data_9FSH
# 
_entry.id   9FSH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9FSH         pdb_00009fsh 10.2210/pdb9fsh/pdb 
WWPDB D_1292139635 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-16 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FSH 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-21 
_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              nils.ostermann@novartis.com 
_pdbx_contact_author.name_first         Nils 
_pdbx_contact_author.name_last          Ostermann 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3391-1228 
# 
_audit_author.name               'Ostermann, N.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-3391-1228 
# 
_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            Cell 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1097-4172 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            188 
_citation.language                  ? 
_citation.page_first                2603 
_citation.page_last                 ? 
_citation.title                     'Therapeutic potential of allosteric HECT E3 ligase inhibition.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.cell.2025.03.001 
_citation.pdbx_database_id_PubMed   40179885 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rothman, A.M.K.'  1  ? 
primary 'Florentin, A.'    2  ? 
primary 'Zink, F.'         3  ? 
primary 'Quigley, C.'      4  ? 
primary 'Bonneau, O.'      5  ? 
primary 'Hemmig, R.'       6  ? 
primary 'Hachey, A.'       7  ? 
primary 'Rejtar, T.'       8  ? 
primary 'Thaker, M.'       9  ? 
primary 'Jain, R.'         10 ? 
primary 'Huang, S.M.'      11 ? 
primary 'Sutton, D.'       12 ? 
primary 'Roger, J.'        13 ? 
primary 'Zhang, J.H.'      14 ? 
primary 'Weiler, S.'       15 ? 
primary 'Cotesta, S.'      16 ? 
primary 'Ottl, J.'         17 ? 
primary 'Srivastava, S.'   18 ? 
primary 'Kordonsky, A.'    19 ? 
primary 'Avishid, R.'      20 ? 
primary 'Yariv, E.'        21 ? 
primary 'Rathi, R.'        22 ? 
primary 'Khvalevsky, O.'   23 ? 
primary 'Troxler, T.'      24 ? 
primary 'Binmahfooz, S.K.' 25 ? 
primary 'Kleifeld, O.'     26 ? 
primary 'Morrell, N.W.'    27 ? 
primary 'Humbert, M.'      28 ? 
primary 'Thomas, M.J.'     29 ? 
primary 'Jarai, G.'        30 ? 
primary 'Beckwith, R.E.J.' 31 ? 
primary 'Cobb, J.S.'       32 ? 
primary 'Smith, N.'        33 ? 
primary 'Ostermann, N.'    34 ? 
primary 'Tallarico, J.'    35 ? 
primary 'Shaw, D.'         36 ? 
primary 'Guth-Gundel, S.'  37 ? 
primary 'Prag, G.'         38 ? 
primary 'Rowlands, D.J.'   39 ? 
# 
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 'E3 ubiquitin-protein ligase SMURF2'                                                            58203.914 1   
2.3.2.26 ? ? ? 
2 non-polymer syn 'ethyl 5-[1,3-benzodioxol-5-ylmethyl(ethyl)carbamoyl]-2,4-dimethyl-1~{H}-pyrrole-3-carboxylate' 372.415   1   ? 
? ? ? 
3 non-polymer syn 'PHOSPHATE ION'                                                                                 94.971    1   ? 
? ? ? 
4 water       nat water                                                                                           18.015    217 ? 
? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;hSMURF2,HECT-type E3 ubiquitin transferase SMURF2,SMAD ubiquitination regulatory factor 2,SMAD-specific E3 ubiquitin-protein ligase 2
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPR
LSANLHLVLNRQNQLKDQQQQQVVSLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQ
VMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRI
MGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGK
SIPVNEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVNDWKVNTRLKHCTPD
SNIVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYE
KLYEKLLTAIEETCGFAVE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPR
LSANLHLVLNRQNQLKDQQQQQVVSLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQ
VMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRI
MGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGK
SIPVNEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVNDWKVNTRLKHCTPD
SNIVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYE
KLYEKLLTAIEETCGFAVE
;
_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 'ethyl 5-[1,3-benzodioxol-5-ylmethyl(ethyl)carbamoyl]-2,4-dimethyl-1~{H}-pyrrole-3-carboxylate' TJQ 
3 'PHOSPHATE ION'                                                                                 PO4 
4 water                                                                                           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   ASP n 
1 4   LEU n 
1 5   PRO n 
1 6   GLU n 
1 7   GLY n 
1 8   TYR n 
1 9   GLU n 
1 10  GLN n 
1 11  ARG n 
1 12  THR n 
1 13  THR n 
1 14  GLN n 
1 15  GLN n 
1 16  GLY n 
1 17  GLN n 
1 18  VAL n 
1 19  TYR n 
1 20  PHE n 
1 21  LEU n 
1 22  HIS n 
1 23  THR n 
1 24  GLN n 
1 25  THR n 
1 26  GLY n 
1 27  VAL n 
1 28  SER n 
1 29  THR n 
1 30  TRP n 
1 31  HIS n 
1 32  ASP n 
1 33  PRO n 
1 34  ARG n 
1 35  VAL n 
1 36  PRO n 
1 37  ARG n 
1 38  ASP n 
1 39  LEU n 
1 40  SER n 
1 41  ASN n 
1 42  ILE n 
1 43  ASN n 
1 44  CYS n 
1 45  GLU n 
1 46  GLU n 
1 47  LEU n 
1 48  GLY n 
1 49  PRO n 
1 50  LEU n 
1 51  PRO n 
1 52  PRO n 
1 53  GLY n 
1 54  TRP n 
1 55  GLU n 
1 56  ILE n 
1 57  ARG n 
1 58  ASN n 
1 59  THR n 
1 60  ALA n 
1 61  THR n 
1 62  GLY n 
1 63  ARG n 
1 64  VAL n 
1 65  TYR n 
1 66  PHE n 
1 67  VAL n 
1 68  ASP n 
1 69  HIS n 
1 70  ASN n 
1 71  ASN n 
1 72  ARG n 
1 73  THR n 
1 74  THR n 
1 75  GLN n 
1 76  PHE n 
1 77  THR n 
1 78  ASP n 
1 79  PRO n 
1 80  ARG n 
1 81  LEU n 
1 82  SER n 
1 83  ALA n 
1 84  ASN n 
1 85  LEU n 
1 86  HIS n 
1 87  LEU n 
1 88  VAL n 
1 89  LEU n 
1 90  ASN n 
1 91  ARG n 
1 92  GLN n 
1 93  ASN n 
1 94  GLN n 
1 95  LEU n 
1 96  LYS n 
1 97  ASP n 
1 98  GLN n 
1 99  GLN n 
1 100 GLN n 
1 101 GLN n 
1 102 GLN n 
1 103 VAL n 
1 104 VAL n 
1 105 SER n 
1 106 LEU n 
1 107 CYS n 
1 108 PRO n 
1 109 ASP n 
1 110 ASP n 
1 111 THR n 
1 112 GLU n 
1 113 CYS n 
1 114 LEU n 
1 115 THR n 
1 116 VAL n 
1 117 PRO n 
1 118 ARG n 
1 119 TYR n 
1 120 LYS n 
1 121 ARG n 
1 122 ASP n 
1 123 LEU n 
1 124 VAL n 
1 125 GLN n 
1 126 LYS n 
1 127 LEU n 
1 128 LYS n 
1 129 ILE n 
1 130 LEU n 
1 131 ARG n 
1 132 GLN n 
1 133 GLU n 
1 134 LEU n 
1 135 SER n 
1 136 GLN n 
1 137 GLN n 
1 138 GLN n 
1 139 PRO n 
1 140 GLN n 
1 141 ALA n 
1 142 GLY n 
1 143 HIS n 
1 144 CYS n 
1 145 ARG n 
1 146 ILE n 
1 147 GLU n 
1 148 VAL n 
1 149 SER n 
1 150 ARG n 
1 151 GLU n 
1 152 GLU n 
1 153 ILE n 
1 154 PHE n 
1 155 GLU n 
1 156 GLU n 
1 157 SER n 
1 158 TYR n 
1 159 ARG n 
1 160 GLN n 
1 161 VAL n 
1 162 MET n 
1 163 LYS n 
1 164 MET n 
1 165 ARG n 
1 166 PRO n 
1 167 LYS n 
1 168 ASP n 
1 169 LEU n 
1 170 TRP n 
1 171 LYS n 
1 172 ARG n 
1 173 LEU n 
1 174 MET n 
1 175 ILE n 
1 176 LYS n 
1 177 PHE n 
1 178 ARG n 
1 179 GLY n 
1 180 GLU n 
1 181 GLU n 
1 182 GLY n 
1 183 LEU n 
1 184 ASP n 
1 185 TYR n 
1 186 GLY n 
1 187 GLY n 
1 188 VAL n 
1 189 ALA n 
1 190 ARG n 
1 191 GLU n 
1 192 TRP n 
1 193 LEU n 
1 194 TYR n 
1 195 LEU n 
1 196 LEU n 
1 197 SER n 
1 198 HIS n 
1 199 GLU n 
1 200 MET n 
1 201 LEU n 
1 202 ASN n 
1 203 PRO n 
1 204 TYR n 
1 205 TYR n 
1 206 GLY n 
1 207 LEU n 
1 208 PHE n 
1 209 GLN n 
1 210 TYR n 
1 211 SER n 
1 212 ARG n 
1 213 ASP n 
1 214 ASP n 
1 215 ILE n 
1 216 TYR n 
1 217 THR n 
1 218 LEU n 
1 219 GLN n 
1 220 ILE n 
1 221 ASN n 
1 222 PRO n 
1 223 ASP n 
1 224 SER n 
1 225 ALA n 
1 226 VAL n 
1 227 ASN n 
1 228 PRO n 
1 229 GLU n 
1 230 HIS n 
1 231 LEU n 
1 232 SER n 
1 233 TYR n 
1 234 PHE n 
1 235 HIS n 
1 236 PHE n 
1 237 VAL n 
1 238 GLY n 
1 239 ARG n 
1 240 ILE n 
1 241 MET n 
1 242 GLY n 
1 243 MET n 
1 244 ALA n 
1 245 VAL n 
1 246 PHE n 
1 247 HIS n 
1 248 GLY n 
1 249 HIS n 
1 250 TYR n 
1 251 ILE n 
1 252 ASP n 
1 253 GLY n 
1 254 GLY n 
1 255 PHE n 
1 256 THR n 
1 257 LEU n 
1 258 PRO n 
1 259 PHE n 
1 260 TYR n 
1 261 LYS n 
1 262 GLN n 
1 263 LEU n 
1 264 LEU n 
1 265 GLY n 
1 266 LYS n 
1 267 SER n 
1 268 ILE n 
1 269 THR n 
1 270 LEU n 
1 271 ASP n 
1 272 ASP n 
1 273 MET n 
1 274 GLU n 
1 275 LEU n 
1 276 VAL n 
1 277 ASP n 
1 278 PRO n 
1 279 ASP n 
1 280 LEU n 
1 281 HIS n 
1 282 ASN n 
1 283 SER n 
1 284 LEU n 
1 285 VAL n 
1 286 TRP n 
1 287 ILE n 
1 288 LEU n 
1 289 GLU n 
1 290 ASN n 
1 291 ASP n 
1 292 ILE n 
1 293 THR n 
1 294 GLY n 
1 295 VAL n 
1 296 LEU n 
1 297 ASP n 
1 298 HIS n 
1 299 THR n 
1 300 PHE n 
1 301 CYS n 
1 302 VAL n 
1 303 GLU n 
1 304 HIS n 
1 305 ASN n 
1 306 ALA n 
1 307 TYR n 
1 308 GLY n 
1 309 GLU n 
1 310 ILE n 
1 311 ILE n 
1 312 GLN n 
1 313 HIS n 
1 314 GLU n 
1 315 LEU n 
1 316 LYS n 
1 317 PRO n 
1 318 ASN n 
1 319 GLY n 
1 320 LYS n 
1 321 SER n 
1 322 ILE n 
1 323 PRO n 
1 324 VAL n 
1 325 ASN n 
1 326 GLU n 
1 327 GLU n 
1 328 ASN n 
1 329 LYS n 
1 330 LYS n 
1 331 GLU n 
1 332 TYR n 
1 333 VAL n 
1 334 ARG n 
1 335 LEU n 
1 336 TYR n 
1 337 VAL n 
1 338 ASN n 
1 339 TRP n 
1 340 ARG n 
1 341 PHE n 
1 342 LEU n 
1 343 ARG n 
1 344 GLY n 
1 345 ILE n 
1 346 GLU n 
1 347 ALA n 
1 348 GLN n 
1 349 PHE n 
1 350 LEU n 
1 351 ALA n 
1 352 LEU n 
1 353 GLN n 
1 354 LYS n 
1 355 GLY n 
1 356 PHE n 
1 357 ASN n 
1 358 GLU n 
1 359 VAL n 
1 360 ILE n 
1 361 PRO n 
1 362 GLN n 
1 363 HIS n 
1 364 LEU n 
1 365 LEU n 
1 366 LYS n 
1 367 THR n 
1 368 PHE n 
1 369 ASP n 
1 370 GLU n 
1 371 LYS n 
1 372 GLU n 
1 373 LEU n 
1 374 GLU n 
1 375 LEU n 
1 376 ILE n 
1 377 ILE n 
1 378 CYS n 
1 379 GLY n 
1 380 LEU n 
1 381 GLY n 
1 382 LYS n 
1 383 ILE n 
1 384 ASP n 
1 385 VAL n 
1 386 ASN n 
1 387 ASP n 
1 388 TRP n 
1 389 LYS n 
1 390 VAL n 
1 391 ASN n 
1 392 THR n 
1 393 ARG n 
1 394 LEU n 
1 395 LYS n 
1 396 HIS n 
1 397 CYS n 
1 398 THR n 
1 399 PRO n 
1 400 ASP n 
1 401 SER n 
1 402 ASN n 
1 403 ILE n 
1 404 VAL n 
1 405 LYS n 
1 406 TRP n 
1 407 PHE n 
1 408 TRP n 
1 409 LYS n 
1 410 ALA n 
1 411 VAL n 
1 412 GLU n 
1 413 PHE n 
1 414 PHE n 
1 415 ASP n 
1 416 GLU n 
1 417 GLU n 
1 418 ARG n 
1 419 ARG n 
1 420 ALA n 
1 421 ARG n 
1 422 LEU n 
1 423 LEU n 
1 424 GLN n 
1 425 PHE n 
1 426 VAL n 
1 427 THR n 
1 428 GLY n 
1 429 SER n 
1 430 SER n 
1 431 ARG n 
1 432 VAL n 
1 433 PRO n 
1 434 LEU n 
1 435 GLN n 
1 436 GLY n 
1 437 PHE n 
1 438 LYS n 
1 439 ALA n 
1 440 LEU n 
1 441 GLN n 
1 442 GLY n 
1 443 ALA n 
1 444 ALA n 
1 445 GLY n 
1 446 PRO n 
1 447 ARG n 
1 448 LEU n 
1 449 PHE n 
1 450 THR n 
1 451 ILE n 
1 452 HIS n 
1 453 GLN n 
1 454 ILE n 
1 455 ASP n 
1 456 ALA n 
1 457 CYS n 
1 458 THR n 
1 459 ASN n 
1 460 ASN n 
1 461 LEU n 
1 462 PRO n 
1 463 LYS n 
1 464 ALA n 
1 465 HIS n 
1 466 THR n 
1 467 CYS n 
1 468 PHE n 
1 469 ASN n 
1 470 ARG n 
1 471 ILE n 
1 472 ASP n 
1 473 ILE n 
1 474 PRO n 
1 475 PRO n 
1 476 TYR n 
1 477 GLU n 
1 478 SER n 
1 479 TYR n 
1 480 GLU n 
1 481 LYS n 
1 482 LEU n 
1 483 TYR n 
1 484 GLU n 
1 485 LYS n 
1 486 LEU n 
1 487 LEU n 
1 488 THR n 
1 489 ALA n 
1 490 ILE n 
1 491 GLU n 
1 492 GLU n 
1 493 THR n 
1 494 CYS n 
1 495 GLY n 
1 496 PHE n 
1 497 ALA n 
1 498 VAL n 
1 499 GLU 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                   499 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SMURF2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                         ? 
'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                                                        ? 
'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                      ? 
'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                                 ? 
'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                                        ? 
'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                                       ? 
'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                 ? 
'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                                                         ? 
'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                       ? 
'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                                                           ? 'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                      ? 
'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                         ? 
'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                                                          ? 
'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                                                      ? 
'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                                   ? 
'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION'                                                                                 ? 
'O4 P -3'        94.971  
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 
TJQ non-polymer         . 'ethyl 5-[1,3-benzodioxol-5-ylmethyl(ethyl)carbamoyl]-2,4-dimethyl-1~{H}-pyrrole-3-carboxylate' ? 
'C20 H24 N2 O5'  372.415 
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   GLY 1   250 ?   ?   ?   A . n 
A 1 2   PRO 2   251 ?   ?   ?   A . n 
A 1 3   ASP 3   252 ?   ?   ?   A . n 
A 1 4   LEU 4   253 ?   ?   ?   A . n 
A 1 5   PRO 5   254 ?   ?   ?   A . n 
A 1 6   GLU 6   255 ?   ?   ?   A . n 
A 1 7   GLY 7   256 ?   ?   ?   A . n 
A 1 8   TYR 8   257 ?   ?   ?   A . n 
A 1 9   GLU 9   258 ?   ?   ?   A . n 
A 1 10  GLN 10  259 ?   ?   ?   A . n 
A 1 11  ARG 11  260 ?   ?   ?   A . n 
A 1 12  THR 12  261 ?   ?   ?   A . n 
A 1 13  THR 13  262 ?   ?   ?   A . n 
A 1 14  GLN 14  263 ?   ?   ?   A . n 
A 1 15  GLN 15  264 ?   ?   ?   A . n 
A 1 16  GLY 16  265 ?   ?   ?   A . n 
A 1 17  GLN 17  266 ?   ?   ?   A . n 
A 1 18  VAL 18  267 ?   ?   ?   A . n 
A 1 19  TYR 19  268 ?   ?   ?   A . n 
A 1 20  PHE 20  269 ?   ?   ?   A . n 
A 1 21  LEU 21  270 ?   ?   ?   A . n 
A 1 22  HIS 22  271 ?   ?   ?   A . n 
A 1 23  THR 23  272 ?   ?   ?   A . n 
A 1 24  GLN 24  273 ?   ?   ?   A . n 
A 1 25  THR 25  274 ?   ?   ?   A . n 
A 1 26  GLY 26  275 ?   ?   ?   A . n 
A 1 27  VAL 27  276 ?   ?   ?   A . n 
A 1 28  SER 28  277 ?   ?   ?   A . n 
A 1 29  THR 29  278 ?   ?   ?   A . n 
A 1 30  TRP 30  279 ?   ?   ?   A . n 
A 1 31  HIS 31  280 ?   ?   ?   A . n 
A 1 32  ASP 32  281 ?   ?   ?   A . n 
A 1 33  PRO 33  282 ?   ?   ?   A . n 
A 1 34  ARG 34  283 ?   ?   ?   A . n 
A 1 35  VAL 35  284 ?   ?   ?   A . n 
A 1 36  PRO 36  285 ?   ?   ?   A . n 
A 1 37  ARG 37  286 ?   ?   ?   A . n 
A 1 38  ASP 38  287 ?   ?   ?   A . n 
A 1 39  LEU 39  288 ?   ?   ?   A . n 
A 1 40  SER 40  289 ?   ?   ?   A . n 
A 1 41  ASN 41  290 ?   ?   ?   A . n 
A 1 42  ILE 42  291 ?   ?   ?   A . n 
A 1 43  ASN 43  292 ?   ?   ?   A . n 
A 1 44  CYS 44  293 ?   ?   ?   A . n 
A 1 45  GLU 45  294 ?   ?   ?   A . n 
A 1 46  GLU 46  295 ?   ?   ?   A . n 
A 1 47  LEU 47  296 ?   ?   ?   A . n 
A 1 48  GLY 48  297 ?   ?   ?   A . n 
A 1 49  PRO 49  298 ?   ?   ?   A . n 
A 1 50  LEU 50  299 ?   ?   ?   A . n 
A 1 51  PRO 51  300 ?   ?   ?   A . n 
A 1 52  PRO 52  301 ?   ?   ?   A . n 
A 1 53  GLY 53  302 ?   ?   ?   A . n 
A 1 54  TRP 54  303 ?   ?   ?   A . n 
A 1 55  GLU 55  304 ?   ?   ?   A . n 
A 1 56  ILE 56  305 ?   ?   ?   A . n 
A 1 57  ARG 57  306 ?   ?   ?   A . n 
A 1 58  ASN 58  307 ?   ?   ?   A . n 
A 1 59  THR 59  308 ?   ?   ?   A . n 
A 1 60  ALA 60  309 ?   ?   ?   A . n 
A 1 61  THR 61  310 ?   ?   ?   A . n 
A 1 62  GLY 62  311 ?   ?   ?   A . n 
A 1 63  ARG 63  312 ?   ?   ?   A . n 
A 1 64  VAL 64  313 ?   ?   ?   A . n 
A 1 65  TYR 65  314 ?   ?   ?   A . n 
A 1 66  PHE 66  315 ?   ?   ?   A . n 
A 1 67  VAL 67  316 ?   ?   ?   A . n 
A 1 68  ASP 68  317 ?   ?   ?   A . n 
A 1 69  HIS 69  318 ?   ?   ?   A . n 
A 1 70  ASN 70  319 ?   ?   ?   A . n 
A 1 71  ASN 71  320 ?   ?   ?   A . n 
A 1 72  ARG 72  321 ?   ?   ?   A . n 
A 1 73  THR 73  322 ?   ?   ?   A . n 
A 1 74  THR 74  323 ?   ?   ?   A . n 
A 1 75  GLN 75  324 ?   ?   ?   A . n 
A 1 76  PHE 76  325 ?   ?   ?   A . n 
A 1 77  THR 77  326 ?   ?   ?   A . n 
A 1 78  ASP 78  327 ?   ?   ?   A . n 
A 1 79  PRO 79  328 ?   ?   ?   A . n 
A 1 80  ARG 80  329 ?   ?   ?   A . n 
A 1 81  LEU 81  330 ?   ?   ?   A . n 
A 1 82  SER 82  331 ?   ?   ?   A . n 
A 1 83  ALA 83  332 ?   ?   ?   A . n 
A 1 84  ASN 84  333 ?   ?   ?   A . n 
A 1 85  LEU 85  334 ?   ?   ?   A . n 
A 1 86  HIS 86  335 ?   ?   ?   A . n 
A 1 87  LEU 87  336 ?   ?   ?   A . n 
A 1 88  VAL 88  337 ?   ?   ?   A . n 
A 1 89  LEU 89  338 ?   ?   ?   A . n 
A 1 90  ASN 90  339 ?   ?   ?   A . n 
A 1 91  ARG 91  340 ?   ?   ?   A . n 
A 1 92  GLN 92  341 ?   ?   ?   A . n 
A 1 93  ASN 93  342 ?   ?   ?   A . n 
A 1 94  GLN 94  343 ?   ?   ?   A . n 
A 1 95  LEU 95  344 ?   ?   ?   A . n 
A 1 96  LYS 96  345 ?   ?   ?   A . n 
A 1 97  ASP 97  346 ?   ?   ?   A . n 
A 1 98  GLN 98  347 ?   ?   ?   A . n 
A 1 99  GLN 99  348 ?   ?   ?   A . n 
A 1 100 GLN 100 349 ?   ?   ?   A . n 
A 1 101 GLN 101 350 ?   ?   ?   A . n 
A 1 102 GLN 102 351 ?   ?   ?   A . n 
A 1 103 VAL 103 352 ?   ?   ?   A . n 
A 1 104 VAL 104 353 ?   ?   ?   A . n 
A 1 105 SER 105 354 ?   ?   ?   A . n 
A 1 106 LEU 106 355 ?   ?   ?   A . n 
A 1 107 CYS 107 356 ?   ?   ?   A . n 
A 1 108 PRO 108 357 ?   ?   ?   A . n 
A 1 109 ASP 109 358 ?   ?   ?   A . n 
A 1 110 ASP 110 359 ?   ?   ?   A . n 
A 1 111 THR 111 360 ?   ?   ?   A . n 
A 1 112 GLU 112 361 ?   ?   ?   A . n 
A 1 113 CYS 113 362 ?   ?   ?   A . n 
A 1 114 LEU 114 363 ?   ?   ?   A . n 
A 1 115 THR 115 364 ?   ?   ?   A . n 
A 1 116 VAL 116 365 ?   ?   ?   A . n 
A 1 117 PRO 117 366 ?   ?   ?   A . n 
A 1 118 ARG 118 367 ?   ?   ?   A . n 
A 1 119 TYR 119 368 ?   ?   ?   A . n 
A 1 120 LYS 120 369 369 LYS LYS A . n 
A 1 121 ARG 121 370 370 ARG ARG A . n 
A 1 122 ASP 122 371 371 ASP ASP A . n 
A 1 123 LEU 123 372 372 LEU LEU A . n 
A 1 124 VAL 124 373 373 VAL VAL A . n 
A 1 125 GLN 125 374 374 GLN GLN A . n 
A 1 126 LYS 126 375 375 LYS LYS A . n 
A 1 127 LEU 127 376 376 LEU LEU A . n 
A 1 128 LYS 128 377 377 LYS LYS A . n 
A 1 129 ILE 129 378 378 ILE ILE A . n 
A 1 130 LEU 130 379 379 LEU LEU A . n 
A 1 131 ARG 131 380 380 ARG ARG A . n 
A 1 132 GLN 132 381 381 GLN GLN A . n 
A 1 133 GLU 133 382 382 GLU GLU A . n 
A 1 134 LEU 134 383 383 LEU LEU A . n 
A 1 135 SER 135 384 384 SER SER A . n 
A 1 136 GLN 136 385 385 GLN GLN A . n 
A 1 137 GLN 137 386 386 GLN GLN A . n 
A 1 138 GLN 138 387 387 GLN GLN A . n 
A 1 139 PRO 139 388 388 PRO PRO A . n 
A 1 140 GLN 140 389 389 GLN GLN A . n 
A 1 141 ALA 141 390 390 ALA ALA A . n 
A 1 142 GLY 142 391 391 GLY GLY A . n 
A 1 143 HIS 143 392 392 HIS HIS A . n 
A 1 144 CYS 144 393 393 CYS CYS A . n 
A 1 145 ARG 145 394 394 ARG ARG A . n 
A 1 146 ILE 146 395 395 ILE ILE A . n 
A 1 147 GLU 147 396 396 GLU GLU A . n 
A 1 148 VAL 148 397 397 VAL VAL A . n 
A 1 149 SER 149 398 398 SER SER A . n 
A 1 150 ARG 150 399 399 ARG ARG A . n 
A 1 151 GLU 151 400 400 GLU GLU A . n 
A 1 152 GLU 152 401 401 GLU GLU A . n 
A 1 153 ILE 153 402 402 ILE ILE A . n 
A 1 154 PHE 154 403 403 PHE PHE A . n 
A 1 155 GLU 155 404 404 GLU GLU A . n 
A 1 156 GLU 156 405 405 GLU GLU A . n 
A 1 157 SER 157 406 406 SER SER A . n 
A 1 158 TYR 158 407 407 TYR TYR A . n 
A 1 159 ARG 159 408 408 ARG ARG A . n 
A 1 160 GLN 160 409 409 GLN GLN A . n 
A 1 161 VAL 161 410 410 VAL VAL A . n 
A 1 162 MET 162 411 411 MET MET A . n 
A 1 163 LYS 163 412 412 LYS LYS A . n 
A 1 164 MET 164 413 413 MET MET A . n 
A 1 165 ARG 165 414 414 ARG ARG A . n 
A 1 166 PRO 166 415 415 PRO PRO A . n 
A 1 167 LYS 167 416 416 LYS LYS A . n 
A 1 168 ASP 168 417 417 ASP ASP A . n 
A 1 169 LEU 169 418 418 LEU LEU A . n 
A 1 170 TRP 170 419 419 TRP TRP A . n 
A 1 171 LYS 171 420 420 LYS LYS A . n 
A 1 172 ARG 172 421 421 ARG ARG A . n 
A 1 173 LEU 173 422 422 LEU LEU A . n 
A 1 174 MET 174 423 423 MET MET A . n 
A 1 175 ILE 175 424 424 ILE ILE A . n 
A 1 176 LYS 176 425 425 LYS LYS A . n 
A 1 177 PHE 177 426 426 PHE PHE A . n 
A 1 178 ARG 178 427 427 ARG ARG A . n 
A 1 179 GLY 179 428 428 GLY GLY A . n 
A 1 180 GLU 180 429 429 GLU GLU A . n 
A 1 181 GLU 181 430 430 GLU GLU A . n 
A 1 182 GLY 182 431 431 GLY GLY A . n 
A 1 183 LEU 183 432 432 LEU LEU A . n 
A 1 184 ASP 184 433 433 ASP ASP A . n 
A 1 185 TYR 185 434 434 TYR TYR A . n 
A 1 186 GLY 186 435 435 GLY GLY A . n 
A 1 187 GLY 187 436 436 GLY GLY A . n 
A 1 188 VAL 188 437 437 VAL VAL A . n 
A 1 189 ALA 189 438 438 ALA ALA A . n 
A 1 190 ARG 190 439 439 ARG ARG A . n 
A 1 191 GLU 191 440 440 GLU GLU A . n 
A 1 192 TRP 192 441 441 TRP TRP A . n 
A 1 193 LEU 193 442 442 LEU LEU A . n 
A 1 194 TYR 194 443 443 TYR TYR A . n 
A 1 195 LEU 195 444 444 LEU LEU A . n 
A 1 196 LEU 196 445 445 LEU LEU A . n 
A 1 197 SER 197 446 446 SER SER A . n 
A 1 198 HIS 198 447 447 HIS HIS A . n 
A 1 199 GLU 199 448 448 GLU GLU A . n 
A 1 200 MET 200 449 449 MET MET A . n 
A 1 201 LEU 201 450 450 LEU LEU A . n 
A 1 202 ASN 202 451 451 ASN ASN A . n 
A 1 203 PRO 203 452 452 PRO PRO A . n 
A 1 204 TYR 204 453 453 TYR TYR A . n 
A 1 205 TYR 205 454 454 TYR TYR A . n 
A 1 206 GLY 206 455 455 GLY GLY A . n 
A 1 207 LEU 207 456 456 LEU LEU A . n 
A 1 208 PHE 208 457 457 PHE PHE A . n 
A 1 209 GLN 209 458 458 GLN GLN A . n 
A 1 210 TYR 210 459 459 TYR TYR A . n 
A 1 211 SER 211 460 460 SER SER A . n 
A 1 212 ARG 212 461 461 ARG ARG A . n 
A 1 213 ASP 213 462 462 ASP ASP A . n 
A 1 214 ASP 214 463 463 ASP ASP A . n 
A 1 215 ILE 215 464 464 ILE ILE A . n 
A 1 216 TYR 216 465 465 TYR TYR A . n 
A 1 217 THR 217 466 466 THR THR A . n 
A 1 218 LEU 218 467 467 LEU LEU A . n 
A 1 219 GLN 219 468 468 GLN GLN A . n 
A 1 220 ILE 220 469 469 ILE ILE A . n 
A 1 221 ASN 221 470 470 ASN ASN A . n 
A 1 222 PRO 222 471 471 PRO PRO A . n 
A 1 223 ASP 223 472 472 ASP ASP A . n 
A 1 224 SER 224 473 473 SER SER A . n 
A 1 225 ALA 225 474 474 ALA ALA A . n 
A 1 226 VAL 226 475 475 VAL VAL A . n 
A 1 227 ASN 227 476 476 ASN ASN A . n 
A 1 228 PRO 228 477 477 PRO PRO A . n 
A 1 229 GLU 229 478 478 GLU GLU A . n 
A 1 230 HIS 230 479 479 HIS HIS A . n 
A 1 231 LEU 231 480 480 LEU LEU A . n 
A 1 232 SER 232 481 481 SER SER A . n 
A 1 233 TYR 233 482 482 TYR TYR A . n 
A 1 234 PHE 234 483 483 PHE PHE A . n 
A 1 235 HIS 235 484 484 HIS HIS A . n 
A 1 236 PHE 236 485 485 PHE PHE A . n 
A 1 237 VAL 237 486 486 VAL VAL A . n 
A 1 238 GLY 238 487 487 GLY GLY A . n 
A 1 239 ARG 239 488 488 ARG ARG A . n 
A 1 240 ILE 240 489 489 ILE ILE A . n 
A 1 241 MET 241 490 490 MET MET A . n 
A 1 242 GLY 242 491 491 GLY GLY A . n 
A 1 243 MET 243 492 492 MET MET A . n 
A 1 244 ALA 244 493 493 ALA ALA A . n 
A 1 245 VAL 245 494 494 VAL VAL A . n 
A 1 246 PHE 246 495 495 PHE PHE A . n 
A 1 247 HIS 247 496 496 HIS HIS A . n 
A 1 248 GLY 248 497 497 GLY GLY A . n 
A 1 249 HIS 249 498 498 HIS HIS A . n 
A 1 250 TYR 250 499 499 TYR TYR A . n 
A 1 251 ILE 251 500 500 ILE ILE A . n 
A 1 252 ASP 252 501 501 ASP ASP A . n 
A 1 253 GLY 253 502 502 GLY GLY A . n 
A 1 254 GLY 254 503 503 GLY GLY A . n 
A 1 255 PHE 255 504 504 PHE PHE A . n 
A 1 256 THR 256 505 505 THR THR A . n 
A 1 257 LEU 257 506 506 LEU LEU A . n 
A 1 258 PRO 258 507 507 PRO PRO A . n 
A 1 259 PHE 259 508 508 PHE PHE A . n 
A 1 260 TYR 260 509 509 TYR TYR A . n 
A 1 261 LYS 261 510 510 LYS LYS A . n 
A 1 262 GLN 262 511 511 GLN GLN A . n 
A 1 263 LEU 263 512 512 LEU LEU A . n 
A 1 264 LEU 264 513 513 LEU LEU A . n 
A 1 265 GLY 265 514 514 GLY GLY A . n 
A 1 266 LYS 266 515 515 LYS LYS A . n 
A 1 267 SER 267 516 516 SER SER A . n 
A 1 268 ILE 268 517 517 ILE ILE A . n 
A 1 269 THR 269 518 518 THR THR A . n 
A 1 270 LEU 270 519 519 LEU LEU A . n 
A 1 271 ASP 271 520 520 ASP ASP A . n 
A 1 272 ASP 272 521 521 ASP ASP A . n 
A 1 273 MET 273 522 522 MET MET A . n 
A 1 274 GLU 274 523 523 GLU GLU A . n 
A 1 275 LEU 275 524 524 LEU LEU A . n 
A 1 276 VAL 276 525 525 VAL VAL A . n 
A 1 277 ASP 277 526 526 ASP ASP A . n 
A 1 278 PRO 278 527 527 PRO PRO A . n 
A 1 279 ASP 279 528 528 ASP ASP A . n 
A 1 280 LEU 280 529 529 LEU LEU A . n 
A 1 281 HIS 281 530 530 HIS HIS A . n 
A 1 282 ASN 282 531 531 ASN ASN A . n 
A 1 283 SER 283 532 532 SER SER A . n 
A 1 284 LEU 284 533 533 LEU LEU A . n 
A 1 285 VAL 285 534 534 VAL VAL A . n 
A 1 286 TRP 286 535 535 TRP TRP A . n 
A 1 287 ILE 287 536 536 ILE ILE A . n 
A 1 288 LEU 288 537 537 LEU LEU A . n 
A 1 289 GLU 289 538 538 GLU GLU A . n 
A 1 290 ASN 290 539 539 ASN ASN A . n 
A 1 291 ASP 291 540 540 ASP ASP A . n 
A 1 292 ILE 292 541 541 ILE ILE A . n 
A 1 293 THR 293 542 542 THR THR A . n 
A 1 294 GLY 294 543 543 GLY GLY A . n 
A 1 295 VAL 295 544 544 VAL VAL A . n 
A 1 296 LEU 296 545 545 LEU LEU A . n 
A 1 297 ASP 297 546 546 ASP ASP A . n 
A 1 298 HIS 298 547 547 HIS HIS A . n 
A 1 299 THR 299 548 548 THR THR A . n 
A 1 300 PHE 300 549 549 PHE PHE A . n 
A 1 301 CYS 301 550 550 CYS CYS A . n 
A 1 302 VAL 302 551 551 VAL VAL A . n 
A 1 303 GLU 303 552 552 GLU GLU A . n 
A 1 304 HIS 304 553 553 HIS HIS A . n 
A 1 305 ASN 305 554 554 ASN ASN A . n 
A 1 306 ALA 306 555 555 ALA ALA A . n 
A 1 307 TYR 307 556 556 TYR TYR A . n 
A 1 308 GLY 308 557 557 GLY GLY A . n 
A 1 309 GLU 309 558 558 GLU GLU A . n 
A 1 310 ILE 310 559 559 ILE ILE A . n 
A 1 311 ILE 311 560 560 ILE ILE A . n 
A 1 312 GLN 312 561 561 GLN GLN A . n 
A 1 313 HIS 313 562 562 HIS HIS A . n 
A 1 314 GLU 314 563 563 GLU GLU A . n 
A 1 315 LEU 315 564 564 LEU LEU A . n 
A 1 316 LYS 316 565 565 LYS LYS A . n 
A 1 317 PRO 317 566 566 PRO PRO A . n 
A 1 318 ASN 318 567 567 ASN ASN A . n 
A 1 319 GLY 319 568 568 GLY GLY A . n 
A 1 320 LYS 320 569 569 LYS LYS A . n 
A 1 321 SER 321 570 570 SER SER A . n 
A 1 322 ILE 322 571 571 ILE ILE A . n 
A 1 323 PRO 323 572 572 PRO PRO A . n 
A 1 324 VAL 324 573 573 VAL VAL A . n 
A 1 325 ASN 325 574 574 ASN ASN A . n 
A 1 326 GLU 326 575 575 GLU GLU A . n 
A 1 327 GLU 327 576 576 GLU GLU A . n 
A 1 328 ASN 328 577 577 ASN ASN A . n 
A 1 329 LYS 329 578 578 LYS LYS A . n 
A 1 330 LYS 330 579 579 LYS LYS A . n 
A 1 331 GLU 331 580 580 GLU GLU A . n 
A 1 332 TYR 332 581 581 TYR TYR A . n 
A 1 333 VAL 333 582 582 VAL VAL A . n 
A 1 334 ARG 334 583 583 ARG ARG A . n 
A 1 335 LEU 335 584 584 LEU LEU A . n 
A 1 336 TYR 336 585 585 TYR TYR A . n 
A 1 337 VAL 337 586 586 VAL VAL A . n 
A 1 338 ASN 338 587 587 ASN ASN A . n 
A 1 339 TRP 339 588 588 TRP TRP A . n 
A 1 340 ARG 340 589 589 ARG ARG A . n 
A 1 341 PHE 341 590 590 PHE PHE A . n 
A 1 342 LEU 342 591 591 LEU LEU A . n 
A 1 343 ARG 343 592 592 ARG ARG A . n 
A 1 344 GLY 344 593 593 GLY GLY A . n 
A 1 345 ILE 345 594 594 ILE ILE A . n 
A 1 346 GLU 346 595 595 GLU GLU A . n 
A 1 347 ALA 347 596 596 ALA ALA A . n 
A 1 348 GLN 348 597 597 GLN GLN A . n 
A 1 349 PHE 349 598 598 PHE PHE A . n 
A 1 350 LEU 350 599 599 LEU LEU A . n 
A 1 351 ALA 351 600 600 ALA ALA A . n 
A 1 352 LEU 352 601 601 LEU LEU A . n 
A 1 353 GLN 353 602 602 GLN GLN A . n 
A 1 354 LYS 354 603 603 LYS LYS A . n 
A 1 355 GLY 355 604 604 GLY GLY A . n 
A 1 356 PHE 356 605 605 PHE PHE A . n 
A 1 357 ASN 357 606 606 ASN ASN A . n 
A 1 358 GLU 358 607 607 GLU GLU A . n 
A 1 359 VAL 359 608 608 VAL VAL A . n 
A 1 360 ILE 360 609 609 ILE ILE A . n 
A 1 361 PRO 361 610 610 PRO PRO A . n 
A 1 362 GLN 362 611 611 GLN GLN A . n 
A 1 363 HIS 363 612 612 HIS HIS A . n 
A 1 364 LEU 364 613 613 LEU LEU A . n 
A 1 365 LEU 365 614 614 LEU LEU A . n 
A 1 366 LYS 366 615 615 LYS LYS A . n 
A 1 367 THR 367 616 616 THR THR A . n 
A 1 368 PHE 368 617 617 PHE PHE A . n 
A 1 369 ASP 369 618 618 ASP ASP A . n 
A 1 370 GLU 370 619 619 GLU GLU A . n 
A 1 371 LYS 371 620 620 LYS LYS A . n 
A 1 372 GLU 372 621 621 GLU GLU A . n 
A 1 373 LEU 373 622 622 LEU LEU A . n 
A 1 374 GLU 374 623 623 GLU GLU A . n 
A 1 375 LEU 375 624 624 LEU LEU A . n 
A 1 376 ILE 376 625 625 ILE ILE A . n 
A 1 377 ILE 377 626 626 ILE ILE A . n 
A 1 378 CYS 378 627 627 CYS CYS A . n 
A 1 379 GLY 379 628 628 GLY GLY A . n 
A 1 380 LEU 380 629 629 LEU LEU A . n 
A 1 381 GLY 381 630 630 GLY GLY A . n 
A 1 382 LYS 382 631 631 LYS LYS A . n 
A 1 383 ILE 383 632 632 ILE ILE A . n 
A 1 384 ASP 384 633 633 ASP ASP A . n 
A 1 385 VAL 385 634 634 VAL VAL A . n 
A 1 386 ASN 386 635 635 ASN ASN A . n 
A 1 387 ASP 387 636 636 ASP ASP A . n 
A 1 388 TRP 388 637 637 TRP TRP A . n 
A 1 389 LYS 389 638 638 LYS LYS A . n 
A 1 390 VAL 390 639 639 VAL VAL A . n 
A 1 391 ASN 391 640 640 ASN ASN A . n 
A 1 392 THR 392 641 641 THR THR A . n 
A 1 393 ARG 393 642 642 ARG ARG A . n 
A 1 394 LEU 394 643 643 LEU LEU A . n 
A 1 395 LYS 395 644 644 LYS LYS A . n 
A 1 396 HIS 396 645 645 HIS HIS A . n 
A 1 397 CYS 397 646 646 CYS CYS A . n 
A 1 398 THR 398 647 647 THR THR A . n 
A 1 399 PRO 399 648 648 PRO PRO A . n 
A 1 400 ASP 400 649 649 ASP ASP A . n 
A 1 401 SER 401 650 650 SER SER A . n 
A 1 402 ASN 402 651 651 ASN ASN A . n 
A 1 403 ILE 403 652 652 ILE ILE A . n 
A 1 404 VAL 404 653 653 VAL VAL A . n 
A 1 405 LYS 405 654 654 LYS LYS A . n 
A 1 406 TRP 406 655 655 TRP TRP A . n 
A 1 407 PHE 407 656 656 PHE PHE A . n 
A 1 408 TRP 408 657 657 TRP TRP A . n 
A 1 409 LYS 409 658 658 LYS LYS A . n 
A 1 410 ALA 410 659 659 ALA ALA A . n 
A 1 411 VAL 411 660 660 VAL VAL A . n 
A 1 412 GLU 412 661 661 GLU GLU A . n 
A 1 413 PHE 413 662 662 PHE PHE A . n 
A 1 414 PHE 414 663 663 PHE PHE A . n 
A 1 415 ASP 415 664 664 ASP ASP A . n 
A 1 416 GLU 416 665 665 GLU GLU A . n 
A 1 417 GLU 417 666 666 GLU GLU A . n 
A 1 418 ARG 418 667 667 ARG ARG A . n 
A 1 419 ARG 419 668 668 ARG ARG A . n 
A 1 420 ALA 420 669 669 ALA ALA A . n 
A 1 421 ARG 421 670 670 ARG ARG A . n 
A 1 422 LEU 422 671 671 LEU LEU A . n 
A 1 423 LEU 423 672 672 LEU LEU A . n 
A 1 424 GLN 424 673 673 GLN GLN A . n 
A 1 425 PHE 425 674 674 PHE PHE A . n 
A 1 426 VAL 426 675 675 VAL VAL A . n 
A 1 427 THR 427 676 676 THR THR A . n 
A 1 428 GLY 428 677 677 GLY GLY A . n 
A 1 429 SER 429 678 678 SER SER A . n 
A 1 430 SER 430 679 679 SER SER A . n 
A 1 431 ARG 431 680 680 ARG ARG A . n 
A 1 432 VAL 432 681 681 VAL VAL A . n 
A 1 433 PRO 433 682 682 PRO PRO A . n 
A 1 434 LEU 434 683 683 LEU LEU A . n 
A 1 435 GLN 435 684 684 GLN GLN A . n 
A 1 436 GLY 436 685 685 GLY GLY A . n 
A 1 437 PHE 437 686 686 PHE PHE A . n 
A 1 438 LYS 438 687 687 LYS LYS A . n 
A 1 439 ALA 439 688 688 ALA ALA A . n 
A 1 440 LEU 440 689 689 LEU LEU A . n 
A 1 441 GLN 441 690 690 GLN GLN A . n 
A 1 442 GLY 442 691 691 GLY GLY A . n 
A 1 443 ALA 443 692 692 ALA ALA A . n 
A 1 444 ALA 444 693 693 ALA ALA A . n 
A 1 445 GLY 445 694 694 GLY GLY A . n 
A 1 446 PRO 446 695 695 PRO PRO A . n 
A 1 447 ARG 447 696 696 ARG ARG A . n 
A 1 448 LEU 448 697 697 LEU LEU A . n 
A 1 449 PHE 449 698 698 PHE PHE A . n 
A 1 450 THR 450 699 699 THR THR A . n 
A 1 451 ILE 451 700 700 ILE ILE A . n 
A 1 452 HIS 452 701 701 HIS HIS A . n 
A 1 453 GLN 453 702 702 GLN GLN A . n 
A 1 454 ILE 454 703 703 ILE ILE A . n 
A 1 455 ASP 455 704 704 ASP ASP A . n 
A 1 456 ALA 456 705 705 ALA ALA A . n 
A 1 457 CYS 457 706 706 CYS CYS A . n 
A 1 458 THR 458 707 707 THR THR A . n 
A 1 459 ASN 459 708 708 ASN ASN A . n 
A 1 460 ASN 460 709 709 ASN ASN A . n 
A 1 461 LEU 461 710 710 LEU LEU A . n 
A 1 462 PRO 462 711 711 PRO PRO A . n 
A 1 463 LYS 463 712 712 LYS LYS A . n 
A 1 464 ALA 464 713 713 ALA ALA A . n 
A 1 465 HIS 465 714 714 HIS HIS A . n 
A 1 466 THR 466 715 715 THR THR A . n 
A 1 467 CYS 467 716 716 CYS CYS A . n 
A 1 468 PHE 468 717 717 PHE PHE A . n 
A 1 469 ASN 469 718 718 ASN ASN A . n 
A 1 470 ARG 470 719 719 ARG ARG A . n 
A 1 471 ILE 471 720 720 ILE ILE A . n 
A 1 472 ASP 472 721 721 ASP ASP A . n 
A 1 473 ILE 473 722 722 ILE ILE A . n 
A 1 474 PRO 474 723 723 PRO PRO A . n 
A 1 475 PRO 475 724 724 PRO PRO A . n 
A 1 476 TYR 476 725 725 TYR TYR A . n 
A 1 477 GLU 477 726 726 GLU GLU A . n 
A 1 478 SER 478 727 727 SER SER A . n 
A 1 479 TYR 479 728 728 TYR TYR A . n 
A 1 480 GLU 480 729 729 GLU GLU A . n 
A 1 481 LYS 481 730 730 LYS LYS A . n 
A 1 482 LEU 482 731 731 LEU LEU A . n 
A 1 483 TYR 483 732 732 TYR TYR A . n 
A 1 484 GLU 484 733 733 GLU GLU A . n 
A 1 485 LYS 485 734 734 LYS LYS A . n 
A 1 486 LEU 486 735 735 LEU LEU A . n 
A 1 487 LEU 487 736 736 LEU LEU A . n 
A 1 488 THR 488 737 737 THR THR A . n 
A 1 489 ALA 489 738 738 ALA ALA A . n 
A 1 490 ILE 490 739 739 ILE ILE A . n 
A 1 491 GLU 491 740 740 GLU GLU A . n 
A 1 492 GLU 492 741 741 GLU GLU A . n 
A 1 493 THR 493 742 ?   ?   ?   A . n 
A 1 494 CYS 494 743 ?   ?   ?   A . n 
A 1 495 GLY 495 744 ?   ?   ?   A . n 
A 1 496 PHE 496 745 ?   ?   ?   A . n 
A 1 497 ALA 497 746 ?   ?   ?   A . n 
A 1 498 VAL 498 747 ?   ?   ?   A . n 
A 1 499 GLU 499 748 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        TJQ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   TJQ 
_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 TJQ 1   801  801  TJQ TJQ A . 
C 3 PO4 1   802  802  PO4 PO4 A . 
D 4 HOH 1   901  901  HOH HOH A . 
D 4 HOH 2   902  902  HOH HOH A . 
D 4 HOH 3   903  903  HOH HOH A . 
D 4 HOH 4   904  904  HOH HOH A . 
D 4 HOH 5   905  905  HOH HOH A . 
D 4 HOH 6   906  906  HOH HOH A . 
D 4 HOH 7   907  907  HOH HOH A . 
D 4 HOH 8   908  908  HOH HOH A . 
D 4 HOH 9   909  909  HOH HOH A . 
D 4 HOH 10  910  910  HOH HOH A . 
D 4 HOH 11  911  911  HOH HOH A . 
D 4 HOH 12  912  912  HOH HOH A . 
D 4 HOH 13  913  913  HOH HOH A . 
D 4 HOH 14  914  914  HOH HOH A . 
D 4 HOH 15  915  915  HOH HOH A . 
D 4 HOH 16  916  916  HOH HOH A . 
D 4 HOH 17  917  917  HOH HOH A . 
D 4 HOH 18  918  918  HOH HOH A . 
D 4 HOH 19  919  919  HOH HOH A . 
D 4 HOH 20  920  920  HOH HOH A . 
D 4 HOH 21  921  921  HOH HOH A . 
D 4 HOH 22  922  922  HOH HOH A . 
D 4 HOH 23  923  923  HOH HOH A . 
D 4 HOH 24  924  924  HOH HOH A . 
D 4 HOH 25  925  925  HOH HOH A . 
D 4 HOH 26  926  926  HOH HOH A . 
D 4 HOH 27  927  927  HOH HOH A . 
D 4 HOH 28  928  928  HOH HOH A . 
D 4 HOH 29  929  929  HOH HOH A . 
D 4 HOH 30  930  930  HOH HOH A . 
D 4 HOH 31  931  931  HOH HOH A . 
D 4 HOH 32  932  932  HOH HOH A . 
D 4 HOH 33  933  933  HOH HOH A . 
D 4 HOH 34  934  934  HOH HOH A . 
D 4 HOH 35  935  935  HOH HOH A . 
D 4 HOH 36  936  936  HOH HOH A . 
D 4 HOH 37  937  937  HOH HOH A . 
D 4 HOH 38  938  938  HOH HOH A . 
D 4 HOH 39  939  939  HOH HOH A . 
D 4 HOH 40  940  940  HOH HOH A . 
D 4 HOH 41  941  941  HOH HOH A . 
D 4 HOH 42  942  942  HOH HOH A . 
D 4 HOH 43  943  943  HOH HOH A . 
D 4 HOH 44  944  944  HOH HOH A . 
D 4 HOH 45  945  945  HOH HOH A . 
D 4 HOH 46  946  946  HOH HOH A . 
D 4 HOH 47  947  947  HOH HOH A . 
D 4 HOH 48  948  948  HOH HOH A . 
D 4 HOH 49  949  949  HOH HOH A . 
D 4 HOH 50  950  950  HOH HOH A . 
D 4 HOH 51  951  951  HOH HOH A . 
D 4 HOH 52  952  952  HOH HOH A . 
D 4 HOH 53  953  953  HOH HOH A . 
D 4 HOH 54  954  954  HOH HOH A . 
D 4 HOH 55  955  955  HOH HOH A . 
D 4 HOH 56  956  956  HOH HOH A . 
D 4 HOH 57  957  957  HOH HOH A . 
D 4 HOH 58  958  958  HOH HOH A . 
D 4 HOH 59  959  959  HOH HOH A . 
D 4 HOH 60  960  960  HOH HOH A . 
D 4 HOH 61  961  961  HOH HOH A . 
D 4 HOH 62  962  962  HOH HOH A . 
D 4 HOH 63  963  963  HOH HOH A . 
D 4 HOH 64  964  964  HOH HOH A . 
D 4 HOH 65  965  965  HOH HOH A . 
D 4 HOH 66  966  966  HOH HOH A . 
D 4 HOH 67  967  967  HOH HOH A . 
D 4 HOH 68  968  968  HOH HOH A . 
D 4 HOH 69  969  969  HOH HOH A . 
D 4 HOH 70  970  970  HOH HOH A . 
D 4 HOH 71  971  971  HOH HOH A . 
D 4 HOH 72  972  972  HOH HOH A . 
D 4 HOH 73  973  973  HOH HOH A . 
D 4 HOH 74  974  974  HOH HOH A . 
D 4 HOH 75  975  975  HOH HOH A . 
D 4 HOH 76  976  976  HOH HOH A . 
D 4 HOH 77  977  977  HOH HOH A . 
D 4 HOH 78  978  978  HOH HOH A . 
D 4 HOH 79  979  979  HOH HOH A . 
D 4 HOH 80  980  980  HOH HOH A . 
D 4 HOH 81  981  981  HOH HOH A . 
D 4 HOH 82  982  982  HOH HOH A . 
D 4 HOH 83  983  983  HOH HOH A . 
D 4 HOH 84  984  984  HOH HOH A . 
D 4 HOH 85  985  985  HOH HOH A . 
D 4 HOH 86  986  986  HOH HOH A . 
D 4 HOH 87  987  987  HOH HOH A . 
D 4 HOH 88  988  988  HOH HOH A . 
D 4 HOH 89  989  989  HOH HOH A . 
D 4 HOH 90  990  990  HOH HOH A . 
D 4 HOH 91  991  991  HOH HOH A . 
D 4 HOH 92  992  992  HOH HOH A . 
D 4 HOH 93  993  993  HOH HOH A . 
D 4 HOH 94  994  994  HOH HOH A . 
D 4 HOH 95  995  995  HOH HOH A . 
D 4 HOH 96  996  996  HOH HOH A . 
D 4 HOH 97  997  997  HOH HOH A . 
D 4 HOH 98  998  998  HOH HOH A . 
D 4 HOH 99  999  999  HOH HOH A . 
D 4 HOH 100 1000 1000 HOH HOH A . 
D 4 HOH 101 1001 1001 HOH HOH A . 
D 4 HOH 102 1002 1002 HOH HOH A . 
D 4 HOH 103 1003 1003 HOH HOH A . 
D 4 HOH 104 1004 1004 HOH HOH A . 
D 4 HOH 105 1005 1005 HOH HOH A . 
D 4 HOH 106 1006 1006 HOH HOH A . 
D 4 HOH 107 1007 1007 HOH HOH A . 
D 4 HOH 108 1008 1008 HOH HOH A . 
D 4 HOH 109 1009 1009 HOH HOH A . 
D 4 HOH 110 1010 1010 HOH HOH A . 
D 4 HOH 111 1011 1011 HOH HOH A . 
D 4 HOH 112 1012 1012 HOH HOH A . 
D 4 HOH 113 1013 1013 HOH HOH A . 
D 4 HOH 114 1014 1014 HOH HOH A . 
D 4 HOH 115 1015 1015 HOH HOH A . 
D 4 HOH 116 1016 1016 HOH HOH A . 
D 4 HOH 117 1017 1017 HOH HOH A . 
D 4 HOH 118 1018 1018 HOH HOH A . 
D 4 HOH 119 1019 1019 HOH HOH A . 
D 4 HOH 120 1020 1020 HOH HOH A . 
D 4 HOH 121 1021 1021 HOH HOH A . 
D 4 HOH 122 1022 1022 HOH HOH A . 
D 4 HOH 123 1023 1023 HOH HOH A . 
D 4 HOH 124 1024 1024 HOH HOH A . 
D 4 HOH 125 1025 1025 HOH HOH A . 
D 4 HOH 126 1026 1026 HOH HOH A . 
D 4 HOH 127 1027 1027 HOH HOH A . 
D 4 HOH 128 1028 1028 HOH HOH A . 
D 4 HOH 129 1029 1029 HOH HOH A . 
D 4 HOH 130 1030 1030 HOH HOH A . 
D 4 HOH 131 1031 1031 HOH HOH A . 
D 4 HOH 132 1032 1032 HOH HOH A . 
D 4 HOH 133 1033 1033 HOH HOH A . 
D 4 HOH 134 1034 1034 HOH HOH A . 
D 4 HOH 135 1035 1035 HOH HOH A . 
D 4 HOH 136 1036 1036 HOH HOH A . 
D 4 HOH 137 1037 1037 HOH HOH A . 
D 4 HOH 138 1038 1038 HOH HOH A . 
D 4 HOH 139 1039 1039 HOH HOH A . 
D 4 HOH 140 1040 1040 HOH HOH A . 
D 4 HOH 141 1041 1041 HOH HOH A . 
D 4 HOH 142 1042 1042 HOH HOH A . 
D 4 HOH 143 1043 1043 HOH HOH A . 
D 4 HOH 144 1044 1044 HOH HOH A . 
D 4 HOH 145 1045 1045 HOH HOH A . 
D 4 HOH 146 1046 1046 HOH HOH A . 
D 4 HOH 147 1047 1047 HOH HOH A . 
D 4 HOH 148 1048 1048 HOH HOH A . 
D 4 HOH 149 1049 1049 HOH HOH A . 
D 4 HOH 150 1050 1050 HOH HOH A . 
D 4 HOH 151 1051 1051 HOH HOH A . 
D 4 HOH 152 1052 1052 HOH HOH A . 
D 4 HOH 153 1053 1053 HOH HOH A . 
D 4 HOH 154 1054 1054 HOH HOH A . 
D 4 HOH 155 1055 1055 HOH HOH A . 
D 4 HOH 156 1056 1056 HOH HOH A . 
D 4 HOH 157 1057 1057 HOH HOH A . 
D 4 HOH 158 1058 1058 HOH HOH A . 
D 4 HOH 159 1059 1059 HOH HOH A . 
D 4 HOH 160 1060 1060 HOH HOH A . 
D 4 HOH 161 1061 1061 HOH HOH A . 
D 4 HOH 162 1062 1062 HOH HOH A . 
D 4 HOH 163 1063 1063 HOH HOH A . 
D 4 HOH 164 1064 1064 HOH HOH A . 
D 4 HOH 165 1065 1065 HOH HOH A . 
D 4 HOH 166 1066 1066 HOH HOH A . 
D 4 HOH 167 1067 1067 HOH HOH A . 
D 4 HOH 168 1068 1068 HOH HOH A . 
D 4 HOH 169 1069 1069 HOH HOH A . 
D 4 HOH 170 1070 1070 HOH HOH A . 
D 4 HOH 171 1071 1071 HOH HOH A . 
D 4 HOH 172 1072 1072 HOH HOH A . 
D 4 HOH 173 1073 1073 HOH HOH A . 
D 4 HOH 174 1074 1074 HOH HOH A . 
D 4 HOH 175 1075 1075 HOH HOH A . 
D 4 HOH 176 1076 1076 HOH HOH A . 
D 4 HOH 177 1077 1077 HOH HOH A . 
D 4 HOH 178 1078 1078 HOH HOH A . 
D 4 HOH 179 1079 1079 HOH HOH A . 
D 4 HOH 180 1080 1080 HOH HOH A . 
D 4 HOH 181 1081 1081 HOH HOH A . 
D 4 HOH 182 1082 1082 HOH HOH A . 
D 4 HOH 183 1083 1083 HOH HOH A . 
D 4 HOH 184 1084 1084 HOH HOH A . 
D 4 HOH 185 1085 1085 HOH HOH A . 
D 4 HOH 186 1086 1086 HOH HOH A . 
D 4 HOH 187 1087 1087 HOH HOH A . 
D 4 HOH 188 1088 1088 HOH HOH A . 
D 4 HOH 189 1089 1089 HOH HOH A . 
D 4 HOH 190 1090 1090 HOH HOH A . 
D 4 HOH 191 1091 1091 HOH HOH A . 
D 4 HOH 192 1092 1092 HOH HOH A . 
D 4 HOH 193 1093 1093 HOH HOH A . 
D 4 HOH 194 1094 1094 HOH HOH A . 
D 4 HOH 195 1095 1095 HOH HOH A . 
D 4 HOH 196 1096 1096 HOH HOH A . 
D 4 HOH 197 1097 1097 HOH HOH A . 
D 4 HOH 198 1098 1098 HOH HOH A . 
D 4 HOH 199 1099 1099 HOH HOH A . 
D 4 HOH 200 1100 1100 HOH HOH A . 
D 4 HOH 201 1101 1101 HOH HOH A . 
D 4 HOH 202 1102 1102 HOH HOH A . 
D 4 HOH 203 1103 1103 HOH HOH A . 
D 4 HOH 204 1104 1104 HOH HOH A . 
D 4 HOH 205 1105 1105 HOH HOH A . 
D 4 HOH 206 1106 1106 HOH HOH A . 
D 4 HOH 207 1107 1107 HOH HOH A . 
D 4 HOH 208 1108 1108 HOH HOH A . 
D 4 HOH 209 1109 1109 HOH HOH A . 
D 4 HOH 210 1110 1110 HOH HOH A . 
D 4 HOH 211 1111 1111 HOH HOH A . 
D 4 HOH 212 1112 1112 HOH HOH A . 
D 4 HOH 213 1113 1113 HOH HOH A . 
D 4 HOH 214 1114 1114 HOH HOH A . 
D 4 HOH 215 1115 1115 HOH HOH A . 
D 4 HOH 216 1116 1116 HOH HOH A . 
D 4 HOH 217 1117 1117 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? 2.11.8 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FSH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.531 
_cell.length_a_esd                 ? 
_cell.length_b                     71.75 
_cell.length_b_esd                 ? 
_cell.length_c                     152.624 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9FSH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FSH 
_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             2.47 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.22 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.5 M NaH2PO4/K2HPO4 pH 6.8, 100 mM NaOAc' 
_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 PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2010-03-13 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00000 
_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                        'SLS BEAMLINE X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FSH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.08 
_reflns.d_resolution_low                               76.31 
_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                                     35457 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.33 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.68 
_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                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.08 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.08 
_reflns_shell.d_res_low                                     2.15 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.72 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             675 
_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                               6.51 
_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                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.499 
_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]                            5.7642 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            -0.301 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -5.4632 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               36.82 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.929 
_refine.correlation_coeff_Fo_to_Fc_free          0.902 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9FSH 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.08 
_refine.ls_d_res_low                             43.27 
_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                     35456 
_refine.ls_number_reflns_R_free                  1773 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2302 
_refine.ls_R_factor_R_free                       0.2590 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2287 
_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                    ? 
_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                      1WAPI 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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   0.165 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.168 
_refine.pdbx_overall_SU_R_Blow_DPI               0.191 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.185 
_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_analyze.entry_id                        9FSH 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.3 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.08 
_refine_hist.d_res_low                        43.27 
_refine_hist.number_atoms_solvent             217 
_refine_hist.number_atoms_total               3339 
_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        3090 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_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 ? 3202 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.85  ? 4331 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1134 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 542  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 3202 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 388  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 2392 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.96  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 17.42 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.08 
_refine_ls_shell.d_res_low                        2.09 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                710 
_refine_ls_shell.number_reflns_R_free             35 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               100 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     0.2783 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2764 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.3175 
# 
_struct.entry_id                     9FSH 
_struct.title                        'Crystal structure of the HECT domain of Smurf 2 in complex with inhibitor 8' 
_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        9FSH 
_struct_keywords.text            
;E3 ubiquitin-protein ligase SMURF2, HECT domain, inhibitor, allosteric inhibition, BMP signaling, pulmonary vascular remodeling, LIGASE
;
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SMUF2_HUMAN 
_struct_ref.pdbx_db_accession          Q9HAU4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRL
SANLHLVLNRQNQLKDQQQQQVVSLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQV
MKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIM
GMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKS
IPVNEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVNDWKVNTRLKHCTPDS
NIVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEK
LYEKLLTAIEETCGFAVE
;
_struct_ref.pdbx_align_begin           251 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9FSH 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 499 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9HAU4 
_struct_ref_seq.db_align_beg                  251 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  748 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       251 
_struct_ref_seq.pdbx_auth_seq_align_end       748 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9FSH 
_struct_ref_seq_dif.mon_id                       GLY 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      1 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q9HAU4 
_struct_ref_seq_dif.db_mon_id                    ? 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          ? 
_struct_ref_seq_dif.details                      'expression tag' 
_struct_ref_seq_dif.pdbx_auth_seq_num            250 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 150   ? 
