data_9ISS
# 
_entry.id   9ISS 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9ISS         pdb_00009iss 10.2210/pdb9iss/pdb 
WWPDB D_1300048713 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-12-04 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9ISS 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
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 shoji.osami.w3@f.mail.nagoya-u.ac.jp Osami   Shoji    ? 'principal investigator/group leader' 0000-0003-3522-0065 
3 sugimoto@spring8.or.jp               Hiroshi Sugimoto ? 'principal investigator/group leader' 0000-0002-3140-8362 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yokoyama, Y.' 1 0000-0002-2145-0030 
'Shoji, O.'    2 0000-0003-3522-0065 
'Sugimoto, H.' 3 0000-0002-3140-8362 
# 
_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                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemcatchem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1867-3899 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Bacterial Acyl Homoserine Lactones Triggered Non-Native Substrate Hydroxylation Catalyzed by Directed-Evolution-Derived Cytochrome P450BM3 Mutants
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/cctc.202401641 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yokoyama, Y.' 1 ? 
primary 'Ariyasu, S.'  2 ? 
primary 'Karasawa, M.' 3 ? 
primary 'Kasai, C.'    4 ? 
primary 'Aiba, Y.'     5 ? 
primary 'Sugimoto, H.' 6 ? 
primary 'Shoji, O.'    7 ? 
# 
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' 52222.539 2   1.14.14.1,1.6.2.4 'R47W, T49L, A74V, L188P' ? 
? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                    616.487   2   ?                 ?                         ? 
? 
3 non-polymer syn 'N-[(3S)-2-oxotetrahydrofuran-3-yl]decanamide'       255.353   2   ?                 ?                         ? 
? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                 78.133    2   ?                 ?                         ? 
? 
5 non-polymer syn GLYCEROL                                             92.094    4   ?                 ?                         ? 
? 
6 water       nat water                                                18.015    611 ?                 ?                         ? 
? 
# 
_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       
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGWVLRYLSSQRLIKEACDESRFDKNLSQVLKFVRD
FAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKPQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGWVLRYLSSQRLIKEACDESRFDKNLSQVLKFVRD
FAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKPQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_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 'N-[(3S)-2-oxotetrahydrofuran-3-yl]decanamide' HL0 
4 'DIMETHYL SULFOXIDE'                           DMS 
5 GLYCEROL                                       GOL 
6 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  TRP n 
1 48  VAL n 
1 49  LEU 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  VAL 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  PHE 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 VAL 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 ALA n 
1 185 MET n 
1 186 ASN n 
1 187 LYS n 
1 188 PRO 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 GLU 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 ILE n 
1 264 ALA 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 VAL 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 ALA 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 LYS 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               ? 
_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                    ? 
_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' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1404 
_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          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET28a(+)' 
_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 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                           ?                                 'C2 H6 O S'        
78.133  
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  
GOL non-polymer         . GLYCEROL                                       'GLYCERIN; PROPANE-1,2,3-TRIOL'   'C3 H8 O3'         
92.094  
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 
HL0 non-polymer         . 'N-[(3S)-2-oxotetrahydrofuran-3-yl]decanamide' 'N-decanoyl-L-homoserine lactone' 'C14 H25 N O3'     
255.353 
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   2   ILE ILE 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  TRP 47  47  47  TRP TRP A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  LEU 49  49  49  LEU LEU 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  VAL 74  74  74  VAL VAL 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  PHE 87  87  87  PHE PHE 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 VAL 127 127 127 VAL VAL 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 ALA 184 184 184 ALA ALA 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 PRO 188 188 188 PRO PRO 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 GLU 207 207 207 GLU GLU 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 ILE 263 263 263 ILE ILE A . n 
A 1 264 ALA 264 264 264 ALA ALA 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 VAL 297 297 297 VAL VAL 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 ALA 328 328 328 ALA ALA 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 LYS 452 452 452 LYS LYS 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   2   ILE ILE 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  TRP 47  47  47  TRP TRP B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  LEU 49  49  49  LEU LEU 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  VAL 74  74  74  VAL VAL 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  PHE 87  87  87  PHE PHE 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 VAL 127 127 127 VAL VAL 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 ALA 184 184 184 ALA ALA 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 PRO 188 188 188 PRO PRO 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 GLU 207 207 207 GLU GLU 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 ILE 263 263 263 ILE ILE B . n 
B 1 264 ALA 264 264 264 ALA ALA 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 VAL 297 297 297 VAL VAL 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 ALA 328 328 328 ALA ALA 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 LYS 452 452 452 LYS LYS 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 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 HEM ? ? HEM ? ? 'SUBJECT OF INVESTIGATION' ? 
2 HL0 ? ? HL0 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 3 HL0 1   502 601 HL0 HL0 A . 
E 4 DMS 1   503 602 DMS DMS A . 
F 5 GOL 1   504 603 GOL GOL A . 
G 5 GOL 1   505 604 GOL GOL A . 
H 2 HEM 1   501 501 HEM HEM B . 
I 3 HL0 1   502 601 HL0 HL0 B . 
J 4 DMS 1   503 602 DMS DMS B . 
K 5 GOL 1   504 603 GOL GOL B . 
L 5 GOL 1   505 604 GOL GOL B . 
M 6 HOH 1   601 292 HOH HOH A . 
M 6 HOH 2   602 570 HOH HOH A . 
M 6 HOH 3   603 589 HOH HOH A . 
M 6 HOH 4   604 529 HOH HOH A . 
M 6 HOH 5   605 519 HOH HOH A . 
M 6 HOH 6   606 418 HOH HOH A . 
M 6 HOH 7   607 565 HOH HOH A . 
M 6 HOH 8   608 481 HOH HOH A . 
M 6 HOH 9   609 207 HOH HOH A . 
M 6 HOH 10  610 364 HOH HOH A . 
M 6 HOH 11  611 509 HOH HOH A . 
M 6 HOH 12  612 351 HOH HOH A . 
M 6 HOH 13  613 105 HOH HOH A . 
M 6 HOH 14  614 304 HOH HOH A . 
M 6 HOH 15  615 264 HOH HOH A . 
M 6 HOH 16  616 327 HOH HOH A . 
M 6 HOH 17  617 361 HOH HOH A . 
M 6 HOH 18  618 611 HOH HOH A . 
M 6 HOH 19  619 500 HOH HOH A . 
M 6 HOH 20  620 357 HOH HOH A . 
M 6 HOH 21  621 352 HOH HOH A . 
M 6 HOH 22  622 204 HOH HOH A . 
M 6 HOH 23  623 527 HOH HOH A . 
M 6 HOH 24  624 246 HOH HOH A . 
M 6 HOH 25  625 474 HOH HOH A . 
M 6 HOH 26  626 199 HOH HOH A . 
M 6 HOH 27  627 11  HOH HOH A . 
M 6 HOH 28  628 218 HOH HOH A . 
M 6 HOH 29  629 44  HOH HOH A . 
M 6 HOH 30  630 169 HOH HOH A . 
M 6 HOH 31  631 137 HOH HOH A . 
M 6 HOH 32  632 294 HOH HOH A . 
M 6 HOH 33  633 97  HOH HOH A . 
M 6 HOH 34  634 77  HOH HOH A . 
M 6 HOH 35  635 377 HOH HOH A . 
M 6 HOH 36  636 117 HOH HOH A . 
M 6 HOH 37  637 428 HOH HOH A . 
M 6 HOH 38  638 343 HOH HOH A . 
M 6 HOH 39  639 33  HOH HOH A . 
M 6 HOH 40  640 253 HOH HOH A . 
M 6 HOH 41  641 41  HOH HOH A . 
M 6 HOH 42  642 98  HOH HOH A . 
M 6 HOH 43  643 49  HOH HOH A . 
M 6 HOH 44  644 162 HOH HOH A . 
M 6 HOH 45  645 289 HOH HOH A . 
M 6 HOH 46  646 537 HOH HOH A . 
M 6 HOH 47  647 306 HOH HOH A . 
M 6 HOH 48  648 591 HOH HOH A . 
M 6 HOH 49  649 58  HOH HOH A . 
M 6 HOH 50  650 112 HOH HOH A . 
M 6 HOH 51  651 477 HOH HOH A . 
M 6 HOH 52  652 425 HOH HOH A . 
M 6 HOH 53  653 57  HOH HOH A . 
M 6 HOH 54  654 73  HOH HOH A . 
M 6 HOH 55  655 7   HOH HOH A . 
M 6 HOH 56  656 109 HOH HOH A . 
M 6 HOH 57  657 346 HOH HOH A . 
M 6 HOH 58  658 186 HOH HOH A . 
M 6 HOH 59  659 172 HOH HOH A . 
M 6 HOH 60  660 168 HOH HOH A . 
M 6 HOH 61  661 299 HOH HOH A . 
M 6 HOH 62  662 35  HOH HOH A . 
M 6 HOH 63  663 459 HOH HOH A . 
M 6 HOH 64  664 19  HOH HOH A . 
M 6 HOH 65  665 347 HOH HOH A . 
M 6 HOH 66  666 373 HOH HOH A . 
M 6 HOH 67  667 309 HOH HOH A . 
M 6 HOH 68  668 70  HOH HOH A . 
M 6 HOH 69  669 242 HOH HOH A . 
M 6 HOH 70  670 32  HOH HOH A . 
M 6 HOH 71  671 27  HOH HOH A . 
M 6 HOH 72  672 31  HOH HOH A . 
M 6 HOH 73  673 338 HOH HOH A . 
M 6 HOH 74  674 378 HOH HOH A . 
M 6 HOH 75  675 302 HOH HOH A . 
M 6 HOH 76  676 335 HOH HOH A . 
M 6 HOH 77  677 330 HOH HOH A . 
M 6 HOH 78  678 75  HOH HOH A . 
M 6 HOH 79  679 265 HOH HOH A . 
M 6 HOH 80  680 211 HOH HOH A . 
M 6 HOH 81  681 303 HOH HOH A . 
M 6 HOH 82  682 227 HOH HOH A . 
M 6 HOH 83  683 140 HOH HOH A . 
M 6 HOH 84  684 438 HOH HOH A . 
M 6 HOH 85  685 30  HOH HOH A . 
M 6 HOH 86  686 43  HOH HOH A . 
M 6 HOH 87  687 25  HOH HOH A . 
M 6 HOH 88  688 55  HOH HOH A . 
M 6 HOH 89  689 239 HOH HOH A . 
M 6 HOH 90  690 420 HOH HOH A . 
M 6 HOH 91  691 369 HOH HOH A . 
M 6 HOH 92  692 91  HOH HOH A . 
M 6 HOH 93  693 443 HOH HOH A . 
M 6 HOH 94  694 196 HOH HOH A . 
M 6 HOH 95  695 129 HOH HOH A . 
M 6 HOH 96  696 64  HOH HOH A . 
M 6 HOH 97  697 131 HOH HOH A . 
M 6 HOH 98  698 200 HOH HOH A . 
M 6 HOH 99  699 542 HOH HOH A . 
M 6 HOH 100 700 63  HOH HOH A . 
M 6 HOH 101 701 489 HOH HOH A . 
M 6 HOH 102 702 365 HOH HOH A . 
M 6 HOH 103 703 276 HOH HOH A . 
M 6 HOH 104 704 54  HOH HOH A . 
M 6 HOH 105 705 100 HOH HOH A . 
M 6 HOH 106 706 10  HOH HOH A . 
M 6 HOH 107 707 556 HOH HOH A . 
M 6 HOH 108 708 26  HOH HOH A . 
M 6 HOH 109 709 255 HOH HOH A . 
M 6 HOH 110 710 266 HOH HOH A . 
M 6 HOH 111 711 108 HOH HOH A . 
M 6 HOH 112 712 326 HOH HOH A . 
M 6 HOH 113 713 331 HOH HOH A . 
M 6 HOH 114 714 171 HOH HOH A . 
M 6 HOH 115 715 530 HOH HOH A . 
M 6 HOH 116 716 421 HOH HOH A . 
M 6 HOH 117 717 329 HOH HOH A . 
M 6 HOH 118 718 197 HOH HOH A . 
M 6 HOH 119 719 571 HOH HOH A . 
M 6 HOH 120 720 187 HOH HOH A . 
M 6 HOH 121 721 600 HOH HOH A . 
M 6 HOH 122 722 156 HOH HOH A . 
M 6 HOH 123 723 176 HOH HOH A . 
M 6 HOH 124 724 66  HOH HOH A . 
M 6 HOH 125 725 295 HOH HOH A . 
M 6 HOH 126 726 116 HOH HOH A . 
M 6 HOH 127 727 1   HOH HOH A . 
M 6 HOH 128 728 89  HOH HOH A . 
M 6 HOH 129 729 111 HOH HOH A . 
M 6 HOH 130 730 290 HOH HOH A . 
M 6 HOH 131 731 273 HOH HOH A . 
M 6 HOH 132 732 271 HOH HOH A . 
M 6 HOH 133 733 604 HOH HOH A . 
M 6 HOH 134 734 17  HOH HOH A . 
M 6 HOH 135 735 336 HOH HOH A . 
M 6 HOH 136 736 392 HOH HOH A . 
M 6 HOH 137 737 126 HOH HOH A . 
M 6 HOH 138 738 248 HOH HOH A . 
M 6 HOH 139 739 180 HOH HOH A . 
M 6 HOH 140 740 521 HOH HOH A . 
M 6 HOH 141 741 340 HOH HOH A . 
M 6 HOH 142 742 413 HOH HOH A . 
M 6 HOH 143 743 376 HOH HOH A . 
M 6 HOH 144 744 138 HOH HOH A . 
M 6 HOH 145 745 531 HOH HOH A . 
M 6 HOH 146 746 269 HOH HOH A . 
M 6 HOH 147 747 435 HOH HOH A . 
M 6 HOH 148 748 229 HOH HOH A . 
M 6 HOH 149 749 536 HOH HOH A . 
M 6 HOH 150 750 467 HOH HOH A . 
M 6 HOH 151 751 107 HOH HOH A . 
M 6 HOH 152 752 482 HOH HOH A . 
M 6 HOH 153 753 223 HOH HOH A . 
M 6 HOH 154 754 389 HOH HOH A . 
M 6 HOH 155 755 484 HOH HOH A . 
M 6 HOH 156 756 160 HOH HOH A . 
M 6 HOH 157 757 333 HOH HOH A . 
M 6 HOH 158 758 268 HOH HOH A . 
M 6 HOH 159 759 51  HOH HOH A . 
M 6 HOH 160 760 69  HOH HOH A . 
M 6 HOH 161 761 29  HOH HOH A . 
M 6 HOH 162 762 451 HOH HOH A . 
M 6 HOH 163 763 191 HOH HOH A . 
M 6 HOH 164 764 387 HOH HOH A . 
M 6 HOH 165 765 78  HOH HOH A . 
M 6 HOH 166 766 151 HOH HOH A . 
M 6 HOH 167 767 260 HOH HOH A . 
M 6 HOH 168 768 42  HOH HOH A . 
M 6 HOH 169 769 450 HOH HOH A . 
M 6 HOH 170 770 194 HOH HOH A . 
M 6 HOH 171 771 439 HOH HOH A . 
M 6 HOH 172 772 215 HOH HOH A . 
M 6 HOH 173 773 155 HOH HOH A . 
M 6 HOH 174 774 243 HOH HOH A . 
M 6 HOH 175 775 236 HOH HOH A . 
M 6 HOH 176 776 102 HOH HOH A . 
M 6 HOH 177 777 272 HOH HOH A . 
M 6 HOH 178 778 545 HOH HOH A . 
M 6 HOH 179 779 4   HOH HOH A . 
M 6 HOH 180 780 245 HOH HOH A . 
M 6 HOH 181 781 316 HOH HOH A . 
M 6 HOH 182 782 263 HOH HOH A . 
M 6 HOH 183 783 164 HOH HOH A . 
M 6 HOH 184 784 127 HOH HOH A . 
M 6 HOH 185 785 12  HOH HOH A . 
M 6 HOH 186 786 307 HOH HOH A . 
M 6 HOH 187 787 449 HOH HOH A . 
M 6 HOH 188 788 226 HOH HOH A . 
M 6 HOH 189 789 470 HOH HOH A . 
M 6 HOH 190 790 462 HOH HOH A . 
M 6 HOH 191 791 308 HOH HOH A . 
M 6 HOH 192 792 344 HOH HOH A . 
M 6 HOH 193 793 371 HOH HOH A . 
M 6 HOH 194 794 337 HOH HOH A . 
M 6 HOH 195 795 106 HOH HOH A . 
M 6 HOH 196 796 495 HOH HOH A . 
M 6 HOH 197 797 92  HOH HOH A . 
M 6 HOH 198 798 81  HOH HOH A . 
M 6 HOH 199 799 401 HOH HOH A . 
M 6 HOH 200 800 523 HOH HOH A . 
M 6 HOH 201 801 59  HOH HOH A . 
M 6 HOH 202 802 561 HOH HOH A . 
M 6 HOH 203 803 458 HOH HOH A . 
M 6 HOH 204 804 202 HOH HOH A . 
M 6 HOH 205 805 491 HOH HOH A . 
M 6 HOH 206 806 388 HOH HOH A . 
M 6 HOH 207 807 113 HOH HOH A . 
M 6 HOH 208 808 147 HOH HOH A . 
M 6 HOH 209 809 534 HOH HOH A . 
M 6 HOH 210 810 71  HOH HOH A . 
M 6 HOH 211 811 559 HOH HOH A . 
M 6 HOH 212 812 312 HOH HOH A . 
M 6 HOH 213 813 593 HOH HOH A . 
M 6 HOH 214 814 383 HOH HOH A . 
M 6 HOH 215 815 283 HOH HOH A . 
M 6 HOH 216 816 142 HOH HOH A . 
M 6 HOH 217 817 36  HOH HOH A . 
M 6 HOH 218 818 87  HOH HOH A . 
M 6 HOH 219 819 367 HOH HOH A . 
M 6 HOH 220 820 348 HOH HOH A . 
M 6 HOH 221 821 300 HOH HOH A . 
M 6 HOH 222 822 95  HOH HOH A . 
M 6 HOH 223 823 225 HOH HOH A . 
M 6 HOH 224 824 224 HOH HOH A . 
M 6 HOH 225 825 258 HOH HOH A . 
M 6 HOH 226 826 469 HOH HOH A . 
M 6 HOH 227 827 233 HOH HOH A . 
M 6 HOH 228 828 460 HOH HOH A . 
M 6 HOH 229 829 34  HOH HOH A . 
M 6 HOH 230 830 279 HOH HOH A . 
M 6 HOH 231 831 432 HOH HOH A . 
M 6 HOH 232 832 422 HOH HOH A . 
M 6 HOH 233 833 181 HOH HOH A . 
M 6 HOH 234 834 53  HOH HOH A . 
M 6 HOH 235 835 554 HOH HOH A . 
M 6 HOH 236 836 596 HOH HOH A . 
M 6 HOH 237 837 547 HOH HOH A . 
M 6 HOH 238 838 21  HOH HOH A . 
M 6 HOH 239 839 605 HOH HOH A . 
M 6 HOH 240 840 592 HOH HOH A . 
M 6 HOH 241 841 252 HOH HOH A . 
M 6 HOH 242 842 259 HOH HOH A . 
M 6 HOH 243 843 502 HOH HOH A . 
M 6 HOH 244 844 416 HOH HOH A . 
M 6 HOH 245 845 339 HOH HOH A . 
M 6 HOH 246 846 368 HOH HOH A . 
M 6 HOH 247 847 257 HOH HOH A . 
M 6 HOH 248 848 293 HOH HOH A . 
M 6 HOH 249 849 15  HOH HOH A . 
M 6 HOH 250 850 603 HOH HOH A . 
M 6 HOH 251 851 468 HOH HOH A . 
M 6 HOH 252 852 394 HOH HOH A . 
M 6 HOH 253 853 274 HOH HOH A . 
M 6 HOH 254 854 237 HOH HOH A . 
M 6 HOH 255 855 577 HOH HOH A . 
M 6 HOH 256 856 579 HOH HOH A . 
M 6 HOH 257 857 132 HOH HOH A . 
M 6 HOH 258 858 311 HOH HOH A . 
M 6 HOH 259 859 506 HOH HOH A . 
M 6 HOH 260 860 493 HOH HOH A . 
M 6 HOH 261 861 522 HOH HOH A . 
M 6 HOH 262 862 249 HOH HOH A . 
M 6 HOH 263 863 410 HOH HOH A . 
M 6 HOH 264 864 563 HOH HOH A . 
M 6 HOH 265 865 405 HOH HOH A . 
M 6 HOH 266 866 557 HOH HOH A . 
M 6 HOH 267 867 585 HOH HOH A . 
M 6 HOH 268 868 65  HOH HOH A . 
M 6 HOH 269 869 586 HOH HOH A . 
M 6 HOH 270 870 480 HOH HOH A . 
M 6 HOH 271 871 381 HOH HOH A . 
M 6 HOH 272 872 409 HOH HOH A . 
M 6 HOH 273 873 598 HOH HOH A . 
M 6 HOH 274 874 590 HOH HOH A . 
M 6 HOH 275 875 182 HOH HOH A . 
M 6 HOH 276 876 328 HOH HOH A . 
M 6 HOH 277 877 103 HOH HOH A . 
M 6 HOH 278 878 475 HOH HOH A . 
M 6 HOH 279 879 501 HOH HOH A . 
M 6 HOH 280 880 133 HOH HOH A . 
M 6 HOH 281 881 175 HOH HOH A . 
M 6 HOH 282 882 407 HOH HOH A . 
M 6 HOH 283 883 419 HOH HOH A . 
M 6 HOH 284 884 231 HOH HOH A . 
M 6 HOH 285 885 599 HOH HOH A . 
M 6 HOH 286 886 508 HOH HOH A . 
M 6 HOH 287 887 350 HOH HOH A . 
M 6 HOH 288 888 235 HOH HOH A . 
M 6 HOH 289 889 490 HOH HOH A . 
M 6 HOH 290 890 363 HOH HOH A . 
M 6 HOH 291 891 427 HOH HOH A . 
M 6 HOH 292 892 584 HOH HOH A . 
M 6 HOH 293 893 205 HOH HOH A . 
M 6 HOH 294 894 472 HOH HOH A . 
M 6 HOH 295 895 511 HOH HOH A . 
M 6 HOH 296 896 396 HOH HOH A . 
M 6 HOH 297 897 341 HOH HOH A . 
M 6 HOH 298 898 360 HOH HOH A . 
M 6 HOH 299 899 442 HOH HOH A . 
M 6 HOH 300 900 370 HOH HOH A . 
M 6 HOH 301 901 587 HOH HOH A . 
N 6 HOH 1   601 580 HOH HOH B . 
N 6 HOH 2   602 574 HOH HOH B . 
N 6 HOH 3   603 576 HOH HOH B . 
N 6 HOH 4   604 573 HOH HOH B . 
N 6 HOH 5   605 568 HOH HOH B . 
N 6 HOH 6   606 569 HOH HOH B . 
N 6 HOH 7   607 597 HOH HOH B . 
N 6 HOH 8   608 437 HOH HOH B . 
N 6 HOH 9   609 208 HOH HOH B . 
N 6 HOH 10  610 157 HOH HOH B . 
N 6 HOH 11  611 228 HOH HOH B . 
N 6 HOH 12  612 146 HOH HOH B . 
N 6 HOH 13  613 250 HOH HOH B . 
N 6 HOH 14  614 393 HOH HOH B . 
N 6 HOH 15  615 185 HOH HOH B . 
N 6 HOH 16  616 471 HOH HOH B . 
N 6 HOH 17  617 342 HOH HOH B . 
N 6 HOH 18  618 520 HOH HOH B . 
N 6 HOH 19  619 497 HOH HOH B . 
N 6 HOH 20  620 391 HOH HOH B . 
N 6 HOH 21  621 454 HOH HOH B . 
N 6 HOH 22  622 403 HOH HOH B . 
N 6 HOH 23  623 310 HOH HOH B . 
N 6 HOH 24  624 193 HOH HOH B . 
N 6 HOH 25  625 499 HOH HOH B . 
N 6 HOH 26  626 287 HOH HOH B . 
N 6 HOH 27  627 152 HOH HOH B . 
N 6 HOH 28  628 48  HOH HOH B . 
N 6 HOH 29  629 270 HOH HOH B . 
N 6 HOH 30  630 457 HOH HOH B . 
N 6 HOH 31  631 221 HOH HOH B . 
N 6 HOH 32  632 487 HOH HOH B . 
N 6 HOH 33  633 86  HOH HOH B . 
N 6 HOH 34  634 319 HOH HOH B . 
N 6 HOH 35  635 159 HOH HOH B . 
N 6 HOH 36  636 80  HOH HOH B . 
N 6 HOH 37  637 28  HOH HOH B . 
N 6 HOH 38  638 206 HOH HOH B . 
N 6 HOH 39  639 431 HOH HOH B . 
N 6 HOH 40  640 473 HOH HOH B . 
N 6 HOH 41  641 135 HOH HOH B . 
N 6 HOH 42  642 301 HOH HOH B . 
N 6 HOH 43  643 583 HOH HOH B . 
N 6 HOH 44  644 476 HOH HOH B . 
N 6 HOH 45  645 84  HOH HOH B . 
N 6 HOH 46  646 375 HOH HOH B . 
N 6 HOH 47  647 395 HOH HOH B . 
N 6 HOH 48  648 297 HOH HOH B . 
N 6 HOH 49  649 386 HOH HOH B . 
N 6 HOH 50  650 46  HOH HOH B . 
N 6 HOH 51  651 88  HOH HOH B . 
N 6 HOH 52  652 94  HOH HOH B . 
N 6 HOH 53  653 40  HOH HOH B . 
N 6 HOH 54  654 8   HOH HOH B . 
N 6 HOH 55  655 125 HOH HOH B . 
N 6 HOH 56  656 76  HOH HOH B . 
N 6 HOH 57  657 141 HOH HOH B . 
N 6 HOH 58  658 433 HOH HOH B . 
N 6 HOH 59  659 275 HOH HOH B . 
N 6 HOH 60  660 134 HOH HOH B . 
N 6 HOH 61  661 220 HOH HOH B . 
N 6 HOH 62  662 16  HOH HOH B . 
N 6 HOH 63  663 83  HOH HOH B . 
N 6 HOH 64  664 230 HOH HOH B . 
N 6 HOH 65  665 154 HOH HOH B . 
N 6 HOH 66  666 544 HOH HOH B . 
N 6 HOH 67  667 251 HOH HOH B . 
N 6 HOH 68  668 288 HOH HOH B . 
N 6 HOH 69  669 183 HOH HOH B . 
N 6 HOH 70  670 74  HOH HOH B . 
N 6 HOH 71  671 14  HOH HOH B . 
N 6 HOH 72  672 256 HOH HOH B . 
N 6 HOH 73  673 3   HOH HOH B . 
N 6 HOH 74  674 122 HOH HOH B . 
N 6 HOH 75  675 85  HOH HOH B . 
N 6 HOH 76  676 609 HOH HOH B . 
N 6 HOH 77  677 298 HOH HOH B . 
N 6 HOH 78  678 82  HOH HOH B . 
N 6 HOH 79  679 158 HOH HOH B . 
N 6 HOH 80  680 13  HOH HOH B . 
N 6 HOH 81  681 355 HOH HOH B . 
N 6 HOH 82  682 79  HOH HOH B . 
N 6 HOH 83  683 415 HOH HOH B . 
N 6 HOH 84  684 192 HOH HOH B . 
N 6 HOH 85  685 121 HOH HOH B . 
N 6 HOH 86  686 305 HOH HOH B . 
N 6 HOH 87  687 282 HOH HOH B . 
N 6 HOH 88  688 278 HOH HOH B . 
N 6 HOH 89  689 325 HOH HOH B . 
N 6 HOH 90  690 448 HOH HOH B . 
N 6 HOH 91  691 436 HOH HOH B . 
N 6 HOH 92  692 110 HOH HOH B . 
N 6 HOH 93  693 222 HOH HOH B . 
N 6 HOH 94  694 553 HOH HOH B . 
N 6 HOH 95  695 479 HOH HOH B . 
N 6 HOH 96  696 402 HOH HOH B . 
N 6 HOH 97  697 62  HOH HOH B . 
N 6 HOH 98  698 161 HOH HOH B . 
N 6 HOH 99  699 362 HOH HOH B . 
N 6 HOH 100 700 38  HOH HOH B . 
N 6 HOH 101 701 334 HOH HOH B . 
N 6 HOH 102 702 546 HOH HOH B . 
N 6 HOH 103 703 384 HOH HOH B . 
N 6 HOH 104 704 539 HOH HOH B . 
N 6 HOH 105 705 261 HOH HOH B . 
N 6 HOH 106 706 163 HOH HOH B . 
N 6 HOH 107 707 67  HOH HOH B . 
N 6 HOH 108 708 277 HOH HOH B . 
N 6 HOH 109 709 119 HOH HOH B . 
N 6 HOH 110 710 244 HOH HOH B . 
N 6 HOH 111 711 123 HOH HOH B . 
N 6 HOH 112 712 2   HOH HOH B . 
N 6 HOH 113 713 148 HOH HOH B . 
N 6 HOH 114 714 190 HOH HOH B . 
N 6 HOH 115 715 595 HOH HOH B . 
N 6 HOH 116 716 52  HOH HOH B . 
N 6 HOH 117 717 441 HOH HOH B . 
N 6 HOH 118 718 203 HOH HOH B . 
N 6 HOH 119 719 414 HOH HOH B . 
N 6 HOH 120 720 60  HOH HOH B . 
N 6 HOH 121 721 551 HOH HOH B . 
N 6 HOH 122 722 456 HOH HOH B . 
N 6 HOH 123 723 528 HOH HOH B . 
N 6 HOH 124 724 165 HOH HOH B . 
N 6 HOH 125 725 23  HOH HOH B . 
N 6 HOH 126 726 558 HOH HOH B . 
N 6 HOH 127 727 104 HOH HOH B . 
N 6 HOH 128 728 68  HOH HOH B . 
N 6 HOH 129 729 345 HOH HOH B . 
N 6 HOH 130 730 90  HOH HOH B . 
N 6 HOH 131 731 189 HOH HOH B . 
N 6 HOH 132 732 167 HOH HOH B . 
N 6 HOH 133 733 548 HOH HOH B . 
N 6 HOH 134 734 56  HOH HOH B . 
N 6 HOH 135 735 313 HOH HOH B . 
N 6 HOH 136 736 532 HOH HOH B . 
N 6 HOH 137 737 24  HOH HOH B . 
N 6 HOH 138 738 323 HOH HOH B . 
N 6 HOH 139 739 18  HOH HOH B . 
N 6 HOH 140 740 179 HOH HOH B . 
N 6 HOH 141 741 254 HOH HOH B . 
N 6 HOH 142 742 247 HOH HOH B . 
N 6 HOH 143 743 188 HOH HOH B . 
N 6 HOH 144 744 93  HOH HOH B . 
N 6 HOH 145 745 505 HOH HOH B . 
N 6 HOH 146 746 39  HOH HOH B . 
N 6 HOH 147 747 461 HOH HOH B . 
N 6 HOH 148 748 281 HOH HOH B . 
N 6 HOH 149 749 444 HOH HOH B . 
N 6 HOH 150 750 398 HOH HOH B . 
N 6 HOH 151 751 22  HOH HOH B . 
N 6 HOH 152 752 149 HOH HOH B . 
N 6 HOH 153 753 213 HOH HOH B . 
N 6 HOH 154 754 72  HOH HOH B . 
N 6 HOH 155 755 496 HOH HOH B . 
N 6 HOH 156 756 139 HOH HOH B . 
N 6 HOH 157 757 241 HOH HOH B . 
N 6 HOH 158 758 423 HOH HOH B . 
N 6 HOH 159 759 262 HOH HOH B . 
N 6 HOH 160 760 9   HOH HOH B . 
N 6 HOH 161 761 406 HOH HOH B . 
N 6 HOH 162 762 201 HOH HOH B . 
N 6 HOH 163 763 61  HOH HOH B . 
N 6 HOH 164 764 5   HOH HOH B . 
N 6 HOH 165 765 517 HOH HOH B . 
N 6 HOH 166 766 20  HOH HOH B . 
N 6 HOH 167 767 37  HOH HOH B . 
N 6 HOH 168 768 562 HOH HOH B . 
N 6 HOH 169 769 120 HOH HOH B . 
N 6 HOH 170 770 445 HOH HOH B . 
N 6 HOH 171 771 510 HOH HOH B . 
N 6 HOH 172 772 607 HOH HOH B . 
N 6 HOH 173 773 178 HOH HOH B . 
N 6 HOH 174 774 400 HOH HOH B . 
N 6 HOH 175 775 525 HOH HOH B . 
N 6 HOH 176 776 358 HOH HOH B . 
N 6 HOH 177 777 434 HOH HOH B . 
N 6 HOH 178 778 322 HOH HOH B . 
N 6 HOH 179 779 296 HOH HOH B . 
N 6 HOH 180 780 198 HOH HOH B . 
N 6 HOH 181 781 397 HOH HOH B . 
N 6 HOH 182 782 115 HOH HOH B . 
N 6 HOH 183 783 354 HOH HOH B . 
N 6 HOH 184 784 210 HOH HOH B . 
N 6 HOH 185 785 124 HOH HOH B . 
N 6 HOH 186 786 317 HOH HOH B . 
N 6 HOH 187 787 411 HOH HOH B . 
N 6 HOH 188 788 177 HOH HOH B . 
N 6 HOH 189 789 455 HOH HOH B . 
N 6 HOH 190 790 440 HOH HOH B . 
N 6 HOH 191 791 549 HOH HOH B . 
N 6 HOH 192 792 145 HOH HOH B . 
N 6 HOH 193 793 114 HOH HOH B . 
N 6 HOH 194 794 280 HOH HOH B . 
N 6 HOH 195 795 478 HOH HOH B . 
N 6 HOH 196 796 550 HOH HOH B . 
N 6 HOH 197 797 216 HOH HOH B . 
N 6 HOH 198 798 267 HOH HOH B . 
N 6 HOH 199 799 566 HOH HOH B . 
N 6 HOH 200 800 494 HOH HOH B . 
N 6 HOH 201 801 238 HOH HOH B . 
N 6 HOH 202 802 170 HOH HOH B . 
N 6 HOH 203 803 214 HOH HOH B . 
N 6 HOH 204 804 380 HOH HOH B . 
N 6 HOH 205 805 382 HOH HOH B . 
N 6 HOH 206 806 219 HOH HOH B . 
N 6 HOH 207 807 488 HOH HOH B . 
N 6 HOH 208 808 453 HOH HOH B . 
N 6 HOH 209 809 524 HOH HOH B . 
N 6 HOH 210 810 6   HOH HOH B . 
N 6 HOH 211 811 538 HOH HOH B . 
N 6 HOH 212 812 564 HOH HOH B . 
N 6 HOH 213 813 424 HOH HOH B . 
N 6 HOH 214 814 174 HOH HOH B . 
N 6 HOH 215 815 533 HOH HOH B . 
N 6 HOH 216 816 96  HOH HOH B . 
N 6 HOH 217 817 166 HOH HOH B . 
N 6 HOH 218 818 321 HOH HOH B . 
N 6 HOH 219 819 498 HOH HOH B . 
N 6 HOH 220 820 535 HOH HOH B . 
N 6 HOH 221 821 128 HOH HOH B . 
N 6 HOH 222 822 464 HOH HOH B . 
N 6 HOH 223 823 240 HOH HOH B . 
N 6 HOH 224 824 567 HOH HOH B . 
N 6 HOH 225 825 552 HOH HOH B . 
N 6 HOH 226 826 232 HOH HOH B . 
N 6 HOH 227 827 50  HOH HOH B . 
N 6 HOH 228 828 318 HOH HOH B . 
N 6 HOH 229 829 136 HOH HOH B . 
N 6 HOH 230 830 463 HOH HOH B . 
N 6 HOH 231 831 286 HOH HOH B . 
N 6 HOH 232 832 99  HOH HOH B . 
N 6 HOH 233 833 173 HOH HOH B . 
N 6 HOH 234 834 153 HOH HOH B . 
N 6 HOH 235 835 101 HOH HOH B . 
N 6 HOH 236 836 560 HOH HOH B . 
N 6 HOH 237 837 284 HOH HOH B . 
N 6 HOH 238 838 217 HOH HOH B . 
N 6 HOH 239 839 150 HOH HOH B . 
N 6 HOH 240 840 452 HOH HOH B . 
N 6 HOH 241 841 447 HOH HOH B . 
N 6 HOH 242 842 541 HOH HOH B . 
N 6 HOH 243 843 540 HOH HOH B . 
N 6 HOH 244 844 144 HOH HOH B . 
N 6 HOH 245 845 446 HOH HOH B . 
N 6 HOH 246 846 356 HOH HOH B . 
N 6 HOH 247 847 130 HOH HOH B . 
N 6 HOH 248 848 426 HOH HOH B . 
N 6 HOH 249 849 366 HOH HOH B . 
N 6 HOH 250 850 485 HOH HOH B . 
N 6 HOH 251 851 594 HOH HOH B . 
N 6 HOH 252 852 606 HOH HOH B . 
N 6 HOH 253 853 324 HOH HOH B . 
N 6 HOH 254 854 507 HOH HOH B . 
N 6 HOH 255 855 572 HOH HOH B . 
N 6 HOH 256 856 385 HOH HOH B . 
N 6 HOH 257 857 601 HOH HOH B . 
N 6 HOH 258 858 483 HOH HOH B . 
N 6 HOH 259 859 45  HOH HOH B . 
N 6 HOH 260 860 195 HOH HOH B . 
N 6 HOH 261 861 417 HOH HOH B . 
N 6 HOH 262 862 408 HOH HOH B . 
N 6 HOH 263 863 543 HOH HOH B . 
N 6 HOH 264 864 353 HOH HOH B . 
N 6 HOH 265 865 118 HOH HOH B . 
N 6 HOH 266 866 526 HOH HOH B . 
N 6 HOH 267 867 374 HOH HOH B . 
N 6 HOH 268 868 555 HOH HOH B . 
N 6 HOH 269 869 412 HOH HOH B . 
N 6 HOH 270 870 503 HOH HOH B . 
N 6 HOH 271 871 285 HOH HOH B . 
N 6 HOH 272 872 513 HOH HOH B . 
N 6 HOH 273 873 486 HOH HOH B . 
N 6 HOH 274 874 602 HOH HOH B . 
N 6 HOH 275 875 332 HOH HOH B . 
N 6 HOH 276 876 372 HOH HOH B . 
N 6 HOH 277 877 47  HOH HOH B . 
N 6 HOH 278 878 404 HOH HOH B . 
N 6 HOH 279 879 359 HOH HOH B . 
N 6 HOH 280 880 516 HOH HOH B . 
N 6 HOH 281 881 212 HOH HOH B . 
N 6 HOH 282 882 608 HOH HOH B . 
N 6 HOH 283 883 209 HOH HOH B . 
N 6 HOH 284 884 610 HOH HOH B . 
N 6 HOH 285 885 581 HOH HOH B . 
N 6 HOH 286 886 399 HOH HOH B . 
N 6 HOH 287 887 184 HOH HOH B . 
N 6 HOH 288 888 466 HOH HOH B . 
N 6 HOH 289 889 514 HOH HOH B . 
N 6 HOH 290 890 575 HOH HOH B . 
N 6 HOH 291 891 143 HOH HOH B . 
N 6 HOH 292 892 429 HOH HOH B . 
N 6 HOH 293 893 349 HOH HOH B . 
N 6 HOH 294 894 234 HOH HOH B . 
N 6 HOH 295 895 291 HOH HOH B . 
N 6 HOH 296 896 314 HOH HOH B . 
N 6 HOH 297 897 518 HOH HOH B . 
N 6 HOH 298 898 320 HOH HOH B . 
N 6 HOH 299 899 588 HOH HOH B . 
N 6 HOH 300 900 512 HOH HOH B . 
N 6 HOH 301 901 504 HOH HOH B . 
N 6 HOH 302 902 430 HOH HOH B . 
N 6 HOH 303 903 465 HOH HOH B . 
N 6 HOH 304 904 582 HOH HOH B . 
N 6 HOH 305 905 578 HOH HOH B . 
N 6 HOH 306 906 379 HOH HOH B . 
N 6 HOH 307 907 390 HOH HOH B . 
N 6 HOH 308 908 492 HOH HOH B . 
N 6 HOH 309 909 315 HOH HOH B . 
N 6 HOH 310 910 515 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0267 1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .        3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .        5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.37 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9ISS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.575 
_cell.length_a_esd                 ? 
_cell.length_b                     145.442 
_cell.length_b_esd                 ? 
_cell.length_c                     63.106 
_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                         9ISS 
_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                   9ISS 
_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             2.56 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.90 
_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          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.4 
_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    'PEG 8000, Tris-HCl, magnesium chloride, N-decanoyl homoserine lactone' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 X 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         2021-11-29 
_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                    M 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_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                        'SPRING-8 BEAMLINE BL45XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL45XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9ISS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.46 
_reflns.d_resolution_low                               47.44 
_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                                     177212 
_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                           98.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.03 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.110 
_reflns.pdbx_Rpim_I_all                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1039925 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.993 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.101 
_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                                    1.46 
_reflns_shell.d_res_low                                     1.48 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8628 
_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                               4.7 
_reflns_shell.pdbx_chi_squared                              0.91 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.838 
_reflns_shell.pdbx_Rpim_I_all                               0.376 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.686 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.745 
_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]                            -0.56 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.11 
_refine.aniso_B[2][2]                            -0.17 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.74 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               18.880 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.968 
_refine.correlation_coeff_Fo_to_Fc_free          0.966 
_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                                 9ISS 
_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                            1.46 
_refine.ls_d_res_low                             47.44 
_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                     168167 
_refine.ls_number_reflns_R_free                  9001 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.00 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16661 
_refine.ls_R_factor_R_free                       0.18242 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16575 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.061 
_refine.pdbx_overall_ESU_R_Free                  0.060 
_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                             1.150 
_refine.overall_SU_ML                            0.044 
_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                       1.46 
_refine_hist.d_res_low                        47.44 
_refine_hist.number_atoms_solvent             611 
_refine_hist.number_atoms_total               8103 
_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        7338 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         154 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.013  0.013  7741  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.016  7356  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.825  1.667  10497 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.548  1.593  17008 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.554  5.000  920   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 33.619 23.511 413   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.204 15.000 1366  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.101 15.000 38    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.100  0.200  955   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  8726  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  1734  ? 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' ? 1.821  1.775  3665  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.817  1.774  3664  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.599  2.660  4590  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.599  2.660  4591  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.853  2.060  4076  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.852  2.060  4077  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.284  2.976  5908  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.214  21.505 8837  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.152  21.231 8718  ? 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                       1.460 
_refine_ls_shell.d_res_low                        1.498 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             650 
_refine_ls_shell.number_reflns_R_work             12248 
_refine_ls_shell.percent_reflns_obs               96.76 
_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                  0.248 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.277 
# 
_struct.entry_id                     9ISS 
_struct.title                        
'Crystal Structure of Cytochrome P450BM3 III-10C1 Mutant Heme Domain with N-Decanoyl-L-Homoserine Lactone' 
_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        9ISS 
_struct_keywords.text            'P450, Monooxygenase, Decoy molecules, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 5 ? 
M N N 6 ? 
N N N 6 ? 
# 
_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 9ISS A 1 ? 455 ? P14779 2 ? 456 ? 1 455 
2 1 9ISS 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 9ISS TRP A 47  ? UNP P14779 ARG 48  'engineered mutation' 47  1 
1 9ISS LEU A 49  ? UNP P14779 THR 50  'engineered mutation' 49  2 
1 9ISS VAL A 74  ? UNP P14779 ALA 75  'engineered mutation' 74  3 
1 9ISS PRO A 188 ? UNP P14779 LEU 189 'engineered mutation' 188 4 
2 9ISS TRP B 47  ? UNP P14779 ARG 48  'engineered mutation' 47  5 
2 9ISS LEU B 49  ? UNP P14779 THR 50  'engineered mutation' 49  6 
2 9ISS VAL B 74  ? UNP P14779 ALA 75  'engineered mutation' 74  7 
2 9ISS PRO B 188 ? UNP P14779 LEU 189 'engineered mutation' 188 8 
# 
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_and_software_defined_assembly PISA monomeric 1 
2 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 
1 'ABSA (A^2)' 1230  ? 
1 MORE         -21   ? 
1 'SSA (A^2)'  19070 ? 
2 'ABSA (A^2)' 1230  ? 
2 MORE         -21   ? 
2 'SSA (A^2)'  18910 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,M 
2 1 B,H,I,J,K,L,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 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 ? LYS A 187 ? HIS A 171 LYS A 187 1 ? 17 
HELX_P HELX_P12 AB3 PRO A 188 ? ARG A 190 ? PRO A 188 ARG A 190 5 ? 3  
HELX_P HELX_P13 AB4 ASP A 195 ? ALA A 197 ? ASP A 195 ALA A 197 5 ? 3  
HELX_P HELX_P14 AB5 TYR A 198 ? GLY A 227 ? TYR A 198 GLY A 227 1 ? 30 
HELX_P HELX_P15 AB6 ASP A 232 ? GLY A 240 ? ASP A 232 GLY A 240 1 ? 9  
HELX_P HELX_P16 AB7 ASP A 250 ? THR A 268 ? ASP A 250 THR A 268 1 ? 19 
HELX_P HELX_P17 AB8 THR A 268 ? ASN A 283 ? THR A 268 ASN A 283 1 ? 16 
HELX_P HELX_P18 AB9 ASN A 283 ? LEU A 298 ? ASN A 283 LEU A 298 1 ? 16 
HELX_P HELX_P19 AC1 SER A 304 ? GLN A 310 ? SER A 304 GLN A 310 1 ? 7  
HELX_P HELX_P20 AC2 LEU A 311 ? TRP A 325 ? LEU A 311 TRP A 325 1 ? 15 
HELX_P HELX_P21 AC3 ILE A 357 ? HIS A 361 ? ILE A 357 HIS A 361 1 ? 5  
HELX_P HELX_P22 AC4 ASP A 363 ? GLY A 368 ? ASP A 363 GLY A 368 1 ? 6  
HELX_P HELX_P23 AC5 ARG A 375 ? GLU A 380 ? ARG A 375 GLU A 380 5 ? 6  
HELX_P HELX_P24 AC6 ASN A 381 ? ILE A 385 ? ASN A 381 ILE A 385 5 ? 5  
HELX_P HELX_P25 AC7 ASN A 395 ? ALA A 399 ? ASN A 395 ALA A 399 5 ? 5  
HELX_P HELX_P26 AC8 GLY A 402 ? HIS A 420 ? GLY A 402 HIS A 420 1 ? 19 
HELX_P HELX_P27 AC9 PHE B 11  ? LYS B 15  ? PHE B 11  LYS B 15  5 ? 5  
HELX_P HELX_P28 AD1 ASN B 16  ? ASN B 21  ? ASN B 16  ASN B 21  5 ? 6  
HELX_P HELX_P29 AD2 LYS B 24  ? GLY B 37  ? LYS B 24  GLY B 37  1 ? 14 
HELX_P HELX_P30 AD3 SER B 54  ? CYS B 62  ? SER B 54  CYS B 62  1 ? 9  
HELX_P HELX_P31 AD4 SER B 72  ? GLY B 83  ? SER B 72  GLY B 83  1 ? 12 
HELX_P HELX_P32 AD5 GLU B 93  ? LEU B 104 ? GLU B 93  LEU B 104 1 ? 12 
HELX_P HELX_P33 AD6 PRO B 105 ? SER B 108 ? PRO B 105 SER B 108 5 ? 4  
HELX_P HELX_P34 AD7 GLN B 109 ? GLN B 110 ? GLN B 109 GLN B 110 5 ? 2  
HELX_P HELX_P35 AD8 ALA B 111 ? ARG B 132 ? ALA B 111 ARG B 132 1 ? 22 
HELX_P HELX_P36 AD9 VAL B 141 ? ASN B 159 ? VAL B 141 ASN B 159 1 ? 19 
HELX_P HELX_P37 AE1 ASN B 163 ? ARG B 167 ? ASN B 163 ARG B 167 5 ? 5  
HELX_P HELX_P38 AE2 HIS B 171 ? LYS B 187 ? HIS B 171 LYS B 187 1 ? 17 
HELX_P HELX_P39 AE3 PRO B 188 ? ARG B 190 ? PRO B 188 ARG B 190 5 ? 3  
HELX_P HELX_P40 AE4 ASP B 195 ? ALA B 197 ? ASP B 195 ALA B 197 5 ? 3  
HELX_P HELX_P41 AE5 TYR B 198 ? GLY B 227 ? TYR B 198 GLY B 227 1 ? 30 
HELX_P HELX_P42 AE6 ASP B 232 ? GLY B 240 ? ASP B 232 GLY B 240 1 ? 9  
HELX_P HELX_P43 AE7 ASP B 250 ? THR B 268 ? ASP B 250 THR B 268 1 ? 19 
HELX_P HELX_P44 AE8 THR B 268 ? ASN B 283 ? THR B 268 ASN B 283 1 ? 16 
HELX_P HELX_P45 AE9 ASN B 283 ? LEU B 298 ? ASN B 283 LEU B 298 1 ? 16 
HELX_P HELX_P46 AF1 SER B 304 ? GLN B 310 ? SER B 304 GLN B 310 1 ? 7  
HELX_P HELX_P47 AF2 LEU B 311 ? TRP B 325 ? LEU B 311 TRP B 325 1 ? 15 
HELX_P HELX_P48 AF3 ILE B 357 ? HIS B 361 ? ILE B 357 HIS B 361 1 ? 5  
HELX_P HELX_P49 AF4 ASP B 363 ? GLY B 368 ? ASP B 363 GLY B 368 1 ? 6  
HELX_P HELX_P50 AF5 ARG B 375 ? GLU B 380 ? ARG B 375 GLU B 380 5 ? 6  
HELX_P HELX_P51 AF6 ASN B 381 ? ILE B 385 ? ASN B 381 ILE B 385 5 ? 5  
HELX_P HELX_P52 AF7 ASN B 395 ? ALA B 399 ? ASN B 395 ALA B 399 5 ? 5  
HELX_P HELX_P53 AF8 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 ? ? ? ? ? ? ? 2.341 ? ? 
metalc2 metalc ? ? C HEM .   FE ? ? ? 1_555 E DMS . S  ? ? A HEM 501 A DMS 503 1_555 ? ? ? ? ? ? ? 2.444 ? ? 
metalc3 metalc ? ? B CYS 400 SG ? ? ? 1_555 H HEM . FE ? ? B CYS 400 B HEM 501 1_555 ? ? ? ? ? ? ? 2.348 ? ? 
metalc4 metalc ? ? H HEM .   FE ? ? ? 1_555 J DMS . S  ? ? B HEM 501 B DMS 503 1_555 ? ? ? ? ? ? ? 2.437 ? ? 
# 
_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 96.7  ? 
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 89.6  ? 
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 88.8  ? 
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 86.6  ? 
5  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 176.1 ? 
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 89.2  ? 
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 97.7  ? 
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 90.8  ? 
9  NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 172.7 ? 
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 90.7  ? 
11 SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 S  ? E DMS . ? A DMS 503 ? 1_555 174.3 ? 
12 NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 S  ? E DMS . ? A DMS 503 ? 1_555 86.5  ? 
13 NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 S  ? E DMS . ? A DMS 503 ? 1_555 85.9  ? 
14 NC ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 S  ? E DMS . ? A DMS 503 ? 1_555 90.0  ? 
15 ND ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 S  ? E DMS . ? A DMS 503 ? 1_555 86.9  ? 
16 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NA ? H HEM . ? B HEM 501 ? 1_555 97.9  ? 
17 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NB ? H HEM . ? B HEM 501 ? 1_555 89.7  ? 
18 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NB ? H HEM . ? B HEM 501 ? 1_555 90.2  ? 
19 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 86.1  ? 
20 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 175.7 ? 
21 NB ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 88.3  ? 
22 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 97.4  ? 
23 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 89.5  ? 
24 NB ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 173.0 ? 
25 NC ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 91.5  ? 
26 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 S  ? J DMS . ? B DMS 503 ? 1_555 174.6 ? 
27 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 S  ? J DMS . ? B DMS 503 ? 1_555 84.7  ? 
