data_9KGP
# 
_entry.id   9KGP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9KGP         pdb_00009kgp 10.2210/pdb9kgp/pdb 
WWPDB D_1300050827 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-07 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9KGP 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-08 
_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           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 lihui@jiangnan.edu.cn          Hui    Li    ? 'principal investigator/group leader' 0000-0003-4623-2125 
3 Ljzhang@chem.ecnu.edu.cn       Lujia  Zhang ? 'principal investigator/group leader' 0000-0003-3566-917X 
4 7210201002@stu.jiangnan.edu.cn Qingbo Deng  ? 'principal investigator/group leader' 0009-0005-3778-5619 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Deng, Q.B.'  1 0009-0005-3778-5619 
'Zhang, L.J.' 2 0000-0003-3566-917X 
'Li, H.'      3 0000-0003-4623-2125 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            307 
_citation.language                  ? 
_citation.page_first                142162 
_citation.page_last                 142162 
_citation.title                     
'Rationally designing P450BM3-H to excavate a novel channel for product exit and enhance overall performance.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2025.142162 
_citation.pdbx_database_id_PubMed   40107536 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Deng, Q.'      1 ? 
primary 'Lu, Z.M.'      2 ? 
primary 'Yuan, Z.'      3 ? 
primary 'Feng, Y.'      4 ? 
primary 'Zhang, L.'     5 ? 
primary 'Shi, J.'       6 ? 
primary 'Xu, Z.'        7 ? 
primary 'Kofas, M.A.G.' 8 ? 
primary 'Li, H.'        9 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Bifunctional cytochrome P450/NADPH--P450 reductase' 52078.293 2   1.14.14.1,1.6.2.4 ? ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                    616.487   2   ?                 ? ? ? 
3 water       nat water                                                18.015    552 ?                 ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytochrome P450(BM-3),Cytochrome P450BM-3,Fatty acid monooxygenase,Flavocytochrome P450 BM3' 
# 
_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       
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQGLKFVRD
FAGDGLVTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLIQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEIMNKLQRANPDDPAYDENKRQFQDDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLGGGHETTSGLLSFALYFLVKNPHVLQKAAEEAARILVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTGPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKQIPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQGLKFVRD
FAGDGLVTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLIQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEIMNKLQRANPDDPAYDENKRQFQDDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLGGGHETTSGLLSFALYFLVKNPHVLQKAAEEAARILVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTGPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKQIPL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
3 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   ILE n 
1 3   LYS n 
1 4   GLU n 
1 5   MET n 
1 6   PRO n 
1 7   GLN n 
1 8   PRO n 
1 9   LYS n 
1 10  THR n 
1 11  PHE n 
1 12  GLY n 
1 13  GLU n 
1 14  LEU n 
1 15  LYS n 
1 16  ASN n 
1 17  LEU n 
1 18  PRO n 
1 19  LEU n 
1 20  LEU n 
1 21  ASN n 
1 22  THR n 
1 23  ASP n 
1 24  LYS n 
1 25  PRO n 
1 26  VAL n 
1 27  GLN n 
1 28  ALA n 
1 29  LEU n 
1 30  MET n 
1 31  LYS n 
1 32  ILE n 
1 33  ALA n 
1 34  ASP n 
1 35  GLU n 
1 36  LEU n 
1 37  GLY n 
1 38  GLU n 
1 39  ILE n 
1 40  PHE n 
1 41  LYS n 
1 42  PHE n 
1 43  GLU n 
1 44  ALA n 
1 45  PRO n 
1 46  GLY n 
1 47  ARG n 
1 48  VAL n 
1 49  THR n 
1 50  ARG n 
1 51  TYR n 
1 52  LEU n 
1 53  SER n 
1 54  SER n 
1 55  GLN n 
1 56  ARG n 
1 57  LEU n 
1 58  ILE n 
1 59  LYS n 
1 60  GLU n 
1 61  ALA n 
1 62  CYS n 
1 63  ASP n 
1 64  GLU n 
1 65  SER n 
1 66  ARG n 
1 67  PHE n 
1 68  ASP n 
1 69  LYS n 
1 70  ASN n 
1 71  LEU n 
1 72  SER n 
1 73  GLN n 
1 74  GLY n 
1 75  LEU n 
1 76  LYS n 
1 77  PHE n 
1 78  VAL n 
1 79  ARG n 
1 80  ASP n 
1 81  PHE n 
1 82  ALA n 
1 83  GLY n 
1 84  ASP n 
1 85  GLY n 
1 86  LEU n 
1 87  VAL n 
1 88  THR n 
1 89  SER n 
1 90  TRP n 
1 91  THR n 
1 92  HIS n 
1 93  GLU n 
1 94  LYS n 
1 95  ASN n 
1 96  TRP n 
1 97  LYS n 
1 98  LYS n 
1 99  ALA n 
1 100 HIS n 
1 101 ASN n 
1 102 ILE n 
1 103 LEU n 
1 104 LEU n 
1 105 PRO n 
1 106 SER n 
1 107 PHE n 
1 108 SER n 
1 109 GLN n 
1 110 GLN n 
1 111 ALA n 
1 112 MET n 
1 113 LYS n 
1 114 GLY n 
1 115 TYR n 
1 116 HIS n 
1 117 ALA n 
1 118 MET n 
1 119 MET n 
1 120 VAL n 
1 121 ASP n 
1 122 ILE n 
1 123 ALA n 
1 124 VAL n 
1 125 GLN n 
1 126 LEU n 
1 127 ILE n 
1 128 GLN n 
1 129 LYS n 
1 130 TRP n 
1 131 GLU n 
1 132 ARG n 
1 133 LEU n 
1 134 ASN n 
1 135 ALA n 
1 136 ASP n 
1 137 GLU n 
1 138 HIS n 
1 139 ILE n 
1 140 GLU n 
1 141 VAL n 
1 142 PRO n 
1 143 GLU n 
1 144 ASP n 
1 145 MET n 
1 146 THR n 
1 147 ARG n 
1 148 LEU n 
1 149 THR n 
1 150 LEU n 
1 151 ASP n 
1 152 THR n 
1 153 ILE n 
1 154 GLY n 
1 155 LEU n 
1 156 CYS n 
1 157 GLY n 
1 158 PHE n 
1 159 ASN n 
1 160 TYR n 
1 161 ARG n 
1 162 PHE n 
1 163 ASN n 
1 164 SER n 
1 165 PHE n 
1 166 TYR n 
1 167 ARG n 
1 168 ASP n 
1 169 GLN n 
1 170 PRO n 
1 171 HIS n 
1 172 PRO n 
1 173 PHE n 
1 174 ILE n 
1 175 THR n 
1 176 SER n 
1 177 MET n 
1 178 VAL n 
1 179 ARG n 
1 180 ALA n 
1 181 LEU n 
1 182 ASP n 
1 183 GLU n 
1 184 ILE n 
1 185 MET n 
1 186 ASN n 
1 187 LYS n 
1 188 LEU n 
1 189 GLN n 
1 190 ARG n 
1 191 ALA n 
1 192 ASN n 
1 193 PRO n 
1 194 ASP n 
1 195 ASP n 
1 196 PRO n 
1 197 ALA n 
1 198 TYR n 
1 199 ASP n 
1 200 GLU n 
1 201 ASN n 
1 202 LYS n 
1 203 ARG n 
1 204 GLN n 
1 205 PHE n 
1 206 GLN n 
1 207 ASP n 
1 208 ASP n 
1 209 ILE n 
1 210 LYS n 
1 211 VAL n 
1 212 MET n 
1 213 ASN n 
1 214 ASP n 
1 215 LEU n 
1 216 VAL n 
1 217 ASP n 
1 218 LYS n 
1 219 ILE n 
1 220 ILE n 
1 221 ALA n 
1 222 ASP n 
1 223 ARG n 
1 224 LYS n 
1 225 ALA n 
1 226 SER n 
1 227 GLY n 
1 228 GLU n 
1 229 GLN n 
1 230 SER n 
1 231 ASP n 
1 232 ASP n 
1 233 LEU n 
1 234 LEU n 
1 235 THR n 
1 236 HIS n 
1 237 MET n 
1 238 LEU n 
1 239 ASN n 
1 240 GLY n 
1 241 LYS n 
1 242 ASP n 
1 243 PRO n 
1 244 GLU n 
1 245 THR n 
1 246 GLY n 
1 247 GLU n 
1 248 PRO n 
1 249 LEU n 
1 250 ASP n 
1 251 ASP n 
1 252 GLU n 
1 253 ASN n 
1 254 ILE n 
1 255 ARG n 
1 256 TYR n 
1 257 GLN n 
1 258 ILE n 
1 259 ILE n 
1 260 THR n 
1 261 PHE n 
1 262 LEU n 
1 263 GLY n 
1 264 GLY n 
1 265 GLY n 
1 266 HIS n 
1 267 GLU n 
1 268 THR n 
1 269 THR n 
1 270 SER n 
1 271 GLY n 
1 272 LEU n 
1 273 LEU n 
1 274 SER n 
1 275 PHE n 
1 276 ALA n 
1 277 LEU n 
1 278 TYR n 
1 279 PHE n 
1 280 LEU n 
1 281 VAL n 
1 282 LYS n 
1 283 ASN n 
1 284 PRO n 
1 285 HIS n 
1 286 VAL n 
1 287 LEU n 
1 288 GLN n 
1 289 LYS n 
1 290 ALA n 
1 291 ALA n 
1 292 GLU n 
1 293 GLU n 
1 294 ALA n 
1 295 ALA n 
1 296 ARG n 
1 297 ILE n 
1 298 LEU n 
1 299 VAL n 
1 300 ASP n 
1 301 PRO n 
1 302 VAL n 
1 303 PRO n 
1 304 SER n 
1 305 TYR n 
1 306 LYS n 
1 307 GLN n 
1 308 VAL n 
1 309 LYS n 
1 310 GLN n 
1 311 LEU n 
1 312 LYS n 
1 313 TYR n 
1 314 VAL n 
1 315 GLY n 
1 316 MET n 
1 317 VAL n 
1 318 LEU n 
1 319 ASN n 
1 320 GLU n 
1 321 ALA n 
1 322 LEU n 
1 323 ARG n 
1 324 LEU n 
1 325 TRP n 
1 326 PRO n 
1 327 THR n 
1 328 GLY n 
1 329 PRO n 
1 330 ALA n 
1 331 PHE n 
1 332 SER n 
1 333 LEU n 
1 334 TYR n 
1 335 ALA n 
1 336 LYS n 
1 337 GLU n 
1 338 ASP n 
1 339 THR n 
1 340 VAL n 
1 341 LEU n 
1 342 GLY n 
1 343 GLY n 
1 344 GLU n 
1 345 TYR n 
1 346 PRO n 
1 347 LEU n 
1 348 GLU n 
1 349 LYS n 
1 350 GLY n 
1 351 ASP n 
1 352 GLU n 
1 353 LEU n 
1 354 MET n 
1 355 VAL n 
1 356 LEU n 
1 357 ILE n 
1 358 PRO n 
1 359 GLN n 
1 360 LEU n 
1 361 HIS n 
1 362 ARG n 
1 363 ASP n 
1 364 LYS n 
1 365 THR n 
1 366 ILE n 
1 367 TRP n 
1 368 GLY n 
1 369 ASP n 
1 370 ASP n 
1 371 VAL n 
1 372 GLU n 
1 373 GLU n 
1 374 PHE n 
1 375 ARG n 
1 376 PRO n 
1 377 GLU n 
1 378 ARG n 
1 379 PHE n 
1 380 GLU n 
1 381 ASN n 
1 382 PRO n 
1 383 SER n 
1 384 ALA n 
1 385 ILE n 
1 386 PRO n 
1 387 GLN n 
1 388 HIS n 
1 389 ALA n 
1 390 PHE n 
1 391 LYS n 
1 392 PRO n 
1 393 PHE n 
1 394 GLY n 
1 395 ASN n 
1 396 GLY n 
1 397 GLN n 
1 398 ARG n 
1 399 ALA n 
1 400 CYS n 
1 401 ILE n 
1 402 GLY n 
1 403 GLN n 
1 404 GLN n 
1 405 PHE n 
1 406 ALA n 
1 407 LEU n 
1 408 HIS n 
1 409 GLU n 
1 410 ALA n 
1 411 THR n 
1 412 LEU n 
1 413 VAL n 
1 414 LEU n 
1 415 GLY n 
1 416 MET n 
1 417 MET n 
1 418 LEU n 
1 419 LYS n 
1 420 HIS n 
1 421 PHE n 
1 422 ASP n 
1 423 PHE n 
1 424 GLU n 
1 425 ASP n 
1 426 HIS n 
1 427 THR n 
1 428 ASN n 
1 429 TYR n 
1 430 GLU n 
1 431 LEU n 
1 432 ASP n 
1 433 ILE n 
1 434 LYS n 
1 435 GLU n 
1 436 THR n 
1 437 LEU n 
1 438 THR n 
1 439 LEU n 
1 440 LYS n 
1 441 PRO n 
1 442 GLU n 
1 443 GLY n 
1 444 PHE n 
1 445 VAL n 
1 446 VAL n 
1 447 LYS n 
1 448 ALA n 
1 449 LYS n 
1 450 SER n 
1 451 LYS n 
1 452 GLN n 
1 453 ILE n 
1 454 PRO n 
1 455 LEU 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                   455 
_entity_src_gen.gene_src_common_name               'Bacillus megaterium' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'cyp102A1, cyp102, BG04_163' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    
'ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19' 
_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      'Priestia megaterium NBRC 15308 = ATCC 14581' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1348623 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                           ?    'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                          ?    'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                        ?    'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                   ?    'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                          ?    'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                         ?    'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                   ?    'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                           ?    'C2 H5 N O2'       75.067  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
HIS 'L-peptide linking' y HISTIDINE                         ?    'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                             ?    'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                        ?    'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                           ?    'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                            ?    'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                        ?    'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                     ?    'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                           ?    'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                            ?    'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                         ?    'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ?    'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                          ?    'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                            ?    'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   THR 1   1   ?   ?   ?   A . n 
A 1 2   ILE 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   MET 5   5   5   MET MET A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   GLN 7   7   7   GLN GLN A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  PRO 18  18  18  PRO PRO A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ASN 21  21  21  ASN ASN A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  ASP 23  23  23  ASP ASP A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  VAL 26  26  26  VAL VAL A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  MET 30  30  30  MET MET A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  GLU 38  38  38  GLU GLU A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  PHE 42  42  42  PHE PHE A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  CYS 62  62  62  CYS CYS A . n 
A 1 63  ASP 63  63  63  ASP ASP A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  PHE 67  67  67  PHE PHE A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  PHE 77  77  77  PHE PHE A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  TRP 90  90  90  TRP TRP A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  HIS 92  92  92  HIS HIS A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  TRP 96  96  96  TRP TRP A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  LYS 98  98  98  LYS LYS A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLN 109 109 109 GLN GLN A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 MET 112 112 112 MET MET A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 HIS 116 116 116 HIS HIS A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 MET 118 118 118 MET MET A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 GLN 125 125 125 GLN GLN A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 TRP 130 130 130 TRP TRP A . n 
A 1 131 GLU 131 131 131 GLU GLU A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 MET 145 145 145 MET MET A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 ARG 147 147 147 ARG ARG A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 PHE 162 162 162 PHE PHE A . n 
A 1 163 ASN 163 163 163 ASN ASN A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 ASP 168 168 168 ASP ASP A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 HIS 171 171 171 HIS HIS A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 ILE 174 174 174 ILE ILE A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 MET 177 177 177 MET MET A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 ILE 184 184 184 ILE ILE A . n 
A 1 185 MET 185 185 185 MET MET A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 LYS 187 187 187 LYS LYS A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ASN 192 192 192 ASN ASN A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 ASP 194 194 194 ASP ASP A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 PRO 196 196 196 PRO PRO A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 ASP 199 199 199 ASP ASP A . n 
A 1 200 GLU 200 200 200 GLU GLU A . n 
A 1 201 ASN 201 201 201 ASN ASN A . n 
A 1 202 LYS 202 202 202 LYS LYS A . n 
A 1 203 ARG 203 203 203 ARG ARG A . n 
A 1 204 GLN 204 204 204 GLN GLN A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 GLN 206 206 206 GLN GLN A . n 
A 1 207 ASP 207 207 207 ASP ASP A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 LYS 210 210 210 LYS LYS A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 MET 212 212 212 MET MET A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 ASP 217 217 217 ASP ASP A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 ARG 223 223 223 ARG ARG A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 THR 235 235 235 THR THR A . n 
A 1 236 HIS 236 236 236 HIS HIS A . n 
A 1 237 MET 237 237 237 MET MET A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 GLU 244 244 244 GLU GLU A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 ASP 250 250 250 ASP ASP A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 GLU 252 252 252 GLU GLU A . n 
A 1 253 ASN 253 253 253 ASN ASN A . n 
A 1 254 ILE 254 254 254 ILE ILE A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 GLN 257 257 257 GLN GLN A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 THR 260 260 260 THR THR A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 HIS 266 266 266 HIS HIS A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 THR 269 269 269 THR THR A . n 
A 1 270 SER 270 270 270 SER SER A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 TYR 278 278 278 TYR TYR A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 VAL 281 281 281 VAL VAL A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 ASN 283 283 283 ASN ASN A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 HIS 285 285 285 HIS HIS A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 GLU 293 293 293 GLU GLU A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 ILE 297 297 297 ILE ILE A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 VAL 299 299 299 VAL VAL A . n 
A 1 300 ASP 300 300 300 ASP ASP A . n 
A 1 301 PRO 301 301 301 PRO PRO A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 SER 304 304 304 SER SER A . n 
A 1 305 TYR 305 305 305 TYR TYR A . n 
A 1 306 LYS 306 306 306 LYS LYS A . n 
A 1 307 GLN 307 307 307 GLN GLN A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 LYS 309 309 309 LYS LYS A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 LYS 312 312 312 LYS LYS A . n 
A 1 313 TYR 313 313 313 TYR TYR A . n 
A 1 314 VAL 314 314 314 VAL VAL A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 MET 316 316 316 MET MET A . n 
A 1 317 VAL 317 317 317 VAL VAL A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 ASN 319 319 319 ASN ASN A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 LEU 322 322 322 LEU LEU A . n 
A 1 323 ARG 323 323 323 ARG ARG A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 TRP 325 325 325 TRP TRP A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 THR 327 327 327 THR THR A . n 
A 1 328 GLY 328 328 328 GLY GLY A . n 
A 1 329 PRO 329 329 329 PRO PRO A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 PHE 331 331 331 PHE PHE A . n 
A 1 332 SER 332 332 332 SER SER A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 TYR 334 334 334 TYR TYR A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 ASP 338 338 338 ASP ASP A . n 
A 1 339 THR 339 339 339 THR THR A . n 
A 1 340 VAL 340 340 340 VAL VAL A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 TYR 345 345 345 TYR TYR A . n 
A 1 346 PRO 346 346 346 PRO PRO A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 GLU 348 348 348 GLU GLU A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 ASP 351 351 351 ASP ASP A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 MET 354 354 354 MET MET A . n 
A 1 355 VAL 355 355 355 VAL VAL A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 ILE 357 357 357 ILE ILE A . n 
A 1 358 PRO 358 358 358 PRO PRO A . n 
A 1 359 GLN 359 359 359 GLN GLN A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 HIS 361 361 361 HIS HIS A . n 
A 1 362 ARG 362 362 362 ARG ARG A . n 
A 1 363 ASP 363 363 363 ASP ASP A . n 
A 1 364 LYS 364 364 364 LYS LYS A . n 
A 1 365 THR 365 365 365 THR THR A . n 
A 1 366 ILE 366 366 366 ILE ILE A . n 
A 1 367 TRP 367 367 367 TRP TRP A . n 
A 1 368 GLY 368 368 368 GLY GLY A . n 
A 1 369 ASP 369 369 369 ASP ASP A . n 
A 1 370 ASP 370 370 370 ASP ASP A . n 
A 1 371 VAL 371 371 371 VAL VAL A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 GLU 373 373 373 GLU GLU A . n 
A 1 374 PHE 374 374 374 PHE PHE A . n 
A 1 375 ARG 375 375 375 ARG ARG A . n 
A 1 376 PRO 376 376 376 PRO PRO A . n 
A 1 377 GLU 377 377 377 GLU GLU A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 PHE 379 379 379 PHE PHE A . n 
A 1 380 GLU 380 380 380 GLU GLU A . n 
A 1 381 ASN 381 381 381 ASN ASN A . n 
A 1 382 PRO 382 382 382 PRO PRO A . n 
A 1 383 SER 383 383 383 SER SER A . n 
A 1 384 ALA 384 384 384 ALA ALA A . n 
A 1 385 ILE 385 385 385 ILE ILE A . n 
A 1 386 PRO 386 386 386 PRO PRO A . n 
A 1 387 GLN 387 387 387 GLN GLN A . n 
A 1 388 HIS 388 388 388 HIS HIS A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 PHE 390 390 390 PHE PHE A . n 
A 1 391 LYS 391 391 391 LYS LYS A . n 
A 1 392 PRO 392 392 392 PRO PRO A . n 
A 1 393 PHE 393 393 393 PHE PHE A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 ASN 395 395 395 ASN ASN A . n 
A 1 396 GLY 396 396 396 GLY GLY A . n 
A 1 397 GLN 397 397 397 GLN GLN A . n 
A 1 398 ARG 398 398 398 ARG ARG A . n 
A 1 399 ALA 399 399 399 ALA ALA A . n 
A 1 400 CYS 400 400 400 CYS CYS A . n 
A 1 401 ILE 401 401 401 ILE ILE A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 GLN 403 403 403 GLN GLN A . n 
A 1 404 GLN 404 404 404 GLN GLN A . n 
A 1 405 PHE 405 405 405 PHE PHE A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 LEU 407 407 407 LEU LEU A . n 
A 1 408 HIS 408 408 408 HIS HIS A . n 
A 1 409 GLU 409 409 409 GLU GLU A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 THR 411 411 411 THR THR A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 VAL 413 413 413 VAL VAL A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 GLY 415 415 415 GLY GLY A . n 
A 1 416 MET 416 416 416 MET MET A . n 
A 1 417 MET 417 417 417 MET MET A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 LYS 419 419 419 LYS LYS A . n 
A 1 420 HIS 420 420 420 HIS HIS A . n 
A 1 421 PHE 421 421 421 PHE PHE A . n 
A 1 422 ASP 422 422 422 ASP ASP A . n 
A 1 423 PHE 423 423 423 PHE PHE A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 ASP 425 425 425 ASP ASP A . n 
A 1 426 HIS 426 426 426 HIS HIS A . n 
A 1 427 THR 427 427 427 THR THR A . n 
A 1 428 ASN 428 428 428 ASN ASN A . n 
A 1 429 TYR 429 429 429 TYR TYR A . n 
A 1 430 GLU 430 430 430 GLU GLU A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 ASP 432 432 432 ASP ASP A . n 
A 1 433 ILE 433 433 433 ILE ILE A . n 
A 1 434 LYS 434 434 434 LYS LYS A . n 
A 1 435 GLU 435 435 435 GLU GLU A . n 
A 1 436 THR 436 436 436 THR THR A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 THR 438 438 438 THR THR A . n 
A 1 439 LEU 439 439 439 LEU LEU A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 PRO 441 441 441 PRO PRO A . n 
A 1 442 GLU 442 442 442 GLU GLU A . n 
A 1 443 GLY 443 443 443 GLY GLY A . n 
A 1 444 PHE 444 444 444 PHE PHE A . n 
A 1 445 VAL 445 445 445 VAL VAL A . n 
A 1 446 VAL 446 446 446 VAL VAL A . n 
A 1 447 LYS 447 447 447 LYS LYS A . n 
A 1 448 ALA 448 448 448 ALA ALA A . n 
A 1 449 LYS 449 449 449 LYS LYS A . n 
A 1 450 SER 450 450 450 SER SER A . n 
A 1 451 LYS 451 451 451 LYS LYS A . n 
A 1 452 GLN 452 452 452 GLN GLN A . n 
A 1 453 ILE 453 453 453 ILE ILE A . n 
A 1 454 PRO 454 454 454 PRO PRO A . n 
A 1 455 LEU 455 455 455 LEU LEU A . n 
B 1 1   THR 1   1   ?   ?   ?   B . n 
B 1 2   ILE 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   GLU 4   4   4   GLU GLU B . n 
B 1 5   MET 5   5   5   MET MET B . n 
B 1 6   PRO 6   6   6   PRO PRO B . n 
B 1 7   GLN 7   7   7   GLN GLN B . n 
B 1 8   PRO 8   8   8   PRO PRO B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  THR 10  10  10  THR THR B . n 
B 1 11  PHE 11  11  11  PHE PHE B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  GLU 13  13  13  GLU GLU B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  LYS 15  15  15  LYS LYS B . n 
B 1 16  ASN 16  16  16  ASN ASN B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  PRO 18  18  18  PRO PRO B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  ASN 21  21  21  ASN ASN B . n 
B 1 22  THR 22  22  22  THR THR B . n 
B 1 23  ASP 23  23  23  ASP ASP B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  PRO 25  25  25  PRO PRO B . n 
B 1 26  VAL 26  26  26  VAL VAL B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  MET 30  30  30  MET MET B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  ALA 33  33  33  ALA ALA B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  GLU 35  35  35  GLU GLU B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  GLU 38  38  38  GLU GLU B . n 
B 1 39  ILE 39  39  39  ILE ILE B . n 
B 1 40  PHE 40  40  40  PHE PHE B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  PHE 42  42  42  PHE PHE B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  ARG 50  50  50  ARG ARG B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  SER 53  53  53  SER SER B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  GLN 55  55  55  GLN GLN B . n 
B 1 56  ARG 56  56  56  ARG ARG B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  ILE 58  58  58  ILE ILE B . n 
B 1 59  LYS 59  59  59  LYS LYS B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  CYS 62  62  62  CYS CYS B . n 
B 1 63  ASP 63  63  63  ASP ASP B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  PHE 67  67  67  PHE PHE B . n 
B 1 68  ASP 68  68  68  ASP ASP B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  ASN 70  70  70  ASN ASN B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  GLN 73  73  73  GLN GLN B . n 
B 1 74  GLY 74  74  74  GLY GLY B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  PHE 77  77  77  PHE PHE B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  PHE 81  81  81  PHE PHE B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  SER 89  89  89  SER SER B . n 
B 1 90  TRP 90  90  90  TRP TRP B . n 
B 1 91  THR 91  91  91  THR THR B . n 
B 1 92  HIS 92  92  92  HIS HIS B . n 
B 1 93  GLU 93  93  93  GLU GLU B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  TRP 96  96  96  TRP TRP B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  LYS 98  98  98  LYS LYS B . n 
B 1 99  ALA 99  99  99  ALA ALA B . n 
B 1 100 HIS 100 100 100 HIS HIS B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 ILE 102 102 102 ILE ILE B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 PRO 105 105 105 PRO PRO B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 PHE 107 107 107 PHE PHE B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLN 109 109 109 GLN GLN B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 MET 112 112 112 MET MET B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 TYR 115 115 115 TYR TYR B . n 
B 1 116 HIS 116 116 116 HIS HIS B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 MET 118 118 118 MET MET B . n 
B 1 119 MET 119 119 119 MET MET B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 ASP 121 121 121 ASP ASP B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 GLN 125 125 125 GLN GLN B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 ILE 127 127 127 ILE ILE B . n 
B 1 128 GLN 128 128 128 GLN GLN B . n 
B 1 129 LYS 129 129 129 LYS LYS B . n 
B 1 130 TRP 130 130 130 TRP TRP B . n 
B 1 131 GLU 131 131 131 GLU GLU B . n 
B 1 132 ARG 132 132 132 ARG ARG B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 ALA 135 135 135 ALA ALA B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 GLU 140 140 140 GLU GLU B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 PRO 142 142 142 PRO PRO B . n 
B 1 143 GLU 143 143 143 GLU GLU B . n 
B 1 144 ASP 144 144 144 ASP ASP B . n 
B 1 145 MET 145 145 145 MET MET B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 ARG 147 147 147 ARG ARG B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 ASP 151 151 151 ASP ASP B . n 
B 1 152 THR 152 152 152 THR THR B . n 
B 1 153 ILE 153 153 153 ILE ILE B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 LEU 155 155 155 LEU LEU B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 GLY 157 157 157 GLY GLY B . n 
B 1 158 PHE 158 158 158 PHE PHE B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 TYR 160 160 160 TYR TYR B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 PHE 162 162 162 PHE PHE B . n 
B 1 163 ASN 163 163 163 ASN ASN B . n 
B 1 164 SER 164 164 164 SER SER B . n 
B 1 165 PHE 165 165 165 PHE PHE B . n 
B 1 166 TYR 166 166 166 TYR TYR B . n 
B 1 167 ARG 167 167 167 ARG ARG B . n 
B 1 168 ASP 168 168 168 ASP ASP B . n 
B 1 169 GLN 169 169 169 GLN GLN B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 HIS 171 171 171 HIS HIS B . n 
B 1 172 PRO 172 172 172 PRO PRO B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 ILE 174 174 174 ILE ILE B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 SER 176 176 176 SER SER B . n 
B 1 177 MET 177 177 177 MET MET B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 ARG 179 179 179 ARG ARG B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 ASP 182 182 182 ASP ASP B . n 
B 1 183 GLU 183 183 183 GLU GLU B . n 
B 1 184 ILE 184 184 184 ILE ILE B . n 
B 1 185 MET 185 185 185 MET MET B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 LYS 187 187 187 LYS LYS B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 ARG 190 190 190 ARG ARG B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 ASN 192 192 192 ASN ASN B . n 
B 1 193 PRO 193 193 193 PRO PRO B . n 
B 1 194 ASP 194 194 194 ASP ASP B . n 
B 1 195 ASP 195 195 195 ASP ASP B . n 
B 1 196 PRO 196 196 196 PRO PRO B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 TYR 198 198 198 TYR TYR B . n 
B 1 199 ASP 199 199 199 ASP ASP B . n 
B 1 200 GLU 200 200 200 GLU GLU B . n 
B 1 201 ASN 201 201 201 ASN ASN B . n 
B 1 202 LYS 202 202 202 LYS LYS B . n 
B 1 203 ARG 203 203 203 ARG ARG B . n 
B 1 204 GLN 204 204 204 GLN GLN B . n 
B 1 205 PHE 205 205 205 PHE PHE B . n 
B 1 206 GLN 206 206 206 GLN GLN B . n 
B 1 207 ASP 207 207 207 ASP ASP B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 ILE 209 209 209 ILE ILE B . n 
B 1 210 LYS 210 210 210 LYS LYS B . n 
B 1 211 VAL 211 211 211 VAL VAL B . n 
B 1 212 MET 212 212 212 MET MET B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 ASP 214 214 214 ASP ASP B . n 
B 1 215 LEU 215 215 215 LEU LEU B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 ASP 217 217 217 ASP ASP B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 ILE 219 219 219 ILE ILE B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 ALA 221 221 221 ALA ALA B . n 
B 1 222 ASP 222 222 222 ASP ASP B . n 
B 1 223 ARG 223 223 223 ARG ARG B . n 
B 1 224 LYS 224 224 224 LYS LYS B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 SER 226 226 226 SER SER B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 GLN 229 229 229 GLN GLN B . n 
B 1 230 SER 230 230 230 SER SER B . n 
B 1 231 ASP 231 231 231 ASP ASP B . n 
B 1 232 ASP 232 232 232 ASP ASP B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 LEU 234 234 234 LEU LEU B . n 
B 1 235 THR 235 235 235 THR THR B . n 
B 1 236 HIS 236 236 236 HIS HIS B . n 
B 1 237 MET 237 237 237 MET MET B . n 
B 1 238 LEU 238 238 238 LEU LEU B . n 
B 1 239 ASN 239 239 239 ASN ASN B . n 
B 1 240 GLY 240 240 240 GLY GLY B . n 
B 1 241 LYS 241 241 241 LYS LYS B . n 
B 1 242 ASP 242 242 242 ASP ASP B . n 
B 1 243 PRO 243 243 243 PRO PRO B . n 
B 1 244 GLU 244 244 244 GLU GLU B . n 
B 1 245 THR 245 245 245 THR THR B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 PRO 248 248 248 PRO PRO B . n 
B 1 249 LEU 249 249 249 LEU LEU B . n 
B 1 250 ASP 250 250 250 ASP ASP B . n 
B 1 251 ASP 251 251 251 ASP ASP B . n 
B 1 252 GLU 252 252 252 GLU GLU B . n 
B 1 253 ASN 253 253 253 ASN ASN B . n 
B 1 254 ILE 254 254 254 ILE ILE B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 TYR 256 256 256 TYR TYR B . n 
B 1 257 GLN 257 257 257 GLN GLN B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 THR 260 260 260 THR THR B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 GLY 263 263 263 GLY GLY B . n 
B 1 264 GLY 264 264 264 GLY GLY B . n 
B 1 265 GLY 265 265 265 GLY GLY B . n 
B 1 266 HIS 266 266 266 HIS HIS B . n 
B 1 267 GLU 267 267 267 GLU GLU B . n 
B 1 268 THR 268 268 268 THR THR B . n 
B 1 269 THR 269 269 269 THR THR B . n 
B 1 270 SER 270 270 270 SER SER B . n 
B 1 271 GLY 271 271 271 GLY GLY B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 LEU 273 273 273 LEU LEU B . n 
B 1 274 SER 274 274 274 SER SER B . n 
B 1 275 PHE 275 275 275 PHE PHE B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 TYR 278 278 278 TYR TYR B . n 
B 1 279 PHE 279 279 279 PHE PHE B . n 
B 1 280 LEU 280 280 280 LEU LEU B . n 
B 1 281 VAL 281 281 281 VAL VAL B . n 
B 1 282 LYS 282 282 282 LYS LYS B . n 
B 1 283 ASN 283 283 283 ASN ASN B . n 
B 1 284 PRO 284 284 284 PRO PRO B . n 
B 1 285 HIS 285 285 285 HIS HIS B . n 
B 1 286 VAL 286 286 286 VAL VAL B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLN 288 288 288 GLN GLN B . n 
B 1 289 LYS 289 289 289 LYS LYS B . n 
B 1 290 ALA 290 290 290 ALA ALA B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 GLU 292 292 292 GLU GLU B . n 
B 1 293 GLU 293 293 293 GLU GLU B . n 
B 1 294 ALA 294 294 294 ALA ALA B . n 
B 1 295 ALA 295 295 295 ALA ALA B . n 
B 1 296 ARG 296 296 296 ARG ARG B . n 
B 1 297 ILE 297 297 297 ILE ILE B . n 
B 1 298 LEU 298 298 298 LEU LEU B . n 
B 1 299 VAL 299 299 299 VAL VAL B . n 
B 1 300 ASP 300 300 300 ASP ASP B . n 
B 1 301 PRO 301 301 301 PRO PRO B . n 
B 1 302 VAL 302 302 302 VAL VAL B . n 
B 1 303 PRO 303 303 303 PRO PRO B . n 
B 1 304 SER 304 304 304 SER SER B . n 
B 1 305 TYR 305 305 305 TYR TYR B . n 
B 1 306 LYS 306 306 306 LYS LYS B . n 
B 1 307 GLN 307 307 307 GLN GLN B . n 
B 1 308 VAL 308 308 308 VAL VAL B . n 
B 1 309 LYS 309 309 309 LYS LYS B . n 
B 1 310 GLN 310 310 310 GLN GLN B . n 
B 1 311 LEU 311 311 311 LEU LEU B . n 
B 1 312 LYS 312 312 312 LYS LYS B . n 
B 1 313 TYR 313 313 313 TYR TYR B . n 
B 1 314 VAL 314 314 314 VAL VAL B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 MET 316 316 316 MET MET B . n 
B 1 317 VAL 317 317 317 VAL VAL B . n 
B 1 318 LEU 318 318 318 LEU LEU B . n 
B 1 319 ASN 319 319 319 ASN ASN B . n 
B 1 320 GLU 320 320 320 GLU GLU B . n 
B 1 321 ALA 321 321 321 ALA ALA B . n 
B 1 322 LEU 322 322 322 LEU LEU B . n 
B 1 323 ARG 323 323 323 ARG ARG B . n 
B 1 324 LEU 324 324 324 LEU LEU B . n 
B 1 325 TRP 325 325 325 TRP TRP B . n 
B 1 326 PRO 326 326 326 PRO PRO B . n 
B 1 327 THR 327 327 327 THR THR B . n 
B 1 328 GLY 328 328 328 GLY GLY B . n 
B 1 329 PRO 329 329 329 PRO PRO B . n 
B 1 330 ALA 330 330 330 ALA ALA B . n 
B 1 331 PHE 331 331 331 PHE PHE B . n 
B 1 332 SER 332 332 332 SER SER B . n 
B 1 333 LEU 333 333 333 LEU LEU B . n 
B 1 334 TYR 334 334 334 TYR TYR B . n 
B 1 335 ALA 335 335 335 ALA ALA B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 GLU 337 337 337 GLU GLU B . n 
B 1 338 ASP 338 338 338 ASP ASP B . n 
B 1 339 THR 339 339 339 THR THR B . n 
B 1 340 VAL 340 340 340 VAL VAL B . n 
B 1 341 LEU 341 341 341 LEU LEU B . n 
B 1 342 GLY 342 342 342 GLY GLY B . n 
B 1 343 GLY 343 343 343 GLY GLY B . n 
B 1 344 GLU 344 344 344 GLU GLU B . n 
B 1 345 TYR 345 345 345 TYR TYR B . n 
B 1 346 PRO 346 346 346 PRO PRO B . n 
B 1 347 LEU 347 347 347 LEU LEU B . n 
B 1 348 GLU 348 348 348 GLU GLU B . n 
B 1 349 LYS 349 349 349 LYS LYS B . n 
B 1 350 GLY 350 350 350 GLY GLY B . n 
B 1 351 ASP 351 351 351 ASP ASP B . n 
B 1 352 GLU 352 352 352 GLU GLU B . n 
B 1 353 LEU 353 353 353 LEU LEU B . n 
B 1 354 MET 354 354 354 MET MET B . n 
B 1 355 VAL 355 355 355 VAL VAL B . n 
B 1 356 LEU 356 356 356 LEU LEU B . n 
B 1 357 ILE 357 357 357 ILE ILE B . n 
B 1 358 PRO 358 358 358 PRO PRO B . n 
B 1 359 GLN 359 359 359 GLN GLN B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 HIS 361 361 361 HIS HIS B . n 
B 1 362 ARG 362 362 362 ARG ARG B . n 
B 1 363 ASP 363 363 363 ASP ASP B . n 
B 1 364 LYS 364 364 364 LYS LYS B . n 
B 1 365 THR 365 365 365 THR THR B . n 
B 1 366 ILE 366 366 366 ILE ILE B . n 
B 1 367 TRP 367 367 367 TRP TRP B . n 
B 1 368 GLY 368 368 368 GLY GLY B . n 
B 1 369 ASP 369 369 369 ASP ASP B . n 
B 1 370 ASP 370 370 370 ASP ASP B . n 
B 1 371 VAL 371 371 371 VAL VAL B . n 
B 1 372 GLU 372 372 372 GLU GLU B . n 
B 1 373 GLU 373 373 373 GLU GLU B . n 
B 1 374 PHE 374 374 374 PHE PHE B . n 
B 1 375 ARG 375 375 375 ARG ARG B . n 
B 1 376 PRO 376 376 376 PRO PRO B . n 
B 1 377 GLU 377 377 377 GLU GLU B . n 
B 1 378 ARG 378 378 378 ARG ARG B . n 
B 1 379 PHE 379 379 379 PHE PHE B . n 
B 1 380 GLU 380 380 380 GLU GLU B . n 
B 1 381 ASN 381 381 381 ASN ASN B . n 
B 1 382 PRO 382 382 382 PRO PRO B . n 
B 1 383 SER 383 383 383 SER SER B . n 
B 1 384 ALA 384 384 384 ALA ALA B . n 
B 1 385 ILE 385 385 385 ILE ILE B . n 
B 1 386 PRO 386 386 386 PRO PRO B . n 
B 1 387 GLN 387 387 387 GLN GLN B . n 
B 1 388 HIS 388 388 388 HIS HIS B . n 
B 1 389 ALA 389 389 389 ALA ALA B . n 
B 1 390 PHE 390 390 390 PHE PHE B . n 
B 1 391 LYS 391 391 391 LYS LYS B . n 
B 1 392 PRO 392 392 392 PRO PRO B . n 
B 1 393 PHE 393 393 393 PHE PHE B . n 
B 1 394 GLY 394 394 394 GLY GLY B . n 
B 1 395 ASN 395 395 395 ASN ASN B . n 
B 1 396 GLY 396 396 396 GLY GLY B . n 
B 1 397 GLN 397 397 397 GLN GLN B . n 
B 1 398 ARG 398 398 398 ARG ARG B . n 
B 1 399 ALA 399 399 399 ALA ALA B . n 
B 1 400 CYS 400 400 400 CYS CYS B . n 
B 1 401 ILE 401 401 401 ILE ILE B . n 
B 1 402 GLY 402 402 402 GLY GLY B . n 
B 1 403 GLN 403 403 403 GLN GLN B . n 
B 1 404 GLN 404 404 404 GLN GLN B . n 
B 1 405 PHE 405 405 405 PHE PHE B . n 
B 1 406 ALA 406 406 406 ALA ALA B . n 
B 1 407 LEU 407 407 407 LEU LEU B . n 
B 1 408 HIS 408 408 408 HIS HIS B . n 
B 1 409 GLU 409 409 409 GLU GLU B . n 
B 1 410 ALA 410 410 410 ALA ALA B . n 
B 1 411 THR 411 411 411 THR THR B . n 
B 1 412 LEU 412 412 412 LEU LEU B . n 
B 1 413 VAL 413 413 413 VAL VAL B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 GLY 415 415 415 GLY GLY B . n 
B 1 416 MET 416 416 416 MET MET B . n 
B 1 417 MET 417 417 417 MET MET B . n 
B 1 418 LEU 418 418 418 LEU LEU B . n 
B 1 419 LYS 419 419 419 LYS LYS B . n 
B 1 420 HIS 420 420 420 HIS HIS B . n 
B 1 421 PHE 421 421 421 PHE PHE B . n 
B 1 422 ASP 422 422 422 ASP ASP B . n 
B 1 423 PHE 423 423 423 PHE PHE B . n 
B 1 424 GLU 424 424 424 GLU GLU B . n 
B 1 425 ASP 425 425 425 ASP ASP B . n 
B 1 426 HIS 426 426 426 HIS HIS B . n 
B 1 427 THR 427 427 427 THR THR B . n 
B 1 428 ASN 428 428 428 ASN ASN B . n 
B 1 429 TYR 429 429 429 TYR TYR B . n 
B 1 430 GLU 430 430 430 GLU GLU B . n 
B 1 431 LEU 431 431 431 LEU LEU B . n 
B 1 432 ASP 432 432 432 ASP ASP B . n 
B 1 433 ILE 433 433 433 ILE ILE B . n 
B 1 434 LYS 434 434 434 LYS LYS B . n 
B 1 435 GLU 435 435 435 GLU GLU B . n 
B 1 436 THR 436 436 436 THR THR B . n 
B 1 437 LEU 437 437 437 LEU LEU B . n 
B 1 438 THR 438 438 438 THR THR B . n 
B 1 439 LEU 439 439 439 LEU LEU B . n 
B 1 440 LYS 440 440 440 LYS LYS B . n 
B 1 441 PRO 441 441 441 PRO PRO B . n 
B 1 442 GLU 442 442 442 GLU GLU B . n 
B 1 443 GLY 443 443 443 GLY GLY B . n 
B 1 444 PHE 444 444 444 PHE PHE B . n 
B 1 445 VAL 445 445 445 VAL VAL B . n 
B 1 446 VAL 446 446 446 VAL VAL B . n 
B 1 447 LYS 447 447 447 LYS LYS B . n 
B 1 448 ALA 448 448 448 ALA ALA B . n 
B 1 449 LYS 449 449 449 LYS LYS B . n 
B 1 450 SER 450 450 450 SER SER B . n 
B 1 451 LYS 451 451 451 LYS LYS B . n 
B 1 452 GLN 452 452 452 GLN GLN B . n 
B 1 453 ILE 453 453 453 ILE ILE B . n 
B 1 454 PRO 454 454 454 PRO PRO B . n 
B 1 455 LEU 455 455 455 LEU LEU B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HEM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HEM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HEM 1   501 501  HEM HEM A . 
D 2 HEM 1   501 501  HEM HEM B . 
E 3 HOH 1   601 904  HOH HOH A . 
E 3 HOH 2   602 854  HOH HOH A . 
E 3 HOH 3   603 1020 HOH HOH A . 
E 3 HOH 4   604 261  HOH HOH A . 
E 3 HOH 5   605 315  HOH HOH A . 
E 3 HOH 6   606 972  HOH HOH A . 
E 3 HOH 7   607 431  HOH HOH A . 
E 3 HOH 8   608 167  HOH HOH A . 
E 3 HOH 9   609 866  HOH HOH A . 
E 3 HOH 10  610 324  HOH HOH A . 
E 3 HOH 11  611 1004 HOH HOH A . 
E 3 HOH 12  612 841  HOH HOH A . 
E 3 HOH 13  613 204  HOH HOH A . 
E 3 HOH 14  614 935  HOH HOH A . 
E 3 HOH 15  615 859  HOH HOH A . 
E 3 HOH 16  616 730  HOH HOH A . 
E 3 HOH 17  617 745  HOH HOH A . 
E 3 HOH 18  618 399  HOH HOH A . 
E 3 HOH 19  619 7    HOH HOH A . 
E 3 HOH 20  620 789  HOH HOH A . 
E 3 HOH 21  621 337  HOH HOH A . 
E 3 HOH 22  622 199  HOH HOH A . 
E 3 HOH 23  623 121  HOH HOH A . 
E 3 HOH 24  624 499  HOH HOH A . 
E 3 HOH 25  625 1219 HOH HOH A . 
E 3 HOH 26  626 239  HOH HOH A . 
E 3 HOH 27  627 334  HOH HOH A . 
E 3 HOH 28  628 898  HOH HOH A . 
E 3 HOH 29  629 242  HOH HOH A . 
E 3 HOH 30  630 198  HOH HOH A . 
E 3 HOH 31  631 508  HOH HOH A . 
E 3 HOH 32  632 219  HOH HOH A . 
E 3 HOH 33  633 1169 HOH HOH A . 
E 3 HOH 34  634 911  HOH HOH A . 
E 3 HOH 35  635 748  HOH HOH A . 
E 3 HOH 36  636 344  HOH HOH A . 
E 3 HOH 37  637 894  HOH HOH A . 
E 3 HOH 38  638 157  HOH HOH A . 
E 3 HOH 39  639 842  HOH HOH A . 
E 3 HOH 40  640 73   HOH HOH A . 
E 3 HOH 41  641 759  HOH HOH A . 
E 3 HOH 42  642 120  HOH HOH A . 
E 3 HOH 43  643 29   HOH HOH A . 
E 3 HOH 44  644 44   HOH HOH A . 
E 3 HOH 45  645 964  HOH HOH A . 
E 3 HOH 46  646 688  HOH HOH A . 
E 3 HOH 47  647 648  HOH HOH A . 
E 3 HOH 48  648 220  HOH HOH A . 
E 3 HOH 49  649 81   HOH HOH A . 
E 3 HOH 50  650 317  HOH HOH A . 
E 3 HOH 51  651 1048 HOH HOH A . 
E 3 HOH 52  652 831  HOH HOH A . 
E 3 HOH 53  653 294  HOH HOH A . 
E 3 HOH 54  654 24   HOH HOH A . 
E 3 HOH 55  655 892  HOH HOH A . 
E 3 HOH 56  656 369  HOH HOH A . 
E 3 HOH 57  657 70   HOH HOH A . 
E 3 HOH 58  658 177  HOH HOH A . 
E 3 HOH 59  659 5    HOH HOH A . 
E 3 HOH 60  660 182  HOH HOH A . 
E 3 HOH 61  661 429  HOH HOH A . 
E 3 HOH 62  662 130  HOH HOH A . 
E 3 HOH 63  663 83   HOH HOH A . 
E 3 HOH 64  664 271  HOH HOH A . 
E 3 HOH 65  665 180  HOH HOH A . 
E 3 HOH 66  666 827  HOH HOH A . 
E 3 HOH 67  667 292  HOH HOH A . 
E 3 HOH 68  668 908  HOH HOH A . 
E 3 HOH 69  669 262  HOH HOH A . 
E 3 HOH 70  670 78   HOH HOH A . 
E 3 HOH 71  671 1015 HOH HOH A . 
E 3 HOH 72  672 187  HOH HOH A . 
E 3 HOH 73  673 379  HOH HOH A . 
E 3 HOH 74  674 260  HOH HOH A . 
E 3 HOH 75  675 52   HOH HOH A . 
E 3 HOH 76  676 144  HOH HOH A . 
E 3 HOH 77  677 339  HOH HOH A . 
E 3 HOH 78  678 33   HOH HOH A . 
E 3 HOH 79  679 172  HOH HOH A . 
E 3 HOH 80  680 155  HOH HOH A . 
E 3 HOH 81  681 819  HOH HOH A . 
E 3 HOH 82  682 173  HOH HOH A . 
E 3 HOH 83  683 516  HOH HOH A . 
E 3 HOH 84  684 141  HOH HOH A . 
E 3 HOH 85  685 13   HOH HOH A . 
E 3 HOH 86  686 191  HOH HOH A . 
E 3 HOH 87  687 2    HOH HOH A . 
E 3 HOH 88  688 932  HOH HOH A . 
E 3 HOH 89  689 361  HOH HOH A . 
E 3 HOH 90  690 67   HOH HOH A . 
E 3 HOH 91  691 432  HOH HOH A . 
E 3 HOH 92  692 328  HOH HOH A . 
E 3 HOH 93  693 114  HOH HOH A . 
E 3 HOH 94  694 98   HOH HOH A . 
E 3 HOH 95  695 77   HOH HOH A . 
E 3 HOH 96  696 138  HOH HOH A . 
E 3 HOH 97  697 277  HOH HOH A . 
E 3 HOH 98  698 573  HOH HOH A . 
E 3 HOH 99  699 305  HOH HOH A . 
E 3 HOH 100 700 723  HOH HOH A . 
E 3 HOH 101 701 213  HOH HOH A . 
E 3 HOH 102 702 707  HOH HOH A . 
E 3 HOH 103 703 397  HOH HOH A . 
E 3 HOH 104 704 6    HOH HOH A . 
E 3 HOH 105 705 3    HOH HOH A . 
E 3 HOH 106 706 211  HOH HOH A . 
E 3 HOH 107 707 788  HOH HOH A . 
E 3 HOH 108 708 897  HOH HOH A . 
E 3 HOH 109 709 68   HOH HOH A . 
E 3 HOH 110 710 768  HOH HOH A . 
E 3 HOH 111 711 225  HOH HOH A . 
E 3 HOH 112 712 800  HOH HOH A . 
E 3 HOH 113 713 1174 HOH HOH A . 
E 3 HOH 114 714 61   HOH HOH A . 
E 3 HOH 115 715 82   HOH HOH A . 
E 3 HOH 116 716 186  HOH HOH A . 
E 3 HOH 117 717 89   HOH HOH A . 
E 3 HOH 118 718 178  HOH HOH A . 
E 3 HOH 119 719 299  HOH HOH A . 
E 3 HOH 120 720 301  HOH HOH A . 
E 3 HOH 121 721 165  HOH HOH A . 
E 3 HOH 122 722 538  HOH HOH A . 
E 3 HOH 123 723 238  HOH HOH A . 
E 3 HOH 124 724 273  HOH HOH A . 
E 3 HOH 125 725 581  HOH HOH A . 
E 3 HOH 126 726 820  HOH HOH A . 
E 3 HOH 127 727 214  HOH HOH A . 
E 3 HOH 128 728 1107 HOH HOH A . 
E 3 HOH 129 729 93   HOH HOH A . 
E 3 HOH 130 730 1068 HOH HOH A . 
E 3 HOH 131 731 153  HOH HOH A . 
E 3 HOH 132 732 323  HOH HOH A . 
E 3 HOH 133 733 269  HOH HOH A . 
E 3 HOH 134 734 858  HOH HOH A . 
E 3 HOH 135 735 62   HOH HOH A . 
E 3 HOH 136 736 808  HOH HOH A . 
E 3 HOH 137 737 434  HOH HOH A . 
E 3 HOH 138 738 331  HOH HOH A . 
E 3 HOH 139 739 268  HOH HOH A . 
E 3 HOH 140 740 133  HOH HOH A . 
E 3 HOH 141 741 456  HOH HOH A . 
E 3 HOH 142 742 257  HOH HOH A . 
E 3 HOH 143 743 30   HOH HOH A . 
E 3 HOH 144 744 185  HOH HOH A . 
E 3 HOH 145 745 38   HOH HOH A . 
E 3 HOH 146 746 770  HOH HOH A . 
E 3 HOH 147 747 304  HOH HOH A . 
E 3 HOH 148 748 224  HOH HOH A . 
E 3 HOH 149 749 869  HOH HOH A . 
E 3 HOH 150 750 45   HOH HOH A . 
E 3 HOH 151 751 664  HOH HOH A . 
E 3 HOH 152 752 1176 HOH HOH A . 
E 3 HOH 153 753 447  HOH HOH A . 
E 3 HOH 154 754 79   HOH HOH A . 
E 3 HOH 155 755 108  HOH HOH A . 
E 3 HOH 156 756 513  HOH HOH A . 
E 3 HOH 157 757 176  HOH HOH A . 
E 3 HOH 158 758 1078 HOH HOH A . 
E 3 HOH 159 759 696  HOH HOH A . 
E 3 HOH 160 760 534  HOH HOH A . 
E 3 HOH 161 761 201  HOH HOH A . 
E 3 HOH 162 762 183  HOH HOH A . 
E 3 HOH 163 763 348  HOH HOH A . 
E 3 HOH 164 764 86   HOH HOH A . 
E 3 HOH 165 765 236  HOH HOH A . 
E 3 HOH 166 766 609  HOH HOH A . 
E 3 HOH 167 767 494  HOH HOH A . 
E 3 HOH 168 768 278  HOH HOH A . 
E 3 HOH 169 769 286  HOH HOH A . 
E 3 HOH 170 770 970  HOH HOH A . 
E 3 HOH 171 771 377  HOH HOH A . 
E 3 HOH 172 772 376  HOH HOH A . 
E 3 HOH 173 773 250  HOH HOH A . 
E 3 HOH 174 774 758  HOH HOH A . 
E 3 HOH 175 775 956  HOH HOH A . 
E 3 HOH 176 776 291  HOH HOH A . 
E 3 HOH 177 777 1152 HOH HOH A . 
E 3 HOH 178 778 41   HOH HOH A . 
E 3 HOH 179 779 515  HOH HOH A . 
E 3 HOH 180 780 351  HOH HOH A . 
E 3 HOH 181 781 241  HOH HOH A . 
E 3 HOH 182 782 1170 HOH HOH A . 
E 3 HOH 183 783 353  HOH HOH A . 
E 3 HOH 184 784 215  HOH HOH A . 
E 3 HOH 185 785 861  HOH HOH A . 
E 3 HOH 186 786 791  HOH HOH A . 
E 3 HOH 187 787 848  HOH HOH A . 
E 3 HOH 188 788 163  HOH HOH A . 
E 3 HOH 189 789 729  HOH HOH A . 
E 3 HOH 190 790 771  HOH HOH A . 
E 3 HOH 191 791 743  HOH HOH A . 
E 3 HOH 192 792 209  HOH HOH A . 
E 3 HOH 193 793 1103 HOH HOH A . 
E 3 HOH 194 794 206  HOH HOH A . 
E 3 HOH 195 795 834  HOH HOH A . 
E 3 HOH 196 796 1040 HOH HOH A . 
E 3 HOH 197 797 111  HOH HOH A . 
E 3 HOH 198 798 856  HOH HOH A . 
E 3 HOH 199 799 330  HOH HOH A . 
E 3 HOH 200 800 880  HOH HOH A . 
E 3 HOH 201 801 297  HOH HOH A . 
E 3 HOH 202 802 360  HOH HOH A . 
E 3 HOH 203 803 868  HOH HOH A . 
E 3 HOH 204 804 229  HOH HOH A . 
E 3 HOH 205 805 249  HOH HOH A . 
E 3 HOH 206 806 571  HOH HOH A . 
E 3 HOH 207 807 200  HOH HOH A . 
E 3 HOH 208 808 415  HOH HOH A . 
E 3 HOH 209 809 902  HOH HOH A . 
E 3 HOH 210 810 585  HOH HOH A . 
E 3 HOH 211 811 544  HOH HOH A . 
E 3 HOH 212 812 480  HOH HOH A . 
E 3 HOH 213 813 813  HOH HOH A . 
E 3 HOH 214 814 792  HOH HOH A . 
E 3 HOH 215 815 701  HOH HOH A . 
E 3 HOH 216 816 1074 HOH HOH A . 
E 3 HOH 217 817 245  HOH HOH A . 
E 3 HOH 218 818 965  HOH HOH A . 
E 3 HOH 219 819 184  HOH HOH A . 
E 3 HOH 220 820 1012 HOH HOH A . 
E 3 HOH 221 821 559  HOH HOH A . 
E 3 HOH 222 822 818  HOH HOH A . 
E 3 HOH 223 823 1019 HOH HOH A . 
E 3 HOH 224 824 97   HOH HOH A . 
E 3 HOH 225 825 752  HOH HOH A . 
E 3 HOH 226 826 978  HOH HOH A . 
E 3 HOH 227 827 1073 HOH HOH A . 
E 3 HOH 228 828 899  HOH HOH A . 
E 3 HOH 229 829 733  HOH HOH A . 
E 3 HOH 230 830 161  HOH HOH A . 
E 3 HOH 231 831 962  HOH HOH A . 
E 3 HOH 232 832 876  HOH HOH A . 
E 3 HOH 233 833 636  HOH HOH A . 
E 3 HOH 234 834 833  HOH HOH A . 
E 3 HOH 235 835 746  HOH HOH A . 
E 3 HOH 236 836 226  HOH HOH A . 
E 3 HOH 237 837 433  HOH HOH A . 
E 3 HOH 238 838 896  HOH HOH A . 
E 3 HOH 239 839 385  HOH HOH A . 
E 3 HOH 240 840 884  HOH HOH A . 
E 3 HOH 241 841 314  HOH HOH A . 
E 3 HOH 242 842 782  HOH HOH A . 
E 3 HOH 243 843 1167 HOH HOH A . 
E 3 HOH 244 844 799  HOH HOH A . 
E 3 HOH 245 845 1007 HOH HOH A . 
E 3 HOH 246 846 753  HOH HOH A . 
E 3 HOH 247 847 969  HOH HOH A . 
E 3 HOH 248 848 312  HOH HOH A . 
E 3 HOH 249 849 550  HOH HOH A . 
E 3 HOH 250 850 998  HOH HOH A . 
E 3 HOH 251 851 801  HOH HOH A . 
E 3 HOH 252 852 205  HOH HOH A . 
E 3 HOH 253 853 210  HOH HOH A . 
E 3 HOH 254 854 396  HOH HOH A . 
E 3 HOH 255 855 914  HOH HOH A . 
E 3 HOH 256 856 444  HOH HOH A . 
E 3 HOH 257 857 1149 HOH HOH A . 
E 3 HOH 258 858 917  HOH HOH A . 
E 3 HOH 259 859 872  HOH HOH A . 
E 3 HOH 260 860 1036 HOH HOH A . 
E 3 HOH 261 861 1216 HOH HOH A . 
E 3 HOH 262 862 822  HOH HOH A . 
E 3 HOH 263 863 393  HOH HOH A . 
E 3 HOH 264 864 1161 HOH HOH A . 
E 3 HOH 265 865 1010 HOH HOH A . 
E 3 HOH 266 866 593  HOH HOH A . 
F 3 HOH 1   601 298  HOH HOH B . 
F 3 HOH 2   602 724  HOH HOH B . 
F 3 HOH 3   603 711  HOH HOH B . 
F 3 HOH 4   604 966  HOH HOH B . 
F 3 HOH 5   605 717  HOH HOH B . 
F 3 HOH 6   606 1090 HOH HOH B . 
F 3 HOH 7   607 779  HOH HOH B . 
F 3 HOH 8   608 263  HOH HOH B . 
F 3 HOH 9   609 829  HOH HOH B . 
F 3 HOH 10  610 436  HOH HOH B . 
F 3 HOH 11  611 71   HOH HOH B . 
F 3 HOH 12  612 96   HOH HOH B . 
F 3 HOH 13  613 356  HOH HOH B . 
F 3 HOH 14  614 910  HOH HOH B . 
F 3 HOH 15  615 999  HOH HOH B . 
F 3 HOH 16  616 147  HOH HOH B . 
F 3 HOH 17  617 445  HOH HOH B . 
F 3 HOH 18  618 520  HOH HOH B . 
F 3 HOH 19  619 366  HOH HOH B . 
F 3 HOH 20  620 326  HOH HOH B . 
F 3 HOH 21  621 272  HOH HOH B . 
F 3 HOH 22  622 19   HOH HOH B . 
F 3 HOH 23  623 769  HOH HOH B . 
F 3 HOH 24  624 958  HOH HOH B . 
F 3 HOH 25  625 287  HOH HOH B . 
F 3 HOH 26  626 132  HOH HOH B . 
F 3 HOH 27  627 1033 HOH HOH B . 
F 3 HOH 28  628 1110 HOH HOH B . 
F 3 HOH 29  629 302  HOH HOH B . 
F 3 HOH 30  630 309  HOH HOH B . 
F 3 HOH 31  631 441  HOH HOH B . 
F 3 HOH 32  632 523  HOH HOH B . 
F 3 HOH 33  633 1035 HOH HOH B . 
F 3 HOH 34  634 681  HOH HOH B . 
F 3 HOH 35  635 207  HOH HOH B . 
F 3 HOH 36  636 195  HOH HOH B . 
F 3 HOH 37  637 794  HOH HOH B . 
F 3 HOH 38  638 378  HOH HOH B . 
F 3 HOH 39  639 276  HOH HOH B . 
F 3 HOH 40  640 383  HOH HOH B . 
F 3 HOH 41  641 924  HOH HOH B . 
F 3 HOH 42  642 25   HOH HOH B . 
F 3 HOH 43  643 123  HOH HOH B . 
F 3 HOH 44  644 23   HOH HOH B . 
F 3 HOH 45  645 849  HOH HOH B . 
F 3 HOH 46  646 318  HOH HOH B . 
F 3 HOH 47  647 478  HOH HOH B . 
F 3 HOH 48  648 69   HOH HOH B . 
F 3 HOH 49  649 929  HOH HOH B . 
F 3 HOH 50  650 313  HOH HOH B . 
F 3 HOH 51  651 40   HOH HOH B . 
F 3 HOH 52  652 722  HOH HOH B . 
F 3 HOH 53  653 270  HOH HOH B . 
F 3 HOH 54  654 137  HOH HOH B . 
F 3 HOH 55  655 933  HOH HOH B . 
F 3 HOH 56  656 781  HOH HOH B . 
F 3 HOH 57  657 22   HOH HOH B . 
F 3 HOH 58  658 1049 HOH HOH B . 
F 3 HOH 59  659 365  HOH HOH B . 
F 3 HOH 60  660 106  HOH HOH B . 
F 3 HOH 61  661 1114 HOH HOH B . 
F 3 HOH 62  662 764  HOH HOH B . 
F 3 HOH 63  663 483  HOH HOH B . 
F 3 HOH 64  664 644  HOH HOH B . 
F 3 HOH 65  665 1002 HOH HOH B . 
F 3 HOH 66  666 761  HOH HOH B . 
F 3 HOH 67  667 1202 HOH HOH B . 
F 3 HOH 68  668 169  HOH HOH B . 
F 3 HOH 69  669 35   HOH HOH B . 
F 3 HOH 70  670 807  HOH HOH B . 
F 3 HOH 71  671 46   HOH HOH B . 
F 3 HOH 72  672 170  HOH HOH B . 
F 3 HOH 73  673 503  HOH HOH B . 
F 3 HOH 74  674 355  HOH HOH B . 
F 3 HOH 75  675 145  HOH HOH B . 
F 3 HOH 76  676 51   HOH HOH B . 
F 3 HOH 77  677 410  HOH HOH B . 
F 3 HOH 78  678 116  HOH HOH B . 
F 3 HOH 79  679 479  HOH HOH B . 
F 3 HOH 80  680 181  HOH HOH B . 
F 3 HOH 81  681 49   HOH HOH B . 
F 3 HOH 82  682 502  HOH HOH B . 
F 3 HOH 83  683 110  HOH HOH B . 
F 3 HOH 84  684 280  HOH HOH B . 
F 3 HOH 85  685 94   HOH HOH B . 
F 3 HOH 86  686 31   HOH HOH B . 
F 3 HOH 87  687 107  HOH HOH B . 
F 3 HOH 88  688 36   HOH HOH B . 
F 3 HOH 89  689 194  HOH HOH B . 
F 3 HOH 90  690 1133 HOH HOH B . 
F 3 HOH 91  691 974  HOH HOH B . 
F 3 HOH 92  692 233  HOH HOH B . 
F 3 HOH 93  693 725  HOH HOH B . 
F 3 HOH 94  694 139  HOH HOH B . 
F 3 HOH 95  695 54   HOH HOH B . 
F 3 HOH 96  696 112  HOH HOH B . 
F 3 HOH 97  697 66   HOH HOH B . 
F 3 HOH 98  698 113  HOH HOH B . 
F 3 HOH 99  699 87   HOH HOH B . 
F 3 HOH 100 700 162  HOH HOH B . 
F 3 HOH 101 701 592  HOH HOH B . 
F 3 HOH 102 702 873  HOH HOH B . 
F 3 HOH 103 703 450  HOH HOH B . 
F 3 HOH 104 704 217  HOH HOH B . 
F 3 HOH 105 705 289  HOH HOH B . 
F 3 HOH 106 706 115  HOH HOH B . 
F 3 HOH 107 707 159  HOH HOH B . 
F 3 HOH 108 708 18   HOH HOH B . 
F 3 HOH 109 709 197  HOH HOH B . 
F 3 HOH 110 710 266  HOH HOH B . 
F 3 HOH 111 711 506  HOH HOH B . 
F 3 HOH 112 712 570  HOH HOH B . 
F 3 HOH 113 713 751  HOH HOH B . 
F 3 HOH 114 714 59   HOH HOH B . 
F 3 HOH 115 715 953  HOH HOH B . 
F 3 HOH 116 716 285  HOH HOH B . 
F 3 HOH 117 717 308  HOH HOH B . 
F 3 HOH 118 718 12   HOH HOH B . 
F 3 HOH 119 719 227  HOH HOH B . 
F 3 HOH 120 720 32   HOH HOH B . 
F 3 HOH 121 721 221  HOH HOH B . 
F 3 HOH 122 722 103  HOH HOH B . 
F 3 HOH 123 723 901  HOH HOH B . 
F 3 HOH 124 724 128  HOH HOH B . 
F 3 HOH 125 725 357  HOH HOH B . 
F 3 HOH 126 726 659  HOH HOH B . 
F 3 HOH 127 727 60   HOH HOH B . 
F 3 HOH 128 728 346  HOH HOH B . 
F 3 HOH 129 729 58   HOH HOH B . 
F 3 HOH 130 730 275  HOH HOH B . 
F 3 HOH 131 731 1023 HOH HOH B . 
F 3 HOH 132 732 811  HOH HOH B . 
F 3 HOH 133 733 719  HOH HOH B . 
F 3 HOH 134 734 586  HOH HOH B . 
F 3 HOH 135 735 212  HOH HOH B . 
F 3 HOH 136 736 64   HOH HOH B . 
F 3 HOH 137 737 57   HOH HOH B . 
F 3 HOH 138 738 595  HOH HOH B . 
F 3 HOH 139 739 247  HOH HOH B . 
F 3 HOH 140 740 350  HOH HOH B . 
F 3 HOH 141 741 363  HOH HOH B . 
F 3 HOH 142 742 945  HOH HOH B . 
F 3 HOH 143 743 166  HOH HOH B . 
F 3 HOH 144 744 140  HOH HOH B . 
F 3 HOH 145 745 152  HOH HOH B . 
F 3 HOH 146 746 406  HOH HOH B . 
F 3 HOH 147 747 846  HOH HOH B . 
F 3 HOH 148 748 192  HOH HOH B . 
F 3 HOH 149 749 264  HOH HOH B . 
F 3 HOH 150 750 143  HOH HOH B . 
F 3 HOH 151 751 222  HOH HOH B . 
F 3 HOH 152 752 786  HOH HOH B . 
F 3 HOH 153 753 430  HOH HOH B . 
F 3 HOH 154 754 118  HOH HOH B . 
F 3 HOH 155 755 150  HOH HOH B . 
F 3 HOH 156 756 1069 HOH HOH B . 
F 3 HOH 157 757 774  HOH HOH B . 
F 3 HOH 158 758 76   HOH HOH B . 
F 3 HOH 159 759 80   HOH HOH B . 
F 3 HOH 160 760 101  HOH HOH B . 
F 3 HOH 161 761 423  HOH HOH B . 
F 3 HOH 162 762 258  HOH HOH B . 
F 3 HOH 163 763 373  HOH HOH B . 
F 3 HOH 164 764 15   HOH HOH B . 
F 3 HOH 165 765 577  HOH HOH B . 
F 3 HOH 166 766 500  HOH HOH B . 
F 3 HOH 167 767 203  HOH HOH B . 
F 3 HOH 168 768 256  HOH HOH B . 
F 3 HOH 169 769 660  HOH HOH B . 
F 3 HOH 170 770 338  HOH HOH B . 
F 3 HOH 171 771 243  HOH HOH B . 
F 3 HOH 172 772 1014 HOH HOH B . 
F 3 HOH 173 773 319  HOH HOH B . 
F 3 HOH 174 774 451  HOH HOH B . 
F 3 HOH 175 775 95   HOH HOH B . 
F 3 HOH 176 776 940  HOH HOH B . 
F 3 HOH 177 777 736  HOH HOH B . 
F 3 HOH 178 778 85   HOH HOH B . 
F 3 HOH 179 779 465  HOH HOH B . 
F 3 HOH 180 780 321  HOH HOH B . 
F 3 HOH 181 781 763  HOH HOH B . 
F 3 HOH 182 782 862  HOH HOH B . 
F 3 HOH 183 783 117  HOH HOH B . 
F 3 HOH 184 784 490  HOH HOH B . 
F 3 HOH 185 785 750  HOH HOH B . 
F 3 HOH 186 786 704  HOH HOH B . 
F 3 HOH 187 787 955  HOH HOH B . 
F 3 HOH 188 788 555  HOH HOH B . 
F 3 HOH 189 789 56   HOH HOH B . 
F 3 HOH 190 790 91   HOH HOH B . 
F 3 HOH 191 791 709  HOH HOH B . 
F 3 HOH 192 792 1077 HOH HOH B . 
F 3 HOH 193 793 104  HOH HOH B . 
F 3 HOH 194 794 925  HOH HOH B . 
F 3 HOH 195 795 691  HOH HOH B . 
F 3 HOH 196 796 171  HOH HOH B . 
F 3 HOH 197 797 720  HOH HOH B . 
F 3 HOH 198 798 237  HOH HOH B . 
F 3 HOH 199 799 218  HOH HOH B . 
F 3 HOH 200 800 871  HOH HOH B . 
F 3 HOH 201 801 142  HOH HOH B . 
F 3 HOH 202 802 284  HOH HOH B . 
F 3 HOH 203 803 703  HOH HOH B . 
F 3 HOH 204 804 119  HOH HOH B . 
F 3 HOH 205 805 668  HOH HOH B . 
F 3 HOH 206 806 136  HOH HOH B . 
F 3 HOH 207 807 727  HOH HOH B . 
F 3 HOH 208 808 823  HOH HOH B . 
F 3 HOH 209 809 411  HOH HOH B . 
F 3 HOH 210 810 619  HOH HOH B . 
F 3 HOH 211 811 53   HOH HOH B . 
F 3 HOH 212 812 963  HOH HOH B . 
F 3 HOH 213 813 228  HOH HOH B . 
F 3 HOH 214 814 900  HOH HOH B . 
F 3 HOH 215 815 787  HOH HOH B . 
F 3 HOH 216 816 773  HOH HOH B . 
F 3 HOH 217 817 160  HOH HOH B . 
F 3 HOH 218 818 514  HOH HOH B . 
F 3 HOH 219 819 839  HOH HOH B . 
F 3 HOH 220 820 1220 HOH HOH B . 
F 3 HOH 221 821 443  HOH HOH B . 
F 3 HOH 222 822 154  HOH HOH B . 
F 3 HOH 223 823 852  HOH HOH B . 
F 3 HOH 224 824 457  HOH HOH B . 
F 3 HOH 225 825 1034 HOH HOH B . 
F 3 HOH 226 826 296  HOH HOH B . 
F 3 HOH 227 827 948  HOH HOH B . 
F 3 HOH 228 828 251  HOH HOH B . 
F 3 HOH 229 829 254  HOH HOH B . 
F 3 HOH 230 830 530  HOH HOH B . 
F 3 HOH 231 831 805  HOH HOH B . 
F 3 HOH 232 832 928  HOH HOH B . 
F 3 HOH 233 833 1186 HOH HOH B . 
F 3 HOH 234 834 1011 HOH HOH B . 
F 3 HOH 235 835 882  HOH HOH B . 
F 3 HOH 236 836 830  HOH HOH B . 
F 3 HOH 237 837 576  HOH HOH B . 
F 3 HOH 238 838 368  HOH HOH B . 
F 3 HOH 239 839 498  HOH HOH B . 
F 3 HOH 240 840 785  HOH HOH B . 
F 3 HOH 241 841 984  HOH HOH B . 
F 3 HOH 242 842 546  HOH HOH B . 
F 3 HOH 243 843 453  HOH HOH B . 
F 3 HOH 244 844 347  HOH HOH B . 
F 3 HOH 245 845 656  HOH HOH B . 
F 3 HOH 246 846 836  HOH HOH B . 
F 3 HOH 247 847 738  HOH HOH B . 
F 3 HOH 248 848 1102 HOH HOH B . 
F 3 HOH 249 849 336  HOH HOH B . 
F 3 HOH 250 850 352  HOH HOH B . 
F 3 HOH 251 851 793  HOH HOH B . 
F 3 HOH 252 852 28   HOH HOH B . 
F 3 HOH 253 853 886  HOH HOH B . 
F 3 HOH 254 854 1177 HOH HOH B . 
F 3 HOH 255 855 1178 HOH HOH B . 
F 3 HOH 256 856 341  HOH HOH B . 
F 3 HOH 257 857 543  HOH HOH B . 
F 3 HOH 258 858 755  HOH HOH B . 
F 3 HOH 259 859 1128 HOH HOH B . 
F 3 HOH 260 860 604  HOH HOH B . 
F 3 HOH 261 861 740  HOH HOH B . 
F 3 HOH 262 862 482  HOH HOH B . 
F 3 HOH 263 863 1154 HOH HOH B . 
F 3 HOH 264 864 857  HOH HOH B . 
F 3 HOH 265 865 996  HOH HOH B . 
F 3 HOH 266 866 747  HOH HOH B . 
F 3 HOH 267 867 1134 HOH HOH B . 
F 3 HOH 268 868 322  HOH HOH B . 
F 3 HOH 269 869 803  HOH HOH B . 
F 3 HOH 270 870 706  HOH HOH B . 
F 3 HOH 271 871 442  HOH HOH B . 
F 3 HOH 272 872 960  HOH HOH B . 
F 3 HOH 273 873 885  HOH HOH B . 
F 3 HOH 274 874 1031 HOH HOH B . 
F 3 HOH 275 875 283  HOH HOH B . 
F 3 HOH 276 876 327  HOH HOH B . 
F 3 HOH 277 877 1189 HOH HOH B . 
F 3 HOH 278 878 281  HOH HOH B . 
F 3 HOH 279 879 388  HOH HOH B . 
F 3 HOH 280 880 947  HOH HOH B . 
F 3 HOH 281 881 741  HOH HOH B . 
F 3 HOH 282 882 1042 HOH HOH B . 
F 3 HOH 283 883 1118 HOH HOH B . 
F 3 HOH 284 884 340  HOH HOH B . 
F 3 HOH 285 885 864  HOH HOH B . 
F 3 HOH 286 886 968  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ARG 255 ? CG  ? A ARG 255 CG  
2 1 Y 1 A ARG 255 ? CD  ? A ARG 255 CD  
3 1 Y 1 A ARG 255 ? NE  ? A ARG 255 NE  
4 1 Y 1 A ARG 255 ? CZ  ? A ARG 255 CZ  
5 1 Y 1 A ARG 255 ? NH1 ? A ARG 255 NH1 
6 1 Y 1 A ARG 255 ? NH2 ? A ARG 255 NH2 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0415 ? 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        ? 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        ? 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.513 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KGP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.914 
_cell.length_a_esd                 ? 
_cell.length_b                     145.713 
_cell.length_b_esd                 ? 
_cell.length_c                     63.233 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9KGP 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9KGP 
_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             2.58 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.34 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Magnesium chloride hexahydrate, 0.1 M HEPES pH 7.5, 25% w/v Polyethylene glycol 3,350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-06 
_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   0.97919 
_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                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97919 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KGP 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.52 
_reflns.d_resolution_low                               72.82 
_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                                     156546 
_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                           97 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_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                                    1.52 
_reflns_shell.d_res_low                                     1.56 
_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                             156546 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.996 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.0 
_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]                            0.17 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.54 
_refine.aniso_B[2][2]                            -0.99 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.93 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               23.711 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.946 
_refine.correlation_coeff_Fo_to_Fc_free          0.925 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9KGP 
_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                            1.52 
_refine.ls_d_res_low                             72.82 
_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                     148647 
_refine.ls_number_reflns_R_free                  7852 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.87 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.225 
_refine.ls_R_factor_R_free                       0.227 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.221 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          MAD 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.097 
_refine.pdbx_overall_ESU_R_Free                  0.099 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             4.695 
_refine.overall_SU_ML                            0.146 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.52 
_refine_hist.d_res_low                        72.82 
_refine_hist.number_atoms_solvent             552 
_refine_hist.number_atoms_total               7930 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        7378 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  0.012  7560  ? r_bond_refined_d             ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  7152  ? r_bond_other_d               ? ? ? 
'X-RAY DIFFRACTION' ? 1.558  1.680  10249 ? r_angle_refined_deg          ? ? ? 
'X-RAY DIFFRACTION' ? 0.507  1.593  16526 ? r_angle_other_deg            ? ? ? 
'X-RAY DIFFRACTION' ? 6.734  5.000  904   ? r_dihedral_angle_1_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 6.183  5.000  39    ? r_dihedral_angle_2_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 15.086 10.000 1347  ? r_dihedral_angle_3_deg       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 0.076  0.200  1086  ? r_chiral_restr               ? ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  8845  ? r_gen_planes_refined         ? ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  1703  ? r_gen_planes_other           ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? ? 
'X-RAY DIFFRACTION' ? 2.281  2.341  3622  ? r_mcbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 2.278  2.341  3622  ? r_mcbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? 3.407  4.201  4524  ? r_mcangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 3.407  4.201  4525  ? r_mcangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 2.947  2.653  3938  ? r_scbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 2.947  2.654  3936  ? r_scbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 4.686  4.707  5725  ? r_scangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 6.615  23.50  8905  ? r_long_range_B_refined       ? ? ? 
'X-RAY DIFFRACTION' ? 6.530  23.20  8776  ? r_long_range_B_other         ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? ? 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          1.520 
_refine_ls_shell.d_res_low                           1.559 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                554 
_refine_ls_shell.number_reflns_R_work                10737 
_refine_ls_shell.percent_reflns_obs                  94.89 
_refine_ls_shell.percent_reflns_R_free               ? 
_refine_ls_shell.R_factor_all                        ? 
_refine_ls_shell.R_factor_obs                        ? 
_refine_ls_shell.R_factor_R_free_error               ? 
_refine_ls_shell.R_factor_R_work                     0.393 
_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.correlation_coeff_Fo_to_Fc          ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free     ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free   ? 
_refine_ls_shell.pdbx_total_number_of_bins_used      20 
_refine_ls_shell.pdbx_phase_error                    ? 
_refine_ls_shell.pdbx_fsc_work                       ? 
_refine_ls_shell.pdbx_fsc_free                       ? 
_refine_ls_shell.R_factor_R_free                     0.401 
# 
_struct.entry_id                     9KGP 
_struct.title                        
'The structure of natural P450BM3-H derived from Bacillus megaterium for catalyzing the steroid DHEA' 
_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        9KGP 
_struct_keywords.text            
'Oxidoreductase, cytochrome P450BM3, heme-binding domain, steroid compound, dehydroepiandrosterone DHEA' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CPXB_PRIM2 
_struct_ref.pdbx_db_accession          P14779 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRD
FAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_struct_ref.pdbx_align_begin           2 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9KGP A 1 ? 455 ? P14779 2 ? 456 ? 1 455 
2 1 9KGP B 1 ? 455 ? P14779 2 ? 456 ? 1 455 
# 
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 9KGP GLY A 74  ? UNP P14779 ALA 75  conflict 74  1  
1 9KGP VAL A 87  ? UNP P14779 PHE 88  conflict 87  2  
1 9KGP ILE A 127 ? UNP P14779 VAL 128 conflict 127 3  
1 9KGP ILE A 184 ? UNP P14779 ALA 185 conflict 184 4  
1 9KGP ASP A 207 ? UNP P14779 GLU 208 conflict 207 5  
1 9KGP GLY A 263 ? UNP P14779 ILE 264 conflict 263 6  
1 9KGP GLY A 264 ? UNP P14779 ALA 265 conflict 264 7  
1 9KGP ILE A 297 ? UNP P14779 VAL 298 conflict 297 8  
1 9KGP GLY A 328 ? UNP P14779 ALA 329 conflict 328 9  
1 9KGP GLN A 452 ? UNP P14779 LYS 453 conflict 452 10 
2 9KGP GLY B 74  ? UNP P14779 ALA 75  conflict 74  11 
2 9KGP VAL B 87  ? UNP P14779 PHE 88  conflict 87  12 
2 9KGP ILE B 127 ? UNP P14779 VAL 128 conflict 127 13 
2 9KGP ILE B 184 ? UNP P14779 ALA 185 conflict 184 14 
2 9KGP ASP B 207 ? UNP P14779 GLU 208 conflict 207 15 
2 9KGP GLY B 263 ? UNP P14779 ILE 264 conflict 263 16 
2 9KGP GLY B 264 ? UNP P14779 ALA 265 conflict 264 17 
2 9KGP ILE B 297 ? UNP P14779 VAL 298 conflict 297 18 
2 9KGP GLY B 328 ? UNP P14779 ALA 329 conflict 328 19 
2 9KGP GLN B 452 ? UNP P14779 LYS 453 conflict 452 20 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly              ?    dimeric   2 
2 author_and_software_defined_assembly PISA monomeric 1 
3 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
2 'ABSA (A^2)' 1260  ? 
2 MORE         -21   ? 
2 'SSA (A^2)'  19580 ? 
3 'ABSA (A^2)' 1270  ? 
3 MORE         -21   ? 
3 'SSA (A^2)'  19500 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F 
2 1 A,C,E       
3 1 B,D,F       
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'native gel electrophoresis' 
_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 PHE A 11  ? LYS A 15  ? PHE A 11  LYS A 15  5 ? 5  
HELX_P HELX_P2  AA2 ASN A 16  ? ASN A 21  ? ASN A 16  ASN A 21  5 ? 6  
HELX_P HELX_P3  AA3 LYS A 24  ? GLY A 37  ? LYS A 24  GLY A 37  1 ? 14 
HELX_P HELX_P4  AA4 SER A 54  ? CYS A 62  ? SER A 54  CYS A 62  1 ? 9  
HELX_P HELX_P5  AA5 SER A 72  ? GLY A 83  ? SER A 72  GLY A 83  1 ? 12 
HELX_P HELX_P6  AA6 GLU A 93  ? LEU A 104 ? GLU A 93  LEU A 104 1 ? 12 
HELX_P HELX_P7  AA7 PRO A 105 ? PHE A 107 ? PRO A 105 PHE A 107 5 ? 3  
HELX_P HELX_P8  AA8 SER A 108 ? ARG A 132 ? SER A 108 ARG A 132 1 ? 25 
HELX_P HELX_P9  AA9 VAL A 141 ? ASN A 159 ? VAL A 141 ASN A 159 1 ? 19 
HELX_P HELX_P10 AB1 ASN A 163 ? ARG A 167 ? ASN A 163 ARG A 167 5 ? 5  
HELX_P HELX_P11 AB2 HIS A 171 ? LEU A 188 ? HIS A 171 LEU A 188 1 ? 18 
HELX_P HELX_P12 AB3 ASP A 195 ? ALA A 197 ? ASP A 195 ALA A 197 5 ? 3  
HELX_P HELX_P13 AB4 TYR A 198 ? GLY A 227 ? TYR A 198 GLY A 227 1 ? 30 
HELX_P HELX_P14 AB5 ASP A 232 ? GLY A 240 ? ASP A 232 GLY A 240 1 ? 9  
HELX_P HELX_P15 AB6 ASP A 250 ? GLY A 265 ? ASP A 250 GLY A 265 1 ? 16 
HELX_P HELX_P16 AB7 HIS A 266 ? ASN A 283 ? HIS A 266 ASN A 283 1 ? 18 
HELX_P HELX_P17 AB8 ASN A 283 ? LEU A 298 ? ASN A 283 LEU A 298 1 ? 16 
HELX_P HELX_P18 AB9 SER A 304 ? LYS A 309 ? SER A 304 LYS A 309 1 ? 6  
HELX_P HELX_P19 AC1 LEU A 311 ? TRP A 325 ? LEU A 311 TRP A 325 1 ? 15 
HELX_P HELX_P20 AC2 ILE A 357 ? HIS A 361 ? ILE A 357 HIS A 361 1 ? 5  
HELX_P HELX_P21 AC3 ASP A 363 ? GLY A 368 ? ASP A 363 GLY A 368 1 ? 6  
HELX_P HELX_P22 AC4 ARG A 375 ? GLU A 380 ? ARG A 375 GLU A 380 5 ? 6  
HELX_P HELX_P23 AC5 ASN A 381 ? ILE A 385 ? ASN A 381 ILE A 385 5 ? 5  
HELX_P HELX_P24 AC6 ASN A 395 ? ALA A 399 ? ASN A 395 ALA A 399 5 ? 5  
HELX_P HELX_P25 AC7 GLY A 402 ? HIS A 420 ? GLY A 402 HIS A 420 1 ? 19 
HELX_P HELX_P26 AC8 PHE B 11  ? LYS B 15  ? PHE B 11  LYS B 15  5 ? 5  
HELX_P HELX_P27 AC9 ASN B 16  ? ASN B 21  ? ASN B 16  ASN B 21  5 ? 6  
HELX_P HELX_P28 AD1 LYS B 24  ? GLY B 37  ? LYS B 24  GLY B 37  1 ? 14 
HELX_P HELX_P29 AD2 SER B 54  ? CYS B 62  ? SER B 54  CYS B 62  1 ? 9  
HELX_P HELX_P30 AD3 SER B 72  ? GLY B 83  ? SER B 72  GLY B 83  1 ? 12 
HELX_P HELX_P31 AD4 GLU B 93  ? LEU B 104 ? GLU B 93  LEU B 104 1 ? 12 
HELX_P HELX_P32 AD5 PRO B 105 ? PHE B 107 ? PRO B 105 PHE B 107 5 ? 3  
HELX_P HELX_P33 AD6 SER B 108 ? ARG B 132 ? SER B 108 ARG B 132 1 ? 25 
HELX_P HELX_P34 AD7 VAL B 141 ? ASN B 159 ? VAL B 141 ASN B 159 1 ? 19 
HELX_P HELX_P35 AD8 ASN B 163 ? ARG B 167 ? ASN B 163 ARG B 167 5 ? 5  
HELX_P HELX_P36 AD9 HIS B 171 ? LEU B 188 ? HIS B 171 LEU B 188 1 ? 18 
HELX_P HELX_P37 AE1 ASP B 195 ? ALA B 197 ? ASP B 195 ALA B 197 5 ? 3  
HELX_P HELX_P38 AE2 TYR B 198 ? SER B 226 ? TYR B 198 SER B 226 1 ? 29 
HELX_P HELX_P39 AE3 ASP B 232 ? GLY B 240 ? ASP B 232 GLY B 240 1 ? 9  
HELX_P HELX_P40 AE4 ASP B 250 ? GLY B 265 ? ASP B 250 GLY B 265 1 ? 16 
HELX_P HELX_P41 AE5 HIS B 266 ? ASN B 283 ? HIS B 266 ASN B 283 1 ? 18 
HELX_P HELX_P42 AE6 ASN B 283 ? LEU B 298 ? ASN B 283 LEU B 298 1 ? 16 
HELX_P HELX_P43 AE7 SER B 304 ? GLN B 310 ? SER B 304 GLN B 310 1 ? 7  
HELX_P HELX_P44 AE8 LEU B 311 ? TRP B 325 ? LEU B 311 TRP B 325 1 ? 15 
HELX_P HELX_P45 AE9 ILE B 357 ? HIS B 361 ? ILE B 357 HIS B 361 1 ? 5  
HELX_P HELX_P46 AF1 ASP B 363 ? GLY B 368 ? ASP B 363 GLY B 368 1 ? 6  
HELX_P HELX_P47 AF2 ARG B 375 ? GLU B 380 ? ARG B 375 GLU B 380 5 ? 6  
HELX_P HELX_P48 AF3 ASN B 381 ? ILE B 385 ? ASN B 381 ILE B 385 5 ? 5  
HELX_P HELX_P49 AF4 ASN B 395 ? ALA B 399 ? ASN B 395 ALA B 399 5 ? 5  
HELX_P HELX_P50 AF5 GLY B 402 ? HIS B 420 ? GLY B 402 HIS B 420 1 ? 19 
# 
_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 
metalc1 metalc ? ? A CYS 400 SG ? ? ? 1_555 C HEM . FE ? ? A CYS 400 A HEM 501 1_555 ? ? ? ? ? ? ? 2.159 ? ? 
metalc2 metalc ? ? B CYS 400 SG ? ? ? 1_555 D HEM . FE ? ? B CYS 400 B HEM 501 1_555 ? ? ? ? ? ? ? 2.196 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NA ? C HEM . ? A HEM 501 ? 1_555 102.7 ? 
2  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 90.8  ? 
3  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 85.4  ? 
4  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 88.3  ? 
5  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 168.4 ? 
6  NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 90.9  ? 
7  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 94.4  ? 
8  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 90.0  ? 
9  NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 173.8 ? 
10 NC ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 92.7  ? 
11 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NA ? D HEM . ? B HEM 501 ? 1_555 102.1 ? 
12 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NB ? D HEM . ? B HEM 501 ? 1_555 89.8  ? 
13 NA ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NB ? D HEM . ? B HEM 501 ? 1_555 90.8  ? 
14 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NC ? D HEM . ? B HEM 501 ? 1_555 84.4  ? 
15 NA ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NC ? D HEM . ? B HEM 501 ? 1_555 173.4 ? 
16 NB ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NC ? D HEM . ? B HEM 501 ? 1_555 87.8  ? 
17 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 95.8  ? 
18 NA ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 89.5  ? 
19 NB ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 174.2 ? 
20 NC ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 91.3  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
AA8 ? 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      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 39  ? ALA A 44  ? ILE A 39  ALA A 44  
AA1 2 ARG A 47  ? LEU A 52  ? ARG A 47  LEU A 52  
AA1 3 GLU A 352 ? LEU A 356 ? GLU A 352 LEU A 356 
AA1 4 ALA A 330 ? ALA A 335 ? ALA A 330 ALA A 335 
AA1 5 PHE A 67  ? ASN A 70  ? PHE A 67  ASN A 70  
AA2 1 ILE A 139 ? GLU A 140 ? ILE A 139 GLU A 140 
AA2 2 VAL A 445 ? SER A 450 ? VAL A 445 SER A 450 
AA2 3 PHE A 421 ? GLU A 424 ? PHE A 421 GLU A 424 
AA3 1 THR A 339 ? LEU A 341 ? THR A 339 LEU A 341 
AA3 2 TYR A 345 ? LEU A 347 ? TYR A 345 LEU A 347 
AA4 1 ILE A 433 ? GLU A 435 ? ILE A 433 GLU A 435 
AA4 2 LEU A 439 ? PRO A 441 ? LEU A 439 PRO A 441 
AA5 1 ILE B 39  ? ALA B 44  ? ILE B 39  ALA B 44  
AA5 2 ARG B 47  ? LEU B 52  ? ARG B 47  LEU B 52  
AA5 3 GLU B 352 ? LEU B 356 ? GLU B 352 LEU B 356 
AA5 4 ALA B 330 ? ALA B 335 ? ALA B 330 ALA B 335 
AA5 5 PHE B 67  ? ASN B 70  ? PHE B 67  ASN B 70  
AA6 1 ILE B 139 ? GLU B 140 ? ILE B 139 GLU B 140 
AA6 2 VAL B 445 ? SER B 450 ? VAL B 445 SER B 450 
AA6 3 PHE B 421 ? GLU B 424 ? PHE B 421 GLU B 424 
AA7 1 THR B 339 ? LEU B 341 ? THR B 339 LEU B 341 
AA7 2 TYR B 345 ? LEU B 347 ? TYR B 345 LEU B 347 
AA8 1 ILE B 433 ? GLU B 435 ? ILE B 433 GLU B 435 
AA8 2 LEU B 439 ? PRO B 441 ? LEU B 439 PRO B 441 
# 
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 PHE A 42  ? N PHE A 42  O THR A 49  ? O THR A 49  
AA1 2 3 N LEU A 52  ? N LEU A 52  O MET A 354 ? O MET A 354 
AA1 3 4 O VAL A 355 ? O VAL A 355 N PHE A 331 ? N PHE A 331 
AA1 4 5 O SER A 332 ? O SER A 332 N ASN A 70  ? N ASN A 70  
AA2 1 2 N ILE A 139 ? N ILE A 139 O VAL A 446 ? O VAL A 446 
AA2 2 3 O LYS A 449 ? O LYS A 449 N ASP A 422 ? N ASP A 422 
AA3 1 2 N THR A 339 ? N THR A 339 O LEU A 347 ? O LEU A 347 
AA4 1 2 N LYS A 434 ? N LYS A 434 O LYS A 440 ? O LYS A 440 
AA5 1 2 N PHE B 42  ? N PHE B 42  O THR B 49  ? O THR B 49  
AA5 2 3 N LEU B 52  ? N LEU B 52  O MET B 354 ? O MET B 354 
AA5 3 4 O VAL B 355 ? O VAL B 355 N PHE B 331 ? N PHE B 331 
AA5 4 5 O SER B 332 ? O SER B 332 N ASN B 70  ? N ASN B 70  
AA6 1 2 N ILE B 139 ? N ILE B 139 O VAL B 446 ? O VAL B 446 
AA6 2 3 O LYS B 449 ? O LYS B 449 N ASP B 422 ? N ASP B 422 
AA7 1 2 N THR B 339 ? N THR B 339 O LEU B 347 ? O LEU B 347 
AA8 1 2 N LYS B 434 ? N LYS B 434 O LYS B 440 ? O LYS B 440 
# 
_pdbx_entry_details.entry_id                   9KGP 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 15  ? ? 62.08   -126.41 
2  1 PRO A 45  ? ? -52.09  108.58  
3  1 LEU A 188 ? ? -69.67  0.20    
4  1 SER A 230 ? ? -52.54  95.89   
5  1 ASP A 231 ? ? -43.81  69.16   
6  1 LYS A 349 ? ? -36.43  130.80  
7  1 ASP A 370 ? ? -91.05  47.25   
8  1 THR A 436 ? ? -115.44 -113.03 
9  1 LYS B 15  ? ? 47.61   -128.49 
10 1 ASP B 84  ? ? -99.86  33.25   
11 1 ASP B 136 ? ? 81.18   3.17    
12 1 SER B 230 ? ? -50.47  95.78   
13 1 ASP B 231 ? ? -55.99  95.19   
14 1 HIS B 266 ? ? -136.97 -39.48  
15 1 ASP B 370 ? ? -97.25  44.89   
16 1 THR B 436 ? ? -114.31 -127.23 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     296 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.074 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       866 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.07 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A THR 1 ? A THR 1 
2 1 Y 1 A ILE 2 ? A ILE 2 
3 1 Y 1 B THR 1 ? B THR 1 
4 1 Y 1 B ILE 2 ? B ILE 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HEM CHA  C  N N 137 
HEM CHB  C  N N 138 
HEM CHC  C  N N 139 
HEM CHD  C  N N 140 
HEM C1A  C  Y N 141 
HEM C2A  C  Y N 142 
HEM C3A  C  Y N 143 
HEM C4A  C  Y N 144 
HEM CMA  C  N N 145 
HEM CAA  C  N N 146 
HEM CBA  C  N N 147 
HEM CGA  C  N N 148 
HEM O1A  O  N N 149 
HEM O2A  O  N N 150 
HEM C1B  C  N N 151 
HEM C2B  C  N N 152 
HEM C3B  C  N N 153 
HEM C4B  C  N N 154 
HEM CMB  C  N N 155 
HEM CAB  C  N N 156 
HEM CBB  C  N N 157 
HEM C1C  C  Y N 158 
HEM C2C  C  Y N 159 
HEM C3C  C  Y N 160 
HEM C4C  C  Y N 161 
HEM CMC  C  N N 162 
HEM CAC  C  N N 163 
HEM CBC  C  N N 164 
HEM C1D  C  N N 165 
HEM C2D  C  N N 166 
HEM C3D  C  N N 167 
HEM C4D  C  N N 168 
HEM CMD  C  N N 169 
HEM CAD  C  N N 170 
HEM CBD  C  N N 171 
HEM CGD  C  N N 172 
HEM O1D  O  N N 173 
HEM O2D  O  N N 174 
HEM NA   N  Y N 175 
HEM NB   N  N N 176 
HEM NC   N  Y N 177 
HEM ND   N  N N 178 
HEM FE   FE N N 179 
HEM HHB  H  N N 180 
HEM HHC  H  N N 181 
HEM HHD  H  N N 182 
HEM HMA  H  N N 183 
HEM HMAA H  N N 184 
HEM HMAB H  N N 185 
HEM HAA  H  N N 186 
HEM HAAA H  N N 187 
HEM HBA  H  N N 188 
HEM HBAA H  N N 189 
HEM HMB  H  N N 190 
HEM HMBA H  N N 191 
HEM HMBB H  N N 192 
HEM HAB  H  N N 193 
HEM HBB  H  N N 194 
HEM HBBA H  N N 195 
HEM HMC  H  N N 196 
HEM HMCA H  N N 197 
HEM HMCB H  N N 198 
HEM HAC  H  N N 199 
HEM HBC  H  N N 200 
HEM HBCA H  N N 201 
HEM HMD  H  N N 202 
HEM HMDA H  N N 203 
HEM HMDB H  N N 204 
HEM HAD  H  N N 205 
HEM HADA H  N N 206 
HEM HBD  H  N N 207 
HEM HBDA H  N N 208 
HEM H2A  H  N N 209 
HEM H2D  H  N N 210 
HEM HHA  H  N N 211 
HIS N    N  N N 212 
HIS CA   C  N S 213 
HIS C    C  N N 214 
HIS O    O  N N 215 
HIS CB   C  N N 216 
HIS CG   C  Y N 217 
HIS ND1  N  Y N 218 
HIS CD2  C  Y N 219 
HIS CE1  C  Y N 220 
HIS NE2  N  Y N 221 
HIS OXT  O  N N 222 
HIS H    H  N N 223 
HIS H2   H  N N 224 
HIS HA   H  N N 225 
HIS HB2  H  N N 226 
HIS HB3  H  N N 227 
HIS HD1  H  N N 228 
HIS HD2  H  N N 229 
HIS HE1  H  N N 230 
HIS HE2  H  N N 231 
HIS HXT  H  N N 232 
HOH O    O  N N 233 
HOH H1   H  N N 234 
HOH H2   H  N N 235 
ILE N    N  N N 236 
ILE CA   C  N S 237 
ILE C    C  N N 238 
ILE O    O  N N 239 
ILE CB   C  N S 240 
ILE CG1  C  N N 241 
ILE CG2  C  N N 242 
ILE CD1  C  N N 243 
ILE OXT  O  N N 244 
ILE H    H  N N 245 
ILE H2   H  N N 246 
ILE HA   H  N N 247 
ILE HB   H  N N 248 
ILE HG12 H  N N 249 
ILE HG13 H  N N 250 
ILE HG21 H  N N 251 
ILE HG22 H  N N 252 
ILE HG23 H  N N 253 
ILE HD11 H  N N 254 
ILE HD12 H  N N 255 
ILE HD13 H  N N 256 
ILE HXT  H  N N 257 
LEU N    N  N N 258 
LEU CA   C  N S 259 
LEU C    C  N N 260 
LEU O    O  N N 261 
LEU CB   C  N N 262 
LEU CG   C  N N 263 
LEU CD1  C  N N 264 
LEU CD2  C  N N 265 
LEU OXT  O  N N 266 
LEU H    H  N N 267 
LEU H2   H  N N 268 
LEU HA   H  N N 269 
LEU HB2  H  N N 270 
LEU HB3  H  N N 271 
LEU HG   H  N N 272 
LEU HD11 H  N N 273 
LEU HD12 H  N N 274 
LEU HD13 H  N N 275 
LEU HD21 H  N N 276 
LEU HD22 H  N N 277 
LEU HD23 H  N N 278 
LEU HXT  H  N N 279 
LYS N    N  N N 280 
LYS CA   C  N S 281 
LYS C    C  N N 282 
LYS O    O  N N 283 
LYS CB   C  N N 284 
LYS CG   C  N N 285 
LYS CD   C  N N 286 
LYS CE   C  N N 287 
LYS NZ   N  N N 288 
LYS OXT  O  N N 289 
LYS H    H  N N 290 
LYS H2   H  N N 291 
LYS HA   H  N N 292 
LYS HB2  H  N N 293 
LYS HB3  H  N N 294 
LYS HG2  H  N N 295 
LYS HG3  H  N N 296 
LYS HD2  H  N N 297 
LYS HD3  H  N N 298 
LYS HE2  H  N N 299 
LYS HE3  H  N N 300 
LYS HZ1  H  N N 301 
LYS HZ2  H  N N 302 
LYS HZ3  H  N N 303 
LYS HXT  H  N N 304 
MET N    N  N N 305 
MET CA   C  N S 306 
MET C    C  N N 307 
MET O    O  N N 308 
MET CB   C  N N 309 
MET CG   C  N N 310 
MET SD   S  N N 311 
MET CE   C  N N 312 
MET OXT  O  N N 313 
MET H    H  N N 314 
MET H2   H  N N 315 
MET HA   H  N N 316 
MET HB2  H  N N 317 
MET HB3  H  N N 318 
MET HG2  H  N N 319 
MET HG3  H  N N 320 
MET HE1  H  N N 321 
MET HE2  H  N N 322 
MET HE3  H  N N 323 
MET HXT  H  N N 324 
PHE N    N  N N 325 
PHE CA   C  N S 326 
PHE C    C  N N 327 
PHE O    O  N N 328 
PHE CB   C  N N 329 
PHE CG   C  Y N 330 
PHE CD1  C  Y N 331 
PHE CD2  C  Y N 332 
PHE CE1  C  Y N 333 
PHE CE2  C  Y N 334 
PHE CZ   C  Y N 335 
PHE OXT  O  N N 336 
PHE H    H  N N 337 
PHE H2   H  N N 338 
PHE HA   H  N N 339 
PHE HB2  H  N N 340 
PHE HB3  H  N N 341 
PHE HD1  H  N N 342 
PHE HD2  H  N N 343 
PHE HE1  H  N N 344 
PHE HE2  H  N N 345 
PHE HZ   H  N N 346 
PHE HXT  H  N N 347 
PRO N    N  N N 348 
PRO CA   C  N S 349 
PRO C    C  N N 350 
PRO O    O  N N 351 
PRO CB   C  N N 352 
PRO CG   C  N N 353 
PRO CD   C  N N 354 
PRO OXT  O  N N 355 
PRO H    H  N N 356 
PRO HA   H  N N 357 
PRO HB2  H  N N 358 
PRO HB3  H  N N 359 
PRO HG2  H  N N 360 
PRO HG3  H  N N 361 
PRO HD2  H  N N 362 
PRO HD3  H  N N 363 
PRO HXT  H  N N 364 
SER N    N  N N 365 
SER CA   C  N S 366 
SER C    C  N N 367 
SER O    O  N N 368 
SER CB   C  N N 369 
SER OG   O  N N 370 
SER OXT  O  N N 371 
SER H    H  N N 372 
SER H2   H  N N 373 
SER HA   H  N N 374 
SER HB2  H  N N 375 
SER HB3  H  N N 376 
SER HG   H  N N 377 
SER HXT  H  N N 378 
THR N    N  N N 379 
THR CA   C  N S 380 
THR C    C  N N 381 
THR O    O  N N 382 
THR CB   C  N R 383 
THR OG1  O  N N 384 
THR CG2  C  N N 385 
THR OXT  O  N N 386 
THR H    H  N N 387 
THR H2   H  N N 388 
THR HA   H  N N 389 
THR HB   H  N N 390 
THR HG1  H  N N 391 
THR HG21 H  N N 392 
THR HG22 H  N N 393 
THR HG23 H  N N 394 
THR HXT  H  N N 395 
TRP N    N  N N 396 
TRP CA   C  N S 397 
TRP C    C  N N 398 
TRP O    O  N N 399 
TRP CB   C  N N 400 
TRP CG   C  Y N 401 
TRP CD1  C  Y N 402 
TRP CD2  C  Y N 403 
TRP NE1  N  Y N 404 
TRP CE2  C  Y N 405 
TRP CE3  C  Y N 406 
TRP CZ2  C  Y N 407 
TRP CZ3  C  Y N 408 
TRP CH2  C  Y N 409 
TRP OXT  O  N N 410 
TRP H    H  N N 411 
TRP H2   H  N N 412 
TRP HA   H  N N 413 
TRP HB2  H  N N 414 
TRP HB3  H  N N 415 
TRP HD1  H  N N 416 
TRP HE1  H  N N 417 
TRP HE3  H  N N 418 
TRP HZ2  H  N N 419 
TRP HZ3  H  N N 420 
TRP HH2  H  N N 421 
TRP HXT  H  N N 422 
TYR N    N  N N 423 
TYR CA   C  N S 424 
TYR C    C  N N 425 
TYR O    O  N N 426 
TYR CB   C  N N 427 
TYR CG   C  Y N 428 
TYR CD1  C  Y N 429 
TYR CD2  C  Y N 430 
TYR CE1  C  Y N 431 
TYR CE2  C  Y N 432 
TYR CZ   C  Y N 433 
TYR OH   O  N N 434 
TYR OXT  O  N N 435 
TYR H    H  N N 436 
TYR H2   H  N N 437 
TYR HA   H  N N 438 
TYR HB2  H  N N 439 
TYR HB3  H  N N 440 
TYR HD1  H  N N 441 
TYR HD2  H  N N 442 
TYR HE1  H  N N 443 
TYR HE2  H  N N 444 
TYR HH   H  N N 445 
TYR HXT  H  N N 446 
VAL N    N  N N 447 
VAL CA   C  N S 448 
VAL C    C  N N 449 
VAL O    O  N N 450 
VAL CB   C  N N 451 
VAL CG1  C  N N 452 
VAL CG2  C  N N 453 
VAL OXT  O  N N 454 
VAL H    H  N N 455 
VAL H2   H  N N 456 
VAL HA   H  N N 457 
VAL HB   H  N N 458 
VAL HG11 H  N N 459 
VAL HG12 H  N N 460 
VAL HG13 H  N N 461 
VAL HG21 H  N N 462 
VAL HG22 H  N N 463 
VAL HG23 H  N N 464 
VAL HXT  H  N N 465 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HEM CHA C1A  sing N N 129 
HEM CHA C4D  doub N N 130 
HEM CHA HHA  sing N N 131 
HEM CHB C4A  sing N N 132 
HEM CHB C1B  doub N N 133 
HEM CHB HHB  sing N N 134 
HEM CHC C4B  sing N N 135 
HEM CHC C1C  doub N N 136 
HEM CHC HHC  sing N N 137 
HEM CHD C4C  doub N N 138 
HEM CHD C1D  sing N N 139 
HEM CHD HHD  sing N N 140 
HEM C1A C2A  doub Y N 141 
HEM C1A NA   sing Y N 142 
HEM C2A C3A  sing Y N 143 
HEM C2A CAA  sing N N 144 
HEM C3A C4A  doub Y N 145 
HEM C3A CMA  sing N N 146 
HEM C4A NA   sing Y N 147 
HEM CMA HMA  sing N N 148 
HEM CMA HMAA sing N N 149 
HEM CMA HMAB sing N N 150 
HEM CAA CBA  sing N N 151 
HEM CAA HAA  sing N N 152 
HEM CAA HAAA sing N N 153 
HEM CBA CGA  sing N N 154 
HEM CBA HBA  sing N N 155 
HEM CBA HBAA sing N N 156 
HEM CGA O1A  doub N N 157 
HEM CGA O2A  sing N N 158 
HEM C1B C2B  sing N N 159 
HEM C1B NB   sing N N 160 
HEM C2B C3B  doub N N 161 
HEM C2B CMB  sing N N 162 
HEM C3B C4B  sing N N 163 
HEM C3B CAB  sing N N 164 
HEM C4B NB   doub N N 165 
HEM CMB HMB  sing N N 166 
HEM CMB HMBA sing N N 167 
HEM CMB HMBB sing N N 168 
HEM CAB CBB  doub N N 169 
HEM CAB HAB  sing N N 170 
HEM CBB HBB  sing N N 171 
HEM CBB HBBA sing N N 172 
HEM C1C C2C  sing Y N 173 
HEM C1C NC   sing Y N 174 
HEM C2C C3C  doub Y N 175 
HEM C2C CMC  sing N N 176 
HEM C3C C4C  sing Y N 177 
HEM C3C CAC  sing N N 178 
HEM C4C NC   sing Y N 179 
HEM CMC HMC  sing N N 180 
HEM CMC HMCA sing N N 181 
HEM CMC HMCB sing N N 182 
HEM CAC CBC  doub N N 183 
HEM CAC HAC  sing N N 184 
HEM CBC HBC  sing N N 185 
HEM CBC HBCA sing N N 186 
HEM C1D C2D  sing N N 187 
HEM C1D ND   doub N N 188 
HEM C2D C3D  doub N N 189 
HEM C2D CMD  sing N N 190 
HEM C3D C4D  sing N N 191 
HEM C3D CAD  sing N N 192 
HEM C4D ND   sing N N 193 
HEM CMD HMD  sing N N 194 
HEM CMD HMDA sing N N 195 
HEM CMD HMDB sing N N 196 
HEM CAD CBD  sing N N 197 
HEM CAD HAD  sing N N 198 
HEM CAD HADA sing N N 199 
HEM CBD CGD  sing N N 200 
HEM CBD HBD  sing N N 201 
HEM CBD HBDA sing N N 202 
HEM CGD O1D  doub N N 203 
HEM CGD O2D  sing N N 204 
HEM O2A H2A  sing N N 205 
HEM O2D H2D  sing N N 206 
HEM FE  NA   sing N N 207 
HEM FE  NB   sing N N 208 
HEM FE  NC   sing N N 209 
HEM FE  ND   sing N N 210 
HIS N   CA   sing N N 211 
HIS N   H    sing N N 212 
HIS N   H2   sing N N 213 
HIS CA  C    sing N N 214 
HIS CA  CB   sing N N 215 
HIS CA  HA   sing N N 216 
HIS C   O    doub N N 217 
HIS C   OXT  sing N N 218 
HIS CB  CG   sing N N 219 
HIS CB  HB2  sing N N 220 
HIS CB  HB3  sing N N 221 
HIS CG  ND1  sing Y N 222 
HIS CG  CD2  doub Y N 223 
HIS ND1 CE1  doub Y N 224 
HIS ND1 HD1  sing N N 225 
HIS CD2 NE2  sing Y N 226 
HIS CD2 HD2  sing N N 227 
HIS CE1 NE2  sing Y N 228 
HIS CE1 HE1  sing N N 229 
HIS NE2 HE2  sing N N 230 
HIS OXT HXT  sing N N 231 
HOH O   H1   sing N N 232 
HOH O   H2   sing N N 233 
ILE N   CA   sing N N 234 
ILE N   H    sing N N 235 
ILE N   H2   sing N N 236 
ILE CA  C    sing N N 237 
ILE CA  CB   sing N N 238 
ILE CA  HA   sing N N 239 
ILE C   O    doub N N 240 
ILE C   OXT  sing N N 241 
ILE CB  CG1  sing N N 242 
ILE CB  CG2  sing N N 243 
ILE CB  HB   sing N N 244 
ILE CG1 CD1  sing N N 245 
ILE CG1 HG12 sing N N 246 
ILE CG1 HG13 sing N N 247 
ILE CG2 HG21 sing N N 248 
ILE CG2 HG22 sing N N 249 
ILE CG2 HG23 sing N N 250 
ILE CD1 HD11 sing N N 251 
ILE CD1 HD12 sing N N 252 
ILE CD1 HD13 sing N N 253 
ILE OXT HXT  sing N N 254 
LEU N   CA   sing N N 255 
LEU N   H    sing N N 256 
LEU N   H2   sing N N 257 
LEU CA  C    sing N N 258 
LEU CA  CB   sing N N 259 
LEU CA  HA   sing N N 260 
LEU C   O    doub N N 261 
LEU C   OXT  sing N N 262 
LEU CB  CG   sing N N 263 
LEU CB  HB2  sing N N 264 
LEU CB  HB3  sing N N 265 
LEU CG  CD1  sing N N 266 
LEU CG  CD2  sing N N 267 
LEU CG  HG   sing N N 268 
LEU CD1 HD11 sing N N 269 
LEU CD1 HD12 sing N N 270 
LEU CD1 HD13 sing N N 271 
LEU CD2 HD21 sing N N 272 
LEU CD2 HD22 sing N N 273 
LEU CD2 HD23 sing N N 274 
LEU OXT HXT  sing N N 275 
LYS N   CA   sing N N 276 
LYS N   H    sing N N 277 
LYS N   H2   sing N N 278 
LYS CA  C    sing N N 279 
LYS CA  CB   sing N N 280 
LYS CA  HA   sing N N 281 
LYS C   O    doub N N 282 
LYS C   OXT  sing N N 283 
LYS CB  CG   sing N N 284 
LYS CB  HB2  sing N N 285 
LYS CB  HB3  sing N N 286 
LYS CG  CD   sing N N 287 
LYS CG  HG2  sing N N 288 
LYS CG  HG3  sing N N 289 
LYS CD  CE   sing N N 290 
LYS CD  HD2  sing N N 291 
LYS CD  HD3  sing N N 292 
LYS CE  NZ   sing N N 293 
LYS CE  HE2  sing N N 294 
LYS CE  HE3  sing N N 295 
LYS NZ  HZ1  sing N N 296 
LYS NZ  HZ2  sing N N 297 
LYS NZ  HZ3  sing N N 298 
LYS OXT HXT  sing N N 299 
MET N   CA   sing N N 300 
MET N   H    sing N N 301 
MET N   H2   sing N N 302 
MET CA  C    sing N N 303 
MET CA  CB   sing N N 304 
MET CA  HA   sing N N 305 
MET C   O    doub N N 306 
MET C   OXT  sing N N 307 
MET CB  CG   sing N N 308 
MET CB  HB2  sing N N 309 
MET CB  HB3  sing N N 310 
MET CG  SD   sing N N 311 
MET CG  HG2  sing N N 312 
MET CG  HG3  sing N N 313 
MET SD  CE   sing N N 314 
MET CE  HE1  sing N N 315 
MET CE  HE2  sing N N 316 
MET CE  HE3  sing N N 317 
MET OXT HXT  sing N N 318 
PHE N   CA   sing N N 319 
PHE N   H    sing N N 320 
PHE N   H2   sing N N 321 
PHE CA  C    sing N N 322 
PHE CA  CB   sing N N 323 
PHE CA  HA   sing N N 324 
PHE C   O    doub N N 325 
PHE C   OXT  sing N N 326 
PHE CB  CG   sing N N 327 
PHE CB  HB2  sing N N 328 
PHE CB  HB3  sing N N 329 
PHE CG  CD1  doub Y N 330 
PHE CG  CD2  sing Y N 331 
PHE CD1 CE1  sing Y N 332 
PHE CD1 HD1  sing N N 333 
PHE CD2 CE2  doub Y N 334 
PHE CD2 HD2  sing N N 335 
PHE CE1 CZ   doub Y N 336 
PHE CE1 HE1  sing N N 337 
PHE CE2 CZ   sing Y N 338 
PHE CE2 HE2  sing N N 339 
PHE CZ  HZ   sing N N 340 
PHE OXT HXT  sing N N 341 
PRO N   CA   sing N N 342 
PRO N   CD   sing N N 343 
PRO N   H    sing N N 344 
PRO CA  C    sing N N 345 
PRO CA  CB   sing N N 346 
PRO CA  HA   sing N N 347 
PRO C   O    doub N N 348 
PRO C   OXT  sing N N 349 
PRO CB  CG   sing N N 350 
PRO CB  HB2  sing N N 351 
PRO CB  HB3  sing N N 352 
PRO CG  CD   sing N N 353 
PRO CG  HG2  sing N N 354 
PRO CG  HG3  sing N N 355 
PRO CD  HD2  sing N N 356 
PRO CD  HD3  sing N N 357 
PRO OXT HXT  sing N N 358 
SER N   CA   sing N N 359 
SER N   H    sing N N 360 
SER N   H2   sing N N 361 
SER CA  C    sing N N 362 
SER CA  CB   sing N N 363 
SER CA  HA   sing N N 364 
SER C   O    doub N N 365 
SER C   OXT  sing N N 366 
SER CB  OG   sing N N 367 
SER CB  HB2  sing N N 368 
SER CB  HB3  sing N N 369 
SER OG  HG   sing N N 370 
SER OXT HXT  sing N N 371 
THR N   CA   sing N N 372 
THR N   H    sing N N 373 
THR N   H2   sing N N 374 
THR CA  C    sing N N 375 
THR CA  CB   sing N N 376 
THR CA  HA   sing N N 377 
THR C   O    doub N N 378 
THR C   OXT  sing N N 379 
THR CB  OG1  sing N N 380 
THR CB  CG2  sing N N 381 
THR CB  HB   sing N N 382 
THR OG1 HG1  sing N N 383 
THR CG2 HG21 sing N N 384 
THR CG2 HG22 sing N N 385 
THR CG2 HG23 sing N N 386 
THR OXT HXT  sing N N 387 
TRP N   CA   sing N N 388 
TRP N   H    sing N N 389 
TRP N   H2   sing N N 390 
TRP CA  C    sing N N 391 
TRP CA  CB   sing N N 392 
TRP CA  HA   sing N N 393 
TRP C   O    doub N N 394 
TRP C   OXT  sing N N 395 
TRP CB  CG   sing N N 396 
TRP CB  HB2  sing N N 397 
TRP CB  HB3  sing N N 398 
TRP CG  CD1  doub Y N 399 
TRP CG  CD2  sing Y N 400 
TRP CD1 NE1  sing Y N 401 
TRP CD1 HD1  sing N N 402 
TRP CD2 CE2  doub Y N 403 
TRP CD2 CE3  sing Y N 404 
TRP NE1 CE2  sing Y N 405 
TRP NE1 HE1  sing N N 406 
TRP CE2 CZ2  sing Y N 407 
TRP CE3 CZ3  doub Y N 408 
TRP CE3 HE3  sing N N 409 
TRP CZ2 CH2  doub Y N 410 
TRP CZ2 HZ2  sing N N 411 
TRP CZ3 CH2  sing Y N 412 
TRP CZ3 HZ3  sing N N 413 
TRP CH2 HH2  sing N N 414 
TRP OXT HXT  sing N N 415 
TYR N   CA   sing N N 416 
TYR N   H    sing N N 417 
TYR N   H2   sing N N 418 
TYR CA  C    sing N N 419 
TYR CA  CB   sing N N 420 
TYR CA  HA   sing N N 421 
TYR C   O    doub N N 422 
TYR C   OXT  sing N N 423 
TYR CB  CG   sing N N 424 
TYR CB  HB2  sing N N 425 
TYR CB  HB3  sing N N 426 
TYR CG  CD1  doub Y N 427 
TYR CG  CD2  sing Y N 428 
TYR CD1 CE1  sing Y N 429 
TYR CD1 HD1  sing N N 430 
TYR CD2 CE2  doub Y N 431 
TYR CD2 HD2  sing N N 432 
TYR CE1 CZ   doub Y N 433 
TYR CE1 HE1  sing N N 434 
TYR CE2 CZ   sing Y N 435 
TYR CE2 HE2  sing N N 436 
TYR CZ  OH   sing N N 437 
TYR OH  HH   sing N N 438 
TYR OXT HXT  sing N N 439 
VAL N   CA   sing N N 440 
VAL N   H    sing N N 441 
VAL N   H2   sing N N 442 
VAL CA  C    sing N N 443 
VAL CA  CB   sing N N 444 
VAL CA  HA   sing N N 445 
VAL C   O    doub N N 446 
VAL C   OXT  sing N N 447 
VAL CB  CG1  sing N N 448 
VAL CB  CG2  sing N N 449 
VAL CB  HB   sing N N 450 
VAL CG1 HG11 sing N N 451 
VAL CG1 HG12 sing N N 452 
VAL CG1 HG13 sing N N 453 
VAL CG2 HG21 sing N N 454 
VAL CG2 HG22 sing N N 455 
VAL CG2 HG23 sing N N 456 
VAL OXT HXT  sing N N 457 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           22078126 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9KGP 
_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]   0.016981 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002242 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006866 
_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]   0.015955 
_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  
FE 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LYS A 1 3   ? 13.813  31.173  57.004  1.00 51.34  ? 3   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 3   ? 12.490  30.627  57.411  1.00 52.09  ? 3   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 3   ? 12.706  29.542  58.467  1.00 53.50  ? 3   LYS A C   1 
ATOM   4    O  O   . LYS A 1 3   ? 13.604  28.711  58.348  1.00 50.82  ? 3   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 3   ? 11.715  30.127  56.183  1.00 56.78  ? 3   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 3   ? 10.489  29.272  56.486  1.00 60.20  ? 3   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 3   ? 9.400   29.355  55.436  1.00 62.75  ? 3   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 3   ? 8.067   28.853  55.951  1.00 62.75  ? 3   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 3   ? 6.961   29.216  55.035  1.00 64.31  ? 3   LYS A NZ  1 
ATOM   10   N  N   . GLU A 1 4   ? 11.878  29.579  59.517  1.00 54.96  ? 4   GLU A N   1 
ATOM   11   C  CA  . GLU A 1 4   ? 11.908  28.580  60.572  1.00 57.40  ? 4   GLU A CA  1 
ATOM   12   C  C   . GLU A 1 4   ? 11.245  27.297  60.061  1.00 50.75  ? 4   GLU A C   1 
ATOM   13   O  O   . GLU A 1 4   ? 10.208  27.350  59.395  1.00 53.96  ? 4   GLU A O   1 
ATOM   14   C  CB  . GLU A 1 4   ? 11.226  29.149  61.823  1.00 59.65  ? 4   GLU A CB  1 
ATOM   15   C  CG  . GLU A 1 4   ? 11.254  28.228  63.032  1.00 62.66  ? 4   GLU A CG  1 
ATOM   16   C  CD  . GLU A 1 4   ? 12.632  27.732  63.435  1.00 68.29  ? 4   GLU A CD  1 
ATOM   17   O  OE1 . GLU A 1 4   ? 12.761  27.177  64.553  1.00 67.59  ? 4   GLU A OE1 1 
ATOM   18   O  OE2 . GLU A 1 4   ? 13.574  27.884  62.624  1.00 69.38  ? 4   GLU A OE2 1 
ATOM   19   N  N   . MET A 1 5   ? 11.855  26.145  60.370  1.00 44.67  ? 5   MET A N   1 
ATOM   20   C  CA  . MET A 1 5   ? 11.462  24.884  59.756  1.00 37.76  ? 5   MET A CA  1 
ATOM   21   C  C   . MET A 1 5   ? 10.513  24.111  60.673  1.00 29.14  ? 5   MET A C   1 
ATOM   22   O  O   . MET A 1 5   ? 10.786  23.928  61.846  1.00 28.34  ? 5   MET A O   1 
ATOM   23   C  CB  . MET A 1 5   ? 12.691  24.027  59.449  1.00 39.87  ? 5   MET A CB  1 
ATOM   24   C  CG  . MET A 1 5   ? 12.341  22.759  58.683  1.00 37.33  ? 5   MET A CG  1 
ATOM   25   S  SD  . MET A 1 5   ? 13.778  21.767  58.265  1.00 38.10  ? 5   MET A SD  1 
ATOM   26   C  CE  . MET A 1 5   ? 14.761  22.957  57.355  1.00 35.42  ? 5   MET A CE  1 
ATOM   27   N  N   . PRO A 1 6   ? 9.362   23.617  60.172  1.00 25.56  ? 6   PRO A N   1 
ATOM   28   C  CA  . PRO A 1 6   ? 8.440   22.830  60.984  1.00 24.46  ? 6   PRO A CA  1 
ATOM   29   C  C   . PRO A 1 6   ? 9.067   21.542  61.492  1.00 23.44  ? 6   PRO A C   1 
ATOM   30   O  O   . PRO A 1 6   ? 10.008  21.044  60.876  1.00 25.40  ? 6   PRO A O   1 
ATOM   31   C  CB  . PRO A 1 6   ? 7.309   22.414  60.036  1.00 26.48  ? 6   PRO A CB  1 
ATOM   32   C  CG  . PRO A 1 6   ? 7.503   23.236  58.789  1.00 25.49  ? 6   PRO A CG  1 
ATOM   33   C  CD  . PRO A 1 6   ? 8.905   23.791  58.800  1.00 25.76  ? 6   PRO A CD  1 
ATOM   34   N  N   . GLN A 1 7   ? 8.535   21.033  62.609  1.00 22.94  ? 7   GLN A N   1 
ATOM   35   C  CA  . GLN A 1 7   ? 9.027   19.821  63.236  1.00 24.31  ? 7   GLN A CA  1 
ATOM   36   C  C   . GLN A 1 7   ? 7.859   19.095  63.876  1.00 21.86  ? 7   GLN A C   1 
ATOM   37   O  O   . GLN A 1 7   ? 6.995   19.724  64.460  1.00 22.21  ? 7   GLN A O   1 
ATOM   38   C  CB  . GLN A 1 7   ? 10.057  20.149  64.306  1.00 26.29  ? 7   GLN A CB  1 
ATOM   39   C  CG  . GLN A 1 7   ? 10.812  18.925  64.774  1.00 27.19  ? 7   GLN A CG  1 
ATOM   40   C  CD  . GLN A 1 7   ? 11.703  19.246  65.939  1.00 30.09  ? 7   GLN A CD  1 
ATOM   41   O  OE1 . GLN A 1 7   ? 11.994  20.403  66.215  1.00 36.33  ? 7   GLN A OE1 1 
ATOM   42   N  NE2 . GLN A 1 7   ? 12.170  18.218  66.611  1.00 29.33  ? 7   GLN A NE2 1 
ATOM   43   N  N   . PRO A 1 8   ? 7.723   17.765  63.717  1.00 23.58  ? 8   PRO A N   1 
ATOM   44   C  CA  . PRO A 1 8   ? 6.588   17.067  64.314  1.00 20.82  ? 8   PRO A CA  1 
ATOM   45   C  C   . PRO A 1 8   ? 6.757   16.980  65.824  1.00 21.56  ? 8   PRO A C   1 
ATOM   46   O  O   . PRO A 1 8   ? 7.811   17.328  66.346  1.00 20.46  ? 8   PRO A O   1 
ATOM   47   C  CB  . PRO A 1 8   ? 6.579   15.707  63.606  1.00 20.61  ? 8   PRO A CB  1 
ATOM   48   C  CG  . PRO A 1 8   ? 8.021   15.503  63.148  1.00 21.55  ? 8   PRO A CG  1 
ATOM   49   C  CD  . PRO A 1 8   ? 8.573   16.883  62.893  1.00 21.44  ? 8   PRO A CD  1 
ATOM   50   N  N   . LYS A 1 9   ? 5.722   16.448  66.486  1.00 23.36  ? 9   LYS A N   1 
ATOM   51   C  CA  . LYS A 1 9   ? 5.662   16.303  67.938  1.00 25.23  ? 9   LYS A CA  1 
ATOM   52   C  C   . LYS A 1 9   ? 6.838   15.498  68.497  1.00 22.10  ? 9   LYS A C   1 
ATOM   53   O  O   . LYS A 1 9   ? 7.395   14.630  67.826  1.00 21.49  ? 9   LYS A O   1 
ATOM   54   C  CB  . LYS A 1 9   ? 4.311   15.679  68.300  1.00 26.78  ? 9   LYS A CB  1 
ATOM   55   C  CG  . LYS A 1 9   ? 4.149   14.215  67.920  1.00 26.88  ? 9   LYS A CG  1 
ATOM   56   C  CD  . LYS A 1 9   ? 2.733   13.709  68.092  1.00 25.10  ? 9   LYS A CD  1 
ATOM   57   C  CE  . LYS A 1 9   ? 2.676   12.212  67.947  1.00 27.01  ? 9   LYS A CE  1 
ATOM   58   N  NZ  . LYS A 1 9   ? 1.392   11.657  68.429  1.00 32.03  ? 9   LYS A NZ  1 
ATOM   59   N  N   . THR A 1 10  ? 7.212   15.780  69.758  1.00 21.48  ? 10  THR A N   1 
ATOM   60   C  CA  . THR A 1 10  ? 8.433   15.249  70.353  1.00 21.82  ? 10  THR A CA  1 
ATOM   61   C  C   . THR A 1 10  ? 8.139   14.387  71.590  1.00 22.99  ? 10  THR A C   1 
ATOM   62   O  O   . THR A 1 10  ? 7.034   14.408  72.116  1.00 22.25  ? 10  THR A O   1 
ATOM   63   C  CB  . THR A 1 10  ? 9.398   16.391  70.711  1.00 26.03  ? 10  THR A CB  1 
ATOM   64   O  OG1 . THR A 1 10  ? 8.712   17.358  71.517  1.00 24.97  ? 10  THR A OG1 1 
ATOM   65   C  CG2 . THR A 1 10  ? 9.983   17.083  69.494  1.00 24.36  ? 10  THR A CG2 1 
ATOM   66   N  N   . PHE A 1 11  ? 9.153   13.623  72.044  1.00 21.89  ? 11  PHE A N   1 
ATOM   67   C  CA  . PHE A 1 11  ? 9.023   12.671  73.148  1.00 21.82  ? 11  PHE A CA  1 
ATOM   68   C  C   . PHE A 1 11  ? 10.164  12.870  74.143  1.00 24.28  ? 11  PHE A C   1 
ATOM   69   O  O   . PHE A 1 11  ? 10.966  11.966  74.386  1.00 27.46  ? 11  PHE A O   1 
ATOM   70   C  CB  . PHE A 1 11  ? 9.029   11.218  72.656  1.00 19.25  ? 11  PHE A CB  1 
ATOM   71   C  CG  . PHE A 1 11  ? 7.893   10.843  71.746  1.00 18.91  ? 11  PHE A CG  1 
ATOM   72   C  CD1 . PHE A 1 11  ? 7.777   11.415  70.485  1.00 19.90  ? 11  PHE A CD1 1 
ATOM   73   C  CD2 . PHE A 1 11  ? 6.917   9.951   72.161  1.00 17.86  ? 11  PHE A CD2 1 
ATOM   74   C  CE1 . PHE A 1 11  ? 6.734   11.068  69.640  1.00 19.23  ? 11  PHE A CE1 1 
ATOM   75   C  CE2 . PHE A 1 11  ? 5.853   9.638   71.333  1.00 17.95  ? 11  PHE A CE2 1 
ATOM   76   C  CZ  . PHE A 1 11  ? 5.775   10.175  70.066  1.00 19.66  ? 11  PHE A CZ  1 
ATOM   77   N  N   . GLY A 1 12  ? 10.242  14.067  74.708  1.00 23.98  ? 12  GLY A N   1 
ATOM   78   C  CA  . GLY A 1 12  ? 11.238  14.332  75.730  1.00 26.04  ? 12  GLY A CA  1 
ATOM   79   C  C   . GLY A 1 12  ? 12.648  14.195  75.154  1.00 28.87  ? 12  GLY A C   1 
ATOM   80   O  O   . GLY A 1 12  ? 12.927  14.773  74.093  1.00 28.76  ? 12  GLY A O   1 
ATOM   81   N  N   . GLU A 1 13  ? 13.503  13.399  75.821  1.00 30.50  ? 13  GLU A N   1 
ATOM   82   C  CA  . GLU A 1 13  ? 14.891  13.208  75.398  1.00 37.44  ? 13  GLU A CA  1 
ATOM   83   C  C   . GLU A 1 13  ? 14.960  12.464  74.059  1.00 33.36  ? 13  GLU A C   1 
ATOM   84   O  O   . GLU A 1 13  ? 15.981  12.490  73.375  1.00 32.51  ? 13  GLU A O   1 
ATOM   85   C  CB  . GLU A 1 13  ? 15.697  12.391  76.421  1.00 45.06  ? 13  GLU A CB  1 
ATOM   86   C  CG  . GLU A 1 13  ? 15.396  10.884  76.391  1.00 56.75  ? 13  GLU A CG  1 
ATOM   87   C  CD  . GLU A 1 13  ? 16.580  9.913   76.401  1.00 62.87  ? 13  GLU A CD  1 
ATOM   88   O  OE1 . GLU A 1 13  ? 16.613  9.041   77.309  1.00 69.38  ? 13  GLU A OE1 1 
ATOM   89   O  OE2 . GLU A 1 13  ? 17.449  9.984   75.479  1.00 59.31  ? 13  GLU A OE2 1 
ATOM   90   N  N   . LEU A 1 14  ? 13.885  11.747  73.714  1.00 27.99  ? 14  LEU A N   1 
ATOM   91   C  CA  . LEU A 1 14  ? 13.898  10.902  72.533  1.00 28.54  ? 14  LEU A CA  1 
ATOM   92   C  C   . LEU A 1 14  ? 13.618  11.724  71.269  1.00 23.80  ? 14  LEU A C   1 
ATOM   93   O  O   . LEU A 1 14  ? 13.866  11.256  70.156  1.00 23.00  ? 14  LEU A O   1 
ATOM   94   C  CB  . LEU A 1 14  ? 12.880  9.785   72.768  1.00 28.46  ? 14  LEU A CB  1 
ATOM   95   C  CG  . LEU A 1 14  ? 13.213  8.836   73.921  1.00 32.29  ? 14  LEU A CG  1 
ATOM   96   C  CD1 . LEU A 1 14  ? 12.177  7.735   74.048  1.00 31.51  ? 14  LEU A CD1 1 
ATOM   97   C  CD2 . LEU A 1 14  ? 14.597  8.218   73.743  1.00 33.47  ? 14  LEU A CD2 1 
ATOM   98   N  N   . LYS A 1 15  ? 13.133  12.960  71.461  1.00 22.91  ? 15  LYS A N   1 
ATOM   99   C  CA  . LYS A 1 15  ? 12.856  13.895  70.385  1.00 22.70  ? 15  LYS A CA  1 