1 MORE         -4    ? 
1 'SSA (A^2)'  20040 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 120 ? GLN A 138 ? LYS A 369 GLN A 387 1 ? 19 
HELX_P HELX_P2  AA2 GLU A 152 ? LYS A 163 ? GLU A 401 LYS A 412 1 ? 12 
HELX_P HELX_P3  AA3 MET A 164 ? LYS A 171 ? MET A 413 LYS A 420 5 ? 8  
HELX_P HELX_P4  AA4 ASP A 184 ? MET A 200 ? ASP A 433 MET A 449 1 ? 17 
HELX_P HELX_P5  AA5 LEU A 201 ? GLY A 206 ? LEU A 450 GLY A 455 5 ? 6  
HELX_P HELX_P6  AA6 ASP A 223 ? ASN A 227 ? ASP A 472 ASN A 476 5 ? 5  
HELX_P HELX_P7  AA7 GLU A 229 ? HIS A 247 ? GLU A 478 HIS A 496 1 ? 19 
HELX_P HELX_P8  AA8 THR A 256 ? LEU A 264 ? THR A 505 LEU A 513 1 ? 9  
HELX_P HELX_P9  AA9 THR A 269 ? ASP A 271 ? THR A 518 ASP A 520 5 ? 3  
HELX_P HELX_P10 AB1 ASP A 272 ? ASP A 277 ? ASP A 521 ASP A 526 1 ? 6  
HELX_P HELX_P11 AB2 ASP A 277 ? ASN A 290 ? ASP A 526 ASN A 539 1 ? 14 
HELX_P HELX_P12 AB3 ASN A 318 ? ILE A 322 ? ASN A 567 ILE A 571 5 ? 5  
HELX_P HELX_P13 AB4 ASN A 328 ? LEU A 342 ? ASN A 577 LEU A 591 1 ? 15 
HELX_P HELX_P14 AB5 ILE A 345 ? GLU A 358 ? ILE A 594 GLU A 607 1 ? 14 
HELX_P HELX_P15 AB6 PRO A 361 ? LYS A 366 ? PRO A 610 LYS A 615 5 ? 6  
HELX_P HELX_P16 AB7 ASP A 369 ? GLY A 379 ? ASP A 618 GLY A 628 1 ? 11 
HELX_P HELX_P17 AB8 ASP A 384 ? ASN A 391 ? ASP A 633 ASN A 640 1 ? 8  
HELX_P HELX_P18 AB9 SER A 401 ? PHE A 414 ? SER A 650 PHE A 663 1 ? 14 
HELX_P HELX_P19 AC1 ASP A 415 ? GLY A 428 ? ASP A 664 GLY A 677 1 ? 14 
HELX_P HELX_P20 AC2 GLY A 436 ? LEU A 440 ? GLY A 685 LEU A 689 5 ? 5  
HELX_P HELX_P21 AC3 SER A 478 ? GLU A 491 ? SER A 727 GLU A 740 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 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      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 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 HIS A 143 ? VAL A 148 ? HIS A 392 VAL A 397 
AA1 2 ARG A 172 ? PHE A 177 ? ARG A 421 PHE A 426 
AA2 1 PHE A 208 ? TYR A 210 ? PHE A 457 TYR A 459 
AA2 2 LEU A 218 ? ILE A 220 ? LEU A 467 ILE A 469 
AA3 1 CYS A 301 ? ALA A 306 ? CYS A 550 ALA A 555 
AA3 2 GLU A 309 ? GLU A 314 ? GLU A 558 GLU A 563 
AA4 1 THR A 392 ? LYS A 395 ? THR A 641 LYS A 644 
AA4 2 PHE A 449 ? GLN A 453 ? PHE A 698 GLN A 702 
AA4 3 ARG A 470 ? ILE A 473 ? ARG A 719 ILE A 722 
AA4 4 LYS A 463 ? HIS A 465 ? LYS A 712 HIS A 714 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N CYS A 144 ? N CYS A 393 O ARG A 172 ? O ARG A 421 
AA2 1 2 N GLN A 209 ? N GLN A 458 O GLN A 219 ? O GLN A 468 
AA3 1 2 N VAL A 302 ? N VAL A 551 O HIS A 313 ? O HIS A 562 
AA4 1 2 N LYS A 395 ? N LYS A 644 O ILE A 451 ? O ILE A 700 
AA4 2 3 N HIS A 452 ? N HIS A 701 O ILE A 471 ? O ILE A 720 
AA4 3 4 O ASP A 472 ? O ASP A 721 N LYS A 463 ? N LYS A 712 
# 
_pdbx_entry_details.entry_id                   9FSH 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 526 ? ? -156.48 85.65 
2 1 PHE A 549 ? ? -81.61  37.35 
# 
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 GLY 250 ? A GLY 1   
2   1 Y 1 A PRO 251 ? A PRO 2   
3   1 Y 1 A ASP 252 ? A ASP 3   
4   1 Y 1 A LEU 253 ? A LEU 4   
5   1 Y 1 A PRO 254 ? A PRO 5   
6   1 Y 1 A GLU 255 ? A GLU 6   
7   1 Y 1 A GLY 256 ? A GLY 7   
8   1 Y 1 A TYR 257 ? A TYR 8   
9   1 Y 1 A GLU 258 ? A GLU 9   
10  1 Y 1 A GLN 259 ? A GLN 10  
11  1 Y 1 A ARG 260 ? A ARG 11  
12  1 Y 1 A THR 261 ? A THR 12  
13  1 Y 1 A THR 262 ? A THR 13  
14  1 Y 1 A GLN 263 ? A GLN 14  
15  1 Y 1 A GLN 264 ? A GLN 15  
16  1 Y 1 A GLY 265 ? A GLY 16  
17  1 Y 1 A GLN 266 ? A GLN 17  
18  1 Y 1 A VAL 267 ? A VAL 18  
19  1 Y 1 A TYR 268 ? A TYR 19  
20  1 Y 1 A PHE 269 ? A PHE 20  
21  1 Y 1 A LEU 270 ? A LEU 21  
22  1 Y 1 A HIS 271 ? A HIS 22  
23  1 Y 1 A THR 272 ? A THR 23  
24  1 Y 1 A GLN 273 ? A GLN 24  
25  1 Y 1 A THR 274 ? A THR 25  
26  1 Y 1 A GLY 275 ? A GLY 26  
27  1 Y 1 A VAL 276 ? A VAL 27  
28  1 Y 1 A SER 277 ? A SER 28  
29  1 Y 1 A THR 278 ? A THR 29  
30  1 Y 1 A TRP 279 ? A TRP 30  
31  1 Y 1 A HIS 280 ? A HIS 31  
32  1 Y 1 A ASP 281 ? A ASP 32  
33  1 Y 1 A PRO 282 ? A PRO 33  
34  1 Y 1 A ARG 283 ? A ARG 34  
35  1 Y 1 A VAL 284 ? A VAL 35  
36  1 Y 1 A PRO 285 ? A PRO 36  
37  1 Y 1 A ARG 286 ? A ARG 37  
38  1 Y 1 A ASP 287 ? A ASP 38  
39  1 Y 1 A LEU 288 ? A LEU 39  
40  1 Y 1 A SER 289 ? A SER 40  
41  1 Y 1 A ASN 290 ? A ASN 41  
42  1 Y 1 A ILE 291 ? A ILE 42  
43  1 Y 1 A ASN 292 ? A ASN 43  
44  1 Y 1 A CYS 293 ? A CYS 44  
45  1 Y 1 A GLU 294 ? A GLU 45  
46  1 Y 1 A GLU 295 ? A GLU 46  
47  1 Y 1 A LEU 296 ? A LEU 47  
48  1 Y 1 A GLY 297 ? A GLY 48  
49  1 Y 1 A PRO 298 ? A PRO 49  
50  1 Y 1 A LEU 299 ? A LEU 50  
51  1 Y 1 A PRO 300 ? A PRO 51  
52  1 Y 1 A PRO 301 ? A PRO 52  
53  1 Y 1 A GLY 302 ? A GLY 53  
54  1 Y 1 A TRP 303 ? A TRP 54  
55  1 Y 1 A GLU 304 ? A GLU 55  
56  1 Y 1 A ILE 305 ? A ILE 56  
57  1 Y 1 A ARG 306 ? A ARG 57  
58  1 Y 1 A ASN 307 ? A ASN 58  
59  1 Y 1 A THR 308 ? A THR 59  
60  1 Y 1 A ALA 309 ? A ALA 60  
61  1 Y 1 A THR 310 ? A THR 61  
62  1 Y 1 A GLY 311 ? A GLY 62  
63  1 Y 1 A ARG 312 ? A ARG 63  
64  1 Y 1 A VAL 313 ? A VAL 64  
65  1 Y 1 A TYR 314 ? A TYR 65  
66  1 Y 1 A PHE 315 ? A PHE 66  
67  1 Y 1 A VAL 316 ? A VAL 67  
68  1 Y 1 A ASP 317 ? A ASP 68  
69  1 Y 1 A HIS 318 ? A HIS 69  
70  1 Y 1 A ASN 319 ? A ASN 70  
71  1 Y 1 A ASN 320 ? A ASN 71  
72  1 Y 1 A ARG 321 ? A ARG 72  
73  1 Y 1 A THR 322 ? A THR 73  
74  1 Y 1 A THR 323 ? A THR 74  
75  1 Y 1 A GLN 324 ? A GLN 75  
76  1 Y 1 A PHE 325 ? A PHE 76  
77  1 Y 1 A THR 326 ? A THR 77  
78  1 Y 1 A ASP 327 ? A ASP 78  
79  1 Y 1 A PRO 328 ? A PRO 79  
80  1 Y 1 A ARG 329 ? A ARG 80  
81  1 Y 1 A LEU 330 ? A LEU 81  
82  1 Y 1 A SER 331 ? A SER 82  
83  1 Y 1 A ALA 332 ? A ALA 83  
84  1 Y 1 A ASN 333 ? A ASN 84  
85  1 Y 1 A LEU 334 ? A LEU 85  
86  1 Y 1 A HIS 335 ? A HIS 86  
87  1 Y 1 A LEU 336 ? A LEU 87  
88  1 Y 1 A VAL 337 ? A VAL 88  
89  1 Y 1 A LEU 338 ? A LEU 89  
90  1 Y 1 A ASN 339 ? A ASN 90  
91  1 Y 1 A ARG 340 ? A ARG 91  
92  1 Y 1 A GLN 341 ? A GLN 92  
93  1 Y 1 A ASN 342 ? A ASN 93  
94  1 Y 1 A GLN 343 ? A GLN 94  
95  1 Y 1 A LEU 344 ? A LEU 95  
96  1 Y 1 A LYS 345 ? A LYS 96  
97  1 Y 1 A ASP 346 ? A ASP 97  
98  1 Y 1 A GLN 347 ? A GLN 98  
99  1 Y 1 A GLN 348 ? A GLN 99  
100 1 Y 1 A GLN 349 ? A GLN 100 
101 1 Y 1 A GLN 350 ? A GLN 101 
102 1 Y 1 A GLN 351 ? A GLN 102 
103 1 Y 1 A VAL 352 ? A VAL 103 
104 1 Y 1 A VAL 353 ? A VAL 104 
105 1 Y 1 A SER 354 ? A SER 105 
106 1 Y 1 A LEU 355 ? A LEU 106 
107 1 Y 1 A CYS 356 ? A CYS 107 
108 1 Y 1 A PRO 357 ? A PRO 108 
109 1 Y 1 A ASP 358 ? A ASP 109 
110 1 Y 1 A ASP 359 ? A ASP 110 
111 1 Y 1 A THR 360 ? A THR 111 
112 1 Y 1 A GLU 361 ? A GLU 112 
113 1 Y 1 A CYS 362 ? A CYS 113 
114 1 Y 1 A LEU 363 ? A LEU 114 
115 1 Y 1 A THR 364 ? A THR 115 
116 1 Y 1 A VAL 365 ? A VAL 116 
117 1 Y 1 A PRO 366 ? A PRO 117 
118 1 Y 1 A ARG 367 ? A ARG 118 
119 1 Y 1 A TYR 368 ? A TYR 119 
120 1 Y 1 A THR 742 ? A THR 493 
121 1 Y 1 A CYS 743 ? A CYS 494 
122 1 Y 1 A GLY 744 ? A GLY 495 
123 1 Y 1 A PHE 745 ? A PHE 496 
124 1 Y 1 A ALA 746 ? A ALA 497 
125 1 Y 1 A VAL 747 ? A VAL 498 
126 1 Y 1 A GLU 748 ? A GLU 499 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PO4 P    P N N 273 
PO4 O1   O N N 274 
PO4 O2   O N N 275 
PO4 O3   O N N 276 
PO4 O4   O N N 277 
PRO N    N N N 278 
PRO CA   C N S 279 
PRO C    C N N 280 
PRO O    O N N 281 
PRO CB   C N N 282 
PRO CG   C N N 283 
PRO CD   C N N 284 
PRO OXT  O N N 285 
PRO H    H N N 286 
PRO HA   H N N 287 
PRO HB2  H N N 288 
PRO HB3  H N N 289 
PRO HG2  H N N 290 
PRO HG3  H N N 291 
PRO HD2  H N N 292 
PRO HD3  H N N 293 
PRO HXT  H N N 294 
SER N    N N N 295 
SER CA   C N S 296 
SER C    C N N 297 
SER O    O N N 298 
SER CB   C N N 299 
SER OG   O N N 300 
SER OXT  O N N 301 
SER H    H N N 302 
SER H2   H N N 303 
SER HA   H N N 304 
SER HB2  H N N 305 
SER HB3  H N N 306 
SER HG   H N N 307 
SER HXT  H N N 308 
THR N    N N N 309 
THR CA   C N S 310 
THR C    C N N 311 
THR O    O N N 312 
THR CB   C N R 313 
THR OG1  O N N 314 
THR CG2  C N N 315 
THR OXT  O N N 316 
THR H    H N N 317 
THR H2   H N N 318 
THR HA   H N N 319 
THR HB   H N N 320 
THR HG1  H N N 321 
THR HG21 H N N 322 
THR HG22 H N N 323 
THR HG23 H N N 324 
THR HXT  H N N 325 
TJQ C1   C Y N 326 
TJQ C2   C Y N 327 
TJQ C3   C Y N 328 
TJQ C12  C N N 329 
TJQ C15  C N N 330 
TJQ C16  C Y N 331 
TJQ C17  C Y N 332 
TJQ C19  C Y N 333 
TJQ C20  C N N 334 
TJQ C22  C N N 335 
TJQ C23  C Y N 336 
TJQ C24  C N N 337 
TJQ C25  C N N 338 
TJQ C26  C N N 339 
TJQ C27  C N N 340 
TJQ N4   N Y N 341 
TJQ C5   C Y N 342 
TJQ C6   C N N 343 
TJQ C7   C N N 344 
TJQ N8   N N N 345 
TJQ C9   C Y N 346 
TJQ C10  C Y N 347 
TJQ O11  O N N 348 
TJQ O13  O N N 349 
TJQ O14  O N N 350 
TJQ O18  O N N 351 
TJQ O21  O N N 352 
TJQ H1   H N N 353 
TJQ H2   H N N 354 
TJQ H3   H N N 355 
TJQ H4   H N N 356 
TJQ H5   H N N 357 
TJQ H6   H N N 358 
TJQ H7   H N N 359 
TJQ H8   H N N 360 
TJQ H9   H N N 361 
TJQ H10  H N N 362 
TJQ H11  H N N 363 
TJQ H12  H N N 364 
TJQ H13  H N N 365 
TJQ H14  H N N 366 
TJQ H15  H N N 367 
TJQ H16  H N N 368 
TJQ H17  H N N 369 
TJQ H18  H N N 370 
TJQ H19  H N N 371 
TJQ H20  H N N 372 
TJQ H21  H N N 373 
TJQ H22  H N N 374 
TJQ H23  H N N 375 
TJQ H24  H N N 376 
TRP N    N N N 377 
TRP CA   C N S 378 
TRP C    C N N 379 
TRP O    O N N 380 
TRP CB   C N N 381 
TRP CG   C Y N 382 
TRP CD1  C Y N 383 
TRP CD2  C Y N 384 
TRP NE1  N Y N 385 
TRP CE2  C Y N 386 
TRP CE3  C Y N 387 
TRP CZ2  C Y N 388 
TRP CZ3  C Y N 389 
TRP CH2  C Y N 390 
TRP OXT  O N N 391 
TRP H    H N N 392 
TRP H2   H N N 393 
TRP HA   H N N 394 
TRP HB2  H N N 395 
TRP HB3  H N N 396 
TRP HD1  H N N 397 
TRP HE1  H N N 398 
TRP HE3  H N N 399 
TRP HZ2  H N N 400 
TRP HZ3  H N N 401 
TRP HH2  H N N 402 
TRP HXT  H N N 403 
TYR N    N N N 404 
TYR CA   C N S 405 
TYR C    C N N 406 
TYR O    O N N 407 
TYR CB   C N N 408 
TYR CG   C Y N 409 
TYR CD1  C Y N 410 
TYR CD2  C Y N 411 
TYR CE1  C Y N 412 
TYR CE2  C Y N 413 
TYR CZ   C Y N 414 
TYR OH   O N N 415 
TYR OXT  O N N 416 
TYR H    H N N 417 
TYR H2   H N N 418 
TYR HA   H N N 419 
TYR HB2  H N N 420 
TYR HB3  H N N 421 
TYR HD1  H N N 422 
TYR HD2  H N N 423 
TYR HE1  H N N 424 
TYR HE2  H N N 425 
TYR HH   H N N 426 
TYR HXT  H N N 427 
VAL N    N N N 428 
VAL CA   C N S 429 
VAL C    C N N 430 
VAL O    O N N 431 
VAL CB   C N N 432 
VAL CG1  C N N 433 
VAL CG2  C N N 434 
VAL OXT  O N N 435 
VAL H    H N N 436 
VAL H2   H N N 437 
VAL HA   H N N 438 
VAL HB   H N N 439 
VAL HG11 H N N 440 
VAL HG12 H N N 441 
VAL HG13 H N N 442 
VAL HG21 H N N 443 
VAL HG22 H N N 444 
VAL HG23 H N N 445 
VAL HXT  H N N 446 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PO4 P   O1   doub N N 260 
PO4 P   O2   sing N N 261 
PO4 P   O3   sing N N 262 
PO4 P   O4   sing N N 263 
PRO N   CA   sing N N 264 
PRO N   CD   sing N N 265 
PRO N   H    sing N N 266 
PRO CA  C    sing N N 267 
PRO CA  CB   sing N N 268 
PRO CA  HA   sing N N 269 
PRO C   O    doub N N 270 
PRO C   OXT  sing N N 271 
PRO CB  CG   sing N N 272 
PRO CB  HB2  sing N N 273 
PRO CB  HB3  sing N N 274 
PRO CG  CD   sing N N 275 
PRO CG  HG2  sing N N 276 
PRO CG  HG3  sing N N 277 
PRO CD  HD2  sing N N 278 
PRO CD  HD3  sing N N 279 
PRO OXT HXT  sing N N 280 
SER N   CA   sing N N 281 
SER N   H    sing N N 282 
SER N   H2   sing N N 283 
SER CA  C    sing N N 284 
SER CA  CB   sing N N 285 
SER CA  HA   sing N N 286 
SER C   O    doub N N 287 
SER C   OXT  sing N N 288 
SER CB  OG   sing N N 289 
SER CB  HB2  sing N N 290 
SER CB  HB3  sing N N 291 
SER OG  HG   sing N N 292 
SER OXT HXT  sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TJQ C27 C25  sing N N 310 
TJQ C26 C24  sing N N 311 
TJQ C24 N8   sing N N 312 
TJQ C25 O21  sing N N 313 
TJQ C20 C3   sing N N 314 
TJQ O21 C7   sing N N 315 
TJQ N8  C12  sing N N 316 
TJQ N8  C6   sing N N 317 
TJQ C12 C17  sing N N 318 
TJQ C16 C17  doub Y N 319 
TJQ C16 C9   sing Y N 320 
TJQ O11 C15  sing N N 321 
TJQ O11 C9   sing N N 322 
TJQ C15 O14  sing N N 323 
TJQ C17 C23  sing Y N 324 
TJQ C3  C2   sing Y N 325 
TJQ C3  C1   doub Y N 326 
TJQ C9  C10  doub Y N 327 
TJQ C7  C2   sing N N 328 
TJQ C7  O18  doub N N 329 
TJQ C23 C19  doub Y N 330 
TJQ C10 O14  sing N N 331 
TJQ C10 C19  sing Y N 332 
TJQ C2  C5   doub Y N 333 
TJQ C6  C1   sing N N 334 
TJQ C6  O13  doub N N 335 
TJQ C1  N4   sing Y N 336 
TJQ C5  N4   sing Y N 337 
TJQ C5  C22  sing N N 338 
TJQ C12 H1   sing N N 339 
TJQ C12 H2   sing N N 340 
TJQ C15 H3   sing N N 341 
TJQ C15 H4   sing N N 342 
TJQ C16 H5   sing N N 343 
TJQ C19 H6   sing N N 344 
TJQ C20 H7   sing N N 345 
TJQ C20 H8   sing N N 346 
TJQ C20 H9   sing N N 347 
TJQ C22 H10  sing N N 348 
TJQ C22 H11  sing N N 349 
TJQ C22 H12  sing N N 350 
TJQ C23 H13  sing N N 351 
TJQ C24 H14  sing N N 352 
TJQ C24 H15  sing N N 353 
TJQ C25 H16  sing N N 354 
TJQ C25 H17  sing N N 355 
TJQ C26 H18  sing N N 356 
TJQ C26 H19  sing N N 357 
TJQ C26 H20  sing N N 358 
TJQ C27 H21  sing N N 359 
TJQ C27 H22  sing N N 360 
TJQ C27 H23  sing N N 361 
TJQ N4  H24  sing N N 362 
TRP N   CA   sing N N 363 
TRP N   H    sing N N 364 
TRP N   H2   sing N N 365 
TRP CA  C    sing N N 366 
TRP CA  CB   sing N N 367 
TRP CA  HA   sing N N 368 
TRP C   O    doub N N 369 
TRP C   OXT  sing N N 370 
TRP CB  CG   sing N N 371 
TRP CB  HB2  sing N N 372 
TRP CB  HB3  sing N N 373 
TRP CG  CD1  doub Y N 374 
TRP CG  CD2  sing Y N 375 
TRP CD1 NE1  sing Y N 376 
TRP CD1 HD1  sing N N 377 
TRP CD2 CE2  doub Y N 378 
TRP CD2 CE3  sing Y N 379 
TRP NE1 CE2  sing Y N 380 
TRP NE1 HE1  sing N N 381 
TRP CE2 CZ2  sing Y N 382 
TRP CE3 CZ3  doub Y N 383 
TRP CE3 HE3  sing N N 384 
TRP CZ2 CH2  doub Y N 385 
TRP CZ2 HZ2  sing N N 386 
TRP CZ3 CH2  sing Y N 387 
TRP CZ3 HZ3  sing N N 388 
TRP CH2 HH2  sing N N 389 
TRP OXT HXT  sing N N 390 
TYR N   CA   sing N N 391 
TYR N   H    sing N N 392 
TYR N   H2   sing N N 393 
TYR CA  C    sing N N 394 
TYR CA  CB   sing N N 395 
TYR CA  HA   sing N N 396 
TYR C   O    doub N N 397 
TYR C   OXT  sing N N 398 
TYR CB  CG   sing N N 399 
TYR CB  HB2  sing N N 400 
TYR CB  HB3  sing N N 401 
TYR CG  CD1  doub Y N 402 
TYR CG  CD2  sing Y N 403 
TYR CD1 CE1  sing Y N 404 
TYR CD1 HD1  sing N N 405 
TYR CD2 CE2  doub Y N 406 
TYR CD2 HD2  sing N N 407 
TYR CE1 CZ   doub Y N 408 
TYR CE1 HE1  sing N N 409 
TYR CE2 CZ   sing Y N 410 
TYR CE2 HE2  sing N N 411 
TYR CZ  OH   sing N N 412 
TYR OH  HH   sing N N 413 
TYR OXT HXT  sing N N 414 
VAL N   CA   sing N N 415 
VAL N   H    sing N N 416 
VAL N   H2   sing N N 417 
VAL CA  C    sing N N 418 
VAL CA  CB   sing N N 419 
VAL CA  HA   sing N N 420 
VAL C   O    doub N N 421 
VAL C   OXT  sing N N 422 
VAL CB  CG1  sing N N 423 
VAL CB  CG2  sing N N 424 
VAL CB  HB   sing N N 425 
VAL CG1 HG11 sing N N 426 
VAL CG1 HG12 sing N N 427 
VAL CG1 HG13 sing N N 428 
VAL CG2 HG21 sing N N 429 
VAL CG2 HG22 sing N N 430 
VAL CG2 HG23 sing N N 431 
VAL OXT HXT  sing N N 432 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1zvd 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FSH 
_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]   0.019036 
_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]   0.013937 
_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]   0.006552 
_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   . LYS A 1 120 ? -2.817  -9.712  26.504  1 65.05 ? 369  LYS A N   1 
ATOM   2    C CA  . LYS A 1 120 ? -1.9    -9.422  27.607  1 65.41 ? 369  LYS A CA  1 
ATOM   3    C C   . LYS A 1 120 ? -0.631  -10.272 27.493  1 65.22 ? 369  LYS A C   1 
ATOM   4    O O   . LYS A 1 120 ? 0.476   -9.765  27.697  1 65.4  ? 369  LYS A O   1 
ATOM   5    C CB  . LYS A 1 120 ? -2.58   -9.662  28.974  1 67.47 ? 369  LYS A CB  1 
ATOM   6    C CG  . LYS A 1 120 ? -3.406  -8.483  29.488  1 71.83 ? 369  LYS A CG  1 
ATOM   7    C CD  . LYS A 1 120 ? -4.869  -8.556  29.054  1 75.92 ? 369  LYS A CD  1 
ATOM   8    C CE  . LYS A 1 120 ? -5.647  -7.345  29.515  1 79.69 ? 369  LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 120 ? -7.087  -7.419  29.139  1 81.66 ? 369  LYS A NZ  1 
ATOM   10   N N   . ARG A 1 121 ? -0.802  -11.57  27.18   1 64.45 ? 370  ARG A N   1 
ATOM   11   C CA  . ARG A 1 121 ? 0.295   -12.528 27.039  1 64.04 ? 370  ARG A CA  1 
ATOM   12   C C   . ARG A 1 121 ? 1.295   -12.082 25.968  1 62.42 ? 370  ARG A C   1 
ATOM   13   O O   . ARG A 1 121 ? 2.503   -12.082 26.221  1 62.9  ? 370  ARG A O   1 
ATOM   14   C CB  . ARG A 1 121 ? -0.265  -13.935 26.729  1 66    ? 370  ARG A CB  1 
ATOM   15   C CG  . ARG A 1 121 ? 0.775   -14.976 26.314  1 69.75 ? 370  ARG A CG  1 
ATOM   16   C CD  . ARG A 1 121 ? 1.494   -15.601 27.499  1 73.58 ? 370  ARG A CD  1 
ATOM   17   N NE  . ARG A 1 121 ? 2.402   -16.662 27.06   1 76.43 ? 370  ARG A NE  1 
ATOM   18   C CZ  . ARG A 1 121 ? 2.046   -17.931 26.879  1 78.43 ? 370  ARG A CZ  1 
ATOM   19   N NH1 . ARG A 1 121 ? 0.803   -18.323 27.133  1 78.42 ? 370  ARG A NH1 1 
ATOM   20   N NH2 . ARG A 1 121 ? 2.932   -18.817 26.452  1 78.11 ? 370  ARG A NH2 1 
ATOM   21   N N   . ASP A 1 122 ? 0.79    -11.679 24.791  1 60.39 ? 371  ASP A N   1 
ATOM   22   C CA  . ASP A 1 122 ? 1.612   -11.231 23.668  1 58.9  ? 371  ASP A CA  1 
ATOM   23   C C   . ASP A 1 122 ? 2.534   -10.071 24.082  1 56.12 ? 371  ASP A C   1 
ATOM   24   O O   . ASP A 1 122 ? 3.735   -10.123 23.821  1 55.8  ? 371  ASP A O   1 
ATOM   25   C CB  . ASP A 1 122 ? 0.72    -10.818 22.485  1 61.73 ? 371  ASP A CB  1 
ATOM   26   C CG  . ASP A 1 122 ? -0.372  -11.822 22.135  1 68.92 ? 371  ASP A CG  1 
ATOM   27   O OD1 . ASP A 1 122 ? -1.311  -12.003 22.964  1 70.25 ? 371  ASP A OD1 1 
ATOM   28   O OD2 . ASP A 1 122 ? -0.308  -12.408 21.024  1 71.4  ? 371  ASP A OD2 1 
ATOM   29   N N   . LEU A 1 123 ? 1.973   -9.064  24.777  1 53.77 ? 372  LEU A N   1 
ATOM   30   C CA  . LEU A 1 123 ? 2.704   -7.895  25.266  1 51.89 ? 372  LEU A CA  1 
ATOM   31   C C   . LEU A 1 123 ? 3.75    -8.285  26.315  1 50.21 ? 372  LEU A C   1 
ATOM   32   O O   . LEU A 1 123 ? 4.881   -7.812  26.251  1 49.57 ? 372  LEU A O   1 
ATOM   33   C CB  . LEU A 1 123 ? 1.726   -6.856  25.846  1 51.58 ? 372  LEU A CB  1 
ATOM   34   C CG  . LEU A 1 123 ? 2.353   -5.618  26.482  1 52.39 ? 372  LEU A CG  1 
ATOM   35   C CD1 . LEU A 1 123 ? 3.183   -4.848  25.477  1 52.7  ? 372  LEU A CD1 1 
ATOM   36   C CD2 . LEU A 1 123 ? 1.298   -4.718  27.071  1 52.94 ? 372  LEU A CD2 1 
ATOM   37   N N   . VAL A 1 124 ? 3.388   -9.154  27.274  1 49.3  ? 373  VAL A N   1 
ATOM   38   C CA  . VAL A 1 124 ? 4.325   -9.603  28.309  1 49.1  ? 373  VAL A CA  1 
ATOM   39   C C   . VAL A 1 124 ? 5.539   -10.299 27.655  1 47.55 ? 373  VAL A C   1 
ATOM   40   O O   . VAL A 1 124 ? 6.68    -10.034 28.025  1 47.86 ? 373  VAL A O   1 
ATOM   41   C CB  . VAL A 1 124 ? 3.588   -10.475 29.376  1 50.87 ? 373  VAL A CB  1 
ATOM   42   C CG1 . VAL A 1 124 ? 4.474   -11.577 29.963  1 51.83 ? 373  VAL A CG1 1 
ATOM   43   C CG2 . VAL A 1 124 ? 3.007   -9.606  30.483  1 51.35 ? 373  VAL A CG2 1 
ATOM   44   N N   . GLN A 1 125 ? 5.284   -11.115 26.631  1 46.06 ? 374  GLN A N   1 
ATOM   45   C CA  . GLN A 1 125 ? 6.35    -11.811 25.924  1 45.07 ? 374  GLN A CA  1 
ATOM   46   C C   . GLN A 1 125 ? 7.272   -10.834 25.173  1 43.02 ? 374  GLN A C   1 
ATOM   47   O O   . GLN A 1 125 ? 8.488   -10.949 25.306  1 43.06 ? 374  GLN A O   1 
ATOM   48   C CB  . GLN A 1 125 ? 5.773   -12.898 25      1 47    ? 374  GLN A CB  1 
ATOM   49   C CG  . GLN A 1 125 ? 5.245   -14.115 25.768  1 50.98 ? 374  GLN A CG  1 
ATOM   50   C CD  . GLN A 1 125 ? 5.467   -15.388 24.984  1 56.86 ? 374  GLN A CD  1 
ATOM   51   O OE1 . GLN A 1 125 ? 5.408   -15.398 23.744  1 59.61 ? 374  GLN A OE1 1 
ATOM   52   N NE2 . GLN A 1 125 ? 5.743   -16.491 25.685  1 56.57 ? 374  GLN A NE2 1 
ATOM   53   N N   . LYS A 1 126 ? 6.697   -9.834  24.445  1 40.63 ? 375  LYS A N   1 
ATOM   54   C CA  . LYS A 1 126 ? 7.473   -8.813  23.73   1 38.59 ? 375  LYS A CA  1 
ATOM   55   C C   . LYS A 1 126 ? 8.341   -8.012  24.694  1 35.98 ? 375  LYS A C   1 
ATOM   56   O O   . LYS A 1 126 ? 9.483   -7.687  24.36   1 35.56 ? 375  LYS A O   1 
ATOM   57   C CB  . LYS A 1 126 ? 6.554   -7.852  22.961  1 39.81 ? 375  LYS A CB  1 
ATOM   58   C CG  . LYS A 1 126 ? 5.827   -8.515  21.814  1 43.65 ? 375  LYS A CG  1 
ATOM   59   C CD  . LYS A 1 126 ? 4.994   -7.519  21.039  1 47.69 ? 375  LYS A CD  1 
ATOM   60   C CE  . LYS A 1 126 ? 4.081   -8.186  20.053  1 51.75 ? 375  LYS A CE  1 
ATOM   61   N NZ  . LYS A 1 126 ? 3.271   -7.188  19.315  1 54.53 ? 375  LYS A NZ  1 
ATOM   62   N N   . LEU A 1 127 ? 7.81    -7.703  25.88   1 34.78 ? 376  LEU A N   1 
ATOM   63   C CA  . LEU A 1 127 ? 8.558   -6.955  26.891  1 34.78 ? 376  LEU A CA  1 
ATOM   64   C C   . LEU A 1 127 ? 9.724   -7.776  27.442  1 35.51 ? 376  LEU A C   1 
ATOM   65   O O   . LEU A 1 127 ? 10.778  -7.219  27.691  1 35.16 ? 376  LEU A O   1 
ATOM   66   C CB  . LEU A 1 127 ? 7.653   -6.497  28.023  1 34.73 ? 376  LEU A CB  1 
ATOM   67   C CG  . LEU A 1 127 ? 6.673   -5.364  27.677  1 36.18 ? 376  LEU A CG  1 
ATOM   68   C CD1 . LEU A 1 127 ? 5.661   -5.18   28.801  1 36.8  ? 376  LEU A CD1 1 
ATOM   69   C CD2 . LEU A 1 127 ? 7.423   -4.045  27.412  1 36.01 ? 376  LEU A CD2 1 
ATOM   70   N N   . LYS A 1 128 ? 9.559   -9.108  27.565  1 36.1  ? 377  LYS A N   1 
ATOM   71   C CA  . LYS A 1 128 ? 10.635  -9.986  28.034  1 36.19 ? 377  LYS A CA  1 
ATOM   72   C C   . LYS A 1 128 ? 11.744  -10.022 27.012  1 35.32 ? 377  LYS A C   1 
ATOM   73   O O   . LYS A 1 128 ? 12.914  -9.976  27.383  1 36.01 ? 377  LYS A O   1 
ATOM   74   C CB  . LYS A 1 128 ? 10.11   -11.411 28.283  1 38.46 ? 377  LYS A CB  1 
ATOM   75   C CG  . LYS A 1 128 ? 9.307   -11.55  29.567  1 43.55 ? 377  LYS A CG  1 
ATOM   76   C CD  . LYS A 1 128 ? 8.797   -12.979 29.716  1 49.22 ? 377  LYS A CD  1 
ATOM   77   C CE  . LYS A 1 128 ? 8.27    -13.243 31.1    1 54.62 ? 377  LYS A CE  1 
ATOM   78   N NZ  . LYS A 1 128 ? 7.838   -14.651 31.26   1 58.5  ? 377  LYS A NZ  1 
ATOM   79   N N   . ILE A 1 129 ? 11.387  -10.107 25.728  1 34.42 ? 378  ILE A N   1 
ATOM   80   C CA  . ILE A 1 129 ? 12.347  -10.11  24.637  1 34.88 ? 378  ILE A CA  1 
ATOM   81   C C   . ILE A 1 129 ? 13.092  -8.778  24.614  1 35.48 ? 378  ILE A C   1 
ATOM   82   O O   . ILE A 1 129 ? 14.332  -8.756  24.566  1 36.13 ? 378  ILE A O   1 
ATOM   83   C CB  . ILE A 1 129 ? 11.625  -10.39  23.299  1 35.56 ? 378  ILE A CB  1 
ATOM   84   C CG1 . ILE A 1 129 ? 11.075  -11.847 23.28   1 37.39 ? 378  ILE A CG1 1 
ATOM   85   C CG2 . ILE A 1 129 ? 12.555  -10.128 22.112  1 35.63 ? 378  ILE A CG2 1 
ATOM   86   C CD1 . ILE A 1 129 ? 10.299  -12.254 21.989  1 38.28 ? 378  ILE A CD1 1 
ATOM   87   N N   . LEU A 1 130 ? 12.338  -7.66   24.717  1 34.56 ? 379  LEU A N   1 
ATOM   88   C CA  . LEU A 1 130 ? 12.957  -6.336  24.735  1 34.44 ? 379  LEU A CA  1 
ATOM   89   C C   . LEU A 1 130 ? 13.975  -6.182  25.875  1 34.25 ? 379  LEU A C   1 
ATOM   90   O O   . LEU A 1 130 ? 15.101  -5.774  25.606  1 33.75 ? 379  LEU A O   1 
ATOM   91   C CB  . LEU A 1 130 ? 11.89   -5.229  24.796  1 34.16 ? 379  LEU A CB  1 
ATOM   92   C CG  . LEU A 1 130 ? 12.428  -3.81   24.857  1 35.29 ? 379  LEU A CG  1 
ATOM   93   C CD1 . LEU A 1 130 ? 13.199  -3.458  23.596  1 35.41 ? 379  LEU A CD1 1 
ATOM   94   C CD2 . LEU A 1 130 ? 11.318  -2.847  25.086  1 36.09 ? 379  LEU A CD2 1 
ATOM   95   N N   . ARG A 1 131 ? 13.605  -6.56   27.115  1 35.02 ? 380  ARG A N   1 
ATOM   96   C CA  . ARG A 1 131 ? 14.515  -6.448  28.26   1 37.45 ? 380  ARG A CA  1 
ATOM   97   C C   . ARG A 1 131 ? 15.785  -7.283  28.024  1 38.56 ? 380  ARG A C   1 
ATOM   98   O O   . ARG A 1 131 ? 16.888  -6.817  28.292  1 38.67 ? 380  ARG A O   1 
ATOM   99   C CB  . ARG A 1 131 ? 13.841  -6.909  29.567  1 40.34 ? 380  ARG A CB  1 
ATOM   100  C CG  . ARG A 1 131 ? 12.483  -6.292  29.872  1 46.28 ? 380  ARG A CG  1 
ATOM   101  C CD  . ARG A 1 131 ? 12.524  -4.977  30.644  1 50.9  ? 380  ARG A CD  1 
ATOM   102  N NE  . ARG A 1 131 ? 11.831  -3.941  29.882  1 54.29 ? 380  ARG A NE  1 
ATOM   103  C CZ  . ARG A 1 131 ? 12.299  -2.721  29.667  1 54.92 ? 380  ARG A CZ  1 
ATOM   104  N NH1 . ARG A 1 131 ? 13.452  -2.343  30.199  1 54.5  ? 380  ARG A NH1 1 
ATOM   105  N NH2 . ARG A 1 131 ? 11.618  -1.869  28.922  1 55.22 ? 380  ARG A NH2 1 
ATOM   106  N N   . GLN A 1 132 ? 15.616  -8.499  27.474  1 39.15 ? 381  GLN A N   1 
ATOM   107  C CA  . GLN A 1 132 ? 16.719  -9.408  27.169  1 39.78 ? 381  GLN A CA  1 
ATOM   108  C C   . GLN A 1 132 ? 17.669  -8.778  26.159  1 39.88 ? 381  GLN A C   1 
ATOM   109  O O   . GLN A 1 132 ? 18.877  -8.813  26.371  1 39.85 ? 381  GLN A O   1 
ATOM   110  C CB  . GLN A 1 132 ? 16.172  -10.75  26.629  1 42.15 ? 381  GLN A CB  1 
ATOM   111  C CG  . GLN A 1 132 ? 17.174  -11.899 26.68   1 47.22 ? 381  GLN A CG  1 
ATOM   112  C CD  . GLN A 1 132 ? 17.402  -12.337 28.113  1 53.72 ? 381  GLN A CD  1 
ATOM   113  O OE1 . GLN A 1 132 ? 16.518  -12.936 28.765  1 56.21 ? 381  GLN A OE1 1 
ATOM   114  N NE2 . GLN A 1 132 ? 18.586  -12.038 28.639  1 53.64 ? 381  GLN A NE2 1 
ATOM   115  N N   . GLU A 1 133 ? 17.14   -8.207  25.058  1 39.82 ? 382  GLU A N   1 
ATOM   116  C CA  . GLU A 1 133 ? 17.991  -7.582  24.046  1 40.69 ? 382  GLU A CA  1 
ATOM   117  C C   . GLU A 1 133 ? 18.73   -6.35   24.6    1 41.32 ? 382  GLU A C   1 
ATOM   118  O O   . GLU A 1 133 ? 19.882  -6.117  24.237  1 41.01 ? 382  GLU A O   1 
ATOM   119  C CB  . GLU A 1 133 ? 17.173  -7.168  22.806  1 43.57 ? 382  GLU A CB  1 
ATOM   120  C CG  . GLU A 1 133 ? 16.507  -8.308  22.053  1 50.56 ? 382  GLU A CG  1 
ATOM   121  C CD  . GLU A 1 133 ? 17.415  -9.107  21.136  1 62.21 ? 382  GLU A CD  1 
ATOM   122  O OE1 . GLU A 1 133 ? 18.396  -9.705  21.639  1 64.39 ? 382  GLU A OE1 1 
ATOM   123  O OE2 . GLU A 1 133 ? 17.15   -9.134  19.91   1 66.23 ? 382  GLU A OE2 1 
ATOM   124  N N   . LEU A 1 134 ? 18.056  -5.553  25.457  1 41.52 ? 383  LEU A N   1 
ATOM   125  C CA  . LEU A 1 134 ? 18.672  -4.355  26.023  1 42.39 ? 383  LEU A CA  1 
ATOM   126  C C   . LEU A 1 134 ? 19.775  -4.708  27.02   1 43.6  ? 383  LEU A C   1 
ATOM   127  O O   . LEU A 1 134 ? 20.772  -4.003  27.077  1 43.42 ? 383  LEU A O   1 
ATOM   128  C CB  . LEU A 1 134 ? 17.629  -3.413  26.653  1 41.89 ? 383  LEU A CB  1 
ATOM   129  C CG  . LEU A 1 134 ? 16.639  -2.757  25.68   1 42.64 ? 383  LEU A CG  1 
ATOM   130  C CD1 . LEU A 1 134 ? 15.554  -2.006  26.428  1 42.92 ? 383  LEU A CD1 1 
ATOM   131  C CD2 . LEU A 1 134 ? 17.342  -1.828  24.698  1 42.93 ? 383  LEU A CD2 1 
ATOM   132  N N   . SER A 1 135 ? 19.634  -5.825  27.76   1 44.78 ? 384  SER A N   1 
ATOM   133  C CA  . SER A 1 135 ? 20.675  -6.238  28.714  1 46.42 ? 384  SER A CA  1 
ATOM   134  C C   . SER A 1 135 ? 22.004  -6.554  27.993  1 47.31 ? 384  SER A C   1 
ATOM   135  O O   . SER A 1 135 ? 23.072  -6.301  28.545  1 47.84 ? 384  SER A O   1 
ATOM   136  C CB  . SER A 1 135 ? 20.213  -7.428  29.55   1 48.19 ? 384  SER A CB  1 
ATOM   137  O OG  . SER A 1 135 ? 20.275  -8.621  28.784  1 51.91 ? 384  SER A OG  1 
ATOM   138  N N   . GLN A 1 136 ? 21.926  -7.059  26.748  1 47.01 ? 385  GLN A N   1 
ATOM   139  C CA  . GLN A 1 136 ? 23.078  -7.361  25.905  1 47.48 ? 385  GLN A CA  1 
ATOM   140  C C   . GLN A 1 136 ? 23.816  -6.083  25.504  1 46.91 ? 385  GLN A C   1 
ATOM   141  O O   . GLN A 1 136 ? 25.039  -6.073  25.383  1 46.92 ? 385  GLN A O   1 
ATOM   142  C CB  . GLN A 1 136 ? 22.623  -8.116  24.642  1 50.36 ? 385  GLN A CB  1 
ATOM   143  C CG  . GLN A 1 136 ? 22.694  -9.633  24.781  1 56.26 ? 385  GLN A CG  1 
ATOM   144  C CD  . GLN A 1 136 ? 24.129  -10.096 24.952  1 63.16 ? 385  GLN A CD  1 
ATOM   145  O OE1 . GLN A 1 136 ? 24.958  -10.022 24.024  1 65.15 ? 385  GLN A OE1 1 
ATOM   146  N NE2 . GLN A 1 136 ? 24.452  -10.59  26.148  1 63.69 ? 385  GLN A NE2 1 
ATOM   147  N N   . GLN A 1 137 ? 23.07   -5.005  25.268  1 46.25 ? 386  GLN A N   1 
ATOM   148  C CA  . GLN A 1 137 ? 23.638  -3.71   24.916  1 45.29 ? 386  GLN A CA  1 
ATOM   149  C C   . GLN A 1 137 ? 24.476  -3.139  26.084  1 44.61 ? 386  GLN A C   1 
ATOM   150  O O   . GLN A 1 137 ? 25.426  -2.405  25.842  1 45.01 ? 386  GLN A O   1 
ATOM   151  C CB  . GLN A 1 137 ? 22.497  -2.756  24.553  1 45.61 ? 386  GLN A CB  1 
ATOM   152  C CG  . GLN A 1 137 ? 22.929  -1.419  24.028  1 47.01 ? 386  GLN A CG  1 
ATOM   153  C CD  . GLN A 1 137 ? 21.699  -0.617  23.692  1 49.12 ? 386  GLN A CD  1 
ATOM   154  O OE1 . GLN A 1 137 ? 20.927  -0.972  22.786  1 48.93 ? 386  GLN A OE1 1 
ATOM   155  N NE2 . GLN A 1 137 ? 21.486  0.464   24.434  1 48.36 ? 386  GLN A NE2 1 
ATOM   156  N N   . GLN A 1 138 ? 24.123  -3.473  27.332  1 43.82 ? 387  GLN A N   1 
ATOM   157  C CA  . GLN A 1 138 ? 24.848  -3.011  28.504  1 43.87 ? 387  GLN A CA  1 
ATOM   158  C C   . GLN A 1 138 ? 26.237  -3.631  28.587  1 44.44 ? 387  GLN A C   1 
ATOM   159  O O   . GLN A 1 138 ? 26.373  -4.848  28.745  1 44.16 ? 387  GLN A O   1 
ATOM   160  C CB  . GLN A 1 138 ? 24.073  -3.308  29.802  1 44.35 ? 387  GLN A CB  1 
ATOM   161  C CG  . GLN A 1 138 ? 24.848  -2.927  31.077  1 45.07 ? 387  GLN A CG  1 
ATOM   162  C CD  . GLN A 1 138 ? 23.956  -2.66   32.254  1 47.36 ? 387  GLN A CD  1 
ATOM   163  O OE1 . GLN A 1 138 ? 23.606  -3.556  33.023  1 49.02 ? 387  GLN A OE1 1 
ATOM   164  N NE2 . GLN A 1 138 ? 23.585  -1.41   32.437  1 47.51 ? 387  GLN A NE2 1 
ATOM   165  N N   . PRO A 1 139 ? 27.279  -2.78   28.578  1 44.71 ? 388  PRO A N   1 
ATOM   166  C CA  . PRO A 1 139 ? 28.645  -3.294  28.742  1 44.59 ? 388  PRO A CA  1 
ATOM   167  C C   . PRO A 1 139 ? 28.819  -4.03   30.068  1 43.99 ? 388  PRO A C   1 
ATOM   168  O O   . PRO A 1 139 ? 28.159  -3.729  31.059  1 43.62 ? 388  PRO A O   1 
ATOM   169  C CB  . PRO A 1 139 ? 29.505  -2.019  28.716  1 45.51 ? 388  PRO A CB  1 
ATOM   170  C CG  . PRO A 1 139 ? 28.667  -1.006  28.004  1 46.13 ? 388  PRO A CG  1 
ATOM   171  C CD  . PRO A 1 139 ? 27.268  -1.312  28.444  1 44.35 ? 388  PRO A CD  1 
ATOM   172  N N   . GLN A 1 140 ? 29.689  -5.022  30.063  1 43.91 ? 389  GLN A N   1 
ATOM   173  C CA  . GLN A 1 140 ? 30.001  -5.807  31.241  1 44.22 ? 389  GLN A CA  1 
ATOM   174  C C   . GLN A 1 140 ? 30.818  -4.943  32.24   1 42.23 ? 389  GLN A C   1 
ATOM   175  O O   . GLN A 1 140 ? 30.582  -4.993  33.443  1 42.31 ? 389  GLN A O   1 
ATOM   176  C CB  . GLN A 1 140 ? 30.805  -7.043  30.798  1 48.35 ? 389  GLN A CB  1 
ATOM   177  C CG  . GLN A 1 140 ? 31.122  -8.003  31.922  1 56.66 ? 389  GLN A CG  1 
ATOM   178  C CD  . GLN A 1 140 ? 29.884  -8.725  32.387  1 65.95 ? 389  GLN A CD  1 
ATOM   179  O OE1 . GLN A 1 140 ? 28.968  -9.025  31.601  1 68.98 ? 389  GLN A OE1 1 
ATOM   180  N NE2 . GLN A 1 140 ? 29.838  -9.035  33.679  1 67.22 ? 389  GLN A NE2 1 
ATOM   181  N N   . ALA A 1 141 ? 31.733  -4.12   31.723  1 40.19 ? 390  ALA A N   1 
ATOM   182  C CA  . ALA A 1 141 ? 32.591  -3.273  32.536  1 38.99 ? 390  ALA A CA  1 
ATOM   183  C C   . ALA A 1 141 ? 32.201  -1.776  32.444  1 37.36 ? 390  ALA A C   1 
ATOM   184  O O   . ALA A 1 141 ? 31.506  -1.367  31.512  1 37.54 ? 390  ALA A O   1 
ATOM   185  C CB  . ALA A 1 141 ? 34.042  -3.462  32.088  1 38.85 ? 390  ALA A CB  1 
ATOM   186  N N   . GLY A 1 142 ? 32.658  -0.986  33.412  1 35.57 ? 391  GLY A N   1 
ATOM   187  C CA  . GLY A 1 142 ? 32.462  0.452   33.42   1 34.32 ? 391  GLY A CA  1 
ATOM   188  C C   . GLY A 1 142 ? 31.153  0.879   34.033  1 32.57 ? 391  GLY A C   1 
ATOM   189  O O   . GLY A 1 142 ? 30.26   0.063   34.252  1 32.33 ? 391  GLY A O   1 
ATOM   190  N N   . HIS A 1 143 ? 31.053  2.167   34.332  1 31.32 ? 392  HIS A N   1 
ATOM   191  C CA  . HIS A 1 143 ? 29.871  2.757   34.944  1 30.27 ? 392  HIS A CA  1 
ATOM   192  C C   . HIS A 1 143 ? 29.549  4.111   34.304  1 29.07 ? 392  HIS A C   1 
ATOM   193  O O   . HIS A 1 143 ? 30.423  4.758   33.73   1 28.29 ? 392  HIS A O   1 
ATOM   194  C CB  . HIS A 1 143 ? 30.09   2.978   36.454  1 30.63 ? 392  HIS A CB  1 
ATOM   195  C CG  . HIS A 1 143 ? 30.182  1.719   37.265  1 33.54 ? 392  HIS A CG  1 
ATOM   196  N ND1 . HIS A 1 143 ? 31.384  1.053   37.427  1 35.57 ? 392  HIS A ND1 1 
ATOM   197  C CD2 . HIS A 1 143 ? 29.223  1.072   37.971  1 34.45 ? 392  HIS A CD2 1 
ATOM   198  C CE1 . HIS A 1 143 ? 31.114  0.017   38.209  1 36.09 ? 392  HIS A CE1 1 
ATOM   199  N NE2 . HIS A 1 143 ? 29.828  -0.015  38.553  1 35.75 ? 392  HIS A NE2 1 
ATOM   200  N N   . CYS A 1 144 ? 28.278  4.53    34.425  1 28.24 ? 393  CYS A N   1 
ATOM   201  C CA  . CYS A 1 144 ? 27.834  5.828   33.995  1 28.27 ? 393  CYS A CA  1 
ATOM   202  C C   . CYS A 1 144 ? 27.765  6.663   35.27   1 27.26 ? 393  CYS A C   1 
ATOM   203  O O   . CYS A 1 144 ? 26.826  6.527   36.055  1 26.44 ? 393  CYS A O   1 
ATOM   204  C CB  . CYS A 1 144 ? 26.476  5.767   33.298  1 29.28 ? 393  CYS A CB  1 
ATOM   205  S SG  . CYS A 1 144 ? 25.902  7.387   32.717  1 32.51 ? 393  CYS A SG  1 
ATOM   206  N N   . ARG A 1 145 ? 28.773  7.49    35.48   1 27.64 ? 394  ARG A N   1 
ATOM   207  C CA  . ARG A 1 145 ? 28.912  8.313   36.682  1 28.65 ? 394  ARG A CA  1 
ATOM   208  C C   . ARG A 1 145 ? 28.295  9.692   36.55   1 29.47 ? 394  ARG A C   1 
ATOM   209  O O   . ARG A 1 145 ? 28.703  10.475  35.694  1 29.08 ? 394  ARG A O   1 
ATOM   210  C CB  . ARG A 1 145 ? 30.393  8.468   37.045  1 29.5  ? 394  ARG A CB  1 
ATOM   211  C CG  . ARG A 1 145 ? 30.939  7.258   37.778  1 30.48 ? 394  ARG A CG  1 
ATOM   212  C CD  . ARG A 1 145 ? 32.437  7.331   37.846  1 31.65 ? 394  ARG A CD  1 
ATOM   213  N NE  . ARG A 1 145 ? 32.963  6.266   38.695  1 33.07 ? 394  ARG A NE  1 
ATOM   214  C CZ  . ARG A 1 145 ? 33.277  5.05    38.263  1 34.2  ? 394  ARG A CZ  1 
ATOM   215  N NH1 . ARG A 1 145 ? 33.696  4.127   39.117  1 33.7  ? 394  ARG A NH1 1 
ATOM   216  N NH2 . ARG A 1 145 ? 33.132  4.734   36.979  1 32.49 ? 394  ARG A NH2 1 
ATOM   217  N N   . ILE A 1 146 ? 27.354  10.009  37.458  1 29.77 ? 395  ILE A N   1 
ATOM   218  C CA  . ILE A 1 146 ? 26.69   11.3    37.465  1 30.07 ? 395  ILE A CA  1 
ATOM   219  C C   . ILE A 1 146 ? 26.754  11.835  38.875  1 28.95 ? 395  ILE A C   1 
ATOM   220  O O   . ILE A 1 146 ? 26.356  11.122  39.802  1 29.61 ? 395  ILE A O   1 
ATOM   221  C CB  . ILE A 1 146 ? 25.193  11.176  37.015  1 31.39 ? 395  ILE A CB  1 
ATOM   222  C CG1 . ILE A 1 146 ? 25.03   10.584  35.593  1 33.19 ? 395  ILE A CG1 1 
ATOM   223  C CG2 . ILE A 1 146 ? 24.459  12.506  37.152  1 31.86 ? 395  ILE A CG2 1 
ATOM   224  C CD1 . ILE A 1 146 ? 25.363  11.6    34.4    1 35.47 ? 395  ILE A CD1 1 
ATOM   225  N N   . GLU A 1 147 ? 27.202  13.088  39.049  1 27.44 ? 396  GLU A N   1 
ATOM   226  C CA  . GLU A 1 147 ? 27.214  13.754  40.361  1 27.32 ? 396  GLU A CA  1 
ATOM   227  C C   . GLU A 1 147 ? 26.52   15.11   40.251  1 27.1  ? 396  GLU A C   1 
ATOM   228  O O   . GLU A 1 147 ? 27.099  16.034  39.703  1 27.37 ? 396  GLU A O   1 
ATOM   229  C CB  . GLU A 1 147 ? 28.64   13.952  40.894  1 27.87 ? 396  GLU A CB  1 
ATOM   230  C CG  . GLU A 1 147 ? 28.646  14.619  42.259  1 31.01 ? 396  GLU A CG  1 
ATOM   231  C CD  . GLU A 1 147 ? 30.016  14.757  42.887  1 34.78 ? 396  GLU A CD  1 
ATOM   232  O OE1 . GLU A 1 147 ? 31.02   14.774  42.143  1 34.91 ? 396  GLU A OE1 1 
ATOM   233  O OE2 . GLU A 1 147 ? 30.088  14.838  44.131  1 37.99 ? 396  GLU A OE2 1 
ATOM   234  N N   . VAL A 1 148 ? 25.294  15.23   40.739  1 27.73 ? 397  VAL A N   1 
ATOM   235  C CA  . VAL A 1 148 ? 24.539  16.475  40.582  1 29.36 ? 397  VAL A CA  1 
ATOM   236  C C   . VAL A 1 148 ? 23.863  16.934  41.861  1 31.77 ? 397  VAL A C   1 
ATOM   237  O O   . VAL A 1 148 ? 23.491  16.106  42.681  1 31.97 ? 397  VAL A O   1 
ATOM   238  C CB  . VAL A 1 148 ? 23.492  16.343  39.429  1 29.19 ? 397  VAL A CB  1 
ATOM   239  C CG1 . VAL A 1 148 ? 24.155  16.002  38.094  1 29.84 ? 397  VAL A CG1 1 
ATOM   240  C CG2 . VAL A 1 148 ? 22.418  15.321  39.768  1 28.33 ? 397  VAL A CG2 1 
ATOM   241  N N   . SER A 1 149 ? 23.645  18.252  42.011  1 33.66 ? 398  SER A N   1 
ATOM   242  C CA  . SER A 1 149 ? 22.882  18.737  43.164  1 35.9  ? 398  SER A CA  1 
ATOM   243  C C   . SER A 1 149 ? 21.395  18.493  42.892  1 36.94 ? 398  SER A C   1 
ATOM   244  O O   . SER A 1 149 ? 20.973  18.505  41.726  1 37    ? 398  SER A O   1 
ATOM   245  C CB  . SER A 1 149 ? 23.131  20.224  43.402  1 38.59 ? 398  SER A CB  1 
ATOM   246  O OG  . SER A 1 149 ? 22.511  21.018  42.405  1 42.21 ? 398  SER A OG  1 
ATOM   247  N N   . ARG A 1 150 ? 20.596  18.282  43.952  1 37.4  ? 399  ARG A N   1 
ATOM   248  C CA  . ARG A 1 150 ? 19.147  18.129  43.807  1 38.73 ? 399  ARG A CA  1 
ATOM   249  C C   . ARG A 1 150 ? 18.508  19.431  43.313  1 39.64 ? 399  ARG A C   1 
ATOM   250  O O   . ARG A 1 150 ? 17.531  19.385  42.568  1 40.02 ? 399  ARG A O   1 
ATOM   251  C CB  . ARG A 1 150 ? 18.504  17.819  45.156  1 40.39 ? 399  ARG A CB  1 
ATOM   252  C CG  . ARG A 1 150 ? 19.073  16.631  45.855  1 42.44 ? 399  ARG A CG  1 
ATOM   253  C CD  . ARG A 1 150 ? 18.198  16.308  47.04   1 43.57 ? 399  ARG A CD  1 
ATOM   254  N NE  . ARG A 1 150 ? 18.467  14.943  47.466  1 44.2  ? 399  ARG A NE  1 
ATOM   255  C CZ  . ARG A 1 150 ? 17.722  13.895  47.145  1 44.46 ? 399  ARG A CZ  1 
ATOM   256  N NH1 . ARG A 1 150 ? 16.605  14.055  46.442  1 43.53 ? 399  ARG A NH1 1 
ATOM   257  N NH2 . ARG A 1 150 ? 18.07   12.678  47.549  1 42.66 ? 399  ARG A NH2 1 
ATOM   258  N N   . GLU A 1 151 ? 19.027  20.581  43.778  1 39.86 ? 400  GLU A N   1 
ATOM   259  C CA  . GLU A 1 151 ? 18.522  21.906  43.427  1 41.03 ? 400  GLU A CA  1 
ATOM   260  C C   . GLU A 1 151 ? 18.773  22.296  41.944  1 40.33 ? 400  GLU A C   1 
ATOM   261  O O   . GLU A 1 151 ? 17.967  23.026  41.364  1 41.5  ? 400  GLU A O   1 
ATOM   262  C CB  . GLU A 1 151 ? 19.071  22.972  44.399  1 44.91 ? 400  GLU A CB  1 
ATOM   263  C CG  . GLU A 1 151 ? 18.312  23.035  45.72   1 53.32 ? 400  GLU A CG  1 
ATOM   264  C CD  . GLU A 1 151 ? 18.413  21.81   46.622  1 64.22 ? 400  GLU A CD  1 
ATOM   265  O OE1 . GLU A 1 151 ? 17.384  21.117  46.803  1 65.74 ? 400  GLU A OE1 1 
ATOM   266  O OE2 . GLU A 1 151 ? 19.519  21.545  47.149  1 67.93 ? 400  GLU A OE2 1 
ATOM   267  N N   . GLU A 1 152 ? 19.854  21.799  41.334  1 37.97 ? 401  GLU A N   1 
ATOM   268  C CA  . GLU A 1 152 ? 20.167  22.071  39.931  1 36.63 ? 401  GLU A CA  1 
ATOM   269  C C   . GLU A 1 152 ? 20.185  20.741  39.144  1 34.09 ? 401  GLU A C   1 
ATOM   270  O O   . GLU A 1 152 ? 21.002  20.578  38.242  1 33.22 ? 401  GLU A O   1 
ATOM   271  C CB  . GLU A 1 152 ? 21.534  22.77   39.79   1 40.16 ? 401  GLU A CB  1 
ATOM   272  C CG  . GLU A 1 152 ? 21.641  24.129  40.453  1 49.15 ? 401  GLU A CG  1 
ATOM   273  C CD  . GLU A 1 152 ? 21.127  25.301  39.637  1 59.97 ? 401  GLU A CD  1 
ATOM   274  O OE1 . GLU A 1 152 ? 21.134  26.436  40.169  1 62.16 ? 401  GLU A OE1 1 
ATOM   275  O OE2 . GLU A 1 152 ? 20.714  25.091  38.472  1 63.26 ? 401  GLU A OE2 1 
ATOM   276  N N   . ILE A 1 153 ? 19.266  19.811  39.458  1 32.98 ? 402  ILE A N   1 
ATOM   277  C CA  . ILE A 1 153 ? 19.263  18.488  38.831  1 32.72 ? 402  ILE A CA  1 
ATOM   278  C C   . ILE A 1 153 ? 19.228  18.562  37.297  1 32.23 ? 402  ILE A C   1 
ATOM   279  O O   . ILE A 1 153 ? 20.038  17.904  36.646  1 32.52 ? 402  ILE A O   1 
ATOM   280  C CB  . ILE A 1 153 ? 18.185  17.507  39.391  1 33    ? 402  ILE A CB  1 
ATOM   281  C CG1 . ILE A 1 153 ? 18.512  16.035  38.985  1 33.63 ? 402  ILE A CG1 1 
ATOM   282  C CG2 . ILE A 1 153 ? 16.757  17.884  38.959  1 33.53 ? 402  ILE A CG2 1 
ATOM   283  C CD1 . ILE A 1 153 ? 17.531  14.93   39.562  1 33.91 ? 402  ILE A CD1 1 
ATOM   284  N N   . PHE A 1 154 ? 18.359  19.414  36.734  1 30.65 ? 403  PHE A N   1 
ATOM   285  C CA  . PHE A 1 154 ? 18.209  19.542  35.3    1 29.42 ? 403  PHE A CA  1 
ATOM   286  C C   . PHE A 1 154 ? 19.483  19.993  34.623  1 27.95 ? 403  PHE A C   1 
ATOM   287  O O   . PHE A 1 154 ? 20.021  19.279  33.771  1 27.86 ? 403  PHE A O   1 
ATOM   288  C CB  . PHE A 1 154 ? 16.999  20.445  34.95   1 29.38 ? 403  PHE A CB  1 
ATOM   289  C CG  . PHE A 1 154 ? 16.766  20.627  33.471  1 30.03 ? 403  PHE A CG  1 
ATOM   290  C CD1 . PHE A 1 154 ? 16.115  19.657  32.733  1 30.98 ? 403  PHE A CD1 1 
ATOM   291  C CD2 . PHE A 1 154 ? 17.274  21.729  32.803  1 30.72 ? 403  PHE A CD2 1 
ATOM   292  C CE1 . PHE A 1 154 ? 15.929  19.812  31.359  1 31.52 ? 403  PHE A CE1 1 
ATOM   293  C CE2 . PHE A 1 154 ? 17.06   21.896  31.446  1 31.21 ? 403  PHE A CE2 1 
ATOM   294  C CZ  . PHE A 1 154 ? 16.405  20.926  30.726  1 30.98 ? 403  PHE A CZ  1 
ATOM   295  N N   . GLU A 1 155 ? 19.972  21.163  34.99   1 27.11 ? 404  GLU A N   1 
ATOM   296  C CA  . GLU A 1 155 ? 21.123  21.756  34.351  1 27.42 ? 404  GLU A CA  1 
ATOM   297  C C   . GLU A 1 155 ? 22.388  20.969  34.55   1 27.55 ? 404  GLU A C   1 
ATOM   298  O O   . GLU A 1 155 ? 23.178  20.831  33.608  1 27.58 ? 404  GLU A O   1 
ATOM   299  C CB  . GLU A 1 155 ? 21.288  23.217  34.817  1 30.27 ? 404  GLU A CB  1 
ATOM   300  C CG  . GLU A 1 155 ? 22.463  23.933  34.181  1 34.55 ? 404  GLU A CG  1 
ATOM   301  C CD  . GLU A 1 155 ? 22.419  24.072  32.668  1 38.88 ? 404  GLU A CD  1 
ATOM   302  O OE1 . GLU A 1 155 ? 21.31   24.065  32.08   1 38.72 ? 404  GLU A OE1 1 
ATOM   303  O OE2 . GLU A 1 155 ? 23.51   24.2    32.072  1 37.47 ? 404  GLU A OE2 1 
ATOM   304  N N   . GLU A 1 156 ? 22.606  20.47   35.773  1 27.35 ? 405  GLU A N   1 
ATOM   305  C CA  . GLU A 1 156 ? 23.822  19.716  36.045  1 27.1  ? 405  GLU A CA  1 
ATOM   306  C C   . GLU A 1 156 ? 23.786  18.369  35.351  1 25.67 ? 405  GLU A C   1 
ATOM   307  O O   . GLU A 1 156 ? 24.801  17.971  34.798  1 24.89 ? 405  GLU A O   1 
ATOM   308  C CB  . GLU A 1 156 ? 24.101  19.611  37.55   1 29.33 ? 405  GLU A CB  1 
ATOM   309  C CG  . GLU A 1 156 ? 24.45   20.953  38.169  1 33.76 ? 405  GLU A CG  1 
ATOM   310  C CD  . GLU A 1 156 ? 25.049  20.892  39.565  1 37.83 ? 405  GLU A CD  1 
ATOM   311  O OE1 . GLU A 1 156 ? 25.183  19.773  40.104  1 34.93 ? 405  GLU A OE1 1 
ATOM   312  O OE2 . GLU A 1 156 ? 25.38   21.965  40.12   1 41.71 ? 405  GLU A OE2 1 
ATOM   313  N N   . SER A 1 157 ? 22.607  17.7    35.293  1 25.22 ? 406  SER A N   1 
ATOM   314  C CA  . SER A 1 157 ? 22.523  16.436  34.536  1 24.68 ? 406  SER A CA  1 
ATOM   315  C C   . SER A 1 157 ? 22.735  16.683  33.074  1 25.45 ? 406  SER A C   1 
ATOM   316  O O   . SER A 1 157 ? 23.409  15.901  32.423  1 26    ? 406  SER A O   1 
ATOM   317  C CB  . SER A 1 157 ? 21.212  15.716  34.76   1 24.31 ? 406  SER A CB  1 
ATOM   318  O OG  . SER A 1 157 ? 21.073  15.409  36.133  1 27.71 ? 406  SER A OG  1 
ATOM   319  N N   . TYR A 1 158 ? 22.233  17.815  32.55   1 25.27 ? 407  TYR A N   1 
ATOM   320  C CA  . TYR A 1 158 ? 22.415  18.203  31.161  1 24.58 ? 407  TYR A CA  1 
ATOM   321  C C   . TYR A 1 158 ? 23.9    18.292  30.826  1 25.07 ? 407  TYR A C   1 
ATOM   322  O O   . TYR A 1 158 ? 24.354  17.638  29.875  1 24.82 ? 407  TYR A O   1 
ATOM   323  C CB  . TYR A 1 158 ? 21.678  19.535  30.865  1 24.31 ? 407  TYR A CB  1 
ATOM   324  C CG  . TYR A 1 158 ? 22.095  20.167  29.555  1 25.9  ? 407  TYR A CG  1 