28 NB ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 S  ? J DMS . ? B DMS 503 ? 1_555 85.6  ? 
29 NC ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 S  ? J DMS . ? B DMS 503 ? 1_555 91.2  ? 
30 ND ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 S  ? J DMS . ? B DMS 503 ? 1_555 87.3  ? 
# 
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  ? GLU A 43  ? ILE A 39  GLU A 43  
AA1 2 VAL A 48  ? LEU A 52  ? VAL A 48  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 TRP B 47  ? LEU B 52  ? TRP 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 LEU A 49  ? O LEU 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 ALA B 44  ? N ALA B 44  O TRP B 47  ? O TRP B 47  
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                   9ISS 
_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  ? ? 54.64   -126.50 
2  1 ASP A 84  ? ? -98.87  35.98   
3  1 PHE A 158 ? ? -149.97 20.90   
4  1 THR A 268 ? ? -97.23  -65.66  
5  1 GLU A 344 ? ? -143.37 -30.69  
6  1 ASP A 370 ? ? -86.88  33.14   
7  1 THR A 436 ? ? -119.22 -128.94 
8  1 LYS B 15  ? ? 54.17   -128.48 
9  1 PHE B 158 ? ? -155.50 21.55   
10 1 PRO B 188 ? ? -60.98  25.09   
11 1 ARG B 190 ? ? -58.19  109.24  
12 1 ASP B 231 ? ? -88.36  32.50   
13 1 THR B 268 ? ? -99.07  -64.16  
14 1 ASP B 370 ? ? -81.85  31.67   
15 1 THR B 436 ? ? -121.20 -127.38 
# 
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 B THR 1 ? B THR 1 
# 
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  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
GOL C1   C  N N 147 
GOL O1   O  N N 148 
GOL C2   C  N N 149 
GOL O2   O  N N 150 
GOL C3   C  N N 151 
GOL O3   O  N N 152 
GOL H11  H  N N 153 
GOL H12  H  N N 154 
GOL HO1  H  N N 155 
GOL H2   H  N N 156 
GOL HO2  H  N N 157 
GOL H31  H  N N 158 
GOL H32  H  N N 159 
GOL HO3  H  N N 160 
HEM CHA  C  N N 161 
HEM CHB  C  N N 162 
HEM CHC  C  N N 163 
HEM CHD  C  N N 164 
HEM C1A  C  Y N 165 
HEM C2A  C  Y N 166 
HEM C3A  C  Y N 167 
HEM C4A  C  Y N 168 
HEM CMA  C  N N 169 
HEM CAA  C  N N 170 
HEM CBA  C  N N 171 
HEM CGA  C  N N 172 
HEM O1A  O  N N 173 
HEM O2A  O  N N 174 
HEM C1B  C  N N 175 
HEM C2B  C  N N 176 
HEM C3B  C  N N 177 
HEM C4B  C  N N 178 
HEM CMB  C  N N 179 
HEM CAB  C  N N 180 
HEM CBB  C  N N 181 
HEM C1C  C  Y N 182 
HEM C2C  C  Y N 183 
HEM C3C  C  Y N 184 
HEM C4C  C  Y N 185 
HEM CMC  C  N N 186 
HEM CAC  C  N N 187 
HEM CBC  C  N N 188 
HEM C1D  C  N N 189 
HEM C2D  C  N N 190 
HEM C3D  C  N N 191 
HEM C4D  C  N N 192 
HEM CMD  C  N N 193 
HEM CAD  C  N N 194 
HEM CBD  C  N N 195 
HEM CGD  C  N N 196 
HEM O1D  O  N N 197 
HEM O2D  O  N N 198 
HEM NA   N  Y N 199 
HEM NB   N  N N 200 
HEM NC   N  Y N 201 
HEM ND   N  N N 202 
HEM FE   FE N N 203 
HEM HHB  H  N N 204 
HEM HHC  H  N N 205 
HEM HHD  H  N N 206 
HEM HMA  H  N N 207 
HEM HMAA H  N N 208 
HEM HMAB H  N N 209 
HEM HAA  H  N N 210 
HEM HAAA H  N N 211 
HEM HBA  H  N N 212 
HEM HBAA H  N N 213 
HEM HMB  H  N N 214 
HEM HMBA H  N N 215 
HEM HMBB H  N N 216 
HEM HAB  H  N N 217 
HEM HBB  H  N N 218 
HEM HBBA H  N N 219 
HEM HMC  H  N N 220 
HEM HMCA H  N N 221 
HEM HMCB H  N N 222 
HEM HAC  H  N N 223 
HEM HBC  H  N N 224 
HEM HBCA H  N N 225 
HEM HMD  H  N N 226 
HEM HMDA H  N N 227 
HEM HMDB H  N N 228 
HEM HAD  H  N N 229 
HEM HADA H  N N 230 
HEM HBD  H  N N 231 
HEM HBDA H  N N 232 
HEM H2A  H  N N 233 
HEM H2D  H  N N 234 
HEM HHA  H  N N 235 
HIS N    N  N N 236 
HIS CA   C  N S 237 
HIS C    C  N N 238 
HIS O    O  N N 239 
HIS CB   C  N N 240 
HIS CG   C  Y N 241 
HIS ND1  N  Y N 242 
HIS CD2  C  Y N 243 
HIS CE1  C  Y N 244 
HIS NE2  N  Y N 245 
HIS OXT  O  N N 246 
HIS H    H  N N 247 
HIS H2   H  N N 248 
HIS HA   H  N N 249 
HIS HB2  H  N N 250 
HIS HB3  H  N N 251 
HIS HD1  H  N N 252 
HIS HD2  H  N N 253 
HIS HE1  H  N N 254 
HIS HE2  H  N N 255 
HIS HXT  H  N N 256 
HL0 N    N  N N 257 
HL0 C1   C  N N 258 
HL0 O1   O  N N 259 
HL0 C2   C  N N 260 
HL0 O2   O  N N 261 
HL0 C3   C  N N 262 
HL0 O3   O  N N 263 
HL0 C4   C  N N 264 
HL0 C5   C  N N 265 
HL0 C6   C  N N 266 
HL0 C7   C  N N 267 
HL0 C8   C  N N 268 
HL0 C9   C  N N 269 
HL0 C10  C  N N 270 
HL0 C11  C  N S 271 
HL0 C12  C  N N 272 
HL0 C13  C  N N 273 
HL0 C14  C  N N 274 
HL0 HN   H  N N 275 
HL0 H1   H  N N 276 
HL0 H1A  H  N N 277 
HL0 H1B  H  N N 278 
HL0 H2   H  N N 279 
HL0 H2A  H  N N 280 
HL0 H3   H  N N 281 
HL0 H3A  H  N N 282 
HL0 H4   H  N N 283 
HL0 H4A  H  N N 284 
HL0 H5   H  N N 285 
HL0 H5A  H  N N 286 
HL0 H6   H  N N 287 
HL0 H6A  H  N N 288 
HL0 H7   H  N N 289 
HL0 H7A  H  N N 290 
HL0 H8   H  N N 291 
HL0 H8A  H  N N 292 
HL0 H9   H  N N 293 
HL0 H9A  H  N N 294 
HL0 H11  H  N N 295 
HL0 H12  H  N N 296 
HL0 H12A H  N N 297 
HL0 H13  H  N N 298 
HL0 H13A H  N N 299 
HOH O    O  N N 300 
HOH H1   H  N N 301 
HOH H2   H  N N 302 
ILE N    N  N N 303 
ILE CA   C  N S 304 
ILE C    C  N N 305 
ILE O    O  N N 306 
ILE CB   C  N S 307 
ILE CG1  C  N N 308 
ILE CG2  C  N N 309 
ILE CD1  C  N N 310 
ILE OXT  O  N N 311 
ILE H    H  N N 312 
ILE H2   H  N N 313 
ILE HA   H  N N 314 
ILE HB   H  N N 315 
ILE HG12 H  N N 316 
ILE HG13 H  N N 317 
ILE HG21 H  N N 318 
ILE HG22 H  N N 319 
ILE HG23 H  N N 320 
ILE HD11 H  N N 321 
ILE HD12 H  N N 322 
ILE HD13 H  N N 323 
ILE HXT  H  N N 324 
LEU N    N  N N 325 
LEU CA   C  N S 326 
LEU C    C  N N 327 
LEU O    O  N N 328 
LEU CB   C  N N 329 
LEU CG   C  N N 330 
LEU CD1  C  N N 331 
LEU CD2  C  N N 332 
LEU OXT  O  N N 333 
LEU H    H  N N 334 
LEU H2   H  N N 335 
LEU HA   H  N N 336 
LEU HB2  H  N N 337 
LEU HB3  H  N N 338 
LEU HG   H  N N 339 
LEU HD11 H  N N 340 
LEU HD12 H  N N 341 
LEU HD13 H  N N 342 
LEU HD21 H  N N 343 
LEU HD22 H  N N 344 
LEU HD23 H  N N 345 
LEU HXT  H  N N 346 
LYS N    N  N N 347 
LYS CA   C  N S 348 
LYS C    C  N N 349 
LYS O    O  N N 350 
LYS CB   C  N N 351 
LYS CG   C  N N 352 
LYS CD   C  N N 353 
LYS CE   C  N N 354 
LYS NZ   N  N N 355 
LYS OXT  O  N N 356 
LYS H    H  N N 357 
LYS H2   H  N N 358 
LYS HA   H  N N 359 
LYS HB2  H  N N 360 
LYS HB3  H  N N 361 
LYS HG2  H  N N 362 
LYS HG3  H  N N 363 
LYS HD2  H  N N 364 
LYS HD3  H  N N 365 
LYS HE2  H  N N 366 
LYS HE3  H  N N 367 
LYS HZ1  H  N N 368 
LYS HZ2  H  N N 369 
LYS HZ3  H  N N 370 
LYS HXT  H  N N 371 
MET N    N  N N 372 
MET CA   C  N S 373 
MET C    C  N N 374 
MET O    O  N N 375 
MET CB   C  N N 376 
MET CG   C  N N 377 
MET SD   S  N N 378 
MET CE   C  N N 379 
MET OXT  O  N N 380 
MET H    H  N N 381 
MET H2   H  N N 382 
MET HA   H  N N 383 
MET HB2  H  N N 384 
MET HB3  H  N N 385 
MET HG2  H  N N 386 
MET HG3  H  N N 387 
MET HE1  H  N N 388 
MET HE2  H  N N 389 
MET HE3  H  N N 390 
MET HXT  H  N N 391 
PHE N    N  N N 392 
PHE CA   C  N S 393 
PHE C    C  N N 394 
PHE O    O  N N 395 
PHE CB   C  N N 396 
PHE CG   C  Y N 397 
PHE CD1  C  Y N 398 
PHE CD2  C  Y N 399 
PHE CE1  C  Y N 400 
PHE CE2  C  Y N 401 
PHE CZ   C  Y N 402 
PHE OXT  O  N N 403 
PHE H    H  N N 404 
PHE H2   H  N N 405 
PHE HA   H  N N 406 
PHE HB2  H  N N 407 
PHE HB3  H  N N 408 
PHE HD1  H  N N 409 
PHE HD2  H  N N 410 
PHE HE1  H  N N 411 
PHE HE2  H  N N 412 
PHE HZ   H  N N 413 
PHE HXT  H  N N 414 
PRO N    N  N N 415 
PRO CA   C  N S 416 
PRO C    C  N N 417 
PRO O    O  N N 418 
PRO CB   C  N N 419 
PRO CG   C  N N 420 
PRO CD   C  N N 421 
PRO OXT  O  N N 422 
PRO H    H  N N 423 
PRO HA   H  N N 424 
PRO HB2  H  N N 425 
PRO HB3  H  N N 426 
PRO HG2  H  N N 427 
PRO HG3  H  N N 428 
PRO HD2  H  N N 429 
PRO HD3  H  N N 430 
PRO HXT  H  N N 431 
SER N    N  N N 432 
SER CA   C  N S 433 
SER C    C  N N 434 
SER O    O  N N 435 
SER CB   C  N N 436 
SER OG   O  N N 437 
SER OXT  O  N N 438 
SER H    H  N N 439 
SER H2   H  N N 440 
SER HA   H  N N 441 
SER HB2  H  N N 442 
SER HB3  H  N N 443 
SER HG   H  N N 444 
SER HXT  H  N N 445 
THR N    N  N N 446 
THR CA   C  N S 447 
THR C    C  N N 448 
THR O    O  N N 449 
THR CB   C  N R 450 
THR OG1  O  N N 451 
THR CG2  C  N N 452 
THR OXT  O  N N 453 
THR H    H  N N 454 
THR H2   H  N N 455 
THR HA   H  N N 456 
THR HB   H  N N 457 
THR HG1  H  N N 458 
THR HG21 H  N N 459 
THR HG22 H  N N 460 
THR HG23 H  N N 461 
THR HXT  H  N N 462 
TRP N    N  N N 463 
TRP CA   C  N S 464 
TRP C    C  N N 465 
TRP O    O  N N 466 
TRP CB   C  N N 467 
TRP CG   C  Y N 468 
TRP CD1  C  Y N 469 
TRP CD2  C  Y N 470 
TRP NE1  N  Y N 471 
TRP CE2  C  Y N 472 
TRP CE3  C  Y N 473 
TRP CZ2  C  Y N 474 
TRP CZ3  C  Y N 475 
TRP CH2  C  Y N 476 
TRP OXT  O  N N 477 
TRP H    H  N N 478 
TRP H2   H  N N 479 
TRP HA   H  N N 480 
TRP HB2  H  N N 481 
TRP HB3  H  N N 482 
TRP HD1  H  N N 483 
TRP HE1  H  N N 484 
TRP HE3  H  N N 485 
TRP HZ2  H  N N 486 
TRP HZ3  H  N N 487 
TRP HH2  H  N N 488 
TRP HXT  H  N N 489 
TYR N    N  N N 490 
TYR CA   C  N S 491 
TYR C    C  N N 492 
TYR O    O  N N 493 
TYR CB   C  N N 494 
TYR CG   C  Y N 495 
TYR CD1  C  Y N 496 
TYR CD2  C  Y N 497 
TYR CE1  C  Y N 498 
TYR CE2  C  Y N 499 
TYR CZ   C  Y N 500 
TYR OH   O  N N 501 
TYR OXT  O  N N 502 
TYR H    H  N N 503 
TYR H2   H  N N 504 
TYR HA   H  N N 505 
TYR HB2  H  N N 506 
TYR HB3  H  N N 507 
TYR HD1  H  N N 508 
TYR HD2  H  N N 509 
TYR HE1  H  N N 510 
TYR HE2  H  N N 511 
TYR HH   H  N N 512 
TYR HXT  H  N N 513 
VAL N    N  N N 514 
VAL CA   C  N S 515 
VAL C    C  N N 516 
VAL O    O  N N 517 
VAL CB   C  N N 518 
VAL CG1  C  N N 519 
VAL CG2  C  N N 520 
VAL OXT  O  N N 521 
VAL H    H  N N 522 
VAL H2   H  N N 523 
VAL HA   H  N N 524 
VAL HB   H  N N 525 
VAL HG11 H  N N 526 
VAL HG12 H  N N 527 
VAL HG13 H  N N 528 
VAL HG21 H  N N 529 
VAL HG22 H  N N 530 
VAL HG23 H  N N 531 
VAL HXT  H  N N 532 
# 
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  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
GOL C1  O1   sing N N 138 
GOL C1  C2   sing N N 139 
GOL C1  H11  sing N N 140 
GOL C1  H12  sing N N 141 
GOL O1  HO1  sing N N 142 
GOL C2  O2   sing N N 143 
GOL C2  C3   sing N N 144 
GOL C2  H2   sing N N 145 
GOL O2  HO2  sing N N 146 
GOL C3  O3   sing N N 147 
GOL C3  H31  sing N N 148 
GOL C3  H32  sing N N 149 
GOL O3  HO3  sing N N 150 
HEM CHA C1A  sing N N 151 
HEM CHA C4D  doub N N 152 
HEM CHA HHA  sing N N 153 
HEM CHB C4A  sing N N 154 
HEM CHB C1B  doub N N 155 
HEM CHB HHB  sing N N 156 
HEM CHC C4B  sing N N 157 
HEM CHC C1C  doub N N 158 
HEM CHC HHC  sing N N 159 
HEM CHD C4C  doub N N 160 
HEM CHD C1D  sing N N 161 
HEM CHD HHD  sing N N 162 
HEM C1A C2A  doub Y N 163 
HEM C1A NA   sing Y N 164 
HEM C2A C3A  sing Y N 165 
HEM C2A CAA  sing N N 166 
HEM C3A C4A  doub Y N 167 
HEM C3A CMA  sing N N 168 
HEM C4A NA   sing Y N 169 
HEM CMA HMA  sing N N 170 
HEM CMA HMAA sing N N 171 
HEM CMA HMAB sing N N 172 
HEM CAA CBA  sing N N 173 
HEM CAA HAA  sing N N 174 
HEM CAA HAAA sing N N 175 
HEM CBA CGA  sing N N 176 
HEM CBA HBA  sing N N 177 
HEM CBA HBAA sing N N 178 
HEM CGA O1A  doub N N 179 
HEM CGA O2A  sing N N 180 
HEM C1B C2B  sing N N 181 
HEM C1B NB   sing N N 182 
HEM C2B C3B  doub N N 183 
HEM C2B CMB  sing N N 184 
HEM C3B C4B  sing N N 185 
HEM C3B CAB  sing N N 186 
HEM C4B NB   doub N N 187 
HEM CMB HMB  sing N N 188 
HEM CMB HMBA sing N N 189 
HEM CMB HMBB sing N N 190 
HEM CAB CBB  doub N N 191 
HEM CAB HAB  sing N N 192 
HEM CBB HBB  sing N N 193 
HEM CBB HBBA sing N N 194 
HEM C1C C2C  sing Y N 195 
HEM C1C NC   sing Y N 196 
HEM C2C C3C  doub Y N 197 
HEM C2C CMC  sing N N 198 
HEM C3C C4C  sing Y N 199 
HEM C3C CAC  sing N N 200 
HEM C4C NC   sing Y N 201 
HEM CMC HMC  sing N N 202 
HEM CMC HMCA sing N N 203 
HEM CMC HMCB sing N N 204 
HEM CAC CBC  doub N N 205 
HEM CAC HAC  sing N N 206 
HEM CBC HBC  sing N N 207 
HEM CBC HBCA sing N N 208 
HEM C1D C2D  sing N N 209 
HEM C1D ND   doub N N 210 
HEM C2D C3D  doub N N 211 
HEM C2D CMD  sing N N 212 
HEM C3D C4D  sing N N 213 
HEM C3D CAD  sing N N 214 
HEM C4D ND   sing N N 215 
HEM CMD HMD  sing N N 216 
HEM CMD HMDA sing N N 217 
HEM CMD HMDB sing N N 218 
HEM CAD CBD  sing N N 219 
HEM CAD HAD  sing N N 220 
HEM CAD HADA sing N N 221 
HEM CBD CGD  sing N N 222 
HEM CBD HBD  sing N N 223 
HEM CBD HBDA sing N N 224 
HEM CGD O1D  doub N N 225 
HEM CGD O2D  sing N N 226 
HEM O2A H2A  sing N N 227 
HEM O2D H2D  sing N N 228 
HEM FE  NA   sing N N 229 
HEM FE  NB   sing N N 230 
HEM FE  NC   sing N N 231 
HEM FE  ND   sing N N 232 
HIS N   CA   sing N N 233 
HIS N   H    sing N N 234 
HIS N   H2   sing N N 235 
HIS CA  C    sing N N 236 
HIS CA  CB   sing N N 237 
HIS CA  HA   sing N N 238 
HIS C   O    doub N N 239 
HIS C   OXT  sing N N 240 
HIS CB  CG   sing N N 241 
HIS CB  HB2  sing N N 242 
HIS CB  HB3  sing N N 243 
HIS CG  ND1  sing Y N 244 
HIS CG  CD2  doub Y N 245 
HIS ND1 CE1  doub Y N 246 
HIS ND1 HD1  sing N N 247 
HIS CD2 NE2  sing Y N 248 
HIS CD2 HD2  sing N N 249 
HIS CE1 NE2  sing Y N 250 
HIS CE1 HE1  sing N N 251 
HIS NE2 HE2  sing N N 252 
HIS OXT HXT  sing N N 253 
HL0 N   C10  sing N N 254 
HL0 N   C11  sing N N 255 
HL0 C1  C2   sing N N 256 
HL0 O1  C10  doub N N 257 
HL0 C2  C3   sing N N 258 
HL0 O2  C13  sing N N 259 
HL0 O2  C14  sing N N 260 
HL0 C3  C4   sing N N 261 
HL0 O3  C14  doub N N 262 
HL0 C4  C5   sing N N 263 
HL0 C5  C6   sing N N 264 
HL0 C6  C7   sing N N 265 
HL0 C7  C8   sing N N 266 
HL0 C8  C9   sing N N 267 
HL0 C9  C10  sing N N 268 
HL0 C11 C12  sing N N 269 
HL0 C11 C14  sing N N 270 
HL0 C12 C13  sing N N 271 
HL0 N   HN   sing N N 272 
HL0 C1  H1   sing N N 273 
HL0 C1  H1A  sing N N 274 
HL0 C1  H1B  sing N N 275 
HL0 C2  H2   sing N N 276 
HL0 C2  H2A  sing N N 277 
HL0 C3  H3   sing N N 278 
HL0 C3  H3A  sing N N 279 
HL0 C4  H4   sing N N 280 
HL0 C4  H4A  sing N N 281 
HL0 C5  H5   sing N N 282 
HL0 C5  H5A  sing N N 283 
HL0 C6  H6   sing N N 284 
HL0 C6  H6A  sing N N 285 
HL0 C7  H7   sing N N 286 
HL0 C7  H7A  sing N N 287 
HL0 C8  H8   sing N N 288 
HL0 C8  H8A  sing N N 289 
HL0 C9  H9   sing N N 290 
HL0 C9  H9A  sing N N 291 
HL0 C11 H11  sing N N 292 
HL0 C12 H12  sing N N 293 
HL0 C12 H12A sing N N 294 
HL0 C13 H13  sing N N 295 
HL0 C13 H13A sing N N 296 
HOH O   H1   sing N N 297 
HOH O   H2   sing N N 298 
ILE N   CA   sing N N 299 
ILE N   H    sing N N 300 
ILE N   H2   sing N N 301 
ILE CA  C    sing N N 302 
ILE CA  CB   sing N N 303 
ILE CA  HA   sing N N 304 
ILE C   O    doub N N 305 
ILE C   OXT  sing N N 306 
ILE CB  CG1  sing N N 307 
ILE CB  CG2  sing N N 308 
ILE CB  HB   sing N N 309 
ILE CG1 CD1  sing N N 310 
ILE CG1 HG12 sing N N 311 
ILE CG1 HG13 sing N N 312 
ILE CG2 HG21 sing N N 313 
ILE CG2 HG22 sing N N 314 
ILE CG2 HG23 sing N N 315 
ILE CD1 HD11 sing N N 316 
ILE CD1 HD12 sing N N 317 
ILE CD1 HD13 sing N N 318 
ILE OXT HXT  sing N N 319 
LEU N   CA   sing N N 320 
LEU N   H    sing N N 321 
LEU N   H2   sing N N 322 
LEU CA  C    sing N N 323 
LEU CA  CB   sing N N 324 
LEU CA  HA   sing N N 325 
LEU C   O    doub N N 326 
LEU C   OXT  sing N N 327 
LEU CB  CG   sing N N 328 
LEU CB  HB2  sing N N 329 
LEU CB  HB3  sing N N 330 
LEU CG  CD1  sing N N 331 
LEU CG  CD2  sing N N 332 
LEU CG  HG   sing N N 333 
LEU CD1 HD11 sing N N 334 
LEU CD1 HD12 sing N N 335 
LEU CD1 HD13 sing N N 336 
LEU CD2 HD21 sing N N 337 
LEU CD2 HD22 sing N N 338 
LEU CD2 HD23 sing N N 339 
LEU OXT HXT  sing N N 340 
LYS N   CA   sing N N 341 
LYS N   H    sing N N 342 
LYS N   H2   sing N N 343 
LYS CA  C    sing N N 344 
LYS CA  CB   sing N N 345 
LYS CA  HA   sing N N 346 
LYS C   O    doub N N 347 
LYS C   OXT  sing N N 348 
LYS CB  CG   sing N N 349 
LYS CB  HB2  sing N N 350 
LYS CB  HB3  sing N N 351 
LYS CG  CD   sing N N 352 
LYS CG  HG2  sing N N 353 
LYS CG  HG3  sing N N 354 
LYS CD  CE   sing N N 355 
LYS CD  HD2  sing N N 356 
LYS CD  HD3  sing N N 357 
LYS CE  NZ   sing N N 358 
LYS CE  HE2  sing N N 359 
LYS CE  HE3  sing N N 360 
LYS NZ  HZ1  sing N N 361 
LYS NZ  HZ2  sing N N 362 
LYS NZ  HZ3  sing N N 363 
LYS OXT HXT  sing N N 364 
MET N   CA   sing N N 365 
MET N   H    sing N N 366 
MET N   H2   sing N N 367 
MET CA  C    sing N N 368 
MET CA  CB   sing N N 369 
MET CA  HA   sing N N 370 
MET C   O    doub N N 371 
MET C   OXT  sing N N 372 
MET CB  CG   sing N N 373 
MET CB  HB2  sing N N 374 
MET CB  HB3  sing N N 375 
MET CG  SD   sing N N 376 
MET CG  HG2  sing N N 377 
MET CG  HG3  sing N N 378 
MET SD  CE   sing N N 379 
MET CE  HE1  sing N N 380 
MET CE  HE2  sing N N 381 
MET CE  HE3  sing N N 382 
MET OXT HXT  sing N N 383 
PHE N   CA   sing N N 384 
PHE N   H    sing N N 385 
PHE N   H2   sing N N 386 
PHE CA  C    sing N N 387 
PHE CA  CB   sing N N 388 
PHE CA  HA   sing N N 389 
PHE C   O    doub N N 390 
PHE C   OXT  sing N N 391 
PHE CB  CG   sing N N 392 
PHE CB  HB2  sing N N 393 
PHE CB  HB3  sing N N 394 
PHE CG  CD1  doub Y N 395 
PHE CG  CD2  sing Y N 396 
PHE CD1 CE1  sing Y N 397 
PHE CD1 HD1  sing N N 398 
PHE CD2 CE2  doub Y N 399 
PHE CD2 HD2  sing N N 400 
PHE CE1 CZ   doub Y N 401 
PHE CE1 HE1  sing N N 402 
PHE CE2 CZ   sing Y N 403 
PHE CE2 HE2  sing N N 404 
PHE CZ  HZ   sing N N 405 
PHE OXT HXT  sing N N 406 
PRO N   CA   sing N N 407 
PRO N   CD   sing N N 408 
PRO N   H    sing N N 409 
PRO CA  C    sing N N 410 
PRO CA  CB   sing N N 411 
PRO CA  HA   sing N N 412 
PRO C   O    doub N N 413 
PRO C   OXT  sing N N 414 
PRO CB  CG   sing N N 415 
PRO CB  HB2  sing N N 416 
PRO CB  HB3  sing N N 417 
PRO CG  CD   sing N N 418 
PRO CG  HG2  sing N N 419 
PRO CG  HG3  sing N N 420 
PRO CD  HD2  sing N N 421 
PRO CD  HD3  sing N N 422 
PRO OXT HXT  sing N N 423 
SER N   CA   sing N N 424 
SER N   H    sing N N 425 
SER N   H2   sing N N 426 
SER CA  C    sing N N 427 
SER CA  CB   sing N N 428 
SER CA  HA   sing N N 429 
SER C   O    doub N N 430 
SER C   OXT  sing N N 431 
SER CB  OG   sing N N 432 
SER CB  HB2  sing N N 433 
SER CB  HB3  sing N N 434 
SER OG  HG   sing N N 435 
SER OXT HXT  sing N N 436 
THR N   CA   sing N N 437 
THR N   H    sing N N 438 
THR N   H2   sing N N 439 
THR CA  C    sing N N 440 
THR CA  CB   sing N N 441 
THR CA  HA   sing N N 442 
THR C   O    doub N N 443 
THR C   OXT  sing N N 444 
THR CB  OG1  sing N N 445 
THR CB  CG2  sing N N 446 
THR CB  HB   sing N N 447 
THR OG1 HG1  sing N N 448 
THR CG2 HG21 sing N N 449 
THR CG2 HG22 sing N N 450 
THR CG2 HG23 sing N N 451 
THR OXT HXT  sing N N 452 
TRP N   CA   sing N N 453 
TRP N   H    sing N N 454 
TRP N   H2   sing N N 455 
TRP CA  C    sing N N 456 
TRP CA  CB   sing N N 457 
TRP CA  HA   sing N N 458 
TRP C   O    doub N N 459 
TRP C   OXT  sing N N 460 
TRP CB  CG   sing N N 461 
TRP CB  HB2  sing N N 462 
TRP CB  HB3  sing N N 463 
TRP CG  CD1  doub Y N 464 
TRP CG  CD2  sing Y N 465 
TRP CD1 NE1  sing Y N 466 
TRP CD1 HD1  sing N N 467 
TRP CD2 CE2  doub Y N 468 
TRP CD2 CE3  sing Y N 469 
TRP NE1 CE2  sing Y N 470 
TRP NE1 HE1  sing N N 471 
TRP CE2 CZ2  sing Y N 472 
TRP CE3 CZ3  doub Y N 473 
TRP CE3 HE3  sing N N 474 
TRP CZ2 CH2  doub Y N 475 
TRP CZ2 HZ2  sing N N 476 
TRP CZ3 CH2  sing Y N 477 
TRP CZ3 HZ3  sing N N 478 
TRP CH2 HH2  sing N N 479 
TRP OXT HXT  sing N N 480 
TYR N   CA   sing N N 481 
TYR N   H    sing N N 482 
TYR N   H2   sing N N 483 
TYR CA  C    sing N N 484 
TYR CA  CB   sing N N 485 
TYR CA  HA   sing N N 486 
TYR C   O    doub N N 487 
TYR C   OXT  sing N N 488 
TYR CB  CG   sing N N 489 
TYR CB  HB2  sing N N 490 
TYR CB  HB3  sing N N 491 
TYR CG  CD1  doub Y N 492 
TYR CG  CD2  sing Y N 493 
TYR CD1 CE1  sing Y N 494 
TYR CD1 HD1  sing N N 495 
TYR CD2 CE2  doub Y N 496 
TYR CD2 HD2  sing N N 497 
TYR CE1 CZ   doub Y N 498 
TYR CE1 HE1  sing N N 499 
TYR CE2 CZ   sing Y N 500 
TYR CE2 HE2  sing N N 501 
TYR CZ  OH   sing N N 502 
TYR OH  HH   sing N N 503 
TYR OXT HXT  sing N N 504 
VAL N   CA   sing N N 505 
VAL N   H    sing N N 506 
VAL N   H2   sing N N 507 
VAL CA  C    sing N N 508 
VAL CA  CB   sing N N 509 
VAL CA  HA   sing N N 510 
VAL C   O    doub N N 511 
VAL C   OXT  sing N N 512 
VAL CB  CG1  sing N N 513 
VAL CB  CG2  sing N N 514 
VAL CB  HB   sing N N 515 
VAL CG1 HG11 sing N N 516 
VAL CG1 HG12 sing N N 517 
VAL CG1 HG13 sing N N 518 
VAL CG2 HG21 sing N N 519 
VAL CG2 HG22 sing N N 520 
VAL CG2 HG23 sing N N 521 
VAL OXT HXT  sing N N 522 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Society for the Promotion of Science (JSPS)' Japan JP22H05129 1 
'Japan Society for the Promotion of Science (JSPS)' Japan JP21H04704 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6JLV 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9ISS 
_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]   0.017072 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002207 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006876 
_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]   0.015978 
_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 
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   . ILE A 1 2   ? 18.715  59.598  24.150  1.00 47.26 ? 2   ILE A N   1 
ATOM   2    C  CA  . ILE A 1 2   ? 19.180  58.445  25.002  1.00 44.19 ? 2   ILE A CA  1 
ATOM   3    C  C   . ILE A 1 2   ? 18.052  58.054  25.963  1.00 46.72 ? 2   ILE A C   1 
ATOM   4    O  O   . ILE A 1 2   ? 17.712  58.859  26.838  1.00 45.35 ? 2   ILE A O   1 
ATOM   5    C  CB  . ILE A 1 2   ? 20.491  58.770  25.748  1.00 44.72 ? 2   ILE A CB  1 
ATOM   6    C  CG1 . ILE A 1 2   ? 21.687  58.928  24.799  1.00 49.64 ? 2   ILE A CG1 1 
ATOM   7    C  CG2 . ILE A 1 2   ? 20.773  57.748  26.840  1.00 45.35 ? 2   ILE A CG2 1 
ATOM   8    C  CD1 . ILE A 1 2   ? 21.821  57.855  23.724  1.00 49.83 ? 2   ILE A CD1 1 
ATOM   9    N  N   . LYS A 1 3   ? 17.514  56.845  25.786  1.00 43.73 ? 3   LYS A N   1 
ATOM   10   C  CA  . LYS A 1 3   ? 16.395  56.239  26.561  1.00 43.21 ? 3   LYS A CA  1 
ATOM   11   C  C   . LYS A 1 3   ? 16.924  55.195  27.559  1.00 39.79 ? 3   LYS A C   1 
ATOM   12   O  O   . LYS A 1 3   ? 17.951  54.511  27.271  1.00 38.25 ? 3   LYS A O   1 
ATOM   13   C  CB  . LYS A 1 3   ? 15.432  55.495  25.629  1.00 45.48 ? 3   LYS A CB  1 
ATOM   14   C  CG  . LYS A 1 3   ? 14.350  56.323  24.956  1.00 51.69 ? 3   LYS A CG  1 
ATOM   15   C  CD  . LYS A 1 3   ? 13.114  55.485  24.660  1.00 54.68 ? 3   LYS A CD  1 
ATOM   16   C  CE  . LYS A 1 3   ? 12.204  56.055  23.591  1.00 57.24 ? 3   LYS A CE  1 
ATOM   17   N  NZ  . LYS A 1 3   ? 11.846  55.026  22.582  1.00 56.00 ? 3   LYS A NZ  1 
ATOM   18   N  N   . GLU A 1 4   ? 16.196  55.030  28.661  1.00 35.15 ? 4   GLU A N   1 
ATOM   19   C  CA  . GLU A 1 4   ? 16.414  53.946  29.650  1.00 37.78 ? 4   GLU A CA  1 
ATOM   20   C  C   . GLU A 1 4   ? 15.637  52.721  29.157  1.00 32.57 ? 4   GLU A C   1 
ATOM   21   O  O   . GLU A 1 4   ? 14.479  52.889  28.767  1.00 33.48 ? 4   GLU A O   1 
ATOM   22   C  CB  . GLU A 1 4   ? 15.910  54.404  31.017  1.00 41.91 ? 4   GLU A CB  1 
ATOM   23   C  CG  . GLU A 1 4   ? 15.684  53.287  32.012  1.00 46.30 ? 4   GLU A CG  1 
ATOM   24   C  CD  . GLU A 1 4   ? 15.037  53.758  33.305  1.00 55.28 ? 4   GLU A CD  1 
ATOM   25   O  OE1 . GLU A 1 4   ? 13.805  53.988  33.305  1.00 57.46 ? 4   GLU A OE1 1 
ATOM   26   O  OE2 . GLU A 1 4   ? 15.768  53.924  34.302  1.00 53.40 ? 4   GLU A OE2 1 
ATOM   27   N  N   . MET A 1 5   ? 16.227  51.533  29.157  1.00 28.58 ? 5   MET A N   1 
ATOM   28   C  CA  . MET A 1 5   ? 15.461  50.391  28.612  1.00 26.73 ? 5   MET A CA  1 
ATOM   29   C  C   . MET A 1 5   ? 14.607  49.764  29.704  1.00 22.26 ? 5   MET A C   1 
ATOM   30   O  O   . MET A 1 5   ? 14.989  49.676  30.860  1.00 22.64 ? 5   MET A O   1 
ATOM   31   C  CB  . MET A 1 5   ? 16.307  49.356  27.863  1.00 29.49 ? 5   MET A CB  1 
ATOM   32   C  CG  . MET A 1 5   ? 17.090  48.421  28.640  1.00 30.17 ? 5   MET A CG  1 
ATOM   33   S  SD  . MET A 1 5   ? 17.902  47.410  27.366  1.00 27.24 ? 5   MET A SD  1 
ATOM   34   C  CE  . MET A 1 5   ? 18.879  48.638  26.521  1.00 26.73 ? 5   MET A CE  1 
ATOM   35   N  N   . PRO A 1 6   ? 13.409  49.320  29.302  1.00 19.39 ? 6   PRO A N   1 
ATOM   36   C  CA  . PRO A 1 6   ? 12.518  48.568  30.149  1.00 20.07 ? 6   PRO A CA  1 
ATOM   37   C  C   . PRO A 1 6   ? 13.180  47.288  30.681  1.00 18.98 ? 6   PRO A C   1 
ATOM   38   O  O   . PRO A 1 6   ? 14.128  46.794  30.086  1.00 18.14 ? 6   PRO A O   1 
ATOM   39   C  CB  . PRO A 1 6   ? 11.412  48.158  29.151  1.00 21.18 ? 6   PRO A CB  1 
ATOM   40   C  CG  . PRO A 1 6   ? 11.431  49.198  28.112  1.00 23.65 ? 6   PRO A CG  1 
ATOM   41   C  CD  . PRO A 1 6   ? 12.885  49.514  27.951  1.00 20.54 ? 6   PRO A CD  1 
ATOM   42   N  N   . GLN A 1 7   ? 12.690  46.782  31.792  1.00 17.23 ? 7   GLN A N   1 
ATOM   43   C  CA  . GLN A 1 7   ? 13.213  45.576  32.453  1.00 17.77 ? 7   GLN A CA  1 
ATOM   44   C  C   . GLN A 1 7   ? 12.022  44.865  33.054  1.00 17.44 ? 7   GLN A C   1 
ATOM   45   O  O   . GLN A 1 7   ? 11.177  45.510  33.690  1.00 17.44 ? 7   GLN A O   1 
ATOM   46   C  CB  . GLN A 1 7   ? 14.269  45.938  33.485  1.00 18.14 ? 7   GLN A CB  1 
ATOM   47   C  CG  . GLN A 1 7   ? 14.826  44.711  34.197  1.00 19.28 ? 7   GLN A CG  1 
ATOM   48   C  CD  . GLN A 1 7   ? 15.768  44.980  35.339  1.00 22.65 ? 7   GLN A CD  1 
ATOM   49   O  OE1 . GLN A 1 7   ? 15.903  46.116  35.784  1.00 25.67 ? 7   GLN A OE1 1 
ATOM   50   N  NE2 . GLN A 1 7   ? 16.425  43.946  35.797  1.00 21.52 ? 7   GLN A NE2 1 
ATOM   51   N  N   . PRO A 1 8   ? 11.888  43.542  32.861  1.00 15.41 ? 8   PRO A N   1 
ATOM   52   C  CA  . PRO A 1 8   ? 10.802  42.782  33.471  1.00 14.85 ? 8   PRO A CA  1 
ATOM   53   C  C   . PRO A 1 8   ? 10.958  42.670  34.994  1.00 14.73 ? 8   PRO A C   1 
ATOM   54   O  O   . PRO A 1 8   ? 11.987  43.037  35.575  1.00 14.83 ? 8   PRO A O   1 
ATOM   55   C  CB  . PRO A 1 8   ? 10.831  41.433  32.729  1.00 15.14 ? 8   PRO A CB  1 
ATOM   56   C  CG  . PRO A 1 8   ? 12.287  41.290  32.345  1.00 14.36 ? 8   PRO A CG  1 
ATOM   57   C  CD  . PRO A 1 8   ? 12.750  42.678  32.022  1.00 14.87 ? 8   PRO A CD  1 
ATOM   58   N  N   . LYS A 1 9   ? 9.975   42.024  35.589  1.00 15.32 ? 9   LYS A N   1 
ATOM   59   C  CA  . LYS A 1 9   ? 9.879   41.884  37.057  1.00 14.57 ? 9   LYS A CA  1 
ATOM   60   C  C   . LYS A 1 9   ? 11.088  41.154  37.628  1.00 14.27 ? 9   LYS A C   1 
ATOM   61   O  O   . LYS A 1 9   ? 11.640  40.190  37.031  1.00 15.18 ? 9   LYS A O   1 
ATOM   62   C  CB  . LYS A 1 9   ? 8.583   41.193  37.467  1.00 14.40 ? 9   LYS A CB  1 
ATOM   63   C  CG  . LYS A 1 9   ? 8.421   39.764  36.986  1.00 15.31 ? 9   LYS A CG  1 
ATOM   64   C  CD  . LYS A 1 9   ? 6.999   39.284  37.178  1.00 15.49 ? 9   LYS A CD  1 
ATOM   65   C  CE  . LYS A 1 9   ? 6.796   37.870  36.700  1.00 18.76 ? 9   LYS A CE  1 
ATOM   66   N  NZ  . LYS A 1 9   ? 5.346   37.608  36.497  1.00 21.92 ? 9   LYS A NZ  1 
ATOM   67   N  N   . THR A 1 10  ? 11.498  41.547  38.844  1.00 14.13 ? 10  THR A N   1 
ATOM   68   C  CA  . THR A 1 10  ? 12.678  41.003  39.545  1.00 14.46 ? 10  THR A CA  1 
ATOM   69   C  C   . THR A 1 10  ? 12.326  40.231  40.821  1.00 13.25 ? 10  THR A C   1 
ATOM   70   O  O   . THR A 1 10  ? 11.179  40.336  41.337  1.00 14.01 ? 10  THR A O   1 
ATOM   71   C  CB  . THR A 1 10  ? 13.638  42.151  39.875  1.00 15.48 ? 10  THR A CB  1 
ATOM   72   O  OG1 . THR A 1 10  ? 12.933  43.091  40.705  1.00 17.74 ? 10  THR A OG1 1 
ATOM   73   C  CG2 . THR A 1 10  ? 14.202  42.813  38.647  1.00 16.03 ? 10  THR A CG2 1 
ATOM   74   N  N   . PHE A 1 11  ? 13.290  39.484  41.296  1.00 13.78 ? 11  PHE A N   1 
ATOM   75   C  CA  . PHE A 1 11  ? 13.179  38.492  42.373  1.00 14.79 ? 11  PHE A CA  1 
ATOM   76   C  C   . PHE A 1 11  ? 14.351  38.747  43.338  1.00 16.86 ? 11  PHE A C   1 
ATOM   77   O  O   . PHE A 1 11  ? 15.153  37.844  43.579  1.00 16.60 ? 11  PHE A O   1 
ATOM   78   C  CB  . PHE A 1 11  ? 13.246  37.072  41.835  1.00 16.14 ? 11  PHE A CB  1 
ATOM   79   C  CG  . PHE A 1 11  ? 12.118  36.695  40.912  1.00 14.05 ? 11  PHE A CG  1 
ATOM   80   C  CD1 . PHE A 1 11  ? 12.052  37.227  39.630  1.00 14.44 ? 11  PHE A CD1 1 
ATOM   81   C  CD2 . PHE A 1 11  ? 11.124  35.821  41.321  1.00 12.69 ? 11  PHE A CD2 1 
ATOM   82   C  CE1 . PHE A 1 11  ? 11.000  36.878  38.794  1.00 15.04 ? 11  PHE A CE1 1 
ATOM   83   C  CE2 . PHE A 1 11  ? 10.071  35.482  40.487  1.00 14.38 ? 11  PHE A CE2 1 
ATOM   84   C  CZ  . PHE A 1 11  ? 10.004  36.021  39.232  1.00 14.53 ? 11  PHE A CZ  1 
ATOM   85   N  N   . GLY A 1 12  ? 14.411  39.971  43.855  1.00 17.64 ? 12  GLY A N   1 
ATOM   86   C  CA  . GLY A 1 12  ? 15.451  40.357  44.830  1.00 18.56 ? 12  GLY A CA  1 
ATOM   87   C  C   . GLY A 1 12  ? 16.831  40.100  44.278  1.00 19.06 ? 12  GLY A C   1 
ATOM   88   O  O   . GLY A 1 12  ? 17.075  40.511  43.158  1.00 19.09 ? 12  GLY A O   1 
ATOM   89   N  N   . GLU A 1 13  ? 17.688  39.396  45.011  1.00 20.18 ? 13  GLU A N   1 
ATOM   90   C  CA  . GLU A 1 13  ? 19.097  39.187  44.610  1.00 23.17 ? 13  GLU A CA  1 
ATOM   91   C  C   . GLU A 1 13  ? 19.208  38.279  43.382  1.00 22.55 ? 13  GLU A C   1 
ATOM   92   O  O   . GLU A 1 13  ? 20.270  38.266  42.775  1.00 23.56 ? 13  GLU A O   1 
ATOM   93   C  CB  . GLU A 1 13  ? 19.858  38.634  45.828  1.00 27.35 ? 13  GLU A CB  1 
ATOM   94   C  CG  . GLU A 1 13  ? 20.238  39.730  46.825  1.00 35.19 ? 13  GLU A CG  1 
ATOM   95   C  CD  . GLU A 1 13  ? 20.818  41.022  46.244  1.00 46.49 ? 13  GLU A CD  1 
ATOM   96   O  OE1 . GLU A 1 13  ? 21.557  40.962  45.213  1.00 54.46 ? 13  GLU A OE1 1 
ATOM   97   O  OE2 . GLU A 1 13  ? 20.530  42.100  46.806  1.00 50.40 ? 13  GLU A OE2 1 
ATOM   98   N  N   . LEU A 1 14  ? 18.148  37.566  42.976  1.00 18.78 ? 14  LEU A N   1 
ATOM   99   C  CA  . LEU A 1 14  ? 18.197  36.729  41.753  1.00 17.83 ? 14  LEU A CA  1 
ATOM   100  C  C   . LEU A 1 14  ? 17.845  37.583  40.517  1.00 16.72 ? 14  LEU A C   1 
ATOM   101  O  O   . LEU A 1 14  ? 17.935  37.068  39.386  1.00 16.97 ? 14  LEU A O   1 
ATOM   102  C  CB  . LEU A 1 14  ? 17.266  35.525  41.921  1.00 20.00 ? 14  LEU A CB  1 
ATOM   103  C  CG  . LEU A 1 14  ? 17.707  34.479  42.962  1.00 22.32 ? 14  LEU A CG  1 
ATOM   104  C  CD1 . LEU A 1 14  ? 16.794  33.266  43.003  1.00 22.56 ? 14  LEU A CD1 1 
ATOM   105  C  CD2 . LEU A 1 14  ? 19.144  34.058  42.782  1.00 26.28 ? 14  LEU A CD2 1 
ATOM   106  N  N   . LYS A 1 15  ? 17.470  38.841  40.696  1.00 15.41 ? 15  LYS A N   1 
ATOM   107  C  CA  . LYS A 1 15  ? 17.190  39.774  39.581  1.00 15.07 ? 15  LYS A CA  1 
ATOM   108  C  C   . LYS A 1 15  ? 16.147  39.107  38.691  1.00 16.02 ? 15  LYS A C   1 
ATOM   109  O  O   . LYS A 1 15  ? 15.093  38.701  39.218  1.00 14.97 ? 15  LYS A O   1 
ATOM   110  C  CB  . LYS A 1 15  ? 18.493  40.185  38.909  1.00 18.58 ? 15  LYS A CB  1 
ATOM   111  C  CG  . LYS A 1 15  ? 19.509  40.748  39.907  1.00 21.89 ? 15  LYS A CG  1 
ATOM   112  C  CD  . LYS A 1 15  ? 20.802  41.235  39.278  1.00 27.74 ? 15  LYS A CD  1 
ATOM   113  C  CE  . LYS A 1 15  ? 21.776  41.678  40.357  1.00 32.15 ? 15  LYS A CE  1 
ATOM   114  N  NZ  . LYS A 1 15  ? 22.664  42.741  39.845  1.00 38.07 ? 15  LYS A NZ  1 
ATOM   115  N  N   . ASN A 1 16  ? 16.397  38.978  37.389  1.00 14.72 ? 16  ASN A N   1 
ATOM   116  C  CA  . ASN A 1 16  ? 15.354  38.429  36.471  1.00 13.60 ? 16  ASN A CA  1 
ATOM   117  C  C   . ASN A 1 16  ? 15.472  36.914  36.316  1.00 13.23 ? 16  ASN A C   1 
ATOM   118  O  O   . ASN A 1 16  ? 14.638  36.328  35.583  1.00 15.69 ? 16  ASN A O   1 
ATOM   119  C  CB  . ASN A 1 16  ? 15.419  39.060  35.067  1.00 13.13 ? 16  ASN A CB  1 
ATOM   120  C  CG  . ASN A 1 16  ? 15.143  40.536  35.102  1.00 13.91 ? 16  ASN A CG  1 
ATOM   121  O  OD1 . ASN A 1 16  ? 15.941  41.355  34.679  1.00 14.19 ? 16  ASN A OD1 1 
ATOM   122  N  ND2 . ASN A 1 16  ? 13.953  40.871  35.622  1.00 14.89 ? 16  ASN A ND2 1 
ATOM   123  N  N   . LEU A 1 17  ? 16.534  36.296  36.858  1.00 14.82 ? 17  LEU A N   1 
ATOM   124  C  CA  . LEU A 1 17  ? 16.859  34.899  36.474  1.00 15.01 ? 17  LEU A CA  1 
ATOM   125  C  C   . LEU A 1 17  ? 15.669  33.958  36.689  1.00 16.57 ? 17  LEU A C   1 
ATOM   126  O  O   . LEU A 1 17  ? 15.442  33.077  35.847  1.00 17.32 ? 17  LEU A O   1 
ATOM   127  C  CB  . LEU A 1 17  ? 18.063  34.413  37.279  1.00 18.34 ? 17  LEU A CB  1 
ATOM   128  C  CG  . LEU A 1 17  ? 18.552  33.013  36.942  1.00 20.99 ? 17  LEU A CG  1 
ATOM   129  C  CD1 . LEU A 1 17  ? 19.025  32.966  35.509  1.00 21.54 ? 17  LEU A CD1 1 
ATOM   130  C  CD2 . LEU A 1 17  ? 19.663  32.642  37.902  1.00 21.46 ? 17  LEU A CD2 1 
ATOM   131  N  N   . PRO A 1 18  ? 14.853  34.049  37.773  1.00 14.09 ? 18  PRO A N   1 
ATOM   132  C  CA  . PRO A 1 18  ? 13.751  33.104  37.924  1.00 15.11 ? 18  PRO A CA  1 
ATOM   133  C  C   . PRO A 1 18  ? 12.710  33.147  36.802  1.00 12.61 ? 18  PRO A C   1 
ATOM   134  O  O   . PRO A 1 18  ? 11.933  32.173  36.702  1.00 14.36 ? 18  PRO A O   1 
ATOM   135  C  CB  . PRO A 1 18  ? 13.121  33.491  39.265  1.00 16.09 ? 18  PRO A CB  1 
ATOM   136  C  CG  . PRO A 1 18  ? 14.289  34.020  40.031  1.00 15.15 ? 18  PRO A CG  1 
ATOM   137  C  CD  . PRO A 1 18  ? 15.034  34.838  39.004  1.00 14.07 ? 18  PRO A CD  1 
ATOM   138  N  N   . LEU A 1 19  ? 12.712  34.173  35.958  1.00 14.10 ? 19  LEU A N   1 
ATOM   139  C  CA  . LEU A 1 19  ? 11.797  34.195  34.790  1.00 15.24 ? 19  LEU A CA  1 
ATOM   140  C  C   . LEU A 1 19  ? 12.156  33.034  33.838  1.00 15.68 ? 19  LEU A C   1 
ATOM   141  O  O   . LEU A 1 19  ? 11.272  32.641  33.043  1.00 17.20 ? 19  LEU A O   1 
ATOM   142  C  CB  . LEU A 1 19  ? 11.835  35.533  34.107  1.00 14.84 ? 19  LEU A CB  1 
ATOM   143  C  CG  . LEU A 1 19  ? 11.314  36.725  34.931  1.00 14.28 ? 19  LEU A CG  1 
ATOM   144  C  CD1 . LEU A 1 19  ? 11.570  37.992  34.182  1.00 15.03 ? 19  LEU A CD1 1 
ATOM   145  C  CD2 . LEU A 1 19  ? 9.827   36.590  35.248  1.00 16.12 ? 19  LEU A CD2 1 
ATOM   146  N  N   . LEU A 1 20  ? 13.387  32.544  33.880  1.00 16.92 ? 20  LEU A N   1 
ATOM   147  C  CA  . LEU A 1 20  ? 13.769  31.448  32.966  1.00 18.54 ? 20  LEU A CA  1 
ATOM   148  C  C   . LEU A 1 20  ? 13.533  30.102  33.648  1.00 18.10 ? 20  LEU A C   1 
ATOM   149  O  O   . LEU A 1 20  ? 13.825  29.077  33.002  1.00 17.70 ? 20  LEU A O   1 
ATOM   150  C  CB  . LEU A 1 20  ? 15.243  31.621  32.556  1.00 20.35 ? 20  LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 20  ? 15.551  32.904  31.810  1.00 26.08 ? 20  LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 20  ? 17.055  33.032  31.592  1.00 31.15 ? 20  LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 20  ? 14.832  32.974  30.492  1.00 30.47 ? 20  LEU A CD2 1 
ATOM   154  N  N   . ASN A 1 21  ? 13.029  30.060  34.884  1.00 17.03 ? 21  ASN A N   1 
ATOM   155  C  CA  . ASN A 1 21  ? 12.713  28.807  35.594  1.00 17.81 ? 21  ASN A CA  1 
ATOM   156  C  C   . ASN A 1 21  ? 11.352  28.349  35.070  1.00 18.18 ? 21  ASN A C   1 
ATOM   157  O  O   . ASN A 1 21  ? 10.335  28.414  35.799  1.00 19.88 ? 21  ASN A O   1 
ATOM   158  C  CB  . ASN A 1 21  ? 12.722  28.949  37.119  1.00 21.27 ? 21  ASN A CB  1 
ATOM   159  C  CG  . ASN A 1 21  ? 12.497  27.623  37.812  1.00 29.14 ? 21  ASN A CG  1 
ATOM   160  O  OD1 . ASN A 1 21  ? 12.401  26.563  37.171  1.00 31.04 ? 21  ASN A OD1 1 
ATOM   161  N  ND2 . ASN A 1 21  ? 12.379  27.677  39.132  1.00 33.54 ? 21  ASN A ND2 1 
ATOM   162  N  N   . THR A 1 22  ? 11.351  27.876  33.820  1.00 15.95 ? 22  THR A N   1 
ATOM   163  C  CA  . THR A 1 22  ? 10.139  27.448  33.078  1.00 17.44 ? 22  THR A CA  1 
ATOM   164  C  C   . THR A 1 22  ? 10.601  26.453  32.017  1.00 18.26 ? 22  THR A C   1 
ATOM   165  O  O   . THR A 1 22  ? 11.760  26.563  31.599  1.00 18.85 ? 22  THR A O   1 
ATOM   166  C  CB  . THR A 1 22  ? 9.344   28.627  32.500  1.00 18.12 ? 22  THR A CB  1 
ATOM   167  O  OG1 . THR A 1 22  ? 8.343   28.145  31.593  1.00 18.88 ? 22  THR A OG1 1 
ATOM   168  C  CG2 . THR A 1 22  ? 10.194  29.649  31.798  1.00 17.43 ? 22  THR A CG2 1 
ATOM   169  N  N   . ASP A 1 23  ? 9.711   25.525  31.652  1.00 18.94 ? 23  ASP A N   1 
ATOM   170  C  CA  . ASP A 1 23  ? 9.893   24.594  30.519  1.00 21.60 ? 23  ASP A CA  1 
ATOM   171  C  C   . ASP A 1 23  ? 9.758   25.359  29.194  1.00 18.25 ? 23  ASP A C   1 
ATOM   172  O  O   . ASP A 1 23  ? 10.201  24.805  28.221  1.00 18.80 ? 23  ASP A O   1 
ATOM   173  C  CB  . ASP A 1 23  ? 8.786   23.517  30.535  1.00 23.74 ? 23  ASP A CB  1 
ATOM   174  C  CG  . ASP A 1 23  ? 8.807   22.635  31.761  1.00 35.36 ? 23  ASP A CG  1 
ATOM   175  O  OD1 . ASP A 1 23  ? 9.852   22.616  32.431  1.00 41.01 ? 23  ASP A OD1 1 
ATOM   176  O  OD2 . ASP A 1 23  ? 7.780   21.964  32.017  1.00 43.80 ? 23  ASP A OD2 1 
ATOM   177  N  N   . LYS A 1 24  ? 9.181   26.563  29.172  1.00 16.21 ? 24  LYS A N   1 
ATOM   178  C  CA  . LYS A 1 24  ? 8.894   27.337  27.928  1.00 13.72 ? 24  LYS A CA  1 
ATOM   179  C  C   . LYS A 1 24  ? 9.497   28.752  28.020  1.00 13.51 ? 24  LYS A C   1 
ATOM   180  O  O   . LYS A 1 24  ? 8.773   29.742  27.980  1.00 14.50 ? 24  LYS A O   1 
ATOM   181  C  CB  . LYS A 1 24  ? 7.395   27.365  27.665  1.00 15.71 ? 24  LYS A CB  1 
ATOM   182  C  CG  . LYS A 1 24  ? 6.834   25.984  27.342  1.00 16.06 ? 24  LYS A CG  1 
ATOM   183  C  CD  . LYS A 1 24  ? 5.335   26.023  27.194  1.00 17.68 ? 24  LYS A CD  1 
ATOM   184  C  CE  . LYS A 1 24  ? 4.730   24.656  26.973  1.00 19.80 ? 24  LYS A CE  1 
ATOM   185  N  NZ  . LYS A 1 24  ? 3.284   24.798  26.703  1.00 22.53 ? 24  LYS A NZ  1 
ATOM   186  N  N   . PRO A 1 25  ? 10.848  28.877  28.125  1.00 14.61 ? 25  PRO A N   1 
ATOM   187  C  CA  . PRO A 1 25  ? 11.466  30.195  28.293  1.00 14.30 ? 25  PRO A CA  1 
ATOM   188  C  C   . PRO A 1 25  ? 11.315  31.103  27.071  1.00 13.53 ? 25  PRO A C   1 
ATOM   189  O  O   . PRO A 1 25  ? 11.090  32.297  27.212  1.00 14.37 ? 25  PRO A O   1 
ATOM   190  C  CB  . PRO A 1 25  ? 12.928  29.881  28.599  1.00 13.66 ? 25  PRO A CB  1 
ATOM   191  C  CG  . PRO A 1 25  ? 13.149  28.564  27.904  1.00 14.85 ? 25  PRO A CG  1 
ATOM   192  C  CD  . PRO A 1 25  ? 11.854  27.794  28.122  1.00 14.93 ? 25  PRO A CD  1 
ATOM   193  N  N   . VAL A 1 26  ? 11.407  30.621  25.836  1.00 14.28 ? 26  VAL A N   1 
ATOM   194  C  CA  . VAL A 1 26  ? 11.263  31.546  24.687  1.00 13.45 ? 26  VAL A CA  1 
ATOM   195  C  C   . VAL A 1 26  ? 9.831   32.102  24.654  1.00 14.25 ? 26  VAL A C   1 
ATOM   196  O  O   . VAL A 1 26  ? 9.631   33.313  24.456  1.00 14.13 ? 26  VAL A O   1 
ATOM   197  C  CB  . VAL A 1 26  ? 11.629  30.802  23.384  1.00 16.14 ? 26  VAL A CB  1 
ATOM   198  C  CG1 . VAL A 1 26  ? 11.202  31.579  22.162  1.00 18.63 ? 26  VAL A CG1 1 
ATOM   199  C  CG2 . VAL A 1 26  ? 13.113  30.558  23.362  1.00 18.03 ? 26  VAL A CG2 1 
ATOM   200  N  N   . GLN A 1 27  ? 8.835   31.264  24.938  1.00 13.64 ? 27  GLN A N   1 
ATOM   201  C  CA  . GLN A 1 27  ? 7.433   31.724  24.937  1.00 13.13 ? 27  GLN A CA  1 
ATOM   202  C  C   . GLN A 1 27  ? 7.246   32.744  26.081  1.00 12.28 ? 27  GLN A C   1 
ATOM   203  O  O   . GLN A 1 27  ? 6.467   33.691  25.888  1.00 14.61 ? 27  GLN A O   1 
ATOM   204  C  CB  . GLN A 1 27  ? 6.456   30.557  24.967  1.00 14.38 ? 27  GLN A CB  1 
ATOM   205  C  CG  . GLN A 1 27  ? 6.474   29.743  23.665  1.00 14.89 ? 27  GLN A CG  1 
ATOM   206  C  CD  . GLN A 1 27  ? 5.970   28.342  23.867  1.00 14.73 ? 27  GLN A CD  1 
ATOM   207  O  OE1 . GLN A 1 27  ? 6.719   27.361  24.012  1.00 16.51 ? 27  GLN A OE1 1 
ATOM   208  N  NE2 . GLN A 1 27  ? 4.698   28.250  23.754  1.00 13.92 ? 27  GLN A NE2 1 
ATOM   209  N  N   . ALA A 1 28  ? 7.933   32.561  27.199  1.00 12.91 ? 28  ALA A N   1 
ATOM   210  C  CA  . ALA A 1 28  ? 7.867   33.565  28.293  1.00 13.22 ? 28  ALA A CA  1 
ATOM   211  C  C   . ALA A 1 28  ? 8.504   34.874  27.840  1.00 13.84 ? 28  ALA A C   1 
ATOM   212  O  O   . ALA A 1 28  ? 7.956   35.963  28.129  1.00 14.60 ? 28  ALA A O   1 
ATOM   213  C  CB  . ALA A 1 28  ? 8.524   33.041  29.508  1.00 13.61 ? 28  ALA A CB  1 
ATOM   214  N  N   . LEU A 1 29  ? 9.648   34.815  27.175  1.00 14.20 ? 29  LEU A N   1 
ATOM   215  C  CA  . LEU A 1 29  ? 10.321  36.032  26.682  1.00 13.70 ? 29  LEU A CA  1 
ATOM   216  C  C   . LEU A 1 29  ? 9.481   36.723  25.606  1.00 14.44 ? 29  LEU A C   1 
ATOM   217  O  O   . LEU A 1 29  ? 9.473   37.980  25.539  1.00 13.57 ? 29  LEU A O   1 
ATOM   218  C  CB  . LEU A 1 29  ? 11.706  35.644  26.190  1.00 13.91 ? 29  LEU A CB  1 
ATOM   219  C  CG  . LEU A 1 29  ? 12.678  35.246  27.288  1.00 14.45 ? 29  LEU A CG  1 
ATOM   220  C  CD1 . LEU A 1 29  ? 13.804  34.404  26.758  1.00 14.41 ? 29  LEU A CD1 1 
ATOM   221  C  CD2 . LEU A 1 29  ? 13.226  36.480  28.006  1.00 15.16 ? 29  LEU A CD2 1 
