data_9KWL
# 
_entry.id   9KWL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9KWL         pdb_00009kwl 10.2210/pdb9kwl/pdb 
WWPDB D_1300050748 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9KWL 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              qjzhao@smmu.edu.cn 
_pdbx_contact_author.name_first         Qingjie 
_pdbx_contact_author.name_last          Zhao 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3033-6085 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gai, C.'  1 0000-0001-6760-5045 
'Zhao, Q.' 2 0000-0003-3033-6085 
# 
_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                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Front Chem' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2296-2646 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            12 
_citation.language                  ? 
_citation.page_first                1504453 
_citation.page_last                 1504453 
_citation.title                     'The study of halogen effect on the reactivity of the serine-targeting covalent warheads.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3389/fchem.2024.1504453 
_citation.pdbx_database_id_PubMed   39691824 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gai, C.'    1  ? 
primary 'Zhang, Y.'  2  ? 
primary 'Zhang, S.'  3  ? 
primary 'Hu, X.'     4  ? 
primary 'Song, Y.Q.' 5  ? 
primary 'Zhuang, X.' 6  ? 
primary 'Chai, X.'   7  ? 
primary 'Zou, Y.'    8  ? 
primary 'Ge, G.B.'   9  ? 
primary 'Zhao, Q.'   10 ? 
# 
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 'Liver carboxylesterase 1'                                 58800.352 1   3.1.1.1,3.1.1.13,3.1.1.56 ? ? ? 
2 non-polymer syn '(1R)-1-(3,4-dichlorophenyl)-2,2,2-tris(fluoranyl)ethanol' 245.026   1   ?                         ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                                            24.305    1   ?                         ? ? ? 
4 water       nat water                                                      18.015    557 ?                         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Acyl-coenzyme A:cholesterol acyltransferase,ACAT,Brain carboxylesterase hBr1,Carboxylesterase 1,CE-1,hCE-1,Cholesteryl ester hydrolase,CEH,Cocaine carboxylesterase,Egasyn,HMSE,Methylumbelliferyl-acetate deacetylase 1,Monocyte/macrophage serine esterase,Retinyl ester hydrolase,REH,Serine esterase 1,Triacylglycerol hydrolase,TGH
;
# 
_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       
;SSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSEL
FTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST
GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGD
VKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLKMKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERN
FHTVPYMVGINKQEFGWLIPQMLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDL
IADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFW
ANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKDKEVAFWTNLFAK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSEL
FTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST
GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGD
VKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLKMKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERN
FHTVPYMVGINKQEFGWLIPQMLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDL
IADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFW
ANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKDKEVAFWTNLFAK
;
_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 '(1R)-1-(3,4-dichlorophenyl)-2,2,2-tris(fluoranyl)ethanol' A1EIY 
3 'MAGNESIUM ION'                                            MG    
4 water                                                      HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   SER n 
1 3   PRO n 
1 4   PRO n 
1 5   VAL n 
1 6   VAL n 
1 7   ASP n 
1 8   THR n 
1 9   VAL n 
1 10  HIS n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  LEU n 
1 15  GLY n 
1 16  LYS n 
1 17  PHE n 
1 18  VAL n 
1 19  SER n 
1 20  LEU n 
1 21  GLU n 
1 22  GLY n 
1 23  PHE n 
1 24  ALA n 
1 25  GLN n 
1 26  PRO n 
1 27  VAL n 
1 28  ALA n 
1 29  ILE n 
1 30  PHE n 
1 31  LEU n 
1 32  GLY n 
1 33  ILE n 
1 34  PRO n 
1 35  PHE n 
1 36  ALA n 
1 37  LYS n 
1 38  PRO n 
1 39  PRO n 
1 40  LEU n 
1 41  GLY n 
1 42  PRO n 
1 43  LEU n 
1 44  ARG n 
1 45  PHE n 
1 46  THR n 
1 47  PRO n 
1 48  PRO n 
1 49  GLN n 
1 50  PRO n 
1 51  ALA n 
1 52  GLU n 
1 53  PRO n 
1 54  TRP n 
1 55  SER n 
1 56  PHE n 
1 57  VAL n 
1 58  LYS n 
1 59  ASN n 
1 60  ALA n 
1 61  THR n 
1 62  SER n 
1 63  TYR n 
1 64  PRO n 
1 65  PRO n 
1 66  MET n 
1 67  CYS n 
1 68  THR n 
1 69  GLN n 
1 70  ASP n 
1 71  PRO n 
1 72  LYS n 
1 73  ALA n 
1 74  GLY n 
1 75  GLN n 
1 76  LEU n 
1 77  LEU n 
1 78  SER n 
1 79  GLU n 
1 80  LEU n 
1 81  PHE n 
1 82  THR n 
1 83  ASN n 
1 84  ARG n 
1 85  LYS n 
1 86  GLU n 
1 87  ASN n 
1 88  ILE n 
1 89  PRO n 
1 90  LEU n 
1 91  LYS n 
1 92  LEU n 
1 93  SER n 
1 94  GLU n 
1 95  ASP n 
1 96  CYS n 
1 97  LEU n 
1 98  TYR n 
1 99  LEU n 
1 100 ASN n 
1 101 ILE n 
1 102 TYR n 
1 103 THR n 
1 104 PRO n 
1 105 ALA n 
1 106 ASP n 
1 107 LEU n 
1 108 THR n 
1 109 LYS n 
1 110 LYS n 
1 111 ASN n 
1 112 ARG n 
1 113 LEU n 
1 114 PRO n 
1 115 VAL n 
1 116 MET n 
1 117 VAL n 
1 118 TRP n 
1 119 ILE n 
1 120 HIS n 
1 121 GLY n 
1 122 GLY n 
1 123 GLY n 
1 124 LEU n 
1 125 MET n 
1 126 VAL n 
1 127 GLY n 
1 128 ALA n 
1 129 ALA n 
1 130 SER n 
1 131 THR n 
1 132 TYR n 
1 133 ASP n 
1 134 GLY n 
1 135 LEU n 
1 136 ALA n 
1 137 LEU n 
1 138 ALA n 
1 139 ALA n 
1 140 HIS n 
1 141 GLU n 
1 142 ASN n 
1 143 VAL n 
1 144 VAL n 
1 145 VAL n 
1 146 VAL n 
1 147 THR n 
1 148 ILE n 
1 149 GLN n 
1 150 TYR n 
1 151 ARG n 
1 152 LEU n 
1 153 GLY n 
1 154 ILE n 
1 155 TRP n 
1 156 GLY n 
1 157 PHE n 
1 158 PHE n 
1 159 SER n 
1 160 THR n 
1 161 GLY n 
1 162 ASP n 
1 163 GLU n 
1 164 HIS n 
1 165 SER n 
1 166 ARG n 
1 167 GLY n 
1 168 ASN n 
1 169 TRP n 
1 170 GLY n 
1 171 HIS n 
1 172 LEU n 
1 173 ASP n 
1 174 GLN n 
1 175 VAL n 
1 176 ALA n 
1 177 ALA n 
1 178 LEU n 
1 179 ARG n 
1 180 TRP n 
1 181 VAL n 
1 182 GLN n 
1 183 ASP n 
1 184 ASN n 
1 185 ILE n 
1 186 ALA n 
1 187 SER n 
1 188 PHE n 
1 189 GLY n 
1 190 GLY n 
1 191 ASN n 
1 192 PRO n 
1 193 GLY n 
1 194 SER n 
1 195 VAL n 
1 196 THR n 
1 197 ILE n 
1 198 PHE n 
1 199 GLY n 
1 200 GLU n 
1 201 SER n 
1 202 ALA n 
1 203 GLY n 
1 204 GLY n 
1 205 GLU n 
1 206 SER n 
1 207 VAL n 
1 208 SER n 
1 209 VAL n 
1 210 LEU n 
1 211 VAL n 
1 212 LEU n 
1 213 SER n 
1 214 PRO n 
1 215 LEU n 
1 216 ALA n 
1 217 LYS n 
1 218 ASN n 
1 219 LEU n 
1 220 PHE n 
1 221 HIS n 
1 222 ARG n 
1 223 ALA n 
1 224 ILE n 
1 225 SER n 
1 226 GLU n 
1 227 SER n 
1 228 GLY n 
1 229 VAL n 
1 230 ALA n 
1 231 LEU n 
1 232 THR n 
1 233 SER n 
1 234 VAL n 
1 235 LEU n 
1 236 VAL n 
1 237 LYS n 
1 238 LYS n 
1 239 GLY n 
1 240 ASP n 
1 241 VAL n 
1 242 LYS n 
1 243 PRO n 
1 244 LEU n 
1 245 ALA n 
1 246 GLU n 
1 247 GLN n 
1 248 ILE n 
1 249 ALA n 
1 250 ILE n 
1 251 THR n 
1 252 ALA n 
1 253 GLY n 
1 254 CYS n 
1 255 LYS n 
1 256 THR n 
1 257 THR n 
1 258 THR n 
1 259 SER n 
1 260 ALA n 
1 261 VAL n 
1 262 MET n 
1 263 VAL n 
1 264 HIS n 
1 265 CYS n 
1 266 LEU n 
1 267 ARG n 
1 268 GLN n 
1 269 LYS n 
1 270 THR n 
1 271 GLU n 
1 272 GLU n 
1 273 GLU n 
1 274 LEU n 
1 275 LEU n 
1 276 GLU n 
1 277 THR n 
1 278 THR n 
1 279 LEU n 
1 280 LYS n 
1 281 MET n 
1 282 LYS n 
1 283 PHE n 
1 284 LEU n 
1 285 SER n 
1 286 LEU n 
1 287 ASP n 
1 288 LEU n 
1 289 GLN n 
1 290 GLY n 
1 291 ASP n 
1 292 PRO n 
1 293 ARG n 
1 294 GLU n 
1 295 SER n 
1 296 GLN n 
1 297 PRO n 
1 298 LEU n 
1 299 LEU n 
1 300 GLY n 
1 301 THR n 
1 302 VAL n 
1 303 ILE n 
1 304 ASP n 
1 305 GLY n 
1 306 MET n 
1 307 LEU n 
1 308 LEU n 
1 309 LEU n 
1 310 LYS n 
1 311 THR n 
1 312 PRO n 
1 313 GLU n 
1 314 GLU n 
1 315 LEU n 
1 316 GLN n 
1 317 ALA n 
1 318 GLU n 
1 319 ARG n 
1 320 ASN n 
1 321 PHE n 
1 322 HIS n 
1 323 THR n 
1 324 VAL n 
1 325 PRO n 
1 326 TYR n 
1 327 MET n 
1 328 VAL n 
1 329 GLY n 
1 330 ILE n 
1 331 ASN n 
1 332 LYS n 
1 333 GLN n 
1 334 GLU n 
1 335 PHE n 
1 336 GLY n 
1 337 TRP n 
1 338 LEU n 
1 339 ILE n 
1 340 PRO n 
1 341 GLN n 
1 342 MET n 
1 343 LEU n 
1 344 MET n 
1 345 SER n 
1 346 TYR n 
1 347 PRO n 
1 348 LEU n 
1 349 SER n 
1 350 GLU n 
1 351 GLY n 
1 352 GLN n 
1 353 LEU n 
1 354 ASP n 
1 355 GLN n 
1 356 LYS n 
1 357 THR n 
1 358 ALA n 
1 359 MET n 
1 360 SER n 
1 361 LEU n 
1 362 LEU n 
1 363 TRP n 
1 364 LYS n 
1 365 SER n 
1 366 TYR n 
1 367 PRO n 
1 368 LEU n 
1 369 VAL n 
1 370 CYS n 
1 371 ILE n 
1 372 ALA n 
1 373 LYS n 
1 374 GLU n 
1 375 LEU n 
1 376 ILE n 
1 377 PRO n 
1 378 GLU n 
1 379 ALA n 
1 380 THR n 
1 381 GLU n 
1 382 LYS n 
1 383 TYR n 
1 384 LEU n 
1 385 GLY n 
1 386 GLY n 
1 387 THR n 
1 388 ASP n 
1 389 ASP n 
1 390 THR n 
1 391 VAL n 
1 392 LYS n 
1 393 LYS n 
1 394 LYS n 
1 395 ASP n 
1 396 LEU n 
1 397 PHE n 
1 398 LEU n 
1 399 ASP n 
1 400 LEU n 
1 401 ILE n 
1 402 ALA n 
1 403 ASP n 
1 404 VAL n 
1 405 MET n 
1 406 PHE n 
1 407 GLY n 
1 408 VAL n 
1 409 PRO n 
1 410 SER n 
1 411 VAL n 
1 412 ILE n 
1 413 VAL n 
1 414 ALA n 
1 415 ARG n 
1 416 ASN n 
1 417 HIS n 
1 418 ARG n 
1 419 ASP n 
1 420 ALA n 
1 421 GLY n 
1 422 ALA n 
1 423 PRO n 
1 424 THR n 
1 425 TYR n 
1 426 MET n 
1 427 TYR n 
1 428 GLU n 
1 429 PHE n 
1 430 GLN n 
1 431 TYR n 
1 432 ARG n 
1 433 PRO n 
1 434 SER n 
1 435 PHE n 
1 436 SER n 
1 437 SER n 
1 438 ASP n 
1 439 MET n 
1 440 LYS n 
1 441 PRO n 
1 442 LYS n 
1 443 THR n 
1 444 VAL n 
1 445 ILE n 
1 446 GLY n 
1 447 ASP n 
1 448 HIS n 
1 449 GLY n 
1 450 ASP n 
1 451 GLU n 
1 452 LEU n 
1 453 PHE n 
1 454 SER n 
1 455 VAL n 
1 456 PHE n 
1 457 GLY n 
1 458 ALA n 
1 459 PRO n 
1 460 PHE n 
1 461 LEU n 
1 462 LYS n 
1 463 GLU n 
1 464 GLY n 
1 465 ALA n 
1 466 SER n 
1 467 GLU n 
1 468 GLU n 
1 469 GLU n 
1 470 ILE n 
1 471 ARG n 
1 472 LEU n 
1 473 SER n 
1 474 LYS n 
1 475 MET n 
1 476 VAL n 
1 477 MET n 
1 478 LYS n 
1 479 PHE n 
1 480 TRP n 
1 481 ALA n 
1 482 ASN n 
1 483 PHE n 
1 484 ALA n 
1 485 ARG n 
1 486 ASN n 
1 487 GLY n 
1 488 ASN n 
1 489 PRO n 
1 490 ASN n 
1 491 GLY n 
1 492 GLU n 
1 493 GLY n 
1 494 LEU n 
1 495 PRO n 
1 496 HIS n 
1 497 TRP n 
1 498 PRO n 
1 499 GLU n 
1 500 TYR n 
1 501 ASN n 
1 502 GLN n 
1 503 LYS n 
1 504 GLU n 
1 505 GLY n 
1 506 TYR n 
1 507 LEU n 
1 508 GLN n 
1 509 ILE n 
1 510 GLY n 
1 511 ALA n 
1 512 ASN n 
1 513 THR n 
1 514 GLN n 
1 515 ALA n 
1 516 ALA n 
1 517 GLN n 
1 518 LYS n 
1 519 LEU n 
1 520 LYS n 
1 521 ASP n 
1 522 LYS n 
1 523 GLU n 
1 524 VAL n 
1 525 ALA n 
1 526 PHE n 
1 527 TRP n 
1 528 THR n 
1 529 ASN n 
1 530 LEU n 
1 531 PHE n 
1 532 ALA n 
1 533 LYS 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                   533 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CES1, CES2, SES1' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_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 
A1EIY non-polymer         . '(1R)-1-(3,4-dichlorophenyl)-2,2,2-tris(fluoranyl)ethanol' 
'(R)-1-(3,4-dichlorophenyl)-2,2,2-trifluoroethanol' 'C8 H5 Cl2 F3 O' 245.026 
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 
MG    non-polymer         . 'MAGNESIUM ION'                                            ? 'Mg 2'           24.305  
PHE   'L-peptide linking' y PHENYLALANINE                                              ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                    ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                     ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                  ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                 ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                   ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                     ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   4   4   SER SER A . n 
A 1 2   SER 2   5   5   SER SER A . n 
A 1 3   PRO 3   6   6   PRO PRO A . n 
A 1 4   PRO 4   7   7   PRO PRO A . n 
A 1 5   VAL 5   8   8   VAL VAL A . n 
A 1 6   VAL 6   9   9   VAL VAL A . n 
A 1 7   ASP 7   10  10  ASP ASP A . n 
A 1 8   THR 8   11  11  THR THR A . n 
A 1 9   VAL 9   12  12  VAL VAL A . n 
A 1 10  HIS 10  13  13  HIS HIS A . n 
A 1 11  GLY 11  14  14  GLY GLY A . n 
A 1 12  LYS 12  15  15  LYS LYS A . n 
A 1 13  VAL 13  16  16  VAL VAL A . n 
A 1 14  LEU 14  17  17  LEU LEU A . n 
A 1 15  GLY 15  18  18  GLY GLY A . n 
A 1 16  LYS 16  19  19  LYS LYS A . n 
A 1 17  PHE 17  20  20  PHE PHE A . n 
A 1 18  VAL 18  21  21  VAL VAL A . n 
A 1 19  SER 19  22  22  SER SER A . n 
A 1 20  LEU 20  23  23  LEU LEU A . n 
A 1 21  GLU 21  24  24  GLU GLU A . n 
A 1 22  GLY 22  25  25  GLY GLY A . n 
A 1 23  PHE 23  26  26  PHE PHE A . n 
A 1 24  ALA 24  27  27  ALA ALA A . n 
A 1 25  GLN 25  28  28  GLN GLN A . n 
A 1 26  PRO 26  29  29  PRO PRO A . n 
A 1 27  VAL 27  30  30  VAL VAL A . n 
A 1 28  ALA 28  31  31  ALA ALA A . n 
A 1 29  ILE 29  32  32  ILE ILE A . n 
A 1 30  PHE 30  33  33  PHE PHE A . n 
A 1 31  LEU 31  34  34  LEU LEU A . n 
A 1 32  GLY 32  35  35  GLY GLY A . n 
A 1 33  ILE 33  36  36  ILE ILE A . n 
A 1 34  PRO 34  37  37  PRO PRO A . n 
A 1 35  PHE 35  38  38  PHE PHE A . n 
A 1 36  ALA 36  39  39  ALA ALA A . n 
A 1 37  LYS 37  40  40  LYS LYS A . n 
A 1 38  PRO 38  41  41  PRO PRO A . n 
A 1 39  PRO 39  42  42  PRO PRO A . n 
A 1 40  LEU 40  43  43  LEU LEU A . n 
A 1 41  GLY 41  44  44  GLY GLY A . n 
A 1 42  PRO 42  45  45  PRO PRO A . n 
A 1 43  LEU 43  46  46  LEU LEU A . n 
A 1 44  ARG 44  47  47  ARG ARG A . n 
A 1 45  PHE 45  48  48  PHE PHE A . n 
A 1 46  THR 46  49  49  THR THR A . n 
A 1 47  PRO 47  50  50  PRO PRO A . n 
A 1 48  PRO 48  51  51  PRO PRO A . n 
A 1 49  GLN 49  52  52  GLN GLN A . n 
A 1 50  PRO 50  53  53  PRO PRO A . n 
A 1 51  ALA 51  54  54  ALA ALA A . n 
A 1 52  GLU 52  55  55  GLU GLU A . n 
A 1 53  PRO 53  56  56  PRO PRO A . n 
A 1 54  TRP 54  57  57  TRP TRP A . n 
A 1 55  SER 55  58  58  SER SER A . n 
A 1 56  PHE 56  59  59  PHE PHE A . n 
A 1 57  VAL 57  60  60  VAL VAL A . n 
A 1 58  LYS 58  61  61  LYS LYS A . n 
A 1 59  ASN 59  62  62  ASN ASN A . n 
A 1 60  ALA 60  63  63  ALA ALA A . n 
A 1 61  THR 61  64  64  THR THR A . n 
A 1 62  SER 62  65  65  SER SER A . n 
A 1 63  TYR 63  66  66  TYR TYR A . n 
A 1 64  PRO 64  67  67  PRO PRO A . n 
A 1 65  PRO 65  68  68  PRO PRO A . n 
A 1 66  MET 66  69  69  MET MET A . n 
A 1 67  CYS 67  70  70  CYS CYS A . n 
A 1 68  THR 68  71  71  THR THR A . n 
A 1 69  GLN 69  72  72  GLN GLN A . n 
A 1 70  ASP 70  73  73  ASP ASP A . n 
A 1 71  PRO 71  74  74  PRO PRO A . n 
A 1 72  LYS 72  75  75  LYS LYS A . n 
A 1 73  ALA 73  76  76  ALA ALA A . n 
A 1 74  GLY 74  77  77  GLY GLY A . n 
A 1 75  GLN 75  78  78  GLN GLN A . n 
A 1 76  LEU 76  79  79  LEU LEU A . n 
A 1 77  LEU 77  80  80  LEU LEU A . n 
A 1 78  SER 78  81  81  SER SER A . n 
A 1 79  GLU 79  82  82  GLU GLU A . n 
A 1 80  LEU 80  83  83  LEU LEU A . n 
A 1 81  PHE 81  84  84  PHE PHE A . n 
A 1 82  THR 82  85  85  THR THR A . n 
A 1 83  ASN 83  86  86  ASN ASN A . n 
A 1 84  ARG 84  87  87  ARG ARG A . n 
A 1 85  LYS 85  88  88  LYS LYS A . n 
A 1 86  GLU 86  89  89  GLU GLU A . n 
A 1 87  ASN 87  90  90  ASN ASN A . n 
A 1 88  ILE 88  91  91  ILE ILE A . n 
A 1 89  PRO 89  92  92  PRO PRO A . n 
A 1 90  LEU 90  93  93  LEU LEU A . n 
A 1 91  LYS 91  94  94  LYS LYS A . n 
A 1 92  LEU 92  95  95  LEU LEU A . n 
A 1 93  SER 93  96  96  SER SER A . n 
A 1 94  GLU 94  97  97  GLU GLU A . n 
A 1 95  ASP 95  98  98  ASP ASP A . n 
A 1 96  CYS 96  99  99  CYS CYS A . n 
A 1 97  LEU 97  100 100 LEU LEU A . n 
A 1 98  TYR 98  101 101 TYR TYR A . n 
A 1 99  LEU 99  102 102 LEU LEU A . n 
A 1 100 ASN 100 103 103 ASN ASN A . n 
A 1 101 ILE 101 104 104 ILE ILE A . n 
A 1 102 TYR 102 105 105 TYR TYR A . n 
A 1 103 THR 103 106 106 THR THR A . n 
A 1 104 PRO 104 107 107 PRO PRO A . n 
A 1 105 ALA 105 108 108 ALA ALA A . n 
A 1 106 ASP 106 109 109 ASP ASP A . n 
A 1 107 LEU 107 110 110 LEU LEU A . n 
A 1 108 THR 108 111 111 THR THR A . n 
A 1 109 LYS 109 112 112 LYS LYS A . n 
A 1 110 LYS 110 113 113 LYS LYS A . n 
A 1 111 ASN 111 114 114 ASN ASN A . n 
A 1 112 ARG 112 115 115 ARG ARG A . n 
A 1 113 LEU 113 116 116 LEU LEU A . n 
A 1 114 PRO 114 117 117 PRO PRO A . n 
A 1 115 VAL 115 118 118 VAL VAL A . n 
A 1 116 MET 116 119 119 MET MET A . n 
A 1 117 VAL 117 120 120 VAL VAL A . n 
A 1 118 TRP 118 121 121 TRP TRP A . n 
A 1 119 ILE 119 122 122 ILE ILE A . n 
A 1 120 HIS 120 123 123 HIS HIS A . n 
A 1 121 GLY 121 124 124 GLY GLY A . n 
A 1 122 GLY 122 125 125 GLY GLY A . n 
A 1 123 GLY 123 126 126 GLY GLY A . n 
A 1 124 LEU 124 127 127 LEU LEU A . n 
A 1 125 MET 125 128 128 MET MET A . n 
A 1 126 VAL 126 129 129 VAL VAL A . n 
A 1 127 GLY 127 130 130 GLY GLY A . n 
A 1 128 ALA 128 131 131 ALA ALA A . n 
A 1 129 ALA 129 132 132 ALA ALA A . n 
A 1 130 SER 130 133 133 SER SER A . n 
A 1 131 THR 131 134 134 THR THR A . n 
A 1 132 TYR 132 135 135 TYR TYR A . n 
A 1 133 ASP 133 136 136 ASP ASP A . n 
A 1 134 GLY 134 137 137 GLY GLY A . n 
A 1 135 LEU 135 138 138 LEU LEU A . n 
A 1 136 ALA 136 139 139 ALA ALA A . n 
A 1 137 LEU 137 140 140 LEU LEU A . n 
A 1 138 ALA 138 141 141 ALA ALA A . n 
A 1 139 ALA 139 142 142 ALA ALA A . n 
A 1 140 HIS 140 143 143 HIS HIS A . n 
A 1 141 GLU 141 144 144 GLU GLU A . n 
A 1 142 ASN 142 145 145 ASN ASN A . n 
A 1 143 VAL 143 146 146 VAL VAL A . n 
A 1 144 VAL 144 147 147 VAL VAL A . n 
A 1 145 VAL 145 148 148 VAL VAL A . n 
A 1 146 VAL 146 149 149 VAL VAL A . n 
A 1 147 THR 147 150 150 THR THR A . n 
A 1 148 ILE 148 151 151 ILE ILE A . n 
A 1 149 GLN 149 152 152 GLN GLN A . n 
A 1 150 TYR 150 153 153 TYR TYR A . n 
A 1 151 ARG 151 154 154 ARG ARG A . n 
A 1 152 LEU 152 155 155 LEU LEU A . n 
A 1 153 GLY 153 156 156 GLY GLY A . n 
A 1 154 ILE 154 157 157 ILE ILE A . n 
A 1 155 TRP 155 158 158 TRP TRP A . n 
A 1 156 GLY 156 159 159 GLY GLY A . n 
A 1 157 PHE 157 160 160 PHE PHE A . n 
A 1 158 PHE 158 161 161 PHE PHE A . n 
A 1 159 SER 159 162 162 SER SER A . n 
A 1 160 THR 160 163 163 THR THR A . n 
A 1 161 GLY 161 164 164 GLY GLY A . n 
A 1 162 ASP 162 165 165 ASP ASP A . n 
A 1 163 GLU 163 166 166 GLU GLU A . n 
A 1 164 HIS 164 167 167 HIS HIS A . n 
A 1 165 SER 165 168 168 SER SER A . n 
A 1 166 ARG 166 169 169 ARG ARG A . n 
A 1 167 GLY 167 170 170 GLY GLY A . n 
A 1 168 ASN 168 171 171 ASN ASN A . n 
A 1 169 TRP 169 172 172 TRP TRP A . n 
A 1 170 GLY 170 173 173 GLY GLY A . n 
A 1 171 HIS 171 174 174 HIS HIS A . n 
A 1 172 LEU 172 175 175 LEU LEU A . n 
A 1 173 ASP 173 176 176 ASP ASP A . n 
A 1 174 GLN 174 177 177 GLN GLN A . n 
A 1 175 VAL 175 178 178 VAL VAL A . n 
A 1 176 ALA 176 179 179 ALA ALA A . n 
A 1 177 ALA 177 180 180 ALA ALA A . n 
A 1 178 LEU 178 181 181 LEU LEU A . n 
A 1 179 ARG 179 182 182 ARG ARG A . n 
A 1 180 TRP 180 183 183 TRP TRP A . n 
A 1 181 VAL 181 184 184 VAL VAL A . n 
A 1 182 GLN 182 185 185 GLN GLN A . n 
A 1 183 ASP 183 186 186 ASP ASP A . n 
A 1 184 ASN 184 187 187 ASN ASN A . n 
A 1 185 ILE 185 188 188 ILE ILE A . n 
A 1 186 ALA 186 189 189 ALA ALA A . n 
A 1 187 SER 187 190 190 SER SER A . n 
A 1 188 PHE 188 191 191 PHE PHE A . n 
A 1 189 GLY 189 192 192 GLY GLY A . n 
A 1 190 GLY 190 193 193 GLY GLY A . n 
A 1 191 ASN 191 194 194 ASN ASN A . n 
A 1 192 PRO 192 195 195 PRO PRO A . n 
A 1 193 GLY 193 196 196 GLY GLY A . n 
A 1 194 SER 194 197 197 SER SER A . n 
A 1 195 VAL 195 198 198 VAL VAL A . n 
A 1 196 THR 196 199 199 THR THR A . n 
A 1 197 ILE 197 200 200 ILE ILE A . n 
A 1 198 PHE 198 201 201 PHE PHE A . n 
A 1 199 GLY 199 202 202 GLY GLY A . n 
A 1 200 GLU 200 203 203 GLU GLU A . n 
A 1 201 SER 201 204 204 SER SER A . n 
A 1 202 ALA 202 205 205 ALA ALA A . n 
A 1 203 GLY 203 206 206 GLY GLY A . n 
A 1 204 GLY 204 207 207 GLY GLY A . n 
A 1 205 GLU 205 208 208 GLU GLU A . n 
A 1 206 SER 206 209 209 SER SER A . n 
A 1 207 VAL 207 210 210 VAL VAL A . n 
A 1 208 SER 208 211 211 SER SER A . n 
A 1 209 VAL 209 212 212 VAL VAL A . n 
A 1 210 LEU 210 213 213 LEU LEU A . n 
A 1 211 VAL 211 214 214 VAL VAL A . n 
A 1 212 LEU 212 215 215 LEU LEU A . n 
A 1 213 SER 213 216 216 SER SER A . n 
A 1 214 PRO 214 217 217 PRO PRO A . n 
A 1 215 LEU 215 218 218 LEU LEU A . n 
A 1 216 ALA 216 219 219 ALA ALA A . n 
A 1 217 LYS 217 220 220 LYS LYS A . n 
A 1 218 ASN 218 221 221 ASN ASN A . n 
A 1 219 LEU 219 222 222 LEU LEU A . n 
A 1 220 PHE 220 223 223 PHE PHE A . n 
A 1 221 HIS 221 224 224 HIS HIS A . n 
A 1 222 ARG 222 225 225 ARG ARG A . n 
A 1 223 ALA 223 226 226 ALA ALA A . n 
A 1 224 ILE 224 227 227 ILE ILE A . n 
A 1 225 SER 225 228 228 SER SER A . n 
A 1 226 GLU 226 229 229 GLU GLU A . n 
A 1 227 SER 227 230 230 SER SER A . n 
A 1 228 GLY 228 231 231 GLY GLY A . n 
A 1 229 VAL 229 232 232 VAL VAL A . n 
A 1 230 ALA 230 233 233 ALA ALA A . n 
A 1 231 LEU 231 234 234 LEU LEU A . n 
A 1 232 THR 232 235 235 THR THR A . n 
A 1 233 SER 233 236 236 SER SER A . n 
A 1 234 VAL 234 237 237 VAL VAL A . n 
A 1 235 LEU 235 238 238 LEU LEU A . n 
A 1 236 VAL 236 239 239 VAL VAL A . n 
A 1 237 LYS 237 240 240 LYS LYS A . n 
A 1 238 LYS 238 241 241 LYS LYS A . n 
A 1 239 GLY 239 242 242 GLY GLY A . n 
A 1 240 ASP 240 243 243 ASP ASP A . n 
A 1 241 VAL 241 244 244 VAL VAL A . n 
A 1 242 LYS 242 245 245 LYS LYS A . n 
A 1 243 PRO 243 246 246 PRO PRO A . n 
A 1 244 LEU 244 247 247 LEU LEU A . n 
A 1 245 ALA 245 248 248 ALA ALA A . n 
A 1 246 GLU 246 249 249 GLU GLU A . n 
A 1 247 GLN 247 250 250 GLN GLN A . n 
A 1 248 ILE 248 251 251 ILE ILE A . n 
A 1 249 ALA 249 252 252 ALA ALA A . n 
A 1 250 ILE 250 253 253 ILE ILE A . n 
A 1 251 THR 251 254 254 THR THR A . n 
A 1 252 ALA 252 255 255 ALA ALA A . n 
A 1 253 GLY 253 256 256 GLY GLY A . n 
A 1 254 CYS 254 257 257 CYS CYS A . n 
A 1 255 LYS 255 258 258 LYS LYS A . n 
A 1 256 THR 256 259 259 THR THR A . n 
A 1 257 THR 257 260 260 THR THR A . n 
A 1 258 THR 258 261 261 THR THR A . n 
A 1 259 SER 259 262 262 SER SER A . n 
A 1 260 ALA 260 263 263 ALA ALA A . n 
A 1 261 VAL 261 264 264 VAL VAL A . n 
A 1 262 MET 262 265 265 MET MET A . n 
A 1 263 VAL 263 266 266 VAL VAL A . n 
A 1 264 HIS 264 267 267 HIS HIS A . n 
A 1 265 CYS 265 268 268 CYS CYS A . n 
A 1 266 LEU 266 269 269 LEU LEU A . n 
A 1 267 ARG 267 270 270 ARG ARG A . n 
A 1 268 GLN 268 271 271 GLN GLN A . n 
A 1 269 LYS 269 272 272 LYS LYS A . n 
A 1 270 THR 270 273 273 THR THR A . n 
A 1 271 GLU 271 274 274 GLU GLU A . n 
A 1 272 GLU 272 275 275 GLU GLU A . n 
A 1 273 GLU 273 276 276 GLU GLU A . n 
A 1 274 LEU 274 277 277 LEU LEU A . n 
A 1 275 LEU 275 278 278 LEU LEU A . n 
A 1 276 GLU 276 279 279 GLU GLU A . n 
A 1 277 THR 277 280 280 THR THR A . n 
A 1 278 THR 278 281 281 THR THR A . n 
A 1 279 LEU 279 282 282 LEU LEU A . n 
A 1 280 LYS 280 283 283 LYS LYS A . n 
A 1 281 MET 281 284 284 MET MET A . n 
A 1 282 LYS 282 285 285 LYS LYS A . n 
A 1 283 PHE 283 286 286 PHE PHE A . n 
A 1 284 LEU 284 287 287 LEU LEU A . n 
A 1 285 SER 285 288 288 SER SER A . n 
A 1 286 LEU 286 289 289 LEU LEU A . n 
A 1 287 ASP 287 290 290 ASP ASP A . n 
A 1 288 LEU 288 291 291 LEU LEU A . n 
A 1 289 GLN 289 292 292 GLN GLN A . n 
A 1 290 GLY 290 293 293 GLY GLY A . n 
A 1 291 ASP 291 294 294 ASP ASP A . n 
A 1 292 PRO 292 295 295 PRO PRO A . n 
A 1 293 ARG 293 296 296 ARG ARG A . n 
A 1 294 GLU 294 297 297 GLU GLU A . n 
A 1 295 SER 295 298 298 SER SER A . n 
A 1 296 GLN 296 299 299 GLN GLN A . n 
A 1 297 PRO 297 300 300 PRO PRO A . n 
A 1 298 LEU 298 301 301 LEU LEU A . n 
A 1 299 LEU 299 302 302 LEU LEU A . n 
A 1 300 GLY 300 303 303 GLY GLY A . n 
A 1 301 THR 301 304 304 THR THR A . n 
A 1 302 VAL 302 305 305 VAL VAL A . n 
A 1 303 ILE 303 306 306 ILE ILE A . n 
A 1 304 ASP 304 307 307 ASP ASP A . n 
A 1 305 GLY 305 308 308 GLY GLY A . n 
A 1 306 MET 306 309 309 MET MET A . n 
A 1 307 LEU 307 310 310 LEU LEU A . n 
A 1 308 LEU 308 311 311 LEU LEU A . n 
A 1 309 LEU 309 312 312 LEU LEU A . n 
A 1 310 LYS 310 313 313 LYS LYS A . n 
A 1 311 THR 311 314 314 THR THR A . n 
A 1 312 PRO 312 315 315 PRO PRO A . n 
A 1 313 GLU 313 316 316 GLU GLU A . n 
A 1 314 GLU 314 317 317 GLU GLU A . n 
A 1 315 LEU 315 318 318 LEU LEU A . n 
A 1 316 GLN 316 319 319 GLN GLN A . n 
A 1 317 ALA 317 320 320 ALA ALA A . n 
A 1 318 GLU 318 321 321 GLU GLU A . n 
A 1 319 ARG 319 322 322 ARG ARG A . n 
A 1 320 ASN 320 323 323 ASN ASN A . n 
A 1 321 PHE 321 324 324 PHE PHE A . n 
A 1 322 HIS 322 325 325 HIS HIS A . n 
A 1 323 THR 323 326 326 THR THR A . n 
A 1 324 VAL 324 327 327 VAL VAL A . n 
A 1 325 PRO 325 328 328 PRO PRO A . n 
A 1 326 TYR 326 329 329 TYR TYR A . n 
A 1 327 MET 327 330 330 MET MET A . n 
A 1 328 VAL 328 331 331 VAL VAL A . n 
A 1 329 GLY 329 332 332 GLY GLY A . n 
A 1 330 ILE 330 333 333 ILE ILE A . n 
A 1 331 ASN 331 334 334 ASN ASN A . n 
A 1 332 LYS 332 335 335 LYS LYS A . n 
A 1 333 GLN 333 336 336 GLN GLN A . n 
A 1 334 GLU 334 337 337 GLU GLU A . n 
A 1 335 PHE 335 338 338 PHE PHE A . n 
A 1 336 GLY 336 339 339 GLY GLY A . n 
A 1 337 TRP 337 340 340 TRP TRP A . n 
A 1 338 LEU 338 341 341 LEU LEU A . n 
A 1 339 ILE 339 342 342 ILE ILE A . n 
A 1 340 PRO 340 343 343 PRO PRO A . n 
A 1 341 GLN 341 344 344 GLN GLN A . n 
A 1 342 MET 342 345 345 MET MET A . n 
A 1 343 LEU 343 346 346 LEU LEU A . n 
A 1 344 MET 344 347 347 MET MET A . n 
A 1 345 SER 345 348 348 SER SER A . n 
A 1 346 TYR 346 349 349 TYR TYR A . n 
A 1 347 PRO 347 350 350 PRO PRO A . n 
A 1 348 LEU 348 351 351 LEU LEU A . n 
A 1 349 SER 349 352 352 SER SER A . n 
A 1 350 GLU 350 353 353 GLU GLU A . n 
A 1 351 GLY 351 354 354 GLY GLY A . n 
A 1 352 GLN 352 355 355 GLN GLN A . n 
A 1 353 LEU 353 356 356 LEU LEU A . n 
A 1 354 ASP 354 357 357 ASP ASP A . n 
A 1 355 GLN 355 358 358 GLN GLN A . n 
A 1 356 LYS 356 359 359 LYS LYS A . n 
A 1 357 THR 357 360 360 THR THR A . n 
A 1 358 ALA 358 361 361 ALA ALA A . n 
A 1 359 MET 359 362 362 MET MET A . n 
A 1 360 SER 360 363 363 SER SER A . n 
A 1 361 LEU 361 364 364 LEU LEU A . n 
A 1 362 LEU 362 365 365 LEU LEU A . n 
A 1 363 TRP 363 366 366 TRP TRP A . n 
A 1 364 LYS 364 367 367 LYS LYS A . n 
A 1 365 SER 365 368 368 SER SER A . n 
A 1 366 TYR 366 369 369 TYR TYR A . n 
A 1 367 PRO 367 370 370 PRO PRO A . n 
A 1 368 LEU 368 371 371 LEU LEU A . n 
A 1 369 VAL 369 372 372 VAL VAL A . n 
A 1 370 CYS 370 373 373 CYS CYS A . n 
A 1 371 ILE 371 374 374 ILE ILE A . n 
A 1 372 ALA 372 375 375 ALA ALA A . n 
A 1 373 LYS 373 376 376 LYS LYS A . n 
A 1 374 GLU 374 377 377 GLU GLU A . n 
A 1 375 LEU 375 378 378 LEU LEU A . n 
A 1 376 ILE 376 379 379 ILE ILE A . n 
A 1 377 PRO 377 380 380 PRO PRO A . n 
A 1 378 GLU 378 381 381 GLU GLU A . n 
A 1 379 ALA 379 382 382 ALA ALA A . n 
A 1 380 THR 380 383 383 THR THR A . n 
A 1 381 GLU 381 384 384 GLU GLU A . n 
A 1 382 LYS 382 385 385 LYS LYS A . n 
A 1 383 TYR 383 386 386 TYR TYR A . n 
A 1 384 LEU 384 387 387 LEU LEU A . n 
A 1 385 GLY 385 388 388 GLY GLY A . n 
A 1 386 GLY 386 389 389 GLY GLY A . n 
A 1 387 THR 387 390 390 THR THR A . n 
A 1 388 ASP 388 391 391 ASP ASP A . n 
A 1 389 ASP 389 392 392 ASP ASP A . n 
A 1 390 THR 390 393 393 THR THR A . n 
A 1 391 VAL 391 394 394 VAL VAL A . n 
A 1 392 LYS 392 395 395 LYS LYS A . n 
A 1 393 LYS 393 396 396 LYS LYS A . n 
A 1 394 LYS 394 397 397 LYS LYS A . n 
A 1 395 ASP 395 398 398 ASP ASP A . n 
A 1 396 LEU 396 399 399 LEU LEU A . n 
A 1 397 PHE 397 400 400 PHE PHE A . n 
A 1 398 LEU 398 401 401 LEU LEU A . n 
A 1 399 ASP 399 402 402 ASP ASP A . n 
A 1 400 LEU 400 403 403 LEU LEU A . n 
A 1 401 ILE 401 404 404 ILE ILE A . n 
A 1 402 ALA 402 405 405 ALA ALA A . n 
A 1 403 ASP 403 406 406 ASP ASP A . n 
A 1 404 VAL 404 407 407 VAL VAL A . n 
A 1 405 MET 405 408 408 MET MET A . n 
A 1 406 PHE 406 409 409 PHE PHE A . n 
A 1 407 GLY 407 410 410 GLY GLY A . n 
A 1 408 VAL 408 411 411 VAL VAL A . n 
A 1 409 PRO 409 412 412 PRO PRO A . n 
A 1 410 SER 410 413 413 SER SER A . n 
A 1 411 VAL 411 414 414 VAL VAL A . n 
A 1 412 ILE 412 415 415 ILE ILE A . n 
A 1 413 VAL 413 416 416 VAL VAL A . n 
A 1 414 ALA 414 417 417 ALA ALA A . n 
A 1 415 ARG 415 418 418 ARG ARG A . n 
A 1 416 ASN 416 419 419 ASN ASN A . n 
A 1 417 HIS 417 420 420 HIS HIS A . n 
A 1 418 ARG 418 421 421 ARG ARG A . n 
A 1 419 ASP 419 422 422 ASP ASP A . n 
A 1 420 ALA 420 423 423 ALA ALA A . n 
A 1 421 GLY 421 424 424 GLY GLY A . n 
A 1 422 ALA 422 425 425 ALA ALA A . n 
A 1 423 PRO 423 426 426 PRO PRO A . n 
A 1 424 THR 424 427 427 THR THR A . n 
A 1 425 TYR 425 428 428 TYR TYR A . n 
A 1 426 MET 426 429 429 MET MET A . n 
A 1 427 TYR 427 430 430 TYR TYR A . n 
A 1 428 GLU 428 431 431 GLU GLU A . n 
A 1 429 PHE 429 432 432 PHE PHE A . n 
A 1 430 GLN 430 433 433 GLN GLN A . n 
A 1 431 TYR 431 434 434 TYR TYR A . n 
A 1 432 ARG 432 435 435 ARG ARG A . n 
A 1 433 PRO 433 436 436 PRO PRO A . n 
A 1 434 SER 434 437 437 SER SER A . n 
A 1 435 PHE 435 438 438 PHE PHE A . n 
A 1 436 SER 436 439 439 SER SER A . n 
A 1 437 SER 437 440 440 SER SER A . n 
A 1 438 ASP 438 441 441 ASP ASP A . n 
A 1 439 MET 439 442 442 MET MET A . n 
A 1 440 LYS 440 443 443 LYS LYS A . n 
A 1 441 PRO 441 444 444 PRO PRO A . n 
A 1 442 LYS 442 445 445 LYS LYS A . n 
A 1 443 THR 443 446 446 THR THR A . n 
A 1 444 VAL 444 447 447 VAL VAL A . n 
A 1 445 ILE 445 448 448 ILE ILE A . n 
A 1 446 GLY 446 449 449 GLY GLY A . n 
A 1 447 ASP 447 450 450 ASP ASP A . n 
A 1 448 HIS 448 451 451 HIS HIS A . n 
A 1 449 GLY 449 452 452 GLY GLY A . n 
A 1 450 ASP 450 453 453 ASP ASP A . n 
A 1 451 GLU 451 454 454 GLU GLU A . n 
A 1 452 LEU 452 455 455 LEU LEU A . n 
A 1 453 PHE 453 456 456 PHE PHE A . n 
A 1 454 SER 454 457 457 SER SER A . n 
A 1 455 VAL 455 458 458 VAL VAL A . n 
A 1 456 PHE 456 459 459 PHE PHE A . n 
A 1 457 GLY 457 460 460 GLY GLY A . n 
A 1 458 ALA 458 461 461 ALA ALA A . n 
A 1 459 PRO 459 462 462 PRO PRO A . n 
A 1 460 PHE 460 463 463 PHE PHE A . n 
A 1 461 LEU 461 464 464 LEU LEU A . n 
A 1 462 LYS 462 465 465 LYS LYS A . n 
A 1 463 GLU 463 466 466 GLU GLU A . n 
A 1 464 GLY 464 467 467 GLY GLY A . n 
A 1 465 ALA 465 468 468 ALA ALA A . n 
A 1 466 SER 466 469 469 SER SER A . n 
A 1 467 GLU 467 470 470 GLU GLU A . n 
A 1 468 GLU 468 471 471 GLU GLU A . n 
A 1 469 GLU 469 472 472 GLU GLU A . n 
A 1 470 ILE 470 473 473 ILE ILE A . n 
A 1 471 ARG 471 474 474 ARG ARG A . n 
A 1 472 LEU 472 475 475 LEU LEU A . n 
A 1 473 SER 473 476 476 SER SER A . n 
A 1 474 LYS 474 477 477 LYS LYS A . n 
A 1 475 MET 475 478 478 MET MET A . n 
A 1 476 VAL 476 479 479 VAL VAL A . n 
A 1 477 MET 477 480 480 MET MET A . n 
A 1 478 LYS 478 481 481 LYS LYS A . n 
A 1 479 PHE 479 482 482 PHE PHE A . n 
A 1 480 TRP 480 483 483 TRP TRP A . n 
A 1 481 ALA 481 484 484 ALA ALA A . n 
A 1 482 ASN 482 485 485 ASN ASN A . n 
A 1 483 PHE 483 486 486 PHE PHE A . n 
A 1 484 ALA 484 487 487 ALA ALA A . n 
A 1 485 ARG 485 488 488 ARG ARG A . n 
A 1 486 ASN 486 489 489 ASN ASN A . n 
A 1 487 GLY 487 490 490 GLY GLY A . n 
A 1 488 ASN 488 491 491 ASN ASN A . n 
A 1 489 PRO 489 492 492 PRO PRO A . n 
A 1 490 ASN 490 493 493 ASN ASN A . n 
A 1 491 GLY 491 494 494 GLY GLY A . n 
A 1 492 GLU 492 495 495 GLU GLU A . n 
A 1 493 GLY 493 496 496 GLY GLY A . n 
A 1 494 LEU 494 497 497 LEU LEU A . n 
A 1 495 PRO 495 498 498 PRO PRO A . n 
A 1 496 HIS 496 499 499 HIS HIS A . n 
A 1 497 TRP 497 500 500 TRP TRP A . n 
A 1 498 PRO 498 501 501 PRO PRO A . n 
A 1 499 GLU 499 502 502 GLU GLU A . n 
A 1 500 TYR 500 503 503 TYR TYR A . n 
A 1 501 ASN 501 504 504 ASN ASN A . n 
A 1 502 GLN 502 505 505 GLN GLN A . n 
A 1 503 LYS 503 506 506 LYS LYS A . n 
A 1 504 GLU 504 507 507 GLU GLU A . n 
A 1 505 GLY 505 508 508 GLY GLY A . n 
A 1 506 TYR 506 509 509 TYR TYR A . n 
A 1 507 LEU 507 510 510 LEU LEU A . n 
A 1 508 GLN 508 511 511 GLN GLN A . n 
A 1 509 ILE 509 512 512 ILE ILE A . n 
A 1 510 GLY 510 513 513 GLY GLY A . n 
A 1 511 ALA 511 514 514 ALA ALA A . n 
A 1 512 ASN 512 515 515 ASN ASN A . n 
A 1 513 THR 513 516 516 THR THR A . n 
A 1 514 GLN 514 517 517 GLN GLN A . n 
A 1 515 ALA 515 518 518 ALA ALA A . n 
A 1 516 ALA 516 519 519 ALA ALA A . n 
A 1 517 GLN 517 520 520 GLN GLN A . n 
A 1 518 LYS 518 521 521 LYS LYS A . n 
A 1 519 LEU 519 522 522 LEU LEU A . n 
A 1 520 LYS 520 523 523 LYS LYS A . n 
A 1 521 ASP 521 524 524 ASP ASP A . n 
A 1 522 LYS 522 525 525 LYS LYS A . n 
A 1 523 GLU 523 526 526 GLU GLU A . n 
A 1 524 VAL 524 527 527 VAL VAL A . n 
A 1 525 ALA 525 528 528 ALA ALA A . n 
A 1 526 PHE 526 529 529 PHE PHE A . n 
A 1 527 TRP 527 530 530 TRP TRP A . n 
A 1 528 THR 528 531 531 THR THR A . n 
A 1 529 ASN 529 532 532 ASN ASN A . n 
A 1 530 LEU 530 533 533 LEU LEU A . n 
A 1 531 PHE 531 534 534 PHE PHE A . n 
A 1 532 ALA 532 535 535 ALA ALA A . n 
A 1 533 LYS 533 536 536 LYS LYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EIY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EIY 
_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 A1EIY 1   601  601 A1EIY L3F A . 
C 3 MG    1   602  1   MG    MG  A . 
D 4 HOH   1   701  525 HOH   HOH A . 
D 4 HOH   2   702  470 HOH   HOH A . 
D 4 HOH   3   703  520 HOH   HOH A . 
D 4 HOH   4   704  399 HOH   HOH A . 
D 4 HOH   5   705  301 HOH   HOH A . 
D 4 HOH   6   706  428 HOH   HOH A . 
D 4 HOH   7   707  234 HOH   HOH A . 
D 4 HOH   8   708  424 HOH   HOH A . 
D 4 HOH   9   709  29  HOH   HOH A . 
D 4 HOH   10  710  60  HOH   HOH A . 
D 4 HOH   11  711  392 HOH   HOH A . 
D 4 HOH   12  712  454 HOH   HOH A . 
D 4 HOH   13  713  422 HOH   HOH A . 
D 4 HOH   14  714  207 HOH   HOH A . 
D 4 HOH   15  715  541 HOH   HOH A . 
D 4 HOH   16  716  216 HOH   HOH A . 
D 4 HOH   17  717  59  HOH   HOH A . 
D 4 HOH   18  718  512 HOH   HOH A . 
D 4 HOH   19  719  132 HOH   HOH A . 
D 4 HOH   20  720  93  HOH   HOH A . 
D 4 HOH   21  721  151 HOH   HOH A . 
D 4 HOH   22  722  413 HOH   HOH A . 
D 4 HOH   23  723  236 HOH   HOH A . 
D 4 HOH   24  724  479 HOH   HOH A . 
D 4 HOH   25  725  12  HOH   HOH A . 
D 4 HOH   26  726  42  HOH   HOH A . 
D 4 HOH   27  727  35  HOH   HOH A . 
D 4 HOH   28  728  531 HOH   HOH A . 
D 4 HOH   29  729  286 HOH   HOH A . 
D 4 HOH   30  730  489 HOH   HOH A . 
D 4 HOH   31  731  375 HOH   HOH A . 
D 4 HOH   32  732  382 HOH   HOH A . 
D 4 HOH   33  733  3   HOH   HOH A . 
D 4 HOH   34  734  434 HOH   HOH A . 
D 4 HOH   35  735  414 HOH   HOH A . 
D 4 HOH   36  736  378 HOH   HOH A . 
D 4 HOH   37  737  148 HOH   HOH A . 
D 4 HOH   38  738  5   HOH   HOH A . 
D 4 HOH   39  739  75  HOH   HOH A . 
D 4 HOH   40  740  95  HOH   HOH A . 
D 4 HOH   41  741  46  HOH   HOH A . 
D 4 HOH   42  742  478 HOH   HOH A . 
D 4 HOH   43  743  140 HOH   HOH A . 
D 4 HOH   44  744  252 HOH   HOH A . 
D 4 HOH   45  745  350 HOH   HOH A . 
D 4 HOH   46  746  150 HOH   HOH A . 
D 4 HOH   47  747  218 HOH   HOH A . 
D 4 HOH   48  748  469 HOH   HOH A . 
D 4 HOH   49  749  138 HOH   HOH A . 
D 4 HOH   50  750  106 HOH   HOH A . 
D 4 HOH   51  751  6   HOH   HOH A . 
D 4 HOH   52  752  22  HOH   HOH A . 
D 4 HOH   53  753  129 HOH   HOH A . 
D 4 HOH   54  754  549 HOH   HOH A . 
D 4 HOH   55  755  389 HOH   HOH A . 
D 4 HOH   56  756  330 HOH   HOH A . 
D 4 HOH   57  757  357 HOH   HOH A . 
D 4 HOH   58  758  162 HOH   HOH A . 
D 4 HOH   59  759  31  HOH   HOH A . 
D 4 HOH   60  760  285 HOH   HOH A . 
D 4 HOH   61  761  482 HOH   HOH A . 
D 4 HOH   62  762  57  HOH   HOH A . 
D 4 HOH   63  763  52  HOH   HOH A . 
D 4 HOH   64  764  387 HOH   HOH A . 
D 4 HOH   65  765  40  HOH   HOH A . 
D 4 HOH   66  766  400 HOH   HOH A . 
D 4 HOH   67  767  245 HOH   HOH A . 
D 4 HOH   68  768  38  HOH   HOH A . 
D 4 HOH   69  769  438 HOH   HOH A . 
D 4 HOH   70  770  273 HOH   HOH A . 
D 4 HOH   71  771  1   HOH   HOH A . 
D 4 HOH   72  772  69  HOH   HOH A . 
D 4 HOH   73  773  258 HOH   HOH A . 
D 4 HOH   74  774  32  HOH   HOH A . 
D 4 HOH   75  775  481 HOH   HOH A . 
D 4 HOH   76  776  241 HOH   HOH A . 
D 4 HOH   77  777  167 HOH   HOH A . 
D 4 HOH   78  778  58  HOH   HOH A . 
D 4 HOH   79  779  401 HOH   HOH A . 
D 4 HOH   80  780  128 HOH   HOH A . 
D 4 HOH   81  781  116 HOH   HOH A . 
D 4 HOH   82  782  322 HOH   HOH A . 
D 4 HOH   83  783  260 HOH   HOH A . 
D 4 HOH   84  784  4   HOH   HOH A . 
D 4 HOH   85  785  27  HOH   HOH A . 
D 4 HOH   86  786  441 HOH   HOH A . 
D 4 HOH   87  787  153 HOH   HOH A . 
D 4 HOH   88  788  468 HOH   HOH A . 
D 4 HOH   89  789  268 HOH   HOH A . 
D 4 HOH   90  790  418 HOH   HOH A . 
D 4 HOH   91  791  49  HOH   HOH A . 
D 4 HOH   92  792  266 HOH   HOH A . 
D 4 HOH   93  793  264 HOH   HOH A . 
D 4 HOH   94  794  221 HOH   HOH A . 
D 4 HOH   95  795  2   HOH   HOH A . 
D 4 HOH   96  796  317 HOH   HOH A . 
D 4 HOH   97  797  237 HOH   HOH A . 
D 4 HOH   98  798  247 HOH   HOH A . 
D 4 HOH   99  799  309 HOH   HOH A . 
D 4 HOH   100 800  246 HOH   HOH A . 
D 4 HOH   101 801  174 HOH   HOH A . 
D 4 HOH   102 802  300 HOH   HOH A . 
D 4 HOH   103 803  70  HOH   HOH A . 
D 4 HOH   104 804  265 HOH   HOH A . 
D 4 HOH   105 805  529 HOH   HOH A . 
D 4 HOH   106 806  385 HOH   HOH A . 
D 4 HOH   107 807  172 HOH   HOH A . 
D 4 HOH   108 808  551 HOH   HOH A . 
D 4 HOH   109 809  126 HOH   HOH A . 
D 4 HOH   110 810  393 HOH   HOH A . 
D 4 HOH   111 811  209 HOH   HOH A . 
D 4 HOH   112 812  112 HOH   HOH A . 
D 4 HOH   113 813  419 HOH   HOH A . 
D 4 HOH   114 814  127 HOH   HOH A . 
D 4 HOH   115 815  45  HOH   HOH A . 
D 4 HOH   116 816  80  HOH   HOH A . 
D 4 HOH   117 817  33  HOH   HOH A . 
D 4 HOH   118 818  41  HOH   HOH A . 
D 4 HOH   119 819  67  HOH   HOH A . 
D 4 HOH   120 820  232 HOH   HOH A . 
D 4 HOH   121 821  74  HOH   HOH A . 
D 4 HOH   122 822  21  HOH   HOH A . 
D 4 HOH   123 823  281 HOH   HOH A . 
D 4 HOH   124 824  118 HOH   HOH A . 
D 4 HOH   125 825  459 HOH   HOH A . 
D 4 HOH   126 826  259 HOH   HOH A . 
D 4 HOH   127 827  329 HOH   HOH A . 
D 4 HOH   128 828  411 HOH   HOH A . 
D 4 HOH   129 829  34  HOH   HOH A . 
D 4 HOH   130 830  361 HOH   HOH A . 
D 4 HOH   131 831  298 HOH   HOH A . 
D 4 HOH   132 832  160 HOH   HOH A . 
D 4 HOH   133 833  238 HOH   HOH A . 
D 4 HOH   134 834  272 HOH   HOH A . 
D 4 HOH   135 835  263 HOH   HOH A . 
D 4 HOH   136 836  412 HOH   HOH A . 
D 4 HOH   137 837  102 HOH   HOH A . 
D 4 HOH   138 838  85  HOH   HOH A . 
D 4 HOH   139 839  47  HOH   HOH A . 
D 4 HOH   140 840  537 HOH   HOH A . 
D 4 HOH   141 841  25  HOH   HOH A . 
D 4 HOH   142 842  284 HOH   HOH A . 
D 4 HOH   143 843  16  HOH   HOH A . 
D 4 HOH   144 844  219 HOH   HOH A . 
D 4 HOH   145 845  71  HOH   HOH A . 
D 4 HOH   146 846  62  HOH   HOH A . 
D 4 HOH   147 847  63  HOH   HOH A . 
D 4 HOH   148 848  185 HOH   HOH A . 
D 4 HOH   149 849  54  HOH   HOH A . 
D 4 HOH   150 850  86  HOH   HOH A . 
D 4 HOH   151 851  28  HOH   HOH A . 
D 4 HOH   152 852  64  HOH   HOH A . 
D 4 HOH   153 853  452 HOH   HOH A . 
D 4 HOH   154 854  277 HOH   HOH A . 
D 4 HOH   155 855  206 HOH   HOH A . 
D 4 HOH   156 856  349 HOH   HOH A . 
D 4 HOH   157 857  18  HOH   HOH A . 
D 4 HOH   158 858  262 HOH   HOH A . 
D 4 HOH   159 859  279 HOH   HOH A . 
D 4 HOH   160 860  290 HOH   HOH A . 
D 4 HOH   161 861  170 HOH   HOH A . 
D 4 HOH   162 862  158 HOH   HOH A . 
D 4 HOH   163 863  337 HOH   HOH A . 
D 4 HOH   164 864  269 HOH   HOH A . 
D 4 HOH   165 865  239 HOH   HOH A . 
D 4 HOH   166 866  88  HOH   HOH A . 
D 4 HOH   167 867  76  HOH   HOH A . 
D 4 HOH   168 868  82  HOH   HOH A . 
D 4 HOH   169 869  109 HOH   HOH A . 
D 4 HOH   170 870  368 HOH   HOH A . 
D 4 HOH   171 871  152 HOH   HOH A . 
D 4 HOH   172 872  372 HOH   HOH A . 
D 4 HOH   173 873  448 HOH   HOH A . 
D 4 HOH   174 874  358 HOH   HOH A . 
D 4 HOH   175 875  331 HOH   HOH A . 
D 4 HOH   176 876  53  HOH   HOH A . 
D 4 HOH   177 877  522 HOH   HOH A . 
D 4 HOH   178 878  342 HOH   HOH A . 
D 4 HOH   179 879  117 HOH   HOH A . 
D 4 HOH   180 880  135 HOH   HOH A . 
D 4 HOH   181 881  299 HOH   HOH A . 
D 4 HOH   182 882  8   HOH   HOH A . 
D 4 HOH   183 883  355 HOH   HOH A . 
D 4 HOH   184 884  164 HOH   HOH A . 
D 4 HOH   185 885  463 HOH   HOH A . 
D 4 HOH   186 886  408 HOH   HOH A . 
D 4 HOH   187 887  338 HOH   HOH A . 
D 4 HOH   188 888  155 HOH   HOH A . 
D 4 HOH   189 889  134 HOH   HOH A . 
D 4 HOH   190 890  39  HOH   HOH A . 
D 4 HOH   191 891  323 HOH   HOH A . 
D 4 HOH   192 892  50  HOH   HOH A . 
D 4 HOH   193 893  15  HOH   HOH A . 
D 4 HOH   194 894  61  HOH   HOH A . 
D 4 HOH   195 895  175 HOH   HOH A . 
D 4 HOH   196 896  213 HOH   HOH A . 
D 4 HOH   197 897  171 HOH   HOH A . 
D 4 HOH   198 898  19  HOH   HOH A . 
D 4 HOH   199 899  115 HOH   HOH A . 
D 4 HOH   200 900  154 HOH   HOH A . 
D 4 HOH   201 901  133 HOH   HOH A . 
D 4 HOH   202 902  347 HOH   HOH A . 
D 4 HOH   203 903  458 HOH   HOH A . 
D 4 HOH   204 904  348 HOH   HOH A . 
D 4 HOH   205 905  386 HOH   HOH A . 
D 4 HOH   206 906  37  HOH   HOH A . 
D 4 HOH   207 907  356 HOH   HOH A . 
D 4 HOH   208 908  545 HOH   HOH A . 
D 4 HOH   209 909  107 HOH   HOH A . 
D 4 HOH   210 910  56  HOH   HOH A . 
D 4 HOH   211 911  360 HOH   HOH A . 
D 4 HOH   212 912  73  HOH   HOH A . 
D 4 HOH   213 913  295 HOH   HOH A . 
D 4 HOH   214 914  308 HOH   HOH A . 
D 4 HOH   215 915  341 HOH   HOH A . 
D 4 HOH   216 916  173 HOH   HOH A . 
D 4 HOH   217 917  211 HOH   HOH A . 
D 4 HOH   218 918  275 HOH   HOH A . 
D 4 HOH   219 919  462 HOH   HOH A . 
D 4 HOH   220 920  297 HOH   HOH A . 
D 4 HOH   221 921  92  HOH   HOH A . 
D 4 HOH   222 922  466 HOH   HOH A . 
D 4 HOH   223 923  267 HOH   HOH A . 
D 4 HOH   224 924  353 HOH   HOH A . 
D 4 HOH   225 925  178 HOH   HOH A . 
D 4 HOH   226 926  130 HOH   HOH A . 
D 4 HOH   227 927  97  HOH   HOH A . 
D 4 HOH   228 928  43  HOH   HOH A . 
D 4 HOH   229 929  200 HOH   HOH A . 
D 4 HOH   230 930  7   HOH   HOH A . 
D 4 HOH   231 931  180 HOH   HOH A . 
D 4 HOH   232 932  365 HOH   HOH A . 
D 4 HOH   233 933  335 HOH   HOH A . 
D 4 HOH   234 934  508 HOH   HOH A . 
D 4 HOH   235 935  242 HOH   HOH A . 
D 4 HOH   236 936  426 HOH   HOH A . 
D 4 HOH   237 937  430 HOH   HOH A . 
D 4 HOH   238 938  36  HOH   HOH A . 
D 4 HOH   239 939  542 HOH   HOH A . 
D 4 HOH   240 940  230 HOH   HOH A . 
D 4 HOH   241 941  403 HOH   HOH A . 
D 4 HOH   242 942  208 HOH   HOH A . 
D 4 HOH   243 943  476 HOH   HOH A . 
D 4 HOH   244 944  11  HOH   HOH A . 
D 4 HOH   245 945  228 HOH   HOH A . 
D 4 HOH   246 946  177 HOH   HOH A . 
D 4 HOH   247 947  352 HOH   HOH A . 
D 4 HOH   248 948  280 HOH   HOH A . 
D 4 HOH   249 949  68  HOH   HOH A . 
D 4 HOH   250 950  421 HOH   HOH A . 
D 4 HOH   251 951  354 HOH   HOH A . 
D 4 HOH   252 952  23  HOH   HOH A . 
D 4 HOH   253 953  94  HOH   HOH A . 
D 4 HOH   254 954  103 HOH   HOH A . 
D 4 HOH   255 955  55  HOH   HOH A . 
D 4 HOH   256 956  261 HOH   HOH A . 
D 4 HOH   257 957  101 HOH   HOH A . 
D 4 HOH   258 958  220 HOH   HOH A . 
D 4 HOH   259 959  20  HOH   HOH A . 
D 4 HOH   260 960  362 HOH   HOH A . 
D 4 HOH   261 961  456 HOH   HOH A . 
D 4 HOH   262 962  96  HOH   HOH A . 
D 4 HOH   263 963  84  HOH   HOH A . 
D 4 HOH   264 964  157 HOH   HOH A . 
D 4 HOH   265 965  17  HOH   HOH A . 
D 4 HOH   266 966  523 HOH   HOH A . 
D 4 HOH   267 967  274 HOH   HOH A . 
D 4 HOH   268 968  161 HOH   HOH A . 
D 4 HOH   269 969  120 HOH   HOH A . 
D 4 HOH   270 970  256 HOH   HOH A . 
D 4 HOH   271 971  333 HOH   HOH A . 
D 4 HOH   272 972  283 HOH   HOH A . 
D 4 HOH   273 973  203 HOH   HOH A . 
D 4 HOH   274 974  276 HOH   HOH A . 
D 4 HOH   275 975  114 HOH   HOH A . 
D 4 HOH   276 976  121 HOH   HOH A . 
D 4 HOH   277 977  287 HOH   HOH A . 
D 4 HOH   278 978  119 HOH   HOH A . 
D 4 HOH   279 979  182 HOH   HOH A . 
D 4 HOH   280 980  181 HOH   HOH A . 
D 4 HOH   281 981  142 HOH   HOH A . 
D 4 HOH   282 982  519 HOH   HOH A . 
D 4 HOH   283 983  248 HOH   HOH A . 
D 4 HOH   284 984  314 HOH   HOH A . 
D 4 HOH   285 985  346 HOH   HOH A . 
D 4 HOH   286 986  552 HOH   HOH A . 
D 4 HOH   287 987  332 HOH   HOH A . 
D 4 HOH   288 988  388 HOH   HOH A . 
D 4 HOH   289 989  315 HOH   HOH A . 
D 4 HOH   290 990  210 HOH   HOH A . 
D 4 HOH   291 991  168 HOH   HOH A . 
D 4 HOH   292 992  98  HOH   HOH A . 
D 4 HOH   293 993  328 HOH   HOH A . 
D 4 HOH   294 994  305 HOH   HOH A . 
D 4 HOH   295 995  505 HOH   HOH A . 
D 4 HOH   296 996  124 HOH   HOH A . 
D 4 HOH   297 997  79  HOH   HOH A . 
D 4 HOH   298 998  169 HOH   HOH A . 
D 4 HOH   299 999  310 HOH   HOH A . 
D 4 HOH   300 1000 321 HOH   HOH A . 
D 4 HOH   301 1001 176 HOH   HOH A . 
D 4 HOH   302 1002 471 HOH   HOH A . 
D 4 HOH   303 1003 91  HOH   HOH A . 
D 4 HOH   304 1004 44  HOH   HOH A . 
D 4 HOH   305 1005 306 HOH   HOH A . 
D 4 HOH   306 1006 104 HOH   HOH A . 
D 4 HOH   307 1007 304 HOH   HOH A . 
D 4 HOH   308 1008 377 HOH   HOH A . 
D 4 HOH   309 1009 163 HOH   HOH A . 
D 4 HOH   310 1010 123 HOH   HOH A . 
D 4 HOH   311 1011 316 HOH   HOH A . 
D 4 HOH   312 1012 13  HOH   HOH A . 
D 4 HOH   313 1013 271 HOH   HOH A . 
D 4 HOH   314 1014 343 HOH   HOH A . 
D 4 HOH   315 1015 48  HOH   HOH A . 
D 4 HOH   316 1016 253 HOH   HOH A . 
D 4 HOH   317 1017 296 HOH   HOH A . 
D 4 HOH   318 1018 24  HOH   HOH A . 
D 4 HOH   319 1019 143 HOH   HOH A . 
D 4 HOH   320 1020 137 HOH   HOH A . 
D 4 HOH   321 1021 100 HOH   HOH A . 
D 4 HOH   322 1022 327 HOH   HOH A . 
D 4 HOH   323 1023 363 HOH   HOH A . 
D 4 HOH   324 1024 78  HOH   HOH A . 
D 4 HOH   325 1025 14  HOH   HOH A . 
D 4 HOH   326 1026 110 HOH   HOH A . 
D 4 HOH   327 1027 325 HOH   HOH A . 
D 4 HOH   328 1028 394 HOH   HOH A . 
D 4 HOH   329 1029 145 HOH   HOH A . 
D 4 HOH   330 1030 87  HOH   HOH A . 
D 4 HOH   331 1031 278 HOH   HOH A . 
D 4 HOH   332 1032 222 HOH   HOH A . 
D 4 HOH   333 1033 235 HOH   HOH A . 
D 4 HOH   334 1034 113 HOH   HOH A . 
D 4 HOH   335 1035 141 HOH   HOH A . 
D 4 HOH   336 1036 30  HOH   HOH A . 
D 4 HOH   337 1037 344 HOH   HOH A . 
D 4 HOH   338 1038 65  HOH   HOH A . 
D 4 HOH   339 1039 250 HOH   HOH A . 
D 4 HOH   340 1040 376 HOH   HOH A . 
D 4 HOH   341 1041 477 HOH   HOH A . 
D 4 HOH   342 1042 289 HOH   HOH A . 
D 4 HOH   343 1043 147 HOH   HOH A . 
D 4 HOH   344 1044 475 HOH   HOH A . 
D 4 HOH   345 1045 282 HOH   HOH A . 
D 4 HOH   346 1046 72  HOH   HOH A . 
D 4 HOH   347 1047 516 HOH   HOH A . 
D 4 HOH   348 1048 474 HOH   HOH A . 
D 4 HOH   349 1049 187 HOH   HOH A . 
D 4 HOH   350 1050 131 HOH   HOH A . 
D 4 HOH   351 1051 105 HOH   HOH A . 
D 4 HOH   352 1052 217 HOH   HOH A . 
D 4 HOH   353 1053 345 HOH   HOH A . 
D 4 HOH   354 1054 383 HOH   HOH A . 
D 4 HOH   355 1055 89  HOH   HOH A . 
D 4 HOH   356 1056 10  HOH   HOH A . 
D 4 HOH   357 1057 251 HOH   HOH A . 
D 4 HOH   358 1058 144 HOH   HOH A . 
D 4 HOH   359 1059 270 HOH   HOH A . 
D 4 HOH   360 1060 425 HOH   HOH A . 
D 4 HOH   361 1061 371 HOH   HOH A . 
D 4 HOH   362 1062 527 HOH   HOH A . 
D 4 HOH   363 1063 402 HOH   HOH A . 
D 4 HOH   364 1064 509 HOH   HOH A . 
D 4 HOH   365 1065 212 HOH   HOH A . 
D 4 HOH   366 1066 539 HOH   HOH A . 
D 4 HOH   367 1067 446 HOH   HOH A . 
D 4 HOH   368 1068 555 HOH   HOH A . 
D 4 HOH   369 1069 81  HOH   HOH A . 
D 4 HOH   370 1070 231 HOH   HOH A . 
D 4 HOH   371 1071 205 HOH   HOH A . 
D 4 HOH   372 1072 149 HOH   HOH A . 
D 4 HOH   373 1073 90  HOH   HOH A . 
D 4 HOH   374 1074 397 HOH   HOH A . 
D 4 HOH   375 1075 518 HOH   HOH A . 
D 4 HOH   376 1076 313 HOH   HOH A . 
D 4 HOH   377 1077 491 HOH   HOH A . 
D 4 HOH   378 1078 455 HOH   HOH A . 
D 4 HOH   379 1079 445 HOH   HOH A . 
D 4 HOH   380 1080 366 HOH   HOH A . 
D 4 HOH   381 1081 501 HOH   HOH A . 
D 4 HOH   382 1082 395 HOH   HOH A . 
D 4 HOH   383 1083 184 HOH   HOH A . 
D 4 HOH   384 1084 9   HOH   HOH A . 
D 4 HOH   385 1085 122 HOH   HOH A . 
D 4 HOH   386 1086 326 HOH   HOH A . 
D 4 HOH   387 1087 359 HOH   HOH A . 
D 4 HOH   388 1088 240 HOH   HOH A . 
D 4 HOH   389 1089 188 HOH   HOH A . 
D 4 HOH   390 1090 334 HOH   HOH A . 
D 4 HOH   391 1091 312 HOH   HOH A . 
D 4 HOH   392 1092 307 HOH   HOH A . 
D 4 HOH   393 1093 436 HOH   HOH A . 
D 4 HOH   394 1094 249 HOH   HOH A . 
D 4 HOH   395 1095 77  HOH   HOH A . 
D 4 HOH   396 1096 320 HOH   HOH A . 
D 4 HOH   397 1097 484 HOH   HOH A . 
D 4 HOH   398 1098 398 HOH   HOH A . 
D 4 HOH   399 1099 538 HOH   HOH A . 
D 4 HOH   400 1100 99  HOH   HOH A . 
D 4 HOH   401 1101 244 HOH   HOH A . 
D 4 HOH   402 1102 324 HOH   HOH A . 
D 4 HOH   403 1103 493 HOH   HOH A . 
D 4 HOH   404 1104 457 HOH   HOH A . 
D 4 HOH   405 1105 473 HOH   HOH A . 
D 4 HOH   406 1106 495 HOH   HOH A . 
D 4 HOH   407 1107 461 HOH   HOH A . 
D 4 HOH   408 1108 51  HOH   HOH A . 
D 4 HOH   409 1109 202 HOH   HOH A . 
D 4 HOH   410 1110 465 HOH   HOH A . 
D 4 HOH   411 1111 500 HOH   HOH A . 
D 4 HOH   412 1112 186 HOH   HOH A . 
D 4 HOH   413 1113 227 HOH   HOH A . 
D 4 HOH   414 1114 510 HOH   HOH A . 
D 4 HOH   415 1115 404 HOH   HOH A . 
D 4 HOH   416 1116 533 HOH   HOH A . 
D 4 HOH   417 1117 255 HOH   HOH A . 
D 4 HOH   418 1118 351 HOH   HOH A . 
D 4 HOH   419 1119 416 HOH   HOH A . 
D 4 HOH   420 1120 294 HOH   HOH A . 
D 4 HOH   421 1121 111 HOH   HOH A . 
D 4 HOH   422 1122 517 HOH   HOH A . 
D 4 HOH   423 1123 506 HOH   HOH A . 
D 4 HOH   424 1124 373 HOH   HOH A . 
D 4 HOH   425 1125 504 HOH   HOH A . 
D 4 HOH   426 1126 156 HOH   HOH A . 
D 4 HOH   427 1127 444 HOH   HOH A . 
D 4 HOH   428 1128 410 HOH   HOH A . 
D 4 HOH   429 1129 204 HOH   HOH A . 
D 4 HOH   430 1130 215 HOH   HOH A . 
D 4 HOH   431 1131 318 HOH   HOH A . 
D 4 HOH   432 1132 292 HOH   HOH A . 
D 4 HOH   433 1133 499 HOH   HOH A . 
D 4 HOH   434 1134 66  HOH   HOH A . 
D 4 HOH   435 1135 233 HOH   HOH A . 
D 4 HOH   436 1136 196 HOH   HOH A . 
D 4 HOH   437 1137 201 HOH   HOH A . 
D 4 HOH   438 1138 540 HOH   HOH A . 
D 4 HOH   439 1139 336 HOH   HOH A . 
D 4 HOH   440 1140 447 HOH   HOH A . 
D 4 HOH   441 1141 550 HOH   HOH A . 
D 4 HOH   442 1142 339 HOH   HOH A . 
D 4 HOH   443 1143 108 HOH   HOH A . 
D 4 HOH   444 1144 480 HOH   HOH A . 
D 4 HOH   445 1145 515 HOH   HOH A . 
D 4 HOH   446 1146 507 HOH   HOH A . 
D 4 HOH   447 1147 534 HOH   HOH A . 
D 4 HOH   448 1148 390 HOH   HOH A . 
D 4 HOH   449 1149 139 HOH   HOH A . 
D 4 HOH   450 1150 391 HOH   HOH A . 
D 4 HOH   451 1151 453 HOH   HOH A . 
D 4 HOH   452 1152 409 HOH   HOH A . 
D 4 HOH   453 1153 521 HOH   HOH A . 
D 4 HOH   454 1154 498 HOH   HOH A . 
D 4 HOH   455 1155 511 HOH   HOH A . 
D 4 HOH   456 1156 513 HOH   HOH A . 
D 4 HOH   457 1157 257 HOH   HOH A . 
D 4 HOH   458 1158 191 HOH   HOH A . 
D 4 HOH   459 1159 303 HOH   HOH A . 
D 4 HOH   460 1160 229 HOH   HOH A . 
D 4 HOH   461 1161 429 HOH   HOH A . 
D 4 HOH   462 1162 556 HOH   HOH A . 
D 4 HOH   463 1163 490 HOH   HOH A . 
D 4 HOH   464 1164 183 HOH   HOH A . 
D 4 HOH   465 1165 166 HOH   HOH A . 
D 4 HOH   466 1166 485 HOH   HOH A . 
D 4 HOH   467 1167 415 HOH   HOH A . 
D 4 HOH   468 1168 396 HOH   HOH A . 
D 4 HOH   469 1169 524 HOH   HOH A . 
D 4 HOH   470 1170 492 HOH   HOH A . 
D 4 HOH   471 1171 467 HOH   HOH A . 
D 4 HOH   472 1172 543 HOH   HOH A . 
D 4 HOH   473 1173 198 HOH   HOH A . 
D 4 HOH   474 1174 214 HOH   HOH A . 
D 4 HOH   475 1175 319 HOH   HOH A . 
D 4 HOH   476 1176 194 HOH   HOH A . 
D 4 HOH   477 1177 439 HOH   HOH A . 
D 4 HOH   478 1178 449 HOH   HOH A . 
D 4 HOH   479 1179 190 HOH   HOH A . 
D 4 HOH   480 1180 442 HOH   HOH A . 
D 4 HOH   481 1181 423 HOH   HOH A . 
D 4 HOH   482 1182 223 HOH   HOH A . 
D 4 HOH   483 1183 488 HOH   HOH A . 
D 4 HOH   484 1184 553 HOH   HOH A . 
D 4 HOH   485 1185 340 HOH   HOH A . 
D 4 HOH   486 1186 197 HOH   HOH A . 
D 4 HOH   487 1187 407 HOH   HOH A . 
D 4 HOH   488 1188 146 HOH   HOH A . 
D 4 HOH   489 1189 530 HOH   HOH A . 
D 4 HOH   490 1190 291 HOH   HOH A . 
D 4 HOH   491 1191 497 HOH   HOH A . 
D 4 HOH   492 1192 528 HOH   HOH A . 
D 4 HOH   493 1193 464 HOH   HOH A . 
D 4 HOH   494 1194 514 HOH   HOH A . 
D 4 HOH   495 1195 311 HOH   HOH A . 
D 4 HOH   496 1196 460 HOH   HOH A . 
D 4 HOH   497 1197 288 HOH   HOH A . 
D 4 HOH   498 1198 405 HOH   HOH A . 
D 4 HOH   499 1199 486 HOH   HOH A . 
D 4 HOH   500 1200 379 HOH   HOH A . 
D 4 HOH   501 1201 189 HOH   HOH A . 
D 4 HOH   502 1202 544 HOH   HOH A . 
D 4 HOH   503 1203 557 HOH   HOH A . 
D 4 HOH   504 1204 302 HOH   HOH A . 
D 4 HOH   505 1205 125 HOH   HOH A . 
D 4 HOH   506 1206 496 HOH   HOH A . 
D 4 HOH   507 1207 450 HOH   HOH A . 
D 4 HOH   508 1208 364 HOH   HOH A . 
D 4 HOH   509 1209 374 HOH   HOH A . 
D 4 HOH   510 1210 192 HOH   HOH A . 
D 4 HOH   511 1211 546 HOH   HOH A . 
D 4 HOH   512 1212 440 HOH   HOH A . 
D 4 HOH   513 1213 367 HOH   HOH A . 
D 4 HOH   514 1214 381 HOH   HOH A . 
D 4 HOH   515 1215 547 HOH   HOH A . 
D 4 HOH   516 1216 179 HOH   HOH A . 
D 4 HOH   517 1217 384 HOH   HOH A . 
D 4 HOH   518 1218 548 HOH   HOH A . 
D 4 HOH   519 1219 472 HOH   HOH A . 
D 4 HOH   520 1220 417 HOH   HOH A . 
D 4 HOH   521 1221 433 HOH   HOH A . 
D 4 HOH   522 1222 136 HOH   HOH A . 
D 4 HOH   523 1223 83  HOH   HOH A . 
D 4 HOH   524 1224 554 HOH   HOH A . 
D 4 HOH   525 1225 535 HOH   HOH A . 
D 4 HOH   526 1226 435 HOH   HOH A . 
D 4 HOH   527 1227 254 HOH   HOH A . 
D 4 HOH   528 1228 437 HOH   HOH A . 
D 4 HOH   529 1229 225 HOH   HOH A . 
D 4 HOH   530 1230 165 HOH   HOH A . 
D 4 HOH   531 1231 487 HOH   HOH A . 
D 4 HOH   532 1232 536 HOH   HOH A . 
D 4 HOH   533 1233 503 HOH   HOH A . 
D 4 HOH   534 1234 199 HOH   HOH A . 
D 4 HOH   535 1235 369 HOH   HOH A . 
D 4 HOH   536 1236 370 HOH   HOH A . 
D 4 HOH   537 1237 380 HOH   HOH A . 
D 4 HOH   538 1238 427 HOH   HOH A . 
D 4 HOH   539 1239 432 HOH   HOH A . 
D 4 HOH   540 1240 224 HOH   HOH A . 
D 4 HOH   541 1241 293 HOH   HOH A . 
D 4 HOH   542 1242 26  HOH   HOH A . 
D 4 HOH   543 1243 532 HOH   HOH A . 
D 4 HOH   544 1244 494 HOH   HOH A . 
D 4 HOH   545 1245 159 HOH   HOH A . 
D 4 HOH   546 1246 406 HOH   HOH A . 
D 4 HOH   547 1247 502 HOH   HOH A . 
D 4 HOH   548 1248 443 HOH   HOH A . 
D 4 HOH   549 1249 243 HOH   HOH A . 
D 4 HOH   550 1250 226 HOH   HOH A . 
D 4 HOH   551 1251 193 HOH   HOH A . 
D 4 HOH   552 1252 451 HOH   HOH A . 
D 4 HOH   553 1253 195 HOH   HOH A . 
D 4 HOH   554 1254 483 HOH   HOH A . 
D 4 HOH   555 1255 431 HOH   HOH A . 
D 4 HOH   556 1256 420 HOH   HOH A . 
D 4 HOH   557 1257 526 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       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KWL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     110.469 
_cell.length_a_esd                 ? 
_cell.length_b                     110.469 
_cell.length_b_esd                 ? 
_cell.length_c                     278.259 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_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                         9KWL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                155 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9KWL 
_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             2.78 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.73 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '14.4% PEG8000(w/v), 0.1M MES 6.4, 0.3M CaAc' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-08-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9789 
_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                        'SSRF BEAMLINE BL17U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9789 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL17U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KWL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.83 
_reflns.d_resolution_low                               78.83 
_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                                     111183 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.205 
_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                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.83 
_reflns_shell.d_res_low                                     1.90 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             57812 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.205 
_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                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9KWL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.83 
_refine.ls_d_res_low                             56.26 
_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                     111183 
_refine.ls_number_reflns_R_free                  3870 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.54 
_refine.ls_percent_reflns_R_free                 3.48 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1722 
_refine.ls_R_factor_R_free                       0.1857 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1717 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 18.75 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4139 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         15 
_refine_hist.number_atoms_solvent             557 
_refine_hist.number_atoms_total               4711 
_refine_hist.d_res_high                       1.83 
_refine_hist.d_res_low                        56.26 
# 
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' ? 5.723 ? 563 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.058 ? 641 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007 ? 743 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.83 1.85 . . 123 3640 94.00  . . . . 0.2795 . . . . . . . . . . . 0.2801 
'X-RAY DIFFRACTION' 1.85 1.88 . . 140 3763 97.00  . . . . 0.2782 . . . . . . . . . . . 0.2934 
'X-RAY DIFFRACTION' 1.88 1.90 . . 126 3762 99.00  . . . . 0.2677 . . . . . . . . . . . 0.2952 
'X-RAY DIFFRACTION' 1.90 1.93 . . 145 3812 99.00  . . . . 0.2575 . . . . . . . . . . . 0.2651 
'X-RAY DIFFRACTION' 1.95 1.98 . . 148 3868 100.00 . . . . 0.2302 . . . . . . . . . . . 0.2329 
'X-RAY DIFFRACTION' 1.98 2.01 . . 144 3854 100.00 . . . . 0.2148 . . . . . . . . . . . 0.2326 
'X-RAY DIFFRACTION' 2.01 2.05 . . 155 3874 100.00 . . . . 0.2112 . . . . . . . . . . . 0.2619 
'X-RAY DIFFRACTION' 2.05 2.08 . . 123 3820 100.00 . . . . 0.1938 . . . . . . . . . . . 0.2066 
'X-RAY DIFFRACTION' 2.08 2.12 . . 146 3876 100.00 . . . . 0.1939 . . . . . . . . . . . 0.1970 
'X-RAY DIFFRACTION' 2.16 2.21 . . 138 3867 100.00 . . . . 0.1737 . . . . . . . . . . . 0.2095 
'X-RAY DIFFRACTION' 2.21 2.25 . . 139 3881 100.00 . . . . 0.1856 . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 2.25 2.31 . . 120 3827 100.00 . . . . 0.1819 . . . . . . . . . . . 0.2159 
'X-RAY DIFFRACTION' 2.31 2.36 . . 139 3829 100.00 . . . . 0.1812 . . . . . . . . . . . 0.2240 
'X-RAY DIFFRACTION' 2.36 2.43 . . 134 3851 100.00 . . . . 0.1814 . . . . . . . . . . . 0.2066 
'X-RAY DIFFRACTION' 2.43 2.50 . . 144 3855 100.00 . . . . 0.1735 . . . . . . . . . . . 0.1914 
'X-RAY DIFFRACTION' 2.50 2.58 . . 134 3829 100.00 . . . . 0.1807 . . . . . . . . . . . 0.1937 
'X-RAY DIFFRACTION' 2.58 2.67 . . 134 3892 100.00 . . . . 0.1717 . . . . . . . . . . . 0.2206 
'X-RAY DIFFRACTION' 2.67 2.78 . . 142 3803 100.00 . . . . 0.1679 . . . . . . . . . . . 0.2173 
# 
_struct.entry_id                     9KWL 
_struct.title                        'hCES1A contently binding with compound F-3 at the catalytic pocket.' 
_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        9KWL 
_struct_keywords.text            'hCES1A, Covalent, Inhibitors, SBDD, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    EST1_HUMAN 
_struct_ref.pdbx_db_accession          P23141 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSEL
FTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST
GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGD
VKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLKMKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERN
FHTVPYMVGINKQEFGWLIPMQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDL
IADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFW
ANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKDKEVAFWTNLFAK
;
_struct_ref.pdbx_align_begin           21 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9KWL 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 533 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P23141 
_struct_ref_seq.db_align_beg                  21 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  553 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       4 
_struct_ref_seq.pdbx_auth_seq_align_end       536 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9KWL GLN A 341 ? UNP P23141 MET 361 conflict 344 1 
1 9KWL MET A 342 ? UNP P23141 GLN 362 conflict 345 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   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)' 100   ? 
1 MORE         -6    ? 
1 'SSA (A^2)'  20320 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LEU A 40  ? ARG A 44  ? LEU A 43  ARG A 47  5 ? 5  
HELX_P HELX_P2  AA2 ASP A 70  ? THR A 82  ? ASP A 73  THR A 85  1 ? 13 
HELX_P HELX_P3  AA3 ALA A 128 ? TYR A 132 ? ALA A 131 TYR A 135 5 ? 5  
HELX_P HELX_P4  AA4 GLY A 134 ? ASN A 142 ? GLY A 137 ASN A 145 1 ? 9  
HELX_P HELX_P5  AA5 LEU A 152 ? PHE A 158 ? LEU A 155 PHE A 161 1 ? 7  
HELX_P HELX_P6  AA6 ASN A 168 ? ILE A 185 ? ASN A 171 ILE A 188 1 ? 18 
HELX_P HELX_P7  AA7 ALA A 186 ? PHE A 188 ? ALA A 189 PHE A 191 5 ? 3  
HELX_P HELX_P8  AA8 SER A 201 ? LEU A 212 ? SER A 204 LEU A 215 1 ? 12 
HELX_P HELX_P9  AA9 SER A 213 ? LYS A 217 ? SER A 216 LYS A 220 5 ? 5  
HELX_P HELX_P10 AB1 THR A 232 ? VAL A 236 ? THR A 235 VAL A 239 5 ? 5  
HELX_P HELX_P11 AB2 VAL A 241 ? GLY A 253 ? VAL A 244 GLY A 256 1 ? 13 
HELX_P HELX_P12 AB3 THR A 258 ? LYS A 269 ? THR A 261 LYS A 272 1 ? 12 
HELX_P HELX_P13 AB4 THR A 270 ? LYS A 282 ? THR A 273 LYS A 285 1 ? 13 
HELX_P HELX_P14 AB5 ASP A 291 ? SER A 295 ? ASP A 294 SER A 298 5 ? 5  
HELX_P HELX_P15 AB6 THR A 311 ? ARG A 319 ? THR A 314 ARG A 322 1 ? 9  
HELX_P HELX_P16 AB7 TRP A 337 ? MET A 342 ? TRP A 340 MET A 345 1 ? 6  
HELX_P HELX_P17 AB8 ASP A 354 ? SER A 365 ? ASP A 357 SER A 368 1 ? 12 
HELX_P HELX_P18 AB9 SER A 365 ? CYS A 370 ? SER A 368 CYS A 373 1 ? 6  
HELX_P HELX_P19 AC1 ALA A 372 ? GLU A 374 ? ALA A 375 GLU A 377 5 ? 3  
HELX_P HELX_P20 AC2 LEU A 375 ? GLY A 385 ? LEU A 378 GLY A 388 1 ? 11 
HELX_P HELX_P21 AC3 ASP A 389 ? PHE A 406 ? ASP A 392 PHE A 409 1 ? 18 
HELX_P HELX_P22 AC4 PHE A 406 ? ALA A 420 ? PHE A 409 ALA A 423 1 ? 15 
HELX_P HELX_P23 AC5 GLU A 451 ? PHE A 456 ? GLU A 454 PHE A 459 1 ? 6  
HELX_P HELX_P24 AC6 GLY A 457 ? LEU A 461 ? GLY A 460 LEU A 464 5 ? 5  
HELX_P HELX_P25 AC7 SER A 466 ? GLY A 487 ? SER A 469 GLY A 490 1 ? 22 
HELX_P HELX_P26 AC8 LYS A 520 ? ALA A 532 ? LYS A 523 ALA A 535 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 67  SG  ? ? ? 1_555 A CYS   96  SG  ? ? A CYS 70  A CYS   99   1_555 ? ? ? ? ? ? ? 2.026 ? ? 
disulf2 disulf ?    ? A CYS 254 SG  ? ? ? 1_555 A CYS   265 SG  ? ? A CYS 257 A CYS   268  1_555 ? ? ? ? ? ? ? 2.096 ? ? 
covale1 covale none ? A SER 201 OG  ? ? ? 1_555 B A1EIY .   C07 ? ? A SER 204 A A1EIY 601  1_555 ? ? ? ? ? ? ? 1.380 ? ? 
metalc1 metalc ?    ? A ASP 287 OD1 ? ? ? 1_555 C MG    .   MG  ? ? A ASP 290 A MG    602  1_555 ? ? ? ? ? ? ? 2.662 ? ? 
metalc2 metalc ?    ? A ASP 287 OD2 ? ? ? 1_555 C MG    .   MG  ? ? A ASP 290 A MG    602  1_555 ? ? ? ? ? ? ? 2.515 ? ? 
metalc3 metalc ?    ? A GLN 289 O   ? ? ? 1_555 C MG    .   MG  ? ? A GLN 292 A MG    602  1_555 ? ? ? ? ? ? ? 2.253 ? ? 
metalc4 metalc ?    ? A GLU 350 OE1 ? ? ? 1_555 C MG    .   MG  ? ? A GLU 353 A MG    602  4_555 ? ? ? ? ? ? ? 2.765 ? ? 
metalc5 metalc ?    ? A GLU 350 OE2 ? ? ? 1_555 C MG    .   MG  ? ? A GLU 353 A MG    602  4_555 ? ? ? ? ? ? ? 2.552 ? ? 
metalc6 metalc ?    ? C MG  .   MG  ? ? ? 1_555 D HOH   .   O   ? ? A MG  602 A HOH   864  1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc7 metalc ?    ? C MG  .   MG  ? ? ? 1_555 D HOH   .   O   ? ? A MG  602 A HOH   1091 1_555 ? ? ? ? ? ? ? 2.395 ? ? 
metalc8 metalc ?    ? C MG  .   MG  ? ? ? 1_555 D HOH   .   O   ? ? A MG  602 A HOH   1118 1_555 ? ? ? ? ? ? ? 2.439 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 OD2 ? A ASP 287 ? A ASP 290  ? 1_555 50.2  ? 
2  OD1 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? A GLN 289 ? A GLN 292  ? 1_555 79.0  ? 
3  OD2 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? A GLN 289 ? A GLN 292  ? 1_555 128.8 ? 
4  OD1 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 OE1 ? A GLU 350 ? A GLU 353  ? 1_555 25.7  ? 
5  OD2 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 OE1 ? A GLU 350 ? A GLU 353  ? 1_555 75.3  ? 
6  O   ? A GLN 289 ? A GLN 292  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 OE1 ? A GLU 350 ? A GLU 353  ? 1_555 53.5  ? 
7  OD1 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 OE2 ? A GLU 350 ? A GLU 353  ? 1_555 25.4  ? 
8  OD2 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 OE2 ? A GLU 350 ? A GLU 353  ? 1_555 75.6  ? 
9  O   ? A GLN 289 ? A GLN 292  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 OE2 ? A GLU 350 ? A GLU 353  ? 1_555 53.8  ? 
10 OE1 ? A GLU 350 ? A GLU 353  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 OE2 ? A GLU 350 ? A GLU 353  ? 1_555 5.4   ? 
11 OD1 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 864  ? 1_555 78.6  ? 
12 OD2 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 864  ? 1_555 76.3  ? 
13 O   ? A GLN 289 ? A GLN 292  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 864  ? 1_555 89.4  ? 
14 OE1 ? A GLU 350 ? A GLU 353  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 864  ? 1_555 77.4  ? 
15 OE2 ? A GLU 350 ? A GLU 353  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 864  ? 1_555 82.8  ? 
16 OD1 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1091 ? 1_555 157.0 ? 
17 OD2 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1091 ? 1_555 142.2 ? 
18 O   ? A GLN 289 ? A GLN 292  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1091 ? 1_555 83.5  ? 
19 OE1 ? A GLU 350 ? A GLU 353  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1091 ? 1_555 133.5 ? 
20 OE2 ? A GLU 350 ? A GLU 353  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1091 ? 1_555 135.8 ? 
21 O   ? D HOH .   ? A HOH 864  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1091 ? 1_555 86.4  ? 
22 OD1 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1118 ? 1_555 129.7 ? 
23 OD2 ? A ASP 287 ? A ASP 290  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1118 ? 1_555 81.0  ? 
24 O   ? A GLN 289 ? A GLN 292  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1118 ? 1_555 149.8 ? 
25 OE1 ? A GLU 350 ? A GLU 353  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1118 ? 1_555 155.3 ? 
26 OE2 ? A GLU 350 ? A GLU 353  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1118 ? 1_555 153.4 ? 
27 O   ? D HOH .   ? A HOH 864  ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1118 ? 1_555 103.9 ? 
28 O   ? D HOH .   ? A HOH 1091 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? D HOH .   ? A HOH 1118 ? 1_555 70.8  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 A1EIY B .   ? SER A 201 ? A1EIY A 601 ? 1_555 SER A 204 ? 1_555 C07 OG SER 1 A1EIY None 'Covalent chemical modification' 
2 CYS   A 67  ? CYS A 96  ? CYS   A 70  ? 1_555 CYS A 99  ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
3 CYS   A 254 ? CYS A 265 ? CYS   A 257 ? 1_555 CYS A 268 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3  ? 
AA2 ? 11 ? 
AA3 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? parallel      
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? parallel      
AA2 5  6  ? parallel      
AA2 6  7  ? parallel      
AA2 7  8  ? parallel      
AA2 8  9  ? parallel      
AA2 9  10 ? parallel      
AA2 10 11 ? anti-parallel 
AA3 1  2  ? 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  VAL A 5   ? THR A 8   ? VAL A 8   THR A 11  
AA1 2  GLY A 11  ? LEU A 14  ? GLY A 14  LEU A 17  
AA1 3  VAL A 57  ? ASN A 59  ? VAL A 60  ASN A 62  
AA2 1  LYS A 16  ? VAL A 18  ? LYS A 19  VAL A 21  
AA2 2  VAL A 27  ? PRO A 34  ? VAL A 30  PRO A 37  
AA2 3  TYR A 98  ? THR A 103 ? TYR A 101 THR A 106 
AA2 4  VAL A 144 ? ILE A 148 ? VAL A 147 ILE A 151 
AA2 5  LEU A 113 ? ILE A 119 ? LEU A 116 ILE A 122 
AA2 6  GLY A 190 ? GLU A 200 ? GLY A 193 GLU A 203 
AA2 7  ARG A 222 ? GLU A 226 ? ARG A 225 GLU A 229 
AA2 8  TYR A 326 ? ASN A 331 ? TYR A 329 ASN A 334 
AA2 9  THR A 424 ? GLN A 430 ? THR A 427 GLN A 433 
AA2 10 GLY A 505 ? GLY A 510 ? GLY A 508 GLY A 513 
AA2 11 GLN A 514 ? GLN A 517 ? GLN A 517 GLN A 520 
AA3 1  MET A 66  ? CYS A 67  ? MET A 69  CYS A 70  
AA3 2  LEU A 92  ? SER A 93  ? LEU A 95  SER A 96  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N VAL A 6   ? N VAL A 9   O VAL A 13  ? O VAL A 16  
AA1 2  3  N LYS A 12  ? N LYS A 15  O LYS A 58  ? O LYS A 61  
AA2 1  2  N LYS A 16  ? N LYS A 19  O ILE A 29  ? O ILE A 32  
AA2 2  3  N PHE A 30  ? N PHE A 33  O ILE A 101 ? O ILE A 104 
AA2 3  4  N TYR A 102 ? N TYR A 105 O VAL A 145 ? O VAL A 148 
AA2 4  5  O VAL A 146 ? O VAL A 149 N TRP A 118 ? N TRP A 121 
AA2 5  6  N LEU A 113 ? N LEU A 116 O ASN A 191 ? O ASN A 194 
AA2 6  7  N GLY A 199 ? N GLY A 202 O GLU A 226 ? O GLU A 229 
AA2 7  8  N ALA A 223 ? N ALA A 226 O MET A 327 ? O MET A 330 
AA2 8  9  N VAL A 328 ? N VAL A 331 O TYR A 425 ? O TYR A 428 
AA2 9  10 N GLN A 430 ? N GLN A 433 O ILE A 509 ? O ILE A 512 
AA2 10 11 N TYR A 506 ? N TYR A 509 O ALA A 516 ? O ALA A 519 
AA3 1  2  N MET A 66  ? N MET A 69  O SER A 93  ? O SER A 96  
# 
_pdbx_entry_details.entry_id                   9KWL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 1138 ? ? O A HOH 1203 ? ? 1.83 
2  1 O   A SER 4    ? ? O A HOH 701  ? ? 1.86 
3  1 OE2 A GLU 381  ? ? O A HOH 702  ? ? 1.91 
4  1 O   A HOH 932  ? ? O A HOH 1221 ? ? 1.97 
5  1 O   A HOH 995  ? ? O A HOH 1068 ? ? 2.01 
6  1 O   A HOH 713  ? ? O A HOH 924  ? ? 2.01 
7  1 O   A HOH 790  ? ? O A HOH 1011 ? ? 2.02 
8  1 O   A HOH 1180 ? ? O A HOH 1221 ? ? 2.08 
9  1 O   A HOH 922  ? ? O A HOH 1153 ? ? 2.10 
10 1 O   A HOH 925  ? ? O A HOH 1182 ? ? 2.10 
11 1 O   A HOH 957  ? ? O A HOH 1129 ? ? 2.11 
12 1 O   A HOH 732  ? ? O A HOH 1116 ? ? 2.12 
13 1 O   A HOH 1141 ? ? O A HOH 1203 ? ? 2.15 
14 1 NZ  A LYS 240  ? ? O A HOH 703  ? ? 2.17 
15 1 O   A HOH 712  ? ? O A HOH 1066 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     840 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     1099 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_555 
_pdbx_validate_symm_contact.dist              2.05 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 59  ? ? 64.83   -153.52 
2  1 ALA A 63  ? ? -113.74 62.48   
3  1 ASP A 73  ? ? -54.45  109.45  
4  1 SER A 168 ? ? -159.86 85.85   
5  1 SER A 204 ? ? 62.75   -124.25 
6  1 ASN A 323 ? ? -103.74 79.32   
7  1 THR A 326 ? ? -86.91  49.87   
8  1 TRP A 340 ? ? -143.20 -60.46  
9  1 LEU A 351 ? ? -140.40 28.55   
10 1 PHE A 409 ? ? -121.23 -53.20  
11 1 ASN A 504 ? ? -111.11 -154.42 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 1171 ? D HOH . 
2 1 A HOH 1207 ? D HOH . 
3 1 A HOH 1252 ? D HOH . 
4 1 A HOH 1254 ? D HOH . 
5 1 A HOH 1256 ? D HOH . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1254 ? 5.85 . 
2 1 O ? A HOH 1255 ? 5.85 . 
3 1 O ? A HOH 1256 ? 6.02 . 
4 1 O ? A HOH 1257 ? 6.13 . 