ATOM   100  C  C   . LYS A 1 15  ? 11.776  13.279  69.492  1.00 19.90  ? 15  LYS A C   1 
ATOM   101  O  O   . LYS A 1 15  ? 10.732  12.895  70.003  1.00 19.52  ? 15  LYS A O   1 
ATOM   102  C  CB  . LYS A 1 15  ? 14.166  14.283  69.700  1.00 25.54  ? 15  LYS A CB  1 
ATOM   103  C  CG  . LYS A 1 15  ? 15.128  14.985  70.640  1.00 29.84  ? 15  LYS A CG  1 
ATOM   104  C  CD  . LYS A 1 15  ? 16.457  15.288  70.048  1.00 33.63  ? 15  LYS A CD  1 
ATOM   105  C  CE  . LYS A 1 15  ? 17.418  15.796  71.095  1.00 36.34  ? 15  LYS A CE  1 
ATOM   106  N  NZ  . LYS A 1 15  ? 18.809  15.750  70.588  1.00 39.77  ? 15  LYS A NZ  1 
ATOM   107  N  N   . ASN A 1 16  ? 12.039  13.187  68.183  1.00 22.37  ? 16  ASN A N   1 
ATOM   108  C  CA  . ASN A 1 16  ? 11.088  12.652  67.221  1.00 23.06  ? 16  ASN A CA  1 
ATOM   109  C  C   . ASN A 1 16  ? 11.242  11.136  67.052  1.00 21.83  ? 16  ASN A C   1 
ATOM   110  O  O   . ASN A 1 16  ? 10.411  10.501  66.399  1.00 21.38  ? 16  ASN A O   1 
ATOM   111  C  CB  . ASN A 1 16  ? 11.231  13.365  65.872  1.00 22.47  ? 16  ASN A CB  1 
ATOM   112  C  CG  . ASN A 1 16  ? 10.966  14.850  65.962  1.00 21.62  ? 16  ASN A CG  1 
ATOM   113  O  OD1 . ASN A 1 16  ? 11.778  15.670  65.537  1.00 22.26  ? 16  ASN A OD1 1 
ATOM   114  N  ND2 . ASN A 1 16  ? 9.821   15.206  66.505  1.00 22.40  ? 16  ASN A ND2 1 
ATOM   115  N  N   . LEU A 1 17  ? 12.271  10.518  67.628  1.00 22.10  ? 17  LEU A N   1 
ATOM   116  C  CA  . LEU A 1 17  ? 12.584  9.145   67.215  1.00 24.62  ? 17  LEU A CA  1 
ATOM   117  C  C   . LEU A 1 17  ? 11.398  8.184   67.403  1.00 25.20  ? 17  LEU A C   1 
ATOM   118  O  O   . LEU A 1 17  ? 11.170  7.319   66.544  1.00 25.97  ? 17  LEU A O   1 
ATOM   119  C  CB  . LEU A 1 17  ? 13.836  8.613   67.924  1.00 25.79  ? 17  LEU A CB  1 
ATOM   120  C  CG  . LEU A 1 17  ? 14.235  7.164   67.596  1.00 29.19  ? 17  LEU A CG  1 
ATOM   121  C  CD1 . LEU A 1 17  ? 14.695  7.026   66.150  1.00 28.22  ? 17  LEU A CD1 1 
ATOM   122  C  CD2 . LEU A 1 17  ? 15.316  6.665   68.550  1.00 31.15  ? 17  LEU A CD2 1 
ATOM   123  N  N   . PRO A 1 18  ? 10.603  8.226   68.500  1.00 22.40  ? 18  PRO A N   1 
ATOM   124  C  CA  . PRO A 1 18  ? 9.476   7.279   68.650  1.00 22.56  ? 18  PRO A CA  1 
ATOM   125  C  C   . PRO A 1 18  ? 8.390   7.342   67.570  1.00 21.69  ? 18  PRO A C   1 
ATOM   126  O  O   . PRO A 1 18  ? 7.594   6.407   67.446  1.00 22.69  ? 18  PRO A O   1 
ATOM   127  C  CB  . PRO A 1 18  ? 8.912   7.582   70.047  1.00 21.54  ? 18  PRO A CB  1 
ATOM   128  C  CG  . PRO A 1 18  ? 10.057  8.236   70.762  1.00 22.17  ? 18  PRO A CG  1 
ATOM   129  C  CD  . PRO A 1 18  ? 10.788  9.048   69.705  1.00 23.29  ? 18  PRO A CD  1 
ATOM   130  N  N   . LEU A 1 19  ? 8.397   8.396   66.744  1.00 21.68  ? 19  LEU A N   1 
ATOM   131  C  CA  . LEU A 1 19  ? 7.483   8.496   65.605  1.00 22.11  ? 19  LEU A CA  1 
ATOM   132  C  C   . LEU A 1 19  ? 7.729   7.336   64.634  1.00 22.12  ? 19  LEU A C   1 
ATOM   133  O  O   . LEU A 1 19  ? 6.821   6.914   63.919  1.00 23.52  ? 19  LEU A O   1 
ATOM   134  C  CB  . LEU A 1 19  ? 7.692   9.853   64.913  1.00 21.53  ? 19  LEU A CB  1 
ATOM   135  C  CG  . LEU A 1 19  ? 7.156   11.080  65.674  1.00 22.54  ? 19  LEU A CG  1 
ATOM   136  C  CD1 . LEU A 1 19  ? 7.401   12.372  64.903  1.00 19.79  ? 19  LEU A CD1 1 
ATOM   137  C  CD2 . LEU A 1 19  ? 5.661   10.957  65.970  1.00 24.11  ? 19  LEU A CD2 1 
ATOM   138  N  N   . LEU A 1 20  ? 8.970   6.840   64.587  1.00 22.37  ? 20  LEU A N   1 
ATOM   139  C  CA  . LEU A 1 20  ? 9.329   5.751   63.690  1.00 24.58  ? 20  LEU A CA  1 
ATOM   140  C  C   . LEU A 1 20  ? 9.220   4.413   64.418  1.00 23.26  ? 20  LEU A C   1 
ATOM   141  O  O   . LEU A 1 20  ? 9.540   3.387   63.844  1.00 24.69  ? 20  LEU A O   1 
ATOM   142  C  CB  . LEU A 1 20  ? 10.756  5.960   63.163  1.00 26.81  ? 20  LEU A CB  1 
ATOM   143  C  CG  . LEU A 1 20  ? 11.011  7.268   62.412  1.00 31.44  ? 20  LEU A CG  1 
ATOM   144  C  CD1 . LEU A 1 20  ? 12.384  7.257   61.743  1.00 34.96  ? 20  LEU A CD1 1 
ATOM   145  C  CD2 . LEU A 1 20  ? 9.923   7.547   61.396  1.00 33.25  ? 20  LEU A CD2 1 
ATOM   146  N  N   . ASN A 1 21  ? 8.826   4.414   65.694  1.00 22.67  ? 21  ASN A N   1 
ATOM   147  C  CA  . ASN A 1 21  ? 8.521   3.164   66.378  1.00 27.25  ? 21  ASN A CA  1 
ATOM   148  C  C   . ASN A 1 21  ? 7.133   2.652   65.976  1.00 26.09  ? 21  ASN A C   1 
ATOM   149  O  O   . ASN A 1 21  ? 6.256   2.543   66.824  1.00 27.35  ? 21  ASN A O   1 
ATOM   150  C  CB  . ASN A 1 21  ? 8.576   3.316   67.897  1.00 28.70  ? 21  ASN A CB  1 
ATOM   151  C  CG  . ASN A 1 21  ? 8.528   1.989   68.632  1.00 32.33  ? 21  ASN A CG  1 
ATOM   152  O  OD1 . ASN A 1 21  ? 8.536   1.966   69.865  1.00 38.71  ? 21  ASN A OD1 1 
ATOM   153  N  ND2 . ASN A 1 21  ? 8.478   0.882   67.904  1.00 31.49  ? 21  ASN A ND2 1 
ATOM   154  N  N   . THR A 1 22  ? 6.967   2.336   64.688  1.00 26.72  ? 22  THR A N   1 
ATOM   155  C  CA  . THR A 1 22  ? 5.786   1.693   64.124  1.00 27.34  ? 22  THR A CA  1 
ATOM   156  C  C   . THR A 1 22  ? 6.231   0.714   63.040  1.00 25.60  ? 22  THR A C   1 
ATOM   157  O  O   . THR A 1 22  ? 7.366   0.772   62.561  1.00 24.63  ? 22  THR A O   1 
ATOM   158  C  CB  . THR A 1 22  ? 4.812   2.667   63.439  1.00 34.09  ? 22  THR A CB  1 
ATOM   159  O  OG1 . THR A 1 22  ? 5.573   3.766   62.933  1.00 38.56  ? 22  THR A OG1 1 
ATOM   160  C  CG2 . THR A 1 22  ? 3.736   3.203   64.351  1.00 37.17  ? 22  THR A CG2 1 
ATOM   161  N  N   . ASP A 1 23  ? 5.322   -0.191  62.670  1.00 25.52  ? 23  ASP A N   1 
ATOM   162  C  CA  . ASP A 1 23  ? 5.543   -1.118  61.577  1.00 26.13  ? 23  ASP A CA  1 
ATOM   163  C  C   . ASP A 1 23  ? 5.546   -0.376  60.239  1.00 22.11  ? 23  ASP A C   1 
ATOM   164  O  O   . ASP A 1 23  ? 6.108   -0.882  59.256  1.00 22.86  ? 23  ASP A O   1 
ATOM   165  C  CB  . ASP A 1 23  ? 4.435   -2.169  61.514  1.00 30.06  ? 23  ASP A CB  1 
ATOM   166  C  CG  . ASP A 1 23  ? 4.300   -3.032  62.750  1.00 38.44  ? 23  ASP A CG  1 
ATOM   167  O  OD1 . ASP A 1 23  ? 5.276   -3.090  63.551  1.00 39.15  ? 23  ASP A OD1 1 
ATOM   168  O  OD2 . ASP A 1 23  ? 3.209   -3.634  62.900  1.00 41.07  ? 23  ASP A OD2 1 
ATOM   169  N  N   . LYS A 1 24  ? 4.936   0.820   60.209  1.00 21.23  ? 24  LYS A N   1 
ATOM   170  C  CA  . LYS A 1 24  ? 4.730   1.560   58.971  1.00 20.69  ? 24  LYS A CA  1 
ATOM   171  C  C   . LYS A 1 24  ? 5.286   2.988   59.053  1.00 20.03  ? 24  LYS A C   1 
ATOM   172  O  O   . LYS A 1 24  ? 4.547   3.968   58.957  1.00 18.15  ? 24  LYS A O   1 
ATOM   173  C  CB  . LYS A 1 24  ? 3.234   1.562   58.652  1.00 22.00  ? 24  LYS A CB  1 
ATOM   174  C  CG  . LYS A 1 24  ? 2.618   0.178   58.524  1.00 23.64  ? 24  LYS A CG  1 
ATOM   175  C  CD  . LYS A 1 24  ? 1.138   0.238   58.206  1.00 25.14  ? 24  LYS A CD  1 
ATOM   176  C  CE  . LYS A 1 24  ? 0.527   -1.131  57.948  1.00 24.51  ? 24  LYS A CE  1 
ATOM   177  N  NZ  . LYS A 1 24  ? -0.835  -0.995  57.391  1.00 27.76  ? 24  LYS A NZ  1 
ATOM   178  N  N   . PRO A 1 25  ? 6.618   3.139   59.189  1.00 19.27  ? 25  PRO A N   1 
ATOM   179  C  CA  . PRO A 1 25  ? 7.251   4.450   59.363  1.00 20.30  ? 25  PRO A CA  1 
ATOM   180  C  C   . PRO A 1 25  ? 7.140   5.399   58.170  1.00 21.66  ? 25  PRO A C   1 
ATOM   181  O  O   . PRO A 1 25  ? 6.814   6.584   58.347  1.00 21.93  ? 25  PRO A O   1 
ATOM   182  C  CB  . PRO A 1 25  ? 8.718   4.122   59.684  1.00 20.66  ? 25  PRO A CB  1 
ATOM   183  C  CG  . PRO A 1 25  ? 8.952   2.708   59.176  1.00 19.57  ? 25  PRO A CG  1 
ATOM   184  C  CD  . PRO A 1 25  ? 7.593   2.033   59.218  1.00 19.65  ? 25  PRO A CD  1 
ATOM   185  N  N   . VAL A 1 26  ? 7.282   4.872   56.948  1.00 18.80  ? 26  VAL A N   1 
ATOM   186  C  CA  . VAL A 1 26  ? 7.201   5.724   55.767  1.00 19.57  ? 26  VAL A CA  1 
ATOM   187  C  C   . VAL A 1 26  ? 5.803   6.325   55.640  1.00 19.22  ? 26  VAL A C   1 
ATOM   188  O  O   . VAL A 1 26  ? 5.649   7.513   55.345  1.00 20.78  ? 26  VAL A O   1 
ATOM   189  C  CB  . VAL A 1 26  ? 7.627   4.973   54.498  1.00 19.82  ? 26  VAL A CB  1 
ATOM   190  C  CG1 . VAL A 1 26  ? 7.229   5.730   53.240  1.00 22.86  ? 26  VAL A CG1 1 
ATOM   191  C  CG2 . VAL A 1 26  ? 9.130   4.708   54.517  1.00 22.49  ? 26  VAL A CG2 1 
ATOM   192  N  N   . GLN A 1 27  ? 4.771   5.512   55.902  1.00 18.32  ? 27  GLN A N   1 
ATOM   193  C  CA  . GLN A 1 27  ? 3.404   6.018   55.856  1.00 16.44  ? 27  GLN A CA  1 
ATOM   194  C  C   . GLN A 1 27  ? 3.159   7.054   56.950  1.00 18.29  ? 27  GLN A C   1 
ATOM   195  O  O   . GLN A 1 27  ? 2.412   8.012   56.742  1.00 17.52  ? 27  GLN A O   1 
ATOM   196  C  CB  . GLN A 1 27  ? 2.419   4.855   55.964  1.00 17.21  ? 27  GLN A CB  1 
ATOM   197  C  CG  . GLN A 1 27  ? 2.467   3.968   54.722  1.00 18.65  ? 27  GLN A CG  1 
ATOM   198  C  CD  . GLN A 1 27  ? 1.857   2.594   54.883  1.00 20.58  ? 27  GLN A CD  1 
ATOM   199  O  OE1 . GLN A 1 27  ? 0.651   2.406   54.758  1.00 19.97  ? 27  GLN A OE1 1 
ATOM   200  N  NE2 . GLN A 1 27  ? 2.712   1.607   55.109  1.00 21.99  ? 27  GLN A NE2 1 
ATOM   201  N  N   . ALA A 1 28  ? 3.746   6.847   58.125  1.00 17.70  ? 28  ALA A N   1 
ATOM   202  C  CA  . ALA A 1 28  ? 3.674   7.843   59.187  1.00 19.01  ? 28  ALA A CA  1 
ATOM   203  C  C   . ALA A 1 28  ? 4.354   9.150   58.737  1.00 17.68  ? 28  ALA A C   1 
ATOM   204  O  O   . ALA A 1 28  ? 3.807   10.224  58.919  1.00 16.85  ? 28  ALA A O   1 
ATOM   205  C  CB  . ALA A 1 28  ? 4.283   7.287   60.452  1.00 19.11  ? 28  ALA A CB  1 
ATOM   206  N  N   . LEU A 1 29  ? 5.536   9.048   58.124  1.00 17.98  ? 29  LEU A N   1 
ATOM   207  C  CA  . LEU A 1 29  ? 6.249   10.198  57.582  1.00 20.60  ? 29  LEU A CA  1 
ATOM   208  C  C   . LEU A 1 29  ? 5.444   10.925  56.506  1.00 21.02  ? 29  LEU A C   1 
ATOM   209  O  O   . LEU A 1 29  ? 5.440   12.144  56.471  1.00 19.29  ? 29  LEU A O   1 
ATOM   210  C  CB  . LEU A 1 29  ? 7.593   9.725   57.047  1.00 20.19  ? 29  LEU A CB  1 
ATOM   211  C  CG  . LEU A 1 29  ? 8.604   9.411   58.142  1.00 20.36  ? 29  LEU A CG  1 
ATOM   212  C  CD1 . LEU A 1 29  ? 9.773   8.623   57.611  1.00 21.69  ? 29  LEU A CD1 1 
ATOM   213  C  CD2 . LEU A 1 29  ? 9.109   10.700  58.797  1.00 22.54  ? 29  LEU A CD2 1 
ATOM   214  N  N   . MET A 1 30  ? 4.692   10.191  55.682  1.00 21.16  ? 30  MET A N   1 
ATOM   215  C  CA  . MET A 1 30  ? 3.854   10.808  54.664  1.00 20.07  ? 30  MET A CA  1 
ATOM   216  C  C   . MET A 1 30  ? 2.755   11.635  55.328  1.00 19.85  ? 30  MET A C   1 
ATOM   217  O  O   . MET A 1 30  ? 2.422   12.710  54.843  1.00 19.70  ? 30  MET A O   1 
ATOM   218  C  CB  . MET A 1 30  ? 3.209   9.755   53.754  1.00 19.96  ? 30  MET A CB  1 
ATOM   219  C  CG  . MET A 1 30  ? 4.204   9.147   52.777  1.00 20.54  ? 30  MET A CG  1 
ATOM   220  S  SD  . MET A 1 30  ? 3.533   7.640   52.018  1.00 20.30  ? 30  MET A SD  1 
ATOM   221  C  CE  . MET A 1 30  ? 2.138   8.306   51.095  1.00 22.24  ? 30  MET A CE  1 
ATOM   222  N  N   . LYS A 1 31  ? 2.195   11.120  56.422  1.00 20.66  ? 31  LYS A N   1 
ATOM   223  C  CA  . LYS A 1 31  ? 1.116   11.798  57.107  1.00 23.69  ? 31  LYS A CA  1 
ATOM   224  C  C   . LYS A 1 31  ? 1.683   13.085  57.727  1.00 24.01  ? 31  LYS A C   1 
ATOM   225  O  O   . LYS A 1 31  ? 1.048   14.124  57.659  1.00 22.71  ? 31  LYS A O   1 
ATOM   226  C  CB  . LYS A 1 31  ? 0.432   10.844  58.087  1.00 27.73  ? 31  LYS A CB  1 
ATOM   227  C  CG  . LYS A 1 31  ? -0.723  11.461  58.871  1.00 31.45  ? 31  LYS A CG  1 
ATOM   228  C  CD  . LYS A 1 31  ? -1.040  10.763  60.162  1.00 33.12  ? 31  LYS A CD  1 
ATOM   229  C  CE  . LYS A 1 31  ? -0.929  11.706  61.358  1.00 39.04  ? 31  LYS A CE  1 
ATOM   230  N  NZ  . LYS A 1 31  ? 0.465   12.217  61.578  1.00 37.38  ? 31  LYS A NZ  1 
ATOM   231  N  N   . ILE A 1 32  ? 2.911   13.040  58.255  1.00 20.21  ? 32  ILE A N   1 
ATOM   232  C  CA  . ILE A 1 32  ? 3.544   14.243  58.770  1.00 20.10  ? 32  ILE A CA  1 
ATOM   233  C  C   . ILE A 1 32  ? 3.748   15.243  57.637  1.00 21.19  ? 32  ILE A C   1 
ATOM   234  O  O   . ILE A 1 32  ? 3.356   16.412  57.768  1.00 20.08  ? 32  ILE A O   1 
ATOM   235  C  CB  . ILE A 1 32  ? 4.862   13.925  59.495  1.00 19.68  ? 32  ILE A CB  1 
ATOM   236  C  CG1 . ILE A 1 32  ? 4.601   13.106  60.767  1.00 19.64  ? 32  ILE A CG1 1 
ATOM   237  C  CG2 . ILE A 1 32  ? 5.612   15.199  59.814  1.00 18.38  ? 32  ILE A CG2 1 
ATOM   238  C  CD1 . ILE A 1 32  ? 5.840   12.390  61.302  1.00 20.73  ? 32  ILE A CD1 1 
ATOM   239  N  N   . ALA A 1 33  ? 4.336   14.774  56.530  1.00 18.25  ? 33  ALA A N   1 
ATOM   240  C  CA  . ALA A 1 33  ? 4.534   15.636  55.384  1.00 20.34  ? 33  ALA A CA  1 
ATOM   241  C  C   . ALA A 1 33  ? 3.235   16.343  54.997  1.00 23.76  ? 33  ALA A C   1 
ATOM   242  O  O   . ALA A 1 33  ? 3.257   17.524  54.647  1.00 22.54  ? 33  ALA A O   1 
ATOM   243  C  CB  . ALA A 1 33  ? 5.120   14.874  54.217  1.00 18.88  ? 33  ALA A CB  1 
ATOM   244  N  N   . ASP A 1 34  ? 2.107   15.621  55.000  1.00 23.58  ? 34  ASP A N   1 
ATOM   245  C  CA  . ASP A 1 34  ? 0.840   16.261  54.678  1.00 27.74  ? 34  ASP A CA  1 
ATOM   246  C  C   . ASP A 1 34  ? 0.506   17.359  55.690  1.00 29.14  ? 34  ASP A C   1 
ATOM   247  O  O   . ASP A 1 34  ? 0.035   18.418  55.309  1.00 27.24  ? 34  ASP A O   1 
ATOM   248  C  CB  . ASP A 1 34  ? -0.317  15.263  54.618  1.00 28.63  ? 34  ASP A CB  1 
ATOM   249  C  CG  . ASP A 1 34  ? -0.292  14.384  53.375  1.00 30.58  ? 34  ASP A CG  1 
ATOM   250  O  OD1 . ASP A 1 34  ? 0.284   14.807  52.367  1.00 35.45  ? 34  ASP A OD1 1 
ATOM   251  O  OD2 . ASP A 1 34  ? -0.829  13.281  53.433  1.00 31.31  ? 34  ASP A OD2 1 
ATOM   252  N  N   . GLU A 1 35  ? 0.720   17.106  56.983  1.00 29.77  ? 35  GLU A N   1 
ATOM   253  C  CA  . GLU A 1 35  ? 0.495   18.127  57.997  1.00 29.77  ? 35  GLU A CA  1 
ATOM   254  C  C   . GLU A 1 35  ? 1.487   19.288  57.820  1.00 27.16  ? 35  GLU A C   1 
ATOM   255  O  O   . GLU A 1 35  ? 1.094   20.438  57.837  1.00 28.58  ? 35  GLU A O   1 
ATOM   256  C  CB  . GLU A 1 35  ? 0.584   17.538  59.411  1.00 32.22  ? 35  GLU A CB  1 
ATOM   257  C  CG  . GLU A 1 35  ? -0.432  16.445  59.695  1.00 37.12  ? 35  GLU A CG  1 
ATOM   258  C  CD  . GLU A 1 35  ? -0.124  15.522  60.870  1.00 43.32  ? 35  GLU A CD  1 
ATOM   259  O  OE1 . GLU A 1 35  ? -1.082  15.092  61.570  1.00 45.44  ? 35  GLU A OE1 1 
ATOM   260  O  OE2 . GLU A 1 35  ? 1.069   15.208  61.080  1.00 45.71  ? 35  GLU A OE2 1 
ATOM   261  N  N   . LEU A 1 36  ? 2.782   19.026  57.665  1.00 20.52  ? 36  LEU A N   1 
ATOM   262  C  CA  . LEU A 1 36  ? 3.750   20.085  57.866  1.00 19.69  ? 36  LEU A CA  1 
ATOM   263  C  C   . LEU A 1 36  ? 4.216   20.714  56.558  1.00 20.90  ? 36  LEU A C   1 
ATOM   264  O  O   . LEU A 1 36  ? 4.780   21.807  56.575  1.00 21.31  ? 36  LEU A O   1 
ATOM   265  C  CB  . LEU A 1 36  ? 4.923   19.496  58.644  1.00 19.97  ? 36  LEU A CB  1 
ATOM   266  C  CG  . LEU A 1 36  ? 4.609   19.090  60.087  1.00 20.86  ? 36  LEU A CG  1 
ATOM   267  C  CD1 . LEU A 1 36  ? 5.868   18.662  60.827  1.00 19.62  ? 36  LEU A CD1 1 
ATOM   268  C  CD2 . LEU A 1 36  ? 3.918   20.221  60.835  1.00 21.68  ? 36  LEU A CD2 1 
ATOM   269  N  N   . GLY A 1 37  ? 4.083   20.002  55.438  1.00 22.28  ? 37  GLY A N   1 
ATOM   270  C  CA  . GLY A 1 37  ? 4.351   20.589  54.138  1.00 22.89  ? 37  GLY A CA  1 
ATOM   271  C  C   . GLY A 1 37  ? 5.656   20.095  53.526  1.00 23.70  ? 37  GLY A C   1 
ATOM   272  O  O   . GLY A 1 37  ? 6.083   18.966  53.790  1.00 22.76  ? 37  GLY A O   1 
ATOM   273  N  N   . GLU A 1 38  ? 6.274   20.960  52.711  1.00 23.90  ? 38  GLU A N   1 
ATOM   274  C  CA  . GLU A 1 38  ? 7.329   20.561  51.787  1.00 23.19  ? 38  GLU A CA  1 
ATOM   275  C  C   . GLU A 1 38  ? 8.621   20.167  52.508  1.00 19.99  ? 38  GLU A C   1 
ATOM   276  O  O   . GLU A 1 38  ? 9.458   19.485  51.920  1.00 18.60  ? 38  GLU A O   1 
ATOM   277  C  CB  . GLU A 1 38  ? 7.626   21.642  50.733  1.00 24.42  ? 38  GLU A CB  1 
ATOM   278  C  CG  . GLU A 1 38  ? 8.165   22.961  51.256  1.00 26.75  ? 38  GLU A CG  1 
ATOM   279  C  CD  . GLU A 1 38  ? 8.367   24.026  50.176  1.00 31.47  ? 38  GLU A CD  1 
ATOM   280  O  OE1 . GLU A 1 38  ? 8.581   23.673  48.996  1.00 30.29  ? 38  GLU A OE1 1 
ATOM   281  O  OE2 . GLU A 1 38  ? 8.293   25.220  50.505  1.00 35.21  ? 38  GLU A OE2 1 
ATOM   282  N  N   . ILE A 1 39  ? 8.794   20.600  53.754  1.00 18.70  ? 39  ILE A N   1 
ATOM   283  C  CA  . ILE A 1 39  ? 10.016  20.258  54.455  1.00 19.48  ? 39  ILE A CA  1 
ATOM   284  C  C   . ILE A 1 39  ? 9.746   20.242  55.950  1.00 18.97  ? 39  ILE A C   1 
ATOM   285  O  O   . ILE A 1 39  ? 9.051   21.119  56.451  1.00 16.20  ? 39  ILE A O   1 
ATOM   286  C  CB  . ILE A 1 39  ? 11.154  21.214  54.068  1.00 21.06  ? 39  ILE A CB  1 
ATOM   287  C  CG1 . ILE A 1 39  ? 12.481  20.785  54.690  1.00 21.65  ? 39  ILE A CG1 1 
ATOM   288  C  CG2 . ILE A 1 39  ? 10.788  22.647  54.440  1.00 22.94  ? 39  ILE A CG2 1 
ATOM   289  C  CD1 . ILE A 1 39  ? 13.667  21.571  54.145  1.00 20.28  ? 39  ILE A CD1 1 
ATOM   290  N  N   . PHE A 1 40  ? 10.255  19.215  56.637  1.00 16.95  ? 40  PHE A N   1 
ATOM   291  C  CA  . PHE A 1 40  ? 10.331  19.274  58.080  1.00 17.23  ? 40  PHE A CA  1 
ATOM   292  C  C   . PHE A 1 40  ? 11.640  18.691  58.596  1.00 19.01  ? 40  PHE A C   1 
ATOM   293  O  O   . PHE A 1 40  ? 12.272  17.861  57.957  1.00 15.48  ? 40  PHE A O   1 
ATOM   294  C  CB  . PHE A 1 40  ? 9.117   18.619  58.719  1.00 17.54  ? 40  PHE A CB  1 
ATOM   295  C  CG  . PHE A 1 40  ? 8.906   17.175  58.374  1.00 18.68  ? 40  PHE A CG  1 
ATOM   296  C  CD1 . PHE A 1 40  ? 8.247   16.828  57.205  1.00 19.15  ? 40  PHE A CD1 1 
ATOM   297  C  CD2 . PHE A 1 40  ? 9.372   16.182  59.213  1.00 19.61  ? 40  PHE A CD2 1 
ATOM   298  C  CE1 . PHE A 1 40  ? 8.048   15.497  56.893  1.00 19.78  ? 40  PHE A CE1 1 
ATOM   299  C  CE2 . PHE A 1 40  ? 9.221   14.850  58.880  1.00 19.78  ? 40  PHE A CE2 1 
ATOM   300  C  CZ  . PHE A 1 40  ? 8.543   14.513  57.732  1.00 21.38  ? 40  PHE A CZ  1 
ATOM   301  N  N   . LYS A 1 41  ? 12.016  19.177  59.784  1.00 20.06  ? 41  LYS A N   1 
ATOM   302  C  CA  . LYS A 1 41  ? 13.148  18.679  60.530  1.00 23.27  ? 41  LYS A CA  1 
ATOM   303  C  C   . LYS A 1 41  ? 12.730  17.486  61.387  1.00 20.42  ? 41  LYS A C   1 
ATOM   304  O  O   . LYS A 1 41  ? 11.687  17.444  62.015  1.00 18.78  ? 41  LYS A O   1 
ATOM   305  C  CB  . LYS A 1 41  ? 13.705  19.788  61.429  1.00 27.40  ? 41  LYS A CB  1 
ATOM   306  C  CG  . LYS A 1 41  ? 14.942  19.411  62.223  1.00 34.16  ? 41  LYS A CG  1 
ATOM   307  C  CD  . LYS A 1 41  ? 15.751  20.599  62.713  1.00 37.66  ? 41  LYS A CD  1 
ATOM   308  C  CE  . LYS A 1 41  ? 14.976  21.446  63.702  1.00 42.96  ? 41  LYS A CE  1 
ATOM   309  N  NZ  . LYS A 1 41  ? 14.188  22.511  63.031  1.00 45.90  ? 41  LYS A NZ  1 
ATOM   310  N  N   . PHE A 1 42  ? 13.604  16.499  61.444  1.00 19.93  ? 42  PHE A N   1 
ATOM   311  C  CA  . PHE A 1 42  ? 13.328  15.354  62.267  1.00 19.29  ? 42  PHE A CA  1 
ATOM   312  C  C   . PHE A 1 42  ? 14.567  15.113  63.110  1.00 20.71  ? 42  PHE A C   1 
ATOM   313  O  O   . PHE A 1 42  ? 15.650  14.960  62.545  1.00 21.63  ? 42  PHE A O   1 
ATOM   314  C  CB  . PHE A 1 42  ? 12.992  14.198  61.332  1.00 20.05  ? 42  PHE A CB  1 
ATOM   315  C  CG  . PHE A 1 42  ? 12.588  12.942  62.044  1.00 20.97  ? 42  PHE A CG  1 
ATOM   316  C  CD1 . PHE A 1 42  ? 13.538  12.161  62.685  1.00 24.19  ? 42  PHE A CD1 1 
ATOM   317  C  CD2 . PHE A 1 42  ? 11.265  12.575  62.095  1.00 21.71  ? 42  PHE A CD2 1 
ATOM   318  C  CE1 . PHE A 1 42  ? 13.160  11.003  63.343  1.00 23.73  ? 42  PHE A CE1 1 
ATOM   319  C  CE2 . PHE A 1 42  ? 10.893  11.407  62.744  1.00 24.08  ? 42  PHE A CE2 1 
ATOM   320  C  CZ  . PHE A 1 42  ? 11.839  10.623  63.351  1.00 22.98  ? 42  PHE A CZ  1 
ATOM   321  N  N   . GLU A 1 43  ? 14.392  15.094  64.427  1.00 23.37  ? 43  GLU A N   1 
ATOM   322  C  CA  . GLU A 1 43  ? 15.518  15.011  65.339  1.00 26.80  ? 43  GLU A CA  1 
ATOM   323  C  C   . GLU A 1 43  ? 15.469  13.679  66.066  1.00 26.00  ? 43  GLU A C   1 
ATOM   324  O  O   . GLU A 1 43  ? 14.418  13.195  66.489  1.00 23.91  ? 43  GLU A O   1 
ATOM   325  C  CB  . GLU A 1 43  ? 15.525  16.202  66.308  1.00 32.72  ? 43  GLU A CB  1 
ATOM   326  C  CG  . GLU A 1 43  ? 15.835  17.505  65.598  1.00 37.61  ? 43  GLU A CG  1 
ATOM   327  C  CD  . GLU A 1 43  ? 16.425  18.628  66.435  1.00 46.12  ? 43  GLU A CD  1 
ATOM   328  O  OE1 . GLU A 1 43  ? 17.329  18.347  67.276  1.00 48.50  ? 43  GLU A OE1 1 
ATOM   329  O  OE2 . GLU A 1 43  ? 16.032  19.797  66.186  1.00 48.95  ? 43  GLU A OE2 1 
ATOM   330  N  N   . ALA A 1 44  ? 16.651  13.104  66.222  1.00 23.62  ? 44  ALA A N   1 
ATOM   331  C  CA  . ALA A 1 44  ? 16.833  11.986  67.119  1.00 28.21  ? 44  ALA A CA  1 
ATOM   332  C  C   . ALA A 1 44  ? 17.998  12.317  68.041  1.00 28.72  ? 44  ALA A C   1 
ATOM   333  O  O   . ALA A 1 44  ? 18.652  13.354  67.886  1.00 25.96  ? 44  ALA A O   1 
ATOM   334  C  CB  . ALA A 1 44  ? 17.080  10.716  66.320  1.00 29.73  ? 44  ALA A CB  1 
ATOM   335  N  N   . PRO A 1 45  ? 18.205  11.473  69.071  1.00 33.84  ? 45  PRO A N   1 
ATOM   336  C  CA  . PRO A 1 45  ? 19.462  11.444  69.817  1.00 35.89  ? 45  PRO A CA  1 
ATOM   337  C  C   . PRO A 1 45  ? 20.640  11.301  68.859  1.00 36.72  ? 45  PRO A C   1 
ATOM   338  O  O   . PRO A 1 45  ? 20.807  10.270  68.212  1.00 38.71  ? 45  PRO A O   1 
ATOM   339  C  CB  . PRO A 1 45  ? 19.344  10.206  70.722  1.00 35.50  ? 45  PRO A CB  1 
ATOM   340  C  CG  . PRO A 1 45  ? 17.850  9.958   70.853  1.00 38.42  ? 45  PRO A CG  1 
ATOM   341  C  CD  . PRO A 1 45  ? 17.216  10.516  69.590  1.00 35.14  ? 45  PRO A CD  1 
ATOM   342  N  N   . GLY A 1 46  ? 21.406  12.381  68.708  1.00 38.26  ? 46  GLY A N   1 
ATOM   343  C  CA  . GLY A 1 46  ? 22.643  12.317  67.949  1.00 39.10  ? 46  GLY A CA  1 
ATOM   344  C  C   . GLY A 1 46  ? 22.449  12.433  66.437  1.00 38.08  ? 46  GLY A C   1 
ATOM   345  O  O   . GLY A 1 46  ? 23.391  12.217  65.681  1.00 39.65  ? 46  GLY A O   1 
ATOM   346  N  N   . ARG A 1 47  ? 21.254  12.796  65.966  1.00 38.60  ? 47  ARG A N   1 
ATOM   347  C  CA  . ARG A 1 47  ? 21.127  13.032  64.541  1.00 37.60  ? 47  ARG A CA  1 
ATOM   348  C  C   . ARG A 1 47  ? 19.955  13.960  64.215  1.00 33.35  ? 47  ARG A C   1 
ATOM   349  O  O   . ARG A 1 47  ? 19.048  14.199  65.005  1.00 32.40  ? 47  ARG A O   1 
ATOM   350  C  CB  . ARG A 1 47  ? 21.095  11.720  63.745  1.00 42.73  ? 47  ARG A CB  1 
ATOM   351  C  CG  . ARG A 1 47  ? 19.956  10.761  64.058  1.00 44.21  ? 47  ARG A CG  1 
ATOM   352  C  CD  . ARG A 1 47  ? 20.176  9.449   63.321  1.00 52.54  ? 47  ARG A CD  1 
ATOM   353  N  NE  . ARG A 1 47  ? 19.001  8.578   63.217  1.00 60.63  ? 47  ARG A NE  1 
ATOM   354  C  CZ  . ARG A 1 47  ? 18.401  7.955   64.232  1.00 57.37  ? 47  ARG A CZ  1 
ATOM   355  N  NH1 . ARG A 1 47  ? 18.866  8.064   65.465  1.00 50.96  ? 47  ARG A NH1 1 
ATOM   356  N  NH2 . ARG A 1 47  ? 17.316  7.228   64.007  1.00 61.77  ? 47  ARG A NH2 1 
ATOM   357  N  N   . VAL A 1 48  ? 20.056  14.528  63.015  1.00 28.65  ? 48  VAL A N   1 
ATOM   358  C  CA  . VAL A 1 48  ? 19.067  15.427  62.450  1.00 30.07  ? 48  VAL A CA  1 
ATOM   359  C  C   . VAL A 1 48  ? 18.986  15.099  60.969  1.00 24.96  ? 48  VAL A C   1 
ATOM   360  O  O   . VAL A 1 48  ? 20.019  14.871  60.333  1.00 22.40  ? 48  VAL A O   1 
ATOM   361  C  CB  . VAL A 1 48  ? 19.449  16.909  62.639  1.00 29.83  ? 48  VAL A CB  1 
ATOM   362  C  CG1 . VAL A 1 48  ? 18.404  17.831  62.025  1.00 32.06  ? 48  VAL A CG1 1 
ATOM   363  C  CG2 . VAL A 1 48  ? 19.676  17.258  64.096  1.00 34.85  ? 48  VAL A CG2 1 
ATOM   364  N  N   . THR A 1 49  ? 17.764  15.020  60.446  1.00 22.92  ? 49  THR A N   1 
ATOM   365  C  CA  . THR A 1 49  ? 17.628  15.052  59.008  1.00 25.12  ? 49  THR A CA  1 
ATOM   366  C  C   . THR A 1 49  ? 16.447  15.959  58.671  1.00 23.75  ? 49  THR A C   1 
ATOM   367  O  O   . THR A 1 49  ? 15.649  16.280  59.546  1.00 25.75  ? 49  THR A O   1 
ATOM   368  C  CB  . THR A 1 49  ? 17.612  13.634  58.421  1.00 28.45  ? 49  THR A CB  1 
ATOM   369  O  OG1 . THR A 1 49  ? 17.677  13.742  56.993  1.00 25.98  ? 49  THR A OG1 1 
ATOM   370  C  CG2 . THR A 1 49  ? 16.404  12.826  58.835  1.00 29.95  ? 49  THR A CG2 1 
ATOM   371  N  N   . ARG A 1 50  ? 16.385  16.392  57.412  1.00 19.18  ? 50  ARG A N   1 
ATOM   372  C  CA  . ARG A 1 50  ? 15.260  17.129  56.884  1.00 20.95  ? 50  ARG A CA  1 
ATOM   373  C  C   . ARG A 1 50  ? 14.563  16.252  55.855  1.00 19.62  ? 50  ARG A C   1 
ATOM   374  O  O   . ARG A 1 50  ? 15.229  15.742  54.964  1.00 21.18  ? 50  ARG A O   1 
ATOM   375  C  CB  . ARG A 1 50  ? 15.801  18.438  56.313  1.00 21.81  ? 50  ARG A CB  1 
ATOM   376  C  CG  . ARG A 1 50  ? 16.556  19.254  57.356  1.00 25.40  ? 50  ARG A CG  1 
ATOM   377  C  CD  . ARG A 1 50  ? 17.768  19.968  56.814  1.00 28.23  ? 50  ARG A CD  1 
ATOM   378  N  NE  . ARG A 1 50  ? 18.614  20.417  57.910  1.00 31.66  ? 50  ARG A NE  1 
ATOM   379  C  CZ  . ARG A 1 50  ? 19.522  19.675  58.524  1.00 30.38  ? 50  ARG A CZ  1 
ATOM   380  N  NH1 . ARG A 1 50  ? 19.738  18.422  58.156  1.00 27.42  ? 50  ARG A NH1 1 
ATOM   381  N  NH2 . ARG A 1 50  ? 20.195  20.192  59.533  1.00 31.28  ? 50  ARG A NH2 1 
ATOM   382  N  N   . TYR A 1 51  ? 13.250  16.055  56.012  1.00 18.84  ? 51  TYR A N   1 
ATOM   383  C  CA  . TYR A 1 51  ? 12.407  15.340  55.055  1.00 18.54  ? 51  TYR A CA  1 
ATOM   384  C  C   . TYR A 1 51  ? 11.842  16.301  54.000  1.00 17.71  ? 51  TYR A C   1 
ATOM   385  O  O   . TYR A 1 51  ? 11.139  17.269  54.321  1.00 18.27  ? 51  TYR A O   1 
ATOM   386  C  CB  . TYR A 1 51  ? 11.299  14.582  55.792  1.00 18.27  ? 51  TYR A CB  1 
ATOM   387  C  CG  . TYR A 1 51  ? 11.804  13.292  56.425  1.00 19.75  ? 51  TYR A CG  1 
ATOM   388  C  CD1 . TYR A 1 51  ? 11.831  12.091  55.721  1.00 22.08  ? 51  TYR A CD1 1 
ATOM   389  C  CD2 . TYR A 1 51  ? 12.337  13.301  57.707  1.00 21.16  ? 51  TYR A CD2 1 
ATOM   390  C  CE1 . TYR A 1 51  ? 12.325  10.930  56.298  1.00 21.72  ? 51  TYR A CE1 1 
ATOM   391  C  CE2 . TYR A 1 51  ? 12.831  12.149  58.295  1.00 21.86  ? 51  TYR A CE2 1 
ATOM   392  C  CZ  . TYR A 1 51  ? 12.854  10.970  57.573  1.00 21.38  ? 51  TYR A CZ  1 
ATOM   393  O  OH  . TYR A 1 51  ? 13.376  9.885   58.190  1.00 27.31  ? 51  TYR A OH  1 
ATOM   394  N  N   . LEU A 1 52  ? 12.130  16.012  52.726  1.00 17.25  ? 52  LEU A N   1 
ATOM   395  C  CA  . LEU A 1 52  ? 11.698  16.832  51.611  1.00 16.38  ? 52  LEU A CA  1 
ATOM   396  C  C   . LEU A 1 52  ? 10.549  16.150  50.854  1.00 16.08  ? 52  LEU A C   1 
ATOM   397  O  O   . LEU A 1 52  ? 10.631  14.965  50.580  1.00 17.93  ? 52  LEU A O   1 
ATOM   398  C  CB  . LEU A 1 52  ? 12.872  17.049  50.663  1.00 16.96  ? 52  LEU A CB  1 
ATOM   399  C  CG  . LEU A 1 52  ? 14.108  17.741  51.226  1.00 19.22  ? 52  LEU A CG  1 
ATOM   400  C  CD1 . LEU A 1 52  ? 15.096  18.021  50.108  1.00 17.69  ? 52  LEU A CD1 1 
ATOM   401  C  CD2 . LEU A 1 52  ? 13.697  19.021  51.921  1.00 20.58  ? 52  LEU A CD2 1 
ATOM   402  N  N   . SER A 1 53  ? 9.520   16.917  50.492  1.00 16.75  ? 53  SER A N   1 
ATOM   403  C  CA  . SER A 1 53  ? 8.352   16.403  49.790  1.00 17.91  ? 53  SER A CA  1 
ATOM   404  C  C   . SER A 1 53  ? 7.973   17.184  48.514  1.00 18.49  ? 53  SER A C   1 
ATOM   405  O  O   . SER A 1 53  ? 7.068   16.763  47.796  1.00 21.53  ? 53  SER A O   1 
ATOM   406  C  CB  . SER A 1 53  ? 7.216   16.390  50.719  1.00 18.50  ? 53  SER A CB  1 
ATOM   407  O  OG  . SER A 1 53  ? 7.467   15.535  51.821  1.00 20.88  ? 53  SER A OG  1 
ATOM   408  N  N   . SER A 1 54  ? 8.567   18.348  48.230  1.00 18.33  ? 54  SER A N   1 
ATOM   409  C  CA  . SER A 1 54  ? 8.134   19.116  47.075  1.00 17.78  ? 54  SER A CA  1 
ATOM   410  C  C   . SER A 1 54  ? 9.111   18.917  45.939  1.00 15.74  ? 54  SER A C   1 
ATOM   411  O  O   . SER A 1 54  ? 10.315  18.775  46.172  1.00 17.56  ? 54  SER A O   1 
ATOM   412  C  CB  . SER A 1 54  ? 7.937   20.603  47.383  1.00 20.22  ? 54  SER A CB  1 
ATOM   413  O  OG  . SER A 1 54  ? 9.181   21.218  47.784  1.00 19.41  ? 54  SER A OG  1 
ATOM   414  N  N   . GLN A 1 55  ? 8.599   18.975  44.709  1.00 15.19  ? 55  GLN A N   1 
ATOM   415  C  CA  . GLN A 1 55  ? 9.445   18.982  43.533  1.00 15.88  ? 55  GLN A CA  1 
ATOM   416  C  C   . GLN A 1 55  ? 10.346  20.203  43.569  1.00 16.22  ? 55  GLN A C   1 
ATOM   417  O  O   . GLN A 1 55  ? 11.485  20.090  43.170  1.00 17.28  ? 55  GLN A O   1 
ATOM   418  C  CB  . GLN A 1 55  ? 8.634   18.956  42.245  1.00 17.31  ? 55  GLN A CB  1 
ATOM   419  C  CG  . GLN A 1 55  ? 9.479   18.843  41.010  1.00 17.76  ? 55  GLN A CG  1 
ATOM   420  C  CD  . GLN A 1 55  ? 9.791   20.171  40.402  1.00 20.17  ? 55  GLN A CD  1 
ATOM   421  O  OE1 . GLN A 1 55  ? 9.329   21.220  40.861  1.00 21.76  ? 55  GLN A OE1 1 
ATOM   422  N  NE2 . GLN A 1 55  ? 10.588  20.117  39.362  1.00 23.15  ? 55  GLN A NE2 1 
ATOM   423  N  N   . ARG A 1 56  ? 9.863   21.343  44.076  1.00 17.16  ? 56  ARG A N   1 
ATOM   424  C  CA  . ARG A 1 56  ? 10.642  22.591  44.093  1.00 19.32  ? 56  ARG A CA  1 
ATOM   425  C  C   . ARG A 1 56  ? 11.975  22.413  44.832  1.00 18.77  ? 56  ARG A C   1 
ATOM   426  O  O   . ARG A 1 56  ? 13.024  22.877  44.373  1.00 18.74  ? 56  ARG A O   1 
ATOM   427  C  CB  . ARG A 1 56  ? 9.789   23.678  44.761  1.00 22.68  ? 56  ARG A CB  1 
ATOM   428  C  CG  . ARG A 1 56  ? 10.387  25.081  44.788  1.00 28.09  ? 56  ARG A CG  1 
ATOM   429  C  CD  . ARG A 1 56  ? 9.498   26.031  45.594  1.00 28.18  ? 56  ARG A CD  1 
ATOM   430  N  NE  . ARG A 1 56  ? 9.604   25.868  47.046  1.00 32.19  ? 56  ARG A NE  1 
ATOM   431  C  CZ  . ARG A 1 56  ? 10.492  26.491  47.809  1.00 37.07  ? 56  ARG A CZ  1 
ATOM   432  N  NH1 . ARG A 1 56  ? 11.363  27.321  47.262  1.00 41.13  ? 56  ARG A NH1 1 
ATOM   433  N  NH2 . ARG A 1 56  ? 10.497  26.304  49.118  1.00 42.98  ? 56  ARG A NH2 1 
ATOM   434  N  N   . LEU A 1 57  ? 11.929  21.727  45.981  1.00 17.26  ? 57  LEU A N   1 
ATOM   435  C  CA  . LEU A 1 57  ? 13.075  21.577  46.844  1.00 17.53  ? 57  LEU A CA  1 
ATOM   436  C  C   . LEU A 1 57  ? 13.877  20.346  46.435  1.00 17.94  ? 57  LEU A C   1 
ATOM   437  O  O   . LEU A 1 57  ? 15.090  20.361  46.517  1.00 17.59  ? 57  LEU A O   1 
ATOM   438  C  CB  . LEU A 1 57  ? 12.609  21.449  48.291  1.00 17.96  ? 57  LEU A CB  1 
ATOM   439  C  CG  . LEU A 1 57  ? 12.088  22.699  48.997  1.00 18.48  ? 57  LEU A CG  1 
ATOM   440  C  CD1 . LEU A 1 57  ? 11.780  22.352  50.444  1.00 17.32  ? 57  LEU A CD1 1 
ATOM   441  C  CD2 . LEU A 1 57  ? 13.093  23.827  48.951  1.00 18.90  ? 57  LEU A CD2 1 
ATOM   442  N  N   . ILE A 1 58  ? 13.180  19.279  46.015  1.00 17.22  ? 58  ILE A N   1 
ATOM   443  C  CA  . ILE A 1 58  ? 13.844  18.054  45.616  1.00 17.07  ? 58  ILE A CA  1 
ATOM   444  C  C   . ILE A 1 58  ? 14.665  18.276  44.351  1.00 18.16  ? 58  ILE A C   1 
ATOM   445  O  O   . ILE A 1 58  ? 15.709  17.642  44.157  1.00 18.52  ? 58  ILE A O   1 
ATOM   446  C  CB  . ILE A 1 58  ? 12.806  16.927  45.488  1.00 16.56  ? 58  ILE A CB  1 
ATOM   447  C  CG1 . ILE A 1 58  ? 12.412  16.448  46.888  1.00 16.24  ? 58  ILE A CG1 1 
ATOM   448  C  CG2 . ILE A 1 58  ? 13.346  15.794  44.602  1.00 18.84  ? 58  ILE A CG2 1 
ATOM   449  C  CD1 . ILE A 1 58  ? 11.085  15.700  46.950  1.00 16.43  ? 58  ILE A CD1 1 
ATOM   450  N  N   . LYS A 1 59  ? 14.208  19.157  43.479  1.00 17.71  ? 59  LYS A N   1 
ATOM   451  C  CA  . LYS A 1 59  ? 14.949  19.377  42.256  1.00 20.22  ? 59  LYS A CA  1 
ATOM   452  C  C   . LYS A 1 59  ? 16.298  20.004  42.603  1.00 19.54  ? 59  LYS A C   1 
ATOM   453  O  O   . LYS A 1 59  ? 17.280  19.742  41.949  1.00 18.72  ? 59  LYS A O   1 
ATOM   454  C  CB  . LYS A 1 59  ? 14.132  20.173  41.238  1.00 24.18  ? 59  LYS A CB  1 
ATOM   455  C  CG  . LYS A 1 59  ? 14.496  21.637  41.113  1.00 27.31  ? 59  LYS A CG  1 
ATOM   456  C  CD  . LYS A 1 59  ? 13.652  22.382  40.117  1.00 29.96  ? 59  LYS A CD  1 
ATOM   457  C  CE  . LYS A 1 59  ? 12.617  23.264  40.783  1.00 34.24  ? 59  LYS A CE  1 
ATOM   458  N  NZ  . LYS A 1 59  ? 12.538  24.590  40.116  1.00 34.42  ? 59  LYS A NZ  1 
ATOM   459  N  N   . GLU A 1 60  ? 16.367  20.761  43.685  1.00 21.91  ? 60  GLU A N   1 
ATOM   460  C  CA  . GLU A 1 60  ? 17.634  21.305  44.137  1.00 23.19  ? 60  GLU A CA  1 
ATOM   461  C  C   . GLU A 1 60  ? 18.468  20.234  44.816  1.00 21.35  ? 60  GLU A C   1 
ATOM   462  O  O   . GLU A 1 60  ? 19.659  20.119  44.550  1.00 18.78  ? 60  GLU A O   1 
ATOM   463  C  CB  . GLU A 1 60  ? 17.399  22.439  45.123  1.00 26.96  ? 60  GLU A CB  1 
ATOM   464  C  CG  . GLU A 1 60  ? 16.960  23.721  44.452  1.00 31.06  ? 60  GLU A CG  1 
ATOM   465  C  CD  . GLU A 1 60  ? 16.932  24.865  45.452  1.00 34.51  ? 60  GLU A CD  1 
ATOM   466  O  OE1 . GLU A 1 60  ? 17.988  25.149  46.084  1.00 28.73  ? 60  GLU A OE1 1 
ATOM   467  O  OE2 . GLU A 1 60  ? 15.840  25.403  45.655  1.00 38.11  ? 60  GLU A OE2 1 
ATOM   468  N  N   . ALA A 1 61  ? 17.828  19.464  45.699  1.00 19.38  ? 61  ALA A N   1 
ATOM   469  C  CA  . ALA A 1 61  ? 18.484  18.345  46.351  1.00 20.60  ? 61  ALA A CA  1 
ATOM   470  C  C   . ALA A 1 61  ? 19.131  17.403  45.331  1.00 20.89  ? 61  ALA A C   1 
ATOM   471  O  O   . ALA A 1 61  ? 20.150  16.790  45.645  1.00 21.00  ? 61  ALA A O   1 
ATOM   472  C  CB  . ALA A 1 61  ? 17.505  17.610  47.222  1.00 20.79  ? 61  ALA A CB  1 
ATOM   473  N  N   . CYS A 1 62  ? 18.597  17.362  44.104  1.00 19.38  ? 62  CYS A N   1 
ATOM   474  C  CA  . CYS A 1 62  ? 19.083  16.427  43.113  1.00 23.03  ? 62  CYS A CA  1 
ATOM   475  C  C   . CYS A 1 62  ? 20.230  17.014  42.296  1.00 24.77  ? 62  CYS A C   1 
ATOM   476  O  O   . CYS A 1 62  ? 20.738  16.333  41.406  1.00 22.08  ? 62  CYS A O   1 
ATOM   477  C  CB  . CYS A 1 62  ? 17.928  15.928  42.257  1.00 23.59  ? 62  CYS A CB  1 
ATOM   478  S  SG  . CYS A 1 62  ? 16.891  14.757  43.189  1.00 25.27  ? 62  CYS A SG  1 
ATOM   479  N  N   . ASP A 1 63  ? 20.673  18.237  42.633  1.00 23.98  ? 63  ASP A N   1 
ATOM   480  C  CA  . ASP A 1 63  ? 21.843  18.819  41.988  1.00 22.19  ? 63  ASP A CA  1 
ATOM   481  C  C   . ASP A 1 63  ? 23.109  18.155  42.562  1.00 21.20  ? 63  ASP A C   1 
ATOM   482  O  O   . ASP A 1 63  ? 23.448  18.327  43.728  1.00 19.17  ? 63  ASP A O   1 
ATOM   483  C  CB  . ASP A 1 63  ? 21.843  20.344  42.157  1.00 23.33  ? 63  ASP A CB  1 
ATOM   484  C  CG  . ASP A 1 63  ? 23.070  21.048  41.608  1.00 24.09  ? 63  ASP A CG  1 
ATOM   485  O  OD1 . ASP A 1 63  ? 24.023  20.344  41.141  1.00 23.16  ? 63  ASP A OD1 1 
ATOM   486  O  OD2 . ASP A 1 63  ? 23.057  22.306  41.657  1.00 22.24  ? 63  ASP A OD2 1 
ATOM   487  N  N   . GLU A 1 64  ? 23.796  17.369  41.731  1.00 19.38  ? 64  GLU A N   1 
ATOM   488  C  CA  . GLU A 1 64  ? 24.945  16.597  42.185  1.00 21.96  ? 64  GLU A CA  1 
ATOM   489  C  C   . GLU A 1 64  ? 26.159  17.464  42.537  1.00 21.51  ? 64  GLU A C   1 
ATOM   490  O  O   . GLU A 1 64  ? 27.062  16.967  43.205  1.00 20.48  ? 64  GLU A O   1 
ATOM   491  C  CB  . GLU A 1 64  ? 25.291  15.544  41.134  1.00 22.78  ? 64  GLU A CB  1 
ATOM   492  C  CG  . GLU A 1 64  ? 24.267  14.414  41.146  1.00 25.11  ? 64  GLU A CG  1 
ATOM   493  C  CD  . GLU A 1 64  ? 24.446  13.371  40.061  1.00 26.39  ? 64  GLU A CD  1 
ATOM   494  O  OE1 . GLU A 1 64  ? 24.262  13.746  38.875  1.00 31.98  ? 64  GLU A OE1 1 
ATOM   495  O  OE2 . GLU A 1 64  ? 24.726  12.197  40.400  1.00 24.99  ? 64  GLU A OE2 1 
ATOM   496  N  N   . SER A 1 65  ? 26.171  18.741  42.119  1.00 22.18  ? 65  SER A N   1 
ATOM   497  C  CA  . SER A 1 65  ? 27.260  19.652  42.460  1.00 25.31  ? 65  SER A CA  1 
ATOM   498  C  C   . SER A 1 65  ? 27.113  20.095  43.905  1.00 23.32  ? 65  SER A C   1 
ATOM   499  O  O   . SER A 1 65  ? 28.093  20.484  44.527  1.00 23.76  ? 65  SER A O   1 
ATOM   500  C  CB  . SER A 1 65  ? 27.326  20.840  41.521  1.00 26.63  ? 65  SER A CB  1 
ATOM   501  O  OG  . SER A 1 65  ? 26.225  21.728  41.734  1.00 27.09  ? 65  SER A OG  1 
ATOM   502  N  N   . ARG A 1 66  ? 25.889  20.006  44.435  1.00 25.01  ? 66  ARG A N   1 
ATOM   503  C  CA  . ARG A 1 66  ? 25.567  20.486  45.772  1.00 22.84  ? 66  ARG A CA  1 
ATOM   504  C  C   . ARG A 1 66  ? 25.346  19.350  46.775  1.00 21.04  ? 66  ARG A C   1 
ATOM   505  O  O   . ARG A 1 66  ? 25.600  19.504  47.967  1.00 21.14  ? 66  ARG A O   1 
ATOM   506  C  CB  . ARG A 1 66  ? 24.316  21.361  45.700  1.00 23.82  ? 66  ARG A CB  1 
ATOM   507  C  CG  . ARG A 1 66  ? 24.496  22.578  44.805  1.00 27.63  ? 66  ARG A CG  1 
ATOM   508  C  CD  . ARG A 1 66  ? 23.175  23.301  44.628  1.00 28.45  ? 66  ARG A CD  1 
ATOM   509  N  NE  . ARG A 1 66  ? 22.813  23.990  45.845  1.00 26.79  ? 66  ARG A NE  1 
ATOM   510  C  CZ  . ARG A 1 66  ? 21.600  24.422  46.119  1.00 24.18  ? 66  ARG A CZ  1 
ATOM   511  N  NH1 . ARG A 1 66  ? 20.646  24.316  45.215  1.00 26.20  ? 66  ARG A NH1 1 
ATOM   512  N  NH2 . ARG A 1 66  ? 21.346  24.959  47.293  1.00 27.63  ? 66  ARG A NH2 1 
ATOM   513  N  N   . PHE A 1 67  ? 24.866  18.210  46.297  1.00 19.70  ? 67  PHE A N   1 
ATOM   514  C  CA  . PHE A 1 67  ? 24.430  17.131  47.171  1.00 17.91  ? 67  PHE A CA  1 
ATOM   515  C  C   . PHE A 1 67  ? 24.848  15.778  46.603  1.00 17.22  ? 67  PHE A C   1 
ATOM   516  O  O   . PHE A 1 67  ? 24.806  15.581  45.391  1.00 18.94  ? 67  PHE A O   1 
ATOM   517  C  CB  . PHE A 1 67  ? 22.914  17.200  47.316  1.00 19.74  ? 67  PHE A CB  1 
ATOM   518  C  CG  . PHE A 1 67  ? 22.400  18.487  47.922  1.00 19.52  ? 67  PHE A CG  1 
ATOM   519  C  CD1 . PHE A 1 67  ? 22.402  18.684  49.296  1.00 19.71  ? 67  PHE A CD1 1 
ATOM   520  C  CD2 . PHE A 1 67  ? 21.899  19.486  47.111  1.00 21.35  ? 67  PHE A CD2 1 
ATOM   521  C  CE1 . PHE A 1 67  ? 21.878  19.846  49.845  1.00 21.68  ? 67  PHE A CE1 1 
ATOM   522  C  CE2 . PHE A 1 67  ? 21.404  20.661  47.657  1.00 21.35  ? 67  PHE A CE2 1 
ATOM   523  C  CZ  . PHE A 1 67  ? 21.396  20.834  49.016  1.00 21.18  ? 67  PHE A CZ  1 
ATOM   524  N  N   . ASP A 1 68  ? 25.253  14.879  47.500  1.00 17.88  ? 68  ASP A N   1 
ATOM   525  C  CA  . ASP A 1 68  ? 25.748  13.544  47.188  1.00 18.54  ? 68  ASP A CA  1 
ATOM   526  C  C   . ASP A 1 68  ? 24.920  12.551  47.994  1.00 16.81  ? 68  ASP A C   1 
ATOM   527  O  O   . ASP A 1 68  ? 24.273  12.901  48.978  1.00 16.30  ? 68  ASP A O   1 
ATOM   528  C  CB  . ASP A 1 68  ? 27.248  13.405  47.462  1.00 18.69  ? 68  ASP A CB  1 
ATOM   529  C  CG  . ASP A 1 68  ? 27.910  12.114  46.982  1.00 24.47  ? 68  ASP A CG  1 
ATOM   530  O  OD1 . ASP A 1 68  ? 27.283  11.357  46.162  1.00 24.21  ? 68  ASP A OD1 1 
ATOM   531  O  OD2 . ASP A 1 68  ? 29.077  11.855  47.433  1.00 24.46  ? 68  ASP A OD2 1 
ATOM   532  N  N   . LYS A 1 69  ? 24.880  11.316  47.501  1.00 16.67  ? 69  LYS A N   1 
ATOM   533  C  CA  . LYS A 1 69  ? 24.165  10.257  48.188  1.00 16.53  ? 69  LYS A CA  1 
ATOM   534  C  C   . LYS A 1 69  ? 24.756  10.059  49.584  1.00 15.84  ? 69  LYS A C   1 
ATOM   535  O  O   . LYS A 1 69  ? 25.985  9.928   49.721  1.00 14.06  ? 69  LYS A O   1 
ATOM   536  C  CB  . LYS A 1 69  ? 24.280  8.943   47.410  1.00 16.13  ? 69  LYS A CB  1 
ATOM   537  C  CG  . LYS A 1 69  ? 23.800  7.732   48.212  1.00 15.70  ? 69  LYS A CG  1 
ATOM   538  C  CD  . LYS A 1 69  ? 23.511  6.442   47.390  1.00 15.26  ? 69  LYS A CD  1 
ATOM   539  C  CE  . LYS A 1 69  ? 23.443  5.243   48.326  1.00 15.29  ? 69  LYS A CE  1 
ATOM   540  N  NZ  . LYS A 1 69  ? 22.585  4.117   47.864  1.00 15.80  ? 69  LYS A NZ  1 
ATOM   541  N  N   . ASN A 1 70  ? 23.847  9.997   50.565  1.00 13.81  ? 70  ASN A N   1 
ATOM   542  C  CA  . ASN A 1 70  ? 24.121  9.682   51.965  1.00 15.77  ? 70  ASN A CA  1 
ATOM   543  C  C   . ASN A 1 70  ? 23.612  8.264   52.260  1.00 17.12  ? 70  ASN A C   1 
ATOM   544  O  O   . ASN A 1 70  ? 22.619  7.827   51.659  1.00 16.93  ? 70  ASN A O   1 
ATOM   545  C  CB  . ASN A 1 70  ? 23.440  10.716  52.891  1.00 16.57  ? 70  ASN A CB  1 
ATOM   546  C  CG  . ASN A 1 70  ? 23.763  10.547  54.366  1.00 16.91  ? 70  ASN A CG  1 
ATOM   547  O  OD1 . ASN A 1 70  ? 24.923  10.496  54.745  1.00 16.84  ? 70  ASN A OD1 1 
ATOM   548  N  ND2 . ASN A 1 70  ? 22.765  10.448  55.221  1.00 16.58  ? 70  ASN A ND2 1 
ATOM   549  N  N   . LEU A 1 71  ? 24.262  7.547   53.185  1.00 20.29  ? 71  LEU A N   1 
ATOM   550  C  CA  . LEU A 1 71  ? 23.665  6.321   53.733  1.00 21.99  ? 71  LEU A CA  1 
ATOM   551  C  C   . LEU A 1 71  ? 22.819  6.679   54.964  1.00 24.71  ? 71  LEU A C   1 
ATOM   552  O  O   . LEU A 1 71  ? 23.347  7.117   55.980  1.00 25.16  ? 71  LEU A O   1 
ATOM   553  C  CB  . LEU A 1 71  ? 24.761  5.311   54.097  1.00 22.35  ? 71  LEU A CB  1 
ATOM   554  C  CG  . LEU A 1 71  ? 25.835  5.049   53.039  1.00 22.15  ? 71  LEU A CG  1 
ATOM   555  C  CD1 . LEU A 1 71  ? 26.798  3.962   53.492  1.00 25.24  ? 71  LEU A CD1 1 
ATOM   556  C  CD2 . LEU A 1 71  ? 25.232  4.655   51.691  1.00 23.18  ? 71  LEU A CD2 1 
ATOM   557  N  N   . SER A 1 72  ? 21.499  6.490   54.866  1.00 30.51  ? 72  SER A N   1 
ATOM   558  C  CA  . SER A 1 72  ? 20.624  6.533   56.022  1.00 29.96  ? 72  SER A CA  1 
ATOM   559  C  C   . SER A 1 72  ? 21.105  5.523   57.065  1.00 35.88  ? 72  SER A C   1 
ATOM   560  O  O   . SER A 1 72  ? 21.906  4.611   56.776  1.00 26.44  ? 72  SER A O   1 
ATOM   561  C  CB  . SER A 1 72  ? 19.228  6.222   55.626  1.00 29.93  ? 72  SER A CB  1 
ATOM   562  O  OG  . SER A 1 72  ? 19.120  4.845   55.318  1.00 30.50  ? 72  SER A OG  1 
ATOM   563  N  N   . GLN A 1 73  ? 20.589  5.687   58.291  1.00 36.82  ? 73  GLN A N   1 
ATOM   564  C  CA  . GLN A 1 73  ? 20.959  4.807   59.391  1.00 37.67  ? 73  GLN A CA  1 
ATOM   565  C  C   . GLN A 1 73  ? 20.662  3.361   58.992  1.00 29.63  ? 73  GLN A C   1 
ATOM   566  O  O   . GLN A 1 73  ? 21.449  2.459   59.260  1.00 30.73  ? 73  GLN A O   1 
ATOM   567  C  CB  . GLN A 1 73  ? 20.237  5.259   60.666  1.00 47.14  ? 73  GLN A CB  1 
ATOM   568  C  CG  . GLN A 1 73  ? 20.776  4.614   61.940  1.00 53.94  ? 73  GLN A CG  1 
ATOM   569  C  CD  . GLN A 1 73  ? 22.252  4.859   62.160  1.00 57.15  ? 73  GLN A CD  1 
ATOM   570  O  OE1 . GLN A 1 73  ? 23.084  3.974   61.954  1.00 54.85  ? 73  GLN A OE1 1 
ATOM   571  N  NE2 . GLN A 1 73  ? 22.591  6.071   62.575  1.00 59.17  ? 73  GLN A NE2 1 
ATOM   572  N  N   . GLY A 1 74  ? 19.543  3.154   58.292  1.00 30.98  ? 74  GLY A N   1 
ATOM   573  C  CA  . GLY A 1 74  ? 19.190  1.847   57.756  1.00 28.24  ? 74  GLY A CA  1 
ATOM   574  C  C   . GLY A 1 74  ? 20.249  1.274   56.815  1.00 28.26  ? 74  GLY A C   1 
ATOM   575  O  O   . GLY A 1 74  ? 20.703  0.144   56.996  1.00 26.73  ? 74  GLY A O   1 
ATOM   576  N  N   . LEU A 1 75  ? 20.671  2.064   55.817  1.00 26.17  ? 75  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 75  ? 21.629  1.567   54.860  1.00 25.98  ? 75  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 75  ? 22.960  1.273   55.551  1.00 22.52  ? 75  LEU A C   1 
ATOM   579  O  O   . LEU A 1 75  ? 23.640  0.308   55.200  1.00 20.95  ? 75  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 75  ? 21.777  2.556   53.705  1.00 26.53  ? 75  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 75  ? 20.751  2.464   52.582  1.00 27.51  ? 75  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 75  ? 21.259  3.244   51.373  1.00 28.68  ? 75  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 75  ? 20.460  1.013   52.189  1.00 28.27  ? 75  LEU A CD2 1 
ATOM   584  N  N   . LYS A 1 76  ? 23.315  2.079   56.550  1.00 23.71  ? 76  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 76  ? 24.561  1.867   57.278  1.00 27.04  ? 76  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 76  ? 24.543  0.516   57.977  1.00 25.83  ? 76  LYS A C   1 
ATOM   587  O  O   . LYS A 1 76  ? 25.572  -0.156  58.042  1.00 25.04  ? 76  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 76  ? 24.844  2.962   58.313  1.00 31.08  ? 76  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 76  ? 25.196  4.307   57.695  1.00 35.01  ? 76  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 76  ? 25.371  5.421   58.686  1.00 39.01  ? 76  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 76  ? 25.941  6.657   58.024  1.00 42.93  ? 76  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 76  ? 27.088  7.184   58.795  1.00 44.86  ? 76  LYS A NZ  1 
ATOM   593  N  N   . PHE A 1 77  ? 23.362  0.108   58.452  1.00 26.60  ? 77  PHE A N   1 
ATOM   594  C  CA  . PHE A 1 77  ? 23.214  -1.191  59.086  1.00 28.11  ? 77  PHE A CA  1 
ATOM   595  C  C   . PHE A 1 77  ? 23.254  -2.308  58.045  1.00 28.54  ? 77  PHE A C   1 
ATOM   596  O  O   . PHE A 1 77  ? 23.883  -3.342  58.285  1.00 29.44  ? 77  PHE A O   1 
ATOM   597  C  CB  . PHE A 1 77  ? 21.961  -1.186  59.968  1.00 36.40  ? 77  PHE A CB  1 
ATOM   598  C  CG  . PHE A 1 77  ? 22.108  -0.436  61.270  1.00 35.83  ? 77  PHE A CG  1 
ATOM   599  C  CD1 . PHE A 1 77  ? 23.357  -0.180  61.814  1.00 38.84  ? 77  PHE A CD1 1 
ATOM   600  C  CD2 . PHE A 1 77  ? 20.991  0.035   61.940  1.00 36.89  ? 77  PHE A CD2 1 
ATOM   601  C  CE1 . PHE A 1 77  ? 23.486  0.514   63.007  1.00 40.78  ? 77  PHE A CE1 1 
ATOM   602  C  CE2 . PHE A 1 77  ? 21.122  0.732   63.131  1.00 38.98  ? 77  PHE A CE2 1 
ATOM   603  C  CZ  . PHE A 1 77  ? 22.366  0.969   63.663  1.00 38.71  ? 77  PHE A CZ  1 
ATOM   604  N  N   . VAL A 1 78  ? 22.643  -2.085  56.867  1.00 27.85  ? 78  VAL A N   1 
ATOM   605  C  CA  . VAL A 1 78  ? 22.680  -3.053  55.781  1.00 25.22  ? 78  VAL A CA  1 
ATOM   606  C  C   . VAL A 1 78  ? 24.128  -3.343  55.384  1.00 25.51  ? 78  VAL A C   1 
ATOM   607  O  O   . VAL A 1 78  ? 24.462  -4.472  55.028  1.00 25.50  ? 78  VAL A O   1 
ATOM   608  C  CB  . VAL A 1 78  ? 21.837  -2.579  54.584  1.00 24.54  ? 78  VAL A CB  1 
ATOM   609  C  CG1 . VAL A 1 78  ? 22.105  -3.358  53.312  1.00 24.15  ? 78  VAL A CG1 1 
ATOM   610  C  CG2 . VAL A 1 78  ? 20.357  -2.620  54.912  1.00 28.80  ? 78  VAL A CG2 1 
ATOM   611  N  N   . ARG A 1 79  ? 24.982  -2.323  55.425  1.00 26.42  ? 79  ARG A N   1 
ATOM   612  C  CA  . ARG A 1 79  ? 26.389  -2.448  55.072  1.00 26.39  ? 79  ARG A CA  1 
ATOM   613  C  C   . ARG A 1 79  ? 27.102  -3.501  55.918  1.00 29.18  ? 79  ARG A C   1 
ATOM   614  O  O   . ARG A 1 79  ? 28.149  -3.992  55.518  1.00 30.99  ? 79  ARG A O   1 
ATOM   615  C  CB  . ARG A 1 79  ? 27.028  -1.069  55.225  1.00 28.17  ? 79  ARG A CB  1 
ATOM   616  C  CG  . ARG A 1 79  ? 28.485  -0.963  54.819  1.00 27.76  ? 79  ARG A CG  1 
ATOM   617  C  CD  . ARG A 1 79  ? 28.713  0.532   54.602  1.00 27.84  ? 79  ARG A CD  1 
ATOM   618  N  NE  . ARG A 1 79  ? 30.103  0.933   54.738  1.00 27.71  ? 79  ARG A NE  1 
ATOM   619  C  CZ  . ARG A 1 79  ? 30.917  1.226   53.734  1.00 26.46  ? 79  ARG A CZ  1 
ATOM   620  N  NH1 . ARG A 1 79  ? 30.450  1.476   52.522  1.00 24.27  ? 79  ARG A NH1 1 
ATOM   621  N  NH2 . ARG A 1 79  ? 32.208  1.331   53.967  1.00 26.02  ? 79  ARG A NH2 1 
ATOM   622  N  N   . ASP A 1 80  ? 26.538  -3.861  57.079  1.00 33.05  ? 80  ASP A N   1 
ATOM   623  C  CA  . ASP A 1 80  ? 27.034  -4.984  57.866  1.00 34.93  ? 80  ASP A CA  1 
ATOM   624  C  C   . ASP A 1 80  ? 27.088  -6.281  57.055  1.00 34.20  ? 80  ASP A C   1 
ATOM   625  O  O   . ASP A 1 80  ? 27.876  -7.158  57.365  1.00 31.88  ? 80  ASP A O   1 
ATOM   626  C  CB  . ASP A 1 80  ? 26.186  -5.233  59.118  1.00 37.44  ? 80  ASP A CB  1 
ATOM   627  C  CG  . ASP A 1 80  ? 26.511  -4.348  60.312  1.00 43.93  ? 80  ASP A CG  1 
ATOM   628  O  OD1 . ASP A 1 80  ? 27.526  -3.604  60.261  1.00 40.05  ? 80  ASP A OD1 1 
ATOM   629  O  OD2 . ASP A 1 80  ? 25.743  -4.416  61.303  1.00 50.39  ? 80  ASP A OD2 1 
ATOM   630  N  N   . PHE A 1 81  ? 26.248  -6.462  56.035  1.00 32.55  ? 81  PHE A N   1 
ATOM   631  C  CA  . PHE A 1 81  ? 26.377  -7.670  55.225  1.00 29.60  ? 81  PHE A CA  1 
ATOM   632  C  C   . PHE A 1 81  ? 26.510  -7.364  53.731  1.00 25.44  ? 81  PHE A C   1 
ATOM   633  O  O   . PHE A 1 81  ? 26.970  -8.212  52.983  1.00 25.75  ? 81  PHE A O   1 
ATOM   634  C  CB  . PHE A 1 81  ? 25.228  -8.630  55.542  1.00 29.89  ? 81  PHE A CB  1 
ATOM   635  C  CG  . PHE A 1 81  ? 23.844  -8.096  55.272  1.00 29.06  ? 81  PHE A CG  1 
ATOM   636  C  CD1 . PHE A 1 81  ? 23.296  -8.156  53.997  1.00 29.09  ? 81  PHE A CD1 1 
ATOM   637  C  CD2 . PHE A 1 81  ? 23.087  -7.544  56.292  1.00 30.35  ? 81  PHE A CD2 1 
ATOM   638  C  CE1 . PHE A 1 81  ? 22.016  -7.682  53.753  1.00 28.81  ? 81  PHE A CE1 1 
ATOM   639  C  CE2 . PHE A 1 81  ? 21.805  -7.068  56.044  1.00 29.23  ? 81  PHE A CE2 1 
ATOM   640  C  CZ  . PHE A 1 81  ? 21.274  -7.137  54.779  1.00 30.95  ? 81  PHE A CZ  1 
ATOM   641  N  N   . ALA A 1 82  ? 26.142  -6.162  53.284  1.00 21.41  ? 82  ALA A N   1 
ATOM   642  C  CA  . ALA A 1 82  ? 26.299  -5.802  51.880  1.00 24.22  ? 82  ALA A CA  1 
ATOM   643  C  C   . ALA A 1 82  ? 27.574  -4.969  51.661  1.00 23.22  ? 82  ALA A C   1 
ATOM   644  O  O   . ALA A 1 82  ? 27.907  -4.639  50.530  1.00 23.75  ? 82  ALA A O   1 
ATOM   645  C  CB  . ALA A 1 82  ? 25.057  -5.078  51.406  1.00 25.43  ? 82  ALA A CB  1 
ATOM   646  N  N   . GLY A 1 83  ? 28.285  -4.624  52.738  1.00 22.11  ? 83  GLY A N   1 
ATOM   647  C  CA  . GLY A 1 83  ? 29.609  -4.019  52.642  1.00 21.14  ? 83  GLY A CA  1 
ATOM   648  C  C   . GLY A 1 83  ? 29.630  -2.773  51.750  1.00 20.99  ? 83  GLY A C   1 
ATOM   649  O  O   . GLY A 1 83  ? 28.765  -1.885  51.808  1.00 23.59  ? 83  GLY A O   1 
ATOM   650  N  N   . ASP A 1 84  ? 30.624  -2.749  50.872  1.00 20.57  ? 84  ASP A N   1 
ATOM   651  C  CA  . ASP A 1 84  ? 30.759  -1.705  49.887  1.00 20.28  ? 84  ASP A CA  1 
ATOM   652  C  C   . ASP A 1 84  ? 30.264  -2.222  48.536  1.00 18.30  ? 84  ASP A C   1 
ATOM   653  O  O   . ASP A 1 84  ? 30.793  -1.823  47.485  1.00 17.33  ? 84  ASP A O   1 
ATOM   654  C  CB  . ASP A 1 84  ? 32.182  -1.140  49.930  1.00 23.31  ? 84  ASP A CB  1 
ATOM   655  C  CG  . ASP A 1 84  ? 33.289  -2.108  49.533  1.00 24.03  ? 84  ASP A CG  1 
ATOM   656  O  OD1 . ASP A 1 84  ? 33.010  -3.337  49.417  1.00 22.60  ? 84  ASP A OD1 1 
ATOM   657  O  OD2 . ASP A 1 84  ? 34.424  -1.619  49.314  1.00 22.01  ? 84  ASP A OD2 1 
ATOM   658  N  N   . GLY A 1 85  ? 29.202  -3.054  48.563  1.00 16.83  ? 85  GLY A N   1 
ATOM   659  C  CA  . GLY A 1 85  ? 28.353  -3.257  47.403  1.00 17.27  ? 85  GLY A CA  1 
ATOM   660  C  C   . GLY A 1 85  ? 27.843  -1.912  46.859  1.00 18.31  ? 85  GLY A C   1 
ATOM   661  O  O   . GLY A 1 85  ? 27.981  -0.881  47.534  1.00 16.50  ? 85  GLY A O   1 
ATOM   662  N  N   . LEU A 1 86  ? 27.284  -1.922  45.637  1.00 17.17  ? 86  LEU A N   1 
ATOM   663  C  CA  . LEU A 1 86  ? 26.940  -0.679  44.941  1.00 17.49  ? 86  LEU A CA  1 
ATOM   664  C  C   . LEU A 1 86  ? 25.911  0.122   45.745  1.00 16.97  ? 86  LEU A C   1 
ATOM   665  O  O   . LEU A 1 86  ? 25.932  1.352   45.713  1.00 17.38  ? 86  LEU A O   1 
ATOM   666  C  CB  . LEU A 1 86  ? 26.350  -0.946  43.552  1.00 16.63  ? 86  LEU A CB  1 
ATOM   667  C  CG  . LEU A 1 86  ? 27.307  -1.251  42.402  1.00 18.32  ? 86  LEU A CG  1 
ATOM   668  C  CD1 . LEU A 1 86  ? 26.517  -1.581  41.137  1.00 18.11  ? 86  LEU A CD1 1 
ATOM   669  C  CD2 . LEU A 1 86  ? 28.258  -0.075  42.134  1.00 20.25  ? 86  LEU A CD2 1 
ATOM   670  N  N   . VAL A 1 87  ? 24.993  -0.557  46.435  1.00 17.08  ? 87  VAL A N   1 
ATOM   671  C  CA  . VAL A 1 87  ? 23.933  0.159   47.121  1.00 18.90  ? 87  VAL A CA  1 
ATOM   672  C  C   . VAL A 1 87  ? 24.457  0.812   48.399  1.00 16.11  ? 87  VAL A C   1 
ATOM   673  O  O   . VAL A 1 87  ? 23.915  1.823   48.821  1.00 16.18  ? 87  VAL A O   1 
ATOM   674  C  CB  . VAL A 1 87  ? 22.715  -0.735  47.438  1.00 22.52  ? 87  VAL A CB  1 
ATOM   675  C  CG1 . VAL A 1 87  ? 21.714  -0.001  48.358  1.00 25.45  ? 87  VAL A CG1 1 
ATOM   676  C  CG2 . VAL A 1 87  ? 22.025  -1.201  46.168  1.00 23.86  ? 87  VAL A CG2 1 
ATOM   677  N  N   . THR A 1 88  ? 25.460  0.213   49.039  1.00 15.19  ? 88  THR A N   1 
ATOM   678  C  CA  . THR A 1 88  ? 25.809  0.591   50.405  1.00 16.25  ? 88  THR A CA  1 
ATOM   679  C  C   . THR A 1 88  ? 27.180  1.245   50.393  1.00 15.31  ? 88  THR A C   1 
ATOM   680  O  O   . THR A 1 88  ? 27.818  1.393   51.432  1.00 16.94  ? 88  THR A O   1 
ATOM   681  C  CB  . THR A 1 88  ? 25.728  -0.610  51.364  1.00 17.10  ? 88  THR A CB  1 
ATOM   682  O  OG1 . THR A 1 88  ? 26.420  -1.728  50.801  1.00 17.35  ? 88  THR A OG1 1 
ATOM   683  C  CG2 . THR A 1 88  ? 24.297  -0.991  51.663  1.00 19.31  ? 88  THR A CG2 1 
ATOM   684  N  N   . SER A 1 89  ? 27.641  1.644   49.209  1.00 15.89  ? 89  SER A N   1 
ATOM   685  C  CA  . SER A 1 89  ? 28.913  2.343   49.132  1.00 16.85  ? 89  SER A CA  1 
ATOM   686  C  C   . SER A 1 89  ? 28.682  3.854   49.023  1.00 15.27  ? 89  SER A C   1 
ATOM   687  O  O   . SER A 1 89  ? 27.651  4.351   48.555  1.00 13.63  ? 89  SER A O   1 
ATOM   688  C  CB  . SER A 1 89  ? 29.757  1.822   48.018  1.00 17.70  ? 89  SER A CB  1 
ATOM   689  O  OG  . SER A 1 89  ? 29.027  1.881   46.820  1.00 21.76  ? 89  SER A OG  1 
ATOM   690  N  N   . TRP A 1 90  ? 29.663  4.589   49.543  1.00 15.28  ? 90  TRP A N   1 
ATOM   691  C  CA  . TRP A 1 90  ? 29.755  6.021   49.334  1.00 15.31  ? 90  TRP A CA  1 
ATOM   692  C  C   . TRP A 1 90  ? 30.327  6.285   47.939  1.00 14.89  ? 90  TRP A C   1 
ATOM   693  O  O   . TRP A 1 90  ? 31.167  5.547   47.442  1.00 15.37  ? 90  TRP A O   1 
ATOM   694  C  CB  . TRP A 1 90  ? 30.651  6.671   50.391  1.00 14.76  ? 90  TRP A CB  1 
ATOM   695  C  CG  . TRP A 1 90  ? 30.182  6.430   51.800  1.00 16.09  ? 90  TRP A CG  1 
ATOM   696  C  CD1 . TRP A 1 90  ? 30.596  5.426   52.626  1.00 16.71  ? 90  TRP A CD1 1 
ATOM   697  C  CD2 . TRP A 1 90  ? 29.256  7.223   52.560  1.00 14.92  ? 90  TRP A CD2 1 
ATOM   698  N  NE1 . TRP A 1 90  ? 29.969  5.520   53.838  1.00 17.33  ? 90  TRP A NE1 1 
ATOM   699  C  CE2 . TRP A 1 90  ? 29.158  6.620   53.831  1.00 16.31  ? 90  TRP A CE2 1 
ATOM   700  C  CE3 . TRP A 1 90  ? 28.513  8.377   52.297  1.00 16.04  ? 90  TRP A CE3 1 
ATOM   701  C  CZ2 . TRP A 1 90  ? 28.339  7.131   54.829  1.00 16.99  ? 90  TRP A CZ2 1 
ATOM   702  C  CZ3 . TRP A 1 90  ? 27.738  8.910   53.301  1.00 17.21  ? 90  TRP A CZ3 1 
ATOM   703  C  CH2 . TRP A 1 90  ? 27.647  8.291   54.538  1.00 17.07  ? 90  TRP A CH2 1 
ATOM   704  N  N   . THR A 1 91  ? 29.898  7.379   47.323  1.00 15.06  ? 91  THR A N   1 
ATOM   705  C  CA  . THR A 1 91  ? 30.294  7.700   45.974  1.00 15.45  ? 91  THR A CA  1 
ATOM   706  C  C   . THR A 1 91  ? 31.808  7.893   45.868  1.00 16.71  ? 91  THR A C   1 
ATOM   707  O  O   . THR A 1 91  ? 32.363  7.640   44.806  1.00 15.52  ? 91  THR A O   1 
ATOM   708  C  CB  . THR A 1 91  ? 29.544  8.959   45.537  1.00 15.51  ? 91  THR A CB  1 
ATOM   709  O  OG1 . THR A 1 91  ? 28.161  8.734   45.794  1.00 15.49  ? 91  THR A OG1 1 
ATOM   710  C  CG2 . THR A 1 91  ? 29.775  9.293   44.093  1.00 16.71  ? 91  THR A CG2 1 
ATOM   711  N  N   . HIS A 1 92  ? 32.442  8.382   46.950  1.00 15.47  ? 92  HIS A N   1 
ATOM   712  C  CA  . HIS A 1 92  ? 33.862  8.671   46.963  1.00 15.91  ? 92  HIS A CA  1 
ATOM   713  C  C   . HIS A 1 92  ? 34.694  7.428   47.276  1.00 18.65  ? 92  HIS A C   1 
ATOM   714  O  O   . HIS A 1 92  ? 35.911  7.491   47.150  1.00 16.77  ? 92  HIS A O   1 
ATOM   715  C  CB  . HIS A 1 92  ? 34.134  9.833   47.921  1.00 17.60  ? 92  HIS A CB  1 
ATOM   716  C  CG  . HIS A 1 92  ? 33.548  9.606   49.284  1.00 16.21  ? 92  HIS A CG  1 
ATOM   717  N  ND1 . HIS A 1 92  ? 34.118  8.739   50.177  1.00 16.28  ? 92  HIS A ND1 1 
ATOM   718  C  CD2 . HIS A 1 92  ? 32.498  10.161  49.895  1.00 15.92  ? 92  HIS A CD2 1 
ATOM   719  C  CE1 . HIS A 1 92  ? 33.395  8.749   51.289  1.00 16.52  ? 92  HIS A CE1 1 
ATOM   720  N  NE2 . HIS A 1 92  ? 32.425  9.624   51.148  1.00 17.22  ? 92  HIS A NE2 1 
ATOM   721  N  N   . GLU A 1 93  ? 34.076  6.277   47.624  1.00 18.48  ? 93  GLU A N   1 
ATOM   722  C  CA  . GLU A 1 93  ? 34.847  5.050   47.817  1.00 17.90  ? 93  GLU A CA  1 
ATOM   723  C  C   . GLU A 1 93  ? 35.268  4.504   46.460  1.00 17.99  ? 93  GLU A C   1 
ATOM   724  O  O   . GLU A 1 93  ? 34.473  4.424   45.536  1.00 18.97  ? 93  GLU A O   1 
ATOM   725  C  CB  . GLU A 1 93  ? 34.076  3.976   48.582  1.00 19.50  ? 93  GLU A CB  1 
ATOM   726  C  CG  . GLU A 1 93  ? 33.932  4.272   50.064  1.00 20.70  ? 93  GLU A CG  1 
ATOM   727  C  CD  . GLU A 1 93  ? 33.113  3.203   50.762  1.00 23.34  ? 93  GLU A CD  1 
ATOM   728  O  OE1 . GLU A 1 93  ? 31.912  3.101   50.480  1.00 22.01  ? 93  GLU A OE1 1 
ATOM   729  O  OE2 . GLU A 1 93  ? 33.703  2.420   51.522  1.00 26.89  ? 93  GLU A OE2 1 
ATOM   730  N  N   . LYS A 1 94  ? 36.529  4.140   46.335  1.00 17.57  ? 94  LYS A N   1 
ATOM   731  C  CA  . LYS A 1 94  ? 37.057  3.606   45.096  1.00 18.50  ? 94  LYS A CA  1 
ATOM   732  C  C   . LYS A 1 94  ? 36.177  2.492   44.533  1.00 16.88  ? 94  LYS A C   1 
ATOM   733  O  O   . LYS A 1 94  ? 36.011  2.417   43.318  1.00 15.74  ? 94  LYS A O   1 
ATOM   734  C  CB  . LYS A 1 94  ? 38.474  3.070   45.328  1.00 22.85  ? 94  LYS A CB  1 
ATOM   735  C  CG  . LYS A 1 94  ? 39.074  2.267   44.184  1.00 26.57  ? 94  LYS A CG  1 
ATOM   736  C  CD  . LYS A 1 94  ? 40.539  1.996   44.418  1.00 30.81  ? 94  LYS A CD  1 
ATOM   737  C  CE  . LYS A 1 94  ? 41.265  1.571   43.164  1.00 31.64  ? 94  LYS A CE  1 
ATOM   738  N  NZ  . LYS A 1 94  ? 42.511  0.860   43.539  1.00 32.56  ? 94  LYS A NZ  1 
ATOM   739  N  N   . ASN A 1 95  ? 35.624  1.643   45.397  1.00 17.17  ? 95  ASN A N   1 
ATOM   740  C  CA  . ASN A 1 95  ? 34.907  0.476   44.936  1.00 17.72  ? 95  ASN A CA  1 
ATOM   741  C  C   . ASN A 1 95  ? 33.563  0.821   44.310  1.00 19.43  ? 95  ASN A C   1 
ATOM   742  O  O   . ASN A 1 95  ? 33.083  -0.016  43.531  1.00 21.71  ? 95  ASN A O   1 
ATOM   743  C  CB  . ASN A 1 95  ? 34.743  -0.584  46.013  1.00 20.30  ? 95  ASN A CB  1 
ATOM   744  C  CG  . ASN A 1 95  ? 35.942  -1.511  46.035  1.00 23.34  ? 95  ASN A CG  1 
ATOM   745  O  OD1 . ASN A 1 95  ? 36.717  -1.539  45.085  1.00 26.86  ? 95  ASN A OD1 1 
ATOM   746  N  ND2 . ASN A 1 95  ? 36.094  -2.277  47.094  1.00 25.86  ? 95  ASN A ND2 1 
ATOM   747  N  N   . TRP A 1 96  ? 33.023  2.016   44.575  1.00 16.14  ? 96  TRP A N   1 
ATOM   748  C  CA  . TRP A 1 96  ? 31.755  2.390   43.971  1.00 16.48  ? 96  TRP A CA  1 
ATOM   749  C  C   . TRP A 1 96  ? 31.926  2.518   42.464  1.00 15.96  ? 96  TRP A C   1 
ATOM   750  O  O   . TRP A 1 96  ? 31.292  1.788   41.706  1.00 15.25  ? 96  TRP A O   1 
ATOM   751  C  CB  . TRP A 1 96  ? 31.121  3.684   44.532  1.00 17.34  ? 96  TRP A CB  1 
ATOM   752  C  CG  . TRP A 1 96  ? 29.903  3.976   43.698  1.00 16.13  ? 96  TRP A CG  1 
ATOM   753  C  CD1 . TRP A 1 96  ? 28.760  3.244   43.737  1.00 17.86  ? 96  TRP A CD1 1 
ATOM   754  C  CD2 . TRP A 1 96  ? 29.756  4.890   42.593  1.00 16.99  ? 96  TRP A CD2 1 
ATOM   755  N  NE1 . TRP A 1 96  ? 27.914  3.640   42.738  1.00 16.73  ? 96  TRP A NE1 1 
ATOM   756  C  CE2 . TRP A 1 96  ? 28.481  4.653   42.029  1.00 16.20  ? 96  TRP A CE2 1 
ATOM   757  C  CE3 . TRP A 1 96  ? 30.534  5.916   42.057  1.00 16.55  ? 96  TRP A CE3 1 
ATOM   758  C  CZ2 . TRP A 1 96  ? 27.980  5.394   40.958  1.00 16.61  ? 96  TRP A CZ2 1 
ATOM   759  C  CZ3 . TRP A 1 96  ? 30.046  6.628   40.985  1.00 16.89  ? 96  TRP A CZ3 1 
ATOM   760  C  CH2 . TRP A 1 96  ? 28.802  6.368   40.430  1.00 16.79  ? 96  TRP A CH2 1 
ATOM   761  N  N   . LYS A 1 97  ? 32.770  3.475   42.024  1.00 15.53  ? 97  LYS A N   1 
ATOM   762  C  CA  . LYS A 1 97  ? 32.859  3.802   40.620  1.00 14.96  ? 97  LYS A CA  1 
ATOM   763  C  C   . LYS A 1 97  ? 33.438  2.598   39.882  1.00 13.14  ? 97  LYS A C   1 
ATOM   764  O  O   . LYS A 1 97  ? 33.130  2.343   38.723  1.00 12.15  ? 97  LYS A O   1 
ATOM   765  C  CB  . LYS A 1 97  ? 33.691  5.085   40.434  1.00 17.97  ? 97  LYS A CB  1 
ATOM   766  C  CG  . LYS A 1 97  ? 33.790  5.609   39.007  1.00 20.56  ? 97  LYS A CG  1 
ATOM   767  C  CD  . LYS A 1 97  ? 32.455  5.910   38.378  1.00 24.13  ? 97  LYS A CD  1 
ATOM   768  C  CE  . LYS A 1 97  ? 32.514  6.506   36.992  1.00 27.07  ? 97  LYS A CE  1 
ATOM   769  N  NZ  . LYS A 1 97  ? 33.212  7.807   37.015  1.00 30.42  ? 97  LYS A NZ  1 
ATOM   770  N  N   . LYS A 1 98  ? 34.332  1.858   40.549  1.00 13.92  ? 98  LYS A N   1 
ATOM   771  C  CA  . LYS A 1 98  ? 34.885  0.669   39.950  1.00 14.20  ? 98  LYS A CA  1 
ATOM   772  C  C   . LYS A 1 98  ? 33.777  -0.330  39.601  1.00 13.80  ? 98  LYS A C   1 
ATOM   773  O  O   . LYS A 1 98  ? 33.668  -0.799  38.475  1.00 14.51  ? 98  LYS A O   1 
ATOM   774  C  CB  . LYS A 1 98  ? 35.898  0.093   40.921  1.00 17.77  ? 98  LYS A CB  1 
ATOM   775  C  CG  . LYS A 1 98  ? 36.621  -1.127  40.420  1.00 19.50  ? 98  LYS A CG  1 
ATOM   776  C  CD  . LYS A 1 98  ? 37.891  -1.273  41.214  1.00 22.13  ? 98  LYS A CD  1 
ATOM   777  C  CE  . LYS A 1 98  ? 38.185  -2.722  41.449  1.00 21.80  ? 98  LYS A CE  1 
ATOM   778  N  NZ  . LYS A 1 98  ? 39.436  -2.826  42.195  1.00 21.68  ? 98  LYS A NZ  1 
ATOM   779  N  N   . ALA A 1 99  ? 32.952  -0.662  40.572  1.00 14.70  ? 99  ALA A N   1 
ATOM   780  C  CA  . ALA A 1 99  ? 31.898  -1.636  40.347  1.00 14.81  ? 99  ALA A CA  1 
ATOM   781  C  C   . ALA A 1 99  ? 30.838  -1.092  39.384  1.00 15.32  ? 99  ALA A C   1 
ATOM   782  O  O   . ALA A 1 99  ? 30.313  -1.833  38.549  1.00 17.31  ? 99  ALA A O   1 
ATOM   783  C  CB  . ALA A 1 99  ? 31.358  -2.071  41.676  1.00 14.05  ? 99  ALA A CB  1 
ATOM   784  N  N   . HIS A 1 100 ? 30.533  0.202   39.482  1.00 15.97  ? 100 HIS A N   1 
ATOM   785  C  CA  . HIS A 1 100 ? 29.549  0.825   38.606  1.00 16.83  ? 100 HIS A CA  1 
ATOM   786  C  C   . HIS A 1 100 ? 30.012  0.731   37.154  1.00 16.02  ? 100 HIS A C   1 
ATOM   787  O  O   . HIS A 1 100 ? 29.259  0.329   36.282  1.00 16.61  ? 100 HIS A O   1 
ATOM   788  C  CB  . HIS A 1 100 ? 29.362  2.277   39.004  1.00 18.44  ? 100 HIS A CB  1 
ATOM   789  C  CG  . HIS A 1 100 ? 28.506  3.048   38.082  1.00 19.76  ? 100 HIS A CG  1 
ATOM   790  N  ND1 . HIS A 1 100 ? 29.004  3.948   37.165  1.00 24.49  ? 100 HIS A ND1 1 
ATOM   791  C  CD2 . HIS A 1 100 ? 27.195  3.038   37.948  1.00 19.86  ? 100 HIS A CD2 1 
ATOM   792  C  CE1 . HIS A 1 100 ? 27.984  4.481   36.508  1.00 25.54  ? 100 HIS A CE1 1 
ATOM   793  N  NE2 . HIS A 1 100 ? 26.873  3.923   36.967  1.00 26.38  ? 100 HIS A NE2 1 
ATOM   794  N  N   . ASN A 1 101 ? 31.292  1.043   36.903  1.00 16.67  ? 101 ASN A N   1 
ATOM   795  C  CA  . ASN A 1 101 ? 31.866  0.938   35.565  1.00 16.89  ? 101 ASN A CA  1 
ATOM   796  C  C   . ASN A 1 101 ? 31.891  -0.508  35.054  1.00 17.74  ? 101 ASN A C   1 
ATOM   797  O  O   . ASN A 1 101 ? 31.640  -0.763  33.887  1.00 20.14  ? 101 ASN A O   1 
ATOM   798  C  CB  . ASN A 1 101 ? 33.281  1.526   35.511  1.00 16.81  ? 101 ASN A CB  1 
ATOM   799  C  CG  . ASN A 1 101 ? 33.328  3.038   35.564  1.00 18.08  ? 101 ASN A CG  1 
ATOM   800  O  OD1 . ASN A 1 101 ? 32.315  3.726   35.389  1.00 15.43  ? 101 ASN A OD1 1 
ATOM   801  N  ND2 . ASN A 1 101 ? 34.519  3.572   35.821  1.00 16.90  ? 101 ASN A ND2 1 
ATOM   802  N  N   . ILE A 1 102 ? 32.214  -1.452  35.914  1.00 18.47  ? 102 ILE A N   1 
ATOM   803  C  CA  . ILE A 1 102 ? 32.305  -2.851  35.560  1.00 18.26  ? 102 ILE A CA  1 
ATOM   804  C  C   . ILE A 1 102 ? 30.928  -3.467  35.278  1.00 17.74  ? 102 ILE A C   1 
ATOM   805  O  O   . ILE A 1 102 ? 30.817  -4.260  34.348  1.00 21.47  ? 102 ILE A O   1 
ATOM   806  C  CB  . ILE A 1 102 ? 33.048  -3.602  36.673  1.00 18.82  ? 102 ILE A CB  1 
ATOM   807  C  CG1 . ILE A 1 102 ? 34.538  -3.257  36.662  1.00 19.89  ? 102 ILE A CG1 1 
ATOM   808  C  CG2 . ILE A 1 102 ? 32.812  -5.092  36.539  1.00 19.07  ? 102 ILE A CG2 1 
ATOM   809  C  CD1 . ILE A 1 102 ? 35.255  -3.650  37.934  1.00 20.28  ? 102 ILE A CD1 1 
ATOM   810  N  N   . LEU A 1 103 ? 29.882  -3.082  36.024  1.00 16.05  ? 103 LEU A N   1 
ATOM   811  C  CA  . LEU A 1 103 ? 28.609  -3.774  35.909  1.00 16.21  ? 103 LEU A CA  1 
ATOM   812  C  C   . LEU A 1 103 ? 27.577  -2.999  35.093  1.00 17.88  ? 103 LEU A C   1 
ATOM   813  O  O   . LEU A 1 103 ? 26.538  -3.586  34.755  1.00 17.55  ? 103 LEU A O   1 
ATOM   814  C  CB  . LEU A 1 103 ? 28.103  -4.068  37.318  1.00 17.17  ? 103 LEU A CB  1 
ATOM   815  C  CG  . LEU A 1 103 ? 29.045  -4.944  38.154  1.00 17.90  ? 103 LEU A CG  1 
ATOM   816  C  CD1 . LEU A 1 103 ? 28.724  -4.907  39.633  1.00 17.31  ? 103 LEU A CD1 1 
ATOM   817  C  CD2 . LEU A 1 103 ? 29.051  -6.380  37.657  1.00 20.17  ? 103 LEU A CD2 1 
ATOM   818  N  N   . LEU A 1 104 ? 27.837  -1.717  34.786  1.00 16.57  ? 104 LEU A N   1 
ATOM   819  C  CA  . LEU A 1 104 ? 26.874  -0.919  34.043  1.00 20.87  ? 104 LEU A CA  1 
ATOM   820  C  C   . LEU A 1 104 ? 26.590  -1.571  32.689  1.00 21.80  ? 104 LEU A C   1 
ATOM   821  O  O   . LEU A 1 104 ? 25.427  -1.663  32.304  1.00 20.61  ? 104 LEU A O   1 
ATOM   822  C  CB  . LEU A 1 104 ? 27.324  0.538   33.868  1.00 22.86  ? 104 LEU A CB  1 
ATOM   823  C  CG  . LEU A 1 104 ? 26.323  1.398   33.100  1.00 23.54  ? 104 LEU A CG  1 
ATOM   824  C  CD1 . LEU A 1 104 ? 25.049  1.597   33.900  1.00 26.56  ? 104 LEU A CD1 1 
ATOM   825  C  CD2 . LEU A 1 104 ? 26.931  2.712   32.718  1.00 25.34  ? 104 LEU A CD2 1 
ATOM   826  N  N   . PRO A 1 105 ? 27.595  -2.109  31.963  1.00 22.43  ? 105 PRO A N   1 
ATOM   827  C  CA  . PRO A 1 105 ? 27.331  -2.835  30.712  1.00 22.94  ? 105 PRO A CA  1 
ATOM   828  C  C   . PRO A 1 105 ? 26.444  -4.075  30.847  1.00 23.06  ? 105 PRO A C   1 
ATOM   829  O  O   . PRO A 1 105 ? 25.932  -4.554  29.841  1.00 27.41  ? 105 PRO A O   1 
ATOM   830  C  CB  . PRO A 1 105 ? 28.726  -3.248  30.213  1.00 23.20  ? 105 PRO A CB  1 
ATOM   831  C  CG  . PRO A 1 105 ? 29.665  -2.264  30.903  1.00 22.91  ? 105 PRO A CG  1 
ATOM   832  C  CD  . PRO A 1 105 ? 29.030  -2.010  32.254  1.00 22.18  ? 105 PRO A CD  1 
ATOM   833  N  N   . SER A 1 106 ? 26.251  -4.593  32.070  1.00 20.63  ? 106 SER A N   1 
ATOM   834  C  CA  . SER A 1 106 ? 25.413  -5.762  32.310  1.00 23.91  ? 106 SER A CA  1 
ATOM   835  C  C   . SER A 1 106 ? 23.937  -5.364  32.253  1.00 23.58  ? 106 SER A C   1 
ATOM   836  O  O   . SER A 1 106 ? 23.071  -6.205  32.444  1.00 25.82  ? 106 SER A O   1 
ATOM   837  C  CB  . SER A 1 106 ? 25.704  -6.424  33.657  1.00 23.31  ? 106 SER A CB  1 
ATOM   838  O  OG  . SER A 1 106 ? 26.909  -7.142  33.609  1.00 28.10  ? 106 SER A OG  1 
ATOM   839  N  N   . PHE A 1 107 ? 23.671  -4.073  32.056  1.00 25.12  ? 107 PHE A N   1 
ATOM   840  C  CA  . PHE A 1 107 ? 22.311  -3.550  32.010  1.00 25.64  ? 107 PHE A CA  1 
ATOM   841  C  C   . PHE A 1 107 ? 22.060  -2.887  30.649  1.00 26.59  ? 107 PHE A C   1 
ATOM   842  O  O   . PHE A 1 107 ? 21.083  -2.176  30.464  1.00 34.16  ? 107 PHE A O   1 
ATOM   843  C  CB  . PHE A 1 107 ? 22.117  -2.716  33.273  1.00 23.18  ? 107 PHE A CB  1 
ATOM   844  C  CG  . PHE A 1 107 ? 22.153  -3.566  34.515  1.00 25.14  ? 107 PHE A CG  1 
ATOM   845  C  CD1 . PHE A 1 107 ? 21.051  -4.334  34.881  1.00 23.24  ? 107 PHE A CD1 1 
ATOM   846  C  CD2 . PHE A 1 107 ? 23.338  -3.743  35.225  1.00 23.15  ? 107 PHE A CD2 1 
ATOM   847  C  CE1 . PHE A 1 107 ? 21.108  -5.182  35.977  1.00 23.22  ? 107 PHE A CE1 1 
ATOM   848  C  CE2 . PHE A 1 107 ? 23.393  -4.581  36.324  1.00 21.48  ? 107 PHE A CE2 1 
ATOM   849  C  CZ  . PHE A 1 107 ? 22.272  -5.297  36.699  1.00 25.56  ? 107 PHE A CZ  1 
ATOM   850  N  N   . SER A 1 108 ? 22.919  -3.173  29.664  1.00 30.60  ? 108 SER A N   1 
ATOM   851  C  CA  . SER A 1 108 ? 22.751  -2.635  28.318  1.00 32.68  ? 108 SER A CA  1 
ATOM   852  C  C   . SER A 1 108 ? 21.624  -3.391  27.613  1.00 44.16  ? 108 SER A C   1 
ATOM   853  O  O   . SER A 1 108 ? 21.440  -4.596  27.824  1.00 37.10  ? 108 SER A O   1 
ATOM   854  C  CB  . SER A 1 108 ? 24.031  -2.710  27.515  1.00 32.49  ? 108 SER A CB  1 
ATOM   855  O  OG  . SER A 1 108 ? 24.407  -4.057  27.212  1.00 31.05  ? 108 SER A OG  1 
ATOM   856  N  N   . GLN A 1 109 ? 20.889  -2.686  26.739  1.00 48.39  ? 109 GLN A N   1 
ATOM   857  C  CA  . GLN A 1 109 ? 19.810  -3.325  26.011  1.00 46.34  ? 109 GLN A CA  1 
ATOM   858  C  C   . GLN A 1 109 ? 20.369  -4.608  25.391  1.00 41.30  ? 109 GLN A C   1 
ATOM   859  O  O   . GLN A 1 109 ? 19.661  -5.609  25.282  1.00 36.05  ? 109 GLN A O   1 
ATOM   860  C  CB  . GLN A 1 109 ? 19.176  -2.318  25.043  1.00 56.75  ? 109 GLN A CB  1 
ATOM   861  C  CG  . GLN A 1 109 ? 20.134  -1.748  24.003  1.00 60.65  ? 109 GLN A CG  1 
ATOM   862  C  CD  . GLN A 1 109 ? 19.935  -2.342  22.629  1.00 65.62  ? 109 GLN A CD  1 
ATOM   863  O  OE1 . GLN A 1 109 ? 18.901  -2.142  21.995  1.00 67.56  ? 109 GLN A OE1 1 
ATOM   864  N  NE2 . GLN A 1 109 ? 20.932  -3.065  22.141  1.00 71.76  ? 109 GLN A NE2 1 
ATOM   865  N  N   . GLN A 1 110 ? 21.662  -4.609  25.045  1.00 35.30  ? 110 GLN A N   1 
ATOM   866  C  CA  . GLN A 1 110 ? 22.292  -5.809  24.526  1.00 37.21  ? 110 GLN A CA  1 
ATOM   867  C  C   . GLN A 1 110 ? 22.226  -6.925  25.564  1.00 39.97  ? 110 GLN A C   1 
ATOM   868  O  O   . GLN A 1 110 ? 21.946  -8.078  25.221  1.00 34.95  ? 110 GLN A O   1 
ATOM   869  C  CB  . GLN A 1 110 ? 23.751  -5.593  24.125  1.00 41.76  ? 110 GLN A CB  1 
ATOM   870  C  CG  . GLN A 1 110 ? 24.248  -6.689  23.195  1.00 45.91  ? 110 GLN A CG  1 
ATOM   871  C  CD  . GLN A 1 110 ? 23.204  -7.018  22.146  1.00 53.83  ? 110 GLN A CD  1 
ATOM   872  O  OE1 . GLN A 1 110 ? 22.867  -6.186  21.306  1.00 56.44  ? 110 GLN A OE1 1 
ATOM   873  N  NE2 . GLN A 1 110 ? 22.629  -8.213  22.214  1.00 52.95  ? 110 GLN A NE2 1 
ATOM   874  N  N   . ALA A 1 111 ? 22.503  -6.563  26.827  1.00 38.13  ? 111 ALA A N   1 
ATOM   875  C  CA  . ALA A 1 111 ? 22.415  -7.489  27.943  1.00 32.87  ? 111 ALA A CA  1 
ATOM   876  C  C   . ALA A 1 111 ? 20.963  -7.875  28.195  1.00 26.94  ? 111 ALA A C   1 
ATOM   877  O  O   . ALA A 1 111 ? 20.680  -9.026  28.514  1.00 23.93  ? 111 ALA A O   1 
ATOM   878  C  CB  . ALA A 1 111 ? 23.033  -6.885  29.179  1.00 33.18  ? 111 ALA A CB  1 
ATOM   879  N  N   . MET A 1 112 ? 20.058  -6.897  28.112  1.00 26.27  ? 112 MET A N   1 
ATOM   880  C  CA  . MET A 1 112 ? 18.638  -7.160  28.312  1.00 25.88  ? 112 MET A CA  1 
ATOM   881  C  C   . MET A 1 112 ? 18.170  -8.231  27.321  1.00 22.57  ? 112 MET A C   1 
ATOM   882  O  O   . MET A 1 112 ? 17.489  -9.168  27.704  1.00 20.34  ? 112 MET A O   1 
ATOM   883  C  CB  . MET A 1 112 ? 17.835  -5.870  28.128  1.00 30.50  ? 112 MET A CB  1 
ATOM   884  C  CG  . MET A 1 112 ? 17.059  -5.393  29.348  1.00 34.40  ? 112 MET A CG  1 
ATOM   885  S  SD  . MET A 1 112 ? 17.757  -5.729  30.985  1.00 32.06  ? 112 MET A SD  1 
ATOM   886  C  CE  . MET A 1 112 ? 18.979  -4.438  31.197  1.00 37.07  ? 112 MET A CE  1 
ATOM   887  N  N   . LYS A 1 113 ? 18.583  -8.103  26.056  1.00 20.03  ? 113 LYS A N   1 
ATOM   888  C  CA  . LYS A 1 113 ? 18.251  -9.069  25.026  1.00 24.50  ? 113 LYS A CA  1 
ATOM   889  C  C   . LYS A 1 113 ? 18.664  -10.474 25.452  1.00 22.99  ? 113 LYS A C   1 
ATOM   890  O  O   . LYS A 1 113 ? 17.912  -11.396 25.193  1.00 23.90  ? 113 LYS A O   1 
ATOM   891  C  CB  . LYS A 1 113 ? 18.863  -8.701  23.673  1.00 23.94  ? 113 LYS A CB  1 
ATOM   892  C  CG  . LYS A 1 113 ? 18.117  -7.570  22.995  1.00 29.30  ? 113 LYS A CG  1 
ATOM   893  C  CD  . LYS A 1 113 ? 18.859  -6.830  21.901  1.00 31.45  ? 113 LYS A CD  1 
ATOM   894  C  CE  . LYS A 1 113 ? 18.078  -5.593  21.510  1.00 34.87  ? 113 LYS A CE  1 
ATOM   895  N  NZ  . LYS A 1 113 ? 18.601  -4.975  20.275  1.00 38.09  ? 113 LYS A NZ  1 
ATOM   896  N  N   . GLY A 1 114 ? 19.824  -10.602 26.118  1.00 21.48  ? 114 GLY A N   1 
ATOM   897  C  CA  . GLY A 1 114 ? 20.351  -11.878 26.548  1.00 20.89  ? 114 GLY A CA  1 
ATOM   898  C  C   . GLY A 1 114 ? 19.675  -12.410 27.810  1.00 19.80  ? 114 GLY A C   1 
ATOM   899  O  O   . GLY A 1 114 ? 19.641  -13.608 28.011  1.00 24.31  ? 114 GLY A O   1 
ATOM   900  N  N   . TYR A 1 115 ? 19.143  -11.543 28.663  1.00 18.47  ? 115 TYR A N   1 
ATOM   901  C  CA  . TYR A 1 115 ? 18.409  -11.995 29.839  1.00 18.49  ? 115 TYR A CA  1 
ATOM   902  C  C   . TYR A 1 115 ? 17.002  -12.490 29.499  1.00 17.95  ? 115 TYR A C   1 
ATOM   903  O  O   . TYR A 1 115 ? 16.382  -13.185 30.306  1.00 15.50  ? 115 TYR A O   1 
ATOM   904  C  CB  . TYR A 1 115 ? 18.256  -10.867 30.845  1.00 18.82  ? 115 TYR A CB  1 
ATOM   905  C  CG  . TYR A 1 115 ? 19.563  -10.336 31.400  1.00 20.29  ? 115 TYR A CG  1 
ATOM   906  C  CD1 . TYR A 1 115 ? 20.647  -11.182 31.602  1.00 20.07  ? 115 TYR A CD1 1 
ATOM   907  C  CD2 . TYR A 1 115 ? 19.720  -8.993  31.695  1.00 19.85  ? 115 TYR A CD2 1 
ATOM   908  C  CE1 . TYR A 1 115 ? 21.835  -10.707 32.120  1.00 22.48  ? 115 TYR A CE1 1 
ATOM   909  C  CE2 . TYR A 1 115 ? 20.909  -8.514  32.221  1.00 19.20  ? 115 TYR A CE2 1 
ATOM   910  C  CZ  . TYR A 1 115 ? 21.969  -9.372  32.430  1.00 21.52  ? 115 TYR A CZ  1 
ATOM   911  O  OH  . TYR A 1 115 ? 23.178  -8.943  32.892  1.00 19.99  ? 115 TYR A OH  1 
ATOM   912  N  N   . HIS A 1 116 ? 16.476  -12.058 28.360  1.00 17.67  ? 116 HIS A N   1 
ATOM   913  C  CA  . HIS A 1 116 ? 15.053  -12.199 28.081  1.00 18.69  ? 116 HIS A CA  1 
ATOM   914  C  C   . HIS A 1 116 ? 14.591  -13.641 28.185  1.00 18.19  ? 116 HIS A C   1 
ATOM   915  O  O   . HIS A 1 116 ? 13.517  -13.905 28.746  1.00 17.13  ? 116 HIS A O   1 
ATOM   916  C  CB  . HIS A 1 116 ? 14.717  -11.710 26.678  1.00 17.59  ? 116 HIS A CB  1 
ATOM   917  C  CG  . HIS A 1 116 ? 13.268  -11.805 26.389  1.00 17.13  ? 116 HIS A CG  1 
ATOM   918  N  ND1 . HIS A 1 116 ? 12.369  -10.813 26.740  1.00 18.00  ? 116 HIS A ND1 1 
ATOM   919  C  CD2 . HIS A 1 116 ? 12.563  -12.727 25.721  1.00 17.32  ? 116 HIS A CD2 1 
ATOM   920  C  CE1 . HIS A 1 116 ? 11.158  -11.171 26.323  1.00 18.36  ? 116 HIS A CE1 1 
ATOM   921  N  NE2 . HIS A 1 116 ? 11.263  -12.310 25.672  1.00 15.22  ? 116 HIS A NE2 1 
ATOM   922  N  N   . ALA A 1 117 ? 15.401  -14.553 27.616  1.00 19.51  ? 117 ALA A N   1 
ATOM   923  C  CA  . ALA A 1 117 ? 15.053  -15.966 27.535  1.00 18.59  ? 117 ALA A CA  1 
ATOM   924  C  C   . ALA A 1 117 ? 14.824  -16.551 28.925  1.00 17.55  ? 117 ALA A C   1 
ATOM   925  O  O   . ALA A 1 117 ? 13.859  -17.285 29.139  1.00 16.07  ? 117 ALA A O   1 
ATOM   926  C  CB  . ALA A 1 117 ? 16.118  -16.708 26.768  1.00 20.61  ? 117 ALA A CB  1 
ATOM   927  N  N   . MET A 1 118 ? 15.689  -16.198 29.876  1.00 16.83  ? 118 MET A N   1 
ATOM   928  C  CA  . MET A 1 118 ? 15.595  -16.711 31.227  1.00 18.64  ? 118 MET A CA  1 
ATOM   929  C  C   . MET A 1 118 ? 14.477  -16.051 32.033  1.00 16.80  ? 118 MET A C   1 
ATOM   930  O  O   . MET A 1 118 ? 13.889  -16.683 32.914  1.00 16.52  ? 118 MET A O   1 
ATOM   931  C  CB  . MET A 1 118 ? 16.942  -16.537 31.933  1.00 20.62  ? 118 MET A CB  1 
ATOM   932  C  CG  . MET A 1 118 ? 17.868  -17.660 31.597  1.00 24.76  ? 118 MET A CG  1 
ATOM   933  S  SD  . MET A 1 118 ? 19.593  -17.316 32.111  1.00 34.10  ? 118 MET A SD  1 
ATOM   934  C  CE  . MET A 1 118 ? 20.326  -18.912 31.731  1.00 39.57  ? 118 MET A CE  1 
ATOM   935  N  N   . MET A 1 119 ? 14.177  -14.771 31.764  1.00 16.35  ? 119 MET A N   1 
ATOM   936  C  CA  . MET A 1 119 ? 13.011  -14.136 32.357  1.00 14.15  ? 119 MET A CA  1 
ATOM   937  C  C   . MET A 1 119 ? 11.712  -14.829 31.959  1.00 12.80  ? 119 MET A C   1 
ATOM   938  O  O   . MET A 1 119 ? 10.830  -14.957 32.780  1.00 14.16  ? 119 MET A O   1 
ATOM   939  C  CB  . MET A 1 119 ? 12.907  -12.686 31.884  1.00 15.11  ? 119 MET A CB  1 
ATOM   940  C  CG  . MET A 1 119 ? 13.950  -11.815 32.490  1.00 15.07  ? 119 MET A CG  1 
ATOM   941  S  SD  . MET A 1 119 ? 13.631  -10.078 32.108  1.00 18.92  ? 119 MET A SD  1 
ATOM   942  C  CE  . MET A 1 119 ? 15.081  -9.368  32.888  1.00 18.52  ? 119 MET A CE  1 
ATOM   943  N  N   . VAL A 1 120 ? 11.611  -15.254 30.705  1.00 13.67  ? 120 VAL A N   1 
ATOM   944  C  CA  . VAL A 1 120 ? 10.439  -15.943 30.191  1.00 13.53  ? 120 VAL A CA  1 
ATOM   945  C  C   . VAL A 1 120 ? 10.313  -17.318 30.852  1.00 15.32  ? 120 VAL A C   1 
ATOM   946  O  O   . VAL A 1 120 ? 9.190   -17.752 31.137  1.00 17.34  ? 120 VAL A O   1 
ATOM   947  C  CB  . VAL A 1 120 ? 10.468  -16.048 28.649  1.00 15.49  ? 120 VAL A CB  1 
ATOM   948  C  CG1 . VAL A 1 120 ? 9.384   -16.995 28.136  1.00 17.53  ? 120 VAL A CG1 1 
ATOM   949  C  CG2 . VAL A 1 120 ? 10.381  -14.713 27.932  1.00 16.05  ? 120 VAL A CG2 1 
ATOM   950  N  N   . ASP A 1 121 ? 11.450  -18.011 31.078  1.00 15.91  ? 121 ASP A N   1 
ATOM   951  C  CA  . ASP A 1 121 ? 11.494  -19.262 31.841  1.00 17.27  ? 121 ASP A CA  1 
ATOM   952  C  C   . ASP A 1 121 ? 10.723  -19.137 33.158  1.00 16.50  ? 121 ASP A C   1 
ATOM   953  O  O   . ASP A 1 121 ? 9.851   -19.964 33.456  1.00 14.48  ? 121 ASP A O   1 
ATOM   954  C  CB  . ASP A 1 121 ? 12.949  -19.685 32.117  1.00 17.68  ? 121 ASP A CB  1 
ATOM   955  C  CG  . ASP A 1 121 ? 13.184  -21.005 32.845  1.00 19.15  ? 121 ASP A CG  1 
ATOM   956  O  OD1 . ASP A 1 121 ? 12.544  -21.270 33.884  1.00 20.03  ? 121 ASP A OD1 1 
ATOM   957  O  OD2 . ASP A 1 121 ? 14.027  -21.769 32.373  1.00 20.42  ? 121 ASP A OD2 1 
ATOM   958  N  N   . ILE A 1 122 ? 11.041  -18.110 33.965  1.00 15.77  ? 122 ILE A N   1 
ATOM   959  C  CA  . ILE A 1 122 ? 10.422  -17.947 35.266  1.00 14.66  ? 122 ILE A CA  1 
ATOM   960  C  C   . ILE A 1 122 ? 8.961   -17.539 35.064  1.00 15.15  ? 122 ILE A C   1 
ATOM   961  O  O   . ILE A 1 122 ? 8.079   -17.983 35.803  1.00 16.00  ? 122 ILE A O   1 
ATOM   962  C  CB  . ILE A 1 122 ? 11.198  -16.931 36.126  1.00 15.11  ? 122 ILE A CB  1 
ATOM   963  C  CG1 . ILE A 1 122 ? 12.698  -17.247 36.195  1.00 17.61  ? 122 ILE A CG1 1 
ATOM   964  C  CG2 . ILE A 1 122 ? 10.580  -16.802 37.512  1.00 15.10  ? 122 ILE A CG2 1 
ATOM   965  C  CD1 . ILE A 1 122 ? 13.033  -18.720 36.478  1.00 18.19  ? 122 ILE A CD1 1 
ATOM   966  N  N   . ALA A 1 123 ? 8.741   -16.582 34.157  1.00 14.82  ? 123 ALA A N   1 
ATOM   967  C  CA  . ALA A 1 123 ? 7.404   -16.107 33.823  1.00 14.06  ? 123 ALA A CA  1 
ATOM   968  C  C   . ALA A 1 123 ? 6.496   -17.268 33.465  1.00 14.67  ? 123 ALA A C   1 
ATOM   969  O  O   . ALA A 1 123 ? 5.377   -17.279 33.933  1.00 16.23  ? 123 ALA A O   1 
ATOM   970  C  CB  . ALA A 1 123 ? 7.474   -15.130 32.675  1.00 14.60  ? 123 ALA A CB  1 
ATOM   971  N  N   . VAL A 1 124 ? 6.975   -18.194 32.630  1.00 14.99  ? 124 VAL A N   1 
ATOM   972  C  CA  . VAL A 1 124 ? 6.203   -19.376 32.259  1.00 15.71  ? 124 VAL A CA  1 
ATOM   973  C  C   . VAL A 1 124 ? 5.869   -20.229 33.488  1.00 14.99  ? 124 VAL A C   1 
ATOM   974  O  O   . VAL A 1 124 ? 4.748   -20.738 33.609  1.00 15.27  ? 124 VAL A O   1 
ATOM   975  C  CB  . VAL A 1 124 ? 6.937   -20.180 31.170  1.00 18.03  ? 124 VAL A CB  1 
ATOM   976  C  CG1 . VAL A 1 124 ? 6.427   -21.601 31.083  1.00 19.29  ? 124 VAL A CG1 1 
ATOM   977  C  CG2 . VAL A 1 124 ? 6.856   -19.477 29.835  1.00 18.86  ? 124 VAL A CG2 1 
ATOM   978  N  N   . GLN A 1 125 ? 6.812   -20.377 34.426  1.00 14.26  ? 125 GLN A N   1 
ATOM   979  C  CA  . GLN A 1 125 ? 6.527   -21.082 35.665  1.00 14.33  ? 125 GLN A CA  1 
ATOM   980  C  C   . GLN A 1 125 ? 5.380   -20.436 36.448  1.00 15.06  ? 125 GLN A C   1 
ATOM   981  O  O   . GLN A 1 125 ? 4.542   -21.136 37.017  1.00 15.45  ? 125 GLN A O   1 
ATOM   982  C  CB  . GLN A 1 125 ? 7.801   -21.199 36.510  1.00 14.73  ? 125 GLN A CB  1 
ATOM   983  C  CG  . GLN A 1 125 ? 8.809   -22.138 35.888  1.00 14.32  ? 125 GLN A CG  1 
ATOM   984  C  CD  . GLN A 1 125 ? 9.948   -22.431 36.819  1.00 15.46  ? 125 GLN A CD  1 
ATOM   985  O  OE1 . GLN A 1 125 ? 9.741   -22.802 37.975  1.00 14.85  ? 125 GLN A OE1 1 
ATOM   986  N  NE2 . GLN A 1 125 ? 11.151  -22.160 36.346  1.00 18.17  ? 125 GLN A NE2 1 
ATOM   987  N  N   . LEU A 1 126 ? 5.308   -19.103 36.458  1.00 13.71  ? 126 LEU A N   1 
ATOM   988  C  CA  . LEU A 1 126 ? 4.256   -18.447 37.192  1.00 14.01  ? 126 LEU A CA  1 
ATOM   989  C  C   . LEU A 1 126 ? 2.924   -18.681 36.482  1.00 13.60  ? 126 LEU A C   1 
ATOM   990  O  O   . LEU A 1 126 ? 1.962   -19.073 37.143  1.00 13.69  ? 126 LEU A O   1 
ATOM   991  C  CB  . LEU A 1 126 ? 4.532   -16.954 37.350  1.00 15.24  ? 126 LEU A CB  1 
ATOM   992  C  CG  . LEU A 1 126 ? 3.343   -16.176 37.916  1.00 17.44  ? 126 LEU A CG  1 
ATOM   993  C  CD1 . LEU A 1 126 ? 3.334   -16.232 39.428  1.00 16.14  ? 126 LEU A CD1 1 
ATOM   994  C  CD2 . LEU A 1 126 ? 3.340   -14.751 37.404  1.00 18.32  ? 126 LEU A CD2 1 
ATOM   995  N  N   . ILE A 1 127 ? 2.901   -18.500 35.158  1.00 12.49  ? 127 ILE A N   1 
ATOM   996  C  CA  . ILE A 1 127 ? 1.658   -18.642 34.400  1.00 13.82  ? 127 ILE A CA  1 
ATOM   997  C  C   . ILE A 1 127 ? 1.129   -20.065 34.575  1.00 15.80  ? 127 ILE A C   1 
ATOM   998  O  O   . ILE A 1 127 ? -0.067  -20.257 34.787  1.00 16.19  ? 127 ILE A O   1 
ATOM   999  C  CB  . ILE A 1 127 ? 1.850   -18.348 32.898  1.00 16.23  ? 127 ILE A CB  1 
ATOM   1000 C  CG1 . ILE A 1 127 ? 2.331   -16.928 32.609  1.00 16.05  ? 127 ILE A CG1 1 
ATOM   1001 C  CG2 . ILE A 1 127 ? 0.570   -18.626 32.125  1.00 16.57  ? 127 ILE A CG2 1 
ATOM   1002 C  CD1 . ILE A 1 127 ? 1.395   -15.863 33.103  1.00 16.61  ? 127 ILE A CD1 1 
ATOM   1003 N  N   . GLN A 1 128 ? 2.018   -21.063 34.482  1.00 14.96  ? 128 GLN A N   1 
ATOM   1004 C  CA  . GLN A 1 128 ? 1.618   -22.469 34.617  1.00 15.89  ? 128 GLN A CA  1 
ATOM   1005 C  C   . GLN A 1 128 ? 1.048   -22.786 36.004  1.00 14.49  ? 128 GLN A C   1 
ATOM   1006 O  O   . GLN A 1 128 ? 0.071   -23.535 36.106  1.00 15.31  ? 128 GLN A O   1 
ATOM   1007 C  CB  . GLN A 1 128 ? 2.819   -23.348 34.277  1.00 16.62  ? 128 GLN A CB  1 
ATOM   1008 C  CG  . GLN A 1 128 ? 3.122   -23.411 32.783  1.00 20.17  ? 128 GLN A CG  1 
ATOM   1009 C  CD  . GLN A 1 128 ? 4.179   -24.443 32.473  1.00 23.11  ? 128 GLN A CD  1 
ATOM   1010 O  OE1 . GLN A 1 128 ? 5.238   -24.468 33.088  1.00 26.79  ? 128 GLN A OE1 1 
ATOM   1011 N  NE2 . GLN A 1 128 ? 3.893   -25.323 31.528  1.00 30.40  ? 128 GLN A NE2 1 
ATOM   1012 N  N   . LYS A 1 129 ? 1.654   -22.238 37.073  1.00 13.16  ? 129 LYS A N   1 
ATOM   1013 C  CA  . LYS A 1 129 ? 1.151   -22.373 38.422  1.00 12.81  ? 129 LYS A CA  1 
ATOM   1014 C  C   . LYS A 1 129 ? -0.317  -21.943 38.453  1.00 13.68  ? 129 LYS A C   1 
ATOM   1015 O  O   . LYS A 1 129 ? -1.163  -22.638 39.016  1.00 13.07  ? 129 LYS A O   1 
ATOM   1016 C  CB  . LYS A 1 129 ? 1.973   -21.558 39.432  1.00 14.49  ? 129 LYS A CB  1 
ATOM   1017 C  CG  . LYS A 1 129 ? 1.449   -21.567 40.860  1.00 14.89  ? 129 LYS A CG  1 
ATOM   1018 C  CD  . LYS A 1 129 ? 2.340   -20.970 41.941  1.00 17.08  ? 129 LYS A CD  1 
ATOM   1019 C  CE  . LYS A 1 129 ? 1.643   -21.033 43.280  1.00 16.69  ? 129 LYS A CE  1 
ATOM   1020 N  NZ  . LYS A 1 129 ? 2.533   -20.719 44.415  1.00 19.13  ? 129 LYS A NZ  1 
ATOM   1021 N  N   . TRP A 1 130 ? -0.600  -20.778 37.863  1.00 13.99  ? 130 TRP A N   1 
ATOM   1022 C  CA  . TRP A 1 130 ? -1.916  -20.186 38.014  1.00 16.06  ? 130 TRP A CA  1 
ATOM   1023 C  C   . TRP A 1 130 ? -2.889  -20.968 37.138  1.00 15.77  ? 130 TRP A C   1 
ATOM   1024 O  O   . TRP A 1 130 ? -4.057  -21.083 37.499  1.00 17.15  ? 130 TRP A O   1 
ATOM   1025 C  CB  . TRP A 1 130 ? -1.880  -18.691 37.659  1.00 16.62  ? 130 TRP A CB  1 
ATOM   1026 C  CG  . TRP A 1 130 ? -1.179  -17.830 38.678  1.00 16.43  ? 130 TRP A CG  1 
ATOM   1027 C  CD1 . TRP A 1 130 ? -0.626  -18.250 39.848  1.00 15.39  ? 130 TRP A CD1 1 
ATOM   1028 C  CD2 . TRP A 1 130 ? -1.007  -16.385 38.646  1.00 16.55  ? 130 TRP A CD2 1 
ATOM   1029 N  NE1 . TRP A 1 130 ? -0.092  -17.186 40.513  1.00 17.60  ? 130 TRP A NE1 1 
ATOM   1030 C  CE2 . TRP A 1 130 ? -0.318  -16.029 39.815  1.00 15.95  ? 130 TRP A CE2 1 
ATOM   1031 C  CE3 . TRP A 1 130 ? -1.355  -15.366 37.753  1.00 18.54  ? 130 TRP A CE3 1 
ATOM   1032 C  CZ2 . TRP A 1 130 ? 0.035   -14.713 40.112  1.00 15.72  ? 130 TRP A CZ2 1 
ATOM   1033 C  CZ3 . TRP A 1 130 ? -1.027  -14.047 38.046  1.00 16.74  ? 130 TRP A CZ3 1 
ATOM   1034 C  CH2 . TRP A 1 130 ? -0.329  -13.733 39.215  1.00 16.20  ? 130 TRP A CH2 1 
ATOM   1035 N  N   . GLU A 1 131 ? -2.402  -21.442 35.990  1.00 15.38  ? 131 GLU A N   1 
ATOM   1036 C  CA  . GLU A 1 131 ? -3.203  -22.281 35.103  1.00 19.24  ? 131 GLU A CA  1 
ATOM   1037 C  C   . GLU A 1 131 ? -3.611  -23.575 35.790  1.00 17.94  ? 131 GLU A C   1 
ATOM   1038 O  O   . GLU A 1 131 ? -4.665  -24.121 35.475  1.00 17.34  ? 131 GLU A O   1 
ATOM   1039 C  CB  . GLU A 1 131 ? -2.460  -22.713 33.838  1.00 20.45  ? 131 GLU A CB  1 
ATOM   1040 C  CG  . GLU A 1 131 ? -2.187  -21.601 32.862  1.00 23.95  ? 131 GLU A CG  1 
ATOM   1041 C  CD  . GLU A 1 131 ? -3.401  -21.027 32.168  1.00 29.03  ? 131 GLU A CD  1 
ATOM   1042 O  OE1 . GLU A 1 131 ? -3.199  -20.241 31.210  1.00 33.94  ? 131 GLU A OE1 1 
ATOM   1043 O  OE2 . GLU A 1 131 ? -4.548  -21.341 32.595  1.00 29.05  ? 131 GLU A OE2 1 
ATOM   1044 N  N   . ARG A 1 132 ? -2.802  -24.051 36.735  1.00 16.56  ? 132 ARG A N   1 
ATOM   1045 C  CA  . ARG A 1 132 ? -3.063  -25.344 37.366  1.00 15.56  ? 132 ARG A CA  1 
ATOM   1046 C  C   . ARG A 1 132 ? -3.855  -25.235 38.664  1.00 15.39  ? 132 ARG A C   1 
ATOM   1047 O  O   . ARG A 1 132 ? -4.150  -26.277 39.263  1.00 16.55  ? 132 ARG A O   1 
ATOM   1048 C  CB  . ARG A 1 132 ? -1.730  -26.040 37.640  1.00 13.35  ? 132 ARG A CB  1 
ATOM   1049 C  CG  . ARG A 1 132 ? -1.052  -26.491 36.361  1.00 13.70  ? 132 ARG A CG  1 
ATOM   1050 C  CD  . ARG A 1 132 ? 0.398   -26.891 36.587  1.00 14.37  ? 132 ARG A CD  1 
ATOM   1051 N  NE  . ARG A 1 132 ? 0.898   -27.338 35.290  1.00 16.09  ? 132 ARG A NE  1 
ATOM   1052 C  CZ  . ARG A 1 132 ? 2.175   -27.508 34.947  1.00 15.98  ? 132 ARG A CZ  1 
ATOM   1053 N  NH1 . ARG A 1 132 ? 3.139   -27.238 35.791  1.00 15.10  ? 132 ARG A NH1 1 
ATOM   1054 N  NH2 . ARG A 1 132 ? 2.467   -27.941 33.741  1.00 16.75  ? 132 ARG A NH2 1 
ATOM   1055 N  N   . LEU A 1 133 ? -4.271  -24.038 39.076  1.00 14.41  ? 133 LEU A N   1 
ATOM   1056 C  CA  . LEU A 1 133 ? -5.100  -23.938 40.269  1.00 15.75  ? 133 LEU A CA  1 
ATOM   1057 C  C   . LEU A 1 133 ? -6.480  -24.526 39.973  1.00 16.46  ? 133 LEU A C   1 
ATOM   1058 O  O   . LEU A 1 133 ? -6.908  -24.507 38.825  1.00 18.64  ? 133 LEU A O   1 
ATOM   1059 C  CB  . LEU A 1 133 ? -5.220  -22.479 40.722  1.00 15.34  ? 133 LEU A CB  1 
ATOM   1060 C  CG  . LEU A 1 133 ? -3.900  -21.815 41.134  1.00 16.31  ? 133 LEU A CG  1 
ATOM   1061 C  CD1 . LEU A 1 133 ? -4.095  -20.339 41.407  1.00 17.03  ? 133 LEU A CD1 1 
ATOM   1062 C  CD2 . LEU A 1 133 ? -3.315  -22.499 42.361  1.00 17.10  ? 133 LEU A CD2 1 
ATOM   1063 N  N   . ASN A 1 134 ? -7.158  -25.025 41.017  1.00 17.51  ? 134 ASN A N   1 
ATOM   1064 C  CA  . ASN A 1 134 ? -8.498  -25.595 40.883  1.00 18.03  ? 134 ASN A CA  1 
ATOM   1065 C  C   . ASN A 1 134 ? -9.546  -24.481 41.010  1.00 20.41  ? 134 ASN A C   1 
ATOM   1066 O  O   . ASN A 1 134 ? -9.244  -23.365 41.427  1.00 19.91  ? 134 ASN A O   1 
ATOM   1067 C  CB  . ASN A 1 134 ? -8.750  -26.693 41.919  1.00 17.42  ? 134 ASN A CB  1 
ATOM   1068 C  CG  . ASN A 1 134 ? -7.688  -27.776 41.854  1.00 16.97  ? 134 ASN A CG  1 
ATOM   1069 O  OD1 . ASN A 1 134 ? -7.589  -28.500 40.861  1.00 16.76  ? 134 ASN A OD1 1 
ATOM   1070 N  ND2 . ASN A 1 134 ? -6.863  -27.833 42.882  1.00 18.89  ? 134 ASN A ND2 1 
ATOM   1071 N  N   . ALA A 1 135 ? -10.785 -24.829 40.660  1.00 24.06  ? 135 ALA A N   1 
ATOM   1072 C  CA  . ALA A 1 135 ? -11.891 -23.904 40.420  1.00 28.90  ? 135 ALA A CA  1 
ATOM   1073 C  C   . ALA A 1 135 ? -11.945 -22.680 41.338  1.00 36.94  ? 135 ALA A C   1 
ATOM   1074 O  O   . ALA A 1 135 ? -11.982 -21.540 40.850  1.00 48.40  ? 135 ALA A O   1 
ATOM   1075 C  CB  . ALA A 1 135 ? -13.193 -24.662 40.493  1.00 30.29  ? 135 ALA A CB  1 
ATOM   1076 N  N   . ASP A 1 136 ? -12.084 -22.839 42.648  1.00 34.17  ? 136 ASP A N   1 
ATOM   1077 C  CA  . ASP A 1 136 ? -12.347 -21.609 43.397  1.00 34.69  ? 136 ASP A CA  1 
ATOM   1078 C  C   . ASP A 1 136 ? -11.099 -21.148 44.150  1.00 29.45  ? 136 ASP A C   1 
ATOM   1079 O  O   . ASP A 1 136 ? -11.215 -20.436 45.136  1.00 30.81  ? 136 ASP A O   1 
ATOM   1080 C  CB  . ASP A 1 136 ? -13.557 -21.726 44.338  1.00 34.58  ? 136 ASP A CB  1 
ATOM   1081 C  CG  . ASP A 1 136 ? -14.894 -21.754 43.625  1.00 40.51  ? 136 ASP A CG  1 
ATOM   1082 O  OD1 . ASP A 1 136 ? -15.323 -20.683 43.137  1.00 39.48  ? 136 ASP A OD1 1 
ATOM   1083 O  OD2 . ASP A 1 136 ? -15.480 -22.864 43.524  1.00 46.48  ? 136 ASP A OD2 1 
ATOM   1084 N  N   . GLU A 1 137 ? -9.904  -21.519 43.687  1.00 24.41  ? 137 GLU A N   1 
ATOM   1085 C  CA  . GLU A 1 137 ? -8.709  -21.198 44.451  1.00 23.47  ? 137 GLU A CA  1 
ATOM   1086 C  C   . GLU A 1 137 ? -8.252  -19.776 44.147  1.00 23.05  ? 137 GLU A C   1 
ATOM   1087 O  O   . GLU A 1 137 ? -8.600  -19.202 43.119  1.00 23.37  ? 137 GLU A O   1 
ATOM   1088 C  CB  . GLU A 1 137 ? -7.622  -22.226 44.173  1.00 23.43  ? 137 GLU A CB  1 
ATOM   1089 C  CG  . GLU A 1 137 ? -8.038  -23.603 44.696  1.00 26.23  ? 137 GLU A CG  1 
ATOM   1090 C  CD  . GLU A 1 137 ? -7.043  -24.728 44.499  1.00 25.92  ? 137 GLU A CD  1 
ATOM   1091 O  OE1 . GLU A 1 137 ? -6.098  -24.564 43.687  1.00 24.74  ? 137 GLU A OE1 1 
ATOM   1092 O  OE2 . GLU A 1 137 ? -7.230  -25.769 45.152  1.00 27.97  ? 137 GLU A OE2 1 
ATOM   1093 N  N   . HIS A 1 138 ? -7.456  -19.230 45.068  1.00 20.98  ? 138 HIS A N   1 
ATOM   1094 C  CA  . HIS A 1 138 ? -6.949  -17.880 44.922  1.00 21.23  ? 138 HIS A CA  1 
ATOM   1095 C  C   . HIS A 1 138 ? -5.432  -17.896 44.859  1.00 19.77  ? 138 HIS A C   1 
ATOM   1096 O  O   . HIS A 1 138 ? -4.782  -18.955 44.917  1.00 15.79  ? 138 HIS A O   1 
ATOM   1097 C  CB  . HIS A 1 138 ? -7.498  -16.993 46.042  1.00 23.03  ? 138 HIS A CB  1 
ATOM   1098 C  CG  . HIS A 1 138 ? -7.129  -17.425 47.403  1.00 25.02  ? 138 HIS A CG  1 
ATOM   1099 N  ND1 . HIS A 1 138 ? -5.900  -17.137 47.941  1.00 29.92  ? 138 HIS A ND1 1 
ATOM   1100 C  CD2 . HIS A 1 138 ? -7.794  -18.108 48.324  1.00 26.23  ? 138 HIS A CD2 1 
ATOM   1101 C  CE1 . HIS A 1 138 ? -5.843  -17.619 49.167  1.00 29.91  ? 138 HIS A CE1 1 
ATOM   1102 N  NE2 . HIS A 1 138 ? -6.991  -18.212 49.419  1.00 30.74  ? 138 HIS A NE2 1 
ATOM   1103 N  N   . ILE A 1 139 ? -4.929  -16.694 44.577  1.00 18.15  ? 139 ILE A N   1 
ATOM   1104 C  CA  . ILE A 1 139 ? -3.521  -16.413 44.396  1.00 17.59  ? 139 ILE A CA  1 
ATOM   1105 C  C   . ILE A 1 139 ? -3.118  -15.476 45.520  1.00 17.74  ? 139 ILE A C   1 
ATOM   1106 O  O   . ILE A 1 139 ? -3.834  -14.509 45.800  1.00 16.15  ? 139 ILE A O   1 
ATOM   1107 C  CB  . ILE A 1 139 ? -3.270  -15.755 43.033  1.00 17.55  ? 139 ILE A CB  1 
ATOM   1108 C  CG1 . ILE A 1 139 ? -3.508  -16.701 41.865  1.00 18.05  ? 139 ILE A CG1 1 
ATOM   1109 C  CG2 . ILE A 1 139 ? -1.870  -15.153 42.970  1.00 17.98  ? 139 ILE A CG2 1 
ATOM   1110 C  CD1 . ILE A 1 139 ? -3.619  -15.976 40.570  1.00 19.84  ? 139 ILE A CD1 1 
ATOM   1111 N  N   . GLU A 1 140 ? -1.984  -15.787 46.173  1.00 17.28  ? 140 GLU A N   1 
ATOM   1112 C  CA  . GLU A 1 140 ? -1.388  -14.902 47.144  1.00 19.72  ? 140 GLU A CA  1 
ATOM   1113 C  C   . GLU A 1 140 ? -0.419  -14.057 46.326  1.00 16.72  ? 140 GLU A C   1 
ATOM   1114 O  O   . GLU A 1 140 ? 0.644   -14.556 45.961  1.00 15.42  ? 140 GLU A O   1 
ATOM   1115 C  CB  . GLU A 1 140 ? -0.719  -15.716 48.260  1.00 22.34  ? 140 GLU A CB  1 
ATOM   1116 C  CG  . GLU A 1 140 ? -1.700  -16.453 49.166  1.00 29.13  ? 140 GLU A CG  1 
ATOM   1117 C  CD  . GLU A 1 140 ? -1.095  -17.478 50.122  1.00 37.34  ? 140 GLU A CD  1 
ATOM   1118 O  OE1 . GLU A 1 140 ? 0.058   -17.949 49.870  1.00 39.85  ? 140 GLU A OE1 1 
ATOM   1119 O  OE2 . GLU A 1 140 ? -1.777  -17.828 51.124  1.00 42.99  ? 140 GLU A OE2 1 
ATOM   1120 N  N   . VAL A 1 141 ? -0.793  -12.801 46.030  1.00 13.63  ? 141 VAL A N   1 
ATOM   1121 C  CA  . VAL A 1 141 ? -0.099  -12.047 44.990  1.00 13.45  ? 141 VAL A CA  1 
ATOM   1122 C  C   . VAL A 1 141 ? 1.342   -11.736 45.395  1.00 13.31  ? 141 VAL A C   1 
ATOM   1123 O  O   . VAL A 1 141 ? 2.244   -12.079 44.644  1.00 14.82  ? 141 VAL A O   1 
ATOM   1124 C  CB  . VAL A 1 141 ? -0.853  -10.764 44.584  1.00 15.26  ? 141 VAL A CB  1 
ATOM   1125 C  CG1 . VAL A 1 141 ? -0.045  -9.982  43.538  1.00 14.98  ? 141 VAL A CG1 1 
ATOM   1126 C  CG2 . VAL A 1 141 ? -2.245  -11.102 44.054  1.00 14.61  ? 141 VAL A CG2 1 
ATOM   1127 N  N   . PRO A 1 142 ? 1.622   -11.030 46.518  1.00 14.13  ? 142 PRO A N   1 
ATOM   1128 C  CA  . PRO A 1 142 ? 2.991   -10.663 46.864  1.00 13.95  ? 142 PRO A CA  1 
ATOM   1129 C  C   . PRO A 1 142 ? 3.892   -11.872 47.031  1.00 15.14  ? 142 PRO A C   1 
ATOM   1130 O  O   . PRO A 1 142 ? 5.059   -11.799 46.706  1.00 13.78  ? 142 PRO A O   1 
ATOM   1131 C  CB  . PRO A 1 142 ? 2.887   -9.872  48.176  1.00 15.44  ? 142 PRO A CB  1 
ATOM   1132 C  CG  . PRO A 1 142 ? 1.465   -10.057 48.631  1.00 15.82  ? 142 PRO A CG  1 
ATOM   1133 C  CD  . PRO A 1 142 ? 0.660   -10.341 47.376  1.00 15.02  ? 142 PRO A CD  1 
ATOM   1134 N  N   . GLU A 1 143 ? 3.316   -12.985 47.520  1.00 16.95  ? 143 GLU A N   1 
ATOM   1135 C  CA  . GLU A 1 143 ? 4.034   -14.231 47.706  1.00 16.54  ? 143 GLU A CA  1 
ATOM   1136 C  C   . GLU A 1 143 ? 4.512   -14.722 46.356  1.00 16.68  ? 143 GLU A C   1 
ATOM   1137 O  O   . GLU A 1 143 ? 5.673   -15.097 46.216  1.00 16.35  ? 143 GLU A O   1 
ATOM   1138 C  CB  . GLU A 1 143 ? 3.148   -15.275 48.391  1.00 19.31  ? 143 GLU A CB  1 
ATOM   1139 C  CG  . GLU A 1 143 ? 2.843   -14.970 49.849  1.00 20.83  ? 143 GLU A CG  1 
ATOM   1140 C  CD  . GLU A 1 143 ? 1.897   -13.803 50.146  1.00 24.66  ? 143 GLU A CD  1 
ATOM   1141 O  OE1 . GLU A 1 143 ? 1.262   -13.280 49.216  1.00 26.22  ? 143 GLU A OE1 1 
ATOM   1142 O  OE2 . GLU A 1 143 ? 1.757   -13.434 51.332  1.00 23.94  ? 143 GLU A OE2 1 
ATOM   1143 N  N   . ASP A 1 144 ? 3.607   -14.777 45.371  1.00 14.62  ? 144 ASP A N   1 
ATOM   1144 C  CA  . ASP A 1 144 ? 3.980   -15.273 44.053  1.00 14.36  ? 144 ASP A CA  1 
ATOM   1145 C  C   . ASP A 1 144 ? 4.894   -14.330 43.279  1.00 14.14  ? 144 ASP A C   1 
ATOM   1146 O  O   . ASP A 1 144 ? 5.742   -14.788 42.496  1.00 13.09  ? 144 ASP A O   1 
ATOM   1147 C  CB  . ASP A 1 144 ? 2.755   -15.629 43.227  1.00 14.68  ? 144 ASP A CB  1 
ATOM   1148 C  CG  . ASP A 1 144 ? 2.287   -17.053 43.502  1.00 15.37  ? 144 ASP A CG  1 
ATOM   1149 O  OD1 . ASP A 1 144 ? 3.105   -17.834 44.049  1.00 16.40  ? 144 ASP A OD1 1 
ATOM   1150 O  OD2 . ASP A 1 144 ? 1.102   -17.361 43.197  1.00 15.59  ? 144 ASP A OD2 1 
ATOM   1151 N  N   . MET A 1 145 ? 4.654   -13.026 43.428  1.00 13.43  ? 145 MET A N   1 
ATOM   1152 C  CA  . MET A 1 145 ? 5.493   -12.041 42.754  1.00 14.56  ? 145 MET A CA  1 
ATOM   1153 C  C   . MET A 1 145 ? 6.915   -12.102 43.318  1.00 13.88  ? 145 MET A C   1 
ATOM   1154 O  O   . MET A 1 145 ? 7.845   -11.991 42.569  1.00 14.65  ? 145 MET A O   1 
ATOM   1155 C  CB  . MET A 1 145 ? 4.909   -10.634 42.870  1.00 15.07  ? 145 MET A CB  1 
ATOM   1156 C  CG  . MET A 1 145 ? 3.542   -10.487 42.235  1.00 15.27  ? 145 MET A CG  1 
ATOM   1157 S  SD  . MET A 1 145 ? 3.491   -10.869 40.468  1.00 17.05  ? 145 MET A SD  1 
ATOM   1158 C  CE  . MET A 1 145 ? 2.919   -12.575 40.545  1.00 20.09  ? 145 MET A CE  1 
ATOM   1159 N  N   . THR A 1 146 ? 7.075   -12.412 44.601  1.00 14.02  ? 146 THR A N   1 
ATOM   1160 C  CA  . THR A 1 146 ? 8.382   -12.516 45.205  1.00 15.77  ? 146 THR A CA  1 
ATOM   1161 C  C   . THR A 1 146 ? 9.102   -13.783 44.764  1.00 14.93  ? 146 THR A C   1 
ATOM   1162 O  O   . THR A 1 146 ? 10.304  -13.724 44.514  1.00 15.29  ? 146 THR A O   1 
ATOM   1163 C  CB  . THR A 1 146 ? 8.317   -12.505 46.732  1.00 16.45  ? 146 THR A CB  1 
ATOM   1164 O  OG1 . THR A 1 146 ? 7.674   -11.287 47.049  1.00 18.78  ? 146 THR A OG1 1 
ATOM   1165 C  CG2 . THR A 1 146 ? 9.680   -12.549 47.390  1.00 18.89  ? 146 THR A CG2 1 
ATOM   1166 N  N   . ARG A 1 147 ? 8.382   -14.912 44.688  1.00 14.25  ? 147 ARG A N   1 
ATOM   1167 C  CA  . ARG A 1 147 ? 8.909   -16.135 44.095  1.00 14.56  ? 147 ARG A CA  1 
ATOM   1168 C  C   . ARG A 1 147 ? 9.433   -15.839 42.689  1.00 13.01  ? 147 ARG A C   1 
ATOM   1169 O  O   . ARG A 1 147 ? 10.546  -16.242 42.347  1.00 13.09  ? 147 ARG A O   1 
ATOM   1170 C  CB  . ARG A 1 147 ? 7.832   -17.232 43.934  1.00 15.63  ? 147 ARG A CB  1 
ATOM   1171 C  CG  . ARG A 1 147 ? 7.264   -17.748 45.236  1.00 16.62  ? 147 ARG A CG  1 
ATOM   1172 C  CD  . ARG A 1 147 ? 6.348   -18.947 44.992  1.00 19.75  ? 147 ARG A CD  1 
ATOM   1173 N  NE  . ARG A 1 147 ? 6.054   -19.621 46.249  1.00 19.31  ? 147 ARG A NE  1 
ATOM   1174 C  CZ  . ARG A 1 147 ? 4.992   -19.414 47.001  1.00 23.26  ? 147 ARG A CZ  1 
ATOM   1175 N  NH1 . ARG A 1 147 ? 4.040   -18.569 46.625  1.00 22.80  ? 147 ARG A NH1 1 
ATOM   1176 N  NH2 . ARG A 1 147 ? 4.893   -20.078 48.144  1.00 24.02  ? 147 ARG A NH2 1 
ATOM   1177 N  N   . LEU A 1 148 ? 8.656   -15.104 41.889  1.00 12.56  ? 148 LEU A N   1 
ATOM   1178 C  CA  . LEU A 1 148 ? 9.060   -14.836 40.517  1.00 12.98  ? 148 LEU A CA  1 
ATOM   1179 C  C   . LEU A 1 148 ? 10.321  -13.958 40.468  1.00 13.54  ? 148 LEU A C   1 
ATOM   1180 O  O   . LEU A 1 148 ? 11.265  -14.276 39.732  1.00 12.60  ? 148 LEU A O   1 
ATOM   1181 C  CB  . LEU A 1 148 ? 7.921   -14.166 39.762  1.00 14.21  ? 148 LEU A CB  1 
ATOM   1182 C  CG  . LEU A 1 148 ? 8.319   -13.747 38.344  1.00 15.79  ? 148 LEU A CG  1 
ATOM   1183 C  CD1 . LEU A 1 148 ? 7.378   -14.286 37.295  1.00 17.48  ? 148 LEU A CD1 1 
ATOM   1184 C  CD2 . LEU A 1 148 ? 8.479   -12.236 38.250  1.00 17.34  ? 148 LEU A CD2 1 
ATOM   1185 N  N   . THR A 1 149 ? 10.338  -12.860 41.243  1.00 12.83  ? 149 THR A N   1 
ATOM   1186 C  CA  . THR A 1 149 ? 11.397  -11.892 41.082  1.00 13.99  ? 149 THR A CA  1 
ATOM   1187 C  C   . THR A 1 149 ? 12.684  -12.478 41.631  1.00 13.54  ? 149 THR A C   1 
ATOM   1188 O  O   . THR A 1 149 ? 13.724  -12.248 41.038  1.00 14.73  ? 149 THR A O   1 
ATOM   1189 C  CB  . THR A 1 149 ? 11.072  -10.513 41.680  1.00 14.03  ? 149 THR A CB  1 
ATOM   1190 O  OG1 . THR A 1 149 ? 10.748  -10.618 43.070  1.00 12.57  ? 149 THR A OG1 1 
ATOM   1191 C  CG2 . THR A 1 149 ? 9.918   -9.849  40.969  1.00 13.97  ? 149 THR A CG2 1 
ATOM   1192 N  N   . LEU A 1 150 ? 12.614  -13.199 42.756  1.00 14.46  ? 150 LEU A N   1 
ATOM   1193 C  CA  . LEU A 1 150 ? 13.813  -13.829 43.297  1.00 16.32  ? 150 LEU A CA  1 
ATOM   1194 C  C   . LEU A 1 150 ? 14.402  -14.797 42.273  1.00 15.35  ? 150 LEU A C   1 
ATOM   1195 O  O   . LEU A 1 150 ? 15.609  -14.793 42.014  1.00 15.33  ? 150 LEU A O   1 
ATOM   1196 C  CB  . LEU A 1 150 ? 13.510  -14.559 44.613  1.00 18.01  ? 150 LEU A CB  1 
ATOM   1197 C  CG  . LEU A 1 150 ? 14.743  -15.237 45.232  1.00 19.35  ? 150 LEU A CG  1 
ATOM   1198 C  CD1 . LEU A 1 150 ? 15.788  -14.207 45.700  1.00 20.67  ? 150 LEU A CD1 1 
ATOM   1199 C  CD2 . LEU A 1 150 ? 14.327  -16.110 46.375  1.00 20.97  ? 150 LEU A CD2 1 
ATOM   1200 N  N   . ASP A 1 151 ? 13.543  -15.646 41.705  1.00 16.18  ? 151 ASP A N   1 
ATOM   1201 C  CA  . ASP A 1 151 ? 13.998  -16.632 40.736  1.00 17.29  ? 151 ASP A CA  1 
ATOM   1202 C  C   . ASP A 1 151 ? 14.621  -15.942 39.513  1.00 15.85  ? 151 ASP A C   1 
ATOM   1203 O  O   . ASP A 1 151 ? 15.632  -16.383 38.971  1.00 14.29  ? 151 ASP A O   1 
ATOM   1204 C  CB  . ASP A 1 151 ? 12.875  -17.632 40.389  1.00 20.33  ? 151 ASP A CB  1 
ATOM   1205 C  CG  . ASP A 1 151 ? 12.714  -18.831 41.342  1.00 27.63  ? 151 ASP A CG  1 
ATOM   1206 O  OD1 . ASP A 1 151 ? 13.128  -18.744 42.517  1.00 28.32  ? 151 ASP A OD1 1 
ATOM   1207 O  OD2 . ASP A 1 151 ? 12.172  -19.891 40.903  1.00 29.08  ? 151 ASP A OD2 1 
ATOM   1208 N  N   . THR A 1 152 ? 14.060  -14.811 39.074  1.00 14.52  ? 152 THR A N   1 
ATOM   1209 C  CA  . THR A 1 152 ? 14.526  -14.170 37.854  1.00 12.79  ? 152 THR A CA  1 
ATOM   1210 C  C   . THR A 1 152 ? 15.943  -13.659 38.073  1.00 11.95  ? 152 THR A C   1 
ATOM   1211 O  O   . THR A 1 152 ? 16.756  -13.745 37.188  1.00 13.71  ? 152 THR A O   1 
ATOM   1212 C  CB  . THR A 1 152 ? 13.555  -13.055 37.411  1.00 13.10  ? 152 THR A CB  1 
ATOM   1213 O  OG1 . THR A 1 152 ? 12.289  -13.650 37.158  1.00 13.47  ? 152 THR A OG1 1 
ATOM   1214 C  CG2 . THR A 1 152 ? 13.982  -12.358 36.156  1.00 13.81  ? 152 THR A CG2 1 
ATOM   1215 N  N   . ILE A 1 153 ? 16.241  -13.094 39.236  1.00 12.65  ? 153 ILE A N   1 
ATOM   1216 C  CA  . ILE A 1 153 ? 17.532  -12.423 39.375  1.00 14.97  ? 153 ILE A CA  1 