ATOM   325  C CD1 . TYR A 1 158 ? 21.649  19.657  28.339  1 26.43 ? 407  TYR A CD1 1 
ATOM   326  C CD2 . TYR A 1 158 ? 22.929  21.278  29.531  1 27.53 ? 407  TYR A CD2 1 
ATOM   327  C CE1 . TYR A 1 158 ? 22.017  20.243  27.131  1 27.39 ? 407  TYR A CE1 1 
ATOM   328  C CE2 . TYR A 1 158 ? 23.333  21.849  28.328  1 28.99 ? 407  TYR A CE2 1 
ATOM   329  C CZ  . TYR A 1 158 ? 22.86   21.339  27.129  1 29.28 ? 407  TYR A CZ  1 
ATOM   330  O OH  . TYR A 1 158 ? 23.247  21.93   25.948  1 31.01 ? 407  TYR A OH  1 
ATOM   331  N N   . ARG A 1 159 ? 24.668  19.047  31.636  1 25.1  ? 408  ARG A N   1 
ATOM   332  C CA  . ARG A 1 159 ? 26.093  19.182  31.382  1 26.77 ? 408  ARG A CA  1 
ATOM   333  C C   . ARG A 1 159 ? 26.84   17.858  31.369  1 27.85 ? 408  ARG A C   1 
ATOM   334  O O   . ARG A 1 159 ? 27.669  17.639  30.48   1 29.57 ? 408  ARG A O   1 
ATOM   335  C CB  . ARG A 1 159 ? 26.738  20.152  32.378  1 28.99 ? 408  ARG A CB  1 
ATOM   336  C CG  . ARG A 1 159 ? 26.215  21.579  32.242  1 34.95 ? 408  ARG A CG  1 
ATOM   337  C CD  . ARG A 1 159 ? 26.524  22.203  30.883  1 40.98 ? 408  ARG A CD  1 
ATOM   338  N NE  . ARG A 1 159 ? 25.504  23.189  30.522  1 46.14 ? 408  ARG A NE  1 
ATOM   339  C CZ  . ARG A 1 159 ? 25.727  24.288  29.807  1 48.6  ? 408  ARG A CZ  1 
ATOM   340  N NH1 . ARG A 1 159 ? 26.943  24.551  29.345  1 50.14 ? 408  ARG A NH1 1 
ATOM   341  N NH2 . ARG A 1 159 ? 24.735  25.132  29.551  1 46.3  ? 408  ARG A NH2 1 
ATOM   342  N N   . GLN A 1 160 ? 26.56   16.981  32.339  1 26.82 ? 409  GLN A N   1 
ATOM   343  C CA  . GLN A 1 160 ? 27.268  15.724  32.432  1 27.3  ? 409  GLN A CA  1 
ATOM   344  C C   . GLN A 1 160 ? 26.842  14.683  31.383  1 27.44 ? 409  GLN A C   1 
ATOM   345  O O   . GLN A 1 160 ? 27.698  14.048  30.769  1 28.13 ? 409  GLN A O   1 
ATOM   346  C CB  . GLN A 1 160 ? 27.168  15.193  33.848  1 29.13 ? 409  GLN A CB  1 
ATOM   347  C CG  . GLN A 1 160 ? 28.154  15.933  34.75   1 31.79 ? 409  GLN A CG  1 
ATOM   348  C CD  . GLN A 1 160 ? 27.896  15.623  36.179  1 35.04 ? 409  GLN A CD  1 
ATOM   349  O OE1 . GLN A 1 160 ? 27.9    14.47   36.59   1 34.89 ? 409  GLN A OE1 1 
ATOM   350  N NE2 . GLN A 1 160 ? 27.664  16.654  36.975  1 38.22 ? 409  GLN A NE2 1 
ATOM   351  N N   . VAL A 1 161 ? 25.549  14.534  31.15   1 27.03 ? 410  VAL A N   1 
ATOM   352  C CA  . VAL A 1 161 ? 25.041  13.568  30.164  1 26.91 ? 410  VAL A CA  1 
ATOM   353  C C   . VAL A 1 161 ? 25.445  13.952  28.731  1 27.91 ? 410  VAL A C   1 
ATOM   354  O O   . VAL A 1 161 ? 25.787  13.068  27.944  1 28.84 ? 410  VAL A O   1 
ATOM   355  C CB  . VAL A 1 161 ? 23.513  13.383  30.322  1 26.37 ? 410  VAL A CB  1 
ATOM   356  C CG1 . VAL A 1 161 ? 22.891  12.693  29.097  1 26.29 ? 410  VAL A CG1 1 
ATOM   357  C CG2 . VAL A 1 161 ? 23.188  12.628  31.612  1 26.73 ? 410  VAL A CG2 1 
ATOM   358  N N   . MET A 1 162 ? 25.458  15.259  28.404  1 27.51 ? 411  MET A N   1 
ATOM   359  C CA  . MET A 1 162 ? 25.8    15.682  27.053  1 28.4  ? 411  MET A CA  1 
ATOM   360  C C   . MET A 1 162 ? 27.299  15.614  26.741  1 30.59 ? 411  MET A C   1 
ATOM   361  O O   . MET A 1 162 ? 27.663  15.688  25.574  1 31.26 ? 411  MET A O   1 
ATOM   362  C CB  . MET A 1 162 ? 25.192  17.054  26.7    1 27.71 ? 411  MET A CB  1 
ATOM   363  C CG  . MET A 1 162 ? 23.657  17.029  26.728  1 28.17 ? 411  MET A CG  1 
ATOM   364  S SD  . MET A 1 162 ? 22.948  15.687  25.745  1 29.29 ? 411  MET A SD  1 
ATOM   365  C CE  . MET A 1 162 ? 23.336  16.269  24.13   1 25.98 ? 411  MET A CE  1 
ATOM   366  N N   . LYS A 1 163 ? 28.15   15.405  27.749  1 31.39 ? 412  LYS A N   1 
ATOM   367  C CA  . LYS A 1 163 ? 29.569  15.141  27.504  1 32.58 ? 412  LYS A CA  1 
ATOM   368  C C   . LYS A 1 163 ? 29.795  13.636  27.209  1 32.96 ? 412  LYS A C   1 
ATOM   369  O O   . LYS A 1 163 ? 30.854  13.273  26.733  1 33.97 ? 412  LYS A O   1 
ATOM   370  C CB  . LYS A 1 163 ? 30.433  15.592  28.694  1 35.27 ? 412  LYS A CB  1 
ATOM   371  C CG  . LYS A 1 163 ? 30.579  17.102  28.752  1 41.13 ? 412  LYS A CG  1 
ATOM   372  C CD  . LYS A 1 163 ? 31.2    17.559  30.049  1 48.11 ? 412  LYS A CD  1 
ATOM   373  C CE  . LYS A 1 163 ? 31.57   19.023  29.966  1 53.73 ? 412  LYS A CE  1 
ATOM   374  N NZ  . LYS A 1 163 ? 32.383  19.318  28.746  1 56.64 ? 412  LYS A NZ  1 
ATOM   375  N N   . MET A 1 164 ? 28.818  12.767  27.487  1 32.56 ? 413  MET A N   1 
ATOM   376  C CA  . MET A 1 164 ? 28.957  11.343  27.268  1 32.56 ? 413  MET A CA  1 
ATOM   377  C C   . MET A 1 164 ? 28.586  10.921  25.866  1 32.01 ? 413  MET A C   1 
ATOM   378  O O   . MET A 1 164 ? 27.788  11.571  25.187  1 31.96 ? 413  MET A O   1 
ATOM   379  C CB  . MET A 1 164 ? 28.107  10.572  28.279  1 33.48 ? 413  MET A CB  1 
ATOM   380  C CG  . MET A 1 164 ? 28.642  10.648  29.65   1 36.23 ? 413  MET A CG  1 
ATOM   381  S SD  . MET A 1 164 ? 27.467  9.922   30.773  1 40.47 ? 413  MET A SD  1 
ATOM   382  C CE  . MET A 1 164 ? 28.019  10.656  32.291  1 37.92 ? 413  MET A CE  1 
ATOM   383  N N   . ARG A 1 165 ? 29.149  9.793   25.447  1 31.21 ? 414  ARG A N   1 
ATOM   384  C CA  . ARG A 1 165 ? 28.844  9.2     24.16   1 31.22 ? 414  ARG A CA  1 
ATOM   385  C C   . ARG A 1 165 ? 27.647  8.291   24.361  1 30.46 ? 414  ARG A C   1 
ATOM   386  O O   . ARG A 1 165 ? 27.401  7.824   25.482  1 30.2  ? 414  ARG A O   1 
ATOM   387  C CB  . ARG A 1 165 ? 30.057  8.365   23.687  1 33.33 ? 414  ARG A CB  1 
ATOM   388  C CG  . ARG A 1 165 ? 31.339  9.184   23.58   1 37.69 ? 414  ARG A CG  1 
ATOM   389  C CD  . ARG A 1 165 ? 32.589  8.319   23.65   1 42.12 ? 414  ARG A CD  1 
ATOM   390  N NE  . ARG A 1 165 ? 32.591  7.455   24.829  1 46.95 ? 414  ARG A NE  1 
ATOM   391  C CZ  . ARG A 1 165 ? 33.517  6.536   25.086  1 50.09 ? 414  ARG A CZ  1 
ATOM   392  N NH1 . ARG A 1 165 ? 34.535  6.355   24.248  1 50.97 ? 414  ARG A NH1 1 
ATOM   393  N NH2 . ARG A 1 165 ? 33.427  5.781   26.172  1 48.7  ? 414  ARG A NH2 1 
ATOM   394  N N   . PRO A 1 166 ? 26.93   7.931   23.275  1 30.32 ? 415  PRO A N   1 
ATOM   395  C CA  . PRO A 1 166 ? 25.817  6.986   23.417  1 30.2  ? 415  PRO A CA  1 
ATOM   396  C C   . PRO A 1 166 ? 26.181  5.696   24.154  1 29.68 ? 415  PRO A C   1 
ATOM   397  O O   . PRO A 1 166 ? 25.405  5.258   24.986  1 29.22 ? 415  PRO A O   1 
ATOM   398  C CB  . PRO A 1 166 ? 25.422  6.703   21.964  1 31.01 ? 415  PRO A CB  1 
ATOM   399  C CG  . PRO A 1 166 ? 25.821  7.91    21.235  1 31.47 ? 415  PRO A CG  1 
ATOM   400  C CD  . PRO A 1 166 ? 27.08   8.379   21.876  1 29.83 ? 415  PRO A CD  1 
ATOM   401  N N   . LYS A 1 167 ? 27.374  5.114   23.904  1 30.08 ? 416  LYS A N   1 
ATOM   402  C CA  . LYS A 1 167 ? 27.76   3.867   24.595  1 30.99 ? 416  LYS A CA  1 
ATOM   403  C C   . LYS A 1 167 ? 27.908  4.033   26.108  1 30.28 ? 416  LYS A C   1 
ATOM   404  O O   . LYS A 1 167 ? 27.583  3.105   26.856  1 30.16 ? 416  LYS A O   1 
ATOM   405  C CB  . LYS A 1 167 ? 29.001  3.187   23.977  1 34.12 ? 416  LYS A CB  1 
ATOM   406  C CG  . LYS A 1 167 ? 30.294  4.005   23.98   1 39.71 ? 416  LYS A CG  1 
ATOM   407  C CD  . LYS A 1 167 ? 31.458  3.05    23.71   1 45.56 ? 416  LYS A CD  1 
ATOM   408  C CE  . LYS A 1 167 ? 32.561  3.668   22.9    1 50.98 ? 416  LYS A CE  1 
ATOM   409  N NZ  . LYS A 1 167 ? 33.699  4.091   23.766  1 55.03 ? 416  LYS A NZ  1 
ATOM   410  N N   . ASP A 1 168 ? 28.272  5.238   26.569  1 29.86 ? 417  ASP A N   1 
ATOM   411  C CA  . ASP A 1 168 ? 28.389  5.498   28.005  1 30.07 ? 417  ASP A CA  1 
ATOM   412  C C   . ASP A 1 168 ? 27.049  5.389   28.745  1 29.9  ? 417  ASP A C   1 
ATOM   413  O O   . ASP A 1 168 ? 27.01   4.982   29.904  1 29.69 ? 417  ASP A O   1 
ATOM   414  C CB  . ASP A 1 168 ? 28.984  6.891   28.236  1 31.53 ? 417  ASP A CB  1 
ATOM   415  C CG  . ASP A 1 168 ? 30.382  7.001   27.688  1 35.72 ? 417  ASP A CG  1 
ATOM   416  O OD1 . ASP A 1 168 ? 31.149  6.027   27.841  1 36.56 ? 417  ASP A OD1 1 
ATOM   417  O OD2 . ASP A 1 168 ? 30.714  8.071   27.103  1 36.97 ? 417  ASP A OD2 1 
ATOM   418  N N   . LEU A 1 169 ? 25.952  5.754   28.068  1 29.71 ? 418  LEU A N   1 
ATOM   419  C CA  . LEU A 1 169 ? 24.609  5.752   28.65   1 29.68 ? 418  LEU A CA  1 
ATOM   420  C C   . LEU A 1 169 ? 24.049  4.368   28.913  1 29.45 ? 418  LEU A C   1 
ATOM   421  O O   . LEU A 1 169 ? 23.077  4.229   29.665  1 28.89 ? 418  LEU A O   1 
ATOM   422  C CB  . LEU A 1 169 ? 23.644  6.577   27.772  1 29.98 ? 418  LEU A CB  1 
ATOM   423  C CG  . LEU A 1 169 ? 24.166  7.966   27.33   1 32.14 ? 418  LEU A CG  1 
ATOM   424  C CD1 . LEU A 1 169 ? 23.342  8.533   26.181  1 32.81 ? 418  LEU A CD1 1 
ATOM   425  C CD2 . LEU A 1 169 ? 24.311  8.929   28.525  1 32.72 ? 418  LEU A CD2 1 
ATOM   426  N N   . TRP A 1 170 ? 24.643  3.331   28.306  1 30.11 ? 419  TRP A N   1 
ATOM   427  C CA  . TRP A 1 170 ? 24.207  1.943   28.525  1 31.28 ? 419  TRP A CA  1 
ATOM   428  C C   . TRP A 1 170 ? 24.87   1.296   29.747  1 30.5  ? 419  TRP A C   1 
ATOM   429  O O   . TRP A 1 170 ? 24.467  0.209   30.139  1 30.71 ? 419  TRP A O   1 
ATOM   430  C CB  . TRP A 1 170 ? 24.486  1.081   27.276  1 33.07 ? 419  TRP A CB  1 
ATOM   431  C CG  . TRP A 1 170 ? 24.082  1.746   25.985  1 36.45 ? 419  TRP A CG  1 
ATOM   432  C CD1 . TRP A 1 170 ? 23.027  2.596   25.789  1 38.13 ? 419  TRP A CD1 1 
ATOM   433  C CD2 . TRP A 1 170 ? 24.745  1.629   24.718  1 37.77 ? 419  TRP A CD2 1 
ATOM   434  N NE1 . TRP A 1 170 ? 23.047  3.081   24.503  1 39.24 ? 419  TRP A NE1 1 
ATOM   435  C CE2 . TRP A 1 170 ? 24.071  2.476   23.813  1 39.2  ? 419  TRP A CE2 1 
ATOM   436  C CE3 . TRP A 1 170 ? 25.842  0.888   24.262  1 39.04 ? 419  TRP A CE3 1 
ATOM   437  C CZ2 . TRP A 1 170 ? 24.441  2.579   22.475  1 40.34 ? 419  TRP A CZ2 1 
ATOM   438  C CZ3 . TRP A 1 170 ? 26.226  1.018   22.946  1 40.37 ? 419  TRP A CZ3 1 
ATOM   439  C CH2 . TRP A 1 170 ? 25.527  1.851   22.067  1 40.84 ? 419  TRP A CH2 1 
ATOM   440  N N   . LYS A 1 171 ? 25.882  1.942   30.344  1 29.53 ? 420  LYS A N   1 
ATOM   441  C CA  . LYS A 1 171 ? 26.616  1.389   31.476  1 29.42 ? 420  LYS A CA  1 
ATOM   442  C C   . LYS A 1 171 ? 25.866  1.473   32.792  1 30.04 ? 420  LYS A C   1 
ATOM   443  O O   . LYS A 1 171 ? 24.994  2.342   32.966  1 29.86 ? 420  LYS A O   1 
ATOM   444  C CB  . LYS A 1 171 ? 27.986  2.082   31.585  1 29.61 ? 420  LYS A CB  1 
ATOM   445  C CG  . LYS A 1 171 ? 28.827  1.908   30.338  1 29.98 ? 420  LYS A CG  1 
ATOM   446  C CD  . LYS A 1 171 ? 30.062  2.789   30.353  1 33.1  ? 420  LYS A CD  1 
ATOM   447  C CE  . LYS A 1 171 ? 30.988  2.399   29.228  1 36    ? 420  LYS A CE  1 
ATOM   448  N NZ  . LYS A 1 171 ? 31.878  3.51    28.813  1 36.63 ? 420  LYS A NZ  1 
ATOM   449  N N   . ARG A 1 172 ? 26.226  0.593   33.776  1 29.18 ? 421  ARG A N   1 
ATOM   450  C CA  . ARG A 1 172 ? 25.567  0.607   35.082  1 29.27 ? 421  ARG A CA  1 
ATOM   451  C C   . ARG A 1 172 ? 25.694  1.978   35.723  1 28.53 ? 421  ARG A C   1 
ATOM   452  O O   . ARG A 1 172 ? 26.748  2.587   35.641  1 28.1  ? 421  ARG A O   1 
ATOM   453  C CB  . ARG A 1 172 ? 26.115  -0.48   36.039  1 31.39 ? 421  ARG A CB  1 
ATOM   454  C CG  . ARG A 1 172 ? 25.898  -1.899  35.526  1 34.82 ? 421  ARG A CG  1 
ATOM   455  C CD  . ARG A 1 172 ? 26.974  -2.849  36.029  1 38.35 ? 421  ARG A CD  1 
ATOM   456  N NE  . ARG A 1 172 ? 28.303  -2.507  35.502  1 40.17 ? 421  ARG A NE  1 
ATOM   457  C CZ  . ARG A 1 172 ? 29.447  -2.838  36.091  1 41.89 ? 421  ARG A CZ  1 
ATOM   458  N NH1 . ARG A 1 172 ? 29.442  -3.509  37.241  1 42.57 ? 421  ARG A NH1 1 
ATOM   459  N NH2 . ARG A 1 172 ? 30.604  -2.494  35.544  1 40.1  ? 421  ARG A NH2 1 
ATOM   460  N N   . LEU A 1 173 ? 24.594  2.488   36.253  1 27.72 ? 422  LEU A N   1 
ATOM   461  C CA  . LEU A 1 173 ? 24.557  3.81    36.819  1 28.02 ? 422  LEU A CA  1 
ATOM   462  C C   . LEU A 1 173 ? 25.232  3.905   38.173  1 28.12 ? 422  LEU A C   1 
ATOM   463  O O   . LEU A 1 173 ? 24.939  3.132   39.08   1 28.11 ? 422  LEU A O   1 
ATOM   464  C CB  . LEU A 1 173 ? 23.111  4.278   36.941  1 28.33 ? 422  LEU A CB  1 
ATOM   465  C CG  . LEU A 1 173 ? 22.312  4.379   35.644  1 30.55 ? 422  LEU A CG  1 
ATOM   466  C CD1 . LEU A 1 173 ? 20.871  4.806   35.942  1 31.9  ? 422  LEU A CD1 1 
ATOM   467  C CD2 . LEU A 1 173 ? 22.952  5.348   34.691  1 30.45 ? 422  LEU A CD2 1 
ATOM   468  N N   . MET A 1 174 ? 26.096  4.901   38.317  1 27.66 ? 423  MET A N   1 
ATOM   469  C CA  . MET A 1 174 ? 26.738  5.187   39.579  1 27.52 ? 423  MET A CA  1 
ATOM   470  C C   . MET A 1 174 ? 26.45   6.666   39.818  1 26.52 ? 423  MET A C   1 
ATOM   471  O O   . MET A 1 174 ? 27.126  7.54    39.275  1 25.74 ? 423  MET A O   1 
ATOM   472  C CB  . MET A 1 174 ? 28.242  4.874   39.51   1 28.42 ? 423  MET A CB  1 
ATOM   473  C CG  . MET A 1 174 ? 28.91   4.935   40.863  1 32.46 ? 423  MET A CG  1 
ATOM   474  S SD  . MET A 1 174 ? 30.639  4.404   40.82   1 37.91 ? 423  MET A SD  1 
ATOM   475  C CE  . MET A 1 174 ? 30.477  2.664   41.141  1 30.38 ? 423  MET A CE  1 
ATOM   476  N N   . ILE A 1 175 ? 25.381  6.938   40.565  1 26.88 ? 424  ILE A N   1 
ATOM   477  C CA  . ILE A 1 175 ? 24.897  8.297   40.796  1 27.44 ? 424  ILE A CA  1 
ATOM   478  C C   . ILE A 1 175 ? 25.145  8.757   42.211  1 27.73 ? 424  ILE A C   1 
ATOM   479  O O   . ILE A 1 175 ? 24.944  7.999   43.16   1 28.33 ? 424  ILE A O   1 
ATOM   480  C CB  . ILE A 1 175 ? 23.363  8.407   40.509  1 28.38 ? 424  ILE A CB  1 
ATOM   481  C CG1 . ILE A 1 175 ? 22.926  7.649   39.222  1 29.73 ? 424  ILE A CG1 1 
ATOM   482  C CG2 . ILE A 1 175 ? 22.878  9.866   40.501  1 28.6  ? 424  ILE A CG2 1 
ATOM   483  C CD1 . ILE A 1 175 ? 23.431  8.155   37.961  1 31.66 ? 424  ILE A CD1 1 
ATOM   484  N N   . LYS A 1 176 ? 25.449  10.04   42.359  1 26.99 ? 425  LYS A N   1 
ATOM   485  C CA  . LYS A 1 176 ? 25.605  10.644  43.653  1 27.18 ? 425  LYS A CA  1 
ATOM   486  C C   . LYS A 1 176 ? 24.973  12.014  43.641  1 27.4  ? 425  LYS A C   1 
ATOM   487  O O   . LYS A 1 176 ? 25.228  12.792  42.721  1 27.36 ? 425  LYS A O   1 
ATOM   488  C CB  . LYS A 1 176 ? 27.098  10.805  43.977  1 28.18 ? 425  LYS A CB  1 
ATOM   489  C CG  . LYS A 1 176 ? 27.369  11.254  45.402  1 29.85 ? 425  LYS A CG  1 
ATOM   490  C CD  . LYS A 1 176 ? 28.863  11.337  45.674  1 32.62 ? 425  LYS A CD  1 
ATOM   491  C CE  . LYS A 1 176 ? 29.102  11.563  47.147  1 35.22 ? 425  LYS A CE  1 
ATOM   492  N NZ  . LYS A 1 176 ? 28.424  12.791  47.625  1 36.45 ? 425  LYS A NZ  1 
ATOM   493  N N   . PHE A 1 177 ? 24.203  12.342  44.681  1 27.84 ? 426  PHE A N   1 
ATOM   494  C CA  . PHE A 1 177 ? 23.676  13.691  44.834  1 29.09 ? 426  PHE A CA  1 
ATOM   495  C C   . PHE A 1 177 ? 24.724  14.492  45.609  1 30.42 ? 426  PHE A C   1 
ATOM   496  O O   . PHE A 1 177 ? 25.219  14.012  46.619  1 30.9  ? 426  PHE A O   1 
ATOM   497  C CB  . PHE A 1 177 ? 22.353  13.68   45.604  1 29.04 ? 426  PHE A CB  1 
ATOM   498  C CG  . PHE A 1 177 ? 21.197  13.311  44.715  1 29.87 ? 426  PHE A CG  1 
ATOM   499  C CD1 . PHE A 1 177 ? 20.824  14.13   43.663  1 30.77 ? 426  PHE A CD1 1 
ATOM   500  C CD2 . PHE A 1 177 ? 20.482  12.148  44.931  1 30.64 ? 426  PHE A CD2 1 
ATOM   501  C CE1 . PHE A 1 177 ? 19.744  13.792  42.854  1 31.5  ? 426  PHE A CE1 1 
ATOM   502  C CE2 . PHE A 1 177 ? 19.408  11.815  44.117  1 31.48 ? 426  PHE A CE2 1 
ATOM   503  C CZ  . PHE A 1 177 ? 19.028  12.654  43.108  1 31.2  ? 426  PHE A CZ  1 
ATOM   504  N N   . ARG A 1 178 ? 25.083  15.666  45.124  1 31.45 ? 427  ARG A N   1 
ATOM   505  C CA  . ARG A 1 178 ? 26.096  16.542  45.705  1 33.71 ? 427  ARG A CA  1 
ATOM   506  C C   . ARG A 1 178 ? 25.809  16.847  47.176  1 34.76 ? 427  ARG A C   1 
ATOM   507  O O   . ARG A 1 178 ? 24.648  17.054  47.556  1 34.82 ? 427  ARG A O   1 
ATOM   508  C CB  . ARG A 1 178 ? 26.186  17.834  44.89   1 36.92 ? 427  ARG A CB  1 
ATOM   509  C CG  . ARG A 1 178 ? 27.596  18.184  44.513  1 41.98 ? 427  ARG A CG  1 
ATOM   510  C CD  . ARG A 1 178 ? 27.674  19.468  43.727  1 46.48 ? 427  ARG A CD  1 
ATOM   511  N NE  . ARG A 1 178 ? 27.417  19.263  42.301  1 50.03 ? 427  ARG A NE  1 
ATOM   512  C CZ  . ARG A 1 178 ? 28.338  18.889  41.418  1 53.22 ? 427  ARG A CZ  1 
ATOM   513  N NH1 . ARG A 1 178 ? 29.583  18.632  41.812  1 53.19 ? 427  ARG A NH1 1 
ATOM   514  N NH2 . ARG A 1 178 ? 28.017  18.737  40.14   1 53.6  ? 427  ARG A NH2 1 
ATOM   515  N N   . GLY A 1 179 ? 26.853  16.752  48.007  1 34.73 ? 428  GLY A N   1 
ATOM   516  C CA  . GLY A 1 179 ? 26.742  16.942  49.446  1 34.67 ? 428  GLY A CA  1 
ATOM   517  C C   . GLY A 1 179 ? 26.052  15.808  50.179  1 35.14 ? 428  GLY A C   1 
ATOM   518  O O   . GLY A 1 179 ? 25.883  15.886  51.398  1 35.14 ? 428  GLY A O   1 
ATOM   519  N N   . GLU A 1 180 ? 25.652  14.726  49.466  1 35.36 ? 429  GLU A N   1 
ATOM   520  C CA  . GLU A 1 180 ? 24.918  13.634  50.11   1 36.69 ? 429  GLU A CA  1 
ATOM   521  C C   . GLU A 1 180 ? 25.617  12.301  49.994  1 39.05 ? 429  GLU A C   1 
ATOM   522  O O   . GLU A 1 180 ? 26.111  11.933  48.912  1 38.91 ? 429  GLU A O   1 
ATOM   523  C CB  . GLU A 1 180 ? 23.488  13.484  49.553  1 38.44 ? 429  GLU A CB  1 
ATOM   524  C CG  . GLU A 1 180 ? 22.747  14.791  49.32   1 43.88 ? 429  GLU A CG  1 
ATOM   525  C CD  . GLU A 1 180 ? 21.252  14.643  49.105  1 49.92 ? 429  GLU A CD  1 
ATOM   526  O OE1 . GLU A 1 180 ? 20.798  13.518  48.794  1 49.02 ? 429  GLU A OE1 1 
ATOM   527  O OE2 . GLU A 1 180 ? 20.534  15.658  49.255  1 54.29 ? 429  GLU A OE2 1 
ATOM   528  N N   . GLU A 1 181 ? 25.576  11.534  51.089  1 40.36 ? 430  GLU A N   1 
ATOM   529  C CA  . GLU A 1 181 ? 26.189  10.216  51.14   1 42.36 ? 430  GLU A CA  1 
ATOM   530  C C   . GLU A 1 181 ? 25.395  9.172   50.354  1 44.39 ? 430  GLU A C   1 
ATOM   531  O O   . GLU A 1 181 ? 25.977  8.447   49.55   1 45.08 ? 430  GLU A O   1 
ATOM   532  C CB  . GLU A 1 181 ? 26.435  9.788   52.601  1 44.37 ? 430  GLU A CB  1 
ATOM   533  C CG  . GLU A 1 181 ? 26.918  8.357   52.737  1 49.3  ? 430  GLU A CG  1 
ATOM   534  C CD  . GLU A 1 181 ? 27.563  8.009   54.064  1 53.72 ? 430  GLU A CD  1 
ATOM   535  O OE1 . GLU A 1 181 ? 27.737  8.918   54.911  1 52.62 ? 430  GLU A OE1 1 
ATOM   536  O OE2 . GLU A 1 181 ? 27.905  6.818   54.246  1 55.95 ? 430  GLU A OE2 1 
ATOM   537  N N   . GLY A 1 182 ? 24.09   9.083   50.593  1 45.54 ? 431  GLY A N   1 
ATOM   538  C CA  . GLY A 1 182 ? 23.257  8.099   49.901  1 47    ? 431  GLY A CA  1 
ATOM   539  C C   . GLY A 1 182 ? 23.303  6.717   50.532  1 48.24 ? 431  GLY A C   1 
ATOM   540  O O   . GLY A 1 182 ? 24.365  6.276   50.977  1 48.27 ? 431  GLY A O   1 
ATOM   541  N N   . LEU A 1 183 ? 22.148  6.011   50.57   1 48.77 ? 432  LEU A N   1 
ATOM   542  C CA  . LEU A 1 183 ? 22.041  4.674   51.174  1 49.5  ? 432  LEU A CA  1 
ATOM   543  C C   . LEU A 1 183 ? 22.675  3.564   50.323  1 48.94 ? 432  LEU A C   1 
ATOM   544  O O   . LEU A 1 183 ? 23.49   2.797   50.833  1 49.78 ? 432  LEU A O   1 
ATOM   545  C CB  . LEU A 1 183 ? 20.58   4.344   51.529  1 50.51 ? 432  LEU A CB  1 
ATOM   546  C CG  . LEU A 1 183 ? 20.025  5.113   52.724  1 53.28 ? 432  LEU A CG  1 
ATOM   547  C CD1 . LEU A 1 183 ? 18.529  4.93    52.848  1 54.22 ? 432  LEU A CD1 1 
ATOM   548  C CD2 . LEU A 1 183 ? 20.72   4.696   54.013  1 54.39 ? 432  LEU A CD2 1 
ATOM   549  N N   . ASP A 1 184 ? 22.301  3.47    49.044  1 47.27 ? 433  ASP A N   1 
ATOM   550  C CA  . ASP A 1 184 ? 22.866  2.502   48.097  1 46.29 ? 433  ASP A CA  1 
ATOM   551  C C   . ASP A 1 184 ? 22.748  3.05    46.682  1 43.68 ? 433  ASP A C   1 
ATOM   552  O O   . ASP A 1 184 ? 21.821  3.813   46.398  1 43.89 ? 433  ASP A O   1 
ATOM   553  C CB  . ASP A 1 184 ? 22.226  1.106   48.206  1 48.97 ? 433  ASP A CB  1 
ATOM   554  C CG  . ASP A 1 184 ? 20.787  1.054   47.773  1 56.35 ? 433  ASP A CG  1 
ATOM   555  O OD1 . ASP A 1 184 ? 19.958  1.742   48.398  1 58.73 ? 433  ASP A OD1 1 
ATOM   556  O OD2 . ASP A 1 184 ? 20.484  0.319   46.805  1 58.91 ? 433  ASP A OD2 1 
ATOM   557  N N   . TYR A 1 185 ? 23.682  2.671   45.8    1 40.79 ? 434  TYR A N   1 
ATOM   558  C CA  . TYR A 1 185 ? 23.714  3.181   44.437  1 38.78 ? 434  TYR A CA  1 
ATOM   559  C C   . TYR A 1 185 ? 22.455  2.894   43.616  1 37.66 ? 434  TYR A C   1 
ATOM   560  O O   . TYR A 1 185 ? 22.028  3.764   42.862  1 36.95 ? 434  TYR A O   1 
ATOM   561  C CB  . TYR A 1 185 ? 24.963  2.713   43.686  1 37.92 ? 434  TYR A CB  1 
ATOM   562  C CG  . TYR A 1 185 ? 26.205  3.477   44.092  1 37.53 ? 434  TYR A CG  1 
ATOM   563  C CD1 . TYR A 1 185 ? 26.267  4.859   43.972  1 37.29 ? 434  TYR A CD1 1 
ATOM   564  C CD2 . TYR A 1 185 ? 27.307  2.818   44.616  1 38.45 ? 434  TYR A CD2 1 
ATOM   565  C CE1 . TYR A 1 185 ? 27.407  5.565   44.342  1 38.16 ? 434  TYR A CE1 1 
ATOM   566  C CE2 . TYR A 1 185 ? 28.451  3.513   44.995  1 39.1  ? 434  TYR A CE2 1 
ATOM   567  C CZ  . TYR A 1 185 ? 28.492  4.887   44.868  1 39.4  ? 434  TYR A CZ  1 
ATOM   568  O OH  . TYR A 1 185 ? 29.615  5.557   45.272  1 40.38 ? 434  TYR A OH  1 
ATOM   569  N N   . GLY A 1 186 ? 21.87   1.71    43.786  1 36.79 ? 435  GLY A N   1 
ATOM   570  C CA  . GLY A 1 186 ? 20.672  1.332   43.047  1 36.86 ? 435  GLY A CA  1 
ATOM   571  C C   . GLY A 1 186 ? 19.5    2.251   43.323  1 36.44 ? 435  GLY A C   1 
ATOM   572  O O   . GLY A 1 186 ? 18.775  2.642   42.403  1 36.79 ? 435  GLY A O   1 
ATOM   573  N N   . GLY A 1 187 ? 19.352  2.613   44.584  1 35.43 ? 436  GLY A N   1 
ATOM   574  C CA  . GLY A 1 187 ? 18.291  3.487   45.054  1 35.49 ? 436  GLY A CA  1 
ATOM   575  C C   . GLY A 1 187 ? 18.51   4.906   44.6    1 35.34 ? 436  GLY A C   1 
ATOM   576  O O   . GLY A 1 187 ? 17.568  5.567   44.156  1 35.45 ? 436  GLY A O   1 
ATOM   577  N N   . VAL A 1 188 ? 19.765  5.378   44.667  1 34.61 ? 437  VAL A N   1 
ATOM   578  C CA  . VAL A 1 188 ? 20.074  6.733   44.217  1 34.09 ? 437  VAL A CA  1 
ATOM   579  C C   . VAL A 1 188 ? 19.888  6.864   42.701  1 33.97 ? 437  VAL A C   1 
ATOM   580  O O   . VAL A 1 188 ? 19.413  7.9     42.239  1 34.75 ? 437  VAL A O   1 
ATOM   581  C CB  . VAL A 1 188 ? 21.448  7.25    44.704  1 33.9  ? 437  VAL A CB  1 
ATOM   582  C CG1 . VAL A 1 188 ? 21.723  8.649   44.162  1 34.05 ? 437  VAL A CG1 1 
ATOM   583  C CG2 . VAL A 1 188 ? 21.515  7.247   46.226  1 34.33 ? 437  VAL A CG2 1 
ATOM   584  N N   . ALA A 1 189 ? 20.192  5.811   41.937  1 33.87 ? 438  ALA A N   1 
ATOM   585  C CA  . ALA A 1 189 ? 20.019  5.832   40.486  1 34.81 ? 438  ALA A CA  1 
ATOM   586  C C   . ALA A 1 189 ? 18.515  5.925   40.153  1 35.93 ? 438  ALA A C   1 
ATOM   587  O O   . ALA A 1 189 ? 18.118  6.717   39.296  1 35.67 ? 438  ALA A O   1 
ATOM   588  C CB  . ALA A 1 189 ? 20.634  4.585   39.857  1 34.71 ? 438  ALA A CB  1 
ATOM   589  N N   . ARG A 1 190 ? 17.691  5.149   40.873  1 36.57 ? 439  ARG A N   1 
ATOM   590  C CA  . ARG A 1 190 ? 16.23   5.143   40.734  1 37.94 ? 439  ARG A CA  1 
ATOM   591  C C   . ARG A 1 190 ? 15.658  6.52    41.063  1 37.12 ? 439  ARG A C   1 
ATOM   592  O O   . ARG A 1 190 ? 14.825  7.025   40.323  1 38.25 ? 439  ARG A O   1 
ATOM   593  C CB  . ARG A 1 190 ? 15.596  4.07    41.642  1 40.8  ? 439  ARG A CB  1 
ATOM   594  C CG  . ARG A 1 190 ? 14.076  4.055   41.597  1 47.7  ? 439  ARG A CG  1 
ATOM   595  C CD  . ARG A 1 190 ? 13.471  3.117   42.623  1 54.57 ? 439  ARG A CD  1 
ATOM   596  N NE  . ARG A 1 190 ? 12.134  3.554   43.031  1 60.55 ? 439  ARG A NE  1 
ATOM   597  C CZ  . ARG A 1 190 ? 11.005  3.178   42.437  1 65.43 ? 439  ARG A CZ  1 
ATOM   598  N NH1 . ARG A 1 190 ? 11.034  2.326   41.418  1 66.12 ? 439  ARG A NH1 1 
ATOM   599  N NH2 . ARG A 1 190 ? 9.835   3.631   42.872  1 66.4  ? 439  ARG A NH2 1 
ATOM   600  N N   . GLU A 1 191 ? 16.137  7.145   42.132  1 35.49 ? 440  GLU A N   1 
ATOM   601  C CA  . GLU A 1 191 ? 15.687  8.464   42.531  1 34.88 ? 440  GLU A CA  1 
ATOM   602  C C   . GLU A 1 191 ? 16.104  9.569   41.557  1 34.26 ? 440  GLU A C   1 
ATOM   603  O O   . GLU A 1 191 ? 15.304  10.463  41.274  1 34.87 ? 440  GLU A O   1 
ATOM   604  C CB  . GLU A 1 191 ? 16.184  8.788   43.939  1 37.47 ? 440  GLU A CB  1 
ATOM   605  C CG  . GLU A 1 191 ? 15.644  10.091  44.487  1 42.65 ? 440  GLU A CG  1 
ATOM   606  C CD  . GLU A 1 191 ? 16.209  10.504  45.83   1 52.12 ? 440  GLU A CD  1 
ATOM   607  O OE1 . GLU A 1 191 ? 17.242  9.932   46.247  1 53.94 ? 440  GLU A OE1 1 
ATOM   608  O OE2 . GLU A 1 191 ? 15.63   11.419  46.458  1 55.4  ? 440  GLU A OE2 1 
ATOM   609  N N   . TRP A 1 192 ? 17.345  9.526   41.041  1 32.36 ? 441  TRP A N   1 
ATOM   610  C CA  . TRP A 1 192 ? 17.796  10.544  40.095  1 30.6  ? 441  TRP A CA  1 
ATOM   611  C C   . TRP A 1 192 ? 16.979  10.428  38.793  1 31.56 ? 441  TRP A C   1 
ATOM   612  O O   . TRP A 1 192 ? 16.59   11.442  38.239  1 31.09 ? 441  TRP A O   1 
ATOM   613  C CB  . TRP A 1 192 ? 19.281  10.346  39.786  1 28.66 ? 441  TRP A CB  1 
ATOM   614  C CG  . TRP A 1 192 ? 19.771  11.117  38.599  1 26.35 ? 441  TRP A CG  1 
ATOM   615  C CD1 . TRP A 1 192 ? 20.035  12.448  38.54   1 26.08 ? 441  TRP A CD1 1 
ATOM   616  C CD2 . TRP A 1 192 ? 20.048  10.593  37.293  1 25.38 ? 441  TRP A CD2 1 
ATOM   617  N NE1 . TRP A 1 192 ? 20.509  12.779  37.291  1 26.14 ? 441  TRP A NE1 1 
ATOM   618  C CE2 . TRP A 1 192 ? 20.488  11.664  36.496  1 25.68 ? 441  TRP A CE2 1 
ATOM   619  C CE3 . TRP A 1 192 ? 19.95   9.324   36.717  1 25.57 ? 441  TRP A CE3 1 
ATOM   620  C CZ2 . TRP A 1 192 ? 20.853  11.499  35.158  1 26.03 ? 441  TRP A CZ2 1 
ATOM   621  C CZ3 . TRP A 1 192 ? 20.356  9.155   35.402  1 26.24 ? 441  TRP A CZ3 1 
ATOM   622  C CH2 . TRP A 1 192 ? 20.798  10.233  34.641  1 26.09 ? 441  TRP A CH2 1 
ATOM   623  N N   . LEU A 1 193 ? 16.788  9.2     38.29   1 32.37 ? 442  LEU A N   1 
ATOM   624  C CA  . LEU A 1 193 ? 16.106  8.992   37.03   1 34.3  ? 442  LEU A CA  1 
ATOM   625  C C   . LEU A 1 193 ? 14.651  9.411   37.101  1 36.77 ? 442  LEU A C   1 
ATOM   626  O O   . LEU A 1 193 ? 14.187  10.124  36.216  1 36.83 ? 442  LEU A O   1 
ATOM   627  C CB  . LEU A 1 193 ? 16.299  7.549   36.542  1 34.58 ? 442  LEU A CB  1 
ATOM   628  C CG  . LEU A 1 193 ? 16.07   7.253   35.068  1 36.27 ? 442  LEU A CG  1 
ATOM   629  C CD1 . LEU A 1 193 ? 16.768  8.261   34.164  1 37.12 ? 442  LEU A CD1 1 
ATOM   630  C CD2 . LEU A 1 193 ? 16.551  5.869   34.73   1 36.98 ? 442  LEU A CD2 1 
ATOM   631  N N   . TYR A 1 194 ? 13.973  9.092   38.22   1 38.57 ? 443  TYR A N   1 
ATOM   632  C CA  . TYR A 1 194 ? 12.598  9.508   38.475  1 39.88 ? 443  TYR A CA  1 
ATOM   633  C C   . TYR A 1 194 ? 12.513  11.031  38.604  1 38.58 ? 443  TYR A C   1 
ATOM   634  O O   . TYR A 1 194 ? 11.684  11.65   37.929  1 38.71 ? 443  TYR A O   1 
ATOM   635  C CB  . TYR A 1 194 ? 12.037  8.84    39.751  1 41.68 ? 443  TYR A CB  1 
ATOM   636  C CG  . TYR A 1 194 ? 10.576  9.151   39.975  1 45.23 ? 443  TYR A CG  1 
ATOM   637  C CD1 . TYR A 1 194 ? 9.588   8.479   39.271  1 47.38 ? 443  TYR A CD1 1 
ATOM   638  C CD2 . TYR A 1 194 ? 10.183  10.148  40.857  1 47.48 ? 443  TYR A CD2 1 
ATOM   639  C CE1 . TYR A 1 194 ? 8.244   8.781   39.444  1 49.18 ? 443  TYR A CE1 1 
ATOM   640  C CE2 . TYR A 1 194 ? 8.839   10.468  41.032  1 49.25 ? 443  TYR A CE2 1 
ATOM   641  C CZ  . TYR A 1 194 ? 7.871   9.777   40.325  1 50.66 ? 443  TYR A CZ  1 
ATOM   642  O OH  . TYR A 1 194 ? 6.533   10.067  40.487  1 53.06 ? 443  TYR A OH  1 
ATOM   643  N N   . LEU A 1 195 ? 13.355  11.64   39.448  1 36.89 ? 444  LEU A N   1 
ATOM   644  C CA  . LEU A 1 195 ? 13.309  13.083  39.659  1 36.65 ? 444  LEU A CA  1 
ATOM   645  C C   . LEU A 1 195 ? 13.63   13.901  38.43   1 35.26 ? 444  LEU A C   1 
ATOM   646  O O   . LEU A 1 195 ? 12.955  14.893  38.171  1 35.75 ? 444  LEU A O   1 
ATOM   647  C CB  . LEU A 1 195 ? 14.191  13.541  40.829  1 38.11 ? 444  LEU A CB  1 
ATOM   648  C CG  . LEU A 1 195 ? 13.849  12.988  42.221  1 41.31 ? 444  LEU A CG  1 
ATOM   649  C CD1 . LEU A 1 195 ? 14.835  13.516  43.27   1 41.7  ? 444  LEU A CD1 1 
ATOM   650  C CD2 . LEU A 1 195 ? 12.391  13.29   42.609  1 42.65 ? 444  LEU A CD2 1 
ATOM   651  N N   . LEU A 1 196 ? 14.674  13.516  37.681  1 33.16 ? 445  LEU A N   1 
ATOM   652  C CA  . LEU A 1 196 ? 15.067  14.257  36.492  1 30.88 ? 445  LEU A CA  1 
ATOM   653  C C   . LEU A 1 196 ? 14.013  14.106  35.38   1 31.41 ? 445  LEU A C   1 
ATOM   654  O O   . LEU A 1 196 ? 13.686  15.098  34.744  1 30.88 ? 445  LEU A O   1 
ATOM   655  C CB  . LEU A 1 196 ? 16.433  13.787  35.995  1 28.68 ? 445  LEU A CB  1 
ATOM   656  C CG  . LEU A 1 196 ? 16.925  14.366  34.663  1 26.97 ? 445  LEU A CG  1 
ATOM   657  C CD1 . LEU A 1 196 ? 17.135  15.904  34.736  1 26.01 ? 445  LEU A CD1 1 
ATOM   658  C CD2 . LEU A 1 196 ? 18.156  13.637  34.179  1 25.22 ? 445  LEU A CD2 1 
ATOM   659  N N   . SER A 1 197 ? 13.5    12.88   35.147  1 32.14 ? 446  SER A N   1 
ATOM   660  C CA  . SER A 1 197 ? 12.501  12.622  34.11   1 33.73 ? 446  SER A CA  1 
ATOM   661  C C   . SER A 1 197 ? 11.261  13.476  34.302  1 34.46 ? 446  SER A C   1 
ATOM   662  O O   . SER A 1 197 ? 10.692  13.963  33.326  1 34.93 ? 446  SER A O   1 
ATOM   663  C CB  . SER A 1 197 ? 12.093  11.155  34.089  1 36.11 ? 446  SER A CB  1 
ATOM   664  O OG  . SER A 1 197 ? 13.067  10.351  33.447  1 40.99 ? 446  SER A OG  1 
ATOM   665  N N   . HIS A 1 198 ? 10.863  13.686  35.551  1 34.38 ? 447  HIS A N   1 
ATOM   666  C CA  . HIS A 1 198 ? 9.716   14.527  35.86   1 34.64 ? 447  HIS A CA  1 
ATOM   667  C C   . HIS A 1 198 ? 10.083  15.993  35.817  1 33.91 ? 447  HIS A C   1 
ATOM   668  O O   . HIS A 1 198 ? 9.322   16.792  35.286  1 34.39 ? 447  HIS A O   1 
ATOM   669  C CB  . HIS A 1 198 ? 9.066   14.113  37.186  1 36.3  ? 447  HIS A CB  1 
ATOM   670  C CG  . HIS A 1 198 ? 8.37    12.793  37.075  1 41.01 ? 447  HIS A CG  1 
ATOM   671  N ND1 . HIS A 1 198 ? 7.097   12.691  36.54   1 43.88 ? 447  HIS A ND1 1 
ATOM   672  C CD2 . HIS A 1 198 ? 8.826   11.548  37.348  1 42.9  ? 447  HIS A CD2 1 
ATOM   673  C CE1 . HIS A 1 198 ? 6.81    11.397  36.534  1 44.59 ? 447  HIS A CE1 1 
ATOM   674  N NE2 . HIS A 1 198 ? 7.813   10.67   37.028  1 44.38 ? 447  HIS A NE2 1 
ATOM   675  N N   . GLU A 1 199 ? 11.243  16.363  36.344  1 32.58 ? 448  GLU A N   1 
ATOM   676  C CA  . GLU A 1 199 ? 11.694  17.766  36.342  1 31.97 ? 448  GLU A CA  1 
ATOM   677  C C   . GLU A 1 199 ? 11.923  18.369  34.937  1 31.32 ? 448  GLU A C   1 
ATOM   678  O O   . GLU A 1 199 ? 11.626  19.546  34.709  1 31.47 ? 448  GLU A O   1 
ATOM   679  C CB  . GLU A 1 199 ? 12.98   17.892  37.194  1 33.73 ? 448  GLU A CB  1 
ATOM   680  C CG  . GLU A 1 199 ? 13.458  19.311  37.459  1 36.94 ? 448  GLU A CG  1 
ATOM   681  C CD  . GLU A 1 199 ? 12.474  20.138  38.27   1 43.61 ? 448  GLU A CD  1 
ATOM   682  O OE1 . GLU A 1 199 ? 11.683  19.541  39.039  1 45.19 ? 448  GLU A OE1 1 
ATOM   683  O OE2 . GLU A 1 199 ? 12.482  21.384  38.124  1 44.49 ? 448  GLU A OE2 1 
ATOM   684  N N   . MET A 1 200 ? 12.477  17.584  33.998  1 30.42 ? 449  MET A N   1 
ATOM   685  C CA  . MET A 1 200 ? 12.737  18.079  32.646  1 29.88 ? 449  MET A CA  1 
ATOM   686  C C   . MET A 1 200 ? 11.457  18.433  31.87   1 29.25 ? 449  MET A C   1 
ATOM   687  O O   . MET A 1 200 ? 11.542  19.173  30.902  1 29.51 ? 449  MET A O   1 
ATOM   688  C CB  . MET A 1 200 ? 13.596  17.089  31.849  1 30.18 ? 449  MET A CB  1 
ATOM   689  C CG  . MET A 1 200 ? 12.909  15.78   31.585  1 30.66 ? 449  MET A CG  1 
ATOM   690  S SD  . MET A 1 200 ? 14.1    14.614  30.882  1 30.17 ? 449  MET A SD  1 
ATOM   691  C CE  . MET A 1 200 ? 12.989  13.26   30.49   1 24.2  ? 449  MET A CE  1 
ATOM   692  N N   . LEU A 1 201 ? 10.299  17.939  32.315  1 28.29 ? 450  LEU A N   1 
ATOM   693  C CA  . LEU A 1 201 ? 8.999   18.244  31.732  1 29.31 ? 450  LEU A CA  1 
ATOM   694  C C   . LEU A 1 201 ? 8.413   19.583  32.23   1 29.92 ? 450  LEU A C   1 
ATOM   695  O O   . LEU A 1 201 ? 7.395   20.024  31.69   1 31.02 ? 450  LEU A O   1 
ATOM   696  C CB  . LEU A 1 201 ? 8.003   17.126  32.054  1 29.19 ? 450  LEU A CB  1 
ATOM   697  C CG  . LEU A 1 201 ? 8.386   15.727  31.558  1 30.85 ? 450  LEU A CG  1 
ATOM   698  C CD1 . LEU A 1 201 ? 7.296   14.74   31.869  1 30.6  ? 450  LEU A CD1 1 
ATOM   699  C CD2 . LEU A 1 201 ? 8.678   15.722  30.055  1 31.76 ? 450  LEU A CD2 1 
ATOM   700  N N   . ASN A 1 202 ? 9.015   20.2    33.273  1 28.2  ? 451  ASN A N   1 
ATOM   701  C CA  . ASN A 1 202 ? 8.549   21.457  33.827  1 27.66 ? 451  ASN A CA  1 
ATOM   702  C C   . ASN A 1 202 ? 8.624   22.571  32.8    1 27.13 ? 451  ASN A C   1 
ATOM   703  O O   . ASN A 1 202 ? 9.719   22.896  32.32   1 27.2  ? 451  ASN A O   1 
ATOM   704  C CB  . ASN A 1 202 ? 9.423   21.837  35.023  1 29.93 ? 451  ASN A CB  1 
ATOM   705  C CG  . ASN A 1 202 ? 8.885   22.962  35.892  1 34.88 ? 451  ASN A CG  1 
ATOM   706  O OD1 . ASN A 1 202 ? 8.369   23.982  35.423  1 35.57 ? 451  ASN A OD1 1 
ATOM   707  N ND2 . ASN A 1 202 ? 9       22.79   37.191  1 36.87 ? 451  ASN A ND2 1 
ATOM   708  N N   . PRO A 1 203 ? 7.495   23.251  32.533  1 26.3  ? 452  PRO A N   1 
ATOM   709  C CA  . PRO A 1 203 ? 7.511   24.378  31.565  1 25.88 ? 452  PRO A CA  1 
ATOM   710  C C   . PRO A 1 203 ? 8.551   25.467  31.796  1 25.31 ? 452  PRO A C   1 
ATOM   711  O O   . PRO A 1 203 ? 8.956   26.161  30.862  1 24.9  ? 452  PRO A O   1 
ATOM   712  C CB  . PRO A 1 203 ? 6.094   24.944  31.672  1 26.41 ? 452  PRO A CB  1 
ATOM   713  C CG  . PRO A 1 203 ? 5.24    23.702  31.989  1 27.03 ? 452  PRO A CG  1 
ATOM   714  C CD  . PRO A 1 203 ? 6.128   22.979  33.017  1 25.76 ? 452  PRO A CD  1 
ATOM   715  N N   . TYR A 1 204 ? 9.021   25.595  33.037  1 25.29 ? 453  TYR A N   1 
ATOM   716  C CA  . TYR A 1 204 ? 10.039  26.557  33.442  1 25.98 ? 453  TYR A CA  1 
ATOM   717  C C   . TYR A 1 204 ? 11.286  26.479  32.562  1 25.39 ? 453  TYR A C   1 
ATOM   718  O O   . TYR A 1 204 ? 11.858  27.511  32.199  1 25.54 ? 453  TYR A O   1 
ATOM   719  C CB  . TYR A 1 204 ? 10.401  26.283  34.914  1 27.36 ? 453  TYR A CB  1 
ATOM   720  C CG  . TYR A 1 204 ? 11.28   27.332  35.534  1 29.24 ? 453  TYR A CG  1 
ATOM   721  C CD1 . TYR A 1 204 ? 10.751  28.534  35.971  1 31.13 ? 453  TYR A CD1 1 
ATOM   722  C CD2 . TYR A 1 204 ? 12.652  27.152  35.626  1 31.28 ? 453  TYR A CD2 1 
ATOM   723  C CE1 . TYR A 1 204 ? 11.561  29.523  36.504  1 32.49 ? 453  TYR A CE1 1 
ATOM   724  C CE2 . TYR A 1 204 ? 13.468  28.118  36.202  1 32.94 ? 453  TYR A CE2 1 
ATOM   725  C CZ  . TYR A 1 204 ? 12.911  29.296  36.657  1 33.89 ? 453  TYR A CZ  1 
ATOM   726  O OH  . TYR A 1 204 ? 13.688  30.272  37.223  1 36.86 ? 453  TYR A OH  1 
ATOM   727  N N   . TYR A 1 205 ? 11.697  25.255  32.176  1 25.27 ? 454  TYR A N   1 
ATOM   728  C CA  . TYR A 1 205 ? 12.904  25.103  31.348  1 25.7  ? 454  TYR A CA  1 
ATOM   729  C C   . TYR A 1 205 ? 12.71   25.438  29.856  1 24.79 ? 454  TYR A C   1 
ATOM   730  O O   . TYR A 1 205 ? 13.663  25.362  29.081  1 25.36 ? 454  TYR A O   1 
ATOM   731  C CB  . TYR A 1 205 ? 13.508  23.705  31.533  1 26.52 ? 454  TYR A CB  1 
ATOM   732  C CG  . TYR A 1 205 ? 13.828  23.441  32.987  1 27.91 ? 454  TYR A CG  1 
ATOM   733  C CD1 . TYR A 1 205 ? 14.858  24.117  33.627  1 28.91 ? 454  TYR A CD1 1 
ATOM   734  C CD2 . TYR A 1 205 ? 13.079  22.544  33.73   1 29.59 ? 454  TYR A CD2 1 
ATOM   735  C CE1 . TYR A 1 205 ? 15.141  23.897  34.968  1 30.31 ? 454  TYR A CE1 1 
ATOM   736  C CE2 . TYR A 1 205 ? 13.349  22.322  35.071  1 30.72 ? 454  TYR A CE2 1 
ATOM   737  C CZ  . TYR A 1 205 ? 14.363  23.021  35.694  1 31.44 ? 454  TYR A CZ  1 
ATOM   738  O OH  . TYR A 1 205 ? 14.651  22.764  37.011  1 33.14 ? 454  TYR A OH  1 
ATOM   739  N N   . GLY A 1 206 ? 11.501  25.812  29.458  1 23.87 ? 455  GLY A N   1 
ATOM   740  C CA  . GLY A 1 206 ? 11.238  26.256  28.097  1 23.48 ? 455  GLY A CA  1 
ATOM   741  C C   . GLY A 1 206 ? 11.156  25.207  27.006  1 23.13 ? 455  GLY A C   1 
ATOM   742  O O   . GLY A 1 206 ? 11.059  25.569  25.826  1 23.42 ? 455  GLY A O   1 
ATOM   743  N N   . LEU A 1 207 ? 11.124  23.913  27.372  1 21.76 ? 456  LEU A N   1 
ATOM   744  C CA  . LEU A 1 207 ? 11.049  22.847  26.362  1 20.52 ? 456  LEU A CA  1 
ATOM   745  C C   . LEU A 1 207 ? 9.64    22.385  26.107  1 20.64 ? 456  LEU A C   1 
ATOM   746  O O   . LEU A 1 207 ? 9.281   22.13   24.979  1 20.69 ? 456  LEU A O   1 
ATOM   747  C CB  . LEU A 1 207 ? 11.931  21.651  26.765  1 19.95 ? 456  LEU A CB  1 
ATOM   748  C CG  . LEU A 1 207 ? 13.39   22.007  27.066  1 22.14 ? 456  LEU A CG  1 
ATOM   749  C CD1 . LEU A 1 207 ? 14.163  20.801  27.604  1 23.41 ? 456  LEU A CD1 1 
ATOM   750  C CD2 . LEU A 1 207 ? 14.076  22.687  25.857  1 22.19 ? 456  LEU A CD2 1 
ATOM   751  N N   . PHE A 1 208 ? 8.856   22.202  27.169  1 21.68 ? 457  PHE A N   1 
ATOM   752  C CA  . PHE A 1 208 ? 7.502   21.698  27.071  1 22.82 ? 457  PHE A CA  1 
ATOM   753  C C   . PHE A 1 208 ? 6.532   22.654  27.763  1 24.83 ? 457  PHE A C   1 
ATOM   754  O O   . PHE A 1 208 ? 6.939   23.51   28.563  1 25.06 ? 457  PHE A O   1 
ATOM   755  C CB  . PHE A 1 208 ? 7.413   20.273  27.708  1 21.99 ? 457  PHE A CB  1 
ATOM   756  C CG  . PHE A 1 208 ? 8.412   19.302  27.132  1 22.56 ? 457  PHE A CG  1 
ATOM   757  C CD1 . PHE A 1 208 ? 8.2     18.716  25.888  1 22.62 ? 457  PHE A CD1 1 
ATOM   758  C CD2 . PHE A 1 208 ? 9.596   19.017  27.803  1 23.3  ? 457  PHE A CD2 1 
ATOM   759  C CE1 . PHE A 1 208 ? 9.139   17.841  25.339  1 22.6  ? 457  PHE A CE1 1 
ATOM   760  C CE2 . PHE A 1 208 ? 10.53   18.138  27.254  1 24.01 ? 457  PHE A CE2 1 
ATOM   761  C CZ  . PHE A 1 208 ? 10.296  17.553  26.026  1 22.92 ? 457  PHE A CZ  1 
ATOM   762  N N   . GLN A 1 209 ? 5.245   22.501  27.474  1 25.38 ? 458  GLN A N   1 
ATOM   763  C CA  . GLN A 1 209 ? 4.215   23.338  28.083  1 25.67 ? 458  GLN A CA  1 
ATOM   764  C C   . GLN A 1 209 ? 2.888   22.587  28.05   1 26.96 ? 458  GLN A C   1 
ATOM   765  O O   . GLN A 1 209 ? 2.736   21.629  27.281  1 26.55 ? 458  GLN A O   1 
ATOM   766  C CB  . GLN A 1 209 ? 4.076   24.652  27.271  1 25.81 ? 458  GLN A CB  1 
ATOM   767  C CG  . GLN A 1 209 ? 3.765   24.376  25.805  1 26.17 ? 458  GLN A CG  1 
ATOM   768  C CD  . GLN A 1 209 ? 3.513   25.604  24.956  1 30.07 ? 458  GLN A CD  1 
ATOM   769  O OE1 . GLN A 1 209 ? 2.863   25.52   23.9    1 30.8  ? 458  GLN A OE1 1 
ATOM   770  N NE2 . GLN A 1 209 ? 4.022   26.765  25.379  1 28.71 ? 458  GLN A NE2 1 
ATOM   771  N N   . TYR A 1 210 ? 1.923   23.008  28.885  1 28.25 ? 459  TYR A N   1 
ATOM   772  C CA  . TYR A 1 210 ? 0.599   22.385  28.858  1 30.99 ? 459  TYR A CA  1 
ATOM   773  C C   . TYR A 1 210 ? -0.247  23.049  27.798  1 34.24 ? 459  TYR A C   1 
ATOM   774  O O   . TYR A 1 210 ? -0.162  24.262  27.615  1 34.03 ? 459  TYR A O   1 
ATOM   775  C CB  . TYR A 1 210 ? -0.084  22.462  30.231  1 31.69 ? 459  TYR A CB  1 
ATOM   776  C CG  . TYR A 1 210 ? 0.558   21.49   31.181  1 33.22 ? 459  TYR A CG  1 
ATOM   777  C CD1 . TYR A 1 210 ? 0.262   20.137  31.121  1 34.52 ? 459  TYR A CD1 1 
ATOM   778  C CD2 . TYR A 1 210 ? 1.576   21.895  32.034  1 34.72 ? 459  TYR A CD2 1 
ATOM   779  C CE1 . TYR A 1 210 ? 0.909   19.221  31.942  1 36.48 ? 459  TYR A CE1 1 
ATOM   780  C CE2 . TYR A 1 210 ? 2.251   20.986  32.835  1 36.17 ? 459  TYR A CE2 1 
ATOM   781  C CZ  . TYR A 1 210 ? 1.903   19.649  32.799  1 37.83 ? 459  TYR A CZ  1 
ATOM   782  O OH  . TYR A 1 210 ? 2.586   18.739  33.572  1 40.92 ? 459  TYR A OH  1 
ATOM   783  N N   . SER A 1 211 ? -1.063  22.263  27.08   1 37.22 ? 460  SER A N   1 
ATOM   784  C CA  . SER A 1 211 ? -1.932  22.819  26.051  1 40.67 ? 460  SER A CA  1 
ATOM   785  C C   . SER A 1 211 ? -2.943  23.797  26.673  1 43.94 ? 460  SER A C   1 
ATOM   786  O O   . SER A 1 211 ? -3.387  23.591  27.803  1 43.51 ? 460  SER A O   1 
ATOM   787  C CB  . SER A 1 211 ? -2.67   21.705  25.312  1 42.46 ? 460  SER A CB  1 
ATOM   788  O OG  . SER A 1 211 ? -3.54   22.256  24.336  1 45.44 ? 460  SER A OG  1 
ATOM   789  N N   . ARG A 1 212 ? -3.25   24.887  25.96   1 47.22 ? 461  ARG A N   1 
ATOM   790  C CA  . ARG A 1 212 ? -4.228  25.867  26.435  1 50.7  ? 461  ARG A CA  1 
ATOM   791  C C   . ARG A 1 212 ? -5.64   25.253  26.39   1 53.22 ? 461  ARG A C   1 
ATOM   792  O O   . ARG A 1 212 ? -6.412  25.404  27.337  1 53.7  ? 461  ARG A O   1 
ATOM   793  C CB  . ARG A 1 212 ? -4.157  27.153  25.592  1 52.98 ? 461  ARG A CB  1 
ATOM   794  C CG  . ARG A 1 212 ? -3.142  28.164  26.126  1 57.48 ? 461  ARG A CG  1 
ATOM   795  C CD  . ARG A 1 212 ? -2.303  28.787  25.017  1 61.57 ? 461  ARG A CD  1 
ATOM   796  N NE  . ARG A 1 212 ? -0.881  28.824  25.372  1 65.33 ? 461  ARG A NE  1 
ATOM   797  C CZ  . ARG A 1 212 ? 0.099   29.12   24.524  1 68.2  ? 461  ARG A CZ  1 
ATOM   798  N NH1 . ARG A 1 212 ? -0.174  29.415  23.258  1 68.18 ? 461  ARG A NH1 1 
ATOM   799  N NH2 . ARG A 1 212 ? 1.361   29.122  24.934  1 68.58 ? 461  ARG A NH2 1 
ATOM   800  N N   . ASP A 1 213 ? -5.934  24.503  25.31   1 54.68 ? 462  ASP A N   1 
ATOM   801  C CA  . ASP A 1 213 ? -7.209  23.821  25.063  1 56.07 ? 462  ASP A CA  1 
ATOM   802  C C   . ASP A 1 213 ? -7.373  22.602  25.967  1 56.88 ? 462  ASP A C   1 
ATOM   803  O O   . ASP A 1 213 ? -8.451  22.391  26.533  1 57.46 ? 462  ASP A O   1 
ATOM   804  C CB  . ASP A 1 213 ? -7.308  23.418  23.586  1 58.28 ? 462  ASP A CB  1 
ATOM   805  C CG  . ASP A 1 213 ? -6.977  24.565  22.647  1 63.66 ? 462  ASP A CG  1 
ATOM   806  O OD1 . ASP A 1 213 ? -7.573  25.658  22.809  1 64.35 ? 462  ASP A OD1 1 
ATOM   807  O OD2 . ASP A 1 213 ? -6.107  24.378  21.765  1 66.04 ? 462  ASP A OD2 1 
ATOM   808  N N   . ASP A 1 214 ? -6.306  21.803  26.116  1 56.5  ? 463  ASP A N   1 
ATOM   809  C CA  . ASP A 1 214 ? -6.345  20.648  27.002  1 56.49 ? 463  ASP A CA  1 
ATOM   810  C C   . ASP A 1 214 ? -5.328  20.826  28.12   1 55.95 ? 463  ASP A C   1 
ATOM   811  O O   . ASP A 1 214 ? -4.162  20.453  27.982  1 55.96 ? 463  ASP A O   1 
ATOM   812  C CB  . ASP A 1 214 ? -6.112  19.34   26.249  1 58.84 ? 463  ASP A CB  1 
ATOM   813  C CG  . ASP A 1 214 ? -6.786  18.177  26.945  1 64.78 ? 463  ASP A CG  1 
ATOM   814  O OD1 . ASP A 1 214 ? -6.415  17.88   28.114  1 65.53 ? 463  ASP A OD1 1 
ATOM   815  O OD2 . ASP A 1 214 ? -7.698  17.576  26.341  1 67.83 ? 463  ASP A OD2 1 
ATOM   816  N N   . ILE A 1 215 ? -5.798  21.363  29.243  1 55.12 ? 464  ILE A N   1 
ATOM   817  C CA  . ILE A 1 215 ? -5.033  21.73   30.431  1 54.44 ? 464  ILE A CA  1 
ATOM   818  C C   . ILE A 1 215 ? -4.179  20.568  31.047  1 52.79 ? 464  ILE A C   1 
ATOM   819  O O   . ILE A 1 215 ? -3.226  20.84   31.779  1 52.76 ? 464  ILE A O   1 
ATOM   820  C CB  . ILE A 1 215 ? -6.034  22.379  31.436  1 55.31 ? 464  ILE A CB  1 
ATOM   821  C CG1 . ILE A 1 215 ? -5.555  23.773  31.862  1 56.6  ? 464  ILE A CG1 1 
ATOM   822  C CG2 . ILE A 1 215 ? -6.405  21.498  32.631  1 55.87 ? 464  ILE A CG2 1 
ATOM   823  C CD1 . ILE A 1 215 ? -5.736  24.845  30.775  1 58.02 ? 464  ILE A CD1 1 
ATOM   824  N N   . TYR A 1 216 ? -4.479  19.303  30.721  1 51.38 ? 465  TYR A N   1 
ATOM   825  C CA  . TYR A 1 216 ? -3.702  18.163  31.238  1 50.17 ? 465  TYR A CA  1 
ATOM   826  C C   . TYR A 1 216 ? -2.646  17.64   30.24   1 46.43 ? 465  TYR A C   1 
ATOM   827  O O   . TYR A 1 216 ? -1.799  16.828  30.616  1 46.7  ? 465  TYR A O   1 