# 
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 
A1EIY C01  C  Y N 1   
A1EIY C02  C  Y N 2   
A1EIY C03  C  Y N 3   
A1EIY C04  C  Y N 4   
A1EIY C05  C  Y N 5   
A1EIY C06  C  Y N 6   
A1EIY C07  C  N R 7   
A1EIY C09  C  N N 8   
A1EIY F10  F  N N 9   
A1EIY F11  F  N N 10  
A1EIY F12  F  N N 11  
A1EIY O08  O  N N 12  
A1EIY CL13 CL N N 13  
A1EIY CL14 CL N N 14  
A1EIY H1   H  N N 15  
A1EIY H2   H  N N 16  
A1EIY H3   H  N N 17  
A1EIY H4   H  N N 18  
A1EIY H5   H  N N 19  
ALA   N    N  N N 20  
ALA   CA   C  N S 21  
ALA   C    C  N N 22  
ALA   O    O  N N 23  
ALA   CB   C  N N 24  
ALA   OXT  O  N N 25  
ALA   H    H  N N 26  
ALA   H2   H  N N 27  
ALA   HA   H  N N 28  
ALA   HB1  H  N N 29  
ALA   HB2  H  N N 30  
ALA   HB3  H  N N 31  
ALA   HXT  H  N N 32  
ARG   N    N  N N 33  
ARG   CA   C  N S 34  
ARG   C    C  N N 35  
ARG   O    O  N N 36  
ARG   CB   C  N N 37  
ARG   CG   C  N N 38  
ARG   CD   C  N N 39  
ARG   NE   N  N N 40  
ARG   CZ   C  N N 41  
ARG   NH1  N  N N 42  
ARG   NH2  N  N N 43  
ARG   OXT  O  N N 44  
ARG   H    H  N N 45  
ARG   H2   H  N N 46  
ARG   HA   H  N N 47  
ARG   HB2  H  N N 48  
ARG   HB3  H  N N 49  
ARG   HG2  H  N N 50  
ARG   HG3  H  N N 51  
ARG   HD2  H  N N 52  
ARG   HD3  H  N N 53  
ARG   HE   H  N N 54  
ARG   HH11 H  N N 55  
ARG   HH12 H  N N 56  
ARG   HH21 H  N N 57  
ARG   HH22 H  N N 58  
ARG   HXT  H  N N 59  
ASN   N    N  N N 60  
ASN   CA   C  N S 61  
ASN   C    C  N N 62  
ASN   O    O  N N 63  
ASN   CB   C  N N 64  
ASN   CG   C  N N 65  
ASN   OD1  O  N N 66  
ASN   ND2  N  N N 67  
ASN   OXT  O  N N 68  
ASN   H    H  N N 69  
ASN   H2   H  N N 70  
ASN   HA   H  N N 71  
ASN   HB2  H  N N 72  
ASN   HB3  H  N N 73  
ASN   HD21 H  N N 74  
ASN   HD22 H  N N 75  
ASN   HXT  H  N N 76  
ASP   N    N  N N 77  
ASP   CA   C  N S 78  
ASP   C    C  N N 79  
ASP   O    O  N N 80  
ASP   CB   C  N N 81  
ASP   CG   C  N N 82  
ASP   OD1  O  N N 83  
ASP   OD2  O  N N 84  
ASP   OXT  O  N N 85  
ASP   H    H  N N 86  
ASP   H2   H  N N 87  
ASP   HA   H  N N 88  
ASP   HB2  H  N N 89  
ASP   HB3  H  N N 90  
ASP   HD2  H  N N 91  
ASP   HXT  H  N N 92  
CYS   N    N  N N 93  
CYS   CA   C  N R 94  
CYS   C    C  N N 95  
CYS   O    O  N N 96  
CYS   CB   C  N N 97  
CYS   SG   S  N N 98  
CYS   OXT  O  N N 99  
CYS   H    H  N N 100 
CYS   H2   H  N N 101 
CYS   HA   H  N N 102 
CYS   HB2  H  N N 103 
CYS   HB3  H  N N 104 
CYS   HG   H  N N 105 
CYS   HXT  H  N N 106 
GLN   N    N  N N 107 
GLN   CA   C  N S 108 
GLN   C    C  N N 109 
GLN   O    O  N N 110 
GLN   CB   C  N N 111 
GLN   CG   C  N N 112 
GLN   CD   C  N N 113 
GLN   OE1  O  N N 114 
GLN   NE2  N  N N 115 
GLN   OXT  O  N N 116 
GLN   H    H  N N 117 
GLN   H2   H  N N 118 
GLN   HA   H  N N 119 
GLN   HB2  H  N N 120 
GLN   HB3  H  N N 121 
GLN   HG2  H  N N 122 
GLN   HG3  H  N N 123 
GLN   HE21 H  N N 124 
GLN   HE22 H  N N 125 
GLN   HXT  H  N N 126 
GLU   N    N  N N 127 
GLU   CA   C  N S 128 
GLU   C    C  N N 129 
GLU   O    O  N N 130 
GLU   CB   C  N N 131 
GLU   CG   C  N N 132 
GLU   CD   C  N N 133 
GLU   OE1  O  N N 134 
GLU   OE2  O  N N 135 
GLU   OXT  O  N N 136 
GLU   H    H  N N 137 
GLU   H2   H  N N 138 
GLU   HA   H  N N 139 
GLU   HB2  H  N N 140 
GLU   HB3  H  N N 141 
GLU   HG2  H  N N 142 
GLU   HG3  H  N N 143 
GLU   HE2  H  N N 144 
GLU   HXT  H  N N 145 
GLY   N    N  N N 146 
GLY   CA   C  N N 147 
GLY   C    C  N N 148 
GLY   O    O  N N 149 
GLY   OXT  O  N N 150 
GLY   H    H  N N 151 
GLY   H2   H  N N 152 
GLY   HA2  H  N N 153 
GLY   HA3  H  N N 154 
GLY   HXT  H  N N 155 
HIS   N    N  N N 156 
HIS   CA   C  N S 157 
HIS   C    C  N N 158 
HIS   O    O  N N 159 
HIS   CB   C  N N 160 
HIS   CG   C  Y N 161 
HIS   ND1  N  Y N 162 
HIS   CD2  C  Y N 163 
HIS   CE1  C  Y N 164 
HIS   NE2  N  Y N 165 
HIS   OXT  O  N N 166 
HIS   H    H  N N 167 
HIS   H2   H  N N 168 
HIS   HA   H  N N 169 
HIS   HB2  H  N N 170 
HIS   HB3  H  N N 171 
HIS   HD1  H  N N 172 
HIS   HD2  H  N N 173 
HIS   HE1  H  N N 174 
HIS   HE2  H  N N 175 
HIS   HXT  H  N N 176 
HOH   O    O  N N 177 
HOH   H1   H  N N 178 
HOH   H2   H  N N 179 
ILE   N    N  N N 180 
ILE   CA   C  N S 181 
ILE   C    C  N N 182 
ILE   O    O  N N 183 
ILE   CB   C  N S 184 
ILE   CG1  C  N N 185 
ILE   CG2  C  N N 186 
ILE   CD1  C  N N 187 
ILE   OXT  O  N N 188 
ILE   H    H  N N 189 
ILE   H2   H  N N 190 
ILE   HA   H  N N 191 
ILE   HB   H  N N 192 
ILE   HG12 H  N N 193 
ILE   HG13 H  N N 194 
ILE   HG21 H  N N 195 
ILE   HG22 H  N N 196 
ILE   HG23 H  N N 197 
ILE   HD11 H  N N 198 
ILE   HD12 H  N N 199 
ILE   HD13 H  N N 200 
ILE   HXT  H  N N 201 
LEU   N    N  N N 202 
LEU   CA   C  N S 203 
LEU   C    C  N N 204 
LEU   O    O  N N 205 
LEU   CB   C  N N 206 
LEU   CG   C  N N 207 
LEU   CD1  C  N N 208 
LEU   CD2  C  N N 209 
LEU   OXT  O  N N 210 
LEU   H    H  N N 211 
LEU   H2   H  N N 212 
LEU   HA   H  N N 213 
LEU   HB2  H  N N 214 
LEU   HB3  H  N N 215 
LEU   HG   H  N N 216 
LEU   HD11 H  N N 217 
LEU   HD12 H  N N 218 
LEU   HD13 H  N N 219 
LEU   HD21 H  N N 220 
LEU   HD22 H  N N 221 
LEU   HD23 H  N N 222 
LEU   HXT  H  N N 223 
LYS   N    N  N N 224 
LYS   CA   C  N S 225 
LYS   C    C  N N 226 
LYS   O    O  N N 227 
LYS   CB   C  N N 228 
LYS   CG   C  N N 229 
LYS   CD   C  N N 230 
LYS   CE   C  N N 231 
LYS   NZ   N  N N 232 
LYS   OXT  O  N N 233 
LYS   H    H  N N 234 
LYS   H2   H  N N 235 
LYS   HA   H  N N 236 
LYS   HB2  H  N N 237 
LYS   HB3  H  N N 238 
LYS   HG2  H  N N 239 
LYS   HG3  H  N N 240 
LYS   HD2  H  N N 241 
LYS   HD3  H  N N 242 
LYS   HE2  H  N N 243 
LYS   HE3  H  N N 244 
LYS   HZ1  H  N N 245 
LYS   HZ2  H  N N 246 
LYS   HZ3  H  N N 247 
LYS   HXT  H  N N 248 
MET   N    N  N N 249 
MET   CA   C  N S 250 
MET   C    C  N N 251 
MET   O    O  N N 252 
MET   CB   C  N N 253 
MET   CG   C  N N 254 
MET   SD   S  N N 255 
MET   CE   C  N N 256 
MET   OXT  O  N N 257 
MET   H    H  N N 258 
MET   H2   H  N N 259 
MET   HA   H  N N 260 
MET   HB2  H  N N 261 
MET   HB3  H  N N 262 
MET   HG2  H  N N 263 
MET   HG3  H  N N 264 
MET   HE1  H  N N 265 
MET   HE2  H  N N 266 
MET   HE3  H  N N 267 
MET   HXT  H  N N 268 
MG    MG   MG N N 269 
PHE   N    N  N N 270 
PHE   CA   C  N S 271 
PHE   C    C  N N 272 
PHE   O    O  N N 273 
PHE   CB   C  N N 274 
PHE   CG   C  Y N 275 
PHE   CD1  C  Y N 276 
PHE   CD2  C  Y N 277 
PHE   CE1  C  Y N 278 
PHE   CE2  C  Y N 279 
PHE   CZ   C  Y N 280 
PHE   OXT  O  N N 281 
PHE   H    H  N N 282 
PHE   H2   H  N N 283 
PHE   HA   H  N N 284 
PHE   HB2  H  N N 285 
PHE   HB3  H  N N 286 
PHE   HD1  H  N N 287 
PHE   HD2  H  N N 288 
PHE   HE1  H  N N 289 
PHE   HE2  H  N N 290 
PHE   HZ   H  N N 291 
PHE   HXT  H  N N 292 
PRO   N    N  N N 293 
PRO   CA   C  N S 294 
PRO   C    C  N N 295 
PRO   O    O  N N 296 
PRO   CB   C  N N 297 
PRO   CG   C  N N 298 
PRO   CD   C  N N 299 
PRO   OXT  O  N N 300 
PRO   H    H  N N 301 
PRO   HA   H  N N 302 
PRO   HB2  H  N N 303 
PRO   HB3  H  N N 304 
PRO   HG2  H  N N 305 
PRO   HG3  H  N N 306 
PRO   HD2  H  N N 307 
PRO   HD3  H  N N 308 
PRO   HXT  H  N N 309 
SER   N    N  N N 310 
SER   CA   C  N S 311 
SER   C    C  N N 312 
SER   O    O  N N 313 
SER   CB   C  N N 314 
SER   OG   O  N N 315 
SER   OXT  O  N N 316 
SER   H    H  N N 317 
SER   H2   H  N N 318 
SER   HA   H  N N 319 
SER   HB2  H  N N 320 
SER   HB3  H  N N 321 
SER   HG   H  N N 322 
SER   HXT  H  N N 323 
THR   N    N  N N 324 
THR   CA   C  N S 325 
THR   C    C  N N 326 
THR   O    O  N N 327 
THR   CB   C  N R 328 
THR   OG1  O  N N 329 
THR   CG2  C  N N 330 
THR   OXT  O  N N 331 
THR   H    H  N N 332 
THR   H2   H  N N 333 
THR   HA   H  N N 334 
THR   HB   H  N N 335 
THR   HG1  H  N N 336 
THR   HG21 H  N N 337 
THR   HG22 H  N N 338 
THR   HG23 H  N N 339 
THR   HXT  H  N N 340 
TRP   N    N  N N 341 
TRP   CA   C  N S 342 
TRP   C    C  N N 343 
TRP   O    O  N N 344 
TRP   CB   C  N N 345 
TRP   CG   C  Y N 346 
TRP   CD1  C  Y N 347 
TRP   CD2  C  Y N 348 
TRP   NE1  N  Y N 349 
TRP   CE2  C  Y N 350 
TRP   CE3  C  Y N 351 
TRP   CZ2  C  Y N 352 
TRP   CZ3  C  Y N 353 
TRP   CH2  C  Y N 354 
TRP   OXT  O  N N 355 
TRP   H    H  N N 356 
TRP   H2   H  N N 357 
TRP   HA   H  N N 358 
TRP   HB2  H  N N 359 
TRP   HB3  H  N N 360 
TRP   HD1  H  N N 361 
TRP   HE1  H  N N 362 
TRP   HE3  H  N N 363 
TRP   HZ2  H  N N 364 
TRP   HZ3  H  N N 365 
TRP   HH2  H  N N 366 
TRP   HXT  H  N N 367 
TYR   N    N  N N 368 
TYR   CA   C  N S 369 
TYR   C    C  N N 370 
TYR   O    O  N N 371 
TYR   CB   C  N N 372 
TYR   CG   C  Y N 373 
TYR   CD1  C  Y N 374 
TYR   CD2  C  Y N 375 
TYR   CE1  C  Y N 376 
TYR   CE2  C  Y N 377 
TYR   CZ   C  Y N 378 
TYR   OH   O  N N 379 
TYR   OXT  O  N N 380 
TYR   H    H  N N 381 
TYR   H2   H  N N 382 
TYR   HA   H  N N 383 
TYR   HB2  H  N N 384 
TYR   HB3  H  N N 385 
TYR   HD1  H  N N 386 
TYR   HD2  H  N N 387 
TYR   HE1  H  N N 388 
TYR   HE2  H  N N 389 
TYR   HH   H  N N 390 
TYR   HXT  H  N N 391 
VAL   N    N  N N 392 
VAL   CA   C  N S 393 
VAL   C    C  N N 394 
VAL   O    O  N N 395 
VAL   CB   C  N N 396 
VAL   CG1  C  N N 397 
VAL   CG2  C  N N 398 
VAL   OXT  O  N N 399 
VAL   H    H  N N 400 
VAL   H2   H  N N 401 
VAL   HA   H  N N 402 
VAL   HB   H  N N 403 
VAL   HG11 H  N N 404 
VAL   HG12 H  N N 405 
VAL   HG13 H  N N 406 
VAL   HG21 H  N N 407 
VAL   HG22 H  N N 408 
VAL   HG23 H  N N 409 
VAL   HXT  H  N N 410 
# 
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 
A1EIY CL14 C03  sing N N 1   
A1EIY C04  C05  doub Y N 2   
A1EIY C04  C03  sing Y N 3   
A1EIY C05  C06  sing Y N 4   
A1EIY F10  C09  sing N N 5   
A1EIY C03  C02  doub Y N 6   
A1EIY F11  C09  sing N N 7   
A1EIY C09  F12  sing N N 8   
A1EIY C09  C07  sing N N 9   
A1EIY C06  C07  sing N N 10  
A1EIY C06  C01  doub Y N 11  
A1EIY C02  C01  sing Y N 12  
A1EIY C02  CL13 sing N N 13  
A1EIY C07  O08  sing N N 14  
A1EIY C01  H1   sing N N 15  
A1EIY C04  H2   sing N N 16  
A1EIY C05  H3   sing N N 17  
A1EIY C07  H4   sing N N 18  
A1EIY O08  H5   sing N N 19  
ALA   N    CA   sing N N 20  
ALA   N    H    sing N N 21  
ALA   N    H2   sing N N 22  
ALA   CA   C    sing N N 23  
ALA   CA   CB   sing N N 24  
ALA   CA   HA   sing N N 25  
ALA   C    O    doub N N 26  
ALA   C    OXT  sing N N 27  
ALA   CB   HB1  sing N N 28  
ALA   CB   HB2  sing N N 29  
ALA   CB   HB3  sing N N 30  
ALA   OXT  HXT  sing N N 31  
ARG   N    CA   sing N N 32  
ARG   N    H    sing N N 33  
ARG   N    H2   sing N N 34  
ARG   CA   C    sing N N 35  
ARG   CA   CB   sing N N 36  
ARG   CA   HA   sing N N 37  
ARG   C    O    doub N N 38  
ARG   C    OXT  sing N N 39  
ARG   CB   CG   sing N N 40  
ARG   CB   HB2  sing N N 41  
ARG   CB   HB3  sing N N 42  
ARG   CG   CD   sing N N 43  
ARG   CG   HG2  sing N N 44  
ARG   CG   HG3  sing N N 45  
ARG   CD   NE   sing N N 46  
ARG   CD   HD2  sing N N 47  
ARG   CD   HD3  sing N N 48  
ARG   NE   CZ   sing N N 49  
ARG   NE   HE   sing N N 50  
ARG   CZ   NH1  sing N N 51  
ARG   CZ   NH2  doub N N 52  
ARG   NH1  HH11 sing N N 53  
ARG   NH1  HH12 sing N N 54  
ARG   NH2  HH21 sing N N 55  
ARG   NH2  HH22 sing N N 56  
ARG   OXT  HXT  sing N N 57  
ASN   N    CA   sing N N 58  
ASN   N    H    sing N N 59  
ASN   N    H2   sing N N 60  
ASN   CA   C    sing N N 61  
ASN   CA   CB   sing N N 62  
ASN   CA   HA   sing N N 63  
ASN   C    O    doub N N 64  
ASN   C    OXT  sing N N 65  
ASN   CB   CG   sing N N 66  
ASN   CB   HB2  sing N N 67  
ASN   CB   HB3  sing N N 68  
ASN   CG   OD1  doub N N 69  
ASN   CG   ND2  sing N N 70  
ASN   ND2  HD21 sing N N 71  
ASN   ND2  HD22 sing N N 72  
ASN   OXT  HXT  sing N N 73  
ASP   N    CA   sing N N 74  
ASP   N    H    sing N N 75  
ASP   N    H2   sing N N 76  
ASP   CA   C    sing N N 77  
ASP   CA   CB   sing N N 78  
ASP   CA   HA   sing N N 79  
ASP   C    O    doub N N 80  
ASP   C    OXT  sing N N 81  
ASP   CB   CG   sing N N 82  
ASP   CB   HB2  sing N N 83  
ASP   CB   HB3  sing N N 84  
ASP   CG   OD1  doub N N 85  
ASP   CG   OD2  sing N N 86  
ASP   OD2  HD2  sing N N 87  
ASP   OXT  HXT  sing N N 88  
CYS   N    CA   sing N N 89  
CYS   N    H    sing N N 90  
CYS   N    H2   sing N N 91  
CYS   CA   C    sing N N 92  
CYS   CA   CB   sing N N 93  
CYS   CA   HA   sing N N 94  
CYS   C    O    doub N N 95  
CYS   C    OXT  sing N N 96  
CYS   CB   SG   sing N N 97  
CYS   CB   HB2  sing N N 98  
CYS   CB   HB3  sing N N 99  
CYS   SG   HG   sing N N 100 
CYS   OXT  HXT  sing N N 101 
GLN   N    CA   sing N N 102 
GLN   N    H    sing N N 103 
GLN   N    H2   sing N N 104 
GLN   CA   C    sing N N 105 
GLN   CA   CB   sing N N 106 
GLN   CA   HA   sing N N 107 
GLN   C    O    doub N N 108 
GLN   C    OXT  sing N N 109 
GLN   CB   CG   sing N N 110 
GLN   CB   HB2  sing N N 111 
GLN   CB   HB3  sing N N 112 
GLN   CG   CD   sing N N 113 
GLN   CG   HG2  sing N N 114 
GLN   CG   HG3  sing N N 115 
GLN   CD   OE1  doub N N 116 
GLN   CD   NE2  sing N N 117 
GLN   NE2  HE21 sing N N 118 
GLN   NE2  HE22 sing N N 119 
GLN   OXT  HXT  sing N N 120 
GLU   N    CA   sing N N 121 
GLU   N    H    sing N N 122 
GLU   N    H2   sing N N 123 
GLU   CA   C    sing N N 124 
GLU   CA   CB   sing N N 125 
GLU   CA   HA   sing N N 126 
GLU   C    O    doub N N 127 
GLU   C    OXT  sing N N 128 
GLU   CB   CG   sing N N 129 
GLU   CB   HB2  sing N N 130 
GLU   CB   HB3  sing N N 131 
GLU   CG   CD   sing N N 132 
GLU   CG   HG2  sing N N 133 
GLU   CG   HG3  sing N N 134 
GLU   CD   OE1  doub N N 135 
GLU   CD   OE2  sing N N 136 
GLU   OE2  HE2  sing N N 137 
GLU   OXT  HXT  sing N N 138 
GLY   N    CA   sing N N 139 
GLY   N    H    sing N N 140 
GLY   N    H2   sing N N 141 
GLY   CA   C    sing N N 142 
GLY   CA   HA2  sing N N 143 
GLY   CA   HA3  sing N N 144 
GLY   C    O    doub N N 145 
GLY   C    OXT  sing N N 146 
GLY   OXT  HXT  sing N N 147 
HIS   N    CA   sing N N 148 
HIS   N    H    sing N N 149 
HIS   N    H2   sing N N 150 
HIS   CA   C    sing N N 151 
HIS   CA   CB   sing N N 152 
HIS   CA   HA   sing N N 153 
HIS   C    O    doub N N 154 
HIS   C    OXT  sing N N 155 
HIS   CB   CG   sing N N 156 
HIS   CB   HB2  sing N N 157 
HIS   CB   HB3  sing N N 158 
HIS   CG   ND1  sing Y N 159 
HIS   CG   CD2  doub Y N 160 
HIS   ND1  CE1  doub Y N 161 
HIS   ND1  HD1  sing N N 162 
HIS   CD2  NE2  sing Y N 163 
HIS   CD2  HD2  sing N N 164 
HIS   CE1  NE2  sing Y N 165 
HIS   CE1  HE1  sing N N 166 
HIS   NE2  HE2  sing N N 167 
HIS   OXT  HXT  sing N N 168 
HOH   O    H1   sing N N 169 
HOH   O    H2   sing N N 170 
ILE   N    CA   sing N N 171 
ILE   N    H    sing N N 172 
ILE   N    H2   sing N N 173 
ILE   CA   C    sing N N 174 
ILE   CA   CB   sing N N 175 
ILE   CA   HA   sing N N 176 
ILE   C    O    doub N N 177 
ILE   C    OXT  sing N N 178 
ILE   CB   CG1  sing N N 179 
ILE   CB   CG2  sing N N 180 
ILE   CB   HB   sing N N 181 
ILE   CG1  CD1  sing N N 182 
ILE   CG1  HG12 sing N N 183 
ILE   CG1  HG13 sing N N 184 
ILE   CG2  HG21 sing N N 185 
ILE   CG2  HG22 sing N N 186 
ILE   CG2  HG23 sing N N 187 
ILE   CD1  HD11 sing N N 188 
ILE   CD1  HD12 sing N N 189 
ILE   CD1  HD13 sing N N 190 
ILE   OXT  HXT  sing N N 191 
LEU   N    CA   sing N N 192 
LEU   N    H    sing N N 193 
LEU   N    H2   sing N N 194 
LEU   CA   C    sing N N 195 
LEU   CA   CB   sing N N 196 
LEU   CA   HA   sing N N 197 
LEU   C    O    doub N N 198 
LEU   C    OXT  sing N N 199 
LEU   CB   CG   sing N N 200 
LEU   CB   HB2  sing N N 201 
LEU   CB   HB3  sing N N 202 
LEU   CG   CD1  sing N N 203 
LEU   CG   CD2  sing N N 204 
LEU   CG   HG   sing N N 205 
LEU   CD1  HD11 sing N N 206 
LEU   CD1  HD12 sing N N 207 
LEU   CD1  HD13 sing N N 208 
LEU   CD2  HD21 sing N N 209 
LEU   CD2  HD22 sing N N 210 
LEU   CD2  HD23 sing N N 211 
LEU   OXT  HXT  sing N N 212 
LYS   N    CA   sing N N 213 
LYS   N    H    sing N N 214 
LYS   N    H2   sing N N 215 
LYS   CA   C    sing N N 216 
LYS   CA   CB   sing N N 217 
LYS   CA   HA   sing N N 218 
LYS   C    O    doub N N 219 
LYS   C    OXT  sing N N 220 
LYS   CB   CG   sing N N 221 
LYS   CB   HB2  sing N N 222 
LYS   CB   HB3  sing N N 223 
LYS   CG   CD   sing N N 224 
LYS   CG   HG2  sing N N 225 
LYS   CG   HG3  sing N N 226 
LYS   CD   CE   sing N N 227 
LYS   CD   HD2  sing N N 228 
LYS   CD   HD3  sing N N 229 
LYS   CE   NZ   sing N N 230 
LYS   CE   HE2  sing N N 231 
LYS   CE   HE3  sing N N 232 
LYS   NZ   HZ1  sing N N 233 
LYS   NZ   HZ2  sing N N 234 
LYS   NZ   HZ3  sing N N 235 
LYS   OXT  HXT  sing N N 236 
MET   N    CA   sing N N 237 
MET   N    H    sing N N 238 
MET   N    H2   sing N N 239 
MET   CA   C    sing N N 240 
MET   CA   CB   sing N N 241 
MET   CA   HA   sing N N 242 
MET   C    O    doub N N 243 
MET   C    OXT  sing N N 244 
MET   CB   CG   sing N N 245 
MET   CB   HB2  sing N N 246 
MET   CB   HB3  sing N N 247 
MET   CG   SD   sing N N 248 
MET   CG   HG2  sing N N 249 
MET   CG   HG3  sing N N 250 
MET   SD   CE   sing N N 251 
MET   CE   HE1  sing N N 252 
MET   CE   HE2  sing N N 253 
MET   CE   HE3  sing N N 254 
MET   OXT  HXT  sing N N 255 
PHE   N    CA   sing N N 256 
PHE   N    H    sing N N 257 
PHE   N    H2   sing N N 258 
PHE   CA   C    sing N N 259 
PHE   CA   CB   sing N N 260 
PHE   CA   HA   sing N N 261 
PHE   C    O    doub N N 262 
PHE   C    OXT  sing N N 263 
PHE   CB   CG   sing N N 264 
PHE   CB   HB2  sing N N 265 
PHE   CB   HB3  sing N N 266 
PHE   CG   CD1  doub Y N 267 
PHE   CG   CD2  sing Y N 268 
PHE   CD1  CE1  sing Y N 269 
PHE   CD1  HD1  sing N N 270 
PHE   CD2  CE2  doub Y N 271 
PHE   CD2  HD2  sing N N 272 
PHE   CE1  CZ   doub Y N 273 
PHE   CE1  HE1  sing N N 274 
PHE   CE2  CZ   sing Y N 275 
PHE   CE2  HE2  sing N N 276 
PHE   CZ   HZ   sing N N 277 
PHE   OXT  HXT  sing N N 278 
PRO   N    CA   sing N N 279 
PRO   N    CD   sing N N 280 
PRO   N    H    sing N N 281 
PRO   CA   C    sing N N 282 
PRO   CA   CB   sing N N 283 
PRO   CA   HA   sing N N 284 
PRO   C    O    doub N N 285 
PRO   C    OXT  sing N N 286 
PRO   CB   CG   sing N N 287 
PRO   CB   HB2  sing N N 288 
PRO   CB   HB3  sing N N 289 
PRO   CG   CD   sing N N 290 
PRO   CG   HG2  sing N N 291 
PRO   CG   HG3  sing N N 292 
PRO   CD   HD2  sing N N 293 
PRO   CD   HD3  sing N N 294 
PRO   OXT  HXT  sing N N 295 
SER   N    CA   sing N N 296 
SER   N    H    sing N N 297 
SER   N    H2   sing N N 298 
SER   CA   C    sing N N 299 
SER   CA   CB   sing N N 300 
SER   CA   HA   sing N N 301 
SER   C    O    doub N N 302 
SER   C    OXT  sing N N 303 
SER   CB   OG   sing N N 304 
SER   CB   HB2  sing N N 305 
SER   CB   HB3  sing N N 306 
SER   OG   HG   sing N N 307 
SER   OXT  HXT  sing N N 308 
THR   N    CA   sing N N 309 
THR   N    H    sing N N 310 
THR   N    H2   sing N N 311 
THR   CA   C    sing N N 312 
THR   CA   CB   sing N N 313 
THR   CA   HA   sing N N 314 
THR   C    O    doub N N 315 
THR   C    OXT  sing N N 316 
THR   CB   OG1  sing N N 317 
THR   CB   CG2  sing N N 318 
THR   CB   HB   sing N N 319 
THR   OG1  HG1  sing N N 320 
THR   CG2  HG21 sing N N 321 
THR   CG2  HG22 sing N N 322 
THR   CG2  HG23 sing N N 323 
THR   OXT  HXT  sing N N 324 
TRP   N    CA   sing N N 325 
TRP   N    H    sing N N 326 
TRP   N    H2   sing N N 327 
TRP   CA   C    sing N N 328 
TRP   CA   CB   sing N N 329 
TRP   CA   HA   sing N N 330 
TRP   C    O    doub N N 331 
TRP   C    OXT  sing N N 332 
TRP   CB   CG   sing N N 333 
TRP   CB   HB2  sing N N 334 
TRP   CB   HB3  sing N N 335 
TRP   CG   CD1  doub Y N 336 
TRP   CG   CD2  sing Y N 337 
TRP   CD1  NE1  sing Y N 338 
TRP   CD1  HD1  sing N N 339 
TRP   CD2  CE2  doub Y N 340 
TRP   CD2  CE3  sing Y N 341 
TRP   NE1  CE2  sing Y N 342 
TRP   NE1  HE1  sing N N 343 
TRP   CE2  CZ2  sing Y N 344 
TRP   CE3  CZ3  doub Y N 345 
TRP   CE3  HE3  sing N N 346 
TRP   CZ2  CH2  doub Y N 347 
TRP   CZ2  HZ2  sing N N 348 
TRP   CZ3  CH2  sing Y N 349 
TRP   CZ3  HZ3  sing N N 350 
TRP   CH2  HH2  sing N N 351 
TRP   OXT  HXT  sing N N 352 
TYR   N    CA   sing N N 353 
TYR   N    H    sing N N 354 
TYR   N    H2   sing N N 355 
TYR   CA   C    sing N N 356 
TYR   CA   CB   sing N N 357 
TYR   CA   HA   sing N N 358 
TYR   C    O    doub N N 359 
TYR   C    OXT  sing N N 360 
TYR   CB   CG   sing N N 361 
TYR   CB   HB2  sing N N 362 
TYR   CB   HB3  sing N N 363 
TYR   CG   CD1  doub Y N 364 
TYR   CG   CD2  sing Y N 365 
TYR   CD1  CE1  sing Y N 366 
TYR   CD1  HD1  sing N N 367 
TYR   CD2  CE2  doub Y N 368 
TYR   CD2  HD2  sing N N 369 
TYR   CE1  CZ   doub Y N 370 
TYR   CE1  HE1  sing N N 371 
TYR   CE2  CZ   sing Y N 372 
TYR   CE2  HE2  sing N N 373 
TYR   CZ   OH   sing N N 374 
TYR   OH   HH   sing N N 375 
TYR   OXT  HXT  sing N N 376 
VAL   N    CA   sing N N 377 
VAL   N    H    sing N N 378 
VAL   N    H2   sing N N 379 
VAL   CA   C    sing N N 380 
VAL   CA   CB   sing N N 381 
VAL   CA   HA   sing N N 382 
VAL   C    O    doub N N 383 
VAL   C    OXT  sing N N 384 
VAL   CB   CG1  sing N N 385 
VAL   CB   CG2  sing N N 386 
VAL   CB   HB   sing N N 387 
VAL   CG1  HG11 sing N N 388 
VAL   CG1  HG12 sing N N 389 
VAL   CG1  HG13 sing N N 390 
VAL   CG2  HG21 sing N N 391 
VAL   CG2  HG22 sing N N 392 
VAL   CG2  HG23 sing N N 393 
VAL   OXT  HXT  sing N N 394 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           82204347 
_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   1MX1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9KWL 
_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]   0.009052 
_atom_sites.fract_transf_matrix[1][2]   0.005226 
_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]   0.010453 
_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]   0.003594 
_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  
CL 
F  
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . SER   A 1 1   ? -38.173 -74.316 29.530 1.00 73.88 ? 4    SER   A N    1 
ATOM   2    C  CA   . SER   A 1 1   ? -38.791 -74.074 30.832 1.00 69.55 ? 4    SER   A CA   1 
ATOM   3    C  C    . SER   A 1 1   ? -39.613 -72.773 30.816 1.00 64.05 ? 4    SER   A C    1 
ATOM   4    O  O    . SER   A 1 1   ? -39.599 -72.034 29.832 1.00 61.93 ? 4    SER   A O    1 
ATOM   5    C  CB   . SER   A 1 1   ? -37.724 -74.038 31.927 1.00 71.71 ? 4    SER   A CB   1 
ATOM   6    O  OG   . SER   A 1 1   ? -36.948 -72.855 31.846 1.00 70.99 ? 4    SER   A OG   1 
ATOM   7    N  N    . SER   A 1 2   ? -40.318 -72.500 31.908 1.00 59.43 ? 5    SER   A N    1 
ATOM   8    C  CA   . SER   A 1 2   ? -41.360 -71.465 31.919 1.00 55.61 ? 5    SER   A CA   1 
ATOM   9    C  C    . SER   A 1 2   ? -40.782 -70.057 31.766 1.00 49.08 ? 5    SER   A C    1 
ATOM   10   O  O    . SER   A 1 2   ? -39.906 -69.669 32.552 1.00 46.75 ? 5    SER   A O    1 
ATOM   11   C  CB   . SER   A 1 2   ? -42.167 -71.571 33.211 1.00 56.58 ? 5    SER   A CB   1 
ATOM   12   O  OG   . SER   A 1 2   ? -43.329 -70.765 33.149 1.00 56.34 ? 5    SER   A OG   1 
ATOM   13   N  N    . PRO   A 1 3   ? -41.253 -69.259 30.807 1.00 46.95 ? 6    PRO   A N    1 
ATOM   14   C  CA   . PRO   A 1 3   ? -40.649 -67.944 30.586 1.00 40.94 ? 6    PRO   A CA   1 
ATOM   15   C  C    . PRO   A 1 3   ? -40.813 -67.058 31.796 1.00 36.41 ? 6    PRO   A C    1 
ATOM   16   O  O    . PRO   A 1 3   ? -41.815 -67.151 32.533 1.00 38.09 ? 6    PRO   A O    1 
ATOM   17   C  CB   . PRO   A 1 3   ? -41.429 -67.402 29.380 1.00 35.00 ? 6    PRO   A CB   1 
ATOM   18   C  CG   . PRO   A 1 3   ? -41.862 -68.610 28.644 1.00 42.01 ? 6    PRO   A CG   1 
ATOM   19   C  CD   . PRO   A 1 3   ? -42.172 -69.630 29.717 1.00 44.67 ? 6    PRO   A CD   1 
ATOM   20   N  N    . PRO   A 1 4   ? -39.854 -66.164 32.054 1.00 29.76 ? 7    PRO   A N    1 
ATOM   21   C  CA   . PRO   A 1 4   ? -39.912 -65.351 33.277 1.00 30.91 ? 7    PRO   A CA   1 
ATOM   22   C  C    . PRO   A 1 4   ? -40.985 -64.260 33.200 1.00 28.00 ? 7    PRO   A C    1 
ATOM   23   O  O    . PRO   A 1 4   ? -41.149 -63.589 32.176 1.00 22.51 ? 7    PRO   A O    1 
ATOM   24   C  CB   . PRO   A 1 4   ? -38.502 -64.745 33.370 1.00 23.85 ? 7    PRO   A CB   1 
ATOM   25   C  CG   . PRO   A 1 4   ? -38.015 -64.691 31.939 1.00 21.95 ? 7    PRO   A CG   1 
ATOM   26   C  CD   . PRO   A 1 4   ? -38.658 -65.884 31.234 1.00 26.89 ? 7    PRO   A CD   1 
ATOM   27   N  N    . VAL   A 1 5   ? -41.708 -64.084 34.311 1.00 27.29 ? 8    VAL   A N    1 
ATOM   28   C  CA   . VAL   A 1 5   ? -42.741 -63.056 34.454 1.00 25.98 ? 8    VAL   A CA   1 
ATOM   29   C  C    . VAL   A 1 5   ? -42.427 -62.236 35.696 1.00 27.13 ? 8    VAL   A C    1 
ATOM   30   O  O    . VAL   A 1 5   ? -42.281 -62.793 36.790 1.00 28.15 ? 8    VAL   A O    1 
ATOM   31   C  CB   . VAL   A 1 5   ? -44.156 -63.657 34.557 1.00 29.93 ? 8    VAL   A CB   1 
ATOM   32   C  CG1  . VAL   A 1 5   ? -45.172 -62.561 34.857 1.00 27.03 ? 8    VAL   A CG1  1 
ATOM   33   C  CG2  . VAL   A 1 5   ? -44.522 -64.356 33.266 1.00 30.47 ? 8    VAL   A CG2  1 
ATOM   34   N  N    . VAL   A 1 6   ? -42.332 -60.918 35.528 1.00 21.92 ? 9    VAL   A N    1 
ATOM   35   C  CA   . VAL   A 1 6   ? -41.892 -60.014 36.580 1.00 21.34 ? 9    VAL   A CA   1 
ATOM   36   C  C    . VAL   A 1 6   ? -42.981 -58.977 36.833 1.00 24.17 ? 9    VAL   A C    1 
ATOM   37   O  O    . VAL   A 1 6   ? -43.585 -58.457 35.889 1.00 21.14 ? 9    VAL   A O    1 
ATOM   38   C  CB   . VAL   A 1 6   ? -40.564 -59.335 36.181 1.00 20.14 ? 9    VAL   A CB   1 
ATOM   39   C  CG1  . VAL   A 1 6   ? -40.221 -58.193 37.110 1.00 20.49 ? 9    VAL   A CG1  1 
ATOM   40   C  CG2  . VAL   A 1 6   ? -39.431 -60.384 36.119 1.00 21.61 ? 9    VAL   A CG2  1 
ATOM   41   N  N    . ASP   A 1 7   ? -43.219 -58.669 38.103 1.00 23.50 ? 10   ASP   A N    1 
ATOM   42   C  CA   . ASP   A 1 7   ? -44.149 -57.615 38.490 1.00 28.68 ? 10   ASP   A CA   1 
ATOM   43   C  C    . ASP   A 1 7   ? -43.417 -56.283 38.561 1.00 30.63 ? 10   ASP   A C    1 
ATOM   44   O  O    . ASP   A 1 7   ? -42.419 -56.158 39.277 1.00 30.85 ? 10   ASP   A O    1 
ATOM   45   C  CB   . ASP   A 1 7   ? -44.801 -57.931 39.835 1.00 32.71 ? 10   ASP   A CB   1 
ATOM   46   C  CG   . ASP   A 1 7   ? -45.707 -59.147 39.767 1.00 42.05 ? 10   ASP   A CG   1 
ATOM   47   O  OD1  . ASP   A 1 7   ? -46.903 -58.972 39.440 1.00 45.42 ? 10   ASP   A OD1  1 
ATOM   48   O  OD2  . ASP   A 1 7   ? -45.228 -60.273 40.033 1.00 48.64 ? 10   ASP   A OD2  1 
ATOM   49   N  N    . THR   A 1 8   ? -43.903 -55.292 37.822 1.00 24.61 ? 11   THR   A N    1 
ATOM   50   C  CA   . THR   A 1 8   ? -43.413 -53.935 37.911 1.00 22.09 ? 11   THR   A CA   1 
ATOM   51   C  C    . THR   A 1 8   ? -44.535 -53.055 38.448 1.00 26.12 ? 11   THR   A C    1 
ATOM   52   O  O    . THR   A 1 8   ? -45.704 -53.462 38.504 1.00 22.64 ? 11   THR   A O    1 
ATOM   53   C  CB   . THR   A 1 8   ? -42.924 -53.426 36.543 1.00 24.26 ? 11   THR   A CB   1 
ATOM   54   O  OG1  . THR   A 1 8   ? -44.038 -52.966 35.767 1.00 23.11 ? 11   THR   A OG1  1 
ATOM   55   C  CG2  . THR   A 1 8   ? -42.189 -54.515 35.775 1.00 22.21 ? 11   THR   A CG2  1 
ATOM   56   N  N    . VAL   A 1 9   ? -44.155 -51.837 38.837 1.00 22.18 ? 12   VAL   A N    1 
ATOM   57   C  CA   . VAL   A 1 9   ? -45.105 -50.879 39.404 1.00 24.65 ? 12   VAL   A CA   1 
ATOM   58   C  C    . VAL   A 1 9   ? -46.345 -50.759 38.522 1.00 24.95 ? 12   VAL   A C    1 
ATOM   59   O  O    . VAL   A 1 9   ? -47.477 -50.711 39.018 1.00 24.14 ? 12   VAL   A O    1 
ATOM   60   C  CB   . VAL   A 1 9   ? -44.421 -49.511 39.599 1.00 25.94 ? 12   VAL   A CB   1 
ATOM   61   C  CG1  . VAL   A 1 9   ? -45.443 -48.445 39.968 1.00 27.85 ? 12   VAL   A CG1  1 
ATOM   62   C  CG2  . VAL   A 1 9   ? -43.294 -49.585 40.648 1.00 24.95 ? 12   VAL   A CG2  1 
ATOM   63   N  N    . HIS   A 1 10  ? -46.154 -50.722 37.203 1.00 21.17 ? 13   HIS   A N    1 
ATOM   64   C  CA   . HIS   A 1 10  ? -47.253 -50.517 36.270 1.00 22.93 ? 13   HIS   A CA   1 
ATOM   65   C  C    . HIS   A 1 10  ? -47.881 -51.796 35.736 1.00 22.55 ? 13   HIS   A C    1 
ATOM   66   O  O    . HIS   A 1 10  ? -48.893 -51.705 35.023 1.00 21.23 ? 13   HIS   A O    1 
ATOM   67   C  CB   . HIS   A 1 10  ? -46.809 -49.646 35.089 1.00 22.10 ? 13   HIS   A CB   1 
ATOM   68   C  CG   . HIS   A 1 10  ? -46.363 -48.280 35.493 1.00 25.83 ? 13   HIS   A CG   1 
ATOM   69   N  ND1  . HIS   A 1 10  ? -45.212 -47.693 35.011 1.00 26.52 ? 13   HIS   A ND1  1 
ATOM   70   C  CD2  . HIS   A 1 10  ? -46.897 -47.399 36.371 1.00 27.67 ? 13   HIS   A CD2  1 
ATOM   71   C  CE1  . HIS   A 1 10  ? -45.072 -46.497 35.557 1.00 24.43 ? 13   HIS   A CE1  1 
ATOM   72   N  NE2  . HIS   A 1 10  ? -46.079 -46.295 36.386 1.00 29.57 ? 13   HIS   A NE2  1 
ATOM   73   N  N    . GLY   A 1 11  ? -47.349 -52.964 36.060 1.00 18.13 ? 14   GLY   A N    1 
ATOM   74   C  CA   . GLY   A 1 11  ? -47.961 -54.203 35.617 1.00 18.15 ? 14   GLY   A CA   1 
ATOM   75   C  C    . GLY   A 1 11  ? -46.934 -55.300 35.402 1.00 21.36 ? 14   GLY   A C    1 
ATOM   76   O  O    . GLY   A 1 11  ? -45.733 -55.113 35.568 1.00 19.25 ? 14   GLY   A O    1 
ATOM   77   N  N    . LYS   A 1 12  ? -47.444 -56.470 35.037 1.00 18.33 ? 15   LYS   A N    1 
ATOM   78   C  CA   . LYS   A 1 12  ? -46.590 -57.633 34.844 1.00 17.53 ? 15   LYS   A CA   1 
ATOM   79   C  C    . LYS   A 1 12  ? -46.002 -57.660 33.442 1.00 20.09 ? 15   LYS   A C    1 
ATOM   80   O  O    . LYS   A 1 12  ? -46.674 -57.314 32.471 1.00 19.61 ? 15   LYS   A O    1 
ATOM   81   C  CB   . LYS   A 1 12  ? -47.383 -58.921 35.066 1.00 23.42 ? 15   LYS   A CB   1 
ATOM   82   C  CG   . LYS   A 1 12  ? -47.981 -59.064 36.448 1.00 27.21 ? 15   LYS   A CG   1 
ATOM   83   C  CD   . LYS   A 1 12  ? -48.943 -60.252 36.468 1.00 31.54 ? 15   LYS   A CD   1 
ATOM   84   C  CE   . LYS   A 1 12  ? -49.634 -60.357 37.807 1.00 43.36 ? 15   LYS   A CE   1 
ATOM   85   N  NZ   . LYS   A 1 12  ? -48.778 -61.114 38.759 1.00 46.77 ? 15   LYS   A NZ   1 
ATOM   86   N  N    . VAL   A 1 13  ? -44.754 -58.125 33.325 1.00 16.99 ? 16   VAL   A N    1 
ATOM   87   C  CA   . VAL   A 1 13  ? -44.105 -58.238 32.026 1.00 16.18 ? 16   VAL   A CA   1 
ATOM   88   C  C    . VAL   A 1 13  ? -43.567 -59.648 31.863 1.00 19.25 ? 16   VAL   A C    1 
ATOM   89   O  O    . VAL   A 1 13  ? -43.104 -60.268 32.823 1.00 19.64 ? 16   VAL   A O    1 
ATOM   90   C  CB   . VAL   A 1 13  ? -42.979 -57.190 31.833 1.00 19.95 ? 16   VAL   A CB   1 
ATOM   91   C  CG1  . VAL   A 1 13  ? -43.569 -55.790 31.932 1.00 18.10 ? 16   VAL   A CG1  1 
ATOM   92   C  CG2  . VAL   A 1 13  ? -41.857 -57.360 32.857 1.00 19.36 ? 16   VAL   A CG2  1 
ATOM   93   N  N    . LEU   A 1 14  ? -43.616 -60.137 30.638 1.00 18.32 ? 17   LEU   A N    1 
ATOM   94   C  CA   . LEU   A 1 14  ? -43.152 -61.464 30.270 1.00 22.38 ? 17   LEU   A CA   1 
ATOM   95   C  C    . LEU   A 1 14  ? -41.914 -61.310 29.394 1.00 21.57 ? 17   LEU   A C    1 
ATOM   96   O  O    . LEU   A 1 14  ? -41.936 -60.578 28.398 1.00 17.70 ? 17   LEU   A O    1 
ATOM   97   C  CB   . LEU   A 1 14  ? -44.274 -62.221 29.546 1.00 22.60 ? 17   LEU   A CB   1 
ATOM   98   C  CG   . LEU   A 1 14  ? -44.135 -63.599 28.886 1.00 28.00 ? 17   LEU   A CG   1 
ATOM   99   C  CD1  . LEU   A 1 14  ? -43.549 -63.513 27.498 1.00 27.94 ? 17   LEU   A CD1  1 
ATOM   100  C  CD2  . LEU   A 1 14  ? -43.290 -64.473 29.756 1.00 27.24 ? 17   LEU   A CD2  1 
ATOM   101  N  N    . GLY   A 1 15  ? -40.831 -61.973 29.781 1.00 18.49 ? 18   GLY   A N    1 
ATOM   102  C  CA   . GLY   A 1 15  ? -39.623 -61.908 28.987 1.00 16.88 ? 18   GLY   A CA   1 
ATOM   103  C  C    . GLY   A 1 15  ? -39.278 -63.245 28.373 1.00 21.38 ? 18   GLY   A C    1 
ATOM   104  O  O    . GLY   A 1 15  ? -40.167 -64.071 28.128 1.00 19.37 ? 18   GLY   A O    1 
ATOM   105  N  N    . LYS   A 1 16  ? -37.992 -63.486 28.119 1.00 15.14 ? 19   LYS   A N    1 
ATOM   106  C  CA   . LYS   A 1 16  ? -37.585 -64.765 27.552 1.00 17.78 ? 19   LYS   A CA   1 
ATOM   107  C  C    . LYS   A 1 16  ? -36.211 -65.143 28.087 1.00 20.65 ? 19   LYS   A C    1 
ATOM   108  O  O    . LYS   A 1 16  ? -35.431 -64.278 28.485 1.00 18.65 ? 19   LYS   A O    1 
ATOM   109  C  CB   . LYS   A 1 16  ? -37.597 -64.702 26.018 1.00 19.78 ? 19   LYS   A CB   1 
ATOM   110  C  CG   . LYS   A 1 16  ? -36.503 -63.837 25.421 1.00 28.86 ? 19   LYS   A CG   1 
ATOM   111  C  CD   . LYS   A 1 16  ? -36.602 -63.797 23.896 1.00 37.95 ? 19   LYS   A CD   1 
ATOM   112  C  CE   . LYS   A 1 16  ? -35.679 -62.729 23.300 1.00 38.93 ? 19   LYS   A CE   1 
ATOM   113  N  NZ   . LYS   A 1 16  ? -35.922 -62.520 21.835 1.00 47.49 ? 19   LYS   A NZ   1 
ATOM   114  N  N    . PHE   A 1 17  ? -35.927 -66.447 28.117 1.00 17.01 ? 20   PHE   A N    1 
ATOM   115  C  CA   . PHE   A 1 17  ? -34.610 -66.935 28.536 1.00 19.92 ? 20   PHE   A CA   1 
ATOM   116  C  C    . PHE   A 1 17  ? -33.697 -67.093 27.336 1.00 22.57 ? 20   PHE   A C    1 
ATOM   117  O  O    . PHE   A 1 17  ? -34.119 -67.584 26.285 1.00 22.74 ? 20   PHE   A O    1 
ATOM   118  C  CB   . PHE   A 1 17  ? -34.713 -68.281 29.247 1.00 21.15 ? 20   PHE   A CB   1 
ATOM   119  C  CG   . PHE   A 1 17  ? -35.249 -68.191 30.634 1.00 23.07 ? 20   PHE   A CG   1 
ATOM   120  C  CD1  . PHE   A 1 17  ? -34.663 -67.357 31.561 1.00 22.38 ? 20   PHE   A CD1  1 
ATOM   121  C  CD2  . PHE   A 1 17  ? -36.334 -68.961 31.016 1.00 29.56 ? 20   PHE   A CD2  1 
ATOM   122  C  CE1  . PHE   A 1 17  ? -35.158 -67.276 32.851 1.00 25.45 ? 20   PHE   A CE1  1 
ATOM   123  C  CE2  . PHE   A 1 17  ? -36.836 -68.889 32.301 1.00 31.33 ? 20   PHE   A CE2  1 
ATOM   124  C  CZ   . PHE   A 1 17  ? -36.254 -68.048 33.219 1.00 32.60 ? 20   PHE   A CZ   1 
ATOM   125  N  N    . VAL   A 1 18  ? -32.436 -66.687 27.495 1.00 18.28 ? 21   VAL   A N    1 
ATOM   126  C  CA   . VAL   A 1 18  ? -31.425 -66.906 26.473 1.00 19.91 ? 21   VAL   A CA   1 
ATOM   127  C  C    . VAL   A 1 18  ? -30.174 -67.406 27.170 1.00 22.42 ? 21   VAL   A C    1 
ATOM   128  O  O    . VAL   A 1 18  ? -29.670 -66.753 28.092 1.00 20.16 ? 21   VAL   A O    1 
ATOM   129  C  CB   . VAL   A 1 18  ? -31.105 -65.642 25.661 1.00 23.55 ? 21   VAL   A CB   1 
ATOM   130  C  CG1  . VAL   A 1 18  ? -29.939 -65.922 24.723 1.00 23.37 ? 21   VAL   A CG1  1 
ATOM   131  C  CG2  . VAL   A 1 18  ? -32.327 -65.186 24.877 1.00 21.87 ? 21   VAL   A CG2  1 
ATOM   132  N  N    . SER   A 1 19  ? -29.688 -68.567 26.746 1.00 24.32 ? 22   SER   A N    1 
ATOM   133  C  CA   . SER   A 1 19  ? -28.491 -69.147 27.327 1.00 27.13 ? 22   SER   A CA   1 
ATOM   134  C  C    . SER   A 1 19  ? -27.263 -68.733 26.537 1.00 27.56 ? 22   SER   A C    1 
ATOM   135  O  O    . SER   A 1 19  ? -27.293 -68.637 25.305 1.00 25.68 ? 22   SER   A O    1 
ATOM   136  C  CB   . SER   A 1 19  ? -28.595 -70.672 27.370 1.00 29.03 ? 22   SER   A CB   1 
ATOM   137  O  OG   . SER   A 1 19  ? -29.412 -71.084 28.452 1.00 34.74 ? 22   SER   A OG   1 
ATOM   138  N  N    . LEU   A 1 20  ? -26.188 -68.471 27.260 1.00 23.10 ? 23   LEU   A N    1 
ATOM   139  C  CA   . LEU   A 1 20  ? -24.873 -68.246 26.682 1.00 22.32 ? 23   LEU   A CA   1 
ATOM   140  C  C    . LEU   A 1 20  ? -24.053 -69.476 27.030 1.00 23.53 ? 23   LEU   A C    1 
ATOM   141  O  O    . LEU   A 1 20  ? -23.957 -69.828 28.209 1.00 22.22 ? 23   LEU   A O    1 
ATOM   142  C  CB   . LEU   A 1 20  ? -24.244 -66.978 27.255 1.00 21.30 ? 23   LEU   A CB   1 
ATOM   143  C  CG   . LEU   A 1 20  ? -22.946 -66.488 26.613 1.00 22.25 ? 23   LEU   A CG   1 
ATOM   144  C  CD1  . LEU   A 1 20  ? -23.168 -66.135 25.149 1.00 23.97 ? 23   LEU   A CD1  1 
ATOM   145  C  CD2  . LEU   A 1 20  ? -22.402 -65.303 27.371 1.00 23.68 ? 23   LEU   A CD2  1 
ATOM   146  N  N    . GLU   A 1 21  ? -23.517 -70.157 26.019 1.00 24.82 ? 24   GLU   A N    1 
ATOM   147  C  CA   . GLU   A 1 21  ? -22.835 -71.423 26.272 1.00 27.61 ? 24   GLU   A CA   1 
ATOM   148  C  C    . GLU   A 1 21  ? -21.783 -71.257 27.362 1.00 25.92 ? 24   GLU   A C    1 
ATOM   149  O  O    . GLU   A 1 21  ? -21.023 -70.280 27.371 1.00 23.45 ? 24   GLU   A O    1 
ATOM   150  C  CB   . GLU   A 1 21  ? -22.193 -71.955 24.992 1.00 32.35 ? 24   GLU   A CB   1 
ATOM   151  C  CG   . GLU   A 1 21  ? -21.319 -73.184 25.248 1.00 40.09 ? 24   GLU   A CG   1 
ATOM   152  C  CD   . GLU   A 1 21  ? -20.592 -73.674 24.010 1.00 47.46 ? 24   GLU   A CD   1 
ATOM   153  O  OE1  . GLU   A 1 21  ? -21.194 -73.618 22.913 1.00 50.00 ? 24   GLU   A OE1  1 
ATOM   154  O  OE2  . GLU   A 1 21  ? -19.432 -74.135 24.138 1.00 47.84 ? 24   GLU   A OE2  1 
ATOM   155  N  N    . GLY   A 1 22  ? -21.776 -72.196 28.313 1.00 27.73 ? 25   GLY   A N    1 
ATOM   156  C  CA   . GLY   A 1 22  ? -20.842 -72.171 29.425 1.00 22.28 ? 25   GLY   A CA   1 
ATOM   157  C  C    . GLY   A 1 22  ? -21.382 -71.563 30.702 1.00 22.98 ? 25   GLY   A C    1 
ATOM   158  O  O    . GLY   A 1 22  ? -20.745 -71.699 31.755 1.00 19.96 ? 25   GLY   A O    1 
ATOM   159  N  N    . PHE   A 1 23  ? -22.518 -70.873 30.643 1.00 19.59 ? 26   PHE   A N    1 
ATOM   160  C  CA   . PHE   A 1 23  ? -23.126 -70.264 31.818 1.00 20.83 ? 26   PHE   A CA   1 
ATOM   161  C  C    . PHE   A 1 23  ? -24.397 -71.038 32.151 1.00 23.42 ? 26   PHE   A C    1 
ATOM   162  O  O    . PHE   A 1 23  ? -25.292 -71.163 31.307 1.00 25.38 ? 26   PHE   A O    1 
ATOM   163  C  CB   . PHE   A 1 23  ? -23.409 -68.778 31.575 1.00 21.47 ? 26   PHE   A CB   1 
ATOM   164  C  CG   . PHE   A 1 23  ? -22.157 -67.960 31.403 1.00 18.38 ? 26   PHE   A CG   1 
ATOM   165  C  CD1  . PHE   A 1 23  ? -21.536 -67.878 30.170 1.00 19.29 ? 26   PHE   A CD1  1 
ATOM   166  C  CD2  . PHE   A 1 23  ? -21.567 -67.343 32.486 1.00 17.20 ? 26   PHE   A CD2  1 
ATOM   167  C  CE1  . PHE   A 1 23  ? -20.369 -67.153 30.012 1.00 21.26 ? 26   PHE   A CE1  1 
ATOM   168  C  CE2  . PHE   A 1 23  ? -20.403 -66.618 32.340 1.00 19.85 ? 26   PHE   A CE2  1 
ATOM   169  C  CZ   . PHE   A 1 23  ? -19.798 -66.523 31.106 1.00 24.05 ? 26   PHE   A CZ   1 
ATOM   170  N  N    . ALA   A 1 24  ? -24.461 -71.570 33.376 1.00 21.75 ? 27   ALA   A N    1 
ATOM   171  C  CA   . ALA   A 1 24  ? -25.559 -72.459 33.751 1.00 22.12 ? 27   ALA   A CA   1 
ATOM   172  C  C    . ALA   A 1 24  ? -26.890 -71.720 33.786 1.00 25.60 ? 27   ALA   A C    1 
ATOM   173  O  O    . ALA   A 1 24  ? -27.914 -72.239 33.319 1.00 24.48 ? 27   ALA   A O    1 
ATOM   174  C  CB   . ALA   A 1 24  ? -25.268 -73.094 35.109 1.00 26.26 ? 27   ALA   A CB   1 
ATOM   175  N  N    . GLN   A 1 25  ? -26.899 -70.515 34.334 1.00 23.22 ? 28   GLN   A N    1 
ATOM   176  C  CA   . GLN   A 1 25  ? -28.142 -69.762 34.488 1.00 23.08 ? 28   GLN   A CA   1 
ATOM   177  C  C    . GLN   A 1 25  ? -28.426 -68.992 33.207 1.00 25.23 ? 28   GLN   A C    1 
ATOM   178  O  O    . GLN   A 1 25  ? -27.619 -68.133 32.821 1.00 21.92 ? 28   GLN   A O    1 
ATOM   179  C  CB   . GLN   A 1 25  ? -28.058 -68.814 35.682 1.00 25.19 ? 28   GLN   A CB   1 
ATOM   180  C  CG   . GLN   A 1 25  ? -29.334 -67.956 35.939 1.00 26.92 ? 28   GLN   A CG   1 
ATOM   181  C  CD   . GLN   A 1 25  ? -30.585 -68.789 36.214 1.00 30.74 ? 28   GLN   A CD   1 
ATOM   182  O  OE1  . GLN   A 1 25  ? -31.688 -68.440 35.779 1.00 31.39 ? 28   GLN   A OE1  1 
ATOM   183  N  NE2  . GLN   A 1 25  ? -30.417 -69.901 36.919 1.00 30.58 ? 28   GLN   A NE2  1 
ATOM   184  N  N    . PRO   A 1 26  ? -29.528 -69.271 32.511 1.00 24.09 ? 29   PRO   A N    1 
ATOM   185  C  CA   . PRO   A 1 26  ? -29.890 -68.444 31.355 1.00 21.34 ? 29   PRO   A CA   1 
ATOM   186  C  C    . PRO   A 1 26  ? -30.145 -67.005 31.784 1.00 20.00 ? 29   PRO   A C    1 
ATOM   187  O  O    . PRO   A 1 26  ? -30.499 -66.719 32.932 1.00 19.41 ? 29   PRO   A O    1 
ATOM   188  C  CB   . PRO   A 1 26  ? -31.165 -69.107 30.817 1.00 25.83 ? 29   PRO   A CB   1 
ATOM   189  C  CG   . PRO   A 1 26  ? -31.688 -69.938 31.942 1.00 27.34 ? 29   PRO   A CG   1 
ATOM   190  C  CD   . PRO   A 1 26  ? -30.528 -70.314 32.807 1.00 24.67 ? 29   PRO   A CD   1 
ATOM   191  N  N    . VAL   A 1 27  ? -29.914 -66.095 30.865 1.00 16.67 ? 30   VAL   A N    1 
ATOM   192  C  CA   . VAL   A 1 27  ? -30.173 -64.678 31.103 1.00 16.76 ? 30   VAL   A CA   1 
ATOM   193  C  C    . VAL   A 1 27  ? -31.631 -64.406 30.757 1.00 14.08 ? 30   VAL   A C    1 
ATOM   194  O  O    . VAL   A 1 27  ? -32.120 -64.833 29.705 1.00 18.43 ? 30   VAL   A O    1 
ATOM   195  C  CB   . VAL   A 1 27  ? -29.220 -63.800 30.274 1.00 16.52 ? 30   VAL   A CB   1 
ATOM   196  C  CG1  . VAL   A 1 27  ? -29.588 -62.301 30.386 1.00 14.15 ? 30   VAL   A CG1  1 
ATOM   197  C  CG2  . VAL   A 1 27  ? -27.758 -64.052 30.712 1.00 16.00 ? 30   VAL   A CG2  1 
ATOM   198  N  N    . ALA   A 1 28  ? -32.332 -63.720 31.652 1.00 16.21 ? 31   ALA   A N    1 
ATOM   199  C  CA   . ALA   A 1 28  ? -33.708 -63.298 31.408 1.00 16.21 ? 31   ALA   A CA   1 
ATOM   200  C  C    . ALA   A 1 28  ? -33.686 -61.947 30.690 1.00 15.61 ? 31   ALA   A C    1 
ATOM   201  O  O    . ALA   A 1 28  ? -33.082 -60.983 31.176 1.00 17.19 ? 31   ALA   A O    1 
ATOM   202  C  CB   . ALA   A 1 28  ? -34.471 -63.227 32.730 1.00 16.89 ? 31   ALA   A CB   1 
ATOM   203  N  N    . ILE   A 1 29  ? -34.311 -61.887 29.520 1.00 15.35 ? 32   ILE   A N    1 
ATOM   204  C  CA   . ILE   A 1 29  ? -34.256 -60.727 28.642 1.00 15.63 ? 32   ILE   A CA   1 
ATOM   205  C  C    . ILE   A 1 29  ? -35.668 -60.169 28.461 1.00 15.09 ? 32   ILE   A C    1 
ATOM   206  O  O    . ILE   A 1 29  ? -36.610 -60.916 28.151 1.00 15.59 ? 32   ILE   A O    1 
ATOM   207  C  CB   . ILE   A 1 29  ? -33.615 -61.102 27.293 1.00 16.13 ? 32   ILE   A CB   1 
ATOM   208  C  CG1  . ILE   A 1 29  ? -32.159 -61.555 27.536 1.00 17.34 ? 32   ILE   A CG1  1 
ATOM   209  C  CG2  . ILE   A 1 29  ? -33.683 -59.936 26.335 1.00 19.28 ? 32   ILE   A CG2  1 
ATOM   210  C  CD1  . ILE   A 1 29  ? -31.475 -62.070 26.315 1.00 21.52 ? 32   ILE   A CD1  1 
ATOM   211  N  N    . PHE   A 1 30  ? -35.804 -58.852 28.637 1.00 14.11 ? 33   PHE   A N    1 
ATOM   212  C  CA   . PHE   A 1 30  ? -37.088 -58.163 28.527 1.00 15.46 ? 33   PHE   A CA   1 
ATOM   213  C  C    . PHE   A 1 30  ? -36.904 -57.024 27.545 1.00 16.26 ? 33   PHE   A C    1 
ATOM   214  O  O    . PHE   A 1 30  ? -36.097 -56.124 27.794 1.00 16.10 ? 33   PHE   A O    1 
ATOM   215  C  CB   . PHE   A 1 30  ? -37.568 -57.644 29.886 1.00 13.53 ? 33   PHE   A CB   1 
ATOM   216  C  CG   . PHE   A 1 30  ? -37.719 -58.712 30.920 1.00 16.36 ? 33   PHE   A CG   1 
ATOM   217  C  CD1  . PHE   A 1 30  ? -36.616 -59.164 31.642 1.00 15.98 ? 33   PHE   A CD1  1 
ATOM   218  C  CD2  . PHE   A 1 30  ? -38.967 -59.293 31.158 1.00 16.71 ? 33   PHE   A CD2  1 
ATOM   219  C  CE1  . PHE   A 1 30  ? -36.753 -60.172 32.603 1.00 17.77 ? 33   PHE   A CE1  1 
ATOM   220  C  CE2  . PHE   A 1 30  ? -39.115 -60.300 32.115 1.00 17.51 ? 33   PHE   A CE2  1 
ATOM   221  C  CZ   . PHE   A 1 30  ? -38.004 -60.743 32.839 1.00 20.84 ? 33   PHE   A CZ   1 
ATOM   222  N  N    . LEU   A 1 31  ? -37.593 -57.099 26.410 1.00 14.36 ? 34   LEU   A N    1 
ATOM   223  C  CA   . LEU   A 1 31  ? -37.406 -56.161 25.308 1.00 16.30 ? 34   LEU   A CA   1 
ATOM   224  C  C    . LEU   A 1 31  ? -38.613 -55.238 25.221 1.00 17.20 ? 34   LEU   A C    1 
ATOM   225  O  O    . LEU   A 1 31  ? -39.758 -55.709 25.186 1.00 16.19 ? 34   LEU   A O    1 
ATOM   226  C  CB   . LEU   A 1 31  ? -37.224 -56.903 23.982 1.00 15.07 ? 34   LEU   A CB   1 
ATOM   227  C  CG   . LEU   A 1 31  ? -36.045 -57.883 23.952 1.00 15.97 ? 34   LEU   A CG   1 
ATOM   228  C  CD1  . LEU   A 1 31  ? -35.952 -58.547 22.585 1.00 18.99 ? 34   LEU   A CD1  1 
ATOM   229  C  CD2  . LEU   A 1 31  ? -34.742 -57.126 24.289 1.00 15.33 ? 34   LEU   A CD2  1 
ATOM   230  N  N    . GLY   A 1 32  ? -38.358 -53.933 25.171 1.00 12.62 ? 35   GLY   A N    1 
ATOM   231  C  CA   . GLY   A 1 32  ? -39.429 -52.985 24.922 1.00 15.05 ? 35   GLY   A CA   1 
ATOM   232  C  C    . GLY   A 1 32  ? -40.348 -52.750 26.102 1.00 15.37 ? 35   GLY   A C    1 
ATOM   233  O  O    . GLY   A 1 32  ? -41.580 -52.759 25.961 1.00 16.48 ? 35   GLY   A O    1 
ATOM   234  N  N    . ILE   A 1 33  ? -39.768 -52.542 27.278 1.00 12.82 ? 36   ILE   A N    1 
ATOM   235  C  CA   . ILE   A 1 33  ? -40.546 -52.084 28.428 1.00 12.32 ? 36   ILE   A CA   1 
ATOM   236  C  C    . ILE   A 1 33  ? -40.732 -50.572 28.345 1.00 11.45 ? 36   ILE   A C    1 
ATOM   237  O  O    . ILE   A 1 33  ? -39.733 -49.840 28.299 1.00 13.13 ? 36   ILE   A O    1 
ATOM   238  C  CB   . ILE   A 1 33  ? -39.857 -52.468 29.741 1.00 13.12 ? 36   ILE   A CB   1 
ATOM   239  C  CG1  . ILE   A 1 33  ? -39.685 -53.993 29.832 1.00 17.48 ? 36   ILE   A CG1  1 
ATOM   240  C  CG2  . ILE   A 1 33  ? -40.682 -51.960 30.919 1.00 13.58 ? 36   ILE   A CG2  1 
ATOM   241  C  CD1  . ILE   A 1 33  ? -38.963 -54.423 31.095 1.00 19.51 ? 36   ILE   A CD1  1 
ATOM   242  N  N    . PRO   A 1 34  ? -41.963 -50.054 28.351 1.00 13.53 ? 37   PRO   A N    1 
ATOM   243  C  CA   . PRO   A 1 34  ? -42.140 -48.595 28.331 1.00 12.06 ? 37   PRO   A CA   1 
ATOM   244  C  C    . PRO   A 1 34  ? -41.785 -47.994 29.675 1.00 16.52 ? 37   PRO   A C    1 
ATOM   245  O  O    . PRO   A 1 34  ? -42.151 -48.531 30.722 1.00 15.27 ? 37   PRO   A O    1 
ATOM   246  C  CB   . PRO   A 1 34  ? -43.643 -48.412 28.028 1.00 14.59 ? 37   PRO   A CB   1 
ATOM   247  C  CG   . PRO   A 1 34  ? -44.288 -49.659 28.559 1.00 14.52 ? 37   PRO   A CG   1 
ATOM   248  C  CD   . PRO   A 1 34  ? -43.247 -50.780 28.404 1.00 13.92 ? 37   PRO   A CD   1 
ATOM   249  N  N    . PHE   A 1 35  ? -41.056 -46.874 29.651 1.00 13.52 ? 38   PHE   A N    1 
ATOM   250  C  CA   . PHE   A 1 35  ? -40.780 -46.138 30.877 1.00 13.56 ? 38   PHE   A CA   1 
ATOM   251  C  C    . PHE   A 1 35  ? -41.484 -44.791 30.919 1.00 14.56 ? 38   PHE   A C    1 
ATOM   252  O  O    . PHE   A 1 35  ? -41.367 -44.079 31.915 1.00 13.91 ? 38   PHE   A O    1 
ATOM   253  C  CB   . PHE   A 1 35  ? -39.266 -45.965 31.097 1.00 14.59 ? 38   PHE   A CB   1 
ATOM   254  C  CG   . PHE   A 1 35  ? -38.552 -45.134 30.053 1.00 12.81 ? 38   PHE   A CG   1 
ATOM   255  C  CD1  . PHE   A 1 35  ? -38.498 -43.749 30.159 1.00 12.93 ? 38   PHE   A CD1  1 
ATOM   256  C  CD2  . PHE   A 1 35  ? -37.884 -45.749 28.996 1.00 14.56 ? 38   PHE   A CD2  1 
ATOM   257  C  CE1  . PHE   A 1 35  ? -37.818 -42.977 29.210 1.00 13.18 ? 38   PHE   A CE1  1 
ATOM   258  C  CE2  . PHE   A 1 35  ? -37.206 -44.990 28.035 1.00 14.96 ? 38   PHE   A CE2  1 
ATOM   259  C  CZ   . PHE   A 1 35  ? -37.170 -43.590 28.156 1.00 12.59 ? 38   PHE   A CZ   1 
ATOM   260  N  N    . ALA   A 1 36  ? -42.228 -44.437 29.875 1.00 13.92 ? 39   ALA   A N    1 
ATOM   261  C  CA   . ALA   A 1 36  ? -42.986 -43.194 29.837 1.00 13.12 ? 39   ALA   A CA   1 
ATOM   262  C  C    . ALA   A 1 36  ? -44.218 -43.399 28.970 1.00 14.41 ? 39   ALA   A C    1 
ATOM   263  O  O    . ALA   A 1 36  ? -44.366 -44.413 28.283 1.00 15.08 ? 39   ALA   A O    1 
ATOM   264  C  CB   . ALA   A 1 36  ? -42.154 -42.034 29.281 1.00 12.19 ? 39   ALA   A CB   1 
ATOM   265  N  N    . LYS   A 1 37  ? -45.100 -42.415 29.000 1.00 13.17 ? 40   LYS   A N    1 
ATOM   266  C  CA   . LYS   A 1 37  ? -46.202 -42.380 28.062 1.00 13.40 ? 40   LYS   A CA   1 
ATOM   267  C  C    . LYS   A 1 37  ? -45.663 -42.022 26.681 1.00 13.78 ? 40   LYS   A C    1 
ATOM   268  O  O    . LYS   A 1 37  ? -44.784 -41.167 26.576 1.00 16.25 ? 40   LYS   A O    1 
ATOM   269  C  CB   . LYS   A 1 37  ? -47.225 -41.331 28.530 1.00 16.35 ? 40   LYS   A CB   1 
ATOM   270  C  CG   . LYS   A 1 37  ? -48.533 -41.340 27.806 1.00 20.28 ? 40   LYS   A CG   1 
ATOM   271  C  CD   . LYS   A 1 37  ? -49.518 -40.390 28.494 1.00 21.67 ? 40   LYS   A CD   1 
ATOM   272  C  CE   . LYS   A 1 37  ? -50.928 -40.634 27.976 1.00 37.16 ? 40   LYS   A CE   1 
ATOM   273  N  NZ   . LYS   A 1 37  ? -51.807 -39.440 28.169 1.00 45.23 ? 40   LYS   A NZ   1 
ATOM   274  N  N    . PRO   A 1 38  ? -46.151 -42.651 25.616 1.00 12.99 ? 41   PRO   A N    1 
ATOM   275  C  CA   . PRO   A 1 38  ? -45.653 -42.324 24.266 1.00 13.74 ? 41   PRO   A CA   1 
ATOM   276  C  C    . PRO   A 1 38  ? -45.831 -40.848 23.968 1.00 16.46 ? 41   PRO   A C    1 
ATOM   277  O  O    . PRO   A 1 38  ? -46.936 -40.298 24.122 1.00 15.32 ? 41   PRO   A O    1 
ATOM   278  C  CB   . PRO   A 1 38  ? -46.519 -43.199 23.349 1.00 16.69 ? 41   PRO   A CB   1 
ATOM   279  C  CG   . PRO   A 1 38  ? -46.901 -44.371 24.245 1.00 16.10 ? 41   PRO   A CG   1 
ATOM   280  C  CD   . PRO   A 1 38  ? -47.143 -43.743 25.584 1.00 16.43 ? 41   PRO   A CD   1 
ATOM   281  N  N    . PRO   A 1 39  ? -44.748 -40.153 23.570 1.00 13.93 ? 42   PRO   A N    1 
ATOM   282  C  CA   . PRO   A 1 39  ? -44.781 -38.675 23.474 1.00 14.13 ? 42   PRO   A CA   1 
ATOM   283  C  C    . PRO   A 1 39  ? -45.352 -38.200 22.141 1.00 18.49 ? 42   PRO   A C    1 
ATOM   284  O  O    . PRO   A 1 39  ? -44.689 -37.570 21.311 1.00 18.74 ? 42   PRO   A O    1 
ATOM   285  C  CB   . PRO   A 1 39  ? -43.303 -38.305 23.659 1.00 12.96 ? 42   PRO   A CB   1 
ATOM   286  C  CG   . PRO   A 1 39  ? -42.567 -39.441 23.003 1.00 12.64 ? 42   PRO   A CG   1 
ATOM   287  C  CD   . PRO   A 1 39  ? -43.403 -40.694 23.273 1.00 15.66 ? 42   PRO   A CD   1 
ATOM   288  N  N    . LEU   A 1 40  ? -46.635 -38.495 21.938 1.00 16.78 ? 43   LEU   A N    1 
ATOM   289  C  CA   . LEU   A 1 40  ? -47.342 -38.260 20.689 1.00 16.49 ? 43   LEU   A CA   1 
ATOM   290  C  C    . LEU   A 1 40  ? -48.233 -37.022 20.791 1.00 18.16 ? 43   LEU   A C    1 
ATOM   291  O  O    . LEU   A 1 40  ? -48.663 -36.619 21.877 1.00 18.00 ? 43   LEU   A O    1 
ATOM   292  C  CB   . LEU   A 1 40  ? -48.202 -39.479 20.341 1.00 16.82 ? 43   LEU   A CB   1 
ATOM   293  C  CG   . LEU   A 1 40  ? -47.503 -40.842 20.324 1.00 17.42 ? 43   LEU   A CG   1 
ATOM   294  C  CD1  . LEU   A 1 40  ? -48.461 -41.930 19.829 1.00 17.69 ? 43   LEU   A CD1  1 
ATOM   295  C  CD2  . LEU   A 1 40  ? -46.260 -40.796 19.437 1.00 18.08 ? 43   LEU   A CD2  1 
ATOM   296  N  N    . GLY   A 1 41  ? -48.526 -36.435 19.638 1.00 16.50 ? 44   GLY   A N    1 
ATOM   297  C  CA   . GLY   A 1 41  ? -49.482 -35.343 19.559 1.00 23.78 ? 44   GLY   A CA   1 
ATOM   298  C  C    . GLY   A 1 41  ? -49.079 -34.133 20.380 1.00 21.15 ? 44   GLY   A C    1 
ATOM   299  O  O    . GLY   A 1 41  ? -47.982 -33.589 20.220 1.00 22.26 ? 44   GLY   A O    1 
ATOM   300  N  N    . PRO   A 1 42  ? -49.946 -33.716 21.310 1.00 22.08 ? 45   PRO   A N    1 
ATOM   301  C  CA   . PRO   A 1 42  ? -49.600 -32.579 22.185 1.00 24.76 ? 45   PRO   A CA   1 
ATOM   302  C  C    . PRO   A 1 42  ? -48.415 -32.842 23.108 1.00 23.29 ? 45   PRO   A C    1 
ATOM   303  O  O    . PRO   A 1 42  ? -47.844 -31.883 23.647 1.00 21.36 ? 45   PRO   A O    1 
ATOM   304  C  CB   . PRO   A 1 42  ? -50.887 -32.358 22.990 1.00 27.82 ? 45   PRO   A CB   1 
ATOM   305  C  CG   . PRO   A 1 42  ? -51.528 -33.700 23.017 1.00 30.98 ? 45   PRO   A CG   1 
ATOM   306  C  CD   . PRO   A 1 42  ? -51.258 -34.284 21.651 1.00 25.63 ? 45   PRO   A CD   1 
ATOM   307  N  N    . LEU   A 1 43  ? -48.030 -34.103 23.327 1.00 20.31 ? 46   LEU   A N    1 
ATOM   308  C  CA   . LEU   A 1 43  ? -46.890 -34.387 24.190 1.00 19.76 ? 46   LEU   A CA   1 
ATOM   309  C  C    . LEU   A 1 43  ? -45.555 -34.174 23.490 1.00 17.62 ? 46   LEU   A C    1 
ATOM   310  O  O    . LEU   A 1 43  ? -44.509 -34.236 24.142 1.00 15.39 ? 46   LEU   A O    1 
ATOM   311  C  CB   . LEU   A 1 43  ? -46.978 -35.816 24.745 1.00 17.09 ? 46   LEU   A CB   1 
ATOM   312  C  CG   . LEU   A 1 43  ? -48.180 -36.097 25.658 1.00 23.27 ? 46   LEU   A CG   1 
ATOM   313  C  CD1  . LEU   A 1 43  ? -48.229 -37.564 26.110 1.00 23.12 ? 46   LEU   A CD1  1 
ATOM   314  C  CD2  . LEU   A 1 43  ? -48.189 -35.163 26.853 1.00 28.01 ? 46   LEU   A CD2  1 
ATOM   315  N  N    . ARG   A 1 44  ? -45.557 -33.913 22.190 1.00 14.98 ? 47   ARG   A N    1 
ATOM   316  C  CA   . ARG   A 1 44  ? -44.321 -33.579 21.504 1.00 16.50 ? 47   ARG   A CA   1 
ATOM   317  C  C    . ARG   A 1 44  ? -43.764 -32.260 22.046 1.00 16.50 ? 47   ARG   A C    1 
ATOM   318  O  O    . ARG   A 1 44  ? -44.513 -31.321 22.345 1.00 16.26 ? 47   ARG   A O    1 
ATOM   319  C  CB   . ARG   A 1 44  ? -44.594 -33.512 20.001 1.00 16.46 ? 47   ARG   A CB   1 
ATOM   320  C  CG   . ARG   A 1 44  ? -43.386 -33.416 19.116 1.00 22.79 ? 47   ARG   A CG   1 
ATOM   321  C  CD   . ARG   A 1 44  ? -43.826 -33.219 17.663 1.00 21.95 ? 47   ARG   A CD   1 
ATOM   322  N  NE   . ARG   A 1 44  ? -44.464 -34.379 17.038 1.00 25.08 ? 47   ARG   A NE   1 
ATOM   323  C  CZ   . ARG   A 1 44  ? -45.129 -34.314 15.888 1.00 26.79 ? 47   ARG   A CZ   1 
ATOM   324  N  NH1  . ARG   A 1 44  ? -45.367 -33.155 15.293 1.00 24.63 ? 47   ARG   A NH1  1 
ATOM   325  N  NH2  . ARG   A 1 44  ? -45.565 -35.435 15.317 1.00 19.95 ? 47   ARG   A NH2  1 
ATOM   326  N  N    . PHE   A 1 45  ? -42.443 -32.225 22.230 1.00 13.25 ? 48   PHE   A N    1 
ATOM   327  C  CA   . PHE   A 1 45  ? -41.724 -31.083 22.821 1.00 16.41 ? 48   PHE   A CA   1 
ATOM   328  C  C    . PHE   A 1 45  ? -42.199 -30.773 24.241 1.00 16.64 ? 48   PHE   A C    1 
ATOM   329  O  O    . PHE   A 1 45  ? -42.273 -29.609 24.646 1.00 16.13 ? 48   PHE   A O    1 
ATOM   330  C  CB   . PHE   A 1 45  ? -41.841 -29.825 21.947 1.00 15.46 ? 48   PHE   A CB   1 
ATOM   331  C  CG   . PHE   A 1 45  ? -41.683 -30.092 20.472 1.00 15.55 ? 48   PHE   A CG   1 
ATOM   332  C  CD1  . PHE   A 1 45  ? -40.566 -30.766 19.989 1.00 14.79 ? 48   PHE   A CD1  1 
ATOM   333  C  CD2  . PHE   A 1 45  ? -42.655 -29.665 19.575 1.00 17.79 ? 48   PHE   A CD2  1 
ATOM   334  C  CE1  . PHE   A 1 45  ? -40.421 -31.015 18.629 1.00 17.58 ? 48   PHE   A CE1  1 
ATOM   335  C  CE2  . PHE   A 1 45  ? -42.524 -29.899 18.212 1.00 16.76 ? 48   PHE   A CE2  1 
ATOM   336  C  CZ   . PHE   A 1 45  ? -41.399 -30.580 17.735 1.00 17.07 ? 48   PHE   A CZ   1 
ATOM   337  N  N    . THR   A 1 46  ? -42.545 -31.799 25.002 1.00 14.60 ? 49   THR   A N    1 
ATOM   338  C  CA   . THR   A 1 46  ? -42.879 -31.663 26.414 1.00 14.56 ? 49   THR   A CA   1 
ATOM   339  C  C    . THR   A 1 46  ? -42.115 -32.707 27.212 1.00 15.11 ? 49   THR   A C    1 
ATOM   340  O  O    . THR   A 1 46  ? -41.617 -33.684 26.643 1.00 16.24 ? 49   THR   A O    1 
ATOM   341  C  CB   . THR   A 1 46  ? -44.391 -31.829 26.689 1.00 17.02 ? 49   THR   A CB   1 
ATOM   342  O  OG1  . THR   A 1 46  ? -44.770 -33.202 26.540 1.00 18.43 ? 49   THR   A OG1  1 
ATOM   343  C  CG2  . THR   A 1 46  ? -45.254 -30.947 25.785 1.00 16.59 ? 49   THR   A CG2  1 
ATOM   344  N  N    . PRO   A 1 47  ? -42.011 -32.539 28.533 1.00 16.27 ? 50   PRO   A N    1 
ATOM   345  C  CA   . PRO   A 1 47  ? -41.319 -33.545 29.344 1.00 12.02 ? 50   PRO   A CA   1 
ATOM   346  C  C    . PRO   A 1 47  ? -42.053 -34.878 29.309 1.00 15.62 ? 50   PRO   A C    1 
ATOM   347  O  O    . PRO   A 1 47  ? -43.282 -34.926 29.109 1.00 14.19 ? 50   PRO   A O    1 
ATOM   348  C  CB   . PRO   A 1 47  ? -41.332 -32.937 30.755 1.00 13.07 ? 50   PRO   A CB   1 
ATOM   349  C  CG   . PRO   A 1 47  ? -41.380 -31.449 30.516 1.00 14.89 ? 50   PRO   A CG   1 
ATOM   350  C  CD   . PRO   A 1 47  ? -42.283 -31.303 29.300 1.00 15.90 ? 50   PRO   A CD   1 
ATOM   351  N  N    . PRO   A 1 48  ? -41.326 -35.979 29.474 1.00 14.00 ? 51   PRO   A N    1 
ATOM   352  C  CA   . PRO   A 1 48  ? -41.978 -37.296 29.484 1.00 12.54 ? 51   PRO   A CA   1 
ATOM   353  C  C    . PRO   A 1 48  ? -42.896 -37.433 30.682 1.00 15.94 ? 51   PRO   A C    1 
ATOM   354  O  O    . PRO   A 1 48  ? -42.569 -37.002 31.788 1.00 15.90 ? 51   PRO   A O    1 
ATOM   355  C  CB   . PRO   A 1 48  ? -40.799 -38.284 29.574 1.00 12.70 ? 51   PRO   A CB   1 
ATOM   356  C  CG   . PRO   A 1 48  ? -39.685 -37.490 30.175 1.00 12.32 ? 51   PRO   A CG   1 
ATOM   357  C  CD   . PRO   A 1 48  ? -39.868 -36.073 29.682 1.00 13.08 ? 51   PRO   A CD   1 
ATOM   358  N  N    . GLN   A 1 49  ? -44.060 -38.035 30.451 1.00 18.34 ? 52   GLN   A N    1 
ATOM   359  C  CA   . GLN   A 1 49  ? -44.999 -38.324 31.516 1.00 17.06 ? 52   GLN   A CA   1 
ATOM   360  C  C    . GLN   A 1 49  ? -44.929 -39.801 31.878 1.00 16.65 ? 52   GLN   A C    1 
ATOM   361  O  O    . GLN   A 1 49  ? -44.477 -40.622 31.076 1.00 16.13 ? 52   GLN   A O    1 
ATOM   362  C  CB   . GLN   A 1 49  ? -46.417 -37.943 31.083 1.00 18.08 ? 52   GLN   A CB   1 
ATOM   363  C  CG   . GLN   A 1 49  ? -46.508 -36.458 30.754 1.00 19.35 ? 52   GLN   A CG   1 
ATOM   364  C  CD   . GLN   A 1 49  ? -47.908 -36.004 30.457 1.00 33.04 ? 52   GLN   A CD   1 
ATOM   365  O  OE1  . GLN   A 1 49  ? -48.824 -36.819 30.330 1.00 38.92 ? 52   GLN   A OE1  1 
ATOM   366  N  NE2  . GLN   A 1 49  ? -48.089 -34.690 30.327 1.00 33.66 ? 52   GLN   A NE2  1 
ATOM   367  N  N    . PRO   A 1 50  ? -45.341 -40.178 33.091 1.00 19.11 ? 53   PRO   A N    1 
ATOM   368  C  CA   . PRO   A 1 50  ? -45.259 -41.594 33.484 1.00 21.20 ? 53   PRO   A CA   1 
ATOM   369  C  C    . PRO   A 1 50  ? -46.095 -42.483 32.576 1.00 19.02 ? 53   PRO   A C    1 
ATOM   370  O  O    . PRO   A 1 50  ? -47.137 -42.078 32.054 1.00 17.82 ? 53   PRO   A O    1 
ATOM   371  C  CB   . PRO   A 1 50  ? -45.797 -41.601 34.920 1.00 24.36 ? 53   PRO   A CB   1 
ATOM   372  C  CG   . PRO   A 1 50  ? -45.637 -40.180 35.397 1.00 27.50 ? 53   PRO   A CG   1 
ATOM   373  C  CD   . PRO   A 1 50  ? -45.802 -39.313 34.195 1.00 23.52 ? 53   PRO   A CD   1 
ATOM   374  N  N    . ALA   A 1 51  ? -45.620 -43.713 32.390 1.00 17.53 ? 54   ALA   A N    1 
ATOM   375  C  CA   . ALA   A 1 51  ? -46.368 -44.702 31.625 1.00 16.55 ? 54   ALA   A CA   1 
ATOM   376  C  C    . ALA   A 1 51  ? -47.694 -45.009 32.311 1.00 22.28 ? 54   ALA   A C    1 
ATOM   377  O  O    . ALA   A 1 51  ? -47.784 -45.049 33.543 1.00 21.01 ? 54   ALA   A O    1 
ATOM   378  C  CB   . ALA   A 1 51  ? -45.543 -45.984 31.477 1.00 16.44 ? 54   ALA   A CB   1 
ATOM   379  N  N    . GLU   A 1 52  ? -48.695 -45.221 31.499 1.00 17.85 ? 55   GLU   A N    1 
ATOM   380  C  CA   . GLU   A 1 52  ? -49.961 -45.646 32.060 1.00 21.68 ? 55   GLU   A CA   1 
ATOM   381  C  C    . GLU   A 1 52  ? -49.899 -47.139 32.419 1.00 19.92 ? 55   GLU   A C    1 
ATOM   382  O  O    . GLU   A 1 52  ? -49.289 -47.908 31.750 1.00 18.55 ? 55   GLU   A O    1 
ATOM   383  C  CB   . GLU   A 1 52  ? -51.102 -45.356 31.091 1.00 22.08 ? 55   GLU   A CB   1 
ATOM   384  C  CG   . GLU   A 1 52  ? -51.390 -43.885 30.892 1.00 23.50 ? 55   GLU   A CG   1 
ATOM   385  C  CD   . GLU   A 1 52  ? -52.154 -43.289 32.054 1.00 40.99 ? 55   GLU   A CD   1 
ATOM   386  O  OE1  . GLU   A 1 52  ? -51.740 -42.237 32.567 1.00 43.81 ? 55   GLU   A OE1  1 
ATOM   387  O  OE2  . GLU   A 1 52  ? -53.172 -43.879 32.467 1.00 50.01 ? 55   GLU   A OE2  1 
ATOM   388  N  N    . PRO   A 1 53  ? -50.544 -47.507 33.502 1.00 22.17 ? 56   PRO   A N    1 
ATOM   389  C  CA   . PRO   A 1 53  ? -50.562 -48.896 33.963 1.00 19.47 ? 56   PRO   A CA   1 
ATOM   390  C  C    . PRO   A 1 53  ? -51.344 -49.842 33.067 1.00 19.43 ? 56   PRO   A C    1 
ATOM   391  O  O    . PRO   A 1 53  ? -52.239 -49.426 32.389 1.00 20.06 ? 56   PRO   A O    1 
ATOM   392  C  CB   . PRO   A 1 53  ? -51.242 -48.787 35.327 1.00 20.71 ? 56   PRO   A CB   1 
ATOM   393  C  CG   . PRO   A 1 53  ? -51.972 -47.504 35.313 1.00 21.97 ? 56   PRO   A CG   1 
ATOM   394  C  CD   . PRO   A 1 53  ? -51.137 -46.594 34.488 1.00 24.80 ? 56   PRO   A CD   1 
ATOM   395  N  N    . TRP   A 1 54  ? -50.954 -51.096 33.042 1.00 16.28 ? 57   TRP   A N    1 
ATOM   396  C  CA   . TRP   A 1 54  ? -51.638 -52.064 32.226 1.00 17.62 ? 57   TRP   A CA   1 
ATOM   397  C  C    . TRP   A 1 54  ? -52.127 -53.289 32.938 1.00 20.44 ? 57   TRP   A C    1 
ATOM   398  O  O    . TRP   A 1 54  ? -51.546 -53.710 33.929 1.00 16.90 ? 57   TRP   A O    1 
ATOM   399  C  CB   . TRP   A 1 54  ? -50.767 -52.512 31.067 1.00 18.92 ? 57   TRP   A CB   1 
ATOM   400  C  CG   . TRP   A 1 54  ? -49.442 -53.099 31.480 1.00 18.74 ? 57   TRP   A CG   1 
ATOM   401  C  CD1  . TRP   A 1 54  ? -49.146 -54.423 31.776 1.00 19.14 ? 57   TRP   A CD1  1 
ATOM   402  C  CD2  . TRP   A 1 54  ? -48.179 -52.385 31.640 1.00 20.05 ? 57   TRP   A CD2  1 
ATOM   403  N  NE1  . TRP   A 1 54  ? -47.826 -54.567 32.099 1.00 20.05 ? 57   TRP   A NE1  1 
ATOM   404  C  CE2  . TRP   A 1 54  ? -47.193 -53.384 32.040 1.00 21.59 ? 57   TRP   A CE2  1 
ATOM   405  C  CE3  . TRP   A 1 54  ? -47.784 -51.073 31.497 1.00 19.01 ? 57   TRP   A CE3  1 
ATOM   406  C  CZ2  . TRP   A 1 54  ? -45.880 -53.051 32.282 1.00 21.56 ? 57   TRP   A CZ2  1 
ATOM   407  C  CZ3  . TRP   A 1 54  ? -46.456 -50.752 31.741 1.00 22.58 ? 57   TRP   A CZ3  1 
ATOM   408  C  CH2  . TRP   A 1 54  ? -45.529 -51.720 32.123 1.00 21.04 ? 57   TRP   A CH2  1 
ATOM   409  N  N    . SER   A 1 55  ? -53.272 -53.774 32.507 1.00 17.92 ? 58   SER   A N    1 
ATOM   410  C  CA   . SER   A 1 55  ? -53.814 -55.000 33.040 1.00 19.98 ? 58   SER   A CA   1 
ATOM   411  C  C    . SER   A 1 55  ? -53.131 -56.249 32.442 1.00 20.86 ? 58   SER   A C    1 
ATOM   412  O  O    . SER   A 1 55  ? -52.531 -56.178 31.402 1.00 24.42 ? 58   SER   A O    1 
ATOM   413  C  CB   . SER   A 1 55  ? -55.355 -54.993 32.886 1.00 21.33 ? 58   SER   A CB   1 
ATOM   414  O  OG   . SER   A 1 55  ? -55.916 -53.780 33.312 1.00 19.21 ? 58   SER   A OG   1 
ATOM   415  N  N    . PHE   A 1 56  ? -53.175 -57.355 33.140 1.00 20.81 ? 59   PHE   A N    1 
ATOM   416  C  CA   . PHE   A 1 56  ? -52.659 -58.601 32.601 1.00 20.27 ? 59   PHE   A CA   1 
ATOM   417  C  C    . PHE   A 1 56  ? -51.142 -58.602 32.349 1.00 20.75 ? 59   PHE   A C    1 
ATOM   418  O  O    . PHE   A 1 56  ? -50.424 -57.868 32.935 1.00 23.64 ? 59   PHE   A O    1 
ATOM   419  C  CB   . PHE   A 1 56  ? -53.410 -58.996 31.337 1.00 19.58 ? 59   PHE   A CB   1 
ATOM   420  C  CG   . PHE   A 1 56  ? -54.883 -58.774 31.427 1.00 25.39 ? 59   PHE   A CG   1 
ATOM   421  C  CD1  . PHE   A 1 56  ? -55.628 -59.404 32.397 1.00 25.66 ? 59   PHE   A CD1  1 
ATOM   422  C  CD2  . PHE   A 1 56  ? -55.517 -57.923 30.548 1.00 24.97 ? 59   PHE   A CD2  1 
ATOM   423  C  CE1  . PHE   A 1 56  ? -56.985 -59.191 32.488 1.00 25.76 ? 59   PHE   A CE1  1 
ATOM   424  C  CE2  . PHE   A 1 56  ? -56.872 -57.707 30.632 1.00 21.94 ? 59   PHE   A CE2  1 
ATOM   425  C  CZ   . PHE   A 1 56  ? -57.606 -58.340 31.602 1.00 20.54 ? 59   PHE   A CZ   1 
ATOM   426  N  N    . VAL   A 1 57  ? -50.701 -59.412 31.419 1.00 18.50 ? 60   VAL   A N    1 
ATOM   427  C  CA   . VAL   A 1 57  ? -49.259 -59.498 31.243 1.00 18.64 ? 60   VAL   A CA   1 
ATOM   428  C  C    . VAL   A 1 57  ? -48.796 -58.965 29.915 1.00 16.61 ? 60   VAL   A C    1 
ATOM   429  O  O    . VAL   A 1 57  ? -49.279 -59.365 28.895 1.00 19.61 ? 60   VAL   A O    1 
ATOM   430  C  CB   . VAL   A 1 57  ? -48.785 -60.956 31.400 1.00 22.69 ? 60   VAL   A CB   1 
ATOM   431  C  CG1  . VAL   A 1 57  ? -47.276 -61.038 31.244 1.00 21.06 ? 60   VAL   A CG1  1 
ATOM   432  C  CG2  . VAL   A 1 57  ? -49.208 -61.514 32.741 1.00 18.54 ? 60   VAL   A CG2  1 
ATOM   433  N  N    . LYS   A 1 58  ? -47.855 -58.043 29.968 1.00 18.94 ? 61   LYS   A N    1 
ATOM   434  C  CA   . LYS   A 1 58  ? -47.301 -57.460 28.764 1.00 18.26 ? 61   LYS   A CA   1 
ATOM   435  C  C    . LYS   A 1 58  ? -46.174 -58.288 28.232 1.00 19.82 ? 61   LYS   A C    1 
ATOM   436  O  O    . LYS   A 1 58  ? -45.282 -58.649 28.952 1.00 19.36 ? 61   LYS   A O    1 
ATOM   437  C  CB   . LYS   A 1 58  ? -46.781 -56.046 29.000 1.00 19.12 ? 61   LYS   A CB   1 
ATOM   438  C  CG   . LYS   A 1 58  ? -46.142 -55.388 27.804 1.00 20.21 ? 61   LYS   A CG   1 
ATOM   439  C  CD   . LYS   A 1 58  ? -45.500 -54.067 28.176 1.00 20.97 ? 61   LYS   A CD   1 
ATOM   440  C  CE   . LYS   A 1 58  ? -46.521 -53.049 28.635 1.00 24.01 ? 61   LYS   A CE   1 
ATOM   441  N  NZ   . LYS   A 1 58  ? -47.466 -52.599 27.589 1.00 22.40 ? 61   LYS   A NZ   1 
ATOM   442  N  N    . ASN   A 1 59  ? -46.214 -58.514 26.945 1.00 17.72 ? 62   ASN   A N    1 
ATOM   443  C  CA   . ASN   A 1 59  ? -45.226 -59.315 26.355 1.00 24.26 ? 62   ASN   A CA   1 
ATOM   444  C  C    . ASN   A 1 59  ? -44.044 -58.443 25.976 1.00 23.22 ? 62   ASN   A C    1 
ATOM   445  O  O    . ASN   A 1 59  ? -44.139 -57.628 25.097 1.00 26.76 ? 62   ASN   A O    1 
ATOM   446  C  CB   . ASN   A 1 59  ? -45.838 -59.938 25.115 1.00 27.92 ? 62   ASN   A CB   1 
ATOM   447  C  CG   . ASN   A 1 59  ? -44.997 -61.035 24.516 1.00 33.22 ? 62   ASN   A CG   1 
ATOM   448  O  OD1  . ASN   A 1 59  ? -43.814 -61.139 24.774 1.00 30.71 ? 62   ASN   A OD1  1 
ATOM   449  N  ND2  . ASN   A 1 59  ? -45.619 -61.857 23.688 1.00 36.45 ? 62   ASN   A ND2  1 
ATOM   450  N  N    . ALA   A 1 60  ? -42.918 -58.695 26.592 1.00 20.65 ? 63   ALA   A N    1 
ATOM   451  C  CA   . ALA   A 1 60  ? -41.731 -57.897 26.367 1.00 18.04 ? 63   ALA   A CA   1 
ATOM   452  C  C    . ALA   A 1 60  ? -40.681 -58.764 25.687 1.00 21.61 ? 63   ALA   A C    1 
ATOM   453  O  O    . ALA   A 1 60  ? -39.633 -59.022 26.236 1.00 19.12 ? 63   ALA   A O    1 
ATOM   454  C  CB   . ALA   A 1 60  ? -41.253 -57.371 27.693 1.00 18.22 ? 63   ALA   A CB   1 
ATOM   455  N  N    . THR   A 1 61  ? -41.005 -59.230 24.491 1.00 19.24 ? 64   THR   A N    1 
ATOM   456  C  CA   . THR   A 1 61  ? -40.097 -60.127 23.786 1.00 20.33 ? 64   THR   A CA   1 
ATOM   457  C  C    . THR   A 1 61  ? -39.857 -59.689 22.343 1.00 21.26 ? 64   THR   A C    1 
ATOM   458  O  O    . THR   A 1 61  ? -39.286 -60.460 21.565 1.00 23.99 ? 64   THR   A O    1 
ATOM   459  C  CB   . THR   A 1 61  ? -40.597 -61.590 23.818 1.00 24.12 ? 64   THR   A CB   1 
ATOM   460  O  OG1  . THR   A 1 61  ? -41.803 -61.718 23.060 1.00 22.51 ? 64   THR   A OG1  1 
ATOM   461  C  CG2  . THR   A 1 61  ? -40.862 -62.065 25.256 1.00 20.16 ? 64   THR   A CG2  1 
ATOM   462  N  N    . SER   A 1 62  ? -40.237 -58.459 21.976 1.00 18.04 ? 65   SER   A N    1 
ATOM   463  C  CA   . SER   A 1 62  ? -39.959 -57.893 20.660 1.00 20.73 ? 65   SER   A CA   1 
ATOM   464  C  C    . SER   A 1 62  ? -39.170 -56.595 20.823 1.00 19.09 ? 65   SER   A C    1 
ATOM   465  O  O    . SER   A 1 62  ? -39.464 -55.794 21.717 1.00 17.18 ? 65   SER   A O    1 
ATOM   466  C  CB   . SER   A 1 62  ? -41.259 -57.598 19.895 1.00 23.49 ? 65   SER   A CB   1 
ATOM   467  O  OG   . SER   A 1 62  ? -41.942 -58.787 19.558 1.00 33.12 ? 65   SER   A OG   1 
ATOM   468  N  N    . TYR   A 1 63  ? -38.176 -56.380 19.960 1.00 18.30 ? 66   TYR   A N    1 
ATOM   469  C  CA   . TYR   A 1 63  ? -37.423 -55.130 20.022 1.00 14.61 ? 66   TYR   A CA   1 
ATOM   470  C  C    . TYR   A 1 63  ? -38.355 -53.937 19.792 1.00 15.41 ? 66   TYR   A C    1 
ATOM   471  O  O    . TYR   A 1 63  ? -39.235 -53.987 18.922 1.00 17.87 ? 66   TYR   A O    1 
ATOM   472  C  CB   . TYR   A 1 63  ? -36.299 -55.119 18.989 1.00 17.41 ? 66   TYR   A CB   1 
ATOM   473  C  CG   . TYR   A 1 63  ? -35.229 -56.109 19.352 1.00 22.07 ? 66   TYR   A CG   1 
ATOM   474  C  CD1  . TYR   A 1 63  ? -34.374 -55.872 20.420 1.00 18.28 ? 66   TYR   A CD1  1 
ATOM   475  C  CD2  . TYR   A 1 63  ? -35.124 -57.322 18.678 1.00 27.12 ? 66   TYR   A CD2  1 