ATOM   222  N  N   . MET A 1 30  ? 8.770   35.954  24.771  1.00 14.59 ? 30  MET A N   1 
ATOM   223  C  CA  . MET A 1 30  ? 7.877   36.576  23.769  1.00 15.13 ? 30  MET A CA  1 
ATOM   224  C  C   . MET A 1 30  ? 6.780   37.398  24.478  1.00 15.27 ? 30  MET A C   1 
ATOM   225  O  O   . MET A 1 30  ? 6.492   38.520  24.046  1.00 15.37 ? 30  MET A O   1 
ATOM   226  C  CB  . MET A 1 30  ? 7.242   35.499  22.879  1.00 15.46 ? 30  MET A CB  1 
ATOM   227  C  CG  . MET A 1 30  ? 8.249   34.867  21.965  1.00 15.91 ? 30  MET A CG  1 
ATOM   228  S  SD  . MET A 1 30  ? 7.544   33.467  21.048  1.00 17.07 ? 30  MET A SD  1 
ATOM   229  C  CE  . MET A 1 30  ? 6.269   34.227  20.070  1.00 18.62 ? 30  MET A CE  1 
ATOM   230  N  N   . LYS A 1 31  ? 6.183   36.869  25.527  1.00 15.05 ? 31  LYS A N   1 
ATOM   231  C  CA  . LYS A 1 31  ? 5.126   37.622  26.256  1.00 16.09 ? 31  LYS A CA  1 
ATOM   232  C  C   . LYS A 1 31  ? 5.718   38.855  26.950  1.00 15.51 ? 31  LYS A C   1 
ATOM   233  O  O   . LYS A 1 31  ? 5.070   39.886  26.941  1.00 16.15 ? 31  LYS A O   1 
ATOM   234  C  CB  . LYS A 1 31  ? 4.422   36.683  27.229  1.00 18.77 ? 31  LYS A CB  1 
ATOM   235  C  CG  . LYS A 1 31  ? 3.452   35.739  26.537  1.00 28.66 ? 31  LYS A CG  1 
ATOM   236  C  CD  . LYS A 1 31  ? 2.904   34.664  27.451  1.00 36.06 ? 31  LYS A CD  1 
ATOM   237  C  CE  . LYS A 1 31  ? 2.108   33.618  26.693  1.00 43.54 ? 31  LYS A CE  1 
ATOM   238  N  NZ  . LYS A 1 31  ? 2.172   32.295  27.360  1.00 50.41 ? 31  LYS A NZ  1 
ATOM   239  N  N   . ILE A 1 32  ? 6.941   38.776  27.480  1.00 13.69 ? 32  ILE A N   1 
ATOM   240  C  CA  . ILE A 1 32  ? 7.623   39.958  28.038  1.00 14.22 ? 32  ILE A CA  1 
ATOM   241  C  C   . ILE A 1 32  ? 7.839   40.977  26.928  1.00 14.94 ? 32  ILE A C   1 
ATOM   242  O  O   . ILE A 1 32  ? 7.588   42.148  27.151  1.00 14.66 ? 32  ILE A O   1 
ATOM   243  C  CB  . ILE A 1 32  ? 8.950   39.556  28.704  1.00 15.20 ? 32  ILE A CB  1 
ATOM   244  C  CG1 . ILE A 1 32  ? 8.648   38.680  29.929  1.00 16.65 ? 32  ILE A CG1 1 
ATOM   245  C  CG2 . ILE A 1 32  ? 9.776   40.790  29.054  1.00 12.87 ? 32  ILE A CG2 1 
ATOM   246  C  CD1 . ILE A 1 32  ? 9.852   37.979  30.530  1.00 18.16 ? 32  ILE A CD1 1 
ATOM   247  N  N   . ALA A 1 33  ? 8.308   40.555  25.751  1.00 13.80 ? 33  ALA A N   1 
ATOM   248  C  CA  . ALA A 1 33  ? 8.507   41.479  24.623  1.00 15.37 ? 33  ALA A CA  1 
ATOM   249  C  C   . ALA A 1 33  ? 7.187   42.177  24.268  1.00 15.08 ? 33  ALA A C   1 
ATOM   250  O  O   . ALA A 1 33  ? 7.179   43.355  23.931  1.00 17.22 ? 33  ALA A O   1 
ATOM   251  C  CB  . ALA A 1 33  ? 9.066   40.712  23.442  1.00 15.01 ? 33  ALA A CB  1 
ATOM   252  N  N   . ASP A 1 34  ? 6.104   41.426  24.308  1.00 15.57 ? 34  ASP A N   1 
ATOM   253  C  CA  . ASP A 1 34  ? 4.756   41.940  23.950  1.00 17.62 ? 34  ASP A CA  1 
ATOM   254  C  C   . ASP A 1 34  ? 4.407   43.035  24.946  1.00 17.17 ? 34  ASP A C   1 
ATOM   255  O  O   . ASP A 1 34  ? 3.856   44.085  24.537  1.00 19.73 ? 34  ASP A O   1 
ATOM   256  C  CB  . ASP A 1 34  ? 3.694   40.842  23.905  1.00 20.19 ? 34  ASP A CB  1 
ATOM   257  C  CG  . ASP A 1 34  ? 3.688   40.072  22.588  1.00 23.32 ? 34  ASP A CG  1 
ATOM   258  O  OD1 . ASP A 1 34  ? 4.258   40.584  21.620  1.00 25.48 ? 34  ASP A OD1 1 
ATOM   259  O  OD2 . ASP A 1 34  ? 3.146   38.953  22.562  1.00 29.25 ? 34  ASP A OD2 1 
ATOM   260  N  N   . GLU A 1 35  ? 4.789   42.854  26.196  1.00 17.01 ? 35  GLU A N   1 
ATOM   261  C  CA  . GLU A 1 35  ? 4.462   43.875  27.208  1.00 18.95 ? 35  GLU A CA  1 
ATOM   262  C  C   . GLU A 1 35  ? 5.414   45.061  27.107  1.00 19.54 ? 35  GLU A C   1 
ATOM   263  O  O   . GLU A 1 35  ? 4.953   46.191  27.371  1.00 22.36 ? 35  GLU A O   1 
ATOM   264  C  CB  . GLU A 1 35  ? 4.550   43.258  28.600  1.00 21.37 ? 35  GLU A CB  1 
ATOM   265  C  CG  . GLU A 1 35  ? 3.507   42.208  28.925  1.00 25.92 ? 35  GLU A CG  1 
ATOM   266  C  CD  . GLU A 1 35  ? 3.611   41.666  30.342  1.00 32.32 ? 35  GLU A CD  1 
ATOM   267  O  OE1 . GLU A 1 35  ? 4.118   42.411  31.241  1.00 31.15 ? 35  GLU A OE1 1 
ATOM   268  O  OE2 . GLU A 1 35  ? 3.158   40.514  30.556  1.00 40.13 ? 35  GLU A OE2 1 
ATOM   269  N  N   . LEU A 1 36  ? 6.724   44.810  26.951  1.00 16.81 ? 36  LEU A N   1 
ATOM   270  C  CA  . LEU A 1 36  ? 7.753   45.869  27.110  1.00 18.60 ? 36  LEU A CA  1 
ATOM   271  C  C   . LEU A 1 36  ? 8.173   46.534  25.801  1.00 17.89 ? 36  LEU A C   1 
ATOM   272  O  O   . LEU A 1 36  ? 8.799   47.616  25.873  1.00 19.04 ? 36  LEU A O   1 
ATOM   273  C  CB  . LEU A 1 36  ? 8.962   45.293  27.842  1.00 16.76 ? 36  LEU A CB  1 
ATOM   274  C  CG  . LEU A 1 36  ? 8.689   44.813  29.256  1.00 16.65 ? 36  LEU A CG  1 
ATOM   275  C  CD1 . LEU A 1 36  ? 9.962   44.379  29.961  1.00 17.32 ? 36  LEU A CD1 1 
ATOM   276  C  CD2 . LEU A 1 36  ? 8.052   45.939  30.074  1.00 20.97 ? 36  LEU A CD2 1 
ATOM   277  N  N   . GLY A 1 37  ? 8.036   45.855  24.669  1.00 16.96 ? 37  GLY A N   1 
ATOM   278  C  CA  . GLY A 1 37  ? 8.354   46.436  23.360  1.00 17.72 ? 37  GLY A CA  1 
ATOM   279  C  C   . GLY A 1 37  ? 9.668   45.968  22.748  1.00 16.20 ? 37  GLY A C   1 
ATOM   280  O  O   . GLY A 1 37  ? 10.080  44.855  22.991  1.00 17.93 ? 37  GLY A O   1 
ATOM   281  N  N   . GLU A 1 38  ? 10.285  46.846  21.994  1.00 15.99 ? 38  GLU A N   1 
ATOM   282  C  CA  . GLU A 1 38  ? 11.281  46.379  20.987  1.00 17.46 ? 38  GLU A CA  1 
ATOM   283  C  C   . GLU A 1 38  ? 12.568  45.975  21.674  1.00 16.26 ? 38  GLU A C   1 
ATOM   284  O  O   . GLU A 1 38  ? 13.395  45.341  21.022  1.00 16.66 ? 38  GLU A O   1 
ATOM   285  C  CB  . GLU A 1 38  ? 11.597  47.420  19.923  1.00 19.07 ? 38  GLU A CB  1 
ATOM   286  C  CG  . GLU A 1 38  ? 12.150  48.701  20.485  1.00 20.07 ? 38  GLU A CG  1 
ATOM   287  C  CD  . GLU A 1 38  ? 12.349  49.767  19.423  1.00 24.68 ? 38  GLU A CD  1 
ATOM   288  O  OE1 . GLU A 1 38  ? 12.400  49.445  18.199  1.00 25.30 ? 38  GLU A OE1 1 
ATOM   289  O  OE2 . GLU A 1 38  ? 12.451  50.928  19.827  1.00 27.55 ? 38  GLU A OE2 1 
ATOM   290  N  N   . ILE A 1 39  ? 12.827  46.426  22.894  1.00 15.67 ? 39  ILE A N   1 
ATOM   291  C  CA  . ILE A 1 39  ? 14.072  46.098  23.626  1.00 16.39 ? 39  ILE A CA  1 
ATOM   292  C  C   . ILE A 1 39  ? 13.794  46.010  25.124  1.00 16.12 ? 39  ILE A C   1 
ATOM   293  O  O   . ILE A 1 39  ? 13.096  46.889  25.665  1.00 15.92 ? 39  ILE A O   1 
ATOM   294  C  CB  . ILE A 1 39  ? 15.196  47.082  23.273  1.00 16.06 ? 39  ILE A CB  1 
ATOM   295  C  CG1 . ILE A 1 39  ? 16.542  46.625  23.836  1.00 17.79 ? 39  ILE A CG1 1 
ATOM   296  C  CG2 . ILE A 1 39  ? 14.885  48.514  23.683  1.00 17.72 ? 39  ILE A CG2 1 
ATOM   297  C  CD1 . ILE A 1 39  ? 17.707  47.450  23.357  1.00 20.11 ? 39  ILE A CD1 1 
ATOM   298  N  N   . PHE A 1 40  ? 14.361  45.030  25.811  1.00 14.54 ? 40  PHE A N   1 
ATOM   299  C  CA  . PHE A 1 40  ? 14.352  44.987  27.282  1.00 14.73 ? 40  PHE A CA  1 
ATOM   300  C  C   . PHE A 1 40  ? 15.667  44.420  27.787  1.00 15.32 ? 40  PHE A C   1 
ATOM   301  O  O   . PHE A 1 40  ? 16.311  43.624  27.084  1.00 14.52 ? 40  PHE A O   1 
ATOM   302  C  CB  . PHE A 1 40  ? 13.107  44.338  27.841  1.00 15.13 ? 40  PHE A CB  1 
ATOM   303  C  CG  . PHE A 1 40  ? 12.960  42.884  27.520  1.00 13.98 ? 40  PHE A CG  1 
ATOM   304  C  CD1 . PHE A 1 40  ? 13.489  41.893  28.320  1.00 14.75 ? 40  PHE A CD1 1 
ATOM   305  C  CD2 . PHE A 1 40  ? 12.222  42.504  26.415  1.00 14.08 ? 40  PHE A CD2 1 
ATOM   306  C  CE1 . PHE A 1 40  ? 13.274  40.558  28.009  1.00 14.92 ? 40  PHE A CE1 1 
ATOM   307  C  CE2 . PHE A 1 40  ? 12.020  41.175  26.112  1.00 14.72 ? 40  PHE A CE2 1 
ATOM   308  C  CZ  . PHE A 1 40  ? 12.528  40.199  26.910  1.00 14.20 ? 40  PHE A CZ  1 
ATOM   309  N  N   . LYS A 1 41  ? 16.060  44.862  28.976  1.00 16.03 ? 41  LYS A N   1 
ATOM   310  C  CA  . LYS A 1 41  ? 17.232  44.349  29.684  1.00 16.14 ? 41  LYS A CA  1 
ATOM   311  C  C   . LYS A 1 41  ? 16.800  43.194  30.577  1.00 17.60 ? 41  LYS A C   1 
ATOM   312  O  O   . LYS A 1 41  ? 15.712  43.209  31.174  1.00 18.68 ? 41  LYS A O   1 
ATOM   313  C  CB  . LYS A 1 41  ? 17.894  45.487  30.446  1.00 21.09 ? 41  LYS A CB  1 
ATOM   314  C  CG  . LYS A 1 41  ? 19.056  45.103  31.325  1.00 26.82 ? 41  LYS A CG  1 
ATOM   315  C  CD  . LYS A 1 41  ? 19.554  46.254  32.238  1.00 35.40 ? 41  LYS A CD  1 
ATOM   316  C  CE  . LYS A 1 41  ? 19.020  47.634  31.914  1.00 40.46 ? 41  LYS A CE  1 
ATOM   317  N  NZ  . LYS A 1 41  ? 17.781  47.963  32.666  1.00 45.52 ? 41  LYS A NZ  1 
ATOM   318  N  N   . PHE A 1 42  ? 17.613  42.153  30.637  1.00 14.51 ? 42  PHE A N   1 
ATOM   319  C  CA  . PHE A 1 42  ? 17.373  40.974  31.471  1.00 13.87 ? 42  PHE A CA  1 
ATOM   320  C  C   . PHE A 1 42  ? 18.644  40.756  32.262  1.00 15.79 ? 42  PHE A C   1 
ATOM   321  O  O   . PHE A 1 42  ? 19.734  40.498  31.658  1.00 15.61 ? 42  PHE A O   1 
ATOM   322  C  CB  . PHE A 1 42  ? 17.017  39.797  30.569  1.00 14.49 ? 42  PHE A CB  1 
ATOM   323  C  CG  . PHE A 1 42  ? 16.591  38.562  31.307  1.00 13.71 ? 42  PHE A CG  1 
ATOM   324  C  CD1 . PHE A 1 42  ? 17.480  37.878  32.117  1.00 16.47 ? 42  PHE A CD1 1 
ATOM   325  C  CD2 . PHE A 1 42  ? 15.266  38.131  31.230  1.00 15.99 ? 42  PHE A CD2 1 
ATOM   326  C  CE1 . PHE A 1 42  ? 17.073  36.731  32.775  1.00 16.56 ? 42  PHE A CE1 1 
ATOM   327  C  CE2 . PHE A 1 42  ? 14.862  37.010  31.942  1.00 16.32 ? 42  PHE A CE2 1 
ATOM   328  C  CZ  . PHE A 1 42  ? 15.770  36.328  32.698  1.00 16.51 ? 42  PHE A CZ  1 
ATOM   329  N  N   . GLU A 1 43  ? 18.556  40.881  33.581  1.00 15.58 ? 43  GLU A N   1 
ATOM   330  C  CA  . GLU A 1 43  ? 19.741  40.840  34.478  1.00 16.38 ? 43  GLU A CA  1 
ATOM   331  C  C   . GLU A 1 43  ? 19.675  39.520  35.227  1.00 17.59 ? 43  GLU A C   1 
ATOM   332  O  O   . GLU A 1 43  ? 18.598  39.128  35.759  1.00 16.12 ? 43  GLU A O   1 
ATOM   333  C  CB  . GLU A 1 43  ? 19.742  42.020  35.455  1.00 19.82 ? 43  GLU A CB  1 
ATOM   334  C  CG  . GLU A 1 43  ? 20.109  43.297  34.742  1.00 25.52 ? 43  GLU A CG  1 
ATOM   335  C  CD  . GLU A 1 43  ? 20.396  44.514  35.601  1.00 33.42 ? 43  GLU A CD  1 
ATOM   336  O  OE1 . GLU A 1 43  ? 20.485  44.357  36.813  1.00 38.02 ? 43  GLU A OE1 1 
ATOM   337  O  OE2 . GLU A 1 43  ? 20.515  45.611  35.039  1.00 39.25 ? 43  GLU A OE2 1 
ATOM   338  N  N   . ALA A 1 44  ? 20.823  38.869  35.373  1.00 16.56 ? 44  ALA A N   1 
ATOM   339  C  CA  . ALA A 1 44  ? 20.990  37.691  36.235  1.00 18.20 ? 44  ALA A CA  1 
ATOM   340  C  C   . ALA A 1 44  ? 22.186  37.946  37.119  1.00 19.71 ? 44  ALA A C   1 
ATOM   341  O  O   . ALA A 1 44  ? 22.970  38.826  36.797  1.00 20.02 ? 44  ALA A O   1 
ATOM   342  C  CB  . ALA A 1 44  ? 21.195  36.466  35.372  1.00 20.04 ? 44  ALA A CB  1 
ATOM   343  N  N   . PRO A 1 45  ? 22.366  37.219  38.231  1.00 20.41 ? 45  PRO A N   1 
ATOM   344  C  CA  . PRO A 1 45  ? 23.574  37.430  39.025  1.00 22.61 ? 45  PRO A CA  1 
ATOM   345  C  C   . PRO A 1 45  ? 24.846  37.408  38.173  1.00 23.00 ? 45  PRO A C   1 
ATOM   346  O  O   . PRO A 1 45  ? 25.683  38.253  38.413  1.00 27.33 ? 45  PRO A O   1 
ATOM   347  C  CB  . PRO A 1 45  ? 23.458  36.278  40.021  1.00 24.78 ? 45  PRO A CB  1 
ATOM   348  C  CG  . PRO A 1 45  ? 21.960  36.179  40.286  1.00 23.05 ? 45  PRO A CG  1 
ATOM   349  C  CD  . PRO A 1 45  ? 21.391  36.328  38.891  1.00 22.10 ? 45  PRO A CD  1 
ATOM   350  N  N   . GLY A 1 46  ? 24.942  36.519  37.188  1.00 24.19 ? 46  GLY A N   1 
ATOM   351  C  CA  . GLY A 1 46  ? 26.201  36.321  36.419  1.00 28.19 ? 46  GLY A CA  1 
ATOM   352  C  C   . GLY A 1 46  ? 26.328  37.144  35.143  1.00 27.77 ? 46  GLY A C   1 
ATOM   353  O  O   . GLY A 1 46  ? 27.446  37.266  34.611  1.00 27.39 ? 46  GLY A O   1 
ATOM   354  N  N   . TRP A 1 47  ? 25.267  37.762  34.629  1.00 23.52 ? 47  TRP A N   1 
ATOM   355  C  CA  . TRP A 1 47  ? 25.273  38.212  33.210  1.00 18.48 ? 47  TRP A CA  1 
ATOM   356  C  C   . TRP A 1 47  ? 24.090  39.130  32.933  1.00 18.29 ? 47  TRP A C   1 
ATOM   357  O  O   . TRP A 1 47  ? 23.165  39.194  33.756  1.00 18.71 ? 47  TRP A O   1 
ATOM   358  C  CB  . TRP A 1 47  ? 25.239  37.050  32.245  1.00 20.98 ? 47  TRP A CB  1 
ATOM   359  C  CG  . TRP A 1 47  ? 24.167  36.055  32.513  1.00 21.41 ? 47  TRP A CG  1 
ATOM   360  C  CD1 . TRP A 1 47  ? 24.310  34.880  33.191  1.00 20.84 ? 47  TRP A CD1 1 
ATOM   361  C  CD2 . TRP A 1 47  ? 22.799  36.085  32.052  1.00 19.15 ? 47  TRP A CD2 1 
ATOM   362  N  NE1 . TRP A 1 47  ? 23.141  34.190  33.208  1.00 19.43 ? 47  TRP A NE1 1 
ATOM   363  C  CE2 . TRP A 1 47  ? 22.207  34.870  32.470  1.00 19.87 ? 47  TRP A CE2 1 
ATOM   364  C  CE3 . TRP A 1 47  ? 22.051  36.967  31.283  1.00 20.91 ? 47  TRP A CE3 1 
ATOM   365  C  CZ2 . TRP A 1 47  ? 20.857  34.606  32.257  1.00 19.66 ? 47  TRP A CZ2 1 
ATOM   366  C  CZ3 . TRP A 1 47  ? 20.737  36.667  31.010  1.00 20.24 ? 47  TRP A CZ3 1 
ATOM   367  C  CH2 . TRP A 1 47  ? 20.154  35.498  31.492  1.00 18.65 ? 47  TRP A CH2 1 
ATOM   368  N  N   . VAL A 1 48  ? 24.175  39.900  31.858  1.00 17.75 ? 48  VAL A N   1 
ATOM   369  C  CA  . VAL A 1 48  ? 23.089  40.790  31.370  1.00 16.98 ? 48  VAL A CA  1 
ATOM   370  C  C   . VAL A 1 48  ? 22.864  40.509  29.894  1.00 18.14 ? 48  VAL A C   1 
ATOM   371  O  O   . VAL A 1 48  ? 23.881  40.334  29.139  1.00 18.23 ? 48  VAL A O   1 
ATOM   372  C  CB  . VAL A 1 48  ? 23.349  42.277  31.632  1.00 18.42 ? 48  VAL A CB  1 
ATOM   373  C  CG1 . VAL A 1 48  ? 22.187  43.124  31.128  1.00 20.54 ? 48  VAL A CG1 1 
ATOM   374  C  CG2 . VAL A 1 48  ? 23.621  42.516  33.109  1.00 20.14 ? 48  VAL A CG2 1 
ATOM   375  N  N   . LEU A 1 49  ? 21.616  40.395  29.475  1.00 15.96 ? 49  LEU A N   1 
ATOM   376  C  CA  . LEU A 1 49  ? 21.238  40.313  28.043  1.00 16.35 ? 49  LEU A CA  1 
ATOM   377  C  C   . LEU A 1 49  ? 20.293  41.443  27.718  1.00 17.01 ? 49  LEU A C   1 
ATOM   378  O  O   . LEU A 1 49  ? 19.531  41.851  28.628  1.00 19.98 ? 49  LEU A O   1 
ATOM   379  C  CB  . LEU A 1 49  ? 20.516  39.011  27.744  1.00 21.19 ? 49  LEU A CB  1 
ATOM   380  C  CG  . LEU A 1 49  ? 21.328  37.834  27.279  1.00 21.19 ? 49  LEU A CG  1 
ATOM   381  C  CD1 . LEU A 1 49  ? 20.400  36.672  27.019  1.00 19.13 ? 49  LEU A CD1 1 
ATOM   382  C  CD2 . LEU A 1 49  ? 22.148  38.122  26.024  1.00 20.32 ? 49  LEU A CD2 1 
ATOM   383  N  N   . ARG A 1 50  ? 20.378  41.994  26.521  1.00 15.67 ? 50  ARG A N   1 
ATOM   384  C  CA  . ARG A 1 50  ? 19.324  42.876  25.985  1.00 15.80 ? 50  ARG A CA  1 
ATOM   385  C  C   . ARG A 1 50  ? 18.602  42.104  24.901  1.00 15.07 ? 50  ARG A C   1 
ATOM   386  O  O   . ARG A 1 50  ? 19.240  41.723  23.891  1.00 15.14 ? 50  ARG A O   1 
ATOM   387  C  CB  . ARG A 1 50  ? 19.922  44.193  25.513  1.00 17.23 ? 50  ARG A CB  1 
ATOM   388  C  CG  . ARG A 1 50  ? 20.639  44.940  26.630  1.00 19.53 ? 50  ARG A CG  1 
ATOM   389  C  CD  . ARG A 1 50  ? 21.981  45.425  26.137  1.00 24.51 ? 50  ARG A CD  1 
ATOM   390  N  NE  . ARG A 1 50  ? 22.795  45.824  27.277  1.00 25.15 ? 50  ARG A NE  1 
ATOM   391  C  CZ  . ARG A 1 50  ? 23.675  45.064  27.880  1.00 25.08 ? 50  ARG A CZ  1 
ATOM   392  N  NH1 . ARG A 1 50  ? 23.864  43.801  27.506  1.00 18.30 ? 50  ARG A NH1 1 
ATOM   393  N  NH2 . ARG A 1 50  ? 24.312  45.570  28.927  1.00 24.24 ? 50  ARG A NH2 1 
ATOM   394  N  N   . TYR A 1 51  ? 17.305  41.911  25.066  1.00 12.70 ? 51  TYR A N   1 
ATOM   395  C  CA  . TYR A 1 51  ? 16.463  41.161  24.136  1.00 12.56 ? 51  TYR A CA  1 
ATOM   396  C  C   . TYR A 1 51  ? 15.836  42.108  23.125  1.00 14.65 ? 51  TYR A C   1 
ATOM   397  O  O   . TYR A 1 51  ? 15.134  43.063  23.512  1.00 14.61 ? 51  TYR A O   1 
ATOM   398  C  CB  . TYR A 1 51  ? 15.384  40.384  24.881  1.00 13.33 ? 51  TYR A CB  1 
ATOM   399  C  CG  . TYR A 1 51  ? 15.878  39.152  25.570  1.00 12.50 ? 51  TYR A CG  1 
ATOM   400  C  CD1 . TYR A 1 51  ? 16.398  39.199  26.848  1.00 14.08 ? 51  TYR A CD1 1 
ATOM   401  C  CD2 . TYR A 1 51  ? 15.843  37.931  24.924  1.00 13.40 ? 51  TYR A CD2 1 
ATOM   402  C  CE1 . TYR A 1 51  ? 16.800  38.057  27.516  1.00 14.43 ? 51  TYR A CE1 1 
ATOM   403  C  CE2 . TYR A 1 51  ? 16.281  36.780  25.561  1.00 13.00 ? 51  TYR A CE2 1 
ATOM   404  C  CZ  . TYR A 1 51  ? 16.786  36.841  26.851  1.00 14.29 ? 51  TYR A CZ  1 
ATOM   405  O  OH  . TYR A 1 51  ? 17.164  35.703  27.536  1.00 14.95 ? 51  TYR A OH  1 
ATOM   406  N  N   . LEU A 1 52  ? 16.061  41.838  21.828  1.00 13.40 ? 52  LEU A N   1 
ATOM   407  C  CA  . LEU A 1 52  ? 15.588  42.677  20.698  1.00 14.80 ? 52  LEU A CA  1 
ATOM   408  C  C   . LEU A 1 52  ? 14.426  42.002  19.985  1.00 14.95 ? 52  LEU A C   1 
ATOM   409  O  O   . LEU A 1 52  ? 14.543  40.829  19.604  1.00 13.62 ? 52  LEU A O   1 
ATOM   410  C  CB  . LEU A 1 52  ? 16.716  42.916  19.693  1.00 15.41 ? 52  LEU A CB  1 
ATOM   411  C  CG  . LEU A 1 52  ? 17.992  43.538  20.235  1.00 20.17 ? 52  LEU A CG  1 
ATOM   412  C  CD1 . LEU A 1 52  ? 18.986  43.855  19.118  1.00 19.10 ? 52  LEU A CD1 1 
ATOM   413  C  CD2 . LEU A 1 52  ? 17.725  44.777  21.042  1.00 23.28 ? 52  LEU A CD2 1 
ATOM   414  N  N   . SER A 1 53  ? 13.420  42.792  19.627  1.00 14.18 ? 53  SER A N   1 
ATOM   415  C  CA  . SER A 1 53  ? 12.213  42.264  18.974  1.00 13.62 ? 53  SER A CA  1 
ATOM   416  C  C   . SER A 1 53  ? 11.829  43.015  17.682  1.00 15.11 ? 53  SER A C   1 
ATOM   417  O  O   . SER A 1 53  ? 10.960  42.497  16.977  1.00 16.51 ? 53  SER A O   1 
ATOM   418  C  CB  . SER A 1 53  ? 11.067  42.242  19.943  1.00 16.19 ? 53  SER A CB  1 
ATOM   419  O  OG  . SER A 1 53  ? 11.346  41.325  20.998  1.00 18.82 ? 53  SER A OG  1 
ATOM   420  N  N   . SER A 1 54  ? 12.316  44.243  17.479  1.00 13.83 ? 54  SER A N   1 
ATOM   421  C  CA  . SER A 1 54  ? 11.908  45.042  16.286  1.00 15.21 ? 54  SER A CA  1 
ATOM   422  C  C   . SER A 1 54  ? 12.890  44.878  15.137  1.00 14.80 ? 54  SER A C   1 
ATOM   423  O  O   . SER A 1 54  ? 14.112  44.797  15.362  1.00 14.03 ? 54  SER A O   1 
ATOM   424  C  CB  . SER A 1 54  ? 11.723  46.526  16.608  1.00 15.51 ? 54  SER A CB  1 
ATOM   425  O  OG  . SER A 1 54  ? 12.965  47.130  16.854  1.00 16.62 ? 54  SER A OG  1 
ATOM   426  N  N   . GLN A 1 55  ? 12.388  44.931  13.894  1.00 14.44 ? 55  GLN A N   1 
ATOM   427  C  CA  . GLN A 1 55  ? 13.244  44.999  12.700  1.00 16.04 ? 55  GLN A CA  1 
ATOM   428  C  C   . GLN A 1 55  ? 14.141  46.219  12.782  1.00 15.41 ? 55  GLN A C   1 
ATOM   429  O  O   . GLN A 1 55  ? 15.295  46.130  12.387  1.00 16.63 ? 55  GLN A O   1 
ATOM   430  C  CB  . GLN A 1 55  ? 12.410  44.934  11.420  1.00 16.84 ? 55  GLN A CB  1 
ATOM   431  C  CG  . GLN A 1 55  ? 13.235  44.882  10.146  1.00 16.58 ? 55  GLN A CG  1 
ATOM   432  C  CD  . GLN A 1 55  ? 13.607  46.225  9.576   1.00 19.63 ? 55  GLN A CD  1 
ATOM   433  O  OE1 . GLN A 1 55  ? 13.203  47.268  10.081  1.00 21.09 ? 55  GLN A OE1 1 
ATOM   434  N  NE2 . GLN A 1 55  ? 14.408  46.200  8.520   1.00 22.26 ? 55  GLN A NE2 1 
ATOM   435  N  N   . ARG A 1 56  ? 13.626  47.335  13.326  1.00 15.93 ? 56  ARG A N   1 
ATOM   436  C  CA  . ARG A 1 56  ? 14.462  48.573  13.344  1.00 18.39 ? 56  ARG A CA  1 
ATOM   437  C  C   . ARG A 1 56  ? 15.794  48.290  14.046  1.00 19.11 ? 56  ARG A C   1 
ATOM   438  O  O   . ARG A 1 56  ? 16.851  48.760  13.585  1.00 20.91 ? 56  ARG A O   1 
ATOM   439  C  CB  . ARG A 1 56  ? 13.675  49.671  14.072  1.00 21.56 ? 56  ARG A CB  1 
ATOM   440  C  CG  . ARG A 1 56  ? 14.443  50.956  14.329  1.00 25.36 ? 56  ARG A CG  1 
ATOM   441  C  CD  . ARG A 1 56  ? 13.537  51.959  15.047  1.00 26.49 ? 56  ARG A CD  1 
ATOM   442  N  NE  . ARG A 1 56  ? 13.621  51.884  16.498  1.00 29.25 ? 56  ARG A NE  1 
ATOM   443  C  CZ  . ARG A 1 56  ? 14.477  52.569  17.246  1.00 25.92 ? 56  ARG A CZ  1 
ATOM   444  N  NH1 . ARG A 1 56  ? 15.368  53.377  16.681  1.00 29.34 ? 56  ARG A NH1 1 
ATOM   445  N  NH2 . ARG A 1 56  ? 14.466  52.428  18.560  1.00 30.31 ? 56  ARG A NH2 1 
ATOM   446  N  N   . LEU A 1 57  ? 15.748  47.635  15.211  1.00 15.22 ? 57  LEU A N   1 
ATOM   447  C  CA  . LEU A 1 57  ? 16.950  47.437  16.048  1.00 15.30 ? 57  LEU A CA  1 
ATOM   448  C  C   . LEU A 1 57  ? 17.685  46.179  15.570  1.00 15.04 ? 57  LEU A C   1 
ATOM   449  O  O   . LEU A 1 57  ? 18.920  46.128  15.614  1.00 15.49 ? 57  LEU A O   1 
ATOM   450  C  CB  . LEU A 1 57  ? 16.585  47.303  17.529  1.00 15.95 ? 57  LEU A CB  1 
ATOM   451  C  CG  . LEU A 1 57  ? 15.929  48.530  18.157  1.00 16.98 ? 57  LEU A CG  1 
ATOM   452  C  CD1 . LEU A 1 57  ? 15.591  48.247  19.624  1.00 16.97 ? 57  LEU A CD1 1 
ATOM   453  C  CD2 . LEU A 1 57  ? 16.848  49.724  18.051  1.00 18.17 ? 57  LEU A CD2 1 
ATOM   454  N  N   . ILE A 1 58  ? 16.937  45.171  15.123  1.00 14.30 ? 58  ILE A N   1 
ATOM   455  C  CA  . ILE A 1 58  ? 17.610  43.921  14.712  1.00 14.93 ? 58  ILE A CA  1 
ATOM   456  C  C   . ILE A 1 58  ? 18.416  44.156  13.437  1.00 16.54 ? 58  ILE A C   1 
ATOM   457  O  O   . ILE A 1 58  ? 19.527  43.598  13.336  1.00 16.09 ? 58  ILE A O   1 
ATOM   458  C  CB  . ILE A 1 58  ? 16.581  42.785  14.597  1.00 14.13 ? 58  ILE A CB  1 
ATOM   459  C  CG1 . ILE A 1 58  ? 16.130  42.380  16.001  1.00 13.46 ? 58  ILE A CG1 1 
ATOM   460  C  CG2 . ILE A 1 58  ? 17.146  41.571  13.871  1.00 14.92 ? 58  ILE A CG2 1 
ATOM   461  C  CD1 . ILE A 1 58  ? 14.857  41.618  16.073  1.00 13.90 ? 58  ILE A CD1 1 
ATOM   462  N  N   . LYS A 1 59  ? 17.985  45.045  12.553  1.00 16.22 ? 59  LYS A N   1 
ATOM   463  C  CA  . LYS A 1 59  ? 18.744  45.376  11.324  1.00 17.28 ? 59  LYS A CA  1 
ATOM   464  C  C   . LYS A 1 59  ? 20.109  45.943  11.734  1.00 17.49 ? 59  LYS A C   1 
ATOM   465  O  O   . LYS A 1 59  ? 21.092  45.582  11.074  1.00 19.59 ? 59  LYS A O   1 
ATOM   466  C  CB  . LYS A 1 59  ? 17.937  46.279  10.389  1.00 19.72 ? 59  LYS A CB  1 
ATOM   467  C  CG  . LYS A 1 59  ? 18.059  47.764  10.670  1.00 27.87 ? 59  LYS A CG  1 
ATOM   468  C  CD  . LYS A 1 59  ? 17.109  48.646  9.883   1.00 31.51 ? 59  LYS A CD  1 
ATOM   469  C  CE  . LYS A 1 59  ? 17.103  50.044  10.471  1.00 35.58 ? 59  LYS A CE  1 
ATOM   470  N  NZ  . LYS A 1 59  ? 16.287  50.983  9.656   1.00 39.79 ? 59  LYS A NZ  1 
ATOM   471  N  N   . GLU A 1 60  ? 20.184  46.797  12.760  1.00 17.02 ? 60  GLU A N   1 
ATOM   472  C  CA  . GLU A 1 60  ? 21.457  47.346  13.268  1.00 17.97 ? 60  GLU A CA  1 
ATOM   473  C  C   . GLU A 1 60  ? 22.288  46.218  13.898  1.00 17.94 ? 60  GLU A C   1 
ATOM   474  O  O   . GLU A 1 60  ? 23.539  46.174  13.712  1.00 17.29 ? 60  GLU A O   1 
ATOM   475  C  CB  . GLU A 1 60  ? 21.264  48.412  14.343  1.00 19.27 ? 60  GLU A CB  1 
ATOM   476  C  CG  . GLU A 1 60  ? 20.631  49.675  13.780  1.00 22.74 ? 60  GLU A CG  1 
ATOM   477  C  CD  . GLU A 1 60  ? 20.767  50.886  14.679  1.00 23.08 ? 60  GLU A CD  1 
ATOM   478  O  OE1 . GLU A 1 60  ? 21.704  50.958  15.505  1.00 23.59 ? 60  GLU A OE1 1 
ATOM   479  O  OE2 . GLU A 1 60  ? 19.921  51.813  14.476  1.00 29.39 ? 60  GLU A OE2 1 
ATOM   480  N  N   . ALA A 1 61  ? 21.642  45.331  14.662  1.00 15.64 ? 61  ALA A N   1 
ATOM   481  C  CA  . ALA A 1 61  ? 22.366  44.254  15.370  1.00 16.06 ? 61  ALA A CA  1 
ATOM   482  C  C   . ALA A 1 61  ? 23.018  43.330  14.343  1.00 15.40 ? 61  ALA A C   1 
ATOM   483  O  O   . ALA A 1 61  ? 24.000  42.661  14.674  1.00 15.97 ? 61  ALA A O   1 
ATOM   484  C  CB  . ALA A 1 61  ? 21.470  43.480  16.283  1.00 17.83 ? 61  ALA A CB  1 
ATOM   485  N  N   . CYS A 1 62  ? 22.442  43.278  13.151  1.00 15.41 ? 62  CYS A N   1 
ATOM   486  C  CA  . CYS A 1 62  ? 22.884  42.380  12.053  1.00 17.08 ? 62  CYS A CA  1 
ATOM   487  C  C   . CYS A 1 62  ? 23.997  43.036  11.218  1.00 16.30 ? 62  CYS A C   1 
ATOM   488  O  O   . CYS A 1 62  ? 24.481  42.415  10.274  1.00 17.54 ? 62  CYS A O   1 
ATOM   489  C  CB  . CYS A 1 62  ? 21.701  42.018  11.186  1.00 16.95 ? 62  CYS A CB  1 
ATOM   490  S  SG  . CYS A 1 62  ? 20.618  40.794  11.966  1.00 21.79 ? 62  CYS A SG  1 
ATOM   491  N  N   . ASP A 1 63  ? 24.485  44.204  11.652  1.00 15.08 ? 63  ASP A N   1 
ATOM   492  C  CA  . ASP A 1 63  ? 25.606  44.874  10.971  1.00 16.21 ? 63  ASP A CA  1 
ATOM   493  C  C   . ASP A 1 63  ? 26.878  44.242  11.501  1.00 15.08 ? 63  ASP A C   1 
ATOM   494  O  O   . ASP A 1 63  ? 27.249  44.521  12.653  1.00 15.15 ? 63  ASP A O   1 
ATOM   495  C  CB  . ASP A 1 63  ? 25.539  46.379  11.233  1.00 17.13 ? 63  ASP A CB  1 
ATOM   496  C  CG  . ASP A 1 63  ? 26.688  47.169  10.622  1.00 20.44 ? 63  ASP A CG  1 
ATOM   497  O  OD1 . ASP A 1 63  ? 27.706  46.571  10.235  1.00 19.47 ? 63  ASP A OD1 1 
ATOM   498  O  OD2 . ASP A 1 63  ? 26.608  48.423  10.657  1.00 22.33 ? 63  ASP A OD2 1 
ATOM   499  N  N   . GLU A 1 64  ? 27.534  43.416  10.698  1.00 16.17 ? 64  GLU A N   1 
ATOM   500  C  CA  . GLU A 1 64  ? 28.714  42.621  11.129  1.00 16.19 ? 64  GLU A CA  1 
ATOM   501  C  C   . GLU A 1 64  ? 29.926  43.516  11.414  1.00 16.42 ? 64  GLU A C   1 
ATOM   502  O  O   . GLU A 1 64  ? 30.885  43.061  12.036  1.00 19.02 ? 64  GLU A O   1 
ATOM   503  C  CB  . GLU A 1 64  ? 29.013  41.574  10.069  1.00 17.58 ? 64  GLU A CB  1 
ATOM   504  C  CG  . GLU A 1 64  ? 27.920  40.541  9.963   1.00 20.33 ? 64  GLU A CG  1 
ATOM   505  C  CD  . GLU A 1 64  ? 28.177  39.594  8.804   1.00 21.04 ? 64  GLU A CD  1 
ATOM   506  O  OE1 . GLU A 1 64  ? 28.081  40.057  7.675   1.00 29.16 ? 64  GLU A OE1 1 
ATOM   507  O  OE2 . GLU A 1 64  ? 28.451  38.432  9.029   1.00 18.94 ? 64  GLU A OE2 1 
ATOM   508  N  N   . SER A 1 65  ? 29.907  44.780  10.992  1.00 17.57 ? 65  SER A N   1 
ATOM   509  C  CA  . SER A 1 65  ? 31.004  45.705  11.354  1.00 17.94 ? 65  SER A CA  1 
ATOM   510  C  C   . SER A 1 65  ? 30.863  46.184  12.806  1.00 18.12 ? 65  SER A C   1 
ATOM   511  O  O   . SER A 1 65  ? 31.863  46.645  13.370  1.00 21.24 ? 65  SER A O   1 
ATOM   512  C  CB  . SER A 1 65  ? 31.029  46.895  10.404  1.00 20.14 ? 65  SER A CB  1 
ATOM   513  O  OG  . SER A 1 65  ? 29.995  47.819  10.695  1.00 22.16 ? 65  SER A OG  1 
ATOM   514  N  N   . ARG A 1 66  ? 29.689  46.009  13.427  1.00 17.17 ? 66  ARG A N   1 
ATOM   515  C  CA  . ARG A 1 66  ? 29.393  46.544  14.771  1.00 17.10 ? 66  ARG A CA  1 
ATOM   516  C  C   . ARG A 1 66  ? 29.173  45.406  15.776  1.00 15.04 ? 66  ARG A C   1 
ATOM   517  O  O   . ARG A 1 66  ? 29.401  45.593  16.947  1.00 16.43 ? 66  ARG A O   1 
ATOM   518  C  CB  . ARG A 1 66  ? 28.137  47.408  14.712  1.00 19.67 ? 66  ARG A CB  1 
ATOM   519  C  CG  . ARG A 1 66  ? 28.299  48.658  13.836  1.00 20.71 ? 66  ARG A CG  1 
ATOM   520  C  CD  . ARG A 1 66  ? 26.993  49.420  13.647  1.00 21.83 ? 66  ARG A CD  1 
ATOM   521  N  NE  . ARG A 1 66  ? 26.605  49.997  14.920  1.00 21.97 ? 66  ARG A NE  1 
ATOM   522  C  CZ  . ARG A 1 66  ? 25.393  50.396  15.254  1.00 18.96 ? 66  ARG A CZ  1 
ATOM   523  N  NH1 . ARG A 1 66  ? 24.370  50.271  14.439  1.00 20.78 ? 66  ARG A NH1 1 
ATOM   524  N  NH2 . ARG A 1 66  ? 25.208  50.861  16.465  1.00 22.37 ? 66  ARG A NH2 1 
ATOM   525  N  N   . PHE A 1 67  ? 28.692  44.255  15.316  1.00 16.03 ? 67  PHE A N   1 
ATOM   526  C  CA  . PHE A 1 67  ? 28.249  43.161  16.206  1.00 14.82 ? 67  PHE A CA  1 
ATOM   527  C  C   . PHE A 1 67  ? 28.676  41.826  15.603  1.00 13.51 ? 67  PHE A C   1 
ATOM   528  O  O   . PHE A 1 67  ? 28.623  41.656  14.392  1.00 14.96 ? 67  PHE A O   1 
ATOM   529  C  CB  . PHE A 1 67  ? 26.727  43.117  16.351  1.00 15.78 ? 67  PHE A CB  1 
ATOM   530  C  CG  . PHE A 1 67  ? 26.162  44.392  16.927  1.00 15.81 ? 67  PHE A CG  1 
ATOM   531  C  CD1 . PHE A 1 67  ? 26.151  44.564  18.290  1.00 17.01 ? 67  PHE A CD1 1 
ATOM   532  C  CD2 . PHE A 1 67  ? 25.714  45.387  16.091  1.00 16.18 ? 67  PHE A CD2 1 
ATOM   533  C  CE1 . PHE A 1 67  ? 25.709  45.770  18.842  1.00 16.85 ? 67  PHE A CE1 1 
ATOM   534  C  CE2 . PHE A 1 67  ? 25.233  46.585  16.627  1.00 17.32 ? 67  PHE A CE2 1 
ATOM   535  C  CZ  . PHE A 1 67  ? 25.216  46.735  18.002  1.00 16.74 ? 67  PHE A CZ  1 
ATOM   536  N  N   . ASP A 1 68  ? 29.119  40.929  16.459  1.00 11.92 ? 68  ASP A N   1 
ATOM   537  C  CA  . ASP A 1 68  ? 29.524  39.550  16.070  1.00 12.25 ? 68  ASP A CA  1 
ATOM   538  C  C   . ASP A 1 68  ? 28.702  38.525  16.849  1.00 12.78 ? 68  ASP A C   1 
ATOM   539  O  O   . ASP A 1 68  ? 28.089  38.864  17.843  1.00 13.50 ? 68  ASP A O   1 
ATOM   540  C  CB  . ASP A 1 68  ? 31.023  39.369  16.282  1.00 12.93 ? 68  ASP A CB  1 
ATOM   541  C  CG  . ASP A 1 68  ? 31.655  38.048  15.879  1.00 14.20 ? 68  ASP A CG  1 
ATOM   542  O  OD1 . ASP A 1 68  ? 31.100  37.352  14.936  1.00 13.97 ? 68  ASP A OD1 1 
ATOM   543  O  OD2 . ASP A 1 68  ? 32.695  37.698  16.536  1.00 15.47 ? 68  ASP A OD2 1 
ATOM   544  N  N   . LYS A 1 69  ? 28.673  37.299  16.369  1.00 11.35 ? 69  LYS A N   1 
ATOM   545  C  CA  . LYS A 1 69  ? 27.968  36.205  17.090  1.00 11.13 ? 69  LYS A CA  1 
ATOM   546  C  C   . LYS A 1 69  ? 28.536  36.036  18.493  1.00 10.45 ? 69  LYS A C   1 
ATOM   547  O  O   . LYS A 1 69  ? 29.777  35.946  18.696  1.00 11.77 ? 69  LYS A O   1 
ATOM   548  C  CB  . LYS A 1 69  ? 28.101  34.866  16.351  1.00 11.00 ? 69  LYS A CB  1 
ATOM   549  C  CG  . LYS A 1 69  ? 27.727  33.657  17.154  1.00 11.53 ? 69  LYS A CG  1 
ATOM   550  C  CD  . LYS A 1 69  ? 27.344  32.487  16.297  1.00 11.23 ? 69  LYS A CD  1 
ATOM   551  C  CE  . LYS A 1 69  ? 27.202  31.275  17.199  1.00 11.61 ? 69  LYS A CE  1 
ATOM   552  N  NZ  . LYS A 1 69  ? 26.352  30.200  16.601  1.00 13.15 ? 69  LYS A NZ  1 
ATOM   553  N  N   . ASN A 1 70  ? 27.615  35.944  19.452  1.00 10.71 ? 70  ASN A N   1 
ATOM   554  C  CA  . ASN A 1 70  ? 27.940  35.613  20.840  1.00 11.23 ? 70  ASN A CA  1 
ATOM   555  C  C   . ASN A 1 70  ? 27.499  34.185  21.156  1.00 12.42 ? 70  ASN A C   1 
ATOM   556  O  O   . ASN A 1 70  ? 26.517  33.726  20.563  1.00 12.65 ? 70  ASN A O   1 
ATOM   557  C  CB  . ASN A 1 70  ? 27.168  36.587  21.730  1.00 12.32 ? 70  ASN A CB  1 
ATOM   558  C  CG  . ASN A 1 70  ? 27.508  36.492  23.203  1.00 12.99 ? 70  ASN A CG  1 
ATOM   559  O  OD1 . ASN A 1 70  ? 28.658  36.415  23.579  1.00 15.61 ? 70  ASN A OD1 1 
ATOM   560  N  ND2 . ASN A 1 70  ? 26.482  36.410  24.019  1.00 15.00 ? 70  ASN A ND2 1 
ATOM   561  N  N   . LEU A 1 71  ? 28.197  33.519  22.059  1.00 12.98 ? 71  LEU A N   1 
ATOM   562  C  CA  . LEU A 1 71  ? 27.699  32.265  22.655  1.00 13.36 ? 71  LEU A CA  1 
ATOM   563  C  C   . LEU A 1 71  ? 26.917  32.649  23.915  1.00 15.40 ? 71  LEU A C   1 
ATOM   564  O  O   . LEU A 1 71  ? 27.525  33.142  24.853  1.00 16.16 ? 71  LEU A O   1 
ATOM   565  C  CB  . LEU A 1 71  ? 28.856  31.307  22.929  1.00 13.54 ? 71  LEU A CB  1 
ATOM   566  C  CG  . LEU A 1 71  ? 29.800  30.971  21.780  1.00 15.88 ? 71  LEU A CG  1 
ATOM   567  C  CD1 . LEU A 1 71  ? 30.835  29.919  22.216  1.00 17.72 ? 71  LEU A CD1 1 
ATOM   568  C  CD2 . LEU A 1 71  ? 29.049  30.520  20.538  1.00 16.82 ? 71  LEU A CD2 1 
ATOM   569  N  N   . SER A 1 72  ? 25.611  32.389  23.919  1.00 15.40 ? 72  SER A N   1 
ATOM   570  C  CA  . SER A 1 72  ? 24.779  32.484  25.155  1.00 18.21 ? 72  SER A CA  1 
ATOM   571  C  C   . SER A 1 72  ? 25.288  31.492  26.209  1.00 17.86 ? 72  SER A C   1 
ATOM   572  O  O   . SER A 1 72  ? 26.054  30.581  25.898  1.00 16.93 ? 72  SER A O   1 
ATOM   573  C  CB  . SER A 1 72  ? 23.346  32.275  24.864  1.00 18.02 ? 72  SER A CB  1 
ATOM   574  O  OG  . SER A 1 72  ? 23.119  30.906  24.556  1.00 21.93 ? 72  SER A OG  1 
ATOM   575  N  N   . GLN A 1 73  ? 24.789  31.613  27.443  1.00 18.54 ? 73  GLN A N   1 
ATOM   576  C  CA  . GLN A 1 73  ? 25.137  30.630  28.489  1.00 20.45 ? 73  GLN A CA  1 
ATOM   577  C  C   . GLN A 1 73  ? 24.784  29.214  27.991  1.00 19.02 ? 73  GLN A C   1 
ATOM   578  O  O   . GLN A 1 73  ? 25.554  28.299  28.229  1.00 19.77 ? 73  GLN A O   1 
ATOM   579  C  CB  . GLN A 1 73  ? 24.394  30.946  29.780  1.00 22.31 ? 73  GLN A CB  1 
ATOM   580  C  CG  . GLN A 1 73  ? 24.749  32.313  30.343  1.00 24.39 ? 73  GLN A CG  1 
ATOM   581  C  CD  . GLN A 1 73  ? 26.186  32.389  30.794  1.00 27.40 ? 73  GLN A CD  1 
ATOM   582  O  OE1 . GLN A 1 73  ? 26.968  33.217  30.334  1.00 37.46 ? 73  GLN A OE1 1 
ATOM   583  N  NE2 . GLN A 1 73  ? 26.553  31.491  31.689  1.00 28.52 ? 73  GLN A NE2 1 
ATOM   584  N  N   . VAL A 1 74  ? 23.658  29.051  27.309  1.00 19.09 ? 74  VAL A N   1 
ATOM   585  C  CA  . VAL A 1 74  ? 23.252  27.707  26.823  1.00 18.70 ? 74  VAL A CA  1 
ATOM   586  C  C   . VAL A 1 74  ? 24.294  27.205  25.795  1.00 16.83 ? 74  VAL A C   1 
ATOM   587  O  O   . VAL A 1 74  ? 24.726  26.071  25.912  1.00 18.35 ? 74  VAL A O   1 
ATOM   588  C  CB  . VAL A 1 74  ? 21.841  27.705  26.235  1.00 21.01 ? 74  VAL A CB  1 
ATOM   589  C  CG1 . VAL A 1 74  ? 21.595  26.423  25.479  1.00 23.43 ? 74  VAL A CG1 1 
ATOM   590  C  CG2 . VAL A 1 74  ? 20.780  27.906  27.304  1.00 21.15 ? 74  VAL A CG2 1 
ATOM   591  N  N   . LEU A 1 75  ? 24.697  28.023  24.815  1.00 14.78 ? 75  LEU A N   1 
ATOM   592  C  CA  . LEU A 1 75  ? 25.690  27.561  23.811  1.00 14.64 ? 75  LEU A CA  1 
ATOM   593  C  C   . LEU A 1 75  ? 27.046  27.289  24.466  1.00 15.18 ? 75  LEU A C   1 
ATOM   594  O  O   . LEU A 1 75  ? 27.704  26.354  24.057  1.00 15.10 ? 75  LEU A O   1 
ATOM   595  C  CB  . LEU A 1 75  ? 25.846  28.543  22.659  1.00 15.45 ? 75  LEU A CB  1 
ATOM   596  C  CG  . LEU A 1 75  ? 24.692  28.572  21.660  1.00 18.53 ? 75  LEU A CG  1 
ATOM   597  C  CD1 . LEU A 1 75  ? 25.122  29.308  20.397  1.00 18.69 ? 75  LEU A CD1 1 
ATOM   598  C  CD2 . LEU A 1 75  ? 24.111  27.192  21.414  1.00 22.51 ? 75  LEU A CD2 1 
ATOM   599  N  N   . LYS A 1 76  ? 27.427  28.039  25.509  1.00 15.17 ? 76  LYS A N   1 
ATOM   600  C  CA  . LYS A 1 76  ? 28.693  27.739  26.223  1.00 16.14 ? 76  LYS A CA  1 
ATOM   601  C  C   . LYS A 1 76  ? 28.619  26.357  26.866  1.00 15.98 ? 76  LYS A C   1 
ATOM   602  O  O   . LYS A 1 76  ? 29.640  25.698  26.919  1.00 17.66 ? 76  LYS A O   1 
ATOM   603  C  CB  . LYS A 1 76  ? 28.986  28.831  27.246  1.00 18.13 ? 76  LYS A CB  1 
ATOM   604  C  CG  . LYS A 1 76  ? 29.370  30.162  26.629  1.00 18.42 ? 76  LYS A CG  1 
ATOM   605  C  CD  . LYS A 1 76  ? 29.421  31.290  27.632  1.00 20.44 ? 76  LYS A CD  1 
ATOM   606  C  CE  . LYS A 1 76  ? 30.077  32.470  26.962  1.00 23.57 ? 76  LYS A CE  1 
ATOM   607  N  NZ  . LYS A 1 76  ? 30.375  33.552  27.924  1.00 30.03 ? 76  LYS A NZ  1 
ATOM   608  N  N   . PHE A 1 77  ? 27.452  25.947  27.343  1.00 16.41 ? 77  PHE A N   1 
ATOM   609  C  CA  . PHE A 1 77  ? 27.280  24.589  27.911  1.00 17.46 ? 77  PHE A CA  1 
ATOM   610  C  C   . PHE A 1 77  ? 27.138  23.552  26.796  1.00 17.06 ? 77  PHE A C   1 
ATOM   611  O  O   . PHE A 1 77  ? 27.639  22.433  26.980  1.00 19.18 ? 77  PHE A O   1 
ATOM   612  C  CB  . PHE A 1 77  ? 26.120  24.551  28.914  1.00 18.43 ? 77  PHE A CB  1 
ATOM   613  C  CG  . PHE A 1 77  ? 26.411  25.280  30.208  1.00 19.43 ? 77  PHE A CG  1 
ATOM   614  C  CD1 . PHE A 1 77  ? 27.610  25.069  30.876  1.00 24.00 ? 77  PHE A CD1 1 
ATOM   615  C  CD2 . PHE A 1 77  ? 25.535  26.234  30.681  1.00 21.12 ? 77  PHE A CD2 1 
ATOM   616  C  CE1 . PHE A 1 77  ? 27.874  25.758  32.059  1.00 24.34 ? 77  PHE A CE1 1 
ATOM   617  C  CE2 . PHE A 1 77  ? 25.799  26.924  31.862  1.00 22.05 ? 77  PHE A CE2 1 
ATOM   618  C  CZ  . PHE A 1 77  ? 26.969  26.685  32.541  1.00 24.44 ? 77  PHE A CZ  1 
ATOM   619  N  N   . VAL A 1 78  ? 26.474  23.854  25.683  1.00 15.29 ? 78  VAL A N   1 
ATOM   620  C  CA  . VAL A 1 78  ? 26.443  22.922  24.515  1.00 16.11 ? 78  VAL A CA  1 
ATOM   621  C  C   . VAL A 1 78  ? 27.878  22.677  24.003  1.00 14.30 ? 78  VAL A C   1 
ATOM   622  O  O   . VAL A 1 78  ? 28.216  21.544  23.611  1.00 15.33 ? 78  VAL A O   1 
ATOM   623  C  CB  . VAL A 1 78  ? 25.486  23.407  23.414  1.00 15.24 ? 78  VAL A CB  1 
ATOM   624  C  CG1 . VAL A 1 78  ? 25.581  22.564  22.153  1.00 16.27 ? 78  VAL A CG1 1 
ATOM   625  C  CG2 . VAL A 1 78  ? 24.055  23.407  23.937  1.00 17.42 ? 78  VAL A CG2 1 
ATOM   626  N  N   . ARG A 1 79  ? 28.738  23.686  24.073  1.00 15.64 ? 79  ARG A N   1 
ATOM   627  C  CA  . ARG A 1 79  ? 30.169  23.547  23.717  1.00 16.47 ? 79  ARG A CA  1 
ATOM   628  C  C   . ARG A 1 79  ? 30.897  22.447  24.512  1.00 16.60 ? 79  ARG A C   1 
ATOM   629  O  O   . ARG A 1 79  ? 31.893  21.921  24.024  1.00 16.92 ? 79  ARG A O   1 
ATOM   630  C  CB  . ARG A 1 79  ? 30.837  24.904  23.886  1.00 17.53 ? 79  ARG A CB  1 
ATOM   631  C  CG  . ARG A 1 79  ? 32.311  24.885  23.548  1.00 16.05 ? 79  ARG A CG  1 
ATOM   632  C  CD  . ARG A 1 79  ? 32.797  26.247  23.222  1.00 19.06 ? 79  ARG A CD  1 
ATOM   633  N  NE  . ARG A 1 79  ? 34.238  26.125  22.952  1.00 20.59 ? 79  ARG A NE  1 
ATOM   634  C  CZ  . ARG A 1 79  ? 34.920  26.816  22.059  1.00 18.58 ? 79  ARG A CZ  1 
ATOM   635  N  NH1 . ARG A 1 79  ? 34.303  27.608  21.202  1.00 15.88 ? 79  ARG A NH1 1 
ATOM   636  N  NH2 . ARG A 1 79  ? 36.223  26.672  21.988  1.00 20.05 ? 79  ARG A NH2 1 
ATOM   637  N  N   . ASP A 1 80  ? 30.396  22.026  25.668  1.00 17.06 ? 80  ASP A N   1 
ATOM   638  C  CA  . ASP A 1 80  ? 31.058  20.919  26.405  1.00 19.51 ? 80  ASP A CA  1 
ATOM   639  C  C   . ASP A 1 80  ? 30.989  19.636  25.570  1.00 19.95 ? 80  ASP A C   1 
ATOM   640  O  O   . ASP A 1 80  ? 31.821  18.728  25.803  1.00 21.12 ? 80  ASP A O   1 
ATOM   641  C  CB  . ASP A 1 80  ? 30.435  20.772  27.809  1.00 21.99 ? 80  ASP A CB  1 
ATOM   642  C  CG  . ASP A 1 80  ? 30.800  21.918  28.752  1.00 27.74 ? 80  ASP A CG  1 
ATOM   643  O  OD1 . ASP A 1 80  ? 31.853  22.561  28.518  1.00 30.49 ? 80  ASP A OD1 1 
ATOM   644  O  OD2 . ASP A 1 80  ? 30.021  22.168  29.700  1.00 40.84 ? 80  ASP A OD2 1 
ATOM   645  N  N   . PHE A 1 81  ? 30.048  19.495  24.618  1.00 16.58 ? 81  PHE A N   1 
ATOM   646  C  CA  . PHE A 1 81  ? 30.028  18.304  23.706  1.00 16.76 ? 81  PHE A CA  1 
ATOM   647  C  C   . PHE A 1 81  ? 30.154  18.677  22.226  1.00 19.18 ? 81  PHE A C   1 
ATOM   648  O  O   . PHE A 1 81  ? 30.609  17.830  21.438  1.00 19.11 ? 81  PHE A O   1 
ATOM   649  C  CB  . PHE A 1 81  ? 28.852  17.367  24.036  1.00 17.13 ? 81  PHE A CB  1 
ATOM   650  C  CG  . PHE A 1 81  ? 27.494  18.023  24.146  1.00 15.92 ? 81  PHE A CG  1 
ATOM   651  C  CD1 . PHE A 1 81  ? 27.089  18.617  25.310  1.00 16.63 ? 81  PHE A CD1 1 
ATOM   652  C  CD2 . PHE A 1 81  ? 26.641  18.062  23.049  1.00 16.49 ? 81  PHE A CD2 1 
ATOM   653  C  CE1 . PHE A 1 81  ? 25.819  19.144  25.442  1.00 17.85 ? 81  PHE A CE1 1 
ATOM   654  C  CE2 . PHE A 1 81  ? 25.374  18.627  23.168  1.00 17.14 ? 81  PHE A CE2 1 
ATOM   655  C  CZ  . PHE A 1 81  ? 24.978  19.209  24.355  1.00 16.19 ? 81  PHE A CZ  1 
ATOM   656  N  N   . ALA A 1 82  ? 29.740  19.879  21.807  1.00 15.93 ? 82  ALA A N   1 
ATOM   657  C  CA  . ALA A 1 82  ? 29.868  20.290  20.404  1.00 17.38 ? 82  ALA A CA  1 
ATOM   658  C  C   . ALA A 1 82  ? 31.200  21.005  20.142  1.00 15.85 ? 82  ALA A C   1 
ATOM   659  O  O   . ALA A 1 82  ? 31.477  21.369  18.984  1.00 14.14 ? 82  ALA A O   1 
ATOM   660  C  CB  . ALA A 1 82  ? 28.692  21.137  19.998  1.00 15.30 ? 82  ALA A CB  1 
ATOM   661  N  N   . GLY A 1 83  ? 31.980  21.267  21.173  1.00 15.54 ? 83  GLY A N   1 
ATOM   662  C  CA  . GLY A 1 83  ? 33.337  21.832  21.091  1.00 14.94 ? 83  GLY A CA  1 
ATOM   663  C  C   . GLY A 1 83  ? 33.431  23.054  20.227  1.00 14.70 ? 83  GLY A C   1 
ATOM   664  O  O   . GLY A 1 83  ? 32.571  23.927  20.371  1.00 14.97 ? 83  GLY A O   1 
ATOM   665  N  N   . ASP A 1 84  ? 34.469  23.125  19.379  1.00 13.74 ? 84  ASP A N   1 
ATOM   666  C  CA  . ASP A 1 84  ? 34.680  24.239  18.445  1.00 14.03 ? 84  ASP A CA  1 
ATOM   667  C  C   . ASP A 1 84  ? 34.171  23.825  17.061  1.00 14.18 ? 84  ASP A C   1 
ATOM   668  O  O   . ASP A 1 84  ? 34.756  24.262  16.061  1.00 16.23 ? 84  ASP A O   1 
ATOM   669  C  CB  . ASP A 1 84  ? 36.121  24.760  18.483  1.00 15.18 ? 84  ASP A CB  1 
ATOM   670  C  CG  . ASP A 1 84  ? 37.186  23.748  18.084  1.00 14.75 ? 84  ASP A CG  1 
ATOM   671  O  OD1 . ASP A 1 84  ? 36.897  22.558  17.987  1.00 16.95 ? 84  ASP A OD1 1 
ATOM   672  O  OD2 . ASP A 1 84  ? 38.342  24.202  17.937  1.00 18.46 ? 84  ASP A OD2 1 
ATOM   673  N  N   . GLY A 1 85  ? 33.081  23.053  17.030  1.00 13.43 ? 85  GLY A N   1 
ATOM   674  C  CA  . GLY A 1 85  ? 32.277  22.882  15.809  1.00 13.19 ? 85  GLY A CA  1 
ATOM   675  C  C   . GLY A 1 85  ? 31.706  24.202  15.354  1.00 12.74 ? 85  GLY A C   1 
ATOM   676  O  O   . GLY A 1 85  ? 31.875  25.249  16.009  1.00 13.55 ? 85  GLY A O   1 
ATOM   677  N  N   . LEU A 1 86  ? 31.146  24.245  14.179  1.00 11.08 ? 86  LEU A N   1 