ATOM   828  C CB  . TYR A 1 216 ? -4.634  16.998  31.612  1 51.77 ? 465  TYR A CB  1 
ATOM   829  C CG  . TYR A 1 216 ? -5.414  17.233  32.886  1 54.99 ? 465  TYR A CG  1 
ATOM   830  C CD1 . TYR A 1 216 ? -6.6    17.954  32.875  1 57.2  ? 465  TYR A CD1 1 
ATOM   831  C CD2 . TYR A 1 216 ? -4.986  16.703  34.095  1 56.67 ? 465  TYR A CD2 1 
ATOM   832  C CE1 . TYR A 1 216 ? -7.318  18.183  34.046  1 58.77 ? 465  TYR A CE1 1 
ATOM   833  C CE2 . TYR A 1 216 ? -5.702  16.912  35.269  1 58.32 ? 465  TYR A CE2 1 
ATOM   834  C CZ  . TYR A 1 216 ? -6.869  17.652  35.242  1 59.99 ? 465  TYR A CZ  1 
ATOM   835  O OH  . TYR A 1 216 ? -7.57   17.873  36.411  1 62.6  ? 465  TYR A OH  1 
ATOM   836  N N   . THR A 1 217 ? -2.724  18.052  28.972  1 42.56 ? 466  THR A N   1 
ATOM   837  C CA  . THR A 1 217 ? -1.818  17.547  27.947  1 39.29 ? 466  THR A CA  1 
ATOM   838  C C   . THR A 1 217 ? -0.484  18.287  27.87   1 34.86 ? 466  THR A C   1 
ATOM   839  O O   . THR A 1 217 ? -0.458  19.507  27.723  1 34.3  ? 466  THR A O   1 
ATOM   840  C CB  . THR A 1 217 ? -2.525  17.529  26.594  1 39.73 ? 466  THR A CB  1 
ATOM   841  O OG1 . THR A 1 217 ? -3.637  16.638  26.686  1 41.25 ? 466  THR A OG1 1 
ATOM   842  C CG2 . THR A 1 217 ? -1.614  17.108  25.476  1 38.75 ? 466  THR A CG2 1 
ATOM   843  N N   . LEU A 1 218 ? 0.617   17.533  27.938  1 31.6  ? 467  LEU A N   1 
ATOM   844  C CA  . LEU A 1 218 ? 1.937   18.116  27.778  1 29.06 ? 467  LEU A CA  1 
ATOM   845  C C   . LEU A 1 218 ? 2.325   18.067  26.295  1 27.06 ? 467  LEU A C   1 
ATOM   846  O O   . LEU A 1 218 ? 2.019   17.094  25.59   1 26.72 ? 467  LEU A O   1 
ATOM   847  C CB  . LEU A 1 218 ? 2.98    17.414  28.649  1 28.66 ? 467  LEU A CB  1 
ATOM   848  C CG  . LEU A 1 218 ? 4.239   18.249  28.897  1 29.83 ? 467  LEU A CG  1 
ATOM   849  C CD1 . LEU A 1 218 ? 3.983   19.374  29.917  1 29.72 ? 467  LEU A CD1 1 
ATOM   850  C CD2 . LEU A 1 218 ? 5.414   17.375  29.313  1 31.31 ? 467  LEU A CD2 1 
ATOM   851  N N   . GLN A 1 219 ? 2.958   19.147  25.802  1 25.51 ? 468  GLN A N   1 
ATOM   852  C CA  . GLN A 1 219 ? 3.397   19.229  24.409  1 24.11 ? 468  GLN A CA  1 
ATOM   853  C C   . GLN A 1 219 ? 4.701   19.998  24.325  1 23.4  ? 468  GLN A C   1 
ATOM   854  O O   . GLN A 1 219 ? 5.058   20.696  25.279  1 24.48 ? 468  GLN A O   1 
ATOM   855  C CB  . GLN A 1 219 ? 2.322   19.933  23.554  1 23.99 ? 468  GLN A CB  1 
ATOM   856  C CG  . GLN A 1 219 ? 2.179   21.422  23.872  1 26.5  ? 468  GLN A CG  1 
ATOM   857  C CD  . GLN A 1 219 ? 0.99    22.085  23.221  1 33.46 ? 468  GLN A CD  1 
ATOM   858  O OE1 . GLN A 1 219 ? 0.962   23.309  23.031  1 36.67 ? 468  GLN A OE1 1 
ATOM   859  N NE2 . GLN A 1 219 ? -0.014  21.309  22.882  1 32.33 ? 468  GLN A NE2 1 
ATOM   860  N N   . ILE A 1 220 ? 5.395   19.914  23.185  1 21.68 ? 469  ILE A N   1 
ATOM   861  C CA  . ILE A 1 220 ? 6.604   20.68   22.966  1 21.29 ? 469  ILE A CA  1 
ATOM   862  C C   . ILE A 1 220 ? 6.232   22.184  22.854  1 21.69 ? 469  ILE A C   1 
ATOM   863  O O   . ILE A 1 220 ? 5.238   22.523  22.204  1 21.77 ? 469  ILE A O   1 
ATOM   864  C CB  . ILE A 1 220 ? 7.284   20.175  21.672  1 20.49 ? 469  ILE A CB  1 
ATOM   865  C CG1 . ILE A 1 220 ? 7.951   18.812  21.909  1 20.69 ? 469  ILE A CG1 1 
ATOM   866  C CG2 . ILE A 1 220 ? 8.291   21.194  21.105  1 20.52 ? 469  ILE A CG2 1 
ATOM   867  C CD1 . ILE A 1 220 ? 8.441   18.181  20.587  1 22.33 ? 469  ILE A CD1 1 
ATOM   868  N N   . ASN A 1 221 ? 7.036   23.057  23.441  1 20.55 ? 470  ASN A N   1 
ATOM   869  C CA  . ASN A 1 221 ? 6.817   24.504  23.329  1 21.42 ? 470  ASN A CA  1 
ATOM   870  C C   . ASN A 1 221 ? 7.28    24.923  21.919  1 22.18 ? 470  ASN A C   1 
ATOM   871  O O   . ASN A 1 221 ? 8.458   24.765  21.604  1 23.17 ? 470  ASN A O   1 
ATOM   872  C CB  . ASN A 1 221 ? 7.614   25.253  24.444  1 22.4  ? 470  ASN A CB  1 
ATOM   873  C CG  . ASN A 1 221 ? 7.667   26.759  24.244  1 23.89 ? 470  ASN A CG  1 
ATOM   874  O OD1 . ASN A 1 221 ? 6.886   27.319  23.487  1 22.71 ? 470  ASN A OD1 1 
ATOM   875  N ND2 . ASN A 1 221 ? 8.622   27.432  24.863  1 25.02 ? 470  ASN A ND2 1 
ATOM   876  N N   . PRO A 1 222 ? 6.368   25.371  21.014  1 22.31 ? 471  PRO A N   1 
ATOM   877  C CA  . PRO A 1 222 ? 6.819   25.779  19.671  1 22.16 ? 471  PRO A CA  1 
ATOM   878  C C   . PRO A 1 222 ? 7.782   26.972  19.616  1 21.64 ? 471  PRO A C   1 
ATOM   879  O O   . PRO A 1 222 ? 8.556   27.084  18.666  1 22.7  ? 471  PRO A O   1 
ATOM   880  C CB  . PRO A 1 222 ? 5.506   26.07   18.9    1 24.01 ? 471  PRO A CB  1 
ATOM   881  C CG  . PRO A 1 222 ? 4.375   25.753  19.854  1 24.42 ? 471  PRO A CG  1 
ATOM   882  C CD  . PRO A 1 222 ? 4.921   25.627  21.227  1 21.95 ? 471  PRO A CD  1 
ATOM   883  N N   . ASP A 1 223 ? 7.796   27.821  20.637  1 21.31 ? 472  ASP A N   1 
ATOM   884  C CA  . ASP A 1 223 ? 8.693   28.979  20.726  1 21.59 ? 472  ASP A CA  1 
ATOM   885  C C   . ASP A 1 223 ? 9.973   28.657  21.528  1 22.93 ? 472  ASP A C   1 
ATOM   886  O O   . ASP A 1 223 ? 10.61   29.581  22.026  1 23.44 ? 472  ASP A O   1 
ATOM   887  C CB  . ASP A 1 223 ? 7.983   30.116  21.474  1 22.42 ? 472  ASP A CB  1 
ATOM   888  C CG  . ASP A 1 223 ? 6.732   30.648  20.783  1 28.9  ? 472  ASP A CG  1 
ATOM   889  O OD1 . ASP A 1 223 ? 6.282   30.016  19.793  1 29.61 ? 472  ASP A OD1 1 
ATOM   890  O OD2 . ASP A 1 223 ? 6.214   31.706  21.223  1 29.74 ? 472  ASP A OD2 1 
ATOM   891  N N   . SER A 1 224 ? 10.314  27.377  21.711  1 22.43 ? 473  SER A N   1 
ATOM   892  C CA  . SER A 1 224 ? 11.473  26.986  22.5    1 23.22 ? 473  SER A CA  1 
ATOM   893  C C   . SER A 1 224 ? 12.775  27.631  22.025  1 25.02 ? 473  SER A C   1 
ATOM   894  O O   . SER A 1 224 ? 13.719  27.76   22.817  1 25.6  ? 473  SER A O   1 
ATOM   895  C CB  . SER A 1 224 ? 11.598  25.463  22.528  1 23.36 ? 473  SER A CB  1 
ATOM   896  O OG  . SER A 1 224 ? 11.923  24.954  21.244  1 23.71 ? 473  SER A OG  1 
ATOM   897  N N   . ALA A 1 225 ? 12.821  28.076  20.749  1 25.56 ? 474  ALA A N   1 
ATOM   898  C CA  . ALA A 1 225 ? 14      28.704  20.163  1 26.37 ? 474  ALA A CA  1 
ATOM   899  C C   . ALA A 1 225 ? 14.41   30.017  20.821  1 27.29 ? 474  ALA A C   1 
ATOM   900  O O   . ALA A 1 225 ? 15.505  30.488  20.549  1 28.07 ? 474  ALA A O   1 
ATOM   901  C CB  . ALA A 1 225 ? 13.823  28.882  18.667  1 26.64 ? 474  ALA A CB  1 
ATOM   902  N N   . VAL A 1 226 ? 13.596  30.582  21.732  1 27.53 ? 475  VAL A N   1 
ATOM   903  C CA  . VAL A 1 226 ? 14.007  31.773  22.491  1 28.83 ? 475  VAL A CA  1 
ATOM   904  C C   . VAL A 1 226 ? 15.339  31.46   23.282  1 29.9  ? 475  VAL A C   1 
ATOM   905  O O   . VAL A 1 226 ? 16.172  32.344  23.461  1 30    ? 475  VAL A O   1 
ATOM   906  C CB  . VAL A 1 226 ? 12.874  32.356  23.374  1 29.86 ? 475  VAL A CB  1 
ATOM   907  C CG1 . VAL A 1 226 ? 11.702  32.824  22.508  1 30.74 ? 475  VAL A CG1 1 
ATOM   908  C CG2 . VAL A 1 226 ? 12.388  31.337  24.406  1 30.5  ? 475  VAL A CG2 1 
ATOM   909  N N   . ASN A 1 227 ? 15.564  30.17   23.637  1 29.65 ? 476  ASN A N   1 
ATOM   910  C CA  . ASN A 1 227 ? 16.817  29.685  24.198  1 30.1  ? 476  ASN A CA  1 
ATOM   911  C C   . ASN A 1 227 ? 17.551  29.132  22.968  1 29.78 ? 476  ASN A C   1 
ATOM   912  O O   . ASN A 1 227 ? 17.132  28.133  22.386  1 29.3  ? 476  ASN A O   1 
ATOM   913  C CB  . ASN A 1 227 ? 16.573  28.581  25.23   1 32.08 ? 476  ASN A CB  1 
ATOM   914  C CG  . ASN A 1 227 ? 17.825  27.841  25.664  1 38.14 ? 476  ASN A CG  1 
ATOM   915  O OD1 . ASN A 1 227 ? 18.959  28.115  25.221  1 39.31 ? 476  ASN A OD1 1 
ATOM   916  N ND2 . ASN A 1 227 ? 17.643  26.865  26.543  1 40.61 ? 476  ASN A ND2 1 
ATOM   917  N N   . PRO A 1 228 ? 18.636  29.789  22.545  1 29.92 ? 477  PRO A N   1 
ATOM   918  C CA  . PRO A 1 228 ? 19.344  29.346  21.329  1 29.97 ? 477  PRO A CA  1 
ATOM   919  C C   . PRO A 1 228 ? 19.924  27.936  21.373  1 29.14 ? 477  PRO A C   1 
ATOM   920  O O   . PRO A 1 228 ? 20.155  27.343  20.327  1 29.51 ? 477  PRO A O   1 
ATOM   921  C CB  . PRO A 1 228 ? 20.441  30.411  21.146  1 31.17 ? 477  PRO A CB  1 
ATOM   922  C CG  . PRO A 1 228 ? 20.604  31.036  22.483  1 31.72 ? 477  PRO A CG  1 
ATOM   923  C CD  . PRO A 1 228 ? 19.247  30.998  23.129  1 29.84 ? 477  PRO A CD  1 
ATOM   924  N N   . GLU A 1 229 ? 20.176  27.408  22.572  1 27.7  ? 478  GLU A N   1 
ATOM   925  C CA  . GLU A 1 229 ? 20.682  26.044  22.743  1 26.96 ? 478  GLU A CA  1 
ATOM   926  C C   . GLU A 1 229 ? 19.551  25.022  22.859  1 24.27 ? 478  GLU A C   1 
ATOM   927  O O   . GLU A 1 229 ? 19.839  23.89   23.233  1 23.93 ? 478  GLU A O   1 
ATOM   928  C CB  . GLU A 1 229 ? 21.47   25.939  24.063  1 30.63 ? 478  GLU A CB  1 
ATOM   929  C CG  . GLU A 1 229 ? 22.908  26.423  24.086  1 40.02 ? 478  GLU A CG  1 
ATOM   930  C CD  . GLU A 1 229 ? 23.608  25.907  25.341  1 52.37 ? 478  GLU A CD  1 
ATOM   931  O OE1 . GLU A 1 229 ? 23.653  26.654  26.349  1 55.79 ? 478  GLU A OE1 1 
ATOM   932  O OE2 . GLU A 1 229 ? 24.061  24.735  25.337  1 54.56 ? 478  GLU A OE2 1 
ATOM   933  N N   . HIS A 1 230 ? 18.28   25.387  22.583  1 22.59 ? 479  HIS A N   1 
ATOM   934  C CA  . HIS A 1 230 ? 17.144  24.495  22.808  1 21.85 ? 479  HIS A CA  1 
ATOM   935  C C   . HIS A 1 230 ? 17.291  23.107  22.181  1 21.32 ? 479  HIS A C   1 
ATOM   936  O O   . HIS A 1 230 ? 16.924  22.144  22.837  1 22.05 ? 479  HIS A O   1 
ATOM   937  C CB  . HIS A 1 230 ? 15.804  25.137  22.419  1 21.52 ? 479  HIS A CB  1 
ATOM   938  C CG  . HIS A 1 230 ? 15.602  25.304  20.93   1 21.81 ? 479  HIS A CG  1 
ATOM   939  N ND1 . HIS A 1 230 ? 14.416  24.921  20.313  1 22.52 ? 479  HIS A ND1 1 
ATOM   940  C CD2 . HIS A 1 230 ? 16.442  25.801  19.986  1 21.91 ? 479  HIS A CD2 1 
ATOM   941  C CE1 . HIS A 1 230 ? 14.574  25.192  19.03   1 22.51 ? 479  HIS A CE1 1 
ATOM   942  N NE2 . HIS A 1 230 ? 15.785  25.698  18.782  1 23.22 ? 479  HIS A NE2 1 
ATOM   943  N N   . LEU A 1 231 ? 17.882  22.978  20.998  1 21.28 ? 480  LEU A N   1 
ATOM   944  C CA  . LEU A 1 231 ? 18.002  21.671  20.342  1 22.18 ? 480  LEU A CA  1 
ATOM   945  C C   . LEU A 1 231 ? 18.875  20.7    21.09   1 23.07 ? 480  LEU A C   1 
ATOM   946  O O   . LEU A 1 231 ? 18.537  19.526  21.188  1 22.84 ? 480  LEU A O   1 
ATOM   947  C CB  . LEU A 1 231 ? 18.443  21.797  18.88   1 22.08 ? 480  LEU A CB  1 
ATOM   948  C CG  . LEU A 1 231 ? 17.445  22.518  17.96   1 23.1  ? 480  LEU A CG  1 
ATOM   949  C CD1 . LEU A 1 231 ? 17.898  22.424  16.501  1 23.08 ? 480  LEU A CD1 1 
ATOM   950  C CD2 . LEU A 1 231 ? 15.992  21.97   18.138  1 23.49 ? 480  LEU A CD2 1 
ATOM   951  N N   . SER A 1 232 ? 19.971  21.194  21.662  1 23.49 ? 481  SER A N   1 
ATOM   952  C CA  . SER A 1 232 ? 20.836  20.362  22.484  1 24.25 ? 481  SER A CA  1 
ATOM   953  C C   . SER A 1 232 ? 20.089  19.916  23.74   1 23.35 ? 481  SER A C   1 
ATOM   954  O O   . SER A 1 232 ? 20.257  18.779  24.156  1 23.64 ? 481  SER A O   1 
ATOM   955  C CB  . SER A 1 232 ? 22.107  21.124  22.857  1 27.12 ? 481  SER A CB  1 
ATOM   956  O OG  . SER A 1 232 ? 22.902  20.266  23.657  1 33.04 ? 481  SER A OG  1 
ATOM   957  N N   . TYR A 1 233 ? 19.208  20.768  24.304  1 22.61 ? 482  TYR A N   1 
ATOM   958  C CA  . TYR A 1 233 ? 18.401  20.385  25.454  1 22.59 ? 482  TYR A CA  1 
ATOM   959  C C   . TYR A 1 233 ? 17.366  19.316  25.115  1 21.85 ? 482  TYR A C   1 
ATOM   960  O O   . TYR A 1 233 ? 17.112  18.451  25.959  1 21.39 ? 482  TYR A O   1 
ATOM   961  C CB  . TYR A 1 233 ? 17.743  21.598  26.14   1 23.11 ? 482  TYR A CB  1 
ATOM   962  C CG  . TYR A 1 233 ? 18.712  22.393  26.985  1 24.6  ? 482  TYR A CG  1 
ATOM   963  C CD1 . TYR A 1 233 ? 19.473  23.408  26.432  1 26.42 ? 482  TYR A CD1 1 
ATOM   964  C CD2 . TYR A 1 233 ? 18.872  22.12   28.333  1 26.26 ? 482  TYR A CD2 1 
ATOM   965  C CE1 . TYR A 1 233 ? 20.361  24.148  27.202  1 28.16 ? 482  TYR A CE1 1 
ATOM   966  C CE2 . TYR A 1 233 ? 19.761  22.85   29.12   1 27.69 ? 482  TYR A CE2 1 
ATOM   967  C CZ  . TYR A 1 233 ? 20.491  23.874  28.552  1 28.98 ? 482  TYR A CZ  1 
ATOM   968  O OH  . TYR A 1 233 ? 21.371  24.589  29.31   1 30.54 ? 482  TYR A OH  1 
ATOM   969  N N   . PHE A 1 234 ? 16.712  19.405  23.928  1 20.41 ? 483  PHE A N   1 
ATOM   970  C CA  . PHE A 1 234 ? 15.757  18.37   23.503  1 19.95 ? 483  PHE A CA  1 
ATOM   971  C C   . PHE A 1 234 ? 16.498  17.057  23.273  1 20.84 ? 483  PHE A C   1 
ATOM   972  O O   . PHE A 1 234 ? 15.978  15.994  23.61   1 20.55 ? 483  PHE A O   1 
ATOM   973  C CB  . PHE A 1 234 ? 14.993  18.762  22.223  1 18.56 ? 483  PHE A CB  1 
ATOM   974  C CG  . PHE A 1 234 ? 13.88   19.754  22.455  1 18.46 ? 483  PHE A CG  1 
ATOM   975  C CD1 . PHE A 1 234 ? 12.678  19.354  22.994  1 19.22 ? 483  PHE A CD1 1 
ATOM   976  C CD2 . PHE A 1 234 ? 14.043  21.095  22.13   1 19.3  ? 483  PHE A CD2 1 
ATOM   977  C CE1 . PHE A 1 234 ? 11.671  20.279  23.235  1 19.92 ? 483  PHE A CE1 1 
ATOM   978  C CE2 . PHE A 1 234 ? 13.041  22.017  22.388  1 19.29 ? 483  PHE A CE2 1 
ATOM   979  C CZ  . PHE A 1 234 ? 11.847  21.601  22.897  1 19.05 ? 483  PHE A CZ  1 
ATOM   980  N N   . HIS A 1 235 ? 17.733  17.118  22.714  1 21.87 ? 484  HIS A N   1 
ATOM   981  C CA  . HIS A 1 235 ? 18.569  15.929  22.519  1 23.19 ? 484  HIS A CA  1 
ATOM   982  C C   . HIS A 1 235 ? 18.818  15.242  23.867  1 22.65 ? 484  HIS A C   1 
ATOM   983  O O   . HIS A 1 235 ? 18.644  14.022  23.998  1 22.68 ? 484  HIS A O   1 
ATOM   984  C CB  . HIS A 1 235 ? 19.885  16.303  21.816  1 25.66 ? 484  HIS A CB  1 
ATOM   985  C CG  . HIS A 1 235 ? 20.762  15.132  21.47   1 32.87 ? 484  HIS A CG  1 
ATOM   986  N ND1 . HIS A 1 235 ? 21.302  14.992  20.213  1 37.53 ? 484  HIS A ND1 1 
ATOM   987  C CD2 . HIS A 1 235 ? 21.185  14.097  22.233  1 34.61 ? 484  HIS A CD2 1 
ATOM   988  C CE1 . HIS A 1 235 ? 22.043  13.891  20.255  1 37.88 ? 484  HIS A CE1 1 
ATOM   989  N NE2 . HIS A 1 235 ? 22.004  13.325  21.449  1 36.19 ? 484  HIS A NE2 1 
ATOM   990  N N   . PHE A 1 236 ? 19.177  16.041  24.873  1 21.97 ? 485  PHE A N   1 
ATOM   991  C CA  . PHE A 1 236 ? 19.373  15.596  26.235  1 22.62 ? 485  PHE A CA  1 
ATOM   992  C C   . PHE A 1 236 ? 18.098  14.921  26.818  1 22.22 ? 485  PHE A C   1 
ATOM   993  O O   . PHE A 1 236 ? 18.195  13.829  27.388  1 23.36 ? 485  PHE A O   1 
ATOM   994  C CB  . PHE A 1 236 ? 19.848  16.794  27.113  1 22.81 ? 485  PHE A CB  1 
ATOM   995  C CG  . PHE A 1 236 ? 19.7    16.57   28.591  1 23.85 ? 485  PHE A CG  1 
ATOM   996  C CD1 . PHE A 1 236 ? 20.474  15.623  29.246  1 24.34 ? 485  PHE A CD1 1 
ATOM   997  C CD2 . PHE A 1 236 ? 18.783  17.301  29.329  1 25.28 ? 485  PHE A CD2 1 
ATOM   998  C CE1 . PHE A 1 236 ? 20.298  15.373  30.594  1 25.41 ? 485  PHE A CE1 1 
ATOM   999  C CE2 . PHE A 1 236 ? 18.619  17.061  30.691  1 26.53 ? 485  PHE A CE2 1 
ATOM   1000 C CZ  . PHE A 1 236 ? 19.375  16.091  31.311  1 26.17 ? 485  PHE A CZ  1 
ATOM   1001 N N   . VAL A 1 237 ? 16.911  15.539  26.665  1 20.81 ? 486  VAL A N   1 
ATOM   1002 C CA  . VAL A 1 237 ? 15.654  14.947  27.162  1 20.11 ? 486  VAL A CA  1 
ATOM   1003 C C   . VAL A 1 237 ? 15.38   13.588  26.489  1 20.6  ? 486  VAL A C   1 
ATOM   1004 O O   . VAL A 1 237 ? 14.911  12.641  27.146  1 19.7  ? 486  VAL A O   1 
ATOM   1005 C CB  . VAL A 1 237 ? 14.458  15.922  27.022  1 20.25 ? 486  VAL A CB  1 
ATOM   1006 C CG1 . VAL A 1 237 ? 13.125  15.231  27.314  1 19.99 ? 486  VAL A CG1 1 
ATOM   1007 C CG2 . VAL A 1 237 ? 14.638  17.141  27.923  1 20.31 ? 486  VAL A CG2 1 
ATOM   1008 N N   . GLY A 1 238 ? 15.694  13.494  25.19   1 20.45 ? 487  GLY A N   1 
ATOM   1009 C CA  . GLY A 1 238 ? 15.542  12.248  24.439  1 20.99 ? 487  GLY A CA  1 
ATOM   1010 C C   . GLY A 1 238 ? 16.419  11.155  25.021  1 21.36 ? 487  GLY A C   1 
ATOM   1011 O O   . GLY A 1 238 ? 15.947  10.043  25.268  1 20.93 ? 487  GLY A O   1 
ATOM   1012 N N   . ARG A 1 239 ? 17.685  11.507  25.351  1 22.31 ? 488  ARG A N   1 
ATOM   1013 C CA  . ARG A 1 239 ? 18.624  10.601  26.004  1 22.4  ? 488  ARG A CA  1 
ATOM   1014 C C   . ARG A 1 239 ? 18.064  10.105  27.316  1 23.23 ? 488  ARG A C   1 
ATOM   1015 O O   . ARG A 1 239 ? 18.129  8.903   27.583  1 24.23 ? 488  ARG A O   1 
ATOM   1016 C CB  . ARG A 1 239 ? 19.986  11.269  26.246  1 22.15 ? 488  ARG A CB  1 
ATOM   1017 C CG  . ARG A 1 239 ? 20.853  11.364  25.016  1 22.34 ? 488  ARG A CG  1 
ATOM   1018 C CD  . ARG A 1 239 ? 22.22   11.921  25.348  1 22.97 ? 488  ARG A CD  1 
ATOM   1019 N NE  . ARG A 1 239 ? 23.123  11.776  24.202  1 26.66 ? 488  ARG A NE  1 
ATOM   1020 C CZ  . ARG A 1 239 ? 24.451  11.809  24.281  1 28.51 ? 488  ARG A CZ  1 
ATOM   1021 N NH1 . ARG A 1 239 ? 25.048  12.045  25.442  1 27.59 ? 488  ARG A NH1 1 
ATOM   1022 N NH2 . ARG A 1 239 ? 25.188  11.647  23.194  1 28.47 ? 488  ARG A NH2 1 
ATOM   1023 N N   . ILE A 1 240 ? 17.495  11.014  28.13   1 22.38 ? 489  ILE A N   1 
ATOM   1024 C CA  . ILE A 1 240 ? 16.9    10.663  29.416  1 22.17 ? 489  ILE A CA  1 
ATOM   1025 C C   . ILE A 1 240 ? 15.681  9.78    29.275  1 22.14 ? 489  ILE A C   1 
ATOM   1026 O O   . ILE A 1 240 ? 15.564  8.797   30.01   1 21.24 ? 489  ILE A O   1 
ATOM   1027 C CB  . ILE A 1 240 ? 16.625  11.909  30.293  1 22.19 ? 489  ILE A CB  1 
ATOM   1028 C CG1 . ILE A 1 240 ? 17.962  12.658  30.552  1 22.39 ? 489  ILE A CG1 1 
ATOM   1029 C CG2 . ILE A 1 240 ? 15.963  11.512  31.592  1 22.47 ? 489  ILE A CG2 1 
ATOM   1030 C CD1 . ILE A 1 240 ? 19.083  11.763  31.207  1 22.65 ? 489  ILE A CD1 1 
ATOM   1031 N N   . MET A 1 241 ? 14.797  10.066  28.302  1 22.54 ? 490  MET A N   1 
ATOM   1032 C CA  . MET A 1 241 ? 13.65   9.188   28.051  1 23.27 ? 490  MET A CA  1 
ATOM   1033 C C   . MET A 1 241 ? 14.125  7.791   27.614  1 23.84 ? 490  MET A C   1 
ATOM   1034 O O   . MET A 1 241 ? 13.51   6.794   27.987  1 24.84 ? 490  MET A O   1 
ATOM   1035 C CB  . MET A 1 241 ? 12.707  9.786   26.993  1 23.77 ? 490  MET A CB  1 
ATOM   1036 C CG  . MET A 1 241 ? 12.056  11.068  27.473  1 26.26 ? 490  MET A CG  1 
ATOM   1037 S SD  . MET A 1 241 ? 10.988  11.838  26.222  1 31.78 ? 490  MET A SD  1 
ATOM   1038 C CE  . MET A 1 241 ? 9.588   10.807  26.378  1 34.47 ? 490  MET A CE  1 
ATOM   1039 N N   . GLY A 1 242 ? 15.2    7.74    26.834  1 23.5  ? 491  GLY A N   1 
ATOM   1040 C CA  . GLY A 1 242 ? 15.802  6.49    26.405  1 24.59 ? 491  GLY A CA  1 
ATOM   1041 C C   . GLY A 1 242 ? 16.358  5.717   27.582  1 25.36 ? 491  GLY A C   1 
ATOM   1042 O O   . GLY A 1 242 ? 16.158  4.503   27.675  1 25.53 ? 491  GLY A O   1 
ATOM   1043 N N   . MET A 1 243 ? 17.03   6.437   28.52   1 25.27 ? 492  MET A N   1 
ATOM   1044 C CA  . MET A 1 243 ? 17.596  5.874   29.743  1 25.91 ? 492  MET A CA  1 
ATOM   1045 C C   . MET A 1 243 ? 16.496  5.362   30.691  1 27.04 ? 492  MET A C   1 
ATOM   1046 O O   . MET A 1 243 ? 16.684  4.326   31.318  1 27.19 ? 492  MET A O   1 
ATOM   1047 C CB  . MET A 1 243 ? 18.517  6.878   30.432  1 26.23 ? 492  MET A CB  1 
ATOM   1048 C CG  . MET A 1 243 ? 19.801  7.122   29.667  1 27.74 ? 492  MET A CG  1 
ATOM   1049 S SD  . MET A 1 243 ? 20.863  8.323   30.501  1 29.36 ? 492  MET A SD  1 
ATOM   1050 C CE  . MET A 1 243 ? 21.512  7.277   31.853  1 25.58 ? 492  MET A CE  1 
ATOM   1051 N N   . ALA A 1 244 ? 15.328  6.026   30.736  1 27.28 ? 493  ALA A N   1 
ATOM   1052 C CA  . ALA A 1 244 ? 14.204  5.55    31.545  1 27.95 ? 493  ALA A CA  1 
ATOM   1053 C C   . ALA A 1 244 ? 13.705  4.217   30.972  1 29.23 ? 493  ALA A C   1 
ATOM   1054 O O   . ALA A 1 244 ? 13.517  3.267   31.736  1 30.07 ? 493  ALA A O   1 
ATOM   1055 C CB  . ALA A 1 244 ? 13.072  6.574   31.56   1 27.93 ? 493  ALA A CB  1 
ATOM   1056 N N   . VAL A 1 245 ? 13.553  4.12    29.633  1 28.74 ? 494  VAL A N   1 
ATOM   1057 C CA  . VAL A 1 245 ? 13.132  2.882   28.971  1 29.34 ? 494  VAL A CA  1 
ATOM   1058 C C   . VAL A 1 245 ? 14.141  1.77    29.263  1 30.06 ? 494  VAL A C   1 
ATOM   1059 O O   . VAL A 1 245 ? 13.763  0.692   29.718  1 30.33 ? 494  VAL A O   1 
ATOM   1060 C CB  . VAL A 1 245 ? 12.934  3.084   27.449  1 29.65 ? 494  VAL A CB  1 
ATOM   1061 C CG1 . VAL A 1 245 ? 12.705  1.74    26.731  1 30.6  ? 494  VAL A CG1 1 
ATOM   1062 C CG2 . VAL A 1 245 ? 11.788  4.047   27.182  1 29    ? 494  VAL A CG2 1 
ATOM   1063 N N   . PHE A 1 246 ? 15.431  2.083   29.082  1 29.71 ? 495  PHE A N   1 
ATOM   1064 C CA  . PHE A 1 246 ? 16.519  1.164   29.329  1 30.81 ? 495  PHE A CA  1 
ATOM   1065 C C   . PHE A 1 246 ? 16.49   0.575   30.749  1 32    ? 495  PHE A C   1 
ATOM   1066 O O   . PHE A 1 246 ? 16.669  -0.634  30.898  1 32.72 ? 495  PHE A O   1 
ATOM   1067 C CB  . PHE A 1 246 ? 17.834  1.874   29.062  1 30.78 ? 495  PHE A CB  1 
ATOM   1068 C CG  . PHE A 1 246 ? 19.04   0.996   28.907  1 31.65 ? 495  PHE A CG  1 
ATOM   1069 C CD1 . PHE A 1 246 ? 19.269  0.307   27.725  1 32.14 ? 495  PHE A CD1 1 
ATOM   1070 C CD2 . PHE A 1 246 ? 19.986  0.901   29.922  1 32.33 ? 495  PHE A CD2 1 
ATOM   1071 C CE1 . PHE A 1 246 ? 20.402  -0.489  27.576  1 32.59 ? 495  PHE A CE1 1 
ATOM   1072 C CE2 . PHE A 1 246 ? 21.133  0.137   29.749  1 32.41 ? 495  PHE A CE2 1 
ATOM   1073 C CZ  . PHE A 1 246 ? 21.335  -0.55   28.58   1 31.78 ? 495  PHE A CZ  1 
ATOM   1074 N N   . HIS A 1 247 ? 16.226  1.4     31.783  1 31.94 ? 496  HIS A N   1 
ATOM   1075 C CA  . HIS A 1 247 ? 16.201  0.904   33.156  1 32.65 ? 496  HIS A CA  1 
ATOM   1076 C C   . HIS A 1 247 ? 14.789  0.51    33.663  1 33.68 ? 496  HIS A C   1 
ATOM   1077 O O   . HIS A 1 247 ? 14.578  0.367   34.868  1 33.74 ? 496  HIS A O   1 
ATOM   1078 C CB  . HIS A 1 247 ? 16.902  1.896   34.102  1 33.27 ? 496  HIS A CB  1 
ATOM   1079 C CG  . HIS A 1 247 ? 18.35   2.073   33.753  1 34.98 ? 496  HIS A CG  1 
ATOM   1080 N ND1 . HIS A 1 247 ? 19.317  1.186   34.212  1 36.53 ? 496  HIS A ND1 1 
ATOM   1081 C CD2 . HIS A 1 247 ? 18.941  2.972   32.928  1 35.35 ? 496  HIS A CD2 1 
ATOM   1082 C CE1 . HIS A 1 247 ? 20.461  1.594   33.677  1 36.46 ? 496  HIS A CE1 1 
ATOM   1083 N NE2 . HIS A 1 247 ? 20.281  2.657   32.887  1 36.31 ? 496  HIS A NE2 1 
ATOM   1084 N N   . GLY A 1 248 ? 13.869  0.28    32.734  1 34.15 ? 497  GLY A N   1 
ATOM   1085 C CA  . GLY A 1 248 ? 12.515  -0.18   33.007  1 34.82 ? 497  GLY A CA  1 
ATOM   1086 C C   . GLY A 1 248 ? 11.61   0.748   33.784  1 35.52 ? 497  GLY A C   1 
ATOM   1087 O O   . GLY A 1 248 ? 10.784  0.275   34.573  1 35.58 ? 497  GLY A O   1 
ATOM   1088 N N   . HIS A 1 249 ? 11.736  2.072   33.563  1 35.67 ? 498  HIS A N   1 
ATOM   1089 C CA  . HIS A 1 249 ? 10.872  3.053   34.221  1 36.5  ? 498  HIS A CA  1 
ATOM   1090 C C   . HIS A 1 249 ? 9.687   3.363   33.31   1 37.1  ? 498  HIS A C   1 
ATOM   1091 O O   . HIS A 1 249 ? 9.876   3.661   32.135  1 37.35 ? 498  HIS A O   1 
ATOM   1092 C CB  . HIS A 1 249 ? 11.616  4.356   34.486  1 37.79 ? 498  HIS A CB  1 
ATOM   1093 C CG  . HIS A 1 249 ? 12.681  4.277   35.525  1 41.04 ? 498  HIS A CG  1 
ATOM   1094 N ND1 . HIS A 1 249 ? 12.666  5.111   36.632  1 43.71 ? 498  HIS A ND1 1 
ATOM   1095 C CD2 . HIS A 1 249 ? 13.81   3.529   35.553  1 42.32 ? 498  HIS A CD2 1 
ATOM   1096 C CE1 . HIS A 1 249 ? 13.758  4.81    37.321  1 44.59 ? 498  HIS A CE1 1 
ATOM   1097 N NE2 . HIS A 1 249 ? 14.474  3.858   36.712  1 44.14 ? 498  HIS A NE2 1 
ATOM   1098 N N   . TYR A 1 250 ? 8.477   3.333   33.852  1 37.71 ? 499  TYR A N   1 
ATOM   1099 C CA  . TYR A 1 250 ? 7.265   3.641   33.101  1 38.98 ? 499  TYR A CA  1 
ATOM   1100 C C   . TYR A 1 250 ? 6.736   4.947   33.635  1 40.02 ? 499  TYR A C   1 
ATOM   1101 O O   . TYR A 1 250 ? 6.115   4.963   34.693  1 40.27 ? 499  TYR A O   1 
ATOM   1102 C CB  . TYR A 1 250 ? 6.222   2.529   33.255  1 39.59 ? 499  TYR A CB  1 
ATOM   1103 C CG  . TYR A 1 250 ? 6.705   1.203   32.713  1 41.12 ? 499  TYR A CG  1 
ATOM   1104 C CD1 . TYR A 1 250 ? 7.414   0.318   33.514  1 42.55 ? 499  TYR A CD1 1 
ATOM   1105 C CD2 . TYR A 1 250 ? 6.476   0.845   31.396  1 42.38 ? 499  TYR A CD2 1 
ATOM   1106 C CE1 . TYR A 1 250 ? 7.901   -0.883  33.01   1 43.92 ? 499  TYR A CE1 1 
ATOM   1107 C CE2 . TYR A 1 250 ? 6.935   -0.365  30.886  1 43.99 ? 499  TYR A CE2 1 
ATOM   1108 C CZ  . TYR A 1 250 ? 7.647   -1.23   31.697  1 45.11 ? 499  TYR A CZ  1 
ATOM   1109 O OH  . TYR A 1 250 ? 8.121   -2.418  31.191  1 46.96 ? 499  TYR A OH  1 
ATOM   1110 N N   . ILE A 1 251 ? 7.019   6.049   32.926  1 40.64 ? 500  ILE A N   1 
ATOM   1111 C CA  . ILE A 1 251 ? 6.649   7.411   33.318  1 41.81 ? 500  ILE A CA  1 
ATOM   1112 C C   . ILE A 1 251 ? 5.473   7.977   32.501  1 42.32 ? 500  ILE A C   1 
ATOM   1113 O O   . ILE A 1 251 ? 5.504   7.989   31.258  1 41.33 ? 500  ILE A O   1 
ATOM   1114 C CB  . ILE A 1 251 ? 7.914   8.285   33.194  1 43.38 ? 500  ILE A CB  1 
ATOM   1115 C CG1 . ILE A 1 251 ? 8.992   7.78    34.162  1 44.96 ? 500  ILE A CG1 1 
ATOM   1116 C CG2 . ILE A 1 251 ? 7.623   9.787   33.402  1 43.8  ? 500  ILE A CG2 1 
ATOM   1117 C CD1 . ILE A 1 251 ? 10.321  8.085   33.738  1 46.46 ? 500  ILE A CD1 1 
ATOM   1118 N N   . ASP A 1 252 ? 4.425   8.43    33.213  1 43.47 ? 501  ASP A N   1 
ATOM   1119 C CA  . ASP A 1 252 ? 3.228   9.031   32.61   1 44.97 ? 501  ASP A CA  1 
ATOM   1120 C C   . ASP A 1 252 ? 3.553   10.51   32.42   1 44.91 ? 501  ASP A C   1 
ATOM   1121 O O   . ASP A 1 252 ? 3.239   11.335  33.283  1 46.34 ? 501  ASP A O   1 
ATOM   1122 C CB  . ASP A 1 252 ? 2.026   8.885   33.56   1 48.47 ? 501  ASP A CB  1 
ATOM   1123 C CG  . ASP A 1 252 ? 0.673   9.135   32.91   1 55.39 ? 501  ASP A CG  1 
ATOM   1124 O OD1 . ASP A 1 252 ? -0.225  9.683   33.6    1 57.07 ? 501  ASP A OD1 1 
ATOM   1125 O OD2 . ASP A 1 252 ? 0.497   8.749   31.722  1 57.27 ? 501  ASP A OD2 1 
ATOM   1126 N N   . GLY A 1 253 ? 4.272   10.817  31.351  1 43.02 ? 502  GLY A N   1 
ATOM   1127 C CA  . GLY A 1 253 ? 4.725   12.174  31.1    1 41.54 ? 502  GLY A CA  1 
ATOM   1128 C C   . GLY A 1 253 ? 3.616   13.153  30.805  1 40    ? 502  GLY A C   1 
ATOM   1129 O O   . GLY A 1 253 ? 3.786   14.349  31.044  1 40.97 ? 502  GLY A O   1 
ATOM   1130 N N   . GLY A 1 254 ? 2.501   12.669  30.264  1 37.46 ? 503  GLY A N   1 
ATOM   1131 C CA  . GLY A 1 254 ? 1.39    13.551  29.925  1 36.18 ? 503  GLY A CA  1 
ATOM   1132 C C   . GLY A 1 254 ? 1.297   13.907  28.45   1 34.39 ? 503  GLY A C   1 
ATOM   1133 O O   . GLY A 1 254 ? 0.401   14.648  28.047  1 33.88 ? 503  GLY A O   1 
ATOM   1134 N N   . PHE A 1 255 ? 2.214   13.383  27.624  1 32.89 ? 504  PHE A N   1 
ATOM   1135 C CA  . PHE A 1 255 ? 2.159   13.598  26.185  1 31.97 ? 504  PHE A CA  1 
ATOM   1136 C C   . PHE A 1 255 ? 0.965   12.843  25.594  1 32.34 ? 504  PHE A C   1 
ATOM   1137 O O   . PHE A 1 255 ? 0.412   11.952  26.25   1 33.26 ? 504  PHE A O   1 
ATOM   1138 C CB  . PHE A 1 255 ? 3.447   13.097  25.522  1 30.7  ? 504  PHE A CB  1 
ATOM   1139 C CG  . PHE A 1 255 ? 4.651   13.88   25.953  1 30.21 ? 504  PHE A CG  1 
ATOM   1140 C CD1 . PHE A 1 255 ? 4.813   15.198  25.564  1 30.55 ? 504  PHE A CD1 1 
ATOM   1141 C CD2 . PHE A 1 255 ? 5.606   13.312  26.768  1 30.42 ? 504  PHE A CD2 1 
ATOM   1142 C CE1 . PHE A 1 255 ? 5.927   15.919  25.952  1 31.09 ? 504  PHE A CE1 1 
ATOM   1143 C CE2 . PHE A 1 255 ? 6.712   14.038  27.176  1 31.41 ? 504  PHE A CE2 1 
ATOM   1144 C CZ  . PHE A 1 255 ? 6.884   15.33   26.746  1 31.19 ? 504  PHE A CZ  1 
ATOM   1145 N N   . THR A 1 256 ? 0.571   13.184  24.363  1 31.03 ? 505  THR A N   1 
ATOM   1146 C CA  . THR A 1 256 ? -0.524  12.478  23.693  1 31.03 ? 505  THR A CA  1 
ATOM   1147 C C   . THR A 1 256 ? -0.005  11.135  23.167  1 31    ? 505  THR A C   1 
ATOM   1148 O O   . THR A 1 256 ? 1.209   10.978  22.974  1 30.05 ? 505  THR A O   1 
ATOM   1149 C CB  . THR A 1 256 ? -1.03   13.306  22.5    1 31.69 ? 505  THR A CB  1 
ATOM   1150 O OG1 . THR A 1 256 ? -0.004  13.37   21.496  1 31.5  ? 505  THR A OG1 1 
ATOM   1151 C CG2 . THR A 1 256 ? -1.501  14.709  22.905  1 32.38 ? 505  THR A CG2 1 
ATOM   1152 N N   . LEU A 1 257 ? -0.917  10.192  22.857  1 31.3  ? 506  LEU A N   1 
ATOM   1153 C CA  . LEU A 1 257 ? -0.496  8.903   22.3    1 32.04 ? 506  LEU A CA  1 
ATOM   1154 C C   . LEU A 1 257 ? 0.242   9.077   20.966  1 32.14 ? 506  LEU A C   1 
ATOM   1155 O O   . LEU A 1 257 ? 1.336   8.526   20.831  1 32.71 ? 506  LEU A O   1 
ATOM   1156 C CB  . LEU A 1 257 ? -1.644  7.89    22.195  1 33.31 ? 506  LEU A CB  1 
ATOM   1157 C CG  . LEU A 1 257 ? -1.224  6.536   21.621  1 36.81 ? 506  LEU A CG  1 
ATOM   1158 C CD1 . LEU A 1 257 ? -0.211  5.833   22.548  1 37.78 ? 506  LEU A CD1 1 
ATOM   1159 C CD2 . LEU A 1 257 ? -2.432  5.649   21.359  1 38.25 ? 506  LEU A CD2 1 
ATOM   1160 N N   . PRO A 1 258 ? -0.265  9.881   19.995  1 30.9  ? 507  PRO A N   1 
ATOM   1161 C CA  . PRO A 1 258 ? 0.506   10.097  18.766  1 30.05 ? 507  PRO A CA  1 
ATOM   1162 C C   . PRO A 1 258 ? 1.904   10.693  18.984  1 29.05 ? 507  PRO A C   1 
ATOM   1163 O O   . PRO A 1 258 ? 2.769   10.413  18.175  1 29.06 ? 507  PRO A O   1 
ATOM   1164 C CB  . PRO A 1 258 ? -0.405  10.994  17.918  1 30.74 ? 507  PRO A CB  1 
ATOM   1165 C CG  . PRO A 1 258 ? -1.773  10.8    18.49   1 31.57 ? 507  PRO A CG  1 
ATOM   1166 C CD  . PRO A 1 258 ? -1.548  10.613  19.951  1 30.18 ? 507  PRO A CD  1 
ATOM   1167 N N   . PHE A 1 259 ? 2.148   11.486  20.052  1 28.7  ? 508  PHE A N   1 
ATOM   1168 C CA  . PHE A 1 259 ? 3.501   11.995  20.362  1 29.05 ? 508  PHE A CA  1 
ATOM   1169 C C   . PHE A 1 259 ? 4.406   10.792  20.662  1 28.37 ? 508  PHE A C   1 
ATOM   1170 O O   . PHE A 1 259 ? 5.491   10.667  20.081  1 27.27 ? 508  PHE A O   1 
ATOM   1171 C CB  . PHE A 1 259 ? 3.487   12.957  21.58   1 29.47 ? 508  PHE A CB  1 
ATOM   1172 C CG  . PHE A 1 259 ? 4.847   13.457  22.049  1 31    ? 508  PHE A CG  1 
ATOM   1173 C CD1 . PHE A 1 259 ? 5.676   12.655  22.818  1 32.27 ? 508  PHE A CD1 1 
ATOM   1174 C CD2 . PHE A 1 259 ? 5.267   14.751  21.765  1 32.34 ? 508  PHE A CD2 1 
ATOM   1175 C CE1 . PHE A 1 259 ? 6.933   13.108  23.219  1 33.43 ? 508  PHE A CE1 1 
ATOM   1176 C CE2 . PHE A 1 259 ? 6.506   15.211  22.198  1 33.15 ? 508  PHE A CE2 1 
ATOM   1177 C CZ  . PHE A 1 259 ? 7.321   14.396  22.935  1 33.17 ? 508  PHE A CZ  1 
ATOM   1178 N N   . TYR A 1 260 ? 3.937   9.899   21.56   1 28.63 ? 509  TYR A N   1 
ATOM   1179 C CA  . TYR A 1 260 ? 4.672   8.695   21.93   1 30.11 ? 509  TYR A CA  1 
ATOM   1180 C C   . TYR A 1 260 ? 4.91    7.78    20.752  1 31.46 ? 509  TYR A C   1 
ATOM   1181 O O   . TYR A 1 260 ? 6.001   7.236   20.63   1 31.14 ? 509  TYR A O   1 
ATOM   1182 C CB  . TYR A 1 260 ? 3.938   7.928   23.03   1 30.08 ? 509  TYR A CB  1 
ATOM   1183 C CG  . TYR A 1 260 ? 4.003   8.631   24.357  1 30.2  ? 509  TYR A CG  1 
ATOM   1184 C CD1 . TYR A 1 260 ? 5.221   9.026   24.898  1 30.9  ? 509  TYR A CD1 1 
ATOM   1185 C CD2 . TYR A 1 260 ? 2.851   8.917   25.066  1 30.55 ? 509  TYR A CD2 1 
ATOM   1186 C CE1 . TYR A 1 260 ? 5.287   9.673   26.12   1 31.75 ? 509  TYR A CE1 1 
ATOM   1187 C CE2 . TYR A 1 260 ? 2.902   9.578   26.28   1 31.91 ? 509  TYR A CE2 1 
ATOM   1188 C CZ  . TYR A 1 260 ? 4.125   9.928   26.822  1 33.01 ? 509  TYR A CZ  1 
ATOM   1189 O OH  . TYR A 1 260 ? 4.167   10.533  28.057  1 34.61 ? 509  TYR A OH  1 
ATOM   1190 N N   . LYS A 1 261 ? 3.911   7.62    19.871  1 32.24 ? 510  LYS A N   1 
ATOM   1191 C CA  . LYS A 1 261 ? 4.075   6.782   18.686  1 33.99 ? 510  LYS A CA  1 
ATOM   1192 C C   . LYS A 1 261 ? 5.115   7.321   17.755  1 35.11 ? 510  LYS A C   1 
ATOM   1193 O O   . LYS A 1 261 ? 5.883   6.534   17.216  1 35.82 ? 510  LYS A O   1 
ATOM   1194 C CB  . LYS A 1 261 ? 2.759   6.608   17.925  1 36.38 ? 510  LYS A CB  1 
ATOM   1195 C CG  . LYS A 1 261 ? 1.742   5.799   18.701  1 41.97 ? 510  LYS A CG  1 
ATOM   1196 C CD  . LYS A 1 261 ? 0.554   5.422   17.835  1 48.5  ? 510  LYS A CD  1 
ATOM   1197 C CE  . LYS A 1 261 ? -0.076  6.574   17.081  1 53.14 ? 510  LYS A CE  1 
ATOM   1198 N NZ  . LYS A 1 261 ? -0.239  6.24    15.633  1 56.25 ? 510  LYS A NZ  1 
ATOM   1199 N N   . GLN A 1 262 ? 5.183   8.648   17.569  1 35.23 ? 511  GLN A N   1 
ATOM   1200 C CA  . GLN A 1 262 ? 6.207   9.225   16.706  1 36.5  ? 511  GLN A CA  1 
ATOM   1201 C C   . GLN A 1 262 ? 7.597   8.979   17.289  1 36.67 ? 511  GLN A C   1 
ATOM   1202 O O   . GLN A 1 262 ? 8.535   8.678   16.545  1 37.19 ? 511  GLN A O   1 
ATOM   1203 C CB  . GLN A 1 262 ? 5.987   10.725  16.517  1 39.77 ? 511  GLN A CB  1 
ATOM   1204 C CG  . GLN A 1 262 ? 5.323   11.069  15.21   1 46.72 ? 511  GLN A CG  1 
ATOM   1205 C CD  . GLN A 1 262 ? 6.237   11.063  14.017  1 51.67 ? 511  GLN A CD  1 
ATOM   1206 O OE1 . GLN A 1 262 ? 6.235   10.124  13.207  1 54.14 ? 511  GLN A OE1 1 
ATOM   1207 N NE2 . GLN A 1 262 ? 7.021   12.114  13.88   1 51.56 ? 511  GLN A NE2 1 
ATOM   1208 N N   . LEU A 1 263 ? 7.73    9.122   18.615  1 35.55 ? 512  LEU A N   1 
ATOM   1209 C CA  . LEU A 1 263 ? 8.991   8.884   19.305  1 35.08 ? 512  LEU A CA  1 
ATOM   1210 C C   . LEU A 1 263 ? 9.415   7.415   19.182  1 36.21 ? 512  LEU A C   1 
ATOM   1211 O O   . LEU A 1 263 ? 10.586  7.127   18.964  1 36.45 ? 512  LEU A O   1 
ATOM   1212 C CB  . LEU A 1 263 ? 8.852   9.284   20.776  1 34.13 ? 512  LEU A CB  1 
ATOM   1213 C CG  . LEU A 1 263 ? 10.168  9.258   21.574  1 35.4  ? 512  LEU A CG  1 
ATOM   1214 C CD1 . LEU A 1 263 ? 11.186  10.287  21.011  1 35.08 ? 512  LEU A CD1 1 
ATOM   1215 C CD2 . LEU A 1 263 ? 9.902   9.464   23.054  1 35.71 ? 512  LEU A CD2 1 
ATOM   1216 N N   . LEU A 1 264 ? 8.457   6.483   19.26   1 37.12 ? 513  LEU A N   1 
ATOM   1217 C CA  . LEU A 1 264 ? 8.76    5.055   19.176  1 38.48 ? 513  LEU A CA  1 
ATOM   1218 C C   . LEU A 1 264 ? 8.715   4.485   17.75   1 40.53 ? 513  LEU A C   1 
ATOM   1219 O O   . LEU A 1 264 ? 8.545   3.272   17.576  1 41.03 ? 513  LEU A O   1 
ATOM   1220 C CB  . LEU A 1 264 ? 7.862   4.251   20.127  1 38.87 ? 513  LEU A CB  1 
ATOM   1221 C CG  . LEU A 1 264 ? 7.823   4.768   21.58   1 41.02 ? 513  LEU A CG  1 
ATOM   1222 C CD1 . LEU A 1 264 ? 6.851   3.992   22.429  1 41.51 ? 513  LEU A CD1 1 
ATOM   1223 C CD2 . LEU A 1 264 ? 9.201   4.787   22.208  1 42.16 ? 513  LEU A CD2 1 
ATOM   1224 N N   . GLY A 1 265 ? 8.907   5.355   16.759  1 41.27 ? 514  GLY A N   1 
ATOM   1225 C CA  . GLY A 1 265 ? 8.969   5.019   15.345  1 42.89 ? 514  GLY A CA  1 
ATOM   1226 C C   . GLY A 1 265 ? 7.731   4.481   14.648  1 43.75 ? 514  GLY A C   1 
ATOM   1227 O O   . GLY A 1 265 ? 7.845   3.695   13.702  1 44.55 ? 514  GLY A O   1 
ATOM   1228 N N   . LYS A 1 266 ? 6.558   4.892   15.094  1 43.04 ? 515  LYS A N   1 
ATOM   1229 C CA  . LYS A 1 266 ? 5.318   4.488   14.458  1 43.21 ? 515  LYS A CA  1 
ATOM   1230 C C   . LYS A 1 266 ? 4.819   5.634   13.598  1 42.86 ? 515  LYS A C   1 
ATOM   1231 O O   . LYS A 1 266 ? 4.957   6.811   13.955  1 41.9  ? 515  LYS A O   1 
ATOM   1232 C CB  . LYS A 1 266 ? 4.259   4.043   15.483  1 45.32 ? 515  LYS A CB  1 
ATOM   1233 C CG  . LYS A 1 266 ? 4.626   2.757   16.214  1 51.36 ? 515  LYS A CG  1 
ATOM   1234 C CD  . LYS A 1 266 ? 3.712   1.579   15.853  1 57.77 ? 515  LYS A CD  1 
ATOM   1235 C CE  . LYS A 1 266 ? 3.861   1.084   14.433  1 62.45 ? 515  LYS A CE  1 
ATOM   1236 N NZ  . LYS A 1 266 ? 2.794   1.601   13.525  1 65.04 ? 515  LYS A NZ  1 
ATOM   1237 N N   . SER A 1 267 ? 4.271   5.287   12.442  1 43.52 ? 516  SER A N   1 
ATOM   1238 C CA  . SER A 1 267 ? 3.738   6.292   11.521  1 44.08 ? 516  SER A CA  1 
ATOM   1239 C C   . SER A 1 267 ? 2.495   6.966   12.119  1 42.88 ? 516  SER A C   1 
ATOM   1240 O O   . SER A 1 267 ? 1.72    6.324   12.823  1 42.88 ? 516  SER A O   1 
ATOM   1241 C CB  . SER A 1 267 ? 3.389   5.645   10.182  1 46.86 ? 516  SER A CB  1 
ATOM   1242 O OG  . SER A 1 267 ? 4.524   5.022   9.595   1 50.83 ? 516  SER A OG  1 
ATOM   1243 N N   . ILE A 1 268 ? 2.354   8.277   11.902  1 42.12 ? 517  ILE A N   1 
ATOM   1244 C CA  . ILE A 1 268 ? 1.172   9.02    12.329  1 41.48 ? 517  ILE A CA  1 
ATOM   1245 C C   . ILE A 1 268 ? 0.043   8.684   11.358  1 39.89 ? 517  ILE A C   1 
ATOM   1246 O O   . ILE A 1 268 ? 0.296   8.529   10.175  1 40.11 ? 517  ILE A O   1 
ATOM   1247 C CB  . ILE A 1 268 ? 1.479   10.533  12.386  1 42.65 ? 517  ILE A CB  1 
ATOM   1248 C CG1 . ILE A 1 268 ? 2.433   10.793  13.535  1 44.88 ? 517  ILE A CG1 1 
ATOM   1249 C CG2 . ILE A 1 268 ? 0.209   11.388  12.565  1 42.92 ? 517  ILE A CG2 1 
ATOM   1250 C CD1 . ILE A 1 268 ? 1.869   10.33   14.949  1 46.69 ? 517  ILE A CD1 1 
ATOM   1251 N N   . THR A 1 269 ? -1.176  8.484   11.862  1 38.83 ? 518  THR A N   1 
ATOM   1252 C CA  . THR A 1 269 ? -2.316  8.135   11.009  1 37.72 ? 518  THR A CA  1 
ATOM   1253 C C   . THR A 1 269 ? -3.31   9.295   10.924  1 35.35 ? 518  THR A C   1 
ATOM   1254 O O   . THR A 1 269 ? -3.328  10.157  11.806  1 34.46 ? 518  THR A O   1 
ATOM   1255 C CB  . THR A 1 269 ? -3.048  6.89    11.579  1 40.01 ? 518  THR A CB  1 
ATOM   1256 O OG1 . THR A 1 269 ? -3.659  7.22    12.831  1 41.15 ? 518  THR A OG1 1 
ATOM   1257 C CG2 . THR A 1 269 ? -2.131  5.685   11.742  1 41.14 ? 518  THR A CG2 1 
ATOM   1258 N N   . LEU A 1 270 ? -4.195  9.268   9.914   1 34.3  ? 519  LEU A N   1 
ATOM   1259 C CA  . LEU A 1 270 ? -5.28   10.233  9.789   1 34.25 ? 519  LEU A CA  1 
ATOM   1260 C C   . LEU A 1 270 ? -6.212  10.132  11.026  1 35.76 ? 519  LEU A C   1 
ATOM   1261 O O   . LEU A 1 270 ? -6.695  11.151  11.52   1 34.92 ? 519  LEU A O   1 
ATOM   1262 C CB  . LEU A 1 270 ? -6.068  9.974   8.487   1 33.26 ? 519  LEU A CB  1 
ATOM   1263 C CG  . LEU A 1 270 ? -7.172  10.987  8.175   1 33.03 ? 519  LEU A CG  1 
ATOM   1264 C CD1 . LEU A 1 270 ? -6.634  12.398  8.129   1 32.63 ? 519  LEU A CD1 1 
ATOM   1265 C CD2 . LEU A 1 270 ? -7.89   10.631  6.898   1 33.19 ? 519  LEU A CD2 1 
ATOM   1266 N N   . ASP A 1 271 ? -6.389  8.911   11.577  1 38.06 ? 520  ASP A N   1 
ATOM   1267 C CA  . ASP A 1 271 ? -7.166  8.663   12.796  1 40.71 ? 520  ASP A CA  1 
ATOM   1268 C C   . ASP A 1 271 ? -6.658  9.525   13.95   1 40.89 ? 520  ASP A C   1 
ATOM   1269 O O   . ASP A 1 271 ? -7.466  10.081  14.681  1 41.04 ? 520  ASP A O   1 
ATOM   1270 C CB  . ASP A 1 271 ? -7.057  7.184   13.2    1 45.52 ? 520  ASP A CB  1 
ATOM   1271 C CG  . ASP A 1 271 ? -8.192  6.316   12.705  1 55.36 ? 520  ASP A CG  1 
ATOM   1272 O OD1 . ASP A 1 271 ? -8.254  6.059   11.479  1 57.02 ? 520  ASP A OD1 1 
ATOM   1273 O OD2 . ASP A 1 271 ? -9.016  5.879   13.548  1 59.92 ? 520  ASP A OD2 1 
ATOM   1274 N N   . ASP A 1 272 ? -5.32   9.696   14.057  1 41    ? 521  ASP A N   1 
ATOM   1275 C CA  . ASP A 1 272 ? -4.685  10.526  15.078  1 42.05 ? 521  ASP A CA  1 
ATOM   1276 C C   . ASP A 1 272 ? -5.001  12.011  14.949  1 43.17 ? 521  ASP A C   1 
ATOM   1277 O O   . ASP A 1 272 ? -4.845  12.752  15.927  1 43.56 ? 521  ASP A O   1 
ATOM   1278 C CB  . ASP A 1 272 ? -3.161  10.338  15.062  1 43.64 ? 521  ASP A CB  1 
ATOM   1279 C CG  . ASP A 1 272 ? -2.715  8.958   15.478  1 47.98 ? 521  ASP A CG  1 
ATOM   1280 O OD1 . ASP A 1 272 ? -3.358  8.374   16.373  1 48.97 ? 521  ASP A OD1 1 
ATOM   1281 O OD2 . ASP A 1 272 ? -1.735  8.454   14.893  1 50.27 ? 521  ASP A OD2 1 
ATOM   1282 N N   . MET A 1 273 ? -5.409  12.466  13.753  1 43.32 ? 522  MET A N   1 
ATOM   1283 C CA  . MET A 1 273 ? -5.716  13.88   13.559  1 44.13 ? 522  MET A CA  1 
ATOM   1284 C C   . MET A 1 273 ? -7.044  14.322  14.143  1 44.41 ? 522  MET A C   1 
ATOM   1285 O O   . MET A 1 273 ? -7.26   15.525  14.285  1 44.04 ? 522  MET A O   1 
ATOM   1286 C CB  . MET A 1 273 ? -5.619  14.296  12.094  1 45.13 ? 522  MET A CB  1 
ATOM   1287 C CG  . MET A 1 273 ? -5.049  15.687  11.936  1 48.86 ? 522  MET A CG  1 
ATOM   1288 S SD  . MET A 1 273 ? -3.285  15.776  11.468  1 55.69 ? 522  MET A SD  1 
ATOM   1289 C CE  . MET A 1 273 ? -2.492  14.478  12.54   1 47.95 ? 522  MET A CE  1 
ATOM   1290 N N   . GLU A 1 274 ? -7.919  13.371  14.509  1 44.82 ? 523  GLU A N   1 
ATOM   1291 C CA  . GLU A 1 274 ? -9.236  13.662  15.071  1 46.24 ? 523  GLU A CA  1 
ATOM   1292 C C   . GLU A 1 274 ? -9.191  14.691  16.218  1 46.8  ? 523  GLU A C   1 
ATOM   1293 O O   . GLU A 1 274 ? -9.853  15.725  16.135  1 47.02 ? 523  GLU A O   1 
ATOM   1294 C CB  . GLU A 1 274 ? -9.902  12.352  15.521  1 49.3  ? 523  GLU A CB  1 
ATOM   1295 C CG  . GLU A 1 274 ? -11.417 12.415  15.639  1 55.82 ? 523  GLU A CG  1 
ATOM   1296 C CD  . GLU A 1 274 ? -12.123 11.085  15.436  1 63.9  ? 523  GLU A CD  1 
ATOM   1297 O OE1 . GLU A 1 274 ? -11.43  10.05   15.285  1 64.71 ? 523  GLU A OE1 1 
ATOM   1298 O OE2 . GLU A 1 274 ? -13.376 11.081  15.414  1 67.68 ? 523  GLU A OE2 1 
ATOM   1299 N N   . LEU A 1 275 ? -8.331  14.462  17.229  1 46.74 ? 524  LEU A N   1 
ATOM   1300 C CA  . LEU A 1 275 ? -8.251  15.371  18.36   1 46.63 ? 524  LEU A CA  1 
ATOM   1301 C C   . LEU A 1 275 ? -7.297  16.539  18.138  1 45.82 ? 524  LEU A C   1 
ATOM   1302 O O   . LEU A 1 275 ? -7.558  17.614  18.662  1 46.53 ? 524  LEU A O   1 
ATOM   1303 C CB  . LEU A 1 275 ? -7.94   14.605  19.641  1 47.73 ? 524  LEU A CB  1 
ATOM   1304 C CG  . LEU A 1 275 ? -9      13.56   20.058  1 49.86 ? 524  LEU A CG  1 
ATOM   1305 C CD1 . LEU A 1 275 ? -8.633  12.914  21.385  1 50.4  ? 524  LEU A CD1 1 
ATOM   1306 C CD2 . LEU A 1 275 ? -10.402 14.177  20.169  1 50.51 ? 524  LEU A CD2 1 
ATOM   1307 N N   . VAL A 1 276 ? -6.265  16.381  17.298  1 44.6  ? 525  VAL A N   1 
ATOM   1308 C CA  . VAL A 1 276 ? -5.305  17.447  16.97   1 43.96 ? 525  VAL A CA  1 
ATOM   1309 C C   . VAL A 1 276 ? -5.948  18.614  16.182  1 43.04 ? 525  VAL A C   1 
ATOM   1310 O O   . VAL A 1 276 ? -5.683  19.784  16.468  1 43.04 ? 525  VAL A O   1 
ATOM   1311 C CB  . VAL A 1 276 ? -4.104  16.836  16.201  1 45.36 ? 525  VAL A CB  1 
ATOM   1312 C CG1 . VAL A 1 276 ? -3.249  17.905  15.524  1 46.46 ? 525  VAL A CG1 1 
ATOM   1313 C CG2 . VAL A 1 276 ? -3.254  15.967  17.121  1 45.98 ? 525  VAL A CG2 1 
ATOM   1314 N N   . ASP A 1 277 ? -6.791  18.294  15.187  1 41.78 ? 526  ASP A N   1 
ATOM   1315 C CA  . ASP A 1 277 ? -7.423  19.309  14.345  1 41.71 ? 526  ASP A CA  1 
ATOM   1316 C C   . ASP A 1 277 ? -8.709  18.682  13.763  1 41.92 ? 526  ASP A C   1 
ATOM   1317 O O   . ASP A 1 277 ? -8.673  18.058  12.693  1 41.41 ? 526  ASP A O   1 
ATOM   1318 C CB  . ASP A 1 277 ? -6.439  19.694  13.229  1 42.81 ? 526  ASP A CB  1 
ATOM   1319 C CG  . ASP A 1 277 ? -6.747  20.994  12.533  1 44.46 ? 526  ASP A CG  1 
ATOM   1320 O OD1 . ASP A 1 277 ? -7.945  21.351  12.446  1 44.14 ? 526  ASP A OD1 1 
ATOM   1321 O OD2 . ASP A 1 277 ? -5.793  21.637  12.031  1 45.69 ? 526  ASP A OD2 1 
ATOM   1322 N N   . PRO A 1 278 ? -9.819  18.755  14.524  1 41.8  ? 527  PRO A N   1 
ATOM   1323 C CA  . PRO A 1 278 ? -11.051 18.07   14.096  1 41.52 ? 527  PRO A CA  1 
ATOM   1324 C C   . PRO A 1 278 ? -11.621 18.479  12.744  1 40.49 ? 527  PRO A C   1 
ATOM   1325 O O   . PRO A 1 278 ? -12.169 17.625  12.055  1 40.71 ? 527  PRO A O   1 
ATOM   1326 C CB  . PRO A 1 278 ? -12.055 18.355  15.229  1 42.66 ? 527  PRO A CB  1 
ATOM   1327 C CG  . PRO A 1 278 ? -11.265 18.9    16.367  1 42.83 ? 527  PRO A CG  1 
ATOM   1328 C CD  . PRO A 1 278 ? -9.974  19.427  15.836  1 41.46 ? 527  PRO A CD  1 
ATOM   1329 N N   . ASP A 1 279 ? -11.515 19.762  12.369  1 39.21 ? 528  ASP A N   1 