ATOM   476  C  CE1  . TYR   A 1 63  ? -33.407 -56.801 20.777 1.00 21.67 ? 66   TYR   A CE1  1 
ATOM   477  C  CE2  . TYR   A 1 63  ? -34.167 -58.249 19.028 1.00 27.82 ? 66   TYR   A CE2  1 
ATOM   478  C  CZ   . TYR   A 1 63  ? -33.308 -57.978 20.078 1.00 27.76 ? 66   TYR   A CZ   1 
ATOM   479  O  OH   . TYR   A 1 63  ? -32.338 -58.895 20.430 1.00 30.90 ? 66   TYR   A OH   1 
ATOM   480  N  N    . PRO   A 1 64  ? -38.187 -52.851 20.533 1.00 16.34 ? 67   PRO   A N    1 
ATOM   481  C  CA   . PRO   A 1 64  ? -39.018 -51.655 20.303 1.00 16.56 ? 67   PRO   A CA   1 
ATOM   482  C  C    . PRO   A 1 64  ? -38.592 -50.923 19.043 1.00 15.85 ? 67   PRO   A C    1 
ATOM   483  O  O    . PRO   A 1 64  ? -37.477 -51.132 18.541 1.00 15.88 ? 67   PRO   A O    1 
ATOM   484  C  CB   . PRO   A 1 64  ? -38.757 -50.808 21.558 1.00 17.42 ? 67   PRO   A CB   1 
ATOM   485  C  CG   . PRO   A 1 64  ? -37.381 -51.214 22.011 1.00 16.12 ? 67   PRO   A CG   1 
ATOM   486  C  CD   . PRO   A 1 64  ? -37.258 -52.687 21.663 1.00 14.42 ? 67   PRO   A CD   1 
ATOM   487  N  N    . PRO   A 1 65  ? -39.435 -50.033 18.511 1.00 16.16 ? 68   PRO   A N    1 
ATOM   488  C  CA   . PRO   A 1 65  ? -38.967 -49.124 17.458 1.00 14.20 ? 68   PRO   A CA   1 
ATOM   489  C  C    . PRO   A 1 65  ? -37.809 -48.282 17.972 1.00 14.99 ? 68   PRO   A C    1 
ATOM   490  O  O    . PRO   A 1 65  ? -37.659 -48.062 19.175 1.00 13.55 ? 68   PRO   A O    1 
ATOM   491  C  CB   . PRO   A 1 65  ? -40.189 -48.240 17.154 1.00 16.62 ? 68   PRO   A CB   1 
ATOM   492  C  CG   . PRO   A 1 65  ? -41.362 -48.937 17.796 1.00 19.17 ? 68   PRO   A CG   1 
ATOM   493  C  CD   . PRO   A 1 65  ? -40.815 -49.740 18.935 1.00 21.13 ? 68   PRO   A CD   1 
ATOM   494  N  N    . MET   A 1 66  ? -36.989 -47.801 17.050 1.00 12.68 ? 69   MET   A N    1 
ATOM   495  C  CA   . MET   A 1 66  ? -36.078 -46.723 17.414 1.00 12.30 ? 69   MET   A CA   1 
ATOM   496  C  C    . MET   A 1 66  ? -36.754 -45.376 17.174 1.00 13.38 ? 69   MET   A C    1 
ATOM   497  O  O    . MET   A 1 66  ? -37.694 -45.268 16.392 1.00 14.86 ? 69   MET   A O    1 
ATOM   498  C  CB   . MET   A 1 66  ? -34.749 -46.790 16.654 1.00 15.01 ? 69   MET   A CB   1 
ATOM   499  C  CG   . MET   A 1 66  ? -34.840 -46.825 15.127 1.00 17.58 ? 69   MET   A CG   1 
ATOM   500  S  SD   . MET   A 1 66  ? -33.170 -47.199 14.471 1.00 23.77 ? 69   MET   A SD   1 
ATOM   501  C  CE   . MET   A 1 66  ? -33.216 -46.411 12.881 1.00 20.87 ? 69   MET   A CE   1 
ATOM   502  N  N    . CYS   A 1 67  ? -36.263 -44.354 17.869 1.00 11.71 ? 70   CYS   A N    1 
ATOM   503  C  CA   . CYS   A 1 67  ? -36.871 -43.031 17.772 1.00 12.93 ? 70   CYS   A CA   1 
ATOM   504  C  C    . CYS   A 1 67  ? -36.658 -42.494 16.363 1.00 13.93 ? 70   CYS   A C    1 
ATOM   505  O  O    . CYS   A 1 67  ? -35.658 -42.801 15.713 1.00 13.98 ? 70   CYS   A O    1 
ATOM   506  C  CB   . CYS   A 1 67  ? -36.282 -42.081 18.825 1.00 14.04 ? 70   CYS   A CB   1 
ATOM   507  S  SG   . CYS   A 1 67  ? -36.666 -42.514 20.588 1.00 21.28 ? 70   CYS   A SG   1 
ATOM   508  N  N    . THR   A 1 68  ? -37.628 -41.720 15.874 1.00 12.24 ? 71   THR   A N    1 
ATOM   509  C  CA   . THR   A 1 68  ? -37.579 -41.256 14.488 1.00 16.93 ? 71   THR   A CA   1 
ATOM   510  C  C    . THR   A 1 68  ? -36.241 -40.590 14.188 1.00 12.54 ? 71   THR   A C    1 
ATOM   511  O  O    . THR   A 1 68  ? -35.745 -39.775 14.971 1.00 15.17 ? 71   THR   A O    1 
ATOM   512  C  CB   . THR   A 1 68  ? -38.727 -40.284 14.200 1.00 15.72 ? 71   THR   A CB   1 
ATOM   513  O  OG1  . THR   A 1 68  ? -39.912 -40.733 14.861 1.00 16.73 ? 71   THR   A OG1  1 
ATOM   514  C  CG2  . THR   A 1 68  ? -38.998 -40.233 12.698 1.00 14.54 ? 71   THR   A CG2  1 
ATOM   515  N  N    . GLN   A 1 69  ? -35.658 -40.952 13.047 1.00 14.27 ? 72   GLN   A N    1 
ATOM   516  C  CA   . GLN   A 1 69  ? -34.308 -40.525 12.696 1.00 14.22 ? 72   GLN   A CA   1 
ATOM   517  C  C    . GLN   A 1 69  ? -34.091 -40.884 11.232 1.00 13.93 ? 72   GLN   A C    1 
ATOM   518  O  O    . GLN   A 1 69  ? -34.871 -41.631 10.633 1.00 15.35 ? 72   GLN   A O    1 
ATOM   519  C  CB   . GLN   A 1 69  ? -33.247 -41.197 13.577 1.00 12.22 ? 72   GLN   A CB   1 
ATOM   520  C  CG   . GLN   A 1 69  ? -33.212 -42.730 13.390 1.00 13.26 ? 72   GLN   A CG   1 
ATOM   521  C  CD   . GLN   A 1 69  ? -32.369 -43.452 14.430 1.00 13.66 ? 72   GLN   A CD   1 
ATOM   522  O  OE1  . GLN   A 1 69  ? -31.241 -43.860 14.149 1.00 13.18 ? 72   GLN   A OE1  1 
ATOM   523  N  NE2  . GLN   A 1 69  ? -32.907 -43.610 15.633 1.00 11.47 ? 72   GLN   A NE2  1 
ATOM   524  N  N    . ASP   A 1 70  ? -33.043 -40.324 10.664 1.00 15.65 ? 73   ASP   A N    1 
ATOM   525  C  CA   . ASP   A 1 70  ? -32.574 -40.663 9.328  1.00 16.81 ? 73   ASP   A CA   1 
ATOM   526  C  C    . ASP   A 1 70  ? -32.361 -42.175 9.304  1.00 16.33 ? 73   ASP   A C    1 
ATOM   527  O  O    . ASP   A 1 70  ? -31.423 -42.666 9.941  1.00 19.18 ? 73   ASP   A O    1 
ATOM   528  C  CB   . ASP   A 1 70  ? -31.280 -39.896 9.029  1.00 19.60 ? 73   ASP   A CB   1 
ATOM   529  C  CG   . ASP   A 1 70  ? -30.668 -40.242 7.679  1.00 22.98 ? 73   ASP   A CG   1 
ATOM   530  O  OD1  . ASP   A 1 70  ? -31.080 -41.232 7.036  1.00 26.34 ? 73   ASP   A OD1  1 
ATOM   531  O  OD2  . ASP   A 1 70  ? -29.752 -39.500 7.270  1.00 28.60 ? 73   ASP   A OD2  1 
ATOM   532  N  N    . PRO   A 1 71  ? -33.200 -42.938 8.591  1.00 18.72 ? 74   PRO   A N    1 
ATOM   533  C  CA   . PRO   A 1 71  ? -33.111 -44.409 8.689  1.00 21.62 ? 74   PRO   A CA   1 
ATOM   534  C  C    . PRO   A 1 71  ? -31.843 -44.974 8.088  1.00 22.74 ? 74   PRO   A C    1 
ATOM   535  O  O    . PRO   A 1 71  ? -31.367 -46.031 8.535  1.00 20.30 ? 74   PRO   A O    1 
ATOM   536  C  CB   . PRO   A 1 71  ? -34.353 -44.901 7.932  1.00 23.03 ? 74   PRO   A CB   1 
ATOM   537  C  CG   . PRO   A 1 71  ? -34.744 -43.757 7.026  1.00 25.00 ? 74   PRO   A CG   1 
ATOM   538  C  CD   . PRO   A 1 71  ? -34.247 -42.482 7.652  1.00 20.45 ? 74   PRO   A CD   1 
ATOM   539  N  N    . LYS   A 1 72  ? -31.274 -44.300 7.092  1.00 21.07 ? 75   LYS   A N    1 
ATOM   540  C  CA   . LYS   A 1 72  ? -30.045 -44.796 6.486  1.00 24.59 ? 75   LYS   A CA   1 
ATOM   541  C  C    . LYS   A 1 72  ? -28.864 -44.616 7.426  1.00 22.00 ? 75   LYS   A C    1 
ATOM   542  O  O    . LYS   A 1 72  ? -28.106 -45.563 7.669  1.00 20.00 ? 75   LYS   A O    1 
ATOM   543  C  CB   . LYS   A 1 72  ? -29.794 -44.093 5.150  1.00 27.48 ? 75   LYS   A CB   1 
ATOM   544  C  CG   . LYS   A 1 72  ? -30.745 -44.504 4.003  1.00 32.85 ? 75   LYS   A CG   1 
ATOM   545  C  CD   . LYS   A 1 72  ? -31.048 -46.026 3.895  1.00 43.46 ? 75   LYS   A CD   1 
ATOM   546  C  CE   . LYS   A 1 72  ? -29.806 -46.932 4.038  1.00 43.49 ? 75   LYS   A CE   1 
ATOM   547  N  NZ   . LYS   A 1 72  ? -30.150 -48.358 4.343  1.00 45.34 ? 75   LYS   A NZ   1 
ATOM   548  N  N    . ALA   A 1 73  ? -28.687 -43.403 7.960  1.00 18.30 ? 76   ALA   A N    1 
ATOM   549  C  CA   . ALA   A 1 73  ? -27.609 -43.170 8.916  1.00 22.04 ? 76   ALA   A CA   1 
ATOM   550  C  C    . ALA   A 1 73  ? -27.831 -43.971 10.196 1.00 18.28 ? 76   ALA   A C    1 
ATOM   551  O  O    . ALA   A 1 73  ? -26.879 -44.497 10.783 1.00 19.55 ? 76   ALA   A O    1 
ATOM   552  C  CB   . ALA   A 1 73  ? -27.495 -41.671 9.214  1.00 21.78 ? 76   ALA   A CB   1 
ATOM   553  N  N    . GLY   A 1 74  ? -29.086 -44.105 10.628 1.00 17.58 ? 77   GLY   A N    1 
ATOM   554  C  CA   . GLY   A 1 74  ? -29.357 -44.914 11.809 1.00 14.31 ? 77   GLY   A CA   1 
ATOM   555  C  C    . GLY   A 1 74  ? -29.000 -46.379 11.613 1.00 20.10 ? 77   GLY   A C    1 
ATOM   556  O  O    . GLY   A 1 74  ? -28.356 -46.994 12.474 1.00 22.38 ? 77   GLY   A O    1 
ATOM   557  N  N    . GLN   A 1 75  ? -29.391 -46.954 10.470 1.00 17.18 ? 78   GLN   A N    1 
ATOM   558  C  CA   . GLN   A 1 75  ? -29.044 -48.350 10.210 1.00 20.46 ? 78   GLN   A CA   1 
ATOM   559  C  C    . GLN   A 1 75  ? -27.540 -48.529 10.056 1.00 21.74 ? 78   GLN   A C    1 
ATOM   560  O  O    . GLN   A 1 75  ? -26.973 -49.521 10.537 1.00 21.15 ? 78   GLN   A O    1 
ATOM   561  C  CB   . GLN   A 1 75  ? -29.758 -48.863 8.961  1.00 26.25 ? 78   GLN   A CB   1 
ATOM   562  C  CG   . GLN   A 1 75  ? -29.246 -50.249 8.544  1.00 33.05 ? 78   GLN   A CG   1 
ATOM   563  C  CD   . GLN   A 1 75  ? -30.110 -50.926 7.502  1.00 42.57 ? 78   GLN   A CD   1 
ATOM   564  O  OE1  . GLN   A 1 75  ? -29.827 -50.851 6.303  1.00 45.50 ? 78   GLN   A OE1  1 
ATOM   565  N  NE2  . GLN   A 1 75  ? -31.164 -51.608 7.955  1.00 40.86 ? 78   GLN   A NE2  1 
ATOM   566  N  N    . LEU   A 1 76  ? -26.878 -47.584 9.382  1.00 18.36 ? 79   LEU   A N    1 
ATOM   567  C  CA   . LEU   A 1 76  ? -25.428 -47.647 9.236  1.00 18.65 ? 79   LEU   A CA   1 
ATOM   568  C  C    . LEU   A 1 76  ? -24.730 -47.640 10.594 1.00 20.15 ? 79   LEU   A C    1 
ATOM   569  O  O    . LEU   A 1 76  ? -23.853 -48.477 10.858 1.00 20.40 ? 79   LEU   A O    1 
ATOM   570  C  CB   . LEU   A 1 76  ? -24.932 -46.482 8.373  1.00 19.39 ? 79   LEU   A CB   1 
ATOM   571  C  CG   . LEU   A 1 76  ? -23.410 -46.325 8.275  1.00 25.18 ? 79   LEU   A CG   1 
ATOM   572  C  CD1  . LEU   A 1 76  ? -22.762 -47.581 7.665  1.00 27.35 ? 79   LEU   A CD1  1 
ATOM   573  C  CD2  . LEU   A 1 76  ? -23.033 -45.086 7.478  1.00 27.34 ? 79   LEU   A CD2  1 
ATOM   574  N  N    . LEU   A 1 77  ? -25.084 -46.688 11.465 1.00 18.19 ? 80   LEU   A N    1 
ATOM   575  C  CA   . LEU   A 1 77  ? -24.457 -46.654 12.783 1.00 18.54 ? 80   LEU   A CA   1 
ATOM   576  C  C    . LEU   A 1 77  ? -24.738 -47.932 13.563 1.00 19.06 ? 80   LEU   A C    1 
ATOM   577  O  O    . LEU   A 1 77  ? -23.842 -48.460 14.237 1.00 17.97 ? 80   LEU   A O    1 
ATOM   578  C  CB   . LEU   A 1 77  ? -24.917 -45.434 13.580 1.00 18.75 ? 80   LEU   A CB   1 
ATOM   579  C  CG   . LEU   A 1 77  ? -24.098 -45.260 14.861 1.00 19.47 ? 80   LEU   A CG   1 
ATOM   580  C  CD1  . LEU   A 1 77  ? -22.633 -44.936 14.528 1.00 22.18 ? 80   LEU   A CD1  1 
ATOM   581  C  CD2  . LEU   A 1 77  ? -24.698 -44.157 15.722 1.00 20.67 ? 80   LEU   A CD2  1 
ATOM   582  N  N    . SER   A 1 78  ? -25.971 -48.447 13.494 1.00 16.93 ? 81   SER   A N    1 
ATOM   583  C  CA   . SER   A 1 78  ? -26.257 -49.714 14.159 1.00 19.71 ? 81   SER   A CA   1 
ATOM   584  C  C    . SER   A 1 78  ? -25.339 -50.824 13.665 1.00 18.00 ? 81   SER   A C    1 
ATOM   585  O  O    . SER   A 1 78  ? -24.771 -51.567 14.469 1.00 17.63 ? 81   SER   A O    1 
ATOM   586  C  CB   . SER   A 1 78  ? -27.716 -50.120 13.963 1.00 19.42 ? 81   SER   A CB   1 
ATOM   587  O  OG   . SER   A 1 78  ? -28.048 -51.105 14.926 1.00 20.38 ? 81   SER   A OG   1 
ATOM   588  N  N    . GLU   A 1 79  ? -25.174 -50.941 12.344 1.00 18.68 ? 82   GLU   A N    1 
ATOM   589  C  CA   . GLU   A 1 79  ? -24.287 -51.963 11.782 1.00 21.98 ? 82   GLU   A CA   1 
ATOM   590  C  C    . GLU   A 1 79  ? -22.843 -51.768 12.228 1.00 22.06 ? 82   GLU   A C    1 
ATOM   591  O  O    . GLU   A 1 79  ? -22.139 -52.747 12.504 1.00 19.02 ? 82   GLU   A O    1 
ATOM   592  C  CB   . GLU   A 1 79  ? -24.383 -51.945 10.258 1.00 22.18 ? 82   GLU   A CB   1 
ATOM   593  C  CG   . GLU   A 1 79  ? -25.769 -52.347 9.754  1.00 24.81 ? 82   GLU   A CG   1 
ATOM   594  C  CD   . GLU   A 1 79  ? -25.914 -52.201 8.252  1.00 35.09 ? 82   GLU   A CD   1 
ATOM   595  O  OE1  . GLU   A 1 79  ? -25.071 -51.509 7.632  1.00 37.24 ? 82   GLU   A OE1  1 
ATOM   596  O  OE2  . GLU   A 1 79  ? -26.901 -52.730 7.695  1.00 38.32 ? 82   GLU   A OE2  1 
ATOM   597  N  N    . LEU   A 1 80  ? -22.378 -50.513 12.307 1.00 18.10 ? 83   LEU   A N    1 
ATOM   598  C  CA   . LEU   A 1 80  ? -20.989 -50.273 12.684 1.00 19.83 ? 83   LEU   A CA   1 
ATOM   599  C  C    . LEU   A 1 80  ? -20.734 -50.541 14.163 1.00 21.46 ? 83   LEU   A C    1 
ATOM   600  O  O    . LEU   A 1 80  ? -19.610 -50.892 14.534 1.00 21.12 ? 83   LEU   A O    1 
ATOM   601  C  CB   . LEU   A 1 80  ? -20.570 -48.834 12.350 1.00 20.34 ? 83   LEU   A CB   1 
ATOM   602  C  CG   . LEU   A 1 80  ? -20.484 -48.468 10.867 1.00 20.44 ? 83   LEU   A CG   1 
ATOM   603  C  CD1  . LEU   A 1 80  ? -20.408 -46.965 10.702 1.00 21.98 ? 83   LEU   A CD1  1 
ATOM   604  C  CD2  . LEU   A 1 80  ? -19.282 -49.177 10.227 1.00 24.67 ? 83   LEU   A CD2  1 
ATOM   605  N  N    . PHE   A 1 81  ? -21.739 -50.358 15.022 1.00 16.40 ? 84   PHE   A N    1 
ATOM   606  C  CA   . PHE   A 1 81  ? -21.545 -50.414 16.467 1.00 14.23 ? 84   PHE   A CA   1 
ATOM   607  C  C    . PHE   A 1 81  ? -22.086 -51.677 17.131 1.00 17.70 ? 84   PHE   A C    1 
ATOM   608  O  O    . PHE   A 1 81  ? -21.766 -51.908 18.303 1.00 16.73 ? 84   PHE   A O    1 
ATOM   609  C  CB   . PHE   A 1 81  ? -22.206 -49.203 17.149 1.00 15.72 ? 84   PHE   A CB   1 
ATOM   610  C  CG   . PHE   A 1 81  ? -21.375 -47.934 17.129 1.00 17.92 ? 84   PHE   A CG   1 
ATOM   611  C  CD1  . PHE   A 1 81  ? -20.100 -47.919 16.585 1.00 21.48 ? 84   PHE   A CD1  1 
ATOM   612  C  CD2  . PHE   A 1 81  ? -21.876 -46.767 17.676 1.00 19.26 ? 84   PHE   A CD2  1 
ATOM   613  C  CE1  . PHE   A 1 81  ? -19.340 -46.745 16.585 1.00 23.05 ? 84   PHE   A CE1  1 
ATOM   614  C  CE2  . PHE   A 1 81  ? -21.125 -45.594 17.688 1.00 24.38 ? 84   PHE   A CE2  1 
ATOM   615  C  CZ   . PHE   A 1 81  ? -19.857 -45.584 17.140 1.00 22.44 ? 84   PHE   A CZ   1 
ATOM   616  N  N    . THR   A 1 82  ? -22.915 -52.474 16.456 1.00 17.55 ? 85   THR   A N    1 
ATOM   617  C  CA   . THR   A 1 82  ? -23.555 -53.585 17.149 1.00 17.82 ? 85   THR   A CA   1 
ATOM   618  C  C    . THR   A 1 82  ? -22.535 -54.655 17.527 1.00 21.65 ? 85   THR   A C    1 
ATOM   619  O  O    . THR   A 1 82  ? -21.550 -54.879 16.818 1.00 17.57 ? 85   THR   A O    1 
ATOM   620  C  CB   . THR   A 1 82  ? -24.675 -54.203 16.310 1.00 21.18 ? 85   THR   A CB   1 
ATOM   621  O  OG1  . THR   A 1 82  ? -25.419 -55.106 17.132 1.00 19.25 ? 85   THR   A OG1  1 
ATOM   622  C  CG2  . THR   A 1 82  ? -24.142 -54.948 15.091 1.00 21.42 ? 85   THR   A CG2  1 
ATOM   623  N  N    . ASN   A 1 83  ? -22.783 -55.318 18.651 1.00 18.29 ? 86   ASN   A N    1 
ATOM   624  C  CA   . ASN   A 1 83  ? -21.928 -56.387 19.106 1.00 20.26 ? 86   ASN   A CA   1 
ATOM   625  C  C    . ASN   A 1 83  ? -22.484 -57.748 18.744 1.00 22.66 ? 86   ASN   A C    1 
ATOM   626  O  O    . ASN   A 1 83  ? -21.880 -58.746 19.074 1.00 21.03 ? 86   ASN   A O    1 
ATOM   627  C  CB   . ASN   A 1 83  ? -21.746 -56.304 20.616 1.00 16.70 ? 86   ASN   A CB   1 
ATOM   628  C  CG   . ASN   A 1 83  ? -23.051 -56.372 21.388 1.00 18.65 ? 86   ASN   A CG   1 
ATOM   629  O  OD1  . ASN   A 1 83  ? -24.072 -55.858 20.962 1.00 16.15 ? 86   ASN   A OD1  1 
ATOM   630  N  ND2  . ASN   A 1 83  ? -22.996 -56.984 22.565 1.00 15.46 ? 86   ASN   A ND2  1 
ATOM   631  N  N    . ARG   A 1 84  ? -23.671 -57.773 18.194 1.00 19.36 ? 87   ARG   A N    1 
ATOM   632  C  CA   . ARG   A 1 84  ? -24.306 -58.983 17.723 1.00 25.37 ? 87   ARG   A CA   1 
ATOM   633  C  C    . ARG   A 1 84  ? -23.735 -59.522 16.407 1.00 28.95 ? 87   ARG   A C    1 
ATOM   634  O  O    . ARG   A 1 84  ? -23.203 -58.774 15.622 1.00 24.33 ? 87   ARG   A O    1 
ATOM   635  C  CB   . ARG   A 1 84  ? -25.804 -58.740 17.503 1.00 25.61 ? 87   ARG   A CB   1 
ATOM   636  C  CG   . ARG   A 1 84  ? -26.472 -57.823 18.479 1.00 29.70 ? 87   ARG   A CG   1 
ATOM   637  C  CD   . ARG   A 1 84  ? -27.844 -57.431 17.961 1.00 35.55 ? 87   ARG   A CD   1 
ATOM   638  N  NE   . ARG   A 1 84  ? -28.568 -56.674 18.964 1.00 26.72 ? 87   ARG   A NE   1 
ATOM   639  C  CZ   . ARG   A 1 84  ? -29.247 -57.257 19.935 1.00 26.87 ? 87   ARG   A CZ   1 
ATOM   640  N  NH1  . ARG   A 1 84  ? -29.302 -58.579 19.985 1.00 28.88 ? 87   ARG   A NH1  1 
ATOM   641  N  NH2  . ARG   A 1 84  ? -29.876 -56.540 20.839 1.00 21.73 ? 87   ARG   A NH2  1 
ATOM   642  N  N    . LYS   A 1 85  ? -23.906 -60.817 16.161 1.00 27.94 ? 88   LYS   A N    1 
ATOM   643  C  CA   . LYS   A 1 85  ? -23.469 -61.387 14.879 1.00 33.61 ? 88   LYS   A CA   1 
ATOM   644  C  C    . LYS   A 1 85  ? -24.166 -60.779 13.676 1.00 34.13 ? 88   LYS   A C    1 
ATOM   645  O  O    . LYS   A 1 85  ? -23.535 -60.515 12.681 1.00 38.47 ? 88   LYS   A O    1 
ATOM   646  C  CB   . LYS   A 1 85  ? -23.633 -62.906 14.871 1.00 34.82 ? 88   LYS   A CB   1 
ATOM   647  C  CG   . LYS   A 1 85  ? -23.158 -63.595 13.609 1.00 45.10 ? 88   LYS   A CG   1 
ATOM   648  C  CD   . LYS   A 1 85  ? -23.547 -65.060 13.645 1.00 55.57 ? 88   LYS   A CD   1 
ATOM   649  C  CE   . LYS   A 1 85  ? -23.366 -65.732 12.296 1.00 62.65 ? 88   LYS   A CE   1 
ATOM   650  N  NZ   . LYS   A 1 85  ? -24.236 -66.933 12.178 1.00 61.14 ? 88   LYS   A NZ   1 
ATOM   651  N  N    . GLU   A 1 86  ? -25.463 -60.573 13.756 1.00 32.25 ? 89   GLU   A N    1 
ATOM   652  C  CA   . GLU   A 1 86  ? -26.159 -59.897 12.668 1.00 37.39 ? 89   GLU   A CA   1 
ATOM   653  C  C    . GLU   A 1 86  ? -26.906 -58.678 13.194 1.00 31.90 ? 89   GLU   A C    1 
ATOM   654  O  O    . GLU   A 1 86  ? -27.563 -58.744 14.237 1.00 26.94 ? 89   GLU   A O    1 
ATOM   655  C  CB   . GLU   A 1 86  ? -27.157 -60.823 11.960 1.00 42.63 ? 89   GLU   A CB   1 
ATOM   656  C  CG   . GLU   A 1 86  ? -26.521 -61.923 11.117 1.00 52.77 ? 89   GLU   A CG   1 
ATOM   657  C  CD   . GLU   A 1 86  ? -26.579 -63.291 11.784 1.00 63.69 ? 89   GLU   A CD   1 
ATOM   658  O  OE1  . GLU   A 1 86  ? -27.093 -63.388 12.923 1.00 65.61 ? 89   GLU   A OE1  1 
ATOM   659  O  OE2  . GLU   A 1 86  ? -26.120 -64.274 11.161 1.00 70.21 ? 89   GLU   A OE2  1 
ATOM   660  N  N    . ASN   A 1 87  ? -26.813 -57.569 12.461 1.00 31.18 ? 90   ASN   A N    1 
ATOM   661  C  CA   . ASN   A 1 87  ? -27.542 -56.367 12.848 1.00 29.16 ? 90   ASN   A CA   1 
ATOM   662  C  C    . ASN   A 1 87  ? -29.038 -56.619 12.690 1.00 31.21 ? 90   ASN   A C    1 
ATOM   663  O  O    . ASN   A 1 87  ? -29.476 -57.259 11.731 1.00 31.83 ? 90   ASN   A O    1 
ATOM   664  C  CB   . ASN   A 1 87  ? -27.125 -55.171 11.989 1.00 28.77 ? 90   ASN   A CB   1 
ATOM   665  C  CG   . ASN   A 1 87  ? -27.709 -53.858 12.497 1.00 31.79 ? 90   ASN   A CG   1 
ATOM   666  O  OD1  . ASN   A 1 87  ? -27.583 -53.532 13.681 1.00 26.90 ? 90   ASN   A OD1  1 
ATOM   667  N  ND2  . ASN   A 1 87  ? -28.417 -53.136 11.621 1.00 28.23 ? 90   ASN   A ND2  1 
ATOM   668  N  N    . ILE   A 1 88  ? -29.820 -56.125 13.641 1.00 30.05 ? 91   ILE   A N    1 
ATOM   669  C  CA   . ILE   A 1 88  ? -31.273 -56.283 13.630 1.00 29.74 ? 91   ILE   A CA   1 
ATOM   670  C  C    . ILE   A 1 88  ? -31.888 -55.033 13.009 1.00 29.86 ? 91   ILE   A C    1 
ATOM   671  O  O    . ILE   A 1 88  ? -31.650 -53.924 13.514 1.00 29.84 ? 91   ILE   A O    1 
ATOM   672  C  CB   . ILE   A 1 88  ? -31.821 -56.532 15.040 1.00 29.05 ? 91   ILE   A CB   1 
ATOM   673  C  CG1  . ILE   A 1 88  ? -31.185 -57.810 15.605 1.00 31.25 ? 91   ILE   A CG1  1 
ATOM   674  C  CG2  . ILE   A 1 88  ? -33.361 -56.594 15.023 1.00 29.98 ? 91   ILE   A CG2  1 
ATOM   675  C  CD1  . ILE   A 1 88  ? -31.487 -58.052 17.051 1.00 32.08 ? 91   ILE   A CD1  1 
ATOM   676  N  N    . PRO   A 1 89  ? -32.647 -55.154 11.923 1.00 34.11 ? 92   PRO   A N    1 
ATOM   677  C  CA   . PRO   A 1 89  ? -33.354 -53.986 11.388 1.00 34.08 ? 92   PRO   A CA   1 
ATOM   678  C  C    . PRO   A 1 89  ? -34.433 -53.532 12.358 1.00 29.51 ? 92   PRO   A C    1 
ATOM   679  O  O    . PRO   A 1 89  ? -35.107 -54.346 12.991 1.00 25.75 ? 92   PRO   A O    1 
ATOM   680  C  CB   . PRO   A 1 89  ? -33.955 -54.510 10.083 1.00 34.31 ? 92   PRO   A CB   1 
ATOM   681  C  CG   . PRO   A 1 89  ? -34.209 -55.963 10.384 1.00 35.31 ? 92   PRO   A CG   1 
ATOM   682  C  CD   . PRO   A 1 89  ? -33.033 -56.397 11.228 1.00 34.09 ? 92   PRO   A CD   1 
ATOM   683  N  N    . LEU   A 1 90  ? -34.585 -52.221 12.492 1.00 27.80 ? 93   LEU   A N    1 
ATOM   684  C  CA   . LEU   A 1 90  ? -35.552 -51.684 13.434 1.00 27.43 ? 93   LEU   A CA   1 
ATOM   685  C  C    . LEU   A 1 90  ? -36.527 -50.758 12.720 1.00 24.53 ? 93   LEU   A C    1 
ATOM   686  O  O    . LEU   A 1 90  ? -36.181 -50.116 11.724 1.00 27.68 ? 93   LEU   A O    1 
ATOM   687  C  CB   . LEU   A 1 90  ? -34.855 -50.946 14.587 1.00 25.31 ? 93   LEU   A CB   1 
ATOM   688  C  CG   . LEU   A 1 90  ? -33.887 -51.773 15.444 1.00 29.38 ? 93   LEU   A CG   1 
ATOM   689  C  CD1  . LEU   A 1 90  ? -32.968 -50.848 16.254 1.00 23.90 ? 93   LEU   A CD1  1 
ATOM   690  C  CD2  . LEU   A 1 90  ? -34.634 -52.740 16.368 1.00 22.76 ? 93   LEU   A CD2  1 
ATOM   691  N  N    . LYS   A 1 91  ? -37.757 -50.723 13.230 1.00 22.24 ? 94   LYS   A N    1 
ATOM   692  C  CA   . LYS   A 1 91  ? -38.756 -49.761 12.782 1.00 23.27 ? 94   LYS   A CA   1 
ATOM   693  C  C    . LYS   A 1 91  ? -38.485 -48.394 13.399 1.00 20.98 ? 94   LYS   A C    1 
ATOM   694  O  O    . LYS   A 1 91  ? -37.904 -48.294 14.485 1.00 19.86 ? 94   LYS   A O    1 
ATOM   695  C  CB   . LYS   A 1 91  ? -40.162 -50.206 13.199 1.00 25.60 ? 94   LYS   A CB   1 
ATOM   696  C  CG   . LYS   A 1 91  ? -40.678 -51.510 12.584 1.00 33.64 ? 94   LYS   A CG   1 
ATOM   697  C  CD   . LYS   A 1 91  ? -40.516 -51.531 11.074 1.00 40.31 ? 94   LYS   A CD   1 
ATOM   698  C  CE   . LYS   A 1 91  ? -41.593 -52.410 10.438 1.00 48.11 ? 94   LYS   A CE   1 
ATOM   699  N  NZ   . LYS   A 1 91  ? -41.421 -53.844 10.799 1.00 46.55 ? 94   LYS   A NZ   1 
ATOM   700  N  N    . LEU   A 1 92  ? -38.928 -47.341 12.704 1.00 20.77 ? 95   LEU   A N    1 
ATOM   701  C  CA   . LEU   A 1 92  ? -38.927 -45.975 13.228 1.00 19.50 ? 95   LEU   A CA   1 
ATOM   702  C  C    . LEU   A 1 92  ? -40.280 -45.673 13.860 1.00 19.48 ? 95   LEU   A C    1 
ATOM   703  O  O    . LEU   A 1 92  ? -41.320 -46.061 13.321 1.00 16.80 ? 95   LEU   A O    1 
ATOM   704  C  CB   . LEU   A 1 92  ? -38.704 -44.946 12.119 1.00 20.23 ? 95   LEU   A CB   1 
ATOM   705  C  CG   . LEU   A 1 92  ? -37.456 -44.864 11.250 1.00 24.57 ? 95   LEU   A CG   1 
ATOM   706  C  CD1  . LEU   A 1 92  ? -37.565 -43.621 10.351 1.00 26.09 ? 95   LEU   A CD1  1 
ATOM   707  C  CD2  . LEU   A 1 92  ? -36.229 -44.824 12.096 1.00 22.34 ? 95   LEU   A CD2  1 
ATOM   708  N  N    . SER   A 1 93  ? -40.272 -44.937 14.972 1.00 18.82 ? 96   SER   A N    1 
ATOM   709  C  CA   . SER   A 1 93  ? -41.529 -44.408 15.491 1.00 15.90 ? 96   SER   A CA   1 
ATOM   710  C  C    . SER   A 1 93  ? -41.259 -43.282 16.479 1.00 16.79 ? 96   SER   A C    1 
ATOM   711  O  O    . SER   A 1 93  ? -40.237 -43.275 17.171 1.00 13.01 ? 96   SER   A O    1 
ATOM   712  C  CB   . SER   A 1 93  ? -42.357 -45.508 16.166 1.00 18.65 ? 96   SER   A CB   1 
ATOM   713  O  OG   . SER   A 1 93  ? -43.608 -44.997 16.591 1.00 16.98 ? 96   SER   A OG   1 
ATOM   714  N  N    . GLU   A 1 94  ? -42.204 -42.336 16.561 1.00 13.57 ? 97   GLU   A N    1 
ATOM   715  C  CA   . GLU   A 1 94  ? -42.196 -41.413 17.694 1.00 13.49 ? 97   GLU   A CA   1 
ATOM   716  C  C    . GLU   A 1 94  ? -42.510 -42.123 19.004 1.00 14.17 ? 97   GLU   A C    1 
ATOM   717  O  O    . GLU   A 1 94  ? -42.186 -41.606 20.079 1.00 14.28 ? 97   GLU   A O    1 
ATOM   718  C  CB   . GLU   A 1 94  ? -43.219 -40.292 17.476 1.00 18.16 ? 97   GLU   A CB   1 
ATOM   719  C  CG   . GLU   A 1 94  ? -43.014 -39.550 16.175 1.00 19.66 ? 97   GLU   A CG   1 
ATOM   720  C  CD   . GLU   A 1 94  ? -44.099 -38.520 15.933 1.00 24.36 ? 97   GLU   A CD   1 
ATOM   721  O  OE1  . GLU   A 1 94  ? -45.289 -38.877 16.082 1.00 25.54 ? 97   GLU   A OE1  1 
ATOM   722  O  OE2  . GLU   A 1 94  ? -43.768 -37.384 15.544 1.00 20.02 ? 97   GLU   A OE2  1 
ATOM   723  N  N    . ASP   A 1 95  ? -43.158 -43.281 18.935 1.00 14.51 ? 98   ASP   A N    1 
ATOM   724  C  CA   . ASP   A 1 95  ? -43.437 -44.122 20.098 1.00 14.80 ? 98   ASP   A CA   1 
ATOM   725  C  C    . ASP   A 1 95  ? -42.191 -44.969 20.349 1.00 13.59 ? 98   ASP   A C    1 
ATOM   726  O  O    . ASP   A 1 95  ? -42.079 -46.114 19.899 1.00 14.33 ? 98   ASP   A O    1 
ATOM   727  C  CB   . ASP   A 1 95  ? -44.659 -44.995 19.824 1.00 14.58 ? 98   ASP   A CB   1 
ATOM   728  C  CG   . ASP   A 1 95  ? -45.014 -45.912 20.983 1.00 18.34 ? 98   ASP   A CG   1 
ATOM   729  O  OD1  . ASP   A 1 95  ? -44.440 -45.767 22.085 1.00 15.72 ? 98   ASP   A OD1  1 
ATOM   730  O  OD2  . ASP   A 1 95  ? -45.889 -46.792 20.794 1.00 18.54 ? 98   ASP   A OD2  1 
ATOM   731  N  N    . CYS   A 1 96  ? -41.227 -44.394 21.089 1.00 14.37 ? 99   CYS   A N    1 
ATOM   732  C  CA   . CYS   A 1 96  ? -39.940 -45.064 21.229 1.00 14.08 ? 99   CYS   A CA   1 
ATOM   733  C  C    . CYS   A 1 96  ? -39.348 -45.014 22.634 1.00 11.39 ? 99   CYS   A C    1 
ATOM   734  O  O    . CYS   A 1 96  ? -38.172 -45.384 22.802 1.00 13.72 ? 99   CYS   A O    1 
ATOM   735  C  CB   . CYS   A 1 96  ? -38.945 -44.450 20.257 1.00 12.24 ? 99   CYS   A CB   1 
ATOM   736  S  SG   . CYS   A 1 96  ? -38.685 -42.683 20.622 1.00 18.62 ? 99   CYS   A SG   1 
ATOM   737  N  N    . LEU   A 1 97  ? -40.097 -44.564 23.643 1.00 12.29 ? 100  LEU   A N    1 
ATOM   738  C  CA   . LEU   A 1 97  ? -39.533 -44.424 24.988 1.00 10.74 ? 100  LEU   A CA   1 
ATOM   739  C  C    . LEU   A 1 97  ? -39.613 -45.781 25.668 1.00 14.08 ? 100  LEU   A C    1 
ATOM   740  O  O    . LEU   A 1 97  ? -40.500 -46.071 26.477 1.00 13.80 ? 100  LEU   A O    1 
ATOM   741  C  CB   . LEU   A 1 97  ? -40.234 -43.330 25.775 1.00 11.20 ? 100  LEU   A CB   1 
ATOM   742  C  CG   . LEU   A 1 97  ? -40.020 -41.945 25.140 1.00 12.00 ? 100  LEU   A CG   1 
ATOM   743  C  CD1  . LEU   A 1 97  ? -40.669 -40.814 25.958 1.00 10.78 ? 100  LEU   A CD1  1 
ATOM   744  C  CD2  . LEU   A 1 97  ? -38.517 -41.665 24.934 1.00 12.79 ? 100  LEU   A CD2  1 
ATOM   745  N  N    . TYR   A 1 98  ? -38.637 -46.631 25.325 1.00 10.55 ? 101  TYR   A N    1 
ATOM   746  C  CA   . TYR   A 1 98  ? -38.592 -47.998 25.805 1.00 12.41 ? 101  TYR   A CA   1 
ATOM   747  C  C    . TYR   A 1 98  ? -37.199 -48.280 26.339 1.00 11.62 ? 101  TYR   A C    1 
ATOM   748  O  O    . TYR   A 1 98  ? -36.234 -47.573 26.025 1.00 12.37 ? 101  TYR   A O    1 
ATOM   749  C  CB   . TYR   A 1 98  ? -38.952 -48.992 24.676 1.00 13.76 ? 101  TYR   A CB   1 
ATOM   750  C  CG   . TYR   A 1 98  ? -40.381 -48.831 24.224 1.00 13.51 ? 101  TYR   A CG   1 
ATOM   751  C  CD1  . TYR   A 1 98  ? -41.419 -49.395 24.952 1.00 14.47 ? 101  TYR   A CD1  1 
ATOM   752  C  CD2  . TYR   A 1 98  ? -40.696 -48.078 23.097 1.00 13.99 ? 101  TYR   A CD2  1 
ATOM   753  C  CE1  . TYR   A 1 98  ? -42.742 -49.228 24.570 1.00 16.89 ? 101  TYR   A CE1  1 
ATOM   754  C  CE2  . TYR   A 1 98  ? -42.028 -47.895 22.702 1.00 15.26 ? 101  TYR   A CE2  1 
ATOM   755  C  CZ   . TYR   A 1 98  ? -43.043 -48.474 23.442 1.00 18.39 ? 101  TYR   A CZ   1 
ATOM   756  O  OH   . TYR   A 1 98  ? -44.373 -48.304 23.074 1.00 19.93 ? 101  TYR   A OH   1 
ATOM   757  N  N    . LEU   A 1 99  ? -37.100 -49.315 27.165 1.00 11.69 ? 102  LEU   A N    1 
ATOM   758  C  CA   . LEU   A 1 99  ? -35.804 -49.831 27.569 1.00 10.28 ? 102  LEU   A CA   1 
ATOM   759  C  C    . LEU   A 1 99  ? -35.829 -51.351 27.505 1.00 13.48 ? 102  LEU   A C    1 
ATOM   760  O  O    . LEU   A 1 99  ? -36.891 -51.990 27.491 1.00 12.96 ? 102  LEU   A O    1 
ATOM   761  C  CB   . LEU   A 1 99  ? -35.401 -49.326 28.968 1.00 11.60 ? 102  LEU   A CB   1 
ATOM   762  C  CG   . LEU   A 1 99  ? -36.414 -49.493 30.107 1.00 12.89 ? 102  LEU   A CG   1 
ATOM   763  C  CD1  . LEU   A 1 99  ? -36.440 -50.934 30.635 1.00 12.90 ? 102  LEU   A CD1  1 
ATOM   764  C  CD2  . LEU   A 1 99  ? -36.114 -48.495 31.205 1.00 13.86 ? 102  LEU   A CD2  1 
ATOM   765  N  N    . ASN   A 1 100 ? -34.629 -51.908 27.425 1.00 10.95 ? 103  ASN   A N    1 
ATOM   766  C  CA   . ASN   A 1 100 ? -34.395 -53.341 27.328 1.00 12.75 ? 103  ASN   A CA   1 
ATOM   767  C  C    . ASN   A 1 100 ? -33.578 -53.774 28.540 1.00 13.03 ? 103  ASN   A C    1 
ATOM   768  O  O    . ASN   A 1 100 ? -32.657 -53.063 28.956 1.00 12.27 ? 103  ASN   A O    1 
ATOM   769  C  CB   . ASN   A 1 100 ? -33.604 -53.715 26.057 1.00 12.80 ? 103  ASN   A CB   1 
ATOM   770  C  CG   . ASN   A 1 100 ? -34.325 -53.395 24.760 1.00 14.06 ? 103  ASN   A CG   1 
ATOM   771  O  OD1  . ASN   A 1 100 ? -35.570 -53.398 24.658 1.00 14.23 ? 103  ASN   A OD1  1 
ATOM   772  N  ND2  . ASN   A 1 100 ? -33.530 -53.148 23.722 1.00 12.56 ? 103  ASN   A ND2  1 
ATOM   773  N  N    . ILE   A 1 101 ? -33.880 -54.954 29.090 1.00 11.38 ? 104  ILE   A N    1 
ATOM   774  C  CA   . ILE   A 1 101 ? -33.239 -55.418 30.319 1.00 12.22 ? 104  ILE   A CA   1 
ATOM   775  C  C    . ILE   A 1 101 ? -32.665 -56.813 30.112 1.00 12.78 ? 104  ILE   A C    1 
ATOM   776  O  O    . ILE   A 1 101 ? -33.366 -57.715 29.635 1.00 13.54 ? 104  ILE   A O    1 
ATOM   777  C  CB   . ILE   A 1 101 ? -34.214 -55.412 31.512 1.00 13.11 ? 104  ILE   A CB   1 
ATOM   778  C  CG1  . ILE   A 1 101 ? -34.809 -54.012 31.699 1.00 14.08 ? 104  ILE   A CG1  1 
ATOM   779  C  CG2  . ILE   A 1 101 ? -33.517 -55.900 32.784 1.00 13.99 ? 104  ILE   A CG2  1 
ATOM   780  C  CD1  . ILE   A 1 101 ? -35.546 -53.842 33.014 1.00 16.87 ? 104  ILE   A CD1  1 
ATOM   781  N  N    . TYR   A 1 102 ? -31.405 -56.989 30.503 1.00 10.71 ? 105  TYR   A N    1 
ATOM   782  C  CA   . TYR   A 1 102 ? -30.680 -58.264 30.444 1.00 13.47 ? 105  TYR   A CA   1 
ATOM   783  C  C    . TYR   A 1 102 ? -30.267 -58.565 31.879 1.00 13.22 ? 105  TYR   A C    1 
ATOM   784  O  O    . TYR   A 1 102 ? -29.331 -57.936 32.395 1.00 13.07 ? 105  TYR   A O    1 
ATOM   785  C  CB   . TYR   A 1 102 ? -29.446 -58.172 29.530 1.00 11.42 ? 105  TYR   A CB   1 
ATOM   786  C  CG   . TYR   A 1 102 ? -29.781 -57.718 28.135 1.00 12.24 ? 105  TYR   A CG   1 
ATOM   787  C  CD1  . TYR   A 1 102 ? -30.018 -56.364 27.866 1.00 12.17 ? 105  TYR   A CD1  1 
ATOM   788  C  CD2  . TYR   A 1 102 ? -29.925 -58.627 27.102 1.00 12.53 ? 105  TYR   A CD2  1 
ATOM   789  C  CE1  . TYR   A 1 102 ? -30.371 -55.943 26.594 1.00 13.03 ? 105  TYR   A CE1  1 
ATOM   790  C  CE2  . TYR   A 1 102 ? -30.265 -58.216 25.819 1.00 14.79 ? 105  TYR   A CE2  1 
ATOM   791  C  CZ   . TYR   A 1 102 ? -30.502 -56.867 25.581 1.00 15.53 ? 105  TYR   A CZ   1 
ATOM   792  O  OH   . TYR   A 1 102 ? -30.854 -56.447 24.316 1.00 16.71 ? 105  TYR   A OH   1 
ATOM   793  N  N    . THR   A 1 103 ? -30.956 -59.502 32.541 1.00 13.15 ? 106  THR   A N    1 
ATOM   794  C  CA   . THR   A 1 103 ? -30.590 -59.799 33.921 1.00 13.33 ? 106  THR   A CA   1 
ATOM   795  C  C    . THR   A 1 103 ? -30.104 -61.236 34.036 1.00 17.93 ? 106  THR   A C    1 
ATOM   796  O  O    . THR   A 1 103 ? -30.816 -62.171 33.619 1.00 15.00 ? 106  THR   A O    1 
ATOM   797  C  CB   . THR   A 1 103 ? -31.717 -59.528 34.913 1.00 15.11 ? 106  THR   A CB   1 
ATOM   798  O  OG1  . THR   A 1 103 ? -31.268 -59.918 36.224 1.00 15.20 ? 106  THR   A OG1  1 
ATOM   799  C  CG2  . THR   A 1 103 ? -33.028 -60.260 34.549 1.00 15.16 ? 106  THR   A CG2  1 
ATOM   800  N  N    . PRO   A 1 104 ? -28.898 -61.450 34.571 1.00 17.30 ? 107  PRO   A N    1 
ATOM   801  C  CA   . PRO   A 1 104 ? -28.390 -62.815 34.762 1.00 16.43 ? 107  PRO   A CA   1 
ATOM   802  C  C    . PRO   A 1 104 ? -28.872 -63.456 36.052 1.00 21.05 ? 107  PRO   A C    1 
ATOM   803  O  O    . PRO   A 1 104 ? -28.521 -64.612 36.318 1.00 24.17 ? 107  PRO   A O    1 
ATOM   804  C  CB   . PRO   A 1 104 ? -26.863 -62.604 34.777 1.00 14.98 ? 107  PRO   A CB   1 
ATOM   805  C  CG   . PRO   A 1 104 ? -26.707 -61.275 35.462 1.00 16.20 ? 107  PRO   A CG   1 
ATOM   806  C  CD   . PRO   A 1 104 ? -27.956 -60.436 35.080 1.00 13.84 ? 107  PRO   A CD   1 
ATOM   807  N  N    . ALA   A 1 105 ? -29.648 -62.729 36.853 1.00 22.14 ? 108  ALA   A N    1 
ATOM   808  C  CA   . ALA   A 1 105 ? -30.101 -63.239 38.137 1.00 26.29 ? 108  ALA   A CA   1 
ATOM   809  C  C    . ALA   A 1 105 ? -31.108 -64.363 37.942 1.00 22.51 ? 108  ALA   A C    1 
ATOM   810  O  O    . ALA   A 1 105 ? -31.874 -64.382 36.973 1.00 21.59 ? 108  ALA   A O    1 
ATOM   811  C  CB   . ALA   A 1 105 ? -30.729 -62.123 38.967 1.00 22.05 ? 108  ALA   A CB   1 
ATOM   812  N  N    . ASP   A 1 106 ? -31.073 -65.331 38.857 1.00 26.06 ? 109  ASP   A N    1 
ATOM   813  C  CA   . ASP   A 1 106 ? -32.107 -66.358 38.907 1.00 25.27 ? 109  ASP   A CA   1 
ATOM   814  C  C    . ASP   A 1 106 ? -33.304 -65.699 39.583 1.00 22.88 ? 109  ASP   A C    1 
ATOM   815  O  O    . ASP   A 1 106 ? -33.259 -65.363 40.772 1.00 21.97 ? 109  ASP   A O    1 
ATOM   816  C  CB   . ASP   A 1 106 ? -31.598 -67.601 39.640 1.00 30.26 ? 109  ASP   A CB   1 
ATOM   817  C  CG   . ASP   A 1 106 ? -32.680 -68.661 39.874 1.00 36.80 ? 109  ASP   A CG   1 
ATOM   818  O  OD1  . ASP   A 1 106 ? -33.832 -68.512 39.407 1.00 31.92 ? 109  ASP   A OD1  1 
ATOM   819  O  OD2  . ASP   A 1 106 ? -32.338 -69.702 40.478 1.00 39.75 ? 109  ASP   A OD2  1 
ATOM   820  N  N    . LEU   A 1 107 ? -34.340 -65.433 38.800 1.00 21.14 ? 110  LEU   A N    1 
ATOM   821  C  CA   . LEU   A 1 107 ? -35.429 -64.607 39.303 1.00 26.79 ? 110  LEU   A CA   1 
ATOM   822  C  C    . LEU   A 1 107 ? -36.318 -65.359 40.288 1.00 29.89 ? 110  LEU   A C    1 
ATOM   823  O  O    . LEU   A 1 107 ? -37.187 -64.739 40.909 1.00 25.50 ? 110  LEU   A O    1 
ATOM   824  C  CB   . LEU   A 1 107 ? -36.240 -64.084 38.119 1.00 22.79 ? 110  LEU   A CB   1 
ATOM   825  C  CG   . LEU   A 1 107 ? -35.450 -63.095 37.252 1.00 20.00 ? 110  LEU   A CG   1 
ATOM   826  C  CD1  . LEU   A 1 107 ? -36.269 -62.706 36.033 1.00 21.97 ? 110  LEU   A CD1  1 
ATOM   827  C  CD2  . LEU   A 1 107 ? -35.056 -61.853 38.041 1.00 19.99 ? 110  LEU   A CD2  1 
ATOM   828  N  N    . THR   A 1 108 ? -36.116 -66.673 40.452 1.00 29.46 ? 111  THR   A N    1 
ATOM   829  C  CA   . THR   A 1 108 ? -36.816 -67.409 41.499 1.00 32.19 ? 111  THR   A CA   1 
ATOM   830  C  C    . THR   A 1 108 ? -36.156 -67.246 42.856 1.00 33.64 ? 111  THR   A C    1 
ATOM   831  O  O    . THR   A 1 108 ? -36.676 -67.770 43.843 1.00 34.74 ? 111  THR   A O    1 
ATOM   832  C  CB   . THR   A 1 108 ? -36.922 -68.898 41.150 1.00 27.69 ? 111  THR   A CB   1 
ATOM   833  O  OG1  . THR   A 1 108 ? -35.619 -69.501 41.147 1.00 32.99 ? 111  THR   A OG1  1 
ATOM   834  C  CG2  . THR   A 1 108 ? -37.574 -69.078 39.784 1.00 31.27 ? 111  THR   A CG2  1 
ATOM   835  N  N    . LYS   A 1 109 ? -35.068 -66.507 42.883 1.00 30.74 ? 112  LYS   A N    1 
ATOM   836  C  CA   . LYS   A 1 109 ? -34.369 -66.268 44.121 1.00 32.81 ? 112  LYS   A CA   1 
ATOM   837  C  C    . LYS   A 1 109 ? -34.277 -64.806 44.340 1.00 33.15 ? 112  LYS   A C    1 
ATOM   838  O  O    . LYS   A 1 109 ? -34.707 -64.036 43.515 1.00 35.33 ? 112  LYS   A O    1 
ATOM   839  C  CB   . LYS   A 1 109 ? -32.953 -66.873 44.067 1.00 35.15 ? 112  LYS   A CB   1 
ATOM   840  C  CG   . LYS   A 1 109 ? -32.950 -68.378 43.861 1.00 38.53 ? 112  LYS   A CG   1 
ATOM   841  C  CD   . LYS   A 1 109 ? -31.545 -68.931 43.734 1.00 43.69 ? 112  LYS   A CD   1 
ATOM   842  C  CE   . LYS   A 1 109 ? -31.528 -70.449 43.862 1.00 52.25 ? 112  LYS   A CE   1 
ATOM   843  N  NZ   . LYS   A 1 109 ? -32.142 -71.153 42.701 1.00 52.07 ? 112  LYS   A NZ   1 
ATOM   844  N  N    . LYS   A 1 110 ? -33.639 -64.417 45.415 1.00 34.24 ? 113  LYS   A N    1 
ATOM   845  C  CA   . LYS   A 1 110 ? -33.519 -63.021 45.745 1.00 32.06 ? 113  LYS   A CA   1 
ATOM   846  C  C    . LYS   A 1 110 ? -32.142 -62.506 45.325 1.00 36.72 ? 113  LYS   A C    1 
ATOM   847  O  O    . LYS   A 1 110 ? -31.143 -63.137 45.622 1.00 35.95 ? 113  LYS   A O    1 
ATOM   848  C  CB   . LYS   A 1 110 ? -33.674 -62.841 47.225 1.00 35.49 ? 113  LYS   A CB   1 
ATOM   849  C  CG   . LYS   A 1 110 ? -33.184 -61.500 47.747 1.00 40.34 ? 113  LYS   A CG   1 
ATOM   850  C  CD   . LYS   A 1 110 ? -32.780 -61.548 49.213 1.00 44.91 ? 113  LYS   A CD   1 
ATOM   851  C  CE   . LYS   A 1 110 ? -31.319 -61.946 49.410 1.00 53.81 ? 113  LYS   A CE   1 
ATOM   852  N  NZ   . LYS   A 1 110 ? -31.074 -63.408 49.565 1.00 52.36 ? 113  LYS   A NZ   1 
ATOM   853  N  N    . ASN   A 1 111 ? -32.100 -61.399 44.595 1.00 29.05 ? 114  ASN   A N    1 
ATOM   854  C  CA   . ASN   A 1 111 ? -30.845 -60.855 44.112 1.00 24.95 ? 114  ASN   A CA   1 
ATOM   855  C  C    . ASN   A 1 111 ? -30.796 -59.339 44.101 1.00 26.25 ? 114  ASN   A C    1 
ATOM   856  O  O    . ASN   A 1 111 ? -31.803 -58.714 43.870 1.00 24.77 ? 114  ASN   A O    1 
ATOM   857  C  CB   . ASN   A 1 111 ? -30.602 -61.296 42.678 1.00 25.99 ? 114  ASN   A CB   1 
ATOM   858  C  CG   . ASN   A 1 111 ? -30.433 -62.794 42.517 1.00 29.83 ? 114  ASN   A CG   1 
ATOM   859  O  OD1  . ASN   A 1 111 ? -29.372 -63.334 42.777 1.00 32.55 ? 114  ASN   A OD1  1 
ATOM   860  N  ND2  . ASN   A 1 111 ? -31.471 -63.458 42.042 1.00 28.65 ? 114  ASN   A ND2  1 
ATOM   861  N  N    . ARG   A 1 112 ? -29.640 -58.761 44.375 1.00 21.54 ? 115  ARG   A N    1 
ATOM   862  C  CA   . ARG   A 1 112 ? -29.443 -57.306 44.296 1.00 23.29 ? 115  ARG   A CA   1 
ATOM   863  C  C    . ARG   A 1 112 ? -28.108 -57.048 43.580 1.00 19.24 ? 115  ARG   A C    1 
ATOM   864  O  O    . ARG   A 1 112 ? -27.138 -56.642 44.201 1.00 22.55 ? 115  ARG   A O    1 
ATOM   865  C  CB   . ARG   A 1 112 ? -29.479 -56.652 45.672 1.00 23.47 ? 115  ARG   A CB   1 
ATOM   866  C  CG   . ARG   A 1 112 ? -30.840 -56.648 46.337 1.00 33.08 ? 115  ARG   A CG   1 
ATOM   867  C  CD   . ARG   A 1 112 ? -30.825 -55.712 47.537 1.00 40.09 ? 115  ARG   A CD   1 
ATOM   868  N  NE   . ARG   A 1 112 ? -31.604 -54.500 47.305 1.00 47.46 ? 115  ARG   A NE   1 
ATOM   869  C  CZ   . ARG   A 1 112 ? -32.905 -54.464 47.037 1.00 50.59 ? 115  ARG   A CZ   1 
ATOM   870  N  NH1  . ARG   A 1 112 ? -33.641 -55.569 46.975 1.00 53.53 ? 115  ARG   A NH1  1 
ATOM   871  N  NH2  . ARG   A 1 112 ? -33.484 -53.288 46.827 1.00 49.28 ? 115  ARG   A NH2  1 
ATOM   872  N  N    . LEU   A 1 113 ? -28.099 -57.262 42.287 1.00 18.16 ? 116  LEU   A N    1 
ATOM   873  C  CA   . LEU   A 1 113 ? -26.902 -57.130 41.468 1.00 16.20 ? 116  LEU   A CA   1 
ATOM   874  C  C    . LEU   A 1 113 ? -26.687 -55.673 41.071 1.00 18.83 ? 116  LEU   A C    1 
ATOM   875  O  O    . LEU   A 1 113 ? -27.645 -54.893 40.991 1.00 16.71 ? 116  LEU   A O    1 
ATOM   876  C  CB   . LEU   A 1 113 ? -27.044 -57.983 40.221 1.00 17.70 ? 116  LEU   A CB   1 
ATOM   877  C  CG   . LEU   A 1 113 ? -27.215 -59.485 40.466 1.00 18.44 ? 116  LEU   A CG   1 
ATOM   878  C  CD1  . LEU   A 1 113 ? -27.370 -60.192 39.149 1.00 18.43 ? 116  LEU   A CD1  1 
ATOM   879  C  CD2  . LEU   A 1 113 ? -26.011 -60.031 41.243 1.00 20.95 ? 116  LEU   A CD2  1 
ATOM   880  N  N    . PRO   A 1 114 ? -25.438 -55.273 40.826 1.00 15.66 ? 117  PRO   A N    1 
ATOM   881  C  CA   . PRO   A 1 114 ? -25.201 -53.922 40.322 1.00 13.76 ? 117  PRO   A CA   1 
ATOM   882  C  C    . PRO   A 1 114 ? -25.892 -53.758 38.978 1.00 14.92 ? 117  PRO   A C    1 
ATOM   883  O  O    . PRO   A 1 114 ? -26.040 -54.710 38.211 1.00 14.34 ? 117  PRO   A O    1 
ATOM   884  C  CB   . PRO   A 1 114 ? -23.676 -53.840 40.170 1.00 17.72 ? 117  PRO   A CB   1 
ATOM   885  C  CG   . PRO   A 1 114 ? -23.129 -55.092 40.846 1.00 18.62 ? 117  PRO   A CG   1 
ATOM   886  C  CD   . PRO   A 1 114 ? -24.216 -56.096 40.884 1.00 17.50 ? 117  PRO   A CD   1 
ATOM   887  N  N    . VAL   A 1 115 ? -26.328 -52.533 38.706 1.00 14.42 ? 118  VAL   A N    1 
ATOM   888  C  CA   . VAL   A 1 115 ? -27.083 -52.197 37.504 1.00 13.79 ? 118  VAL   A CA   1 
ATOM   889  C  C    . VAL   A 1 115 ? -26.231 -51.268 36.652 1.00 13.10 ? 118  VAL   A C    1 
ATOM   890  O  O    . VAL   A 1 115 ? -25.664 -50.311 37.162 1.00 15.40 ? 118  VAL   A O    1 
ATOM   891  C  CB   . VAL   A 1 115 ? -28.426 -51.533 37.867 1.00 15.61 ? 118  VAL   A CB   1 
ATOM   892  C  CG1  . VAL   A 1 115 ? -29.234 -51.254 36.586 1.00 11.89 ? 118  VAL   A CG1  1 
ATOM   893  C  CG2  . VAL   A 1 115 ? -29.230 -52.427 38.816 1.00 16.54 ? 118  VAL   A CG2  1 
ATOM   894  N  N    . MET   A 1 116 ? -26.193 -51.513 35.359 1.00 12.31 ? 119  MET   A N    1 
ATOM   895  C  CA   . MET   A 1 116 ? -25.377 -50.792 34.393 1.00 12.95 ? 119  MET   A CA   1 
ATOM   896  C  C    . MET   A 1 116 ? -26.352 -50.306 33.334 1.00 12.28 ? 119  MET   A C    1 
ATOM   897  O  O    . MET   A 1 116 ? -26.926 -51.140 32.635 1.00 12.77 ? 119  MET   A O    1 
ATOM   898  C  CB   . MET   A 1 116 ? -24.348 -51.794 33.864 1.00 16.19 ? 119  MET   A CB   1 
ATOM   899  C  CG   . MET   A 1 116 ? -23.239 -52.053 34.854 1.00 14.68 ? 119  MET   A CG   1 
ATOM   900  S  SD   . MET   A 1 116 ? -21.677 -52.596 34.115 1.00 16.49 ? 119  MET   A SD   1 
ATOM   901  C  CE   . MET   A 1 116 ? -20.814 -51.084 33.851 1.00 13.51 ? 119  MET   A CE   1 
ATOM   902  N  N    . VAL   A 1 117 ? -26.592 -48.988 33.263 1.00 11.30 ? 120  VAL   A N    1 
ATOM   903  C  CA   . VAL   A 1 117 ? -27.579 -48.393 32.366 1.00 10.87 ? 120  VAL   A CA   1 
ATOM   904  C  C    . VAL   A 1 117 ? -26.830 -47.726 31.212 1.00 10.79 ? 120  VAL   A C    1 
ATOM   905  O  O    . VAL   A 1 117 ? -26.124 -46.724 31.398 1.00 10.66 ? 120  VAL   A O    1 
ATOM   906  C  CB   . VAL   A 1 117 ? -28.480 -47.381 33.089 1.00 12.94 ? 120  VAL   A CB   1 
ATOM   907  C  CG1  . VAL   A 1 117 ? -29.460 -46.758 32.092 1.00 12.48 ? 120  VAL   A CG1  1 
ATOM   908  C  CG2  . VAL   A 1 117 ? -29.254 -48.034 34.238 1.00 10.06 ? 120  VAL   A CG2  1 
ATOM   909  N  N    . TRP   A 1 118 ? -27.032 -48.256 30.021 1.00 9.95  ? 121  TRP   A N    1 
ATOM   910  C  CA   . TRP   A 1 118 ? -26.350 -47.814 28.815 1.00 12.33 ? 121  TRP   A CA   1 
ATOM   911  C  C    . TRP   A 1 118 ? -27.154 -46.761 28.048 1.00 10.56 ? 121  TRP   A C    1 
ATOM   912  O  O    . TRP   A 1 118 ? -28.321 -46.983 27.678 1.00 10.99 ? 121  TRP   A O    1 
ATOM   913  C  CB   . TRP   A 1 118 ? -26.086 -49.015 27.914 1.00 11.13 ? 121  TRP   A CB   1 
ATOM   914  C  CG   . TRP   A 1 118 ? -25.463 -48.635 26.618 1.00 10.16 ? 121  TRP   A CG   1 
ATOM   915  C  CD1  . TRP   A 1 118 ? -26.054 -48.621 25.394 1.00 12.45 ? 121  TRP   A CD1  1 
ATOM   916  C  CD2  . TRP   A 1 118 ? -24.103 -48.226 26.418 1.00 11.62 ? 121  TRP   A CD2  1 
ATOM   917  N  NE1  . TRP   A 1 118 ? -25.139 -48.208 24.440 1.00 11.96 ? 121  TRP   A NE1  1 
ATOM   918  C  CE2  . TRP   A 1 118 ? -23.936 -47.979 25.043 1.00 11.99 ? 121  TRP   A CE2  1 
ATOM   919  C  CE3  . TRP   A 1 118 ? -23.007 -48.067 27.267 1.00 11.19 ? 121  TRP   A CE3  1 
ATOM   920  C  CZ2  . TRP   A 1 118 ? -22.710 -47.568 24.496 1.00 12.61 ? 121  TRP   A CZ2  1 
ATOM   921  C  CZ3  . TRP   A 1 118 ? -21.793 -47.654 26.724 1.00 12.78 ? 121  TRP   A CZ3  1 
ATOM   922  C  CH2  . TRP   A 1 118 ? -21.665 -47.402 25.353 1.00 11.30 ? 121  TRP   A CH2  1 
ATOM   923  N  N    . ILE   A 1 119 ? -26.461 -45.671 27.735 1.00 11.91 ? 122  ILE   A N    1 
ATOM   924  C  CA   . ILE   A 1 119 ? -27.034 -44.609 26.960 1.00 10.13 ? 122  ILE   A CA   1 
ATOM   925  C  C    . ILE   A 1 119 ? -26.293 -44.562 25.614 1.00 10.37 ? 122  ILE   A C    1 
ATOM   926  O  O    . ILE   A 1 119 ? -25.135 -44.235 25.554 1.00 11.66 ? 122  ILE   A O    1 
ATOM   927  C  CB   . ILE   A 1 119 ? -26.960 -43.239 27.651 1.00 12.14 ? 122  ILE   A CB   1 
ATOM   928  C  CG1  . ILE   A 1 119 ? -27.409 -43.340 29.111 1.00 11.63 ? 122  ILE   A CG1  1 
ATOM   929  C  CG2  . ILE   A 1 119 ? -27.785 -42.213 26.904 1.00 12.13 ? 122  ILE   A CG2  1 
ATOM   930  C  CD1  . ILE   A 1 119 ? -27.297 -42.033 29.859 1.00 14.27 ? 122  ILE   A CD1  1 
ATOM   931  N  N    . HIS   A 1 120 ? -27.004 -44.889 24.563 1.00 10.37 ? 123  HIS   A N    1 
ATOM   932  C  CA   . HIS   A 1 120 ? -26.400 -44.955 23.264 1.00 12.33 ? 123  HIS   A CA   1 
ATOM   933  C  C    . HIS   A 1 120 ? -25.963 -43.654 22.656 1.00 13.13 ? 123  HIS   A C    1 
ATOM   934  O  O    . HIS   A 1 120 ? -26.481 -42.607 23.021 1.00 11.68 ? 123  HIS   A O    1 
ATOM   935  C  CB   . HIS   A 1 120 ? -27.316 -45.655 22.254 1.00 11.50 ? 123  HIS   A CB   1 
ATOM   936  C  CG   . HIS   A 1 120 ? -28.505 -44.854 21.831 1.00 11.02 ? 123  HIS   A CG   1 
ATOM   937  N  ND1  . HIS   A 1 120 ? -28.437 -43.889 20.908 1.00 10.56 ? 123  HIS   A ND1  1 
ATOM   938  C  CD2  . HIS   A 1 120 ? -29.835 -44.942 22.208 1.00 14.21 ? 123  HIS   A CD2  1 
ATOM   939  C  CE1  . HIS   A 1 120 ? -29.650 -43.365 20.728 1.00 11.90 ? 123  HIS   A CE1  1 
ATOM   940  N  NE2  . HIS   A 1 120 ? -30.504 -44.016 21.519 1.00 14.17 ? 123  HIS   A NE2  1 
ATOM   941  N  N    . GLY   A 1 121 ? -24.969 -43.724 21.772 1.00 12.61 ? 124  GLY   A N    1 
ATOM   942  C  CA   . GLY   A 1 121 ? -24.491 -42.593 21.017 1.00 14.39 ? 124  GLY   A CA   1 
ATOM   943  C  C    . GLY   A 1 121 ? -25.228 -42.332 19.693 1.00 15.12 ? 124  GLY   A C    1 
ATOM   944  O  O    . GLY   A 1 121 ? -26.176 -43.036 19.397 1.00 13.26 ? 124  GLY   A O    1 
ATOM   945  N  N    . GLY   A 1 122 ? -24.708 -41.479 18.821 1.00 13.97 ? 125  GLY   A N    1 
ATOM   946  C  CA   . GLY   A 1 122 ? -25.443 -41.062 17.641 1.00 12.13 ? 125  GLY   A CA   1 
ATOM   947  C  C    . GLY   A 1 122 ? -25.624 -39.569 17.378 1.00 14.22 ? 125  GLY   A C    1 
ATOM   948  O  O    . GLY   A 1 122 ? -26.512 -39.187 16.661 1.00 14.80 ? 125  GLY   A O    1 
ATOM   949  N  N    . GLY   A 1 123 ? -24.937 -38.752 18.138 1.00 13.95 ? 126  GLY   A N    1 
ATOM   950  C  CA   . GLY   A 1 123 ? -24.943 -37.328 17.882 1.00 13.74 ? 126  GLY   A CA   1 
ATOM   951  C  C    . GLY   A 1 123 ? -26.182 -36.666 18.397 1.00 14.94 ? 126  GLY   A C    1 
ATOM   952  O  O    . GLY   A 1 123 ? -26.422 -35.541 18.035 1.00 14.76 ? 126  GLY   A O    1 
ATOM   953  N  N    . LEU   A 1 124 ? -26.995 -37.421 19.115 1.00 13.40 ? 127  LEU   A N    1 
ATOM   954  C  CA   . LEU   A 1 124 ? -28.279 -36.944 19.627 1.00 12.30 ? 127  LEU   A CA   1 
ATOM   955  C  C    . LEU   A 1 124 ? -29.288 -36.929 18.458 1.00 14.81 ? 127  LEU   A C    1 
ATOM   956  O  O    . LEU   A 1 124 ? -30.403 -36.488 18.632 1.00 13.44 ? 127  LEU   A O    1 
ATOM   957  C  CB   . LEU   A 1 124 ? -28.185 -35.616 20.355 1.00 13.72 ? 127  LEU   A CB   1 
ATOM   958  C  CG   . LEU   A 1 124 ? -27.294 -35.580 21.600 1.00 15.77 ? 127  LEU   A CG   1 
ATOM   959  C  CD1  . LEU   A 1 124 ? -27.231 -34.191 22.201 1.00 14.76 ? 127  LEU   A CD1  1 
ATOM   960  C  CD2  . LEU   A 1 124 ? -27.714 -36.608 22.634 1.00 12.39 ? 127  LEU   A CD2  1 
ATOM   961  N  N    . MET   A 1 125 ? -28.864 -37.412 17.283 1.00 13.27 ? 128  MET   A N    1 
ATOM   962  C  CA   . MET   A 1 125 ? -29.710 -37.473 16.103 1.00 13.56 ? 128  MET   A CA   1 
ATOM   963  C  C    . MET   A 1 125 ? -30.124 -38.871 15.610 1.00 13.68 ? 128  MET   A C    1 
ATOM   964  O  O    . MET   A 1 125 ? -31.146 -39.009 14.991 1.00 15.01 ? 128  MET   A O    1 
ATOM   965  C  CB   . MET   A 1 125 ? -28.924 -36.826 14.973 1.00 13.72 ? 128  MET   A CB   1 
ATOM   966  C  CG   . MET   A 1 125 ? -28.497 -35.395 15.216 1.00 14.21 ? 128  MET   A CG   1 
ATOM   967  S  SD   . MET   A 1 125 ? -29.907 -34.283 15.222 1.00 18.28 ? 128  MET   A SD   1 
ATOM   968  C  CE   . MET   A 1 125 ? -30.769 -34.827 13.761 1.00 18.80 ? 128  MET   A CE   1 
ATOM   969  N  N    . VAL   A 1 126 ? -29.340 -39.879 15.942 1.00 12.06 ? 129  VAL   A N    1 
ATOM   970  C  CA   . VAL   A 1 126 ? -29.558 -41.245 15.507 1.00 11.83 ? 129  VAL   A CA   1 
ATOM   971  C  C    . VAL   A 1 126 ? -29.165 -42.224 16.609 1.00 12.90 ? 129  VAL   A C    1 
ATOM   972  O  O    . VAL   A 1 126 ? -28.616 -41.832 17.600 1.00 12.72 ? 129  VAL   A O    1 
ATOM   973  C  CB   . VAL   A 1 126 ? -28.767 -41.624 14.243 1.00 13.97 ? 129  VAL   A CB   1 
ATOM   974  C  CG1  . VAL   A 1 126 ? -29.206 -40.833 13.025 1.00 17.01 ? 129  VAL   A CG1  1 
ATOM   975  C  CG2  . VAL   A 1 126 ? -27.273 -41.521 14.473 1.00 14.71 ? 129  VAL   A CG2  1 
ATOM   976  N  N    . GLY   A 1 127 ? -29.570 -43.473 16.458 1.00 13.69 ? 130  GLY   A N    1 
ATOM   977  C  CA   . GLY   A 1 127 ? -29.159 -44.479 17.395 1.00 12.51 ? 130  GLY   A CA   1 
ATOM   978  C  C    . GLY   A 1 127 ? -30.300 -45.274 17.979 1.00 13.35 ? 130  GLY   A C    1 
ATOM   979  O  O    . GLY   A 1 127 ? -31.438 -44.925 17.813 1.00 13.25 ? 130  GLY   A O    1 
ATOM   980  N  N    . ALA   A 1 128 ? -29.947 -46.349 18.679 1.00 12.05 ? 131  ALA   A N    1 
ATOM   981  C  CA   . ALA   A 1 128 ? -30.992 -47.206 19.247 1.00 15.28 ? 131  ALA   A CA   1 
ATOM   982  C  C    . ALA   A 1 128 ? -30.423 -48.041 20.387 1.00 12.98 ? 131  ALA   A C    1 
ATOM   983  O  O    . ALA   A 1 128 ? -29.240 -48.384 20.386 1.00 12.73 ? 131  ALA   A O    1 
ATOM   984  C  CB   . ALA   A 1 128 ? -31.601 -48.135 18.191 1.00 12.58 ? 131  ALA   A CB   1 
ATOM   985  N  N    . ALA   A 1 129 ? -31.279 -48.361 21.366 1.00 12.40 ? 132  ALA   A N    1 
ATOM   986  C  CA   . ALA   A 1 129 ? -30.867 -49.263 22.443 1.00 15.43 ? 132  ALA   A CA   1 
ATOM   987  C  C    . ALA   A 1 129 ? -30.594 -50.670 21.915 1.00 12.38 ? 132  ALA   A C    1 
ATOM   988  O  O    . ALA   A 1 129 ? -29.612 -51.317 22.308 1.00 14.38 ? 132  ALA   A O    1 
ATOM   989  C  CB   . ALA   A 1 129 ? -31.949 -49.326 23.527 1.00 13.30 ? 132  ALA   A CB   1 
ATOM   990  N  N    . SER   A 1 130 ? -31.438 -51.140 21.000 1.00 13.13 ? 133  SER   A N    1 
ATOM   991  C  CA   . SER   A 1 130 ? -31.436 -52.538 20.567 1.00 14.47 ? 133  SER   A CA   1 
ATOM   992  C  C    . SER   A 1 130 ? -30.168 -52.931 19.815 1.00 14.88 ? 133  SER   A C    1 
ATOM   993  O  O    . SER   A 1 130 ? -29.919 -54.129 19.630 1.00 14.91 ? 133  SER   A O    1 
ATOM   994  C  CB   . SER   A 1 130 ? -32.657 -52.778 19.689 1.00 15.72 ? 133  SER   A CB   1 
ATOM   995  O  OG   . SER   A 1 130 ? -33.833 -52.547 20.442 1.00 16.03 ? 133  SER   A OG   1 
ATOM   996  N  N    . THR   A 1 131 ? -29.387 -51.945 19.369 1.00 13.99 ? 134  THR   A N    1 
ATOM   997  C  CA   . THR   A 1 131 ? -28.072 -52.167 18.769 1.00 15.44 ? 134  THR   A CA   1 
ATOM   998  C  C    . THR   A 1 131 ? -27.151 -52.928 19.707 1.00 15.84 ? 134  THR   A C    1 
ATOM   999  O  O    . THR   A 1 131 ? -26.272 -53.671 19.254 1.00 16.56 ? 134  THR   A O    1 
ATOM   1000 C  CB   . THR   A 1 131 ? -27.456 -50.801 18.412 1.00 15.65 ? 134  THR   A CB   1 
ATOM   1001 O  OG1  . THR   A 1 131 ? -28.254 -50.180 17.409 1.00 15.38 ? 134  THR   A OG1  1 
ATOM   1002 C  CG2  . THR   A 1 131 ? -26.011 -50.908 17.904 1.00 13.95 ? 134  THR   A CG2  1 
ATOM   1003 N  N    . TYR   A 1 132 ? -27.337 -52.754 21.010 1.00 15.06 ? 135  TYR   A N    1 
ATOM   1004 C  CA   . TYR   A 1 132 ? -26.404 -53.232 22.012 1.00 16.64 ? 135  TYR   A CA   1 
ATOM   1005 C  C    . TYR   A 1 132 ? -27.031 -54.415 22.724 1.00 15.75 ? 135  TYR   A C    1 
ATOM   1006 O  O    . TYR   A 1 132 ? -28.059 -54.277 23.394 1.00 15.76 ? 135  TYR   A O    1 
ATOM   1007 C  CB   . TYR   A 1 132 ? -26.026 -52.121 22.990 1.00 13.41 ? 135  TYR   A CB   1 
ATOM   1008 C  CG   . TYR   A 1 132 ? -25.525 -50.917 22.246 1.00 12.78 ? 135  TYR   A CG   1 
ATOM   1009 C  CD1  . TYR   A 1 132 ? -26.418 -49.972 21.741 1.00 15.98 ? 135  TYR   A CD1  1 
ATOM   1010 C  CD2  . TYR   A 1 132 ? -24.160 -50.759 21.982 1.00 13.16 ? 135  TYR   A CD2  1 
ATOM   1011 C  CE1  . TYR   A 1 132 ? -25.979 -48.880 21.029 1.00 12.90 ? 135  TYR   A CE1  1 
ATOM   1012 C  CE2  . TYR   A 1 132 ? -23.706 -49.667 21.263 1.00 15.84 ? 135  TYR   A CE2  1 
ATOM   1013 C  CZ   . TYR   A 1 132 ? -24.623 -48.731 20.790 1.00 17.65 ? 135  TYR   A CZ   1 
ATOM   1014 O  OH   . TYR   A 1 132 ? -24.207 -47.633 20.067 1.00 23.13 ? 135  TYR   A OH   1 
ATOM   1015 N  N    . ASP   A 1 133 ? -26.420 -55.572 22.558 1.00 13.08 ? 136  ASP   A N    1 
ATOM   1016 C  CA   . ASP   A 1 133 ? -26.892 -56.791 23.189 1.00 15.03 ? 136  ASP   A CA   1 
ATOM   1017 C  C    . ASP   A 1 133 ? -26.212 -56.890 24.550 1.00 14.96 ? 136  ASP   A C    1 
ATOM   1018 O  O    . ASP   A 1 133 ? -24.977 -56.975 24.613 1.00 16.52 ? 136  ASP   A O    1 
ATOM   1019 C  CB   . ASP   A 1 133 ? -26.505 -57.980 22.315 1.00 17.47 ? 136  ASP   A CB   1 
ATOM   1020 C  CG   . ASP   A 1 133 ? -27.200 -59.250 22.710 1.00 20.99 ? 136  ASP   A CG   1 
ATOM   1021 O  OD1  . ASP   A 1 133 ? -27.523 -59.430 23.908 1.00 19.98 ? 136  ASP   A OD1  1 
ATOM   1022 O  OD2  . ASP   A 1 133 ? -27.315 -60.125 21.826 1.00 24.88 ? 136  ASP   A OD2  1 
ATOM   1023 N  N    . GLY   A 1 134 ? -26.998 -56.887 25.630 1.00 14.23 ? 137  GLY   A N    1 
ATOM   1024 C  CA   . GLY   A 1 134 ? -26.441 -56.989 26.970 1.00 12.49 ? 137  GLY   A CA   1 
ATOM   1025 C  C    . GLY   A 1 134 ? -26.111 -58.393 27.464 1.00 15.81 ? 137  GLY   A C    1 
ATOM   1026 O  O    . GLY   A 1 134 ? -25.667 -58.542 28.606 1.00 16.42 ? 137  GLY   A O    1 
ATOM   1027 N  N    . LEU   A 1 135 ? -26.293 -59.417 26.630 1.00 14.74 ? 138  LEU   A N    1 
ATOM   1028 C  CA   . LEU   A 1 135 ? -26.216 -60.808 27.089 1.00 16.26 ? 138  LEU   A CA   1 
ATOM   1029 C  C    . LEU   A 1 135 ? -24.831 -61.153 27.644 1.00 16.84 ? 138  LEU   A C    1 
ATOM   1030 O  O    . LEU   A 1 135 ? -24.701 -61.717 28.745 1.00 16.27 ? 138  LEU   A O    1 
ATOM   1031 C  CB   . LEU   A 1 135 ? -26.579 -61.733 25.928 1.00 15.74 ? 138  LEU   A CB   1 
ATOM   1032 C  CG   . LEU   A 1 135 ? -26.406 -63.254 26.107 1.00 17.75 ? 138  LEU   A CG   1 
ATOM   1033 C  CD1  . LEU   A 1 135 ? -27.399 -63.797 27.123 1.00 20.76 ? 138  LEU   A CD1  1 
ATOM   1034 C  CD2  . LEU   A 1 135 ? -26.573 -63.987 24.779 1.00 19.82 ? 138  LEU   A CD2  1 
ATOM   1035 N  N    . ALA   A 1 136 ? -23.780 -60.805 26.902 1.00 14.75 ? 139  ALA   A N    1 
ATOM   1036 C  CA   . ALA   A 1 136 ? -22.439 -61.242 27.275 1.00 16.40 ? 139  ALA   A CA   1 
ATOM   1037 C  C    . ALA   A 1 136 ? -21.951 -60.523 28.525 1.00 14.68 ? 139  ALA   A C    1 
ATOM   1038 O  O    . ALA   A 1 136 ? -21.392 -61.146 29.433 1.00 15.13 ? 139  ALA   A O    1 
ATOM   1039 C  CB   . ALA   A 1 136 ? -21.479 -61.032 26.103 1.00 18.52 ? 139  ALA   A CB   1 
ATOM   1040 N  N    . LEU   A 1 137 ? -22.146 -59.207 28.592 1.00 12.43 ? 140  LEU   A N    1 
ATOM   1041 C  CA   . LEU   A 1 137 ? -21.704 -58.460 29.759 1.00 12.48 ? 140  LEU   A CA   1 
ATOM   1042 C  C    . LEU   A 1 137 ? -22.451 -58.895 31.008 1.00 13.72 ? 140  LEU   A C    1 
ATOM   1043 O  O    . LEU   A 1 137 ? -21.850 -59.040 32.081 1.00 14.55 ? 140  LEU   A O    1 
ATOM   1044 C  CB   . LEU   A 1 137 ? -21.900 -56.954 29.511 1.00 13.94 ? 140  LEU   A CB   1 
ATOM   1045 C  CG   . LEU   A 1 137 ? -21.602 -55.992 30.656 1.00 15.71 ? 140  LEU   A CG   1 
ATOM   1046 C  CD1  . LEU   A 1 137 ? -20.148 -56.144 31.169 1.00 14.43 ? 140  LEU   A CD1  1 
ATOM   1047 C  CD2  . LEU   A 1 137 ? -21.910 -54.532 30.205 1.00 11.66 ? 140  LEU   A CD2  1 
ATOM   1048 N  N    . ALA   A 1 138 ? -23.773 -59.087 30.892 1.00 14.47 ? 141  ALA   A N    1 
ATOM   1049 C  CA   . ALA   A 1 138 ? -24.573 -59.554 32.022 1.00 16.11 ? 141  ALA   A CA   1 
ATOM   1050 C  C    . ALA   A 1 138 ? -24.096 -60.914 32.522 1.00 15.31 ? 141  ALA   A C    1 
ATOM   1051 O  O    . ALA   A 1 138 ? -23.918 -61.115 33.729 1.00 14.82 ? 141  ALA   A O    1 
ATOM   1052 C  CB   . ALA   A 1 138 ? -26.056 -59.640 31.620 1.00 13.68 ? 141  ALA   A CB   1 
ATOM   1053 N  N    . ALA   A 1 139 ? -23.940 -61.878 31.611 1.00 12.53 ? 142  ALA   A N    1 
ATOM   1054 C  CA   . ALA   A 1 139 ? -23.554 -63.229 32.034 1.00 16.71 ? 142  ALA   A CA   1 
ATOM   1055 C  C    . ALA   A 1 139 ? -22.121 -63.263 32.558 1.00 22.31 ? 142  ALA   A C    1 
ATOM   1056 O  O    . ALA   A 1 139 ? -21.850 -63.851 33.613 1.00 20.59 ? 142  ALA   A O    1 
ATOM   1057 C  CB   . ALA   A 1 139 ? -23.718 -64.210 30.872 1.00 15.85 ? 142  ALA   A CB   1 
ATOM   1058 N  N    . HIS   A 1 140 ? -21.192 -62.609 31.856 1.00 16.57 ? 143  HIS   A N    1 
ATOM   1059 C  CA   . HIS   A 1 140 ? -19.789 -62.689 32.235 1.00 19.38 ? 143  HIS   A CA   1 
ATOM   1060 C  C    . HIS   A 1 140 ? -19.516 -61.972 33.541 1.00 20.99 ? 143  HIS   A C    1 
ATOM   1061 O  O    . HIS   A 1 140 ? -18.659 -62.414 34.315 1.00 18.40 ? 143  HIS   A O    1 
ATOM   1062 C  CB   . HIS   A 1 140 ? -18.912 -62.106 31.134 1.00 18.67 ? 143  HIS   A CB   1 
ATOM   1063 C  CG   . HIS   A 1 140 ? -18.635 -63.068 30.024 1.00 19.41 ? 143  HIS   A CG   1 
ATOM   1064 N  ND1  . HIS   A 1 140 ? -17.450 -63.772 29.928 1.00 19.56 ? 143  HIS   A ND1  1 
ATOM   1065 C  CD2  . HIS   A 1 140 ? -19.389 -63.453 28.968 1.00 20.32 ? 143  HIS   A CD2  1 
ATOM   1066 C  CE1  . HIS   A 1 140 ? -17.485 -64.541 28.854 1.00 19.21 ? 143  HIS   A CE1  1 
ATOM   1067 N  NE2  . HIS   A 1 140 ? -18.653 -64.374 28.258 1.00 22.51 ? 143  HIS   A NE2  1 
ATOM   1068 N  N    . GLU   A 1 141 ? -20.204 -60.861 33.807 1.00 14.72 ? 144  GLU   A N    1 
ATOM   1069 C  CA   . GLU   A 1 141 ? -19.868 -60.084 34.986 1.00 13.90 ? 144  GLU   A CA   1 
ATOM   1070 C  C    . GLU   A 1 141 ? -20.961 -60.019 36.049 1.00 17.90 ? 144  GLU   A C    1 
ATOM   1071 O  O    . GLU   A 1 141 ? -20.779 -59.322 37.057 1.00 17.55 ? 144  GLU   A O    1 
ATOM   1072 C  CB   . GLU   A 1 141 ? -19.448 -58.672 34.563 1.00 15.68 ? 144  GLU   A CB   1 
ATOM   1073 C  CG   . GLU   A 1 141 ? -18.012 -58.661 33.989 1.00 18.41 ? 144  GLU   A CG   1 
ATOM   1074 C  CD   . GLU   A 1 141 ? -16.977 -59.282 34.941 1.00 21.17 ? 144  GLU   A CD   1 
ATOM   1075 O  OE1  . GLU   A 1 141 ? -17.096 -59.108 36.180 1.00 20.33 ? 144  GLU   A OE1  1 
ATOM   1076 O  OE2  . GLU   A 1 141 ? -16.033 -59.950 34.445 1.00 21.90 ? 144  GLU   A OE2  1 
ATOM   1077 N  N    . ASN   A 1 142 ? -22.066 -60.748 35.885 1.00 15.96 ? 145  ASN   A N    1 
ATOM   1078 C  CA   . ASN   A 1 142 ? -23.098 -60.803 36.920 1.00 19.41 ? 145  ASN   A CA   1 
ATOM   1079 C  C    . ASN   A 1 142 ? -23.611 -59.398 37.259 1.00 16.61 ? 145  ASN   A C    1 
ATOM   1080 O  O    . ASN   A 1 142 ? -23.647 -58.973 38.418 1.00 16.75 ? 145  ASN   A O    1 
ATOM   1081 C  CB   . ASN   A 1 142 ? -22.574 -61.521 38.167 1.00 17.17 ? 145  ASN   A CB   1 
ATOM   1082 C  CG   . ASN   A 1 142 ? -23.651 -62.311 38.870 1.00 34.32 ? 145  ASN   A CG   1 
ATOM   1083 O  OD1  . ASN   A 1 142 ? -24.450 -63.001 38.226 1.00 35.93 ? 145  ASN   A OD1  1 
ATOM   1084 N  ND2  . ASN   A 1 142 ? -23.683 -62.221 40.200 1.00 35.46 ? 145  ASN   A ND2  1 
ATOM   1085 N  N    . VAL   A 1 143 ? -23.961 -58.653 36.218 1.00 15.89 ? 146  VAL   A N    1 
ATOM   1086 C  CA   . VAL   A 1 143 ? -24.577 -57.338 36.366 1.00 14.55 ? 146  VAL   A CA   1 
ATOM   1087 C  C    . VAL   A 1 143 ? -25.848 -57.304 35.533 1.00 15.01 ? 146  VAL   A C    1 
ATOM   1088 O  O    . VAL   A 1 143 ? -25.968 -57.992 34.514 1.00 14.83 ? 146  VAL   A O    1 
ATOM   1089 C  CB   . VAL   A 1 143 ? -23.635 -56.189 35.936 1.00 17.69 ? 146  VAL   A CB   1 
ATOM   1090 C  CG1  . VAL   A 1 143 ? -22.374 -56.154 36.789 1.00 18.41 ? 146  VAL   A CG1  1 
ATOM   1091 C  CG2  . VAL   A 1 143 ? -23.281 -56.330 34.469 1.00 16.61 ? 146  VAL   A CG2  1 
ATOM   1092 N  N    . VAL   A 1 144 ? -26.804 -56.490 35.971 1.00 15.12 ? 147  VAL   A N    1 
ATOM   1093 C  CA   . VAL   A 1 144 ? -28.019 -56.237 35.203 1.00 15.07 ? 147  VAL   A CA   1 
ATOM   1094 C  C    . VAL   A 1 144 ? -27.711 -55.125 34.206 1.00 11.72 ? 147  VAL   A C    1 
ATOM   1095 O  O    . VAL   A 1 144 ? -27.337 -54.019 34.604 1.00 14.92 ? 147  VAL   A O    1 
ATOM   1096 C  CB   . VAL   A 1 144 ? -29.180 -55.831 36.123 1.00 14.82 ? 147  VAL   A CB   1 
ATOM   1097 C  CG1  . VAL   A 1 144 ? -30.425 -55.481 35.304 1.00 16.28 ? 147  VAL   A CG1  1 
ATOM   1098 C  CG2  . VAL   A 1 144 ? -29.477 -56.939 37.149 1.00 16.37 ? 147  VAL   A CG2  1 
ATOM   1099 N  N    . VAL   A 1 145 ? -27.881 -55.401 32.915 1.00 13.84 ? 148  VAL   A N    1 
ATOM   1100 C  CA   . VAL   A 1 145 ? -27.632 -54.399 31.883 1.00 11.78 ? 148  VAL   A CA   1 
ATOM   1101 C  C    . VAL   A 1 145 ? -28.974 -53.870 31.392 1.00 11.29 ? 148  VAL   A C    1 
ATOM   1102 O  O    . VAL   A 1 145 ? -29.873 -54.649 31.056 1.00 12.76 ? 148  VAL   A O    1 
ATOM   1103 C  CB   . VAL   A 1 145 ? -26.806 -54.957 30.711 1.00 15.57 ? 148  VAL   A CB   1 
ATOM   1104 C  CG1  . VAL   A 1 145 ? -26.565 -53.851 29.678 1.00 13.31 ? 148  VAL   A CG1  1 
ATOM   1105 C  CG2  . VAL   A 1 145 ? -25.454 -55.550 31.191 1.00 11.53 ? 148  VAL   A CG2  1 
ATOM   1106 N  N    . VAL   A 1 146 ? -29.112 -52.548 31.349 1.00 10.84 ? 149  VAL   A N    1 
ATOM   1107 C  CA   . VAL   A 1 146 ? -30.336 -51.880 30.884 1.00 10.85 ? 149  VAL   A CA   1 
ATOM   1108 C  C    . VAL   A 1 146 ? -29.929 -50.971 29.731 1.00 12.45 ? 149  VAL   A C    1 
ATOM   1109 O  O    . VAL   A 1 146 ? -29.056 -50.122 29.901 1.00 14.40 ? 149  VAL   A O    1 
ATOM   1110 C  CB   . VAL   A 1 146 ? -30.995 -51.065 32.012 1.00 10.30 ? 149  VAL   A CB   1 
ATOM   1111 C  CG1  . VAL   A 1 146 ? -32.318 -50.363 31.532 1.00 11.00 ? 149  VAL   A CG1  1 
ATOM   1112 C  CG2  . VAL   A 1 146 ? -31.230 -51.926 33.257 1.00 12.82 ? 149  VAL   A CG2  1 
ATOM   1113 N  N    . THR   A 1 147 ? -30.517 -51.151 28.558 1.00 10.56 ? 150  THR   A N    1 
ATOM   1114 C  CA   . THR   A 1 147 ? -30.237 -50.241 27.455 1.00 9.71  ? 150  THR   A CA   1 
ATOM   1115 C  C    . THR   A 1 147 ? -31.448 -49.333 27.260 1.00 10.50 ? 150  THR   A C    1 
ATOM   1116 O  O    . THR   A 1 147 ? -32.578 -49.827 27.172 1.00 11.40 ? 150  THR   A O    1 
ATOM   1117 C  CB   . THR   A 1 147 ? -29.887 -51.012 26.178 1.00 9.99  ? 150  THR   A CB   1 
ATOM   1118 O  OG1  . THR   A 1 147 ? -30.971 -51.876 25.818 1.00 13.60 ? 150  THR   A OG1  1 
ATOM   1119 C  CG2  . THR   A 1 147 ? -28.608 -51.879 26.401 1.00 11.38 ? 150  THR   A CG2  1 
ATOM   1120 N  N    . ILE   A 1 148 ? -31.228 -48.010 27.228 1.00 10.72 ? 151  ILE   A N    1 
ATOM   1121 C  CA   . ILE   A 1 148 ? -32.376 -47.088 27.193 1.00 11.35 ? 151  ILE   A CA   1 
ATOM   1122 C  C    . ILE   A 1 148 ? -32.456 -46.334 25.872 1.00 9.82  ? 151  ILE   A C    1 
ATOM   1123 O  O    . ILE   A 1 148 ? -31.467 -46.140 25.171 1.00 13.82 ? 151  ILE   A O    1 
ATOM   1124 C  CB   . ILE   A 1 148 ? -32.354 -46.087 28.365 1.00 10.59 ? 151  ILE   A CB   1 
ATOM   1125 C  CG1  . ILE   A 1 148 ? -31.203 -45.084 28.213 1.00 11.43 ? 151  ILE   A CG1  1 
ATOM   1126 C  CG2  . ILE   A 1 148 ? -32.287 -46.846 29.702 1.00 9.60  ? 151  ILE   A CG2  1 
ATOM   1127 C  CD1  . ILE   A 1 148 ? -31.337 -43.883 29.121 1.00 13.30 ? 151  ILE   A CD1  1 
ATOM   1128 N  N    . GLN   A 1 149 ? -33.661 -45.853 25.561 1.00 10.57 ? 152  GLN   A N    1 
ATOM   1129 C  CA   . GLN   A 1 149 ? -33.870 -44.980 24.424 1.00 11.26 ? 152  GLN   A CA   1 
ATOM   1130 C  C    . GLN   A 1 149 ? -34.354 -43.628 24.921 1.00 11.74 ? 152  GLN   A C    1 
ATOM   1131 O  O    . GLN   A 1 149 ? -34.733 -43.462 26.085 1.00 12.80 ? 152  GLN   A O    1 
ATOM   1132 C  CB   . GLN   A 1 149 ? -34.843 -45.590 23.396 1.00 11.38 ? 152  GLN   A CB   1 
ATOM   1133 C  CG   . GLN   A 1 149 ? -34.128 -46.742 22.672 1.00 12.62 ? 152  GLN   A CG   1 
ATOM   1134 C  CD   . GLN   A 1 149 ? -34.878 -47.385 21.530 1.00 13.56 ? 152  GLN   A CD   1 
ATOM   1135 O  OE1  . GLN   A 1 149 ? -34.314 -48.225 20.828 1.00 13.01 ? 152  GLN   A OE1  1 
ATOM   1136 N  NE2  . GLN   A 1 149 ? -36.144 -47.029 21.344 1.00 11.52 ? 152  GLN   A NE2  1 
ATOM   1137 N  N    . TYR   A 1 150 ? -34.250 -42.647 24.040 1.00 11.18 ? 153  TYR   A N    1 
ATOM   1138 C  CA   . TYR   A 1 150 ? -34.546 -41.261 24.383 1.00 10.39 ? 153  TYR   A CA   1 
ATOM   1139 C  C    . TYR   A 1 150 ? -34.795 -40.528 23.083 1.00 11.48 ? 153  TYR   A C    1 
ATOM   1140 O  O    . TYR   A 1 150 ? -34.253 -40.899 22.047 1.00 10.61 ? 153  TYR   A O    1 
ATOM   1141 C  CB   . TYR   A 1 150 ? -33.393 -40.618 25.175 1.00 11.38 ? 153  TYR   A CB   1 
ATOM   1142 C  CG   . TYR   A 1 150 ? -32.037 -40.649 24.468 1.00 11.29 ? 153  TYR   A CG   1 
ATOM   1143 C  CD1  . TYR   A 1 150 ? -31.213 -41.764 24.551 1.00 12.67 ? 153  TYR   A CD1  1 
ATOM   1144 C  CD2  . TYR   A 1 150 ? -31.582 -39.547 23.734 1.00 11.94 ? 153  TYR   A CD2  1 
ATOM   1145 C  CE1  . TYR   A 1 150 ? -29.957 -41.790 23.912 1.00 11.13 ? 153  TYR   A CE1  1 
ATOM   1146 C  CE2  . TYR   A 1 150 ? -30.334 -39.555 23.102 1.00 12.65 ? 153  TYR   A CE2  1 
ATOM   1147 C  CZ   . TYR   A 1 150 ? -29.526 -40.687 23.193 1.00 12.96 ? 153  TYR   A CZ   1 
ATOM   1148 O  OH   . TYR   A 1 150 ? -28.297 -40.711 22.557 1.00 12.85 ? 153  TYR   A OH   1 
ATOM   1149 N  N    . ARG   A 1 151 ? -35.652 -39.509 23.131 1.00 11.05 ? 154  ARG   A N    1 
ATOM   1150 C  CA   . ARG   A 1 151 ? -36.014 -38.824 21.898 1.00 11.54 ? 154  ARG   A CA   1 
ATOM   1151 C  C    . ARG   A 1 151 ? -34.793 -38.170 21.261 1.00 9.59  ? 154  ARG   A C    1 
ATOM   1152 O  O    . ARG   A 1 151 ? -33.914 -37.653 21.946 1.00 11.33 ? 154  ARG   A O    1 
ATOM   1153 C  CB   . ARG   A 1 151 ? -37.098 -37.786 22.185 1.00 11.27 ? 154  ARG   A CB   1 
ATOM   1154 C  CG   . ARG   A 1 151 ? -38.480 -38.413 22.367 1.00 11.26 ? 154  ARG   A CG   1 
ATOM   1155 C  CD   . ARG   A 1 151 ? -39.459 -37.324 22.800 1.00 12.61 ? 154  ARG   A CD   1 
ATOM   1156 N  NE   . ARG   A 1 151 ? -39.357 -37.099 24.235 1.00 14.16 ? 154  ARG   A NE   1 
ATOM   1157 C  CZ   . ARG   A 1 151 ? -40.094 -36.226 24.900 1.00 16.77 ? 154  ARG   A CZ   1 
ATOM   1158 N  NH1  . ARG   A 1 151 ? -40.954 -35.438 24.275 1.00 15.24 ? 154  ARG   A NH1  1 
ATOM   1159 N  NH2  . ARG   A 1 151 ? -39.958 -36.134 26.224 1.00 15.59 ? 154  ARG   A NH2  1 
ATOM   1160 N  N    . LEU   A 1 152 ? -34.744 -38.190 19.926 1.00 11.33 ? 155  LEU   A N    1 
ATOM   1161 C  CA   . LEU   A 1 152 ? -33.586 -37.761 19.154 1.00 12.05 ? 155  LEU   A CA   1 
ATOM   1162 C  C    . LEU   A 1 152 ? -33.972 -36.612 18.225 1.00 13.05 ? 155  LEU   A C    1 
ATOM   1163 O  O    . LEU   A 1 152 ? -35.144 -36.451 17.866 1.00 11.64 ? 155  LEU   A O    1 
ATOM   1164 C  CB   . LEU   A 1 152 ? -33.052 -38.925 18.306 1.00 13.91 ? 155  LEU   A CB   1 
ATOM   1165 C  CG   . LEU   A 1 152 ? -32.611 -40.174 19.067 1.00 13.98 ? 155  LEU   A CG   1 
ATOM   1166 C  CD1  . LEU   A 1 152 ? -32.421 -41.367 18.121 1.00 12.67 ? 155  LEU   A CD1  1 
ATOM   1167 C  CD2  . LEU   A 1 152 ? -31.315 -39.864 19.795 1.00 11.95 ? 155  LEU   A CD2  1 
ATOM   1168 N  N    . GLY   A 1 153 ? -32.971 -35.829 17.824 1.00 13.62 ? 156  GLY   A N    1 
ATOM   1169 C  CA   . GLY   A 1 153 ? -33.176 -34.880 16.743 1.00 13.70 ? 156  GLY   A CA   1 
ATOM   1170 C  C    . GLY   A 1 153 ? -34.194 -33.816 17.106 1.00 13.97 ? 156  GLY   A C    1 
ATOM   1171 O  O    . GLY   A 1 153 ? -34.223 -33.314 18.234 1.00 12.34 ? 156  GLY   A O    1 
ATOM   1172 N  N    . ILE   A 1 154 ? -35.040 -33.461 16.135 1.00 13.52 ? 157  ILE   A N    1 
ATOM   1173 C  CA   . ILE   A 1 154 ? -36.072 -32.447 16.379 1.00 13.73 ? 157  ILE   A CA   1 
ATOM   1174 C  C    . ILE   A 1 154 ? -36.948 -32.841 17.563 1.00 13.28 ? 157  ILE   A C    1 
ATOM   1175 O  O    . ILE   A 1 154 ? -37.234 -32.015 18.441 1.00 11.45 ? 157  ILE   A O    1 
ATOM   1176 C  CB   . ILE   A 1 154 ? -36.906 -32.213 15.105 1.00 13.61 ? 157  ILE   A CB   1 
ATOM   1177 C  CG1  . ILE   A 1 154 ? -36.031 -31.640 13.985 1.00 15.90 ? 157  ILE   A CG1  1 
ATOM   1178 C  CG2  . ILE   A 1 154 ? -38.119 -31.322 15.385 1.00 15.89 ? 157  ILE   A CG2  1 
ATOM   1179 C  CD1  . ILE   A 1 154 ? -36.739 -31.623 12.634 1.00 19.78 ? 157  ILE   A CD1  1 
ATOM   1180 N  N    . TRP   A 1 155 ? -37.363 -34.115 17.623 1.00 11.54 ? 158  TRP   A N    1 
ATOM   1181 C  CA   . TRP   A 1 155 ? -38.268 -34.558 18.682 1.00 13.05 ? 158  TRP   A CA   1 