ATOM   678  C  CA  . LEU A 1 86  ? 30.771  25.540  13.537  1.00 11.54 ? 86  LEU A CA  1 
ATOM   679  C  C   . LEU A 1 86  ? 29.779  26.306  14.410  1.00 11.68 ? 86  LEU A C   1 
ATOM   680  O  O   . LEU A 1 86  ? 29.793  27.507  14.359  1.00 12.80 ? 86  LEU A O   1 
ATOM   681  C  CB  . LEU A 1 86  ? 30.137  25.295  12.160  1.00 12.13 ? 86  LEU A CB  1 
ATOM   682  C  CG  . LEU A 1 86  ? 31.101  24.961  11.014  1.00 12.72 ? 86  LEU A CG  1 
ATOM   683  C  CD1 . LEU A 1 86  ? 30.309  24.485  9.795   1.00 14.36 ? 86  LEU A CD1 1 
ATOM   684  C  CD2 . LEU A 1 86  ? 31.970  26.175  10.672  1.00 12.65 ? 86  LEU A CD2 1 
ATOM   685  N  N   . PHE A 1 87  ? 28.851  25.604  15.060  1.00 10.77 ? 87  PHE A N   1 
ATOM   686  C  CA  . PHE A 1 87  ? 27.765  26.278  15.793  1.00 11.68 ? 87  PHE A CA  1 
ATOM   687  C  C   . PHE A 1 87  ? 28.235  26.864  17.125  1.00 11.19 ? 87  PHE A C   1 
ATOM   688  O  O   . PHE A 1 87  ? 27.608  27.859  17.555  1.00 12.54 ? 87  PHE A O   1 
ATOM   689  C  CB  . PHE A 1 87  ? 26.649  25.260  15.987  1.00 11.97 ? 87  PHE A CB  1 
ATOM   690  C  CG  . PHE A 1 87  ? 25.420  25.693  16.738  1.00 13.90 ? 87  PHE A CG  1 
ATOM   691  C  CD1 . PHE A 1 87  ? 24.668  26.783  16.369  1.00 14.02 ? 87  PHE A CD1 1 
ATOM   692  C  CD2 . PHE A 1 87  ? 25.060  24.966  17.858  1.00 15.42 ? 87  PHE A CD2 1 
ATOM   693  C  CE1 . PHE A 1 87  ? 23.528  27.124  17.102  1.00 15.07 ? 87  PHE A CE1 1 
ATOM   694  C  CE2 . PHE A 1 87  ? 23.927  25.290  18.587  1.00 16.39 ? 87  PHE A CE2 1 
ATOM   695  C  CZ  . PHE A 1 87  ? 23.134  26.333  18.175  1.00 16.13 ? 87  PHE A CZ  1 
ATOM   696  N  N   . THR A 1 88  ? 29.221  26.272  17.795  1.00 11.71 ? 88  THR A N   1 
ATOM   697  C  CA  . THR A 1 88  ? 29.648  26.684  19.165  1.00 11.45 ? 88  THR A CA  1 
ATOM   698  C  C   . THR A 1 88  ? 31.057  27.272  19.173  1.00 11.96 ? 88  THR A C   1 
ATOM   699  O  O   . THR A 1 88  ? 31.642  27.424  20.228  1.00 13.22 ? 88  THR A O   1 
ATOM   700  C  CB  . THR A 1 88  ? 29.490  25.555  20.188  1.00 12.16 ? 88  THR A CB  1 
ATOM   701  O  OG1 . THR A 1 88  ? 30.046  24.364  19.631  1.00 13.64 ? 88  THR A OG1 1 
ATOM   702  C  CG2 . THR A 1 88  ? 28.032  25.266  20.504  1.00 14.25 ? 88  THR A CG2 1 
ATOM   703  N  N   . SER A 1 89  ? 31.564  27.688  18.036  1.00 12.09 ? 89  SER A N   1 
ATOM   704  C  CA  . SER A 1 89  ? 32.863  28.391  17.924  1.00 11.65 ? 89  SER A CA  1 
ATOM   705  C  C   . SER A 1 89  ? 32.606  29.897  17.836  1.00 13.35 ? 89  SER A C   1 
ATOM   706  O  O   . SER A 1 89  ? 31.549  30.376  17.333  1.00 11.67 ? 89  SER A O   1 
ATOM   707  C  CB  . SER A 1 89  ? 33.693  27.826  16.762  1.00 15.37 ? 89  SER A CB  1 
ATOM   708  O  OG  . SER A 1 89  ? 32.942  27.914  15.599  1.00 17.84 ? 89  SER A OG  1 
ATOM   709  N  N   . TRP A 1 90  ? 33.557  30.659  18.334  1.00 12.00 ? 90  TRP A N   1 
ATOM   710  C  CA  . TRP A 1 90  ? 33.616  32.118  18.109  1.00 12.83 ? 90  TRP A CA  1 
ATOM   711  C  C   . TRP A 1 90  ? 34.182  32.393  16.725  1.00 12.36 ? 90  TRP A C   1 
ATOM   712  O  O   . TRP A 1 90  ? 35.033  31.638  16.294  1.00 12.29 ? 90  TRP A O   1 
ATOM   713  C  CB  . TRP A 1 90  ? 34.493  32.773  19.191  1.00 12.31 ? 90  TRP A CB  1 
ATOM   714  C  CG  . TRP A 1 90  ? 34.046  32.494  20.602  1.00 13.15 ? 90  TRP A CG  1 
ATOM   715  C  CD1 . TRP A 1 90  ? 34.433  31.489  21.450  1.00 14.42 ? 90  TRP A CD1 1 
ATOM   716  C  CD2 . TRP A 1 90  ? 33.097  33.273  21.330  1.00 12.75 ? 90  TRP A CD2 1 
ATOM   717  N  NE1 . TRP A 1 90  ? 33.779  31.605  22.656  1.00 14.93 ? 90  TRP A NE1 1 
ATOM   718  C  CE2 . TRP A 1 90  ? 32.977  32.707  22.630  1.00 13.51 ? 90  TRP A CE2 1 
ATOM   719  C  CE3 . TRP A 1 90  ? 32.392  34.454  21.024  1.00 12.62 ? 90  TRP A CE3 1 
ATOM   720  C  CZ2 . TRP A 1 90  ? 32.164  33.281  23.609  1.00 13.69 ? 90  TRP A CZ2 1 
ATOM   721  C  CZ3 . TRP A 1 90  ? 31.596  35.013  22.009  1.00 13.61 ? 90  TRP A CZ3 1 
ATOM   722  C  CH2 . TRP A 1 90  ? 31.476  34.417  23.255  1.00 14.83 ? 90  TRP A CH2 1 
ATOM   723  N  N   . THR A 1 91  ? 33.743  33.463  16.076  1.00 11.50 ? 91  THR A N   1 
ATOM   724  C  CA  . THR A 1 91  ? 34.132  33.771  14.687  1.00 11.97 ? 91  THR A CA  1 
ATOM   725  C  C   . THR A 1 91  ? 35.659  33.914  14.596  1.00 13.30 ? 91  THR A C   1 
ATOM   726  O  O   . THR A 1 91  ? 36.233  33.627  13.543  1.00 14.42 ? 91  THR A O   1 
ATOM   727  C  CB  . THR A 1 91  ? 33.443  35.054  14.272  1.00 12.94 ? 91  THR A CB  1 
ATOM   728  O  OG1 . THR A 1 91  ? 32.043  34.887  14.401  1.00 12.33 ? 91  THR A OG1 1 
ATOM   729  C  CG2 . THR A 1 91  ? 33.737  35.424  12.840  1.00 14.87 ? 91  THR A CG2 1 
ATOM   730  N  N   . HIS A 1 92  ? 36.274  34.426  15.654  1.00 12.23 ? 92  HIS A N   1 
ATOM   731  C  CA  . HIS A 1 92  ? 37.734  34.673  15.715  1.00 12.47 ? 92  HIS A CA  1 
ATOM   732  C  C   . HIS A 1 92  ? 38.565  33.417  15.952  1.00 12.07 ? 92  HIS A C   1 
ATOM   733  O  O   . HIS A 1 92  ? 39.820  33.511  15.920  1.00 13.38 ? 92  HIS A O   1 
ATOM   734  C  CB  . HIS A 1 92  ? 38.007  35.771  16.720  1.00 12.31 ? 92  HIS A CB  1 
ATOM   735  C  CG  . HIS A 1 92  ? 37.424  35.556  18.069  1.00 12.73 ? 92  HIS A CG  1 
ATOM   736  N  ND1 . HIS A 1 92  ? 37.975  34.737  18.984  1.00 12.79 ? 92  HIS A ND1 1 
ATOM   737  C  CD2 . HIS A 1 92  ? 36.342  36.137  18.650  1.00 11.74 ? 92  HIS A CD2 1 
ATOM   738  C  CE1 . HIS A 1 92  ? 37.214  34.783  20.088  1.00 12.16 ? 92  HIS A CE1 1 
ATOM   739  N  NE2 . HIS A 1 92  ? 36.204  35.606  19.901  1.00 13.39 ? 92  HIS A NE2 1 
ATOM   740  N  N   . GLU A 1 93  ? 37.979  32.298  16.339  1.00 11.80 ? 93  GLU A N   1 
ATOM   741  C  CA  . GLU A 1 93  ? 38.746  31.052  16.514  1.00 12.88 ? 93  GLU A CA  1 
ATOM   742  C  C   . GLU A 1 93  ? 39.153  30.531  15.153  1.00 14.09 ? 93  GLU A C   1 
ATOM   743  O  O   . GLU A 1 93  ? 38.331  30.456  14.264  1.00 13.76 ? 93  GLU A O   1 
ATOM   744  C  CB  . GLU A 1 93  ? 37.928  30.008  17.254  1.00 13.12 ? 93  GLU A CB  1 
ATOM   745  C  CG  . GLU A 1 93  ? 37.802  30.286  18.756  1.00 14.47 ? 93  GLU A CG  1 
ATOM   746  C  CD  . GLU A 1 93  ? 37.010  29.206  19.448  1.00 14.95 ? 93  GLU A CD  1 
ATOM   747  O  OE1 . GLU A 1 93  ? 35.756  29.192  19.356  1.00 14.59 ? 93  GLU A OE1 1 
ATOM   748  O  OE2 . GLU A 1 93  ? 37.633  28.324  20.084  1.00 17.24 ? 93  GLU A OE2 1 
ATOM   749  N  N   . LYS A 1 94  ? 40.419  30.160  14.999  1.00 14.51 ? 94  LYS A N   1 
ATOM   750  C  CA  . LYS A 1 94  ? 40.911  29.585  13.739  1.00 15.50 ? 94  LYS A CA  1 
ATOM   751  C  C   . LYS A 1 94  ? 40.003  28.479  13.237  1.00 14.12 ? 94  LYS A C   1 
ATOM   752  O  O   . LYS A 1 94  ? 39.770  28.428  11.983  1.00 14.36 ? 94  LYS A O   1 
ATOM   753  C  CB  . LYS A 1 94  ? 42.316  29.022  13.950  1.00 15.54 ? 94  LYS A CB  1 
ATOM   754  C  CG  . LYS A 1 94  ? 42.988  28.489  12.693  1.00 19.37 ? 94  LYS A CG  1 
ATOM   755  C  CD  . LYS A 1 94  ? 44.314  27.894  13.062  1.00 23.04 ? 94  LYS A CD  1 
ATOM   756  C  CE  . LYS A 1 94  ? 45.053  27.318  11.897  1.00 26.17 ? 94  LYS A CE  1 
ATOM   757  N  NZ  . LYS A 1 94  ? 46.399  26.923  12.383  1.00 27.70 ? 94  LYS A NZ  1 
ATOM   758  N  N   . ASN A 1 95  ? 39.530  27.591  14.092  1.00 14.05 ? 95  ASN A N   1 
ATOM   759  C  CA  . ASN A 1 95  ? 38.757  26.426  13.600  1.00 14.40 ? 95  ASN A CA  1 
ATOM   760  C  C   . ASN A 1 95  ? 37.402  26.843  13.023  1.00 15.35 ? 95  ASN A C   1 
ATOM   761  O  O   . ASN A 1 95  ? 36.826  26.054  12.293  1.00 14.57 ? 95  ASN A O   1 
ATOM   762  C  CB  . ASN A 1 95  ? 38.569  25.340  14.646  1.00 16.13 ? 95  ASN A CB  1 
ATOM   763  C  CG  . ASN A 1 95  ? 39.744  24.393  14.732  1.00 21.72 ? 95  ASN A CG  1 
ATOM   764  O  OD1 . ASN A 1 95  ? 40.509  24.306  13.781  1.00 29.20 ? 95  ASN A OD1 1 
ATOM   765  N  ND2 . ASN A 1 95  ? 39.897  23.722  15.850  1.00 20.10 ? 95  ASN A ND2 1 
ATOM   766  N  N   . TRP A 1 96  ? 36.883  28.030  13.332  1.00 13.54 ? 96  TRP A N   1 
ATOM   767  C  CA  . TRP A 1 96  ? 35.604  28.404  12.697  1.00 11.69 ? 96  TRP A CA  1 
ATOM   768  C  C   . TRP A 1 96  ? 35.775  28.655  11.215  1.00 11.73 ? 96  TRP A C   1 
ATOM   769  O  O   . TRP A 1 96  ? 35.128  28.012  10.423  1.00 12.46 ? 96  TRP A O   1 
ATOM   770  C  CB  . TRP A 1 96  ? 34.941  29.633  13.354  1.00 11.90 ? 96  TRP A CB  1 
ATOM   771  C  CG  . TRP A 1 96  ? 33.699  29.965  12.600  1.00 11.86 ? 96  TRP A CG  1 
ATOM   772  C  CD1 . TRP A 1 96  ? 32.515  29.283  12.637  1.00 12.80 ? 96  TRP A CD1 1 
ATOM   773  C  CD2 . TRP A 1 96  ? 33.565  30.913  11.533  1.00 12.21 ? 96  TRP A CD2 1 
ATOM   774  N  NE1 . TRP A 1 96  ? 31.678  29.748  11.686  1.00 12.37 ? 96  TRP A NE1 1 
ATOM   775  C  CE2 . TRP A 1 96  ? 32.275  30.747  10.987  1.00 11.83 ? 96  TRP A CE2 1 
ATOM   776  C  CE3 . TRP A 1 96  ? 34.386  31.910  10.981  1.00 12.63 ? 96  TRP A CE3 1 
ATOM   777  C  CZ2 . TRP A 1 96  ? 31.801  31.516  9.932   1.00 13.73 ? 96  TRP A CZ2 1 
ATOM   778  C  CZ3 . TRP A 1 96  ? 33.907  32.689  9.958   1.00 13.52 ? 96  TRP A CZ3 1 
ATOM   779  C  CH2 . TRP A 1 96  ? 32.638  32.483  9.417   1.00 15.04 ? 96  TRP A CH2 1 
ATOM   780  N  N   . LYS A 1 97  ? 36.683  29.563  10.845  1.00 14.16 ? 97  LYS A N   1 
ATOM   781  C  CA  . LYS A 1 97  ? 36.815  29.940  9.428   1.00 15.13 ? 97  LYS A CA  1 
ATOM   782  C  C   . LYS A 1 97  ? 37.362  28.737  8.654   1.00 13.90 ? 97  LYS A C   1 
ATOM   783  O  O   . LYS A 1 97  ? 36.940  28.535  7.529   1.00 14.09 ? 97  LYS A O   1 
ATOM   784  C  CB  . LYS A 1 97  ? 37.703  31.186  9.239   1.00 18.05 ? 97  LYS A CB  1 
ATOM   785  C  CG  . LYS A 1 97  ? 37.687  31.765  7.837   1.00 23.09 ? 97  LYS A CG  1 
ATOM   786  C  CD  . LYS A 1 97  ? 36.336  32.168  7.303   1.00 27.04 ? 97  LYS A CD  1 
ATOM   787  C  CE  . LYS A 1 97  ? 36.359  32.925  5.988   1.00 33.71 ? 97  LYS A CE  1 
ATOM   788  N  NZ  . LYS A 1 97  ? 37.663  33.601  5.769   1.00 40.60 ? 97  LYS A NZ  1 
ATOM   789  N  N   . LYS A 1 98  ? 38.221  27.961  9.282   1.00 13.58 ? 98  LYS A N   1 
ATOM   790  C  CA  . LYS A 1 98  ? 38.767  26.761  8.622   1.00 14.10 ? 98  LYS A CA  1 
ATOM   791  C  C   . LYS A 1 98  ? 37.638  25.822  8.248   1.00 13.18 ? 98  LYS A C   1 
ATOM   792  O  O   . LYS A 1 98  ? 37.525  25.412  7.051   1.00 13.42 ? 98  LYS A O   1 
ATOM   793  C  CB  . LYS A 1 98  ? 39.719  26.097  9.576   1.00 18.05 ? 98  LYS A CB  1 
ATOM   794  C  CG  . LYS A 1 98  ? 40.550  25.005  9.034   1.00 20.19 ? 98  LYS A CG  1 
ATOM   795  C  CD  . LYS A 1 98  ? 41.678  24.723  10.013  1.00 21.29 ? 98  LYS A CD  1 
ATOM   796  C  CE  . LYS A 1 98  ? 42.073  23.295  9.925   1.00 22.25 ? 98  LYS A CE  1 
ATOM   797  N  NZ  . LYS A 1 98  ? 43.127  23.040  10.919  1.00 22.04 ? 98  LYS A NZ  1 
ATOM   798  N  N   . ALA A 1 99  ? 36.798  25.464  9.223   1.00 12.76 ? 99  ALA A N   1 
ATOM   799  C  CA  . ALA A 1 99  ? 35.702  24.511  8.964   1.00 13.76 ? 99  ALA A CA  1 
ATOM   800  C  C   . ALA A 1 99  ? 34.702  25.149  8.011   1.00 12.98 ? 99  ALA A C   1 
ATOM   801  O  O   . ALA A 1 99  ? 34.184  24.439  7.125   1.00 13.18 ? 99  ALA A O   1 
ATOM   802  C  CB  . ALA A 1 99  ? 35.065  24.072  10.256  1.00 14.05 ? 99  ALA A CB  1 
ATOM   803  N  N   . HIS A 1 100 ? 34.391  26.428  8.173   1.00 12.58 ? 100 HIS A N   1 
ATOM   804  C  CA  . HIS A 1 100 ? 33.466  27.156  7.271   1.00 12.46 ? 100 HIS A CA  1 
ATOM   805  C  C   . HIS A 1 100 ? 33.939  27.042  5.821   1.00 13.56 ? 100 HIS A C   1 
ATOM   806  O  O   . HIS A 1 100 ? 33.137  26.706  4.968   1.00 12.65 ? 100 HIS A O   1 
ATOM   807  C  CB  . HIS A 1 100 ? 33.323  28.590  7.739   1.00 13.56 ? 100 HIS A CB  1 
ATOM   808  C  CG  . HIS A 1 100 ? 32.599  29.460  6.799   1.00 16.08 ? 100 HIS A CG  1 
ATOM   809  N  ND1 . HIS A 1 100 ? 31.216  29.543  6.833   1.00 17.25 ? 100 HIS A ND1 1 
ATOM   810  C  CD2 . HIS A 1 100 ? 33.034  30.396  5.929   1.00 19.56 ? 100 HIS A CD2 1 
ATOM   811  C  CE1 . HIS A 1 100 ? 30.823  30.424  5.936   1.00 19.79 ? 100 HIS A CE1 1 
ATOM   812  N  NE2 . HIS A 1 100 ? 31.925  30.962  5.352   1.00 21.96 ? 100 HIS A NE2 1 
ATOM   813  N  N   . ASN A 1 101 ? 35.213  27.328  5.557   1.00 13.25 ? 101 ASN A N   1 
ATOM   814  C  CA  . ASN A 1 101 ? 35.690  27.300  4.169   1.00 13.59 ? 101 ASN A CA  1 
ATOM   815  C  C   . ASN A 1 101 ? 35.665  25.873  3.616   1.00 14.05 ? 101 ASN A C   1 
ATOM   816  O  O   . ASN A 1 101 ? 35.369  25.737  2.432   1.00 14.11 ? 101 ASN A O   1 
ATOM   817  C  CB  . ASN A 1 101 ? 37.107  27.840  4.049   1.00 12.89 ? 101 ASN A CB  1 
ATOM   818  C  CG  . ASN A 1 101 ? 37.218  29.310  4.297   1.00 14.73 ? 101 ASN A CG  1 
ATOM   819  O  OD1 . ASN A 1 101 ? 36.250  30.060  4.251   1.00 14.94 ? 101 ASN A OD1 1 
ATOM   820  N  ND2 . ASN A 1 101 ? 38.420  29.756  4.583   1.00 16.52 ? 101 ASN A ND2 1 
ATOM   821  N  N   . ILE A 1 102 ? 35.975  24.884  4.408   1.00 12.44 ? 102 ILE A N   1 
ATOM   822  C  CA  . ILE A 1 102 ? 35.996  23.473  3.965   1.00 12.06 ? 102 ILE A CA  1 
ATOM   823  C  C   . ILE A 1 102 ? 34.592  23.001  3.715   1.00 12.67 ? 102 ILE A C   1 
ATOM   824  O  O   . ILE A 1 102 ? 34.372  22.344  2.664   1.00 16.82 ? 102 ILE A O   1 
ATOM   825  C  CB  . ILE A 1 102 ? 36.719  22.605  4.987   1.00 13.03 ? 102 ILE A CB  1 
ATOM   826  C  CG1 . ILE A 1 102 ? 38.217  22.933  4.948   1.00 11.90 ? 102 ILE A CG1 1 
ATOM   827  C  CG2 . ILE A 1 102 ? 36.490  21.136  4.681   1.00 15.51 ? 102 ILE A CG2 1 
ATOM   828  C  CD1 . ILE A 1 102 ? 38.916  22.362  6.149   1.00 13.08 ? 102 ILE A CD1 1 
ATOM   829  N  N   . LEU A 1 103 ? 33.651  23.354  4.570   1.00 13.18 ? 103 LEU A N   1 
ATOM   830  C  CA  . LEU A 1 103 ? 32.301  22.739  4.461   1.00 14.18 ? 103 LEU A CA  1 
ATOM   831  C  C   . LEU A 1 103 ? 31.334  23.570  3.623   1.00 13.65 ? 103 LEU A C   1 
ATOM   832  O  O   . LEU A 1 103 ? 30.340  22.958  3.199   1.00 14.19 ? 103 LEU A O   1 
ATOM   833  C  CB  . LEU A 1 103 ? 31.712  22.568  5.844   1.00 14.86 ? 103 LEU A CB  1 
ATOM   834  C  CG  . LEU A 1 103 ? 32.354  21.449  6.638   1.00 15.27 ? 103 LEU A CG  1 
ATOM   835  C  CD1 . LEU A 1 103 ? 32.147  21.681  8.100   1.00 16.95 ? 103 LEU A CD1 1 
ATOM   836  C  CD2 . LEU A 1 103 ? 31.763  20.099  6.214   1.00 16.80 ? 103 LEU A CD2 1 
ATOM   837  N  N   . LEU A 1 104 ? 31.571  24.850  3.334   1.00 14.11 ? 104 LEU A N   1 
ATOM   838  C  CA  . LEU A 1 104 ? 30.574  25.613  2.526   1.00 13.85 ? 104 LEU A CA  1 
ATOM   839  C  C   . LEU A 1 104 ? 30.231  24.891  1.225   1.00 14.96 ? 104 LEU A C   1 
ATOM   840  O  O   . LEU A 1 104 ? 29.041  24.783  0.898   1.00 14.01 ? 104 LEU A O   1 
ATOM   841  C  CB  . LEU A 1 104 ? 31.050  27.059  2.303   1.00 17.87 ? 104 LEU A CB  1 
ATOM   842  C  CG  . LEU A 1 104 ? 29.960  28.067  1.956   1.00 23.83 ? 104 LEU A CG  1 
ATOM   843  C  CD1 . LEU A 1 104 ? 29.033  28.298  3.118   1.00 25.16 ? 104 LEU A CD1 1 
ATOM   844  C  CD2 . LEU A 1 104 ? 30.582  29.385  1.528   1.00 24.11 ? 104 LEU A CD2 1 
ATOM   845  N  N   . PRO A 1 105 ? 31.184  24.422  0.410   1.00 14.78 ? 105 PRO A N   1 
ATOM   846  C  CA  . PRO A 1 105 ? 30.822  23.810  -0.875  1.00 16.24 ? 105 PRO A CA  1 
ATOM   847  C  C   . PRO A 1 105 ? 29.983  22.529  -0.689  1.00 15.71 ? 105 PRO A C   1 
ATOM   848  O  O   . PRO A 1 105 ? 29.181  22.188  -1.586  1.00 18.69 ? 105 PRO A O   1 
ATOM   849  C  CB  . PRO A 1 105 ? 32.177  23.550  -1.543  1.00 18.68 ? 105 PRO A CB  1 
ATOM   850  C  CG  . PRO A 1 105 ? 33.143  24.482  -0.839  1.00 18.64 ? 105 PRO A CG  1 
ATOM   851  C  CD  . PRO A 1 105 ? 32.658  24.535  0.589   1.00 16.30 ? 105 PRO A CD  1 
ATOM   852  N  N   . SER A 1 106 ? 30.129  21.837  0.419   1.00 14.08 ? 106 SER A N   1 
ATOM   853  C  CA  . SER A 1 106 ? 29.362  20.606  0.724   1.00 15.28 ? 106 SER A CA  1 
ATOM   854  C  C   . SER A 1 106 ? 27.922  20.928  1.087   1.00 13.86 ? 106 SER A C   1 
ATOM   855  O  O   . SER A 1 106 ? 27.125  19.987  1.167   1.00 14.71 ? 106 SER A O   1 
ATOM   856  C  CB  . SER A 1 106 ? 29.989  19.791  1.791   1.00 19.97 ? 106 SER A CB  1 
ATOM   857  O  OG  . SER A 1 106 ? 31.221  19.276  1.314   1.00 26.58 ? 106 SER A OG  1 
ATOM   858  N  N   . PHE A 1 107 ? 27.590  22.185  1.294   1.00 13.68 ? 107 PHE A N   1 
ATOM   859  C  CA  . PHE A 1 107 ? 26.233  22.580  1.749   1.00 13.62 ? 107 PHE A CA  1 
ATOM   860  C  C   . PHE A 1 107 ? 25.561  23.475  0.735   1.00 15.30 ? 107 PHE A C   1 
ATOM   861  O  O   . PHE A 1 107 ? 24.479  23.995  1.009   1.00 15.73 ? 107 PHE A O   1 
ATOM   862  C  CB  . PHE A 1 107 ? 26.347  23.244  3.108   1.00 12.23 ? 107 PHE A CB  1 
ATOM   863  C  CG  . PHE A 1 107 ? 26.353  22.286  4.270   1.00 12.56 ? 107 PHE A CG  1 
ATOM   864  C  CD1 . PHE A 1 107 ? 25.202  21.605  4.646   1.00 13.02 ? 107 PHE A CD1 1 
ATOM   865  C  CD2 . PHE A 1 107 ? 27.526  22.024  4.967   1.00 12.50 ? 107 PHE A CD2 1 
ATOM   866  C  CE1 . PHE A 1 107 ? 25.225  20.750  5.736   1.00 13.52 ? 107 PHE A CE1 1 
ATOM   867  C  CE2 . PHE A 1 107 ? 27.548  21.184  6.054   1.00 13.57 ? 107 PHE A CE2 1 
ATOM   868  C  CZ  . PHE A 1 107 ? 26.396  20.525  6.419   1.00 14.99 ? 107 PHE A CZ  1 
ATOM   869  N  N   . SER A 1 108 ? 26.186  23.661  -0.447  1.00 16.06 ? 108 SER A N   1 
ATOM   870  C  CA  . SER A 1 108 ? 25.627  24.550  -1.492  1.00 16.84 ? 108 SER A CA  1 
ATOM   871  C  C   . SER A 1 108 ? 24.357  23.945  -2.069  1.00 16.67 ? 108 SER A C   1 
ATOM   872  O  O   . SER A 1 108 ? 24.156  22.740  -2.022  1.00 18.88 ? 108 SER A O   1 
ATOM   873  C  CB  . SER A 1 108 ? 26.624  24.777  -2.596  1.00 18.75 ? 108 SER A CB  1 
ATOM   874  O  OG  . SER A 1 108 ? 26.863  23.576  -3.314  1.00 18.34 ? 108 SER A OG  1 
ATOM   875  N  N   . GLN A 1 109 ? 23.561  24.789  -2.700  1.00 20.26 ? 109 GLN A N   1 
ATOM   876  C  CA  . GLN A 1 109 ? 22.444  24.288  -3.526  1.00 19.68 ? 109 GLN A CA  1 
ATOM   877  C  C   . GLN A 1 109 ? 22.931  23.239  -4.550  1.00 19.11 ? 109 GLN A C   1 
ATOM   878  O  O   . GLN A 1 109 ? 22.276  22.205  -4.710  1.00 19.85 ? 109 GLN A O   1 
ATOM   879  C  CB  . GLN A 1 109 ? 21.761  25.476  -4.179  1.00 20.32 ? 109 GLN A CB  1 
ATOM   880  C  CG  . GLN A 1 109 ? 20.510  25.073  -4.948  1.00 21.15 ? 109 GLN A CG  1 
ATOM   881  C  CD  . GLN A 1 109 ? 19.495  24.337  -4.116  1.00 24.17 ? 109 GLN A CD  1 
ATOM   882  O  OE1 . GLN A 1 109 ? 18.917  23.338  -4.527  1.00 21.47 ? 109 GLN A OE1 1 
ATOM   883  N  NE2 . GLN A 1 109 ? 19.259  24.855  -2.932  1.00 18.84 ? 109 GLN A NE2 1 
ATOM   884  N  N   . GLN A 1 110 ? 24.084  23.441  -5.179  1.00 20.82 ? 110 GLN A N   1 
ATOM   885  C  CA  . GLN A 1 110 ? 24.624  22.483  -6.170  1.00 23.06 ? 110 GLN A CA  1 
ATOM   886  C  C   . GLN A 1 110 ? 24.889  21.124  -5.504  1.00 22.71 ? 110 GLN A C   1 
ATOM   887  O  O   . GLN A 1 110 ? 24.569  20.029  -6.114  1.00 21.89 ? 110 GLN A O   1 
ATOM   888  C  CB  . GLN A 1 110 ? 25.853  23.113  -6.794  1.00 28.83 ? 110 GLN A CB  1 
ATOM   889  C  CG  . GLN A 1 110 ? 26.584  22.219  -7.779  1.00 36.16 ? 110 GLN A CG  1 
ATOM   890  C  CD  . GLN A 1 110 ? 25.777  21.862  -9.006  1.00 41.69 ? 110 GLN A CD  1 
ATOM   891  O  OE1 . GLN A 1 110 ? 24.768  22.503  -9.330  1.00 45.02 ? 110 GLN A OE1 1 
ATOM   892  N  NE2 . GLN A 1 110 ? 26.221  20.817  -9.700  1.00 44.81 ? 110 GLN A NE2 1 
ATOM   893  N  N   . ALA A 1 111 ? 25.385  21.108  -4.260  1.00 18.84 ? 111 ALA A N   1 
ATOM   894  C  CA  . ALA A 1 111 ? 25.669  19.867  -3.514  1.00 17.73 ? 111 ALA A CA  1 
ATOM   895  C  C   . ALA A 1 111 ? 24.377  19.086  -3.247  1.00 16.25 ? 111 ALA A C   1 
ATOM   896  O  O   . ALA A 1 111 ? 24.430  17.861  -3.015  1.00 17.39 ? 111 ALA A O   1 
ATOM   897  C  CB  . ALA A 1 111 ? 26.369  20.190  -2.219  1.00 16.56 ? 111 ALA A CB  1 
ATOM   898  N  N   . MET A 1 112 ? 23.255  19.784  -3.218  1.00 16.42 ? 112 MET A N   1 
ATOM   899  C  CA  . MET A 1 112 ? 21.999  19.072  -2.886  1.00 14.82 ? 112 MET A CA  1 
ATOM   900  C  C   . MET A 1 112 ? 21.691  18.006  -3.935  1.00 14.78 ? 112 MET A C   1 
ATOM   901  O  O   . MET A 1 112 ? 20.985  17.016  -3.626  1.00 14.12 ? 112 MET A O   1 
ATOM   902  C  CB  . MET A 1 112 ? 20.822  20.042  -2.737  1.00 15.61 ? 112 MET A CB  1 
ATOM   903  C  CG  . MET A 1 112 ? 21.020  20.970  -1.594  1.00 16.79 ? 112 MET A CG  1 
ATOM   904  S  SD  . MET A 1 112 ? 21.364  20.168  -0.012  1.00 18.12 ? 112 MET A SD  1 
ATOM   905  C  CE  . MET A 1 112 ? 22.939  20.883  0.419   1.00 18.36 ? 112 MET A CE  1 
ATOM   906  N  N   . LYS A 1 113 ? 22.083  18.231  -5.186  1.00 16.47 ? 113 LYS A N   1 
ATOM   907  C  CA  . LYS A 1 113 ? 21.885  17.189  -6.232  1.00 17.37 ? 113 LYS A CA  1 
ATOM   908  C  C   . LYS A 1 113 ? 22.473  15.858  -5.790  1.00 16.58 ? 113 LYS A C   1 
ATOM   909  O  O   . LYS A 1 113 ? 21.869  14.819  -6.079  1.00 17.73 ? 113 LYS A O   1 
ATOM   910  C  CB  . LYS A 1 113 ? 22.513  17.605  -7.579  1.00 17.96 ? 113 LYS A CB  1 
ATOM   911  C  CG  . LYS A 1 113 ? 21.883  18.841  -8.178  1.00 20.90 ? 113 LYS A CG  1 
ATOM   912  C  CD  . LYS A 1 113 ? 22.627  19.473  -9.350  1.00 22.60 ? 113 LYS A CD  1 
ATOM   913  C  CE  . LYS A 1 113 ? 21.861  20.633  -9.934  1.00 25.76 ? 113 LYS A CE  1 
ATOM   914  N  NZ  . LYS A 1 113 ? 22.599  21.237  -11.077 1.00 29.21 ? 113 LYS A NZ  1 
ATOM   915  N  N   . GLY A 1 114 ? 23.608  15.880  -5.110  1.00 15.34 ? 114 GLY A N   1 
ATOM   916  C  CA  . GLY A 1 114 ? 24.269  14.657  -4.653  1.00 16.49 ? 114 GLY A CA  1 
ATOM   917  C  C   . GLY A 1 114 ? 23.585  14.030  -3.460  1.00 17.81 ? 114 GLY A C   1 
ATOM   918  O  O   . GLY A 1 114 ? 23.706  12.798  -3.297  1.00 22.39 ? 114 GLY A O   1 
ATOM   919  N  N   . TYR A 1 115 ? 22.969  14.804  -2.562  1.00 14.11 ? 115 TYR A N   1 
ATOM   920  C  CA  . TYR A 1 115 ? 22.324  14.233  -1.353  1.00 14.39 ? 115 TYR A CA  1 
ATOM   921  C  C   . TYR A 1 115 ? 20.906  13.737  -1.665  1.00 13.07 ? 115 TYR A C   1 
ATOM   922  O  O   . TYR A 1 115 ? 20.360  12.984  -0.892  1.00 13.80 ? 115 TYR A O   1 
ATOM   923  C  CB  . TYR A 1 115 ? 22.195  15.259  -0.228  1.00 14.11 ? 115 TYR A CB  1 
ATOM   924  C  CG  . TYR A 1 115 ? 23.518  15.808  0.259   1.00 14.05 ? 115 TYR A CG  1 
ATOM   925  C  CD1 . TYR A 1 115 ? 24.546  14.974  0.669   1.00 15.00 ? 115 TYR A CD1 1 
ATOM   926  C  CD2 . TYR A 1 115 ? 23.749  17.161  0.342   1.00 13.82 ? 115 TYR A CD2 1 
ATOM   927  C  CE1 . TYR A 1 115 ? 25.776  15.470  1.099   1.00 17.90 ? 115 TYR A CE1 1 
ATOM   928  C  CE2 . TYR A 1 115 ? 24.967  17.672  0.734   1.00 14.79 ? 115 TYR A CE2 1 
ATOM   929  C  CZ  . TYR A 1 115 ? 25.974  16.842  1.133   1.00 17.03 ? 115 TYR A CZ  1 
ATOM   930  O  OH  . TYR A 1 115 ? 27.202  17.372  1.520   1.00 18.64 ? 115 TYR A OH  1 
ATOM   931  N  N   . HIS A 1 116 ? 20.343  14.182  -2.779  1.00 13.71 ? 116 HIS A N   1 
ATOM   932  C  CA  . HIS A 1 116 ? 18.906  13.982  -3.084  1.00 13.19 ? 116 HIS A CA  1 
ATOM   933  C  C   . HIS A 1 116 ? 18.529  12.496  -2.940  1.00 14.00 ? 116 HIS A C   1 
ATOM   934  O  O   . HIS A 1 116 ? 17.508  12.185  -2.363  1.00 13.85 ? 116 HIS A O   1 
ATOM   935  C  CB  . HIS A 1 116 ? 18.629  14.550  -4.481  1.00 14.16 ? 116 HIS A CB  1 
ATOM   936  C  CG  . HIS A 1 116 ? 17.201  14.386  -4.859  1.00 13.04 ? 116 HIS A CG  1 
ATOM   937  N  ND1 . HIS A 1 116 ? 16.234  15.288  -4.446  1.00 13.40 ? 116 HIS A ND1 1 
ATOM   938  C  CD2 . HIS A 1 116 ? 16.564  13.384  -5.505  1.00 12.87 ? 116 HIS A CD2 1 
ATOM   939  C  CE1 . HIS A 1 116 ? 15.064  14.844  -4.866  1.00 13.87 ? 116 HIS A CE1 1 
ATOM   940  N  NE2 . HIS A 1 116 ? 15.234  13.690  -5.546  1.00 12.66 ? 116 HIS A NE2 1 
ATOM   941  N  N   . ALA A 1 117 ? 19.304  11.589  -3.534  1.00 14.23 ? 117 ALA A N   1 
ATOM   942  C  CA  . ALA A 1 117 ? 18.929  10.163  -3.532  1.00 15.80 ? 117 ALA A CA  1 
ATOM   943  C  C   . ALA A 1 117 ? 18.839  9.589   -2.123  1.00 14.84 ? 117 ALA A C   1 
ATOM   944  O  O   . ALA A 1 117 ? 17.911  8.789   -1.843  1.00 15.50 ? 117 ALA A O   1 
ATOM   945  C  CB  . ALA A 1 117 ? 19.863  9.369   -4.390  1.00 16.50 ? 117 ALA A CB  1 
ATOM   946  N  N   A MET A 1 118 ? 19.720  9.963   -1.202  0.50 14.24 ? 118 MET A N   1 
ATOM   947  N  N   B MET A 1 118 ? 19.766  9.970   -1.241  0.50 13.41 ? 118 MET A N   1 
ATOM   948  C  CA  A MET A 1 118 ? 19.597  9.404   0.166   0.50 15.36 ? 118 MET A CA  1 
ATOM   949  C  CA  B MET A 1 118 ? 19.755  9.555   0.187   0.50 13.84 ? 118 MET A CA  1 
ATOM   950  C  C   A MET A 1 118 ? 18.529  10.171  0.963   0.50 14.21 ? 118 MET A C   1 
ATOM   951  C  C   B MET A 1 118 ? 18.521  10.156  0.877   0.50 13.44 ? 118 MET A C   1 
ATOM   952  O  O   A MET A 1 118 ? 17.978  9.586   1.897   0.50 13.42 ? 118 MET A O   1 
ATOM   953  O  O   B MET A 1 118 ? 17.833  9.449   1.590   0.50 12.70 ? 118 MET A O   1 
ATOM   954  C  CB  A MET A 1 118 ? 20.948  9.351   0.879   0.50 18.52 ? 118 MET A CB  1 
ATOM   955  C  CB  B MET A 1 118 ? 21.061  9.968   0.877   0.50 15.71 ? 118 MET A CB  1 
ATOM   956  C  CG  A MET A 1 118 ? 21.863  8.219   0.370   0.50 20.45 ? 118 MET A CG  1 
ATOM   957  C  CG  B MET A 1 118 ? 22.233  9.095   0.448   0.50 16.78 ? 118 MET A CG  1 
ATOM   958  S  SD  A MET A 1 118 ? 21.113  6.562   0.211   0.50 24.57 ? 118 MET A SD  1 
ATOM   959  S  SD  B MET A 1 118 ? 23.790  9.546   1.235   0.50 20.07 ? 118 MET A SD  1 
ATOM   960  C  CE  A MET A 1 118 ? 20.788  6.536   -1.550  0.50 22.12 ? 118 MET A CE  1 
ATOM   961  C  CE  B MET A 1 118 ? 24.022  11.121  0.416   0.50 14.39 ? 118 MET A CE  1 
ATOM   962  N  N   . MET A 1 119 ? 18.196  11.422  0.597   1.00 13.33 ? 119 MET A N   1 
ATOM   963  C  CA  . MET A 1 119 ? 17.017  12.068  1.212   1.00 13.30 ? 119 MET A CA  1 
ATOM   964  C  C   . MET A 1 119 ? 15.785  11.274  0.787   1.00 13.21 ? 119 MET A C   1 
ATOM   965  O  O   . MET A 1 119 ? 14.854  11.033  1.618   1.00 13.66 ? 119 MET A O   1 
ATOM   966  C  CB  . MET A 1 119 ? 16.898  13.539  0.812   1.00 12.88 ? 119 MET A CB  1 
ATOM   967  C  CG  . MET A 1 119 ? 18.045  14.359  1.309   1.00 12.95 ? 119 MET A CG  1 
ATOM   968  S  SD  . MET A 1 119 ? 17.621  16.096  1.033   1.00 17.20 ? 119 MET A SD  1 
ATOM   969  C  CE  . MET A 1 119 ? 19.069  16.945  1.702   1.00 17.45 ? 119 MET A CE  1 
ATOM   970  N  N   . VAL A 1 120 ? 15.718  10.892  -0.491  1.00 12.17 ? 120 VAL A N   1 
ATOM   971  C  CA  . VAL A 1 120 ? 14.529  10.131  -0.981  1.00 12.64 ? 120 VAL A CA  1 
ATOM   972  C  C   . VAL A 1 120 ? 14.437  8.778   -0.255  1.00 12.74 ? 120 VAL A C   1 
ATOM   973  O  O   . VAL A 1 120 ? 13.347  8.315   0.107   1.00 12.56 ? 120 VAL A O   1 
ATOM   974  C  CB  . VAL A 1 120 ? 14.599  9.940   -2.489  1.00 13.34 ? 120 VAL A CB  1 
ATOM   975  C  CG1 . VAL A 1 120 ? 13.582  8.914   -2.939  1.00 14.47 ? 120 VAL A CG1 1 
ATOM   976  C  CG2 . VAL A 1 120 ? 14.452  11.278  -3.212  1.00 13.45 ? 120 VAL A CG2 1 
ATOM   977  N  N   . ASP A 1 121 ? 15.567  8.121   -0.019  1.00 13.14 ? 121 ASP A N   1 
ATOM   978  C  CA  . ASP A 1 121 ? 15.585  6.839   0.723   1.00 13.08 ? 121 ASP A CA  1 
ATOM   979  C  C   . ASP A 1 121 ? 14.805  7.013   2.026   1.00 11.91 ? 121 ASP A C   1 
ATOM   980  O  O   . ASP A 1 121 ? 13.903  6.203   2.326   1.00 11.76 ? 121 ASP A O   1 
ATOM   981  C  CB  . ASP A 1 121 ? 17.020  6.395   0.960   1.00 12.60 ? 121 ASP A CB  1 
ATOM   982  C  CG  . ASP A 1 121 ? 17.166  5.071   1.699   1.00 13.40 ? 121 ASP A CG  1 
ATOM   983  O  OD1 . ASP A 1 121 ? 16.662  4.934   2.796   1.00 15.30 ? 121 ASP A OD1 1 
ATOM   984  O  OD2 . ASP A 1 121 ? 17.907  4.211   1.134   1.00 16.26 ? 121 ASP A OD2 1 
ATOM   985  N  N   . ILE A 1 122 ? 15.108  8.043   2.815   1.00 11.64 ? 122 ILE A N   1 
ATOM   986  C  CA  . ILE A 1 122 ? 14.439  8.187   4.103   1.00 11.68 ? 122 ILE A CA  1 
ATOM   987  C  C   . ILE A 1 122 ? 12.979  8.613   3.901   1.00 11.29 ? 122 ILE A C   1 
ATOM   988  O  O   . ILE A 1 122 ? 12.093  8.159   4.636   1.00 12.01 ? 122 ILE A O   1 
ATOM   989  C  CB  . ILE A 1 122 ? 15.232  9.112   5.045   1.00 12.67 ? 122 ILE A CB  1 
ATOM   990  C  CG1 . ILE A 1 122 ? 16.723  8.709   5.166   1.00 13.44 ? 122 ILE A CG1 1 
ATOM   991  C  CG2 . ILE A 1 122 ? 14.560  9.160   6.380   1.00 12.79 ? 122 ILE A CG2 1 
ATOM   992  C  CD1 . ILE A 1 122 ? 16.946  7.272   5.588   1.00 13.75 ? 122 ILE A CD1 1 
ATOM   993  N  N   . ALA A 1 123 ? 12.736  9.543   2.984   1.00 10.82 ? 123 ALA A N   1 
ATOM   994  C  CA  . ALA A 1 123 ? 11.362  10.023  2.731   1.00 11.11 ? 123 ALA A CA  1 
ATOM   995  C  C   . ALA A 1 123 ? 10.462  8.870   2.309   1.00 10.95 ? 123 ALA A C   1 
ATOM   996  O  O   . ALA A 1 123 ? 9.327   8.780   2.756   1.00 12.10 ? 123 ALA A O   1 
ATOM   997  C  CB  . ALA A 1 123 ? 11.389  11.084  1.698   1.00 11.36 ? 123 ALA A CB  1 
ATOM   998  N  N   . VAL A 1 124 ? 10.967  7.971   1.491   1.00 11.11 ? 124 VAL A N   1 
ATOM   999  C  CA  . VAL A 1 124 ? 10.164  6.785   1.103   1.00 12.43 ? 124 VAL A CA  1 
ATOM   1000 C  C   . VAL A 1 124 ? 9.893   5.951   2.341   1.00 11.86 ? 124 VAL A C   1 
ATOM   1001 O  O   . VAL A 1 124 ? 8.755   5.399   2.514   1.00 12.57 ? 124 VAL A O   1 
ATOM   1002 C  CB  . VAL A 1 124 ? 10.869  5.983   0.008   1.00 13.41 ? 124 VAL A CB  1 
ATOM   1003 C  CG1 . VAL A 1 124 ? 10.243  4.614   -0.158  1.00 15.69 ? 124 VAL A CG1 1 
ATOM   1004 C  CG2 . VAL A 1 124 ? 10.801  6.761   -1.274  1.00 13.44 ? 124 VAL A CG2 1 
ATOM   1005 N  N   . GLN A 1 125 ? 10.853  5.822   3.262   1.00 11.41 ? 125 GLN A N   1 
ATOM   1006 C  CA  . GLN A 1 125 ? 10.551  5.051   4.486   1.00 12.13 ? 125 GLN A CA  1 
ATOM   1007 C  C   . GLN A 1 125 ? 9.401   5.692   5.273   1.00 12.07 ? 125 GLN A C   1 
ATOM   1008 O  O   . GLN A 1 125 ? 8.560   4.977   5.811   1.00 11.83 ? 125 GLN A O   1 
ATOM   1009 C  CB  . GLN A 1 125 ? 11.778  4.905   5.393   1.00 12.37 ? 125 GLN A CB  1 
ATOM   1010 C  CG  . GLN A 1 125 ? 12.895  4.064   4.831   1.00 12.53 ? 125 GLN A CG  1 
ATOM   1011 C  CD  . GLN A 1 125 ? 13.986  3.817   5.842   1.00 13.16 ? 125 GLN A CD  1 
ATOM   1012 O  OE1 . GLN A 1 125 ? 13.716  3.359   6.939   1.00 12.69 ? 125 GLN A OE1 1 
ATOM   1013 N  NE2 . GLN A 1 125 ? 15.225  4.020   5.417   1.00 13.74 ? 125 GLN A NE2 1 
ATOM   1014 N  N   A LEU A 1 126 ? 9.342   7.027   5.337   0.50 11.58 ? 126 LEU A N   1 
ATOM   1015 N  N   B LEU A 1 126 ? 9.326   7.034   5.348   0.50 12.11 ? 126 LEU A N   1 
ATOM   1016 C  CA  A LEU A 1 126 ? 8.225   7.696   6.035   0.50 11.38 ? 126 LEU A CA  1 
ATOM   1017 C  CA  B LEU A 1 126 ? 8.211   7.727   6.048   0.50 12.30 ? 126 LEU A CA  1 
ATOM   1018 C  C   A LEU A 1 126 ? 6.907   7.386   5.315   0.50 12.14 ? 126 LEU A C   1 
ATOM   1019 C  C   B LEU A 1 126 ? 6.891   7.432   5.321   0.50 12.65 ? 126 LEU A C   1 
ATOM   1020 O  O   A LEU A 1 126 ? 5.927   6.959   5.967   0.50 12.16 ? 126 LEU A O   1 
ATOM   1021 O  O   B LEU A 1 126 ? 5.895   7.034   5.971   0.50 12.67 ? 126 LEU A O   1 
ATOM   1022 C  CB  A LEU A 1 126 ? 8.458   9.203   6.048   0.50 10.90 ? 126 LEU A CB  1 
ATOM   1023 C  CB  B LEU A 1 126 ? 8.488   9.234   6.077   0.50 12.41 ? 126 LEU A CB  1 
ATOM   1024 C  CG  A LEU A 1 126 ? 7.312   9.973   6.688   0.50 11.34 ? 126 LEU A CG  1 
ATOM   1025 C  CG  B LEU A 1 126 ? 7.467   10.102  6.820   0.50 13.82 ? 126 LEU A CG  1 
ATOM   1026 C  CD1 A LEU A 1 126 ? 7.442   9.929   8.203   0.50 10.71 ? 126 LEU A CD1 1 
ATOM   1027 C  CD1 B LEU A 1 126 ? 6.307   10.509  5.932   0.50 13.14 ? 126 LEU A CD1 1 
ATOM   1028 C  CD2 A LEU A 1 126 ? 7.334   11.423  6.233   0.50 11.52 ? 126 LEU A CD2 1 
ATOM   1029 C  CD2 B LEU A 1 126 ? 6.969   9.458   8.103   0.50 13.63 ? 126 LEU A CD2 1 
ATOM   1030 N  N   . VAL A 1 127 ? 6.885   7.584   3.999   1.00 11.99 ? 127 VAL A N   1 
ATOM   1031 C  CA  . VAL A 1 127 ? 5.627   7.359   3.241   1.00 12.17 ? 127 VAL A CA  1 
ATOM   1032 C  C   . VAL A 1 127 ? 5.187   5.910   3.440   1.00 12.39 ? 127 VAL A C   1 
ATOM   1033 O  O   . VAL A 1 127 ? 3.976   5.653   3.648   1.00 12.34 ? 127 VAL A O   1 
ATOM   1034 C  CB  . VAL A 1 127 ? 5.795   7.698   1.765   1.00 12.81 ? 127 VAL A CB  1 
ATOM   1035 C  CG1 . VAL A 1 127 ? 4.571   7.286   0.974   1.00 13.87 ? 127 VAL A CG1 1 
ATOM   1036 C  CG2 . VAL A 1 127 ? 6.017   9.194   1.589   1.00 14.00 ? 127 VAL A CG2 1 
ATOM   1037 N  N   . GLN A 1 128 ? 6.103   4.955   3.362   1.00 11.83 ? 128 GLN A N   1 
ATOM   1038 C  CA  . GLN A 1 128 ? 5.731   3.527   3.517   1.00 12.99 ? 128 GLN A CA  1 
ATOM   1039 C  C   . GLN A 1 128 ? 5.200   3.282   4.911   1.00 12.12 ? 128 GLN A C   1 
ATOM   1040 O  O   . GLN A 1 128 ? 4.236   2.538   5.035   1.00 12.30 ? 128 GLN A O   1 
ATOM   1041 C  CB  . GLN A 1 128 ? 6.892   2.577   3.207   1.00 14.22 ? 128 GLN A CB  1 
ATOM   1042 C  CG  . GLN A 1 128 ? 7.290   2.603   1.743   1.00 16.06 ? 128 GLN A CG  1 
ATOM   1043 C  CD  . GLN A 1 128 ? 8.469   1.718   1.465   1.00 23.93 ? 128 GLN A CD  1 
ATOM   1044 O  OE1 . GLN A 1 128 ? 9.499   1.815   2.131   1.00 28.56 ? 128 GLN A OE1 1 
ATOM   1045 N  NE2 . GLN A 1 128 ? 8.334   0.887   0.453   1.00 28.85 ? 128 GLN A NE2 1 
ATOM   1046 N  N   . LYS A 1 129 ? 5.770   3.900   5.957   1.00 11.40 ? 129 LYS A N   1 
ATOM   1047 C  CA  . LYS A 1 129 ? 5.226   3.737   7.316   1.00 11.96 ? 129 LYS A CA  1 
ATOM   1048 C  C   . LYS A 1 129 ? 3.738   4.152   7.340   1.00 12.20 ? 129 LYS A C   1 
ATOM   1049 O  O   . LYS A 1 129 ? 2.898   3.473   7.862   1.00 11.95 ? 129 LYS A O   1 
ATOM   1050 C  CB  . LYS A 1 129 ? 5.997   4.564   8.362   1.00 12.37 ? 129 LYS A CB  1 
ATOM   1051 C  CG  . LYS A 1 129 ? 5.462   4.431   9.771   1.00 13.23 ? 129 LYS A CG  1 
ATOM   1052 C  CD  . LYS A 1 129 ? 6.231   5.150   10.840  1.00 14.77 ? 129 LYS A CD  1 
ATOM   1053 C  CE  . LYS A 1 129 ? 5.502   5.015   12.152  1.00 16.78 ? 129 LYS A CE  1 
ATOM   1054 N  NZ  . LYS A 1 129 ? 6.344   5.462   13.289  1.00 17.69 ? 129 LYS A NZ  1 
ATOM   1055 N  N   . TRP A 1 130 ? 3.461   5.339   6.823   1.00 12.19 ? 130 TRP A N   1 
ATOM   1056 C  CA  . TRP A 1 130 ? 2.076   5.876   6.865   1.00 12.36 ? 130 TRP A CA  1 
ATOM   1057 C  C   . TRP A 1 130 ? 1.125   5.083   5.971   1.00 11.65 ? 130 TRP A C   1 
ATOM   1058 O  O   . TRP A 1 130 ? -0.042  4.878   6.352   1.00 12.74 ? 130 TRP A O   1 
ATOM   1059 C  CB  . TRP A 1 130 ? 2.098   7.370   6.551   1.00 12.07 ? 130 TRP A CB  1 
ATOM   1060 C  CG  . TRP A 1 130 ? 2.809   8.168   7.591   1.00 12.08 ? 130 TRP A CG  1 
ATOM   1061 C  CD1 . TRP A 1 130 ? 3.350   7.769   8.783   1.00 13.76 ? 130 TRP A CD1 1 
ATOM   1062 C  CD2 . TRP A 1 130 ? 2.984   9.592   7.537   1.00 12.75 ? 130 TRP A CD2 1 
ATOM   1063 N  NE1 . TRP A 1 130 ? 3.860   8.855   9.447   1.00 11.66 ? 130 TRP A NE1 1 
ATOM   1064 C  CE2 . TRP A 1 130 ? 3.640   9.984   8.722   1.00 12.37 ? 130 TRP A CE2 1 
ATOM   1065 C  CE3 . TRP A 1 130 ? 2.570   10.577  6.633   1.00 12.30 ? 130 TRP A CE3 1 
ATOM   1066 C  CZ2 . TRP A 1 130 ? 3.974   11.302  9.008   1.00 12.17 ? 130 TRP A CZ2 1 
ATOM   1067 C  CZ3 . TRP A 1 130 ? 2.909   11.892  6.899   1.00 13.56 ? 130 TRP A CZ3 1 
ATOM   1068 C  CH2 . TRP A 1 130 ? 3.594   12.234  8.067   1.00 12.79 ? 130 TRP A CH2 1 
ATOM   1069 N  N   . GLU A 1 131 ? 1.617   4.589   4.847   1.00 11.94 ? 131 GLU A N   1 
ATOM   1070 C  CA  . GLU A 1 131 ? 0.777   3.718   3.985   1.00 12.87 ? 131 GLU A CA  1 
ATOM   1071 C  C   . GLU A 1 131 ? 0.419   2.451   4.767   1.00 14.46 ? 131 GLU A C   1 
ATOM   1072 O  O   . GLU A 1 131 ? -0.618  1.850   4.460   1.00 16.73 ? 131 GLU A O   1 
ATOM   1073 C  CB  . GLU A 1 131 ? 1.503   3.290   2.713   1.00 13.36 ? 131 GLU A CB  1 
ATOM   1074 C  CG  . GLU A 1 131 ? 1.712   4.360   1.698   1.00 15.25 ? 131 GLU A CG  1 
ATOM   1075 C  CD  . GLU A 1 131 ? 0.523   4.843   0.903   1.00 18.25 ? 131 GLU A CD  1 
ATOM   1076 O  OE1 . GLU A 1 131 ? -0.621  4.559   1.288   1.00 20.53 ? 131 GLU A OE1 1 
ATOM   1077 O  OE2 . GLU A 1 131 ? 0.765   5.511   -0.160  1.00 21.23 ? 131 GLU A OE2 1 
ATOM   1078 N  N   . ARG A 1 132 ? 1.242   2.000   5.698   1.00 12.41 ? 132 ARG A N   1 
ATOM   1079 C  CA  . ARG A 1 132 ? 1.039   0.695   6.381   1.00 12.71 ? 132 ARG A CA  1 
ATOM   1080 C  C   . ARG A 1 132 ? 0.255   0.841   7.666   1.00 13.70 ? 132 ARG A C   1 
ATOM   1081 O  O   . ARG A 1 132 ? 0.012   -0.167  8.321   1.00 13.68 ? 132 ARG A O   1 
ATOM   1082 C  CB  . ARG A 1 132 ? 2.428   0.105   6.616   1.00 12.21 ? 132 ARG A CB  1 
ATOM   1083 C  CG  . ARG A 1 132 ? 3.028   -0.446  5.349   1.00 12.05 ? 132 ARG A CG  1 
ATOM   1084 C  CD  . ARG A 1 132 ? 4.516   -0.781  5.434   1.00 12.91 ? 132 ARG A CD  1 
ATOM   1085 N  NE  . ARG A 1 132 ? 5.024   -1.288  4.181   1.00 13.48 ? 132 ARG A NE  1 
ATOM   1086 C  CZ  . ARG A 1 132 ? 6.309   -1.402  3.843   1.00 15.01 ? 132 ARG A CZ  1 
ATOM   1087 N  NH1 . ARG A 1 132 ? 7.265   -1.061  4.698   1.00 14.42 ? 132 ARG A NH1 1 
ATOM   1088 N  NH2 . ARG A 1 132 ? 6.595   -1.859  2.642   1.00 17.15 ? 132 ARG A NH2 1 
ATOM   1089 N  N   . LEU A 1 133 ? -0.189  2.041   8.048   1.00 13.42 ? 133 LEU A N   1 
ATOM   1090 C  CA  . LEU A 1 133 ? -1.029  2.182   9.246   1.00 15.77 ? 133 LEU A CA  1 
ATOM   1091 C  C   . LEU A 1 133 ? -2.408  1.602   8.964   1.00 14.48 ? 133 LEU A C   1 
ATOM   1092 O  O   . LEU A 1 133 ? -2.866  1.638   7.822   1.00 15.62 ? 133 LEU A O   1 
ATOM   1093 C  CB  . LEU A 1 133 ? -1.157  3.641   9.665   1.00 16.21 ? 133 LEU A CB  1 
ATOM   1094 C  CG  . LEU A 1 133 ? 0.165   4.266   10.115  1.00 18.08 ? 133 LEU A CG  1 
ATOM   1095 C  CD1 . LEU A 1 133 ? 0.014   5.733   10.476  1.00 20.26 ? 133 LEU A CD1 1 
ATOM   1096 C  CD2 . LEU A 1 133 ? 0.789   3.535   11.258  1.00 18.18 ? 133 LEU A CD2 1 
ATOM   1097 N  N   . ASN A 1 134 ? -3.005  1.059   9.986   1.00 14.01 ? 134 ASN A N   1 
ATOM   1098 C  CA  . ASN A 1 134 ? -4.397  0.561   9.887   1.00 14.82 ? 134 ASN A CA  1 
ATOM   1099 C  C   . ASN A 1 134 ? -5.388  1.715   10.050  1.00 17.73 ? 134 ASN A C   1 
ATOM   1100 O  O   . ASN A 1 134 ? -5.029  2.771   10.548  1.00 19.24 ? 134 ASN A O   1 
ATOM   1101 C  CB  . ASN A 1 134 ? -4.609  -0.507  10.950  1.00 15.55 ? 134 ASN A CB  1 
ATOM   1102 C  CG  . ASN A 1 134 ? -3.631  -1.662  10.830  1.00 15.89 ? 134 ASN A CG  1 
ATOM   1103 O  OD1 . ASN A 1 134 ? -3.641  -2.401  9.839   1.00 15.96 ? 134 ASN A OD1 1 
ATOM   1104 N  ND2 . ASN A 1 134 ? -2.692  -1.753  11.759  1.00 17.35 ? 134 ASN A ND2 1 
ATOM   1105 N  N   . ALA A 1 135 ? -6.651  1.414   9.709   1.00 20.37 ? 135 ALA A N   1 
ATOM   1106 C  CA  . ALA A 1 135 ? -7.755  2.412   9.705   1.00 25.51 ? 135 ALA A CA  1 
ATOM   1107 C  C   . ALA A 1 135 ? -7.872  3.157   11.035  1.00 26.54 ? 135 ALA A C   1 
ATOM   1108 O  O   . ALA A 1 135 ? -8.067  4.395   10.992  1.00 29.42 ? 135 ALA A O   1 
ATOM   1109 C  CB  . ALA A 1 135 ? -9.058  1.728   9.365   1.00 30.21 ? 135 ALA A CB  1 
ATOM   1110 N  N   . ASP A 1 136 ? -7.783  2.481   12.173  1.00 27.17 ? 136 ASP A N   1 
ATOM   1111 C  CA  . ASP A 1 136 ? -8.102  3.141   13.484  1.00 34.90 ? 136 ASP A CA  1 
ATOM   1112 C  C   . ASP A 1 136 ? -6.896  3.951   14.008  1.00 33.39 ? 136 ASP A C   1 
ATOM   1113 O  O   . ASP A 1 136 ? -6.939  4.416   15.160  1.00 37.10 ? 136 ASP A O   1 
ATOM   1114 C  CB  . ASP A 1 136 ? -8.579  2.131   14.548  1.00 39.03 ? 136 ASP A CB  1 
ATOM   1115 C  CG  . ASP A 1 136 ? -7.694  0.900   14.699  1.00 47.11 ? 136 ASP A CG  1 
ATOM   1116 O  OD1 . ASP A 1 136 ? -6.784  0.729   13.850  1.00 50.70 ? 136 ASP A OD1 1 
ATOM   1117 O  OD2 . ASP A 1 136 ? -7.942  0.084   15.640  1.00 54.06 ? 136 ASP A OD2 1 
ATOM   1118 N  N   . GLU A 1 137 ? -5.829  4.124   13.232  1.00 24.57 ? 137 GLU A N   1 
ATOM   1119 C  CA  . GLU A 1 137 ? -4.548  4.523   13.842  1.00 21.76 ? 137 GLU A CA  1 
ATOM   1120 C  C   . GLU A 1 137 ? -4.294  5.968   13.506  1.00 19.38 ? 137 GLU A C   1 
ATOM   1121 O  O   . GLU A 1 137 ? -4.913  6.481   12.619  1.00 22.20 ? 137 GLU A O   1 
ATOM   1122 C  CB  . GLU A 1 137 ? -3.406  3.618   13.377  1.00 19.19 ? 137 GLU A CB  1 
ATOM   1123 C  CG  . GLU A 1 137 ? -3.639  2.216   13.889  1.00 22.78 ? 137 GLU A CG  1 
ATOM   1124 C  CD  . GLU A 1 137 ? -2.624  1.162   13.503  1.00 25.11 ? 137 GLU A CD  1 
ATOM   1125 O  OE1 . GLU A 1 137 ? -1.815  1.378   12.585  1.00 21.04 ? 137 GLU A OE1 1 
ATOM   1126 O  OE2 . GLU A 1 137 ? -2.733  0.066   14.099  1.00 31.16 ? 137 GLU A OE2 1 
ATOM   1127 N  N   . HIS A 1 138 ? -3.350  6.581   14.195  1.00 17.16 ? 138 HIS A N   1 
ATOM   1128 C  CA  . HIS A 1 138 ? -2.978  7.977   13.902  1.00 16.51 ? 138 HIS A CA  1 
ATOM   1129 C  C   . HIS A 1 138 ? -1.450  8.083   13.859  1.00 15.02 ? 138 HIS A C   1 
ATOM   1130 O  O   . HIS A 1 138 ? -0.759  7.134   14.163  1.00 15.45 ? 138 HIS A O   1 
ATOM   1131 C  CB  . HIS A 1 138 ? -3.593  8.892   14.943  1.00 17.15 ? 138 HIS A CB  1 
ATOM   1132 C  CG  . HIS A 1 138 ? -3.091  8.698   16.326  1.00 18.72 ? 138 HIS A CG  1 
