.892   -18.929 1.00 35.68  ? 712 HOH A O     1 
HETATM 3767 O O     . HOH C 3 .   ? -2.987  6.821   -39.649 1.00 32.39  ? 713 HOH A O     1 
HETATM 3768 O O     . HOH C 3 .   ? 1.124   -17.206 -23.670 1.00 41.05  ? 714 HOH A O     1 
HETATM 3769 O O     . HOH C 3 .   ? 4.133   -4.562  -43.751 1.00 28.44  ? 715 HOH A O     1 
HETATM 3770 O O     . HOH C 3 .   ? 4.324   -3.005  -32.033 1.00 38.21  ? 716 HOH A O     1 
HETATM 3771 O O     . HOH C 3 .   ? 5.297   -13.755 -27.428 1.00 31.99  ? 717 HOH A O     1 
HETATM 3772 O O     . HOH C 3 .   ? 17.162  -16.604 -25.159 1.00 33.69  ? 718 HOH A O     1 
HETATM 3773 O O     . HOH C 3 .   ? 0.323   -10.252 -45.691 1.00 30.85  ? 719 HOH A O     1 
HETATM 3774 O O     . HOH C 3 .   ? -22.522 -2.797  -18.639 1.00 33.04  ? 720 HOH A O     1 
HETATM 3775 O O     . HOH C 3 .   ? -18.453 -14.159 -18.173 1.00 39.79  ? 721 HOH A O     1 
HETATM 3776 O O     . HOH C 3 .   ? 7.337   -12.902 -12.130 1.00 39.71  ? 722 HOH A O     1 
HETATM 3777 O O     . HOH C 3 .   ? -4.430  17.383  -31.123 1.00 29.43  ? 723 HOH A O     1 
HETATM 3778 O O     . HOH C 3 .   ? 2.049   15.931  -20.445 1.00 33.35  ? 724 HOH A O     1 
HETATM 3779 O O     . HOH C 3 .   ? -11.584 -5.144  -39.060 1.00 30.95  ? 725 HOH A O     1 
HETATM 3780 O O     . HOH C 3 .   ? 0.064   -8.203  -26.931 1.00 38.05  ? 726 HOH A O     1 
HETATM 3781 O O     . HOH C 3 .   ? -21.375 9.258   -50.931 1.00 36.91  ? 727 HOH A O     1 
HETATM 3782 O O     . HOH C 3 .   ? 4.624   -5.356  -30.834 1.00 28.91  ? 728 HOH A O     1 
HETATM 3783 O O     . HOH C 3 .   ? -1.284  -1.207  -25.328 1.00 30.30  ? 729 HOH A O     1 
HETATM 3784 O O     . HOH C 3 .   ? -10.598 1.155   -38.194 1.00 30.72  ? 730 HOH A O     1 
HETATM 3785 O O     . HOH C 3 .   ? -3.044  -3.250  -26.947 1.00 27.42  ? 731 HOH A O     1 
HETATM 3786 O O     . HOH C 3 .   ? -8.896  -7.833  -34.219 1.00 27.42  ? 732 HOH A O     1 
HETATM 3787 O O     . HOH C 3 .   ? -1.607  -1.860  -12.984 1.00 34.52  ? 733 HOH A O     1 
HETATM 3788 O O     . HOH C 3 .   ? -22.718 4.179   -15.689 1.00 42.63  ? 734 HOH A O     1 
HETATM 3789 O O     . HOH C 3 .   ? -18.203 -3.831  -48.208 1.00 35.35  ? 735 HOH A O     1 
HETATM 3790 O O     . HOH C 3 .   ? -14.184 10.202  -38.148 1.00 27.41  ? 736 HOH A O     1 
HETATM 3791 O O     . HOH C 3 .   ? -3.918  -14.792 -19.605 1.00 41.04  ? 737 HOH A O     1 
HETATM 3792 O O     . HOH C 3 .   ? -6.123  15.335  -40.720 1.00 32.08  ? 738 HOH A O     1 
HETATM 3793 O O     . HOH C 3 .   ? 0.405   20.364  -17.586 1.00 44.24  ? 739 HOH A O     1 
HETATM 3794 O O     . HOH C 3 .   ? -3.666  -10.596 -9.794  1.00 49.87  ? 740 HOH A O     1 
HETATM 3795 O O     . HOH C 3 .   ? -6.402  -4.794  -13.443 1.00 36.50  ? 741 HOH A O     1 