ATOM   1182 C  C    . TRP   A 1 155 ? -37.622 -34.443 20.052 1.00 12.70 ? 158  TRP   A C    1 
ATOM   1183 O  O    . TRP   A 1 155 ? -38.306 -34.167 21.046 1.00 12.62 ? 158  TRP   A O    1 
ATOM   1184 C  CB   . TRP   A 1 155 ? -38.694 -36.021 18.458 1.00 11.12 ? 158  TRP   A CB   1 
ATOM   1185 C  CG   . TRP   A 1 155 ? -39.481 -36.241 17.209 1.00 13.89 ? 158  TRP   A CG   1 
ATOM   1186 C  CD1  . TRP   A 1 155 ? -40.847 -36.350 17.099 1.00 15.56 ? 158  TRP   A CD1  1 
ATOM   1187 C  CD2  . TRP   A 1 155 ? -38.954 -36.446 15.889 1.00 14.42 ? 158  TRP   A CD2  1 
ATOM   1188 N  NE1  . TRP   A 1 155 ? -41.197 -36.562 15.783 1.00 15.06 ? 158  TRP   A NE1  1 
ATOM   1189 C  CE2  . TRP   A 1 155 ? -40.058 -36.626 15.021 1.00 15.55 ? 158  TRP   A CE2  1 
ATOM   1190 C  CE3  . TRP   A 1 155 ? -37.657 -36.469 15.354 1.00 13.80 ? 158  TRP   A CE3  1 
ATOM   1191 C  CZ2  . TRP   A 1 155 ? -39.906 -36.856 13.648 1.00 16.32 ? 158  TRP   A CZ2  1 
ATOM   1192 C  CZ3  . TRP   A 1 155 ? -37.504 -36.679 13.984 1.00 15.64 ? 158  TRP   A CZ3  1 
ATOM   1193 C  CH2  . TRP   A 1 155 ? -38.632 -36.868 13.146 1.00 16.48 ? 158  TRP   A CH2  1 
ATOM   1194 N  N    . GLY   A 1 156 ? -36.315 -34.693 20.135 1.00 11.50 ? 159  GLY   A N    1 
ATOM   1195 C  CA   . GLY   A 1 156 ? -35.671 -34.712 21.434 1.00 11.11 ? 159  GLY   A CA   1 
ATOM   1196 C  C    . GLY   A 1 156 ? -35.052 -33.388 21.839 1.00 13.04 ? 159  GLY   A C    1 
ATOM   1197 O  O    . GLY   A 1 156 ? -34.788 -33.158 23.024 1.00 12.65 ? 159  GLY   A O    1 
ATOM   1198 N  N    . PHE   A 1 157 ? -34.781 -32.510 20.881 1.00 10.31 ? 160  PHE   A N    1 
ATOM   1199 C  CA   . PHE   A 1 157 ? -33.948 -31.360 21.217 1.00 10.45 ? 160  PHE   A CA   1 
ATOM   1200 C  C    . PHE   A 1 157 ? -34.392 -30.044 20.594 1.00 14.64 ? 160  PHE   A C    1 
ATOM   1201 O  O    . PHE   A 1 157 ? -33.686 -29.041 20.759 1.00 13.06 ? 160  PHE   A O    1 
ATOM   1202 C  CB   . PHE   A 1 157 ? -32.483 -31.687 20.867 1.00 12.79 ? 160  PHE   A CB   1 
ATOM   1203 C  CG   . PHE   A 1 157 ? -31.958 -32.809 21.686 1.00 11.83 ? 160  PHE   A CG   1 
ATOM   1204 C  CD1  . PHE   A 1 157 ? -31.490 -32.570 22.973 1.00 11.95 ? 160  PHE   A CD1  1 
ATOM   1205 C  CD2  . PHE   A 1 157 ? -32.061 -34.131 21.240 1.00 13.20 ? 160  PHE   A CD2  1 
ATOM   1206 C  CE1  . PHE   A 1 157 ? -31.064 -33.629 23.776 1.00 14.61 ? 160  PHE   A CE1  1 
ATOM   1207 C  CE2  . PHE   A 1 157 ? -31.649 -35.186 22.043 1.00 13.80 ? 160  PHE   A CE2  1 
ATOM   1208 C  CZ   . PHE   A 1 157 ? -31.146 -34.934 23.312 1.00 12.39 ? 160  PHE   A CZ   1 
ATOM   1209 N  N    . PHE   A 1 158 ? -35.567 -29.983 19.970 1.00 13.96 ? 161  PHE   A N    1 
ATOM   1210 C  CA   . PHE   A 1 158 ? -36.049 -28.704 19.451 1.00 16.66 ? 161  PHE   A CA   1 
ATOM   1211 C  C    . PHE   A 1 158 ? -36.218 -27.699 20.584 1.00 14.86 ? 161  PHE   A C    1 
ATOM   1212 O  O    . PHE   A 1 158 ? -36.914 -27.970 21.566 1.00 13.45 ? 161  PHE   A O    1 
ATOM   1213 C  CB   . PHE   A 1 158 ? -37.379 -28.865 18.726 1.00 15.22 ? 161  PHE   A CB   1 
ATOM   1214 C  CG   . PHE   A 1 158 ? -37.886 -27.573 18.136 1.00 16.76 ? 161  PHE   A CG   1 
ATOM   1215 C  CD1  . PHE   A 1 158 ? -37.317 -27.048 16.975 1.00 18.37 ? 161  PHE   A CD1  1 
ATOM   1216 C  CD2  . PHE   A 1 158 ? -38.888 -26.848 18.777 1.00 18.76 ? 161  PHE   A CD2  1 
ATOM   1217 C  CE1  . PHE   A 1 158 ? -37.770 -25.835 16.442 1.00 17.10 ? 161  PHE   A CE1  1 
ATOM   1218 C  CE2  . PHE   A 1 158 ? -39.336 -25.634 18.252 1.00 16.81 ? 161  PHE   A CE2  1 
ATOM   1219 C  CZ   . PHE   A 1 158 ? -38.771 -25.132 17.088 1.00 17.35 ? 161  PHE   A CZ   1 
ATOM   1220 N  N    . SER   A 1 159 ? -35.581 -26.534 20.440 1.00 15.24 ? 162  SER   A N    1 
ATOM   1221 C  CA   . SER   A 1 159 ? -35.606 -25.498 21.467 1.00 17.29 ? 162  SER   A CA   1 
ATOM   1222 C  C    . SER   A 1 159 ? -35.849 -24.135 20.831 1.00 18.00 ? 162  SER   A C    1 
ATOM   1223 O  O    . SER   A 1 159 ? -35.168 -23.777 19.870 1.00 17.29 ? 162  SER   A O    1 
ATOM   1224 C  CB   . SER   A 1 159 ? -34.291 -25.464 22.257 1.00 17.46 ? 162  SER   A CB   1 
ATOM   1225 O  OG   . SER   A 1 159 ? -34.325 -24.412 23.220 1.00 18.19 ? 162  SER   A OG   1 
ATOM   1226 N  N    . THR   A 1 160 ? -36.825 -23.388 21.350 1.00 15.81 ? 163  THR   A N    1 
ATOM   1227 C  CA   . THR   A 1 160 ? -36.984 -21.985 20.986 1.00 17.17 ? 163  THR   A CA   1 
ATOM   1228 C  C    . THR   A 1 160 ? -36.152 -21.052 21.853 1.00 22.41 ? 163  THR   A C    1 
ATOM   1229 O  O    . THR   A 1 160 ? -36.201 -19.832 21.650 1.00 20.58 ? 163  THR   A O    1 
ATOM   1230 C  CB   . THR   A 1 160 ? -38.451 -21.556 21.099 1.00 14.61 ? 163  THR   A CB   1 
ATOM   1231 O  OG1  . THR   A 1 160 ? -38.958 -21.926 22.389 1.00 18.08 ? 163  THR   A OG1  1 
ATOM   1232 C  CG2  . THR   A 1 160 ? -39.296 -22.223 20.010 1.00 16.04 ? 163  THR   A CG2  1 
ATOM   1233 N  N    . GLY   A 1 161 ? -35.417 -21.584 22.830 1.00 20.05 ? 164  GLY   A N    1 
ATOM   1234 C  CA   . GLY   A 1 161 ? -34.672 -20.756 23.759 1.00 22.86 ? 164  GLY   A CA   1 
ATOM   1235 C  C    . GLY   A 1 161 ? -35.501 -20.104 24.842 1.00 24.63 ? 164  GLY   A C    1 
ATOM   1236 O  O    . GLY   A 1 161 ? -34.994 -19.222 25.539 1.00 19.79 ? 164  GLY   A O    1 
ATOM   1237 N  N    . ASP   A 1 162 ? -36.754 -20.506 25.015 1.00 19.01 ? 165  ASP   A N    1 
ATOM   1238 C  CA   . ASP   A 1 162 ? -37.626 -19.866 25.988 1.00 20.48 ? 165  ASP   A CA   1 
ATOM   1239 C  C    . ASP   A 1 162 ? -38.627 -20.904 26.489 1.00 21.36 ? 165  ASP   A C    1 
ATOM   1240 O  O    . ASP   A 1 162 ? -38.488 -22.102 26.222 1.00 18.03 ? 165  ASP   A O    1 
ATOM   1241 C  CB   . ASP   A 1 162 ? -38.271 -18.613 25.371 1.00 22.22 ? 165  ASP   A CB   1 
ATOM   1242 C  CG   . ASP   A 1 162 ? -39.220 -18.931 24.210 1.00 23.36 ? 165  ASP   A CG   1 
ATOM   1243 O  OD1  . ASP   A 1 162 ? -39.745 -20.068 24.111 1.00 19.78 ? 165  ASP   A OD1  1 
ATOM   1244 O  OD2  . ASP   A 1 162 ? -39.442 -18.027 23.372 1.00 25.29 ? 165  ASP   A OD2  1 
ATOM   1245 N  N    . GLU   A 1 163 ? -39.650 -20.434 27.208 1.00 17.43 ? 166  GLU   A N    1 
ATOM   1246 C  CA   . GLU   A 1 163 ? -40.521 -21.346 27.939 1.00 18.34 ? 166  GLU   A CA   1 
ATOM   1247 C  C    . GLU   A 1 163 ? -41.458 -22.122 27.025 1.00 19.18 ? 166  GLU   A C    1 
ATOM   1248 O  O    . GLU   A 1 163 ? -42.022 -23.136 27.453 1.00 17.00 ? 166  GLU   A O    1 
ATOM   1249 C  CB   . GLU   A 1 163 ? -41.331 -20.587 28.997 1.00 19.66 ? 166  GLU   A CB   1 
ATOM   1250 C  CG   . GLU   A 1 163 ? -42.385 -19.603 28.457 1.00 17.82 ? 166  GLU   A CG   1 
ATOM   1251 C  CD   . GLU   A 1 163 ? -41.835 -18.215 28.088 1.00 22.17 ? 166  GLU   A CD   1 
ATOM   1252 O  OE1  . GLU   A 1 163 ? -40.611 -18.055 27.878 1.00 19.58 ? 166  GLU   A OE1  1 
ATOM   1253 O  OE2  . GLU   A 1 163 ? -42.646 -17.264 28.024 1.00 19.06 ? 166  GLU   A OE2  1 
ATOM   1254 N  N    . HIS   A 1 164 ? -41.619 -21.701 25.771 1.00 16.42 ? 167  HIS   A N    1 
ATOM   1255 C  CA   . HIS   A 1 164 ? -42.533 -22.393 24.869 1.00 17.90 ? 167  HIS   A CA   1 
ATOM   1256 C  C    . HIS   A 1 164 ? -41.949 -23.703 24.331 1.00 18.41 ? 167  HIS   A C    1 
ATOM   1257 O  O    . HIS   A 1 164 ? -42.708 -24.612 23.961 1.00 17.90 ? 167  HIS   A O    1 
ATOM   1258 C  CB   . HIS   A 1 164 ? -42.933 -21.455 23.734 1.00 15.75 ? 167  HIS   A CB   1 
ATOM   1259 C  CG   . HIS   A 1 164 ? -43.649 -20.234 24.223 1.00 20.49 ? 167  HIS   A CG   1 
ATOM   1260 N  ND1  . HIS   A 1 164 ? -44.852 -20.301 24.897 1.00 19.31 ? 167  HIS   A ND1  1 
ATOM   1261 C  CD2  . HIS   A 1 164 ? -43.292 -18.927 24.222 1.00 19.29 ? 167  HIS   A CD2  1 
ATOM   1262 C  CE1  . HIS   A 1 164 ? -45.228 -19.079 25.243 1.00 21.01 ? 167  HIS   A CE1  1 
ATOM   1263 N  NE2  . HIS   A 1 164 ? -44.293 -18.229 24.856 1.00 17.87 ? 167  HIS   A NE2  1 
ATOM   1264 N  N    . SER   A 1 165 ? -40.622 -23.836 24.295 1.00 16.28 ? 168  SER   A N    1 
ATOM   1265 C  CA   . SER   A 1 165 ? -39.994 -25.132 23.995 1.00 16.07 ? 168  SER   A CA   1 
ATOM   1266 C  C    . SER   A 1 165 ? -38.563 -25.030 24.534 1.00 14.96 ? 168  SER   A C    1 
ATOM   1267 O  O    . SER   A 1 165 ? -37.643 -24.699 23.793 1.00 15.81 ? 168  SER   A O    1 
ATOM   1268 C  CB   . SER   A 1 165 ? -40.002 -25.479 22.517 1.00 15.73 ? 168  SER   A CB   1 
ATOM   1269 O  OG   . SER   A 1 165 ? -39.564 -26.834 22.321 1.00 17.08 ? 168  SER   A OG   1 
ATOM   1270 N  N    . ARG   A 1 166 ? -38.400 -25.333 25.824 1.00 13.47 ? 169  ARG   A N    1 
ATOM   1271 C  CA   . ARG   A 1 166 ? -37.111 -25.144 26.480 1.00 16.93 ? 169  ARG   A CA   1 
ATOM   1272 C  C    . ARG   A 1 166 ? -36.018 -25.968 25.810 1.00 14.79 ? 169  ARG   A C    1 
ATOM   1273 O  O    . ARG   A 1 166 ? -34.895 -25.476 25.602 1.00 15.01 ? 169  ARG   A O    1 
ATOM   1274 C  CB   . ARG   A 1 166 ? -37.227 -25.528 27.952 1.00 15.57 ? 169  ARG   A CB   1 
ATOM   1275 C  CG   . ARG   A 1 166 ? -37.777 -24.467 28.863 1.00 15.98 ? 169  ARG   A CG   1 
ATOM   1276 C  CD   . ARG   A 1 166 ? -37.500 -24.837 30.306 1.00 21.49 ? 169  ARG   A CD   1 
ATOM   1277 N  NE   . ARG   A 1 166 ? -37.691 -23.712 31.218 1.00 24.51 ? 169  ARG   A NE   1 
ATOM   1278 C  CZ   . ARG   A 1 166 ? -38.884 -23.328 31.639 1.00 23.93 ? 169  ARG   A CZ   1 
ATOM   1279 N  NH1  . ARG   A 1 166 ? -39.978 -23.927 31.215 1.00 25.81 ? 169  ARG   A NH1  1 
ATOM   1280 N  NH2  . ARG   A 1 166 ? -38.987 -22.296 32.483 1.00 21.02 ? 169  ARG   A NH2  1 
ATOM   1281 N  N    . GLY   A 1 167 ? -36.332 -27.223 25.477 1.00 15.95 ? 170  GLY   A N    1 
ATOM   1282 C  CA   . GLY   A 1 167 ? -35.390 -28.152 24.873 1.00 13.18 ? 170  GLY   A CA   1 
ATOM   1283 C  C    . GLY   A 1 167 ? -35.021 -29.287 25.819 1.00 13.46 ? 170  GLY   A C    1 
ATOM   1284 O  O    . GLY   A 1 167 ? -35.599 -29.460 26.897 1.00 15.16 ? 170  GLY   A O    1 
ATOM   1285 N  N    . ASN   A 1 168 ? -34.020 -30.066 25.393 1.00 11.57 ? 171  ASN   A N    1 
ATOM   1286 C  CA   . ASN   A 1 168 ? -33.450 -31.162 26.187 1.00 10.54 ? 171  ASN   A CA   1 
ATOM   1287 C  C    . ASN   A 1 168 ? -34.473 -32.250 26.508 1.00 12.63 ? 171  ASN   A C    1 
ATOM   1288 O  O    . ASN   A 1 168 ? -34.339 -32.929 27.530 1.00 12.99 ? 171  ASN   A O    1 
ATOM   1289 C  CB   . ASN   A 1 168 ? -32.836 -30.648 27.492 1.00 12.27 ? 171  ASN   A CB   1 
ATOM   1290 C  CG   . ASN   A 1 168 ? -31.594 -29.825 27.263 1.00 15.70 ? 171  ASN   A CG   1 
ATOM   1291 O  OD1  . ASN   A 1 168 ? -30.988 -29.887 26.194 1.00 13.49 ? 171  ASN   A OD1  1 
ATOM   1292 N  ND2  . ASN   A 1 168 ? -31.214 -29.037 28.260 1.00 19.54 ? 171  ASN   A ND2  1 
ATOM   1293 N  N    . TRP   A 1 169 ? -35.494 -32.426 25.649 1.00 12.14 ? 172  TRP   A N    1 
ATOM   1294 C  CA   . TRP   A 1 169 ? -36.493 -33.475 25.871 1.00 10.23 ? 172  TRP   A CA   1 
ATOM   1295 C  C    . TRP   A 1 169 ? -35.848 -34.855 25.975 1.00 11.03 ? 172  TRP   A C    1 
ATOM   1296 O  O    . TRP   A 1 169 ? -36.241 -35.664 26.824 1.00 14.12 ? 172  TRP   A O    1 
ATOM   1297 C  CB   . TRP   A 1 169 ? -37.551 -33.453 24.759 1.00 12.13 ? 172  TRP   A CB   1 
ATOM   1298 C  CG   . TRP   A 1 169 ? -37.933 -32.042 24.416 1.00 13.22 ? 172  TRP   A CG   1 
ATOM   1299 C  CD1  . TRP   A 1 169 ? -37.730 -31.398 23.227 1.00 14.03 ? 172  TRP   A CD1  1 
ATOM   1300 C  CD2  . TRP   A 1 169 ? -38.515 -31.080 25.305 1.00 13.19 ? 172  TRP   A CD2  1 
ATOM   1301 N  NE1  . TRP   A 1 169 ? -38.182 -30.093 23.317 1.00 13.58 ? 172  TRP   A NE1  1 
ATOM   1302 C  CE2  . TRP   A 1 169 ? -38.655 -29.873 24.583 1.00 14.57 ? 172  TRP   A CE2  1 
ATOM   1303 C  CE3  . TRP   A 1 169 ? -38.941 -31.124 26.644 1.00 12.95 ? 172  TRP   A CE3  1 
ATOM   1304 C  CZ2  . TRP   A 1 169 ? -39.217 -28.718 25.149 1.00 15.72 ? 172  TRP   A CZ2  1 
ATOM   1305 C  CZ3  . TRP   A 1 169 ? -39.480 -29.972 27.211 1.00 16.28 ? 172  TRP   A CZ3  1 
ATOM   1306 C  CH2  . TRP   A 1 169 ? -39.605 -28.787 26.466 1.00 16.93 ? 172  TRP   A CH2  1 
ATOM   1307 N  N    . GLY   A 1 170 ? -34.851 -35.140 25.135 1.00 12.04 ? 173  GLY   A N    1 
ATOM   1308 C  CA   . GLY   A 1 170 ? -34.193 -36.441 25.202 1.00 12.19 ? 173  GLY   A CA   1 
ATOM   1309 C  C    . GLY   A 1 170 ? -33.441 -36.673 26.499 1.00 11.55 ? 173  GLY   A C    1 
ATOM   1310 O  O    . GLY   A 1 170 ? -33.382 -37.805 26.992 1.00 12.89 ? 173  GLY   A O    1 
ATOM   1311 N  N    . HIS   A 1 171 ? -32.838 -35.617 27.068 1.00 12.02 ? 174  HIS   A N    1 
ATOM   1312 C  CA   . HIS   A 1 171 ? -32.178 -35.771 28.370 1.00 11.68 ? 174  HIS   A CA   1 
ATOM   1313 C  C    . HIS   A 1 171 ? -33.200 -35.969 29.480 1.00 12.22 ? 174  HIS   A C    1 
ATOM   1314 O  O    . HIS   A 1 171 ? -32.962 -36.721 30.441 1.00 11.19 ? 174  HIS   A O    1 
ATOM   1315 C  CB   . HIS   A 1 171 ? -31.296 -34.562 28.695 1.00 12.72 ? 174  HIS   A CB   1 
ATOM   1316 C  CG   . HIS   A 1 171 ? -30.111 -34.389 27.794 1.00 13.49 ? 174  HIS   A CG   1 
ATOM   1317 N  ND1  . HIS   A 1 171 ? -29.239 -35.417 27.491 1.00 12.59 ? 174  HIS   A ND1  1 
ATOM   1318 C  CD2  . HIS   A 1 171 ? -29.616 -33.283 27.184 1.00 13.97 ? 174  HIS   A CD2  1 
ATOM   1319 C  CE1  . HIS   A 1 171 ? -28.276 -34.959 26.711 1.00 12.88 ? 174  HIS   A CE1  1 
ATOM   1320 N  NE2  . HIS   A 1 171 ? -28.481 -33.666 26.508 1.00 15.05 ? 174  HIS   A NE2  1 
ATOM   1321 N  N    . LEU   A 1 172 ? -34.336 -35.275 29.388 1.00 11.63 ? 175  LEU   A N    1 
ATOM   1322 C  CA   . LEU   A 1 172 ? -35.423 -35.548 30.319 1.00 11.61 ? 175  LEU   A CA   1 
ATOM   1323 C  C    . LEU   A 1 172 ? -35.904 -36.991 30.202 1.00 11.66 ? 175  LEU   A C    1 
ATOM   1324 O  O    . LEU   A 1 172 ? -36.280 -37.601 31.210 1.00 11.56 ? 175  LEU   A O    1 
ATOM   1325 C  CB   . LEU   A 1 172 ? -36.577 -34.572 30.079 1.00 10.47 ? 175  LEU   A CB   1 
ATOM   1326 C  CG   . LEU   A 1 172 ? -36.249 -33.116 30.397 1.00 12.64 ? 175  LEU   A CG   1 
ATOM   1327 C  CD1  . LEU   A 1 172 ? -37.461 -32.268 30.007 1.00 12.24 ? 175  LEU   A CD1  1 
ATOM   1328 C  CD2  . LEU   A 1 172 ? -35.953 -32.993 31.873 1.00 13.62 ? 175  LEU   A CD2  1 
ATOM   1329 N  N    . ASP   A 1 173 ? -35.871 -37.567 28.992 1.00 10.58 ? 176  ASP   A N    1 
ATOM   1330 C  CA   . ASP   A 1 173 ? -36.220 -38.980 28.831 1.00 10.60 ? 176  ASP   A CA   1 
ATOM   1331 C  C    . ASP   A 1 173 ? -35.204 -39.877 29.526 1.00 10.16 ? 176  ASP   A C    1 
ATOM   1332 O  O    . ASP   A 1 173 ? -35.564 -40.913 30.103 1.00 11.31 ? 176  ASP   A O    1 
ATOM   1333 C  CB   . ASP   A 1 173 ? -36.271 -39.335 27.343 1.00 10.64 ? 176  ASP   A CB   1 
ATOM   1334 C  CG   . ASP   A 1 173 ? -37.364 -38.598 26.604 1.00 14.40 ? 176  ASP   A CG   1 
ATOM   1335 O  OD1  . ASP   A 1 173 ? -38.352 -38.183 27.251 1.00 14.40 ? 176  ASP   A OD1  1 
ATOM   1336 O  OD2  . ASP   A 1 173 ? -37.255 -38.478 25.359 1.00 14.37 ? 176  ASP   A OD2  1 
ATOM   1337 N  N    . GLN   A 1 174 ? -33.914 -39.521 29.429 1.00 8.27  ? 177  GLN   A N    1 
ATOM   1338 C  CA   . GLN   A 1 174 ? -32.886 -40.303 30.118 1.00 10.53 ? 177  GLN   A CA   1 
ATOM   1339 C  C    . GLN   A 1 174 ? -33.116 -40.275 31.624 1.00 9.42  ? 177  GLN   A C    1 
ATOM   1340 O  O    . GLN   A 1 174 ? -33.002 -41.305 32.302 1.00 9.99  ? 177  GLN   A O    1 
ATOM   1341 C  CB   . GLN   A 1 174 ? -31.492 -39.754 29.774 1.00 8.93  ? 177  GLN   A CB   1 
ATOM   1342 C  CG   . GLN   A 1 174 ? -31.181 -39.893 28.285 1.00 8.53  ? 177  GLN   A CG   1 
ATOM   1343 C  CD   . GLN   A 1 174 ? -30.041 -39.009 27.835 1.00 13.08 ? 177  GLN   A CD   1 
ATOM   1344 O  OE1  . GLN   A 1 174 ? -29.620 -38.126 28.562 1.00 12.33 ? 177  GLN   A OE1  1 
ATOM   1345 N  NE2  . GLN   A 1 174 ? -29.575 -39.210 26.597 1.00 13.15 ? 177  GLN   A NE2  1 
ATOM   1346 N  N    . VAL   A 1 175 ? -33.491 -39.105 32.145 1.00 8.70  ? 178  VAL   A N    1 
ATOM   1347 C  CA   . VAL   A 1 175 ? -33.808 -38.981 33.573 1.00 11.23 ? 178  VAL   A CA   1 
ATOM   1348 C  C    . VAL   A 1 175 ? -35.020 -39.844 33.926 1.00 11.48 ? 178  VAL   A C    1 
ATOM   1349 O  O    . VAL   A 1 175 ? -35.048 -40.516 34.968 1.00 12.48 ? 178  VAL   A O    1 
ATOM   1350 C  CB   . VAL   A 1 175 ? -34.054 -37.506 33.943 1.00 11.45 ? 178  VAL   A CB   1 
ATOM   1351 C  CG1  . VAL   A 1 175 ? -34.614 -37.414 35.363 1.00 13.95 ? 178  VAL   A CG1  1 
ATOM   1352 C  CG2  . VAL   A 1 175 ? -32.758 -36.683 33.806 1.00 12.84 ? 178  VAL   A CG2  1 
ATOM   1353 N  N    . ALA   A 1 176 ? -36.062 -39.794 33.090 1.00 11.23 ? 179  ALA   A N    1 
ATOM   1354 C  CA   . ALA   A 1 176 ? -37.256 -40.611 33.336 1.00 10.41 ? 179  ALA   A CA   1 
ATOM   1355 C  C    . ALA   A 1 176 ? -36.910 -42.091 33.375 1.00 13.05 ? 179  ALA   A C    1 
ATOM   1356 O  O    . ALA   A 1 176 ? -37.437 -42.845 34.206 1.00 13.73 ? 179  ALA   A O    1 
ATOM   1357 C  CB   . ALA   A 1 176 ? -38.316 -40.353 32.260 1.00 13.72 ? 179  ALA   A CB   1 
ATOM   1358 N  N    . ALA   A 1 177 ? -36.036 -42.534 32.469 1.00 11.83 ? 180  ALA   A N    1 
ATOM   1359 C  CA   . ALA   A 1 177 ? -35.651 -43.941 32.474 1.00 10.67 ? 180  ALA   A CA   1 
ATOM   1360 C  C    . ALA   A 1 177 ? -34.913 -44.295 33.759 1.00 10.10 ? 180  ALA   A C    1 
ATOM   1361 O  O    . ALA   A 1 177 ? -35.115 -45.384 34.316 1.00 11.46 ? 180  ALA   A O    1 
ATOM   1362 C  CB   . ALA   A 1 177 ? -34.805 -44.261 31.240 1.00 14.25 ? 180  ALA   A CB   1 
ATOM   1363 N  N    . LEU   A 1 178 ? -34.044 -43.397 34.243 1.00 11.81 ? 181  LEU   A N    1 
ATOM   1364 C  CA   . LEU   A 1 178 ? -33.346 -43.683 35.502 1.00 11.41 ? 181  LEU   A CA   1 
ATOM   1365 C  C    . LEU   A 1 178 ? -34.305 -43.702 36.692 1.00 14.36 ? 181  LEU   A C    1 
ATOM   1366 O  O    . LEU   A 1 178 ? -34.120 -44.491 37.626 1.00 14.37 ? 181  LEU   A O    1 
ATOM   1367 C  CB   . LEU   A 1 178 ? -32.229 -42.664 35.731 1.00 11.02 ? 181  LEU   A CB   1 
ATOM   1368 C  CG   . LEU   A 1 178 ? -31.022 -42.744 34.793 1.00 11.70 ? 181  LEU   A CG   1 
ATOM   1369 C  CD1  . LEU   A 1 178 ? -30.123 -41.552 34.999 1.00 11.94 ? 181  LEU   A CD1  1 
ATOM   1370 C  CD2  . LEU   A 1 178 ? -30.235 -44.046 35.000 1.00 12.46 ? 181  LEU   A CD2  1 
ATOM   1371 N  N    . ARG   A 1 179 ? -35.327 -42.832 36.694 1.00 14.00 ? 182  ARG   A N    1 
ATOM   1372 C  CA   . ARG   A 1 179 ? -36.327 -42.922 37.754 1.00 14.34 ? 182  ARG   A CA   1 
ATOM   1373 C  C    . ARG   A 1 179 ? -37.085 -44.244 37.667 1.00 12.00 ? 182  ARG   A C    1 
ATOM   1374 O  O    . ARG   A 1 179 ? -37.406 -44.856 38.696 1.00 13.76 ? 182  ARG   A O    1 
ATOM   1375 C  CB   . ARG   A 1 179 ? -37.326 -41.759 37.698 1.00 14.86 ? 182  ARG   A CB   1 
ATOM   1376 C  CG   . ARG   A 1 179 ? -36.724 -40.376 37.877 1.00 21.51 ? 182  ARG   A CG   1 
ATOM   1377 C  CD   . ARG   A 1 179 ? -37.825 -39.279 37.959 1.00 22.95 ? 182  ARG   A CD   1 
ATOM   1378 N  NE   . ARG   A 1 179 ? -37.260 -37.936 37.844 1.00 34.93 ? 182  ARG   A NE   1 
ATOM   1379 C  CZ   . ARG   A 1 179 ? -36.651 -37.271 38.820 1.00 41.65 ? 182  ARG   A CZ   1 
ATOM   1380 N  NH1  . ARG   A 1 179 ? -36.535 -37.786 40.041 1.00 41.34 ? 182  ARG   A NH1  1 
ATOM   1381 N  NH2  . ARG   A 1 179 ? -36.128 -36.063 38.561 1.00 28.36 ? 182  ARG   A NH2  1 
ATOM   1382 N  N    . TRP   A 1 180 ? -37.375 -44.701 36.448 1.00 10.38 ? 183  TRP   A N    1 
ATOM   1383 C  CA   . TRP   A 1 180 ? -38.021 -45.994 36.300 1.00 11.71 ? 183  TRP   A CA   1 
ATOM   1384 C  C    . TRP   A 1 180 ? -37.148 -47.099 36.879 1.00 13.53 ? 183  TRP   A C    1 
ATOM   1385 O  O    . TRP   A 1 180 ? -37.642 -48.002 37.565 1.00 12.70 ? 183  TRP   A O    1 
ATOM   1386 C  CB   . TRP   A 1 180 ? -38.343 -46.269 34.823 1.00 13.52 ? 183  TRP   A CB   1 
ATOM   1387 C  CG   . TRP   A 1 180 ? -39.122 -47.546 34.631 1.00 14.34 ? 183  TRP   A CG   1 
ATOM   1388 C  CD1  . TRP   A 1 180 ? -40.482 -47.670 34.483 1.00 15.64 ? 183  TRP   A CD1  1 
ATOM   1389 C  CD2  . TRP   A 1 180 ? -38.591 -48.878 34.582 1.00 15.04 ? 183  TRP   A CD2  1 
ATOM   1390 N  NE1  . TRP   A 1 180 ? -40.821 -48.997 34.356 1.00 15.21 ? 183  TRP   A NE1  1 
ATOM   1391 C  CE2  . TRP   A 1 180 ? -39.680 -49.756 34.405 1.00 15.11 ? 183  TRP   A CE2  1 
ATOM   1392 C  CE3  . TRP   A 1 180 ? -37.298 -49.410 34.678 1.00 14.47 ? 183  TRP   A CE3  1 
ATOM   1393 C  CZ2  . TRP   A 1 180 ? -39.519 -51.134 34.323 1.00 16.25 ? 183  TRP   A CZ2  1 
ATOM   1394 C  CZ3  . TRP   A 1 180 ? -37.134 -50.774 34.592 1.00 13.84 ? 183  TRP   A CZ3  1 
ATOM   1395 C  CH2  . TRP   A 1 180 ? -38.244 -51.629 34.414 1.00 13.95 ? 183  TRP   A CH2  1 
ATOM   1396 N  N    . VAL   A 1 181 ? -35.842 -47.037 36.614 1.00 12.69 ? 184  VAL   A N    1 
ATOM   1397 C  CA   . VAL   A 1 181 ? -34.919 -48.032 37.148 1.00 12.59 ? 184  VAL   A CA   1 
ATOM   1398 C  C    . VAL   A 1 181 ? -34.952 -48.017 38.673 1.00 13.78 ? 184  VAL   A C    1 
ATOM   1399 O  O    . VAL   A 1 181 ? -35.053 -49.068 39.315 1.00 14.47 ? 184  VAL   A O    1 
ATOM   1400 C  CB   . VAL   A 1 181 ? -33.497 -47.779 36.604 1.00 13.13 ? 184  VAL   A CB   1 
ATOM   1401 C  CG1  . VAL   A 1 181 ? -32.451 -48.508 37.465 1.00 13.53 ? 184  VAL   A CG1  1 
ATOM   1402 C  CG2  . VAL   A 1 181 ? -33.423 -48.214 35.130 1.00 13.93 ? 184  VAL   A CG2  1 
ATOM   1403 N  N    . GLN   A 1 182 ? -34.879 -46.823 39.267 1.00 14.73 ? 185  GLN   A N    1 
ATOM   1404 C  CA   . GLN   A 1 182 ? -35.007 -46.690 40.720 1.00 16.74 ? 185  GLN   A CA   1 
ATOM   1405 C  C    . GLN   A 1 182 ? -36.253 -47.410 41.228 1.00 17.82 ? 185  GLN   A C    1 
ATOM   1406 O  O    . GLN   A 1 182 ? -36.191 -48.190 42.185 1.00 20.13 ? 185  GLN   A O    1 
ATOM   1407 C  CB   . GLN   A 1 182 ? -35.056 -45.210 41.104 1.00 15.20 ? 185  GLN   A CB   1 
ATOM   1408 C  CG   . GLN   A 1 182 ? -33.725 -44.510 41.335 1.00 22.13 ? 185  GLN   A CG   1 
ATOM   1409 C  CD   . GLN   A 1 182 ? -32.666 -45.379 42.010 1.00 24.74 ? 185  GLN   A CD   1 
ATOM   1410 O  OE1  . GLN   A 1 182 ? -31.724 -45.856 41.370 1.00 20.36 ? 185  GLN   A OE1  1 
ATOM   1411 N  NE2  . GLN   A 1 182 ? -32.796 -45.544 43.321 1.00 23.57 ? 185  GLN   A NE2  1 
ATOM   1412 N  N    . ASP   A 1 183 ? -37.394 -47.179 40.577 1.00 15.18 ? 186  ASP   A N    1 
ATOM   1413 C  CA   . ASP   A 1 183 ? -38.652 -47.727 41.093 1.00 16.42 ? 186  ASP   A CA   1 
ATOM   1414 C  C    . ASP   A 1 183 ? -38.869 -49.207 40.784 1.00 21.32 ? 186  ASP   A C    1 
ATOM   1415 O  O    . ASP   A 1 183 ? -39.710 -49.835 41.437 1.00 20.28 ? 186  ASP   A O    1 
ATOM   1416 C  CB   . ASP   A 1 183 ? -39.855 -46.941 40.553 1.00 19.85 ? 186  ASP   A CB   1 
ATOM   1417 C  CG   . ASP   A 1 183 ? -39.790 -45.460 40.859 1.00 27.86 ? 186  ASP   A CG   1 
ATOM   1418 O  OD1  . ASP   A 1 183 ? -39.152 -45.094 41.872 1.00 28.61 ? 186  ASP   A OD1  1 
ATOM   1419 O  OD2  . ASP   A 1 183 ? -40.424 -44.664 40.113 1.00 28.35 ? 186  ASP   A OD2  1 
ATOM   1420 N  N    . ASN   A 1 184 ? -38.165 -49.785 39.806 1.00 17.25 ? 187  ASN   A N    1 
ATOM   1421 C  CA   . ASN   A 1 184 ? -38.525 -51.115 39.323 1.00 13.23 ? 187  ASN   A CA   1 
ATOM   1422 C  C    . ASN   A 1 184 ? -37.401 -52.141 39.257 1.00 14.60 ? 187  ASN   A C    1 
ATOM   1423 O  O    . ASN   A 1 184 ? -37.707 -53.333 39.182 1.00 15.04 ? 187  ASN   A O    1 
ATOM   1424 C  CB   . ASN   A 1 184 ? -39.133 -51.016 37.919 1.00 15.05 ? 187  ASN   A CB   1 
ATOM   1425 C  CG   . ASN   A 1 184 ? -40.486 -50.322 37.918 1.00 20.39 ? 187  ASN   A CG   1 
ATOM   1426 O  OD1  . ASN   A 1 184 ? -41.517 -50.962 38.098 1.00 20.14 ? 187  ASN   A OD1  1 
ATOM   1427 N  ND2  . ASN   A 1 184 ? -40.479 -49.009 37.739 1.00 17.89 ? 187  ASN   A ND2  1 
ATOM   1428 N  N    . ILE   A 1 185 ? -36.131 -51.744 39.233 1.00 14.32 ? 188  ILE   A N    1 
ATOM   1429 C  CA   . ILE   A 1 185 ? -35.098 -52.711 38.871 1.00 15.11 ? 188  ILE   A CA   1 
ATOM   1430 C  C    . ILE   A 1 185 ? -34.922 -53.817 39.912 1.00 15.08 ? 188  ILE   A C    1 
ATOM   1431 O  O    . ILE   A 1 185 ? -34.469 -54.916 39.560 1.00 14.70 ? 188  ILE   A O    1 
ATOM   1432 C  CB   . ILE   A 1 185 ? -33.770 -51.973 38.574 1.00 14.28 ? 188  ILE   A CB   1 
ATOM   1433 C  CG1  . ILE   A 1 185 ? -32.904 -52.832 37.658 1.00 14.36 ? 188  ILE   A CG1  1 
ATOM   1434 C  CG2  . ILE   A 1 185 ? -33.030 -51.567 39.851 1.00 14.25 ? 188  ILE   A CG2  1 
ATOM   1435 C  CD1  . ILE   A 1 185 ? -33.460 -52.928 36.228 1.00 14.50 ? 188  ILE   A CD1  1 
ATOM   1436 N  N    . ALA   A 1 186 ? -35.285 -53.577 41.179 1.00 16.07 ? 189  ALA   A N    1 
ATOM   1437 C  CA   . ALA   A 1 186 ? -35.225 -54.656 42.170 1.00 17.76 ? 189  ALA   A CA   1 
ATOM   1438 C  C    . ALA   A 1 186 ? -36.077 -55.866 41.767 1.00 19.66 ? 189  ALA   A C    1 
ATOM   1439 O  O    . ALA   A 1 186 ? -35.731 -57.005 42.102 1.00 18.14 ? 189  ALA   A O    1 
ATOM   1440 C  CB   . ALA   A 1 186 ? -35.641 -54.133 43.544 1.00 18.36 ? 189  ALA   A CB   1 
ATOM   1441 N  N    . SER   A 1 187 ? -37.170 -55.660 41.024 1.00 18.22 ? 190  SER   A N    1 
ATOM   1442 C  CA   . SER   A 1 187 ? -37.955 -56.807 40.569 1.00 20.09 ? 190  SER   A CA   1 
ATOM   1443 C  C    . SER   A 1 187 ? -37.217 -57.642 39.531 1.00 20.68 ? 190  SER   A C    1 
ATOM   1444 O  O    . SER   A 1 187 ? -37.597 -58.792 39.296 1.00 17.40 ? 190  SER   A O    1 
ATOM   1445 C  CB   . SER   A 1 187 ? -39.302 -56.349 39.997 1.00 24.23 ? 190  SER   A CB   1 
ATOM   1446 O  OG   . SER   A 1 187 ? -39.939 -55.442 40.872 1.00 26.08 ? 190  SER   A OG   1 
ATOM   1447 N  N    . PHE   A 1 188 ? -36.161 -57.099 38.919 1.00 18.59 ? 191  PHE   A N    1 
ATOM   1448 C  CA   . PHE   A 1 188 ? -35.349 -57.827 37.957 1.00 18.62 ? 191  PHE   A CA   1 
ATOM   1449 C  C    . PHE   A 1 188 ? -34.036 -58.309 38.562 1.00 17.07 ? 191  PHE   A C    1 
ATOM   1450 O  O    . PHE   A 1 188 ? -33.121 -58.681 37.828 1.00 17.82 ? 191  PHE   A O    1 
ATOM   1451 C  CB   . PHE   A 1 188 ? -35.075 -56.971 36.713 1.00 17.17 ? 191  PHE   A CB   1 
ATOM   1452 C  CG   . PHE   A 1 188 ? -36.321 -56.545 35.980 1.00 16.32 ? 191  PHE   A CG   1 
ATOM   1453 C  CD1  . PHE   A 1 188 ? -37.082 -55.476 36.428 1.00 16.52 ? 191  PHE   A CD1  1 
ATOM   1454 C  CD2  . PHE   A 1 188 ? -36.745 -57.241 34.861 1.00 15.31 ? 191  PHE   A CD2  1 
ATOM   1455 C  CE1  . PHE   A 1 188 ? -38.256 -55.109 35.756 1.00 18.07 ? 191  PHE   A CE1  1 
ATOM   1456 C  CE2  . PHE   A 1 188 ? -37.904 -56.896 34.191 1.00 18.21 ? 191  PHE   A CE2  1 
ATOM   1457 C  CZ   . PHE   A 1 188 ? -38.667 -55.820 34.632 1.00 16.25 ? 191  PHE   A CZ   1 
ATOM   1458 N  N    . GLY   A 1 189 ? -33.921 -58.295 39.883 1.00 17.47 ? 192  GLY   A N    1 
ATOM   1459 C  CA   . GLY   A 1 189 ? -32.726 -58.761 40.537 1.00 19.36 ? 192  GLY   A CA   1 
ATOM   1460 C  C    . GLY   A 1 189 ? -31.637 -57.726 40.662 1.00 19.33 ? 192  GLY   A C    1 
ATOM   1461 O  O    . GLY   A 1 189 ? -30.505 -58.084 41.006 1.00 18.82 ? 192  GLY   A O    1 
ATOM   1462 N  N    . GLY   A 1 190 ? -31.947 -56.455 40.404 1.00 17.07 ? 193  GLY   A N    1 
ATOM   1463 C  CA   . GLY   A 1 190 ? -30.969 -55.394 40.440 1.00 17.59 ? 193  GLY   A CA   1 
ATOM   1464 C  C    . GLY   A 1 190 ? -31.033 -54.622 41.739 1.00 20.53 ? 193  GLY   A C    1 
ATOM   1465 O  O    . GLY   A 1 190 ? -32.041 -54.613 42.430 1.00 20.14 ? 193  GLY   A O    1 
ATOM   1466 N  N    . ASN   A 1 191 ? -29.930 -53.959 42.060 1.00 16.95 ? 194  ASN   A N    1 
ATOM   1467 C  CA   . ASN   A 1 191 ? -29.819 -53.138 43.256 1.00 18.42 ? 194  ASN   A CA   1 
ATOM   1468 C  C    . ASN   A 1 191 ? -30.053 -51.671 42.911 1.00 17.40 ? 194  ASN   A C    1 
ATOM   1469 O  O    . ASN   A 1 191 ? -29.166 -51.038 42.309 1.00 17.80 ? 194  ASN   A O    1 
ATOM   1470 C  CB   . ASN   A 1 191 ? -28.429 -53.338 43.871 1.00 20.05 ? 194  ASN   A CB   1 
ATOM   1471 C  CG   . ASN   A 1 191 ? -28.209 -52.519 45.117 1.00 24.80 ? 194  ASN   A CG   1 
ATOM   1472 O  OD1  . ASN   A 1 191 ? -29.126 -51.894 45.640 1.00 23.01 ? 194  ASN   A OD1  1 
ATOM   1473 N  ND2  . ASN   A 1 191 ? -26.972 -52.525 45.612 1.00 24.33 ? 194  ASN   A ND2  1 
ATOM   1474 N  N    . PRO   A 1 192 ? -31.197 -51.069 43.282 1.00 17.85 ? 195  PRO   A N    1 
ATOM   1475 C  CA   . PRO   A 1 192 ? -31.400 -49.647 42.957 1.00 19.18 ? 195  PRO   A CA   1 
ATOM   1476 C  C    . PRO   A 1 192 ? -30.441 -48.725 43.690 1.00 18.35 ? 195  PRO   A C    1 
ATOM   1477 O  O    . PRO   A 1 192 ? -30.297 -47.566 43.287 1.00 19.01 ? 195  PRO   A O    1 
ATOM   1478 C  CB   . PRO   A 1 192 ? -32.861 -49.381 43.360 1.00 17.26 ? 195  PRO   A CB   1 
ATOM   1479 C  CG   . PRO   A 1 192 ? -33.168 -50.419 44.373 1.00 22.54 ? 195  PRO   A CG   1 
ATOM   1480 C  CD   . PRO   A 1 192 ? -32.325 -51.632 44.049 1.00 19.11 ? 195  PRO   A CD   1 
ATOM   1481 N  N    . GLY   A 1 193 ? -29.779 -49.191 44.748 1.00 16.31 ? 196  GLY   A N    1 
ATOM   1482 C  CA   . GLY   A 1 193 ? -28.737 -48.398 45.367 1.00 19.70 ? 196  GLY   A CA   1 
ATOM   1483 C  C    . GLY   A 1 193 ? -27.356 -48.509 44.740 1.00 22.35 ? 196  GLY   A C    1 
ATOM   1484 O  O    . GLY   A 1 193 ? -26.397 -47.945 45.279 1.00 23.30 ? 196  GLY   A O    1 
ATOM   1485 N  N    . SER   A 1 194 ? -27.210 -49.216 43.603 1.00 20.04 ? 197  SER   A N    1 
ATOM   1486 C  CA   . SER   A 1 194 ? -25.937 -49.290 42.865 1.00 17.83 ? 197  SER   A CA   1 
ATOM   1487 C  C    . SER   A 1 194 ? -26.231 -49.232 41.367 1.00 16.91 ? 197  SER   A C    1 
ATOM   1488 O  O    . SER   A 1 194 ? -26.248 -50.250 40.679 1.00 16.34 ? 197  SER   A O    1 
ATOM   1489 C  CB   . SER   A 1 194 ? -25.140 -50.550 43.210 1.00 24.49 ? 197  SER   A CB   1 
ATOM   1490 O  OG   . SER   A 1 194 ? -23.824 -50.441 42.664 1.00 24.95 ? 197  SER   A OG   1 
ATOM   1491 N  N    . VAL   A 1 195 ? -26.442 -48.025 40.850 1.00 16.32 ? 198  VAL   A N    1 
ATOM   1492 C  CA   . VAL   A 1 195 ? -26.725 -47.827 39.434 1.00 15.93 ? 198  VAL   A CA   1 
ATOM   1493 C  C    . VAL   A 1 195 ? -25.565 -47.059 38.817 1.00 13.70 ? 198  VAL   A C    1 
ATOM   1494 O  O    . VAL   A 1 195 ? -25.220 -45.963 39.273 1.00 14.52 ? 198  VAL   A O    1 
ATOM   1495 C  CB   . VAL   A 1 195 ? -28.060 -47.090 39.219 1.00 17.96 ? 198  VAL   A CB   1 
ATOM   1496 C  CG1  . VAL   A 1 195 ? -28.263 -46.774 37.731 1.00 16.26 ? 198  VAL   A CG1  1 
ATOM   1497 C  CG2  . VAL   A 1 195 ? -29.227 -47.944 39.763 1.00 15.15 ? 198  VAL   A CG2  1 
ATOM   1498 N  N    . THR   A 1 196 ? -24.986 -47.622 37.761 1.00 13.17 ? 199  THR   A N    1 
ATOM   1499 C  CA   . THR   A 1 196 ? -23.903 -46.993 37.017 1.00 14.09 ? 199  THR   A CA   1 
ATOM   1500 C  C    . THR   A 1 196 ? -24.467 -46.592 35.665 1.00 12.58 ? 199  THR   A C    1 
ATOM   1501 O  O    . THR   A 1 196 ? -25.028 -47.438 34.981 1.00 13.58 ? 199  THR   A O    1 
ATOM   1502 C  CB   . THR   A 1 196 ? -22.747 -47.979 36.824 1.00 15.27 ? 199  THR   A CB   1 
ATOM   1503 O  OG1  . THR   A 1 196 ? -22.181 -48.295 38.100 1.00 15.68 ? 199  THR   A OG1  1 
ATOM   1504 C  CG2  . THR   A 1 196 ? -21.655 -47.388 35.907 1.00 13.58 ? 199  THR   A CG2  1 
ATOM   1505 N  N    . ILE   A 1 197 ? -24.279 -45.353 35.269 1.00 11.44 ? 200  ILE   A N    1 
ATOM   1506 C  CA   . ILE   A 1 197 ? -24.673 -44.920 33.955 1.00 11.19 ? 200  ILE   A CA   1 
ATOM   1507 C  C    . ILE   A 1 197 ? -23.436 -44.877 33.058 1.00 11.52 ? 200  ILE   A C    1 
ATOM   1508 O  O    . ILE   A 1 197 ? -22.405 -44.392 33.435 1.00 12.72 ? 200  ILE   A O    1 
ATOM   1509 C  CB   . ILE   A 1 197 ? -25.373 -43.542 33.949 1.00 10.83 ? 200  ILE   A CB   1 
ATOM   1510 C  CG1  . ILE   A 1 197 ? -24.551 -42.491 34.682 1.00 11.32 ? 200  ILE   A CG1  1 
ATOM   1511 C  CG2  . ILE   A 1 197 ? -26.750 -43.645 34.569 1.00 12.26 ? 200  ILE   A CG2  1 
ATOM   1512 C  CD1  . ILE   A 1 197 ? -25.144 -41.111 34.584 1.00 11.69 ? 200  ILE   A CD1  1 
ATOM   1513 N  N    . PHE   A 1 198 ? -23.572 -45.454 31.894 1.00 11.04 ? 201  PHE   A N    1 
ATOM   1514 C  CA   . PHE   A 1 198 ? -22.489 -45.449 30.960 1.00 12.48 ? 201  PHE   A CA   1 
ATOM   1515 C  C    . PHE   A 1 198 ? -22.965 -45.196 29.545 1.00 13.19 ? 201  PHE   A C    1 
ATOM   1516 O  O    . PHE   A 1 198 ? -24.047 -45.541 29.185 1.00 10.61 ? 201  PHE   A O    1 
ATOM   1517 C  CB   . PHE   A 1 198 ? -21.552 -46.674 31.083 1.00 10.39 ? 201  PHE   A CB   1 
ATOM   1518 C  CG   . PHE   A 1 198 ? -22.125 -48.017 30.724 1.00 11.91 ? 201  PHE   A CG   1 
ATOM   1519 C  CD1  . PHE   A 1 198 ? -23.393 -48.403 31.083 1.00 9.87  ? 201  PHE   A CD1  1 
ATOM   1520 C  CD2  . PHE   A 1 198 ? -21.311 -48.944 30.092 1.00 11.88 ? 201  PHE   A CD2  1 
ATOM   1521 C  CE1  . PHE   A 1 198 ? -23.861 -49.663 30.770 1.00 10.43 ? 201  PHE   A CE1  1 
ATOM   1522 C  CE2  . PHE   A 1 198 ? -21.770 -50.201 29.779 1.00 12.65 ? 201  PHE   A CE2  1 
ATOM   1523 C  CZ   . PHE   A 1 198 ? -23.055 -50.562 30.117 1.00 11.11 ? 201  PHE   A CZ   1 
ATOM   1524 N  N    . GLY   A 1 199 ? -22.093 -44.567 28.795 1.00 10.53 ? 202  GLY   A N    1 
ATOM   1525 C  CA   . GLY   A 1 199 ? -22.418 -44.238 27.434 1.00 12.85 ? 202  GLY   A CA   1 
ATOM   1526 C  C    . GLY   A 1 199 ? -21.250 -43.813 26.561 1.00 11.22 ? 202  GLY   A C    1 
ATOM   1527 O  O    . GLY   A 1 199 ? -20.225 -43.450 27.057 1.00 12.42 ? 202  GLY   A O    1 
ATOM   1528 N  N    . GLU   A 1 200 ? -21.470 -43.839 25.253 1.00 14.07 ? 203  GLU   A N    1 
ATOM   1529 C  CA   . GLU   A 1 200 ? -20.381 -43.541 24.334 1.00 14.13 ? 203  GLU   A CA   1 
ATOM   1530 C  C    . GLU   A 1 200 ? -20.827 -42.428 23.391 1.00 13.47 ? 203  GLU   A C    1 
ATOM   1531 O  O    . GLU   A 1 200 ? -22.002 -42.369 23.011 1.00 11.93 ? 203  GLU   A O    1 
ATOM   1532 C  CB   . GLU   A 1 200 ? -20.008 -44.775 23.536 1.00 14.01 ? 203  GLU   A CB   1 
ATOM   1533 C  CG   . GLU   A 1 200 ? -18.768 -44.611 22.699 1.00 17.73 ? 203  GLU   A CG   1 
ATOM   1534 C  CD   . GLU   A 1 200 ? -19.101 -44.322 21.262 1.00 20.75 ? 203  GLU   A CD   1 
ATOM   1535 O  OE1  . GLU   A 1 200 ? -20.307 -44.375 20.899 1.00 20.61 ? 203  GLU   A OE1  1 
ATOM   1536 O  OE2  . GLU   A 1 200 ? -18.150 -44.096 20.482 1.00 21.55 ? 203  GLU   A OE2  1 
ATOM   1537 N  N    . SER   A 1 201 ? -19.895 -41.537 23.036 1.00 13.14 ? 204  SER   A N    1 
ATOM   1538 C  CA   . SER   A 1 201 ? -20.127 -40.451 22.073 1.00 13.53 ? 204  SER   A CA   1 
ATOM   1539 C  C    . SER   A 1 201 ? -21.203 -39.546 22.665 1.00 12.74 ? 204  SER   A C    1 
ATOM   1540 O  O    . SER   A 1 201 ? -21.018 -39.076 23.803 1.00 14.27 ? 204  SER   A O    1 
ATOM   1541 C  CB   . SER   A 1 201 ? -20.429 -41.051 20.694 1.00 14.94 ? 204  SER   A CB   1 
ATOM   1542 O  OG   . SER   A 1 201 ? -20.348 -40.088 19.640 1.00 17.84 ? 204  SER   A OG   1 
ATOM   1543 N  N    . ALA   A 1 202 ? -22.316 -39.287 21.976 1.00 12.82 ? 205  ALA   A N    1 
ATOM   1544 C  CA   . ALA   A 1 202 ? -23.363 -38.466 22.580 1.00 14.22 ? 205  ALA   A CA   1 
ATOM   1545 C  C    . ALA   A 1 202 ? -23.901 -39.104 23.856 1.00 14.20 ? 205  ALA   A C    1 
ATOM   1546 O  O    . ALA   A 1 202 ? -24.339 -38.390 24.771 1.00 12.55 ? 205  ALA   A O    1 
ATOM   1547 C  CB   . ALA   A 1 202 ? -24.494 -38.221 21.582 1.00 13.52 ? 205  ALA   A CB   1 
ATOM   1548 N  N    . GLY   A 1 203 ? -23.813 -40.435 23.967 1.00 10.99 ? 206  GLY   A N    1 
ATOM   1549 C  CA   . GLY   A 1 203 ? -24.208 -41.085 25.210 1.00 11.08 ? 206  GLY   A CA   1 
ATOM   1550 C  C    . GLY   A 1 203 ? -23.268 -40.747 26.348 1.00 10.56 ? 206  GLY   A C    1 
ATOM   1551 O  O    . GLY   A 1 203 ? -23.699 -40.562 27.487 1.00 13.37 ? 206  GLY   A O    1 
ATOM   1552 N  N    . GLY   A 1 204 ? -21.967 -40.653 26.055 1.00 14.02 ? 207  GLY   A N    1 
ATOM   1553 C  CA   . GLY   A 1 204 ? -21.023 -40.168 27.049 1.00 11.45 ? 207  GLY   A CA   1 
ATOM   1554 C  C    . GLY   A 1 204 ? -21.246 -38.703 27.379 1.00 11.82 ? 207  GLY   A C    1 
ATOM   1555 O  O    . GLY   A 1 204 ? -21.178 -38.301 28.548 1.00 10.73 ? 207  GLY   A O    1 
ATOM   1556 N  N    . GLU   A 1 205 ? -21.591 -37.894 26.373 1.00 11.50 ? 208  GLU   A N    1 
ATOM   1557 C  CA   . GLU   A 1 205 ? -21.956 -36.516 26.704 1.00 10.19 ? 208  GLU   A CA   1 
ATOM   1558 C  C    . GLU   A 1 205 ? -23.198 -36.511 27.587 1.00 12.09 ? 208  GLU   A C    1 
ATOM   1559 O  O    . GLU   A 1 205 ? -23.296 -35.721 28.543 1.00 13.37 ? 208  GLU   A O    1 
ATOM   1560 C  CB   . GLU   A 1 205 ? -22.193 -35.714 25.427 1.00 12.10 ? 208  GLU   A CB   1 
ATOM   1561 C  CG   . GLU   A 1 205 ? -22.521 -34.204 25.618 1.00 11.73 ? 208  GLU   A CG   1 
ATOM   1562 C  CD   . GLU   A 1 205 ? -24.022 -33.867 25.517 1.00 13.76 ? 208  GLU   A CD   1 
ATOM   1563 O  OE1  . GLU   A 1 205 ? -24.870 -34.788 25.396 1.00 14.00 ? 208  GLU   A OE1  1 
ATOM   1564 O  OE2  . GLU   A 1 205 ? -24.354 -32.656 25.517 1.00 14.28 ? 208  GLU   A OE2  1 
ATOM   1565 N  N    . SER   A 1 206 ? -24.133 -37.445 27.334 1.00 12.32 ? 209  SER   A N    1 
ATOM   1566 C  CA   . SER   A 1 206 ? -25.352 -37.435 28.138 1.00 10.93 ? 209  SER   A CA   1 
ATOM   1567 C  C    . SER   A 1 206 ? -25.024 -37.793 29.577 1.00 11.27 ? 209  SER   A C    1 
ATOM   1568 O  O    . SER   A 1 206 ? -25.534 -37.157 30.513 1.00 11.73 ? 209  SER   A O    1 
ATOM   1569 C  CB   . SER   A 1 206 ? -26.396 -38.405 27.569 1.00 13.10 ? 209  SER   A CB   1 
ATOM   1570 O  OG   . SER   A 1 206 ? -26.835 -37.992 26.287 1.00 11.38 ? 209  SER   A OG   1 
ATOM   1571 N  N    . VAL   A 1 207 ? -24.099 -38.748 29.767 1.00 11.01 ? 210  VAL   A N    1 
ATOM   1572 C  CA   . VAL   A 1 207 ? -23.707 -39.101 31.126 1.00 10.53 ? 210  VAL   A CA   1 
ATOM   1573 C  C    . VAL   A 1 207 ? -23.145 -37.878 31.826 1.00 11.62 ? 210  VAL   A C    1 
ATOM   1574 O  O    . VAL   A 1 207 ? -23.467 -37.595 32.991 1.00 11.80 ? 210  VAL   A O    1 
ATOM   1575 C  CB   . VAL   A 1 207 ? -22.689 -40.258 31.101 1.00 9.65  ? 210  VAL   A CB   1 
ATOM   1576 C  CG1  . VAL   A 1 207 ? -21.929 -40.323 32.437 1.00 11.37 ? 210  VAL   A CG1  1 
ATOM   1577 C  CG2  . VAL   A 1 207 ? -23.385 -41.603 30.797 1.00 10.06 ? 210  VAL   A CG2  1 
ATOM   1578 N  N    . SER   A 1 208 ? -22.307 -37.119 31.109 1.00 12.42 ? 211  SER   A N    1 
ATOM   1579 C  CA   . SER   A 1 208 ? -21.670 -35.944 31.683 1.00 10.79 ? 211  SER   A CA   1 
ATOM   1580 C  C    . SER   A 1 208 ? -22.720 -34.880 32.005 1.00 13.01 ? 211  SER   A C    1 
ATOM   1581 O  O    . SER   A 1 208 ? -22.681 -34.260 33.077 1.00 13.50 ? 211  SER   A O    1 
ATOM   1582 C  CB   . SER   A 1 208 ? -20.615 -35.437 30.695 1.00 13.86 ? 211  SER   A CB   1 
ATOM   1583 O  OG   . SER   A 1 208 ? -19.919 -34.301 31.179 1.00 14.61 ? 211  SER   A OG   1 
ATOM   1584 N  N    . VAL   A 1 209 ? -23.714 -34.727 31.128 1.00 11.26 ? 212  VAL   A N    1 
ATOM   1585 C  CA   . VAL   A 1 209 ? -24.802 -33.781 31.395 1.00 14.05 ? 212  VAL   A CA   1 
ATOM   1586 C  C    . VAL   A 1 209 ? -25.586 -34.212 32.623 1.00 12.95 ? 212  VAL   A C    1 
ATOM   1587 O  O    . VAL   A 1 209 ? -26.003 -33.375 33.435 1.00 14.00 ? 212  VAL   A O    1 
ATOM   1588 C  CB   . VAL   A 1 209 ? -25.716 -33.657 30.165 1.00 12.88 ? 212  VAL   A CB   1 
ATOM   1589 C  CG1  . VAL   A 1 209 ? -27.059 -33.033 30.552 1.00 13.81 ? 212  VAL   A CG1  1 
ATOM   1590 C  CG2  . VAL   A 1 209 ? -25.021 -32.858 29.077 1.00 13.13 ? 212  VAL   A CG2  1 
ATOM   1591 N  N    . LEU   A 1 210 ? -25.790 -35.524 32.791 1.00 12.23 ? 213  LEU   A N    1 
ATOM   1592 C  CA   . LEU   A 1 210 ? -26.537 -35.950 33.967 1.00 10.75 ? 213  LEU   A CA   1 
ATOM   1593 C  C    . LEU   A 1 210 ? -25.731 -35.728 35.239 1.00 14.03 ? 213  LEU   A C    1 
ATOM   1594 O  O    . LEU   A 1 210 ? -26.315 -35.453 36.300 1.00 13.36 ? 213  LEU   A O    1 
ATOM   1595 C  CB   . LEU   A 1 210 ? -26.972 -37.405 33.836 1.00 12.32 ? 213  LEU   A CB   1 
ATOM   1596 C  CG   . LEU   A 1 210 ? -27.974 -37.696 32.711 1.00 11.86 ? 213  LEU   A CG   1 
ATOM   1597 C  CD1  . LEU   A 1 210 ? -28.092 -39.193 32.462 1.00 13.85 ? 213  LEU   A CD1  1 
ATOM   1598 C  CD2  . LEU   A 1 210 ? -29.344 -37.102 33.035 1.00 17.53 ? 213  LEU   A CD2  1 
ATOM   1599 N  N    . VAL   A 1 211 ? -24.393 -35.809 35.161 1.00 12.84 ? 214  VAL   A N    1 
ATOM   1600 C  CA   . VAL   A 1 211 ? -23.587 -35.488 36.340 1.00 13.87 ? 214  VAL   A CA   1 
ATOM   1601 C  C    . VAL   A 1 211 ? -23.776 -34.021 36.721 1.00 14.20 ? 214  VAL   A C    1 
ATOM   1602 O  O    . VAL   A 1 211 ? -23.676 -33.651 37.899 1.00 15.91 ? 214  VAL   A O    1 
ATOM   1603 C  CB   . VAL   A 1 211 ? -22.105 -35.854 36.064 1.00 12.83 ? 214  VAL   A CB   1 
ATOM   1604 C  CG1  . VAL   A 1 211 ? -21.146 -35.159 37.026 1.00 15.81 ? 214  VAL   A CG1  1 
ATOM   1605 C  CG2  . VAL   A 1 211 ? -21.911 -37.374 36.131 1.00 12.40 ? 214  VAL   A CG2  1 
ATOM   1606 N  N    . LEU   A 1 212 ? -24.099 -33.169 35.748 1.00 12.76 ? 215  LEU   A N    1 
ATOM   1607 C  CA   . LEU   A 1 212 ? -24.242 -31.732 35.964 1.00 12.71 ? 215  LEU   A CA   1 
ATOM   1608 C  C    . LEU   A 1 212 ? -25.673 -31.307 36.291 1.00 16.11 ? 215  LEU   A C    1 
ATOM   1609 O  O    . LEU   A 1 212 ? -25.910 -30.119 36.539 1.00 17.58 ? 215  LEU   A O    1 
ATOM   1610 C  CB   . LEU   A 1 212 ? -23.770 -30.983 34.712 1.00 15.02 ? 215  LEU   A CB   1 
ATOM   1611 C  CG   . LEU   A 1 212 ? -22.289 -31.188 34.411 1.00 16.33 ? 215  LEU   A CG   1 
ATOM   1612 C  CD1  . LEU   A 1 212 ? -21.997 -30.673 33.007 1.00 17.83 ? 215  LEU   A CD1  1 
ATOM   1613 C  CD2  . LEU   A 1 212 ? -21.429 -30.482 35.437 1.00 18.47 ? 215  LEU   A CD2  1 
ATOM   1614 N  N    . SER   A 1 213 ? -26.632 -32.233 36.291 1.00 15.14 ? 216  SER   A N    1 
ATOM   1615 C  CA   . SER   A 1 213 ? -28.045 -31.848 36.357 1.00 14.88 ? 216  SER   A CA   1 
ATOM   1616 C  C    . SER   A 1 213 ? -28.641 -32.104 37.730 1.00 16.86 ? 216  SER   A C    1 
ATOM   1617 O  O    . SER   A 1 213 ? -28.609 -33.246 38.211 1.00 16.15 ? 216  SER   A O    1 
ATOM   1618 C  CB   . SER   A 1 213 ? -28.874 -32.610 35.325 1.00 14.08 ? 216  SER   A CB   1 
ATOM   1619 O  OG   . SER   A 1 213 ? -30.263 -32.284 35.480 1.00 17.95 ? 216  SER   A OG   1 
ATOM   1620 N  N    . PRO   A 1 214 ? -29.298 -31.110 38.330 1.00 18.03 ? 217  PRO   A N    1 
ATOM   1621 C  CA   . PRO   A 1 214 ? -29.996 -31.366 39.601 1.00 16.76 ? 217  PRO   A CA   1 
ATOM   1622 C  C    . PRO   A 1 214 ? -31.123 -32.372 39.465 1.00 16.81 ? 217  PRO   A C    1 
ATOM   1623 O  O    . PRO   A 1 214 ? -31.480 -33.019 40.457 1.00 18.29 ? 217  PRO   A O    1 
ATOM   1624 C  CB   . PRO   A 1 214 ? -30.527 -29.983 40.006 1.00 18.74 ? 217  PRO   A CB   1 
ATOM   1625 C  CG   . PRO   A 1 214 ? -30.579 -29.179 38.734 1.00 21.18 ? 217  PRO   A CG   1 
ATOM   1626 C  CD   . PRO   A 1 214 ? -29.480 -29.728 37.842 1.00 18.45 ? 217  PRO   A CD   1 
ATOM   1627 N  N    . LEU   A 1 215 ? -31.698 -32.533 38.268 1.00 14.79 ? 218  LEU   A N    1 
ATOM   1628 C  CA   . LEU   A 1 215 ? -32.801 -33.478 38.091 1.00 16.50 ? 218  LEU   A CA   1 
ATOM   1629 C  C    . LEU   A 1 215 ? -32.358 -34.928 38.243 1.00 18.21 ? 218  LEU   A C    1 
ATOM   1630 O  O    . LEU   A 1 215 ? -33.197 -35.802 38.465 1.00 17.33 ? 218  LEU   A O    1 
ATOM   1631 C  CB   . LEU   A 1 215 ? -33.443 -33.287 36.715 1.00 14.46 ? 218  LEU   A CB   1 
ATOM   1632 C  CG   . LEU   A 1 215 ? -34.057 -31.910 36.431 1.00 19.39 ? 218  LEU   A CG   1 
ATOM   1633 C  CD1  . LEU   A 1 215 ? -34.638 -31.859 35.030 1.00 18.94 ? 218  LEU   A CD1  1 
ATOM   1634 C  CD2  . LEU   A 1 215 ? -35.112 -31.570 37.461 1.00 20.68 ? 218  LEU   A CD2  1 
ATOM   1635 N  N    . ALA   A 1 216 ? -31.064 -35.213 38.124 1.00 17.48 ? 219  ALA   A N    1 
ATOM   1636 C  CA   . ALA   A 1 216 ? -30.582 -36.583 38.222 1.00 17.48 ? 219  ALA   A CA   1 
ATOM   1637 C  C    . ALA   A 1 216 ? -30.063 -36.925 39.615 1.00 20.34 ? 219  ALA   A C    1 
ATOM   1638 O  O    . ALA   A 1 216 ? -29.456 -37.984 39.790 1.00 18.27 ? 219  ALA   A O    1 
ATOM   1639 C  CB   . ALA   A 1 216 ? -29.491 -36.834 37.181 1.00 19.30 ? 219  ALA   A CB   1 
ATOM   1640 N  N    . LYS   A 1 217 ? -30.290 -36.059 40.606 1.00 20.96 ? 220  LYS   A N    1 
ATOM   1641 C  CA   . LYS   A 1 217 ? -29.840 -36.349 41.963 1.00 25.47 ? 220  LYS   A CA   1 
ATOM   1642 C  C    . LYS   A 1 217 ? -30.424 -37.668 42.470 1.00 23.82 ? 220  LYS   A C    1 
ATOM   1643 O  O    . LYS   A 1 217 ? -31.618 -37.946 42.304 1.00 21.07 ? 220  LYS   A O    1 
ATOM   1644 C  CB   . LYS   A 1 217 ? -30.218 -35.200 42.903 1.00 29.79 ? 220  LYS   A CB   1 
ATOM   1645 C  CG   . LYS   A 1 217 ? -29.859 -35.458 44.369 1.00 34.00 ? 220  LYS   A CG   1 
ATOM   1646 C  CD   . LYS   A 1 217 ? -29.178 -34.232 44.987 1.00 42.51 ? 220  LYS   A CD   1 
ATOM   1647 C  CE   . LYS   A 1 217 ? -28.405 -34.585 46.254 1.00 41.42 ? 220  LYS   A CE   1 
ATOM   1648 N  NZ   . LYS   A 1 217 ? -27.275 -35.545 46.002 1.00 43.44 ? 220  LYS   A NZ   1 
ATOM   1649 N  N    . ASN   A 1 218 ? -29.553 -38.492 43.062 1.00 25.34 ? 221  ASN   A N    1 
ATOM   1650 C  CA   . ASN   A 1 218 ? -29.893 -39.781 43.667 1.00 24.75 ? 221  ASN   A CA   1 
ATOM   1651 C  C    . ASN   A 1 218 ? -30.388 -40.816 42.664 1.00 19.72 ? 221  ASN   A C    1 
ATOM   1652 O  O    . ASN   A 1 218 ? -30.961 -41.833 43.058 1.00 22.61 ? 221  ASN   A O    1 
ATOM   1653 C  CB   . ASN   A 1 218 ? -30.913 -39.613 44.799 1.00 32.96 ? 221  ASN   A CB   1 
ATOM   1654 C  CG   . ASN   A 1 218 ? -30.376 -38.765 45.937 1.00 34.94 ? 221  ASN   A CG   1 
ATOM   1655 O  OD1  . ASN   A 1 218 ? -29.220 -38.914 46.346 1.00 39.33 ? 221  ASN   A OD1  1 
ATOM   1656 N  ND2  . ASN   A 1 218 ? -31.204 -37.855 46.441 1.00 37.61 ? 221  ASN   A ND2  1 
ATOM   1657 N  N    . LEU   A 1 219 ? -30.167 -40.611 41.367 1.00 15.15 ? 222  LEU   A N    1 
ATOM   1658 C  CA   . LEU   A 1 219 ? -30.568 -41.602 40.379 1.00 16.86 ? 222  LEU   A CA   1 
ATOM   1659 C  C    . LEU   A 1 219 ? -29.426 -42.512 39.926 1.00 16.15 ? 222  LEU   A C    1 
ATOM   1660 O  O    . LEU   A 1 219 ? -29.679 -43.489 39.214 1.00 14.22 ? 222  LEU   A O    1 
ATOM   1661 C  CB   . LEU   A 1 219 ? -31.178 -40.915 39.153 1.00 15.91 ? 222  LEU   A CB   1 
ATOM   1662 C  CG   . LEU   A 1 219 ? -32.415 -40.055 39.455 1.00 17.59 ? 222  LEU   A CG   1 
ATOM   1663 C  CD1  . LEU   A 1 219 ? -33.025 -39.580 38.140 1.00 17.47 ? 222  LEU   A CD1  1 
ATOM   1664 C  CD2  . LEU   A 1 219 ? -33.427 -40.816 40.283 1.00 21.66 ? 222  LEU   A CD2  1 
ATOM   1665 N  N    . PHE   A 1 220 ? -28.187 -42.203 40.284 1.00 13.48 ? 223  PHE   A N    1 
ATOM   1666 C  CA   . PHE   A 1 220 ? -27.077 -43.076 39.921 1.00 15.39 ? 223  PHE   A CA   1 
ATOM   1667 C  C    . PHE   A 1 220 ? -25.931 -42.859 40.896 1.00 14.91 ? 223  PHE   A C    1 
ATOM   1668 O  O    . PHE   A 1 220 ? -25.856 -41.833 41.581 1.00 16.67 ? 223  PHE   A O    1 
ATOM   1669 C  CB   . PHE   A 1 220 ? -26.595 -42.838 38.482 1.00 14.87 ? 223  PHE   A CB   1 
ATOM   1670 C  CG   . PHE   A 1 220 ? -26.122 -41.443 38.224 1.00 15.96 ? 223  PHE   A CG   1 
ATOM   1671 C  CD1  . PHE   A 1 220 ? -27.030 -40.432 37.944 1.00 17.68 ? 223  PHE   A CD1  1 
ATOM   1672 C  CD2  . PHE   A 1 220 ? -24.768 -41.128 38.288 1.00 14.92 ? 223  PHE   A CD2  1 
ATOM   1673 C  CE1  . PHE   A 1 220 ? -26.599 -39.138 37.716 1.00 16.17 ? 223  PHE   A CE1  1 
ATOM   1674 C  CE2  . PHE   A 1 220 ? -24.328 -39.839 38.068 1.00 16.19 ? 223  PHE   A CE2  1 
ATOM   1675 C  CZ   . PHE   A 1 220 ? -25.247 -38.830 37.781 1.00 15.72 ? 223  PHE   A CZ   1 
ATOM   1676 N  N    . HIS   A 1 221 ? -25.009 -43.830 40.910 1.00 14.02 ? 224  HIS   A N    1 
ATOM   1677 C  CA   . HIS   A 1 221 ? -23.968 -43.888 41.925 1.00 17.35 ? 224  HIS   A CA   1 
ATOM   1678 C  C    . HIS   A 1 221 ? -22.561 -44.016 41.355 1.00 15.65 ? 224  HIS   A C    1 
ATOM   1679 O  O    . HIS   A 1 221 ? -21.601 -43.905 42.118 1.00 17.54 ? 224  HIS   A O    1 
ATOM   1680 C  CB   . HIS   A 1 221 ? -24.265 -45.056 42.875 1.00 16.47 ? 224  HIS   A CB   1 
ATOM   1681 C  CG   . HIS   A 1 221 ? -25.682 -45.047 43.356 1.00 20.64 ? 224  HIS   A CG   1 
ATOM   1682 N  ND1  . HIS   A 1 221 ? -26.676 -45.770 42.736 1.00 18.33 ? 224  HIS   A ND1  1 
ATOM   1683 C  CD2  . HIS   A 1 221 ? -26.286 -44.343 44.345 1.00 21.29 ? 224  HIS   A CD2  1 
ATOM   1684 C  CE1  . HIS   A 1 221 ? -27.828 -45.544 43.344 1.00 20.47 ? 224  HIS   A CE1  1 
ATOM   1685 N  NE2  . HIS   A 1 221 ? -27.619 -44.680 44.323 1.00 22.12 ? 224  HIS   A NE2  1 
ATOM   1686 N  N    . ARG   A 1 222 ? -22.417 -44.254 40.053 1.00 14.78 ? 225  ARG   A N    1 
ATOM   1687 C  CA   . ARG   A 1 222 ? -21.153 -44.211 39.334 1.00 15.82 ? 225  ARG   A CA   1 
ATOM   1688 C  C    . ARG   A 1 222 ? -21.487 -43.786 37.916 1.00 16.06 ? 225  ARG   A C    1 
ATOM   1689 O  O    . ARG   A 1 222 ? -22.619 -43.967 37.453 1.00 12.04 ? 225  ARG   A O    1 
ATOM   1690 C  CB   . ARG   A 1 222 ? -20.427 -45.570 39.290 1.00 12.60 ? 225  ARG   A CB   1 
ATOM   1691 C  CG   . ARG   A 1 222 ? -20.014 -46.179 40.625 1.00 15.79 ? 225  ARG   A CG   1 
ATOM   1692 C  CD   . ARG   A 1 222 ? -21.146 -47.060 41.155 1.00 17.04 ? 225  ARG   A CD   1 
ATOM   1693 N  NE   . ARG   A 1 222 ? -20.727 -47.917 42.255 1.00 17.62 ? 225  ARG   A NE   1 
ATOM   1694 C  CZ   . ARG   A 1 222 ? -20.433 -47.499 43.478 1.00 19.24 ? 225  ARG   A CZ   1 
ATOM   1695 N  NH1  . ARG   A 1 222 ? -20.458 -46.215 43.798 1.00 20.90 ? 225  ARG   A NH1  1 
ATOM   1696 N  NH2  . ARG   A 1 222 ? -20.076 -48.395 44.398 1.00 20.68 ? 225  ARG   A NH2  1 
ATOM   1697 N  N    . ALA   A 1 223 ? -20.492 -43.242 37.223 1.00 11.37 ? 226  ALA   A N    1 
ATOM   1698 C  CA   . ALA   A 1 223 ? -20.679 -42.773 35.857 1.00 11.23 ? 226  ALA   A CA   1 
ATOM   1699 C  C    . ALA   A 1 223 ? -19.463 -43.131 35.016 1.00 13.56 ? 226  ALA   A C    1 
ATOM   1700 O  O    . ALA   A 1 223 ? -18.330 -43.115 35.507 1.00 12.03 ? 226  ALA   A O    1 
ATOM   1701 C  CB   . ALA   A 1 223 ? -20.908 -41.252 35.825 1.00 11.37 ? 226  ALA   A CB   1 
ATOM   1702 N  N    . ILE   A 1 224 ? -19.711 -43.418 33.741 1.00 13.32 ? 227  ILE   A N    1 
ATOM   1703 C  CA   . ILE   A 1 224 ? -18.645 -43.701 32.808 1.00 12.60 ? 227  ILE   A CA   1 
ATOM   1704 C  C    . ILE   A 1 224 ? -18.928 -42.985 31.461 1.00 11.51 ? 227  ILE   A C    1 
ATOM   1705 O  O    . ILE   A 1 224 ? -19.913 -43.274 30.849 1.00 11.72 ? 227  ILE   A O    1 
ATOM   1706 C  CB   . ILE   A 1 224 ? -18.481 -45.214 32.504 1.00 12.13 ? 227  ILE   A CB   1 
ATOM   1707 C  CG1  . ILE   A 1 224 ? -18.179 -46.011 33.762 1.00 13.20 ? 227  ILE   A CG1  1 
ATOM   1708 C  CG2  . ILE   A 1 224 ? -17.392 -45.437 31.470 1.00 13.29 ? 227  ILE   A CG2  1 
ATOM   1709 C  CD1  . ILE   A 1 224 ? -18.170 -47.497 33.513 1.00 14.04 ? 227  ILE   A CD1  1 
ATOM   1710 N  N    . SER   A 1 225 ? -18.066 -42.050 31.058 1.00 10.04 ? 228  SER   A N    1 
ATOM   1711 C  CA   . SER   A 1 225 ? -18.211 -41.415 29.760 1.00 11.59 ? 228  SER   A CA   1 
ATOM   1712 C  C    . SER   A 1 225 ? -17.127 -41.947 28.832 1.00 13.21 ? 228  SER   A C    1 
ATOM   1713 O  O    . SER   A 1 225 ? -15.963 -41.771 29.091 1.00 14.45 ? 228  SER   A O    1 
ATOM   1714 C  CB   . SER   A 1 225 ? -18.144 -39.881 29.903 1.00 13.34 ? 228  SER   A CB   1 
ATOM   1715 O  OG   . SER   A 1 225 ? -19.325 -39.332 30.433 1.00 11.70 ? 228  SER   A OG   1 
ATOM   1716 N  N    . GLU   A 1 226 ? -17.549 -42.551 27.717 1.00 14.64 ? 229  GLU   A N    1 
ATOM   1717 C  CA   . GLU   A 1 226 ? -16.616 -43.097 26.800 1.00 14.66 ? 229  GLU   A CA   1 
ATOM   1718 C  C    . GLU   A 1 226 ? -16.645 -42.186 25.574 1.00 15.61 ? 229  GLU   A C    1 
ATOM   1719 O  O    . GLU   A 1 226 ? -17.631 -42.110 24.900 1.00 12.50 ? 229  GLU   A O    1 
ATOM   1720 C  CB   . GLU   A 1 226 ? -16.995 -44.544 26.429 1.00 14.64 ? 229  GLU   A CB   1 
ATOM   1721 C  CG   . GLU   A 1 226 ? -17.184 -45.470 27.626 1.00 17.20 ? 229  GLU   A CG   1 
ATOM   1722 C  CD   . GLU   A 1 226 ? -17.759 -46.851 27.298 1.00 18.95 ? 229  GLU   A CD   1 
ATOM   1723 O  OE1  . GLU   A 1 226 ? -18.202 -47.519 28.236 1.00 16.03 ? 229  GLU   A OE1  1 
ATOM   1724 O  OE2  . GLU   A 1 226 ? -17.782 -47.275 26.131 1.00 17.97 ? 229  GLU   A OE2  1 
ATOM   1725 N  N    . SER   A 1 227 ? -15.549 -41.492 25.343 1.00 12.92 ? 230  SER   A N    1 
ATOM   1726 C  CA   . SER   A 1 227 ? -15.404 -40.667 24.152 1.00 14.08 ? 230  SER   A CA   1 
ATOM   1727 C  C    . SER   A 1 227 ? -16.487 -39.586 23.962 1.00 14.61 ? 230  SER   A C    1 
ATOM   1728 O  O    . SER   A 1 227 ? -17.026 -39.456 22.895 1.00 11.88 ? 230  SER   A O    1 
ATOM   1729 C  CB   . SER   A 1 227 ? -15.260 -41.591 22.944 1.00 15.70 ? 230  SER   A CB   1 
ATOM   1730 O  OG   . SER   A 1 227 ? -14.267 -42.567 23.151 1.00 19.09 ? 230  SER   A OG   1 
ATOM   1731 N  N    . GLY   A 1 228 ? -16.960 -39.024 25.039 1.00 11.83 ? 231  GLY   A N    1 
ATOM   1732 C  CA   . GLY   A 1 228 ? -17.853 -37.889 24.933 1.00 11.76 ? 231  GLY   A CA   1 
ATOM   1733 C  C    . GLY   A 1 228 ? -17.988 -37.233 26.288 1.00 15.87 ? 231  GLY   A C    1 
ATOM   1734 O  O    . GLY   A 1 228 ? -18.204 -37.941 27.222 1.00 12.16 ? 231  GLY   A O    1 
ATOM   1735 N  N    . VAL   A 1 229 ? -18.130 -35.922 26.318 1.00 12.69 ? 232  VAL   A N    1 
ATOM   1736 C  CA   . VAL   A 1 229 ? -18.333 -35.210 27.557 1.00 14.19 ? 232  VAL   A CA   1 
ATOM   1737 C  C    . VAL   A 1 229 ? -19.089 -33.905 27.288 1.00 12.21 ? 232  VAL   A C    1 
ATOM   1738 O  O    . VAL   A 1 229 ? -19.286 -33.524 26.174 1.00 13.36 ? 232  VAL   A O    1 
ATOM   1739 C  CB   . VAL   A 1 229 ? -17.044 -34.925 28.366 1.00 15.01 ? 232  VAL   A CB   1 
ATOM   1740 C  CG1  . VAL   A 1 229 ? -16.442 -36.171 28.994 1.00 14.82 ? 232  VAL   A CG1  1 
ATOM   1741 C  CG2  . VAL   A 1 229 ? -16.041 -34.168 27.526 1.00 14.32 ? 232  VAL   A CG2  1 
ATOM   1742 N  N    . ALA   A 1 230 ? -19.542 -33.277 28.338 1.00 13.26 ? 233  ALA   A N    1 
ATOM   1743 C  CA   . ALA   A 1 230 ? -20.321 -32.019 28.229 1.00 14.67 ? 233  ALA   A CA   1 
ATOM   1744 C  C    . ALA   A 1 230 ? -19.490 -30.864 27.635 1.00 18.39 ? 233  ALA   A C    1 
ATOM   1745 O  O    . ALA   A 1 230 ? -20.045 -29.866 27.246 1.00 15.79 ? 233  ALA   A O    1 
ATOM   1746 C  CB   . ALA   A 1 230 ? -20.968 -31.655 29.536 1.00 14.86 ? 233  ALA   A CB   1 
ATOM   1747 N  N    . LEU   A 1 231 ? -18.182 -30.978 27.700 1.00 14.57 ? 234  LEU   A N    1 
ATOM   1748 C  CA   . LEU   A 1 231 ? -17.290 -29.987 27.096 1.00 18.03 ? 234  LEU   A CA   1 
ATOM   1749 C  C    . LEU   A 1 231 ? -17.015 -30.331 25.611 1.00 19.46 ? 234  LEU   A C    1 
ATOM   1750 O  O    . LEU   A 1 231 ? -16.239 -29.680 24.980 1.00 19.31 ? 234  LEU   A O    1 
ATOM   1751 C  CB   . LEU   A 1 231 ? -16.017 -29.828 27.868 1.00 15.80 ? 234  LEU   A CB   1 
ATOM   1752 C  CG   . LEU   A 1 231 ? -16.158 -29.317 29.300 1.00 22.78 ? 234  LEU   A CG   1 
ATOM   1753 C  CD1  . LEU   A 1 231 ? -14.789 -28.989 29.856 1.00 20.56 ? 234  LEU   A CD1  1 
ATOM   1754 C  CD2  . LEU   A 1 231 ? -17.037 -28.083 29.341 1.00 23.59 ? 234  LEU   A CD2  1 
ATOM   1755 N  N    . THR   A 1 232 ? -17.653 -31.382 25.087 1.00 16.87 ? 235  THR   A N    1 
ATOM   1756 C  CA   . THR   A 1 232 ? -17.491 -31.685 23.687 1.00 14.61 ? 235  THR   A CA   1 
ATOM   1757 C  C    . THR   A 1 232 ? -18.479 -30.666 23.136 1.00 18.27 ? 235  THR   A C    1 
ATOM   1758 O  O    . THR   A 1 232 ? -19.667 -30.884 23.102 1.00 17.73 ? 235  THR   A O    1 
ATOM   1759 C  CB   . THR   A 1 232 ? -17.806 -33.177 23.413 1.00 19.14 ? 235  THR   A CB   1 
ATOM   1760 O  OG1  . THR   A 1 232 ? -16.827 -34.012 24.032 1.00 15.59 ? 235  THR   A OG1  1 
ATOM   1761 C  CG2  . THR   A 1 232 ? -17.857 -33.463 21.917 1.00 19.16 ? 235  THR   A CG2  1 
ATOM   1762 N  N    . SER   A 1 233 ? -17.936 -29.603 22.545 1.00 19.91 ? 236  SER   A N    1 
ATOM   1763 C  CA   . SER   A 1 233 ? -18.760 -28.423 22.209 1.00 21.24 ? 236  SER   A CA   1 
ATOM   1764 C  C    . SER   A 1 233 ? -19.826 -28.543 21.149 1.00 22.21 ? 236  SER   A C    1 
ATOM   1765 O  O    . SER   A 1 233 ? -20.838 -27.892 21.198 1.00 17.73 ? 236  SER   A O    1 
ATOM   1766 C  CB   . SER   A 1 233 ? -17.812 -27.266 21.828 1.00 27.44 ? 236  SER   A CB   1 
ATOM   1767 O  OG   . SER   A 1 233 ? -17.193 -27.511 20.592 1.00 28.67 ? 236  SER   A OG   1 
ATOM   1768 N  N    . VAL   A 1 234 ? -19.553 -29.388 20.192 1.00 18.12 ? 237  VAL   A N    1 
ATOM   1769 C  CA   . VAL   A 1 234 ? -20.521 -29.557 19.114 1.00 21.73 ? 237  VAL   A CA   1 
ATOM   1770 C  C    . VAL   A 1 234 ? -21.855 -30.076 19.642 1.00 20.43 ? 237  VAL   A C    1 
ATOM   1771 O  O    . VAL   A 1 234 ? -22.892 -29.868 19.005 1.00 18.65 ? 237  VAL   A O    1 
ATOM   1772 C  CB   . VAL   A 1 234 ? -19.952 -30.493 18.027 1.00 21.30 ? 237  VAL   A CB   1 
ATOM   1773 C  CG1  . VAL   A 1 234 ? -19.826 -31.920 18.561 1.00 19.59 ? 237  VAL   A CG1  1 
ATOM   1774 C  CG2  . VAL   A 1 234 ? -20.818 -30.448 16.775 1.00 25.99 ? 237  VAL   A CG2  1 
ATOM   1775 N  N    . LEU   A 1 235 ? -21.866 -30.703 20.819 1.00 16.63 ? 238  LEU   A N    1 
ATOM   1776 C  CA   . LEU   A 1 235 ? -23.098 -31.257 21.367 1.00 19.65 ? 238  LEU   A CA   1 
ATOM   1777 C  C    . LEU   A 1 235 ? -23.814 -30.301 22.317 1.00 21.91 ? 238  LEU   A C    1 
ATOM   1778 O  O    . LEU   A 1 235 ? -24.939 -30.597 22.727 1.00 16.97 ? 238  LEU   A O    1 
ATOM   1779 C  CB   . LEU   A 1 235 ? -22.798 -32.581 22.090 1.00 17.48 ? 238  LEU   A CB   1 
ATOM   1780 C  CG   . LEU   A 1 235 ? -22.424 -33.760 21.182 1.00 17.15 ? 238  LEU   A CG   1 
ATOM   1781 C  CD1  . LEU   A 1 235 ? -21.850 -34.941 21.976 1.00 19.85 ? 238  LEU   A CD1  1 
ATOM   1782 C  CD2  . LEU   A 1 235 ? -23.603 -34.216 20.327 1.00 23.77 ? 238  LEU   A CD2  1 
ATOM   1783 N  N    . VAL   A 1 236 ? -23.206 -29.170 22.681 1.00 17.35 ? 239  VAL   A N    1 
ATOM   1784 C  CA   . VAL   A 1 236 ? -23.807 -28.240 23.634 1.00 20.02 ? 239  VAL   A CA   1 
ATOM   1785 C  C    . VAL   A 1 236 ? -23.904 -26.856 22.990 1.00 25.41 ? 239  VAL   A C    1 
ATOM   1786 O  O    . VAL   A 1 236 ? -22.881 -26.248 22.648 1.00 23.48 ? 239  VAL   A O    1 
ATOM   1787 C  CB   . VAL   A 1 236 ? -23.034 -28.176 24.963 1.00 20.29 ? 239  VAL   A CB   1 
ATOM   1788 C  CG1  . VAL   A 1 236 ? -23.815 -27.316 25.960 1.00 19.49 ? 239  VAL   A CG1  1 
ATOM   1789 C  CG2  . VAL   A 1 236 ? -22.831 -29.583 25.541 1.00 18.37 ? 239  VAL   A CG2  1 
ATOM   1790 N  N    . LYS   A 1 237 ? -25.140 -26.384 22.813 1.00 20.93 ? 240  LYS   A N    1 
ATOM   1791 C  CA   . LYS   A 1 237 ? -25.467 -25.069 22.263 1.00 27.31 ? 240  LYS   A CA   1 
ATOM   1792 C  C    . LYS   A 1 237 ? -25.337 -23.988 23.324 1.00 29.60 ? 240  LYS   A C    1 
ATOM   1793 O  O    . LYS   A 1 237 ? -26.034 -24.031 24.337 1.00 31.83 ? 240  LYS   A O    1 
ATOM   1794 C  CB   . LYS   A 1 237 ? -26.896 -25.065 21.721 1.00 27.75 ? 240  LYS   A CB   1 
ATOM   1795 C  CG   . LYS   A 1 237 ? -27.403 -26.309 21.017 1.00 32.94 ? 240  LYS   A CG   1 
ATOM   1796 C  CD   . LYS   A 1 237 ? -26.434 -26.782 19.933 1.00 35.04 ? 240  LYS   A CD   1 
ATOM   1797 C  CE   . LYS   A 1 237 ? -27.193 -27.514 18.831 1.00 39.20 ? 240  LYS   A CE   1 
ATOM   1798 N  NZ   . LYS   A 1 237 ? -26.799 -27.048 17.472 1.00 31.49 ? 240  LYS   A NZ   1 
ATOM   1799 N  N    . LYS   A 1 238 ? -24.479 -23.004 23.088 1.00 34.72 ? 241  LYS   A N    1 
ATOM   1800 C  CA   . LYS   A 1 238 ? -24.462 -21.818 23.933 1.00 40.26 ? 241  LYS   A CA   1 
ATOM   1801 C  C    . LYS   A 1 238 ? -24.931 -20.606 23.134 1.00 38.01 ? 241  LYS   A C    1 
ATOM   1802 O  O    . LYS   A 1 238 ? -24.810 -20.553 21.906 1.00 41.62 ? 241  LYS   A O    1 
ATOM   1803 C  CB   . LYS   A 1 238 ? -23.069 -21.566 24.524 1.00 36.33 ? 241  LYS   A CB   1 
ATOM   1804 C  CG   . LYS   A 1 238 ? -22.459 -22.799 25.198 1.00 38.80 ? 241  LYS   A CG   1 
ATOM   1805 C  CD   . LYS   A 1 238 ? -21.099 -22.502 25.830 1.00 41.82 ? 241  LYS   A CD   1 
ATOM   1806 C  CE   . LYS   A 1 238 ? -20.078 -22.061 24.797 1.00 48.89 ? 241  LYS   A CE   1 
ATOM   1807 N  NZ   . LYS   A 1 238 ? -20.067 -22.945 23.599 1.00 52.99 ? 241  LYS   A NZ   1 
ATOM   1808 N  N    . GLY   A 1 239 ? -25.475 -19.629 23.847 1.00 40.27 ? 242  GLY   A N    1 
ATOM   1809 C  CA   . GLY   A 1 239 ? -25.925 -18.419 23.191 1.00 41.12 ? 242  GLY   A CA   1 
ATOM   1810 C  C    . GLY   A 1 239 ? -27.264 -18.571 22.496 1.00 41.30 ? 242  GLY   A C    1 
ATOM   1811 O  O    . GLY   A 1 239 ? -28.135 -19.302 22.981 1.00 41.16 ? 242  GLY   A O    1 
ATOM   1812 N  N    . ASP   A 1 240 ? -27.427 -17.909 21.346 1.00 33.88 ? 243  ASP   A N    1 
ATOM   1813 C  CA   . ASP   A 1 240 ? -28.720 -17.798 20.675 1.00 34.90 ? 243  ASP   A CA   1 
ATOM   1814 C  C    . ASP   A 1 240 ? -29.066 -19.073 19.921 1.00 30.36 ? 243  ASP   A C    1 
ATOM   1815 O  O    . ASP   A 1 240 ? -28.456 -19.387 18.891 1.00 29.85 ? 243  ASP   A O    1 
ATOM   1816 C  CB   . ASP   A 1 240 ? -28.734 -16.605 19.727 1.00 36.68 ? 243  ASP   A CB   1 
ATOM   1817 C  CG   . ASP   A 1 240 ? -30.131 -16.029 19.542 1.00 41.59 ? 243  ASP   A CG   1 
ATOM   1818 O  OD1  . ASP   A 1 240 ? -31.118 -16.684 19.976 1.00 39.91 ? 243  ASP   A OD1  1 
ATOM   1819 O  OD2  . ASP   A 1 240 ? -30.246 -14.932 18.954 1.00 44.25 ? 243  ASP   A OD2  1 
ATOM   1820 N  N    . VAL   A 1 241 ? -30.089 -19.785 20.409 1.00 27.63 ? 244  VAL   A N    1 
ATOM   1821 C  CA   . VAL   A 1 241 ? -30.591 -20.963 19.710 1.00 27.87 ? 244  VAL   A CA   1 
ATOM   1822 C  C    . VAL   A 1 241 ? -31.761 -20.637 18.786 1.00 26.42 ? 244  VAL   A C    1 
ATOM   1823 O  O    . VAL   A 1 241 ? -32.180 -21.505 18.007 1.00 22.89 ? 244  VAL   A O    1 
ATOM   1824 C  CB   . VAL   A 1 241 ? -30.993 -22.059 20.723 1.00 28.10 ? 244  VAL   A CB   1 
ATOM   1825 C  CG1  . VAL   A 1 241 ? -29.878 -22.288 21.734 1.00 30.25 ? 244  VAL   A CG1  1 
ATOM   1826 C  CG2  . VAL   A 1 241 ? -32.290 -21.714 21.418 1.00 25.80 ? 244  VAL   A CG2  1 
ATOM   1827 N  N    . LYS   A 1 242 ? -32.276 -19.401 18.812 1.00 27.52 ? 245  LYS   A N    1 
ATOM   1828 C  CA   . LYS   A 1 242 ? -33.423 -19.053 17.971 1.00 26.42 ? 245  LYS   A CA   1 
ATOM   1829 C  C    . LYS   A 1 242 ? -33.175 -19.183 16.472 1.00 24.47 ? 245  LYS   A C    1 
ATOM   1830 O  O    . LYS   A 1 242 ? -34.104 -19.600 15.762 1.00 25.02 ? 245  LYS   A O    1 
ATOM   1831 C  CB   . LYS   A 1 242 ? -33.888 -17.630 18.302 1.00 30.39 ? 245  LYS   A CB   1 
ATOM   1832 C  CG   . LYS   A 1 242 ? -34.853 -17.552 19.465 1.00 38.26 ? 245  LYS   A CG   1 
ATOM   1833 C  CD   . LYS   A 1 242 ? -36.308 -17.859 19.072 1.00 39.97 ? 245  LYS   A CD   1 
ATOM   1834 C  CE   . LYS   A 1 242 ? -37.095 -16.559 18.860 1.00 41.84 ? 245  LYS   A CE   1 
ATOM   1835 N  NZ   . LYS   A 1 242 ? -38.536 -16.793 18.549 1.00 33.50 ? 245  LYS   A NZ   1 
ATOM   1836 N  N    . PRO   A 1 243 ? -32.009 -18.827 15.919 1.00 28.56 ? 246  PRO   A N    1 
ATOM   1837 C  CA   . PRO   A 1 243 ? -31.827 -19.018 14.470 1.00 26.95 ? 246  PRO   A CA   1 
ATOM   1838 C  C    . PRO   A 1 243 ? -32.033 -20.452 13.999 1.00 25.09 ? 246  PRO   A C    1 
ATOM   1839 O  O    . PRO   A 1 243 ? -32.693 -20.660 12.972 1.00 25.52 ? 246  PRO   A O    1 
ATOM   1840 C  CB   . PRO   A 1 243 ? -30.391 -18.529 14.249 1.00 31.21 ? 246  PRO   A CB   1 
ATOM   1841 C  CG   . PRO   A 1 243 ? -30.238 -17.459 15.271 1.00 30.12 ? 246  PRO   A CG   1 
ATOM   1842 C  CD   . PRO   A 1 243 ? -30.910 -18.022 16.490 1.00 30.44 ? 246  PRO   A CD   1 
ATOM   1843 N  N    . LEU   A 1 244 ? -31.493 -21.447 14.714 1.00 22.52 ? 247  LEU   A N    1 
ATOM   1844 C  CA   . LEU   A 1 244 ? -31.692 -22.835 14.307 1.00 24.92 ? 247  LEU   A CA   1 
ATOM   1845 C  C    . LEU   A 1 244 ? -33.171 -23.208 14.363 1.00 20.40 ? 247  LEU   A C    1 
ATOM   1846 O  O    . LEU   A 1 244 ? -33.690 -23.872 13.455 1.00 22.48 ? 247  LEU   A O    1 
ATOM   1847 C  CB   . LEU   A 1 244 ? -30.892 -23.777 15.209 1.00 22.23 ? 247  LEU   A CB   1 
ATOM   1848 C  CG   . LEU   A 1 244 ? -30.957 -25.284 14.893 1.00 29.42 ? 247  LEU   A CG   1 
ATOM   1849 C  CD1  . LEU   A 1 244 ? -30.988 -25.563 13.384 1.00 27.46 ? 247  LEU   A CD1  1 
ATOM   1850 C  CD2  . LEU   A 1 244 ? -29.888 -26.113 15.612 1.00 34.09 ? 247  LEU   A CD2  1 
ATOM   1851 N  N    . ALA   A 1 245 ? -33.852 -22.821 15.444 1.00 20.82 ? 248  ALA   A N    1 
ATOM   1852 C  CA   . ALA   A 1 245 ? -35.281 -23.102 15.565 1.00 21.17 ? 248  ALA   A CA   1 
ATOM   1853 C  C    . ALA   A 1 245 ? -36.056 -22.522 14.391 1.00 20.45 ? 248  ALA   A C    1 
ATOM   1854 O  O    . ALA   A 1 245 ? -36.940 -23.180 13.823 1.00 20.26 ? 248  ALA   A O    1 
ATOM   1855 C  CB   . ALA   A 1 245 ? -35.813 -22.542 16.883 1.00 20.08 ? 248  ALA   A CB   1 
ATOM   1856 N  N    . GLU   A 1 246 ? -35.744 -21.279 14.015 1.00 19.81 ? 249  GLU   A N    1 
ATOM   1857 C  CA   . GLU   A 1 246 ? -36.451 -20.650 12.902 1.00 20.25 ? 249  GLU   A CA   1 
ATOM   1858 C  C    . GLU   A 1 246 ? -36.180 -21.380 11.601 1.00 19.52 ? 249  GLU   A C    1 
ATOM   1859 O  O    . GLU   A 1 246 ? -37.089 -21.572 10.785 1.00 18.79 ? 249  GLU   A O    1 
ATOM   1860 C  CB   . GLU   A 1 246 ? -36.046 -19.180 12.788 1.00 19.85 ? 249  GLU   A CB   1 
ATOM   1861 C  CG   . GLU   A 1 246 ? -36.544 -18.379 13.973 1.00 26.85 ? 249  GLU   A CG   1 
ATOM   1862 C  CD   . GLU   A 1 246 ? -36.178 -16.901 13.906 1.00 37.25 ? 249  GLU   A CD   1 
ATOM   1863 O  OE1  . GLU   A 1 246 ? -36.603 -16.157 14.817 1.00 37.20 ? 249  GLU   A OE1  1 
ATOM   1864 O  OE2  . GLU   A 1 246 ? -35.469 -16.491 12.959 1.00 35.83 ? 249  GLU   A OE2  1 
ATOM   1865 N  N    . GLN   A 1 247 ? -34.931 -21.805 11.395 1.00 20.72 ? 250  GLN   A N    1 
ATOM   1866 C  CA   . GLN   A 1 247 ? -34.581 -22.543 10.187 1.00 21.16 ? 250  GLN   A CA   1 
ATOM   1867 C  C    . GLN   A 1 247 ? -35.366 -23.847 10.097 1.00 18.22 ? 250  GLN   A C    1 
ATOM   1868 O  O    . GLN   A 1 247 ? -35.852 -24.227 9.021  1.00 20.32 ? 250  GLN   A O    1 
ATOM   1869 C  CB   . GLN   A 1 247 ? -33.079 -22.808 10.200 1.00 22.49 ? 250  GLN   A CB   1 
ATOM   1870 C  CG   . GLN   A 1 247 ? -32.452 -23.233 8.899  1.00 35.50 ? 250  GLN   A CG   1 
ATOM   1871 C  CD   . GLN   A 1 247 ? -30.919 -23.243 9.003  1.00 45.46 ? 250  GLN   A CD   1 
ATOM   1872 O  OE1  . GLN   A 1 247 ? -30.241 -24.028 8.333  1.00 54.10 ? 250  GLN   A OE1  1 
ATOM   1873 N  NE2  . GLN   A 1 247 ? -30.373 -22.371 9.862  1.00 44.48 ? 250  GLN   A NE2  1 
ATOM   1874 N  N    . ILE   A 1 248 ? -35.511 -24.539 11.225 1.00 16.99 ? 251  ILE   A N    1 
ATOM   1875 C  CA   . ILE   A 1 248 ? -36.274 -25.788 11.245 1.00 19.90 ? 251  ILE   A CA   1 
ATOM   1876 C  C    . ILE   A 1 248 ? -37.740 -25.514 10.947 1.00 18.34 ? 251  ILE   A C    1 
ATOM   1877 O  O    . ILE   A 1 248 ? -38.371 -26.201 10.132 1.00 18.19 ? 251  ILE   A O    1 
ATOM   1878 C  CB   . ILE   A 1 248 ? -36.107 -26.472 12.607 1.00 19.88 ? 251  ILE   A CB   1 
ATOM   1879 C  CG1  . ILE   A 1 248 ? -34.671 -26.967 12.739 1.00 23.52 ? 251  ILE   A CG1  1 
ATOM   1880 C  CG2  . ILE   A 1 248 ? -37.133 -27.633 12.769 1.00 17.27 ? 251  ILE   A CG2  1 
ATOM   1881 C  CD1  . ILE   A 1 248 ? -34.309 -27.221 14.135 1.00 22.42 ? 251  ILE   A CD1  1 
ATOM   1882 N  N    . ALA   A 1 249 ? -38.298 -24.493 11.596 1.00 18.84 ? 252  ALA   A N    1 
ATOM   1883 C  CA   . ALA   A 1 249 ? -39.705 -24.158 11.386 1.00 16.63 ? 252  ALA   A CA   1 
ATOM   1884 C  C    . ALA   A 1 249 ? -39.976 -23.815 9.926  1.00 18.38 ? 252  ALA   A C    1 
ATOM   1885 O  O    . ALA   A 1 249 ? -40.954 -24.292 9.338  1.00 19.83 ? 252  ALA   A O    1 
ATOM   1886 C  CB   . ALA   A 1 249 ? -40.108 -23.001 12.301 1.00 19.79 ? 252  ALA   A CB   1 
ATOM   1887 N  N    . ILE   A 1 250 ? -39.111 -22.994 9.323  1.00 19.88 ? 253  ILE   A N    1 