ATOM   1330 C CA  . ASP A 1 279 ? -12.046 20.223  11.081  1 38.33 ? 528  ASP A CA  1 
ATOM   1331 C C   . ASP A 1 279 ? -11.192 19.7    9.929   1 35.78 ? 528  ASP A C   1 
ATOM   1332 O O   . ASP A 1 279 ? -11.726 19.273  8.905   1 35.58 ? 528  ASP A O   1 
ATOM   1333 C CB  . ASP A 1 279 ? -12.117 21.761  11.025  1 40.54 ? 528  ASP A CB  1 
ATOM   1334 C CG  . ASP A 1 279 ? -13.184 22.368  11.913  1 46.32 ? 528  ASP A CG  1 
ATOM   1335 O OD1 . ASP A 1 279 ? -14.111 21.624  12.326  1 47.7  ? 528  ASP A OD1 1 
ATOM   1336 O OD2 . ASP A 1 279 ? -13.101 23.585  12.189  1 48.12 ? 528  ASP A OD2 1 
ATOM   1337 N N   . LEU A 1 280 ? -9.867  19.72   10.114  1 33.43 ? 529  LEU A N   1 
ATOM   1338 C CA  . LEU A 1 280 ? -8.932  19.218  9.117   1 31.79 ? 529  LEU A CA  1 
ATOM   1339 C C   . LEU A 1 280 ? -9.12   17.724  8.948   1 30.09 ? 529  LEU A C   1 
ATOM   1340 O O   . LEU A 1 280 ? -9.167  17.251  7.83    1 30.57 ? 529  LEU A O   1 
ATOM   1341 C CB  . LEU A 1 280 ? -7.491  19.553  9.514   1 31.81 ? 529  LEU A CB  1 
ATOM   1342 C CG  . LEU A 1 280 ? -6.417  19.052  8.577   1 32.73 ? 529  LEU A CG  1 
ATOM   1343 C CD1 . LEU A 1 280 ? -6.535  19.717  7.222   1 32.46 ? 529  LEU A CD1 1 
ATOM   1344 C CD2 . LEU A 1 280 ? -5.037  19.256  9.187   1 33.39 ? 529  LEU A CD2 1 
ATOM   1345 N N   . HIS A 1 281 ? -9.305  16.991  10.036  1 29.29 ? 530  HIS A N   1 
ATOM   1346 C CA  . HIS A 1 281 ? -9.538  15.559  10.015  1 28.89 ? 530  HIS A CA  1 
ATOM   1347 C C   . HIS A 1 281 ? -10.758 15.201  9.131   1 29.21 ? 530  HIS A C   1 
ATOM   1348 O O   . HIS A 1 281 ? -10.649 14.328  8.273   1 29.09 ? 530  HIS A O   1 
ATOM   1349 C CB  . HIS A 1 281 ? -9.722  15.029  11.451  1 28.54 ? 530  HIS A CB  1 
ATOM   1350 C CG  . HIS A 1 281 ? -10.247 13.628  11.508  1 30.09 ? 530  HIS A CG  1 
ATOM   1351 N ND1 . HIS A 1 281 ? -9.442  12.53   11.192  1 32.38 ? 530  HIS A ND1 1 
ATOM   1352 C CD2 . HIS A 1 281 ? -11.496 13.185  11.771  1 30.58 ? 530  HIS A CD2 1 
ATOM   1353 C CE1 . HIS A 1 281 ? -10.222 11.467  11.318  1 31.92 ? 530  HIS A CE1 1 
ATOM   1354 N NE2 . HIS A 1 281 ? -11.469 11.812  11.637  1 31.63 ? 530  HIS A NE2 1 
ATOM   1355 N N   . ASN A 1 282 ? -11.902 15.886  9.348   1 28.66 ? 531  ASN A N   1 
ATOM   1356 C CA  . ASN A 1 282 ? -13.116 15.663  8.552   1 28.59 ? 531  ASN A CA  1 
ATOM   1357 C C   . ASN A 1 282 ? -12.893 15.956  7.092   1 26.73 ? 531  ASN A C   1 
ATOM   1358 O O   . ASN A 1 282 ? -13.394 15.211  6.247   1 26.93 ? 531  ASN A O   1 
ATOM   1359 C CB  . ASN A 1 282 ? -14.296 16.515  9.081   1 30.33 ? 531  ASN A CB  1 
ATOM   1360 C CG  . ASN A 1 282 ? -15.012 15.904  10.257  1 36.34 ? 531  ASN A CG  1 
ATOM   1361 O OD1 . ASN A 1 282 ? -15.607 16.615  11.076  1 39.3  ? 531  ASN A OD1 1 
ATOM   1362 N ND2 . ASN A 1 282 ? -14.974 14.579  10.383  1 37.34 ? 531  ASN A ND2 1 
ATOM   1363 N N   . SER A 1 283 ? -12.161 17.038  6.787   1 26.03 ? 532  SER A N   1 
ATOM   1364 C CA  . SER A 1 283 ? -11.847 17.429  5.404   1 26.41 ? 532  SER A CA  1 
ATOM   1365 C C   . SER A 1 283 ? -10.992 16.394  4.697   1 25.3  ? 532  SER A C   1 
ATOM   1366 O O   . SER A 1 283 ? -11.249 16.081  3.552   1 24.59 ? 532  SER A O   1 
ATOM   1367 C CB  . SER A 1 283 ? -11.112 18.76   5.368   1 28.64 ? 532  SER A CB  1 
ATOM   1368 O OG  . SER A 1 283 ? -12.036 19.773  5.695   1 34.26 ? 532  SER A OG  1 
ATOM   1369 N N   . LEU A 1 284 ? -9.966  15.874  5.38    1 24.96 ? 533  LEU A N   1 
ATOM   1370 C CA  . LEU A 1 284 ? -9.075  14.875  4.813   1 23.99 ? 533  LEU A CA  1 
ATOM   1371 C C   . LEU A 1 284 ? -9.766  13.535  4.654   1 23.33 ? 533  LEU A C   1 
ATOM   1372 O O   . LEU A 1 284 ? -9.494  12.817  3.693   1 23.13 ? 533  LEU A O   1 
ATOM   1373 C CB  . LEU A 1 284 ? -7.82   14.738  5.697   1 23.82 ? 533  LEU A CB  1 
ATOM   1374 C CG  . LEU A 1 284 ? -6.978  16      5.853   1 25.75 ? 533  LEU A CG  1 
ATOM   1375 C CD1 . LEU A 1 284 ? -5.834  15.781  6.889   1 26.7  ? 533  LEU A CD1 1 
ATOM   1376 C CD2 . LEU A 1 284 ? -6.41   16.444  4.538   1 25.54 ? 533  LEU A CD2 1 
ATOM   1377 N N   . VAL A 1 285 ? -10.636 13.163  5.605   1 23.71 ? 534  VAL A N   1 
ATOM   1378 C CA  . VAL A 1 285 ? -11.417 11.918  5.514   1 25.27 ? 534  VAL A CA  1 
ATOM   1379 C C   . VAL A 1 285 ? -12.358 12.043  4.268   1 25.08 ? 534  VAL A C   1 
ATOM   1380 O O   . VAL A 1 285 ? -12.451 11.131  3.431   1 25.08 ? 534  VAL A O   1 
ATOM   1381 C CB  . VAL A 1 285 ? -12.229 11.668  6.838   1 27.29 ? 534  VAL A CB  1 
ATOM   1382 C CG1 . VAL A 1 285 ? -13.355 10.654  6.617   1 28.1  ? 534  VAL A CG1 1 
ATOM   1383 C CG2 . VAL A 1 285 ? -11.314 11.207  7.965   1 27.5  ? 534  VAL A CG2 1 
ATOM   1384 N N   . TRP A 1 286 ? -12.964 13.222  4.109   1 24.79 ? 535  TRP A N   1 
ATOM   1385 C CA  . TRP A 1 286 ? -13.812 13.526  2.962   1 25.06 ? 535  TRP A CA  1 
ATOM   1386 C C   . TRP A 1 286 ? -13.051 13.369  1.638   1 24.87 ? 535  TRP A C   1 
ATOM   1387 O O   . TRP A 1 286 ? -13.582 12.762  0.71    1 24.87 ? 535  TRP A O   1 
ATOM   1388 C CB  . TRP A 1 286 ? -14.407 14.924  3.102   1 25.6  ? 535  TRP A CB  1 
ATOM   1389 C CG  . TRP A 1 286 ? -15.35  15.252  1.998   1 27.96 ? 535  TRP A CG  1 
ATOM   1390 C CD1 . TRP A 1 286 ? -16.644 14.839  1.86    1 28.79 ? 535  TRP A CD1 1 
ATOM   1391 C CD2 . TRP A 1 286 ? -15.044 16.026  0.838   1 29.91 ? 535  TRP A CD2 1 
ATOM   1392 N NE1 . TRP A 1 286 ? -17.175 15.346  0.697   1 30.04 ? 535  TRP A NE1 1 
ATOM   1393 C CE2 . TRP A 1 286 ? -16.209 16.067  0.042   1 30.8  ? 535  TRP A CE2 1 
ATOM   1394 C CE3 . TRP A 1 286 ? -13.889 16.694  0.391   1 31.59 ? 535  TRP A CE3 1 
ATOM   1395 C CZ2 . TRP A 1 286 ? -16.253 16.745  -1.174  1 32.45 ? 535  TRP A CZ2 1 
ATOM   1396 C CZ3 . TRP A 1 286 ? -13.918 17.326  -0.837  1 33.13 ? 535  TRP A CZ3 1 
ATOM   1397 C CH2 . TRP A 1 286 ? -15.087 17.335  -1.615  1 33.46 ? 535  TRP A CH2 1 
ATOM   1398 N N   . ILE A 1 287 ? -11.789 13.858  1.566   1 24.43 ? 536  ILE A N   1 
ATOM   1399 C CA  . ILE A 1 287 ? -10.96  13.73   0.356   1 25.03 ? 536  ILE A CA  1 
ATOM   1400 C C   . ILE A 1 287 ? -10.759 12.246  -0.006  1 25.23 ? 536  ILE A C   1 
ATOM   1401 O O   . ILE A 1 287 ? -10.997 11.837  -1.129  1 25.56 ? 536  ILE A O   1 
ATOM   1402 C CB  . ILE A 1 287 ? -9.587  14.465  0.532   1 25.06 ? 536  ILE A CB  1 
ATOM   1403 C CG1 . ILE A 1 287 ? -9.801  15.977  0.635   1 26.16 ? 536  ILE A CG1 1 
ATOM   1404 C CG2 . ILE A 1 287 ? -8.599  14.093  -0.592  1 25.25 ? 536  ILE A CG2 1 
ATOM   1405 C CD1 . ILE A 1 287 ? -8.582  16.808  0.873   1 26.48 ? 536  ILE A CD1 1 
ATOM   1406 N N   . LEU A 1 288 ? -10.37  11.445  0.973   1 25.13 ? 537  LEU A N   1 
ATOM   1407 C CA  . LEU A 1 288 ? -10.11  10.035  0.773   1 26.08 ? 537  LEU A CA  1 
ATOM   1408 C C   . LEU A 1 288 ? -11.336 9.216   0.383   1 26.86 ? 537  LEU A C   1 
ATOM   1409 O O   . LEU A 1 288 ? -11.21  8.241   -0.356  1 26.92 ? 537  LEU A O   1 
ATOM   1410 C CB  . LEU A 1 288 ? -9.524  9.47    2.075   1 26.42 ? 537  LEU A CB  1 
ATOM   1411 C CG  . LEU A 1 288 ? -8.005  9.159   2.176   1 29.58 ? 537  LEU A CG  1 
ATOM   1412 C CD1 . LEU A 1 288 ? -7.116  9.937   1.186   1 29.54 ? 537  LEU A CD1 1 
ATOM   1413 C CD2 . LEU A 1 288 ? -7.54   9.126   3.614   1 30.25 ? 537  LEU A CD2 1 
ATOM   1414 N N   . GLU A 1 289 ? -12.494 9.551   0.945   1 26.85 ? 538  GLU A N   1 
ATOM   1415 C CA  . GLU A 1 289 ? -13.701 8.752   0.792   1 27.71 ? 538  GLU A CA  1 
ATOM   1416 C C   . GLU A 1 289 ? -14.626 9.153   -0.336  1 27.79 ? 538  GLU A C   1 
ATOM   1417 O O   . GLU A 1 289 ? -15.601 8.45    -0.575  1 28.09 ? 538  GLU A O   1 
ATOM   1418 C CB  . GLU A 1 289 ? -14.472 8.75    2.126   1 30.37 ? 538  GLU A CB  1 
ATOM   1419 C CG  . GLU A 1 289 ? -13.729 7.957   3.188   1 37.13 ? 538  GLU A CG  1 
ATOM   1420 C CD  . GLU A 1 289 ? -14.397 7.871   4.544   1 46.15 ? 538  GLU A CD  1 
ATOM   1421 O OE1 . GLU A 1 289 ? -13.847 7.183   5.434   1 48.84 ? 538  GLU A OE1 1 
ATOM   1422 O OE2 . GLU A 1 289 ? -15.455 8.513   4.728   1 49.24 ? 538  GLU A OE2 1 
ATOM   1423 N N   . ASN A 1 290 ? -14.373 10.281  -0.99   1 27.23 ? 539  ASN A N   1 
ATOM   1424 C CA  . ASN A 1 290 ? -15.281 10.789  -2.018  1 27.56 ? 539  ASN A CA  1 
ATOM   1425 C C   . ASN A 1 290 ? -14.511 11.29   -3.239  1 29.59 ? 539  ASN A C   1 
ATOM   1426 O O   . ASN A 1 290 ? -13.37  11.715  -3.103  1 29.5  ? 539  ASN A O   1 
ATOM   1427 C CB  . ASN A 1 290 ? -16.068 11.962  -1.429  1 26.55 ? 539  ASN A CB  1 
ATOM   1428 C CG  . ASN A 1 290 ? -16.924 11.589  -0.227  1 26.59 ? 539  ASN A CG  1 
ATOM   1429 O OD1 . ASN A 1 290 ? -18.042 11.118  -0.376  1 25.54 ? 539  ASN A OD1 1 
ATOM   1430 N ND2 . ASN A 1 290 ? -16.405 11.747  0.981   1 25.8  ? 539  ASN A ND2 1 
ATOM   1431 N N   . ASP A 1 291 ? -15.153 11.303  -4.422  1 31.01 ? 540  ASP A N   1 
ATOM   1432 C CA  . ASP A 1 291 ? -14.55  11.856  -5.632  1 32.48 ? 540  ASP A CA  1 
ATOM   1433 C C   . ASP A 1 291 ? -14.472 13.387  -5.477  1 33.96 ? 540  ASP A C   1 
ATOM   1434 O O   . ASP A 1 291 ? -15.508 14.037  -5.446  1 34.25 ? 540  ASP A O   1 
ATOM   1435 C CB  . ASP A 1 291 ? -15.375 11.495  -6.886  1 34.41 ? 540  ASP A CB  1 
ATOM   1436 C CG  . ASP A 1 291 ? -14.613 11.716  -8.196  1 39    ? 540  ASP A CG  1 
ATOM   1437 O OD1 . ASP A 1 291 ? -13.742 12.598  -8.232  1 38.06 ? 540  ASP A OD1 1 
ATOM   1438 O OD2 . ASP A 1 291 ? -14.891 10.992  -9.177  1 42.76 ? 540  ASP A OD2 1 
ATOM   1439 N N   . ILE A 1 292 ? -13.24  13.956  -5.42   1 34.46 ? 541  ILE A N   1 
ATOM   1440 C CA  . ILE A 1 292 ? -12.981 15.399  -5.202  1 35.14 ? 541  ILE A CA  1 
ATOM   1441 C C   . ILE A 1 292 ? -12.947 16.244  -6.473  1 35.19 ? 541  ILE A C   1 
ATOM   1442 O O   . ILE A 1 292 ? -12.809 17.467  -6.37   1 35.02 ? 541  ILE A O   1 
ATOM   1443 C CB  . ILE A 1 292 ? -11.608 15.563  -4.474  1 35.91 ? 541  ILE A CB  1 
ATOM   1444 C CG1 . ILE A 1 292 ? -10.432 15.13   -5.401  1 37.33 ? 541  ILE A CG1 1 
ATOM   1445 C CG2 . ILE A 1 292 ? -11.578 14.775  -3.182  1 36.35 ? 541  ILE A CG2 1 
ATOM   1446 C CD1 . ILE A 1 292 ? -9.055  15.425  -4.903  1 39.04 ? 541  ILE A CD1 1 
ATOM   1447 N N   . THR A 1 293 ? -12.982 15.596  -7.663  1 35.01 ? 542  THR A N   1 
ATOM   1448 C CA  . THR A 1 293 ? -12.796 16.254  -8.954  1 35.38 ? 542  THR A CA  1 
ATOM   1449 C C   . THR A 1 293 ? -13.7   17.455  -9.196  1 36.08 ? 542  THR A C   1 
ATOM   1450 O O   . THR A 1 293 ? -14.921 17.347  -9.158  1 36.74 ? 542  THR A O   1 
ATOM   1451 C CB  . THR A 1 293 ? -12.876 15.276  -10.124 1 35.49 ? 542  THR A CB  1 
ATOM   1452 O OG1 . THR A 1 293 ? -12.161 14.075  -9.811  1 34.97 ? 542  THR A OG1 1 
ATOM   1453 C CG2 . THR A 1 293 ? -12.306 15.875  -11.366 1 35.34 ? 542  THR A CG2 1 
ATOM   1454 N N   . GLY A 1 294 ? -13.072 18.603  -9.403  1 36.15 ? 543  GLY A N   1 
ATOM   1455 C CA  . GLY A 1 294 ? -13.773 19.851  -9.646  1 37.11 ? 543  GLY A CA  1 
ATOM   1456 C C   . GLY A 1 294 ? -14.426 20.487  -8.43   1 38.18 ? 543  GLY A C   1 
ATOM   1457 O O   . GLY A 1 294 ? -15.132 21.493  -8.576  1 39.01 ? 543  GLY A O   1 
ATOM   1458 N N   . VAL A 1 295 ? -14.237 19.894  -7.229  1 37.17 ? 544  VAL A N   1 
ATOM   1459 C CA  . VAL A 1 295 ? -14.799 20.417  -5.981  1 37.35 ? 544  VAL A CA  1 
ATOM   1460 C C   . VAL A 1 295 ? -13.604 20.887  -5.128  1 36.72 ? 544  VAL A C   1 
ATOM   1461 O O   . VAL A 1 295 ? -13.524 22.067  -4.778  1 37.2  ? 544  VAL A O   1 
ATOM   1462 C CB  . VAL A 1 295 ? -15.671 19.363  -5.248  1 38.4  ? 544  VAL A CB  1 
ATOM   1463 C CG1 . VAL A 1 295 ? -16.318 19.961  -4.01   1 39.17 ? 544  VAL A CG1 1 
ATOM   1464 C CG2 . VAL A 1 295 ? -16.725 18.777  -6.182  1 39.45 ? 544  VAL A CG2 1 
ATOM   1465 N N   . LEU A 1 296 ? -12.631 19.984  -4.874  1 35.09 ? 545  LEU A N   1 
ATOM   1466 C CA  . LEU A 1 296 ? -11.427 20.363  -4.151  1 34.45 ? 545  LEU A CA  1 
ATOM   1467 C C   . LEU A 1 296 ? -10.468 21.043  -5.143  1 34.56 ? 545  LEU A C   1 
ATOM   1468 O O   . LEU A 1 296 ? -10.059 20.418  -6.122  1 35.15 ? 545  LEU A O   1 
ATOM   1469 C CB  . LEU A 1 296 ? -10.734 19.129  -3.538  1 33.76 ? 545  LEU A CB  1 
ATOM   1470 C CG  . LEU A 1 296 ? -9.483  19.48   -2.707  1 34.39 ? 545  LEU A CG  1 
ATOM   1471 C CD1 . LEU A 1 296 ? -9.877  20.043  -1.342  1 35.07 ? 545  LEU A CD1 1 
ATOM   1472 C CD2 . LEU A 1 296 ? -8.549  18.298  -2.574  1 34.04 ? 545  LEU A CD2 1 
ATOM   1473 N N   . ASP A 1 297 ? -10.139 22.307  -4.913  1 33.84 ? 546  ASP A N   1 
ATOM   1474 C CA  . ASP A 1 297 ? -9.221  23.045  -5.771  1 34.22 ? 546  ASP A CA  1 
ATOM   1475 C C   . ASP A 1 297 ? -7.981  23.309  -4.924  1 34.64 ? 546  ASP A C   1 
ATOM   1476 O O   . ASP A 1 297 ? -7.854  24.361  -4.289  1 35.4  ? 546  ASP A O   1 
ATOM   1477 C CB  . ASP A 1 297 ? -9.85   24.374  -6.211  1 36.22 ? 546  ASP A CB  1 
ATOM   1478 C CG  . ASP A 1 297 ? -9.011  25.169  -7.19   1 42.9  ? 546  ASP A CG  1 
ATOM   1479 O OD1 . ASP A 1 297 ? -8.124  24.566  -7.843  1 44.26 ? 546  ASP A OD1 1 
ATOM   1480 O OD2 . ASP A 1 297 ? -9.244  26.393  -7.313  1 46.35 ? 546  ASP A OD2 1 
ATOM   1481 N N   . HIS A 1 298 ? -7.097  22.331  -4.88   1 33.82 ? 547  HIS A N   1 
ATOM   1482 C CA  . HIS A 1 298 ? -5.895  22.392  -4.066  1 33.62 ? 547  HIS A CA  1 
ATOM   1483 C C   . HIS A 1 298 ? -4.684  21.886  -4.81   1 30.45 ? 547  HIS A C   1 
ATOM   1484 O O   . HIS A 1 298 ? -4.828  21.071  -5.714  1 28.48 ? 547  HIS A O   1 
ATOM   1485 C CB  . HIS A 1 298 ? -6.087  21.475  -2.85   1 37    ? 547  HIS A CB  1 
ATOM   1486 C CG  . HIS A 1 298 ? -6.75   22.169  -1.718  1 44.95 ? 547  HIS A CG  1 
ATOM   1487 N ND1 . HIS A 1 298 ? -6.013  22.746  -0.701  1 48.3  ? 547  HIS A ND1 1 
ATOM   1488 C CD2 . HIS A 1 298 ? -8.064  22.421  -1.512  1 47.55 ? 547  HIS A CD2 1 
ATOM   1489 C CE1 . HIS A 1 298 ? -6.902  23.301  0.111   1 49.61 ? 547  HIS A CE1 1 
ATOM   1490 N NE2 . HIS A 1 298 ? -8.149  23.129  -0.335  1 49.42 ? 547  HIS A NE2 1 
ATOM   1491 N N   . THR A 1 299 ? -3.48   22.281  -4.33   1 29.4  ? 548  THR A N   1 
ATOM   1492 C CA  . THR A 1 299 ? -2.186  21.805  -4.809  1 29.12 ? 548  THR A CA  1 
ATOM   1493 C C   . THR A 1 299 ? -1.379  21.152  -3.622  1 27.41 ? 548  THR A C   1 
ATOM   1494 O O   . THR A 1 299 ? -1.865  21.103  -2.484  1 26.94 ? 548  THR A O   1 
ATOM   1495 C CB  . THR A 1 299 ? -1.41   22.957  -5.479  1 31.54 ? 548  THR A CB  1 
ATOM   1496 O OG1 . THR A 1 299 ? -1.02   23.913  -4.473  1 32.77 ? 548  THR A OG1 1 
ATOM   1497 C CG2 . THR A 1 299 ? -2.185  23.606  -6.636  1 32.24 ? 548  THR A CG2 1 
ATOM   1498 N N   . PHE A 1 300 ? -0.173  20.633  -3.89   1 26.23 ? 549  PHE A N   1 
ATOM   1499 C CA  . PHE A 1 300 ? 0.683   20.06   -2.851  1 26.63 ? 549  PHE A CA  1 
ATOM   1500 C C   . PHE A 1 300 ? 1.461   21.149  -2.095  1 28.8  ? 549  PHE A C   1 
ATOM   1501 O O   . PHE A 1 300 ? 2.633   20.978  -1.77   1 30.26 ? 549  PHE A O   1 
ATOM   1502 C CB  . PHE A 1 300 ? 1.625   19.001  -3.42   1 25.47 ? 549  PHE A CB  1 
ATOM   1503 C CG  . PHE A 1 300 ? 1.001   17.641  -3.595  1 24.98 ? 549  PHE A CG  1 
ATOM   1504 C CD1 . PHE A 1 300 ? 0.006   17.433  -4.536  1 24.8  ? 549  PHE A CD1 1 
ATOM   1505 C CD2 . PHE A 1 300 ? 1.387   16.578  -2.801  1 24.84 ? 549  PHE A CD2 1 
ATOM   1506 C CE1 . PHE A 1 300 ? -0.576  16.183  -4.685  1 24.64 ? 549  PHE A CE1 1 
ATOM   1507 C CE2 . PHE A 1 300 ? 0.815   15.325  -2.97   1 25.34 ? 549  PHE A CE2 1 
ATOM   1508 C CZ  . PHE A 1 300 ? -0.145  15.134  -3.929  1 24.53 ? 549  PHE A CZ  1 
ATOM   1509 N N   . CYS A 1 301 ? 0.823   22.279  -1.867  1 29.42 ? 550  CYS A N   1 
ATOM   1510 C CA  . CYS A 1 301 ? 1.349   23.402  -1.118  1 30.73 ? 550  CYS A CA  1 
ATOM   1511 C C   . CYS A 1 301 ? 0.312   23.758  -0.071  1 31.86 ? 550  CYS A C   1 
ATOM   1512 O O   . CYS A 1 301 ? -0.866  23.884  -0.388  1 32.22 ? 550  CYS A O   1 
ATOM   1513 C CB  . CYS A 1 301 ? 1.639   24.593  -2.023  1 31.36 ? 550  CYS A CB  1 
ATOM   1514 S SG  . CYS A 1 301 ? 2.614   25.889  -1.22   1 36.57 ? 550  CYS A SG  1 
ATOM   1515 N N   . VAL A 1 302 ? 0.737   23.886  1.175   1 32.24 ? 551  VAL A N   1 
ATOM   1516 C CA  . VAL A 1 302 ? -0.128  24.225  2.298   1 32.97 ? 551  VAL A CA  1 
ATOM   1517 C C   . VAL A 1 302 ? 0.341   25.556  2.86    1 34.53 ? 551  VAL A C   1 
ATOM   1518 O O   . VAL A 1 302 ? 1.545   25.827  2.876   1 34.44 ? 551  VAL A O   1 
ATOM   1519 C CB  . VAL A 1 302 ? -0.117  23.121  3.391   1 33.1  ? 551  VAL A CB  1 
ATOM   1520 C CG1 . VAL A 1 302 ? -0.458  21.775  2.795   1 33.99 ? 551  VAL A CG1 1 
ATOM   1521 C CG2 . VAL A 1 302 ? 1.244   23.028  4.065   1 34.01 ? 551  VAL A CG2 1 
ATOM   1522 N N   . GLU A 1 303 ? -0.59   26.411  3.258   1 35.6  ? 552  GLU A N   1 
ATOM   1523 C CA  . GLU A 1 303 ? -0.191  27.681  3.847   1 37.41 ? 552  GLU A CA  1 
ATOM   1524 C C   . GLU A 1 303 ? -0.604  27.733  5.305   1 38.21 ? 552  GLU A C   1 
ATOM   1525 O O   . GLU A 1 303 ? -1.593  27.122  5.708   1 38.71 ? 552  GLU A O   1 
ATOM   1526 C CB  . GLU A 1 303 ? -0.626  28.888  3.021   1 40.48 ? 552  GLU A CB  1 
ATOM   1527 C CG  . GLU A 1 303 ? -2.088  29.241  3.088   1 48.36 ? 552  GLU A CG  1 
ATOM   1528 C CD  . GLU A 1 303 ? -2.359  30.619  2.508   1 57.72 ? 552  GLU A CD  1 
ATOM   1529 O OE1 . GLU A 1 303 ? -3.257  31.313  3.04    1 60.61 ? 552  GLU A OE1 1 
ATOM   1530 O OE2 . GLU A 1 303 ? -1.654  31.019  1.551   1 58.81 ? 552  GLU A OE2 1 
ATOM   1531 N N   . HIS A 1 304 ? 0.24    28.333  6.121   1 37.66 ? 553  HIS A N   1 
ATOM   1532 C CA  . HIS A 1 304 ? -0.014  28.47   7.544   1 38.23 ? 553  HIS A CA  1 
ATOM   1533 C C   . HIS A 1 304 ? 0.562   29.794  8.012   1 37.17 ? 553  HIS A C   1 
ATOM   1534 O O   . HIS A 1 304 ? 1.53    30.287  7.434   1 36.47 ? 553  HIS A O   1 
ATOM   1535 C CB  . HIS A 1 304 ? 0.585   27.296  8.348   1 40.75 ? 553  HIS A CB  1 
ATOM   1536 C CG  . HIS A 1 304 ? 2.085   27.209  8.304   1 46.72 ? 553  HIS A CG  1 
ATOM   1537 N ND1 . HIS A 1 304 ? 2.859   27.395  9.45    1 49.39 ? 553  HIS A ND1 1 
ATOM   1538 C CD2 . HIS A 1 304 ? 2.91    26.934  7.261   1 49.05 ? 553  HIS A CD2 1 
ATOM   1539 C CE1 . HIS A 1 304 ? 4.119   27.249  9.064   1 50.13 ? 553  HIS A CE1 1 
ATOM   1540 N NE2 . HIS A 1 304 ? 4.204   26.958  7.76    1 50.49 ? 553  HIS A NE2 1 
ATOM   1541 N N   . ASN A 1 305 ? -0.027  30.365  9.055   1 36.93 ? 554  ASN A N   1 
ATOM   1542 C CA  . ASN A 1 305 ? 0.452   31.628  9.585   1 37.47 ? 554  ASN A CA  1 
ATOM   1543 C C   . ASN A 1 305 ? 1.339   31.341  10.769  1 38.1  ? 554  ASN A C   1 
ATOM   1544 O O   . ASN A 1 305 ? 0.845   30.995  11.834  1 38.99 ? 554  ASN A O   1 
ATOM   1545 C CB  . ASN A 1 305 ? -0.711  32.554  9.964   1 38.64 ? 554  ASN A CB  1 
ATOM   1546 C CG  . ASN A 1 305 ? -0.294  33.971  10.315  1 42.48 ? 554  ASN A CG  1 
ATOM   1547 O OD1 . ASN A 1 305 ? -0.826  34.961  9.789   1 44.39 ? 554  ASN A OD1 1 
ATOM   1548 N ND2 . ASN A 1 305 ? 0.663   34.112  11.219  1 42.26 ? 554  ASN A ND2 1 
ATOM   1549 N N   . ALA A 1 306 ? 2.645   31.523  10.598  1 37.71 ? 555  ALA A N   1 
ATOM   1550 C CA  . ALA A 1 306 ? 3.587   31.375  11.693  1 38.19 ? 555  ALA A CA  1 
ATOM   1551 C C   . ALA A 1 306 ? 4.104   32.766  12.083  1 38.22 ? 555  ALA A C   1 
ATOM   1552 O O   . ALA A 1 306 ? 4.76    33.419  11.264  1 38.37 ? 555  ALA A O   1 
ATOM   1553 C CB  . ALA A 1 306 ? 4.758   30.5    11.27   1 38.14 ? 555  ALA A CB  1 
ATOM   1554 N N   . TYR A 1 307 ? 3.785   33.21   13.312  1 37.9  ? 556  TYR A N   1 
ATOM   1555 C CA  . TYR A 1 307 ? 4.255   34.464  13.911  1 37.96 ? 556  TYR A CA  1 
ATOM   1556 C C   . TYR A 1 307 ? 3.936   35.724  13.077  1 40.26 ? 556  TYR A C   1 
ATOM   1557 O O   . TYR A 1 307 ? 4.776   36.62   12.996  1 40.07 ? 556  TYR A O   1 
ATOM   1558 C CB  . TYR A 1 307 ? 5.771   34.372  14.224  1 36.22 ? 556  TYR A CB  1 
ATOM   1559 C CG  . TYR A 1 307 ? 6.128   33.147  15.042  1 34.88 ? 556  TYR A CG  1 
ATOM   1560 C CD1 . TYR A 1 307 ? 5.802   33.069  16.386  1 34.68 ? 556  TYR A CD1 1 
ATOM   1561 C CD2 . TYR A 1 307 ? 6.69    32.025  14.444  1 34.98 ? 556  TYR A CD2 1 
ATOM   1562 C CE1 . TYR A 1 307 ? 6.081   31.933  17.134  1 35.09 ? 556  TYR A CE1 1 
ATOM   1563 C CE2 . TYR A 1 307 ? 6.96    30.874  15.177  1 35.28 ? 556  TYR A CE2 1 
ATOM   1564 C CZ  . TYR A 1 307 ? 6.628   30.822  16.519  1 35.82 ? 556  TYR A CZ  1 
ATOM   1565 O OH  . TYR A 1 307 ? 6.913   29.704  17.269  1 36.61 ? 556  TYR A OH  1 
ATOM   1566 N N   . GLY A 1 308 ? 2.741   35.764  12.466  1 41.72 ? 557  GLY A N   1 
ATOM   1567 C CA  . GLY A 1 308 ? 2.277   36.9    11.668  1 43.08 ? 557  GLY A CA  1 
ATOM   1568 C C   . GLY A 1 308 ? 2.644   36.882  10.198  1 44.89 ? 557  GLY A C   1 
ATOM   1569 O O   . GLY A 1 308 ? 2.29    37.806  9.463   1 45.96 ? 557  GLY A O   1 
ATOM   1570 N N   . GLU A 1 309 ? 3.366   35.85   9.75    1 44.91 ? 558  GLU A N   1 
ATOM   1571 C CA  . GLU A 1 309 ? 3.769   35.727  8.357   1 45.5  ? 558  GLU A CA  1 
ATOM   1572 C C   . GLU A 1 309 ? 3.153   34.458  7.742   1 45.08 ? 558  GLU A C   1 
ATOM   1573 O O   . GLU A 1 309 ? 3.133   33.417  8.386   1 44.72 ? 558  GLU A O   1 
ATOM   1574 C CB  . GLU A 1 309 ? 5.3     35.666  8.252   1 49.22 ? 558  GLU A CB  1 
ATOM   1575 C CG  . GLU A 1 309 ? 5.884   36.592  7.198   1 58.45 ? 558  GLU A CG  1 
ATOM   1576 C CD  . GLU A 1 309 ? 5.841   38.071  7.539   1 69.33 ? 558  GLU A CD  1 
ATOM   1577 O OE1 . GLU A 1 309 ? 4.823   38.731  7.22    1 72.1  ? 558  GLU A OE1 1 
ATOM   1578 O OE2 . GLU A 1 309 ? 6.833   38.575  8.114   1 72.64 ? 558  GLU A OE2 1 
ATOM   1579 N N   . ILE A 1 310 ? 2.655   34.545  6.507   1 44.93 ? 559  ILE A N   1 
ATOM   1580 C CA  . ILE A 1 310 ? 2.068   33.388  5.836   1 44.83 ? 559  ILE A CA  1 
ATOM   1581 C C   . ILE A 1 310 ? 3.157   32.582  5.153   1 43.76 ? 559  ILE A C   1 
ATOM   1582 O O   . ILE A 1 310 ? 3.864   33.085  4.284   1 44.23 ? 559  ILE A O   1 
ATOM   1583 C CB  . ILE A 1 310 ? 0.932   33.764  4.86    1 45.88 ? 559  ILE A CB  1 
ATOM   1584 C CG1 . ILE A 1 310 ? -0.122  34.661  5.538   1 46.92 ? 559  ILE A CG1 1 
ATOM   1585 C CG2 . ILE A 1 310 ? 0.315   32.491  4.232   1 46.44 ? 559  ILE A CG2 1 
ATOM   1586 C CD1 . ILE A 1 310 ? -1.066  33.938  6.519   1 48.86 ? 559  ILE A CD1 1 
ATOM   1587 N N   . ILE A 1 311 ? 3.336   31.35   5.59    1 42.58 ? 560  ILE A N   1 
ATOM   1588 C CA  . ILE A 1 311 ? 4.344   30.458  5.033   1 42.04 ? 560  ILE A CA  1 
ATOM   1589 C C   . ILE A 1 311 ? 3.671   29.561  4.025   1 39.98 ? 560  ILE A C   1 
ATOM   1590 O O   . ILE A 1 311 ? 2.675   28.931  4.356   1 39.77 ? 560  ILE A O   1 
ATOM   1591 C CB  . ILE A 1 311 ? 4.976   29.596  6.164   1 43.25 ? 560  ILE A CB  1 
ATOM   1592 C CG1 . ILE A 1 311 ? 5.493   30.472  7.32    1 44.62 ? 560  ILE A CG1 1 
ATOM   1593 C CG2 . ILE A 1 311 ? 6.07    28.659  5.625   1 43.73 ? 560  ILE A CG2 1 
ATOM   1594 C CD1 . ILE A 1 311 ? 6.579   31.441  6.913   1 46.1  ? 560  ILE A CD1 1 
ATOM   1595 N N   . GLN A 1 312 ? 4.191   29.504  2.806   1 38.29 ? 561  GLN A N   1 
ATOM   1596 C CA  . GLN A 1 312 ? 3.685   28.591  1.79    1 37.45 ? 561  GLN A CA  1 
ATOM   1597 C C   . GLN A 1 312 ? 4.644   27.412  1.81    1 34.63 ? 561  GLN A C   1 
ATOM   1598 O O   . GLN A 1 312 ? 5.793   27.573  1.431   1 35.03 ? 561  GLN A O   1 
ATOM   1599 C CB  . GLN A 1 312 ? 3.722   29.248  0.404   1 41.18 ? 561  GLN A CB  1 
ATOM   1600 C CG  . GLN A 1 312 ? 2.938   30.543  0.312   1 48.01 ? 561  GLN A CG  1 
ATOM   1601 C CD  . GLN A 1 312 ? 1.608   30.317  -0.354  1 56.75 ? 561  GLN A CD  1 
ATOM   1602 O OE1 . GLN A 1 312 ? 0.546   30.368  0.284   1 59.87 ? 561  GLN A OE1 1 
ATOM   1603 N NE2 . GLN A 1 312 ? 1.641   30.063  -1.66   1 58.26 ? 561  GLN A NE2 1 
ATOM   1604 N N   . HIS A 1 313 ? 4.21    26.254  2.298   1 31.62 ? 562  HIS A N   1 
ATOM   1605 C CA  . HIS A 1 313 ? 5.051   25.072  2.408   1 29.1  ? 562  HIS A CA  1 
ATOM   1606 C C   . HIS A 1 313 ? 4.675   24.004  1.386   1 27.23 ? 562  HIS A C   1 
ATOM   1607 O O   . HIS A 1 313 ? 3.574   23.459  1.446   1 26.87 ? 562  HIS A O   1 
ATOM   1608 C CB  . HIS A 1 313 ? 4.937   24.48   3.83    1 28.55 ? 562  HIS A CB  1 
ATOM   1609 C CG  . HIS A 1 313 ? 5.714   23.208  4.012   1 27.46 ? 562  HIS A CG  1 
ATOM   1610 N ND1 . HIS A 1 313 ? 7.088   23.223  4.2     1 28.32 ? 562  HIS A ND1 1 
ATOM   1611 C CD2 . HIS A 1 313 ? 5.293   21.924  3.968   1 27.36 ? 562  HIS A CD2 1 
ATOM   1612 C CE1 . HIS A 1 313 ? 7.449   21.951  4.286   1 28.31 ? 562  HIS A CE1 1 
ATOM   1613 N NE2 . HIS A 1 313 ? 6.4     21.135  4.176   1 27.68 ? 562  HIS A NE2 1 
ATOM   1614 N N   . GLU A 1 314 ? 5.621   23.633  0.513   1 25.31 ? 563  GLU A N   1 
ATOM   1615 C CA  . GLU A 1 314 ? 5.392   22.566  -0.447  1 24.23 ? 563  GLU A CA  1 
ATOM   1616 C C   . GLU A 1 314 ? 5.604   21.206  0.211   1 24.11 ? 563  GLU A C   1 
ATOM   1617 O O   . GLU A 1 314 ? 6.676   20.927  0.771   1 24.05 ? 563  GLU A O   1 
ATOM   1618 C CB  . GLU A 1 314 ? 6.311   22.726  -1.654  1 24.94 ? 563  GLU A CB  1 
ATOM   1619 C CG  . GLU A 1 314 ? 5.951   23.919  -2.509  1 27.33 ? 563  GLU A CG  1 
ATOM   1620 C CD  . GLU A 1 314 ? 6.908   24.109  -3.668  1 31.99 ? 563  GLU A CD  1 
ATOM   1621 O OE1 . GLU A 1 314 ? 8.121   24.277  -3.404  1 30.49 ? 563  GLU A OE1 1 
ATOM   1622 O OE2 . GLU A 1 314 ? 6.448   24.088  -4.835  1 32.92 ? 563  GLU A OE2 1 
ATOM   1623 N N   . LEU A 1 315 ? 4.57    20.373  0.184   1 23.32 ? 564  LEU A N   1 
ATOM   1624 C CA  . LEU A 1 315 ? 4.621   19.025  0.751   1 23.52 ? 564  LEU A CA  1 
ATOM   1625 C C   . LEU A 1 315 ? 5.638   18.12   0.054   1 24.44 ? 564  LEU A C   1 
ATOM   1626 O O   . LEU A 1 315 ? 6.124   17.166  0.659   1 25.56 ? 564  LEU A O   1 
ATOM   1627 C CB  . LEU A 1 315 ? 3.228   18.37   0.714   1 22.75 ? 564  LEU A CB  1 
ATOM   1628 C CG  . LEU A 1 315 ? 2.209   19      1.699   1 23.39 ? 564  LEU A CG  1 
ATOM   1629 C CD1 . LEU A 1 315 ? 0.81    18.357  1.515   1 23.92 ? 564  LEU A CD1 1 
ATOM   1630 C CD2 . LEU A 1 315 ? 2.699   18.866  3.156   1 23.04 ? 564  LEU A CD2 1 
ATOM   1631 N N   . LYS A 1 316 ? 5.919   18.389  -1.21   1 23.9  ? 565  LYS A N   1 
ATOM   1632 C CA  . LYS A 1 316 ? 6.884   17.62   -2.01   1 24.53 ? 565  LYS A CA  1 
ATOM   1633 C C   . LYS A 1 316 ? 7.472   18.537  -3.108  1 25.02 ? 565  LYS A C   1 
ATOM   1634 O O   . LYS A 1 316 ? 6.938   19.631  -3.328  1 24.76 ? 565  LYS A O   1 
ATOM   1635 C CB  . LYS A 1 316 ? 6.234   16.326  -2.591  1 24.9  ? 565  LYS A CB  1 
ATOM   1636 C CG  . LYS A 1 316 ? 5.193   16.572  -3.687  1 27.83 ? 565  LYS A CG  1 
ATOM   1637 C CD  . LYS A 1 316 ? 4.727   15.258  -4.33   1 33.01 ? 565  LYS A CD  1 
ATOM   1638 C CE  . LYS A 1 316 ? 3.619   15.474  -5.36   1 37.69 ? 565  LYS A CE  1 
ATOM   1639 N NZ  . LYS A 1 316 ? 3.153   14.196  -5.995  1 41.12 ? 565  LYS A NZ  1 
ATOM   1640 N N   . PRO A 1 317 ? 8.573   18.127  -3.794  1 26.36 ? 566  PRO A N   1 
ATOM   1641 C CA  . PRO A 1 317 ? 9.153   18.992  -4.832  1 27.61 ? 566  PRO A CA  1 
ATOM   1642 C C   . PRO A 1 317 ? 8.151   19.389  -5.915  1 29.01 ? 566  PRO A C   1 
ATOM   1643 O O   . PRO A 1 317 ? 7.298   18.585  -6.277  1 29.36 ? 566  PRO A O   1 
ATOM   1644 C CB  . PRO A 1 317 ? 10.322  18.153  -5.385  1 28.05 ? 566  PRO A CB  1 
ATOM   1645 C CG  . PRO A 1 317 ? 10.716  17.268  -4.246  1 28.04 ? 566  PRO A CG  1 
ATOM   1646 C CD  . PRO A 1 317 ? 9.377   16.896  -3.611  1 26.18 ? 566  PRO A CD  1 
ATOM   1647 N N   . ASN A 1 318 ? 8.187   20.654  -6.34   1 29.48 ? 567  ASN A N   1 
ATOM   1648 C CA  . ASN A 1 318 ? 7.268   21.211  -7.335  1 31.86 ? 567  ASN A CA  1 
ATOM   1649 C C   . ASN A 1 318 ? 5.776   21.24   -6.883  1 32.44 ? 567  ASN A C   1 
ATOM   1650 O O   . ASN A 1 318 ? 4.886   21.462  -7.702  1 32.38 ? 567  ASN A O   1 
ATOM   1651 C CB  . ASN A 1 318 ? 7.43    20.488  -8.688  1 35.07 ? 567  ASN A CB  1 
ATOM   1652 C CG  . ASN A 1 318 ? 6.951   21.293  -9.858  1 40.16 ? 567  ASN A CG  1 
ATOM   1653 O OD1 . ASN A 1 318 ? 6.203   20.799  -10.712 1 43.78 ? 567  ASN A OD1 1 
ATOM   1654 N ND2 . ASN A 1 318 ? 7.33    22.549  -9.906  1 40.89 ? 567  ASN A ND2 1 
ATOM   1655 N N   . GLY A 1 319 ? 5.532   21.058  -5.587  1 32.34 ? 568  GLY A N   1 
ATOM   1656 C CA  . GLY A 1 319 ? 4.19    21.007  -5.009  1 32.87 ? 568  GLY A CA  1 
ATOM   1657 C C   . GLY A 1 319 ? 3.204   22.077  -5.435  1 32.92 ? 568  GLY A C   1 
ATOM   1658 O O   . GLY A 1 319 ? 2.024   21.79   -5.636  1 32.22 ? 568  GLY A O   1 
ATOM   1659 N N   . LYS A 1 320 ? 3.674   23.321  -5.555  1 33.43 ? 569  LYS A N   1 
ATOM   1660 C CA  . LYS A 1 320 ? 2.859   24.468  -5.954  1 34.41 ? 569  LYS A CA  1 
ATOM   1661 C C   . LYS A 1 320 ? 2.213   24.272  -7.324  1 35.04 ? 569  LYS A C   1 
ATOM   1662 O O   . LYS A 1 320 ? 1.18    24.873  -7.599  1 34.99 ? 569  LYS A O   1 
ATOM   1663 C CB  . LYS A 1 320 ? 3.726   25.742  -6.003  1 37.14 ? 569  LYS A CB  1 
ATOM   1664 C CG  . LYS A 1 320 ? 3.832   26.454  -4.669  1 43.19 ? 569  LYS A CG  1 
ATOM   1665 C CD  . LYS A 1 320 ? 4.935   27.509  -4.635  1 49.4  ? 569  LYS A CD  1 
ATOM   1666 C CE  . LYS A 1 320 ? 5.225   27.907  -3.197  1 54.81 ? 569  LYS A CE  1 
ATOM   1667 N NZ  . LYS A 1 320 ? 6.051   29.14   -3.102  1 58.28 ? 569  LYS A NZ  1 
ATOM   1668 N N   . SER A 1 321 ? 2.854   23.483  -8.203  1 35.36 ? 570  SER A N   1 
ATOM   1669 C CA  . SER A 1 321 ? 2.363   23.268  -9.548  1 35.8  ? 570  SER A CA  1 
ATOM   1670 C C   . SER A 1 321 ? 1.689   21.927  -9.752  1 35.75 ? 570  SER A C   1 
ATOM   1671 O O   . SER A 1 321 ? 1.371   21.606  -10.891 1 36.88 ? 570  SER A O   1 
ATOM   1672 C CB  . SER A 1 321 ? 3.492   23.461  -10.558 1 36.88 ? 570  SER A CB  1 
ATOM   1673 O OG  . SER A 1 321 ? 4.035   24.76   -10.401 1 38.88 ? 570  SER A OG  1 
ATOM   1674 N N   . ILE A 1 322 ? 1.459   21.14   -8.676  1 34.31 ? 571  ILE A N   1 
ATOM   1675 C CA  . ILE A 1 322 ? 0.833   19.833  -8.774  1 33.11 ? 571  ILE A CA  1 
ATOM   1676 C C   . ILE A 1 322 ? -0.554  19.87   -8.123  1 32.83 ? 571  ILE A C   1 
ATOM   1677 O O   . ILE A 1 322 ? -0.669  19.954  -6.892  1 31.9  ? 571  ILE A O   1 
ATOM   1678 C CB  . ILE A 1 322 ? 1.697   18.761  -8.087  1 33.42 ? 571  ILE A CB  1 
ATOM   1679 C CG1 . ILE A 1 322 ? 3.139   18.755  -8.641  1 35.06 ? 571  ILE A CG1 1 
ATOM   1680 C CG2 . ILE A 1 322 ? 1.046   17.381  -8.199  1 33.18 ? 571  ILE A CG2 1 
ATOM   1681 C CD1 . ILE A 1 322 ? 4.074   17.808  -7.924  1 36.34 ? 571  ILE A CD1 1 
ATOM   1682 N N   . PRO A 1 323 ? -1.621  19.805  -8.935  1 32.1  ? 572  PRO A N   1 
ATOM   1683 C CA  . PRO A 1 323 ? -2.965  19.794  -8.344  1 30.94 ? 572  PRO A CA  1 
ATOM   1684 C C   . PRO A 1 323 ? -3.269  18.463  -7.661  1 28.83 ? 572  PRO A C   1 
ATOM   1685 O O   . PRO A 1 323 ? -2.742  17.423  -8.044  1 28.8  ? 572  PRO A O   1 
ATOM   1686 C CB  . PRO A 1 323 ? -3.898  20.062  -9.537  1 32.27 ? 572  PRO A CB  1 
ATOM   1687 C CG  . PRO A 1 323 ? -3.115  19.687  -10.757 1 33.42 ? 572  PRO A CG  1 
ATOM   1688 C CD  . PRO A 1 323 ? -1.643  19.719  -10.413 1 31.96 ? 572  PRO A CD  1 
ATOM   1689 N N   . VAL A 1 324 ? -4.075  18.503  -6.612  1 27.55 ? 573  VAL A N   1 
ATOM   1690 C CA  . VAL A 1 324 ? -4.522  17.292  -5.947  1 27.01 ? 573  VAL A CA  1 
ATOM   1691 C C   . VAL A 1 324 ? -5.683  16.744  -6.812  1 27.15 ? 573  VAL A C   1 
ATOM   1692 O O   . VAL A 1 324 ? -6.598  17.481  -7.165  1 26.48 ? 573  VAL A O   1 
ATOM   1693 C CB  . VAL A 1 324 ? -4.986  17.571  -4.504  1 27.62 ? 573  VAL A CB  1 
ATOM   1694 C CG1 . VAL A 1 324 ? -5.357  16.262  -3.799  1 28.16 ? 573  VAL A CG1 1 
ATOM   1695 C CG2 . VAL A 1 324 ? -3.902  18.306  -3.727  1 27.55 ? 573  VAL A CG2 1 
ATOM   1696 N N   . ASN A 1 325 ? -5.627  15.464  -7.145  1 27.75 ? 574  ASN A N   1 
ATOM   1697 C CA  . ASN A 1 325 ? -6.625  14.797  -7.968  1 28.6  ? 574  ASN A CA  1 
ATOM   1698 C C   . ASN A 1 325 ? -6.856  13.372  -7.423  1 28.62 ? 574  ASN A C   1 
ATOM   1699 O O   . ASN A 1 325 ? -6.237  12.981  -6.43   1 28.18 ? 574  ASN A O   1 
ATOM   1700 C CB  . ASN A 1 325 ? -6.183  14.816  -9.467  1 30.14 ? 574  ASN A CB  1 
ATOM   1701 C CG  . ASN A 1 325 ? -4.864  14.106  -9.728  1 32.72 ? 574  ASN A CG  1 
ATOM   1702 O OD1 . ASN A 1 325 ? -4.52   13.102  -9.091  1 32.21 ? 574  ASN A OD1 1 
ATOM   1703 N ND2 . ASN A 1 325 ? -4.101  14.615  -10.683 1 33.5  ? 574  ASN A ND2 1 
ATOM   1704 N N   . GLU A 1 326 ? -7.733  12.599  -8.056  1 28.61 ? 575  GLU A N   1 
ATOM   1705 C CA  . GLU A 1 326 ? -8.039  11.241  -7.618  1 29.22 ? 575  GLU A CA  1 
ATOM   1706 C C   . GLU A 1 326 ? -6.833  10.285  -7.554  1 29.85 ? 575  GLU A C   1 
ATOM   1707 O O   . GLU A 1 326 ? -6.768  9.437   -6.655  1 30.75 ? 575  GLU A O   1 
ATOM   1708 C CB  . GLU A 1 326 ? -9.157  10.662  -8.515  1 31.68 ? 575  GLU A CB  1 
ATOM   1709 C CG  . GLU A 1 326 ? -10.508 11.293  -8.211  1 33.89 ? 575  GLU A CG  1 
ATOM   1710 C CD  . GLU A 1 326 ? -10.974 10.97   -6.801  1 36.58 ? 575  GLU A CD  1 
ATOM   1711 O OE1 . GLU A 1 326 ? -11.137 11.906  -5.981  1 37.63 ? 575  GLU A OE1 1 
ATOM   1712 O OE2 . GLU A 1 326 ? -11.145 9.766   -6.509  1 36.99 ? 575  GLU A OE2 1 
ATOM   1713 N N   . GLU A 1 327 ? -5.869  10.433  -8.472  1 29.79 ? 576  GLU A N   1 
ATOM   1714 C CA  . GLU A 1 327 ? -4.686  9.575   -8.528  1 30.66 ? 576  GLU A CA  1 
ATOM   1715 C C   . GLU A 1 327 ? -3.671  9.866   -7.403  1 29.45 ? 576  GLU A C   1 
ATOM   1716 O O   . GLU A 1 327 ? -3.042  8.936   -6.883  1 29.38 ? 576  GLU A O   1 
ATOM   1717 C CB  . GLU A 1 327 ? -3.985  9.734   -9.91   1 36.03 ? 576  GLU A CB  1 
ATOM   1718 C CG  . GLU A 1 327 ? -2.708  8.916   -10.094 1 44.39 ? 576  GLU A CG  1 
ATOM   1719 C CD  . GLU A 1 327 ? -1.399  9.565   -9.658  1 56.39 ? 576  GLU A CD  1 
ATOM   1720 O OE1 . GLU A 1 327 ? -1.232  10.789  -9.885  1 58.25 ? 576  GLU A OE1 1 
ATOM   1721 O OE2 . GLU A 1 327 ? -0.545  8.849   -9.079  1 59.6  ? 576  GLU A OE2 1 
ATOM   1722 N N   . ASN A 1 328 ? -3.505  11.147  -7.039  1 28.14 ? 577  ASN A N   1 
ATOM   1723 C CA  . ASN A 1 328 ? -2.479  11.519  -6.057  1 27.16 ? 577  ASN A CA  1 
ATOM   1724 C C   . ASN A 1 328 ? -3.04   11.953  -4.676  1 27.48 ? 577  ASN A C   1 
ATOM   1725 O O   . ASN A 1 328 ? -2.258  12.268  -3.778  1 28.39 ? 577  ASN A O   1 
ATOM   1726 C CB  . ASN A 1 328 ? -1.559  12.592  -6.68   1 26.19 ? 577  ASN A CB  1 
ATOM   1727 C CG  . ASN A 1 328 ? -2.23   13.921  -6.863  1 25.76 ? 577  ASN A CG  1 
ATOM   1728 O OD1 . ASN A 1 328 ? -3.233  14.215  -6.204  1 26.51 ? 577  ASN A OD1 1 
ATOM   1729 N ND2 . ASN A 1 328 ? -1.705  14.781  -7.736  1 22.75 ? 577  ASN A ND2 1 
ATOM   1730 N N   . LYS A 1 329 ? -4.37   11.909  -4.476  1 26.36 ? 578  LYS A N   1 
ATOM   1731 C CA  . LYS A 1 329 ? -4.962  12.336  -3.195  1 25.96 ? 578  LYS A CA  1 
ATOM   1732 C C   . LYS A 1 329 ? -4.529  11.519  -1.962  1 25.65 ? 578  LYS A C   1 
ATOM   1733 O O   . LYS A 1 329 ? -4.414  12.103  -0.89   1 24.77 ? 578  LYS A O   1 
ATOM   1734 C CB  . LYS A 1 329 ? -6.488  12.421  -3.256  1 26.08 ? 578  LYS A CB  1 
ATOM   1735 C CG  . LYS A 1 329 ? -7.189  11.071  -3.316  1 28.68 ? 578  LYS A CG  1 
ATOM   1736 C CD  . LYS A 1 329 ? -8.678  11.264  -3.588  1 30.81 ? 578  LYS A CD  1 
ATOM   1737 C CE  . LYS A 1 329 ? -9.426  9.957   -3.486  1 34.06 ? 578  LYS A CE  1 
ATOM   1738 N NZ  . LYS A 1 329 ? -10.899 10.19   -3.46   1 36.59 ? 578  LYS A NZ  1 
ATOM   1739 N N   . LYS A 1 330 ? -4.254  10.22   -2.097  1 26.05 ? 579  LYS A N   1 
ATOM   1740 C CA  . LYS A 1 330 ? -3.812  9.41    -0.957  1 26.8  ? 579  LYS A CA  1 
ATOM   1741 C C   . LYS A 1 330 ? -2.426  9.885   -0.451  1 27.06 ? 579  LYS A C   1 
ATOM   1742 O O   . LYS A 1 330 ? -2.178  9.957   0.768   1 26.73 ? 579  LYS A O   1 
ATOM   1743 C CB  . LYS A 1 330 ? -3.758  7.924   -1.343  1 30.23 ? 579  LYS A CB  1 
ATOM   1744 C CG  . LYS A 1 330 ? -5.016  7.13    -0.987  1 36.71 ? 579  LYS A CG  1 
ATOM   1745 C CD  . LYS A 1 330 ? -5.094  5.771   -1.719  1 44.02 ? 579  LYS A CD  1 
ATOM   1746 C CE  . LYS A 1 330 ? -5.199  5.965   -3.23   1 51.13 ? 579  LYS A CE  1 
ATOM   1747 N NZ  . LYS A 1 330 ? -5.236  4.68    -3.992  1 54.85 ? 579  LYS A NZ  1 
ATOM   1748 N N   . GLU A 1 331 ? -1.544  10.244  -1.391  1 26.46 ? 580  GLU A N   1 
ATOM   1749 C CA  . GLU A 1 331 ? -0.212  10.756  -1.071  1 26.32 ? 580  GLU A CA  1 
ATOM   1750 C C   . GLU A 1 331 ? -0.339  12.174  -0.474  1 25.34 ? 580  GLU A C   1 
ATOM   1751 O O   . GLU A 1 331 ? 0.366   12.524  0.457   1 26    ? 580  GLU A O   1 
ATOM   1752 C CB  . GLU A 1 331 ? 0.632   10.832  -2.358  1 28.29 ? 580  GLU A CB  1 
ATOM   1753 C CG  . GLU A 1 331 ? 2.063   11.259  -2.093  1 33.47 ? 580  GLU A CG  1 
ATOM   1754 C CD  . GLU A 1 331 ? 2.865   11.623  -3.333  1 41.25 ? 580  GLU A CD  1 
ATOM   1755 O OE1 . GLU A 1 331 ? 4.11    11.693  -3.219  1 43.24 ? 580  GLU A OE1 1 
ATOM   1756 O OE2 . GLU A 1 331 ? 2.256   11.841  -4.41   1 42.89 ? 580  GLU A OE2 1 
ATOM   1757 N N   . TYR A 1 332 ? -1.254  12.981  -0.995  1 24.25 ? 581  TYR A N   1 
ATOM   1758 C CA  . TYR A 1 332 ? -1.502  14.323  -0.489  1 24.29 ? 581  TYR A CA  1 
ATOM   1759 C C   . TYR A 1 332 ? -1.944  14.259  0.963   1 23.64 ? 581  TYR A C   1 
ATOM   1760 O O   . TYR A 1 332 ? -1.364  14.958  1.799   1 22.55 ? 581  TYR A O   1 
ATOM   1761 C CB  . TYR A 1 332 ? -2.542  15.048  -1.355  1 23.54 ? 581  TYR A CB  1 
ATOM   1762 C CG  . TYR A 1 332 ? -3.037  16.348  -0.765  1 23.72 ? 581  TYR A CG  1 
ATOM   1763 C CD1 . TYR A 1 332 ? -2.252  17.49   -0.792  1 23.72 ? 581  TYR A CD1 1 
ATOM   1764 C CD2 . TYR A 1 332 ? -4.296  16.436  -0.181  1 24.23 ? 581  TYR A CD2 1 
ATOM   1765 C CE1 . TYR A 1 332 ? -2.72   18.694  -0.296  1 24.24 ? 581  TYR A CE1 1 
ATOM   1766 C CE2 . TYR A 1 332 ? -4.778  17.642  0.307   1 24.47 ? 581  TYR A CE2 1 
ATOM   1767 C CZ  . TYR A 1 332 ? -4.004  18.777  0.207   1 25.1  ? 581  TYR A CZ  1 
ATOM   1768 O OH  . TYR A 1 332 ? -4.458  19.977  0.703   1 26.9  ? 581  TYR A OH  1 
ATOM   1769 N N   . VAL A 1 333 ? -2.919  13.372  1.266   1 23.48 ? 582  VAL A N   1 
ATOM   1770 C CA  . VAL A 1 333 ? -3.415  13.248  2.632   1 24.1  ? 582  VAL A CA  1 
ATOM   1771 C C   . VAL A 1 333 ? -2.309  12.741  3.597   1 24.16 ? 582  VAL A C   1 
ATOM   1772 O O   . VAL A 1 333 ? -2.14   13.313  4.679   1 23.07 ? 582  VAL A O   1 
ATOM   1773 C CB  . VAL A 1 333 ? -4.734  12.441  2.723   1 24.75 ? 582  VAL A CB  1 
ATOM   1774 C CG1 . VAL A 1 333 ? -5.092  12.172  4.182   1 24.99 ? 582  VAL A CG1 1 
ATOM   1775 C CG2 . VAL A 1 333 ? -5.873  13.21   2.035   1 24.7  ? 582  VAL A CG2 1 
ATOM   1776 N N   . ARG A 1 334 ? -1.519  11.737  3.174   1 24.63 ? 583  ARG A N   1 
ATOM   1777 C CA  . ARG A 1 334 ? -0.427  11.221  3.997   1 25.11 ? 583  ARG A CA  1 
ATOM   1778 C C   . ARG A 1 334 ? 0.608   12.317  4.303   1 24.31 ? 583  ARG A C   1 
ATOM   1779 O O   . ARG A 1 334 ? 0.977   12.502  5.459   1 25.33 ? 583  ARG A O   1 
ATOM   1780 C CB  . ARG A 1 334 ? 0.248   10.001  3.326   1 27.64 ? 583  ARG A CB  1 
ATOM   1781 C CG  . ARG A 1 334 ? 1.405   9.438   4.18    1 32.58 ? 583  ARG A CG  1 
ATOM   1782 C CD  . ARG A 1 334 ? 2.204   8.364   3.477   1 38.37 ? 583  ARG A CD  1 
ATOM   1783 N NE  . ARG A 1 334 ? 3.159   8.94    2.524   1 44.19 ? 583  ARG A NE  1 
ATOM   1784 C CZ  . ARG A 1 334 ? 3.009   8.908   1.207   1 48.48 ? 583  ARG A CZ  1 
ATOM   1785 N NH1 . ARG A 1 334 ? 1.958   8.299   0.665   1 49.05 ? 583  ARG A NH1 1 
ATOM   1786 N NH2 . ARG A 1 334 ? 3.912   9.471   0.417   1 49.85 ? 583  ARG A NH2 1 
ATOM   1787 N N   . LEU A 1 335 ? 1.07    13.045  3.28    1 23.11 ? 584  LEU A N   1 
ATOM   1788 C CA  . LEU A 1 335 ? 2.06    14.106  3.473   1 22.82 ? 584  LEU A CA  1 
ATOM   1789 C C   . LEU A 1 335 ? 1.481   15.229  4.358   1 23.15 ? 584  LEU A C   1 
ATOM   1790 O O   . LEU A 1 335 ? 2.183   15.774  5.219   1 22.73 ? 584  LEU A O   1 
ATOM   1791 C CB  . LEU A 1 335 ? 2.509   14.667  2.106   1 22.6  ? 584  LEU A CB  1 
ATOM   1792 C CG  . LEU A 1 335 ? 3.333   13.694  1.228   1 23.04 ? 584  LEU A CG  1 
ATOM   1793 C CD1 . LEU A 1 335 ? 3.652   14.331  -0.1    1 23.17 ? 584  LEU A CD1 1 
ATOM   1794 C CD2 . LEU A 1 335 ? 4.655   13.297  1.929   1 23.19 ? 584  LEU A CD2 1 
ATOM   1795 N N   . TYR A 1 336 ? 0.191   15.564  4.149   1 23.07 ? 585  TYR A N   1 
ATOM   1796 C CA  . TYR A 1 336 ? -0.479  16.609  4.909   1 23.43 ? 585  TYR A CA  1 
ATOM   1797 C C   . TYR A 1 336 ? -0.541  16.225  6.391   1 23.6  ? 585  TYR A C   1 
ATOM   1798 O O   . TYR A 1 336 ? -0.265  17.06   7.256   1 23.28 ? 585  TYR A O   1 
ATOM   1799 C CB  . TYR A 1 336 ? -1.896  16.858  4.355   1 23.88 ? 585  TYR A CB  1 
ATOM   1800 C CG  . TYR A 1 336 ? -2.43   18.241  4.643   1 25.3  ? 585  TYR A CG  1 
ATOM   1801 C CD1 . TYR A 1 336 ? -2.6    18.685  5.942   1 26.96 ? 585  TYR A CD1 1 
ATOM   1802 C CD2 . TYR A 1 336 ? -2.854  19.065  3.622   1 26.64 ? 585  TYR A CD2 1 
ATOM   1803 C CE1 . TYR A 1 336 ? -3.048  19.975  6.211   1 28.29 ? 585  TYR A CE1 1 
ATOM   1804 C CE2 . TYR A 1 336 ? -3.378  20.323  3.881   1 27.95 ? 585  TYR A CE2 1 
ATOM   1805 C CZ  . TYR A 1 336 ? -3.449  20.786  5.175   1 29    ? 585  TYR A CZ  1 
ATOM   1806 O OH  . TYR A 1 336 ? -3.926  22.048  5.408   1 31.56 ? 585  TYR A OH  1 
ATOM   1807 N N   . VAL A 1 337 ? -0.938  14.978  6.688   1 23.56 ? 586  VAL A N   1 
ATOM   1808 C CA  . VAL A 1 337 ? -1.041  14.48   8.068   1 23.13 ? 586  VAL A CA  1 
ATOM   1809 C C   . VAL A 1 337 ? 0.334   14.575  8.766   1 23.07 ? 586  VAL A C   1 
ATOM   1810 O O   . VAL A 1 337 ? 0.407   15.103  9.862   1 23.68 ? 586  VAL A O   1 
ATOM   1811 C CB  . VAL A 1 337 ? -1.643  13.045  8.12    1 23.69 ? 586  VAL A CB  1 
ATOM   1812 C CG1 . VAL A 1 337 ? -1.567  12.465  9.527   1 24.12 ? 586  VAL A CG1 1 
ATOM   1813 C CG2 . VAL A 1 337 ? -3.107  13.035  7.632   1 23.96 ? 586  VAL A CG2 1 
ATOM   1814 N N   . ASN A 1 338 ? 1.425   14.167  8.092   1 23.56 ? 587  ASN A N   1 
ATOM   1815 C CA  . ASN A 1 338 ? 2.773   14.223  8.676   1 24.52 ? 587  ASN A CA  1 
ATOM   1816 C C   . ASN A 1 338 ? 3.211   15.637  8.978   1 25.5  ? 587  ASN A C   1 
ATOM   1817 O O   . ASN A 1 338 ? 3.725   15.902  10.075  1 26.65 ? 587  ASN A O   1 
ATOM   1818 C CB  . ASN A 1 338 ? 3.782   13.512  7.774   1 26.67 ? 587  ASN A CB  1 
ATOM   1819 C CG  . ASN A 1 338 ? 3.523   12.027  7.661   1 32.28 ? 587  ASN A CG  1 
ATOM   1820 O OD1 . ASN A 1 338 ? 2.79    11.43   8.463   1 33.35 ? 587  ASN A OD1 1 
ATOM   1821 N ND2 . ASN A 1 338 ? 4.113   11.393  6.648   1 34.26 ? 587  ASN A ND2 1 
ATOM   1822 N N   . TRP A 1 339 ? 2.983   16.56   8.033   1 25.07 ? 588  TRP A N   1 
ATOM   1823 C CA  . TRP A 1 339 ? 3.354   17.961  8.187   1 25.54 ? 588  TRP A CA  1 
ATOM   1824 C C   . TRP A 1 339 ? 2.539   18.612  9.309   1 24.9  ? 588  TRP A C   1 
ATOM   1825 O O   . TRP A 1 339 ? 3.105   19.324  10.127  1 24    ? 588  TRP A O   1 
ATOM   1826 C CB  . TRP A 1 339 ? 3.13    18.731  6.861   1 25.94 ? 588  TRP A CB  1 
ATOM   1827 C CG  . TRP A 1 339 ? 3.203   20.227  7.009   1 27.23 ? 588  TRP A CG  1 
ATOM   1828 C CD1 . TRP A 1 339 ? 4.335   20.989  7.033   1 27.85 ? 588  TRP A CD1 1 
ATOM   1829 C CD2 . TRP A 1 339 ? 2.108   21.128  7.247   1 27.74 ? 588  TRP A CD2 1 
ATOM   1830 N NE1 . TRP A 1 339 ? 4.016   22.3    7.278   1 28.26 ? 588  TRP A NE1 1 
ATOM   1831 C CE2 . TRP A 1 339 ? 2.657   22.416  7.413   1 28.49 ? 588  TRP A CE2 1 