ATOM   1217 C  C   . ILE A 1 153 ? 18.543  -13.524 39.622  1.00 14.17  ? 153 ILE A C   1 
ATOM   1218 O  O   . ILE A 1 153 ? 19.650  -13.452 39.126  1.00 16.12  ? 153 ILE A O   1 
ATOM   1219 C  CB  . ILE A 1 153 ? 17.603  -11.303 40.451  1.00 14.58  ? 153 ILE A CB  1 
ATOM   1220 C  CG1 . ILE A 1 153 ? 19.005  -10.685 40.540  1.00 15.00  ? 153 ILE A CG1 1 
ATOM   1221 C  CG2 . ILE A 1 153 ? 17.170  -11.764 41.825  1.00 16.05  ? 153 ILE A CG2 1 
ATOM   1222 C  CD1 . ILE A 1 153 ? 19.478  -10.025 39.274  1.00 16.49  ? 153 ILE A CD1 1 
ATOM   1223 N  N   . GLY A 1 154 ? 18.103  -14.590 40.314  1.00 14.85  ? 154 GLY A N   1 
ATOM   1224 C  CA  . GLY A 1 154 ? 18.985  -15.734 40.510  1.00 13.61  ? 154 GLY A CA  1 
ATOM   1225 C  C   . GLY A 1 154 ? 19.435  -16.303 39.182  1.00 12.18  ? 154 GLY A C   1 
ATOM   1226 O  O   . GLY A 1 154 ? 20.608  -16.582 39.002  1.00 13.48  ? 154 GLY A O   1 
ATOM   1227 N  N   . LEU A 1 155 ? 18.463  -16.597 38.316  1.00 12.67  ? 155 LEU A N   1 
ATOM   1228 C  CA  . LEU A 1 155 ? 18.737  -17.292 37.069  1.00 14.66  ? 155 LEU A CA  1 
ATOM   1229 C  C   . LEU A 1 155 ? 19.442  -16.379 36.072  1.00 17.01  ? 155 LEU A C   1 
ATOM   1230 O  O   . LEU A 1 155 ? 20.433  -16.780 35.487  1.00 17.01  ? 155 LEU A O   1 
ATOM   1231 C  CB  . LEU A 1 155 ? 17.438  -17.848 36.488  1.00 17.49  ? 155 LEU A CB  1 
ATOM   1232 C  CG  . LEU A 1 155 ? 17.565  -18.591 35.159  1.00 18.66  ? 155 LEU A CG  1 
ATOM   1233 C  CD1 . LEU A 1 155 ? 18.512  -19.767 35.255  1.00 20.94  ? 155 LEU A CD1 1 
ATOM   1234 C  CD2 . LEU A 1 155 ? 16.184  -19.101 34.748  1.00 19.60  ? 155 LEU A CD2 1 
ATOM   1235 N  N   . CYS A 1 156 ? 18.931  -15.163 35.860  1.00 16.23  ? 156 CYS A N   1 
ATOM   1236 C  CA  . CYS A 1 156 ? 19.490  -14.302 34.824  1.00 17.18  ? 156 CYS A CA  1 
ATOM   1237 C  C   . CYS A 1 156 ? 20.833  -13.756 35.280  1.00 16.48  ? 156 CYS A C   1 
ATOM   1238 O  O   . CYS A 1 156 ? 21.692  -13.535 34.443  1.00 18.56  ? 156 CYS A O   1 
ATOM   1239 C  CB  . CYS A 1 156 ? 18.665  -13.060 34.504  1.00 17.14  ? 156 CYS A CB  1 
ATOM   1240 S  SG  . CYS A 1 156 ? 16.991  -13.386 33.908  1.00 19.06  ? 156 CYS A SG  1 
ATOM   1241 N  N   . GLY A 1 157 ? 20.964  -13.516 36.596  1.00 18.29  ? 157 GLY A N   1 
ATOM   1242 C  CA  . GLY A 1 157 ? 22.159  -12.909 37.160  1.00 16.93  ? 157 GLY A CA  1 
ATOM   1243 C  C   . GLY A 1 157 ? 23.297  -13.913 37.324  1.00 16.63  ? 157 GLY A C   1 
ATOM   1244 O  O   . GLY A 1 157 ? 24.424  -13.596 36.983  1.00 16.74  ? 157 GLY A O   1 
ATOM   1245 N  N   . PHE A 1 158 ? 22.971  -15.098 37.852  1.00 16.18  ? 158 PHE A N   1 
ATOM   1246 C  CA  . PHE A 1 158 ? 23.948  -15.991 38.453  1.00 15.85  ? 158 PHE A CA  1 
ATOM   1247 C  C   . PHE A 1 158 ? 23.799  -17.440 38.014  1.00 17.17  ? 158 PHE A C   1 
ATOM   1248 O  O   . PHE A 1 158 ? 24.546  -18.292 38.510  1.00 16.58  ? 158 PHE A O   1 
ATOM   1249 C  CB  . PHE A 1 158 ? 23.813  -15.865 39.964  1.00 16.47  ? 158 PHE A CB  1 
ATOM   1250 C  CG  . PHE A 1 158 ? 23.986  -14.447 40.402  1.00 17.70  ? 158 PHE A CG  1 
ATOM   1251 C  CD1 . PHE A 1 158 ? 25.253  -13.916 40.526  1.00 16.23  ? 158 PHE A CD1 1 
ATOM   1252 C  CD2 . PHE A 1 158 ? 22.883  -13.640 40.652  1.00 19.68  ? 158 PHE A CD2 1 
ATOM   1253 C  CE1 . PHE A 1 158 ? 25.409  -12.573 40.851  1.00 17.42  ? 158 PHE A CE1 1 
ATOM   1254 C  CE2 . PHE A 1 158 ? 23.042  -12.302 40.994  1.00 20.31  ? 158 PHE A CE2 1 
ATOM   1255 C  CZ  . PHE A 1 158 ? 24.309  -11.783 41.136  1.00 18.01  ? 158 PHE A CZ  1 
ATOM   1256 N  N   . ASN A 1 159 ? 22.845  -17.707 37.121  1.00 18.66  ? 159 ASN A N   1 
ATOM   1257 C  CA  . ASN A 1 159 ? 22.512  -19.045 36.661  1.00 18.90  ? 159 ASN A CA  1 
ATOM   1258 C  C   . ASN A 1 159 ? 22.312  -19.966 37.861  1.00 18.97  ? 159 ASN A C   1 
ATOM   1259 O  O   . ASN A 1 159 ? 22.781  -21.116 37.900  1.00 17.74  ? 159 ASN A O   1 
ATOM   1260 C  CB  . ASN A 1 159 ? 23.604  -19.543 35.718  1.00 22.47  ? 159 ASN A CB  1 
ATOM   1261 C  CG  . ASN A 1 159 ? 23.129  -20.598 34.748  1.00 24.64  ? 159 ASN A CG  1 
ATOM   1262 O  OD1 . ASN A 1 159 ? 21.961  -20.671 34.390  1.00 25.49  ? 159 ASN A OD1 1 
ATOM   1263 N  ND2 . ASN A 1 159 ? 24.056  -21.404 34.277  1.00 30.16  ? 159 ASN A ND2 1 
ATOM   1264 N  N   . TYR A 1 160 ? 21.656  -19.408 38.867  1.00 18.20  ? 160 TYR A N   1 
ATOM   1265 C  CA  . TYR A 1 160 ? 21.300  -20.137 40.058  1.00 17.82  ? 160 TYR A CA  1 
ATOM   1266 C  C   . TYR A 1 160 ? 19.778  -20.204 40.095  1.00 18.60  ? 160 TYR A C   1 
ATOM   1267 O  O   . TYR A 1 160 ? 19.101  -19.225 39.818  1.00 16.32  ? 160 TYR A O   1 
ATOM   1268 C  CB  . TYR A 1 160 ? 21.881  -19.479 41.300  1.00 17.45  ? 160 TYR A CB  1 
ATOM   1269 C  CG  . TYR A 1 160 ? 21.629  -20.303 42.535  1.00 18.90  ? 160 TYR A CG  1 
ATOM   1270 C  CD1 . TYR A 1 160 ? 22.408  -21.422 42.794  1.00 21.32  ? 160 TYR A CD1 1 
ATOM   1271 C  CD2 . TYR A 1 160 ? 20.618  -19.988 43.429  1.00 18.65  ? 160 TYR A CD2 1 
ATOM   1272 C  CE1 . TYR A 1 160 ? 22.194  -22.190 43.917  1.00 19.49  ? 160 TYR A CE1 1 
ATOM   1273 C  CE2 . TYR A 1 160 ? 20.362  -20.787 44.527  1.00 19.90  ? 160 TYR A CE2 1 
ATOM   1274 C  CZ  . TYR A 1 160 ? 21.161  -21.892 44.762  1.00 20.54  ? 160 TYR A CZ  1 
ATOM   1275 O  OH  . TYR A 1 160 ? 20.981  -22.693 45.835  1.00 24.04  ? 160 TYR A OH  1 
ATOM   1276 N  N   . ARG A 1 161 ? 19.259  -21.385 40.434  1.00 18.02  ? 161 ARG A N   1 
ATOM   1277 C  CA  . ARG A 1 161 ? 17.830  -21.601 40.501  1.00 16.69  ? 161 ARG A CA  1 
ATOM   1278 C  C   . ARG A 1 161 ? 17.398  -21.739 41.960  1.00 16.34  ? 161 ARG A C   1 
ATOM   1279 O  O   . ARG A 1 161 ? 17.718  -22.706 42.635  1.00 17.13  ? 161 ARG A O   1 
ATOM   1280 C  CB  . ARG A 1 161 ? 17.470  -22.809 39.646  1.00 19.12  ? 161 ARG A CB  1 
ATOM   1281 C  CG  . ARG A 1 161 ? 17.460  -22.509 38.161  1.00 21.85  ? 161 ARG A CG  1 
ATOM   1282 C  CD  . ARG A 1 161 ? 17.014  -23.752 37.404  1.00 23.62  ? 161 ARG A CD  1 
ATOM   1283 N  NE  . ARG A 1 161 ? 16.331  -23.419 36.188  1.00 24.57  ? 161 ARG A NE  1 
ATOM   1284 C  CZ  . ARG A 1 161 ? 16.900  -23.092 35.068  1.00 27.25  ? 161 ARG A CZ  1 
ATOM   1285 N  NH1 . ARG A 1 161 ? 16.159  -22.843 34.012  1.00 21.52  ? 161 ARG A NH1 1 
ATOM   1286 N  NH2 . ARG A 1 161 ? 18.221  -23.033 35.007  1.00 43.07  ? 161 ARG A NH2 1 
ATOM   1287 N  N   . PHE A 1 162 ? 16.637  -20.748 42.425  1.00 13.75  ? 162 PHE A N   1 
ATOM   1288 C  CA  . PHE A 1 162 ? 16.044  -20.756 43.746  1.00 14.21  ? 162 PHE A CA  1 
ATOM   1289 C  C   . PHE A 1 162 ? 14.887  -21.750 43.806  1.00 14.31  ? 162 PHE A C   1 
ATOM   1290 O  O   . PHE A 1 162 ? 14.497  -22.142 44.898  1.00 15.10  ? 162 PHE A O   1 
ATOM   1291 C  CB  . PHE A 1 162 ? 15.571  -19.334 44.090  1.00 15.33  ? 162 PHE A CB  1 
ATOM   1292 C  CG  . PHE A 1 162 ? 16.707  -18.438 44.522  1.00 15.95  ? 162 PHE A CG  1 
ATOM   1293 C  CD1 . PHE A 1 162 ? 17.262  -18.582 45.778  1.00 15.96  ? 162 PHE A CD1 1 
ATOM   1294 C  CD2 . PHE A 1 162 ? 17.274  -17.545 43.636  1.00 17.49  ? 162 PHE A CD2 1 
ATOM   1295 C  CE1 . PHE A 1 162 ? 18.339  -17.807 46.169  1.00 18.87  ? 162 PHE A CE1 1 
ATOM   1296 C  CE2 . PHE A 1 162 ? 18.335  -16.750 44.034  1.00 19.21  ? 162 PHE A CE2 1 
ATOM   1297 C  CZ  . PHE A 1 162 ? 18.869  -16.888 45.289  1.00 17.86  ? 162 PHE A CZ  1 
ATOM   1298 N  N   . ASN A 1 163 ? 14.299  -22.057 42.647  1.00 13.77  ? 163 ASN A N   1 
ATOM   1299 C  CA  . ASN A 1 163 ? 13.216  -23.038 42.568  1.00 15.27  ? 163 ASN A CA  1 
ATOM   1300 C  C   . ASN A 1 163 ? 12.079  -22.688 43.537  1.00 16.10  ? 163 ASN A C   1 
ATOM   1301 O  O   . ASN A 1 163 ? 11.513  -23.545 44.225  1.00 16.94  ? 163 ASN A O   1 
ATOM   1302 C  CB  . ASN A 1 163 ? 13.799  -24.460 42.716  1.00 13.35  ? 163 ASN A CB  1 
ATOM   1303 C  CG  . ASN A 1 163 ? 14.543  -24.859 41.461  1.00 13.29  ? 163 ASN A CG  1 
ATOM   1304 O  OD1 . ASN A 1 163 ? 14.037  -24.638 40.358  1.00 14.65  ? 163 ASN A OD1 1 
ATOM   1305 N  ND2 . ASN A 1 163 ? 15.763  -25.370 41.564  1.00 12.91  ? 163 ASN A ND2 1 
ATOM   1306 N  N   . SER A 1 164 ? 11.710  -21.403 43.575  1.00 15.15  ? 164 SER A N   1 
ATOM   1307 C  CA  . SER A 1 164 ? 10.784  -20.882 44.566  1.00 14.49  ? 164 SER A CA  1 
ATOM   1308 C  C   . SER A 1 164 ? 9.346   -21.386 44.340  1.00 14.04  ? 164 SER A C   1 
ATOM   1309 O  O   . SER A 1 164 ? 8.570   -21.463 45.296  1.00 12.60  ? 164 SER A O   1 
ATOM   1310 C  CB  . SER A 1 164 ? 10.852  -19.379 44.539  1.00 15.61  ? 164 SER A CB  1 
ATOM   1311 O  OG  . SER A 1 164 ? 12.178  -18.950 44.856  1.00 17.32  ? 164 SER A OG  1 
ATOM   1312 N  N   . PHE A 1 165 ? 9.023   -21.748 43.093  1.00 14.70  ? 165 PHE A N   1 
ATOM   1313 C  CA  . PHE A 1 165 ? 7.705   -22.271 42.750  1.00 16.84  ? 165 PHE A CA  1 
ATOM   1314 C  C   . PHE A 1 165 ? 7.589   -23.738 43.180  1.00 18.96  ? 165 PHE A C   1 
ATOM   1315 O  O   . PHE A 1 165 ? 6.515   -24.322 43.010  1.00 21.07  ? 165 PHE A O   1 
ATOM   1316 C  CB  . PHE A 1 165 ? 7.406   -22.038 41.258  1.00 18.06  ? 165 PHE A CB  1 
ATOM   1317 C  CG  . PHE A 1 165 ? 7.107   -20.600 40.896  1.00 17.94  ? 165 PHE A CG  1 
ATOM   1318 C  CD1 . PHE A 1 165 ? 5.999   -19.949 41.420  1.00 19.62  ? 165 PHE A CD1 1 
ATOM   1319 C  CD2 . PHE A 1 165 ? 7.970   -19.877 40.083  1.00 20.28  ? 165 PHE A CD2 1 
ATOM   1320 C  CE1 . PHE A 1 165 ? 5.743   -18.628 41.118  1.00 18.88  ? 165 PHE A CE1 1 
ATOM   1321 C  CE2 . PHE A 1 165 ? 7.737   -18.544 39.800  1.00 18.87  ? 165 PHE A CE2 1 
ATOM   1322 C  CZ  . PHE A 1 165 ? 6.630   -17.915 40.329  1.00 20.30  ? 165 PHE A CZ  1 
ATOM   1323 N  N   . TYR A 1 166 ? 8.679   -24.355 43.681  1.00 16.74  ? 166 TYR A N   1 
ATOM   1324 C  CA  . TYR A 1 166 ? 8.600   -25.728 44.175  1.00 19.40  ? 166 TYR A CA  1 
ATOM   1325 C  C   . TYR A 1 166 ? 8.437   -25.716 45.690  1.00 20.13  ? 166 TYR A C   1 
ATOM   1326 O  O   . TYR A 1 166 ? 8.431   -26.765 46.311  1.00 22.25  ? 166 TYR A O   1 
ATOM   1327 C  CB  . TYR A 1 166 ? 9.799   -26.558 43.717  1.00 17.66  ? 166 TYR A CB  1 
ATOM   1328 C  CG  . TYR A 1 166 ? 9.829   -26.794 42.207  1.00 19.22  ? 166 TYR A CG  1 
ATOM   1329 C  CD1 . TYR A 1 166 ? 10.368  -25.859 41.335  1.00 17.20  ? 166 TYR A CD1 1 
ATOM   1330 C  CD2 . TYR A 1 166 ? 9.208   -27.908 41.631  1.00 16.48  ? 166 TYR A CD2 1 
ATOM   1331 C  CE1 . TYR A 1 166 ? 10.376  -26.068 39.958  1.00 18.84  ? 166 TYR A CE1 1 
ATOM   1332 C  CE2 . TYR A 1 166 ? 9.180   -28.104 40.255  1.00 15.24  ? 166 TYR A CE2 1 
ATOM   1333 C  CZ  . TYR A 1 166 ? 9.761   -27.183 39.403  1.00 15.97  ? 166 TYR A CZ  1 
ATOM   1334 O  OH  . TYR A 1 166 ? 9.734   -27.324 38.029  1.00 16.85  ? 166 TYR A OH  1 
ATOM   1335 N  N   . ARG A 1 167 ? 8.295   -24.528 46.286  1.00 21.41  ? 167 ARG A N   1 
ATOM   1336 C  CA  . ARG A 1 167 ? 8.296   -24.382 47.735  1.00 23.21  ? 167 ARG A CA  1 
ATOM   1337 C  C   . ARG A 1 167 ? 7.013   -23.708 48.210  1.00 27.55  ? 167 ARG A C   1 
ATOM   1338 O  O   . ARG A 1 167 ? 6.464   -22.859 47.504  1.00 27.62  ? 167 ARG A O   1 
ATOM   1339 C  CB  . ARG A 1 167 ? 9.470   -23.505 48.178  1.00 23.52  ? 167 ARG A CB  1 
ATOM   1340 C  CG  . ARG A 1 167 ? 10.825  -23.938 47.660  1.00 25.10  ? 167 ARG A CG  1 
ATOM   1341 C  CD  . ARG A 1 167 ? 11.909  -22.901 47.926  1.00 25.62  ? 167 ARG A CD  1 
ATOM   1342 N  NE  . ARG A 1 167 ? 13.177  -23.422 47.405  1.00 28.32  ? 167 ARG A NE  1 
ATOM   1343 C  CZ  . ARG A 1 167 ? 14.156  -23.935 48.153  1.00 29.67  ? 167 ARG A CZ  1 
ATOM   1344 N  NH1 . ARG A 1 167 ? 13.988  -24.056 49.458  1.00 29.50  ? 167 ARG A NH1 1 
ATOM   1345 N  NH2 . ARG A 1 167 ? 15.303  -24.312 47.602  1.00 27.05  ? 167 ARG A NH2 1 
ATOM   1346 N  N   . ASP A 1 168 ? 6.575   -24.087 49.419  1.00 30.12  ? 168 ASP A N   1 
ATOM   1347 C  CA  . ASP A 1 168 ? 5.521   -23.409 50.160  1.00 38.92  ? 168 ASP A CA  1 
ATOM   1348 C  C   . ASP A 1 168 ? 6.120   -22.217 50.898  1.00 41.39  ? 168 ASP A C   1 
ATOM   1349 O  O   . ASP A 1 168 ? 5.531   -21.148 50.946  1.00 46.30  ? 168 ASP A O   1 
ATOM   1350 C  CB  . ASP A 1 168 ? 4.893   -24.310 51.234  1.00 46.00  ? 168 ASP A CB  1 
ATOM   1351 C  CG  . ASP A 1 168 ? 3.870   -25.317 50.740  1.00 50.24  ? 168 ASP A CG  1 
ATOM   1352 O  OD1 . ASP A 1 168 ? 2.783   -24.883 50.293  1.00 54.56  ? 168 ASP A OD1 1 
ATOM   1353 O  OD2 . ASP A 1 168 ? 4.155   -26.532 50.853  1.00 54.50  ? 168 ASP A OD2 1 
ATOM   1354 N  N   . GLN A 1 169 ? 7.284   -22.440 51.506  1.00 41.87  ? 169 GLN A N   1 
ATOM   1355 C  CA  . GLN A 1 169 ? 7.924   -21.464 52.369  1.00 47.17  ? 169 GLN A CA  1 
ATOM   1356 C  C   . GLN A 1 169 ? 8.977   -20.724 51.555  1.00 43.77  ? 169 GLN A C   1 
ATOM   1357 O  O   . GLN A 1 169 ? 9.559   -21.298 50.631  1.00 42.90  ? 169 GLN A O   1 
ATOM   1358 C  CB  . GLN A 1 169 ? 8.586   -22.167 53.554  1.00 52.31  ? 169 GLN A CB  1 
ATOM   1359 C  CG  . GLN A 1 169 ? 7.607   -22.971 54.398  1.00 58.39  ? 169 GLN A CG  1 
ATOM   1360 C  CD  . GLN A 1 169 ? 6.726   -22.082 55.243  1.00 61.90  ? 169 GLN A CD  1 
ATOM   1361 O  OE1 . GLN A 1 169 ? 7.202   -21.390 56.141  1.00 65.99  ? 169 GLN A OE1 1 
ATOM   1362 N  NE2 . GLN A 1 169 ? 5.430   -22.103 54.973  1.00 64.04  ? 169 GLN A NE2 1 
ATOM   1363 N  N   . PRO A 1 170 ? 9.253   -19.435 51.835  1.00 37.56  ? 170 PRO A N   1 
ATOM   1364 C  CA  . PRO A 1 170 ? 10.276  -18.729 51.063  1.00 36.41  ? 170 PRO A CA  1 
ATOM   1365 C  C   . PRO A 1 170 ? 11.594  -19.503 51.168  1.00 36.06  ? 170 PRO A C   1 
ATOM   1366 O  O   . PRO A 1 170 ? 11.789  -20.271 52.122  1.00 31.42  ? 170 PRO A O   1 
ATOM   1367 C  CB  . PRO A 1 170 ? 10.287  -17.328 51.708  1.00 40.77  ? 170 PRO A CB  1 
ATOM   1368 C  CG  . PRO A 1 170 ? 8.906   -17.185 52.344  1.00 38.65  ? 170 PRO A CG  1 
ATOM   1369 C  CD  . PRO A 1 170 ? 8.580   -18.582 52.834  1.00 39.47  ? 170 PRO A CD  1 
ATOM   1370 N  N   . HIS A 1 171 ? 12.469  -19.333 50.160  1.00 32.38  ? 171 HIS A N   1 
ATOM   1371 C  CA  . HIS A 1 171 ? 13.809  -19.915 50.167  1.00 30.41  ? 171 HIS A CA  1 
ATOM   1372 C  C   . HIS A 1 171 ? 14.588  -19.428 51.392  1.00 31.25  ? 171 HIS A C   1 
ATOM   1373 O  O   . HIS A 1 171 ? 14.440  -18.275 51.793  1.00 31.27  ? 171 HIS A O   1 
ATOM   1374 C  CB  . HIS A 1 171 ? 14.526  -19.590 48.852  1.00 27.52  ? 171 HIS A CB  1 
ATOM   1375 C  CG  . HIS A 1 171 ? 15.833  -20.289 48.655  1.00 28.34  ? 171 HIS A CG  1 
ATOM   1376 N  ND1 . HIS A 1 171 ? 16.950  -20.064 49.431  1.00 30.10  ? 171 HIS A ND1 1 
ATOM   1377 C  CD2 . HIS A 1 171 ? 16.224  -21.149 47.711  1.00 26.03  ? 171 HIS A CD2 1 
ATOM   1378 C  CE1 . HIS A 1 171 ? 17.962  -20.786 48.977  1.00 25.98  ? 171 HIS A CE1 1 
ATOM   1379 N  NE2 . HIS A 1 171 ? 17.546  -21.452 47.928  1.00 23.60  ? 171 HIS A NE2 1 
ATOM   1380 N  N   . PRO A 1 172 ? 15.431  -20.265 52.047  1.00 36.68  ? 172 PRO A N   1 
ATOM   1381 C  CA  . PRO A 1 172 ? 16.161  -19.832 53.250  1.00 39.13  ? 172 PRO A CA  1 
ATOM   1382 C  C   . PRO A 1 172 ? 16.940  -18.523 53.113  1.00 39.04  ? 172 PRO A C   1 
ATOM   1383 O  O   . PRO A 1 172 ? 17.022  -17.738 54.062  1.00 41.10  ? 172 PRO A O   1 
ATOM   1384 C  CB  . PRO A 1 172 ? 17.131  -20.992 53.512  1.00 38.79  ? 172 PRO A CB  1 
ATOM   1385 C  CG  . PRO A 1 172 ? 16.404  -22.197 52.966  1.00 37.17  ? 172 PRO A CG  1 
ATOM   1386 C  CD  . PRO A 1 172 ? 15.652  -21.689 51.748  1.00 35.35  ? 172 PRO A CD  1 
ATOM   1387 N  N   . PHE A 1 173 ? 17.517  -18.292 51.929  1.00 38.07  ? 173 PHE A N   1 
ATOM   1388 C  CA  . PHE A 1 173 ? 18.163  -17.023 51.636  1.00 35.91  ? 173 PHE A CA  1 
ATOM   1389 C  C   . PHE A 1 173 ? 17.228  -15.849 51.913  1.00 34.64  ? 173 PHE A C   1 
ATOM   1390 O  O   . PHE A 1 173 ? 17.649  -14.858 52.506  1.00 34.30  ? 173 PHE A O   1 
ATOM   1391 C  CB  . PHE A 1 173 ? 18.627  -16.932 50.180  1.00 36.69  ? 173 PHE A CB  1 
ATOM   1392 C  CG  . PHE A 1 173 ? 19.400  -15.669 49.879  1.00 33.42  ? 173 PHE A CG  1 
ATOM   1393 C  CD1 . PHE A 1 173 ? 20.749  -15.569 50.191  1.00 35.03  ? 173 PHE A CD1 1 
ATOM   1394 C  CD2 . PHE A 1 173 ? 18.766  -14.564 49.335  1.00 32.62  ? 173 PHE A CD2 1 
ATOM   1395 C  CE1 . PHE A 1 173 ? 21.457  -14.406 49.916  1.00 34.41  ? 173 PHE A CE1 1 
ATOM   1396 C  CE2 . PHE A 1 173 ? 19.463  -13.394 49.080  1.00 33.14  ? 173 PHE A CE2 1 
ATOM   1397 C  CZ  . PHE A 1 173 ? 20.806  -13.313 49.379  1.00 32.94  ? 173 PHE A CZ  1 
ATOM   1398 N  N   . ILE A 1 174 ? 15.976  -15.923 51.454  1.00 33.16  ? 174 ILE A N   1 
ATOM   1399 C  CA  . ILE A 1 174 ? 15.089  -14.776 51.597  1.00 40.81  ? 174 ILE A CA  1 
ATOM   1400 C  C   . ILE A 1 174 ? 14.547  -14.721 53.027  1.00 41.11  ? 174 ILE A C   1 
ATOM   1401 O  O   . ILE A 1 174 ? 14.233  -13.646 53.534  1.00 48.56  ? 174 ILE A O   1 
ATOM   1402 C  CB  . ILE A 1 174 ? 13.981  -14.710 50.514  1.00 44.91  ? 174 ILE A CB  1 
ATOM   1403 C  CG1 . ILE A 1 174 ? 12.678  -14.105 51.060  1.00 49.82  ? 174 ILE A CG1 1 
ATOM   1404 C  CG2 . ILE A 1 174 ? 13.728  -16.062 49.864  1.00 47.27  ? 174 ILE A CG2 1 
ATOM   1405 C  CD1 . ILE A 1 174 ? 11.608  -13.840 50.005  1.00 54.34  ? 174 ILE A CD1 1 
ATOM   1406 N  N   . THR A 1 175 ? 14.456  -15.866 53.696  1.00 38.65  ? 175 THR A N   1 
ATOM   1407 C  CA  . THR A 1 175 ? 13.975  -15.876 55.066  1.00 39.33  ? 175 THR A CA  1 
ATOM   1408 C  C   . THR A 1 175 ? 14.948  -15.102 55.948  1.00 34.23  ? 175 THR A C   1 
ATOM   1409 O  O   . THR A 1 175 ? 14.522  -14.359 56.831  1.00 34.15  ? 175 THR A O   1 
ATOM   1410 C  CB  . THR A 1 175 ? 13.777  -17.312 55.567  1.00 40.95  ? 175 THR A CB  1 
ATOM   1411 O  OG1 . THR A 1 175 ? 12.860  -17.943 54.675  1.00 43.47  ? 175 THR A OG1 1 
ATOM   1412 C  CG2 . THR A 1 175 ? 13.233  -17.386 56.977  1.00 42.11  ? 175 THR A CG2 1 
ATOM   1413 N  N   . SER A 1 176 ? 16.241  -15.300 55.679  1.00 33.44  ? 176 SER A N   1 
ATOM   1414 C  CA  . SER A 1 176 ? 17.330  -14.752 56.469  1.00 33.82  ? 176 SER A CA  1 
ATOM   1415 C  C   . SER A 1 176 ? 17.571  -13.294 56.116  1.00 35.82  ? 176 SER A C   1 
ATOM   1416 O  O   . SER A 1 176 ? 17.869  -12.478 56.980  1.00 33.27  ? 176 SER A O   1 
ATOM   1417 C  CB  . SER A 1 176 ? 18.571  -15.543 56.248  1.00 34.57  ? 176 SER A CB  1 
ATOM   1418 O  OG  . SER A 1 176 ? 18.398  -16.875 56.693  1.00 36.83  ? 176 SER A OG  1 
ATOM   1419 N  N   . MET A 1 177 ? 17.454  -12.984 54.826  1.00 35.64  ? 177 MET A N   1 
ATOM   1420 C  CA  . MET A 1 177 ? 17.584  -11.618 54.375  1.00 41.17  ? 177 MET A CA  1 
ATOM   1421 C  C   . MET A 1 177 ? 16.478  -10.779 55.014  1.00 39.99  ? 177 MET A C   1 
ATOM   1422 O  O   . MET A 1 177 ? 16.743  -9.661  55.454  1.00 42.19  ? 177 MET A O   1 
ATOM   1423 C  CB  . MET A 1 177 ? 17.528  -11.554 52.841  1.00 46.77  ? 177 MET A CB  1 
ATOM   1424 C  CG  . MET A 1 177 ? 17.309  -10.162 52.272  1.00 54.20  ? 177 MET A CG  1 
ATOM   1425 S  SD  . MET A 1 177 ? 18.175  -9.929  50.708  1.00 65.11  ? 177 MET A SD  1 
ATOM   1426 C  CE  . MET A 1 177 ? 19.855  -9.681  51.284  1.00 63.30  ? 177 MET A CE  1 
ATOM   1427 N  N   . VAL A 1 178 ? 15.257  -11.330 55.084  1.00 36.95  ? 178 VAL A N   1 
ATOM   1428 C  CA  . VAL A 1 178 ? 14.113  -10.612 55.627  1.00 38.59  ? 178 VAL A CA  1 
ATOM   1429 C  C   . VAL A 1 178 ? 14.248  -10.449 57.144  1.00 38.05  ? 178 VAL A C   1 
ATOM   1430 O  O   . VAL A 1 178 ? 13.964  -9.376  57.684  1.00 36.98  ? 178 VAL A O   1 
ATOM   1431 C  CB  . VAL A 1 178 ? 12.787  -11.305 55.255  1.00 40.10  ? 178 VAL A CB  1 
ATOM   1432 C  CG1 . VAL A 1 178 ? 11.645  -10.903 56.188  1.00 38.80  ? 178 VAL A CG1 1 
ATOM   1433 C  CG2 . VAL A 1 178 ? 12.426  -11.034 53.796  1.00 40.63  ? 178 VAL A CG2 1 
ATOM   1434 N  N   . ARG A 1 179 ? 14.677  -11.518 57.813  1.00 35.48  ? 179 ARG A N   1 
ATOM   1435 C  CA  . ARG A 1 179 ? 14.854  -11.520 59.259  1.00 38.03  ? 179 ARG A CA  1 
ATOM   1436 C  C   . ARG A 1 179 ? 16.008  -10.588 59.640  1.00 33.86  ? 179 ARG A C   1 
ATOM   1437 O  O   . ARG A 1 179 ? 15.993  -10.011 60.728  1.00 38.63  ? 179 ARG A O   1 
ATOM   1438 C  CB  . ARG A 1 179 ? 15.121  -12.939 59.778  1.00 40.49  ? 179 ARG A CB  1 
ATOM   1439 C  CG  . ARG A 1 179 ? 14.629  -13.194 61.196  1.00 43.96  ? 179 ARG A CG  1 
ATOM   1440 C  CD  . ARG A 1 179 ? 15.533  -14.111 62.001  1.00 46.43  ? 179 ARG A CD  1 
ATOM   1441 N  NE  . ARG A 1 179 ? 16.048  -15.232 61.232  1.00 48.99  ? 179 ARG A NE  1 
ATOM   1442 C  CZ  . ARG A 1 179 ? 15.307  -16.218 60.741  1.00 50.74  ? 179 ARG A CZ  1 
ATOM   1443 N  NH1 . ARG A 1 179 ? 14.033  -16.319 61.076  1.00 55.17  ? 179 ARG A NH1 1 
ATOM   1444 N  NH2 . ARG A 1 179 ? 15.849  -17.119 59.941  1.00 47.09  ? 179 ARG A NH2 1 
ATOM   1445 N  N   . ALA A 1 180 ? 17.011  -10.455 58.764  1.00 31.81  ? 180 ALA A N   1 
ATOM   1446 C  CA  . ALA A 1 180 ? 18.169  -9.607  59.043  1.00 30.86  ? 180 ALA A CA  1 
ATOM   1447 C  C   . ALA A 1 180 ? 17.779  -8.132  58.929  1.00 34.42  ? 180 ALA A C   1 
ATOM   1448 O  O   . ALA A 1 180 ? 18.245  -7.312  59.715  1.00 31.61  ? 180 ALA A O   1 
ATOM   1449 C  CB  . ALA A 1 180 ? 19.315  -9.956  58.117  1.00 29.15  ? 180 ALA A CB  1 
ATOM   1450 N  N   . LEU A 1 181 ? 16.918  -7.817  57.950  1.00 34.20  ? 181 LEU A N   1 
ATOM   1451 C  CA  . LEU A 1 181 ? 16.490  -6.461  57.678  1.00 38.04  ? 181 LEU A CA  1 
ATOM   1452 C  C   . LEU A 1 181 ? 15.496  -6.008  58.743  1.00 41.27  ? 181 LEU A C   1 
ATOM   1453 O  O   . LEU A 1 181 ? 15.507  -4.844  59.132  1.00 42.39  ? 181 LEU A O   1 
ATOM   1454 C  CB  . LEU A 1 181 ? 15.902  -6.414  56.263  1.00 39.73  ? 181 LEU A CB  1 
ATOM   1455 C  CG  . LEU A 1 181 ? 16.946  -6.475  55.144  1.00 42.35  ? 181 LEU A CG  1 
ATOM   1456 C  CD1 . LEU A 1 181 ? 16.308  -6.622  53.764  1.00 44.70  ? 181 LEU A CD1 1 
ATOM   1457 C  CD2 . LEU A 1 181 ? 17.840  -5.252  55.172  1.00 41.29  ? 181 LEU A CD2 1 
ATOM   1458 N  N   . ASP A 1 182 ? 14.673  -6.949  59.227  1.00 45.54  ? 182 ASP A N   1 
ATOM   1459 C  CA  . ASP A 1 182 ? 13.796  -6.731  60.368  1.00 49.86  ? 182 ASP A CA  1 
ATOM   1460 C  C   . ASP A 1 182 ? 14.611  -6.423  61.634  1.00 42.99  ? 182 ASP A C   1 
ATOM   1461 O  O   . ASP A 1 182 ? 14.259  -5.530  62.398  1.00 42.53  ? 182 ASP A O   1 
ATOM   1462 C  CB  . ASP A 1 182 ? 12.866  -7.936  60.574  1.00 54.27  ? 182 ASP A CB  1 
ATOM   1463 C  CG  . ASP A 1 182 ? 11.930  -7.793  61.767  1.00 59.89  ? 182 ASP A CG  1 
ATOM   1464 O  OD1 . ASP A 1 182 ? 11.331  -6.701  61.917  1.00 61.25  ? 182 ASP A OD1 1 
ATOM   1465 O  OD2 . ASP A 1 182 ? 11.799  -8.775  62.538  1.00 62.93  ? 182 ASP A OD2 1 
ATOM   1466 N  N   . GLU A 1 183 ? 15.709  -7.148  61.857  1.00 38.74  ? 183 GLU A N   1 
ATOM   1467 C  CA  . GLU A 1 183 ? 16.554  -6.897  63.018  1.00 40.80  ? 183 GLU A CA  1 
ATOM   1468 C  C   . GLU A 1 183 ? 17.186  -5.501  62.900  1.00 43.71  ? 183 GLU A C   1 
ATOM   1469 O  O   . GLU A 1 183 ? 17.483  -4.844  63.904  1.00 42.18  ? 183 GLU A O   1 
ATOM   1470 C  CB  . GLU A 1 183 ? 17.568  -8.037  63.156  1.00 38.29  ? 183 GLU A CB  1 
ATOM   1471 C  CG  . GLU A 1 183 ? 18.846  -7.659  63.882  1.00 41.51  ? 183 GLU A CG  1 
ATOM   1472 C  CD  . GLU A 1 183 ? 18.680  -7.370  65.366  1.00 45.29  ? 183 GLU A CD  1 
ATOM   1473 O  OE1 . GLU A 1 183 ? 19.714  -7.185  66.062  1.00 51.95  ? 183 GLU A OE1 1 
ATOM   1474 O  OE2 . GLU A 1 183 ? 17.531  -7.360  65.837  1.00 44.33  ? 183 GLU A OE2 1 
ATOM   1475 N  N   . ILE A 1 184 ? 17.400  -5.048  61.659  1.00 40.38  ? 184 ILE A N   1 
ATOM   1476 C  CA  . ILE A 1 184 ? 17.898  -3.702  61.401  1.00 39.41  ? 184 ILE A CA  1 
ATOM   1477 C  C   . ILE A 1 184 ? 16.821  -2.685  61.786  1.00 37.43  ? 184 ILE A C   1 
ATOM   1478 O  O   . ILE A 1 184 ? 17.113  -1.743  62.523  1.00 35.96  ? 184 ILE A O   1 
ATOM   1479 C  CB  . ILE A 1 184 ? 18.382  -3.576  59.938  1.00 36.42  ? 184 ILE A CB  1 
ATOM   1480 C  CG1 . ILE A 1 184 ? 19.738  -4.266  59.777  1.00 34.27  ? 184 ILE A CG1 1 
ATOM   1481 C  CG2 . ILE A 1 184 ? 18.414  -2.126  59.478  1.00 39.58  ? 184 ILE A CG2 1 
ATOM   1482 C  CD1 . ILE A 1 184 ? 20.127  -4.584  58.358  1.00 37.06  ? 184 ILE A CD1 1 
ATOM   1483 N  N   . MET A 1 185 ? 15.592  -2.917  61.309  1.00 38.70  ? 185 MET A N   1 
ATOM   1484 C  CA  . MET A 1 185 ? 14.429  -2.091  61.607  1.00 45.60  ? 185 MET A CA  1 
ATOM   1485 C  C   . MET A 1 185 ? 14.244  -1.914  63.114  1.00 43.52  ? 185 MET A C   1 
ATOM   1486 O  O   . MET A 1 185 ? 14.036  -0.799  63.575  1.00 43.93  ? 185 MET A O   1 
ATOM   1487 C  CB  . MET A 1 185 ? 13.149  -2.708  61.023  1.00 49.57  ? 185 MET A CB  1 
ATOM   1488 C  CG  . MET A 1 185 ? 12.417  -1.810  60.050  1.00 56.15  ? 185 MET A CG  1 
ATOM   1489 S  SD  . MET A 1 185 ? 13.551  -0.967  58.908  1.00 75.79  ? 185 MET A SD  1 
ATOM   1490 C  CE  . MET A 1 185 ? 12.916  0.708   59.003  1.00 68.16  ? 185 MET A CE  1 
ATOM   1491 N  N   . ASN A 1 186 ? 14.305  -3.016  63.870  1.00 43.29  ? 186 ASN A N   1 
ATOM   1492 C  CA  . ASN A 1 186 ? 14.201  -2.964  65.322  1.00 40.65  ? 186 ASN A CA  1 
ATOM   1493 C  C   . ASN A 1 186 ? 15.410  -2.256  65.938  1.00 42.32  ? 186 ASN A C   1 
ATOM   1494 O  O   . ASN A 1 186 ? 15.229  -1.447  66.850  1.00 42.55  ? 186 ASN A O   1 
ATOM   1495 C  CB  . ASN A 1 186 ? 13.996  -4.351  65.922  1.00 41.90  ? 186 ASN A CB  1 
ATOM   1496 C  CG  . ASN A 1 186 ? 12.724  -4.979  65.402  1.00 46.90  ? 186 ASN A CG  1 
ATOM   1497 O  OD1 . ASN A 1 186 ? 11.701  -4.306  65.315  1.00 54.84  ? 186 ASN A OD1 1 
ATOM   1498 N  ND2 . ASN A 1 186 ? 12.788  -6.237  64.996  1.00 53.58  ? 186 ASN A ND2 1 
ATOM   1499 N  N   . LYS A 1 187 ? 16.625  -2.507  65.422  1.00 37.65  ? 187 LYS A N   1 
ATOM   1500 C  CA  . LYS A 1 187 ? 17.810  -1.826  65.936  1.00 42.25  ? 187 LYS A CA  1 
ATOM   1501 C  C   . LYS A 1 187 ? 17.712  -0.308  65.773  1.00 40.53  ? 187 LYS A C   1 
ATOM   1502 O  O   . LYS A 1 187 ? 18.283  0.404   66.589  1.00 45.94  ? 187 LYS A O   1 
ATOM   1503 C  CB  . LYS A 1 187 ? 19.106  -2.321  65.287  1.00 44.63  ? 187 LYS A CB  1 
ATOM   1504 C  CG  . LYS A 1 187 ? 20.385  -1.741  65.878  1.00 44.20  ? 187 LYS A CG  1 
ATOM   1505 C  CD  . LYS A 1 187 ? 21.642  -2.393  65.347  1.00 47.02  ? 187 LYS A CD  1 
ATOM   1506 C  CE  . LYS A 1 187 ? 21.518  -2.811  63.897  1.00 50.79  ? 187 LYS A CE  1 
ATOM   1507 N  NZ  . LYS A 1 187 ? 22.814  -3.247  63.341  1.00 55.81  ? 187 LYS A NZ  1 
ATOM   1508 N  N   . LEU A 1 188 ? 16.960  0.195   64.783  1.00 38.20  ? 188 LEU A N   1 
ATOM   1509 C  CA  . LEU A 1 188 ? 16.833  1.636   64.576  1.00 42.77  ? 188 LEU A CA  1 
ATOM   1510 C  C   . LEU A 1 188 ? 16.027  2.304   65.693  1.00 45.84  ? 188 LEU A C   1 
ATOM   1511 O  O   . LEU A 1 188 ? 15.832  3.522   65.649  1.00 57.33  ? 188 LEU A O   1 
ATOM   1512 C  CB  . LEU A 1 188 ? 16.157  1.918   63.226  1.00 40.58  ? 188 LEU A CB  1 
ATOM   1513 C  CG  . LEU A 1 188 ? 16.978  1.645   61.966  1.00 39.83  ? 188 LEU A CG  1 
ATOM   1514 C  CD1 . LEU A 1 188 ? 16.186  2.002   60.712  1.00 39.48  ? 188 LEU A CD1 1 
ATOM   1515 C  CD2 . LEU A 1 188 ? 18.292  2.412   61.987  1.00 39.14  ? 188 LEU A CD2 1 
ATOM   1516 N  N   . GLN A 1 189 ? 15.559  1.526   66.684  1.00 45.11  ? 189 GLN A N   1 
ATOM   1517 C  CA  . GLN A 1 189 ? 14.712  2.043   67.755  1.00 43.87  ? 189 GLN A CA  1 
ATOM   1518 C  C   . GLN A 1 189 ? 15.255  1.732   69.157  1.00 44.21  ? 189 GLN A C   1 
ATOM   1519 O  O   . GLN A 1 189 ? 14.704  2.205   70.146  1.00 44.08  ? 189 GLN A O   1 
ATOM   1520 C  CB  . GLN A 1 189 ? 13.294  1.491   67.574  1.00 41.86  ? 189 GLN A CB  1 
ATOM   1521 C  CG  . GLN A 1 189 ? 12.492  2.198   66.492  1.00 39.64  ? 189 GLN A CG  1 
ATOM   1522 C  CD  . GLN A 1 189 ? 12.281  3.649   66.857  1.00 41.80  ? 189 GLN A CD  1 
ATOM   1523 O  OE1 . GLN A 1 189 ? 12.074  3.980   68.031  1.00 40.87  ? 189 GLN A OE1 1 
ATOM   1524 N  NE2 . GLN A 1 189 ? 12.370  4.531   65.868  1.00 32.71  ? 189 GLN A NE2 1 
ATOM   1525 N  N   . ARG A 1 190 ? 16.373  1.007   69.272  1.00 48.29  ? 190 ARG A N   1 
ATOM   1526 C  CA  . ARG A 1 190 ? 16.791  0.486   70.569  1.00 54.80  ? 190 ARG A CA  1 
ATOM   1527 C  C   . ARG A 1 190 ? 17.655  1.511   71.309  1.00 56.13  ? 190 ARG A C   1 
ATOM   1528 O  O   . ARG A 1 190 ? 18.627  2.028   70.761  1.00 62.02  ? 190 ARG A O   1 
ATOM   1529 C  CB  . ARG A 1 190 ? 17.492  -0.866  70.387  1.00 52.40  ? 190 ARG A CB  1 
ATOM   1530 C  CG  . ARG A 1 190 ? 16.713  -1.789  69.461  1.00 56.35  ? 190 ARG A CG  1 
ATOM   1531 C  CD  . ARG A 1 190 ? 16.712  -3.264  69.790  1.00 51.28  ? 190 ARG A CD  1 
ATOM   1532 N  NE  . ARG A 1 190 ? 17.965  -3.902  69.423  1.00 53.23  ? 190 ARG A NE  1 
ATOM   1533 C  CZ  . ARG A 1 190 ? 18.090  -4.883  68.537  1.00 51.15  ? 190 ARG A CZ  1 
ATOM   1534 N  NH1 . ARG A 1 190 ? 19.298  -5.292  68.194  1.00 50.13  ? 190 ARG A NH1 1 
ATOM   1535 N  NH2 . ARG A 1 190 ? 17.021  -5.409  67.960  1.00 48.67  ? 190 ARG A NH2 1 
ATOM   1536 N  N   . ALA A 1 191 ? 17.314  1.748   72.582  1.00 58.17  ? 191 ALA A N   1 
ATOM   1537 C  CA  . ALA A 1 191 ? 17.874  2.841   73.362  1.00 63.11  ? 191 ALA A CA  1 
ATOM   1538 C  C   . ALA A 1 191 ? 19.302  2.520   73.819  1.00 69.71  ? 191 ALA A C   1 
ATOM   1539 O  O   . ALA A 1 191 ? 20.184  3.379   73.745  1.00 63.85  ? 191 ALA A O   1 
ATOM   1540 C  CB  . ALA A 1 191 ? 16.948  3.142   74.522  1.00 58.64  ? 191 ALA A CB  1 
ATOM   1541 N  N   . ASN A 1 192 ? 19.510  1.287   74.314  1.00 77.94  ? 192 ASN A N   1 
ATOM   1542 C  CA  . ASN A 1 192 ? 20.836  0.743   74.592  1.00 75.14  ? 192 ASN A CA  1 
ATOM   1543 C  C   . ASN A 1 192 ? 21.033  -0.548  73.791  1.00 79.19  ? 192 ASN A C   1 
ATOM   1544 O  O   . ASN A 1 192 ? 20.729  -1.640  74.273  1.00 84.57  ? 192 ASN A O   1 
ATOM   1545 C  CB  . ASN A 1 192 ? 21.056  0.508   76.093  1.00 69.31  ? 192 ASN A CB  1 
ATOM   1546 C  CG  . ASN A 1 192 ? 21.799  1.630   76.793  1.00 66.44  ? 192 ASN A CG  1 
ATOM   1547 O  OD1 . ASN A 1 192 ? 22.407  2.495   76.166  1.00 56.08  ? 192 ASN A OD1 1 
ATOM   1548 N  ND2 . ASN A 1 192 ? 21.790  1.598   78.113  1.00 66.69  ? 192 ASN A ND2 1 
ATOM   1549 N  N   . PRO A 1 193 ? 21.532  -0.467  72.533  1.00 77.77  ? 193 PRO A N   1 
ATOM   1550 C  CA  . PRO A 1 193 ? 21.779  -1.656  71.711  1.00 78.88  ? 193 PRO A CA  1 
ATOM   1551 C  C   . PRO A 1 193 ? 22.555  -2.803  72.366  1.00 80.73  ? 193 PRO A C   1 
ATOM   1552 O  O   . PRO A 1 193 ? 22.307  -3.965  72.043  1.00 83.76  ? 193 PRO A O   1 
ATOM   1553 C  CB  . PRO A 1 193 ? 22.618  -1.102  70.544  1.00 76.28  ? 193 PRO A CB  1 
ATOM   1554 C  CG  . PRO A 1 193 ? 22.165  0.341   70.403  1.00 75.00  ? 193 PRO A CG  1 
ATOM   1555 C  CD  . PRO A 1 193 ? 21.839  0.784   71.815  1.00 76.95  ? 193 PRO A CD  1 
ATOM   1556 N  N   . ASP A 1 194 ? 23.490  -2.473  73.275  1.00 76.95  ? 194 ASP A N   1 
ATOM   1557 C  CA  . ASP A 1 194 ? 24.439  -3.440  73.818  1.00 73.13  ? 194 ASP A CA  1 
ATOM   1558 C  C   . ASP A 1 194 ? 23.883  -4.172  75.039  1.00 68.82  ? 194 ASP A C   1 
ATOM   1559 O  O   . ASP A 1 194 ? 24.543  -5.069  75.566  1.00 63.54  ? 194 ASP A O   1 
ATOM   1560 C  CB  . ASP A 1 194 ? 25.759  -2.762  74.186  1.00 71.10  ? 194 ASP A CB  1 
ATOM   1561 C  CG  . ASP A 1 194 ? 26.509  -2.271  72.966  1.00 71.37  ? 194 ASP A CG  1 
ATOM   1562 O  OD1 . ASP A 1 194 ? 27.164  -3.109  72.308  1.00 62.16  ? 194 ASP A OD1 1 
ATOM   1563 O  OD2 . ASP A 1 194 ? 26.386  -1.066  72.660  1.00 67.71  ? 194 ASP A OD2 1 
ATOM   1564 N  N   . ASP A 1 195 ? 22.681  -3.772  75.478  1.00 68.31  ? 195 ASP A N   1 
ATOM   1565 C  CA  . ASP A 1 195 ? 21.928  -4.472  76.507  1.00 69.54  ? 195 ASP A CA  1 
ATOM   1566 C  C   . ASP A 1 195 ? 22.014  -5.987  76.275  1.00 71.72  ? 195 ASP A C   1 
ATOM   1567 O  O   . ASP A 1 195 ? 21.970  -6.438  75.129  1.00 65.55  ? 195 ASP A O   1 
ATOM   1568 C  CB  . ASP A 1 195 ? 20.485  -3.960  76.489  1.00 68.30  ? 195 ASP A CB  1 
ATOM   1569 C  CG  . ASP A 1 195 ? 19.676  -4.282  77.730  1.00 75.14  ? 195 ASP A CG  1 
ATOM   1570 O  OD1 . ASP A 1 195 ? 19.365  -5.476  77.940  1.00 73.90  ? 195 ASP A OD1 1 
ATOM   1571 O  OD2 . ASP A 1 195 ? 19.361  -3.327  78.474  1.00 76.21  ? 195 ASP A OD2 1 
ATOM   1572 N  N   . PRO A 1 196 ? 22.148  -6.833  77.330  1.00 68.77  ? 196 PRO A N   1 
ATOM   1573 C  CA  . PRO A 1 196 ? 22.122  -8.293  77.157  1.00 66.34  ? 196 PRO A CA  1 
ATOM   1574 C  C   . PRO A 1 196 ? 20.780  -8.887  76.714  1.00 58.85  ? 196 PRO A C   1 
ATOM   1575 O  O   . PRO A 1 196 ? 20.731  -10.050 76.320  1.00 58.56  ? 196 PRO A O   1 
ATOM   1576 C  CB  . PRO A 1 196 ? 22.500  -8.837  78.547  1.00 67.51  ? 196 PRO A CB  1 
ATOM   1577 C  CG  . PRO A 1 196 ? 22.110  -7.726  79.498  1.00 69.66  ? 196 PRO A CG  1 
ATOM   1578 C  CD  . PRO A 1 196 ? 22.374  -6.443  78.731  1.00 65.94  ? 196 PRO A CD  1 
ATOM   1579 N  N   . ALA A 1 197 ? 19.704  -8.085  76.739  1.00 52.66  ? 197 ALA A N   1 
ATOM   1580 C  CA  . ALA A 1 197 ? 18.390  -8.528  76.282  1.00 58.08  ? 197 ALA A CA  1 
ATOM   1581 C  C   . ALA A 1 197 ? 18.332  -8.707  74.757  1.00 59.56  ? 197 ALA A C   1 
ATOM   1582 O  O   . ALA A 1 197 ? 17.421  -9.354  74.238  1.00 52.37  ? 197 ALA A O   1 
ATOM   1583 C  CB  . ALA A 1 197 ? 17.331  -7.552  76.748  1.00 57.52  ? 197 ALA A CB  1 
ATOM   1584 N  N   . TYR A 1 198 ? 19.294  -8.127  74.030  1.00 62.24  ? 198 TYR A N   1 
ATOM   1585 C  CA  . TYR A 1 198 ? 19.307  -8.198  72.577  1.00 59.32  ? 198 TYR A CA  1 
ATOM   1586 C  C   . TYR A 1 198 ? 20.431  -9.096  72.068  1.00 60.35  ? 198 TYR A C   1 
ATOM   1587 O  O   . TYR A 1 198 ? 20.717  -9.080  70.873  1.00 65.99  ? 198 TYR A O   1 
ATOM   1588 C  CB  . TYR A 1 198 ? 19.544  -6.804  71.992  1.00 59.27  ? 198 TYR A CB  1 
ATOM   1589 C  CG  . TYR A 1 198 ? 18.561  -5.735  72.438  1.00 59.28  ? 198 TYR A CG  1 
ATOM   1590 C  CD1 . TYR A 1 198 ? 17.202  -5.841  72.148  1.00 53.85  ? 198 TYR A CD1 1 
ATOM   1591 C  CD2 . TYR A 1 198 ? 19.001  -4.611  73.134  1.00 59.53  ? 198 TYR A CD2 1 
ATOM   1592 C  CE1 . TYR A 1 198 ? 16.309  -4.858  72.543  1.00 54.20  ? 198 TYR A CE1 1 
ATOM   1593 C  CE2 . TYR A 1 198 ? 18.117  -3.620  73.529  1.00 55.86  ? 198 TYR A CE2 1 
ATOM   1594 C  CZ  . TYR A 1 198 ? 16.771  -3.748  73.233  1.00 57.45  ? 198 TYR A CZ  1 
ATOM   1595 O  OH  . TYR A 1 198 ? 15.909  -2.768  73.618  1.00 63.20  ? 198 TYR A OH  1 
ATOM   1596 N  N   . ASP A 1 199 ? 21.092  -9.848  72.961  1.00 55.66  ? 199 ASP A N   1 
ATOM   1597 C  CA  . ASP A 1 199 ? 22.208  -10.690 72.550  1.00 59.36  ? 199 ASP A CA  1 
ATOM   1598 C  C   . ASP A 1 199 ? 21.699  -11.898 71.756  1.00 58.60  ? 199 ASP A C   1 
ATOM   1599 O  O   . ASP A 1 199 ? 22.423  -12.416 70.905  1.00 51.49  ? 199 ASP A O   1 
ATOM   1600 C  CB  . ASP A 1 199 ? 23.084  -11.070 73.750  1.00 64.93  ? 199 ASP A CB  1 
ATOM   1601 C  CG  . ASP A 1 199 ? 24.007  -9.946  74.198  1.00 69.45  ? 199 ASP A CG  1 
ATOM   1602 O  OD1 . ASP A 1 199 ? 24.113  -8.935  73.453  1.00 65.38  ? 199 ASP A OD1 1 
ATOM   1603 O  OD2 . ASP A 1 199 ? 24.610  -10.079 75.287  1.00 77.81  ? 199 ASP A OD2 1 
ATOM   1604 N  N   . GLU A 1 200 ? 20.450  -12.324 72.015  1.00 54.90  ? 200 GLU A N   1 
ATOM   1605 C  CA  . GLU A 1 200 ? 19.794  -13.360 71.224  1.00 56.63  ? 200 GLU A CA  1 
ATOM   1606 C  C   . GLU A 1 200 ? 19.609  -12.884 69.780  1.00 52.66  ? 200 GLU A C   1 
ATOM   1607 O  O   . GLU A 1 200 ? 19.841  -13.647 68.843  1.00 41.65  ? 200 GLU A O   1 
ATOM   1608 C  CB  . GLU A 1 200 ? 18.443  -13.767 71.824  1.00 58.20  ? 200 GLU A CB  1 
ATOM   1609 C  CG  . GLU A 1 200 ? 17.472  -12.610 72.035  1.00 64.42  ? 200 GLU A CG  1 
ATOM   1610 C  CD  . GLU A 1 200 ? 16.055  -12.995 72.442  1.00 67.06  ? 200 GLU A CD  1 
ATOM   1611 O  OE1 . GLU A 1 200 ? 15.901  -13.705 73.467  1.00 67.53  ? 200 GLU A OE1 1 
ATOM   1612 O  OE2 . GLU A 1 200 ? 15.099  -12.555 71.756  1.00 63.25  ? 200 GLU A OE2 1 
ATOM   1613 N  N   . ASN A 1 201 ? 19.205  -11.615 69.618  1.00 51.84  ? 201 ASN A N   1 
ATOM   1614 C  CA  . ASN A 1 201 ? 18.980  -11.016 68.311  1.00 48.88  ? 201 ASN A CA  1 
ATOM   1615 C  C   . ASN A 1 201 ? 20.286  -10.965 67.515  1.00 50.29  ? 201 ASN A C   1 
ATOM   1616 O  O   . ASN A 1 201 ? 20.288  -11.202 66.304  1.00 47.10  ? 201 ASN A O   1 
ATOM   1617 C  CB  . ASN A 1 201 ? 18.395  -9.606  68.433  1.00 50.64  ? 201 ASN A CB  1 
ATOM   1618 C  CG  . ASN A 1 201 ? 17.005  -9.570  69.036  1.00 53.03  ? 201 ASN A CG  1 
ATOM   1619 O  OD1 . ASN A 1 201 ? 16.773  -8.930  70.063  1.00 50.47  ? 201 ASN A OD1 1 
ATOM   1620 N  ND2 . ASN A 1 201 ? 16.067  -10.235 68.385  1.00 51.77  ? 201 ASN A ND2 1 
ATOM   1621 N  N   . LYS A 1 202 ? 21.398  -10.655 68.195  1.00 51.02  ? 202 LYS A N   1 
ATOM   1622 C  CA  . LYS A 1 202 ? 22.668  -10.404 67.526  1.00 55.55  ? 202 LYS A CA  1 
ATOM   1623 C  C   . LYS A 1 202 ? 23.274  -11.726 67.059  1.00 52.70  ? 202 LYS A C   1 
ATOM   1624 O  O   . LYS A 1 202 ? 23.951  -11.756 66.035  1.00 55.03  ? 202 LYS A O   1 
ATOM   1625 C  CB  . LYS A 1 202 ? 23.619  -9.591  68.419  1.00 60.50  ? 202 LYS A CB  1 
ATOM   1626 C  CG  . LYS A 1 202 ? 23.200  -8.134  68.648  1.00 64.38  ? 202 LYS A CG  1 
ATOM   1627 C  CD  . LYS A 1 202 ? 24.091  -7.338  69.595  1.00 69.12  ? 202 LYS A CD  1 
ATOM   1628 C  CE  . LYS A 1 202 ? 25.539  -7.295  69.144  1.00 76.50  ? 202 LYS A CE  1 
ATOM   1629 N  NZ  . LYS A 1 202 ? 26.345  -6.296  69.888  1.00 76.65  ? 202 LYS A NZ  1 
ATOM   1630 N  N   . ARG A 1 203 ? 23.021  -12.820 67.791  1.00 51.97  ? 203 ARG A N   1 
ATOM   1631 C  CA  . ARG A 1 203 ? 23.497  -14.129 67.363  1.00 53.75  ? 203 ARG A CA  1 
ATOM   1632 C  C   . ARG A 1 203 ? 22.745  -14.565 66.101  1.00 50.35  ? 203 ARG A C   1 
ATOM   1633 O  O   . ARG A 1 203 ? 23.360  -15.024 65.142  1.00 50.16  ? 203 ARG A O   1 
ATOM   1634 C  CB  . ARG A 1 203 ? 23.344  -15.163 68.485  1.00 60.56  ? 203 ARG A CB  1 
ATOM   1635 C  CG  . ARG A 1 203 ? 24.218  -14.905 69.707  1.00 69.68  ? 203 ARG A CG  1 
ATOM   1636 C  CD  . ARG A 1 203 ? 23.834  -15.804 70.875  1.00 77.83  ? 203 ARG A CD  1 
ATOM   1637 N  NE  . ARG A 1 203 ? 23.796  -15.091 72.150  1.00 84.90  ? 203 ARG A NE  1 
ATOM   1638 C  CZ  . ARG A 1 203 ? 23.005  -15.414 73.171  1.00 90.32  ? 203 ARG A CZ  1 
ATOM   1639 N  NH1 . ARG A 1 203 ? 22.221  -16.476 73.092  1.00 89.00  ? 203 ARG A NH1 1 
ATOM   1640 N  NH2 . ARG A 1 203 ? 22.994  -14.673 74.268  1.00 96.66  ? 203 ARG A NH2 1 
ATOM   1641 N  N   . GLN A 1 204 ? 21.410  -14.415 66.112  1.00 46.90  ? 204 GLN A N   1 
ATOM   1642 C  CA  . GLN A 1 204 ? 20.565  -14.746 64.972  1.00 45.90  ? 204 GLN A CA  1 
ATOM   1643 C  C   . GLN A 1 204 ? 20.946  -13.897 63.746  1.00 43.49  ? 204 GLN A C   1 
ATOM   1644 O  O   . GLN A 1 204 ? 21.009  -14.421 62.639  1.00 40.60  ? 204 GLN A O   1 
ATOM   1645 C  CB  . GLN A 1 204 ? 19.088  -14.597 65.364  1.00 47.27  ? 204 GLN A CB  1 
ATOM   1646 C  CG  . GLN A 1 204 ? 18.096  -15.007 64.276  1.00 51.09  ? 204 GLN A CG  1 
ATOM   1647 C  CD  . GLN A 1 204 ? 18.216  -16.457 63.840  1.00 53.36  ? 204 GLN A CD  1 
ATOM   1648 O  OE1 . GLN A 1 204 ? 18.636  -16.760 62.723  1.00 50.28  ? 204 GLN A OE1 1 
ATOM   1649 N  NE2 . GLN A 1 204 ? 17.832  -17.377 64.714  1.00 49.68  ? 204 GLN A NE2 1 
ATOM   1650 N  N   . PHE A 1 205 ? 21.243  -12.601 63.940  1.00 39.81  ? 205 PHE A N   1 
ATOM   1651 C  CA  . PHE A 1 205 ? 21.668  -11.716 62.858  1.00 38.06  ? 205 PHE A CA  1 
ATOM   1652 C  C   . PHE A 1 205 ? 22.943  -12.242 62.197  1.00 36.57  ? 205 PHE A C   1 
ATOM   1653 O  O   . PHE A 1 205 ? 23.024  -12.293 60.966  1.00 34.97  ? 205 PHE A O   1 
ATOM   1654 C  CB  . PHE A 1 205 ? 21.873  -10.297 63.382  1.00 37.74  ? 205 PHE A CB  1 
ATOM   1655 C  CG  . PHE A 1 205 ? 22.215  -9.255  62.350  1.00 36.41  ? 205 PHE A CG  1 
ATOM   1656 C  CD1 . PHE A 1 205 ? 21.267  -8.834  61.431  1.00 36.81  ? 205 PHE A CD1 1 
ATOM   1657 C  CD2 . PHE A 1 205 ? 23.478  -8.674  62.322  1.00 37.22  ? 205 PHE A CD2 1 
ATOM   1658 C  CE1 . PHE A 1 205 ? 21.571  -7.849  60.503  1.00 36.49  ? 205 PHE A CE1 1 
ATOM   1659 C  CE2 . PHE A 1 205 ? 23.784  -7.692  61.390  1.00 38.92  ? 205 PHE A CE2 1 
ATOM   1660 C  CZ  . PHE A 1 205 ? 22.830  -7.283  60.480  1.00 37.56  ? 205 PHE A CZ  1 
ATOM   1661 N  N   . GLN A 1 206 ? 23.910  -12.686 63.013  1.00 36.16  ? 206 GLN A N   1 
ATOM   1662 C  CA  . GLN A 1 206 ? 25.091  -13.368 62.497  1.00 38.40  ? 206 GLN A CA  1 
ATOM   1663 C  C   . GLN A 1 206 ? 24.721  -14.672 61.790  1.00 37.00  ? 206 GLN A C   1 
ATOM   1664 O  O   . GLN A 1 206 ? 25.367  -15.025 60.815  1.00 37.89  ? 206 GLN A O   1 
ATOM   1665 C  CB  . GLN A 1 206 ? 26.105  -13.669 63.603  1.00 42.84  ? 206 GLN A CB  1 
ATOM   1666 C  CG  . GLN A 1 206 ? 26.672  -12.420 64.265  1.00 48.72  ? 206 GLN A CG  1 
ATOM   1667 C  CD  . GLN A 1 206 ? 27.282  -11.446 63.284  1.00 53.21  ? 206 GLN A CD  1 
ATOM   1668 O  OE1 . GLN A 1 206 ? 26.981  -10.254 63.293  1.00 58.94  ? 206 GLN A OE1 1 
ATOM   1669 N  NE2 . GLN A 1 206 ? 28.173  -11.939 62.442  1.00 50.59  ? 206 GLN A NE2 1 
ATOM   1670 N  N   . ASP A 1 207 ? 23.695  -15.389 62.273  1.00 39.17  ? 207 ASP A N   1 
ATOM   1671 C  CA  . ASP A 1 207 ? 23.287  -16.654 61.665  1.00 40.49  ? 207 ASP A CA  1 
ATOM   1672 C  C   . ASP A 1 207 ? 22.705  -16.401 60.266  1.00 40.42  ? 207 ASP A C   1 
ATOM   1673 O  O   . ASP A 1 207 ? 23.013  -17.118 59.313  1.00 35.66  ? 207 ASP A O   1 
ATOM   1674 C  CB  . ASP A 1 207 ? 22.303  -17.418 62.563  1.00 43.97  ? 207 ASP A CB  1 
ATOM   1675 C  CG  . ASP A 1 207 ? 22.924  -18.156 63.747  1.00 47.72  ? 207 ASP A CG  1 
ATOM   1676 O  OD1 . ASP A 1 207 ? 24.163  -18.173 63.858  1.00 54.24  ? 207 ASP A OD1 1 
ATOM   1677 O  OD2 . ASP A 1 207 ? 22.153  -18.706 64.568  1.00 49.51  ? 207 ASP A OD2 1 
ATOM   1678 N  N   . ASP A 1 208 ? 21.898  -15.341 60.147  1.00 37.73  ? 208 ASP A N   1 
ATOM   1679 C  CA  . ASP A 1 208 ? 21.301  -14.914 58.891  1.00 41.16  ? 208 ASP A CA  1 
ATOM   1680 C  C   . ASP A 1 208 ? 22.380  -14.443 57.905  1.00 40.34  ? 208 ASP A C   1 
ATOM   1681 O  O   . ASP A 1 208 ? 22.273  -14.704 56.704  1.00 39.18  ? 208 ASP A O   1 
ATOM   1682 C  CB  . ASP A 1 208 ? 20.223  -13.856 59.169  1.00 43.77  ? 208 ASP A CB  1 
ATOM   1683 C  CG  . ASP A 1 208 ? 18.962  -14.427 59.812  1.00 47.13  ? 208 ASP A CG  1 
ATOM   1684 O  OD1 . ASP A 1 208 ? 18.695  -15.639 59.628  1.00 42.54  ? 208 ASP A OD1 1 
ATOM   1685 O  OD2 . ASP A 1 208 ? 18.265  -13.666 60.522  1.00 45.40  ? 208 ASP A OD2 1 
ATOM   1686 N  N   . ILE A 1 209 ? 23.418  -13.753 58.401  1.00 37.01  ? 209 ILE A N   1 
ATOM   1687 C  CA  . ILE A 1 209 ? 24.564  -13.398 57.575  1.00 36.39  ? 209 ILE A CA  1 
ATOM   1688 C  C   . ILE A 1 209 ? 25.228  -14.678 57.052  1.00 36.90  ? 209 ILE A C   1 
ATOM   1689 O  O   . ILE A 1 209 ? 25.719  -14.707 55.924  1.00 33.94  ? 209 ILE A O   1 
ATOM   1690 C  CB  . ILE A 1 209 ? 25.571  -12.492 58.328  1.00 38.79  ? 209 ILE A CB  1 
ATOM   1691 C  CG1 . ILE A 1 209 ? 24.972  -11.158 58.790  1.00 39.56  ? 209 ILE A CG1 1 
ATOM   1692 C  CG2 . ILE A 1 209 ? 26.849  -12.269 57.521  1.00 38.02  ? 209 ILE A CG2 1 
ATOM   1693 C  CD1 . ILE A 1 209 ? 23.885  -10.606 57.900  1.00 40.65  ? 209 ILE A CD1 1 
ATOM   1694 N  N   . LYS A 1 210 ? 25.270  -15.736 57.871  1.00 33.59  ? 210 LYS A N   1 
ATOM   1695 C  CA  . LYS A 1 210 ? 26.033  -16.916 57.501  1.00 36.01  ? 210 LYS A CA  1 
ATOM   1696 C  C   . LYS A 1 210 ? 25.320  -17.706 56.400  1.00 35.78  ? 210 LYS A C   1 
ATOM   1697 O  O   . LYS A 1 210 ? 25.978  -18.303 55.549  1.00 36.40  ? 210 LYS A O   1 
ATOM   1698 C  CB  . LYS A 1 210 ? 26.315  -17.774 58.736  1.00 42.72  ? 210 LYS A CB  1 
ATOM   1699 C  CG  . LYS A 1 210 ? 27.181  -19.003 58.496  1.00 48.09  ? 210 LYS A CG  1 
ATOM   1700 C  CD  . LYS A 1 210 ? 28.566  -18.705 57.966  1.00 56.63  ? 210 LYS A CD  1 
ATOM   1701 C  CE  . LYS A 1 210 ? 29.425  -19.954 57.914  1.00 63.88  ? 210 LYS A CE  1 
ATOM   1702 N  NZ  . LYS A 1 210 ? 30.819  -19.666 57.503  1.00 65.28  ? 210 LYS A NZ  1 
ATOM   1703 N  N   . VAL A 1 211 ? 23.982  -17.695 56.367  1.00 34.41  ? 211 VAL A N   1 
ATOM   1704 C  CA  . VAL A 1 211 ? 23.296  -18.424 55.306  1.00 36.05  ? 211 VAL A CA  1 
ATOM   1705 C  C   . VAL A 1 211 ? 23.464  -17.660 53.988  1.00 35.36  ? 211 VAL A C   1 
ATOM   1706 O  O   . VAL A 1 211 ? 23.663  -18.263 52.929  1.00 31.60  ? 211 VAL A O   1 
ATOM   1707 C  CB  . VAL A 1 211 ? 21.808  -18.710 55.611  1.00 38.93  ? 211 VAL A CB  1 
ATOM   1708 C  CG1 . VAL A 1 211 ? 21.604  -19.297 56.998  1.00 39.06  ? 211 VAL A CG1 1 
ATOM   1709 C  CG2 . VAL A 1 211 ? 20.913  -17.502 55.425  1.00 42.24  ? 211 VAL A CG2 1 
ATOM   1710 N  N   . MET A 1 212 ? 23.393  -16.322 54.051  1.00 29.35  ? 212 MET A N   1 
ATOM   1711 C  CA  . MET A 1 212 ? 23.559  -15.522 52.850  1.00 32.17  ? 212 MET A CA  1 
ATOM   1712 C  C   . MET A 1 212 ? 24.933  -15.830 52.256  1.00 30.20  ? 212 MET A C   1 
ATOM   1713 O  O   . MET A 1 212 ? 25.046  -16.165 51.090  1.00 28.80  ? 212 MET A O   1 
ATOM   1714 C  CB  . MET A 1 212 ? 23.399  -14.027 53.166  1.00 34.66  ? 212 MET A CB  1 
ATOM   1715 C  CG  . MET A 1 212 ? 21.948  -13.652 53.532  1.00 39.02  ? 212 MET A CG  1 
ATOM   1716 S  SD  . MET A 1 212 ? 21.623  -11.860 53.781  1.00 48.52  ? 212 MET A SD  1 
ATOM   1717 C  CE  . MET A 1 212 ? 23.202  -11.365 54.452  1.00 43.76  ? 212 MET A CE  1 
ATOM   1718 N  N   . ASN A 1 213 ? 25.966  -15.813 53.100  1.00 30.84  ? 213 ASN A N   1 
ATOM   1719 C  CA  . ASN A 1 213 ? 27.330  -16.030 52.666  1.00 31.06  ? 213 ASN A CA  1 
ATOM   1720 C  C   . ASN A 1 213 ? 27.516  -17.465 52.190  1.00 28.18  ? 213 ASN A C   1 
ATOM   1721 O  O   . ASN A 1 213 ? 28.252  -17.686 51.237  1.00 28.17  ? 213 ASN A O   1 
ATOM   1722 C  CB  . ASN A 1 213 ? 28.329  -15.604 53.749  1.00 33.28  ? 213 ASN A CB  1 
ATOM   1723 C  CG  . ASN A 1 213 ? 28.582  -14.113 53.702  1.00 34.45  ? 213 ASN A CG  1 
ATOM   1724 O  OD1 . ASN A 1 213 ? 27.920  -13.315 54.372  1.00 39.66  ? 213 ASN A OD1 1 
ATOM   1725 N  ND2 . ASN A 1 213 ? 29.492  -13.724 52.835  1.00 35.85  ? 213 ASN A ND2 1 
ATOM   1726 N  N   . ASP A 1 214 ? 26.829  -18.430 52.811  1.00 29.82  ? 214 ASP A N   1 
ATOM   1727 C  CA  . ASP A 1 214 ? 26.848  -19.807 52.326  1.00 29.63  ? 214 ASP A CA  1 
ATOM   1728 C  C   . ASP A 1 214 ? 26.336  -19.890 50.883  1.00 29.14  ? 214 ASP A C   1 
ATOM   1729 O  O   . ASP A 1 214 ? 26.970  -20.510 50.031  1.00 29.00  ? 214 ASP A O   1 
ATOM   1730 C  CB  . ASP A 1 214 ? 26.044  -20.723 53.252  1.00 33.44  ? 214 ASP A CB  1 
ATOM   1731 C  CG  . ASP A 1 214 ? 26.694  -20.980 54.608  1.00 36.54  ? 214 ASP A CG  1 
ATOM   1732 O  OD1 . ASP A 1 214 ? 27.908  -20.711 54.751  1.00 34.75  ? 214 ASP A OD1 1 
ATOM   1733 O  OD2 . ASP A 1 214 ? 25.975  -21.434 55.531  1.00 40.87  ? 214 ASP A OD2 1 
ATOM   1734 N  N   . LEU A 1 215 ? 25.188  -19.275 50.587  1.00 27.51  ? 215 LEU A N   1 
ATOM   1735 C  CA  . LEU A 1 215 ? 24.668  -19.294 49.219  1.00 26.35  ? 215 LEU A CA  1 
ATOM   1736 C  C   . LEU A 1 215 ? 25.631  -18.606 48.243  1.00 23.62  ? 215 LEU A C   1 
ATOM   1737 O  O   . LEU A 1 215 ? 25.881  -19.101 47.138  1.00 25.22  ? 215 LEU A O   1 
ATOM   1738 C  CB  . LEU A 1 215 ? 23.296  -18.619 49.177  1.00 25.53  ? 215 LEU A CB  1 
ATOM   1739 C  CG  . LEU A 1 215 ? 22.707  -18.512 47.775  1.00 27.54  ? 215 LEU A CG  1 
ATOM   1740 C  CD1 . LEU A 1 215 ? 22.346  -19.883 47.226  1.00 29.60  ? 215 LEU A CD1 1 
ATOM   1741 C  CD2 . LEU A 1 215 ? 21.502  -17.587 47.770  1.00 29.44  ? 215 LEU A CD2 1 
ATOM   1742 N  N   . VAL A 1 216 ? 26.188  -17.461 48.636  1.00 23.53  ? 216 VAL A N   1 
ATOM   1743 C  CA  . VAL A 1 216 ? 27.200  -16.807 47.814  1.00 24.30  ? 216 VAL A CA  1 
ATOM   1744 C  C   . VAL A 1 216 ? 28.303  -17.810 47.452  1.00 25.56  ? 216 VAL A C   1 
ATOM   1745 O  O   . VAL A 1 216 ? 28.707  -17.934 46.286  1.00 23.52  ? 216 VAL A O   1 
ATOM   1746 C  CB  . VAL A 1 216 ? 27.788  -15.572 48.540  1.00 25.46  ? 216 VAL A CB  1 
ATOM   1747 C  CG1 . VAL A 1 216 ? 29.035  -15.037 47.863  1.00 26.84  ? 216 VAL A CG1 1 
ATOM   1748 C  CG2 . VAL A 1 216 ? 26.781  -14.465 48.719  1.00 25.98  ? 216 VAL A CG2 1 
ATOM   1749 N  N   . ASP A 1 217 ? 28.843  -18.508 48.461  1.00 27.44  ? 217 ASP A N   1 
ATOM   1750 C  CA  . ASP A 1 217 ? 30.019  -19.351 48.239  1.00 30.81  ? 217 ASP A CA  1 
ATOM   1751 C  C   . ASP A 1 217 ? 29.727  -20.411 47.180  1.00 31.24  ? 217 ASP A C   1 
ATOM   1752 O  O   . ASP A 1 217 ? 30.597  -20.819 46.400  1.00 32.57  ? 217 ASP A O   1 
ATOM   1753 C  CB  . ASP A 1 217 ? 30.434  -20.077 49.520  1.00 35.23  ? 217 ASP A CB  1 
ATOM   1754 C  CG  . ASP A 1 217 ? 31.053  -19.222 50.611  1.00 40.29  ? 217 ASP A CG  1 
ATOM   1755 O  OD1 . ASP A 1 217 ? 31.412  -18.054 50.333  1.00 46.44  ? 217 ASP A OD1 1 
ATOM   1756 O  OD2 . ASP A 1 217 ? 31.166  -19.741 51.743  1.00 46.49  ? 217 ASP A OD2 1 
ATOM   1757 N  N   . LYS A 1 218 ? 28.482  -20.894 47.212  1.00 30.74  ? 218 LYS A N   1 
ATOM   1758 C  CA  . LYS A 1 218 ? 28.006  -21.927 46.317  1.00 29.41  ? 218 LYS A CA  1 
ATOM   1759 C  C   . LYS A 1 218 ? 27.869  -21.361 44.897  1.00 25.94  ? 218 LYS A C   1 
ATOM   1760 O  O   . LYS A 1 218 ? 28.273  -21.967 43.896  1.00 24.49  ? 218 LYS A O   1 
ATOM   1761 C  CB  . LYS A 1 218 ? 26.756  -22.466 47.021  1.00 33.28  ? 218 LYS A CB  1 
ATOM   1762 C  CG  . LYS A 1 218 ? 25.717  -23.182 46.182  1.00 38.98  ? 218 LYS A CG  1 
ATOM   1763 C  CD  . LYS A 1 218 ? 26.129  -24.501 45.590  1.00 37.59  ? 218 LYS A CD  1 
ATOM   1764 C  CE  . LYS A 1 218 ? 24.902  -25.278 45.150  1.00 35.51  ? 218 LYS A CE  1 
ATOM   1765 N  NZ  . LYS A 1 218 ? 25.080  -25.933 43.839  1.00 34.31  ? 218 LYS A NZ  1 
ATOM   1766 N  N   . ILE A 1 219 ? 27.306  -20.162 44.788  1.00 24.63  ? 219 ILE A N   1 
ATOM   1767 C  CA  . ILE A 1 219 ? 27.124  -19.560 43.485  1.00 22.88  ? 219 ILE A CA  1 
ATOM   1768 C  C   . ILE A 1 219 ? 28.478  -19.428 42.792  1.00 22.26  ? 219 ILE A C   1 
ATOM   1769 O  O   . ILE A 1 219 ? 28.592  -19.655 41.587  1.00 22.17  ? 219 ILE A O   1 
ATOM   1770 C  CB  . ILE A 1 219 ? 26.376  -18.222 43.644  1.00 23.68  ? 219 ILE A CB  1 
ATOM   1771 C  CG1 . ILE A 1 219 ? 24.877  -18.495 43.781  1.00 23.79  ? 219 ILE A CG1 1 
ATOM   1772 C  CG2 . ILE A 1 219 ? 26.700  -17.272 42.492  1.00 25.01  ? 219 ILE A CG2 1 
ATOM   1773 C  CD1 . ILE A 1 219 ? 24.035  -17.332 44.210  1.00 22.42  ? 219 ILE A CD1 1 
ATOM   1774 N  N   . ILE A 1 220 ? 29.508  -19.062 43.563  1.00 21.44  ? 220 ILE A N   1 
ATOM   1775 C  CA  . ILE A 1 220 ? 30.835  -18.846 42.995  1.00 25.19  ? 220 ILE A CA  1 
ATOM   1776 C  C   . ILE A 1 220 ? 31.475  -20.191 42.648  1.00 28.15  ? 220 ILE A C   1 
ATOM   1777 O  O   . ILE A 1 220 ? 32.104  -20.331 41.605  1.00 29.81  ? 220 ILE A O   1 
ATOM   1778 C  CB  . ILE A 1 220 ? 31.728  -18.037 43.959  1.00 26.24  ? 220 ILE A CB  1 
ATOM   1779 C  CG1 . ILE A 1 220 ? 31.287  -16.567 44.058  1.00 26.84  ? 220 ILE A CG1 1 
ATOM   1780 C  CG2 . ILE A 1 220 ? 33.189  -18.159 43.562  1.00 26.93  ? 220 ILE A CG2 1 
ATOM   1781 C  CD1 . ILE A 1 220 ? 31.856  -15.847 45.277  1.00 27.49  ? 220 ILE A CD1 1 
ATOM   1782 N  N   . ALA A 1 221 ? 31.329  -21.143 43.564  1.00 28.84  ? 221 ALA A N   1 
ATOM   1783 C  CA  . ALA A 1 221 ? 31.834  -22.489 43.385  1.00 32.94  ? 221 ALA A CA  1 
ATOM   1784 C  C   . ALA A 1 221 ? 31.274  -23.086 42.098  1.00 31.74  ? 221 ALA A C   1 
ATOM   1785 O  O   . ALA A 1 221 ? 32.037  -23.521 41.235  1.00 31.67  ? 221 ALA A O   1 
ATOM   1786 C  CB  . ALA A 1 221 ? 31.447  -23.298 44.599  1.00 33.66  ? 221 ALA A CB  1 
ATOM   1787 N  N   . ASP A 1 222 ? 29.936  -23.079 42.007  1.00 30.11  ? 222 ASP A N   1 
ATOM   1788 C  CA  . ASP A 1 222 ? 29.189  -23.585 40.870  1.00 34.52  ? 222 ASP A CA  1 
ATOM   1789 C  C   . ASP A 1 222 ? 29.774  -23.017 39.572  1.00 34.95  ? 222 ASP A C   1 
ATOM   1790 O  O   . ASP A 1 222 ? 29.999  -23.775 38.636  1.00 31.62  ? 222 ASP A O   1 
ATOM   1791 C  CB  . ASP A 1 222 ? 27.692  -23.245 40.990  1.00 35.24  ? 222 ASP A CB  1 
ATOM   1792 C  CG  . ASP A 1 222 ? 26.815  -24.169 41.844  1.00 44.05  ? 222 ASP A CG  1 
ATOM   1793 O  OD1 . ASP A 1 222 ? 27.355  -25.117 42.471  1.00 42.40  ? 222 ASP A OD1 1 
ATOM   1794 O  OD2 . ASP A 1 222 ? 25.561  -23.940 41.881  1.00 40.70  ? 222 ASP A OD2 1 
ATOM   1795 N  N   . ARG A 1 223 ? 29.971  -21.681 39.511  1.00 32.40  ? 223 ARG A N   1 
ATOM   1796 C  CA  . ARG A 1 223 ? 30.402  -21.003 38.288  1.00 34.15  ? 223 ARG A CA  1 
ATOM   1797 C  C   . ARG A 1 223 ? 31.805  -21.431 37.866  1.00 32.99  ? 223 ARG A C   1 
ATOM   1798 O  O   . ARG A 1 223 ? 32.064  -21.543 36.667  1.00 30.77  ? 223 ARG A O   1 
ATOM   1799 C  CB  . ARG A 1 223 ? 30.396  -19.475 38.455  1.00 30.33  ? 223 ARG A CB  1 
ATOM   1800 C  CG  . ARG A 1 223 ? 30.893  -18.678 37.254  1.00 27.84  ? 223 ARG A CG  1 
ATOM   1801 C  CD  . ARG A 1 223 ? 30.281  -19.077 35.914  1.00 28.53  ? 223 ARG A CD  1 
ATOM   1802 N  NE  . ARG A 1 223 ? 28.819  -18.987 35.868  1.00 28.77  ? 223 ARG A NE  1 
ATOM   1803 C  CZ  . ARG A 1 223 ? 28.132  -17.867 35.656  1.00 27.27  ? 223 ARG A CZ  1 
ATOM   1804 N  NH1 . ARG A 1 223 ? 28.749  -16.773 35.258  1.00 26.76  ? 223 ARG A NH1 1 
ATOM   1805 N  NH2 . ARG A 1 223 ? 26.821  -17.859 35.778  1.00 23.60  ? 223 ARG A NH2 1 
ATOM   1806 N  N   . LYS A 1 224 ? 32.703  -21.598 38.847  1.00 37.79  ? 224 LYS A N   1 
ATOM   1807 C  CA  . LYS A 1 224 ? 34.105  -21.905 38.571  1.00 42.23  ? 224 LYS A CA  1 
ATOM   1808 C  C   . LYS A 1 224 ? 34.246  -23.331 38.037  1.00 47.45  ? 224 LYS A C   1 
ATOM   1809 O  O   . LYS A 1 224 ? 34.983  -23.550 37.078  1.00 46.17  ? 224 LYS A O   1 
ATOM   1810 C  CB  . LYS A 1 224 ? 34.982  -21.719 39.812  1.00 41.36  ? 224 LYS A CB  1 
ATOM   1811 C  CG  . LYS A 1 224 ? 35.386  -20.276 40.093  1.00 46.90  ? 224 LYS A CG  1 
ATOM   1812 C  CD  . LYS A 1 224 ? 36.535  -20.120 41.071  1.00 51.82  ? 224 LYS A CD  1 
ATOM   1813 C  CE  . LYS A 1 224 ? 37.900  -20.216 40.422  1.00 50.17  ? 224 LYS A CE  1 
ATOM   1814 N  NZ  . LYS A 1 224 ? 38.966  -19.849 41.379  1.00 53.85  ? 224 LYS A NZ  1 
ATOM   1815 N  N   . ALA A 1 225 ? 33.528  -24.278 38.661  1.00 49.13  ? 225 ALA A N   1 
ATOM   1816 C  CA  . ALA A 1 225 ? 33.592  -25.687 38.297  1.00 52.07  ? 225 ALA A CA  1 
ATOM   1817 C  C   . ALA A 1 225 ? 32.895  -25.920 36.960  1.00 56.61  ? 225 ALA A C   1 
ATOM   1818 O  O   . ALA A 1 225 ? 33.184  -26.898 36.281  1.00 60.32  ? 225 ALA A O   1 
ATOM   1819 C  CB  . ALA A 1 225 ? 32.967  -26.535 39.377  1.00 49.24  ? 225 ALA A CB  1 
ATOM   1820 N  N   . SER A 1 226 ? 31.959  -25.031 36.609  1.00 60.06  ? 226 SER A N   1 
ATOM   1821 C  CA  . SER A 1 226 ? 31.290  -25.064 35.319  1.00 64.75  ? 226 SER A CA  1 
ATOM   1822 C  C   . SER A 1 226 ? 32.275  -24.767 34.191  1.00 65.26  ? 226 SER A C   1 
ATOM   1823 O  O   . SER A 1 226 ? 32.109  -25.275 33.088  1.00 67.72  ? 226 SER A O   1 
ATOM   1824 C  CB  . SER A 1 226 ? 30.138  -24.085 35.287  1.00 66.49  ? 226 SER A CB  1 
ATOM   1825 O  OG  . SER A 1 226 ? 29.579  -24.008 33.984  1.00 66.04  ? 226 SER A OG  1 
ATOM   1826 N  N   . GLY A 1 227 ? 33.268  -23.914 34.469  1.00 69.91  ? 227 GLY A N   1 
ATOM   1827 C  CA  . GLY A 1 227 ? 34.204  -23.456 33.455  1.00 78.14  ? 227 GLY A CA  1 
ATOM   1828 C  C   . GLY A 1 227 ? 33.507  -22.663 32.349  1.00 86.52  ? 227 GLY A C   1 
ATOM   1829 O  O   . GLY A 1 227 ? 33.998  -22.624 31.222  1.00 90.13  ? 227 GLY A O   1 
ATOM   1830 N  N   . GLU A 1 228 ? 32.373  -22.027 32.686  1.00 95.78  ? 228 GLU A N   1 
ATOM   1831 C  CA  . GLU A 1 228 ? 31.552  -21.314 31.714  1.00 98.11  ? 228 GLU A CA  1 
ATOM   1832 C  C   . GLU A 1 228 ? 31.878  -19.820 31.776  1.00 102.92 ? 228 GLU A C   1 
ATOM   1833 O  O   . GLU A 1 228 ? 32.467  -19.349 32.751  1.00 107.49 ? 228 GLU A O   1 
ATOM   1834 C  CB  . GLU A 1 228 ? 30.059  -21.584 31.948  1.00 95.59  ? 228 GLU A CB  1 
ATOM   1835 C  CG  . GLU A 1 228 ? 29.527  -21.057 33.275  1.00 98.94  ? 228 GLU A CG  1 
ATOM   1836 C  CD  . GLU A 1 228 ? 28.060  -21.332 33.572  1.00 107.81 ? 228 GLU A CD  1 
ATOM   1837 O  OE1 . GLU A 1 228 ? 27.776  -22.031 34.575  1.00 108.92 ? 228 GLU A OE1 1 
ATOM   1838 O  OE2 . GLU A 1 228 ? 27.198  -20.824 32.822  1.00 117.51 ? 228 GLU A OE2 1 
ATOM   1839 N  N   . GLN A 1 229 ? 31.526  -19.105 30.693  1.00 105.43 ? 229 GLN A N   1 
ATOM   1840 C  CA  . GLN A 1 229 ? 31.483  -17.647 30.664  1.00 92.08  ? 229 GLN A CA  1 
ATOM   1841 C  C   . GLN A 1 229 ? 30.098  -17.218 30.169  1.00 83.19  ? 229 GLN A C   1 
ATOM   1842 O  O   . GLN A 1 229 ? 29.999  -16.349 29.302  1.00 73.46  ? 229 GLN A O   1 
ATOM   1843 C  CB  . GLN A 1 229 ? 32.575  -17.058 29.756  1.00 83.84  ? 229 GLN A CB  1 
ATOM   1844 C  CG  . GLN A 1 229 ? 33.977  -17.624 29.970  1.00 81.16  ? 229 GLN A CG  1 
ATOM   1845 C  CD  . GLN A 1 229 ? 34.729  -16.998 31.120  1.00 75.38  ? 229 GLN A CD  1 
ATOM   1846 O  OE1 . GLN A 1 229 ? 34.303  -17.061 32.270  1.00 74.70  ? 229 GLN A OE1 1 
ATOM   1847 N  NE2 . GLN A 1 229 ? 35.878  -16.409 30.820  1.00 69.65  ? 229 GLN A NE2 1 
ATOM   1848 N  N   . SER A 1 230 ? 29.037  -17.851 30.710  1.00 77.03  ? 230 SER A N   1 
ATOM   1849 C  CA  . SER A 1 230 ? 27.665  -17.475 30.397  1.00 71.50  ? 230 SER A CA  1 
ATOM   1850 C  C   . SER A 1 230 ? 27.495  -15.974 30.629  1.00 62.09  ? 230 SER A C   1 
ATOM   1851 O  O   . SER A 1 230 ? 27.278  -15.523 31.755  1.00 66.77  ? 230 SER A O   1 
ATOM   1852 C  CB  . SER A 1 230 ? 26.630  -18.302 31.158  1.00 73.33  ? 230 SER A CB  1 
ATOM   1853 O  OG  . SER A 1 230 ? 26.871  -18.336 32.560  1.00 69.98  ? 230 SER A OG  1 
ATOM   1854 N  N   . ASP A 1 231 ? 27.633  -15.221 29.535  1.00 54.91  ? 231 ASP A N   1 
ATOM   1855 C  CA  . ASP A 1 231 ? 27.650  -13.764 29.512  1.00 52.76  ? 231 ASP A CA  1 
ATOM   1856 C  C   . ASP A 1 231 ? 26.546  -13.194 30.415  1.00 47.02  ? 231 ASP A C   1 
ATOM   1857 O  O   . ASP A 1 231 ? 25.576  -12.615 29.927  1.00 53.98  ? 231 ASP A O   1 
ATOM   1858 C  CB  . ASP A 1 231 ? 27.504  -13.304 28.052  1.00 56.46  ? 231 ASP A CB  1 
ATOM   1859 C  CG  . ASP A 1 231 ? 28.081  -11.939 27.714  1.00 61.84  ? 231 ASP A CG  1 
ATOM   1860 O  OD1 . ASP A 1 231 ? 29.327  -11.837 27.648  1.00 62.50  ? 231 ASP A OD1 1 
ATOM   1861 O  OD2 . ASP A 1 231 ? 27.280  -10.995 27.490  1.00 60.65  ? 231 ASP A OD2 1 
ATOM   1862 N  N   . ASP A 1 232 ? 26.692  -13.355 31.739  1.00 35.41  ? 232 ASP A N   1 
ATOM   1863 C  CA  . ASP A 1 232 ? 25.692  -12.889 32.686  1.00 31.20  ? 232 ASP A CA  1 
ATOM   1864 C  C   . ASP A 1 232 ? 26.340  -11.926 33.688  1.00 27.76  ? 232 ASP A C   1 
ATOM   1865 O  O   . ASP A 1 232 ? 27.525  -11.593 33.583  1.00 29.05  ? 232 ASP A O   1 
ATOM   1866 C  CB  . ASP A 1 232 ? 24.950  -14.085 33.305  1.00 30.37  ? 232 ASP A CB  1 
ATOM   1867 C  CG  . ASP A 1 232 ? 25.754  -14.972 34.246  1.00 33.62  ? 232 ASP A CG  1 
ATOM   1868 O  OD1 . ASP A 1 232 ? 26.920  -14.600 34.567  1.00 30.16  ? 232 ASP A OD1 1 
ATOM   1869 O  OD2 . ASP A 1 232 ? 25.199  -16.038 34.673  1.00 28.55  ? 232 ASP A OD2 1 
ATOM   1870 N  N   . LEU A 1 233 ? 25.559  -11.479 34.675  1.00 25.29  ? 233 LEU A N   1 
ATOM   1871 C  CA  . LEU A 1 233 ? 26.015  -10.503 35.661  1.00 24.70  ? 233 LEU A CA  1 
ATOM   1872 C  C   . LEU A 1 233 ? 27.184  -11.030 36.501  1.00 24.39  ? 233 LEU A C   1 
ATOM   1873 O  O   . LEU A 1 233 ? 28.129  -10.296 36.805  1.00 21.63  ? 233 LEU A O   1 
ATOM   1874 C  CB  . LEU A 1 233 ? 24.795  -10.137 36.506  1.00 23.80  ? 233 LEU A CB  1 
ATOM   1875 C  CG  . LEU A 1 233 ? 25.058  -9.224  37.688  1.00 25.52  ? 233 LEU A CG  1 
ATOM   1876 C  CD1 . LEU A 1 233 ? 25.604  -7.886  37.213  1.00 25.43  ? 233 LEU A CD1 1 
ATOM   1877 C  CD2 . LEU A 1 233 ? 23.785  -9.015  38.496  1.00 25.23  ? 233 LEU A CD2 1 
ATOM   1878 N  N   . LEU A 1 234 ? 27.168  -12.336 36.818  1.00 25.03  ? 234 LEU A N   1 
ATOM   1879 C  CA  . LEU A 1 234 ? 28.290  -12.995 37.484  1.00 22.59  ? 234 LEU A CA  1 
ATOM   1880 C  C   . LEU A 1 234 ? 29.541  -13.031 36.609  1.00 20.52  ? 234 LEU A C   1 
ATOM   1881 O  O   . LEU A 1 234 ? 30.633  -12.856 37.116  1.00 18.64  ? 234 LEU A O   1 
ATOM   1882 C  CB  . LEU A 1 234 ? 27.872  -14.395 37.935  1.00 23.44  ? 234 LEU A CB  1 
ATOM   1883 C  CG  . LEU A 1 234 ? 28.880  -15.132 38.811  1.00 24.11  ? 234 LEU A CG  1 
ATOM   1884 C  CD1 . LEU A 1 234 ? 29.162  -14.346 40.068  1.00 23.38  ? 234 LEU A CD1 1 
ATOM   1885 C  CD2 . LEU A 1 234 ? 28.384  -16.527 39.142  1.00 25.31  ? 234 LEU A CD2 1 
ATOM   1886 N  N   . THR A 1 235 ? 29.405  -13.228 35.297  1.00 22.43  ? 235 THR A N   1 
ATOM   1887 C  CA  . THR A 1 235 ? 30.551  -13.246 34.395  1.00 24.09  ? 235 THR A CA  1 
ATOM   1888 C  C   . THR A 1 235 ? 31.329  -11.922 34.467  1.00 25.78  ? 235 THR A C   1 
ATOM   1889 O  O   . THR A 1 235 ? 32.571  -11.905 34.501  1.00 22.29  ? 235 THR A O   1 
ATOM   1890 C  CB  . THR A 1 235 ? 30.115  -13.544 32.949  1.00 26.28  ? 235 THR A CB  1 
ATOM   1891 O  OG1 . THR A 1 235 ? 29.295  -14.713 32.938  1.00 25.66  ? 235 THR A OG1 1 
ATOM   1892 C  CG2 . THR A 1 235 ? 31.272  -13.764 32.003  1.00 28.46  ? 235 THR A CG2 1 
ATOM   1893 N  N   . HIS A 1 236 ? 30.586  -10.809 34.490  1.00 24.73  ? 236 HIS A N   1 
ATOM   1894 C  CA  . HIS A 1 236 ? 31.176  -9.477  34.549  1.00 26.74  ? 236 HIS A CA  1 
ATOM   1895 C  C   . HIS A 1 236 ? 31.860  -9.241  35.901  1.00 25.12  ? 236 HIS A C   1 
ATOM   1896 O  O   . HIS A 1 236 ? 32.968  -8.724  35.957  1.00 20.73  ? 236 HIS A O   1 
ATOM   1897 C  CB  . HIS A 1 236 ? 30.095  -8.437  34.221  1.00 30.52  ? 236 HIS A CB  1 
ATOM   1898 C  CG  . HIS A 1 236 ? 29.723  -8.453  32.783  1.00 36.61  ? 236 HIS A CG  1 
ATOM   1899 N  ND1 . HIS A 1 236 ? 28.912  -9.420  32.231  1.00 40.17  ? 236 HIS A ND1 1 
ATOM   1900 C  CD2 . HIS A 1 236 ? 30.089  -7.639  31.775  1.00 42.62  ? 236 HIS A CD2 1 
ATOM   1901 C  CE1 . HIS A 1 236 ? 28.766  -9.174  30.935  1.00 46.73  ? 236 HIS A CE1 1 
ATOM   1902 N  NE2 . HIS A 1 236 ? 29.475  -8.092  30.636  1.00 46.76  ? 236 HIS A NE2 1 
ATOM   1903 N  N   . MET A 1 237 ? 31.217  -9.666  36.999  1.00 22.98  ? 237 MET A N   1 
ATOM   1904 C  CA  . MET A 1 237 ? 31.784  -9.476  38.324  1.00 22.57  ? 237 MET A CA  1 
ATOM   1905 C  C   . MET A 1 237 ? 33.125  -10.193 38.404  1.00 25.66  ? 237 MET A C   1 
ATOM   1906 O  O   . MET A 1 237 ? 34.092  -9.644  38.911  1.00 27.08  ? 237 MET A O   1 
ATOM   1907 C  CB  . MET A 1 237 ? 30.894  -10.054 39.416  1.00 21.73  ? 237 MET A CB  1 
ATOM   1908 C  CG  . MET A 1 237 ? 29.630  -9.265  39.678  1.00 23.44  ? 237 MET A CG  1 
ATOM   1909 S  SD  . MET A 1 237 ? 28.719  -10.123 40.951  1.00 26.17  ? 237 MET A SD  1 
ATOM   1910 C  CE  . MET A 1 237 ? 27.107  -9.347  40.888  1.00 24.76  ? 237 MET A CE  1 
ATOM   1911 N  N   . LEU A 1 238 ? 33.173  -11.415 37.865  1.00 23.96  ? 238 LEU A N   1 
ATOM   1912 C  CA  . LEU A 1 238 ? 34.311  -12.304 38.042  1.00 25.57  ? 238 LEU A CA  1 
ATOM   1913 C  C   . LEU A 1 238 ? 35.475  -11.975 37.106  1.00 28.19  ? 238 LEU A C   1 
ATOM   1914 O  O   . LEU A 1 238 ? 36.616  -12.285 37.439  1.00 35.54  ? 238 LEU A O   1 
ATOM   1915 C  CB  . LEU A 1 238 ? 33.812  -13.739 37.800  1.00 27.18  ? 238 LEU A CB  1 
ATOM   1916 C  CG  . LEU A 1 238 ? 33.051  -14.390 38.950  1.00 25.38  ? 238 LEU A CG  1 
ATOM   1917 C  CD1 . LEU A 1 238 ? 32.613  -15.814 38.565  1.00 28.52  ? 238 LEU A CD1 1 
ATOM   1918 C  CD2 . LEU A 1 238 ? 33.905  -14.459 40.189  1.00 25.48  ? 238 LEU A CD2 1 
ATOM   1919 N  N   . ASN A 1 239 ? 35.206  -11.416 35.921  1.00 26.25  ? 239 ASN A N   1 
ATOM   1920 C  CA  . ASN A 1 239 ? 36.215  -11.263 34.878  1.00 27.79  ? 239 ASN A CA  1 
ATOM   1921 C  C   . ASN A 1 239 ? 36.330  -9.826  34.348  1.00 27.68  ? 239 ASN A C   1 
ATOM   1922 O  O   . ASN A 1 239 ? 37.264  -9.537  33.620  1.00 33.66  ? 239 ASN A O   1 
ATOM   1923 C  CB  . ASN A 1 239 ? 35.913  -12.127 33.648  1.00 23.25  ? 239 ASN A CB  1 
ATOM   1924 C  CG  . ASN A 1 239 ? 35.691  -13.580 34.010  1.00 27.52  ? 239 ASN A CG  1 
ATOM   1925 O  OD1 . ASN A 1 239 ? 36.591  -14.245 34.508  1.00 26.96  ? 239 ASN A OD1 1 
ATOM   1926 N  ND2 . ASN A 1 239 ? 34.470  -14.050 33.818  1.00 24.97  ? 239 ASN A ND2 1 
ATOM   1927 N  N   . GLY A 1 240 ? 35.327  -8.977  34.593  1.00 27.26  ? 240 GLY A N   1 
ATOM   1928 C  CA  . GLY A 1 240 ? 35.299  -7.623  34.069  1.00 26.54  ? 240 GLY A CA  1 
ATOM   1929 C  C   . GLY A 1 240 ? 36.358  -6.734  34.726  1.00 27.78  ? 240 GLY A C   1 
ATOM   1930 O  O   . GLY A 1 240 ? 36.601  -6.818  35.934  1.00 26.86  ? 240 GLY A O   1 
ATOM   1931 N  N   . LYS A 1 241 ? 36.987  -5.872  33.922  1.00 27.10  ? 241 LYS A N   1 
ATOM   1932 C  CA  . LYS A 1 241 ? 37.944  -4.906  34.454  1.00 26.56  ? 241 LYS A CA  1 
ATOM   1933 C  C   . LYS A 1 241 ? 37.385  -3.500  34.283  1.00 22.56  ? 241 LYS A C   1 
ATOM   1934 O  O   . LYS A 1 241 ? 36.726  -3.237  33.299  1.00 20.65  ? 241 LYS A O   1 
ATOM   1935 C  CB  . LYS A 1 241 ? 39.291  -5.060  33.753  1.00 30.48  ? 241 LYS A CB  1 
ATOM   1936 C  CG  . LYS A 1 241 ? 39.989  -6.382  34.008  1.00 34.78  ? 241 LYS A CG  1 
ATOM   1937 C  CD  . LYS A 1 241 ? 41.359  -6.428  33.376  1.00 40.87  ? 241 LYS A CD  1 
ATOM   1938 C  CE  . LYS A 1 241 ? 42.270  -7.458  34.013  1.00 48.59  ? 241 LYS A CE  1 
ATOM   1939 N  NZ  . LYS A 1 241 ? 43.656  -7.346  33.492  1.00 48.79  ? 241 LYS A NZ  1 
ATOM   1940 N  N   . ASP A 1 242 ? 37.605  -2.634  35.273  1.00 20.59  ? 242 ASP A N   1 
ATOM   1941 C  CA  . ASP A 1 242 ? 37.170  -1.245  35.214  1.00 19.51  ? 242 ASP A CA  1 
ATOM   1942 C  C   . ASP A 1 242 ? 38.010  -0.487  34.187  1.00 19.29  ? 242 ASP A C   1 
ATOM   1943 O  O   . ASP A 1 242 ? 39.231  -0.444  34.291  1.00 17.70  ? 242 ASP A O   1 
ATOM   1944 C  CB  . ASP A 1 242 ? 37.231  -0.606  36.601  1.00 19.55  ? 242 ASP A CB  1 
ATOM   1945 C  CG  . ASP A 1 242 ? 37.237  0.917   36.602  1.00 21.66  ? 242 ASP A CG  1 
ATOM   1946 O  OD1 . ASP A 1 242 ? 36.545  1.497   35.721  1.00 24.28  ? 242 ASP A OD1 1 
ATOM   1947 O  OD2 . ASP A 1 242 ? 37.886  1.516   37.518  1.00 19.92  ? 242 ASP A OD2 1 
ATOM   1948 N  N   . PRO A 1 243 ? 37.411  0.153   33.170  1.00 23.02  ? 243 PRO A N   1 
ATOM   1949 C  CA  . PRO A 1 243 ? 38.213  0.825   32.146  1.00 22.98  ? 243 PRO A CA  1 
ATOM   1950 C  C   . PRO A 1 243 ? 39.094  1.931   32.729  1.00 23.79  ? 243 PRO A C   1 
ATOM   1951 O  O   . PRO A 1 243 ? 40.185  2.173   32.235  1.00 23.32  ? 243 PRO A O   1 
ATOM   1952 C  CB  . PRO A 1 243 ? 37.191  1.401   31.145  1.00 23.58  ? 243 PRO A CB  1 
ATOM   1953 C  CG  . PRO A 1 243 ? 35.902  0.642   31.424  1.00 26.54  ? 243 PRO A CG  1 
ATOM   1954 C  CD  . PRO A 1 243 ? 35.960  0.244   32.895  1.00 25.87  ? 243 PRO A CD  1 
ATOM   1955 N  N   . GLU A 1 244 ? 38.619  2.606   33.780  1.00 22.29  ? 244 GLU A N   1 
ATOM   1956 C  CA  . GLU A 1 244 ? 39.330  3.736   34.342  1.00 23.45  ? 244 GLU A CA  1 
ATOM   1957 C  C   . GLU A 1 244 ? 40.552  3.303   35.124  1.00 23.13  ? 244 GLU A C   1 
ATOM   1958 O  O   . GLU A 1 244 ? 41.607  3.904   34.924  1.00 27.39  ? 244 GLU A O   1 
ATOM   1959 C  CB  . GLU A 1 244 ? 38.502  4.518   35.343  1.00 27.67  ? 244 GLU A CB  1 
ATOM   1960 C  CG  . GLU A 1 244 ? 37.443  5.363   34.697  1.00 35.59  ? 244 GLU A CG  1 
ATOM   1961 C  CD  . GLU A 1 244 ? 36.624  6.119   35.728  1.00 38.66  ? 244 GLU A CD  1 
ATOM   1962 O  OE1 . GLU A 1 244 ? 37.179  6.414   36.849  1.00 40.09  ? 244 GLU A OE1 1 
ATOM   1963 O  OE2 . GLU A 1 244 ? 35.425  6.327   35.442  1.00 34.87  ? 244 GLU A OE2 1 
ATOM   1964 N  N   . THR A 1 245 ? 40.369  2.387   36.087  1.00 22.48  ? 245 THR A N   1 
ATOM   1965 C  CA  . THR A 1 245 ? 41.471  1.929   36.916  1.00 23.17  ? 245 THR A CA  1 
ATOM   1966 C  C   . THR A 1 245 ? 42.245  0.786   36.271  1.00 21.75  ? 245 THR A C   1 
ATOM   1967 O  O   . THR A 1 245 ? 43.406  0.617   36.602  1.00 21.32  ? 245 THR A O   1 
ATOM   1968 C  CB  . THR A 1 245 ? 41.056  1.515   38.331  1.00 23.59  ? 245 THR A CB  1 
ATOM   1969 O  OG1 . THR A 1 245 ? 40.217  0.354   38.244  1.00 21.29  ? 245 THR A OG1 1 
ATOM   1970 C  CG2 . THR A 1 245 ? 40.439  2.674   39.093  1.00 24.33  ? 245 THR A CG2 1 
ATOM   1971 N  N   . GLY A 1 246 ? 41.604  0.005   35.399  1.00 21.44  ? 246 GLY A N   1 
ATOM   1972 C  CA  . GLY A 1 246 ? 42.224  -1.170  34.807  1.00 19.89  ? 246 GLY A CA  1 
ATOM   1973 C  C   . GLY A 1 246 ? 42.145  -2.405  35.702  1.00 19.20  ? 246 GLY A C   1 
ATOM   1974 O  O   . GLY A 1 246 ? 42.761  -3.429  35.397  1.00 18.33  ? 246 GLY A O   1 
ATOM   1975 N  N   . GLU A 1 247 ? 41.438  -2.272  36.825  1.00 19.26  ? 247 GLU A N   1 
ATOM   1976 C  CA  . GLU A 1 247 ? 41.344  -3.299  37.850  1.00 21.73  ? 247 GLU A CA  1 
ATOM   1977 C  C   . GLU A 1 247 ? 40.025  -4.086  37.804  1.00 20.72  ? 247 GLU A C   1 
ATOM   1978 O  O   . GLU A 1 247 ? 38.936  -3.544  37.616  1.00 19.67  ? 247 GLU A O   1 
ATOM   1979 C  CB  . GLU A 1 247 ? 41.369  -2.668  39.248  1.00 24.06  ? 247 GLU A CB  1 
ATOM   1980 C  CG  . GLU A 1 247 ? 42.706  -2.101  39.692  1.00 23.72  ? 247 GLU A CG  1 
ATOM   1981 C  CD  . GLU A 1 247 ? 42.665  -1.514  41.097  1.00 29.02  ? 247 GLU A CD  1 
ATOM   1982 O  OE1 . GLU A 1 247 ? 41.804  -1.938  41.892  1.00 28.79  ? 247 GLU A OE1 1 
ATOM   1983 O  OE2 . GLU A 1 247 ? 43.476  -0.600  41.403  1.00 32.36  ? 247 GLU A OE2 1 
ATOM   1984 N  N   . PRO A 1 248 ? 40.049  -5.391  38.117  1.00 22.12  ? 248 PRO A N   1 
ATOM   1985 C  CA  . PRO A 1 248 ? 38.818  -6.109  38.465  1.00 20.94  ? 248 PRO A CA  1 
ATOM   1986 C  C   . PRO A 1 248 ? 38.352  -5.898  39.904  1.00 19.15  ? 248 PRO A C   1 
ATOM   1987 O  O   . PRO A 1 248 ? 39.079  -5.405  40.760  1.00 20.06  ? 248 PRO A O   1 
ATOM   1988 C  CB  . PRO A 1 248 ? 39.250  -7.573  38.225  1.00 21.84  ? 248 PRO A CB  1 
ATOM   1989 C  CG  . PRO A 1 248 ? 40.695  -7.565  38.661  1.00 24.39  ? 248 PRO A CG  1 
ATOM   1990 C  CD  . PRO A 1 248 ? 41.242  -6.245  38.153  1.00 24.22  ? 248 PRO A CD  1 
ATOM   1991 N  N   . LEU A 1 249 ? 37.117  -6.299  40.206  1.00 19.32  ? 249 LEU A N   1 
ATOM   1992 C  CA  . LEU A 1 249 ? 36.710  -6.300  41.607  1.00 20.38  ? 249 LEU A CA  1 
ATOM   1993 C  C   . LEU A 1 249 ? 37.567  -7.345  42.315  1.00 20.64  ? 249 LEU A C   1 
ATOM   1994 O  O   . LEU A 1 249 ? 37.891  -8.370  41.734  1.00 22.10  ? 249 LEU A O   1 
ATOM   1995 C  CB  . LEU A 1 249 ? 35.222  -6.643  41.743  1.00 23.60  ? 249 LEU A CB  1 
ATOM   1996 C  CG  . LEU A 1 249 ? 34.271  -5.800  40.903  1.00 24.55  ? 249 LEU A CG  1 
ATOM   1997 C  CD1 . LEU A 1 249 ? 32.834  -6.272  41.072  1.00 24.83  ? 249 LEU A CD1 1 
ATOM   1998 C  CD2 . LEU A 1 249 ? 34.412  -4.327  41.268  1.00 25.56  ? 249 LEU A CD2 1 
ATOM   1999 N  N   . ASP A 1 250 ? 37.923  -7.105  43.568  1.00 22.36  ? 250 ASP A N   1 
ATOM   2000 C  CA  . ASP A 1 250 ? 38.605  -8.114  44.358  1.00 25.08  ? 250 ASP A CA  1 
ATOM   2001 C  C   . ASP A 1 250 ? 37.563  -9.121  44.843  1.00 25.14  ? 250 ASP A C   1 
ATOM   2002 O  O   . ASP A 1 250 ? 36.373  -8.829  44.777  1.00 21.57  ? 250 ASP A O   1 
ATOM   2003 C  CB  . ASP A 1 250 ? 39.359  -7.503  45.527  1.00 28.61  ? 250 ASP A CB  1 
ATOM   2004 C  CG  . ASP A 1 250 ? 38.465  -6.738  46.483  1.00 37.40  ? 250 ASP A CG  1 
ATOM   2005 O  OD1 . ASP A 1 250 ? 37.492  -7.320  46.982  1.00 39.57  ? 250 ASP A OD1 1 
ATOM   2006 O  OD2 . ASP A 1 250 ? 38.771  -5.555  46.744  1.00 53.50  ? 250 ASP A OD2 1 
ATOM   2007 N  N   . ASP A 1 251 ? 38.016  -10.270 45.357  1.00 26.67  ? 251 ASP A N   1 
ATOM   2008 C  CA  . ASP A 1 251 ? 37.143  -11.323 45.882  1.00 28.73  ? 251 ASP A CA  1 
ATOM   2009 C  C   . ASP A 1 251 ? 36.105  -10.771 46.852  1.00 25.88  ? 251 ASP A C   1 
ATOM   2010 O  O   . ASP A 1 251 ? 34.929  -11.084 46.728  1.00 22.63  ? 251 ASP A O   1 
ATOM   2011 C  CB  . ASP A 1 251 ? 37.921  -12.420 46.614  1.00 32.85  ? 251 ASP A CB  1 
ATOM   2012 C  CG  . ASP A 1 251 ? 38.703  -13.334 45.689  1.00 40.93  ? 251 ASP A CG  1 
ATOM   2013 O  OD1 . ASP A 1 251 ? 38.846  -12.979 44.503  1.00 43.00  ? 251 ASP A OD1 1 
ATOM   2014 O  OD2 . ASP A 1 251 ? 39.146  -14.411 46.155  1.00 47.46  ? 251 ASP A OD2 1 
ATOM   2015 N  N   . GLU A 1 252 ? 36.542  -9.971  47.832  1.00 23.58  ? 252 GLU A N   1 
ATOM   2016 C  CA  . GLU A 1 252 ? 35.648  -9.546  48.892  1.00 26.49  ? 252 GLU A CA  1 
ATOM   2017 C  C   . GLU A 1 252 ? 34.456  -8.780  48.321  1.00 23.49  ? 252 GLU A C   1 
ATOM   2018 O  O   . GLU A 1 252 ? 33.306  -9.075  48.654  1.00 21.78  ? 252 GLU A O   1 
ATOM   2019 C  CB  . GLU A 1 252 ? 36.370  -8.660  49.896  1.00 29.69  ? 252 GLU A CB  1 
ATOM   2020 C  CG  . GLU A 1 252 ? 35.576  -8.476  51.151  1.00 36.81  ? 252 GLU A CG  1 
ATOM   2021 C  CD  . GLU A 1 252 ? 36.262  -7.652  52.223  1.00 45.79  ? 252 GLU A CD  1 
ATOM   2022 O  OE1 . GLU A 1 252 ? 37.217  -6.883  51.884  1.00 51.29  ? 252 GLU A OE1 1 
ATOM   2023 O  OE2 . GLU A 1 252 ? 35.851  -7.811  53.399  1.00 46.35  ? 252 GLU A OE2 1 
ATOM   2024 N  N   . ASN A 1 253 ? 34.767  -7.797  47.469  1.00 21.39  ? 253 ASN A N   1 
ATOM   2025 C  CA  . ASN A 1 253 ? 33.763  -6.931  46.862  1.00 19.18  ? 253 ASN A CA  1 
ATOM   2026 C  C   . ASN A 1 253 ? 32.812  -7.756  46.001  1.00 18.13  ? 253 ASN A C   1 
ATOM   2027 O  O   . ASN A 1 253 ? 31.639  -7.435  45.937  1.00 15.85  ? 253 ASN A O   1 
ATOM   2028 C  CB  . ASN A 1 253 ? 34.379  -5.821  46.000  1.00 18.13  ? 253 ASN A CB  1 
ATOM   2029 C  CG  . ASN A 1 253 ? 33.325  -4.825  45.538  1.00 17.36  ? 253 ASN A CG  1 
ATOM   2030 O  OD1 . ASN A 1 253 ? 32.914  -4.850  44.375  1.00 17.01  ? 253 ASN A OD1 1 
ATOM   2031 N  ND2 . ASN A 1 253 ? 32.790  -4.043  46.473  1.00 17.06  ? 253 ASN A ND2 1 
ATOM   2032 N  N   . ILE A 1 254 ? 33.319  -8.817  45.340  1.00 16.46  ? 254 ILE A N   1 
ATOM   2033 C  CA  . ILE A 1 254 ? 32.451  -9.669  44.540  1.00 21.52  ? 254 ILE A CA  1 
ATOM   2034 C  C   . ILE A 1 254 ? 31.358  -10.274 45.420  1.00 18.98  ? 254 ILE A C   1 
ATOM   2035 O  O   . ILE A 1 254 ? 30.204  -10.292 45.002  1.00 18.77  ? 254 ILE A O   1 
ATOM   2036 C  CB  . ILE A 1 254 ? 33.236  -10.752 43.759  1.00 22.78  ? 254 ILE A CB  1 
ATOM   2037 C  CG1 . ILE A 1 254 ? 34.109  -10.134 42.668  1.00 25.33  ? 254 ILE A CG1 1 
ATOM   2038 C  CG2 . ILE A 1 254 ? 32.318  -11.795 43.158  1.00 25.08  ? 254 ILE A CG2 1 
ATOM   2039 C  CD1 . ILE A 1 254 ? 35.222  -11.048 42.170  1.00 27.02  ? 254 ILE A CD1 1 
ATOM   2040 N  N   . ARG A 1 255 ? 31.712  -10.690 46.647  1.00 18.11  ? 255 ARG A N   1 
ATOM   2041 C  CA  . ARG A 1 255 ? 30.758  -11.337 47.527  1.00 17.30  ? 255 ARG A CA  1 
ATOM   2042 C  C   . ARG A 1 255 ? 29.661  -10.348 47.903  1.00 17.30  ? 255 ARG A C   1 
ATOM   2043 O  O   . ARG A 1 255 ? 28.485  -10.667 47.891  1.00 15.49  ? 255 ARG A O   1 
ATOM   2044 C  CB  . ARG A 1 255 ? 31.447  -11.883 48.788  1.00 17.15  ? 255 ARG A CB  1 
ATOM   2045 N  N   . TYR A 1 256 ? 30.080  -9.126  48.222  1.00 16.45  ? 256 TYR A N   1 
ATOM   2046 C  CA  . TYR A 1 256 ? 29.172  -8.037  48.539  1.00 17.93  ? 256 TYR A CA  1 
ATOM   2047 C  C   . TYR A 1 256 ? 28.254  -7.698  47.370  1.00 15.87  ? 256 TYR A C   1 
ATOM   2048 O  O   . TYR A 1 256 ? 27.066  -7.474  47.609  1.00 16.26  ? 256 TYR A O   1 
ATOM   2049 C  CB  . TYR A 1 256 ? 29.982  -6.796  48.910  1.00 19.09  ? 256 TYR A CB  1 
ATOM   2050 C  CG  . TYR A 1 256 ? 30.700  -6.914  50.244  1.00 23.51  ? 256 TYR A CG  1 
ATOM   2051 C  CD1 . TYR A 1 256 ? 30.072  -7.493  51.346  1.00 25.63  ? 256 TYR A CD1 1 
ATOM   2052 C  CD2 . TYR A 1 256 ? 32.001  -6.439  50.394  1.00 25.24  ? 256 TYR A CD2 1 
ATOM   2053 C  CE1 . TYR A 1 256 ? 30.715  -7.586  52.565  1.00 28.49  ? 256 TYR A CE1 1 
ATOM   2054 C  CE2 . TYR A 1 256 ? 32.641  -6.502  51.624  1.00 27.71  ? 256 TYR A CE2 1 
ATOM   2055 C  CZ  . TYR A 1 256 ? 32.006  -7.107  52.691  1.00 26.97  ? 256 TYR A CZ  1 
ATOM   2056 O  OH  . TYR A 1 256 ? 32.609  -7.183  53.907  1.00 31.66  ? 256 TYR A OH  1 
ATOM   2057 N  N   . GLN A 1 257 ? 28.792  -7.646  46.136  1.00 14.99  ? 257 GLN A N   1 
ATOM   2058 C  CA  . GLN A 1 257 ? 27.941  -7.412  44.980  1.00 14.19  ? 257 GLN A CA  1 
ATOM   2059 C  C   . GLN A 1 257 ? 26.883  -8.513  44.881  1.00 15.33  ? 257 GLN A C   1 
ATOM   2060 O  O   . GLN A 1 257 ? 25.721  -8.193  44.613  1.00 14.32  ? 257 GLN A O   1 
ATOM   2061 C  CB  . GLN A 1 257 ? 28.713  -7.293  43.670  1.00 13.80  ? 257 GLN A CB  1 
ATOM   2062 C  CG  . GLN A 1 257 ? 29.635  -6.061  43.542  1.00 13.93  ? 257 GLN A CG  1 
ATOM   2063 C  CD  . GLN A 1 257 ? 29.105  -4.695  43.960  1.00 13.37  ? 257 GLN A CD  1 
ATOM   2064 O  OE1 . GLN A 1 257 ? 27.917  -4.420  44.117  1.00 14.03  ? 257 GLN A OE1 1 
ATOM   2065 N  NE2 . GLN A 1 257 ? 30.030  -3.775  44.150  1.00 12.61  ? 257 GLN A NE2 1 
ATOM   2066 N  N   . ILE A 1 258 ? 27.275  -9.788  45.063  1.00 17.18  ? 258 ILE A N   1 
ATOM   2067 C  CA  . ILE A 1 258 ? 26.317  -10.880 44.886  1.00 18.99  ? 258 ILE A CA  1 
ATOM   2068 C  C   . ILE A 1 258 ? 25.151  -10.694 45.854  1.00 20.94  ? 258 ILE A C   1 
ATOM   2069 O  O   . ILE A 1 258 ? 23.982  -10.659 45.448  1.00 21.82  ? 258 ILE A O   1 
ATOM   2070 C  CB  . ILE A 1 258 ? 26.980  -12.271 44.990  1.00 21.85  ? 258 ILE A CB  1 
ATOM   2071 C  CG1 . ILE A 1 258 ? 27.979  -12.476 43.852  1.00 22.67  ? 258 ILE A CG1 1 
ATOM   2072 C  CG2 . ILE A 1 258 ? 25.932  -13.381 45.003  1.00 22.20  ? 258 ILE A CG2 1 
ATOM   2073 C  CD1 . ILE A 1 258 ? 29.116  -13.420 44.179  1.00 23.97  ? 258 ILE A CD1 1 
ATOM   2074 N  N   . ILE A 1 259 ? 25.477  -10.485 47.130  1.00 20.29  ? 259 ILE A N   1 
ATOM   2075 C  CA  . ILE A 1 259 ? 24.464  -10.263 48.136  1.00 21.69  ? 259 ILE A CA  1 
ATOM   2076 C  C   . ILE A 1 259 ? 23.593  -9.055  47.789  1.00 21.71  ? 259 ILE A C   1 
ATOM   2077 O  O   . ILE A 1 259 ? 22.372  -9.123  47.925  1.00 21.83  ? 259 ILE A O   1 
ATOM   2078 C  CB  . ILE A 1 259 ? 25.128  -10.117 49.513  1.00 23.29  ? 259 ILE A CB  1 
ATOM   2079 C  CG1 . ILE A 1 259 ? 25.804  -11.428 49.923  1.00 24.38  ? 259 ILE A CG1 1 
ATOM   2080 C  CG2 . ILE A 1 259 ? 24.106  -9.643  50.543  1.00 25.44  ? 259 ILE A CG2 1 
ATOM   2081 C  CD1 . ILE A 1 259 ? 26.535  -11.360 51.225  1.00 24.76  ? 259 ILE A CD1 1 
ATOM   2082 N  N   . THR A 1 260 ? 24.222  -7.946  47.376  1.00 19.32  ? 260 THR A N   1 
ATOM   2083 C  CA  . THR A 1 260 ? 23.507  -6.722  47.026  1.00 20.27  ? 260 THR A CA  1 
ATOM   2084 C  C   . THR A 1 260 ? 22.468  -6.961  45.928  1.00 20.99  ? 260 THR A C   1 
ATOM   2085 O  O   . THR A 1 260 ? 21.319  -6.561  46.061  1.00 23.02  ? 260 THR A O   1 
ATOM   2086 C  CB  . THR A 1 260 ? 24.486  -5.635  46.571  1.00 20.14  ? 260 THR A CB  1 
ATOM   2087 O  OG1 . THR A 1 260 ? 25.408  -5.402  47.646  1.00 19.56  ? 260 THR A OG1 1 
ATOM   2088 C  CG2 . THR A 1 260 ? 23.795  -4.361  46.150  1.00 21.49  ? 260 THR A CG2 1 
ATOM   2089 N  N   . PHE A 1 261 ? 22.884  -7.606  44.843  1.00 18.76  ? 261 PHE A N   1 
ATOM   2090 C  CA  . PHE A 1 261 ? 22.021  -7.835  43.706  1.00 18.87  ? 261 PHE A CA  1 
ATOM   2091 C  C   . PHE A 1 261 ? 20.927  -8.853  44.066  1.00 22.14  ? 261 PHE A C   1 
ATOM   2092 O  O   . PHE A 1 261 ? 19.772  -8.662  43.695  1.00 22.99  ? 261 PHE A O   1 
ATOM   2093 C  CB  . PHE A 1 261 ? 22.889  -8.203  42.510  1.00 19.15  ? 261 PHE A CB  1 
ATOM   2094 C  CG  . PHE A 1 261 ? 23.435  -7.000  41.782  1.00 20.55  ? 261 PHE A CG  1 
ATOM   2095 C  CD1 . PHE A 1 261 ? 22.616  -6.234  40.972  1.00 18.86  ? 261 PHE A CD1 1 
ATOM   2096 C  CD2 . PHE A 1 261 ? 24.738  -6.583  41.987  1.00 19.81  ? 261 PHE A CD2 1 
ATOM   2097 C  CE1 . PHE A 1 261 ? 23.099  -5.129  40.317  1.00 20.22  ? 261 PHE A CE1 1 
ATOM   2098 C  CE2 . PHE A 1 261 ? 25.237  -5.496  41.299  1.00 19.34  ? 261 PHE A CE2 1 
ATOM   2099 C  CZ  . PHE A 1 261 ? 24.415  -4.756  40.485  1.00 19.27  ? 261 PHE A CZ  1 
ATOM   2100 N  N   . LEU A 1 262 ? 21.271  -9.932  44.779  1.00 22.54  ? 262 LEU A N   1 
ATOM   2101 C  CA  . LEU A 1 262 ? 20.274  -10.925 45.140  1.00 26.76  ? 262 LEU A CA  1 
ATOM   2102 C  C   . LEU A 1 262 ? 19.204  -10.308 46.039  1.00 29.61  ? 262 LEU A C   1 
ATOM   2103 O  O   . LEU A 1 262 ? 18.047  -10.704 45.954  1.00 33.00  ? 262 LEU A O   1 
ATOM   2104 C  CB  . LEU A 1 262 ? 20.921  -12.130 45.826  1.00 25.83  ? 262 LEU A CB  1 
ATOM   2105 C  CG  . LEU A 1 262 ? 21.687  -13.080 44.901  1.00 26.33  ? 262 LEU A CG  1 
ATOM   2106 C  CD1 . LEU A 1 262 ? 22.087  -14.305 45.684  1.00 26.41  ? 262 LEU A CD1 1 
ATOM   2107 C  CD2 . LEU A 1 262 ? 20.869  -13.478 43.669  1.00 25.80  ? 262 LEU A CD2 1 
ATOM   2108 N  N   . GLY A 1 263 ? 19.577  -9.333  46.875  1.00 34.35  ? 263 GLY A N   1 
ATOM   2109 C  CA  . GLY A 1 263 ? 18.608  -8.596  47.683  1.00 32.10  ? 263 GLY A CA  1 
ATOM   2110 C  C   . GLY A 1 263 ? 17.793  -7.585  46.868  1.00 33.00  ? 263 GLY A C   1 
ATOM   2111 O  O   . GLY A 1 263 ? 16.579  -7.737  46.658  1.00 39.24  ? 263 GLY A O   1 
ATOM   2112 N  N   . GLY A 1 264 ? 18.456  -6.527  46.401  1.00 30.02  ? 264 GLY A N   1 
ATOM   2113 C  CA  . GLY A 1 264 ? 17.754  -5.431  45.757  1.00 27.19  ? 264 GLY A CA  1 
ATOM   2114 C  C   . GLY A 1 264 ? 17.240  -5.811  44.370  1.00 25.45  ? 264 GLY A C   1 
ATOM   2115 O  O   . GLY A 1 264 ? 16.340  -5.177  43.817  1.00 20.90  ? 264 GLY A O   1 
ATOM   2116 N  N   . GLY A 1 265 ? 17.848  -6.845  43.786  1.00 22.45  ? 265 GLY A N   1 
ATOM   2117 C  CA  . GLY A 1 265 ? 17.377  -7.360  42.510  1.00 22.67  ? 265 GLY A CA  1 
ATOM   2118 C  C   . GLY A 1 265 ? 15.930  -7.877  42.499  1.00 23.42  ? 265 GLY A C   1 
ATOM   2119 O  O   . GLY A 1 265 ? 15.367  -8.016  41.414  1.00 28.66  ? 265 GLY A O   1 
ATOM   2120 N  N   . HIS A 1 266 ? 15.296  -8.120  43.656  1.00 22.45  ? 266 HIS A N   1 
ATOM   2121 C  CA  . HIS A 1 266 ? 13.985  -8.768  43.660  1.00 21.25  ? 266 HIS A CA  1 
ATOM   2122 C  C   . HIS A 1 266 ? 12.896  -8.018  44.442  1.00 19.89  ? 266 HIS A C   1 
ATOM   2123 O  O   . HIS A 1 266 ? 11.766  -7.941  44.008  1.00 17.72  ? 266 HIS A O   1 
ATOM   2124 C  CB  . HIS A 1 266 ? 14.064  -10.207 44.186  1.00 18.34  ? 266 HIS A CB  1 
ATOM   2125 C  CG  . HIS A 1 266 ? 14.201  -10.373 45.645  1.00 18.98  ? 266 HIS A CG  1 
ATOM   2126 N  ND1 . HIS A 1 266 ? 15.421  -10.378 46.287  1.00 19.08  ? 266 HIS A ND1 1 
ATOM   2127 C  CD2 . HIS A 1 266 ? 13.271  -10.646 46.604  1.00 21.91  ? 266 HIS A CD2 1 
ATOM   2128 C  CE1 . HIS A 1 266 ? 15.215  -10.572 47.593  1.00 20.86  ? 266 HIS A CE1 1 
ATOM   2129 N  NE2 . HIS A 1 266 ? 13.916  -10.764 47.799  1.00 22.02  ? 266 HIS A NE2 1 
ATOM   2130 N  N   . GLU A 1 267 ? 13.191  -7.564  45.652  1.00 21.29  ? 267 GLU A N   1 
ATOM   2131 C  CA  . GLU A 1 267 ? 12.140  -7.123  46.552  1.00 24.14  ? 267 GLU A CA  1 
ATOM   2132 C  C   . GLU A 1 267 ? 11.365  -5.901  45.982  1.00 21.71  ? 267 GLU A C   1 
ATOM   2133 O  O   . GLU A 1 267 ? 10.128  -5.865  45.958  1.00 22.09  ? 267 GLU A O   1 
ATOM   2134 C  CB  . GLU A 1 267 ? 12.802  -6.828  47.906  1.00 32.15  ? 267 GLU A CB  1 
ATOM   2135 C  CG  . GLU A 1 267 ? 11.880  -6.149  48.898  1.00 39.51  ? 267 GLU A CG  1 
ATOM   2136 C  CD  . GLU A 1 267 ? 10.604  -6.922  49.209  1.00 51.33  ? 267 GLU A CD  1 
ATOM   2137 O  OE1 . GLU A 1 267 ? 10.577  -8.156  48.911  1.00 48.52  ? 267 GLU A OE1 1 
ATOM   2138 O  OE2 . GLU A 1 267 ? 9.624   -6.285  49.734  1.00 53.62  ? 267 GLU A OE2 1 
ATOM   2139 N  N   . THR A 1 268 ? 12.066  -4.876  45.504  1.00 17.67  ? 268 THR A N   1 
ATOM   2140 C  CA  . THR A 1 268 ? 11.375  -3.713  44.968  1.00 15.67  ? 268 THR A CA  1 
ATOM   2141 C  C   . THR A 1 268 ? 10.547  -4.070  43.734  1.00 13.88  ? 268 THR A C   1 
ATOM   2142 O  O   . THR A 1 268 ? 9.468   -3.513  43.533  1.00 14.94  ? 268 THR A O   1 
ATOM   2143 C  CB  . THR A 1 268 ? 12.343  -2.578  44.607  1.00 16.48  ? 268 THR A CB  1 
ATOM   2144 O  OG1 . THR A 1 268 ? 13.473  -3.231  44.036  1.00 16.64  ? 268 THR A OG1 1 
ATOM   2145 C  CG2 . THR A 1 268 ? 12.749  -1.725  45.783  1.00 18.14  ? 268 THR A CG2 1 
ATOM   2146 N  N   . THR A 1 269 ? 11.071  -4.935  42.872  1.00 15.28  ? 269 THR A N   1 
ATOM   2147 C  CA  . THR A 1 269 ? 10.348  -5.378  41.683  1.00 14.66  ? 269 THR A CA  1 
ATOM   2148 C  C   . THR A 1 269 ? 9.071   -6.137  42.059  1.00 14.36  ? 269 THR A C   1 
ATOM   2149 O  O   . THR A 1 269 ? 8.067   -5.991  41.390  1.00 13.65  ? 269 THR A O   1 
ATOM   2150 C  CB  . THR A 1 269 ? 11.267  -6.163  40.731  1.00 14.46  ? 269 THR A CB  1 
ATOM   2151 O  OG1 . THR A 1 269 ? 12.456  -5.398  40.489  1.00 12.29  ? 269 THR A OG1 1 
ATOM   2152 C  CG2 . THR A 1 269 ? 10.584  -6.452  39.407  1.00 13.66  ? 269 THR A CG2 1 
ATOM   2153 N  N   . SER A 1 270 ? 9.113   -6.983  43.099  1.00 14.99  ? 270 SER A N   1 
ATOM   2154 C  CA  . SER A 1 270 ? 7.957   -7.790  43.452  1.00 15.93  ? 270 SER A CA  1 
ATOM   2155 C  C   . SER A 1 270 ? 6.881   -6.908  44.069  1.00 14.69  ? 270 SER A C   1 
ATOM   2156 O  O   . SER A 1 270 ? 5.690   -7.126  43.833  1.00 14.32  ? 270 SER A O   1 
ATOM   2157 C  CB  . SER A 1 270 ? 8.277   -8.909  44.400  1.00 16.74  ? 270 SER A CB  1 
ATOM   2158 O  OG  . SER A 1 270 ? 8.866   -8.388  45.563  1.00 18.78  ? 270 SER A OG  1 
ATOM   2159 N  N   . GLY A 1 271 ? 7.319   -5.898  44.827  1.00 14.09  ? 271 GLY A N   1 
ATOM   2160 C  CA  . GLY A 1 271 ? 6.406   -4.849  45.251  1.00 13.79  ? 271 GLY A CA  1 
ATOM   2161 C  C   . GLY A 1 271 ? 5.679   -4.160  44.087  1.00 12.96  ? 271 GLY A C   1 
ATOM   2162 O  O   . GLY A 1 271 ? 4.449   -3.980  44.115  1.00 12.08  ? 271 GLY A O   1 
ATOM   2163 N  N   . LEU A 1 272 ? 6.457   -3.679  43.105  1.00 13.37  ? 272 LEU A N   1 
ATOM   2164 C  CA  . LEU A 1 272 ? 5.919   -3.020  41.910  1.00 13.11  ? 272 LEU A CA  1 
ATOM   2165 C  C   . LEU A 1 272 ? 4.837   -3.895  41.259  1.00 12.57  ? 272 LEU A C   1 
ATOM   2166 O  O   . LEU A 1 272 ? 3.738   -3.427  40.979  1.00 10.91  ? 272 LEU A O   1 
ATOM   2167 C  CB  . LEU A 1 272 ? 7.020   -2.732  40.898  1.00 13.10  ? 272 LEU A CB  1 
ATOM   2168 C  CG  . LEU A 1 272 ? 6.571   -2.209  39.526  1.00 14.55  ? 272 LEU A CG  1 
ATOM   2169 C  CD1 . LEU A 1 272 ? 5.606   -1.015  39.646  1.00 15.00  ? 272 LEU A CD1 1 
ATOM   2170 C  CD2 . LEU A 1 272 ? 7.775   -1.832  38.699  1.00 13.56  ? 272 LEU A CD2 1 
ATOM   2171 N  N   . LEU A 1 273 ? 5.153   -5.170  41.000  1.00 12.90  ? 273 LEU A N   1 
ATOM   2172 C  CA  . LEU A 1 273 ? 4.171   -6.030  40.340  1.00 12.45  ? 273 LEU A CA  1 
ATOM   2173 C  C   . LEU A 1 273 ? 2.912   -6.161  41.180  1.00 11.97  ? 273 LEU A C   1 
ATOM   2174 O  O   . LEU A 1 273 ? 1.803   -6.157  40.626  1.00 11.33  ? 273 LEU A O   1 
ATOM   2175 C  CB  . LEU A 1 273 ? 4.809   -7.384  40.053  1.00 12.74  ? 273 LEU A CB  1 
ATOM   2176 C  CG  . LEU A 1 273 ? 5.597   -7.434  38.755  1.00 13.81  ? 273 LEU A CG  1 
ATOM   2177 C  CD1 . LEU A 1 273 ? 6.549   -8.619  38.721  1.00 15.55  ? 273 LEU A CD1 1 
ATOM   2178 C  CD2 . LEU A 1 273 ? 4.658   -7.516  37.560  1.00 15.62  ? 273 LEU A CD2 1 
ATOM   2179 N  N   . SER A 1 274 ? 3.084   -6.257  42.508  1.00 11.47  ? 274 SER A N   1 
ATOM   2180 C  CA  . SER A 1 274 ? 1.975   -6.457  43.423  1.00 10.90  ? 274 SER A CA  1 
ATOM   2181 C  C   . SER A 1 274 ? 1.090   -5.225  43.432  1.00 11.25  ? 274 SER A C   1 
ATOM   2182 O  O   . SER A 1 274 ? -0.165  -5.334  43.432  1.00 10.53  ? 274 SER A O   1 
ATOM   2183 C  CB  . SER A 1 274 ? 2.463   -6.831  44.791  1.00 11.10  ? 274 SER A CB  1 
ATOM   2184 O  OG  . SER A 1 274 ? 3.199   -8.089  44.743  1.00 11.89  ? 274 SER A OG  1 
ATOM   2185 N  N   . PHE A 1 275 ? 1.718   -4.027  43.509  1.00 9.75   ? 275 PHE A N   1 
ATOM   2186 C  CA  . PHE A 1 275 ? 0.917   -2.807  43.477  1.00 10.38  ? 275 PHE A CA  1 
ATOM   2187 C  C   . PHE A 1 275 ? 0.212   -2.615  42.123  1.00 9.64   ? 275 PHE A C   1 
ATOM   2188 O  O   . PHE A 1 275 ? -0.934  -2.151  41.988  1.00 10.73  ? 275 PHE A O   1 
ATOM   2189 C  CB  . PHE A 1 275 ? 1.795   -1.584  43.785  1.00 12.25  ? 275 PHE A CB  1 
ATOM   2190 C  CG  . PHE A 1 275 ? 2.033   -1.358  45.252  1.00 12.37  ? 275 PHE A CG  1 
ATOM   2191 C  CD1 . PHE A 1 275 ? 1.006   -1.018  46.092  1.00 13.49  ? 275 PHE A CD1 1 
ATOM   2192 C  CD2 . PHE A 1 275 ? 3.317   -1.484  45.779  1.00 13.42  ? 275 PHE A CD2 1 
ATOM   2193 C  CE1 . PHE A 1 275 ? 1.211   -0.863  47.448  1.00 13.81  ? 275 PHE A CE1 1 
ATOM   2194 C  CE2 . PHE A 1 275 ? 3.524   -1.292  47.130  1.00 13.45  ? 275 PHE A CE2 1 
ATOM   2195 C  CZ  . PHE A 1 275 ? 2.482   -0.982  47.953  1.00 13.34  ? 275 PHE A CZ  1 
ATOM   2196 N  N   . ALA A 1 276 ? 0.905   -2.946  41.061  1.00 11.08  ? 276 ALA A N   1 
ATOM   2197 C  CA  . ALA A 1 276 ? 0.302   -2.799  39.752  1.00 11.62  ? 276 ALA A CA  1 
ATOM   2198 C  C   . ALA A 1 276 ? -0.950  -3.666  39.680  1.00 13.61  ? 276 ALA A C   1 
ATOM   2199 O  O   . ALA A 1 276 ? -2.010  -3.170  39.276  1.00 13.15  ? 276 ALA A O   1 
ATOM   2200 C  CB  . ALA A 1 276 ? 1.264   -3.215  38.664  1.00 12.15  ? 276 ALA A CB  1 
ATOM   2201 N  N   . LEU A 1 277 ? -0.837  -4.948  40.097  1.00 12.64  ? 277 LEU A N   1 
ATOM   2202 C  CA  . LEU A 1 277 ? -1.989  -5.819  40.000  1.00 13.50  ? 277 LEU A CA  1 
ATOM   2203 C  C   . LEU A 1 277 ? -3.125  -5.304  40.871  1.00 12.52  ? 277 LEU A C   1 
ATOM   2204 O  O   . LEU A 1 277 ? -4.255  -5.406  40.435  1.00 12.34  ? 277 LEU A O   1 
ATOM   2205 C  CB  . LEU A 1 277 ? -1.665  -7.274  40.342  1.00 15.51  ? 277 LEU A CB  1 
ATOM   2206 C  CG  . LEU A 1 277 ? -2.836  -8.237  40.146  1.00 16.24  ? 277 LEU A CG  1 
ATOM   2207 C  CD1 . LEU A 1 277 ? -3.463  -8.083  38.781  1.00 16.08  ? 277 LEU A CD1 1 
ATOM   2208 C  CD2 . LEU A 1 277 ? -2.379  -9.701  40.289  1.00 17.29  ? 277 LEU A CD2 1 
ATOM   2209 N  N   . TYR A 1 278 ? -2.807  -4.854  42.091  1.00 12.94  ? 278 TYR A N   1 
ATOM   2210 C  CA  . TYR A 1 278 ? -3.724  -4.150  42.971  1.00 14.36  ? 278 TYR A CA  1 
ATOM   2211 C  C   . TYR A 1 278 ? -4.485  -3.071  42.199  1.00 14.49  ? 278 TYR A C   1 
ATOM   2212 O  O   . TYR A 1 278 ? -5.728  -3.076  42.159  1.00 14.42  ? 278 TYR A O   1 
ATOM   2213 C  CB  . TYR A 1 278 ? -3.061  -3.574  44.237  1.00 13.51  ? 278 TYR A CB  1 
ATOM   2214 C  CG  . TYR A 1 278 ? -3.972  -2.631  45.026  1.00 13.74  ? 278 TYR A CG  1 
ATOM   2215 C  CD1 . TYR A 1 278 ? -4.954  -3.117  45.884  1.00 15.28  ? 278 TYR A CD1 1 
ATOM   2216 C  CD2 . TYR A 1 278 ? -3.898  -1.258  44.857  1.00 14.70  ? 278 TYR A CD2 1 
ATOM   2217 C  CE1 . TYR A 1 278 ? -5.815  -2.259  46.560  1.00 17.25  ? 278 TYR A CE1 1 
ATOM   2218 C  CE2 . TYR A 1 278 ? -4.734  -0.391  45.545  1.00 15.89  ? 278 TYR A CE2 1 
ATOM   2219 C  CZ  . TYR A 1 278 ? -5.707  -0.883  46.398  1.00 17.47  ? 278 TYR A CZ  1 
ATOM   2220 O  OH  . TYR A 1 278 ? -6.573  0.003   47.069  1.00 17.26  ? 278 TYR A OH  1 
ATOM   2221 N  N   . PHE A 1 279 ? -3.770  -2.060  41.688  1.00 15.19  ? 279 PHE A N   1 
ATOM   2222 C  CA  . PHE A 1 279 ? -4.463  -0.967  41.043  1.00 14.34  ? 279 PHE A CA  1 
ATOM   2223 C  C   . PHE A 1 279 ? -5.301  -1.427  39.845  1.00 13.62  ? 279 PHE A C   1 
ATOM   2224 O  O   . PHE A 1 279 ? -6.375  -0.900  39.612  1.00 14.04  ? 279 PHE A O   1 
ATOM   2225 C  CB  . PHE A 1 279 ? -3.455  0.117   40.639  1.00 15.46  ? 279 PHE A CB  1 
ATOM   2226 C  CG  . PHE A 1 279 ? -2.958  0.941   41.787  1.00 14.67  ? 279 PHE A CG  1 
ATOM   2227 C  CD1 . PHE A 1 279 ? -3.854  1.641   42.570  1.00 15.08  ? 279 PHE A CD1 1 
ATOM   2228 C  CD2 . PHE A 1 279 ? -1.610  0.987   42.079  1.00 14.86  ? 279 PHE A CD2 1 
ATOM   2229 C  CE1 . PHE A 1 279 ? -3.390  2.372   43.642  1.00 15.66  ? 279 PHE A CE1 1 
ATOM   2230 C  CE2 . PHE A 1 279 ? -1.149  1.734   43.134  1.00 15.16  ? 279 PHE A CE2 1 
ATOM   2231 C  CZ  . PHE A 1 279 ? -2.044  2.434   43.893  1.00 16.43  ? 279 PHE A CZ  1 
ATOM   2232 N  N   . LEU A 1 280 ? -4.847  -2.423  39.082  1.00 14.13  ? 280 LEU A N   1 
ATOM   2233 C  CA  . LEU A 1 280 ? -5.593  -2.918  37.939  1.00 14.81  ? 280 LEU A CA  1 
ATOM   2234 C  C   . LEU A 1 280 ? -6.939  -3.480  38.385  1.00 15.49  ? 280 LEU A C   1 
ATOM   2235 O  O   . LEU A 1 280 ? -7.957  -3.175  37.766  1.00 15.40  ? 280 LEU A O   1 
ATOM   2236 C  CB  . LEU A 1 280 ? -4.751  -3.993  37.247  1.00 15.27  ? 280 LEU A CB  1 
ATOM   2237 C  CG  . LEU A 1 280 ? -3.534  -3.426  36.538  1.00 17.46  ? 280 LEU A CG  1 
ATOM   2238 C  CD1 . LEU A 1 280 ? -2.573  -4.519  36.102  1.00 17.96  ? 280 LEU A CD1 1 
ATOM   2239 C  CD2 . LEU A 1 280 ? -3.997  -2.629  35.350  1.00 18.66  ? 280 LEU A CD2 1 
ATOM   2240 N  N   . VAL A 1 281 ? -6.975  -4.256  39.481  1.00 14.71  ? 281 VAL A N   1 
ATOM   2241 C  CA  . VAL A 1 281 ? -8.229  -4.888  39.867  1.00 15.90  ? 281 VAL A CA  1 
ATOM   2242 C  C   . VAL A 1 281 ? -9.133  -3.828  40.490  1.00 15.97  ? 281 VAL A C   1 
ATOM   2243 O  O   . VAL A 1 281 ? -10.344 -3.936  40.416  1.00 18.26  ? 281 VAL A O   1 
ATOM   2244 C  CB  . VAL A 1 281 ? -8.080  -6.153  40.747  1.00 16.59  ? 281 VAL A CB  1 
ATOM   2245 C  CG1 . VAL A 1 281 ? -7.283  -7.226  40.011  1.00 17.97  ? 281 VAL A CG1 1 
ATOM   2246 C  CG2 . VAL A 1 281 ? -7.507  -5.924  42.117  1.00 16.19  ? 281 VAL A CG2 1 
ATOM   2247 N  N   . LYS A 1 282 ? -8.548  -2.784  41.062  1.00 14.98  ? 282 LYS A N   1 
ATOM   2248 C  CA  . LYS A 1 282 ? -9.330  -1.667  41.569  1.00 16.49  ? 282 LYS A CA  1 
ATOM   2249 C  C   . LYS A 1 282 ? -9.806  -0.730  40.457  1.00 15.40  ? 282 LYS A C   1 
ATOM   2250 O  O   . LYS A 1 282 ? -10.719 0.045   40.696  1.00 18.14  ? 282 LYS A O   1 
ATOM   2251 C  CB  . LYS A 1 282 ? -8.550  -0.883  42.634  1.00 18.15  ? 282 LYS A CB  1 
ATOM   2252 C  CG  . LYS A 1 282 ? -8.260  -1.671  43.908  1.00 19.52  ? 282 LYS A CG  1 
ATOM   2253 C  CD  . LYS A 1 282 ? -9.478  -2.062  44.722  1.00 20.35  ? 282 LYS A CD  1 
ATOM   2254 C  CE  . LYS A 1 282 ? -9.111  -2.828  45.975  1.00 20.87  ? 282 LYS A CE  1 
ATOM   2255 N  NZ  . LYS A 1 282 ? -10.267 -3.500  46.603  1.00 20.03  ? 282 LYS A NZ  1 
ATOM   2256 N  N   . ASN A 1 283 ? -9.236  -0.816  39.251  1.00 13.73  ? 283 ASN A N   1 
ATOM   2257 C  CA  . ASN A 1 283 ? -9.582  0.093   38.177  1.00 13.76  ? 283 ASN A CA  1 
ATOM   2258 C  C   . ASN A 1 283 ? -9.872  -0.723  36.929  1.00 12.53  ? 283 ASN A C   1 
ATOM   2259 O  O   . ASN A 1 283 ? -9.035  -0.808  36.059  1.00 13.91  ? 283 ASN A O   1 
ATOM   2260 C  CB  . ASN A 1 283 ? -8.502  1.155   37.967  1.00 13.92  ? 283 ASN A CB  1 
ATOM   2261 C  CG  . ASN A 1 283 ? -8.343  2.008   39.193  1.00 14.29  ? 283 ASN A CG  1 
ATOM   2262 O  OD1 . ASN A 1 283 ? -9.063  2.973   39.360  1.00 14.39  ? 283 ASN A OD1 1 
ATOM   2263 N  ND2 . ASN A 1 283 ? -7.548  1.546   40.129  1.00 14.48  ? 283 ASN A ND2 1 
ATOM   2264 N  N   . PRO A 1 284 ? -11.043 -1.395  36.834  1.00 13.90  ? 284 PRO A N   1 
ATOM   2265 C  CA  . PRO A 1 284 ? -11.327 -2.306  35.729  1.00 16.19  ? 284 PRO A CA  1 
ATOM   2266 C  C   . PRO A 1 284 ? -11.184 -1.714  34.321  1.00 14.21  ? 284 PRO A C   1 
ATOM   2267 O  O   . PRO A 1 284 ? -10.830 -2.461  33.412  1.00 13.12  ? 284 PRO A O   1 
ATOM   2268 C  CB  . PRO A 1 284 ? -12.776 -2.782  35.969  1.00 15.68  ? 284 PRO A CB  1 
ATOM   2269 C  CG  . PRO A 1 284 ? -13.065 -2.441  37.420  1.00 15.82  ? 284 PRO A CG  1 
ATOM   2270 C  CD  . PRO A 1 284 ? -12.156 -1.289  37.790  1.00 15.80  ? 284 PRO A CD  1 
ATOM   2271 N  N   . HIS A 1 285 ? -11.473 -0.408  34.133  1.00 14.21  ? 285 HIS A N   1 
ATOM   2272 C  CA  . HIS A 1 285 ? -11.292 0.228   32.828  1.00 15.35  ? 285 HIS A CA  1 
ATOM   2273 C  C   . HIS A 1 285 ? -9.817  0.282   32.439  1.00 15.98  ? 285 HIS A C   1 
ATOM   2274 O  O   . HIS A 1 285 ? -9.488  0.106   31.277  1.00 18.21  ? 285 HIS A O   1 
ATOM   2275 C  CB  . HIS A 1 285 ? -11.878 1.641   32.776  1.00 16.29  ? 285 HIS A CB  1 
ATOM   2276 C  CG  . HIS A 1 285 ? -13.352 1.636   32.925  1.00 17.40  ? 285 HIS A CG  1 
ATOM   2277 N  ND1 . HIS A 1 285 ? -14.029 2.511   33.741  1.00 20.46  ? 285 HIS A ND1 1 
ATOM   2278 C  CD2 . HIS A 1 285 ? -14.274 0.880   32.361  1.00 18.63  ? 285 HIS A CD2 1 
ATOM   2279 C  CE1 . HIS A 1 285 ? -15.327 2.276   33.636  1.00 16.54  ? 285 HIS A CE1 1 
ATOM   2280 N  NE2 . HIS A 1 285 ? -15.500 1.316   32.796  1.00 18.14  ? 285 HIS A NE2 1 
ATOM   2281 N  N   . VAL A 1 286 ? -8.913  0.468   33.403  1.00 15.47  ? 286 VAL A N   1 
ATOM   2282 C  CA  . VAL A 1 286 ? -7.483  0.396   33.122  1.00 15.87  ? 286 VAL A CA  1 
ATOM   2283 C  C   . VAL A 1 286 ? -7.089  -1.060  32.860  1.00 15.11  ? 286 VAL A C   1 
ATOM   2284 O  O   . VAL A 1 286 ? -6.291  -1.328  31.970  1.00 14.20  ? 286 VAL A O   1 
ATOM   2285 C  CB  . VAL A 1 286 ? -6.647  0.992   34.267  1.00 16.05  ? 286 VAL A CB  1 
ATOM   2286 C  CG1 . VAL A 1 286 ? -5.175  0.751   34.022  1.00 16.69  ? 286 VAL A CG1 1 
ATOM   2287 C  CG2 . VAL A 1 286 ? -6.955  2.467   34.481  1.00 17.37  ? 286 VAL A CG2 1 
ATOM   2288 N  N   . LEU A 1 287 ? -7.661  -2.004  33.621  1.00 15.85  ? 287 LEU A N   1 
ATOM   2289 C  CA  . LEU A 1 287 ? -7.368  -3.426  33.410  1.00 16.22  ? 287 LEU A CA  1 
ATOM   2290 C  C   . LEU A 1 287 ? -7.760  -3.796  31.987  1.00 15.64  ? 287 LEU A C   1 
ATOM   2291 O  O   . LEU A 1 287 ? -6.977  -4.385  31.278  1.00 13.58  ? 287 LEU A O   1 
ATOM   2292 C  CB  . LEU A 1 287 ? -8.085  -4.274  34.470  1.00 16.85  ? 287 LEU A CB  1 
ATOM   2293 C  CG  . LEU A 1 287 ? -8.043  -5.813  34.357  1.00 18.73  ? 287 LEU A CG  1 
ATOM   2294 C  CD1 . LEU A 1 287 ? -6.653  -6.345  34.168  1.00 19.82  ? 287 LEU A CD1 1 
ATOM   2295 C  CD2 . LEU A 1 287 ? -8.599  -6.423  35.628  1.00 21.61  ? 287 LEU A CD2 1 
ATOM   2296 N  N   . GLN A 1 288 ? -8.949  -3.394  31.530  1.00 15.69  ? 288 GLN A N   1 
ATOM   2297 C  CA  . GLN A 1 288 ? -9.330  -3.746  30.173  1.00 17.48  ? 288 GLN A CA  1 
ATOM   2298 C  C   . GLN A 1 288 ? -8.375  -3.115  29.155  1.00 15.50  ? 288 GLN A C   1 
ATOM   2299 O  O   . GLN A 1 288 ? -8.143  -3.731  28.149  1.00 16.69  ? 288 GLN A O   1 
ATOM   2300 C  CB  . GLN A 1 288 ? -10.773 -3.354  29.850  1.00 23.48  ? 288 GLN A CB  1 
ATOM   2301 C  CG  . GLN A 1 288 ? -11.340 -4.077  28.635  1.00 31.88  ? 288 GLN A CG  1 
ATOM   2302 C  CD  . GLN A 1 288 ? -11.682 -5.533  28.889  1.00 42.17  ? 288 GLN A CD  1 
ATOM   2303 O  OE1 . GLN A 1 288 ? -11.716 -6.016  30.026  1.00 49.91  ? 288 GLN A OE1 1 
ATOM   2304 N  NE2 . GLN A 1 288 ? -11.976 -6.251  27.811  1.00 46.64  ? 288 GLN A NE2 1 
ATOM   2305 N  N   . LYS A 1 289 ? -7.909  -1.878  29.338  1.00 14.01  ? 289 LYS A N   1 
ATOM   2306 C  CA  . LYS A 1 289 ? -7.008  -1.266  28.366  1.00 14.67  ? 289 LYS A CA  1 
ATOM   2307 C  C   . LYS A 1 289 ? -5.685  -2.028  28.318  1.00 14.22  ? 289 LYS A C   1 
ATOM   2308 O  O   . LYS A 1 289 ? -5.170  -2.324  27.250  1.00 15.13  ? 289 LYS A O   1 
ATOM   2309 C  CB  . LYS A 1 289 ? -6.695  0.187   28.719  1.00 14.87  ? 289 LYS A CB  1 
ATOM   2310 C  CG  . LYS A 1 289 ? -7.841  1.147   28.471  1.00 16.62  ? 289 LYS A CG  1 
ATOM   2311 C  CD  . LYS A 1 289 ? -7.533  2.590   28.850  1.00 16.73  ? 289 LYS A CD  1 
ATOM   2312 C  CE  . LYS A 1 289 ? -8.671  3.511   28.481  1.00 17.76  ? 289 LYS A CE  1 
ATOM   2313 N  NZ  . LYS A 1 289 ? -9.879  3.192   29.261  1.00 19.62  ? 289 LYS A NZ  1 
ATOM   2314 N  N   . ALA A 1 290 ? -5.129  -2.319  29.486  1.00 14.56  ? 290 ALA A N   1 
ATOM   2315 C  CA  . ALA A 1 290 ? -3.906  -3.093  29.581  1.00 15.23  ? 290 ALA A CA  1 
ATOM   2316 C  C   . ALA A 1 290 ? -4.051  -4.499  28.981  1.00 14.33  ? 290 ALA A C   1 
ATOM   2317 O  O   . ALA A 1 290 ? -3.162  -4.978  28.278  1.00 13.48  ? 290 ALA A O   1 
ATOM   2318 C  CB  . ALA A 1 290 ? -3.551  -3.155  31.040  1.00 15.89  ? 290 ALA A CB  1 
ATOM   2319 N  N   . ALA A 1 291 ? -5.170  -5.181  29.262  1.00 14.39  ? 291 ALA A N   1 
ATOM   2320 C  CA  . ALA A 1 291 ? -5.370  -6.538  28.784  1.00 15.59  ? 291 ALA A CA  1 
ATOM   2321 C  C   . ALA A 1 291 ? -5.538  -6.528  27.265  1.00 17.97  ? 291 ALA A C   1 
ATOM   2322 O  O   . ALA A 1 291 ? -5.057  -7.443  26.605  1.00 17.52  ? 291 ALA A O   1 
ATOM   2323 C  CB  . ALA A 1 291 ? -6.543  -7.215  29.467  1.00 15.13  ? 291 ALA A CB  1 
ATOM   2324 N  N   . GLU A 1 292 ? -6.184  -5.488  26.720  1.00 19.72  ? 292 GLU A N   1 
ATOM   2325 C  CA  . GLU A 1 292 ? -6.384  -5.369  25.276  1.00 20.11  ? 292 GLU A CA  1 
ATOM   2326 C  C   . GLU A 1 292 ? -5.034  -5.208  24.594  1.00 19.83  ? 292 GLU A C   1 
ATOM   2327 O  O   . GLU A 1 292 ? -4.765  -5.837  23.576  1.00 20.42  ? 292 GLU A O   1 
ATOM   2328 C  CB  . GLU A 1 292 ? -7.298  -4.178  24.954  1.00 24.08  ? 292 GLU A CB  1 
ATOM   2329 C  CG  . GLU A 1 292 ? -7.699  -4.007  23.501  1.00 29.75  ? 292 GLU A CG  1 
ATOM   2330 C  CD  . GLU A 1 292 ? -6.673  -3.465  22.508  1.00 32.34  ? 292 GLU A CD  1 
ATOM   2331 O  OE1 . GLU A 1 292 ? -5.860  -2.542  22.849  1.00 33.50  ? 292 GLU A OE1 1 
ATOM   2332 O  OE2 . GLU A 1 292 ? -6.675  -3.978  21.366  1.00 38.62  ? 292 GLU A OE2 1 
ATOM   2333 N  N   . GLU A 1 293 ? -4.181  -4.351  25.167  1.00 19.22  ? 293 GLU A N   1 
ATOM   2334 C  CA  . GLU A 1 293 ? -2.841  -4.184  24.650  1.00 19.86  ? 293 GLU A CA  1 