ATOM   1888 C  CA   . ILE   A 1 250 ? -39.273 -22.616 7.918  1.00 20.90 ? 253  ILE   A CA   1 
ATOM   1889 C  C    . ILE   A 1 250 ? -39.168 -23.838 7.011  1.00 22.53 ? 253  ILE   A C    1 
ATOM   1890 O  O    . ILE   A 1 250 ? -39.954 -24.003 6.065  1.00 23.00 ? 253  ILE   A O    1 
ATOM   1891 C  CB   . ILE   A 1 250 ? -38.227 -21.554 7.538  1.00 23.17 ? 253  ILE   A CB   1 
ATOM   1892 C  CG1  . ILE   A 1 250 ? -38.513 -20.225 8.243  1.00 24.03 ? 253  ILE   A CG1  1 
ATOM   1893 C  CG2  . ILE   A 1 250 ? -38.197 -21.361 6.027  1.00 28.06 ? 253  ILE   A CG2  1 
ATOM   1894 C  CD1  . ILE   A 1 250 ? -37.290 -19.304 8.255  1.00 25.40 ? 253  ILE   A CD1  1 
ATOM   1895 N  N    . THR   A 1 251 ? -38.184 -24.707 7.268  1.00 17.74 ? 254  THR   A N    1 
ATOM   1896 C  CA   . THR   A 1 251 ? -38.053 -25.914 6.458  1.00 18.97 ? 254  THR   A CA   1 
ATOM   1897 C  C    . THR   A 1 251 ? -39.296 -26.796 6.556  1.00 19.86 ? 254  THR   A C    1 
ATOM   1898 O  O    . THR   A 1 251 ? -39.726 -27.389 5.558  1.00 21.64 ? 254  THR   A O    1 
ATOM   1899 C  CB   . THR   A 1 251 ? -36.791 -26.671 6.875  1.00 21.51 ? 254  THR   A CB   1 
ATOM   1900 O  OG1  . THR   A 1 251 ? -35.674 -25.783 6.755  1.00 24.77 ? 254  THR   A OG1  1 
ATOM   1901 C  CG2  . THR   A 1 251 ? -36.559 -27.893 5.996  1.00 22.50 ? 254  THR   A CG2  1 
ATOM   1902 N  N    . ALA   A 1 252 ? -39.916 -26.860 7.736  1.00 18.33 ? 255  ALA   A N    1 
ATOM   1903 C  CA   . ALA   A 1 252 ? -41.131 -27.654 7.903  1.00 19.09 ? 255  ALA   A CA   1 
ATOM   1904 C  C    . ALA   A 1 252 ? -42.375 -26.993 7.312  1.00 22.04 ? 255  ALA   A C    1 
ATOM   1905 O  O    . ALA   A 1 252 ? -43.428 -27.634 7.259  1.00 22.50 ? 255  ALA   A O    1 
ATOM   1906 C  CB   . ALA   A 1 252 ? -41.369 -27.937 9.384  1.00 17.90 ? 255  ALA   A CB   1 
ATOM   1907 N  N    . GLY   A 1 253 ? -42.289 -25.743 6.867  1.00 21.35 ? 256  GLY   A N    1 
ATOM   1908 C  CA   . GLY   A 1 253 ? -43.455 -25.038 6.370  1.00 23.02 ? 256  GLY   A CA   1 
ATOM   1909 C  C    . GLY   A 1 253 ? -44.174 -24.175 7.383  1.00 24.78 ? 256  GLY   A C    1 
ATOM   1910 O  O    . GLY   A 1 253 ? -45.331 -23.813 7.153  1.00 30.90 ? 256  GLY   A O    1 
ATOM   1911 N  N    . CYS   A 1 254 ? -43.527 -23.818 8.485  1.00 24.98 ? 257  CYS   A N    1 
ATOM   1912 C  CA   . CYS   A 1 254 ? -44.141 -23.078 9.579  1.00 22.90 ? 257  CYS   A CA   1 
ATOM   1913 C  C    . CYS   A 1 254 ? -43.742 -21.610 9.565  1.00 26.05 ? 257  CYS   A C    1 
ATOM   1914 O  O    . CYS   A 1 254 ? -42.636 -21.254 9.162  1.00 26.00 ? 257  CYS   A O    1 
ATOM   1915 C  CB   . CYS   A 1 254 ? -43.752 -23.685 10.927 1.00 21.80 ? 257  CYS   A CB   1 
ATOM   1916 S  SG   . CYS   A 1 254 ? -44.466 -25.329 11.178 1.00 28.51 ? 257  CYS   A SG   1 
ATOM   1917 N  N    . LYS   A 1 255 ? -44.654 -20.760 10.039 1.00 26.50 ? 258  LYS   A N    1 
ATOM   1918 C  CA   . LYS   A 1 255 ? -44.307 -19.362 10.230 1.00 24.62 ? 258  LYS   A CA   1 
ATOM   1919 C  C    . LYS   A 1 255 ? -43.500 -19.190 11.509 1.00 25.50 ? 258  LYS   A C    1 
ATOM   1920 O  O    . LYS   A 1 255 ? -43.561 -20.014 12.426 1.00 24.16 ? 258  LYS   A O    1 
ATOM   1921 C  CB   . LYS   A 1 255 ? -45.561 -18.493 10.283 1.00 30.32 ? 258  LYS   A CB   1 
ATOM   1922 C  CG   . LYS   A 1 255 ? -46.237 -18.346 8.931  1.00 33.66 ? 258  LYS   A CG   1 
ATOM   1923 C  CD   . LYS   A 1 255 ? -47.451 -17.433 9.004  1.00 39.56 ? 258  LYS   A CD   1 
ATOM   1924 C  CE   . LYS   A 1 255 ? -48.668 -18.166 9.527  1.00 41.14 ? 258  LYS   A CE   1 
ATOM   1925 N  NZ   . LYS   A 1 255 ? -48.604 -18.700 10.936 1.00 41.41 ? 258  LYS   A NZ   1 
ATOM   1926 N  N    . THR   A 1 256 ? -42.735 -18.095 11.567 1.00 20.92 ? 259  THR   A N    1 
ATOM   1927 C  CA   . THR   A 1 256 ? -41.857 -17.833 12.701 1.00 22.03 ? 259  THR   A CA   1 
ATOM   1928 C  C    . THR   A 1 256 ? -42.293 -16.587 13.468 1.00 21.41 ? 259  THR   A C    1 
ATOM   1929 O  O    . THR   A 1 256 ? -41.472 -15.936 14.110 1.00 20.62 ? 259  THR   A O    1 
ATOM   1930 C  CB   . THR   A 1 256 ? -40.403 -17.705 12.245 1.00 25.22 ? 259  THR   A CB   1 
ATOM   1931 O  OG1  . THR   A 1 256 ? -40.270 -16.548 11.413 1.00 26.23 ? 259  THR   A OG1  1 
ATOM   1932 C  CG2  . THR   A 1 256 ? -39.959 -18.946 11.461 1.00 24.22 ? 259  THR   A CG2  1 
ATOM   1933 N  N    . THR   A 1 257 ? -43.595 -16.281 13.432 1.00 20.18 ? 260  THR   A N    1 
ATOM   1934 C  CA   . THR   A 1 257 ? -44.114 -15.053 14.035 1.00 21.67 ? 260  THR   A CA   1 
ATOM   1935 C  C    . THR   A 1 257 ? -43.732 -14.938 15.508 1.00 22.96 ? 260  THR   A C    1 
ATOM   1936 O  O    . THR   A 1 257 ? -43.325 -13.866 15.976 1.00 19.79 ? 260  THR   A O    1 
ATOM   1937 C  CB   . THR   A 1 257 ? -45.641 -15.010 13.874 1.00 20.01 ? 260  THR   A CB   1 
ATOM   1938 O  OG1  . THR   A 1 257 ? -45.997 -15.461 12.561 1.00 23.47 ? 260  THR   A OG1  1 
ATOM   1939 C  CG2  . THR   A 1 257 ? -46.186 -13.581 14.082 1.00 24.09 ? 260  THR   A CG2  1 
ATOM   1940 N  N    . THR   A 1 258 ? -43.903 -16.022 16.267 1.00 16.85 ? 261  THR   A N    1 
ATOM   1941 C  CA   . THR   A 1 258 ? -43.529 -16.086 17.677 1.00 17.56 ? 261  THR   A CA   1 
ATOM   1942 C  C    . THR   A 1 258 ? -43.046 -17.502 17.975 1.00 18.44 ? 261  THR   A C    1 
ATOM   1943 O  O    . THR   A 1 258 ? -43.291 -18.427 17.202 1.00 17.47 ? 261  THR   A O    1 
ATOM   1944 C  CB   . THR   A 1 258 ? -44.700 -15.767 18.627 1.00 18.70 ? 261  THR   A CB   1 
ATOM   1945 O  OG1  . THR   A 1 258 ? -45.558 -16.912 18.716 1.00 15.35 ? 261  THR   A OG1  1 
ATOM   1946 C  CG2  . THR   A 1 258 ? -45.533 -14.568 18.172 1.00 19.95 ? 261  THR   A CG2  1 
ATOM   1947 N  N    . SER   A 1 259 ? -42.400 -17.673 19.135 1.00 16.03 ? 262  SER   A N    1 
ATOM   1948 C  CA   . SER   A 1 259 ? -41.980 -19.006 19.575 1.00 18.06 ? 262  SER   A CA   1 
ATOM   1949 C  C    . SER   A 1 259 ? -43.174 -19.947 19.723 1.00 19.10 ? 262  SER   A C    1 
ATOM   1950 O  O    . SER   A 1 259 ? -43.135 -21.098 19.265 1.00 17.20 ? 262  SER   A O    1 
ATOM   1951 C  CB   . SER   A 1 259 ? -41.232 -18.913 20.909 1.00 19.27 ? 262  SER   A CB   1 
ATOM   1952 O  OG   . SER   A 1 259 ? -40.008 -18.197 20.800 1.00 22.99 ? 262  SER   A OG   1 
ATOM   1953 N  N    . ALA   A 1 260 ? -44.236 -19.481 20.399 1.00 16.17 ? 263  ALA   A N    1 
ATOM   1954 C  CA   . ALA   A 1 260 ? -45.413 -20.323 20.613 1.00 16.64 ? 263  ALA   A CA   1 
ATOM   1955 C  C    . ALA   A 1 260 ? -46.046 -20.743 19.290 1.00 16.99 ? 263  ALA   A C    1 
ATOM   1956 O  O    . ALA   A 1 260 ? -46.518 -21.882 19.146 1.00 15.36 ? 263  ALA   A O    1 
ATOM   1957 C  CB   . ALA   A 1 260 ? -46.430 -19.587 21.483 1.00 15.44 ? 263  ALA   A CB   1 
ATOM   1958 N  N    . VAL   A 1 261 ? -46.050 -19.834 18.313 1.00 17.04 ? 264  VAL   A N    1 
ATOM   1959 C  CA   . VAL   A 1 261 ? -46.578 -20.134 16.983 1.00 17.37 ? 264  VAL   A CA   1 
ATOM   1960 C  C    . VAL   A 1 261 ? -45.761 -21.239 16.323 1.00 15.74 ? 264  VAL   A C    1 
ATOM   1961 O  O    . VAL   A 1 261 ? -46.314 -22.194 15.757 1.00 16.99 ? 264  VAL   A O    1 
ATOM   1962 C  CB   . VAL   A 1 261 ? -46.600 -18.850 16.130 1.00 20.42 ? 264  VAL   A CB   1 
ATOM   1963 C  CG1  . VAL   A 1 261 ? -46.745 -19.175 14.654 1.00 23.99 ? 264  VAL   A CG1  1 
ATOM   1964 C  CG2  . VAL   A 1 261 ? -47.744 -17.947 16.579 1.00 18.91 ? 264  VAL   A CG2  1 
ATOM   1965 N  N    . MET   A 1 262 ? -44.434 -21.120 16.394 1.00 16.92 ? 265  MET   A N    1 
ATOM   1966 C  CA   . MET   A 1 262 ? -43.527 -22.105 15.802 1.00 15.84 ? 265  MET   A CA   1 
ATOM   1967 C  C    . MET   A 1 262 ? -43.764 -23.486 16.398 1.00 16.92 ? 265  MET   A C    1 
ATOM   1968 O  O    . MET   A 1 262 ? -43.900 -24.482 15.675 1.00 16.54 ? 265  MET   A O    1 
ATOM   1969 C  CB   . MET   A 1 262 ? -42.097 -21.652 16.079 1.00 14.61 ? 265  MET   A CB   1 
ATOM   1970 C  CG   . MET   A 1 262 ? -41.626 -20.589 15.114 1.00 21.37 ? 265  MET   A CG   1 
ATOM   1971 S  SD   . MET   A 1 262 ? -39.851 -20.374 15.175 1.00 30.69 ? 265  MET   A SD   1 
ATOM   1972 C  CE   . MET   A 1 262 ? -39.753 -19.334 16.622 1.00 25.03 ? 265  MET   A CE   1 
ATOM   1973 N  N    . VAL   A 1 263 ? -43.815 -23.559 17.735 1.00 14.69 ? 266  VAL   A N    1 
ATOM   1974 C  CA   . VAL   A 1 263 ? -43.968 -24.854 18.395 1.00 18.17 ? 266  VAL   A CA   1 
ATOM   1975 C  C    . VAL   A 1 263 ? -45.347 -25.453 18.119 1.00 18.49 ? 266  VAL   A C    1 
ATOM   1976 O  O    . VAL   A 1 263 ? -45.475 -26.665 17.893 1.00 15.89 ? 266  VAL   A O    1 
ATOM   1977 C  CB   . VAL   A 1 263 ? -43.697 -24.729 19.904 1.00 20.02 ? 266  VAL   A CB   1 
ATOM   1978 C  CG1  . VAL   A 1 263 ? -43.789 -26.107 20.566 1.00 23.54 ? 266  VAL   A CG1  1 
ATOM   1979 C  CG2  . VAL   A 1 263 ? -42.326 -24.143 20.117 1.00 19.94 ? 266  VAL   A CG2  1 
ATOM   1980 N  N    . HIS   A 1 264 ? -46.401 -24.633 18.140 1.00 15.35 ? 267  HIS   A N    1 
ATOM   1981 C  CA   . HIS   A 1 264 ? -47.730 -25.167 17.866 1.00 16.99 ? 267  HIS   A CA   1 
ATOM   1982 C  C    . HIS   A 1 264 ? -47.808 -25.726 16.447 1.00 15.86 ? 267  HIS   A C    1 
ATOM   1983 O  O    . HIS   A 1 264 ? -48.353 -26.823 16.215 1.00 17.73 ? 267  HIS   A O    1 
ATOM   1984 C  CB   . HIS   A 1 264 ? -48.785 -24.070 18.072 1.00 19.38 ? 267  HIS   A CB   1 
ATOM   1985 C  CG   . HIS   A 1 264 ? -50.175 -24.527 17.783 1.00 18.19 ? 267  HIS   A CG   1 
ATOM   1986 N  ND1  . HIS   A 1 264 ? -50.840 -25.420 18.596 1.00 24.45 ? 267  HIS   A ND1  1 
ATOM   1987 C  CD2  . HIS   A 1 264 ? -51.009 -24.260 16.751 1.00 22.42 ? 267  HIS   A CD2  1 
ATOM   1988 C  CE1  . HIS   A 1 264 ? -52.036 -25.665 18.090 1.00 23.58 ? 267  HIS   A CE1  1 
ATOM   1989 N  NE2  . HIS   A 1 264 ? -52.163 -24.979 16.968 1.00 23.38 ? 267  HIS   A NE2  1 
ATOM   1990 N  N    . CYS   A 1 265 ? -47.238 -24.993 15.487 1.00 16.74 ? 268  CYS   A N    1 
ATOM   1991 C  CA   . CYS   A 1 265 ? -47.220 -25.467 14.107 1.00 17.59 ? 268  CYS   A CA   1 
ATOM   1992 C  C    . CYS   A 1 265 ? -46.473 -26.788 13.990 1.00 16.14 ? 268  CYS   A C    1 
ATOM   1993 O  O    . CYS   A 1 265 ? -46.970 -27.742 13.379 1.00 18.39 ? 268  CYS   A O    1 
ATOM   1994 C  CB   . CYS   A 1 265 ? -46.586 -24.412 13.202 1.00 16.93 ? 268  CYS   A CB   1 
ATOM   1995 S  SG   . CYS   A 1 265 ? -46.490 -24.849 11.438 1.00 34.19 ? 268  CYS   A SG   1 
ATOM   1996 N  N    . LEU   A 1 266 ? -45.277 -26.866 14.583 1.00 15.85 ? 269  LEU   A N    1 
ATOM   1997 C  CA   . LEU   A 1 266 ? -44.512 -28.114 14.521 1.00 15.65 ? 269  LEU   A CA   1 
ATOM   1998 C  C    . LEU   A 1 266 ? -45.258 -29.266 15.191 1.00 18.59 ? 269  LEU   A C    1 
ATOM   1999 O  O    . LEU   A 1 266 ? -45.157 -30.417 14.745 1.00 17.69 ? 269  LEU   A O    1 
ATOM   2000 C  CB   . LEU   A 1 266 ? -43.136 -27.898 15.155 1.00 16.27 ? 269  LEU   A CB   1 
ATOM   2001 C  CG   . LEU   A 1 266 ? -42.232 -27.019 14.293 1.00 17.94 ? 269  LEU   A CG   1 
ATOM   2002 C  CD1  . LEU   A 1 266 ? -41.045 -26.573 15.090 1.00 18.34 ? 269  LEU   A CD1  1 
ATOM   2003 C  CD2  . LEU   A 1 266 ? -41.785 -27.755 13.028 1.00 16.36 ? 269  LEU   A CD2  1 
ATOM   2004 N  N    . ARG   A 1 267 ? -46.032 -28.980 16.246 1.00 18.19 ? 270  ARG   A N    1 
ATOM   2005 C  CA   . ARG   A 1 267 ? -46.824 -30.036 16.862 1.00 17.44 ? 270  ARG   A CA   1 
ATOM   2006 C  C    . ARG   A 1 267 ? -47.950 -30.515 15.964 1.00 20.78 ? 270  ARG   A C    1 
ATOM   2007 O  O    . ARG   A 1 267 ? -48.485 -31.603 16.204 1.00 20.82 ? 270  ARG   A O    1 
ATOM   2008 C  CB   . ARG   A 1 267 ? -47.418 -29.589 18.196 1.00 17.95 ? 270  ARG   A CB   1 
ATOM   2009 C  CG   . ARG   A 1 267 ? -46.452 -29.533 19.324 1.00 18.46 ? 270  ARG   A CG   1 
ATOM   2010 C  CD   . ARG   A 1 267 ? -47.135 -29.145 20.634 1.00 21.93 ? 270  ARG   A CD   1 
ATOM   2011 N  NE   . ARG   A 1 267 ? -46.182 -29.236 21.728 1.00 21.44 ? 270  ARG   A NE   1 
ATOM   2012 C  CZ   . ARG   A 1 267 ? -45.963 -28.271 22.607 1.00 22.59 ? 270  ARG   A CZ   1 
ATOM   2013 N  NH1  . ARG   A 1 267 ? -46.669 -27.149 22.595 1.00 22.90 ? 270  ARG   A NH1  1 
ATOM   2014 N  NH2  . ARG   A 1 267 ? -45.000 -28.425 23.507 1.00 21.77 ? 270  ARG   A NH2  1 
ATOM   2015 N  N    . GLN   A 1 268 ? -48.349 -29.731 14.957 1.00 18.48 ? 271  GLN   A N    1 
ATOM   2016 C  CA   . GLN   A 1 268 ? -49.369 -30.253 14.038 1.00 21.01 ? 271  GLN   A CA   1 
ATOM   2017 C  C    . GLN   A 1 268 ? -48.805 -31.132 12.917 1.00 23.40 ? 271  GLN   A C    1 
ATOM   2018 O  O    . GLN   A 1 268 ? -49.580 -31.840 12.258 1.00 21.24 ? 271  GLN   A O    1 
ATOM   2019 C  CB   . GLN   A 1 268 ? -50.174 -29.111 13.406 1.00 20.54 ? 271  GLN   A CB   1 
ATOM   2020 C  CG   . GLN   A 1 268 ? -50.680 -28.079 14.396 1.00 23.18 ? 271  GLN   A CG   1 
ATOM   2021 C  CD   . GLN   A 1 268 ? -51.353 -28.700 15.598 1.00 25.44 ? 271  GLN   A CD   1 
ATOM   2022 O  OE1  . GLN   A 1 268 ? -52.317 -29.459 15.464 1.00 27.86 ? 271  GLN   A OE1  1 
ATOM   2023 N  NE2  . GLN   A 1 268 ? -50.848 -28.384 16.790 1.00 22.89 ? 271  GLN   A NE2  1 
ATOM   2024 N  N    . LYS   A 1 269 ? -47.494 -31.129 12.690 1.00 19.15 ? 272  LYS   A N    1 
ATOM   2025 C  CA   . LYS   A 1 269 ? -46.916 -31.875 11.580 1.00 19.43 ? 272  LYS   A CA   1 
ATOM   2026 C  C    . LYS   A 1 269 ? -46.931 -33.370 11.868 1.00 18.63 ? 272  LYS   A C    1 
ATOM   2027 O  O    . LYS   A 1 269 ? -46.833 -33.800 13.017 1.00 17.75 ? 272  LYS   A O    1 
ATOM   2028 C  CB   . LYS   A 1 269 ? -45.471 -31.424 11.323 1.00 17.52 ? 272  LYS   A CB   1 
ATOM   2029 C  CG   . LYS   A 1 269 ? -45.321 -29.938 10.925 1.00 20.55 ? 272  LYS   A CG   1 
ATOM   2030 C  CD   . LYS   A 1 269 ? -45.901 -29.638 9.549  1.00 23.37 ? 272  LYS   A CD   1 
ATOM   2031 C  CE   . LYS   A 1 269 ? -45.829 -28.134 9.258  1.00 26.15 ? 272  LYS   A CE   1 
ATOM   2032 N  NZ   . LYS   A 1 269 ? -46.416 -27.783 7.936  1.00 33.28 ? 272  LYS   A NZ   1 
ATOM   2033 N  N    . THR   A 1 270 ? -47.049 -34.164 10.808 1.00 17.43 ? 273  THR   A N    1 
ATOM   2034 C  CA   . THR   A 1 270 ? -46.967 -35.613 10.960 1.00 18.99 ? 273  THR   A CA   1 
ATOM   2035 C  C    . THR   A 1 270 ? -45.527 -36.039 11.214 1.00 18.37 ? 273  THR   A C    1 
ATOM   2036 O  O    . THR   A 1 270 ? -44.573 -35.304 10.929 1.00 16.28 ? 273  THR   A O    1 
ATOM   2037 C  CB   . THR   A 1 270 ? -47.492 -36.331 9.716  1.00 20.49 ? 273  THR   A CB   1 
ATOM   2038 O  OG1  . THR   A 1 270 ? -46.615 -36.071 8.612  1.00 17.90 ? 273  THR   A OG1  1 
ATOM   2039 C  CG2  . THR   A 1 270 ? -48.924 -35.899 9.387  1.00 21.77 ? 273  THR   A CG2  1 
ATOM   2040 N  N    . GLU   A 1 271 ? -45.372 -37.249 11.759 1.00 17.82 ? 274  GLU   A N    1 
ATOM   2041 C  CA   . GLU   A 1 271 ? -44.029 -37.806 11.884 1.00 17.31 ? 274  GLU   A CA   1 
ATOM   2042 C  C    . GLU   A 1 271 ? -43.296 -37.749 10.550 1.00 17.85 ? 274  GLU   A C    1 
ATOM   2043 O  O    . GLU   A 1 271 ? -42.117 -37.379 10.483 1.00 18.00 ? 274  GLU   A O    1 
ATOM   2044 C  CB   . GLU   A 1 271 ? -44.095 -39.253 12.369 1.00 20.15 ? 274  GLU   A CB   1 
ATOM   2045 C  CG   . GLU   A 1 271 ? -42.731 -39.906 12.456 1.00 18.52 ? 274  GLU   A CG   1 
ATOM   2046 C  CD   . GLU   A 1 271 ? -42.833 -41.361 12.869 1.00 25.42 ? 274  GLU   A CD   1 
ATOM   2047 O  OE1  . GLU   A 1 271 ? -43.934 -41.932 12.740 1.00 27.98 ? 274  GLU   A OE1  1 
ATOM   2048 O  OE2  . GLU   A 1 271 ? -41.812 -41.949 13.293 1.00 23.63 ? 274  GLU   A OE2  1 
ATOM   2049 N  N    . GLU   A 1 272 ? -43.994 -38.101 9.472  1.00 17.94 ? 275  GLU   A N    1 
ATOM   2050 C  CA   . GLU   A 1 272 ? -43.365 -38.153 8.158  1.00 20.38 ? 275  GLU   A CA   1 
ATOM   2051 C  C    . GLU   A 1 272 ? -42.912 -36.772 7.688  1.00 21.67 ? 275  GLU   A C    1 
ATOM   2052 O  O    . GLU   A 1 272 ? -41.837 -36.639 7.087  1.00 18.69 ? 275  GLU   A O    1 
ATOM   2053 C  CB   . GLU   A 1 272 ? -44.318 -38.806 7.152  1.00 24.54 ? 275  GLU   A CB   1 
ATOM   2054 C  CG   . GLU   A 1 272 ? -44.756 -40.261 7.522  1.00 35.93 ? 275  GLU   A CG   1 
ATOM   2055 C  CD   . GLU   A 1 272 ? -45.799 -40.466 8.676  1.00 38.43 ? 275  GLU   A CD   1 
ATOM   2056 O  OE1  . GLU   A 1 272 ? -46.344 -39.526 9.304  1.00 25.52 ? 275  GLU   A OE1  1 
ATOM   2057 O  OE2  . GLU   A 1 272 ? -46.025 -41.654 9.001  1.00 45.77 ? 275  GLU   A OE2  1 
ATOM   2058 N  N    . GLU   A 1 273 ? -43.703 -35.737 7.968  1.00 19.80 ? 276  GLU   A N    1 
ATOM   2059 C  CA   . GLU   A 1 273 ? -43.302 -34.365 7.650  1.00 20.55 ? 276  GLU   A CA   1 
ATOM   2060 C  C    . GLU   A 1 273 ? -42.075 -33.935 8.445  1.00 19.16 ? 276  GLU   A C    1 
ATOM   2061 O  O    . GLU   A 1 273 ? -41.186 -33.260 7.912  1.00 18.58 ? 276  GLU   A O    1 
ATOM   2062 C  CB   . GLU   A 1 273 ? -44.474 -33.417 7.893  1.00 19.51 ? 276  GLU   A CB   1 
ATOM   2063 C  CG   . GLU   A 1 273 ? -45.542 -33.470 6.781  1.00 27.38 ? 276  GLU   A CG   1 
ATOM   2064 C  CD   . GLU   A 1 273 ? -46.909 -32.878 7.163  1.00 28.78 ? 276  GLU   A CD   1 
ATOM   2065 O  OE1  . GLU   A 1 273 ? -47.221 -32.711 8.364  1.00 23.31 ? 276  GLU   A OE1  1 
ATOM   2066 O  OE2  . GLU   A 1 273 ? -47.683 -32.563 6.232  1.00 38.97 ? 276  GLU   A OE2  1 
ATOM   2067 N  N    . LEU   A 1 274 ? -41.998 -34.311 9.721  1.00 16.94 ? 277  LEU   A N    1 
ATOM   2068 C  CA   . LEU   A 1 274 ? -40.830 -33.904 10.498 1.00 16.52 ? 277  LEU   A CA   1 
ATOM   2069 C  C    . LEU   A 1 274 ? -39.590 -34.696 10.090 1.00 17.99 ? 277  LEU   A C    1 
ATOM   2070 O  O    . LEU   A 1 274 ? -38.469 -34.179 10.159 1.00 17.55 ? 277  LEU   A O    1 
ATOM   2071 C  CB   . LEU   A 1 274 ? -41.114 -34.067 11.993 1.00 15.41 ? 277  LEU   A CB   1 
ATOM   2072 C  CG   . LEU   A 1 274 ? -42.133 -33.093 12.607 1.00 16.44 ? 277  LEU   A CG   1 
ATOM   2073 C  CD1  . LEU   A 1 274 ? -42.200 -33.298 14.114 1.00 18.82 ? 277  LEU   A CD1  1 
ATOM   2074 C  CD2  . LEU   A 1 274 ? -41.818 -31.638 12.272 1.00 17.31 ? 277  LEU   A CD2  1 
ATOM   2075 N  N    . LEU   A 1 275 ? -39.769 -35.933 9.631  1.00 15.05 ? 278  LEU   A N    1 
ATOM   2076 C  CA   . LEU   A 1 275 ? -38.623 -36.683 9.131  1.00 17.65 ? 278  LEU   A CA   1 
ATOM   2077 C  C    . LEU   A 1 275 ? -38.129 -36.088 7.819  1.00 20.27 ? 278  LEU   A C    1 
ATOM   2078 O  O    . LEU   A 1 275 ? -36.917 -35.941 7.616  1.00 16.99 ? 278  LEU   A O    1 
ATOM   2079 C  CB   . LEU   A 1 275 ? -38.987 -38.159 8.960  1.00 15.44 ? 278  LEU   A CB   1 
ATOM   2080 C  CG   . LEU   A 1 275 ? -37.886 -39.071 8.401  1.00 19.04 ? 278  LEU   A CG   1 
ATOM   2081 C  CD1  . LEU   A 1 275 ? -36.601 -38.946 9.225  1.00 19.05 ? 278  LEU   A CD1  1 
ATOM   2082 C  CD2  . LEU   A 1 275 ? -38.357 -40.532 8.344  1.00 19.85 ? 278  LEU   A CD2  1 
ATOM   2083 N  N    . GLU   A 1 276 ? -39.058 -35.749 6.918  1.00 18.10 ? 279  GLU   A N    1 
ATOM   2084 C  CA   . GLU   A 1 276 ? -38.720 -34.988 5.716  1.00 20.97 ? 279  GLU   A CA   1 
ATOM   2085 C  C    . GLU   A 1 276 ? -37.925 -33.726 6.052  1.00 21.44 ? 279  GLU   A C    1 
ATOM   2086 O  O    . GLU   A 1 276 ? -36.920 -33.410 5.401  1.00 21.05 ? 279  GLU   A O    1 
ATOM   2087 C  CB   . GLU   A 1 276 ? -40.012 -34.620 4.985  1.00 25.62 ? 279  GLU   A CB   1 
ATOM   2088 C  CG   . GLU   A 1 276 ? -39.831 -33.907 3.654  1.00 33.26 ? 279  GLU   A CG   1 
ATOM   2089 C  CD   . GLU   A 1 276 ? -41.152 -33.721 2.895  1.00 47.50 ? 279  GLU   A CD   1 
ATOM   2090 O  OE1  . GLU   A 1 276 ? -42.245 -33.849 3.513  1.00 41.18 ? 279  GLU   A OE1  1 
ATOM   2091 O  OE2  . GLU   A 1 276 ? -41.083 -33.417 1.678  1.00 49.70 ? 279  GLU   A OE2  1 
ATOM   2092 N  N    . THR   A 1 277 ? -38.376 -32.980 7.063  1.00 18.52 ? 280  THR   A N    1 
ATOM   2093 C  CA   . THR   A 1 277 ? -37.645 -31.789 7.490  1.00 19.95 ? 280  THR   A CA   1 
ATOM   2094 C  C    . THR   A 1 277 ? -36.231 -32.144 7.955  1.00 19.76 ? 280  THR   A C    1 
ATOM   2095 O  O    . THR   A 1 277 ? -35.253 -31.476 7.592  1.00 18.95 ? 280  THR   A O    1 
ATOM   2096 C  CB   . THR   A 1 277 ? -38.416 -31.096 8.611  1.00 17.56 ? 280  THR   A CB   1 
ATOM   2097 O  OG1  . THR   A 1 277 ? -39.726 -30.732 8.145  1.00 22.48 ? 280  THR   A OG1  1 
ATOM   2098 C  CG2  . THR   A 1 277 ? -37.672 -29.868 9.114  1.00 17.28 ? 280  THR   A CG2  1 
ATOM   2099 N  N    . THR   A 1 278 ? -36.117 -33.188 8.778  1.00 16.77 ? 281  THR   A N    1 
ATOM   2100 C  CA   . THR   A 1 278 ? -34.818 -33.650 9.265  1.00 18.52 ? 281  THR   A CA   1 
ATOM   2101 C  C    . THR   A 1 278 ? -33.868 -33.916 8.102  1.00 20.52 ? 281  THR   A C    1 
ATOM   2102 O  O    . THR   A 1 278 ? -32.713 -33.465 8.097  1.00 17.80 ? 281  THR   A O    1 
ATOM   2103 C  CB   . THR   A 1 278 ? -35.021 -34.921 10.104 1.00 16.13 ? 281  THR   A CB   1 
ATOM   2104 O  OG1  . THR   A 1 278 ? -35.812 -34.615 11.267 1.00 16.68 ? 281  THR   A OG1  1 
ATOM   2105 C  CG2  . THR   A 1 278 ? -33.673 -35.533 10.555 1.00 19.13 ? 281  THR   A CG2  1 
ATOM   2106 N  N    . LEU   A 1 279 ? -34.355 -34.642 7.099  1.00 17.73 ? 282  LEU   A N    1 
ATOM   2107 C  CA   . LEU   A 1 279 ? -33.504 -35.016 5.976  1.00 21.77 ? 282  LEU   A CA   1 
ATOM   2108 C  C    . LEU   A 1 279 ? -33.135 -33.798 5.141  1.00 21.09 ? 282  LEU   A C    1 
ATOM   2109 O  O    . LEU   A 1 279 ? -32.005 -33.702 4.645  1.00 21.46 ? 282  LEU   A O    1 
ATOM   2110 C  CB   . LEU   A 1 279 ? -34.191 -36.078 5.119  1.00 22.43 ? 282  LEU   A CB   1 
ATOM   2111 C  CG   . LEU   A 1 279 ? -34.432 -37.424 5.837  1.00 25.42 ? 282  LEU   A CG   1 
ATOM   2112 C  CD1  . LEU   A 1 279 ? -35.232 -38.402 4.977  1.00 27.69 ? 282  LEU   A CD1  1 
ATOM   2113 C  CD2  . LEU   A 1 279 ? -33.145 -38.064 6.319  1.00 23.18 ? 282  LEU   A CD2  1 
ATOM   2114 N  N    . LYS   A 1 280 ? -34.070 -32.854 4.979  1.00 20.70 ? 283  LYS   A N    1 
ATOM   2115 C  CA   . LYS   A 1 280 ? -33.757 -31.619 4.262  1.00 20.15 ? 283  LYS   A CA   1 
ATOM   2116 C  C    . LYS   A 1 280 ? -32.695 -30.790 4.974  1.00 22.28 ? 283  LYS   A C    1 
ATOM   2117 O  O    . LYS   A 1 280 ? -31.922 -30.092 4.312  1.00 24.60 ? 283  LYS   A O    1 
ATOM   2118 C  CB   . LYS   A 1 280 ? -35.023 -30.779 4.070  1.00 21.79 ? 283  LYS   A CB   1 
ATOM   2119 C  CG   . LYS   A 1 280 ? -35.942 -31.281 2.959  1.00 24.71 ? 283  LYS   A CG   1 
ATOM   2120 C  CD   . LYS   A 1 280 ? -37.213 -30.439 2.877  1.00 29.00 ? 283  LYS   A CD   1 
ATOM   2121 C  CE   . LYS   A 1 280 ? -38.248 -31.090 1.972  1.00 34.10 ? 283  LYS   A CE   1 
ATOM   2122 N  NZ   . LYS   A 1 280 ? -39.564 -30.394 2.017  1.00 39.01 ? 283  LYS   A NZ   1 
ATOM   2123 N  N    . MET   A 1 281 ? -32.652 -30.825 6.311  1.00 19.49 ? 284  MET   A N    1 
ATOM   2124 C  CA   . MET   A 1 281 ? -31.647 -30.057 7.043  1.00 20.15 ? 284  MET   A CA   1 
ATOM   2125 C  C    . MET   A 1 281 ? -30.235 -30.638 6.896  1.00 23.91 ? 284  MET   A C    1 
ATOM   2126 O  O    . MET   A 1 281 ? -29.258 -29.930 7.166  1.00 22.78 ? 284  MET   A O    1 
ATOM   2127 C  CB   . MET   A 1 281 ? -32.013 -30.004 8.530  1.00 20.48 ? 284  MET   A CB   1 
ATOM   2128 C  CG   . MET   A 1 281 ? -33.324 -29.268 8.851  1.00 22.81 ? 284  MET   A CG   1 
ATOM   2129 S  SD   . MET   A 1 281 ? -33.262 -27.480 8.781  1.00 34.92 ? 284  MET   A SD   1 
ATOM   2130 C  CE   . MET   A 1 281 ? -31.823 -27.081 9.768  1.00 25.84 ? 284  MET   A CE   1 
ATOM   2131 N  N    . LYS   A 1 282 ? -30.111 -31.906 6.507  1.00 20.20 ? 285  LYS   A N    1 
ATOM   2132 C  CA   . LYS   A 1 282 ? -28.820 -32.583 6.319  1.00 24.02 ? 285  LYS   A CA   1 
ATOM   2133 C  C    . LYS   A 1 282 ? -27.930 -32.448 7.554  1.00 23.52 ? 285  LYS   A C    1 
ATOM   2134 O  O    . LYS   A 1 282 ? -26.806 -31.939 7.498  1.00 25.41 ? 285  LYS   A O    1 
ATOM   2135 C  CB   . LYS   A 1 282 ? -28.082 -32.053 5.086  1.00 27.61 ? 285  LYS   A CB   1 
ATOM   2136 C  CG   . LYS   A 1 282 ? -28.851 -32.162 3.787  1.00 33.56 ? 285  LYS   A CG   1 
ATOM   2137 C  CD   . LYS   A 1 282 ? -28.309 -33.274 2.902  1.00 42.14 ? 285  LYS   A CD   1 
ATOM   2138 C  CE   . LYS   A 1 282 ? -29.386 -33.799 1.944  1.00 45.21 ? 285  LYS   A CE   1 
ATOM   2139 N  NZ   . LYS   A 1 282 ? -28.976 -33.692 0.497  1.00 44.31 ? 285  LYS   A NZ   1 
ATOM   2140 N  N    . PHE   A 1 283 ? -28.449 -32.918 8.682  1.00 19.58 ? 286  PHE   A N    1 
ATOM   2141 C  CA   . PHE   A 1 283 ? -27.659 -32.937 9.903  1.00 21.46 ? 286  PHE   A CA   1 
ATOM   2142 C  C    . PHE   A 1 283 ? -26.537 -33.974 9.790  1.00 25.75 ? 286  PHE   A C    1 
ATOM   2143 O  O    . PHE   A 1 283 ? -26.520 -34.815 8.887  1.00 24.54 ? 286  PHE   A O    1 
ATOM   2144 C  CB   . PHE   A 1 283 ? -28.560 -33.243 11.099 1.00 17.93 ? 286  PHE   A CB   1 
ATOM   2145 C  CG   . PHE   A 1 283 ? -29.537 -32.137 11.414 1.00 21.45 ? 286  PHE   A CG   1 
ATOM   2146 C  CD1  . PHE   A 1 283 ? -29.080 -30.873 11.762 1.00 21.48 ? 286  PHE   A CD1  1 
ATOM   2147 C  CD2  . PHE   A 1 283 ? -30.900 -32.353 11.324 1.00 20.11 ? 286  PHE   A CD2  1 
ATOM   2148 C  CE1  . PHE   A 1 283 ? -29.966 -29.843 12.045 1.00 22.84 ? 286  PHE   A CE1  1 
ATOM   2149 C  CE2  . PHE   A 1 283 ? -31.802 -31.339 11.599 1.00 21.46 ? 286  PHE   A CE2  1 
ATOM   2150 C  CZ   . PHE   A 1 283 ? -31.338 -30.072 11.956 1.00 21.82 ? 286  PHE   A CZ   1 
ATOM   2151 N  N    . LEU   A 1 284 ? -25.571 -33.891 10.704 1.00 22.82 ? 287  LEU   A N    1 
ATOM   2152 C  CA   . LEU   A 1 284 ? -24.491 -34.871 10.812 1.00 25.53 ? 287  LEU   A CA   1 
ATOM   2153 C  C    . LEU   A 1 284 ? -23.585 -34.893 9.585  1.00 33.71 ? 287  LEU   A C    1 
ATOM   2154 O  O    . LEU   A 1 284 ? -22.689 -35.737 9.521  1.00 41.26 ? 287  LEU   A O    1 
ATOM   2155 C  CB   . LEU   A 1 284 ? -25.029 -36.294 11.029 1.00 29.74 ? 287  LEU   A CB   1 
ATOM   2156 C  CG   . LEU   A 1 284 ? -25.589 -36.617 12.410 1.00 30.26 ? 287  LEU   A CG   1 
ATOM   2157 C  CD1  . LEU   A 1 284 ? -25.710 -38.144 12.582 1.00 29.23 ? 287  LEU   A CD1  1 
ATOM   2158 C  CD2  . LEU   A 1 284 ? -24.744 -35.981 13.506 1.00 29.02 ? 287  LEU   A CD2  1 
ATOM   2159 N  N    . SER   A 1 285 ? -23.816 -34.038 8.593  1.00 26.39 ? 288  SER   A N    1 
ATOM   2160 C  CA   . SER   A 1 285 ? -22.993 -33.948 7.395  1.00 26.85 ? 288  SER   A CA   1 
ATOM   2161 C  C    . SER   A 1 285 ? -22.241 -32.632 7.459  1.00 27.60 ? 288  SER   A C    1 
ATOM   2162 O  O    . SER   A 1 285 ? -22.844 -31.597 7.764  1.00 29.55 ? 288  SER   A O    1 
ATOM   2163 C  CB   . SER   A 1 285 ? -23.851 -33.972 6.126  1.00 28.96 ? 288  SER   A CB   1 
ATOM   2164 O  OG   . SER   A 1 285 ? -24.226 -35.289 5.772  1.00 41.17 ? 288  SER   A OG   1 
ATOM   2165 N  N    . LEU   A 1 286 ? -20.942 -32.661 7.166  1.00 25.57 ? 289  LEU   A N    1 
ATOM   2166 C  CA   . LEU   A 1 286 ? -20.178 -31.418 7.191  1.00 26.41 ? 289  LEU   A CA   1 
ATOM   2167 C  C    . LEU   A 1 286 ? -20.712 -30.442 6.151  1.00 25.86 ? 289  LEU   A C    1 
ATOM   2168 O  O    . LEU   A 1 286 ? -20.829 -30.767 4.963  1.00 22.65 ? 289  LEU   A O    1 
ATOM   2169 C  CB   . LEU   A 1 286 ? -18.693 -31.680 6.970  1.00 27.96 ? 289  LEU   A CB   1 
ATOM   2170 C  CG   . LEU   A 1 286 ? -17.872 -30.389 6.943  1.00 30.10 ? 289  LEU   A CG   1 
ATOM   2171 C  CD1  . LEU   A 1 286 ? -17.764 -29.815 8.343  1.00 27.30 ? 289  LEU   A CD1  1 
ATOM   2172 C  CD2  . LEU   A 1 286 ? -16.485 -30.705 6.383  1.00 28.42 ? 289  LEU   A CD2  1 
ATOM   2173 N  N    . ASP   A 1 287 ? -21.040 -29.241 6.614  1.00 26.01 ? 290  ASP   A N    1 
ATOM   2174 C  CA   . ASP   A 1 287 ? -21.740 -28.239 5.818  1.00 27.02 ? 290  ASP   A CA   1 
ATOM   2175 C  C    . ASP   A 1 287 ? -20.681 -27.415 5.091  1.00 29.20 ? 290  ASP   A C    1 
ATOM   2176 O  O    . ASP   A 1 287 ? -19.882 -26.718 5.723  1.00 26.15 ? 290  ASP   A O    1 
ATOM   2177 C  CB   . ASP   A 1 287 ? -22.632 -27.413 6.750  1.00 27.29 ? 290  ASP   A CB   1 
ATOM   2178 C  CG   . ASP   A 1 287 ? -23.285 -26.197 6.088  1.00 29.66 ? 290  ASP   A CG   1 
ATOM   2179 O  OD1  . ASP   A 1 287 ? -22.884 -25.760 4.986  1.00 31.83 ? 290  ASP   A OD1  1 
ATOM   2180 O  OD2  . ASP   A 1 287 ? -24.258 -25.689 6.702  1.00 28.26 ? 290  ASP   A OD2  1 
ATOM   2181 N  N    . LEU   A 1 288 ? -20.654 -27.519 3.762  1.00 27.97 ? 291  LEU   A N    1 
ATOM   2182 C  CA   . LEU   A 1 288 ? -19.662 -26.827 2.948  1.00 31.07 ? 291  LEU   A CA   1 
ATOM   2183 C  C    . LEU   A 1 288 ? -20.252 -25.684 2.132  1.00 33.42 ? 291  LEU   A C    1 
ATOM   2184 O  O    . LEU   A 1 288 ? -19.586 -25.179 1.222  1.00 36.34 ? 291  LEU   A O    1 
ATOM   2185 C  CB   . LEU   A 1 288 ? -18.960 -27.823 2.023  1.00 31.04 ? 291  LEU   A CB   1 
ATOM   2186 C  CG   . LEU   A 1 288 ? -18.138 -28.886 2.756  1.00 28.37 ? 291  LEU   A CG   1 
ATOM   2187 C  CD1  . LEU   A 1 288 ? -17.626 -29.951 1.791  1.00 28.15 ? 291  LEU   A CD1  1 
ATOM   2188 C  CD2  . LEU   A 1 288 ? -16.979 -28.235 3.511  1.00 26.81 ? 291  LEU   A CD2  1 
ATOM   2189 N  N    . GLN   A 1 289 ? -21.474 -25.254 2.438  1.00 30.82 ? 292  GLN   A N    1 
ATOM   2190 C  CA   . GLN   A 1 289 ? -22.159 -24.194 1.698  1.00 30.83 ? 292  GLN   A CA   1 
ATOM   2191 C  C    . GLN   A 1 289 ? -22.366 -22.992 2.609  1.00 30.13 ? 292  GLN   A C    1 
ATOM   2192 O  O    . GLN   A 1 289 ? -23.230 -23.016 3.492  1.00 32.26 ? 292  GLN   A O    1 
ATOM   2193 C  CB   . GLN   A 1 289 ? -23.494 -24.686 1.134  1.00 30.74 ? 292  GLN   A CB   1 
ATOM   2194 C  CG   . GLN   A 1 289 ? -23.561 -26.181 0.931  1.00 39.09 ? 292  GLN   A CG   1 
ATOM   2195 C  CD   . GLN   A 1 289 ? -24.964 -26.669 0.595  1.00 42.93 ? 292  GLN   A CD   1 
ATOM   2196 O  OE1  . GLN   A 1 289 ? -25.792 -25.919 0.040  1.00 36.47 ? 292  GLN   A OE1  1 
ATOM   2197 N  NE2  . GLN   A 1 289 ? -25.227 -27.947 0.894  1.00 35.30 ? 292  GLN   A NE2  1 
ATOM   2198 N  N    . GLY   A 1 290 ? -21.585 -21.945 2.384  1.00 31.48 ? 293  GLY   A N    1 
ATOM   2199 C  CA   . GLY   A 1 290 ? -21.763 -20.692 3.090  1.00 32.63 ? 293  GLY   A CA   1 
ATOM   2200 C  C    . GLY   A 1 290 ? -20.798 -20.527 4.246  1.00 33.82 ? 293  GLY   A C    1 
ATOM   2201 O  O    . GLY   A 1 290 ? -19.803 -21.246 4.398  1.00 30.66 ? 293  GLY   A O    1 
ATOM   2202 N  N    . ASP   A 1 291 ? -21.118 -19.539 5.073  1.00 30.44 ? 294  ASP   A N    1 
ATOM   2203 C  CA   . ASP   A 1 291 ? -20.334 -19.222 6.263  1.00 32.72 ? 294  ASP   A CA   1 
ATOM   2204 C  C    . ASP   A 1 291 ? -20.409 -20.363 7.274  1.00 27.38 ? 294  ASP   A C    1 
ATOM   2205 O  O    . ASP   A 1 291 ? -21.508 -20.688 7.746  1.00 25.02 ? 294  ASP   A O    1 
ATOM   2206 C  CB   . ASP   A 1 291 ? -20.859 -17.912 6.863  1.00 32.62 ? 294  ASP   A CB   1 
ATOM   2207 C  CG   . ASP   A 1 291 ? -20.026 -17.404 8.035  1.00 35.68 ? 294  ASP   A CG   1 
ATOM   2208 O  OD1  . ASP   A 1 291 ? -19.149 -18.133 8.533  1.00 32.10 ? 294  ASP   A OD1  1 
ATOM   2209 O  OD2  . ASP   A 1 291 ? -20.280 -16.266 8.487  1.00 45.23 ? 294  ASP   A OD2  1 
ATOM   2210 N  N    . PRO   A 1 292 ? -19.282 -20.980 7.648  1.00 26.12 ? 295  PRO   A N    1 
ATOM   2211 C  CA   . PRO   A 1 292 ? -19.343 -22.117 8.587  1.00 29.46 ? 295  PRO   A CA   1 
ATOM   2212 C  C    . PRO   A 1 292 ? -19.779 -21.728 9.985  1.00 29.02 ? 295  PRO   A C    1 
ATOM   2213 O  O    . PRO   A 1 292 ? -20.148 -22.610 10.771 1.00 25.73 ? 295  PRO   A O    1 
ATOM   2214 C  CB   . PRO   A 1 292 ? -17.908 -22.665 8.584  1.00 27.70 ? 295  PRO   A CB   1 
ATOM   2215 C  CG   . PRO   A 1 292 ? -17.051 -21.527 8.122  1.00 27.99 ? 295  PRO   A CG   1 
ATOM   2216 C  CD   . PRO   A 1 292 ? -17.904 -20.677 7.212  1.00 27.33 ? 295  PRO   A CD   1 
ATOM   2217 N  N    . ARG   A 1 293 ? -19.762 -20.440 10.321 1.00 28.17 ? 296  ARG   A N    1 
ATOM   2218 C  CA   . ARG   A 1 293 ? -20.299 -20.016 11.607 1.00 28.73 ? 296  ARG   A CA   1 
ATOM   2219 C  C    . ARG   A 1 293 ? -21.806 -20.204 11.695 1.00 29.77 ? 296  ARG   A C    1 
ATOM   2220 O  O    . ARG   A 1 293 ? -22.344 -20.227 12.808 1.00 31.60 ? 296  ARG   A O    1 
ATOM   2221 C  CB   . ARG   A 1 293 ? -19.940 -18.556 11.873 1.00 30.91 ? 296  ARG   A CB   1 
ATOM   2222 C  CG   . ARG   A 1 293 ? -18.550 -18.362 12.442 1.00 32.88 ? 296  ARG   A CG   1 
ATOM   2223 C  CD   . ARG   A 1 293 ? -18.180 -16.890 12.424 1.00 38.17 ? 296  ARG   A CD   1 
ATOM   2224 N  NE   . ARG   A 1 293 ? -18.369 -16.323 11.096 1.00 41.74 ? 296  ARG   A NE   1 
ATOM   2225 C  CZ   . ARG   A 1 293 ? -18.126 -15.059 10.782 1.00 46.97 ? 296  ARG   A CZ   1 
ATOM   2226 N  NH1  . ARG   A 1 293 ? -17.720 -14.188 11.692 1.00 45.92 ? 296  ARG   A NH1  1 
ATOM   2227 N  NH2  . ARG   A 1 293 ? -18.302 -14.658 9.526  1.00 45.45 ? 296  ARG   A NH2  1 
ATOM   2228 N  N    . GLU   A 1 294 ? -22.499 -20.340 10.558 1.00 28.77 ? 297  GLU   A N    1 
ATOM   2229 C  CA   . GLU   A 1 294 ? -23.930 -20.618 10.561 1.00 29.16 ? 297  GLU   A CA   1 
ATOM   2230 C  C    . GLU   A 1 294 ? -24.250 -22.101 10.413 1.00 30.84 ? 297  GLU   A C    1 
ATOM   2231 O  O    . GLU   A 1 294 ? -25.429 -22.458 10.354 1.00 30.68 ? 297  GLU   A O    1 
ATOM   2232 C  CB   . GLU   A 1 294 ? -24.645 -19.854 9.442  1.00 30.92 ? 297  GLU   A CB   1 
ATOM   2233 C  CG   . GLU   A 1 294 ? -24.228 -18.412 9.262  1.00 35.87 ? 297  GLU   A CG   1 
ATOM   2234 C  CD   . GLU   A 1 294 ? -24.483 -17.928 7.839  1.00 49.09 ? 297  GLU   A CD   1 
ATOM   2235 O  OE1  . GLU   A 1 294 ? -25.269 -16.969 7.663  1.00 52.78 ? 297  GLU   A OE1  1 
ATOM   2236 O  OE2  . GLU   A 1 294 ? -23.941 -18.542 6.891  1.00 51.30 ? 297  GLU   A OE2  1 
ATOM   2237 N  N    . SER   A 1 295 ? -23.241 -22.965 10.334 1.00 25.74 ? 298  SER   A N    1 
ATOM   2238 C  CA   . SER   A 1 295 ? -23.488 -24.398 10.214 1.00 29.05 ? 298  SER   A CA   1 
ATOM   2239 C  C    . SER   A 1 295 ? -24.070 -24.969 11.500 1.00 31.32 ? 298  SER   A C    1 
ATOM   2240 O  O    . SER   A 1 295 ? -23.623 -24.639 12.604 1.00 27.11 ? 298  SER   A O    1 
ATOM   2241 C  CB   . SER   A 1 295 ? -22.191 -25.130 9.878  1.00 26.87 ? 298  SER   A CB   1 
ATOM   2242 O  OG   . SER   A 1 295 ? -21.684 -24.695 8.630  1.00 24.61 ? 298  SER   A OG   1 
ATOM   2243 N  N    . GLN   A 1 296 ? -25.056 -25.857 11.351 1.00 30.33 ? 299  GLN   A N    1 
ATOM   2244 C  CA   . GLN   A 1 296 ? -25.675 -26.550 12.482 1.00 32.95 ? 299  GLN   A CA   1 
ATOM   2245 C  C    . GLN   A 1 296 ? -25.740 -28.050 12.218 1.00 26.38 ? 299  GLN   A C    1 
ATOM   2246 O  O    . GLN   A 1 296 ? -26.729 -28.553 11.667 1.00 24.05 ? 299  GLN   A O    1 
ATOM   2247 C  CB   . GLN   A 1 296 ? -27.063 -25.987 12.778 1.00 33.71 ? 299  GLN   A CB   1 
ATOM   2248 C  CG   . GLN   A 1 296 ? -27.166 -24.467 12.638 1.00 37.73 ? 299  GLN   A CG   1 
ATOM   2249 C  CD   . GLN   A 1 296 ? -27.142 -23.764 13.993 1.00 40.58 ? 299  GLN   A CD   1 
ATOM   2250 O  OE1  . GLN   A 1 296 ? -26.829 -24.381 15.024 1.00 42.30 ? 299  GLN   A OE1  1 
ATOM   2251 N  NE2  . GLN   A 1 296 ? -27.473 -22.469 13.999 1.00 36.54 ? 299  GLN   A NE2  1 
ATOM   2252 N  N    . PRO   A 1 297 ? -24.713 -28.803 12.624 1.00 26.04 ? 300  PRO   A N    1 
ATOM   2253 C  CA   . PRO   A 1 297 ? -24.671 -30.235 12.278 1.00 25.43 ? 300  PRO   A CA   1 
ATOM   2254 C  C    . PRO   A 1 297 ? -25.629 -31.100 13.077 1.00 24.89 ? 300  PRO   A C    1 
ATOM   2255 O  O    . PRO   A 1 297 ? -25.887 -32.234 12.661 1.00 22.60 ? 300  PRO   A O    1 
ATOM   2256 C  CB   . PRO   A 1 297 ? -23.211 -30.625 12.557 1.00 29.83 ? 300  PRO   A CB   1 
ATOM   2257 C  CG   . PRO   A 1 297 ? -22.744 -29.636 13.548 1.00 29.11 ? 300  PRO   A CG   1 
ATOM   2258 C  CD   . PRO   A 1 297 ? -23.474 -28.350 13.270 1.00 31.64 ? 300  PRO   A CD   1 
ATOM   2259 N  N    . LEU   A 1 298 ? -26.151 -30.625 14.206 1.00 29.19 ? 301  LEU   A N    1 
ATOM   2260 C  CA   . LEU   A 1 298 ? -27.095 -31.420 14.978 1.00 24.99 ? 301  LEU   A CA   1 
ATOM   2261 C  C    . LEU   A 1 298 ? -27.862 -30.512 15.925 1.00 28.57 ? 301  LEU   A C    1 
ATOM   2262 O  O    . LEU   A 1 298 ? -27.414 -29.411 16.259 1.00 24.63 ? 301  LEU   A O    1 
ATOM   2263 C  CB   . LEU   A 1 298 ? -26.379 -32.520 15.758 1.00 23.41 ? 301  LEU   A CB   1 
ATOM   2264 C  CG   . LEU   A 1 298 ? -25.172 -32.039 16.565 1.00 26.32 ? 301  LEU   A CG   1 
ATOM   2265 C  CD1  . LEU   A 1 298 ? -25.595 -31.632 17.983 1.00 28.25 ? 301  LEU   A CD1  1 
ATOM   2266 C  CD2  . LEU   A 1 298 ? -24.085 -33.101 16.600 1.00 21.88 ? 301  LEU   A CD2  1 
ATOM   2267 N  N    . LEU   A 1 299 ? -29.024 -30.994 16.363 1.00 27.24 ? 302  LEU   A N    1 
ATOM   2268 C  CA   . LEU   A 1 299 ? -29.732 -30.389 17.481 1.00 22.94 ? 302  LEU   A CA   1 
ATOM   2269 C  C    . LEU   A 1 299 ? -29.269 -31.064 18.756 1.00 25.35 ? 302  LEU   A C    1 
ATOM   2270 O  O    . LEU   A 1 299 ? -29.355 -32.294 18.881 1.00 30.52 ? 302  LEU   A O    1 
ATOM   2271 C  CB   . LEU   A 1 299 ? -31.240 -30.553 17.349 1.00 22.85 ? 302  LEU   A CB   1 
ATOM   2272 C  CG   . LEU   A 1 299 ? -31.756 -30.003 16.045 1.00 28.47 ? 302  LEU   A CG   1 
ATOM   2273 C  CD1  . LEU   A 1 299 ? -32.381 -31.101 15.236 1.00 24.16 ? 302  LEU   A CD1  1 
ATOM   2274 C  CD2  . LEU   A 1 299 ? -32.759 -28.996 16.447 1.00 39.64 ? 302  LEU   A CD2  1 
ATOM   2275 N  N    . GLY   A 1 300 ? -28.798 -30.271 19.699 1.00 23.07 ? 303  GLY   A N    1 
ATOM   2276 C  CA   . GLY   A 1 300 ? -28.215 -30.865 20.872 1.00 20.45 ? 303  GLY   A CA   1 
ATOM   2277 C  C    . GLY   A 1 300 ? -28.681 -30.238 22.160 1.00 17.02 ? 303  GLY   A C    1 
ATOM   2278 O  O    . GLY   A 1 300 ? -29.750 -29.612 22.228 1.00 16.65 ? 303  GLY   A O    1 
ATOM   2279 N  N    . THR   A 1 301 ? -27.852 -30.421 23.178 1.00 13.97 ? 304  THR   A N    1 
ATOM   2280 C  CA   . THR   A 1 301 ? -28.133 -29.958 24.526 1.00 12.74 ? 304  THR   A CA   1 
ATOM   2281 C  C    . THR   A 1 301 ? -28.131 -28.437 24.559 1.00 16.04 ? 304  THR   A C    1 
ATOM   2282 O  O    . THR   A 1 301 ? -27.248 -27.803 23.974 1.00 16.12 ? 304  THR   A O    1 
ATOM   2283 C  CB   . THR   A 1 301 ? -27.048 -30.492 25.466 1.00 11.70 ? 304  THR   A CB   1 
ATOM   2284 O  OG1  . THR   A 1 301 ? -26.865 -31.909 25.251 1.00 13.89 ? 304  THR   A OG1  1 
ATOM   2285 C  CG2  . THR   A 1 301 ? -27.401 -30.225 26.909 1.00 15.59 ? 304  THR   A CG2  1 
ATOM   2286 N  N    . VAL   A 1 302 ? -29.100 -27.848 25.267 1.00 14.32 ? 305  VAL   A N    1 
ATOM   2287 C  CA   . VAL   A 1 302 ? -29.110 -26.404 25.495 1.00 13.79 ? 305  VAL   A CA   1 
ATOM   2288 C  C    . VAL   A 1 302 ? -29.067 -26.151 27.000 1.00 15.24 ? 305  VAL   A C    1 
ATOM   2289 O  O    . VAL   A 1 302 ? -29.225 -27.059 27.809 1.00 15.40 ? 305  VAL   A O    1 
ATOM   2290 C  CB   . VAL   A 1 302 ? -30.338 -25.703 24.867 1.00 15.60 ? 305  VAL   A CB   1 
ATOM   2291 C  CG1  . VAL   A 1 302 ? -30.382 -25.938 23.354 1.00 16.59 ? 305  VAL   A CG1  1 
ATOM   2292 C  CG2  . VAL   A 1 302 ? -31.615 -26.188 25.527 1.00 13.79 ? 305  VAL   A CG2  1 
ATOM   2293 N  N    . ILE   A 1 303 ? -28.870 -24.887 27.365 1.00 13.39 ? 306  ILE   A N    1 
ATOM   2294 C  CA   . ILE   A 1 303 ? -28.973 -24.469 28.763 1.00 12.30 ? 306  ILE   A CA   1 
ATOM   2295 C  C    . ILE   A 1 303 ? -30.426 -24.046 28.943 1.00 15.53 ? 306  ILE   A C    1 
ATOM   2296 O  O    . ILE   A 1 303 ? -30.800 -22.915 28.651 1.00 19.42 ? 306  ILE   A O    1 
ATOM   2297 C  CB   . ILE   A 1 303 ? -27.993 -23.352 29.108 1.00 17.60 ? 306  ILE   A CB   1 
ATOM   2298 C  CG1  . ILE   A 1 303 ? -26.586 -23.658 28.564 1.00 17.35 ? 306  ILE   A CG1  1 
ATOM   2299 C  CG2  . ILE   A 1 303 ? -27.995 -23.105 30.609 1.00 15.34 ? 306  ILE   A CG2  1 
ATOM   2300 C  CD1  . ILE   A 1 303 ? -26.068 -25.048 28.936 1.00 17.59 ? 306  ILE   A CD1  1 
ATOM   2301 N  N    . ASP   A 1 304 ? -31.258 -24.975 29.423 1.00 16.95 ? 307  ASP   A N    1 
ATOM   2302 C  CA   . ASP   A 1 304 ? -32.706 -24.780 29.386 1.00 18.51 ? 307  ASP   A CA   1 
ATOM   2303 C  C    . ASP   A 1 304 ? -33.271 -24.180 30.666 1.00 20.71 ? 307  ASP   A C    1 
ATOM   2304 O  O    . ASP   A 1 304 ? -34.399 -23.668 30.652 1.00 21.92 ? 307  ASP   A O    1 
ATOM   2305 C  CB   . ASP   A 1 304 ? -33.400 -26.116 29.117 1.00 20.10 ? 307  ASP   A CB   1 
ATOM   2306 C  CG   . ASP   A 1 304 ? -33.107 -27.156 30.186 1.00 23.36 ? 307  ASP   A CG   1 
ATOM   2307 O  OD1  . ASP   A 1 304 ? -31.919 -27.420 30.494 1.00 22.69 ? 307  ASP   A OD1  1 
ATOM   2308 O  OD2  . ASP   A 1 304 ? -34.072 -27.774 30.669 1.00 22.86 ? 307  ASP   A OD2  1 
ATOM   2309 N  N    . GLY   A 1 305 ? -32.533 -24.251 31.770 1.00 17.03 ? 308  GLY   A N    1 
ATOM   2310 C  CA   . GLY   A 1 305 ? -33.012 -23.776 33.046 1.00 18.96 ? 308  GLY   A CA   1 
ATOM   2311 C  C    . GLY   A 1 305 ? -33.759 -24.788 33.881 1.00 22.25 ? 308  GLY   A C    1 
ATOM   2312 O  O    . GLY   A 1 305 ? -34.145 -24.461 35.008 1.00 22.84 ? 308  GLY   A O    1 
ATOM   2313 N  N    . MET   A 1 306 ? -33.993 -25.997 33.366 1.00 19.29 ? 309  MET   A N    1 
ATOM   2314 C  CA   . MET   A 1 306 ? -34.602 -27.082 34.130 1.00 20.35 ? 309  MET   A CA   1 
ATOM   2315 C  C    . MET   A 1 306 ? -33.610 -28.224 34.316 1.00 19.17 ? 309  MET   A C    1 
ATOM   2316 O  O    . MET   A 1 306 ? -33.281 -28.589 35.450 1.00 18.23 ? 309  MET   A O    1 
ATOM   2317 C  CB   . MET   A 1 306 ? -35.864 -27.589 33.408 1.00 19.60 ? 309  MET   A CB   1 
ATOM   2318 C  CG   . MET   A 1 306 ? -37.083 -26.649 33.452 1.00 24.83 ? 309  MET   A CG   1 
ATOM   2319 S  SD   . MET   A 1 306 ? -37.693 -26.362 35.115 1.00 36.15 ? 309  MET   A SD   1 
ATOM   2320 C  CE   . MET   A 1 306 ? -38.747 -24.927 34.847 1.00 35.77 ? 309  MET   A CE   1 
ATOM   2321 N  N    . LEU   A 1 307 ? -33.113 -28.790 33.218 1.00 17.89 ? 310  LEU   A N    1 
ATOM   2322 C  CA   . LEU   A 1 307 ? -32.101 -29.845 33.304 1.00 20.04 ? 310  LEU   A CA   1 
ATOM   2323 C  C    . LEU   A 1 307 ? -30.714 -29.263 33.564 1.00 20.04 ? 310  LEU   A C    1 
ATOM   2324 O  O    . LEU   A 1 307 ? -30.000 -29.718 34.462 1.00 19.80 ? 310  LEU   A O    1 
ATOM   2325 C  CB   . LEU   A 1 307 ? -32.080 -30.661 32.010 1.00 21.59 ? 310  LEU   A CB   1 
ATOM   2326 C  CG   . LEU   A 1 307 ? -31.016 -31.771 31.957 1.00 20.01 ? 310  LEU   A CG   1 
ATOM   2327 C  CD1  . LEU   A 1 307 ? -31.656 -33.123 32.271 1.00 22.97 ? 310  LEU   A CD1  1 
ATOM   2328 C  CD2  . LEU   A 1 307 ? -30.317 -31.762 30.614 1.00 16.67 ? 310  LEU   A CD2  1 
ATOM   2329 N  N    . LEU   A 1 308 ? -30.314 -28.264 32.780 1.00 18.68 ? 311  LEU   A N    1 
ATOM   2330 C  CA   . LEU   A 1 308 ? -29.050 -27.559 32.975 1.00 20.15 ? 311  LEU   A CA   1 
ATOM   2331 C  C    . LEU   A 1 308 ? -29.366 -26.108 33.302 1.00 20.69 ? 311  LEU   A C    1 
ATOM   2332 O  O    . LEU   A 1 308 ? -30.037 -25.428 32.514 1.00 22.23 ? 311  LEU   A O    1 
ATOM   2333 C  CB   . LEU   A 1 308 ? -28.164 -27.615 31.734 1.00 20.31 ? 311  LEU   A CB   1 
ATOM   2334 C  CG   . LEU   A 1 308 ? -27.333 -28.862 31.466 1.00 23.79 ? 311  LEU   A CG   1 
ATOM   2335 C  CD1  . LEU   A 1 308 ? -26.523 -28.653 30.185 1.00 19.56 ? 311  LEU   A CD1  1 
ATOM   2336 C  CD2  . LEU   A 1 308 ? -26.450 -29.195 32.661 1.00 21.86 ? 311  LEU   A CD2  1 
ATOM   2337 N  N    . LEU   A 1 309 ? -28.885 -25.635 34.457 1.00 18.87 ? 312  LEU   A N    1 
ATOM   2338 C  CA   . LEU   A 1 309 ? -29.200 -24.282 34.906 1.00 21.79 ? 312  LEU   A CA   1 
ATOM   2339 C  C    . LEU   A 1 309 ? -28.173 -23.252 34.458 1.00 21.71 ? 312  LEU   A C    1 
ATOM   2340 O  O    . LEU   A 1 309 ? -28.499 -22.065 34.387 1.00 19.33 ? 312  LEU   A O    1 
ATOM   2341 C  CB   . LEU   A 1 309 ? -29.303 -24.225 36.434 1.00 26.44 ? 312  LEU   A CB   1 
ATOM   2342 C  CG   . LEU   A 1 309 ? -30.261 -25.200 37.127 1.00 30.12 ? 312  LEU   A CG   1 
ATOM   2343 C  CD1  . LEU   A 1 309 ? -30.547 -24.773 38.568 1.00 32.51 ? 312  LEU   A CD1  1 
ATOM   2344 C  CD2  . LEU   A 1 309 ? -31.530 -25.419 36.357 1.00 27.60 ? 312  LEU   A CD2  1 
ATOM   2345 N  N    . LYS   A 1 310 ? -26.930 -23.675 34.210 1.00 19.72 ? 313  LYS   A N    1 
ATOM   2346 C  CA   . LYS   A 1 310 ? -25.891 -22.851 33.607 1.00 21.90 ? 313  LYS   A CA   1 
ATOM   2347 C  C    . LYS   A 1 310 ? -25.041 -23.704 32.671 1.00 20.62 ? 313  LYS   A C    1 
ATOM   2348 O  O    . LYS   A 1 310 ? -25.273 -24.907 32.513 1.00 16.59 ? 313  LYS   A O    1 
ATOM   2349 C  CB   . LYS   A 1 310 ? -25.009 -22.150 34.642 1.00 25.79 ? 313  LYS   A CB   1 
ATOM   2350 C  CG   . LYS   A 1 310 ? -25.708 -21.548 35.852 1.00 27.83 ? 313  LYS   A CG   1 
ATOM   2351 C  CD   . LYS   A 1 310 ? -24.692 -21.297 36.946 1.00 33.80 ? 313  LYS   A CD   1 
ATOM   2352 C  CE   . LYS   A 1 310 ? -25.343 -20.866 38.233 1.00 36.77 ? 313  LYS   A CE   1 
ATOM   2353 N  NZ   . LYS   A 1 310 ? -24.718 -19.618 38.737 1.00 37.08 ? 313  LYS   A NZ   1 
ATOM   2354 N  N    . THR   A 1 311 ? -24.055 -23.066 32.041 1.00 17.08 ? 314  THR   A N    1 
ATOM   2355 C  CA   . THR   A 1 311 ? -23.190 -23.784 31.128 1.00 19.13 ? 314  THR   A CA   1 
ATOM   2356 C  C    . THR   A 1 311 ? -22.341 -24.794 31.905 1.00 17.64 ? 314  THR   A C    1 
ATOM   2357 O  O    . THR   A 1 311 ? -22.050 -24.598 33.088 1.00 16.91 ? 314  THR   A O    1 
ATOM   2358 C  CB   . THR   A 1 311 ? -22.264 -22.832 30.358 1.00 24.66 ? 314  THR   A CB   1 
ATOM   2359 O  OG1  . THR   A 1 311 ? -21.286 -22.299 31.248 1.00 22.01 ? 314  THR   A OG1  1 
ATOM   2360 C  CG2  . THR   A 1 311 ? -23.035 -21.673 29.691 1.00 25.02 ? 314  THR   A CG2  1 
ATOM   2361 N  N    . PRO   A 1 312 ? -21.971 -25.904 31.273 1.00 17.68 ? 315  PRO   A N    1 
ATOM   2362 C  CA   . PRO   A 1 312 ? -21.074 -26.854 31.947 1.00 17.80 ? 315  PRO   A CA   1 
ATOM   2363 C  C    . PRO   A 1 312 ? -19.840 -26.185 32.532 1.00 18.03 ? 315  PRO   A C    1 
ATOM   2364 O  O    . PRO   A 1 312 ? -19.438 -26.514 33.655 1.00 18.21 ? 315  PRO   A O    1 
ATOM   2365 C  CB   . PRO   A 1 312 ? -20.728 -27.848 30.830 1.00 15.43 ? 315  PRO   A CB   1 
ATOM   2366 C  CG   . PRO   A 1 312 ? -21.951 -27.862 29.958 1.00 14.31 ? 315  PRO   A CG   1 
ATOM   2367 C  CD   . PRO   A 1 312 ? -22.395 -26.383 29.945 1.00 16.88 ? 315  PRO   A CD   1 
ATOM   2368 N  N    . GLU   A 1 313 ? -19.258 -25.212 31.833 1.00 16.37 ? 316  GLU   A N    1 
ATOM   2369 C  CA   . GLU   A 1 313 ? -18.078 -24.547 32.380 1.00 18.72 ? 316  GLU   A CA   1 
ATOM   2370 C  C    . GLU   A 1 313 ? -18.405 -23.835 33.696 1.00 21.77 ? 316  GLU   A C    1 
ATOM   2371 O  O    . GLU   A 1 313 ? -17.665 -23.960 34.687 1.00 19.06 ? 316  GLU   A O    1 
ATOM   2372 C  CB   . GLU   A 1 313 ? -17.485 -23.555 31.371 1.00 24.53 ? 316  GLU   A CB   1 
ATOM   2373 C  CG   . GLU   A 1 313 ? -16.934 -24.178 30.072 1.00 28.62 ? 316  GLU   A CG   1 
ATOM   2374 C  CD   . GLU   A 1 313 ? -17.990 -24.573 29.021 1.00 38.89 ? 316  GLU   A CD   1 
ATOM   2375 O  OE1  . GLU   A 1 313 ? -19.216 -24.727 29.315 1.00 27.38 ? 316  GLU   A OE1  1 
ATOM   2376 O  OE2  . GLU   A 1 313 ? -17.551 -24.779 27.861 1.00 42.37 ? 316  GLU   A OE2  1 
ATOM   2377 N  N    . GLU   A 1 314 ? -19.510 -23.076 33.723 1.00 17.42 ? 317  GLU   A N    1 
ATOM   2378 C  CA   . GLU   A 1 314 ? -19.886 -22.378 34.949 1.00 19.72 ? 317  GLU   A CA   1 
ATOM   2379 C  C    . GLU   A 1 314 ? -20.186 -23.345 36.081 1.00 21.94 ? 317  GLU   A C    1 
ATOM   2380 O  O    . GLU   A 1 314 ? -19.789 -23.103 37.228 1.00 19.94 ? 317  GLU   A O    1 
ATOM   2381 C  CB   . GLU   A 1 314 ? -21.071 -21.428 34.718 1.00 22.88 ? 317  GLU   A CB   1 
ATOM   2382 C  CG   . GLU   A 1 314 ? -20.825 -20.389 33.607 1.00 24.71 ? 317  GLU   A CG   1 
ATOM   2383 C  CD   . GLU   A 1 314 ? -22.082 -19.726 33.025 1.00 31.34 ? 317  GLU   A CD   1 
ATOM   2384 O  OE1  . GLU   A 1 314 ? -23.171 -20.341 32.965 1.00 29.77 ? 317  GLU   A OE1  1 
ATOM   2385 O  OE2  . GLU   A 1 314 ? -21.948 -18.569 32.571 1.00 37.97 ? 317  GLU   A OE2  1 
ATOM   2386 N  N    . LEU   A 1 315 ? -20.896 -24.438 35.793 1.00 15.92 ? 318  LEU   A N    1 
ATOM   2387 C  CA   . LEU   A 1 315 ? -21.191 -25.405 36.844 1.00 17.87 ? 318  LEU   A CA   1 
ATOM   2388 C  C    . LEU   A 1 315 ? -19.912 -26.032 37.383 1.00 21.08 ? 318  LEU   A C    1 
ATOM   2389 O  O    . LEU   A 1 315 ? -19.777 -26.262 38.591 1.00 19.81 ? 318  LEU   A O    1 
ATOM   2390 C  CB   . LEU   A 1 315 ? -22.134 -26.484 36.311 1.00 15.95 ? 318  LEU   A CB   1 
ATOM   2391 C  CG   . LEU   A 1 315 ? -23.534 -26.011 35.919 1.00 17.87 ? 318  LEU   A CG   1 
ATOM   2392 C  CD1  . LEU   A 1 315 ? -24.251 -27.120 35.169 1.00 15.20 ? 318  LEU   A CD1  1 
ATOM   2393 C  CD2  . LEU   A 1 315 ? -24.345 -25.554 37.156 1.00 21.19 ? 318  LEU   A CD2  1 
ATOM   2394 N  N    . GLN   A 1 316 ? -18.965 -26.338 36.500 1.00 16.85 ? 319  GLN   A N    1 
ATOM   2395 C  CA   . GLN   A 1 316 ? -17.686 -26.869 36.964 1.00 21.77 ? 319  GLN   A CA   1 
ATOM   2396 C  C    . GLN   A 1 316 ? -16.959 -25.878 37.859 1.00 22.27 ? 319  GLN   A C    1 
ATOM   2397 O  O    . GLN   A 1 316 ? -16.414 -26.258 38.901 1.00 21.82 ? 319  GLN   A O    1 
ATOM   2398 C  CB   . GLN   A 1 316 ? -16.826 -27.235 35.763 1.00 23.71 ? 319  GLN   A CB   1 
ATOM   2399 C  CG   . GLN   A 1 316 ? -17.265 -28.514 35.105 1.00 21.93 ? 319  GLN   A CG   1 
ATOM   2400 C  CD   . GLN   A 1 316 ? -16.451 -28.791 33.865 1.00 30.18 ? 319  GLN   A CD   1 
ATOM   2401 O  OE1  . GLN   A 1 316 ? -16.402 -29.920 33.388 1.00 35.99 ? 319  GLN   A OE1  1 
ATOM   2402 N  NE2  . GLN   A 1 316 ? -15.885 -27.734 33.275 1.00 26.04 ? 319  GLN   A NE2  1 
ATOM   2403 N  N    . ALA   A 1 317 ? -16.943 -24.596 37.475 1.00 21.58 ? 320  ALA   A N    1 
ATOM   2404 C  CA   . ALA   A 1 317 ? -16.252 -23.605 38.295 1.00 25.41 ? 320  ALA   A CA   1 
ATOM   2405 C  C    . ALA   A 1 317 ? -16.902 -23.470 39.665 1.00 27.26 ? 320  ALA   A C    1 
ATOM   2406 O  O    . ALA   A 1 317 ? -16.215 -23.206 40.657 1.00 24.52 ? 320  ALA   A O    1 
ATOM   2407 C  CB   . ALA   A 1 317 ? -16.229 -22.262 37.576 1.00 22.12 ? 320  ALA   A CB   1 
ATOM   2408 N  N    . GLU   A 1 318 ? -18.216 -23.658 39.739 1.00 25.58 ? 321  GLU   A N    1 
ATOM   2409 C  CA   . GLU   A 1 318 ? -18.946 -23.604 40.998 1.00 24.08 ? 321  GLU   A CA   1 
ATOM   2410 C  C    . GLU   A 1 318 ? -18.891 -24.911 41.778 1.00 24.52 ? 321  GLU   A C    1 
ATOM   2411 O  O    . GLU   A 1 318 ? -19.393 -24.957 42.905 1.00 23.54 ? 321  GLU   A O    1 
ATOM   2412 C  CB   . GLU   A 1 318 ? -20.403 -23.250 40.719 1.00 24.09 ? 321  GLU   A CB   1 
ATOM   2413 C  CG   . GLU   A 1 318 ? -20.651 -21.776 40.476 1.00 34.82 ? 321  GLU   A CG   1 
ATOM   2414 C  CD   . GLU   A 1 318 ? -22.119 -21.499 40.167 1.00 42.17 ? 321  GLU   A CD   1 
ATOM   2415 O  OE1  . GLU   A 1 318 ? -22.505 -20.308 40.080 1.00 47.78 ? 321  GLU   A OE1  1 
ATOM   2416 O  OE2  . GLU   A 1 318 ? -22.881 -22.483 40.010 1.00 42.37 ? 321  GLU   A OE2  1 
ATOM   2417 N  N    . ARG   A 1 319 ? -18.315 -25.969 41.204 1.00 19.69 ? 322  ARG   A N    1 
ATOM   2418 C  CA   . ARG   A 1 319 ? -18.295 -27.298 41.819 1.00 21.51 ? 322  ARG   A CA   1 
ATOM   2419 C  C    . ARG   A 1 319 ? -19.706 -27.806 42.085 1.00 22.84 ? 322  ARG   A C    1 
ATOM   2420 O  O    . ARG   A 1 319 ? -19.957 -28.518 43.059 1.00 19.89 ? 322  ARG   A O    1 
ATOM   2421 C  CB   . ARG   A 1 319 ? -17.460 -27.310 43.101 1.00 25.28 ? 322  ARG   A CB   1 
ATOM   2422 C  CG   . ARG   A 1 319 ? -16.042 -26.784 42.889 1.00 26.10 ? 322  ARG   A CG   1 
ATOM   2423 C  CD   . ARG   A 1 319 ? -15.352 -26.398 44.210 1.00 26.10 ? 322  ARG   A CD   1 
ATOM   2424 N  NE   . ARG   A 1 319 ? -15.972 -25.244 44.855 1.00 24.95 ? 322  ARG   A NE   1 
ATOM   2425 C  CZ   . ARG   A 1 319 ? -16.811 -25.320 45.879 1.00 22.21 ? 322  ARG   A CZ   1 
ATOM   2426 N  NH1  . ARG   A 1 319 ? -17.100 -26.478 46.449 1.00 21.61 ? 322  ARG   A NH1  1 
ATOM   2427 N  NH2  . ARG   A 1 319 ? -17.370 -24.206 46.343 1.00 21.70 ? 322  ARG   A NH2  1 
ATOM   2428 N  N    . ASN   A 1 320 ? -20.635 -27.446 41.206 1.00 19.64 ? 323  ASN   A N    1 
ATOM   2429 C  CA   . ASN   A 1 320 ? -22.041 -27.768 41.391 1.00 21.06 ? 323  ASN   A CA   1 
ATOM   2430 C  C    . ASN   A 1 320 ? -22.390 -28.928 40.461 1.00 20.06 ? 323  ASN   A C    1 
ATOM   2431 O  O    . ASN   A 1 320 ? -22.941 -28.744 39.376 1.00 19.56 ? 323  ASN   A O    1 
ATOM   2432 C  CB   . ASN   A 1 320 ? -22.895 -26.527 41.123 1.00 23.73 ? 323  ASN   A CB   1 
ATOM   2433 C  CG   . ASN   A 1 320 ? -24.331 -26.716 41.539 1.00 28.46 ? 323  ASN   A CG   1 
ATOM   2434 O  OD1  . ASN   A 1 320 ? -24.676 -27.729 42.147 1.00 27.27 ? 323  ASN   A OD1  1 
ATOM   2435 N  ND2  . ASN   A 1 320 ? -25.171 -25.729 41.252 1.00 30.97 ? 323  ASN   A ND2  1 
ATOM   2436 N  N    . PHE   A 1 321 ? -22.023 -30.141 40.887 1.00 20.15 ? 324  PHE   A N    1 
ATOM   2437 C  CA   . PHE   A 1 321 ? -22.317 -31.365 40.142 1.00 19.45 ? 324  PHE   A CA   1 
ATOM   2438 C  C    . PHE   A 1 321 ? -22.242 -32.553 41.094 1.00 20.09 ? 324  PHE   A C    1 
ATOM   2439 O  O    . PHE   A 1 321 ? -21.847 -32.413 42.252 1.00 19.73 ? 324  PHE   A O    1 
ATOM   2440 C  CB   . PHE   A 1 321 ? -21.381 -31.543 38.942 1.00 18.53 ? 324  PHE   A CB   1 
ATOM   2441 C  CG   . PHE   A 1 321 ? -19.921 -31.393 39.261 1.00 19.61 ? 324  PHE   A CG   1 
ATOM   2442 C  CD1  . PHE   A 1 321 ? -19.184 -32.464 39.745 1.00 19.50 ? 324  PHE   A CD1  1 
ATOM   2443 C  CD2  . PHE   A 1 321 ? -19.283 -30.171 39.068 1.00 18.22 ? 324  PHE   A CD2  1 
ATOM   2444 C  CE1  . PHE   A 1 321 ? -17.828 -32.328 40.023 1.00 19.45 ? 324  PHE   A CE1  1 
ATOM   2445 C  CE2  . PHE   A 1 321 ? -17.919 -30.023 39.344 1.00 19.75 ? 324  PHE   A CE2  1 
ATOM   2446 C  CZ   . PHE   A 1 321 ? -17.191 -31.104 39.825 1.00 19.42 ? 324  PHE   A CZ   1 
ATOM   2447 N  N    . HIS   A 1 322 ? -22.669 -33.721 40.604 1.00 15.19 ? 325  HIS   A N    1 
ATOM   2448 C  CA   . HIS   A 1 322 ? -22.752 -34.916 41.436 1.00 15.33 ? 325  HIS   A CA   1 
ATOM   2449 C  C    . HIS   A 1 322 ? -21.379 -35.574 41.520 1.00 17.38 ? 325  HIS   A C    1 
ATOM   2450 O  O    . HIS   A 1 322 ? -20.855 -36.059 40.513 1.00 16.68 ? 325  HIS   A O    1 
ATOM   2451 C  CB   . HIS   A 1 322 ? -23.765 -35.901 40.873 1.00 16.25 ? 325  HIS   A CB   1 
ATOM   2452 C  CG   . HIS   A 1 322 ? -25.131 -35.312 40.718 1.00 21.26 ? 325  HIS   A CG   1 
ATOM   2453 N  ND1  . HIS   A 1 322 ? -25.825 -34.767 41.777 1.00 22.68 ? 325  HIS   A ND1  1 
ATOM   2454 C  CD2  . HIS   A 1 322 ? -25.915 -35.154 39.627 1.00 17.21 ? 325  HIS   A CD2  1 
ATOM   2455 C  CE1  . HIS   A 1 322 ? -26.984 -34.301 41.344 1.00 24.88 ? 325  HIS   A CE1  1 
ATOM   2456 N  NE2  . HIS   A 1 322 ? -27.064 -34.522 40.043 1.00 20.45 ? 325  HIS   A NE2  1 
ATOM   2457 N  N    . THR   A 1 323 ? -20.815 -35.616 42.720 1.00 17.77 ? 326  THR   A N    1 
ATOM   2458 C  CA   . THR   A 1 323 ? -19.431 -36.039 42.918 1.00 17.12 ? 326  THR   A CA   1 
ATOM   2459 C  C    . THR   A 1 323 ? -19.318 -37.557 43.076 1.00 18.89 ? 326  THR   A C    1 
ATOM   2460 O  O    . THR   A 1 323 ? -18.692 -38.059 44.009 1.00 19.89 ? 326  THR   A O    1 
ATOM   2461 C  CB   . THR   A 1 323 ? -18.838 -35.298 44.117 1.00 21.35 ? 326  THR   A CB   1 
ATOM   2462 O  OG1  . THR   A 1 323 ? -19.643 -35.512 45.285 1.00 19.29 ? 326  THR   A OG1  1 
ATOM   2463 C  CG2  . THR   A 1 323 ? -18.783 -33.790 43.853 1.00 17.33 ? 326  THR   A CG2  1 
ATOM   2464 N  N    . VAL   A 1 324 ? -19.933 -38.303 42.155 1.00 16.06 ? 327  VAL   A N    1 
ATOM   2465 C  CA   . VAL   A 1 324 ? -19.908 -39.766 42.170 1.00 14.62 ? 327  VAL   A CA   1 
ATOM   2466 C  C    . VAL   A 1 324 ? -18.583 -40.234 41.577 1.00 13.08 ? 327  VAL   A C    1 
ATOM   2467 O  O    . VAL   A 1 324 ? -17.940 -39.461 40.862 1.00 13.91 ? 327  VAL   A O    1 
ATOM   2468 C  CB   . VAL   A 1 324 ? -21.078 -40.367 41.372 1.00 19.96 ? 327  VAL   A CB   1 
ATOM   2469 C  CG1  . VAL   A 1 324 ? -22.428 -40.016 42.016 1.00 17.25 ? 327  VAL   A CG1  1 
ATOM   2470 C  CG2  . VAL   A 1 324 ? -21.006 -39.895 39.915 1.00 16.68 ? 327  VAL   A CG2  1 
ATOM   2471 N  N    . PRO   A 1 325 ? -18.146 -41.468 41.826 1.00 16.26 ? 328  PRO   A N    1 
ATOM   2472 C  CA   . PRO   A 1 325 ? -17.017 -42.011 41.060 1.00 17.58 ? 328  PRO   A CA   1 
ATOM   2473 C  C    . PRO   A 1 325 ? -17.312 -41.923 39.563 1.00 16.33 ? 328  PRO   A C    1 
ATOM   2474 O  O    . PRO   A 1 325 ? -18.412 -42.266 39.106 1.00 13.90 ? 328  PRO   A O    1 
ATOM   2475 C  CB   . PRO   A 1 325 ? -16.934 -43.465 41.538 1.00 15.33 ? 328  PRO   A CB   1 
ATOM   2476 C  CG   . PRO   A 1 325 ? -17.509 -43.429 42.937 1.00 19.95 ? 328  PRO   A CG   1 
ATOM   2477 C  CD   . PRO   A 1 325 ? -18.660 -42.440 42.811 1.00 19.77 ? 328  PRO   A CD   1 
ATOM   2478 N  N    . TYR   A 1 326 ? -16.331 -41.440 38.805 1.00 11.67 ? 329  TYR   A N    1 
ATOM   2479 C  CA   . TYR   A 1 326 ? -16.502 -41.116 37.388 1.00 11.94 ? 329  TYR   A CA   1 
ATOM   2480 C  C    . TYR   A 1 326 ? -15.281 -41.596 36.604 1.00 15.55 ? 329  TYR   A C    1 
ATOM   2481 O  O    . TYR   A 1 326 ? -14.157 -41.148 36.863 1.00 15.60 ? 329  TYR   A O    1 
ATOM   2482 C  CB   . TYR   A 1 326 ? -16.690 -39.603 37.230 1.00 12.63 ? 329  TYR   A CB   1 
ATOM   2483 C  CG   . TYR   A 1 326 ? -17.222 -39.074 35.901 1.00 12.74 ? 329  TYR   A CG   1 
ATOM   2484 C  CD1  . TYR   A 1 326 ? -17.651 -39.916 34.883 1.00 10.88 ? 329  TYR   A CD1  1 
ATOM   2485 C  CD2  . TYR   A 1 326 ? -17.321 -37.701 35.699 1.00 15.63 ? 329  TYR   A CD2  1 
ATOM   2486 C  CE1  . TYR   A 1 326 ? -18.153 -39.395 33.697 1.00 12.05 ? 329  TYR   A CE1  1 
ATOM   2487 C  CE2  . TYR   A 1 326 ? -17.817 -37.174 34.534 1.00 14.02 ? 329  TYR   A CE2  1 
ATOM   2488 C  CZ   . TYR   A 1 326 ? -18.233 -38.007 33.540 1.00 13.14 ? 329  TYR   A CZ   1 
ATOM   2489 O  OH   . TYR   A 1 326 ? -18.724 -37.429 32.385 1.00 14.09 ? 329  TYR   A OH   1 
ATOM   2490 N  N    . MET   A 1 327 ? -15.513 -42.469 35.627 1.00 13.40 ? 330  MET   A N    1 
ATOM   2491 C  CA   . MET   A 1 327 ? -14.504 -42.920 34.668 1.00 16.49 ? 330  MET   A CA   1 
ATOM   2492 C  C    . MET   A 1 327 ? -14.696 -42.184 33.350 1.00 14.13 ? 330  MET   A C    1 
ATOM   2493 O  O    . MET   A 1 327 ? -15.786 -42.220 32.781 1.00 13.50 ? 330  MET   A O    1 
ATOM   2494 C  CB   . MET   A 1 327 ? -14.591 -44.435 34.483 1.00 13.21 ? 330  MET   A CB   1 
ATOM   2495 C  CG   . MET   A 1 327 ? -13.489 -45.079 33.633 1.00 15.51 ? 330  MET   A CG   1 
ATOM   2496 S  SD   . MET   A 1 327 ? -14.011 -46.707 33.007 1.00 17.80 ? 330  MET   A SD   1 
ATOM   2497 C  CE   . MET   A 1 327 ? -13.828 -47.655 34.523 1.00 16.65 ? 330  MET   A CE   1 
ATOM   2498 N  N    . VAL   A 1 328 ? -13.649 -41.484 32.895 1.00 12.92 ? 331  VAL   A N    1 
ATOM   2499 C  CA   . VAL   A 1 328 ? -13.661 -40.708 31.655 1.00 12.33 ? 331  VAL   A CA   1 
ATOM   2500 C  C    . VAL   A 1 328 ? -12.560 -41.251 30.747 1.00 15.81 ? 331  VAL   A C    1 
ATOM   2501 O  O    . VAL   A 1 328 ? -11.382 -41.328 31.144 1.00 14.31 ? 331  VAL   A O    1 
ATOM   2502 C  CB   . VAL   A 1 328 ? -13.471 -39.204 31.926 1.00 13.54 ? 331  VAL   A CB   1 
ATOM   2503 C  CG1  . VAL   A 1 328 ? -13.605 -38.412 30.642 1.00 14.02 ? 331  VAL   A CG1  1 
ATOM   2504 C  CG2  . VAL   A 1 328 ? -14.504 -38.692 32.933 1.00 15.12 ? 331  VAL   A CG2  1 
ATOM   2505 N  N    . GLY   A 1 329 ? -12.935 -41.649 29.534 1.00 13.82 ? 332  GLY   A N    1 
ATOM   2506 C  CA   . GLY   A 1 329 ? -11.984 -42.296 28.654 1.00 17.87 ? 332  GLY   A CA   1 
ATOM   2507 C  C    . GLY   A 1 329 ? -12.077 -41.779 27.235 1.00 15.37 ? 332  GLY   A C    1 
ATOM   2508 O  O    . GLY   A 1 329 ? -13.106 -41.248 26.804 1.00 13.78 ? 332  GLY   A O    1 
ATOM   2509 N  N    . ILE   A 1 330 ? -10.972 -41.944 26.534 1.00 13.15 ? 333  ILE   A N    1 
ATOM   2510 C  CA   . ILE   A 1 330 ? -10.958 -41.635 25.138 1.00 14.62 ? 333  ILE   A CA   1 
ATOM   2511 C  C    . ILE   A 1 330 ? -10.260 -42.769 24.366 1.00 13.70 ? 333  ILE   A C    1 
ATOM   2512 O  O    . ILE   A 1 330 ? -9.687  -43.642 24.942 1.00 14.03 ? 333  ILE   A O    1 
ATOM   2513 C  CB   . ILE   A 1 330 ? -10.243 -40.299 24.839 1.00 15.43 ? 333  ILE   A CB   1 
ATOM   2514 C  CG1  . ILE   A 1 330 ? -8.775  -40.399 25.273 1.00 17.67 ? 333  ILE   A CG1  1 
ATOM   2515 C  CG2  . ILE   A 1 330 ? -10.952 -39.127 25.484 1.00 14.68 ? 333  ILE   A CG2  1 
ATOM   2516 C  CD1  . ILE   A 1 330 ? -7.950  -39.171 24.986 1.00 16.34 ? 333  ILE   A CD1  1 
ATOM   2517 N  N    . ASN   A 1 331 ? -10.327 -42.692 23.060 1.00 16.49 ? 334  ASN   A N    1 
ATOM   2518 C  CA   . ASN   A 1 331 ? -9.675  -43.644 22.201 1.00 15.61 ? 334  ASN   A CA   1 
ATOM   2519 C  C    . ASN   A 1 331 ? -8.496  -42.942 21.516 1.00 19.74 ? 334  ASN   A C    1 
ATOM   2520 O  O    . ASN   A 1 331 ? -8.497  -41.759 21.361 1.00 17.11 ? 334  ASN   A O    1 
ATOM   2521 C  CB   . ASN   A 1 331 ? -10.615 -44.207 21.177 1.00 16.88 ? 334  ASN   A CB   1 
ATOM   2522 C  CG   . ASN   A 1 331 ? -11.649 -45.144 21.788 1.00 18.07 ? 334  ASN   A CG   1 
ATOM   2523 O  OD1  . ASN   A 1 331 ? -11.622 -45.405 22.980 1.00 15.54 ? 334  ASN   A OD1  1 
ATOM   2524 N  ND2  . ASN   A 1 331 ? -12.557 -45.646 20.970 1.00 17.69 ? 334  ASN   A ND2  1 
ATOM   2525 N  N    . LYS   A 1 332 ? -7.520  -43.711 21.096 1.00 18.64 ? 335  LYS   A N    1 
ATOM   2526 C  CA   . LYS   A 1 332 ? -6.306  -43.118 20.541 1.00 17.76 ? 335  LYS   A CA   1 
ATOM   2527 C  C    . LYS   A 1 332 ? -6.542  -42.273 19.302 1.00 19.77 ? 335  LYS   A C    1 
ATOM   2528 O  O    . LYS   A 1 332 ? -5.886  -41.277 19.157 1.00 20.37 ? 335  LYS   A O    1 
ATOM   2529 C  CB   . LYS   A 1 332 ? -5.318  -44.217 20.224 1.00 22.38 ? 335  LYS   A CB   1 
ATOM   2530 C  CG   . LYS   A 1 332 ? -3.899  -43.765 19.962 1.00 25.18 ? 335  LYS   A CG   1 
ATOM   2531 C  CD   . LYS   A 1 332 ? -3.251  -43.405 21.273 1.00 28.47 ? 335  LYS   A CD   1 
ATOM   2532 C  CE   . LYS   A 1 332 ? -1.762  -43.173 21.139 1.00 38.16 ? 335  LYS   A CE   1 
ATOM   2533 N  NZ   . LYS   A 1 332 ? -1.138  -43.069 22.485 1.00 39.67 ? 335  LYS   A NZ   1 
ATOM   2534 N  N    . GLN   A 1 333 ? -7.435  -42.682 18.417 1.00 15.86 ? 336  GLN   A N    1 
ATOM   2535 C  CA   . GLN   A 1 333 ? -7.732  -41.965 17.174 1.00 18.89 ? 336  GLN   A CA   1 
ATOM   2536 C  C    . GLN   A 1 333 ? -9.262  -41.717 17.027 1.00 20.38 ? 336  GLN   A C    1 
ATOM   2537 O  O    . GLN   A 1 333 ? -9.916  -42.273 16.179 1.00 17.63 ? 336  GLN   A O    1 
ATOM   2538 C  CB   . GLN   A 1 333 ? -7.163  -42.698 15.960 1.00 18.53 ? 336  GLN   A CB   1 
ATOM   2539 C  CG   . GLN   A 1 333 ? -5.664  -42.958 16.017 1.00 22.40 ? 336  GLN   A CG   1 
ATOM   2540 C  CD   . GLN   A 1 333 ? -5.129  -43.721 14.815 1.00 28.40 ? 336  GLN   A CD   1 
ATOM   2541 O  OE1  . GLN   A 1 333 ? -5.835  -43.957 13.847 1.00 31.13 ? 336  GLN   A OE1  1 
ATOM   2542 N  NE2  . GLN   A 1 333 ? -3.868  -44.090 14.874 1.00 32.25 ? 336  GLN   A NE2  1 
ATOM   2543 N  N    . GLU   A 1 334 ? -9.756  -40.772 17.809 1.00 18.27 ? 337  GLU   A N    1 
ATOM   2544 C  CA   . GLU   A 1 334 ? -11.195 -40.478 17.837 1.00 21.73 ? 337  GLU   A CA   1 
ATOM   2545 C  C    . GLU   A 1 334 ? -11.739 -39.995 16.496 1.00 19.87 ? 337  GLU   A C    1 
ATOM   2546 O  O    . GLU   A 1 334 ? -12.877 -40.195 16.197 1.00 22.39 ? 337  GLU   A O    1 
ATOM   2547 C  CB   . GLU   A 1 334 ? -11.505 -39.504 18.965 1.00 19.13 ? 337  GLU   A CB   1 
ATOM   2548 C  CG   . GLU   A 1 334 ? -11.252 -40.033 20.350 1.00 19.27 ? 337  GLU   A CG   1 
ATOM   2549 C  CD   . GLU   A 1 334 ? -12.369 -40.913 20.856 1.00 21.65 ? 337  GLU   A CD   1 
ATOM   2550 O  OE1  . GLU   A 1 334 ? -13.232 -41.320 20.062 1.00 20.17 ? 337  GLU   A OE1  1 
ATOM   2551 O  OE2  . GLU   A 1 334 ? -12.363 -41.192 22.059 1.00 20.12 ? 337  GLU   A OE2  1 
ATOM   2552 N  N    . PHE   A 1 335 ? -10.948 -39.234 15.793 1.00 17.12 ? 338  PHE   A N    1 
ATOM   2553 C  CA   . PHE   A 1 335 ? -11.355 -38.719 14.481 1.00 18.26 ? 338  PHE   A CA   1 
ATOM   2554 C  C    . PHE   A 1 335 ? -10.733 -39.504 13.323 1.00 22.60 ? 338  PHE   A C    1 
ATOM   2555 O  O    . PHE   A 1 335 ? -10.642 -39.007 12.227 1.00 23.99 ? 338  PHE   A O    1 
ATOM   2556 C  CB   . PHE   A 1 335 ? -11.121 -37.220 14.359 1.00 18.43 ? 338  PHE   A CB   1 
ATOM   2557 C  CG   . PHE   A 1 335 ? -12.190 -36.504 13.601 1.00 20.33 ? 338  PHE   A CG   1 
ATOM   2558 C  CD1  . PHE   A 1 335 ? -13.448 -36.357 14.139 1.00 20.48 ? 338  PHE   A CD1  1 
ATOM   2559 C  CD2  . PHE   A 1 335 ? -11.938 -35.972 12.354 1.00 25.60 ? 338  PHE   A CD2  1 
ATOM   2560 C  CE1  . PHE   A 1 335 ? -14.436 -35.693 13.450 1.00 20.16 ? 338  PHE   A CE1  1 
ATOM   2561 C  CE2  . PHE   A 1 335 ? -12.923 -35.307 11.662 1.00 22.89 ? 338  PHE   A CE2  1 
ATOM   2562 C  CZ   . PHE   A 1 335 ? -14.172 -35.169 12.209 1.00 19.63 ? 338  PHE   A CZ   1 
ATOM   2563 N  N    . GLY   A 1 336 ? -10.191 -40.671 13.597 1.00 20.58 ? 339  GLY   A N    1 
ATOM   2564 C  CA   . GLY   A 1 336 ? -9.482  -41.383 12.558 1.00 21.14 ? 339  GLY   A CA   1 
ATOM   2565 C  C    . GLY   A 1 336 ? -10.193 -41.840 11.323 1.00 25.02 ? 339  GLY   A C    1 
ATOM   2566 O  O    . GLY   A 1 336 ? -9.621  -41.785 10.268 1.00 23.74 ? 339  GLY   A O    1 
ATOM   2567 N  N    . TRP   A 1 337 ? -11.385 -42.388 11.475 1.00 21.29 ? 340  TRP   A N    1 
ATOM   2568 C  CA   . TRP   A 1 337 ? -12.173 -42.816 10.332 1.00 19.45 ? 340  TRP   A CA   1 
ATOM   2569 C  C    . TRP   A 1 337 ? -13.658 -42.636 10.380 1.00 19.08 ? 340  TRP   A C    1 
ATOM   2570 O  O    . TRP   A 1 337 ? -14.270 -42.029 9.530  1.00 21.79 ? 340  TRP   A O    1 
ATOM   2571 C  CB   . TRP   A 1 337 ? -11.818 -44.242 9.991  1.00 20.77 ? 340  TRP   A CB   1 
ATOM   2572 C  CG   . TRP   A 1 337 ? -12.476 -44.776 8.767  1.00 25.05 ? 340  TRP   A CG   1 
ATOM   2573 C  CD1  . TRP   A 1 337 ? -12.168 -44.502 7.446  1.00 25.39 ? 340  TRP   A CD1  1 
ATOM   2574 C  CD2  . TRP   A 1 337 ? -13.577 -45.726 8.713  1.00 25.60 ? 340  TRP   A CD2  1 
ATOM   2575 N  NE1  . TRP   A 1 337 ? -12.990 -45.188 6.608  1.00 26.23 ? 340  TRP   A NE1  1 
ATOM   2576 C  CE2  . TRP   A 1 337 ? -13.858 -45.940 7.302  1.00 26.89 ? 340  TRP   A CE2  1 
ATOM   2577 C  CE3  . TRP   A 1 337 ? -14.337 -46.386 9.657  1.00 25.05 ? 340  TRP   A CE3  1 
ATOM   2578 C  CZ2  . TRP   A 1 337 ? -14.853 -46.785 6.880  1.00 32.74 ? 340  TRP   A CZ2  1 
ATOM   2579 C  CZ3  . TRP   A 1 337 ? -15.342 -47.238 9.218  1.00 26.76 ? 340  TRP   A CZ3  1 
ATOM   2580 C  CH2  . TRP   A 1 337 ? -15.587 -47.438 7.863  1.00 28.83 ? 340  TRP   A CH2  1 
ATOM   2581 N  N    . LEU   A 1 338 ? -14.272 -43.278 11.361 1.00 18.31 ? 341  LEU   A N    1 
ATOM   2582 C  CA   . LEU   A 1 338 ? -15.719 -43.343 11.335 1.00 19.42 ? 341  LEU   A CA   1 
ATOM   2583 C  C    . LEU   A 1 338 ? -16.484 -42.059 11.399 1.00 19.02 ? 341  LEU   A C    1 
ATOM   2584 O  O    . LEU   A 1 338 ? -17.380 -41.872 10.611 1.00 19.68 ? 341  LEU   A O    1 
ATOM   2585 C  CB   . LEU   A 1 338 ? -16.161 -44.214 12.526 1.00 20.86 ? 341  LEU   A CB   1 
ATOM   2586 C  CG   . LEU   A 1 338 ? -17.631 -44.520 12.778 1.00 22.25 ? 341  LEU   A CG   1 
ATOM   2587 C  CD1  . LEU   A 1 338 ? -17.782 -45.972 13.179 1.00 21.48 ? 341  LEU   A CD1  1 
ATOM   2588 C  CD2  . LEU   A 1 338 ? -18.199 -43.607 13.849 1.00 24.02 ? 341  LEU   A CD2  1 
ATOM   2589 N  N    . ILE   A 1 339 ? -16.129 -41.150 12.278 1.00 19.12 ? 342  ILE   A N    1 
ATOM   2590 C  CA   . ILE   A 1 339 ? -16.875 -39.916 12.219 1.00 21.31 ? 342  ILE   A CA   1 
ATOM   2591 C  C    . ILE   A 1 339 ? -16.661 -39.085 10.937 1.00 22.55 ? 342  ILE   A C    1 
ATOM   2592 O  O    . ILE   A 1 339 ? -17.613 -38.778 10.243 1.00 21.86 ? 342  ILE   A O    1 
ATOM   2593 C  CB   . ILE   A 1 339 ? -16.580 -39.041 13.465 1.00 19.97 ? 342  ILE   A CB   1 