ATOM   1133 N  ND1 . HIS A 1 138 ? -3.734  7.884   17.250  1.00 24.69 ? 138 HIS A ND1 1 
ATOM   1134 C  CD2 . HIS A 1 138 ? -1.989  9.165   16.957  1.00 21.70 ? 138 HIS A CD2 1 
ATOM   1135 C  CE1 . HIS A 1 138 ? -3.066  7.920   18.381  1.00 24.84 ? 138 HIS A CE1 1 
ATOM   1136 N  NE2 . HIS A 1 138 ? -1.992  8.685   18.225  1.00 23.94 ? 138 HIS A NE2 1 
ATOM   1137 N  N   . ILE A 1 139 ? -0.998  9.248   13.404  1.00 13.76 ? 139 ILE A N   1 
ATOM   1138 C  CA  . ILE A 1 139 ? 0.413   9.630   13.245  1.00 14.27 ? 139 ILE A CA  1 
ATOM   1139 C  C   . ILE A 1 139 ? 0.781   10.521  14.419  1.00 13.32 ? 139 ILE A C   1 
ATOM   1140 O  O   . ILE A 1 139 ? 0.055   11.492  14.691  1.00 13.31 ? 139 ILE A O   1 
ATOM   1141 C  CB  . ILE A 1 139 ? 0.604   10.340  11.922  1.00 13.68 ? 139 ILE A CB  1 
ATOM   1142 C  CG1 . ILE A 1 139 ? 0.394   9.339   10.789  1.00 14.09 ? 139 ILE A CG1 1 
ATOM   1143 C  CG2 . ILE A 1 139 ? 1.975   11.006  11.866  1.00 14.73 ? 139 ILE A CG2 1 
ATOM   1144 C  CD1 . ILE A 1 139 ? 0.090   10.012  9.490   1.00 16.09 ? 139 ILE A CD1 1 
ATOM   1145 N  N   . GLU A 1 140 ? 1.924   10.235  15.000  1.00 13.48 ? 140 GLU A N   1 
ATOM   1146 C  CA  . GLU A 1 140 ? 2.536   11.111  16.002  1.00 13.62 ? 140 GLU A CA  1 
ATOM   1147 C  C   . GLU A 1 140 ? 3.518   12.014  15.244  1.00 12.28 ? 140 GLU A C   1 
ATOM   1148 O  O   . GLU A 1 140 ? 4.554   11.506  14.852  1.00 11.91 ? 140 GLU A O   1 
ATOM   1149 C  CB  . GLU A 1 140 ? 3.220   10.283  17.082  1.00 15.77 ? 140 GLU A CB  1 
ATOM   1150 C  CG  . GLU A 1 140 ? 2.296   9.295   17.812  1.00 17.49 ? 140 GLU A CG  1 
ATOM   1151 C  CD  . GLU A 1 140 ? 2.973   8.487   18.924  1.00 22.14 ? 140 GLU A CD  1 
ATOM   1152 O  OE1 . GLU A 1 140 ? 4.165   8.137   18.790  1.00 22.42 ? 140 GLU A OE1 1 
ATOM   1153 O  OE2 . GLU A 1 140 ? 2.283   8.193   19.932  1.00 28.41 ? 140 GLU A OE2 1 
ATOM   1154 N  N   . VAL A 1 141 ? 3.122   13.256  14.963  1.00 11.57 ? 141 VAL A N   1 
ATOM   1155 C  CA  . VAL A 1 141 ? 3.814   14.053  13.926  1.00 11.54 ? 141 VAL A CA  1 
ATOM   1156 C  C   . VAL A 1 141 ? 5.262   14.365  14.302  1.00 11.69 ? 141 VAL A C   1 
ATOM   1157 O  O   . VAL A 1 141 ? 6.154   13.979  13.533  1.00 11.93 ? 141 VAL A O   1 
ATOM   1158 C  CB  . VAL A 1 141 ? 2.977   15.275  13.554  1.00 12.09 ? 141 VAL A CB  1 
ATOM   1159 C  CG1 . VAL A 1 141 ? 3.771   16.140  12.610  1.00 11.79 ? 141 VAL A CG1 1 
ATOM   1160 C  CG2 . VAL A 1 141 ? 1.647   14.839  12.947  1.00 13.06 ? 141 VAL A CG2 1 
ATOM   1161 N  N   . PRO A 1 142 ? 5.560   15.120  15.385  1.00 12.80 ? 142 PRO A N   1 
ATOM   1162 C  CA  . PRO A 1 142 ? 6.950   15.475  15.640  1.00 12.41 ? 142 PRO A CA  1 
ATOM   1163 C  C   . PRO A 1 142 ? 7.815   14.231  15.863  1.00 12.61 ? 142 PRO A C   1 
ATOM   1164 O  O   . PRO A 1 142 ? 9.002   14.192  15.491  1.00 13.41 ? 142 PRO A O   1 
ATOM   1165 C  CB  . PRO A 1 142 ? 6.909   16.323  16.929  1.00 12.39 ? 142 PRO A CB  1 
ATOM   1166 C  CG  . PRO A 1 142 ? 5.568   16.117  17.504  1.00 14.32 ? 142 PRO A CG  1 
ATOM   1167 C  CD  . PRO A 1 142 ? 4.661   15.786  16.330  1.00 12.52 ? 142 PRO A CD  1 
ATOM   1168 N  N   . GLU A 1 143 ? 7.212   13.176  16.405  1.00 11.17 ? 143 GLU A N   1 
ATOM   1169 C  CA  . GLU A 1 143 ? 7.958   11.894  16.570  1.00 12.24 ? 143 GLU A CA  1 
ATOM   1170 C  C   . GLU A 1 143 ? 8.421   11.363  15.210  1.00 11.59 ? 143 GLU A C   1 
ATOM   1171 O  O   . GLU A 1 143 ? 9.630   11.034  14.985  1.00 12.61 ? 143 GLU A O   1 
ATOM   1172 C  CB  . GLU A 1 143 ? 7.102   10.861  17.291  1.00 13.62 ? 143 GLU A CB  1 
ATOM   1173 C  CG  . GLU A 1 143 ? 6.862   11.199  18.755  1.00 15.33 ? 143 GLU A CG  1 
ATOM   1174 C  CD  . GLU A 1 143 ? 5.814   12.268  19.084  1.00 17.10 ? 143 GLU A CD  1 
ATOM   1175 O  OE1 . GLU A 1 143 ? 5.112   12.747  18.183  1.00 15.20 ? 143 GLU A OE1 1 
ATOM   1176 O  OE2 . GLU A 1 143 ? 5.673   12.629  20.287  1.00 22.27 ? 143 GLU A OE2 1 
ATOM   1177 N  N   . ASP A 1 144 ? 7.523   11.259  14.233  1.00 11.77 ? 144 ASP A N   1 
ATOM   1178 C  CA  . ASP A 1 144 ? 7.932   10.726  12.932  1.00 11.17 ? 144 ASP A CA  1 
ATOM   1179 C  C   . ASP A 1 144 ? 8.812   11.712  12.142  1.00 11.37 ? 144 ASP A C   1 
ATOM   1180 O  O   . ASP A 1 144 ? 9.675   11.258  11.398  1.00 11.93 ? 144 ASP A O   1 
ATOM   1181 C  CB  . ASP A 1 144 ? 6.724   10.326  12.103  1.00 11.81 ? 144 ASP A CB  1 
ATOM   1182 C  CG  . ASP A 1 144 ? 6.231   8.925   12.427  1.00 13.15 ? 144 ASP A CG  1 
ATOM   1183 O  OD1 . ASP A 1 144 ? 7.000   8.124   13.055  1.00 14.63 ? 144 ASP A OD1 1 
ATOM   1184 O  OD2 . ASP A 1 144 ? 5.061   8.595   12.063  1.00 13.38 ? 144 ASP A OD2 1 
ATOM   1185 N  N   . MET A 1 145 ? 8.546   13.025  12.233  1.00 11.71 ? 145 MET A N   1 
ATOM   1186 C  CA  . MET A 1 145 ? 9.430   13.982  11.557  1.00 10.80 ? 145 MET A CA  1 
ATOM   1187 C  C   . MET A 1 145 ? 10.846  13.889  12.137  1.00 11.68 ? 145 MET A C   1 
ATOM   1188 O  O   . MET A 1 145 ? 11.787  14.101  11.358  1.00 12.29 ? 145 MET A O   1 
ATOM   1189 C  CB  . MET A 1 145 ? 8.895   15.403  11.681  1.00 10.73 ? 145 MET A CB  1 
ATOM   1190 C  CG  . MET A 1 145 ? 7.539   15.615  10.983  1.00 11.96 ? 145 MET A CG  1 
ATOM   1191 S  SD  . MET A 1 145 ? 7.455   15.189  9.238   1.00 14.00 ? 145 MET A SD  1 
ATOM   1192 C  CE  . MET A 1 145 ? 6.771   13.539  9.362   1.00 16.53 ? 145 MET A CE  1 
ATOM   1193 N  N   . THR A 1 146 ? 10.981  13.689  13.441  1.00 12.38 ? 146 THR A N   1 
ATOM   1194 C  CA  . THR A 1 146 ? 12.318  13.613  14.039  1.00 11.65 ? 146 THR A CA  1 
ATOM   1195 C  C   . THR A 1 146 ? 12.987  12.318  13.590  1.00 12.29 ? 146 THR A C   1 
ATOM   1196 O  O   . THR A 1 146 ? 14.183  12.340  13.360  1.00 12.66 ? 146 THR A O   1 
ATOM   1197 C  CB  . THR A 1 146 ? 12.237  13.728  15.557  1.00 11.99 ? 146 THR A CB  1 
ATOM   1198 O  OG1 . THR A 1 146 ? 11.562  14.954  15.878  1.00 12.62 ? 146 THR A OG1 1 
ATOM   1199 C  CG2 . THR A 1 146 ? 13.595  13.668  16.249  1.00 13.41 ? 146 THR A CG2 1 
ATOM   1200 N  N   . ARG A 1 147 ? 12.252  11.201  13.520  1.00 11.41 ? 147 ARG A N   1 
ATOM   1201 C  CA  . ARG A 1 147 ? 12.853  9.958   12.949  1.00 11.90 ? 147 ARG A CA  1 
ATOM   1202 C  C   . ARG A 1 147 ? 13.415  10.264  11.554  1.00 12.64 ? 147 ARG A C   1 
ATOM   1203 O  O   . ARG A 1 147 ? 14.554  9.880   11.231  1.00 12.56 ? 147 ARG A O   1 
ATOM   1204 C  CB  . ARG A 1 147 ? 11.804  8.852   12.836  1.00 13.00 ? 147 ARG A CB  1 
ATOM   1205 C  CG  . ARG A 1 147 ? 11.355  8.290   14.187  1.00 14.46 ? 147 ARG A CG  1 
ATOM   1206 C  CD  . ARG A 1 147 ? 10.314  7.233   13.920  1.00 17.24 ? 147 ARG A CD  1 
ATOM   1207 N  NE  . ARG A 1 147 ? 10.018  6.433   15.098  1.00 20.06 ? 147 ARG A NE  1 
ATOM   1208 C  CZ  . ARG A 1 147 ? 8.964   6.604   15.874  1.00 20.67 ? 147 ARG A CZ  1 
ATOM   1209 N  NH1 . ARG A 1 147 ? 8.023   7.473   15.570  1.00 19.47 ? 147 ARG A NH1 1 
ATOM   1210 N  NH2 . ARG A 1 147 ? 8.795   5.797   16.917  1.00 24.75 ? 147 ARG A NH2 1 
ATOM   1211 N  N   . LEU A 1 148 ? 12.638  10.955  10.718  1.00 11.53 ? 148 LEU A N   1 
ATOM   1212 C  CA  . LEU A 1 148 ? 13.058  11.263  9.343   1.00 12.72 ? 148 LEU A CA  1 
ATOM   1213 C  C   . LEU A 1 148 ? 14.338  12.138  9.343   1.00 12.50 ? 148 LEU A C   1 
ATOM   1214 O  O   . LEU A 1 148 ? 15.302  11.860  8.613   1.00 12.12 ? 148 LEU A O   1 
ATOM   1215 C  CB  . LEU A 1 148 ? 11.939  11.977  8.576   1.00 15.02 ? 148 LEU A CB  1 
ATOM   1216 C  CG  . LEU A 1 148 ? 12.399  12.345  7.160   1.00 16.84 ? 148 LEU A CG  1 
ATOM   1217 C  CD1 . LEU A 1 148 ? 11.515  11.773  6.081   1.00 19.21 ? 148 LEU A CD1 1 
ATOM   1218 C  CD2 . LEU A 1 148 ? 12.584  13.820  7.017   1.00 21.54 ? 148 LEU A CD2 1 
ATOM   1219 N  N   . THR A 1 149 ? 14.274  13.290  10.028  1.00 11.36 ? 149 THR A N   1 
ATOM   1220 C  CA  . THR A 1 149 ? 15.352  14.296  9.860   1.00 11.93 ? 149 THR A CA  1 
ATOM   1221 C  C   . THR A 1 149 ? 16.657  13.782  10.487  1.00 11.21 ? 149 THR A C   1 
ATOM   1222 O  O   . THR A 1 149 ? 17.745  14.067  9.948   1.00 13.74 ? 149 THR A O   1 
ATOM   1223 C  CB  . THR A 1 149 ? 14.920  15.666  10.353  1.00 11.67 ? 149 THR A CB  1 
ATOM   1224 O  OG1 . THR A 1 149 ? 14.650  15.634  11.757  1.00 13.75 ? 149 THR A OG1 1 
ATOM   1225 C  CG2 . THR A 1 149 ? 13.725  16.194  9.600   1.00 11.75 ? 149 THR A CG2 1 
ATOM   1226 N  N   . LEU A 1 150 ? 16.593  13.088  11.622  1.00 12.61 ? 150 LEU A N   1 
ATOM   1227 C  CA  . LEU A 1 150 ? 17.805  12.487  12.185  1.00 13.97 ? 150 LEU A CA  1 
ATOM   1228 C  C   . LEU A 1 150 ? 18.366  11.531  11.144  1.00 12.32 ? 150 LEU A C   1 
ATOM   1229 O  O   . LEU A 1 150 ? 19.568  11.512  10.920  1.00 13.41 ? 150 LEU A O   1 
ATOM   1230 C  CB  . LEU A 1 150 ? 17.485  11.699  13.446  1.00 15.49 ? 150 LEU A CB  1 
ATOM   1231 C  CG  . LEU A 1 150 ? 18.634  10.823  13.973  1.00 16.97 ? 150 LEU A CG  1 
ATOM   1232 C  CD1 . LEU A 1 150 ? 19.776  11.730  14.354  1.00 17.42 ? 150 LEU A CD1 1 
ATOM   1233 C  CD2 . LEU A 1 150 ? 18.186  9.923   15.084  1.00 17.66 ? 150 LEU A CD2 1 
ATOM   1234 N  N   . ASP A 1 151 ? 17.520  10.652  10.583  1.00 12.29 ? 151 ASP A N   1 
ATOM   1235 C  CA  . ASP A 1 151 ? 18.031  9.580   9.705   1.00 12.75 ? 151 ASP A CA  1 
ATOM   1236 C  C   . ASP A 1 151 ? 18.623  10.221  8.459   1.00 11.58 ? 151 ASP A C   1 
ATOM   1237 O  O   . ASP A 1 151 ? 19.632  9.701   7.944   1.00 11.77 ? 151 ASP A O   1 
ATOM   1238 C  CB  . ASP A 1 151 ? 16.953  8.538   9.403   1.00 14.16 ? 151 ASP A CB  1 
ATOM   1239 C  CG  . ASP A 1 151 ? 16.843  7.531   10.554  1.00 17.02 ? 151 ASP A CG  1 
ATOM   1240 O  OD1 . ASP A 1 151 ? 17.112  7.944   11.730  1.00 19.89 ? 151 ASP A OD1 1 
ATOM   1241 O  OD2 . ASP A 1 151 ? 16.310  6.463   10.305  1.00 22.10 ? 151 ASP A OD2 1 
ATOM   1242 N  N   . THR A 1 152 ? 17.995  11.283  7.937   1.00 11.04 ? 152 THR A N   1 
ATOM   1243 C  CA  . THR A 1 152 ? 18.547  11.928  6.733   1.00 11.75 ? 152 THR A CA  1 
ATOM   1244 C  C   . THR A 1 152 ? 19.963  12.460  6.989   1.00 11.88 ? 152 THR A C   1 
ATOM   1245 O  O   . THR A 1 152 ? 20.841  12.225  6.171   1.00 12.27 ? 152 THR A O   1 
ATOM   1246 C  CB  . THR A 1 152 ? 17.590  13.033  6.293   1.00 12.21 ? 152 THR A CB  1 
ATOM   1247 O  OG1 . THR A 1 152 ? 16.309  12.441  6.020   1.00 13.27 ? 152 THR A OG1 1 
ATOM   1248 C  CG2 . THR A 1 152 ? 18.125  13.748  5.064   1.00 12.96 ? 152 THR A CG2 1 
ATOM   1249 N  N   . ILE A 1 153 ? 20.174  13.181  8.077   1.00 11.97 ? 153 ILE A N   1 
ATOM   1250 C  CA  . ILE A 1 153 ? 21.539  13.728  8.293   1.00 13.95 ? 153 ILE A CA  1 
ATOM   1251 C  C   . ILE A 1 153 ? 22.502  12.590  8.607   1.00 13.23 ? 153 ILE A C   1 
ATOM   1252 O  O   . ILE A 1 153 ? 23.682  12.648  8.122   1.00 16.21 ? 153 ILE A O   1 
ATOM   1253 C  CB  . ILE A 1 153 ? 21.582  14.877  9.288   1.00 14.69 ? 153 ILE A CB  1 
ATOM   1254 C  CG1 . ILE A 1 153 ? 22.956  15.574  9.287   1.00 17.11 ? 153 ILE A CG1 1 
ATOM   1255 C  CG2 . ILE A 1 153 ? 21.193  14.448  10.671  1.00 16.80 ? 153 ILE A CG2 1 
ATOM   1256 C  CD1 . ILE A 1 153 ? 23.321  16.251  8.009   1.00 19.24 ? 153 ILE A CD1 1 
ATOM   1257 N  N   . GLY A 1 154 ? 22.056  11.526  9.272   1.00 12.76 ? 154 GLY A N   1 
ATOM   1258 C  CA  . GLY A 1 154 ? 22.938  10.385  9.495   1.00 12.54 ? 154 GLY A CA  1 
ATOM   1259 C  C   . GLY A 1 154 ? 23.441  9.815   8.196   1.00 13.08 ? 154 GLY A C   1 
ATOM   1260 O  O   . GLY A 1 154 ? 24.653  9.512   8.031   1.00 12.95 ? 154 GLY A O   1 
ATOM   1261 N  N   . LEU A 1 155 ? 22.524  9.640   7.273   1.00 12.23 ? 155 LEU A N   1 
ATOM   1262 C  CA  . LEU A 1 155 ? 22.873  8.930   6.040   1.00 13.92 ? 155 LEU A CA  1 
ATOM   1263 C  C   . LEU A 1 155 ? 23.647  9.857   5.115   1.00 16.93 ? 155 LEU A C   1 
ATOM   1264 O  O   . LEU A 1 155 ? 24.652  9.440   4.538   1.00 17.44 ? 155 LEU A O   1 
ATOM   1265 C  CB  . LEU A 1 155 ? 21.556  8.465   5.446   1.00 15.21 ? 155 LEU A CB  1 
ATOM   1266 C  CG  . LEU A 1 155 ? 21.650  7.604   4.200   1.00 16.70 ? 155 LEU A CG  1 
ATOM   1267 C  CD1 . LEU A 1 155 ? 22.511  6.351   4.385   1.00 15.75 ? 155 LEU A CD1 1 
ATOM   1268 C  CD2 . LEU A 1 155 ? 20.266  7.236   3.770   1.00 15.30 ? 155 LEU A CD2 1 
ATOM   1269 N  N   . CYS A 1 156 ? 23.158  11.079  4.907   1.00 17.73 ? 156 CYS A N   1 
ATOM   1270 C  CA  . CYS A 1 156 ? 23.841  12.033  4.012   1.00 21.84 ? 156 CYS A CA  1 
ATOM   1271 C  C   . CYS A 1 156 ? 25.156  12.465  4.620   1.00 22.69 ? 156 CYS A C   1 
ATOM   1272 O  O   . CYS A 1 156 ? 26.080  12.731  3.826   1.00 29.59 ? 156 CYS A O   1 
ATOM   1273 C  CB  . CYS A 1 156 ? 22.992  13.287  3.787   1.00 22.34 ? 156 CYS A CB  1 
ATOM   1274 S  SG  . CYS A 1 156 ? 21.505  12.942  2.868   1.00 22.46 ? 156 CYS A SG  1 
ATOM   1275 N  N   . GLY A 1 157 ? 25.234  12.601  5.932   1.00 20.14 ? 157 GLY A N   1 
ATOM   1276 C  CA  . GLY A 1 157 ? 26.364  13.147  6.711   1.00 22.03 ? 157 GLY A CA  1 
ATOM   1277 C  C   . GLY A 1 157 ? 27.509  12.151  6.819   1.00 26.05 ? 157 GLY A C   1 
ATOM   1278 O  O   . GLY A 1 157 ? 28.685  12.548  6.676   1.00 26.15 ? 157 GLY A O   1 
ATOM   1279 N  N   . PHE A 1 158 ? 27.247  10.878  7.132   1.00 20.03 ? 158 PHE A N   1 
ATOM   1280 C  CA  . PHE A 1 158 ? 28.353  9.923   7.393   1.00 21.23 ? 158 PHE A CA  1 
ATOM   1281 C  C   . PHE A 1 158 ? 27.977  8.494   7.013   1.00 17.80 ? 158 PHE A C   1 
ATOM   1282 O  O   . PHE A 1 158 ? 28.640  7.549   7.485   1.00 15.80 ? 158 PHE A O   1 
ATOM   1283 C  CB  . PHE A 1 158 ? 28.952  9.990   8.807   1.00 27.17 ? 158 PHE A CB  1 
ATOM   1284 C  CG  . PHE A 1 158 ? 28.010  10.007  9.968   1.00 34.14 ? 158 PHE A CG  1 
ATOM   1285 C  CD1 . PHE A 1 158 ? 27.208  11.114  10.205  1.00 38.16 ? 158 PHE A CD1 1 
ATOM   1286 C  CD2 . PHE A 1 158 ? 27.985  8.953   10.868  1.00 37.64 ? 158 PHE A CD2 1 
ATOM   1287 C  CE1 . PHE A 1 158 ? 26.378  11.134  11.312  1.00 42.66 ? 158 PHE A CE1 1 
ATOM   1288 C  CE2 . PHE A 1 158 ? 27.148  8.978   11.975  1.00 36.14 ? 158 PHE A CE2 1 
ATOM   1289 C  CZ  . PHE A 1 158 ? 26.333  10.057  12.182  1.00 37.15 ? 158 PHE A CZ  1 
ATOM   1290 N  N   . ASN A 1 159 ? 26.983  8.335   6.156   1.00 16.57 ? 159 ASN A N   1 
ATOM   1291 C  CA  . ASN A 1 159 ? 26.591  6.991   5.652   1.00 17.22 ? 159 ASN A CA  1 
ATOM   1292 C  C   . ASN A 1 159 ? 26.307  6.080   6.857   1.00 16.75 ? 159 ASN A C   1 
ATOM   1293 O  O   . ASN A 1 159 ? 26.704  4.899   6.829   1.00 17.98 ? 159 ASN A O   1 
ATOM   1294 C  CB  . ASN A 1 159 ? 27.650  6.406   4.724   1.00 19.57 ? 159 ASN A CB  1 
ATOM   1295 C  CG  . ASN A 1 159 ? 27.114  5.280   3.882   1.00 29.78 ? 159 ASN A CG  1 
ATOM   1296 O  OD1 . ASN A 1 159 ? 25.918  5.232   3.568   1.00 33.09 ? 159 ASN A OD1 1 
ATOM   1297 N  ND2 . ASN A 1 159 ? 27.981  4.337   3.557   1.00 34.29 ? 159 ASN A ND2 1 
ATOM   1298 N  N   . TYR A 1 160 ? 25.659  6.590   7.867   1.00 14.40 ? 160 TYR A N   1 
ATOM   1299 C  CA  . TYR A 1 160 ? 25.283  5.822   9.080   1.00 14.88 ? 160 TYR A CA  1 
ATOM   1300 C  C   . TYR A 1 160 ? 23.758  5.791   9.160   1.00 14.53 ? 160 TYR A C   1 
ATOM   1301 O  O   . TYR A 1 160 ? 23.084  6.847   9.061   1.00 14.39 ? 160 TYR A O   1 
ATOM   1302 C  CB  . TYR A 1 160 ? 25.826  6.447   10.358  1.00 15.58 ? 160 TYR A CB  1 
ATOM   1303 C  CG  . TYR A 1 160 ? 25.560  5.604   11.577  1.00 16.16 ? 160 TYR A CG  1 
ATOM   1304 C  CD1 . TYR A 1 160 ? 26.364  4.515   11.892  1.00 17.94 ? 160 TYR A CD1 1 
ATOM   1305 C  CD2 . TYR A 1 160 ? 24.484  5.847   12.390  1.00 16.98 ? 160 TYR A CD2 1 
ATOM   1306 C  CE1 . TYR A 1 160 ? 26.117  3.744   13.002  1.00 20.09 ? 160 TYR A CE1 1 
ATOM   1307 C  CE2 . TYR A 1 160 ? 24.218  5.072   13.510  1.00 18.65 ? 160 TYR A CE2 1 
ATOM   1308 C  CZ  . TYR A 1 160 ? 25.029  3.992   13.805  1.00 20.43 ? 160 TYR A CZ  1 
ATOM   1309 O  OH  . TYR A 1 160 ? 24.762  3.217   14.907  1.00 22.42 ? 160 TYR A OH  1 
ATOM   1310 N  N   . ARG A 1 161 ? 23.192  4.591   9.304   1.00 13.00 ? 161 ARG A N   1 
ATOM   1311 C  CA  . ARG A 1 161 ? 21.720  4.451   9.365   1.00 14.20 ? 161 ARG A CA  1 
ATOM   1312 C  C   . ARG A 1 161 ? 21.319  4.344   10.817  1.00 13.52 ? 161 ARG A C   1 
ATOM   1313 O  O   . ARG A 1 161 ? 21.578  3.318   11.512  1.00 13.85 ? 161 ARG A O   1 
ATOM   1314 C  CB  . ARG A 1 161 ? 21.291  3.268   8.509   1.00 14.32 ? 161 ARG A CB  1 
ATOM   1315 C  CG  . ARG A 1 161 ? 21.274  3.608   7.035   1.00 14.39 ? 161 ARG A CG  1 
ATOM   1316 C  CD  . ARG A 1 161 ? 20.787  2.452   6.208   1.00 14.91 ? 161 ARG A CD  1 
ATOM   1317 N  NE  . ARG A 1 161 ? 20.902  2.765   4.810   1.00 14.83 ? 161 ARG A NE  1 
ATOM   1318 C  CZ  . ARG A 1 161 ? 19.980  3.297   4.046   1.00 13.88 ? 161 ARG A CZ  1 
ATOM   1319 N  NH1 . ARG A 1 161 ? 18.787  3.523   4.542   1.00 14.38 ? 161 ARG A NH1 1 
ATOM   1320 N  NH2 . ARG A 1 161 ? 20.223  3.507   2.770   1.00 14.51 ? 161 ARG A NH2 1 
ATOM   1321 N  N   . PHE A 1 162 ? 20.685  5.367   11.359  1.00 12.82 ? 162 PHE A N   1 
ATOM   1322 C  CA  . PHE A 1 162 ? 20.093  5.298   12.702  1.00 13.12 ? 162 PHE A CA  1 
ATOM   1323 C  C   . PHE A 1 162 ? 18.871  4.363   12.743  1.00 12.49 ? 162 PHE A C   1 
ATOM   1324 O  O   . PHE A 1 162 ? 18.530  3.912   13.833  1.00 14.46 ? 162 PHE A O   1 
ATOM   1325 C  CB  . PHE A 1 162 ? 19.689  6.700   13.191  1.00 13.97 ? 162 PHE A CB  1 
ATOM   1326 C  CG  . PHE A 1 162 ? 20.873  7.502   13.666  1.00 13.35 ? 162 PHE A CG  1 
ATOM   1327 C  CD1 . PHE A 1 162 ? 21.438  7.273   14.911  1.00 14.90 ? 162 PHE A CD1 1 
ATOM   1328 C  CD2 . PHE A 1 162 ? 21.453  8.426   12.824  1.00 13.59 ? 162 PHE A CD2 1 
ATOM   1329 C  CE1 . PHE A 1 162 ? 22.550  7.983   15.334  1.00 16.40 ? 162 PHE A CE1 1 
ATOM   1330 C  CE2 . PHE A 1 162 ? 22.590  9.100   13.227  1.00 15.04 ? 162 PHE A CE2 1 
ATOM   1331 C  CZ  . PHE A 1 162 ? 23.117  8.867   14.478  1.00 15.85 ? 162 PHE A CZ  1 
ATOM   1332 N  N   . ASN A 1 163 ? 18.293  4.096   11.580  1.00 11.28 ? 163 ASN A N   1 
ATOM   1333 C  CA  . ASN A 1 163 ? 17.171  3.129   11.475  1.00 12.01 ? 163 ASN A CA  1 
ATOM   1334 C  C   . ASN A 1 163 ? 16.068  3.529   12.451  1.00 12.70 ? 163 ASN A C   1 
ATOM   1335 O  O   . ASN A 1 163 ? 15.457  2.652   13.103  1.00 12.50 ? 163 ASN A O   1 
ATOM   1336 C  CB  . ASN A 1 163 ? 17.658  1.686   11.644  1.00 11.11 ? 163 ASN A CB  1 
ATOM   1337 C  CG  . ASN A 1 163 ? 18.383  1.291   10.400  1.00 12.16 ? 163 ASN A CG  1 
ATOM   1338 O  OD1 . ASN A 1 163 ? 17.919  1.526   9.276   1.00 14.77 ? 163 ASN A OD1 1 
ATOM   1339 N  ND2 . ASN A 1 163 ? 19.559  0.718   10.549  1.00 12.96 ? 163 ASN A ND2 1 
ATOM   1340 N  N   . SER A 1 164 ? 15.705  4.806   12.470  1.00 11.60 ? 164 SER A N   1 
ATOM   1341 C  CA  . SER A 1 164 ? 14.744  5.358   13.433  1.00 13.44 ? 164 SER A CA  1 
ATOM   1342 C  C   . SER A 1 164 ? 13.334  4.799   13.211  1.00 12.52 ? 164 SER A C   1 
ATOM   1343 O  O   . SER A 1 164 ? 12.589  4.715   14.153  1.00 14.15 ? 164 SER A O   1 
ATOM   1344 C  CB  . SER A 1 164 ? 14.741  6.842   13.398  1.00 14.56 ? 164 SER A CB  1 
ATOM   1345 O  OG  . SER A 1 164 ? 16.024  7.320   13.795  1.00 15.96 ? 164 SER A OG  1 
ATOM   1346 N  N   . PHE A 1 165 ? 13.023  4.411   11.970  1.00 12.60 ? 165 PHE A N   1 
ATOM   1347 C  CA  . PHE A 1 165 ? 11.664  3.873   11.688  1.00 13.40 ? 165 PHE A CA  1 
ATOM   1348 C  C   . PHE A 1 165 ? 11.584  2.419   12.126  1.00 15.94 ? 165 PHE A C   1 
ATOM   1349 O  O   . PHE A 1 165 ? 10.459  1.882   12.070  1.00 18.35 ? 165 PHE A O   1 
ATOM   1350 C  CB  . PHE A 1 165 ? 11.293  4.040   10.222  1.00 14.36 ? 165 PHE A CB  1 
ATOM   1351 C  CG  . PHE A 1 165 ? 11.020  5.480   9.854   1.00 14.29 ? 165 PHE A CG  1 
ATOM   1352 C  CD1 . PHE A 1 165 ? 9.943   6.121   10.424  1.00 15.90 ? 165 PHE A CD1 1 
ATOM   1353 C  CD2 . PHE A 1 165 ? 11.836  6.197   8.997   1.00 14.04 ? 165 PHE A CD2 1 
ATOM   1354 C  CE1 . PHE A 1 165 ? 9.643   7.434   10.094  1.00 16.67 ? 165 PHE A CE1 1 
ATOM   1355 C  CE2 . PHE A 1 165 ? 11.571  7.521   8.714   1.00 15.22 ? 165 PHE A CE2 1 
ATOM   1356 C  CZ  . PHE A 1 165 ? 10.474  8.136   9.274   1.00 15.72 ? 165 PHE A CZ  1 
ATOM   1357 N  N   . TYR A 1 166 ? 12.637  1.807   12.633  1.00 13.35 ? 166 TYR A N   1 
ATOM   1358 C  CA  . TYR A 1 166 ? 12.666  0.399   13.100  1.00 14.64 ? 166 TYR A CA  1 
ATOM   1359 C  C   . TYR A 1 166 ? 12.612  0.361   14.621  1.00 16.96 ? 166 TYR A C   1 
ATOM   1360 O  O   . TYR A 1 166 ? 12.742  -0.725  15.166  1.00 20.36 ? 166 TYR A O   1 
ATOM   1361 C  CB  . TYR A 1 166 ? 13.871  -0.340  12.579  1.00 13.26 ? 166 TYR A CB  1 
ATOM   1362 C  CG  . TYR A 1 166 ? 13.890  -0.532  11.090  1.00 12.42 ? 166 TYR A CG  1 
ATOM   1363 C  CD1 . TYR A 1 166 ? 14.401  0.404   10.207  1.00 13.60 ? 166 TYR A CD1 1 
ATOM   1364 C  CD2 . TYR A 1 166 ? 13.324  -1.666  10.537  1.00 12.88 ? 166 TYR A CD2 1 
ATOM   1365 C  CE1 . TYR A 1 166 ? 14.363  0.202   8.844   1.00 12.58 ? 166 TYR A CE1 1 
ATOM   1366 C  CE2 . TYR A 1 166 ? 13.275  -1.876  9.176   1.00 12.61 ? 166 TYR A CE2 1 
ATOM   1367 C  CZ  . TYR A 1 166 ? 13.781  -0.927  8.299   1.00 12.28 ? 166 TYR A CZ  1 
ATOM   1368 O  OH  . TYR A 1 166 ? 13.761  -1.112  6.951   1.00 12.82 ? 166 TYR A OH  1 
ATOM   1369 N  N   . ARG A 1 167 ? 12.391  1.506   15.269  1.00 19.36 ? 167 ARG A N   1 
ATOM   1370 C  CA  . ARG A 1 167 ? 12.560  1.664   16.732  1.00 23.35 ? 167 ARG A CA  1 
ATOM   1371 C  C   . ARG A 1 167 ? 11.411  2.439   17.346  1.00 22.97 ? 167 ARG A C   1 
ATOM   1372 O  O   . ARG A 1 167 ? 10.915  3.368   16.708  1.00 23.42 ? 167 ARG A O   1 
ATOM   1373 C  CB  . ARG A 1 167 ? 13.798  2.510   17.029  1.00 24.35 ? 167 ARG A CB  1 
ATOM   1374 C  CG  . ARG A 1 167 ? 15.076  1.936   16.489  1.00 25.28 ? 167 ARG A CG  1 
ATOM   1375 C  CD  . ARG A 1 167 ? 16.155  2.943   16.823  1.00 25.57 ? 167 ARG A CD  1 
ATOM   1376 N  NE  . ARG A 1 167 ? 17.369  2.597   16.122  1.00 25.65 ? 167 ARG A NE  1 
ATOM   1377 C  CZ  . ARG A 1 167 ? 18.345  1.863   16.636  1.00 29.43 ? 167 ARG A CZ  1 
ATOM   1378 N  NH1 . ARG A 1 167 ? 18.229  1.360   17.862  1.00 27.79 ? 167 ARG A NH1 1 
ATOM   1379 N  NH2 . ARG A 1 167 ? 19.430  1.636   15.926  1.00 27.70 ? 167 ARG A NH2 1 
ATOM   1380 N  N   . ASP A 1 168 ? 11.055  2.081   18.579  1.00 28.11 ? 168 ASP A N   1 
ATOM   1381 C  CA  . ASP A 1 168 ? 10.277  2.956   19.497  1.00 35.59 ? 168 ASP A CA  1 
ATOM   1382 C  C   . ASP A 1 168 ? 11.234  3.730   20.399  1.00 37.10 ? 168 ASP A C   1 
ATOM   1383 O  O   . ASP A 1 168 ? 11.031  4.929   20.568  1.00 54.65 ? 168 ASP A O   1 
ATOM   1384 C  CB  . ASP A 1 168 ? 9.360   2.140   20.395  1.00 39.17 ? 168 ASP A CB  1 
ATOM   1385 C  CG  . ASP A 1 168 ? 8.209   1.557   19.622  1.00 41.71 ? 168 ASP A CG  1 
ATOM   1386 O  OD1 . ASP A 1 168 ? 7.490   2.366   18.996  1.00 49.49 ? 168 ASP A OD1 1 
ATOM   1387 O  OD2 . ASP A 1 168 ? 8.065   0.309   19.641  1.00 39.03 ? 168 ASP A OD2 1 
ATOM   1388 N  N   . GLN A 1 169 ? 12.211  3.033   20.973  1.00 42.74 ? 169 GLN A N   1 
ATOM   1389 C  CA  . GLN A 1 169 ? 13.185  3.593   21.946  1.00 47.71 ? 169 GLN A CA  1 
ATOM   1390 C  C   . GLN A 1 169 ? 14.310  4.221   21.144  1.00 43.94 ? 169 GLN A C   1 
ATOM   1391 O  O   . GLN A 1 169 ? 14.811  3.599   20.208  1.00 38.46 ? 169 GLN A O   1 
ATOM   1392 C  CB  . GLN A 1 169 ? 13.773  2.514   22.858  1.00 56.28 ? 169 GLN A CB  1 
ATOM   1393 C  CG  . GLN A 1 169 ? 12.804  2.001   23.922  1.00 68.20 ? 169 GLN A CG  1 
ATOM   1394 C  CD  . GLN A 1 169 ? 11.857  0.939   23.408  1.00 76.72 ? 169 GLN A CD  1 
ATOM   1395 O  OE1 . GLN A 1 169 ? 12.235  0.074   22.620  1.00 83.77 ? 169 GLN A OE1 1 
ATOM   1396 N  NE2 . GLN A 1 169 ? 10.615  0.984   23.869  1.00 77.58 ? 169 GLN A NE2 1 
ATOM   1397 N  N   . PRO A 1 170 ? 14.792  5.426   21.511  1.00 39.49 ? 170 PRO A N   1 
ATOM   1398 C  CA  . PRO A 1 170 ? 15.800  6.083   20.697  1.00 38.37 ? 170 PRO A CA  1 
ATOM   1399 C  C   . PRO A 1 170 ? 17.051  5.203   20.661  1.00 28.84 ? 170 PRO A C   1 
ATOM   1400 O  O   . PRO A 1 170 ? 17.337  4.458   21.568  1.00 31.59 ? 170 PRO A O   1 
ATOM   1401 C  CB  . PRO A 1 170 ? 16.013  7.440   21.401  1.00 40.63 ? 170 PRO A CB  1 
ATOM   1402 C  CG  . PRO A 1 170 ? 14.778  7.604   22.288  1.00 41.67 ? 170 PRO A CG  1 
ATOM   1403 C  CD  . PRO A 1 170 ? 14.457  6.192   22.720  1.00 40.93 ? 170 PRO A CD  1 
ATOM   1404 N  N   . HIS A 1 171 ? 17.825  5.352   19.590  1.00 31.44 ? 171 HIS A N   1 
ATOM   1405 C  CA  . HIS A 1 171 ? 19.231  4.910   19.511  1.00 28.51 ? 171 HIS A CA  1 
ATOM   1406 C  C   . HIS A 1 171 ? 19.948  5.399   20.766  1.00 32.68 ? 171 HIS A C   1 
ATOM   1407 O  O   . HIS A 1 171 ? 19.699  6.523   21.213  1.00 31.48 ? 171 HIS A O   1 
ATOM   1408 C  CB  . HIS A 1 171 ? 19.835  5.473   18.221  1.00 26.67 ? 171 HIS A CB  1 
ATOM   1409 C  CG  . HIS A 1 171 ? 21.190  4.961   17.872  1.00 26.89 ? 171 HIS A CG  1 
ATOM   1410 N  ND1 . HIS A 1 171 ? 22.323  5.272   18.577  1.00 28.74 ? 171 HIS A ND1 1 
ATOM   1411 C  CD2 . HIS A 1 171 ? 21.594  4.203   16.828  1.00 25.76 ? 171 HIS A CD2 1 
ATOM   1412 C  CE1 . HIS A 1 171 ? 23.372  4.710   18.016  1.00 32.19 ? 171 HIS A CE1 1 
ATOM   1413 N  NE2 . HIS A 1 171 ? 22.942  4.049   16.930  1.00 26.82 ? 171 HIS A NE2 1 
ATOM   1414 N  N   . PRO A 1 172 ? 20.811  4.590   21.428  1.00 30.81 ? 172 PRO A N   1 
ATOM   1415 C  CA  . PRO A 1 172 ? 21.526  5.045   22.623  1.00 33.20 ? 172 PRO A CA  1 
ATOM   1416 C  C   . PRO A 1 172 ? 22.324  6.350   22.448  1.00 30.72 ? 172 PRO A C   1 
ATOM   1417 O  O   . PRO A 1 172 ? 22.395  7.146   23.393  1.00 28.84 ? 172 PRO A O   1 
ATOM   1418 C  CB  . PRO A 1 172 ? 22.512  3.907   22.966  1.00 34.12 ? 172 PRO A CB  1 
ATOM   1419 C  CG  . PRO A 1 172 ? 22.494  3.014   21.737  1.00 34.50 ? 172 PRO A CG  1 
ATOM   1420 C  CD  . PRO A 1 172 ? 21.136  3.192   21.090  1.00 32.18 ? 172 PRO A CD  1 
ATOM   1421 N  N   . PHE A 1 173 ? 22.886  6.592   21.260  1.00 27.43 ? 173 PHE A N   1 
ATOM   1422 C  CA  . PHE A 1 173 ? 23.574  7.870   20.940  1.00 23.34 ? 173 PHE A CA  1 
ATOM   1423 C  C   . PHE A 1 173 ? 22.593  9.032   21.159  1.00 20.64 ? 173 PHE A C   1 
ATOM   1424 O  O   . PHE A 1 173 ? 22.975  10.053  21.808  1.00 18.56 ? 173 PHE A O   1 
ATOM   1425 C  CB  . PHE A 1 173 ? 24.140  7.927   19.518  1.00 25.50 ? 173 PHE A CB  1 
ATOM   1426 C  CG  . PHE A 1 173 ? 24.726  9.273   19.192  1.00 24.69 ? 173 PHE A CG  1 
ATOM   1427 C  CD1 . PHE A 1 173 ? 23.933  10.297  18.679  1.00 25.16 ? 173 PHE A CD1 1 
ATOM   1428 C  CD2 . PHE A 1 173 ? 26.061  9.557   19.411  1.00 24.34 ? 173 PHE A CD2 1 
ATOM   1429 C  CE1 . PHE A 1 173 ? 24.456  11.562  18.448  1.00 28.58 ? 173 PHE A CE1 1 
ATOM   1430 C  CE2 . PHE A 1 173 ? 26.590  10.811  19.159  1.00 26.33 ? 173 PHE A CE2 1 
ATOM   1431 C  CZ  . PHE A 1 173 ? 25.791  11.824  18.681  1.00 28.56 ? 173 PHE A CZ  1 
ATOM   1432 N  N   . ILE A 1 174 ? 21.352  8.854   20.703  1.00 19.86 ? 174 ILE A N   1 
ATOM   1433 C  CA  . ILE A 1 174 ? 20.321  9.919   20.753  1.00 20.11 ? 174 ILE A CA  1 
ATOM   1434 C  C   . ILE A 1 174 ? 19.832  10.081  22.190  1.00 21.14 ? 174 ILE A C   1 
ATOM   1435 O  O   . ILE A 1 174 ? 19.642  11.212  22.654  1.00 21.12 ? 174 ILE A O   1 
ATOM   1436 C  CB  . ILE A 1 174 ? 19.196  9.625   19.750  1.00 21.27 ? 174 ILE A CB  1 
ATOM   1437 C  CG1 . ILE A 1 174 ? 19.751  9.598   18.322  1.00 22.17 ? 174 ILE A CG1 1 
ATOM   1438 C  CG2 . ILE A 1 174 ? 18.040  10.559  19.917  1.00 20.51 ? 174 ILE A CG2 1 
ATOM   1439 C  CD1 . ILE A 1 174 ? 20.415  10.906  17.888  1.00 22.51 ? 174 ILE A CD1 1 
ATOM   1440 N  N   . THR A 1 175 ? 19.696  8.987   22.934  1.00 20.12 ? 175 THR A N   1 
ATOM   1441 C  CA  . THR A 1 175 ? 19.359  9.118   24.367  1.00 21.17 ? 175 THR A CA  1 
ATOM   1442 C  C   . THR A 1 175 ? 20.341  10.068  25.048  1.00 18.56 ? 175 THR A C   1 
ATOM   1443 O  O   . THR A 1 175 ? 19.906  10.980  25.775  1.00 21.01 ? 175 THR A O   1 
ATOM   1444 C  CB  . THR A 1 175 ? 19.353  7.737   25.020  1.00 23.44 ? 175 THR A CB  1 
ATOM   1445 O  OG1 . THR A 1 175 ? 18.212  7.108   24.433  1.00 26.91 ? 175 THR A OG1 1 
ATOM   1446 C  CG2 . THR A 1 175 ? 19.261  7.857   26.525  1.00 24.96 ? 175 THR A CG2 1 
ATOM   1447 N  N   . SER A 1 176 ? 21.639  9.847   24.843  1.00 18.42 ? 176 SER A N   1 
ATOM   1448 C  CA  . SER A 1 176 ? 22.721  10.639  25.456  1.00 17.83 ? 176 SER A CA  1 
ATOM   1449 C  C   . SER A 1 176 ? 22.730  12.079  24.914  1.00 17.34 ? 176 SER A C   1 
ATOM   1450 O  O   . SER A 1 176 ? 22.899  13.006  25.693  1.00 16.74 ? 176 SER A O   1 
ATOM   1451 C  CB  . SER A 1 176 ? 24.086  10.008  25.315  1.00 21.08 ? 176 SER A CB  1 
ATOM   1452 O  OG  . SER A 1 176 ? 24.158  8.868   26.201  1.00 22.41 ? 176 SER A OG  1 
ATOM   1453 N  N   . MET A 1 177 ? 22.561  12.257  23.611  1.00 17.30 ? 177 MET A N   1 
ATOM   1454 C  CA  . MET A 1 177 ? 22.555  13.626  23.035  1.00 15.79 ? 177 MET A CA  1 
ATOM   1455 C  C   . MET A 1 177 ? 21.381  14.438  23.601  1.00 15.93 ? 177 MET A C   1 
ATOM   1456 O  O   . MET A 1 177 ? 21.547  15.596  23.990  1.00 15.91 ? 177 MET A O   1 
ATOM   1457 C  CB  . MET A 1 177 ? 22.421  13.539  21.523  1.00 17.53 ? 177 MET A CB  1 
ATOM   1458 C  CG  . MET A 1 177 ? 22.636  14.863  20.830  1.00 16.70 ? 177 MET A CG  1 
ATOM   1459 S  SD  . MET A 1 177 ? 22.224  14.764  19.033  1.00 21.48 ? 177 MET A SD  1 
ATOM   1460 C  CE  . MET A 1 177 ? 20.438  14.687  19.136  1.00 23.93 ? 177 MET A CE  1 
ATOM   1461 N  N   . VAL A 1 178 ? 20.178  13.852  23.659  1.00 15.83 ? 178 VAL A N   1 
ATOM   1462 C  CA  . VAL A 1 178 ? 18.966  14.562  24.138  1.00 15.97 ? 178 VAL A CA  1 
ATOM   1463 C  C   . VAL A 1 178 ? 19.164  14.935  25.603  1.00 15.68 ? 178 VAL A C   1 
ATOM   1464 O  O   . VAL A 1 178 ? 18.781  16.019  25.997  1.00 16.82 ? 178 VAL A O   1 
ATOM   1465 C  CB  . VAL A 1 178 ? 17.707  13.715  23.917  1.00 17.64 ? 178 VAL A CB  1 
ATOM   1466 C  CG1 . VAL A 1 178 ? 16.495  14.255  24.670  1.00 17.70 ? 178 VAL A CG1 1 
ATOM   1467 C  CG2 . VAL A 1 178 ? 17.446  13.632  22.423  1.00 18.79 ? 178 VAL A CG2 1 
ATOM   1468 N  N   . ARG A 1 179 ? 19.734  14.015  26.389  1.00 16.19 ? 179 ARG A N   1 
ATOM   1469 C  CA  . ARG A 1 179 ? 19.924  14.262  27.820  1.00 16.71 ? 179 ARG A CA  1 
ATOM   1470 C  C   . ARG A 1 179 ? 21.023  15.296  28.039  1.00 17.73 ? 179 ARG A C   1 
ATOM   1471 O  O   . ARG A 1 179 ? 20.901  16.072  28.981  1.00 17.47 ? 179 ARG A O   1 
ATOM   1472 C  CB  . ARG A 1 179 ? 20.203  12.935  28.526  1.00 20.09 ? 179 ARG A CB  1 
ATOM   1473 C  CG  . ARG A 1 179 ? 20.125  13.006  30.042  1.00 20.74 ? 179 ARG A CG  1 
ATOM   1474 C  CD  . ARG A 1 179 ? 19.950  11.619  30.617  1.00 20.32 ? 179 ARG A CD  1 
ATOM   1475 N  NE  . ARG A 1 179 ? 20.963  10.697  30.125  1.00 19.97 ? 179 ARG A NE  1 
ATOM   1476 C  CZ  . ARG A 1 179 ? 20.776  9.380   29.946  1.00 22.32 ? 179 ARG A CZ  1 
ATOM   1477 N  NH1 . ARG A 1 179 ? 19.617  8.811   30.251  1.00 25.17 ? 179 ARG A NH1 1 
ATOM   1478 N  NH2 . ARG A 1 179 ? 21.730  8.633   29.418  1.00 24.24 ? 179 ARG A NH2 1 
ATOM   1479 N  N   . ALA A 1 180 ? 22.053  15.287  27.211  1.00 16.85 ? 180 ALA A N   1 
ATOM   1480 C  CA  . ALA A 1 180 ? 23.131  16.304  27.296  1.00 17.09 ? 180 ALA A CA  1 
ATOM   1481 C  C   . ALA A 1 180 ? 22.575  17.707  26.950  1.00 17.38 ? 180 ALA A C   1 
ATOM   1482 O  O   . ALA A 1 180 ? 22.889  18.686  27.640  1.00 16.84 ? 180 ALA A O   1 
ATOM   1483 C  CB  . ALA A 1 180 ? 24.259  15.950  26.382  1.00 17.63 ? 180 ALA A CB  1 
ATOM   1484 N  N   . LEU A 1 181 ? 21.769  17.786  25.893  1.00 16.84 ? 181 LEU A N   1 
ATOM   1485 C  CA  . LEU A 1 181 ? 21.096  19.057  25.501  1.00 16.78 ? 181 LEU A CA  1 
ATOM   1486 C  C   . LEU A 1 181 ? 20.210  19.527  26.656  1.00 19.36 ? 181 LEU A C   1 
ATOM   1487 O  O   . LEU A 1 181 ? 20.244  20.721  26.963  1.00 18.44 ? 181 LEU A O   1 
ATOM   1488 C  CB  . LEU A 1 181 ? 20.305  18.879  24.205  1.00 16.15 ? 181 LEU A CB  1 
ATOM   1489 C  CG  . LEU A 1 181 ? 21.109  18.828  22.890  1.00 17.70 ? 181 LEU A CG  1 
ATOM   1490 C  CD1 . LEU A 1 181 ? 20.284  18.271  21.749  1.00 19.01 ? 181 LEU A CD1 1 
ATOM   1491 C  CD2 . LEU A 1 181 ? 21.674  20.205  22.535  1.00 17.41 ? 181 LEU A CD2 1 
ATOM   1492 N  N   . ASP A 1 182 ? 19.452  18.624  27.294  1.00 16.79 ? 182 ASP A N   1 
ATOM   1493 C  CA  . ASP A 1 182 ? 18.531  19.018  28.382  1.00 18.64 ? 182 ASP A CA  1 
ATOM   1494 C  C   . ASP A 1 182 ? 19.340  19.592  29.540  1.00 18.47 ? 182 ASP A C   1 
ATOM   1495 O  O   . ASP A 1 182 ? 18.950  20.633  30.100  1.00 20.04 ? 182 ASP A O   1 
ATOM   1496 C  CB  . ASP A 1 182 ? 17.715  17.796  28.800  1.00 21.00 ? 182 ASP A CB  1 
ATOM   1497 C  CG  . ASP A 1 182 ? 16.698  18.114  29.870  1.00 26.93 ? 182 ASP A CG  1 
ATOM   1498 O  OD1 . ASP A 1 182 ? 15.918  19.076  29.690  1.00 28.49 ? 182 ASP A OD1 1 
ATOM   1499 O  OD2 . ASP A 1 182 ? 16.756  17.442  30.912  1.00 30.79 ? 182 ASP A OD2 1 
ATOM   1500 N  N   . GLU A 1 183 ? 20.448  18.959  29.892  1.00 17.03 ? 183 GLU A N   1 
ATOM   1501 C  CA  . GLU A 1 183 ? 21.313  19.449  31.000  1.00 19.77 ? 183 GLU A CA  1 
ATOM   1502 C  C   . GLU A 1 183 ? 21.895  20.821  30.627  1.00 21.24 ? 183 GLU A C   1 
ATOM   1503 O  O   . GLU A 1 183 ? 21.833  21.738  31.420  1.00 20.74 ? 183 GLU A O   1 
ATOM   1504 C  CB  . GLU A 1 183 ? 22.421  18.449  31.296  1.00 19.71 ? 183 GLU A CB  1 
ATOM   1505 C  CG  . GLU A 1 183 ? 23.432  18.961  32.319  1.00 21.45 ? 183 GLU A CG  1 
ATOM   1506 C  CD  . GLU A 1 183 ? 22.964  19.132  33.756  1.00 25.42 ? 183 GLU A CD  1 
ATOM   1507 O  OE1 . GLU A 1 183 ? 21.812  18.743  34.074  1.00 26.40 ? 183 GLU A OE1 1 
ATOM   1508 O  OE2 . GLU A 1 183 ? 23.760  19.661  34.538  1.00 27.11 ? 183 GLU A OE2 1 
ATOM   1509 N  N   . ALA A 1 184 ? 22.354  21.009  29.388  1.00 21.19 ? 184 ALA A N   1 
ATOM   1510 C  CA  . ALA A 1 184 ? 22.920  22.310  28.973  1.00 21.50 ? 184 ALA A CA  1 
ATOM   1511 C  C   . ALA A 1 184 ? 21.886  23.413  29.095  1.00 22.94 ? 184 ALA A C   1 
ATOM   1512 O  O   . ALA A 1 184 ? 22.270  24.558  29.474  1.00 22.19 ? 184 ALA A O   1 
ATOM   1513 C  CB  . ALA A 1 184 ? 23.467  22.250  27.552  1.00 19.90 ? 184 ALA A CB  1 
ATOM   1514 N  N   . MET A 1 185 ? 20.641  23.118  28.725  1.00 22.01 ? 185 MET A N   1 
ATOM   1515 C  CA  . MET A 1 185 ? 19.593  24.175  28.713  1.00 25.20 ? 185 MET A CA  1 
ATOM   1516 C  C   . MET A 1 185 ? 19.161  24.506  30.149  1.00 26.79 ? 185 MET A C   1 
ATOM   1517 O  O   . MET A 1 185 ? 18.613  25.606  30.351  1.00 25.89 ? 185 MET A O   1 
ATOM   1518 C  CB  . MET A 1 185 ? 18.350  23.715  27.969  1.00 32.05 ? 185 MET A CB  1 
ATOM   1519 C  CG  . MET A 1 185 ? 18.664  22.802  26.873  1.00 39.32 ? 185 MET A CG  1 
ATOM   1520 S  SD  . MET A 1 185 ? 17.953  23.366  25.392  1.00 39.34 ? 185 MET A SD  1 
ATOM   1521 C  CE  . MET A 1 185 ? 19.184  24.570  24.965  1.00 26.63 ? 185 MET A CE  1 
ATOM   1522 N  N   . ASN A 1 186 ? 19.280  23.558  31.052  1.00 25.14 ? 186 ASN A N   1 
ATOM   1523 C  CA  . ASN A 1 186 ? 18.813  23.733  32.456  1.00 27.67 ? 186 ASN A CA  1 
ATOM   1524 C  C   . ASN A 1 186 ? 19.879  24.423  33.315  1.00 29.71 ? 186 ASN A C   1 
ATOM   1525 O  O   . ASN A 1 186 ? 19.503  25.141  34.289  1.00 25.99 ? 186 ASN A O   1 
ATOM   1526 C  CB  . ASN A 1 186 ? 18.376  22.403  33.074  1.00 32.61 ? 186 ASN A CB  1 
ATOM   1527 C  CG  . ASN A 1 186 ? 16.934  22.059  32.791  1.00 40.29 ? 186 ASN A CG  1 
ATOM   1528 O  OD1 . ASN A 1 186 ? 16.078  22.937  32.684  1.00 48.09 ? 186 ASN A OD1 1 
ATOM   1529 N  ND2 . ASN A 1 186 ? 16.656  20.769  32.686  1.00 48.74 ? 186 ASN A ND2 1 
ATOM   1530 N  N   . LYS A 1 187 ? 21.170  24.249  33.029  1.00 25.46 ? 187 LYS A N   1 
ATOM   1531 C  CA  . LYS A 1 187 ? 22.235  24.728  33.939  1.00 26.07 ? 187 LYS A CA  1 
ATOM   1532 C  C   . LYS A 1 187 ? 22.108  26.239  34.193  1.00 26.60 ? 187 LYS A C   1 
ATOM   1533 O  O   . LYS A 1 187 ? 22.362  26.647  35.313  1.00 29.11 ? 187 LYS A O   1 
ATOM   1534 C  CB  . LYS A 1 187 ? 23.631  24.423  33.401  1.00 26.93 ? 187 LYS A CB  1 
ATOM   1535 C  CG  . LYS A 1 187 ? 24.148  23.002  33.493  1.00 26.66 ? 187 LYS A CG  1 
ATOM   1536 C  CD  . LYS A 1 187 ? 25.534  22.897  32.858  1.00 29.32 ? 187 LYS A CD  1 
ATOM   1537 C  CE  . LYS A 1 187 ? 26.110  21.504  32.729  1.00 29.11 ? 187 LYS A CE  1 
ATOM   1538 N  NZ  . LYS A 1 187 ? 26.196  20.797  34.026  1.00 32.72 ? 187 LYS A NZ  1 
ATOM   1539 N  N   . PRO A 1 188 ? 21.796  27.116  33.215  1.00 25.83 ? 188 PRO A N   1 
ATOM   1540 C  CA  . PRO A 1 188 ? 21.794  28.566  33.477  1.00 25.26 ? 188 PRO A CA  1 
ATOM   1541 C  C   . PRO A 1 188 ? 20.742  29.077  34.478  1.00 29.94 ? 188 PRO A C   1 
ATOM   1542 O  O   . PRO A 1 188 ? 21.093  30.013  35.204  1.00 28.18 ? 188 PRO A O   1 
ATOM   1543 C  CB  . PRO A 1 188 ? 21.535  29.194  32.102  1.00 25.83 ? 188 PRO A CB  1 
ATOM   1544 C  CG  . PRO A 1 188 ? 21.970  28.115  31.130  1.00 24.71 ? 188 PRO A CG  1 
ATOM   1545 C  CD  . PRO A 1 188 ? 21.526  26.832  31.805  1.00 24.51 ? 188 PRO A CD  1 
ATOM   1546 N  N   . GLN A 1 189 ? 19.541  28.475  34.512  1.00 31.10 ? 189 GLN A N   1 
ATOM   1547 C  CA  . GLN A 1 189 ? 18.411  28.910  35.393  1.00 34.51 ? 189 GLN A CA  1 
ATOM   1548 C  C   . GLN A 1 189 ? 18.728  28.553  36.853  1.00 31.80 ? 189 GLN A C   1 
ATOM   1549 O  O   . GLN A 1 189 ? 17.967  29.006  37.757  1.00 33.39 ? 189 GLN A O   1 
ATOM   1550 C  CB  . GLN A 1 189 ? 17.071  28.307  34.952  1.00 36.62 ? 189 GLN A CB  1 
ATOM   1551 C  CG  . GLN A 1 189 ? 16.829  26.896  35.479  1.00 42.34 ? 189 GLN A CG  1 
ATOM   1552 C  CD  . GLN A 1 189 ? 15.626  26.152  34.926  1.00 48.09 ? 189 GLN A CD  1 
ATOM   1553 O  OE1 . GLN A 1 189 ? 14.627  25.941  35.626  1.00 47.09 ? 189 GLN A OE1 1 
ATOM   1554 N  NE2 . GLN A 1 189 ? 15.728  25.691  33.686  1.00 42.28 ? 189 GLN A NE2 1 
ATOM   1555 N  N   . ARG A 1 190 ? 19.769  27.750  37.104  1.00 29.88 ? 190 ARG A N   1 
ATOM   1556 C  CA  . ARG A 1 190 ? 20.231  27.361  38.472  1.00 31.27 ? 190 ARG A CA  1 
ATOM   1557 C  C   . ARG A 1 190 ? 20.981  28.506  39.167  1.00 41.28 ? 190 ARG A C   1 
ATOM   1558 O  O   . ARG A 1 190 ? 22.068  28.909  38.679  1.00 39.74 ? 190 ARG A O   1 
ATOM   1559 C  CB  . ARG A 1 190 ? 21.183  26.164  38.435  1.00 33.11 ? 190 ARG A CB  1 
ATOM   1560 C  CG  . ARG A 1 190 ? 20.535  24.888  37.920  1.00 31.62 ? 190 ARG A CG  1 
ATOM   1561 C  CD  . ARG A 1 190 ? 21.483  23.711  37.756  1.00 30.40 ? 190 ARG A CD  1 
ATOM   1562 N  NE  . ARG A 1 190 ? 20.798  22.656  36.983  1.00 28.13 ? 190 ARG A NE  1 
ATOM   1563 C  CZ  . ARG A 1 190 ? 21.379  21.561  36.468  1.00 25.72 ? 190 ARG A CZ  1 
ATOM   1564 N  NH1 . ARG A 1 190 ? 22.665  21.337  36.644  1.00 26.29 ? 190 ARG A NH1 1 
ATOM   1565 N  NH2 . ARG A 1 190 ? 20.658  20.684  35.792  1.00 26.23 ? 190 ARG A NH2 1 
ATOM   1566 N  N   . ALA A 1 191 ? 20.476  28.955  40.317  1.00 50.48 ? 191 ALA A N   1 
ATOM   1567 C  CA  . ALA A 1 191 ? 21.097  30.044  41.112  1.00 54.67 ? 191 ALA A CA  1 
ATOM   1568 C  C   . ALA A 1 191 ? 22.352  29.520  41.830  1.00 53.69 ? 191 ALA A C   1 
ATOM   1569 O  O   . ALA A 1 191 ? 23.351  30.247  41.838  1.00 55.87 ? 191 ALA A O   1 
ATOM   1570 C  CB  . ALA A 1 191 ? 20.091  30.632  42.068  1.00 53.88 ? 191 ALA A CB  1 
ATOM   1571 N  N   . ASN A 1 192 ? 22.320  28.303  42.389  1.00 51.42 ? 192 ASN A N   1 
ATOM   1572 C  CA  . ASN A 1 192 ? 23.504  27.664  43.029  1.00 52.89 ? 192 ASN A CA  1 
ATOM   1573 C  C   . ASN A 1 192 ? 23.886  26.407  42.253  1.00 51.16 ? 192 ASN A C   1 
ATOM   1574 O  O   . ASN A 1 192 ? 23.505  25.306  42.644  1.00 41.36 ? 192 ASN A O   1 
ATOM   1575 C  CB  . ASN A 1 192 ? 23.272  27.311  44.499  1.00 53.86 ? 192 ASN A CB  1 
ATOM   1576 C  CG  . ASN A 1 192 ? 24.550  26.881  45.199  1.00 59.20 ? 192 ASN A CG  1 
ATOM   1577 O  OD1 . ASN A 1 192 ? 25.640  26.887  44.612  1.00 54.84 ? 192 ASN A OD1 1 
ATOM   1578 N  ND2 . ASN A 1 192 ? 24.425  26.503  46.460  1.00 57.58 ? 192 ASN A ND2 1 
ATOM   1579 N  N   . PRO A 1 193 ? 24.680  26.534  41.163  1.00 50.91 ? 193 PRO A N   1 
ATOM   1580 C  CA  . PRO A 1 193 ? 25.059  25.387  40.333  1.00 47.95 ? 193 PRO A CA  1 
ATOM   1581 C  C   . PRO A 1 193 ? 25.975  24.374  41.027  1.00 41.62 ? 193 PRO A C   1 
ATOM   1582 O  O   . PRO A 1 193 ? 26.129  23.292  40.499  1.00 35.64 ? 193 PRO A O   1 
ATOM   1583 C  CB  . PRO A 1 193 ? 25.833  26.025  39.167  1.00 50.11 ? 193 PRO A CB  1 
ATOM   1584 C  CG  . PRO A 1 193 ? 26.408  27.276  39.783  1.00 50.52 ? 193 PRO A CG  1 
ATOM   1585 C  CD  . PRO A 1 193 ? 25.292  27.782  40.675  1.00 51.55 ? 193 PRO A CD  1 
ATOM   1586 N  N   . ASP A 1 194 ? 26.576  24.743  42.158  1.00 37.95 ? 194 ASP A N   1 
ATOM   1587 C  CA  . ASP A 1 194 ? 27.499  23.856  42.918  1.00 43.85 ? 194 ASP A CA  1 
ATOM   1588 C  C   . ASP A 1 194 ? 26.728  23.084  43.994  1.00 39.55 ? 194 ASP A C   1 