HETATM 3796 O O     . HOH C 3 .   ? 0.256   13.874  -5.713  1.00 41.18  ? 742 HOH A O     1 
HETATM 3797 O O     . HOH C 3 .   ? -0.151  4.086   -39.317 1.00 40.34  ? 743 HOH A O     1 
HETATM 3798 O O     . HOH C 3 .   ? -0.090  4.165   -5.639  1.00 30.61  ? 744 HOH A O     1 
HETATM 3799 O O     . HOH C 3 .   ? -5.978  23.278  -25.918 1.00 41.93  ? 745 HOH A O     1 
HETATM 3800 O O     . HOH C 3 .   ? -33.799 -16.579 -34.651 1.00 41.42  ? 746 HOH A O     1 
HETATM 3801 O O     . HOH C 3 .   ? 8.386   -6.102  -31.718 1.00 36.56  ? 747 HOH A O     1 
HETATM 3802 O O     . HOH C 3 .   ? -8.043  5.984   1.152   1.00 50.42  ? 748 HOH A O     1 
HETATM 3803 O O     . HOH C 3 .   ? -29.301 5.415   -15.717 1.00 42.37  ? 749 HOH A O     1 
HETATM 3804 O O     . HOH C 3 .   ? 22.816  -4.791  -20.121 1.00 40.87  ? 750 HOH A O     1 
HETATM 3805 O O     . HOH C 3 .   ? 0.859   -2.653  -12.045 1.00 35.86  ? 751 HOH A O     1 
HETATM 3806 O O     . HOH C 3 .   ? 1.239   -8.975  -22.454 1.00 31.56  ? 752 HOH A O     1 
HETATM 3807 O O     . HOH C 3 .   ? -12.561 2.206   -35.903 1.00 24.61  ? 753 HOH A O     1 
HETATM 3808 O O     . HOH C 3 .   ? -12.202 20.603  -35.848 1.00 54.30  ? 754 HOH A O     1 
HETATM 3809 O O     . HOH C 3 .   ? 15.249  -7.598  -29.720 1.00 38.58  ? 755 HOH A O     1 
HETATM 3810 O O     . HOH C 3 .   ? 7.614   12.809  -21.974 1.00 39.81  ? 756 HOH A O     1 
HETATM 3811 O O     . HOH C 3 .   ? 9.040   15.327  -18.770 1.00 52.29  ? 757 HOH A O     1 
HETATM 3812 O O     . HOH C 3 .   ? 5.943   14.050  -14.953 1.00 29.67  ? 758 HOH A O     1 
HETATM 3813 O O     . HOH C 3 .   ? 5.009   -8.577  -45.487 1.00 44.77  ? 759 HOH A O     1 
HETATM 3814 O O     . HOH C 3 .   ? 8.800   11.276  -23.633 1.00 36.37  ? 760 HOH A O     1 
HETATM 3815 O O     . HOH C 3 .   ? -26.724 -3.386  -19.288 1.00 55.73  ? 761 HOH A O     1 
HETATM 3816 O O     . HOH C 3 .   ? -0.742  10.291  -37.543 1.00 37.80  ? 762 HOH A O     1 
HETATM 3817 O O     . HOH C 3 .   ? 3.140   -1.199  -11.492 1.00 28.60  ? 763 HOH A O     1 
HETATM 3818 O O     . HOH C 3 .   ? 9.740   3.358   -32.788 1.00 36.60  ? 764 HOH A O     1 
HETATM 3819 O O     . HOH C 3 .   ? -20.467 -5.619  -10.499 1.00 45.33  ? 765 HOH A O     1 
HETATM 3820 O O     . HOH C 3 .   ? -3.448  15.520  -40.780 1.00 37.25  ? 766 HOH A O     1 
HETATM 3821 O O     . HOH C 3 .   ? -4.639  2.284   -33.254 1.00 31.20  ? 767 HOH A O     1 
HETATM 3822 O O     . HOH C 3 .   ? 4.266   -1.120  -38.066 1.00 38.73  ? 768 HOH A O     1 
HETATM 3823 O O     . HOH C 3 .   ? -8.067  0.650   -62.363 1.00 34.69  ? 769 HOH A O     1 
HETATM 3824 O O     . HOH C 3 .   ? 6.080   2.130   -35.507 1.00 40.21  ? 770 HOH A O     1 
HETATM 3825 O O     . HOH C 3 .   ? 10.365  -8.518  -28.521 1.00 43.51  ? 771 HOH A O     1 
# 