ATOM   2594 C  CG1  . ILE   A 1 339 ? -16.947 -39.772 14.743 1.00 18.70 ? 342  ILE   A CG1  1 
ATOM   2595 C  CG2  . ILE   A 1 339 ? -17.329 -37.723 13.390 1.00 19.88 ? 342  ILE   A CG2  1 
ATOM   2596 C  CD1  . ILE   A 1 339 ? -16.523 -39.015 15.975 1.00 19.35 ? 342  ILE   A CD1  1 
ATOM   2597 N  N    . PRO   A 1 340 ? -15.391 -38.894 10.549 1.00 20.39 ? 343  PRO   A N    1 
ATOM   2598 C  CA   . PRO   A 1 340 ? -15.252 -38.149 9.296  1.00 22.23 ? 343  PRO   A CA   1 
ATOM   2599 C  C    . PRO   A 1 340 ? -15.745 -38.829 8.021  1.00 25.90 ? 343  PRO   A C    1 
ATOM   2600 O  O    . PRO   A 1 340 ? -16.391 -38.209 7.202  1.00 25.99 ? 343  PRO   A O    1 
ATOM   2601 C  CB   . PRO   A 1 340 ? -13.740 -37.934 9.203  1.00 21.93 ? 343  PRO   A CB   1 
ATOM   2602 C  CG   . PRO   A 1 340 ? -13.123 -38.935 10.096 1.00 22.16 ? 343  PRO   A CG   1 
ATOM   2603 C  CD   . PRO   A 1 340 ? -14.092 -39.084 11.213 1.00 21.13 ? 343  PRO   A CD   1 
ATOM   2604 N  N    . GLN   A 1 341 ? -15.424 -40.100 7.885  1.00 19.70 ? 344  GLN   A N    1 
ATOM   2605 C  CA   . GLN   A 1 341 ? -15.739 -40.787 6.660  1.00 21.21 ? 344  GLN   A CA   1 
ATOM   2606 C  C    . GLN   A 1 341 ? -17.060 -41.513 6.585  1.00 27.26 ? 344  GLN   A C    1 
ATOM   2607 O  O    . GLN   A 1 341 ? -17.536 -41.749 5.503  1.00 32.70 ? 344  GLN   A O    1 
ATOM   2608 C  CB   . GLN   A 1 341 ? -14.613 -41.752 6.313  1.00 22.99 ? 344  GLN   A CB   1 
ATOM   2609 C  CG   . GLN   A 1 341 ? -13.222 -41.147 6.313  1.00 29.15 ? 344  GLN   A CG   1 
ATOM   2610 C  CD   . GLN   A 1 341 ? -13.098 -39.918 5.437  1.00 26.03 ? 344  GLN   A CD   1 
ATOM   2611 O  OE1  . GLN   A 1 341 ? -12.719 -38.870 5.906  1.00 32.48 ? 344  GLN   A OE1  1 
ATOM   2612 N  NE2  . GLN   A 1 341 ? -13.407 -40.055 4.164  1.00 35.89 ? 344  GLN   A NE2  1 
ATOM   2613 N  N    . MET   A 1 342 ? -17.604 -41.966 7.704  1.00 23.59 ? 345  MET   A N    1 
ATOM   2614 C  CA   . MET   A 1 342 ? -18.908 -42.588 7.590  1.00 23.84 ? 345  MET   A CA   1 
ATOM   2615 C  C    . MET   A 1 342 ? -20.054 -41.706 8.019  1.00 27.49 ? 345  MET   A C    1 
ATOM   2616 O  O    . MET   A 1 342 ? -21.082 -41.753 7.404  1.00 29.06 ? 345  MET   A O    1 
ATOM   2617 C  CB   . MET   A 1 342 ? -18.900 -43.897 8.343  1.00 25.72 ? 345  MET   A CB   1 
ATOM   2618 C  CG   . MET   A 1 342 ? -17.805 -44.829 7.912  1.00 28.89 ? 345  MET   A CG   1 
ATOM   2619 S  SD   . MET   A 1 342 ? -18.098 -45.329 6.214  1.00 51.90 ? 345  MET   A SD   1 
ATOM   2620 C  CE   . MET   A 1 342 ? -19.478 -46.424 6.470  1.00 30.44 ? 345  MET   A CE   1 
ATOM   2621 N  N    . LEU   A 1 343 ? -19.974 -41.080 9.175  1.00 24.23 ? 346  LEU   A N    1 
ATOM   2622 C  CA   . LEU   A 1 343 ? -20.970 -40.099 9.568  1.00 26.05 ? 346  LEU   A CA   1 
ATOM   2623 C  C    . LEU   A 1 343 ? -21.069 -38.725 8.919  1.00 29.90 ? 346  LEU   A C    1 
ATOM   2624 O  O    . LEU   A 1 343 ? -22.133 -38.299 8.574  1.00 28.72 ? 346  LEU   A O    1 
ATOM   2625 C  CB   . LEU   A 1 343 ? -20.848 -39.881 11.066 1.00 24.49 ? 346  LEU   A CB   1 
ATOM   2626 C  CG   . LEU   A 1 343 ? -20.981 -41.113 11.952 1.00 31.91 ? 346  LEU   A CG   1 
ATOM   2627 C  CD1  . LEU   A 1 343 ? -20.826 -40.725 13.410 1.00 29.00 ? 346  LEU   A CD1  1 
ATOM   2628 C  CD2  . LEU   A 1 343 ? -22.313 -41.807 11.729 1.00 35.01 ? 346  LEU   A CD2  1 
ATOM   2629 N  N    . MET   A 1 344 ? -19.931 -38.070 8.742  1.00 23.91 ? 347  MET   A N    1 
ATOM   2630 C  CA   . MET   A 1 344 ? -19.971 -36.674 8.325  1.00 27.33 ? 347  MET   A CA   1 
ATOM   2631 C  C    . MET   A 1 344 ? -19.561 -36.285 6.923  1.00 28.28 ? 347  MET   A C    1 
ATOM   2632 O  O    . MET   A 1 344 ? -19.565 -35.111 6.603  1.00 27.22 ? 347  MET   A O    1 
ATOM   2633 C  CB   . MET   A 1 344 ? -19.141 -35.871 9.309  1.00 26.46 ? 347  MET   A CB   1 
ATOM   2634 C  CG   . MET   A 1 344 ? -19.628 -35.904 10.733 1.00 28.12 ? 347  MET   A CG   1 
ATOM   2635 S  SD   . MET   A 1 344 ? -18.727 -34.734 11.758 1.00 45.78 ? 347  MET   A SD   1 
ATOM   2636 C  CE   . MET   A 1 344 ? -19.858 -34.613 13.137 1.00 44.14 ? 347  MET   A CE   1 
ATOM   2637 N  N    . SER   A 1 345 ? -19.194 -37.263 6.141  1.00 26.01 ? 348  SER   A N    1 
ATOM   2638 C  CA   . SER   A 1 345 ? -18.844 -36.998 4.763  1.00 26.79 ? 348  SER   A CA   1 
ATOM   2639 C  C    . SER   A 1 345 ? -17.748 -35.920 4.635  1.00 30.74 ? 348  SER   A C    1 
ATOM   2640 O  O    . SER   A 1 345 ? -17.886 -34.972 3.892  1.00 30.14 ? 348  SER   A O    1 
ATOM   2641 C  CB   . SER   A 1 345 ? -20.116 -36.643 4.017  1.00 31.98 ? 348  SER   A CB   1 
ATOM   2642 O  OG   . SER   A 1 345 ? -21.034 -37.717 3.990  1.00 35.01 ? 348  SER   A OG   1 
ATOM   2643 N  N    . TYR   A 1 346 ? -16.670 -36.099 5.366  1.00 27.49 ? 349  TYR   A N    1 
ATOM   2644 C  CA   . TYR   A 1 346 ? -15.563 -35.158 5.273  1.00 29.20 ? 349  TYR   A CA   1 
ATOM   2645 C  C    . TYR   A 1 346 ? -14.895 -35.252 3.904  1.00 33.84 ? 349  TYR   A C    1 
ATOM   2646 O  O    . TYR   A 1 346 ? -14.710 -36.354 3.377  1.00 32.20 ? 349  TYR   A O    1 
ATOM   2647 C  CB   . TYR   A 1 346 ? -14.531 -35.422 6.365  1.00 30.11 ? 349  TYR   A CB   1 
ATOM   2648 C  CG   . TYR   A 1 346 ? -14.573 -34.377 7.443  1.00 28.28 ? 349  TYR   A CG   1 
ATOM   2649 C  CD1  . TYR   A 1 346 ? -15.660 -34.290 8.288  1.00 28.42 ? 349  TYR   A CD1  1 
ATOM   2650 C  CD2  . TYR   A 1 346 ? -13.549 -33.449 7.584  1.00 29.12 ? 349  TYR   A CD2  1 
ATOM   2651 C  CE1  . TYR   A 1 346 ? -15.721 -33.333 9.270  1.00 27.14 ? 349  TYR   A CE1  1 
ATOM   2652 C  CE2  . TYR   A 1 346 ? -13.602 -32.472 8.564  1.00 25.78 ? 349  TYR   A CE2  1 
ATOM   2653 C  CZ   . TYR   A 1 346 ? -14.691 -32.423 9.400  1.00 27.56 ? 349  TYR   A CZ   1 
ATOM   2654 O  OH   . TYR   A 1 346 ? -14.767 -31.473 10.386 1.00 32.23 ? 349  TYR   A OH   1 
ATOM   2655 N  N    . PRO   A 1 347 ? -14.524 -34.110 3.294  1.00 31.76 ? 350  PRO   A N    1 
ATOM   2656 C  CA   . PRO   A 1 347 ? -13.725 -34.162 2.061  1.00 33.04 ? 350  PRO   A CA   1 
ATOM   2657 C  C    . PRO   A 1 347 ? -12.286 -34.558 2.347  1.00 34.40 ? 350  PRO   A C    1 
ATOM   2658 O  O    . PRO   A 1 347 ? -11.384 -33.716 2.337  1.00 33.40 ? 350  PRO   A O    1 
ATOM   2659 C  CB   . PRO   A 1 347 ? -13.834 -32.733 1.514  1.00 32.84 ? 350  PRO   A CB   1 
ATOM   2660 C  CG   . PRO   A 1 347 ? -14.031 -31.890 2.737  1.00 33.74 ? 350  PRO   A CG   1 
ATOM   2661 C  CD   . PRO   A 1 347 ? -14.851 -32.727 3.692  1.00 32.21 ? 350  PRO   A CD   1 
ATOM   2662 N  N    . LEU   A 1 348 ? -12.063 -35.845 2.622  1.00 31.59 ? 351  LEU   A N    1 
ATOM   2663 C  CA   . LEU   A 1 348 ? -10.738 -36.331 2.994  1.00 32.67 ? 351  LEU   A CA   1 
ATOM   2664 C  C    . LEU   A 1 348 ? -10.437 -37.682 2.361  1.00 36.99 ? 351  LEU   A C    1 
ATOM   2665 O  O    . LEU   A 1 348 ? -9.674  -38.479 2.919  1.00 35.98 ? 351  LEU   A O    1 
ATOM   2666 C  CB   . LEU   A 1 348 ? -10.598 -36.435 4.514  1.00 34.46 ? 351  LEU   A CB   1 
ATOM   2667 C  CG   . LEU   A 1 348 ? -10.423 -35.095 5.230  1.00 35.22 ? 351  LEU   A CG   1 
ATOM   2668 C  CD1  . LEU   A 1 348 ? -10.511 -35.297 6.726  1.00 32.42 ? 351  LEU   A CD1  1 
ATOM   2669 C  CD2  . LEU   A 1 348 ? -9.092  -34.456 4.849  1.00 33.22 ? 351  LEU   A CD2  1 
ATOM   2670 N  N    . SER   A 1 349 ? -11.026 -37.964 1.198  1.00 37.17 ? 352  SER   A N    1 
ATOM   2671 C  CA   . SER   A 1 349 ? -10.748 -39.240 0.557  1.00 37.68 ? 352  SER   A CA   1 
ATOM   2672 C  C    . SER   A 1 349 ? -9.309  -39.351 0.064  1.00 39.41 ? 352  SER   A C    1 
ATOM   2673 O  O    . SER   A 1 349 ? -8.830  -40.474 -0.124 1.00 37.60 ? 352  SER   A O    1 
ATOM   2674 C  CB   . SER   A 1 349 ? -11.696 -39.467 -0.616 1.00 40.78 ? 352  SER   A CB   1 
ATOM   2675 O  OG   . SER   A 1 349 ? -11.894 -38.266 -1.337 1.00 45.61 ? 352  SER   A OG   1 
ATOM   2676 N  N    . GLU   A 1 350 ? -8.602  -38.229 -0.142 1.00 33.47 ? 353  GLU   A N    1 
ATOM   2677 C  CA   . GLU   A 1 350 ? -7.368  -38.302 -0.921 1.00 37.47 ? 353  GLU   A CA   1 
ATOM   2678 C  C    . GLU   A 1 350 ? -6.135  -38.692 -0.108 1.00 41.18 ? 353  GLU   A C    1 
ATOM   2679 O  O    . GLU   A 1 350 ? -5.125  -39.086 -0.702 1.00 45.59 ? 353  GLU   A O    1 
ATOM   2680 C  CB   . GLU   A 1 350 ? -7.107  -36.988 -1.658 1.00 37.11 ? 353  GLU   A CB   1 
ATOM   2681 C  CG   . GLU   A 1 350 ? -7.930  -36.878 -2.943 1.00 39.43 ? 353  GLU   A CG   1 
ATOM   2682 C  CD   . GLU   A 1 350 ? -8.099  -35.451 -3.448 1.00 37.82 ? 353  GLU   A CD   1 
ATOM   2683 O  OE1  . GLU   A 1 350 ? -7.217  -34.607 -3.184 1.00 33.84 ? 353  GLU   A OE1  1 
ATOM   2684 O  OE2  . GLU   A 1 350 ? -9.115  -35.179 -4.118 1.00 37.13 ? 353  GLU   A OE2  1 
ATOM   2685 N  N    . GLY   A 1 351 ? -6.173  -38.618 1.217  1.00 39.69 ? 354  GLY   A N    1 
ATOM   2686 C  CA   . GLY   A 1 351 ? -5.091  -39.212 1.978  1.00 42.48 ? 354  GLY   A CA   1 
ATOM   2687 C  C    . GLY   A 1 351 ? -3.803  -38.417 2.044  1.00 42.79 ? 354  GLY   A C    1 
ATOM   2688 O  O    . GLY   A 1 351 ? -2.868  -38.845 2.736  1.00 41.44 ? 354  GLY   A O    1 
ATOM   2689 N  N    . GLN   A 1 352 ? -3.702  -37.297 1.337  1.00 40.25 ? 355  GLN   A N    1 
ATOM   2690 C  CA   . GLN   A 1 352 ? -2.689  -36.293 1.625  1.00 39.72 ? 355  GLN   A CA   1 
ATOM   2691 C  C    . GLN   A 1 352 ? -3.377  -34.947 1.765  1.00 34.75 ? 355  GLN   A C    1 
ATOM   2692 O  O    . GLN   A 1 352 ? -4.412  -34.690 1.146  1.00 34.80 ? 355  GLN   A O    1 
ATOM   2693 C  CB   . GLN   A 1 352 ? -1.594  -36.221 0.548  1.00 42.38 ? 355  GLN   A CB   1 
ATOM   2694 C  CG   . GLN   A 1 352 ? -2.076  -35.813 -0.822 1.00 46.34 ? 355  GLN   A CG   1 
ATOM   2695 C  CD   . GLN   A 1 352 ? -1.484  -36.688 -1.910 1.00 57.51 ? 355  GLN   A CD   1 
ATOM   2696 O  OE1  . GLN   A 1 352 ? -0.283  -36.624 -2.188 1.00 58.42 ? 355  GLN   A OE1  1 
ATOM   2697 N  NE2  . GLN   A 1 352 ? -2.319  -37.535 -2.511 1.00 58.60 ? 355  GLN   A NE2  1 
ATOM   2698 N  N    . LEU   A 1 353 ? -2.791  -34.095 2.595  1.00 34.75 ? 356  LEU   A N    1 
ATOM   2699 C  CA   . LEU   A 1 353 ? -3.384  -32.812 2.943  1.00 35.62 ? 356  LEU   A CA   1 
ATOM   2700 C  C    . LEU   A 1 353 ? -2.268  -31.790 3.056  1.00 33.45 ? 356  LEU   A C    1 
ATOM   2701 O  O    . LEU   A 1 353 ? -1.377  -31.938 3.894  1.00 36.36 ? 356  LEU   A O    1 
ATOM   2702 C  CB   . LEU   A 1 353 ? -4.164  -32.918 4.259  1.00 36.08 ? 356  LEU   A CB   1 
ATOM   2703 C  CG   . LEU   A 1 353 ? -5.073  -31.761 4.660  1.00 35.47 ? 356  LEU   A CG   1 
ATOM   2704 C  CD1  . LEU   A 1 353 ? -6.277  -31.671 3.738  1.00 29.75 ? 356  LEU   A CD1  1 
ATOM   2705 C  CD2  . LEU   A 1 353 ? -5.523  -31.956 6.107  1.00 31.48 ? 356  LEU   A CD2  1 
ATOM   2706 N  N    . ASP   A 1 354 ? -2.300  -30.771 2.212  1.00 37.10 ? 357  ASP   A N    1 
ATOM   2707 C  CA   . ASP   A 1 354 ? -1.355  -29.678 2.370  1.00 40.16 ? 357  ASP   A CA   1 
ATOM   2708 C  C    . ASP   A 1 354 ? -1.910  -28.662 3.364  1.00 38.54 ? 357  ASP   A C    1 
ATOM   2709 O  O    . ASP   A 1 354 ? -3.108  -28.637 3.660  1.00 35.41 ? 357  ASP   A O    1 
ATOM   2710 C  CB   . ASP   A 1 354 ? -1.048  -29.027 1.018  1.00 41.75 ? 357  ASP   A CB   1 
ATOM   2711 C  CG   . ASP   A 1 354 ? -2.241  -28.290 0.436  1.00 45.83 ? 357  ASP   A CG   1 
ATOM   2712 O  OD1  . ASP   A 1 354 ? -2.517  -27.156 0.887  1.00 48.40 ? 357  ASP   A OD1  1 
ATOM   2713 O  OD2  . ASP   A 1 354 ? -2.899  -28.839 -0.479 1.00 50.59 ? 357  ASP   A OD2  1 
ATOM   2714 N  N    . GLN   A 1 355 ? -1.019  -27.816 3.882  1.00 38.03 ? 358  GLN   A N    1 
ATOM   2715 C  CA   . GLN   A 1 355 ? -1.392  -26.962 5.004  1.00 35.87 ? 358  GLN   A CA   1 
ATOM   2716 C  C    . GLN   A 1 355 ? -2.448  -25.930 4.629  1.00 40.63 ? 358  GLN   A C    1 
ATOM   2717 O  O    . GLN   A 1 355 ? -3.235  -25.522 5.491  1.00 39.75 ? 358  GLN   A O    1 
ATOM   2718 C  CB   . GLN   A 1 355 ? -0.160  -26.271 5.565  1.00 36.77 ? 358  GLN   A CB   1 
ATOM   2719 C  CG   . GLN   A 1 355 ? 0.592   -27.131 6.551  1.00 40.37 ? 358  GLN   A CG   1 
ATOM   2720 C  CD   . GLN   A 1 355 ? 1.070   -26.359 7.751  1.00 38.87 ? 358  GLN   A CD   1 
ATOM   2721 O  OE1  . GLN   A 1 355 ? 0.553   -25.284 8.074  1.00 38.71 ? 358  GLN   A OE1  1 
ATOM   2722 N  NE2  . GLN   A 1 355 ? 2.074   -26.899 8.422  1.00 41.03 ? 358  GLN   A NE2  1 
ATOM   2723 N  N    . LYS   A 1 356 ? -2.491  -25.492 3.366  1.00 38.36 ? 359  LYS   A N    1 
ATOM   2724 C  CA   . LYS   A 1 356 ? -3.503  -24.511 2.983  1.00 37.76 ? 359  LYS   A CA   1 
ATOM   2725 C  C    . LYS   A 1 356 ? -4.888  -25.145 2.931  1.00 34.80 ? 359  LYS   A C    1 
ATOM   2726 O  O    . LYS   A 1 356 ? -5.875  -24.559 3.404  1.00 34.22 ? 359  LYS   A O    1 
ATOM   2727 C  CB   . LYS   A 1 356 ? -3.141  -23.882 1.641  1.00 39.09 ? 359  LYS   A CB   1 
ATOM   2728 C  CG   . LYS   A 1 356 ? -2.433  -22.542 1.785  1.00 56.62 ? 359  LYS   A CG   1 
ATOM   2729 C  CD   . LYS   A 1 356 ? -3.082  -21.453 0.927  1.00 68.29 ? 359  LYS   A CD   1 
ATOM   2730 C  CE   . LYS   A 1 356 ? -2.514  -20.069 1.250  1.00 70.79 ? 359  LYS   A CE   1 
ATOM   2731 N  NZ   . LYS   A 1 356 ? -2.622  -19.123 0.099  1.00 78.21 ? 359  LYS   A NZ   1 
ATOM   2732 N  N    . THR   A 1 357 ? -4.978  -26.344 2.354  1.00 33.10 ? 360  THR   A N    1 
ATOM   2733 C  CA   . THR   A 1 357 ? -6.235  -27.077 2.368  1.00 32.28 ? 360  THR   A CA   1 
ATOM   2734 C  C    . THR   A 1 357 ? -6.643  -27.408 3.796  1.00 32.24 ? 360  THR   A C    1 
ATOM   2735 O  O    . THR   A 1 357 ? -7.830  -27.341 4.138  1.00 31.81 ? 360  THR   A O    1 
ATOM   2736 C  CB   . THR   A 1 357 ? -6.109  -28.349 1.525  1.00 35.64 ? 360  THR   A CB   1 
ATOM   2737 O  OG1  . THR   A 1 357 ? -5.713  -27.993 0.195  1.00 35.50 ? 360  THR   A OG1  1 
ATOM   2738 C  CG2  . THR   A 1 357 ? -7.449  -29.099 1.456  1.00 31.83 ? 360  THR   A CG2  1 
ATOM   2739 N  N    . ALA   A 1 358 ? -5.668  -27.750 4.646  1.00 28.84 ? 361  ALA   A N    1 
ATOM   2740 C  CA   . ALA   A 1 358 ? -5.962  -28.026 6.049  1.00 30.32 ? 361  ALA   A CA   1 
ATOM   2741 C  C    . ALA   A 1 358 ? -6.540  -26.805 6.756  1.00 32.43 ? 361  ALA   A C    1 
ATOM   2742 O  O    . ALA   A 1 358 ? -7.499  -26.931 7.525  1.00 27.43 ? 361  ALA   A O    1 
ATOM   2743 C  CB   . ALA   A 1 358 ? -4.712  -28.512 6.770  1.00 26.65 ? 361  ALA   A CB   1 
ATOM   2744 N  N    . MET   A 1 359 ? -5.969  -25.617 6.521  1.00 25.95 ? 362  MET   A N    1 
ATOM   2745 C  CA   . MET   A 1 359 ? -6.530  -24.402 7.121  1.00 29.67 ? 362  MET   A CA   1 
ATOM   2746 C  C    . MET   A 1 359 ? -7.949  -24.135 6.623  1.00 29.47 ? 362  MET   A C    1 
ATOM   2747 O  O    . MET   A 1 359 ? -8.839  -23.765 7.406  1.00 27.80 ? 362  MET   A O    1 
ATOM   2748 C  CB   . MET   A 1 359 ? -5.629  -23.205 6.818  1.00 29.48 ? 362  MET   A CB   1 
ATOM   2749 C  CG   . MET   A 1 359 ? -4.307  -23.213 7.571  1.00 34.27 ? 362  MET   A CG   1 
ATOM   2750 S  SD   . MET   A 1 359 ? -3.469  -21.607 7.515  1.00 37.80 ? 362  MET   A SD   1 
ATOM   2751 C  CE   . MET   A 1 359 ? -3.014  -21.584 5.782  1.00 39.80 ? 362  MET   A CE   1 
ATOM   2752 N  N    . SER   A 1 360 ? -8.179  -24.302 5.320  1.00 27.93 ? 363  SER   A N    1 
ATOM   2753 C  CA   . SER   A 1 360 ? -9.526  -24.093 4.807  1.00 32.28 ? 363  SER   A CA   1 
ATOM   2754 C  C    . SER   A 1 360 ? -10.508 -25.090 5.429  1.00 28.60 ? 363  SER   A C    1 
ATOM   2755 O  O    . SER   A 1 360 ? -11.628 -24.723 5.813  1.00 26.76 ? 363  SER   A O    1 
ATOM   2756 C  CB   . SER   A 1 360 ? -9.513  -24.189 3.282  1.00 32.31 ? 363  SER   A CB   1 
ATOM   2757 O  OG   . SER   A 1 360 ? -10.722 -24.729 2.799  1.00 43.90 ? 363  SER   A OG   1 
ATOM   2758 N  N    . LEU   A 1 361 ? -10.077 -26.346 5.588  1.00 27.84 ? 364  LEU   A N    1 
ATOM   2759 C  CA   . LEU   A 1 361 ? -10.945 -27.387 6.130  1.00 28.54 ? 364  LEU   A CA   1 
ATOM   2760 C  C    . LEU   A 1 361 ? -11.200 -27.174 7.616  1.00 26.20 ? 364  LEU   A C    1 
ATOM   2761 O  O    . LEU   A 1 361 ? -12.305 -27.429 8.105  1.00 23.61 ? 364  LEU   A O    1 
ATOM   2762 C  CB   . LEU   A 1 361 ? -10.314 -28.762 5.891  1.00 24.34 ? 364  LEU   A CB   1 
ATOM   2763 C  CG   . LEU   A 1 361 ? -11.196 -29.979 6.172  1.00 26.88 ? 364  LEU   A CG   1 
ATOM   2764 C  CD1  . LEU   A 1 361 ? -12.532 -29.864 5.459  1.00 27.13 ? 364  LEU   A CD1  1 
ATOM   2765 C  CD2  . LEU   A 1 361 ? -10.470 -31.252 5.754  1.00 31.54 ? 364  LEU   A CD2  1 
ATOM   2766 N  N    . LEU   A 1 362 ? -10.189 -26.705 8.349  1.00 23.97 ? 365  LEU   A N    1 
ATOM   2767 C  CA   . LEU   A 1 362 ? -10.369 -26.421 9.767  1.00 24.08 ? 365  LEU   A CA   1 
ATOM   2768 C  C    . LEU   A 1 362 ? -11.307 -25.239 9.971  1.00 25.54 ? 365  LEU   A C    1 
ATOM   2769 O  O    . LEU   A 1 362 ? -12.053 -25.203 10.958 1.00 22.93 ? 365  LEU   A O    1 
ATOM   2770 C  CB   . LEU   A 1 362 ? -9.014  -26.167 10.430 1.00 22.06 ? 365  LEU   A CB   1 
ATOM   2771 C  CG   . LEU   A 1 362 ? -9.019  -26.173 11.968 1.00 22.76 ? 365  LEU   A CG   1 
ATOM   2772 C  CD1  . LEU   A 1 362 ? -9.295  -27.576 12.506 1.00 23.68 ? 365  LEU   A CD1  1 
ATOM   2773 C  CD2  . LEU   A 1 362 ? -7.701  -25.665 12.521 1.00 24.13 ? 365  LEU   A CD2  1 
ATOM   2774 N  N    . TRP   A 1 363 ? -11.303 -24.272 9.049  1.00 24.33 ? 366  TRP   A N    1 
ATOM   2775 C  CA   . TRP   A 1 363 ? -12.315 -23.224 9.124  1.00 23.77 ? 366  TRP   A CA   1 
ATOM   2776 C  C    . TRP   A 1 363 ? -13.700 -23.786 8.833  1.00 23.50 ? 366  TRP   A C    1 
ATOM   2777 O  O    . TRP   A 1 363 ? -14.675 -23.430 9.506  1.00 23.91 ? 366  TRP   A O    1 
ATOM   2778 C  CB   . TRP   A 1 363 ? -11.980 -22.082 8.159  1.00 27.70 ? 366  TRP   A CB   1 
ATOM   2779 C  CG   . TRP   A 1 363 ? -13.036 -20.983 8.099  1.00 27.77 ? 366  TRP   A CG   1 
ATOM   2780 C  CD1  . TRP   A 1 363 ? -13.663 -20.510 6.981  1.00 30.37 ? 366  TRP   A CD1  1 
ATOM   2781 C  CD2  . TRP   A 1 363 ? -13.547 -20.210 9.199  1.00 27.48 ? 366  TRP   A CD2  1 
ATOM   2782 N  NE1  . TRP   A 1 363 ? -14.550 -19.510 7.318  1.00 30.93 ? 366  TRP   A NE1  1 
ATOM   2783 C  CE2  . TRP   A 1 363 ? -14.492 -19.302 8.671  1.00 29.76 ? 366  TRP   A CE2  1 
ATOM   2784 C  CE3  . TRP   A 1 363 ? -13.306 -20.204 10.580 1.00 28.32 ? 366  TRP   A CE3  1 
ATOM   2785 C  CZ2  . TRP   A 1 363 ? -15.192 -18.399 9.473  1.00 29.99 ? 366  TRP   A CZ2  1 
ATOM   2786 C  CZ3  . TRP   A 1 363 ? -14.006 -19.303 11.376 1.00 30.38 ? 366  TRP   A CZ3  1 
ATOM   2787 C  CH2  . TRP   A 1 363 ? -14.939 -18.416 10.818 1.00 28.75 ? 366  TRP   A CH2  1 
ATOM   2788 N  N    . LYS   A 1 364 ? -13.810 -24.668 7.832  1.00 23.97 ? 367  LYS   A N    1 
ATOM   2789 C  CA   . LYS   A 1 364 ? -15.101 -25.299 7.569  1.00 25.08 ? 367  LYS   A CA   1 
ATOM   2790 C  C    . LYS   A 1 364 ? -15.563 -26.157 8.752  1.00 23.88 ? 367  LYS   A C    1 
ATOM   2791 O  O    . LYS   A 1 364 ? -16.770 -26.355 8.941  1.00 25.41 ? 367  LYS   A O    1 
ATOM   2792 C  CB   . LYS   A 1 364 ? -15.027 -26.132 6.288  1.00 27.78 ? 367  LYS   A CB   1 
ATOM   2793 C  CG   . LYS   A 1 364 ? -15.095 -25.295 5.010  1.00 29.06 ? 367  LYS   A CG   1 
ATOM   2794 C  CD   . LYS   A 1 364 ? -16.410 -24.507 4.927  1.00 32.00 ? 367  LYS   A CD   1 
ATOM   2795 C  CE   . LYS   A 1 364 ? -16.640 -23.914 3.536  1.00 32.20 ? 367  LYS   A CE   1 
ATOM   2796 N  NZ   . LYS   A 1 364 ? -17.766 -22.927 3.517  1.00 31.04 ? 367  LYS   A NZ   1 
ATOM   2797 N  N    . SER   A 1 365 ? -14.627 -26.657 9.555  1.00 24.05 ? 368  SER   A N    1 
ATOM   2798 C  CA   . SER   A 1 365 ? -14.896 -27.471 10.742 1.00 21.68 ? 368  SER   A CA   1 
ATOM   2799 C  C    . SER   A 1 365 ? -15.333 -26.653 11.954 1.00 23.50 ? 368  SER   A C    1 
ATOM   2800 O  O    . SER   A 1 365 ? -15.460 -27.223 13.044 1.00 20.36 ? 368  SER   A O    1 
ATOM   2801 C  CB   . SER   A 1 365 ? -13.657 -28.294 11.117 1.00 19.80 ? 368  SER   A CB   1 
ATOM   2802 O  OG   . SER   A 1 365 ? -13.292 -29.177 10.071 1.00 23.57 ? 368  SER   A OG   1 
ATOM   2803 N  N    . TYR   A 1 366 ? -15.581 -25.353 11.783 1.00 22.37 ? 369  TYR   A N    1 
ATOM   2804 C  CA   . TYR   A 1 366 ? -15.978 -24.487 12.894 1.00 22.42 ? 369  TYR   A CA   1 
ATOM   2805 C  C    . TYR   A 1 366 ? -17.082 -25.064 13.777 1.00 22.43 ? 369  TYR   A C    1 
ATOM   2806 O  O    . TYR   A 1 366 ? -16.938 -25.020 15.010 1.00 23.72 ? 369  TYR   A O    1 
ATOM   2807 C  CB   . TYR   A 1 366 ? -16.410 -23.122 12.346 1.00 22.47 ? 369  TYR   A CB   1 
ATOM   2808 C  CG   . TYR   A 1 366 ? -16.638 -22.106 13.436 1.00 26.13 ? 369  TYR   A CG   1 
ATOM   2809 C  CD1  . TYR   A 1 366 ? -15.569 -21.416 13.990 1.00 27.24 ? 369  TYR   A CD1  1 
ATOM   2810 C  CD2  . TYR   A 1 366 ? -17.908 -21.851 13.924 1.00 27.67 ? 369  TYR   A CD2  1 
ATOM   2811 C  CE1  . TYR   A 1 366 ? -15.757 -20.487 14.975 1.00 30.75 ? 369  TYR   A CE1  1 
ATOM   2812 C  CE2  . TYR   A 1 366 ? -18.108 -20.919 14.921 1.00 29.56 ? 369  TYR   A CE2  1 
ATOM   2813 C  CZ   . TYR   A 1 366 ? -17.025 -20.241 15.439 1.00 35.41 ? 369  TYR   A CZ   1 
ATOM   2814 O  OH   . TYR   A 1 366 ? -17.196 -19.310 16.431 1.00 39.58 ? 369  TYR   A OH   1 
ATOM   2815 N  N    . PRO   A 1 367 ? -18.190 -25.589 13.250 1.00 21.59 ? 370  PRO   A N    1 
ATOM   2816 C  CA   . PRO   A 1 367 ? -19.202 -26.169 14.150 1.00 25.50 ? 370  PRO   A CA   1 
ATOM   2817 C  C    . PRO   A 1 367 ? -18.661 -27.265 15.051 1.00 25.36 ? 370  PRO   A C    1 
ATOM   2818 O  O    . PRO   A 1 367 ? -19.206 -27.465 16.141 1.00 26.21 ? 370  PRO   A O    1 
ATOM   2819 C  CB   . PRO   A 1 367 ? -20.270 -26.706 13.187 1.00 26.89 ? 370  PRO   A CB   1 
ATOM   2820 C  CG   . PRO   A 1 367 ? -19.571 -26.852 11.878 1.00 27.26 ? 370  PRO   A CG   1 
ATOM   2821 C  CD   . PRO   A 1 367 ? -18.597 -25.709 11.841 1.00 21.73 ? 370  PRO   A CD   1 
ATOM   2822 N  N    . LEU   A 1 368 ? -17.594 -27.959 14.651 1.00 21.01 ? 371  LEU   A N    1 
ATOM   2823 C  CA   . LEU   A 1 368 ? -16.998 -29.007 15.475 1.00 22.46 ? 371  LEU   A CA   1 
ATOM   2824 C  C    . LEU   A 1 368 ? -15.950 -28.493 16.457 1.00 25.53 ? 371  LEU   A C    1 
ATOM   2825 O  O    . LEU   A 1 368 ? -15.874 -28.989 17.588 1.00 25.68 ? 371  LEU   A O    1 
ATOM   2826 C  CB   . LEU   A 1 368 ? -16.351 -30.074 14.595 1.00 24.74 ? 371  LEU   A CB   1 
ATOM   2827 C  CG   . LEU   A 1 368 ? -17.220 -30.913 13.660 1.00 30.85 ? 371  LEU   A CG   1 
ATOM   2828 C  CD1  . LEU   A 1 368 ? -16.398 -32.039 13.064 1.00 29.14 ? 371  LEU   A CD1  1 
ATOM   2829 C  CD2  . LEU   A 1 368 ? -18.395 -31.477 14.413 1.00 34.01 ? 371  LEU   A CD2  1 
ATOM   2830 N  N    . VAL   A 1 369 ? -15.105 -27.545 16.051 1.00 20.94 ? 372  VAL   A N    1 
ATOM   2831 C  CA   . VAL   A 1 369 ? -13.935 -27.195 16.848 1.00 21.83 ? 372  VAL   A CA   1 
ATOM   2832 C  C    . VAL   A 1 369 ? -13.966 -25.763 17.358 1.00 24.08 ? 372  VAL   A C    1 
ATOM   2833 O  O    . VAL   A 1 369 ? -13.272 -25.467 18.342 1.00 26.83 ? 372  VAL   A O    1 
ATOM   2834 C  CB   . VAL   A 1 369 ? -12.622 -27.447 16.073 1.00 22.16 ? 372  VAL   A CB   1 
ATOM   2835 C  CG1  . VAL   A 1 369 ? -12.434 -28.940 15.808 1.00 23.12 ? 372  VAL   A CG1  1 
ATOM   2836 C  CG2  . VAL   A 1 369 ? -12.606 -26.641 14.782 1.00 22.74 ? 372  VAL   A CG2  1 
ATOM   2837 N  N    . CYS   A 1 370 ? -14.720 -24.861 16.729 1.00 21.97 ? 373  CYS   A N    1 
ATOM   2838 C  CA   . CYS   A 1 370 ? -14.965 -23.524 17.274 1.00 26.56 ? 373  CYS   A CA   1 
ATOM   2839 C  C    . CYS   A 1 370 ? -13.693 -22.678 17.285 1.00 27.58 ? 373  CYS   A C    1 
ATOM   2840 O  O    . CYS   A 1 370 ? -13.439 -21.927 18.227 1.00 28.34 ? 373  CYS   A O    1 
ATOM   2841 C  CB   . CYS   A 1 370 ? -15.539 -23.607 18.690 1.00 28.41 ? 373  CYS   A CB   1 
ATOM   2842 S  SG   . CYS   A 1 370 ? -17.005 -24.595 18.769 1.00 38.62 ? 373  CYS   A SG   1 
ATOM   2843 N  N    . ILE   A 1 371 ? -12.881 -22.785 16.247 1.00 24.71 ? 374  ILE   A N    1 
ATOM   2844 C  CA   . ILE   A 1 371 ? -11.628 -22.040 16.197 1.00 25.37 ? 374  ILE   A CA   1 
ATOM   2845 C  C    . ILE   A 1 371 ? -11.827 -20.823 15.306 1.00 28.15 ? 374  ILE   A C    1 
ATOM   2846 O  O    . ILE   A 1 371 ? -12.049 -20.958 14.097 1.00 24.93 ? 374  ILE   A O    1 
ATOM   2847 C  CB   . ILE   A 1 371 ? -10.469 -22.911 15.696 1.00 24.18 ? 374  ILE   A CB   1 
ATOM   2848 C  CG1  . ILE   A 1 371 ? -10.296 -24.140 16.590 1.00 23.86 ? 374  ILE   A CG1  1 
ATOM   2849 C  CG2  . ILE   A 1 371 ? -9.180  -22.084 15.664 1.00 25.62 ? 374  ILE   A CG2  1 
ATOM   2850 C  CD1  . ILE   A 1 371 ? -9.361  -25.189 16.014 1.00 18.92 ? 374  ILE   A CD1  1 
ATOM   2851 N  N    . ALA   A 1 372 ? -11.743 -19.635 15.906 1.00 31.93 ? 375  ALA   A N    1 
ATOM   2852 C  CA   . ALA   A 1 372 ? -11.922 -18.388 15.174 1.00 30.65 ? 375  ALA   A CA   1 
ATOM   2853 C  C    . ALA   A 1 372 ? -10.974 -18.315 13.982 1.00 30.39 ? 375  ALA   A C    1 
ATOM   2854 O  O    . ALA   A 1 372 ? -9.859  -18.839 14.016 1.00 30.36 ? 375  ALA   A O    1 
ATOM   2855 C  CB   . ALA   A 1 372 ? -11.688 -17.196 16.101 1.00 33.21 ? 375  ALA   A CB   1 
ATOM   2856 N  N    . LYS   A 1 373 ? -11.427 -17.645 12.918 1.00 31.50 ? 376  LYS   A N    1 
ATOM   2857 C  CA   . LYS   A 1 373 ? -10.658 -17.637 11.675 1.00 34.41 ? 376  LYS   A CA   1 
ATOM   2858 C  C    . LYS   A 1 373 ? -9.238  -17.120 11.885 1.00 35.00 ? 376  LYS   A C    1 
ATOM   2859 O  O    . LYS   A 1 373 ? -8.293  -17.625 11.268 1.00 34.51 ? 376  LYS   A O    1 
ATOM   2860 C  CB   . LYS   A 1 373 ? -11.377 -16.812 10.605 1.00 39.94 ? 376  LYS   A CB   1 
ATOM   2861 C  CG   . LYS   A 1 373 ? -10.653 -16.820 9.256  1.00 42.50 ? 376  LYS   A CG   1 
ATOM   2862 C  CD   . LYS   A 1 373 ? -11.617 -16.877 8.082  1.00 41.69 ? 376  LYS   A CD   1 
ATOM   2863 C  CE   . LYS   A 1 373 ? -12.631 -15.757 8.141  1.00 46.70 ? 376  LYS   A CE   1 
ATOM   2864 N  NZ   . LYS   A 1 373 ? -13.144 -15.386 6.788  1.00 51.25 ? 376  LYS   A NZ   1 
ATOM   2865 N  N    . GLU   A 1 374 ? -9.062  -16.133 12.770 1.00 34.13 ? 377  GLU   A N    1 
ATOM   2866 C  CA   . GLU   A 1 374 ? -7.735  -15.561 12.978 1.00 38.48 ? 377  GLU   A CA   1 
ATOM   2867 C  C    . GLU   A 1 374 ? -6.793  -16.542 13.651 1.00 34.72 ? 377  GLU   A C    1 
ATOM   2868 O  O    . GLU   A 1 374 ? -5.573  -16.369 13.571 1.00 34.97 ? 377  GLU   A O    1 
ATOM   2869 C  CB   . GLU   A 1 374 ? -7.812  -14.286 13.829 1.00 38.64 ? 377  GLU   A CB   1 
ATOM   2870 C  CG   . GLU   A 1 374 ? -8.936  -14.265 14.862 1.00 43.55 ? 377  GLU   A CG   1 
ATOM   2871 C  CD   . GLU   A 1 374 ? -10.268 -13.786 14.301 1.00 53.04 ? 377  GLU   A CD   1 
ATOM   2872 O  OE1  . GLU   A 1 374 ? -10.728 -12.697 14.714 1.00 62.14 ? 377  GLU   A OE1  1 
ATOM   2873 O  OE2  . GLU   A 1 374 ? -10.866 -14.509 13.470 1.00 59.76 ? 377  GLU   A OE2  1 
ATOM   2874 N  N    . LEU   A 1 375 ? -7.330  -17.563 14.317 1.00 31.68 ? 378  LEU   A N    1 
ATOM   2875 C  CA   . LEU   A 1 375 ? -6.531  -18.534 15.051 1.00 33.29 ? 378  LEU   A CA   1 
ATOM   2876 C  C    . LEU   A 1 375 ? -6.264  -19.802 14.248 1.00 30.61 ? 378  LEU   A C    1 
ATOM   2877 O  O    . LEU   A 1 375 ? -5.465  -20.642 14.685 1.00 29.34 ? 378  LEU   A O    1 
ATOM   2878 C  CB   . LEU   A 1 375 ? -7.240  -18.887 16.363 1.00 33.18 ? 378  LEU   A CB   1 
ATOM   2879 C  CG   . LEU   A 1 375 ? -7.422  -17.687 17.294 1.00 31.16 ? 378  LEU   A CG   1 
ATOM   2880 C  CD1  . LEU   A 1 375 ? -8.029  -18.097 18.613 1.00 30.66 ? 378  LEU   A CD1  1 
ATOM   2881 C  CD2  . LEU   A 1 375 ? -6.088  -16.972 17.505 1.00 34.74 ? 378  LEU   A CD2  1 
ATOM   2882 N  N    . ILE   A 1 376 ? -6.910  -19.946 13.089 1.00 29.56 ? 379  ILE   A N    1 
ATOM   2883 C  CA   . ILE   A 1 376 ? -6.694  -21.117 12.235 1.00 29.33 ? 379  ILE   A CA   1 
ATOM   2884 C  C    . ILE   A 1 376 ? -5.209  -21.330 11.929 1.00 28.60 ? 379  ILE   A C    1 
ATOM   2885 O  O    . ILE   A 1 376 ? -4.725  -22.460 12.088 1.00 26.44 ? 379  ILE   A O    1 
ATOM   2886 C  CB   . ILE   A 1 376 ? -7.553  -21.016 10.973 1.00 29.47 ? 379  ILE   A CB   1 
ATOM   2887 C  CG1  . ILE   A 1 376 ? -9.060  -20.958 11.300 1.00 28.44 ? 379  ILE   A CG1  1 
ATOM   2888 C  CG2  . ILE   A 1 376 ? -7.241  -22.153 10.001 1.00 26.44 ? 379  ILE   A CG2  1 
ATOM   2889 C  CD1  . ILE   A 1 376 ? -9.661  -22.260 11.705 1.00 28.17 ? 379  ILE   A CD1  1 
ATOM   2890 N  N    . PRO   A 1 377 ? -4.438  -20.313 11.496 1.00 31.20 ? 380  PRO   A N    1 
ATOM   2891 C  CA   . PRO   A 1 377 ? -3.031  -20.583 11.145 1.00 29.47 ? 380  PRO   A CA   1 
ATOM   2892 C  C    . PRO   A 1 377 ? -2.206  -21.109 12.302 1.00 29.88 ? 380  PRO   A C    1 
ATOM   2893 O  O    . PRO   A 1 377 ? -1.407  -22.033 12.118 1.00 29.71 ? 380  PRO   A O    1 
ATOM   2894 C  CB   . PRO   A 1 377 ? -2.514  -19.213 10.672 1.00 32.33 ? 380  PRO   A CB   1 
ATOM   2895 C  CG   . PRO   A 1 377 ? -3.706  -18.447 10.294 1.00 32.65 ? 380  PRO   A CG   1 
ATOM   2896 C  CD   . PRO   A 1 377 ? -4.833  -18.933 11.144 1.00 31.38 ? 380  PRO   A CD   1 
ATOM   2897 N  N    . GLU   A 1 378 ? -2.367  -20.535 13.493 1.00 28.48 ? 381  GLU   A N    1 
ATOM   2898 C  CA   . GLU   A 1 378 ? -1.570  -20.972 14.635 1.00 30.74 ? 381  GLU   A CA   1 
ATOM   2899 C  C    . GLU   A 1 378 ? -1.902  -22.414 15.024 1.00 28.79 ? 381  GLU   A C    1 
ATOM   2900 O  O    . GLU   A 1 378 ? -1.003  -23.227 15.279 1.00 27.63 ? 381  GLU   A O    1 
ATOM   2901 C  CB   . GLU   A 1 378 ? -1.812  -20.016 15.801 1.00 31.88 ? 381  GLU   A CB   1 
ATOM   2902 C  CG   . GLU   A 1 378 ? -1.196  -20.422 17.124 1.00 42.82 ? 381  GLU   A CG   1 
ATOM   2903 C  CD   . GLU   A 1 378 ? -1.644  -19.508 18.257 1.00 50.93 ? 381  GLU   A CD   1 
ATOM   2904 O  OE1  . GLU   A 1 378 ? -1.229  -19.744 19.421 1.00 53.51 ? 381  GLU   A OE1  1 
ATOM   2905 O  OE2  . GLU   A 1 378 ? -2.401  -18.546 17.971 1.00 49.76 ? 381  GLU   A OE2  1 
ATOM   2906 N  N    . ALA   A 1 379 ? -3.197  -22.746 15.077 1.00 28.91 ? 382  ALA   A N    1 
ATOM   2907 C  CA   . ALA   A 1 379 ? -3.612  -24.110 15.414 1.00 29.59 ? 382  ALA   A CA   1 
ATOM   2908 C  C    . ALA   A 1 379 ? -3.082  -25.112 14.391 1.00 24.31 ? 382  ALA   A C    1 
ATOM   2909 O  O    . ALA   A 1 379 ? -2.483  -26.148 14.743 1.00 27.89 ? 382  ALA   A O    1 
ATOM   2910 C  CB   . ALA   A 1 379 ? -5.140  -24.168 15.493 1.00 25.37 ? 382  ALA   A CB   1 
ATOM   2911 N  N    . THR   A 1 380 ? -3.266  -24.790 13.107 1.00 26.01 ? 383  THR   A N    1 
ATOM   2912 C  CA   . THR   A 1 380 ? -2.807  -25.680 12.053 1.00 26.02 ? 383  THR   A CA   1 
ATOM   2913 C  C    . THR   A 1 380 ? -1.293  -25.847 12.089 1.00 29.40 ? 383  THR   A C    1 
ATOM   2914 O  O    . THR   A 1 380 ? -0.788  -26.956 11.912 1.00 27.83 ? 383  THR   A O    1 
ATOM   2915 C  CB   . THR   A 1 380 ? -3.260  -25.152 10.702 1.00 24.10 ? 383  THR   A CB   1 
ATOM   2916 O  OG1  . THR   A 1 380 ? -4.668  -24.891 10.758 1.00 30.05 ? 383  THR   A OG1  1 
ATOM   2917 C  CG2  . THR   A 1 380 ? -3.004  -26.189 9.627  1.00 30.58 ? 383  THR   A CG2  1 
ATOM   2918 N  N    . GLU   A 1 381 ? -0.553  -24.758 12.324 1.00 27.99 ? 384  GLU   A N    1 
ATOM   2919 C  CA   . GLU   A 1 381 ? 0.904   -24.839 12.374 1.00 28.46 ? 384  GLU   A CA   1 
ATOM   2920 C  C    . GLU   A 1 381 ? 1.380   -25.679 13.551 1.00 30.07 ? 384  GLU   A C    1 
ATOM   2921 O  O    . GLU   A 1 381 ? 2.332   -26.461 13.420 1.00 28.33 ? 384  GLU   A O    1 
ATOM   2922 C  CB   . GLU   A 1 381 ? 1.501   -23.431 12.457 1.00 29.48 ? 384  GLU   A CB   1 
ATOM   2923 C  CG   . GLU   A 1 381 ? 3.006   -23.399 12.778 1.00 35.48 ? 384  GLU   A CG   1 
ATOM   2924 C  CD   . GLU   A 1 381 ? 3.888   -23.958 11.658 1.00 42.23 ? 384  GLU   A CD   1 
ATOM   2925 O  OE1  . GLU   A 1 381 ? 3.450   -23.981 10.488 1.00 39.79 ? 384  GLU   A OE1  1 
ATOM   2926 O  OE2  . GLU   A 1 381 ? 5.028   -24.382 11.956 1.00 48.05 ? 384  GLU   A OE2  1 
ATOM   2927 N  N    . LYS   A 1 382 ? 0.750   -25.506 14.715 1.00 31.68 ? 385  LYS   A N    1 
ATOM   2928 C  CA   . LYS   A 1 382 ? 1.108   -26.299 15.884 1.00 28.86 ? 385  LYS   A CA   1 
ATOM   2929 C  C    . LYS   A 1 382 ? 1.019   -27.787 15.584 1.00 27.75 ? 385  LYS   A C    1 
ATOM   2930 O  O    . LYS   A 1 382 ? 1.891   -28.566 15.989 1.00 27.89 ? 385  LYS   A O    1 
ATOM   2931 C  CB   . LYS   A 1 382 ? 0.185   -25.937 17.049 1.00 30.26 ? 385  LYS   A CB   1 
ATOM   2932 C  CG   . LYS   A 1 382 ? 0.514   -26.636 18.352 1.00 34.46 ? 385  LYS   A CG   1 
ATOM   2933 C  CD   . LYS   A 1 382 ? 1.805   -26.105 18.949 1.00 36.34 ? 385  LYS   A CD   1 
ATOM   2934 C  CE   . LYS   A 1 382 ? 2.211   -26.917 20.161 1.00 37.86 ? 385  LYS   A CE   1 
ATOM   2935 N  NZ   . LYS   A 1 382 ? 3.144   -26.131 21.036 1.00 45.71 ? 385  LYS   A NZ   1 
ATOM   2936 N  N    . TYR   A 1 383 ? -0.033  -28.206 14.876 1.00 27.92 ? 386  TYR   A N    1 
ATOM   2937 C  CA   . TYR   A 1 383 ? -0.127  -29.649 14.632 1.00 26.61 ? 386  TYR   A CA   1 
ATOM   2938 C  C    . TYR   A 1 383 ? 0.619   -30.128 13.381 1.00 26.41 ? 386  TYR   A C    1 
ATOM   2939 O  O    . TYR   A 1 383 ? 1.203   -31.222 13.387 1.00 26.32 ? 386  TYR   A O    1 
ATOM   2940 C  CB   . TYR   A 1 383 ? -1.597  -30.070 14.559 1.00 24.77 ? 386  TYR   A CB   1 
ATOM   2941 C  CG   . TYR   A 1 383 ? -2.174  -30.317 15.937 1.00 25.67 ? 386  TYR   A CG   1 
ATOM   2942 C  CD1  . TYR   A 1 383 ? -2.467  -29.260 16.791 1.00 22.97 ? 386  TYR   A CD1  1 
ATOM   2943 C  CD2  . TYR   A 1 383 ? -2.393  -31.618 16.395 1.00 26.16 ? 386  TYR   A CD2  1 
ATOM   2944 C  CE1  . TYR   A 1 383 ? -2.981  -29.485 18.061 1.00 23.08 ? 386  TYR   A CE1  1 
ATOM   2945 C  CE2  . TYR   A 1 383 ? -2.903  -31.858 17.668 1.00 25.02 ? 386  TYR   A CE2  1 
ATOM   2946 C  CZ   . TYR   A 1 383 ? -3.198  -30.790 18.493 1.00 22.56 ? 386  TYR   A CZ   1 
ATOM   2947 O  OH   . TYR   A 1 383 ? -3.703  -31.019 19.756 1.00 21.02 ? 386  TYR   A OH   1 
ATOM   2948 N  N    . LEU   A 1 384 ? 0.608   -29.343 12.307 1.00 26.68 ? 387  LEU   A N    1 
ATOM   2949 C  CA   . LEU   A 1 384 ? 1.061   -29.783 10.992 1.00 27.00 ? 387  LEU   A CA   1 
ATOM   2950 C  C    . LEU   A 1 384 ? 2.439   -29.250 10.617 1.00 32.18 ? 387  LEU   A C    1 
ATOM   2951 O  O    . LEU   A 1 384 ? 3.049   -29.771 9.680  1.00 33.84 ? 387  LEU   A O    1 
ATOM   2952 C  CB   . LEU   A 1 384 ? 0.086   -29.312 9.903  1.00 26.72 ? 387  LEU   A CB   1 
ATOM   2953 C  CG   . LEU   A 1 384 ? -1.371  -29.794 9.847  1.00 32.26 ? 387  LEU   A CG   1 
ATOM   2954 C  CD1  . LEU   A 1 384 ? -1.857  -29.930 8.406  1.00 32.21 ? 387  LEU   A CD1  1 
ATOM   2955 C  CD2  . LEU   A 1 384 ? -1.599  -31.049 10.641 1.00 28.75 ? 387  LEU   A CD2  1 
ATOM   2956 N  N    . GLY   A 1 385 ? 2.922   -28.210 11.303 1.00 32.09 ? 388  GLY   A N    1 
ATOM   2957 C  CA   . GLY   A 1 385 ? 4.113   -27.493 10.878 1.00 36.23 ? 388  GLY   A CA   1 
ATOM   2958 C  C    . GLY   A 1 385 ? 5.409   -28.269 11.003 1.00 40.17 ? 388  GLY   A C    1 
ATOM   2959 O  O    . GLY   A 1 385 ? 6.407   -27.887 10.380 1.00 44.22 ? 388  GLY   A O    1 
ATOM   2960 N  N    . GLY   A 1 386 ? 5.425   -29.344 11.790 1.00 37.43 ? 389  GLY   A N    1 
ATOM   2961 C  CA   . GLY   A 1 386 ? 6.647   -30.078 12.037 1.00 37.01 ? 389  GLY   A CA   1 
ATOM   2962 C  C    . GLY   A 1 386 ? 7.114   -31.016 10.943 1.00 42.76 ? 389  GLY   A C    1 
ATOM   2963 O  O    . GLY   A 1 386 ? 8.191   -31.607 11.074 1.00 46.19 ? 389  GLY   A O    1 
ATOM   2964 N  N    . THR   A 1 387 ? 6.344   -31.181 9.869  1.00 40.21 ? 390  THR   A N    1 
ATOM   2965 C  CA   . THR   A 1 387 ? 6.714   -32.078 8.784  1.00 40.59 ? 390  THR   A CA   1 
ATOM   2966 C  C    . THR   A 1 387 ? 6.249   -31.485 7.461  1.00 45.53 ? 390  THR   A C    1 
ATOM   2967 O  O    . THR   A 1 387 ? 5.279   -30.720 7.413  1.00 39.82 ? 390  THR   A O    1 
ATOM   2968 C  CB   . THR   A 1 387 ? 6.116   -33.488 8.984  1.00 41.83 ? 390  THR   A CB   1 
ATOM   2969 O  OG1  . THR   A 1 387 ? 6.224   -34.243 7.770  1.00 42.23 ? 390  THR   A OG1  1 
ATOM   2970 C  CG2  . THR   A 1 387 ? 4.644   -33.399 9.366  1.00 37.50 ? 390  THR   A CG2  1 
ATOM   2971 N  N    . ASP   A 1 388 ? 6.960   -31.838 6.386  1.00 44.14 ? 391  ASP   A N    1 
ATOM   2972 C  CA   . ASP   A 1 388 ? 6.542   -31.505 5.029  1.00 45.19 ? 391  ASP   A CA   1 
ATOM   2973 C  C    . ASP   A 1 388 ? 5.853   -32.669 4.320  1.00 41.33 ? 391  ASP   A C    1 
ATOM   2974 O  O    . ASP   A 1 388 ? 5.346   -32.486 3.208  1.00 42.99 ? 391  ASP   A O    1 
ATOM   2975 C  CB   . ASP   A 1 388 ? 7.746   -31.042 4.194  1.00 48.67 ? 391  ASP   A CB   1 
ATOM   2976 C  CG   . ASP   A 1 388 ? 8.594   -30.003 4.916  1.00 55.66 ? 391  ASP   A CG   1 
ATOM   2977 O  OD1  . ASP   A 1 388 ? 8.037   -28.963 5.328  1.00 57.03 ? 391  ASP   A OD1  1 
ATOM   2978 O  OD2  . ASP   A 1 388 ? 9.816   -30.228 5.077  1.00 61.55 ? 391  ASP   A OD2  1 
ATOM   2979 N  N    . ASP   A 1 389 ? 5.840   -33.853 4.927  1.00 37.90 ? 392  ASP   A N    1 
ATOM   2980 C  CA   . ASP   A 1 389 ? 5.113   -34.996 4.388  1.00 39.05 ? 392  ASP   A CA   1 
ATOM   2981 C  C    . ASP   A 1 389 ? 3.609   -34.770 4.548  1.00 38.72 ? 392  ASP   A C    1 
ATOM   2982 O  O    . ASP   A 1 389 ? 3.107   -34.689 5.674  1.00 38.20 ? 392  ASP   A O    1 
ATOM   2983 C  CB   . ASP   A 1 389 ? 5.564   -36.261 5.118  1.00 39.57 ? 392  ASP   A CB   1 
ATOM   2984 C  CG   . ASP   A 1 389 ? 4.907   -37.522 4.591  1.00 40.36 ? 392  ASP   A CG   1 
ATOM   2985 O  OD1  . ASP   A 1 389 ? 3.949   -37.436 3.791  1.00 44.11 ? 392  ASP   A OD1  1 
ATOM   2986 O  OD2  . ASP   A 1 389 ? 5.354   -38.615 4.998  1.00 42.04 ? 392  ASP   A OD2  1 
ATOM   2987 N  N    . THR   A 1 390 ? 2.884   -34.678 3.427  1.00 36.91 ? 393  THR   A N    1 
ATOM   2988 C  CA   . THR   A 1 390 ? 1.475   -34.301 3.489  1.00 36.40 ? 393  THR   A CA   1 
ATOM   2989 C  C    . THR   A 1 390 ? 0.564   -35.456 3.895  1.00 35.69 ? 393  THR   A C    1 
ATOM   2990 O  O    . THR   A 1 390 ? -0.561  -35.207 4.358  1.00 34.34 ? 393  THR   A O    1 
ATOM   2991 C  CB   . THR   A 1 390 ? 1.018   -33.706 2.150  1.00 37.81 ? 393  THR   A CB   1 
ATOM   2992 O  OG1  . THR   A 1 390 ? 1.316   -34.612 1.079  1.00 42.07 ? 393  THR   A OG1  1 
ATOM   2993 C  CG2  . THR   A 1 390 ? 1.693   -32.361 1.899  1.00 37.86 ? 393  THR   A CG2  1 
ATOM   2994 N  N    . VAL   A 1 391 ? 1.019   -36.702 3.754  1.00 34.39 ? 394  VAL   A N    1 
ATOM   2995 C  CA   . VAL   A 1 391 ? 0.294   -37.821 4.351  1.00 36.36 ? 394  VAL   A CA   1 
ATOM   2996 C  C    . VAL   A 1 391 ? 0.313   -37.701 5.872  1.00 35.73 ? 394  VAL   A C    1 
ATOM   2997 O  O    . VAL   A 1 391 ? -0.722  -37.840 6.555  1.00 32.65 ? 394  VAL   A O    1 
ATOM   2998 C  CB   . VAL   A 1 391 ? 0.901   -39.153 3.874  1.00 38.88 ? 394  VAL   A CB   1 
ATOM   2999 C  CG1  . VAL   A 1 391 ? 0.300   -40.327 4.638  1.00 35.32 ? 394  VAL   A CG1  1 
ATOM   3000 C  CG2  . VAL   A 1 391 ? 0.694   -39.316 2.376  1.00 37.47 ? 394  VAL   A CG2  1 
ATOM   3001 N  N    . LYS   A 1 392 ? 1.498   -37.425 6.423  1.00 33.84 ? 395  LYS   A N    1 
ATOM   3002 C  CA   . LYS   A 1 392 ? 1.613   -37.176 7.851  1.00 35.97 ? 395  LYS   A CA   1 
ATOM   3003 C  C    . LYS   A 1 392 ? 0.786   -35.968 8.258  1.00 33.20 ? 395  LYS   A C    1 
ATOM   3004 O  O    . LYS   A 1 392 ? 0.207   -35.949 9.349  1.00 31.04 ? 395  LYS   A O    1 
ATOM   3005 C  CB   . LYS   A 1 392 ? 3.077   -36.976 8.238  1.00 34.63 ? 395  LYS   A CB   1 
ATOM   3006 C  CG   . LYS   A 1 392 ? 3.910   -38.249 8.146  1.00 40.95 ? 395  LYS   A CG   1 
ATOM   3007 C  CD   . LYS   A 1 392 ? 5.218   -38.138 8.924  1.00 45.46 ? 395  LYS   A CD   1 
ATOM   3008 C  CE   . LYS   A 1 392 ? 5.973   -39.467 8.916  1.00 49.92 ? 395  LYS   A CE   1 
ATOM   3009 N  NZ   . LYS   A 1 392 ? 7.384   -39.325 9.369  1.00 54.62 ? 395  LYS   A NZ   1 
ATOM   3010 N  N    . LYS   A 1 393 ? 0.720   -34.947 7.397  1.00 31.06 ? 396  LYS   A N    1 
ATOM   3011 C  CA   . LYS   A 1 393 ? -0.102  -33.787 7.720  1.00 28.46 ? 396  LYS   A CA   1 
ATOM   3012 C  C    . LYS   A 1 393 ? -1.572  -34.170 7.837  1.00 29.39 ? 396  LYS   A C    1 
ATOM   3013 O  O    . LYS   A 1 393 ? -2.270  -33.672 8.723  1.00 28.03 ? 396  LYS   A O    1 
ATOM   3014 C  CB   . LYS   A 1 393 ? 0.076   -32.680 6.685  1.00 31.04 ? 396  LYS   A CB   1 
ATOM   3015 C  CG   . LYS   A 1 393 ? 1.379   -31.893 6.793  1.00 30.69 ? 396  LYS   A CG   1 
ATOM   3016 C  CD   . LYS   A 1 393 ? 1.360   -30.742 5.787  1.00 35.64 ? 396  LYS   A CD   1 
ATOM   3017 C  CE   . LYS   A 1 393 ? 2.717   -30.045 5.657  1.00 37.73 ? 396  LYS   A CE   1 
ATOM   3018 N  NZ   . LYS   A 1 393 ? 3.173   -29.445 6.940  1.00 33.58 ? 396  LYS   A NZ   1 
ATOM   3019 N  N    . LYS   A 1 394 ? -2.068  -35.037 6.946  1.00 26.13 ? 397  LYS   A N    1 
ATOM   3020 C  CA   . LYS   A 1 394 ? -3.451  -35.488 7.087  1.00 29.69 ? 397  LYS   A CA   1 
ATOM   3021 C  C    . LYS   A 1 394 ? -3.657  -36.173 8.437  1.00 32.05 ? 397  LYS   A C    1 
ATOM   3022 O  O    . LYS   A 1 394 ? -4.624  -35.882 9.162  1.00 28.44 ? 397  LYS   A O    1 
ATOM   3023 C  CB   . LYS   A 1 394 ? -3.842  -36.437 5.954  1.00 33.45 ? 397  LYS   A CB   1 
ATOM   3024 C  CG   . LYS   A 1 394 ? -5.191  -37.107 6.220  1.00 35.86 ? 397  LYS   A CG   1 
ATOM   3025 C  CD   . LYS   A 1 394 ? -5.424  -38.368 5.402  1.00 41.70 ? 397  LYS   A CD   1 
ATOM   3026 C  CE   . LYS   A 1 394 ? -6.920  -38.725 5.385  1.00 36.70 ? 397  LYS   A CE   1 
ATOM   3027 N  NZ   . LYS   A 1 394 ? -7.356  -39.504 4.186  1.00 38.10 ? 397  LYS   A NZ   1 
ATOM   3028 N  N    . ASP   A 1 395 ? -2.745  -37.084 8.795  1.00 26.75 ? 398  ASP   A N    1 
ATOM   3029 C  CA   . ASP   A 1 395 ? -2.890  -37.787 10.074 1.00 30.58 ? 398  ASP   A CA   1 
ATOM   3030 C  C    . ASP   A 1 395 ? -2.857  -36.824 11.256 1.00 28.67 ? 398  ASP   A C    1 
ATOM   3031 O  O    . ASP   A 1 395 ? -3.613  -36.981 12.230 1.00 26.49 ? 398  ASP   A O    1 
ATOM   3032 C  CB   . ASP   A 1 395 ? -1.801  -38.844 10.229 1.00 30.45 ? 398  ASP   A CB   1 
ATOM   3033 C  CG   . ASP   A 1 395 ? -1.988  -40.013 9.278  1.00 38.43 ? 398  ASP   A CG   1 
ATOM   3034 O  OD1  . ASP   A 1 395 ? -3.141  -40.253 8.847  1.00 40.03 ? 398  ASP   A OD1  1 
ATOM   3035 O  OD2  . ASP   A 1 395 ? -0.981  -40.682 8.957  1.00 43.00 ? 398  ASP   A OD2  1 
ATOM   3036 N  N    . LEU   A 1 396 ? -1.986  -35.816 11.191 1.00 24.09 ? 399  LEU   A N    1 
ATOM   3037 C  CA   . LEU   A 1 396 ? -1.883  -34.849 12.281 1.00 24.49 ? 399  LEU   A CA   1 
ATOM   3038 C  C    . LEU   A 1 396 ? -3.107  -33.940 12.346 1.00 23.81 ? 399  LEU   A C    1 
ATOM   3039 O  O    . LEU   A 1 396 ? -3.495  -33.496 13.432 1.00 21.28 ? 399  LEU   A O    1 
ATOM   3040 C  CB   . LEU   A 1 396 ? -0.606  -34.024 12.116 1.00 25.15 ? 399  LEU   A CB   1 
ATOM   3041 C  CG   . LEU   A 1 396 ? 0.687   -34.801 12.403 1.00 28.91 ? 399  LEU   A CG   1 
ATOM   3042 C  CD1  . LEU   A 1 396 ? 1.909   -34.106 11.787 1.00 29.54 ? 399  LEU   A CD1  1 
ATOM   3043 C  CD2  . LEU   A 1 396 ? 0.874   -35.011 13.903 1.00 27.38 ? 399  LEU   A CD2  1 
ATOM   3044 N  N    . PHE   A 1 397 ? -3.715  -33.644 11.200 1.00 21.48 ? 400  PHE   A N    1 
ATOM   3045 C  CA   . PHE   A 1 397 ? -4.967  -32.895 11.188 1.00 22.56 ? 400  PHE   A CA   1 
ATOM   3046 C  C    . PHE   A 1 397 ? -6.070  -33.678 11.893 1.00 25.06 ? 400  PHE   A C    1 
ATOM   3047 O  O    . PHE   A 1 397 ? -6.873  -33.112 12.660 1.00 21.54 ? 400  PHE   A O    1 
ATOM   3048 C  CB   . PHE   A 1 397 ? -5.358  -32.605 9.739  1.00 22.06 ? 400  PHE   A CB   1 
ATOM   3049 C  CG   . PHE   A 1 397 ? -6.594  -31.778 9.593  1.00 25.48 ? 400  PHE   A CG   1 
ATOM   3050 C  CD1  . PHE   A 1 397 ? -6.546  -30.406 9.741  1.00 29.81 ? 400  PHE   A CD1  1 
ATOM   3051 C  CD2  . PHE   A 1 397 ? -7.814  -32.380 9.310  1.00 27.80 ? 400  PHE   A CD2  1 
ATOM   3052 C  CE1  . PHE   A 1 397 ? -7.696  -29.640 9.604  1.00 28.11 ? 400  PHE   A CE1  1 
ATOM   3053 C  CE2  . PHE   A 1 397 ? -8.965  -31.628 9.173  1.00 29.20 ? 400  PHE   A CE2  1 
ATOM   3054 C  CZ   . PHE   A 1 397 ? -8.907  -30.253 9.321  1.00 27.84 ? 400  PHE   A CZ   1 
ATOM   3055 N  N    . LEU   A 1 398 ? -6.130  -34.987 11.627 1.00 20.62 ? 401  LEU   A N    1 
ATOM   3056 C  CA   . LEU   A 1 398 ? -7.105  -35.823 12.323 1.00 26.06 ? 401  LEU   A CA   1 
ATOM   3057 C  C    . LEU   A 1 398 ? -6.848  -35.835 13.828 1.00 22.92 ? 401  LEU   A C    1 
ATOM   3058 O  O    . LEU   A 1 398 ? -7.799  -35.806 14.626 1.00 21.81 ? 401  LEU   A O    1 
ATOM   3059 C  CB   . LEU   A 1 398 ? -7.084  -37.237 11.745 1.00 24.54 ? 401  LEU   A CB   1 
ATOM   3060 C  CG   . LEU   A 1 398 ? -7.565  -37.317 10.292 1.00 24.52 ? 401  LEU   A CG   1 
ATOM   3061 C  CD1  . LEU   A 1 398 ? -7.620  -38.770 9.826  1.00 28.67 ? 401  LEU   A CD1  1 
ATOM   3062 C  CD2  . LEU   A 1 398 ? -8.916  -36.632 10.121 1.00 24.17 ? 401  LEU   A CD2  1 
ATOM   3063 N  N    . ASP   A 1 399 ? -5.567  -35.847 14.236 1.00 20.92 ? 402  ASP   A N    1 
ATOM   3064 C  CA   . ASP   A 1 399 ? -5.240  -35.712 15.663 1.00 22.50 ? 402  ASP   A CA   1 
ATOM   3065 C  C    . ASP   A 1 399 ? -5.738  -34.387 16.235 1.00 22.60 ? 402  ASP   A C    1 
ATOM   3066 O  O    . ASP   A 1 399 ? -6.192  -34.331 17.384 1.00 20.31 ? 402  ASP   A O    1 
ATOM   3067 C  CB   . ASP   A 1 399 ? -3.728  -35.799 15.912 1.00 25.00 ? 402  ASP   A CB   1 
ATOM   3068 C  CG   . ASP   A 1 399 ? -3.145  -37.170 15.634 1.00 33.85 ? 402  ASP   A CG   1 
ATOM   3069 O  OD1  . ASP   A 1 399 ? -3.904  -38.163 15.528 1.00 32.79 ? 402  ASP   A OD1  1 
ATOM   3070 O  OD2  . ASP   A 1 399 ? -1.897  -37.252 15.577 1.00 34.16 ? 402  ASP   A OD2  1 
ATOM   3071 N  N    . LEU   A 1 400 ? -5.564  -33.296 15.481 1.00 21.02 ? 403  LEU   A N    1 
ATOM   3072 C  CA   . LEU   A 1 400 ? -6.019  -31.978 15.924 1.00 21.22 ? 403  LEU   A CA   1 
ATOM   3073 C  C    . LEU   A 1 400 ? -7.510  -31.991 16.247 1.00 17.86 ? 403  LEU   A C    1 
ATOM   3074 O  O    . LEU   A 1 400 ? -7.937  -31.563 17.333 1.00 20.29 ? 403  LEU   A O    1 
ATOM   3075 C  CB   . LEU   A 1 400 ? -5.726  -30.938 14.831 1.00 21.10 ? 403  LEU   A CB   1 
ATOM   3076 C  CG   . LEU   A 1 400 ? -5.849  -29.438 15.127 1.00 20.69 ? 403  LEU   A CG   1 
ATOM   3077 C  CD1  . LEU   A 1 400 ? -5.160  -28.647 14.025 1.00 22.37 ? 403  LEU   A CD1  1 
ATOM   3078 C  CD2  . LEU   A 1 400 ? -7.314  -28.989 15.230 1.00 18.54 ? 403  LEU   A CD2  1 
ATOM   3079 N  N    . ILE   A 1 401 ? -8.318  -32.427 15.287 1.00 18.28 ? 404  ILE   A N    1 
ATOM   3080 C  CA   . ILE   A 1 401 ? -9.764  -32.463 15.518 1.00 20.05 ? 404  ILE   A CA   1 
ATOM   3081 C  C    . ILE   A 1 401 ? -10.104 -33.372 16.702 1.00 19.33 ? 404  ILE   A C    1 
ATOM   3082 O  O    . ILE   A 1 401 ? -10.928 -33.011 17.558 1.00 18.38 ? 404  ILE   A O    1 
ATOM   3083 C  CB   . ILE   A 1 401 ? -10.504 -32.866 14.231 1.00 21.17 ? 404  ILE   A CB   1 
ATOM   3084 C  CG1  . ILE   A 1 401 ? -10.264 -31.787 13.164 1.00 24.15 ? 404  ILE   A CG1  1 
ATOM   3085 C  CG2  . ILE   A 1 401 ? -12.002 -33.050 14.500 1.00 20.70 ? 404  ILE   A CG2  1 
ATOM   3086 C  CD1  . ILE   A 1 401 ? -11.219 -31.803 12.017 1.00 32.48 ? 404  ILE   A CD1  1 
ATOM   3087 N  N    . ALA   A 1 402 ? -9.446  -34.535 16.805 1.00 18.60 ? 405  ALA   A N    1 
ATOM   3088 C  CA   . ALA   A 1 402 ? -9.733  -35.440 17.921 1.00 17.21 ? 405  ALA   A CA   1 
ATOM   3089 C  C    . ALA   A 1 402 ? -9.417  -34.801 19.271 1.00 17.98 ? 405  ALA   A C    1 
ATOM   3090 O  O    . ALA   A 1 402 ? -10.179 -34.961 20.236 1.00 16.23 ? 405  ALA   A O    1 
ATOM   3091 C  CB   . ALA   A 1 402 ? -8.951  -36.746 17.758 1.00 17.04 ? 405  ALA   A CB   1 
ATOM   3092 N  N    . ASP   A 1 403 ? -8.293  -34.085 19.367 1.00 14.89 ? 406  ASP   A N    1 
ATOM   3093 C  CA   . ASP   A 1 403 ? -7.926  -33.424 20.617 1.00 14.95 ? 406  ASP   A CA   1 
ATOM   3094 C  C    . ASP   A 1 403 ? -8.916  -32.321 20.981 1.00 17.71 ? 406  ASP   A C    1 
ATOM   3095 O  O    . ASP   A 1 403 ? -9.237  -32.131 22.163 1.00 14.71 ? 406  ASP   A O    1 
ATOM   3096 C  CB   . ASP   A 1 403 ? -6.510  -32.835 20.517 1.00 17.51 ? 406  ASP   A CB   1 
ATOM   3097 C  CG   . ASP   A 1 403 ? -5.431  -33.881 20.589 1.00 23.55 ? 406  ASP   A CG   1 
ATOM   3098 O  OD1  . ASP   A 1 403 ? -5.763  -35.058 20.859 1.00 22.30 ? 406  ASP   A OD1  1 
ATOM   3099 O  OD2  . ASP   A 1 403 ? -4.242  -33.522 20.363 1.00 22.73 ? 406  ASP   A OD2  1 
ATOM   3100 N  N    . VAL   A 1 404 ? -9.377  -31.547 19.996 1.00 15.24 ? 407  VAL   A N    1 
ATOM   3101 C  CA   . VAL   A 1 404 ? -10.309 -30.466 20.328 1.00 16.25 ? 407  VAL   A CA   1 
ATOM   3102 C  C    . VAL   A 1 404 ? -11.679 -31.018 20.727 1.00 18.45 ? 407  VAL   A C    1 
ATOM   3103 O  O    . VAL   A 1 404 ? -12.313 -30.515 21.665 1.00 16.34 ? 407  VAL   A O    1 
ATOM   3104 C  CB   . VAL   A 1 404 ? -10.435 -29.466 19.168 1.00 18.14 ? 407  VAL   A CB   1 
ATOM   3105 C  CG1  . VAL   A 1 404 ? -11.501 -28.409 19.506 1.00 21.38 ? 407  VAL   A CG1  1 
ATOM   3106 C  CG2  . VAL   A 1 404 ? -9.099  -28.783 18.935 1.00 20.05 ? 407  VAL   A CG2  1 
ATOM   3107 N  N    . MET   A 1 405 ? -12.172 -32.034 20.022 1.00 16.29 ? 408  MET   A N    1 
ATOM   3108 C  CA   . MET   A 1 405 ? -13.522 -32.523 20.323 1.00 18.23 ? 408  MET   A CA   1 
ATOM   3109 C  C    . MET   A 1 405 ? -13.569 -33.449 21.534 1.00 18.35 ? 408  MET   A C    1 
ATOM   3110 O  O    . MET   A 1 405 ? -14.542 -33.408 22.300 1.00 18.87 ? 408  MET   A O    1 
ATOM   3111 C  CB   . MET   A 1 405 ? -14.125 -33.239 19.124 1.00 17.75 ? 408  MET   A CB   1 
ATOM   3112 C  CG   . MET   A 1 405 ? -14.083 -32.477 17.830 1.00 20.81 ? 408  MET   A CG   1 
ATOM   3113 S  SD   . MET   A 1 405 ? -14.962 -33.460 16.593 1.00 27.07 ? 408  MET   A SD   1 
ATOM   3114 C  CE   . MET   A 1 405 ? -16.505 -33.845 17.450 1.00 26.87 ? 408  MET   A CE   1 
ATOM   3115 N  N    . PHE   A 1 406 ? -12.567 -34.306 21.708 1.00 13.97 ? 409  PHE   A N    1 
ATOM   3116 C  CA   . PHE   A 1 406 ? -12.642 -35.379 22.695 1.00 17.15 ? 409  PHE   A CA   1 
ATOM   3117 C  C    . PHE   A 1 406 ? -11.540 -35.332 23.742 1.00 15.93 ? 409  PHE   A C    1 
ATOM   3118 O  O    . PHE   A 1 406 ? -11.849 -35.346 24.935 1.00 18.14 ? 409  PHE   A O    1 
ATOM   3119 C  CB   . PHE   A 1 406 ? -12.630 -36.738 21.975 1.00 15.84 ? 409  PHE   A CB   1 
ATOM   3120 C  CG   . PHE   A 1 406 ? -13.824 -36.951 21.096 1.00 18.88 ? 409  PHE   A CG   1 
ATOM   3121 C  CD1  . PHE   A 1 406 ? -15.093 -37.127 21.645 1.00 19.40 ? 409  PHE   A CD1  1 
ATOM   3122 C  CD2  . PHE   A 1 406 ? -13.695 -36.889 19.713 1.00 19.12 ? 409  PHE   A CD2  1 
ATOM   3123 C  CE1  . PHE   A 1 406 ? -16.205 -37.296 20.828 1.00 20.62 ? 409  PHE   A CE1  1 
ATOM   3124 C  CE2  . PHE   A 1 406 ? -14.793 -37.051 18.886 1.00 18.88 ? 409  PHE   A CE2  1 
ATOM   3125 C  CZ   . PHE   A 1 406 ? -16.063 -37.257 19.443 1.00 20.40 ? 409  PHE   A CZ   1 
ATOM   3126 N  N    . GLY   A 1 407 ? -10.261 -35.277 23.346 1.00 15.71 ? 410  GLY   A N    1 
ATOM   3127 C  CA   . GLY   A 1 407 ? -9.188  -35.485 24.320 1.00 15.33 ? 410  GLY   A CA   1 
ATOM   3128 C  C    . GLY   A 1 407 ? -9.108  -34.385 25.367 1.00 14.43 ? 410  GLY   A C    1 
ATOM   3129 O  O    . GLY   A 1 407 ? -9.102  -34.649 26.579 1.00 14.92 ? 410  GLY   A O    1 
ATOM   3130 N  N    . VAL   A 1 408 ? -9.027  -33.140 24.919 1.00 15.84 ? 411  VAL   A N    1 
ATOM   3131 C  CA   . VAL   A 1 408 ? -8.902  -32.007 25.830 1.00 16.51 ? 411  VAL   A CA   1 
ATOM   3132 C  C    . VAL   A 1 408 ? -10.177 -31.853 26.661 1.00 14.92 ? 411  VAL   A C    1 
ATOM   3133 O  O    . VAL   A 1 408 ? -10.074 -31.724 27.899 1.00 13.62 ? 411  VAL   A O    1 
ATOM   3134 C  CB   . VAL   A 1 408 ? -8.530  -30.735 25.046 1.00 16.21 ? 411  VAL   A CB   1 
ATOM   3135 C  CG1  . VAL   A 1 408 ? -8.749  -29.499 25.877 1.00 17.03 ? 411  VAL   A CG1  1 
ATOM   3136 C  CG2  . VAL   A 1 408 ? -7.053  -30.845 24.593 1.00 16.03 ? 411  VAL   A CG2  1 
ATOM   3137 N  N    . PRO   A 1 409 ? -11.385 -31.855 26.062 1.00 14.18 ? 412  PRO   A N    1 
ATOM   3138 C  CA   . PRO   A 1 409 ? -12.597 -31.788 26.902 1.00 16.06 ? 412  PRO   A CA   1 
ATOM   3139 C  C    . PRO   A 1 409 ? -12.643 -32.876 27.957 1.00 14.73 ? 412  PRO   A C    1 
ATOM   3140 O  O    . PRO   A 1 409 ? -12.987 -32.596 29.115 1.00 13.70 ? 412  PRO   A O    1 
ATOM   3141 C  CB   . PRO   A 1 409 ? -13.739 -31.927 25.882 1.00 17.72 ? 412  PRO   A CB   1 
ATOM   3142 C  CG   . PRO   A 1 409 ? -13.187 -31.340 24.644 1.00 19.48 ? 412  PRO   A CG   1 
ATOM   3143 C  CD   . PRO   A 1 409 ? -11.732 -31.786 24.625 1.00 13.75 ? 412  PRO   A CD   1 
ATOM   3144 N  N    . SER   A 1 410 ? -12.245 -34.102 27.596 1.00 13.78 ? 413  SER   A N    1 
ATOM   3145 C  CA   . SER   A 1 410 ? -12.276 -35.205 28.546 1.00 13.52 ? 413  SER   A CA   1 
ATOM   3146 C  C    . SER   A 1 410 ? -11.343 -34.949 29.712 1.00 15.52 ? 413  SER   A C    1 
ATOM   3147 O  O    . SER   A 1 410 ? -11.718 -35.148 30.873 1.00 13.09 ? 413  SER   A O    1 
ATOM   3148 C  CB   . SER   A 1 410 ? -11.920 -36.522 27.850 1.00 15.64 ? 413  SER   A CB   1 
ATOM   3149 O  OG   . SER   A 1 410 ? -12.933 -36.858 26.909 1.00 17.74 ? 413  SER   A OG   1 
ATOM   3150 N  N    . VAL   A 1 411 ? -10.114 -34.498 29.429 1.00 14.81 ? 414  VAL   A N    1 
ATOM   3151 C  CA   . VAL   A 1 411 ? -9.181  -34.282 30.529 1.00 13.82 ? 414  VAL   A CA   1 
ATOM   3152 C  C    . VAL   A 1 411 ? -9.631  -33.109 31.394 1.00 14.35 ? 414  VAL   A C    1 
ATOM   3153 O  O    . VAL   A 1 411 ? -9.507  -33.154 32.622 1.00 14.20 ? 414  VAL   A O    1 
ATOM   3154 C  CB   . VAL   A 1 411 ? -7.744  -34.109 29.995 1.00 14.26 ? 414  VAL   A CB   1 
ATOM   3155 C  CG1  . VAL   A 1 411 ? -6.813  -33.553 31.087 1.00 15.50 ? 414  VAL   A CG1  1 
ATOM   3156 C  CG2  . VAL   A 1 411 ? -7.231  -35.452 29.493 1.00 13.86 ? 414  VAL   A CG2  1 
ATOM   3157 N  N    . ILE   A 1 412 ? -10.179 -32.054 30.785 1.00 12.44 ? 415  ILE   A N    1 
ATOM   3158 C  CA   . ILE   A 1 412 ? -10.670 -30.938 31.592 1.00 14.93 ? 415  ILE   A CA   1 
ATOM   3159 C  C    . ILE   A 1 412 ? -11.810 -31.392 32.505 1.00 15.91 ? 415  ILE   A C    1 
ATOM   3160 O  O    . ILE   A 1 412 ? -11.848 -31.042 33.695 1.00 15.34 ? 415  ILE   A O    1 
ATOM   3161 C  CB   . ILE   A 1 412 ? -11.074 -29.755 30.694 1.00 17.48 ? 415  ILE   A CB   1 
ATOM   3162 C  CG1  . ILE   A 1 412 ? -9.833  -29.191 29.975 1.00 16.30 ? 415  ILE   A CG1  1 
ATOM   3163 C  CG2  . ILE   A 1 412 ? -11.744 -28.649 31.517 1.00 17.14 ? 415  ILE   A CG2  1 
ATOM   3164 C  CD1  . ILE   A 1 412 ? -10.155 -28.078 29.007 1.00 20.88 ? 415  ILE   A CD1  1 
ATOM   3165 N  N    . VAL   A 1 413 ? -12.732 -32.209 31.982 1.00 14.18 ? 416  VAL   A N    1 
ATOM   3166 C  CA   . VAL   A 1 413 ? -13.819 -32.723 32.811 1.00 12.57 ? 416  VAL   A CA   1 
ATOM   3167 C  C    . VAL   A 1 413 ? -13.260 -33.556 33.953 1.00 15.12 ? 416  VAL   A C    1 
ATOM   3168 O  O    . VAL   A 1 413 ? -13.656 -33.391 35.115 1.00 14.75 ? 416  VAL   A O    1 
ATOM   3169 C  CB   . VAL   A 1 413 ? -14.825 -33.518 31.953 1.00 15.78 ? 416  VAL   A CB   1 
ATOM   3170 C  CG1  . VAL   A 1 413 ? -15.678 -34.456 32.822 1.00 17.25 ? 416  VAL   A CG1  1 
ATOM   3171 C  CG2  . VAL   A 1 413 ? -15.724 -32.563 31.178 1.00 12.93 ? 416  VAL   A CG2  1 
ATOM   3172 N  N    . ALA   A 1 414 ? -12.301 -34.444 33.648 1.00 13.41 ? 417  ALA   A N    1 
ATOM   3173 C  CA   . ALA   A 1 414 ? -11.735 -35.294 34.684 1.00 13.16 ? 417  ALA   A CA   1 
ATOM   3174 C  C    . ALA   A 1 414 ? -11.027 -34.467 35.750 1.00 16.00 ? 417  ALA   A C    1 
ATOM   3175 O  O    . ALA   A 1 414 ? -11.142 -34.754 36.946 1.00 15.18 ? 417  ALA   A O    1 
ATOM   3176 C  CB   . ALA   A 1 414 ? -10.769 -36.311 34.061 1.00 14.74 ? 417  ALA   A CB   1 
ATOM   3177 N  N    . ARG   A 1 415 ? -10.257 -33.458 35.332 1.00 14.65 ? 418  ARG   A N    1 
ATOM   3178 C  CA   . ARG   A 1 415 ? -9.550  -32.616 36.290 1.00 18.38 ? 418  ARG   A CA   1 
ATOM   3179 C  C    . ARG   A 1 415 ? -10.522 -31.882 37.212 1.00 18.61 ? 418  ARG   A C    1 
ATOM   3180 O  O    . ARG   A 1 415 ? -10.332 -31.847 38.434 1.00 17.53 ? 418  ARG   A O    1 
ATOM   3181 C  CB   . ARG   A 1 415 ? -8.655  -31.629 35.540 1.00 17.37 ? 418  ARG   A CB   1 
ATOM   3182 C  CG   . ARG   A 1 415 ? -7.368  -32.268 35.047 1.00 16.69 ? 418  ARG   A CG   1 
ATOM   3183 C  CD   . ARG   A 1 415 ? -6.557  -31.277 34.211 1.00 19.64 ? 418  ARG   A CD   1 
ATOM   3184 N  NE   . ARG   A 1 415 ? -5.286  -31.859 33.793 1.00 20.27 ? 418  ARG   A NE   1 
ATOM   3185 C  CZ   . ARG   A 1 415 ? -4.419  -31.259 32.988 1.00 22.04 ? 418  ARG   A CZ   1 
ATOM   3186 N  NH1  . ARG   A 1 415 ? -4.695  -30.093 32.428 1.00 17.22 ? 418  ARG   A NH1  1 
ATOM   3187 N  NH2  . ARG   A 1 415 ? -3.249  -31.847 32.736 1.00 21.18 ? 418  ARG   A NH2  1 
ATOM   3188 N  N    . ASN   A 1 416 ? -11.574 -31.290 36.643 1.00 15.04 ? 419  ASN   A N    1 
ATOM   3189 C  CA   . ASN   A 1 416 ? -12.565 -30.604 37.469 1.00 19.67 ? 419  ASN   A CA   1 
ATOM   3190 C  C    . ASN   A 1 416 ? -13.281 -31.567 38.425 1.00 19.57 ? 419  ASN   A C    1 
ATOM   3191 O  O    . ASN   A 1 416 ? -13.513 -31.242 39.605 1.00 20.16 ? 419  ASN   A O    1 
ATOM   3192 C  CB   . ASN   A 1 416 ? -13.554 -29.881 36.559 1.00 19.01 ? 419  ASN   A CB   1 
ATOM   3193 C  CG   . ASN   A 1 416 ? -13.034 -28.542 36.108 1.00 24.94 ? 419  ASN   A CG   1 
ATOM   3194 O  OD1  . ASN   A 1 416 ? -12.579 -28.378 34.970 1.00 25.81 ? 419  ASN   A OD1  1 
ATOM   3195 N  ND2  . ASN   A 1 416 ? -13.082 -27.569 37.004 1.00 22.86 ? 419  ASN   A ND2  1 
ATOM   3196 N  N    . HIS   A 1 417 ? -13.601 -32.774 37.949 1.00 17.60 ? 420  HIS   A N    1 
ATOM   3197 C  CA   . HIS   A 1 417 ? -14.232 -33.775 38.809 1.00 17.76 ? 420  HIS   A CA   1 
ATOM   3198 C  C    . HIS   A 1 417 ? -13.319 -34.173 39.962 1.00 18.48 ? 420  HIS   A C    1 
ATOM   3199 O  O    . HIS   A 1 417 ? -13.742 -34.214 41.125 1.00 20.99 ? 420  HIS   A O    1 
ATOM   3200 C  CB   . HIS   A 1 417 ? -14.594 -35.015 37.994 1.00 17.75 ? 420  HIS   A CB   1 
ATOM   3201 C  CG   . HIS   A 1 417 ? -15.783 -35.741 38.527 1.00 16.10 ? 420  HIS   A CG   1 
ATOM   3202 N  ND1  . HIS   A 1 417 ? -17.063 -35.249 38.385 1.00 15.70 ? 420  HIS   A ND1  1 
ATOM   3203 C  CD2  . HIS   A 1 417 ? -15.895 -36.895 39.228 1.00 18.01 ? 420  HIS   A CD2  1 
ATOM   3204 C  CE1  . HIS   A 1 417 ? -17.917 -36.082 38.956 1.00 13.33 ? 420  HIS   A CE1  1 
ATOM   3205 N  NE2  . HIS   A 1 417 ? -17.233 -37.082 39.483 1.00 16.10 ? 420  HIS   A NE2  1 
ATOM   3206 N  N    . ARG   A 1 418 ? -12.063 -34.489 39.648 1.00 17.64 ? 421  ARG   A N    1 
ATOM   3207 C  CA   . ARG   A 1 418 ? -11.060 -34.777 40.666 1.00 21.39 ? 421  ARG   A CA   1 
ATOM   3208 C  C    . ARG   A 1 418 ? -10.966 -33.645 41.682 1.00 21.74 ? 421  ARG   A C    1 
ATOM   3209 O  O    . ARG   A 1 418 ? -10.888 -33.883 42.893 1.00 23.70 ? 421  ARG   A O    1 
ATOM   3210 C  CB   . ARG   A 1 418 ? -9.696  -34.985 39.999 1.00 18.32 ? 421  ARG   A CB   1 
ATOM   3211 C  CG   . ARG   A 1 418 ? -8.530  -35.064 40.967 1.00 24.57 ? 421  ARG   A CG   1 
ATOM   3212 C  CD   . ARG   A 1 418 ? -7.226  -34.759 40.232 1.00 21.06 ? 421  ARG   A CD   1 
ATOM   3213 N  NE   . ARG   A 1 418 ? -7.236  -33.406 39.692 1.00 20.51 ? 421  ARG   A NE   1 
ATOM   3214 C  CZ   . ARG   A 1 418 ? -6.331  -32.935 38.846 1.00 22.27 ? 421  ARG   A CZ   1 
ATOM   3215 N  NH1  . ARG   A 1 418 ? -5.389  -33.713 38.343 1.00 20.85 ? 421  ARG   A NH1  1 
ATOM   3216 N  NH2  . ARG   A 1 418 ? -6.376  -31.651 38.493 1.00 21.53 ? 421  ARG   A NH2  1 
ATOM   3217 N  N    . ASP   A 1 419 ? -10.942 -32.404 41.197 1.00 18.26 ? 422  ASP   A N    1 
ATOM   3218 C  CA   . ASP   A 1 419 ? -10.751 -31.252 42.072 1.00 23.87 ? 422  ASP   A CA   1 
ATOM   3219 C  C    . ASP   A 1 419 ? -11.957 -30.990 42.954 1.00 26.99 ? 422  ASP   A C    1 
ATOM   3220 O  O    . ASP   A 1 419 ? -11.837 -30.241 43.927 1.00 23.58 ? 422  ASP   A O    1 
ATOM   3221 C  CB   . ASP   A 1 419 ? -10.407 -30.019 41.235 1.00 24.91 ? 422  ASP   A CB   1 
ATOM   3222 C  CG   . ASP   A 1 419 ? -8.987  -30.080 40.679 1.00 28.19 ? 422  ASP   A CG   1 
ATOM   3223 O  OD1  . ASP   A 1 419 ? -8.280  -31.055 40.989 1.00 29.91 ? 422  ASP   A OD1  1 
ATOM   3224 O  OD2  . ASP   A 1 419 ? -8.598  -29.183 39.905 1.00 39.01 ? 422  ASP   A OD2  1 
ATOM   3225 N  N    . ALA   A 1 420 ? -13.114 -31.586 42.647 1.00 22.17 ? 423  ALA   A N    1 
ATOM   3226 C  CA   . ALA   A 1 420 ? -14.227 -31.543 43.587 1.00 27.04 ? 423  ALA   A CA   1 
ATOM   3227 C  C    . ALA   A 1 420 ? -14.170 -32.666 44.616 1.00 23.80 ? 423  ALA   A C    1 
ATOM   3228 O  O    . ALA   A 1 420 ? -15.148 -32.880 45.344 1.00 29.81 ? 423  ALA   A O    1 
ATOM   3229 C  CB   . ALA   A 1 420 ? -15.562 -31.591 42.844 1.00 25.05 ? 423  ALA   A CB   1 
ATOM   3230 N  N    . GLY   A 1 421 ? -13.069 -33.404 44.681 1.00 21.83 ? 424  GLY   A N    1 
ATOM   3231 C  CA   . GLY   A 1 421 ? -12.923 -34.472 45.640 1.00 23.89 ? 424  GLY   A CA   1 
ATOM   3232 C  C    . GLY   A 1 421 ? -13.503 -35.808 45.226 1.00 24.37 ? 424  GLY   A C    1 
ATOM   3233 O  O    . GLY   A 1 421 ? -13.499 -36.737 46.036 1.00 24.61 ? 424  GLY   A O    1 
ATOM   3234 N  N    . ALA   A 1 422 ? -13.995 -35.941 44.002 1.00 22.13 ? 425  ALA   A N    1 
ATOM   3235 C  CA   . ALA   A 1 422 ? -14.620 -37.204 43.651 1.00 22.30 ? 425  ALA   A CA   1 
ATOM   3236 C  C    . ALA   A 1 422 ? -13.591 -38.182 43.091 1.00 21.32 ? 425  ALA   A C    1 
ATOM   3237 O  O    . ALA   A 1 422 ? -12.656 -37.771 42.398 1.00 23.14 ? 425  ALA   A O    1 
ATOM   3238 C  CB   . ALA   A 1 422 ? -15.720 -36.979 42.615 1.00 21.78 ? 425  ALA   A CB   1 
ATOM   3239 N  N    . PRO   A 1 423 ? -13.759 -39.478 43.368 1.00 21.98 ? 426  PRO   A N    1 
ATOM   3240 C  CA   . PRO   A 1 423 ? -12.899 -40.488 42.736 1.00 24.30 ? 426  PRO   A CA   1 
ATOM   3241 C  C    . PRO   A 1 423 ? -13.052 -40.434 41.223 1.00 24.60 ? 426  PRO   A C    1 
ATOM   3242 O  O    . PRO   A 1 423 ? -14.163 -40.475 40.693 1.00 19.10 ? 426  PRO   A O    1 
ATOM   3243 C  CB   . PRO   A 1 423 ? -13.412 -41.816 43.313 1.00 23.29 ? 426  PRO   A CB   1 
ATOM   3244 C  CG   . PRO   A 1 423 ? -14.228 -41.448 44.513 1.00 24.54 ? 426  PRO   A CG   1 
ATOM   3245 C  CD   . PRO   A 1 423 ? -14.820 -40.099 44.184 1.00 23.23 ? 426  PRO   A CD   1 
ATOM   3246 N  N    . THR   A 1 424 ? -11.927 -40.301 40.531 1.00 18.42 ? 427  THR   A N    1 
ATOM   3247 C  CA   . THR   A 1 424 ? -11.923 -40.093 39.090 1.00 15.82 ? 427  THR   A CA   1 
ATOM   3248 C  C    . THR   A 1 424 ? -10.924 -41.053 38.472 1.00 20.08 ? 427  THR   A C    1 
ATOM   3249 O  O    . THR   A 1 424 ? -9.854  -41.297 39.045 1.00 18.72 ? 427  THR   A O    1 
ATOM   3250 C  CB   . THR   A 1 424 ? -11.573 -38.635 38.732 1.00 17.38 ? 427  THR   A CB   1 
ATOM   3251 O  OG1  . THR   A 1 424 ? -12.438 -37.733 39.443 1.00 18.58 ? 427  THR   A OG1  1 
ATOM   3252 C  CG2  . THR   A 1 424 ? -11.707 -38.386 37.229 1.00 15.43 ? 427  THR   A CG2  1 
ATOM   3253 N  N    . TYR   A 1 425 ? -11.280 -41.610 37.312 1.00 15.81 ? 428  TYR   A N    1 
ATOM   3254 C  CA   . TYR   A 1 425 ? -10.416 -42.550 36.610 1.00 17.54 ? 428  TYR   A CA   1 
ATOM   3255 C  C    . TYR   A 1 425 ? -10.397 -42.192 35.136 1.00 18.28 ? 428  TYR   A C    1 
ATOM   3256 O  O    . TYR   A 1 425 ? -11.398 -41.734 34.597 1.00 16.91 ? 428  TYR   A O    1 
ATOM   3257 C  CB   . TYR   A 1 425 ? -10.898 -43.995 36.770 1.00 15.88 ? 428  TYR   A CB   1 
ATOM   3258 C  CG   . TYR   A 1 425 ? -10.671 -44.541 38.149 1.00 17.87 ? 428  TYR   A CG   1 
ATOM   3259 C  CD1  . TYR   A 1 425 ? -11.588 -44.301 39.170 1.00 18.50 ? 428  TYR   A CD1  1 
ATOM   3260 C  CD2  . TYR   A 1 425 ? -9.537  -45.295 38.436 1.00 16.36 ? 428  TYR   A CD2  1 
ATOM   3261 C  CE1  . TYR   A 1 425 ? -11.374 -44.782 40.440 1.00 20.93 ? 428  TYR   A CE1  1 
ATOM   3262 C  CE2  . TYR   A 1 425 ? -9.314  -45.785 39.712 1.00 18.03 ? 428  TYR   A CE2  1 
ATOM   3263 C  CZ   . TYR   A 1 425 ? -10.232 -45.532 40.699 1.00 21.62 ? 428  TYR   A CZ   1 
ATOM   3264 O  OH   . TYR   A 1 425 ? -10.018 -46.028 41.950 1.00 23.71 ? 428  TYR   A OH   1 
ATOM   3265 N  N    . MET   A 1 426 ? -9.265  -42.393 34.476 1.00 13.93 ? 429  MET   A N    1 
ATOM   3266 C  CA   . MET   A 1 426 ? -9.169  -42.068 33.061 1.00 12.35 ? 429  MET   A CA   1 
ATOM   3267 C  C    . MET   A 1 426 ? -8.550  -43.229 32.300 1.00 15.16 ? 429  MET   A C    1 
ATOM   3268 O  O    . MET   A 1 426 ? -7.707  -43.965 32.833 1.00 15.12 ? 429  MET   A O    1 
ATOM   3269 C  CB   . MET   A 1 426 ? -8.331  -40.801 32.857 1.00 13.98 ? 429  MET   A CB   1 
ATOM   3270 C  CG   . MET   A 1 426 ? -9.131  -39.543 32.985 1.00 16.52 ? 429  MET   A CG   1 
ATOM   3271 S  SD   . MET   A 1 426 ? -8.442  -38.132 32.118 1.00 17.66 ? 429  MET   A SD   1 
ATOM   3272 C  CE   . MET   A 1 426 ? -9.501  -38.155 30.683 1.00 16.69 ? 429  MET   A CE   1 
ATOM   3273 N  N    . TYR   A 1 427 ? -8.950  -43.375 31.039 1.00 12.77 ? 430  TYR   A N    1 
ATOM   3274 C  CA   . TYR   A 1 427 ? -8.284  -44.364 30.195 1.00 15.43 ? 430  TYR   A CA   1 
ATOM   3275 C  C    . TYR   A 1 427 ? -8.074  -43.811 28.789 1.00 14.73 ? 430  TYR   A C    1 
ATOM   3276 O  O    . TYR   A 1 427 ? -8.737  -42.859 28.356 1.00 15.10 ? 430  TYR   A O    1 
ATOM   3277 C  CB   . TYR   A 1 427 ? -9.042  -45.716 30.119 1.00 12.64 ? 430  TYR   A CB   1 
ATOM   3278 C  CG   . TYR   A 1 427 ? -10.347 -45.657 29.348 1.00 14.86 ? 430  TYR   A CG   1 
ATOM   3279 C  CD1  . TYR   A 1 427 ? -10.359 -45.693 27.948 1.00 15.64 ? 430  TYR   A CD1  1 
ATOM   3280 C  CD2  . TYR   A 1 427 ? -11.578 -45.582 30.016 1.00 13.84 ? 430  TYR   A CD2  1 
ATOM   3281 C  CE1  . TYR   A 1 427 ? -11.556 -45.614 27.241 1.00 14.77 ? 430  TYR   A CE1  1 
ATOM   3282 C  CE2  . TYR   A 1 427 ? -12.771 -45.525 29.317 1.00 12.94 ? 430  TYR   A CE2  1 
ATOM   3283 C  CZ   . TYR   A 1 427 ? -12.757 -45.551 27.928 1.00 15.96 ? 430  TYR   A CZ   1 
ATOM   3284 O  OH   . TYR   A 1 427 ? -13.925 -45.449 27.205 1.00 16.06 ? 430  TYR   A OH   1 
ATOM   3285 N  N    . GLU   A 1 428 ? -7.105  -44.419 28.094 1.00 14.98 ? 431  GLU   A N    1 
ATOM   3286 C  CA   . GLU   A 1 428 ? -6.910  -44.242 26.657 1.00 15.68 ? 431  GLU   A CA   1 
ATOM   3287 C  C    . GLU   A 1 428 ? -6.859  -45.612 26.007 1.00 17.19 ? 431  GLU   A C    1 
ATOM   3288 O  O    . GLU   A 1 428 ? -5.958  -46.401 26.313 1.00 16.35 ? 431  GLU   A O    1 
ATOM   3289 C  CB   . GLU   A 1 428 ? -5.620  -43.469 26.352 1.00 17.31 ? 431  GLU   A CB   1 
ATOM   3290 C  CG   . GLU   A 1 428 ? -5.610  -42.943 24.934 1.00 21.30 ? 431  GLU   A CG   1 
ATOM   3291 C  CD   . GLU   A 1 428 ? -4.262  -42.390 24.508 1.00 30.38 ? 431  GLU   A CD   1 
ATOM   3292 O  OE1  . GLU   A 1 428 ? -4.278  -41.439 23.700 1.00 28.54 ? 431  GLU   A OE1  1 
ATOM   3293 O  OE2  . GLU   A 1 428 ? -3.210  -42.924 24.943 1.00 29.72 ? 431  GLU   A OE2  1 
ATOM   3294 N  N    . PHE   A 1 429 ? -7.797  -45.871 25.093 1.00 15.09 ? 432  PHE   A N    1 
ATOM   3295 C  CA   . PHE   A 1 429 ? -8.018  -47.187 24.498 1.00 14.64 ? 432  PHE   A CA   1 
ATOM   3296 C  C    . PHE   A 1 429 ? -7.374  -47.247 23.120 1.00 18.83 ? 432  PHE   A C    1 
ATOM   3297 O  O    . PHE   A 1 429 ? -7.658  -46.406 22.259 1.00 16.29 ? 432  PHE   A O    1 
ATOM   3298 C  CB   . PHE   A 1 429 ? -9.517  -47.474 24.368 1.00 14.45 ? 432  PHE   A CB   1 
ATOM   3299 C  CG   . PHE   A 1 429 ? -9.831  -48.832 23.821 1.00 13.49 ? 432  PHE   A CG   1 
ATOM   3300 C  CD1  . PHE   A 1 429 ? -9.891  -49.930 24.652 1.00 16.11 ? 432  PHE   A CD1  1 