ATOM   2335 C  C   . GLU A 1 293 ? -2.125  -5.534  24.610  1.00 17.00  ? 293 GLU A C   1 
ATOM   2336 O  O   . GLU A 1 293 ? -1.553  -5.893  23.586  1.00 16.03  ? 293 GLU A O   1 
ATOM   2337 C  CB  . GLU A 1 293 ? -2.030  -3.169  25.455  1.00 19.65  ? 293 GLU A CB  1 
ATOM   2338 C  CG  . GLU A 1 293 ? -0.700  -2.902  24.784  1.00 22.08  ? 293 GLU A CG  1 
ATOM   2339 C  CD  . GLU A 1 293 ? 0.219   -1.951  25.523  1.00 23.09  ? 293 GLU A CD  1 
ATOM   2340 O  OE1 . GLU A 1 293 ? 0.679   -2.358  26.634  1.00 24.15  ? 293 GLU A OE1 1 
ATOM   2341 O  OE2 . GLU A 1 293 ? 0.486   -0.796  24.984  1.00 21.59  ? 293 GLU A OE2 1 
ATOM   2342 N  N   . ALA A 1 294 ? -2.187  -6.274  25.709  1.00 16.95  ? 294 ALA A N   1 
ATOM   2343 C  CA  . ALA A 1 294 ? -1.441  -7.527  25.820  1.00 17.25  ? 294 ALA A CA  1 
ATOM   2344 C  C   . ALA A 1 294 ? -1.929  -8.523  24.769  1.00 17.92  ? 294 ALA A C   1 
ATOM   2345 O  O   . ALA A 1 294 ? -1.126  -9.176  24.120  1.00 18.47  ? 294 ALA A O   1 
ATOM   2346 C  CB  . ALA A 1 294 ? -1.602  -8.081  27.203  1.00 17.80  ? 294 ALA A CB  1 
ATOM   2347 N  N   . ALA A 1 295 ? -3.254  -8.610  24.604  1.00 17.54  ? 295 ALA A N   1 
ATOM   2348 C  CA  . ALA A 1 295 ? -3.837  -9.480  23.600  1.00 19.12  ? 295 ALA A CA  1 
ATOM   2349 C  C   . ALA A 1 295 ? -3.438  -9.036  22.198  1.00 18.28  ? 295 ALA A C   1 
ATOM   2350 O  O   . ALA A 1 295 ? -3.096  -9.884  21.386  1.00 21.35  ? 295 ALA A O   1 
ATOM   2351 C  CB  . ALA A 1 295 ? -5.332  -9.596  23.776  1.00 18.53  ? 295 ALA A CB  1 
ATOM   2352 N  N   . ARG A 1 296 ? -3.356  -7.732  21.929  1.00 20.11  ? 296 ARG A N   1 
ATOM   2353 C  CA  . ARG A 1 296 ? -3.016  -7.267  20.592  1.00 22.18  ? 296 ARG A CA  1 
ATOM   2354 C  C   . ARG A 1 296 ? -1.522  -7.446  20.273  1.00 21.66  ? 296 ARG A C   1 
ATOM   2355 O  O   . ARG A 1 296 ? -1.186  -7.634  19.105  1.00 18.43  ? 296 ARG A O   1 
ATOM   2356 C  CB  . ARG A 1 296 ? -3.461  -5.800  20.460  1.00 25.15  ? 296 ARG A CB  1 
ATOM   2357 C  CG  . ARG A 1 296 ? -2.955  -5.075  19.226  1.00 28.19  ? 296 ARG A CG  1 
ATOM   2358 C  CD  . ARG A 1 296 ? -3.773  -3.815  18.977  1.00 31.35  ? 296 ARG A CD  1 
ATOM   2359 N  NE  . ARG A 1 296 ? -3.987  -3.068  20.212  1.00 31.25  ? 296 ARG A NE  1 
ATOM   2360 C  CZ  . ARG A 1 296 ? -3.115  -2.237  20.782  1.00 36.85  ? 296 ARG A CZ  1 
ATOM   2361 N  NH1 . ARG A 1 296 ? -2.014  -1.863  20.142  1.00 36.88  ? 296 ARG A NH1 1 
ATOM   2362 N  NH2 . ARG A 1 296 ? -3.376  -1.742  21.988  1.00 36.80  ? 296 ARG A NH2 1 
ATOM   2363 N  N   . ILE A 1 297 ? -0.625  -7.364  21.282  1.00 18.15  ? 297 ILE A N   1 
ATOM   2364 C  CA  . ILE A 1 297 ? 0.812   -7.330  21.037  1.00 18.94  ? 297 ILE A CA  1 
ATOM   2365 C  C   . ILE A 1 297 ? 1.466   -8.709  21.202  1.00 19.39  ? 297 ILE A C   1 
ATOM   2366 O  O   . ILE A 1 297 ? 2.397   -9.033  20.460  1.00 19.40  ? 297 ILE A O   1 
ATOM   2367 C  CB  . ILE A 1 297 ? 1.488   -6.301  21.967  1.00 19.49  ? 297 ILE A CB  1 
ATOM   2368 C  CG1 . ILE A 1 297 ? 1.031   -4.867  21.678  1.00 19.31  ? 297 ILE A CG1 1 
ATOM   2369 C  CG2 . ILE A 1 297 ? 2.994   -6.428  21.885  1.00 20.57  ? 297 ILE A CG2 1 
ATOM   2370 C  CD1 . ILE A 1 297 ? 1.124   -4.474  20.248  1.00 20.18  ? 297 ILE A CD1 1 
ATOM   2371 N  N   . LEU A 1 298 ? 1.047   -9.485  22.213  1.00 20.56  ? 298 LEU A N   1 
ATOM   2372 C  CA  . LEU A 1 298 ? 1.680   -10.764 22.514  1.00 21.27  ? 298 LEU A CA  1 
ATOM   2373 C  C   . LEU A 1 298 ? 1.006   -11.894 21.726  1.00 21.44  ? 298 LEU A C   1 
ATOM   2374 O  O   . LEU A 1 298 ? 0.292   -12.731 22.280  1.00 21.28  ? 298 LEU A O   1 
ATOM   2375 C  CB  . LEU A 1 298 ? 1.601   -11.012 24.023  1.00 21.26  ? 298 LEU A CB  1 
ATOM   2376 C  CG  . LEU A 1 298 ? 2.298   -9.976  24.896  1.00 20.46  ? 298 LEU A CG  1 
ATOM   2377 C  CD1 . LEU A 1 298 ? 2.375   -10.473 26.319  1.00 22.64  ? 298 LEU A CD1 1 
ATOM   2378 C  CD2 . LEU A 1 298 ? 3.683   -9.664  24.364  1.00 21.37  ? 298 LEU A CD2 1 
ATOM   2379 N  N   . VAL A 1 299 ? 1.254   -11.913 20.419  1.00 21.87  ? 299 VAL A N   1 
ATOM   2380 C  CA  . VAL A 1 299 ? 0.510   -12.772 19.499  1.00 24.71  ? 299 VAL A CA  1 
ATOM   2381 C  C   . VAL A 1 299 ? 1.153   -14.159 19.359  1.00 27.96  ? 299 VAL A C   1 
ATOM   2382 O  O   . VAL A 1 299 ? 0.613   -15.011 18.658  1.00 31.68  ? 299 VAL A O   1 
ATOM   2383 C  CB  . VAL A 1 299 ? 0.397   -12.108 18.118  1.00 23.68  ? 299 VAL A CB  1 
ATOM   2384 C  CG1 . VAL A 1 299 ? -0.317  -10.772 18.208  1.00 25.24  ? 299 VAL A CG1 1 
ATOM   2385 C  CG2 . VAL A 1 299 ? 1.747   -11.966 17.449  1.00 23.81  ? 299 VAL A CG2 1 
ATOM   2386 N  N   . ASP A 1 300 ? 2.317   -14.377 19.982  1.00 25.81  ? 300 ASP A N   1 
ATOM   2387 C  CA  . ASP A 1 300 ? 3.013   -15.655 19.917  1.00 25.83  ? 300 ASP A CA  1 
ATOM   2388 C  C   . ASP A 1 300 ? 2.952   -16.343 21.261  1.00 24.58  ? 300 ASP A C   1 
ATOM   2389 O  O   . ASP A 1 300 ? 2.719   -15.677 22.254  1.00 24.32  ? 300 ASP A O   1 
ATOM   2390 C  CB  . ASP A 1 300 ? 4.471   -15.456 19.524  1.00 29.29  ? 300 ASP A CB  1 
ATOM   2391 C  CG  . ASP A 1 300 ? 4.581   -14.974 18.100  1.00 36.11  ? 300 ASP A CG  1 
ATOM   2392 O  OD1 . ASP A 1 300 ? 3.916   -15.606 17.223  1.00 36.54  ? 300 ASP A OD1 1 
ATOM   2393 O  OD2 . ASP A 1 300 ? 5.304   -13.955 17.881  1.00 39.57  ? 300 ASP A OD2 1 
ATOM   2394 N  N   . PRO A 1 301 ? 3.159   -17.686 21.329  1.00 29.08  ? 301 PRO A N   1 
ATOM   2395 C  CA  . PRO A 1 301 ? 3.006   -18.447 22.569  1.00 25.97  ? 301 PRO A CA  1 
ATOM   2396 C  C   . PRO A 1 301 ? 3.918   -17.988 23.699  1.00 24.63  ? 301 PRO A C   1 
ATOM   2397 O  O   . PRO A 1 301 ? 3.517   -18.041 24.859  1.00 23.14  ? 301 PRO A O   1 
ATOM   2398 C  CB  . PRO A 1 301 ? 3.385   -19.887 22.175  1.00 29.43  ? 301 PRO A CB  1 
ATOM   2399 C  CG  . PRO A 1 301 ? 3.114   -19.921 20.705  1.00 32.72  ? 301 PRO A CG  1 
ATOM   2400 C  CD  . PRO A 1 301 ? 3.538   -18.556 20.206  1.00 30.07  ? 301 PRO A CD  1 
ATOM   2401 N  N   . VAL A 1 302 ? 5.150   -17.588 23.346  1.00 26.29  ? 302 VAL A N   1 
ATOM   2402 C  CA  . VAL A 1 302 ? 6.060   -16.933 24.277  1.00 29.78  ? 302 VAL A CA  1 
ATOM   2403 C  C   . VAL A 1 302 ? 6.395   -15.536 23.766  1.00 23.94  ? 302 VAL A C   1 
ATOM   2404 O  O   . VAL A 1 302 ? 6.561   -15.334 22.576  1.00 24.89  ? 302 VAL A O   1 
ATOM   2405 C  CB  . VAL A 1 302 ? 7.349   -17.747 24.508  1.00 34.00  ? 302 VAL A CB  1 
ATOM   2406 C  CG1 . VAL A 1 302 ? 7.038   -19.073 25.197  1.00 39.68  ? 302 VAL A CG1 1 
ATOM   2407 C  CG2 . VAL A 1 302 ? 8.142   -17.942 23.220  1.00 34.12  ? 302 VAL A CG2 1 
ATOM   2408 N  N   . PRO A 1 303 ? 6.484   -14.506 24.621  1.00 22.50  ? 303 PRO A N   1 
ATOM   2409 C  CA  . PRO A 1 303 ? 6.774   -13.170 24.131  1.00 21.45  ? 303 PRO A CA  1 
ATOM   2410 C  C   . PRO A 1 303 ? 8.239   -13.032 23.744  1.00 20.29  ? 303 PRO A C   1 
ATOM   2411 O  O   . PRO A 1 303 ? 9.114   -13.567 24.423  1.00 21.14  ? 303 PRO A O   1 
ATOM   2412 C  CB  . PRO A 1 303 ? 6.429   -12.268 25.326  1.00 22.63  ? 303 PRO A CB  1 
ATOM   2413 C  CG  . PRO A 1 303 ? 5.618   -13.136 26.235  1.00 23.50  ? 303 PRO A CG  1 
ATOM   2414 C  CD  . PRO A 1 303 ? 6.209   -14.518 26.060  1.00 23.72  ? 303 PRO A CD  1 
ATOM   2415 N  N   . SER A 1 304 ? 8.489   -12.210 22.720  1.00 18.20  ? 304 SER A N   1 
ATOM   2416 C  CA  . SER A 1 304 ? 9.836   -11.864 22.321  1.00 17.67  ? 304 SER A CA  1 
ATOM   2417 C  C   . SER A 1 304 ? 10.245  -10.549 22.979  1.00 17.56  ? 304 SER A C   1 
ATOM   2418 O  O   . SER A 1 304 ? 9.407   -9.787  23.449  1.00 15.47  ? 304 SER A O   1 
ATOM   2419 C  CB  . SER A 1 304 ? 9.878   -11.710 20.844  1.00 19.98  ? 304 SER A CB  1 
ATOM   2420 O  OG  . SER A 1 304 ? 9.164   -10.538 20.486  1.00 19.71  ? 304 SER A OG  1 
ATOM   2421 N  N   . TYR A 1 305 ? 11.546  -10.289 22.991  1.00 18.80  ? 305 TYR A N   1 
ATOM   2422 C  CA  . TYR A 1 305 ? 12.049  -9.049  23.543  1.00 20.06  ? 305 TYR A CA  1 
ATOM   2423 C  C   . TYR A 1 305 ? 11.403  -7.844  22.855  1.00 20.24  ? 305 TYR A C   1 
ATOM   2424 O  O   . TYR A 1 305 ? 10.990  -6.894  23.522  1.00 17.60  ? 305 TYR A O   1 
ATOM   2425 C  CB  . TYR A 1 305 ? 13.562  -9.043  23.427  1.00 21.11  ? 305 TYR A CB  1 
ATOM   2426 C  CG  . TYR A 1 305 ? 14.185  -7.694  23.721  1.00 24.50  ? 305 TYR A CG  1 
ATOM   2427 C  CD1 . TYR A 1 305 ? 14.538  -7.313  25.015  1.00 26.44  ? 305 TYR A CD1 1 
ATOM   2428 C  CD2 . TYR A 1 305 ? 14.404  -6.798  22.686  1.00 25.62  ? 305 TYR A CD2 1 
ATOM   2429 C  CE1 . TYR A 1 305 ? 15.102  -6.069  25.265  1.00 27.15  ? 305 TYR A CE1 1 
ATOM   2430 C  CE2 . TYR A 1 305 ? 14.971  -5.560  22.924  1.00 27.84  ? 305 TYR A CE2 1 
ATOM   2431 C  CZ  . TYR A 1 305 ? 15.319  -5.191  24.211  1.00 29.61  ? 305 TYR A CZ  1 
ATOM   2432 O  OH  . TYR A 1 305 ? 15.904  -3.953  24.384  1.00 31.90  ? 305 TYR A OH  1 
ATOM   2433 N  N   . LYS A 1 306 ? 11.298  -7.909  21.529  1.00 20.32  ? 306 LYS A N   1 
ATOM   2434 C  CA  . LYS A 1 306 ? 10.720  -6.832  20.746  1.00 23.48  ? 306 LYS A CA  1 
ATOM   2435 C  C   . LYS A 1 306 ? 9.252   -6.582  21.111  1.00 21.10  ? 306 LYS A C   1 
ATOM   2436 O  O   . LYS A 1 306 ? 8.842   -5.424  21.165  1.00 20.34  ? 306 LYS A O   1 
ATOM   2437 C  CB  . LYS A 1 306 ? 10.890  -7.127  19.255  1.00 27.01  ? 306 LYS A CB  1 
ATOM   2438 C  CG  . LYS A 1 306 ? 10.306  -6.064  18.328  1.00 35.55  ? 306 LYS A CG  1 
ATOM   2439 C  CD  . LYS A 1 306 ? 10.980  -4.677  18.433  1.00 39.33  ? 306 LYS A CD  1 
ATOM   2440 C  CE  . LYS A 1 306 ? 10.006  -3.510  18.420  1.00 37.11  ? 306 LYS A CE  1 
ATOM   2441 N  NZ  . LYS A 1 306 ? 9.426   -3.252  19.761  1.00 32.62  ? 306 LYS A NZ  1 
ATOM   2442 N  N   . GLN A 1 307 ? 8.476   -7.631  21.413  1.00 17.57  ? 307 GLN A N   1 
ATOM   2443 C  CA  . GLN A 1 307 ? 7.059   -7.469  21.750  1.00 17.36  ? 307 GLN A CA  1 
ATOM   2444 C  C   . GLN A 1 307 ? 6.910   -6.821  23.130  1.00 17.13  ? 307 GLN A C   1 
ATOM   2445 O  O   . GLN A 1 307 ? 6.008   -6.032  23.374  1.00 19.50  ? 307 GLN A O   1 
ATOM   2446 C  CB  . GLN A 1 307 ? 6.342   -8.822  21.725  1.00 19.69  ? 307 GLN A CB  1 
ATOM   2447 C  CG  . GLN A 1 307 ? 6.123   -9.356  20.319  1.00 20.61  ? 307 GLN A CG  1 
ATOM   2448 C  CD  . GLN A 1 307 ? 5.818   -10.834 20.247  1.00 22.45  ? 307 GLN A CD  1 
ATOM   2449 O  OE1 . GLN A 1 307 ? 5.939   -11.589 21.212  1.00 23.07  ? 307 GLN A OE1 1 
ATOM   2450 N  NE2 . GLN A 1 307 ? 5.401   -11.260 19.073  1.00 22.66  ? 307 GLN A NE2 1 
ATOM   2451 N  N   . VAL A 1 308 ? 7.821   -7.133  24.046  1.00 17.63  ? 308 VAL A N   1 
ATOM   2452 C  CA  . VAL A 1 308 ? 7.750   -6.589  25.387  1.00 18.15  ? 308 VAL A CA  1 
ATOM   2453 C  C   . VAL A 1 308 ? 7.971   -5.080  25.299  1.00 18.76  ? 308 VAL A C   1 
ATOM   2454 O  O   . VAL A 1 308 ? 7.272   -4.341  25.973  1.00 18.68  ? 308 VAL A O   1 
ATOM   2455 C  CB  . VAL A 1 308 ? 8.732   -7.312  26.338  1.00 19.00  ? 308 VAL A CB  1 
ATOM   2456 C  CG1 . VAL A 1 308 ? 8.927   -6.543  27.635  1.00 21.35  ? 308 VAL A CG1 1 
ATOM   2457 C  CG2 . VAL A 1 308 ? 8.239   -8.722  26.607  1.00 19.92  ? 308 VAL A CG2 1 
ATOM   2458 N  N   . LYS A 1 309 ? 8.874   -4.638  24.423  1.00 19.00  ? 309 LYS A N   1 
ATOM   2459 C  CA  . LYS A 1 309 ? 9.119   -3.217  24.193  1.00 21.70  ? 309 LYS A CA  1 
ATOM   2460 C  C   . LYS A 1 309 ? 7.916   -2.514  23.556  1.00 21.32  ? 309 LYS A C   1 
ATOM   2461 O  O   . LYS A 1 309 ? 7.818   -1.289  23.596  1.00 21.35  ? 309 LYS A O   1 
ATOM   2462 C  CB  . LYS A 1 309 ? 10.333  -3.016  23.283  1.00 24.75  ? 309 LYS A CB  1 
ATOM   2463 C  CG  . LYS A 1 309 ? 11.672  -3.433  23.886  1.00 29.01  ? 309 LYS A CG  1 
ATOM   2464 C  CD  . LYS A 1 309 ? 11.784  -3.030  25.324  1.00 31.05  ? 309 LYS A CD  1 
ATOM   2465 C  CE  . LYS A 1 309 ? 13.193  -3.060  25.866  1.00 38.46  ? 309 LYS A CE  1 
ATOM   2466 N  NZ  . LYS A 1 309 ? 13.202  -2.963  27.354  1.00 40.73  ? 309 LYS A NZ  1 
ATOM   2467 N  N   . GLN A 1 310 ? 6.980   -3.275  22.999  1.00 20.93  ? 310 GLN A N   1 
ATOM   2468 C  CA  . GLN A 1 310 ? 5.798   -2.702  22.378  1.00 20.80  ? 310 GLN A CA  1 
ATOM   2469 C  C   . GLN A 1 310 ? 4.664   -2.521  23.370  1.00 18.25  ? 310 GLN A C   1 
ATOM   2470 O  O   . GLN A 1 310 ? 3.666   -1.906  23.003  1.00 18.17  ? 310 GLN A O   1 
ATOM   2471 C  CB  . GLN A 1 310 ? 5.245   -3.603  21.279  1.00 23.00  ? 310 GLN A CB  1 
ATOM   2472 C  CG  . GLN A 1 310 ? 6.185   -3.797  20.119  1.00 26.05  ? 310 GLN A CG  1 
ATOM   2473 C  CD  . GLN A 1 310 ? 5.486   -4.425  18.943  1.00 31.18  ? 310 GLN A CD  1 
ATOM   2474 O  OE1 . GLN A 1 310 ? 4.850   -5.472  19.047  1.00 27.91  ? 310 GLN A OE1 1 
ATOM   2475 N  NE2 . GLN A 1 310 ? 5.636   -3.792  17.790  1.00 40.76  ? 310 GLN A NE2 1 
ATOM   2476 N  N   . LEU A 1 311 ? 4.809   -3.024  24.605  1.00 14.72  ? 311 LEU A N   1 
ATOM   2477 C  CA  . LEU A 1 311 ? 3.719   -2.933  25.565  1.00 16.92  ? 311 LEU A CA  1 
ATOM   2478 C  C   . LEU A 1 311 ? 3.743   -1.576  26.258  1.00 16.11  ? 311 LEU A C   1 
ATOM   2479 O  O   . LEU A 1 311 ? 4.063   -1.463  27.435  1.00 16.26  ? 311 LEU A O   1 
ATOM   2480 C  CB  . LEU A 1 311 ? 3.819   -4.066  26.586  1.00 14.86  ? 311 LEU A CB  1 
ATOM   2481 C  CG  . LEU A 1 311 ? 3.631   -5.475  26.037  1.00 15.11  ? 311 LEU A CG  1 
ATOM   2482 C  CD1 . LEU A 1 311 ? 4.002   -6.488  27.101  1.00 15.62  ? 311 LEU A CD1 1 
ATOM   2483 C  CD2 . LEU A 1 311 ? 2.214   -5.687  25.548  1.00 15.00  ? 311 LEU A CD2 1 
ATOM   2484 N  N   . LYS A 1 312 ? 3.344   -0.547  25.524  1.00 18.50  ? 312 LYS A N   1 
ATOM   2485 C  CA  . LYS A 1 312 ? 3.521   0.823   25.985  1.00 17.62  ? 312 LYS A CA  1 
ATOM   2486 C  C   . LYS A 1 312 ? 2.589   1.095   27.152  1.00 15.91  ? 312 LYS A C   1 
ATOM   2487 O  O   . LYS A 1 312 ? 3.006   1.674   28.142  1.00 14.22  ? 312 LYS A O   1 
ATOM   2488 C  CB  . LYS A 1 312 ? 3.279   1.776   24.820  1.00 21.22  ? 312 LYS A CB  1 
ATOM   2489 C  CG  . LYS A 1 312 ? 3.440   3.245   25.162  1.00 23.59  ? 312 LYS A CG  1 
ATOM   2490 C  CD  . LYS A 1 312 ? 3.027   4.120   23.992  1.00 29.47  ? 312 LYS A CD  1 
ATOM   2491 C  CE  . LYS A 1 312 ? 3.477   5.554   24.172  1.00 31.47  ? 312 LYS A CE  1 
ATOM   2492 N  NZ  . LYS A 1 312 ? 2.856   6.131   25.386  1.00 34.54  ? 312 LYS A NZ  1 
ATOM   2493 N  N   . TYR A 1 313 ? 1.313   0.692   27.016  1.00 16.07  ? 313 TYR A N   1 
ATOM   2494 C  CA  . TYR A 1 313 ? 0.329   0.955   28.049  1.00 14.67  ? 313 TYR A CA  1 
ATOM   2495 C  C   . TYR A 1 313 ? 0.653   0.180   29.325  1.00 13.95  ? 313 TYR A C   1 
ATOM   2496 O  O   . TYR A 1 313 ? 0.506   0.688   30.421  1.00 13.03  ? 313 TYR A O   1 
ATOM   2497 C  CB  . TYR A 1 313 ? -1.075  0.604   27.547  1.00 14.49  ? 313 TYR A CB  1 
ATOM   2498 C  CG  . TYR A 1 313 ? -2.131  1.185   28.461  1.00 15.05  ? 313 TYR A CG  1 
ATOM   2499 C  CD1 . TYR A 1 313 ? -2.610  2.479   28.290  1.00 15.93  ? 313 TYR A CD1 1 
ATOM   2500 C  CD2 . TYR A 1 313 ? -2.613  0.438   29.521  1.00 15.06  ? 313 TYR A CD2 1 
ATOM   2501 C  CE1 . TYR A 1 313 ? -3.549  3.009   29.153  1.00 16.91  ? 313 TYR A CE1 1 
ATOM   2502 C  CE2 . TYR A 1 313 ? -3.541  0.955   30.393  1.00 16.64  ? 313 TYR A CE2 1 
ATOM   2503 C  CZ  . TYR A 1 313 ? -4.023  2.237   30.202  1.00 15.82  ? 313 TYR A CZ  1 
ATOM   2504 O  OH  . TYR A 1 313 ? -4.938  2.711   31.077  1.00 15.18  ? 313 TYR A OH  1 
ATOM   2505 N  N   . VAL A 1 314 ? 1.144   -1.050  29.200  1.00 14.13  ? 314 VAL A N   1 
ATOM   2506 C  CA  . VAL A 1 314 ? 1.584   -1.800  30.363  1.00 14.31  ? 314 VAL A CA  1 
ATOM   2507 C  C   . VAL A 1 314 ? 2.700   -1.034  31.071  1.00 13.45  ? 314 VAL A C   1 
ATOM   2508 O  O   . VAL A 1 314 ? 2.694   -0.983  32.281  1.00 14.02  ? 314 VAL A O   1 
ATOM   2509 C  CB  . VAL A 1 314 ? 2.027   -3.228  29.994  1.00 14.26  ? 314 VAL A CB  1 
ATOM   2510 C  CG1 . VAL A 1 314 ? 2.682   -3.913  31.185  1.00 15.26  ? 314 VAL A CG1 1 
ATOM   2511 C  CG2 . VAL A 1 314 ? 0.865   -4.047  29.435  1.00 14.86  ? 314 VAL A CG2 1 
ATOM   2512 N  N   . GLY A 1 315 ? 3.615   -0.447  30.307  1.00 14.75  ? 315 GLY A N   1 
ATOM   2513 C  CA  . GLY A 1 315 ? 4.676   0.404   30.832  1.00 15.91  ? 315 GLY A CA  1 
ATOM   2514 C  C   . GLY A 1 315 ? 4.128   1.603   31.610  1.00 15.13  ? 315 GLY A C   1 
ATOM   2515 O  O   . GLY A 1 315 ? 4.655   1.959   32.676  1.00 14.59  ? 315 GLY A O   1 
ATOM   2516 N  N   . MET A 1 316 ? 3.007   2.143   31.111  1.00 15.90  ? 316 MET A N   1 
ATOM   2517 C  CA  . MET A 1 316 ? 2.353   3.275   31.753  1.00 15.59  ? 316 MET A CA  1 
ATOM   2518 C  C   . MET A 1 316 ? 1.740   2.830   33.073  1.00 15.01  ? 316 MET A C   1 
ATOM   2519 O  O   . MET A 1 316 ? 1.850   3.533   34.074  1.00 16.27  ? 316 MET A O   1 
ATOM   2520 C  CB  . MET A 1 316 ? 1.312   3.880   30.816  1.00 15.90  ? 316 MET A CB  1 
ATOM   2521 C  CG  . MET A 1 316 ? 1.998   4.616   29.679  1.00 18.96  ? 316 MET A CG  1 
ATOM   2522 S  SD  . MET A 1 316 ? 0.959   4.917   28.242  1.00 23.77  ? 316 MET A SD  1 
ATOM   2523 C  CE  . MET A 1 316 ? -0.391  5.859   28.941  1.00 22.73  ? 316 MET A CE  1 
ATOM   2524 N  N   . VAL A 1 317 ? 1.155   1.629   33.100  1.00 13.27  ? 317 VAL A N   1 
ATOM   2525 C  CA  . VAL A 1 317 ? 0.587   1.102   34.325  1.00 13.31  ? 317 VAL A CA  1 
ATOM   2526 C  C   . VAL A 1 317 ? 1.653   0.935   35.402  1.00 13.07  ? 317 VAL A C   1 
ATOM   2527 O  O   . VAL A 1 317 ? 1.398   1.224   36.559  1.00 11.05  ? 317 VAL A O   1 
ATOM   2528 C  CB  . VAL A 1 317 ? -0.163  -0.219  34.058  1.00 14.21  ? 317 VAL A CB  1 
ATOM   2529 C  CG1 . VAL A 1 317 ? -0.466  -0.994  35.316  1.00 15.26  ? 317 VAL A CG1 1 
ATOM   2530 C  CG2 . VAL A 1 317 ? -1.443  0.090   33.306  1.00 14.68  ? 317 VAL A CG2 1 
ATOM   2531 N  N   . LEU A 1 318 ? 2.821   0.421   35.011  1.00 12.63  ? 318 LEU A N   1 
ATOM   2532 C  CA  . LEU A 1 318 ? 3.893   0.241   35.970  1.00 12.99  ? 318 LEU A CA  1 
ATOM   2533 C  C   . LEU A 1 318 ? 4.373   1.599   36.503  1.00 13.35  ? 318 LEU A C   1 
ATOM   2534 O  O   . LEU A 1 318 ? 4.695   1.737   37.670  1.00 12.89  ? 318 LEU A O   1 
ATOM   2535 C  CB  . LEU A 1 318 ? 5.021   -0.511  35.255  1.00 13.48  ? 318 LEU A CB  1 
ATOM   2536 C  CG  . LEU A 1 318 ? 4.693   -1.951  34.880  1.00 14.14  ? 318 LEU A CG  1 
ATOM   2537 C  CD1 . LEU A 1 318 ? 5.821   -2.543  34.076  1.00 13.69  ? 318 LEU A CD1 1 
ATOM   2538 C  CD2 . LEU A 1 318 ? 4.371   -2.809  36.087  1.00 14.39  ? 318 LEU A CD2 1 
ATOM   2539 N  N   . ASN A 1 319 ? 4.536   2.583   35.645  1.00 14.77  ? 319 ASN A N   1 
ATOM   2540 C  CA  . ASN A 1 319 ? 5.003   3.892   36.101  1.00 14.96  ? 319 ASN A CA  1 
ATOM   2541 C  C   . ASN A 1 319 ? 3.951   4.549   36.992  1.00 14.29  ? 319 ASN A C   1 
ATOM   2542 O  O   . ASN A 1 319 ? 4.341   5.162   37.985  1.00 14.04  ? 319 ASN A O   1 
ATOM   2543 C  CB  . ASN A 1 319 ? 5.456   4.776   34.951  1.00 16.14  ? 319 ASN A CB  1 
ATOM   2544 C  CG  . ASN A 1 319 ? 6.826   4.390   34.434  1.00 19.84  ? 319 ASN A CG  1 
ATOM   2545 O  OD1 . ASN A 1 319 ? 7.740   4.086   35.196  1.00 20.52  ? 319 ASN A OD1 1 
ATOM   2546 N  ND2 . ASN A 1 319 ? 6.989   4.385   33.121  1.00 23.69  ? 319 ASN A ND2 1 
ATOM   2547 N  N   . GLU A 1 320 ? 2.645   4.331   36.738  1.00 12.38  ? 320 GLU A N   1 
ATOM   2548 C  CA  . GLU A 1 320 ? 1.635   4.924   37.597  1.00 12.79  ? 320 GLU A CA  1 
ATOM   2549 C  C   . GLU A 1 320 ? 1.594   4.216   38.948  1.00 12.95  ? 320 GLU A C   1 
ATOM   2550 O  O   . GLU A 1 320 ? 1.325   4.851   39.965  1.00 13.43  ? 320 GLU A O   1 
ATOM   2551 C  CB  . GLU A 1 320 ? 0.312   5.043   36.844  1.00 14.69  ? 320 GLU A CB  1 
ATOM   2552 C  CG  . GLU A 1 320 ? -0.840  5.700   37.595  1.00 15.15  ? 320 GLU A CG  1 
ATOM   2553 C  CD  . GLU A 1 320 ? -0.765  7.177   37.985  1.00 17.22  ? 320 GLU A CD  1 
ATOM   2554 O  OE1 . GLU A 1 320 ? -1.839  7.780   38.448  1.00 15.53  ? 320 GLU A OE1 1 
ATOM   2555 O  OE2 . GLU A 1 320 ? 0.358   7.753   37.876  1.00 21.96  ? 320 GLU A OE2 1 
ATOM   2556 N  N   . ALA A 1 321 ? 1.925   2.907   39.012  1.00 14.10  ? 321 ALA A N   1 
ATOM   2557 C  CA  . ALA A 1 321 ? 2.019   2.244   40.308  1.00 11.98  ? 321 ALA A CA  1 
ATOM   2558 C  C   . ALA A 1 321 ? 3.254   2.749   41.068  1.00 12.39  ? 321 ALA A C   1 
ATOM   2559 O  O   . ALA A 1 321 ? 3.145   2.911   42.290  1.00 12.80  ? 321 ALA A O   1 
ATOM   2560 C  CB  . ALA A 1 321 ? 2.023   0.743   40.154  1.00 12.59  ? 321 ALA A CB  1 
ATOM   2561 N  N   . LEU A 1 322 ? 4.368   3.051   40.364  1.00 12.27  ? 322 LEU A N   1 
ATOM   2562 C  CA  . LEU A 1 322 ? 5.556   3.654   40.959  1.00 13.30  ? 322 LEU A CA  1 
ATOM   2563 C  C   . LEU A 1 322 ? 5.291   5.099   41.377  1.00 16.11  ? 322 LEU A C   1 
ATOM   2564 O  O   . LEU A 1 322 ? 5.985   5.612   42.267  1.00 15.39  ? 322 LEU A O   1 
ATOM   2565 C  CB  . LEU A 1 322 ? 6.754   3.606   40.004  1.00 13.94  ? 322 LEU A CB  1 
ATOM   2566 C  CG  . LEU A 1 322 ? 7.372   2.222   39.797  1.00 13.23  ? 322 LEU A CG  1 
ATOM   2567 C  CD1 . LEU A 1 322 ? 8.375   2.224   38.702  1.00 13.18  ? 322 LEU A CD1 1 
ATOM   2568 C  CD2 . LEU A 1 322 ? 8.033   1.683   41.056  1.00 13.68  ? 322 LEU A CD2 1 
ATOM   2569 N  N   . ARG A 1 323 ? 4.311   5.769   40.769  1.00 14.27  ? 323 ARG A N   1 
ATOM   2570 C  CA  . ARG A 1 323 ? 4.045   7.138   41.227  1.00 15.08  ? 323 ARG A CA  1 
ATOM   2571 C  C   . ARG A 1 323 ? 3.418   7.090   42.627  1.00 14.13  ? 323 ARG A C   1 
ATOM   2572 O  O   . ARG A 1 323 ? 3.910   7.672   43.588  1.00 12.64  ? 323 ARG A O   1 
ATOM   2573 C  CB  . ARG A 1 323 ? 3.190   7.943   40.247  1.00 14.70  ? 323 ARG A CB  1 
ATOM   2574 C  CG  . ARG A 1 323 ? 3.041   9.423   40.636  1.00 15.04  ? 323 ARG A CG  1 
ATOM   2575 C  CD  . ARG A 1 323 ? 2.084   10.200  39.749  1.00 14.73  ? 323 ARG A CD  1 
ATOM   2576 N  NE  . ARG A 1 323 ? 0.706   9.677   39.799  1.00 15.08  ? 323 ARG A NE  1 
ATOM   2577 C  CZ  . ARG A 1 323 ? -0.141  9.855   40.795  1.00 14.71  ? 323 ARG A CZ  1 
ATOM   2578 N  NH1 . ARG A 1 323 ? 0.093   10.759  41.720  1.00 18.88  ? 323 ARG A NH1 1 
ATOM   2579 N  NH2 . ARG A 1 323 ? -1.315  9.254   40.784  1.00 16.24  ? 323 ARG A NH2 1 
ATOM   2580 N  N   . LEU A 1 324 ? 2.346   6.307   42.782  1.00 13.83  ? 324 LEU A N   1 
ATOM   2581 C  CA  . LEU A 1 324 ? 1.629   6.211   44.038  1.00 13.50  ? 324 LEU A CA  1 
ATOM   2582 C  C   . LEU A 1 324 ? 2.427   5.512   45.148  1.00 14.62  ? 324 LEU A C   1 
ATOM   2583 O  O   . LEU A 1 324 ? 2.439   5.992   46.305  1.00 13.54  ? 324 LEU A O   1 
ATOM   2584 C  CB  . LEU A 1 324 ? 0.307   5.533   43.710  1.00 15.40  ? 324 LEU A CB  1 
ATOM   2585 C  CG  . LEU A 1 324 ? -0.675  6.455   42.998  1.00 17.53  ? 324 LEU A CG  1 
ATOM   2586 C  CD1 . LEU A 1 324 ? -1.929  5.713   42.554  1.00 17.25  ? 324 LEU A CD1 1 
ATOM   2587 C  CD2 . LEU A 1 324 ? -1.042  7.607   43.922  1.00 18.26  ? 324 LEU A CD2 1 
ATOM   2588 N  N   . TRP A 1 325 ? 3.104   4.391   44.804  1.00 12.81  ? 325 TRP A N   1 
ATOM   2589 C  CA  . TRP A 1 325 ? 3.765   3.554   45.790  1.00 13.30  ? 325 TRP A CA  1 
ATOM   2590 C  C   . TRP A 1 325 ? 5.144   3.112   45.315  1.00 12.41  ? 325 TRP A C   1 
ATOM   2591 O  O   . TRP A 1 325 ? 5.409   1.905   45.130  1.00 13.31  ? 325 TRP A O   1 
ATOM   2592 C  CB  . TRP A 1 325 ? 2.843   2.376   46.145  1.00 13.70  ? 325 TRP A CB  1 
ATOM   2593 C  CG  . TRP A 1 325 ? 1.635   2.856   46.903  1.00 14.52  ? 325 TRP A CG  1 
ATOM   2594 C  CD1 . TRP A 1 325 ? 0.321   2.781   46.546  1.00 15.74  ? 325 TRP A CD1 1 
ATOM   2595 C  CD2 . TRP A 1 325 ? 1.671   3.528   48.175  1.00 15.95  ? 325 TRP A CD2 1 
ATOM   2596 N  NE1 . TRP A 1 325 ? -0.465  3.360   47.519  1.00 17.02  ? 325 TRP A NE1 1 
ATOM   2597 C  CE2 . TRP A 1 325 ? 0.342   3.823   48.525  1.00 17.05  ? 325 TRP A CE2 1 
ATOM   2598 C  CE3 . TRP A 1 325 ? 2.713   3.906   49.029  1.00 16.78  ? 325 TRP A CE3 1 
ATOM   2599 C  CZ2 . TRP A 1 325 ? 0.029   4.445   49.724  1.00 19.65  ? 325 TRP A CZ2 1 
ATOM   2600 C  CZ3 . TRP A 1 325 ? 2.399   4.538   50.206  1.00 18.02  ? 325 TRP A CZ3 1 
ATOM   2601 C  CH2 . TRP A 1 325 ? 1.075   4.771   50.556  1.00 18.14  ? 325 TRP A CH2 1 
ATOM   2602 N  N   . PRO A 1 326 ? 6.093   4.056   45.196  1.00 11.91  ? 326 PRO A N   1 
ATOM   2603 C  CA  . PRO A 1 326 ? 7.472   3.722   44.830  1.00 13.59  ? 326 PRO A CA  1 
ATOM   2604 C  C   . PRO A 1 326 ? 8.031   2.758   45.873  1.00 14.34  ? 326 PRO A C   1 
ATOM   2605 O  O   . PRO A 1 326 ? 7.977   3.060   47.076  1.00 14.69  ? 326 PRO A O   1 
ATOM   2606 C  CB  . PRO A 1 326 ? 8.216   5.071   44.829  1.00 13.32  ? 326 PRO A CB  1 
ATOM   2607 C  CG  . PRO A 1 326 ? 7.336   6.017   45.639  1.00 13.54  ? 326 PRO A CG  1 
ATOM   2608 C  CD  . PRO A 1 326 ? 5.919   5.485   45.527  1.00 12.58  ? 326 PRO A CD  1 
ATOM   2609 N  N   . THR A 1 327 ? 8.515   1.588   45.426  1.00 14.05  ? 327 THR A N   1 
ATOM   2610 C  CA  . THR A 1 327 ? 8.687   0.468   46.340  1.00 14.83  ? 327 THR A CA  1 
ATOM   2611 C  C   . THR A 1 327 ? 9.958   0.617   47.158  1.00 14.66  ? 327 THR A C   1 
ATOM   2612 O  O   . THR A 1 327 ? 10.000  0.078   48.260  1.00 14.60  ? 327 THR A O   1 
ATOM   2613 C  CB  . THR A 1 327 ? 8.541   -0.875  45.613  1.00 14.12  ? 327 THR A CB  1 
ATOM   2614 O  OG1 . THR A 1 327 ? 9.422   -0.841  44.481  1.00 14.42  ? 327 THR A OG1 1 
ATOM   2615 C  CG2 . THR A 1 327 ? 7.081   -1.075  45.229  1.00 12.83  ? 327 THR A CG2 1 
ATOM   2616 N  N   . GLY A 1 328 ? 10.906  1.437   46.670  1.00 16.67  ? 328 GLY A N   1 
ATOM   2617 C  CA  . GLY A 1 328 ? 12.022  1.928   47.477  1.00 17.94  ? 328 GLY A CA  1 
ATOM   2618 C  C   . GLY A 1 328 ? 11.769  3.391   47.857  1.00 17.47  ? 328 GLY A C   1 
ATOM   2619 O  O   . GLY A 1 328 ? 12.156  4.285   47.116  1.00 20.19  ? 328 GLY A O   1 
ATOM   2620 N  N   . PRO A 1 329 ? 11.002  3.669   48.928  1.00 17.38  ? 329 PRO A N   1 
ATOM   2621 C  CA  . PRO A 1 329 ? 10.276  4.941   49.049  1.00 17.15  ? 329 PRO A CA  1 
ATOM   2622 C  C   . PRO A 1 329 ? 11.086  6.160   49.508  1.00 16.99  ? 329 PRO A C   1 
ATOM   2623 O  O   . PRO A 1 329 ? 10.557  7.263   49.550  1.00 15.02  ? 329 PRO A O   1 
ATOM   2624 C  CB  . PRO A 1 329 ? 9.233   4.615   50.128  1.00 17.39  ? 329 PRO A CB  1 
ATOM   2625 C  CG  . PRO A 1 329 ? 9.963   3.646   51.037  1.00 17.18  ? 329 PRO A CG  1 
ATOM   2626 C  CD  . PRO A 1 329 ? 10.714  2.758   50.059  1.00 18.40  ? 329 PRO A CD  1 
ATOM   2627 N  N   . ALA A 1 330 ? 12.367  5.964   49.853  1.00 15.76  ? 330 ALA A N   1 
ATOM   2628 C  CA  . ALA A 1 330 ? 13.146  7.096   50.332  1.00 17.69  ? 330 ALA A CA  1 
ATOM   2629 C  C   . ALA A 1 330 ? 14.590  6.966   49.879  1.00 17.29  ? 330 ALA A C   1 
ATOM   2630 O  O   . ALA A 1 330 ? 15.094  5.863   49.713  1.00 21.14  ? 330 ALA A O   1 
ATOM   2631 C  CB  . ALA A 1 330 ? 13.053  7.199   51.837  1.00 16.89  ? 330 ALA A CB  1 
ATOM   2632 N  N   . PHE A 1 331 ? 15.242  8.115   49.663  1.00 17.71  ? 331 PHE A N   1 
ATOM   2633 C  CA  . PHE A 1 331 ? 16.683  8.134   49.514  1.00 17.98  ? 331 PHE A CA  1 
ATOM   2634 C  C   . PHE A 1 331 ? 17.236  9.357   50.224  1.00 17.81  ? 331 PHE A C   1 
ATOM   2635 O  O   . PHE A 1 331 ? 16.519  10.344  50.412  1.00 18.12  ? 331 PHE A O   1 
ATOM   2636 C  CB  . PHE A 1 331 ? 17.078  7.992   48.041  1.00 19.89  ? 331 PHE A CB  1 
ATOM   2637 C  CG  . PHE A 1 331 ? 16.735  9.118   47.108  1.00 20.09  ? 331 PHE A CG  1 
ATOM   2638 C  CD1 . PHE A 1 331 ? 15.589  9.055   46.342  1.00 24.02  ? 331 PHE A CD1 1 
ATOM   2639 C  CD2 . PHE A 1 331 ? 17.622  10.163  46.879  1.00 23.21  ? 331 PHE A CD2 1 
ATOM   2640 C  CE1 . PHE A 1 331 ? 15.297  10.044  45.414  1.00 23.33  ? 331 PHE A CE1 1 
ATOM   2641 C  CE2 . PHE A 1 331 ? 17.318  11.165  45.970  1.00 23.61  ? 331 PHE A CE2 1 
ATOM   2642 C  CZ  . PHE A 1 331 ? 16.162  11.098  45.223  1.00 25.10  ? 331 PHE A CZ  1 
ATOM   2643 N  N   . SER A 1 332 ? 18.510  9.245   50.613  1.00 16.95  ? 332 SER A N   1 
ATOM   2644 C  CA  . SER A 1 332 ? 19.134  10.206  51.512  1.00 17.33  ? 332 SER A CA  1 
ATOM   2645 C  C   . SER A 1 332 ? 20.283  10.909  50.800  1.00 15.38  ? 332 SER A C   1 
ATOM   2646 O  O   . SER A 1 332 ? 21.023  10.304  50.006  1.00 14.78  ? 332 SER A O   1 
ATOM   2647 C  CB  . SER A 1 332 ? 19.545  9.504   52.797  1.00 19.14  ? 332 SER A CB  1 
ATOM   2648 O  OG  . SER A 1 332 ? 20.091  10.372  53.768  1.00 18.24  ? 332 SER A OG  1 
ATOM   2649 N  N   . LEU A 1 333 ? 20.419  12.203  51.086  1.00 15.67  ? 333 LEU A N   1 
ATOM   2650 C  CA  . LEU A 1 333 ? 21.525  13.005  50.587  1.00 16.06  ? 333 LEU A CA  1 
ATOM   2651 C  C   . LEU A 1 333 ? 22.220  13.778  51.713  1.00 15.35  ? 333 LEU A C   1 
ATOM   2652 O  O   . LEU A 1 333 ? 21.672  13.941  52.792  1.00 15.43  ? 333 LEU A O   1 
ATOM   2653 C  CB  . LEU A 1 333 ? 20.940  13.971  49.561  1.00 17.34  ? 333 LEU A CB  1 
ATOM   2654 C  CG  . LEU A 1 333 ? 20.103  13.348  48.449  1.00 19.88  ? 333 LEU A CG  1 
ATOM   2655 C  CD1 . LEU A 1 333 ? 19.152  14.373  47.863  1.00 19.44  ? 333 LEU A CD1 1 
ATOM   2656 C  CD2 . LEU A 1 333 ? 21.001  12.770  47.369  1.00 20.40  ? 333 LEU A CD2 1 
ATOM   2657 N  N   . TYR A 1 334 ? 23.425  14.285  51.429  1.00 15.89  ? 334 TYR A N   1 
ATOM   2658 C  CA  . TYR A 1 334 ? 24.090  15.256  52.290  1.00 16.13  ? 334 TYR A CA  1 
ATOM   2659 C  C   . TYR A 1 334 ? 24.646  16.415  51.471  1.00 17.58  ? 334 TYR A C   1 
ATOM   2660 O  O   . TYR A 1 334 ? 25.008  16.275  50.302  1.00 15.32  ? 334 TYR A O   1 
ATOM   2661 C  CB  . TYR A 1 334 ? 25.266  14.716  53.093  1.00 19.46  ? 334 TYR A CB  1 
ATOM   2662 C  CG  . TYR A 1 334 ? 26.475  14.235  52.307  1.00 21.05  ? 334 TYR A CG  1 
ATOM   2663 C  CD1 . TYR A 1 334 ? 26.492  12.984  51.690  1.00 23.81  ? 334 TYR A CD1 1 
ATOM   2664 C  CD2 . TYR A 1 334 ? 27.616  15.033  52.192  1.00 23.41  ? 334 TYR A CD2 1 
ATOM   2665 C  CE1 . TYR A 1 334 ? 27.595  12.546  50.964  1.00 23.82  ? 334 TYR A CE1 1 
ATOM   2666 C  CE2 . TYR A 1 334 ? 28.732  14.602  51.496  1.00 24.80  ? 334 TYR A CE2 1 
ATOM   2667 C  CZ  . TYR A 1 334 ? 28.716  13.361  50.872  1.00 27.28  ? 334 TYR A CZ  1 
ATOM   2668 O  OH  . TYR A 1 334 ? 29.803  12.946  50.156  1.00 28.69  ? 334 TYR A OH  1 
ATOM   2669 N  N   . ALA A 1 335 ? 24.720  17.590  52.138  1.00 18.74  ? 335 ALA A N   1 
ATOM   2670 C  CA  . ALA A 1 335 ? 25.285  18.809  51.581  1.00 19.19  ? 335 ALA A CA  1 
ATOM   2671 C  C   . ALA A 1 335 ? 26.806  18.667  51.472  1.00 19.61  ? 335 ALA A C   1 
ATOM   2672 O  O   . ALA A 1 335 ? 27.480  18.358  52.441  1.00 20.73  ? 335 ALA A O   1 
ATOM   2673 C  CB  . ALA A 1 335 ? 24.915  19.971  52.461  1.00 20.47  ? 335 ALA A CB  1 
ATOM   2674 N  N   . LYS A 1 336 ? 27.341  18.872  50.270  1.00 21.57  ? 336 LYS A N   1 
ATOM   2675 C  CA  . LYS A 1 336 ? 28.773  18.768  50.037  1.00 25.45  ? 336 LYS A CA  1 
ATOM   2676 C  C   . LYS A 1 336 ? 29.471  20.002  50.596  1.00 26.32  ? 336 LYS A C   1 
ATOM   2677 O  O   . LYS A 1 336 ? 30.618  19.897  51.015  1.00 25.94  ? 336 LYS A O   1 
ATOM   2678 C  CB  . LYS A 1 336 ? 29.036  18.588  48.545  1.00 26.51  ? 336 LYS A CB  1 
ATOM   2679 C  CG  . LYS A 1 336 ? 28.694  17.197  48.008  1.00 27.71  ? 336 LYS A CG  1 
ATOM   2680 C  CD  . LYS A 1 336 ? 28.540  17.160  46.486  1.00 28.02  ? 336 LYS A CD  1 
ATOM   2681 C  CE  . LYS A 1 336 ? 29.713  17.723  45.720  1.00 30.26  ? 336 LYS A CE  1 
ATOM   2682 N  NZ  . LYS A 1 336 ? 30.930  16.929  45.997  1.00 30.53  ? 336 LYS A NZ  1 
ATOM   2683 N  N   . GLU A 1 337 ? 28.771  21.147  50.561  1.00 26.75  ? 337 GLU A N   1 
ATOM   2684 C  CA  . GLU A 1 337 ? 29.251  22.402  51.127  1.00 28.01  ? 337 GLU A CA  1 
ATOM   2685 C  C   . GLU A 1 337 ? 28.082  23.118  51.808  1.00 28.81  ? 337 GLU A C   1 
ATOM   2686 O  O   . GLU A 1 337 ? 26.923  22.736  51.638  1.00 24.16  ? 337 GLU A O   1 
ATOM   2687 C  CB  . GLU A 1 337 ? 29.864  23.314  50.052  1.00 30.89  ? 337 GLU A CB  1 
ATOM   2688 C  CG  . GLU A 1 337 ? 31.052  22.715  49.292  1.00 34.20  ? 337 GLU A CG  1 
ATOM   2689 C  CD  . GLU A 1 337 ? 32.328  22.365  50.065  1.00 39.09  ? 337 GLU A CD  1 
ATOM   2690 O  OE1 . GLU A 1 337 ? 32.467  22.747  51.242  1.00 38.32  ? 337 GLU A OE1 1 
ATOM   2691 O  OE2 . GLU A 1 337 ? 33.191  21.678  49.488  1.00 42.62  ? 337 GLU A OE2 1 
ATOM   2692 N  N   . ASP A 1 338 ? 28.394  24.155  52.599  1.00 29.43  ? 338 ASP A N   1 
ATOM   2693 C  CA  . ASP A 1 338 ? 27.376  25.079  53.075  1.00 30.12  ? 338 ASP A CA  1 
ATOM   2694 C  C   . ASP A 1 338 ? 26.580  25.576  51.873  1.00 28.69  ? 338 ASP A C   1 
ATOM   2695 O  O   . ASP A 1 338 ? 27.111  25.771  50.788  1.00 26.51  ? 338 ASP A O   1 
ATOM   2696 C  CB  . ASP A 1 338 ? 27.969  26.250  53.862  1.00 30.81  ? 338 ASP A CB  1 
ATOM   2697 C  CG  . ASP A 1 338 ? 28.800  25.869  55.083  1.00 34.56  ? 338 ASP A CG  1 
ATOM   2698 O  OD1 . ASP A 1 338 ? 28.481  24.866  55.758  1.00 34.62  ? 338 ASP A OD1 1 
ATOM   2699 O  OD2 . ASP A 1 338 ? 29.770  26.585  55.362  1.00 40.11  ? 338 ASP A OD2 1 
ATOM   2700 N  N   . THR A 1 339 ? 25.264  25.691  52.045  1.00 30.36  ? 339 THR A N   1 
ATOM   2701 C  CA  . THR A 1 339 ? 24.403  26.007  50.922  1.00 30.26  ? 339 THR A CA  1 
ATOM   2702 C  C   . THR A 1 339 ? 23.050  26.403  51.494  1.00 29.58  ? 339 THR A C   1 
ATOM   2703 O  O   . THR A 1 339 ? 22.791  26.194  52.675  1.00 32.91  ? 339 THR A O   1 
ATOM   2704 C  CB  . THR A 1 339 ? 24.360  24.837  49.920  1.00 31.13  ? 339 THR A CB  1 
ATOM   2705 O  OG1 . THR A 1 339 ? 23.916  25.316  48.648  1.00 30.99  ? 339 THR A OG1 1 
ATOM   2706 C  CG2 . THR A 1 339 ? 23.471  23.689  50.362  1.00 30.20  ? 339 THR A CG2 1 
ATOM   2707 N  N   . VAL A 1 340 ? 22.206  26.985  50.653  1.00 30.25  ? 340 VAL A N   1 
ATOM   2708 C  CA  . VAL A 1 340 ? 20.888  27.432  51.072  1.00 31.60  ? 340 VAL A CA  1 
ATOM   2709 C  C   . VAL A 1 340 ? 19.889  26.750  50.157  1.00 26.18  ? 340 VAL A C   1 
ATOM   2710 O  O   . VAL A 1 340 ? 20.029  26.822  48.944  1.00 26.65  ? 340 VAL A O   1 
ATOM   2711 C  CB  . VAL A 1 340 ? 20.747  28.971  51.046  1.00 33.71  ? 340 VAL A CB  1 
ATOM   2712 C  CG1 . VAL A 1 340 ? 21.890  29.656  51.790  1.00 32.08  ? 340 VAL A CG1 1 
ATOM   2713 C  CG2 . VAL A 1 340 ? 20.638  29.529  49.638  1.00 34.65  ? 340 VAL A CG2 1 
ATOM   2714 N  N   . LEU A 1 341 ? 18.915  26.073  50.765  1.00 27.82  ? 341 LEU A N   1 
ATOM   2715 C  CA  . LEU A 1 341 ? 17.921  25.294  50.047  1.00 27.51  ? 341 LEU A CA  1 
ATOM   2716 C  C   . LEU A 1 341 ? 16.663  26.140  49.820  1.00 28.14  ? 341 LEU A C   1 
ATOM   2717 O  O   . LEU A 1 341 ? 16.094  26.717  50.756  1.00 27.49  ? 341 LEU A O   1 
ATOM   2718 C  CB  . LEU A 1 341 ? 17.641  24.025  50.857  1.00 26.85  ? 341 LEU A CB  1 
ATOM   2719 C  CG  . LEU A 1 341 ? 16.869  22.924  50.142  1.00 27.39  ? 341 LEU A CG  1 
ATOM   2720 C  CD1 . LEU A 1 341 ? 17.719  22.237  49.096  1.00 27.87  ? 341 LEU A CD1 1 
ATOM   2721 C  CD2 . LEU A 1 341 ? 16.344  21.908  51.130  1.00 27.65  ? 341 LEU A CD2 1 
ATOM   2722 N  N   . GLY A 1 342 ? 16.311  26.275  48.533  1.00 28.67  ? 342 GLY A N   1 
ATOM   2723 C  CA  . GLY A 1 342 ? 15.069  26.898  48.104  1.00 28.37  ? 342 GLY A CA  1 
ATOM   2724 C  C   . GLY A 1 342 ? 15.036  28.395  48.394  1.00 31.94  ? 342 GLY A C   1 
ATOM   2725 O  O   . GLY A 1 342 ? 13.955  28.964  48.486  1.00 32.10  ? 342 GLY A O   1 
ATOM   2726 N  N   . GLY A 1 343 ? 16.225  28.997  48.578  1.00 33.12  ? 343 GLY A N   1 
ATOM   2727 C  CA  . GLY A 1 343 ? 16.362  30.391  48.953  1.00 33.62  ? 343 GLY A CA  1 
ATOM   2728 C  C   . GLY A 1 343 ? 16.077  30.675  50.425  1.00 31.51  ? 343 GLY A C   1 
ATOM   2729 O  O   . GLY A 1 343 ? 16.230  31.812  50.838  1.00 32.01  ? 343 GLY A O   1 
ATOM   2730 N  N   . GLU A 1 344 ? 15.666  29.679  51.218  1.00 33.47  ? 344 GLU A N   1 
ATOM   2731 C  CA  . GLU A 1 344 ? 15.073  29.957  52.521  1.00 35.34  ? 344 GLU A CA  1 
ATOM   2732 C  C   . GLU A 1 344 ? 15.682  29.134  53.649  1.00 31.69  ? 344 GLU A C   1 
ATOM   2733 O  O   . GLU A 1 344 ? 15.539  29.517  54.809  1.00 31.73  ? 344 GLU A O   1 
ATOM   2734 C  CB  . GLU A 1 344 ? 13.577  29.633  52.551  1.00 45.92  ? 344 GLU A CB  1 
ATOM   2735 C  CG  . GLU A 1 344 ? 12.796  30.122  51.341  1.00 52.47  ? 344 GLU A CG  1 
ATOM   2736 C  CD  . GLU A 1 344 ? 11.302  29.827  51.397  1.00 62.58  ? 344 GLU A CD  1 
ATOM   2737 O  OE1 . GLU A 1 344 ? 10.609  30.104  50.387  1.00 70.85  ? 344 GLU A OE1 1 
ATOM   2738 O  OE2 . GLU A 1 344 ? 10.829  29.332  52.454  1.00 59.30  ? 344 GLU A OE2 1 
ATOM   2739 N  N   . TYR A 1 345 ? 16.291  27.982  53.334  1.00 30.12  ? 345 TYR A N   1 
ATOM   2740 C  CA  . TYR A 1 345 ? 16.679  27.031  54.367  1.00 29.46  ? 345 TYR A CA  1 
ATOM   2741 C  C   . TYR A 1 345 ? 18.192  26.842  54.301  1.00 30.91  ? 345 TYR A C   1 
ATOM   2742 O  O   . TYR A 1 345 ? 18.693  26.185  53.402  1.00 30.16  ? 345 TYR A O   1 
ATOM   2743 C  CB  . TYR A 1 345 ? 15.908  25.721  54.194  1.00 28.70  ? 345 TYR A CB  1 
ATOM   2744 C  CG  . TYR A 1 345 ? 14.390  25.868  54.151  1.00 27.11  ? 345 TYR A CG  1 
ATOM   2745 C  CD1 . TYR A 1 345 ? 13.638  26.087  55.301  1.00 28.94  ? 345 TYR A CD1 1 
ATOM   2746 C  CD2 . TYR A 1 345 ? 13.709  25.786  52.953  1.00 29.87  ? 345 TYR A CD2 1 
ATOM   2747 C  CE1 . TYR A 1 345 ? 12.253  26.210  55.253  1.00 27.71  ? 345 TYR A CE1 1 
ATOM   2748 C  CE2 . TYR A 1 345 ? 12.328  25.906  52.895  1.00 31.74  ? 345 TYR A CE2 1 
ATOM   2749 C  CZ  . TYR A 1 345 ? 11.598  26.126  54.045  1.00 29.21  ? 345 TYR A CZ  1 
ATOM   2750 O  OH  . TYR A 1 345 ? 10.234  26.211  53.932  1.00 34.18  ? 345 TYR A OH  1 
ATOM   2751 N  N   . PRO A 1 346 ? 18.974  27.463  55.217  1.00 28.62  ? 346 PRO A N   1 
ATOM   2752 C  CA  . PRO A 1 346 ? 20.427  27.358  55.190  1.00 27.94  ? 346 PRO A CA  1 
ATOM   2753 C  C   . PRO A 1 346 ? 20.813  25.959  55.639  1.00 24.29  ? 346 PRO A C   1 
ATOM   2754 O  O   . PRO A 1 346 ? 20.254  25.449  56.597  1.00 25.94  ? 346 PRO A O   1 
ATOM   2755 C  CB  . PRO A 1 346 ? 20.925  28.372  56.225  1.00 29.01  ? 346 PRO A CB  1 
ATOM   2756 C  CG  . PRO A 1 346 ? 19.703  29.203  56.548  1.00 30.67  ? 346 PRO A CG  1 
ATOM   2757 C  CD  . PRO A 1 346 ? 18.509  28.299  56.328  1.00 29.38  ? 346 PRO A CD  1 
ATOM   2758 N  N   . LEU A 1 347 ? 21.804  25.387  54.967  1.00 25.45  ? 347 LEU A N   1 
ATOM   2759 C  CA  . LEU A 1 347 ? 22.353  24.094  55.337  1.00 24.14  ? 347 LEU A CA  1 
ATOM   2760 C  C   . LEU A 1 347 ? 23.861  24.230  55.523  1.00 24.81  ? 347 LEU A C   1 
ATOM   2761 O  O   . LEU A 1 347 ? 24.510  24.937  54.763  1.00 24.03  ? 347 LEU A O   1 
ATOM   2762 C  CB  . LEU A 1 347 ? 22.018  23.112  54.211  1.00 24.23  ? 347 LEU A CB  1 
ATOM   2763 C  CG  . LEU A 1 347 ? 20.522  22.921  53.950  1.00 23.02  ? 347 LEU A CG  1 
ATOM   2764 C  CD1 . LEU A 1 347 ? 20.290  21.934  52.819  1.00 24.92  ? 347 LEU A CD1 1 
ATOM   2765 C  CD2 . LEU A 1 347 ? 19.836  22.428  55.208  1.00 24.04  ? 347 LEU A CD2 1 
ATOM   2766 N  N   . GLU A 1 348 ? 24.394  23.507  56.508  1.00 27.20  ? 348 GLU A N   1 
ATOM   2767 C  CA  . GLU A 1 348 ? 25.835  23.381  56.684  1.00 30.24  ? 348 GLU A CA  1 
ATOM   2768 C  C   . GLU A 1 348 ? 26.341  22.140  55.947  1.00 28.64  ? 348 GLU A C   1 
ATOM   2769 O  O   . GLU A 1 348 ? 25.628  21.141  55.847  1.00 24.29  ? 348 GLU A O   1 
ATOM   2770 C  CB  . GLU A 1 348 ? 26.162  23.267  58.177  1.00 34.97  ? 348 GLU A CB  1 
ATOM   2771 C  CG  . GLU A 1 348 ? 25.933  24.546  58.957  1.00 40.74  ? 348 GLU A CG  1 
ATOM   2772 C  CD  . GLU A 1 348 ? 25.842  24.344  60.463  1.00 48.03  ? 348 GLU A CD  1 
ATOM   2773 O  OE1 . GLU A 1 348 ? 25.769  23.180  60.909  1.00 45.87  ? 348 GLU A OE1 1 
ATOM   2774 O  OE2 . GLU A 1 348 ? 25.838  25.359  61.193  1.00 57.14  ? 348 GLU A OE2 1 
ATOM   2775 N  N   . LYS A 1 349 ? 27.581  22.200  55.443  1.00 24.50  ? 349 LYS A N   1 
ATOM   2776 C  CA  . LYS A 1 349 ? 28.290  21.013  54.998  1.00 25.98  ? 349 LYS A CA  1 
ATOM   2777 C  C   . LYS A 1 349 ? 27.975  19.816  55.899  1.00 24.36  ? 349 LYS A C   1 
ATOM   2778 O  O   . LYS A 1 349 ? 28.105  19.896  57.115  1.00 26.37  ? 349 LYS A O   1 
ATOM   2779 C  CB  . LYS A 1 349 ? 29.789  21.315  55.008  1.00 26.28  ? 349 LYS A CB  1 
ATOM   2780 C  CG  . LYS A 1 349 ? 30.696  20.144  54.671  1.00 30.80  ? 349 LYS A CG  1 
ATOM   2781 C  CD  . LYS A 1 349 ? 32.136  20.542  54.391  1.00 32.01  ? 349 LYS A CD  1 
ATOM   2782 C  CE  . LYS A 1 349 ? 33.001  19.324  54.159  1.00 35.10  ? 349 LYS A CE  1 
ATOM   2783 N  NZ  . LYS A 1 349 ? 34.428  19.690  54.029  1.00 35.75  ? 349 LYS A NZ  1 
ATOM   2784 N  N   . GLY A 1 350 ? 27.622  18.675  55.290  1.00 23.52  ? 350 GLY A N   1 
ATOM   2785 C  CA  . GLY A 1 350 ? 27.328  17.446  56.010  1.00 24.19  ? 350 GLY A CA  1 
ATOM   2786 C  C   . GLY A 1 350 ? 25.842  17.306  56.375  1.00 24.73  ? 350 GLY A C   1 
ATOM   2787 O  O   . GLY A 1 350 ? 25.394  16.257  56.775  1.00 24.80  ? 350 GLY A O   1 
ATOM   2788 N  N   . ASP A 1 351 ? 25.048  18.370  56.293  1.00 23.33  ? 351 ASP A N   1 
ATOM   2789 C  CA  . ASP A 1 351 ? 23.641  18.237  56.656  1.00 22.96  ? 351 ASP A CA  1 
ATOM   2790 C  C   . ASP A 1 351 ? 22.941  17.155  55.794  1.00 21.60  ? 351 ASP A C   1 
ATOM   2791 O  O   . ASP A 1 351 ? 23.152  17.051  54.600  1.00 18.75  ? 351 ASP A O   1 
ATOM   2792 C  CB  . ASP A 1 351 ? 22.979  19.619  56.636  1.00 24.09  ? 351 ASP A CB  1 
ATOM   2793 C  CG  . ASP A 1 351 ? 23.261  20.511  57.846  1.00 28.53  ? 351 ASP A CG  1 
ATOM   2794 O  OD1 . ASP A 1 351 ? 23.880  20.038  58.797  1.00 32.14  ? 351 ASP A OD1 1 
ATOM   2795 O  OD2 . ASP A 1 351 ? 22.786  21.685  57.856  1.00 36.89  ? 351 ASP A OD2 1 
ATOM   2796 N  N   . GLU A 1 352 ? 22.052  16.370  56.416  1.00 22.90  ? 352 GLU A N   1 
ATOM   2797 C  CA  . GLU A 1 352 ? 21.329  15.284  55.756  1.00 22.29  ? 352 GLU A CA  1 
ATOM   2798 C  C   . GLU A 1 352 ? 19.904  15.677  55.369  1.00 20.75  ? 352 GLU A C   1 
ATOM   2799 O  O   . GLU A 1 352 ? 19.214  16.387  56.095  1.00 19.79  ? 352 GLU A O   1 
ATOM   2800 C  CB  . GLU A 1 352 ? 21.261  14.076  56.686  1.00 24.73  ? 352 GLU A CB  1 
ATOM   2801 C  CG  . GLU A 1 352 ? 22.627  13.489  56.973  1.00 29.97  ? 352 GLU A CG  1 
ATOM   2802 C  CD  . GLU A 1 352 ? 22.572  12.352  57.978  1.00 40.84  ? 352 GLU A CD  1 
ATOM   2803 O  OE1 . GLU A 1 352 ? 21.870  11.335  57.698  1.00 41.29  ? 352 GLU A OE1 1 
ATOM   2804 O  OE2 . GLU A 1 352 ? 23.209  12.499  59.059  1.00 48.20  ? 352 GLU A OE2 1 
ATOM   2805 N  N   . LEU A 1 353 ? 19.506  15.183  54.197  1.00 19.50  ? 353 LEU A N   1 
ATOM   2806 C  CA  . LEU A 1 353 ? 18.184  15.337  53.611  1.00 19.29  ? 353 LEU A CA  1 
ATOM   2807 C  C   . LEU A 1 353 ? 17.673  13.941  53.286  1.00 19.87  ? 353 LEU A C   1 
ATOM   2808 O  O   . LEU A 1 353 ? 18.487  13.053  53.003  1.00 19.36  ? 353 LEU A O   1 
ATOM   2809 C  CB  . LEU A 1 353 ? 18.305  16.119  52.297  1.00 20.83  ? 353 LEU A CB  1 
ATOM   2810 C  CG  . LEU A 1 353 ? 18.973  17.494  52.355  1.00 22.33  ? 353 LEU A CG  1 
ATOM   2811 C  CD1 . LEU A 1 353 ? 18.933  18.169  51.005  1.00 24.42  ? 353 LEU A CD1 1 
ATOM   2812 C  CD2 . LEU A 1 353 ? 18.289  18.387  53.380  1.00 23.98  ? 353 LEU A CD2 1 
ATOM   2813 N  N   . MET A 1 354 ? 16.349  13.783  53.343  1.00 17.50  ? 354 MET A N   1 
ATOM   2814 C  CA  . MET A 1 354 ? 15.663  12.565  52.972  1.00 19.00  ? 354 MET A CA  1 
ATOM   2815 C  C   . MET A 1 354 ? 14.563  12.954  51.992  1.00 18.62  ? 354 MET A C   1 
ATOM   2816 O  O   . MET A 1 354 ? 13.709  13.785  52.286  1.00 15.87  ? 354 MET A O   1 
ATOM   2817 C  CB  . MET A 1 354 ? 15.037  11.895  54.195  1.00 21.55  ? 354 MET A CB  1 
ATOM   2818 C  CG  . MET A 1 354 ? 14.518  10.474  53.945  1.00 28.08  ? 354 MET A CG  1 
ATOM   2819 S  SD  . MET A 1 354 ? 15.854  9.243   53.770  1.00 36.04  ? 354 MET A SD  1 
ATOM   2820 C  CE  . MET A 1 354 ? 16.937  9.739   55.094  1.00 25.77  ? 354 MET A CE  1 
ATOM   2821 N  N   . VAL A 1 355 ? 14.646  12.411  50.786  1.00 17.03  ? 355 VAL A N   1 
ATOM   2822 C  CA  . VAL A 1 355 ? 13.605  12.616  49.799  1.00 16.28  ? 355 VAL A CA  1 
ATOM   2823 C  C   . VAL A 1 355 ? 12.483  11.619  50.097  1.00 18.00  ? 355 VAL A C   1 
ATOM   2824 O  O   . VAL A 1 355 ? 12.719  10.414  50.040  1.00 16.71  ? 355 VAL A O   1 
ATOM   2825 C  CB  . VAL A 1 355 ? 14.177  12.442  48.390  1.00 16.84  ? 355 VAL A CB  1 
ATOM   2826 C  CG1 . VAL A 1 355 ? 13.137  12.584  47.299  1.00 17.19  ? 355 VAL A CG1 1 
ATOM   2827 C  CG2 . VAL A 1 355 ? 15.339  13.384  48.160  1.00 19.14  ? 355 VAL A CG2 1 
ATOM   2828 N  N   . LEU A 1 356 ? 11.273  12.117  50.390  1.00 16.24  ? 356 LEU A N   1 
ATOM   2829 C  CA  . LEU A 1 356 ? 10.144  11.225  50.606  1.00 18.24  ? 356 LEU A CA  1 
ATOM   2830 C  C   . LEU A 1 356 ? 9.399   10.995  49.289  1.00 17.10  ? 356 LEU A C   1 
ATOM   2831 O  O   . LEU A 1 356 ? 8.538   11.787  48.898  1.00 18.16  ? 356 LEU A O   1 
ATOM   2832 C  CB  . LEU A 1 356 ? 9.240   11.848  51.674  1.00 21.99  ? 356 LEU A CB  1 
ATOM   2833 C  CG  . LEU A 1 356 ? 8.297   10.881  52.389  1.00 26.29  ? 356 LEU A CG  1 
ATOM   2834 C  CD1 . LEU A 1 356 ? 9.078   9.855   53.171  1.00 27.90  ? 356 LEU A CD1 1 
ATOM   2835 C  CD2 . LEU A 1 356 ? 7.364   11.614  53.330  1.00 28.45  ? 356 LEU A CD2 1 
ATOM   2836 N  N   . ILE A 1 357 ? 9.743   9.926   48.571  1.00 15.49  ? 357 ILE A N   1 
ATOM   2837 C  CA  . ILE A 1 357 ? 9.388   9.848   47.163  1.00 15.19  ? 357 ILE A CA  1 
ATOM   2838 C  C   . ILE A 1 357 ? 7.863   9.743   47.006  1.00 15.15  ? 357 ILE A C   1 
ATOM   2839 O  O   . ILE A 1 357 ? 7.276   10.383  46.120  1.00 15.08  ? 357 ILE A O   1 
ATOM   2840 C  CB  . ILE A 1 357 ? 10.107  8.694   46.440  1.00 14.60  ? 357 ILE A CB  1 
ATOM   2841 C  CG1 . ILE A 1 357 ? 11.629  8.688   46.614  1.00 13.75  ? 357 ILE A CG1 1 
ATOM   2842 C  CG2 . ILE A 1 357 ? 9.755   8.693   44.969  1.00 14.47  ? 357 ILE A CG2 1 
ATOM   2843 C  CD1 . ILE A 1 357 ? 12.289  7.445   46.088  1.00 14.06  ? 357 ILE A CD1 1 
ATOM   2844 N  N   . PRO A 1 358 ? 7.126   9.033   47.877  1.00 15.44  ? 358 PRO A N   1 
ATOM   2845 C  CA  . PRO A 1 358 ? 5.666   8.979   47.707  1.00 16.45  ? 358 PRO A CA  1 
ATOM   2846 C  C   . PRO A 1 358 ? 5.010   10.356  47.812  1.00 17.72  ? 358 PRO A C   1 
ATOM   2847 O  O   . PRO A 1 358 ? 3.999   10.595  47.139  1.00 15.20  ? 358 PRO A O   1 
ATOM   2848 C  CB  . PRO A 1 358 ? 5.181   8.071   48.831  1.00 16.40  ? 358 PRO A CB  1 
ATOM   2849 C  CG  . PRO A 1 358 ? 6.410   7.260   49.221  1.00 15.05  ? 358 PRO A CG  1 
ATOM   2850 C  CD  . PRO A 1 358 ? 7.582   8.198   49.000  1.00 14.98  ? 358 PRO A CD  1 
ATOM   2851 N  N   . GLN A 1 359 ? 5.618   11.259  48.607  1.00 17.42  ? 359 GLN A N   1 
ATOM   2852 C  CA  . GLN A 1 359 ? 5.096   12.609  48.742  1.00 18.32  ? 359 GLN A CA  1 
ATOM   2853 C  C   . GLN A 1 359 ? 5.449   13.473  47.543  1.00 17.02  ? 359 GLN A C   1 
ATOM   2854 O  O   . GLN A 1 359 ? 4.599   14.232  47.097  1.00 19.79  ? 359 GLN A O   1 
ATOM   2855 C  CB  . GLN A 1 359 ? 5.598   13.302  50.004  1.00 20.12  ? 359 GLN A CB  1 
ATOM   2856 C  CG  . GLN A 1 359 ? 4.933   12.794  51.253  1.00 21.15  ? 359 GLN A CG  1 
ATOM   2857 C  CD  . GLN A 1 359 ? 3.434   12.895  51.142  1.00 22.74  ? 359 GLN A CD  1 
ATOM   2858 O  OE1 . GLN A 1 359 ? 2.866   13.976  51.063  1.00 29.48  ? 359 GLN A OE1 1 
ATOM   2859 N  NE2 . GLN A 1 359 ? 2.793   11.754  51.095  1.00 22.96  ? 359 GLN A NE2 1 
ATOM   2860 N  N   . LEU A 1 360 ? 6.703   13.401  47.097  1.00 14.74  ? 360 LEU A N   1 
ATOM   2861 C  CA  . LEU A 1 360 ? 7.125   14.021  45.854  1.00 14.70  ? 360 LEU A CA  1 
ATOM   2862 C  C   . LEU A 1 360 ? 6.092   13.758  44.761  1.00 15.13  ? 360 LEU A C   1 
ATOM   2863 O  O   . LEU A 1 360 ? 5.701   14.676  44.025  1.00 13.32  ? 360 LEU A O   1 
ATOM   2864 C  CB  . LEU A 1 360 ? 8.483   13.466  45.432  1.00 13.57  ? 360 LEU A CB  1 
ATOM   2865 C  CG  . LEU A 1 360 ? 8.891   13.832  44.014  1.00 14.04  ? 360 LEU A CG  1 
ATOM   2866 C  CD1 . LEU A 1 360 ? 9.027   15.365  43.888  1.00 14.68  ? 360 LEU A CD1 1 
ATOM   2867 C  CD2 . LEU A 1 360 ? 10.177  13.133  43.628  1.00 15.14  ? 360 LEU A CD2 1 
ATOM   2868 N  N   . HIS A 1 361 ? 5.701   12.488  44.653  1.00 12.72  ? 361 HIS A N   1 
ATOM   2869 C  CA  . HIS A 1 361 ? 4.847   12.000  43.578  1.00 13.73  ? 361 HIS A CA  1 
ATOM   2870 C  C   . HIS A 1 361 ? 3.391   12.430  43.764  1.00 15.02  ? 361 HIS A C   1 
ATOM   2871 O  O   . HIS A 1 361 ? 2.574   12.075  42.923  1.00 16.51  ? 361 HIS A O   1 
ATOM   2872 C  CB  . HIS A 1 361 ? 4.925   10.466  43.517  1.00 12.48  ? 361 HIS A CB  1 
ATOM   2873 C  CG  . HIS A 1 361 ? 6.224   9.967   42.976  1.00 12.00  ? 361 HIS A CG  1 
ATOM   2874 N  ND1 . HIS A 1 361 ? 6.541   8.624   42.930  1.00 13.00  ? 361 HIS A ND1 1 
ATOM   2875 C  CD2 . HIS A 1 361 ? 7.301   10.622  42.496  1.00 11.99  ? 361 HIS A CD2 1 
ATOM   2876 C  CE1 . HIS A 1 361 ? 7.738   8.480   42.373  1.00 11.93  ? 361 HIS A CE1 1 
ATOM   2877 N  NE2 . HIS A 1 361 ? 8.225   9.683   42.137  1.00 12.63  ? 361 HIS A NE2 1 
ATOM   2878 N  N   . ARG A 1 362 ? 3.066   13.060  44.909  1.00 15.64  ? 362 ARG A N   1 
ATOM   2879 C  CA  . ARG A 1 362 ? 1.742   13.578  45.187  1.00 15.71  ? 362 ARG A CA  1 
ATOM   2880 C  C   . ARG A 1 362 ? 1.747   15.107  45.214  1.00 18.03  ? 362 ARG A C   1 
ATOM   2881 O  O   . ARG A 1 362 ? 0.798   15.693  45.730  1.00 21.41  ? 362 ARG A O   1 
ATOM   2882 C  CB  . ARG A 1 362 ? 1.211   13.018  46.512  1.00 16.05  ? 362 ARG A CB  1 
ATOM   2883 C  CG  . ARG A 1 362 ? 0.855   11.544  46.475  1.00 14.84  ? 362 ARG A CG  1 
ATOM   2884 C  CD  . ARG A 1 362 ? 0.634   10.967  47.858  1.00 16.33  ? 362 ARG A CD  1 
ATOM   2885 N  NE  . ARG A 1 362 ? 0.049   9.616   47.815  1.00 14.46  ? 362 ARG A NE  1 
ATOM   2886 C  CZ  . ARG A 1 362 ? 0.696   8.519   47.434  1.00 13.98  ? 362 ARG A CZ  1 
ATOM   2887 N  NH1 . ARG A 1 362 ? 1.941   8.593   47.008  1.00 13.54  ? 362 ARG A NH1 1 
ATOM   2888 N  NH2 . ARG A 1 362 ? 0.124   7.338   47.578  1.00 13.80  ? 362 ARG A NH2 1 
ATOM   2889 N  N   . ASP A 1 363 ? 2.809   15.754  44.693  1.00 19.26  ? 363 ASP A N   1 
ATOM   2890 C  CA  . ASP A 1 363 ? 2.879   17.207  44.618  1.00 17.24  ? 363 ASP A CA  1 
ATOM   2891 C  C   . ASP A 1 363 ? 1.824   17.720  43.650  1.00 16.57  ? 363 ASP A C   1 
ATOM   2892 O  O   . ASP A 1 363 ? 2.004   17.605  42.454  1.00 13.85  ? 363 ASP A O   1 
ATOM   2893 C  CB  . ASP A 1 363 ? 4.241   17.661  44.083  1.00 18.13  ? 363 ASP A CB  1 
ATOM   2894 C  CG  . ASP A 1 363 ? 4.484   19.149  44.224  1.00 20.02  ? 363 ASP A CG  1 
ATOM   2895 O  OD1 . ASP A 1 363 ? 3.461   19.901  44.334  1.00 19.10  ? 363 ASP A OD1 1 
ATOM   2896 O  OD2 . ASP A 1 363 ? 5.700   19.548  44.269  1.00 18.49  ? 363 ASP A OD2 1 
ATOM   2897 N  N   . LYS A 1 364 ? 0.776   18.358  44.172  1.00 20.36  ? 364 LYS A N   1 
ATOM   2898 C  CA  . LYS A 1 364 ? -0.350  18.774  43.340  1.00 22.63  ? 364 LYS A CA  1 
ATOM   2899 C  C   . LYS A 1 364 ? 0.038   19.859  42.338  1.00 20.81  ? 364 LYS A C   1 
ATOM   2900 O  O   . LYS A 1 364 ? -0.634  20.003  41.320  1.00 18.59  ? 364 LYS A O   1 
ATOM   2901 C  CB  . LYS A 1 364 ? -1.504  19.275  44.201  1.00 25.38  ? 364 LYS A CB  1 
ATOM   2902 C  CG  . LYS A 1 364 ? -2.169  18.201  45.043  1.00 27.40  ? 364 LYS A CG  1 
ATOM   2903 C  CD  . LYS A 1 364 ? -3.269  18.696  45.964  1.00 29.86  ? 364 LYS A CD  1 
ATOM   2904 C  CE  . LYS A 1 364 ? -3.873  17.586  46.791  1.00 33.85  ? 364 LYS A CE  1 
ATOM   2905 N  NZ  . LYS A 1 364 ? -4.718  16.700  45.954  1.00 38.85  ? 364 LYS A NZ  1 
ATOM   2906 N  N   . THR A 1 365 ? 1.099   20.606  42.645  1.00 19.30  ? 365 THR A N   1 
ATOM   2907 C  CA  . THR A 1 365 ? 1.628   21.644  41.789  1.00 21.35  ? 365 THR A CA  1 
ATOM   2908 C  C   . THR A 1 365 ? 2.101   21.074  40.464  1.00 18.91  ? 365 THR A C   1 
ATOM   2909 O  O   . THR A 1 365 ? 2.065   21.756  39.447  1.00 18.55  ? 365 THR A O   1 
ATOM   2910 C  CB  . THR A 1 365 ? 2.809   22.311  42.512  1.00 27.70  ? 365 THR A CB  1 
ATOM   2911 O  OG1 . THR A 1 365 ? 2.232   23.297  43.370  1.00 32.08  ? 365 THR A OG1 1 
ATOM   2912 C  CG2 . THR A 1 365 ? 3.830   22.922  41.590  1.00 33.20  ? 365 THR A CG2 1 
ATOM   2913 N  N   . ILE A 1 366 ? 2.574   19.821  40.504  1.00 19.42  ? 366 ILE A N   1 
ATOM   2914 C  CA  . ILE A 1 366 ? 3.104   19.106  39.357  1.00 18.51  ? 366 ILE A CA  1 
ATOM   2915 C  C   . ILE A 1 366 ? 2.017   18.303  38.657  1.00 18.16  ? 366 ILE A C   1 
ATOM   2916 O  O   . ILE A 1 366 ? 1.964   18.340  37.415  1.00 17.11  ? 366 ILE A O   1 
ATOM   2917 C  CB  . ILE A 1 366 ? 4.233   18.161  39.807  1.00 18.82  ? 366 ILE A CB  1 
ATOM   2918 C  CG1 . ILE A 1 366 ? 5.417   18.933  40.385  1.00 20.00  ? 366 ILE A CG1 1 
ATOM   2919 C  CG2 . ILE A 1 366 ? 4.659   17.251  38.685  1.00 20.86  ? 366 ILE A CG2 1 
ATOM   2920 C  CD1 . ILE A 1 366 ? 6.140   19.816  39.374  1.00 22.13  ? 366 ILE A CD1 1 
ATOM   2921 N  N   . TRP A 1 367 ? 1.262   17.509  39.447  1.00 17.24  ? 367 TRP A N   1 
ATOM   2922 C  CA  . TRP A 1 367 ? 0.425   16.443  38.913  1.00 17.89  ? 367 TRP A CA  1 
ATOM   2923 C  C   . TRP A 1 367 ? -1.028  16.861  38.748  1.00 19.48  ? 367 TRP A C   1 
ATOM   2924 O  O   . TRP A 1 367 ? -1.788  16.178  38.053  1.00 19.14  ? 367 TRP A O   1 
ATOM   2925 C  CB  . TRP A 1 367 ? 0.488   15.209  39.819  1.00 18.58  ? 367 TRP A CB  1 
ATOM   2926 C  CG  . TRP A 1 367 ? 1.889   14.655  39.869  1.00 18.48  ? 367 TRP A CG  1 
ATOM   2927 C  CD1 . TRP A 1 367 ? 2.790   14.892  40.857  1.00 17.17  ? 367 TRP A CD1 1 
ATOM   2928 C  CD2 . TRP A 1 367 ? 2.542   13.801  38.911  1.00 16.74  ? 367 TRP A CD2 1 
ATOM   2929 N  NE1 . TRP A 1 367 ? 3.979   14.298  40.559  1.00 16.87  ? 367 TRP A NE1 1 
ATOM   2930 C  CE2 . TRP A 1 367 ? 3.859   13.615  39.382  1.00 16.38  ? 367 TRP A CE2 1 
ATOM   2931 C  CE3 . TRP A 1 367 ? 2.168   13.202  37.709  1.00 15.31  ? 367 TRP A CE3 1 
ATOM   2932 C  CZ2 . TRP A 1 367 ? 4.784   12.827  38.706  1.00 16.45  ? 367 TRP A CZ2 1 
ATOM   2933 C  CZ3 . TRP A 1 367 ? 3.088   12.449  37.032  1.00 15.02  ? 367 TRP A CZ3 1 
ATOM   2934 C  CH2 . TRP A 1 367 ? 4.381   12.260  37.519  1.00 15.83  ? 367 TRP A CH2 1 
ATOM   2935 N  N   . GLY A 1 368 ? -1.441  17.931  39.437  1.00 21.98  ? 368 GLY A N   1 
ATOM   2936 C  CA  . GLY A 1 368 ? -2.853  18.280  39.478  1.00 22.65  ? 368 GLY A CA  1 
ATOM   2937 C  C   . GLY A 1 368 ? -3.488  17.816  40.782  1.00 22.30  ? 368 GLY A C   1 
ATOM   2938 O  O   . GLY A 1 368 ? -2.803  17.217  41.602  1.00 19.73  ? 368 GLY A O   1 
ATOM   2939 N  N   . ASP A 1 369 ? -4.778  18.119  40.973  1.00 23.30  ? 369 ASP A N   1 
ATOM   2940 C  CA  . ASP A 1 369 ? -5.442  17.909  42.255  1.00 28.20  ? 369 ASP A CA  1 
ATOM   2941 C  C   . ASP A 1 369 ? -5.788  16.447  42.505  1.00 27.85  ? 369 ASP A C   1 
ATOM   2942 O  O   . ASP A 1 369 ? -5.939  16.056  43.677  1.00 26.70  ? 369 ASP A O   1 
ATOM   2943 C  CB  . ASP A 1 369 ? -6.752  18.700  42.400  1.00 32.05  ? 369 ASP A CB  1 
ATOM   2944 C  CG  . ASP A 1 369 ? -6.558  20.058  43.054  1.00 40.53  ? 369 ASP A CG  1 
ATOM   2945 O  OD1 . ASP A 1 369 ? -5.399  20.516  43.097  1.00 42.85  ? 369 ASP A OD1 1 
ATOM   2946 O  OD2 . ASP A 1 369 ? -7.558  20.630  43.555  1.00 50.04  ? 369 ASP A OD2 1 
ATOM   2947 N  N   . ASP A 1 370 ? -5.908  15.658  41.429  1.00 24.99  ? 370 ASP A N   1 
ATOM   2948 C  CA  . ASP A 1 370 ? -6.481  14.313  41.514  1.00 27.43  ? 370 ASP A CA  1 
ATOM   2949 C  C   . ASP A 1 370 ? -5.375  13.291  41.769  1.00 24.22  ? 370 ASP A C   1 
ATOM   2950 O  O   . ASP A 1 370 ? -5.339  12.224  41.161  1.00 25.81  ? 370 ASP A O   1 
ATOM   2951 C  CB  . ASP A 1 370 ? -7.185  13.922  40.212  1.00 29.92  ? 370 ASP A CB  1 
ATOM   2952 C  CG  . ASP A 1 370 ? -6.230  13.945  39.025  1.00 34.84  ? 370 ASP A CG  1 
ATOM   2953 O  OD1 . ASP A 1 370 ? -5.105  14.526  39.166  1.00 37.12  ? 370 ASP A OD1 1 
ATOM   2954 O  OD2 . ASP A 1 370 ? -6.591  13.378  37.978  1.00 39.92  ? 370 ASP A OD2 1 
ATOM   2955 N  N   . VAL A 1 371 ? -4.512  13.604  42.733  1.00 23.99  ? 371 VAL A N   1 
ATOM   2956 C  CA  . VAL A 1 371 ? -3.194  13.014  42.816  1.00 24.58  ? 371 VAL A CA  1 
ATOM   2957 C  C   . VAL A 1 371 ? -3.279  11.573  43.332  1.00 23.17  ? 371 VAL A C   1 
ATOM   2958 O  O   . VAL A 1 371 ? -2.356  10.788  43.111  1.00 25.00  ? 371 VAL A O   1 
ATOM   2959 C  CB  . VAL A 1 371 ? -2.318  13.956  43.667  1.00 28.30  ? 371 VAL A CB  1 
ATOM   2960 C  CG1 . VAL A 1 371 ? -2.190  13.517  45.109  1.00 29.34  ? 371 VAL A CG1 1 
ATOM   2961 C  CG2 . VAL A 1 371 ? -0.963  14.194  43.035  1.00 27.63  ? 371 VAL A CG2 1 
ATOM   2962 N  N   . GLU A 1 372 ? -4.402  11.193  43.950  1.00 22.13  ? 372 GLU A N   1 
ATOM   2963 C  CA  . GLU A 1 372 ? -4.589  9.852   44.494  1.00 24.46  ? 372 GLU A CA  1 
ATOM   2964 C  C   . GLU A 1 372 ? -5.264  8.891   43.508  1.00 24.29  ? 372 GLU A C   1 
ATOM   2965 O  O   . GLU A 1 372 ? -5.450  7.718   43.824  1.00 21.36  ? 372 GLU A O   1 
ATOM   2966 C  CB  . GLU A 1 372 ? -5.430  9.931   45.765  1.00 25.43  ? 372 GLU A CB  1 
ATOM   2967 C  CG  . GLU A 1 372 ? -4.680  10.554  46.925  1.00 31.60  ? 372 GLU A CG  1 
ATOM   2968 C  CD  . GLU A 1 372 ? -3.574  9.664   47.484  1.00 33.81  ? 372 GLU A CD  1 
ATOM   2969 O  OE1 . GLU A 1 372 ? -3.772  8.412   47.504  1.00 34.47  ? 372 GLU A OE1 1 
ATOM   2970 O  OE2 . GLU A 1 372 ? -2.553  10.214  47.951  1.00 29.52  ? 372 GLU A OE2 1 
ATOM   2971 N  N   . GLU A 1 373 ? -5.635  9.371   42.315  1.00 25.54  ? 373 GLU A N   1 
ATOM   2972 C  CA  . GLU A 1 373 ? -6.298  8.532   41.330  1.00 25.45  ? 373 GLU A CA  1 
ATOM   2973 C  C   . GLU A 1 373 ? -5.247  7.756   40.537  1.00 20.14  ? 373 GLU A C   1 
ATOM   2974 O  O   . GLU A 1 373 ? -4.156  8.279   40.315  1.00 18.63  ? 373 GLU A O   1 
ATOM   2975 C  CB  . GLU A 1 373 ? -7.128  9.379   40.367  1.00 30.01  ? 373 GLU A CB  1 
ATOM   2976 C  CG  . GLU A 1 373 ? -8.459  9.808   40.948  1.00 35.49  ? 373 GLU A CG  1 
ATOM   2977 C  CD  . GLU A 1 373 ? -9.358  10.490  39.928  1.00 44.65  ? 373 GLU A CD  1 
ATOM   2978 O  OE1 . GLU A 1 373 ? -9.079  10.374  38.712  1.00 53.50  ? 373 GLU A OE1 1 
ATOM   2979 O  OE2 . GLU A 1 373 ? -10.310 11.169  40.349  1.00 53.23  ? 373 GLU A OE2 1 
ATOM   2980 N  N   . PHE A 1 374 ? -5.607  6.553   40.102  1.00 17.47  ? 374 PHE A N   1 
ATOM   2981 C  CA  . PHE A 1 374 ? -4.730  5.735   39.271  1.00 16.28  ? 374 PHE A CA  1 
ATOM   2982 C  C   . PHE A 1 374 ? -5.026  6.036   37.808  1.00 17.64  ? 374 PHE A C   1 
ATOM   2983 O  O   . PHE A 1 374 ? -6.024  5.568   37.261  1.00 18.41  ? 374 PHE A O   1 
ATOM   2984 C  CB  . PHE A 1 374 ? -4.880  4.237   39.584  1.00 13.99  ? 374 PHE A CB  1 
ATOM   2985 C  CG  . PHE A 1 374 ? -3.882  3.337   38.914  1.00 13.69  ? 374 PHE A CG  1 
ATOM   2986 C  CD1 . PHE A 1 374 ? -2.544  3.352   39.314  1.00 14.08  ? 374 PHE A CD1 1 
ATOM   2987 C  CD2 . PHE A 1 374 ? -4.245  2.481   37.890  1.00 14.52  ? 374 PHE A CD2 1 
ATOM   2988 C  CE1 . PHE A 1 374 ? -1.599  2.551   38.706  1.00 14.71  ? 374 PHE A CE1 1 
ATOM   2989 C  CE2 . PHE A 1 374 ? -3.277  1.727   37.238  1.00 16.15  ? 374 PHE A CE2 1 
ATOM   2990 C  CZ  . PHE A 1 374 ? -1.958  1.745   37.661  1.00 15.87  ? 374 PHE A CZ  1 
ATOM   2991 N  N   . ARG A 1 375 ? -4.162  6.827   37.171  1.00 17.63  ? 375 ARG A N   1 
ATOM   2992 C  CA  . ARG A 1 375 ? -4.385  7.210   35.786  1.00 17.78  ? 375 ARG A CA  1 
ATOM   2993 C  C   . ARG A 1 375 ? -3.096  7.037   34.984  1.00 16.46  ? 375 ARG A C   1 
ATOM   2994 O  O   . ARG A 1 375 ? -2.284  7.969   34.895  1.00 16.19  ? 375 ARG A O   1 
ATOM   2995 C  CB  . ARG A 1 375 ? -4.866  8.665   35.719  1.00 20.47  ? 375 ARG A CB  1 
ATOM   2996 C  CG  . ARG A 1 375 ? -6.209  8.903   36.379  1.00 26.08  ? 375 ARG A CG  1 
ATOM   2997 C  CD  . ARG A 1 375 ? -6.897  10.114  35.757  1.00 34.06  ? 375 ARG A CD  1 
ATOM   2998 N  NE  . ARG A 1 375 ? -6.156  11.358  35.929  1.00 39.30  ? 375 ARG A NE  1 
ATOM   2999 C  CZ  . ARG A 1 375 ? -5.503  12.022  34.973  1.00 44.12  ? 375 ARG A CZ  1 
ATOM   3000 N  NH1 . ARG A 1 375 ? -5.374  11.531  33.752  1.00 48.48  ? 375 ARG A NH1 1 
ATOM   3001 N  NH2 . ARG A 1 375 ? -4.931  13.176  35.268  1.00 45.02  ? 375 ARG A NH2 1 
ATOM   3002 N  N   . PRO A 1 376 ? -2.874  5.853   34.368  1.00 14.42  ? 376 PRO A N   1 
ATOM   3003 C  CA  . PRO A 1 376 ? -1.676  5.588   33.552  1.00 14.76  ? 376 PRO A CA  1 
ATOM   3004 C  C   . PRO A 1 376 ? -1.372  6.623   32.464  1.00 15.04  ? 376 PRO A C   1 
ATOM   3005 O  O   . PRO A 1 376 ? -0.215  6.896   32.113  1.00 13.40  ? 376 PRO A O   1 
ATOM   3006 C  CB  . PRO A 1 376 ? -1.941  4.182   32.977  1.00 14.80  ? 376 PRO A CB  1 
ATOM   3007 C  CG  . PRO A 1 376 ? -2.811  3.555   34.051  1.00 13.87  ? 376 PRO A CG  1 
ATOM   3008 C  CD  . PRO A 1 376 ? -3.725  4.659   34.513  1.00 14.92  ? 376 PRO A CD  1 
ATOM   3009 N  N   . GLU A 1 377 ? -2.428  7.289   32.012  1.00 16.17  ? 377 GLU A N   1 
ATOM   3010 C  CA  . GLU A 1 377 ? -2.354  8.234   30.902  1.00 18.67  ? 377 GLU A CA  1 
ATOM   3011 C  C   . GLU A 1 377 ? -1.542  9.472   31.266  1.00 19.62  ? 377 GLU A C   1 
ATOM   3012 O  O   . GLU A 1 377 ? -1.194  10.228  30.367  1.00 22.07  ? 377 GLU A O   1 
ATOM   3013 C  CB  . GLU A 1 377 ? -3.767  8.602   30.427  1.00 21.38  ? 377 GLU A CB  1 
ATOM   3014 C  CG  . GLU A 1 377 ? -4.573  7.389   29.975  1.00 25.90  ? 377 GLU A CG  1 
ATOM   3015 C  CD  . GLU A 1 377 ? -5.199  6.513   31.057  1.00 26.82  ? 377 GLU A CD  1 
ATOM   3016 O  OE1 . GLU A 1 377 ? -5.768  5.440   30.668  1.00 28.83  ? 377 GLU A OE1 1 
ATOM   3017 O  OE2 . GLU A 1 377 ? -5.193  6.925   32.276  1.00 23.49  ? 377 GLU A OE2 1 
ATOM   3018 N  N   . ARG A 1 378 ? -1.214  9.669   32.554  1.00 18.79  ? 378 ARG A N   1 
ATOM   3019 C  CA  . ARG A 1 378 ? -0.272  10.706  32.966  1.00 20.33  ? 378 ARG A CA  1 
ATOM   3020 C  C   . ARG A 1 378 ? 1.109   10.480  32.348  1.00 21.66  ? 378 ARG A C   1 
ATOM   3021 O  O   . ARG A 1 378 ? 1.899   11.426  32.254  1.00 22.77  ? 378 ARG A O   1 
ATOM   3022 C  CB  . ARG A 1 378 ? -0.030  10.662  34.475  1.00 19.68  ? 378 ARG A CB  1 
ATOM   3023 C  CG  . ARG A 1 378 ? -1.233  11.021  35.316  1.00 17.91  ? 378 ARG A CG  1 
ATOM   3024 C  CD  . ARG A 1 378 ? -0.827  10.933  36.760  1.00 18.52  ? 378 ARG A CD  1 
ATOM   3025 N  NE  . ARG A 1 378 ? -1.948  10.549  37.568  1.00 17.76  ? 378 ARG A NE  1 
ATOM   3026 C  CZ  . ARG A 1 378 ? -2.720  11.389  38.232  1.00 18.62  ? 378 ARG A CZ  1 
ATOM   3027 N  NH1 . ARG A 1 378 ? -2.577  12.691  38.070  1.00 18.89  ? 378 ARG A NH1 1 
ATOM   3028 N  NH2 . ARG A 1 378 ? -3.671  10.927  39.008  1.00 20.43  ? 378 ARG A NH2 1 
ATOM   3029 N  N   . PHE A 1 379 ? 1.416   9.217   31.986  1.00 17.86  ? 379 PHE A N   1 
ATOM   3030 C  CA  . PHE A 1 379 ? 2.711   8.859   31.431  1.00 19.57  ? 379 PHE A CA  1 
ATOM   3031 C  C   . PHE A 1 379 ? 2.667   8.589   29.929  1.00 20.88  ? 379 PHE A C   1 
ATOM   3032 O  O   . PHE A 1 379 ? 3.643   8.100   29.375  1.00 21.10  ? 379 PHE A O   1 
ATOM   3033 C  CB  . PHE A 1 379 ? 3.271   7.651   32.166  1.00 18.19  ? 379 PHE A CB  1 
ATOM   3034 C  CG  . PHE A 1 379 ? 3.657   7.978   33.578  1.00 17.39  ? 379 PHE A CG  1 
ATOM   3035 C  CD1 . PHE A 1 379 ? 4.900   8.531   33.854  1.00 17.15  ? 379 PHE A CD1 1 
ATOM   3036 C  CD2 . PHE A 1 379 ? 2.775   7.767   34.611  1.00 14.97  ? 379 PHE A CD2 1 
ATOM   3037 C  CE1 . PHE A 1 379 ? 5.238   8.884   35.150  1.00 15.28  ? 379 PHE A CE1 1 
ATOM   3038 C  CE2 . PHE A 1 379 ? 3.100   8.164   35.895  1.00 15.42  ? 379 PHE A CE2 1 
ATOM   3039 C  CZ  . PHE A 1 379 ? 4.337   8.702   36.163  1.00 14.77  ? 379 PHE A CZ  1 
ATOM   3040 N  N   . GLU A 1 380 ? 1.587   8.986   29.243  1.00 23.65  ? 380 GLU A N   1 
ATOM   3041 C  CA  . GLU A 1 380 ? 1.522   8.732   27.808  1.00 30.78  ? 380 GLU A CA  1 
ATOM   3042 C  C   . GLU A 1 380 ? 2.632   9.478   27.076  1.00 32.61  ? 380 GLU A C   1 
ATOM   3043 O  O   . GLU A 1 380 ? 3.177   8.941   26.113  1.00 33.14  ? 380 GLU A O   1 
ATOM   3044 C  CB  . GLU A 1 380 ? 0.154   9.036   27.188  1.00 36.02  ? 380 GLU A CB  1 
ATOM   3045 C  CG  . GLU A 1 380 ? -0.342  10.453  27.383  1.00 43.86  ? 380 GLU A CG  1 
ATOM   3046 C  CD  . GLU A 1 380 ? -1.863  10.525  27.419  1.00 49.57  ? 380 GLU A CD  1 
ATOM   3047 O  OE1 . GLU A 1 380 ? -2.515  9.599   26.871  1.00 53.04  ? 380 GLU A OE1 1 
ATOM   3048 O  OE2 . GLU A 1 380 ? -2.396  11.450  28.057  1.00 52.40  ? 380 GLU A OE2 1 
ATOM   3049 N  N   . ASN A 1 381 ? 2.992   10.680  27.549  1.00 32.04  ? 381 ASN A N   1 
ATOM   3050 C  CA  . ASN A 1 381 ? 4.028   11.459  26.892  1.00 37.31  ? 381 ASN A CA  1 
ATOM   3051 C  C   . ASN A 1 381 ? 5.124   11.779  27.907  1.00 35.80  ? 381 ASN A C   1 
ATOM   3052 O  O   . ASN A 1 381 ? 5.010   12.753  28.649  1.00 30.91  ? 381 ASN A O   1 
ATOM   3053 C  CB  . ASN A 1 381 ? 3.423   12.684  26.206  1.00 41.18  ? 381 ASN A CB  1 
ATOM   3054 C  CG  . ASN A 1 381 ? 4.308   13.253  25.116  1.00 48.44  ? 381 ASN A CG  1 
ATOM   3055 O  OD1 . ASN A 1 381 ? 3.822   13.977  24.253  1.00 46.29  ? 381 ASN A OD1 1 
ATOM   3056 N  ND2 . ASN A 1 381 ? 5.596   12.925  25.119  1.00 55.48  ? 381 ASN A ND2 1 
ATOM   3057 N  N   . PRO A 1 382 ? 6.197   10.955  27.953  1.00 34.70  ? 382 PRO A N   1 
ATOM   3058 C  CA  . PRO A 1 382 ? 7.301   11.128  28.899  1.00 35.43  ? 382 PRO A CA  1 
ATOM   3059 C  C   . PRO A 1 382 ? 7.788   12.564  29.078  1.00 28.85  ? 382 PRO A C   1 
ATOM   3060 O  O   . PRO A 1 382 ? 8.062   12.978  30.201  1.00 30.48  ? 382 PRO A O   1 
ATOM   3061 C  CB  . PRO A 1 382 ? 8.434   10.288  28.284  1.00 36.91  ? 382 PRO A CB  1 
ATOM   3062 C  CG  . PRO A 1 382 ? 7.722   9.190   27.523  1.00 39.46  ? 382 PRO A CG  1 
ATOM   3063 C  CD  . PRO A 1 382 ? 6.430   9.815   27.044  1.00 39.83  ? 382 PRO A CD  1 
ATOM   3064 N  N   . SER A 1 383 ? 7.883   13.318  27.977  1.00 24.03  ? 383 SER A N   1 
ATOM   3065 C  CA  . SER A 1 383 ? 8.476   14.650  28.029  1.00 25.86  ? 383 SER A CA  1 
ATOM   3066 C  C   . SER A 1 383 ? 7.630   15.632  28.838  1.00 22.49  ? 383 SER A C   1 
ATOM   3067 O  O   . SER A 1 383 ? 8.154   16.650  29.295  1.00 21.49  ? 383 SER A O   1 
ATOM   3068 C  CB  . SER A 1 383 ? 8.783   15.182  26.638  1.00 24.95  ? 383 SER A CB  1 
ATOM   3069 O  OG  . SER A 1 383 ? 9.881   14.464  26.105  1.00 25.59  ? 383 SER A OG  1 
ATOM   3070 N  N   . ALA A 1 384 ? 6.349   15.286  29.063  1.00 21.33  ? 384 ALA A N   1 
ATOM   3071 C  CA  . ALA A 1 384 ? 5.423   16.116  29.823  1.00 22.87  ? 384 ALA A CA  1 
ATOM   3072 C  C   . ALA A 1 384 ? 5.668   16.025  31.339  1.00 22.19  ? 384 ALA A C   1 
ATOM   3073 O  O   . ALA A 1 384 ? 5.044   16.743  32.112  1.00 22.04  ? 384 ALA A O   1 
ATOM   3074 C  CB  . ALA A 1 384 ? 3.994   15.723  29.485  1.00 23.75  ? 384 ALA A CB  1 
ATOM   3075 N  N   . ILE A 1 385 ? 6.580   15.167  31.786  1.00 22.58  ? 385 ILE A N   1 
ATOM   3076 C  CA  . ILE A 1 385 ? 6.843   15.032  33.214  1.00 25.39  ? 385 ILE A CA  1 
ATOM   3077 C  C   . ILE A 1 385 ? 8.075   15.883  33.511  1.00 25.67  ? 385 ILE A C   1 
ATOM   3078 O  O   . ILE A 1 385 ? 9.165   15.588  33.010  1.00 24.74  ? 385 ILE A O   1 
ATOM   3079 C  CB  . ILE A 1 385 ? 7.062   13.559  33.635  1.00 27.77  ? 385 ILE A CB  1 
ATOM   3080 C  CG1 . ILE A 1 385 ? 5.936   12.648  33.142  1.00 30.44  ? 385 ILE A CG1 1 
ATOM   3081 C  CG2 . ILE A 1 385 ? 7.282   13.423  35.139  1.00 25.91  ? 385 ILE A CG2 1 
ATOM   3082 C  CD1 . ILE A 1 385 ? 4.567   13.219  33.358  1.00 30.15  ? 385 ILE A CD1 1 
ATOM   3083 N  N   . PRO A 1 386 ? 7.925   16.954  34.325  1.00 26.65  ? 386 PRO A N   1 
ATOM   3084 C  CA  . PRO A 1 386 ? 9.035   17.854  34.636  1.00 27.78  ? 386 PRO A CA  1 
ATOM   3085 C  C   . PRO A 1 386 ? 10.255  17.128  35.177  1.00 30.13  ? 386 PRO A C   1 
ATOM   3086 O  O   . PRO A 1 386 ? 10.166  16.050  35.760  1.00 28.03  ? 386 PRO A O   1 
ATOM   3087 C  CB  . PRO A 1 386 ? 8.433   18.762  35.704  1.00 27.00  ? 386 PRO A CB  1 
ATOM   3088 C  CG  . PRO A 1 386 ? 6.986   18.799  35.344  1.00 27.71  ? 386 PRO A CG  1 
ATOM   3089 C  CD  . PRO A 1 386 ? 6.672   17.370  34.968  1.00 26.26  ? 386 PRO A CD  1 
ATOM   3090 N  N   . GLN A 1 387 ? 11.418  17.753  35.028  1.00 35.29  ? 387 GLN A N   1 
ATOM   3091 C  CA  . GLN A 1 387 ? 12.610  17.143  35.577  1.00 34.44  ? 387 GLN A CA  1 
ATOM   3092 C  C   . GLN A 1 387 ? 12.527  17.107  37.102  1.00 27.79  ? 387 GLN A C   1 
ATOM   3093 O  O   . GLN A 1 387 ? 11.996  18.014  37.746  1.00 30.75  ? 387 GLN A O   1 
ATOM   3094 C  CB  . GLN A 1 387 ? 13.873  17.839  35.088  1.00 42.07  ? 387 GLN A CB  1 
ATOM   3095 C  CG  . GLN A 1 387 ? 15.103  16.994  35.365  1.00 44.91  ? 387 GLN A CG  1 
ATOM   3096 C  CD  . GLN A 1 387 ? 16.177  17.256  34.349  1.00 49.37  ? 387 GLN A CD  1 
ATOM   3097 O  OE1 . GLN A 1 387 ? 15.884  17.658  33.225  1.00 53.25  ? 387 GLN A OE1 1 
ATOM   3098 N  NE2 . GLN A 1 387 ? 17.419  17.026  34.750  1.00 46.37  ? 387 GLN A NE2 1 
ATOM   3099 N  N   . HIS A 1 388 ? 12.968  15.971  37.641  1.00 23.04  ? 388 HIS A N   1 
ATOM   3100 C  CA  . HIS A 1 388 ? 13.021  15.694  39.063  1.00 20.51  ? 388 HIS A CA  1 
ATOM   3101 C  C   . HIS A 1 388 ? 11.641  15.538  39.703  1.00 17.18  ? 388 HIS A C   1 
ATOM   3102 O  O   . HIS A 1 388 ? 11.536  15.496  40.935  1.00 17.59  ? 388 HIS A O   1 
ATOM   3103 C  CB  . HIS A 1 388 ? 13.949  16.697  39.758  1.00 23.08  ? 388 HIS A CB  1 
ATOM   3104 C  CG  . HIS A 1 388 ? 15.342  16.621  39.244  1.00 24.67  ? 388 HIS A CG  1 
ATOM   3105 N  ND1 . HIS A 1 388 ? 15.987  15.424  38.984  1.00 28.40  ? 388 HIS A ND1 1 
ATOM   3106 C  CD2 . HIS A 1 388 ? 16.204  17.588  38.925  1.00 28.32  ? 388 HIS A CD2 1 
ATOM   3107 C  CE1 . HIS A 1 388 ? 17.208  15.682  38.531  1.00 30.13  ? 388 HIS A CE1 1 
ATOM   3108 N  NE2 . HIS A 1 388 ? 17.361  16.992  38.500  1.00 27.96  ? 388 HIS A NE2 1 
ATOM   3109 N  N   . ALA A 1 389 ? 10.592  15.406  38.893  1.00 16.20  ? 389 ALA A N   1 
ATOM   3110 C  CA  . ALA A 1 389 ? 9.255   15.253  39.447  1.00 15.99  ? 389 ALA A CA  1 
ATOM   3111 C  C   . ALA A 1 389 ? 8.898   13.781  39.673  1.00 14.47  ? 389 ALA A C   1 
ATOM   3112 O  O   . ALA A 1 389 ? 7.988   13.470  40.432  1.00 15.66  ? 389 ALA A O   1 
ATOM   3113 C  CB  . ALA A 1 389 ? 8.269   15.908  38.538  1.00 17.24  ? 389 ALA A CB  1 
ATOM   3114 N  N   . PHE A 1 390 ? 9.610   12.864  39.025  1.00 14.81  ? 390 PHE A N   1 
ATOM   3115 C  CA  . PHE A 1 390 ? 9.287   11.435  39.121  1.00 13.64  ? 390 PHE A CA  1 
ATOM   3116 C  C   . PHE A 1 390 ? 10.576  10.653  39.345  1.00 14.99  ? 390 PHE A C   1 
ATOM   3117 O  O   . PHE A 1 390 ? 11.394  10.590  38.436  1.00 17.07  ? 390 PHE A O   1 
ATOM   3118 C  CB  . PHE A 1 390 ? 8.574   11.020  37.837  1.00 13.92  ? 390 PHE A CB  1 
ATOM   3119 C  CG  . PHE A 1 390 ? 8.167   9.568   37.772  1.00 14.44  ? 390 PHE A CG  1 
ATOM   3120 C  CD1 . PHE A 1 390 ? 7.234   9.053   38.647  1.00 14.25  ? 390 PHE A CD1 1 
ATOM   3121 C  CD2 . PHE A 1 390 ? 8.752   8.727   36.834  1.00 14.38  ? 390 PHE A CD2 1 
ATOM   3122 C  CE1 . PHE A 1 390 ? 6.876   7.710   38.559  1.00 16.00  ? 390 PHE A CE1 1 
ATOM   3123 C  CE2 . PHE A 1 390 ? 8.399   7.391   36.750  1.00 14.31  ? 390 PHE A CE2 1 
ATOM   3124 C  CZ  . PHE A 1 390 ? 7.463   6.879   37.617  1.00 14.21  ? 390 PHE A CZ  1 
ATOM   3125 N  N   . LYS A 1 391 ? 10.809  10.161  40.557  1.00 13.95  ? 391 LYS A N   1 
ATOM   3126 C  CA  . LYS A 1 391 ? 12.129  9.621   40.893  1.00 16.65  ? 391 LYS A CA  1 
ATOM   3127 C  C   . LYS A 1 391 ? 12.046  8.269   41.594  1.00 14.95  ? 391 LYS A C   1 
ATOM   3128 O  O   . LYS A 1 391 ? 12.728  8.049   42.599  1.00 14.60  ? 391 LYS A O   1 
ATOM   3129 C  CB  . LYS A 1 391 ? 12.830  10.512  41.914  1.00 18.53  ? 391 LYS A CB  1 
ATOM   3130 C  CG  . LYS A 1 391 ? 12.885  11.986  41.577  1.00 21.48  ? 391 LYS A CG  1 
ATOM   3131 C  CD  . LYS A 1 391 ? 13.747  12.279  40.441  1.00 25.06  ? 391 LYS A CD  1 
ATOM   3132 C  CE  . LYS A 1 391 ? 15.214  12.218  40.800  1.00 25.92  ? 391 LYS A CE  1 
ATOM   3133 N  NZ  . LYS A 1 391 ? 15.992  12.406  39.556  1.00 25.65  ? 391 LYS A NZ  1 
ATOM   3134 N  N   . PRO A 1 392 ? 11.278  7.281   41.088  1.00 13.65  ? 392 PRO A N   1 
ATOM   3135 C  CA  . PRO A 1 392 ? 11.196  6.010   41.780  1.00 13.46  ? 392 PRO A CA  1 
ATOM   3136 C  C   . PRO A 1 392 ? 12.520  5.251   41.818  1.00 13.22  ? 392 PRO A C   1 
ATOM   3137 O  O   . PRO A 1 392 ? 12.602  4.306   42.589  1.00 14.10  ? 392 PRO A O   1 
ATOM   3138 C  CB  . PRO A 1 392 ? 10.170  5.219   40.961  1.00 14.44  ? 392 PRO A CB  1 
ATOM   3139 C  CG  . PRO A 1 392 ? 10.287  5.805   39.571  1.00 13.50  ? 392 PRO A CG  1 
ATOM   3140 C  CD  . PRO A 1 392 ? 10.570  7.268   39.812  1.00 13.21  ? 392 PRO A CD  1 
ATOM   3141 N  N   . PHE A 1 393 ? 13.470  5.632   40.948  1.00 12.69  ? 393 PHE A N   1 
ATOM   3142 C  CA  . PHE A 1 393 ? 14.732  4.924   40.762  1.00 13.26  ? 393 PHE A CA  1 
ATOM   3143 C  C   . PHE A 1 393 ? 15.914  5.753   41.255  1.00 15.42  ? 393 PHE A C   1 
ATOM   3144 O  O   . PHE A 1 393 ? 17.060  5.482   40.873  1.00 16.10  ? 393 PHE A O   1 
ATOM   3145 C  CB  . PHE A 1 393 ? 14.946  4.533   39.296  1.00 13.87  ? 393 PHE A CB  1 
ATOM   3146 C  CG  . PHE A 1 393 ? 14.002  3.453   38.836  1.00 12.87  ? 393 PHE A CG  1 
ATOM   3147 C  CD1 . PHE A 1 393 ? 14.133  2.172   39.323  1.00 13.90  ? 393 PHE A CD1 1 
ATOM   3148 C  CD2 . PHE A 1 393 ? 12.887  3.771   38.069  1.00 14.93  ? 393 PHE A CD2 1 
ATOM   3149 C  CE1 . PHE A 1 393 ? 13.217  1.193   38.970  1.00 13.87  ? 393 PHE A CE1 1 
ATOM   3150 C  CE2 . PHE A 1 393 ? 11.950  2.801   37.757  1.00 14.28  ? 393 PHE A CE2 1 
ATOM   3151 C  CZ  . PHE A 1 393 ? 12.140  1.516   38.181  1.00 15.27  ? 393 PHE A CZ  1 
ATOM   3152 N  N   . GLY A 1 394 ? 15.614  6.750   42.093  1.00 14.45  ? 394 GLY A N   1 
ATOM   3153 C  CA  . GLY A 1 394 ? 16.632  7.586   42.681  1.00 15.90  ? 394 GLY A CA  1 
ATOM   3154 C  C   . GLY A 1 394 ? 17.132  8.671   41.720  1.00 15.65  ? 394 GLY A C   1 
ATOM   3155 O  O   . GLY A 1 394 ? 16.376  9.187   40.894  1.00 15.07  ? 394 GLY A O   1 
ATOM   3156 N  N   . ASN A 1 395 ? 18.396  9.080   41.897  1.00 14.29  ? 395 ASN A N   1 
ATOM   3157 C  CA  . ASN A 1 395 ? 18.876  10.268  41.211  1.00 15.30  ? 395 ASN A CA  1 
ATOM   3158 C  C   . ASN A 1 395 ? 20.320  10.157  40.769  1.00 14.40  ? 395 ASN A C   1 
ATOM   3159 O  O   . ASN A 1 395 ? 21.177  9.729   41.540  1.00 13.76  ? 395 ASN A O   1 
ATOM   3160 C  CB  . ASN A 1 395 ? 18.782  11.490  42.128  1.00 17.09  ? 395 ASN A CB  1 
ATOM   3161 C  CG  . ASN A 1 395 ? 19.269  12.747  41.430  1.00 17.48  ? 395 ASN A CG  1 
ATOM   3162 O  OD1 . ASN A 1 395 ? 18.637  13.207  40.492  1.00 17.01  ? 395 ASN A OD1 1 
ATOM   3163 N  ND2 . ASN A 1 395 ? 20.413  13.266  41.838  1.00 17.80  ? 395 ASN A ND2 1 
ATOM   3164 N  N   . GLY A 1 396 ? 20.560  10.604  39.523  1.00 14.74  ? 396 GLY A N   1 
ATOM   3165 C  CA  . GLY A 1 396 ? 21.887  10.883  38.997  1.00 16.15  ? 396 GLY A CA  1 
ATOM   3166 C  C   . GLY A 1 396 ? 22.742  9.615   38.856  1.00 15.23  ? 396 GLY A C   1 
ATOM   3167 O  O   . GLY A 1 396 ? 22.259  8.553   38.484  1.00 15.36  ? 396 GLY A O   1 
ATOM   3168 N  N   . GLN A 1 397 ? 24.036  9.753   39.120  1.00 14.61  ? 397 GLN A N   1 
ATOM   3169 C  CA  . GLN A 1 397 ? 24.989  8.676   38.967  1.00 15.19  ? 397 GLN A CA  1 
ATOM   3170 C  C   . GLN A 1 397 ? 24.690  7.581   39.997  1.00 15.29  ? 397 GLN A C   1 
ATOM   3171 O  O   . GLN A 1 397 ? 25.160  6.462   39.811  1.00 16.33  ? 397 GLN A O   1 
ATOM   3172 C  CB  . GLN A 1 397 ? 26.429  9.209   39.070  1.00 16.04  ? 397 GLN A CB  1 
ATOM   3173 C  CG  . GLN A 1 397 ? 26.809  9.748   40.424  1.00 18.82  ? 397 GLN A CG  1 
ATOM   3174 C  CD  . GLN A 1 397 ? 28.266  10.180  40.434  1.00 20.14  ? 397 GLN A CD  1 
ATOM   3175 O  OE1 . GLN A 1 397 ? 29.068  9.783   39.602  1.00 21.69  ? 397 GLN A OE1 1 
ATOM   3176 N  NE2 . GLN A 1 397 ? 28.636  10.965  41.419  1.00 21.97  ? 397 GLN A NE2 1 
ATOM   3177 N  N   . ARG A 1 398 ? 23.939  7.890   41.069  1.00 13.53  ? 398 ARG A N   1 
ATOM   3178 C  CA  . ARG A 1 398 ? 23.553  6.899   42.083  1.00 13.98  ? 398 ARG A CA  1 
ATOM   3179 C  C   . ARG A 1 398 ? 22.121  6.397   41.894  1.00 13.01  ? 398 ARG A C   1 
ATOM   3180 O  O   . ARG A 1 398 ? 21.510  5.881   42.823  1.00 12.87  ? 398 ARG A O   1 
ATOM   3181 C  CB  . ARG A 1 398 ? 23.748  7.421   43.510  1.00 12.72  ? 398 ARG A CB  1 
ATOM   3182 C  CG  . ARG A 1 398 ? 25.188  7.822   43.809  1.00 13.45  ? 398 ARG A CG  1 
ATOM   3183 C  CD  . ARG A 1 398 ? 26.164  6.663   43.665  1.00 14.29  ? 398 ARG A CD  1 
ATOM   3184 N  NE  . ARG A 1 398 ? 25.857  5.463   44.426  1.00 13.73  ? 398 ARG A NE  1 
ATOM   3185 C  CZ  . ARG A 1 398 ? 26.369  5.173   45.615  1.00 15.86  ? 398 ARG A CZ  1 
ATOM   3186 N  NH1 . ARG A 1 398 ? 27.142  6.050   46.247  1.00 14.66  ? 398 ARG A NH1 1 
ATOM   3187 N  NH2 . ARG A 1 398 ? 26.077  4.027   46.202  1.00 17.21  ? 398 ARG A NH2 1 
ATOM   3188 N  N   . ALA A 1 399 ? 21.556  6.603   40.703  1.00 14.51  ? 399 ALA A N   1 
ATOM   3189 C  CA  . ALA A 1 399 ? 20.239  6.064   40.432  1.00 14.95  ? 399 ALA A CA  1 
ATOM   3190 C  C   . ALA A 1 399 ? 20.338  4.545   40.287  1.00 14.76  ? 399 ALA A C   1 
ATOM   3191 O  O   . ALA A 1 399 ? 21.416  3.964   40.104  1.00 13.64  ? 399 ALA A O   1 
ATOM   3192 C  CB  . ALA A 1 399 ? 19.681  6.735   39.192  1.00 17.05  ? 399 ALA A CB  1 
ATOM   3193 N  N   . CYS A 1 400 ? 19.173  3.903   40.354  1.00 14.23  ? 400 CYS A N   1 
ATOM   3194 C  CA  . CYS A 1 400 ? 19.096  2.465   40.194  1.00 13.70  ? 400 CYS A CA  1 
ATOM   3195 C  C   . CYS A 1 400 ? 19.829  1.988   38.940  1.00 13.41  ? 400 CYS A C   1 
ATOM   3196 O  O   . CYS A 1 400 ? 19.464  2.315   37.823  1.00 14.47  ? 400 CYS A O   1 
ATOM   3197 C  CB  . CYS A 1 400 ? 17.646  2.013   40.136  1.00 13.22  ? 400 CYS A CB  1 
ATOM   3198 S  SG  . CYS A 1 400 ? 17.492  0.216   40.293  1.00 15.40  ? 400 CYS A SG  1 
ATOM   3199 N  N   . ILE A 1 401 ? 20.813  1.103   39.107  1.00 13.60  ? 401 ILE A N   1 
ATOM   3200 C  CA  . ILE A 1 401 ? 21.440  0.496   37.941  1.00 13.49  ? 401 ILE A CA  1 
ATOM   3201 C  C   . ILE A 1 401 ? 20.550  -0.592  37.300  1.00 13.77  ? 401 ILE A C   1 
ATOM   3202 O  O   . ILE A 1 401 ? 20.730  -0.899  36.120  1.00 13.54  ? 401 ILE A O   1 
ATOM   3203 C  CB  . ILE A 1 401 ? 22.798  -0.087  38.354  1.00 14.50  ? 401 ILE A CB  1 
ATOM   3204 C  CG1 . ILE A 1 401 ? 23.683  -0.281  37.145  1.00 14.08  ? 401 ILE A CG1 1 
ATOM   3205 C  CG2 . ILE A 1 401 ? 22.600  -1.382  39.145  1.00 14.98  ? 401 ILE A CG2 1 
ATOM   3206 C  CD1 . ILE A 1 401 ? 24.940  -0.987  37.510  1.00 16.24  ? 401 ILE A CD1 1 
ATOM   3207 N  N   . GLY A 1 402 ? 19.620  -1.159  38.082  1.00 13.64  ? 402 GLY A N   1 
ATOM   3208 C  CA  . GLY A 1 402 ? 18.749  -2.233  37.640  1.00 13.77  ? 402 GLY A CA  1 
ATOM   3209 C  C   . GLY A 1 402 ? 17.412  -1.758  37.050  1.00 13.76  ? 402 GLY A C   1 
ATOM   3210 O  O   . GLY A 1 402 ? 16.527  -2.583  36.878  1.00 13.58  ? 402 GLY A O   1 
ATOM   3211 N  N   . GLN A 1 403 ? 17.245  -0.463  36.754  1.00 13.73  ? 403 GLN A N   1 
ATOM   3212 C  CA  . GLN A 1 403 ? 15.960  0.091   36.356  1.00 14.83  ? 403 GLN A CA  1 
ATOM   3213 C  C   . GLN A 1 403 ? 15.418  -0.601  35.096  1.00 14.78  ? 403 GLN A C   1 
ATOM   3214 O  O   . GLN A 1 403 ? 14.242  -0.978  35.012  1.00 13.68  ? 403 GLN A O   1 
ATOM   3215 C  CB  . GLN A 1 403 ? 16.093  1.595   36.081  1.00 15.34  ? 403 GLN A CB  1 
ATOM   3216 C  CG  . GLN A 1 403 ? 14.802  2.150   35.514  1.00 17.18  ? 403 GLN A CG  1 
ATOM   3217 C  CD  . GLN A 1 403 ? 14.833  3.644   35.309  1.00 19.10  ? 403 GLN A CD  1 
ATOM   3218 O  OE1 . GLN A 1 403 ? 15.748  4.346   35.768  1.00 17.22  ? 403 GLN A OE1 1 
ATOM   3219 N  NE2 . GLN A 1 403 ? 13.787  4.120   34.650  1.00 20.63  ? 403 GLN A NE2 1 
ATOM   3220 N  N   . GLN A 1 404 ? 16.246  -0.686  34.059  1.00 14.85  ? 404 GLN A N   1 
ATOM   3221 C  CA  . GLN A 1 404 ? 15.805  -1.324  32.821  1.00 19.60  ? 404 GLN A CA  1 
ATOM   3222 C  C   . GLN A 1 404 ? 15.425  -2.794  33.049  1.00 17.09  ? 404 GLN A C   1 
ATOM   3223 O  O   . GLN A 1 404 ? 14.443  -3.249  32.483  1.00 15.96  ? 404 GLN A O   1 
ATOM   3224 C  CB  . GLN A 1 404 ? 16.850  -1.252  31.707  1.00 23.31  ? 404 GLN A CB  1 
ATOM   3225 C  CG  . GLN A 1 404 ? 16.799  0.041   30.911  1.00 30.43  ? 404 GLN A CG  1 
ATOM   3226 C  CD  . GLN A 1 404 ? 17.185  1.203   31.785  1.00 38.46  ? 404 GLN A CD  1 
ATOM   3227 O  OE1 . GLN A 1 404 ? 18.296  1.254   32.310  1.00 45.40  ? 404 GLN A OE1 1 
ATOM   3228 N  NE2 . GLN A 1 404 ? 16.259  2.132   31.982  1.00 44.25  ? 404 GLN A NE2 1 
ATOM   3229 N  N   . PHE A 1 405 ? 16.243  -3.527  33.823  1.00 16.30  ? 405 PHE A N   1 
ATOM   3230 C  CA  . PHE A 1 405 ? 16.010  -4.928  34.144  1.00 16.63  ? 405 PHE A CA  1 
ATOM   3231 C  C   . PHE A 1 405 ? 14.657  -5.059  34.856  1.00 16.11  ? 405 PHE A C   1 
ATOM   3232 O  O   . PHE A 1 405 ? 13.825  -5.864  34.439  1.00 15.77  ? 405 PHE A O   1 
ATOM   3233 C  CB  . PHE A 1 405 ? 17.218  -5.443  34.945  1.00 17.30  ? 405 PHE A CB  1 
ATOM   3234 C  CG  . PHE A 1 405 ? 17.207  -6.902  35.285  1.00 14.14  ? 405 PHE A CG  1 
ATOM   3235 C  CD1 . PHE A 1 405 ? 16.359  -7.410  36.259  1.00 14.75  ? 405 PHE A CD1 1 
ATOM   3236 C  CD2 . PHE A 1 405 ? 17.988  -7.781  34.553  1.00 16.02  ? 405 PHE A CD2 1 
ATOM   3237 C  CE1 . PHE A 1 405 ? 16.328  -8.774  36.535  1.00 14.51  ? 405 PHE A CE1 1 
ATOM   3238 C  CE2 . PHE A 1 405 ? 17.909  -9.144  34.797  1.00 13.95  ? 405 PHE A CE2 1 
ATOM   3239 C  CZ  . PHE A 1 405 ? 17.118  -9.627  35.816  1.00 14.35  ? 405 PHE A CZ  1 
ATOM   3240 N  N   . ALA A 1 406 ? 14.428  -4.247  35.903  1.00 15.12  ? 406 ALA A N   1 
ATOM   3241 C  CA  . ALA A 1 406 ? 13.185  -4.255  36.668  1.00 15.66  ? 406 ALA A CA  1 
ATOM   3242 C  C   . ALA A 1 406 ? 11.974  -4.058  35.753  1.00 14.36  ? 406 ALA A C   1 
ATOM   3243 O  O   . ALA A 1 406 ? 11.004  -4.819  35.823  1.00 14.96  ? 406 ALA A O   1 
ATOM   3244 C  CB  . ALA A 1 406 ? 13.191  -3.165  37.697  1.00 16.66  ? 406 ALA A CB  1 
ATOM   3245 N  N   . LEU A 1 407 ? 12.025  -3.054  34.884  1.00 14.01  ? 407 LEU A N   1 
ATOM   3246 C  CA  . LEU A 1 407 ? 10.854  -2.731  34.076  1.00 16.01  ? 407 LEU A CA  1 
ATOM   3247 C  C   . LEU A 1 407 ? 10.662  -3.770  32.961  1.00 14.46  ? 407 LEU A C   1 
ATOM   3248 O  O   . LEU A 1 407 ? 9.535   -4.055  32.561  1.00 13.56  ? 407 LEU A O   1 
ATOM   3249 C  CB  . LEU A 1 407 ? 10.985  -1.327  33.482  1.00 16.24  ? 407 LEU A CB  1 
ATOM   3250 C  CG  . LEU A 1 407 ? 10.973  -0.182  34.495  1.00 15.45  ? 407 LEU A CG  1 
ATOM   3251 C  CD1 . LEU A 1 407 ? 11.203  1.121   33.778  1.00 14.43  ? 407 LEU A CD1 1 
ATOM   3252 C  CD2 . LEU A 1 407 ? 9.695   -0.172  35.323  1.00 16.06  ? 407 LEU A CD2 1 
ATOM   3253 N  N   . HIS A 1 408 ? 11.752  -4.350  32.446  1.00 15.98  ? 408 HIS A N   1 
ATOM   3254 C  CA  . HIS A 1 408 ? 11.591  -5.365  31.402  1.00 17.73  ? 408 HIS A CA  1 
ATOM   3255 C  C   . HIS A 1 408 ? 10.873  -6.574  31.976  1.00 17.13  ? 408 HIS A C   1 
ATOM   3256 O  O   . HIS A 1 408 ? 9.895   -7.049  31.397  1.00 15.42  ? 408 HIS A O   1 
ATOM   3257 C  CB  . HIS A 1 408 ? 12.904  -5.790  30.758  1.00 18.35  ? 408 HIS A CB  1 
ATOM   3258 C  CG  . HIS A 1 408 ? 12.687  -6.552  29.500  1.00 18.98  ? 408 HIS A CG  1 
ATOM   3259 N  ND1 . HIS A 1 408 ? 12.393  -5.952  28.301  1.00 20.80  ? 408 HIS A ND1 1 
ATOM   3260 C  CD2 . HIS A 1 408 ? 12.780  -7.862  29.244  1.00 19.47  ? 408 HIS A CD2 1 
ATOM   3261 C  CE1 . HIS A 1 408 ? 12.269  -6.896  27.373  1.00 20.83  ? 408 HIS A CE1 1 
ATOM   3262 N  NE2 . HIS A 1 408 ? 12.560  -8.048  27.919  1.00 18.46  ? 408 HIS A NE2 1 
ATOM   3263 N  N   . GLU A 1 409 ? 11.378  -7.044  33.120  1.00 17.91  ? 409 GLU A N   1 
ATOM   3264 C  CA  . GLU A 1 409 ? 10.806  -8.183  33.831  1.00 15.79  ? 409 GLU A CA  1 
ATOM   3265 C  C   . GLU A 1 409 ? 9.344   -7.916  34.142  1.00 16.17  ? 409 GLU A C   1 
ATOM   3266 O  O   . GLU A 1 409 ? 8.514   -8.798  33.933  1.00 13.92  ? 409 GLU A O   1 
ATOM   3267 C  CB  . GLU A 1 409 ? 11.527  -8.428  35.153  1.00 16.85  ? 409 GLU A CB  1 
ATOM   3268 C  CG  . GLU A 1 409 ? 11.000  -9.622  35.936  1.00 18.57  ? 409 GLU A CG  1 
ATOM   3269 C  CD  . GLU A 1 409 ? 11.736  -9.882  37.250  1.00 20.91  ? 409 GLU A CD  1 
ATOM   3270 O  OE1 . GLU A 1 409 ? 12.723  -9.127  37.559  1.00 20.39  ? 409 GLU A OE1 1 
ATOM   3271 O  OE2 . GLU A 1 409 ? 11.367  -10.876 37.939  1.00 23.38  ? 409 GLU A OE2 1 
ATOM   3272 N  N   . ALA A 1 410 ? 9.049   -6.701  34.650  1.00 14.01  ? 410 ALA A N   1 
ATOM   3273 C  CA  . ALA A 1 410 ? 7.721   -6.421  35.159  1.00 12.49  ? 410 ALA A CA  1 
ATOM   3274 C  C   . ALA A 1 410 ? 6.729   -6.292  34.005  1.00 13.14  ? 410 ALA A C   1 
ATOM   3275 O  O   . ALA A 1 410 ? 5.541   -6.630  34.147  1.00 12.43  ? 410 ALA A O   1 
ATOM   3276 C  CB  . ALA A 1 410 ? 7.714   -5.188  36.055  1.00 12.69  ? 410 ALA A CB  1 
ATOM   3277 N  N   . THR A 1 411 ? 7.210   -5.731  32.887  1.00 13.82  ? 411 THR A N   1 
ATOM   3278 C  CA  . THR A 1 411 ? 6.382   -5.499  31.718  1.00 13.62  ? 411 THR A CA  1 
ATOM   3279 C  C   . THR A 1 411 ? 6.082   -6.853  31.085  1.00 14.44  ? 411 THR A C   1 
ATOM   3280 O  O   . THR A 1 411 ? 4.923   -7.136  30.761  1.00 12.75  ? 411 THR A O   1 
ATOM   3281 C  CB  . THR A 1 411 ? 7.032   -4.532  30.718  1.00 14.60  ? 411 THR A CB  1 
ATOM   3282 O  OG1 . THR A 1 411 ? 7.287   -3.288  31.367  1.00 14.11  ? 411 THR A OG1 1 
ATOM   3283 C  CG2 . THR A 1 411 ? 6.169   -4.246  29.513  1.00 14.66  ? 411 THR A CG2 1 
ATOM   3284 N  N   . LEU A 1 412 ? 7.132   -7.672  30.915  1.00 14.89  ? 412 LEU A N   1 
ATOM   3285 C  CA  . LEU A 1 412 ? 6.965   -9.040  30.428  1.00 15.94  ? 412 LEU A CA  1 
ATOM   3286 C  C   . LEU A 1 412 ? 5.961   -9.826  31.260  1.00 16.48  ? 412 LEU A C   1 
ATOM   3287 O  O   . LEU A 1 412 ? 5.045   -10.474 30.716  1.00 15.76  ? 412 LEU A O   1 
ATOM   3288 C  CB  . LEU A 1 412 ? 8.307   -9.767  30.432  1.00 17.37  ? 412 LEU A CB  1 
ATOM   3289 C  CG  . LEU A 1 412 ? 8.216   -11.274 30.188  1.00 19.16  ? 412 LEU A CG  1 
ATOM   3290 C  CD1 . LEU A 1 412 ? 7.754   -11.546 28.783  1.00 19.36  ? 412 LEU A CD1 1 
ATOM   3291 C  CD2 . LEU A 1 412 ? 9.557   -11.939 30.429  1.00 22.58  ? 412 LEU A CD2 1 
ATOM   3292 N  N   . VAL A 1 413 ? 6.102   -9.749  32.585  1.00 14.48  ? 413 VAL A N   1 
ATOM   3293 C  CA  . VAL A 1 413 ? 5.301   -10.611 33.433  1.00 15.53  ? 413 VAL A CA  1 
ATOM   3294 C  C   . VAL A 1 413 ? 3.848   -10.138 33.511  1.00 15.43  ? 413 VAL A C   1 
ATOM   3295 O  O   . VAL A 1 413 ? 2.912   -10.940 33.403  1.00 14.73  ? 413 VAL A O   1 
ATOM   3296 C  CB  . VAL A 1 413 ? 5.973   -10.743 34.806  1.00 16.54  ? 413 VAL A CB  1 
ATOM   3297 C  CG1 . VAL A 1 413 ? 5.027   -11.299 35.840  1.00 18.13  ? 413 VAL A CG1 1 
ATOM   3298 C  CG2 . VAL A 1 413 ? 7.253   -11.575 34.666  1.00 15.85  ? 413 VAL A CG2 1 
ATOM   3299 N  N   . LEU A 1 414 ? 3.642   -8.828  33.686  1.00 15.77  ? 414 LEU A N   1 
ATOM   3300 C  CA  . LEU A 1 414 ? 2.290   -8.293  33.763  1.00 15.50  ? 414 LEU A CA  1 
ATOM   3301 C  C   . LEU A 1 414 ? 1.598   -8.483  32.409  1.00 15.32  ? 414 LEU A C   1 
ATOM   3302 O  O   . LEU A 1 414 ? 0.404   -8.768  32.365  1.00 15.35  ? 414 LEU A O   1 
ATOM   3303 C  CB  . LEU A 1 414 ? 2.349   -6.831  34.191  1.00 15.93  ? 414 LEU A CB  1 
ATOM   3304 C  CG  . LEU A 1 414 ? 1.011   -6.143  34.429  1.00 15.01  ? 414 LEU A CG  1 
ATOM   3305 C  CD1 . LEU A 1 414 ? 0.127   -6.897  35.411  1.00 14.87  ? 414 LEU A CD1 1 
ATOM   3306 C  CD2 . LEU A 1 414 ? 1.271   -4.724  34.933  1.00 14.35  ? 414 LEU A CD2 1 
ATOM   3307 N  N   . GLY A 1 415 ? 2.331   -8.324  31.306  1.00 14.93  ? 415 GLY A N   1 
ATOM   3308 C  CA  . GLY A 1 415 ? 1.770   -8.587  29.984  1.00 16.97  ? 415 GLY A CA  1 
ATOM   3309 C  C   . GLY A 1 415 ? 1.210   -10.010 29.856  1.00 16.66  ? 415 GLY A C   1 
ATOM   3310 O  O   . GLY A 1 415 ? 0.056   -10.215 29.476  1.00 16.27  ? 415 GLY A O   1 
ATOM   3311 N  N   . MET A 1 416 ? 2.008   -10.998 30.255  1.00 17.05  ? 416 MET A N   1 
ATOM   3312 C  CA  . MET A 1 416 ? 1.619   -12.403 30.141  1.00 16.77  ? 416 MET A CA  1 
ATOM   3313 C  C   . MET A 1 416 ? 0.443   -12.694 31.059  1.00 15.26  ? 416 MET A C   1 
ATOM   3314 O  O   . MET A 1 416 ? -0.502  -13.383 30.669  1.00 13.91  ? 416 MET A O   1 
ATOM   3315 C  CB  . MET A 1 416 ? 2.812   -13.314 30.478  1.00 18.34  ? 416 MET A CB  1 
ATOM   3316 C  CG  . MET A 1 416 ? 3.905   -13.234 29.461  1.00 20.15  ? 416 MET A CG  1 
ATOM   3317 S  SD  . MET A 1 416 ? 5.315   -14.382 29.792  1.00 26.26  ? 416 MET A SD  1 
ATOM   3318 C  CE  . MET A 1 416 ? 4.547   -15.970 29.471  1.00 26.76  ? 416 MET A CE  1 
ATOM   3319 N  N   . MET A 1 417 ? 0.456   -12.093 32.263  1.00 15.01  ? 417 MET A N   1 
ATOM   3320 C  CA  . MET A 1 417 ? -0.597  -12.271 33.240  1.00 14.89  ? 417 MET A CA  1 
ATOM   3321 C  C   . MET A 1 417 ? -1.926  -11.756 32.673  1.00 15.14  ? 417 MET A C   1 
ATOM   3322 O  O   . MET A 1 417 ? -2.965  -12.375 32.856  1.00 12.88  ? 417 MET A O   1 
ATOM   3323 C  CB  . MET A 1 417 ? -0.313  -11.491 34.521  1.00 16.52  ? 417 MET A CB  1 
ATOM   3324 C  CG  . MET A 1 417 ? 0.663   -12.154 35.475  1.00 18.16  ? 417 MET A CG  1 
ATOM   3325 S  SD  . MET A 1 417 ? 1.292   -11.030 36.771  1.00 20.30  ? 417 MET A SD  1 
ATOM   3326 C  CE  . MET A 1 417 ? -0.237  -10.250 37.292  1.00 24.07  ? 417 MET A CE  1 
ATOM   3327 N  N   . LEU A 1 418 ? -1.887  -10.586 32.029  1.00 15.51  ? 418 LEU A N   1 
ATOM   3328 C  CA  . LEU A 1 418 ? -3.080  -10.011 31.434  1.00 15.76  ? 418 LEU A CA  1 
ATOM   3329 C  C   . LEU A 1 418 ? -3.489  -10.755 30.161  1.00 15.75  ? 418 LEU A C   1 
ATOM   3330 O  O   . LEU A 1 418 ? -4.682  -10.802 29.833  1.00 17.26  ? 418 LEU A O   1 
ATOM   3331 C  CB  . LEU A 1 418 ? -2.774  -8.542  31.109  1.00 17.80  ? 418 LEU A CB  1 
ATOM   3332 C  CG  . LEU A 1 418 ? -2.543  -7.658  32.328  1.00 19.84  ? 418 LEU A CG  1 
ATOM   3333 C  CD1 . LEU A 1 418 ? -2.198  -6.254  31.883  1.00 22.02  ? 418 LEU A CD1 1 
ATOM   3334 C  CD2 . LEU A 1 418 ? -3.773  -7.657  33.217  1.00 20.96  ? 418 LEU A CD2 1 
ATOM   3335 N  N   . LYS A 1 419 ? -2.527  -11.304 29.406  1.00 14.35  ? 419 LYS A N   1 
ATOM   3336 C  CA  . LYS A 1 419 ? -2.878  -12.130 28.247  1.00 16.84  ? 419 LYS A CA  1 
ATOM   3337 C  C   . LYS A 1 419 ? -3.633  -13.405 28.669  1.00 17.08  ? 419 LYS A C   1 
ATOM   3338 O  O   . LYS A 1 419 ? -4.637  -13.791 28.060  1.00 16.85  ? 419 LYS A O   1 
ATOM   3339 C  CB  . LYS A 1 419 ? -1.615  -12.480 27.470  1.00 17.43  ? 419 LYS A CB  1 
ATOM   3340 C  CG  . LYS A 1 419 ? -1.817  -13.398 26.284  1.00 18.56  ? 419 LYS A CG  1 
ATOM   3341 C  CD  . LYS A 1 419 ? -0.534  -13.845 25.649  1.00 20.85  ? 419 LYS A CD  1 
ATOM   3342 C  CE  . LYS A 1 419 ? -0.775  -14.839 24.531  1.00 22.67  ? 419 LYS A CE  1 
ATOM   3343 N  NZ  . LYS A 1 419 ? 0.444   -15.040 23.719  1.00 23.36  ? 419 LYS A NZ  1 
ATOM   3344 N  N   . HIS A 1 420 ? -3.198  -14.047 29.748  1.00 14.93  ? 420 HIS A N   1 
ATOM   3345 C  CA  . HIS A 1 420 ? -3.649  -15.398 30.075  1.00 14.01  ? 420 HIS A CA  1 
ATOM   3346 C  C   . HIS A 1 420 ? -4.847  -15.492 31.021  1.00 12.92  ? 420 HIS A C   1 
ATOM   3347 O  O   . HIS A 1 420 ? -5.500  -16.531 31.046  1.00 13.68  ? 420 HIS A O   1 
ATOM   3348 C  CB  . HIS A 1 420 ? -2.459  -16.225 30.593  1.00 14.24  ? 420 HIS A CB  1 
ATOM   3349 C  CG  . HIS A 1 420 ? -1.545  -16.556 29.492  1.00 14.81  ? 420 HIS A CG  1 
ATOM   3350 N  ND1 . HIS A 1 420 ? -1.913  -17.557 28.628  1.00 15.95  ? 420 HIS A ND1 1 
ATOM   3351 C  CD2 . HIS A 1 420 ? -0.394  -16.058 29.028  1.00 15.36  ? 420 HIS A CD2 1 
ATOM   3352 C  CE1 . HIS A 1 420 ? -0.962  -17.694 27.707  1.00 15.95  ? 420 HIS A CE1 1 
ATOM   3353 N  NE2 . HIS A 1 420 ? -0.034  -16.796 27.927  1.00 16.61  ? 420 HIS A NE2 1 
ATOM   3354 N  N   . PHE A 1 421 ? -5.126  -14.476 31.847  1.00 13.61  ? 421 PHE A N   1 
ATOM   3355 C  CA  . PHE A 1 421 ? -6.135  -14.581 32.875  1.00 14.75  ? 421 PHE A CA  1 
ATOM   3356 C  C   . PHE A 1 421 ? -7.013  -13.328 32.983  1.00 16.54  ? 421 PHE A C   1 
ATOM   3357 O  O   . PHE A 1 421 ? -6.549  -12.197 32.814  1.00 14.67  ? 421 PHE A O   1 
ATOM   3358 C  CB  . PHE A 1 421 ? -5.504  -14.772 34.254  1.00 16.37  ? 421 PHE A CB  1 
ATOM   3359 C  CG  . PHE A 1 421 ? -4.631  -15.996 34.372  1.00 14.88  ? 421 PHE A CG  1 
ATOM   3360 C  CD1 . PHE A 1 421 ? -5.170  -17.225 34.726  1.00 15.56  ? 421 PHE A CD1 1 
ATOM   3361 C  CD2 . PHE A 1 421 ? -3.271  -15.896 34.136  1.00 16.18  ? 421 PHE A CD2 1 
ATOM   3362 C  CE1 . PHE A 1 421 ? -4.372  -18.360 34.792  1.00 17.01  ? 421 PHE A CE1 1 
ATOM   3363 C  CE2 . PHE A 1 421 ? -2.466  -17.027 34.175  1.00 15.61  ? 421 PHE A CE2 1 
ATOM   3364 C  CZ  . PHE A 1 421 ? -3.020  -18.248 34.527  1.00 16.53  ? 421 PHE A CZ  1 
ATOM   3365 N  N   . ASP A 1 422 ? -8.256  -13.561 33.403  1.00 16.24  ? 422 ASP A N   1 
ATOM   3366 C  CA  . ASP A 1 422 ? -9.105  -12.532 34.000  1.00 19.33  ? 422 ASP A CA  1 
ATOM   3367 C  C   . ASP A 1 422 ? -8.909  -12.587 35.512  1.00 21.36  ? 422 ASP A C   1 
ATOM   3368 O  O   . ASP A 1 422 ? -8.787  -13.670 36.131  1.00 21.18  ? 422 ASP A O   1 
ATOM   3369 C  CB  . ASP A 1 422 ? -10.586 -12.751 33.663  1.00 21.49  ? 422 ASP A CB  1 
ATOM   3370 C  CG  . ASP A 1 422 ? -10.962 -12.589 32.193  1.00 27.54  ? 422 ASP A CG  1 
ATOM   3371 O  OD1 . ASP A 1 422 ? -10.542 -11.597 31.568  1.00 31.40  ? 422 ASP A OD1 1 
ATOM   3372 O  OD2 . ASP A 1 422 ? -11.705 -13.431 31.683  1.00 32.42  ? 422 ASP A OD2 1 
ATOM   3373 N  N   . PHE A 1 423 ? -8.903  -11.401 36.116  1.00 20.35  ? 423 PHE A N   1 
ATOM   3374 C  CA  . PHE A 1 423 ? -8.658  -11.242 37.539  1.00 20.05  ? 423 PHE A CA  1 
ATOM   3375 C  C   . PHE A 1 423 ? -9.901  -10.746 38.250  1.00 21.60  ? 423 PHE A C   1 
ATOM   3376 O  O   . PHE A 1 423 ? -10.606 -9.890  37.730  1.00 26.35  ? 423 PHE A O   1 
ATOM   3377 C  CB  . PHE A 1 423 ? -7.484  -10.281 37.752  1.00 21.27  ? 423 PHE A CB  1 
ATOM   3378 C  CG  . PHE A 1 423 ? -6.185  -10.907 37.327  1.00 19.73  ? 423 PHE A CG  1 
ATOM   3379 C  CD1 . PHE A 1 423 ? -5.538  -11.814 38.153  1.00 19.32  ? 423 PHE A CD1 1 
ATOM   3380 C  CD2 . PHE A 1 423 ? -5.692  -10.692 36.049  1.00 17.94  ? 423 PHE A CD2 1 
ATOM   3381 C  CE1 . PHE A 1 423 ? -4.381  -12.461 37.727  1.00 19.76  ? 423 PHE A CE1 1 
ATOM   3382 C  CE2 . PHE A 1 423 ? -4.496  -11.287 35.656  1.00 19.32  ? 423 PHE A CE2 1 
ATOM   3383 C  CZ  . PHE A 1 423 ? -3.859  -12.197 36.481  1.00 18.14  ? 423 PHE A CZ  1 
ATOM   3384 N  N   . GLU A 1 424 ? -10.128 -11.272 39.452  1.00 22.00  ? 424 GLU A N   1 
ATOM   3385 C  CA  . GLU A 1 424 ? -11.216 -10.843 40.307  1.00 24.43  ? 424 GLU A CA  1 
ATOM   3386 C  C   . GLU A 1 424 ? -10.690 -10.552 41.720  1.00 22.93  ? 424 GLU A C   1 
ATOM   3387 O  O   . GLU A 1 424 ? -10.049 -11.402 42.351  1.00 21.31  ? 424 GLU A O   1 
ATOM   3388 C  CB  . GLU A 1 424 ? -12.298 -11.924 40.315  1.00 25.29  ? 424 GLU A CB  1 
ATOM   3389 C  CG  . GLU A 1 424 ? -13.590 -11.481 40.948  1.00 29.58  ? 424 GLU A CG  1 
ATOM   3390 C  CD  . GLU A 1 424 ? -14.442 -12.644 41.448  1.00 31.71  ? 424 GLU A CD  1 
ATOM   3391 O  OE1 . GLU A 1 424 ? -14.176 -13.792 41.034  1.00 33.72  ? 424 GLU A OE1 1 
ATOM   3392 O  OE2 . GLU A 1 424 ? -15.346 -12.402 42.282  1.00 31.17  ? 424 GLU A OE2 1 
ATOM   3393 N  N   . ASP A 1 425 ? -11.001 -9.332  42.188  1.00 18.17  ? 425 ASP A N   1 
ATOM   3394 C  CA  . ASP A 1 425 ? -10.843 -8.901  43.569  1.00 17.91  ? 425 ASP A CA  1 
ATOM   3395 C  C   . ASP A 1 425 ? -11.976 -9.464  44.428  1.00 18.75  ? 425 ASP A C   1 
ATOM   3396 O  O   . ASP A 1 425 ? -12.909 -8.736  44.836  1.00 19.46  ? 425 ASP A O   1 
ATOM   3397 C  CB  . ASP A 1 425 ? -10.769 -7.362  43.573  1.00 18.12  ? 425 ASP A CB  1 
ATOM   3398 C  CG  . ASP A 1 425 ? -10.685 -6.736  44.944  1.00 17.95  ? 425 ASP A CG  1 
ATOM   3399 O  OD1 . ASP A 1 425 ? -10.158 -7.376  45.860  1.00 17.38  ? 425 ASP A OD1 1 
ATOM   3400 O  OD2 . ASP A 1 425 ? -11.116 -5.571  45.059  1.00 22.56  ? 425 ASP A OD2 1 
ATOM   3401 N  N   . HIS A 1 426 ? -11.857 -10.764 44.745  1.00 18.90  ? 426 HIS A N   1 
ATOM   3402 C  CA  . HIS A 1 426 ? -12.968 -11.545 45.273  1.00 22.10  ? 426 HIS A CA  1 
ATOM   3403 C  C   . HIS A 1 426 ? -13.243 -11.189 46.733  1.00 20.29  ? 426 HIS A C   1 
ATOM   3404 O  O   . HIS A 1 426 ? -14.367 -11.339 47.190  1.00 20.98  ? 426 HIS A O   1 
ATOM   3405 C  CB  . HIS A 1 426 ? -12.774 -13.039 44.978  1.00 22.07  ? 426 HIS A CB  1 
ATOM   3406 C  CG  . HIS A 1 426 ? -11.651 -13.637 45.737  1.00 22.37  ? 426 HIS A CG  1 
ATOM   3407 N  ND1 . HIS A 1 426 ? -10.334 -13.324 45.471  1.00 20.99  ? 426 HIS A ND1 1 
ATOM   3408 C  CD2 . HIS A 1 426 ? -11.646 -14.413 46.819  1.00 23.24  ? 426 HIS A CD2 1 
ATOM   3409 C  CE1 . HIS A 1 426 ? -9.559  -13.924 46.357  1.00 21.53  ? 426 HIS A CE1 1 
ATOM   3410 N  NE2 . HIS A 1 426 ? -10.333 -14.613 47.177  1.00 23.57  ? 426 HIS A NE2 1 
ATOM   3411 N  N   . THR A 1 427 ? -12.257 -10.639 47.435  1.00 20.00  ? 427 THR A N   1 
ATOM   3412 C  CA  . THR A 1 427 ? -12.413 -10.309 48.846  1.00 20.62  ? 427 THR A CA  1 
ATOM   3413 C  C   . THR A 1 427 ? -12.658 -8.828  49.084  1.00 20.88  ? 427 THR A C   1 
ATOM   3414 O  O   . THR A 1 427 ? -12.788 -8.433  50.244  1.00 23.03  ? 427 THR A O   1 
ATOM   3415 C  CB  . THR A 1 427 ? -11.167 -10.617 49.691  1.00 21.91  ? 427 THR A CB  1 
ATOM   3416 O  OG1 . THR A 1 427 ? -10.087 -9.721  49.352  1.00 21.03  ? 427 THR A OG1 1 
ATOM   3417 C  CG2 . THR A 1 427 ? -10.757 -12.074 49.588  1.00 21.06  ? 427 THR A CG2 1 
ATOM   3418 N  N   . ASN A 1 428 ? -12.701 -8.055  47.997  1.00 20.51  ? 428 ASN A N   1 
ATOM   3419 C  CA  . ASN A 1 428 ? -12.695 -6.601  48.019  1.00 21.56  ? 428 ASN A CA  1 
ATOM   3420 C  C   . ASN A 1 428 ? -11.572 -6.081  48.929  1.00 19.49  ? 428 ASN A C   1 
ATOM   3421 O  O   . ASN A 1 428 ? -11.780 -5.371  49.898  1.00 16.84  ? 428 ASN A O   1 
ATOM   3422 C  CB  . ASN A 1 428 ? -14.072 -6.037  48.383  1.00 24.32  ? 428 ASN A CB  1 
ATOM   3423 C  CG  . ASN A 1 428 ? -14.014 -4.547  48.631  1.00 26.14  ? 428 ASN A CG  1 
ATOM   3424 O  OD1 . ASN A 1 428 ? -13.659 -3.780  47.743  1.00 25.05  ? 428 ASN A OD1 1 
ATOM   3425 N  ND2 . ASN A 1 428 ? -14.238 -4.149  49.871  1.00 30.96  ? 428 ASN A ND2 1 
ATOM   3426 N  N   . TYR A 1 429 ? -10.343 -6.397  48.574  1.00 17.99  ? 429 TYR A N   1 
ATOM   3427 C  CA  . TYR A 1 429 ? -9.209  -6.183  49.453  1.00 16.69  ? 429 TYR A CA  1 
ATOM   3428 C  C   . TYR A 1 429 ? -9.000  -4.715  49.849  1.00 16.44  ? 429 TYR A C   1 
ATOM   3429 O  O   . TYR A 1 429 ? -9.010  -3.820  49.029  1.00 20.73  ? 429 TYR A O   1 
ATOM   3430 C  CB  . TYR A 1 429 ? -8.006  -6.737  48.699  1.00 16.09  ? 429 TYR A CB  1 
ATOM   3431 C  CG  . TYR A 1 429 ? -6.663  -6.401  49.329  1.00 15.63  ? 429 TYR A CG  1 
ATOM   3432 C  CD1 . TYR A 1 429 ? -6.226  -6.994  50.513  1.00 16.14  ? 429 TYR A CD1 1 
ATOM   3433 C  CD2 . TYR A 1 429 ? -5.794  -5.557  48.673  1.00 15.36  ? 429 TYR A CD2 1 
ATOM   3434 C  CE1 . TYR A 1 429 ? -4.972  -6.729  51.038  1.00 16.30  ? 429 TYR A CE1 1 
ATOM   3435 C  CE2 . TYR A 1 429 ? -4.568  -5.231  49.218  1.00 15.45  ? 429 TYR A CE2 1 
ATOM   3436 C  CZ  . TYR A 1 429 ? -4.158  -5.805  50.404  1.00 15.96  ? 429 TYR A CZ  1 
ATOM   3437 O  OH  . TYR A 1 429 ? -2.923  -5.436  50.853  1.00 15.82  ? 429 TYR A OH  1 
ATOM   3438 N  N   . GLU A 1 430 ? -8.762  -4.481  51.147  1.00 19.44  ? 430 GLU A N   1 
ATOM   3439 C  CA  . GLU A 1 430 ? -8.389  -3.165  51.659  1.00 21.89  ? 430 GLU A CA  1 
ATOM   3440 C  C   . GLU A 1 430 ? -6.866  -3.054  51.695  1.00 21.73  ? 430 GLU A C   1 
ATOM   3441 O  O   . GLU A 1 430 ? -6.196  -3.815  52.377  1.00 21.19  ? 430 GLU A O   1 
ATOM   3442 C  CB  . GLU A 1 430 ? -9.015  -3.009  53.037  1.00 25.99  ? 430 GLU A CB  1 
ATOM   3443 C  CG  . GLU A 1 430 ? -8.599  -1.794  53.822  1.00 32.25  ? 430 GLU A CG  1 
ATOM   3444 C  CD  . GLU A 1 430 ? -9.177  -1.892  55.221  1.00 39.49  ? 430 GLU A CD  1 
ATOM   3445 O  OE1 . GLU A 1 430 ? -10.413 -1.674  55.360  1.00 41.72  ? 430 GLU A OE1 1 
ATOM   3446 O  OE2 . GLU A 1 430 ? -8.423  -2.319  56.144  1.00 38.88  ? 430 GLU A OE2 1 
ATOM   3447 N  N   . LEU A 1 431 ? -6.310  -2.111  50.933  1.00 21.59  ? 431 LEU A N   1 
ATOM   3448 C  CA  . LEU A 1 431 ? -4.856  -2.047  50.811  1.00 21.84  ? 431 LEU A CA  1 
ATOM   3449 C  C   . LEU A 1 431 ? -4.208  -2.001  52.204  1.00 20.63  ? 431 LEU A C   1 
ATOM   3450 O  O   . LEU A 1 431 ? -4.596  -1.214  53.060  1.00 20.78  ? 431 LEU A O   1 
ATOM   3451 C  CB  . LEU A 1 431 ? -4.484  -0.839  49.953  1.00 22.63  ? 431 LEU A CB  1 
ATOM   3452 C  CG  . LEU A 1 431 ? -2.980  -0.613  49.770  1.00 24.27  ? 431 LEU A CG  1 
ATOM   3453 C  CD1 . LEU A 1 431 ? -2.310  -1.790  49.047  1.00 23.83  ? 431 LEU A CD1 1 