ATOM   1589 O  O   . ASP A 1 194 ? 27.335  22.205  44.611  1.00 37.35 ? 194 ASP A O   1 
ATOM   1590 C  CB  . ASP A 1 194 ? 28.661  24.664  43.500  1.00 48.92 ? 194 ASP A CB  1 
ATOM   1591 C  CG  . ASP A 1 194 ? 29.538  25.242  42.406  1.00 57.48 ? 194 ASP A CG  1 
ATOM   1592 O  OD1 . ASP A 1 194 ? 29.953  24.458  41.521  1.00 59.52 ? 194 ASP A OD1 1 
ATOM   1593 O  OD2 . ASP A 1 194 ? 29.758  26.476  42.419  1.00 63.10 ? 194 ASP A OD2 1 
ATOM   1594 N  N   . ASP A 1 195 ? 25.442  23.373  44.193  1.00 35.68 ? 195 ASP A N   1 
ATOM   1595 C  CA  . ASP A 1 195 ? 24.584  22.652  45.174  1.00 36.89 ? 195 ASP A CA  1 
ATOM   1596 C  C   . ASP A 1 195 ? 24.750  21.148  44.965  1.00 38.27 ? 195 ASP A C   1 
ATOM   1597 O  O   . ASP A 1 195 ? 24.717  20.686  43.825  1.00 37.00 ? 195 ASP A O   1 
ATOM   1598 C  CB  . ASP A 1 195 ? 23.122  23.074  45.023  1.00 40.16 ? 195 ASP A CB  1 
ATOM   1599 C  CG  . ASP A 1 195 ? 22.182  22.558  46.107  1.00 45.26 ? 195 ASP A CG  1 
ATOM   1600 O  OD1 . ASP A 1 195 ? 22.159  21.343  46.355  1.00 42.17 ? 195 ASP A OD1 1 
ATOM   1601 O  OD2 . ASP A 1 195 ? 21.433  23.384  46.667  1.00 53.10 ? 195 ASP A OD2 1 
ATOM   1602 N  N   . PRO A 1 196 ? 24.883  20.309  46.022  1.00 39.94 ? 196 PRO A N   1 
ATOM   1603 C  CA  . PRO A 1 196 ? 25.116  18.869  45.827  1.00 41.99 ? 196 PRO A CA  1 
ATOM   1604 C  C   . PRO A 1 196 ? 23.960  18.086  45.178  1.00 37.14 ? 196 PRO A C   1 
ATOM   1605 O  O   . PRO A 1 196 ? 24.215  16.989  44.730  1.00 39.09 ? 196 PRO A O   1 
ATOM   1606 C  CB  . PRO A 1 196 ? 25.345  18.300  47.237  1.00 41.30 ? 196 PRO A CB  1 
ATOM   1607 C  CG  . PRO A 1 196 ? 25.551  19.514  48.119  1.00 41.24 ? 196 PRO A CG  1 
ATOM   1608 C  CD  . PRO A 1 196 ? 24.818  20.664  47.451  1.00 42.58 ? 196 PRO A CD  1 
ATOM   1609 N  N   . ALA A 1 197 ? 22.738  18.638  45.198  1.00 34.98 ? 197 ALA A N   1 
ATOM   1610 C  CA  . ALA A 1 197 ? 21.540  18.144  44.486  1.00 36.40 ? 197 ALA A CA  1 
ATOM   1611 C  C   . ALA A 1 197 ? 21.779  18.072  42.963  1.00 35.74 ? 197 ALA A C   1 
ATOM   1612 O  O   . ALA A 1 197 ? 20.922  17.513  42.264  1.00 38.68 ? 197 ALA A O   1 
ATOM   1613 C  CB  . ALA A 1 197 ? 20.354  19.032  44.797  1.00 36.23 ? 197 ALA A CB  1 
ATOM   1614 N  N   . TYR A 1 198 ? 22.839  18.686  42.435  1.00 32.42 ? 198 TYR A N   1 
ATOM   1615 C  CA  . TYR A 1 198 ? 23.115  18.679  40.964  1.00 31.63 ? 198 TYR A CA  1 
ATOM   1616 C  C   . TYR A 1 198 ? 24.279  17.735  40.652  1.00 32.38 ? 198 TYR A C   1 
ATOM   1617 O  O   . TYR A 1 198 ? 24.727  17.610  39.458  1.00 29.64 ? 198 TYR A O   1 
ATOM   1618 C  CB  . TYR A 1 198 ? 23.423  20.083  40.451  1.00 29.65 ? 198 TYR A CB  1 
ATOM   1619 C  CG  . TYR A 1 198 ? 22.292  21.068  40.624  1.00 30.32 ? 198 TYR A CG  1 
ATOM   1620 C  CD1 . TYR A 1 198 ? 21.019  20.793  40.162  1.00 30.46 ? 198 TYR A CD1 1 
ATOM   1621 C  CD2 . TYR A 1 198 ? 22.486  22.262  41.303  1.00 30.06 ? 198 TYR A CD2 1 
ATOM   1622 C  CE1 . TYR A 1 198 ? 19.982  21.698  40.317  1.00 29.79 ? 198 TYR A CE1 1 
ATOM   1623 C  CE2 . TYR A 1 198 ? 21.454  23.162  41.491  1.00 28.43 ? 198 TYR A CE2 1 
ATOM   1624 C  CZ  . TYR A 1 198 ? 20.189  22.872  41.020  1.00 30.28 ? 198 TYR A CZ  1 
ATOM   1625 O  OH  . TYR A 1 198 ? 19.179  23.782  41.145  1.00 37.50 ? 198 TYR A OH  1 
ATOM   1626 N  N   . ASP A 1 199 ? 24.792  17.072  41.678  1.00 31.43 ? 199 ASP A N   1 
ATOM   1627 C  CA  . ASP A 1 199 ? 25.938  16.144  41.527  1.00 33.52 ? 199 ASP A CA  1 
ATOM   1628 C  C   . ASP A 1 199 ? 25.552  15.029  40.547  1.00 31.72 ? 199 ASP A C   1 
ATOM   1629 O  O   . ASP A 1 199 ? 26.386  14.735  39.707  1.00 29.35 ? 199 ASP A O   1 
ATOM   1630 C  CB  . ASP A 1 199 ? 26.429  15.574  42.859  1.00 37.75 ? 199 ASP A CB  1 
ATOM   1631 C  CG  . ASP A 1 199 ? 27.112  16.590  43.768  1.00 39.93 ? 199 ASP A CG  1 
ATOM   1632 O  OD1 . ASP A 1 199 ? 27.445  17.687  43.295  1.00 41.87 ? 199 ASP A OD1 1 
ATOM   1633 O  OD2 . ASP A 1 199 ? 27.256  16.286  44.962  1.00 45.48 ? 199 ASP A OD2 1 
ATOM   1634 N  N   . GLU A 1 200 ? 24.366  14.418  40.656  1.00 30.18 ? 200 GLU A N   1 
ATOM   1635 C  CA  . GLU A 1 200 ? 23.993  13.282  39.761  1.00 31.95 ? 200 GLU A CA  1 
ATOM   1636 C  C   . GLU A 1 200 ? 23.838  13.815  38.330  1.00 27.22 ? 200 GLU A C   1 
ATOM   1637 O  O   . GLU A 1 200 ? 24.246  13.111  37.377  1.00 28.44 ? 200 GLU A O   1 
ATOM   1638 C  CB  . GLU A 1 200 ? 22.710  12.571  40.221  1.00 32.87 ? 200 GLU A CB  1 
ATOM   1639 C  CG  . GLU A 1 200 ? 22.166  11.558  39.235  1.00 38.45 ? 200 GLU A CG  1 
ATOM   1640 C  CD  . GLU A 1 200 ? 23.112  10.418  38.912  1.00 44.26 ? 200 GLU A CD  1 
ATOM   1641 O  OE1 . GLU A 1 200 ? 24.193  10.354  39.533  1.00 49.33 ? 200 GLU A OE1 1 
ATOM   1642 O  OE2 . GLU A 1 200 ? 22.757  9.586   38.056  1.00 47.65 ? 200 GLU A OE2 1 
ATOM   1643 N  N   . ASN A 1 201 ? 23.296  15.010  38.183  1.00 27.35 ? 201 ASN A N   1 
ATOM   1644 C  CA  . ASN A 1 201 ? 23.181  15.670  36.852  1.00 26.85 ? 201 ASN A CA  1 
ATOM   1645 C  C   . ASN A 1 201 ? 24.560  15.769  36.206  1.00 28.52 ? 201 ASN A C   1 
ATOM   1646 O  O   . ASN A 1 201 ? 24.651  15.490  34.982  1.00 26.20 ? 201 ASN A O   1 
ATOM   1647 C  CB  . ASN A 1 201 ? 22.574  17.065  36.978  1.00 29.04 ? 201 ASN A CB  1 
ATOM   1648 C  CG  . ASN A 1 201 ? 21.207  17.033  37.613  1.00 32.64 ? 201 ASN A CG  1 
ATOM   1649 O  OD1 . ASN A 1 201 ? 21.064  17.395  38.774  1.00 38.61 ? 201 ASN A OD1 1 
ATOM   1650 N  ND2 . ASN A 1 201 ? 20.210  16.584  36.881  1.00 35.70 ? 201 ASN A ND2 1 
ATOM   1651 N  N   . LYS A 1 202 ? 25.564  16.225  36.961  1.00 26.99 ? 202 LYS A N   1 
ATOM   1652 C  CA  . LYS A 1 202 ? 26.946  16.440  36.454  1.00 29.49 ? 202 LYS A CA  1 
ATOM   1653 C  C   . LYS A 1 202 ? 27.573  15.098  36.068  1.00 28.46 ? 202 LYS A C   1 
ATOM   1654 O  O   . LYS A 1 202 ? 28.175  14.987  35.009  1.00 28.17 ? 202 LYS A O   1 
ATOM   1655 C  CB  . LYS A 1 202 ? 27.771  17.192  37.499  1.00 31.85 ? 202 LYS A CB  1 
ATOM   1656 C  CG  . LYS A 1 202 ? 27.448  18.677  37.563  1.00 33.91 ? 202 LYS A CG  1 
ATOM   1657 C  CD  . LYS A 1 202 ? 28.115  19.414  38.717  1.00 39.30 ? 202 LYS A CD  1 
ATOM   1658 C  CE  . LYS A 1 202 ? 27.511  20.783  38.945  1.00 39.15 ? 202 LYS A CE  1 
ATOM   1659 N  NZ  . LYS A 1 202 ? 27.832  21.292  40.302  1.00 43.10 ? 202 LYS A NZ  1 
ATOM   1660 N  N   . ARG A 1 203 ? 27.379  14.071  36.882  1.00 31.03 ? 203 ARG A N   1 
ATOM   1661 C  CA  . ARG A 1 203 ? 27.877  12.707  36.579  1.00 27.83 ? 203 ARG A CA  1 
ATOM   1662 C  C   . ARG A 1 203 ? 27.216  12.174  35.293  1.00 28.19 ? 203 ARG A C   1 
ATOM   1663 O  O   . ARG A 1 203 ? 27.942  11.593  34.424  1.00 28.78 ? 203 ARG A O   1 
ATOM   1664 C  CB  . ARG A 1 203 ? 27.670  11.823  37.815  1.00 33.79 ? 203 ARG A CB  1 
ATOM   1665 C  CG  . ARG A 1 203 ? 27.888  10.333  37.570  1.00 36.85 ? 203 ARG A CG  1 
ATOM   1666 C  CD  . ARG A 1 203 ? 26.550  9.620   37.623  1.00 45.33 ? 203 ARG A CD  1 
ATOM   1667 N  NE  . ARG A 1 203 ? 26.512  8.407   36.816  1.00 48.89 ? 203 ARG A NE  1 
ATOM   1668 C  CZ  . ARG A 1 203 ? 25.477  7.990   36.092  1.00 49.84 ? 203 ARG A CZ  1 
ATOM   1669 N  NH1 . ARG A 1 203 ? 24.351  8.681   36.032  1.00 48.31 ? 203 ARG A NH1 1 
ATOM   1670 N  NH2 . ARG A 1 203 ? 25.576  6.863   35.414  1.00 52.50 ? 203 ARG A NH2 1 
ATOM   1671 N  N   . GLN A 1 204 ? 25.908  12.381  35.126  1.00 25.68 ? 204 GLN A N   1 
ATOM   1672 C  CA  . GLN A 1 204 ? 25.175  11.858  33.951  1.00 25.39 ? 204 GLN A CA  1 
ATOM   1673 C  C   . GLN A 1 204 ? 25.690  12.592  32.699  1.00 23.78 ? 204 GLN A C   1 
ATOM   1674 O  O   . GLN A 1 204 ? 25.763  11.968  31.621  1.00 22.41 ? 204 GLN A O   1 
ATOM   1675 C  CB  . GLN A 1 204 ? 23.665  12.011  34.163  1.00 24.56 ? 204 GLN A CB  1 
ATOM   1676 C  CG  . GLN A 1 204 ? 22.827  11.507  32.997  1.00 25.73 ? 204 GLN A CG  1 
ATOM   1677 C  CD  . GLN A 1 204 ? 22.933  10.022  32.766  1.00 28.91 ? 204 GLN A CD  1 
ATOM   1678 O  OE1 . GLN A 1 204 ? 22.212  9.216   33.365  1.00 31.98 ? 204 GLN A OE1 1 
ATOM   1679 N  NE2 . GLN A 1 204 ? 23.844  9.640   31.885  1.00 28.06 ? 204 GLN A NE2 1 
ATOM   1680 N  N   . PHE A 1 205 ? 25.980  13.873  32.841  1.00 22.81 ? 205 PHE A N   1 
ATOM   1681 C  CA  . PHE A 1 205 ? 26.427  14.736  31.711  1.00 20.58 ? 205 PHE A CA  1 
ATOM   1682 C  C   . PHE A 1 205 ? 27.761  14.216  31.175  1.00 23.06 ? 205 PHE A C   1 
ATOM   1683 O  O   . PHE A 1 205 ? 27.905  14.015  29.949  1.00 23.58 ? 205 PHE A O   1 
ATOM   1684 C  CB  . PHE A 1 205 ? 26.531  16.186  32.178  1.00 20.90 ? 205 PHE A CB  1 
ATOM   1685 C  CG  . PHE A 1 205 ? 26.728  17.224  31.109  1.00 21.14 ? 205 PHE A CG  1 
ATOM   1686 C  CD1 . PHE A 1 205 ? 25.777  17.367  30.117  1.00 22.05 ? 205 PHE A CD1 1 
ATOM   1687 C  CD2 . PHE A 1 205 ? 27.736  18.168  31.204  1.00 20.85 ? 205 PHE A CD2 1 
ATOM   1688 C  CE1 . PHE A 1 205 ? 25.918  18.350  29.155  1.00 21.96 ? 205 PHE A CE1 1 
ATOM   1689 C  CE2 . PHE A 1 205 ? 27.888  19.142  30.229  1.00 21.17 ? 205 PHE A CE2 1 
ATOM   1690 C  CZ  . PHE A 1 205 ? 26.960  19.248  29.225  1.00 22.94 ? 205 PHE A CZ  1 
ATOM   1691 N  N   . GLN A 1 206 ? 28.705  13.913  32.075  1.00 24.73 ? 206 GLN A N   1 
ATOM   1692 C  CA  . GLN A 1 206 ? 30.029  13.358  31.692  1.00 26.39 ? 206 GLN A CA  1 
ATOM   1693 C  C   . GLN A 1 206 ? 29.851  12.020  30.998  1.00 24.88 ? 206 GLN A C   1 
ATOM   1694 O  O   . GLN A 1 206 ? 30.543  11.747  30.015  1.00 26.10 ? 206 GLN A O   1 
ATOM   1695 C  CB  . GLN A 1 206 ? 30.951  13.247  32.907  1.00 28.10 ? 206 GLN A CB  1 
ATOM   1696 C  CG  . GLN A 1 206 ? 31.343  14.609  33.448  1.00 29.92 ? 206 GLN A CG  1 
ATOM   1697 C  CD  . GLN A 1 206 ? 31.964  15.518  32.404  1.00 32.58 ? 206 GLN A CD  1 
ATOM   1698 O  OE1 . GLN A 1 206 ? 32.837  15.115  31.632  1.00 42.21 ? 206 GLN A OE1 1 
ATOM   1699 N  NE2 . GLN A 1 206 ? 31.496  16.753  32.345  1.00 31.29 ? 206 GLN A NE2 1 
ATOM   1700 N  N   . GLU A 1 207 ? 28.955  11.168  31.484  1.00 25.29 ? 207 GLU A N   1 
ATOM   1701 C  CA  . GLU A 1 207 ? 28.685  9.862   30.849  1.00 26.11 ? 207 GLU A CA  1 
ATOM   1702 C  C   . GLU A 1 207 ? 28.128  10.040  29.430  1.00 24.28 ? 207 GLU A C   1 
ATOM   1703 O  O   . GLU A 1 207 ? 28.545  9.292   28.530  1.00 23.79 ? 207 GLU A O   1 
ATOM   1704 C  CB  . GLU A 1 207 ? 27.691  9.084   31.714  1.00 31.74 ? 207 GLU A CB  1 
ATOM   1705 C  CG  . GLU A 1 207 ? 27.247  7.765   31.144  1.00 38.21 ? 207 GLU A CG  1 
ATOM   1706 C  CD  . GLU A 1 207 ? 26.342  7.043   32.133  1.00 49.61 ? 207 GLU A CD  1 
ATOM   1707 O  OE1 . GLU A 1 207 ? 25.136  6.839   31.817  1.00 52.58 ? 207 GLU A OE1 1 
ATOM   1708 O  OE2 . GLU A 1 207 ? 26.833  6.730   33.234  1.00 54.96 ? 207 GLU A OE2 1 
ATOM   1709 N  N   . ASP A 1 208 ? 27.156  10.943  29.264  1.00 23.01 ? 208 ASP A N   1 
ATOM   1710 C  CA  . ASP A 1 208 ? 26.506  11.181  27.942  1.00 22.32 ? 208 ASP A CA  1 
ATOM   1711 C  C   . ASP A 1 208 ? 27.518  11.723  26.916  1.00 20.98 ? 208 ASP A C   1 
ATOM   1712 O  O   . ASP A 1 208 ? 27.450  11.289  25.731  1.00 21.05 ? 208 ASP A O   1 
ATOM   1713 C  CB  . ASP A 1 208 ? 25.308  12.100  28.157  1.00 20.61 ? 208 ASP A CB  1 
ATOM   1714 C  CG  . ASP A 1 208 ? 24.145  11.400  28.832  1.00 19.87 ? 208 ASP A CG  1 
ATOM   1715 O  OD1 . ASP A 1 208 ? 23.954  10.192  28.584  1.00 20.91 ? 208 ASP A OD1 1 
ATOM   1716 O  OD2 . ASP A 1 208 ? 23.362  12.101  29.462  1.00 19.61 ? 208 ASP A OD2 1 
ATOM   1717 N  N   . ILE A 1 209 ? 28.428  12.557  27.370  1.00 21.37 ? 209 ILE A N   1 
ATOM   1718 C  CA  . ILE A 1 209 ? 29.490  13.115  26.500  1.00 23.17 ? 209 ILE A CA  1 
ATOM   1719 C  C   . ILE A 1 209 ? 30.366  11.944  26.043  1.00 25.03 ? 209 ILE A C   1 
ATOM   1720 O  O   . ILE A 1 209 ? 30.699  11.885  24.875  1.00 24.72 ? 209 ILE A O   1 
ATOM   1721 C  CB  . ILE A 1 209 ? 30.272  14.253  27.161  1.00 22.17 ? 209 ILE A CB  1 
ATOM   1722 C  CG1 . ILE A 1 209 ? 29.370  15.454  27.472  1.00 24.57 ? 209 ILE A CG1 1 
ATOM   1723 C  CG2 . ILE A 1 209 ? 31.478  14.626  26.297  1.00 23.10 ? 209 ILE A CG2 1 
ATOM   1724 C  CD1 . ILE A 1 209 ? 29.980  16.489  28.392  1.00 23.07 ? 209 ILE A CD1 1 
ATOM   1725 N  N   . LYS A 1 210 ? 30.669  10.998  26.938  1.00 26.43 ? 210 LYS A N   1 
ATOM   1726 C  CA  . LYS A 1 210 ? 31.437  9.776   26.572  1.00 26.82 ? 210 LYS A CA  1 
ATOM   1727 C  C   . LYS A 1 210 ? 30.709  8.937   25.524  1.00 25.67 ? 210 LYS A C   1 
ATOM   1728 O  O   . LYS A 1 210 ? 31.375  8.476   24.580  1.00 25.46 ? 210 LYS A O   1 
ATOM   1729 C  CB  . LYS A 1 210 ? 31.702  8.923   27.821  1.00 32.47 ? 210 LYS A CB  1 
ATOM   1730 C  CG  . LYS A 1 210 ? 33.065  8.249   27.860  1.00 38.36 ? 210 LYS A CG  1 
ATOM   1731 C  CD  . LYS A 1 210 ? 33.217  7.272   29.011  1.00 40.22 ? 210 LYS A CD  1 
ATOM   1732 C  CE  . LYS A 1 210 ? 34.505  6.480   28.962  1.00 46.57 ? 210 LYS A CE  1 
ATOM   1733 N  NZ  . LYS A 1 210 ? 34.522  5.552   27.802  1.00 48.79 ? 210 LYS A NZ  1 
ATOM   1734 N  N   . VAL A 1 211 ? 29.418  8.667   25.680  1.00 21.79 ? 211 VAL A N   1 
ATOM   1735 C  CA  . VAL A 1 211 ? 28.638  7.856   24.717  1.00 25.68 ? 211 VAL A CA  1 
ATOM   1736 C  C   . VAL A 1 211 ? 28.750  8.519   23.346  1.00 27.74 ? 211 VAL A C   1 
ATOM   1737 O  O   . VAL A 1 211 ? 28.886  7.793   22.346  1.00 26.18 ? 211 VAL A O   1 
ATOM   1738 C  CB  . VAL A 1 211 ? 27.161  7.709   25.122  1.00 22.54 ? 211 VAL A CB  1 
ATOM   1739 C  CG1 . VAL A 1 211 ? 26.276  7.215   23.996  1.00 23.13 ? 211 VAL A CG1 1 
ATOM   1740 C  CG2 . VAL A 1 211 ? 27.008  6.825   26.368  1.00 27.53 ? 211 VAL A CG2 1 
ATOM   1741 N  N   . MET A 1 212 ? 28.602  9.847   23.298  1.00 24.40 ? 212 MET A N   1 
ATOM   1742 C  CA  . MET A 1 212 ? 28.609  10.566  22.010  1.00 22.99 ? 212 MET A CA  1 
ATOM   1743 C  C   . MET A 1 212 ? 30.003  10.496  21.385  1.00 21.84 ? 212 MET A C   1 
ATOM   1744 O  O   . MET A 1 212 ? 30.080  10.160  20.192  1.00 20.64 ? 212 MET A O   1 
ATOM   1745 C  CB  . MET A 1 212 ? 28.181  12.019  22.221  1.00 21.78 ? 212 MET A CB  1 
ATOM   1746 C  CG  . MET A 1 212 ? 26.685  12.121  22.498  1.00 21.23 ? 212 MET A CG  1 
ATOM   1747 S  SD  . MET A 1 212 ? 26.094  13.868  22.460  1.00 20.68 ? 212 MET A SD  1 
ATOM   1748 C  CE  . MET A 1 212 ? 26.605  14.402  24.072  1.00 19.40 ? 212 MET A CE  1 
ATOM   1749 N  N   . ASN A 1 213 ? 31.041  10.795  22.145  1.00 20.83 ? 213 ASN A N   1 
ATOM   1750 C  CA  . ASN A 1 213 ? 32.444  10.811  21.635  1.00 24.01 ? 213 ASN A CA  1 
ATOM   1751 C  C   . ASN A 1 213 ? 32.773  9.389   21.124  1.00 27.45 ? 213 ASN A C   1 
ATOM   1752 O  O   . ASN A 1 213 ? 33.408  9.227   20.054  1.00 23.89 ? 213 ASN A O   1 
ATOM   1753 C  CB  . ASN A 1 213 ? 33.405  11.346  22.680  1.00 24.29 ? 213 ASN A CB  1 
ATOM   1754 C  CG  . ASN A 1 213 ? 33.257  12.824  22.961  1.00 25.06 ? 213 ASN A CG  1 
ATOM   1755 O  OD1 . ASN A 1 213 ? 32.519  13.525  22.249  1.00 22.86 ? 213 ASN A OD1 1 
ATOM   1756 N  ND2 . ASN A 1 213 ? 33.909  13.305  23.995  1.00 27.29 ? 213 ASN A ND2 1 
ATOM   1757 N  N   . ASP A 1 214 ? 32.283  8.353   21.803  1.00 27.56 ? 214 ASP A N   1 
ATOM   1758 C  CA  . ASP A 1 214 ? 32.729  6.975   21.459  1.00 27.01 ? 214 ASP A CA  1 
ATOM   1759 C  C   . ASP A 1 214 ? 32.115  6.518   20.147  1.00 27.90 ? 214 ASP A C   1 
ATOM   1760 O  O   . ASP A 1 214 ? 32.868  6.020   19.321  1.00 27.66 ? 214 ASP A O   1 
ATOM   1761 C  CB  . ASP A 1 214 ? 32.512  6.028   22.638  1.00 31.75 ? 214 ASP A CB  1 
ATOM   1762 C  CG  . ASP A 1 214 ? 33.466  6.333   23.778  1.00 32.82 ? 214 ASP A CG  1 
ATOM   1763 O  OD1 . ASP A 1 214 ? 34.435  7.089   23.577  1.00 42.01 ? 214 ASP A OD1 1 
ATOM   1764 O  OD2 . ASP A 1 214 ? 33.216  5.849   24.884  1.00 43.23 ? 214 ASP A OD2 1 
ATOM   1765 N  N   . LEU A 1 215 ? 30.814  6.699   19.921  1.00 23.96 ? 215 LEU A N   1 
ATOM   1766 C  CA  . LEU A 1 215 ? 30.215  6.325   18.626  1.00 25.12 ? 215 LEU A CA  1 
ATOM   1767 C  C   . LEU A 1 215 ? 30.865  7.190   17.549  1.00 22.71 ? 215 LEU A C   1 
ATOM   1768 O  O   . LEU A 1 215 ? 31.240  6.626   16.549  1.00 21.69 ? 215 LEU A O   1 
ATOM   1769 C  CB  . LEU A 1 215 ? 28.691  6.477   18.579  1.00 27.94 ? 215 LEU A CB  1 
ATOM   1770 C  CG  . LEU A 1 215 ? 28.069  6.203   17.194  1.00 31.18 ? 215 LEU A CG  1 
ATOM   1771 C  CD1 . LEU A 1 215 ? 28.058  4.713   16.837  1.00 38.13 ? 215 LEU A CD1 1 
ATOM   1772 C  CD2 . LEU A 1 215 ? 26.669  6.766   17.078  1.00 34.67 ? 215 LEU A CD2 1 
ATOM   1773 N  N   . VAL A 1 216 ? 30.953  8.521   17.737  1.00 22.01 ? 216 VAL A N   1 
ATOM   1774 C  CA  . VAL A 1 216 ? 31.420  9.364   16.612  1.00 18.93 ? 216 VAL A CA  1 
ATOM   1775 C  C   . VAL A 1 216 ? 32.922  9.093   16.316  1.00 17.99 ? 216 VAL A C   1 
ATOM   1776 O  O   . VAL A 1 216 ? 33.246  9.029   15.134  1.00 17.84 ? 216 VAL A O   1 
ATOM   1777 C  CB  . VAL A 1 216 ? 31.092  10.840  16.906  1.00 18.50 ? 216 VAL A CB  1 
ATOM   1778 C  CG1 . VAL A 1 216 ? 31.813  11.757  15.916  1.00 19.61 ? 216 VAL A CG1 1 
ATOM   1779 C  CG2 . VAL A 1 216 ? 29.582  11.041  16.875  1.00 18.87 ? 216 VAL A CG2 1 
ATOM   1780 N  N   . ASP A 1 217 ? 33.756  8.973   17.338  1.00 19.39 ? 217 ASP A N   1 
ATOM   1781 C  CA  . ASP A 1 217 ? 35.215  8.728   17.170  1.00 19.75 ? 217 ASP A CA  1 
ATOM   1782 C  C   . ASP A 1 217 ? 35.374  7.400   16.443  1.00 22.54 ? 217 ASP A C   1 
ATOM   1783 O  O   . ASP A 1 217 ? 36.259  7.315   15.597  1.00 21.13 ? 217 ASP A O   1 
ATOM   1784 C  CB  . ASP A 1 217 ? 36.015  8.804   18.462  1.00 19.43 ? 217 ASP A CB  1 
ATOM   1785 C  CG  . ASP A 1 217 ? 36.176  10.202  19.033  1.00 21.47 ? 217 ASP A CG  1 
ATOM   1786 O  OD1 . ASP A 1 217 ? 35.888  11.166  18.271  1.00 23.16 ? 217 ASP A OD1 1 
ATOM   1787 O  OD2 . ASP A 1 217 ? 36.620  10.358  20.194  1.00 26.18 ? 217 ASP A OD2 1 
ATOM   1788 N  N   . LYS A 1 218 ? 34.527  6.409   16.752  1.00 22.11 ? 218 LYS A N   1 
ATOM   1789 C  CA  . LYS A 1 218 ? 34.602  5.075   16.084  1.00 23.34 ? 218 LYS A CA  1 
ATOM   1790 C  C   . LYS A 1 218 ? 34.169  5.220   14.636  1.00 22.25 ? 218 LYS A C   1 
ATOM   1791 O  O   . LYS A 1 218 ? 34.783  4.620   13.745  1.00 22.47 ? 218 LYS A O   1 
ATOM   1792 C  CB  . LYS A 1 218 ? 33.724  4.037   16.811  1.00 26.61 ? 218 LYS A CB  1 
ATOM   1793 C  CG  . LYS A 1 218 ? 33.675  2.642   16.186  1.00 29.87 ? 218 LYS A CG  1 
ATOM   1794 C  CD  . LYS A 1 218 ? 33.031  1.599   17.107  1.00 37.09 ? 218 LYS A CD  1 
ATOM   1795 C  CE  . LYS A 1 218 ? 32.423  0.395   16.405  1.00 41.68 ? 218 LYS A CE  1 
ATOM   1796 N  NZ  . LYS A 1 218 ? 33.369  -0.203  15.430  1.00 45.62 ? 218 LYS A NZ  1 
ATOM   1797 N  N   . ILE A 1 219 ? 33.119  5.985   14.357  1.00 21.05 ? 219 ILE A N   1 
ATOM   1798 C  CA  . ILE A 1 219 ? 32.658  6.217   12.966  1.00 23.09 ? 219 ILE A CA  1 
ATOM   1799 C  C   . ILE A 1 219 ? 33.846  6.797   12.173  1.00 20.49 ? 219 ILE A C   1 
ATOM   1800 O  O   . ILE A 1 219 ? 34.124  6.332   11.078  1.00 19.04 ? 219 ILE A O   1 
ATOM   1801 C  CB  . ILE A 1 219 ? 31.428  7.150   12.951  1.00 25.43 ? 219 ILE A CB  1 
ATOM   1802 C  CG1 . ILE A 1 219 ? 30.177  6.425   13.462  1.00 29.84 ? 219 ILE A CG1 1 
ATOM   1803 C  CG2 . ILE A 1 219 ? 31.194  7.756   11.580  1.00 28.42 ? 219 ILE A CG2 1 
ATOM   1804 C  CD1 . ILE A 1 219 ? 29.964  5.084   12.827  1.00 33.80 ? 219 ILE A CD1 1 
ATOM   1805 N  N   . ILE A 1 220 ? 34.504  7.810   12.713  1.00 18.07 ? 220 ILE A N   1 
ATOM   1806 C  CA  . ILE A 1 220 ? 35.635  8.460   11.992  1.00 18.82 ? 220 ILE A CA  1 
ATOM   1807 C  C   . ILE A 1 220 ? 36.758  7.430   11.784  1.00 18.71 ? 220 ILE A C   1 
ATOM   1808 O  O   . ILE A 1 220 ? 37.235  7.340   10.654  1.00 18.90 ? 220 ILE A O   1 
ATOM   1809 C  CB  . ILE A 1 220 ? 36.108  9.695   12.769  1.00 18.07 ? 220 ILE A CB  1 
ATOM   1810 C  CG1 . ILE A 1 220 ? 34.984  10.730  12.906  1.00 17.44 ? 220 ILE A CG1 1 
ATOM   1811 C  CG2 . ILE A 1 220 ? 37.330  10.298  12.113  1.00 19.56 ? 220 ILE A CG2 1 
ATOM   1812 C  CD1 . ILE A 1 220 ? 35.257  11.823  13.876  1.00 17.73 ? 220 ILE A CD1 1 
ATOM   1813 N  N   . ALA A 1 221 ? 37.106  6.706   12.829  1.00 20.60 ? 221 ALA A N   1 
ATOM   1814 C  CA  . ALA A 1 221 ? 38.296  5.814   12.787  1.00 22.30 ? 221 ALA A CA  1 
ATOM   1815 C  C   . ALA A 1 221 ? 37.991  4.683   11.789  1.00 22.03 ? 221 ALA A C   1 
ATOM   1816 O  O   . ALA A 1 221 ? 38.871  4.344   10.922  1.00 21.74 ? 221 ALA A O   1 
ATOM   1817 C  CB  . ALA A 1 221 ? 38.627  5.310   14.184  1.00 23.61 ? 221 ALA A CB  1 
ATOM   1818 N  N   . ASP A 1 222 ? 36.750  4.202   11.775  1.00 21.19 ? 222 ASP A N   1 
ATOM   1819 C  CA  . ASP A 1 222 ? 36.328  3.110   10.863  1.00 23.56 ? 222 ASP A CA  1 
ATOM   1820 C  C   . ASP A 1 222 ? 36.429  3.620   9.417   1.00 23.47 ? 222 ASP A C   1 
ATOM   1821 O  O   . ASP A 1 222 ? 36.909  2.911   8.528   1.00 23.99 ? 222 ASP A O   1 
ATOM   1822 C  CB  . ASP A 1 222 ? 34.918  2.617   11.181  1.00 25.01 ? 222 ASP A CB  1 
ATOM   1823 C  CG  . ASP A 1 222 ? 34.697  1.765   12.425  1.00 28.70 ? 222 ASP A CG  1 
ATOM   1824 O  OD1 . ASP A 1 222 ? 35.681  1.329   13.040  1.00 32.64 ? 222 ASP A OD1 1 
ATOM   1825 O  OD2 . ASP A 1 222 ? 33.518  1.567   12.757  1.00 29.18 ? 222 ASP A OD2 1 
ATOM   1826 N  N   . ARG A 1 223 ? 36.031  4.872   9.116   1.00 19.20 ? 223 ARG A N   1 
ATOM   1827 C  CA  . ARG A 1 223 ? 36.109  5.357   7.729   1.00 18.87 ? 223 ARG A CA  1 
ATOM   1828 C  C   . ARG A 1 223 ? 37.578  5.561   7.301   1.00 21.20 ? 223 ARG A C   1 
ATOM   1829 O  O   . ARG A 1 223 ? 37.924  5.289   6.164   1.00 21.68 ? 223 ARG A O   1 
ATOM   1830 C  CB  . ARG A 1 223 ? 35.417  6.725   7.644   1.00 18.32 ? 223 ARG A CB  1 
ATOM   1831 C  CG  . ARG A 1 223 ? 35.371  7.294   6.250   1.00 17.39 ? 223 ARG A CG  1 
ATOM   1832 C  CD  . ARG A 1 223 ? 34.653  6.470   5.219   1.00 20.05 ? 223 ARG A CD  1 
ATOM   1833 N  NE  . ARG A 1 223 ? 33.226  6.462   5.510   1.00 21.15 ? 223 ARG A NE  1 
ATOM   1834 C  CZ  . ARG A 1 223 ? 32.384  7.485   5.268   1.00 23.03 ? 223 ARG A CZ  1 
ATOM   1835 N  NH1 . ARG A 1 223 ? 32.809  8.587   4.675   1.00 23.79 ? 223 ARG A NH1 1 
ATOM   1836 N  NH2 . ARG A 1 223 ? 31.113  7.390   5.606   1.00 25.68 ? 223 ARG A NH2 1 
ATOM   1837 N  N   . LYS A 1 224 ? 38.399  6.123   8.183   1.00 20.80 ? 224 LYS A N   1 
ATOM   1838 C  CA  . LYS A 1 224 ? 39.849  6.280   7.905   1.00 24.38 ? 224 LYS A CA  1 
ATOM   1839 C  C   . LYS A 1 224 ? 40.490  4.915   7.627   1.00 25.77 ? 224 LYS A C   1 
ATOM   1840 O  O   . LYS A 1 224 ? 41.312  4.864   6.723   1.00 30.37 ? 224 LYS A O   1 
ATOM   1841 C  CB  . LYS A 1 224 ? 40.542  6.943   9.096   1.00 23.56 ? 224 LYS A CB  1 
ATOM   1842 C  CG  . LYS A 1 224 ? 40.226  8.420   9.216   1.00 28.82 ? 224 LYS A CG  1 
ATOM   1843 C  CD  . LYS A 1 224 ? 41.065  9.112   10.262  1.00 30.61 ? 224 LYS A CD  1 
ATOM   1844 C  CE  . LYS A 1 224 ? 42.238  9.867   9.681   1.00 33.06 ? 224 LYS A CE  1 
ATOM   1845 N  NZ  . LYS A 1 224 ? 42.964  10.565  10.763  1.00 35.00 ? 224 LYS A NZ  1 
ATOM   1846 N  N   . ALA A 1 225 ? 40.091  3.863   8.320   1.00 26.90 ? 225 ALA A N   1 
ATOM   1847 C  CA  . ALA A 1 225 ? 40.727  2.531   8.160   1.00 28.71 ? 225 ALA A CA  1 
ATOM   1848 C  C   . ALA A 1 225 ? 40.320  1.991   6.778   1.00 36.25 ? 225 ALA A C   1 
ATOM   1849 O  O   . ALA A 1 225 ? 41.246  1.542   6.019   1.00 40.34 ? 225 ALA A O   1 
ATOM   1850 C  CB  . ALA A 1 225 ? 40.361  1.637   9.297   1.00 28.61 ? 225 ALA A CB  1 
ATOM   1851 N  N   . SER A 1 226 ? 39.045  2.144   6.370   1.00 29.34 ? 226 SER A N   1 
ATOM   1852 C  CA  . SER A 1 226 ? 38.529  1.512   5.114   1.00 31.86 ? 226 SER A CA  1 
ATOM   1853 C  C   . SER A 1 226 ? 39.146  2.142   3.861   1.00 35.11 ? 226 SER A C   1 
ATOM   1854 O  O   . SER A 1 226 ? 39.397  1.397   2.902   1.00 42.56 ? 226 SER A O   1 
ATOM   1855 C  CB  . SER A 1 226 ? 37.034  1.489   5.039   1.00 31.96 ? 226 SER A CB  1 
ATOM   1856 O  OG  . SER A 1 226 ? 36.532  2.793   4.894   1.00 27.71 ? 226 SER A OG  1 
ATOM   1857 N  N   . GLY A 1 227 ? 39.387  3.452   3.851   1.00 33.88 ? 227 GLY A N   1 
ATOM   1858 C  CA  . GLY A 1 227 ? 39.699  4.246   2.646   1.00 34.85 ? 227 GLY A CA  1 
ATOM   1859 C  C   . GLY A 1 227 ? 38.489  4.494   1.751   1.00 35.65 ? 227 GLY A C   1 
ATOM   1860 O  O   . GLY A 1 227 ? 38.673  5.120   0.682   1.00 39.01 ? 227 GLY A O   1 
ATOM   1861 N  N   . GLU A 1 228 ? 37.301  4.040   2.156   1.00 35.08 ? 228 GLU A N   1 
ATOM   1862 C  CA  . GLU A 1 228 ? 36.051  4.112   1.356   1.00 36.86 ? 228 GLU A CA  1 
ATOM   1863 C  C   . GLU A 1 228 ? 35.751  5.588   1.078   1.00 37.07 ? 228 GLU A C   1 
ATOM   1864 O  O   . GLU A 1 228 ? 35.836  6.383   2.027   1.00 34.90 ? 228 GLU A O   1 
ATOM   1865 C  CB  . GLU A 1 228 ? 34.932  3.417   2.127   1.00 42.59 ? 228 GLU A CB  1 
ATOM   1866 C  CG  . GLU A 1 228 ? 33.565  3.494   1.471   1.00 49.38 ? 228 GLU A CG  1 
ATOM   1867 C  CD  . GLU A 1 228 ? 32.470  2.798   2.269   1.00 56.10 ? 228 GLU A CD  1 
ATOM   1868 O  OE1 . GLU A 1 228 ? 32.712  2.460   3.453   1.00 62.62 ? 228 GLU A OE1 1 
ATOM   1869 O  OE2 . GLU A 1 228 ? 31.379  2.585   1.709   1.00 61.88 ? 228 GLU A OE2 1 
ATOM   1870 N  N   . GLN A 1 229 ? 35.468  5.937   -0.178  1.00 38.81 ? 229 GLN A N   1 
ATOM   1871 C  CA  . GLN A 1 229 ? 35.209  7.337   -0.596  1.00 38.72 ? 229 GLN A CA  1 
ATOM   1872 C  C   . GLN A 1 229 ? 33.724  7.461   -0.888  1.00 41.53 ? 229 GLN A C   1 
ATOM   1873 O  O   . GLN A 1 229 ? 33.341  7.311   -2.053  1.00 50.68 ? 229 GLN A O   1 
ATOM   1874 C  CB  . GLN A 1 229 ? 36.073  7.728   -1.796  1.00 38.54 ? 229 GLN A CB  1 
ATOM   1875 C  CG  . GLN A 1 229 ? 37.561  7.566   -1.539  1.00 40.74 ? 229 GLN A CG  1 
ATOM   1876 C  CD  . GLN A 1 229 ? 38.070  8.553   -0.516  1.00 39.93 ? 229 GLN A CD  1 
ATOM   1877 O  OE1 . GLN A 1 229 ? 37.863  9.759   -0.636  1.00 44.00 ? 229 GLN A OE1 1 
ATOM   1878 N  NE2 . GLN A 1 229 ? 38.738  8.050   0.501   1.00 38.11 ? 229 GLN A NE2 1 
ATOM   1879 N  N   . SER A 1 230 ? 32.923  7.693   0.149   1.00 44.86 ? 230 SER A N   1 
ATOM   1880 C  CA  . SER A 1 230 ? 31.456  7.872   0.021   1.00 42.03 ? 230 SER A CA  1 
ATOM   1881 C  C   . SER A 1 230 ? 31.168  9.310   -0.398  1.00 43.38 ? 230 SER A C   1 
ATOM   1882 O  O   . SER A 1 230 ? 32.061  10.150  -0.303  1.00 48.23 ? 230 SER A O   1 
ATOM   1883 C  CB  . SER A 1 230 ? 30.737  7.500   1.288   1.00 44.64 ? 230 SER A CB  1 
ATOM   1884 O  OG  . SER A 1 230 ? 31.331  6.348   1.863   1.00 51.88 ? 230 SER A OG  1 
ATOM   1885 N  N   . ASP A 1 231 ? 29.943  9.562   -0.830  1.00 43.30 ? 231 ASP A N   1 
ATOM   1886 C  CA  . ASP A 1 231 ? 29.442  10.910  -1.195  1.00 47.18 ? 231 ASP A CA  1 
ATOM   1887 C  C   . ASP A 1 231 ? 28.948  11.594  0.065   1.00 40.23 ? 231 ASP A C   1 
ATOM   1888 O  O   . ASP A 1 231 ? 27.752  11.992  0.071   1.00 41.07 ? 231 ASP A O   1 
ATOM   1889 C  CB  . ASP A 1 231 ? 28.245  10.836  -2.147  1.00 54.61 ? 231 ASP A CB  1 
ATOM   1890 C  CG  . ASP A 1 231 ? 27.298  9.660   -1.900  1.00 63.24 ? 231 ASP A CG  1 
ATOM   1891 O  OD1 . ASP A 1 231 ? 26.946  9.393   -0.709  1.00 68.72 ? 231 ASP A OD1 1 
ATOM   1892 O  OD2 . ASP A 1 231 ? 26.923  9.007   -2.902  1.00 64.97 ? 231 ASP A OD2 1 
ATOM   1893 N  N   . ASP A 1 232 ? 29.799  11.756  1.086   1.00 34.37 ? 232 ASP A N   1 
ATOM   1894 C  CA  . ASP A 1 232 ? 29.232  12.289  2.349   1.00 29.54 ? 232 ASP A CA  1 
ATOM   1895 C  C   . ASP A 1 232 ? 30.137  13.357  2.971   1.00 23.25 ? 232 ASP A C   1 
ATOM   1896 O  O   . ASP A 1 232 ? 31.316  13.564  2.552   1.00 23.34 ? 232 ASP A O   1 
ATOM   1897 C  CB  . ASP A 1 232 ? 28.809  11.145  3.259   1.00 28.18 ? 232 ASP A CB  1 
ATOM   1898 C  CG  . ASP A 1 232 ? 29.940  10.310  3.820   1.00 25.29 ? 232 ASP A CG  1 
ATOM   1899 O  OD1 . ASP A 1 232 ? 31.097  10.777  3.858   1.00 24.80 ? 232 ASP A OD1 1 
ATOM   1900 O  OD2 . ASP A 1 232 ? 29.636  9.239   4.308   1.00 25.86 ? 232 ASP A OD2 1 
ATOM   1901 N  N   . LEU A 1 233 ? 29.571  14.043  3.946   1.00 20.24 ? 233 LEU A N   1 
ATOM   1902 C  CA  . LEU A 1 233 ? 30.286  15.117  4.665   1.00 19.21 ? 233 LEU A CA  1 
ATOM   1903 C  C   . LEU A 1 233 ? 31.539  14.561  5.309   1.00 18.73 ? 233 LEU A C   1 
ATOM   1904 O  O   . LEU A 1 233 ? 32.533  15.275  5.420   1.00 18.36 ? 233 LEU A O   1 
ATOM   1905 C  CB  . LEU A 1 233 ? 29.346  15.720  5.709   1.00 18.70 ? 233 LEU A CB  1 
ATOM   1906 C  CG  . LEU A 1 233 ? 28.179  16.489  5.145   1.00 19.15 ? 233 LEU A CG  1 
ATOM   1907 C  CD1 . LEU A 1 233 ? 27.186  16.835  6.234   1.00 20.09 ? 233 LEU A CD1 1 
ATOM   1908 C  CD2 . LEU A 1 233 ? 28.670  17.754  4.454   1.00 19.15 ? 233 LEU A CD2 1 
ATOM   1909 N  N   . LEU A 1 234 ? 31.505  13.310  5.798   1.00 16.51 ? 234 LEU A N   1 
ATOM   1910 C  CA  . LEU A 1 234 ? 32.682  12.773  6.501   1.00 16.32 ? 234 LEU A CA  1 
ATOM   1911 C  C   . LEU A 1 234 ? 33.838  12.581  5.515   1.00 18.06 ? 234 LEU A C   1 
ATOM   1912 O  O   . LEU A 1 234 ? 34.953  12.930  5.847   1.00 18.76 ? 234 LEU A O   1 
ATOM   1913 C  CB  . LEU A 1 234 ? 32.333  11.453  7.186   1.00 15.43 ? 234 LEU A CB  1 
ATOM   1914 C  CG  . LEU A 1 234 ? 33.505  10.743  7.868   1.00 16.93 ? 234 LEU A CG  1 
ATOM   1915 C  CD1 . LEU A 1 234 ? 34.255  11.643  8.840   1.00 17.52 ? 234 LEU A CD1 1 
ATOM   1916 C  CD2 . LEU A 1 234 ? 33.013  9.478   8.583   1.00 16.84 ? 234 LEU A CD2 1 
ATOM   1917 N  N   . THR A 1 235 ? 33.545  12.071  4.329   1.00 18.34 ? 235 THR A N   1 
ATOM   1918 C  CA  . THR A 1 235 ? 34.562  11.990  3.236   1.00 21.52 ? 235 THR A CA  1 
ATOM   1919 C  C   . THR A 1 235 ? 35.102  13.402  2.935   1.00 21.28 ? 235 THR A C   1 
ATOM   1920 O  O   . THR A 1 235 ? 36.347  13.577  2.918   1.00 21.92 ? 235 THR A O   1 
ATOM   1921 C  CB  . THR A 1 235 ? 33.973  11.373  1.966   1.00 23.64 ? 235 THR A CB  1 
ATOM   1922 O  OG1 . THR A 1 235 ? 33.652  10.006  2.235   1.00 29.48 ? 235 THR A OG1 1 
ATOM   1923 C  CG2 . THR A 1 235 ? 34.940  11.438  0.800   1.00 22.72 ? 235 THR A CG2 1 
ATOM   1924 N  N   . HIS A 1 236 ? 34.198  14.369  2.797   1.00 21.69 ? 236 HIS A N   1 
ATOM   1925 C  CA  . HIS A 1 236 ? 34.585  15.785  2.514   1.00 22.76 ? 236 HIS A CA  1 
ATOM   1926 C  C   . HIS A 1 236 ? 35.522  16.295  3.617   1.00 23.89 ? 236 HIS A C   1 
ATOM   1927 O  O   . HIS A 1 236 ? 36.549  16.931  3.281   1.00 24.91 ? 236 HIS A O   1 
ATOM   1928 C  CB  . HIS A 1 236 ? 33.358  16.690  2.329   1.00 27.37 ? 236 HIS A CB  1 
ATOM   1929 C  CG  . HIS A 1 236 ? 32.400  16.297  1.250   1.00 33.19 ? 236 HIS A CG  1 
ATOM   1930 N  ND1 . HIS A 1 236 ? 31.058  16.663  1.308   1.00 36.75 ? 236 HIS A ND1 1 
ATOM   1931 C  CD2 . HIS A 1 236 ? 32.549  15.592  0.097   1.00 40.06 ? 236 HIS A CD2 1 
ATOM   1932 C  CE1 . HIS A 1 236 ? 30.418  16.204  0.254   1.00 37.31 ? 236 HIS A CE1 1 
ATOM   1933 N  NE2 . HIS A 1 236 ? 31.318  15.544  -0.518  1.00 46.28 ? 236 HIS A NE2 1 
ATOM   1934 N  N   . MET A 1 237 ? 35.250  16.016  4.902   1.00 20.45 ? 237 MET A N   1 
ATOM   1935 C  CA  . MET A 1 237 ? 36.062  16.519  6.030   1.00 19.10 ? 237 MET A CA  1 
ATOM   1936 C  C   . MET A 1 237 ? 37.409  15.784  6.137   1.00 19.60 ? 237 MET A C   1 
ATOM   1937 O  O   . MET A 1 237 ? 38.414  16.404  6.517   1.00 21.04 ? 237 MET A O   1 
ATOM   1938 C  CB  . MET A 1 237 ? 35.305  16.450  7.369   1.00 16.58 ? 237 MET A CB  1 
ATOM   1939 C  CG  . MET A 1 237 ? 34.169  17.457  7.429   1.00 18.04 ? 237 MET A CG  1 
ATOM   1940 S  SD  . MET A 1 237 ? 33.331  17.528  9.027   1.00 17.12 ? 237 MET A SD  1 
ATOM   1941 C  CE  . MET A 1 237 ? 32.274  16.108  8.944   1.00 15.00 ? 237 MET A CE  1 
ATOM   1942 N  N   . LEU A 1 238 ? 37.444  14.479  5.855   1.00 19.72 ? 238 LEU A N   1 
ATOM   1943 C  CA  . LEU A 1 238 ? 38.706  13.722  5.898   1.00 20.28 ? 238 LEU A CA  1 
ATOM   1944 C  C   . LEU A 1 238 ? 39.606  14.167  4.734   1.00 22.67 ? 238 LEU A C   1 
ATOM   1945 O  O   . LEU A 1 238 ? 40.827  14.160  4.927   1.00 29.94 ? 238 LEU A O   1 
ATOM   1946 C  CB  . LEU A 1 238 ? 38.360  12.232  5.790   1.00 20.31 ? 238 LEU A CB  1 
ATOM   1947 C  CG  . LEU A 1 238 ? 37.781  11.646  7.068   1.00 20.88 ? 238 LEU A CG  1 
ATOM   1948 C  CD1 . LEU A 1 238 ? 37.358  10.186  6.846   1.00 21.94 ? 238 LEU A CD1 1 
ATOM   1949 C  CD2 . LEU A 1 238 ? 38.733  11.751  8.218   1.00 21.88 ? 238 LEU A CD2 1 
ATOM   1950 N  N   . ASN A 1 239 ? 39.049  14.523  3.599   1.00 22.32 ? 239 ASN A N   1 
ATOM   1951 C  CA  . ASN A 1 239 ? 39.893  14.829  2.399   1.00 26.44 ? 239 ASN A CA  1 
ATOM   1952 C  C   . ASN A 1 239 ? 40.153  16.326  2.252   1.00 26.61 ? 239 ASN A C   1 
ATOM   1953 O  O   . ASN A 1 239 ? 41.132  16.670  1.566   1.00 30.40 ? 239 ASN A O   1 
ATOM   1954 C  CB  . ASN A 1 239 ? 39.281  14.342  1.089   1.00 27.32 ? 239 ASN A CB  1 
ATOM   1955 C  CG  . ASN A 1 239 ? 39.239  12.828  1.004   1.00 29.38 ? 239 ASN A CG  1 
ATOM   1956 O  OD1 . ASN A 1 239 ? 39.919  12.151  1.775   1.00 33.52 ? 239 ASN A OD1 1 
ATOM   1957 N  ND2 . ASN A 1 239 ? 38.370  12.319  0.150   1.00 31.40 ? 239 ASN A ND2 1 
ATOM   1958 N  N   . GLY A 1 240 ? 39.295  17.182  2.791   1.00 22.26 ? 240 GLY A N   1 
ATOM   1959 C  CA  . GLY A 1 240 ? 39.290  18.621  2.477   1.00 22.79 ? 240 GLY A CA  1 
ATOM   1960 C  C   . GLY A 1 240 ? 40.458  19.346  3.098   1.00 20.21 ? 240 GLY A C   1 
ATOM   1961 O  O   . GLY A 1 240 ? 41.004  18.947  4.106   1.00 20.78 ? 240 GLY A O   1 
ATOM   1962 N  N   . LYS A 1 241 ? 40.843  20.408  2.415   1.00 19.80 ? 241 LYS A N   1 
ATOM   1963 C  CA  . LYS A 1 241 ? 41.865  21.370  2.879   1.00 20.23 ? 241 LYS A CA  1 
ATOM   1964 C  C   . LYS A 1 241 ? 41.262  22.755  2.814   1.00 18.40 ? 241 LYS A C   1 
ATOM   1965 O  O   . LYS A 1 241 ? 40.628  23.124  1.832   1.00 18.77 ? 241 LYS A O   1 
ATOM   1966 C  CB  . LYS A 1 241 ? 43.114  21.333  1.987   1.00 22.80 ? 241 LYS A CB  1 
ATOM   1967 C  CG  . LYS A 1 241 ? 43.818  19.991  1.906   1.00 28.41 ? 241 LYS A CG  1 
ATOM   1968 C  CD  . LYS A 1 241 ? 44.388  19.491  3.205   1.00 34.24 ? 241 LYS A CD  1 
ATOM   1969 C  CE  . LYS A 1 241 ? 44.959  18.095  3.072   1.00 40.41 ? 241 LYS A CE  1 
ATOM   1970 N  NZ  . LYS A 1 241 ? 46.357  18.147  2.579   1.00 43.05 ? 241 LYS A NZ  1 
ATOM   1971 N  N   . ASP A 1 242 ? 41.427  23.504  3.885   1.00 15.05 ? 242 ASP A N   1 
ATOM   1972 C  CA  . ASP A 1 242 ? 40.986  24.909  3.868   1.00 15.55 ? 242 ASP A CA  1 
ATOM   1973 C  C   . ASP A 1 242 ? 41.837  25.674  2.863   1.00 15.82 ? 242 ASP A C   1 
ATOM   1974 O  O   . ASP A 1 242 ? 43.063  25.738  3.031   1.00 15.68 ? 242 ASP A O   1 
ATOM   1975 C  CB  . ASP A 1 242 ? 41.115  25.510  5.258   1.00 14.62 ? 242 ASP A CB  1 
ATOM   1976 C  CG  . ASP A 1 242 ? 40.976  27.021  5.356   1.00 14.04 ? 242 ASP A CG  1 
ATOM   1977 O  OD1 . ASP A 1 242 ? 40.318  27.605  4.485   1.00 15.80 ? 242 ASP A OD1 1 
ATOM   1978 O  OD2 . ASP A 1 242 ? 41.587  27.592  6.295   1.00 15.64 ? 242 ASP A OD2 1 
ATOM   1979 N  N   . PRO A 1 243 ? 41.255  26.315  1.827   1.00 15.50 ? 243 PRO A N   1 
ATOM   1980 C  CA  . PRO A 1 243 ? 42.068  27.077  0.868   1.00 17.22 ? 243 PRO A CA  1 
ATOM   1981 C  C   . PRO A 1 243 ? 42.847  28.207  1.538   1.00 18.87 ? 243 PRO A C   1 
ATOM   1982 O  O   . PRO A 1 243 ? 43.871  28.576  1.037   1.00 18.87 ? 243 PRO A O   1 
ATOM   1983 C  CB  . PRO A 1 243 ? 41.057  27.686  -0.125  1.00 20.75 ? 243 PRO A CB  1 
ATOM   1984 C  CG  . PRO A 1 243 ? 39.784  26.905  0.081   1.00 22.08 ? 243 PRO A CG  1 
ATOM   1985 C  CD  . PRO A 1 243 ? 39.818  26.357  1.501   1.00 18.40 ? 243 PRO A CD  1 
ATOM   1986 N  N   . GLU A 1 244 ? 42.380  28.757  2.641   1.00 16.09 ? 244 GLU A N   1 
ATOM   1987 C  CA  . GLU A 1 244 ? 43.014  29.931  3.269   1.00 19.53 ? 244 GLU A CA  1 
ATOM   1988 C  C   . GLU A 1 244 ? 44.234  29.438  4.062   1.00 18.68 ? 244 GLU A C   1 
ATOM   1989 O  O   . GLU A 1 244 ? 45.330  29.898  3.736   1.00 16.99 ? 244 GLU A O   1 
ATOM   1990 C  CB  . GLU A 1 244 ? 42.009  30.715  4.122   1.00 20.48 ? 244 GLU A CB  1 
ATOM   1991 C  CG  . GLU A 1 244 ? 42.662  31.867  4.865   1.00 26.20 ? 244 GLU A CG  1 
ATOM   1992 C  CD  . GLU A 1 244 ? 41.881  32.717  5.875   1.00 34.06 ? 244 GLU A CD  1 
ATOM   1993 O  OE1 . GLU A 1 244 ? 40.820  32.302  6.346   1.00 32.99 ? 244 GLU A OE1 1 
ATOM   1994 O  OE2 . GLU A 1 244 ? 42.393  33.801  6.236   1.00 38.33 ? 244 GLU A OE2 1 
ATOM   1995 N  N   . THR A 1 245 ? 44.072  28.574  5.081   1.00 17.35 ? 245 THR A N   1 
ATOM   1996 C  CA  . THR A 1 245 ? 45.211  28.111  5.920   1.00 17.34 ? 245 THR A CA  1 
ATOM   1997 C  C   . THR A 1 245 ? 45.973  26.972  5.232   1.00 16.27 ? 245 THR A C   1 
ATOM   1998 O  O   . THR A 1 245 ? 47.172  26.735  5.611   1.00 16.83 ? 245 THR A O   1 
ATOM   1999 C  CB  . THR A 1 245 ? 44.768  27.657  7.316   1.00 18.13 ? 245 THR A CB  1 
ATOM   2000 O  OG1 . THR A 1 245 ? 43.944  26.520  7.105   1.00 17.07 ? 245 THR A OG1 1 
ATOM   2001 C  CG2 . THR A 1 245 ? 44.030  28.709  8.120   1.00 20.13 ? 245 THR A CG2 1 
ATOM   2002 N  N   . GLY A 1 246 ? 45.371  26.255  4.298   1.00 15.07 ? 246 GLY A N   1 
ATOM   2003 C  CA  . GLY A 1 246 ? 45.965  25.059  3.704   1.00 14.21 ? 246 GLY A CA  1 
ATOM   2004 C  C   . GLY A 1 246 ? 45.838  23.820  4.592   1.00 15.20 ? 246 GLY A C   1 
ATOM   2005 O  O   . GLY A 1 246 ? 46.368  22.747  4.235   1.00 15.97 ? 246 GLY A O   1 
ATOM   2006 N  N   . GLU A 1 247 ? 45.170  23.964  5.738   1.00 17.31 ? 247 GLU A N   1 
ATOM   2007 C  CA  . GLU A 1 247 ? 45.079  22.877  6.759   1.00 17.37 ? 247 GLU A CA  1 
ATOM   2008 C  C   . GLU A 1 247 ? 43.803  22.074  6.587   1.00 17.37 ? 247 GLU A C   1 
ATOM   2009 O  O   . GLU A 1 247 ? 42.762  22.628  6.248   1.00 16.06 ? 247 GLU A O   1 
ATOM   2010 C  CB  . GLU A 1 247 ? 45.087  23.457  8.143   1.00 17.75 ? 247 GLU A CB  1 
ATOM   2011 C  CG  . GLU A 1 247 ? 46.389  24.150  8.534   1.00 20.63 ? 247 GLU A CG  1 
ATOM   2012 C  CD  . GLU A 1 247 ? 46.369  24.851  9.877   1.00 24.42 ? 247 GLU A CD  1 
ATOM   2013 O  OE1 . GLU A 1 247 ? 45.462  24.570  10.699  1.00 25.02 ? 247 GLU A OE1 1 
ATOM   2014 O  OE2 . GLU A 1 247 ? 47.245  25.722  10.121  1.00 27.46 ? 247 GLU A OE2 1 
ATOM   2015 N  N   . PRO A 1 248 ? 43.857  20.767  6.868   1.00 19.25 ? 248 PRO A N   1 
ATOM   2016 C  CA  . PRO A 1 248 ? 42.657  19.961  7.006   1.00 19.74 ? 248 PRO A CA  1 
ATOM   2017 C  C   . PRO A 1 248 ? 42.156  20.081  8.436   1.00 17.62 ? 248 PRO A C   1 
ATOM   2018 O  O   . PRO A 1 248 ? 42.817  20.559  9.328   1.00 19.40 ? 248 PRO A O   1 
ATOM   2019 C  CB  . PRO A 1 248 ? 43.159  18.543  6.716   1.00 21.73 ? 248 PRO A CB  1 
ATOM   2020 C  CG  . PRO A 1 248 ? 44.518  18.548  7.268   1.00 22.18 ? 248 PRO A CG  1 
ATOM   2021 C  CD  . PRO A 1 248 ? 45.066  19.965  7.125   1.00 21.47 ? 248 PRO A CD  1 
ATOM   2022 N  N   . LEU A 1 249 ? 40.915  19.662  8.635   1.00 18.23 ? 249 LEU A N   1 
ATOM   2023 C  CA  . LEU A 1 249 ? 40.360  19.547  10.009  1.00 17.00 ? 249 LEU A CA  1 
ATOM   2024 C  C   . LEU A 1 249 ? 41.007  18.360  10.716  1.00 17.39 ? 249 LEU A C   1 
ATOM   2025 O  O   . LEU A 1 249 ? 41.157  17.311  10.057  1.00 20.84 ? 249 LEU A O   1 
ATOM   2026 C  CB  . LEU A 1 249 ? 38.854  19.273  9.940   1.00 18.29 ? 249 LEU A CB  1 
ATOM   2027 C  CG  . LEU A 1 249 ? 38.010  20.385  9.320   1.00 18.13 ? 249 LEU A CG  1 
ATOM   2028 C  CD1 . LEU A 1 249 ? 36.537  20.039  9.396   1.00 19.72 ? 249 LEU A CD1 1 
ATOM   2029 C  CD2 . LEU A 1 249 ? 38.286  21.700  10.004  1.00 18.12 ? 249 LEU A CD2 1 
ATOM   2030 N  N   . ASP A 1 250 ? 41.319  18.454  11.976  1.00 17.56 ? 250 ASP A N   1 
ATOM   2031 C  CA  . ASP A 1 250 ? 41.811  17.259  12.691  1.00 19.61 ? 250 ASP A CA  1 
ATOM   2032 C  C   . ASP A 1 250 ? 40.638  16.379  13.132  1.00 18.67 ? 250 ASP A C   1 
ATOM   2033 O  O   . ASP A 1 250 ? 39.446  16.833  13.101  1.00 18.10 ? 250 ASP A O   1 
ATOM   2034 C  CB  . ASP A 1 250 ? 42.742  17.595  13.847  1.00 22.65 ? 250 ASP A CB  1 
ATOM   2035 C  CG  . ASP A 1 250 ? 42.202  18.418  14.977  1.00 27.22 ? 250 ASP A CG  1 
ATOM   2036 O  OD1 . ASP A 1 250 ? 40.992  18.358  15.252  1.00 25.49 ? 250 ASP A OD1 1 
ATOM   2037 O  OD2 . ASP A 1 250 ? 43.060  18.981  15.698  1.00 33.84 ? 250 ASP A OD2 1 
ATOM   2038 N  N   . ASP A 1 251 ? 40.904  15.183  13.626  1.00 17.54 ? 251 ASP A N   1 
ATOM   2039 C  CA  . ASP A 1 251 ? 39.815  14.221  13.894  1.00 18.26 ? 251 ASP A CA  1 
ATOM   2040 C  C   . ASP A 1 251 ? 38.930  14.727  15.044  1.00 16.99 ? 251 ASP A C   1 
ATOM   2041 O  O   . ASP A 1 251 ? 37.714  14.383  15.058  1.00 16.45 ? 251 ASP A O   1 
ATOM   2042 C  CB  . ASP A 1 251 ? 40.398  12.840  14.167  1.00 19.35 ? 251 ASP A CB  1 
ATOM   2043 C  CG  . ASP A 1 251 ? 40.982  12.124  12.961  1.00 22.69 ? 251 ASP A CG  1 