ATOM   3301 C  CD2  . PHE   A 1 429 ? -10.069 -49.015 22.459 1.00 15.02 ? 432  PHE   A CD2  1 
ATOM   3302 C  CE1  . PHE   A 1 429 ? -10.192 -51.207 24.155 1.00 14.90 ? 432  PHE   A CE1  1 
ATOM   3303 C  CE2  . PHE   A 1 429 ? -10.371 -50.289 21.948 1.00 15.89 ? 432  PHE   A CE2  1 
ATOM   3304 C  CZ   . PHE   A 1 429 ? -10.434 -51.378 22.792 1.00 15.24 ? 432  PHE   A CZ   1 
ATOM   3305 N  N    . GLN   A 1 430 ? -6.525  -48.249 22.907 1.00 16.13 ? 433  GLN   A N    1 
ATOM   3306 C  CA   . GLN   A 1 430 ? -5.765  -48.369 21.658 1.00 21.45 ? 433  GLN   A CA   1 
ATOM   3307 C  C    . GLN   A 1 430 ? -5.830  -49.814 21.175 1.00 22.90 ? 433  GLN   A C    1 
ATOM   3308 O  O    . GLN   A 1 430 ? -5.043  -50.655 21.614 1.00 23.82 ? 433  GLN   A O    1 
ATOM   3309 C  CB   . GLN   A 1 430 ? -4.318  -47.943 21.854 1.00 21.24 ? 433  GLN   A CB   1 
ATOM   3310 C  CG   . GLN   A 1 430 ? -3.613  -47.663 20.562 1.00 26.95 ? 433  GLN   A CG   1 
ATOM   3311 C  CD   . GLN   A 1 430 ? -2.184  -47.182 20.783 1.00 33.93 ? 433  GLN   A CD   1 
ATOM   3312 O  OE1  . GLN   A 1 430 ? -1.779  -46.903 21.912 1.00 37.42 ? 433  GLN   A OE1  1 
ATOM   3313 N  NE2  . GLN   A 1 430 ? -1.424  -47.078 19.705 1.00 35.43 ? 433  GLN   A NE2  1 
ATOM   3314 N  N    . TYR   A 1 431 ? -6.746  -50.091 20.257 1.00 20.13 ? 434  TYR   A N    1 
ATOM   3315 C  CA   . TYR   A 1 431 ? -6.871  -51.428 19.694 1.00 21.15 ? 434  TYR   A CA   1 
ATOM   3316 C  C    . TYR   A 1 431 ? -7.645  -51.316 18.399 1.00 23.08 ? 434  TYR   A C    1 
ATOM   3317 O  O    . TYR   A 1 431 ? -8.490  -50.426 18.240 1.00 24.03 ? 434  TYR   A O    1 
ATOM   3318 C  CB   . TYR   A 1 431 ? -7.576  -52.400 20.645 1.00 18.81 ? 434  TYR   A CB   1 
ATOM   3319 C  CG   . TYR   A 1 431 ? -7.331  -53.858 20.321 1.00 19.21 ? 434  TYR   A CG   1 
ATOM   3320 C  CD1  . TYR   A 1 431 ? -6.091  -54.444 20.555 1.00 21.00 ? 434  TYR   A CD1  1 
ATOM   3321 C  CD2  . TYR   A 1 431 ? -8.334  -54.645 19.769 1.00 19.88 ? 434  TYR   A CD2  1 
ATOM   3322 C  CE1  . TYR   A 1 431 ? -5.862  -55.777 20.266 1.00 19.64 ? 434  TYR   A CE1  1 
ATOM   3323 C  CE2  . TYR   A 1 431 ? -8.116  -55.984 19.466 1.00 22.51 ? 434  TYR   A CE2  1 
ATOM   3324 C  CZ   . TYR   A 1 431 ? -6.873  -56.544 19.718 1.00 25.47 ? 434  TYR   A CZ   1 
ATOM   3325 O  OH   . TYR   A 1 431 ? -6.648  -57.876 19.432 1.00 29.82 ? 434  TYR   A OH   1 
ATOM   3326 N  N    . ARG   A 1 432 ? -7.350  -52.220 17.473 1.00 19.20 ? 435  ARG   A N    1 
ATOM   3327 C  CA   . ARG   A 1 432 ? -8.124  -52.275 16.240 1.00 20.19 ? 435  ARG   A CA   1 
ATOM   3328 C  C    . ARG   A 1 432 ? -8.940  -53.560 16.231 1.00 21.07 ? 435  ARG   A C    1 
ATOM   3329 O  O    . ARG   A 1 432 ? -8.382  -54.647 16.017 1.00 21.71 ? 435  ARG   A O    1 
ATOM   3330 C  CB   . ARG   A 1 432 ? -7.221  -52.201 15.006 1.00 24.57 ? 435  ARG   A CB   1 
ATOM   3331 C  CG   . ARG   A 1 432 ? -8.027  -52.023 13.732 1.00 24.48 ? 435  ARG   A CG   1 
ATOM   3332 C  CD   . ARG   A 1 432 ? -7.175  -52.000 12.483 1.00 29.78 ? 435  ARG   A CD   1 
ATOM   3333 N  NE   . ARG   A 1 432 ? -7.974  -51.641 11.316 1.00 32.60 ? 435  ARG   A NE   1 
ATOM   3334 C  CZ   . ARG   A 1 432 ? -8.803  -52.475 10.699 1.00 35.77 ? 435  ARG   A CZ   1 
ATOM   3335 N  NH1  . ARG   A 1 432 ? -8.978  -53.718 11.123 1.00 34.98 ? 435  ARG   A NH1  1 
ATOM   3336 N  NH2  . ARG   A 1 432 ? -9.466  -52.054 9.623  1.00 36.49 ? 435  ARG   A NH2  1 
ATOM   3337 N  N    . PRO   A 1 433 ? -10.251 -53.500 16.460 1.00 19.10 ? 436  PRO   A N    1 
ATOM   3338 C  CA   . PRO   A 1 433 ? -11.036 -54.739 16.535 1.00 18.25 ? 436  PRO   A CA   1 
ATOM   3339 C  C    . PRO   A 1 433 ? -11.111 -55.429 15.186 1.00 21.90 ? 436  PRO   A C    1 
ATOM   3340 O  O    . PRO   A 1 433 ? -11.126 -54.784 14.138 1.00 22.74 ? 436  PRO   A O    1 
ATOM   3341 C  CB   . PRO   A 1 433 ? -12.424 -54.277 17.006 1.00 21.79 ? 436  PRO   A CB   1 
ATOM   3342 C  CG   . PRO   A 1 433 ? -12.330 -52.805 17.231 1.00 23.04 ? 436  PRO   A CG   1 
ATOM   3343 C  CD   . PRO   A 1 433 ? -11.042 -52.283 16.732 1.00 21.14 ? 436  PRO   A CD   1 
ATOM   3344 N  N    . SER   A 1 434 ? -11.140 -56.765 15.221 1.00 21.18 ? 437  SER   A N    1 
ATOM   3345 C  CA   . SER   A 1 434 ? -11.392 -57.520 13.999 1.00 26.23 ? 437  SER   A CA   1 
ATOM   3346 C  C    . SER   A 1 434 ? -12.783 -57.240 13.440 1.00 25.56 ? 437  SER   A C    1 
ATOM   3347 O  O    . SER   A 1 434 ? -13.025 -57.459 12.248 1.00 27.09 ? 437  SER   A O    1 
ATOM   3348 C  CB   . SER   A 1 434 ? -11.202 -59.017 14.274 1.00 29.11 ? 437  SER   A CB   1 
ATOM   3349 O  OG   . SER   A 1 434 ? -12.138 -59.479 15.236 1.00 29.02 ? 437  SER   A OG   1 
ATOM   3350 N  N    . PHE   A 1 435 ? -13.687 -56.723 14.267 1.00 24.32 ? 438  PHE   A N    1 
ATOM   3351 C  CA   . PHE   A 1 435 ? -15.052 -56.391 13.877 1.00 25.00 ? 438  PHE   A CA   1 
ATOM   3352 C  C    . PHE   A 1 435 ? -15.148 -55.068 13.128 1.00 30.60 ? 438  PHE   A C    1 
ATOM   3353 O  O    . PHE   A 1 435 ? -16.259 -54.646 12.787 1.00 32.37 ? 438  PHE   A O    1 
ATOM   3354 C  CB   . PHE   A 1 435 ? -15.909 -56.344 15.134 1.00 24.22 ? 438  PHE   A CB   1 
ATOM   3355 C  CG   . PHE   A 1 435 ? -15.693 -57.516 16.023 1.00 23.55 ? 438  PHE   A CG   1 
ATOM   3356 C  CD1  . PHE   A 1 435 ? -15.978 -58.801 15.583 1.00 28.89 ? 438  PHE   A CD1  1 
ATOM   3357 C  CD2  . PHE   A 1 435 ? -15.135 -57.348 17.280 1.00 22.03 ? 438  PHE   A CD2  1 
ATOM   3358 C  CE1  . PHE   A 1 435 ? -15.749 -59.898 16.402 1.00 27.04 ? 438  PHE   A CE1  1 
ATOM   3359 C  CE2  . PHE   A 1 435 ? -14.899 -58.436 18.101 1.00 24.05 ? 438  PHE   A CE2  1 
ATOM   3360 C  CZ   . PHE   A 1 435 ? -15.208 -59.716 17.662 1.00 23.76 ? 438  PHE   A CZ   1 
ATOM   3361 N  N    . SER   A 1 436 ? -14.016 -54.401 12.900 1.00 27.77 ? 439  SER   A N    1 
ATOM   3362 C  CA   . SER   A 1 436 ? -13.984 -53.158 12.143 1.00 31.09 ? 439  SER   A CA   1 
ATOM   3363 C  C    . SER   A 1 436 ? -14.565 -53.366 10.753 1.00 31.87 ? 439  SER   A C    1 
ATOM   3364 O  O    . SER   A 1 436 ? -14.459 -54.449 10.169 1.00 29.72 ? 439  SER   A O    1 
ATOM   3365 C  CB   . SER   A 1 436 ? -12.541 -52.646 12.010 1.00 30.75 ? 439  SER   A CB   1 
ATOM   3366 O  OG   . SER   A 1 436 ? -11.935 -52.426 13.272 1.00 30.47 ? 439  SER   A OG   1 
ATOM   3367 N  N    . SER   A 1 437 ? -15.172 -52.304 10.219 1.00 28.35 ? 440  SER   A N    1 
ATOM   3368 C  CA   . SER   A 1 437 ? -15.635 -52.315 8.838  1.00 32.79 ? 440  SER   A CA   1 
ATOM   3369 C  C    . SER   A 1 437 ? -14.486 -52.643 7.887  1.00 33.75 ? 440  SER   A C    1 
ATOM   3370 O  O    . SER   A 1 437 ? -13.346 -52.227 8.100  1.00 29.53 ? 440  SER   A O    1 
ATOM   3371 C  CB   . SER   A 1 437 ? -16.244 -50.957 8.478  1.00 33.49 ? 440  SER   A CB   1 
ATOM   3372 O  OG   . SER   A 1 437 ? -16.551 -50.881 7.094  1.00 31.67 ? 440  SER   A OG   1 
ATOM   3373 N  N    . ASP   A 1 438 ? -14.791 -53.404 6.830  1.00 37.17 ? 441  ASP   A N    1 
ATOM   3374 C  CA   . ASP   A 1 438 ? -13.794 -53.674 5.798  1.00 40.41 ? 441  ASP   A CA   1 
ATOM   3375 C  C    . ASP   A 1 438 ? -13.402 -52.418 5.033  1.00 42.10 ? 441  ASP   A C    1 
ATOM   3376 O  O    . ASP   A 1 438 ? -12.362 -52.413 4.362  1.00 42.96 ? 441  ASP   A O    1 
ATOM   3377 C  CB   . ASP   A 1 438 ? -14.309 -54.727 4.816  1.00 44.19 ? 441  ASP   A CB   1 
ATOM   3378 C  CG   . ASP   A 1 438 ? -14.529 -56.075 5.472  1.00 50.30 ? 441  ASP   A CG   1 
ATOM   3379 O  OD1  . ASP   A 1 438 ? -13.638 -56.526 6.230  1.00 57.25 ? 441  ASP   A OD1  1 
ATOM   3380 O  OD2  . ASP   A 1 438 ? -15.594 -56.682 5.231  1.00 55.04 ? 441  ASP   A OD2  1 
ATOM   3381 N  N    . MET   A 1 439 ? -14.211 -51.362 5.114  1.00 39.56 ? 442  MET   A N    1 
ATOM   3382 C  CA   . MET   A 1 439 ? -13.888 -50.087 4.487  1.00 36.55 ? 442  MET   A CA   1 
ATOM   3383 C  C    . MET   A 1 439 ? -12.862 -49.280 5.273  1.00 37.03 ? 442  MET   A C    1 
ATOM   3384 O  O    . MET   A 1 439 ? -12.375 -48.267 4.762  1.00 37.30 ? 442  MET   A O    1 
ATOM   3385 C  CB   . MET   A 1 439 ? -15.164 -49.260 4.310  1.00 39.64 ? 442  MET   A CB   1 
ATOM   3386 C  CG   . MET   A 1 439 ? -16.280 -49.986 3.569  1.00 40.20 ? 442  MET   A CG   1 
ATOM   3387 S  SD   . MET   A 1 439 ? -17.644 -48.891 3.124  1.00 60.99 ? 442  MET   A SD   1 
ATOM   3388 C  CE   . MET   A 1 439 ? -16.957 -48.014 1.719  1.00 55.18 ? 442  MET   A CE   1 
ATOM   3389 N  N    . LYS   A 1 440 ? -12.519 -49.700 6.481  1.00 33.15 ? 443  LYS   A N    1 
ATOM   3390 C  CA   . LYS   A 1 440 ? -11.663 -48.928 7.379  1.00 33.51 ? 443  LYS   A CA   1 
ATOM   3391 C  C    . LYS   A 1 440 ? -10.199 -49.276 7.134  1.00 33.74 ? 443  LYS   A C    1 
ATOM   3392 O  O    . LYS   A 1 440 ? -9.850  -50.459 7.125  1.00 30.08 ? 443  LYS   A O    1 
ATOM   3393 C  CB   . LYS   A 1 440 ? -12.044 -49.223 8.823  1.00 30.10 ? 443  LYS   A CB   1 
ATOM   3394 C  CG   . LYS   A 1 440 ? -11.214 -48.600 9.933  1.00 29.10 ? 443  LYS   A CG   1 
ATOM   3395 C  CD   . LYS   A 1 440 ? -11.699 -49.245 11.249 1.00 29.31 ? 443  LYS   A CD   1 
ATOM   3396 C  CE   . LYS   A 1 440 ? -10.941 -48.829 12.501 1.00 32.82 ? 443  LYS   A CE   1 
ATOM   3397 N  NZ   . LYS   A 1 440 ? -11.608 -49.438 13.712 1.00 28.30 ? 443  LYS   A NZ   1 
ATOM   3398 N  N    . PRO   A 1 441 ? -9.331  -48.282 6.921  1.00 33.19 ? 444  PRO   A N    1 
ATOM   3399 C  CA   . PRO   A 1 441 ? -7.908  -48.572 6.688  1.00 32.58 ? 444  PRO   A CA   1 
ATOM   3400 C  C    . PRO   A 1 441 ? -7.312  -49.375 7.829  1.00 35.28 ? 444  PRO   A C    1 
ATOM   3401 O  O    . PRO   A 1 441 ? -7.658  -49.183 8.996  1.00 31.52 ? 444  PRO   A O    1 
ATOM   3402 C  CB   . PRO   A 1 441 ? -7.272  -47.182 6.599  1.00 33.95 ? 444  PRO   A CB   1 
ATOM   3403 C  CG   . PRO   A 1 441 ? -8.383  -46.287 6.171  1.00 35.99 ? 444  PRO   A CG   1 
ATOM   3404 C  CD   . PRO   A 1 441 ? -9.624  -46.843 6.826  1.00 32.04 ? 444  PRO   A CD   1 
ATOM   3405 N  N    . LYS   A 1 442 ? -6.392  -50.277 7.481  1.00 33.93 ? 445  LYS   A N    1 
ATOM   3406 C  CA   . LYS   A 1 442 ? -5.801  -51.147 8.490  1.00 32.38 ? 445  LYS   A CA   1 
ATOM   3407 C  C    . LYS   A 1 442 ? -4.933  -50.372 9.476  1.00 31.62 ? 445  LYS   A C    1 
ATOM   3408 O  O    . LYS   A 1 442 ? -4.635  -50.889 10.558 1.00 32.56 ? 445  LYS   A O    1 
ATOM   3409 C  CB   . LYS   A 1 442 ? -4.974  -52.255 7.822  1.00 39.02 ? 445  LYS   A CB   1 
ATOM   3410 C  CG   . LYS   A 1 442 ? -5.760  -53.118 6.819  1.00 43.74 ? 445  LYS   A CG   1 
ATOM   3411 C  CD   . LYS   A 1 442 ? -7.091  -53.622 7.388  1.00 45.14 ? 445  LYS   A CD   1 
ATOM   3412 C  CE   . LYS   A 1 442 ? -6.901  -54.693 8.462  1.00 49.09 ? 445  LYS   A CE   1 
ATOM   3413 N  NZ   . LYS   A 1 442 ? -7.700  -55.922 8.186  1.00 51.41 ? 445  LYS   A NZ   1 
ATOM   3414 N  N    . THR   A 1 443 ? -4.533  -49.148 9.134  1.00 30.63 ? 446  THR   A N    1 
ATOM   3415 C  CA   . THR   A 1 443 ? -3.683  -48.342 10.002 1.00 32.73 ? 446  THR   A CA   1 
ATOM   3416 C  C    . THR   A 1 443 ? -4.456  -47.560 11.059 1.00 29.46 ? 446  THR   A C    1 
ATOM   3417 O  O    . THR   A 1 443 ? -3.833  -47.005 11.968 1.00 30.17 ? 446  THR   A O    1 
ATOM   3418 C  CB   . THR   A 1 443 ? -2.845  -47.370 9.168  1.00 35.54 ? 446  THR   A CB   1 
ATOM   3419 O  OG1  . THR   A 1 443 ? -3.717  -46.485 8.450  1.00 36.57 ? 446  THR   A OG1  1 
ATOM   3420 C  CG2  . THR   A 1 443 ? -1.947  -48.136 8.184  1.00 35.83 ? 446  THR   A CG2  1 
ATOM   3421 N  N    . VAL   A 1 444 ? -5.780  -47.496 10.971 1.00 27.32 ? 447  VAL   A N    1 
ATOM   3422 C  CA   . VAL   A 1 444 ? -6.573  -46.789 11.972 1.00 27.16 ? 447  VAL   A CA   1 
ATOM   3423 C  C    . VAL   A 1 444 ? -6.736  -47.685 13.193 1.00 24.29 ? 447  VAL   A C    1 
ATOM   3424 O  O    . VAL   A 1 444 ? -7.275  -48.793 13.096 1.00 25.43 ? 447  VAL   A O    1 
ATOM   3425 C  CB   . VAL   A 1 444 ? -7.936  -46.373 11.405 1.00 27.21 ? 447  VAL   A CB   1 
ATOM   3426 C  CG1  . VAL   A 1 444 ? -8.787  -45.759 12.505 1.00 23.28 ? 447  VAL   A CG1  1 
ATOM   3427 C  CG2  . VAL   A 1 444 ? -7.752  -45.391 10.241 1.00 25.61 ? 447  VAL   A CG2  1 
ATOM   3428 N  N    . ILE   A 1 445 ? -6.279  -47.208 14.348 1.00 24.95 ? 448  ILE   A N    1 
ATOM   3429 C  CA   . ILE   A 1 445 ? -6.279  -47.995 15.577 1.00 22.77 ? 448  ILE   A CA   1 
ATOM   3430 C  C    . ILE   A 1 445 ? -6.861  -47.148 16.711 1.00 25.38 ? 448  ILE   A C    1 
ATOM   3431 O  O    . ILE   A 1 445 ? -6.474  -45.987 16.895 1.00 21.40 ? 448  ILE   A O    1 
ATOM   3432 C  CB   . ILE   A 1 445 ? -4.862  -48.495 15.918 1.00 24.01 ? 448  ILE   A CB   1 
ATOM   3433 C  CG1  . ILE   A 1 445 ? -4.868  -49.254 17.245 1.00 26.18 ? 448  ILE   A CG1  1 
ATOM   3434 C  CG2  . ILE   A 1 445 ? -3.866  -47.339 15.940 1.00 28.88 ? 448  ILE   A CG2  1 
ATOM   3435 C  CD1  . ILE   A 1 445 ? -3.637  -50.080 17.479 1.00 29.14 ? 448  ILE   A CD1  1 
ATOM   3436 N  N    . GLY   A 1 446 ? -7.802  -47.716 17.457 1.00 21.85 ? 449  GLY   A N    1 
ATOM   3437 C  CA   . GLY   A 1 446 ? -8.481  -46.905 18.453 1.00 20.57 ? 449  GLY   A CA   1 
ATOM   3438 C  C    . GLY   A 1 446 ? -9.345  -45.822 17.840 1.00 17.03 ? 449  GLY   A C    1 
ATOM   3439 O  O    . GLY   A 1 446 ? -9.348  -44.683 18.327 1.00 19.10 ? 449  GLY   A O    1 
ATOM   3440 N  N    . ASP   A 1 447 ? -10.057 -46.146 16.763 1.00 18.87 ? 450  ASP   A N    1 
ATOM   3441 C  CA   . ASP   A 1 447 ? -11.065 -45.262 16.191 1.00 19.24 ? 450  ASP   A CA   1 
ATOM   3442 C  C    . ASP   A 1 447 ? -12.196 -45.048 17.194 1.00 18.05 ? 450  ASP   A C    1 
ATOM   3443 O  O    . ASP   A 1 447 ? -12.364 -45.806 18.160 1.00 16.46 ? 450  ASP   A O    1 
ATOM   3444 C  CB   . ASP   A 1 447 ? -11.609 -45.861 14.889 1.00 19.49 ? 450  ASP   A CB   1 
ATOM   3445 C  CG   . ASP   A 1 447 ? -12.284 -44.839 13.978 1.00 20.60 ? 450  ASP   A CG   1 
ATOM   3446 O  OD1  . ASP   A 1 447 ? -12.213 -43.606 14.230 1.00 21.34 ? 450  ASP   A OD1  1 
ATOM   3447 O  OD2  . ASP   A 1 447 ? -12.894 -45.279 12.974 1.00 19.67 ? 450  ASP   A OD2  1 
ATOM   3448 N  N    . HIS   A 1 448 ? -12.952 -43.972 16.977 1.00 17.59 ? 451  HIS   A N    1 
ATOM   3449 C  CA   . HIS   A 1 448 ? -14.178 -43.749 17.735 1.00 16.87 ? 451  HIS   A CA   1 
ATOM   3450 C  C    . HIS   A 1 448 ? -15.042 -45.003 17.715 1.00 16.02 ? 451  HIS   A C    1 
ATOM   3451 O  O    . HIS   A 1 448 ? -15.316 -45.565 16.653 1.00 17.41 ? 451  HIS   A O    1 
ATOM   3452 C  CB   . HIS   A 1 448 ? -14.942 -42.568 17.136 1.00 18.74 ? 451  HIS   A CB   1 
ATOM   3453 C  CG   . HIS   A 1 448 ? -15.997 -41.992 18.031 1.00 16.80 ? 451  HIS   A CG   1 
ATOM   3454 N  ND1  . HIS   A 1 448 ? -15.702 -41.379 19.231 1.00 18.86 ? 451  HIS   A ND1  1 
ATOM   3455 C  CD2  . HIS   A 1 448 ? -17.334 -41.862 17.860 1.00 23.66 ? 451  HIS   A CD2  1 
ATOM   3456 C  CE1  . HIS   A 1 448 ? -16.817 -40.921 19.776 1.00 19.98 ? 451  HIS   A CE1  1 
ATOM   3457 N  NE2  . HIS   A 1 448 ? -17.819 -41.197 18.962 1.00 20.01 ? 451  HIS   A NE2  1 
ATOM   3458 N  N    . GLY   A 1 449 ? -15.444 -45.451 18.902 1.00 13.26 ? 452  GLY   A N    1 
ATOM   3459 C  CA   . GLY   A 1 449 ? -16.310 -46.608 19.042 1.00 15.25 ? 452  GLY   A CA   1 
ATOM   3460 C  C    . GLY   A 1 449 ? -15.600 -47.943 19.173 1.00 18.71 ? 452  GLY   A C    1 
ATOM   3461 O  O    . GLY   A 1 449 ? -16.266 -48.959 19.422 1.00 16.52 ? 452  GLY   A O    1 
ATOM   3462 N  N    . ASP   A 1 450 ? -14.271 -47.981 19.016 1.00 15.45 ? 453  ASP   A N    1 
ATOM   3463 C  CA   . ASP   A 1 450 ? -13.580 -49.268 19.003 1.00 14.62 ? 453  ASP   A CA   1 
ATOM   3464 C  C    . ASP   A 1 450 ? -13.655 -49.977 20.352 1.00 17.27 ? 453  ASP   A C    1 
ATOM   3465 O  O    . ASP   A 1 450 ? -13.590 -51.215 20.397 1.00 18.10 ? 453  ASP   A O    1 
ATOM   3466 C  CB   . ASP   A 1 450 ? -12.106 -49.107 18.582 1.00 15.84 ? 453  ASP   A CB   1 
ATOM   3467 C  CG   . ASP   A 1 450 ? -11.916 -49.046 17.053 1.00 23.34 ? 453  ASP   A CG   1 
ATOM   3468 O  OD1  . ASP   A 1 450 ? -12.910 -49.226 16.314 1.00 21.39 ? 453  ASP   A OD1  1 
ATOM   3469 O  OD2  . ASP   A 1 450 ? -10.765 -48.820 16.586 1.00 22.66 ? 453  ASP   A OD2  1 
ATOM   3470 N  N    . GLU   A 1 451 ? -13.794 -49.234 21.455 1.00 14.00 ? 454  GLU   A N    1 
ATOM   3471 C  CA   . GLU   A 1 451 ? -13.847 -49.916 22.738 1.00 15.57 ? 454  GLU   A CA   1 
ATOM   3472 C  C    . GLU   A 1 451 ? -15.181 -50.635 22.959 1.00 15.41 ? 454  GLU   A C    1 
ATOM   3473 O  O    . GLU   A 1 451 ? -15.259 -51.511 23.825 1.00 13.87 ? 454  GLU   A O    1 
ATOM   3474 C  CB   . GLU   A 1 451 ? -13.581 -48.950 23.907 1.00 13.45 ? 454  GLU   A CB   1 
ATOM   3475 C  CG   . GLU   A 1 451 ? -14.790 -48.114 24.400 1.00 18.27 ? 454  GLU   A CG   1 
ATOM   3476 C  CD   . GLU   A 1 451 ? -15.435 -47.125 23.424 1.00 19.36 ? 454  GLU   A CD   1 
ATOM   3477 O  OE1  . GLU   A 1 451 ? -15.112 -47.044 22.206 1.00 19.87 ? 454  GLU   A OE1  1 
ATOM   3478 O  OE2  . GLU   A 1 451 ? -16.419 -46.498 23.886 1.00 22.00 ? 454  GLU   A OE2  1 
ATOM   3479 N  N    . LEU   A 1 452 ? -16.225 -50.275 22.203 1.00 16.55 ? 455  LEU   A N    1 
ATOM   3480 C  CA   . LEU   A 1 452 ? -17.552 -50.845 22.420 1.00 13.32 ? 455  LEU   A CA   1 
ATOM   3481 C  C    . LEU   A 1 452 ? -17.511 -52.363 22.333 1.00 15.69 ? 455  LEU   A C    1 
ATOM   3482 O  O    . LEU   A 1 452 ? -18.119 -53.065 23.155 1.00 16.64 ? 455  LEU   A O    1 
ATOM   3483 C  CB   . LEU   A 1 452 ? -18.521 -50.303 21.370 1.00 14.40 ? 455  LEU   A CB   1 
ATOM   3484 C  CG   . LEU   A 1 452 ? -18.880 -48.814 21.511 1.00 15.51 ? 455  LEU   A CG   1 
ATOM   3485 C  CD1  . LEU   A 1 452 ? -19.775 -48.398 20.364 1.00 17.01 ? 455  LEU   A CD1  1 
ATOM   3486 C  CD2  . LEU   A 1 452 ? -19.551 -48.565 22.835 1.00 15.10 ? 455  LEU   A CD2  1 
ATOM   3487 N  N    . PHE   A 1 453 ? -16.776 -52.877 21.341 1.00 15.34 ? 456  PHE   A N    1 
ATOM   3488 C  CA   . PHE   A 1 453 ? -16.673 -54.314 21.122 1.00 15.68 ? 456  PHE   A CA   1 
ATOM   3489 C  C    . PHE   A 1 453 ? -16.090 -55.024 22.334 1.00 15.95 ? 456  PHE   A C    1 
ATOM   3490 O  O    . PHE   A 1 453 ? -16.481 -56.163 22.632 1.00 16.20 ? 456  PHE   A O    1 
ATOM   3491 C  CB   . PHE   A 1 453 ? -15.839 -54.556 19.861 1.00 17.69 ? 456  PHE   A CB   1 
ATOM   3492 C  CG   . PHE   A 1 453 ? -16.454 -53.959 18.619 1.00 16.37 ? 456  PHE   A CG   1 
ATOM   3493 C  CD1  . PHE   A 1 453 ? -17.582 -54.525 18.044 1.00 20.02 ? 456  PHE   A CD1  1 
ATOM   3494 C  CD2  . PHE   A 1 453 ? -15.966 -52.770 18.089 1.00 21.52 ? 456  PHE   A CD2  1 
ATOM   3495 C  CE1  . PHE   A 1 453 ? -18.174 -53.964 16.915 1.00 19.06 ? 456  PHE   A CE1  1 
ATOM   3496 C  CE2  . PHE   A 1 453 ? -16.554 -52.194 16.957 1.00 24.18 ? 456  PHE   A CE2  1 
ATOM   3497 C  CZ   . PHE   A 1 453 ? -17.671 -52.794 16.377 1.00 23.48 ? 456  PHE   A CZ   1 
ATOM   3498 N  N    . SER   A 1 454 ? -15.164 -54.379 23.053 1.00 15.18 ? 457  SER   A N    1 
ATOM   3499 C  CA   . SER   A 1 454 ? -14.654 -54.987 24.277 1.00 15.27 ? 457  SER   A CA   1 
ATOM   3500 C  C    . SER   A 1 454 ? -15.649 -54.838 25.427 1.00 14.65 ? 457  SER   A C    1 
ATOM   3501 O  O    . SER   A 1 454 ? -15.889 -55.798 26.176 1.00 13.75 ? 457  SER   A O    1 
ATOM   3502 C  CB   . SER   A 1 454 ? -13.296 -54.376 24.664 1.00 14.96 ? 457  SER   A CB   1 
ATOM   3503 O  OG   . SER   A 1 454 ? -12.310 -54.555 23.648 1.00 16.41 ? 457  SER   A OG   1 
ATOM   3504 N  N    . VAL   A 1 455 ? -16.263 -53.656 25.554 1.00 13.65 ? 458  VAL   A N    1 
ATOM   3505 C  CA   . VAL   A 1 455 ? -17.143 -53.384 26.693 1.00 14.40 ? 458  VAL   A CA   1 
ATOM   3506 C  C    . VAL   A 1 455 ? -18.343 -54.317 26.658 1.00 12.80 ? 458  VAL   A C    1 
ATOM   3507 O  O    . VAL   A 1 455 ? -18.791 -54.822 27.690 1.00 12.96 ? 458  VAL   A O    1 
ATOM   3508 C  CB   . VAL   A 1 455 ? -17.573 -51.894 26.692 1.00 12.30 ? 458  VAL   A CB   1 
ATOM   3509 C  CG1  . VAL   A 1 455 ? -18.771 -51.623 27.641 1.00 12.93 ? 458  VAL   A CG1  1 
ATOM   3510 C  CG2  . VAL   A 1 455 ? -16.396 -50.990 27.053 1.00 13.10 ? 458  VAL   A CG2  1 
ATOM   3511 N  N    . PHE   A 1 456 ? -18.859 -54.590 25.465 1.00 9.89  ? 459  PHE   A N    1 
ATOM   3512 C  CA   . PHE   A 1 456 ? -20.084 -55.356 25.310 1.00 15.30 ? 459  PHE   A CA   1 
ATOM   3513 C  C    . PHE   A 1 456 ? -19.814 -56.801 24.899 1.00 15.13 ? 459  PHE   A C    1 
ATOM   3514 O  O    . PHE   A 1 456 ? -20.751 -57.531 24.557 1.00 14.33 ? 459  PHE   A O    1 
ATOM   3515 C  CB   . PHE   A 1 456 ? -21.002 -54.643 24.316 1.00 14.20 ? 459  PHE   A CB   1 
ATOM   3516 C  CG   . PHE   A 1 456 ? -21.842 -53.547 24.955 1.00 12.30 ? 459  PHE   A CG   1 
ATOM   3517 C  CD1  . PHE   A 1 456 ? -22.975 -53.866 25.692 1.00 17.92 ? 459  PHE   A CD1  1 
ATOM   3518 C  CD2  . PHE   A 1 456 ? -21.453 -52.221 24.876 1.00 14.07 ? 459  PHE   A CD2  1 
ATOM   3519 C  CE1  . PHE   A 1 456 ? -23.746 -52.865 26.301 1.00 15.53 ? 459  PHE   A CE1  1 
ATOM   3520 C  CE2  . PHE   A 1 456 ? -22.195 -51.203 25.489 1.00 14.69 ? 459  PHE   A CE2  1 
ATOM   3521 C  CZ   . PHE   A 1 456 ? -23.353 -51.532 26.199 1.00 15.49 ? 459  PHE   A CZ   1 
ATOM   3522 N  N    . GLY   A 1 457 ? -18.559 -57.235 24.943 1.00 12.94 ? 460  GLY   A N    1 
ATOM   3523 C  CA   . GLY   A 1 457 ? -18.272 -58.661 24.790 1.00 12.41 ? 460  GLY   A CA   1 
ATOM   3524 C  C    . GLY   A 1 457 ? -18.567 -59.217 23.421 1.00 15.95 ? 460  GLY   A C    1 
ATOM   3525 O  O    . GLY   A 1 457 ? -18.969 -60.385 23.297 1.00 17.54 ? 460  GLY   A O    1 
ATOM   3526 N  N    . ALA   A 1 458 ? -18.381 -58.407 22.385 1.00 11.70 ? 461  ALA   A N    1 
ATOM   3527 C  CA   . ALA   A 1 458 ? -18.565 -58.879 21.016 1.00 15.48 ? 461  ALA   A CA   1 
ATOM   3528 C  C    . ALA   A 1 458 ? -17.788 -60.153 20.693 1.00 15.67 ? 461  ALA   A C    1 
ATOM   3529 O  O    . ALA   A 1 458 ? -18.293 -60.952 19.889 1.00 17.58 ? 461  ALA   A O    1 
ATOM   3530 C  CB   . ALA   A 1 458 ? -18.185 -57.756 20.040 1.00 15.01 ? 461  ALA   A CB   1 
ATOM   3531 N  N    . PRO   A 1 459 ? -16.573 -60.385 21.214 1.00 15.69 ? 462  PRO   A N    1 
ATOM   3532 C  CA   . PRO   A 1 459 ? -15.873 -61.651 20.901 1.00 16.99 ? 462  PRO   A CA   1 
ATOM   3533 C  C    . PRO   A 1 459 ? -16.611 -62.896 21.344 1.00 21.07 ? 462  PRO   A C    1 
ATOM   3534 O  O    . PRO   A 1 459 ? -16.284 -63.996 20.870 1.00 20.86 ? 462  PRO   A O    1 
ATOM   3535 C  CB   . PRO   A 1 459 ? -14.541 -61.503 21.645 1.00 16.37 ? 462  PRO   A CB   1 
ATOM   3536 C  CG   . PRO   A 1 459 ? -14.276 -60.045 21.618 1.00 18.36 ? 462  PRO   A CG   1 
ATOM   3537 C  CD   . PRO   A 1 459 ? -15.653 -59.422 21.850 1.00 15.84 ? 462  PRO   A CD   1 
ATOM   3538 N  N    . PHE   A 1 460 ? -17.592 -62.767 22.236 1.00 17.05 ? 463  PHE   A N    1 
ATOM   3539 C  CA   . PHE   A 1 460 ? -18.392 -63.885 22.706 1.00 20.75 ? 463  PHE   A CA   1 
ATOM   3540 C  C    . PHE   A 1 460 ? -19.705 -64.029 21.960 1.00 21.80 ? 463  PHE   A C    1 
ATOM   3541 O  O    . PHE   A 1 460 ? -20.436 -64.993 22.209 1.00 21.68 ? 463  PHE   A O    1 
ATOM   3542 C  CB   . PHE   A 1 460 ? -18.643 -63.731 24.206 1.00 19.39 ? 463  PHE   A CB   1 
ATOM   3543 C  CG   . PHE   A 1 460 ? -17.389 -63.598 24.980 1.00 20.06 ? 463  PHE   A CG   1 
ATOM   3544 C  CD1  . PHE   A 1 460 ? -16.548 -64.703 25.140 1.00 20.15 ? 463  PHE   A CD1  1 
ATOM   3545 C  CD2  . PHE   A 1 460 ? -16.973 -62.359 25.441 1.00 17.79 ? 463  PHE   A CD2  1 
ATOM   3546 C  CE1  . PHE   A 1 460 ? -15.347 -64.587 25.822 1.00 21.88 ? 463  PHE   A CE1  1 
ATOM   3547 C  CE2  . PHE   A 1 460 ? -15.763 -62.221 26.119 1.00 18.81 ? 463  PHE   A CE2  1 
ATOM   3548 C  CZ   . PHE   A 1 460 ? -14.947 -63.346 26.312 1.00 21.21 ? 463  PHE   A CZ   1 
ATOM   3549 N  N    . LEU   A 1 461 ? -20.011 -63.107 21.044 1.00 21.57 ? 464  LEU   A N    1 
ATOM   3550 C  CA   . LEU   A 1 461 ? -21.251 -63.102 20.283 1.00 19.97 ? 464  LEU   A CA   1 
ATOM   3551 C  C    . LEU   A 1 461 ? -21.031 -63.125 18.775 1.00 23.03 ? 464  LEU   A C    1 
ATOM   3552 O  O    . LEU   A 1 461 ? -21.763 -63.808 18.063 1.00 29.03 ? 464  LEU   A O    1 
ATOM   3553 C  CB   . LEU   A 1 461 ? -22.092 -61.860 20.667 1.00 19.51 ? 464  LEU   A CB   1 
ATOM   3554 C  CG   . LEU   A 1 461 ? -22.476 -61.757 22.143 1.00 20.85 ? 464  LEU   A CG   1 
ATOM   3555 C  CD1  . LEU   A 1 461 ? -23.196 -60.439 22.409 1.00 21.31 ? 464  LEU   A CD1  1 
ATOM   3556 C  CD2  . LEU   A 1 461 ? -23.353 -62.934 22.543 1.00 22.09 ? 464  LEU   A CD2  1 
ATOM   3557 N  N    . LYS   A 1 462 ? -20.057 -62.381 18.261 1.00 21.25 ? 465  LYS   A N    1 
ATOM   3558 C  CA   . LYS   A 1 462 ? -19.721 -62.400 16.843 1.00 24.75 ? 465  LYS   A CA   1 
ATOM   3559 C  C    . LYS   A 1 462 ? -18.635 -63.444 16.593 1.00 29.14 ? 465  LYS   A C    1 
ATOM   3560 O  O    . LYS   A 1 462 ? -17.965 -63.895 17.518 1.00 25.57 ? 465  LYS   A O    1 
ATOM   3561 C  CB   . LYS   A 1 462 ? -19.224 -61.032 16.377 1.00 30.47 ? 465  LYS   A CB   1 
ATOM   3562 C  CG   . LYS   A 1 462 ? -20.091 -59.890 16.834 1.00 25.87 ? 465  LYS   A CG   1 
ATOM   3563 C  CD   . LYS   A 1 462 ? -19.563 -58.552 16.350 1.00 31.75 ? 465  LYS   A CD   1 
ATOM   3564 C  CE   . LYS   A 1 462 ? -20.228 -58.192 15.044 1.00 36.85 ? 465  LYS   A CE   1 
ATOM   3565 N  NZ   . LYS   A 1 462 ? -20.346 -56.740 14.871 1.00 34.70 ? 465  LYS   A NZ   1 
ATOM   3566 N  N    . GLU   A 1 463 ? -18.435 -63.792 15.323 1.00 29.35 ? 466  GLU   A N    1 
ATOM   3567 C  CA   . GLU   A 1 463 ? -17.435 -64.788 14.952 1.00 37.60 ? 466  GLU   A CA   1 
ATOM   3568 C  C    . GLU   A 1 463 ? -16.069 -64.153 14.710 1.00 36.97 ? 466  GLU   A C    1 
ATOM   3569 O  O    . GLU   A 1 463 ? -15.961 -62.990 14.306 1.00 32.44 ? 466  GLU   A O    1 
ATOM   3570 C  CB   . GLU   A 1 463 ? -17.856 -65.547 13.693 1.00 42.60 ? 466  GLU   A CB   1 
ATOM   3571 C  CG   . GLU   A 1 463 ? -19.059 -66.453 13.872 1.00 49.27 ? 466  GLU   A CG   1 
ATOM   3572 C  CD   . GLU   A 1 463 ? -18.659 -67.896 14.120 1.00 61.57 ? 466  GLU   A CD   1 
ATOM   3573 O  OE1  . GLU   A 1 463 ? -19.183 -68.500 15.085 1.00 64.79 ? 466  GLU   A OE1  1 
ATOM   3574 O  OE2  . GLU   A 1 463 ? -17.816 -68.421 13.356 1.00 62.40 ? 466  GLU   A OE2  1 
ATOM   3575 N  N    . GLY   A 1 464 ? -15.023 -64.937 14.970 1.00 35.89 ? 467  GLY   A N    1 
ATOM   3576 C  CA   . GLY   A 1 464 ? -13.711 -64.659 14.418 1.00 38.18 ? 467  GLY   A CA   1 
ATOM   3577 C  C    . GLY   A 1 464 ? -12.791 -63.784 15.235 1.00 35.52 ? 467  GLY   A C    1 
ATOM   3578 O  O    . GLY   A 1 464 ? -11.802 -63.278 14.686 1.00 35.02 ? 467  GLY   A O    1 
ATOM   3579 N  N    . ALA   A 1 465 ? -13.065 -63.591 16.523 1.00 28.94 ? 468  ALA   A N    1 
ATOM   3580 C  CA   . ALA   A 1 465 ? -12.143 -62.844 17.364 1.00 28.67 ? 468  ALA   A CA   1 
ATOM   3581 C  C    . ALA   A 1 465 ? -10.889 -63.663 17.622 1.00 31.97 ? 468  ALA   A C    1 
ATOM   3582 O  O    . ALA   A 1 465 ? -10.958 -64.867 17.884 1.00 29.46 ? 468  ALA   A O    1 
ATOM   3583 C  CB   . ALA   A 1 465 ? -12.794 -62.471 18.697 1.00 28.45 ? 468  ALA   A CB   1 
ATOM   3584 N  N    . SER   A 1 466 ? -9.735  -63.002 17.544 1.00 26.28 ? 469  SER   A N    1 
ATOM   3585 C  CA   . SER   A 1 466 ? -8.495  -63.639 17.938 1.00 27.95 ? 469  SER   A CA   1 
ATOM   3586 C  C    . SER   A 1 466 ? -8.517  -63.891 19.436 1.00 26.53 ? 469  SER   A C    1 
ATOM   3587 O  O    . SER   A 1 466 ? -9.382  -63.398 20.167 1.00 23.56 ? 469  SER   A O    1 
ATOM   3588 C  CB   . SER   A 1 466 ? -7.294  -62.768 17.567 1.00 27.60 ? 469  SER   A CB   1 
ATOM   3589 O  OG   . SER   A 1 466 ? -7.255  -61.578 18.346 1.00 28.05 ? 469  SER   A OG   1 
ATOM   3590 N  N    . GLU   A 1 467 ? -7.546  -64.663 19.902 1.00 24.53 ? 470  GLU   A N    1 
ATOM   3591 C  CA   . GLU   A 1 467 ? -7.485  -64.941 21.328 1.00 28.18 ? 470  GLU   A CA   1 
ATOM   3592 C  C    . GLU   A 1 467 ? -7.092  -63.707 22.140 1.00 26.05 ? 470  GLU   A C    1 
ATOM   3593 O  O    . GLU   A 1 467 ? -7.570  -63.510 23.273 1.00 26.14 ? 470  GLU   A O    1 
ATOM   3594 C  CB   . GLU   A 1 467 ? -6.537  -66.103 21.596 1.00 30.11 ? 470  GLU   A CB   1 
ATOM   3595 C  CG   . GLU   A 1 467 ? -6.442  -66.216 23.077 1.00 38.51 ? 470  GLU   A CG   1 
ATOM   3596 C  CD   . GLU   A 1 467 ? -7.798  -66.572 23.702 1.00 42.92 ? 470  GLU   A CD   1 
ATOM   3597 O  OE1  . GLU   A 1 467 ? -8.629  -67.294 23.103 1.00 49.37 ? 470  GLU   A OE1  1 
ATOM   3598 O  OE2  . GLU   A 1 467 ? -8.121  -65.947 24.724 1.00 37.46 ? 470  GLU   A OE2  1 
ATOM   3599 N  N    . GLU   A 1 468 ? -6.241  -62.854 21.568 1.00 22.36 ? 471  GLU   A N    1 
ATOM   3600 C  CA   . GLU   A 1 468 ? -5.903  -61.588 22.209 1.00 23.59 ? 471  GLU   A CA   1 
ATOM   3601 C  C    . GLU   A 1 468 ? -7.150  -60.718 22.394 1.00 17.18 ? 471  GLU   A C    1 
ATOM   3602 O  O    . GLU   A 1 468 ? -7.331  -60.085 23.438 1.00 18.62 ? 471  GLU   A O    1 
ATOM   3603 C  CB   . GLU   A 1 468 ? -4.848  -60.891 21.353 1.00 25.05 ? 471  GLU   A CB   1 
ATOM   3604 C  CG   . GLU   A 1 468 ? -4.540  -59.452 21.702 1.00 23.33 ? 471  GLU   A CG   1 
ATOM   3605 C  CD   . GLU   A 1 468 ? -3.565  -58.843 20.708 1.00 30.60 ? 471  GLU   A CD   1 
ATOM   3606 O  OE1  . GLU   A 1 468 ? -4.023  -58.291 19.678 1.00 30.85 ? 471  GLU   A OE1  1 
ATOM   3607 O  OE2  . GLU   A 1 468 ? -2.339  -58.946 20.938 1.00 31.62 ? 471  GLU   A OE2  1 
ATOM   3608 N  N    . GLU   A 1 469 ? -8.023  -60.692 21.389 1.00 19.02 ? 472  GLU   A N    1 
ATOM   3609 C  CA   . GLU   A 1 469 ? -9.229  -59.867 21.446 1.00 20.03 ? 472  GLU   A CA   1 
ATOM   3610 C  C    . GLU   A 1 469 ? -10.208 -60.380 22.503 1.00 20.20 ? 472  GLU   A C    1 
ATOM   3611 O  O    . GLU   A 1 469 ? -10.868 -59.588 23.201 1.00 17.29 ? 472  GLU   A O    1 
ATOM   3612 C  CB   . GLU   A 1 469 ? -9.865  -59.844 20.056 1.00 22.30 ? 472  GLU   A CB   1 
ATOM   3613 C  CG   . GLU   A 1 469 ? -10.725 -58.654 19.763 1.00 22.61 ? 472  GLU   A CG   1 
ATOM   3614 C  CD   . GLU   A 1 469 ? -11.105 -58.566 18.300 1.00 29.80 ? 472  GLU   A CD   1 
ATOM   3615 O  OE1  . GLU   A 1 469 ? -11.024 -59.590 17.585 1.00 26.00 ? 472  GLU   A OE1  1 
ATOM   3616 O  OE2  . GLU   A 1 469 ? -11.501 -57.465 17.862 1.00 25.63 ? 472  GLU   A OE2  1 
ATOM   3617 N  N    . ILE   A 1 470 ? -10.302 -61.706 22.650 1.00 19.62 ? 473  ILE   A N    1 
ATOM   3618 C  CA   . ILE   A 1 470 ? -11.125 -62.296 23.703 1.00 16.49 ? 473  ILE   A CA   1 
ATOM   3619 C  C    . ILE   A 1 470 ? -10.583 -61.912 25.074 1.00 18.49 ? 473  ILE   A C    1 
ATOM   3620 O  O    . ILE   A 1 470 ? -11.334 -61.497 25.968 1.00 18.14 ? 473  ILE   A O    1 
ATOM   3621 C  CB   . ILE   A 1 470 ? -11.186 -63.827 23.529 1.00 19.00 ? 473  ILE   A CB   1 
ATOM   3622 C  CG1  . ILE   A 1 470 ? -11.956 -64.199 22.271 1.00 25.00 ? 473  ILE   A CG1  1 
ATOM   3623 C  CG2  . ILE   A 1 470 ? -11.785 -64.485 24.757 1.00 23.64 ? 473  ILE   A CG2  1 
ATOM   3624 C  CD1  . ILE   A 1 470 ? -11.681 -65.608 21.797 1.00 28.99 ? 473  ILE   A CD1  1 
ATOM   3625 N  N    . ARG   A 1 471 ? -9.265  -62.060 25.268 1.00 15.93 ? 474  ARG   A N    1 
ATOM   3626 C  CA   . ARG   A 1 471 ? -8.661  -61.653 26.537 1.00 21.37 ? 474  ARG   A CA   1 
ATOM   3627 C  C    . ARG   A 1 471 ? -8.915  -60.174 26.837 1.00 18.33 ? 474  ARG   A C    1 
ATOM   3628 O  O    . ARG   A 1 471 ? -9.194  -59.790 27.988 1.00 17.81 ? 474  ARG   A O    1 
ATOM   3629 C  CB   . ARG   A 1 471 ? -7.154  -61.936 26.493 1.00 26.86 ? 474  ARG   A CB   1 
ATOM   3630 C  CG   . ARG   A 1 471 ? -6.474  -62.013 27.841 1.00 29.08 ? 474  ARG   A CG   1 
ATOM   3631 C  CD   . ARG   A 1 471 ? -5.128  -62.752 27.712 1.00 37.01 ? 474  ARG   A CD   1 
ATOM   3632 N  NE   . ARG   A 1 471 ? -4.748  -62.959 26.315 1.00 36.84 ? 474  ARG   A NE   1 
ATOM   3633 C  CZ   . ARG   A 1 471 ? -4.561  -64.147 25.745 1.00 38.93 ? 474  ARG   A CZ   1 
ATOM   3634 N  NH1  . ARG   A 1 471 ? -4.684  -65.274 26.432 1.00 45.64 ? 474  ARG   A NH1  1 
ATOM   3635 N  NH2  . ARG   A 1 471 ? -4.238  -64.205 24.452 1.00 37.65 ? 474  ARG   A NH2  1 
ATOM   3636 N  N    . LEU   A 1 472 ? -8.791  -59.324 25.818 1.00 17.15 ? 475  LEU   A N    1 
ATOM   3637 C  CA   . LEU   A 1 472 ? -9.011  -57.899 26.028 1.00 16.41 ? 475  LEU   A CA   1 
ATOM   3638 C  C    . LEU   A 1 472 ? -10.443 -57.648 26.481 1.00 16.73 ? 475  LEU   A C    1 
ATOM   3639 O  O    . LEU   A 1 472 ? -10.676 -56.875 27.419 1.00 15.58 ? 475  LEU   A O    1 
ATOM   3640 C  CB   . LEU   A 1 472 ? -8.710  -57.125 24.749 1.00 15.92 ? 475  LEU   A CB   1 
ATOM   3641 C  CG   . LEU   A 1 472 ? -8.984  -55.607 24.730 1.00 15.21 ? 475  LEU   A CG   1 
ATOM   3642 C  CD1  . LEU   A 1 472 ? -8.154  -54.897 25.779 1.00 17.58 ? 475  LEU   A CD1  1 
ATOM   3643 C  CD2  . LEU   A 1 472 ? -8.700  -55.033 23.360 1.00 17.69 ? 475  LEU   A CD2  1 
ATOM   3644 N  N    . SER   A 1 473 ? -11.413 -58.310 25.844 1.00 14.64 ? 476  SER   A N    1 
ATOM   3645 C  CA   . SER   A 1 473 ? -12.805 -58.079 26.234 1.00 15.15 ? 476  SER   A CA   1 
ATOM   3646 C  C    . SER   A 1 473 ? -13.050 -58.527 27.669 1.00 18.06 ? 476  SER   A C    1 
ATOM   3647 O  O    . SER   A 1 473 ? -13.713 -57.824 28.436 1.00 15.22 ? 476  SER   A O    1 
ATOM   3648 C  CB   . SER   A 1 473 ? -13.769 -58.776 25.281 1.00 17.59 ? 476  SER   A CB   1 
ATOM   3649 O  OG   . SER   A 1 473 ? -15.135 -58.567 25.682 1.00 15.39 ? 476  SER   A OG   1 
ATOM   3650 N  N    . LYS   A 1 474 ? -12.551 -59.715 28.056 1.00 16.79 ? 477  LYS   A N    1 
ATOM   3651 C  CA   . LYS   A 1 474 ? -12.779 -60.120 29.445 1.00 16.70 ? 477  LYS   A CA   1 
ATOM   3652 C  C    . LYS   A 1 474 ? -12.188 -59.122 30.416 1.00 16.86 ? 477  LYS   A C    1 
ATOM   3653 O  O    . LYS   A 1 474 ? -12.790 -58.827 31.460 1.00 18.96 ? 477  LYS   A O    1 
ATOM   3654 C  CB   . LYS   A 1 474 ? -12.213 -61.493 29.783 1.00 17.68 ? 477  LYS   A CB   1 
ATOM   3655 C  CG   . LYS   A 1 474 ? -12.690 -62.625 28.993 1.00 24.01 ? 477  LYS   A CG   1 
ATOM   3656 C  CD   . LYS   A 1 474 ? -12.115 -63.804 29.724 1.00 35.26 ? 477  LYS   A CD   1 
ATOM   3657 C  CE   . LYS   A 1 474 ? -11.977 -65.007 28.893 1.00 38.38 ? 477  LYS   A CE   1 
ATOM   3658 N  NZ   . LYS   A 1 474 ? -11.500 -66.051 29.835 1.00 42.09 ? 477  LYS   A NZ   1 
ATOM   3659 N  N    . MET   A 1 475 ? -11.004 -58.592 30.108 1.00 17.00 ? 478  MET   A N    1 
ATOM   3660 C  CA   . MET   A 1 475 ? -10.415 -57.665 31.058 1.00 16.32 ? 478  MET   A CA   1 
ATOM   3661 C  C    . MET   A 1 475 ? -11.222 -56.366 31.128 1.00 14.87 ? 478  MET   A C    1 
ATOM   3662 O  O    . MET   A 1 475 ? -11.439 -55.831 32.218 1.00 12.83 ? 478  MET   A O    1 
ATOM   3663 C  CB   . MET   A 1 475 ? -8.955  -57.387 30.691 1.00 16.22 ? 478  MET   A CB   1 
ATOM   3664 C  CG   . MET   A 1 475 ? -8.337  -56.307 31.504 1.00 17.29 ? 478  MET   A CG   1 
ATOM   3665 S  SD   . MET   A 1 475 ? -6.786  -55.688 30.794 1.00 23.13 ? 478  MET   A SD   1 
ATOM   3666 C  CE   . MET   A 1 475 ? -7.438  -54.698 29.440 1.00 22.39 ? 478  MET   A CE   1 
ATOM   3667 N  N    . VAL   A 1 476 ? -11.649 -55.836 29.977 1.00 12.80 ? 479  VAL   A N    1 
ATOM   3668 C  CA   . VAL   A 1 476 ? -12.395 -54.571 29.959 1.00 13.55 ? 479  VAL   A CA   1 
ATOM   3669 C  C    . VAL   A 1 476 ? -13.738 -54.748 30.660 1.00 13.33 ? 479  VAL   A C    1 
ATOM   3670 O  O    . VAL   A 1 476 ? -14.165 -53.893 31.447 1.00 14.52 ? 479  VAL   A O    1 
ATOM   3671 C  CB   . VAL   A 1 476 ? -12.591 -54.067 28.510 1.00 11.91 ? 479  VAL   A CB   1 
ATOM   3672 C  CG1  . VAL   A 1 476 ? -13.623 -52.921 28.462 1.00 13.56 ? 479  VAL   A CG1  1 
ATOM   3673 C  CG2  . VAL   A 1 476 ? -11.271 -53.557 27.929 1.00 13.87 ? 479  VAL   A CG2  1 
ATOM   3674 N  N    . MET   A 1 477 ? -14.428 -55.843 30.415 1.00 15.00 ? 480  MET   A N    1 
ATOM   3675 C  CA   . MET   A 1 477 ? -15.719 -56.074 31.039 1.00 15.39 ? 480  MET   A CA   1 
ATOM   3676 C  C    . MET   A 1 477 ? -15.534 -56.100 32.580 1.00 17.27 ? 480  MET   A C    1 
ATOM   3677 O  O    . MET   A 1 477 ? -16.289 -55.523 33.313 1.00 13.85 ? 480  MET   A O    1 
ATOM   3678 C  CB   . MET   A 1 477 ? -16.387 -57.334 30.492 1.00 14.09 ? 480  MET   A CB   1 
ATOM   3679 C  CG   . MET   A 1 477 ? -16.958 -57.209 29.090 1.00 14.22 ? 480  MET   A CG   1 
ATOM   3680 S  SD   . MET   A 1 477 ? -18.023 -58.595 28.639 1.00 18.36 ? 480  MET   A SD   1 
ATOM   3681 C  CE   . MET   A 1 477 ? -16.833 -59.925 28.630 1.00 14.89 ? 480  MET   A CE   1 
ATOM   3682 N  N    . LYS   A 1 478 ? -14.493 -56.790 33.022 1.00 14.86 ? 481  LYS   A N    1 
ATOM   3683 C  CA   . LYS   A 1 478 ? -14.238 -56.860 34.469 1.00 16.73 ? 481  LYS   A CA   1 
ATOM   3684 C  C    . LYS   A 1 478 ? -13.920 -55.535 35.097 1.00 14.32 ? 481  LYS   A C    1 
ATOM   3685 O  O    . LYS   A 1 478 ? -14.360 -55.265 36.181 1.00 16.33 ? 481  LYS   A O    1 
ATOM   3686 C  CB   . LYS   A 1 478 ? -13.136 -57.875 34.813 1.00 16.56 ? 481  LYS   A CB   1 
ATOM   3687 C  CG   . LYS   A 1 478 ? -13.234 -58.426 36.219 1.00 19.08 ? 481  LYS   A CG   1 
ATOM   3688 C  CD   . LYS   A 1 478 ? -12.221 -59.528 36.465 1.00 26.29 ? 481  LYS   A CD   1 
ATOM   3689 C  CE   . LYS   A 1 478 ? -12.548 -60.776 35.676 1.00 29.72 ? 481  LYS   A CE   1 
ATOM   3690 N  NZ   . LYS   A 1 478 ? -13.872 -61.341 36.049 1.00 29.26 ? 481  LYS   A NZ   1 
ATOM   3691 N  N    . PHE   A 1 479 ? -13.123 -54.719 34.432 1.00 14.52 ? 482  PHE   A N    1 
ATOM   3692 C  CA   . PHE   A 1 479 ? -12.855 -53.410 34.935 1.00 14.17 ? 482  PHE   A CA   1 
ATOM   3693 C  C    . PHE   A 1 479 ? -14.167 -52.635 35.046 1.00 13.54 ? 482  PHE   A C    1 
ATOM   3694 O  O    . PHE   A 1 479 ? -14.419 -51.995 36.028 1.00 13.43 ? 482  PHE   A O    1 
ATOM   3695 C  CB   . PHE   A 1 479 ? -11.938 -52.641 34.003 1.00 10.69 ? 482  PHE   A CB   1 
ATOM   3696 C  CG   . PHE   A 1 479 ? -10.472 -52.878 34.228 1.00 15.08 ? 482  PHE   A CG   1 
ATOM   3697 C  CD1  . PHE   A 1 479 ? -9.938  -52.864 35.495 1.00 14.07 ? 482  PHE   A CD1  1 
ATOM   3698 C  CD2  . PHE   A 1 479 ? -9.622  -53.059 33.160 1.00 15.52 ? 482  PHE   A CD2  1 
ATOM   3699 C  CE1  . PHE   A 1 479 ? -8.589  -53.052 35.698 1.00 21.02 ? 482  PHE   A CE1  1 
ATOM   3700 C  CE2  . PHE   A 1 479 ? -8.269  -53.246 33.352 1.00 16.31 ? 482  PHE   A CE2  1 
ATOM   3701 C  CZ   . PHE   A 1 479 ? -7.751  -53.246 34.624 1.00 16.39 ? 482  PHE   A CZ   1 
ATOM   3702 N  N    . TRP   A 1 480 ? -14.952 -52.688 33.991 1.00 12.48 ? 483  TRP   A N    1 
ATOM   3703 C  CA   . TRP   A 1 480 ? -16.192 -51.902 33.993 1.00 16.27 ? 483  TRP   A CA   1 
ATOM   3704 C  C    . TRP   A 1 480 ? -17.125 -52.355 35.113 1.00 13.24 ? 483  TRP   A C    1 
ATOM   3705 O  O    . TRP   A 1 480 ? -17.681 -51.532 35.855 1.00 17.23 ? 483  TRP   A O    1 
ATOM   3706 C  CB   . TRP   A 1 480 ? -16.890 -52.022 32.634 1.00 12.34 ? 483  TRP   A CB   1 
ATOM   3707 C  CG   . TRP   A 1 480 ? -16.644 -50.891 31.641 1.00 14.75 ? 483  TRP   A CG   1 
ATOM   3708 C  CD1  . TRP   A 1 480 ? -17.606 -50.190 30.964 1.00 14.03 ? 483  TRP   A CD1  1 
ATOM   3709 C  CD2  . TRP   A 1 480 ? -15.375 -50.351 31.205 1.00 15.00 ? 483  TRP   A CD2  1 
ATOM   3710 N  NE1  . TRP   A 1 480 ? -17.025 -49.250 30.144 1.00 12.72 ? 483  TRP   A NE1  1 
ATOM   3711 C  CE2  . TRP   A 1 480 ? -15.659 -49.330 30.267 1.00 16.49 ? 483  TRP   A CE2  1 
ATOM   3712 C  CE3  . TRP   A 1 480 ? -14.036 -50.640 31.505 1.00 15.76 ? 483  TRP   A CE3  1 
ATOM   3713 C  CZ2  . TRP   A 1 480 ? -14.655 -48.589 29.631 1.00 15.39 ? 483  TRP   A CZ2  1 
ATOM   3714 C  CZ3  . TRP   A 1 480 ? -13.024 -49.899 30.865 1.00 16.42 ? 483  TRP   A CZ3  1 
ATOM   3715 C  CH2  . TRP   A 1 480 ? -13.346 -48.888 29.939 1.00 13.88 ? 483  TRP   A CH2  1 
ATOM   3716 N  N    . ALA   A 1 481 ? -17.298 -53.668 35.263 1.00 12.76 ? 484  ALA   A N    1 
ATOM   3717 C  CA   . ALA   A 1 481 ? -18.216 -54.175 36.280 1.00 13.28 ? 484  ALA   A CA   1 
ATOM   3718 C  C    . ALA   A 1 481 ? -17.642 -54.065 37.682 1.00 15.50 ? 484  ALA   A C    1 
ATOM   3719 O  O    . ALA   A 1 481 ? -18.398 -53.902 38.636 1.00 14.10 ? 484  ALA   A O    1 
ATOM   3720 C  CB   . ALA   A 1 481 ? -18.602 -55.625 35.970 1.00 11.44 ? 484  ALA   A CB   1 
ATOM   3721 N  N    . ASN   A 1 482 ? -16.316 -54.151 37.851 1.00 15.37 ? 485  ASN   A N    1 
ATOM   3722 C  CA   . ASN   A 1 482 ? -15.724 -53.798 39.137 1.00 13.62 ? 485  ASN   A CA   1 
ATOM   3723 C  C    . ASN   A 1 482 ? -16.025 -52.349 39.482 1.00 15.14 ? 485  ASN   A C    1 
ATOM   3724 O  O    . ASN   A 1 482 ? -16.290 -52.017 40.644 1.00 17.86 ? 485  ASN   A O    1 
ATOM   3725 C  CB   . ASN   A 1 482 ? -14.200 -53.999 39.104 1.00 15.82 ? 485  ASN   A CB   1 
ATOM   3726 C  CG   . ASN   A 1 482 ? -13.788 -55.462 39.177 1.00 20.82 ? 485  ASN   A CG   1 
ATOM   3727 O  OD1  . ASN   A 1 482 ? -14.610 -56.342 39.438 1.00 17.48 ? 485  ASN   A OD1  1 
ATOM   3728 N  ND2  . ASN   A 1 482 ? -12.493 -55.729 38.929 1.00 19.27 ? 485  ASN   A ND2  1 
ATOM   3729 N  N    . PHE   A 1 483 ? -15.936 -51.458 38.494 1.00 13.70 ? 486  PHE   A N    1 
ATOM   3730 C  CA   . PHE   A 1 483 ? -16.262 -50.061 38.748 1.00 13.22 ? 486  PHE   A CA   1 
ATOM   3731 C  C    . PHE   A 1 483 ? -17.732 -49.906 39.138 1.00 14.86 ? 486  PHE   A C    1 
ATOM   3732 O  O    . PHE   A 1 483 ? -18.063 -49.140 40.049 1.00 14.68 ? 486  PHE   A O    1 
ATOM   3733 C  CB   . PHE   A 1 483 ? -15.938 -49.228 37.511 1.00 14.63 ? 486  PHE   A CB   1 
ATOM   3734 C  CG   . PHE   A 1 483 ? -16.068 -47.754 37.727 1.00 16.33 ? 486  PHE   A CG   1 
ATOM   3735 C  CD1  . PHE   A 1 483 ? -15.149 -47.071 38.505 1.00 13.51 ? 486  PHE   A CD1  1 
ATOM   3736 C  CD2  . PHE   A 1 483 ? -17.124 -47.044 37.140 1.00 16.74 ? 486  PHE   A CD2  1 
ATOM   3737 C  CE1  . PHE   A 1 483 ? -15.265 -45.683 38.698 1.00 17.70 ? 486  PHE   A CE1  1 
ATOM   3738 C  CE2  . PHE   A 1 483 ? -17.254 -45.664 37.321 1.00 13.43 ? 486  PHE   A CE2  1 
ATOM   3739 C  CZ   . PHE   A 1 483 ? -16.328 -44.982 38.099 1.00 14.71 ? 486  PHE   A CZ   1 
ATOM   3740 N  N    . ALA   A 1 484 ? -18.619 -50.649 38.473 1.00 15.55 ? 487  ALA   A N    1 
ATOM   3741 C  CA   . ALA   A 1 484 ? -20.038 -50.616 38.843 1.00 14.27 ? 487  ALA   A CA   1 
ATOM   3742 C  C    . ALA   A 1 484 ? -20.241 -51.117 40.268 1.00 17.78 ? 487  ALA   A C    1 
ATOM   3743 O  O    . ALA   A 1 484 ? -20.981 -50.510 41.047 1.00 19.47 ? 487  ALA   A O    1 
ATOM   3744 C  CB   . ALA   A 1 484 ? -20.869 -51.444 37.868 1.00 13.73 ? 487  ALA   A CB   1 
ATOM   3745 N  N    . ARG   A 1 485 ? -19.557 -52.206 40.639 1.00 17.45 ? 488  ARG   A N    1 
ATOM   3746 C  CA   . ARG   A 1 485 ? -19.676 -52.736 41.996 1.00 19.53 ? 488  ARG   A CA   1 
ATOM   3747 C  C    . ARG   A 1 485 ? -19.146 -51.758 43.039 1.00 22.46 ? 488  ARG   A C    1 
ATOM   3748 O  O    . ARG   A 1 485 ? -19.820 -51.483 44.036 1.00 21.42 ? 488  ARG   A O    1 
ATOM   3749 C  CB   . ARG   A 1 485 ? -18.961 -54.087 42.108 1.00 18.78 ? 488  ARG   A CB   1 
ATOM   3750 C  CG   . ARG   A 1 485 ? -19.734 -55.237 41.469 1.00 20.48 ? 488  ARG   A CG   1 
ATOM   3751 C  CD   . ARG   A 1 485 ? -19.038 -56.586 41.602 1.00 18.79 ? 488  ARG   A CD   1 
ATOM   3752 N  NE   . ARG   A 1 485 ? -17.990 -56.729 40.601 1.00 18.15 ? 488  ARG   A NE   1 
ATOM   3753 C  CZ   . ARG   A 1 485 ? -18.168 -57.326 39.434 1.00 20.54 ? 488  ARG   A CZ   1 
ATOM   3754 N  NH1  . ARG   A 1 485 ? -19.354 -57.800 39.075 1.00 17.60 ? 488  ARG   A NH1  1 
ATOM   3755 N  NH2  . ARG   A 1 485 ? -17.142 -57.433 38.598 1.00 17.98 ? 488  ARG   A NH2  1 
ATOM   3756 N  N    . ASN   A 1 486 ? -17.938 -51.209 42.824 1.00 18.00 ? 489  ASN   A N    1 
ATOM   3757 C  CA   . ASN   A 1 486 ? -17.155 -50.580 43.883 1.00 19.80 ? 489  ASN   A CA   1 
ATOM   3758 C  C    . ASN   A 1 486 ? -16.750 -49.140 43.639 1.00 21.36 ? 489  ASN   A C    1 
ATOM   3759 O  O    . ASN   A 1 486 ? -16.158 -48.539 44.541 1.00 21.72 ? 489  ASN   A O    1 
ATOM   3760 C  CB   . ASN   A 1 486 ? -15.857 -51.375 44.137 1.00 21.40 ? 489  ASN   A CB   1 
ATOM   3761 C  CG   . ASN   A 1 486 ? -16.128 -52.818 44.435 1.00 26.75 ? 489  ASN   A CG   1 
ATOM   3762 O  OD1  . ASN   A 1 486 ? -17.071 -53.127 45.164 1.00 28.23 ? 489  ASN   A OD1  1 
ATOM   3763 N  ND2  . ASN   A 1 486 ? -15.324 -53.720 43.867 1.00 26.80 ? 489  ASN   A ND2  1 
ATOM   3764 N  N    . GLY   A 1 487 ? -17.015 -48.568 42.466 1.00 15.61 ? 490  GLY   A N    1 
ATOM   3765 C  CA   . GLY   A 1 487 ? -16.503 -47.232 42.221 1.00 16.58 ? 490  GLY   A CA   1 
ATOM   3766 C  C    . GLY   A 1 487 ? -14.999 -47.181 42.058 1.00 17.77 ? 490  GLY   A C    1 
ATOM   3767 O  O    . GLY   A 1 487 ? -14.397 -46.112 42.207 1.00 18.65 ? 490  GLY   A O    1 
ATOM   3768 N  N    . ASN   A 1 488 ? -14.388 -48.323 41.763 1.00 18.26 ? 491  ASN   A N    1 
ATOM   3769 C  CA   . ASN   A 1 488 ? -12.950 -48.557 41.633 1.00 21.24 ? 491  ASN   A CA   1 
ATOM   3770 C  C    . ASN   A 1 488 ? -12.828 -49.769 40.720 1.00 16.89 ? 491  ASN   A C    1 
ATOM   3771 O  O    . ASN   A 1 488 ? -13.370 -50.832 41.041 1.00 17.58 ? 491  ASN   A O    1 
ATOM   3772 C  CB   . ASN   A 1 488 ? -12.308 -48.793 43.008 1.00 19.29 ? 491  ASN   A CB   1 
ATOM   3773 C  CG   . ASN   A 1 488 ? -10.796 -49.014 42.943 1.00 22.92 ? 491  ASN   A CG   1 
ATOM   3774 O  OD1  . ASN   A 1 488 ? -10.262 -49.493 41.938 1.00 20.29 ? 491  ASN   A OD1  1 
ATOM   3775 N  ND2  . ASN   A 1 488 ? -10.105 -48.665 44.025 1.00 20.26 ? 491  ASN   A ND2  1 
ATOM   3776 N  N    . PRO   A 1 489 ? -12.173 -49.650 39.558 1.00 17.14 ? 492  PRO   A N    1 
ATOM   3777 C  CA   . PRO   A 1 489 ? -12.150 -50.778 38.613 1.00 16.03 ? 492  PRO   A CA   1 
ATOM   3778 C  C    . PRO   A 1 489 ? -11.214 -51.925 39.012 1.00 18.97 ? 492  PRO   A C    1 
ATOM   3779 O  O    . PRO   A 1 489 ? -11.254 -52.976 38.362 1.00 18.90 ? 492  PRO   A O    1 
ATOM   3780 C  CB   . PRO   A 1 489 ? -11.690 -50.131 37.300 1.00 17.30 ? 492  PRO   A CB   1 
ATOM   3781 C  CG   . PRO   A 1 489 ? -10.900 -48.903 37.734 1.00 18.20 ? 492  PRO   A CG   1 
ATOM   3782 C  CD   . PRO   A 1 489 ? -11.436 -48.468 39.067 1.00 19.28 ? 492  PRO   A CD   1 
ATOM   3783 N  N    . ASN   A 1 490 ? -10.394 -51.770 40.049 1.00 18.13 ? 493  ASN   A N    1 
ATOM   3784 C  CA   . ASN   A 1 490 ? -9.306  -52.707 40.304 1.00 19.71 ? 493  ASN   A CA   1 
ATOM   3785 C  C    . ASN   A 1 490 ? -9.803  -54.031 40.888 1.00 24.98 ? 493  ASN   A C    1 
ATOM   3786 O  O    . ASN   A 1 490 ? -10.889 -54.121 41.469 1.00 22.26 ? 493  ASN   A O    1 
ATOM   3787 C  CB   . ASN   A 1 490 ? -8.292  -52.078 41.246 1.00 21.05 ? 493  ASN   A CB   1 
ATOM   3788 C  CG   . ASN   A 1 490 ? -7.449  -51.040 40.560 1.00 22.01 ? 493  ASN   A CG   1 
ATOM   3789 O  OD1  . ASN   A 1 490 ? -6.607  -51.374 39.737 1.00 21.77 ? 493  ASN   A OD1  1 
ATOM   3790 N  ND2  . ASN   A 1 490 ? -7.668  -49.777 40.889 1.00 17.44 ? 493  ASN   A ND2  1 
ATOM   3791 N  N    . GLY   A 1 491 ? -8.987  -55.070 40.722 1.00 23.58 ? 494  GLY   A N    1 
ATOM   3792 C  CA   . GLY   A 1 491 ? -9.327  -56.371 41.269 1.00 23.36 ? 494  GLY   A CA   1 
ATOM   3793 C  C    . GLY   A 1 491 ? -8.247  -57.400 40.993 1.00 28.21 ? 494  GLY   A C    1 
ATOM   3794 O  O    . GLY   A 1 491 ? -7.279  -57.150 40.264 1.00 25.18 ? 494  GLY   A O    1 
ATOM   3795 N  N    . GLU   A 1 492 ? -8.445  -58.576 41.592 1.00 29.26 ? 495  GLU   A N    1 
ATOM   3796 C  CA   . GLU   A 1 492 ? -7.564  -59.726 41.399 1.00 33.80 ? 495  GLU   A CA   1 
ATOM   3797 C  C    . GLU   A 1 492 ? -7.317  -60.009 39.920 1.00 33.42 ? 495  GLU   A C    1 
ATOM   3798 O  O    . GLU   A 1 492 ? -8.256  -60.107 39.122 1.00 35.36 ? 495  GLU   A O    1 
ATOM   3799 C  CB   . GLU   A 1 492 ? -8.184  -60.961 42.069 1.00 40.37 ? 495  GLU   A CB   1 
ATOM   3800 C  CG   . GLU   A 1 492 ? -9.658  -61.205 41.649 1.00 51.50 ? 495  GLU   A CG   1 
ATOM   3801 C  CD   . GLU   A 1 492 ? -10.237 -62.554 42.092 1.00 63.48 ? 495  GLU   A CD   1 
ATOM   3802 O  OE1  . GLU   A 1 492 ? -9.519  -63.579 42.021 1.00 64.40 ? 495  GLU   A OE1  1 
ATOM   3803 O  OE2  . GLU   A 1 492 ? -11.426 -62.585 42.496 1.00 66.21 ? 495  GLU   A OE2  1 
ATOM   3804 N  N    . GLY   A 1 493 ? -6.040  -60.128 39.560 1.00 33.43 ? 496  GLY   A N    1 
ATOM   3805 C  CA   . GLY   A 1 493 ? -5.666  -60.559 38.226 1.00 39.47 ? 496  GLY   A CA   1 
ATOM   3806 C  C    . GLY   A 1 493 ? -5.758  -59.503 37.149 1.00 33.55 ? 496  GLY   A C    1 
ATOM   3807 O  O    . GLY   A 1 493 ? -5.606  -59.831 35.967 1.00 36.67 ? 496  GLY   A O    1 
ATOM   3808 N  N    . LEU   A 1 494 ? -6.004  -58.262 37.511 1.00 26.49 ? 497  LEU   A N    1 
ATOM   3809 C  CA   . LEU   A 1 494 ? -6.117  -57.164 36.571 1.00 25.24 ? 497  LEU   A CA   1 
ATOM   3810 C  C    . LEU   A 1 494 ? -4.954  -56.206 36.740 1.00 18.56 ? 497  LEU   A C    1 
ATOM   3811 O  O    . LEU   A 1 494 ? -4.518  -55.958 37.867 1.00 20.06 ? 497  LEU   A O    1 
ATOM   3812 C  CB   . LEU   A 1 494 ? -7.414  -56.374 36.775 1.00 18.00 ? 497  LEU   A CB   1 
ATOM   3813 C  CG   . LEU   A 1 494 ? -8.700  -57.169 36.576 1.00 19.28 ? 497  LEU   A CG   1 
ATOM   3814 C  CD1  . LEU   A 1 494 ? -9.887  -56.395 37.119 1.00 19.01 ? 497  LEU   A CD1  1 
ATOM   3815 C  CD2  . LEU   A 1 494 ? -8.879  -57.425 35.082 1.00 22.00 ? 497  LEU   A CD2  1 
ATOM   3816 N  N    . PRO   A 1 495 ? -4.479  -55.606 35.650 1.00 18.27 ? 498  PRO   A N    1 
ATOM   3817 C  CA   . PRO   A 1 495 ? -3.450  -54.566 35.767 1.00 21.34 ? 498  PRO   A CA   1 
ATOM   3818 C  C    . PRO   A 1 495 ? -3.917  -53.443 36.672 1.00 25.11 ? 498  PRO   A C    1 
ATOM   3819 O  O    . PRO   A 1 495 ? -5.105  -53.103 36.708 1.00 21.79 ? 498  PRO   A O    1 
ATOM   3820 C  CB   . PRO   A 1 495 ? -3.265  -54.073 34.327 1.00 23.26 ? 498  PRO   A CB   1 
ATOM   3821 C  CG   . PRO   A 1 495 ? -3.852  -55.121 33.464 1.00 24.35 ? 498  PRO   A CG   1 
ATOM   3822 C  CD   . PRO   A 1 495 ? -4.896  -55.840 34.260 1.00 19.49 ? 498  PRO   A CD   1 
ATOM   3823 N  N    . HIS   A 1 496 ? -2.971  -52.872 37.417 1.00 21.39 ? 499  HIS   A N    1 
ATOM   3824 C  CA   . HIS   A 1 496 ? -3.317  -51.806 38.343 1.00 23.37 ? 499  HIS   A CA   1 
ATOM   3825 C  C    . HIS   A 1 496 ? -3.739  -50.553 37.591 1.00 21.94 ? 499  HIS   A C    1 
ATOM   3826 O  O    . HIS   A 1 496 ? -3.047  -50.087 36.681 1.00 21.48 ? 499  HIS   A O    1 
ATOM   3827 C  CB   . HIS   A 1 496 ? -2.160  -51.472 39.278 1.00 22.60 ? 499  HIS   A CB   1 
ATOM   3828 C  CG   . HIS   A 1 496 ? -2.505  -50.414 40.283 1.00 23.42 ? 499  HIS   A CG   1 
ATOM   3829 N  ND1  . HIS   A 1 496 ? -3.431  -50.615 41.284 1.00 24.03 ? 499  HIS   A ND1  1 
ATOM   3830 C  CD2  . HIS   A 1 496 ? -2.084  -49.132 40.412 1.00 26.03 ? 499  HIS   A CD2  1 
ATOM   3831 C  CE1  . HIS   A 1 496 ? -3.545  -49.512 42.004 1.00 25.84 ? 499  HIS   A CE1  1 
ATOM   3832 N  NE2  . HIS   A 1 496 ? -2.739  -48.596 41.496 1.00 27.15 ? 499  HIS   A NE2  1 
ATOM   3833 N  N    . TRP   A 1 497 ? -4.875  -50.004 37.989 1.00 18.04 ? 500  TRP   A N    1 
ATOM   3834 C  CA   . TRP   A 1 497 ? -5.422  -48.802 37.380 1.00 19.55 ? 500  TRP   A CA   1 
ATOM   3835 C  C    . TRP   A 1 497 ? -5.397  -47.710 38.435 1.00 18.04 ? 500  TRP   A C    1 
ATOM   3836 O  O    . TRP   A 1 497 ? -6.185  -47.770 39.391 1.00 19.54 ? 500  TRP   A O    1 
ATOM   3837 C  CB   . TRP   A 1 497 ? -6.849  -49.075 36.886 1.00 17.61 ? 500  TRP   A CB   1 
ATOM   3838 C  CG   . TRP   A 1 497 ? -7.474  -47.993 36.043 1.00 16.27 ? 500  TRP   A CG   1 
ATOM   3839 C  CD1  . TRP   A 1 497 ? -7.132  -46.673 36.005 1.00 17.50 ? 500  TRP   A CD1  1 
ATOM   3840 C  CD2  . TRP   A 1 497 ? -8.538  -48.161 35.089 1.00 14.95 ? 500  TRP   A CD2  1 
ATOM   3841 N  NE1  . TRP   A 1 497 ? -7.935  -46.003 35.102 1.00 15.01 ? 500  TRP   A NE1  1 
ATOM   3842 C  CE2  . TRP   A 1 497 ? -8.808  -46.893 34.536 1.00 14.88 ? 500  TRP   A CE2  1 
ATOM   3843 C  CE3  . TRP   A 1 497 ? -9.305  -49.258 34.674 1.00 13.32 ? 500  TRP   A CE3  1 
ATOM   3844 C  CZ2  . TRP   A 1 497 ? -9.799  -46.691 33.574 1.00 14.42 ? 500  TRP   A CZ2  1 
ATOM   3845 C  CZ3  . TRP   A 1 497 ? -10.293 -49.058 33.711 1.00 14.11 ? 500  TRP   A CZ3  1 
ATOM   3846 C  CH2  . TRP   A 1 497 ? -10.529 -47.787 33.174 1.00 15.08 ? 500  TRP   A CH2  1 
ATOM   3847 N  N    . PRO   A 1 498 ? -4.484  -46.740 38.350 1.00 20.76 ? 501  PRO   A N    1 
ATOM   3848 C  CA   . PRO   A 1 498 ? -4.393  -45.726 39.401 1.00 22.08 ? 501  PRO   A CA   1 
ATOM   3849 C  C    . PRO   A 1 498 ? -5.543  -44.738 39.316 1.00 19.27 ? 501  PRO   A C    1 
ATOM   3850 O  O    . PRO   A 1 498 ? -6.068  -44.445 38.242 1.00 18.09 ? 501  PRO   A O    1 
ATOM   3851 C  CB   . PRO   A 1 498 ? -3.056  -45.029 39.113 1.00 22.09 ? 501  PRO   A CB   1 
ATOM   3852 C  CG   . PRO   A 1 498 ? -2.891  -45.170 37.632 1.00 22.09 ? 501  PRO   A CG   1 
ATOM   3853 C  CD   . PRO   A 1 498 ? -3.507  -46.509 37.269 1.00 20.48 ? 501  PRO   A CD   1 
ATOM   3854 N  N    . GLU   A 1 499 ? -5.896  -44.184 40.467 1.00 21.15 ? 502  GLU   A N    1 
ATOM   3855 C  CA   . GLU   A 1 499 ? -6.849  -43.090 40.487 1.00 20.02 ? 502  GLU   A CA   1 
ATOM   3856 C  C    . GLU   A 1 499 ? -6.267  -41.888 39.750 1.00 24.90 ? 502  GLU   A C    1 
ATOM   3857 O  O    . GLU   A 1 499 ? -5.059  -41.628 39.795 1.00 20.96 ? 502  GLU   A O    1 
ATOM   3858 C  CB   . GLU   A 1 499 ? -7.197  -42.739 41.935 1.00 27.06 ? 502  GLU   A CB   1 
ATOM   3859 C  CG   . GLU   A 1 499 ? -8.239  -41.644 42.069 1.00 35.26 ? 502  GLU   A CG   1 
ATOM   3860 C  CD   . GLU   A 1 499 ? -8.488  -41.236 43.517 1.00 42.03 ? 502  GLU   A CD   1 
ATOM   3861 O  OE1  . GLU   A 1 499 ? -8.448  -42.128 44.401 1.00 47.34 ? 502  GLU   A OE1  1 
ATOM   3862 O  OE2  . GLU   A 1 499 ? -8.741  -40.027 43.761 1.00 44.32 ? 502  GLU   A OE2  1 
ATOM   3863 N  N    . TYR   A 1 500 ? -7.128  -41.163 39.040 1.00 17.70 ? 503  TYR   A N    1 
ATOM   3864 C  CA   . TYR   A 1 500 ? -6.725  -39.910 38.408 1.00 19.22 ? 503  TYR   A CA   1 
ATOM   3865 C  C    . TYR   A 1 500 ? -6.660  -38.838 39.494 1.00 22.67 ? 503  TYR   A C    1 
ATOM   3866 O  O    . TYR   A 1 500 ? -7.632  -38.139 39.777 1.00 19.95 ? 503  TYR   A O    1 
ATOM   3867 C  CB   . TYR   A 1 500 ? -7.689  -39.540 37.285 1.00 19.01 ? 503  TYR   A CB   1 
ATOM   3868 C  CG   . TYR   A 1 500 ? -7.228  -38.399 36.410 1.00 19.55 ? 503  TYR   A CG   1 
ATOM   3869 C  CD1  . TYR   A 1 500 ? -6.326  -38.608 35.373 1.00 19.54 ? 503  TYR   A CD1  1 
ATOM   3870 C  CD2  . TYR   A 1 500 ? -7.704  -37.113 36.618 1.00 18.28 ? 503  TYR   A CD2  1 
ATOM   3871 C  CE1  . TYR   A 1 500 ? -5.907  -37.567 34.576 1.00 16.70 ? 503  TYR   A CE1  1 
ATOM   3872 C  CE2  . TYR   A 1 500 ? -7.295  -36.063 35.831 1.00 20.80 ? 503  TYR   A CE2  1 
ATOM   3873 C  CZ   . TYR   A 1 500 ? -6.394  -36.298 34.808 1.00 20.28 ? 503  TYR   A CZ   1 
ATOM   3874 O  OH   . TYR   A 1 500 ? -5.983  -35.247 34.032 1.00 21.29 ? 503  TYR   A OH   1 
ATOM   3875 N  N    . ASN   A 1 501 ? -5.491  -38.698 40.116 1.00 22.56 ? 504  ASN   A N    1 
ATOM   3876 C  CA   . ASN   A 1 501 ? -5.302  -37.732 41.179 1.00 23.17 ? 504  ASN   A CA   1 
ATOM   3877 C  C    . ASN   A 1 501 ? -4.367  -36.622 40.686 1.00 24.45 ? 504  ASN   A C    1 
ATOM   3878 O  O    . ASN   A 1 501 ? -4.303  -36.345 39.482 1.00 22.45 ? 504  ASN   A O    1 
ATOM   3879 C  CB   . ASN   A 1 501 ? -4.831  -38.457 42.455 1.00 25.46 ? 504  ASN   A CB   1 
ATOM   3880 C  CG   . ASN   A 1 501 ? -3.530  -39.246 42.272 1.00 27.55 ? 504  ASN   A CG   1 
ATOM   3881 O  OD1  . ASN   A 1 501 ? -2.778  -39.061 41.311 1.00 25.23 ? 504  ASN   A OD1  1 
ATOM   3882 N  ND2  . ASN   A 1 501 ? -3.272  -40.147 43.215 1.00 30.46 ? 504  ASN   A ND2  1 
ATOM   3883 N  N    . GLN   A 1 502 ? -3.670  -35.961 41.615 1.00 25.48 ? 505  GLN   A N    1 
ATOM   3884 C  CA   . GLN   A 1 502 ? -2.797  -34.870 41.195 1.00 27.75 ? 505  GLN   A CA   1 
ATOM   3885 C  C    . GLN   A 1 502 ? -1.672  -35.355 40.288 1.00 25.60 ? 505  GLN   A C    1 
ATOM   3886 O  O    . GLN   A 1 502 ? -1.150  -34.563 39.496 1.00 26.41 ? 505  GLN   A O    1 
ATOM   3887 C  CB   . GLN   A 1 502 ? -2.222  -34.140 42.410 1.00 27.69 ? 505  GLN   A CB   1 
ATOM   3888 C  CG   . GLN   A 1 502 ? -3.266  -33.347 43.199 1.00 34.00 ? 505  GLN   A CG   1 
ATOM   3889 C  CD   . GLN   A 1 502 ? -4.103  -32.425 42.316 1.00 34.02 ? 505  GLN   A CD   1 
ATOM   3890 O  OE1  . GLN   A 1 502 ? -3.577  -31.530 41.648 1.00 40.79 ? 505  GLN   A OE1  1 
ATOM   3891 N  NE2  . GLN   A 1 502 ? -5.416  -32.615 42.347 1.00 34.10 ? 505  GLN   A NE2  1 
ATOM   3892 N  N    . LYS   A 1 503 ? -1.312  -36.643 40.364 1.00 25.30 ? 506  LYS   A N    1 
ATOM   3893 C  CA   . LYS   A 1 503 ? -0.328  -37.223 39.451 1.00 21.91 ? 506  LYS   A CA   1 
ATOM   3894 C  C    . LYS   A 1 503 ? -0.914  -37.573 38.089 1.00 25.59 ? 506  LYS   A C    1 
ATOM   3895 O  O    . LYS   A 1 503 ? -0.153  -37.842 37.152 1.00 21.32 ? 506  LYS   A O    1 
ATOM   3896 C  CB   . LYS   A 1 503 ? 0.299   -38.469 40.069 1.00 27.98 ? 506  LYS   A CB   1 
ATOM   3897 C  CG   . LYS   A 1 503 ? 1.074   -38.210 41.357 1.00 32.55 ? 506  LYS   A CG   1 
ATOM   3898 C  CD   . LYS   A 1 503 ? 1.486   -39.528 41.999 1.00 39.11 ? 506  LYS   A CD   1 
ATOM   3899 C  CE   . LYS   A 1 503 ? 2.807   -39.401 42.722 1.00 47.88 ? 506  LYS   A CE   1 
ATOM   3900 N  NZ   . LYS   A 1 503 ? 3.062   -37.987 43.121 1.00 55.04 ? 506  LYS   A NZ   1 
ATOM   3901 N  N    . GLU   A 1 504 ? -2.246  -37.597 37.968 1.00 20.11 ? 507  GLU   A N    1 
ATOM   3902 C  CA   . GLU   A 1 504 ? -2.923  -37.807 36.688 1.00 18.67 ? 507  GLU   A CA   1 
ATOM   3903 C  C    . GLU   A 1 504 ? -2.580  -39.164 36.075 1.00 19.23 ? 507  GLU   A C    1 
ATOM   3904 O  O    . GLU   A 1 504 ? -2.403  -39.296 34.859 1.00 20.21 ? 507  GLU   A O    1 
ATOM   3905 C  CB   . GLU   A 1 504 ? -2.618  -36.658 35.738 1.00 19.62 ? 507  GLU   A CB   1 
ATOM   3906 C  CG   . GLU   A 1 504 ? -3.196  -35.390 36.309 1.00 19.08 ? 507  GLU   A CG   1 
ATOM   3907 C  CD   . GLU   A 1 504 ? -3.176  -34.217 35.383 1.00 28.95 ? 507  GLU   A CD   1 
ATOM   3908 O  OE1  . GLU   A 1 504 ? -2.771  -34.365 34.205 1.00 30.56 ? 507  GLU   A OE1  1 
ATOM   3909 O  OE2  . GLU   A 1 504 ? -3.599  -33.135 35.845 1.00 33.04 ? 507  GLU   A OE2  1 
ATOM   3910 N  N    . GLY   A 1 505 ? -2.536  -40.190 36.924 1.00 16.63 ? 508  GLY   A N    1 
ATOM   3911 C  CA   . GLY   A 1 505 ? -2.458  -41.549 36.422 1.00 16.56 ? 508  GLY   A CA   1 
ATOM   3912 C  C    . GLY   A 1 505 ? -3.678  -41.905 35.586 1.00 20.43 ? 508  GLY   A C    1 
ATOM   3913 O  O    . GLY   A 1 505 ? -4.797  -41.451 35.847 1.00 18.25 ? 508  GLY   A O    1 
ATOM   3914 N  N    . TYR   A 1 506 ? -3.445  -42.702 34.551 1.00 16.88 ? 509  TYR   A N    1 
ATOM   3915 C  CA   . TYR   A 1 506 ? -4.510  -43.222 33.707 1.00 17.48 ? 509  TYR   A CA   1 
ATOM   3916 C  C    . TYR   A 1 506 ? -4.068  -44.574 33.182 1.00 17.24 ? 509  TYR   A C    1 
ATOM   3917 O  O    . TYR   A 1 506 ? -2.902  -44.955 33.292 1.00 18.10 ? 509  TYR   A O    1 
ATOM   3918 C  CB   . TYR   A 1 506 ? -4.858  -42.269 32.562 1.00 15.52 ? 509  TYR   A CB   1 
ATOM   3919 C  CG   . TYR   A 1 506 ? -3.784  -42.115 31.496 1.00 18.17 ? 509  TYR   A CG   1 
ATOM   3920 C  CD1  . TYR   A 1 506 ? -2.662  -41.315 31.716 1.00 20.63 ? 509  TYR   A CD1  1 
ATOM   3921 C  CD2  . TYR   A 1 506 ? -3.917  -42.731 30.257 1.00 17.31 ? 509  TYR   A CD2  1 
ATOM   3922 C  CE1  . TYR   A 1 506 ? -1.682  -41.155 30.737 1.00 20.29 ? 509  TYR   A CE1  1 
ATOM   3923 C  CE2  . TYR   A 1 506 ? -2.942  -42.591 29.275 1.00 18.49 ? 509  TYR   A CE2  1 
ATOM   3924 C  CZ   . TYR   A 1 506 ? -1.830  -41.804 29.524 1.00 22.63 ? 509  TYR   A CZ   1 
ATOM   3925 O  OH   . TYR   A 1 506 ? -0.871  -41.655 28.549 1.00 22.84 ? 509  TYR   A OH   1 
ATOM   3926 N  N    . LEU   A 1 507 ? -5.014  -45.325 32.638 1.00 15.93 ? 510  LEU   A N    1 
ATOM   3927 C  CA   . LEU   A 1 507 ? -4.731  -46.665 32.145 1.00 14.90 ? 510  LEU   A CA   1 
ATOM   3928 C  C    . LEU   A 1 507 ? -4.679  -46.642 30.625 1.00 17.34 ? 510  LEU   A C    1 
ATOM   3929 O  O    . LEU   A 1 507 ? -5.629  -46.191 29.980 1.00 16.59 ? 510  LEU   A O    1 
ATOM   3930 C  CB   . LEU   A 1 507 ? -5.781  -47.670 32.628 1.00 13.42 ? 510  LEU   A CB   1 
ATOM   3931 C  CG   . LEU   A 1 507 ? -5.381  -49.128 32.341 1.00 17.65 ? 510  LEU   A CG   1 
ATOM   3932 C  CD1  . LEU   A 1 507 ? -4.132  -49.526 33.118 1.00 17.69 ? 510  LEU   A CD1  1 
ATOM   3933 C  CD2  . LEU   A 1 507 ? -6.561  -50.083 32.640 1.00 16.48 ? 510  LEU   A CD2  1 
ATOM   3934 N  N    . GLN   A 1 508 ? -3.563  -47.107 30.054 1.00 14.59 ? 511  GLN   A N    1 
ATOM   3935 C  CA   . GLN   A 1 508 ? -3.472  -47.393 28.625 1.00 15.53 ? 511  GLN   A CA   1 
ATOM   3936 C  C    . GLN   A 1 508 ? -4.003  -48.805 28.408 1.00 19.02 ? 511  GLN   A C    1 
ATOM   3937 O  O    . GLN   A 1 508 ? -3.385  -49.787 28.850 1.00 17.67 ? 511  GLN   A O    1 
ATOM   3938 C  CB   . GLN   A 1 508 ? -2.024  -47.252 28.137 1.00 18.58 ? 511  GLN   A CB   1 
ATOM   3939 C  CG   . GLN   A 1 508 ? -1.438  -45.838 28.289 1.00 19.05 ? 511  GLN   A CG   1 
ATOM   3940 C  CD   . GLN   A 1 508 ? 0.079   -45.790 28.080 1.00 23.37 ? 511  GLN   A CD   1 
ATOM   3941 O  OE1  . GLN   A 1 508 ? 0.812   -46.675 28.539 1.00 19.63 ? 511  GLN   A OE1  1 
ATOM   3942 N  NE2  . GLN   A 1 508 ? 0.551   -44.743 27.401 1.00 22.83 ? 511  GLN   A NE2  1 
ATOM   3943 N  N    . ILE   A 1 509 ? -5.163  -48.904 27.741 1.00 15.32 ? 512  ILE   A N    1 
ATOM   3944 C  CA   . ILE   A 1 509 ? -5.862  -50.167 27.540 1.00 15.19 ? 512  ILE   A CA   1 
ATOM   3945 C  C    . ILE   A 1 509 ? -5.607  -50.647 26.119 1.00 13.96 ? 512  ILE   A C    1 
ATOM   3946 O  O    . ILE   A 1 509 ? -5.822  -49.902 25.159 1.00 17.06 ? 512  ILE   A O    1 
ATOM   3947 C  CB   . ILE   A 1 509 ? -7.377  -50.020 27.792 1.00 14.89 ? 512  ILE   A CB   1 
ATOM   3948 C  CG1  . ILE   A 1 509 ? -7.646  -49.558 29.236 1.00 16.16 ? 512  ILE   A CG1  1 
ATOM   3949 C  CG2  . ILE   A 1 509 ? -8.064  -51.344 27.534 1.00 15.65 ? 512  ILE   A CG2  1 
ATOM   3950 C  CD1  . ILE   A 1 509 ? -9.156  -49.353 29.545 1.00 14.55 ? 512  ILE   A CD1  1 
ATOM   3951 N  N    . GLY   A 1 510 ? -5.167  -51.893 25.981 1.00 18.37 ? 513  GLY   A N    1 
ATOM   3952 C  CA   . GLY   A 1 510 ? -4.943  -52.451 24.661 1.00 19.73 ? 513  GLY   A CA   1 
ATOM   3953 C  C    . GLY   A 1 510 ? -4.305  -53.823 24.783 1.00 20.60 ? 513  GLY   A C    1 
ATOM   3954 O  O    . GLY   A 1 510 ? -4.381  -54.455 25.836 1.00 18.46 ? 513  GLY   A O    1 
ATOM   3955 N  N    . ALA   A 1 511 ? -3.666  -54.263 23.690 1.00 23.43 ? 514  ALA   A N    1 
ATOM   3956 C  CA   . ALA   A 1 511 ? -2.930  -55.529 23.709 1.00 27.57 ? 514  ALA   A CA   1 
ATOM   3957 C  C    . ALA   A 1 511 ? -1.952  -55.578 24.881 1.00 26.76 ? 514  ALA   A C    1 
ATOM   3958 O  O    . ALA   A 1 511 ? -1.866  -56.590 25.591 1.00 28.34 ? 514  ALA   A O    1 
ATOM   3959 C  CB   . ALA   A 1 511 ? -2.199  -55.738 22.382 1.00 26.92 ? 514  ALA   A CB   1 
ATOM   3960 N  N    . ASN   A 1 512 ? -1.194  -54.497 25.090 1.00 19.35 ? 515  ASN   A N    1 
ATOM   3961 C  CA   . ASN   A 1 512 ? -0.536  -54.255 26.370 1.00 24.90 ? 515  ASN   A CA   1 
ATOM   3962 C  C    . ASN   A 1 512 ? -1.285  -53.187 27.138 1.00 23.23 ? 515  ASN   A C    1 
ATOM   3963 O  O    . ASN   A 1 512 ? -1.495  -52.085 26.625 1.00 26.48 ? 515  ASN   A O    1 
ATOM   3964 C  CB   . ASN   A 1 512 ? 0.910   -53.784 26.245 1.00 28.76 ? 515  ASN   A CB   1 
ATOM   3965 C  CG   . ASN   A 1 512 ? 1.785   -54.383 27.329 1.00 43.31 ? 515  ASN   A CG   1 
ATOM   3966 O  OD1  . ASN   A 1 512 ? 2.378   -55.469 27.177 1.00 43.15 ? 515  ASN   A OD1  1 
ATOM   3967 N  ND2  . ASN   A 1 512 ? 1.768   -53.739 28.485 1.00 42.14 ? 515  ASN   A ND2  1 
ATOM   3968 N  N    . THR   A 1 513 ? -1.616  -53.493 28.385 1.00 23.43 ? 516  THR   A N    1 
ATOM   3969 C  CA   . THR   A 1 513 ? -2.378  -52.599 29.240 1.00 23.57 ? 516  THR   A CA   1 
ATOM   3970 C  C    . THR   A 1 513 ? -1.504  -52.262 30.434 1.00 23.36 ? 516  THR   A C    1 
ATOM   3971 O  O    . THR   A 1 513 ? -1.000  -53.169 31.106 1.00 22.75 ? 516  THR   A O    1 
ATOM   3972 C  CB   . THR   A 1 513 ? -3.689  -53.263 29.676 1.00 18.90 ? 516  THR   A CB   1 
ATOM   3973 O  OG1  . THR   A 1 513 ? -4.499  -53.500 28.516 1.00 19.78 ? 516  THR   A OG1  1 
ATOM   3974 C  CG2  . THR   A 1 513 ? -4.446  -52.375 30.648 1.00 20.61 ? 516  THR   A CG2  1 
ATOM   3975 N  N    . GLN   A 1 514 ? -1.278  -50.985 30.642 1.00 18.78 ? 517  GLN   A N    1 
ATOM   3976 C  CA   . GLN   A 1 514 ? -0.474  -50.527 31.734 1.00 20.16 ? 517  GLN   A CA   1 
ATOM   3977 C  C    . GLN   A 1 514 ? -0.747  -49.068 32.101 1.00 15.49 ? 517  GLN   A C    1 
ATOM   3978 O  O    . GLN   A 1 514 ? -1.184  -48.289 31.304 1.00 18.28 ? 517  GLN   A O    1 
ATOM   3979 C  CB   . GLN   A 1 514 ? 1.036   -50.649 31.422 1.00 23.80 ? 517  GLN   A CB   1 
ATOM   3980 C  CG   . GLN   A 1 514 ? 1.522   -49.692 30.369 1.00 22.87 ? 517  GLN   A CG   1 
ATOM   3981 C  CD   . GLN   A 1 514 ? 1.230   -50.246 29.017 1.00 24.52 ? 517  GLN   A CD   1 
ATOM   3982 O  OE1  . GLN   A 1 514 ? 1.224   -51.446 28.856 1.00 25.02 ? 517  GLN   A OE1  1 
ATOM   3983 N  NE2  . GLN   A 1 514 ? 0.971   -49.395 28.052 1.00 24.71 ? 517  GLN   A NE2  1 
ATOM   3984 N  N    . ALA   A 1 515 ? -0.472  -48.741 33.346 1.00 16.55 ? 518  ALA   A N    1 
ATOM   3985 C  CA   . ALA   A 1 515 ? -0.659  -47.391 33.822 1.00 20.22 ? 518  ALA   A CA   1 
ATOM   3986 C  C    . ALA   A 1 515 ? 0.311   -46.386 33.245 1.00 22.08 ? 518  ALA   A C    1 
ATOM   3987 O  O    . ALA   A 1 515 ? 1.414   -46.728 32.909 1.00 20.89 ? 518  ALA   A O    1 
ATOM   3988 C  CB   . ALA   A 1 515 ? -0.588  -47.341 35.325 1.00 20.84 ? 518  ALA   A CB   1 
ATOM   3989 N  N    . ALA   A 1 516 ? -0.121  -45.155 33.130 1.00 16.69 ? 519  ALA   A N    1 
ATOM   3990 C  CA   . ALA   A 1 516 ? 0.677   -44.073 32.592 1.00 19.51 ? 519  ALA   A CA   1 
ATOM   3991 C  C    . ALA   A 1 516 ? 0.240   -42.782 33.275 1.00 22.62 ? 519  ALA   A C    1 
ATOM   3992 O  O    . ALA   A 1 516 ? -0.652  -42.804 34.090 1.00 21.88 ? 519  ALA   A O    1 
ATOM   3993 C  CB   . ALA   A 1 516 ? 0.559   -43.958 31.098 1.00 18.69 ? 519  ALA   A CB   1 
ATOM   3994 N  N    . GLN   A 1 517 ? 0.959   -41.703 33.042 1.00 20.26 ? 520  GLN   A N    1 
ATOM   3995 C  CA   . GLN   A 1 517 ? 0.632   -40.464 33.674 1.00 20.39 ? 520  GLN   A CA   1 
ATOM   3996 C  C    . GLN   A 1 517 ? 0.479   -39.256 32.735 1.00 21.61 ? 520  GLN   A C    1 
ATOM   3997 O  O    . GLN   A 1 517 ? 1.095   -39.216 31.698 1.00 22.71 ? 520  GLN   A O    1 
ATOM   3998 C  CB   . GLN   A 1 517 ? 1.664   -40.185 34.761 1.00 20.92 ? 520  GLN   A CB   1 
ATOM   3999 C  CG   . GLN   A 1 517 ? 1.526   -41.073 35.982 1.00 22.17 ? 520  GLN   A CG   1 
ATOM   4000 C  CD   . GLN   A 1 517 ? 2.557   -40.791 37.054 1.00 29.40 ? 520  GLN   A CD   1 
ATOM   4001 O  OE1  . GLN   A 1 517 ? 3.680   -40.411 36.761 1.00 28.09 ? 520  GLN   A OE1  1 
ATOM   4002 N  NE2  . GLN   A 1 517 ? 2.176   -40.992 38.303 1.00 27.10 ? 520  GLN   A NE2  1 
ATOM   4003 N  N    . LYS   A 1 518 ? -0.285  -38.270 33.159 1.00 17.67 ? 521  LYS   A N    1 
ATOM   4004 C  CA   . LYS   A 1 518 ? -0.485  -37.039 32.391 1.00 21.46 ? 521  LYS   A CA   1 
ATOM   4005 C  C    . LYS   A 1 518 ? -1.062  -37.040 30.979 1.00 23.26 ? 521  LYS   A C    1 
ATOM   4006 O  O    . LYS   A 1 518 ? -0.515  -36.447 30.069 1.00 23.70 ? 521  LYS   A O    1 