ATOM   1832 C CE3 . TRP A 1 339 ? 0.709   20.988  7.24    1 28.65 ? 588  TRP A CE3 1 
ATOM   1833 C CZ2 . TRP A 1 339 ? 1.858   23.556  7.546   1 30.01 ? 588  TRP A CZ2 1 
ATOM   1834 C CZ3 . TRP A 1 339 ? -0.075  22.094  7.491   1 30.18 ? 588  TRP A CZ3 1 
ATOM   1835 C CH2 . TRP A 1 339 ? 0.493   23.371  7.595   1 30.68 ? 588  TRP A CH2 1 
ATOM   1836 N N   . ARG A 1 340 ? 1.214   18.427  9.305   1 24.92 ? 589  ARG A N   1 
ATOM   1837 C CA  . ARG A 1 340 ? 0.358   19.059  10.317  1 25.56 ? 589  ARG A CA  1 
ATOM   1838 C C   . ARG A 1 340 ? 0.749   18.641  11.75   1 26.26 ? 589  ARG A C   1 
ATOM   1839 O O   . ARG A 1 340 ? 0.799   19.466  12.666  1 26.34 ? 589  ARG A O   1 
ATOM   1840 C CB  . ARG A 1 340 ? -1.119  18.713  10.039  1 25.94 ? 589  ARG A CB  1 
ATOM   1841 C CG  . ARG A 1 340 ? -2.081  19.245  11.084  1 28.88 ? 589  ARG A CG  1 
ATOM   1842 C CD  . ARG A 1 340 ? -2.103  20.768  11.14   1 31.82 ? 589  ARG A CD  1 
ATOM   1843 N NE  . ARG A 1 340 ? -2.939  21.227  12.255  1 35.81 ? 589  ARG A NE  1 
ATOM   1844 C CZ  . ARG A 1 340 ? -2.523  21.362  13.511  1 38.58 ? 589  ARG A CZ  1 
ATOM   1845 N NH1 . ARG A 1 340 ? -1.256  21.119  13.829  1 36.09 ? 589  ARG A NH1 1 
ATOM   1846 N NH2 . ARG A 1 340 ? -3.36   21.781  14.452  1 40.52 ? 589  ARG A NH2 1 
ATOM   1847 N N   . PHE A 1 341 ? 0.986   17.363  11.929  1 27.16 ? 590  PHE A N   1 
ATOM   1848 C CA  . PHE A 1 341 ? 1.343   16.783  13.21   1 29.39 ? 590  PHE A CA  1 
ATOM   1849 C C   . PHE A 1 341 ? 2.593   17.433  13.867  1 29.35 ? 590  PHE A C   1 
ATOM   1850 O O   . PHE A 1 341 ? 2.592   17.681  15.062  1 30.42 ? 590  PHE A O   1 
ATOM   1851 C CB  . PHE A 1 341 ? 1.541   15.271  13.037  1 31.22 ? 590  PHE A CB  1 
ATOM   1852 C CG  . PHE A 1 341 ? 1.707   14.606  14.368  1 34.39 ? 590  PHE A CG  1 
ATOM   1853 C CD1 . PHE A 1 341 ? 0.645   14.524  15.254  1 36.39 ? 590  PHE A CD1 1 
ATOM   1854 C CD2 . PHE A 1 341 ? 2.943   14.133  14.774  1 36.23 ? 590  PHE A CD2 1 
ATOM   1855 C CE1 . PHE A 1 341 ? 0.815   13.969  16.515  1 37.82 ? 590  PHE A CE1 1 
ATOM   1856 C CE2 . PHE A 1 341 ? 3.115   13.597  16.048  1 37.75 ? 590  PHE A CE2 1 
ATOM   1857 C CZ  . PHE A 1 341 ? 2.049   13.515  16.908  1 37.71 ? 590  PHE A CZ  1 
ATOM   1858 N N   . LEU A 1 342 ? 3.644   17.702  13.091  1 27.82 ? 591  LEU A N   1 
ATOM   1859 C CA  . LEU A 1 342 ? 4.869   18.294  13.617  1 27.51 ? 591  LEU A CA  1 
ATOM   1860 C C   . LEU A 1 342 ? 5.001   19.788  13.308  1 25.94 ? 591  LEU A C   1 
ATOM   1861 O O   . LEU A 1 342 ? 6.091   20.321  13.454  1 24.9  ? 591  LEU A O   1 
ATOM   1862 C CB  . LEU A 1 342 ? 6.073   17.554  13.002  1 28.55 ? 591  LEU A CB  1 
ATOM   1863 C CG  . LEU A 1 342 ? 6.28    16.094  13.462  1 31.77 ? 591  LEU A CG  1 
ATOM   1864 C CD1 . LEU A 1 342 ? 7.529   15.526  12.859  1 33.42 ? 591  LEU A CD1 1 
ATOM   1865 C CD2 . LEU A 1 342 ? 6.44    16.009  14.963  1 33.1  ? 591  LEU A CD2 1 
ATOM   1866 N N   . ARG A 1 343 ? 3.945   20.437  12.794  1 25.02 ? 592  ARG A N   1 
ATOM   1867 C CA  . ARG A 1 343 ? 4.024   21.84   12.378  1 25.39 ? 592  ARG A CA  1 
ATOM   1868 C C   . ARG A 1 343 ? 4.498   22.766  13.516  1 24.44 ? 592  ARG A C   1 
ATOM   1869 O O   . ARG A 1 343 ? 3.903   22.778  14.579  1 23.64 ? 592  ARG A O   1 
ATOM   1870 C CB  . ARG A 1 343 ? 2.677   22.311  11.827  1 26.59 ? 592  ARG A CB  1 
ATOM   1871 C CG  . ARG A 1 343 ? 2.725   23.714  11.272  1 30.27 ? 592  ARG A CG  1 
ATOM   1872 C CD  . ARG A 1 343 ? 1.32    24.176  10.934  1 34.67 ? 592  ARG A CD  1 
ATOM   1873 N NE  . ARG A 1 343 ? 0.437   24.304  12.094  1 38.49 ? 592  ARG A NE  1 
ATOM   1874 C CZ  . ARG A 1 343 ? -0.882  24.475  12.01   1 41.92 ? 592  ARG A CZ  1 
ATOM   1875 N NH1 . ARG A 1 343 ? -1.486  24.486  10.823  1 42.67 ? 592  ARG A NH1 1 
ATOM   1876 N NH2 . ARG A 1 343 ? -1.611  24.615  13.109  1 42.21 ? 592  ARG A NH2 1 
ATOM   1877 N N   . GLY A 1 344 ? 5.593   23.464  13.281  1 24.31 ? 593  GLY A N   1 
ATOM   1878 C CA  . GLY A 1 344 ? 6.201   24.394  14.229  1 24.8  ? 593  GLY A CA  1 
ATOM   1879 C C   . GLY A 1 344 ? 7.137   23.768  15.251  1 25.07 ? 593  GLY A C   1 
ATOM   1880 O O   . GLY A 1 344 ? 7.794   24.478  16.014  1 25.63 ? 593  GLY A O   1 
ATOM   1881 N N   . ILE A 1 345 ? 7.174   22.435  15.316  1 24.47 ? 594  ILE A N   1 
ATOM   1882 C CA  . ILE A 1 345 ? 8.01    21.713  16.28   1 23.62 ? 594  ILE A CA  1 
ATOM   1883 C C   . ILE A 1 345 ? 8.887   20.634  15.614  1 22.92 ? 594  ILE A C   1 
ATOM   1884 O O   . ILE A 1 345 ? 9.359   19.71   16.302  1 22.72 ? 594  ILE A O   1 
ATOM   1885 C CB  . ILE A 1 345 ? 7.111   21.093  17.386  1 23.85 ? 594  ILE A CB  1 
ATOM   1886 C CG1 . ILE A 1 345 ? 6.122   20.093  16.775  1 24.36 ? 594  ILE A CG1 1 
ATOM   1887 C CG2 . ILE A 1 345 ? 6.364   22.178  18.171  1 24.32 ? 594  ILE A CG2 1 
ATOM   1888 C CD1 . ILE A 1 345 ? 5.576   19.058  17.753  1 25.87 ? 594  ILE A CD1 1 
ATOM   1889 N N   . GLU A 1 346 ? 9.148   20.775  14.305  1 22.64 ? 595  GLU A N   1 
ATOM   1890 C CA  . GLU A 1 346 ? 9.942   19.818  13.525  1 23.52 ? 595  GLU A CA  1 
ATOM   1891 C C   . GLU A 1 346 ? 11.358  19.616  14.109  1 23.89 ? 595  GLU A C   1 
ATOM   1892 O O   . GLU A 1 346 ? 11.73   18.496  14.432  1 23.57 ? 595  GLU A O   1 
ATOM   1893 C CB  . GLU A 1 346 ? 10.011  20.25   12.049  1 26.51 ? 595  GLU A CB  1 
ATOM   1894 C CG  . GLU A 1 346 ? 8.666   20.412  11.336  1 28.32 ? 595  GLU A CG  1 
ATOM   1895 C CD  . GLU A 1 346 ? 8.063   21.8    11.4    1 31.49 ? 595  GLU A CD  1 
ATOM   1896 O OE1 . GLU A 1 346 ? 8.554   22.642  12.187  1 31.44 ? 595  GLU A OE1 1 
ATOM   1897 O OE2 . GLU A 1 346 ? 7.047   22.032  10.706  1 34.48 ? 595  GLU A OE2 1 
ATOM   1898 N N   . ALA A 1 347 ? 12.101  20.693  14.319  1 24.18 ? 596  ALA A N   1 
ATOM   1899 C CA  . ALA A 1 347 ? 13.476  20.619  14.834  1 25.04 ? 596  ALA A CA  1 
ATOM   1900 C C   . ALA A 1 347 ? 13.561  20.053  16.233  1 24.43 ? 596  ALA A C   1 
ATOM   1901 O O   . ALA A 1 347 ? 14.461  19.281  16.514  1 25.3  ? 596  ALA A O   1 
ATOM   1902 C CB  . ALA A 1 347 ? 14.132  22.003  14.786  1 25.62 ? 596  ALA A CB  1 
ATOM   1903 N N   . GLN A 1 348 ? 12.637  20.441  17.108  1 23.59 ? 597  GLN A N   1 
ATOM   1904 C CA  . GLN A 1 348 ? 12.591  19.989  18.494  1 22.67 ? 597  GLN A CA  1 
ATOM   1905 C C   . GLN A 1 348 ? 12.355  18.506  18.565  1 23.22 ? 597  GLN A C   1 
ATOM   1906 O O   . GLN A 1 348 ? 13.078  17.802  19.28   1 22.76 ? 597  GLN A O   1 
ATOM   1907 C CB  . GLN A 1 348 ? 11.514  20.743  19.277  1 21.63 ? 597  GLN A CB  1 
ATOM   1908 C CG  . GLN A 1 348 ? 11.75   22.247  19.326  1 22.17 ? 597  GLN A CG  1 
ATOM   1909 C CD  . GLN A 1 348 ? 10.959  23.025  18.28   1 24.39 ? 597  GLN A CD  1 
ATOM   1910 O OE1 . GLN A 1 348 ? 10.994  22.746  17.067  1 23.34 ? 597  GLN A OE1 1 
ATOM   1911 N NE2 . GLN A 1 348 ? 10.295  24.059  18.724  1 23.61 ? 597  GLN A NE2 1 
ATOM   1912 N N   . PHE A 1 349 ? 11.364  18.021  17.8    1 23.49 ? 598  PHE A N   1 
ATOM   1913 C CA  . PHE A 1 349 ? 11.012  16.618  17.765  1 25.44 ? 598  PHE A CA  1 
ATOM   1914 C C   . PHE A 1 349 ? 12.152  15.758  17.225  1 24.22 ? 598  PHE A C   1 
ATOM   1915 O O   . PHE A 1 349 ? 12.408  14.682  17.757  1 24.09 ? 598  PHE A O   1 
ATOM   1916 C CB  . PHE A 1 349 ? 9.72    16.382  16.943  1 27.34 ? 598  PHE A CB  1 
ATOM   1917 C CG  . PHE A 1 349 ? 9.059   15.137  17.455  1 30.54 ? 598  PHE A CG  1 
ATOM   1918 C CD1 . PHE A 1 349 ? 9.394   13.893  16.945  1 32.92 ? 598  PHE A CD1 1 
ATOM   1919 C CD2 . PHE A 1 349 ? 8.154   15.196  18.495  1 32.31 ? 598  PHE A CD2 1 
ATOM   1920 C CE1 . PHE A 1 349 ? 8.852   12.733  17.491  1 33.82 ? 598  PHE A CE1 1 
ATOM   1921 C CE2 . PHE A 1 349 ? 7.599   14.036  19.018  1 33.48 ? 598  PHE A CE2 1 
ATOM   1922 C CZ  . PHE A 1 349 ? 7.974   12.817  18.536  1 33.41 ? 598  PHE A CZ  1 
ATOM   1923 N N   . LEU A 1 350 ? 12.824  16.233  16.176  1 23.18 ? 599  LEU A N   1 
ATOM   1924 C CA  . LEU A 1 350 ? 13.942  15.53   15.561  1 23.56 ? 599  LEU A CA  1 
ATOM   1925 C C   . LEU A 1 350 ? 15.115  15.394  16.554  1 23.45 ? 599  LEU A C   1 
ATOM   1926 O O   . LEU A 1 350 ? 15.737  14.334  16.63   1 23.62 ? 599  LEU A O   1 
ATOM   1927 C CB  . LEU A 1 350 ? 14.366  16.308  14.296  1 24.16 ? 599  LEU A CB  1 
ATOM   1928 C CG  . LEU A 1 350 ? 15.514  15.754  13.48   1 27.08 ? 599  LEU A CG  1 
ATOM   1929 C CD1 . LEU A 1 350 ? 15.164  14.389  12.909  1 27.89 ? 599  LEU A CD1 1 
ATOM   1930 C CD2 . LEU A 1 350 ? 15.902  16.749  12.356  1 27.92 ? 599  LEU A CD2 1 
ATOM   1931 N N   . ALA A 1 351 ? 15.371  16.44   17.369  1 22.62 ? 600  ALA A N   1 
ATOM   1932 C CA  . ALA A 1 351 ? 16.455  16.398  18.368  1 21.97 ? 600  ALA A CA  1 
ATOM   1933 C C   . ALA A 1 351 ? 16.099  15.41   19.465  1 22.68 ? 600  ALA A C   1 
ATOM   1934 O O   . ALA A 1 351 ? 16.94   14.615  19.854  1 23.85 ? 600  ALA A O   1 
ATOM   1935 C CB  . ALA A 1 351 ? 16.697  17.794  18.95   1 21.15 ? 600  ALA A CB  1 
ATOM   1936 N N   . LEU A 1 352 ? 14.843  15.416  19.929  1 22.62 ? 601  LEU A N   1 
ATOM   1937 C CA  . LEU A 1 352 ? 14.342  14.484  20.947  1 23.38 ? 601  LEU A CA  1 
ATOM   1938 C C   . LEU A 1 352 ? 14.428  13.014  20.457  1 24.29 ? 601  LEU A C   1 
ATOM   1939 O O   . LEU A 1 352 ? 14.89   12.135  21.196  1 24.56 ? 601  LEU A O   1 
ATOM   1940 C CB  . LEU A 1 352 ? 12.894  14.865  21.273  1 24.54 ? 601  LEU A CB  1 
ATOM   1941 C CG  . LEU A 1 352 ? 12.27   14.142  22.442  1 27.93 ? 601  LEU A CG  1 
ATOM   1942 C CD1 . LEU A 1 352 ? 12.64   14.831  23.738  1 28.03 ? 601  LEU A CD1 1 
ATOM   1943 C CD2 . LEU A 1 352 ? 10.751  14.13   22.303  1 30.01 ? 601  LEU A CD2 1 
ATOM   1944 N N   . GLN A 1 353 ? 14.015  12.755  19.196  1 24.6  ? 602  GLN A N   1 
ATOM   1945 C CA  . GLN A 1 353 ? 14.094  11.425  18.579  1 26.07 ? 602  GLN A CA  1 
ATOM   1946 C C   . GLN A 1 353 ? 15.558  10.958  18.465  1 26.5  ? 602  GLN A C   1 
ATOM   1947 O O   . GLN A 1 353 ? 15.864  9.801   18.751  1 26.67 ? 602  GLN A O   1 
ATOM   1948 C CB  . GLN A 1 353 ? 13.472  11.437  17.168  1 29.29 ? 602  GLN A CB  1 
ATOM   1949 C CG  . GLN A 1 353 ? 12.002  11.138  17.149  1 36.47 ? 602  GLN A CG  1 
ATOM   1950 C CD  . GLN A 1 353 ? 11.524  10.857  15.738  1 47.51 ? 602  GLN A CD  1 
ATOM   1951 O OE1 . GLN A 1 353 ? 11.034  11.748  15.024  1 49.83 ? 602  GLN A OE1 1 
ATOM   1952 N NE2 . GLN A 1 353 ? 11.658  9.607   15.308  1 49.96 ? 602  GLN A NE2 1 
ATOM   1953 N N   . LYS A 1 354 ? 16.452  11.867  18.081  1 26.4  ? 603  LYS A N   1 
ATOM   1954 C CA  . LYS A 1 354 ? 17.874  11.553  17.951  1 27.28 ? 603  LYS A CA  1 
ATOM   1955 C C   . LYS A 1 354 ? 18.466  11.138  19.309  1 26.72 ? 603  LYS A C   1 
ATOM   1956 O O   . LYS A 1 354 ? 19.166  10.12   19.389  1 26.72 ? 603  LYS A O   1 
ATOM   1957 C CB  . LYS A 1 354 ? 18.637  12.754  17.355  1 29.87 ? 603  LYS A CB  1 
ATOM   1958 C CG  . LYS A 1 354 ? 20.144  12.548  17.293  1 37.26 ? 603  LYS A CG  1 
ATOM   1959 C CD  . LYS A 1 354 ? 20.874  13.817  16.851  1 43.36 ? 603  LYS A CD  1 
ATOM   1960 C CE  . LYS A 1 354 ? 22.349  13.552  16.645  1 47.99 ? 603  LYS A CE  1 
ATOM   1961 N NZ  . LYS A 1 354 ? 22.576  12.512  15.603  1 51.12 ? 603  LYS A NZ  1 
ATOM   1962 N N   . GLY A 1 355 ? 18.139  11.882  20.371  1 25.42 ? 604  GLY A N   1 
ATOM   1963 C CA  . GLY A 1 355 ? 18.625  11.533  21.704  1 24.3  ? 604  GLY A CA  1 
ATOM   1964 C C   . GLY A 1 355 ? 18.098  10.187  22.156  1 23.7  ? 604  GLY A C   1 
ATOM   1965 O O   . GLY A 1 355 ? 18.816  9.391   22.776  1 23.01 ? 604  GLY A O   1 
ATOM   1966 N N   . PHE A 1 356 ? 16.814  9.933   21.86   1 23.53 ? 605  PHE A N   1 
ATOM   1967 C CA  . PHE A 1 356 ? 16.156  8.712   22.273  1 24.37 ? 605  PHE A CA  1 
ATOM   1968 C C   . PHE A 1 356 ? 16.755  7.486   21.532  1 25.34 ? 605  PHE A C   1 
ATOM   1969 O O   . PHE A 1 356 ? 17.004  6.442   22.137  1 26.15 ? 605  PHE A O   1 
ATOM   1970 C CB  . PHE A 1 356 ? 14.638  8.83    22.022  1 23.98 ? 605  PHE A CB  1 
ATOM   1971 C CG  . PHE A 1 356 ? 13.88   7.616   22.481  1 24.13 ? 605  PHE A CG  1 
ATOM   1972 C CD1 . PHE A 1 356 ? 13.504  7.476   23.807  1 23.73 ? 605  PHE A CD1 1 
ATOM   1973 C CD2 . PHE A 1 356 ? 13.521  6.616   21.58   1 24.86 ? 605  PHE A CD2 1 
ATOM   1974 C CE1 . PHE A 1 356 ? 12.826  6.343   24.235  1 25.14 ? 605  PHE A CE1 1 
ATOM   1975 C CE2 . PHE A 1 356 ? 12.851  5.477   22.015  1 25.12 ? 605  PHE A CE2 1 
ATOM   1976 C CZ  . PHE A 1 356 ? 12.502  5.354   23.335  1 25.13 ? 605  PHE A CZ  1 
ATOM   1977 N N   . ASN A 1 357 ? 16.977  7.623   20.251  1 25.98 ? 606  ASN A N   1 
ATOM   1978 C CA  . ASN A 1 357 ? 17.516  6.522   19.432  1 27.54 ? 606  ASN A CA  1 
ATOM   1979 C C   . ASN A 1 357 ? 18.994  6.222   19.709  1 28.78 ? 606  ASN A C   1 
ATOM   1980 O O   . ASN A 1 357 ? 19.455  5.158   19.352  1 29.8  ? 606  ASN A O   1 
ATOM   1981 C CB  . ASN A 1 357 ? 17.229  6.743   17.969  1 27.93 ? 606  ASN A CB  1 
ATOM   1982 C CG  . ASN A 1 357 ? 15.733  6.644   17.705  1 30.8  ? 606  ASN A CG  1 
ATOM   1983 O OD1 . ASN A 1 357 ? 15.187  7.419   16.964  1 32.33 ? 606  ASN A OD1 1 
ATOM   1984 N ND2 . ASN A 1 357 ? 15.029  5.701   18.333  1 30.89 ? 606  ASN A ND2 1 
ATOM   1985 N N   . GLU A 1 358 ? 19.684  7.08    20.46   1 28.71 ? 607  GLU A N   1 
ATOM   1986 C CA  . GLU A 1 358 ? 21.039  6.812   20.903  1 28.81 ? 607  GLU A CA  1 
ATOM   1987 C C   . GLU A 1 358 ? 21.046  5.819   22.078  1 29.13 ? 607  GLU A C   1 
ATOM   1988 O O   . GLU A 1 358 ? 22.09   5.233   22.362  1 29.19 ? 607  GLU A O   1 
ATOM   1989 C CB  . GLU A 1 358 ? 21.737  8.12    21.292  1 29.64 ? 607  GLU A CB  1 
ATOM   1990 C CG  . GLU A 1 358 ? 22.314  8.836   20.085  1 32.46 ? 607  GLU A CG  1 
ATOM   1991 C CD  . GLU A 1 358 ? 22.824  10.237  20.352  1 37.55 ? 607  GLU A CD  1 
ATOM   1992 O OE1 . GLU A 1 358 ? 23.526  10.788  19.478  1 40.29 ? 607  GLU A OE1 1 
ATOM   1993 O OE2 . GLU A 1 358 ? 22.506  10.794  21.425  1 38.29 ? 607  GLU A OE2 1 
ATOM   1994 N N   . VAL A 1 359 ? 19.919  5.664   22.797  1 29.13 ? 608  VAL A N   1 
ATOM   1995 C CA  . VAL A 1 359 ? 19.845  4.73    23.91   1 29.36 ? 608  VAL A CA  1 
ATOM   1996 C C   . VAL A 1 359 ? 19.031  3.492   23.504  1 30.13 ? 608  VAL A C   1 
ATOM   1997 O O   . VAL A 1 359 ? 19.396  2.359   23.845  1 30.51 ? 608  VAL A O   1 
ATOM   1998 C CB  . VAL A 1 359 ? 19.267  5.386   25.188  1 29.62 ? 608  VAL A CB  1 
ATOM   1999 C CG1 . VAL A 1 359 ? 19.388  4.446   26.379  1 29.78 ? 608  VAL A CG1 1 
ATOM   2000 C CG2 . VAL A 1 359 ? 19.962  6.703   25.492  1 30.17 ? 608  VAL A CG2 1 
ATOM   2001 N N   . ILE A 1 360 ? 17.92   3.704   22.785  1 29.83 ? 609  ILE A N   1 
ATOM   2002 C CA  . ILE A 1 360 ? 17.025  2.61    22.418  1 30.92 ? 609  ILE A CA  1 
ATOM   2003 C C   . ILE A 1 360 ? 16.997  2.456   20.917  1 32.73 ? 609  ILE A C   1 
ATOM   2004 O O   . ILE A 1 360 ? 16.473  3.318   20.214  1 32.01 ? 609  ILE A O   1 
ATOM   2005 C CB  . ILE A 1 360 ? 15.6    2.854   22.996  1 30.32 ? 609  ILE A CB  1 
ATOM   2006 C CG1 . ILE A 1 360 ? 15.636  3.109   24.505  1 30.09 ? 609  ILE A CG1 1 
ATOM   2007 C CG2 . ILE A 1 360 ? 14.647  1.722   22.634  1 30.53 ? 609  ILE A CG2 1 
ATOM   2008 C CD1 . ILE A 1 360 ? 16.162  1.942   25.316  1 30.94 ? 609  ILE A CD1 1 
ATOM   2009 N N   . PRO A 1 361 ? 17.57   1.361   20.393  1 34.47 ? 610  PRO A N   1 
ATOM   2010 C CA  . PRO A 1 361 ? 17.56   1.168   18.935  1 35.15 ? 610  PRO A CA  1 
ATOM   2011 C C   . PRO A 1 361 ? 16.134  1.046   18.433  1 35.22 ? 610  PRO A C   1 
ATOM   2012 O O   . PRO A 1 361 ? 15.319  0.376   19.055  1 34.64 ? 610  PRO A O   1 
ATOM   2013 C CB  . PRO A 1 361 ? 18.334  -0.145  18.729  1 36.13 ? 610  PRO A CB  1 
ATOM   2014 C CG  . PRO A 1 361 ? 19.03   -0.425  20.027  1 36.61 ? 610  PRO A CG  1 
ATOM   2015 C CD  . PRO A 1 361 ? 18.183  0.217   21.096  1 34.73 ? 610  PRO A CD  1 
ATOM   2016 N N   . GLN A 1 362 ? 15.823  1.752   17.352  1 36.06 ? 611  GLN A N   1 
ATOM   2017 C CA  . GLN A 1 362 ? 14.494  1.752   16.757  1 37.87 ? 611  GLN A CA  1 
ATOM   2018 C C   . GLN A 1 362 ? 14.054  0.323   16.372  1 38.34 ? 611  GLN A C   1 
ATOM   2019 O O   . GLN A 1 362 ? 12.922  -0.069  16.659  1 38.07 ? 611  GLN A O   1 
ATOM   2020 C CB  . GLN A 1 362 ? 14.503  2.666   15.517  1 40.82 ? 611  GLN A CB  1 
ATOM   2021 C CG  . GLN A 1 362 ? 13.24   2.631   14.686  1 47.18 ? 611  GLN A CG  1 
ATOM   2022 C CD  . GLN A 1 362 ? 12.238  3.558   15.278  1 55.53 ? 611  GLN A CD  1 
ATOM   2023 O OE1 . GLN A 1 362 ? 12.164  4.744   14.911  1 58.14 ? 611  GLN A OE1 1 
ATOM   2024 N NE2 . GLN A 1 362 ? 11.476  3.045   16.246  1 57.39 ? 611  GLN A NE2 1 
ATOM   2025 N N   . HIS A 1 363 ? 14.976  -0.47   15.791  1 38.81 ? 612  HIS A N   1 
ATOM   2026 C CA  . HIS A 1 363 ? 14.654  -1.835  15.354  1 39.78 ? 612  HIS A CA  1 
ATOM   2027 C C   . HIS A 1 363 ? 14.08   -2.711  16.478  1 39.18 ? 612  HIS A C   1 
ATOM   2028 O O   . HIS A 1 363 ? 13.25   -3.58   16.213  1 39.43 ? 612  HIS A O   1 
ATOM   2029 C CB  . HIS A 1 363 ? 15.862  -2.515  14.662  1 41.22 ? 612  HIS A CB  1 
ATOM   2030 C CG  . HIS A 1 363 ? 16.908  -3.032  15.606  1 44.52 ? 612  HIS A CG  1 
ATOM   2031 N ND1 . HIS A 1 363 ? 16.898  -4.346  16.049  1 46.65 ? 612  HIS A ND1 1 
ATOM   2032 C CD2 . HIS A 1 363 ? 17.987  -2.404  16.133  1 45.61 ? 612  HIS A CD2 1 
ATOM   2033 C CE1 . HIS A 1 363 ? 17.946  -4.463  16.854  1 46.97 ? 612  HIS A CE1 1 
ATOM   2034 N NE2 . HIS A 1 363 ? 18.631  -3.323  16.936  1 46.41 ? 612  HIS A NE2 1 
ATOM   2035 N N   . LEU A 1 364 ? 14.47   -2.441  17.728  1 38.07 ? 613  LEU A N   1 
ATOM   2036 C CA  . LEU A 1 364 ? 13.986  -3.211  18.875  1 37.6  ? 613  LEU A CA  1 
ATOM   2037 C C   . LEU A 1 364 ? 12.52   -2.958  19.255  1 37.1  ? 613  LEU A C   1 
ATOM   2038 O O   . LEU A 1 364 ? 11.978  -3.685  20.079  1 37.09 ? 613  LEU A O   1 
ATOM   2039 C CB  . LEU A 1 364 ? 14.894  -2.981  20.092  1 37.85 ? 613  LEU A CB  1 
ATOM   2040 C CG  . LEU A 1 364 ? 16.306  -3.579  19.991  1 39.75 ? 613  LEU A CG  1 
ATOM   2041 C CD1 . LEU A 1 364 ? 17.061  -3.414  21.305  1 39.64 ? 613  LEU A CD1 1 
ATOM   2042 C CD2 . LEU A 1 364 ? 16.255  -5.089  19.631  1 40.88 ? 613  LEU A CD2 1 
ATOM   2043 N N   . LEU A 1 365 ? 11.883  -1.936  18.669  1 36.38 ? 614  LEU A N   1 
ATOM   2044 C CA  . LEU A 1 365 ? 10.508  -1.592  19.016  1 36.38 ? 614  LEU A CA  1 
ATOM   2045 C C   . LEU A 1 365 ? 9.487   -1.893  17.915  1 37.33 ? 614  LEU A C   1 
ATOM   2046 O O   . LEU A 1 365 ? 8.297   -1.735  18.167  1 37.38 ? 614  LEU A O   1 
ATOM   2047 C CB  . LEU A 1 365 ? 10.414  -0.099  19.372  1 35.55 ? 614  LEU A CB  1 
ATOM   2048 C CG  . LEU A 1 365 ? 11.45   0.455   20.347  1 36.35 ? 614  LEU A CG  1 
ATOM   2049 C CD1 . LEU A 1 365 ? 11.296  1.946   20.498  1 36.96 ? 614  LEU A CD1 1 
ATOM   2050 C CD2 . LEU A 1 365 ? 11.354  -0.22   21.693  1 36.51 ? 614  LEU A CD2 1 
ATOM   2051 N N   . LYS A 1 366 ? 9.93    -2.278  16.702  1 38.19 ? 615  LYS A N   1 
ATOM   2052 C CA  . LYS A 1 366 ? 9.049   -2.507  15.544  1 39.78 ? 615  LYS A CA  1 
ATOM   2053 C C   . LYS A 1 366 ? 7.935   -3.538  15.786  1 40.33 ? 615  LYS A C   1 
ATOM   2054 O O   . LYS A 1 366 ? 6.858   -3.447  15.205  1 41    ? 615  LYS A O   1 
ATOM   2055 C CB  . LYS A 1 366 ? 9.867   -2.865  14.291  1 43.15 ? 615  LYS A CB  1 
ATOM   2056 C CG  . LYS A 1 366 ? 10.478  -4.255  14.319  1 50.11 ? 615  LYS A CG  1 
ATOM   2057 C CD  . LYS A 1 366 ? 9.827   -5.191  13.293  1 56.62 ? 615  LYS A CD  1 
ATOM   2058 C CE  . LYS A 1 366 ? 10.232  -6.631  13.514  1 61.14 ? 615  LYS A CE  1 
ATOM   2059 N NZ  . LYS A 1 366 ? 11.708  -6.788  13.572  1 63.51 ? 615  LYS A NZ  1 
ATOM   2060 N N   . THR A 1 367 ? 8.193   -4.477  16.667  1 39.99 ? 616  THR A N   1 
ATOM   2061 C CA  . THR A 1 367 ? 7.304   -5.554  17.08   1 40.94 ? 616  THR A CA  1 
ATOM   2062 C C   . THR A 1 367 ? 6.042   -5.053  17.827  1 41.07 ? 616  THR A C   1 
ATOM   2063 O O   . THR A 1 367 ? 4.974   -5.662  17.726  1 41.16 ? 616  THR A O   1 
ATOM   2064 C CB  . THR A 1 367 ? 8.143   -6.574  17.91   1 43.32 ? 616  THR A CB  1 
ATOM   2065 O OG1 . THR A 1 367 ? 7.285   -7.474  18.59   1 45.22 ? 616  THR A OG1 1 
ATOM   2066 C CG2 . THR A 1 367 ? 9.087   -5.904  18.946  1 43.86 ? 616  THR A CG2 1 
ATOM   2067 N N   . PHE A 1 368 ? 6.172   -3.959  18.586  1 40.74 ? 617  PHE A N   1 
ATOM   2068 C CA  . PHE A 1 368 ? 5.078   -3.428  19.388  1 40.69 ? 617  PHE A CA  1 
ATOM   2069 C C   . PHE A 1 368 ? 4.071   -2.664  18.536  1 43.24 ? 617  PHE A C   1 
ATOM   2070 O O   . PHE A 1 368 ? 4.469   -1.802  17.749  1 43.71 ? 617  PHE A O   1 
ATOM   2071 C CB  . PHE A 1 368 ? 5.616   -2.508  20.501  1 38.66 ? 617  PHE A CB  1 
ATOM   2072 C CG  . PHE A 1 368 ? 6.484   -3.163  21.557  1 37.33 ? 617  PHE A CG  1 
ATOM   2073 C CD1 . PHE A 1 368 ? 7.85    -3.311  21.363  1 37.1  ? 617  PHE A CD1 1 
ATOM   2074 C CD2 . PHE A 1 368 ? 5.946   -3.566  22.768  1 36.87 ? 617  PHE A CD2 1 
ATOM   2075 C CE1 . PHE A 1 368 ? 8.65    -3.9    22.341  1 37.14 ? 617  PHE A CE1 1 
ATOM   2076 C CE2 . PHE A 1 368 ? 6.749   -4.145  23.75   1 37.09 ? 617  PHE A CE2 1 
ATOM   2077 C CZ  . PHE A 1 368 ? 8.092   -4.324  23.525  1 36.6  ? 617  PHE A CZ  1 
ATOM   2078 N N   . ASP A 1 369 ? 2.771   -2.952  18.709  1 44.27 ? 618  ASP A N   1 
ATOM   2079 C CA  . ASP A 1 369 ? 1.741   -2.22   17.976  1 46.31 ? 618  ASP A CA  1 
ATOM   2080 C C   . ASP A 1 369 ? 1.19    -1.041  18.808  1 47.1  ? 618  ASP A C   1 
ATOM   2081 O O   . ASP A 1 369 ? 1.522   -0.907  19.99   1 47.04 ? 618  ASP A O   1 
ATOM   2082 C CB  . ASP A 1 369 ? 0.637   -3.156  17.436  1 49.48 ? 618  ASP A CB  1 
ATOM   2083 C CG  . ASP A 1 369 ? -0.103  -3.949  18.494  1 57.22 ? 618  ASP A CG  1 
ATOM   2084 O OD1 . ASP A 1 369 ? -0.637  -3.324  19.442  1 59.12 ? 618  ASP A OD1 1 
ATOM   2085 O OD2 . ASP A 1 369 ? -0.173  -5.194  18.362  1 60.54 ? 618  ASP A OD2 1 
ATOM   2086 N N   . GLU A 1 370 ? 0.37    -0.179  18.178  1 47.44 ? 619  GLU A N   1 
ATOM   2087 C CA  . GLU A 1 370 ? -0.216  1.027   18.766  1 47.99 ? 619  GLU A CA  1 
ATOM   2088 C C   . GLU A 1 370 ? -0.95   0.772   20.087  1 47.5  ? 619  GLU A C   1 
ATOM   2089 O O   . GLU A 1 370 ? -0.742  1.503   21.065  1 47.49 ? 619  GLU A O   1 
ATOM   2090 C CB  . GLU A 1 370 ? -1.13   1.688   17.721  1 51.44 ? 619  GLU A CB  1 
ATOM   2091 C CG  . GLU A 1 370 ? -2.048  2.789   18.225  1 57.74 ? 619  GLU A CG  1 
ATOM   2092 C CD  . GLU A 1 370 ? -2.559  3.709   17.13   1 65.18 ? 619  GLU A CD  1 
ATOM   2093 O OE1 . GLU A 1 370 ? -2.506  3.316   15.94   1 66.56 ? 619  GLU A OE1 1 
ATOM   2094 O OE2 . GLU A 1 370 ? -2.993  4.836   17.463  1 67.45 ? 619  GLU A OE2 1 
ATOM   2095 N N   . LYS A 1 371 ? -1.767  -0.286  20.122  1 46.85 ? 620  LYS A N   1 
ATOM   2096 C CA  . LYS A 1 371 ? -2.553  -0.686  21.296  1 46.54 ? 620  LYS A CA  1 
ATOM   2097 C C   . LYS A 1 371 ? -1.636  -1.028  22.477  1 44.47 ? 620  LYS A C   1 
ATOM   2098 O O   . LYS A 1 371 ? -1.89   -0.607  23.613  1 43.97 ? 620  LYS A O   1 
ATOM   2099 C CB  . LYS A 1 371 ? -3.445  -1.902  20.949  1 49.69 ? 620  LYS A CB  1 
ATOM   2100 C CG  . LYS A 1 371 ? -4.742  -1.544  20.214  1 55.86 ? 620  LYS A CG  1 
ATOM   2101 C CD  . LYS A 1 371 ? -4.513  -1.051  18.781  1 61.14 ? 620  LYS A CD  1 
ATOM   2102 C CE  . LYS A 1 371 ? -5.479  0.048   18.401  1 65.19 ? 620  LYS A CE  1 
ATOM   2103 N NZ  . LYS A 1 371 ? -6.868  -0.47   18.268  1 67.7  ? 620  LYS A NZ  1 
ATOM   2104 N N   . GLU A 1 372 ? -0.547  -1.761  22.187  1 42.71 ? 621  GLU A N   1 
ATOM   2105 C CA  . GLU A 1 372 ? 0.429   -2.17   23.189  1 41.36 ? 621  GLU A CA  1 
ATOM   2106 C C   . GLU A 1 372 ? 1.171   -0.964  23.739  1 40.3  ? 621  GLU A C   1 
ATOM   2107 O O   . GLU A 1 372 ? 1.383   -0.88   24.944  1 40.15 ? 621  GLU A O   1 
ATOM   2108 C CB  . GLU A 1 372 ? 1.403   -3.19   22.588  1 42.56 ? 621  GLU A CB  1 
ATOM   2109 C CG  . GLU A 1 372 ? 0.742   -4.524  22.301  1 45.81 ? 621  GLU A CG  1 
ATOM   2110 C CD  . GLU A 1 372 ? 1.582   -5.478  21.477  1 52.22 ? 621  GLU A CD  1 
ATOM   2111 O OE1 . GLU A 1 372 ? 1.311   -6.699  21.519  1 55.11 ? 621  GLU A OE1 1 
ATOM   2112 O OE2 . GLU A 1 372 ? 2.515   -5.009  20.789  1 54.15 ? 621  GLU A OE2 1 
ATOM   2113 N N   . LEU A 1 373 ? 1.519   0.005   22.868  1 39.5  ? 622  LEU A N   1 
ATOM   2114 C CA  . LEU A 1 373 ? 2.205   1.22    23.315  1 38.93 ? 622  LEU A CA  1 
ATOM   2115 C C   . LEU A 1 373 ? 1.337   2.009   24.272  1 38.1  ? 622  LEU A C   1 
ATOM   2116 O O   . LEU A 1 373 ? 1.827   2.477   25.295  1 38.31 ? 622  LEU A O   1 
ATOM   2117 C CB  . LEU A 1 373 ? 2.627   2.099   22.128  1 39.06 ? 622  LEU A CB  1 
ATOM   2118 C CG  . LEU A 1 373 ? 3.517   1.448   21.083  1 41.04 ? 622  LEU A CG  1 
ATOM   2119 C CD1 . LEU A 1 373 ? 3.89    2.453   19.997  1 42.05 ? 622  LEU A CD1 1 
ATOM   2120 C CD2 . LEU A 1 373 ? 4.79    0.88    21.708  1 41.3  ? 622  LEU A CD2 1 
ATOM   2121 N N   . GLU A 1 374 ? 0.042   2.099   23.967  1 37.93 ? 623  GLU A N   1 
ATOM   2122 C CA  . GLU A 1 374 ? -0.948  2.788   24.787  1 38.45 ? 623  GLU A CA  1 
ATOM   2123 C C   . GLU A 1 374 ? -1.01   2.202   26.205  1 37.53 ? 623  GLU A C   1 
ATOM   2124 O O   . GLU A 1 374 ? -0.94   2.949   27.186  1 36.93 ? 623  GLU A O   1 
ATOM   2125 C CB  . GLU A 1 374 ? -2.318  2.724   24.096  1 42.21 ? 623  GLU A CB  1 
ATOM   2126 C CG  . GLU A 1 374 ? -3.376  3.58    24.778  1 50.48 ? 623  GLU A CG  1 
ATOM   2127 C CD  . GLU A 1 374 ? -4.768  3.496   24.171  1 58.61 ? 623  GLU A CD  1 
ATOM   2128 O OE1 . GLU A 1 374 ? -4.906  2.921   23.066  1 60.1  ? 623  GLU A OE1 1 
ATOM   2129 O OE2 . GLU A 1 374 ? -5.721  4.012   24.8    1 61.62 ? 623  GLU A OE2 1 
ATOM   2130 N N   . LEU A 1 375 ? -1.049  0.854   26.31   1 37.15 ? 624  LEU A N   1 
ATOM   2131 C CA  . LEU A 1 375 ? -1.088  0.168   27.607  1 36.64 ? 624  LEU A CA  1 
ATOM   2132 C C   . LEU A 1 375 ? 0.196   0.387   28.373  1 35.7  ? 624  LEU A C   1 
ATOM   2133 O O   . LEU A 1 375 ? 0.153   0.586   29.575  1 35.55 ? 624  LEU A O   1 
ATOM   2134 C CB  . LEU A 1 375 ? -1.344  -1.349  27.422  1 37.27 ? 624  LEU A CB  1 
ATOM   2135 C CG  . LEU A 1 375 ? -2.8    -1.846  27.449  1 39.48 ? 624  LEU A CG  1 
ATOM   2136 C CD1 . LEU A 1 375 ? -2.847  -3.349  27.514  1 40.83 ? 624  LEU A CD1 1 
ATOM   2137 C CD2 . LEU A 1 375 ? -3.545  -1.335  28.667  1 40.1  ? 624  LEU A CD2 1 
ATOM   2138 N N   . ILE A 1 376 ? 1.344   0.37    27.688  1 35.44 ? 625  ILE A N   1 
ATOM   2139 C CA  . ILE A 1 376 ? 2.626   0.574   28.363  1 36.08 ? 625  ILE A CA  1 
ATOM   2140 C C   . ILE A 1 376 ? 2.759   1.967   28.994  1 37.01 ? 625  ILE A C   1 
ATOM   2141 O O   . ILE A 1 376 ? 3.147   2.057   30.162  1 37.09 ? 625  ILE A O   1 
ATOM   2142 C CB  . ILE A 1 376 ? 3.831   0.248   27.426  1 36.17 ? 625  ILE A CB  1 
ATOM   2143 C CG1 . ILE A 1 376 ? 3.885   -1.244  27.107  1 37.16 ? 625  ILE A CG1 1 
ATOM   2144 C CG2 . ILE A 1 376 ? 5.154   0.7     28.026  1 36.01 ? 625  ILE A CG2 1 
ATOM   2145 C CD1 . ILE A 1 376 ? 4.64    -1.537  25.854  1 38.96 ? 625  ILE A CD1 1 
ATOM   2146 N N   . ILE A 1 377 ? 2.487   3.041   28.234  1 37.72 ? 626  ILE A N   1 
ATOM   2147 C CA  . ILE A 1 377 ? 2.706   4.389   28.774  1 38.86 ? 626  ILE A CA  1 
ATOM   2148 C C   . ILE A 1 377 ? 1.604   4.852   29.721  1 39.34 ? 626  ILE A C   1 
ATOM   2149 O O   . ILE A 1 377 ? 1.898   5.425   30.779  1 39.97 ? 626  ILE A O   1 
ATOM   2150 C CB  . ILE A 1 377 ? 2.97    5.434   27.661  1 40.06 ? 626  ILE A CB  1 
ATOM   2151 C CG1 . ILE A 1 377 ? 4.257   5.091   26.884  1 41.1  ? 626  ILE A CG1 1 
ATOM   2152 C CG2 . ILE A 1 377 ? 3.067   6.862   28.254  1 40.6  ? 626  ILE A CG2 1 
ATOM   2153 C CD1 . ILE A 1 377 ? 4.111   5.171   25.471  1 42.31 ? 626  ILE A CD1 1 
ATOM   2154 N N   . CYS A 1 378 ? 0.362   4.602   29.361  1 39.27 ? 627  CYS A N   1 
ATOM   2155 C CA  . CYS A 1 378 ? -0.764  5.087   30.134  1 40.75 ? 627  CYS A CA  1 
ATOM   2156 C C   . CYS A 1 378 ? -1.325  4.096   31.173  1 40.78 ? 627  CYS A C   1 
ATOM   2157 O O   . CYS A 1 378 ? -2.101  4.51    32.036  1 41.09 ? 627  CYS A O   1 
ATOM   2158 C CB  . CYS A 1 378 ? -1.842  5.585   29.18   1 42.99 ? 627  CYS A CB  1 
ATOM   2159 S SG  . CYS A 1 378 ? -1.23   6.851   28.028  1 49.1  ? 627  CYS A SG  1 
ATOM   2160 N N   . GLY A 1 379 ? -0.894  2.833   31.133  1 40    ? 628  GLY A N   1 
ATOM   2161 C CA  . GLY A 1 379 ? -1.354  1.843   32.109  1 39.4  ? 628  GLY A CA  1 
ATOM   2162 C C   . GLY A 1 379 ? -2.737  1.31    31.804  1 38.61 ? 628  GLY A C   1 
ATOM   2163 O O   . GLY A 1 379 ? -3.211  1.44    30.677  1 38.56 ? 628  GLY A O   1 
ATOM   2164 N N   . LEU A 1 380 ? -3.413  0.713   32.809  1 38.11 ? 629  LEU A N   1 
ATOM   2165 C CA  . LEU A 1 380 ? -4.756  0.142   32.61   1 37.4  ? 629  LEU A CA  1 
ATOM   2166 C C   . LEU A 1 380 ? -5.792  1.187   32.147  1 36.73 ? 629  LEU A C   1 
ATOM   2167 O O   . LEU A 1 380 ? -5.813  2.302   32.669  1 36.42 ? 629  LEU A O   1 
ATOM   2168 C CB  . LEU A 1 380 ? -5.235  -0.583  33.874  1 37.41 ? 629  LEU A CB  1 
ATOM   2169 C CG  . LEU A 1 380 ? -4.358  -1.753  34.343  1 39.28 ? 629  LEU A CG  1 
ATOM   2170 C CD1 . LEU A 1 380 ? -4.899  -2.356  35.636  1 40.22 ? 629  LEU A CD1 1 
ATOM   2171 C CD2 . LEU A 1 380 ? -4.272  -2.836  33.277  1 40    ? 629  LEU A CD2 1 
ATOM   2172 N N   . GLY A 1 381 ? -6.625  0.815   31.178  1 36.25 ? 630  GLY A N   1 
ATOM   2173 C CA  . GLY A 1 381 ? -7.632  1.704   30.606  1 36.87 ? 630  GLY A CA  1 
ATOM   2174 C C   . GLY A 1 381 ? -8.68   2.23    31.573  1 37.27 ? 630  GLY A C   1 
ATOM   2175 O O   . GLY A 1 381 ? -9.297  3.267   31.316  1 37.21 ? 630  GLY A O   1 
ATOM   2176 N N   . LYS A 1 382 ? -8.9    1.532   32.691  1 36.97 ? 631  LYS A N   1 
ATOM   2177 C CA  . LYS A 1 382 ? -9.89   1.969   33.684  1 37    ? 631  LYS A CA  1 
ATOM   2178 C C   . LYS A 1 382 ? -9.351  1.784   35.096  1 35.93 ? 631  LYS A C   1 
ATOM   2179 O O   . LYS A 1 382 ? -8.628  0.828   35.363  1 35.99 ? 631  LYS A O   1 
ATOM   2180 C CB  . LYS A 1 382 ? -11.207 1.179   33.52   1 39.97 ? 631  LYS A CB  1 
ATOM   2181 C CG  . LYS A 1 382 ? -12.462 1.862   34.095  1 46.95 ? 631  LYS A CG  1 
ATOM   2182 C CD  . LYS A 1 382 ? -12.949 3.081   33.244  1 53.28 ? 631  LYS A CD  1 
ATOM   2183 C CE  . LYS A 1 382 ? -14.468 3.209   33.08   1 56.69 ? 631  LYS A CE  1 
ATOM   2184 N NZ  . LYS A 1 382 ? -15.144 3.868   34.246  1 57.6  ? 631  LYS A NZ  1 
ATOM   2185 N N   . ILE A 1 383 ? -9.71   2.689   36      1 35.05 ? 632  ILE A N   1 
ATOM   2186 C CA  . ILE A 1 383 ? -9.338  2.577   37.396  1 34.79 ? 632  ILE A CA  1 
ATOM   2187 C C   . ILE A 1 383 ? -10.451 1.786   38.076  1 34.36 ? 632  ILE A C   1 
ATOM   2188 O O   . ILE A 1 383 ? -11.59  2.254   38.169  1 34.38 ? 632  ILE A O   1 
ATOM   2189 C CB  . ILE A 1 383 ? -9.161  3.961   38.046  1 34.82 ? 632  ILE A CB  1 
ATOM   2190 C CG1 . ILE A 1 383 ? -8.093  4.773   37.291  1 35.95 ? 632  ILE A CG1 1 
ATOM   2191 C CG2 . ILE A 1 383 ? -8.829  3.795   39.521  1 34.56 ? 632  ILE A CG2 1 
ATOM   2192 C CD1 . ILE A 1 383 ? -7.834  6.157   37.859  1 36.92 ? 632  ILE A CD1 1 
ATOM   2193 N N   . ASP A 1 384 ? -10.128 0.572   38.502  1 33.35 ? 633  ASP A N   1 
ATOM   2194 C CA  . ASP A 1 384 ? -11.078 -0.352  39.122  1 32.47 ? 633  ASP A CA  1 
ATOM   2195 C C   . ASP A 1 384 ? -11.073 -0.191  40.64   1 30.46 ? 633  ASP A C   1 
ATOM   2196 O O   . ASP A 1 384 ? -10.04  -0.411  41.26   1 29.9  ? 633  ASP A O   1 
ATOM   2197 C CB  . ASP A 1 384 ? -10.678 -1.786  38.724  1 35.03 ? 633  ASP A CB  1 
ATOM   2198 C CG  . ASP A 1 384 ? -11.72  -2.822  39.043  1 41.63 ? 633  ASP A CG  1 
ATOM   2199 O OD1 . ASP A 1 384 ? -12.061 -2.961  40.206  1 42.06 ? 633  ASP A OD1 1 
ATOM   2200 O OD2 . ASP A 1 384 ? -12.179 -3.515  38.109  1 46.24 ? 633  ASP A OD2 1 
ATOM   2201 N N   . VAL A 1 385 ? -12.235 0.159   41.244  1 28.96 ? 634  VAL A N   1 
ATOM   2202 C CA  . VAL A 1 385 ? -12.371 0.343   42.685  1 28.1  ? 634  VAL A CA  1 
ATOM   2203 C C   . VAL A 1 385 ? -12.191 -0.995  43.469  1 27.19 ? 634  VAL A C   1 
ATOM   2204 O O   . VAL A 1 385 ? -11.715 -0.972  44.611  1 26.73 ? 634  VAL A O   1 
ATOM   2205 C CB  . VAL A 1 385 ? -13.683 1.094   43.056  1 29.02 ? 634  VAL A CB  1 
ATOM   2206 C CG1 . VAL A 1 385 ? -14.923 0.284   42.679  1 29.46 ? 634  VAL A CG1 1 
ATOM   2207 C CG2 . VAL A 1 385 ? -13.71  1.48    44.537  1 29.37 ? 634  VAL A CG2 1 
ATOM   2208 N N   . ASN A 1 386 ? -12.502 -2.148  42.852  1 26.67 ? 635  ASN A N   1 
ATOM   2209 C CA  . ASN A 1 386 ? -12.307 -3.443  43.534  1 27.02 ? 635  ASN A CA  1 
ATOM   2210 C C   . ASN A 1 386 ? -10.834 -3.759  43.674  1 25.77 ? 635  ASN A C   1 
ATOM   2211 O O   . ASN A 1 386 ? -10.378 -4.027  44.776  1 24.92 ? 635  ASN A O   1 
ATOM   2212 C CB  . ASN A 1 386 ? -13.029 -4.592  42.821  1 29.29 ? 635  ASN A CB  1 
ATOM   2213 C CG  . ASN A 1 386 ? -14.493 -4.36   42.8    1 35.72 ? 635  ASN A CG  1 
ATOM   2214 O OD1 . ASN A 1 386 ? -15.137 -4.354  43.839  1 37.49 ? 635  ASN A OD1 1 
ATOM   2215 N ND2 . ASN A 1 386 ? -15.04  -4.119  41.617  1 38.43 ? 635  ASN A ND2 1 
ATOM   2216 N N   . ASP A 1 387 ? -10.08  -3.667  42.574  1 25.06 ? 636  ASP A N   1 
ATOM   2217 C CA  . ASP A 1 387 ? -8.646  -3.917  42.616  1 25.99 ? 636  ASP A CA  1 
ATOM   2218 C C   . ASP A 1 387 ? -7.942  -2.893  43.554  1 26.68 ? 636  ASP A C   1 
ATOM   2219 O O   . ASP A 1 387 ? -6.985  -3.22   44.251  1 26.48 ? 636  ASP A O   1 
ATOM   2220 C CB  . ASP A 1 387 ? -8.075  -3.858  41.192  1 26.73 ? 636  ASP A CB  1 
ATOM   2221 C CG  . ASP A 1 387 ? -6.581  -4.071  41.12   1 31.57 ? 636  ASP A CG  1 
ATOM   2222 O OD1 . ASP A 1 387 ? -6.099  -5.109  41.629  1 32.12 ? 636  ASP A OD1 1 
ATOM   2223 O OD2 . ASP A 1 387 ? -5.9    -3.234  40.519  1 33.95 ? 636  ASP A OD2 1 
ATOM   2224 N N   . TRP A 1 388 ? -8.426  -1.648  43.545  1 26.68 ? 637  TRP A N   1 
ATOM   2225 C CA  . TRP A 1 388 ? -7.899  -0.596  44.391  1 26.61 ? 637  TRP A CA  1 
ATOM   2226 C C   . TRP A 1 388 ? -8.104  -0.945  45.864  1 25.35 ? 637  TRP A C   1 
ATOM   2227 O O   . TRP A 1 388 ? -7.128  -0.939  46.616  1 23.84 ? 637  TRP A O   1 
ATOM   2228 C CB  . TRP A 1 388 ? -8.613  0.728   44.04   1 26.95 ? 637  TRP A CB  1 
ATOM   2229 C CG  . TRP A 1 388 ? -7.941  1.991   44.48   1 28.02 ? 637  TRP A CG  1 
ATOM   2230 C CD1 . TRP A 1 388 ? -6.932  2.125   45.387  1 28.99 ? 637  TRP A CD1 1 
ATOM   2231 C CD2 . TRP A 1 388 ? -8.249  3.312   44.017  1 27.92 ? 637  TRP A CD2 1 
ATOM   2232 N NE1 . TRP A 1 388 ? -6.595  3.453   45.521  1 29.37 ? 637  TRP A NE1 1 
ATOM   2233 C CE2 . TRP A 1 388 ? -7.384  4.202   44.681  1 29.09 ? 637  TRP A CE2 1 
ATOM   2234 C CE3 . TRP A 1 388 ? -9.143  3.824   43.063  1 28.48 ? 637  TRP A CE3 1 
ATOM   2235 C CZ2 . TRP A 1 388 ? -7.379  5.582   44.412  1 29.77 ? 637  TRP A CZ2 1 
ATOM   2236 C CZ3 . TRP A 1 388 ? -9.153  5.192   42.817  1 29.24 ? 637  TRP A CZ3 1 
ATOM   2237 C CH2 . TRP A 1 388 ? -8.297  6.054   43.504  1 29.57 ? 637  TRP A CH2 1 
ATOM   2238 N N   . LYS A 1 389 ? -9.361  -1.242  46.289  1 25.79 ? 638  LYS A N   1 
ATOM   2239 C CA  . LYS A 1 389 ? -9.605  -1.5    47.709  1 26.64 ? 638  LYS A CA  1 
ATOM   2240 C C   . LYS A 1 389 ? -8.955  -2.755  48.286  1 26.7  ? 638  LYS A C   1 
ATOM   2241 O O   . LYS A 1 389 ? -8.603  -2.725  49.454  1 27.06 ? 638  LYS A O   1 
ATOM   2242 C CB  . LYS A 1 389 ? -11.094 -1.479  48.077  1 29.91 ? 638  LYS A CB  1 
ATOM   2243 C CG  . LYS A 1 389 ? -11.961 -2.587  47.55   1 36.64 ? 638  LYS A CG  1 
ATOM   2244 C CD  . LYS A 1 389 ? -13.275 -2.515  48.299  1 43.49 ? 638  LYS A CD  1 
ATOM   2245 C CE  . LYS A 1 389 ? -14.433 -2.236  47.386  1 49.04 ? 638  LYS A CE  1 
ATOM   2246 N NZ  . LYS A 1 389 ? -15.704 -2.215  48.152  1 52.2  ? 638  LYS A NZ  1 
ATOM   2247 N N   . VAL A 1 390 ? -8.82   -3.846  47.519  1 26.49 ? 639  VAL A N   1 
ATOM   2248 C CA  . VAL A 1 390 ? -8.189  -5.06   48.072  1 26.5  ? 639  VAL A CA  1 
ATOM   2249 C C   . VAL A 1 390 ? -6.65   -4.917  48.177  1 25.95 ? 639  VAL A C   1 
ATOM   2250 O O   . VAL A 1 390 ? -6      -5.734  48.835  1 25.06 ? 639  VAL A O   1 
ATOM   2251 C CB  . VAL A 1 390 ? -8.619  -6.328  47.297  1 27.29 ? 639  VAL A CB  1 
ATOM   2252 C CG1 . VAL A 1 390 ? -10.141 -6.401  47.195  1 27.15 ? 639  VAL A CG1 1 
ATOM   2253 C CG2 . VAL A 1 390 ? -7.985  -6.354  45.911  1 28.2  ? 639  VAL A CG2 1 
ATOM   2254 N N   . ASN A 1 391 ? -6.073  -3.858  47.547  1 25.9  ? 640  ASN A N   1 
ATOM   2255 C CA  . ASN A 1 391 ? -4.633  -3.593  47.553  1 26.09 ? 640  ASN A CA  1 
ATOM   2256 C C   . ASN A 1 391 ? -4.271  -2.292  48.299  1 27.08 ? 640  ASN A C   1 
ATOM   2257 O O   . ASN A 1 391 ? -3.275  -1.65   47.981  1 27.67 ? 640  ASN A O   1 
ATOM   2258 C CB  . ASN A 1 391 ? -4.119  -3.58   46.137  1 25.93 ? 640  ASN A CB  1 
ATOM   2259 C CG  . ASN A 1 391 ? -4.106  -4.966  45.542  1 28.77 ? 640  ASN A CG  1 
ATOM   2260 O OD1 . ASN A 1 391 ? -3.348  -5.817  45.978  1 29.2  ? 640  ASN A OD1 1 
ATOM   2261 N ND2 . ASN A 1 391 ? -4.919  -5.22   44.516  1 28.7  ? 640  ASN A ND2 1 
ATOM   2262 N N   . THR A 1 392 ? -5.067  -1.934  49.293  1 27.28 ? 641  THR A N   1 
ATOM   2263 C CA  . THR A 1 392 ? -4.866  -0.735  50.1    1 28.32 ? 641  THR A CA  1 
ATOM   2264 C C   . THR A 1 392 ? -4.52   -1.127  51.539  1 29.96 ? 641  THR A C   1 
ATOM   2265 O O   . THR A 1 392 ? -5.185  -1.986  52.133  1 30.13 ? 641  THR A O   1 
ATOM   2266 C CB  . THR A 1 392 ? -6.149  0.155   50.084  1 28.63 ? 641  THR A CB  1 
ATOM   2267 O OG1 . THR A 1 392 ? -6.35   0.667   48.765  1 28.98 ? 641  THR A OG1 1 
ATOM   2268 C CG2 . THR A 1 392 ? -6.073  1.323   51.073  1 29.01 ? 641  THR A CG2 1 
ATOM   2269 N N   . ARG A 1 393 ? -3.504  -0.453  52.103  1 30.28 ? 642  ARG A N   1 
ATOM   2270 C CA  . ARG A 1 393 ? -3.061  -0.624  53.478  1 31.53 ? 642  ARG A CA  1 
ATOM   2271 C C   . ARG A 1 393 ? -3.818  0.345   54.362  1 31.3  ? 642  ARG A C   1 
ATOM   2272 O O   . ARG A 1 393 ? -4.002  1.51    53.993  1 31.19 ? 642  ARG A O   1 
ATOM   2273 C CB  . ARG A 1 393 ? -1.542  -0.362  53.568  1 34.71 ? 642  ARG A CB  1 
ATOM   2274 C CG  . ARG A 1 393 ? -0.869  -1.144  54.692  1 43.87 ? 642  ARG A CG  1 
ATOM   2275 C CD  . ARG A 1 393 ? 0.627   -1.356  54.452  1 51.29 ? 642  ARG A CD  1 
ATOM   2276 N NE  . ARG A 1 393 ? 1.338   -0.094  54.229  1 58.07 ? 642  ARG A NE  1 
ATOM   2277 C CZ  . ARG A 1 393 ? 1.75    0.719   55.2    1 62.56 ? 642  ARG A CZ  1 
ATOM   2278 N NH1 . ARG A 1 393 ? 1.525   0.412   56.474  1 63    ? 642  ARG A NH1 1 
ATOM   2279 N NH2 . ARG A 1 393 ? 2.373   1.851   54.905  1 63.27 ? 642  ARG A NH2 1 
ATOM   2280 N N   . LEU A 1 394 ? -4.266  -0.117  55.525  1 31.46 ? 643  LEU A N   1 
ATOM   2281 C CA  . LEU A 1 394 ? -4.991  0.742   56.466  1 32.72 ? 643  LEU A CA  1 
ATOM   2282 C C   . LEU A 1 394 ? -4.139  1.101   57.706  1 35.06 ? 643  LEU A C   1 
ATOM   2283 O O   . LEU A 1 394 ? -3.57   0.211   58.337  1 35.26 ? 643  LEU A O   1 
ATOM   2284 C CB  . LEU A 1 394 ? -6.285  0.071   56.91   1 32.12 ? 643  LEU A CB  1 
ATOM   2285 C CG  . LEU A 1 394 ? -7.192  -0.432  55.775  1 31.6  ? 643  LEU A CG  1 
ATOM   2286 C CD1 . LEU A 1 394 ? -8.357  -1.195  56.326  1 30.41 ? 643  LEU A CD1 1 
ATOM   2287 C CD2 . LEU A 1 394 ? -7.63   0.731   54.855  1 31.71 ? 643  LEU A CD2 1 
ATOM   2288 N N   . LYS A 1 395 ? -4.06   2.404   58.055  1 36.03 ? 644  LYS A N   1 
ATOM   2289 C CA  . LYS A 1 395 ? -3.297  2.874   59.223  1 37    ? 644  LYS A CA  1 
ATOM   2290 C C   . LYS A 1 395 ? -4.222  3.641   60.138  1 36.92 ? 644  LYS A C   1 
ATOM   2291 O O   . LYS A 1 395 ? -4.842  4.609   59.69   1 38.02 ? 644  LYS A O   1 
ATOM   2292 C CB  . LYS A 1 395 ? -2.159  3.798   58.788  1 40.73 ? 644  LYS A CB  1 
ATOM   2293 C CG  . LYS A 1 395 ? -0.983  3.096   58.116  1 47.73 ? 644  LYS A CG  1 
ATOM   2294 C CD  . LYS A 1 395 ? 0.16    4.084   57.803  1 54.57 ? 644  LYS A CD  1 
ATOM   2295 C CE  . LYS A 1 395 ? 1.533   3.469   58.034  1 59.95 ? 644  LYS A CE  1 
ATOM   2296 N NZ  . LYS A 1 395 ? 2.646   4.356   57.586  1 62.61 ? 644  LYS A NZ  1 
ATOM   2297 N N   . HIS A 1 396 ? -4.339  3.21    61.404  1 35.58 ? 645  HIS A N   1 
ATOM   2298 C CA  . HIS A 1 396 ? -5.187  3.808   62.444  1 35.57 ? 645  HIS A CA  1 
ATOM   2299 C C   . HIS A 1 396 ? -6.688  3.772   62.114  1 34.58 ? 645  HIS A C   1 
ATOM   2300 O O   . HIS A 1 396 ? -7.477  4.5     62.723  1 35.16 ? 645  HIS A O   1 
ATOM   2301 C CB  . HIS A 1 396 ? -4.718  5.219   62.863  1 37.52 ? 645  HIS A CB  1 
ATOM   2302 C CG  . HIS A 1 396 ? -3.346  5.166   63.459  1 41.1  ? 645  HIS A CG  1 
ATOM   2303 N ND1 . HIS A 1 396 ? -3.15   4.806   64.785  1 43.15 ? 645  HIS A ND1 1 
ATOM   2304 C CD2 . HIS A 1 396 ? -2.14   5.282   62.854  1 42.71 ? 645  HIS A CD2 1 
ATOM   2305 C CE1 . HIS A 1 396 ? -1.838  4.756   64.951  1 43.92 ? 645  HIS A CE1 1 
ATOM   2306 N NE2 . HIS A 1 396 ? -1.188  5.029   63.815  1 44.11 ? 645  HIS A NE2 1 
ATOM   2307 N N   . CYS A 1 397 ? -7.087  2.854   61.219  1 32.17 ? 646  CYS A N   1 
ATOM   2308 C CA  . CYS A 1 397 ? -8.482  2.544   60.922  1 30.37 ? 646  CYS A CA  1 
ATOM   2309 C C   . CYS A 1 397 ? -8.57   1.049   60.577  1 28.83 ? 646  CYS A C   1 
ATOM   2310 O O   . CYS A 1 397 ? -7.607  0.456   60.066  1 28.59 ? 646  CYS A O   1 
ATOM   2311 C CB  . CYS A 1 397 ? -9.067  3.431   59.82   1 29.46 ? 646  CYS A CB  1 
ATOM   2312 S SG  . CYS A 1 397 ? -8.077  3.496   58.31   1 32.95 ? 646  CYS A SG  1 
ATOM   2313 N N   . THR A 1 398 ? -9.69   0.443   60.904  1 27.87 ? 647  THR A N   1 
ATOM   2314 C CA  . THR A 1 398 ? -9.903  -0.977  60.662  1 28.23 ? 647  THR A CA  1 
ATOM   2315 C C   . THR A 1 398 ? -10.699 -1.243  59.381  1 28.62 ? 647  THR A C   1 
ATOM   2316 O O   . THR A 1 398 ? -11.425 -0.369  58.901  1 28.18 ? 647  THR A O   1 
ATOM   2317 C CB  . THR A 1 398 ? -10.6   -1.587  61.876  1 29.27 ? 647  THR A CB  1 
ATOM   2318 O OG1 . THR A 1 398 ? -11.896 -1.002  62.009  1 30.56 ? 647  THR A OG1 1 
ATOM   2319 C CG2 . THR A 1 398 ? -9.793  -1.399  63.161  1 29.75 ? 647  THR A CG2 1 
ATOM   2320 N N   . PRO A 1 399 ? -10.605 -2.486  58.854  1 28.9  ? 648  PRO A N   1 
ATOM   2321 C CA  . PRO A 1 399 ? -11.369 -2.85   57.655  1 28.36 ? 648  PRO A CA  1 
ATOM   2322 C C   . PRO A 1 399 ? -12.861 -2.568  57.732  1 29.25 ? 648  PRO A C   1 
ATOM   2323 O O   . PRO A 1 399 ? -13.442 -2.157  56.756  1 28.97 ? 648  PRO A O   1 
ATOM   2324 C CB  . PRO A 1 399 ? -11.101 -4.353  57.526  1 28.39 ? 648  PRO A CB  1 
ATOM   2325 C CG  . PRO A 1 399 ? -9.777  -4.541  58.117  1 29.05 ? 648  PRO A CG  1 
ATOM   2326 C CD  . PRO A 1 399 ? -9.754  -3.611  59.296  1 27.95 ? 648  PRO A CD  1 
ATOM   2327 N N   . ASP A 1 400 ? -13.474 -2.802  58.873  1 30.85 ? 649  ASP A N   1 
ATOM   2328 C CA  . ASP A 1 400 ? -14.913 -2.619  59.046  1 32.93 ? 649  ASP A CA  1 
ATOM   2329 C C   . ASP A 1 400 ? -15.313 -1.25   59.589  1 32.98 ? 649  ASP A C   1 
ATOM   2330 O O   . ASP A 1 400 ? -16.45  -1.104  59.993  1 33.16 ? 649  ASP A O   1 
ATOM   2331 C CB  . ASP A 1 400 ? -15.465 -3.72   59.968  1 36.34 ? 649  ASP A CB  1 
ATOM   2332 C CG  . ASP A 1 400 ? -14.9   -3.683  61.383  1 43.2  ? 649  ASP A CG  1 
ATOM   2333 O OD1 . ASP A 1 400 ? -13.867 -3.009  61.601  1 44.91 ? 649  ASP A OD1 1 