ATOM   3454 C  CD2 . LEU A 1 431 ? -2.739  0.682   49.029  1.00 24.09  ? 431 LEU A CD2 1 
ATOM   3455 N  N   . ASP A 1 432 ? -3.248  -2.907  52.423  1.00 21.85  ? 432 ASP A N   1 
ATOM   3456 C  CA  . ASP A 1 432 ? -2.470  -2.972  53.651  1.00 22.64  ? 432 ASP A CA  1 
ATOM   3457 C  C   . ASP A 1 432 ? -0.991  -3.039  53.270  1.00 20.04  ? 432 ASP A C   1 
ATOM   3458 O  O   . ASP A 1 432 ? -0.551  -4.019  52.676  1.00 20.60  ? 432 ASP A O   1 
ATOM   3459 C  CB  . ASP A 1 432 ? -2.967  -4.138  54.504  1.00 24.35  ? 432 ASP A CB  1 
ATOM   3460 C  CG  . ASP A 1 432 ? -2.314  -4.245  55.869  1.00 29.67  ? 432 ASP A CG  1 
ATOM   3461 O  OD1 . ASP A 1 432 ? -1.531  -3.335  56.209  1.00 29.68  ? 432 ASP A OD1 1 
ATOM   3462 O  OD2 . ASP A 1 432 ? -2.530  -5.285  56.545  1.00 31.92  ? 432 ASP A OD2 1 
ATOM   3463 N  N   . ILE A 1 433 ? -0.230  -1.965  53.558  1.00 18.37  ? 433 ILE A N   1 
ATOM   3464 C  CA  . ILE A 1 433 ? 1.108   -1.849  53.012  1.00 19.05  ? 433 ILE A CA  1 
ATOM   3465 C  C   . ILE A 1 433 ? 2.095   -2.238  54.111  1.00 19.27  ? 433 ILE A C   1 
ATOM   3466 O  O   . ILE A 1 433 ? 2.219   -1.549  55.109  1.00 17.16  ? 433 ILE A O   1 
ATOM   3467 C  CB  . ILE A 1 433 ? 1.377   -0.443  52.428  1.00 19.61  ? 433 ILE A CB  1 
ATOM   3468 C  CG1 . ILE A 1 433 ? 0.412   -0.112  51.285  1.00 20.47  ? 433 ILE A CG1 1 
ATOM   3469 C  CG2 . ILE A 1 433 ? 2.820   -0.310  51.963  1.00 18.96  ? 433 ILE A CG2 1 
ATOM   3470 C  CD1 . ILE A 1 433 ? 0.637   1.247   50.681  1.00 20.21  ? 433 ILE A CD1 1 
ATOM   3471 N  N   . LYS A 1 434 ? 2.767   -3.360  53.907  1.00 19.00  ? 434 LYS A N   1 
ATOM   3472 C  CA  . LYS A 1 434 ? 3.811   -3.822  54.801  1.00 23.24  ? 434 LYS A CA  1 
ATOM   3473 C  C   . LYS A 1 434 ? 5.097   -3.087  54.446  1.00 19.97  ? 434 LYS A C   1 
ATOM   3474 O  O   . LYS A 1 434 ? 5.422   -2.960  53.272  1.00 17.94  ? 434 LYS A O   1 
ATOM   3475 C  CB  . LYS A 1 434 ? 3.956   -5.344  54.650  1.00 26.51  ? 434 LYS A CB  1 
ATOM   3476 C  CG  . LYS A 1 434 ? 4.874   -6.066  55.636  1.00 30.95  ? 434 LYS A CG  1 
ATOM   3477 C  CD  . LYS A 1 434 ? 5.383   -7.387  55.081  1.00 35.01  ? 434 LYS A CD  1 
ATOM   3478 C  CE  . LYS A 1 434 ? 6.490   -7.167  54.056  1.00 41.47  ? 434 LYS A CE  1 
ATOM   3479 N  NZ  . LYS A 1 434 ? 6.267   -7.876  52.771  1.00 40.55  ? 434 LYS A NZ  1 
ATOM   3480 N  N   . GLU A 1 435 ? 5.851   -2.626  55.449  1.00 19.94  ? 435 GLU A N   1 
ATOM   3481 C  CA  . GLU A 1 435 ? 7.110   -1.944  55.174  1.00 20.52  ? 435 GLU A CA  1 
ATOM   3482 C  C   . GLU A 1 435 ? 8.262   -2.737  55.761  1.00 21.05  ? 435 GLU A C   1 
ATOM   3483 O  O   . GLU A 1 435 ? 8.204   -3.210  56.880  1.00 20.99  ? 435 GLU A O   1 
ATOM   3484 C  CB  . GLU A 1 435 ? 7.193   -0.549  55.770  1.00 21.11  ? 435 GLU A CB  1 
ATOM   3485 C  CG  . GLU A 1 435 ? 5.973   0.276   55.495  1.00 22.82  ? 435 GLU A CG  1 
ATOM   3486 C  CD  . GLU A 1 435 ? 6.124   1.739   55.841  1.00 25.04  ? 435 GLU A CD  1 
ATOM   3487 O  OE1 . GLU A 1 435 ? 7.257   2.134   56.195  1.00 25.81  ? 435 GLU A OE1 1 
ATOM   3488 O  OE2 . GLU A 1 435 ? 5.100   2.468   55.745  1.00 23.24  ? 435 GLU A OE2 1 
ATOM   3489 N  N   . THR A 1 436 ? 9.311   -2.883  54.976  1.00 23.60  ? 436 THR A N   1 
ATOM   3490 C  CA  . THR A 1 436 ? 10.563  -3.387  55.494  1.00 26.17  ? 436 THR A CA  1 
ATOM   3491 C  C   . THR A 1 436 ? 11.481  -2.193  55.310  1.00 28.01  ? 436 THR A C   1 
ATOM   3492 O  O   . THR A 1 436 ? 11.220  -1.141  55.868  1.00 35.81  ? 436 THR A O   1 
ATOM   3493 C  CB  . THR A 1 436 ? 10.896  -4.733  54.831  1.00 29.39  ? 436 THR A CB  1 
ATOM   3494 O  OG1 . THR A 1 436 ? 10.888  -4.603  53.404  1.00 32.55  ? 436 THR A OG1 1 
ATOM   3495 C  CG2 . THR A 1 436 ? 9.914   -5.827  55.207  1.00 29.49  ? 436 THR A CG2 1 
ATOM   3496 N  N   . LEU A 1 437 ? 12.466  -2.285  54.439  1.00 31.66  ? 437 LEU A N   1 
ATOM   3497 C  CA  . LEU A 1 437 ? 13.018  -1.061  53.877  1.00 30.80  ? 437 LEU A CA  1 
ATOM   3498 C  C   . LEU A 1 437 ? 12.209  -0.689  52.635  1.00 27.84  ? 437 LEU A C   1 
ATOM   3499 O  O   . LEU A 1 437 ? 12.220  0.458   52.184  1.00 32.77  ? 437 LEU A O   1 
ATOM   3500 C  CB  . LEU A 1 437 ? 14.492  -1.284  53.543  1.00 33.11  ? 437 LEU A CB  1 
ATOM   3501 C  CG  . LEU A 1 437 ? 15.379  -1.674  54.726  1.00 36.13  ? 437 LEU A CG  1 
ATOM   3502 C  CD1 . LEU A 1 437 ? 16.835  -1.396  54.392  1.00 36.91  ? 437 LEU A CD1 1 
ATOM   3503 C  CD2 . LEU A 1 437 ? 14.974  -0.949  56.000  1.00 36.17  ? 437 LEU A CD2 1 
ATOM   3504 N  N   . THR A 1 438 ? 11.502  -1.681  52.099  1.00 21.53  ? 438 THR A N   1 
ATOM   3505 C  CA  . THR A 1 438 ? 10.761  -1.532  50.865  1.00 22.30  ? 438 THR A CA  1 
ATOM   3506 C  C   . THR A 1 438 ? 9.272   -1.626  51.178  1.00 20.82  ? 438 THR A C   1 
ATOM   3507 O  O   . THR A 1 438 ? 8.890   -1.969  52.298  1.00 20.77  ? 438 THR A O   1 
ATOM   3508 C  CB  . THR A 1 438 ? 11.252  -2.565  49.857  1.00 22.99  ? 438 THR A CB  1 
ATOM   3509 O  OG1 . THR A 1 438 ? 11.030  -3.816  50.491  1.00 27.20  ? 438 THR A OG1 1 
ATOM   3510 C  CG2 . THR A 1 438 ? 12.713  -2.426  49.497  1.00 22.61  ? 438 THR A CG2 1 
ATOM   3511 N  N   . LEU A 1 439 ? 8.433   -1.346  50.177  1.00 20.59  ? 439 LEU A N   1 
ATOM   3512 C  CA  . LEU A 1 439 ? 6.989   -1.379  50.380  1.00 19.10  ? 439 LEU A CA  1 
ATOM   3513 C  C   . LEU A 1 439 ? 6.351   -2.533  49.612  1.00 18.00  ? 439 LEU A C   1 
ATOM   3514 O  O   . LEU A 1 439 ? 6.712   -2.799  48.464  1.00 15.90  ? 439 LEU A O   1 
ATOM   3515 C  CB  . LEU A 1 439 ? 6.392   -0.053  49.894  1.00 19.05  ? 439 LEU A CB  1 
ATOM   3516 C  CG  . LEU A 1 439 ? 6.874   1.203   50.624  1.00 19.65  ? 439 LEU A CG  1 
ATOM   3517 C  CD1 . LEU A 1 439 ? 6.142   2.444   50.129  1.00 18.78  ? 439 LEU A CD1 1 
ATOM   3518 C  CD2 . LEU A 1 439 ? 6.667   1.018   52.123  1.00 20.15  ? 439 LEU A CD2 1 
ATOM   3519 N  N   . LYS A 1 440 ? 5.314   -3.138  50.197  1.00 18.01  ? 440 LYS A N   1 
ATOM   3520 C  CA  . LYS A 1 440 ? 4.563   -4.151  49.477  1.00 20.51  ? 440 LYS A CA  1 
ATOM   3521 C  C   . LYS A 1 440 ? 3.165   -4.341  50.067  1.00 18.05  ? 440 LYS A C   1 
ATOM   3522 O  O   . LYS A 1 440 ? 2.965   -4.319  51.274  1.00 18.25  ? 440 LYS A O   1 
ATOM   3523 C  CB  . LYS A 1 440 ? 5.343   -5.472  49.481  1.00 24.29  ? 440 LYS A CB  1 
ATOM   3524 C  CG  . LYS A 1 440 ? 4.987   -6.435  48.366  1.00 27.06  ? 440 LYS A CG  1 
ATOM   3525 C  CD  . LYS A 1 440 ? 6.060   -7.441  48.069  1.00 33.28  ? 440 LYS A CD  1 
ATOM   3526 C  CE  . LYS A 1 440 ? 6.478   -8.231  49.282  1.00 37.95  ? 440 LYS A CE  1 
ATOM   3527 N  NZ  . LYS A 1 440 ? 7.270   -9.421  48.893  1.00 41.59  ? 440 LYS A NZ  1 
ATOM   3528 N  N   . PRO A 1 441 ? 2.135   -4.633  49.253  1.00 17.50  ? 441 PRO A N   1 
ATOM   3529 C  CA  . PRO A 1 441 ? 0.840   -5.011  49.813  1.00 18.53  ? 441 PRO A CA  1 
ATOM   3530 C  C   . PRO A 1 441 ? 1.011   -6.271  50.658  1.00 22.45  ? 441 PRO A C   1 
ATOM   3531 O  O   . PRO A 1 441 ? 1.876   -7.120  50.368  1.00 25.43  ? 441 PRO A O   1 
ATOM   3532 C  CB  . PRO A 1 441 ? -0.073  -5.241  48.614  1.00 18.66  ? 441 PRO A CB  1 
ATOM   3533 C  CG  . PRO A 1 441 ? 0.686   -4.791  47.406  1.00 17.62  ? 441 PRO A CG  1 
ATOM   3534 C  CD  . PRO A 1 441 ? 2.153   -4.650  47.791  1.00 17.93  ? 441 PRO A CD  1 
ATOM   3535 N  N   . GLU A 1 442 ? 0.296   -6.334  51.784  1.00 20.24  ? 442 GLU A N   1 
ATOM   3536 C  CA  . GLU A 1 442 ? 0.259   -7.549  52.559  1.00 20.53  ? 442 GLU A CA  1 
ATOM   3537 C  C   . GLU A 1 442 ? -1.169  -8.075  52.527  1.00 18.77  ? 442 GLU A C   1 
ATOM   3538 O  O   . GLU A 1 442 ? -2.106  -7.302  52.668  1.00 17.84  ? 442 GLU A O   1 
ATOM   3539 C  CB  . GLU A 1 442 ? 0.662   -7.302  54.005  1.00 24.13  ? 442 GLU A CB  1 
ATOM   3540 C  CG  . GLU A 1 442 ? 0.845   -8.608  54.750  1.00 27.65  ? 442 GLU A CG  1 
ATOM   3541 C  CD  . GLU A 1 442 ? 1.412   -8.484  56.148  1.00 32.32  ? 442 GLU A CD  1 
ATOM   3542 O  OE1 . GLU A 1 442 ? 1.889   -9.540  56.670  1.00 37.70  ? 442 GLU A OE1 1 
ATOM   3543 O  OE2 . GLU A 1 442 ? 1.378   -7.347  56.705  1.00 28.81  ? 442 GLU A OE2 1 
ATOM   3544 N  N   . GLY A 1 443 ? -1.303  -9.382  52.315  1.00 17.69  ? 443 GLY A N   1 
ATOM   3545 C  CA  . GLY A 1 443 ? -2.596  -10.051 52.346  1.00 16.79  ? 443 GLY A CA  1 
ATOM   3546 C  C   . GLY A 1 443 ? -3.393  -9.879  51.056  1.00 17.30  ? 443 GLY A C   1 
ATOM   3547 O  O   . GLY A 1 443 ? -4.586  -10.143 51.049  1.00 20.07  ? 443 GLY A O   1 
ATOM   3548 N  N   . PHE A 1 444 ? -2.760  -9.358  49.993  1.00 16.92  ? 444 PHE A N   1 
ATOM   3549 C  CA  . PHE A 1 444 ? -3.433  -9.156  48.728  1.00 15.51  ? 444 PHE A CA  1 
ATOM   3550 C  C   . PHE A 1 444 ? -3.640  -10.516 48.062  1.00 15.85  ? 444 PHE A C   1 
ATOM   3551 O  O   . PHE A 1 444 ? -2.663  -11.267 47.838  1.00 16.62  ? 444 PHE A O   1 
ATOM   3552 C  CB  . PHE A 1 444 ? -2.668  -8.148  47.878  1.00 14.60  ? 444 PHE A CB  1 
ATOM   3553 C  CG  . PHE A 1 444 ? -3.269  -7.859  46.531  1.00 13.03  ? 444 PHE A CG  1 
ATOM   3554 C  CD1 . PHE A 1 444 ? -4.638  -7.848  46.326  1.00 12.91  ? 444 PHE A CD1 1 
ATOM   3555 C  CD2 . PHE A 1 444 ? -2.450  -7.571  45.478  1.00 14.57  ? 444 PHE A CD2 1 
ATOM   3556 C  CE1 . PHE A 1 444 ? -5.161  -7.629  45.062  1.00 13.99  ? 444 PHE A CE1 1 
ATOM   3557 C  CE2 . PHE A 1 444 ? -2.979  -7.371  44.213  1.00 14.34  ? 444 PHE A CE2 1 
ATOM   3558 C  CZ  . PHE A 1 444 ? -4.330  -7.422  44.000  1.00 13.56  ? 444 PHE A CZ  1 
ATOM   3559 N  N   . VAL A 1 445 ? -4.937  -10.817 47.799  1.00 16.55  ? 445 VAL A N   1 
ATOM   3560 C  CA  . VAL A 1 445 ? -5.345  -12.049 47.146  1.00 16.82  ? 445 VAL A CA  1 
ATOM   3561 C  C   . VAL A 1 445 ? -6.290  -11.739 45.989  1.00 17.11  ? 445 VAL A C   1 
ATOM   3562 O  O   . VAL A 1 445 ? -7.078  -10.795 46.096  1.00 17.64  ? 445 VAL A O   1 
ATOM   3563 C  CB  . VAL A 1 445 ? -5.979  -13.038 48.158  1.00 17.63  ? 445 VAL A CB  1 
ATOM   3564 C  CG1 . VAL A 1 445 ? -4.993  -13.449 49.243  1.00 17.84  ? 445 VAL A CG1 1 
ATOM   3565 C  CG2 . VAL A 1 445 ? -7.257  -12.531 48.797  1.00 19.61  ? 445 VAL A CG2 1 
ATOM   3566 N  N   . VAL A 1 446 ? -6.184  -12.507 44.900  1.00 16.22  ? 446 VAL A N   1 
ATOM   3567 C  CA  . VAL A 1 446 ? -7.126  -12.420 43.787  1.00 18.14  ? 446 VAL A CA  1 
ATOM   3568 C  C   . VAL A 1 446 ? -7.480  -13.819 43.289  1.00 18.57  ? 446 VAL A C   1 
ATOM   3569 O  O   . VAL A 1 446 ? -6.762  -14.777 43.516  1.00 18.75  ? 446 VAL A O   1 
ATOM   3570 C  CB  . VAL A 1 446 ? -6.599  -11.618 42.584  1.00 16.70  ? 446 VAL A CB  1 
ATOM   3571 C  CG1 . VAL A 1 446 ? -6.161  -10.220 42.962  1.00 18.05  ? 446 VAL A CG1 1 
ATOM   3572 C  CG2 . VAL A 1 446 ? -5.494  -12.353 41.824  1.00 16.43  ? 446 VAL A CG2 1 
ATOM   3573 N  N   . LYS A 1 447 ? -8.561  -13.899 42.517  1.00 20.74  ? 447 LYS A N   1 
ATOM   3574 C  CA  . LYS A 1 447 ? -8.874  -15.092 41.735  1.00 20.50  ? 447 LYS A CA  1 
ATOM   3575 C  C   . LYS A 1 447 ? -8.504  -14.859 40.284  1.00 18.04  ? 447 LYS A C   1 
ATOM   3576 O  O   . LYS A 1 447 ? -8.850  -13.843 39.717  1.00 20.37  ? 447 LYS A O   1 
ATOM   3577 C  CB  . LYS A 1 447 ? -10.358 -15.453 41.916  1.00 21.52  ? 447 LYS A CB  1 
ATOM   3578 C  CG  . LYS A 1 447 ? -10.648 -15.999 43.309  1.00 23.41  ? 447 LYS A CG  1 
ATOM   3579 C  CD  . LYS A 1 447 ? -12.104 -16.245 43.624  1.00 27.82  ? 447 LYS A CD  1 
ATOM   3580 C  CE  . LYS A 1 447 ? -12.435 -17.681 43.966  1.00 33.63  ? 447 LYS A CE  1 
ATOM   3581 N  NZ  . LYS A 1 447 ? -13.807 -17.799 44.521  1.00 34.14  ? 447 LYS A NZ  1 
ATOM   3582 N  N   . ALA A 1 448 ? -7.847  -15.831 39.660  1.00 20.40  ? 448 ALA A N   1 
ATOM   3583 C  CA  . ALA A 1 448 ? -7.488  -15.730 38.254  1.00 21.47  ? 448 ALA A CA  1 
ATOM   3584 C  C   . ALA A 1 448 ? -8.251  -16.770 37.441  1.00 25.59  ? 448 ALA A C   1 
ATOM   3585 O  O   . ALA A 1 448 ? -8.046  -17.954 37.632  1.00 26.14  ? 448 ALA A O   1 
ATOM   3586 C  CB  . ALA A 1 448 ? -6.004  -15.896 38.094  1.00 24.82  ? 448 ALA A CB  1 
ATOM   3587 N  N   . LYS A 1 449 ? -9.116  -16.325 36.521  1.00 25.43  ? 449 LYS A N   1 
ATOM   3588 C  CA  . LYS A 1 449 ? -9.801  -17.232 35.625  1.00 24.38  ? 449 LYS A CA  1 
ATOM   3589 C  C   . LYS A 1 449 ? -9.034  -17.271 34.315  1.00 22.77  ? 449 LYS A C   1 
ATOM   3590 O  O   . LYS A 1 449 ? -8.848  -16.234 33.670  1.00 20.31  ? 449 LYS A O   1 
ATOM   3591 C  CB  . LYS A 1 449 ? -11.256 -16.789 35.431  1.00 28.21  ? 449 LYS A CB  1 
ATOM   3592 C  CG  . LYS A 1 449 ? -11.948 -17.429 34.236  1.00 34.33  ? 449 LYS A CG  1 
ATOM   3593 C  CD  . LYS A 1 449 ? -13.459 -17.290 34.253  1.00 37.02  ? 449 LYS A CD  1 
ATOM   3594 C  CE  . LYS A 1 449 ? -14.114 -18.296 35.170  1.00 39.08  ? 449 LYS A CE  1 
ATOM   3595 N  NZ  . LYS A 1 449 ? -15.469 -17.837 35.552  1.00 41.36  ? 449 LYS A NZ  1 
ATOM   3596 N  N   . SER A 1 450 ? -8.549  -18.465 33.969  1.00 19.40  ? 450 SER A N   1 
ATOM   3597 C  CA  . SER A 1 450 ? -7.832  -18.697 32.732  1.00 18.94  ? 450 SER A CA  1 
ATOM   3598 C  C   . SER A 1 450 ? -8.676  -18.307 31.527  1.00 20.82  ? 450 SER A C   1 
ATOM   3599 O  O   . SER A 1 450 ? -9.861  -18.653 31.464  1.00 19.08  ? 450 SER A O   1 
ATOM   3600 C  CB  . SER A 1 450 ? -7.402  -20.143 32.633  1.00 18.18  ? 450 SER A CB  1 
ATOM   3601 O  OG  . SER A 1 450 ? -6.770  -20.369 31.391  1.00 19.00  ? 450 SER A OG  1 
ATOM   3602 N  N   . LYS A 1 451 ? -8.048  -17.620 30.574  1.00 20.51  ? 451 LYS A N   1 
ATOM   3603 C  CA  . LYS A 1 451 ? -8.611  -17.441 29.245  1.00 26.01  ? 451 LYS A CA  1 
ATOM   3604 C  C   . LYS A 1 451 ? -8.276  -18.636 28.336  1.00 28.15  ? 451 LYS A C   1 
ATOM   3605 O  O   . LYS A 1 451 ? -8.564  -18.612 27.137  1.00 25.39  ? 451 LYS A O   1 
ATOM   3606 C  CB  . LYS A 1 451 ? -8.059  -16.157 28.625  1.00 25.29  ? 451 LYS A CB  1 
ATOM   3607 C  CG  . LYS A 1 451 ? -8.401  -14.884 29.393  1.00 27.81  ? 451 LYS A CG  1 
ATOM   3608 C  CD  . LYS A 1 451 ? -7.802  -13.629 28.773  1.00 29.54  ? 451 LYS A CD  1 
ATOM   3609 C  CE  . LYS A 1 451 ? -8.473  -12.373 29.268  1.00 32.11  ? 451 LYS A CE  1 
ATOM   3610 N  NZ  . LYS A 1 451 ? -7.497  -11.282 29.459  1.00 39.07  ? 451 LYS A NZ  1 
ATOM   3611 N  N   . GLN A 1 452 ? -7.642  -19.670 28.893  1.00 29.83  ? 452 GLN A N   1 
ATOM   3612 C  CA  . GLN A 1 452 ? -7.311  -20.873 28.149  1.00 33.32  ? 452 GLN A CA  1 
ATOM   3613 C  C   . GLN A 1 452 ? -6.632  -20.545 26.825  1.00 31.32  ? 452 GLN A C   1 
ATOM   3614 O  O   . GLN A 1 452 ? -7.064  -21.043 25.796  1.00 32.00  ? 452 GLN A O   1 
ATOM   3615 C  CB  . GLN A 1 452 ? -8.580  -21.675 27.840  1.00 39.03  ? 452 GLN A CB  1 
ATOM   3616 C  CG  . GLN A 1 452 ? -9.178  -22.358 29.050  1.00 40.92  ? 452 GLN A CG  1 
ATOM   3617 C  CD  . GLN A 1 452 ? -10.426 -23.120 28.676  1.00 46.96  ? 452 GLN A CD  1 
ATOM   3618 O  OE1 . GLN A 1 452 ? -10.970 -22.983 27.578  1.00 50.85  ? 452 GLN A OE1 1 
ATOM   3619 N  NE2 . GLN A 1 452 ? -10.905 -23.928 29.605  1.00 47.19  ? 452 GLN A NE2 1 
ATOM   3620 N  N   . ILE A 1 453 ? -5.593  -19.707 26.855  1.00 28.93  ? 453 ILE A N   1 
ATOM   3621 C  CA  . ILE A 1 453 ? -4.761  -19.440 25.690  1.00 30.70  ? 453 ILE A CA  1 
ATOM   3622 C  C   . ILE A 1 453 ? -3.464  -20.227 25.858  1.00 29.92  ? 453 ILE A C   1 
ATOM   3623 O  O   . ILE A 1 453 ? -2.842  -20.150 26.910  1.00 23.54  ? 453 ILE A O   1 
ATOM   3624 C  CB  . ILE A 1 453 ? -4.507  -17.931 25.553  1.00 31.11  ? 453 ILE A CB  1 
ATOM   3625 C  CG1 . ILE A 1 453 ? -5.788  -17.189 25.173  1.00 34.07  ? 453 ILE A CG1 1 
ATOM   3626 C  CG2 . ILE A 1 453 ? -3.390  -17.638 24.573  1.00 34.68  ? 453 ILE A CG2 1 
ATOM   3627 C  CD1 . ILE A 1 453 ? -5.696  -15.700 25.381  1.00 34.04  ? 453 ILE A CD1 1 
ATOM   3628 N  N   . PRO A 1 454 ? -3.035  -21.048 24.873  1.00 36.64  ? 454 PRO A N   1 
ATOM   3629 C  CA  . PRO A 1 454 ? -1.905  -21.947 25.090  1.00 35.12  ? 454 PRO A CA  1 
ATOM   3630 C  C   . PRO A 1 454 ? -0.601  -21.181 25.250  1.00 29.90  ? 454 PRO A C   1 
ATOM   3631 O  O   . PRO A 1 454 ? -0.421  -20.104 24.688  1.00 27.24  ? 454 PRO A O   1 
ATOM   3632 C  CB  . PRO A 1 454 ? -1.853  -22.855 23.849  1.00 41.59  ? 454 PRO A CB  1 
ATOM   3633 C  CG  . PRO A 1 454 ? -3.152  -22.575 23.094  1.00 42.36  ? 454 PRO A CG  1 
ATOM   3634 C  CD  . PRO A 1 454 ? -3.599  -21.185 23.516  1.00 42.59  ? 454 PRO A CD  1 
ATOM   3635 N  N   . LEU A 1 455 ? 0.305   -21.774 26.021  1.00 28.98  ? 455 LEU A N   1 
ATOM   3636 C  CA  . LEU A 1 455 ? 1.540   -21.124 26.426  1.00 32.12  ? 455 LEU A CA  1 
ATOM   3637 C  C   . LEU A 1 455 ? 2.714   -21.869 25.775  1.00 33.56  ? 455 LEU A C   1 
ATOM   3638 O  O   . LEU A 1 455 ? 2.649   -23.106 25.808  1.00 29.88  ? 455 LEU A O   1 
ATOM   3639 C  CB  . LEU A 1 455 ? 1.546   -21.192 27.956  1.00 32.51  ? 455 LEU A CB  1 
ATOM   3640 C  CG  . LEU A 1 455 ? 2.742   -20.606 28.688  1.00 34.36  ? 455 LEU A CG  1 
ATOM   3641 C  CD1 . LEU A 1 455 ? 2.749   -19.080 28.599  1.00 34.21  ? 455 LEU A CD1 1 
ATOM   3642 C  CD2 . LEU A 1 455 ? 2.694   -21.060 30.133  1.00 33.86  ? 455 LEU A CD2 1 
ATOM   3643 N  N   . LYS B 1 3   ? -7.146  -9.679  2.611   1.00 63.13  ? 3   LYS B N   1 
ATOM   3644 C  CA  . LYS B 1 3   ? -8.384  -9.191  1.944   1.00 59.62  ? 3   LYS B CA  1 
ATOM   3645 C  C   . LYS B 1 3   ? -8.056  -7.979  1.068   1.00 63.14  ? 3   LYS B C   1 
ATOM   3646 O  O   . LYS B 1 3   ? -7.187  -7.173  1.414   1.00 62.64  ? 3   LYS B O   1 
ATOM   3647 C  CB  . LYS B 1 3   ? -9.453  -8.874  2.993   1.00 60.13  ? 3   LYS B CB  1 
ATOM   3648 C  CG  . LYS B 1 3   ? -10.701 -8.191  2.447   1.00 67.99  ? 3   LYS B CG  1 
ATOM   3649 C  CD  . LYS B 1 3   ? -11.954 -8.448  3.256   1.00 70.41  ? 3   LYS B CD  1 
ATOM   3650 C  CE  . LYS B 1 3   ? -11.769 -8.200  4.737   1.00 73.78  ? 3   LYS B CE  1 
ATOM   3651 N  NZ  . LYS B 1 3   ? -13.071 -8.011  5.420   1.00 74.51  ? 3   LYS B NZ  1 
ATOM   3652 N  N   . GLU B 1 4   ? -8.751  -7.877  -0.078  1.00 60.48  ? 4   GLU B N   1 
ATOM   3653 C  CA  . GLU B 1 4   ? -8.581  -6.763  -0.999  1.00 55.83  ? 4   GLU B CA  1 
ATOM   3654 C  C   . GLU B 1 4   ? -9.413  -5.575  -0.518  1.00 46.70  ? 4   GLU B C   1 
ATOM   3655 O  O   . GLU B 1 4   ? -10.487 -5.738  0.061   1.00 38.66  ? 4   GLU B O   1 
ATOM   3656 C  CB  . GLU B 1 4   ? -8.971  -7.137  -2.431  1.00 59.73  ? 4   GLU B CB  1 
ATOM   3657 C  CG  . GLU B 1 4   ? -8.661  -6.031  -3.431  1.00 65.76  ? 4   GLU B CG  1 
ATOM   3658 C  CD  . GLU B 1 4   ? -8.653  -6.436  -4.896  1.00 71.43  ? 4   GLU B CD  1 
ATOM   3659 O  OE1 . GLU B 1 4   ? -9.242  -7.488  -5.226  1.00 76.39  ? 4   GLU B OE1 1 
ATOM   3660 O  OE2 . GLU B 1 4   ? -8.035  -5.705  -5.702  1.00 73.41  ? 4   GLU B OE2 1 
ATOM   3661 N  N   . MET B 1 5   ? -8.904  -4.370  -0.780  1.00 38.03  ? 5   MET B N   1 
ATOM   3662 C  CA  . MET B 1 5   ? -9.428  -3.184  -0.136  1.00 32.16  ? 5   MET B CA  1 
ATOM   3663 C  C   . MET B 1 5   ? -10.538 -2.581  -0.984  1.00 26.38  ? 5   MET B C   1 
ATOM   3664 O  O   . MET B 1 5   ? -10.359 -2.418  -2.178  1.00 28.17  ? 5   MET B O   1 
ATOM   3665 C  CB  . MET B 1 5   ? -8.312  -2.156  0.076   1.00 33.54  ? 5   MET B CB  1 
ATOM   3666 C  CG  . MET B 1 5   ? -8.503  -1.368  1.339   1.00 34.81  ? 5   MET B CG  1 
ATOM   3667 S  SD  . MET B 1 5   ? -7.004  -0.598  1.948   1.00 38.13  ? 5   MET B SD  1 
ATOM   3668 C  CE  . MET B 1 5   ? -6.663  0.509   0.604   1.00 36.99  ? 5   MET B CE  1 
ATOM   3669 N  N   . PRO B 1 6   ? -11.686 -2.181  -0.385  1.00 22.43  ? 6   PRO B N   1 
ATOM   3670 C  CA  . PRO B 1 6   ? -12.660 -1.343  -1.073  1.00 23.10  ? 6   PRO B CA  1 
ATOM   3671 C  C   . PRO B 1 6   ? -12.019 -0.045  -1.541  1.00 22.30  ? 6   PRO B C   1 
ATOM   3672 O  O   . PRO B 1 6   ? -11.018 0.407   -0.983  1.00 23.44  ? 6   PRO B O   1 
ATOM   3673 C  CB  . PRO B 1 6   ? -13.756 -1.063  -0.037  1.00 23.41  ? 6   PRO B CB  1 
ATOM   3674 C  CG  . PRO B 1 6   ? -13.563 -2.127  1.025   1.00 23.14  ? 6   PRO B CG  1 
ATOM   3675 C  CD  . PRO B 1 6   ? -12.110 -2.514  0.977   1.00 21.79  ? 6   PRO B CD  1 
ATOM   3676 N  N   . GLN B 1 7   ? -12.568 0.491   -2.625  1.00 19.60  ? 7   GLN B N   1 
ATOM   3677 C  CA  . GLN B 1 7   ? -12.107 1.711   -3.238  1.00 20.64  ? 7   GLN B CA  1 
ATOM   3678 C  C   . GLN B 1 7   ? -13.307 2.425   -3.834  1.00 19.83  ? 7   GLN B C   1 
ATOM   3679 O  O   . GLN B 1 7   ? -14.136 1.778   -4.489  1.00 20.05  ? 7   GLN B O   1 
ATOM   3680 C  CB  . GLN B 1 7   ? -11.096 1.415   -4.331  1.00 22.64  ? 7   GLN B CB  1 
ATOM   3681 C  CG  . GLN B 1 7   ? -10.519 2.691   -4.885  1.00 23.08  ? 7   GLN B CG  1 
ATOM   3682 C  CD  . GLN B 1 7   ? -9.497  2.452   -5.957  1.00 26.33  ? 7   GLN B CD  1 
ATOM   3683 O  OE1 . GLN B 1 7   ? -9.275  1.323   -6.379  1.00 29.13  ? 7   GLN B OE1 1 
ATOM   3684 N  NE2 . GLN B 1 7   ? -8.882  3.531   -6.412  1.00 26.36  ? 7   GLN B NE2 1 
ATOM   3685 N  N   . PRO B 1 8   ? -13.459 3.752   -3.612  1.00 18.58  ? 8   PRO B N   1 
ATOM   3686 C  CA  . PRO B 1 8   ? -14.542 4.511   -4.225  1.00 17.59  ? 8   PRO B CA  1 
ATOM   3687 C  C   . PRO B 1 8   ? -14.344 4.735   -5.723  1.00 16.88  ? 8   PRO B C   1 
ATOM   3688 O  O   . PRO B 1 8   ? -13.321 4.403   -6.308  1.00 18.21  ? 8   PRO B O   1 
ATOM   3689 C  CB  . PRO B 1 8   ? -14.533 5.819   -3.417  1.00 18.17  ? 8   PRO B CB  1 
ATOM   3690 C  CG  . PRO B 1 8   ? -13.100 5.983   -2.953  1.00 18.23  ? 8   PRO B CG  1 
ATOM   3691 C  CD  . PRO B 1 8   ? -12.563 4.594   -2.797  1.00 18.14  ? 8   PRO B CD  1 
ATOM   3692 N  N   . LYS B 1 9   ? -15.360 5.318   -6.353  1.00 19.53  ? 9   LYS B N   1 
ATOM   3693 C  CA  . LYS B 1 9   ? -15.440 5.378   -7.799  1.00 18.56  ? 9   LYS B CA  1 
ATOM   3694 C  C   . LYS B 1 9   ? -14.270 6.169   -8.353  1.00 19.93  ? 9   LYS B C   1 
ATOM   3695 O  O   . LYS B 1 9   ? -13.799 7.097   -7.699  1.00 15.78  ? 9   LYS B O   1 
ATOM   3696 C  CB  . LYS B 1 9   ? -16.770 6.014   -8.226  1.00 19.67  ? 9   LYS B CB  1 
ATOM   3697 C  CG  . LYS B 1 9   ? -16.964 7.458   -7.802  1.00 19.45  ? 9   LYS B CG  1 
ATOM   3698 C  CD  . LYS B 1 9   ? -18.394 7.860   -7.849  1.00 20.23  ? 9   LYS B CD  1 
ATOM   3699 C  CE  . LYS B 1 9   ? -18.527 9.341   -7.629  1.00 19.80  ? 9   LYS B CE  1 
ATOM   3700 N  NZ  . LYS B 1 9   ? -19.918 9.791   -7.794  1.00 21.37  ? 9   LYS B NZ  1 
ATOM   3701 N  N   . THR B 1 10  ? -13.849 5.796   -9.582  1.00 19.04  ? 10  THR B N   1 
ATOM   3702 C  CA  . THR B 1 10  ? -12.677 6.371   -10.228 1.00 22.31  ? 10  THR B CA  1 
ATOM   3703 C  C   . THR B 1 10  ? -13.045 7.138   -11.503 1.00 20.12  ? 10  THR B C   1 
ATOM   3704 O  O   . THR B 1 10  ? -14.110 6.967   -12.092 1.00 18.75  ? 10  THR B O   1 
ATOM   3705 C  CB  . THR B 1 10  ? -11.640 5.275   -10.509 1.00 23.98  ? 10  THR B CB  1 
ATOM   3706 O  OG1 . THR B 1 10  ? -12.276 4.343   -11.380 1.00 27.26  ? 10  THR B OG1 1 
ATOM   3707 C  CG2 . THR B 1 10  ? -11.144 4.565   -9.267  1.00 24.03  ? 10  THR B CG2 1 
ATOM   3708 N  N   . PHE B 1 11  ? -12.131 8.013   -11.923 1.00 19.25  ? 11  PHE B N   1 
ATOM   3709 C  CA  . PHE B 1 11  ? -12.365 8.952   -13.008 1.00 20.00  ? 11  PHE B CA  1 
ATOM   3710 C  C   . PHE B 1 11  ? -11.268 8.798   -14.055 1.00 23.12  ? 11  PHE B C   1 
ATOM   3711 O  O   . PHE B 1 11  ? -10.592 9.771   -14.403 1.00 27.37  ? 11  PHE B O   1 
ATOM   3712 C  CB  . PHE B 1 11  ? -12.380 10.401  -12.508 1.00 19.04  ? 11  PHE B CB  1 
ATOM   3713 C  CG  . PHE B 1 11  ? -13.492 10.752  -11.557 1.00 20.09  ? 11  PHE B CG  1 
ATOM   3714 C  CD1 . PHE B 1 11  ? -13.523 10.211  -10.270 1.00 21.00  ? 11  PHE B CD1 1 
ATOM   3715 C  CD2 . PHE B 1 11  ? -14.520 11.602  -11.949 1.00 19.78  ? 11  PHE B CD2 1 
ATOM   3716 C  CE1 . PHE B 1 11  ? -14.582 10.470  -9.413  1.00 21.45  ? 11  PHE B CE1 1 
ATOM   3717 C  CE2 . PHE B 1 11  ? -15.573 11.873  -11.089 1.00 22.15  ? 11  PHE B CE2 1 
ATOM   3718 C  CZ  . PHE B 1 11  ? -15.614 11.309  -9.822  1.00 21.75  ? 11  PHE B CZ  1 
ATOM   3719 N  N   . GLY B 1 12  ? -11.030 7.567   -14.507 1.00 23.01  ? 12  GLY B N   1 
ATOM   3720 C  CA  . GLY B 1 12  ? -10.027 7.361   -15.532 1.00 23.04  ? 12  GLY B CA  1 
ATOM   3721 C  C   . GLY B 1 12  ? -8.625  7.558   -14.968 1.00 25.14  ? 12  GLY B C   1 
ATOM   3722 O  O   . GLY B 1 12  ? -8.309  7.002   -13.924 1.00 25.19  ? 12  GLY B O   1 
ATOM   3723 N  N   . GLU B 1 13  ? -7.824  8.416   -15.614 1.00 27.63  ? 13  GLU B N   1 
ATOM   3724 C  CA  . GLU B 1 13  ? -6.433  8.600   -15.231 1.00 31.76  ? 13  GLU B CA  1 
ATOM   3725 C  C   . GLU B 1 13  ? -6.322  9.503   -14.009 1.00 30.32  ? 13  GLU B C   1 
ATOM   3726 O  O   . GLU B 1 13  ? -5.247  9.603   -13.418 1.00 31.60  ? 13  GLU B O   1 
ATOM   3727 C  CB  . GLU B 1 13  ? -5.602  9.113   -16.406 1.00 36.66  ? 13  GLU B CB  1 
ATOM   3728 C  CG  . GLU B 1 13  ? -5.330  8.026   -17.435 1.00 43.64  ? 13  GLU B CG  1 
ATOM   3729 C  CD  . GLU B 1 13  ? -5.045  6.669   -16.810 1.00 53.09  ? 13  GLU B CD  1 
ATOM   3730 O  OE1 . GLU B 1 13  ? -3.974  6.531   -16.171 1.00 55.85  ? 13  GLU B OE1 1 
ATOM   3731 O  OE2 . GLU B 1 13  ? -5.922  5.763   -16.909 1.00 54.83  ? 13  GLU B OE2 1 
ATOM   3732 N  N   . LEU B 1 14  ? -7.442  10.111  -13.608 1.00 25.98  ? 14  LEU B N   1 
ATOM   3733 C  CA  . LEU B 1 14  ? -7.470  10.902  -12.392 1.00 30.48  ? 14  LEU B CA  1 
ATOM   3734 C  C   . LEU B 1 14  ? -7.737  10.029  -11.166 1.00 26.66  ? 14  LEU B C   1 
ATOM   3735 O  O   . LEU B 1 14  ? -7.697  10.536  -10.048 1.00 25.34  ? 14  LEU B O   1 
ATOM   3736 C  CB  . LEU B 1 14  ? -8.570  11.957  -12.531 1.00 30.97  ? 14  LEU B CB  1 
ATOM   3737 C  CG  . LEU B 1 14  ? -8.387  12.947  -13.675 1.00 35.12  ? 14  LEU B CG  1 
ATOM   3738 C  CD1 . LEU B 1 14  ? -9.722  13.570  -14.045 1.00 39.30  ? 14  LEU B CD1 1 
ATOM   3739 C  CD2 . LEU B 1 14  ? -7.386  14.029  -13.286 1.00 38.54  ? 14  LEU B CD2 1 
ATOM   3740 N  N   . LYS B 1 15  ? -8.042  8.743   -11.367 1.00 24.50  ? 15  LYS B N   1 
ATOM   3741 C  CA  . LYS B 1 15  ? -8.355  7.858   -10.258 1.00 25.57  ? 15  LYS B CA  1 
ATOM   3742 C  C   . LYS B 1 15  ? -9.359  8.562   -9.353  1.00 24.85  ? 15  LYS B C   1 
ATOM   3743 O  O   . LYS B 1 15  ? -10.358 9.067   -9.865  1.00 22.58  ? 15  LYS B O   1 
ATOM   3744 C  CB  . LYS B 1 15  ? -7.061  7.483   -9.542  1.00 27.86  ? 15  LYS B CB  1 
ATOM   3745 C  CG  . LYS B 1 15  ? -5.992  6.883   -10.438 1.00 32.35  ? 15  LYS B CG  1 
ATOM   3746 C  CD  . LYS B 1 15  ? -4.606  6.973   -9.834  1.00 31.39  ? 15  LYS B CD  1 
ATOM   3747 C  CE  . LYS B 1 15  ? -3.812  5.708   -10.071 1.00 33.26  ? 15  LYS B CE  1 
ATOM   3748 N  NZ  . LYS B 1 15  ? -3.812  5.373   -11.505 1.00 34.06  ? 15  LYS B NZ  1 
ATOM   3749 N  N   . ASN B 1 16  ? -9.081  8.634   -8.032  1.00 23.17  ? 16  ASN B N   1 
ATOM   3750 C  CA  . ASN B 1 16  ? -10.097 9.076   -7.083  1.00 22.62  ? 16  ASN B CA  1 
ATOM   3751 C  C   . ASN B 1 16  ? -10.074 10.578  -6.877  1.00 20.66  ? 16  ASN B C   1 
ATOM   3752 O  O   . ASN B 1 16  ? -10.923 11.123  -6.176  1.00 21.61  ? 16  ASN B O   1 
ATOM   3753 C  CB  . ASN B 1 16  ? -9.944  8.399   -5.722  1.00 22.46  ? 16  ASN B CB  1 
ATOM   3754 C  CG  . ASN B 1 16  ? -10.249 6.925   -5.798  1.00 20.22  ? 16  ASN B CG  1 
ATOM   3755 O  OD1 . ASN B 1 16  ? -9.461  6.120   -5.328  1.00 19.31  ? 16  ASN B OD1 1 
ATOM   3756 N  ND2 . ASN B 1 16  ? -11.394 6.570   -6.365  1.00 19.73  ? 16  ASN B ND2 1 
ATOM   3757 N  N   . LEU B 1 17  ? -9.087  11.240  -7.470  1.00 22.60  ? 17  LEU B N   1 
ATOM   3758 C  CA  . LEU B 1 17  ? -8.784  12.620  -7.095  1.00 24.88  ? 17  LEU B CA  1 
ATOM   3759 C  C   . LEU B 1 17  ? -9.995  13.551  -7.227  1.00 22.94  ? 17  LEU B C   1 
ATOM   3760 O  O   . LEU B 1 17  ? -10.223 14.385  -6.341  1.00 22.25  ? 17  LEU B O   1 
ATOM   3761 C  CB  . LEU B 1 17  ? -7.596  13.162  -7.897  1.00 27.04  ? 17  LEU B CB  1 
ATOM   3762 C  CG  . LEU B 1 17  ? -7.067  14.519  -7.402  1.00 29.76  ? 17  LEU B CG  1 
ATOM   3763 C  CD1 . LEU B 1 17  ? -6.684  14.463  -5.911  1.00 29.10  ? 17  LEU B CD1 1 
ATOM   3764 C  CD2 . LEU B 1 17  ? -5.884  14.984  -8.239  1.00 30.17  ? 17  LEU B CD2 1 
ATOM   3765 N  N   . PRO B 1 18  ? -10.813 13.502  -8.309  1.00 19.87  ? 18  PRO B N   1 
ATOM   3766 C  CA  . PRO B 1 18  ? -11.973 14.392  -8.401  1.00 18.95  ? 18  PRO B CA  1 
ATOM   3767 C  C   . PRO B 1 18  ? -12.995 14.335  -7.267  1.00 18.87  ? 18  PRO B C   1 
ATOM   3768 O  O   . PRO B 1 18  ? -13.828 15.238  -7.135  1.00 22.92  ? 18  PRO B O   1 
ATOM   3769 C  CB  . PRO B 1 18  ? -12.584 13.997  -9.752  1.00 18.25  ? 18  PRO B CB  1 
ATOM   3770 C  CG  . PRO B 1 18  ? -11.434 13.497  -10.539 1.00 18.24  ? 18  PRO B CG  1 
ATOM   3771 C  CD  . PRO B 1 18  ? -10.630 12.710  -9.527  1.00 19.37  ? 18  PRO B CD  1 
ATOM   3772 N  N   . LEU B 1 19  ? -12.925 13.316  -6.413  1.00 18.10  ? 19  LEU B N   1 
ATOM   3773 C  CA  . LEU B 1 19  ? -13.850 13.211  -5.299  1.00 21.62  ? 19  LEU B CA  1 
ATOM   3774 C  C   . LEU B 1 19  ? -13.584 14.271  -4.234  1.00 21.97  ? 19  LEU B C   1 
ATOM   3775 O  O   . LEU B 1 19  ? -14.463 14.572  -3.423  1.00 22.06  ? 19  LEU B O   1 
ATOM   3776 C  CB  . LEU B 1 19  ? -13.742 11.816  -4.685  1.00 22.51  ? 19  LEU B CB  1 
ATOM   3777 C  CG  . LEU B 1 19  ? -14.157 10.691  -5.617  1.00 23.17  ? 19  LEU B CG  1 
ATOM   3778 C  CD1 . LEU B 1 19  ? -14.084 9.378   -4.888  1.00 23.47  ? 19  LEU B CD1 1 
ATOM   3779 C  CD2 . LEU B 1 19  ? -15.571 10.947  -6.133  1.00 23.84  ? 19  LEU B CD2 1 
ATOM   3780 N  N   . LEU B 1 20  ? -12.357 14.791  -4.200  1.00 24.31  ? 20  LEU B N   1 
ATOM   3781 C  CA  . LEU B 1 20  ? -12.008 15.859  -3.276  1.00 24.47  ? 20  LEU B CA  1 
ATOM   3782 C  C   . LEU B 1 20  ? -12.109 17.246  -3.934  1.00 27.38  ? 20  LEU B C   1 
ATOM   3783 O  O   . LEU B 1 20  ? -11.838 18.248  -3.285  1.00 27.18  ? 20  LEU B O   1 
ATOM   3784 C  CB  . LEU B 1 20  ? -10.570 15.615  -2.812  1.00 25.16  ? 20  LEU B CB  1 
ATOM   3785 C  CG  . LEU B 1 20  ? -10.318 14.302  -2.076  1.00 25.21  ? 20  LEU B CG  1 
ATOM   3786 C  CD1 . LEU B 1 20  ? -8.993  14.366  -1.336  1.00 24.97  ? 20  LEU B CD1 1 
ATOM   3787 C  CD2 . LEU B 1 20  ? -11.455 13.988  -1.129  1.00 27.23  ? 20  LEU B CD2 1 
ATOM   3788 N  N   . ASN B 1 21  ? -12.475 17.324  -5.226  1.00 26.82  ? 21  ASN B N   1 
ATOM   3789 C  CA  . ASN B 1 21  ? -12.797 18.596  -5.853  1.00 26.19  ? 21  ASN B CA  1 
ATOM   3790 C  C   . ASN B 1 21  ? -14.184 19.014  -5.380  1.00 26.83  ? 21  ASN B C   1 
ATOM   3791 O  O   . ASN B 1 21  ? -15.164 18.917  -6.107  1.00 25.10  ? 21  ASN B O   1 
ATOM   3792 C  CB  . ASN B 1 21  ? -12.713 18.526  -7.378  1.00 27.57  ? 21  ASN B CB  1 
ATOM   3793 C  CG  . ASN B 1 21  ? -12.661 19.881  -8.060  1.00 30.39  ? 21  ASN B CG  1 
ATOM   3794 O  OD1 . ASN B 1 21  ? -12.698 20.933  -7.413  1.00 30.56  ? 21  ASN B OD1 1 
ATOM   3795 N  ND2 . ASN B 1 21  ? -12.579 19.861  -9.383  1.00 30.14  ? 21  ASN B ND2 1 
ATOM   3796 N  N   . THR B 1 22  ? -14.228 19.508  -4.149  1.00 24.59  ? 22  THR B N   1 
ATOM   3797 C  CA  . THR B 1 22  ? -15.465 19.826  -3.476  1.00 25.96  ? 22  THR B CA  1 
ATOM   3798 C  C   . THR B 1 22  ? -15.148 20.810  -2.344  1.00 26.12  ? 22  THR B C   1 
ATOM   3799 O  O   . THR B 1 22  ? -14.043 20.803  -1.823  1.00 26.01  ? 22  THR B O   1 
ATOM   3800 C  CB  . THR B 1 22  ? -16.134 18.540  -2.968  1.00 28.40  ? 22  THR B CB  1 
ATOM   3801 O  OG1 . THR B 1 22  ? -17.314 18.850  -2.227  1.00 32.07  ? 22  THR B OG1 1 
ATOM   3802 C  CG2 . THR B 1 22  ? -15.258 17.735  -2.037  1.00 28.51  ? 22  THR B CG2 1 
ATOM   3803 N  N   . ASP B 1 23  ? -16.132 21.625  -1.968  1.00 26.78  ? 23  ASP B N   1 
ATOM   3804 C  CA  . ASP B 1 23  ? -16.026 22.514  -0.828  1.00 31.84  ? 23  ASP B CA  1 
ATOM   3805 C  C   . ASP B 1 23  ? -15.899 21.711  0.472   1.00 27.38  ? 23  ASP B C   1 
ATOM   3806 O  O   . ASP B 1 23  ? -15.301 22.192  1.427   1.00 25.03  ? 23  ASP B O   1 
ATOM   3807 C  CB  . ASP B 1 23  ? -17.248 23.438  -0.718  1.00 38.17  ? 23  ASP B CB  1 
ATOM   3808 C  CG  . ASP B 1 23  ? -17.475 24.406  -1.871  1.00 46.26  ? 23  ASP B CG  1 
ATOM   3809 O  OD1 . ASP B 1 23  ? -16.559 24.575  -2.711  1.00 48.52  ? 23  ASP B OD1 1 
ATOM   3810 O  OD2 . ASP B 1 23  ? -18.592 24.984  -1.931  1.00 53.23  ? 23  ASP B OD2 1 
ATOM   3811 N  N   . LYS B 1 24  ? -16.447 20.485  0.504   1.00 25.12  ? 24  LYS B N   1 
ATOM   3812 C  CA  . LYS B 1 24  ? -16.552 19.731  1.744   1.00 22.31  ? 24  LYS B CA  1 
ATOM   3813 C  C   . LYS B 1 24  ? -15.917 18.342  1.610   1.00 20.56  ? 24  LYS B C   1 
ATOM   3814 O  O   . LYS B 1 24  ? -16.611 17.340  1.675   1.00 17.57  ? 24  LYS B O   1 
ATOM   3815 C  CB  . LYS B 1 24  ? -18.016 19.728  2.180   1.00 22.61  ? 24  LYS B CB  1 
ATOM   3816 C  CG  . LYS B 1 24  ? -18.565 21.104  2.508   1.00 22.92  ? 24  LYS B CG  1 
ATOM   3817 C  CD  . LYS B 1 24  ? -20.082 21.131  2.635   1.00 25.79  ? 24  LYS B CD  1 
ATOM   3818 C  CE  . LYS B 1 24  ? -20.615 22.511  2.963   1.00 25.30  ? 24  LYS B CE  1 
ATOM   3819 N  NZ  . LYS B 1 24  ? -21.983 22.440  3.510   1.00 26.08  ? 24  LYS B NZ  1 
ATOM   3820 N  N   . PRO B 1 25  ? -14.566 18.248  1.492   1.00 19.89  ? 25  PRO B N   1 
ATOM   3821 C  CA  . PRO B 1 25  ? -13.892 16.971  1.287   1.00 20.08  ? 25  PRO B CA  1 
ATOM   3822 C  C   . PRO B 1 25  ? -14.021 15.950  2.419   1.00 20.79  ? 25  PRO B C   1 
ATOM   3823 O  O   . PRO B 1 25  ? -14.251 14.758  2.163   1.00 20.63  ? 25  PRO B O   1 
ATOM   3824 C  CB  . PRO B 1 25  ? -12.417 17.348  1.082   1.00 20.88  ? 25  PRO B CB  1 
ATOM   3825 C  CG  . PRO B 1 25  ? -12.278 18.741  1.666   1.00 21.24  ? 25  PRO B CG  1 
ATOM   3826 C  CD  . PRO B 1 25  ? -13.631 19.383  1.507   1.00 19.42  ? 25  PRO B CD  1 
ATOM   3827 N  N   . VAL B 1 26  ? -13.865 16.392  3.673   1.00 20.09  ? 26  VAL B N   1 
ATOM   3828 C  CA  . VAL B 1 26  ? -13.977 15.478  4.799   1.00 18.72  ? 26  VAL B CA  1 
ATOM   3829 C  C   . VAL B 1 26  ? -15.379 14.883  4.862   1.00 17.90  ? 26  VAL B C   1 
ATOM   3830 O  O   . VAL B 1 26  ? -15.534 13.687  5.099   1.00 17.56  ? 26  VAL B O   1 
ATOM   3831 C  CB  . VAL B 1 26  ? -13.593 16.161  6.125   1.00 20.75  ? 26  VAL B CB  1 
ATOM   3832 C  CG1 . VAL B 1 26  ? -13.916 15.301  7.339   1.00 20.01  ? 26  VAL B CG1 1 
ATOM   3833 C  CG2 . VAL B 1 26  ? -12.115 16.507  6.128   1.00 22.99  ? 26  VAL B CG2 1 
ATOM   3834 N  N   . GLN B 1 27  ? -16.412 15.729  4.692   1.00 17.44  ? 27  GLN B N   1 
ATOM   3835 C  CA  . GLN B 1 27  ? -17.773 15.249  4.698   1.00 18.27  ? 27  GLN B CA  1 
ATOM   3836 C  C   . GLN B 1 27  ? -17.986 14.270  3.532   1.00 18.91  ? 27  GLN B C   1 
ATOM   3837 O  O   . GLN B 1 27  ? -18.680 13.276  3.698   1.00 16.90  ? 27  GLN B O   1 
ATOM   3838 C  CB  . GLN B 1 27  ? -18.728 16.439  4.692   1.00 20.14  ? 27  GLN B CB  1 
ATOM   3839 C  CG  . GLN B 1 27  ? -18.648 17.167  6.022   1.00 23.02  ? 27  GLN B CG  1 
ATOM   3840 C  CD  . GLN B 1 27  ? -19.312 18.515  5.991   1.00 22.58  ? 27  GLN B CD  1 
ATOM   3841 O  OE1 . GLN B 1 27  ? -20.513 18.608  6.209   1.00 22.39  ? 27  GLN B OE1 1 
ATOM   3842 N  NE2 . GLN B 1 27  ? -18.527 19.549  5.714   1.00 24.26  ? 27  GLN B NE2 1 
ATOM   3843 N  N   . ALA B 1 28  ? -17.380 14.553  2.371   1.00 18.06  ? 28  ALA B N   1 
ATOM   3844 C  CA  . ALA B 1 28  ? -17.381 13.607  1.261   1.00 19.92  ? 28  ALA B CA  1 
ATOM   3845 C  C   . ALA B 1 28  ? -16.759 12.245  1.631   1.00 19.23  ? 28  ALA B C   1 
ATOM   3846 O  O   . ALA B 1 28  ? -17.304 11.169  1.313   1.00 18.84  ? 28  ALA B O   1 
ATOM   3847 C  CB  . ALA B 1 28  ? -16.675 14.258  0.082   1.00 19.25  ? 28  ALA B CB  1 
ATOM   3848 N  N   . LEU B 1 29  ? -15.591 12.269  2.277   1.00 16.78  ? 29  LEU B N   1 
ATOM   3849 C  CA  . LEU B 1 29  ? -14.924 11.034  2.673   1.00 17.36  ? 29  LEU B CA  1 
ATOM   3850 C  C   . LEU B 1 29  ? -15.749 10.261  3.696   1.00 16.50  ? 29  LEU B C   1 
ATOM   3851 O  O   . LEU B 1 29  ? -15.713 9.034   3.718   1.00 16.48  ? 29  LEU B O   1 
ATOM   3852 C  CB  . LEU B 1 29  ? -13.530 11.353  3.229   1.00 16.60  ? 29  LEU B CB  1 
ATOM   3853 C  CG  . LEU B 1 29  ? -12.536 11.809  2.184   1.00 15.74  ? 29  LEU B CG  1 
ATOM   3854 C  CD1 . LEU B 1 29  ? -11.376 12.556  2.819   1.00 16.04  ? 29  LEU B CD1 1 
ATOM   3855 C  CD2 . LEU B 1 29  ? -12.015 10.614  1.384   1.00 17.37  ? 29  LEU B CD2 1 
ATOM   3856 N  N   . MET B 1 30  ? -16.427 10.979  4.597   1.00 15.78  ? 30  MET B N   1 
ATOM   3857 C  CA  . MET B 1 30  ? -17.249 10.357  5.616   1.00 16.73  ? 30  MET B CA  1 
ATOM   3858 C  C   . MET B 1 30  ? -18.344 9.528   4.942   1.00 19.55  ? 30  MET B C   1 
ATOM   3859 O  O   . MET B 1 30  ? -18.721 8.460   5.428   1.00 19.23  ? 30  MET B O   1 
ATOM   3860 C  CB  . MET B 1 30  ? -17.897 11.413  6.516   1.00 16.58  ? 30  MET B CB  1 
ATOM   3861 C  CG  . MET B 1 30  ? -17.001 11.895  7.615   1.00 17.36  ? 30  MET B CG  1 
ATOM   3862 S  SD  . MET B 1 30  ? -17.648 13.383  8.473   1.00 20.36  ? 30  MET B SD  1 
ATOM   3863 C  CE  . MET B 1 30  ? -18.871 12.535  9.476   1.00 19.84  ? 30  MET B CE  1 
ATOM   3864 N  N   . LYS B 1 31  ? -18.886 10.087  3.853   1.00 20.26  ? 31  LYS B N   1 
ATOM   3865 C  CA  . LYS B 1 31  ? -19.957 9.447   3.092   1.00 23.62  ? 31  LYS B CA  1 
ATOM   3866 C  C   . LYS B 1 31  ? -19.417 8.175   2.423   1.00 20.65  ? 31  LYS B C   1 
ATOM   3867 O  O   . LYS B 1 31  ? -20.005 7.109   2.550   1.00 19.06  ? 31  LYS B O   1 
ATOM   3868 C  CB  . LYS B 1 31  ? -20.566 10.509  2.168   1.00 26.44  ? 31  LYS B CB  1 
ATOM   3869 C  CG  . LYS B 1 31  ? -21.677 10.079  1.207   1.00 33.23  ? 31  LYS B CG  1 
ATOM   3870 C  CD  . LYS B 1 31  ? -22.280 8.679   1.381   1.00 40.33  ? 31  LYS B CD  1 
ATOM   3871 C  CE  . LYS B 1 31  ? -22.960 8.386   2.702   1.00 45.18  ? 31  LYS B CE  1 
ATOM   3872 N  NZ  . LYS B 1 31  ? -23.599 7.050   2.697   1.00 46.16  ? 31  LYS B NZ  1 
ATOM   3873 N  N   . ILE B 1 32  ? -18.259 8.276   1.771   1.00 17.95  ? 32  ILE B N   1 
ATOM   3874 C  CA  . ILE B 1 32  ? -17.547 7.102   1.300   1.00 20.65  ? 32  ILE B CA  1 
ATOM   3875 C  C   . ILE B 1 32  ? -17.419 6.070   2.434   1.00 22.29  ? 32  ILE B C   1 
ATOM   3876 O  O   . ILE B 1 32  ? -17.812 4.908   2.284   1.00 18.03  ? 32  ILE B O   1 
ATOM   3877 C  CB  . ILE B 1 32  ? -16.227 7.560   0.642   1.00 21.07  ? 32  ILE B CB  1 
ATOM   3878 C  CG1 . ILE B 1 32  ? -16.551 8.413   -0.589  1.00 20.24  ? 32  ILE B CG1 1 
ATOM   3879 C  CG2 . ILE B 1 32  ? -15.315 6.391   0.296   1.00 21.52  ? 32  ILE B CG2 1 
ATOM   3880 C  CD1 . ILE B 1 32  ? -15.380 9.092   -1.248  1.00 21.76  ? 32  ILE B CD1 1 
ATOM   3881 N  N   . ALA B 1 33  ? -16.909 6.480   3.601   1.00 20.43  ? 33  ALA B N   1 
ATOM   3882 C  CA  . ALA B 1 33  ? -16.713 5.538   4.692   1.00 20.53  ? 33  ALA B CA  1 
ATOM   3883 C  C   . ALA B 1 33  ? -18.030 4.861   5.059   1.00 20.37  ? 33  ALA B C   1 
ATOM   3884 O  O   . ALA B 1 33  ? -18.050 3.666   5.331   1.00 19.81  ? 33  ALA B O   1 
ATOM   3885 C  CB  . ALA B 1 33  ? -16.097 6.201   5.894   1.00 20.36  ? 33  ALA B CB  1 
ATOM   3886 N  N   . ASP B 1 34  ? -19.137 5.599   5.045   1.00 22.15  ? 34  ASP B N   1 
ATOM   3887 C  CA  . ASP B 1 34  ? -20.435 4.999   5.321   1.00 26.23  ? 34  ASP B CA  1 
ATOM   3888 C  C   . ASP B 1 34  ? -20.740 3.890   4.312   1.00 22.74  ? 34  ASP B C   1 
ATOM   3889 O  O   . ASP B 1 34  ? -21.230 2.837   4.694   1.00 23.97  ? 34  ASP B O   1 
ATOM   3890 C  CB  . ASP B 1 34  ? -21.575 6.027   5.314   1.00 30.66  ? 34  ASP B CB  1 
ATOM   3891 C  CG  . ASP B 1 34  ? -21.533 7.039   6.451   1.00 36.43  ? 34  ASP B CG  1 
ATOM   3892 O  OD1 . ASP B 1 34  ? -21.229 6.645   7.603   1.00 38.77  ? 34  ASP B OD1 1 
ATOM   3893 O  OD2 . ASP B 1 34  ? -21.808 8.219   6.183   1.00 44.44  ? 34  ASP B OD2 1 
ATOM   3894 N  N   . GLU B 1 35  ? -20.410 4.108   3.035   1.00 23.07  ? 35  GLU B N   1 
ATOM   3895 C  CA  . GLU B 1 35  ? -20.686 3.137   1.986   1.00 25.12  ? 35  GLU B CA  1 
ATOM   3896 C  C   . GLU B 1 35  ? -19.725 1.944   2.090   1.00 23.81  ? 35  GLU B C   1 
ATOM   3897 O  O   . GLU B 1 35  ? -20.166 0.812   1.976   1.00 24.50  ? 35  GLU B O   1 
ATOM   3898 C  CB  . GLU B 1 35  ? -20.591 3.776   0.591   1.00 28.65  ? 35  GLU B CB  1 
ATOM   3899 C  CG  . GLU B 1 35  ? -21.676 4.794   0.289   1.00 33.27  ? 35  GLU B CG  1 
ATOM   3900 C  CD  . GLU B 1 35  ? -21.454 5.693   -0.925  1.00 42.85  ? 35  GLU B CD  1 
ATOM   3901 O  OE1 . GLU B 1 35  ? -20.380 6.398   -0.997  1.00 35.21  ? 35  GLU B OE1 1 
ATOM   3902 O  OE2 . GLU B 1 35  ? -22.384 5.743   -1.779  1.00 46.86  ? 35  GLU B OE2 1 
ATOM   3903 N  N   . LEU B 1 36  ? -18.413 2.180   2.271   1.00 20.77  ? 36  LEU B N   1 
ATOM   3904 C  CA  . LEU B 1 36  ? -17.418 1.135   2.041   1.00 20.22  ? 36  LEU B CA  1 
ATOM   3905 C  C   . LEU B 1 36  ? -16.870 0.499   3.326   1.00 21.70  ? 36  LEU B C   1 
ATOM   3906 O  O   . LEU B 1 36  ? -16.172 -0.510  3.219   1.00 22.82  ? 36  LEU B O   1 
ATOM   3907 C  CB  . LEU B 1 36  ? -16.241 1.696   1.250   1.00 19.25  ? 36  LEU B CB  1 
ATOM   3908 C  CG  . LEU B 1 36  ? -16.560 2.351   -0.092  1.00 18.38  ? 36  LEU B CG  1 
ATOM   3909 C  CD1 . LEU B 1 36  ? -15.298 2.688   -0.824  1.00 15.43  ? 36  LEU B CD1 1 
ATOM   3910 C  CD2 . LEU B 1 36  ? -17.481 1.500   -0.949  1.00 19.00  ? 36  LEU B CD2 1 
ATOM   3911 N  N   . GLY B 1 37  ? -17.118 1.078   4.513   1.00 19.73  ? 37  GLY B N   1 
ATOM   3912 C  CA  . GLY B 1 37  ? -16.713 0.460   5.770   1.00 18.16  ? 37  GLY B CA  1 
ATOM   3913 C  C   . GLY B 1 37  ? -15.389 1.006   6.319   1.00 22.17  ? 37  GLY B C   1 
ATOM   3914 O  O   . GLY B 1 37  ? -14.926 2.106   5.991   1.00 23.24  ? 37  GLY B O   1 
ATOM   3915 N  N   . GLU B 1 38  ? -14.765 0.189   7.161   1.00 22.76  ? 38  GLU B N   1 
ATOM   3916 C  CA  . GLU B 1 38  ? -13.719 0.640   8.064   1.00 23.56  ? 38  GLU B CA  1 
ATOM   3917 C  C   . GLU B 1 38  ? -12.430 1.035   7.345   1.00 21.11  ? 38  GLU B C   1 
ATOM   3918 O  O   . GLU B 1 38  ? -11.570 1.651   7.972   1.00 20.83  ? 38  GLU B O   1 
ATOM   3919 C  CB  . GLU B 1 38  ? -13.417 -0.447  9.090   1.00 22.89  ? 38  GLU B CB  1 
ATOM   3920 C  CG  . GLU B 1 38  ? -12.984 -1.747  8.452   1.00 26.40  ? 38  GLU B CG  1 
ATOM   3921 C  CD  . GLU B 1 38  ? -12.609 -2.874  9.402   1.00 28.82  ? 38  GLU B CD  1 
ATOM   3922 O  OE1 . GLU B 1 38  ? -12.707 -2.697  10.643  1.00 28.70  ? 38  GLU B OE1 1 
ATOM   3923 O  OE2 . GLU B 1 38  ? -12.235 -3.940  8.881   1.00 32.63  ? 38  GLU B OE2 1 
ATOM   3924 N  N   . ILE B 1 39  ? -12.260 0.671   6.063   1.00 21.67  ? 39  ILE B N   1 
ATOM   3925 C  CA  . ILE B 1 39  ? -11.056 1.049   5.338   1.00 18.83  ? 39  ILE B CA  1 
ATOM   3926 C  C   . ILE B 1 39  ? -11.322 1.108   3.847   1.00 17.89  ? 39  ILE B C   1 
ATOM   3927 O  O   . ILE B 1 39  ? -11.965 0.229   3.279   1.00 18.95  ? 39  ILE B O   1 
ATOM   3928 C  CB  . ILE B 1 39  ? -9.885  0.080   5.633   1.00 20.04  ? 39  ILE B CB  1 
ATOM   3929 C  CG1 . ILE B 1 39  ? -8.607  0.515   4.920   1.00 20.24  ? 39  ILE B CG1 1 
ATOM   3930 C  CG2 . ILE B 1 39  ? -10.243 -1.371  5.301   1.00 23.03  ? 39  ILE B CG2 1 
ATOM   3931 C  CD1 . ILE B 1 39  ? -7.380  -0.289  5.317   1.00 21.98  ? 39  ILE B CD1 1 
ATOM   3932 N  N   . PHE B 1 40  ? -10.730 2.104   3.190   1.00 17.18  ? 40  PHE B N   1 
ATOM   3933 C  CA  . PHE B 1 40  ? -10.776 2.155   1.739   1.00 16.91  ? 40  PHE B CA  1 
ATOM   3934 C  C   . PHE B 1 40  ? -9.507  2.794   1.190   1.00 19.29  ? 40  PHE B C   1 
ATOM   3935 O  O   . PHE B 1 40  ? -8.892  3.640   1.836   1.00 18.35  ? 40  PHE B O   1 
ATOM   3936 C  CB  . PHE B 1 40  ? -12.046 2.842   1.226   1.00 15.66  ? 40  PHE B CB  1 
ATOM   3937 C  CG  . PHE B 1 40  ? -12.191 4.299   1.576   1.00 16.12  ? 40  PHE B CG  1 
ATOM   3938 C  CD1 . PHE B 1 40  ? -11.632 5.284   0.772   1.00 15.68  ? 40  PHE B CD1 1 
ATOM   3939 C  CD2 . PHE B 1 40  ? -12.903 4.690   2.712   1.00 16.37  ? 40  PHE B CD2 1 
ATOM   3940 C  CE1 . PHE B 1 40  ? -11.788 6.621   1.096   1.00 16.70  ? 40  PHE B CE1 1 
ATOM   3941 C  CE2 . PHE B 1 40  ? -13.034 6.031   3.036   1.00 16.01  ? 40  PHE B CE2 1 
ATOM   3942 C  CZ  . PHE B 1 40  ? -12.481 6.991   2.218   1.00 15.91  ? 40  PHE B CZ  1 
ATOM   3943 N  N   . LYS B 1 41  ? -9.095  2.292   0.013   1.00 20.77  ? 41  LYS B N   1 
ATOM   3944 C  CA  . LYS B 1 41  ? -8.028  2.858   -0.790  1.00 23.59  ? 41  LYS B CA  1 
ATOM   3945 C  C   . LYS B 1 41  ? -8.489  4.135   -1.471  1.00 21.81  ? 41  LYS B C   1 
ATOM   3946 O  O   . LYS B 1 41  ? -9.591  4.179   -2.028  1.00 20.21  ? 41  LYS B O   1 
ATOM   3947 C  CB  . LYS B 1 41  ? -7.564  1.921   -1.917  1.00 29.04  ? 41  LYS B CB  1 
ATOM   3948 C  CG  . LYS B 1 41  ? -6.275  2.373   -2.588  1.00 34.65  ? 41  LYS B CG  1 
ATOM   3949 C  CD  . LYS B 1 41  ? -5.260  1.268   -2.816  1.00 40.04  ? 41  LYS B CD  1 
ATOM   3950 C  CE  . LYS B 1 41  ? -5.783  0.135   -3.661  1.00 43.23  ? 41  LYS B CE  1 
ATOM   3951 N  NZ  . LYS B 1 41  ? -4.885  -1.037  -3.520  1.00 47.61  ? 41  LYS B NZ  1 
ATOM   3952 N  N   . PHE B 1 42  ? -7.581  5.122   -1.466  1.00 19.73  ? 42  PHE B N   1 
ATOM   3953 C  CA  . PHE B 1 42  ? -7.769  6.378   -2.168  1.00 20.95  ? 42  PHE B CA  1 
ATOM   3954 C  C   . PHE B 1 42  ? -6.527  6.648   -3.010  1.00 23.44  ? 42  PHE B C   1 
ATOM   3955 O  O   . PHE B 1 42  ? -5.419  6.814   -2.497  1.00 25.24  ? 42  PHE B O   1 
ATOM   3956 C  CB  . PHE B 1 42  ? -8.117  7.501   -1.185  1.00 20.71  ? 42  PHE B CB  1 
ATOM   3957 C  CG  . PHE B 1 42  ? -8.658  8.738   -1.854  1.00 21.30  ? 42  PHE B CG  1 
ATOM   3958 C  CD1 . PHE B 1 42  ? -7.801  9.623   -2.494  1.00 23.45  ? 42  PHE B CD1 1 
ATOM   3959 C  CD2 . PHE B 1 42  ? -10.025 8.977   -1.917  1.00 22.50  ? 42  PHE B CD2 1 
ATOM   3960 C  CE1 . PHE B 1 42  ? -8.303  10.749  -3.137  1.00 23.91  ? 42  PHE B CE1 1 
ATOM   3961 C  CE2 . PHE B 1 42  ? -10.517 10.112  -2.538  1.00 21.33  ? 42  PHE B CE2 1 
ATOM   3962 C  CZ  . PHE B 1 42  ? -9.658  10.979  -3.175  1.00 21.18  ? 42  PHE B CZ  1 
ATOM   3963 N  N   . GLU B 1 43  ? -6.702  6.644   -4.326  1.00 23.94  ? 43  GLU B N   1 
ATOM   3964 C  CA  . GLU B 1 43  ? -5.581  6.808   -5.232  1.00 25.95  ? 43  GLU B CA  1 
ATOM   3965 C  C   . GLU B 1 43  ? -5.780  8.101   -5.989  1.00 25.59  ? 43  GLU B C   1 
ATOM   3966 O  O   . GLU B 1 43  ? -6.893  8.396   -6.434  1.00 26.93  ? 43  GLU B O   1 
ATOM   3967 C  CB  . GLU B 1 43  ? -5.493  5.696   -6.273  1.00 29.58  ? 43  GLU B CB  1 
ATOM   3968 C  CG  . GLU B 1 43  ? -5.467  4.295   -5.699  1.00 35.36  ? 43  GLU B CG  1 
ATOM   3969 C  CD  . GLU B 1 43  ? -5.245  3.218   -6.754  1.00 44.39  ? 43  GLU B CD  1 
ATOM   3970 O  OE1 . GLU B 1 43  ? -6.016  3.200   -7.752  1.00 43.79  ? 43  GLU B OE1 1 
ATOM   3971 O  OE2 . GLU B 1 43  ? -4.322  2.377   -6.572  1.00 48.52  ? 43  GLU B OE2 1 
ATOM   3972 N  N   . ALA B 1 44  ? -4.674  8.827   -6.161  1.00 26.01  ? 44  ALA B N   1 
ATOM   3973 C  CA  . ALA B 1 44  ? -4.600  9.989   -7.027  1.00 27.65  ? 44  ALA B CA  1 
ATOM   3974 C  C   . ALA B 1 44  ? -3.347  9.820   -7.876  1.00 28.58  ? 44  ALA B C   1 
ATOM   3975 O  O   . ALA B 1 44  ? -2.548  8.937   -7.579  1.00 30.51  ? 44  ALA B O   1 
ATOM   3976 C  CB  . ALA B 1 44  ? -4.583  11.237  -6.190  1.00 24.85  ? 44  ALA B CB  1 
ATOM   3977 N  N   . PRO B 1 45  ? -3.148  10.590  -8.968  1.00 30.52  ? 45  PRO B N   1 
ATOM   3978 C  CA  . PRO B 1 45  ? -1.946  10.438  -9.791  1.00 36.33  ? 45  PRO B CA  1 
ATOM   3979 C  C   . PRO B 1 45  ? -0.659  10.448  -8.961  1.00 36.17  ? 45  PRO B C   1 
ATOM   3980 O  O   . PRO B 1 45  ? -0.316  11.442  -8.352  1.00 40.00  ? 45  PRO B O   1 
ATOM   3981 C  CB  . PRO B 1 45  ? -2.030  11.644  -10.751 1.00 37.01  ? 45  PRO B CB  1 
ATOM   3982 C  CG  . PRO B 1 45  ? -3.516  11.950  -10.859 1.00 32.51  ? 45  PRO B CG  1 
ATOM   3983 C  CD  . PRO B 1 45  ? -4.053  11.630  -9.478  1.00 32.20  ? 45  PRO B CD  1 
ATOM   3984 N  N   . GLY B 1 46  ? 0.015   9.300   -8.869  1.00 45.57  ? 46  GLY B N   1 
ATOM   3985 C  CA  . GLY B 1 46  ? 1.311   9.219   -8.214  1.00 44.61  ? 46  GLY B CA  1 
ATOM   3986 C  C   . GLY B 1 46  ? 1.222   9.221   -6.688  1.00 43.14  ? 46  GLY B C   1 
ATOM   3987 O  O   . GLY B 1 46  ? 2.208   9.517   -6.011  1.00 43.28  ? 46  GLY B O   1 
ATOM   3988 N  N   . ARG B 1 47  ? 0.055   8.889   -6.122  1.00 39.30  ? 47  ARG B N   1 
ATOM   3989 C  CA  . ARG B 1 47  ? -0.029  8.770   -4.676  1.00 36.61  ? 47  ARG B CA  1 
ATOM   3990 C  C   . ARG B 1 47  ? -1.228  7.898   -4.302  1.00 35.16  ? 47  ARG B C   1 
ATOM   3991 O  O   . ARG B 1 47  ? -2.204  7.786   -5.039  1.00 30.87  ? 47  ARG B O   1 
ATOM   3992 C  CB  . ARG B 1 47  ? -0.004  10.155  -4.008  1.00 44.55  ? 47  ARG B CB  1 
ATOM   3993 C  CG  . ARG B 1 47  ? -1.322  10.920  -4.051  1.00 49.58  ? 47  ARG B CG  1 
ATOM   3994 C  CD  . ARG B 1 47  ? -1.318  12.232  -3.281  1.00 51.12  ? 47  ARG B CD  1 
ATOM   3995 N  NE  . ARG B 1 47  ? -2.556  12.413  -2.518  1.00 56.79  ? 47  ARG B NE  1 
ATOM   3996 C  CZ  . ARG B 1 47  ? -2.965  13.550  -1.948  1.00 59.64  ? 47  ARG B CZ  1 
ATOM   3997 N  NH1 . ARG B 1 47  ? -2.334  14.689  -2.183  1.00 59.21  ? 47  ARG B NH1 1 
ATOM   3998 N  NH2 . ARG B 1 47  ? -4.040  13.555  -1.176  1.00 57.09  ? 47  ARG B NH2 1 
ATOM   3999 N  N   . VAL B 1 48  ? -1.108  7.247   -3.138  1.00 29.74  ? 48  VAL B N   1 
ATOM   4000 C  CA  . VAL B 1 48  ? -2.128  6.353   -2.626  1.00 27.48  ? 48  VAL B CA  1 
ATOM   4001 C  C   . VAL B 1 48  ? -2.173  6.501   -1.102  1.00 26.43  ? 48  VAL B C   1 
ATOM   4002 O  O   . VAL B 1 48  ? -1.137  6.697   -0.445  1.00 24.15  ? 48  VAL B O   1 
ATOM   4003 C  CB  . VAL B 1 48  ? -1.873  4.907   -3.110  1.00 27.01  ? 48  VAL B CB  1 
ATOM   4004 C  CG1 . VAL B 1 48  ? -0.446  4.456   -2.854  1.00 26.71  ? 48  VAL B CG1 1 
ATOM   4005 C  CG2 . VAL B 1 48  ? -2.888  3.919   -2.549  1.00 27.31  ? 48  VAL B CG2 1 
ATOM   4006 N  N   . THR B 1 49  ? -3.393  6.520   -0.558  1.00 22.57  ? 49  THR B N   1 
ATOM   4007 C  CA  . THR B 1 49  ? -3.585  6.451   0.877   1.00 25.03  ? 49  THR B CA  1 
ATOM   4008 C  C   . THR B 1 49  ? -4.777  5.557   1.186   1.00 23.80  ? 49  THR B C   1 
ATOM   4009 O  O   . THR B 1 49  ? -5.535  5.165   0.296   1.00 20.24  ? 49  THR B O   1 
ATOM   4010 C  CB  . THR B 1 49  ? -3.784  7.822   1.539   1.00 29.32  ? 49  THR B CB  1 
ATOM   4011 O  OG1 . THR B 1 49  ? -3.011  8.800   0.847   1.00 40.79  ? 49  THR B OG1 1 
ATOM   4012 C  CG2 . THR B 1 49  ? -3.355  7.820   2.984   1.00 25.36  ? 49  THR B CG2 1 
ATOM   4013 N  N   . ARG B 1 50  ? -4.892  5.242   2.474   1.00 22.85  ? 50  ARG B N   1 
ATOM   4014 C  CA  . ARG B 1 50  ? -5.910  4.345   2.982   1.00 22.95  ? 50  ARG B CA  1 
ATOM   4015 C  C   . ARG B 1 50  ? -6.604  5.041   4.129   1.00 21.07  ? 50  ARG B C   1 
ATOM   4016 O  O   . ARG B 1 50  ? -5.958  5.382   5.120   1.00 21.21  ? 50  ARG B O   1 
ATOM   4017 C  CB  . ARG B 1 50  ? -5.209  3.058   3.395   1.00 22.98  ? 50  ARG B CB  1 
ATOM   4018 C  CG  . ARG B 1 50  ? -4.281  2.576   2.299   1.00 24.99  ? 50  ARG B CG  1 
ATOM   4019 C  CD  . ARG B 1 50  ? -3.217  1.647   2.818   1.00 24.33  ? 50  ARG B CD  1 
ATOM   4020 N  NE  . ARG B 1 50  ? -2.378  1.303   1.704   1.00 28.21  ? 50  ARG B NE  1 
ATOM   4021 C  CZ  . ARG B 1 50  ? -1.509  2.114   1.124   1.00 30.70  ? 50  ARG B CZ  1 
ATOM   4022 N  NH1 . ARG B 1 50  ? -1.328  3.341   1.590   1.00 28.52  ? 50  ARG B NH1 1 
ATOM   4023 N  NH2 . ARG B 1 50  ? -0.844  1.688   0.058   1.00 29.32  ? 50  ARG B NH2 1 
ATOM   4024 N  N   . TYR B 1 51  ? -7.910  5.259   3.985   1.00 18.20  ? 51  TYR B N   1 
ATOM   4025 C  CA  . TYR B 1 51  ? -8.676  5.901   5.032   1.00 17.42  ? 51  TYR B CA  1 
ATOM   4026 C  C   . TYR B 1 51  ? -9.211  4.873   6.019   1.00 17.47  ? 51  TYR B C   1 
ATOM   4027 O  O   . TYR B 1 51  ? -9.930  3.947   5.633   1.00 18.45  ? 51  TYR B O   1 
ATOM   4028 C  CB  . TYR B 1 51  ? -9.825  6.708   4.423   1.00 16.23  ? 51  TYR B CB  1 
ATOM   4029 C  CG  . TYR B 1 51  ? -9.338  8.011   3.819   1.00 16.55  ? 51  TYR B CG  1 
ATOM   4030 C  CD1 . TYR B 1 51  ? -8.801  8.025   2.539   1.00 17.04  ? 51  TYR B CD1 1 
ATOM   4031 C  CD2 . TYR B 1 51  ? -9.410  9.221   4.518   1.00 19.33  ? 51  TYR B CD2 1 
ATOM   4032 C  CE1 . TYR B 1 51  ? -8.372  9.203   1.958   1.00 18.93  ? 51  TYR B CE1 1 
ATOM   4033 C  CE2 . TYR B 1 51  ? -8.973  10.417  3.949   1.00 18.84  ? 51  TYR B CE2 1 
ATOM   4034 C  CZ  . TYR B 1 51  ? -8.436  10.392  2.672   1.00 19.82  ? 51  TYR B CZ  1 
ATOM   4035 O  OH  . TYR B 1 51  ? -7.971  11.488  2.010   1.00 22.29  ? 51  TYR B OH  1 
ATOM   4036 N  N   . LEU B 1 52  ? -8.884  5.065   7.307   1.00 17.29  ? 52  LEU B N   1 
ATOM   4037 C  CA  . LEU B 1 52  ? -9.405  4.232   8.381   1.00 16.19  ? 52  LEU B CA  1 
ATOM   4038 C  C   . LEU B 1 52  ? -10.519 4.930   9.156   1.00 16.81  ? 52  LEU B C   1 
ATOM   4039 O  O   . LEU B 1 52  ? -10.401 6.108   9.515   1.00 15.30  ? 52  LEU B O   1 
ATOM   4040 C  CB  . LEU B 1 52  ? -8.261  3.956   9.345   1.00 16.34  ? 52  LEU B CB  1 
ATOM   4041 C  CG  . LEU B 1 52  ? -7.029  3.283   8.773   1.00 19.69  ? 52  LEU B CG  1 
ATOM   4042 C  CD1 . LEU B 1 52  ? -6.094  2.856   9.909   1.00 19.10  ? 52  LEU B CD1 1 
ATOM   4043 C  CD2 . LEU B 1 52  ? -7.393  2.081   7.933   1.00 22.22  ? 52  LEU B CD2 1 
ATOM   4044 N  N   . SER B 1 53  ? -11.548 4.154   9.508   1.00 16.08  ? 53  SER B N   1 
ATOM   4045 C  CA  . SER B 1 53  ? -12.724 4.654   10.196  1.00 16.56  ? 53  SER B CA  1 
ATOM   4046 C  C   . SER B 1 53  ? -13.087 3.822   11.423  1.00 15.93  ? 53  SER B C   1 
ATOM   4047 O  O   . SER B 1 53  ? -13.926 4.254   12.185  1.00 16.88  ? 53  SER B O   1 
ATOM   4048 C  CB  . SER B 1 53  ? -13.908 4.735   9.274   1.00 18.78  ? 53  SER B CB  1 
ATOM   4049 O  OG  . SER B 1 53  ? -13.620 5.589   8.193   1.00 21.84  ? 53  SER B OG  1 
ATOM   4050 N  N   . SER B 1 54  ? -12.534 2.614   11.620  1.00 17.88  ? 54  SER B N   1 
ATOM   4051 C  CA  . SER B 1 54  ? -12.948 1.798   12.755  1.00 17.88  ? 54  SER B CA  1 
ATOM   4052 C  C   . SER B 1 54  ? -11.918 1.841   13.861  1.00 15.87  ? 54  SER B C   1 
ATOM   4053 O  O   . SER B 1 54  ? -10.735 2.009   13.584  1.00 15.12  ? 54  SER B O   1 
ATOM   4054 C  CB  . SER B 1 54  ? -13.240 0.349   12.393  1.00 18.84  ? 54  SER B CB  1 
ATOM   4055 O  OG  . SER B 1 54  ? -12.044 -0.315  12.033  1.00 17.75  ? 54  SER B OG  1 
ATOM   4056 N  N   . GLN B 1 55  ? -12.407 1.667   15.097  1.00 14.94  ? 55  GLN B N   1 
ATOM   4057 C  CA  . GLN B 1 55  ? -11.564 1.628   16.270  1.00 15.73  ? 55  GLN B CA  1 
ATOM   4058 C  C   . GLN B 1 55  ? -10.649 0.411   16.159  1.00 15.61  ? 55  GLN B C   1 
ATOM   4059 O  O   . GLN B 1 55  ? -9.496  0.503   16.535  1.00 15.73  ? 55  GLN B O   1 
ATOM   4060 C  CB  . GLN B 1 55  ? -12.379 1.694   17.562  1.00 14.94  ? 55  GLN B CB  1 
ATOM   4061 C  CG  . GLN B 1 55  ? -11.526 1.820   18.830  1.00 16.03  ? 55  GLN B CG  1 
ATOM   4062 C  CD  . GLN B 1 55  ? -11.154 0.488   19.446  1.00 16.63  ? 55  GLN B CD  1 
ATOM   4063 O  OE1 . GLN B 1 55  ? -11.503 -0.580  18.937  1.00 15.18  ? 55  GLN B OE1 1 
ATOM   4064 N  NE2 . GLN B 1 55  ? -10.395 0.520   20.527  1.00 17.14  ? 55  GLN B NE2 1 
ATOM   4065 N  N   . ARG B 1 56  ? -11.167 -0.700  15.629  1.00 16.67  ? 56  ARG B N   1 
ATOM   4066 C  CA  . ARG B 1 56  ? -10.393 -1.935  15.477  1.00 18.27  ? 56  ARG B CA  1 
ATOM   4067 C  C   . ARG B 1 56  ? -9.090  -1.686  14.712  1.00 17.28  ? 56  ARG B C   1 
ATOM   4068 O  O   . ARG B 1 56  ? -8.028  -2.180  15.088  1.00 18.57  ? 56  ARG B O   1 
ATOM   4069 C  CB  . ARG B 1 56  ? -11.217 -3.006  14.747  1.00 21.87  ? 56  ARG B CB  1 
ATOM   4070 C  CG  . ARG B 1 56  ? -10.504 -4.345  14.593  1.00 26.42  ? 56  ARG B CG  1 
ATOM   4071 C  CD  . ARG B 1 56  ? -11.402 -5.400  13.967  1.00 31.05  ? 56  ARG B CD  1 
ATOM   4072 N  NE  . ARG B 1 56  ? -11.440 -5.337  12.502  1.00 32.23  ? 56  ARG B NE  1 
ATOM   4073 C  CZ  . ARG B 1 56  ? -10.537 -5.874  11.685  1.00 31.19  ? 56  ARG B CZ  1 
ATOM   4074 N  NH1 . ARG B 1 56  ? -9.481  -6.511  12.165  1.00 32.53  ? 56  ARG B NH1 1 
ATOM   4075 N  NH2 . ARG B 1 56  ? -10.691 -5.758  10.376  1.00 33.64  ? 56  ARG B NH2 1 
ATOM   4076 N  N   . LEU B 1 57  ? -9.161  -0.995  13.576  1.00 16.65  ? 57  LEU B N   1 
ATOM   4077 C  CA  . LEU B 1 57  ? -7.969  -0.741  12.778  1.00 17.72  ? 57  LEU B CA  1 
ATOM   4078 C  C   . LEU B 1 57  ? -7.138  0.426   13.321  1.00 17.05  ? 57  LEU B C   1 
ATOM   4079 O  O   . LEU B 1 57  ? -5.895  0.462   13.224  1.00 17.10  ? 57  LEU B O   1 
ATOM   4080 C  CB  . LEU B 1 57  ? -8.416  -0.477  11.330  1.00 19.69  ? 57  LEU B CB  1 
ATOM   4081 C  CG  . LEU B 1 57  ? -9.008  -1.690  10.614  1.00 20.37  ? 57  LEU B CG  1 
ATOM   4082 C  CD1 . LEU B 1 57  ? -9.283  -1.358  9.164   1.00 20.97  ? 57  LEU B CD1 1 
ATOM   4083 C  CD2 . LEU B 1 57  ? -8.056  -2.868  10.707  1.00 21.90  ? 57  LEU B CD2 1 
ATOM   4084 N  N   . ILE B 1 58  ? -7.824  1.434   13.842  1.00 15.91  ? 58  ILE B N   1 
ATOM   4085 C  CA  . ILE B 1 58  ? -7.154  2.655   14.263  1.00 15.22  ? 58  ILE B CA  1 
ATOM   4086 C  C   . ILE B 1 58  ? -6.310  2.390   15.507  1.00 17.11  ? 58  ILE B C   1 
ATOM   4087 O  O   . ILE B 1 58  ? -5.216  2.971   15.657  1.00 16.50  ? 58  ILE B O   1 
ATOM   4088 C  CB  . ILE B 1 58  ? -8.174  3.820   14.377  1.00 15.46  ? 58  ILE B CB  1 
ATOM   4089 C  CG1 . ILE B 1 58  ? -8.646  4.199   12.965  1.00 15.21  ? 58  ILE B CG1 1 
ATOM   4090 C  CG2 . ILE B 1 58  ? -7.585  5.030   15.117  1.00 17.24  ? 58  ILE B CG2 1 
ATOM   4091 C  CD1 . ILE B 1 58  ? -9.765  5.205   12.897  1.00 15.23  ? 58  ILE B CD1 1 
ATOM   4092 N  N   . LYS B 1 59  ? -6.722  1.440   16.354  1.00 17.29  ? 59  LYS B N   1 
ATOM   4093 C  CA  . LYS B 1 59  ? -5.910  1.162   17.522  1.00 18.98  ? 59  LYS B CA  1 
ATOM   4094 C  C   . LYS B 1 59  ? -4.585  0.520   17.128  1.00 19.47  ? 59  LYS B C   1 
ATOM   4095 O  O   . LYS B 1 59  ? -3.619  0.604   17.885  1.00 19.31  ? 59  LYS B O   1 
ATOM   4096 C  CB  . LYS B 1 59  ? -6.645  0.291   18.531  1.00 19.94  ? 59  LYS B CB  1 
ATOM   4097 C  CG  . LYS B 1 59  ? -6.805  -1.149  18.106  1.00 20.93  ? 59  LYS B CG  1 
ATOM   4098 C  CD  . LYS B 1 59  ? -7.700  -1.930  19.026  1.00 22.23  ? 59  LYS B CD  1 
ATOM   4099 C  CE  . LYS B 1 59  ? -7.717  -3.381  18.613  1.00 22.19  ? 59  LYS B CE  1 
ATOM   4100 N  NZ  . LYS B 1 59  ? -8.550  -4.168  19.534  1.00 26.68  ? 59  LYS B NZ  1 
ATOM   4101 N  N   . GLU B 1 60  ? -4.524  -0.100  15.944  1.00 20.18  ? 60  GLU B N   1 
ATOM   4102 C  CA  . GLU B 1 60  ? -3.247  -0.578  15.433  1.00 19.90  ? 60  GLU B CA  1 
ATOM   4103 C  C   . GLU B 1 60  ? -2.446  0.582   14.838  1.00 20.58  ? 60  GLU B C   1 
ATOM   4104 O  O   . GLU B 1 60  ? -1.242  0.705   15.092  1.00 16.89  ? 60  GLU B O   1 
ATOM   4105 C  CB  . GLU B 1 60  ? -3.472  -1.657  14.390  1.00 22.23  ? 60  GLU B CB  1 
ATOM   4106 C  CG  . GLU B 1 60  ? -3.987  -2.951  14.966  1.00 26.61  ? 60  GLU B CG  1 
ATOM   4107 C  CD  . GLU B 1 60  ? -4.053  -4.044  13.906  1.00 31.31  ? 60  GLU B CD  1 
ATOM   4108 O  OE1 . GLU B 1 60  ? -3.015  -4.313  13.230  1.00 31.82  ? 60  GLU B OE1 1 
ATOM   4109 O  OE2 . GLU B 1 60  ? -5.146  -4.601  13.729  1.00 33.89  ? 60  GLU B OE2 1 
ATOM   4110 N  N   . ALA B 1 61  ? -3.116  1.452   14.057  1.00 17.93  ? 61  ALA B N   1 
ATOM   4111 C  CA  . ALA B 1 61  ? -2.424  2.579   13.457  1.00 17.18  ? 61  ALA B CA  1 
ATOM   4112 C  C   . ALA B 1 61  ? -1.799  3.464   14.537  1.00 15.89  ? 61  ALA B C   1 
ATOM   4113 O  O   . ALA B 1 61  ? -0.812  4.160   14.279  1.00 17.36  ? 61  ALA B O   1 
ATOM   4114 C  CB  . ALA B 1 61  ? -3.374  3.369   12.592  1.00 19.47  ? 61  ALA B CB  1 
ATOM   4115 N  N   . CYS B 1 62  ? -2.389  3.482   15.731  1.00 18.58  ? 62  CYS B N   1 
ATOM   4116 C  CA  . CYS B 1 62  ? -1.928  4.372   16.786  1.00 19.75  ? 62  CYS B CA  1 
ATOM   4117 C  C   . CYS B 1 62  ? -0.821  3.742   17.634  1.00 20.03  ? 62  CYS B C   1 
ATOM   4118 O  O   . CYS B 1 62  ? -0.416  4.353   18.621  1.00 21.41  ? 62  CYS B O   1 
ATOM   4119 C  CB  . CYS B 1 62  ? -3.061  4.760   17.724  1.00 21.30  ? 62  CYS B CB  1 
ATOM   4120 S  SG  . CYS B 1 62  ? -4.239  5.906   16.971  1.00 22.13  ? 62  CYS B SG  1 
ATOM   4121 N  N   . ASP B 1 63  ? -0.336  2.562   17.239  1.00 18.33  ? 63  ASP B N   1 
ATOM   4122 C  CA  . ASP B 1 63  ? 0.875   1.954   17.784  1.00 18.13  ? 63  ASP B CA  1 
ATOM   4123 C  C   . ASP B 1 63  ? 2.088   2.690   17.200  1.00 18.17  ? 63  ASP B C   1 
ATOM   4124 O  O   . ASP B 1 63  ? 2.414   2.587   15.999  1.00 18.07  ? 63  ASP B O   1 
ATOM   4125 C  CB  . ASP B 1 63  ? 0.822   0.424   17.550  1.00 21.52  ? 63  ASP B CB  1 
ATOM   4126 C  CG  . ASP B 1 63  ? 2.044   -0.360  18.022  1.00 24.14  ? 63  ASP B CG  1 
ATOM   4127 O  OD1 . ASP B 1 63  ? 3.048   0.296   18.340  1.00 22.66  ? 63  ASP B OD1 1 
ATOM   4128 O  OD2 . ASP B 1 63  ? 1.983   -1.638  18.075  1.00 25.04  ? 63  ASP B OD2 1 
ATOM   4129 N  N   . GLU B 1 64  ? 2.810   3.413   18.071  1.00 18.10  ? 64  GLU B N   1 
ATOM   4130 C  CA  . GLU B 1 64  ? 3.927   4.244   17.635  1.00 19.93  ? 64  GLU B CA  1 
ATOM   4131 C  C   . GLU B 1 64  ? 5.152   3.396   17.322  1.00 19.36  ? 64  GLU B C   1 
ATOM   4132 O  O   . GLU B 1 64  ? 6.122   3.911   16.769  1.00 19.11  ? 64  GLU B O   1 
ATOM   4133 C  CB  . GLU B 1 64  ? 4.298   5.274   18.697  1.00 23.40  ? 64  GLU B CB  1 
ATOM   4134 C  CG  . GLU B 1 64  ? 3.219   6.310   18.926  1.00 25.27  ? 64  GLU B CG  1 
ATOM   4135 C  CD  . GLU B 1 64  ? 3.488   7.133   20.171  1.00 28.16  ? 64  GLU B CD  1 
ATOM   4136 O  OE1 . GLU B 1 64  ? 3.147   6.668   21.277  1.00 31.41  ? 64  GLU B OE1 1 
ATOM   4137 O  OE2 . GLU B 1 64  ? 4.010   8.240   20.030  1.00 30.77  ? 64  GLU B OE2 1 
ATOM   4138 N  N   . SER B 1 65  ? 5.116   2.095   17.660  1.00 18.07  ? 65  SER B N   1 
ATOM   4139 C  CA  . SER B 1 65  ? 6.247   1.261   17.283  1.00 20.38  ? 65  SER B CA  1 
ATOM   4140 C  C   . SER B 1 65  ? 6.112   0.887   15.802  1.00 21.19  ? 65  SER B C   1 
ATOM   4141 O  O   . SER B 1 65  ? 7.118   0.610   15.163  1.00 20.87  ? 65  SER B O   1 
ATOM   4142 C  CB  . SER B 1 65  ? 6.383   0.066   18.196  1.00 22.54  ? 65  SER B CB  1 
ATOM   4143 O  OG  . SER B 1 65  ? 5.233   -0.752  18.113  1.00 23.22  ? 65  SER B OG  1 
ATOM   4144 N  N   . ARG B 1 66  ? 4.891   0.974   15.239  1.00 19.31  ? 66  ARG B N   1 
ATOM   4145 C  CA  . ARG B 1 66  ? 4.626   0.503   13.884  1.00 19.49  ? 66  ARG B CA  1 
ATOM   4146 C  C   . ARG B 1 66  ? 4.364   1.661   12.918  1.00 17.34  ? 66  ARG B C   1 
ATOM   4147 O  O   . ARG B 1 66  ? 4.531   1.491   11.731  1.00 17.60  ? 66  ARG B O   1 
ATOM   4148 C  CB  . ARG B 1 66  ? 3.441   -0.472  13.876  1.00 21.63  ? 66  ARG B CB  1 
ATOM   4149 C  CG  . ARG B 1 66  ? 3.656   -1.770  14.666  1.00 22.91  ? 66  ARG B CG  1 
ATOM   4150 C  CD  . ARG B 1 66  ? 2.368   -2.565  14.870  1.00 24.61  ? 66  ARG B CD  1 
ATOM   4151 N  NE  . ARG B 1 66  ? 1.773   -3.035  13.626  1.00 24.96  ? 66  ARG B NE  1 
ATOM   4152 C  CZ  . ARG B 1 66  ? 0.521   -3.472  13.467  1.00 24.92  ? 66  ARG B CZ  1 
ATOM   4153 N  NH1 . ARG B 1 66  ? -0.393  -3.292  14.400  1.00 23.46  ? 66  ARG B NH1 1 
ATOM   4154 N  NH2 . ARG B 1 66  ? 0.167   -4.050  12.336  1.00 24.60  ? 66  ARG B NH2 1 
ATOM   4155 N  N   . PHE B 1 67  ? 3.835   2.790   13.382  1.00 17.46  ? 67  PHE B N   1 
ATOM   4156 C  CA  . PHE B 1 67  ? 3.503   3.903   12.507  1.00 15.14  ? 67  PHE B CA  1 
ATOM   4157 C  C   . PHE B 1 67  ? 3.907   5.211   13.188  1.00 15.37  ? 67  PHE B C   1 
ATOM   4158 O  O   . PHE B 1 67  ? 3.814   5.343   14.406  1.00 15.47  ? 67  PHE B O   1 
ATOM   4159 C  CB  . PHE B 1 67  ? 2.007   3.978   12.212  1.00 15.33  ? 67  PHE B CB  1 
ATOM   4160 C  CG  . PHE B 1 67  ? 1.387   2.701   11.699  1.00 15.64  ? 67  PHE B CG  1 
ATOM   4161 C  CD1 . PHE B 1 67  ? 0.987   1.694   12.579  1.00 17.59  ? 67  PHE B CD1 1 
ATOM   4162 C  CD2 . PHE B 1 67  ? 1.249   2.489   10.337  1.00 16.66  ? 67  PHE B CD2 1 
ATOM   4163 C  CE1 . PHE B 1 67  ? 0.396   0.525   12.109  1.00 17.56  ? 67  PHE B CE1 1 
ATOM   4164 C  CE2 . PHE B 1 67  ? 0.724   1.293   9.863   1.00 17.72  ? 67  PHE B CE2 1 
ATOM   4165 C  CZ  . PHE B 1 67  ? 0.318   0.310   10.749  1.00 17.49  ? 67  PHE B CZ  1 
ATOM   4166 N  N   . ASP B 1 68  ? 4.297   6.191   12.378  1.00 16.59  ? 68  ASP B N   1 
ATOM   4167 C  CA  . ASP B 1 68  ? 4.680   7.512   12.852  1.00 16.51  ? 68  ASP B CA  1 
ATOM   4168 C  C   . ASP B 1 68  ? 3.832   8.540   12.109  1.00 17.42  ? 68  ASP B C   1 
ATOM   4169 O  O   . ASP B 1 68  ? 3.204   8.224   11.081  1.00 17.37  ? 68  ASP B O   1 
ATOM   4170 C  CB  . ASP B 1 68  ? 6.176   7.741   12.624  1.00 17.14  ? 68  ASP B CB  1 
ATOM   4171 C  CG  . ASP B 1 68  ? 6.710   9.114   13.045  1.00 20.14  ? 68  ASP B CG  1 
ATOM   4172 O  OD1 . ASP B 1 68  ? 6.063   9.775   13.898  1.00 18.48  ? 68  ASP B OD1 1 
ATOM   4173 O  OD2 . ASP B 1 68  ? 7.790   9.504   12.526  1.00 26.85  ? 68  ASP B OD2 1 
ATOM   4174 N  N   . LYS B 1 69  ? 3.823   9.776   12.604  1.00 16.71  ? 69  LYS B N   1 
ATOM   4175 C  CA  . LYS B 1 69  ? 3.019   10.806  11.974  1.00 15.91  ? 69  LYS B CA  1 
ATOM   4176 C  C   . LYS B 1 69  ? 3.559   11.078  10.574  1.00 16.26  ? 69  LYS B C   1 
ATOM   4177 O  O   . LYS B 1 69  ? 4.779   11.168  10.393  1.00 17.86  ? 69  LYS B O   1 
ATOM   4178 C  CB  . LYS B 1 69  ? 3.035   12.101  12.771  1.00 15.32  ? 69  LYS B CB  1 
ATOM   4179 C  CG  . LYS B 1 69  ? 2.589   13.309  11.973  1.00 17.06  ? 69  LYS B CG  1 
ATOM   4180 C  CD  . LYS B 1 69  ? 2.298   14.503  12.846  1.00 17.00  ? 69  LYS B CD  1 
ATOM   4181 C  CE  . LYS B 1 69  ? 2.285   15.798  12.058  1.00 17.94  ? 69  LYS B CE  1 
ATOM   4182 N  NZ  . LYS B 1 69  ? 1.441   16.812  12.738  1.00 17.20  ? 69  LYS B NZ  1 
ATOM   4183 N  N   . ASN B 1 70  ? 2.635   11.140  9.608   1.00 15.46  ? 70  ASN B N   1 
ATOM   4184 C  CA  . ASN B 1 70  ? 2.931   11.541  8.244   1.00 17.16  ? 70  ASN B CA  1 
ATOM   4185 C  C   . ASN B 1 70  ? 2.443   12.968  8.008   1.00 16.11  ? 70  ASN B C   1 
ATOM   4186 O  O   . ASN B 1 70  ? 1.508   13.405  8.653   1.00 15.74  ? 70  ASN B O   1 
ATOM   4187 C  CB  . ASN B 1 70  ? 2.292   10.574  7.248   1.00 17.83  ? 70  ASN B CB  1 
ATOM   4188 C  CG  . ASN B 1 70  ? 2.631   10.897  5.807   1.00 20.31  ? 70  ASN B CG  1 
ATOM   4189 O  OD1 . ASN B 1 70  ? 3.797   11.051  5.441   1.00 17.22  ? 70  ASN B OD1 1 
ATOM   4190 N  ND2 . ASN B 1 70  ? 1.598   11.052  4.993   1.00 22.29  ? 70  ASN B ND2 1 
ATOM   4191 N  N   . LEU B 1 71  ? 3.109   13.696  7.107   1.00 17.71  ? 71  LEU B N   1 
ATOM   4192 C  CA  . LEU B 1 71  ? 2.613   14.996  6.666   1.00 21.27  ? 71  LEU B CA  1 
ATOM   4193 C  C   . LEU B 1 71  ? 1.772   14.754  5.403   1.00 23.81  ? 71  LEU B C   1 
ATOM   4194 O  O   . LEU B 1 71  ? 2.298   14.383  4.365   1.00 26.04  ? 71  LEU B O   1 
ATOM   4195 C  CB  . LEU B 1 71  ? 3.763   15.966  6.366   1.00 21.00  ? 71  LEU B CB  1 
ATOM   4196 C  CG  . LEU B 1 71  ? 4.752   16.264  7.491   1.00 21.91  ? 71  LEU B CG  1 
ATOM   4197 C  CD1 . LEU B 1 71  ? 5.670   17.432  7.112   1.00 25.91  ? 71  LEU B CD1 1 
ATOM   4198 C  CD2 . LEU B 1 71  ? 4.042   16.578  8.786   1.00 22.80  ? 71  LEU B CD2 1 
ATOM   4199 N  N   . SER B 1 72  ? 0.463   14.942  5.536   1.00 26.00  ? 72  SER B N   1 
ATOM   4200 C  CA  . SER B 1 72  ? -0.423  14.941  4.395   1.00 27.59  ? 72  SER B CA  1 
ATOM   4201 C  C   . SER B 1 72  ? -0.006  16.032  3.416   1.00 30.06  ? 72  SER B C   1 
ATOM   4202 O  O   . SER B 1 72  ? 0.719   16.968  3.768   1.00 27.12  ? 72  SER B O   1 
ATOM   4203 C  CB  . SER B 1 72  ? -1.830  15.092  4.836   1.00 26.33  ? 72  SER B CB  1 
ATOM   4204 O  OG  . SER B 1 72  ? -2.084  16.396  5.311   1.00 28.30  ? 72  SER B OG  1 
ATOM   4205 N  N   . GLN B 1 73  ? -0.476  15.894  2.165   1.00 32.72  ? 73  GLN B N   1 
ATOM   4206 C  CA  . GLN B 1 73  ? -0.179  16.886  1.143   1.00 32.92  ? 73  GLN B CA  1 
ATOM   4207 C  C   . GLN B 1 73  ? -0.511  18.289  1.649   1.00 26.34  ? 73  GLN B C   1 
ATOM   4208 O  O   . GLN B 1 73  ? 0.228   19.230  1.400   1.00 27.54  ? 73  GLN B O   1 
ATOM   4209 C  CB  . GLN B 1 73  ? -0.969  16.569  -0.127  1.00 39.28  ? 73  GLN B CB  1 
ATOM   4210 C  CG  . GLN B 1 73  ? -0.514  17.397  -1.321  1.00 46.87  ? 73  GLN B CG  1 
ATOM   4211 C  CD  . GLN B 1 73  ? 0.930   17.128  -1.675  1.00 47.83  ? 73  GLN B CD  1 
ATOM   4212 O  OE1 . GLN B 1 73  ? 1.824   17.927  -1.378  1.00 39.92  ? 73  GLN B OE1 1 
ATOM   4213 N  NE2 . GLN B 1 73  ? 1.160   15.974  -2.293  1.00 49.01  ? 73  GLN B NE2 1 
ATOM   4214 N  N   . GLY B 1 74  ? -1.664  18.444  2.306   1.00 28.31  ? 74  GLY B N   1 
ATOM   4215 C  CA  . GLY B 1 74  ? -2.069  19.717  2.882   1.00 27.81  ? 74  GLY B CA  1 
ATOM   4216 C  C   . GLY B 1 74  ? -1.041  20.257  3.870   1.00 28.93  ? 74  GLY B C   1 
ATOM   4217 O  O   . GLY B 1 74  ? -0.659  21.433  3.787   1.00 28.89  ? 74  GLY B O   1 
ATOM   4218 N  N   . LEU B 1 75  ? -0.567  19.378  4.777   1.00 26.22  ? 75  LEU B N   1 
ATOM   4219 C  CA  . LEU B 1 75  ? 0.386   19.814  5.782   1.00 25.64  ? 75  LEU B CA  1 
ATOM   4220 C  C   . LEU B 1 75  ? 1.731   20.151  5.133   1.00 22.85  ? 75  LEU B C   1 
ATOM   4221 O  O   . LEU B 1 75  ? 2.415   21.037  5.626   1.00 22.62  ? 75  LEU B O   1 
ATOM   4222 C  CB  . LEU B 1 75  ? 0.584   18.761  6.880   1.00 24.48  ? 75  LEU B CB  1 
ATOM   4223 C  CG  . LEU B 1 75  ? -0.334  18.845  8.096   1.00 28.77  ? 75  LEU B CG  1 
ATOM   4224 C  CD1 . LEU B 1 75  ? 0.148   17.871  9.191   1.00 29.81  ? 75  LEU B CD1 1 
ATOM   4225 C  CD2 . LEU B 1 75  ? -0.452  20.261  8.627   1.00 29.93  ? 75  LEU B CD2 1 
ATOM   4226 N  N   . LYS B 1 76  ? 2.128   19.400  4.093   1.00 23.41  ? 76  LYS B N   1 
ATOM   4227 C  CA  . LYS B 1 76  ? 3.326   19.679  3.319   1.00 25.75  ? 76  LYS B CA  1 
ATOM   4228 C  C   . LYS B 1 76  ? 3.277   21.089  2.732   1.00 25.51  ? 76  LYS B C   1 
ATOM   4229 O  O   . LYS B 1 76  ? 4.302   21.762  2.636   1.00 26.22  ? 76  LYS B O   1 
ATOM   4230 C  CB  . LYS B 1 76  ? 3.496   18.708  2.141   1.00 27.67  ? 76  LYS B CB  1 
ATOM   4231 C  CG  . LYS B 1 76  ? 4.150   17.380  2.477   1.00 31.77  ? 76  LYS B CG  1 
ATOM   4232 C  CD  . LYS B 1 76  ? 4.318   16.518  1.245   1.00 35.22  ? 76  LYS B CD  1 
ATOM   4233 C  CE  . LYS B 1 76  ? 4.500   15.047  1.555   1.00 38.05  ? 76  LYS B CE  1 
ATOM   4234 N  NZ  . LYS B 1 76  ? 5.893   14.772  1.954   1.00 40.32  ? 76  LYS B NZ  1 
ATOM   4235 N  N   . PHE B 1 77  ? 2.097   21.531  2.290   1.00 26.47  ? 77  PHE B N   1 
ATOM   4236 C  CA  . PHE B 1 77  ? 2.001   22.864  1.730   1.00 28.33  ? 77  PHE B CA  1 
ATOM   4237 C  C   . PHE B 1 77  ? 1.985   23.897  2.864   1.00 27.94  ? 77  PHE B C   1 
ATOM   4238 O  O   . PHE B 1 77  ? 2.555   24.979  2.688   1.00 25.11  ? 77  PHE B O   1 
ATOM   4239 C  CB  . PHE B 1 77  ? 0.785   22.987  0.807   1.00 32.24  ? 77  PHE B CB  1 
ATOM   4240 C  CG  . PHE B 1 77  ? 0.902   22.281  -0.523  1.00 33.54  ? 77  PHE B CG  1 
ATOM   4241 C  CD1 . PHE B 1 77  ? 2.103   22.223  -1.210  1.00 35.57  ? 77  PHE B CD1 1 
ATOM   4242 C  CD2 . PHE B 1 77  ? -0.221  21.752  -1.129  1.00 33.65  ? 77  PHE B CD2 1 
ATOM   4243 C  CE1 . PHE B 1 77  ? 2.192   21.606  -2.447  1.00 36.65  ? 77  PHE B CE1 1 
ATOM   4244 C  CE2 . PHE B 1 77  ? -0.129  21.126  -2.360  1.00 34.69  ? 77  PHE B CE2 1 
ATOM   4245 C  CZ  . PHE B 1 77  ? 1.077   21.045  -3.012  1.00 36.00  ? 77  PHE B CZ  1 
ATOM   4246 N  N   . VAL B 1 78  ? 1.389   23.533  4.027   1.00 24.20  ? 78  VAL B N   1 
ATOM   4247 C  CA  . VAL B 1 78  ? 1.404   24.376  5.214   1.00 23.86  ? 78  VAL B CA  1 
ATOM   4248 C  C   . VAL B 1 78  ? 2.854   24.671  5.613   1.00 23.74  ? 78  VAL B C   1 
ATOM   4249 O  O   . VAL B 1 78  ? 3.191   25.766  6.012   1.00 24.52  ? 78  VAL B O   1 
ATOM   4250 C  CB  . VAL B 1 78  ? 0.602   23.751  6.357   1.00 24.28  ? 78  VAL B CB  1 
ATOM   4251 C  CG1 . VAL B 1 78  ? 0.846   24.443  7.680   1.00 25.51  ? 78  VAL B CG1 1 
ATOM   4252 C  CG2 . VAL B 1 78  ? -0.887  23.731  6.049   1.00 26.52  ? 78  VAL B CG2 1 
ATOM   4253 N  N   . ARG B 1 79  ? 3.724   23.700  5.408   1.00 23.76  ? 79  ARG B N   1 
ATOM   4254 C  CA  . ARG B 1 79  ? 5.119   23.805  5.774   1.00 24.70  ? 79  ARG B CA  1 
ATOM   4255 C  C   . ARG B 1 79  ? 5.802   24.955  5.038   1.00 25.57  ? 79  ARG B C   1 
ATOM   4256 O  O   . ARG B 1 79  ? 6.825   25.461  5.500   1.00 25.44  ? 79  ARG B O   1 
ATOM   4257 C  CB  . ARG B 1 79  ? 5.754   22.451  5.474   1.00 25.93  ? 79  ARG B CB  1 
ATOM   4258 C  CG  . ARG B 1 79  ? 7.191   22.289  5.914   1.00 26.87  ? 79  ARG B CG  1 
ATOM   4259 C  CD  . ARG B 1 79  ? 7.540   20.810  5.864   1.00 28.43  ? 79  ARG B CD  1 
ATOM   4260 N  NE  . ARG B 1 79  ? 8.988   20.693  5.911   1.00 28.43  ? 79  ARG B NE  1 
ATOM   4261 C  CZ  . ARG B 1 79  ? 9.710   20.288  6.951   1.00 28.75  ? 79  ARG B CZ  1 
ATOM   4262 N  NH1 . ARG B 1 79  ? 9.146   19.745  8.021   1.00 28.66  ? 79  ARG B NH1 1 
ATOM   4263 N  NH2 . ARG B 1 79  ? 11.019  20.417  6.894   1.00 29.51  ? 79  ARG B NH2 1 
ATOM   4264 N  N   . ASP B 1 80  ? 5.231   25.403  3.909   1.00 27.88  ? 80  ASP B N   1 
ATOM   4265 C  CA  . ASP B 1 80  ? 5.812   26.532  3.194   1.00 28.64  ? 80  ASP B CA  1 
ATOM   4266 C  C   . ASP B 1 80  ? 5.838   27.813  4.023   1.00 26.62  ? 80  ASP B C   1 
ATOM   4267 O  O   . ASP B 1 80  ? 6.701   28.657  3.790   1.00 28.42  ? 80  ASP B O   1 
ATOM   4268 C  CB  . ASP B 1 80  ? 5.145   26.759  1.840   1.00 31.88  ? 80  ASP B CB  1 
ATOM   4269 C  CG  . ASP B 1 80  ? 5.504   25.636  0.887   1.00 35.88  ? 80  ASP B CG  1 
ATOM   4270 O  OD1 . ASP B 1 80  ? 6.683   25.179  0.948   1.00 34.68  ? 80  ASP B OD1 1 
ATOM   4271 O  OD2 . ASP B 1 80  ? 4.601   25.214  0.112   1.00 43.05  ? 80  ASP B OD2 1 
ATOM   4272 N  N   . PHE B 1 81  ? 4.948   27.960  5.007   1.00 25.89  ? 81  PHE B N   1 
ATOM   4273 C  CA  . PHE B 1 81  ? 5.066   29.082  5.930   1.00 24.31  ? 81  PHE B CA  1 
ATOM   4274 C  C   . PHE B 1 81  ? 5.252   28.676  7.395   1.00 23.10  ? 81  PHE B C   1 
ATOM   4275 O  O   . PHE B 1 81  ? 5.775   29.474  8.166   1.00 27.13  ? 81  PHE B O   1 
ATOM   4276 C  CB  . PHE B 1 81  ? 3.865   30.013  5.771   1.00 24.33  ? 81  PHE B CB  1 
ATOM   4277 C  CG  . PHE B 1 81  ? 2.499   29.441  6.040   1.00 24.07  ? 81  PHE B CG  1 
ATOM   4278 C  CD1 . PHE B 1 81  ? 1.974   29.437  7.324   1.00 25.63  ? 81  PHE B CD1 1 
ATOM   4279 C  CD2 . PHE B 1 81  ? 1.689   29.025  4.998   1.00 24.61  ? 81  PHE B CD2 1 
ATOM   4280 C  CE1 . PHE B 1 81  ? 0.683   28.984  7.570   1.00 27.62  ? 81  PHE B CE1 1 
ATOM   4281 C  CE2 . PHE B 1 81  ? 0.400   28.565  5.242   1.00 23.59  ? 81  PHE B CE2 1 
ATOM   4282 C  CZ  . PHE B 1 81  ? -0.099  28.549  6.524   1.00 25.74  ? 81  PHE B CZ  1 
ATOM   4283 N  N   . ALA B 1 82  ? 4.818   27.468  7.788   1.00 24.39  ? 82  ALA B N   1 
ATOM   4284 C  CA  . ALA B 1 82  ? 4.938   26.995  9.165   1.00 21.94  ? 82  ALA B CA  1 
ATOM   4285 C  C   . ALA B 1 82  ? 6.219   26.188  9.346   1.00 21.57  ? 82  ALA B C   1 
ATOM   4286 O  O   . ALA B 1 82  ? 6.569   25.822  10.465  1.00 24.51  ? 82  ALA B O   1 
ATOM   4287 C  CB  . ALA B 1 82  ? 3.735   26.169  9.529   1.00 20.87  ? 82  ALA B CB  1 
ATOM   4288 N  N   . GLY B 1 83  ? 6.914   25.901  8.244   1.00 20.41  ? 83  GLY B N   1 
ATOM   4289 C  CA  . GLY B 1 83  ? 8.261   25.340  8.303   1.00 21.71  ? 83  GLY B CA  1 
ATOM   4290 C  C   . GLY B 1 83  ? 8.323   24.129  9.241   1.00 20.84  ? 83  GLY B C   1 
ATOM   4291 O  O   . GLY B 1 83  ? 7.450   23.239  9.186   1.00 20.11  ? 83  GLY B O   1 
ATOM   4292 N  N   . ASP B 1 84  ? 9.374   24.096  10.077  1.00 19.12  ? 84  ASP B N   1 
ATOM   4293 C  CA  . ASP B 1 84  ? 9.569   22.984  10.973  1.00 19.35  ? 84  ASP B CA  1 
ATOM   4294 C  C   . ASP B 1 84  ? 9.078   23.354  12.367  1.00 18.20  ? 84  ASP B C   1 
ATOM   4295 O  O   . ASP B 1 84  ? 9.620   22.868  13.357  1.00 16.68  ? 84  ASP B O   1 
ATOM   4296 C  CB  . ASP B 1 84  ? 10.995  22.426  10.877  1.00 24.20  ? 84  ASP B CB  1 
ATOM   4297 C  CG  . ASP B 1 84  ? 12.154  23.341  11.246  1.00 26.10  ? 84  ASP B CG  1 
ATOM   4298 O  OD1 . ASP B 1 84  ? 11.948  24.581  11.384  1.00 22.18  ? 84  ASP B OD1 1 
ATOM   4299 O  OD2 . ASP B 1 84  ? 13.281  22.767  11.418  1.00 25.44  ? 84  ASP B OD2 1 
ATOM   4300 N  N   . GLY B 1 85  ? 8.018   24.189  12.428  1.00 16.34  ? 85  GLY B N   1 
ATOM   4301 C  CA  . GLY B 1 85  ? 7.183   24.297  13.616  1.00 15.20  ? 85  GLY B CA  1 
ATOM   4302 C  C   . GLY B 1 85  ? 6.643   22.924  14.020  1.00 14.94  ? 85  GLY B C   1 
ATOM   4303 O  O   . GLY B 1 85  ? 6.845   21.963  13.276  1.00 14.85  ? 85  GLY B O   1 
ATOM   4304 N  N   . LEU B 1 86  ? 6.065   22.824  15.233  1.00 15.45  ? 86  LEU B N   1 
ATOM   4305 C  CA  . LEU B 1 86  ? 5.724   21.531  15.812  1.00 16.29  ? 86  LEU B CA  1 
ATOM   4306 C  C   . LEU B 1 86  ? 4.702   20.771  14.955  1.00 17.11  ? 86  LEU B C   1 
ATOM   4307 O  O   . LEU B 1 86  ? 4.746   19.547  14.966  1.00 17.07  ? 86  LEU B O   1 
ATOM   4308 C  CB  . LEU B 1 86  ? 5.157   21.669  17.228  1.00 15.20  ? 86  LEU B CB  1 
ATOM   4309 C  CG  . LEU B 1 86  ? 6.119   21.823  18.408  1.00 16.27  ? 86  LEU B CG  1 
ATOM   4310 C  CD1 . LEU B 1 86  ? 5.343   22.055  19.683  1.00 15.05  ? 86  LEU B CD1 1 
ATOM   4311 C  CD2 . LEU B 1 86  ? 7.037   20.621  18.587  1.00 16.84  ? 86  LEU B CD2 1 
ATOM   4312 N  N   . VAL B 1 87  ? 3.739   21.452  14.304  1.00 17.81  ? 87  VAL B N   1 
ATOM   4313 C  CA  . VAL B 1 87  ? 2.682   20.755  13.580  1.00 17.15  ? 87  VAL B CA  1 
ATOM   4314 C  C   . VAL B 1 87  ? 3.209   20.162  12.265  1.00 16.72  ? 87  VAL B C   1 
ATOM   4315 O  O   . VAL B 1 87  ? 2.770   19.090  11.842  1.00 14.89  ? 87  VAL B O   1 
ATOM   4316 C  CB  . VAL B 1 87  ? 1.470   21.670  13.333  1.00 18.96  ? 87  VAL B CB  1 
ATOM   4317 C  CG1 . VAL B 1 87  ? 0.469   21.050  12.377  1.00 18.55  ? 87  VAL B CG1 1 
ATOM   4318 C  CG2 . VAL B 1 87  ? 0.774   22.042  14.634  1.00 22.76  ? 87  VAL B CG2 1 
ATOM   4319 N  N   . THR B 1 88  ? 4.161   20.856  11.631  1.00 16.08  ? 88  THR B N   1 
ATOM   4320 C  CA  . THR B 1 88  ? 4.552   20.550  10.264  1.00 16.20  ? 88  THR B CA  1 
ATOM   4321 C  C   . THR B 1 88  ? 5.975   19.999  10.234  1.00 15.28  ? 88  THR B C   1 
ATOM   4322 O  O   . THR B 1 88  ? 6.567   19.886  9.168   1.00 17.60  ? 88  THR B O   1 
ATOM   4323 C  CB  . THR B 1 88  ? 4.413   21.796  9.370   1.00 18.36  ? 88  THR B CB  1 
ATOM   4324 O  OG1 . THR B 1 88  ? 5.055   22.902  9.987   1.00 15.55  ? 88  THR B OG1 1 
ATOM   4325 C  CG2 . THR B 1 88  ? 2.971   22.171  9.110   1.00 18.35  ? 88  THR B CG2 1 
ATOM   4326 N  N   . SER B 1 89  ? 6.506   19.598  11.388  1.00 14.82  ? 89  SER B N   1 
ATOM   4327 C  CA  . SER B 1 89  ? 7.785   18.885  11.435  1.00 16.78  ? 89  SER B CA  1 
ATOM   4328 C  C   . SER B 1 89  ? 7.546   17.370  11.434  1.00 14.81  ? 89  SER B C   1 
ATOM   4329 O  O   . SER B 1 89  ? 6.517   16.889  11.867  1.00 13.79  ? 89  SER B O   1 
ATOM   4330 C  CB  . SER B 1 89  ? 8.601   19.334  12.635  1.00 17.36  ? 89  SER B CB  1 
ATOM   4331 O  OG  . SER B 1 89  ? 7.794   19.217  13.807  1.00 21.34  ? 89  SER B OG  1 
ATOM   4332 N  N   . TRP B 1 90  ? 8.495   16.634  10.859  1.00 16.93  ? 90  TRP B N   1 
ATOM   4333 C  CA  . TRP B 1 90  ? 8.581   15.184  10.984  1.00 17.09  ? 90  TRP B CA  1 
ATOM   4334 C  C   . TRP B 1 90  ? 9.164   14.856  12.356  1.00 16.09  ? 90  TRP B C   1 
ATOM   4335 O  O   . TRP B 1 90  ? 10.040  15.574  12.837  1.00 17.21  ? 90  TRP B O   1 
ATOM   4336 C  CB  . TRP B 1 90  ? 9.485   14.619  9.870   1.00 17.74  ? 90  TRP B CB  1 
ATOM   4337 C  CG  . TRP B 1 90  ? 9.064   15.003  8.469   1.00 17.75  ? 90  TRP B CG  1 
ATOM   4338 C  CD1 . TRP B 1 90  ? 9.480   16.055  7.689   1.00 18.26  ? 90  TRP B CD1 1 
ATOM   4339 C  CD2 . TRP B 1 90  ? 8.134   14.250  7.669   1.00 18.12  ? 90  TRP B CD2 1 
ATOM   4340 N  NE1 . TRP B 1 90  ? 8.816   16.040  6.482   1.00 20.18  ? 90  TRP B NE1 1 
ATOM   4341 C  CE2 . TRP B 1 90  ? 8.004   14.928  6.436   1.00 19.29  ? 90  TRP B CE2 1 
ATOM   4342 C  CE3 . TRP B 1 90  ? 7.420   13.068  7.889   1.00 18.15  ? 90  TRP B CE3 1 
ATOM   4343 C  CZ2 . TRP B 1 90  ? 7.168   14.447  5.428   1.00 21.27  ? 90  TRP B CZ2 1 
ATOM   4344 C  CZ3 . TRP B 1 90  ? 6.627   12.574  6.875   1.00 20.21  ? 90  TRP B CZ3 1 
ATOM   4345 C  CH2 . TRP B 1 90  ? 6.486   13.271  5.672   1.00 19.02  ? 90  TRP B CH2 1 
ATOM   4346 N  N   . THR B 1 91  ? 8.739   13.733  12.930  1.00 14.30  ? 91  THR B N   1 
ATOM   4347 C  CA  . THR B 1 91  ? 9.185   13.272  14.232  1.00 15.12  ? 91  THR B CA  1 
ATOM   4348 C  C   . THR B 1 91  ? 10.708  13.118  14.281  1.00 15.95  ? 91  THR B C   1 
ATOM   4349 O  O   . THR B 1 91  ? 11.310  13.361  15.320  1.00 16.86  ? 91  THR B O   1 
ATOM   4350 C  CB  . THR B 1 91  ? 8.488   11.965  14.589  1.00 15.40  ? 91  THR B CB  1 
ATOM   4351 O  OG1 . THR B 1 91  ? 7.078   12.152  14.415  1.00 14.35  ? 91  THR B OG1 1 
ATOM   4352 C  CG2 . THR B 1 91  ? 8.828   11.492  15.986  1.00 15.06  ? 91  THR B CG2 1 
ATOM   4353 N  N   . HIS B 1 92  ? 11.328  12.735  13.153  1.00 14.80  ? 92  HIS B N   1 
ATOM   4354 C  CA  . HIS B 1 92  ? 12.747  12.432  13.087  1.00 16.34  ? 92  HIS B CA  1 
ATOM   4355 C  C   . HIS B 1 92  ? 13.570  13.701  12.855  1.00 16.27  ? 92  HIS B C   1 
ATOM   4356 O  O   . HIS B 1 92  ? 14.792  13.633  12.867  1.00 16.56  ? 92  HIS B O   1 
ATOM   4357 C  CB  . HIS B 1 92  ? 12.959  11.345  12.028  1.00 19.31  ? 92  HIS B CB  1 
ATOM   4358 C  CG  . HIS B 1 92  ? 12.424  11.739  10.675  1.00 18.54  ? 92  HIS B CG  1 
ATOM   4359 N  ND1 . HIS B 1 92  ? 12.976  12.755  9.925   1.00 17.77  ? 92  HIS B ND1 1 
ATOM   4360 C  CD2 . HIS B 1 92  ? 11.340  11.307  9.988   1.00 17.52  ? 92  HIS B CD2 1 
ATOM   4361 C  CE1 . HIS B 1 92  ? 12.298  12.875  8.785   1.00 18.45  ? 92  HIS B CE1 1 
ATOM   4362 N  NE2 . HIS B 1 92  ? 11.291  12.016  8.794   1.00 17.36  ? 92  HIS B NE2 1 
ATOM   4363 N  N   . GLU B 1 93  ? 12.934  14.864  12.609  1.00 16.44  ? 93  GLU B N   1 
ATOM   4364 C  CA  . GLU B 1 93  ? 13.665  16.126  12.505  1.00 18.81  ? 93  GLU B CA  1 
ATOM   4365 C  C   . GLU B 1 93  ? 14.107  16.576  13.898  1.00 16.32  ? 93  GLU B C   1 
ATOM   4366 O  O   . GLU B 1 93  ? 13.361  16.473  14.855  1.00 15.95  ? 93  GLU B O   1 
ATOM   4367 C  CB  . GLU B 1 93  ? 12.808  17.229  11.883  1.00 18.98  ? 93  GLU B CB  1 
ATOM   4368 C  CG  . GLU B 1 93  ? 12.660  17.131  10.378  1.00 22.02  ? 93  GLU B CG  1 
ATOM   4369 C  CD  . GLU B 1 93  ? 11.749  18.192  9.770   1.00 25.41  ? 93  GLU B CD  1 
ATOM   4370 O  OE1 . GLU B 1 93  ? 10.521  18.205  10.059  1.00 25.24  ? 93  GLU B OE1 1 
ATOM   4371 O  OE2 . GLU B 1 93  ? 12.267  18.999  9.014   1.00 25.96  ? 93  GLU B OE2 1 
ATOM   4372 N  N   . LYS B 1 94  ? 15.374  16.999  14.012  1.00 17.94  ? 94  LYS B N   1 
ATOM   4373 C  CA  . LYS B 1 94  ? 15.937  17.430  15.283  1.00 17.20  ? 94  LYS B CA  1 
ATOM   4374 C  C   . LYS B 1 94  ? 15.061  18.492  15.934  1.00 14.96  ? 94  LYS B C   1 
ATOM   4375 O  O   . LYS B 1 94  ? 14.888  18.512  17.160  1.00 15.49  ? 94  LYS B O   1 
ATOM   4376 C  CB  . LYS B 1 94  ? 17.334  18.038  15.063  1.00 19.43  ? 94  LYS B CB  1 
ATOM   4377 C  CG  . LYS B 1 94  ? 18.063  18.458  16.328  1.00 21.13  ? 94  LYS B CG  1 
ATOM   4378 C  CD  . LYS B 1 94  ? 19.506  18.822  16.076  1.00 25.43  ? 94  LYS B CD  1 
ATOM   4379 C  CE  . LYS B 1 94  ? 20.188  19.340  17.319  1.00 30.89  ? 94  LYS B CE  1 
ATOM   4380 N  NZ  . LYS B 1 94  ? 21.638  19.518  17.090  1.00 34.03  ? 94  LYS B NZ  1 
ATOM   4381 N  N   . ASN B 1 95  ? 14.523  19.395  15.123  1.00 15.31  ? 95  ASN B N   1 
ATOM   4382 C  CA  . ASN B 1 95  ? 13.760  20.516  15.664  1.00 16.03  ? 95  ASN B CA  1 
ATOM   4383 C  C   . ASN B 1 95  ? 12.414  20.077  16.226  1.00 15.66  ? 95  ASN B C   1 
ATOM   4384 O  O   . ASN B 1 95  ? 11.827  20.833  17.013  1.00 15.52  ? 95  ASN B O   1 
ATOM   4385 C  CB  . ASN B 1 95  ? 13.580  21.652  14.655  1.00 17.04  ? 95  ASN B CB  1 
ATOM   4386 C  CG  . ASN B 1 95  ? 14.777  22.593  14.636  1.00 17.48  ? 95  ASN B CG  1 
ATOM   4387 O  OD1 . ASN B 1 95  ? 15.499  22.729  15.611  1.00 22.24  ? 95  ASN B OD1 1 
ATOM   4388 N  ND2 . ASN B 1 95  ? 15.020  23.223  13.518  1.00 18.56  ? 95  ASN B ND2 1 
ATOM   4389 N  N   . TRP B 1 96  ? 11.933  18.873  15.878  1.00 15.31  ? 96  TRP B N   1 
ATOM   4390 C  CA  . TRP B 1 96  ? 10.668  18.464  16.478  1.00 14.07  ? 96  TRP B CA  1 
ATOM   4391 C  C   . TRP B 1 96  ? 10.878  18.189  17.966  1.00 13.86  ? 96  TRP B C   1 
ATOM   4392 O  O   . TRP B 1 96  ? 10.259  18.807  18.818  1.00 15.23  ? 96  TRP B O   1 
ATOM   4393 C  CB  . TRP B 1 96  ? 9.977   17.291  15.780  1.00 13.43  ? 96  TRP B CB  1 
ATOM   4394 C  CG  . TRP B 1 96  ? 8.772   16.936  16.593  1.00 13.35  ? 96  TRP B CG  1 
ATOM   4395 C  CD1 . TRP B 1 96  ? 7.588   17.617  16.673  1.00 13.06  ? 96  TRP B CD1 1 
ATOM   4396 C  CD2 . TRP B 1 96  ? 8.729   15.930  17.607  1.00 14.12  ? 96  TRP B CD2 1 
ATOM   4397 N  NE1 . TRP B 1 96  ? 6.825   17.114  17.684  1.00 14.88  ? 96  TRP B NE1 1 
ATOM   4398 C  CE2 . TRP B 1 96  ? 7.482   16.045  18.250  1.00 14.47  ? 96  TRP B CE2 1 
ATOM   4399 C  CE3 . TRP B 1 96  ? 9.593   14.911  17.999  1.00 14.36  ? 96  TRP B CE3 1 
ATOM   4400 C  CZ2 . TRP B 1 96  ? 7.105   15.186  19.273  1.00 14.03  ? 96  TRP B CZ2 1 
ATOM   4401 C  CZ3 . TRP B 1 96  ? 9.209   14.072  19.022  1.00 14.88  ? 96  TRP B CZ3 1 
ATOM   4402 C  CH2 . TRP B 1 96  ? 8.010   14.237  19.673  1.00 15.43  ? 96  TRP B CH2 1 
ATOM   4403 N  N   . LYS B 1 97  ? 11.739  17.234  18.303  1.00 15.50  ? 97  LYS B N   1 
ATOM   4404 C  CA  . LYS B 1 97  ? 11.858  16.806  19.685  1.00 17.28  ? 97  LYS B CA  1 
ATOM   4405 C  C   . LYS B 1 97  ? 12.388  17.946  20.550  1.00 15.24  ? 97  LYS B C   1 
ATOM   4406 O  O   . LYS B 1 97  ? 12.047  18.027  21.718  1.00 14.85  ? 97  LYS B O   1 
ATOM   4407 C  CB  . LYS B 1 97  ? 12.799  15.596  19.830  1.00 17.69  ? 97  LYS B CB  1 
ATOM   4408 C  CG  . LYS B 1 97  ? 12.813  14.979  21.216  1.00 19.19  ? 97  LYS B CG  1 
ATOM   4409 C  CD  . LYS B 1 97  ? 11.455  14.427  21.628  1.00 21.86  ? 97  LYS B CD  1 
ATOM   4410 C  CE  . LYS B 1 97  ? 11.396  13.768  22.983  1.00 23.92  ? 97  LYS B CE  1 
ATOM   4411 N  NZ  . LYS B 1 97  ? 12.068  12.463  22.982  1.00 27.50  ? 97  LYS B NZ  1 
ATOM   4412 N  N   . LYS B 1 98  ? 13.288  18.753  19.993  1.00 14.19  ? 98  LYS B N   1 
ATOM   4413 C  CA  . LYS B 1 98  ? 13.825  19.925  20.668  1.00 15.87  ? 98  LYS B CA  1 
ATOM   4414 C  C   . LYS B 1 98  ? 12.689  20.843  21.077  1.00 12.89  ? 98  LYS B C   1 
ATOM   4415 O  O   . LYS B 1 98  ? 12.528  21.212  22.234  1.00 14.49  ? 98  LYS B O   1 
ATOM   4416 C  CB  . LYS B 1 98  ? 14.755  20.668  19.713  1.00 18.91  ? 98  LYS B CB  1 
ATOM   4417 C  CG  . LYS B 1 98  ? 15.947  21.389  20.289  1.00 22.62  ? 98  LYS B CG  1 
ATOM   4418 C  CD  . LYS B 1 98  ? 16.813  21.849  19.150  1.00 21.73  ? 98  LYS B CD  1 
ATOM   4419 C  CE  . LYS B 1 98  ? 17.887  22.815  19.547  1.00 24.34  ? 98  LYS B CE  1 
ATOM   4420 N  NZ  . LYS B 1 98  ? 18.348  23.621  18.398  1.00 24.41  ? 98  LYS B NZ  1 
ATOM   4421 N  N   . ALA B 1 99  ? 11.886  21.224  20.110  1.00 13.47  ? 99  ALA B N   1 
ATOM   4422 C  CA  . ALA B 1 99  ? 10.812  22.163  20.405  1.00 14.01  ? 99  ALA B CA  1 
ATOM   4423 C  C   . ALA B 1 99  ? 9.760   21.532  21.321  1.00 13.87  ? 99  ALA B C   1 
ATOM   4424 O  O   . ALA B 1 99  ? 9.195   22.170  22.211  1.00 15.01  ? 99  ALA B O   1 
ATOM   4425 C  CB  . ALA B 1 99  ? 10.253  22.674  19.113  1.00 13.80  ? 99  ALA B CB  1 
ATOM   4426 N  N   . HIS B 1 100 ? 9.491   20.238  21.127  1.00 14.98  ? 100 HIS B N   1 
ATOM   4427 C  CA  . HIS B 1 100 ? 8.587   19.476  21.977  1.00 13.75  ? 100 HIS B CA  1 
ATOM   4428 C  C   . HIS B 1 100 ? 9.030   19.568  23.435  1.00 13.64  ? 100 HIS B C   1 
ATOM   4429 O  O   . HIS B 1 100 ? 8.240   19.911  24.340  1.00 14.63  ? 100 HIS B O   1 
ATOM   4430 C  CB  . HIS B 1 100 ? 8.555   18.032  21.462  1.00 14.45  ? 100 HIS B CB  1 
ATOM   4431 C  CG  . HIS B 1 100 ? 7.708   17.065  22.227  1.00 14.10  ? 100 HIS B CG  1 
ATOM   4432 N  ND1 . HIS B 1 100 ? 6.326   17.015  22.173  1.00 14.23  ? 100 HIS B ND1 1 
ATOM   4433 C  CD2 . HIS B 1 100 ? 8.087   16.063  22.983  1.00 14.36  ? 100 HIS B CD2 1 
ATOM   4434 C  CE1 . HIS B 1 100 ? 5.895   16.013  22.900  1.00 14.13  ? 100 HIS B CE1 1 
ATOM   4435 N  NE2 . HIS B 1 100 ? 6.940   15.403  23.431  1.00 15.32  ? 100 HIS B NE2 1 
ATOM   4436 N  N   . ASN B 1 101 ? 10.311  19.265  23.663  1.00 13.39  ? 101 ASN B N   1 
ATOM   4437 C  CA  . ASN B 1 101 ? 10.885  19.329  24.997  1.00 15.41  ? 101 ASN B CA  1 
ATOM   4438 C  C   . ASN B 1 101 ? 10.843  20.751  25.576  1.00 13.27  ? 101 ASN B C   1 
ATOM   4439 O  O   . ASN B 1 101 ? 10.471  20.912  26.726  1.00 15.08  ? 101 ASN B O   1 
ATOM   4440 C  CB  . ASN B 1 101 ? 12.294  18.724  25.047  1.00 15.08  ? 101 ASN B CB  1 
ATOM   4441 C  CG  . ASN B 1 101 ? 12.294  17.213  24.938  1.00 19.02  ? 101 ASN B CG  1 
ATOM   4442 O  OD1 . ASN B 1 101 ? 11.262  16.555  25.048  1.00 18.04  ? 101 ASN B OD1 1 
ATOM   4443 N  ND2 . ASN B 1 101 ? 13.457  16.629  24.686  1.00 19.76  ? 101 ASN B ND2 1 
ATOM   4444 N  N   . ILE B 1 102 ? 11.170  21.767  24.784  1.00 14.08  ? 102 ILE B N   1 
ATOM   4445 C  CA  . ILE B 1 102 ? 11.209  23.153  25.223  1.00 14.03  ? 102 ILE B CA  1 
ATOM   4446 C  C   . ILE B 1 102 ? 9.833   23.751  25.539  1.00 15.45  ? 102 ILE B C   1 
ATOM   4447 O  O   . ILE B 1 102 ? 9.670   24.480  26.532  1.00 15.11  ? 102 ILE B O   1 
ATOM   4448 C  CB  . ILE B 1 102 ? 12.019  23.978  24.198  1.00 14.50  ? 102 ILE B CB  1 
ATOM   4449 C  CG1 . ILE B 1 102 ? 13.505  23.597  24.283  1.00 13.83  ? 102 ILE B CG1 1 
ATOM   4450 C  CG2 . ILE B 1 102 ? 11.824  25.481  24.409  1.00 14.98  ? 102 ILE B CG2 1 
ATOM   4451 C  CD1 . ILE B 1 102 ? 14.368  24.230  23.244  1.00 13.80  ? 102 ILE B CD1 1 
ATOM   4452 N  N   . LEU B 1 103 ? 8.811   23.364  24.799  1.00 15.77  ? 103 LEU B N   1 
ATOM   4453 C  CA  . LEU B 1 103 ? 7.535   24.039  24.918  1.00 15.07  ? 103 LEU B CA  1 
ATOM   4454 C  C   . LEU B 1 103 ? 6.537   23.273  25.772  1.00 17.71  ? 103 LEU B C   1 
ATOM   4455 O  O   . LEU B 1 103 ? 5.541   23.851  26.212  1.00 16.25  ? 103 LEU B O   1 
ATOM   4456 C  CB  . LEU B 1 103 ? 7.038   24.243  23.490  1.00 15.65  ? 103 LEU B CB  1 
ATOM   4457 C  CG  . LEU B 1 103 ? 7.909   25.170  22.648  1.00 16.93  ? 103 LEU B CG  1 
ATOM   4458 C  CD1 . LEU B 1 103 ? 7.345   25.398  21.250  1.00 17.65  ? 103 LEU B CD1 1 
ATOM   4459 C  CD2 . LEU B 1 103 ? 8.103   26.509  23.350  1.00 17.46  ? 103 LEU B CD2 1 
ATOM   4460 N  N   . LEU B 1 104 ? 6.789   21.990  26.058  1.00 17.98  ? 104 LEU B N   1 
ATOM   4461 C  CA  . LEU B 1 104 ? 5.858   21.234  26.887  1.00 20.06  ? 104 LEU B CA  1 
ATOM   4462 C  C   . LEU B 1 104 ? 5.672   21.862  28.269  1.00 18.86  ? 104 LEU B C   1 
ATOM   4463 O  O   . LEU B 1 104 ? 4.566   21.844  28.801  1.00 16.62  ? 104 LEU B O   1 
ATOM   4464 C  CB  . LEU B 1 104 ? 6.317   19.782  27.002  1.00 22.52  ? 104 LEU B CB  1 
ATOM   4465 C  CG  . LEU B 1 104 ? 5.652   18.809  26.041  1.00 24.20  ? 104 LEU B CG  1 
ATOM   4466 C  CD1 . LEU B 1 104 ? 6.273   17.438  26.216  1.00 24.81  ? 104 LEU B CD1 1 
ATOM   4467 C  CD2 . LEU B 1 104 ? 4.141   18.729  26.243  1.00 24.64  ? 104 LEU B CD2 1 
ATOM   4468 N  N   . PRO B 1 105 ? 6.710   22.435  28.935  1.00 20.80  ? 105 PRO B N   1 
ATOM   4469 C  CA  . PRO B 1 105 ? 6.504   23.135  30.215  1.00 17.85  ? 105 PRO B CA  1 
ATOM   4470 C  C   . PRO B 1 105 ? 5.580   24.358  30.159  1.00 18.02  ? 105 PRO B C   1 
ATOM   4471 O  O   . PRO B 1 105 ? 5.041   24.777  31.177  1.00 17.05  ? 105 PRO B O   1 
ATOM   4472 C  CB  . PRO B 1 105 ? 7.924   23.568  30.621  1.00 19.14  ? 105 PRO B CB  1 
ATOM   4473 C  CG  . PRO B 1 105 ? 8.834   22.623  29.868  1.00 19.32  ? 105 PRO B CG  1 
ATOM   4474 C  CD  . PRO B 1 105 ? 8.127   22.351  28.561  1.00 19.91  ? 105 PRO B CD  1 
ATOM   4475 N  N   . SER B 1 106 ? 5.368   24.901  28.961  1.00 17.24  ? 106 SER B N   1 
ATOM   4476 C  CA  . SER B 1 106 ? 4.420   25.984  28.712  1.00 18.30  ? 106 SER B CA  1 
ATOM   4477 C  C   . SER B 1 106 ? 2.977   25.497  28.854  1.00 19.23  ? 106 SER B C   1 
ATOM   4478 O  O   . SER B 1 106 ? 2.054   26.312  28.849  1.00 16.63  ? 106 SER B O   1 
ATOM   4479 C  CB  . SER B 1 106 ? 4.644   26.583  27.329  1.00 19.87  ? 106 SER B CB  1 
ATOM   4480 O  OG  . SER B 1 106 ? 5.897   27.239  27.275  1.00 28.26  ? 106 SER B OG  1 
ATOM   4481 N  N   . PHE B 1 107 ? 2.783   24.173  28.976  1.00 18.64  ? 107 PHE B N   1 
ATOM   4482 C  CA  . PHE B 1 107 ? 1.459   23.603  29.155  1.00 19.78  ? 107 PHE B CA  1 
ATOM   4483 C  C   . PHE B 1 107 ? 1.409   22.787  30.436  1.00 20.21  ? 107 PHE B C   1 
ATOM   4484 O  O   . PHE B 1 107 ? 0.506   22.010  30.626  1.00 18.51  ? 107 PHE B O   1 
ATOM   4485 C  CB  . PHE B 1 107 ? 1.069   22.847  27.884  1.00 19.61  ? 107 PHE B CB  1 
ATOM   4486 C  CG  . PHE B 1 107 ? 0.996   23.756  26.695  1.00 17.61  ? 107 PHE B CG  1 
ATOM   4487 C  CD1 . PHE B 1 107 ? -0.142  24.515  26.454  1.00 19.67  ? 107 PHE B CD1 1 
ATOM   4488 C  CD2 . PHE B 1 107 ? 2.100   23.975  25.898  1.00 18.24  ? 107 PHE B CD2 1 
ATOM   4489 C  CE1 . PHE B 1 107 ? -0.202  25.360  25.368  1.00 17.66  ? 107 PHE B CE1 1 
ATOM   4490 C  CE2 . PHE B 1 107 ? 2.054   24.861  24.838  1.00 17.82  ? 107 PHE B CE2 1 
ATOM   4491 C  CZ  . PHE B 1 107 ? 0.897   25.548  24.569  1.00 17.79  ? 107 PHE B CZ  1 
ATOM   4492 N  N   . SER B 1 108 ? 2.368   23.015  31.340  1.00 23.83  ? 108 SER B N   1 
ATOM   4493 C  CA  . SER B 1 108 ? 2.304   22.423  32.668  1.00 22.39  ? 108 SER B CA  1 
ATOM   4494 C  C   . SER B 1 108 ? 1.150   23.015  33.464  1.00 22.05  ? 108 SER B C   1 
ATOM   4495 O  O   . SER B 1 108 ? 0.527   24.010  33.081  1.00 20.76  ? 108 SER B O   1 
ATOM   4496 C  CB  . SER B 1 108 ? 3.599   22.625  33.397  1.00 22.59  ? 108 SER B CB  1 
ATOM   4497 O  OG  . SER B 1 108 ? 3.661   23.960  33.858  1.00 19.14  ? 108 SER B OG  1 
ATOM   4498 N  N   . GLN B 1 109 ? 0.882   22.366  34.598  1.00 24.06  ? 109 GLN B N   1 
ATOM   4499 C  CA  . GLN B 1 109 ? -0.215  22.720  35.477  1.00 25.59  ? 109 GLN B CA  1 
ATOM   4500 C  C   . GLN B 1 109 ? 0.042   24.122  36.038  1.00 23.36  ? 109 GLN B C   1 
ATOM   4501 O  O   . GLN B 1 109 ? -0.893  24.933  36.092  1.00 23.11  ? 109 GLN B O   1 
ATOM   4502 C  CB  . GLN B 1 109 ? -0.328  21.606  36.521  1.00 32.63  ? 109 GLN B CB  1 
ATOM   4503 C  CG  . GLN B 1 109 ? -1.562  21.661  37.417  1.00 41.38  ? 109 GLN B CG  1 
ATOM   4504 C  CD  . GLN B 1 109 ? -2.888  21.529  36.695  1.00 47.63  ? 109 GLN B CD  1 
ATOM   4505 O  OE1 . GLN B 1 109 ? -3.879  22.147  37.088  1.00 47.97  ? 109 GLN B OE1 1 
ATOM   4506 N  NE2 . GLN B 1 109 ? -2.929  20.684  35.669  1.00 45.13  ? 109 GLN B NE2 1 
ATOM   4507 N  N   . GLN B 1 110 ? 1.303   24.427  36.418  1.00 22.31  ? 110 GLN B N   1 
ATOM   4508 C  CA  . GLN B 1 110 ? 1.639   25.772  36.868  1.00 24.14  ? 110 GLN B CA  1 
ATOM   4509 C  C   . GLN B 1 110 ? 1.399   26.759  35.735  1.00 20.87  ? 110 GLN B C   1 
ATOM   4510 O  O   . GLN B 1 110 ? 0.847   27.827  35.979  1.00 22.42  ? 110 GLN B O   1 
ATOM   4511 C  CB  . GLN B 1 110 ? 3.077   25.969  37.362  1.00 26.49  ? 110 GLN B CB  1 
ATOM   4512 C  CG  . GLN B 1 110 ? 3.255   25.840  38.867  1.00 33.13  ? 110 GLN B CG  1 
ATOM   4513 C  CD  . GLN B 1 110 ? 2.244   26.593  39.709  1.00 38.77  ? 110 GLN B CD  1 
ATOM   4514 O  OE1 . GLN B 1 110 ? 1.644   26.033  40.629  1.00 36.95  ? 110 GLN B OE1 1 
ATOM   4515 N  NE2 . GLN B 1 110 ? 2.043   27.872  39.412  1.00 40.11  ? 110 GLN B NE2 1 
ATOM   4516 N  N   . ALA B 1 111 ? 1.825   26.411  34.515  1.00 19.46  ? 111 ALA B N   1 
ATOM   4517 C  CA  . ALA B 1 111 ? 1.631   27.303  33.376  1.00 19.15  ? 111 ALA B CA  1 
ATOM   4518 C  C   . ALA B 1 111 ? 0.142   27.563  33.147  1.00 18.15  ? 111 ALA B C   1 
ATOM   4519 O  O   . ALA B 1 111 ? -0.252  28.695  32.874  1.00 15.84  ? 111 ALA B O   1 
ATOM   4520 C  CB  . ALA B 1 111 ? 2.296   26.776  32.128  1.00 18.82  ? 111 ALA B CB  1 
ATOM   4521 N  N   . MET B 1 112 ? -0.676  26.513  33.254  1.00 19.30  ? 112 MET B N   1 
ATOM   4522 C  CA  . MET B 1 112 ? -2.097  26.647  32.972  1.00 20.22  ? 112 MET B CA  1 
ATOM   4523 C  C   . MET B 1 112 ? -2.726  27.606  33.986  1.00 19.40  ? 112 MET B C   1 
ATOM   4524 O  O   . MET B 1 112 ? -3.577  28.422  33.638  1.00 19.44  ? 112 MET B O   1 
ATOM   4525 C  CB  . MET B 1 112 ? -2.799  25.283  33.013  1.00 20.66  ? 112 MET B CB  1 
ATOM   4526 C  CG  . MET B 1 112 ? -2.645  24.431  31.730  1.00 24.91  ? 112 MET B CG  1 
ATOM   4527 S  SD  . MET B 1 112 ? -3.009  25.327  30.175  1.00 25.89  ? 112 MET B SD  1 
ATOM   4528 C  CE  . MET B 1 112 ? -4.547  26.156  30.570  1.00 25.26  ? 112 MET B CE  1 
ATOM   4529 N  N   . LYS B 1 113 ? -2.295  27.530  35.247  1.00 18.47  ? 113 LYS B N   1 
ATOM   4530 C  CA  . LYS B 1 113 ? -2.790  28.445  36.261  1.00 19.61  ? 113 LYS B CA  1 
ATOM   4531 C  C   . LYS B 1 113 ? -2.413  29.863  35.884  1.00 21.05  ? 113 LYS B C   1 
ATOM   4532 O  O   . LYS B 1 113 ? -3.190  30.777  36.110  1.00 20.39  ? 113 LYS B O   1 
ATOM   4533 C  CB  . LYS B 1 113 ? -2.237  28.100  37.650  1.00 22.51  ? 113 LYS B CB  1 
ATOM   4534 C  CG  . LYS B 1 113 ? -2.873  26.866  38.277  1.00 24.10  ? 113 LYS B CG  1 
ATOM   4535 C  CD  . LYS B 1 113 ? -2.265  26.477  39.614  1.00 27.01  ? 113 LYS B CD  1 
ATOM   4536 C  CE  . LYS B 1 113 ? -3.065  25.400  40.320  1.00 31.82  ? 113 LYS B CE  1 
ATOM   4537 N  NZ  . LYS B 1 113 ? -2.720  24.051  39.830  1.00 38.38  ? 113 LYS B NZ  1 
ATOM   4538 N  N   . GLY B 1 114 ? -1.204  30.032  35.338  1.00 19.64  ? 114 GLY B N   1 
ATOM   4539 C  CA  . GLY B 1 114 ? -0.698  31.356  35.013  1.00 20.71  ? 114 GLY B CA  1 
ATOM   4540 C  C   . GLY B 1 114 ? -1.411  31.997  33.814  1.00 22.48  ? 114 GLY B C   1 
ATOM   4541 O  O   . GLY B 1 114 ? -1.303  33.202  33.582  1.00 23.11  ? 114 GLY B O   1 
ATOM   4542 N  N   . TYR B 1 115 ? -2.075  31.195  32.988  1.00 19.72  ? 115 TYR B N   1 
ATOM   4543 C  CA  . TYR B 1 115 ? -2.765  31.747  31.825  1.00 18.48  ? 115 TYR B CA  1 
ATOM   4544 C  C   . TYR B 1 115 ? -4.195  32.156  32.173  1.00 18.87  ? 115 TYR B C   1 
ATOM   4545 O  O   . TYR B 1 115 ? -4.809  32.891  31.391  1.00 18.61  ? 115 TYR B O   1 
ATOM   4546 C  CB  . TYR B 1 115 ? -2.874  30.752  30.668  1.00 17.87  ? 115 TYR B CB  1 
ATOM   4547 C  CG  . TYR B 1 115 ? -1.568  30.295  30.035  1.00 17.19  ? 115 TYR B CG  1 
ATOM   4548 C  CD1 . TYR B 1 115 ? -0.588  31.205  29.662  1.00 19.18  ? 115 TYR B CD1 1 
ATOM   4549 C  CD2 . TYR B 1 115 ? -1.326  28.943  29.799  1.00 17.18  ? 115 TYR B CD2 1 
ATOM   4550 C  CE1 . TYR B 1 115 ? 0.584   30.789  29.057  1.00 20.75  ? 115 TYR B CE1 1 
ATOM   4551 C  CE2 . TYR B 1 115 ? -0.167  28.523  29.171  1.00 18.30  ? 115 TYR B CE2 1 
ATOM   4552 C  CZ  . TYR B 1 115 ? 0.812   29.443  28.846  1.00 20.65  ? 115 TYR B CZ  1 
ATOM   4553 O  OH  . TYR B 1 115 ? 1.977   29.074  28.256  1.00 21.93  ? 115 TYR B OH  1 
ATOM   4554 N  N   . HIS B 1 116 ? -4.723  31.670  33.306  1.00 18.20  ? 116 HIS B N   1 
ATOM   4555 C  CA  . HIS B 1 116 ? -6.144  31.764  33.631  1.00 17.62  ? 116 HIS B CA  1 
ATOM   4556 C  C   . HIS B 1 116 ? -6.632  33.215  33.641  1.00 17.57  ? 116 HIS B C   1 
ATOM   4557 O  O   . HIS B 1 116 ? -7.712  33.522  33.131  1.00 16.99  ? 116 HIS B O   1 
ATOM   4558 C  CB  . HIS B 1 116 ? -6.434  31.119  34.988  1.00 18.20  ? 116 HIS B CB  1 
ATOM   4559 C  CG  . HIS B 1 116 ? -7.878  31.126  35.342  1.00 17.10  ? 116 HIS B CG  1 
ATOM   4560 N  ND1 . HIS B 1 116 ? -8.827  30.219  34.904  1.00 17.77  ? 116 HIS B ND1 1 
ATOM   4561 C  CD2 . HIS B 1 116 ? -8.530  32.020  36.108  1.00 17.38  ? 116 HIS B CD2 1 
ATOM   4562 C  CE1 . HIS B 1 116 ? -10.009 30.573  35.383  1.00 16.42  ? 116 HIS B CE1 1 
ATOM   4563 N  NE2 . HIS B 1 116 ? -9.859  31.701  36.089  1.00 15.86  ? 116 HIS B NE2 1 
ATOM   4564 N  N   . ALA B 1 117 ? -5.839  34.113  34.245  1.00 18.25  ? 117 ALA B N   1 
ATOM   4565 C  CA  . ALA B 1 117 ? -6.212  35.524  34.380  1.00 18.41  ? 117 ALA B CA  1 
ATOM   4566 C  C   . ALA B 1 117 ? -6.394  36.176  33.012  1.00 17.18  ? 117 ALA B C   1 
ATOM   4567 O  O   . ALA B 1 117 ? -7.307  36.958  32.802  1.00 18.19  ? 117 ALA B O   1 
ATOM   4568 C  CB  . ALA B 1 117 ? -5.154  36.265  35.167  1.00 18.99  ? 117 ALA B CB  1 
ATOM   4569 N  N   . MET B 1 118 ? -5.519  35.879  32.068  1.00 17.05  ? 118 MET B N   1 
ATOM   4570 C  CA  . MET B 1 118 ? -5.622  36.531  30.775  1.00 19.73  ? 118 MET B CA  1 
ATOM   4571 C  C   . MET B 1 118 ? -6.769  35.878  29.995  1.00 20.32  ? 118 MET B C   1 
ATOM   4572 O  O   . MET B 1 118 ? -7.389  36.520  29.166  1.00 18.59  ? 118 MET B O   1 