ATOM   2044 O  OD1 . ASP A 1 251 ? 40.795  12.567  11.815  1.00 21.78 ? 251 ASP A OD1 1 
ATOM   2045 O  OD2 . ASP A 1 251 ? 41.639  11.096  13.186  1.00 25.90 ? 251 ASP A OD2 1 
ATOM   2046 N  N   . GLU A 1 252 ? 39.483  15.404  16.052  1.00 16.40 ? 252 GLU A N   1 
ATOM   2047 C  CA  . GLU A 1 252 ? 38.685  15.948  17.165  1.00 17.14 ? 252 GLU A CA  1 
ATOM   2048 C  C   . GLU A 1 252 ? 37.677  16.934  16.572  1.00 16.44 ? 252 GLU A C   1 
ATOM   2049 O  O   . GLU A 1 252 ? 36.508  16.915  16.934  1.00 15.50 ? 252 GLU A O   1 
ATOM   2050 C  CB  . GLU A 1 252 ? 39.571  16.602  18.218  1.00 19.71 ? 252 GLU A CB  1 
ATOM   2051 C  CG  . GLU A 1 252 ? 38.801  17.132  19.407  1.00 22.00 ? 252 GLU A CG  1 
ATOM   2052 C  CD  . GLU A 1 252 ? 39.666  17.857  20.419  1.00 28.40 ? 252 GLU A CD  1 
ATOM   2053 O  OE1 . GLU A 1 252 ? 40.908  17.857  20.266  1.00 32.64 ? 252 GLU A OE1 1 
ATOM   2054 O  OE2 . GLU A 1 252 ? 39.106  18.412  21.368  1.00 32.51 ? 252 GLU A OE2 1 
ATOM   2055 N  N   . ASN A 1 253 ? 38.139  17.837  15.724  1.00 15.76 ? 253 ASN A N   1 
ATOM   2056 C  CA  . ASN A 1 253 ? 37.208  18.865  15.188  1.00 14.61 ? 253 ASN A CA  1 
ATOM   2057 C  C   . ASN A 1 253 ? 36.182  18.209  14.249  1.00 13.10 ? 253 ASN A C   1 
ATOM   2058 O  O   . ASN A 1 253 ? 35.012  18.580  14.325  1.00 13.12 ? 253 ASN A O   1 
ATOM   2059 C  CB  . ASN A 1 253 ? 37.945  19.999  14.484  1.00 14.44 ? 253 ASN A CB  1 
ATOM   2060 C  CG  . ASN A 1 253 ? 36.987  21.092  14.060  1.00 13.64 ? 253 ASN A CG  1 
ATOM   2061 O  OD1 . ASN A 1 253 ? 36.508  21.107  12.936  1.00 13.68 ? 253 ASN A OD1 1 
ATOM   2062 N  ND2 . ASN A 1 253 ? 36.603  21.957  14.979  1.00 14.73 ? 253 ASN A ND2 1 
ATOM   2063 N  N   . ILE A 1 254 ? 36.533  17.139  13.553  1.00 13.15 ? 254 ILE A N   1 
ATOM   2064 C  CA  . ILE A 1 254 ? 35.567  16.412  12.707  1.00 13.10 ? 254 ILE A CA  1 
ATOM   2065 C  C   . ILE A 1 254 ? 34.492  15.824  13.622  1.00 13.36 ? 254 ILE A C   1 
ATOM   2066 O  O   . ILE A 1 254 ? 33.295  15.929  13.256  1.00 13.55 ? 254 ILE A O   1 
ATOM   2067 C  CB  . ILE A 1 254 ? 36.237  15.339  11.809  1.00 14.36 ? 254 ILE A CB  1 
ATOM   2068 C  CG1 . ILE A 1 254 ? 37.121  16.020  10.763  1.00 14.83 ? 254 ILE A CG1 1 
ATOM   2069 C  CG2 . ILE A 1 254 ? 35.182  14.483  11.141  1.00 14.79 ? 254 ILE A CG2 1 
ATOM   2070 C  CD1 . ILE A 1 254 ? 37.937  15.002  9.977   1.00 17.17 ? 254 ILE A CD1 1 
ATOM   2071 N  N   . ARG A 1 255 ? 34.887  15.284  14.790  1.00 14.48 ? 255 ARG A N   1 
ATOM   2072 C  CA  . ARG A 1 255 ? 33.893  14.733  15.741  1.00 13.63 ? 255 ARG A CA  1 
ATOM   2073 C  C   . ARG A 1 255 ? 32.915  15.841  16.162  1.00 12.47 ? 255 ARG A C   1 
ATOM   2074 O  O   . ARG A 1 255 ? 31.685  15.609  16.153  1.00 12.03 ? 255 ARG A O   1 
ATOM   2075 C  CB  . ARG A 1 255 ? 34.598  14.157  16.957  1.00 15.40 ? 255 ARG A CB  1 
ATOM   2076 C  CG  . ARG A 1 255 ? 33.646  13.758  18.069  1.00 16.63 ? 255 ARG A CG  1 
ATOM   2077 C  CD  . ARG A 1 255 ? 34.098  14.336  19.366  1.00 19.66 ? 255 ARG A CD  1 
ATOM   2078 N  NE  . ARG A 1 255 ? 35.230  13.549  19.863  1.00 19.64 ? 255 ARG A NE  1 
ATOM   2079 C  CZ  . ARG A 1 255 ? 35.981  13.854  20.903  1.00 22.67 ? 255 ARG A CZ  1 
ATOM   2080 N  NH1 . ARG A 1 255 ? 35.838  15.009  21.522  1.00 23.53 ? 255 ARG A NH1 1 
ATOM   2081 N  NH2 . ARG A 1 255 ? 36.940  13.026  21.274  1.00 23.81 ? 255 ARG A NH2 1 
ATOM   2082 N  N   . TYR A 1 256 ? 33.434  17.010  16.500  1.00 11.70 ? 256 TYR A N   1 
ATOM   2083 C  CA  . TYR A 1 256 ? 32.568  18.137  16.924  1.00 13.02 ? 256 TYR A CA  1 
ATOM   2084 C  C   . TYR A 1 256 ? 31.637  18.547  15.779  1.00 12.43 ? 256 TYR A C   1 
ATOM   2085 O  O   . TYR A 1 256 ? 30.463  18.845  16.065  1.00 11.61 ? 256 TYR A O   1 
ATOM   2086 C  CB  . TYR A 1 256 ? 33.395  19.350  17.333  1.00 12.83 ? 256 TYR A CB  1 
ATOM   2087 C  CG  . TYR A 1 256 ? 34.207  19.148  18.590  1.00 16.50 ? 256 TYR A CG  1 
ATOM   2088 C  CD1 . TYR A 1 256 ? 33.714  18.460  19.676  1.00 17.32 ? 256 TYR A CD1 1 
ATOM   2089 C  CD2 . TYR A 1 256 ? 35.476  19.709  18.697  1.00 18.42 ? 256 TYR A CD2 1 
ATOM   2090 C  CE1 . TYR A 1 256 ? 34.485  18.262  20.823  1.00 19.12 ? 256 TYR A CE1 1 
ATOM   2091 C  CE2 . TYR A 1 256 ? 36.243  19.557  19.830  1.00 19.23 ? 256 TYR A CE2 1 
ATOM   2092 C  CZ  . TYR A 1 256 ? 35.754  18.812  20.863  1.00 19.02 ? 256 TYR A CZ  1 
ATOM   2093 O  OH  . TYR A 1 256 ? 36.602  18.739  21.953  1.00 26.32 ? 256 TYR A OH  1 
ATOM   2094 N  N   . GLN A 1 257 ? 32.082  18.568  14.533  1.00 12.25 ? 257 GLN A N   1 
ATOM   2095 C  CA  . GLN A 1 257 ? 31.173  18.889  13.421  1.00 11.26 ? 257 GLN A CA  1 
ATOM   2096 C  C   . GLN A 1 257 ? 30.077  17.807  13.331  1.00 12.37 ? 257 GLN A C   1 
ATOM   2097 O  O   . GLN A 1 257 ? 28.919  18.163  13.114  1.00 11.40 ? 257 GLN A O   1 
ATOM   2098 C  CB  . GLN A 1 257 ? 31.867  19.018  12.055  1.00 11.05 ? 257 GLN A CB  1 
ATOM   2099 C  CG  . GLN A 1 257 ? 33.078  19.963  12.027  1.00 12.03 ? 257 GLN A CG  1 
ATOM   2100 C  CD  . GLN A 1 257 ? 32.781  21.390  12.426  1.00 12.08 ? 257 GLN A CD  1 
ATOM   2101 O  OE1 . GLN A 1 257 ? 31.629  21.811  12.554  1.00 12.41 ? 257 GLN A OE1 1 
ATOM   2102 N  NE2 . GLN A 1 257 ? 33.850  22.151  12.645  1.00 13.12 ? 257 GLN A NE2 1 
ATOM   2103 N  N   . ILE A 1 258 ? 30.431  16.525  13.407  1.00 12.30 ? 258 ILE A N   1 
ATOM   2104 C  CA  . ILE A 1 258 ? 29.399  15.468  13.289  1.00 13.01 ? 258 ILE A CA  1 
ATOM   2105 C  C   . ILE A 1 258 ? 28.374  15.618  14.409  1.00 11.97 ? 258 ILE A C   1 
ATOM   2106 O  O   . ILE A 1 258 ? 27.180  15.515  14.136  1.00 11.80 ? 258 ILE A O   1 
ATOM   2107 C  CB  . ILE A 1 258 ? 30.073  14.097  13.248  1.00 14.70 ? 258 ILE A CB  1 
ATOM   2108 C  CG1 . ILE A 1 258 ? 30.902  13.981  11.972  1.00 16.29 ? 258 ILE A CG1 1 
ATOM   2109 C  CG2 . ILE A 1 258 ? 29.019  12.997  13.372  1.00 13.90 ? 258 ILE A CG2 1 
ATOM   2110 C  CD1 . ILE A 1 258 ? 31.656  12.711  11.855  1.00 19.63 ? 258 ILE A CD1 1 
ATOM   2111 N  N   . ILE A 1 259 ? 28.836  15.829  15.624  1.00 12.46 ? 259 ILE A N   1 
ATOM   2112 C  CA  . ILE A 1 259 ? 27.904  15.982  16.772  1.00 12.63 ? 259 ILE A CA  1 
ATOM   2113 C  C   . ILE A 1 259 ? 26.976  17.163  16.466  1.00 12.22 ? 259 ILE A C   1 
ATOM   2114 O  O   . ILE A 1 259 ? 25.757  17.079  16.663  1.00 11.79 ? 259 ILE A O   1 
ATOM   2115 C  CB  . ILE A 1 259 ? 28.681  16.125  18.076  1.00 14.13 ? 259 ILE A CB  1 
ATOM   2116 C  CG1 . ILE A 1 259 ? 29.330  14.781  18.439  1.00 15.06 ? 259 ILE A CG1 1 
ATOM   2117 C  CG2 . ILE A 1 259 ? 27.776  16.690  19.160  1.00 13.46 ? 259 ILE A CG2 1 
ATOM   2118 C  CD1 . ILE A 1 259 ? 30.211  14.791  19.674  1.00 17.04 ? 259 ILE A CD1 1 
ATOM   2119 N  N   . THR A 1 260 ? 27.562  18.240  15.942  1.00 11.44 ? 260 THR A N   1 
ATOM   2120 C  CA  . THR A 1 260 ? 26.795  19.461  15.642  1.00 12.24 ? 260 THR A CA  1 
ATOM   2121 C  C   . THR A 1 260 ? 25.710  19.166  14.600  1.00 11.28 ? 260 THR A C   1 
ATOM   2122 O  O   . THR A 1 260 ? 24.559  19.606  14.719  1.00 12.17 ? 260 THR A O   1 
ATOM   2123 C  CB  . THR A 1 260 ? 27.735  20.574  15.183  1.00 11.63 ? 260 THR A CB  1 
ATOM   2124 O  OG1 . THR A 1 260 ? 28.663  20.844  16.233  1.00 13.91 ? 260 THR A OG1 1 
ATOM   2125 C  CG2 . THR A 1 260 ? 26.920  21.790  14.824  1.00 12.94 ? 260 THR A CG2 1 
ATOM   2126 N  N   . PHE A 1 261 ? 26.092  18.482  13.516  1.00 12.01 ? 261 PHE A N   1 
ATOM   2127 C  CA  . PHE A 1 261 ? 25.121  18.196  12.436  1.00 12.34 ? 261 PHE A CA  1 
ATOM   2128 C  C   . PHE A 1 261 ? 24.016  17.272  12.929  1.00 12.70 ? 261 PHE A C   1 
ATOM   2129 O  O   . PHE A 1 261 ? 22.880  17.411  12.470  1.00 13.25 ? 261 PHE A O   1 
ATOM   2130 C  CB  . PHE A 1 261 ? 25.822  17.569  11.241  1.00 13.21 ? 261 PHE A CB  1 
ATOM   2131 C  CG  . PHE A 1 261 ? 26.856  18.437  10.601  1.00 14.17 ? 261 PHE A CG  1 
ATOM   2132 C  CD1 . PHE A 1 261 ? 26.738  19.803  10.589  1.00 15.51 ? 261 PHE A CD1 1 
ATOM   2133 C  CD2 . PHE A 1 261 ? 27.975  17.861  10.022  1.00 18.04 ? 261 PHE A CD2 1 
ATOM   2134 C  CE1 . PHE A 1 261 ? 27.689  20.581  9.946   1.00 19.85 ? 261 PHE A CE1 1 
ATOM   2135 C  CE2 . PHE A 1 261 ? 28.930  18.650  9.412   1.00 17.73 ? 261 PHE A CE2 1 
ATOM   2136 C  CZ  . PHE A 1 261 ? 28.770  19.997  9.357   1.00 18.06 ? 261 PHE A CZ  1 
ATOM   2137 N  N   . LEU A 1 262 ? 24.351  16.329  13.798  1.00 12.02 ? 262 LEU A N   1 
ATOM   2138 C  CA  . LEU A 1 262 ? 23.314  15.412  14.354  1.00 14.23 ? 262 LEU A CA  1 
ATOM   2139 C  C   . LEU A 1 262 ? 22.366  16.189  15.271  1.00 13.43 ? 262 LEU A C   1 
ATOM   2140 O  O   . LEU A 1 262 ? 21.138  15.906  15.254  1.00 14.28 ? 262 LEU A O   1 
ATOM   2141 C  CB  . LEU A 1 262 ? 23.977  14.248  15.090  1.00 13.65 ? 262 LEU A CB  1 
ATOM   2142 C  CG  . LEU A 1 262 ? 24.726  13.294  14.176  1.00 14.89 ? 262 LEU A CG  1 
ATOM   2143 C  CD1 . LEU A 1 262 ? 25.537  12.286  14.972  1.00 16.07 ? 262 LEU A CD1 1 
ATOM   2144 C  CD2 . LEU A 1 262 ? 23.794  12.600  13.229  1.00 16.35 ? 262 LEU A CD2 1 
ATOM   2145 N  N   . ILE A 1 263 ? 22.875  17.092  16.092  1.00 12.29 ? 263 ILE A N   1 
ATOM   2146 C  CA  . ILE A 1 263 ? 21.999  17.979  16.900  1.00 12.87 ? 263 ILE A CA  1 
ATOM   2147 C  C   . ILE A 1 263 ? 21.061  18.719  15.946  1.00 13.16 ? 263 ILE A C   1 
ATOM   2148 O  O   . ILE A 1 263 ? 19.831  18.765  16.183  1.00 12.15 ? 263 ILE A O   1 
ATOM   2149 C  CB  . ILE A 1 263 ? 22.845  18.965  17.723  1.00 13.18 ? 263 ILE A CB  1 
ATOM   2150 C  CG1 . ILE A 1 263 ? 23.666  18.305  18.858  1.00 13.94 ? 263 ILE A CG1 1 
ATOM   2151 C  CG2 . ILE A 1 263 ? 21.987  20.085  18.286  1.00 14.41 ? 263 ILE A CG2 1 
ATOM   2152 C  CD1 . ILE A 1 263 ? 24.748  19.197  19.371  1.00 16.35 ? 263 ILE A CD1 1 
ATOM   2153 N  N   . ALA A 1 264 ? 21.613  19.347  14.905  1.00 12.73 ? 264 ALA A N   1 
ATOM   2154 C  CA  . ALA A 1 264 ? 20.763  20.110  13.954  1.00 15.00 ? 264 ALA A CA  1 
ATOM   2155 C  C   . ALA A 1 264 ? 19.717  19.230  13.315  1.00 15.91 ? 264 ALA A C   1 
ATOM   2156 O  O   . ALA A 1 264 ? 18.544  19.660  13.252  1.00 17.71 ? 264 ALA A O   1 
ATOM   2157 C  CB  . ALA A 1 264 ? 21.619  20.768  12.910  1.00 15.35 ? 264 ALA A CB  1 
ATOM   2158 N  N   . GLY A 1 265 ? 20.129  18.092  12.808  1.00 15.91 ? 265 GLY A N   1 
ATOM   2159 C  CA  . GLY A 1 265 ? 19.180  17.225  12.091  1.00 18.98 ? 265 GLY A CA  1 
ATOM   2160 C  C   . GLY A 1 265 ? 18.059  16.804  13.013  1.00 18.97 ? 265 GLY A C   1 
ATOM   2161 O  O   . GLY A 1 265 ? 16.868  16.779  12.547  1.00 23.24 ? 265 GLY A O   1 
ATOM   2162 N  N   . HIS A 1 266 ? 18.377  16.424  14.253  1.00 14.24 ? 266 HIS A N   1 
ATOM   2163 C  CA  . HIS A 1 266 ? 17.350  15.969  15.230  1.00 14.66 ? 266 HIS A CA  1 
ATOM   2164 C  C   . HIS A 1 266 ? 16.390  17.099  15.587  1.00 14.63 ? 266 HIS A C   1 
ATOM   2165 O  O   . HIS A 1 266 ? 15.181  16.845  15.753  1.00 16.72 ? 266 HIS A O   1 
ATOM   2166 C  CB  . HIS A 1 266 ? 18.052  15.456  16.476  1.00 14.67 ? 266 HIS A CB  1 
ATOM   2167 C  CG  . HIS A 1 266 ? 17.164  14.809  17.459  1.00 14.74 ? 266 HIS A CG  1 
ATOM   2168 N  ND1 . HIS A 1 266 ? 16.538  15.525  18.445  1.00 15.97 ? 266 HIS A ND1 1 
ATOM   2169 C  CD2 . HIS A 1 266 ? 16.849  13.515  17.659  1.00 16.01 ? 266 HIS A CD2 1 
ATOM   2170 C  CE1 . HIS A 1 266 ? 15.814  14.691  19.173  1.00 17.72 ? 266 HIS A CE1 1 
ATOM   2171 N  NE2 . HIS A 1 266 ? 16.014  13.479  18.733  1.00 16.62 ? 266 HIS A NE2 1 
ATOM   2172 N  N   . GLU A 1 267 ? 16.935  18.299  15.807  1.00 13.80 ? 267 GLU A N   1 
ATOM   2173 C  CA  . GLU A 1 267 ? 16.176  19.362  16.519  1.00 14.27 ? 267 GLU A CA  1 
ATOM   2174 C  C   . GLU A 1 267 ? 15.428  20.288  15.540  1.00 14.77 ? 267 GLU A C   1 
ATOM   2175 O  O   . GLU A 1 267 ? 14.352  20.789  15.911  1.00 16.52 ? 267 GLU A O   1 
ATOM   2176 C  CB  . GLU A 1 267 ? 17.150  20.204  17.348  1.00 15.78 ? 267 GLU A CB  1 
ATOM   2177 C  CG  . GLU A 1 267 ? 17.734  19.465  18.512  1.00 16.85 ? 267 GLU A CG  1 
ATOM   2178 C  CD  . GLU A 1 267 ? 16.754  19.110  19.609  1.00 21.35 ? 267 GLU A CD  1 
ATOM   2179 O  OE1 . GLU A 1 267 ? 16.508  19.991  20.455  1.00 24.20 ? 267 GLU A OE1 1 
ATOM   2180 O  OE2 . GLU A 1 267 ? 16.195  18.028  19.563  1.00 22.90 ? 267 GLU A OE2 1 
ATOM   2181 N  N   . THR A 1 268 ? 15.995  20.632  14.388  1.00 14.55 ? 268 THR A N   1 
ATOM   2182 C  CA  . THR A 1 268 ? 15.518  21.805  13.618  1.00 15.39 ? 268 THR A CA  1 
ATOM   2183 C  C   . THR A 1 268 ? 14.556  21.467  12.500  1.00 13.78 ? 268 THR A C   1 
ATOM   2184 O  O   . THR A 1 268 ? 13.430  21.871  12.545  1.00 14.71 ? 268 THR A O   1 
ATOM   2185 C  CB  . THR A 1 268 ? 16.717  22.568  13.050  1.00 15.49 ? 268 THR A CB  1 
ATOM   2186 O  OG1 . THR A 1 268 ? 17.388  21.737  12.113  1.00 19.76 ? 268 THR A OG1 1 
ATOM   2187 C  CG2 . THR A 1 268 ? 17.662  22.975  14.147  1.00 19.39 ? 268 THR A CG2 1 
ATOM   2188 N  N   . THR A 1 269 ? 14.990  20.760  11.483  1.00 13.89 ? 269 THR A N   1 
ATOM   2189 C  CA  . THR A 1 269 ? 14.134  20.505  10.312  1.00 13.79 ? 269 THR A CA  1 
ATOM   2190 C  C   . THR A 1 269 ? 12.864  19.794  10.771  1.00 12.17 ? 269 THR A C   1 
ATOM   2191 O  O   . THR A 1 269 ? 11.812  19.974  10.142  1.00 13.30 ? 269 THR A O   1 
ATOM   2192 C  CB  . THR A 1 269 ? 14.882  19.686  9.261   1.00 13.44 ? 269 THR A CB  1 
ATOM   2193 O  OG1 . THR A 1 269 ? 16.120  20.385  9.037   1.00 16.01 ? 269 THR A OG1 1 
ATOM   2194 C  CG2 . THR A 1 269 ? 14.138  19.643  7.963   1.00 15.28 ? 269 THR A CG2 1 
ATOM   2195 N  N   . SER A 1 270 ? 12.966  18.902  11.750  1.00 12.25 ? 270 SER A N   1 
ATOM   2196 C  CA  . SER A 1 270 ? 11.784  18.173  12.255  1.00 11.52 ? 270 SER A CA  1 
ATOM   2197 C  C   . SER A 1 270 ? 10.745  19.131  12.843  1.00 11.75 ? 270 SER A C   1 
ATOM   2198 O  O   . SER A 1 270 ? 9.543   18.884  12.671  1.00 12.83 ? 270 SER A O   1 
ATOM   2199 C  CB  . SER A 1 270 ? 12.200  17.122  13.267  1.00 13.13 ? 270 SER A CB  1 
ATOM   2200 O  OG  . SER A 1 270 ? 12.995  17.726  14.271  1.00 14.28 ? 270 SER A OG  1 
ATOM   2201 N  N   . GLY A 1 271 ? 11.197  20.164  13.521  1.00 11.95 ? 271 GLY A N   1 
ATOM   2202 C  CA  . GLY A 1 271 ? 10.254  21.180  14.012  1.00 11.03 ? 271 GLY A CA  1 
ATOM   2203 C  C   . GLY A 1 271 ? 9.557   21.907  12.872  1.00 11.26 ? 271 GLY A C   1 
ATOM   2204 O  O   . GLY A 1 271 ? 8.337   22.113  12.912  1.00 11.19 ? 271 GLY A O   1 
ATOM   2205 N  N   . LEU A 1 272 ? 10.331  22.321  11.888  1.00 11.25 ? 272 LEU A N   1 
ATOM   2206 C  CA  . LEU A 1 272 ? 9.771   23.013  10.698  1.00 11.32 ? 272 LEU A CA  1 
ATOM   2207 C  C   . LEU A 1 272 ? 8.696   22.141  10.068  1.00 12.24 ? 272 LEU A C   1 
ATOM   2208 O  O   . LEU A 1 272 ? 7.571   22.602  9.785   1.00 12.10 ? 272 LEU A O   1 
ATOM   2209 C  CB  . LEU A 1 272 ? 10.909  23.316  9.742   1.00 11.90 ? 272 LEU A CB  1 
ATOM   2210 C  CG  . LEU A 1 272 ? 10.463  23.783  8.353   1.00 13.04 ? 272 LEU A CG  1 
ATOM   2211 C  CD1 . LEU A 1 272 ? 9.476   24.943  8.423   1.00 13.20 ? 272 LEU A CD1 1 
ATOM   2212 C  CD2 . LEU A 1 272 ? 11.640  24.123  7.470   1.00 14.74 ? 272 LEU A CD2 1 
ATOM   2213 N  N   . LEU A 1 273 ? 9.020   20.878  9.827   1.00 10.20 ? 273 LEU A N   1 
ATOM   2214 C  CA  . LEU A 1 273 ? 8.022   20.021  9.137   1.00 11.11 ? 273 LEU A CA  1 
ATOM   2215 C  C   . LEU A 1 273 ? 6.765   19.847  9.998   1.00 11.65 ? 273 LEU A C   1 
ATOM   2216 O  O   . LEU A 1 273 ? 5.639   19.815  9.519   1.00 12.37 ? 273 LEU A O   1 
ATOM   2217 C  CB  . LEU A 1 273 ? 8.651   18.675  8.836   1.00 11.52 ? 273 LEU A CB  1 
ATOM   2218 C  CG  . LEU A 1 273 ? 9.517   18.666  7.576   1.00 10.55 ? 273 LEU A CG  1 
ATOM   2219 C  CD1 . LEU A 1 273 ? 10.384  17.435  7.571   1.00 12.07 ? 273 LEU A CD1 1 
ATOM   2220 C  CD2 . LEU A 1 273 ? 8.618   18.726  6.337   1.00 10.76 ? 273 LEU A CD2 1 
ATOM   2221 N  N   . SER A 1 274 ? 6.954   19.756  11.294  1.00 11.15 ? 274 SER A N   1 
ATOM   2222 C  CA  . SER A 1 274 ? 5.825   19.538  12.225  1.00 11.42 ? 274 SER A CA  1 
ATOM   2223 C  C   . SER A 1 274 ? 4.960   20.801  12.244  1.00 11.11 ? 274 SER A C   1 
ATOM   2224 O  O   . SER A 1 274 ? 3.719   20.704  12.152  1.00 10.84 ? 274 SER A O   1 
ATOM   2225 C  CB  . SER A 1 274 ? 6.305   19.227  13.645  1.00 11.57 ? 274 SER A CB  1 
ATOM   2226 O  OG  . SER A 1 274 ? 7.068   18.025  13.621  1.00 13.18 ? 274 SER A OG  1 
ATOM   2227 N  N   . PHE A 1 275 ? 5.573   21.977  12.341  1.00 11.71 ? 275 PHE A N   1 
ATOM   2228 C  CA  . PHE A 1 275 ? 4.749   23.224  12.326  1.00 10.62 ? 275 PHE A CA  1 
ATOM   2229 C  C   . PHE A 1 275 ? 4.061   23.408  10.976  1.00 11.04 ? 275 PHE A C   1 
ATOM   2230 O  O   . PHE A 1 275 ? 2.941   23.882  10.888  1.00 11.53 ? 275 PHE A O   1 
ATOM   2231 C  CB  . PHE A 1 275 ? 5.604   24.469  12.618  1.00 11.32 ? 275 PHE A CB  1 
ATOM   2232 C  CG  . PHE A 1 275 ? 5.873   24.666  14.084  1.00 11.67 ? 275 PHE A CG  1 
ATOM   2233 C  CD1 . PHE A 1 275 ? 4.831   24.985  14.933  1.00 11.77 ? 275 PHE A CD1 1 
ATOM   2234 C  CD2 . PHE A 1 275 ? 7.156   24.565  14.582  1.00 13.09 ? 275 PHE A CD2 1 
ATOM   2235 C  CE1 . PHE A 1 275 ? 5.084   25.178  16.288  1.00 13.47 ? 275 PHE A CE1 1 
ATOM   2236 C  CE2 . PHE A 1 275 ? 7.388   24.724  15.940  1.00 13.31 ? 275 PHE A CE2 1 
ATOM   2237 C  CZ  . PHE A 1 275 ? 6.353   25.036  16.771  1.00 14.45 ? 275 PHE A CZ  1 
ATOM   2238 N  N   . ALA A 1 276 ? 4.755   23.084  9.885   1.00 11.28 ? 276 ALA A N   1 
ATOM   2239 C  CA  . ALA A 1 276 ? 4.159   23.209  8.537   1.00 12.06 ? 276 ALA A CA  1 
ATOM   2240 C  C   . ALA A 1 276 ? 2.911   22.325  8.444   1.00 11.85 ? 276 ALA A C   1 
ATOM   2241 O  O   . ALA A 1 276 ? 1.871   22.804  7.994   1.00 12.21 ? 276 ALA A O   1 
ATOM   2242 C  CB  . ALA A 1 276 ? 5.158   22.851  7.459   1.00 12.26 ? 276 ALA A CB  1 
ATOM   2243 N  N   . LEU A 1 277 ? 3.005   21.075  8.853   1.00 11.38 ? 277 LEU A N   1 
ATOM   2244 C  CA  . LEU A 1 277 ? 1.811   20.207  8.815   1.00 11.99 ? 277 LEU A CA  1 
ATOM   2245 C  C   . LEU A 1 277 ? 0.713   20.731  9.752   1.00 11.80 ? 277 LEU A C   1 
ATOM   2246 O  O   . LEU A 1 277 ? -0.487  20.673  9.386   1.00 11.48 ? 277 LEU A O   1 
ATOM   2247 C  CB  . LEU A 1 277 ? 2.173   18.769  9.127   1.00 13.19 ? 277 LEU A CB  1 
ATOM   2248 C  CG  . LEU A 1 277 ? 1.025   17.808  8.877   1.00 16.54 ? 277 LEU A CG  1 
ATOM   2249 C  CD1 . LEU A 1 277 ? 0.533   17.826  7.453   1.00 16.92 ? 277 LEU A CD1 1 
ATOM   2250 C  CD2 . LEU A 1 277 ? 1.422   16.413  9.241   1.00 17.66 ? 277 LEU A CD2 1 
ATOM   2251 N  N   . TYR A 1 278 ? 1.075   21.290  10.902  1.00 10.90 ? 278 TYR A N   1 
ATOM   2252 C  CA  . TYR A 1 278 ? 0.095   21.916  11.827  1.00 10.80 ? 278 TYR A CA  1 
ATOM   2253 C  C   . TYR A 1 278 ? -0.640  23.032  11.094  1.00 11.08 ? 278 TYR A C   1 
ATOM   2254 O  O   . TYR A 1 278 ? -1.895  23.051  11.076  1.00 11.40 ? 278 TYR A O   1 
ATOM   2255 C  CB  . TYR A 1 278 ? 0.817   22.400  13.090  1.00 11.89 ? 278 TYR A CB  1 
ATOM   2256 C  CG  . TYR A 1 278 ? -0.042  23.340  13.885  1.00 11.69 ? 278 TYR A CG  1 
ATOM   2257 C  CD1 . TYR A 1 278 ? -0.970  22.816  14.790  1.00 12.49 ? 278 TYR A CD1 1 
ATOM   2258 C  CD2 . TYR A 1 278 ? 0.005   24.703  13.718  1.00 12.39 ? 278 TYR A CD2 1 
ATOM   2259 C  CE1 . TYR A 1 278 ? -1.806  23.669  15.498  1.00 12.50 ? 278 TYR A CE1 1 
ATOM   2260 C  CE2 . TYR A 1 278 ? -0.811  25.562  14.439  1.00 12.75 ? 278 TYR A CE2 1 
ATOM   2261 C  CZ  . TYR A 1 278 ? -1.760  25.036  15.299  1.00 12.53 ? 278 TYR A CZ  1 
ATOM   2262 O  OH  . TYR A 1 278 ? -2.619  25.873  16.004  1.00 15.00 ? 278 TYR A OH  1 
ATOM   2263 N  N   . PHE A 1 279 ? 0.084   23.947  10.464  1.00 10.81 ? 279 PHE A N   1 
ATOM   2264 C  CA  . PHE A 1 279 ? -0.590  25.078  9.796   1.00 11.14 ? 279 PHE A CA  1 
ATOM   2265 C  C   . PHE A 1 279 ? -1.428  24.569  8.633   1.00 13.47 ? 279 PHE A C   1 
ATOM   2266 O  O   . PHE A 1 279 ? -2.496  25.143  8.421   1.00 13.42 ? 279 PHE A O   1 
ATOM   2267 C  CB  . PHE A 1 279 ? 0.441   26.127  9.412   1.00 10.67 ? 279 PHE A CB  1 
ATOM   2268 C  CG  . PHE A 1 279 ? 0.891   26.938  10.597  1.00 11.26 ? 279 PHE A CG  1 
ATOM   2269 C  CD1 . PHE A 1 279 ? -0.048  27.731  11.249  1.00 11.43 ? 279 PHE A CD1 1 
ATOM   2270 C  CD2 . PHE A 1 279 ? 2.224   26.964  11.008  1.00 12.30 ? 279 PHE A CD2 1 
ATOM   2271 C  CE1 . PHE A 1 279 ? 0.317   28.534  12.317  1.00 12.88 ? 279 PHE A CE1 1 
ATOM   2272 C  CE2 . PHE A 1 279 ? 2.580   27.812  12.053  1.00 13.93 ? 279 PHE A CE2 1 
ATOM   2273 C  CZ  . PHE A 1 279 ? 1.627   28.539  12.738  1.00 13.64 ? 279 PHE A CZ  1 
ATOM   2274 N  N   . LEU A 1 280 ? -0.998  23.531  7.939   1.00 12.15 ? 280 LEU A N   1 
ATOM   2275 C  CA  . LEU A 1 280 ? -1.774  23.027  6.779   1.00 12.18 ? 280 LEU A CA  1 
ATOM   2276 C  C   . LEU A 1 280 ? -3.108  22.471  7.275   1.00 13.40 ? 280 LEU A C   1 
ATOM   2277 O  O   . LEU A 1 280 ? -4.140  22.755  6.662   1.00 13.66 ? 280 LEU A O   1 
ATOM   2278 C  CB  . LEU A 1 280 ? -0.964  22.013  6.007   1.00 13.75 ? 280 LEU A CB  1 
ATOM   2279 C  CG  . LEU A 1 280 ? 0.177   22.620  5.194   1.00 15.06 ? 280 LEU A CG  1 
ATOM   2280 C  CD1 . LEU A 1 280 ? 1.006   21.484  4.649   1.00 18.33 ? 280 LEU A CD1 1 
ATOM   2281 C  CD2 . LEU A 1 280 ? -0.345  23.551  4.103   1.00 19.61 ? 280 LEU A CD2 1 
ATOM   2282 N  N   . VAL A 1 281 ? -3.118  21.672  8.329   1.00 12.36 ? 281 VAL A N   1 
ATOM   2283 C  CA  . VAL A 1 281 ? -4.404  21.043  8.747   1.00 12.26 ? 281 VAL A CA  1 
ATOM   2284 C  C   . VAL A 1 281 ? -5.308  22.096  9.365   1.00 13.71 ? 281 VAL A C   1 
ATOM   2285 O  O   . VAL A 1 281 ? -6.545  21.937  9.302   1.00 16.04 ? 281 VAL A O   1 
ATOM   2286 C  CB  . VAL A 1 281 ? -4.221  19.832  9.656   1.00 13.10 ? 281 VAL A CB  1 
ATOM   2287 C  CG1 . VAL A 1 281 ? -3.443  18.736  8.950   1.00 14.22 ? 281 VAL A CG1 1 
ATOM   2288 C  CG2 . VAL A 1 281 ? -3.596  20.129  10.995  1.00 13.10 ? 281 VAL A CG2 1 
ATOM   2289 N  N   . LYS A 1 282 ? -4.741  23.172  9.875   1.00 12.08 ? 282 LYS A N   1 
ATOM   2290 C  CA  . LYS A 1 282 ? -5.537  24.263  10.438  1.00 12.92 ? 282 LYS A CA  1 
ATOM   2291 C  C   . LYS A 1 282 ? -6.044  25.220  9.357   1.00 13.53 ? 282 LYS A C   1 
ATOM   2292 O  O   . LYS A 1 282 ? -6.935  26.064  9.635   1.00 14.97 ? 282 LYS A O   1 
ATOM   2293 C  CB  . LYS A 1 282 ? -4.761  25.018  11.524  1.00 13.83 ? 282 LYS A CB  1 
ATOM   2294 C  CG  . LYS A 1 282 ? -4.434  24.198  12.780  1.00 14.07 ? 282 LYS A CG  1 
ATOM   2295 C  CD  . LYS A 1 282 ? -5.662  23.655  13.505  1.00 13.56 ? 282 LYS A CD  1 
ATOM   2296 C  CE  . LYS A 1 282 ? -5.242  23.000  14.788  1.00 14.77 ? 282 LYS A CE  1 
ATOM   2297 N  NZ  . LYS A 1 282 ? -6.407  22.461  15.541  1.00 15.22 ? 282 LYS A NZ  1 
ATOM   2298 N  N   . ASN A 1 283 ? -5.490  25.168  8.143   1.00 13.28 ? 283 ASN A N   1 
ATOM   2299 C  CA  . ASN A 1 283 ? -5.813  26.105  7.061   1.00 13.43 ? 283 ASN A CA  1 
ATOM   2300 C  C   . ASN A 1 283 ? -6.061  25.271  5.815   1.00 12.44 ? 283 ASN A C   1 
ATOM   2301 O  O   . ASN A 1 283 ? -5.216  25.210  4.898   1.00 12.86 ? 283 ASN A O   1 
ATOM   2302 C  CB  . ASN A 1 283 ? -4.679  27.108  6.877   1.00 13.39 ? 283 ASN A CB  1 
ATOM   2303 C  CG  . ASN A 1 283 ? -4.525  28.022  8.061   1.00 15.92 ? 283 ASN A CG  1 
ATOM   2304 O  OD1 . ASN A 1 283 ? -5.207  29.057  8.166   1.00 17.83 ? 283 ASN A OD1 1 
ATOM   2305 N  ND2 . ASN A 1 283 ? -3.658  27.665  8.988   1.00 13.47 ? 283 ASN A ND2 1 
ATOM   2306 N  N   . PRO A 1 284 ? -7.212  24.593  5.692   1.00 12.82 ? 284 PRO A N   1 
ATOM   2307 C  CA  . PRO A 1 284 ? -7.427  23.652  4.597   1.00 14.99 ? 284 PRO A CA  1 
ATOM   2308 C  C   . PRO A 1 284 ? -7.383  24.240  3.190   1.00 13.73 ? 284 PRO A C   1 
ATOM   2309 O  O   . PRO A 1 284 ? -7.014  23.487  2.279   1.00 13.27 ? 284 PRO A O   1 
ATOM   2310 C  CB  . PRO A 1 284 ? -8.813  23.030  4.861   1.00 17.02 ? 284 PRO A CB  1 
ATOM   2311 C  CG  . PRO A 1 284 ? -9.367  23.764  6.044   1.00 17.70 ? 284 PRO A CG  1 
ATOM   2312 C  CD  . PRO A 1 284 ? -8.296  24.615  6.678   1.00 16.10 ? 284 PRO A CD  1 
ATOM   2313 N  N   . HIS A 1 285 ? -7.663  25.506  3.010   1.00 14.10 ? 285 HIS A N   1 
ATOM   2314 C  CA  . HIS A 1 285 ? -7.482  26.092  1.659   1.00 13.73 ? 285 HIS A CA  1 
ATOM   2315 C  C   . HIS A 1 285 ? -5.997  26.086  1.265   1.00 14.29 ? 285 HIS A C   1 
ATOM   2316 O  O   . HIS A 1 285 ? -5.652  25.931  0.053   1.00 14.93 ? 285 HIS A O   1 
ATOM   2317 C  CB  . HIS A 1 285 ? -8.027  27.507  1.582   1.00 14.17 ? 285 HIS A CB  1 
ATOM   2318 C  CG  . HIS A 1 285 ? -9.508  27.601  1.712   1.00 14.98 ? 285 HIS A CG  1 
ATOM   2319 N  ND1 . HIS A 1 285 ? -10.390 26.836  0.983   1.00 17.33 ? 285 HIS A ND1 1 
ATOM   2320 C  CD2 . HIS A 1 285 ? -10.234 28.458  2.448   1.00 18.53 ? 285 HIS A CD2 1 
ATOM   2321 C  CE1 . HIS A 1 285 ? -11.640 27.233  1.296   1.00 17.52 ? 285 HIS A CE1 1 
ATOM   2322 N  NE2 . HIS A 1 285 ? -11.519 28.208  2.170   1.00 16.47 ? 285 HIS A NE2 1 
ATOM   2323 N  N   . VAL A 1 286 ? -5.117  26.345  2.213   1.00 12.28 ? 286 VAL A N   1 
ATOM   2324 C  CA  . VAL A 1 286 ? -3.658  26.308  1.984   1.00 12.03 ? 286 VAL A CA  1 
ATOM   2325 C  C   . VAL A 1 286 ? -3.232  24.859  1.717   1.00 13.34 ? 286 VAL A C   1 
ATOM   2326 O  O   . VAL A 1 286 ? -2.452  24.608  0.789   1.00 11.96 ? 286 VAL A O   1 
ATOM   2327 C  CB  . VAL A 1 286 ? -2.866  26.902  3.142   1.00 13.80 ? 286 VAL A CB  1 
ATOM   2328 C  CG1 . VAL A 1 286 ? -1.374  26.777  2.862   1.00 15.89 ? 286 VAL A CG1 1 
ATOM   2329 C  CG2 . VAL A 1 286 ? -3.283  28.336  3.445   1.00 15.42 ? 286 VAL A CG2 1 
ATOM   2330 N  N   . LEU A 1 287 ? -3.739  23.919  2.518   1.00 12.80 ? 287 LEU A N   1 
ATOM   2331 C  CA  . LEU A 1 287 ? -3.456  22.496  2.271   1.00 13.99 ? 287 LEU A CA  1 
ATOM   2332 C  C   . LEU A 1 287 ? -3.840  22.166  0.833   1.00 14.16 ? 287 LEU A C   1 
ATOM   2333 O  O   . LEU A 1 287 ? -3.076  21.509  0.099   1.00 14.48 ? 287 LEU A O   1 
ATOM   2334 C  CB  . LEU A 1 287 ? -4.152  21.626  3.332   1.00 13.81 ? 287 LEU A CB  1 
ATOM   2335 C  CG  . LEU A 1 287 ? -3.624  20.201  3.417   1.00 20.50 ? 287 LEU A CG  1 
ATOM   2336 C  CD1 . LEU A 1 287 ? -3.938  19.592  4.781   1.00 22.26 ? 287 LEU A CD1 1 
ATOM   2337 C  CD2 . LEU A 1 287 ? -4.186  19.361  2.325   1.00 21.18 ? 287 LEU A CD2 1 
ATOM   2338 N  N   . GLN A 1 288 ? -5.009  22.590  0.386   1.00 15.21 ? 288 GLN A N   1 
ATOM   2339 C  CA  . GLN A 1 288 ? -5.415  22.212  -0.982  1.00 15.33 ? 288 GLN A CA  1 
ATOM   2340 C  C   . GLN A 1 288 ? -4.495  22.847  -2.057  1.00 13.95 ? 288 GLN A C   1 
ATOM   2341 O  O   . GLN A 1 288 ? -4.159  22.169  -2.988  1.00 13.84 ? 288 GLN A O   1 
ATOM   2342 C  CB  . GLN A 1 288 ? -6.857  22.630  -1.219  1.00 20.33 ? 288 GLN A CB  1 
ATOM   2343 C  CG  . GLN A 1 288 ? -7.393  22.034  -2.527  1.00 26.13 ? 288 GLN A CG  1 
ATOM   2344 C  CD  . GLN A 1 288 ? -7.025  20.566  -2.686  1.00 37.52 ? 288 GLN A CD  1 
ATOM   2345 O  OE1 . GLN A 1 288 ? -7.536  19.678  -1.984  1.00 42.84 ? 288 GLN A OE1 1 
ATOM   2346 N  NE2 . GLN A 1 288 ? -6.038  20.280  -3.541  1.00 39.59 ? 288 GLN A NE2 1 
ATOM   2347 N  N   . LYS A 1 289 ? -4.044  24.073  -1.878  1.00 13.26 ? 289 LYS A N   1 
ATOM   2348 C  CA  . LYS A 1 289 ? -3.122  24.680  -2.856  1.00 13.76 ? 289 LYS A CA  1 
ATOM   2349 C  C   . LYS A 1 289 ? -1.831  23.850  -2.877  1.00 13.32 ? 289 LYS A C   1 
ATOM   2350 O  O   . LYS A 1 289 ? -1.250  23.606  -3.985  1.00 14.28 ? 289 LYS A O   1 
ATOM   2351 C  CB  . LYS A 1 289 ? -2.830  26.134  -2.500  1.00 14.31 ? 289 LYS A CB  1 
ATOM   2352 C  CG  . LYS A 1 289 ? -3.992  27.069  -2.772  1.00 15.14 ? 289 LYS A CG  1 
ATOM   2353 C  CD  . LYS A 1 289 ? -3.627  28.491  -2.411  1.00 15.53 ? 289 LYS A CD  1 
ATOM   2354 C  CE  . LYS A 1 289 ? -4.712  29.522  -2.656  1.00 16.63 ? 289 LYS A CE  1 
ATOM   2355 N  NZ  . LYS A 1 289 ? -5.950  29.179  -1.930  1.00 17.84 ? 289 LYS A NZ  1 
ATOM   2356 N  N   . ALA A 1 290 ? -1.299  23.517  -1.707  1.00 13.10 ? 290 ALA A N   1 
ATOM   2357 C  CA  . ALA A 1 290 ? -0.039  22.764  -1.637  1.00 12.81 ? 290 ALA A CA  1 
ATOM   2358 C  C   . ALA A 1 290 ? -0.216  21.348  -2.213  1.00 12.64 ? 290 ALA A C   1 
ATOM   2359 O  O   . ALA A 1 290 ? 0.719   20.854  -2.924  1.00 12.13 ? 290 ALA A O   1 
ATOM   2360 C  CB  . ALA A 1 290 ? 0.466   22.805  -0.229  1.00 12.99 ? 290 ALA A CB  1 
ATOM   2361 N  N   . ALA A 1 291 ? -1.324  20.686  -1.912  1.00 11.54 ? 291 ALA A N   1 
ATOM   2362 C  CA  . ALA A 1 291 ? -1.600  19.340  -2.443  1.00 11.46 ? 291 ALA A CA  1 
ATOM   2363 C  C   . ALA A 1 291 ? -1.755  19.370  -3.970  1.00 11.59 ? 291 ALA A C   1 
ATOM   2364 O  O   . ALA A 1 291 ? -1.331  18.438  -4.610  1.00 14.14 ? 291 ALA A O   1 
ATOM   2365 C  CB  . ALA A 1 291 ? -2.771  18.724  -1.767  1.00 12.11 ? 291 ALA A CB  1 
ATOM   2366 N  N   . GLU A 1 292 ? -2.413  20.425  -4.475  1.00 13.19 ? 292 GLU A N   1 
ATOM   2367 C  CA  . GLU A 1 292 ? -2.588  20.541  -5.928  1.00 14.04 ? 292 GLU A CA  1 
ATOM   2368 C  C   . GLU A 1 292 ? -1.201  20.687  -6.561  1.00 12.79 ? 292 GLU A C   1 
ATOM   2369 O  O   . GLU A 1 292 ? -0.963  20.068  -7.623  1.00 13.58 ? 292 GLU A O   1 
ATOM   2370 C  CB  . GLU A 1 292 ? -3.460  21.742  -6.255  1.00 16.56 ? 292 GLU A CB  1 
ATOM   2371 C  CG  . GLU A 1 292 ? -3.679  21.937  -7.750  1.00 20.60 ? 292 GLU A CG  1 
ATOM   2372 C  CD  . GLU A 1 292 ? -2.577  22.526  -8.662  1.00 25.09 ? 292 GLU A CD  1 
ATOM   2373 O  OE1 . GLU A 1 292 ? -1.856  23.507  -8.313  1.00 24.43 ? 292 GLU A OE1 1 
ATOM   2374 O  OE2 . GLU A 1 292 ? -2.520  22.039  -9.829  1.00 26.87 ? 292 GLU A OE2 1 
ATOM   2375 N  N   . GLU A 1 293 ? -0.329  21.500  -5.996  1.00 13.21 ? 293 GLU A N   1 
ATOM   2376 C  CA  . GLU A 1 293 ? 1.001   21.710  -6.573  1.00 12.84 ? 293 GLU A CA  1 
ATOM   2377 C  C   . GLU A 1 293 ? 1.725   20.376  -6.545  1.00 13.09 ? 293 GLU A C   1 
ATOM   2378 O  O   . GLU A 1 293 ? 2.405   20.027  -7.525  1.00 13.97 ? 293 GLU A O   1 
ATOM   2379 C  CB  . GLU A 1 293 ? 1.782   22.769  -5.828  1.00 12.24 ? 293 GLU A CB  1 
ATOM   2380 C  CG  . GLU A 1 293 ? 3.174   22.940  -6.382  1.00 14.32 ? 293 GLU A CG  1 
ATOM   2381 C  CD  . GLU A 1 293 ? 3.986   23.982  -5.687  1.00 15.03 ? 293 GLU A CD  1 
ATOM   2382 O  OE1 . GLU A 1 293 ? 4.478   23.638  -4.539  1.00 16.23 ? 293 GLU A OE1 1 
ATOM   2383 O  OE2 . GLU A 1 293 ? 4.159   25.116  -6.230  1.00 17.17 ? 293 GLU A OE2 1 
ATOM   2384 N  N   . ALA A 1 294 ? 1.680   19.670  -5.401  1.00 12.31 ? 294 ALA A N   1 
ATOM   2385 C  CA  . ALA A 1 294 ? 2.386   18.377  -5.298  1.00 13.81 ? 294 ALA A CA  1 
ATOM   2386 C  C   . ALA A 1 294 ? 1.895   17.440  -6.412  1.00 13.88 ? 294 ALA A C   1 
ATOM   2387 O  O   . ALA A 1 294 ? 2.747   16.792  -7.084  1.00 13.48 ? 294 ALA A O   1 
ATOM   2388 C  CB  . ALA A 1 294 ? 2.253   17.842  -3.901  1.00 13.33 ? 294 ALA A CB  1 
ATOM   2389 N  N   . ALA A 1 295 ? 0.600   17.328  -6.609  1.00 13.97 ? 295 ALA A N   1 
ATOM   2390 C  CA  . ALA A 1 295 ? 0.005   16.422  -7.634  1.00 15.19 ? 295 ALA A CA  1 
ATOM   2391 C  C   . ALA A 1 295 ? 0.463   16.847  -9.032  1.00 14.76 ? 295 ALA A C   1 
ATOM   2392 O  O   . ALA A 1 295 ? 0.879   15.942  -9.824  1.00 17.30 ? 295 ALA A O   1 
ATOM   2393 C  CB  . ALA A 1 295 ? -1.504  16.422  -7.568  1.00 15.83 ? 295 ALA A CB  1 
ATOM   2394 N  N   . ARG A 1 296 ? 0.520   18.139  -9.311  1.00 14.79 ? 296 ARG A N   1 
ATOM   2395 C  CA  . ARG A 1 296 ? 0.844   18.666  -10.668 1.00 15.48 ? 296 ARG A CA  1 
ATOM   2396 C  C   . ARG A 1 296 ? 2.326   18.438  -10.943 1.00 16.07 ? 296 ARG A C   1 
ATOM   2397 O  O   . ARG A 1 296 ? 2.708   18.168  -12.110 1.00 18.13 ? 296 ARG A O   1 
ATOM   2398 C  CB  . ARG A 1 296 ? 0.469   20.154  -10.777 1.00 16.62 ? 296 ARG A CB  1 
ATOM   2399 C  CG  . ARG A 1 296 ? 0.933   20.907  -12.011 1.00 20.32 ? 296 ARG A CG  1 
ATOM   2400 C  CD  . ARG A 1 296 ? 0.179   22.225  -12.204 1.00 21.52 ? 296 ARG A CD  1 
ATOM   2401 N  NE  . ARG A 1 296 ? -0.043  22.992  -10.961 1.00 20.54 ? 296 ARG A NE  1 
ATOM   2402 C  CZ  . ARG A 1 296 ? 0.864   23.754  -10.355 1.00 23.92 ? 296 ARG A CZ  1 
ATOM   2403 N  NH1 . ARG A 1 296 ? 2.089   23.864  -10.866 1.00 27.52 ? 296 ARG A NH1 1 
ATOM   2404 N  NH2 . ARG A 1 296 ? 0.551   24.399  -9.228  1.00 22.08 ? 296 ARG A NH2 1 
ATOM   2405 N  N   . VAL A 1 297 ? 3.181   18.623  -9.943  1.00 14.73 ? 297 VAL A N   1 
ATOM   2406 C  CA  . VAL A 1 297 ? 4.655   18.645  -10.121 1.00 14.46 ? 297 VAL A CA  1 
ATOM   2407 C  C   . VAL A 1 297 ? 5.232   17.226  -9.968  1.00 14.48 ? 297 VAL A C   1 
ATOM   2408 O  O   . VAL A 1 297 ? 6.162   16.858  -10.735 1.00 14.81 ? 297 VAL A O   1 
ATOM   2409 C  CB  . VAL A 1 297 ? 5.275   19.626  -9.115  1.00 14.12 ? 297 VAL A CB  1 
ATOM   2410 C  CG1 . VAL A 1 297 ? 6.791   19.437  -9.013  1.00 16.34 ? 297 VAL A CG1 1 
ATOM   2411 C  CG2 . VAL A 1 297 ? 4.887   21.039  -9.527  1.00 16.02 ? 297 VAL A CG2 1 
ATOM   2412 N  N   . LEU A 1 298 ? 4.863   16.504  -8.920  1.00 15.69 ? 298 LEU A N   1 
ATOM   2413 C  CA  . LEU A 1 298 ? 5.536   15.215  -8.621  1.00 15.67 ? 298 LEU A CA  1 
ATOM   2414 C  C   . LEU A 1 298 ? 4.898   14.083  -9.430  1.00 15.64 ? 298 LEU A C   1 
ATOM   2415 O  O   . LEU A 1 298 ? 4.207   13.230  -8.860  1.00 16.10 ? 298 LEU A O   1 
ATOM   2416 C  CB  . LEU A 1 298 ? 5.445   14.969  -7.119  1.00 15.33 ? 298 LEU A CB  1 
ATOM   2417 C  CG  . LEU A 1 298 ? 6.177   15.983  -6.250  1.00 15.37 ? 298 LEU A CG  1 
ATOM   2418 C  CD1 . LEU A 1 298 ? 5.998   15.747  -4.743  1.00 17.20 ? 298 LEU A CD1 1 
ATOM   2419 C  CD2 . LEU A 1 298 ? 7.662   16.040  -6.603  1.00 15.67 ? 298 LEU A CD2 1 
ATOM   2420 N  N   . VAL A 1 299 ? 5.210   14.058  -10.733 1.00 17.81 ? 299 VAL A N   1 
ATOM   2421 C  CA  . VAL A 1 299 ? 4.536   13.154  -11.713 1.00 20.34 ? 299 VAL A CA  1 
ATOM   2422 C  C   . VAL A 1 299 ? 5.195   11.775  -11.784 1.00 20.86 ? 299 VAL A C   1 
ATOM   2423 O  O   . VAL A 1 299 ? 4.607   10.897  -12.490 1.00 23.87 ? 299 VAL A O   1 
ATOM   2424 C  CB  . VAL A 1 299 ? 4.445   13.796  -13.101 1.00 21.61 ? 299 VAL A CB  1 
ATOM   2425 C  CG1 . VAL A 1 299 ? 3.592   15.052  -13.105 1.00 22.75 ? 299 VAL A CG1 1 
ATOM   2426 C  CG2 . VAL A 1 299 ? 5.800   14.072  -13.685 1.00 21.62 ? 299 VAL A CG2 1 
ATOM   2427 N  N   . ASP A 1 300 ? 6.311   11.549  -11.101 1.00 18.19 ? 300 ASP A N   1 
ATOM   2428 C  CA  . ASP A 1 300 ? 7.030   10.265  -11.139 1.00 20.02 ? 300 ASP A CA  1 
ATOM   2429 C  C   . ASP A 1 300 ? 6.914   9.576   -9.794  1.00 20.05 ? 300 ASP A C   1 
ATOM   2430 O  O   . ASP A 1 300 ? 6.663   10.209  -8.771  1.00 18.94 ? 300 ASP A O   1 
ATOM   2431 C  CB  . ASP A 1 300 ? 8.502   10.486  -11.495 1.00 20.71 ? 300 ASP A CB  1 
ATOM   2432 C  CG  . ASP A 1 300 ? 8.696   11.104  -12.862 1.00 23.58 ? 300 ASP A CG  1 
ATOM   2433 O  OD1 . ASP A 1 300 ? 7.972   10.668  -13.809 1.00 27.75 ? 300 ASP A OD1 1 
ATOM   2434 O  OD2 . ASP A 1 300 ? 9.608   11.919  -12.990 1.00 27.02 ? 300 ASP A OD2 1 
ATOM   2435 N  N   . PRO A 1 301 ? 7.175   8.257   -9.742  1.00 21.71 ? 301 PRO A N   1 
ATOM   2436 C  CA  . PRO A 1 301 ? 7.127   7.521   -8.482  1.00 21.39 ? 301 PRO A CA  1 
ATOM   2437 C  C   . PRO A 1 301 ? 8.090   8.006   -7.389  1.00 20.85 ? 301 PRO A C   1 
ATOM   2438 O  O   . PRO A 1 301 ? 7.744   8.026   -6.229  1.00 25.95 ? 301 PRO A O   1 
ATOM   2439 C  CB  . PRO A 1 301 ? 7.451   6.086   -8.876  1.00 25.55 ? 301 PRO A CB  1 
ATOM   2440 C  CG  . PRO A 1 301 ? 7.281   6.009   -10.403 1.00 25.81 ? 301 PRO A CG  1 
ATOM   2441 C  CD  . PRO A 1 301 ? 7.425   7.411   -10.929 1.00 25.63 ? 301 PRO A CD  1 
ATOM   2442 N  N   . VAL A 1 302 ? 9.264   8.426   -7.808  1.00 20.47 ? 302 VAL A N   1 
ATOM   2443 C  CA  . VAL A 1 302 ? 10.393  8.965   -7.012  1.00 26.03 ? 302 VAL A CA  1 
ATOM   2444 C  C   . VAL A 1 302 ? 10.516  10.434  -7.428  1.00 22.31 ? 302 VAL A C   1 
ATOM   2445 O  O   . VAL A 1 302 ? 10.730  10.669  -8.611  1.00 26.57 ? 302 VAL A O   1 
ATOM   2446 C  CB  . VAL A 1 302 ? 11.663  8.158   -7.368  1.00 29.69 ? 302 VAL A CB  1 
ATOM   2447 C  CG1 . VAL A 1 302 ? 12.870  8.575   -6.555  1.00 32.86 ? 302 VAL A CG1 1 
ATOM   2448 C  CG2 . VAL A 1 302 ? 11.451  6.646   -7.245  1.00 29.86 ? 302 VAL A CG2 1 
ATOM   2449 N  N   . PRO A 1 303 ? 10.448  11.447  -6.540  1.00 18.39 ? 303 PRO A N   1 
ATOM   2450 C  CA  . PRO A 1 303 ? 10.737  12.824  -6.944  1.00 17.49 ? 303 PRO A CA  1 
ATOM   2451 C  C   . PRO A 1 303 ? 12.194  12.984  -7.410  1.00 16.03 ? 303 PRO A C   1 
ATOM   2452 O  O   . PRO A 1 303 ? 13.115  12.446  -6.764  1.00 16.74 ? 303 PRO A O   1 
ATOM   2453 C  CB  . PRO A 1 303 ? 10.455  13.647  -5.680  1.00 19.97 ? 303 PRO A CB  1 
ATOM   2454 C  CG  . PRO A 1 303 ? 9.489   12.786  -4.923  1.00 22.37 ? 303 PRO A CG  1 
ATOM   2455 C  CD  . PRO A 1 303 ? 9.979   11.382  -5.142  1.00 21.20 ? 303 PRO A CD  1 
ATOM   2456 N  N   . SER A 1 304 ? 12.399  13.791  -8.418  1.00 14.50 ? 304 SER A N   1 
ATOM   2457 C  CA  . SER A 1 304 ? 13.744  14.228  -8.862  1.00 15.59 ? 304 SER A CA  1 
ATOM   2458 C  C   . SER A 1 304 ? 14.150  15.511  -8.153  1.00 13.84 ? 304 SER A C   1 
ATOM   2459 O  O   . SER A 1 304 ? 13.272  16.224  -7.659  1.00 13.27 ? 304 SER A O   1 
ATOM   2460 C  CB  . SER A 1 304 ? 13.800  14.445  -10.327 1.00 16.14 ? 304 SER A CB  1 
ATOM   2461 O  OG  . SER A 1 304 ? 13.026  15.575  -10.696 1.00 17.23 ? 304 SER A OG  1 
ATOM   2462 N  N   . TYR A 1 305 ? 15.436  15.852  -8.200  1.00 13.69 ? 305 TYR A N   1 
ATOM   2463 C  CA  . TYR A 1 305 ? 15.957  17.124  -7.681  1.00 14.86 ? 305 TYR A CA  1 
ATOM   2464 C  C   . TYR A 1 305 ? 15.212  18.271  -8.380  1.00 14.84 ? 305 TYR A C   1 
ATOM   2465 O  O   . TYR A 1 305 ? 14.733  19.212  -7.706  1.00 15.11 ? 305 TYR A O   1 
ATOM   2466 C  CB  . TYR A 1 305 ? 17.468  17.191  -7.907  1.00 15.05 ? 305 TYR A CB  1 
ATOM   2467 C  CG  . TYR A 1 305 ? 17.998  18.559  -7.624  1.00 16.13 ? 305 TYR A CG  1 
ATOM   2468 C  CD1 . TYR A 1 305 ? 18.406  18.927  -6.346  1.00 15.55 ? 305 TYR A CD1 1 
ATOM   2469 C  CD2 . TYR A 1 305 ? 18.107  19.490  -8.651  1.00 16.86 ? 305 TYR A CD2 1 
ATOM   2470 C  CE1 . TYR A 1 305 ? 18.892  20.195  -6.088  1.00 17.62 ? 305 TYR A CE1 1 
ATOM   2471 C  CE2 . TYR A 1 305 ? 18.549  20.770  -8.391  1.00 17.98 ? 305 TYR A CE2 1 
ATOM   2472 C  CZ  . TYR A 1 305 ? 18.954  21.118  -7.115  1.00 18.44 ? 305 TYR A CZ  1 
ATOM   2473 O  OH  . TYR A 1 305 ? 19.413  22.409  -6.978  1.00 19.91 ? 305 TYR A OH  1 
ATOM   2474 N  N   . LYS A 1 306 ? 15.106  18.238  -9.704  1.00 15.27 ? 306 LYS A N   1 
ATOM   2475 C  CA  . LYS A 1 306 ? 14.476  19.317  -10.479 1.00 15.16 ? 306 LYS A CA  1 
ATOM   2476 C  C   . LYS A 1 306 ? 13.015  19.472  -10.051 1.00 13.66 ? 306 LYS A C   1 
ATOM   2477 O  O   . LYS A 1 306 ? 12.536  20.628  -9.954  1.00 16.61 ? 306 LYS A O   1 
ATOM   2478 C  CB  . LYS A 1 306 ? 14.572  19.031  -11.985 1.00 18.80 ? 306 LYS A CB  1 
ATOM   2479 C  CG  . LYS A 1 306 ? 15.898  19.429  -12.592 1.00 24.74 ? 306 LYS A CG  1 
ATOM   2480 C  CD  . LYS A 1 306 ? 15.924  19.183  -14.130 1.00 31.98 ? 306 LYS A CD  1 
ATOM   2481 C  CE  . LYS A 1 306 ? 17.315  19.290  -14.718 1.00 36.32 ? 306 LYS A CE  1 
ATOM   2482 N  NZ  . LYS A 1 306 ? 17.329  19.030  -16.178 1.00 41.28 ? 306 LYS A NZ  1 
ATOM   2483 N  N   . GLN A 1 307 ? 12.313  18.378  -9.808  1.00 14.02 ? 307 GLN A N   1 
ATOM   2484 C  CA  . GLN A 1 307 ? 10.883  18.451  -9.371  1.00 13.40 ? 307 GLN A CA  1 
ATOM   2485 C  C   . GLN A 1 307 ? 10.799  19.126  -8.000  1.00 16.23 ? 307 GLN A C   1 
ATOM   2486 O  O   . GLN A 1 307 ? 9.884   19.970  -7.784  1.00 15.81 ? 307 GLN A O   1 
ATOM   2487 C  CB  . GLN A 1 307 ? 10.250  17.080  -9.338  1.00 14.77 ? 307 GLN A CB  1 
ATOM   2488 C  CG  . GLN A 1 307 ? 9.971   16.598  -10.757 1.00 15.16 ? 307 GLN A CG  1 
ATOM   2489 C  CD  . GLN A 1 307 ? 9.738   15.106  -10.838 1.00 17.46 ? 307 GLN A CD  1 
ATOM   2490 O  OE1 . GLN A 1 307 ? 9.947   14.355  -9.902  1.00 17.18 ? 307 GLN A OE1 1 
ATOM   2491 N  NE2 . GLN A 1 307 ? 9.185   14.622  -11.938 1.00 19.88 ? 307 GLN A NE2 1 
ATOM   2492 N  N   . VAL A 1 308 ? 11.723  18.823  -7.070  1.00 13.98 ? 308 VAL A N   1 
ATOM   2493 C  CA  . VAL A 1 308 ? 11.650  19.482  -5.751  1.00 14.73 ? 308 VAL A CA  1 
ATOM   2494 C  C   . VAL A 1 308 ? 11.809  20.993  -5.945  1.00 15.50 ? 308 VAL A C   1 
ATOM   2495 O  O   . VAL A 1 308 ? 11.105  21.776  -5.327  1.00 14.29 ? 308 VAL A O   1 
ATOM   2496 C  CB  . VAL A 1 308 ? 12.695  18.881  -4.793  1.00 14.85 ? 308 VAL A CB  1 
ATOM   2497 C  CG1 . VAL A 1 308 ? 12.780  19.683  -3.512  1.00 15.77 ? 308 VAL A CG1 1 
ATOM   2498 C  CG2 . VAL A 1 308 ? 12.385  17.446  -4.519  1.00 16.66 ? 308 VAL A CG2 1 
ATOM   2499 N  N   . LYS A 1 309 ? 12.717  21.422  -6.814  1.00 15.30 ? 309 LYS A N   1 