ATOM   2334 O OD2 . ASP A 1 400 ? -15.487 -4.326  62.27   1 45.7  ? 649  ASP A OD2 1 
ATOM   2335 N N   . SER A 1 401 ? -14.384 -0.278  59.668  1 32.74 ? 650  SER A N   1 
ATOM   2336 C CA  . SER A 1 401 ? -14.721 1.051   60.182  1 32.57 ? 650  SER A CA  1 
ATOM   2337 C C   . SER A 1 401 ? -15.528 1.885   59.176  1 32.83 ? 650  SER A C   1 
ATOM   2338 O O   . SER A 1 401 ? -15.476 1.652   57.977  1 31.7  ? 650  SER A O   1 
ATOM   2339 C CB  . SER A 1 401 ? -13.472 1.821   60.599  1 32.34 ? 650  SER A CB  1 
ATOM   2340 O OG  . SER A 1 401 ? -12.707 2.207   59.474  1 33.08 ? 650  SER A OG  1 
ATOM   2341 N N   . ASN A 1 402 ? -16.243 2.885   59.703  1 33.85 ? 651  ASN A N   1 
ATOM   2342 C CA  . ASN A 1 402 ? -17.077 3.804   58.961  1 34.17 ? 651  ASN A CA  1 
ATOM   2343 C C   . ASN A 1 402 ? -16.237 4.604   58.014  1 32.94 ? 651  ASN A C   1 
ATOM   2344 O O   . ASN A 1 402 ? -16.644 4.758   56.877  1 32.17 ? 651  ASN A O   1 
ATOM   2345 C CB  . ASN A 1 402 ? -17.824 4.747   59.919  1 36.11 ? 651  ASN A CB  1 
ATOM   2346 C CG  . ASN A 1 402 ? -18.996 4.121   60.613  1 40.53 ? 651  ASN A CG  1 
ATOM   2347 O OD1 . ASN A 1 402 ? -19.439 3.023   60.279  1 42.89 ? 651  ASN A OD1 1 
ATOM   2348 N ND2 . ASN A 1 402 ? -19.541 4.82    61.596  1 41.77 ? 651  ASN A ND2 1 
ATOM   2349 N N   . ILE A 1 403 ? -15.051 5.09    58.448  1 32.08 ? 652  ILE A N   1 
ATOM   2350 C CA  . ILE A 1 403 ? -14.224 5.916   57.578  1 32.33 ? 652  ILE A CA  1 
ATOM   2351 C C   . ILE A 1 403 ? -13.778 5.17    56.31   1 30.77 ? 652  ILE A C   1 
ATOM   2352 O O   . ILE A 1 403 ? -13.743 5.773   55.24   1 31.29 ? 652  ILE A O   1 
ATOM   2353 C CB  . ILE A 1 403 ? -13.033 6.577   58.316  1 34.26 ? 652  ILE A CB  1 
ATOM   2354 C CG1 . ILE A 1 403 ? -12.609 7.885   57.64   1 36.08 ? 652  ILE A CG1 1 
ATOM   2355 C CG2 . ILE A 1 403 ? -11.833 5.633   58.492  1 35.02 ? 652  ILE A CG2 1 
ATOM   2356 C CD1 . ILE A 1 403 ? -13.511 9.101   58.049  1 37.68 ? 652  ILE A CD1 1 
ATOM   2357 N N   . VAL A 1 404 ? -13.456 3.874   56.429  1 28.7  ? 653  VAL A N   1 
ATOM   2358 C CA  . VAL A 1 404 ? -13.016 3.043   55.304  1 27.26 ? 653  VAL A CA  1 
ATOM   2359 C C   . VAL A 1 404 ? -14.215 2.719   54.403  1 26.6  ? 653  VAL A C   1 
ATOM   2360 O O   . VAL A 1 404 ? -14.128 2.871   53.186  1 26.31 ? 653  VAL A O   1 
ATOM   2361 C CB  . VAL A 1 404 ? -12.307 1.778   55.843  1 27.09 ? 653  VAL A CB  1 
ATOM   2362 C CG1 . VAL A 1 404 ? -12.069 0.751   54.739  1 26.89 ? 653  VAL A CG1 1 
ATOM   2363 C CG2 . VAL A 1 404 ? -10.999 2.164   56.548  1 27.25 ? 653  VAL A CG2 1 
ATOM   2364 N N   . LYS A 1 405 ? -15.357 2.364   55.015  1 26.52 ? 654  LYS A N   1 
ATOM   2365 C CA  . LYS A 1 405 ? -16.58  2.095   54.281  1 27.5  ? 654  LYS A CA  1 
ATOM   2366 C C   . LYS A 1 405 ? -17.013 3.338   53.461  1 26.77 ? 654  LYS A C   1 
ATOM   2367 O O   . LYS A 1 405 ? -17.274 3.223   52.266  1 26.31 ? 654  LYS A O   1 
ATOM   2368 C CB  . LYS A 1 405 ? -17.7   1.662   55.241  1 29.49 ? 654  LYS A CB  1 
ATOM   2369 C CG  . LYS A 1 405 ? -18.998 1.345   54.505  1 35.11 ? 654  LYS A CG  1 
ATOM   2370 C CD  . LYS A 1 405 ? -20.157 0.975   55.449  1 40.62 ? 654  LYS A CD  1 
ATOM   2371 C CE  . LYS A 1 405 ? -20.652 2.161   56.242  1 45.96 ? 654  LYS A CE  1 
ATOM   2372 N NZ  . LYS A 1 405 ? -20.194 2.119   57.662  1 49.36 ? 654  LYS A NZ  1 
ATOM   2373 N N   . TRP A 1 406 ? -17.005 4.524   54.09   1 25.92 ? 655  TRP A N   1 
ATOM   2374 C CA  . TRP A 1 406 ? -17.374 5.768   53.424  1 25.92 ? 655  TRP A CA  1 
ATOM   2375 C C   . TRP A 1 406 ? -16.386 6.164   52.354  1 24.96 ? 655  TRP A C   1 
ATOM   2376 O O   . TRP A 1 406 ? -16.792 6.627   51.268  1 25.17 ? 655  TRP A O   1 
ATOM   2377 C CB  . TRP A 1 406 ? -17.589 6.882   54.448  1 26.67 ? 655  TRP A CB  1 
ATOM   2378 C CG  . TRP A 1 406 ? -18.684 6.6     55.445  1 28.45 ? 655  TRP A CG  1 
ATOM   2379 C CD1 . TRP A 1 406 ? -19.78  5.799   55.273  1 29.86 ? 655  TRP A CD1 1 
ATOM   2380 C CD2 . TRP A 1 406 ? -18.816 7.18    56.741  1 29.48 ? 655  TRP A CD2 1 
ATOM   2381 N NE1 . TRP A 1 406 ? -20.564 5.826   56.394  1 30.5  ? 655  TRP A NE1 1 
ATOM   2382 C CE2 . TRP A 1 406 ? -20.005 6.682   57.306  1 30.42 ? 655  TRP A CE2 1 
ATOM   2383 C CE3 . TRP A 1 406 ? -18.058 8.099   57.474  1 30.94 ? 655  TRP A CE3 1 
ATOM   2384 C CZ2 . TRP A 1 406 ? -20.454 7.079   58.564  1 31.3  ? 655  TRP A CZ2 1 
ATOM   2385 C CZ3 . TRP A 1 406 ? -18.503 8.48    58.724  1 31.08 ? 655  TRP A CZ3 1 
ATOM   2386 C CH2 . TRP A 1 406 ? -19.68  7.969   59.257  1 30.98 ? 655  TRP A CH2 1 
ATOM   2387 N N   . PHE A 1 407 ? -15.086 5.896   52.591  1 23.22 ? 656  PHE A N   1 
ATOM   2388 C CA  . PHE A 1 407 ? -14.094 6.183   51.547  1 23.45 ? 656  PHE A CA  1 
ATOM   2389 C C   . PHE A 1 407 ? -14.361 5.36    50.277  1 22.95 ? 656  PHE A C   1 
ATOM   2390 O O   . PHE A 1 407 ? -14.342 5.919   49.187  1 22.32 ? 656  PHE A O   1 
ATOM   2391 C CB  . PHE A 1 407 ? -12.663 5.929   52.049  1 23.46 ? 656  PHE A CB  1 
ATOM   2392 C CG  . PHE A 1 407 ? -11.598 6.331   51.068  1 24.34 ? 656  PHE A CG  1 
ATOM   2393 C CD1 . PHE A 1 407 ? -11.128 7.636   51.029  1 25.67 ? 656  PHE A CD1 1 
ATOM   2394 C CD2 . PHE A 1 407 ? -11.059 5.407   50.189  1 24.37 ? 656  PHE A CD2 1 
ATOM   2395 C CE1 . PHE A 1 407 ? -10.133 8.001   50.133  1 26.26 ? 656  PHE A CE1 1 
ATOM   2396 C CE2 . PHE A 1 407 ? -10.096 5.781   49.282  1 25.55 ? 656  PHE A CE2 1 
ATOM   2397 C CZ  . PHE A 1 407 ? -9.649  7.08    49.244  1 26.17 ? 656  PHE A CZ  1 
ATOM   2398 N N   . TRP A 1 408 ? -14.581 4.031   50.415  1 22.55 ? 657  TRP A N   1 
ATOM   2399 C CA  . TRP A 1 408 ? -14.788 3.194   49.236  1 22.19 ? 657  TRP A CA  1 
ATOM   2400 C C   . TRP A 1 408 ? -16.144 3.431   48.593  1 23.16 ? 657  TRP A C   1 
ATOM   2401 O O   . TRP A 1 408 ? -16.244 3.315   47.387  1 23.75 ? 657  TRP A O   1 
ATOM   2402 C CB  . TRP A 1 408 ? -14.514 1.7     49.513  1 21.13 ? 657  TRP A CB  1 
ATOM   2403 C CG  . TRP A 1 408 ? -13.067 1.431   49.852  1 20.94 ? 657  TRP A CG  1 
ATOM   2404 C CD1 . TRP A 1 408 ? -12.581 0.979   51.043  1 21.04 ? 657  TRP A CD1 1 
ATOM   2405 C CD2 . TRP A 1 408 ? -11.915 1.755   49.046  1 20.57 ? 657  TRP A CD2 1 
ATOM   2406 N NE1 . TRP A 1 408 ? -11.203 0.94    51.004  1 21.23 ? 657  TRP A NE1 1 
ATOM   2407 C CE2 . TRP A 1 408 ? -10.772 1.459   49.812  1 20.89 ? 657  TRP A CE2 1 
ATOM   2408 C CE3 . TRP A 1 408 ? -11.741 2.241   47.743  1 20.9  ? 657  TRP A CE3 1 
ATOM   2409 C CZ2 . TRP A 1 408 ? -9.484  1.608   49.31   1 21.25 ? 657  TRP A CZ2 1 
ATOM   2410 C CZ3 . TRP A 1 408 ? -10.464 2.446   47.274  1 20.98 ? 657  TRP A CZ3 1 
ATOM   2411 C CH2 . TRP A 1 408 ? -9.351  2.147   48.058  1 21.22 ? 657  TRP A CH2 1 
ATOM   2412 N N   . LYS A 1 409 ? -17.147 3.848   49.367  1 23.88 ? 658  LYS A N   1 
ATOM   2413 C CA  . LYS A 1 409 ? -18.45  4.195   48.822  1 25.07 ? 658  LYS A CA  1 
ATOM   2414 C C   . LYS A 1 409 ? -18.313 5.474   47.933  1 25.19 ? 658  LYS A C   1 
ATOM   2415 O O   . LYS A 1 409 ? -18.917 5.548   46.862  1 25.85 ? 658  LYS A O   1 
ATOM   2416 C CB  . LYS A 1 409 ? -19.445 4.381   49.979  1 27.98 ? 658  LYS A CB  1 
ATOM   2417 C CG  . LYS A 1 409 ? -20.874 4.687   49.542  1 34.78 ? 658  LYS A CG  1 
ATOM   2418 C CD  . LYS A 1 409 ? -21.799 4.983   50.754  1 41.18 ? 658  LYS A CD  1 
ATOM   2419 C CE  . LYS A 1 409 ? -23.256 5.154   50.357  1 46.47 ? 658  LYS A CE  1 
ATOM   2420 N NZ  . LYS A 1 409 ? -24.104 5.53    51.531  1 50.25 ? 658  LYS A NZ  1 
ATOM   2421 N N   . ALA A 1 410 ? -17.455 6.429   48.333  1 24.77 ? 659  ALA A N   1 
ATOM   2422 C CA  . ALA A 1 410 ? -17.209 7.634   47.562  1 24.77 ? 659  ALA A CA  1 
ATOM   2423 C C   . ALA A 1 410 ? -16.455 7.285   46.276  1 24.28 ? 659  ALA A C   1 
ATOM   2424 O O   . ALA A 1 410 ? -16.894 7.679   45.198  1 24.52 ? 659  ALA A O   1 
ATOM   2425 C CB  . ALA A 1 410 ? -16.424 8.666   48.387  1 24.74 ? 659  ALA A CB  1 
ATOM   2426 N N   . VAL A 1 411 ? -15.396 6.475   46.368  1 22.96 ? 660  VAL A N   1 
ATOM   2427 C CA  . VAL A 1 411 ? -14.615 6.057   45.201  1 23.16 ? 660  VAL A CA  1 
ATOM   2428 C C   . VAL A 1 411 ? -15.455 5.275   44.196  1 23.5  ? 660  VAL A C   1 
ATOM   2429 O O   . VAL A 1 411 ? -15.326 5.489   42.98   1 24.36 ? 660  VAL A O   1 
ATOM   2430 C CB  . VAL A 1 411 ? -13.347 5.289   45.613  1 24.03 ? 660  VAL A CB  1 
ATOM   2431 C CG1 . VAL A 1 411 ? -12.497 4.95    44.39   1 24.41 ? 660  VAL A CG1 1 
ATOM   2432 C CG2 . VAL A 1 411 ? -12.542 6.105   46.621  1 24.31 ? 660  VAL A CG2 1 
ATOM   2433 N N   . GLU A 1 412 ? -16.324 4.399   44.691  1 22.87 ? 661  GLU A N   1 
ATOM   2434 C CA  . GLU A 1 412 ? -17.259 3.662   43.845  1 23.85 ? 661  GLU A CA  1 
ATOM   2435 C C   . GLU A 1 412 ? -18.188 4.649   43.067  1 24.74 ? 661  GLU A C   1 
ATOM   2436 O O   . GLU A 1 412 ? -18.377 4.475   41.871  1 24.89 ? 661  GLU A O   1 
ATOM   2437 C CB  . GLU A 1 412 ? -18.102 2.709   44.686  1 25.43 ? 661  GLU A CB  1 
ATOM   2438 C CG  . GLU A 1 412 ? -19.095 1.95    43.832  1 32.53 ? 661  GLU A CG  1 
ATOM   2439 C CD  . GLU A 1 412 ? -20.177 1.207   44.586  1 40.8  ? 661  GLU A CD  1 
ATOM   2440 O OE1 . GLU A 1 412 ? -20.618 1.685   45.659  1 42.54 ? 661  GLU A OE1 1 
ATOM   2441 O OE2 . GLU A 1 412 ? -20.589 0.138   44.086  1 43.93 ? 661  GLU A OE2 1 
ATOM   2442 N N   . PHE A 1 413 ? -18.716 5.695   43.734  1 25.39 ? 662  PHE A N   1 
ATOM   2443 C CA  . PHE A 1 413 ? -19.559 6.674   43.043  1 26.01 ? 662  PHE A CA  1 
ATOM   2444 C C   . PHE A 1 413 ? -18.737 7.484   42.043  1 25.88 ? 662  PHE A C   1 
ATOM   2445 O O   . PHE A 1 413 ? -19.248 7.845   40.989  1 25.9  ? 662  PHE A O   1 
ATOM   2446 C CB  . PHE A 1 413 ? -20.318 7.619   44.006  1 26.15 ? 662  PHE A CB  1 
ATOM   2447 C CG  . PHE A 1 413 ? -21.312 8.464   43.228  1 26.97 ? 662  PHE A CG  1 
ATOM   2448 C CD1 . PHE A 1 413 ? -22.419 7.881   42.622  1 27.83 ? 662  PHE A CD1 1 
ATOM   2449 C CD2 . PHE A 1 413 ? -21.076 9.812   43.002  1 28.02 ? 662  PHE A CD2 1 
ATOM   2450 C CE1 . PHE A 1 413 ? -23.29  8.641   41.829  1 28.11 ? 662  PHE A CE1 1 
ATOM   2451 C CE2 . PHE A 1 413 ? -21.938 10.565  42.194  1 28.67 ? 662  PHE A CE2 1 
ATOM   2452 C CZ  . PHE A 1 413 ? -23.043 9.975   41.627  1 27.76 ? 662  PHE A CZ  1 
ATOM   2453 N N   . PHE A 1 414 ? -17.465 7.773   42.352  1 25.72 ? 663  PHE A N   1 
ATOM   2454 C CA  . PHE A 1 414 ? -16.608 8.548   41.456  1 25.8  ? 663  PHE A CA  1 
ATOM   2455 C C   . PHE A 1 414 ? -16.51  7.95    40.079  1 26.96 ? 663  PHE A C   1 
ATOM   2456 O O   . PHE A 1 414 ? -16.37  6.73    39.929  1 26.54 ? 663  PHE A O   1 
ATOM   2457 C CB  . PHE A 1 414 ? -15.191 8.698   42.007  1 25.39 ? 663  PHE A CB  1 
ATOM   2458 C CG  . PHE A 1 414 ? -14.986 9.658   43.154  1 25.2  ? 663  PHE A CG  1 
ATOM   2459 C CD1 . PHE A 1 414 ? -16.051 10.361  43.694  1 25.63 ? 663  PHE A CD1 1 
ATOM   2460 C CD2 . PHE A 1 414 ? -13.735 9.832   43.713  1 25.46 ? 663  PHE A CD2 1 
ATOM   2461 C CE1 . PHE A 1 414 ? -15.873 11.171  44.8    1 25.89 ? 663  PHE A CE1 1 
ATOM   2462 C CE2 . PHE A 1 414 ? -13.549 10.707  44.767  1 26.05 ? 663  PHE A CE2 1 
ATOM   2463 C CZ  . PHE A 1 414 ? -14.62  11.355  45.314  1 25.78 ? 663  PHE A CZ  1 
ATOM   2464 N N   . ASP A 1 415 ? -16.616 8.809   39.06   1 27.24 ? 664  ASP A N   1 
ATOM   2465 C CA  . ASP A 1 415 ? -16.499 8.366   37.681  1 27.78 ? 664  ASP A CA  1 
ATOM   2466 C C   . ASP A 1 415 ? -15.008 8.228   37.318  1 28.09 ? 664  ASP A C   1 
ATOM   2467 O O   . ASP A 1 415 ? -14.153 8.493   38.174  1 27.76 ? 664  ASP A O   1 
ATOM   2468 C CB  . ASP A 1 415 ? -17.261 9.315   36.73   1 29.68 ? 664  ASP A CB  1 
ATOM   2469 C CG  . ASP A 1 415 ? -16.733 10.733  36.656  1 35.37 ? 664  ASP A CG  1 
ATOM   2470 O OD1 . ASP A 1 415 ? -15.706 11.017  37.279  1 34.29 ? 664  ASP A OD1 1 
ATOM   2471 O OD2 . ASP A 1 415 ? -17.343 11.552  35.95   1 41.16 ? 664  ASP A OD2 1 
ATOM   2472 N N   . GLU A 1 416 ? -14.666 7.817   36.061  1 28.76 ? 665  GLU A N   1 
ATOM   2473 C CA  . GLU A 1 416 ? -13.254 7.66    35.694  1 29.82 ? 665  GLU A CA  1 
ATOM   2474 C C   . GLU A 1 416 ? -12.446 8.933   35.915  1 30.43 ? 665  GLU A C   1 
ATOM   2475 O O   . GLU A 1 416 ? -11.37  8.868   36.523  1 30.04 ? 665  GLU A O   1 
ATOM   2476 C CB  . GLU A 1 416 ? -13.082 7.123   34.269  1 33.09 ? 665  GLU A CB  1 
ATOM   2477 C CG  . GLU A 1 416 ? -11.624 6.949   33.843  1 38.73 ? 665  GLU A CG  1 
ATOM   2478 C CD  . GLU A 1 416 ? -10.801 5.82    34.451  1 44.99 ? 665  GLU A CD  1 
ATOM   2479 O OE1 . GLU A 1 416 ? -11.31  5.076   35.321  1 43.01 ? 665  GLU A OE1 1 
ATOM   2480 O OE2 . GLU A 1 416 ? -9.632  5.669   34.03   1 50.11 ? 665  GLU A OE2 1 
ATOM   2481 N N   . GLU A 1 417 ? -13.015 10.104  35.52   1 30.75 ? 666  GLU A N   1 
ATOM   2482 C CA  . GLU A 1 417 ? -12.335 11.386  35.719  1 32.31 ? 666  GLU A CA  1 
ATOM   2483 C C   . GLU A 1 417 ? -12.019 11.68   37.198  1 31.08 ? 666  GLU A C   1 
ATOM   2484 O O   . GLU A 1 417 ? -10.885 12.032  37.532  1 31.08 ? 666  GLU A O   1 
ATOM   2485 C CB  . GLU A 1 417 ? -13.145 12.542  35.09   1 37.81 ? 666  GLU A CB  1 
ATOM   2486 C CG  . GLU A 1 417 ? -12.287 13.747  34.734  1 48    ? 666  GLU A CG  1 
ATOM   2487 C CD  . GLU A 1 417 ? -12.29  14.942  35.677  1 60.53 ? 666  GLU A CD  1 
ATOM   2488 O OE1 . GLU A 1 417 ? -12.903 14.86   36.769  1 62.26 ? 666  GLU A OE1 1 
ATOM   2489 O OE2 . GLU A 1 417 ? -11.672 15.971  35.312  1 64.46 ? 666  GLU A OE2 1 
ATOM   2490 N N   . ARG A 1 418 ? -13.018 11.544  38.077  1 30.05 ? 667  ARG A N   1 
ATOM   2491 C CA  . ARG A 1 418 ? -12.815 11.767  39.497  1 29.59 ? 667  ARG A CA  1 
ATOM   2492 C C   . ARG A 1 418 ? -11.811 10.763  40.103  1 28.88 ? 667  ARG A C   1 
ATOM   2493 O O   . ARG A 1 418 ? -10.953 11.168  40.882  1 28.27 ? 667  ARG A O   1 
ATOM   2494 C CB  . ARG A 1 418 ? -14.155 11.737  40.232  1 31.07 ? 667  ARG A CB  1 
ATOM   2495 C CG  . ARG A 1 418 ? -15.015 12.975  39.959  1 31.93 ? 667  ARG A CG  1 
ATOM   2496 C CD  . ARG A 1 418 ? -16.414 12.752  40.469  1 33.55 ? 667  ARG A CD  1 
ATOM   2497 N NE  . ARG A 1 418 ? -17.152 13.998  40.649  1 34.04 ? 667  ARG A NE  1 
ATOM   2498 C CZ  . ARG A 1 418 ? -18.308 14.093  41.303  1 36.2  ? 667  ARG A CZ  1 
ATOM   2499 N NH1 . ARG A 1 418 ? -18.871 13.009  41.839  1 35.06 ? 667  ARG A NH1 1 
ATOM   2500 N NH2 . ARG A 1 418 ? -18.897 15.274  41.454  1 35.26 ? 667  ARG A NH2 1 
ATOM   2501 N N   . ARG A 1 419 ? -11.877 9.47    39.71   1 28.36 ? 668  ARG A N   1 
ATOM   2502 C CA  . ARG A 1 419 ? -10.922 8.476   40.212  1 28.07 ? 668  ARG A CA  1 
ATOM   2503 C C   . ARG A 1 419 ? -9.5    8.824   39.789  1 29.29 ? 668  ARG A C   1 
ATOM   2504 O O   . ARG A 1 419 ? -8.577  8.622   40.569  1 29.7  ? 668  ARG A O   1 
ATOM   2505 C CB  . ARG A 1 419 ? -11.285 7.051   39.74   1 26.7  ? 668  ARG A CB  1 
ATOM   2506 C CG  . ARG A 1 419 ? -12.464 6.449   40.502  1 25.23 ? 668  ARG A CG  1 
ATOM   2507 C CD  . ARG A 1 419 ? -12.786 5.027   40.057  1 25.32 ? 668  ARG A CD  1 
ATOM   2508 N NE  . ARG A 1 419 ? -14.105 4.593   40.554  1 25.49 ? 668  ARG A NE  1 
ATOM   2509 C CZ  . ARG A 1 419 ? -14.717 3.473   40.179  1 24.9  ? 668  ARG A CZ  1 
ATOM   2510 N NH1 . ARG A 1 419 ? -14.124 2.633   39.335  1 22.64 ? 668  ARG A NH1 1 
ATOM   2511 N NH2 . ARG A 1 419 ? -15.933 3.192   40.63   1 23.69 ? 668  ARG A NH2 1 
ATOM   2512 N N   . ALA A 1 420 ? -9.316  9.345   38.573  1 29.94 ? 669  ALA A N   1 
ATOM   2513 C CA  . ALA A 1 420 ? -7.982  9.747   38.113  1 31.17 ? 669  ALA A CA  1 
ATOM   2514 C C   . ALA A 1 420 ? -7.487  10.928  38.932  1 32.27 ? 669  ALA A C   1 
ATOM   2515 O O   . ALA A 1 420 ? -6.335  10.916  39.375  1 33.33 ? 669  ALA A O   1 
ATOM   2516 C CB  . ALA A 1 420 ? -8.016  10.103  36.638  1 31.81 ? 669  ALA A CB  1 
ATOM   2517 N N   . ARG A 1 421 ? -8.372  11.898  39.228  1 31.92 ? 670  ARG A N   1 
ATOM   2518 C CA  . ARG A 1 421 ? -8.013  13.055  40.063  1 32.09 ? 670  ARG A CA  1 
ATOM   2519 C C   . ARG A 1 421 ? -7.602  12.601  41.451  1 31.6  ? 670  ARG A C   1 
ATOM   2520 O O   . ARG A 1 421 ? -6.601  13.096  41.99   1 31.77 ? 670  ARG A O   1 
ATOM   2521 C CB  . ARG A 1 421 ? -9.16   14.076  40.141  1 34    ? 670  ARG A CB  1 
ATOM   2522 C CG  . ARG A 1 421 ? -9.287  14.913  38.871  1 38.5  ? 670  ARG A CG  1 
ATOM   2523 C CD  . ARG A 1 421 ? -10.023 16.218  39.109  1 43.27 ? 670  ARG A CD  1 
ATOM   2524 N NE  . ARG A 1 421 ? -11.461 16.091  38.868  1 47.76 ? 670  ARG A NE  1 
ATOM   2525 C CZ  . ARG A 1 421 ? -12.401 16.356  39.77   1 50.44 ? 670  ARG A CZ  1 
ATOM   2526 N NH1 . ARG A 1 421 ? -12.067 16.783  40.982  1 51.68 ? 670  ARG A NH1 1 
ATOM   2527 N NH2 . ARG A 1 421 ? -13.681 16.212  39.464  1 49.73 ? 670  ARG A NH2 1 
ATOM   2528 N N   . LEU A 1 422 ? -8.353  11.63   42.021  1 30.54 ? 671  LEU A N   1 
ATOM   2529 C CA  . LEU A 1 422 ? -8.041  11.062  43.328  1 29.86 ? 671  LEU A CA  1 
ATOM   2530 C C   . LEU A 1 422 ? -6.699  10.338  43.319  1 30.23 ? 671  LEU A C   1 
ATOM   2531 O O   . LEU A 1 422 ? -5.877  10.578  44.199  1 30.87 ? 671  LEU A O   1 
ATOM   2532 C CB  . LEU A 1 422 ? -9.161  10.116  43.805  1 29.61 ? 671  LEU A CB  1 
ATOM   2533 C CG  . LEU A 1 422 ? -8.928  9.459   45.17   1 30.69 ? 671  LEU A CG  1 
ATOM   2534 C CD1 . LEU A 1 422 ? -8.662  10.511  46.284  1 31.32 ? 671  LEU A CD1 1 
ATOM   2535 C CD2 . LEU A 1 422 ? -10.086 8.561   45.55   1 30.32 ? 671  LEU A CD2 1 
ATOM   2536 N N   . LEU A 1 423 ? -6.467  9.463   42.34   1 30.9  ? 672  LEU A N   1 
ATOM   2537 C CA  . LEU A 1 423 ? -5.211  8.735   42.226  1 32.64 ? 672  LEU A CA  1 
ATOM   2538 C C   . LEU A 1 423 ? -4.026  9.699   42.056  1 34.91 ? 672  LEU A C   1 
ATOM   2539 O O   . LEU A 1 423 ? -3.006  9.526   42.728  1 35.18 ? 672  LEU A O   1 
ATOM   2540 C CB  . LEU A 1 423 ? -5.26   7.717   41.079  1 32.52 ? 672  LEU A CB  1 
ATOM   2541 C CG  . LEU A 1 423 ? -4.066  6.753   40.984  1 33.77 ? 672  LEU A CG  1 
ATOM   2542 C CD1 . LEU A 1 423 ? -3.835  5.998   42.312  1 33.79 ? 672  LEU A CD1 1 
ATOM   2543 C CD2 . LEU A 1 423 ? -4.239  5.786   39.85   1 34.46 ? 672  LEU A CD2 1 
ATOM   2544 N N   . GLN A 1 424 ? -4.187  10.747  41.229  1 36.2  ? 673  GLN A N   1 
ATOM   2545 C CA  . GLN A 1 424 ? -3.134  11.755  41.023  1 38.15 ? 673  GLN A CA  1 
ATOM   2546 C C   . GLN A 1 424 ? -2.856  12.533  42.306  1 37.82 ? 673  GLN A C   1 
ATOM   2547 O O   . GLN A 1 424 ? -1.696  12.729  42.664  1 37.94 ? 673  GLN A O   1 
ATOM   2548 C CB  . GLN A 1 424 ? -3.513  12.72   39.895  1 42.39 ? 673  GLN A CB  1 
ATOM   2549 C CG  . GLN A 1 424 ? -2.41   13.735  39.59   1 49.6  ? 673  GLN A CG  1 
ATOM   2550 C CD  . GLN A 1 424 ? -2.19   13.844  38.109  1 57.03 ? 673  GLN A CD  1 
ATOM   2551 O OE1 . GLN A 1 424 ? -2.375  14.905  37.509  1 61.24 ? 673  GLN A OE1 1 
ATOM   2552 N NE2 . GLN A 1 424 ? -1.797  12.748  37.483  1 57.32 ? 673  GLN A NE2 1 
ATOM   2553 N N   . PHE A 1 425 ? -3.921  12.91   43.035  1 37.14 ? 674  PHE A N   1 
ATOM   2554 C CA  . PHE A 1 425 ? -3.824  13.61   44.305  1 36.93 ? 674  PHE A CA  1 
ATOM   2555 C C   . PHE A 1 425 ? -2.995  12.823  45.32   1 37.51 ? 674  PHE A C   1 
ATOM   2556 O O   . PHE A 1 425 ? -2.121  13.398  45.978  1 38.17 ? 674  PHE A O   1 
ATOM   2557 C CB  . PHE A 1 425 ? -5.237  13.869  44.885  1 36.73 ? 674  PHE A CB  1 
ATOM   2558 C CG  . PHE A 1 425 ? -5.27   14.46   46.284  1 37.42 ? 674  PHE A CG  1 
ATOM   2559 C CD1 . PHE A 1 425 ? -4.857  15.76   46.516  1 38.25 ? 674  PHE A CD1 1 
ATOM   2560 C CD2 . PHE A 1 425 ? -5.769  13.734  47.35   1 38.36 ? 674  PHE A CD2 1 
ATOM   2561 C CE1 . PHE A 1 425 ? -4.893  16.304  47.797  1 38.76 ? 674  PHE A CE1 1 
ATOM   2562 C CE2 . PHE A 1 425 ? -5.806  14.281  48.631  1 39.18 ? 674  PHE A CE2 1 
ATOM   2563 C CZ  . PHE A 1 425 ? -5.37   15.564  48.845  1 38.79 ? 674  PHE A CZ  1 
ATOM   2564 N N   . VAL A 1 426 ? -3.278  11.516  45.478  1 36.45 ? 675  VAL A N   1 
ATOM   2565 C CA  . VAL A 1 426 ? -2.58   10.71   46.47   1 36.43 ? 675  VAL A CA  1 
ATOM   2566 C C   . VAL A 1 426 ? -1.197  10.189  46.024  1 36.79 ? 675  VAL A C   1 
ATOM   2567 O O   . VAL A 1 426 ? -0.317  10.053  46.865  1 37.16 ? 675  VAL A O   1 
ATOM   2568 C CB  . VAL A 1 426 ? -3.487  9.538   46.941  1 36.7  ? 675  VAL A CB  1 
ATOM   2569 C CG1 . VAL A 1 426 ? -2.794  8.694   48.01   1 37.04 ? 675  VAL A CG1 1 
ATOM   2570 C CG2 . VAL A 1 426 ? -4.825  10.055  47.458  1 36.71 ? 675  VAL A CG2 1 
ATOM   2571 N N   . THR A 1 427 ? -1.007  9.871   44.732  1 36.97 ? 676  THR A N   1 
ATOM   2572 C CA  . THR A 1 427 ? 0.225   9.228   44.281  1 37.78 ? 676  THR A CA  1 
ATOM   2573 C C   . THR A 1 427 ? 1.151   10.058  43.399  1 39.33 ? 676  THR A C   1 
ATOM   2574 O O   . THR A 1 427 ? 2.316   9.701   43.25   1 40.33 ? 676  THR A O   1 
ATOM   2575 C CB  . THR A 1 427 ? -0.104  7.902   43.563  1 37.94 ? 676  THR A CB  1 
ATOM   2576 O OG1 . THR A 1 427 ? -0.649  8.169   42.268  1 39.2  ? 676  THR A OG1 1 
ATOM   2577 C CG2 . THR A 1 427 ? -1.052  7.005   44.377  1 37.83 ? 676  THR A CG2 1 
ATOM   2578 N N   . GLY A 1 428 ? 0.633   11.106  42.787  1 39.33 ? 677  GLY A N   1 
ATOM   2579 C CA  . GLY A 1 428 ? 1.402   11.92   41.85   1 39.44 ? 677  GLY A CA  1 
ATOM   2580 C C   . GLY A 1 428 ? 1.133   11.556  40.399  1 39.65 ? 677  GLY A C   1 
ATOM   2581 O O   . GLY A 1 428 ? 1.579   12.247  39.482  1 40.06 ? 677  GLY A O   1 
ATOM   2582 N N   . SER A 1 429 ? 0.377   10.479  40.164  1 38.73 ? 678  SER A N   1 
ATOM   2583 C CA  . SER A 1 429 ? 0.075   10.015  38.828  1 38.32 ? 678  SER A CA  1 
ATOM   2584 C C   . SER A 1 429 ? -1.273  9.329   38.792  1 38.09 ? 678  SER A C   1 
ATOM   2585 O O   . SER A 1 429 ? -1.685  8.73    39.789  1 38.45 ? 678  SER A O   1 
ATOM   2586 C CB  . SER A 1 429 ? 1.157   9.04    38.366  1 39.03 ? 678  SER A CB  1 
ATOM   2587 O OG  . SER A 1 429 ? 0.897   8.528   37.068  1 41.42 ? 678  SER A OG  1 
ATOM   2588 N N   . SER A 1 430 ? -1.962  9.421   37.646  1 37.46 ? 679  SER A N   1 
ATOM   2589 C CA  . SER A 1 430 ? -3.233  8.737   37.418  1 37.39 ? 679  SER A CA  1 
ATOM   2590 C C   . SER A 1 430 ? -3.013  7.44    36.577  1 36.75 ? 679  SER A C   1 
ATOM   2591 O O   . SER A 1 430 ? -3.972  6.915   35.997  1 36.8  ? 679  SER A O   1 
ATOM   2592 C CB  . SER A 1 430 ? -4.213  9.66    36.697  1 39.6  ? 679  SER A CB  1 
ATOM   2593 O OG  . SER A 1 430 ? -3.894  9.804   35.319  1 43.27 ? 679  SER A OG  1 
ATOM   2594 N N   . ARG A 1 431 ? -1.757  6.971   36.454  1 36.15 ? 680  ARG A N   1 
ATOM   2595 C CA  . ARG A 1 431 ? -1.432  5.788   35.671  1 36.2  ? 680  ARG A CA  1 
ATOM   2596 C C   . ARG A 1 431 ? -1.515  4.549   36.577  1 35    ? 680  ARG A C   1 
ATOM   2597 O O   . ARG A 1 431 ? -0.838  4.505   37.605  1 34.73 ? 680  ARG A O   1 
ATOM   2598 C CB  . ARG A 1 431 ? -0.016  5.912   35.081  1 38.11 ? 680  ARG A CB  1 
ATOM   2599 C CG  . ARG A 1 431 ? 0.387   4.687   34.261  1 40.73 ? 680  ARG A CG  1 
ATOM   2600 C CD  . ARG A 1 431 ? 1.851   4.655   33.86   1 42.53 ? 680  ARG A CD  1 
ATOM   2601 N NE  . ARG A 1 431 ? 2.132   3.449   33.069  1 43.6  ? 680  ARG A NE  1 
ATOM   2602 C CZ  . ARG A 1 431 ? 2.485   2.278   33.595  1 42.78 ? 680  ARG A CZ  1 
ATOM   2603 N NH1 . ARG A 1 431 ? 2.64    2.152   34.909  1 40.38 ? 680  ARG A NH1 1 
ATOM   2604 N NH2 . ARG A 1 431 ? 2.692   1.228   32.812  1 42.55 ? 680  ARG A NH2 1 
ATOM   2605 N N   . VAL A 1 432 ? -2.357  3.571   36.216  1 34.26 ? 681  VAL A N   1 
ATOM   2606 C CA  . VAL A 1 432 ? -2.468  2.35    37.028  1 33.59 ? 681  VAL A CA  1 
ATOM   2607 C C   . VAL A 1 432 ? -1.556  1.339   36.402  1 32.89 ? 681  VAL A C   1 
ATOM   2608 O O   . VAL A 1 432 ? -1.704  1.06    35.215  1 32.74 ? 681  VAL A O   1 
ATOM   2609 C CB  . VAL A 1 432 ? -3.918  1.806   37.11   1 33.62 ? 681  VAL A CB  1 
ATOM   2610 C CG1 . VAL A 1 432 ? -3.968  0.488   37.896  1 33.58 ? 681  VAL A CG1 1 
ATOM   2611 C CG2 . VAL A 1 432 ? -4.85   2.835   37.729  1 33.63 ? 681  VAL A CG2 1 
ATOM   2612 N N   . PRO A 1 433 ? -0.599  0.771   37.148  1 33.19 ? 682  PRO A N   1 
ATOM   2613 C CA  . PRO A 1 433 ? 0.293   -0.247  36.54   1 33.9  ? 682  PRO A CA  1 
ATOM   2614 C C   . PRO A 1 433 ? -0.477  -1.38   35.862  1 35    ? 682  PRO A C   1 
ATOM   2615 O O   . PRO A 1 433 ? -1.64   -1.619  36.198  1 34.26 ? 682  PRO A O   1 
ATOM   2616 C CB  . PRO A 1 433 ? 1.121   -0.77   37.72   1 34.31 ? 682  PRO A CB  1 
ATOM   2617 C CG  . PRO A 1 433 ? 1.015   0.283   38.778  1 34.49 ? 682  PRO A CG  1 
ATOM   2618 C CD  . PRO A 1 433 ? -0.287  1.012   38.571  1 32.61 ? 682  PRO A CD  1 
ATOM   2619 N N   . LEU A 1 434 ? 0.141   -2.041  34.88   1 36.26 ? 683  LEU A N   1 
ATOM   2620 C CA  . LEU A 1 434 ? -0.516  -3.125  34.157  1 37.49 ? 683  LEU A CA  1 
ATOM   2621 C C   . LEU A 1 434 ? -0.913  -4.298  35.062  1 37.62 ? 683  LEU A C   1 
ATOM   2622 O O   . LEU A 1 434 ? -1.872  -4.989  34.752  1 38.34 ? 683  LEU A O   1 
ATOM   2623 C CB  . LEU A 1 434 ? 0.322   -3.583  32.953  1 38.68 ? 683  LEU A CB  1 
ATOM   2624 C CG  . LEU A 1 434 ? 0.394   -2.58   31.757  1 40.98 ? 683  LEU A CG  1 
ATOM   2625 C CD1 . LEU A 1 434 ? 1.142   -3.197  30.571  1 41.74 ? 683  LEU A CD1 1 
ATOM   2626 C CD2 . LEU A 1 434 ? -1.002  -2.194  31.271  1 41.81 ? 683  LEU A CD2 1 
ATOM   2627 N N   . GLN A 1 435 ? -0.236  -4.475  36.2    1 37.11 ? 684  GLN A N   1 
ATOM   2628 C CA  . GLN A 1 435 ? -0.59   -5.514  37.173  1 37.55 ? 684  GLN A CA  1 
ATOM   2629 C C   . GLN A 1 435 ? -1.57   -5.024  38.269  1 35.99 ? 684  GLN A C   1 
ATOM   2630 O O   . GLN A 1 435 ? -1.897  -5.76   39.202  1 35.63 ? 684  GLN A O   1 
ATOM   2631 C CB  . GLN A 1 435 ? 0.671   -6.144  37.778  1 41.08 ? 684  GLN A CB  1 
ATOM   2632 C CG  . GLN A 1 435 ? 1.353   -7.094  36.785  1 48.79 ? 684  GLN A CG  1 
ATOM   2633 C CD  . GLN A 1 435 ? 2.865   -7      36.781  1 59.18 ? 684  GLN A CD  1 
ATOM   2634 O OE1 . GLN A 1 435 ? 3.575   -8.019  36.671  1 62.6  ? 684  GLN A OE1 1 
ATOM   2635 N NE2 . GLN A 1 435 ? 3.403   -5.782  36.889  1 60.89 ? 684  GLN A NE2 1 
ATOM   2636 N N   . GLY A 1 436 ? -2.059  -3.797  38.125  1 34.24 ? 685  GLY A N   1 
ATOM   2637 C CA  . GLY A 1 436 ? -3.001  -3.231  39.065  1 32.86 ? 685  GLY A CA  1 
ATOM   2638 C C   . GLY A 1 436 ? -2.341  -2.583  40.247  1 30.72 ? 685  GLY A C   1 
ATOM   2639 O O   . GLY A 1 436 ? -1.129  -2.367  40.254  1 30.23 ? 685  GLY A O   1 
ATOM   2640 N N   . PHE A 1 437 ? -3.156  -2.313  41.273  1 29.47 ? 686  PHE A N   1 
ATOM   2641 C CA  . PHE A 1 437 ? -2.787  -1.607  42.49   1 29.24 ? 686  PHE A CA  1 
ATOM   2642 C C   . PHE A 1 437 ? -1.819  -2.348  43.407  1 29.84 ? 686  PHE A C   1 
ATOM   2643 O O   . PHE A 1 437 ? -1.165  -1.718  44.237  1 28.98 ? 686  PHE A O   1 
ATOM   2644 C CB  . PHE A 1 437 ? -4.045  -1.209  43.25   1 28.41 ? 686  PHE A CB  1 
ATOM   2645 C CG  . PHE A 1 437 ? -4.693  0.012   42.659  1 28.21 ? 686  PHE A CG  1 
ATOM   2646 C CD1 . PHE A 1 437 ? -5.609  -0.101  41.631  1 28.73 ? 686  PHE A CD1 1 
ATOM   2647 C CD2 . PHE A 1 437 ? -4.348  1.276   43.095  1 28.71 ? 686  PHE A CD2 1 
ATOM   2648 C CE1 . PHE A 1 437 ? -6.194  1.027   41.075  1 29    ? 686  PHE A CE1 1 
ATOM   2649 C CE2 . PHE A 1 437 ? -4.937  2.398   42.542  1 29.24 ? 686  PHE A CE2 1 
ATOM   2650 C CZ  . PHE A 1 437 ? -5.867  2.262   41.544  1 28.83 ? 686  PHE A CZ  1 
ATOM   2651 N N   . LYS A 1 438 ? -1.7    -3.673  43.24   1 30.98 ? 687  LYS A N   1 
ATOM   2652 C CA  . LYS A 1 438 ? -0.73   -4.437  44.035  1 32.72 ? 687  LYS A CA  1 
ATOM   2653 C C   . LYS A 1 438 ? 0.717   -4.062  43.635  1 32.91 ? 687  LYS A C   1 
ATOM   2654 O O   . LYS A 1 438 ? 1.622   -4.254  44.441  1 32.28 ? 687  LYS A O   1 
ATOM   2655 C CB  . LYS A 1 438 ? -0.948  -5.956  43.898  1 35.26 ? 687  LYS A CB  1 
ATOM   2656 C CG  . LYS A 1 438 ? -0.638  -6.498  42.528  1 40.72 ? 687  LYS A CG  1 
ATOM   2657 C CD  . LYS A 1 438 ? -0.51   -8.026  42.538  1 46.21 ? 687  LYS A CD  1 
ATOM   2658 C CE  . LYS A 1 438 ? -0.29   -8.581  41.141  1 50.75 ? 687  LYS A CE  1 
ATOM   2659 N NZ  . LYS A 1 438 ? -1.503  -8.449  40.269  1 53.28 ? 687  LYS A NZ  1 
ATOM   2660 N N   . ALA A 1 439 ? 0.907   -3.522  42.406  1 33.27 ? 688  ALA A N   1 
ATOM   2661 C CA  . ALA A 1 439 ? 2.183   -3.085  41.846  1 35.09 ? 688  ALA A CA  1 
ATOM   2662 C C   . ALA A 1 439 ? 2.423   -1.561  41.981  1 37.19 ? 688  ALA A C   1 
ATOM   2663 O O   . ALA A 1 439 ? 3.364   -1.045  41.38   1 37.55 ? 688  ALA A O   1 
ATOM   2664 C CB  . ALA A 1 439 ? 2.274   -3.505  40.378  1 34.52 ? 688  ALA A CB  1 
ATOM   2665 N N   . LEU A 1 440 ? 1.608   -0.855  42.79   1 38.36 ? 689  LEU A N   1 
ATOM   2666 C CA  . LEU A 1 440 ? 1.746   0.585   42.994  1 39.97 ? 689  LEU A CA  1 
ATOM   2667 C C   . LEU A 1 440 ? 3.106   0.88    43.631  1 42.55 ? 689  LEU A C   1 
ATOM   2668 O O   . LEU A 1 440 ? 3.551   0.152   44.517  1 41.77 ? 689  LEU A O   1 
ATOM   2669 C CB  . LEU A 1 440 ? 0.622   1.121   43.887  1 39.48 ? 689  LEU A CB  1 
ATOM   2670 C CG  . LEU A 1 440 ? 0.115   2.505   43.528  1 40.74 ? 689  LEU A CG  1 
ATOM   2671 C CD1 . LEU A 1 440 ? -0.596  2.482   42.2    1 41.09 ? 689  LEU A CD1 1 
ATOM   2672 C CD2 . LEU A 1 440 ? -0.833  3.041   44.598  1 41.19 ? 689  LEU A CD2 1 
ATOM   2673 N N   . GLN A 1 441 ? 3.771   1.934   43.156  1 45.16 ? 690  GLN A N   1 
ATOM   2674 C CA  . GLN A 1 441 ? 5.093   2.281   43.66   1 48.32 ? 690  GLN A CA  1 
ATOM   2675 C C   . GLN A 1 441 ? 5.19    3.692   44.17   1 50.88 ? 690  GLN A C   1 
ATOM   2676 O O   . GLN A 1 441 ? 4.572   4.611   43.623  1 51.09 ? 690  GLN A O   1 
ATOM   2677 C CB  . GLN A 1 441 ? 6.158   2.057   42.582  1 50.4  ? 690  GLN A CB  1 
ATOM   2678 C CG  . GLN A 1 441 ? 6.233   0.616   42.124  1 54.27 ? 690  GLN A CG  1 
ATOM   2679 C CD  . GLN A 1 441 ? 7.601   0.293   41.643  1 59.83 ? 690  GLN A CD  1 
ATOM   2680 O OE1 . GLN A 1 441 ? 8.598   0.707   42.239  1 63.15 ? 690  GLN A OE1 1 
ATOM   2681 N NE2 . GLN A 1 441 ? 7.683   -0.46   40.563  1 59.92 ? 690  GLN A NE2 1 
ATOM   2682 N N   . GLY A 1 442 ? 5.985   3.843   45.221  1 52.44 ? 691  GLY A N   1 
ATOM   2683 C CA  . GLY A 1 442 ? 6.269   5.12    45.849  1 54.3  ? 691  GLY A CA  1 
ATOM   2684 C C   . GLY A 1 442 ? 7.635   5.635   45.44   1 56.28 ? 691  GLY A C   1 
ATOM   2685 O O   . GLY A 1 442 ? 8.098   5.379   44.317  1 56.41 ? 691  GLY A O   1 
ATOM   2686 N N   . ALA A 1 443 ? 8.294   6.375   46.352  1 57.17 ? 692  ALA A N   1 
ATOM   2687 C CA  . ALA A 1 443 ? 9.602   6.948   46.053  1 58.02 ? 692  ALA A CA  1 
ATOM   2688 C C   . ALA A 1 443 ? 10.724  5.887   46.049  1 57.98 ? 692  ALA A C   1 
ATOM   2689 O O   . ALA A 1 443 ? 11.392  5.726   45.023  1 58.23 ? 692  ALA A O   1 
ATOM   2690 C CB  . ALA A 1 443 ? 9.914   8.107   47.01   1 58.37 ? 692  ALA A CB  1 
ATOM   2691 N N   . ALA A 1 444 ? 10.885  5.128   47.159  1 57.39 ? 693  ALA A N   1 
ATOM   2692 C CA  . ALA A 1 444 ? 11.917  4.104   47.29   1 57.3  ? 693  ALA A CA  1 
ATOM   2693 C C   . ALA A 1 444 ? 11.71   2.89    46.369  1 56.77 ? 693  ALA A C   1 
ATOM   2694 O O   . ALA A 1 444 ? 12.655  2.45    45.718  1 57.38 ? 693  ALA A O   1 
ATOM   2695 C CB  . ALA A 1 444 ? 12.035  3.658   48.744  1 57.63 ? 693  ALA A CB  1 
ATOM   2696 N N   . GLY A 1 445 ? 10.49   2.364   46.319  1 55.28 ? 694  GLY A N   1 
ATOM   2697 C CA  . GLY A 1 445 ? 10.17   1.199   45.509  1 54.15 ? 694  GLY A CA  1 
ATOM   2698 C C   . GLY A 1 445 ? 8.699   0.858   45.615  1 52.76 ? 694  GLY A C   1 
ATOM   2699 O O   . GLY A 1 445 ? 7.857   1.717   45.373  1 53.03 ? 694  GLY A O   1 
ATOM   2700 N N   . PRO A 1 446 ? 8.349   -0.38   46      1 50.76 ? 695  PRO A N   1 
ATOM   2701 C CA  . PRO A 1 446 ? 6.922   -0.734  46.106  1 49.05 ? 695  PRO A CA  1 
ATOM   2702 C C   . PRO A 1 446 ? 6.229   -0.085  47.292  1 46.39 ? 695  PRO A C   1 
ATOM   2703 O O   . PRO A 1 446 ? 6.696   -0.213  48.419  1 46.3  ? 695  PRO A O   1 
ATOM   2704 C CB  . PRO A 1 446 ? 6.93    -2.265  46.242  1 50.27 ? 695  PRO A CB  1 
ATOM   2705 C CG  . PRO A 1 446 ? 8.368   -2.699  46.045  1 51.21 ? 695  PRO A CG  1 
ATOM   2706 C CD  . PRO A 1 446 ? 9.223   -1.513  46.346  1 50.01 ? 695  PRO A CD  1 
ATOM   2707 N N   . ARG A 1 447 ? 5.093   0.585   47.051  1 44.34 ? 696  ARG A N   1 
ATOM   2708 C CA  . ARG A 1 447 ? 4.347   1.215   48.145  1 42.9  ? 696  ARG A CA  1 
ATOM   2709 C C   . ARG A 1 447 ? 2.858   1.127   47.842  1 39.97 ? 696  ARG A C   1 
ATOM   2710 O O   . ARG A 1 447 ? 2.392   1.766   46.897  1 39.15 ? 696  ARG A O   1 
ATOM   2711 C CB  . ARG A 1 447 ? 4.76    2.687   48.311  1 45.53 ? 696  ARG A CB  1 
ATOM   2712 C CG  . ARG A 1 447 ? 4.518   3.237   49.706  1 50.56 ? 696  ARG A CG  1 
ATOM   2713 C CD  . ARG A 1 447 ? 5.65    2.833   50.631  1 56.27 ? 696  ARG A CD  1 
ATOM   2714 N NE  . ARG A 1 447 ? 5.528   3.446   51.954  1 61.63 ? 696  ARG A NE  1 
ATOM   2715 C CZ  . ARG A 1 447 ? 4.795   2.949   52.947  1 65.35 ? 696  ARG A CZ  1 
ATOM   2716 N NH1 . ARG A 1 447 ? 4.104   1.827   52.776  1 65.96 ? 696  ARG A NH1 1 
ATOM   2717 N NH2 . ARG A 1 447 ? 4.735   3.576   54.115  1 65.54 ? 696  ARG A NH2 1 
ATOM   2718 N N   . LEU A 1 448 ? 2.124   0.311   48.605  1 38.05 ? 697  LEU A N   1 
ATOM   2719 C CA  . LEU A 1 448 ? 0.688   0.19    48.37   1 36.9  ? 697  LEU A CA  1 
ATOM   2720 C C   . LEU A 1 448 ? 0       1.49    48.761  1 35.6  ? 697  LEU A C   1 
ATOM   2721 O O   . LEU A 1 448 ? 0.401   2.155   49.725  1 35.51 ? 697  LEU A O   1 
ATOM   2722 C CB  . LEU A 1 448 ? 0.072   -0.964  49.175  1 36.69 ? 697  LEU A CB  1 
ATOM   2723 C CG  . LEU A 1 448 ? 0.489   -2.385  48.766  1 37.4  ? 697  LEU A CG  1 
ATOM   2724 C CD1 . LEU A 1 448 ? -0.091  -3.399  49.729  1 38.29 ? 697  LEU A CD1 1 
ATOM   2725 C CD2 . LEU A 1 448 ? 0.098   -2.683  47.367  1 37.42 ? 697  LEU A CD2 1 
ATOM   2726 N N   . PHE A 1 449 ? -1.13   1.78    48.094  1 33.77 ? 698  PHE A N   1 
ATOM   2727 C CA  . PHE A 1 449 ? -2.015  2.898   48.405  1 32.24 ? 698  PHE A CA  1 
ATOM   2728 C C   . PHE A 1 449 ? -2.414  2.775   49.896  1 31.11 ? 698  PHE A C   1 
ATOM   2729 O O   . PHE A 1 449 ? -2.632  1.656   50.364  1 31.21 ? 698  PHE A O   1 
ATOM   2730 C CB  . PHE A 1 449 ? -3.251  2.824   47.467  1 31.75 ? 698  PHE A CB  1 
ATOM   2731 C CG  . PHE A 1 449 ? -4.191  3.991   47.602  1 32.01 ? 698  PHE A CG  1 
ATOM   2732 C CD1 . PHE A 1 449 ? -5.206  3.977   48.543  1 32.34 ? 698  PHE A CD1 1 
ATOM   2733 C CD2 . PHE A 1 449 ? -4.034  5.124   46.812  1 32.71 ? 698  PHE A CD2 1 
ATOM   2734 C CE1 . PHE A 1 449 ? -6.06   5.071   48.683  1 32.99 ? 698  PHE A CE1 1 
ATOM   2735 C CE2 . PHE A 1 449 ? -4.907  6.2     46.936  1 32.85 ? 698  PHE A CE2 1 
ATOM   2736 C CZ  . PHE A 1 449 ? -5.901  6.176   47.881  1 32.31 ? 698  PHE A CZ  1 
ATOM   2737 N N   . THR A 1 450 ? -2.343  3.873   50.662  1 30.16 ? 699  THR A N   1 
ATOM   2738 C CA  . THR A 1 450 ? -2.582  3.818   52.092  1 30.75 ? 699  THR A CA  1 
ATOM   2739 C C   . THR A 1 450 ? -3.597  4.837   52.607  1 31.39 ? 699  THR A C   1 
ATOM   2740 O O   . THR A 1 450 ? -3.469  6.033   52.352  1 31.56 ? 699  THR A O   1 
ATOM   2741 C CB  . THR A 1 450 ? -1.24   4.019   52.84   1 32.94 ? 699  THR A CB  1 
ATOM   2742 O OG1 . THR A 1 450 ? -0.315  3.015   52.443  1 34.99 ? 699  THR A OG1 1 
ATOM   2743 C CG2 . THR A 1 450 ? -1.399  4.001   54.34   1 33.42 ? 699  THR A CG2 1 
ATOM   2744 N N   . ILE A 1 451 ? -4.551  4.372   53.411  1 30.81 ? 700  ILE A N   1 
ATOM   2745 C CA  . ILE A 1 451 ? -5.525  5.253   54.033  1 30.76 ? 700  ILE A CA  1 
ATOM   2746 C C   . ILE A 1 451 ? -5.081  5.358   55.458  1 31.13 ? 700  ILE A C   1 
ATOM   2747 O O   . ILE A 1 451 ? -5.018  4.349   56.139  1 30.62 ? 700  ILE A O   1 
ATOM   2748 C CB  . ILE A 1 451 ? -6.949  4.663   53.983  1 30.52 ? 700  ILE A CB  1 
ATOM   2749 C CG1 . ILE A 1 451 ? -7.44   4.463   52.534  1 31.34 ? 700  ILE A CG1 1 
ATOM   2750 C CG2 . ILE A 1 451 ? -7.909  5.503   54.798  1 30.53 ? 700  ILE A CG2 1 
ATOM   2751 C CD1 . ILE A 1 451 ? -8.765  3.633   52.466  1 32.05 ? 700  ILE A CD1 1 
ATOM   2752 N N   . HIS A 1 452 ? -4.772  6.567   55.912  1 31.91 ? 701  HIS A N   1 
ATOM   2753 C CA  . HIS A 1 452 ? -4.338  6.801   57.266  1 33.82 ? 701  HIS A CA  1 
ATOM   2754 C C   . HIS A 1 452 ? -5.325  7.726   57.965  1 34.44 ? 701  HIS A C   1 
ATOM   2755 O O   . HIS A 1 452 ? -5.389  8.908   57.635  1 34.45 ? 701  HIS A O   1 
ATOM   2756 C CB  . HIS A 1 452 ? -2.913  7.395   57.229  1 36.03 ? 701  HIS A CB  1 
ATOM   2757 C CG  . HIS A 1 452 ? -2.314  7.745   58.554  1 40.71 ? 701  HIS A CG  1 
ATOM   2758 N ND1 . HIS A 1 452 ? -1.152  8.495   58.632  1 44.28 ? 701  HIS A ND1 1 
ATOM   2759 C CD2 . HIS A 1 452 ? -2.723  7.445   59.809  1 42.9  ? 701  HIS A CD2 1 
ATOM   2760 C CE1 . HIS A 1 452 ? -0.895  8.644   59.925  1 44.91 ? 701  HIS A CE1 1 
ATOM   2761 N NE2 . HIS A 1 452 ? -1.813  8.033   60.677  1 44.79 ? 701  HIS A NE2 1 
ATOM   2762 N N   . GLN A 1 453 ? -6.099  7.205   58.927  1 35.42 ? 702  GLN A N   1 
ATOM   2763 C CA  . GLN A 1 453 ? -7.012  8.051   59.69   1 36.79 ? 702  GLN A CA  1 
ATOM   2764 C C   . GLN A 1 453 ? -6.185  8.872   60.708  1 39.63 ? 702  GLN A C   1 
ATOM   2765 O O   . GLN A 1 453 ? -5.541  8.3     61.603  1 39.37 ? 702  GLN A O   1 
ATOM   2766 C CB  . GLN A 1 453 ? -8.091  7.228   60.4    1 37.38 ? 702  GLN A CB  1 
ATOM   2767 C CG  . GLN A 1 453 ? -9.004  8.088   61.258  1 39.52 ? 702  GLN A CG  1 
ATOM   2768 C CD  . GLN A 1 453 ? -10.246 7.367   61.657  1 45.39 ? 702  GLN A CD  1 
ATOM   2769 O OE1 . GLN A 1 453 ? -10.22  6.38    62.387  1 48.12 ? 702  GLN A OE1 1 
ATOM   2770 N NE2 . GLN A 1 453 ? -11.376 7.854   61.2    1 46.57 ? 702  GLN A NE2 1 
ATOM   2771 N N   . ILE A 1 454 ? -6.162  10.207  60.54   1 41.44 ? 703  ILE A N   1 
ATOM   2772 C CA  . ILE A 1 454 ? -5.4    11.065  61.447  1 43.61 ? 703  ILE A CA  1 
ATOM   2773 C C   . ILE A 1 454 ? -6.28   11.714  62.504  1 46.62 ? 703  ILE A C   1 
ATOM   2774 O O   . ILE A 1 454 ? -7.498  11.827  62.337  1 46.88 ? 703  ILE A O   1 
ATOM   2775 C CB  . ILE A 1 454 ? -4.546  12.111  60.693  1 43.88 ? 703  ILE A CB  1 
ATOM   2776 C CG1 . ILE A 1 454 ? -5.434  13.105  59.911  1 44.86 ? 703  ILE A CG1 1 
ATOM   2777 C CG2 . ILE A 1 454 ? -3.479  11.447  59.825  1 44.15 ? 703  ILE A CG2 1 
ATOM   2778 C CD1 . ILE A 1 454 ? -4.664  14.252  59.278  1 46.15 ? 703  ILE A CD1 1 
ATOM   2779 N N   . ASP A 1 455 ? -5.664  12.131  63.61   1 48.52 ? 704  ASP A N   1 
ATOM   2780 C CA  . ASP A 1 455 ? -6.374  12.828  64.666  1 50.41 ? 704  ASP A CA  1 
ATOM   2781 C C   . ASP A 1 455 ? -6.249  14.309  64.306  1 50.87 ? 704  ASP A C   1 
ATOM   2782 O O   . ASP A 1 455 ? -5.255  14.939  64.655  1 51.81 ? 704  ASP A O   1 
ATOM   2783 C CB  . ASP A 1 455 ? -5.704  12.54   66.017  1 53.59 ? 704  ASP A CB  1 
ATOM   2784 C CG  . ASP A 1 455 ? -6.305  13.294  67.186  1 60.69 ? 704  ASP A CG  1 
ATOM   2785 O OD1 . ASP A 1 455 ? -7.544  13.491  67.194  1 62.26 ? 704  ASP A OD1 1 
ATOM   2786 O OD2 . ASP A 1 455 ? -5.538  13.681  68.097  1 63.32 ? 704  ASP A OD2 1 
ATOM   2787 N N   . ALA A 1 456 ? -7.2    14.837  63.531  1 50.11 ? 705  ALA A N   1 
ATOM   2788 C CA  . ALA A 1 456 ? -7.169  16.233  63.098  1 49.73 ? 705  ALA A CA  1 
ATOM   2789 C C   . ALA A 1 456 ? -8.595  16.856  63.088  1 49.4  ? 705  ALA A C   1 
ATOM   2790 O O   . ALA A 1 456 ? -9.571  16.146  63.369  1 49.24 ? 705  ALA A O   1 
ATOM   2791 C CB  . ALA A 1 456 ? -6.496  16.333  61.729  1 49.91 ? 705  ALA A CB  1 
ATOM   2792 N N   . CYS A 1 457 ? -8.711  18.196  62.879  1 49.24 ? 706  CYS A N   1 
ATOM   2793 C CA  . CYS A 1 457 ? -10.008 18.88   62.831  1 49.39 ? 706  CYS A CA  1 
ATOM   2794 C C   . CYS A 1 457 ? -10.807 18.323  61.642  1 48.25 ? 706  CYS A C   1 
ATOM   2795 O O   . CYS A 1 457 ? -10.264 18.205  60.544  1 47.44 ? 706  CYS A O   1 
ATOM   2796 C CB  . CYS A 1 457 ? -9.822  20.396  62.72   1 50.59 ? 706  CYS A CB  1 
ATOM   2797 S SG  . CYS A 1 457 ? -11.371 21.331  62.551  1 54.67 ? 706  CYS A SG  1 
ATOM   2798 N N   . THR A 1 458 ? -12.077 17.951  61.871  1 48.34 ? 707  THR A N   1 
ATOM   2799 C CA  . THR A 1 458 ? -12.916 17.373  60.817  1 48.95 ? 707  THR A CA  1 
ATOM   2800 C C   . THR A 1 458 ? -13.387 18.37   59.761  1 48.69 ? 707  THR A C   1 
ATOM   2801 O O   . THR A 1 458 ? -14.152 17.989  58.882  1 49.36 ? 707  THR A O   1 
ATOM   2802 C CB  . THR A 1 458 ? -14.078 16.611  61.395  1 51.05 ? 707  THR A CB  1 
ATOM   2803 O OG1 . THR A 1 458 ? -14.953 17.543  62.028  1 53    ? 707  THR A OG1 1 
ATOM   2804 C CG2 . THR A 1 458 ? -13.631 15.554  62.379  1 51.39 ? 707  THR A CG2 1 
ATOM   2805 N N   . ASN A 1 459 ? -12.957 19.629  59.834  1 47.48 ? 708  ASN A N   1 
ATOM   2806 C CA  . ASN A 1 459 ? -13.254 20.595  58.783  1 47.26 ? 708  ASN A CA  1 
ATOM   2807 C C   . ASN A 1 459 ? -12.087 20.695  57.772  1 45.59 ? 708  ASN A C   1 
ATOM   2808 O O   . ASN A 1 459 ? -12.26  21.272  56.699  1 45.49 ? 708  ASN A O   1 
ATOM   2809 C CB  . ASN A 1 459 ? -13.679 21.952  59.356  1 49.75 ? 708  ASN A CB  1 
ATOM   2810 C CG  . ASN A 1 459 ? -14.928 21.87   60.221  1 55.04 ? 708  ASN A CG  1 
ATOM   2811 O OD1 . ASN A 1 459 ? -15.089 22.624  61.188  1 57.37 ? 708  ASN A OD1 1 
ATOM   2812 N ND2 . ASN A 1 459 ? -15.843 20.947  59.915  1 56.02 ? 708  ASN A ND2 1 
ATOM   2813 N N   . ASN A 1 460 ? -10.911 20.106  58.1    1 44.14 ? 709  ASN A N   1 
ATOM   2814 C CA  . ASN A 1 460 ? -9.758  20.065  57.209  1 43.85 ? 709  ASN A CA  1 
ATOM   2815 C C   . ASN A 1 460 ? -10.063 19.116  56.066  1 42.94 ? 709  ASN A C   1 
ATOM   2816 O O   . ASN A 1 460 ? -10.823 18.167  56.223  1 43.19 ? 709  ASN A O   1 
ATOM   2817 C CB  . ASN A 1 460 ? -8.513  19.517  57.933  1 45.72 ? 709  ASN A CB  1 
ATOM   2818 C CG  . ASN A 1 460 ? -7.947  20.39   59.028  1 49.7  ? 709  ASN A CG  1 
ATOM   2819 O OD1 . ASN A 1 460 ? -8.632  21.251  59.591  1 51.52 ? 709  ASN A OD1 1 
ATOM   2820 N ND2 . ASN A 1 460 ? -6.681  20.173  59.353  1 49.55 ? 709  ASN A ND2 1 
ATOM   2821 N N   . LEU A 1 461 ? -9.44   19.356  54.934  1 42.02 ? 710  LEU A N   1 
ATOM   2822 C CA  . LEU A 1 461 ? -9.553  18.5    53.78   1 41.89 ? 710  LEU A CA  1 
ATOM   2823 C C   . LEU A 1 461 ? -8.586  17.319  53.949  1 42.74 ? 710  LEU A C   1 
ATOM   2824 O O   . LEU A 1 461 ? -7.575  17.453  54.651  1 42.56 ? 710  LEU A O   1 
ATOM   2825 C CB  . LEU A 1 461 ? -9.107  19.304  52.542  1 41.06 ? 710  LEU A CB  1 
ATOM   2826 C CG  . LEU A 1 461 ? -9.954  20.494  52.119  1 41.29 ? 710  LEU A CG  1 
ATOM   2827 C CD1 . LEU A 1 461 ? -9.469  21.036  50.788  1 41.42 ? 710  LEU A CD1 1 
ATOM   2828 C CD2 . LEU A 1 461 ? -11.436 20.138  52.037  1 41.78 ? 710  LEU A CD2 1 
ATOM   2829 N N   . PRO A 1 462 ? -8.8    16.191  53.228  1 42.7  ? 711  PRO A N   1 
ATOM   2830 C CA  . PRO A 1 462 ? -7.797  15.118  53.249  1 42.63 ? 711  PRO A CA  1 
ATOM   2831 C C   . PRO A 1 462 ? -6.44   15.633  52.745  1 42.5  ? 711  PRO A C   1 
ATOM   2832 O O   . PRO A 1 462 ? -6.384  16.516  51.88   1 42.62 ? 711  PRO A O   1 
ATOM   2833 C CB  . PRO A 1 462 ? -8.382  14.077  52.269  1 43.51 ? 711  PRO A CB  1 
ATOM   2834 C CG  . PRO A 1 462 ? -9.87   14.361  52.254  1 43.67 ? 711  PRO A CG  1 
ATOM   2835 C CD  . PRO A 1 462 ? -9.918  15.862  52.317  1 42.26 ? 711  PRO A CD  1 
ATOM   2836 N N   . LYS A 1 463 ? -5.355  15.125  53.313  1 42.18 ? 712  LYS A N   1 