ATOM   4573 C  CB  . MET B 1 118 ? -4.323  36.422  29.982  1.00 22.38  ? 118 MET B CB  1 
ATOM   4574 C  CG  . MET B 1 118 ? -3.248  37.363  30.496  1.00 27.80  ? 118 MET B CG  1 
ATOM   4575 S  SD  . MET B 1 118 ? -1.637  36.961  29.753  1.00 38.60  ? 118 MET B SD  1 
ATOM   4576 C  CE  . MET B 1 118 ? -1.282  35.315  30.372  1.00 35.58  ? 118 MET B CE  1 
ATOM   4577 N  N   . MET B 1 119 ? -7.046  34.580  30.220  1.00 18.78  ? 119 MET B N   1 
ATOM   4578 C  CA  . MET B 1 119 ? -8.209  33.982  29.540  1.00 15.34  ? 119 MET B CA  1 
ATOM   4579 C  C   . MET B 1 119 ? -9.484  34.661  30.013  1.00 14.11  ? 119 MET B C   1 
ATOM   4580 O  O   . MET B 1 119 ? -10.439 34.824  29.250  1.00 13.48  ? 119 MET B O   1 
ATOM   4581 C  CB  . MET B 1 119 ? -8.293  32.480  29.827  1.00 15.19  ? 119 MET B CB  1 
ATOM   4582 C  CG  . MET B 1 119 ? -7.203  31.681  29.152  1.00 15.61  ? 119 MET B CG  1 
ATOM   4583 S  SD  . MET B 1 119 ? -7.560  29.936  29.396  1.00 18.90  ? 119 MET B SD  1 
ATOM   4584 C  CE  . MET B 1 119 ? -6.214  29.209  28.458  1.00 19.82  ? 119 MET B CE  1 
ATOM   4585 N  N   . VAL B 1 120 ? -9.510  35.000  31.296  1.00 14.13  ? 120 VAL B N   1 
ATOM   4586 C  CA  . VAL B 1 120 ? -10.632 35.700  31.870  1.00 14.93  ? 120 VAL B CA  1 
ATOM   4587 C  C   . VAL B 1 120 ? -10.756 37.085  31.226  1.00 16.41  ? 120 VAL B C   1 
ATOM   4588 O  O   . VAL B 1 120 ? -11.875 37.510  30.904  1.00 15.00  ? 120 VAL B O   1 
ATOM   4589 C  CB  . VAL B 1 120 ? -10.579 35.701  33.409  1.00 15.05  ? 120 VAL B CB  1 
ATOM   4590 C  CG1 . VAL B 1 120 ? -11.547 36.684  34.034  1.00 17.04  ? 120 VAL B CG1 1 
ATOM   4591 C  CG2 . VAL B 1 120 ? -10.840 34.314  33.976  1.00 14.84  ? 120 VAL B CG2 1 
ATOM   4592 N  N   . ASP B 1 121 ? -9.618  37.757  30.981  1.00 17.26  ? 121 ASP B N   1 
ATOM   4593 C  CA  . ASP B 1 121 ? -9.598  39.081  30.364  1.00 17.94  ? 121 ASP B CA  1 
ATOM   4594 C  C   . ASP B 1 121 ? -10.376 39.056  29.053  1.00 16.47  ? 121 ASP B C   1 
ATOM   4595 O  O   . ASP B 1 121 ? -11.295 39.865  28.877  1.00 16.70  ? 121 ASP B O   1 
ATOM   4596 C  CB  . ASP B 1 121 ? -8.155  39.590  30.211  1.00 20.94  ? 121 ASP B CB  1 
ATOM   4597 C  CG  . ASP B 1 121 ? -7.989  40.906  29.467  1.00 25.07  ? 121 ASP B CG  1 
ATOM   4598 O  OD1 . ASP B 1 121 ? -8.569  41.058  28.351  1.00 24.27  ? 121 ASP B OD1 1 
ATOM   4599 O  OD2 . ASP B 1 121 ? -7.277  41.782  30.001  1.00 23.28  ? 121 ASP B OD2 1 
ATOM   4600 N  N   . ILE B 1 122 ? -10.049 38.088  28.168  1.00 15.61  ? 122 ILE B N   1 
ATOM   4601 C  CA  . ILE B 1 122 ? -10.689 37.943  26.873  1.00 14.83  ? 122 ILE B CA  1 
ATOM   4602 C  C   . ILE B 1 122 ? -12.141 37.502  27.038  1.00 15.86  ? 122 ILE B C   1 
ATOM   4603 O  O   . ILE B 1 122 ? -13.025 38.094  26.393  1.00 15.57  ? 122 ILE B O   1 
ATOM   4604 C  CB  . ILE B 1 122 ? -9.884  37.002  25.961  1.00 14.87  ? 122 ILE B CB  1 
ATOM   4605 C  CG1 . ILE B 1 122 ? -8.405  37.394  25.907  1.00 16.43  ? 122 ILE B CG1 1 
ATOM   4606 C  CG2 . ILE B 1 122 ? -10.500 36.940  24.578  1.00 15.39  ? 122 ILE B CG2 1 
ATOM   4607 C  CD1 . ILE B 1 122 ? -8.125  38.831  25.449  1.00 17.36  ? 122 ILE B CD1 1 
ATOM   4608 N  N   . ALA B 1 123 ? -12.404 36.540  27.943  1.00 13.53  ? 123 ALA B N   1 
ATOM   4609 C  CA  . ALA B 1 123 ? -13.763 36.059  28.165  1.00 13.36  ? 123 ALA B CA  1 
ATOM   4610 C  C   . ALA B 1 123 ? -14.691 37.183  28.636  1.00 14.31  ? 123 ALA B C   1 
ATOM   4611 O  O   . ALA B 1 123 ? -15.854 37.231  28.229  1.00 12.20  ? 123 ALA B O   1 
ATOM   4612 C  CB  . ALA B 1 123 ? -13.770 34.911  29.148  1.00 14.14  ? 123 ALA B CB  1 
ATOM   4613 N  N   . VAL B 1 124 ? -14.206 38.034  29.557  1.00 15.18  ? 124 VAL B N   1 
ATOM   4614 C  CA  . VAL B 1 124 ? -14.989 39.186  30.003  1.00 15.91  ? 124 VAL B CA  1 
ATOM   4615 C  C   . VAL B 1 124 ? -15.316 40.068  28.808  1.00 14.79  ? 124 VAL B C   1 
ATOM   4616 O  O   . VAL B 1 124 ? -16.439 40.568  28.715  1.00 17.08  ? 124 VAL B O   1 
ATOM   4617 C  CB  . VAL B 1 124 ? -14.291 39.938  31.151  1.00 17.79  ? 124 VAL B CB  1 
ATOM   4618 C  CG1 . VAL B 1 124 ? -14.786 41.370  31.319  1.00 19.25  ? 124 VAL B CG1 1 
ATOM   4619 C  CG2 . VAL B 1 124 ? -14.460 39.181  32.451  1.00 18.99  ? 124 VAL B CG2 1 
ATOM   4620 N  N   . GLN B 1 125 ? -14.400 40.232  27.857  1.00 14.25  ? 125 GLN B N   1 
ATOM   4621 C  CA  . GLN B 1 125 ? -14.663 41.078  26.708  1.00 15.52  ? 125 GLN B CA  1 
ATOM   4622 C  C   . GLN B 1 125 ? -15.787 40.493  25.850  1.00 16.92  ? 125 GLN B C   1 
ATOM   4623 O  O   . GLN B 1 125 ? -16.654 41.243  25.419  1.00 14.29  ? 125 GLN B O   1 
ATOM   4624 C  CB  . GLN B 1 125 ? -13.435 41.293  25.830  1.00 16.10  ? 125 GLN B CB  1 
ATOM   4625 C  CG  . GLN B 1 125 ? -12.380 42.162  26.475  1.00 15.82  ? 125 GLN B CG  1 
ATOM   4626 C  CD  . GLN B 1 125 ? -11.264 42.456  25.506  1.00 17.79  ? 125 GLN B CD  1 
ATOM   4627 O  OE1 . GLN B 1 125 ? -11.485 42.920  24.375  1.00 17.47  ? 125 GLN B OE1 1 
ATOM   4628 N  NE2 . GLN B 1 125 ? -10.043 42.177  25.947  1.00 15.93  ? 125 GLN B NE2 1 
ATOM   4629 N  N   . LEU B 1 126 ? -15.814 39.155  25.653  1.00 14.37  ? 126 LEU B N   1 
ATOM   4630 C  CA  . LEU B 1 126 ? -16.932 38.511  24.963  1.00 15.40  ? 126 LEU B CA  1 
ATOM   4631 C  C   . LEU B 1 126 ? -18.244 38.741  25.713  1.00 14.04  ? 126 LEU B C   1 
ATOM   4632 O  O   . LEU B 1 126 ? -19.254 39.142  25.139  1.00 13.83  ? 126 LEU B O   1 
ATOM   4633 C  CB  . LEU B 1 126 ? -16.691 36.998  24.786  1.00 15.91  ? 126 LEU B CB  1 
ATOM   4634 C  CG  . LEU B 1 126 ? -17.867 36.252  24.138  1.00 16.05  ? 126 LEU B CG  1 
ATOM   4635 C  CD1 . LEU B 1 126 ? -17.721 36.305  22.650  1.00 15.97  ? 126 LEU B CD1 1 
ATOM   4636 C  CD2 . LEU B 1 126 ? -17.957 34.813  24.600  1.00 19.65  ? 126 LEU B CD2 1 
ATOM   4637 N  N   . ILE B 1 127 ? -18.268 38.459  27.008  1.00 13.55  ? 127 ILE B N   1 
ATOM   4638 C  CA  . ILE B 1 127 ? -19.505 38.562  27.739  1.00 13.66  ? 127 ILE B CA  1 
ATOM   4639 C  C   . ILE B 1 127 ? -20.034 40.011  27.659  1.00 14.55  ? 127 ILE B C   1 
ATOM   4640 O  O   . ILE B 1 127 ? -21.225 40.252  27.501  1.00 14.09  ? 127 ILE B O   1 
ATOM   4641 C  CB  . ILE B 1 127 ? -19.307 38.116  29.194  1.00 14.29  ? 127 ILE B CB  1 
ATOM   4642 C  CG1 . ILE B 1 127 ? -18.858 36.657  29.288  1.00 15.75  ? 127 ILE B CG1 1 
ATOM   4643 C  CG2 . ILE B 1 127 ? -20.584 38.369  29.968  1.00 15.39  ? 127 ILE B CG2 1 
ATOM   4644 C  CD1 . ILE B 1 127 ? -19.877 35.644  28.767  1.00 15.94  ? 127 ILE B CD1 1 
ATOM   4645 N  N   . GLN B 1 128 ? -19.132 40.991  27.784  1.00 15.31  ? 128 GLN B N   1 
ATOM   4646 C  CA  . GLN B 1 128 ? -19.511 42.402  27.753  1.00 17.27  ? 128 GLN B CA  1 
ATOM   4647 C  C   . GLN B 1 128 ? -20.069 42.796  26.391  1.00 14.50  ? 128 GLN B C   1 
ATOM   4648 O  O   . GLN B 1 128 ? -21.047 43.532  26.348  1.00 17.33  ? 128 GLN B O   1 
ATOM   4649 C  CB  . GLN B 1 128 ? -18.334 43.319  28.111  1.00 19.34  ? 128 GLN B CB  1 
ATOM   4650 C  CG  . GLN B 1 128 ? -18.102 43.397  29.609  1.00 22.92  ? 128 GLN B CG  1 
ATOM   4651 C  CD  . GLN B 1 128 ? -16.913 44.263  29.942  1.00 29.86  ? 128 GLN B CD  1 
ATOM   4652 O  OE1 . GLN B 1 128 ? -15.875 44.214  29.280  1.00 36.63  ? 128 GLN B OE1 1 
ATOM   4653 N  NE2 . GLN B 1 128 ? -17.078 45.105  30.947  1.00 37.53  ? 128 GLN B NE2 1 
ATOM   4654 N  N   . LYS B 1 129 ? -19.483 42.300  25.311  1.00 12.86  ? 129 LYS B N   1 
ATOM   4655 C  CA  . LYS B 1 129 ? -20.001 42.552  23.983  1.00 13.79  ? 129 LYS B CA  1 
ATOM   4656 C  C   . LYS B 1 129 ? -21.462 42.113  23.897  1.00 15.56  ? 129 LYS B C   1 
ATOM   4657 O  O   . LYS B 1 129 ? -22.328 42.847  23.396  1.00 14.65  ? 129 LYS B O   1 
ATOM   4658 C  CB  . LYS B 1 129 ? -19.159 41.841  22.919  1.00 15.06  ? 129 LYS B CB  1 
ATOM   4659 C  CG  . LYS B 1 129 ? -19.706 41.990  21.512  1.00 14.46  ? 129 LYS B CG  1 
ATOM   4660 C  CD  . LYS B 1 129 ? -18.919 41.362  20.422  1.00 15.40  ? 129 LYS B CD  1 
ATOM   4661 C  CE  . LYS B 1 129 ? -19.598 41.609  19.089  1.00 14.72  ? 129 LYS B CE  1 
ATOM   4662 N  NZ  . LYS B 1 129 ? -18.716 41.265  17.961  1.00 16.63  ? 129 LYS B NZ  1 
ATOM   4663 N  N   . TRP B 1 130 ? -21.753 40.915  24.422  1.00 15.15  ? 130 TRP B N   1 
ATOM   4664 C  CA  . TRP B 1 130 ? -23.091 40.365  24.269  1.00 15.89  ? 130 TRP B CA  1 
ATOM   4665 C  C   . TRP B 1 130 ? -24.058 41.064  25.213  1.00 16.70  ? 130 TRP B C   1 
ATOM   4666 O  O   . TRP B 1 130 ? -25.208 41.286  24.838  1.00 18.31  ? 130 TRP B O   1 
ATOM   4667 C  CB  . TRP B 1 130 ? -23.073 38.841  24.478  1.00 14.03  ? 130 TRP B CB  1 
ATOM   4668 C  CG  . TRP B 1 130 ? -22.363 38.090  23.376  1.00 13.73  ? 130 TRP B CG  1 
ATOM   4669 C  CD1 . TRP B 1 130 ? -21.864 38.575  22.210  1.00 13.50  ? 130 TRP B CD1 1 
ATOM   4670 C  CD2 . TRP B 1 130 ? -22.158 36.654  23.315  1.00 12.73  ? 130 TRP B CD2 1 
ATOM   4671 N  NE1 . TRP B 1 130 ? -21.287 37.557  21.485  1.00 14.82  ? 130 TRP B NE1 1 
ATOM   4672 C  CE2 . TRP B 1 130 ? -21.499 36.365  22.116  1.00 12.90  ? 130 TRP B CE2 1 
ATOM   4673 C  CE3 . TRP B 1 130 ? -22.485 35.599  24.165  1.00 14.30  ? 130 TRP B CE3 1 
ATOM   4674 C  CZ2 . TRP B 1 130 ? -21.128 35.066  21.740  1.00 13.36  ? 130 TRP B CZ2 1 
ATOM   4675 C  CZ3 . TRP B 1 130 ? -22.130 34.306  23.799  1.00 15.06  ? 130 TRP B CZ3 1 
ATOM   4676 C  CH2 . TRP B 1 130 ? -21.490 34.043  22.596  1.00 13.97  ? 130 TRP B CH2 1 
ATOM   4677 N  N   . GLU B 1 131 ? -23.602 41.432  26.411  1.00 18.30  ? 131 GLU B N   1 
ATOM   4678 C  CA  . GLU B 1 131 ? -24.423 42.205  27.342  1.00 17.68  ? 131 GLU B CA  1 
ATOM   4679 C  C   . GLU B 1 131 ? -24.849 43.527  26.722  1.00 17.51  ? 131 GLU B C   1 
ATOM   4680 O  O   . GLU B 1 131 ? -25.877 44.050  27.094  1.00 17.76  ? 131 GLU B O   1 
ATOM   4681 C  CB  . GLU B 1 131 ? -23.701 42.551  28.640  1.00 20.39  ? 131 GLU B CB  1 
ATOM   4682 C  CG  . GLU B 1 131 ? -23.447 41.398  29.576  1.00 23.87  ? 131 GLU B CG  1 
ATOM   4683 C  CD  . GLU B 1 131 ? -24.636 40.878  30.360  1.00 28.19  ? 131 GLU B CD  1 
ATOM   4684 O  OE1 . GLU B 1 131 ? -25.788 41.257  30.034  1.00 32.22  ? 131 GLU B OE1 1 
ATOM   4685 O  OE2 . GLU B 1 131 ? -24.406 40.068  31.301  1.00 33.73  ? 131 GLU B OE2 1 
ATOM   4686 N  N   . ARG B 1 132 ? -24.081 44.056  25.774  1.00 17.18  ? 132 ARG B N   1 
ATOM   4687 C  CA  . ARG B 1 132 ? -24.266 45.418  25.295  1.00 17.20  ? 132 ARG B CA  1 
ATOM   4688 C  C   . ARG B 1 132 ? -25.071 45.404  23.999  1.00 17.83  ? 132 ARG B C   1 
ATOM   4689 O  O   . ARG B 1 132 ? -25.306 46.443  23.411  1.00 17.30  ? 132 ARG B O   1 
ATOM   4690 C  CB  . ARG B 1 132 ? -22.903 46.099  25.079  1.00 15.97  ? 132 ARG B CB  1 
ATOM   4691 C  CG  . ARG B 1 132 ? -22.228 46.521  26.368  1.00 16.07  ? 132 ARG B CG  1 
ATOM   4692 C  CD  . ARG B 1 132 ? -20.733 46.755  26.215  1.00 15.79  ? 132 ARG B CD  1 
ATOM   4693 N  NE  . ARG B 1 132 ? -20.213 47.261  27.477  1.00 17.01  ? 132 ARG B NE  1 
ATOM   4694 C  CZ  . ARG B 1 132 ? -18.926 47.468  27.741  1.00 18.51  ? 132 ARG B CZ  1 
ATOM   4695 N  NH1 . ARG B 1 132 ? -18.009 47.126  26.870  1.00 16.94  ? 132 ARG B NH1 1 
ATOM   4696 N  NH2 . ARG B 1 132 ? -18.573 48.036  28.882  1.00 22.44  ? 132 ARG B NH2 1 
ATOM   4697 N  N   . LEU B 1 133 ? -25.532 44.218  23.553  1.00 18.46  ? 133 LEU B N   1 
ATOM   4698 C  CA  . LEU B 1 133 ? -26.360 44.177  22.369  1.00 17.26  ? 133 LEU B CA  1 
ATOM   4699 C  C   . LEU B 1 133 ? -27.740 44.747  22.686  1.00 16.61  ? 133 LEU B C   1 
ATOM   4700 O  O   . LEU B 1 133 ? -28.270 44.589  23.788  1.00 17.61  ? 133 LEU B O   1 
ATOM   4701 C  CB  . LEU B 1 133 ? -26.447 42.736  21.854  1.00 18.45  ? 133 LEU B CB  1 
ATOM   4702 C  CG  . LEU B 1 133 ? -25.162 42.179  21.252  1.00 17.54  ? 133 LEU B CG  1 
ATOM   4703 C  CD1 . LEU B 1 133 ? -25.404 40.780  20.675  1.00 20.03  ? 133 LEU B CD1 1 
ATOM   4704 C  CD2 . LEU B 1 133 ? -24.611 43.092  20.173  1.00 16.15  ? 133 LEU B CD2 1 
ATOM   4705 N  N   . ASN B 1 134 ? -28.347 45.332  21.670  1.00 15.87  ? 134 ASN B N   1 
ATOM   4706 C  CA  . ASN B 1 134 ? -29.690 45.874  21.770  1.00 17.42  ? 134 ASN B CA  1 
ATOM   4707 C  C   . ASN B 1 134 ? -30.720 44.758  21.577  1.00 19.62  ? 134 ASN B C   1 
ATOM   4708 O  O   . ASN B 1 134 ? -30.411 43.681  21.071  1.00 18.43  ? 134 ASN B O   1 
ATOM   4709 C  CB  . ASN B 1 134 ? -29.935 46.986  20.735  1.00 15.83  ? 134 ASN B CB  1 
ATOM   4710 C  CG  . ASN B 1 134 ? -28.918 48.120  20.825  1.00 14.53  ? 134 ASN B CG  1 
ATOM   4711 O  OD1 . ASN B 1 134 ? -28.824 48.819  21.827  1.00 14.97  ? 134 ASN B OD1 1 
ATOM   4712 N  ND2 . ASN B 1 134 ? -28.146 48.277  19.776  1.00 14.96  ? 134 ASN B ND2 1 
ATOM   4713 N  N   . ALA B 1 135 ? -31.960 45.083  21.953  1.00 20.73  ? 135 ALA B N   1 
ATOM   4714 C  CA  . ALA B 1 135 ? -33.089 44.173  21.867  1.00 20.48  ? 135 ALA B CA  1 
ATOM   4715 C  C   . ALA B 1 135 ? -33.185 43.655  20.443  1.00 22.39  ? 135 ALA B C   1 
ATOM   4716 O  O   . ALA B 1 135 ? -33.062 44.410  19.489  1.00 24.95  ? 135 ALA B O   1 
ATOM   4717 C  CB  . ALA B 1 135 ? -34.346 44.874  22.303  1.00 21.02  ? 135 ALA B CB  1 
ATOM   4718 N  N   . ASP B 1 136 ? -33.238 42.336  20.311  1.00 27.52  ? 136 ASP B N   1 
ATOM   4719 C  CA  . ASP B 1 136 ? -33.516 41.682  19.041  1.00 27.53  ? 136 ASP B CA  1 
ATOM   4720 C  C   . ASP B 1 136 ? -32.300 41.577  18.141  1.00 25.87  ? 136 ASP B C   1 
ATOM   4721 O  O   . ASP B 1 136 ? -32.438 41.122  17.016  1.00 31.20  ? 136 ASP B O   1 
ATOM   4722 C  CB  . ASP B 1 136 ? -34.627 42.390  18.270  1.00 30.06  ? 136 ASP B CB  1 
ATOM   4723 C  CG  . ASP B 1 136 ? -35.931 41.642  18.311  1.00 35.22  ? 136 ASP B CG  1 
ATOM   4724 O  OD1 . ASP B 1 136 ? -36.526 41.564  19.409  1.00 39.96  ? 136 ASP B OD1 1 
ATOM   4725 O  OD2 . ASP B 1 136 ? -36.333 41.160  17.237  1.00 45.31  ? 136 ASP B OD2 1 
ATOM   4726 N  N   . GLU B 1 137 ? -31.123 42.010  18.592  1.00 23.68  ? 137 GLU B N   1 
ATOM   4727 C  CA  . GLU B 1 137 ? -29.920 41.787  17.814  1.00 22.58  ? 137 GLU B CA  1 
ATOM   4728 C  C   . GLU B 1 137 ? -29.452 40.349  18.019  1.00 21.20  ? 137 GLU B C   1 
ATOM   4729 O  O   . GLU B 1 137 ? -29.820 39.704  18.996  1.00 20.47  ? 137 GLU B O   1 
ATOM   4730 C  CB  . GLU B 1 137 ? -28.849 42.777  18.230  1.00 25.06  ? 137 GLU B CB  1 
ATOM   4731 C  CG  . GLU B 1 137 ? -29.270 44.205  17.883  1.00 27.45  ? 137 GLU B CG  1 
ATOM   4732 C  CD  . GLU B 1 137 ? -28.213 45.258  18.170  1.00 30.86  ? 137 GLU B CD  1 
ATOM   4733 O  OE1 . GLU B 1 137 ? -27.268 44.949  18.947  1.00 28.67  ? 137 GLU B OE1 1 
ATOM   4734 O  OE2 . GLU B 1 137 ? -28.309 46.363  17.586  1.00 33.54  ? 137 GLU B OE2 1 
ATOM   4735 N  N   . HIS B 1 138 ? -28.638 39.854  17.092  1.00 20.53  ? 138 HIS B N   1 
ATOM   4736 C  CA  . HIS B 1 138 ? -28.167 38.482  17.208  1.00 19.71  ? 138 HIS B CA  1 
ATOM   4737 C  C   . HIS B 1 138 ? -26.653 38.449  17.310  1.00 18.32  ? 138 HIS B C   1 
ATOM   4738 O  O   . HIS B 1 138 ? -25.996 39.471  17.148  1.00 15.22  ? 138 HIS B O   1 
ATOM   4739 C  CB  . HIS B 1 138 ? -28.647 37.652  16.016  1.00 20.13  ? 138 HIS B CB  1 
ATOM   4740 C  CG  . HIS B 1 138 ? -28.158 38.084  14.696  1.00 21.80  ? 138 HIS B CG  1 
ATOM   4741 N  ND1 . HIS B 1 138 ? -28.976 38.788  13.842  1.00 22.10  ? 138 HIS B ND1 1 
ATOM   4742 C  CD2 . HIS B 1 138 ? -26.999 37.921  14.060  1.00 24.29  ? 138 HIS B CD2 1 
ATOM   4743 C  CE1 . HIS B 1 138 ? -28.333 38.991  12.707  1.00 23.84  ? 138 HIS B CE1 1 
ATOM   4744 N  NE2 . HIS B 1 138 ? -27.109 38.519  12.835  1.00 24.82  ? 138 HIS B NE2 1 
ATOM   4745 N  N   . ILE B 1 139 ? -26.150 37.225  17.504  1.00 18.64  ? 139 ILE B N   1 
ATOM   4746 C  CA  . ILE B 1 139 ? -24.735 36.911  17.628  1.00 18.81  ? 139 ILE B CA  1 
ATOM   4747 C  C   . ILE B 1 139 ? -24.333 36.036  16.440  1.00 18.22  ? 139 ILE B C   1 
ATOM   4748 O  O   . ILE B 1 139 ? -25.045 35.105  16.096  1.00 14.69  ? 139 ILE B O   1 
ATOM   4749 C  CB  . ILE B 1 139 ? -24.479 36.216  18.975  1.00 18.35  ? 139 ILE B CB  1 
ATOM   4750 C  CG1 . ILE B 1 139 ? -24.709 37.195  20.120  1.00 20.99  ? 139 ILE B CG1 1 
ATOM   4751 C  CG2 . ILE B 1 139 ? -23.086 35.611  19.032  1.00 18.48  ? 139 ILE B CG2 1 
ATOM   4752 C  CD1 . ILE B 1 139 ? -25.044 36.534  21.385  1.00 19.30  ? 139 ILE B CD1 1 
ATOM   4753 N  N   . GLU B 1 140 ? -23.248 36.427  15.782  1.00 16.00  ? 140 GLU B N   1 
ATOM   4754 C  CA  . GLU B 1 140 ? -22.620 35.641  14.756  1.00 18.05  ? 140 GLU B CA  1 
ATOM   4755 C  C   . GLU B 1 140 ? -21.597 34.782  15.479  1.00 16.47  ? 140 GLU B C   1 
ATOM   4756 O  O   . GLU B 1 140 ? -20.559 35.275  15.900  1.00 15.18  ? 140 GLU B O   1 
ATOM   4757 C  CB  . GLU B 1 140 ? -21.977 36.534  13.695  1.00 22.41  ? 140 GLU B CB  1 
ATOM   4758 C  CG  . GLU B 1 140 ? -22.975 37.401  12.936  1.00 24.45  ? 140 GLU B CG  1 
ATOM   4759 C  CD  . GLU B 1 140 ? -22.304 38.351  11.965  1.00 30.14  ? 140 GLU B CD  1 
ATOM   4760 O  OE1 . GLU B 1 140 ? -21.139 38.732  12.225  1.00 33.93  ? 140 GLU B OE1 1 
ATOM   4761 O  OE2 . GLU B 1 140 ? -22.929 38.686  10.944  1.00 34.04  ? 140 GLU B OE2 1 
ATOM   4762 N  N   . VAL B 1 141 ? -21.935 33.507  15.652  1.00 16.26  ? 141 VAL B N   1 
ATOM   4763 C  CA  . VAL B 1 141 ? -21.327 32.684  16.678  1.00 14.91  ? 141 VAL B CA  1 
ATOM   4764 C  C   . VAL B 1 141 ? -19.898 32.322  16.305  1.00 15.65  ? 141 VAL B C   1 
ATOM   4765 O  O   . VAL B 1 141 ? -18.982 32.630  17.065  1.00 16.63  ? 141 VAL B O   1 
ATOM   4766 C  CB  . VAL B 1 141 ? -22.155 31.420  16.956  1.00 16.41  ? 141 VAL B CB  1 
ATOM   4767 C  CG1 . VAL B 1 141 ? -21.347 30.451  17.818  1.00 17.04  ? 141 VAL B CG1 1 
ATOM   4768 C  CG2 . VAL B 1 141 ? -23.483 31.739  17.585  1.00 15.59  ? 141 VAL B CG2 1 
ATOM   4769 N  N   . PRO B 1 142 ? -19.617 31.714  15.143  1.00 16.04  ? 142 PRO B N   1 
ATOM   4770 C  CA  . PRO B 1 142 ? -18.235 31.388  14.807  1.00 15.55  ? 142 PRO B CA  1 
ATOM   4771 C  C   . PRO B 1 142 ? -17.316 32.603  14.721  1.00 15.88  ? 142 PRO B C   1 
ATOM   4772 O  O   . PRO B 1 142 ? -16.123 32.511  15.035  1.00 15.59  ? 142 PRO B O   1 
ATOM   4773 C  CB  . PRO B 1 142 ? -18.298 30.635  13.482  1.00 15.63  ? 142 PRO B CB  1 
ATOM   4774 C  CG  . PRO B 1 142 ? -19.747 30.623  13.043  1.00 17.03  ? 142 PRO B CG  1 
ATOM   4775 C  CD  . PRO B 1 142 ? -20.586 31.204  14.165  1.00 16.88  ? 142 PRO B CD  1 
ATOM   4776 N  N   . GLU B 1 143 ? -17.863 33.733  14.263  1.00 15.31  ? 143 GLU B N   1 
ATOM   4777 C  CA  . GLU B 1 143 ? -17.091 34.961  14.137  1.00 16.63  ? 143 GLU B CA  1 
ATOM   4778 C  C   . GLU B 1 143 ? -16.658 35.426  15.522  1.00 15.71  ? 143 GLU B C   1 
ATOM   4779 O  O   . GLU B 1 143 ? -15.478 35.744  15.711  1.00 16.32  ? 143 GLU B O   1 
ATOM   4780 C  CB  . GLU B 1 143 ? -17.849 36.068  13.376  1.00 18.17  ? 143 GLU B CB  1 
ATOM   4781 C  CG  . GLU B 1 143 ? -18.071 35.775  11.895  1.00 18.95  ? 143 GLU B CG  1 
ATOM   4782 C  CD  . GLU B 1 143 ? -19.242 34.846  11.568  1.00 22.62  ? 143 GLU B CD  1 
ATOM   4783 O  OE1 . GLU B 1 143 ? -19.936 34.394  12.508  1.00 21.02  ? 143 GLU B OE1 1 
ATOM   4784 O  OE2 . GLU B 1 143 ? -19.458 34.555  10.354  1.00 26.26  ? 143 GLU B OE2 1 
ATOM   4785 N  N   . ASP B 1 144 ? -17.596 35.433  16.477  1.00 14.81  ? 144 ASP B N   1 
ATOM   4786 C  CA  . ASP B 1 144 ? -17.280 35.837  17.847  1.00 15.25  ? 144 ASP B CA  1 
ATOM   4787 C  C   . ASP B 1 144 ? -16.366 34.819  18.526  1.00 15.30  ? 144 ASP B C   1 
ATOM   4788 O  O   . ASP B 1 144 ? -15.479 35.196  19.290  1.00 11.73  ? 144 ASP B O   1 
ATOM   4789 C  CB  . ASP B 1 144 ? -18.525 36.190  18.670  1.00 15.07  ? 144 ASP B CB  1 
ATOM   4790 C  CG  . ASP B 1 144 ? -18.973 37.639  18.514  1.00 16.43  ? 144 ASP B CG  1 
ATOM   4791 O  OD1 . ASP B 1 144 ? -18.177 38.442  17.913  1.00 15.39  ? 144 ASP B OD1 1 
ATOM   4792 O  OD2 . ASP B 1 144 ? -20.121 37.958  18.954  1.00 16.06  ? 144 ASP B OD2 1 
ATOM   4793 N  N   . MET B 1 145 ? -16.576 33.534  18.262  1.00 14.78  ? 145 MET B N   1 
ATOM   4794 C  CA  . MET B 1 145 ? -15.726 32.549  18.926  1.00 16.97  ? 145 MET B CA  1 
ATOM   4795 C  C   . MET B 1 145 ? -14.297 32.646  18.397  1.00 14.73  ? 145 MET B C   1 
ATOM   4796 O  O   . MET B 1 145 ? -13.405 32.442  19.188  1.00 14.54  ? 145 MET B O   1 
ATOM   4797 C  CB  . MET B 1 145 ? -16.255 31.114  18.799  1.00 18.00  ? 145 MET B CB  1 
ATOM   4798 C  CG  . MET B 1 145 ? -17.582 30.923  19.440  1.00 16.74  ? 145 MET B CG  1 
ATOM   4799 S  SD  . MET B 1 145 ? -17.641 31.241  21.183  1.00 19.01  ? 145 MET B SD  1 
ATOM   4800 C  CE  . MET B 1 145 ? -18.327 32.908  21.149  1.00 20.44  ? 145 MET B CE  1 
ATOM   4801 N  N   . THR B 1 146 ? -14.107 33.051  17.130  1.00 15.04  ? 146 THR B N   1 
ATOM   4802 C  CA  . THR B 1 146 ? -12.793 33.181  16.518  1.00 17.93  ? 146 THR B CA  1 
ATOM   4803 C  C   . THR B 1 146 ? -12.077 34.422  17.049  1.00 17.18  ? 146 THR B C   1 
ATOM   4804 O  O   . THR B 1 146 ? -10.864 34.377  17.241  1.00 18.03  ? 146 THR B O   1 
ATOM   4805 C  CB  . THR B 1 146 ? -12.884 33.138  14.983  1.00 19.80  ? 146 THR B CB  1 
ATOM   4806 O  OG1 . THR B 1 146 ? -13.474 31.880  14.667  1.00 23.40  ? 146 THR B OG1 1 
ATOM   4807 C  CG2 . THR B 1 146 ? -11.557 33.244  14.262  1.00 22.20  ? 146 THR B CG2 1 
ATOM   4808 N  N   . ARG B 1 147 ? -12.830 35.507  17.292  1.00 15.05  ? 147 ARG B N   1 
ATOM   4809 C  CA  . ARG B 1 147 ? -12.328 36.677  18.009  1.00 16.21  ? 147 ARG B CA  1 
ATOM   4810 C  C   . ARG B 1 147 ? -11.773 36.297  19.389  1.00 14.37  ? 147 ARG B C   1 
ATOM   4811 O  O   . ARG B 1 147 ? -10.615 36.624  19.731  1.00 13.78  ? 147 ARG B O   1 
ATOM   4812 C  CB  . ARG B 1 147 ? -13.439 37.739  18.176  1.00 16.43  ? 147 ARG B CB  1 
ATOM   4813 C  CG  . ARG B 1 147 ? -13.944 38.314  16.861  1.00 15.64  ? 147 ARG B CG  1 
ATOM   4814 C  CD  . ARG B 1 147 ? -14.835 39.512  17.127  1.00 17.67  ? 147 ARG B CD  1 
ATOM   4815 N  NE  . ARG B 1 147 ? -15.081 40.297  15.913  1.00 19.40  ? 147 ARG B NE  1 
ATOM   4816 C  CZ  . ARG B 1 147 ? -16.183 40.212  15.174  1.00 21.49  ? 147 ARG B CZ  1 
ATOM   4817 N  NH1 . ARG B 1 147 ? -17.111 39.310  15.463  1.00 23.28  ? 147 ARG B NH1 1 
ATOM   4818 N  NH2 . ARG B 1 147 ? -16.323 40.973  14.102  1.00 22.81  ? 147 ARG B NH2 1 
ATOM   4819 N  N   . LEU B 1 148 ? -12.557 35.525  20.151  1.00 13.68  ? 148 LEU B N   1 
ATOM   4820 C  CA  . LEU B 1 148 ? -12.128 35.113  21.477  1.00 12.87  ? 148 LEU B CA  1 
ATOM   4821 C  C   . LEU B 1 148 ? -10.861 34.263  21.418  1.00 12.85  ? 148 LEU B C   1 
ATOM   4822 O  O   . LEU B 1 148 ? -9.919  34.514  22.182  1.00 13.27  ? 148 LEU B O   1 
ATOM   4823 C  CB  . LEU B 1 148 ? -13.248 34.363  22.179  1.00 14.49  ? 148 LEU B CB  1 
ATOM   4824 C  CG  . LEU B 1 148 ? -12.882 33.788  23.548  1.00 15.21  ? 148 LEU B CG  1 
ATOM   4825 C  CD1 . LEU B 1 148 ? -13.756 34.274  24.664  1.00 16.23  ? 148 LEU B CD1 1 
ATOM   4826 C  CD2 . LEU B 1 148 ? -12.878 32.272  23.510  1.00 17.58  ? 148 LEU B CD2 1 
ATOM   4827 N  N   . THR B 1 149 ? -10.794 33.290  20.509  1.00 13.35  ? 149 THR B N   1 
ATOM   4828 C  CA  . THR B 1 149 ? -9.717  32.308  20.579  1.00 13.20  ? 149 THR B CA  1 
ATOM   4829 C  C   . THR B 1 149 ? -8.427  32.884  20.030  1.00 14.85  ? 149 THR B C   1 
ATOM   4830 O  O   . THR B 1 149 ? -7.352  32.602  20.602  1.00 13.63  ? 149 THR B O   1 
ATOM   4831 C  CB  . THR B 1 149 ? -10.079 30.946  19.954  1.00 13.40  ? 149 THR B CB  1 
ATOM   4832 O  OG1 . THR B 1 149 ? -10.364 31.090  18.565  1.00 12.61  ? 149 THR B OG1 1 
ATOM   4833 C  CG2 . THR B 1 149 ? -11.258 30.322  20.650  1.00 12.26  ? 149 THR B CG2 1 
ATOM   4834 N  N   . LEU B 1 150 ? -8.516  33.642  18.934  1.00 14.75  ? 150 LEU B N   1 
ATOM   4835 C  CA  . LEU B 1 150 ? -7.350  34.351  18.440  1.00 15.39  ? 150 LEU B CA  1 
ATOM   4836 C  C   . LEU B 1 150 ? -6.795  35.272  19.531  1.00 15.20  ? 150 LEU B C   1 
ATOM   4837 O  O   . LEU B 1 150 ? -5.592  35.242  19.808  1.00 15.49  ? 150 LEU B O   1 
ATOM   4838 C  CB  . LEU B 1 150 ? -7.682  35.117  17.161  1.00 16.45  ? 150 LEU B CB  1 
ATOM   4839 C  CG  . LEU B 1 150 ? -6.531  35.947  16.582  1.00 16.60  ? 150 LEU B CG  1 
ATOM   4840 C  CD1 . LEU B 1 150 ? -5.345  35.083  16.136  1.00 17.86  ? 150 LEU B CD1 1 
ATOM   4841 C  CD2 . LEU B 1 150 ? -7.026  36.762  15.419  1.00 16.94  ? 150 LEU B CD2 1 
ATOM   4842 N  N   . ASP B 1 151 ? -7.651  36.057  20.171  1.00 14.49  ? 151 ASP B N   1 
ATOM   4843 C  CA  . ASP B 1 151 ? -7.182  36.987  21.191  1.00 15.54  ? 151 ASP B CA  1 
ATOM   4844 C  C   . ASP B 1 151 ? -6.582  36.227  22.380  1.00 14.21  ? 151 ASP B C   1 
ATOM   4845 O  O   . ASP B 1 151 ? -5.601  36.669  22.982  1.00 11.30  ? 151 ASP B O   1 
ATOM   4846 C  CB  . ASP B 1 151 ? -8.253  37.996  21.608  1.00 17.76  ? 151 ASP B CB  1 
ATOM   4847 C  CG  . ASP B 1 151 ? -8.497  39.156  20.633  1.00 21.88  ? 151 ASP B CG  1 
ATOM   4848 O  OD1 . ASP B 1 151 ? -8.203  39.017  19.418  1.00 23.92  ? 151 ASP B OD1 1 
ATOM   4849 O  OD2 . ASP B 1 151 ? -8.998  40.219  21.095  1.00 25.93  ? 151 ASP B OD2 1 
ATOM   4850 N  N   . THR B 1 152 ? -7.182  35.091  22.745  1.00 13.92  ? 152 THR B N   1 
ATOM   4851 C  CA  . THR B 1 152 ? -6.724  34.333  23.900  1.00 13.91  ? 152 THR B CA  1 
ATOM   4852 C  C   . THR B 1 152 ? -5.290  33.841  23.675  1.00 13.43  ? 152 THR B C   1 
ATOM   4853 O  O   . THR B 1 152 ? -4.443  34.010  24.542  1.00 14.14  ? 152 THR B O   1 
ATOM   4854 C  CB  . THR B 1 152 ? -7.729  33.234  24.284  1.00 14.54  ? 152 THR B CB  1 
ATOM   4855 O  OG1 . THR B 1 152 ? -9.010  33.772  24.637  1.00 18.01  ? 152 THR B OG1 1 
ATOM   4856 C  CG2 . THR B 1 152 ? -7.250  32.451  25.469  1.00 15.34  ? 152 THR B CG2 1 
ATOM   4857 N  N   . ILE B 1 153 ? -4.989  33.265  22.512  1.00 14.23  ? 153 ILE B N   1 
ATOM   4858 C  CA  . ILE B 1 153 ? -3.678  32.692  22.285  1.00 15.47  ? 153 ILE B CA  1 
ATOM   4859 C  C   . ILE B 1 153 ? -2.705  33.844  22.108  1.00 17.04  ? 153 ILE B C   1 
ATOM   4860 O  O   . ILE B 1 153 ? -1.586  33.769  22.580  1.00 14.88  ? 153 ILE B O   1 
ATOM   4861 C  CB  . ILE B 1 153 ? -3.609  31.717  21.088  1.00 15.41  ? 153 ILE B CB  1 
ATOM   4862 C  CG1 . ILE B 1 153 ? -2.219  31.067  20.978  1.00 16.17  ? 153 ILE B CG1 1 
ATOM   4863 C  CG2 . ILE B 1 153 ? -4.010  32.359  19.768  1.00 16.35  ? 153 ILE B CG2 1 
ATOM   4864 C  CD1 . ILE B 1 153 ? -1.658  30.532  22.297  1.00 16.42  ? 153 ILE B CD1 1 
ATOM   4865 N  N   . GLY B 1 154 ? -3.169  34.926  21.484  1.00 16.45  ? 154 GLY B N   1 
ATOM   4866 C  CA  . GLY B 1 154 ? -2.282  36.068  21.343  1.00 16.94  ? 154 GLY B CA  1 
ATOM   4867 C  C   . GLY B 1 154 ? -1.827  36.570  22.708  1.00 15.92  ? 154 GLY B C   1 
ATOM   4868 O  O   . GLY B 1 154 ? -0.640  36.754  22.964  1.00 14.71  ? 154 GLY B O   1 
ATOM   4869 N  N   . LEU B 1 155 ? -2.761  36.737  23.635  1.00 15.90  ? 155 LEU B N   1 
ATOM   4870 C  CA  . LEU B 1 155 ? -2.418  37.367  24.907  1.00 17.84  ? 155 LEU B CA  1 
ATOM   4871 C  C   . LEU B 1 155 ? -1.711  36.370  25.851  1.00 17.26  ? 155 LEU B C   1 
ATOM   4872 O  O   . LEU B 1 155 ? -0.662  36.663  26.443  1.00 16.54  ? 155 LEU B O   1 
ATOM   4873 C  CB  . LEU B 1 155 ? -3.690  37.965  25.536  1.00 18.24  ? 155 LEU B CB  1 
ATOM   4874 C  CG  . LEU B 1 155 ? -3.499  38.729  26.856  1.00 20.91  ? 155 LEU B CG  1 
ATOM   4875 C  CD1 . LEU B 1 155 ? -2.592  39.927  26.666  1.00 20.50  ? 155 LEU B CD1 1 
ATOM   4876 C  CD2 . LEU B 1 155 ? -4.821  39.213  27.439  1.00 21.25  ? 155 LEU B CD2 1 
ATOM   4877 N  N   . CYS B 1 156 ? -2.275  35.167  26.009  1.00 16.73  ? 156 CYS B N   1 
ATOM   4878 C  CA  . CYS B 1 156 ? -1.734  34.176  26.937  1.00 16.93  ? 156 CYS B CA  1 
ATOM   4879 C  C   . CYS B 1 156 ? -0.341  33.751  26.491  1.00 17.49  ? 156 CYS B C   1 
ATOM   4880 O  O   . CYS B 1 156 ? 0.517   33.540  27.326  1.00 17.36  ? 156 CYS B O   1 
ATOM   4881 C  CB  . CYS B 1 156 ? -2.624  32.946  27.031  1.00 19.07  ? 156 CYS B CB  1 
ATOM   4882 S  SG  . CYS B 1 156 ? -4.190  33.298  27.853  1.00 20.77  ? 156 CYS B SG  1 
ATOM   4883 N  N   . GLY B 1 157 ? -0.143  33.631  25.173  1.00 16.55  ? 157 GLY B N   1 
ATOM   4884 C  CA  . GLY B 1 157 ? 1.055   33.057  24.604  1.00 15.71  ? 157 GLY B CA  1 
ATOM   4885 C  C   . GLY B 1 157 ? 2.164   34.079  24.435  1.00 15.92  ? 157 GLY B C   1 
ATOM   4886 O  O   . GLY B 1 157 ? 3.319   33.758  24.632  1.00 15.75  ? 157 GLY B O   1 
ATOM   4887 N  N   . PHE B 1 158 ? 1.787   35.321  24.079  1.00 15.73  ? 158 PHE B N   1 
ATOM   4888 C  CA  . PHE B 1 158 ? 2.704   36.249  23.456  1.00 16.52  ? 158 PHE B CA  1 
ATOM   4889 C  C   . PHE B 1 158 ? 2.555   37.673  23.999  1.00 17.30  ? 158 PHE B C   1 
ATOM   4890 O  O   . PHE B 1 158 ? 3.295   38.559  23.587  1.00 16.55  ? 158 PHE B O   1 
ATOM   4891 C  CB  . PHE B 1 158 ? 2.514   36.210  21.941  1.00 17.15  ? 158 PHE B CB  1 
ATOM   4892 C  CG  . PHE B 1 158 ? 2.733   34.856  21.336  1.00 16.91  ? 158 PHE B CG  1 
ATOM   4893 C  CD1 . PHE B 1 158 ? 4.008   34.395  21.092  1.00 18.73  ? 158 PHE B CD1 1 
ATOM   4894 C  CD2 . PHE B 1 158 ? 1.655   34.026  21.056  1.00 18.58  ? 158 PHE B CD2 1 
ATOM   4895 C  CE1 . PHE B 1 158 ? 4.199   33.131  20.569  1.00 18.90  ? 158 PHE B CE1 1 
ATOM   4896 C  CE2 . PHE B 1 158 ? 1.848   32.738  20.571  1.00 19.83  ? 158 PHE B CE2 1 
ATOM   4897 C  CZ  . PHE B 1 158 ? 3.122   32.299  20.304  1.00 17.85  ? 158 PHE B CZ  1 
ATOM   4898 N  N   . ASN B 1 159 ? 1.611   37.870  24.912  1.00 18.09  ? 159 ASN B N   1 
ATOM   4899 C  CA  . ASN B 1 159 ? 1.318   39.169  25.486  1.00 19.14  ? 159 ASN B CA  1 
ATOM   4900 C  C   . ASN B 1 159 ? 1.063   40.168  24.363  1.00 20.34  ? 159 ASN B C   1 
ATOM   4901 O  O   . ASN B 1 159 ? 1.450   41.329  24.474  1.00 21.92  ? 159 ASN B O   1 
ATOM   4902 C  CB  . ASN B 1 159 ? 2.455   39.599  26.422  1.00 20.91  ? 159 ASN B CB  1 
ATOM   4903 C  CG  . ASN B 1 159 ? 2.043   40.706  27.361  1.00 23.38  ? 159 ASN B CG  1 
ATOM   4904 O  OD1 . ASN B 1 159 ? 0.923   40.719  27.865  1.00 25.61  ? 159 ASN B OD1 1 
ATOM   4905 N  ND2 . ASN B 1 159 ? 2.916   41.683  27.528  1.00 27.93  ? 159 ASN B ND2 1 
ATOM   4906 N  N   . TYR B 1 160 ? 0.437   39.686  23.278  1.00 19.36  ? 160 TYR B N   1 
ATOM   4907 C  CA  . TYR B 1 160 ? 0.079   40.466  22.106  1.00 19.31  ? 160 TYR B CA  1 
ATOM   4908 C  C   . TYR B 1 160 ? -1.445  40.565  22.076  1.00 19.48  ? 160 TYR B C   1 
ATOM   4909 O  O   . TYR B 1 160 ? -2.142  39.548  22.201  1.00 16.87  ? 160 TYR B O   1 
ATOM   4910 C  CB  . TYR B 1 160 ? 0.673   39.866  20.827  1.00 19.55  ? 160 TYR B CB  1 
ATOM   4911 C  CG  . TYR B 1 160 ? 0.443   40.760  19.625  1.00 22.56  ? 160 TYR B CG  1 
ATOM   4912 C  CD1 . TYR B 1 160 ? 1.171   41.936  19.463  1.00 26.14  ? 160 TYR B CD1 1 
ATOM   4913 C  CD2 . TYR B 1 160 ? -0.584  40.497  18.729  1.00 22.90  ? 160 TYR B CD2 1 
ATOM   4914 C  CE1 . TYR B 1 160 ? 0.919   42.798  18.405  1.00 29.54  ? 160 TYR B CE1 1 
ATOM   4915 C  CE2 . TYR B 1 160 ? -0.878  41.365  17.695  1.00 25.84  ? 160 TYR B CE2 1 
ATOM   4916 C  CZ  . TYR B 1 160 ? -0.107  42.504  17.526  1.00 27.82  ? 160 TYR B CZ  1 
ATOM   4917 O  OH  . TYR B 1 160 ? -0.357  43.301  16.477  1.00 31.93  ? 160 TYR B OH  1 
ATOM   4918 N  N   . ARG B 1 161 ? -1.955  41.790  21.868  1.00 16.13  ? 161 ARG B N   1 
ATOM   4919 C  CA  . ARG B 1 161 ? -3.389  42.020  21.788  1.00 15.16  ? 161 ARG B CA  1 
ATOM   4920 C  C   . ARG B 1 161 ? -3.803  42.227  20.336  1.00 16.82  ? 161 ARG B C   1 
ATOM   4921 O  O   . ARG B 1 161 ? -3.519  43.249  19.691  1.00 18.28  ? 161 ARG B O   1 
ATOM   4922 C  CB  . ARG B 1 161 ? -3.780  43.168  22.721  1.00 16.15  ? 161 ARG B CB  1 
ATOM   4923 C  CG  . ARG B 1 161 ? -3.611  42.800  24.186  1.00 15.99  ? 161 ARG B CG  1 
ATOM   4924 C  CD  . ARG B 1 161 ? -4.355  43.710  25.096  1.00 16.97  ? 161 ARG B CD  1 
ATOM   4925 N  NE  . ARG B 1 161 ? -4.225  43.359  26.496  1.00 15.99  ? 161 ARG B NE  1 
ATOM   4926 C  CZ  . ARG B 1 161 ? -5.225  42.975  27.257  1.00 16.52  ? 161 ARG B CZ  1 
ATOM   4927 N  NH1 . ARG B 1 161 ? -6.411  42.734  26.728  1.00 18.95  ? 161 ARG B NH1 1 
ATOM   4928 N  NH2 . ARG B 1 161 ? -5.030  42.766  28.543  1.00 16.33  ? 161 ARG B NH2 1 
ATOM   4929 N  N   . PHE B 1 162 ? -4.508  41.217  19.810  1.00 15.20  ? 162 PHE B N   1 
ATOM   4930 C  CA  . PHE B 1 162 ? -5.131  41.309  18.508  1.00 14.93  ? 162 PHE B CA  1 
ATOM   4931 C  C   . PHE B 1 162 ? -6.298  42.293  18.512  1.00 13.48  ? 162 PHE B C   1 
ATOM   4932 O  O   . PHE B 1 162 ? -6.619  42.807  17.443  1.00 14.76  ? 162 PHE B O   1 
ATOM   4933 C  CB  . PHE B 1 162 ? -5.625  39.939  18.076  1.00 15.79  ? 162 PHE B CB  1 
ATOM   4934 C  CG  . PHE B 1 162 ? -4.523  39.051  17.580  1.00 14.78  ? 162 PHE B CG  1 
ATOM   4935 C  CD1 . PHE B 1 162 ? -3.977  39.253  16.321  1.00 17.90  ? 162 PHE B CD1 1 
ATOM   4936 C  CD2 . PHE B 1 162 ? -3.936  38.124  18.414  1.00 14.92  ? 162 PHE B CD2 1 
ATOM   4937 C  CE1 . PHE B 1 162 ? -2.922  38.465  15.877  1.00 18.68  ? 162 PHE B CE1 1 
ATOM   4938 C  CE2 . PHE B 1 162 ? -2.933  37.286  17.940  1.00 15.68  ? 162 PHE B CE2 1 
ATOM   4939 C  CZ  . PHE B 1 162 ? -2.418  37.467  16.681  1.00 16.80  ? 162 PHE B CZ  1 
ATOM   4940 N  N   . ASN B 1 163 ? -6.881  42.539  19.688  1.00 12.74  ? 163 ASN B N   1 
ATOM   4941 C  CA  . ASN B 1 163 ? -8.010  43.450  19.852  1.00 13.77  ? 163 ASN B CA  1 
ATOM   4942 C  C   . ASN B 1 163 ? -9.119  43.160  18.820  1.00 15.55  ? 163 ASN B C   1 
ATOM   4943 O  O   . ASN B 1 163 ? -9.723  44.056  18.202  1.00 16.55  ? 163 ASN B O   1 
ATOM   4944 C  CB  . ASN B 1 163 ? -7.482  44.886  19.816  1.00 14.94  ? 163 ASN B CB  1 
ATOM   4945 C  CG  . ASN B 1 163 ? -6.720  45.219  21.078  1.00 14.27  ? 163 ASN B CG  1 
ATOM   4946 O  OD1 . ASN B 1 163 ? -7.171  44.927  22.188  1.00 16.10  ? 163 ASN B OD1 1 
ATOM   4947 N  ND2 . ASN B 1 163 ? -5.527  45.763  20.918  1.00 16.40  ? 163 ASN B ND2 1 
ATOM   4948 N  N   . SER B 1 164 ? -9.446  41.885  18.663  1.00 15.32  ? 164 SER B N   1 
ATOM   4949 C  CA  . SER B 1 164 ? -10.436 41.420  17.700  1.00 16.20  ? 164 SER B CA  1 
ATOM   4950 C  C   . SER B 1 164 ? -11.839 41.935  17.994  1.00 17.23  ? 164 SER B C   1 
ATOM   4951 O  O   . SER B 1 164 ? -12.606 42.038  17.049  1.00 19.34  ? 164 SER B O   1 
ATOM   4952 C  CB  . SER B 1 164 ? -10.498 39.932  17.681  1.00 16.83  ? 164 SER B CB  1 
ATOM   4953 O  OG  . SER B 1 164 ? -9.219  39.379  17.379  1.00 17.41  ? 164 SER B OG  1 
ATOM   4954 N  N   . PHE B 1 165 ? -12.213 42.115  19.278  1.00 16.04  ? 165 PHE B N   1 
ATOM   4955 C  CA  . PHE B 1 165 ? -13.526 42.657  19.621  1.00 17.53  ? 165 PHE B CA  1 
ATOM   4956 C  C   . PHE B 1 165 ? -13.633 44.162  19.311  1.00 19.41  ? 165 PHE B C   1 
ATOM   4957 O  O   . PHE B 1 165 ? -14.720 44.714  19.465  1.00 20.32  ? 165 PHE B O   1 
ATOM   4958 C  CB  . PHE B 1 165 ? -13.893 42.372  21.084  1.00 17.15  ? 165 PHE B CB  1 
ATOM   4959 C  CG  . PHE B 1 165 ? -14.187 40.921  21.387  1.00 16.97  ? 165 PHE B CG  1 
ATOM   4960 C  CD1 . PHE B 1 165 ? -15.290 40.292  20.838  1.00 18.18  ? 165 PHE B CD1 1 
ATOM   4961 C  CD2 . PHE B 1 165 ? -13.282 40.149  22.124  1.00 17.61  ? 165 PHE B CD2 1 
ATOM   4962 C  CE1 . PHE B 1 165 ? -15.534 38.946  21.104  1.00 18.88  ? 165 PHE B CE1 1 
ATOM   4963 C  CE2 . PHE B 1 165 ? -13.525 38.810  22.398  1.00 17.00  ? 165 PHE B CE2 1 
ATOM   4964 C  CZ  . PHE B 1 165 ? -14.640 38.201  21.857  1.00 17.83  ? 165 PHE B CZ  1 
ATOM   4965 N  N   . TYR B 1 166 ? -12.541 44.825  18.896  1.00 16.10  ? 166 TYR B N   1 
ATOM   4966 C  CA  . TYR B 1 166 ? -12.582 46.222  18.471  1.00 18.98  ? 166 TYR B CA  1 
ATOM   4967 C  C   . TYR B 1 166 ? -12.739 46.296  16.952  1.00 21.39  ? 166 TYR B C   1 
ATOM   4968 O  O   . TYR B 1 166 ? -12.703 47.375  16.398  1.00 23.35  ? 166 TYR B O   1 
ATOM   4969 C  CB  . TYR B 1 166 ? -11.341 47.005  18.941  1.00 17.30  ? 166 TYR B CB  1 
ATOM   4970 C  CG  . TYR B 1 166 ? -11.336 47.182  20.459  1.00 17.98  ? 166 TYR B CG  1 
ATOM   4971 C  CD1 . TYR B 1 166 ? -10.795 46.206  21.295  1.00 16.94  ? 166 TYR B CD1 1 
ATOM   4972 C  CD2 . TYR B 1 166 ? -11.958 48.269  21.073  1.00 14.76  ? 166 TYR B CD2 1 
ATOM   4973 C  CE1 . TYR B 1 166 ? -10.814 46.327  22.674  1.00 16.52  ? 166 TYR B CE1 1 
ATOM   4974 C  CE2 . TYR B 1 166 ? -12.009 48.382  22.448  1.00 15.25  ? 166 TYR B CE2 1 
ATOM   4975 C  CZ  . TYR B 1 166 ? -11.407 47.426  23.265  1.00 16.53  ? 166 TYR B CZ  1 
ATOM   4976 O  OH  . TYR B 1 166 ? -11.455 47.501  24.647  1.00 15.30  ? 166 TYR B OH  1 
ATOM   4977 N  N   . ARG B 1 167 ? -12.935 45.147  16.287  1.00 23.36  ? 167 ARG B N   1 
ATOM   4978 C  CA  . ARG B 1 167 ? -12.835 45.046  14.843  1.00 25.64  ? 167 ARG B CA  1 
ATOM   4979 C  C   . ARG B 1 167 ? -14.123 44.447  14.286  1.00 30.37  ? 167 ARG B C   1 
ATOM   4980 O  O   . ARG B 1 167 ? -14.670 43.485  14.847  1.00 28.39  ? 167 ARG B O   1 
ATOM   4981 C  CB  . ARG B 1 167 ? -11.673 44.130  14.445  1.00 26.37  ? 167 ARG B CB  1 
ATOM   4982 C  CG  . ARG B 1 167 ? -10.280 44.685  14.694  1.00 27.28  ? 167 ARG B CG  1 
ATOM   4983 C  CD  . ARG B 1 167 ? -9.255  43.598  14.413  1.00 28.39  ? 167 ARG B CD  1 
ATOM   4984 N  NE  . ARG B 1 167 ? -7.993  43.937  15.040  1.00 29.35  ? 167 ARG B NE  1 
ATOM   4985 C  CZ  . ARG B 1 167 ? -7.102  44.828  14.601  1.00 29.36  ? 167 ARG B CZ  1 
ATOM   4986 N  NH1 . ARG B 1 167 ? -7.159  45.319  13.368  1.00 26.42  ? 167 ARG B NH1 1 
ATOM   4987 N  NH2 . ARG B 1 167 ? -6.084  45.138  15.390  1.00 28.85  ? 167 ARG B NH2 1 
ATOM   4988 N  N   . ASP B 1 168 ? -14.595 45.053  13.191  1.00 34.80  ? 168 ASP B N   1 
ATOM   4989 C  CA  . ASP B 1 168 ? -15.669 44.515  12.366  1.00 46.53  ? 168 ASP B CA  1 
ATOM   4990 C  C   . ASP B 1 168 ? -15.172 43.327  11.544  1.00 44.10  ? 168 ASP B C   1 
ATOM   4991 O  O   . ASP B 1 168 ? -15.892 42.352  11.369  1.00 49.78  ? 168 ASP B O   1 
ATOM   4992 C  CB  . ASP B 1 168 ? -16.197 45.570  11.383  1.00 52.61  ? 168 ASP B CB  1 
ATOM   4993 C  CG  . ASP B 1 168 ? -17.248 46.482  11.978  1.00 58.24  ? 168 ASP B CG  1 
ATOM   4994 O  OD1 . ASP B 1 168 ? -18.178 45.942  12.621  1.00 61.29  ? 168 ASP B OD1 1 
ATOM   4995 O  OD2 . ASP B 1 168 ? -17.140 47.717  11.776  1.00 64.96  ? 168 ASP B OD2 1 
ATOM   4996 N  N   . GLN B 1 169 ? -13.954 43.446  11.014  1.00 45.16  ? 169 GLN B N   1 
ATOM   4997 C  CA  . GLN B 1 169 ? -13.393 42.446  10.126  1.00 49.92  ? 169 GLN B CA  1 
ATOM   4998 C  C   . GLN B 1 169 ? -12.227 41.746  10.819  1.00 46.49  ? 169 GLN B C   1 
ATOM   4999 O  O   . GLN B 1 169 ? -11.498 42.343  11.617  1.00 40.36  ? 169 GLN B O   1 
ATOM   5000 C  CB  . GLN B 1 169 ? -12.962 43.102  8.811   1.00 62.43  ? 169 GLN B CB  1 
ATOM   5001 C  CG  . GLN B 1 169 ? -14.112 43.736  8.028   1.00 67.79  ? 169 GLN B CG  1 
ATOM   5002 C  CD  . GLN B 1 169 ? -15.225 42.759  7.714   1.00 79.59  ? 169 GLN B CD  1 
ATOM   5003 O  OE1 . GLN B 1 169 ? -14.992 41.636  7.266   1.00 80.07  ? 169 GLN B OE1 1 
ATOM   5004 N  NE2 . GLN B 1 169 ? -16.457 43.177  7.963   1.00 86.61  ? 169 GLN B NE2 1 
ATOM   5005 N  N   . PRO B 1 170 ? -12.013 40.442  10.548  1.00 38.60  ? 170 PRO B N   1 
ATOM   5006 C  CA  . PRO B 1 170 ? -10.889 39.719  11.148  1.00 38.95  ? 170 PRO B CA  1 
ATOM   5007 C  C   . PRO B 1 170 ? -9.584  40.520  11.071  1.00 37.03  ? 170 PRO B C   1 
ATOM   5008 O  O   . PRO B 1 170 ? -9.395  41.330  10.161  1.00 38.68  ? 170 PRO B O   1 
ATOM   5009 C  CB  . PRO B 1 170 ? -10.838 38.425  10.315  1.00 40.77  ? 170 PRO B CB  1 
ATOM   5010 C  CG  . PRO B 1 170 ? -12.282 38.205  9.849   1.00 41.39  ? 170 PRO B CG  1 
ATOM   5011 C  CD  . PRO B 1 170 ? -12.838 39.603  9.656   1.00 43.89  ? 170 PRO B CD  1 
ATOM   5012 N  N   . HIS B 1 171 ? -8.698  40.324  12.055  1.00 31.96  ? 171 HIS B N   1 
ATOM   5013 C  CA  . HIS B 1 171 ? -7.389  40.954  12.047  1.00 30.05  ? 171 HIS B CA  1 
ATOM   5014 C  C   . HIS B 1 171 ? -6.671  40.514  10.774  1.00 33.63  ? 171 HIS B C   1 
ATOM   5015 O  O   . HIS B 1 171 ? -6.863  39.385  10.318  1.00 34.36  ? 171 HIS B O   1 
ATOM   5016 C  CB  . HIS B 1 171 ? -6.659  40.608  13.347  1.00 28.27  ? 171 HIS B CB  1 
ATOM   5017 C  CG  . HIS B 1 171 ? -5.278  41.153  13.527  1.00 28.10  ? 171 HIS B CG  1 
ATOM   5018 N  ND1 . HIS B 1 171 ? -4.170  40.802  12.785  1.00 28.33  ? 171 HIS B ND1 1 
ATOM   5019 C  CD2 . HIS B 1 171 ? -4.841  41.992  14.471  1.00 25.57  ? 171 HIS B CD2 1 
ATOM   5020 C  CE1 . HIS B 1 171 ? -3.120  41.466  13.239  1.00 26.70  ? 171 HIS B CE1 1 
ATOM   5021 N  NE2 . HIS B 1 171 ? -3.507  42.183  14.271  1.00 25.64  ? 171 HIS B NE2 1 
ATOM   5022 N  N   . PRO B 1 172 ? -5.847  41.398  10.169  1.00 38.12  ? 172 PRO B N   1 
ATOM   5023 C  CA  . PRO B 1 172 ? -5.114  41.092  8.942   1.00 40.06  ? 172 PRO B CA  1 
ATOM   5024 C  C   . PRO B 1 172 ? -4.390  39.752  8.947   1.00 43.22  ? 172 PRO B C   1 
ATOM   5025 O  O   . PRO B 1 172 ? -4.345  39.064  7.922   1.00 43.87  ? 172 PRO B O   1 
ATOM   5026 C  CB  . PRO B 1 172 ? -4.068  42.216  8.904   1.00 38.97  ? 172 PRO B CB  1 
ATOM   5027 C  CG  . PRO B 1 172 ? -4.797  43.381  9.488   1.00 36.70  ? 172 PRO B CG  1 
ATOM   5028 C  CD  . PRO B 1 172 ? -5.610  42.782  10.613  1.00 39.72  ? 172 PRO B CD  1 
ATOM   5029 N  N   . PHE B 1 173 ? -3.804  39.415  10.107  1.00 38.94  ? 173 PHE B N   1 
ATOM   5030 C  CA  . PHE B 1 173 ? -3.071  38.170  10.257  1.00 37.68  ? 173 PHE B CA  1 
ATOM   5031 C  C   . PHE B 1 173 ? -3.959  36.989  9.876   1.00 34.35  ? 173 PHE B C   1 
ATOM   5032 O  O   . PHE B 1 173 ? -3.501  36.094  9.179   1.00 33.31  ? 173 PHE B O   1 
ATOM   5033 C  CB  . PHE B 1 173 ? -2.523  38.018  11.682  1.00 37.98  ? 173 PHE B CB  1 
ATOM   5034 C  CG  . PHE B 1 173 ? -1.777  36.727  11.912  1.00 37.05  ? 173 PHE B CG  1 
ATOM   5035 C  CD1 . PHE B 1 173 ? -2.449  35.575  12.294  1.00 36.95  ? 173 PHE B CD1 1 
ATOM   5036 C  CD2 . PHE B 1 173 ? -0.409  36.658  11.692  1.00 37.95  ? 173 PHE B CD2 1 
ATOM   5037 C  CE1 . PHE B 1 173 ? -1.757  34.391  12.480  1.00 40.11  ? 173 PHE B CE1 1 
ATOM   5038 C  CE2 . PHE B 1 173 ? 0.285   35.473  11.880  1.00 35.81  ? 173 PHE B CE2 1 
ATOM   5039 C  CZ  . PHE B 1 173 ? -0.392  34.340  12.271  1.00 36.14  ? 173 PHE B CZ  1 
ATOM   5040 N  N   . ILE B 1 174 ? -5.211  36.994  10.350  1.00 36.44  ? 174 ILE B N   1 
ATOM   5041 C  CA  . ILE B 1 174 ? -6.152  35.913  10.099  1.00 38.96  ? 174 ILE B CA  1 
ATOM   5042 C  C   . ILE B 1 174 ? -6.617  35.914  8.644   1.00 36.12  ? 174 ILE B C   1 
ATOM   5043 O  O   . ILE B 1 174 ? -6.768  34.845  8.055   1.00 36.61  ? 174 ILE B O   1 
ATOM   5044 C  CB  . ILE B 1 174 ? -7.335  35.959  11.092  1.00 47.10  ? 174 ILE B CB  1 
ATOM   5045 C  CG1 . ILE B 1 174 ? -7.074  35.001  12.260  1.00 53.79  ? 174 ILE B CG1 1 
ATOM   5046 C  CG2 . ILE B 1 174 ? -8.664  35.648  10.411  1.00 52.54  ? 174 ILE B CG2 1 
ATOM   5047 C  CD1 . ILE B 1 174 ? -8.330  34.492  12.956  1.00 51.38  ? 174 ILE B CD1 1 
ATOM   5048 N  N   . THR B 1 175 ? -6.855  37.100  8.071   1.00 35.62  ? 175 THR B N   1 
ATOM   5049 C  CA  . THR B 1 175 ? -7.213  37.221  6.661   1.00 36.58  ? 175 THR B CA  1 
ATOM   5050 C  C   . THR B 1 175 ? -6.135  36.569  5.803   1.00 36.05  ? 175 THR B C   1 
ATOM   5051 O  O   . THR B 1 175 ? -6.437  35.746  4.949   1.00 32.83  ? 175 THR B O   1 
ATOM   5052 C  CB  . THR B 1 175 ? -7.432  38.686  6.258   1.00 37.92  ? 175 THR B CB  1 
ATOM   5053 O  OG1 . THR B 1 175 ? -8.633  39.118  6.884   1.00 39.62  ? 175 THR B OG1 1 
ATOM   5054 C  CG2 . THR B 1 175 ? -7.611  38.900  4.776   1.00 38.33  ? 175 THR B CG2 1 
ATOM   5055 N  N   . SER B 1 176 ? -4.878  36.944  6.043   1.00 35.45  ? 176 SER B N   1 
ATOM   5056 C  CA  . SER B 1 176 ? -3.757  36.335  5.351   1.00 38.01  ? 176 SER B CA  1 
ATOM   5057 C  C   . SER B 1 176 ? -3.712  34.820  5.580   1.00 37.45  ? 176 SER B C   1 
ATOM   5058 O  O   . SER B 1 176 ? -3.626  34.050  4.629   1.00 37.92  ? 176 SER B O   1 
ATOM   5059 C  CB  . SER B 1 176 ? -2.479  36.989  5.767   1.00 38.00  ? 176 SER B CB  1 
ATOM   5060 O  OG  . SER B 1 176 ? -2.491  38.349  5.379   1.00 41.38  ? 176 SER B OG  1 
ATOM   5061 N  N   . MET B 1 177 ? -3.788  34.404  6.845   1.00 36.78  ? 177 MET B N   1 
ATOM   5062 C  CA  . MET B 1 177 ? -3.749  33.003  7.218   1.00 42.26  ? 177 MET B CA  1 
ATOM   5063 C  C   . MET B 1 177 ? -4.800  32.225  6.419   1.00 36.66  ? 177 MET B C   1 
ATOM   5064 O  O   . MET B 1 177 ? -4.483  31.239  5.763   1.00 30.13  ? 177 MET B O   1 
ATOM   5065 C  CB  . MET B 1 177 ? -4.005  32.862  8.726   1.00 45.46  ? 177 MET B CB  1 
ATOM   5066 C  CG  . MET B 1 177 ? -4.205  31.442  9.214   1.00 53.06  ? 177 MET B CG  1 
ATOM   5067 S  SD  . MET B 1 177 ? -2.708  30.448  9.013   1.00 72.46  ? 177 MET B SD  1 
ATOM   5068 C  CE  . MET B 1 177 ? -1.768  31.007  10.435  1.00 72.60  ? 177 MET B CE  1 
ATOM   5069 N  N   . VAL B 1 178 ? -6.051  32.688  6.474   1.00 34.55  ? 178 VAL B N   1 
ATOM   5070 C  CA  . VAL B 1 178 ? -7.156  32.006  5.824   1.00 36.58  ? 178 VAL B CA  1 
ATOM   5071 C  C   . VAL B 1 178 ? -6.994  32.021  4.301   1.00 35.03  ? 178 VAL B C   1 
ATOM   5072 O  O   . VAL B 1 178 ? -7.312  31.039  3.630   1.00 35.47  ? 178 VAL B O   1 
ATOM   5073 C  CB  . VAL B 1 178 ? -8.510  32.601  6.256   1.00 39.45  ? 178 VAL B CB  1 
ATOM   5074 C  CG1 . VAL B 1 178 ? -9.611  32.321  5.237   1.00 38.80  ? 178 VAL B CG1 1 
ATOM   5075 C  CG2 . VAL B 1 178 ? -8.896  32.096  7.645   1.00 36.01  ? 178 VAL B CG2 1 
ATOM   5076 N  N   . ARG B 1 179 ? -6.452  33.103  3.758   1.00 32.23  ? 179 ARG B N   1 
ATOM   5077 C  CA  . ARG B 1 179 ? -6.209  33.147  2.329   1.00 36.69  ? 179 ARG B CA  1 
ATOM   5078 C  C   . ARG B 1 179 ? -5.097  32.169  1.946   1.00 36.32  ? 179 ARG B C   1 
ATOM   5079 O  O   . ARG B 1 179 ? -5.123  31.619  0.848   1.00 39.14  ? 179 ARG B O   1 
ATOM   5080 C  CB  . ARG B 1 179 ? -5.895  34.580  1.895   1.00 39.48  ? 179 ARG B CB  1 
ATOM   5081 C  CG  . ARG B 1 179 ? -5.926  34.772  0.384   1.00 41.31  ? 179 ARG B CG  1 
ATOM   5082 C  CD  . ARG B 1 179 ? -6.270  36.198  0.005   1.00 42.99  ? 179 ARG B CD  1 
ATOM   5083 N  NE  . ARG B 1 179 ? -5.344  37.158  0.600   1.00 48.55  ? 179 ARG B NE  1 
ATOM   5084 C  CZ  . ARG B 1 179 ? -5.703  38.264  1.248   1.00 50.37  ? 179 ARG B CZ  1 
ATOM   5085 N  NH1 . ARG B 1 179 ? -6.961  38.670  1.226   1.00 51.01  ? 179 ARG B NH1 1 
ATOM   5086 N  NH2 . ARG B 1 179 ? -4.794  38.986  1.883   1.00 51.12  ? 179 ARG B NH2 1 
ATOM   5087 N  N   . ALA B 1 180 ? -4.117  31.952  2.836   1.00 34.66  ? 180 ALA B N   1 
ATOM   5088 C  CA  . ALA B 1 180 ? -2.993  31.075  2.537   1.00 33.56  ? 180 ALA B CA  1 
ATOM   5089 C  C   . ALA B 1 180 ? -3.455  29.621  2.577   1.00 34.84  ? 180 ALA B C   1 
ATOM   5090 O  O   . ALA B 1 180 ? -3.108  28.838  1.689   1.00 34.04  ? 180 ALA B O   1 
ATOM   5091 C  CB  . ALA B 1 180 ? -1.858  31.319  3.489   1.00 33.39  ? 180 ALA B CB  1 
ATOM   5092 N  N   . LEU B 1 181 ? -4.256  29.281  3.599   1.00 36.45  ? 181 LEU B N   1 
ATOM   5093 C  CA  . LEU B 1 181 ? -4.877  27.970  3.705   1.00 37.72  ? 181 LEU B CA  1 
ATOM   5094 C  C   . LEU B 1 181 ? -5.822  27.747  2.524   1.00 39.96  ? 181 LEU B C   1 
ATOM   5095 O  O   . LEU B 1 181 ? -5.918  26.630  2.033   1.00 41.38  ? 181 LEU B O   1 
ATOM   5096 C  CB  . LEU B 1 181 ? -5.626  27.857  5.040   1.00 39.49  ? 181 LEU B CB  1 
ATOM   5097 C  CG  . LEU B 1 181 ? -4.836  27.261  6.205   1.00 40.39  ? 181 LEU B CG  1 
ATOM   5098 C  CD1 . LEU B 1 181 ? -3.509  27.957  6.378   1.00 45.09  ? 181 LEU B CD1 1 
ATOM   5099 C  CD2 . LEU B 1 181 ? -5.622  27.356  7.501   1.00 41.44  ? 181 LEU B CD2 1 
ATOM   5100 N  N   . ASP B 1 182 ? -6.514  28.803  2.072   1.00 41.42  ? 182 ASP B N   1 
ATOM   5101 C  CA  . ASP B 1 182 ? -7.449  28.682  0.959   1.00 45.85  ? 182 ASP B CA  1 
ATOM   5102 C  C   . ASP B 1 182 ? -6.678  28.400  -0.323  1.00 39.72  ? 182 ASP B C   1 
ATOM   5103 O  O   . ASP B 1 182 ? -7.050  27.531  -1.105  1.00 40.19  ? 182 ASP B O   1 
ATOM   5104 C  CB  . ASP B 1 182 ? -8.310  29.932  0.786   1.00 51.99  ? 182 ASP B CB  1 
ATOM   5105 C  CG  . ASP B 1 182 ? -9.513  29.689  -0.109  1.00 63.42  ? 182 ASP B CG  1 
ATOM   5106 O  OD1 . ASP B 1 182 ? -10.430 28.965  0.346   1.00 69.06  ? 182 ASP B OD1 1 
ATOM   5107 O  OD2 . ASP B 1 182 ? -9.516  30.204  -1.259  1.00 67.00  ? 182 ASP B OD2 1 
ATOM   5108 N  N   . GLU B 1 183 ? -5.582  29.137  -0.512  1.00 38.08  ? 183 GLU B N   1 
ATOM   5109 C  CA  . GLU B 1 183 ? -4.684  28.890  -1.626  1.00 37.56  ? 183 GLU B CA  1 
ATOM   5110 C  C   . GLU B 1 183 ? -4.216  27.430  -1.571  1.00 36.46  ? 183 GLU B C   1 
ATOM   5111 O  O   . GLU B 1 183 ? -4.144  26.762  -2.603  1.00 36.69  ? 183 GLU B O   1 
ATOM   5112 C  CB  . GLU B 1 183 ? -3.572  29.942  -1.596  1.00 38.79  ? 183 GLU B CB  1 
ATOM   5113 C  CG  . GLU B 1 183 ? -2.451  29.709  -2.580  1.00 42.16  ? 183 GLU B CG  1 
ATOM   5114 C  CD  . GLU B 1 183 ? -2.899  29.438  -4.006  1.00 43.26  ? 183 GLU B CD  1 
ATOM   5115 O  OE1 . GLU B 1 183 ? -2.120  28.817  -4.745  1.00 40.89  ? 183 GLU B OE1 1 
ATOM   5116 O  OE2 . GLU B 1 183 ? -4.023  29.836  -4.373  1.00 47.76  ? 183 GLU B OE2 1 
ATOM   5117 N  N   . ILE B 1 184 ? -3.962  26.909  -0.359  1.00 34.14  ? 184 ILE B N   1 
ATOM   5118 C  CA  . ILE B 1 184 ? -3.445  25.558  -0.198  1.00 31.82  ? 184 ILE B CA  1 
ATOM   5119 C  C   . ILE B 1 184 ? -4.522  24.547  -0.581  1.00 31.40  ? 184 ILE B C   1 
ATOM   5120 O  O   . ILE B 1 184 ? -4.259  23.646  -1.381  1.00 32.30  ? 184 ILE B O   1 
ATOM   5121 C  CB  . ILE B 1 184 ? -2.864  25.342  1.213   1.00 31.82  ? 184 ILE B CB  1 
ATOM   5122 C  CG1 . ILE B 1 184 ? -1.554  26.121  1.354   1.00 34.54  ? 184 ILE B CG1 1 
ATOM   5123 C  CG2 . ILE B 1 184 ? -2.662  23.859  1.496   1.00 32.18  ? 184 ILE B CG2 1 
ATOM   5124 C  CD1 . ILE B 1 184 ? -1.012  26.192  2.764   1.00 35.40  ? 184 ILE B CD1 1 
ATOM   5125 N  N   . MET B 1 185 ? -5.738  24.739  -0.071  1.00 34.58  ? 185 MET B N   1 
ATOM   5126 C  CA  . MET B 1 185 ? -6.856  23.866  -0.410  1.00 43.42  ? 185 MET B CA  1 
ATOM   5127 C  C   . MET B 1 185 ? -7.015  23.755  -1.929  1.00 41.20  ? 185 MET B C   1 
ATOM   5128 O  O   . MET B 1 185 ? -7.169  22.664  -2.460  1.00 41.66  ? 185 MET B O   1 
ATOM   5129 C  CB  . MET B 1 185 ? -8.158  24.410  0.179   1.00 51.49  ? 185 MET B CB  1 
ATOM   5130 C  CG  . MET B 1 185 ? -8.486  23.879  1.554   1.00 53.90  ? 185 MET B CG  1 
ATOM   5131 S  SD  . MET B 1 185 ? -9.615  25.017  2.377   1.00 63.53  ? 185 MET B SD  1 
ATOM   5132 C  CE  . MET B 1 185 ? -10.994 25.084  1.229   1.00 60.89  ? 185 MET B CE  1 
ATOM   5133 N  N   . ASN B 1 186 ? -6.974  24.897  -2.624  1.00 42.60  ? 186 ASN B N   1 
ATOM   5134 C  CA  . ASN B 1 186 ? -7.130  24.933  -4.069  1.00 43.16  ? 186 ASN B CA  1 
ATOM   5135 C  C   . ASN B 1 186 ? -5.937  24.260  -4.752  1.00 41.62  ? 186 ASN B C   1 
ATOM   5136 O  O   . ASN B 1 186 ? -6.112  23.630  -5.789  1.00 47.39  ? 186 ASN B O   1 
ATOM   5137 C  CB  . ASN B 1 186 ? -7.368  26.360  -4.590  1.00 45.64  ? 186 ASN B CB  1 
ATOM   5138 C  CG  . ASN B 1 186 ? -8.731  26.908  -4.216  1.00 51.16  ? 186 ASN B CG  1 
ATOM   5139 O  OD1 . ASN B 1 186 ? -9.758  26.271  -4.445  1.00 58.06  ? 186 ASN B OD1 1 
ATOM   5140 N  ND2 . ASN B 1 186 ? -8.756  28.085  -3.617  1.00 53.93  ? 186 ASN B ND2 1 
ATOM   5141 N  N   . LYS B 1 187 ? -4.728  24.362  -4.178  1.00 36.98  ? 187 LYS B N   1 
ATOM   5142 C  CA  . LYS B 1 187 ? -3.558  23.697  -4.742  1.00 35.72  ? 187 LYS B CA  1 
ATOM   5143 C  C   . LYS B 1 187 ? -3.713  22.171  -4.759  1.00 31.93  ? 187 LYS B C   1 
ATOM   5144 O  O   . LYS B 1 187 ? -3.232  21.538  -5.681  1.00 36.88  ? 187 LYS B O   1 
ATOM   5145 C  CB  . LYS B 1 187 ? -2.280  24.048  -3.973  1.00 40.64  ? 187 LYS B CB  1 
ATOM   5146 C  CG  . LYS B 1 187 ? -1.731  25.448  -4.225  1.00 44.28  ? 187 LYS B CG  1 
ATOM   5147 C  CD  . LYS B 1 187 ? -0.814  25.985  -3.123  1.00 46.42  ? 187 LYS B CD  1 
ATOM   5148 C  CE  . LYS B 1 187 ? 0.419   25.143  -2.876  1.00 49.10  ? 187 LYS B CE  1 
ATOM   5149 N  NZ  . LYS B 1 187 ? 1.333   25.172  -4.039  1.00 52.81  ? 187 LYS B NZ  1 
ATOM   5150 N  N   . LEU B 1 188 ? -4.411  21.586  -3.783  1.00 29.34  ? 188 LEU B N   1 
ATOM   5151 C  CA  . LEU B 1 188 ? -4.513  20.137  -3.639  1.00 35.87  ? 188 LEU B CA  1 
ATOM   5152 C  C   . LEU B 1 188 ? -5.145  19.490  -4.870  1.00 40.92  ? 188 LEU B C   1 
ATOM   5153 O  O   . LEU B 1 188 ? -4.934  18.314  -5.150  1.00 44.07  ? 188 LEU B O   1 
ATOM   5154 C  CB  . LEU B 1 188 ? -5.359  19.823  -2.398  1.00 36.86  ? 188 LEU B CB  1 
ATOM   5155 C  CG  . LEU B 1 188 ? -4.678  20.016  -1.038  1.00 36.77  ? 188 LEU B CG  1 
ATOM   5156 C  CD1 . LEU B 1 188 ? -5.606  19.605  0.104   1.00 35.66  ? 188 LEU B CD1 1 
ATOM   5157 C  CD2 . LEU B 1 188 ? -3.371  19.225  -0.960  1.00 35.69  ? 188 LEU B CD2 1 
ATOM   5158 N  N   . GLN B 1 189 ? -5.959  20.255  -5.591  1.00 45.61  ? 189 GLN B N   1 
ATOM   5159 C  CA  . GLN B 1 189 ? -6.735  19.703  -6.685  1.00 50.14  ? 189 GLN B CA  1 
ATOM   5160 C  C   . GLN B 1 189 ? -6.359  20.374  -8.014  1.00 55.73  ? 189 GLN B C   1 
ATOM   5161 O  O   . GLN B 1 189 ? -7.251  20.667  -8.809  1.00 58.17  ? 189 GLN B O   1 
ATOM   5162 C  CB  . GLN B 1 189 ? -8.204  19.873  -6.296  1.00 47.27  ? 189 GLN B CB  1 
ATOM   5163 C  CG  . GLN B 1 189 ? -9.147  18.979  -7.083  1.00 54.25  ? 189 GLN B CG  1 
ATOM   5164 C  CD  . GLN B 1 189 ? -9.189  17.542  -6.627  1.00 52.51  ? 189 GLN B CD  1 
ATOM   5165 O  OE1 . GLN B 1 189 ? -8.849  17.191  -5.496  1.00 42.35  ? 189 GLN B OE1 1 
ATOM   5166 N  NE2 . GLN B 1 189 ? -9.659  16.689  -7.521  1.00 55.09  ? 189 GLN B NE2 1 
ATOM   5167 N  N   . ARG B 1 190 ? -5.048  20.601  -8.258  1.00 54.01  ? 190 ARG B N   1 
ATOM   5168 C  CA  . ARG B 1 190 ? -4.554  21.206  -9.495  1.00 56.14  ? 190 ARG B CA  1 
ATOM   5169 C  C   . ARG B 1 190 ? -3.548  20.294  -10.196 1.00 58.37  ? 190 ARG B C   1 
ATOM   5170 O  O   . ARG B 1 190 ? -2.559  19.887  -9.589  1.00 54.09  ? 190 ARG B O   1 
ATOM   5171 C  CB  . ARG B 1 190 ? -3.829  22.533  -9.246  1.00 55.03  ? 190 ARG B CB  1 
ATOM   5172 C  CG  . ARG B 1 190 ? -4.731  23.732  -8.982  1.00 50.49  ? 190 ARG B CG  1 
ATOM   5173 C  CD  . ARG B 1 190 ? -3.840  24.912  -8.671  1.00 51.06  ? 190 ARG B CD  1 
ATOM   5174 N  NE  . ARG B 1 190 ? -4.486  25.961  -7.902  1.00 48.66  ? 190 ARG B NE  1 
ATOM   5175 C  CZ  . ARG B 1 190 ? -3.811  26.916  -7.284  1.00 49.15  ? 190 ARG B CZ  1 
ATOM   5176 N  NH1 . ARG B 1 190 ? -2.490  26.915  -7.344  1.00 48.28  ? 190 ARG B NH1 1 
ATOM   5177 N  NH2 . ARG B 1 190 ? -4.444  27.863  -6.609  1.00 52.74  ? 190 ARG B NH2 1 
ATOM   5178 N  N   . ALA B 1 191 ? -3.774  20.058  -11.501 1.00 59.99  ? 191 ALA B N   1 
ATOM   5179 C  CA  . ALA B 1 191 ? -2.985  19.126  -12.297 1.00 58.06  ? 191 ALA B CA  1 
ATOM   5180 C  C   . ALA B 1 191 ? -1.637  19.722  -12.704 1.00 65.63  ? 191 ALA B C   1 
ATOM   5181 O  O   . ALA B 1 191 ? -0.663  18.980  -12.858 1.00 68.26  ? 191 ALA B O   1 
ATOM   5182 C  CB  . ALA B 1 191 ? -3.762  18.709  -13.516 1.00 57.39  ? 191 ALA B CB  1 
ATOM   5183 N  N   . ASN B 1 192 ? -1.580  21.046  -12.907 1.00 63.12  ? 192 ASN B N   1 
ATOM   5184 C  CA  . ASN B 1 192 ? -0.343  21.690  -13.325 1.00 68.19  ? 192 ASN B CA  1 
ATOM   5185 C  C   . ASN B 1 192 ? 0.008   22.803  -12.338 1.00 63.06  ? 192 ASN B C   1 
ATOM   5186 O  O   . ASN B 1 192 ? -0.347  23.958  -12.560 1.00 54.47  ? 192 ASN B O   1 
ATOM   5187 C  CB  . ASN B 1 192 ? -0.426  22.248  -14.752 1.00 74.14  ? 192 ASN B CB  1 
ATOM   5188 C  CG  . ASN B 1 192 ? -1.256  21.409  -15.705 1.00 74.12  ? 192 ASN B CG  1 
ATOM   5189 O  OD1 . ASN B 1 192 ? -0.874  20.292  -16.056 1.00 70.38  ? 192 ASN B OD1 1 
ATOM   5190 N  ND2 . ASN B 1 192 ? -2.376  21.957  -16.156 1.00 75.81  ? 192 ASN B ND2 1 
ATOM   5191 N  N   . PRO B 1 193 ? 0.739   22.506  -11.236 1.00 66.66  ? 193 PRO B N   1 
ATOM   5192 C  CA  . PRO B 1 193 ? 1.113   23.536  -10.259 1.00 64.01  ? 193 PRO B CA  1 
ATOM   5193 C  C   . PRO B 1 193 ? 1.933   24.676  -10.867 1.00 66.92  ? 193 PRO B C   1 
ATOM   5194 O  O   . PRO B 1 193 ? 1.785   25.830  -10.460 1.00 59.78  ? 193 PRO B O   1 
ATOM   5195 C  CB  . PRO B 1 193 ? 1.961   22.786  -9.210  1.00 59.20  ? 193 PRO B CB  1 
ATOM   5196 C  CG  . PRO B 1 193 ? 1.634   21.314  -9.413  1.00 60.81  ? 193 PRO B CG  1 
ATOM   5197 C  CD  . PRO B 1 193 ? 1.251   21.171  -10.873 1.00 63.88  ? 193 PRO B CD  1 
ATOM   5198 N  N   . ASP B 1 194 ? 2.775   24.324  -11.854 1.00 67.95  ? 194 ASP B N   1 
ATOM   5199 C  CA  . ASP B 1 194 ? 3.769   25.216  -12.433 1.00 66.64  ? 194 ASP B CA  1 
ATOM   5200 C  C   . ASP B 1 194 ? 3.187   26.055  -13.571 1.00 58.45  ? 194 ASP B C   1 
ATOM   5201 O  O   . ASP B 1 194 ? 3.872   26.940  -14.078 1.00 60.17  ? 194 ASP B O   1 
ATOM   5202 C  CB  . ASP B 1 194 ? 4.961   24.425  -12.984 1.00 68.42  ? 194 ASP B CB  1 
ATOM   5203 C  CG  . ASP B 1 194 ? 5.673   23.544  -11.971 1.00 77.08  ? 194 ASP B CG  1 
ATOM   5204 O  OD1 . ASP B 1 194 ? 5.268   23.560  -10.785 1.00 81.96  ? 194 ASP B OD1 1 
ATOM   5205 O  OD2 . ASP B 1 194 ? 6.628   22.838  -12.382 1.00 74.65  ? 194 ASP B OD2 1 
ATOM   5206 N  N   . ASP B 1 195 ? 1.955   25.748  -13.996 1.00 52.39  ? 195 ASP B N   1 
ATOM   5207 C  CA  . ASP B 1 195 ? 1.285   26.459  -15.076 1.00 54.48  ? 195 ASP B CA  1 
ATOM   5208 C  C   . ASP B 1 195 ? 1.343   27.968  -14.806 1.00 51.02  ? 195 ASP B C   1 
ATOM   5209 O  O   . ASP B 1 195 ? 0.976   28.426  -13.724 1.00 45.66  ? 195 ASP B O   1 
ATOM   5210 C  CB  . ASP B 1 195 ? -0.143  25.918  -15.242 1.00 58.07  ? 195 ASP B CB  1 
ATOM   5211 C  CG  . ASP B 1 195 ? -1.022  26.604  -16.282 1.00 65.07  ? 195 ASP B CG  1 
ATOM   5212 O  OD1 . ASP B 1 195 ? -0.587  27.630  -16.842 1.00 63.70  ? 195 ASP B OD1 1 
ATOM   5213 O  OD2 . ASP B 1 195 ? -2.159  26.106  -16.521 1.00 63.65  ? 195 ASP B OD2 1 
ATOM   5214 N  N   . PRO B 1 196 ? 1.827   28.801  -15.761 1.00 46.88  ? 196 PRO B N   1 
ATOM   5215 C  CA  . PRO B 1 196 ? 1.869   30.253  -15.555 1.00 48.64  ? 196 PRO B CA  1 
ATOM   5216 C  C   . PRO B 1 196 ? 0.548   30.900  -15.131 1.00 45.30  ? 196 PRO B C   1 
ATOM   5217 O  O   . PRO B 1 196 ? 0.569   31.968  -14.528 1.00 52.15  ? 196 PRO B O   1 
ATOM   5218 C  CB  . PRO B 1 196 ? 2.350   30.849  -16.896 1.00 47.94  ? 196 PRO B CB  1 
ATOM   5219 C  CG  . PRO B 1 196 ? 2.554   29.664  -17.845 1.00 47.87  ? 196 PRO B CG  1 
ATOM   5220 C  CD  . PRO B 1 196 ? 2.467   28.395  -17.022 1.00 44.94  ? 196 PRO B CD  1 
ATOM   5221 N  N   . ALA B 1 197 ? -0.592  30.267  -15.438 1.00 44.32  ? 197 ALA B N   1 
ATOM   5222 C  CA  . ALA B 1 197 ? -1.897  30.773  -15.034 1.00 44.71  ? 197 ALA B CA  1 
ATOM   5223 C  C   . ALA B 1 197 ? -1.932  31.056  -13.528 1.00 46.13  ? 197 ALA B C   1 
ATOM   5224 O  O   . ALA B 1 197 ? -2.583  32.006  -13.104 1.00 53.56  ? 197 ALA B O   1 
ATOM   5225 C  CB  . ALA B 1 197 ? -2.988  29.796  -15.425 1.00 42.02  ? 197 ALA B CB  1 
ATOM   5226 N  N   . TYR B 1 198 ? -1.227  30.236  -12.732 1.00 49.84  ? 198 TYR B N   1 
ATOM   5227 C  CA  . TYR B 1 198 ? -1.293  30.301  -11.277 1.00 50.05  ? 198 TYR B CA  1 
ATOM   5228 C  C   . TYR B 1 198 ? -0.192  31.198  -10.705 1.00 53.80  ? 198 TYR B C   1 
ATOM   5229 O  O   . TYR B 1 198 ? 0.142   31.081  -9.527  1.00 56.07  ? 198 TYR B O   1 
ATOM   5230 C  CB  . TYR B 1 198 ? -1.167  28.890  -10.692 1.00 50.76  ? 198 TYR B CB  1 
ATOM   5231 C  CG  . TYR B 1 198 ? -2.179  27.860  -11.179 1.00 48.08  ? 198 TYR B CG  1 
ATOM   5232 C  CD1 . TYR B 1 198 ? -3.535  27.987  -10.892 1.00 44.17  ? 198 TYR B CD1 1 
ATOM   5233 C  CD2 . TYR B 1 198 ? -1.768  26.740  -11.894 1.00 44.85  ? 198 TYR B CD2 1 
ATOM   5234 C  CE1 . TYR B 1 198 ? -4.453  27.042  -11.324 1.00 46.85  ? 198 TYR B CE1 1 
ATOM   5235 C  CE2 . TYR B 1 198 ? -2.677  25.793  -12.333 1.00 44.68  ? 198 TYR B CE2 1 
ATOM   5236 C  CZ  . TYR B 1 198 ? -4.020  25.943  -12.048 1.00 47.05  ? 198 TYR B CZ  1 
ATOM   5237 O  OH  . TYR B 1 198 ? -4.888  24.986  -12.478 1.00 52.64  ? 198 TYR B OH  1 
ATOM   5238 N  N   . ASP B 1 199 ? 0.347   32.120  -11.516 1.00 54.18  ? 199 ASP B N   1 
ATOM   5239 C  CA  . ASP B 1 199 ? 1.391   33.030  -11.061 1.00 57.10  ? 199 ASP B CA  1 
ATOM   5240 C  C   . ASP B 1 199 ? 0.826   34.097  -10.123 1.00 58.46  ? 199 ASP B C   1 
ATOM   5241 O  O   . ASP B 1 199 ? 1.538   34.553  -9.229  1.00 56.51  ? 199 ASP B O   1 
ATOM   5242 C  CB  . ASP B 1 199 ? 2.132   33.676  -12.236 1.00 57.12  ? 199 ASP B CB  1 
ATOM   5243 C  CG  . ASP B 1 199 ? 3.159   32.754  -12.875 1.00 60.45  ? 199 ASP B CG  1 
ATOM   5244 O  OD1 . ASP B 1 199 ? 3.200   31.563  -12.479 1.00 65.40  ? 199 ASP B OD1 1 
ATOM   5245 O  OD2 . ASP B 1 199 ? 3.920   33.228  -13.751 1.00 56.21  ? 199 ASP B OD2 1 
ATOM   5246 N  N   . GLU B 1 200 ? -0.435  34.498  -10.332 1.00 57.46  ? 200 GLU B N   1 
ATOM   5247 C  CA  . GLU B 1 200 ? -1.059  35.533  -9.522  1.00 61.84  ? 200 GLU B CA  1 
ATOM   5248 C  C   . GLU B 1 200 ? -1.349  34.996  -8.120  1.00 65.26  ? 200 GLU B C   1 
ATOM   5249 O  O   . GLU B 1 200 ? -1.245  35.733  -7.136  1.00 68.77  ? 200 GLU B O   1 
ATOM   5250 C  CB  . GLU B 1 200 ? -2.351  36.032  -10.172 1.00 64.34  ? 200 GLU B CB  1 
ATOM   5251 C  CG  . GLU B 1 200 ? -2.976  37.210  -9.441  1.00 70.54  ? 200 GLU B CG  1 
ATOM   5252 C  CD  . GLU B 1 200 ? -4.237  37.777  -10.069 1.00 79.76  ? 200 GLU B CD  1 
ATOM   5253 O  OE1 . GLU B 1 200 ? -4.752  37.173  -11.031 1.00 85.53  ? 200 GLU B OE1 1 
ATOM   5254 O  OE2 . GLU B 1 200 ? -4.697  38.834  -9.597  1.00 89.92  ? 200 GLU B OE2 1 
ATOM   5255 N  N   . ASN B 1 201 ? -1.741  33.717  -8.046  1.00 58.25  ? 201 ASN B N   1 
ATOM   5256 C  CA  . ASN B 1 201 ? -2.022  33.061  -6.779  1.00 52.44  ? 201 ASN B CA  1 
ATOM   5257 C  C   . ASN B 1 201 ? -0.773  33.040  -5.909  1.00 51.55  ? 201 ASN B C   1 
ATOM   5258 O  O   . ASN B 1 201 ? -0.835  33.438  -4.749  1.00 45.03  ? 201 ASN B O   1 
ATOM   5259 C  CB  . ASN B 1 201 ? -2.473  31.610  -6.950  1.00 53.29  ? 201 ASN B CB  1 
ATOM   5260 C  CG  . ASN B 1 201 ? -3.754  31.480  -7.738  1.00 55.29  ? 201 ASN B CG  1 
ATOM   5261 O  OD1 . ASN B 1 201 ? -4.801  31.941  -7.297  1.00 48.80  ? 201 ASN B OD1 1 
ATOM   5262 N  ND2 . ASN B 1 201 ? -3.669  30.858  -8.903  1.00 58.57  ? 201 ASN B ND2 1 
ATOM   5263 N  N   . LYS B 1 202 ? 0.349   32.560  -6.472  1.00 47.36  ? 202 LYS B N   1 
ATOM   5264 C  CA  . LYS B 1 202 ? 1.568   32.403  -5.691  1.00 50.87  ? 202 LYS B CA  1 
ATOM   5265 C  C   . LYS B 1 202 ? 2.196   33.761  -5.387  1.00 52.83  ? 202 LYS B C   1 
ATOM   5266 O  O   . LYS B 1 202 ? 2.971   33.855  -4.438  1.00 53.97  ? 202 LYS B O   1 
ATOM   5267 C  CB  . LYS B 1 202 ? 2.576   31.434  -6.320  1.00 52.64  ? 202 LYS B CB  1 
ATOM   5268 C  CG  . LYS B 1 202 ? 2.879   31.590  -7.801  1.00 61.20  ? 202 LYS B CG  1 
ATOM   5269 C  CD  . LYS B 1 202 ? 3.583   30.374  -8.385  1.00 62.84  ? 202 LYS B CD  1 
ATOM   5270 C  CE  . LYS B 1 202 ? 2.959   29.057  -7.955  1.00 61.61  ? 202 LYS B CE  1 
ATOM   5271 N  NZ  . LYS B 1 202 ? 3.271   27.956  -8.899  1.00 61.42  ? 202 LYS B NZ  1 
ATOM   5272 N  N   . ARG B 1 203 ? 1.847   34.804  -6.155  1.00 52.74  ? 203 ARG B N   1 
ATOM   5273 C  CA  . ARG B 1 203 ? 2.184   36.168  -5.765  1.00 55.58  ? 203 ARG B CA  1 
ATOM   5274 C  C   . ARG B 1 203 ? 1.376   36.543  -4.522  1.00 47.76  ? 203 ARG B C   1 
ATOM   5275 O  O   . ARG B 1 203 ? 1.908   37.152  -3.593  1.00 42.58  ? 203 ARG B O   1 
ATOM   5276 C  CB  . ARG B 1 203 ? 1.954   37.169  -6.908  1.00 59.53  ? 203 ARG B CB  1 
ATOM   5277 C  CG  . ARG B 1 203 ? 3.116   37.280  -7.893  1.00 64.02  ? 203 ARG B CG  1 
ATOM   5278 C  CD  . ARG B 1 203 ? 3.128   38.552  -8.744  1.00 65.08  ? 203 ARG B CD  1 
ATOM   5279 N  NE  . ARG B 1 203 ? 2.483   38.423  -10.055 1.00 67.66  ? 203 ARG B NE  1 
ATOM   5280 C  CZ  . ARG B 1 203 ? 1.177   38.550  -10.315 1.00 65.34  ? 203 ARG B CZ  1 
ATOM   5281 N  NH1 . ARG B 1 203 ? 0.717   38.212  -11.508 1.00 62.29  ? 203 ARG B NH1 1 
ATOM   5282 N  NH2 . ARG B 1 203 ? 0.324   38.968  -9.393  1.00 64.15  ? 203 ARG B NH2 1 
ATOM   5283 N  N   . GLN B 1 204 ? 0.093   36.160  -4.500  1.00 47.87  ? 204 GLN B N   1 
ATOM   5284 C  CA  . GLN B 1 204 ? -0.755  36.430  -3.346  1.00 48.18  ? 204 GLN B CA  1 
ATOM   5285 C  C   . GLN B 1 204 ? -0.290  35.559  -2.166  1.00 43.12  ? 204 GLN B C   1 
ATOM   5286 O  O   . GLN B 1 204 ? -0.241  36.041  -1.040  1.00 40.85  ? 204 GLN B O   1 
ATOM   5287 C  CB  . GLN B 1 204 ? -2.237  36.318  -3.734  1.00 47.59  ? 204 GLN B CB  1 
ATOM   5288 C  CG  . GLN B 1 204 ? -3.206  36.439  -2.560  1.00 53.95  ? 204 GLN B CG  1 
ATOM   5289 C  CD  . GLN B 1 204 ? -4.315  37.451  -2.761  1.00 60.42  ? 204 GLN B CD  1 
ATOM   5290 O  OE1 . GLN B 1 204 ? -5.427  37.120  -3.172  1.00 63.59  ? 204 GLN B OE1 1 
ATOM   5291 N  NE2 . GLN B 1 204 ? -4.018  38.708  -2.459  1.00 56.54  ? 204 GLN B NE2 1 
ATOM   5292 N  N   . PHE B 1 205 ? 0.093   34.297  -2.415  1.00 40.81  ? 205 PHE B N   1 
ATOM   5293 C  CA  . PHE B 1 205 ? 0.589   33.421  -1.359  1.00 37.62  ? 205 PHE B CA  1 
ATOM   5294 C  C   . PHE B 1 205 ? 1.822   34.047  -0.705  1.00 35.15  ? 205 PHE B C   1 
ATOM   5295 O  O   . PHE B 1 205 ? 1.930   34.083  0.519   1.00 35.10  ? 205 PHE B O   1 
ATOM   5296 C  CB  . PHE B 1 205 ? 0.915   32.018  -1.900  1.00 40.15  ? 205 PHE B CB  1 
ATOM   5297 C  CG  . PHE B 1 205 ? 1.032   30.933  -0.850  1.00 37.94  ? 205 PHE B CG  1 
ATOM   5298 C  CD1 . PHE B 1 205 ? -0.068  30.555  -0.095  1.00 37.65  ? 205 PHE B CD1 1 
ATOM   5299 C  CD2 . PHE B 1 205 ? 2.249   30.314  -0.587  1.00 38.43  ? 205 PHE B CD2 1 
ATOM   5300 C  CE1 . PHE B 1 205 ? 0.038   29.563  0.869   1.00 40.91  ? 205 PHE B CE1 1 
ATOM   5301 C  CE2 . PHE B 1 205 ? 2.354   29.327  0.382   1.00 37.73  ? 205 PHE B CE2 1 
ATOM   5302 C  CZ  . PHE B 1 205 ? 1.247   28.945  1.098   1.00 40.33  ? 205 PHE B CZ  1 
ATOM   5303 N  N   . GLN B 1 206 ? 2.763   34.542  -1.516  1.00 32.60  ? 206 GLN B N   1 
ATOM   5304 C  CA  . GLN B 1 206 ? 3.955   35.161  -0.958  1.00 37.43  ? 206 GLN B CA  1 
ATOM   5305 C  C   . GLN B 1 206 ? 3.596   36.424  -0.165  1.00 38.15  ? 206 GLN B C   1 
ATOM   5306 O  O   . GLN B 1 206 ? 4.298   36.745  0.788   1.00 35.06  ? 206 GLN B O   1 
ATOM   5307 C  CB  . GLN B 1 206 ? 5.007   35.434  -2.034  1.00 38.29  ? 206 GLN B CB  1 
ATOM   5308 C  CG  . GLN B 1 206 ? 5.612   34.180  -2.668  1.00 41.32  ? 206 GLN B CG  1 
ATOM   5309 C  CD  . GLN B 1 206 ? 6.030   33.101  -1.688  1.00 47.16  ? 206 GLN B CD  1 
ATOM   5310 O  OE1 . GLN B 1 206 ? 6.698   33.349  -0.685  1.00 45.33  ? 206 GLN B OE1 1 
ATOM   5311 N  NE2 . GLN B 1 206 ? 5.626   31.870  -1.963  1.00 51.20  ? 206 GLN B NE2 1 
ATOM   5312 N  N   . ASP B 1 207 ? 2.515   37.138  -0.529  1.00 38.51  ? 207 ASP B N   1 
ATOM   5313 C  CA  . ASP B 1 207 ? 2.126   38.347  0.197   1.00 41.09  ? 207 ASP B CA  1 
ATOM   5314 C  C   . ASP B 1 207 ? 1.545   37.981  1.565   1.00 42.21  ? 207 ASP B C   1 
ATOM   5315 O  O   . ASP B 1 207 ? 1.777   38.679  2.559   1.00 41.41  ? 207 ASP B O   1 
ATOM   5316 C  CB  . ASP B 1 207 ? 1.108   39.202  -0.565  1.00 40.64  ? 207 ASP B CB  1 
ATOM   5317 C  CG  . ASP B 1 207 ? 1.637   39.802  -1.860  1.00 44.59  ? 207 ASP B CG  1 
ATOM   5318 O  OD1 . ASP B 1 207 ? 2.814   40.216  -1.884  1.00 47.43  ? 207 ASP B OD1 1 
ATOM   5319 O  OD2 . ASP B 1 207 ? 0.871   39.844  -2.846  1.00 44.89  ? 207 ASP B OD2 1 
ATOM   5320 N  N   . ASP B 1 208 ? 0.767   36.889  1.602   1.00 40.80  ? 208 ASP B N   1 
ATOM   5321 C  CA  . ASP B 1 208 ? 0.144   36.425  2.833   1.00 41.22  ? 208 ASP B CA  1 
ATOM   5322 C  C   . ASP B 1 208 ? 1.224   35.980  3.822   1.00 32.74  ? 208 ASP B C   1 
ATOM   5323 O  O   . ASP B 1 208 ? 1.104   36.251  5.014   1.00 34.59  ? 208 ASP B O   1 
ATOM   5324 C  CB  . ASP B 1 208 ? -0.924  35.352  2.556   1.00 42.72  ? 208 ASP B CB  1 
ATOM   5325 C  CG  . ASP B 1 208 ? -2.124  35.858  1.758   1.00 45.84  ? 208 ASP B CG  1 
ATOM   5326 O  OD1 . ASP B 1 208 ? -2.510  37.036  1.948   1.00 44.36  ? 208 ASP B OD1 1 
ATOM   5327 O  OD2 . ASP B 1 208 ? -2.685  35.069  0.959   1.00 46.34  ? 208 ASP B OD2 1 
ATOM   5328 N  N   . ILE B 1 209 ? 2.297   35.346  3.329   1.00 29.67  ? 209 ILE B N   1 
ATOM   5329 C  CA  . ILE B 1 209 ? 3.392   34.910  4.194   1.00 30.27  ? 209 ILE B CA  1 
ATOM   5330 C  C   . ILE B 1 209 ? 4.141   36.114  4.759   1.00 30.93  ? 209 ILE B C   1 
ATOM   5331 O  O   . ILE B 1 209 ? 4.487   36.140  5.943   1.00 28.99  ? 209 ILE B O   1 
ATOM   5332 C  CB  . ILE B 1 209 ? 4.317   33.919  3.465   1.00 34.85  ? 209 ILE B CB  1 
ATOM   5333 C  CG1 . ILE B 1 209 ? 3.570   32.620  3.148   1.00 35.63  ? 209 ILE B CG1 1 
ATOM   5334 C  CG2 . ILE B 1 209 ? 5.592   33.653  4.266   1.00 35.61  ? 209 ILE B CG2 1 
ATOM   5335 C  CD1 . ILE B 1 209 ? 4.243   31.787  2.064   1.00 37.78  ? 209 ILE B CD1 1 
ATOM   5336 N  N   . LYS B 1 210 ? 4.321   37.132  3.918   1.00 30.85  ? 210 LYS B N   1 
ATOM   5337 C  CA  . LYS B 1 210 ? 4.907   38.395  4.311   1.00 34.14  ? 210 LYS B CA  1 
ATOM   5338 C  C   . LYS B 1 210 ? 4.130   38.999  5.483   1.00 34.59  ? 210 LYS B C   1 
ATOM   5339 O  O   . LYS B 1 210 ? 4.756   39.506  6.412   1.00 32.28  ? 210 LYS B O   1 
ATOM   5340 C  CB  . LYS B 1 210 ? 4.923   39.329  3.098   1.00 41.02  ? 210 LYS B CB  1 
ATOM   5341 C  CG  . LYS B 1 210 ? 6.190   40.144  2.926   1.00 46.21  ? 210 LYS B CG  1 
ATOM   5342 C  CD  . LYS B 1 210 ? 6.396   41.166  4.002   1.00 50.33  ? 210 LYS B CD  1 
ATOM   5343 C  CE  . LYS B 1 210 ? 7.602   42.040  3.728   1.00 54.90  ? 210 LYS B CE  1 
ATOM   5344 N  NZ  . LYS B 1 210 ? 7.572   43.265  4.561   1.00 58.62  ? 210 LYS B NZ  1 
ATOM   5345 N  N   . VAL B 1 211 ? 2.780   38.957  5.431   1.00 33.13  ? 211 VAL B N   1 
ATOM   5346 C  CA  . VAL B 1 211 ? 1.945   39.535  6.478   1.00 35.46  ? 211 VAL B CA  1 
ATOM   5347 C  C   . VAL B 1 211 ? 2.176   38.801  7.803   1.00 34.97  ? 211 VAL B C   1 
ATOM   5348 O  O   . VAL B 1 211 ? 2.392   39.409  8.853   1.00 29.37  ? 211 VAL B O   1 
ATOM   5349 C  CB  . VAL B 1 211 ? 0.449   39.519  6.107   1.00 37.08  ? 211 VAL B CB  1 
ATOM   5350 C  CG1 . VAL B 1 211 ? -0.432  39.719  7.326   1.00 37.76  ? 211 VAL B CG1 1 
ATOM   5351 C  CG2 . VAL B 1 211 ? 0.124   40.561  5.042   1.00 42.30  ? 211 VAL B CG2 1 
ATOM   5352 N  N   . MET B 1 212 ? 2.108   37.474  7.752   1.00 34.02  ? 212 MET B N   1 
ATOM   5353 C  CA  . MET B 1 212 ? 2.280   36.671  8.946   1.00 35.99  ? 212 MET B CA  1 
ATOM   5354 C  C   . MET B 1 212 ? 3.641   36.965  9.584   1.00 35.03  ? 212 MET B C   1 
ATOM   5355 O  O   . MET B 1 212 ? 3.712   37.152  10.795  1.00 34.47  ? 212 MET B O   1 
ATOM   5356 C  CB  . MET B 1 212 ? 2.141   35.192  8.580   1.00 33.24  ? 212 MET B CB  1 
ATOM   5357 C  CG  . MET B 1 212 ? 0.726   34.847  8.134   1.00 36.96  ? 212 MET B CG  1 
ATOM   5358 S  SD  . MET B 1 212 ? 0.458   33.076  7.824   1.00 39.86  ? 212 MET B SD  1 
ATOM   5359 C  CE  . MET B 1 212 ? 2.031   32.636  7.109   1.00 38.06  ? 212 MET B CE  1 
ATOM   5360 N  N   . ASN B 1 213 ? 4.701   37.077  8.764   1.00 34.19  ? 213 ASN B N   1 
ATOM   5361 C  CA  . ASN B 1 213 ? 6.049   37.317  9.266   1.00 34.67  ? 213 ASN B CA  1 
ATOM   5362 C  C   . ASN B 1 213 ? 6.223   38.728  9.825   1.00 35.28  ? 213 ASN B C   1 
ATOM   5363 O  O   . ASN B 1 213 ? 7.079   38.973  10.676  1.00 32.61  ? 213 ASN B O   1 
ATOM   5364 C  CB  . ASN B 1 213 ? 7.105   37.020  8.201   1.00 33.98  ? 213 ASN B CB  1 
ATOM   5365 C  CG  . ASN B 1 213 ? 7.379   35.535  8.154   1.00 38.34  ? 213 ASN B CG  1 
ATOM   5366 O  OD1 . ASN B 1 213 ? 8.246   35.048  8.874   1.00 44.39  ? 213 ASN B OD1 1 
ATOM   5367 N  ND2 . ASN B 1 213 ? 6.568   34.791  7.424   1.00 39.76  ? 213 ASN B ND2 1 
ATOM   5368 N  N   . ASP B 1 214 ? 5.442   39.679  9.323   1.00 34.98  ? 214 ASP B N   1 
ATOM   5369 C  CA  . ASP B 1 214 ? 5.541   41.041  9.817   1.00 35.28  ? 214 ASP B CA  1 
ATOM   5370 C  C   . ASP B 1 214 ? 5.068   41.073  11.270  1.00 31.97  ? 214 ASP B C   1 
ATOM   5371 O  O   . ASP B 1 214 ? 5.667   41.719  12.135  1.00 25.93  ? 214 ASP B O   1 
ATOM   5372 C  CB  . ASP B 1 214 ? 4.774   41.997  8.901   1.00 38.47  ? 214 ASP B CB  1 
ATOM   5373 C  CG  . ASP B 1 214 ? 5.535   42.396  7.642   1.00 42.84  ? 214 ASP B CG  1 
ATOM   5374 O  OD1 . ASP B 1 214 ? 6.767   42.154  7.572   1.00 45.07  ? 214 ASP B OD1 1 
ATOM   5375 O  OD2 . ASP B 1 214 ? 4.896   42.968  6.735   1.00 50.77  ? 214 ASP B OD2 1 
ATOM   5376 N  N   . LEU B 1 215 ? 3.988   40.349  11.553  1.00 26.22  ? 215 LEU B N   1 
ATOM   5377 C  CA  . LEU B 1 215 ? 3.494   40.298  12.912  1.00 27.17  ? 215 LEU B CA  1 
ATOM   5378 C  C   . LEU B 1 215 ? 4.463   39.518  13.804  1.00 25.53  ? 215 LEU B C   1 
ATOM   5379 O  O   . LEU B 1 215 ? 4.665   39.852  14.969  1.00 21.59  ? 215 LEU B O   1 
ATOM   5380 C  CB  . LEU B 1 215 ? 2.101   39.659  12.927  1.00 28.44  ? 215 LEU B CB  1 
ATOM   5381 C  CG  . LEU B 1 215 ? 1.584   39.412  14.335  1.00 29.95  ? 215 LEU B CG  1 
ATOM   5382 C  CD1 . LEU B 1 215 ? 1.316   40.733  15.023  1.00 29.10  ? 215 LEU B CD1 1 
ATOM   5383 C  CD2 . LEU B 1 215 ? 0.346   38.528  14.328  1.00 31.87  ? 215 LEU B CD2 1 
ATOM   5384 N  N   . VAL B 1 216 ? 5.039   38.438  13.272  1.00 25.35  ? 216 VAL B N   1 
ATOM   5385 C  CA  . VAL B 1 216 ? 6.046   37.723  14.041  1.00 25.57  ? 216 VAL B CA  1 
ATOM   5386 C  C   . VAL B 1 216 ? 7.132   38.697  14.481  1.00 23.77  ? 216 VAL B C   1 
ATOM   5387 O  O   . VAL B 1 216 ? 7.457   38.766  15.662  1.00 25.96  ? 216 VAL B O   1 
ATOM   5388 C  CB  . VAL B 1 216 ? 6.657   36.574  13.230  1.00 24.67  ? 216 VAL B CB  1 
ATOM   5389 C  CG1 . VAL B 1 216 ? 7.963   36.094  13.850  1.00 24.90  ? 216 VAL B CG1 1 
ATOM   5390 C  CG2 . VAL B 1 216 ? 5.654   35.452  13.031  1.00 24.32  ? 216 VAL B CG2 1 
ATOM   5391 N  N   . ASP B 1 217 ? 7.681   39.463  13.536  1.00 29.68  ? 217 ASP B N   1 
ATOM   5392 C  CA  . ASP B 1 217 ? 8.803   40.347  13.837  1.00 33.11  ? 217 ASP B CA  1 
ATOM   5393 C  C   . ASP B 1 217 ? 8.439   41.275  14.996  1.00 32.99  ? 217 ASP B C   1 
ATOM   5394 O  O   . ASP B 1 217 ? 9.269   41.516  15.870  1.00 30.08  ? 217 ASP B O   1 
ATOM   5395 C  CB  . ASP B 1 217 ? 9.227   41.154  12.609  1.00 36.86  ? 217 ASP B CB  1 
ATOM   5396 C  CG  . ASP B 1 217 ? 9.839   40.296  11.518  1.00 43.34  ? 217 ASP B CG  1 
ATOM   5397 O  OD1 . ASP B 1 217 ? 10.520  39.318  11.880  1.00 47.83  ? 217 ASP B OD1 1 
ATOM   5398 O  OD2 . ASP B 1 217 ? 9.661   40.623  10.320  1.00 47.51  ? 217 ASP B OD2 1 
ATOM   5399 N  N   . LYS B 1 218 ? 7.199   41.786  14.980  1.00 28.66  ? 218 LYS B N   1 
ATOM   5400 C  CA  . LYS B 1 218 ? 6.704   42.708  15.985  1.00 30.04  ? 218 LYS B CA  1 
ATOM   5401 C  C   . LYS B 1 218 ? 6.654   42.025  17.357  1.00 23.70  ? 218 LYS B C   1 
ATOM   5402 O  O   . LYS B 1 218 ? 7.171   42.524  18.357  1.00 19.42  ? 218 LYS B O   1 
ATOM   5403 C  CB  . LYS B 1 218 ? 5.341   43.216  15.492  1.00 33.97  ? 218 LYS B CB  1 
ATOM   5404 C  CG  . LYS B 1 218 ? 4.614   44.223  16.374  1.00 39.75  ? 218 LYS B CG  1 
ATOM   5405 C  CD  . LYS B 1 218 ? 5.321   45.547  16.561  1.00 44.56  ? 218 LYS B CD  1 
ATOM   5406 C  CE  . LYS B 1 218 ? 4.433   46.631  17.140  1.00 42.59  ? 218 LYS B CE  1 
ATOM   5407 N  NZ  . LYS B 1 218 ? 3.612   46.156  18.283  1.00 42.15  ? 218 LYS B NZ  1 
ATOM   5408 N  N   . ILE B 1 219 ? 6.028   40.856  17.415  1.00 21.64  ? 219 ILE B N   1 
ATOM   5409 C  CA  . ILE B 1 219 ? 5.887   40.182  18.688  1.00 23.64  ? 219 ILE B CA  1 
ATOM   5410 C  C   . ILE B 1 219 ? 7.271   40.026  19.332  1.00 25.43  ? 219 ILE B C   1 
ATOM   5411 O  O   . ILE B 1 219 ? 7.421   40.258  20.534  1.00 23.55  ? 219 ILE B O   1 
ATOM   5412 C  CB  . ILE B 1 219 ? 5.150   38.839  18.512  1.00 22.96  ? 219 ILE B CB  1 
ATOM   5413 C  CG1 . ILE B 1 219 ? 3.689   39.071  18.117  1.00 24.12  ? 219 ILE B CG1 1 
ATOM   5414 C  CG2 . ILE B 1 219 ? 5.287   37.991  19.761  1.00 24.26  ? 219 ILE B CG2 1 
ATOM   5415 C  CD1 . ILE B 1 219 ? 2.906   37.800  17.766  1.00 25.82  ? 219 ILE B CD1 1 
ATOM   5416 N  N   . ILE B 1 220 ? 8.259   39.597  18.529  1.00 25.27  ? 220 ILE B N   1 
ATOM   5417 C  CA  . ILE B 1 220 ? 9.603   39.345  19.028  1.00 29.44  ? 220 ILE B CA  1 
ATOM   5418 C  C   . ILE B 1 220 ? 10.231  40.650  19.528  1.00 34.78  ? 220 ILE B C   1 
ATOM   5419 O  O   . ILE B 1 220 ? 10.712  40.690  20.660  1.00 32.64  ? 220 ILE B O   1 
ATOM   5420 C  CB  . ILE B 1 220 ? 10.462  38.649  17.951  1.00 31.24  ? 220 ILE B CB  1 
ATOM   5421 C  CG1 . ILE B 1 220 ? 10.014  37.192  17.765  1.00 28.55  ? 220 ILE B CG1 1 
ATOM   5422 C  CG2 . ILE B 1 220 ? 11.957  38.748  18.258  1.00 29.49  ? 220 ILE B CG2 1 
ATOM   5423 C  CD1 . ILE B 1 220 ? 10.534  36.546  16.473  1.00 30.33  ? 220 ILE B CD1 1 
ATOM   5424 N  N   . ALA B 1 221 ? 10.171  41.696  18.687  1.00 32.18  ? 221 ALA B N   1 
ATOM   5425 C  CA  . ALA B 1 221 ? 10.739  43.002  18.970  1.00 35.89  ? 221 ALA B CA  1 
ATOM   5426 C  C   . ALA B 1 221 ? 10.109  43.634  20.218  1.00 38.69  ? 221 ALA B C   1 
ATOM   5427 O  O   . ALA B 1 221 ? 10.825  44.277  20.985  1.00 38.51  ? 221 ALA B O   1 
ATOM   5428 C  CB  . ALA B 1 221 ? 10.560  43.878  17.749  1.00 35.09  ? 221 ALA B CB  1 
ATOM   5429 N  N   . ASP B 1 222 ? 8.787   43.472  20.418  1.00 31.60  ? 222 ASP B N   1 
ATOM   5430 C  CA  . ASP B 1 222 ? 8.129   43.960  21.624  1.00 35.97  ? 222 ASP B CA  1 
ATOM   5431 C  C   . ASP B 1 222 ? 8.690   43.258  22.859  1.00 34.44  ? 222 ASP B C   1 
ATOM   5432 O  O   . ASP B 1 222 ? 8.929   43.888  23.881  1.00 28.66  ? 222 ASP B O   1 
ATOM   5433 C  CB  . ASP B 1 222 ? 6.606   43.749  21.637  1.00 38.91  ? 222 ASP B CB  1 
ATOM   5434 C  CG  . ASP B 1 222 ? 5.808   44.675  20.726  1.00 49.55  ? 222 ASP B CG  1 
ATOM   5435 O  OD1 . ASP B 1 222 ? 6.445   45.516  20.047  1.00 57.53  ? 222 ASP B OD1 1 
ATOM   5436 O  OD2 . ASP B 1 222 ? 4.547   44.546  20.682  1.00 49.45  ? 222 ASP B OD2 1 
ATOM   5437 N  N   . ARG B 1 223 ? 8.850   41.929  22.798  1.00 36.13  ? 223 ARG B N   1 
ATOM   5438 C  CA  . ARG B 1 223 ? 9.321   41.207  23.967  1.00 37.94  ? 223 ARG B CA  1 
ATOM   5439 C  C   . ARG B 1 223 ? 10.751  41.641  24.275  1.00 34.29  ? 223 ARG B C   1 
ATOM   5440 O  O   . ARG B 1 223 ? 11.087  41.868  25.427  1.00 37.26  ? 223 ARG B O   1 
ATOM   5441 C  CB  . ARG B 1 223 ? 9.245   39.689  23.776  1.00 33.07  ? 223 ARG B CB  1 
ATOM   5442 C  CG  . ARG B 1 223 ? 9.797   38.874  24.936  1.00 30.95  ? 223 ARG B CG  1 
ATOM   5443 C  CD  . ARG B 1 223 ? 9.066   39.060  26.238  1.00 29.63  ? 223 ARG B CD  1 
ATOM   5444 N  NE  . ARG B 1 223 ? 7.618   38.994  26.086  1.00 30.12  ? 223 ARG B NE  1 
ATOM   5445 C  CZ  . ARG B 1 223 ? 6.861   37.944  26.372  1.00 28.44  ? 223 ARG B CZ  1 
ATOM   5446 N  NH1 . ARG B 1 223 ? 7.414   36.839  26.829  1.00 26.94  ? 223 ARG B NH1 1 
ATOM   5447 N  NH2 . ARG B 1 223 ? 5.559   37.984  26.128  1.00 28.67  ? 223 ARG B NH2 1 
ATOM   5448 N  N   . LYS B 1 224 ? 11.593  41.732  23.252  1.00 36.39  ? 224 LYS B N   1 
ATOM   5449 C  CA  . LYS B 1 224 ? 12.983  42.098  23.487  1.00 41.31  ? 224 LYS B CA  1 
ATOM   5450 C  C   . LYS B 1 224 ? 13.048  43.498  24.094  1.00 47.60  ? 224 LYS B C   1 
ATOM   5451 O  O   . LYS B 1 224 ? 13.916  43.758  24.917  1.00 49.20  ? 224 LYS B O   1 
ATOM   5452 C  CB  . LYS B 1 224 ? 13.809  41.931  22.208  1.00 41.11  ? 224 LYS B CB  1 
ATOM   5453 C  CG  . LYS B 1 224 ? 14.422  40.541  22.070  1.00 49.25  ? 224 LYS B CG  1 
ATOM   5454 C  CD  . LYS B 1 224 ? 14.600  40.068  20.641  1.00 50.55  ? 224 LYS B CD  1 
ATOM   5455 C  CE  . LYS B 1 224 ? 14.931  38.593  20.547  1.00 48.21  ? 224 LYS B CE  1 
ATOM   5456 N  NZ  . LYS B 1 224 ? 15.206  38.198  19.146  1.00 54.92  ? 224 LYS B NZ  1 
ATOM   5457 N  N   . ALA B 1 225 ? 12.074  44.352  23.748  1.00 48.55  ? 225 ALA B N   1 
ATOM   5458 C  CA  . ALA B 1 225 ? 12.117  45.773  24.058  1.00 50.86  ? 225 ALA B CA  1 
ATOM   5459 C  C   . ALA B 1 225 ? 11.328  46.104  25.324  1.00 60.41  ? 225 ALA B C   1 
ATOM   5460 O  O   . ALA B 1 225 ? 11.552  47.147  25.932  1.00 58.37  ? 225 ALA B O   1 
ATOM   5461 C  CB  . ALA B 1 225 ? 11.579  46.550  22.885  1.00 49.44  ? 225 ALA B CB  1 
ATOM   5462 N  N   . SER B 1 226 ? 10.389  45.234  25.716  1.00 70.98  ? 226 SER B N   1 
ATOM   5463 C  CA  . SER B 1 226 ? 9.690   45.399  26.982  1.00 72.48  ? 226 SER B CA  1 
ATOM   5464 C  C   . SER B 1 226 ? 10.575  44.939  28.142  1.00 78.89  ? 226 SER B C   1 
ATOM   5465 O  O   . SER B 1 226 ? 10.161  45.016  29.300  1.00 78.88  ? 226 SER B O   1 
ATOM   5466 C  CB  . SER B 1 226 ? 8.379   44.663  26.973  1.00 70.97  ? 226 SER B CB  1 
ATOM   5467 O  OG  . SER B 1 226 ? 8.585   43.274  26.770  1.00 74.07  ? 226 SER B OG  1 
ATOM   5468 N  N   . GLY B 1 227 ? 11.789  44.461  27.824  1.00 80.61  ? 227 GLY B N   1 
ATOM   5469 C  CA  . GLY B 1 227 ? 12.689  43.926  28.827  1.00 84.43  ? 227 GLY B CA  1 
ATOM   5470 C  C   . GLY B 1 227 ? 11.921  43.040  29.800  1.00 87.62  ? 227 GLY B C   1 
ATOM   5471 O  O   . GLY B 1 227 ? 11.906  43.296  31.006  1.00 87.10  ? 227 GLY B O   1 
ATOM   5472 N  N   . GLU B 1 228 ? 11.258  42.019  29.242  1.00 89.40  ? 228 GLU B N   1 
ATOM   5473 C  CA  . GLU B 1 228 ? 10.309  41.226  30.003  1.00 87.71  ? 228 GLU B CA  1 
ATOM   5474 C  C   . GLU B 1 228 ? 10.666  39.743  29.921  1.00 89.60  ? 228 GLU B C   1 
ATOM   5475 O  O   . GLU B 1 228 ? 11.177  39.283  28.902  1.00 89.01  ? 228 GLU B O   1 
ATOM   5476 C  CB  . GLU B 1 228 ? 8.886   41.505  29.511  1.00 81.68  ? 228 GLU B CB  1 
ATOM   5477 C  CG  . GLU B 1 228 ? 7.836   41.296  30.592  1.00 82.14  ? 228 GLU B CG  1 
ATOM   5478 C  CD  . GLU B 1 228 ? 8.307   41.629  32.003  1.00 80.51  ? 228 GLU B CD  1 
ATOM   5479 O  OE1 . GLU B 1 228 ? 8.698   42.805  32.239  1.00 73.73  ? 228 GLU B OE1 1 
ATOM   5480 O  OE2 . GLU B 1 228 ? 8.319   40.703  32.862  1.00 70.21  ? 228 GLU B OE2 1 
ATOM   5481 N  N   . GLN B 1 229 ? 10.409  39.033  31.034  1.00 95.23  ? 229 GLN B N   1 
ATOM   5482 C  CA  . GLN B 1 229 ? 10.476  37.577  31.119  1.00 91.95  ? 229 GLN B CA  1 
ATOM   5483 C  C   . GLN B 1 229 ? 9.126   37.043  31.621  1.00 83.07  ? 229 GLN B C   1 
ATOM   5484 O  O   . GLN B 1 229 ? 9.078   36.052  32.356  1.00 70.42  ? 229 GLN B O   1 
ATOM   5485 C  CB  . GLN B 1 229 ? 11.619  37.134  32.047  1.00 91.77  ? 229 GLN B CB  1 
ATOM   5486 C  CG  . GLN B 1 229 ? 12.958  37.833  31.806  1.00 88.49  ? 229 GLN B CG  1 
ATOM   5487 C  CD  . GLN B 1 229 ? 13.675  37.400  30.546  1.00 82.59  ? 229 GLN B CD  1 
ATOM   5488 O  OE1 . GLN B 1 229 ? 14.419  36.418  30.524  1.00 77.72  ? 229 GLN B OE1 1 
ATOM   5489 N  NE2 . GLN B 1 229 ? 13.505  38.178  29.491  1.00 79.86  ? 229 GLN B NE2 1 
ATOM   5490 N  N   . SER B 1 230 ? 8.036   37.719  31.212  1.00 73.38  ? 230 SER B N   1 
ATOM   5491 C  CA  . SER B 1 230 ? 6.673   37.327  31.535  1.00 64.34  ? 230 SER B CA  1 
ATOM   5492 C  C   . SER B 1 230 ? 6.486   35.853  31.196  1.00 55.54  ? 230 SER B C   1 
ATOM   5493 O  O   . SER B 1 230 ? 6.243   35.522  30.040  1.00 68.33  ? 230 SER B O   1 
ATOM   5494 C  CB  . SER B 1 230 ? 5.669   38.197  30.793  1.00 64.86  ? 230 SER B CB  1 
ATOM   5495 O  OG  . SER B 1 230 ? 6.104   38.493  29.469  1.00 57.38  ? 230 SER B OG  1 
ATOM   5496 N  N   . ASP B 1 231 ? 6.638   34.964  32.179  1.00 49.17  ? 231 ASP B N   1 
ATOM   5497 C  CA  . ASP B 1 231 ? 6.669   33.538  31.873  1.00 45.89  ? 231 ASP B CA  1 
ATOM   5498 C  C   . ASP B 1 231 ? 5.399   33.148  31.117  1.00 38.94  ? 231 ASP B C   1 
ATOM   5499 O  O   . ASP B 1 231 ? 4.351   32.929  31.726  1.00 36.50  ? 231 ASP B O   1 
ATOM   5500 C  CB  . ASP B 1 231 ? 6.929   32.674  33.108  1.00 49.86  ? 231 ASP B CB  1 
ATOM   5501 C  CG  . ASP B 1 231 ? 8.363   32.182  33.154  1.00 55.65  ? 231 ASP B CG  1 
ATOM   5502 O  OD1 . ASP B 1 231 ? 8.691   31.253  32.373  1.00 58.92  ? 231 ASP B OD1 1 
ATOM   5503 O  OD2 . ASP B 1 231 ? 9.157   32.771  33.910  1.00 57.88  ? 231 ASP B OD2 1 
ATOM   5504 N  N   . ASP B 1 232 ? 5.517   33.137  29.776  1.00 31.25  ? 232 ASP B N   1 
ATOM   5505 C  CA  . ASP B 1 232 ? 4.467   32.667  28.884  1.00 25.90  ? 232 ASP B CA  1 
ATOM   5506 C  C   . ASP B 1 232 ? 5.124   31.777  27.832  1.00 23.12  ? 232 ASP B C   1 
ATOM   5507 O  O   . ASP B 1 232 ? 6.318   31.489  27.902  1.00 21.25  ? 232 ASP B O   1 
ATOM   5508 C  CB  . ASP B 1 232 ? 3.651   33.861  28.360  1.00 26.20  ? 232 ASP B CB  1 
ATOM   5509 C  CG  . ASP B 1 232 ? 4.394   34.894  27.505  1.00 29.59  ? 232 ASP B CG  1 
ATOM   5510 O  OD1 . ASP B 1 232 ? 5.586   34.639  27.167  1.00 24.08  ? 232 ASP B OD1 1 
ATOM   5511 O  OD2 . ASP B 1 232 ? 3.784   35.983  27.167  1.00 27.61  ? 232 ASP B OD2 1 
ATOM   5512 N  N   . LEU B 1 233 ? 4.349   31.358  26.830  1.00 19.84  ? 233 LEU B N   1 
ATOM   5513 C  CA  . LEU B 1 233 ? 4.849   30.488  25.790  1.00 18.55  ? 233 LEU B CA  1 
ATOM   5514 C  C   . LEU B 1 233 ? 6.067   31.109  25.114  1.00 18.90  ? 233 LEU B C   1 
ATOM   5515 O  O   . LEU B 1 233 ? 7.067   30.441  24.875  1.00 16.56  ? 233 LEU B O   1 
ATOM   5516 C  CB  . LEU B 1 233 ? 3.680   30.269  24.827  1.00 20.99  ? 233 LEU B CB  1 
ATOM   5517 C  CG  . LEU B 1 233 ? 3.914   29.402  23.598  1.00 19.96  ? 233 LEU B CG  1 
ATOM   5518 C  CD1 . LEU B 1 233 ? 4.392   28.003  23.979  1.00 22.29  ? 233 LEU B CD1 1 
ATOM   5519 C  CD2 . LEU B 1 233 ? 2.606   29.270  22.805  1.00 19.07  ? 233 LEU B CD2 1 
ATOM   5520 N  N   . LEU B 1 234 ? 6.012   32.417  24.843  1.00 18.01  ? 234 LEU B N   1 
ATOM   5521 C  CA  . LEU B 1 234 ? 7.122   33.070  24.168  1.00 18.25  ? 234 LEU B CA  1 
ATOM   5522 C  C   . LEU B 1 234 ? 8.388   33.033  25.031  1.00 16.79  ? 234 LEU B C   1 
ATOM   5523 O  O   . LEU B 1 234 ? 9.480   32.945  24.505  1.00 17.35  ? 234 LEU B O   1 
ATOM   5524 C  CB  . LEU B 1 234 ? 6.719   34.517  23.853  1.00 18.06  ? 234 LEU B CB  1 
ATOM   5525 C  CG  . LEU B 1 234 ? 7.680   35.311  22.986  1.00 17.95  ? 234 LEU B CG  1 
ATOM   5526 C  CD1 . LEU B 1 234 ? 7.872   34.649  21.644  1.00 20.14  ? 234 LEU B CD1 1 
ATOM   5527 C  CD2 . LEU B 1 234 ? 7.145   36.721  22.787  1.00 21.44  ? 234 LEU B CD2 1 
ATOM   5528 N  N   . THR B 1 235 ? 8.222   33.122  26.350  1.00 19.13  ? 235 THR B N   1 
ATOM   5529 C  CA  . THR B 1 235 ? 9.350   33.088  27.269  1.00 20.41  ? 235 THR B CA  1 
ATOM   5530 C  C   . THR B 1 235 ? 10.138  31.804  27.060  1.00 20.67  ? 235 THR B C   1 
ATOM   5531 O  O   . THR B 1 235 ? 11.372  31.816  26.975  1.00 21.40  ? 235 THR B O   1 
ATOM   5532 C  CB  . THR B 1 235 ? 8.892   33.145  28.730  1.00 22.55  ? 235 THR B CB  1 
ATOM   5533 O  OG1 . THR B 1 235 ? 8.138   34.362  28.895  1.00 20.43  ? 235 THR B OG1 1 
ATOM   5534 C  CG2 . THR B 1 235 ? 10.067  33.077  29.688  1.00 23.39  ? 235 THR B CG2 1 
ATOM   5535 N  N   . HIS B 1 236 ? 9.385   30.710  26.970  1.00 18.61  ? 236 HIS B N   1 
ATOM   5536 C  CA  . HIS B 1 236 ? 9.963   29.392  26.794  1.00 20.76  ? 236 HIS B CA  1 
ATOM   5537 C  C   . HIS B 1 236 ? 10.622  29.312  25.424  1.00 19.45  ? 236 HIS B C   1 
ATOM   5538 O  O   . HIS B 1 236 ? 11.732  28.828  25.341  1.00 21.29  ? 236 HIS B O   1 
ATOM   5539 C  CB  . HIS B 1 236 ? 8.916   28.309  27.084  1.00 20.18  ? 236 HIS B CB  1 
ATOM   5540 C  CG  . HIS B 1 236 ? 8.612   28.196  28.534  1.00 23.20  ? 236 HIS B CG  1 
ATOM   5541 N  ND1 . HIS B 1 236 ? 7.593   28.906  29.133  1.00 27.47  ? 236 HIS B ND1 1 
ATOM   5542 C  CD2 . HIS B 1 236 ? 9.144   27.429  29.492  1.00 26.01  ? 236 HIS B CD2 1 
ATOM   5543 C  CE1 . HIS B 1 236 ? 7.532   28.591  30.421  1.00 27.02  ? 236 HIS B CE1 1 
ATOM   5544 N  NE2 . HIS B 1 236 ? 8.486   27.711  30.661  1.00 28.00  ? 236 HIS B NE2 1 
ATOM   5545 N  N   . MET B 1 237 ? 9.974   29.816  24.361  1.00 19.06  ? 237 MET B N   1 
ATOM   5546 C  CA  . MET B 1 237 ? 10.554  29.748  23.031  1.00 20.14  ? 237 MET B CA  1 
ATOM   5547 C  C   . MET B 1 237 ? 11.904  30.457  23.016  1.00 23.07  ? 237 MET B C   1 
ATOM   5548 O  O   . MET B 1 237 ? 12.844  29.976  22.394  1.00 24.06  ? 237 MET B O   1 
ATOM   5549 C  CB  . MET B 1 237 ? 9.679   30.429  21.981  1.00 20.22  ? 237 MET B CB  1 
ATOM   5550 C  CG  . MET B 1 237 ? 8.568   29.567  21.449  1.00 20.40  ? 237 MET B CG  1 
ATOM   5551 S  SD  . MET B 1 237 ? 7.504   30.578  20.398  1.00 22.76  ? 237 MET B SD  1 
ATOM   5552 C  CE  . MET B 1 237 ? 5.904   29.783  20.564  1.00 22.86  ? 237 MET B CE  1 
ATOM   5553 N  N   . LEU B 1 238 ? 12.004  31.593  23.711  1.00 21.34  ? 238 LEU B N   1 
ATOM   5554 C  CA  . LEU B 1 238 ? 13.174  32.454  23.587  1.00 21.82  ? 238 LEU B CA  1 
ATOM   5555 C  C   . LEU B 1 238 ? 14.299  31.991  24.516  1.00 23.08  ? 238 LEU B C   1 
ATOM   5556 O  O   . LEU B 1 238 ? 15.464  32.246  24.206  1.00 27.39  ? 238 LEU B O   1 
ATOM   5557 C  CB  . LEU B 1 238 ? 12.782  33.912  23.887  1.00 22.72  ? 238 LEU B CB  1 
ATOM   5558 C  CG  . LEU B 1 238 ? 11.886  34.602  22.858  1.00 23.14  ? 238 LEU B CG  1 
ATOM   5559 C  CD1 . LEU B 1 238 ? 11.453  36.016  23.314  1.00 25.77  ? 238 LEU B CD1 1 
ATOM   5560 C  CD2 . LEU B 1 238 ? 12.550  34.703  21.512  1.00 22.51  ? 238 LEU B CD2 1 
ATOM   5561 N  N   . ASN B 1 239 ? 13.956  31.347  25.642  1.00 23.58  ? 239 ASN B N   1 
ATOM   5562 C  CA  . ASN B 1 239 ? 14.889  31.109  26.740  1.00 24.94  ? 239 ASN B CA  1 
ATOM   5563 C  C   . ASN B 1 239 ? 15.053  29.636  27.125  1.00 24.46  ? 239 ASN B C   1 
ATOM   5564 O  O   . ASN B 1 239 ? 16.056  29.302  27.745  1.00 23.98  ? 239 ASN B O   1 
ATOM   5565 C  CB  . ASN B 1 239 ? 14.465  31.831  28.022  1.00 26.48  ? 239 ASN B CB  1 
ATOM   5566 C  CG  . ASN B 1 239 ? 14.243  33.311  27.784  1.00 30.44  ? 239 ASN B CG  1 
ATOM   5567 O  OD1 . ASN B 1 239 ? 13.127  33.810  27.956  1.00 32.37  ? 239 ASN B OD1 1 
ATOM   5568 N  ND2 . ASN B 1 239 ? 15.278  33.986  27.318  1.00 26.63  ? 239 ASN B ND2 1 
ATOM   5569 N  N   . GLY B 1 240 ? 14.058  28.771  26.868  1.00 20.60  ? 240 GLY B N   1 
ATOM   5570 C  CA  . GLY B 1 240 ? 14.130  27.406  27.350  1.00 18.93  ? 240 GLY B CA  1 
ATOM   5571 C  C   . GLY B 1 240 ? 15.170  26.586  26.594  1.00 20.62  ? 240 GLY B C   1 
ATOM   5572 O  O   . GLY B 1 240 ? 15.406  26.818  25.410  1.00 18.66  ? 240 GLY B O   1 
ATOM   5573 N  N   . LYS B 1 241 ? 15.830  25.654  27.290  1.00 21.06  ? 241 LYS B N   1 
ATOM   5574 C  CA  . LYS B 1 241 ? 16.807  24.799  26.643  1.00 22.31  ? 241 LYS B CA  1 
ATOM   5575 C  C   . LYS B 1 241 ? 16.301  23.369  26.702  1.00 19.81  ? 241 LYS B C   1 
ATOM   5576 O  O   . LYS B 1 241 ? 15.643  22.972  27.654  1.00 19.64  ? 241 LYS B O   1 
ATOM   5577 C  CB  . LYS B 1 241 ? 18.212  25.007  27.234  1.00 27.55  ? 241 LYS B CB  1 
ATOM   5578 C  CG  . LYS B 1 241 ? 18.790  26.381  26.915  1.00 32.77  ? 241 LYS B CG  1 
ATOM   5579 C  CD  . LYS B 1 241 ? 20.307  26.534  26.965  1.00 40.77  ? 241 LYS B CD  1 
ATOM   5580 C  CE  . LYS B 1 241 ? 20.790  27.314  28.173  1.00 47.38  ? 241 LYS B CE  1 
ATOM   5581 N  NZ  . LYS B 1 241 ? 22.112  27.947  27.944  1.00 48.29  ? 241 LYS B NZ  1 
ATOM   5582 N  N   . ASP B 1 242 ? 16.520  22.631  25.624  1.00 19.62  ? 242 ASP B N   1 
ATOM   5583 C  CA  . ASP B 1 242 ? 16.094  21.242  25.560  1.00 20.55  ? 242 ASP B CA  1 
ATOM   5584 C  C   . ASP B 1 242 ? 16.991  20.389  26.460  1.00 20.76  ? 242 ASP B C   1 
ATOM   5585 O  O   . ASP B 1 242 ? 18.203  20.426  26.309  1.00 23.48  ? 242 ASP B O   1 
ATOM   5586 C  CB  . ASP B 1 242 ? 16.109  20.728  24.122  1.00 20.12  ? 242 ASP B CB  1 
ATOM   5587 C  CG  . ASP B 1 242 ? 16.170  19.215  23.956  1.00 20.12  ? 242 ASP B CG  1 
ATOM   5588 O  OD1 . ASP B 1 242 ? 15.517  18.525  24.733  1.00 24.70  ? 242 ASP B OD1 1 
ATOM   5589 O  OD2 . ASP B 1 242 ? 16.795  18.748  23.005  1.00 18.80  ? 242 ASP B OD2 1 
ATOM   5590 N  N   . PRO B 1 243 ? 16.446  19.626  27.428  1.00 20.92  ? 243 PRO B N   1 
ATOM   5591 C  CA  . PRO B 1 243 ? 17.262  18.763  28.285  1.00 22.74  ? 243 PRO B CA  1 
ATOM   5592 C  C   . PRO B 1 243 ? 18.116  17.731  27.555  1.00 26.99  ? 243 PRO B C   1 
ATOM   5593 O  O   . PRO B 1 243 ? 19.266  17.524  27.939  1.00 28.69  ? 243 PRO B O   1 
ATOM   5594 C  CB  . PRO B 1 243 ? 16.269  18.106  29.262  1.00 24.95  ? 243 PRO B CB  1 
ATOM   5595 C  CG  . PRO B 1 243 ? 14.906  18.403  28.710  1.00 26.85  ? 243 PRO B CG  1 
ATOM   5596 C  CD  . PRO B 1 243 ? 15.034  19.657  27.866  1.00 24.81  ? 243 PRO B CD  1 
ATOM   5597 N  N   . GLU B 1 244 ? 17.611  17.126  26.476  1.00 22.06  ? 244 GLU B N   1 
ATOM   5598 C  CA  . GLU B 1 244 ? 18.385  16.144  25.744  1.00 25.97  ? 244 GLU B CA  1 
ATOM   5599 C  C   . GLU B 1 244 ? 19.615  16.795  25.107  1.00 26.34  ? 244 GLU B C   1 
ATOM   5600 O  O   . GLU B 1 244 ? 20.743  16.409  25.413  1.00 30.06  ? 244 GLU B O   1 
ATOM   5601 C  CB  . GLU B 1 244 ? 17.523  15.458  24.683  1.00 29.33  ? 244 GLU B CB  1 
ATOM   5602 C  CG  . GLU B 1 244 ? 16.421  14.583  25.269  1.00 34.99  ? 244 GLU B CG  1 
ATOM   5603 C  CD  . GLU B 1 244 ? 15.507  13.965  24.221  1.00 36.62  ? 244 GLU B CD  1 
ATOM   5604 O  OE1 . GLU B 1 244 ? 15.926  13.969  23.007  1.00 37.99  ? 244 GLU B OE1 1 
ATOM   5605 O  OE2 . GLU B 1 244 ? 14.374  13.527  24.601  1.00 35.44  ? 244 GLU B OE2 1 
ATOM   5606 N  N   . THR B 1 245 ? 19.408  17.777  24.221  1.00 25.83  ? 245 THR B N   1 
ATOM   5607 C  CA  . THR B 1 245 ? 20.491  18.386  23.456  1.00 24.13  ? 245 THR B CA  1 
ATOM   5608 C  C   . THR B 1 245 ? 21.259  19.412  24.284  1.00 23.44  ? 245 THR B C   1 
ATOM   5609 O  O   . THR B 1 245 ? 22.416  19.658  23.978  1.00 23.97  ? 245 THR B O   1 
ATOM   5610 C  CB  . THR B 1 245 ? 19.995  19.027  22.154  1.00 23.53  ? 245 THR B CB  1 
ATOM   5611 O  OG1 . THR B 1 245 ? 19.037  20.062  22.442  1.00 22.40  ? 245 THR B OG1 1 
ATOM   5612 C  CG2 . THR B 1 245 ? 19.419  17.985  21.211  1.00 23.75  ? 245 THR B CG2 1 
ATOM   5613 N  N   . GLY B 1 246 ? 20.621  19.977  25.322  1.00 20.96  ? 246 GLY B N   1 
ATOM   5614 C  CA  . GLY B 1 246 ? 21.078  21.168  26.018  1.00 19.00  ? 246 GLY B CA  1 
ATOM   5615 C  C   . GLY B 1 246 ? 20.997  22.438  25.164  1.00 18.87  ? 246 GLY B C   1 
ATOM   5616 O  O   . GLY B 1 246 ? 21.491  23.475  25.595  1.00 17.96  ? 246 GLY B O   1 
ATOM   5617 N  N   . GLU B 1 247 ? 20.384  22.384  23.963  1.00 17.85  ? 247 GLU B N   1 
ATOM   5618 C  CA  . GLU B 1 247 ? 20.307  23.532  23.065  1.00 18.56  ? 247 GLU B CA  1 
ATOM   5619 C  C   . GLU B 1 247 ? 18.972  24.293  23.171  1.00 19.79  ? 247 GLU B C   1 
ATOM   5620 O  O   . GLU B 1 247 ? 17.920  23.732  23.513  1.00 18.30  ? 247 GLU B O   1 
ATOM   5621 C  CB  . GLU B 1 247 ? 20.449  23.122  21.603  1.00 20.18  ? 247 GLU B CB  1 
ATOM   5622 C  CG  . GLU B 1 247 ? 21.804  22.562  21.165  1.00 20.27  ? 247 GLU B CG  1 
ATOM   5623 C  CD  . GLU B 1 247 ? 21.707  21.961  19.767  1.00 23.69  ? 247 GLU B CD  1 
ATOM   5624 O  OE1 . GLU B 1 247 ? 20.831  22.422  19.028  1.00 27.36  ? 247 GLU B OE1 1 
ATOM   5625 O  OE2 . GLU B 1 247 ? 22.422  20.977  19.433  1.00 26.42  ? 247 GLU B OE2 1 
ATOM   5626 N  N   . PRO B 1 248 ? 18.965  25.620  22.884  1.00 20.63  ? 248 PRO B N   1 
ATOM   5627 C  CA  . PRO B 1 248 ? 17.724  26.378  22.709  1.00 19.29  ? 248 PRO B CA  1 
ATOM   5628 C  C   . PRO B 1 248 ? 17.232  26.257  21.264  1.00 18.76  ? 248 PRO B C   1 
ATOM   5629 O  O   . PRO B 1 248 ? 17.914  25.725  20.399  1.00 18.76  ? 248 PRO B O   1 
ATOM   5630 C  CB  . PRO B 1 248 ? 18.141  27.820  23.030  1.00 20.99  ? 248 PRO B CB  1 
ATOM   5631 C  CG  . PRO B 1 248 ? 19.592  27.891  22.615  1.00 22.02  ? 248 PRO B CG  1 
ATOM   5632 C  CD  . PRO B 1 248 ? 20.147  26.474  22.703  1.00 21.50  ? 248 PRO B CD  1 
ATOM   5633 N  N   . LEU B 1 249 ? 16.045  26.811  20.987  1.00 19.30  ? 249 LEU B N   1 
ATOM   5634 C  CA  . LEU B 1 249 ? 15.564  26.945  19.621  1.00 18.98  ? 249 LEU B CA  1 
ATOM   5635 C  C   . LEU B 1 249 ? 16.425  27.977  18.907  1.00 21.40  ? 249 LEU B C   1 
ATOM   5636 O  O   . LEU B 1 249 ? 16.820  28.930  19.543  1.00 22.33  ? 249 LEU B O   1 
ATOM   5637 C  CB  . LEU B 1 249 ? 14.104  27.417  19.682  1.00 18.98  ? 249 LEU B CB  1 
ATOM   5638 C  CG  . LEU B 1 249 ? 13.104  26.431  20.268  1.00 20.06  ? 249 LEU B CG  1 
ATOM   5639 C  CD1 . LEU B 1 249 ? 11.666  26.919  20.123  1.00 20.27  ? 249 LEU B CD1 1 
ATOM   5640 C  CD2 . LEU B 1 249 ? 13.299  25.077  19.619  1.00 22.39  ? 249 LEU B CD2 1 
ATOM   5641 N  N   . ASP B 1 250 ? 16.689  27.829  17.602  1.00 20.21  ? 250 ASP B N   1 
ATOM   5642 C  CA  . ASP B 1 250 ? 17.369  28.909  16.919  1.00 25.92  ? 250 ASP B CA  1 
ATOM   5643 C  C   . ASP B 1 250 ? 16.319  29.923  16.446  1.00 25.11  ? 250 ASP B C   1 
ATOM   5644 O  O   . ASP B 1 250 ? 15.113  29.673  16.535  1.00 20.71  ? 250 ASP B O   1 
ATOM   5645 C  CB  . ASP B 1 250 ? 18.309  28.374  15.835  1.00 28.31  ? 250 ASP B CB  1 
ATOM   5646 C  CG  . ASP B 1 250 ? 17.600  27.628  14.730  1.00 32.71  ? 250 ASP B CG  1 
ATOM   5647 O  OD1 . ASP B 1 250 ? 16.380  27.691  14.699  1.00 33.74  ? 250 ASP B OD1 1 
ATOM   5648 O  OD2 . ASP B 1 250 ? 18.286  26.958  13.933  1.00 43.77  ? 250 ASP B OD2 1 
ATOM   5649 N  N   . ASP B 1 251 ? 16.788  31.055  15.898  1.00 25.73  ? 251 ASP B N   1 
ATOM   5650 C  CA  . ASP B 1 251 ? 15.913  32.178  15.578  1.00 25.96  ? 251 ASP B CA  1 
ATOM   5651 C  C   . ASP B 1 251 ? 14.829  31.774  14.587  1.00 23.66  ? 251 ASP B C   1 
ATOM   5652 O  O   . ASP B 1 251 ? 13.659  32.074  14.788  1.00 23.10  ? 251 ASP B O   1 
ATOM   5653 C  CB  . ASP B 1 251 ? 16.708  33.373  15.055  1.00 27.11  ? 251 ASP B CB  1 
ATOM   5654 C  CG  . ASP B 1 251 ? 17.168  34.347  16.132  1.00 32.15  ? 251 ASP B CG  1 
ATOM   5655 O  OD1 . ASP B 1 251 ? 16.672  34.255  17.292  1.00 32.99  ? 251 ASP B OD1 1 
ATOM   5656 O  OD2 . ASP B 1 251 ? 18.004  35.222  15.803  1.00 33.17  ? 251 ASP B OD2 1 
ATOM   5657 N  N   . GLU B 1 252 ? 15.238  31.091  13.521  1.00 26.21  ? 252 GLU B N   1 
ATOM   5658 C  CA  . GLU B 1 252 ? 14.355  30.744  12.422  1.00 27.59  ? 252 GLU B CA  1 
ATOM   5659 C  C   . GLU B 1 252 ? 13.217  29.862  12.936  1.00 23.28  ? 252 GLU B C   1 
ATOM   5660 O  O   . GLU B 1 252 ? 12.047  30.026  12.544  1.00 20.57  ? 252 GLU B O   1 
ATOM   5661 C  CB  . GLU B 1 252 ? 15.183  30.080  11.309  1.00 34.64  ? 252 GLU B CB  1 
ATOM   5662 C  CG  . GLU B 1 252 ? 14.343  29.381  10.249  1.00 43.18  ? 252 GLU B CG  1 
ATOM   5663 C  CD  . GLU B 1 252 ? 15.076  28.605  9.160   1.00 47.82  ? 252 GLU B CD  1 
ATOM   5664 O  OE1 . GLU B 1 252 ? 15.296  27.394  9.355   1.00 52.58  ? 252 GLU B OE1 1 
ATOM   5665 O  OE2 . GLU B 1 252 ? 15.339  29.185  8.078   1.00 49.70  ? 252 GLU B OE2 1 
ATOM   5666 N  N   . ASN B 1 253 ? 13.558  28.897  13.796  1.00 21.73  ? 253 ASN B N   1 
ATOM   5667 C  CA  . ASN B 1 253 ? 12.565  27.952  14.307  1.00 18.80  ? 253 ASN B CA  1 
ATOM   5668 C  C   . ASN B 1 253 ? 11.548  28.652  15.207  1.00 16.56  ? 253 ASN B C   1 
ATOM   5669 O  O   . ASN B 1 253 ? 10.350  28.337  15.207  1.00 15.40  ? 253 ASN B O   1 
ATOM   5670 C  CB  . ASN B 1 253 ? 13.204  26.794  15.079  1.00 17.99  ? 253 ASN B CB  1 
ATOM   5671 C  CG  . ASN B 1 253 ? 12.171  25.747  15.460  1.00 17.44  ? 253 ASN B CG  1 
ATOM   5672 O  OD1 . ASN B 1 253 ? 11.729  25.653  16.605  1.00 16.77  ? 253 ASN B OD1 1 
ATOM   5673 N  ND2 . ASN B 1 253 ? 11.747  24.972  14.484  1.00 19.70  ? 253 ASN B ND2 1 
ATOM   5674 N  N   . ILE B 1 254 ? 12.039  29.541  16.074  1.00 16.34  ? 254 ILE B N   1 
ATOM   5675 C  CA  . ILE B 1 254 ? 11.176  30.367  16.915  1.00 18.17  ? 254 ILE B CA  1 
ATOM   5676 C  C   . ILE B 1 254 ? 10.112  31.056  16.058  1.00 18.02  ? 254 ILE B C   1 
ATOM   5677 O  O   . ILE B 1 254 ? 8.940   31.061  16.413  1.00 16.85  ? 254 ILE B O   1 
ATOM   5678 C  CB  . ILE B 1 254 ? 12.001  31.387  17.723  1.00 19.86  ? 254 ILE B CB  1 
ATOM   5679 C  CG1 . ILE B 1 254 ? 12.929  30.702  18.725  1.00 21.40  ? 254 ILE B CG1 1 
ATOM   5680 C  CG2 . ILE B 1 254 ? 11.094  32.383  18.437  1.00 20.13  ? 254 ILE B CG2 1 
ATOM   5681 C  CD1 . ILE B 1 254 ? 14.068  31.580  19.199  1.00 21.70  ? 254 ILE B CD1 1 
ATOM   5682 N  N   . ARG B 1 255 ? 10.519  31.598  14.903  1.00 18.02  ? 255 ARG B N   1 
ATOM   5683 C  CA  . ARG B 1 255 ? 9.596   32.289  14.018  1.00 20.72  ? 255 ARG B CA  1 
ATOM   5684 C  C   . ARG B 1 255 ? 8.495   31.337  13.567  1.00 18.39  ? 255 ARG B C   1 
ATOM   5685 O  O   . ARG B 1 255 ? 7.300   31.640  13.658  1.00 16.45  ? 255 ARG B O   1 
ATOM   5686 C  CB  . ARG B 1 255 ? 10.359  32.900  12.828  1.00 22.76  ? 255 ARG B CB  1 
ATOM   5687 C  CG  . ARG B 1 255 ? 11.233  34.089  13.194  1.00 26.79  ? 255 ARG B CG  1 
ATOM   5688 C  CD  . ARG B 1 255 ? 12.039  34.523  11.977  1.00 28.88  ? 255 ARG B CD  1 
ATOM   5689 N  NE  . ARG B 1 255 ? 11.208  35.228  11.013  1.00 30.66  ? 255 ARG B NE  1 
ATOM   5690 C  CZ  . ARG B 1 255 ? 10.737  36.455  11.203  1.00 34.23  ? 255 ARG B CZ  1 
ATOM   5691 N  NH1 . ARG B 1 255 ? 11.196  37.179  12.212  1.00 35.28  ? 255 ARG B NH1 1 