ATOM   4007 C  CB   . LYS   A 1 518 ? 0.845   -36.246 32.406 1.00 26.10 ? 521  LYS   A CB   1 
ATOM   4008 C  CG   . LYS   A 1 518 ? 1.256   -35.759 33.781 1.00 26.89 ? 521  LYS   A CG   1 
ATOM   4009 C  CD   . LYS   A 1 518 ? 0.475   -34.519 34.147 1.00 33.27 ? 521  LYS   A CD   1 
ATOM   4010 C  CE   . LYS   A 1 518 ? 0.469   -34.272 35.642 1.00 36.05 ? 521  LYS   A CE   1 
ATOM   4011 N  NZ   . LYS   A 1 518 ? 1.820   -33.990 36.177 1.00 42.82 ? 521  LYS   A NZ   1 
ATOM   4012 N  N    . LEU   A 1 519 ? -2.183  -37.718 30.820 1.00 18.40 ? 522  LEU   A N    1 
ATOM   4013 C  CA   . LEU   A 1 519 ? -2.774  -37.754 29.514 1.00 18.84 ? 522  LEU   A CA   1 
ATOM   4014 C  C    . LEU   A 1 519 ? -3.142  -36.375 28.954 1.00 18.90 ? 522  LEU   A C    1 
ATOM   4015 O  O    . LEU   A 1 519 ? -3.717  -35.577 29.632 1.00 19.33 ? 522  LEU   A O    1 
ATOM   4016 C  CB   . LEU   A 1 519 ? -4.074  -38.574 29.622 1.00 15.81 ? 522  LEU   A CB   1 
ATOM   4017 C  CG   . LEU   A 1 519 ? -4.996  -38.752 28.427 1.00 19.17 ? 522  LEU   A CG   1 
ATOM   4018 C  CD1  . LEU   A 1 519 ? -4.288  -39.503 27.321 1.00 19.59 ? 522  LEU   A CD1  1 
ATOM   4019 C  CD2  . LEU   A 1 519 ? -6.225  -39.521 28.876 1.00 17.70 ? 522  LEU   A CD2  1 
ATOM   4020 N  N    . LYS   A 1 520 ? -2.712  -36.096 27.728 1.00 18.79 ? 523  LYS   A N    1 
ATOM   4021 C  CA   . LYS   A 1 520 ? -3.035  -34.853 27.004 1.00 23.13 ? 523  LYS   A CA   1 
ATOM   4022 C  C    . LYS   A 1 520 ? -2.588  -33.572 27.735 1.00 22.25 ? 523  LYS   A C    1 
ATOM   4023 O  O    . LYS   A 1 520 ? -3.106  -32.514 27.462 1.00 20.32 ? 523  LYS   A O    1 
ATOM   4024 C  CB   . LYS   A 1 520 ? -4.516  -34.775 26.583 1.00 19.51 ? 523  LYS   A CB   1 
ATOM   4025 C  CG   . LYS   A 1 520 ? -5.012  -35.944 25.758 1.00 19.57 ? 523  LYS   A CG   1 
ATOM   4026 C  CD   . LYS   A 1 520 ? -4.504  -35.893 24.333 1.00 22.65 ? 523  LYS   A CD   1 
ATOM   4027 C  CE   . LYS   A 1 520 ? -4.850  -37.170 23.595 1.00 21.59 ? 523  LYS   A CE   1 
ATOM   4028 N  NZ   . LYS   A 1 520 ? -4.342  -37.161 22.202 1.00 19.86 ? 523  LYS   A NZ   1 
ATOM   4029 N  N    . ASP   A 1 521 ? -1.633  -33.667 28.620 1.00 20.11 ? 524  ASP   A N    1 
ATOM   4030 C  CA   . ASP   A 1 521 ? -1.214  -32.493 29.386 1.00 25.42 ? 524  ASP   A CA   1 
ATOM   4031 C  C    . ASP   A 1 521 ? -0.799  -31.283 28.507 1.00 24.23 ? 524  ASP   A C    1 
ATOM   4032 O  O    . ASP   A 1 521 ? -1.320  -30.205 28.648 1.00 20.26 ? 524  ASP   A O    1 
ATOM   4033 C  CB   . ASP   A 1 521 ? -0.107  -32.904 30.341 1.00 28.12 ? 524  ASP   A CB   1 
ATOM   4034 C  CG   . ASP   A 1 521 ? 0.252   -31.820 31.328 1.00 32.44 ? 524  ASP   A CG   1 
ATOM   4035 O  OD1  . ASP   A 1 521 ? -0.654  -31.266 31.958 1.00 26.52 ? 524  ASP   A OD1  1 
ATOM   4036 O  OD2  . ASP   A 1 521 ? 1.452   -31.532 31.477 1.00 31.67 ? 524  ASP   A OD2  1 
ATOM   4037 N  N    . LYS   A 1 522 ? 0.117   -31.509 27.574 1.00 25.55 ? 525  LYS   A N    1 
ATOM   4038 C  CA   . LYS   A 1 522 ? 0.574   -30.442 26.697 1.00 26.40 ? 525  LYS   A CA   1 
ATOM   4039 C  C    . LYS   A 1 522 ? -0.539  -29.886 25.812 1.00 27.26 ? 525  LYS   A C    1 
ATOM   4040 O  O    . LYS   A 1 522 ? -0.608  -28.703 25.566 1.00 21.87 ? 525  LYS   A O    1 
ATOM   4041 C  CB   . LYS   A 1 522 ? 1.715   -30.941 25.833 1.00 28.86 ? 525  LYS   A CB   1 
ATOM   4042 C  CG   . LYS   A 1 522 ? 2.951   -31.343 26.604 1.00 36.12 ? 525  LYS   A CG   1 
ATOM   4043 C  CD   . LYS   A 1 522 ? 4.074   -31.669 25.634 1.00 45.11 ? 525  LYS   A CD   1 
ATOM   4044 C  CE   . LYS   A 1 522 ? 5.337   -32.108 26.356 1.00 39.43 ? 525  LYS   A CE   1 
ATOM   4045 N  NZ   . LYS   A 1 522 ? 5.886   -31.030 27.217 1.00 39.50 ? 525  LYS   A NZ   1 
ATOM   4046 N  N    . GLU   A 1 523 ? -1.387  -30.775 25.319 1.00 23.39 ? 526  GLU   A N    1 
ATOM   4047 C  CA   . GLU   A 1 523 ? -2.497  -30.372 24.476 1.00 21.48 ? 526  GLU   A CA   1 
ATOM   4048 C  C    . GLU   A 1 523 ? -3.503  -29.537 25.217 1.00 20.33 ? 526  GLU   A C    1 
ATOM   4049 O  O    . GLU   A 1 523 ? -3.985  -28.563 24.698 1.00 19.07 ? 526  GLU   A O    1 
ATOM   4050 C  CB   . GLU   A 1 523 ? -3.171  -31.618 23.941 1.00 23.25 ? 526  GLU   A CB   1 
ATOM   4051 C  CG   . GLU   A 1 523 ? -2.377  -32.363 22.882 1.00 24.27 ? 526  GLU   A CG   1 
ATOM   4052 C  CD   . GLU   A 1 523 ? -1.352  -33.329 23.451 1.00 28.69 ? 526  GLU   A CD   1 
ATOM   4053 O  OE1  . GLU   A 1 523 ? -1.178  -33.388 24.677 1.00 25.62 ? 526  GLU   A OE1  1 
ATOM   4054 O  OE2  . GLU   A 1 523 ? -0.712  -34.031 22.657 1.00 36.33 ? 526  GLU   A OE2  1 
ATOM   4055 N  N    . VAL   A 1 524 ? -3.803  -29.949 26.444 1.00 17.75 ? 527  VAL   A N    1 
ATOM   4056 C  CA   . VAL   A 1 524 ? -4.698  -29.129 27.251 1.00 19.61 ? 527  VAL   A CA   1 
ATOM   4057 C  C    . VAL   A 1 524 ? -4.110  -27.735 27.433 1.00 20.86 ? 527  VAL   A C    1 
ATOM   4058 O  O    . VAL   A 1 524 ? -4.805  -26.724 27.274 1.00 21.06 ? 527  VAL   A O    1 
ATOM   4059 C  CB   . VAL   A 1 524 ? -4.980  -29.805 28.603 1.00 20.47 ? 527  VAL   A CB   1 
ATOM   4060 C  CG1  . VAL   A 1 524 ? -5.773  -28.857 29.488 1.00 20.46 ? 527  VAL   A CG1  1 
ATOM   4061 C  CG2  . VAL   A 1 524 ? -5.750  -31.128 28.391 1.00 16.23 ? 527  VAL   A CG2  1 
ATOM   4062 N  N    . ALA   A 1 525 ? -2.818  -27.655 27.759 1.00 20.63 ? 528  ALA   A N    1 
ATOM   4063 C  CA   . ALA   A 1 525 ? -2.211  -26.332 27.932 1.00 20.92 ? 528  ALA   A CA   1 
ATOM   4064 C  C    . ALA   A 1 525 ? -2.302  -25.510 26.646 1.00 20.44 ? 528  ALA   A C    1 
ATOM   4065 O  O    . ALA   A 1 525 ? -2.727  -24.341 26.662 1.00 22.91 ? 528  ALA   A O    1 
ATOM   4066 C  CB   . ALA   A 1 525 ? -0.761  -26.478 28.390 1.00 21.56 ? 528  ALA   A CB   1 
ATOM   4067 N  N    . PHE   A 1 526 ? -1.942  -26.122 25.511 1.00 22.75 ? 529  PHE   A N    1 
ATOM   4068 C  CA   . PHE   A 1 526 ? -1.993  -25.413 24.235 1.00 21.42 ? 529  PHE   A CA   1 
ATOM   4069 C  C    . PHE   A 1 526 ? -3.392  -24.882 23.935 1.00 23.94 ? 529  PHE   A C    1 
ATOM   4070 O  O    . PHE   A 1 526 ? -3.577  -23.686 23.653 1.00 21.02 ? 529  PHE   A O    1 
ATOM   4071 C  CB   . PHE   A 1 526 ? -1.526  -26.324 23.099 1.00 22.14 ? 529  PHE   A CB   1 
ATOM   4072 C  CG   . PHE   A 1 526 ? -1.704  -25.698 21.755 1.00 25.77 ? 529  PHE   A CG   1 
ATOM   4073 C  CD1  . PHE   A 1 526 ? -0.827  -24.706 21.327 1.00 27.73 ? 529  PHE   A CD1  1 
ATOM   4074 C  CD2  . PHE   A 1 526 ? -2.788  -26.027 20.956 1.00 22.89 ? 529  PHE   A CD2  1 
ATOM   4075 C  CE1  . PHE   A 1 526 ? -1.004  -24.088 20.105 1.00 25.76 ? 529  PHE   A CE1  1 
ATOM   4076 C  CE2  . PHE   A 1 526 ? -2.972  -25.423 19.732 1.00 25.02 ? 529  PHE   A CE2  1 
ATOM   4077 C  CZ   . PHE   A 1 526 ? -2.079  -24.439 19.303 1.00 29.74 ? 529  PHE   A CZ   1 
ATOM   4078 N  N    . TRP   A 1 527 ? -4.398  -25.764 23.974 1.00 18.56 ? 530  TRP   A N    1 
ATOM   4079 C  CA   . TRP   A 1 527 ? -5.731  -25.354 23.549 1.00 20.28 ? 530  TRP   A CA   1 
ATOM   4080 C  C    . TRP   A 1 527 ? -6.376  -24.410 24.550 1.00 23.84 ? 530  TRP   A C    1 
ATOM   4081 O  O    . TRP   A 1 527 ? -7.136  -23.524 24.149 1.00 24.76 ? 530  TRP   A O    1 
ATOM   4082 C  CB   . TRP   A 1 527 ? -6.614  -26.584 23.316 1.00 19.57 ? 530  TRP   A CB   1 
ATOM   4083 C  CG   . TRP   A 1 527 ? -6.220  -27.283 22.064 1.00 16.89 ? 530  TRP   A CG   1 
ATOM   4084 C  CD1  . TRP   A 1 527 ? -5.539  -28.449 21.965 1.00 18.12 ? 530  TRP   A CD1  1 
ATOM   4085 C  CD2  . TRP   A 1 527 ? -6.426  -26.818 20.721 1.00 19.75 ? 530  TRP   A CD2  1 
ATOM   4086 N  NE1  . TRP   A 1 527 ? -5.326  -28.762 20.644 1.00 19.00 ? 530  TRP   A NE1  1 
ATOM   4087 C  CE2  . TRP   A 1 527 ? -5.860  -27.775 19.860 1.00 18.58 ? 530  TRP   A CE2  1 
ATOM   4088 C  CE3  . TRP   A 1 527 ? -7.037  -25.687 20.167 1.00 20.85 ? 530  TRP   A CE3  1 
ATOM   4089 C  CZ2  . TRP   A 1 527 ? -5.892  -27.643 18.469 1.00 19.15 ? 530  TRP   A CZ2  1 
ATOM   4090 C  CZ3  . TRP   A 1 527 ? -7.068  -25.552 18.787 1.00 20.76 ? 530  TRP   A CZ3  1 
ATOM   4091 C  CH2  . TRP   A 1 527 ? -6.503  -26.527 17.954 1.00 19.37 ? 530  TRP   A CH2  1 
ATOM   4092 N  N    . THR   A 1 528 ? -6.101  -24.575 25.847 1.00 22.63 ? 531  THR   A N    1 
ATOM   4093 C  CA   . THR   A 1 528 ? -6.648  -23.642 26.823 1.00 25.87 ? 531  THR   A CA   1 
ATOM   4094 C  C    . THR   A 1 528 ? -6.100  -22.244 26.577 1.00 29.18 ? 531  THR   A C    1 
ATOM   4095 O  O    . THR   A 1 528 ? -6.859  -21.262 26.559 1.00 29.06 ? 531  THR   A O    1 
ATOM   4096 C  CB   . THR   A 1 528 ? -6.315  -24.106 28.242 1.00 25.02 ? 531  THR   A CB   1 
ATOM   4097 O  OG1  . THR   A 1 528 ? -6.918  -25.387 28.480 1.00 27.74 ? 531  THR   A OG1  1 
ATOM   4098 C  CG2  . THR   A 1 528 ? -6.854  -23.111 29.253 1.00 28.11 ? 531  THR   A CG2  1 
ATOM   4099 N  N    . ASN   A 1 529 ? -4.785  -22.146 26.338 1.00 29.11 ? 532  ASN   A N    1 
ATOM   4100 C  CA   . ASN   A 1 529 ? -4.191  -20.851 26.021 1.00 28.02 ? 532  ASN   A CA   1 
ATOM   4101 C  C    . ASN   A 1 529 ? -4.778  -20.263 24.743 1.00 31.55 ? 532  ASN   A C    1 
ATOM   4102 O  O    . ASN   A 1 529 ? -5.094  -19.069 24.688 1.00 35.38 ? 532  ASN   A O    1 
ATOM   4103 C  CB   . ASN   A 1 529 ? -2.682  -20.978 25.892 1.00 31.36 ? 532  ASN   A CB   1 
ATOM   4104 C  CG   . ASN   A 1 529 ? -2.039  -19.657 25.536 1.00 43.93 ? 532  ASN   A CG   1 
ATOM   4105 O  OD1  . ASN   A 1 529 ? -2.133  -18.696 26.299 1.00 41.45 ? 532  ASN   A OD1  1 
ATOM   4106 N  ND2  . ASN   A 1 529 ? -1.419  -19.586 24.356 1.00 43.90 ? 532  ASN   A ND2  1 
ATOM   4107 N  N    . LEU   A 1 530 ? -4.918  -21.082 23.697 1.00 28.81 ? 533  LEU   A N    1 
ATOM   4108 C  CA   . LEU   A 1 530 ? -5.431  -20.569 22.429 1.00 31.10 ? 533  LEU   A CA   1 
ATOM   4109 C  C    . LEU   A 1 530 ? -6.873  -20.094 22.570 1.00 34.10 ? 533  LEU   A C    1 
ATOM   4110 O  O    . LEU   A 1 530 ? -7.232  -19.013 22.083 1.00 39.13 ? 533  LEU   A O    1 
ATOM   4111 C  CB   . LEU   A 1 530 ? -5.292  -21.630 21.328 1.00 27.30 ? 533  LEU   A CB   1 
ATOM   4112 C  CG   . LEU   A 1 530 ? -5.782  -21.304 19.904 1.00 30.88 ? 533  LEU   A CG   1 
ATOM   4113 C  CD1  . LEU   A 1 530 ? -5.103  -22.180 18.888 1.00 29.49 ? 533  LEU   A CD1  1 
ATOM   4114 C  CD2  . LEU   A 1 530 ? -7.299  -21.506 19.769 1.00 32.43 ? 533  LEU   A CD2  1 
ATOM   4115 N  N    . PHE   A 1 531 ? -7.724  -20.888 23.227 1.00 29.67 ? 534  PHE   A N    1 
ATOM   4116 C  CA   . PHE   A 1 531 ? -9.122  -20.500 23.361 1.00 31.38 ? 534  PHE   A CA   1 
ATOM   4117 C  C    . PHE   A 1 531 ? -9.311  -19.347 24.340 1.00 39.60 ? 534  PHE   A C    1 
ATOM   4118 O  O    . PHE   A 1 531 ? -10.379 -18.724 24.340 1.00 38.69 ? 534  PHE   A O    1 
ATOM   4119 C  CB   . PHE   A 1 531 ? -9.959  -21.701 23.787 1.00 28.20 ? 534  PHE   A CB   1 
ATOM   4120 C  CG   . PHE   A 1 531 ? -10.251 -22.655 22.666 1.00 28.11 ? 534  PHE   A CG   1 
ATOM   4121 C  CD1  . PHE   A 1 531 ? -10.811 -22.201 21.483 1.00 34.39 ? 534  PHE   A CD1  1 
ATOM   4122 C  CD2  . PHE   A 1 531 ? -9.980  -24.005 22.796 1.00 31.19 ? 534  PHE   A CD2  1 
ATOM   4123 C  CE1  . PHE   A 1 531 ? -11.093 -23.077 20.444 1.00 32.38 ? 534  PHE   A CE1  1 
ATOM   4124 C  CE2  . PHE   A 1 531 ? -10.262 -24.891 21.764 1.00 28.21 ? 534  PHE   A CE2  1 
ATOM   4125 C  CZ   . PHE   A 1 531 ? -10.816 -24.424 20.583 1.00 26.98 ? 534  PHE   A CZ   1 
ATOM   4126 N  N    . ALA   A 1 532 ? -8.313  -19.058 25.184 1.00 36.65 ? 535  ALA   A N    1 
ATOM   4127 C  CA   . ALA   A 1 532 ? -8.383  -17.849 25.996 1.00 39.92 ? 535  ALA   A CA   1 
ATOM   4128 C  C    . ALA   A 1 532 ? -8.215  -16.600 25.147 1.00 48.21 ? 535  ALA   A C    1 
ATOM   4129 O  O    . ALA   A 1 532 ? -8.555  -15.504 25.607 1.00 55.37 ? 535  ALA   A O    1 
ATOM   4130 C  CB   . ALA   A 1 532 ? -7.329  -17.881 27.103 1.00 36.22 ? 535  ALA   A CB   1 
ATOM   4131 N  N    . LYS   A 1 533 ? -7.684  -16.753 23.932 1.00 54.27 ? 536  LYS   A N    1 
ATOM   4132 C  CA   . LYS   A 1 533 ? -7.668  -15.724 22.891 1.00 59.90 ? 536  LYS   A CA   1 
ATOM   4133 C  C    . LYS   A 1 533 ? -6.666  -14.617 23.189 1.00 66.86 ? 536  LYS   A C    1 
ATOM   4134 O  O    . LYS   A 1 533 ? -6.492  -14.211 24.337 1.00 74.03 ? 536  LYS   A O    1 
ATOM   4135 C  CB   . LYS   A 1 533 ? -9.075  -15.137 22.699 1.00 63.86 ? 536  LYS   A CB   1 
ATOM   4136 C  CG   . LYS   A 1 533 ? -9.266  -14.360 21.411 1.00 74.58 ? 536  LYS   A CG   1 
ATOM   4137 C  CD   . LYS   A 1 533 ? -10.444 -13.400 21.523 1.00 81.94 ? 536  LYS   A CD   1 
ATOM   4138 C  CE   . LYS   A 1 533 ? -10.457 -12.407 20.371 1.00 90.15 ? 536  LYS   A CE   1 
ATOM   4139 N  NZ   . LYS   A 1 533 ? -11.383 -11.267 20.618 1.00 88.16 ? 536  LYS   A NZ   1 
HETATM 4140 C  C01  . A1EIY B 2 .   ? -20.487 -37.599 18.759 0.87 21.22 ? 601  A1EIY A C01  1 
HETATM 4141 C  C02  . A1EIY B 2 .   ? -20.210 -36.391 18.152 0.63 25.10 ? 601  A1EIY A C02  1 
HETATM 4142 C  C03  . A1EIY B 2 .   ? -20.487 -36.194 16.810 1.00 27.16 ? 601  A1EIY A C03  1 
HETATM 4143 C  C04  . A1EIY B 2 .   ? -21.048 -37.210 16.062 0.97 29.12 ? 601  A1EIY A C04  1 
HETATM 4144 C  C05  . A1EIY B 2 .   ? -21.329 -38.419 16.669 1.00 21.54 ? 601  A1EIY A C05  1 
HETATM 4145 C  C06  . A1EIY B 2 .   ? -21.054 -38.628 18.019 0.95 19.05 ? 601  A1EIY A C06  1 
HETATM 4146 C  C07  . A1EIY B 2 .   ? -21.338 -39.956 18.688 0.68 17.49 ? 601  A1EIY A C07  1 
HETATM 4147 C  C09  . A1EIY B 2 .   ? -21.322 -41.092 17.676 0.64 18.71 ? 601  A1EIY A C09  1 
HETATM 4148 F  F10  . A1EIY B 2 .   ? -22.304 -40.976 16.775 0.92 20.30 ? 601  A1EIY A F10  1 
HETATM 4149 F  F11  . A1EIY B 2 .   ? -20.170 -41.099 16.997 0.90 22.96 ? 601  A1EIY A F11  1 
HETATM 4150 F  F12  . A1EIY B 2 .   ? -21.454 -42.294 18.249 0.91 20.88 ? 601  A1EIY A F12  1 
HETATM 4151 O  O08  . A1EIY B 2 .   ? -22.567 -39.861 19.367 1.00 16.33 ? 601  A1EIY A O08  1 
HETATM 4152 CL CL13 . A1EIY B 2 .   ? -19.516 -35.143 19.101 0.57 38.66 ? 601  A1EIY A CL13 1 
HETATM 4153 CL CL14 . A1EIY B 2 .   ? -20.144 -34.683 16.052 0.36 56.95 ? 601  A1EIY A CL14 1 
HETATM 4154 MG MG   . MG    C 3 .   ? -24.507 -23.664 5.231  1.00 17.85 ? 602  MG    A MG   1 
HETATM 4155 O  O    . HOH   D 4 .   ? -38.738 -70.683 28.882 1.00 45.31 ? 701  HOH   A O    1 
HETATM 4156 O  O    . HOH   D 4 .   ? -2.765  -17.265 16.600 1.00 38.56 ? 702  HOH   A O    1 
HETATM 4157 O  O    . HOH   D 4 .   ? -25.886 -26.840 15.516 1.00 46.46 ? 703  HOH   A O    1 
HETATM 4158 O  O    . HOH   D 4 .   ? -25.023 -22.718 40.473 1.00 39.75 ? 704  HOH   A O    1 
HETATM 4159 O  O    . HOH   D 4 .   ? -10.551 -68.461 22.991 1.00 33.18 ? 705  HOH   A O    1 
HETATM 4160 O  O    . HOH   D 4 .   ? -50.733 -19.190 11.524 1.00 43.27 ? 706  HOH   A O    1 
HETATM 4161 O  O    . HOH   D 4 .   ? -4.353  -44.404 9.103  1.00 38.27 ? 707  HOH   A O    1 
HETATM 4162 O  O    . HOH   D 4 .   ? 1.973   -54.370 30.673 1.00 48.24 ? 708  HOH   A O    1 
HETATM 4163 O  O    . HOH   D 4 .   ? 5.222   -40.915 35.119 1.00 25.35 ? 709  HOH   A O    1 
HETATM 4164 O  O    . HOH   D 4 .   ? -44.463 -42.956 14.748 1.00 26.41 ? 710  HOH   A O    1 
HETATM 4165 O  O    . HOH   D 4 .   ? -50.981 -37.061 29.495 1.00 37.65 ? 711  HOH   A O    1 
HETATM 4166 O  O    . HOH   D 4 .   ? -21.454 -18.993 38.462 1.00 44.00 ? 712  HOH   A O    1 
HETATM 4167 O  O    . HOH   D 4 .   ? -20.721 -25.369 22.362 1.00 32.79 ? 713  HOH   A O    1 
HETATM 4168 O  O    . HOH   D 4 .   ? -0.900  -42.446 26.326 1.00 32.60 ? 714  HOH   A O    1 
HETATM 4169 O  O    . HOH   D 4 .   ? -35.654 -52.348 47.147 1.00 45.25 ? 715  HOH   A O    1 
HETATM 4170 O  O    . HOH   D 4 .   ? -24.112 -19.038 4.557  1.00 37.78 ? 716  HOH   A O    1 
HETATM 4171 O  O    . HOH   D 4 .   ? -20.681 -54.410 14.409 1.00 22.25 ? 717  HOH   A O    1 
HETATM 4172 O  O    . HOH   D 4 .   ? -9.555  -38.988 41.749 1.00 27.30 ? 718  HOH   A O    1 
HETATM 4173 O  O    . HOH   D 4 .   ? -11.343 -62.624 12.405 1.00 48.69 ? 719  HOH   A O    1 
HETATM 4174 O  O    . HOH   D 4 .   ? -27.107 -35.725 6.724  1.00 28.61 ? 720  HOH   A O    1 
HETATM 4175 O  O    . HOH   D 4 .   ? -24.874 -30.921 8.918  1.00 30.44 ? 721  HOH   A O    1 
HETATM 4176 O  O    . HOH   D 4 .   ? -38.554 -45.322 44.226 1.00 38.98 ? 722  HOH   A O    1 
HETATM 4177 O  O    . HOH   D 4 .   ? -31.092 -58.532 22.504 1.00 25.98 ? 723  HOH   A O    1 
HETATM 4178 O  O    . HOH   D 4 .   ? -8.698  -67.940 20.715 1.00 39.32 ? 724  HOH   A O    1 
HETATM 4179 O  O    . HOH   D 4 .   ? -47.492 -33.845 17.764 1.00 26.79 ? 725  HOH   A O    1 
HETATM 4180 O  O    . HOH   D 4 .   ? -2.463  -40.987 39.706 1.00 24.06 ? 726  HOH   A O    1 
HETATM 4181 O  O    . HOH   D 4 .   ? -27.199 -65.875 33.887 1.00 24.43 ? 727  HOH   A O    1 
HETATM 4182 O  O    . HOH   D 4 .   ? -22.394 -31.486 44.554 1.00 46.70 ? 728  HOH   A O    1 
HETATM 4183 O  O    . HOH   D 4 .   ? -12.777 -52.700 42.667 1.00 22.35 ? 729  HOH   A O    1 
HETATM 4184 O  O    . HOH   D 4 .   ? -15.226 -67.395 15.605 1.00 44.84 ? 730  HOH   A O    1 
HETATM 4185 O  O    . HOH   D 4 .   ? -17.507 -25.890 25.568 1.00 44.84 ? 731  HOH   A O    1 
HETATM 4186 O  O    . HOH   D 4 .   ? -25.320 -19.531 31.857 1.00 38.50 ? 732  HOH   A O    1 
HETATM 4187 O  O    . HOH   D 4 .   ? -13.736 -44.666 24.784 1.00 15.16 ? 733  HOH   A O    1 
HETATM 4188 O  O    . HOH   D 4 .   ? -27.997 -72.132 30.301 1.00 41.75 ? 734  HOH   A O    1 
HETATM 4189 O  O    . HOH   D 4 .   ? -43.473 -36.004 4.126  1.00 37.33 ? 735  HOH   A O    1 
HETATM 4190 O  O    . HOH   D 4 .   ? -39.742 -16.124 16.393 1.00 34.07 ? 736  HOH   A O    1 
HETATM 4191 O  O    . HOH   D 4 .   ? -2.274  -35.148 20.126 1.00 29.84 ? 737  HOH   A O    1 
HETATM 4192 O  O    . HOH   D 4 .   ? -34.929 -50.307 19.463 1.00 14.45 ? 738  HOH   A O    1 
HETATM 4193 O  O    . HOH   D 4 .   ? -25.606 -28.785 38.708 1.00 21.85 ? 739  HOH   A O    1 
HETATM 4194 O  O    . HOH   D 4 .   ? -49.227 -40.779 32.788 1.00 28.54 ? 740  HOH   A O    1 
HETATM 4195 O  O    . HOH   D 4 .   ? -50.454 -56.241 34.924 1.00 22.22 ? 741  HOH   A O    1 
HETATM 4196 O  O    . HOH   D 4 .   ? -40.186 -63.375 38.161 1.00 35.41 ? 742  HOH   A O    1 
HETATM 4197 O  O    . HOH   D 4 .   ? -44.317 -23.793 28.408 1.00 32.60 ? 743  HOH   A O    1 
HETATM 4198 O  O    . HOH   D 4 .   ? -18.898 -55.938 12.899 1.00 35.32 ? 744  HOH   A O    1 
HETATM 4199 O  O    . HOH   D 4 .   ? -47.577 -36.792 6.335  1.00 30.21 ? 745  HOH   A O    1 
HETATM 4200 O  O    . HOH   D 4 .   ? -48.761 -29.560 24.330 1.00 31.29 ? 746  HOH   A O    1 
HETATM 4201 O  O    . HOH   D 4 .   ? -23.949 -65.088 18.599 1.00 36.81 ? 747  HOH   A O    1 
HETATM 4202 O  O    . HOH   D 4 .   ? -4.094  -39.367 13.114 1.00 32.95 ? 748  HOH   A O    1 
HETATM 4203 O  O    . HOH   D 4 .   ? -15.076 -60.419 32.083 1.00 20.93 ? 749  HOH   A O    1 
HETATM 4204 O  O    . HOH   D 4 .   ? -19.660 -20.603 30.146 1.00 30.67 ? 750  HOH   A O    1 
HETATM 4205 O  O    . HOH   D 4 .   ? -15.743 -44.390 21.412 1.00 16.14 ? 751  HOH   A O    1 
HETATM 4206 O  O    . HOH   D 4 .   ? -42.760 -27.626 26.252 1.00 22.70 ? 752  HOH   A O    1 
HETATM 4207 O  O    . HOH   D 4 .   ? -22.837 -37.475 6.057  1.00 30.28 ? 753  HOH   A O    1 
HETATM 4208 O  O    . HOH   D 4 .   ? 3.887   -32.698 35.255 1.00 47.88 ? 754  HOH   A O    1 
HETATM 4209 O  O    . HOH   D 4 .   ? -26.364 -64.113 39.603 1.00 35.61 ? 755  HOH   A O    1 
HETATM 4210 O  O    . HOH   D 4 .   ? -43.688 -48.468 33.040 1.00 27.35 ? 756  HOH   A O    1 
HETATM 4211 O  O    . HOH   D 4 .   ? -54.530 -57.088 35.355 1.00 32.71 ? 757  HOH   A O    1 
HETATM 4212 O  O    . HOH   D 4 .   ? -44.271 -36.714 18.191 1.00 30.48 ? 758  HOH   A O    1 
HETATM 4213 O  O    . HOH   D 4 .   ? -45.376 -33.487 29.712 1.00 26.45 ? 759  HOH   A O    1 
HETATM 4214 O  O    . HOH   D 4 .   ? -12.412 -53.611 21.215 1.00 18.78 ? 760  HOH   A O    1 
HETATM 4215 O  O    . HOH   D 4 .   ? -31.862 -45.979 45.722 1.00 40.15 ? 761  HOH   A O    1 
HETATM 4216 O  O    . HOH   D 4 .   ? -29.100 -65.535 40.558 1.00 32.93 ? 762  HOH   A O    1 
HETATM 4217 O  O    . HOH   D 4 .   ? -29.079 -53.836 9.192  1.00 35.11 ? 763  HOH   A O    1 
HETATM 4218 O  O    . HOH   D 4 .   ? -32.139 -41.124 4.647  1.00 33.71 ? 764  HOH   A O    1 
HETATM 4219 O  O    . HOH   D 4 .   ? -48.081 -47.878 29.422 1.00 22.79 ? 765  HOH   A O    1 
HETATM 4220 O  O    . HOH   D 4 .   ? -26.938 -62.007 20.034 1.00 41.76 ? 766  HOH   A O    1 
HETATM 4221 O  O    . HOH   D 4 .   ? -11.467 -54.026 8.478  1.00 40.02 ? 767  HOH   A O    1 
HETATM 4222 O  O    . HOH   D 4 .   ? -30.535 -34.899 8.444  1.00 20.81 ? 768  HOH   A O    1 
HETATM 4223 O  O    . HOH   D 4 .   ? -26.182 -49.987 5.796  1.00 39.48 ? 769  HOH   A O    1 
HETATM 4224 O  O    . HOH   D 4 .   ? -19.717 -33.934 33.778 1.00 14.58 ? 770  HOH   A O    1 
HETATM 4225 O  O    . HOH   D 4 .   ? -31.618 -45.293 38.797 1.00 13.69 ? 771  HOH   A O    1 
HETATM 4226 O  O    . HOH   D 4 .   ? -26.706 -46.362 47.364 1.00 30.77 ? 772  HOH   A O    1 
HETATM 4227 O  O    . HOH   D 4 .   ? -33.062 -43.370 21.521 1.00 12.00 ? 773  HOH   A O    1 
HETATM 4228 O  O    . HOH   D 4 .   ? -22.926 -45.645 21.237 1.00 17.86 ? 774  HOH   A O    1 
HETATM 4229 O  O    . HOH   D 4 .   ? -9.776  -52.415 4.924  1.00 45.38 ? 775  HOH   A O    1 
HETATM 4230 O  O    . HOH   D 4 .   ? -12.930 -66.632 17.945 1.00 42.15 ? 776  HOH   A O    1 
HETATM 4231 O  O    . HOH   D 4 .   ? -43.972 -30.116 6.510  1.00 35.80 ? 777  HOH   A O    1 
HETATM 4232 O  O    . HOH   D 4 .   ? -19.182 -34.018 47.426 1.00 25.95 ? 778  HOH   A O    1 
HETATM 4233 O  O    . HOH   D 4 .   ? -28.130 -25.562 7.853  1.00 53.32 ? 779  HOH   A O    1 
HETATM 4234 O  O    . HOH   D 4 .   ? -7.636  -26.000 30.960 1.00 28.99 ? 780  HOH   A O    1 
HETATM 4235 O  O    . HOH   D 4 .   ? -19.766 -67.069 23.725 1.00 27.84 ? 781  HOH   A O    1 
HETATM 4236 O  O    . HOH   D 4 .   ? -19.422 -26.049 8.297  1.00 30.55 ? 782  HOH   A O    1 
HETATM 4237 O  O    . HOH   D 4 .   ? -30.691 -53.846 23.797 1.00 14.44 ? 783  HOH   A O    1 
HETATM 4238 O  O    . HOH   D 4 .   ? -4.000  -35.719 32.274 1.00 18.37 ? 784  HOH   A O    1 
HETATM 4239 O  O    . HOH   D 4 .   ? -15.439 -64.346 18.218 1.00 29.00 ? 785  HOH   A O    1 
HETATM 4240 O  O    . HOH   D 4 .   ? -28.088 -14.449 17.475 1.00 44.46 ? 786  HOH   A O    1 
HETATM 4241 O  O    . HOH   D 4 .   ? -15.169 -27.246 25.086 1.00 31.66 ? 787  HOH   A O    1 
HETATM 4242 O  O    . HOH   D 4 .   ? -23.082 -65.129 35.601 1.00 28.77 ? 788  HOH   A O    1 
HETATM 4243 O  O    . HOH   D 4 .   ? -23.506 -50.165 39.469 1.00 17.53 ? 789  HOH   A O    1 
HETATM 4244 O  O    . HOH   D 4 .   ? -43.162 -51.011 34.172 1.00 33.24 ? 790  HOH   A O    1 
HETATM 4245 O  O    . HOH   D 4 .   ? -15.249 -63.128 31.302 1.00 21.95 ? 791  HOH   A O    1 
HETATM 4246 O  O    . HOH   D 4 .   ? -13.824 -41.484 13.998 1.00 17.98 ? 792  HOH   A O    1 
HETATM 4247 O  O    . HOH   D 4 .   ? -7.048  -43.086 36.154 1.00 13.91 ? 793  HOH   A O    1 
HETATM 4248 O  O    . HOH   D 4 .   ? -9.868  -67.280 18.284 1.00 40.23 ? 794  HOH   A O    1 
HETATM 4249 O  O    . HOH   D 4 .   ? -22.984 -57.971 26.100 1.00 14.86 ? 795  HOH   A O    1 
HETATM 4250 O  O    . HOH   D 4 .   ? -45.342 -24.954 24.318 1.00 28.90 ? 796  HOH   A O    1 
HETATM 4251 O  O    . HOH   D 4 .   ? -25.745 -26.703 8.688  1.00 29.80 ? 797  HOH   A O    1 
HETATM 4252 O  O    . HOH   D 4 .   ? -4.558  -30.889 0.005  1.00 39.78 ? 798  HOH   A O    1 
HETATM 4253 O  O    . HOH   D 4 .   ? -14.063 -25.911 32.534 1.00 29.45 ? 799  HOH   A O    1 
HETATM 4254 O  O    . HOH   D 4 .   ? -2.175  -22.892 28.851 1.00 39.67 ? 800  HOH   A O    1 
HETATM 4255 O  O    . HOH   D 4 .   ? -32.693 -24.029 18.865 1.00 30.77 ? 801  HOH   A O    1 
HETATM 4256 O  O    . HOH   D 4 .   ? -29.390 -46.609 14.920 1.00 20.97 ? 802  HOH   A O    1 
HETATM 4257 O  O    . HOH   D 4 .   ? -41.809 -55.890 23.464 1.00 27.28 ? 803  HOH   A O    1 
HETATM 4258 O  O    . HOH   D 4 .   ? -40.937 -34.557 21.412 1.00 14.51 ? 804  HOH   A O    1 
HETATM 4259 O  O    . HOH   D 4 .   ? -18.352 -70.037 27.563 1.00 37.74 ? 805  HOH   A O    1 
HETATM 4260 O  O    . HOH   D 4 .   ? 3.880   -31.313 13.142 1.00 34.73 ? 806  HOH   A O    1 
HETATM 4261 O  O    . HOH   D 4 .   ? -9.839  -42.582 -1.457 1.00 33.29 ? 807  HOH   A O    1 
HETATM 4262 O  O    . HOH   D 4 .   ? -32.850 -15.910 12.744 1.00 41.86 ? 808  HOH   A O    1 
HETATM 4263 O  O    . HOH   D 4 .   ? -25.240 -34.529 44.396 1.00 32.58 ? 809  HOH   A O    1 
HETATM 4264 O  O    . HOH   D 4 .   ? -27.176 -66.015 38.186 1.00 36.25 ? 810  HOH   A O    1 
HETATM 4265 O  O    . HOH   D 4 .   ? -31.238 -59.304 11.760 1.00 47.15 ? 811  HOH   A O    1 
HETATM 4266 O  O    . HOH   D 4 .   ? -16.652 -34.449 46.948 1.00 24.87 ? 812  HOH   A O    1 
HETATM 4267 O  O    . HOH   D 4 .   ? -28.897 -47.070 25.040 1.00 11.74 ? 813  HOH   A O    1 
HETATM 4268 O  O    . HOH   D 4 .   ? -49.001 -43.859 35.649 1.00 29.26 ? 814  HOH   A O    1 
HETATM 4269 O  O    . HOH   D 4 .   ? -24.267 -27.619 18.368 1.00 35.94 ? 815  HOH   A O    1 
HETATM 4270 O  O    . HOH   D 4 .   ? -42.313 -23.156 32.362 1.00 24.12 ? 816  HOH   A O    1 
HETATM 4271 O  O    . HOH   D 4 .   ? -36.366 -28.659 29.513 1.00 16.36 ? 817  HOH   A O    1 
HETATM 4272 O  O    . HOH   D 4 .   ? -34.379 -27.860 37.828 1.00 25.31 ? 818  HOH   A O    1 
HETATM 4273 O  O    . HOH   D 4 .   ? -39.993 -42.718 35.135 1.00 22.10 ? 819  HOH   A O    1 
HETATM 4274 O  O    . HOH   D 4 .   ? -21.546 -42.727 4.904  1.00 41.59 ? 820  HOH   A O    1 
HETATM 4275 O  O    . HOH   D 4 .   ? -15.373 -48.064 15.564 1.00 23.55 ? 821  HOH   A O    1 
HETATM 4276 O  O    . HOH   D 4 .   ? -16.918 -30.544 19.570 1.00 18.18 ? 822  HOH   A O    1 
HETATM 4277 O  O    . HOH   D 4 .   ? -35.356 -21.834 28.875 1.00 19.64 ? 823  HOH   A O    1 
HETATM 4278 O  O    . HOH   D 4 .   ? 2.326   -36.729 37.386 1.00 30.65 ? 824  HOH   A O    1 
HETATM 4279 O  O    . HOH   D 4 .   ? -3.743  -59.404 40.850 1.00 54.83 ? 825  HOH   A O    1 
HETATM 4280 O  O    . HOH   D 4 .   ? -42.913 -44.176 23.700 1.00 13.74 ? 826  HOH   A O    1 
HETATM 4281 O  O    . HOH   D 4 .   ? -41.148 -48.929 43.578 1.00 28.10 ? 827  HOH   A O    1 
HETATM 4282 O  O    . HOH   D 4 .   ? -14.142 -51.207 14.889 1.00 34.88 ? 828  HOH   A O    1 
HETATM 4283 O  O    . HOH   D 4 .   ? -0.634  -50.729 35.561 1.00 22.15 ? 829  HOH   A O    1 
HETATM 4284 O  O    . HOH   D 4 .   ? -37.681 -16.017 22.778 1.00 36.28 ? 830  HOH   A O    1 
HETATM 4285 O  O    . HOH   D 4 .   ? -34.782 -66.279 36.234 1.00 23.67 ? 831  HOH   A O    1 
HETATM 4286 O  O    . HOH   D 4 .   ? -43.466 -54.620 25.259 1.00 36.37 ? 832  HOH   A O    1 
HETATM 4287 O  O    . HOH   D 4 .   ? -44.346 -68.008 31.919 1.00 43.68 ? 833  HOH   A O    1 
HETATM 4288 O  O    . HOH   D 4 .   ? -47.548 -48.695 21.864 1.00 18.70 ? 834  HOH   A O    1 
HETATM 4289 O  O    . HOH   D 4 .   ? -27.582 -40.113 19.977 1.00 12.93 ? 835  HOH   A O    1 
HETATM 4290 O  O    . HOH   D 4 .   ? -38.980 -69.633 35.135 1.00 41.29 ? 836  HOH   A O    1 
HETATM 4291 O  O    . HOH   D 4 .   ? -39.241 -60.784 40.225 1.00 27.39 ? 837  HOH   A O    1 
HETATM 4292 O  O    . HOH   D 4 .   ? -21.407 -23.296 13.513 1.00 31.65 ? 838  HOH   A O    1 
HETATM 4293 O  O    . HOH   D 4 .   ? -19.842 -23.996 5.351  1.00 31.22 ? 839  HOH   A O    1 
HETATM 4294 O  O    . HOH   D 4 .   ? -12.673 -26.663 2.696  1.00 46.88 ? 840  HOH   A O    1 
HETATM 4295 O  O    . HOH   D 4 .   ? -14.039 -47.778 13.038 1.00 24.66 ? 841  HOH   A O    1 
HETATM 4296 O  O    . HOH   D 4 .   ? -43.277 -44.710 33.792 1.00 20.38 ? 842  HOH   A O    1 
HETATM 4297 O  O    . HOH   D 4 .   ? -32.462 -28.977 23.223 1.00 12.83 ? 843  HOH   A O    1 
HETATM 4298 O  O    . HOH   D 4 .   ? -9.001  -42.197 7.618  1.00 38.62 ? 844  HOH   A O    1 
HETATM 4299 O  O    . HOH   D 4 .   ? 3.357   -51.184 27.136 1.00 33.89 ? 845  HOH   A O    1 
HETATM 4300 O  O    . HOH   D 4 .   ? -2.128  -49.976 24.972 1.00 26.27 ? 846  HOH   A O    1 
HETATM 4301 O  O    . HOH   D 4 .   ? -3.210  -17.680 14.100 1.00 34.59 ? 847  HOH   A O    1 
HETATM 4302 O  O    . HOH   D 4 .   ? -19.069 -26.232 18.600 1.00 37.27 ? 848  HOH   A O    1 
HETATM 4303 O  O    . HOH   D 4 .   ? -27.516 -47.546 17.079 1.00 17.09 ? 849  HOH   A O    1 
HETATM 4304 O  O    . HOH   D 4 .   ? -51.919 -55.558 28.786 1.00 29.10 ? 850  HOH   A O    1 
HETATM 4305 O  O    . HOH   D 4 .   ? -26.117 -46.068 18.839 1.00 15.98 ? 851  HOH   A O    1 
HETATM 4306 O  O    . HOH   D 4 .   ? -23.648 -47.797 45.108 1.00 25.41 ? 852  HOH   A O    1 
HETATM 4307 O  O    . HOH   D 4 .   ? -25.221 -63.698 41.953 1.00 42.48 ? 853  HOH   A O    1 
HETATM 4308 O  O    . HOH   D 4 .   ? -12.151 -57.087 22.558 1.00 15.45 ? 854  HOH   A O    1 
HETATM 4309 O  O    . HOH   D 4 .   ? 1.704   -27.194 25.646 1.00 33.91 ? 855  HOH   A O    1 
HETATM 4310 O  O    . HOH   D 4 .   ? -2.437  -45.553 24.592 1.00 33.29 ? 856  HOH   A O    1 
HETATM 4311 O  O    . HOH   D 4 .   ? -51.509 -52.549 36.436 1.00 24.90 ? 857  HOH   A O    1 
HETATM 4312 O  O    . HOH   D 4 .   ? -43.209 -45.639 26.092 1.00 14.14 ? 858  HOH   A O    1 
HETATM 4313 O  O    . HOH   D 4 .   ? -44.638 -38.640 27.699 1.00 16.77 ? 859  HOH   A O    1 
HETATM 4314 O  O    . HOH   D 4 .   ? 3.981   -46.235 31.991 1.00 23.72 ? 860  HOH   A O    1 
HETATM 4315 O  O    . HOH   D 4 .   ? -30.330 -52.856 15.705 1.00 30.78 ? 861  HOH   A O    1 
HETATM 4316 O  O    . HOH   D 4 .   ? -32.836 -61.254 19.052 1.00 37.34 ? 862  HOH   A O    1 
HETATM 4317 O  O    . HOH   D 4 .   ? -43.144 -44.626 11.794 1.00 27.91 ? 863  HOH   A O    1 
HETATM 4318 O  O    . HOH   D 4 .   ? -22.809 -23.090 6.661  1.00 26.05 ? 864  HOH   A O    1 
HETATM 4319 O  O    . HOH   D 4 .   ? -34.314 -57.741 44.564 1.00 30.86 ? 865  HOH   A O    1 
HETATM 4320 O  O    . HOH   D 4 .   ? -47.312 -37.273 17.278 1.00 26.66 ? 866  HOH   A O    1 
HETATM 4321 O  O    . HOH   D 4 .   ? -1.790  -21.576 22.443 1.00 30.40 ? 867  HOH   A O    1 
HETATM 4322 O  O    . HOH   D 4 .   ? -32.499 -65.657 34.575 1.00 25.74 ? 868  HOH   A O    1 
HETATM 4323 O  O    . HOH   D 4 .   ? -40.172 -30.056 4.877  1.00 30.58 ? 869  HOH   A O    1 
HETATM 4324 O  O    . HOH   D 4 .   ? -34.492 -69.271 36.806 1.00 34.35 ? 870  HOH   A O    1 
HETATM 4325 O  O    . HOH   D 4 .   ? -19.521 -62.195 13.311 1.00 41.03 ? 871  HOH   A O    1 
HETATM 4326 O  O    . HOH   D 4 .   ? -2.489  -46.017 42.533 1.00 37.12 ? 872  HOH   A O    1 
HETATM 4327 O  O    . HOH   D 4 .   ? 1.487   -22.467 16.287 1.00 39.15 ? 873  HOH   A O    1 
HETATM 4328 O  O    . HOH   D 4 .   ? -30.203 -43.393 45.246 1.00 35.71 ? 874  HOH   A O    1 
HETATM 4329 O  O    . HOH   D 4 .   ? -38.040 -68.134 27.420 1.00 28.13 ? 875  HOH   A O    1 
HETATM 4330 O  O    . HOH   D 4 .   ? -27.754 -40.365 5.521  1.00 29.74 ? 876  HOH   A O    1 
HETATM 4331 O  O    . HOH   D 4 .   ? -1.027  -60.059 23.138 1.00 35.44 ? 877  HOH   A O    1 
HETATM 4332 O  O    . HOH   D 4 .   ? -7.483  -46.918 42.715 1.00 29.14 ? 878  HOH   A O    1 
HETATM 4333 O  O    . HOH   D 4 .   ? -3.085  -52.644 21.470 1.00 28.10 ? 879  HOH   A O    1 
HETATM 4334 O  O    . HOH   D 4 .   ? 0.504   -48.942 25.334 1.00 34.31 ? 880  HOH   A O    1 
HETATM 4335 O  O    . HOH   D 4 .   ? -12.696 -56.181 20.038 1.00 22.66 ? 881  HOH   A O    1 
HETATM 4336 O  O    . HOH   D 4 .   ? -0.159  -42.373 38.984 1.00 23.15 ? 882  HOH   A O    1 
HETATM 4337 O  O    . HOH   D 4 .   ? -35.770 -47.835 10.157 1.00 31.00 ? 883  HOH   A O    1 
HETATM 4338 O  O    . HOH   D 4 .   ? -34.956 -25.009 37.629 1.00 33.46 ? 884  HOH   A O    1 
HETATM 4339 O  O    . HOH   D 4 .   ? -14.888 -24.112 34.377 1.00 24.60 ? 885  HOH   A O    1 
HETATM 4340 O  O    . HOH   D 4 .   ? -42.136 -20.325 6.567  1.00 38.89 ? 886  HOH   A O    1 
HETATM 4341 O  O    . HOH   D 4 .   ? -1.203  -37.801 26.096 1.00 26.61 ? 887  HOH   A O    1 
HETATM 4342 O  O    . HOH   D 4 .   ? -41.155 -65.681 26.059 1.00 30.49 ? 888  HOH   A O    1 
HETATM 4343 O  O    . HOH   D 4 .   ? -27.997 -38.153 8.989  1.00 28.94 ? 889  HOH   A O    1 
HETATM 4344 O  O    . HOH   D 4 .   ? -10.408 -36.485 43.820 1.00 27.73 ? 890  HOH   A O    1 
HETATM 4345 O  O    . HOH   D 4 .   ? -41.395 -53.045 40.854 1.00 28.12 ? 891  HOH   A O    1 
HETATM 4346 O  O    . HOH   D 4 .   ? -8.096  -39.334 20.008 1.00 22.99 ? 892  HOH   A O    1 
HETATM 4347 O  O    . HOH   D 4 .   ? -34.624 -34.962 13.794 1.00 17.59 ? 893  HOH   A O    1 
HETATM 4348 O  O    . HOH   D 4 .   ? -28.377 -22.807 25.296 1.00 26.36 ? 894  HOH   A O    1 
HETATM 4349 O  O    . HOH   D 4 .   ? -50.575 -38.067 23.350 1.00 35.54 ? 895  HOH   A O    1 
HETATM 4350 O  O    . HOH   D 4 .   ? -48.215 -50.662 41.736 1.00 42.93 ? 896  HOH   A O    1 
HETATM 4351 O  O    . HOH   D 4 .   ? -11.893 -19.628 18.744 1.00 35.53 ? 897  HOH   A O    1 
HETATM 4352 O  O    . HOH   D 4 .   ? -54.117 -53.264 29.867 1.00 17.47 ? 898  HOH   A O    1 
HETATM 4353 O  O    . HOH   D 4 .   ? -26.683 -68.997 30.154 1.00 26.56 ? 899  HOH   A O    1 
HETATM 4354 O  O    . HOH   D 4 .   ? -15.528 -66.520 21.878 1.00 31.06 ? 900  HOH   A O    1 
HETATM 4355 O  O    . HOH   D 4 .   ? -9.459  -21.204 27.655 1.00 31.28 ? 901  HOH   A O    1 
HETATM 4356 O  O    . HOH   D 4 .   ? -4.921  -39.882 21.435 1.00 28.69 ? 902  HOH   A O    1 
HETATM 4357 O  O    . HOH   D 4 .   ? -23.920 -69.762 23.253 1.00 38.71 ? 903  HOH   A O    1 
HETATM 4358 O  O    . HOH   D 4 .   ? -24.897 -54.076 44.482 1.00 29.64 ? 904  HOH   A O    1 
HETATM 4359 O  O    . HOH   D 4 .   ? -16.210 -20.577 3.729  1.00 38.42 ? 905  HOH   A O    1 
HETATM 4360 O  O    . HOH   D 4 .   ? -14.821 -38.952 27.129 1.00 14.96 ? 906  HOH   A O    1 
HETATM 4361 O  O    . HOH   D 4 .   ? -20.104 -32.954 3.323  1.00 31.80 ? 907  HOH   A O    1 
HETATM 4362 O  O    . HOH   D 4 .   ? -19.008 -45.184 45.997 1.00 50.82 ? 908  HOH   A O    1 
HETATM 4363 O  O    . HOH   D 4 .   ? -13.425 -24.818 36.442 1.00 28.15 ? 909  HOH   A O    1 
HETATM 4364 O  O    . HOH   D 4 .   ? -14.364 -59.139 39.789 1.00 29.85 ? 910  HOH   A O    1 
HETATM 4365 O  O    . HOH   D 4 .   ? -5.572  -37.359 19.222 1.00 28.50 ? 911  HOH   A O    1 
HETATM 4366 O  O    . HOH   D 4 .   ? -46.021 -48.215 25.374 1.00 25.58 ? 912  HOH   A O    1 
HETATM 4367 O  O    . HOH   D 4 .   ? -16.139 -31.882 35.412 1.00 23.62 ? 913  HOH   A O    1 
HETATM 4368 O  O    . HOH   D 4 .   ? -17.006 -49.863 14.111 1.00 28.18 ? 914  HOH   A O    1 
HETATM 4369 O  O    . HOH   D 4 .   ? -3.677  -47.363 24.938 1.00 27.19 ? 915  HOH   A O    1 
HETATM 4370 O  O    . HOH   D 4 .   ? -14.268 -64.009 35.184 1.00 36.92 ? 916  HOH   A O    1 
HETATM 4371 O  O    . HOH   D 4 .   ? -2.535  -56.347 18.253 1.00 44.82 ? 917  HOH   A O    1 
HETATM 4372 O  O    . HOH   D 4 .   ? -33.760 -37.756 14.873 1.00 15.75 ? 918  HOH   A O    1 
HETATM 4373 O  O    . HOH   D 4 .   ? -36.559 -38.889 17.562 1.00 14.17 ? 919  HOH   A O    1 
HETATM 4374 O  O    . HOH   D 4 .   ? -34.235 -22.828 26.371 1.00 23.20 ? 920  HOH   A O    1 
HETATM 4375 O  O    . HOH   D 4 .   ? -19.825 -27.099 26.666 1.00 24.86 ? 921  HOH   A O    1 
HETATM 4376 O  O    . HOH   D 4 .   ? -29.909 -60.942 23.619 1.00 26.32 ? 922  HOH   A O    1 
HETATM 4377 O  O    . HOH   D 4 .   ? -42.133 -36.869 20.291 1.00 15.50 ? 923  HOH   A O    1 
HETATM 4378 O  O    . HOH   D 4 .   ? -20.591 -25.635 24.347 1.00 33.09 ? 924  HOH   A O    1 
HETATM 4379 O  O    . HOH   D 4 .   ? 0.433   -54.154 33.353 1.00 35.91 ? 925  HOH   A O    1 
HETATM 4380 O  O    . HOH   D 4 .   ? -19.759 -40.018 5.127  1.00 36.42 ? 926  HOH   A O    1 
HETATM 4381 O  O    . HOH   D 4 .   ? -34.031 -36.928 41.198 1.00 29.00 ? 927  HOH   A O    1 
HETATM 4382 O  O    . HOH   D 4 .   ? -21.735 -58.569 40.484 1.00 19.26 ? 928  HOH   A O    1 
HETATM 4383 O  O    . HOH   D 4 .   ? -15.723 -60.674 38.117 1.00 31.86 ? 929  HOH   A O    1 
HETATM 4384 O  O    . HOH   D 4 .   ? -41.041 -25.803 27.306 1.00 14.71 ? 930  HOH   A O    1 
HETATM 4385 O  O    . HOH   D 4 .   ? 2.897   -48.789 34.194 1.00 28.38 ? 931  HOH   A O    1 
HETATM 4386 O  O    . HOH   D 4 .   ? -41.496 -53.808 21.532 1.00 31.06 ? 932  HOH   A O    1 
HETATM 4387 O  O    . HOH   D 4 .   ? -25.921 -40.527 44.111 1.00 33.23 ? 933  HOH   A O    1 
HETATM 4388 O  O    . HOH   D 4 .   ? -18.137 -33.397 36.505 1.00 23.30 ? 934  HOH   A O    1 
HETATM 4389 O  O    . HOH   D 4 .   ? -40.773 -39.145 19.819 1.00 16.82 ? 935  HOH   A O    1 
HETATM 4390 O  O    . HOH   D 4 .   ? -20.767 -59.835 12.675 1.00 40.47 ? 936  HOH   A O    1 
HETATM 4391 O  O    . HOH   D 4 .   ? -13.879 -16.221 13.222 1.00 39.42 ? 937  HOH   A O    1 
HETATM 4392 O  O    . HOH   D 4 .   ? -24.622 -69.136 35.362 1.00 27.60 ? 938  HOH   A O    1 
HETATM 4393 O  O    . HOH   D 4 .   ? -29.626 -70.318 41.119 1.00 44.57 ? 939  HOH   A O    1 
HETATM 4394 O  O    . HOH   D 4 .   ? -13.347 -24.066 1.895  1.00 37.48 ? 940  HOH   A O    1 
HETATM 4395 O  O    . HOH   D 4 .   ? -23.913 -41.552 7.709  1.00 33.86 ? 941  HOH   A O    1 
HETATM 4396 O  O    . HOH   D 4 .   ? 0.434   -35.700 25.134 1.00 34.93 ? 942  HOH   A O    1 
HETATM 4397 O  O    . HOH   D 4 .   ? -30.591 -20.939 35.971 1.00 36.36 ? 943  HOH   A O    1 
HETATM 4398 O  O    . HOH   D 4 .   ? -6.465  -54.190 39.285 1.00 18.94 ? 944  HOH   A O    1 
HETATM 4399 O  O    . HOH   D 4 .   ? -2.816  -61.147 25.245 1.00 35.66 ? 945  HOH   A O    1 
HETATM 4400 O  O    . HOH   D 4 .   ? -16.800 -64.577 34.065 1.00 34.29 ? 946  HOH   A O    1 
HETATM 4401 O  O    . HOH   D 4 .   ? -46.592 -22.520 24.394 1.00 32.00 ? 947  HOH   A O    1 
HETATM 4402 O  O    . HOH   D 4 .   ? -48.636 -44.961 28.647 1.00 18.95 ? 948  HOH   A O    1 
HETATM 4403 O  O    . HOH   D 4 .   ? -49.842 -31.809 9.090  1.00 35.38 ? 949  HOH   A O    1 
HETATM 4404 O  O    . HOH   D 4 .   ? -33.070 -26.938 18.907 1.00 30.12 ? 950  HOH   A O    1 
HETATM 4405 O  O    . HOH   D 4 .   ? -41.723 -22.116 4.820  1.00 33.33 ? 951  HOH   A O    1 
HETATM 4406 O  O    . HOH   D 4 .   ? -2.496  -28.964 30.968 1.00 20.24 ? 952  HOH   A O    1 
HETATM 4407 O  O    . HOH   D 4 .   ? -49.655 -54.457 27.561 1.00 30.21 ? 953  HOH   A O    1 
HETATM 4408 O  O    . HOH   D 4 .   ? -20.012 -22.695 44.562 1.00 29.78 ? 954  HOH   A O    1 
HETATM 4409 O  O    . HOH   D 4 .   ? -48.745 -25.751 21.187 1.00 27.78 ? 955  HOH   A O    1 
HETATM 4410 O  O    . HOH   D 4 .   ? -33.844 -44.801 19.376 1.00 11.22 ? 956  HOH   A O    1 
HETATM 4411 O  O    . HOH   D 4 .   ? -45.684 -55.493 23.947 1.00 35.87 ? 957  HOH   A O    1 
HETATM 4412 O  O    . HOH   D 4 .   ? -5.730  -59.428 33.122 1.00 42.05 ? 958  HOH   A O    1 
HETATM 4413 O  O    . HOH   D 4 .   ? -7.955  -36.763 21.609 1.00 20.66 ? 959  HOH   A O    1 
HETATM 4414 O  O    . HOH   D 4 .   ? -14.230 -28.560 40.359 1.00 29.96 ? 960  HOH   A O    1 
HETATM 4415 O  O    . HOH   D 4 .   ? -6.891  -59.164 16.822 1.00 44.39 ? 961  HOH   A O    1 
HETATM 4416 O  O    . HOH   D 4 .   ? 3.549   -46.716 29.430 1.00 28.26 ? 962  HOH   A O    1 
HETATM 4417 O  O    . HOH   D 4 .   ? -21.819 -42.557 44.653 1.00 24.62 ? 963  HOH   A O    1 
HETATM 4418 O  O    . HOH   D 4 .   ? -24.907 -39.075 8.573  1.00 35.06 ? 964  HOH   A O    1 
HETATM 4419 O  O    . HOH   D 4 .   ? -37.754 -36.505 33.430 1.00 14.63 ? 965  HOH   A O    1 
HETATM 4420 O  O    . HOH   D 4 .   ? -1.956  -39.767 24.042 1.00 33.96 ? 966  HOH   A O    1 
HETATM 4421 O  O    . HOH   D 4 .   ? -31.640 -38.245 12.256 1.00 15.90 ? 967  HOH   A O    1 
HETATM 4422 O  O    . HOH   D 4 .   ? -14.460 -44.788 44.767 1.00 42.98 ? 968  HOH   A O    1 
HETATM 4423 O  O    . HOH   D 4 .   ? -4.260  -30.371 37.009 1.00 36.69 ? 969  HOH   A O    1 
HETATM 4424 O  O    . HOH   D 4 .   ? -12.387 -66.365 32.564 1.00 38.91 ? 970  HOH   A O    1 
HETATM 4425 O  O    . HOH   D 4 .   ? -42.544 -46.995 37.604 1.00 26.25 ? 971  HOH   A O    1 
HETATM 4426 O  O    . HOH   D 4 .   ? -15.013 -29.490 21.606 1.00 19.10 ? 972  HOH   A O    1 
HETATM 4427 O  O    . HOH   D 4 .   ? -50.244 -51.044 38.256 1.00 31.36 ? 973  HOH   A O    1 
HETATM 4428 O  O    . HOH   D 4 .   ? -12.858 -23.609 13.278 1.00 19.67 ? 974  HOH   A O    1 
HETATM 4429 O  O    . HOH   D 4 .   ? -8.448  -61.182 30.409 1.00 26.05 ? 975  HOH   A O    1 
HETATM 4430 O  O    . HOH   D 4 .   ? -14.238 -60.823 13.469 1.00 36.40 ? 976  HOH   A O    1 
HETATM 4431 O  O    . HOH   D 4 .   ? -27.591 -27.529 36.219 1.00 20.26 ? 977  HOH   A O    1 
HETATM 4432 O  O    . HOH   D 4 .   ? -12.687 -56.012 42.720 1.00 28.82 ? 978  HOH   A O    1 
HETATM 4433 O  O    . HOH   D 4 .   ? -21.572 -26.088 44.438 1.00 32.03 ? 979  HOH   A O    1 
HETATM 4434 O  O    . HOH   D 4 .   ? -48.484 -61.694 27.370 1.00 34.20 ? 980  HOH   A O    1 
HETATM 4435 O  O    . HOH   D 4 .   ? -41.667 -41.497 33.198 1.00 23.89 ? 981  HOH   A O    1 
HETATM 4436 O  O    . HOH   D 4 .   ? -22.198 -25.755 19.787 1.00 40.40 ? 982  HOH   A O    1 
HETATM 4437 O  O    . HOH   D 4 .   ? -51.359 -29.804 19.266 1.00 36.46 ? 983  HOH   A O    1 
HETATM 4438 O  O    . HOH   D 4 .   ? -17.924 -52.304 12.397 1.00 30.90 ? 984  HOH   A O    1 
HETATM 4439 O  O    . HOH   D 4 .   ? -41.844 -59.894 40.344 1.00 31.39 ? 985  HOH   A O    1 
HETATM 4440 O  O    . HOH   D 4 .   ? -10.597 -27.168 39.302 1.00 48.33 ? 986  HOH   A O    1 
HETATM 4441 O  O    . HOH   D 4 .   ? 0.597   -39.172 28.232 1.00 30.99 ? 987  HOH   A O    1 
HETATM 4442 O  O    . HOH   D 4 .   ? -17.673 -55.940 45.569 1.00 41.35 ? 988  HOH   A O    1 
HETATM 4443 O  O    . HOH   D 4 .   ? -28.364 -54.911 16.120 1.00 28.83 ? 989  HOH   A O    1 
HETATM 4444 O  O    . HOH   D 4 .   ? -1.228  -52.088 23.454 1.00 28.03 ? 990  HOH   A O    1 
HETATM 4445 O  O    . HOH   D 4 .   ? -7.782  -55.333 13.234 1.00 36.47 ? 991  HOH   A O    1 
HETATM 4446 O  O    . HOH   D 4 .   ? -11.223 -26.004 33.953 1.00 28.97 ? 992  HOH   A O    1 
HETATM 4447 O  O    . HOH   D 4 .   ? -18.935 -22.243 0.931  1.00 34.61 ? 993  HOH   A O    1 
HETATM 4448 O  O    . HOH   D 4 .   ? -47.149 -56.146 38.735 1.00 35.57 ? 994  HOH   A O    1 
HETATM 4449 O  O    . HOH   D 4 .   ? -14.722 -19.602 19.451 1.00 45.92 ? 995  HOH   A O    1 
HETATM 4450 O  O    . HOH   D 4 .   ? -29.839 -36.705 6.414  1.00 27.49 ? 996  HOH   A O    1 
HETATM 4451 O  O    . HOH   D 4 .   ? -42.936 -16.311 9.256  1.00 32.83 ? 997  HOH   A O    1 
HETATM 4452 O  O    . HOH   D 4 .   ? -18.760 -52.045 47.297 1.00 42.47 ? 998  HOH   A O    1 
HETATM 4453 O  O    . HOH   D 4 .   ? -14.275 -26.655 20.827 1.00 29.27 ? 999  HOH   A O    1 
HETATM 4454 O  O    . HOH   D 4 .   ? -15.639 -56.553 42.344 1.00 26.43 ? 1000 HOH   A O    1 
HETATM 4455 O  O    . HOH   D 4 .   ? -1.421  -37.372 22.377 1.00 40.94 ? 1001 HOH   A O    1 
HETATM 4456 O  O    . HOH   D 4 .   ? -7.283  -49.469 44.080 1.00 31.38 ? 1002 HOH   A O    1 
HETATM 4457 O  O    . HOH   D 4 .   ? -33.205 -48.108 9.497  1.00 29.07 ? 1003 HOH   A O    1 
HETATM 4458 O  O    . HOH   D 4 .   ? -47.423 -21.474 10.712 1.00 30.97 ? 1004 HOH   A O    1 
HETATM 4459 O  O    . HOH   D 4 .   ? -11.724 -28.095 23.223 1.00 25.71 ? 1005 HOH   A O    1 
HETATM 4460 O  O    . HOH   D 4 .   ? -6.930  -28.233 32.859 1.00 25.54 ? 1006 HOH   A O    1 
HETATM 4461 O  O    . HOH   D 4 .   ? -15.538 -49.921 11.902 1.00 29.33 ? 1007 HOH   A O    1 
HETATM 4462 O  O    . HOH   D 4 .   ? -27.015 -38.985 41.088 1.00 28.70 ? 1008 HOH   A O    1 
HETATM 4463 O  O    . HOH   D 4 .   ? -31.228 -18.562 22.830 1.00 33.30 ? 1009 HOH   A O    1 
HETATM 4464 O  O    . HOH   D 4 .   ? -38.070 -52.092 15.824 1.00 22.20 ? 1010 HOH   A O    1 
HETATM 4465 O  O    . HOH   D 4 .   ? -43.605 -50.050 35.896 1.00 26.14 ? 1011 HOH   A O    1 
HETATM 4466 O  O    . HOH   D 4 .   ? -41.397 -66.230 36.300 1.00 33.94 ? 1012 HOH   A O    1 
HETATM 4467 O  O    . HOH   D 4 .   ? -36.278 -51.116 42.493 1.00 17.41 ? 1013 HOH   A O    1 
HETATM 4468 O  O    . HOH   D 4 .   ? -43.219 -45.594 39.992 1.00 33.91 ? 1014 HOH   A O    1 
HETATM 4469 O  O    . HOH   D 4 .   ? -48.490 -57.702 25.256 1.00 29.08 ? 1015 HOH   A O    1 
HETATM 4470 O  O    . HOH   D 4 .   ? -40.825 -38.646 5.178  1.00 34.19 ? 1016 HOH   A O    1 
HETATM 4471 O  O    . HOH   D 4 .   ? -41.486 -15.274 20.587 1.00 24.02 ? 1017 HOH   A O    1 
HETATM 4472 O  O    . HOH   D 4 .   ? -20.153 -53.395 20.275 1.00 24.52 ? 1018 HOH   A O    1 
HETATM 4473 O  O    . HOH   D 4 .   ? 1.662   -27.915 2.654  1.00 40.19 ? 1019 HOH   A O    1 
HETATM 4474 O  O    . HOH   D 4 .   ? 3.402   -33.746 31.301 1.00 40.03 ? 1020 HOH   A O    1 
HETATM 4475 O  O    . HOH   D 4 .   ? -34.749 -60.114 44.860 1.00 34.52 ? 1021 HOH   A O    1 
HETATM 4476 O  O    . HOH   D 4 .   ? -30.695 -51.301 12.526 1.00 29.35 ? 1022 HOH   A O    1 
HETATM 4477 O  O    . HOH   D 4 .   ? -22.015 -26.527 16.229 1.00 32.53 ? 1023 HOH   A O    1 
HETATM 4478 O  O    . HOH   D 4 .   ? -22.614 -29.104 2.200  1.00 29.04 ? 1024 HOH   A O    1 
HETATM 4479 O  O    . HOH   D 4 .   ? -21.319 -37.908 45.786 1.00 28.77 ? 1025 HOH   A O    1 
HETATM 4480 O  O    . HOH   D 4 .   ? -40.075 -47.599 9.980  1.00 34.36 ? 1026 HOH   A O    1 
HETATM 4481 O  O    . HOH   D 4 .   ? -31.709 -21.800 26.055 1.00 28.09 ? 1027 HOH   A O    1 
HETATM 4482 O  O    . HOH   D 4 .   ? -39.312 -53.152 42.656 1.00 35.03 ? 1028 HOH   A O    1 
HETATM 4483 O  O    . HOH   D 4 .   ? -50.701 -32.348 18.036 1.00 33.93 ? 1029 HOH   A O    1 
HETATM 4484 O  O    . HOH   D 4 .   ? -7.205  -25.720 -1.014 1.00 42.24 ? 1030 HOH   A O    1 
HETATM 4485 O  O    . HOH   D 4 .   ? -8.034  -38.864 15.308 1.00 18.53 ? 1031 HOH   A O    1 
HETATM 4486 O  O    . HOH   D 4 .   ? -41.657 -57.503 42.166 1.00 37.87 ? 1032 HOH   A O    1 
HETATM 4487 O  O    . HOH   D 4 .   ? -0.492  -30.356 34.791 1.00 40.08 ? 1033 HOH   A O    1 
HETATM 4488 O  O    . HOH   D 4 .   ? -30.912 -70.063 24.474 1.00 30.60 ? 1034 HOH   A O    1 
HETATM 4489 O  O    . HOH   D 4 .   ? -3.489  -40.348 17.643 1.00 31.84 ? 1035 HOH   A O    1 
HETATM 4490 O  O    . HOH   D 4 .   ? -0.197  -53.971 37.493 1.00 31.12 ? 1036 HOH   A O    1 
HETATM 4491 O  O    . HOH   D 4 .   ? -26.600 -38.125 43.306 1.00 31.02 ? 1037 HOH   A O    1 
HETATM 4492 O  O    . HOH   D 4 .   ? -29.146 -21.259 16.551 1.00 29.15 ? 1038 HOH   A O    1 
HETATM 4493 O  O    . HOH   D 4 .   ? -5.757  -29.158 40.826 1.00 40.84 ? 1039 HOH   A O    1 
HETATM 4494 O  O    . HOH   D 4 .   ? -22.653 -66.652 21.087 1.00 36.28 ? 1040 HOH   A O    1 
HETATM 4495 O  O    . HOH   D 4 .   ? -24.577 -56.764 10.648 1.00 52.15 ? 1041 HOH   A O    1 
HETATM 4496 O  O    . HOH   D 4 .   ? -4.749  -53.694 17.430 1.00 27.64 ? 1042 HOH   A O    1 
HETATM 4497 O  O    . HOH   D 4 .   ? -6.289  -21.596 3.371  1.00 46.95 ? 1043 HOH   A O    1 
HETATM 4498 O  O    . HOH   D 4 .   ? -19.282 -20.166 37.511 1.00 43.48 ? 1044 HOH   A O    1 
HETATM 4499 O  O    . HOH   D 4 .   ? -46.481 -46.434 27.646 1.00 22.02 ? 1045 HOH   A O    1 
HETATM 4500 O  O    . HOH   D 4 .   ? -19.209 -66.613 26.336 1.00 22.97 ? 1046 HOH   A O    1 
HETATM 4501 O  O    . HOH   D 4 .   ? -11.537 -58.466 39.714 1.00 27.23 ? 1047 HOH   A O    1 
HETATM 4502 O  O    . HOH   D 4 .   ? -29.494 -28.440 3.671  1.00 34.47 ? 1048 HOH   A O    1 
HETATM 4503 O  O    . HOH   D 4 .   ? -48.503 -29.801 7.104  1.00 38.22 ? 1049 HOH   A O    1 
HETATM 4504 O  O    . HOH   D 4 .   ? -27.268 -60.471 45.094 1.00 30.46 ? 1050 HOH   A O    1 
HETATM 4505 O  O    . HOH   D 4 .   ? -36.284 -51.520 9.061  1.00 40.20 ? 1051 HOH   A O    1 
HETATM 4506 O  O    . HOH   D 4 .   ? -23.804 -28.747 16.362 1.00 38.77 ? 1052 HOH   A O    1 
HETATM 4507 O  O    . HOH   D 4 .   ? -19.381 -69.945 33.791 1.00 27.63 ? 1053 HOH   A O    1 
HETATM 4508 O  O    . HOH   D 4 .   ? -16.910 -21.332 45.558 1.00 38.62 ? 1054 HOH   A O    1 
HETATM 4509 O  O    . HOH   D 4 .   ? -0.614  -41.230 44.149 1.00 40.46 ? 1055 HOH   A O    1 
HETATM 4510 O  O    . HOH   D 4 .   ? -40.483 -26.568 29.842 1.00 24.80 ? 1056 HOH   A O    1 
HETATM 4511 O  O    . HOH   D 4 .   ? -39.395 -39.484 17.563 1.00 18.74 ? 1057 HOH   A O    1 
HETATM 4512 O  O    . HOH   D 4 .   ? -47.386 -23.205 21.720 1.00 26.65 ? 1058 HOH   A O    1 
HETATM 4513 O  O    . HOH   D 4 .   ? -43.857 -36.235 26.445 1.00 14.59 ? 1059 HOH   A O    1 
HETATM 4514 O  O    . HOH   D 4 .   ? -6.149  -38.773 17.483 1.00 36.58 ? 1060 HOH   A O    1 
HETATM 4515 O  O    . HOH   D 4 .   ? -3.575  -56.369 28.076 1.00 34.53 ? 1061 HOH   A O    1 
HETATM 4516 O  O    . HOH   D 4 .   ? -35.540 -16.959 22.341 1.00 44.22 ? 1062 HOH   A O    1 
HETATM 4517 O  O    . HOH   D 4 .   ? -25.714 -50.713 47.688 1.00 38.48 ? 1063 HOH   A O    1 
HETATM 4518 O  O    . HOH   D 4 .   ? -22.548 -34.451 44.916 1.00 28.29 ? 1064 HOH   A O    1 
HETATM 4519 O  O    . HOH   D 4 .   ? -11.705 -47.250 46.184 1.00 31.57 ? 1065 HOH   A O    1 
HETATM 4520 O  O    . HOH   D 4 .   ? -22.828 -17.497 37.658 1.00 50.44 ? 1066 HOH   A O    1 
HETATM 4521 O  O    . HOH   D 4 .   ? -32.025 -19.229 26.188 1.00 41.22 ? 1067 HOH   A O    1 
HETATM 4522 O  O    . HOH   D 4 .   ? -15.175 -18.022 18.300 1.00 56.10 ? 1068 HOH   A O    1 
HETATM 4523 O  O    . HOH   D 4 .   ? -42.180 -39.116 33.940 1.00 27.03 ? 1069 HOH   A O    1 
HETATM 4524 O  O    . HOH   D 4 .   ? -49.654 -38.235 32.891 1.00 32.75 ? 1070 HOH   A O    1 
HETATM 4525 O  O    . HOH   D 4 .   ? -11.011 -58.503 43.229 1.00 38.21 ? 1071 HOH   A O    1 
HETATM 4526 O  O    . HOH   D 4 .   ? -5.047  -59.052 25.176 1.00 28.87 ? 1072 HOH   A O    1 
HETATM 4527 O  O    . HOH   D 4 .   ? -45.840 -51.243 25.387 1.00 29.32 ? 1073 HOH   A O    1 
HETATM 4528 O  O    . HOH   D 4 .   ? -7.845  -37.114 43.974 1.00 39.63 ? 1074 HOH   A O    1 
HETATM 4529 O  O    . HOH   D 4 .   ? -46.949 -41.399 15.595 1.00 30.41 ? 1075 HOH   A O    1 
HETATM 4530 O  O    . HOH   D 4 .   ? -25.005 -62.670 18.334 1.00 28.96 ? 1076 HOH   A O    1 
HETATM 4531 O  O    . HOH   D 4 .   ? -47.909 -63.865 37.734 1.00 44.30 ? 1077 HOH   A O    1 
HETATM 4532 O  O    . HOH   D 4 .   ? -34.170 -51.983 7.469  1.00 51.16 ? 1078 HOH   A O    1 
HETATM 4533 O  O    . HOH   D 4 .   ? -1.734  -31.831 38.227 1.00 41.53 ? 1079 HOH   A O    1 
HETATM 4534 O  O    . HOH   D 4 .   ? -4.300  -63.713 19.347 1.00 33.89 ? 1080 HOH   A O    1 
HETATM 4535 O  O    . HOH   D 4 .   ? -9.000  -10.283 15.509 1.00 52.87 ? 1081 HOH   A O    1 
HETATM 4536 O  O    . HOH   D 4 .   ? -11.799 -36.696 48.600 1.00 37.05 ? 1082 HOH   A O    1 
HETATM 4537 O  O    . HOH   D 4 .   ? -5.369  -40.974 45.309 1.00 40.44 ? 1083 HOH   A O    1 
HETATM 4538 O  O    . HOH   D 4 .   ? -21.307 -28.820 9.651  1.00 27.29 ? 1084 HOH   A O    1 
HETATM 4539 O  O    . HOH   D 4 .   ? -38.303 -58.297 17.551 1.00 28.26 ? 1085 HOH   A O    1 
HETATM 4540 O  O    . HOH   D 4 .   ? -18.529 -23.553 17.207 1.00 34.56 ? 1086 HOH   A O    1 
HETATM 4541 O  O    . HOH   D 4 .   ? -51.749 -61.316 29.231 1.00 32.15 ? 1087 HOH   A O    1 
HETATM 4542 O  O    . HOH   D 4 .   ? -38.832 -21.336 35.411 1.00 29.64 ? 1088 HOH   A O    1 
HETATM 4543 O  O    . HOH   D 4 .   ? 4.544   -38.094 38.613 1.00 39.55 ? 1089 HOH   A O    1 
HETATM 4544 O  O    . HOH   D 4 .   ? -41.109 -44.709 37.099 1.00 27.54 ? 1090 HOH   A O    1 
HETATM 4545 O  O    . HOH   D 4 .   ? -25.128 -21.352 5.283  1.00 33.24 ? 1091 HOH   A O    1 
HETATM 4546 O  O    . HOH   D 4 .   ? -30.848 -27.780 19.987 1.00 25.74 ? 1092 HOH   A O    1 
HETATM 4547 O  O    . HOH   D 4 .   ? -24.996 -29.992 5.909  1.00 34.96 ? 1093 HOH   A O    1 
HETATM 4548 O  O    . HOH   D 4 .   ? -41.986 -31.381 5.576  1.00 41.09 ? 1094 HOH   A O    1 
HETATM 4549 O  O    . HOH   D 4 .   ? -2.887  -36.589 44.555 1.00 31.88 ? 1095 HOH   A O    1 
HETATM 4550 O  O    . HOH   D 4 .   ? -32.592 -50.483 10.858 1.00 29.69 ? 1096 HOH   A O    1 
HETATM 4551 O  O    . HOH   D 4 .   ? -12.915 -22.512 4.039  1.00 41.68 ? 1097 HOH   A O    1 
HETATM 4552 O  O    . HOH   D 4 .   ? -6.436  -35.018 44.063 1.00 38.33 ? 1098 HOH   A O    1 
HETATM 4553 O  O    . HOH   D 4 .   ? -17.984 -25.387 -1.459 1.00 44.33 ? 1099 HOH   A O    1 
HETATM 4554 O  O    . HOH   D 4 .   ? -30.484 -36.355 3.974  1.00 32.12 ? 1100 HOH   A O    1 
HETATM 4555 O  O    . HOH   D 4 .   ? -23.692 -28.579 9.670  1.00 39.02 ? 1101 HOH   A O    1 
HETATM 4556 O  O    . HOH   D 4 .   ? -40.139 -35.397 32.958 1.00 28.91 ? 1102 HOH   A O    1 
HETATM 4557 O  O    . HOH   D 4 .   ? -47.598 -21.665 7.464  1.00 43.87 ? 1103 HOH   A O    1 
HETATM 4558 O  O    . HOH   D 4 .   ? -1.880  -42.363 16.583 1.00 48.16 ? 1104 HOH   A O    1 
HETATM 4559 O  O    . HOH   D 4 .   ? -4.428  -44.999 43.121 1.00 38.07 ? 1105 HOH   A O    1 
HETATM 4560 O  O    . HOH   D 4 .   ? -3.601  -46.917 5.341  1.00 46.19 ? 1106 HOH   A O    1 
HETATM 4561 O  O    . HOH   D 4 .   ? 3.106   -28.445 23.176 1.00 47.23 ? 1107 HOH   A O    1 
HETATM 4562 O  O    . HOH   D 4 .   ? -20.286 -23.250 47.071 1.00 25.71 ? 1108 HOH   A O    1 
HETATM 4563 O  O    . HOH   D 4 .   ? -28.842 -61.110 18.160 1.00 37.29 ? 1109 HOH   A O    1 
HETATM 4564 O  O    . HOH   D 4 .   ? -22.984 -55.681 11.704 1.00 38.56 ? 1110 HOH   A O    1 
HETATM 4565 O  O    . HOH   D 4 .   ? -13.403 -24.222 41.679 1.00 39.07 ? 1111 HOH   A O    1 
HETATM 4566 O  O    . HOH   D 4 .   ? -36.236 -47.684 45.313 1.00 38.90 ? 1112 HOH   A O    1 
HETATM 4567 O  O    . HOH   D 4 .   ? -29.575 -56.883 8.584  1.00 42.65 ? 1113 HOH   A O    1 
HETATM 4568 O  O    . HOH   D 4 .   ? -49.258 -22.033 14.582 1.00 34.53 ? 1114 HOH   A O    1 
HETATM 4569 O  O    . HOH   D 4 .   ? -25.081 -20.171 26.954 1.00 39.36 ? 1115 HOH   A O    1 
HETATM 4570 O  O    . HOH   D 4 .   ? -27.139 -19.577 32.940 1.00 48.47 ? 1116 HOH   A O    1 
HETATM 4571 O  O    . HOH   D 4 .   ? 2.869   -23.018 21.735 1.00 44.79 ? 1117 HOH   A O    1 
HETATM 4572 O  O    . HOH   D 4 .   ? -26.523 -23.404 6.579  1.00 32.26 ? 1118 HOH   A O    1 
HETATM 4573 O  O    . HOH   D 4 .   ? -2.652  -63.936 21.654 1.00 39.34 ? 1119 HOH   A O    1 
HETATM 4574 O  O    . HOH   D 4 .   ? -27.909 -41.855 46.119 1.00 36.82 ? 1120 HOH   A O    1 
HETATM 4575 O  O    . HOH   D 4 .   ? -37.040 -34.784 35.731 1.00 27.50 ? 1121 HOH   A O    1 
HETATM 4576 O  O    . HOH   D 4 .   ? -27.988 -24.639 42.417 1.00 42.98 ? 1122 HOH   A O    1 
HETATM 4577 O  O    . HOH   D 4 .   ? -24.844 -31.220 42.549 1.00 42.95 ? 1123 HOH   A O    1 
HETATM 4578 O  O    . HOH   D 4 .   ? -26.759 -23.953 39.038 1.00 32.07 ? 1124 HOH   A O    1 
HETATM 4579 O  O    . HOH   D 4 .   ? -25.300 -72.808 28.457 1.00 41.76 ? 1125 HOH   A O    1 
HETATM 4580 O  O    . HOH   D 4 .   ? -28.085 -20.334 26.098 1.00 37.14 ? 1126 HOH   A O    1 
HETATM 4581 O  O    . HOH   D 4 .   ? -24.563 -58.644 44.598 1.00 41.82 ? 1127 HOH   A O    1 
HETATM 4582 O  O    . HOH   D 4 .   ? 2.557   -35.396 29.561 1.00 40.69 ? 1128 HOH   A O    1 
HETATM 4583 O  O    . HOH   D 4 .   ? -46.442 -53.649 24.637 1.00 39.72 ? 1129 HOH   A O    1 
HETATM 4584 O  O    . HOH   D 4 .   ? -34.375 -34.054 41.676 1.00 37.25 ? 1130 HOH   A O    1 
HETATM 4585 O  O    . HOH   D 4 .   ? -41.879 -15.780 23.296 1.00 28.73 ? 1131 HOH   A O    1 
HETATM 4586 O  O    . HOH   D 4 .   ? -46.394 -21.903 27.357 1.00 29.02 ? 1132 HOH   A O    1 
HETATM 4587 O  O    . HOH   D 4 .   ? -9.486  -25.597 26.343 1.00 43.28 ? 1133 HOH   A O    1 
HETATM 4588 O  O    . HOH   D 4 .   ? -28.269 -23.493 17.913 1.00 34.79 ? 1134 HOH   A O    1 
HETATM 4589 O  O    . HOH   D 4 .   ? -27.267 -26.627 38.780 1.00 27.72 ? 1135 HOH   A O    1 
HETATM 4590 O  O    . HOH   D 4 .   ? -22.513 -28.625 45.271 1.00 39.06 ? 1136 HOH   A O    1 
HETATM 4591 O  O    . HOH   D 4 .   ? 0.317   -44.259 36.990 1.00 26.26 ? 1137 HOH   A O    1 
HETATM 4592 O  O    . HOH   D 4 .   ? 1.366   -30.655 18.616 1.00 47.12 ? 1138 HOH   A O    1 
HETATM 4593 O  O    . HOH   D 4 .   ? -25.858 -42.577 6.189  1.00 30.97 ? 1139 HOH   A O    1 
HETATM 4594 O  O    . HOH   D 4 .   ? 5.002   -29.916 15.405 1.00 44.22 ? 1140 HOH   A O    1 
HETATM 4595 O  O    . HOH   D 4 .   ? 0.625   -32.767 19.719 1.00 43.55 ? 1141 HOH   A O    1 
HETATM 4596 O  O    . HOH   D 4 .   ? -5.521  -57.501 27.062 1.00 29.88 ? 1142 HOH   A O    1 
HETATM 4597 O  O    . HOH   D 4 .   ? -14.699 -66.903 28.672 1.00 31.00 ? 1143 HOH   A O    1 
HETATM 4598 O  O    . HOH   D 4 .   ? -49.097 -36.220 14.171 1.00 40.48 ? 1144 HOH   A O    1 
HETATM 4599 O  O    . HOH   D 4 .   ? -23.311 -23.567 19.821 1.00 43.74 ? 1145 HOH   A O    1 
HETATM 4600 O  O    . HOH   D 4 .   ? -27.074 -30.064 41.004 1.00 41.47 ? 1146 HOH   A O    1 
HETATM 4601 O  O    . HOH   D 4 .   ? -2.326  -41.252 13.396 1.00 45.30 ? 1147 HOH   A O    1 
HETATM 4602 O  O    . HOH   D 4 .   ? -49.329 -31.344 26.850 1.00 35.62 ? 1148 HOH   A O    1 
HETATM 4603 O  O    . HOH   D 4 .   ? -47.608 -31.452 28.895 1.00 34.14 ? 1149 HOH   A O    1 
HETATM 4604 O  O    . HOH   D 4 .   ? -19.467 -53.296 10.165 1.00 35.65 ? 1150 HOH   A O    1 
HETATM 4605 O  O    . HOH   D 4 .   ? 5.596   -27.007 14.844 1.00 45.42 ? 1151 HOH   A O    1 
HETATM 4606 O  O    . HOH   D 4 .   ? -11.335 -18.035 20.922 1.00 46.97 ? 1152 HOH   A O    1 
HETATM 4607 O  O    . HOH   D 4 .   ? -30.180 -62.327 22.062 1.00 37.37 ? 1153 HOH   A O    1 
HETATM 4608 O  O    . HOH   D 4 .   ? 0.657   -22.532 23.717 1.00 53.40 ? 1154 HOH   A O    1 
HETATM 4609 O  O    . HOH   D 4 .   ? -28.619 -26.949 41.043 1.00 31.63 ? 1155 HOH   A O    1 
HETATM 4610 O  O    . HOH   D 4 .   ? 5.360   -33.935 37.136 1.00 43.79 ? 1156 HOH   A O    1 
HETATM 4611 O  O    . HOH   D 4 .   ? -24.916 -66.577 34.794 1.00 32.01 ? 1157 HOH   A O    1 
HETATM 4612 O  O    . HOH   D 4 .   ? 3.681   -26.702 4.495  1.00 45.67 ? 1158 HOH   A O    1 
HETATM 4613 O  O    . HOH   D 4 .   ? -25.991 -70.606 37.943 1.00 35.77 ? 1159 HOH   A O    1 
HETATM 4614 O  O    . HOH   D 4 .   ? -17.149 -20.186 33.798 1.00 38.61 ? 1160 HOH   A O    1 
HETATM 4615 O  O    . HOH   D 4 .   ? -6.312  -40.235 13.557 1.00 40.39 ? 1161 HOH   A O    1 
HETATM 4616 O  O    . HOH   D 4 .   ? -8.151  -26.325 42.275 1.00 52.21 ? 1162 HOH   A O    1 
HETATM 4617 O  O    . HOH   D 4 .   ? -38.079 -54.827 15.220 1.00 45.31 ? 1163 HOH   A O    1 
HETATM 4618 O  O    . HOH   D 4 .   ? -20.040 -60.810 41.213 1.00 40.24 ? 1164 HOH   A O    1 
HETATM 4619 O  O    . HOH   D 4 .   ? -22.876 -50.067 46.335 1.00 32.84 ? 1165 HOH   A O    1 
HETATM 4620 O  O    . HOH   D 4 .   ? 0.332   -46.346 41.231 1.00 42.06 ? 1166 HOH   A O    1 
HETATM 4621 O  O    . HOH   D 4 .   ? -42.808 -52.804 19.573 1.00 34.31 ? 1167 HOH   A O    1 
HETATM 4622 O  O    . HOH   D 4 .   ? -9.206  -19.948 6.885  1.00 46.76 ? 1168 HOH   A O    1 
HETATM 4623 O  O    . HOH   D 4 .   ? -26.321 -23.311 19.632 1.00 51.06 ? 1169 HOH   A O    1 
HETATM 4624 O  O    . HOH   D 4 .   ? -52.198 -37.239 24.992 1.00 46.72 ? 1170 HOH   A O    1 
HETATM 4625 O  O    . HOH   D 4 .   ? -20.592 -31.890 46.377 0.50 27.89 ? 1171 HOH   A O    1 
HETATM 4626 O  O    . HOH   D 4 .   ? -51.983 -35.638 27.293 1.00 49.36 ? 1172 HOH   A O    1 
HETATM 4627 O  O    . HOH   D 4 .   ? 2.433   -50.358 24.558 1.00 35.55 ? 1173 HOH   A O    1 
HETATM 4628 O  O    . HOH   D 4 .   ? 2.835   -44.857 36.032 1.00 29.59 ? 1174 HOH   A O    1 
HETATM 4629 O  O    . HOH   D 4 .   ? -0.954  -50.925 19.164 1.00 39.55 ? 1175 HOH   A O    1 
HETATM 4630 O  O    . HOH   D 4 .   ? -47.857 -27.840 26.267 1.00 36.51 ? 1176 HOH   A O    1 
HETATM 4631 O  O    . HOH   D 4 .   ? -49.821 -29.231 9.238  1.00 38.16 ? 1177 HOH   A O    1 
HETATM 4632 O  O    . HOH   D 4 .   ? -11.875 -51.970 45.184 1.00 38.26 ? 1178 HOH   A O    1 
HETATM 4633 O  O    . HOH   D 4 .   ? -8.853  -20.469 4.594  1.00 44.06 ? 1179 HOH   A O    1 
HETATM 4634 O  O    . HOH   D 4 .   ? -44.574 -51.727 21.083 1.00 42.69 ? 1180 HOH   A O    1 
HETATM 4635 O  O    . HOH   D 4 .   ? -39.740 -65.740 37.691 1.00 34.96 ? 1181 HOH   A O    1 
HETATM 4636 O  O    . HOH   D 4 .   ? 0.368   -53.217 35.234 1.00 31.75 ? 1182 HOH   A O    1 
HETATM 4637 O  O    . HOH   D 4 .   ? -6.963  -19.178 7.772  1.00 45.84 ? 1183 HOH   A O    1 
HETATM 4638 O  O    . HOH   D 4 .   ? 4.014   -23.979 16.576 1.00 44.88 ? 1184 HOH   A O    1 
HETATM 4639 O  O    . HOH   D 4 .   ? -11.059 -20.756 3.618  1.00 44.39 ? 1185 HOH   A O    1 
HETATM 4640 O  O    . HOH   D 4 .   ? -11.205 -68.601 20.205 1.00 38.82 ? 1186 HOH   A O    1 
HETATM 4641 O  O    . HOH   D 4 .   ? -43.208 -46.340 42.604 1.00 38.37 ? 1187 HOH   A O    1 
HETATM 4642 O  O    . HOH   D 4 .   ? -53.150 -54.579 37.607 1.00 38.04 ? 1188 HOH   A O    1 
HETATM 4643 O  O    . HOH   D 4 .   ? -26.316 -73.177 25.812 1.00 39.67 ? 1189 HOH   A O    1 
HETATM 4644 O  O    . HOH   D 4 .   ? -43.185 -43.331 36.430 1.00 33.52 ? 1190 HOH   A O    1 
HETATM 4645 O  O    . HOH   D 4 .   ? -20.897 -41.856 2.974  1.00 53.29 ? 1191 HOH   A O    1 
HETATM 4646 O  O    . HOH   D 4 .   ? -20.024 -23.930 19.504 1.00 45.03 ? 1192 HOH   A O    1 
HETATM 4647 O  O    . HOH   D 4 .   ? -28.596 -31.454 43.100 1.00 35.17 ? 1193 HOH   A O    1 
HETATM 4648 O  O    . HOH   D 4 .   ? -7.248  -28.453 44.146 1.00 47.40 ? 1194 HOH   A O    1 
HETATM 4649 O  O    . HOH   D 4 .   ? -29.775 -36.757 10.758 1.00 21.39 ? 1195 HOH   A O    1 
HETATM 4650 O  O    . HOH   D 4 .   ? -49.673 -61.477 24.829 1.00 43.10 ? 1196 HOH   A O    1 
HETATM 4651 O  O    . HOH   D 4 .   ? 0.238   -46.831 39.059 1.00 33.54 ? 1197 HOH   A O    1 
HETATM 4652 O  O    . HOH   D 4 .   ? -23.705 -37.633 45.069 1.00 36.32 ? 1198 HOH   A O    1 
HETATM 4653 O  O    . HOH   D 4 .   ? -19.581 -56.331 10.723 1.00 47.51 ? 1199 HOH   A O    1 
HETATM 4654 O  O    . HOH   D 4 .   ? -15.999 -44.703 46.338 1.00 44.29 ? 1200 HOH   A O    1 
HETATM 4655 O  O    . HOH   D 4 .   ? -38.569 -39.215 4.515  1.00 35.13 ? 1201 HOH   A O    1 
HETATM 4656 O  O    . HOH   D 4 .   ? -31.996 -16.625 27.086 1.00 48.23 ? 1202 HOH   A O    1 
HETATM 4657 O  O    . HOH   D 4 .   ? 0.521   -30.686 20.239 1.00 41.62 ? 1203 HOH   A O    1 
HETATM 4658 O  O    . HOH   D 4 .   ? -37.233 -51.176 45.050 1.00 35.10 ? 1204 HOH   A O    1 
HETATM 4659 O  O    . HOH   D 4 .   ? -9.761  -61.397 33.093 1.00 39.96 ? 1205 HOH   A O    1 
HETATM 4660 O  O    . HOH   D 4 .   ? -45.855 -36.141 3.824  1.00 47.06 ? 1206 HOH   A O    1 
HETATM 4661 O  O    . HOH   D 4 .   ? 0.000   -63.779 23.886 0.33 46.93 ? 1207 HOH   A O    1 
HETATM 4662 O  O    . HOH   D 4 .   ? -8.413  -27.331 35.099 1.00 38.74 ? 1208 HOH   A O    1 
HETATM 4663 O  O    . HOH   D 4 .   ? -30.289 -25.320 19.305 1.00 31.84 ? 1209 HOH   A O    1 
HETATM 4664 O  O    . HOH   D 4 .   ? 5.462   -48.199 32.769 1.00 33.08 ? 1210 HOH   A O    1 
HETATM 4665 O  O    . HOH   D 4 .   ? -44.415 -66.925 36.107 1.00 41.42 ? 1211 HOH   A O    1 
HETATM 4666 O  O    . HOH   D 4 .   ? -12.741 -26.749 41.557 1.00 42.16 ? 1212 HOH   A O    1 
HETATM 4667 O  O    . HOH   D 4 .   ? -10.634 -23.643 27.027 1.00 36.05 ? 1213 HOH   A O    1 
HETATM 4668 O  O    . HOH   D 4 .   ? 1.124   -49.497 37.806 1.00 33.48 ? 1214 HOH   A O    1 
HETATM 4669 O  O    . HOH   D 4 .   ? 0.600   -43.605 41.454 1.00 44.91 ? 1215 HOH   A O    1 
HETATM 4670 O  O    . HOH   D 4 .   ? 4.084   -57.299 30.782 1.00 40.26 ? 1216 HOH   A O    1 
HETATM 4671 O  O    . HOH   D 4 .   ? -28.336 -68.140 41.463 1.00 43.70 ? 1217 HOH   A O    1 
HETATM 4672 O  O    . HOH   D 4 .   ? -14.681 -23.934 22.236 1.00 54.07 ? 1218 HOH   A O    1 
HETATM 4673 O  O    . HOH   D 4 .   ? -11.688 -27.468 25.657 1.00 33.85 ? 1219 HOH   A O    1 
HETATM 4674 O  O    . HOH   D 4 .   ? -13.769 -26.052 22.987 1.00 37.20 ? 1220 HOH   A O    1 
HETATM 4675 O  O    . HOH   D 4 .   ? -42.643 -52.214 21.690 1.00 34.43 ? 1221 HOH   A O    1 
HETATM 4676 O  O    . HOH   D 4 .   ? -51.330 -57.082 37.206 1.00 36.13 ? 1222 HOH   A O    1 
HETATM 4677 O  O    . HOH   D 4 .   ? -2.877  -53.473 18.923 1.00 32.15 ? 1223 HOH   A O    1 
HETATM 4678 O  O    . HOH   D 4 .   ? -33.485 -61.427 16.944 1.00 49.96 ? 1224 HOH   A O    1 
HETATM 4679 O  O    . HOH   D 4 .   ? -37.606 -47.584 8.306  1.00 40.54 ? 1225 HOH   A O    1 
HETATM 4680 O  O    . HOH   D 4 .   ? -24.093 -41.513 45.719 1.00 39.08 ? 1226 HOH   A O    1 
HETATM 4681 O  O    . HOH   D 4 .   ? -57.269 -44.772 30.776 1.00 36.91 ? 1227 HOH   A O    1 
HETATM 4682 O  O    . HOH   D 4 .   ? -44.409 -28.473 28.479 1.00 32.77 ? 1228 HOH   A O    1 
HETATM 4683 O  O    . HOH   D 4 .   ? -51.239 -28.815 21.595 1.00 41.47 ? 1229 HOH   A O    1 
HETATM 4684 O  O    . HOH   D 4 .   ? -10.297 -24.927 31.495 1.00 33.00 ? 1230 HOH   A O    1 
HETATM 4685 O  O    . HOH   D 4 .   ? -4.542  -58.931 28.440 1.00 50.35 ? 1231 HOH   A O    1 
HETATM 4686 O  O    . HOH   D 4 .   ? -25.616 -44.099 4.145  1.00 43.26 ? 1232 HOH   A O    1 
HETATM 4687 O  O    . HOH   D 4 .   ? -36.679 -58.042 15.146 1.00 51.65 ? 1233 HOH   A O    1 
HETATM 4688 O  O    . HOH   D 4 .   ? -34.478 -41.958 4.072  1.00 36.55 ? 1234 HOH   A O    1 
HETATM 4689 O  O    . HOH   D 4 .   ? -41.322 -41.269 6.482  1.00 38.18 ? 1235 HOH   A O    1 
HETATM 4690 O  O    . HOH   D 4 .   ? -22.574 -58.299 43.023 1.00 33.51 ? 1236 HOH   A O    1 
HETATM 4691 O  O    . HOH   D 4 .   ? -14.001 -68.020 19.986 1.00 41.82 ? 1237 HOH   A O    1 
HETATM 4692 O  O    . HOH   D 4 .   ? -37.280 -28.637 37.950 1.00 31.70 ? 1238 HOH   A O    1 
HETATM 4693 O  O    . HOH   D 4 .   ? -13.403 -25.065 30.110 1.00 36.26 ? 1239 HOH   A O    1 
HETATM 4694 O  O    . HOH   D 4 .   ? -17.391 -19.227 35.941 1.00 37.81 ? 1240 HOH   A O    1 
HETATM 4695 O  O    . HOH   D 4 .   ? -3.513  -53.121 14.806 1.00 40.10 ? 1241 HOH   A O    1 
HETATM 4696 O  O    . HOH   D 4 .   ? -38.775 -28.621 30.600 1.00 16.49 ? 1242 HOH   A O    1 
HETATM 4697 O  O    . HOH   D 4 .   ? -19.033 -58.115 45.104 1.00 50.97 ? 1243 HOH   A O    1 
HETATM 4698 O  O    . HOH   D 4 .   ? -33.805 -28.641 40.262 1.00 37.83 ? 1244 HOH   A O    1 
HETATM 4699 O  O    . HOH   D 4 .   ? -51.697 -28.937 23.822 1.00 43.40 ? 1245 HOH   A O    1 
HETATM 4700 O  O    . HOH   D 4 .   ? -39.877 -68.047 25.243 1.00 39.54 ? 1246 HOH   A O    1 
HETATM 4701 O  O    . HOH   D 4 .   ? -52.558 -37.364 33.505 1.00 51.11 ? 1247 HOH   A O    1 
HETATM 4702 O  O    . HOH   D 4 .   ? -12.023 -22.711 37.589 1.00 44.62 ? 1248 HOH   A O    1 
HETATM 4703 O  O    . HOH   D 4 .   ? -31.678 -37.025 51.486 1.00 37.20 ? 1249 HOH   A O    1 
HETATM 4704 O  O    . HOH   D 4 .   ? -38.606 -32.585 35.687 1.00 29.96 ? 1250 HOH   A O    1 
HETATM 4705 O  O    . HOH   D 4 .   ? 3.993   -48.414 23.981 1.00 42.52 ? 1251 HOH   A O    1 
HETATM 4706 O  O    . HOH   D 4 .   ? 0.000   -63.779 21.210 0.33 48.28 ? 1252 HOH   A O    1 
HETATM 4707 O  O    . HOH   D 4 .   ? -37.199 -41.864 4.711  1.00 41.96 ? 1253 HOH   A O    1 
HETATM 4708 O  O    . HOH   D 4 .   ? 0.000   -63.779 18.619 0.33 40.20 ? 1254 HOH   A O    1 
HETATM 4709 O  O    . HOH   D 4 .   ? -53.281 -30.346 25.178 1.00 42.48 ? 1255 HOH   A O    1 
HETATM 4710 O  O    . HOH   D 4 .   ? -55.234 -31.890 23.530 0.33 29.66 ? 1256 HOH   A O    1 
HETATM 4711 O  O    . HOH   D 4 .   ? -38.746 -43.493 6.029  1.00 40.32 ? 1257 HOH   A O    1 
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