ATOM   2837 C CA  . LYS A 1 463 ? -4.015  15.55   52.947  1 42.87 ? 712  LYS A CA  1 
ATOM   2838 C C   . LYS A 1 463 ? -3.26   14.405  52.286  1 42.87 ? 712  LYS A C   1 
ATOM   2839 O O   . LYS A 1 463 ? -3.367  13.276  52.736  1 42.8  ? 712  LYS A O   1 
ATOM   2840 C CB  . LYS A 1 463 ? -3.269  16.073  54.194  1 46.66 ? 712  LYS A CB  1 
ATOM   2841 C CG  . LYS A 1 463 ? -1.874  16.629  53.888  1 53.84 ? 712  LYS A CG  1 
ATOM   2842 C CD  . LYS A 1 463 ? -1.313  17.473  55.034  1 60.28 ? 712  LYS A CD  1 
ATOM   2843 C CE  . LYS A 1 463 ? 0.021   18.101  54.666  1 65.43 ? 712  LYS A CE  1 
ATOM   2844 N NZ  . LYS A 1 463 ? 0.423   19.186  55.62   1 67.76 ? 712  LYS A NZ  1 
ATOM   2845 N N   . ALA A 1 464 ? -2.531  14.675  51.203  1 43.08 ? 713  ALA A N   1 
ATOM   2846 C CA  . ALA A 1 464 ? -1.79   13.632  50.5    1 44.01 ? 713  ALA A CA  1 
ATOM   2847 C C   . ALA A 1 464 ? -0.275  13.687  50.719  1 45.47 ? 713  ALA A C   1 
ATOM   2848 O O   . ALA A 1 464 ? 0.301   14.76   50.9    1 45.5  ? 713  ALA A O   1 
ATOM   2849 C CB  . ALA A 1 464 ? -2.103  13.673  49.025  1 43.44 ? 713  ALA A CB  1 
ATOM   2850 N N   . HIS A 1 465 ? 0.363   12.512  50.695  1 45.76 ? 714  HIS A N   1 
ATOM   2851 C CA  . HIS A 1 465 ? 1.804   12.363  50.836  1 46.42 ? 714  HIS A CA  1 
ATOM   2852 C C   . HIS A 1 465 ? 2.221   11.441  49.704  1 46.89 ? 714  HIS A C   1 
ATOM   2853 O O   . HIS A 1 465 ? 2.389   10.246  49.911  1 46.89 ? 714  HIS A O   1 
ATOM   2854 C CB  . HIS A 1 465 ? 2.159   11.751  52.196  1 47.41 ? 714  HIS A CB  1 
ATOM   2855 C CG  . HIS A 1 465 ? 1.646   12.538  53.36   1 50.58 ? 714  HIS A CG  1 
ATOM   2856 N ND1 . HIS A 1 465 ? 2.266   13.705  53.772  1 52.68 ? 714  HIS A ND1 1 
ATOM   2857 C CD2 . HIS A 1 465 ? 0.587   12.298  54.166  1 52.12 ? 714  HIS A CD2 1 
ATOM   2858 C CE1 . HIS A 1 465 ? 1.57    14.135  54.812  1 53.44 ? 714  HIS A CE1 1 
ATOM   2859 N NE2 . HIS A 1 465 ? 0.559   13.313  55.097  1 53.57 ? 714  HIS A NE2 1 
ATOM   2860 N N   . THR A 1 466 ? 2.351   12.005  48.501  1 47.44 ? 715  THR A N   1 
ATOM   2861 C CA  . THR A 1 466 ? 2.643   11.315  47.251  1 48.92 ? 715  THR A CA  1 
ATOM   2862 C C   . THR A 1 466 ? 3.891   10.433  47.278  1 50.4  ? 715  THR A C   1 
ATOM   2863 O O   . THR A 1 466 ? 4.022   9.539   46.437  1 50.69 ? 715  THR A O   1 
ATOM   2864 C CB  . THR A 1 466 ? 2.698   12.323  46.113  1 50.85 ? 715  THR A CB  1 
ATOM   2865 O OG1 . THR A 1 466 ? 3.847   13.162  46.279  1 52.39 ? 715  THR A OG1 1 
ATOM   2866 C CG2 . THR A 1 466 ? 1.426   13.161  46.019  1 51.15 ? 715  THR A CG2 1 
ATOM   2867 N N   . CYS A 1 467 ? 4.794   10.667  48.237  1 51.14 ? 716  CYS A N   1 
ATOM   2868 C CA  . CYS A 1 467 ? 5.998   9.858   48.396  1 52.19 ? 716  CYS A CA  1 
ATOM   2869 C C   . CYS A 1 467 ? 5.623   8.438   48.795  1 51.31 ? 716  CYS A C   1 
ATOM   2870 O O   . CYS A 1 467 ? 6.175   7.474   48.268  1 51.43 ? 716  CYS A O   1 
ATOM   2871 C CB  . CYS A 1 467 ? 6.941   10.485  49.423  1 54.36 ? 716  CYS A CB  1 
ATOM   2872 S SG  . CYS A 1 467 ? 7.956   11.833  48.767  1 64.53 ? 716  CYS A SG  1 
ATOM   2873 N N   . PHE A 1 468 ? 4.68    8.321   49.727  1 50.09 ? 717  PHE A N   1 
ATOM   2874 C CA  . PHE A 1 468 ? 4.254   7.045   50.276  1 49.28 ? 717  PHE A CA  1 
ATOM   2875 C C   . PHE A 1 468 ? 2.863   6.612   49.803  1 45.98 ? 717  PHE A C   1 
ATOM   2876 O O   . PHE A 1 468 ? 2.275   5.748   50.449  1 45.72 ? 717  PHE A O   1 
ATOM   2877 C CB  . PHE A 1 468 ? 4.285   7.12    51.809  1 50.58 ? 717  PHE A CB  1 
ATOM   2878 C CG  . PHE A 1 468 ? 5.565   7.715   52.35   1 53.19 ? 717  PHE A CG  1 
ATOM   2879 C CD1 . PHE A 1 468 ? 6.782   7.077   52.154  1 54.83 ? 717  PHE A CD1 1 
ATOM   2880 C CD2 . PHE A 1 468 ? 5.564   8.951   52.972  1 54.62 ? 717  PHE A CD2 1 
ATOM   2881 C CE1 . PHE A 1 468 ? 7.962   7.639   52.624  1 55.96 ? 717  PHE A CE1 1 
ATOM   2882 C CE2 . PHE A 1 468 ? 6.744   9.507   53.446  1 55.83 ? 717  PHE A CE2 1 
ATOM   2883 C CZ  . PHE A 1 468 ? 7.936   8.852   53.262  1 55.85 ? 717  PHE A CZ  1 
ATOM   2884 N N   . ASN A 1 469 ? 2.313   7.238   48.725  1 43.32 ? 718  ASN A N   1 
ATOM   2885 C CA  . ASN A 1 469 ? 0.978   6.939   48.157  1 41    ? 718  ASN A CA  1 
ATOM   2886 C C   . ASN A 1 469 ? -0.069  6.921   49.268  1 38.85 ? 718  ASN A C   1 
ATOM   2887 O O   . ASN A 1 469 ? -0.874  6.003   49.362  1 38.43 ? 718  ASN A O   1 
ATOM   2888 C CB  . ASN A 1 469 ? 1.014   5.591   47.424  1 41.08 ? 718  ASN A CB  1 
ATOM   2889 C CG  . ASN A 1 469 ? 1.909   5.616   46.218  1 42.6  ? 718  ASN A CG  1 
ATOM   2890 O OD1 . ASN A 1 469 ? 2.158   6.664   45.629  1 43.62 ? 718  ASN A OD1 1 
ATOM   2891 N ND2 . ASN A 1 469 ? 2.411   4.467   45.82   1 42.35 ? 718  ASN A ND2 1 
ATOM   2892 N N   . ARG A 1 470 ? 0.001   7.908   50.154  1 37.5  ? 719  ARG A N   1 
ATOM   2893 C CA  . ARG A 1 470 ? -0.805  7.927   51.36   1 37.5  ? 719  ARG A CA  1 
ATOM   2894 C C   . ARG A 1 470 ? -1.788  9.116   51.48   1 36.99 ? 719  ARG A C   1 
ATOM   2895 O O   . ARG A 1 470 ? -1.473  10.255  51.11   1 37.41 ? 719  ARG A O   1 
ATOM   2896 C CB  . ARG A 1 470 ? 0.157   7.864   52.557  1 38.34 ? 719  ARG A CB  1 
ATOM   2897 C CG  . ARG A 1 470 ? -0.461  7.943   53.927  1 42.26 ? 719  ARG A CG  1 
ATOM   2898 C CD  . ARG A 1 470 ? 0.61    7.766   54.98   1 47.25 ? 719  ARG A CD  1 
ATOM   2899 N NE  . ARG A 1 470 ? 0.409   8.674   56.11   1 53.16 ? 719  ARG A NE  1 
ATOM   2900 C CZ  . ARG A 1 470 ? 1.29    9.585   56.512  1 57.3  ? 719  ARG A CZ  1 
ATOM   2901 N NH1 . ARG A 1 470 ? 2.451   9.723   55.88   1 57.25 ? 719  ARG A NH1 1 
ATOM   2902 N NH2 . ARG A 1 470 ? 1.011   10.376  57.543  1 58.06 ? 719  ARG A NH2 1 
ATOM   2903 N N   . ILE A 1 471 ? -2.986  8.831   51.989  1 35.19 ? 720  ILE A N   1 
ATOM   2904 C CA  . ILE A 1 471 ? -3.984  9.854   52.205  1 34.5  ? 720  ILE A CA  1 
ATOM   2905 C C   . ILE A 1 471 ? -4.312  9.907   53.687  1 34.52 ? 720  ILE A C   1 
ATOM   2906 O O   . ILE A 1 471 ? -4.512  8.875   54.327  1 34.61 ? 720  ILE A O   1 
ATOM   2907 C CB  . ILE A 1 471 ? -5.218  9.722   51.254  1 34.45 ? 720  ILE A CB  1 
ATOM   2908 C CG1 . ILE A 1 471 ? -6.192  10.906  51.399  1 35.01 ? 720  ILE A CG1 1 
ATOM   2909 C CG2 . ILE A 1 471 ? -5.943  8.378   51.389  1 34.22 ? 720  ILE A CG2 1 
ATOM   2910 C CD1 . ILE A 1 471 ? -7.189  11.028  50.209  1 35.28 ? 720  ILE A CD1 1 
ATOM   2911 N N   . ASP A 1 472 ? -4.264  11.108  54.259  1 34.12 ? 721  ASP A N   1 
ATOM   2912 C CA  . ASP A 1 472 ? -4.539  11.331  55.66   1 34.97 ? 721  ASP A CA  1 
ATOM   2913 C C   . ASP A 1 472 ? -5.937  11.86   55.778  1 35.34 ? 721  ASP A C   1 
ATOM   2914 O O   . ASP A 1 472 ? -6.262  12.882  55.185  1 35.27 ? 721  ASP A O   1 
ATOM   2915 C CB  . ASP A 1 472 ? -3.542  12.332  56.259  1 37.53 ? 721  ASP A CB  1 
ATOM   2916 C CG  . ASP A 1 472 ? -2.131  11.796  56.438  1 43.47 ? 721  ASP A CG  1 
ATOM   2917 O OD1 . ASP A 1 472 ? -1.869  10.642  56.006  1 42.95 ? 721  ASP A OD1 1 
ATOM   2918 O OD2 . ASP A 1 472 ? -1.283  12.532  56.998  1 47.04 ? 721  ASP A OD2 1 
ATOM   2919 N N   . ILE A 1 473 ? -6.768  11.165  56.538  1 35.73 ? 722  ILE A N   1 
ATOM   2920 C CA  . ILE A 1 473 ? -8.157  11.527  56.66   1 36.78 ? 722  ILE A CA  1 
ATOM   2921 C C   . ILE A 1 473 ? -8.592  11.784  58.092  1 37.26 ? 722  ILE A C   1 
ATOM   2922 O O   . ILE A 1 473 ? -8.475  10.919  58.953  1 37    ? 722  ILE A O   1 
ATOM   2923 C CB  . ILE A 1 473 ? -9.076  10.471  55.96   1 37.66 ? 722  ILE A CB  1 
ATOM   2924 C CG1 . ILE A 1 473 ? -8.554  10.069  54.565  1 38.86 ? 722  ILE A CG1 1 
ATOM   2925 C CG2 . ILE A 1 473 ? -10.487 10.978  55.843  1 38.3  ? 722  ILE A CG2 1 
ATOM   2926 C CD1 . ILE A 1 473 ? -9.313  8.869   53.924  1 40.6  ? 722  ILE A CD1 1 
ATOM   2927 N N   . PRO A 1 474 ? -9.193  12.959  58.342  1 37.5  ? 723  PRO A N   1 
ATOM   2928 C CA  . PRO A 1 474 ? -9.766  13.22   59.674  1 37.86 ? 723  PRO A CA  1 
ATOM   2929 C C   . PRO A 1 474 ? -10.976 12.317  59.947  1 38.75 ? 723  PRO A C   1 
ATOM   2930 O O   . PRO A 1 474 ? -11.59  11.791  59.01   1 39.18 ? 723  PRO A O   1 
ATOM   2931 C CB  . PRO A 1 474 ? -10.209 14.697  59.582  1 38.42 ? 723  PRO A CB  1 
ATOM   2932 C CG  . PRO A 1 474 ? -9.484  15.263  58.367  1 38.95 ? 723  PRO A CG  1 
ATOM   2933 C CD  . PRO A 1 474 ? -9.399  14.097  57.423  1 36.88 ? 723  PRO A CD  1 
ATOM   2934 N N   . PRO A 1 475 ? -11.372 12.145  61.222  1 38.62 ? 724  PRO A N   1 
ATOM   2935 C CA  . PRO A 1 475 ? -12.542 11.302  61.517  1 38.23 ? 724  PRO A CA  1 
ATOM   2936 C C   . PRO A 1 475 ? -13.896 11.964  61.193  1 38.02 ? 724  PRO A C   1 
ATOM   2937 O O   . PRO A 1 475 ? -14.666 12.263  62.1    1 38.62 ? 724  PRO A O   1 
ATOM   2938 C CB  . PRO A 1 475 ? -12.393 11.037  63.012  1 38.77 ? 724  PRO A CB  1 
ATOM   2939 C CG  . PRO A 1 475 ? -11.743 12.305  63.528  1 39.42 ? 724  PRO A CG  1 
ATOM   2940 C CD  . PRO A 1 475 ? -10.765 12.688  62.458  1 38.23 ? 724  PRO A CD  1 
ATOM   2941 N N   . TYR A 1 476 ? -14.224 12.137  59.9    1 37.1  ? 725  TYR A N   1 
ATOM   2942 C CA  . TYR A 1 476 ? -15.488 12.755  59.464  1 35.62 ? 725  TYR A CA  1 
ATOM   2943 C C   . TYR A 1 476 ? -16.696 12.064  60.06   1 35.89 ? 725  TYR A C   1 
ATOM   2944 O O   . TYR A 1 476 ? -16.727 10.846  60.165  1 36.57 ? 725  TYR A O   1 
ATOM   2945 C CB  . TYR A 1 476 ? -15.594 12.81   57.941  1 33.73 ? 725  TYR A CB  1 
ATOM   2946 C CG  . TYR A 1 476 ? -14.473 13.562  57.264  1 32.3  ? 725  TYR A CG  1 
ATOM   2947 C CD1 . TYR A 1 476 ? -14.248 14.905  57.533  1 31.88 ? 725  TYR A CD1 1 
ATOM   2948 C CD2 . TYR A 1 476 ? -13.729 12.973  56.255  1 32.74 ? 725  TYR A CD2 1 
ATOM   2949 C CE1 . TYR A 1 476 ? -13.258 15.619  56.866  1 31.93 ? 725  TYR A CE1 1 
ATOM   2950 C CE2 . TYR A 1 476 ? -12.74  13.676  55.581  1 32.9  ? 725  TYR A CE2 1 
ATOM   2951 C CZ  . TYR A 1 476 ? -12.506 15.001  55.888  1 32.57 ? 725  TYR A CZ  1 
ATOM   2952 O OH  . TYR A 1 476 ? -11.524 15.682  55.21   1 32.42 ? 725  TYR A OH  1 
ATOM   2953 N N   . GLU A 1 477 ? -17.666 12.857  60.49   1 35.28 ? 726  GLU A N   1 
ATOM   2954 C CA  . GLU A 1 477 ? -18.876 12.453  61.184  1 35.81 ? 726  GLU A CA  1 
ATOM   2955 C C   . GLU A 1 477 ? -19.908 11.719  60.321  1 35.46 ? 726  GLU A C   1 
ATOM   2956 O O   . GLU A 1 477 ? -20.779 11.021  60.858  1 35.88 ? 726  GLU A O   1 
ATOM   2957 C CB  . GLU A 1 477 ? -19.519 13.709  61.795  1 39.29 ? 726  GLU A CB  1 
ATOM   2958 C CG  . GLU A 1 477 ? -18.647 14.399  62.839  1 44.74 ? 726  GLU A CG  1 
ATOM   2959 C CD  . GLU A 1 477 ? -17.645 15.434  62.371  1 52.27 ? 726  GLU A CD  1 
ATOM   2960 O OE1 . GLU A 1 477 ? -17.453 15.588  61.144  1 51.28 ? 726  GLU A OE1 1 
ATOM   2961 O OE2 . GLU A 1 477 ? -17.035 16.091  63.247  1 57.85 ? 726  GLU A OE2 1 
ATOM   2962 N N   . SER A 1 478 ? -19.846 11.902  59.001  1 34.03 ? 727  SER A N   1 
ATOM   2963 C CA  . SER A 1 478 ? -20.818 11.25   58.114  1 33.04 ? 727  SER A CA  1 
ATOM   2964 C C   . SER A 1 478 ? -20.199 10.933  56.759  1 31.17 ? 727  SER A C   1 
ATOM   2965 O O   . SER A 1 478 ? -19.14  11.478  56.407  1 30.92 ? 727  SER A O   1 
ATOM   2966 C CB  . SER A 1 478 ? -22.057 12.131  57.942  1 34.38 ? 727  SER A CB  1 
ATOM   2967 O OG  . SER A 1 478 ? -21.737 13.303  57.209  1 36.52 ? 727  SER A OG  1 
ATOM   2968 N N   . TYR A 1 479 ? -20.866 10.045  55.978  1 30.19 ? 728  TYR A N   1 
ATOM   2969 C CA  . TYR A 1 479 ? -20.441 9.723   54.612  1 29.12 ? 728  TYR A CA  1 
ATOM   2970 C C   . TYR A 1 479 ? -20.486 11.005  53.779  1 28.41 ? 728  TYR A C   1 
ATOM   2971 O O   . TYR A 1 479 ? -19.541 11.302  53.067  1 27.31 ? 728  TYR A O   1 
ATOM   2972 C CB  . TYR A 1 479 ? -21.391 8.679   53.958  1 28.41 ? 728  TYR A CB  1 
ATOM   2973 C CG  . TYR A 1 479 ? -21.19  8.559   52.457  1 28.13 ? 728  TYR A CG  1 
ATOM   2974 C CD1 . TYR A 1 479 ? -19.979 8.128   51.931  1 28.05 ? 728  TYR A CD1 1 
ATOM   2975 C CD2 . TYR A 1 479 ? -22.178 8.967   51.566  1 28.85 ? 728  TYR A CD2 1 
ATOM   2976 C CE1 . TYR A 1 479 ? -19.775 8.047   50.56   1 28.16 ? 728  TYR A CE1 1 
ATOM   2977 C CE2 . TYR A 1 479 ? -21.984 8.897   50.192  1 28.89 ? 728  TYR A CE2 1 
ATOM   2978 C CZ  . TYR A 1 479 ? -20.777 8.439   49.692  1 28.99 ? 728  TYR A CZ  1 
ATOM   2979 O OH  . TYR A 1 479 ? -20.59  8.332   48.338  1 29.33 ? 728  TYR A OH  1 
ATOM   2980 N N   . GLU A 1 480 ? -21.591 11.757  53.869  1 29.58 ? 729  GLU A N   1 
ATOM   2981 C CA  . GLU A 1 480 ? -21.75  12.985  53.076  1 30.55 ? 729  GLU A CA  1 
ATOM   2982 C C   . GLU A 1 480 ? -20.617 13.983  53.299  1 31.74 ? 729  GLU A C   1 
ATOM   2983 O O   . GLU A 1 480 ? -20.083 14.531  52.335  1 32.83 ? 729  GLU A O   1 
ATOM   2984 C CB  . GLU A 1 480 ? -23.131 13.617  53.311  1 32.23 ? 729  GLU A CB  1 
ATOM   2985 C CG  . GLU A 1 480 ? -23.525 14.646  52.261  1 34.63 ? 729  GLU A CG  1 
ATOM   2986 C CD  . GLU A 1 480 ? -23.35  14.268  50.796  1 35.56 ? 729  GLU A CD  1 
ATOM   2987 O OE1 . GLU A 1 480 ? -23.591 13.094  50.434  1 36.34 ? 729  GLU A OE1 1 
ATOM   2988 O OE2 . GLU A 1 480 ? -22.989 15.165  50.003  1 36.5  ? 729  GLU A OE2 1 
ATOM   2989 N N   . LYS A 1 481 ? -20.166 14.135  54.551  1 31.4  ? 730  LYS A N   1 
ATOM   2990 C CA  . LYS A 1 481 ? -19.046 15.019  54.851  1 31.17 ? 730  LYS A CA  1 
ATOM   2991 C C   . LYS A 1 481 ? -17.752 14.515  54.206  1 29.6  ? 730  LYS A C   1 
ATOM   2992 O O   . LYS A 1 481 ? -17.034 15.282  53.559  1 28.55 ? 730  LYS A O   1 
ATOM   2993 C CB  . LYS A 1 481 ? -18.877 15.164  56.368  1 34.26 ? 730  LYS A CB  1 
ATOM   2994 C CG  . LYS A 1 481 ? -17.821 16.198  56.74   1 40.43 ? 730  LYS A CG  1 
ATOM   2995 C CD  . LYS A 1 481 ? -17.993 16.654  58.172  1 45.71 ? 730  LYS A CD  1 
ATOM   2996 C CE  . LYS A 1 481 ? -17.352 18.001  58.404  1 49.97 ? 730  LYS A CE  1 
ATOM   2997 N NZ  . LYS A 1 481 ? -17.219 18.312  59.852  1 52.58 ? 730  LYS A NZ  1 
ATOM   2998 N N   . LEU A 1 482 ? -17.468 13.19   54.318  1 28.71 ? 731  LEU A N   1 
ATOM   2999 C CA  . LEU A 1 482 ? -16.257 12.63   53.687  1 27.56 ? 731  LEU A CA  1 
ATOM   3000 C C   . LEU A 1 482 ? -16.288 12.843  52.189  1 26.1  ? 731  LEU A C   1 
ATOM   3001 O O   . LEU A 1 482 ? -15.308 13.283  51.589  1 25.54 ? 731  LEU A O   1 
ATOM   3002 C CB  . LEU A 1 482 ? -16.12  11.11   54.005  1 27.79 ? 731  LEU A CB  1 
ATOM   3003 C CG  . LEU A 1 482 ? -14.813 10.463  53.551  1 28.84 ? 731  LEU A CG  1 
ATOM   3004 C CD1 . LEU A 1 482 ? -14.456 9.281   54.438  1 29.34 ? 731  LEU A CD1 1 
ATOM   3005 C CD2 . LEU A 1 482 ? -14.866 10.026  52.072  1 29.3  ? 731  LEU A CD2 1 
ATOM   3006 N N   . TYR A 1 483 ? -17.446 12.541  51.587  1 26.22 ? 732  TYR A N   1 
ATOM   3007 C CA  . TYR A 1 483 ? -17.683 12.66   50.155  1 26.62 ? 732  TYR A CA  1 
ATOM   3008 C C   . TYR A 1 483 ? -17.381 14.077  49.653  1 26.28 ? 732  TYR A C   1 
ATOM   3009 O O   . TYR A 1 483 ? -16.593 14.237  48.726  1 24.83 ? 732  TYR A O   1 
ATOM   3010 C CB  . TYR A 1 483 ? -19.136 12.237  49.835  1 26.76 ? 732  TYR A CB  1 
ATOM   3011 C CG  . TYR A 1 483 ? -19.478 12.378  48.373  1 28.54 ? 732  TYR A CG  1 
ATOM   3012 C CD1 . TYR A 1 483 ? -19.083 11.417  47.448  1 29.6  ? 732  TYR A CD1 1 
ATOM   3013 C CD2 . TYR A 1 483 ? -20.197 13.47   47.912  1 30.01 ? 732  TYR A CD2 1 
ATOM   3014 C CE1 . TYR A 1 483 ? -19.354 11.565  46.097  1 30.5  ? 732  TYR A CE1 1 
ATOM   3015 C CE2 . TYR A 1 483 ? -20.471 13.631  46.564  1 31.3  ? 732  TYR A CE2 1 
ATOM   3016 C CZ  . TYR A 1 483 ? -20.084 12.657  45.663  1 32.13 ? 732  TYR A CZ  1 
ATOM   3017 O OH  . TYR A 1 483 ? -20.397 12.822  44.338  1 33.35 ? 732  TYR A OH  1 
ATOM   3018 N N   . GLU A 1 484 ? -17.977 15.099  50.288  1 27.32 ? 733  GLU A N   1 
ATOM   3019 C CA  . GLU A 1 484 ? -17.743 16.496  49.88   1 28.22 ? 733  GLU A CA  1 
ATOM   3020 C C   . GLU A 1 484 ? -16.307 16.956  50.086  1 28.63 ? 733  GLU A C   1 
ATOM   3021 O O   . GLU A 1 484 ? -15.749 17.569  49.187  1 28.91 ? 733  GLU A O   1 
ATOM   3022 C CB  . GLU A 1 484 ? -18.713 17.447  50.608  1 29.86 ? 733  GLU A CB  1 
ATOM   3023 C CG  . GLU A 1 484 ? -20.174 17.096  50.378  1 34.34 ? 733  GLU A CG  1 
ATOM   3024 C CD  . GLU A 1 484 ? -21.181 17.962  51.113  1 41.81 ? 733  GLU A CD  1 
ATOM   3025 O OE1 . GLU A 1 484 ? -20.761 18.963  51.736  1 44.03 ? 733  GLU A OE1 1 
ATOM   3026 O OE2 . GLU A 1 484 ? -22.389 17.625  51.089  1 43.34 ? 733  GLU A OE2 1 
ATOM   3027 N N   . LYS A 1 485 ? -15.694 16.637  51.247  1 28.91 ? 734  LYS A N   1 
ATOM   3028 C CA  . LYS A 1 485 ? -14.324 17.052  51.566  1 29.42 ? 734  LYS A CA  1 
ATOM   3029 C C   . LYS A 1 485 ? -13.326 16.434  50.61   1 30.1  ? 734  LYS A C   1 
ATOM   3030 O O   . LYS A 1 485 ? -12.408 17.118  50.151  1 30.18 ? 734  LYS A O   1 
ATOM   3031 C CB  . LYS A 1 485 ? -13.963 16.682  53.02   1 31.25 ? 734  LYS A CB  1 
ATOM   3032 C CG  . LYS A 1 485 ? -14.838 17.366  54.073  1 34.88 ? 734  LYS A CG  1 
ATOM   3033 C CD  . LYS A 1 485 ? -14.492 18.833  54.247  1 38.77 ? 734  LYS A CD  1 
ATOM   3034 C CE  . LYS A 1 485 ? -15.257 19.419  55.416  1 41.93 ? 734  LYS A CE  1 
ATOM   3035 N NZ  . LYS A 1 485 ? -14.868 20.83   55.644  1 44.81 ? 734  LYS A NZ  1 
ATOM   3036 N N   . LEU A 1 486 ? -13.528 15.142  50.272  1 29.51 ? 735  LEU A N   1 
ATOM   3037 C CA  . LEU A 1 486 ? -12.682 14.446  49.304  1 29.1  ? 735  LEU A CA  1 
ATOM   3038 C C   . LEU A 1 486 ? -12.835 15.106  47.935  1 27.87 ? 735  LEU A C   1 
ATOM   3039 O O   . LEU A 1 486 ? -11.835 15.366  47.271  1 27.8  ? 735  LEU A O   1 
ATOM   3040 C CB  . LEU A 1 486 ? -13.1   12.956  49.246  1 29.49 ? 735  LEU A CB  1 
ATOM   3041 C CG  . LEU A 1 486 ? -12.139 11.988  48.589  1 30.88 ? 735  LEU A CG  1 
ATOM   3042 C CD1 . LEU A 1 486 ? -10.775 12.005  49.282  1 31.8  ? 735  LEU A CD1 1 
ATOM   3043 C CD2 . LEU A 1 486 ? -12.741 10.538  48.6    1 30.53 ? 735  LEU A CD2 1 
ATOM   3044 N N   . LEU A 1 487 ? -14.077 15.394  47.514  1 27.69 ? 736  LEU A N   1 
ATOM   3045 C CA  . LEU A 1 487 ? -14.283 16.074  46.239  1 29.03 ? 736  LEU A CA  1 
ATOM   3046 C C   . LEU A 1 487 ? -13.611 17.469  46.211  1 29.93 ? 736  LEU A C   1 
ATOM   3047 O O   . LEU A 1 487 ? -12.929 17.796  45.239  1 30.4  ? 736  LEU A O   1 
ATOM   3048 C CB  . LEU A 1 487 ? -15.763 16.169  45.885  1 29.37 ? 736  LEU A CB  1 
ATOM   3049 C CG  . LEU A 1 487 ? -16.297 15.012  45.064  1 31.01 ? 736  LEU A CG  1 
ATOM   3050 C CD1 . LEU A 1 487 ? -17.783 15.142  44.912  1 31.71 ? 736  LEU A CD1 1 
ATOM   3051 C CD2 . LEU A 1 487 ? -15.624 14.955  43.683  1 30.82 ? 736  LEU A CD2 1 
ATOM   3052 N N   . THR A 1 488 ? -13.759 18.256  47.285  1 30.67 ? 737  THR A N   1 
ATOM   3053 C CA  . THR A 1 488 ? -13.133 19.594  47.37   1 32.07 ? 737  THR A CA  1 
ATOM   3054 C C   . THR A 1 488 ? -11.62  19.482  47.275  1 34.32 ? 737  THR A C   1 
ATOM   3055 O O   . THR A 1 488 ? -10.991 20.214  46.505  1 34.76 ? 737  THR A O   1 
ATOM   3056 C CB  . THR A 1 488 ? -13.549 20.281  48.659  1 32.37 ? 737  THR A CB  1 
ATOM   3057 O OG1 . THR A 1 488 ? -14.964 20.338  48.678  1 32.53 ? 737  THR A OG1 1 
ATOM   3058 C CG2 . THR A 1 488 ? -12.943 21.686  48.809  1 33.34 ? 737  THR A CG2 1 
ATOM   3059 N N   . ALA A 1 489 ? -11.038 18.503  47.99   1 35.43 ? 738  ALA A N   1 
ATOM   3060 C CA  . ALA A 1 489 ? -9.597  18.305  47.955  1 37.04 ? 738  ALA A CA  1 
ATOM   3061 C C   . ALA A 1 489 ? -9.054  17.918  46.573  1 38.56 ? 738  ALA A C   1 
ATOM   3062 O O   . ALA A 1 489 ? -7.935  18.317  46.237  1 38.29 ? 738  ALA A O   1 
ATOM   3063 C CB  . ALA A 1 489 ? -9.182  17.271  48.995  1 36.84 ? 738  ALA A CB  1 
ATOM   3064 N N   . ILE A 1 490 ? -9.808  17.128  45.786  1 40.21 ? 739  ILE A N   1 
ATOM   3065 C CA  . ILE A 1 490 ? -9.294  16.703  44.475  1 42.5  ? 739  ILE A CA  1 
ATOM   3066 C C   . ILE A 1 490 ? -9.704  17.648  43.326  1 44.94 ? 739  ILE A C   1 
ATOM   3067 O O   . ILE A 1 490 ? -9.325  17.391  42.193  1 44.44 ? 739  ILE A O   1 
ATOM   3068 C CB  . ILE A 1 490 ? -9.62   15.213  44.153  1 42.93 ? 739  ILE A CB  1 
ATOM   3069 C CG1 . ILE A 1 490 ? -11.13  14.993  43.926  1 43.56 ? 739  ILE A CG1 1 
ATOM   3070 C CG2 . ILE A 1 490 ? -9.078  14.307  45.259  1 43.35 ? 739  ILE A CG2 1 
ATOM   3071 C CD1 . ILE A 1 490 ? -11.528 13.591  43.52   1 44.33 ? 739  ILE A CD1 1 
ATOM   3072 N N   . GLU A 1 491 ? -10.445 18.738  43.612  1 47.52 ? 740  GLU A N   1 
ATOM   3073 C CA  . GLU A 1 491 ? -10.878 19.728  42.609  1 50.76 ? 740  GLU A CA  1 
ATOM   3074 C C   . GLU A 1 491 ? -9.711  20.433  41.932  1 53.79 ? 740  GLU A C   1 
ATOM   3075 O O   . GLU A 1 491 ? -8.636  20.527  42.514  1 53.73 ? 740  GLU A O   1 
ATOM   3076 C CB  . GLU A 1 491 ? -11.69  20.838  43.287  1 53.34 ? 740  GLU A CB  1 
ATOM   3077 C CG  . GLU A 1 491 ? -13.183 20.621  43.419  1 59.36 ? 740  GLU A CG  1 
ATOM   3078 C CD  . GLU A 1 491 ? -13.876 21.73   44.199  1 67.68 ? 740  GLU A CD  1 
ATOM   3079 O OE1 . GLU A 1 491 ? -13.18  22.48   44.926  1 69.08 ? 740  GLU A OE1 1 
ATOM   3080 O OE2 . GLU A 1 491 ? -15.12  21.841  44.091  1 69.67 ? 740  GLU A OE2 1 
ATOM   3081 N N   . GLU A 1 492 ? -9.947  20.98   40.721  1 56.67 ? 741  GLU A N   1 
ATOM   3082 C CA  . GLU A 1 492 ? -9.011  21.831  39.975  1 59.79 ? 741  GLU A CA  1 
ATOM   3083 C C   . GLU A 1 492 ? -7.625  21.181  39.723  1 61.84 ? 741  GLU A C   1 
ATOM   3084 O O   . GLU A 1 492 ? -7.273  20.975  38.532  1 62.69 ? 741  GLU A O   1 
ATOM   3085 C CB  . GLU A 1 492 ? -8.908  23.205  40.7    1 62.95 ? 741  GLU A CB  1 
ATOM   3086 C CG  . GLU A 1 492 ? -7.612  23.99   40.558  1 69.4  ? 741  GLU A CG  1 
ATOM   3087 C CD  . GLU A 1 492 ? -7.188  24.652  41.857  1 76.64 ? 741  GLU A CD  1 
ATOM   3088 O OE1 . GLU A 1 492 ? -8.08   25.02   42.657  1 77.5  ? 741  GLU A OE1 1 
ATOM   3089 O OE2 . GLU A 1 492 ? -5.963  24.79   42.082  1 79.13 ? 741  GLU A OE2 1 
HETATM 3090 C C1  . TJQ B 2 .   ? 8.429   3.556   28.542  1 29.02 ? 801  TJQ A C1  1 
HETATM 3091 C C2  . TJQ B 2 .   ? 8.832   1.407   27.873  1 28.81 ? 801  TJQ A C2  1 
HETATM 3092 C C3  . TJQ B 2 .   ? 8.172   2.711   27.535  1 28.6  ? 801  TJQ A C3  1 
HETATM 3093 C C12 . TJQ B 2 .   ? 7.268   7.23    28.408  1 28.68 ? 801  TJQ A C12 1 
HETATM 3094 C C15 . TJQ B 2 .   ? 9.571   12.17   30.605  1 31.31 ? 801  TJQ A C15 1 
HETATM 3095 C C16 . TJQ B 2 .   ? 7.737   9.506   29.274  1 29.26 ? 801  TJQ A C16 1 
HETATM 3096 C C17 . TJQ B 2 .   ? 8.217   8.202   29.112  1 28.99 ? 801  TJQ A C17 1 
HETATM 3097 C C19 . TJQ B 2 .   ? 10.341  8.749   30.221  1 28.79 ? 801  TJQ A C19 1 
HETATM 3098 C C20 . TJQ B 2 .   ? 7.359   3.028   26.288  1 28.07 ? 801  TJQ A C20 1 
HETATM 3099 C C22 . TJQ B 2 .   ? 10.217  0.794   30.022  1 29.61 ? 801  TJQ A C22 1 
HETATM 3100 C C23 . TJQ B 2 .   ? 9.501   7.827   29.593  1 28.83 ? 801  TJQ A C23 1 
HETATM 3101 C C24 . TJQ B 2 .   ? 8.467   5.931   26.587  1 29.96 ? 801  TJQ A C24 1 
HETATM 3102 C C25 . TJQ B 2 .   ? 8.297   -0.829  24.877  1 31.58 ? 801  TJQ A C25 1 
HETATM 3103 C C26 . TJQ B 2 .   ? 9.647   6.879   26.267  1 30.53 ? 801  TJQ A C26 1 
HETATM 3104 C C27 . TJQ B 2 .   ? 7.787   -0.298  23.516  1 32.39 ? 801  TJQ A C27 1 
HETATM 3105 N N4  . TJQ B 2 .   ? 9.093   2.869   29.426  1 30.16 ? 801  TJQ A N4  1 
HETATM 3106 C C5  . TJQ B 2 .   ? 9.388   1.643   29.072  1 29.66 ? 801  TJQ A C5  1 
HETATM 3107 C C6  . TJQ B 2 .   ? 7.905   4.916   28.83   1 28.96 ? 801  TJQ A C6  1 
HETATM 3108 C C7  . TJQ B 2 .   ? 8.895   0.229   26.969  1 29.65 ? 801  TJQ A C7  1 
HETATM 3109 N N8  . TJQ B 2 .   ? 7.938   6.007   27.966  1 29.01 ? 801  TJQ A N8  1 
HETATM 3110 C C9  . TJQ B 2 .   ? 8.555   10.386  29.956  1 30.1  ? 801  TJQ A C9  1 
HETATM 3111 C C10 . TJQ B 2 .   ? 9.825   10.035  30.38   1 29.73 ? 801  TJQ A C10 1 
HETATM 3112 O O11 . TJQ B 2 .   ? 8.225   11.704  30.222  1 31.4  ? 801  TJQ A O11 1 
HETATM 3113 O O13 . TJQ B 2 .   ? 7.447   4.993   29.986  1 28.34 ? 801  TJQ A O13 1 
HETATM 3114 O O14 . TJQ B 2 .   ? 10.482  11.085  30.988  1 30.8  ? 801  TJQ A O14 1 
HETATM 3115 O O18 . TJQ B 2 .   ? 9.545   -0.772  27.281  1 29.51 ? 801  TJQ A O18 1 
HETATM 3116 O O21 . TJQ B 2 .   ? 8.282   0.303   25.775  1 30.9  ? 801  TJQ A O21 1 
HETATM 3117 P P   . PO4 C 3 .   ? 35.214  1.578   36.442  1 39.9  ? 802  PO4 A P   1 
HETATM 3118 O O1  . PO4 C 3 .   ? 35.508  1.979   35.005  1 40.76 ? 802  PO4 A O1  1 
HETATM 3119 O O2  . PO4 C 3 .   ? 33.735  1.991   36.893  1 40.14 ? 802  PO4 A O2  1 
HETATM 3120 O O3  . PO4 C 3 .   ? 35.321  -0.008  36.601  1 40.86 ? 802  PO4 A O3  1 
HETATM 3121 O O4  . PO4 C 3 .   ? 36.3    2.321   37.347  1 40    ? 802  PO4 A O4  1 
HETATM 3122 O O   . HOH D 4 .   ? 15.763  25.762  27.203  1 64.67 ? 901  HOH A O   1 
HETATM 3123 O O   . HOH D 4 .   ? 2.174   4.56    52.398  1 45.72 ? 902  HOH A O   1 
HETATM 3124 O O   . HOH D 4 .   ? 2.499   -3.676  36.944  1 44.79 ? 903  HOH A O   1 
HETATM 3125 O O   . HOH D 4 .   ? -5.274  6.408   34.17   1 28.36 ? 904  HOH A O   1 
HETATM 3126 O O   . HOH D 4 .   ? 10.046  24.323  -4.715  1 32.96 ? 905  HOH A O   1 
HETATM 3127 O O   . HOH D 4 .   ? 29.501  12.526  34.929  1 49.53 ? 906  HOH A O   1 
HETATM 3128 O O   . HOH D 4 .   ? 5.761   11.254  -1.633  1 46.91 ? 907  HOH A O   1 
HETATM 3129 O O   . HOH D 4 .   ? -8.422  23.249  11.173  1 48.55 ? 908  HOH A O   1 
HETATM 3130 O O   . HOH D 4 .   ? 19.19   24.872  32.66   1 35.05 ? 909  HOH A O   1 
HETATM 3131 O O   . HOH D 4 .   ? -9.355  12.874  65.802  1 52.63 ? 910  HOH A O   1 
HETATM 3132 O O   . HOH D 4 .   ? 28.489  11.162  55.027  1 33.67 ? 911  HOH A O   1 
HETATM 3133 O O   . HOH D 4 .   ? -13.238 4.234   36.429  1 30.09 ? 912  HOH A O   1 
HETATM 3134 O O   . HOH D 4 .   ? -5.036  4.243   66.136  1 64.96 ? 913  HOH A O   1 
HETATM 3135 O O   . HOH D 4 .   ? 32.436  -0.823  29.355  1 40.4  ? 914  HOH A O   1 
HETATM 3136 O O   . HOH D 4 .   ? 22.365  3.124   31.759  1 36.15 ? 915  HOH A O   1 
HETATM 3137 O O   . HOH D 4 .   ? 13.483  -11.033 29.479  1 43.78 ? 916  HOH A O   1 
HETATM 3138 O O   . HOH D 4 .   ? -7.319  -2.987  52.792  1 35.1  ? 917  HOH A O   1 
HETATM 3139 O O   . HOH D 4 .   ? 6.771   18.712  4.251   1 34.56 ? 918  HOH A O   1 
HETATM 3140 O O   . HOH D 4 .   ? 6.375   -15.854 27.969  1 52.2  ? 919  HOH A O   1 
HETATM 3141 O O   . HOH D 4 .   ? 31.460  4.190   46.177  1 25.85 ? 920  HOH A O   1 
HETATM 3142 O O   . HOH D 4 .   ? 3.919   7.944   44.439  1 38.08 ? 921  HOH A O   1 
HETATM 3143 O O   . HOH D 4 .   ? 23.694  4.651   41.231  1 32.77 ? 922  HOH A O   1 
HETATM 3144 O O   . HOH D 4 .   ? 25.452  -7.05   29.476  1 51.26 ? 923  HOH A O   1 
HETATM 3145 O O   . HOH D 4 .   ? -7.646  19.779  -6.239  1 37.32 ? 924  HOH A O   1 
HETATM 3146 O O   . HOH D 4 .   ? -9.253  13.266  36.06   1 49.88 ? 925  HOH A O   1 
HETATM 3147 O O   . HOH D 4 .   ? -16.197 16.416  39.388  1 53.79 ? 926  HOH A O   1 
HETATM 3148 O O   . HOH D 4 .   ? 25.368  24.994  33.601  1 50.92 ? 927  HOH A O   1 
HETATM 3149 O O   . HOH D 4 .   ? 28.984  15.287  46.377  1 32.9  ? 928  HOH A O   1 
HETATM 3150 O O   . HOH D 4 .   ? 1.908   10.262  29.2    1 47.25 ? 929  HOH A O   1 
HETATM 3151 O O   . HOH D 4 .   ? 10.998  27.781  18.451  1 24.99 ? 930  HOH A O   1 
HETATM 3152 O O   . HOH D 4 .   ? 36.609  4.834   37.65   1 31.64 ? 931  HOH A O   1 
HETATM 3153 O O   . HOH D 4 .   ? -15.509 -0.747  56.261  1 34.89 ? 932  HOH A O   1 
HETATM 3154 O O   . HOH D 4 .   ? 27.492  22.282  41.526  1 55.02 ? 933  HOH A O   1 
HETATM 3155 O O   . HOH D 4 .   ? -3.538  8.672   2.518   1 28.21 ? 934  HOH A O   1 
HETATM 3156 O O   . HOH D 4 .   ? 5.854   19.854  10.048  1 25.78 ? 935  HOH A O   1 
HETATM 3157 O O   . HOH D 4 .   ? 1.07    11.04   -8.769  1 46.15 ? 936  HOH A O   1 
HETATM 3158 O O   . HOH D 4 .   ? 1.508   26.874  22.181  1 38.14 ? 937  HOH A O   1 
HETATM 3159 O O   . HOH D 4 .   ? 7.251   16.199  -7.246  1 43.67 ? 938  HOH A O   1 
HETATM 3160 O O   . HOH D 4 .   ? 1.83    15.732  23.408  1 26.66 ? 939  HOH A O   1 
HETATM 3161 O O   . HOH D 4 .   ? -16.597 8.835   7.03    1 45.12 ? 940  HOH A O   1 
HETATM 3162 O O   . HOH D 4 .   ? -16.898 18.465  -10.41  1 35.79 ? 941  HOH A O   1 
HETATM 3163 O O   . HOH D 4 .   ? 12.384  8.317   17.52   1 59.99 ? 942  HOH A O   1 
HETATM 3164 O O   . HOH D 4 .   ? -3.971  3.869   33.725  1 39.11 ? 943  HOH A O   1 
HETATM 3165 O O   . HOH D 4 .   ? 7.798   24.725  -6.967  1 39.67 ? 944  HOH A O   1 
HETATM 3166 O O   . HOH D 4 .   ? -3.722  23.068  7.796   1 46.53 ? 945  HOH A O   1 
HETATM 3167 O O   . HOH D 4 .   ? -16.454 6.837   34.432  1 36.63 ? 946  HOH A O   1 
HETATM 3168 O O   . HOH D 4 .   ? -2.35   8.656   63.155  1 55.2  ? 947  HOH A O   1 
HETATM 3169 O O   . HOH D 4 .   ? 22.42   17.611  46.278  1 34.09 ? 948  HOH A O   1 
HETATM 3170 O O   . HOH D 4 .   ? 17.392  30.951  18.779  1 54.54 ? 949  HOH A O   1 
HETATM 3171 O O   . HOH D 4 .   ? 12.055  5.085   18.201  1 50.38 ? 950  HOH A O   1 
HETATM 3172 O O   . HOH D 4 .   ? -2.15   -0.162  46.113  1 26.98 ? 951  HOH A O   1 
HETATM 3173 O O   . HOH D 4 .   ? 22.949  1.793   40.159  1 46.39 ? 952  HOH A O   1 
HETATM 3174 O O   . HOH D 4 .   ? -3.481  22.352  0.131   1 42.77 ? 953  HOH A O   1 
HETATM 3175 O O   . HOH D 4 .   ? -22.77  8.032   46.888  1 29.62 ? 954  HOH A O   1 
HETATM 3176 O O   . HOH D 4 .   ? 32.367  -4.791  29.251  1 55.41 ? 955  HOH A O   1 
HETATM 3177 O O   . HOH D 4 .   ? 7.027   17.996  35.786  1 36.21 ? 956  HOH A O   1 
HETATM 3178 O O   . HOH D 4 .   ? -15.972 20.421  51.121  1 37.85 ? 957  HOH A O   1 
HETATM 3179 O O   . HOH D 4 .   ? 4.825   1.426   11.839  1 55.3  ? 958  HOH A O   1 
HETATM 3180 O O   . HOH D 4 .   ? 16.763  21.611  38.113  1 37.05 ? 959  HOH A O   1 
HETATM 3181 O O   . HOH D 4 .   ? -15.152 12.154  64.705  1 43.97 ? 960  HOH A O   1 
HETATM 3182 O O   . HOH D 4 .   ? 24.998  19.119  22.504  1 56.76 ? 961  HOH A O   1 
HETATM 3183 O O   . HOH D 4 .   ? -8.399  17.78   -9.094  1 41.43 ? 962  HOH A O   1 
HETATM 3184 O O   . HOH D 4 .   ? 25.049  24.35   38.994  1 52.58 ? 963  HOH A O   1 
HETATM 3185 O O   . HOH D 4 .   ? 13.286  26.963  25.322  1 38.04 ? 964  HOH A O   1 
HETATM 3186 O O   . HOH D 4 .   ? 0.111   33.567  13.77   1 53.15 ? 965  HOH A O   1 
HETATM 3187 O O   . HOH D 4 .   ? 6.591   16.613  3.237   1 45.32 ? 966  HOH A O   1 
HETATM 3188 O O   . HOH D 4 .   ? 7.064   37.15   11.709  1 46.41 ? 967  HOH A O   1 
HETATM 3189 O O   . HOH D 4 .   ? 4.073   33.035  20.303  1 28.91 ? 968  HOH A O   1 
HETATM 3190 O O   . HOH D 4 .   ? 7.373   27.133  15.989  1 24.98 ? 969  HOH A O   1 
HETATM 3191 O O   . HOH D 4 .   ? 7.763   27.48   -0.413  1 39.9  ? 970  HOH A O   1 
HETATM 3192 O O   . HOH D 4 .   ? 4.879   15.713  5.011   1 27.93 ? 971  HOH A O   1 
HETATM 3193 O O   . HOH D 4 .   ? 4.448   2.478   58.335  1 73.39 ? 972  HOH A O   1 
HETATM 3194 O O   . HOH D 4 .   ? 8.116   25.928  28.239  1 24.26 ? 973  HOH A O   1 
HETATM 3195 O O   . HOH D 4 .   ? 19.631  -7.679  20.332  1 54.27 ? 974  HOH A O   1 
HETATM 3196 O O   . HOH D 4 .   ? 8.423   25.567  4.461   1 24.77 ? 975  HOH A O   1 
HETATM 3197 O O   . HOH D 4 .   ? 29.112  8.662   57.233  1 43.13 ? 976  HOH A O   1 
HETATM 3198 O O   . HOH D 4 .   ? 16.822  18.994  15.202  1 28.29 ? 977  HOH A O   1 
HETATM 3199 O O   . HOH D 4 .   ? 10.447  22.246  29.784  1 21.87 ? 978  HOH A O   1 
HETATM 3200 O O   . HOH D 4 .   ? 10.834  24.808  15.303  1 38.81 ? 979  HOH A O   1 
HETATM 3201 O O   . HOH D 4 .   ? -9.471  14.468  -9.889  1 38.42 ? 980  HOH A O   1 
HETATM 3202 O O   . HOH D 4 .   ? -3.405  -5.554  41.57   1 27.92 ? 981  HOH A O   1 
HETATM 3203 O O   . HOH D 4 .   ? -6.951  -2.697  38.05   1 33.25 ? 982  HOH A O   1 
HETATM 3204 O O   . HOH D 4 .   ? -10.537 19.327  -8.665  1 41.76 ? 983  HOH A O   1 
HETATM 3205 O O   . HOH D 4 .   ? 33.582  2.549   26.897  1 61.59 ? 984  HOH A O   1 
HETATM 3206 O O   . HOH D 4 .   ? 2.205   -5.779  46.642  1 52.46 ? 985  HOH A O   1 
HETATM 3207 O O   . HOH D 4 .   ? 8.863   -9.139  20.091  1 46.08 ? 986  HOH A O   1 
HETATM 3208 O O   . HOH D 4 .   ? 19.29   9.709   48.059  1 56.12 ? 987  HOH A O   1 
HETATM 3209 O O   . HOH D 4 .   ? 7.479   22.403  8.022   1 34.65 ? 988  HOH A O   1 
HETATM 3210 O O   . HOH D 4 .   ? -8.771  7.155   -1.016  1 27.52 ? 989  HOH A O   1 
HETATM 3211 O O   . HOH D 4 .   ? -7.188  -7.588  42.113  1 33.1  ? 990  HOH A O   1 
HETATM 3212 O O   . HOH D 4 .   ? 19.753  24.76   19.431  1 26.57 ? 991  HOH A O   1 
HETATM 3213 O O   . HOH D 4 .   ? 10.85   16.462  12.774  1 34.61 ? 992  HOH A O   1 
HETATM 3214 O O   . HOH D 4 .   ? 3.324   24.642  16.543  1 46.38 ? 993  HOH A O   1 
HETATM 3215 O O   . HOH D 4 .   ? -17.923 0.788   51.112  1 31.2  ? 994  HOH A O   1 
HETATM 3216 O O   . HOH D 4 .   ? 25.105  8.117   45.925  1 25.84 ? 995  HOH A O   1 
HETATM 3217 O O   . HOH D 4 .   ? 10.399  22.308  -6.02   1 35.74 ? 996  HOH A O   1 
HETATM 3218 O O   . HOH D 4 .   ? -12.321 7.803   -3.301  1 37.93 ? 997  HOH A O   1 
HETATM 3219 O O   . HOH D 4 .   ? 20.217  8.916   17.1    1 31.88 ? 998  HOH A O   1 
HETATM 3220 O O   . HOH D 4 .   ? -4.753  8.544   -4.701  1 38.92 ? 999  HOH A O   1 
HETATM 3221 O O   . HOH D 4 .   ? -5.212  23.355  9.896   1 47.85 ? 1000 HOH A O   1 
HETATM 3222 O O   . HOH D 4 .   ? -5.825  -8.531  48.696  1 27.78 ? 1001 HOH A O   1 
HETATM 3223 O O   . HOH D 4 .   ? -17.76  1.104   40.176  1 34.25 ? 1002 HOH A O   1 
HETATM 3224 O O   . HOH D 4 .   ? -7.471  -0.28   37.68   1 33.74 ? 1003 HOH A O   1 
HETATM 3225 O O   . HOH D 4 .   ? -3.97   -8.493  46.604  1 30.02 ? 1004 HOH A O   1 
HETATM 3226 O O   . HOH D 4 .   ? -6.303  15.796  56.545  1 42.94 ? 1005 HOH A O   1 
HETATM 3227 O O   . HOH D 4 .   ? 16.867  26.715  16.382  1 35.87 ? 1006 HOH A O   1 
HETATM 3228 O O   . HOH D 4 .   ? -0.619  6.097   40.341  1 45.52 ? 1007 HOH A O   1 
HETATM 3229 O O   . HOH D 4 .   ? -12.03  3.685   30.702  1 55.59 ? 1008 HOH A O   1 
HETATM 3230 O O   . HOH D 4 .   ? 1.243   17.855  17.547  1 58.48 ? 1009 HOH A O   1 
HETATM 3231 O O   . HOH D 4 .   ? 1.122   -14.586 22.146  1 61.08 ? 1010 HOH A O   1 
HETATM 3232 O O   . HOH D 4 .   ? 3.261   21.476  20.448  1 30.32 ? 1011 HOH A O   1 
HETATM 3233 O O   . HOH D 4 .   ? 33.308  6.145   34.514  1 34.38 ? 1012 HOH A O   1 
HETATM 3234 O O   . HOH D 4 .   ? -4.568  5.567   15.206  1 64.41 ? 1013 HOH A O   1 
HETATM 3235 O O   . HOH D 4 .   ? -3.05   11.345  64.427  1 46.03 ? 1014 HOH A O   1 
HETATM 3236 O O   . HOH D 4 .   ? 2.711   3.202   40.835  1 41.53 ? 1015 HOH A O   1 
HETATM 3237 O O   . HOH D 4 .   ? 9.2     30.219  24.727  1 33.94 ? 1016 HOH A O   1 
HETATM 3238 O O   . HOH D 4 .   ? 18.794  23.033  36.797  1 32.69 ? 1017 HOH A O   1 
HETATM 3239 O O   . HOH D 4 .   ? 6.397   17.95   -10.775 1 50.54 ? 1018 HOH A O   1 
HETATM 3240 O O   . HOH D 4 .   ? 17.398  0.73    14.84   1 38.55 ? 1019 HOH A O   1 
HETATM 3241 O O   . HOH D 4 .   ? 5.418   19.24   33.613  1 37.61 ? 1020 HOH A O   1 
HETATM 3242 O O   . HOH D 4 .   ? 11.24   23.291  13.447  1 37.89 ? 1021 HOH A O   1 
HETATM 3243 O O   . HOH D 4 .   ? 22.421  0.625   36.499  1 35.27 ? 1022 HOH A O   1 
HETATM 3244 O O   . HOH D 4 .   ? 2.403   25.427  30.363  1 29.11 ? 1023 HOH A O   1 
HETATM 3245 O O   . HOH D 4 .   ? -2.541  25.058  30.127  1 50.17 ? 1024 HOH A O   1 
HETATM 3246 O O   . HOH D 4 .   ? 28.235  -1.412  32.763  1 30.52 ? 1025 HOH A O   1 
HETATM 3247 O O   . HOH D 4 .   ? -13.398 11.601  -11.561 1 46.02 ? 1026 HOH A O   1 
HETATM 3248 O O   . HOH D 4 .   ? 7.905   2.364   36.502  1 46.09 ? 1027 HOH A O   1 
HETATM 3249 O O   . HOH D 4 .   ? 12.754  11.343  46.306  1 50.15 ? 1028 HOH A O   1 
HETATM 3250 O O   . HOH D 4 .   ? 27.913  19.455  28.251  1 48.89 ? 1029 HOH A O   1 
HETATM 3251 O O   . HOH D 4 .   ? 2.207   3.764   37.265  1 55.76 ? 1030 HOH A O   1 
HETATM 3252 O O   . HOH D 4 .   ? 33.396  3.768   33.749  1 32.17 ? 1031 HOH A O   1 
HETATM 3253 O O   . HOH D 4 .   ? -13.99  -0.14   63.82   1 56.47 ? 1032 HOH A O   1 
HETATM 3254 O O   . HOH D 4 .   ? -17.534 17.755  65.569  1 66.95 ? 1033 HOH A O   1 
HETATM 3255 O O   . HOH D 4 .   ? 3.44    29.67   19.296  1 44.25 ? 1034 HOH A O   1 
HETATM 3256 O O   . HOH D 4 .   ? -18.934 10.593  40.058  1 26.2  ? 1035 HOH A O   1 
HETATM 3257 O O   . HOH D 4 .   ? -3.773  10.792  22.878  1 45.37 ? 1036 HOH A O   1 
HETATM 3258 O O   . HOH D 4 .   ? 26.196  27.745  27.312  1 56.2  ? 1037 HOH A O   1 
HETATM 3259 O O   . HOH D 4 .   ? -1.677  8.686   -4.3    1 31.75 ? 1038 HOH A O   1 
HETATM 3260 O O   . HOH D 4 .   ? -8.911  -1.964  34.507  1 48.75 ? 1039 HOH A O   1 
HETATM 3261 O O   . HOH D 4 .   ? 7.065   26.581  35.82   1 41.56 ? 1040 HOH A O   1 
HETATM 3262 O O   . HOH D 4 .   ? 4.208   18.474  20.914  1 24.76 ? 1041 HOH A O   1 
HETATM 3263 O O   . HOH D 4 .   ? 0.279   10.085  7.68    1 44.54 ? 1042 HOH A O   1 
HETATM 3264 O O   . HOH D 4 .   ? -10.415 22.181  13.823  1 54.74 ? 1043 HOH A O   1 
HETATM 3265 O O   . HOH D 4 .   ? -16.656 0.199   46.753  1 41.89 ? 1044 HOH A O   1 
HETATM 3266 O O   . HOH D 4 .   ? -5.548  23.908  13.906  1 48.18 ? 1045 HOH A O   1 
HETATM 3267 O O   . HOH D 4 .   ? 10.941  13.811  12.908  1 45.24 ? 1046 HOH A O   1 
HETATM 3268 O O   . HOH D 4 .   ? 17.373  3.991   37.299  1 43.34 ? 1047 HOH A O   1 
HETATM 3269 O O   . HOH D 4 .   ? -15.968 12.516  8.505   1 49.34 ? 1048 HOH A O   1 
HETATM 3270 O O   . HOH D 4 .   ? 30.304  13.403  32.021  1 38.19 ? 1049 HOH A O   1 
HETATM 3271 O O   . HOH D 4 .   ? 27.482  19.422  35.935  1 40.2  ? 1050 HOH A O   1 
HETATM 3272 O O   . HOH D 4 .   ? 5.341   12.642  50.378  1 58.44 ? 1051 HOH A O   1 
HETATM 3273 O O   . HOH D 4 .   ? -14.755 -0.264  39.22   1 36.99 ? 1052 HOH A O   1 
HETATM 3274 O O   . HOH D 4 .   ? -9.233  -1.099  51.895  1 24.97 ? 1053 HOH A O   1 
HETATM 3275 O O   . HOH D 4 .   ? 3.296   -1.243  34.353  1 43.22 ? 1054 HOH A O   1 
HETATM 3276 O O   . HOH D 4 .   ? 31.1    7.927   33.674  1 35.82 ? 1055 HOH A O   1 
HETATM 3277 O O   . HOH D 4 .   ? 12.734  -6.301  21.289  1 37.74 ? 1056 HOH A O   1 
HETATM 3278 O O   . HOH D 4 .   ? 2.333   20.408  16.239  1 39.67 ? 1057 HOH A O   1 
HETATM 3279 O O   . HOH D 4 .   ? -0.063  22.307  16.292  1 45    ? 1058 HOH A O   1 
HETATM 3280 O O   . HOH D 4 .   ? 24.225  10.518  47.083  1 27.48 ? 1059 HOH A O   1 
HETATM 3281 O O   . HOH D 4 .   ? -17.704 8.164   -2.674  1 36.64 ? 1060 HOH A O   1 
HETATM 3282 O O   . HOH D 4 .   ? -3.384  26.117  2.24    1 49.14 ? 1061 HOH A O   1 
HETATM 3283 O O   . HOH D 4 .   ? -0.25   26.597  29.479  1 46.68 ? 1062 HOH A O   1 
HETATM 3284 O O   . HOH D 4 .   ? 22.195  -1.271  35.101  1 41.6  ? 1063 HOH A O   1 
HETATM 3285 O O   . HOH D 4 .   ? 10.256  -7.203  21.489  1 35.6  ? 1064 HOH A O   1 
HETATM 3286 O O   . HOH D 4 .   ? 28.85   5.453   21.282  1 39.5  ? 1065 HOH A O   1 
HETATM 3287 O O   . HOH D 4 .   ? 0.028   26.692  -5.459  1 52.49 ? 1066 HOH A O   1 
HETATM 3288 O O   . HOH D 4 .   ? -12.924 20.994  3.059   1 50.71 ? 1067 HOH A O   1 
HETATM 3289 O O   . HOH D 4 .   ? 25.527  0.454   46.764  1 41.51 ? 1068 HOH A O   1 
HETATM 3290 O O   . HOH D 4 .   ? -11.229 23.737  -2.448  1 46.78 ? 1069 HOH A O   1 
HETATM 3291 O O   . HOH D 4 .   ? 13.519  29.15   30.224  1 43.8  ? 1070 HOH A O   1 
HETATM 3292 O O   . HOH D 4 .   ? 17.964  15.511  50.912  1 60.95 ? 1071 HOH A O   1 
HETATM 3293 O O   . HOH D 4 .   ? -4.843  -8.036  43.317  1 29.12 ? 1072 HOH A O   1 
HETATM 3294 O O   . HOH D 4 .   ? 17.654  3.781   15.971  1 44.76 ? 1073 HOH A O   1 
HETATM 3295 O O   . HOH D 4 .   ? 31.931  -3.895  39.001  1 52.51 ? 1074 HOH A O   1 
HETATM 3296 O O   . HOH D 4 .   ? 27.873  12.349  21.868  1 34.93 ? 1075 HOH A O   1 
HETATM 3297 O O   . HOH D 4 .   ? 8.045   14.753  0.561   1 39.65 ? 1076 HOH A O   1 
HETATM 3298 O O   . HOH D 4 .   ? -6.341  21.956  -8.26   1 48.12 ? 1077 HOH A O   1 
HETATM 3299 O O   . HOH D 4 .   ? 21.765  23.37   20.396  1 30.45 ? 1078 HOH A O   1 
HETATM 3300 O O   . HOH D 4 .   ? -3.501  24.332  -1.963  1 47.99 ? 1079 HOH A O   1 
HETATM 3301 O O   . HOH D 4 .   ? -3.089  30.007  9.406   1 44.91 ? 1080 HOH A O   1 
HETATM 3302 O O   . HOH D 4 .   ? 16.078  11.918  14.701  1 45.92 ? 1081 HOH A O   1 
HETATM 3303 O O   . HOH D 4 .   ? -16.638 12.648  12.171  1 61.69 ? 1082 HOH A O   1 
HETATM 3304 O O   . HOH D 4 .   ? 33.704  -2.683  36.925  1 53.98 ? 1083 HOH A O   1 
HETATM 3305 O O   . HOH D 4 .   ? -14.381 22.166  52.838  1 44.4  ? 1084 HOH A O   1 
HETATM 3306 O O   . HOH D 4 .   ? -14.464 5.195   61.546  1 35.24 ? 1085 HOH A O   1 
HETATM 3307 O O   . HOH D 4 .   ? -13.208 18.003  64.823  1 43.79 ? 1086 HOH A O   1 
HETATM 3308 O O   . HOH D 4 .   ? -6.698  11.619  -11.326 1 32.06 ? 1087 HOH A O   1 
HETATM 3309 O O   . HOH D 4 .   ? 29.555  13.27   23.123  1 57.34 ? 1088 HOH A O   1 
HETATM 3310 O O   . HOH D 4 .   ? 18.104  -1.184  36.014  1 55.53 ? 1089 HOH A O   1 
HETATM 3311 O O   . HOH D 4 .   ? 2.764   31.683  15.957  1 40.94 ? 1090 HOH A O   1 
HETATM 3312 O O   . HOH D 4 .   ? 19.587  7.392   49.146  1 42.27 ? 1091 HOH A O   1 
HETATM 3313 O O   . HOH D 4 .   ? 1.693   18.84   -12.585 1 50.01 ? 1092 HOH A O   1 
HETATM 3314 O O   . HOH D 4 .   ? 38.466  0.359   35.814  1 52.16 ? 1093 HOH A O   1 
HETATM 3315 O O   . HOH D 4 .   ? -11.503 2.095   63.083  1 42.02 ? 1094 HOH A O   1 
HETATM 3316 O O   . HOH D 4 .   ? 2.921   15.239  39.233  1 53.93 ? 1095 HOH A O   1 
HETATM 3317 O O   . HOH D 4 .   ? 4.669   -0.248  36.194  1 61.72 ? 1096 HOH A O   1 
HETATM 3318 O O   . HOH D 4 .   ? -9.7    8.895   10.229  1 42.95 ? 1097 HOH A O   1 
HETATM 3319 O O   . HOH D 4 .   ? 0.229   9.415   -5.741  1 43.48 ? 1098 HOH A O   1 
HETATM 3320 O O   . HOH D 4 .   ? 6.693   24.461  7.424   1 41.64 ? 1099 HOH A O   1 
HETATM 3321 O O   . HOH D 4 .   ? 5.407   26.805  11.706  1 38.11 ? 1100 HOH A O   1 
HETATM 3322 O O   . HOH D 4 .   ? 1.5     5.601   41.202  1 54.75 ? 1101 HOH A O   1 
HETATM 3323 O O   . HOH D 4 .   ? 25.396  -5.838  35.009  1 60.29 ? 1102 HOH A O   1 
HETATM 3324 O O   . HOH D 4 .   ? 4.872   15.005  35.059  1 52.79 ? 1103 HOH A O   1 
HETATM 3325 O O   . HOH D 4 .   ? 17.045  25.957  30.139  1 43.92 ? 1104 HOH A O   1 
HETATM 3326 O O   . HOH D 4 .   ? -2.368  13.229  29.859  1 50.68 ? 1105 HOH A O   1 
HETATM 3327 O O   . HOH D 4 .   ? 18.373  1.99    37.619  1 45.15 ? 1106 HOH A O   1 
HETATM 3328 O O   . HOH D 4 .   ? 26.789  17.199  22.383  1 56.86 ? 1107 HOH A O   1 
HETATM 3329 O O   . HOH D 4 .   ? 1.782   16.264  20.201  1 43.93 ? 1108 HOH A O   1 
HETATM 3330 O O   . HOH D 4 .   ? 21.652  27.652  32.63   1 60.95 ? 1109 HOH A O   1 
HETATM 3331 O O   . HOH D 4 .   ? -17.463 8.727   -7.923  1 60.08 ? 1110 HOH A O   1 
HETATM 3332 O O   . HOH D 4 .   ? 23.445  17.975  20.489  1 43.49 ? 1111 HOH A O   1 
HETATM 3333 O O   . HOH D 4 .   ? 23.831  24.601  21.567  1 56.81 ? 1112 HOH A O   1 
HETATM 3334 O O   . HOH D 4 .   ? 20.733  18.237  18.244  1 56.83 ? 1113 HOH A O   1 
HETATM 3335 O O   . HOH D 4 .   ? 15.492  1.685   39.722  1 59.76 ? 1114 HOH A O   1 
HETATM 3336 O O   . HOH D 4 .   ? -1.721  8.545   6.724   1 45.55 ? 1115 HOH A O   1 
HETATM 3337 O O   . HOH D 4 .   ? -3.827  9.122   5.326   1 44.15 ? 1116 HOH A O   1 
HETATM 3338 O O   . HOH D 4 .   ? 20.732  1.294   38.37   1 52.93 ? 1117 HOH A O   1 
# 