ATOM   5692 N  NH2 . ARG B 1 255 ? 9.794   36.936  10.405  1.00 35.79  ? 255 ARG B NH2 1 
ATOM   5693 N  N   . TYR B 1 256 ? 8.908   30.149  13.109  1.00 20.84  ? 256 TYR B N   1 
ATOM   5694 C  CA  . TYR B 1 256 ? 7.950   29.141  12.719  1.00 19.98  ? 256 TYR B CA  1 
ATOM   5695 C  C   . TYR B 1 256 ? 7.039   28.732  13.875  1.00 18.60  ? 256 TYR B C   1 
ATOM   5696 O  O   . TYR B 1 256 ? 5.853   28.468  13.642  1.00 20.91  ? 256 TYR B O   1 
ATOM   5697 C  CB  . TYR B 1 256 ? 8.643   27.900  12.182  1.00 22.61  ? 256 TYR B CB  1 
ATOM   5698 C  CG  . TYR B 1 256 ? 9.316   28.098  10.842  1.00 23.88  ? 256 TYR B CG  1 
ATOM   5699 C  CD1 . TYR B 1 256 ? 8.633   28.661  9.771   1.00 25.35  ? 256 TYR B CD1 1 
ATOM   5700 C  CD2 . TYR B 1 256 ? 10.649  27.729  10.662  1.00 23.26  ? 256 TYR B CD2 1 
ATOM   5701 C  CE1 . TYR B 1 256 ? 9.278   28.880  8.559   1.00 28.33  ? 256 TYR B CE1 1 
ATOM   5702 C  CE2 . TYR B 1 256 ? 11.281  27.900  9.443   1.00 25.61  ? 256 TYR B CE2 1 
ATOM   5703 C  CZ  . TYR B 1 256 ? 10.592  28.467  8.393   1.00 28.14  ? 256 TYR B CZ  1 
ATOM   5704 O  OH  . TYR B 1 256 ? 11.234  28.595  7.202   1.00 40.16  ? 256 TYR B OH  1 
ATOM   5705 N  N   . GLN B 1 257 ? 7.575   28.632  15.095  1.00 15.28  ? 257 GLN B N   1 
ATOM   5706 C  CA  . GLN B 1 257 ? 6.732   28.264  16.217  1.00 13.51  ? 257 GLN B CA  1 
ATOM   5707 C  C   . GLN B 1 257 ? 5.638   29.315  16.456  1.00 14.43  ? 257 GLN B C   1 
ATOM   5708 O  O   . GLN B 1 257 ? 4.515   28.957  16.799  1.00 12.80  ? 257 GLN B O   1 
ATOM   5709 C  CB  . GLN B 1 257 ? 7.525   28.017  17.490  1.00 12.65  ? 257 GLN B CB  1 
ATOM   5710 C  CG  . GLN B 1 257 ? 8.497   26.838  17.453  1.00 12.65  ? 257 GLN B CG  1 
ATOM   5711 C  CD  . GLN B 1 257 ? 7.965   25.498  16.991  1.00 12.93  ? 257 GLN B CD  1 
ATOM   5712 O  OE1 . GLN B 1 257 ? 6.758   25.261  16.909  1.00 13.62  ? 257 GLN B OE1 1 
ATOM   5713 N  NE2 . GLN B 1 257 ? 8.887   24.569  16.784  1.00 12.43  ? 257 GLN B NE2 1 
ATOM   5714 N  N   . ILE B 1 258 ? 5.986   30.602  16.319  1.00 13.16  ? 258 ILE B N   1 
ATOM   5715 C  CA  . ILE B 1 258 ? 5.044   31.685  16.560  1.00 14.18  ? 258 ILE B CA  1 
ATOM   5716 C  C   . ILE B 1 258 ? 3.906   31.558  15.559  1.00 14.18  ? 258 ILE B C   1 
ATOM   5717 O  O   . ILE B 1 258 ? 2.754   31.516  15.957  1.00 14.45  ? 258 ILE B O   1 
ATOM   5718 C  CB  . ILE B 1 258 ? 5.754   33.057  16.574  1.00 14.09  ? 258 ILE B CB  1 
ATOM   5719 C  CG1 . ILE B 1 258 ? 6.774   33.093  17.715  1.00 14.57  ? 258 ILE B CG1 1 
ATOM   5720 C  CG2 . ILE B 1 258 ? 4.724   34.181  16.733  1.00 14.96  ? 258 ILE B CG2 1 
ATOM   5721 C  CD1 . ILE B 1 258 ? 7.795   34.183  17.627  1.00 16.00  ? 258 ILE B CD1 1 
ATOM   5722 N  N   . ILE B 1 259 ? 4.261   31.415  14.278  1.00 14.07  ? 259 ILE B N   1 
ATOM   5723 C  CA  . ILE B 1 259 ? 3.279   31.230  13.233  1.00 18.78  ? 259 ILE B CA  1 
ATOM   5724 C  C   . ILE B 1 259 ? 2.412   30.017  13.553  1.00 18.29  ? 259 ILE B C   1 
ATOM   5725 O  O   . ILE B 1 259 ? 1.191   30.087  13.494  1.00 17.65  ? 259 ILE B O   1 
ATOM   5726 C  CB  . ILE B 1 259 ? 3.951   31.116  11.849  1.00 21.78  ? 259 ILE B CB  1 
ATOM   5727 C  CG1 . ILE B 1 259 ? 4.561   32.448  11.436  1.00 23.94  ? 259 ILE B CG1 1 
ATOM   5728 C  CG2 . ILE B 1 259 ? 2.965   30.584  10.797  1.00 26.27  ? 259 ILE B CG2 1 
ATOM   5729 C  CD1 . ILE B 1 259 ? 5.429   32.354  10.218  1.00 25.82  ? 259 ILE B CD1 1 
ATOM   5730 N  N   . THR B 1 260 ? 3.069   28.903  13.888  1.00 17.98  ? 260 THR B N   1 
ATOM   5731 C  CA  . THR B 1 260 ? 2.353   27.671  14.173  1.00 18.02  ? 260 THR B CA  1 
ATOM   5732 C  C   . THR B 1 260 ? 1.310   27.847  15.274  1.00 16.41  ? 260 THR B C   1 
ATOM   5733 O  O   . THR B 1 260 ? 0.161   27.376  15.141  1.00 14.22  ? 260 THR B O   1 
ATOM   5734 C  CB  . THR B 1 260 ? 3.349   26.570  14.552  1.00 17.23  ? 260 THR B CB  1 
ATOM   5735 O  OG1 . THR B 1 260 ? 4.199   26.344  13.419  1.00 18.04  ? 260 THR B OG1 1 
ATOM   5736 C  CG2 . THR B 1 260 ? 2.662   25.297  14.995  1.00 18.21  ? 260 THR B CG2 1 
ATOM   5737 N  N   . PHE B 1 261 ? 1.745   28.384  16.416  1.00 16.14  ? 261 PHE B N   1 
ATOM   5738 C  CA  . PHE B 1 261 ? 0.889   28.518  17.587  1.00 17.67  ? 261 PHE B CA  1 
ATOM   5739 C  C   . PHE B 1 261 ? -0.204  29.575  17.358  1.00 19.21  ? 261 PHE B C   1 
ATOM   5740 O  O   . PHE B 1 261 ? -1.342  29.381  17.796  1.00 18.90  ? 261 PHE B O   1 
ATOM   5741 C  CB  . PHE B 1 261 ? 1.753   28.794  18.818  1.00 18.50  ? 261 PHE B CB  1 
ATOM   5742 C  CG  . PHE B 1 261 ? 2.299   27.562  19.475  1.00 19.85  ? 261 PHE B CG  1 
ATOM   5743 C  CD1 . PHE B 1 261 ? 1.520   26.848  20.367  1.00 22.07  ? 261 PHE B CD1 1 
ATOM   5744 C  CD2 . PHE B 1 261 ? 3.563   27.092  19.173  1.00 20.68  ? 261 PHE B CD2 1 
ATOM   5745 C  CE1 . PHE B 1 261 ? 2.002   25.711  20.969  1.00 21.82  ? 261 PHE B CE1 1 
ATOM   5746 C  CE2 . PHE B 1 261 ? 4.065   25.974  19.812  1.00 23.38  ? 261 PHE B CE2 1 
ATOM   5747 C  CZ  . PHE B 1 261 ? 3.283   25.287  20.705  1.00 22.75  ? 261 PHE B CZ  1 
ATOM   5748 N  N   . LEU B 1 262 ? 0.116   30.647  16.625  1.00 18.62  ? 262 LEU B N   1 
ATOM   5749 C  CA  . LEU B 1 262 ? -0.883  31.658  16.293  1.00 21.13  ? 262 LEU B CA  1 
ATOM   5750 C  C   . LEU B 1 262 ? -1.983  31.090  15.380  1.00 25.70  ? 262 LEU B C   1 
ATOM   5751 O  O   . LEU B 1 262 ? -3.152  31.381  15.618  1.00 24.99  ? 262 LEU B O   1 
ATOM   5752 C  CB  . LEU B 1 262 ? -0.193  32.867  15.668  1.00 20.15  ? 262 LEU B CB  1 
ATOM   5753 C  CG  . LEU B 1 262 ? 0.522   33.786  16.662  1.00 18.28  ? 262 LEU B CG  1 
ATOM   5754 C  CD1 . LEU B 1 262 ? 1.045   35.022  15.971  1.00 20.69  ? 262 LEU B CD1 1 
ATOM   5755 C  CD2 . LEU B 1 262 ? -0.343  34.166  17.857  1.00 17.77  ? 262 LEU B CD2 1 
ATOM   5756 N  N   . GLY B 1 263 ? -1.630  30.268  14.373  1.00 30.48  ? 263 GLY B N   1 
ATOM   5757 C  CA  . GLY B 1 263 ? -2.624  29.546  13.572  1.00 33.03  ? 263 GLY B CA  1 
ATOM   5758 C  C   . GLY B 1 263 ? -3.317  28.395  14.320  1.00 32.93  ? 263 GLY B C   1 
ATOM   5759 O  O   . GLY B 1 263 ? -4.537  28.391  14.521  1.00 34.40  ? 263 GLY B O   1 
ATOM   5760 N  N   . GLY B 1 264 ? -2.532  27.412  14.780  1.00 29.97  ? 264 GLY B N   1 
ATOM   5761 C  CA  . GLY B 1 264 ? -3.088  26.227  15.410  1.00 27.73  ? 264 GLY B CA  1 
ATOM   5762 C  C   . GLY B 1 264 ? -3.769  26.508  16.751  1.00 28.76  ? 264 GLY B C   1 
ATOM   5763 O  O   . GLY B 1 264 ? -4.662  25.765  17.177  1.00 26.96  ? 264 GLY B O   1 
ATOM   5764 N  N   . GLY B 1 265 ? -3.367  27.606  17.410  1.00 23.99  ? 265 GLY B N   1 
ATOM   5765 C  CA  . GLY B 1 265 ? -3.805  27.870  18.772  1.00 24.28  ? 265 GLY B CA  1 
ATOM   5766 C  C   . GLY B 1 265 ? -5.221  28.439  18.907  1.00 22.55  ? 265 GLY B C   1 
ATOM   5767 O  O   . GLY B 1 265 ? -5.679  28.630  20.028  1.00 26.66  ? 265 GLY B O   1 
ATOM   5768 N  N   . HIS B 1 266 ? -5.943  28.654  17.804  1.00 20.69  ? 266 HIS B N   1 
ATOM   5769 C  CA  . HIS B 1 266 ? -7.241  29.298  17.916  1.00 20.85  ? 266 HIS B CA  1 
ATOM   5770 C  C   . HIS B 1 266 ? -8.299  28.626  17.043  1.00 19.39  ? 266 HIS B C   1 
ATOM   5771 O  O   . HIS B 1 266 ? -9.433  28.547  17.455  1.00 17.79  ? 266 HIS B O   1 
ATOM   5772 C  CB  . HIS B 1 266 ? -7.129  30.799  17.606  1.00 18.47  ? 266 HIS B CB  1 
ATOM   5773 C  CG  . HIS B 1 266 ? -7.188  31.110  16.166  1.00 17.57  ? 266 HIS B CG  1 
ATOM   5774 N  ND1 . HIS B 1 266 ? -6.040  31.211  15.410  1.00 20.57  ? 266 HIS B ND1 1 
ATOM   5775 C  CD2 . HIS B 1 266 ? -8.223  31.304  15.322  1.00 20.81  ? 266 HIS B CD2 1 
ATOM   5776 C  CE1 . HIS B 1 266 ? -6.370  31.472  14.140  1.00 20.94  ? 266 HIS B CE1 1 
ATOM   5777 N  NE2 . HIS B 1 266 ? -7.697  31.532  14.059  1.00 21.28  ? 266 HIS B NE2 1 
ATOM   5778 N  N   . GLU B 1 267 ? -7.959  28.198  15.823  1.00 24.11  ? 267 GLU B N   1 
ATOM   5779 C  CA  . GLU B 1 267 ? -8.983  27.836  14.851  1.00 25.68  ? 267 GLU B CA  1 
ATOM   5780 C  C   . GLU B 1 267 ? -9.830  26.643  15.327  1.00 21.68  ? 267 GLU B C   1 
ATOM   5781 O  O   . GLU B 1 267 ? -11.065 26.667  15.286  1.00 19.44  ? 267 GLU B O   1 
ATOM   5782 C  CB  . GLU B 1 267 ? -8.317  27.525  13.507  1.00 33.81  ? 267 GLU B CB  1 
ATOM   5783 C  CG  . GLU B 1 267 ? -9.292  27.195  12.384  1.00 41.91  ? 267 GLU B CG  1 
ATOM   5784 C  CD  . GLU B 1 267 ? -8.768  27.494  10.980  1.00 57.23  ? 267 GLU B CD  1 
ATOM   5785 O  OE1 . GLU B 1 267 ? -8.549  26.531  10.191  1.00 61.43  ? 267 GLU B OE1 1 
ATOM   5786 O  OE2 . GLU B 1 267 ? -8.578  28.696  10.659  1.00 64.03  ? 267 GLU B OE2 1 
ATOM   5787 N  N   . THR B 1 268 ? -9.166  25.567  15.756  1.00 16.95  ? 268 THR B N   1 
ATOM   5788 C  CA  . THR B 1 268 ? -9.860  24.372  16.197  1.00 16.16  ? 268 THR B CA  1 
ATOM   5789 C  C   . THR B 1 268 ? -10.684 24.666  17.438  1.00 15.53  ? 268 THR B C   1 
ATOM   5790 O  O   . THR B 1 268 ? -11.797 24.129  17.596  1.00 14.59  ? 268 THR B O   1 
ATOM   5791 C  CB  . THR B 1 268 ? -8.887  23.214  16.446  1.00 14.62  ? 268 THR B CB  1 
ATOM   5792 O  OG1 . THR B 1 268 ? -7.721  23.820  17.011  1.00 13.91  ? 268 THR B OG1 1 
ATOM   5793 C  CG2 . THR B 1 268 ? -8.548  22.454  15.189  1.00 15.01  ? 268 THR B CG2 1 
ATOM   5794 N  N   . THR B 1 269 ? -10.165 25.559  18.292  1.00 15.08  ? 269 THR B N   1 
ATOM   5795 C  CA  . THR B 1 269 ? -10.876 25.846  19.521  1.00 14.06  ? 269 THR B CA  1 
ATOM   5796 C  C   . THR B 1 269 ? -12.159 26.606  19.182  1.00 13.48  ? 269 THR B C   1 
ATOM   5797 O  O   . THR B 1 269 ? -13.164 26.373  19.835  1.00 13.49  ? 269 THR B O   1 
ATOM   5798 C  CB  . THR B 1 269 ? -9.979  26.594  20.513  1.00 13.26  ? 269 THR B CB  1 
ATOM   5799 O  OG1 . THR B 1 269 ? -8.766  25.862  20.692  1.00 13.84  ? 269 THR B OG1 1 
ATOM   5800 C  CG2 . THR B 1 269 ? -10.638 26.840  21.847  1.00 13.38  ? 269 THR B CG2 1 
ATOM   5801 N  N   . SER B 1 270 ? -12.080 27.610  18.280  1.00 13.42  ? 270 SER B N   1 
ATOM   5802 C  CA  . SER B 1 270 ? -13.272 28.369  17.914  1.00 13.73  ? 270 SER B CA  1 
ATOM   5803 C  C   . SER B 1 270 ? -14.343 27.462  17.288  1.00 13.46  ? 270 SER B C   1 
ATOM   5804 O  O   . SER B 1 270 ? -15.535 27.572  17.595  1.00 11.87  ? 270 SER B O   1 
ATOM   5805 C  CB  . SER B 1 270 ? -12.945 29.526  17.026  1.00 14.49  ? 270 SER B CB  1 
ATOM   5806 O  OG  . SER B 1 270 ? -12.398 29.101  15.809  1.00 15.97  ? 270 SER B OG  1 
ATOM   5807 N  N   . GLY B 1 271 ? -13.880 26.505  16.459  1.00 12.80  ? 271 GLY B N   1 
ATOM   5808 C  CA  . GLY B 1 271 ? -14.746 25.448  15.950  1.00 12.88  ? 271 GLY B CA  1 
ATOM   5809 C  C   . GLY B 1 271 ? -15.490 24.718  17.077  1.00 12.33  ? 271 GLY B C   1 
ATOM   5810 O  O   . GLY B 1 271 ? -16.699 24.585  17.045  1.00 10.20  ? 271 GLY B O   1 
ATOM   5811 N  N   . LEU B 1 272 ? -14.733 24.234  18.067  1.00 11.86  ? 272 LEU B N   1 
ATOM   5812 C  CA  . LEU B 1 272 ? -15.268 23.505  19.194  1.00 11.08  ? 272 LEU B CA  1 
ATOM   5813 C  C   . LEU B 1 272 ? -16.349 24.314  19.906  1.00 11.46  ? 272 LEU B C   1 
ATOM   5814 O  O   . LEU B 1 272 ? -17.451 23.798  20.193  1.00 9.39   ? 272 LEU B O   1 
ATOM   5815 C  CB  . LEU B 1 272 ? -14.141 23.140  20.151  1.00 11.24  ? 272 LEU B CB  1 
ATOM   5816 C  CG  . LEU B 1 272 ? -14.609 22.601  21.489  1.00 11.91  ? 272 LEU B CG  1 
ATOM   5817 C  CD1 . LEU B 1 272 ? -15.571 21.446  21.325  1.00 11.51  ? 272 LEU B CD1 1 
ATOM   5818 C  CD2 . LEU B 1 272 ? -13.414 22.197  22.335  1.00 13.09  ? 272 LEU B CD2 1 
ATOM   5819 N  N   . LEU B 1 273 ? -16.039 25.583  20.189  1.00 11.57  ? 273 LEU B N   1 
ATOM   5820 C  CA  . LEU B 1 273 ? -17.015 26.398  20.903  1.00 11.53  ? 273 LEU B CA  1 
ATOM   5821 C  C   . LEU B 1 273 ? -18.281 26.600  20.078  1.00 10.92  ? 273 LEU B C   1 
ATOM   5822 O  O   . LEU B 1 273 ? -19.357 26.569  20.669  1.00 12.37  ? 273 LEU B O   1 
ATOM   5823 C  CB  . LEU B 1 273 ? -16.403 27.751  21.292  1.00 12.41  ? 273 LEU B CB  1 
ATOM   5824 C  CG  . LEU B 1 273 ? -15.520 27.696  22.545  1.00 11.69  ? 273 LEU B CG  1 
ATOM   5825 C  CD1 . LEU B 1 273 ? -14.611 28.920  22.652  1.00 12.67  ? 273 LEU B CD1 1 
ATOM   5826 C  CD2 . LEU B 1 273 ? -16.338 27.494  23.790  1.00 11.81  ? 273 LEU B CD2 1 
ATOM   5827 N  N   . SER B 1 274 ? -18.139 26.777  18.755  1.00 10.56  ? 274 SER B N   1 
ATOM   5828 C  CA  . SER B 1 274 ? -19.259 27.034  17.866  1.00 11.61  ? 274 SER B CA  1 
ATOM   5829 C  C   . SER B 1 274 ? -20.156 25.785  17.769  1.00 12.60  ? 274 SER B C   1 
ATOM   5830 O  O   . SER B 1 274 ? -21.383 25.885  17.860  1.00 13.12  ? 274 SER B O   1 
ATOM   5831 C  CB  . SER B 1 274 ? -18.759 27.510  16.527  1.00 11.50  ? 274 SER B CB  1 
ATOM   5832 O  OG  . SER B 1 274 ? -17.945 28.693  16.675  1.00 12.36  ? 274 SER B OG  1 
ATOM   5833 N  N   . PHE B 1 275 ? -19.533 24.598  17.625  1.00 11.97  ? 275 PHE B N   1 
ATOM   5834 C  CA  . PHE B 1 275 ? -20.294 23.343  17.625  1.00 12.35  ? 275 PHE B CA  1 
ATOM   5835 C  C   . PHE B 1 275 ? -20.976 23.076  18.976  1.00 12.56  ? 275 PHE B C   1 
ATOM   5836 O  O   . PHE B 1 275 ? -22.149 22.667  19.068  1.00 13.19  ? 275 PHE B O   1 
ATOM   5837 C  CB  . PHE B 1 275 ? -19.437 22.129  17.235  1.00 12.82  ? 275 PHE B CB  1 
ATOM   5838 C  CG  . PHE B 1 275 ? -19.139 21.994  15.767  1.00 13.14  ? 275 PHE B CG  1 
ATOM   5839 C  CD1 . PHE B 1 275 ? -20.149 21.703  14.868  1.00 14.64  ? 275 PHE B CD1 1 
ATOM   5840 C  CD2 . PHE B 1 275 ? -17.861 22.176  15.270  1.00 12.94  ? 275 PHE B CD2 1 
ATOM   5841 C  CE1 . PHE B 1 275 ? -19.883 21.563  13.508  1.00 14.05  ? 275 PHE B CE1 1 
ATOM   5842 C  CE2 . PHE B 1 275 ? -17.595 22.035  13.916  1.00 14.04  ? 275 PHE B CE2 1 
ATOM   5843 C  CZ  . PHE B 1 275 ? -18.617 21.746  13.024  1.00 14.14  ? 275 PHE B CZ  1 
ATOM   5844 N  N   . ALA B 1 276 ? -20.233 23.283  20.047  1.00 13.16  ? 276 ALA B N   1 
ATOM   5845 C  CA  . ALA B 1 276 ? -20.812 23.083  21.365  1.00 13.45  ? 276 ALA B CA  1 
ATOM   5846 C  C   . ALA B 1 276 ? -22.039 23.982  21.563  1.00 15.37  ? 276 ALA B C   1 
ATOM   5847 O  O   . ALA B 1 276 ? -23.062 23.509  22.089  1.00 16.59  ? 276 ALA B O   1 
ATOM   5848 C  CB  . ALA B 1 276 ? -19.783 23.338  22.443  1.00 14.58  ? 276 ALA B CB  1 
ATOM   5849 N  N   . LEU B 1 277 ? -21.978 25.267  21.145  1.00 14.62  ? 277 LEU B N   1 
ATOM   5850 C  CA  . LEU B 1 277 ? -23.164 26.124  21.293  1.00 14.88  ? 277 LEU B CA  1 
ATOM   5851 C  C   . LEU B 1 277 ? -24.288 25.635  20.378  1.00 13.64  ? 277 LEU B C   1 
ATOM   5852 O  O   . LEU B 1 277 ? -25.432 25.720  20.779  1.00 13.86  ? 277 LEU B O   1 
ATOM   5853 C  CB  . LEU B 1 277 ? -22.881 27.615  21.056  1.00 16.55  ? 277 LEU B CB  1 
ATOM   5854 C  CG  . LEU B 1 277 ? -24.050 28.582  21.355  1.00 19.36  ? 277 LEU B CG  1 
ATOM   5855 C  CD1 . LEU B 1 277 ? -24.576 28.399  22.769  1.00 20.36  ? 277 LEU B CD1 1 
ATOM   5856 C  CD2 . LEU B 1 277 ? -23.655 30.041  21.187  1.00 19.74  ? 277 LEU B CD2 1 
ATOM   5857 N  N   . TYR B 1 278 ? -23.961 25.236  19.143  1.00 14.00  ? 278 TYR B N   1 
ATOM   5858 C  CA  . TYR B 1 278 ? -24.917 24.624  18.229  1.00 15.01  ? 278 TYR B CA  1 
ATOM   5859 C  C   . TYR B 1 278 ? -25.662 23.475  18.920  1.00 14.50  ? 278 TYR B C   1 
ATOM   5860 O  O   . TYR B 1 278 ? -26.887 23.420  18.898  1.00 12.94  ? 278 TYR B O   1 
ATOM   5861 C  CB  . TYR B 1 278 ? -24.240 24.151  16.945  1.00 13.15  ? 278 TYR B CB  1 
ATOM   5862 C  CG  . TYR B 1 278 ? -25.132 23.271  16.096  1.00 14.43  ? 278 TYR B CG  1 
ATOM   5863 C  CD1 . TYR B 1 278 ? -26.147 23.814  15.297  1.00 16.26  ? 278 TYR B CD1 1 
ATOM   5864 C  CD2 . TYR B 1 278 ? -25.094 21.895  16.221  1.00 15.98  ? 278 TYR B CD2 1 
ATOM   5865 C  CE1 . TYR B 1 278 ? -26.988 23.000  14.555  1.00 15.94  ? 278 TYR B CE1 1 
ATOM   5866 C  CE2 . TYR B 1 278 ? -25.949 21.072  15.508  1.00 16.45  ? 278 TYR B CE2 1 
ATOM   5867 C  CZ  . TYR B 1 278 ? -26.897 21.621  14.664  1.00 17.62  ? 278 TYR B CZ  1 
ATOM   5868 O  OH  . TYR B 1 278 ? -27.700 20.776  13.913  1.00 17.86  ? 278 TYR B OH  1 
ATOM   5869 N  N   . PHE B 1 279 ? -24.922 22.502  19.474  1.00 13.44  ? 279 PHE B N   1 
ATOM   5870 C  CA  . PHE B 1 279 ? -25.578 21.337  20.048  1.00 15.14  ? 279 PHE B CA  1 
ATOM   5871 C  C   . PHE B 1 279 ? -26.412 21.696  21.270  1.00 15.30  ? 279 PHE B C   1 
ATOM   5872 O  O   . PHE B 1 279 ? -27.457 21.086  21.460  1.00 16.09  ? 279 PHE B O   1 
ATOM   5873 C  CB  . PHE B 1 279 ? -24.594 20.208  20.402  1.00 14.34  ? 279 PHE B CB  1 
ATOM   5874 C  CG  . PHE B 1 279 ? -24.111 19.479  19.172  1.00 16.18  ? 279 PHE B CG  1 
ATOM   5875 C  CD1 . PHE B 1 279 ? -25.014 18.769  18.367  1.00 17.21  ? 279 PHE B CD1 1 
ATOM   5876 C  CD2 . PHE B 1 279 ? -22.757 19.462  18.835  1.00 16.10  ? 279 PHE B CD2 1 
ATOM   5877 C  CE1 . PHE B 1 279 ? -24.573 18.121  17.217  1.00 17.90  ? 279 PHE B CE1 1 
ATOM   5878 C  CE2 . PHE B 1 279 ? -22.322 18.803  17.693  1.00 16.12  ? 279 PHE B CE2 1 
ATOM   5879 C  CZ  . PHE B 1 279 ? -23.236 18.139  16.872  1.00 16.47  ? 279 PHE B CZ  1 
ATOM   5880 N  N   . LEU B 1 280 ? -25.967 22.683  22.067  1.00 13.38  ? 280 LEU B N   1 
ATOM   5881 C  CA  . LEU B 1 280 ? -26.703 23.113  23.237  1.00 14.95  ? 280 LEU B CA  1 
ATOM   5882 C  C   . LEU B 1 280 ? -28.087 23.680  22.851  1.00 15.42  ? 280 LEU B C   1 
ATOM   5883 O  O   . LEU B 1 280 ? -29.086 23.220  23.416  1.00 14.65  ? 280 LEU B O   1 
ATOM   5884 C  CB  . LEU B 1 280 ? -25.831 24.130  23.990  1.00 16.65  ? 280 LEU B CB  1 
ATOM   5885 C  CG  . LEU B 1 280 ? -24.742 23.508  24.857  1.00 15.55  ? 280 LEU B CG  1 
ATOM   5886 C  CD1 . LEU B 1 280 ? -23.758 24.524  25.404  1.00 15.74  ? 280 LEU B CD1 1 
ATOM   5887 C  CD2 . LEU B 1 280 ? -25.371 22.765  26.000  1.00 16.45  ? 280 LEU B CD2 1 
ATOM   5888 N  N   . VAL B 1 281 ? -28.156 24.596  21.852  1.00 16.31  ? 281 VAL B N   1 
ATOM   5889 C  CA  . VAL B 1 281 ? -29.432 25.185  21.425  1.00 16.90  ? 281 VAL B CA  1 
ATOM   5890 C  C   . VAL B 1 281 ? -30.329 24.176  20.723  1.00 18.15  ? 281 VAL B C   1 
ATOM   5891 O  O   . VAL B 1 281 ? -31.523 24.364  20.723  1.00 18.87  ? 281 VAL B O   1 
ATOM   5892 C  CB  . VAL B 1 281 ? -29.282 26.450  20.556  1.00 16.28  ? 281 VAL B CB  1 
ATOM   5893 C  CG1 . VAL B 1 281 ? -28.389 27.469  21.255  1.00 18.06  ? 281 VAL B CG1 1 
ATOM   5894 C  CG2 . VAL B 1 281 ? -28.781 26.171  19.162  1.00 15.52  ? 281 VAL B CG2 1 
ATOM   5895 N  N   . LYS B 1 282 ? -29.768 23.140  20.098  1.00 17.98  ? 282 LYS B N   1 
ATOM   5896 C  CA  . LYS B 1 282 ? -30.555 22.074  19.505  1.00 18.16  ? 282 LYS B CA  1 
ATOM   5897 C  C   . LYS B 1 282 ? -30.973 21.030  20.542  1.00 18.43  ? 282 LYS B C   1 
ATOM   5898 O  O   . LYS B 1 282 ? -31.774 20.144  20.218  1.00 18.61  ? 282 LYS B O   1 
ATOM   5899 C  CB  . LYS B 1 282 ? -29.762 21.379  18.400  1.00 17.20  ? 282 LYS B CB  1 
ATOM   5900 C  CG  . LYS B 1 282 ? -29.452 22.223  17.172  1.00 18.32  ? 282 LYS B CG  1 
ATOM   5901 C  CD  . LYS B 1 282 ? -30.717 22.685  16.434  1.00 18.98  ? 282 LYS B CD  1 
ATOM   5902 C  CE  . LYS B 1 282 ? -30.407 23.317  15.102  1.00 19.01  ? 282 LYS B CE  1 
ATOM   5903 N  NZ  . LYS B 1 282 ? -31.591 24.069  14.572  1.00 19.32  ? 282 LYS B NZ  1 
ATOM   5904 N  N   . ASN B 1 283 ? -30.442 21.117  21.771  1.00 16.80  ? 283 ASN B N   1 
ATOM   5905 C  CA  . ASN B 1 283 ? -30.778 20.172  22.834  1.00 17.97  ? 283 ASN B CA  1 
ATOM   5906 C  C   . ASN B 1 283 ? -31.054 20.902  24.140  1.00 18.98  ? 283 ASN B C   1 
ATOM   5907 O  O   . ASN B 1 283 ? -30.249 20.872  25.062  1.00 17.97  ? 283 ASN B O   1 
ATOM   5908 C  CB  . ASN B 1 283 ? -29.662 19.133  23.013  1.00 18.50  ? 283 ASN B CB  1 
ATOM   5909 C  CG  . ASN B 1 283 ? -29.528 18.274  21.779  1.00 16.43  ? 283 ASN B CG  1 
ATOM   5910 O  OD1 . ASN B 1 283 ? -30.264 17.309  21.645  1.00 17.17  ? 283 ASN B OD1 1 
ATOM   5911 N  ND2 . ASN B 1 283 ? -28.705 18.668  20.817  1.00 16.67  ? 283 ASN B ND2 1 
ATOM   5912 N  N   . PRO B 1 284 ? -32.234 21.529  24.301  1.00 18.96  ? 284 PRO B N   1 
ATOM   5913 C  CA  . PRO B 1 284 ? -32.511 22.377  25.447  1.00 19.95  ? 284 PRO B CA  1 
ATOM   5914 C  C   . PRO B 1 284 ? -32.398 21.700  26.808  1.00 18.01  ? 284 PRO B C   1 
ATOM   5915 O  O   . PRO B 1 284 ? -32.163 22.403  27.778  1.00 15.45  ? 284 PRO B O   1 
ATOM   5916 C  CB  . PRO B 1 284 ? -33.968 22.813  25.252  1.00 20.98  ? 284 PRO B CB  1 
ATOM   5917 C  CG  . PRO B 1 284 ? -34.194 22.650  23.780  1.00 19.97  ? 284 PRO B CG  1 
ATOM   5918 C  CD  . PRO B 1 284 ? -33.384 21.440  23.381  1.00 20.28  ? 284 PRO B CD  1 
ATOM   5919 N  N   . HIS B 1 285 ? -32.638 20.382  26.904  1.00 17.19  ? 285 HIS B N   1 
ATOM   5920 C  CA  . HIS B 1 285 ? -32.518 19.686  28.182  1.00 17.25  ? 285 HIS B CA  1 
ATOM   5921 C  C   . HIS B 1 285 ? -31.040 19.663  28.615  1.00 15.72  ? 285 HIS B C   1 
ATOM   5922 O  O   . HIS B 1 285 ? -30.718 19.804  29.794  1.00 17.51  ? 285 HIS B O   1 
ATOM   5923 C  CB  . HIS B 1 285 ? -33.123 18.274  28.142  1.00 18.10  ? 285 HIS B CB  1 
ATOM   5924 C  CG  . HIS B 1 285 ? -34.624 18.280  28.070  1.00 23.05  ? 285 HIS B CG  1 
ATOM   5925 N  ND1 . HIS B 1 285 ? -35.404 19.113  28.856  1.00 24.32  ? 285 HIS B ND1 1 
ATOM   5926 C  CD2 . HIS B 1 285 ? -35.475 17.624  27.274  1.00 25.59  ? 285 HIS B CD2 1 
ATOM   5927 C  CE1 . HIS B 1 285 ? -36.675 18.932  28.560  1.00 23.48  ? 285 HIS B CE1 1 
ATOM   5928 N  NE2 . HIS B 1 285 ? -36.739 18.046  27.597  1.00 24.75  ? 285 HIS B NE2 1 
ATOM   5929 N  N   . VAL B 1 286 ? -30.145 19.502  27.643  1.00 16.94  ? 286 VAL B N   1 
ATOM   5930 C  CA  . VAL B 1 286 ? -28.708 19.517  27.890  1.00 16.14  ? 286 VAL B CA  1 
ATOM   5931 C  C   . VAL B 1 286 ? -28.234 20.933  28.241  1.00 17.51  ? 286 VAL B C   1 
ATOM   5932 O  O   . VAL B 1 286 ? -27.487 21.091  29.195  1.00 16.07  ? 286 VAL B O   1 
ATOM   5933 C  CB  . VAL B 1 286 ? -27.948 18.958  26.686  1.00 15.47  ? 286 VAL B CB  1 
ATOM   5934 C  CG1 . VAL B 1 286 ? -26.438 19.145  26.839  1.00 13.43  ? 286 VAL B CG1 1 
ATOM   5935 C  CG2 . VAL B 1 286 ? -28.345 17.507  26.446  1.00 15.54  ? 286 VAL B CG2 1 
ATOM   5936 N  N   . LEU B 1 287 ? -28.766 21.953  27.557  1.00 18.88  ? 287 LEU B N   1 
ATOM   5937 C  CA  . LEU B 1 287 ? -28.435 23.349  27.841  1.00 20.22  ? 287 LEU B CA  1 
ATOM   5938 C  C   . LEU B 1 287 ? -28.825 23.652  29.286  1.00 19.44  ? 287 LEU B C   1 
ATOM   5939 O  O   . LEU B 1 287 ? -28.043 24.227  30.049  1.00 16.78  ? 287 LEU B O   1 
ATOM   5940 C  CB  . LEU B 1 287 ? -29.155 24.259  26.830  1.00 22.27  ? 287 LEU B CB  1 
ATOM   5941 C  CG  . LEU B 1 287 ? -29.003 25.778  26.984  1.00 24.34  ? 287 LEU B CG  1 
ATOM   5942 C  CD1 . LEU B 1 287 ? -27.569 26.174  27.199  1.00 27.60  ? 287 LEU B CD1 1 
ATOM   5943 C  CD2 . LEU B 1 287 ? -29.515 26.510  25.754  1.00 23.54  ? 287 LEU B CD2 1 
ATOM   5944 N  N   . GLN B 1 288 ? -30.036 23.244  29.672  1.00 16.84  ? 288 GLN B N   1 
ATOM   5945 C  CA  . GLN B 1 288 ? -30.542 23.537  31.000  1.00 18.89  ? 288 GLN B CA  1 
ATOM   5946 C  C   . GLN B 1 288 ? -29.660 22.914  32.078  1.00 17.26  ? 288 GLN B C   1 
ATOM   5947 O  O   . GLN B 1 288 ? -29.440 23.507  33.114  1.00 17.80  ? 288 GLN B O   1 
ATOM   5948 C  CB  . GLN B 1 288 ? -31.947 22.984  31.182  1.00 21.91  ? 288 GLN B CB  1 
ATOM   5949 C  CG  . GLN B 1 288 ? -32.597 23.342  32.500  1.00 24.58  ? 288 GLN B CG  1 
ATOM   5950 C  CD  . GLN B 1 288 ? -33.990 22.749  32.565  1.00 32.14  ? 288 GLN B CD  1 
ATOM   5951 O  OE1 . GLN B 1 288 ? -34.905 23.136  31.826  1.00 31.93  ? 288 GLN B OE1 1 
ATOM   5952 N  NE2 . GLN B 1 288 ? -34.142 21.770  33.446  1.00 33.15  ? 288 GLN B NE2 1 
ATOM   5953 N  N   . LYS B 1 289 ? -29.228 21.687  31.857  1.00 18.93  ? 289 LYS B N   1 
ATOM   5954 C  CA  . LYS B 1 289 ? -28.406 20.983  32.813  1.00 17.81  ? 289 LYS B CA  1 
ATOM   5955 C  C   . LYS B 1 289 ? -27.036 21.640  32.867  1.00 15.18  ? 289 LYS B C   1 
ATOM   5956 O  O   . LYS B 1 289 ? -26.454 21.723  33.944  1.00 14.20  ? 289 LYS B O   1 
ATOM   5957 C  CB  . LYS B 1 289 ? -28.286 19.512  32.424  1.00 20.10  ? 289 LYS B CB  1 
ATOM   5958 C  CG  . LYS B 1 289 ? -27.585 18.659  33.457  1.00 22.59  ? 289 LYS B CG  1 
ATOM   5959 C  CD  . LYS B 1 289 ? -27.691 17.180  33.172  1.00 27.37  ? 289 LYS B CD  1 
ATOM   5960 C  CE  . LYS B 1 289 ? -26.909 16.339  34.168  1.00 29.39  ? 289 LYS B CE  1 
ATOM   5961 N  NZ  . LYS B 1 289 ? -27.055 14.890  33.862  1.00 30.31  ? 289 LYS B NZ  1 
ATOM   5962 N  N   . ALA B 1 290 ? -26.538 22.085  31.716  1.00 14.38  ? 290 ALA B N   1 
ATOM   5963 C  CA  . ALA B 1 290 ? -25.246 22.764  31.661  1.00 14.79  ? 290 ALA B CA  1 
ATOM   5964 C  C   . ALA B 1 290 ? -25.313 24.128  32.370  1.00 16.03  ? 290 ALA B C   1 
ATOM   5965 O  O   . ALA B 1 290 ? -24.395 24.498  33.095  1.00 13.46  ? 290 ALA B O   1 
ATOM   5966 C  CB  . ALA B 1 290 ? -24.781 22.877  30.233  1.00 14.66  ? 290 ALA B CB  1 
ATOM   5967 N  N   . ALA B 1 291 ? -26.409 24.870  32.169  1.00 18.25  ? 291 ALA B N   1 
ATOM   5968 C  CA  . ALA B 1 291 ? -26.672 26.132  32.850  1.00 18.36  ? 291 ALA B CA  1 
ATOM   5969 C  C   . ALA B 1 291 ? -26.806 25.954  34.360  1.00 19.05  ? 291 ALA B C   1 
ATOM   5970 O  O   . ALA B 1 291 ? -26.338 26.803  35.109  1.00 20.53  ? 291 ALA B O   1 
ATOM   5971 C  CB  . ALA B 1 291 ? -27.934 26.755  32.278  1.00 18.83  ? 291 ALA B CB  1 
ATOM   5972 N  N   . GLU B 1 292 ? -27.455 24.862  34.792  1.00 18.56  ? 292 GLU B N   1 
ATOM   5973 C  CA  . GLU B 1 292 ? -27.608 24.531  36.208  1.00 22.09  ? 292 GLU B CA  1 
ATOM   5974 C  C   . GLU B 1 292 ? -26.237 24.406  36.873  1.00 19.16  ? 292 GLU B C   1 
ATOM   5975 O  O   . GLU B 1 292 ? -25.997 24.954  37.961  1.00 17.62  ? 292 GLU B O   1 
ATOM   5976 C  CB  . GLU B 1 292 ? -28.471 23.277  36.357  1.00 25.30  ? 292 GLU B CB  1 
ATOM   5977 C  CG  . GLU B 1 292 ? -28.854 22.913  37.784  1.00 33.96  ? 292 GLU B CG  1 
ATOM   5978 C  CD  . GLU B 1 292 ? -27.832 22.145  38.621  1.00 38.62  ? 292 GLU B CD  1 
ATOM   5979 O  OE1 . GLU B 1 292 ? -28.131 21.787  39.814  1.00 41.18  ? 292 GLU B OE1 1 
ATOM   5980 O  OE2 . GLU B 1 292 ? -26.718 21.930  38.114  1.00 45.98  ? 292 GLU B OE2 1 
ATOM   5981 N  N   . GLU B 1 293 ? -25.315 23.737  36.186  1.00 19.90  ? 293 GLU B N   1 
ATOM   5982 C  CA  . GLU B 1 293 ? -23.980 23.569  36.730  1.00 19.05  ? 293 GLU B CA  1 
ATOM   5983 C  C   . GLU B 1 293 ? -23.257 24.917  36.760  1.00 18.37  ? 293 GLU B C   1 
ATOM   5984 O  O   . GLU B 1 293 ? -22.610 25.232  37.742  1.00 17.17  ? 293 GLU B O   1 
ATOM   5985 C  CB  . GLU B 1 293 ? -23.169 22.590  35.886  1.00 21.95  ? 293 GLU B CB  1 
ATOM   5986 C  CG  . GLU B 1 293 ? -21.729 22.447  36.370  1.00 21.59  ? 293 GLU B CG  1 
ATOM   5987 C  CD  . GLU B 1 293 ? -20.971 21.424  35.561  1.00 20.73  ? 293 GLU B CD  1 
ATOM   5988 O  OE1 . GLU B 1 293 ? -20.509 21.802  34.462  1.00 19.35  ? 293 GLU B OE1 1 
ATOM   5989 O  OE2 . GLU B 1 293 ? -20.916 20.222  36.000  1.00 21.49  ? 293 GLU B OE2 1 
ATOM   5990 N  N   . ALA B 1 294 ? -23.337 25.685  35.664  1.00 18.42  ? 294 ALA B N   1 
ATOM   5991 C  CA  . ALA B 1 294 ? -22.646 26.955  35.590  1.00 17.54  ? 294 ALA B CA  1 
ATOM   5992 C  C   . ALA B 1 294 ? -23.090 27.831  36.751  1.00 17.00  ? 294 ALA B C   1 
ATOM   5993 O  O   . ALA B 1 294 ? -22.267 28.380  37.472  1.00 16.66  ? 294 ALA B O   1 
ATOM   5994 C  CB  . ALA B 1 294 ? -22.831 27.616  34.249  1.00 16.90  ? 294 ALA B CB  1 
ATOM   5995 N  N   . ALA B 1 295 ? -24.390 27.907  36.996  1.00 17.58  ? 295 ALA B N   1 
ATOM   5996 C  CA  . ALA B 1 295 ? -24.857 28.791  38.045  1.00 19.26  ? 295 ALA B CA  1 
ATOM   5997 C  C   . ALA B 1 295 ? -24.472 28.278  39.434  1.00 18.92  ? 295 ALA B C   1 
ATOM   5998 O  O   . ALA B 1 295 ? -24.238 29.073  40.336  1.00 21.45  ? 295 ALA B O   1 
ATOM   5999 C  CB  . ALA B 1 295 ? -26.346 29.041  37.891  1.00 16.94  ? 295 ALA B CB  1 
ATOM   6000 N  N   . ARG B 1 296 ? -24.441 26.952  39.631  1.00 21.46  ? 296 ARG B N   1 
ATOM   6001 C  CA  . ARG B 1 296 ? -24.170 26.374  40.934  1.00 19.06  ? 296 ARG B CA  1 
ATOM   6002 C  C   . ARG B 1 296 ? -22.687 26.554  41.259  1.00 18.93  ? 296 ARG B C   1 
ATOM   6003 O  O   . ARG B 1 296 ? -22.334 26.746  42.421  1.00 16.24  ? 296 ARG B O   1 
ATOM   6004 C  CB  . ARG B 1 296 ? -24.596 24.902  40.973  1.00 21.15  ? 296 ARG B CB  1 
ATOM   6005 C  CG  . ARG B 1 296 ? -24.074 24.112  42.176  1.00 24.06  ? 296 ARG B CG  1 
ATOM   6006 C  CD  . ARG B 1 296 ? -24.785 22.780  42.342  1.00 26.29  ? 296 ARG B CD  1 
ATOM   6007 N  NE  . ARG B 1 296 ? -24.984 22.092  41.077  1.00 23.97  ? 296 ARG B NE  1 
ATOM   6008 C  CZ  . ARG B 1 296 ? -24.046 21.458  40.379  1.00 28.67  ? 296 ARG B CZ  1 
ATOM   6009 N  NH1 . ARG B 1 296 ? -22.907 21.093  40.935  1.00 30.55  ? 296 ARG B NH1 1 
ATOM   6010 N  NH2 . ARG B 1 296 ? -24.284 21.131  39.120  1.00 30.48  ? 296 ARG B NH2 1 
ATOM   6011 N  N   . ILE B 1 297 ? -21.820 26.449  40.240  1.00 18.98  ? 297 ILE B N   1 
ATOM   6012 C  CA  . ILE B 1 297 ? -20.377 26.425  40.455  1.00 19.15  ? 297 ILE B CA  1 
ATOM   6013 C  C   . ILE B 1 297 ? -19.761 27.827  40.374  1.00 20.15  ? 297 ILE B C   1 
ATOM   6014 O  O   . ILE B 1 297 ? -18.837 28.116  41.131  1.00 18.66  ? 297 ILE B O   1 
ATOM   6015 C  CB  . ILE B 1 297 ? -19.706 25.469  39.450  1.00 18.94  ? 297 ILE B CB  1 
ATOM   6016 C  CG1 . ILE B 1 297 ? -20.090 24.006  39.687  1.00 19.77  ? 297 ILE B CG1 1 
ATOM   6017 C  CG2 . ILE B 1 297 ? -18.198 25.696  39.401  1.00 17.79  ? 297 ILE B CG2 1 
ATOM   6018 C  CD1 . ILE B 1 297 ? -19.639 23.445  41.000  1.00 21.24  ? 297 ILE B CD1 1 
ATOM   6019 N  N   . LEU B 1 298 ? -20.171 28.663  39.395  1.00 20.51  ? 298 LEU B N   1 
ATOM   6020 C  CA  . LEU B 1 298 ? -19.522 29.941  39.129  1.00 19.85  ? 298 LEU B CA  1 
ATOM   6021 C  C   . LEU B 1 298 ? -20.157 31.028  39.994  1.00 22.50  ? 298 LEU B C   1 
ATOM   6022 O  O   . LEU B 1 298 ? -20.951 31.837  39.500  1.00 21.58  ? 298 LEU B O   1 
ATOM   6023 C  CB  . LEU B 1 298 ? -19.632 30.271  37.640  1.00 22.45  ? 298 LEU B CB  1 
ATOM   6024 C  CG  . LEU B 1 298 ? -18.952 29.258  36.716  1.00 22.17  ? 298 LEU B CG  1 
ATOM   6025 C  CD1 . LEU B 1 298 ? -19.051 29.682  35.275  1.00 23.66  ? 298 LEU B CD1 1 
ATOM   6026 C  CD2 . LEU B 1 298 ? -17.491 29.093  37.093  1.00 24.23  ? 298 LEU B CD2 1 
ATOM   6027 N  N   . VAL B 1 299 ? -19.812 31.016  41.296  1.00 21.65  ? 299 VAL B N   1 
ATOM   6028 C  CA  . VAL B 1 299 ? -20.542 31.770  42.308  1.00 24.05  ? 299 VAL B CA  1 
ATOM   6029 C  C   . VAL B 1 299 ? -19.887 33.135  42.550  1.00 24.42  ? 299 VAL B C   1 
ATOM   6030 O  O   . VAL B 1 299 ? -20.433 33.954  43.292  1.00 24.19  ? 299 VAL B O   1 
ATOM   6031 C  CB  . VAL B 1 299 ? -20.727 30.970  43.628  1.00 25.46  ? 299 VAL B CB  1 
ATOM   6032 C  CG1 . VAL B 1 299 ? -21.560 29.716  43.413  1.00 25.27  ? 299 VAL B CG1 1 
ATOM   6033 C  CG2 . VAL B 1 299 ? -19.422 30.589  44.311  1.00 25.58  ? 299 VAL B CG2 1 
ATOM   6034 N  N   . ASP B 1 300 ? -18.790 33.419  41.846  1.00 25.50  ? 300 ASP B N   1 
ATOM   6035 C  CA  . ASP B 1 300 ? -18.045 34.661  42.012  1.00 26.39  ? 300 ASP B CA  1 
ATOM   6036 C  C   . ASP B 1 300 ? -18.173 35.490  40.742  1.00 26.72  ? 300 ASP B C   1 
ATOM   6037 O  O   . ASP B 1 300 ? -18.488 34.959  39.690  1.00 28.69  ? 300 ASP B O   1 
ATOM   6038 C  CB  . ASP B 1 300 ? -16.584 34.359  42.361  1.00 26.86  ? 300 ASP B CB  1 
ATOM   6039 C  CG  . ASP B 1 300 ? -16.442 33.566  43.653  1.00 30.37  ? 300 ASP B CG  1 
ATOM   6040 O  OD1 . ASP B 1 300 ? -17.038 33.983  44.641  1.00 35.19  ? 300 ASP B OD1 1 
ATOM   6041 O  OD2 . ASP B 1 300 ? -15.735 32.526  43.666  1.00 29.92  ? 300 ASP B OD2 1 
ATOM   6042 N  N   . PRO B 1 301 ? -17.975 36.827  40.797  1.00 30.62  ? 301 PRO B N   1 
ATOM   6043 C  CA  . PRO B 1 301 ? -18.127 37.680  39.618  1.00 33.29  ? 301 PRO B CA  1 
ATOM   6044 C  C   . PRO B 1 301 ? -17.248 37.289  38.431  1.00 30.74  ? 301 PRO B C   1 
ATOM   6045 O  O   . PRO B 1 301 ? -17.588 37.570  37.290  1.00 27.69  ? 301 PRO B O   1 
ATOM   6046 C  CB  . PRO B 1 301 ? -17.721 39.087  40.085  1.00 35.46  ? 301 PRO B CB  1 
ATOM   6047 C  CG  . PRO B 1 301 ? -17.094 38.891  41.458  1.00 36.54  ? 301 PRO B CG  1 
ATOM   6048 C  CD  . PRO B 1 301 ? -17.663 37.602  42.008  1.00 33.50  ? 301 PRO B CD  1 
ATOM   6049 N  N   . VAL B 1 302 ? -16.083 36.697  38.698  1.00 30.64  ? 302 VAL B N   1 
ATOM   6050 C  CA  . VAL B 1 302 ? -15.326 36.080  37.625  1.00 30.62  ? 302 VAL B CA  1 
ATOM   6051 C  C   . VAL B 1 302 ? -14.905 34.685  38.071  1.00 25.75  ? 302 VAL B C   1 
ATOM   6052 O  O   . VAL B 1 302 ? -14.716 34.454  39.251  1.00 26.68  ? 302 VAL B O   1 
ATOM   6053 C  CB  . VAL B 1 302 ? -14.116 36.937  37.213  1.00 33.00  ? 302 VAL B CB  1 
ATOM   6054 C  CG1 . VAL B 1 302 ? -14.548 38.191  36.457  1.00 31.95  ? 302 VAL B CG1 1 
ATOM   6055 C  CG2 . VAL B 1 302 ? -13.241 37.288  38.412  1.00 36.30  ? 302 VAL B CG2 1 
ATOM   6056 N  N   . PRO B 1 303 ? -14.775 33.713  37.148  1.00 22.81  ? 303 PRO B N   1 
ATOM   6057 C  CA  . PRO B 1 303 ? -14.371 32.359  37.514  1.00 21.63  ? 303 PRO B CA  1 
ATOM   6058 C  C   . PRO B 1 303 ? -12.929 32.241  37.972  1.00 18.25  ? 303 PRO B C   1 
ATOM   6059 O  O   . PRO B 1 303 ? -12.056 32.897  37.422  1.00 17.85  ? 303 PRO B O   1 
ATOM   6060 C  CB  . PRO B 1 303 ? -14.558 31.572  36.211  1.00 23.00  ? 303 PRO B CB  1 
ATOM   6061 C  CG  . PRO B 1 303 ? -15.608 32.365  35.476  1.00 24.64  ? 303 PRO B CG  1 
ATOM   6062 C  CD  . PRO B 1 303 ? -15.184 33.796  35.737  1.00 23.76  ? 303 PRO B CD  1 
ATOM   6063 N  N   . SER B 1 304 ? -12.726 31.357  38.944  1.00 18.08  ? 304 SER B N   1 
ATOM   6064 C  CA  . SER B 1 304 ? -11.405 30.918  39.363  1.00 18.67  ? 304 SER B CA  1 
ATOM   6065 C  C   . SER B 1 304 ? -10.965 29.705  38.544  1.00 17.76  ? 304 SER B C   1 
ATOM   6066 O  O   . SER B 1 304 ? -11.764 29.012  37.931  1.00 16.37  ? 304 SER B O   1 
ATOM   6067 C  CB  . SER B 1 304 ? -11.398 30.580  40.837  1.00 17.37  ? 304 SER B CB  1 
ATOM   6068 O  OG  . SER B 1 304 ? -12.126 29.387  41.136  1.00 18.44  ? 304 SER B OG  1 
ATOM   6069 N  N   . TYR B 1 305 ? -9.668  29.418  38.570  1.00 17.99  ? 305 TYR B N   1 
ATOM   6070 C  CA  . TYR B 1 305 ? -9.135  28.253  37.894  1.00 18.40  ? 305 TYR B CA  1 
ATOM   6071 C  C   . TYR B 1 305 ? -9.821  26.987  38.437  1.00 18.52  ? 305 TYR B C   1 
ATOM   6072 O  O   . TYR B 1 305 ? -10.264 26.125  37.697  1.00 17.29  ? 305 TYR B O   1 
ATOM   6073 C  CB  . TYR B 1 305 ? -7.610  28.309  38.122  1.00 19.64  ? 305 TYR B CB  1 
ATOM   6074 C  CG  . TYR B 1 305 ? -6.906  27.149  37.464  1.00 19.35  ? 305 TYR B CG  1 
ATOM   6075 C  CD1 . TYR B 1 305 ? -6.494  27.236  36.150  1.00 18.38  ? 305 TYR B CD1 1 
ATOM   6076 C  CD2 . TYR B 1 305 ? -6.748  25.936  38.135  1.00 19.39  ? 305 TYR B CD2 1 
ATOM   6077 C  CE1 . TYR B 1 305 ? -5.900  26.162  35.527  1.00 19.08  ? 305 TYR B CE1 1 
ATOM   6078 C  CE2 . TYR B 1 305 ? -6.164  24.856  37.520  1.00 19.52  ? 305 TYR B CE2 1 
ATOM   6079 C  CZ  . TYR B 1 305 ? -5.750  24.971  36.208  1.00 21.73  ? 305 TYR B CZ  1 
ATOM   6080 O  OH  . TYR B 1 305 ? -5.162  23.912  35.586  1.00 27.34  ? 305 TYR B OH  1 
ATOM   6081 N  N   . LYS B 1 306 ? -9.906  26.884  39.759  1.00 19.69  ? 306 LYS B N   1 
ATOM   6082 C  CA  . LYS B 1 306 ? -10.475 25.724  40.429  1.00 21.53  ? 306 LYS B CA  1 
ATOM   6083 C  C   . LYS B 1 306 ? -11.962 25.574  40.063  1.00 18.55  ? 306 LYS B C   1 
ATOM   6084 O  O   . LYS B 1 306 ? -12.462 24.468  39.908  1.00 17.39  ? 306 LYS B O   1 
ATOM   6085 C  CB  . LYS B 1 306 ? -10.154 25.872  41.921  1.00 28.04  ? 306 LYS B CB  1 
ATOM   6086 C  CG  . LYS B 1 306 ? -10.993 25.101  42.931  1.00 37.59  ? 306 LYS B CG  1 
ATOM   6087 C  CD  . LYS B 1 306 ? -11.281 23.667  42.623  1.00 43.89  ? 306 LYS B CD  1 
ATOM   6088 C  CE  . LYS B 1 306 ? -10.073 22.858  42.200  1.00 54.41  ? 306 LYS B CE  1 
ATOM   6089 N  NZ  . LYS B 1 306 ? -10.502 21.626  41.492  1.00 61.03  ? 306 LYS B NZ  1 
ATOM   6090 N  N   . GLN B 1 307 ? -12.690 26.683  39.920  1.00 18.01  ? 307 GLN B N   1 
ATOM   6091 C  CA  . GLN B 1 307 ? -14.109 26.588  39.579  1.00 16.69  ? 307 GLN B CA  1 
ATOM   6092 C  C   . GLN B 1 307 ? -14.249 25.991  38.175  1.00 16.64  ? 307 GLN B C   1 
ATOM   6093 O  O   . GLN B 1 307 ? -15.056 25.093  37.934  1.00 16.75  ? 307 GLN B O   1 
ATOM   6094 C  CB  . GLN B 1 307 ? -14.739 27.975  39.683  1.00 16.99  ? 307 GLN B CB  1 
ATOM   6095 C  CG  . GLN B 1 307 ? -15.037 28.392  41.108  1.00 17.48  ? 307 GLN B CG  1 
ATOM   6096 C  CD  . GLN B 1 307 ? -15.389 29.857  41.175  1.00 17.89  ? 307 GLN B CD  1 
ATOM   6097 O  OE1 . GLN B 1 307 ? -15.210 30.606  40.221  1.00 17.65  ? 307 GLN B OE1 1 
ATOM   6098 N  NE2 . GLN B 1 307 ? -15.861 30.283  42.331  1.00 19.86  ? 307 GLN B NE2 1 
ATOM   6099 N  N   . VAL B 1 308 ? -13.358 26.388  37.274  1.00 15.12  ? 308 VAL B N   1 
ATOM   6100 C  CA  . VAL B 1 308 ? -13.388 25.898  35.900  1.00 17.13  ? 308 VAL B CA  1 
ATOM   6101 C  C   . VAL B 1 308 ? -13.132 24.382  35.875  1.00 18.64  ? 308 VAL B C   1 
ATOM   6102 O  O   . VAL B 1 308 ? -13.781 23.689  35.104  1.00 19.33  ? 308 VAL B O   1 
ATOM   6103 C  CB  . VAL B 1 308 ? -12.422 26.711  35.021  1.00 16.76  ? 308 VAL B CB  1 
ATOM   6104 C  CG1 . VAL B 1 308 ? -12.244 26.152  33.619  1.00 17.38  ? 308 VAL B CG1 1 
ATOM   6105 C  CG2 . VAL B 1 308 ? -12.872 28.176  34.980  1.00 15.39  ? 308 VAL B CG2 1 
ATOM   6106 N  N   . LYS B 1 309 ? -12.232 23.870  36.736  1.00 17.00  ? 309 LYS B N   1 
ATOM   6107 C  CA  . LYS B 1 309 ? -11.955 22.439  36.825  1.00 17.73  ? 309 LYS B CA  1 
ATOM   6108 C  C   . LYS B 1 309 ? -13.163 21.677  37.355  1.00 18.68  ? 309 LYS B C   1 
ATOM   6109 O  O   . LYS B 1 309 ? -13.297 20.492  37.065  1.00 18.66  ? 309 LYS B O   1 
ATOM   6110 C  CB  . LYS B 1 309 ? -10.693 22.215  37.656  1.00 19.83  ? 309 LYS B CB  1 
ATOM   6111 C  CG  . LYS B 1 309 ? -9.412  22.492  36.868  1.00 26.04  ? 309 LYS B CG  1 
ATOM   6112 C  CD  . LYS B 1 309 ? -8.814  21.218  36.256  1.00 31.36  ? 309 LYS B CD  1 
ATOM   6113 C  CE  . LYS B 1 309 ? -7.822  21.436  35.133  1.00 36.11  ? 309 LYS B CE  1 
ATOM   6114 N  NZ  . LYS B 1 309 ? -8.450  22.021  33.923  1.00 44.90  ? 309 LYS B NZ  1 
ATOM   6115 N  N   . GLN B 1 310 ? -14.095 22.379  38.008  1.00 17.50  ? 310 GLN B N   1 
ATOM   6116 C  CA  . GLN B 1 310 ? -15.262 21.764  38.608  1.00 19.09  ? 310 GLN B CA  1 
ATOM   6117 C  C   . GLN B 1 310 ? -16.456 21.753  37.655  1.00 17.78  ? 310 GLN B C   1 
ATOM   6118 O  O   . GLN B 1 310 ? -17.477 21.147  38.006  1.00 17.04  ? 310 GLN B O   1 
ATOM   6119 C  CB  . GLN B 1 310 ? -15.671 22.471  39.901  1.00 22.24  ? 310 GLN B CB  1 
ATOM   6120 C  CG  . GLN B 1 310 ? -14.656 22.320  41.032  1.00 27.04  ? 310 GLN B CG  1 
ATOM   6121 C  CD  . GLN B 1 310 ? -14.463 20.873  41.384  1.00 32.56  ? 310 GLN B CD  1 
ATOM   6122 O  OE1 . GLN B 1 310 ? -13.647 20.185  40.772  1.00 39.23  ? 310 GLN B OE1 1 
ATOM   6123 N  NE2 . GLN B 1 310 ? -15.262 20.379  42.321  1.00 41.23  ? 310 GLN B NE2 1 
ATOM   6124 N  N   . LEU B 1 311 ? -16.333 22.365  36.464  1.00 15.68  ? 311 LEU B N   1 
ATOM   6125 C  CA  . LEU B 1 311 ? -17.443 22.384  35.516  1.00 15.91  ? 311 LEU B CA  1 
ATOM   6126 C  C   . LEU B 1 311 ? -17.473 21.066  34.742  1.00 15.06  ? 311 LEU B C   1 
ATOM   6127 O  O   . LEU B 1 311 ? -17.214 20.998  33.537  1.00 14.71  ? 311 LEU B O   1 
ATOM   6128 C  CB  . LEU B 1 311 ? -17.302 23.616  34.605  1.00 16.36  ? 311 LEU B CB  1 
ATOM   6129 C  CG  . LEU B 1 311 ? -17.454 24.989  35.279  1.00 15.32  ? 311 LEU B CG  1 
ATOM   6130 C  CD1 . LEU B 1 311 ? -17.223 26.115  34.281  1.00 15.28  ? 311 LEU B CD1 1 
ATOM   6131 C  CD2 . LEU B 1 311 ? -18.821 25.140  35.926  1.00 15.49  ? 311 LEU B CD2 1 
ATOM   6132 N  N   . LYS B 1 312 ? -17.812 19.995  35.454  1.00 16.55  ? 312 LYS B N   1 
ATOM   6133 C  CA  . LYS B 1 312 ? -17.679 18.638  34.950  1.00 16.78  ? 312 LYS B CA  1 
ATOM   6134 C  C   . LYS B 1 312 ? -18.591 18.468  33.734  1.00 15.21  ? 312 LYS B C   1 
ATOM   6135 O  O   . LYS B 1 312 ? -18.159 18.005  32.692  1.00 12.59  ? 312 LYS B O   1 
ATOM   6136 C  CB  . LYS B 1 312 ? -18.050 17.669  36.064  1.00 19.85  ? 312 LYS B CB  1 
ATOM   6137 C  CG  . LYS B 1 312 ? -18.104 16.195  35.695  1.00 19.95  ? 312 LYS B CG  1 
ATOM   6138 C  CD  . LYS B 1 312 ? -18.228 15.335  36.937  1.00 25.09  ? 312 LYS B CD  1 
ATOM   6139 C  CE  . LYS B 1 312 ? -18.487 13.875  36.641  1.00 28.63  ? 312 LYS B CE  1 
ATOM   6140 N  NZ  . LYS B 1 312 ? -17.918 13.453  35.346  1.00 29.73  ? 312 LYS B NZ  1 
ATOM   6141 N  N   . TYR B 1 313 ? -19.854 18.886  33.853  1.00 16.66  ? 313 TYR B N   1 
ATOM   6142 C  CA  . TYR B 1 313 ? -20.816 18.653  32.784  1.00 15.75  ? 313 TYR B CA  1 
ATOM   6143 C  C   . TYR B 1 313 ? -20.500 19.541  31.581  1.00 15.51  ? 313 TYR B C   1 
ATOM   6144 O  O   . TYR B 1 313 ? -20.690 19.140  30.429  1.00 13.28  ? 313 TYR B O   1 
ATOM   6145 C  CB  . TYR B 1 313 ? -22.243 18.837  33.306  1.00 15.88  ? 313 TYR B CB  1 
ATOM   6146 C  CG  . TYR B 1 313 ? -23.295 18.312  32.352  1.00 16.49  ? 313 TYR B CG  1 
ATOM   6147 C  CD1 . TYR B 1 313 ? -23.516 16.952  32.196  1.00 17.59  ? 313 TYR B CD1 1 
ATOM   6148 C  CD2 . TYR B 1 313 ? -24.046 19.187  31.569  1.00 17.22  ? 313 TYR B CD2 1 
ATOM   6149 C  CE1 . TYR B 1 313 ? -24.479 16.486  31.318  1.00 17.44  ? 313 TYR B CE1 1 
ATOM   6150 C  CE2 . TYR B 1 313 ? -24.992 18.724  30.671  1.00 16.22  ? 313 TYR B CE2 1 
ATOM   6151 C  CZ  . TYR B 1 313 ? -25.225 17.371  30.563  1.00 17.58  ? 313 TYR B CZ  1 
ATOM   6152 O  OH  . TYR B 1 313 ? -26.168 16.958  29.683  1.00 18.50  ? 313 TYR B OH  1 
ATOM   6153 N  N   . VAL B 1 314 ? -20.087 20.785  31.824  1.00 14.81  ? 314 VAL B N   1 
ATOM   6154 C  CA  . VAL B 1 314 ? -19.618 21.610  30.715  1.00 14.74  ? 314 VAL B CA  1 
ATOM   6155 C  C   . VAL B 1 314 ? -18.520 20.875  29.937  1.00 13.74  ? 314 VAL B C   1 
ATOM   6156 O  O   . VAL B 1 314 ? -18.527 20.867  28.713  1.00 12.06  ? 314 VAL B O   1 
ATOM   6157 C  CB  . VAL B 1 314 ? -19.166 23.012  31.173  1.00 14.79  ? 314 VAL B CB  1 
ATOM   6158 C  CG1 . VAL B 1 314 ? -18.594 23.782  30.006  1.00 14.84  ? 314 VAL B CG1 1 
ATOM   6159 C  CG2 . VAL B 1 314 ? -20.301 23.776  31.823  1.00 15.60  ? 314 VAL B CG2 1 
ATOM   6160 N  N   . GLY B 1 315 ? -17.579 20.248  30.646  1.00 14.35  ? 315 GLY B N   1 
ATOM   6161 C  CA  . GLY B 1 315 ? -16.528 19.449  30.046  1.00 15.24  ? 315 GLY B CA  1 
ATOM   6162 C  C   . GLY B 1 315 ? -17.041 18.294  29.186  1.00 15.19  ? 315 GLY B C   1 
ATOM   6163 O  O   . GLY B 1 315 ? -16.517 18.074  28.098  1.00 13.49  ? 315 GLY B O   1 
ATOM   6164 N  N   . MET B 1 316 ? -18.078 17.619  29.682  1.00 15.84  ? 316 MET B N   1 
ATOM   6165 C  CA  . MET B 1 316 ? -18.740 16.519  28.976  1.00 16.61  ? 316 MET B CA  1 
ATOM   6166 C  C   . MET B 1 316 ? -19.398 17.027  27.691  1.00 14.75  ? 316 MET B C   1 
ATOM   6167 O  O   . MET B 1 316 ? -19.304 16.364  26.653  1.00 13.24  ? 316 MET B O   1 
ATOM   6168 C  CB  . MET B 1 316 ? -19.783 15.862  29.882  1.00 16.97  ? 316 MET B CB  1 
ATOM   6169 C  CG  . MET B 1 316 ? -19.183 14.995  30.998  1.00 17.22  ? 316 MET B CG  1 
ATOM   6170 S  SD  . MET B 1 316 ? -20.259 14.834  32.453  1.00 21.66  ? 316 MET B SD  1 
ATOM   6171 C  CE  . MET B 1 316 ? -21.575 13.806  31.808  1.00 22.19  ? 316 MET B CE  1 
ATOM   6172 N  N   . VAL B 1 317 ? -20.026 18.222  27.762  1.00 13.69  ? 317 VAL B N   1 
ATOM   6173 C  CA  . VAL B 1 317 ? -20.609 18.894  26.602  1.00 13.33  ? 317 VAL B CA  1 
ATOM   6174 C  C   . VAL B 1 317 ? -19.549 19.123  25.528  1.00 13.39  ? 317 VAL B C   1 
ATOM   6175 O  O   . VAL B 1 317 ? -19.813 18.994  24.335  1.00 14.43  ? 317 VAL B O   1 
ATOM   6176 C  CB  . VAL B 1 317 ? -21.326 20.230  26.986  1.00 13.58  ? 317 VAL B CB  1 
ATOM   6177 C  CG1 . VAL B 1 317 ? -21.755 20.975  25.747  1.00 13.05  ? 317 VAL B CG1 1 
ATOM   6178 C  CG2 . VAL B 1 317 ? -22.525 19.983  27.887  1.00 14.07  ? 317 VAL B CG2 1 
ATOM   6179 N  N   . LEU B 1 318 ? -18.352 19.565  25.942  1.00 13.42  ? 318 LEU B N   1 
ATOM   6180 C  CA  . LEU B 1 318 ? -17.298 19.912  25.014  1.00 12.82  ? 318 LEU B CA  1 
ATOM   6181 C  C   . LEU B 1 318 ? -16.776 18.611  24.396  1.00 12.19  ? 318 LEU B C   1 
ATOM   6182 O  O   . LEU B 1 318 ? -16.563 18.565  23.203  1.00 11.84  ? 318 LEU B O   1 
ATOM   6183 C  CB  . LEU B 1 318 ? -16.192 20.665  25.772  1.00 13.59  ? 318 LEU B CB  1 
ATOM   6184 C  CG  . LEU B 1 318 ? -16.552 22.106  26.125  1.00 14.15  ? 318 LEU B CG  1 
ATOM   6185 C  CD1 . LEU B 1 318 ? -15.518 22.712  27.082  1.00 14.00  ? 318 LEU B CD1 1 
ATOM   6186 C  CD2 . LEU B 1 318 ? -16.708 22.938  24.872  1.00 14.30  ? 318 LEU B CD2 1 
ATOM   6187 N  N   . ASN B 1 319 ? -16.623 17.550  25.183  1.00 13.68  ? 319 ASN B N   1 
ATOM   6188 C  CA  . ASN B 1 319 ? -16.175 16.261  24.651  1.00 14.67  ? 319 ASN B CA  1 
ATOM   6189 C  C   . ASN B 1 319 ? -17.162 15.709  23.617  1.00 13.71  ? 319 ASN B C   1 
ATOM   6190 O  O   . ASN B 1 319 ? -16.755 15.162  22.607  1.00 13.63  ? 319 ASN B O   1 
ATOM   6191 C  CB  . ASN B 1 319 ? -15.890 15.241  25.755  1.00 15.83  ? 319 ASN B CB  1 
ATOM   6192 C  CG  . ASN B 1 319 ? -14.518 15.469  26.364  1.00 19.34  ? 319 ASN B CG  1 
ATOM   6193 O  OD1 . ASN B 1 319 ? -13.579 15.847  25.661  1.00 20.05  ? 319 ASN B OD1 1 
ATOM   6194 N  ND2 . ASN B 1 319 ? -14.406 15.309  27.669  1.00 24.11  ? 319 ASN B ND2 1 
ATOM   6195 N  N   . GLU B 1 320 ? -18.455 15.835  23.886  1.00 14.59  ? 320 GLU B N   1 
ATOM   6196 C  CA  . GLU B 1 320 ? -19.485 15.277  23.019  1.00 14.58  ? 320 GLU B CA  1 
ATOM   6197 C  C   . GLU B 1 320 ? -19.607 16.081  21.728  1.00 15.53  ? 320 GLU B C   1 
ATOM   6198 O  O   . GLU B 1 320 ? -19.983 15.533  20.687  1.00 15.66  ? 320 GLU B O   1 
ATOM   6199 C  CB  . GLU B 1 320 ? -20.778 15.153  23.815  1.00 16.67  ? 320 GLU B CB  1 
ATOM   6200 C  CG  . GLU B 1 320 ? -21.955 14.582  23.043  1.00 16.65  ? 320 GLU B CG  1 
ATOM   6201 C  CD  . GLU B 1 320 ? -21.827 13.152  22.568  1.00 19.57  ? 320 GLU B CD  1 
ATOM   6202 O  OE1 . GLU B 1 320 ? -20.692 12.615  22.599  1.00 23.20  ? 320 GLU B OE1 1 
ATOM   6203 O  OE2 . GLU B 1 320 ? -22.885 12.538  22.186  1.00 16.44  ? 320 GLU B OE2 1 
ATOM   6204 N  N   . ALA B 1 321 ? -19.249 17.386  21.762  1.00 16.61  ? 321 ALA B N   1 
ATOM   6205 C  CA  . ALA B 1 321 ? -19.088 18.154  20.536  1.00 13.55  ? 321 ALA B CA  1 
ATOM   6206 C  C   . ALA B 1 321 ? -17.861 17.697  19.750  1.00 13.75  ? 321 ALA B C   1 
ATOM   6207 O  O   . ALA B 1 321 ? -17.907 17.650  18.513  1.00 12.48  ? 321 ALA B O   1 
ATOM   6208 C  CB  . ALA B 1 321 ? -19.058 19.627  20.836  1.00 14.50  ? 321 ALA B CB  1 
ATOM   6209 N  N   . LEU B 1 322 ? -16.760 17.314  20.422  1.00 13.25  ? 322 LEU B N   1 
ATOM   6210 C  CA  . LEU B 1 322 ? -15.584 16.820  19.732  1.00 12.27  ? 322 LEU B CA  1 
ATOM   6211 C  C   . LEU B 1 322 ? -15.815 15.390  19.225  1.00 12.70  ? 322 LEU B C   1 
ATOM   6212 O  O   . LEU B 1 322 ? -15.196 14.964  18.244  1.00 12.98  ? 322 LEU B O   1 
ATOM   6213 C  CB  . LEU B 1 322 ? -14.365 16.881  20.680  1.00 12.72  ? 322 LEU B CB  1 
ATOM   6214 C  CG  . LEU B 1 322 ? -13.786 18.274  20.962  1.00 13.48  ? 322 LEU B CG  1 
ATOM   6215 C  CD1 . LEU B 1 322 ? -12.741 18.194  22.047  1.00 13.86  ? 322 LEU B CD1 1 
ATOM   6216 C  CD2 . LEU B 1 322 ? -13.195 18.910  19.717  1.00 12.47  ? 322 LEU B CD2 1 
ATOM   6217 N  N   . ARG B 1 323 ? -16.716 14.647  19.866  1.00 11.67  ? 323 ARG B N   1 
ATOM   6218 C  CA  . ARG B 1 323 ? -17.040 13.335  19.344  1.00 12.52  ? 323 ARG B CA  1 
ATOM   6219 C  C   . ARG B 1 323 ? -17.668 13.532  17.969  1.00 12.50  ? 323 ARG B C   1 
ATOM   6220 O  O   . ARG B 1 323 ? -17.197 13.026  16.978  1.00 11.46  ? 323 ARG B O   1 
ATOM   6221 C  CB  . ARG B 1 323 ? -17.899 12.513  20.311  1.00 12.73  ? 323 ARG B CB  1 
ATOM   6222 C  CG  . ARG B 1 323 ? -18.000 11.043  19.906  1.00 13.90  ? 323 ARG B CG  1 
ATOM   6223 C  CD  . ARG B 1 323 ? -19.040 10.243  20.653  1.00 14.39  ? 323 ARG B CD  1 
ATOM   6224 N  NE  . ARG B 1 323 ? -20.393 10.778  20.564  1.00 15.08  ? 323 ARG B NE  1 
ATOM   6225 C  CZ  . ARG B 1 323 ? -21.235 10.607  19.569  1.00 14.80  ? 323 ARG B CZ  1 
ATOM   6226 N  NH1 . ARG B 1 323 ? -20.912 9.866   18.535  1.00 17.28  ? 323 ARG B NH1 1 
ATOM   6227 N  NH2 . ARG B 1 323 ? -22.434 11.150  19.637  1.00 14.44  ? 323 ARG B NH2 1 
ATOM   6228 N  N   . LEU B 1 324 ? -18.714 14.350  17.871  1.00 13.40  ? 324 LEU B N   1 
ATOM   6229 C  CA  . LEU B 1 324 ? -19.458 14.402  16.624  1.00 13.71  ? 324 LEU B CA  1 
ATOM   6230 C  C   . LEU B 1 324 ? -18.724 15.176  15.522  1.00 13.72  ? 324 LEU B C   1 
ATOM   6231 O  O   . LEU B 1 324 ? -18.625 14.719  14.364  1.00 12.83  ? 324 LEU B O   1 
ATOM   6232 C  CB  . LEU B 1 324 ? -20.840 14.950  16.952  1.00 16.57  ? 324 LEU B CB  1 
ATOM   6233 C  CG  . LEU B 1 324 ? -21.771 13.924  17.599  1.00 19.06  ? 324 LEU B CG  1 
ATOM   6234 C  CD1 . LEU B 1 324 ? -22.970 14.581  18.252  1.00 19.95  ? 324 LEU B CD1 1 
ATOM   6235 C  CD2 . LEU B 1 324 ? -22.221 12.907  16.554  1.00 20.30  ? 324 LEU B CD2 1 
ATOM   6236 N  N   . TRP B 1 325 ? -18.106 16.310  15.891  1.00 14.08  ? 325 TRP B N   1 
ATOM   6237 C  CA  . TRP B 1 325 ? -17.410 17.157  14.945  1.00 13.53  ? 325 TRP B CA  1 
ATOM   6238 C  C   . TRP B 1 325 ? -16.032 17.552  15.473  1.00 12.77  ? 325 TRP B C   1 
ATOM   6239 O  O   . TRP B 1 325 ? -15.762 18.710  15.762  1.00 12.33  ? 325 TRP B O   1 
ATOM   6240 C  CB  . TRP B 1 325 ? -18.296 18.351  14.578  1.00 14.27  ? 325 TRP B CB  1 
ATOM   6241 C  CG  . TRP B 1 325 ? -19.472 17.863  13.778  1.00 14.87  ? 325 TRP B CG  1 
ATOM   6242 C  CD1 . TRP B 1 325 ? -20.780 17.835  14.151  1.00 16.22  ? 325 TRP B CD1 1 
ATOM   6243 C  CD2 . TRP B 1 325 ? -19.410 17.241  12.472  1.00 16.70  ? 325 TRP B CD2 1 
ATOM   6244 N  NE1 . TRP B 1 325 ? -21.543 17.288  13.155  1.00 16.12  ? 325 TRP B NE1 1 
ATOM   6245 C  CE2 . TRP B 1 325 ? -20.737 16.921  12.115  1.00 18.05  ? 325 TRP B CE2 1 
ATOM   6246 C  CE3 . TRP B 1 325 ? -18.381 16.953  11.570  1.00 17.85  ? 325 TRP B CE3 1 
ATOM   6247 C  CZ2 . TRP B 1 325 ? -21.044 16.280  10.912  1.00 18.36  ? 325 TRP B CZ2 1 
ATOM   6248 C  CZ3 . TRP B 1 325 ? -18.688 16.342  10.377  1.00 20.67  ? 325 TRP B CZ3 1 
ATOM   6249 C  CH2 . TRP B 1 325 ? -20.003 16.012  10.057  1.00 18.68  ? 325 TRP B CH2 1 
ATOM   6250 N  N   . PRO B 1 326 ? -15.071 16.605  15.477  1.00 12.60  ? 326 PRO B N   1 
ATOM   6251 C  CA  . PRO B 1 326 ? -13.684 16.929  15.869  1.00 13.86  ? 326 PRO B CA  1 
ATOM   6252 C  C   . PRO B 1 326 ? -13.219 17.969  14.876  1.00 14.55  ? 326 PRO B C   1 
ATOM   6253 O  O   . PRO B 1 326 ? -13.305 17.714  13.685  1.00 17.05  ? 326 PRO B O   1 
ATOM   6254 C  CB  . PRO B 1 326 ? -12.951 15.593  15.760  1.00 13.59  ? 326 PRO B CB  1 
ATOM   6255 C  CG  . PRO B 1 326 ? -13.772 14.820  14.746  1.00 13.52  ? 326 PRO B CG  1 
ATOM   6256 C  CD  . PRO B 1 326 ? -15.208 15.256  14.957  1.00 13.45  ? 326 PRO B CD  1 
ATOM   6257 N  N   . THR B 1 327 ? -12.740 19.137  15.346  1.00 15.40  ? 327 THR B N   1 
ATOM   6258 C  CA  . THR B 1 327 ? -12.497 20.266  14.457  1.00 14.69  ? 327 THR B CA  1 
ATOM   6259 C  C   . THR B 1 327 ? -11.201 20.142  13.657  1.00 15.70  ? 327 THR B C   1 
ATOM   6260 O  O   . THR B 1 327 ? -11.089 20.798  12.619  1.00 17.42  ? 327 THR B O   1 
ATOM   6261 C  CB  . THR B 1 327 ? -12.619 21.566  15.239  1.00 14.80  ? 327 THR B CB  1 
ATOM   6262 O  OG1 . THR B 1 327 ? -11.835 21.442  16.433  1.00 14.76  ? 327 THR B OG1 1 
ATOM   6263 C  CG2 . THR B 1 327 ? -14.043 21.857  15.639  1.00 15.25  ? 327 THR B CG2 1 
ATOM   6264 N  N   . GLY B 1 328 ? -10.236 19.313  14.089  1.00 16.30  ? 328 GLY B N   1 
ATOM   6265 C  CA  . GLY B 1 328 ? -9.128  18.888  13.249  1.00 16.48  ? 328 GLY B CA  1 
ATOM   6266 C  C   . GLY B 1 328 ? -9.363  17.453  12.766  1.00 18.95  ? 328 GLY B C   1 
ATOM   6267 O  O   . GLY B 1 328 ? -9.002  16.496  13.452  1.00 21.92  ? 328 GLY B O   1 
ATOM   6268 N  N   . PRO B 1 329 ? -10.069 17.221  11.636  1.00 16.27  ? 329 PRO B N   1 
ATOM   6269 C  CA  . PRO B 1 329 ? -10.830 15.976  11.500  1.00 15.75  ? 329 PRO B CA  1 
ATOM   6270 C  C   . PRO B 1 329 ? -10.050 14.761  11.003  1.00 16.35  ? 329 PRO B C   1 
ATOM   6271 O  O   . PRO B 1 329 ? -10.586 13.660  10.956  1.00 14.98  ? 329 PRO B O   1 
ATOM   6272 C  CB  . PRO B 1 329 ? -11.921 16.371  10.507  1.00 16.30  ? 329 PRO B CB  1 
ATOM   6273 C  CG  . PRO B 1 329 ? -11.273 17.393  9.610   1.00 16.43  ? 329 PRO B CG  1 
ATOM   6274 C  CD  . PRO B 1 329 ? -10.300 18.144  10.516  1.00 18.05  ? 329 PRO B CD  1 
ATOM   6275 N  N   . ALA B 1 330 ? -8.762  14.947  10.715  1.00 16.00  ? 330 ALA B N   1 
ATOM   6276 C  CA  . ALA B 1 330 ? -7.997  13.851  10.155  1.00 18.13  ? 330 ALA B CA  1 
ATOM   6277 C  C   . ALA B 1 330 ? -6.555  13.995  10.597  1.00 17.44  ? 330 ALA B C   1 
ATOM   6278 O  O   . ALA B 1 330 ? -6.065  15.095  10.817  1.00 19.00  ? 330 ALA B O   1 
ATOM   6279 C  CB  . ALA B 1 330 ? -8.149  13.843  8.650   1.00 17.84  ? 330 ALA B CB  1 
ATOM   6280 N  N   . PHE B 1 331 ? -5.870  12.871  10.737  1.00 17.54  ? 331 PHE B N   1 
ATOM   6281 C  CA  . PHE B 1 331 ? -4.423  12.926  10.839  1.00 16.45  ? 331 PHE B CA  1 
ATOM   6282 C  C   . PHE B 1 331 ? -3.869  11.741  10.078  1.00 16.54  ? 331 PHE B C   1 
ATOM   6283 O  O   . PHE B 1 331 ? -4.594  10.794  9.774   1.00 16.06  ? 331 PHE B O   1 
ATOM   6284 C  CB  . PHE B 1 331 ? -3.995  13.007  12.303  1.00 16.59  ? 331 PHE B CB  1 
ATOM   6285 C  CG  . PHE B 1 331 ? -4.347  11.860  13.192  1.00 15.94  ? 331 PHE B CG  1 
ATOM   6286 C  CD1 . PHE B 1 331 ? -3.529  10.742  13.284  1.00 18.46  ? 331 PHE B CD1 1 
ATOM   6287 C  CD2 . PHE B 1 331 ? -5.474  11.909  13.987  1.00 16.27  ? 331 PHE B CD2 1 
ATOM   6288 C  CE1 . PHE B 1 331 ? -3.861  9.688   14.127  1.00 18.18  ? 331 PHE B CE1 1 
ATOM   6289 C  CE2 . PHE B 1 331 ? -5.797  10.864  14.831  1.00 15.78  ? 331 PHE B CE2 1 
ATOM   6290 C  CZ  . PHE B 1 331 ? -4.983  9.756   14.915  1.00 17.65  ? 331 PHE B CZ  1 
ATOM   6291 N  N   . SER B 1 332 ? -2.595  11.863  9.710   1.00 14.88  ? 332 SER B N   1 
ATOM   6292 C  CA  . SER B 1 332 ? -1.996  11.007  8.709   1.00 16.08  ? 332 SER B CA  1 
ATOM   6293 C  C   . SER B 1 332 ? -0.844  10.276  9.372   1.00 14.64  ? 332 SER B C   1 
ATOM   6294 O  O   . SER B 1 332 ? -0.111  10.886  10.138  1.00 14.18  ? 332 SER B O   1 
ATOM   6295 C  CB  . SER B 1 332 ? -1.542  11.784  7.502   1.00 17.39  ? 332 SER B CB  1 
ATOM   6296 O  OG  . SER B 1 332 ? -1.015  10.918  6.502   1.00 18.97  ? 332 SER B OG  1 
ATOM   6297 N  N   . LEU B 1 333 ? -0.669  9.002   8.996   1.00 16.66  ? 333 LEU B N   1 
ATOM   6298 C  CA  . LEU B 1 333 ? 0.404   8.149   9.489   1.00 16.19  ? 333 LEU B CA  1 
ATOM   6299 C  C   . LEU B 1 333 ? 1.130   7.476   8.331   1.00 14.34  ? 333 LEU B C   1 
ATOM   6300 O  O   . LEU B 1 333 ? 0.599   7.387   7.238   1.00 13.92  ? 333 LEU B O   1 
ATOM   6301 C  CB  . LEU B 1 333 ? -0.211  7.092   10.390  1.00 17.87  ? 333 LEU B CB  1 
ATOM   6302 C  CG  . LEU B 1 333 ? -0.909  7.629   11.626  1.00 22.35  ? 333 LEU B CG  1 
ATOM   6303 C  CD1 . LEU B 1 333 ? -1.767  6.541   12.253  1.00 23.50  ? 333 LEU B CD1 1 
ATOM   6304 C  CD2 . LEU B 1 333 ? 0.107   8.175   12.628  1.00 21.41  ? 333 LEU B CD2 1 
ATOM   6305 N  N   . TYR B 1 334 ? 2.320   6.938   8.609   1.00 14.72  ? 334 TYR B N   1 
ATOM   6306 C  CA  . TYR B 1 334 ? 3.024   6.088   7.656   1.00 14.79  ? 334 TYR B CA  1 
ATOM   6307 C  C   . TYR B 1 334 ? 3.598   4.879   8.393   1.00 16.37  ? 334 TYR B C   1 
ATOM   6308 O  O   . TYR B 1 334 ? 3.886   4.958   9.585   1.00 13.62  ? 334 TYR B O   1 
ATOM   6309 C  CB  . TYR B 1 334 ? 4.076   6.873   6.869   1.00 15.42  ? 334 TYR B CB  1 
ATOM   6310 C  CG  . TYR B 1 334 ? 5.324   7.224   7.660   1.00 17.40  ? 334 TYR B CG  1 
ATOM   6311 C  CD1 . TYR B 1 334 ? 6.389   6.342   7.733   1.00 19.45  ? 334 TYR B CD1 1 
ATOM   6312 C  CD2 . TYR B 1 334 ? 5.433   8.421   8.366   1.00 19.60  ? 334 TYR B CD2 1 
ATOM   6313 C  CE1 . TYR B 1 334 ? 7.512   6.627   8.504   1.00 20.63  ? 334 TYR B CE1 1 
ATOM   6314 C  CE2 . TYR B 1 334 ? 6.580   8.742   9.087   1.00 19.54  ? 334 TYR B CE2 1 
ATOM   6315 C  CZ  . TYR B 1 334 ? 7.616   7.836   9.172   1.00 19.65  ? 334 TYR B CZ  1 
ATOM   6316 O  OH  . TYR B 1 334 ? 8.757   8.131   9.883   1.00 21.41  ? 334 TYR B OH  1 
ATOM   6317 N  N   . ALA B 1 335 ? 3.753   3.752   7.653   1.00 16.70  ? 335 ALA B N   1 
ATOM   6318 C  CA  . ALA B 1 335 ? 4.253   2.498   8.191   1.00 16.68  ? 335 ALA B CA  1 
ATOM   6319 C  C   . ALA B 1 335 ? 5.772   2.562   8.387   1.00 17.38  ? 335 ALA B C   1 
ATOM   6320 O  O   . ALA B 1 335 ? 6.510   2.808   7.440   1.00 15.15  ? 335 ALA B O   1 
ATOM   6321 C  CB  . ALA B 1 335 ? 3.882   1.357   7.272   1.00 16.34  ? 335 ALA B CB  1 
ATOM   6322 N  N   . LYS B 1 336 ? 6.238   2.320   9.619   1.00 17.21  ? 336 LYS B N   1 
ATOM   6323 C  CA  . LYS B 1 336 ? 7.671   2.409   9.888   1.00 21.43  ? 336 LYS B CA  1 
ATOM   6324 C  C   . LYS B 1 336 ? 8.388   1.238   9.225   1.00 22.40  ? 336 LYS B C   1 
ATOM   6325 O  O   . LYS B 1 336 ? 9.536   1.391   8.799   1.00 22.43  ? 336 LYS B O   1 
ATOM   6326 C  CB  . LYS B 1 336 ? 7.941   2.481   11.390  1.00 20.40  ? 336 LYS B CB  1 
ATOM   6327 C  CG  . LYS B 1 336 ? 7.597   3.832   11.989  1.00 21.29  ? 336 LYS B CG  1 
ATOM   6328 C  CD  . LYS B 1 336 ? 7.417   3.817   13.499  1.00 23.10  ? 336 LYS B CD  1 
ATOM   6329 C  CE  . LYS B 1 336 ? 8.688   3.562   14.270  1.00 25.66  ? 336 LYS B CE  1 
ATOM   6330 N  NZ  . LYS B 1 336 ? 9.589   4.730   14.174  1.00 29.46  ? 336 LYS B NZ  1 
ATOM   6331 N  N   . GLU B 1 337 ? 7.702   0.082   9.188   1.00 21.67  ? 337 GLU B N   1 
ATOM   6332 C  CA  . GLU B 1 337 ? 8.224   -1.124  8.571   1.00 24.69  ? 337 GLU B CA  1 
ATOM   6333 C  C   . GLU B 1 337 ? 7.065   -1.876  7.914   1.00 27.97  ? 337 GLU B C   1 
ATOM   6334 O  O   . GLU B 1 337 ? 5.889   -1.567  8.164   1.00 23.72  ? 337 GLU B O   1 
ATOM   6335 C  CB  . GLU B 1 337 ? 8.879   -2.046  9.605   1.00 26.50  ? 337 GLU B CB  1 
ATOM   6336 C  CG  . GLU B 1 337 ? 10.036  -1.442  10.381  1.00 30.06  ? 337 GLU B CG  1 
ATOM   6337 C  CD  . GLU B 1 337 ? 11.343  -1.191  9.641   1.00 33.02  ? 337 GLU B CD  1 
ATOM   6338 O  OE1 . GLU B 1 337 ? 11.459  -1.551  8.462   1.00 37.19  ? 337 GLU B OE1 1 
ATOM   6339 O  OE2 . GLU B 1 337 ? 12.249  -0.597  10.256  1.00 34.64  ? 337 GLU B OE2 1 
ATOM   6340 N  N   . ASP B 1 338 ? 7.407   -2.898  7.109   1.00 27.12  ? 338 ASP B N   1 
ATOM   6341 C  CA  . ASP B 1 338 ? 6.398   -3.786  6.549   1.00 29.66  ? 338 ASP B CA  1 
ATOM   6342 C  C   . ASP B 1 338 ? 5.542   -4.331  7.684   1.00 29.10  ? 338 ASP B C   1 
ATOM   6343 O  O   . ASP B 1 338 ? 6.059   -4.698  8.750   1.00 26.90  ? 338 ASP B O   1 
ATOM   6344 C  CB  . ASP B 1 338 ? 6.984   -4.959  5.754   1.00 33.23  ? 338 ASP B CB  1 
ATOM   6345 C  CG  . ASP B 1 338 ? 7.804   -4.561  4.542   1.00 32.63  ? 338 ASP B CG  1 
ATOM   6346 O  OD1 . ASP B 1 338 ? 7.584   -3.454  4.012   1.00 35.35  ? 338 ASP B OD1 1 
ATOM   6347 O  OD2 . ASP B 1 338 ? 8.689   -5.341  4.166   1.00 38.27  ? 338 ASP B OD2 1 
ATOM   6348 N  N   . THR B 1 339 ? 4.221   -4.337  7.461   1.00 25.66  ? 339 THR B N   1 
ATOM   6349 C  CA  . THR B 1 339 ? 3.319   -4.731  8.519   1.00 28.10  ? 339 THR B CA  1 
ATOM   6350 C  C   . THR B 1 339 ? 2.000   -5.180  7.902   1.00 25.71  ? 339 THR B C   1 
ATOM   6351 O  O   . THR B 1 339 ? 1.711   -4.940  6.742   1.00 24.32  ? 339 THR B O   1 
ATOM   6352 C  CB  . THR B 1 339 ? 3.272   -3.628  9.599   1.00 31.33  ? 339 THR B CB  1 
ATOM   6353 O  OG1 . THR B 1 339 ? 2.771   -4.192  10.814  1.00 33.92  ? 339 THR B OG1 1 
ATOM   6354 C  CG2 . THR B 1 339 ? 2.466   -2.403  9.207   1.00 31.10  ? 339 THR B CG2 1 
ATOM   6355 N  N   . VAL B 1 340 ? 1.222   -5.868  8.712   1.00 25.64  ? 340 VAL B N   1 
ATOM   6356 C  CA  . VAL B 1 340 ? -0.093  -6.311  8.315   1.00 27.75  ? 340 VAL B CA  1 
ATOM   6357 C  C   . VAL B 1 340 ? -1.090  -5.606  9.223   1.00 26.14  ? 340 VAL B C   1 
ATOM   6358 O  O   . VAL B 1 340 ? -0.959  -5.607  10.443  1.00 26.91  ? 340 VAL B O   1 
ATOM   6359 C  CB  . VAL B 1 340 ? -0.221  -7.848  8.384   1.00 26.02  ? 340 VAL B CB  1 
ATOM   6360 C  CG1 . VAL B 1 340 ? -1.620  -8.297  7.976   1.00 25.35  ? 340 VAL B CG1 1 
ATOM   6361 C  CG2 . VAL B 1 340 ? 0.834   -8.547  7.534   1.00 24.24  ? 340 VAL B CG2 1 
ATOM   6362 N  N   . LEU B 1 341 ? -2.120  -5.036  8.622   1.00 26.53  ? 341 LEU B N   1 
ATOM   6363 C  CA  . LEU B 1 341 ? -3.068  -4.251  9.381   1.00 27.35  ? 341 LEU B CA  1 
ATOM   6364 C  C   . LEU B 1 341 ? -4.339  -5.077  9.598   1.00 26.46  ? 341 LEU B C   1 
ATOM   6365 O  O   . LEU B 1 341 ? -4.979  -5.550  8.666   1.00 27.64  ? 341 LEU B O   1 
ATOM   6366 C  CB  . LEU B 1 341 ? -3.289  -2.939  8.611   1.00 25.68  ? 341 LEU B CB  1 
ATOM   6367 C  CG  . LEU B 1 341 ? -4.152  -1.901  9.327   1.00 26.86  ? 341 LEU B CG  1 
ATOM   6368 C  CD1 . LEU B 1 341 ? -3.379  -1.277  10.483  1.00 28.76  ? 341 LEU B CD1 1 
ATOM   6369 C  CD2 . LEU B 1 341 ? -4.635  -0.842  8.351   1.00 26.61  ? 341 LEU B CD2 1 
ATOM   6370 N  N   . GLY B 1 342 ? -4.659  -5.336  10.859  1.00 25.54  ? 342 GLY B N   1 
ATOM   6371 C  CA  . GLY B 1 342 ? -5.895  -6.005  11.187  1.00 28.44  ? 342 GLY B CA  1 
ATOM   6372 C  C   . GLY B 1 342 ? -5.903  -7.454  10.712  1.00 30.16  ? 342 GLY B C   1 
ATOM   6373 O  O   . GLY B 1 342 ? -6.969  -8.025  10.519  1.00 30.73  ? 342 GLY B O   1 
ATOM   6374 N  N   . GLY B 1 343 ? -4.708  -8.030  10.547  1.00 30.07  ? 343 GLY B N   1 
ATOM   6375 C  CA  . GLY B 1 343 ? -4.537  -9.400  10.098  1.00 32.21  ? 343 GLY B CA  1 
ATOM   6376 C  C   . GLY B 1 343 ? -5.060  -9.654  8.682   1.00 35.26  ? 343 GLY B C   1 
ATOM   6377 O  O   . GLY B 1 343 ? -5.146  -10.806 8.262   1.00 37.77  ? 343 GLY B O   1 
ATOM   6378 N  N   . GLU B 1 344 ? -5.392  -8.589  7.948   1.00 34.56  ? 344 GLU B N   1 
ATOM   6379 C  CA  . GLU B 1 344 ? -6.058  -8.719  6.660   1.00 37.40  ? 344 GLU B CA  1 
ATOM   6380 C  C   . GLU B 1 344 ? -5.314  -7.920  5.595   1.00 33.66  ? 344 GLU B C   1 
ATOM   6381 O  O   . GLU B 1 344 ? -5.214  -8.382  4.466   1.00 34.19  ? 344 GLU B O   1 
ATOM   6382 C  CB  . GLU B 1 344 ? -7.516  -8.251  6.756   1.00 43.81  ? 344 GLU B CB  1 
ATOM   6383 C  CG  . GLU B 1 344 ? -8.357  -9.061  7.732   1.00 51.98  ? 344 GLU B CG  1 
ATOM   6384 C  CD  . GLU B 1 344 ? -9.759  -8.538  8.036   1.00 64.17  ? 344 GLU B CD  1 
ATOM   6385 O  OE1 . GLU B 1 344 ? -10.502 -9.231  8.781   1.00 66.33  ? 344 GLU B OE1 1 
ATOM   6386 O  OE2 . GLU B 1 344 ? -10.125 -7.453  7.528   1.00 61.23  ? 344 GLU B OE2 1 
ATOM   6387 N  N   . TYR B 1 345 ? -4.778  -6.735  5.943   1.00 30.96  ? 345 TYR B N   1 
ATOM   6388 C  CA  . TYR B 1 345 ? -4.283  -5.795  4.941   1.00 28.52  ? 345 TYR B CA  1 
ATOM   6389 C  C   . TYR B 1 345 ? -2.783  -5.600  5.075   1.00 29.37  ? 345 TYR B C   1 
ATOM   6390 O  O   . TYR B 1 345 ? -2.355  -4.871  5.967   1.00 29.54  ? 345 TYR B O   1 
ATOM   6391 C  CB  . TYR B 1 345 ? -4.978  -4.447  5.115   1.00 28.12  ? 345 TYR B CB  1 
ATOM   6392 C  CG  . TYR B 1 345 ? -6.487  -4.578  5.048   1.00 28.45  ? 345 TYR B CG  1 
ATOM   6393 C  CD1 . TYR B 1 345 ? -7.118  -4.846  3.845   1.00 30.38  ? 345 TYR B CD1 1 
ATOM   6394 C  CD2 . TYR B 1 345 ? -7.264  -4.518  6.193   1.00 30.25  ? 345 TYR B CD2 1 
ATOM   6395 C  CE1 . TYR B 1 345 ? -8.492  -4.969  3.769   1.00 29.82  ? 345 TYR B CE1 1 
ATOM   6396 C  CE2 . TYR B 1 345 ? -8.638  -4.681  6.137   1.00 33.75  ? 345 TYR B CE2 1 
ATOM   6397 C  CZ  . TYR B 1 345 ? -9.253  -4.904  4.918   1.00 33.85  ? 345 TYR B CZ  1 
ATOM   6398 O  OH  . TYR B 1 345 ? -10.611 -5.049  4.848   1.00 43.03  ? 345 TYR B OH  1 
ATOM   6399 N  N   . PRO B 1 346 ? -1.947  -6.217  4.202   1.00 27.88  ? 346 PRO B N   1 
ATOM   6400 C  CA  . PRO B 1 346 ? -0.499  -6.014  4.258   1.00 27.55  ? 346 PRO B CA  1 
ATOM   6401 C  C   . PRO B 1 346 ? -0.119  -4.607  3.806   1.00 27.37  ? 346 PRO B C   1 
ATOM   6402 O  O   . PRO B 1 346 ? -0.707  -4.067  2.876   1.00 26.54  ? 346 PRO B O   1 
ATOM   6403 C  CB  . PRO B 1 346 ? 0.101   -7.061  3.316   1.00 28.51  ? 346 PRO B CB  1 
ATOM   6404 C  CG  . PRO B 1 346 ? -1.059  -7.484  2.417   1.00 29.70  ? 346 PRO B CG  1 
ATOM   6405 C  CD  . PRO B 1 346 ? -2.349  -7.151  3.135   1.00 29.62  ? 346 PRO B CD  1 
ATOM   6406 N  N   . LEU B 1 347 ? 0.856   -4.015  4.503   1.00 29.19  ? 347 LEU B N   1 
ATOM   6407 C  CA  . LEU B 1 347 ? 1.370   -2.695  4.194   1.00 28.81  ? 347 LEU B CA  1 
ATOM   6408 C  C   . LEU B 1 347 ? 2.877   -2.800  4.031   1.00 27.97  ? 347 LEU B C   1 
ATOM   6409 O  O   . LEU B 1 347 ? 3.522   -3.581  4.720   1.00 28.36  ? 347 LEU B O   1 
ATOM   6410 C  CB  . LEU B 1 347 ? 1.055   -1.723  5.335   1.00 29.26  ? 347 LEU B CB  1 
ATOM   6411 C  CG  . LEU B 1 347 ? -0.417  -1.435  5.622   1.00 30.73  ? 347 LEU B CG  1 
ATOM   6412 C  CD1 . LEU B 1 347 ? -0.529  -0.388  6.728   1.00 29.58  ? 347 LEU B CD1 1 
ATOM   6413 C  CD2 . LEU B 1 347 ? -1.165  -0.972  4.373   1.00 29.16  ? 347 LEU B CD2 1 
ATOM   6414 N  N   . GLU B 1 348 ? 3.417   -1.993  3.122   1.00 28.59  ? 348 GLU B N   1 
ATOM   6415 C  CA  . GLU B 1 348 ? 4.853   -1.852  2.989   1.00 31.74  ? 348 GLU B CA  1 
ATOM   6416 C  C   . GLU B 1 348 ? 5.350   -0.588  3.707   1.00 28.28  ? 348 GLU B C   1 
ATOM   6417 O  O   . GLU B 1 348 ? 4.644   0.405   3.831   1.00 25.87  ? 348 GLU B O   1 
ATOM   6418 C  CB  . GLU B 1 348 ? 5.211   -1.796  1.511   1.00 36.56  ? 348 GLU B CB  1 
ATOM   6419 C  CG  . GLU B 1 348 ? 4.908   -3.064  0.741   1.00 41.11  ? 348 GLU B CG  1 
ATOM   6420 C  CD  . GLU B 1 348 ? 5.487   -2.991  -0.663  1.00 43.86  ? 348 GLU B CD  1 
ATOM   6421 O  OE1 . GLU B 1 348 ? 6.725   -3.121  -0.804  1.00 45.63  ? 348 GLU B OE1 1 
ATOM   6422 O  OE2 . GLU B 1 348 ? 4.715   -2.725  -1.596  1.00 47.24  ? 348 GLU B OE2 1 
ATOM   6423 N  N   . LYS B 1 349 ? 6.601   -0.640  4.176   1.00 24.61  ? 349 LYS B N   1 
ATOM   6424 C  CA  . LYS B 1 349 ? 7.288   0.500   4.758   1.00 25.50  ? 349 LYS B CA  1 
ATOM   6425 C  C   . LYS B 1 349 ? 7.029   1.725   3.899   1.00 24.90  ? 349 LYS B C   1 
ATOM   6426 O  O   . LYS B 1 349 ? 7.184   1.695   2.690   1.00 24.04  ? 349 LYS B O   1 
ATOM   6427 C  CB  . LYS B 1 349 ? 8.793   0.232   4.844   1.00 26.80  ? 349 LYS B CB  1 
ATOM   6428 C  CG  . LYS B 1 349 ? 9.618   1.324   5.504   1.00 30.04  ? 349 LYS B CG  1 
ATOM   6429 C  CD  . LYS B 1 349 ? 11.060  0.915   5.732   1.00 33.44  ? 349 LYS B CD  1 
ATOM   6430 C  CE  . LYS B 1 349 ? 11.791  1.744   6.767   1.00 37.48  ? 349 LYS B CE  1 
ATOM   6431 N  NZ  . LYS B 1 349 ? 12.396  2.990   6.231   1.00 40.05  ? 349 LYS B NZ  1 
ATOM   6432 N  N   . GLY B 1 350 ? 6.612   2.810   4.525   1.00 22.76  ? 350 GLY B N   1 
ATOM   6433 C  CA  . GLY B 1 350 ? 6.305   4.005   3.763   1.00 21.38  ? 350 GLY B CA  1 
ATOM   6434 C  C   . GLY B 1 350 ? 4.811   4.180   3.463   1.00 18.66  ? 350 GLY B C   1 
ATOM   6435 O  O   . GLY B 1 350 ? 4.410   5.305   3.212   1.00 17.01  ? 350 GLY B O   1 
ATOM   6436 N  N   . ASP B 1 351 ? 3.995   3.109   3.526   1.00 19.01  ? 351 ASP B N   1 
ATOM   6437 C  CA  . ASP B 1 351 ? 2.591   3.195   3.146   1.00 21.24  ? 351 ASP B CA  1 
ATOM   6438 C  C   . ASP B 1 351 ? 1.826   4.155   4.074   1.00 20.76  ? 351 ASP B C   1 
ATOM   6439 O  O   . ASP B 1 351 ? 1.949   4.093   5.306   1.00 19.43  ? 351 ASP B O   1 
ATOM   6440 C  CB  . ASP B 1 351 ? 1.908   1.821   3.141   1.00 22.62  ? 351 ASP B CB  1 
ATOM   6441 C  CG  . ASP B 1 351 ? 2.157   0.945   1.907   1.00 28.15  ? 351 ASP B CG  1 
ATOM   6442 O  OD1 . ASP B 1 351 ? 2.809   1.426   0.936   1.00 28.40  ? 351 ASP B OD1 1 
ATOM   6443 O  OD2 . ASP B 1 351 ? 1.726   -0.245  1.935   1.00 30.28  ? 351 ASP B OD2 1 
ATOM   6444 N  N   . GLU B 1 352 ? 0.958   4.985   3.483   1.00 21.15  ? 352 GLU B N   1 
ATOM   6445 C  CA  . GLU B 1 352 ? 0.260   6.010   4.245   1.00 23.68  ? 352 GLU B CA  1 
ATOM   6446 C  C   . GLU B 1 352 ? -1.123  5.562   4.687   1.00 22.92  ? 352 GLU B C   1 
ATOM   6447 O  O   . GLU B 1 352 ? -1.842  4.899   3.947   1.00 19.95  ? 352 GLU B O   1 
ATOM   6448 C  CB  . GLU B 1 352 ? 0.129   7.294   3.430   1.00 29.60  ? 352 GLU B CB  1 
ATOM   6449 C  CG  . GLU B 1 352 ? 1.475   7.818   2.999   1.00 34.21  ? 352 GLU B CG  1 
ATOM   6450 C  CD  . GLU B 1 352 ? 1.496   9.189   2.344   1.00 39.83  ? 352 GLU B CD  1 
ATOM   6451 O  OE1 . GLU B 1 352 ? 0.468   9.915   2.397   1.00 42.03  ? 352 GLU B OE1 1 
ATOM   6452 O  OE2 . GLU B 1 352 ? 2.553   9.519   1.762   1.00 46.45  ? 352 GLU B OE2 1 
ATOM   6453 N  N   . LEU B 1 353 ? -1.498  6.005   5.894   1.00 21.10  ? 353 LEU B N   1 
ATOM   6454 C  CA  . LEU B 1 353 ? -2.840  5.874   6.445   1.00 20.27  ? 353 LEU B CA  1 
ATOM   6455 C  C   . LEU B 1 353 ? -3.405  7.273   6.708   1.00 19.16  ? 353 LEU B C   1 
ATOM   6456 O  O   . LEU B 1 353 ? -2.639  8.200   6.973   1.00 19.47  ? 353 LEU B O   1 
ATOM   6457 C  CB  . LEU B 1 353 ? -2.768  5.079   7.756   1.00 20.22  ? 353 LEU B CB  1 
ATOM   6458 C  CG  . LEU B 1 353 ? -2.220  3.653   7.634   1.00 20.02  ? 353 LEU B CG  1 
ATOM   6459 C  CD1 . LEU B 1 353 ? -2.112  2.995   8.986   1.00 19.73  ? 353 LEU B CD1 1 
ATOM   6460 C  CD2 . LEU B 1 353 ? -3.112  2.814   6.740   1.00 22.50  ? 353 LEU B CD2 1 
ATOM   6461 N  N   . MET B 1 354 ? -4.736  7.401   6.633   1.00 18.09  ? 354 MET B N   1 
ATOM   6462 C  CA  . MET B 1 354 ? -5.447  8.582   7.098   1.00 18.11  ? 354 MET B CA  1 
ATOM   6463 C  C   . MET B 1 354 ? -6.489  8.137   8.104   1.00 17.20  ? 354 MET B C   1 
ATOM   6464 O  O   . MET B 1 354 ? -7.355  7.359   7.755   1.00 18.06  ? 354 MET B O   1 
ATOM   6465 C  CB  . MET B 1 354 ? -6.210  9.290   5.970   1.00 22.11  ? 354 MET B CB  1 
ATOM   6466 C  CG  . MET B 1 354 ? -5.342  10.002  4.948   1.00 26.22  ? 354 MET B CG  1 
ATOM   6467 S  SD  . MET B 1 354 ? -4.341  11.384  5.623   1.00 33.81  ? 354 MET B SD  1 
ATOM   6468 C  CE  . MET B 1 354 ? -5.473  12.092  6.807   1.00 23.27  ? 354 MET B CE  1 
ATOM   6469 N  N   . VAL B 1 355 ? -6.467  8.697   9.320   1.00 14.93  ? 355 VAL B N   1 
ATOM   6470 C  CA  . VAL B 1 355 ? -7.490  8.433   10.303  1.00 16.11  ? 355 VAL B CA  1 
ATOM   6471 C  C   . VAL B 1 355 ? -8.608  9.445   10.109  1.00 16.77  ? 355 VAL B C   1 
ATOM   6472 O  O   . VAL B 1 355 ? -8.365  10.656  10.198  1.00 16.06  ? 355 VAL B O   1 
ATOM   6473 C  CB  . VAL B 1 355 ? -6.936  8.552   11.729  1.00 16.36  ? 355 VAL B CB  1 
ATOM   6474 C  CG1 . VAL B 1 355 ? -8.033  8.352   12.747  1.00 17.79  ? 355 VAL B CG1 1 
ATOM   6475 C  CG2 . VAL B 1 355 ? -5.778  7.585   11.909  1.00 16.68  ? 355 VAL B CG2 1 
ATOM   6476 N  N   . LEU B 1 356 ? -9.810  8.926   9.843   1.00 15.57  ? 356 LEU B N   1 
ATOM   6477 C  CA  . LEU B 1 356 ? -10.946 9.800   9.629   1.00 18.42  ? 356 LEU B CA  1 
ATOM   6478 C  C   . LEU B 1 356 ? -11.683 9.902   10.960  1.00 16.71  ? 356 LEU B C   1 
ATOM   6479 O  O   . LEU B 1 356 ? -12.461 9.017   11.300  1.00 16.60  ? 356 LEU B O   1 
ATOM   6480 C  CB  . LEU B 1 356 ? -11.762 9.171   8.489   1.00 21.61  ? 356 LEU B CB  1 
ATOM   6481 C  CG  . LEU B 1 356 ? -12.815 10.027  7.791   1.00 25.48  ? 356 LEU B CG  1 
ATOM   6482 C  CD1 . LEU B 1 356 ? -12.235 11.325  7.230   1.00 28.61  ? 356 LEU B CD1 1 
ATOM   6483 C  CD2 . LEU B 1 356 ? -13.431 9.208   6.677   1.00 26.43  ? 356 LEU B CD2 1 
ATOM   6484 N  N   . ILE B 1 357 ? -11.355 10.946  11.733  1.00 15.03  ? 357 ILE B N   1 
ATOM   6485 C  CA  . ILE B 1 357 ? -11.713 10.997  13.139  1.00 14.17  ? 357 ILE B CA  1 
ATOM   6486 C  C   . ILE B 1 357 ? -13.240 11.035  13.261  1.00 13.75  ? 357 ILE B C   1 
ATOM   6487 O  O   . ILE B 1 357 ? -13.780 10.376  14.156  1.00 12.79  ? 357 ILE B O   1 
ATOM   6488 C  CB  . ILE B 1 357 ? -11.035 12.187  13.875  1.00 14.84  ? 357 ILE B CB  1 
ATOM   6489 C  CG1 . ILE B 1 357 ? -9.509  12.206  13.750  1.00 14.29  ? 357 ILE B CG1 1 
ATOM   6490 C  CG2 . ILE B 1 357 ? -11.455 12.174  15.330  1.00 14.86  ? 357 ILE B CG2 1 
ATOM   6491 C  CD1 . ILE B 1 357 ? -8.841  13.431  14.390  1.00 14.69  ? 357 ILE B CD1 1 
ATOM   6492 N  N   . PRO B 1 358 ? -13.995 11.833  12.463  1.00 12.94  ? 358 PRO B N   1 
ATOM   6493 C  CA  . PRO B 1 358 ? -15.452 11.847  12.620  1.00 14.79  ? 358 PRO B CA  1 
ATOM   6494 C  C   . PRO B 1 358 ? -16.073 10.446  12.531  1.00 15.13  ? 358 PRO B C   1 
ATOM   6495 O  O   . PRO B 1 358 ? -17.051 10.146  13.224  1.00 16.07  ? 358 PRO B O   1 
ATOM   6496 C  CB  . PRO B 1 358 ? -15.902 12.750  11.481  1.00 15.43  ? 358 PRO B CB  1 
ATOM   6497 C  CG  . PRO B 1 358 ? -14.718 13.686  11.256  1.00 14.45  ? 358 PRO B CG  1 
ATOM   6498 C  CD  . PRO B 1 358 ? -13.516 12.777  11.440  1.00 13.95  ? 358 PRO B CD  1 
ATOM   6499 N  N   . GLN B 1 359 ? -15.521 9.586   11.657  1.00 15.34  ? 359 GLN B N   1 
ATOM   6500 C  CA  . GLN B 1 359 ? -16.066 8.252   11.461  1.00 18.16  ? 359 GLN B CA  1 
ATOM   6501 C  C   . GLN B 1 359 ? -15.676 7.338   12.605  1.00 17.47  ? 359 GLN B C   1 
ATOM   6502 O  O   . GLN B 1 359 ? -16.495 6.551   13.034  1.00 15.94  ? 359 GLN B O   1 
ATOM   6503 C  CB  . GLN B 1 359 ? -15.576 7.581   10.171  1.00 20.63  ? 359 GLN B CB  1 
ATOM   6504 C  CG  . GLN B 1 359 ? -16.188 8.143   8.934   1.00 22.55  ? 359 GLN B CG  1 
ATOM   6505 C  CD  . GLN B 1 359 ? -17.688 8.037   9.003   1.00 23.59  ? 359 GLN B CD  1 
ATOM   6506 O  OE1 . GLN B 1 359 ? -18.386 9.040   9.105   1.00 23.96  ? 359 GLN B OE1 1 
ATOM   6507 N  NE2 . GLN B 1 359 ? -18.181 6.816   8.971   1.00 27.53  ? 359 GLN B NE2 1 
ATOM   6508 N  N   . LEU B 1 360 ? -14.403 7.395   13.052  1.00 16.71  ? 360 LEU B N   1 
ATOM   6509 C  CA  . LEU B 1 360 ? -14.004 6.698   14.257  1.00 15.12  ? 360 LEU B CA  1 
ATOM   6510 C  C   . LEU B 1 360 ? -15.004 6.978   15.377  1.00 14.00  ? 360 LEU B C   1 
ATOM   6511 O  O   . LEU B 1 360 ? -15.446 6.035   16.045  1.00 13.44  ? 360 LEU B O   1 
ATOM   6512 C  CB  . LEU B 1 360 ? -12.578 7.129   14.632  1.00 15.98  ? 360 LEU B CB  1 
ATOM   6513 C  CG  . LEU B 1 360 ? -12.091 6.690   16.005  1.00 16.68  ? 360 LEU B CG  1 
ATOM   6514 C  CD1 . LEU B 1 360 ? -12.010 5.159   16.133  1.00 17.30  ? 360 LEU B CD1 1 
ATOM   6515 C  CD2 . LEU B 1 360 ? -10.740 7.340   16.292  1.00 17.42  ? 360 LEU B CD2 1 
ATOM   6516 N  N   . HIS B 1 361 ? -15.376 8.273   15.537  1.00 11.71  ? 361 HIS B N   1 
ATOM   6517 C  CA  . HIS B 1 361 ? -16.210 8.705   16.625  1.00 12.29  ? 361 HIS B CA  1 
ATOM   6518 C  C   . HIS B 1 361 ? -17.674 8.287   16.423  1.00 13.30  ? 361 HIS B C   1 
ATOM   6519 O  O   . HIS B 1 361 ? -18.491 8.493   17.308  1.00 16.26  ? 361 HIS B O   1 
ATOM   6520 C  CB  . HIS B 1 361 ? -16.152 10.219  16.789  1.00 12.53  ? 361 HIS B CB  1 
ATOM   6521 C  CG  . HIS B 1 361 ? -14.847 10.673  17.336  1.00 11.92  ? 361 HIS B CG  1 
ATOM   6522 N  ND1 . HIS B 1 361 ? -14.542 12.008  17.477  1.00 12.44  ? 361 HIS B ND1 1 
ATOM   6523 C  CD2 . HIS B 1 361 ? -13.785 9.967   17.779  1.00 11.56  ? 361 HIS B CD2 1 
ATOM   6524 C  CE1 . HIS B 1 361 ? -13.319 12.099  18.022  1.00 12.55  ? 361 HIS B CE1 1 
ATOM   6525 N  NE2 . HIS B 1 361 ? -12.853 10.871  18.202  1.00 11.60  ? 361 HIS B NE2 1 
ATOM   6526 N  N   . ARG B 1 362 ? -17.999 7.657   15.296  1.00 14.13  ? 362 ARG B N   1 
ATOM   6527 C  CA  . ARG B 1 362 ? -19.344 7.125   15.063  1.00 14.95  ? 362 ARG B CA  1 
ATOM   6528 C  C   . ARG B 1 362 ? -19.324 5.591   14.954  1.00 16.90  ? 362 ARG B C   1 
ATOM   6529 O  O   . ARG B 1 362 ? -20.295 4.996   14.475  1.00 18.17  ? 362 ARG B O   1 
ATOM   6530 C  CB  . ARG B 1 362 ? -19.928 7.752   13.793  1.00 15.51  ? 362 ARG B CB  1 
ATOM   6531 C  CG  . ARG B 1 362 ? -20.326 9.219   13.937  1.00 14.93  ? 362 ARG B CG  1 
ATOM   6532 C  CD  . ARG B 1 362 ? -20.592 9.870   12.595  1.00 15.99  ? 362 ARG B CD  1 
ATOM   6533 N  NE  . ARG B 1 362 ? -21.117 11.252  12.692  1.00 15.32  ? 362 ARG B NE  1 
ATOM   6534 C  CZ  . ARG B 1 362 ? -20.408 12.330  13.007  1.00 16.16  ? 362 ARG B CZ  1 
ATOM   6535 N  NH1 . ARG B 1 362 ? -19.153 12.198  13.388  1.00 15.89  ? 362 ARG B NH1 1 
ATOM   6536 N  NH2 . ARG B 1 362 ? -20.947 13.543  12.961  1.00 14.73  ? 362 ARG B NH2 1 
ATOM   6537 N  N   . ASP B 1 363 ? -18.285 4.923   15.488  1.00 17.86  ? 363 ASP B N   1 
ATOM   6538 C  CA  . ASP B 1 363 ? -18.175 3.456   15.421  1.00 17.10  ? 363 ASP B CA  1 
ATOM   6539 C  C   . ASP B 1 363 ? -19.172 2.856   16.404  1.00 16.82  ? 363 ASP B C   1 
ATOM   6540 O  O   . ASP B 1 363 ? -19.065 3.036   17.621  1.00 17.18  ? 363 ASP B O   1 
ATOM   6541 C  CB  . ASP B 1 363 ? -16.742 2.995   15.739  1.00 18.57  ? 363 ASP B CB  1 
ATOM   6542 C  CG  . ASP B 1 363 ? -16.468 1.500   15.589  1.00 19.77  ? 363 ASP B CG  1 
ATOM   6543 O  OD1 . ASP B 1 363 ? -17.427 0.687   15.710  1.00 17.23  ? 363 ASP B OD1 1 
ATOM   6544 O  OD2 . ASP B 1 363 ? -15.293 1.160   15.360  1.00 19.63  ? 363 ASP B OD2 1 
ATOM   6545 N  N   . LYS B 1 364 ? -20.223 2.216   15.870  1.00 18.95  ? 364 LYS B N   1 
ATOM   6546 C  CA  . LYS B 1 364 ? -21.292 1.694   16.709  1.00 20.88  ? 364 LYS B CA  1 
ATOM   6547 C  C   . LYS B 1 364 ? -20.834 0.573   17.642  1.00 19.69  ? 364 LYS B C   1 
ATOM   6548 O  O   . LYS B 1 364 ? -21.434 0.395   18.698  1.00 22.67  ? 364 LYS B O   1 
ATOM   6549 C  CB  . LYS B 1 364 ? -22.457 1.199   15.852  1.00 23.23  ? 364 LYS B CB  1 
ATOM   6550 C  CG  . LYS B 1 364 ? -23.155 2.271   15.035  1.00 25.45  ? 364 LYS B CG  1 
ATOM   6551 C  CD  . LYS B 1 364 ? -24.309 1.691   14.231  1.00 31.29  ? 364 LYS B CD  1 
ATOM   6552 C  CE  . LYS B 1 364 ? -24.820 2.612   13.147  1.00 39.35  ? 364 LYS B CE  1 
ATOM   6553 N  NZ  . LYS B 1 364 ? -25.285 3.905   13.712  1.00 40.41  ? 364 LYS B NZ  1 
ATOM   6554 N  N   . THR B 1 365 ? -19.743 -0.130  17.333  1.00 22.90  ? 365 THR B N   1 
ATOM   6555 C  CA  . THR B 1 365 ? -19.292 -1.185  18.240  1.00 25.52  ? 365 THR B CA  1 
ATOM   6556 C  C   . THR B 1 365 ? -18.752 -0.573  19.531  1.00 24.93  ? 365 THR B C   1 
ATOM   6557 O  O   . THR B 1 365 ? -18.736 -1.241  20.548  1.00 22.71  ? 365 THR B O   1 
ATOM   6558 C  CB  . THR B 1 365 ? -18.249 -2.122  17.611  1.00 26.87  ? 365 THR B CB  1 
ATOM   6559 O  OG1 . THR B 1 365 ? -17.014 -1.419  17.500  1.00 27.80  ? 365 THR B OG1 1 
ATOM   6560 C  CG2 . THR B 1 365 ? -18.678 -2.664  16.262  1.00 27.97  ? 365 THR B CG2 1 
ATOM   6561 N  N   . ILE B 1 366 ? -18.301 0.699   19.473  1.00 22.86  ? 366 ILE B N   1 
ATOM   6562 C  CA  . ILE B 1 366 ? -17.782 1.425   20.620  1.00 20.88  ? 366 ILE B CA  1 
ATOM   6563 C  C   . ILE B 1 366 ? -18.889 2.234   21.281  1.00 20.03  ? 366 ILE B C   1 
ATOM   6564 O  O   . ILE B 1 366 ? -19.021 2.233   22.512  1.00 19.92  ? 366 ILE B O   1 
ATOM   6565 C  CB  . ILE B 1 366 ? -16.628 2.377   20.216  1.00 20.12  ? 366 ILE B CB  1 
ATOM   6566 C  CG1 . ILE B 1 366 ? -15.450 1.640   19.580  1.00 20.69  ? 366 ILE B CG1 1 
ATOM   6567 C  CG2 . ILE B 1 366 ? -16.204 3.210   21.426  1.00 20.95  ? 366 ILE B CG2 1 
ATOM   6568 C  CD1 . ILE B 1 366 ? -14.705 0.712   20.554  1.00 21.28  ? 366 ILE B CD1 1 
ATOM   6569 N  N   . TRP B 1 367 ? -19.651 2.982   20.484  1.00 18.02  ? 367 TRP B N   1 
ATOM   6570 C  CA  . TRP B 1 367 ? -20.505 4.004   21.070  1.00 18.96  ? 367 TRP B CA  1 
ATOM   6571 C  C   . TRP B 1 367 ? -21.961 3.567   21.145  1.00 20.01  ? 367 TRP B C   1 
ATOM   6572 O  O   . TRP B 1 367 ? -22.754 4.247   21.771  1.00 21.87  ? 367 TRP B O   1 
ATOM   6573 C  CB  . TRP B 1 367 ? -20.381 5.315   20.292  1.00 17.61  ? 367 TRP B CB  1 
ATOM   6574 C  CG  . TRP B 1 367 ? -18.974 5.841   20.268  1.00 17.99  ? 367 TRP B CG  1 
ATOM   6575 C  CD1 . TRP B 1 367 ? -18.041 5.710   19.286  1.00 18.22  ? 367 TRP B CD1 1 
ATOM   6576 C  CD2 . TRP B 1 367 ? -18.360 6.637   21.298  1.00 17.44  ? 367 TRP B CD2 1 
ATOM   6577 N  NE1 . TRP B 1 367 ? -16.875 6.348   19.652  1.00 17.77  ? 367 TRP B NE1 1 
ATOM   6578 C  CE2 . TRP B 1 367 ? -17.046 6.908   20.879  1.00 16.95  ? 367 TRP B CE2 1 
ATOM   6579 C  CE3 . TRP B 1 367 ? -18.792 7.117   22.541  1.00 16.73  ? 367 TRP B CE3 1 
ATOM   6580 C  CZ2 . TRP B 1 367 ? -16.176 7.663   21.640  1.00 16.93  ? 367 TRP B CZ2 1 
ATOM   6581 C  CZ3 . TRP B 1 367 ? -17.913 7.849   23.296  1.00 18.01  ? 367 TRP B CZ3 1 
ATOM   6582 C  CH2 . TRP B 1 367 ? -16.623 8.096   22.862  1.00 17.80  ? 367 TRP B CH2 1 
ATOM   6583 N  N   . GLY B 1 368 ? -22.310 2.428   20.551  1.00 22.05  ? 368 GLY B N   1 
ATOM   6584 C  CA  . GLY B 1 368 ? -23.684 1.965   20.572  1.00 22.64  ? 368 GLY B CA  1 
ATOM   6585 C  C   . GLY B 1 368 ? -24.467 2.493   19.377  1.00 24.88  ? 368 GLY B C   1 
ATOM   6586 O  O   . GLY B 1 368 ? -23.916 3.145   18.498  1.00 29.70  ? 368 GLY B O   1 
ATOM   6587 N  N   . ASP B 1 369 ? -25.780 2.286   19.402  1.00 26.28  ? 369 ASP B N   1 
ATOM   6588 C  CA  . ASP B 1 369 ? -26.644 2.518   18.251  1.00 31.25  ? 369 ASP B CA  1 
ATOM   6589 C  C   . ASP B 1 369 ? -26.731 4.006   17.919  1.00 29.65  ? 369 ASP B C   1 
ATOM   6590 O  O   . ASP B 1 369 ? -26.759 4.390   16.751  1.00 31.23  ? 369 ASP B O   1 
ATOM   6591 C  CB  . ASP B 1 369 ? -28.046 1.946   18.499  1.00 35.02  ? 369 ASP B CB  1 
ATOM   6592 C  CG  . ASP B 1 369 ? -28.064 0.570   19.149  1.00 42.91  ? 369 ASP B CG  1 
ATOM   6593 O  OD1 . ASP B 1 369 ? -27.531 0.448   20.288  1.00 43.13  ? 369 ASP B OD1 1 
ATOM   6594 O  OD2 . ASP B 1 369 ? -28.610 -0.372  18.519  1.00 44.93  ? 369 ASP B OD2 1 
ATOM   6595 N  N   . ASP B 1 370 ? -26.745 4.844   18.947  1.00 28.41  ? 370 ASP B N   1 
ATOM   6596 C  CA  . ASP B 1 370 ? -27.315 6.178   18.814  1.00 31.74  ? 370 ASP B CA  1 
ATOM   6597 C  C   . ASP B 1 370 ? -26.199 7.194   18.545  1.00 30.74  ? 370 ASP B C   1 
ATOM   6598 O  O   . ASP B 1 370 ? -26.184 8.257   19.161  1.00 30.31  ? 370 ASP B O   1 
ATOM   6599 C  CB  . ASP B 1 370 ? -28.093 6.516   20.093  1.00 33.30  ? 370 ASP B CB  1 
ATOM   6600 C  CG  . ASP B 1 370 ? -27.205 6.429   21.323  1.00 37.25  ? 370 ASP B CG  1 
ATOM   6601 O  OD1 . ASP B 1 370 ? -26.131 5.788   21.201  1.00 39.41  ? 370 ASP B OD1 1 
ATOM   6602 O  OD2 . ASP B 1 370 ? -27.536 7.056   22.372  1.00 43.74  ? 370 ASP B OD2 1 
ATOM   6603 N  N   . VAL B 1 371 ? -25.260 6.870   17.637  1.00 29.12  ? 371 VAL B N   1 
ATOM   6604 C  CA  . VAL B 1 371 ? -24.005 7.604   17.520  1.00 29.83  ? 371 VAL B CA  1 
ATOM   6605 C  C   . VAL B 1 371 ? -24.244 9.025   17.020  1.00 27.70  ? 371 VAL B C   1 
ATOM   6606 O  O   . VAL B 1 371 ? -23.394 9.904   17.208  1.00 24.76  ? 371 VAL B O   1 
ATOM   6607 C  CB  . VAL B 1 371 ? -22.997 6.897   16.598  1.00 30.85  ? 371 VAL B CB  1 
ATOM   6608 C  CG1 . VAL B 1 371 ? -22.603 5.561   17.163  1.00 32.69  ? 371 VAL B CG1 1 
ATOM   6609 C  CG2 . VAL B 1 371 ? -23.501 6.747   15.170  1.00 30.78  ? 371 VAL B CG2 1 
ATOM   6610 N  N   . GLU B 1 372 ? -25.404 9.259   16.400  1.00 23.80  ? 372 GLU B N   1 
ATOM   6611 C  CA  . GLU B 1 372 ? -25.717 10.579  15.912  1.00 23.36  ? 372 GLU B CA  1 
ATOM   6612 C  C   . GLU B 1 372 ? -26.294 11.466  17.020  1.00 21.60  ? 372 GLU B C   1 
ATOM   6613 O  O   . GLU B 1 372 ? -26.397 12.669  16.824  1.00 26.31  ? 372 GLU B O   1 
ATOM   6614 C  CB  . GLU B 1 372 ? -26.625 10.483  14.683  1.00 23.86  ? 372 GLU B CB  1 
ATOM   6615 C  CG  . GLU B 1 372 ? -25.900 10.033  13.426  1.00 26.01  ? 372 GLU B CG  1 
ATOM   6616 C  CD  . GLU B 1 372 ? -24.618 10.786  13.083  1.00 31.04  ? 372 GLU B CD  1 
ATOM   6617 O  OE1 . GLU B 1 372 ? -24.599 12.028  13.266  1.00 37.99  ? 372 GLU B OE1 1 
ATOM   6618 O  OE2 . GLU B 1 372 ? -23.654 10.149  12.565  1.00 27.21  ? 372 GLU B OE2 1 
ATOM   6619 N  N   . GLU B 1 373 ? -26.634 10.915  18.181  1.00 22.20  ? 373 GLU B N   1 
ATOM   6620 C  CA  . GLU B 1 373 ? -27.316 11.663  19.232  1.00 22.51  ? 373 GLU B CA  1 
ATOM   6621 C  C   . GLU B 1 373 ? -26.293 12.465  20.030  1.00 21.93  ? 373 GLU B C   1 
ATOM   6622 O  O   . GLU B 1 373 ? -25.244 11.906  20.334  1.00 19.19  ? 373 GLU B O   1 
ATOM   6623 C  CB  . GLU B 1 373 ? -27.989 10.697  20.212  1.00 28.15  ? 373 GLU B CB  1 
ATOM   6624 C  CG  . GLU B 1 373 ? -29.224 10.007  19.647  1.00 34.57  ? 373 GLU B CG  1 
ATOM   6625 C  CD  . GLU B 1 373 ? -30.303 10.974  19.183  1.00 41.03  ? 373 GLU B CD  1 
ATOM   6626 O  OE1 . GLU B 1 373 ? -30.786 11.779  20.021  1.00 44.50  ? 373 GLU B OE1 1 
ATOM   6627 O  OE2 . GLU B 1 373 ? -30.648 10.937  17.983  1.00 46.07  ? 373 GLU B OE2 1 
ATOM   6628 N  N   . PHE B 1 374 ? -26.624 13.714  20.398  1.00 18.09  ? 374 PHE B N   1 
ATOM   6629 C  CA  . PHE B 1 374 ? -25.805 14.492  21.319  1.00 17.62  ? 374 PHE B CA  1 
ATOM   6630 C  C   . PHE B 1 374 ? -26.149 14.148  22.772  1.00 18.97  ? 374 PHE B C   1 
ATOM   6631 O  O   . PHE B 1 374 ? -27.133 14.617  23.330  1.00 19.68  ? 374 PHE B O   1 
ATOM   6632 C  CB  . PHE B 1 374 ? -25.945 15.994  21.058  1.00 16.31  ? 374 PHE B CB  1 
ATOM   6633 C  CG  . PHE B 1 374 ? -24.973 16.835  21.816  1.00 15.56  ? 374 PHE B CG  1 
ATOM   6634 C  CD1 . PHE B 1 374 ? -23.673 16.960  21.378  1.00 14.97  ? 374 PHE B CD1 1 
ATOM   6635 C  CD2 . PHE B 1 374 ? -25.373 17.542  22.937  1.00 17.19  ? 374 PHE B CD2 1 
ATOM   6636 C  CE1 . PHE B 1 374 ? -22.779 17.761  22.066  1.00 16.65  ? 374 PHE B CE1 1 
ATOM   6637 C  CE2 . PHE B 1 374 ? -24.474 18.352  23.617  1.00 16.98  ? 374 PHE B CE2 1 
ATOM   6638 C  CZ  . PHE B 1 374 ? -23.167 18.413  23.217  1.00 16.66  ? 374 PHE B CZ  1 
ATOM   6639 N  N   . ARG B 1 375 ? -25.258 13.396  23.430  1.00 19.31  ? 375 ARG B N   1 
ATOM   6640 C  CA  . ARG B 1 375 ? -25.503 12.907  24.778  1.00 19.17  ? 375 ARG B CA  1 
ATOM   6641 C  C   . ARG B 1 375 ? -24.206 13.017  25.584  1.00 18.40  ? 375 ARG B C   1 
ATOM   6642 O  O   . ARG B 1 375 ? -23.383 12.113  25.554  1.00 16.79  ? 375 ARG B O   1 
ATOM   6643 C  CB  . ARG B 1 375 ? -26.032 11.472  24.668  1.00 24.78  ? 375 ARG B CB  1 
ATOM   6644 C  CG  . ARG B 1 375 ? -26.517 10.881  25.982  1.00 30.55  ? 375 ARG B CG  1 
ATOM   6645 C  CD  . ARG B 1 375 ? -27.399 9.670   25.743  1.00 35.95  ? 375 ARG B CD  1 
ATOM   6646 N  NE  . ARG B 1 375 ? -26.672 8.526   25.214  1.00 41.45  ? 375 ARG B NE  1 
ATOM   6647 C  CZ  . ARG B 1 375 ? -25.750 7.832   25.891  1.00 51.04  ? 375 ARG B CZ  1 
ATOM   6648 N  NH1 . ARG B 1 375 ? -25.401 8.191   27.118  1.00 49.57  ? 375 ARG B NH1 1 
ATOM   6649 N  NH2 . ARG B 1 375 ? -25.172 6.775   25.338  1.00 49.81  ? 375 ARG B NH2 1 
ATOM   6650 N  N   . PRO B 1 376 ? -23.969 14.142  26.297  1.00 17.45  ? 376 PRO B N   1 
ATOM   6651 C  CA  . PRO B 1 376 ? -22.731 14.360  27.045  1.00 17.04  ? 376 PRO B CA  1 
ATOM   6652 C  C   . PRO B 1 376 ? -22.485 13.316  28.126  1.00 17.65  ? 376 PRO B C   1 
ATOM   6653 O  O   . PRO B 1 376 ? -21.325 13.002  28.413  1.00 16.06  ? 376 PRO B O   1 
ATOM   6654 C  CB  . PRO B 1 376 ? -22.928 15.780  27.615  1.00 17.15  ? 376 PRO B CB  1 
ATOM   6655 C  CG  . PRO B 1 376 ? -23.905 16.440  26.683  1.00 17.28  ? 376 PRO B CG  1 
ATOM   6656 C  CD  . PRO B 1 376 ? -24.825 15.338  26.273  1.00 16.18  ? 376 PRO B CD  1 
ATOM   6657 N  N   . GLU B 1 377 ? -23.584 12.700  28.602  1.00 17.81  ? 377 GLU B N   1 
ATOM   6658 C  CA  . GLU B 1 377 ? -23.537 11.615  29.578  1.00 20.02  ? 377 GLU B CA  1 
ATOM   6659 C  C   . GLU B 1 377 ? -22.704 10.427  29.084  1.00 18.25  ? 377 GLU B C   1 
ATOM   6660 O  O   . GLU B 1 377 ? -22.241 9.644   29.894  1.00 19.23  ? 377 GLU B O   1 
ATOM   6661 C  CB  . GLU B 1 377 ? -24.952 11.150  29.958  1.00 22.57  ? 377 GLU B CB  1 
ATOM   6662 C  CG  . GLU B 1 377 ? -25.807 12.229  30.624  1.00 25.58  ? 377 GLU B CG  1 
ATOM   6663 C  CD  . GLU B 1 377 ? -26.378 13.302  29.699  1.00 27.86  ? 377 GLU B CD  1 
ATOM   6664 O  OE1 . GLU B 1 377 ? -26.277 13.126  28.447  1.00 27.83  ? 377 GLU B OE1 1 
ATOM   6665 O  OE2 . GLU B 1 377 ? -26.904 14.328  30.232  1.00 25.19  ? 377 GLU B OE2 1 
ATOM   6666 N  N   . ARG B 1 378 ? -22.428 10.300  27.782  1.00 16.64  ? 378 ARG B N   1 
ATOM   6667 C  CA  . ARG B 1 378 ? -21.488 9.266   27.350  1.00 18.30  ? 378 ARG B CA  1 
ATOM   6668 C  C   . ARG B 1 378 ? -20.122 9.428   28.029  1.00 20.02  ? 378 ARG B C   1 
ATOM   6669 O  O   . ARG B 1 378 ? -19.352 8.458   28.096  1.00 17.33  ? 378 ARG B O   1 
ATOM   6670 C  CB  . ARG B 1 378 ? -21.139 9.358   25.862  1.00 18.79  ? 378 ARG B CB  1 
ATOM   6671 C  CG  . ARG B 1 378 ? -22.303 9.180   24.905  1.00 19.01  ? 378 ARG B CG  1 
ATOM   6672 C  CD  . ARG B 1 378 ? -21.852 9.550   23.496  1.00 20.35  ? 378 ARG B CD  1 
ATOM   6673 N  NE  . ARG B 1 378 ? -22.982 9.848   22.629  1.00 23.70  ? 378 ARG B NE  1 
ATOM   6674 C  CZ  . ARG B 1 378 ? -23.794 8.942   22.092  1.00 24.93  ? 378 ARG B CZ  1 
ATOM   6675 N  NH1 . ARG B 1 378 ? -23.545 7.645   22.248  1.00 23.97  ? 378 ARG B NH1 1 
ATOM   6676 N  NH2 . ARG B 1 378 ? -24.831 9.341   21.369  1.00 24.99  ? 378 ARG B NH2 1 
ATOM   6677 N  N   . PHE B 1 379 ? -19.807 10.664  28.459  1.00 16.82  ? 379 PHE B N   1 
ATOM   6678 C  CA  . PHE B 1 379 ? -18.515 10.993  29.036  1.00 16.99  ? 379 PHE B CA  1 
ATOM   6679 C  C   . PHE B 1 379 ? -18.592 11.152  30.560  1.00 17.50  ? 379 PHE B C   1 
ATOM   6680 O  O   . PHE B 1 379 ? -17.677 11.714  31.160  1.00 19.83  ? 379 PHE B O   1 
ATOM   6681 C  CB  . PHE B 1 379 ? -17.967 12.254  28.352  1.00 17.51  ? 379 PHE B CB  1 
ATOM   6682 C  CG  . PHE B 1 379 ? -17.513 12.032  26.931  1.00 17.45  ? 379 PHE B CG  1 
ATOM   6683 C  CD1 . PHE B 1 379 ? -16.214 11.619  26.655  1.00 16.83  ? 379 PHE B CD1 1 
ATOM   6684 C  CD2 . PHE B 1 379 ? -18.370 12.283  25.864  1.00 17.23  ? 379 PHE B CD2 1 
ATOM   6685 C  CE1 . PHE B 1 379 ? -15.812 11.392  25.352  1.00 17.89  ? 379 PHE B CE1 1 
ATOM   6686 C  CE2 . PHE B 1 379 ? -17.964 12.047  24.563  1.00 17.36  ? 379 PHE B CE2 1 
ATOM   6687 C  CZ  . PHE B 1 379 ? -16.699 11.596  24.303  1.00 16.12  ? 379 PHE B CZ  1 
ATOM   6688 N  N   . GLU B 1 380 ? -19.635 10.622  31.211  1.00 19.10  ? 380 GLU B N   1 
ATOM   6689 C  CA  . GLU B 1 380 ? -19.750 10.651  32.666  1.00 22.03  ? 380 GLU B CA  1 
ATOM   6690 C  C   . GLU B 1 380 ? -18.444 10.188  33.326  1.00 21.84  ? 380 GLU B C   1 
ATOM   6691 O  O   . GLU B 1 380 ? -18.040 10.730  34.359  1.00 18.65  ? 380 GLU B O   1 
ATOM   6692 C  CB  . GLU B 1 380 ? -20.795 9.665   33.206  1.00 24.05  ? 380 GLU B CB  1 
ATOM   6693 C  CG  . GLU B 1 380 ? -22.232 10.128  33.110  1.00 34.46  ? 380 GLU B CG  1 
ATOM   6694 C  CD  . GLU B 1 380 ? -22.665 11.280  34.012  1.00 42.81  ? 380 GLU B CD  1 
ATOM   6695 O  OE1 . GLU B 1 380 ? -21.794 11.893  34.704  1.00 40.27  ? 380 GLU B OE1 1 
ATOM   6696 O  OE2 . GLU B 1 380 ? -23.892 11.583  33.997  1.00 50.69  ? 380 GLU B OE2 1 
ATOM   6697 N  N   . ASN B 1 381 ? -17.906 9.073   32.807  1.00 18.50  ? 381 ASN B N   1 
ATOM   6698 C  CA  . ASN B 1 381 ? -16.642 8.516   33.272  1.00 20.97  ? 381 ASN B CA  1 
ATOM   6699 C  C   . ASN B 1 381 ? -15.762 8.351   32.043  1.00 20.89  ? 381 ASN B C   1 
ATOM   6700 O  O   . ASN B 1 381 ? -15.909 7.407   31.262  1.00 20.33  ? 381 ASN B O   1 
ATOM   6701 C  CB  . ASN B 1 381 ? -16.808 7.209   34.049  1.00 20.33  ? 381 ASN B CB  1 
ATOM   6702 C  CG  . ASN B 1 381 ? -15.487 6.674   34.588  1.00 23.78  ? 381 ASN B CG  1 
ATOM   6703 O  OD1 . ASN B 1 381 ? -15.464 5.645   35.261  1.00 26.96  ? 381 ASN B OD1 1 
ATOM   6704 N  ND2 . ASN B 1 381 ? -14.381 7.349   34.298  1.00 21.93  ? 381 ASN B ND2 1 
ATOM   6705 N  N   . PRO B 1 382 ? -14.893 9.336   31.776  1.00 22.19  ? 382 PRO B N   1 
ATOM   6706 C  CA  . PRO B 1 382 ? -14.133 9.343   30.534  1.00 25.19  ? 382 PRO B CA  1 
ATOM   6707 C  C   . PRO B 1 382 ? -13.250 8.117   30.392  1.00 22.34  ? 382 PRO B C   1 
ATOM   6708 O  O   . PRO B 1 382 ? -12.989 7.683   29.276  1.00 22.58  ? 382 PRO B O   1 
ATOM   6709 C  CB  . PRO B 1 382 ? -13.285 10.616  30.661  1.00 27.21  ? 382 PRO B CB  1 
ATOM   6710 C  CG  . PRO B 1 382 ? -14.094 11.500  31.591  1.00 28.39  ? 382 PRO B CG  1 
ATOM   6711 C  CD  . PRO B 1 382 ? -14.639 10.526  32.607  1.00 26.89  ? 382 PRO B CD  1 
ATOM   6712 N  N   . SER B 1 383 ? -12.820 7.558   31.532  1.00 21.53  ? 383 SER B N   1 
ATOM   6713 C  CA  . SER B 1 383 ? -11.906 6.422   31.505  1.00 24.15  ? 383 SER B CA  1 
ATOM   6714 C  C   . SER B 1 383 ? -12.608 5.162   30.996  1.00 22.01  ? 383 SER B C   1 
ATOM   6715 O  O   . SER B 1 383 ? -11.923 4.223   30.622  1.00 23.84  ? 383 SER B O   1 
ATOM   6716 C  CB  . SER B 1 383 ? -11.220 6.215   32.851  1.00 28.09  ? 383 SER B CB  1 
ATOM   6717 O  OG  . SER B 1 383 ? -12.046 5.477   33.735  1.00 33.41  ? 383 SER B OG  1 
ATOM   6718 N  N   . ALA B 1 384 ? -13.954 5.173   30.891  1.00 20.12  ? 384 ALA B N   1 
ATOM   6719 C  CA  . ALA B 1 384 ? -14.708 4.047   30.341  1.00 19.12  ? 384 ALA B CA  1 
ATOM   6720 C  C   . ALA B 1 384 ? -14.498 3.914   28.836  1.00 19.45  ? 384 ALA B C   1 
ATOM   6721 O  O   . ALA B 1 384 ? -14.715 2.839   28.280  1.00 19.86  ? 384 ALA B O   1 
ATOM   6722 C  CB  . ALA B 1 384 ? -16.179 4.179   30.644  1.00 18.39  ? 384 ALA B CB  1 
ATOM   6723 N  N   . ILE B 1 385 ? -14.012 4.976   28.193  1.00 19.95  ? 385 ILE B N   1 
ATOM   6724 C  CA  . ILE B 1 385 ? -13.799 4.950   26.757  1.00 21.04  ? 385 ILE B CA  1 
ATOM   6725 C  C   . ILE B 1 385 ? -12.543 4.150   26.429  1.00 19.15  ? 385 ILE B C   1 
ATOM   6726 O  O   . ILE B 1 385 ? -11.470 4.415   26.960  1.00 17.00  ? 385 ILE B O   1 
ATOM   6727 C  CB  . ILE B 1 385 ? -13.742 6.383   26.197  1.00 23.09  ? 385 ILE B CB  1 
ATOM   6728 C  CG1 . ILE B 1 385 ? -15.050 7.120   26.492  1.00 25.73  ? 385 ILE B CG1 1 
ATOM   6729 C  CG2 . ILE B 1 385 ? -13.418 6.366   24.699  1.00 23.75  ? 385 ILE B CG2 1 
ATOM   6730 C  CD1 . ILE B 1 385 ? -14.866 8.614   26.611  1.00 30.01  ? 385 ILE B CD1 1 
ATOM   6731 N  N   . PRO B 1 386 ? -12.634 3.129   25.544  1.00 18.94  ? 386 PRO B N   1 
ATOM   6732 C  CA  . PRO B 1 386 ? -11.485 2.264   25.236  1.00 18.49  ? 386 PRO B CA  1 
ATOM   6733 C  C   . PRO B 1 386 ? -10.341 3.062   24.622  1.00 18.22  ? 386 PRO B C   1 
ATOM   6734 O  O   . PRO B 1 386 ? -10.575 4.111   24.068  1.00 17.18  ? 386 PRO B O   1 
ATOM   6735 C  CB  . PRO B 1 386 ? -12.043 1.253   24.236  1.00 18.58  ? 386 PRO B CB  1 
ATOM   6736 C  CG  . PRO B 1 386 ? -13.553 1.305   24.420  1.00 18.21  ? 386 PRO B CG  1 
ATOM   6737 C  CD  . PRO B 1 386 ? -13.851 2.712   24.844  1.00 18.93  ? 386 PRO B CD  1 
ATOM   6738 N  N   . GLN B 1 387 ? -9.104  2.548   24.682  1.00 18.82  ? 387 GLN B N   1 
ATOM   6739 C  CA  . GLN B 1 387 ? -7.966  3.174   24.014  1.00 20.06  ? 387 GLN B CA  1 
ATOM   6740 C  C   . GLN B 1 387 ? -8.211  3.360   22.515  1.00 19.65  ? 387 GLN B C   1 
ATOM   6741 O  O   . GLN B 1 387 ? -8.797  2.489   21.851  1.00 16.10  ? 387 GLN B O   1 
ATOM   6742 C  CB  . GLN B 1 387 ? -6.717  2.302   24.155  1.00 23.92  ? 387 GLN B CB  1 
ATOM   6743 C  CG  . GLN B 1 387 ? -5.677  2.869   25.077  1.00 27.63  ? 387 GLN B CG  1 
ATOM   6744 C  CD  . GLN B 1 387 ? -4.319  2.281   24.782  1.00 30.42  ? 387 GLN B CD  1 
ATOM   6745 O  OE1 . GLN B 1 387 ? -3.355  3.007   24.544  1.00 33.32  ? 387 GLN B OE1 1 
ATOM   6746 N  NE2 . GLN B 1 387 ? -4.239  0.959   24.763  1.00 29.41  ? 387 GLN B NE2 1 
ATOM   6747 N  N   . HIS B 1 388 ? -7.849  4.557   22.014  1.00 17.29  ? 388 HIS B N   1 
ATOM   6748 C  CA  . HIS B 1 388 ? -7.840  4.852   20.585  1.00 16.83  ? 388 HIS B CA  1 
ATOM   6749 C  C   . HIS B 1 388 ? -9.260  4.921   20.035  1.00 14.69  ? 388 HIS B C   1 
ATOM   6750 O  O   . HIS B 1 388 ? -9.497  4.790   18.838  1.00 15.13  ? 388 HIS B O   1 
ATOM   6751 C  CB  . HIS B 1 388 ? -6.926  3.878   19.850  1.00 19.35  ? 388 HIS B CB  1 
ATOM   6752 C  CG  . HIS B 1 388 ? -5.548  3.813   20.432  1.00 20.83  ? 388 HIS B CG  1 
ATOM   6753 N  ND1 . HIS B 1 388 ? -4.863  4.945   20.813  1.00 21.50  ? 388 HIS B ND1 1 
ATOM   6754 C  CD2 . HIS B 1 388 ? -4.729  2.781   20.681  1.00 21.20  ? 388 HIS B CD2 1 
ATOM   6755 C  CE1 . HIS B 1 388 ? -3.650  4.608   21.244  1.00 22.75  ? 388 HIS B CE1 1 
ATOM   6756 N  NE2 . HIS B 1 388 ? -3.529  3.297   21.159  1.00 22.50  ? 388 HIS B NE2 1 
ATOM   6757 N  N   . ALA B 1 389 ? -10.217 5.196   20.903  1.00 15.07  ? 389 ALA B N   1 
ATOM   6758 C  CA  . ALA B 1 389 ? -11.592 5.282   20.442  1.00 14.73  ? 389 ALA B CA  1 
ATOM   6759 C  C   . ALA B 1 389 ? -12.050 6.730   20.296  1.00 13.89  ? 389 ALA B C   1 
ATOM   6760 O  O   . ALA B 1 389 ? -12.978 6.988   19.541  1.00 12.94  ? 389 ALA B O   1 
ATOM   6761 C  CB  . ALA B 1 389 ? -12.485 4.529   21.377  1.00 14.39  ? 389 ALA B CB  1 
ATOM   6762 N  N   . PHE B 1 390 ? -11.424 7.644   21.040  1.00 13.98  ? 390 PHE B N   1 
ATOM   6763 C  CA  . PHE B 1 390 ? -11.801 9.059   21.053  1.00 13.16  ? 390 PHE B CA  1 
ATOM   6764 C  C   . PHE B 1 390 ? -10.517 9.833   20.833  1.00 12.73  ? 390 PHE B C   1 
ATOM   6765 O  O   . PHE B 1 390 ? -9.658  9.800   21.704  1.00 15.25  ? 390 PHE B O   1 
ATOM   6766 C  CB  . PHE B 1 390 ? -12.477 9.397   22.374  1.00 13.51  ? 390 PHE B CB  1 
ATOM   6767 C  CG  . PHE B 1 390 ? -12.926 10.825  22.537  1.00 13.44  ? 390 PHE B CG  1 
ATOM   6768 C  CD1 . PHE B 1 390 ? -13.868 11.385  21.699  1.00 13.36  ? 390 PHE B CD1 1 
ATOM   6769 C  CD2 . PHE B 1 390 ? -12.436 11.589  23.587  1.00 14.78  ? 390 PHE B CD2 1 
ATOM   6770 C  CE1 . PHE B 1 390 ? -14.303 12.685  21.897  1.00 12.28  ? 390 PHE B CE1 1 
ATOM   6771 C  CE2 . PHE B 1 390 ? -12.816 12.917  23.744  1.00 13.57  ? 390 PHE B CE2 1 
ATOM   6772 C  CZ  . PHE B 1 390 ? -13.768 13.442  22.904  1.00 12.77  ? 390 PHE B CZ  1 
ATOM   6773 N  N   . LYS B 1 391 ? -10.328 10.399  19.644  1.00 11.88  ? 391 LYS B N   1 
ATOM   6774 C  CA  . LYS B 1 391 ? -9.011  10.877  19.266  1.00 12.22  ? 391 LYS B CA  1 
ATOM   6775 C  C   . LYS B 1 391 ? -9.058  12.288  18.689  1.00 11.37  ? 391 LYS B C   1 
ATOM   6776 O  O   . LYS B 1 391 ? -8.398  12.570  17.678  1.00 10.80  ? 391 LYS B O   1 
ATOM   6777 C  CB  . LYS B 1 391 ? -8.393  9.931   18.237  1.00 14.18  ? 391 LYS B CB  1 
ATOM   6778 C  CG  . LYS B 1 391 ? -8.220  8.501   18.728  1.00 17.21  ? 391 LYS B CG  1 
ATOM   6779 C  CD  . LYS B 1 391 ? -7.206  8.365   19.811  1.00 22.20  ? 391 LYS B CD  1 
ATOM   6780 C  CE  . LYS B 1 391 ? -5.811  8.155   19.253  1.00 23.18  ? 391 LYS B CE  1 
ATOM   6781 N  NZ  . LYS B 1 391 ? -4.882  7.946   20.369  1.00 22.95  ? 391 LYS B NZ  1 
ATOM   6782 N  N   . PRO B 1 392 ? -9.820  13.246  19.264  1.00 10.99  ? 392 PRO B N   1 
ATOM   6783 C  CA  . PRO B 1 392 ? -9.886  14.583  18.679  1.00 12.21  ? 392 PRO B CA  1 
ATOM   6784 C  C   . PRO B 1 392 ? -8.597  15.389  18.769  1.00 12.58  ? 392 PRO B C   1 
ATOM   6785 O  O   . PRO B 1 392 ? -8.468  16.442  18.125  1.00 13.39  ? 392 PRO B O   1 
ATOM   6786 C  CB  . PRO B 1 392 ? -10.950 15.288  19.514  1.00 12.49  ? 392 PRO B CB  1 
ATOM   6787 C  CG  . PRO B 1 392 ? -10.950 14.544  20.813  1.00 11.19  ? 392 PRO B CG  1 
ATOM   6788 C  CD  . PRO B 1 392 ? -10.573 13.119  20.507  1.00 10.82  ? 392 PRO B CD  1 
ATOM   6789 N  N   . PHE B 1 393 ? -7.629  14.873  19.558  1.00 12.80  ? 393 PHE B N   1 
ATOM   6790 C  CA  . PHE B 1 393 ? -6.349  15.561  19.736  1.00 11.82  ? 393 PHE B CA  1 
ATOM   6791 C  C   . PHE B 1 393 ? -5.178  14.767  19.176  1.00 13.43  ? 393 PHE B C   1 
ATOM   6792 O  O   . PHE B 1 393 ? -4.018  15.072  19.479  1.00 13.82  ? 393 PHE B O   1 
ATOM   6793 C  CB  . PHE B 1 393 ? -6.202  15.885  21.218  1.00 12.46  ? 393 PHE B CB  1 
ATOM   6794 C  CG  . PHE B 1 393 ? -7.195  16.881  21.752  1.00 11.37  ? 393 PHE B CG  1 
ATOM   6795 C  CD1 . PHE B 1 393 ? -7.066  18.224  21.455  1.00 12.30  ? 393 PHE B CD1 1 
ATOM   6796 C  CD2 . PHE B 1 393 ? -8.244  16.472  22.548  1.00 11.68  ? 393 PHE B CD2 1 
ATOM   6797 C  CE1 . PHE B 1 393 ? -7.966  19.155  21.963  1.00 13.76  ? 393 PHE B CE1 1 
ATOM   6798 C  CE2 . PHE B 1 393 ? -9.129  17.384  23.061  1.00 12.06  ? 393 PHE B CE2 1 
ATOM   6799 C  CZ  . PHE B 1 393 ? -9.016  18.718  22.749  1.00 13.35  ? 393 PHE B CZ  1 
ATOM   6800 N  N   . GLY B 1 394 ? -5.472  13.821  18.286  1.00 13.97  ? 394 GLY B N   1 
ATOM   6801 C  CA  . GLY B 1 394 ? -4.461  13.009  17.629  1.00 14.55  ? 394 GLY B CA  1 
ATOM   6802 C  C   . GLY B 1 394 ? -3.913  11.907  18.552  1.00 13.68  ? 394 GLY B C   1 
ATOM   6803 O  O   . GLY B 1 394 ? -4.580  11.398  19.448  1.00 13.64  ? 394 GLY B O   1 
ATOM   6804 N  N   . ASN B 1 395 ? -2.647  11.560  18.354  1.00 14.88  ? 395 ASN B N   1 
ATOM   6805 C  CA  . ASN B 1 395 ? -2.120  10.344  18.921  1.00 15.19  ? 395 ASN B CA  1 
ATOM   6806 C  C   . ASN B 1 395 ? -0.682  10.495  19.380  1.00 14.45  ? 395 ASN B C   1 
ATOM   6807 O  O   . ASN B 1 395 ? 0.165   10.865  18.591  1.00 15.02  ? 395 ASN B O   1 
ATOM   6808 C  CB  . ASN B 1 395 ? -2.084  9.196   17.907  1.00 16.21  ? 395 ASN B CB  1 
ATOM   6809 C  CG  . ASN B 1 395 ? -1.703  7.910   18.606  1.00 15.86  ? 395 ASN B CG  1 
ATOM   6810 O  OD1 . ASN B 1 395 ? -2.386  7.485   19.545  1.00 16.85  ? 395 ASN B OD1 1 
ATOM   6811 N  ND2 . ASN B 1 395 ? -0.573  7.347   18.236  1.00 17.92  ? 395 ASN B ND2 1 
ATOM   6812 N  N   . GLY B 1 396 ? -0.447  10.076  20.625  1.00 14.33  ? 396 GLY B N   1 
ATOM   6813 C  CA  . GLY B 1 396 ? 0.895   9.750   21.086  1.00 15.13  ? 396 GLY B CA  1 
ATOM   6814 C  C   . GLY B 1 396 ? 1.741   10.999  21.289  1.00 14.60  ? 396 GLY B C   1 
ATOM   6815 O  O   . GLY B 1 396 ? 1.227   12.020  21.693  1.00 15.41  ? 396 GLY B O   1 
ATOM   6816 N  N   . GLN B 1 397 ? 3.033   10.891  20.998  1.00 14.76  ? 397 GLN B N   1 
ATOM   6817 C  CA  . GLN B 1 397 ? 3.966   11.980  21.191  1.00 16.78  ? 397 GLN B CA  1 
ATOM   6818 C  C   . GLN B 1 397 ? 3.659   13.119  20.214  1.00 16.16  ? 397 GLN B C   1 
ATOM   6819 O  O   . GLN B 1 397 ? 4.091   14.247  20.431  1.00 15.62  ? 397 GLN B O   1 
ATOM   6820 C  CB  . GLN B 1 397 ? 5.408   11.474  21.091  1.00 15.92  ? 397 GLN B CB  1 
ATOM   6821 C  CG  . GLN B 1 397 ? 5.857   11.001  19.714  1.00 16.43  ? 397 GLN B CG  1 
ATOM   6822 C  CD  . GLN B 1 397 ? 7.306   10.575  19.743  1.00 18.04  ? 397 GLN B CD  1 
ATOM   6823 O  OE1 . GLN B 1 397 ? 8.005   10.771  20.725  1.00 17.65  ? 397 GLN B OE1 1 
ATOM   6824 N  NE2 . GLN B 1 397 ? 7.778   9.989   18.661  1.00 20.24  ? 397 GLN B NE2 1 
ATOM   6825 N  N   . ARG B 1 398 ? 2.901   12.847  19.148  1.00 15.27  ? 398 ARG B N   1 
ATOM   6826 C  CA  . ARG B 1 398 ? 2.490   13.892  18.228  1.00 12.96  ? 398 ARG B CA  1 
ATOM   6827 C  C   . ARG B 1 398 ? 1.039   14.297  18.451  1.00 13.03  ? 398 ARG B C   1 
ATOM   6828 O  O   . ARG B 1 398 ? 0.438   14.866  17.555  1.00 15.33  ? 398 ARG B O   1 
ATOM   6829 C  CB  . ARG B 1 398 ? 2.702   13.431  16.785  1.00 12.53  ? 398 ARG B CB  1 
ATOM   6830 C  CG  . ARG B 1 398 ? 4.126   13.007  16.456  1.00 12.38  ? 398 ARG B CG  1 
ATOM   6831 C  CD  . ARG B 1 398 ? 5.138   14.129  16.705  1.00 13.21  ? 398 ARG B CD  1 
ATOM   6832 N  NE  . ARG B 1 398 ? 4.772   15.341  16.020  1.00 12.46  ? 398 ARG B NE  1 
ATOM   6833 C  CZ  . ARG B 1 398 ? 5.208   15.695  14.815  1.00 13.46  ? 398 ARG B CZ  1 
ATOM   6834 N  NH1 . ARG B 1 398 ? 5.874   14.840  14.059  1.00 13.96  ? 398 ARG B NH1 1 
ATOM   6835 N  NH2 . ARG B 1 398 ? 4.899   16.878  14.318  1.00 14.11  ? 398 ARG B NH2 1 
ATOM   6836 N  N   . ALA B 1 399 ? 0.481   13.985  19.621  1.00 12.61  ? 399 ALA B N   1 
ATOM   6837 C  CA  . ALA B 1 399 ? -0.810  14.511  19.993  1.00 13.24  ? 399 ALA B CA  1 
ATOM   6838 C  C   . ALA B 1 399 ? -0.709  16.014  20.294  1.00 13.72  ? 399 ALA B C   1 
ATOM   6839 O  O   . ALA B 1 399 ? 0.381   16.612  20.403  1.00 12.13  ? 399 ALA B O   1 
ATOM   6840 C  CB  . ALA B 1 399 ? -1.361  13.756  21.172  1.00 13.84  ? 399 ALA B CB  1 
ATOM   6841 N  N   . CYS B 1 400 ? -1.898  16.623  20.326  1.00 12.20  ? 400 CYS B N   1 
ATOM   6842 C  CA  . CYS B 1 400 ? -2.012  18.050  20.486  1.00 12.23  ? 400 CYS B CA  1 
ATOM   6843 C  C   . CYS B 1 400 ? -1.359  18.497  21.781  1.00 13.26  ? 400 CYS B C   1 
ATOM   6844 O  O   . CYS B 1 400 ? -1.805  18.112  22.864  1.00 11.61  ? 400 CYS B O   1 
ATOM   6845 C  CB  . CYS B 1 400 ? -3.460  18.462  20.538  1.00 11.51  ? 400 CYS B CB  1 
ATOM   6846 S  SG  . CYS B 1 400 ? -3.734  20.253  20.609  1.00 13.46  ? 400 CYS B SG  1 
ATOM   6847 N  N   . ILE B 1 401 ? -0.366  19.378  21.653  1.00 14.04  ? 401 ILE B N   1 
ATOM   6848 C  CA  . ILE B 1 401 ? 0.290   19.929  22.835  1.00 14.50  ? 401 ILE B CA  1 
ATOM   6849 C  C   . ILE B 1 401 ? -0.651  20.866  23.612  1.00 15.04  ? 401 ILE B C   1 
ATOM   6850 O  O   . ILE B 1 401 ? -0.544  20.984  24.829  1.00 14.45  ? 401 ILE B O   1 
ATOM   6851 C  CB  . ILE B 1 401 ? 1.623   20.589  22.398  1.00 14.91  ? 401 ILE B CB  1 
ATOM   6852 C  CG1 . ILE B 1 401 ? 2.580   20.686  23.571  1.00 15.37  ? 401 ILE B CG1 1 
ATOM   6853 C  CG2 . ILE B 1 401 ? 1.409   21.927  21.703  1.00 15.72  ? 401 ILE B CG2 1 
ATOM   6854 C  CD1 . ILE B 1 401 ? 3.828   21.570  23.266  1.00 15.68  ? 401 ILE B CD1 1 
ATOM   6855 N  N   . GLY B 1 402 ? -1.605  21.488  22.911  1.00 16.49  ? 402 GLY B N   1 
ATOM   6856 C  CA  . GLY B 1 402 ? -2.460  22.538  23.455  1.00 16.89  ? 402 GLY B CA  1 
ATOM   6857 C  C   . GLY B 1 402 ? -3.816  22.040  23.944  1.00 17.03  ? 402 GLY B C   1 
ATOM   6858 O  O   . GLY B 1 402 ? -4.678  22.837  24.311  1.00 16.65  ? 402 GLY B O   1 
ATOM   6859 N  N   . GLN B 1 403 ? -3.951  20.733  24.102  1.00 15.85  ? 403 GLN B N   1 
ATOM   6860 C  CA  . GLN B 1 403 ? -5.237  20.160  24.481  1.00 15.44  ? 403 GLN B CA  1 
ATOM   6861 C  C   . GLN B 1 403 ? -5.758  20.735  25.790  1.00 13.82  ? 403 GLN B C   1 
ATOM   6862 O  O   . GLN B 1 403 ? -6.953  21.030  25.918  1.00 14.59  ? 403 GLN B O   1 
ATOM   6863 C  CB  . GLN B 1 403 ? -5.129  18.644  24.590  1.00 15.64  ? 403 GLN B CB  1 
ATOM   6864 C  CG  . GLN B 1 403 ? -6.384  17.995  25.162  1.00 17.54  ? 403 GLN B CG  1 
ATOM   6865 C  CD  . GLN B 1 403 ? -6.249  16.501  25.324  1.00 20.87  ? 403 GLN B CD  1 
ATOM   6866 O  OE1 . GLN B 1 403 ? -5.274  15.925  24.862  1.00 22.26  ? 403 GLN B OE1 1 
ATOM   6867 N  NE2 . GLN B 1 403 ? -7.266  15.866  25.905  1.00 20.65  ? 403 GLN B NE2 1 
ATOM   6868 N  N   . GLN B 1 404 ? -4.934  20.780  26.835  1.00 12.85  ? 404 GLN B N   1 
ATOM   6869 C  CA  . GLN B 1 404 ? -5.495  21.214  28.106  1.00 15.94  ? 404 GLN B CA  1 
ATOM   6870 C  C   . GLN B 1 404 ? -5.767  22.723  28.029  1.00 13.33  ? 404 GLN B C   1 
ATOM   6871 O  O   . GLN B 1 404 ? -6.698  23.220  28.620  1.00 14.13  ? 404 GLN B O   1 
ATOM   6872 C  CB  . GLN B 1 404 ? -4.580  20.791  29.261  1.00 22.05  ? 404 GLN B CB  1 
ATOM   6873 C  CG  . GLN B 1 404 ? -5.277  20.684  30.621  1.00 30.25  ? 404 GLN B CG  1 
ATOM   6874 C  CD  . GLN B 1 404 ? -4.303  20.659  31.789  1.00 39.71  ? 404 GLN B CD  1 
ATOM   6875 O  OE1 . GLN B 1 404 ? -4.511  21.294  32.831  1.00 43.28  ? 404 GLN B OE1 1 
ATOM   6876 N  NE2 . GLN B 1 404 ? -3.236  19.883  31.637  1.00 35.98  ? 404 GLN B NE2 1 
ATOM   6877 N  N   . PHE B 1 405 ? -4.952  23.463  27.273  1.00 13.79  ? 405 PHE B N   1 
ATOM   6878 C  CA  . PHE B 1 405 ? -5.190  24.885  27.055  1.00 14.24  ? 405 PHE B CA  1 
ATOM   6879 C  C   . PHE B 1 405 ? -6.566  25.047  26.405  1.00 13.60  ? 405 PHE B C   1 
ATOM   6880 O  O   . PHE B 1 405 ? -7.401  25.813  26.909  1.00 13.82  ? 405 PHE B O   1 
ATOM   6881 C  CB  . PHE B 1 405 ? -4.030  25.452  26.233  1.00 16.75  ? 405 PHE B CB  1 
ATOM   6882 C  CG  . PHE B 1 405 ? -4.055  26.946  26.010  1.00 16.65  ? 405 PHE B CG  1 
ATOM   6883 C  CD1 . PHE B 1 405 ? -4.822  27.500  25.000  1.00 19.62  ? 405 PHE B CD1 1 
ATOM   6884 C  CD2 . PHE B 1 405 ? -3.322  27.793  26.829  1.00 19.44  ? 405 PHE B CD2 1 
ATOM   6885 C  CE1 . PHE B 1 405 ? -4.873  28.873  24.799  1.00 19.22  ? 405 PHE B CE1 1 
ATOM   6886 C  CE2 . PHE B 1 405 ? -3.341  29.166  26.620  1.00 18.17  ? 405 PHE B CE2 1 
ATOM   6887 C  CZ  . PHE B 1 405 ? -4.111  29.698  25.600  1.00 21.63  ? 405 PHE B CZ  1 
ATOM   6888 N  N   . ALA B 1 406 ? -6.782  24.331  25.298  1.00 12.12  ? 406 ALA B N   1 
ATOM   6889 C  CA  . ALA B 1 406 ? -8.019  24.413  24.530  1.00 13.98  ? 406 ALA B CA  1 
ATOM   6890 C  C   . ALA B 1 406 ? -9.209  24.129  25.422  1.00 13.62  ? 406 ALA B C   1 
ATOM   6891 O  O   . ALA B 1 406 ? -10.189 24.871  25.386  1.00 16.45  ? 406 ALA B O   1 
ATOM   6892 C  CB  . ALA B 1 406 ? -8.008  23.479  23.352  1.00 15.51  ? 406 ALA B CB  1 
ATOM   6893 N  N   . LEU B 1 407 ? -9.165  23.026  26.158  1.00 14.00  ? 407 LEU B N   1 
ATOM   6894 C  CA  . LEU B 1 407 ? -10.290 22.655  26.988  1.00 14.43  ? 407 LEU B CA  1 
ATOM   6895 C  C   . LEU B 1 407 ? -10.482 23.619  28.159  1.00 14.55  ? 407 LEU B C   1 
ATOM   6896 O  O   . LEU B 1 407 ? -11.603 23.845  28.582  1.00 13.86  ? 407 LEU B O   1 
ATOM   6897 C  CB  . LEU B 1 407 ? -10.163 21.212  27.466  1.00 16.37  ? 407 LEU B CB  1 
ATOM   6898 C  CG  . LEU B 1 407 ? -10.246 20.172  26.342  1.00 18.03  ? 407 LEU B CG  1 
ATOM   6899 C  CD1 . LEU B 1 407 ? -9.938  18.781  26.827  1.00 18.28  ? 407 LEU B CD1 1 
ATOM   6900 C  CD2 . LEU B 1 407 ? -11.628 20.219  25.711  1.00 19.85  ? 407 LEU B CD2 1 
ATOM   6901 N  N   . HIS B 1 408 ? -9.423  24.242  28.682  1.00 13.47  ? 408 HIS B N   1 
ATOM   6902 C  CA  . HIS B 1 408 ? -9.636  25.156  29.790  1.00 14.57  ? 408 HIS B CA  1 
ATOM   6903 C  C   . HIS B 1 408 ? -10.337 26.421  29.286  1.00 13.24  ? 408 HIS B C   1 
ATOM   6904 O  O   . HIS B 1 408 ? -11.301 26.886  29.887  1.00 13.09  ? 408 HIS B O   1 
ATOM   6905 C  CB  . HIS B 1 408 ? -8.323  25.452  30.511  1.00 14.44  ? 408 HIS B CB  1 
ATOM   6906 C  CG  . HIS B 1 408 ? -8.507  26.266  31.732  1.00 15.74  ? 408 HIS B CG  1 
ATOM   6907 N  ND1 . HIS B 1 408 ? -8.855  25.714  32.936  1.00 16.03  ? 408 HIS B ND1 1 
ATOM   6908 C  CD2 . HIS B 1 408 ? -8.409  27.615  31.932  1.00 15.24  ? 408 HIS B CD2 1 
ATOM   6909 C  CE1 . HIS B 1 408 ? -8.943  26.686  33.834  1.00 16.68  ? 408 HIS B CE1 1 
ATOM   6910 N  NE2 . HIS B 1 408 ? -8.699  27.845  33.236  1.00 15.48  ? 408 HIS B NE2 1 
ATOM   6911 N  N   . GLU B 1 409 ? -9.841  26.979  28.173  1.00 12.67  ? 409 GLU B N   1 
ATOM   6912 C  CA  . GLU B 1 409 ? -10.404 28.166  27.552  1.00 12.78  ? 409 GLU B CA  1 
ATOM   6913 C  C   . GLU B 1 409 ? -11.878 27.923  27.238  1.00 11.99  ? 409 GLU B C   1 
ATOM   6914 O  O   . GLU B 1 409 ? -12.729 28.706  27.637  1.00 11.83  ? 409 GLU B O   1 
ATOM   6915 C  CB  . GLU B 1 409 ? -9.646  28.469  26.259  1.00 14.68  ? 409 GLU B CB  1 
ATOM   6916 C  CG  . GLU B 1 409 ? -10.032 29.776  25.593  1.00 18.10  ? 409 GLU B CG  1 
ATOM   6917 C  CD  . GLU B 1 409 ? -9.428  30.028  24.218  1.00 17.42  ? 409 GLU B CD  1 
ATOM   6918 O  OE1 . GLU B 1 409 ? -8.510  29.312  23.795  1.00 21.90  ? 409 GLU B OE1 1 
ATOM   6919 O  OE2 . GLU B 1 409 ? -9.874  30.962  23.582  1.00 25.53  ? 409 GLU B OE2 1 
ATOM   6920 N  N   . ALA B 1 410 ? -12.163 26.777  26.627  1.00 12.56  ? 410 ALA B N   1 
ATOM   6921 C  CA  . ALA B 1 410 ? -13.503 26.490  26.135  1.00 13.63  ? 410 ALA B CA  1 
ATOM   6922 C  C   . ALA B 1 410 ? -14.466 26.252  27.292  1.00 12.64  ? 410 ALA B C   1 
ATOM   6923 O  O   . ALA B 1 410 ? -15.621 26.657  27.237  1.00 12.42  ? 410 ALA B O   1 
ATOM   6924 C  CB  . ALA B 1 410 ? -13.480 25.318  25.185  1.00 12.76  ? 410 ALA B CB  1 
ATOM   6925 N  N   . THR B 1 411 ? -13.965 25.640  28.376  1.00 14.60  ? 411 THR B N   1 
ATOM   6926 C  CA  . THR B 1 411 ? -14.753 25.392  29.557  1.00 14.27  ? 411 THR B CA  1 
ATOM   6927 C  C   . THR B 1 411 ? -15.033 26.702  30.285  1.00 13.86  ? 411 THR B C   1 
ATOM   6928 O  O   . THR B 1 411 ? -16.175 26.943  30.645  1.00 11.55  ? 411 THR B O   1 
ATOM   6929 C  CB  . THR B 1 411 ? -14.109 24.369  30.500  1.00 14.54  ? 411 THR B CB  1 
ATOM   6930 O  OG1 . THR B 1 411 ? -13.776 23.171  29.788  1.00 16.46  ? 411 THR B OG1 1 
ATOM   6931 C  CG2 . THR B 1 411 ? -15.000 24.070  31.678  1.00 13.98  ? 411 THR B CG2 1 
ATOM   6932 N  N   . LEU B 1 412 ? -14.006 27.552  30.443  1.00 13.17  ? 412 LEU B N   1 
ATOM   6933 C  CA  . LEU B 1 412 ? -14.195 28.866  31.037  1.00 14.01  ? 412 LEU B CA  1 
ATOM   6934 C  C   . LEU B 1 412 ? -15.264 29.636  30.268  1.00 14.28  ? 412 LEU B C   1 
ATOM   6935 O  O   . LEU B 1 412 ? -16.174 30.211  30.869  1.00 14.97  ? 412 LEU B O   1 
ATOM   6936 C  CB  . LEU B 1 412 ? -12.868 29.648  31.019  1.00 15.22  ? 412 LEU B CB  1 
ATOM   6937 C  CG  . LEU B 1 412 ? -12.979 31.105  31.447  1.00 16.69  ? 412 LEU B CG  1 
ATOM   6938 C  CD1 . LEU B 1 412 ? -13.306 31.174  32.903  1.00 17.60  ? 412 LEU B CD1 1 
ATOM   6939 C  CD2 . LEU B 1 412 ? -11.694 31.863  31.193  1.00 20.91  ? 412 LEU B CD2 1 
ATOM   6940 N  N   . VAL B 1 413 ? -15.130 29.691  28.943  1.00 15.61  ? 413 VAL B N   1 
ATOM   6941 C  CA  . VAL B 1 413 ? -15.934 30.633  28.182  1.00 17.91  ? 413 VAL B CA  1 
ATOM   6942 C  C   . VAL B 1 413 ? -17.382 30.150  28.168  1.00 17.96  ? 413 VAL B C   1 
ATOM   6943 O  O   . VAL B 1 413 ? -18.311 30.935  28.324  1.00 16.93  ? 413 VAL B O   1 
ATOM   6944 C  CB  . VAL B 1 413 ? -15.402 30.804  26.748  1.00 20.37  ? 413 VAL B CB  1 
ATOM   6945 C  CG1 . VAL B 1 413 ? -16.336 31.678  25.929  1.00 24.41  ? 413 VAL B CG1 1 
ATOM   6946 C  CG2 . VAL B 1 413 ? -13.977 31.348  26.707  1.00 21.33  ? 413 VAL B CG2 1 
ATOM   6947 N  N   . LEU B 1 414 ? -17.561 28.852  27.936  1.00 15.76  ? 414 LEU B N   1 
ATOM   6948 C  CA  . LEU B 1 414 ? -18.899 28.293  27.802  1.00 15.79  ? 414 LEU B CA  1 
ATOM   6949 C  C   . LEU B 1 414 ? -19.614 28.393  29.139  1.00 14.59  ? 414 LEU B C   1 
ATOM   6950 O  O   . LEU B 1 414 ? -20.804 28.695  29.218  1.00 13.44  ? 414 LEU B O   1 
ATOM   6951 C  CB  . LEU B 1 414 ? -18.754 26.841  27.330  1.00 16.52  ? 414 LEU B CB  1 
ATOM   6952 C  CG  . LEU B 1 414 ? -20.052 26.152  26.953  1.00 17.13  ? 414 LEU B CG  1 
ATOM   6953 C  CD1 . LEU B 1 414 ? -20.856 27.016  25.982  1.00 15.95  ? 414 LEU B CD1 1 
ATOM   6954 C  CD2 . LEU B 1 414 ? -19.768 24.790  26.367  1.00 18.15  ? 414 LEU B CD2 1 
ATOM   6955 N  N   . GLY B 1 415 ? -18.869 28.119  30.220  1.00 14.98  ? 415 GLY B N   1 
ATOM   6956 C  CA  . GLY B 1 415 ? -19.410 28.284  31.550  1.00 14.13  ? 415 GLY B CA  1 
ATOM   6957 C  C   . GLY B 1 415 ? -19.930 29.703  31.775  1.00 14.33  ? 415 GLY B C   1 
ATOM   6958 O  O   . GLY B 1 415 ? -21.042 29.904  32.289  1.00 13.78  ? 415 GLY B O   1 
ATOM   6959 N  N   . MET B 1 416 ? -19.118 30.697  31.410  1.00 15.19  ? 416 MET B N   1 
ATOM   6960 C  CA  . MET B 1 416 ? -19.550 32.068  31.616  1.00 14.88  ? 416 MET B CA  1 
ATOM   6961 C  C   . MET B 1 416 ? -20.763 32.350  30.734  1.00 14.14  ? 416 MET B C   1 
ATOM   6962 O  O   . MET B 1 416 ? -21.668 33.048  31.162  1.00 12.64  ? 416 MET B O   1 
ATOM   6963 C  CB  . MET B 1 416 ? -18.428 33.067  31.335  1.00 17.09  ? 416 MET B CB  1 
ATOM   6964 C  CG  . MET B 1 416 ? -17.398 33.010  32.440  1.00 19.18  ? 416 MET B CG  1 
ATOM   6965 S  SD  . MET B 1 416 ? -15.964 34.028  32.024  1.00 23.42  ? 416 MET B SD  1 
ATOM   6966 C  CE  . MET B 1 416 ? -16.623 35.599  32.597  1.00 20.12  ? 416 MET B CE  1 
ATOM   6967 N  N   . MET B 1 417 ? -20.749 31.840  29.495  1.00 15.39  ? 417 MET B N   1 
ATOM   6968 C  CA  . MET B 1 417 ? -21.845 32.081  28.563  1.00 17.19  ? 417 MET B CA  1 
ATOM   6969 C  C   . MET B 1 417 ? -23.152 31.552  29.161  1.00 16.70  ? 417 MET B C   1 
ATOM   6970 O  O   . MET B 1 417 ? -24.162 32.255  29.188  1.00 19.45  ? 417 MET B O   1 
ATOM   6971 C  CB  . MET B 1 417 ? -21.564 31.420  27.208  1.00 15.97  ? 417 MET B CB  1 
ATOM   6972 C  CG  . MET B 1 417 ? -20.613 32.184  26.348  1.00 19.41  ? 417 MET B CG  1 
ATOM   6973 S  SD  . MET B 1 417 ? -19.988 31.235  24.924  1.00 21.62  ? 417 MET B SD  1 
ATOM   6974 C  CE  . MET B 1 417 ? -21.504 30.474  24.336  1.00 21.86  ? 417 MET B CE  1 
ATOM   6975 N  N   . LEU B 1 418 ? -23.130 30.322  29.698  1.00 15.65  ? 418 LEU B N   1 
ATOM   6976 C  CA  . LEU B 1 418 ? -24.312 29.718  30.296  1.00 14.78  ? 418 LEU B CA  1 
ATOM   6977 C  C   . LEU B 1 418 ? -24.702 30.409  31.607  1.00 15.23  ? 418 LEU B C   1 
ATOM   6978 O  O   . LEU B 1 418 ? -25.868 30.434  31.958  1.00 18.04  ? 418 LEU B O   1 
ATOM   6979 C  CB  . LEU B 1 418 ? -24.041 28.230  30.558  1.00 16.42  ? 418 LEU B CB  1 
ATOM   6980 C  CG  . LEU B 1 418 ? -23.672 27.415  29.310  1.00 16.62  ? 418 LEU B CG  1 
ATOM   6981 C  CD1 . LEU B 1 418 ? -23.299 25.986  29.664  1.00 17.85  ? 418 LEU B CD1 1 
ATOM   6982 C  CD2 . LEU B 1 418 ? -24.793 27.449  28.303  1.00 20.10  ? 418 LEU B CD2 1 
ATOM   6983 N  N   . LYS B 1 419 ? -23.756 30.944  32.382  1.00 14.00  ? 419 LYS B N   1 
ATOM   6984 C  CA  . LYS B 1 419 ? -24.154 31.666  33.583  1.00 15.51  ? 419 LYS B CA  1 
ATOM   6985 C  C   . LYS B 1 419 ? -24.886 32.996  33.286  1.00 15.08  ? 419 LYS B C   1 
ATOM   6986 O  O   . LYS B 1 419 ? -25.820 33.373  34.005  1.00 16.30  ? 419 LYS B O   1 
ATOM   6987 C  CB  . LYS B 1 419 ? -22.912 31.962  34.416  1.00 15.59  ? 419 LYS B CB  1 
ATOM   6988 C  CG  . LYS B 1 419 ? -23.171 32.788  35.673  1.00 17.53  ? 419 LYS B CG  1 
ATOM   6989 C  CD  . LYS B 1 419 ? -21.894 33.151  36.370  1.00 17.85  ? 419 LYS B CD  1 
ATOM   6990 C  CE  . LYS B 1 419 ? -22.108 34.100  37.520  1.00 19.56  ? 419 LYS B CE  1 
ATOM   6991 N  NZ  . LYS B 1 419 ? -20.855 34.294  38.279  1.00 22.24  ? 419 LYS B NZ  1 
ATOM   6992 N  N   . HIS B 1 420 ? -24.533 33.654  32.183  1.00 14.21  ? 420 HIS B N   1 
ATOM   6993 C  CA  . HIS B 1 420 ? -24.886 35.045  31.947  1.00 15.15  ? 420 HIS B CA  1 
ATOM   6994 C  C   . HIS B 1 420 ? -26.089 35.251  31.016  1.00 14.77  ? 420 HIS B C   1 
ATOM   6995 O  O   . HIS B 1 420 ? -26.697 36.305  31.083  1.00 14.82  ? 420 HIS B O   1 
ATOM   6996 C  CB  . HIS B 1 420 ? -23.648 35.810  31.494  1.00 16.17  ? 420 HIS B CB  1 
ATOM   6997 C  CG  . HIS B 1 420 ? -22.786 36.095  32.662  1.00 16.42  ? 420 HIS B CG  1 
ATOM   6998 N  ND1 . HIS B 1 420 ? -23.194 37.012  33.606  1.00 20.82  ? 420 HIS B ND1 1 
ATOM   6999 C  CD2 . HIS B 1 420 ? -21.608 35.632  33.077  1.00 18.24  ? 420 HIS B CD2 1 
ATOM   7000 C  CE1 . HIS B 1 420 ? -22.266 37.089  34.557  1.00 21.51  ? 420 HIS B CE1 1 
ATOM   7001 N  NE2 . HIS B 1 420 ? -21.302 36.259  34.259  1.00 19.86  ? 420 HIS B NE2 1 
ATOM   7002 N  N   . PHE B 1 421 ? -26.354 34.311  30.104  1.00 14.63  ? 421 PHE B N   1 
ATOM   7003 C  CA  . PHE B 1 421 ? -27.390 34.438  29.093  1.00 13.92  ? 421 PHE B CA  1 
ATOM   7004 C  C   . PHE B 1 421 ? -28.229 33.175  28.910  1.00 15.73  ? 421 PHE B C   1 
ATOM   7005 O  O   . PHE B 1 421 ? -27.766 32.033  29.056  1.00 15.10  ? 421 PHE B O   1 
ATOM   7006 C  CB  . PHE B 1 421 ? -26.777 34.715  27.715  1.00 15.03  ? 421 PHE B CB  1 
ATOM   7007 C  CG  . PHE B 1 421 ? -25.858 35.913  27.674  1.00 15.58  ? 421 PHE B CG  1 
ATOM   7008 C  CD1 . PHE B 1 421 ? -26.349 37.189  27.462  1.00 16.94  ? 421 PHE B CD1 1 
ATOM   7009 C  CD2 . PHE B 1 421 ? -24.503 35.760  27.901  1.00 16.66  ? 421 PHE B CD2 1 
ATOM   7010 C  CE1 . PHE B 1 421 ? -25.487 38.269  27.447  1.00 18.23  ? 421 PHE B CE1 1 
ATOM   7011 C  CE2 . PHE B 1 421 ? -23.636 36.841  27.863  1.00 17.38  ? 421 PHE B CE2 1 
ATOM   7012 C  CZ  . PHE B 1 421 ? -24.133 38.094  27.615  1.00 17.00  ? 421 PHE B CZ  1 
ATOM   7013 N  N   . ASP B 1 422 ? -29.447 33.422  28.436  1.00 16.05  ? 422 ASP B N   1 
ATOM   7014 C  CA  . ASP B 1 422 ? -30.295 32.386  27.870  1.00 19.91  ? 422 ASP B CA  1 
ATOM   7015 C  C   . ASP B 1 422 ? -30.163 32.483  26.361  1.00 20.31  ? 422 ASP B C   1 
ATOM   7016 O  O   . ASP B 1 422 ? -30.051 33.595  25.833  1.00 21.92  ? 422 ASP B O   1 
ATOM   7017 C  CB  . ASP B 1 422 ? -31.756 32.578  28.278  1.00 24.99  ? 422 ASP B CB  1 
ATOM   7018 C  CG  . ASP B 1 422 ? -32.012 32.278  29.742  1.00 28.86  ? 422 ASP B CG  1 
ATOM   7019 O  OD1 . ASP B 1 422 ? -31.721 31.121  30.166  1.00 36.31  ? 422 ASP B OD1 1 
ATOM   7020 O  OD2 . ASP B 1 422 ? -32.480 33.188  30.444  1.00 32.84  ? 422 ASP B OD2 1 
ATOM   7021 N  N   . PHE B 1 423 ? -30.173 31.337  25.675  1.00 17.52  ? 423 PHE B N   1 
ATOM   7022 C  CA  . PHE B 1 423 ? -29.905 31.298  24.240  1.00 18.61  ? 423 PHE B CA  1 
ATOM   7023 C  C   . PHE B 1 423 ? -31.135 30.841  23.443  1.00 20.99  ? 423 PHE B C   1 
ATOM   7024 O  O   . PHE B 1 423 ? -31.870 29.960  23.871  1.00 19.72  ? 423 PHE B O   1 
ATOM   7025 C  CB  . PHE B 1 423 ? -28.682 30.409  23.995  1.00 19.78  ? 423 PHE B CB  1 
ATOM   7026 C  CG  . PHE B 1 423 ? -27.397 31.050  24.454  1.00 19.52  ? 423 PHE B CG  1 
ATOM   7027 C  CD1 . PHE B 1 423 ? -26.819 32.067  23.715  1.00 20.02  ? 423 PHE B CD1 1 
ATOM   7028 C  CD2 . PHE B 1 423 ? -26.771 30.632  25.610  1.00 21.37  ? 423 PHE B CD2 1 
ATOM   7029 C  CE1 . PHE B 1 423 ? -25.649 32.693  24.128  1.00 20.52  ? 423 PHE B CE1 1 
ATOM   7030 C  CE2 . PHE B 1 423 ? -25.588 31.234  26.014  1.00 22.81  ? 423 PHE B CE2 1 
ATOM   7031 C  CZ  . PHE B 1 423 ? -25.026 32.268  25.274  1.00 22.83  ? 423 PHE B CZ  1 
ATOM   7032 N  N   . GLU B 1 424 ? -31.341 31.456  22.271  1.00 20.57  ? 424 GLU B N   1 
ATOM   7033 C  CA  . GLU B 1 424 ? -32.420 31.093  21.370  1.00 21.07  ? 424 GLU B CA  1 
ATOM   7034 C  C   . GLU B 1 424 ? -31.876 30.902  19.959  1.00 21.32  ? 424 GLU B C   1 
ATOM   7035 O  O   . GLU B 1 424 ? -31.193 31.786  19.420  1.00 21.47  ? 424 GLU B O   1 
ATOM   7036 C  CB  . GLU B 1 424 ? -33.493 32.180  21.379  1.00 24.28  ? 424 GLU B CB  1 
ATOM   7037 C  CG  . GLU B 1 424 ? -34.704 31.877  20.528  1.00 26.41  ? 424 GLU B CG  1 
ATOM   7038 C  CD  . GLU B 1 424 ? -35.638 33.076  20.395  1.00 30.22  ? 424 GLU B CD  1 
ATOM   7039 O  OE1 . GLU B 1 424 ? -35.348 34.129  21.002  1.00 32.34  ? 424 GLU B OE1 1 
ATOM   7040 O  OE2 . GLU B 1 424 ? -36.645 32.968  19.665  1.00 33.90  ? 424 GLU B OE2 1 
ATOM   7041 N  N   . ASP B 1 425 ? -32.191 29.719  19.401  1.00 20.17  ? 425 ASP B N   1 
ATOM   7042 C  CA  . ASP B 1 425 ? -31.965 29.371  18.007  1.00 19.41  ? 425 ASP B CA  1 
ATOM   7043 C  C   . ASP B 1 425 ? -33.122 29.927  17.167  1.00 21.76  ? 425 ASP B C   1 
ATOM   7044 O  O   . ASP B 1 425 ? -34.057 29.200  16.823  1.00 19.04  ? 425 ASP B O   1 
ATOM   7045 C  CB  . ASP B 1 425 ? -31.858 27.837  17.866  1.00 19.16  ? 425 ASP B CB  1 
ATOM   7046 C  CG  . ASP B 1 425 ? -31.788 27.370  16.425  1.00 19.43  ? 425 ASP B CG  1 
ATOM   7047 O  OD1 . ASP B 1 425 ? -31.340 28.151  15.522  1.00 18.68  ? 425 ASP B OD1 1 
ATOM   7048 O  OD2 . ASP B 1 425 ? -32.227 26.244  16.199  1.00 26.05  ? 425 ASP B OD2 1 
ATOM   7049 N  N   . HIS B 1 426 ? -33.032 31.224  16.842  1.00 19.51  ? 426 HIS B N   1 
ATOM   7050 C  CA  . HIS B 1 426 ? -34.160 32.019  16.406  1.00 24.10  ? 426 HIS B CA  1 
ATOM   7051 C  C   . HIS B 1 426 ? -34.401 31.843  14.907  1.00 21.09  ? 426 HIS B C   1 
ATOM   7052 O  O   . HIS B 1 426 ? -35.491 32.134  14.432  1.00 21.52  ? 426 HIS B O   1 
ATOM   7053 C  CB  . HIS B 1 426 ? -33.958 33.489  16.828  1.00 25.76  ? 426 HIS B CB  1 
ATOM   7054 C  CG  . HIS B 1 426 ? -32.862 34.153  16.100  1.00 25.58  ? 426 HIS B CG  1 
ATOM   7055 N  ND1 . HIS B 1 426 ? -31.533 33.801  16.241  1.00 25.27  ? 426 HIS B ND1 1 
ATOM   7056 C  CD2 . HIS B 1 426 ? -32.902 35.145  15.194  1.00 26.53  ? 426 HIS B CD2 1 
ATOM   7057 C  CE1 . HIS B 1 426 ? -30.813 34.567  15.442  1.00 24.95  ? 426 HIS B CE1 1 
ATOM   7058 N  NE2 . HIS B 1 426 ? -31.630 35.385  14.797  1.00 25.04  ? 426 HIS B NE2 1 
ATOM   7059 N  N   . THR B 1 427 ? -33.400 31.376  14.165  1.00 22.92  ? 427 THR B N   1 
ATOM   7060 C  CA  . THR B 1 427 ? -33.552 31.072  12.752  1.00 22.89  ? 427 THR B CA  1 
ATOM   7061 C  C   . THR B 1 427 ? -33.799 29.580  12.497  1.00 24.34  ? 427 THR B C   1 
ATOM   7062 O  O   . THR B 1 427 ? -33.936 29.182  11.344  1.00 23.29  ? 427 THR B O   1 
ATOM   7063 C  CB  . THR B 1 427 ? -32.300 31.486  11.961  1.00 24.79  ? 427 THR B CB  1 
ATOM   7064 O  OG1 . THR B 1 427 ? -31.201 30.592  12.213  1.00 23.55  ? 427 THR B OG1 1 
ATOM   7065 C  CG2 . THR B 1 427 ? -31.855 32.897  12.279  1.00 22.77  ? 427 THR B CG2 1 
ATOM   7066 N  N   . ASN B 1 428 ? -33.790 28.731  13.536  1.00 22.77  ? 428 ASN B N   1 
ATOM   7067 C  CA  . ASN B 1 428 ? -33.811 27.288  13.314  1.00 24.70  ? 428 ASN B CA  1 
ATOM   7068 C  C   . ASN B 1 428 ? -32.689 26.923  12.340  1.00 23.45  ? 428 ASN B C   1 
ATOM   7069 O  O   . ASN B 1 428 ? -32.895 26.442  11.221  1.00 21.77  ? 428 ASN B O   1 
ATOM   7070 C  CB  . ASN B 1 428 ? -35.203 26.840  12.851  1.00 29.48  ? 428 ASN B CB  1 
ATOM   7071 C  CG  . ASN B 1 428 ? -35.465 25.358  13.018  1.00 34.35  ? 428 ASN B CG  1 
ATOM   7072 O  OD1 . ASN B 1 428 ? -34.621 24.606  13.490  1.00 38.72  ? 428 ASN B OD1 1 
ATOM   7073 N  ND2 . ASN B 1 428 ? -36.644 24.923  12.623  1.00 39.48  ? 428 ASN B ND2 1 
ATOM   7074 N  N   . TYR B 1 429 ? -31.462 27.237  12.751  1.00 17.39  ? 429 TYR B N   1 
ATOM   7075 C  CA  . TYR B 1 429 ? -30.323 27.105  11.883  1.00 17.56  ? 429 TYR B CA  1 
ATOM   7076 C  C   . TYR B 1 429 ? -30.130 25.634  11.455  1.00 17.99  ? 429 TYR B C   1 
ATOM   7077 O  O   . TYR B 1 429 ? -30.196 24.708  12.264  1.00 17.70  ? 429 TYR B O   1 
ATOM   7078 C  CB  . TYR B 1 429 ? -29.136 27.658  12.665  1.00 16.67  ? 429 TYR B CB  1 
ATOM   7079 C  CG  . TYR B 1 429 ? -27.798 27.283  12.035  1.00 16.22  ? 429 TYR B CG  1 
ATOM   7080 C  CD1 . TYR B 1 429 ? -27.328 27.915  10.893  1.00 16.86  ? 429 TYR B CD1 1 
ATOM   7081 C  CD2 . TYR B 1 429 ? -26.977 26.349  12.637  1.00 16.26  ? 429 TYR B CD2 1 
ATOM   7082 C  CE1 . TYR B 1 429 ? -26.093 27.623  10.349  1.00 18.79  ? 429 TYR B CE1 1 
ATOM   7083 C  CE2 . TYR B 1 429 ? -25.762 26.011  12.081  1.00 17.13  ? 429 TYR B CE2 1 
ATOM   7084 C  CZ  . TYR B 1 429 ? -25.317 26.643  10.937  1.00 17.56  ? 429 TYR B CZ  1 
ATOM   7085 O  OH  . TYR B 1 429 ? -24.133 26.253  10.401  1.00 18.21  ? 429 TYR B OH  1 
ATOM   7086 N  N   . GLU B 1 430 ? -29.912 25.469  10.145  1.00 18.12  ? 430 GLU B N   1 
ATOM   7087 C  CA  . GLU B 1 430 ? -29.568 24.216  9.500   1.00 24.56  ? 430 GLU B CA  1 
ATOM   7088 C  C   . GLU B 1 430 ? -28.047 24.122  9.453   1.00 22.65  ? 430 GLU B C   1 
ATOM   7089 O  O   . GLU B 1 430 ? -27.376 24.980  8.883   1.00 20.96  ? 430 GLU B O   1 
ATOM   7090 C  CB  . GLU B 1 430 ? -30.145 24.172  8.079   1.00 30.50  ? 430 GLU B CB  1 
ATOM   7091 C  CG  . GLU B 1 430 ? -29.958 22.830  7.368   1.00 36.08  ? 430 GLU B CG  1 
ATOM   7092 C  CD  . GLU B 1 430 ? -30.874 22.540  6.180   1.00 42.64  ? 430 GLU B CD  1 
ATOM   7093 O  OE1 . GLU B 1 430 ? -31.886 23.267  5.977   1.00 45.13  ? 430 GLU B OE1 1 
ATOM   7094 O  OE2 . GLU B 1 430 ? -30.583 21.577  5.458   1.00 45.90  ? 430 GLU B OE2 1 
ATOM   7095 N  N   . LEU B 1 431 ? -27.515 23.100  10.111  1.00 23.56  ? 431 LEU B N   1 
ATOM   7096 C  CA  . LEU B 1 431 ? -26.073 22.995  10.250  1.00 23.38  ? 431 LEU B CA  1 
ATOM   7097 C  C   . LEU B 1 431 ? -25.446 22.962  8.868   1.00 23.74  ? 431 LEU B C   1 
ATOM   7098 O  O   . LEU B 1 431 ? -25.824 22.145  8.039   1.00 22.81  ? 431 LEU B O   1 
ATOM   7099 C  CB  . LEU B 1 431 ? -25.733 21.728  11.035  1.00 22.99  ? 431 LEU B CB  1 
ATOM   7100 C  CG  . LEU B 1 431 ? -24.252 21.506  11.347  1.00 25.32  ? 431 LEU B CG  1 
ATOM   7101 C  CD1 . LEU B 1 431 ? -23.638 22.701  12.084  1.00 22.67  ? 431 LEU B CD1 1 
ATOM   7102 C  CD2 . LEU B 1 431 ? -24.099 20.236  12.187  1.00 25.67  ? 431 LEU B CD2 1 
ATOM   7103 N  N   . ASP B 1 432 ? -24.490 23.872  8.646   1.00 21.44  ? 432 ASP B N   1 
ATOM   7104 C  CA  . ASP B 1 432 ? -23.707 23.911  7.431   1.00 24.15  ? 432 ASP B CA  1 
ATOM   7105 C  C   . ASP B 1 432 ? -22.225 24.011  7.807   1.00 20.87  ? 432 ASP B C   1 
ATOM   7106 O  O   . ASP B 1 432 ? -21.782 25.013  8.369   1.00 22.16  ? 432 ASP B O   1 
ATOM   7107 C  CB  . ASP B 1 432 ? -24.193 25.075  6.583   1.00 27.23  ? 432 ASP B CB  1 
ATOM   7108 C  CG  . ASP B 1 432 ? -23.422 25.269  5.304   1.00 30.66  ? 432 ASP B CG  1 
ATOM   7109 O  OD1 . ASP B 1 432 ? -22.404 24.593  5.123   1.00 31.78  ? 432 ASP B OD1 1 
ATOM   7110 O  OD2 . ASP B 1 432 ? -23.858 26.090  4.512   1.00 36.49  ? 432 ASP B OD2 1 
ATOM   7111 N  N   . ILE B 1 433 ? -21.464 22.967  7.483   1.00 20.84  ? 433 ILE B N   1 
ATOM   7112 C  CA  . ILE B 1 433 ? -20.112 22.839  7.987   1.00 20.65  ? 433 ILE B CA  1 
ATOM   7113 C  C   . ILE B 1 433 ? -19.135 23.275  6.918   1.00 22.19  ? 433 ILE B C   1 
ATOM   7114 O  O   . ILE B 1 433 ? -18.959 22.581  5.907   1.00 23.89  ? 433 ILE B O   1 
ATOM   7115 C  CB  . ILE B 1 433 ? -19.831 21.409  8.469   1.00 20.20  ? 433 ILE B CB  1 
ATOM   7116 C  CG1 . ILE B 1 433 ? -20.722 21.090  9.667   1.00 20.69  ? 433 ILE B CG1 1 
ATOM   7117 C  CG2 . ILE B 1 433 ? -18.343 21.223  8.792   1.00 20.77  ? 433 ILE B CG2 1 
ATOM   7118 C  CD1 . ILE B 1 433 ? -20.709 19.661  10.071  1.00 21.11  ? 433 ILE B CD1 1 
ATOM   7119 N  N   . LYS B 1 434 ? -18.466 24.400  7.186   1.00 18.85  ? 434 LYS B N   1 
ATOM   7120 C  CA  . LYS B 1 434 ? -17.427 24.872  6.293   1.00 19.21  ? 434 LYS B CA  1 
ATOM   7121 C  C   . LYS B 1 434 ? -16.141 24.108  6.581   1.00 18.22  ? 434 LYS B C   1 
ATOM   7122 O  O   . LYS B 1 434 ? -15.764 23.901  7.737   1.00 18.18  ? 434 LYS B O   1 
ATOM   7123 C  CB  . LYS B 1 434 ? -17.205 26.383  6.462   1.00 19.58  ? 434 LYS B CB  1 
ATOM   7124 C  CG  . LYS B 1 434 ? -16.219 27.017  5.492   1.00 23.18  ? 434 LYS B CG  1 
ATOM   7125 C  CD  . LYS B 1 434 ? -16.325 28.531  5.438   1.00 27.75  ? 434 LYS B CD  1 
ATOM   7126 C  CE  . LYS B 1 434 ? -15.444 29.193  4.390   1.00 30.94  ? 434 LYS B CE  1 
ATOM   7127 N  NZ  . LYS B 1 434 ? -14.008 29.132  4.755   1.00 35.75  ? 434 LYS B NZ  1 
ATOM   7128 N  N   . GLU B 1 435 ? -15.448 23.740  5.516   1.00 18.80  ? 435 GLU B N   1 
ATOM   7129 C  CA  . GLU B 1 435 ? -14.174 23.078  5.680   1.00 20.07  ? 435 GLU B CA  1 
ATOM   7130 C  C   . GLU B 1 435 ? -13.051 23.952  5.154   1.00 22.38  ? 435 GLU B C   1 
ATOM   7131 O  O   . GLU B 1 435 ? -13.072 24.415  4.024   1.00 24.19  ? 435 GLU B O   1 
ATOM   7132 C  CB  . GLU B 1 435 ? -14.143 21.790  4.898   1.00 19.56  ? 435 GLU B CB  1 
ATOM   7133 C  CG  . GLU B 1 435 ? -15.298 20.901  5.242   1.00 22.54  ? 435 GLU B CG  1 
ATOM   7134 C  CD  . GLU B 1 435 ? -15.056 19.471  4.806   1.00 21.47  ? 435 GLU B CD  1 
ATOM   7135 O  OE1 . GLU B 1 435 ? -13.870 19.174  4.443   1.00 21.42  ? 435 GLU B OE1 1 
ATOM   7136 O  OE2 . GLU B 1 435 ? -16.041 18.659  4.863   1.00 22.89  ? 435 GLU B OE2 1 
ATOM   7137 N  N   . THR B 1 436 ? -12.046 24.098  5.993   1.00 25.37  ? 436 THR B N   1 
ATOM   7138 C  CA  . THR B 1 436 ? -10.768 24.665  5.628   1.00 27.50  ? 436 THR B CA  1 
ATOM   7139 C  C   . THR B 1 436 ? -9.846  23.456  5.800   1.00 33.53  ? 436 THR B C   1 
ATOM   7140 O  O   . THR B 1 436 ? -10.159 22.382  5.292   1.00 38.44  ? 436 THR B O   1 
ATOM   7141 C  CB  . THR B 1 436 ? -10.643 26.008  6.371   1.00 26.77  ? 436 THR B CB  1 
ATOM   7142 O  OG1 . THR B 1 436 ? -10.822 25.897  7.784   1.00 27.77  ? 436 THR B OG1 1 
ATOM   7143 C  CG2 . THR B 1 436 ? -11.734 26.966  5.927   1.00 24.95  ? 436 THR B CG2 1 
ATOM   7144 N  N   . LEU B 1 437 ? -8.761  23.556  6.551   1.00 32.57  ? 437 LEU B N   1 
ATOM   7145 C  CA  . LEU B 1 437 ? -8.164  22.324  7.032   1.00 32.53  ? 437 LEU B CA  1 
ATOM   7146 C  C   . LEU B 1 437 ? -8.914  21.890  8.290   1.00 30.00  ? 437 LEU B C   1 
ATOM   7147 O  O   . LEU B 1 437 ? -8.767  20.766  8.756   1.00 40.50  ? 437 LEU B O   1 
ATOM   7148 C  CB  . LEU B 1 437 ? -6.676  22.557  7.302   1.00 34.53  ? 437 LEU B CB  1 
ATOM   7149 C  CG  . LEU B 1 437 ? -5.821  22.908  6.087   1.00 34.14  ? 437 LEU B CG  1 
ATOM   7150 C  CD1 . LEU B 1 437 ? -4.372  22.626  6.404   1.00 37.47  ? 437 LEU B CD1 1 
ATOM   7151 C  CD2 . LEU B 1 437 ? -6.254  22.158  4.834   1.00 36.44  ? 437 LEU B CD2 1 
ATOM   7152 N  N   . THR B 1 438 ? -9.746  22.792  8.807   1.00 24.90  ? 438 THR B N   1 
ATOM   7153 C  CA  . THR B 1 438 ? -10.489 22.607  10.035  1.00 24.41  ? 438 THR B CA  1 
ATOM   7154 C  C   . THR B 1 438 ? -11.979 22.689  9.709   1.00 19.92  ? 438 THR B C   1 
ATOM   7155 O  O   . THR B 1 438 ? -12.349 23.030  8.592   1.00 19.54  ? 438 THR B O   1 
ATOM   7156 C  CB  . THR B 1 438 ? -9.988  23.645  11.051  1.00 26.80  ? 438 THR B CB  1 
ATOM   7157 O  OG1 . THR B 1 438 ? -10.258 24.934  10.501  1.00 28.82  ? 438 THR B OG1 1 
ATOM   7158 C  CG2 . THR B 1 438 ? -8.499  23.537  11.341  1.00 26.83  ? 438 THR B CG2 1 
ATOM   7159 N  N   . LEU B 1 439 ? -12.832 22.341  10.673  1.00 19.47  ? 439 LEU B N   1 
ATOM   7160 C  CA  . LEU B 1 439 ? -14.281 22.345  10.495  1.00 17.86  ? 439 LEU B CA  1 
ATOM   7161 C  C   . LEU B 1 439 ? -14.903 23.410  11.385  1.00 18.70  ? 439 LEU B C   1 
ATOM   7162 O  O   . LEU B 1 439 ? -14.533 23.507  12.565  1.00 18.38  ? 439 LEU B O   1 
ATOM   7163 C  CB  . LEU B 1 439 ? -14.853 20.998  10.941  1.00 16.88  ? 439 LEU B CB  1 
ATOM   7164 C  CG  . LEU B 1 439 ? -14.417 19.741  10.189  1.00 17.40  ? 439 LEU B CG  1 
ATOM   7165 C  CD1 . LEU B 1 439 ? -15.319 18.591  10.569  1.00 17.04  ? 439 LEU B CD1 1 
ATOM   7166 C  CD2 . LEU B 1 439 ? -14.453 19.936  8.687   1.00 17.38  ? 439 LEU B CD2 1 
ATOM   7167 N  N   . LYS B 1 440 ? -15.927 24.096  10.873  1.00 16.43  ? 440 LYS B N   1 
ATOM   7168 C  CA  . LYS B 1 440 ? -16.637 25.085  11.661  1.00 21.32  ? 440 LYS B CA  1 
ATOM   7169 C  C   . LYS B 1 440 ? -18.075 25.215  11.166  1.00 18.89  ? 440 LYS B C   1 
ATOM   7170 O  O   . LYS B 1 440 ? -18.310 25.075  9.985   1.00 18.68  ? 440 LYS B O   1 
ATOM   7171 C  CB  . LYS B 1 440 ? -15.944 26.451  11.550  1.00 25.21  ? 440 LYS B CB  1 
ATOM   7172 C  CG  . LYS B 1 440 ? -16.178 27.363  12.749  1.00 32.53  ? 440 LYS B CG  1 
ATOM   7173 C  CD  . LYS B 1 440 ? -15.236 28.582  12.810  1.00 37.10  ? 440 LYS B CD  1 
ATOM   7174 C  CE  . LYS B 1 440 ? -13.769 28.238  13.007  1.00 40.57  ? 440 LYS B CE  1 
ATOM   7175 N  NZ  . LYS B 1 440 ? -12.932 29.466  13.017  1.00 40.53  ? 440 LYS B NZ  1 
ATOM   7176 N  N   . PRO B 1 441 ? -19.071 25.501  12.020  1.00 18.70  ? 441 PRO B N   1 
ATOM   7177 C  CA  . PRO B 1 441 ? -20.385 25.917  11.525  1.00 19.16  ? 441 PRO B CA  1 
ATOM   7178 C  C   . PRO B 1 441 ? -20.224 27.242  10.772  1.00 24.10  ? 441 PRO B C   1 
ATOM   7179 O  O   . PRO B 1 441 ? -19.353 28.058  11.100  1.00 26.00  ? 441 PRO B O   1 
ATOM   7180 C  CB  . PRO B 1 441 ? -21.271 26.006  12.776  1.00 19.05  ? 441 PRO B CB  1 
ATOM   7181 C  CG  . PRO B 1 441 ? -20.483 25.357  13.872  1.00 19.35  ? 441 PRO B CG  1 
ATOM   7182 C  CD  . PRO B 1 441 ? -19.020 25.433  13.486  1.00 19.71  ? 441 PRO B CD  1 
ATOM   7183 N  N   . GLU B 1 442 ? -20.947 27.378  9.657   1.00 23.23  ? 442 GLU B N   1 
ATOM   7184 C  CA  . GLU B 1 442 ? -20.983 28.616  8.902   1.00 23.90  ? 442 GLU B CA  1 
ATOM   7185 C  C   . GLU B 1 442 ? -22.402 29.161  9.018   1.00 22.32  ? 442 GLU B C   1 
ATOM   7186 O  O   . GLU B 1 442 ? -23.357 28.411  8.903   1.00 19.93  ? 442 GLU B O   1 
ATOM   7187 C  CB  . GLU B 1 442 ? -20.593 28.396  7.439   1.00 27.11  ? 442 GLU B CB  1 
ATOM   7188 C  CG  . GLU B 1 442 ? -20.428 29.681  6.653   1.00 32.65  ? 442 GLU B CG  1 
ATOM   7189 C  CD  . GLU B 1 442 ? -20.112 29.502  5.173   1.00 38.74  ? 442 GLU B CD  1 
ATOM   7190 O  OE1 . GLU B 1 442 ? -20.428 28.425  4.609   1.00 37.66  ? 442 GLU B OE1 1 
ATOM   7191 O  OE2 . GLU B 1 442 ? -19.505 30.434  4.591   1.00 44.26  ? 442 GLU B OE2 1 
ATOM   7192 N  N   . GLY B 1 443 ? -22.518 30.469  9.287   1.00 21.50  ? 443 GLY B N   1 
ATOM   7193 C  CA  . GLY B 1 443 ? -23.801 31.140  9.290   1.00 21.50  ? 443 GLY B CA  1 
ATOM   7194 C  C   . GLY B 1 443 ? -24.605 30.814  10.541  1.00 20.26  ? 443 GLY B C   1 
ATOM   7195 O  O   . GLY B 1 443 ? -25.808 31.083  10.589  1.00 21.78  ? 443 GLY B O   1 
ATOM   7196 N  N   . PHE B 1 444 ? -23.948 30.233  11.561  1.00 17.94  ? 444 PHE B N   1 
ATOM   7197 C  CA  . PHE B 1 444 ? -24.614 29.970  12.819  1.00 17.20  ? 444 PHE B CA  1 
ATOM   7198 C  C   . PHE B 1 444 ? -24.786 31.291  13.579  1.00 18.14  ? 444 PHE B C   1 
ATOM   7199 O  O   . PHE B 1 444 ? -23.798 31.938  13.918  1.00 18.89  ? 444 PHE B O   1 
ATOM   7200 C  CB  . PHE B 1 444 ? -23.848 28.907  13.598  1.00 16.13  ? 444 PHE B CB  1 
ATOM   7201 C  CG  . PHE B 1 444 ? -24.417 28.564  14.947  1.00 15.77  ? 444 PHE B CG  1 
ATOM   7202 C  CD1 . PHE B 1 444 ? -25.784 28.470  15.154  1.00 15.37  ? 444 PHE B CD1 1 
ATOM   7203 C  CD2 . PHE B 1 444 ? -23.574 28.246  15.989  1.00 13.67  ? 444 PHE B CD2 1 
ATOM   7204 C  CE1 . PHE B 1 444 ? -26.288 28.180  16.405  1.00 14.27  ? 444 PHE B CE1 1 
ATOM   7205 C  CE2 . PHE B 1 444 ? -24.077 27.973  17.239  1.00 15.67  ? 444 PHE B CE2 1 
ATOM   7206 C  CZ  . PHE B 1 444 ? -25.434 27.955  17.453  1.00 14.50  ? 444 PHE B CZ  1 
ATOM   7207 N  N   . VAL B 1 445 ? -26.055 31.624  13.877  1.00 18.57  ? 445 VAL B N   1 
ATOM   7208 C  CA  . VAL B 1 445 ? -26.450 32.802  14.619  1.00 17.68  ? 445 VAL B CA  1 
ATOM   7209 C  C   . VAL B 1 445 ? -27.438 32.422  15.719  1.00 17.75  ? 445 VAL B C   1 
ATOM   7210 O  O   . VAL B 1 445 ? -28.254 31.500  15.582  1.00 17.61  ? 445 VAL B O   1 
ATOM   7211 C  CB  . VAL B 1 445 ? -27.041 33.886  13.682  1.00 19.71  ? 445 VAL B CB  1 
ATOM   7212 C  CG1 . VAL B 1 445 ? -26.012 34.419  12.684  1.00 19.11  ? 445 VAL B CG1 1 
ATOM   7213 C  CG2 . VAL B 1 445 ? -28.271 33.382  12.929  1.00 20.73  ? 445 VAL B CG2 1 
ATOM   7214 N  N   . VAL B 1 446 ? -27.393 33.198  16.812  1.00 17.34  ? 446 VAL B N   1 
ATOM   7215 C  CA  . VAL B 1 446 ? -28.242 32.976  17.960  1.00 17.85  ? 446 VAL B CA  1 
ATOM   7216 C  C   . VAL B 1 446 ? -28.622 34.338  18.512  1.00 18.93  ? 446 VAL B C   1 
ATOM   7217 O  O   . VAL B 1 446 ? -28.043 35.361  18.165  1.00 19.49  ? 446 VAL B O   1 
ATOM   7218 C  CB  . VAL B 1 446 ? -27.619 32.109  19.080  1.00 18.06  ? 446 VAL B CB  1 
ATOM   7219 C  CG1 . VAL B 1 446 ? -27.241 30.724  18.620  1.00 18.13  ? 446 VAL B CG1 1 
ATOM   7220 C  CG2 . VAL B 1 446 ? -26.413 32.777  19.732  1.00 20.55  ? 446 VAL B CG2 1 
ATOM   7221 N  N   . LYS B 1 447 ? -29.611 34.293  19.396  1.00 19.43  ? 447 LYS B N   1 
ATOM   7222 C  CA  . LYS B 1 447 ? -29.971 35.401  20.245  1.00 20.16  ? 447 LYS B CA  1 
ATOM   7223 C  C   . LYS B 1 447 ? -29.668 35.026  21.686  1.00 18.73  ? 447 LYS B C   1 
ATOM   7224 O  O   . LYS B 1 447 ? -30.012 33.947  22.129  1.00 19.25  ? 447 LYS B O   1 
ATOM   7225 C  CB  . LYS B 1 447 ? -31.458 35.697  20.039  1.00 20.66  ? 447 LYS B CB  1 
ATOM   7226 C  CG  . LYS B 1 447 ? -31.781 36.470  18.777  1.00 22.96  ? 447 LYS B CG  1 
ATOM   7227 C  CD  . LYS B 1 447 ? -33.211 36.958  18.769  1.00 22.61  ? 447 LYS B CD  1 
ATOM   7228 C  CE  . LYS B 1 447 ? -33.549 37.791  17.557  1.00 26.22  ? 447 LYS B CE  1 
ATOM   7229 N  NZ  . LYS B 1 447 ? -34.982 38.155  17.580  1.00 24.02  ? 447 LYS B NZ  1 
ATOM   7230 N  N   . ALA B 1 448 ? -29.055 35.957  22.408  1.00 19.39  ? 448 ALA B N   1 
ATOM   7231 C  CA  . ALA B 1 448 ? -28.688 35.788  23.800  1.00 20.51  ? 448 ALA B CA  1 
ATOM   7232 C  C   . ALA B 1 448 ? -29.393 36.836  24.649  1.00 24.08  ? 448 ALA B C   1 
ATOM   7233 O  O   . ALA B 1 448 ? -29.109 38.031  24.526  1.00 27.51  ? 448 ALA B O   1 
ATOM   7234 C  CB  . ALA B 1 448 ? -27.198 35.942  23.929  1.00 21.20  ? 448 ALA B CB  1 
ATOM   7235 N  N   . LYS B 1 449 ? -30.278 36.385  25.539  1.00 21.63  ? 449 LYS B N   1 
ATOM   7236 C  CA  . LYS B 1 449 ? -30.966 37.261  26.460  1.00 21.82  ? 449 LYS B CA  1 
ATOM   7237 C  C   . LYS B 1 449 ? -30.219 37.212  27.785  1.00 21.68  ? 449 LYS B C   1 
ATOM   7238 O  O   . LYS B 1 449 ? -30.106 36.127  28.360  1.00 18.15  ? 449 LYS B O   1 
ATOM   7239 C  CB  . LYS B 1 449 ? -32.404 36.803  26.679  1.00 25.02  ? 449 LYS B CB  1 
ATOM   7240 C  CG  . LYS B 1 449 ? -33.250 37.774  27.488  1.00 29.86  ? 449 LYS B CG  1 
ATOM   7241 C  CD  . LYS B 1 449 ? -34.644 37.282  27.760  1.00 32.49  ? 449 LYS B CD  1 
ATOM   7242 C  CE  . LYS B 1 449 ? -35.582 38.442  28.017  1.00 34.76  ? 449 LYS B CE  1 
ATOM   7243 N  NZ  . LYS B 1 449 ? -36.713 38.021  28.868  1.00 40.19  ? 449 LYS B NZ  1 
ATOM   7244 N  N   . SER B 1 450 ? -29.721 38.387  28.223  1.00 18.76  ? 450 SER B N   1 
ATOM   7245 C  CA  . SER B 1 450 ? -28.971 38.528  29.453  1.00 18.26  ? 450 SER B CA  1 
ATOM   7246 C  C   . SER B 1 450 ? -29.814 38.105  30.636  1.00 19.36  ? 450 SER B C   1 
ATOM   7247 O  O   . SER B 1 450 ? -30.995 38.442  30.754  1.00 18.55  ? 450 SER B O   1 
ATOM   7248 C  CB  . SER B 1 450 ? -28.409 39.933  29.634  1.00 21.01  ? 450 SER B CB  1 
ATOM   7249 O  OG  . SER B 1 450 ? -27.858 40.053  30.945  1.00 21.46  ? 450 SER B OG  1 
ATOM   7250 N  N   . LYS B 1 451 ? -29.162 37.376  31.532  1.00 19.75  ? 451 LYS B N   1 
ATOM   7251 C  CA  . LYS B 1 451 ? -29.730 37.069  32.834  1.00 23.67  ? 451 LYS B CA  1 
ATOM   7252 C  C   . LYS B 1 451 ? -29.478 38.214  33.816  1.00 23.21  ? 451 LYS B C   1 
ATOM   7253 O  O   . LYS B 1 451 ? -29.953 38.180  34.944  1.00 23.55  ? 451 LYS B O   1 
ATOM   7254 C  CB  . LYS B 1 451 ? -29.158 35.738  33.327  1.00 24.23  ? 451 LYS B CB  1 
ATOM   7255 C  CG  . LYS B 1 451 ? -29.561 34.550  32.487  1.00 27.28  ? 451 LYS B CG  1 
ATOM   7256 C  CD  . LYS B 1 451 ? -28.924 33.266  32.962  1.00 28.63  ? 451 LYS B CD  1 
ATOM   7257 C  CE  . LYS B 1 451 ? -29.688 32.048  32.496  1.00 31.98  ? 451 LYS B CE  1 
ATOM   7258 N  NZ  . LYS B 1 451 ? -29.217 30.843  33.200  1.00 35.97  ? 451 LYS B NZ  1 
ATOM   7259 N  N   . GLN B 1 452 ? -28.711 39.218  33.392  1.00 24.47  ? 452 GLN B N   1 
ATOM   7260 C  CA  . GLN B 1 452 ? -28.519 40.438  34.162  1.00 31.74  ? 452 GLN B CA  1 
ATOM   7261 C  C   . GLN B 1 452 ? -27.846 40.096  35.489  1.00 29.84  ? 452 GLN B C   1 
ATOM   7262 O  O   . GLN B 1 452 ? -28.187 40.615  36.538  1.00 27.37  ? 452 GLN B O   1 
ATOM   7263 C  CB  . GLN B 1 452 ? -29.837 41.208  34.326  1.00 34.78  ? 452 GLN B CB  1 
ATOM   7264 C  CG  . GLN B 1 452 ? -30.304 41.886  33.042  1.00 39.58  ? 452 GLN B CG  1 
ATOM   7265 C  CD  . GLN B 1 452 ? -31.246 43.026  33.342  1.00 48.06  ? 452 GLN B CD  1 
ATOM   7266 O  OE1 . GLN B 1 452 ? -32.277 42.849  33.987  1.00 51.72  ? 452 GLN B OE1 1 
ATOM   7267 N  NE2 . GLN B 1 452 ? -30.879 44.227  32.919  1.00 55.16  ? 452 GLN B NE2 1 
ATOM   7268 N  N   . ILE B 1 453 ? -26.830 39.251  35.394  1.00 29.40  ? 453 ILE B N   1 
ATOM   7269 C  CA  . ILE B 1 453 ? -25.998 38.888  36.518  1.00 29.52  ? 453 ILE B CA  1 
ATOM   7270 C  C   . ILE B 1 453 ? -24.687 39.655  36.409  1.00 27.90  ? 453 ILE B C   1 
ATOM   7271 O  O   . ILE B 1 453 ? -23.995 39.559  35.398  1.00 24.78  ? 453 ILE B O   1 
ATOM   7272 C  CB  . ILE B 1 453 ? -25.780 37.373  36.509  1.00 27.10  ? 453 ILE B CB  1 
ATOM   7273 C  CG1 . ILE B 1 453 ? -27.132 36.663  36.548  1.00 29.70  ? 453 ILE B CG1 1 
ATOM   7274 C  CG2 . ILE B 1 453 ? -24.841 36.950  37.633  1.00 29.26  ? 453 ILE B CG2 1 
ATOM   7275 C  CD1 . ILE B 1 453 ? -27.018 35.170  36.600  1.00 30.96  ? 453 ILE B CD1 1 
ATOM   7276 N  N   . PRO B 1 454 ? -24.280 40.420  37.446  1.00 31.89  ? 454 PRO B N   1 
ATOM   7277 C  CA  . PRO B 1 454 ? -23.113 41.293  37.313  1.00 33.13  ? 454 PRO B CA  1 
ATOM   7278 C  C   . PRO B 1 454 ? -21.832 40.471  37.125  1.00 31.55  ? 454 PRO B C   1 
ATOM   7279 O  O   . PRO B 1 454 ? -21.720 39.306  37.528  1.00 30.16  ? 454 PRO B O   1 
ATOM   7280 C  CB  . PRO B 1 454 ? -23.145 42.136  38.605  1.00 36.27  ? 454 PRO B CB  1 
ATOM   7281 C  CG  . PRO B 1 454 ? -24.571 41.965  39.105  1.00 36.45  ? 454 PRO B CG  1 
ATOM   7282 C  CD  . PRO B 1 454 ? -24.898 40.517  38.780  1.00 34.12  ? 454 PRO B CD  1 
ATOM   7283 N  N   . LEU B 1 455 ? -20.894 41.093  36.422  1.00 32.00  ? 455 LEU B N   1 
ATOM   7284 C  CA  . LEU B 1 455 ? -19.689 40.444  35.950  1.00 35.06  ? 455 LEU B CA  1 
ATOM   7285 C  C   . LEU B 1 455 ? -18.491 41.088  36.661  1.00 37.29  ? 455 LEU B C   1 
ATOM   7286 O  O   . LEU B 1 455 ? -18.642 42.250  37.041  1.00 44.38  ? 455 LEU B O   1 
ATOM   7287 C  CB  . LEU B 1 455 ? -19.701 40.645  34.437  1.00 31.96  ? 455 LEU B CB  1 
ATOM   7288 C  CG  . LEU B 1 455 ? -18.521 40.102  33.651  1.00 34.01  ? 455 LEU B CG  1 
ATOM   7289 C  CD1 . LEU B 1 455 ? -18.545 38.581  33.610  1.00 33.71  ? 455 LEU B CD1 1 
ATOM   7290 C  CD2 . LEU B 1 455 ? -18.541 40.689  32.252  1.00 31.77  ? 455 LEU B CD2 1 
HETATM 7291 C  CHA . HEM C 2 .   ? 19.543  1.823   43.605  1.00 14.14  ? 501 HEM A CHA 1 
HETATM 7292 C  CHB . HEM C 2 .   ? 14.723  1.732   43.335  1.00 13.78  ? 501 HEM A CHB 1 
HETATM 7293 C  CHC . HEM C 2 .   ? 15.042  -2.490  41.041  1.00 13.89  ? 501 HEM A CHC 1 
HETATM 7294 C  CHD . HEM C 2 .   ? 19.761  -2.708  41.864  1.00 15.42  ? 501 HEM A CHD 1 
HETATM 7295 C  C1A . HEM C 2 .   ? 18.219  2.141   43.699  1.00 13.43  ? 501 HEM A C1A 1 
HETATM 7296 C  C2A . HEM C 2 .   ? 17.764  3.374   44.270  1.00 14.01  ? 501 HEM A C2A 1 
HETATM 7297 C  C3A . HEM C 2 .   ? 16.389  3.333   44.192  1.00 12.52  ? 501 HEM A C3A 1 
HETATM 7298 C  C4A . HEM C 2 .   ? 16.036  2.080   43.638  1.00 12.10  ? 501 HEM A C4A 1 
HETATM 7299 C  CMA . HEM C 2 .   ? 15.384  4.365   44.670  1.00 13.23  ? 501 HEM A CMA 1 
HETATM 7300 C  CAA . HEM C 2 .   ? 18.659  4.481   44.832  1.00 13.49  ? 501 HEM A CAA 1 
HETATM 7301 C  CBA . HEM C 2 .   ? 18.922  4.257   46.292  1.00 14.53  ? 501 HEM A CBA 1 
HETATM 7302 C  CGA . HEM C 2 .   ? 19.567  5.419   47.022  1.00 14.24  ? 501 HEM A CGA 1 
HETATM 7303 O  O1A . HEM C 2 .   ? 19.720  6.550   46.479  1.00 14.82  ? 501 HEM A O1A 1 
HETATM 7304 O  O2A . HEM C 2 .   ? 19.965  5.212   48.202  1.00 15.26  ? 501 HEM A O2A 1 
HETATM 7305 C  C1B . HEM C 2 .   ? 14.415  0.570   42.615  1.00 12.59  ? 501 HEM A C1B 1 
HETATM 7306 C  C2B . HEM C 2 .   ? 13.065  0.202   42.269  1.00 12.47  ? 501 HEM A C2B 1 
HETATM 7307 C  C3B . HEM C 2 .   ? 13.106  -1.002  41.661  1.00 12.14  ? 501 HEM A C3B 1 
HETATM 7308 C  C4B . HEM C 2 .   ? 14.555  -1.356  41.616  1.00 13.12  ? 501 HEM A C4B 1 
HETATM 7309 C  CMB . HEM C 2 .   ? 11.846  0.993   42.596  1.00 12.64  ? 501 HEM A CMB 1 
HETATM 7310 C  CAB . HEM C 2 .   ? 12.019  -1.798  41.025  1.00 12.84  ? 501 HEM A CAB 1 
HETATM 7311 C  CBB . HEM C 2 .   ? 10.798  -1.320  40.714  1.00 13.24  ? 501 HEM A CBB 1 
HETATM 7312 C  C1C . HEM C 2 .   ? 16.341  -2.933  41.047  1.00 12.91  ? 501 HEM A C1C 1 
HETATM 7313 C  C2C . HEM C 2 .   ? 16.820  -4.079  40.383  1.00 14.81  ? 501 HEM A C2C 1 
HETATM 7314 C  C3C . HEM C 2 .   ? 18.180  -4.161  40.652  1.00 14.22  ? 501 HEM A C3C 1 
HETATM 7315 C  C4C . HEM C 2 .   ? 18.478  -3.035  41.428  1.00 13.71  ? 501 HEM A C4C 1 
HETATM 7316 C  CMC . HEM C 2 .   ? 15.998  -5.116  39.630  1.00 13.28  ? 501 HEM A CMC 1 
HETATM 7317 C  CAC . HEM C 2 .   ? 19.213  -5.151  40.244  1.00 15.66  ? 501 HEM A CAC 1 
HETATM 7318 C  CBC . HEM C 2 .   ? 19.134  -6.084  39.324  1.00 15.83  ? 501 HEM A CBC 1 
HETATM 7319 C  C1D . HEM C 2 .   ? 20.061  -1.452  42.419  1.00 13.90  ? 501 HEM A C1D 1 
HETATM 7320 C  C2D . HEM C 2 .   ? 21.458  -1.110  42.705  1.00 13.51  ? 501 HEM A C2D 1 
HETATM 7321 C  C3D . HEM C 2 .   ? 21.376  0.160   43.187  1.00 13.21  ? 501 HEM A C3D 1 
HETATM 7322 C  C4D . HEM C 2 .   ? 19.962  0.543   43.131  1.00 12.59  ? 501 HEM A C4D 1 
HETATM 7323 C  CMD . HEM C 2 .   ? 22.679  -2.030  42.542  1.00 13.42  ? 501 HEM A CMD 1 
HETATM 7324 C  CAD . HEM C 2 .   ? 22.565  1.010   43.646  1.00 13.56  ? 501 HEM A CAD 1 
HETATM 7325 C  CBD . HEM C 2 .   ? 23.150  1.686   42.425  1.00 13.56  ? 501 HEM A CBD 1 
HETATM 7326 C  CGD . HEM C 2 .   ? 24.362  2.522   42.784  1.00 16.00  ? 501 HEM A CGD 1 
HETATM 7327 O  O1D . HEM C 2 .   ? 25.395  2.467   42.103  1.00 15.93  ? 501 HEM A O1D 1 
HETATM 7328 O  O2D . HEM C 2 .   ? 24.314  3.319   43.713  1.00 16.22  ? 501 HEM A O2D 1 
HETATM 7329 N  NA  . HEM C 2 .   ? 17.124  1.324   43.361  1.00 12.92  ? 501 HEM A NA  1 
HETATM 7330 N  NB  . HEM C 2 .   ? 15.245  -0.386  42.206  1.00 12.77  ? 501 HEM A NB  1 
HETATM 7331 N  NC  . HEM C 2 .   ? 17.342  -2.375  41.666  1.00 13.85  ? 501 HEM A NC  1 
HETATM 7332 N  ND  . HEM C 2 .   ? 19.220  -0.423  42.671  1.00 11.36  ? 501 HEM A ND  1 
HETATM 7333 FE FE  . HEM C 2 .   ? 17.311  -0.437  42.343  1.00 12.27  ? 501 HEM A FE  1 
HETATM 7334 C  CHA . HEM D 2 .   ? -1.527  18.917  17.121  1.00 11.85  ? 501 HEM B CHA 1 
HETATM 7335 C  CHB . HEM D 2 .   ? -6.332  18.963  17.432  1.00 13.23  ? 501 HEM B CHB 1 
HETATM 7336 C  CHC . HEM D 2 .   ? -6.163  23.031  20.028  1.00 12.05  ? 501 HEM B CHC 1 
HETATM 7337 C  CHD . HEM D 2 .   ? -1.370  23.328  19.219  1.00 12.43  ? 501 HEM B CHD 1 
HETATM 7338 C  C1A . HEM D 2 .   ? -2.839  18.580  17.015  1.00 12.12  ? 501 HEM B C1A 1 
HETATM 7339 C  C2A . HEM D 2 .   ? -3.339  17.445  16.310  1.00 13.07  ? 501 HEM B C2A 1 
HETATM 7340 C  C3A . HEM D 2 .   ? -4.697  17.485  16.389  1.00 13.46  ? 501 HEM B C3A 1 
HETATM 7341 C  C4A . HEM D 2 .   ? -5.058  18.600  17.135  1.00 12.24  ? 501 HEM B C4A 1 
HETATM 7342 C  CMA . HEM D 2 .   ? -5.649  16.443  15.837  1.00 12.40  ? 501 HEM B CMA 1 
HETATM 7343 C  CAA . HEM D 2 .   ? -2.538  16.363  15.590  1.00 12.46  ? 501 HEM B CAA 1 
HETATM 7344 C  CBA . HEM D 2 .   ? -2.333  16.778  14.136  1.00 13.73  ? 501 HEM B CBA 1 
HETATM 7345 C  CGA . HEM D 2 .   ? -1.581  15.681  13.364  1.00 15.72  ? 501 HEM B CGA 1 
HETATM 7346 O  O1A . HEM D 2 .   ? -1.139  15.981  12.220  1.00 15.39  ? 501 HEM B O1A 1 
HETATM 7347 O  O2A . HEM D 2 .   ? -1.427  14.477  13.825  1.00 14.39  ? 501 HEM B O2A 1 
HETATM 7348 C  C1B . HEM D 2 .   ? -6.723  20.098  18.204  1.00 13.08  ? 501 HEM B C1B 1 
HETATM 7349 C  C2B . HEM D 2 .   ? -8.072  20.418  18.561  1.00 13.17  ? 501 HEM B C2B 1 
HETATM 7350 C  C3B . HEM D 2 .   ? -8.044  21.575  19.262  1.00 12.36  ? 501 HEM B C3B 1 
HETATM 7351 C  C4B . HEM D 2 .   ? -6.630  21.917  19.353  1.00 12.48  ? 501 HEM B C4B 1 
HETATM 7352 C  CMB . HEM D 2 .   ? -9.362  19.654  18.204  1.00 12.92  ? 501 HEM B CMB 1 
HETATM 7353 C  CAB . HEM D 2 .   ? -9.059  22.317  19.949  1.00 11.91  ? 501 HEM B CAB 1 
HETATM 7354 C  CBB . HEM D 2 .   ? -10.279 21.843  20.265  1.00 12.84  ? 501 HEM B CBB 1 
HETATM 7355 C  C1C . HEM D 2 .   ? -4.853  23.464  20.058  1.00 13.13  ? 501 HEM B C1C 1 
HETATM 7356 C  C2C . HEM D 2 .   ? -4.357  24.574  20.804  1.00 14.54  ? 501 HEM B C2C 1 
HETATM 7357 C  C3C . HEM D 2 .   ? -2.990  24.688  20.557  1.00 15.74  ? 501 HEM B C3C 1 
HETATM 7358 C  C4C . HEM D 2 .   ? -2.680  23.615  19.667  1.00 14.15  ? 501 HEM B C4C 1 
HETATM 7359 C  CMC . HEM D 2 .   ? -5.152  25.498  21.659  1.00 14.13  ? 501 HEM B CMC 1 
HETATM 7360 C  CAC . HEM D 2 .   ? -1.992  25.656  21.115  1.00 18.51  ? 501 HEM B CAC 1 
HETATM 7361 C  CBC . HEM D 2 .   ? -2.233  26.496  22.101  1.00 20.82  ? 501 HEM B CBC 1 
HETATM 7362 C  C1D . HEM D 2 .   ? -1.081  22.140  18.560  1.00 12.67  ? 501 HEM B C1D 1 
HETATM 7363 C  C2D . HEM D 2 .   ? 0.327   21.821  18.209  1.00 12.89  ? 501 HEM B C2D 1 
HETATM 7364 C  C3D . HEM D 2 .   ? 0.283   20.585  17.645  1.00 13.09  ? 501 HEM B C3D 1 
HETATM 7365 C  C4D . HEM D 2 .   ? -1.152  20.151  17.704  1.00 12.38  ? 501 HEM B C4D 1 
HETATM 7366 C  CMD . HEM D 2 .   ? 1.543   22.701  18.407  1.00 13.33  ? 501 HEM B CMD 1 
HETATM 7367 C  CAD . HEM D 2 .   ? 1.424   19.739  17.103  1.00 15.08  ? 501 HEM B CAD 1 
HETATM 7368 C  CBD . HEM D 2 .   ? 1.993   18.862  18.245  1.00 14.80  ? 501 HEM B CBD 1 
HETATM 7369 C  CGD . HEM D 2 .   ? 3.230   18.082  17.836  1.00 18.54  ? 501 HEM B CGD 1 
HETATM 7370 O  O1D . HEM D 2 .   ? 3.223   17.350  16.809  1.00 18.06  ? 501 HEM B O1D 1 
HETATM 7371 O  O2D . HEM D 2 .   ? 4.283   18.054  18.561  1.00 20.21  ? 501 HEM B O2D 1 
HETATM 7372 N  NA  . HEM D 2 .   ? -3.913  19.282  17.484  1.00 13.17  ? 501 HEM B NA  1 
HETATM 7373 N  NB  . HEM D 2 .   ? -5.916  21.022  18.679  1.00 11.50  ? 501 HEM B NB  1 
HETATM 7374 N  NC  . HEM D 2 .   ? -3.850  22.892  19.448  1.00 12.96  ? 501 HEM B NC  1 
HETATM 7375 N  ND  . HEM D 2 .   ? -1.941  21.081  18.261  1.00 11.02  ? 501 HEM B ND  1 
HETATM 7376 FE FE  . HEM D 2 .   ? -3.851  20.995  18.546  1.00 12.27  ? 501 HEM B FE  1 
HETATM 7377 O  O   . HOH E 3 .   ? 25.159  -9.403  32.008  1.00 38.63  ? 601 HOH A O   1 
HETATM 7378 O  O   . HOH E 3 .   ? 20.518  14.539  69.764  1.00 38.11  ? 602 HOH A O   1 
HETATM 7379 O  O   . HOH E 3 .   ? 8.016   -1.289  30.480  1.00 40.90  ? 603 HOH A O   1 
HETATM 7380 O  O   . HOH E 3 .   ? 7.541   -24.298 33.128  1.00 30.96  ? 604 HOH A O   1 
HETATM 7381 O  O   . HOH E 3 .   ? 31.353  12.310  47.119  1.00 31.53  ? 605 HOH A O   1 
HETATM 7382 O  O   . HOH E 3 .   ? 3.231   -14.400 24.150  1.00 40.54  ? 606 HOH A O   1 
HETATM 7383 O  O   . HOH E 3 .   ? 35.149  0.482   50.064  1.00 37.00  ? 607 HOH A O   1 
HETATM 7384 O  O   . HOH E 3 .   ? -9.228  -26.819 45.793  1.00 33.57  ? 608 HOH A O   1 
HETATM 7385 O  O   . HOH E 3 .   ? -12.611 -3.626  40.993  1.00 32.51  ? 609 HOH A O   1 
HETATM 7386 O  O   . HOH E 3 .   ? 37.196  9.325   46.387  1.00 35.76  ? 610 HOH A O   1 
HETATM 7387 O  O   . HOH E 3 .   ? 25.504  -10.268 29.556  1.00 35.64  ? 611 HOH A O   1 
HETATM 7388 O  O   . HOH E 3 .   ? 32.913  -20.723 46.980  1.00 28.15  ? 612 HOH A O   1 
HETATM 7389 O  O   . HOH E 3 .   ? 4.520   7.543   64.096  1.00 27.87  ? 613 HOH A O   1 
HETATM 7390 O  O   . HOH E 3 .   ? 22.576  23.013  59.842  1.00 48.15  ? 614 HOH A O   1 
HETATM 7391 O  O   . HOH E 3 .   ? 16.948  -3.349  19.641  1.00 34.94  ? 615 HOH A O   1 
HETATM 7392 O  O   . HOH E 3 .   ? -2.322  7.064   48.876  1.00 29.50  ? 616 HOH A O   1 
HETATM 7393 O  O   . HOH E 3 .   ? -7.749  1.487   45.546  1.00 33.13  ? 617 HOH A O   1 
HETATM 7394 O  O   . HOH E 3 .   ? 18.813  -23.220 46.813  1.00 35.58  ? 618 HOH A O   1 
HETATM 7395 O  O   . HOH E 3 .   ? 22.375  4.138   44.971  1.00 13.20  ? 619 HOH A O   1 
HETATM 7396 O  O   . HOH E 3 .   ? 34.837  -2.663  43.978  1.00 33.48  ? 620 HOH A O   1 
HETATM 7397 O  O   . HOH E 3 .   ? -0.930  15.905  47.475  1.00 44.20  ? 621 HOH A O   1 
HETATM 7398 O  O   . HOH E 3 .   ? 35.606  -7.793  38.272  1.00 23.87  ? 622 HOH A O   1 
HETATM 7399 O  O   . HOH E 3 .   ? 24.233  10.888  42.443  1.00 20.27  ? 623 HOH A O   1 
HETATM 7400 O  O   . HOH E 3 .   ? 12.206  16.465  72.435  1.00 45.50  ? 624 HOH A O   1 
HETATM 7401 O  O   . HOH E 3 .   ? 30.091  3.972   34.321  1.00 40.52  ? 625 HOH A O   1 
HETATM 7402 O  O   . HOH E 3 .   ? 23.696  4.120   39.138  1.00 20.81  ? 626 HOH A O   1 
HETATM 7403 O  O   . HOH E 3 .   ? 34.758  -4.267  32.191  1.00 31.65  ? 627 HOH A O   1 
HETATM 7404 O  O   . HOH E 3 .   ? -0.999  4.153   54.127  1.00 32.73  ? 628 HOH A O   1 
HETATM 7405 O  O   . HOH E 3 .   ? -13.200 -15.458 39.468  1.00 31.27  ? 629 HOH A O   1 
HETATM 7406 O  O   . HOH E 3 .   ? -1.061  0.614   54.964  1.00 24.58  ? 630 HOH A O   1 
HETATM 7407 O  O   . HOH E 3 .   ? 8.787   -4.026  47.830  1.00 32.68  ? 631 HOH A O   1 
HETATM 7408 O  O   . HOH E 3 .   ? 1.007   -11.222 52.208  1.00 22.78  ? 632 HOH A O   1 
HETATM 7409 O  O   . HOH E 3 .   ? -2.978  13.653  52.212  1.00 36.55  ? 633 HOH A O   1 
HETATM 7410 O  O   . HOH E 3 .   ? 21.341  -4.355  69.289  1.00 37.67  ? 634 HOH A O   1 
HETATM 7411 O  O   . HOH E 3 .   ? 15.945  -2.775  26.608  1.00 36.29  ? 635 HOH A O   1 
HETATM 7412 O  O   . HOH E 3 .   ? 21.683  0.225   34.079  1.00 29.05  ? 636 HOH A O   1 
HETATM 7413 O  O   . HOH E 3 .   ? -4.159  -17.307 51.788  1.00 48.55  ? 637 HOH A O   1 
HETATM 7414 O  O   . HOH E 3 .   ? 7.210   22.475  55.372  1.00 21.64  ? 638 HOH A O   1 
HETATM 7415 O  O   . HOH E 3 .   ? 18.539  -15.529 29.242  1.00 27.28  ? 639 HOH A O   1 
HETATM 7416 O  O   . HOH E 3 .   ? 7.858   -28.892 37.353  1.00 17.68  ? 640 HOH A O   1 
HETATM 7417 O  O   . HOH E 3 .   ? 18.429  -11.423 61.698  1.00 36.62  ? 641 HOH A O   1 
HETATM 7418 O  O   . HOH E 3 .   ? -9.447  -9.822  46.893  1.00 28.85  ? 642 HOH A O   1 
HETATM 7419 O  O   . HOH E 3 .   ? 14.398  -20.675 39.950  1.00 14.67  ? 643 HOH A O   1 
HETATM 7420 O  O   . HOH E 3 .   ? 13.905  -5.369  42.724  1.00 19.10  ? 644 HOH A O   1 
HETATM 7421 O  O   . HOH E 3 .   ? 19.082  20.224  40.217  1.00 34.56  ? 645 HOH A O   1 
HETATM 7422 O  O   . HOH E 3 .   ? 0.169   7.997   55.537  1.00 28.28  ? 646 HOH A O   1 
HETATM 7423 O  O   . HOH E 3 .   ? -6.911  5.651   43.503  1.00 34.90  ? 647 HOH A O   1 
HETATM 7424 O  O   . HOH E 3 .   ? 18.061  22.446  59.360  1.00 38.55  ? 648 HOH A O   1 
HETATM 7425 O  O   . HOH E 3 .   ? 18.163  4.355   36.655  1.00 16.75  ? 649 HOH A O   1 
HETATM 7426 O  O   . HOH E 3 .   ? 13.154  -2.311  30.445  1.00 26.80  ? 650 HOH A O   1 
HETATM 7427 O  O   . HOH E 3 .   ? 31.383  -7.756  56.113  1.00 30.56  ? 651 HOH A O   1 
HETATM 7428 O  O   . HOH E 3 .   ? 11.798  9.475   36.130  1.00 32.84  ? 652 HOH A O   1 
HETATM 7429 O  O   . HOH E 3 .   ? 35.048  -4.943  49.433  1.00 29.82  ? 653 HOH A O   1 
HETATM 7430 O  O   . HOH E 3 .   ? 8.188   16.890  53.914  1.00 20.44  ? 654 HOH A O   1 
HETATM 7431 O  O   . HOH E 3 .   ? 25.616  10.231  57.235  1.00 38.32  ? 655 HOH A O   1 
HETATM 7432 O  O   . HOH E 3 .   ? 7.200   1.459   32.845  1.00 29.96  ? 656 HOH A O   1 
HETATM 7433 O  O   . HOH E 3 .   ? 10.739  -22.035 40.559  1.00 18.15  ? 657 HOH A O   1 
HETATM 7434 O  O   . HOH E 3 .   ? 3.455   -7.704  18.484  1.00 21.90  ? 658 HOH A O   1 
HETATM 7435 O  O   . HOH E 3 .   ? 11.283  3.624   44.750  1.00 17.05  ? 659 HOH A O   1 
HETATM 7436 O  O   . HOH E 3 .   ? 22.008  16.236  59.327  1.00 24.16  ? 660 HOH A O   1 
HETATM 7437 O  O   . HOH E 3 .   ? -2.750  21.522  41.080  1.00 28.48  ? 661 HOH A O   1 
HETATM 7438 O  O   . HOH E 3 .   ? 30.322  -0.944  45.056  1.00 19.66  ? 662 HOH A O   1 
HETATM 7439 O  O   . HOH E 3 .   ? 25.385  -2.647  48.565  1.00 16.84  ? 663 HOH A O   1 
HETATM 7440 O  O   . HOH E 3 .   ? -4.154  6.269   46.028  1.00 35.59  ? 664 HOH A O   1 
HETATM 7441 O  O   . HOH E 3 .   ? -1.229  14.278  36.321  1.00 25.92  ? 665 HOH A O   1 
HETATM 7442 O  O   . HOH E 3 .   ? 3.751   17.720  52.066  1.00 32.79  ? 666 HOH A O   1 
HETATM 7443 O  O   . HOH E 3 .   ? 2.891   19.934  35.532  1.00 25.30  ? 667 HOH A O   1 
HETATM 7444 O  O   . HOH E 3 .   ? -1.892  9.922   50.486  1.00 33.81  ? 668 HOH A O   1 
HETATM 7445 O  O   . HOH E 3 .   ? 10.715  -13.296 34.825  1.00 21.16  ? 669 HOH A O   1 
HETATM 7446 O  O   . HOH E 3 .   ? 34.228  5.871   43.343  1.00 16.99  ? 670 HOH A O   1 
HETATM 7447 O  O   . HOH E 3 .   ? 7.640   -14.740 18.831  1.00 46.86  ? 671 HOH A O   1 
HETATM 7448 O  O   . HOH E 3 .   ? -0.408  -28.238 33.175  1.00 24.43  ? 672 HOH A O   1 
HETATM 7449 O  O   . HOH E 3 .   ? 17.321  -23.676 45.062  1.00 29.53  ? 673 HOH A O   1 
HETATM 7450 O  O   . HOH E 3 .   ? 1.054   -4.720  56.522  1.00 36.01  ? 674 HOH A O   1 
HETATM 7451 O  O   . HOH E 3 .   ? 14.198  -9.684  39.693  1.00 17.51  ? 675 HOH A O   1 
HETATM 7452 O  O   . HOH E 3 .   ? 5.187   3.136   28.529  1.00 17.65  ? 676 HOH A O   1 
HETATM 7453 O  O   . HOH E 3 .   ? 1.299   -21.533 46.621  1.00 23.77  ? 677 HOH A O   1 
HETATM 7454 O  O   . HOH E 3 .   ? -0.422  -18.081 45.251  1.00 16.92  ? 678 HOH A O   1 
HETATM 7455 O  O   . HOH E 3 .   ? 3.852   -12.970 22.111  1.00 21.02  ? 679 HOH A O   1 
HETATM 7456 O  O   . HOH E 3 .   ? 20.307  6.898   50.234  1.00 11.65  ? 680 HOH A O   1 
HETATM 7457 O  O   . HOH E 3 .   ? 26.687  21.761  48.871  1.00 40.63  ? 681 HOH A O   1 
HETATM 7458 O  O   . HOH E 3 .   ? -11.087 0.840   28.926  1.00 16.75  ? 682 HOH A O   1 
HETATM 7459 O  O   . HOH E 3 .   ? 30.675  1.090   32.225  1.00 36.17  ? 683 HOH A O   1 
HETATM 7460 O  O   . HOH E 3 .   ? 2.387   10.388  61.175  1.00 28.00  ? 684 HOH A O   1 
HETATM 7461 O  O   . HOH E 3 .   ? 28.425  9.287   48.838  1.00 17.52  ? 685 HOH A O   1 
HETATM 7462 O  O   . HOH E 3 .   ? 36.134  3.170   52.352  1.00 29.31  ? 686 HOH A O   1 
HETATM 7463 O  O   . HOH E 3 .   ? 19.941  7.699   44.071  1.00 12.60  ? 687 HOH A O   1 
HETATM 7464 O  O   . HOH E 3 .   ? 26.448  18.950  58.996  1.00 35.75  ? 688 HOH A O   1 
HETATM 7465 O  O   . HOH E 3 .   ? -2.781  12.778  48.696  1.00 32.01  ? 689 HOH A O   1 
HETATM 7466 O  O   . HOH E 3 .   ? 6.491   15.623  41.643  1.00 19.91  ? 690 HOH A O   1 
HETATM 7467 O  O   . HOH E 3 .   ? 0.760   19.086  46.754  1.00 33.36  ? 691 HOH A O   1 
HETATM 7468 O  O   . HOH E 3 .   ? -6.812  -17.886 41.042  1.00 26.25  ? 692 HOH A O   1 
HETATM 7469 O  O   . HOH E 3 .   ? -7.995  -0.880  49.168  1.00 22.03  ? 693 HOH A O   1 
HETATM 7470 O  O   . HOH E 3 .   ? 13.477  -22.853 38.425  1.00 17.74  ? 694 HOH A O   1 
HETATM 7471 O  O   . HOH E 3 .   ? 6.988   21.908  44.130  1.00 18.63  ? 695 HOH A O   1 
HETATM 7472 O  O   . HOH E 3 .   ? -11.884 -4.938  33.450  1.00 26.18  ? 696 HOH A O   1 
HETATM 7473 O  O   . HOH E 3 .   ? -6.532  -9.814  31.523  1.00 25.31  ? 697 HOH A O   1 
HETATM 7474 O  O   . HOH E 3 .   ? -0.071  -15.307 52.031  1.00 48.16  ? 698 HOH A O   1 
HETATM 7475 O  O   . HOH E 3 .   ? -11.203 -20.864 32.272  1.00 35.50  ? 699 HOH A O   1 
HETATM 7476 O  O   . HOH E 3 .   ? 4.357   24.036  58.060  1.00 36.11  ? 700 HOH A O   1 
HETATM 7477 O  O   . HOH E 3 .   ? 22.931  -16.908 33.468  1.00 38.45  ? 701 HOH A O   1 
HETATM 7478 O  O   . HOH E 3 .   ? -2.502  -12.430 22.109  1.00 24.78  ? 702 HOH A O   1 
HETATM 7479 O  O   . HOH E 3 .   ? 4.784   -9.532  17.075  1.00 33.72  ? 703 HOH A O   1 
HETATM 7480 O  O   . HOH E 3 .   ? 16.375  -18.711 40.149  1.00 14.48  ? 704 HOH A O   1 
HETATM 7481 O  O   . HOH E 3 .   ? 9.080   16.969  74.180  1.00 17.78  ? 705 HOH A O   1 
HETATM 7482 O  O   . HOH E 3 .   ? -1.455  -12.379 50.003  1.00 20.78  ? 706 HOH A O   1 
HETATM 7483 O  O   . HOH E 3 .   ? 32.973  -9.870  51.236  1.00 29.35  ? 707 HOH A O   1 
HETATM 7484 O  O   . HOH E 3 .   ? 29.647  21.689  58.476  1.00 28.76  ? 708 HOH A O   1 
HETATM 7485 O  O   . HOH E 3 .   ? 2.115   -15.990 25.997  1.00 23.39  ? 709 HOH A O   1 
HETATM 7486 O  O   . HOH E 3 .   ? 20.550  8.675   36.355  1.00 26.25  ? 710 HOH A O   1 
HETATM 7487 O  O   . HOH E 3 .   ? 20.793  23.633  42.430  1.00 23.91  ? 711 HOH A O   1 
HETATM 7488 O  O   . HOH E 3 .   ? 30.482  4.431   56.297  1.00 27.43  ? 712 HOH A O   1 
HETATM 7489 O  O   . HOH E 3 .   ? 17.369  4.769   58.702  1.00 43.90  ? 713 HOH A O   1 
HETATM 7490 O  O   . HOH E 3 .   ? -8.170  5.652   40.478  1.00 18.09  ? 714 HOH A O   1 
HETATM 7491 O  O   . HOH E 3 .   ? 10.328  4.809   34.646  1.00 18.26  ? 715 HOH A O   1 
HETATM 7492 O  O   . HOH E 3 .   ? 45.105  2.451   37.733  1.00 27.28  ? 716 HOH A O   1 
HETATM 7493 O  O   . HOH E 3 .   ? -4.549  -18.709 29.373  1.00 18.37  ? 717 HOH A O   1 
HETATM 7494 O  O   . HOH E 3 .   ? -2.251  -19.996 45.157  1.00 24.02  ? 718 HOH A O   1 
HETATM 7495 O  O   . HOH E 3 .   ? 9.023   -10.433 17.738  1.00 29.78  ? 719 HOH A O   1 
HETATM 7496 O  O   . HOH E 3 .   ? -5.867  -19.236 38.733  1.00 25.64  ? 720 HOH A O   1 
HETATM 7497 O  O   . HOH E 3 .   ? 2.407   12.333  29.678  1.00 24.52  ? 721 HOH A O   1 
HETATM 7498 O  O   . HOH E 3 .   ? -6.610  -25.919 36.248  1.00 30.79  ? 722 HOH A O   1 
HETATM 7499 O  O   . HOH E 3 .   ? -6.040  -23.624 33.040  1.00 35.16  ? 723 HOH A O   1 
HETATM 7500 O  O   . HOH E 3 .   ? 14.852  -4.678  46.097  1.00 24.13  ? 724 HOH A O   1 
HETATM 7501 O  O   . HOH E 3 .   ? 4.636   5.621   27.445  1.00 36.50  ? 725 HOH A O   1 
HETATM 7502 O  O   . HOH E 3 .   ? 4.830   23.302  52.391  1.00 38.22  ? 726 HOH A O   1 
HETATM 7503 O  O   . HOH E 3 .   ? 32.526  -5.842  32.837  1.00 28.97  ? 727 HOH A O   1 
HETATM 7504 O  O   . HOH E 3 .   ? 13.132  -24.382 32.710  1.00 26.02  ? 728 HOH A O   1 
HETATM 7505 O  O   . HOH E 3 .   ? 37.035  3.830   38.808  1.00 24.51  ? 729 HOH A O   1 
HETATM 7506 O  O   . HOH E 3 .   ? 14.720  7.044   77.758  1.00 37.58  ? 730 HOH A O   1 
HETATM 7507 O  O   . HOH E 3 .   ? 6.408   18.456  70.394  1.00 28.90  ? 731 HOH A O   1 
HETATM 7508 O  O   . HOH E 3 .   ? 20.143  5.794   52.529  1.00 30.47  ? 732 HOH A O   1 
HETATM 7509 O  O   . HOH E 3 .   ? 17.374  -14.103 25.611  1.00 16.68  ? 733 HOH A O   1 
HETATM 7510 O  O   . HOH E 3 .   ? 15.398  10.192  60.095  1.00 32.38  ? 734 HOH A O   1 
HETATM 7511 O  O   . HOH E 3 .   ? -5.779  -10.190 27.336  1.00 23.18  ? 735 HOH A O   1 
HETATM 7512 O  O   . HOH E 3 .   ? -4.277  16.239  36.773  1.00 36.51  ? 736 HOH A O   1 
HETATM 7513 O  O   . HOH E 3 .   ? 4.176   19.201  33.145  1.00 32.19  ? 737 HOH A O   1 
HETATM 7514 O  O   . HOH E 3 .   ? 9.964   1.525   55.745  1.00 29.23  ? 738 HOH A O   1 
HETATM 7515 O  O   . HOH E 3 .   ? -8.841  -9.417  51.854  1.00 24.14  ? 739 HOH A O   1 
HETATM 7516 O  O   . HOH E 3 .   ? 7.466   -24.366 38.517  1.00 21.51  ? 740 HOH A O   1 
HETATM 7517 O  O   . HOH E 3 .   ? 28.324  -10.582 53.835  1.00 36.06  ? 741 HOH A O   1 
HETATM 7518 O  O   . HOH E 3 .   ? 18.076  11.378  37.963  1.00 29.65  ? 742 HOH A O   1 
HETATM 7519 O  O   . HOH E 3 .   ? 4.598   0.149   43.078  1.00 15.11  ? 743 HOH A O   1 
HETATM 7520 O  O   . HOH E 3 .   ? 5.103   -3.260  58.110  1.00 19.01  ? 744 HOH A O   1 
HETATM 7521 O  O   . HOH E 3 .   ? 20.863  8.913   47.526  1.00 20.39  ? 745 HOH A O   1 
HETATM 7522 O  O   . HOH E 3 .   ? 8.108   19.065  30.764  1.00 27.66  ? 746 HOH A O   1 
HETATM 7523 O  O   . HOH E 3 .   ? 7.383   -15.834 48.352  1.00 23.42  ? 747 HOH A O   1 
HETATM 7524 O  O   . HOH E 3 .   ? 26.406  12.305  43.634  1.00 29.95  ? 748 HOH A O   1 
HETATM 7525 O  O   . HOH E 3 .   ? 27.923  -23.092 50.727  1.00 31.91  ? 749 HOH A O   1 
HETATM 7526 O  O   . HOH E 3 .   ? 4.812   -22.370 44.791  1.00 22.87  ? 750 HOH A O   1 
HETATM 7527 O  O   . HOH E 3 .   ? 3.863   -8.812  51.494  1.00 34.54  ? 751 HOH A O   1 
HETATM 7528 O  O   . HOH E 3 .   ? 10.174  -28.637 47.550  1.00 43.47  ? 752 HOH A O   1 
HETATM 7529 O  O   . HOH E 3 .   ? 36.234  1.004   48.102  1.00 30.30  ? 753 HOH A O   1 
HETATM 7530 O  O   . HOH E 3 .   ? 22.184  14.889  44.525  1.00 12.50  ? 754 HOH A O   1 
HETATM 7531 O  O   . HOH E 3 .   ? -6.552  -5.915  54.269  1.00 23.75  ? 755 HOH A O   1 
HETATM 7532 O  O   . HOH E 3 .   ? 39.533  4.430   30.623  1.00 46.58  ? 756 HOH A O   1 
HETATM 7533 O  O   . HOH E 3 .   ? -3.737  -25.997 44.393  1.00 25.40  ? 757 HOH A O   1 
HETATM 7534 O  O   . HOH E 3 .   ? 19.547  15.991  67.240  1.00 33.85  ? 758 HOH A O   1 
HETATM 7535 O  O   . HOH E 3 .   ? -5.701  -12.364 25.818  1.00 15.85  ? 759 HOH A O   1 
HETATM 7536 O  O   . HOH E 3 .   ? 23.230  17.352  38.923  1.00 37.47  ? 760 HOH A O   1 
HETATM 7537 O  O   . HOH E 3 .   ? 4.193   16.982  47.795  1.00 27.57  ? 761 HOH A O   1 
HETATM 7538 O  O   . HOH E 3 .   ? 27.572  14.271  44.056  1.00 28.52  ? 762 HOH A O   1 
HETATM 7539 O  O   . HOH E 3 .   ? 9.685   -22.372 31.894  1.00 27.46  ? 763 HOH A O   1 
HETATM 7540 O  O   . HOH E 3 .   ? 37.398  4.045   41.386  1.00 19.06  ? 764 HOH A O   1 
HETATM 7541 O  O   . HOH E 3 .   ? 1.217   -18.603 47.313  1.00 24.07  ? 765 HOH A O   1 
HETATM 7542 O  O   . HOH E 3 .   ? 26.436  -20.170 39.629  1.00 28.08  ? 766 HOH A O   1 
HETATM 7543 O  O   . HOH E 3 .   ? 7.999   10.818  32.131  1.00 72.72  ? 767 HOH A O   1 
HETATM 7544 O  O   . HOH E 3 .   ? -8.957  -6.750  52.939  1.00 28.34  ? 768 HOH A O   1 
HETATM 7545 O  O   . HOH E 3 .   ? 31.221  24.729  52.954  1.00 31.81  ? 769 HOH A O   1 
HETATM 7546 O  O   . HOH E 3 .   ? -11.785 -2.561  50.629  1.00 33.60  ? 770 HOH A O   1 
HETATM 7547 O  O   . HOH E 3 .   ? 6.856   22.491  41.703  1.00 29.90  ? 771 HOH A O   1 
HETATM 7548 O  O   . HOH E 3 .   ? -11.207 -14.102 37.693  1.00 34.84  ? 772 HOH A O   1 
HETATM 7549 O  O   . HOH E 3 .   ? -3.275  4.115   47.256  1.00 21.72  ? 773 HOH A O   1 
HETATM 7550 O  O   . HOH E 3 .   ? -8.993  -9.123  31.337  1.00 25.77  ? 774 HOH A O   1 
HETATM 7551 O  O   . HOH E 3 .   ? 17.532  24.737  57.419  1.00 37.98  ? 775 HOH A O   1 
HETATM 7552 O  O   . HOH E 3 .   ? 37.152  -10.205 39.436  1.00 33.23  ? 776 HOH A O   1 
HETATM 7553 O  O   . HOH E 3 .   ? 9.122   4.385   71.417  1.00 45.21  ? 777 HOH A O   1 
HETATM 7554 O  O   . HOH E 3 .   ? 22.197  12.326  43.969  1.00 17.79  ? 778 HOH A O   1 
HETATM 7555 O  O   . HOH E 3 .   ? 28.259  1.023   58.124  1.00 34.84  ? 779 HOH A O   1 
HETATM 7556 O  O   . HOH E 3 .   ? 8.752   -20.099 47.894  1.00 24.30  ? 780 HOH A O   1 
HETATM 7557 O  O   . HOH E 3 .   ? 17.720  4.315   49.876  1.00 24.69  ? 781 HOH A O   1 
HETATM 7558 O  O   . HOH E 3 .   ? 22.580  18.873  61.170  1.00 30.94  ? 782 HOH A O   1 
HETATM 7559 O  O   . HOH E 3 .   ? 13.547  -12.291 22.159  1.00 24.30  ? 783 HOH A O   1 
HETATM 7560 O  O   . HOH E 3 .   ? 11.241  13.157  36.584  1.00 24.16  ? 784 HOH A O   1 
HETATM 7561 O  O   . HOH E 3 .   ? 23.718  -19.902 60.006  1.00 47.93  ? 785 HOH A O   1 
HETATM 7562 O  O   . HOH E 3 .   ? 11.693  -23.187 51.412  1.00 32.57  ? 786 HOH A O   1 
HETATM 7563 O  O   . HOH E 3 .   ? -11.671 3.238   40.728  1.00 30.89  ? 787 HOH A O   1 
HETATM 7564 O  O   . HOH E 3 .   ? -0.517  -24.649 41.086  1.00 16.16  ? 788 HOH A O   1 
HETATM 7565 O  O   . HOH E 3 .   ? 18.949  -2.181  34.128  1.00 24.55  ? 789 HOH A O   1 
HETATM 7566 O  O   . HOH E 3 .   ? 7.216   -18.340 48.783  1.00 40.55  ? 790 HOH A O   1 
HETATM 7567 O  O   . HOH E 3 .   ? 39.261  -9.069  48.631  1.00 29.58  ? 791 HOH A O   1 
HETATM 7568 O  O   . HOH E 3 .   ? 14.353  7.957   39.093  1.00 15.70  ? 792 HOH A O   1 
HETATM 7569 O  O   . HOH E 3 .   ? 38.157  -2.698  30.747  1.00 30.90  ? 793 HOH A O   1 
HETATM 7570 O  O   . HOH E 3 .   ? 13.012  -9.622  19.795  1.00 23.54  ? 794 HOH A O   1 
HETATM 7571 O  O   . HOH E 3 .   ? 6.831   -0.407  27.816  1.00 34.09  ? 795 HOH A O   1 
HETATM 7572 O  O   . HOH E 3 .   ? 3.509   22.050  36.825  1.00 28.02  ? 796 HOH A O   1 
HETATM 7573 O  O   . HOH E 3 .   ? -11.377 1.824   36.147  1.00 17.02  ? 797 HOH A O   1 
HETATM 7574 O  O   . HOH E 3 .   ? -0.543  -17.351 22.062  1.00 37.52  ? 798 HOH A O   1 
HETATM 7575 O  O   . HOH E 3 .   ? -0.236  -5.513  17.192  1.00 28.51  ? 799 HOH A O   1 
HETATM 7576 O  O   . HOH E 3 .   ? -11.433 -6.522  39.325  1.00 43.82  ? 800 HOH A O   1 
HETATM 7577 O  O   . HOH E 3 .   ? 5.218   5.021   30.751  1.00 23.49  ? 801 HOH A O   1 
HETATM 7578 O  O   . HOH E 3 .   ? -6.222  20.140  39.217  1.00 29.64  ? 802 HOH A O   1 
HETATM 7579 O  O   . HOH E 3 .   ? 23.057  -10.789 29.219  1.00 28.55  ? 803 HOH A O   1 
HETATM 7580 O  O   . HOH E 3 .   ? -7.174  2.933   42.814  1.00 19.70  ? 804 HOH A O   1 
HETATM 7581 O  O   . HOH E 3 .   ? 33.361  8.800   42.173  1.00 33.24  ? 805 HOH A O   1 
HETATM 7582 O  O   . HOH E 3 .   ? 7.375   19.819  68.044  1.00 32.78  ? 806 HOH A O   1 
HETATM 7583 O  O   . HOH E 3 .   ? 3.346   15.482  64.816  1.00 19.66  ? 807 HOH A O   1 
HETATM 7584 O  O   . HOH E 3 .   ? 12.909  -25.956 45.494  1.00 28.98  ? 808 HOH A O   1 
HETATM 7585 O  O   . HOH E 3 .   ? 20.781  -14.798 31.765  1.00 39.51  ? 809 HOH A O   1 
HETATM 7586 O  O   . HOH E 3 .   ? 4.325   0.606   21.314  1.00 65.44  ? 810 HOH A O   1 
HETATM 7587 O  O   . HOH E 3 .   ? 22.611  -13.493 29.565  1.00 33.16  ? 811 HOH A O   1 
HETATM 7588 O  O   . HOH E 3 .   ? 8.530   -2.109  27.799  1.00 37.94  ? 812 HOH A O   1 
HETATM 7589 O  O   . HOH E 3 .   ? 12.671  6.563   70.191  1.00 56.71  ? 813 HOH A O   1 
HETATM 7590 O  O   . HOH E 3 .   ? -7.955  6.012   33.486  1.00 33.35  ? 814 HOH A O   1 
HETATM 7591 O  O   . HOH E 3 .   ? 6.388   -26.209 40.423  1.00 21.16  ? 815 HOH A O   1 
HETATM 7592 O  O   . HOH E 3 .   ? -0.725  13.701  49.458  1.00 51.24  ? 816 HOH A O   1 
HETATM 7593 O  O   . HOH E 3 .   ? 11.415  4.109   32.331  1.00 32.52  ? 817 HOH A O   1 
HETATM 7594 O  O   . HOH E 3 .   ? 2.374   8.628   69.378  1.00 37.14  ? 818 HOH A O   1 
HETATM 7595 O  O   . HOH E 3 .   ? -10.321 -1.492  26.950  1.00 23.45  ? 819 HOH A O   1 
HETATM 7596 O  O   . HOH E 3 .   ? -1.765  -16.094 54.007  1.00 47.84  ? 820 HOH A O   1 
HETATM 7597 O  O   . HOH E 3 .   ? 2.449   -5.766  16.697  1.00 30.90  ? 821 HOH A O   1 
HETATM 7598 O  O   . HOH E 3 .   ? 2.530   12.834  64.174  1.00 32.63  ? 822 HOH A O   1 
HETATM 7599 O  O   . HOH E 3 .   ? 30.912  13.148  44.878  1.00 35.45  ? 823 HOH A O   1 
HETATM 7600 O  O   . HOH E 3 .   ? 21.222  10.135  44.966  1.00 16.42  ? 824 HOH A O   1 
HETATM 7601 O  O   . HOH E 3 .   ? 4.895   19.312  49.973  1.00 32.58  ? 825 HOH A O   1 
HETATM 7602 O  O   . HOH E 3 .   ? 9.721   -11.187 50.709  1.00 32.03  ? 826 HOH A O   1 
HETATM 7603 O  O   . HOH E 3 .   ? 32.577  9.717   39.940  1.00 37.06  ? 827 HOH A O   1 
HETATM 7604 O  O   . HOH E 3 .   ? -8.288  -8.874  26.399  1.00 32.68  ? 828 HOH A O   1 
HETATM 7605 O  O   . HOH E 3 .   ? 6.362   20.050  32.285  1.00 31.17  ? 829 HOH A O   1 
HETATM 7606 O  O   . HOH E 3 .   ? 11.876  6.965   35.986  1.00 20.52  ? 830 HOH A O   1 
HETATM 7607 O  O   . HOH E 3 .   ? -2.565  -14.277 52.002  1.00 31.23  ? 831 HOH A O   1 
HETATM 7608 O  O   . HOH E 3 .   ? -1.473  13.691  25.127  1.00 30.15  ? 832 HOH A O   1 
HETATM 7609 O  O   . HOH E 3 .   ? 11.649  -10.852 17.592  1.00 31.33  ? 833 HOH A O   1 
HETATM 7610 O  O   . HOH E 3 .   ? -12.639 -12.932 36.483  1.00 31.34  ? 834 HOH A O   1 
HETATM 7611 O  O   . HOH E 3 .   ? 3.343   10.500  63.509  1.00 27.74  ? 835 HOH A O   1 
HETATM 7612 O  O   . HOH E 3 .   ? 13.769  -27.726 43.910  1.00 31.53  ? 836 HOH A O   1 
HETATM 7613 O  O   . HOH E 3 .   ? 33.516  -2.883  53.504  1.00 37.72  ? 837 HOH A O   1 
HETATM 7614 O  O   . HOH E 3 .   ? 10.274  19.356  31.535  1.00 35.88  ? 838 HOH A O   1 
HETATM 7615 O  O   . HOH E 3 .   ? 47.097  -6.318  35.370  1.00 30.23  ? 839 HOH A O   1 
HETATM 7616 O  O   . HOH E 3 .   ? -11.748 -2.919  25.502  1.00 36.94  ? 840 HOH A O   1 
HETATM 7617 O  O   . HOH E 3 .   ? 0.770   8.158   61.282  1.00 32.96  ? 841 HOH A O   1 
HETATM 7618 O  O   . HOH E 3 .   ? 23.006  4.913   36.096  1.00 48.27  ? 842 HOH A O   1 
HETATM 7619 O  O   . HOH E 3 .   ? 36.565  -17.377 44.996  1.00 38.67  ? 843 HOH A O   1 
HETATM 7620 O  O   . HOH E 3 .   ? 7.134   -13.929 50.148  1.00 25.09  ? 844 HOH A O   1 
HETATM 7621 O  O   . HOH E 3 .   ? 5.878   23.996  45.906  1.00 40.66  ? 845 HOH A O   1 
HETATM 7622 O  O   . HOH E 3 .   ? -4.651  -13.299 23.145  1.00 21.35  ? 846 HOH A O   1 
HETATM 7623 O  O   . HOH E 3 .   ? 19.204  -4.298  49.846  1.00 34.06  ? 847 HOH A O   1 
HETATM 7624 O  O   . HOH E 3 .   ? 2.416   -3.826  58.700  1.00 33.77  ? 848 HOH A O   1 
HETATM 7625 O  O   . HOH E 3 .   ? -6.286  4.060   46.040  1.00 42.12  ? 849 HOH A O   1 
HETATM 7626 O  O   . HOH E 3 .   ? -1.658  7.018   57.090  1.00 41.73  ? 850 HOH A O   1 
HETATM 7627 O  O   . HOH E 3 .   ? 11.208  18.833  74.597  1.00 30.91  ? 851 HOH A O   1 
HETATM 7628 O  O   . HOH E 3 .   ? -1.218  -22.362 45.543  1.00 21.13  ? 852 HOH A O   1 
HETATM 7629 O  O   . HOH E 3 .   ? 36.703  6.478   42.234  1.00 24.91  ? 853 HOH A O   1 
HETATM 7630 O  O   . HOH E 3 .   ? 7.684   -8.352  16.917  1.00 42.25  ? 854 HOH A O   1 
HETATM 7631 O  O   . HOH E 3 .   ? 15.038  -8.413  19.450  1.00 41.43  ? 855 HOH A O   1 
HETATM 7632 O  O   . HOH E 3 .   ? 16.754  -10.579 21.088  1.00 41.92  ? 856 HOH A O   1 
HETATM 7633 O  O   . HOH E 3 .   ? 4.088   21.796  49.018  1.00 41.07  ? 857 HOH A O   1 
HETATM 7634 O  O   . HOH E 3 .   ? 0.768   14.373  28.962  1.00 35.15  ? 858 HOH A O   1 
HETATM 7635 O  O   . HOH E 3 .   ? 8.797   8.449   32.876  1.00 37.10  ? 859 HOH A O   1 
HETATM 7636 O  O   . HOH E 3 .   ? 11.935  3.195   56.608  1.00 34.88  ? 860 HOH A O   1 
HETATM 7637 O  O   . HOH E 3 .   ? 9.632   21.549  33.415  1.00 39.40  ? 861 HOH A O   1 
HETATM 7638 O  O   . HOH E 3 .   ? -7.991  -13.066 24.750  1.00 35.12  ? 862 HOH A O   1 
HETATM 7639 O  O   . HOH E 3 .   ? 39.493  5.610   41.698  1.00 27.91  ? 863 HOH A O   1 
HETATM 7640 O  O   . HOH E 3 .   ? 6.613   -16.203 55.212  1.00 48.55  ? 864 HOH A O   1 
HETATM 7641 O  O   . HOH E 3 .   ? 11.371  3.810   74.443  1.00 32.50  ? 865 HOH A O   1 
HETATM 7642 O  O   . HOH E 3 .   ? 8.640   -22.098 25.415  1.00 41.14  ? 866 HOH A O   1 
HETATM 7643 O  O   . HOH F 3 .   ? -6.972  -4.938  15.056  1.00 28.14  ? 601 HOH B O   1 
HETATM 7644 O  O   . HOH F 3 .   ? 14.094  20.930  10.287  1.00 34.29  ? 602 HOH B O   1 
HETATM 7645 O  O   . HOH F 3 .   ? -19.793 11.078  -9.704  1.00 28.12  ? 603 HOH B O   1 
HETATM 7646 O  O   . HOH F 3 .   ? 9.012   26.063  5.030   1.00 43.56  ? 604 HOH B O   1 
HETATM 7647 O  O   . HOH F 3 .   ? 1.673   36.786  27.990  1.00 23.51  ? 605 HOH B O   1 
HETATM 7648 O  O   . HOH F 3 .   ? -5.898  11.235  0.790   1.00 38.38  ? 606 HOH B O   1 
HETATM 7649 O  O   . HOH F 3 .   ? -33.578 24.545  17.283  1.00 29.59  ? 607 HOH B O   1 
HETATM 7650 O  O   . HOH F 3 .   ? -13.536 44.213  29.926  1.00 20.96  ? 608 HOH B O   1 
HETATM 7651 O  O   . HOH F 3 .   ? -8.123  4.737   -16.838 1.00 35.47  ? 609 HOH B O   1 
HETATM 7652 O  O   . HOH F 3 .   ? -30.378 47.352  16.653  1.00 36.64  ? 610 HOH B O   1 
HETATM 7653 O  O   . HOH F 3 .   ? -13.289 49.014  25.338  1.00 16.60  ? 611 HOH B O   1 
HETATM 7654 O  O   . HOH F 3 .   ? 13.041  14.927  16.770  1.00 17.60  ? 612 HOH B O   1 
HETATM 7655 O  O   . HOH F 3 .   ? -2.801  34.982  32.683  1.00 30.80  ? 613 HOH B O   1 
HETATM 7656 O  O   . HOH F 3 .   ? 11.666  41.380  15.186  1.00 36.99  ? 614 HOH B O   1 
HETATM 7657 O  O   . HOH F 3 .   ? -2.845  32.985  -0.415  1.00 55.27  ? 615 HOH B O   1 
HETATM 7658 O  O   . HOH F 3 .   ? 2.611   16.388  21.521  1.00 17.49  ? 616 HOH B O   1 
HETATM 7659 O  O   . HOH F 3 .   ? -30.258 30.504  9.891   1.00 27.72  ? 617 HOH B O   1 
HETATM 7660 O  O   . HOH F 3 .   ? -20.265 25.743  4.495   1.00 28.30  ? 618 HOH B O   1 
HETATM 7661 O  O   . HOH F 3 .   ? -8.563  -7.002  14.449  1.00 26.93  ? 619 HOH B O   1 
HETATM 7662 O  O   . HOH F 3 .   ? -31.448 40.015  14.988  1.00 30.29  ? 620 HOH B O   1 
HETATM 7663 O  O   . HOH F 3 .   ? -28.861 13.523  24.794  1.00 28.53  ? 621 HOH B O   1 
HETATM 7664 O  O   . HOH F 3 .   ? -5.975  -0.844  25.016  1.00 15.45  ? 622 HOH B O   1 
HETATM 7665 O  O   . HOH F 3 .   ? -2.051  0.825   19.842  1.00 30.19  ? 623 HOH B O   1 
HETATM 7666 O  O   . HOH F 3 .   ? -9.976  6.421   27.255  1.00 31.36  ? 624 HOH B O   1 
HETATM 7667 O  O   . HOH F 3 .   ? -27.764 31.641  9.102   1.00 27.19  ? 625 HOH B O   1 
HETATM 7668 O  O   . HOH F 3 .   ? -27.731 26.910  7.292   1.00 22.66  ? 626 HOH B O   1 
HETATM 7669 O  O   . HOH F 3 .   ? -11.550 29.480  4.268   1.00 61.21  ? 627 HOH B O   1 
HETATM 7670 O  O   . HOH F 3 .   ? -17.711 29.406  9.707   1.00 35.98  ? 628 HOH B O   1 
HETATM 7671 O  O   . HOH F 3 .   ? 5.374   -0.771  10.930  1.00 24.04  ? 629 HOH B O   1 
HETATM 7672 O  O   . HOH F 3 .   ? -29.861 49.079  24.139  1.00 24.96  ? 630 HOH B O   1 
HETATM 7673 O  O   . HOH F 3 .   ? -27.713 26.006  39.524  1.00 31.85  ? 631 HOH B O   1 
HETATM 7674 O  O   . HOH F 3 .   ? 3.302   20.062  30.142  1.00 25.83  ? 632 HOH B O   1 
HETATM 7675 O  O   . HOH F 3 .   ? 14.369  35.041  18.109  1.00 37.01  ? 633 HOH B O   1 
HETATM 7676 O  O   . HOH F 3 .   ? 16.762  28.598  30.115  1.00 49.29  ? 634 HOH B O   1 
HETATM 7677 O  O   . HOH F 3 .   ? -18.094 26.835  43.242  1.00 24.52  ? 635 HOH B O   1 
HETATM 7678 O  O   . HOH F 3 .   ? -23.782 31.573  39.868  1.00 19.37  ? 636 HOH B O   1 
HETATM 7679 O  O   . HOH F 3 .   ? 1.430   2.748   -0.807  1.00 34.39  ? 637 HOH B O   1 
HETATM 7680 O  O   . HOH F 3 .   ? -16.706 13.627  33.067  1.00 23.37  ? 638 HOH B O   1 
HETATM 7681 O  O   . HOH F 3 .   ? 24.075  17.847  23.153  1.00 23.95  ? 639 HOH B O   1 
HETATM 7682 O  O   . HOH F 3 .   ? -34.301 35.602  22.867  1.00 29.11  ? 640 HOH B O   1 
HETATM 7683 O  O   . HOH F 3 .   ? -9.573  44.026  11.159  1.00 32.85  ? 641 HOH B O   1 
HETATM 7684 O  O   . HOH F 3 .   ? 1.102   16.611  15.502  1.00 14.66  ? 642 HOH B O   1 
HETATM 7685 O  O   . HOH F 3 .   ? 1.537   30.497  32.300  1.00 23.66  ? 643 HOH B O   1 
HETATM 7686 O  O   . HOH F 3 .   ? -30.673 30.575  14.844  1.00 18.51  ? 644 HOH B O   1 
HETATM 7687 O  O   . HOH F 3 .   ? 16.434  24.942  16.617  1.00 28.17  ? 645 HOH B O   1 
HETATM 7688 O  O   . HOH F 3 .   ? -25.445 14.143  14.532  1.00 33.05  ? 646 HOH B O   1 
HETATM 7689 O  O   . HOH F 3 .   ? -33.955 23.725  20.038  1.00 23.72  ? 647 HOH B O   1 
HETATM 7690 O  O   . HOH F 3 .   ? -7.266  25.933  18.469  1.00 21.71  ? 648 HOH B O   1 
HETATM 7691 O  O   . HOH F 3 .   ? 19.326  31.603  16.161  1.00 38.68  ? 649 HOH B O   1 
HETATM 7692 O  O   . HOH F 3 .   ? -26.060 20.259  36.220  1.00 27.02  ? 650 HOH B O   1 
HETATM 7693 O  O   . HOH F 3 .   ? -6.821  41.014  22.297  1.00 15.28  ? 651 HOH B O   1 
HETATM 7694 O  O   . HOH F 3 .   ? -15.034 18.577  36.698  1.00 28.52  ? 652 HOH B O   1 
HETATM 7695 O  O   . HOH F 3 .   ? -20.917 9.516   8.669   1.00 28.37  ? 653 HOH B O   1 
HETATM 7696 O  O   . HOH F 3 .   ? 11.384  25.458  28.254  1.00 22.53  ? 654 HOH B O   1 
HETATM 7697 O  O   . HOH F 3 .   ? 1.123   29.845  37.951  1.00 35.46  ? 655 HOH B O   1 
HETATM 7698 O  O   . HOH F 3 .   ? -11.304 20.038  4.992   1.00 35.17  ? 656 HOH B O   1 
HETATM 7699 O  O   . HOH F 3 .   ? -6.884  30.090  21.885  1.00 15.29  ? 657 HOH B O   1 
HETATM 7700 O  O   . HOH F 3 .   ? -10.288 34.719  38.101  1.00 30.93  ? 658 HOH B O   1 
HETATM 7701 O  O   . HOH F 3 .   ? -2.063  21.494  26.913  1.00 23.96  ? 659 HOH B O   1 
HETATM 7702 O  O   . HOH F 3 .   ? -3.731  33.341  36.343  1.00 19.35  ? 660 HOH B O   1 
HETATM 7703 O  O   . HOH F 3 .   ? -6.094  23.370  33.180  1.00 40.17  ? 661 HOH B O   1 
HETATM 7704 O  O   . HOH F 3 .   ? 16.206  26.146  12.534  1.00 32.51  ? 662 HOH B O   1 
HETATM 7705 O  O   . HOH F 3 .   ? 13.975  26.319  11.368  1.00 29.48  ? 663 HOH B O   1 
HETATM 7706 O  O   . HOH F 3 .   ? -1.718  0.452   24.179  1.00 37.25  ? 664 HOH B O   1 
HETATM 7707 O  O   . HOH F 3 .   ? 8.739   7.081   15.013  1.00 39.25  ? 665 HOH B O   1 
HETATM 7708 O  O   . HOH F 3 .   ? -1.602  29.103  -18.788 1.00 44.54  ? 666 HOH B O   1 
HETATM 7709 O  O   . HOH F 3 .   ? 0.620   -4.323  0.604   1.00 37.10  ? 667 HOH B O   1 
HETATM 7710 O  O   . HOH F 3 .   ? -27.882 29.692  30.281  1.00 23.07  ? 668 HOH B O   1 
HETATM 7711 O  O   . HOH F 3 .   ? -12.831 4.072   6.171   1.00 15.29  ? 669 HOH B O   1 
HETATM 7712 O  O   . HOH F 3 .   ? -26.737 18.376  13.337  1.00 31.67  ? 670 HOH B O   1 
HETATM 7713 O  O   . HOH F 3 .   ? -26.768 32.054  36.099  1.00 18.11  ? 671 HOH B O   1 
HETATM 7714 O  O   . HOH F 3 .   ? 0.395   23.971  39.528  1.00 23.47  ? 672 HOH B O   1 
HETATM 7715 O  O   . HOH F 3 .   ? -13.618 -1.854  17.973  1.00 33.21  ? 673 HOH B O   1 
HETATM 7716 O  O   . HOH F 3 .   ? -12.325 29.220  43.774  1.00 26.90  ? 674 HOH B O   1 
HETATM 7717 O  O   . HOH F 3 .   ? -11.717 42.100  30.239  1.00 24.85  ? 675 HOH B O   1 
HETATM 7718 O  O   . HOH F 3 .   ? -25.670 38.292  32.810  1.00 16.41  ? 676 HOH B O   1 
HETATM 7719 O  O   . HOH F 3 .   ? -29.075 21.701  11.737  1.00 24.43  ? 677 HOH B O   1 
HETATM 7720 O  O   . HOH F 3 .   ? -13.760 -1.474  4.235   1.00 20.03  ? 678 HOH B O   1 
HETATM 7721 O  O   . HOH F 3 .   ? -18.771 16.825  0.224   1.00 40.29  ? 679 HOH B O   1 
HETATM 7722 O  O   . HOH F 3 .   ? -2.933  15.766  23.616  1.00 17.52  ? 680 HOH B O   1 
HETATM 7723 O  O   . HOH F 3 .   ? -21.648 38.632  16.884  1.00 17.97  ? 681 HOH B O   1 
HETATM 7724 O  O   . HOH F 3 .   ? -23.410 13.776  11.652  1.00 28.75  ? 682 HOH B O   1 
HETATM 7725 O  O   . HOH F 3 .   ? -27.223 29.643  34.488  1.00 17.79  ? 683 HOH B O   1 
HETATM 7726 O  O   . HOH F 3 .   ? -32.826 24.976  27.907  1.00 21.15  ? 684 HOH B O   1 
HETATM 7727 O  O   . HOH F 3 .   ? -14.007 -1.170  15.470  1.00 20.46  ? 685 HOH B O   1 
HETATM 7728 O  O   . HOH F 3 .   ? -4.821  39.032  22.030  1.00 14.19  ? 686 HOH B O   1 
HETATM 7729 O  O   . HOH F 3 .   ? -0.323  -2.831  17.472  1.00 21.99  ? 687 HOH B O   1 
HETATM 7730 O  O   . HOH F 3 .   ? 14.589  28.118  23.183  1.00 22.32  ? 688 HOH B O   1 
HETATM 7731 O  O   . HOH F 3 .   ? -15.912 16.579  32.447  1.00 18.57  ? 689 HOH B O   1 
HETATM 7732 O  O   . HOH F 3 .   ? -19.577 -1.313  0.466   1.00 45.87  ? 690 HOH B O   1 
HETATM 7733 O  O   . HOH F 3 .   ? -18.270 19.841  40.199  1.00 35.89  ? 691 HOH B O   1 
HETATM 7734 O  O   . HOH F 3 .   ? 0.408   19.430  26.790  1.00 31.42  ? 692 HOH B O   1 
HETATM 7735 O  O   . HOH F 3 .   ? 7.044   31.734  7.492   1.00 26.19  ? 693 HOH B O   1 
HETATM 7736 O  O   . HOH F 3 .   ? -7.611  42.979  23.974  1.00 18.50  ? 694 HOH B O   1 
HETATM 7737 O  O   . HOH F 3 .   ? 9.232   21.972  15.853  1.00 15.55  ? 695 HOH B O   1 
HETATM 7738 O  O   . HOH F 3 .   ? 4.183   23.846  12.339  1.00 21.74  ? 696 HOH B O   1 
HETATM 7739 O  O   . HOH F 3 .   ? -10.373 42.411  21.799  1.00 19.14  ? 697 HOH B O   1 
HETATM 7740 O  O   . HOH F 3 .   ? 4.262   18.467  21.211  1.00 18.20  ? 698 HOH B O   1 
HETATM 7741 O  O   . HOH F 3 .   ? -25.083 46.454  18.548  1.00 22.76  ? 699 HOH B O   1 
HETATM 7742 O  O   . HOH F 3 .   ? 0.854   5.213   0.580   1.00 25.91  ? 700 HOH B O   1 
HETATM 7743 O  O   . HOH F 3 .   ? -1.149  15.526  7.675   1.00 39.06  ? 701 HOH B O   1 
HETATM 7744 O  O   . HOH F 3 .   ? -22.838 40.935  33.311  1.00 32.17  ? 702 HOH B O   1 
HETATM 7745 O  O   . HOH F 3 .   ? -15.832 14.758  29.886  1.00 39.98  ? 703 HOH B O   1 
HETATM 7746 O  O   . HOH F 3 .   ? -32.345 19.106  31.825  1.00 18.24  ? 704 HOH B O   1 
HETATM 7747 O  O   . HOH F 3 .   ? -12.478 25.010  13.450  1.00 30.66  ? 705 HOH B O   1 
HETATM 7748 O  O   . HOH F 3 .   ? -23.526 40.512  17.434  1.00 22.66  ? 706 HOH B O   1 
HETATM 7749 O  O   . HOH F 3 .   ? -19.993 42.279  15.814  1.00 23.72  ? 707 HOH B O   1 
HETATM 7750 O  O   . HOH F 3 .   ? -9.962  17.056  15.966  1.00 14.87  ? 708 HOH B O   1 
HETATM 7751 O  O   . HOH F 3 .   ? -0.568  6.387   21.207  1.00 42.75  ? 709 HOH B O   1 
HETATM 7752 O  O   . HOH F 3 .   ? -3.027  -3.281  1.739   1.00 29.58  ? 710 HOH B O   1 
HETATM 7753 O  O   . HOH F 3 .   ? -28.735 13.737  27.510  1.00 29.31  ? 711 HOH B O   1 
HETATM 7754 O  O   . HOH F 3 .   ? -19.767 -3.736  20.633  1.00 37.75  ? 712 HOH B O   1 
HETATM 7755 O  O   . HOH F 3 .   ? -17.165 -2.315  1.472   1.00 38.47  ? 713 HOH B O   1 
HETATM 7756 O  O   . HOH F 3 .   ? 7.232   11.877  11.276  1.00 16.77  ? 714 HOH B O   1 
HETATM 7757 O  O   . HOH F 3 .   ? -30.497 29.000  31.316  1.00 34.60  ? 715 HOH B O   1 
HETATM 7758 O  O   . HOH F 3 .   ? -20.308 32.138  9.480   1.00 29.94  ? 716 HOH B O   1 
HETATM 7759 O  O   . HOH F 3 .   ? -8.176  38.784  34.603  1.00 28.74  ? 717 HOH B O   1 
HETATM 7760 O  O   . HOH F 3 .   ? -1.127  13.010  16.349  1.00 11.93  ? 718 HOH B O   1 
HETATM 7761 O  O   . HOH F 3 .   ? -26.815 39.481  23.595  1.00 27.91  ? 719 HOH B O   1 
HETATM 7762 O  O   . HOH F 3 .   ? -14.575 5.043   18.423  1.00 18.26  ? 720 HOH B O   1 
HETATM 7763 O  O   . HOH F 3 .   ? -1.560  20.783  29.348  1.00 20.62  ? 721 HOH B O   1 
HETATM 7764 O  O   . HOH F 3 .   ? 15.297  19.878  12.554  1.00 24.51  ? 722 HOH B O   1 
HETATM 7765 O  O   . HOH F 3 .   ? 2.288   3.303   20.753  1.00 26.87  ? 723 HOH B O   1 
HETATM 7766 O  O   . HOH F 3 .   ? -18.934 11.181  -0.885  1.00 23.29  ? 724 HOH B O   1 
HETATM 7767 O  O   . HOH F 3 .   ? 1.375   12.496  2.220   1.00 34.38  ? 725 HOH B O   1 
HETATM 7768 O  O   . HOH F 3 .   ? -34.021 28.262  20.836  1.00 29.80  ? 726 HOH B O   1 
HETATM 7769 O  O   . HOH F 3 .   ? -16.529 20.250  17.904  1.00 14.75  ? 727 HOH B O   1 
HETATM 7770 O  O   . HOH F 3 .   ? -19.176 35.684  35.902  1.00 24.32  ? 728 HOH B O   1 
HETATM 7771 O  O   . HOH F 3 .   ? -0.878  14.129  10.207  1.00 15.23  ? 729 HOH B O   1 
HETATM 7772 O  O   . HOH F 3 .   ? -20.627 1.570   13.224  1.00 24.83  ? 730 HOH B O   1 
HETATM 7773 O  O   . HOH F 3 .   ? 8.056   11.053  23.465  1.00 23.49  ? 731 HOH B O   1 
HETATM 7774 O  O   . HOH F 3 .   ? -21.682 36.382  39.895  1.00 30.27  ? 732 HOH B O   1 
HETATM 7775 O  O   . HOH F 3 .   ? -4.052  44.652  17.211  1.00 28.74  ? 733 HOH B O   1 
HETATM 7776 O  O   . HOH F 3 .   ? 5.197   40.243  22.477  1.00 25.94  ? 734 HOH B O   1 
HETATM 7777 O  O   . HOH F 3 .   ? -16.252 24.346  2.899   1.00 22.93  ? 735 HOH B O   1 
HETATM 7778 O  O   . HOH F 3 .   ? -17.371 32.181  39.459  1.00 19.48  ? 736 HOH B O   1 
HETATM 7779 O  O   . HOH F 3 .   ? -14.388 45.047  27.082  1.00 23.79  ? 737 HOH B O   1 
HETATM 7780 O  O   . HOH F 3 .   ? -19.961 25.262  0.476   1.00 47.87  ? 738 HOH B O   1 
HETATM 7781 O  O   . HOH F 3 .   ? -14.564 26.264  2.555   1.00 35.66  ? 739 HOH B O   1 
HETATM 7782 O  O   . HOH F 3 .   ? -10.206 3.860   35.079  1.00 30.52  ? 740 HOH B O   1 
HETATM 7783 O  O   . HOH F 3 .   ? -9.693  39.043  14.646  1.00 28.00  ? 741 HOH B O   1 
HETATM 7784 O  O   . HOH F 3 .   ? -11.919 22.327  -0.833  1.00 38.52  ? 742 HOH B O   1 
HETATM 7785 O  O   . HOH F 3 .   ? -22.385 20.885  5.801   1.00 22.58  ? 743 HOH B O   1 
HETATM 7786 O  O   . HOH F 3 .   ? 15.972  16.543  21.485  1.00 19.21  ? 744 HOH B O   1 
HETATM 7787 O  O   . HOH F 3 .   ? -10.521 32.907  26.833  1.00 23.31  ? 745 HOH B O   1 
HETATM 7788 O  O   . HOH F 3 .   ? 9.194   17.589  4.173   1.00 26.77  ? 746 HOH B O   1 
HETATM 7789 O  O   . HOH F 3 .   ? 16.108  30.536  22.074  1.00 33.20  ? 747 HOH B O   1 
HETATM 7790 O  O   . HOH F 3 .   ? -22.762 33.473  11.806  1.00 21.13  ? 748 HOH B O   1 
HETATM 7791 O  O   . HOH F 3 .   ? -10.834 15.324  25.953  1.00 18.64  ? 749 HOH B O   1 
HETATM 7792 O  O   . HOH F 3 .   ? -13.781 44.527  24.128  1.00 17.77  ? 750 HOH B O   1 
HETATM 7793 O  O   . HOH F 3 .   ? -18.974 7.294   30.907  1.00 29.96  ? 751 HOH B O   1 
HETATM 7794 O  O   . HOH F 3 .   ? 11.770  20.139  29.101  1.00 33.16  ? 752 HOH B O   1 
HETATM 7795 O  O   . HOH F 3 .   ? -13.162 33.757  41.497  1.00 30.82  ? 753 HOH B O   1 
HETATM 7796 O  O   . HOH F 3 .   ? -20.076 39.533  14.716  1.00 23.71  ? 754 HOH B O   1 
HETATM 7797 O  O   . HOH F 3 .   ? -21.979 5.989   23.935  1.00 19.55  ? 755 HOH B O   1 
HETATM 7798 O  O   . HOH F 3 .   ? -4.963  -5.427  1.198   1.00 55.26  ? 756 HOH B O   1 
HETATM 7799 O  O   . HOH F 3 .   ? -4.634  30.637  38.548  1.00 43.73  ? 757 HOH B O   1 
HETATM 7800 O  O   . HOH F 3 .   ? -9.851  7.038   23.329  1.00 18.27  ? 758 HOH B O   1 
HETATM 7801 O  O   . HOH F 3 .   ? -28.497 17.530  18.215  1.00 18.52  ? 759 HOH B O   1 
HETATM 7802 O  O   . HOH F 3 .   ? -6.549  6.551   23.578  1.00 20.44  ? 760 HOH B O   1 
HETATM 7803 O  O   . HOH F 3 .   ? 10.102  -3.494  6.385   1.00 25.66  ? 761 HOH B O   1 
HETATM 7804 O  O   . HOH F 3 .   ? -2.764  -1.193  0.347   1.00 26.06  ? 762 HOH B O   1 
HETATM 7805 O  O   . HOH F 3 .   ? -29.304 15.008  20.222  1.00 21.35  ? 763 HOH B O   1 
HETATM 7806 O  O   . HOH F 3 .   ? 1.154   5.901   15.441  1.00 13.32  ? 764 HOH B O   1 
HETATM 7807 O  O   . HOH F 3 .   ? -6.273  25.282  14.847  1.00 29.06  ? 765 HOH B O   1 
HETATM 7808 O  O   . HOH F 3 .   ? -32.732 23.627  10.658  1.00 26.00  ? 766 HOH B O   1 
HETATM 7809 O  O   . HOH F 3 .   ? -13.308 2.004   -7.899  1.00 28.05  ? 767 HOH B O   1 
HETATM 7810 O  O   . HOH F 3 .   ? -8.819  4.590   -12.436 1.00 30.94  ? 768 HOH B O   1 
HETATM 7811 O  O   . HOH F 3 .   ? -20.387 26.064  44.431  1.00 33.72  ? 769 HOH B O   1 
HETATM 7812 O  O   . HOH F 3 .   ? -13.671 20.427  30.660  1.00 33.51  ? 770 HOH B O   1 
HETATM 7813 O  O   . HOH F 3 .   ? 16.237  16.777  19.031  1.00 20.29  ? 771 HOH B O   1 
HETATM 7814 O  O   . HOH F 3 .   ? -13.680 18.417  27.690  1.00 28.43  ? 772 HOH B O   1 
HETATM 7815 O  O   . HOH F 3 .   ? -13.667 36.296  13.528  1.00 22.96  ? 773 HOH B O   1 
HETATM 7816 O  O   . HOH F 3 .   ? -6.592  13.079  25.539  1.00 40.73  ? 774 HOH B O   1 
HETATM 7817 O  O   . HOH F 3 .   ? -0.204  12.064  12.794  1.00 15.35  ? 775 HOH B O   1 
HETATM 7818 O  O   . HOH F 3 .   ? -22.062 4.429   12.232  1.00 32.05  ? 776 HOH B O   1 
HETATM 7819 O  O   . HOH F 3 .   ? -30.420 12.558  22.803  1.00 39.05  ? 777 HOH B O   1 
HETATM 7820 O  O   . HOH F 3 .   ? -30.167 27.872  8.515   1.00 22.47  ? 778 HOH B O   1 
HETATM 7821 O  O   . HOH F 3 .   ? 11.467  31.219  9.947   1.00 28.75  ? 779 HOH B O   1 
HETATM 7822 O  O   . HOH F 3 .   ? -13.651 25.842  8.508   1.00 32.24  ? 780 HOH B O   1 
HETATM 7823 O  O   . HOH F 3 .   ? -27.656 7.505   15.774  1.00 24.35  ? 781 HOH B O   1 
HETATM 7824 O  O   . HOH F 3 .   ? -1.879  6.092   -7.539  1.00 36.02  ? 782 HOH B O   1 
HETATM 7825 O  O   . HOH F 3 .   ? -15.164 47.709  27.217  1.00 23.74  ? 783 HOH B O   1 
HETATM 7826 O  O   . HOH F 3 .   ? 9.064   32.318  9.538   1.00 35.05  ? 784 HOH B O   1 
HETATM 7827 O  O   . HOH F 3 .   ? -32.617 47.333  23.710  1.00 35.81  ? 785 HOH B O   1 
HETATM 7828 O  O   . HOH F 3 .   ? -21.845 45.127  21.614  1.00 20.79  ? 786 HOH B O   1 
HETATM 7829 O  O   . HOH F 3 .   ? 3.619   42.040  21.894  1.00 38.85  ? 787 HOH B O   1 
HETATM 7830 O  O   . HOH F 3 .   ? -0.557  11.617  23.992  1.00 24.08  ? 788 HOH B O   1 
HETATM 7831 O  O   . HOH F 3 .   ? -12.030 4.497   -14.306 1.00 17.43  ? 789 HOH B O   1 
HETATM 7832 O  O   . HOH F 3 .   ? -6.777  12.517  21.103  1.00 22.22  ? 790 HOH B O   1 
HETATM 7833 O  O   . HOH F 3 .   ? -16.309 -2.295  7.513   1.00 20.51  ? 791 HOH B O   1 
HETATM 7834 O  O   . HOH F 3 .   ? -0.097  3.438   21.403  1.00 37.94  ? 792 HOH B O   1 
HETATM 7835 O  O   . HOH F 3 .   ? -28.097 38.358  20.993  1.00 18.83  ? 793 HOH B O   1 
HETATM 7836 O  O   . HOH F 3 .   ? 10.415  8.720   13.620  1.00 36.42  ? 794 HOH B O   1 
HETATM 7837 O  O   . HOH F 3 .   ? -2.301  13.600  1.716   1.00 39.42  ? 795 HOH B O   1 
HETATM 7838 O  O   . HOH F 3 .   ? 1.096   8.655   16.159  1.00 16.01  ? 796 HOH B O   1 
HETATM 7839 O  O   . HOH F 3 .   ? 18.032  30.278  12.915  1.00 32.15  ? 797 HOH B O   1 
HETATM 7840 O  O   . HOH F 3 .   ? -9.454  -1.384  22.608  1.00 33.71  ? 798 HOH B O   1 
HETATM 7841 O  O   . HOH F 3 .   ? -17.735 5.875   -4.623  1.00 21.71  ? 799 HOH B O   1 
HETATM 7842 O  O   . HOH F 3 .   ? -31.429 40.195  21.469  1.00 42.34  ? 800 HOH B O   1 
HETATM 7843 O  O   . HOH F 3 .   ? 5.710   8.946   16.766  1.00 22.22  ? 801 HOH B O   1 
HETATM 7844 O  O   . HOH F 3 .   ? -24.499 16.836  13.371  1.00 30.77  ? 802 HOH B O   1 
HETATM 7845 O  O   . HOH F 3 .   ? -32.666 18.252  24.784  1.00 22.77  ? 803 HOH B O   1 
HETATM 7846 O  O   . HOH F 3 .   ? -8.604  -0.409  24.936  1.00 18.74  ? 804 HOH B O   1 
HETATM 7847 O  O   . HOH F 3 .   ? -12.631 14.697  30.033  1.00 33.49  ? 805 HOH B O   1 
HETATM 7848 O  O   . HOH F 3 .   ? -16.310 43.091  17.470  1.00 21.96  ? 806 HOH B O   1 
HETATM 7849 O  O   . HOH F 3 .   ? 17.289  22.444  30.136  1.00 26.55  ? 807 HOH B O   1 
HETATM 7850 O  O   . HOH F 3 .   ? 4.252   29.434  30.221  1.00 27.97  ? 808 HOH B O   1 
HETATM 7851 O  O   . HOH F 3 .   ? -2.829  9.406   22.375  1.00 34.01  ? 809 HOH B O   1 
HETATM 7852 O  O   . HOH F 3 .   ? 1.381   33.436  32.059  1.00 26.60  ? 810 HOH B O   1 
HETATM 7853 O  O   . HOH F 3 .   ? 3.128   9.842   17.601  1.00 18.82  ? 811 HOH B O   1 
HETATM 7854 O  O   . HOH F 3 .   ? -5.763  16.051  -0.955  1.00 52.96  ? 812 HOH B O   1 
HETATM 7855 O  O   . HOH F 3 .   ? -22.538 16.483  7.004   1.00 32.32  ? 813 HOH B O   1 
HETATM 7856 O  O   . HOH F 3 .   ? -16.294 28.120  44.439  1.00 24.93  ? 814 HOH B O   1 
HETATM 7857 O  O   . HOH F 3 .   ? -16.929 3.659   12.160  1.00 31.48  ? 815 HOH B O   1 
HETATM 7858 O  O   . HOH F 3 .   ? -31.212 17.913  18.192  1.00 30.85  ? 816 HOH B O   1 
HETATM 7859 O  O   . HOH F 3 .   ? 6.582   6.810   15.884  1.00 24.05  ? 817 HOH B O   1 
HETATM 7860 O  O   . HOH F 3 .   ? 23.861  18.752  20.991  1.00 42.82  ? 818 HOH B O   1 
HETATM 7861 O  O   . HOH F 3 .   ? -14.268 44.986  32.218  1.00 36.68  ? 819 HOH B O   1 
HETATM 7862 O  O   . HOH F 3 .   ? -20.843 19.452  38.995  1.00 45.84  ? 820 HOH B O   1 
HETATM 7863 O  O   . HOH F 3 .   ? -26.158 0.214   16.701  1.00 55.40  ? 821 HOH B O   1 
HETATM 7864 O  O   . HOH F 3 .   ? -7.765  31.599  39.764  1.00 23.80  ? 822 HOH B O   1 
HETATM 7865 O  O   . HOH F 3 .   ? -13.506 -3.879  4.542   1.00 30.09  ? 823 HOH B O   1 
HETATM 7866 O  O   . HOH F 3 .   ? -12.159 40.669  14.258  1.00 28.23  ? 824 HOH B O   1 
HETATM 7867 O  O   . HOH F 3 .   ? -13.647 38.940  12.779  1.00 50.58  ? 825 HOH B O   1 
HETATM 7868 O  O   . HOH F 3 .   ? -17.711 3.053   8.402   1.00 35.26  ? 826 HOH B O   1 
HETATM 7869 O  O   . HOH F 3 .   ? -20.328 15.166  1.435   1.00 37.99  ? 827 HOH B O   1 
HETATM 7870 O  O   . HOH F 3 .   ? -12.443 21.801  32.959  1.00 33.29  ? 828 HOH B O   1 
HETATM 7871 O  O   . HOH F 3 .   ? -8.250  28.818  41.659  1.00 22.18  ? 829 HOH B O   1 
HETATM 7872 O  O   . HOH F 3 .   ? -16.743 0.665   24.156  1.00 35.10  ? 830 HOH B O   1 
HETATM 7873 O  O   . HOH F 3 .   ? -16.439 0.727   12.383  1.00 50.54  ? 831 HOH B O   1 
HETATM 7874 O  O   . HOH F 3 .   ? 8.643   13.354  2.848   1.00 39.81  ? 832 HOH B O   1 
HETATM 7875 O  O   . HOH F 3 .   ? 16.241  33.265  21.251  1.00 30.19  ? 833 HOH B O   1 
HETATM 7876 O  O   . HOH F 3 .   ? -32.687 33.992  23.946  1.00 39.42  ? 834 HOH B O   1 
HETATM 7877 O  O   . HOH F 3 .   ? -23.594 18.656  36.916  1.00 34.94  ? 835 HOH B O   1 
HETATM 7878 O  O   . HOH F 3 .   ? -29.188 28.260  35.576  1.00 33.17  ? 836 HOH B O   1 
HETATM 7879 O  O   . HOH F 3 .   ? 12.788  23.296  29.161  1.00 35.23  ? 837 HOH B O   1 
HETATM 7880 O  O   . HOH F 3 .   ? -4.913  10.527  22.556  1.00 39.87  ? 838 HOH B O   1 
HETATM 7881 O  O   . HOH F 3 .   ? -31.822 21.711  12.336  1.00 37.16  ? 839 HOH B O   1 
HETATM 7882 O  O   . HOH F 3 .   ? -21.689 1.522   24.270  1.00 38.23  ? 840 HOH B O   1 
HETATM 7883 O  O   . HOH F 3 .   ? -21.524 43.520  34.297  1.00 40.52  ? 841 HOH B O   1 
HETATM 7884 O  O   . HOH F 3 .   ? 23.414  15.518  23.653  1.00 35.02  ? 842 HOH B O   1 
HETATM 7885 O  O   . HOH F 3 .   ? -17.964 4.587   -2.442  1.00 29.59  ? 843 HOH B O   1 
HETATM 7886 O  O   . HOH F 3 .   ? -4.837  12.840  23.447  1.00 38.69  ? 844 HOH B O   1 
HETATM 7887 O  O   . HOH F 3 .   ? -7.291  8.909   24.052  1.00 45.43  ? 845 HOH B O   1 
HETATM 7888 O  O   . HOH F 3 .   ? -21.979 22.096  44.108  1.00 31.47  ? 846 HOH B O   1 
HETATM 7889 O  O   . HOH F 3 .   ? -12.357 12.506  27.697  1.00 31.30  ? 847 HOH B O   1 
HETATM 7890 O  O   . HOH F 3 .   ? -9.248  3.769   -14.874 1.00 28.58  ? 848 HOH B O   1 
HETATM 7891 O  O   . HOH F 3 .   ? -9.325  13.219  24.883  1.00 25.69  ? 849 HOH B O   1 
HETATM 7892 O  O   . HOH F 3 .   ? -16.065 1.938   9.959   1.00 29.82  ? 850 HOH B O   1 
HETATM 7893 O  O   . HOH F 3 .   ? -15.771 32.839  11.519  1.00 32.29  ? 851 HOH B O   1 
HETATM 7894 O  O   . HOH F 3 .   ? 0.209   10.849  14.988  1.00 17.44  ? 852 HOH B O   1 
HETATM 7895 O  O   . HOH F 3 .   ? -7.460  48.317  19.091  1.00 35.66  ? 853 HOH B O   1 
HETATM 7896 O  O   . HOH F 3 .   ? -21.555 -0.619  22.914  1.00 34.84  ? 854 HOH B O   1 
HETATM 7897 O  O   . HOH F 3 .   ? -5.464  33.886  38.002  1.00 35.74  ? 855 HOH B O   1 
HETATM 7898 O  O   . HOH F 3 .   ? -32.011 26.492  30.198  1.00 27.68  ? 856 HOH B O   1 
HETATM 7899 O  O   . HOH F 3 .   ? 0.176   18.166  31.112  1.00 45.47  ? 857 HOH B O   1 
HETATM 7900 O  O   . HOH F 3 .   ? 11.882  9.537   15.241  1.00 29.66  ? 858 HOH B O   1 
HETATM 7901 O  O   . HOH F 3 .   ? -6.047  46.312  29.943  1.00 45.47  ? 859 HOH B O   1 
HETATM 7902 O  O   . HOH F 3 .   ? -23.480 34.956  9.696   1.00 36.35  ? 860 HOH B O   1 
HETATM 7903 O  O   . HOH F 3 .   ? -18.955 15.208  -2.349  1.00 35.77  ? 861 HOH B O   1 
HETATM 7904 O  O   . HOH F 3 .   ? -12.886 18.130  30.082  1.00 34.80  ? 862 HOH B O   1 
HETATM 7905 O  O   . HOH F 3 .   ? -0.640  32.005  38.994  1.00 38.18  ? 863 HOH B O   1 
HETATM 7906 O  O   . HOH F 3 .   ? -15.198 -3.002  13.825  1.00 29.21  ? 864 HOH B O   1 
HETATM 7907 O  O   . HOH F 3 .   ? 18.040  20.552  12.845  1.00 37.55  ? 865 HOH B O   1 
HETATM 7908 O  O   . HOH F 3 .   ? -18.476 8.386   -4.120  1.00 30.59  ? 866 HOH B O   1 
HETATM 7909 O  O   . HOH F 3 .   ? -8.980  37.586  36.562  1.00 42.93  ? 867 HOH B O   1 
HETATM 7910 O  O   . HOH F 3 .   ? -25.847 32.520  38.594  1.00 26.86  ? 868 HOH B O   1 
HETATM 7911 O  O   . HOH F 3 .   ? -7.324  5.933   26.399  1.00 29.26  ? 869 HOH B O   1 
HETATM 7912 O  O   . HOH F 3 .   ? 7.418   22.061  34.003  1.00 27.38  ? 870 HOH B O   1 
HETATM 7913 O  O   . HOH F 3 .   ? 15.407  14.232  17.786  1.00 31.92  ? 871 HOH B O   1 
HETATM 7914 O  O   . HOH F 3 .   ? -10.576 8.869   25.777  1.00 30.00  ? 872 HOH B O   1 
HETATM 7915 O  O   . HOH F 3 .   ? -29.205 32.400  37.273  1.00 34.09  ? 873 HOH B O   1 
HETATM 7916 O  O   . HOH F 3 .   ? -35.635 25.730  21.383  1.00 35.42  ? 874 HOH B O   1 
HETATM 7917 O  O   . HOH F 3 .   ? -16.376 24.776  42.649  1.00 29.49  ? 875 HOH B O   1 
HETATM 7918 O  O   . HOH F 3 .   ? -22.745 42.937  17.145  1.00 19.19  ? 876 HOH B O   1 
HETATM 7919 O  O   . HOH F 3 .   ? -14.604 28.111  9.033   1.00 53.02  ? 877 HOH B O   1 
HETATM 7920 O  O   . HOH F 3 .   ? -12.310 -2.552  23.135  1.00 31.61  ? 878 HOH B O   1 
HETATM 7921 O  O   . HOH F 3 .   ? -14.020 34.947  11.432  1.00 28.60  ? 879 HOH B O   1 
HETATM 7922 O  O   . HOH F 3 .   ? -29.800 27.674  37.920  1.00 32.35  ? 880 HOH B O   1 
HETATM 7923 O  O   . HOH F 3 .   ? -5.896  27.153  42.043  1.00 23.41  ? 881 HOH B O   1 
HETATM 7924 O  O   . HOH F 3 .   ? -18.068 11.116  -3.322  1.00 32.41  ? 882 HOH B O   1 
HETATM 7925 O  O   . HOH F 3 .   ? -24.630 17.561  9.564   1.00 40.54  ? 883 HOH B O   1 
HETATM 7926 O  O   . HOH F 3 .   ? -20.540 13.693  -1.128  1.00 29.67  ? 884 HOH B O   1 
HETATM 7927 O  O   . HOH F 3 .   ? -18.389 50.119  33.196  1.00 36.11  ? 885 HOH B O   1 
HETATM 7928 O  O   . HOH F 3 .   ? -15.989 -4.809  1.020   1.00 37.51  ? 886 HOH B O   1 
# 