ATOM   2500 C  CA  . LYS A 1 309 ? 12.955  22.857  -7.039  1.00 16.67 ? 309 LYS A CA  1 
ATOM   2501 C  C   . LYS A 1 309 ? 11.708  23.522  -7.611  1.00 16.54 ? 309 LYS A C   1 
ATOM   2502 O  O   . LYS A 1 309 ? 11.552  24.750  -7.411  1.00 17.90 ? 309 LYS A O   1 
ATOM   2503 C  CB  . LYS A 1 309 ? 14.135  23.080  -7.989  1.00 19.13 ? 309 LYS A CB  1 
ATOM   2504 C  CG  . LYS A 1 309 ? 15.464  22.587  -7.463  1.00 21.71 ? 309 LYS A CG  1 
ATOM   2505 C  CD  . LYS A 1 309 ? 15.853  23.203  -6.139  1.00 26.77 ? 309 LYS A CD  1 
ATOM   2506 C  CE  . LYS A 1 309 ? 15.897  22.168  -5.027  1.00 28.65 ? 309 LYS A CE  1 
ATOM   2507 N  NZ  . LYS A 1 309 ? 16.254  22.751  -3.680  1.00 28.09 ? 309 LYS A NZ  1 
ATOM   2508 N  N   . GLN A 1 310 ? 10.845  22.764  -8.255  1.00 14.84 ? 310 GLN A N   1 
ATOM   2509 C  CA  . GLN A 1 310 ? 9.622   23.271  -8.903  1.00 16.65 ? 310 GLN A CA  1 
ATOM   2510 C  C   . GLN A 1 310 ? 8.481   23.477  -7.904  1.00 14.65 ? 310 GLN A C   1 
ATOM   2511 O  O   . GLN A 1 310 ? 7.464   24.107  -8.269  1.00 15.09 ? 310 GLN A O   1 
ATOM   2512 C  CB  . GLN A 1 310 ? 9.344   22.301  -10.034 1.00 17.50 ? 310 GLN A CB  1 
ATOM   2513 C  CG  . GLN A 1 310 ? 8.134   22.604  -10.881 1.00 18.05 ? 310 GLN A CG  1 
ATOM   2514 C  CD  . GLN A 1 310 ? 7.955   21.582  -11.976 1.00 18.08 ? 310 GLN A CD  1 
ATOM   2515 O  OE1 . GLN A 1 310 ? 8.593   20.493  -11.997 1.00 17.22 ? 310 GLN A OE1 1 
ATOM   2516 N  NE2 . GLN A 1 310 ? 7.044   21.876  -12.876 1.00 17.84 ? 310 GLN A NE2 1 
ATOM   2517 N  N   . LEU A 1 311 ? 8.613   22.993  -6.651  1.00 13.62 ? 311 LEU A N   1 
ATOM   2518 C  CA  . LEU A 1 311 ? 7.541   23.125  -5.612  1.00 13.79 ? 311 LEU A CA  1 
ATOM   2519 C  C   . LEU A 1 311 ? 7.570   24.504  -4.947  1.00 14.21 ? 311 LEU A C   1 
ATOM   2520 O  O   . LEU A 1 311 ? 7.866   24.594  -3.751  1.00 13.93 ? 311 LEU A O   1 
ATOM   2521 C  CB  . LEU A 1 311 ? 7.733   22.002  -4.582  1.00 12.12 ? 311 LEU A CB  1 
ATOM   2522 C  CG  . LEU A 1 311 ? 7.508   20.584  -5.117  1.00 14.25 ? 311 LEU A CG  1 
ATOM   2523 C  CD1 . LEU A 1 311 ? 7.899   19.555  -4.104  1.00 14.09 ? 311 LEU A CD1 1 
ATOM   2524 C  CD2 . LEU A 1 311 ? 6.058   20.376  -5.563  1.00 15.20 ? 311 LEU A CD2 1 
ATOM   2525 N  N   . LYS A 1 312 ? 7.269   25.559  -5.702  1.00 14.42 ? 312 LYS A N   1 
ATOM   2526 C  CA  . LYS A 1 312 ? 7.300   26.935  -5.188  1.00 15.07 ? 312 LYS A CA  1 
ATOM   2527 C  C   . LYS A 1 312 ? 6.313   27.086  -4.037  1.00 13.87 ? 312 LYS A C   1 
ATOM   2528 O  O   . LYS A 1 312 ? 6.692   27.726  -3.015  1.00 13.71 ? 312 LYS A O   1 
ATOM   2529 C  CB  . LYS A 1 312 ? 7.018   27.895  -6.341  1.00 17.13 ? 312 LYS A CB  1 
ATOM   2530 C  CG  . LYS A 1 312 ? 6.963   29.372  -5.977  1.00 22.13 ? 312 LYS A CG  1 
ATOM   2531 C  CD  . LYS A 1 312 ? 6.325   30.193  -7.091  1.00 29.00 ? 312 LYS A CD  1 
ATOM   2532 C  CE  . LYS A 1 312 ? 5.989   31.593  -6.654  1.00 33.47 ? 312 LYS A CE  1 
ATOM   2533 N  NZ  . LYS A 1 312 ? 7.204   32.175  -6.078  1.00 34.12 ? 312 LYS A NZ  1 
ATOM   2534 N  N   . TYR A 1 313 ? 5.091   26.638  -4.156  1.00 13.66 ? 313 TYR A N   1 
ATOM   2535 C  CA  . TYR A 1 313 ? 4.078   26.923  -3.114  1.00 12.32 ? 313 TYR A CA  1 
ATOM   2536 C  C   . TYR A 1 313 ? 4.431   26.152  -1.843  1.00 12.24 ? 313 TYR A C   1 
ATOM   2537 O  O   . TYR A 1 313 ? 4.297   26.715  -0.757  1.00 11.95 ? 313 TYR A O   1 
ATOM   2538 C  CB  . TYR A 1 313 ? 2.661   26.585  -3.576  1.00 13.10 ? 313 TYR A CB  1 
ATOM   2539 C  CG  . TYR A 1 313 ? 1.597   27.147  -2.691  1.00 13.33 ? 313 TYR A CG  1 
ATOM   2540 C  CD1 . TYR A 1 313 ? 1.219   28.471  -2.796  1.00 15.20 ? 313 TYR A CD1 1 
ATOM   2541 C  CD2 . TYR A 1 313 ? 1.084   26.426  -1.625  1.00 13.14 ? 313 TYR A CD2 1 
ATOM   2542 C  CE1 . TYR A 1 313 ? 0.321   29.058  -1.919  1.00 14.39 ? 313 TYR A CE1 1 
ATOM   2543 C  CE2 . TYR A 1 313 ? 0.147   26.978  -0.776  1.00 13.75 ? 313 TYR A CE2 1 
ATOM   2544 C  CZ  . TYR A 1 313 ? -0.235  28.297  -0.910  1.00 15.22 ? 313 TYR A CZ  1 
ATOM   2545 O  OH  . TYR A 1 313 ? -1.104  28.832  0.019   1.00 15.77 ? 313 TYR A OH  1 
ATOM   2546 N  N   . VAL A 1 314 ? 4.874   24.914  -1.977  1.00 11.70 ? 314 VAL A N   1 
ATOM   2547 C  CA  . VAL A 1 314 ? 5.373   24.168  -0.778  1.00 12.41 ? 314 VAL A CA  1 
ATOM   2548 C  C   . VAL A 1 314 ? 6.486   24.992  -0.130  1.00 12.70 ? 314 VAL A C   1 
ATOM   2549 O  O   . VAL A 1 314 ? 6.507   25.125  1.123   1.00 12.02 ? 314 VAL A O   1 
ATOM   2550 C  CB  . VAL A 1 314 ? 5.860   22.780  -1.177  1.00 12.87 ? 314 VAL A CB  1 
ATOM   2551 C  CG1 . VAL A 1 314 ? 6.488   22.055  0.019   1.00 14.65 ? 314 VAL A CG1 1 
ATOM   2552 C  CG2 . VAL A 1 314 ? 4.716   21.948  -1.747  1.00 14.76 ? 314 VAL A CG2 1 
ATOM   2553 N  N   . GLY A 1 315 ? 7.404   25.586  -0.888  1.00 12.69 ? 315 GLY A N   1 
ATOM   2554 C  CA  . GLY A 1 315 ? 8.456   26.440  -0.279  1.00 13.00 ? 315 GLY A CA  1 
ATOM   2555 C  C   . GLY A 1 315 ? 7.871   27.643  0.443   1.00 12.28 ? 315 GLY A C   1 
ATOM   2556 O  O   . GLY A 1 315 ? 8.411   28.061  1.502   1.00 14.00 ? 315 GLY A O   1 
ATOM   2557 N  N   . MET A 1 316 ? 6.811   28.232  -0.076  1.00 12.34 ? 316 MET A N   1 
ATOM   2558 C  CA  . MET A 1 316 ? 6.140   29.392  0.550   1.00 13.09 ? 316 MET A CA  1 
ATOM   2559 C  C   . MET A 1 316 ? 5.483   28.947  1.869   1.00 11.62 ? 316 MET A C   1 
ATOM   2560 O  O   . MET A 1 316 ? 5.571   29.688  2.850   1.00 12.18 ? 316 MET A O   1 
ATOM   2561 C  CB  . MET A 1 316 ? 5.090   29.931  -0.407  1.00 15.74 ? 316 MET A CB  1 
ATOM   2562 C  CG  . MET A 1 316 ? 5.709   30.624  -1.597  1.00 15.03 ? 316 MET A CG  1 
ATOM   2563 S  SD  . MET A 1 316 ? 4.562   30.868  -2.976  1.00 18.46 ? 316 MET A SD  1 
ATOM   2564 C  CE  . MET A 1 316 ? 3.232   31.729  -2.183  1.00 18.54 ? 316 MET A CE  1 
ATOM   2565 N  N   . VAL A 1 317 ? 4.878   27.759  1.895   1.00 11.98 ? 317 VAL A N   1 
ATOM   2566 C  CA  . VAL A 1 317 ? 4.316   27.179  3.137   1.00 11.99 ? 317 VAL A CA  1 
ATOM   2567 C  C   . VAL A 1 317 ? 5.437   27.054  4.167   1.00 11.26 ? 317 VAL A C   1 
ATOM   2568 O  O   . VAL A 1 317 ? 5.202   27.410  5.358   1.00 11.43 ? 317 VAL A O   1 
ATOM   2569 C  CB  . VAL A 1 317 ? 3.634   25.827  2.850   1.00 11.41 ? 317 VAL A CB  1 
ATOM   2570 C  CG1 . VAL A 1 317 ? 3.317   25.071  4.125   1.00 12.29 ? 317 VAL A CG1 1 
ATOM   2571 C  CG2 . VAL A 1 317 ? 2.386   25.975  2.015   1.00 12.57 ? 317 VAL A CG2 1 
ATOM   2572 N  N   . LEU A 1 318 ? 6.594   26.497  3.781   1.00 11.23 ? 318 LEU A N   1 
ATOM   2573 C  CA  . LEU A 1 318 ? 7.700   26.300  4.756   1.00 11.12 ? 318 LEU A CA  1 
ATOM   2574 C  C   . LEU A 1 318 ? 8.143   27.662  5.272   1.00 11.82 ? 318 LEU A C   1 
ATOM   2575 O  O   . LEU A 1 318 ? 8.383   27.818  6.494   1.00 12.16 ? 318 LEU A O   1 
ATOM   2576 C  CB  . LEU A 1 318 ? 8.816   25.493  4.078   1.00 11.38 ? 318 LEU A CB  1 
ATOM   2577 C  CG  . LEU A 1 318 ? 8.413   24.052  3.791   1.00 11.79 ? 318 LEU A CG  1 
ATOM   2578 C  CD1 . LEU A 1 318 ? 9.406   23.378  2.894   1.00 13.70 ? 318 LEU A CD1 1 
ATOM   2579 C  CD2 . LEU A 1 318 ? 8.276   23.246  5.084   1.00 12.83 ? 318 LEU A CD2 1 
ATOM   2580 N  N   . ASN A 1 319 ? 8.295   28.669  4.396   1.00 11.58 ? 319 ASN A N   1 
ATOM   2581 C  CA  . ASN A 1 319 ? 8.736   29.988  4.858   1.00 12.80 ? 319 ASN A CA  1 
ATOM   2582 C  C   . ASN A 1 319 ? 7.707   30.626  5.771   1.00 11.37 ? 319 ASN A C   1 
ATOM   2583 O  O   . ASN A 1 319 ? 8.120   31.262  6.762   1.00 12.04 ? 319 ASN A O   1 
ATOM   2584 C  CB  . ASN A 1 319 ? 9.091   30.936  3.732   1.00 13.40 ? 319 ASN A CB  1 
ATOM   2585 C  CG  . ASN A 1 319 ? 10.462  30.660  3.183   1.00 17.22 ? 319 ASN A CG  1 
ATOM   2586 O  OD1 . ASN A 1 319 ? 11.383  30.309  3.921   1.00 17.43 ? 319 ASN A OD1 1 
ATOM   2587 N  ND2 . ASN A 1 319 ? 10.615  30.888  1.890   1.00 22.57 ? 319 ASN A ND2 1 
ATOM   2588 N  N   . GLU A 1 320 ? 6.422   30.434  5.538   1.00 12.28 ? 320 GLU A N   1 
ATOM   2589 C  CA  . GLU A 1 320 ? 5.407   31.032  6.432   1.00 13.48 ? 320 GLU A CA  1 
ATOM   2590 C  C   . GLU A 1 320 ? 5.336   30.294  7.757   1.00 13.61 ? 320 GLU A C   1 
ATOM   2591 O  O   . GLU A 1 320 ? 5.139   30.986  8.769   1.00 13.85 ? 320 GLU A O   1 
ATOM   2592 C  CB  . GLU A 1 320 ? 4.104   31.150  5.651   1.00 14.53 ? 320 GLU A CB  1 
ATOM   2593 C  CG  . GLU A 1 320 ? 2.982   31.768  6.476   1.00 14.03 ? 320 GLU A CG  1 
ATOM   2594 C  CD  . GLU A 1 320 ? 3.084   33.243  6.830   1.00 16.21 ? 320 GLU A CD  1 
ATOM   2595 O  OE1 . GLU A 1 320 ? 4.191   33.860  6.657   1.00 17.63 ? 320 GLU A OE1 1 
ATOM   2596 O  OE2 . GLU A 1 320 ? 2.016   33.811  7.236   1.00 14.65 ? 320 GLU A OE2 1 
ATOM   2597 N  N   . ALA A 1 321 ? 5.648   28.998  7.832   1.00 12.21 ? 321 ALA A N   1 
ATOM   2598 C  CA  . ALA A 1 321 ? 5.820   28.277  9.113   1.00 12.99 ? 321 ALA A CA  1 
ATOM   2599 C  C   . ALA A 1 321 ? 7.034   28.825  9.842   1.00 12.58 ? 321 ALA A C   1 
ATOM   2600 O  O   . ALA A 1 321 ? 6.952   28.983  11.094  1.00 11.98 ? 321 ALA A O   1 
ATOM   2601 C  CB  . ALA A 1 321 ? 5.903   26.803  8.846   1.00 12.75 ? 321 ALA A CB  1 
ATOM   2602 N  N   . LEU A 1 322 ? 8.167   29.062  9.173   1.00 12.39 ? 322 LEU A N   1 
ATOM   2603 C  CA  . LEU A 1 322 ? 9.358   29.666  9.814   1.00 12.93 ? 322 LEU A CA  1 
ATOM   2604 C  C   . LEU A 1 322 ? 9.035   31.078  10.296  1.00 12.26 ? 322 LEU A C   1 
ATOM   2605 O  O   . LEU A 1 322 ? 9.746   31.569  11.206  1.00 12.81 ? 322 LEU A O   1 
ATOM   2606 C  CB  . LEU A 1 322 ? 10.501  29.682  8.798   1.00 12.65 ? 322 LEU A CB  1 
ATOM   2607 C  CG  . LEU A 1 322 ? 11.109  28.327  8.480   1.00 14.69 ? 322 LEU A CG  1 
ATOM   2608 C  CD1 . LEU A 1 322 ? 12.115  28.458  7.379   1.00 15.00 ? 322 LEU A CD1 1 
ATOM   2609 C  CD2 . LEU A 1 322 ? 11.725  27.681  9.728   1.00 14.15 ? 322 LEU A CD2 1 
ATOM   2610 N  N   . ARG A 1 323 ? 8.158   31.807  9.629   1.00 12.29 ? 323 ARG A N   1 
ATOM   2611 C  CA  . ARG A 1 323 ? 7.836   33.180  10.070  1.00 12.14 ? 323 ARG A CA  1 
ATOM   2612 C  C   . ARG A 1 323 ? 7.170   33.072  11.430  1.00 12.35 ? 323 ARG A C   1 
ATOM   2613 O  O   . ARG A 1 323 ? 7.668   33.677  12.408  1.00 12.31 ? 323 ARG A O   1 
ATOM   2614 C  CB  . ARG A 1 323 ? 6.985   33.955  9.089   1.00 12.96 ? 323 ARG A CB  1 
ATOM   2615 C  CG  . ARG A 1 323 ? 6.826   35.392  9.552   1.00 12.51 ? 323 ARG A CG  1 
ATOM   2616 C  CD  . ARG A 1 323 ? 5.888   36.183  8.651   1.00 13.21 ? 323 ARG A CD  1 
ATOM   2617 N  NE  . ARG A 1 323 ? 4.535   35.685  8.733   1.00 13.20 ? 323 ARG A NE  1 
ATOM   2618 C  CZ  . ARG A 1 323 ? 3.639   35.963  9.681   1.00 13.71 ? 323 ARG A CZ  1 
ATOM   2619 N  NH1 . ARG A 1 323 ? 3.947   36.755  10.687  1.00 14.05 ? 323 ARG A NH1 1 
ATOM   2620 N  NH2 . ARG A 1 323 ? 2.463   35.364  9.641   1.00 13.55 ? 323 ARG A NH2 1 
ATOM   2621 N  N   . LEU A 1 324 ? 6.085   32.294  11.527  1.00 13.01 ? 324 LEU A N   1 
ATOM   2622 C  CA  . LEU A 1 324 ? 5.323   32.231  12.808  1.00 14.02 ? 324 LEU A CA  1 
ATOM   2623 C  C   . LEU A 1 324 ? 6.070   31.497  13.906  1.00 14.52 ? 324 LEU A C   1 
ATOM   2624 O  O   . LEU A 1 324 ? 6.085   31.983  15.042  1.00 14.35 ? 324 LEU A O   1 
ATOM   2625 C  CB  . LEU A 1 324 ? 3.946   31.647  12.580  1.00 14.01 ? 324 LEU A CB  1 
ATOM   2626 C  CG  . LEU A 1 324 ? 2.973   32.660  11.980  1.00 16.72 ? 324 LEU A CG  1 
ATOM   2627 C  CD1 . LEU A 1 324 ? 1.784   31.925  11.396  1.00 17.42 ? 324 LEU A CD1 1 
ATOM   2628 C  CD2 . LEU A 1 324 ? 2.582   33.769  12.969  1.00 18.55 ? 324 LEU A CD2 1 
ATOM   2629 N  N   . TRP A 1 325 ? 6.715   30.375  13.609  1.00 13.96 ? 325 TRP A N   1 
ATOM   2630 C  CA  . TRP A 1 325 ? 7.394   29.581  14.646  1.00 13.51 ? 325 TRP A CA  1 
ATOM   2631 C  C   . TRP A 1 325 ? 8.779   29.204  14.165  1.00 12.83 ? 325 TRP A C   1 
ATOM   2632 O  O   . TRP A 1 325 ? 9.029   28.018  13.823  1.00 15.26 ? 325 TRP A O   1 
ATOM   2633 C  CB  . TRP A 1 325 ? 6.505   28.414  15.059  1.00 14.09 ? 325 TRP A CB  1 
ATOM   2634 C  CG  . TRP A 1 325 ? 5.330   28.877  15.866  1.00 13.92 ? 325 TRP A CG  1 
ATOM   2635 C  CD1 . TRP A 1 325 ? 4.029   28.833  15.496  1.00 16.92 ? 325 TRP A CD1 1 
ATOM   2636 C  CD2 . TRP A 1 325 ? 5.376   29.566  17.124  1.00 14.64 ? 325 TRP A CD2 1 
ATOM   2637 N  NE1 . TRP A 1 325 ? 3.241   29.392  16.467  1.00 16.85 ? 325 TRP A NE1 1 
ATOM   2638 C  CE2 . TRP A 1 325 ? 4.047   29.851  17.477  1.00 15.65 ? 325 TRP A CE2 1 
ATOM   2639 C  CE3 . TRP A 1 325 ? 6.424   29.892  17.976  1.00 17.25 ? 325 TRP A CE3 1 
ATOM   2640 C  CZ2 . TRP A 1 325 ? 3.741   30.511  18.671  1.00 16.45 ? 325 TRP A CZ2 1 
ATOM   2641 C  CZ3 . TRP A 1 325 ? 6.121   30.557  19.141  1.00 17.34 ? 325 TRP A CZ3 1 
ATOM   2642 C  CH2 . TRP A 1 325 ? 4.802   30.826  19.475  1.00 16.66 ? 325 TRP A CH2 1 
ATOM   2643 N  N   . PRO A 1 326 ? 9.732   30.141  14.083  1.00 12.51 ? 326 PRO A N   1 
ATOM   2644 C  CA  . PRO A 1 326 ? 11.088  29.814  13.617  1.00 13.26 ? 326 PRO A CA  1 
ATOM   2645 C  C   . PRO A 1 326 ? 11.638  28.800  14.613  1.00 14.91 ? 326 PRO A C   1 
ATOM   2646 O  O   . PRO A 1 326 ? 11.771  29.098  15.823  1.00 14.22 ? 326 PRO A O   1 
ATOM   2647 C  CB  . PRO A 1 326 ? 11.796  31.172  13.641  1.00 14.17 ? 326 PRO A CB  1 
ATOM   2648 C  CG  . PRO A 1 326 ? 10.982  31.995  14.641  1.00 13.38 ? 326 PRO A CG  1 
ATOM   2649 C  CD  . PRO A 1 326 ? 9.559   31.565  14.504  1.00 12.30 ? 326 PRO A CD  1 
ATOM   2650 N  N   . THR A 1 327 ? 11.931  27.583  14.163  1.00 14.07 ? 327 THR A N   1 
ATOM   2651 C  CA  . THR A 1 327 ? 12.145  26.477  15.107  1.00 13.72 ? 327 THR A CA  1 
ATOM   2652 C  C   . THR A 1 327 ? 13.428  26.685  15.881  1.00 13.99 ? 327 THR A C   1 
ATOM   2653 O  O   . THR A 1 327 ? 13.476  26.183  16.979  1.00 13.99 ? 327 THR A O   1 
ATOM   2654 C  CB  . THR A 1 327 ? 12.079  25.148  14.358  1.00 16.76 ? 327 THR A CB  1 
ATOM   2655 O  OG1 . THR A 1 327 ? 12.236  24.048  15.245  1.00 22.51 ? 327 THR A OG1 1 
ATOM   2656 C  CG2 . THR A 1 327 ? 13.156  25.096  13.335  1.00 16.01 ? 327 THR A CG2 1 
ATOM   2657 N  N   . ALA A 1 328 ? 14.437  27.390  15.356  1.00 14.30 ? 328 ALA A N   1 
ATOM   2658 C  CA  . ALA A 1 328 ? 15.582  27.860  16.138  1.00 15.03 ? 328 ALA A CA  1 
ATOM   2659 C  C   . ALA A 1 328 ? 15.272  29.308  16.443  1.00 18.75 ? 328 ALA A C   1 
ATOM   2660 O  O   . ALA A 1 328 ? 15.384  30.151  15.559  1.00 22.75 ? 328 ALA A O   1 
ATOM   2661 C  CB  . ALA A 1 328 ? 16.852  27.716  15.346  1.00 16.93 ? 328 ALA A CB  1 
ATOM   2662 N  N   . PRO A 1 329 ? 14.764  29.633  17.635  1.00 12.83 ? 329 PRO A N   1 
ATOM   2663 C  CA  . PRO A 1 329 ? 14.079  30.919  17.819  1.00 13.58 ? 329 PRO A CA  1 
ATOM   2664 C  C   . PRO A 1 329 ? 14.915  32.110  18.255  1.00 13.34 ? 329 PRO A C   1 
ATOM   2665 O  O   . PRO A 1 329 ? 14.360  33.195  18.353  1.00 14.14 ? 329 PRO A O   1 
ATOM   2666 C  CB  . PRO A 1 329 ? 13.051  30.519  18.907  1.00 14.80 ? 329 PRO A CB  1 
ATOM   2667 C  CG  . PRO A 1 329 ? 13.750  29.534  19.738  1.00 14.81 ? 329 PRO A CG  1 
ATOM   2668 C  CD  . PRO A 1 329 ? 14.605  28.712  18.770  1.00 15.76 ? 329 PRO A CD  1 
ATOM   2669 N  N   . ALA A 1 330 ? 16.204  31.931  18.477  1.00 13.68 ? 330 ALA A N   1 
ATOM   2670 C  CA  . ALA A 1 330 ? 16.997  33.055  18.988  1.00 14.13 ? 330 ALA A CA  1 
ATOM   2671 C  C   . ALA A 1 330 ? 18.435  32.905  18.546  1.00 15.62 ? 330 ALA A C   1 
ATOM   2672 O  O   . ALA A 1 330 ? 18.906  31.760  18.323  1.00 17.77 ? 330 ALA A O   1 
ATOM   2673 C  CB  . ALA A 1 330 ? 16.883  33.057  20.478  1.00 15.41 ? 330 ALA A CB  1 
ATOM   2674 N  N   . PHE A 1 331 ? 19.132  34.007  18.453  1.00 12.83 ? 331 PHE A N   1 
ATOM   2675 C  CA  . PHE A 1 331 ? 20.591  34.009  18.316  1.00 12.73 ? 331 PHE A CA  1 
ATOM   2676 C  C   . PHE A 1 331 ? 21.133  35.241  19.028  1.00 11.86 ? 331 PHE A C   1 
ATOM   2677 O  O   . PHE A 1 331 ? 20.393  36.262  19.160  1.00 12.67 ? 331 PHE A O   1 
ATOM   2678 C  CB  . PHE A 1 331 ? 20.997  33.922  16.845  1.00 12.27 ? 331 PHE A CB  1 
ATOM   2679 C  CG  . PHE A 1 331 ? 20.586  35.017  15.906  1.00 13.24 ? 331 PHE A CG  1 
ATOM   2680 C  CD1 . PHE A 1 331 ? 19.356  34.985  15.308  1.00 12.48 ? 331 PHE A CD1 1 
ATOM   2681 C  CD2 . PHE A 1 331 ? 21.427  36.086  15.596  1.00 14.64 ? 331 PHE A CD2 1 
ATOM   2682 C  CE1 . PHE A 1 331 ? 18.967  35.921  14.389  1.00 15.07 ? 331 PHE A CE1 1 
ATOM   2683 C  CE2 . PHE A 1 331 ? 21.006  37.067  14.735  1.00 13.79 ? 331 PHE A CE2 1 
ATOM   2684 C  CZ  . PHE A 1 331 ? 19.784  36.989  14.134  1.00 12.81 ? 331 PHE A CZ  1 
ATOM   2685 N  N   . SER A 1 332 ? 22.364  35.149  19.486  1.00 12.05 ? 332 SER A N   1 
ATOM   2686 C  CA  . SER A 1 332 ? 22.990  36.146  20.374  1.00 12.98 ? 332 SER A CA  1 
ATOM   2687 C  C   . SER A 1 332 ? 24.088  36.849  19.598  1.00 13.24 ? 332 SER A C   1 
ATOM   2688 O  O   . SER A 1 332 ? 24.823  36.206  18.831  1.00 12.39 ? 332 SER A O   1 
ATOM   2689 C  CB  . SER A 1 332 ? 23.436  35.477  21.629  1.00 14.21 ? 332 SER A CB  1 
ATOM   2690 O  OG  . SER A 1 332 ? 23.822  36.426  22.608  1.00 14.56 ? 332 SER A OG  1 
ATOM   2691 N  N   . LEU A 1 333 ? 24.294  38.121  19.951  1.00 13.59 ? 333 LEU A N   1 
ATOM   2692 C  CA  . LEU A 1 333 ? 25.362  38.958  19.388  1.00 12.58 ? 333 LEU A CA  1 
ATOM   2693 C  C   . LEU A 1 333 ? 26.063  39.696  20.495  1.00 13.19 ? 333 LEU A C   1 
ATOM   2694 O  O   . LEU A 1 333 ? 25.488  39.856  21.559  1.00 13.38 ? 333 LEU A O   1 
ATOM   2695 C  CB  . LEU A 1 333 ? 24.756  39.947  18.396  1.00 14.58 ? 333 LEU A CB  1 
ATOM   2696 C  CG  . LEU A 1 333 ? 23.905  39.298  17.311  1.00 17.07 ? 333 LEU A CG  1 
ATOM   2697 C  CD1 . LEU A 1 333 ? 22.842  40.214  16.818  1.00 21.08 ? 333 LEU A CD1 1 
ATOM   2698 C  CD2 . LEU A 1 333 ? 24.787  38.779  16.191  1.00 14.18 ? 333 LEU A CD2 1 
ATOM   2699 N  N   . TYR A 1 334 ? 27.274  40.182  20.212  1.00 12.76 ? 334 TYR A N   1 
ATOM   2700 C  CA  . TYR A 1 334 ? 27.987  41.053  21.173  1.00 13.84 ? 334 TYR A CA  1 
ATOM   2701 C  C   . TYR A 1 334 ? 28.466  42.281  20.427  1.00 13.42 ? 334 TYR A C   1 
ATOM   2702 O  O   . TYR A 1 334 ? 28.771  42.226  19.246  1.00 14.37 ? 334 TYR A O   1 
ATOM   2703 C  CB  . TYR A 1 334 ? 29.134  40.368  21.931  1.00 14.20 ? 334 TYR A CB  1 
ATOM   2704 C  CG  . TYR A 1 334 ? 30.331  40.008  21.111  1.00 13.84 ? 334 TYR A CG  1 
ATOM   2705 C  CD1 . TYR A 1 334 ? 31.365  40.909  20.911  1.00 15.00 ? 334 TYR A CD1 1 
ATOM   2706 C  CD2 . TYR A 1 334 ? 30.418  38.785  20.469  1.00 14.45 ? 334 TYR A CD2 1 
ATOM   2707 C  CE1 . TYR A 1 334 ? 32.437  40.607  20.106  1.00 16.37 ? 334 TYR A CE1 1 
ATOM   2708 C  CE2 . TYR A 1 334 ? 31.499  38.453  19.680  1.00 15.53 ? 334 TYR A CE2 1 
ATOM   2709 C  CZ  . TYR A 1 334 ? 32.513  39.374  19.486  1.00 17.57 ? 334 TYR A CZ  1 
ATOM   2710 O  OH  . TYR A 1 334 ? 33.571  39.090  18.666  1.00 18.21 ? 334 TYR A OH  1 
ATOM   2711 N  N   . ALA A 1 335 ? 28.552  43.382  21.159  1.00 14.34 ? 335 ALA A N   1 
ATOM   2712 C  CA  . ALA A 1 335 ? 29.058  44.653  20.606  1.00 14.55 ? 335 ALA A CA  1 
ATOM   2713 C  C   . ALA A 1 335 ? 30.587  44.578  20.477  1.00 14.64 ? 335 ALA A C   1 
ATOM   2714 O  O   . ALA A 1 335 ? 31.279  44.354  21.445  1.00 15.16 ? 335 ALA A O   1 
ATOM   2715 C  CB  . ALA A 1 335 ? 28.605  45.784  21.513  1.00 15.84 ? 335 ALA A CB  1 
ATOM   2716 N  N   . LYS A 1 336 ? 31.085  44.791  19.276  1.00 15.42 ? 336 LYS A N   1 
ATOM   2717 C  CA  . LYS A 1 336 ? 32.548  44.727  19.005  1.00 17.45 ? 336 LYS A CA  1 
ATOM   2718 C  C   . LYS A 1 336 ? 33.248  45.929  19.644  1.00 16.63 ? 336 LYS A C   1 
ATOM   2719 O  O   . LYS A 1 336 ? 34.456  45.820  19.984  1.00 19.52 ? 336 LYS A O   1 
ATOM   2720 C  CB  . LYS A 1 336 ? 32.755  44.683  17.488  1.00 17.44 ? 336 LYS A CB  1 
ATOM   2721 C  CG  . LYS A 1 336 ? 32.408  43.346  16.836  1.00 19.32 ? 336 LYS A CG  1 
ATOM   2722 C  CD  . LYS A 1 336 ? 32.305  43.356  15.325  1.00 20.68 ? 336 LYS A CD  1 
ATOM   2723 C  CE  . LYS A 1 336 ? 33.577  43.664  14.556  1.00 24.34 ? 336 LYS A CE  1 
ATOM   2724 N  NZ  . LYS A 1 336 ? 34.695  42.758  14.907  1.00 26.74 ? 336 LYS A NZ  1 
ATOM   2725 N  N   . GLU A 1 337 ? 32.539  47.047  19.747  1.00 18.48 ? 337 GLU A N   1 
ATOM   2726 C  CA  . GLU A 1 337 ? 33.077  48.320  20.306  1.00 19.29 ? 337 GLU A CA  1 
ATOM   2727 C  C   . GLU A 1 337 ? 31.921  49.040  20.986  1.00 23.40 ? 337 GLU A C   1 
ATOM   2728 O  O   . GLU A 1 337 ? 30.756  48.631  20.769  1.00 21.47 ? 337 GLU A O   1 
ATOM   2729 C  CB  . GLU A 1 337 ? 33.669  49.211  19.216  1.00 23.02 ? 337 GLU A CB  1 
ATOM   2730 C  CG  . GLU A 1 337 ? 34.794  48.583  18.400  1.00 25.36 ? 337 GLU A CG  1 
ATOM   2731 C  CD  . GLU A 1 337 ? 36.087  48.282  19.143  1.00 27.29 ? 337 GLU A CD  1 
ATOM   2732 O  OE1 . GLU A 1 337 ? 36.249  48.729  20.297  1.00 28.83 ? 337 GLU A OE1 1 
ATOM   2733 O  OE2 . GLU A 1 337 ? 36.937  47.582  18.561  1.00 29.30 ? 337 GLU A OE2 1 
ATOM   2734 N  N   . ASP A 1 338 ? 32.210  50.060  21.803  1.00 24.18 ? 338 ASP A N   1 
ATOM   2735 C  CA  . ASP A 1 338 ? 31.155  50.963  22.309  1.00 24.65 ? 338 ASP A CA  1 
ATOM   2736 C  C   . ASP A 1 338 ? 30.382  51.497  21.103  1.00 25.18 ? 338 ASP A C   1 
ATOM   2737 O  O   . ASP A 1 338 ? 30.983  51.822  20.042  1.00 25.05 ? 338 ASP A O   1 
ATOM   2738 C  CB  . ASP A 1 338 ? 31.760  52.117  23.122  1.00 24.05 ? 338 ASP A CB  1 
ATOM   2739 C  CG  . ASP A 1 338 ? 32.504  51.741  24.394  1.00 29.48 ? 338 ASP A CG  1 
ATOM   2740 O  OD1 . ASP A 1 338 ? 32.391  50.611  24.925  1.00 22.03 ? 338 ASP A OD1 1 
ATOM   2741 O  OD2 . ASP A 1 338 ? 33.248  52.629  24.886  1.00 35.78 ? 338 ASP A OD2 1 
ATOM   2742 N  N   . THR A 1 339 ? 29.059  51.584  21.220  1.00 22.91 ? 339 THR A N   1 
ATOM   2743 C  CA  . THR A 1 339 ? 28.201  51.971  20.089  1.00 23.27 ? 339 THR A CA  1 
ATOM   2744 C  C   . THR A 1 339 ? 26.852  52.360  20.680  1.00 24.04 ? 339 THR A C   1 
ATOM   2745 O  O   . THR A 1 339 ? 26.568  51.989  21.808  1.00 27.85 ? 339 THR A O   1 
ATOM   2746 C  CB  . THR A 1 339 ? 28.129  50.887  18.996  1.00 25.83 ? 339 THR A CB  1 
ATOM   2747 O  OG1 . THR A 1 339 ? 27.565  51.404  17.789  1.00 25.46 ? 339 THR A OG1 1 
ATOM   2748 C  CG2 . THR A 1 339 ? 27.328  49.675  19.418  1.00 23.73 ? 339 THR A CG2 1 
ATOM   2749 N  N   . VAL A 1 340 ? 26.033  53.005  19.882  1.00 24.15 ? 340 VAL A N   1 
ATOM   2750 C  CA  . VAL A 1 340 ? 24.671  53.377  20.329  1.00 23.48 ? 340 VAL A CA  1 
ATOM   2751 C  C   . VAL A 1 340 ? 23.710  52.665  19.403  1.00 22.30 ? 340 VAL A C   1 
ATOM   2752 O  O   . VAL A 1 340 ? 23.816  52.826  18.191  1.00 23.80 ? 340 VAL A O   1 
ATOM   2753 C  CB  . VAL A 1 340 ? 24.471  54.901  20.310  1.00 23.81 ? 340 VAL A CB  1 
ATOM   2754 C  CG1 . VAL A 1 340 ? 23.036  55.244  20.707  1.00 25.93 ? 340 VAL A CG1 1 
ATOM   2755 C  CG2 . VAL A 1 340 ? 25.493  55.553  21.225  1.00 24.95 ? 340 VAL A CG2 1 
ATOM   2756 N  N   . LEU A 1 341 ? 22.800  51.871  19.963  1.00 20.85 ? 341 LEU A N   1 
ATOM   2757 C  CA  . LEU A 1 341 ? 21.784  51.158  19.180  1.00 20.55 ? 341 LEU A CA  1 
ATOM   2758 C  C   . LEU A 1 341 ? 20.532  52.023  19.014  1.00 23.38 ? 341 LEU A C   1 
ATOM   2759 O  O   . LEU A 1 341 ? 20.016  52.515  20.043  1.00 24.73 ? 341 LEU A O   1 
ATOM   2760 C  CB  . LEU A 1 341 ? 21.435  49.872  19.937  1.00 22.65 ? 341 LEU A CB  1 
ATOM   2761 C  CG  . LEU A 1 341 ? 20.620  48.842  19.181  1.00 23.13 ? 341 LEU A CG  1 
ATOM   2762 C  CD1 . LEU A 1 341 ? 21.425  48.247  18.059  1.00 25.35 ? 341 LEU A CD1 1 
ATOM   2763 C  CD2 . LEU A 1 341 ? 20.199  47.733  20.122  1.00 23.99 ? 341 LEU A CD2 1 
ATOM   2764 N  N   . GLY A 1 342 ? 20.051  52.131  17.777  1.00 23.56 ? 342 GLY A N   1 
ATOM   2765 C  CA  . GLY A 1 342 ? 18.805  52.816  17.406  1.00 24.30 ? 342 GLY A CA  1 
ATOM   2766 C  C   . GLY A 1 342 ? 18.806  54.308  17.775  1.00 23.91 ? 342 GLY A C   1 
ATOM   2767 O  O   . GLY A 1 342 ? 17.710  54.850  17.949  1.00 26.65 ? 342 GLY A O   1 
ATOM   2768 N  N   . GLY A 1 343 ? 19.992  54.917  17.934  1.00 23.77 ? 343 GLY A N   1 
ATOM   2769 C  CA  . GLY A 1 343 ? 20.155  56.322  18.361  1.00 25.36 ? 343 GLY A CA  1 
ATOM   2770 C  C   . GLY A 1 343 ? 19.679  56.600  19.767  1.00 27.39 ? 343 GLY A C   1 
ATOM   2771 O  O   . GLY A 1 343 ? 19.477  57.792  20.103  1.00 29.16 ? 343 GLY A O   1 
ATOM   2772 N  N   . GLU A 1 344 ? 19.519  55.584  20.616  1.00 25.29 ? 344 GLU A N   1 
ATOM   2773 C  CA  . GLU A 1 344 ? 18.819  55.705  21.919  1.00 27.13 ? 344 GLU A CA  1 
ATOM   2774 C  C   . GLU A 1 344 ? 19.465  54.854  23.003  1.00 25.79 ? 344 GLU A C   1 
ATOM   2775 O  O   . GLU A 1 344 ? 19.345  55.213  24.174  1.00 29.60 ? 344 GLU A O   1 
ATOM   2776 C  CB  . GLU A 1 344 ? 17.354  55.259  21.842  1.00 30.61 ? 344 GLU A CB  1 
ATOM   2777 C  CG  . GLU A 1 344 ? 16.515  56.053  20.871  1.00 33.90 ? 344 GLU A CG  1 
ATOM   2778 C  CD  . GLU A 1 344 ? 15.108  55.517  20.695  1.00 41.53 ? 344 GLU A CD  1 
ATOM   2779 O  OE1 . GLU A 1 344 ? 14.910  54.662  19.814  1.00 42.98 ? 344 GLU A OE1 1 
ATOM   2780 O  OE2 . GLU A 1 344 ? 14.219  55.953  21.447  1.00 51.66 ? 344 GLU A OE2 1 
ATOM   2781 N  N   . TYR A 1 345 ? 20.075  53.715  22.665  1.00 22.40 ? 345 TYR A N   1 
ATOM   2782 C  CA  . TYR A 1 345 ? 20.504  52.748  23.704  1.00 22.56 ? 345 TYR A CA  1 
ATOM   2783 C  C   . TYR A 1 345 ? 22.008  52.553  23.650  1.00 25.31 ? 345 TYR A C   1 
ATOM   2784 O  O   . TYR A 1 345 ? 22.512  51.825  22.787  1.00 22.29 ? 345 TYR A O   1 
ATOM   2785 C  CB  . TYR A 1 345 ? 19.780  51.416  23.524  1.00 22.70 ? 345 TYR A CB  1 
ATOM   2786 C  CG  . TYR A 1 345 ? 18.287  51.538  23.571  1.00 22.09 ? 345 TYR A CG  1 
ATOM   2787 C  CD1 . TYR A 1 345 ? 17.660  51.848  24.763  1.00 25.93 ? 345 TYR A CD1 1 
ATOM   2788 C  CD2 . TYR A 1 345 ? 17.533  51.470  22.428  1.00 22.32 ? 345 TYR A CD2 1 
ATOM   2789 C  CE1 . TYR A 1 345 ? 16.295  52.007  24.827  1.00 22.57 ? 345 TYR A CE1 1 
ATOM   2790 C  CE2 . TYR A 1 345 ? 16.160  51.614  22.470  1.00 24.91 ? 345 TYR A CE2 1 
ATOM   2791 C  CZ  . TYR A 1 345 ? 15.545  51.908  23.674  1.00 25.24 ? 345 TYR A CZ  1 
ATOM   2792 O  OH  . TYR A 1 345 ? 14.191  52.043  23.763  1.00 29.52 ? 345 TYR A OH  1 
ATOM   2793 N  N   . PRO A 1 346 ? 22.780  53.191  24.545  1.00 24.25 ? 346 PRO A N   1 
ATOM   2794 C  CA  . PRO A 1 346 ? 24.234  53.072  24.512  1.00 24.48 ? 346 PRO A CA  1 
ATOM   2795 C  C   . PRO A 1 346 ? 24.647  51.677  24.979  1.00 22.31 ? 346 PRO A C   1 
ATOM   2796 O  O   . PRO A 1 346 ? 24.134  51.160  25.958  1.00 23.05 ? 346 PRO A O   1 
ATOM   2797 C  CB  . PRO A 1 346 ? 24.721  54.174  25.462  1.00 24.19 ? 346 PRO A CB  1 
ATOM   2798 C  CG  . PRO A 1 346 ? 23.541  55.101  25.531  1.00 29.50 ? 346 PRO A CG  1 
ATOM   2799 C  CD  . PRO A 1 346 ? 22.333  54.195  25.533  1.00 26.25 ? 346 PRO A CD  1 
ATOM   2800 N  N   . LEU A 1 347 ? 25.602  51.102  24.263  1.00 21.88 ? 347 LEU A N   1 
ATOM   2801 C  CA  . LEU A 1 347 ? 26.170  49.774  24.564  1.00 20.51 ? 347 LEU A CA  1 
ATOM   2802 C  C   . LEU A 1 347 ? 27.666  49.927  24.746  1.00 19.26 ? 347 LEU A C   1 
ATOM   2803 O  O   . LEU A 1 347 ? 28.255  50.752  24.021  1.00 22.31 ? 347 LEU A O   1 
ATOM   2804 C  CB  . LEU A 1 347 ? 25.889  48.819  23.399  1.00 19.25 ? 347 LEU A CB  1 
ATOM   2805 C  CG  . LEU A 1 347 ? 24.419  48.556  23.070  1.00 19.20 ? 347 LEU A CG  1 
ATOM   2806 C  CD1 . LEU A 1 347 ? 24.334  47.613  21.894  1.00 19.52 ? 347 LEU A CD1 1 
ATOM   2807 C  CD2 . LEU A 1 347 ? 23.699  47.996  24.278  1.00 20.34 ? 347 LEU A CD2 1 
ATOM   2808 N  N   . GLU A 1 348 ? 28.194  49.184  25.702  1.00 19.19 ? 348 GLU A N   1 
ATOM   2809 C  CA  . GLU A 1 348 ? 29.642  49.031  25.910  1.00 19.96 ? 348 GLU A CA  1 
ATOM   2810 C  C   . GLU A 1 348 ? 30.177  47.851  25.107  1.00 20.74 ? 348 GLU A C   1 
ATOM   2811 O  O   . GLU A 1 348 ? 29.431  46.875  24.884  1.00 16.93 ? 348 GLU A O   1 
ATOM   2812 C  CB  . GLU A 1 348 ? 29.926  48.824  27.385  1.00 23.08 ? 348 GLU A CB  1 
ATOM   2813 C  CG  . GLU A 1 348 ? 29.681  50.061  28.223  1.00 29.30 ? 348 GLU A CG  1 
ATOM   2814 C  CD  . GLU A 1 348 ? 29.990  49.719  29.672  1.00 32.27 ? 348 GLU A CD  1 
ATOM   2815 O  OE1 . GLU A 1 348 ? 29.126  49.093  30.341  1.00 39.64 ? 348 GLU A OE1 1 
ATOM   2816 O  OE2 . GLU A 1 348 ? 31.133  49.977  30.088  1.00 37.47 ? 348 GLU A OE2 1 
ATOM   2817 N  N   . LYS A 1 349 ? 31.447  47.954  24.741  1.00 18.12 ? 349 LYS A N   1 
ATOM   2818 C  CA  . LYS A 1 349 ? 32.159  46.855  24.093  1.00 18.30 ? 349 LYS A CA  1 
ATOM   2819 C  C   . LYS A 1 349 ? 31.886  45.592  24.906  1.00 17.67 ? 349 LYS A C   1 
ATOM   2820 O  O   . LYS A 1 349 ? 32.051  45.581  26.128  1.00 20.07 ? 349 LYS A O   1 
ATOM   2821 C  CB  . LYS A 1 349 ? 33.661  47.151  24.018  1.00 19.64 ? 349 LYS A CB  1 
ATOM   2822 C  CG  . LYS A 1 349 ? 34.479  46.004  23.458  1.00 18.89 ? 349 LYS A CG  1 
ATOM   2823 C  CD  . LYS A 1 349 ? 35.976  46.347  23.417  1.00 20.94 ? 349 LYS A CD  1 
ATOM   2824 C  CE  . LYS A 1 349 ? 36.801  45.258  22.785  1.00 22.38 ? 349 LYS A CE  1 
ATOM   2825 N  NZ  . LYS A 1 349 ? 38.230  45.642  22.673  1.00 25.84 ? 349 LYS A NZ  1 
ATOM   2826 N  N   . GLY A 1 350 ? 31.443  44.509  24.249  1.00 15.96 ? 350 GLY A N   1 
ATOM   2827 C  CA  . GLY A 1 350 ? 31.208  43.212  24.894  1.00 16.60 ? 350 GLY A CA  1 
ATOM   2828 C  C   . GLY A 1 350 ? 29.763  43.007  25.343  1.00 16.04 ? 350 GLY A C   1 
ATOM   2829 O  O   . GLY A 1 350 ? 29.443  41.898  25.760  1.00 16.90 ? 350 GLY A O   1 
ATOM   2830 N  N   . ASP A 1 351 ? 28.945  44.055  25.339  1.00 16.30 ? 351 ASP A N   1 
ATOM   2831 C  CA  . ASP A 1 351 ? 27.541  43.907  25.791  1.00 16.93 ? 351 ASP A CA  1 
ATOM   2832 C  C   . ASP A 1 351 ? 26.815  42.892  24.891  1.00 15.63 ? 351 ASP A C   1 
ATOM   2833 O  O   . ASP A 1 351 ? 27.008  42.896  23.684  1.00 15.97 ? 351 ASP A O   1 
ATOM   2834 C  CB  . ASP A 1 351 ? 26.754  45.216  25.797  1.00 16.31 ? 351 ASP A CB  1 
ATOM   2835 C  CG  . ASP A 1 351 ? 27.070  46.121  26.967  1.00 18.41 ? 351 ASP A CG  1 
ATOM   2836 O  OD1 . ASP A 1 351 ? 27.740  45.642  27.881  1.00 20.26 ? 351 ASP A OD1 1 
ATOM   2837 O  OD2 . ASP A 1 351 ? 26.569  47.269  26.912  1.00 21.32 ? 351 ASP A OD2 1 
ATOM   2838 N  N   . GLU A 1 352 ? 26.016  42.036  25.508  1.00 14.27 ? 352 GLU A N   1 
ATOM   2839 C  CA  . GLU A 1 352 ? 25.367  40.903  24.846  1.00 14.21 ? 352 GLU A CA  1 
ATOM   2840 C  C   . GLU A 1 352 ? 23.915  41.242  24.516  1.00 15.51 ? 352 GLU A C   1 
ATOM   2841 O  O   . GLU A 1 352 ? 23.205  41.792  25.358  1.00 15.69 ? 352 GLU A O   1 
ATOM   2842 C  CB  . GLU A 1 352 ? 25.429  39.679  25.735  1.00 15.48 ? 352 GLU A CB  1 
ATOM   2843 C  CG  . GLU A 1 352 ? 26.843  39.226  26.045  1.00 18.34 ? 352 GLU A CG  1 
ATOM   2844 C  CD  . GLU A 1 352 ? 26.920  38.090  27.073  1.00 24.66 ? 352 GLU A CD  1 
ATOM   2845 O  OE1 . GLU A 1 352 ? 26.449  36.990  26.795  1.00 25.49 ? 352 GLU A OE1 1 
ATOM   2846 O  OE2 . GLU A 1 352 ? 27.429  38.312  28.210  1.00 37.79 ? 352 GLU A OE2 1 
ATOM   2847 N  N   . LEU A 1 353 ? 23.503  40.861  23.313  1.00 13.29 ? 353 LEU A N   1 
ATOM   2848 C  CA  . LEU A 1 353 ? 22.153  41.034  22.741  1.00 14.05 ? 353 LEU A CA  1 
ATOM   2849 C  C   . LEU A 1 353 ? 21.589  39.655  22.415  1.00 14.22 ? 353 LEU A C   1 
ATOM   2850 O  O   . LEU A 1 353 ? 22.353  38.775  22.032  1.00 14.06 ? 353 LEU A O   1 
ATOM   2851 C  CB  . LEU A 1 353 ? 22.182  41.872  21.462  1.00 13.75 ? 353 LEU A CB  1 
ATOM   2852 C  CG  . LEU A 1 353 ? 22.970  43.164  21.530  1.00 18.07 ? 353 LEU A CG  1 
ATOM   2853 C  CD1 . LEU A 1 353 ? 22.926  43.833  20.178  1.00 18.77 ? 353 LEU A CD1 1 
ATOM   2854 C  CD2 . LEU A 1 353 ? 22.416  44.057  22.612  1.00 19.52 ? 353 LEU A CD2 1 
ATOM   2855 N  N   . MET A 1 354 ? 20.281  39.495  22.500  1.00 13.53 ? 354 MET A N   1 
ATOM   2856 C  CA  . MET A 1 354 ? 19.615  38.277  22.041  1.00 12.33 ? 354 MET A CA  1 
ATOM   2857 C  C   . MET A 1 354 ? 18.507  38.694  21.120  1.00 14.56 ? 354 MET A C   1 
ATOM   2858 O  O   . MET A 1 354 ? 17.650  39.522  21.500  1.00 14.83 ? 354 MET A O   1 
ATOM   2859 C  CB  . MET A 1 354 ? 19.054  37.473  23.214  1.00 13.61 ? 354 MET A CB  1 
ATOM   2860 C  CG  . MET A 1 354 ? 18.482  36.170  22.781  1.00 14.41 ? 354 MET A CG  1 
ATOM   2861 S  SD  . MET A 1 354 ? 19.704  34.955  22.269  1.00 16.00 ? 354 MET A SD  1 
ATOM   2862 C  CE  . MET A 1 354 ? 20.341  34.474  23.851  1.00 17.81 ? 354 MET A CE  1 
ATOM   2863 N  N   . VAL A 1 355 ? 18.487  38.160  19.910  1.00 12.93 ? 355 VAL A N   1 
ATOM   2864 C  CA  . VAL A 1 355 ? 17.421  38.418  18.896  1.00 12.81 ? 355 VAL A CA  1 
ATOM   2865 C  C   . VAL A 1 355 ? 16.316  37.402  19.122  1.00 13.25 ? 355 VAL A C   1 
ATOM   2866 O  O   . VAL A 1 355 ? 16.579  36.172  19.076  1.00 13.33 ? 355 VAL A O   1 
ATOM   2867 C  CB  . VAL A 1 355 ? 17.974  38.315  17.476  1.00 14.24 ? 355 VAL A CB  1 
ATOM   2868 C  CG1 . VAL A 1 355 ? 16.828  38.388  16.482  1.00 14.68 ? 355 VAL A CG1 1 
ATOM   2869 C  CG2 . VAL A 1 355 ? 19.017  39.399  17.219  1.00 14.48 ? 355 VAL A CG2 1 
ATOM   2870 N  N   . LEU A 1 356 ? 15.111  37.874  19.408  1.00 12.36 ? 356 LEU A N   1 
ATOM   2871 C  CA  . LEU A 1 356 ? 13.929  37.003  19.546  1.00 12.82 ? 356 LEU A CA  1 
ATOM   2872 C  C   . LEU A 1 356 ? 13.262  36.880  18.189  1.00 12.84 ? 356 LEU A C   1 
ATOM   2873 O  O   . LEU A 1 356 ? 12.467  37.745  17.783  1.00 14.02 ? 356 LEU A O   1 
ATOM   2874 C  CB  . LEU A 1 356 ? 12.953  37.569  20.588  1.00 14.74 ? 356 LEU A CB  1 
ATOM   2875 C  CG  . LEU A 1 356 ? 13.416  37.527  22.029  1.00 16.34 ? 356 LEU A CG  1 
ATOM   2876 C  CD1 . LEU A 1 356 ? 12.352  38.232  22.872  1.00 15.55 ? 356 LEU A CD1 1 
ATOM   2877 C  CD2 . LEU A 1 356 ? 13.651  36.107  22.520  1.00 19.96 ? 356 LEU A CD2 1 
ATOM   2878 N  N   . ILE A 1 357 ? 13.588  35.834  17.449  1.00 11.94 ? 357 ILE A N   1 
ATOM   2879 C  CA  . ILE A 1 357 ? 13.174  35.752  16.034  1.00 11.50 ? 357 ILE A CA  1 
ATOM   2880 C  C   . ILE A 1 357 ? 11.644  35.698  15.957  1.00 11.71 ? 357 ILE A C   1 
ATOM   2881 O  O   . ILE A 1 357 ? 11.099  36.280  15.019  1.00 12.60 ? 357 ILE A O   1 
ATOM   2882 C  CB  . ILE A 1 357 ? 13.829  34.582  15.276  1.00 12.99 ? 357 ILE A CB  1 
ATOM   2883 C  CG1 . ILE A 1 357 ? 15.363  34.574  15.426  1.00 12.90 ? 357 ILE A CG1 1 
ATOM   2884 C  CG2 . ILE A 1 357 ? 13.435  34.634  13.799  1.00 14.19 ? 357 ILE A CG2 1 
ATOM   2885 C  CD1 . ILE A 1 357 ? 16.029  33.333  14.841  1.00 11.64 ? 357 ILE A CD1 1 
ATOM   2886 N  N   . PRO A 1 358 ? 10.909  34.991  16.818  1.00 11.82 ? 358 PRO A N   1 
ATOM   2887 C  CA  . PRO A 1 358 ? 9.447   34.984  16.696  1.00 12.95 ? 358 PRO A CA  1 
ATOM   2888 C  C   . PRO A 1 358 ? 8.830   36.378  16.838  1.00 13.37 ? 358 PRO A C   1 
ATOM   2889 O  O   . PRO A 1 358 ? 7.813   36.654  16.156  1.00 13.30 ? 358 PRO A O   1 
ATOM   2890 C  CB  . PRO A 1 358 ? 8.964   34.086  17.830  1.00 13.43 ? 358 PRO A CB  1 
ATOM   2891 C  CG  . PRO A 1 358 ? 10.131  33.195  18.084  1.00 13.94 ? 358 PRO A CG  1 
ATOM   2892 C  CD  . PRO A 1 358 ? 11.314  34.109  17.921  1.00 13.23 ? 358 PRO A CD  1 
ATOM   2893 N  N   . GLN A 1 359 ? 9.462   37.253  17.614  1.00 13.44 ? 359 GLN A N   1 
ATOM   2894 C  CA  . GLN A 1 359 ? 8.971   38.645  17.759  1.00 14.16 ? 359 GLN A CA  1 
ATOM   2895 C  C   . GLN A 1 359 ? 9.347   39.502  16.560  1.00 13.31 ? 359 GLN A C   1 
ATOM   2896 O  O   . GLN A 1 359 ? 8.496   40.241  16.083  1.00 14.67 ? 359 GLN A O   1 
ATOM   2897 C  CB  . GLN A 1 359 ? 9.552   39.266  19.026  1.00 14.73 ? 359 GLN A CB  1 
ATOM   2898 C  CG  . GLN A 1 359 ? 9.019   38.678  20.304  1.00 17.17 ? 359 GLN A CG  1 
ATOM   2899 C  CD  . GLN A 1 359 ? 7.507   38.685  20.361  1.00 16.41 ? 359 GLN A CD  1 
ATOM   2900 O  OE1 . GLN A 1 359 ? 6.856   37.653  20.339  1.00 17.61 ? 359 GLN A OE1 1 
ATOM   2901 N  NE2 . GLN A 1 359 ? 6.964   39.872  20.557  1.00 20.51 ? 359 GLN A NE2 1 
ATOM   2902 N  N   . LEU A 1 360 ? 10.557  39.359  16.026  1.00 12.83 ? 360 LEU A N   1 
ATOM   2903 C  CA  . LEU A 1 360 ? 10.934  40.028  14.769  1.00 13.09 ? 360 LEU A CA  1 
ATOM   2904 C  C   . LEU A 1 360 ? 9.861   39.713  13.714  1.00 13.47 ? 360 LEU A C   1 
ATOM   2905 O  O   . LEU A 1 360 ? 9.432   40.580  12.955  1.00 14.67 ? 360 LEU A O   1 
ATOM   2906 C  CB  . LEU A 1 360 ? 12.295  39.491  14.315  1.00 13.00 ? 360 LEU A CB  1 
ATOM   2907 C  CG  . LEU A 1 360 ? 12.737  39.916  12.919  1.00 13.40 ? 360 LEU A CG  1 
ATOM   2908 C  CD1 . LEU A 1 360 ? 12.976  41.428  12.841  1.00 14.43 ? 360 LEU A CD1 1 
ATOM   2909 C  CD2 . LEU A 1 360 ? 13.987  39.130  12.532  1.00 15.29 ? 360 LEU A CD2 1 
ATOM   2910 N  N   . HIS A 1 361 ? 9.471   38.444  13.598  1.00 11.98 ? 361 HIS A N   1 
ATOM   2911 C  CA  . HIS A 1 361 ? 8.540   37.945  12.564  1.00 12.63 ? 361 HIS A CA  1 
ATOM   2912 C  C   . HIS A 1 361 ? 7.096   38.360  12.829  1.00 13.17 ? 361 HIS A C   1 
ATOM   2913 O  O   . HIS A 1 361 ? 6.253   38.079  11.962  1.00 15.63 ? 361 HIS A O   1 
ATOM   2914 C  CB  . HIS A 1 361 ? 8.689   36.426  12.477  1.00 12.01 ? 361 HIS A CB  1 
ATOM   2915 C  CG  . HIS A 1 361 ? 9.988   35.993  11.878  1.00 12.36 ? 361 HIS A CG  1 
ATOM   2916 N  ND1 . HIS A 1 361 ? 10.295  34.659  11.784  1.00 12.50 ? 361 HIS A ND1 1 
ATOM   2917 C  CD2 . HIS A 1 361 ? 11.049  36.683  11.358  1.00 11.81 ? 361 HIS A CD2 1 
ATOM   2918 C  CE1 . HIS A 1 361 ? 11.518  34.553  11.215  1.00 12.38 ? 361 HIS A CE1 1 
ATOM   2919 N  NE2 . HIS A 1 361 ? 12.028  35.797  10.965  1.00 11.31 ? 361 HIS A NE2 1 
ATOM   2920 N  N   . ARG A 1 362 ? 6.829   38.994  13.994  1.00 13.95 ? 362 ARG A N   1 
ATOM   2921 C  CA  . ARG A 1 362 ? 5.501   39.574  14.331  1.00 14.64 ? 362 ARG A CA  1 
ATOM   2922 C  C   . ARG A 1 362 ? 5.549   41.106  14.341  1.00 14.58 ? 362 ARG A C   1 
ATOM   2923 O  O   . ARG A 1 362 ? 4.575   41.735  14.860  1.00 16.28 ? 362 ARG A O   1 
ATOM   2924 C  CB  . ARG A 1 362 ? 5.066   39.008  15.675  1.00 14.97 ? 362 ARG A CB  1 
ATOM   2925 C  CG  . ARG A 1 362 ? 4.530   37.601  15.611  1.00 15.33 ? 362 ARG A CG  1 
ATOM   2926 C  CD  . ARG A 1 362 ? 4.562   36.939  16.986  1.00 15.22 ? 362 ARG A CD  1 
ATOM   2927 N  NE  . ARG A 1 362 ? 3.925   35.638  16.946  1.00 15.98 ? 362 ARG A NE  1 
ATOM   2928 C  CZ  . ARG A 1 362 ? 4.532   34.518  16.515  1.00 15.16 ? 362 ARG A CZ  1 
ATOM   2929 N  NH1 . ARG A 1 362 ? 5.791   34.561  16.089  1.00 13.85 ? 362 ARG A NH1 1 
ATOM   2930 N  NH2 . ARG A 1 362 ? 3.841   33.382  16.486  1.00 16.50 ? 362 ARG A NH2 1 
ATOM   2931 N  N   . ASP A 1 363 ? 6.593   41.725  13.798  1.00 14.25 ? 363 ASP A N   1 
ATOM   2932 C  CA  . ASP A 1 363 ? 6.674   43.205  13.768  1.00 15.32 ? 363 ASP A CA  1 
ATOM   2933 C  C   . ASP A 1 363 ? 5.617   43.718  12.795  1.00 15.98 ? 363 ASP A C   1 
ATOM   2934 O  O   . ASP A 1 363 ? 5.828   43.655  11.578  1.00 16.61 ? 363 ASP A O   1 
ATOM   2935 C  CB  . ASP A 1 363 ? 8.081   43.635  13.452  1.00 15.17 ? 363 ASP A CB  1 
ATOM   2936 C  CG  . ASP A 1 363 ? 8.346   45.121  13.529  1.00 17.04 ? 363 ASP A CG  1 
ATOM   2937 O  OD1 . ASP A 1 363 ? 7.342   45.898  13.412  1.00 18.80 ? 363 ASP A OD1 1 
ATOM   2938 O  OD2 . ASP A 1 363 ? 9.524   45.472  13.614  1.00 17.11 ? 363 ASP A OD2 1 
ATOM   2939 N  N   . LYS A 1 364 ? 4.581   44.361  13.346  1.00 16.10 ? 364 LYS A N   1 
ATOM   2940 C  CA  . LYS A 1 364 ? 3.451   44.831  12.520  1.00 15.63 ? 364 LYS A CA  1 
ATOM   2941 C  C   . LYS A 1 364 ? 3.886   45.969  11.599  1.00 16.44 ? 364 LYS A C   1 
ATOM   2942 O  O   . LYS A 1 364 ? 3.219   46.148  10.554  1.00 18.79 ? 364 LYS A O   1 
ATOM   2943 C  CB  . LYS A 1 364 ? 2.289   45.246  13.434  1.00 17.38 ? 364 LYS A CB  1 
ATOM   2944 C  CG  . LYS A 1 364 ? 1.692   44.088  14.212  1.00 20.12 ? 364 LYS A CG  1 
ATOM   2945 C  CD  . LYS A 1 364 ? 0.509   44.490  15.082  1.00 22.90 ? 364 LYS A CD  1 
ATOM   2946 C  CE  . LYS A 1 364 ? -0.132  43.283  15.721  1.00 27.65 ? 364 LYS A CE  1 
ATOM   2947 N  NZ  . LYS A 1 364 ? -1.053  43.696  16.811  1.00 36.25 ? 364 LYS A NZ  1 
ATOM   2948 N  N   . THR A 1 365 ? 4.969   46.679  11.898  1.00 16.80 ? 365 THR A N   1 
ATOM   2949 C  CA  . THR A 1 365 ? 5.452   47.796  11.044  1.00 18.34 ? 365 THR A CA  1 
ATOM   2950 C  C   . THR A 1 365 ? 5.996   47.222  9.736   1.00 20.05 ? 365 THR A C   1 
ATOM   2951 O  O   . THR A 1 365 ? 6.053   47.940  8.752   1.00 21.94 ? 365 THR A O   1 
ATOM   2952 C  CB  . THR A 1 365 ? 6.479   48.686  11.718  1.00 19.27 ? 365 THR A CB  1 
ATOM   2953 O  OG1 . THR A 1 365 ? 7.719   48.005  11.811  1.00 20.17 ? 365 THR A OG1 1 
ATOM   2954 C  CG2 . THR A 1 365 ? 6.019   49.157  13.077  1.00 20.95 ? 365 THR A CG2 1 
ATOM   2955 N  N   . ILE A 1 366 ? 6.398   45.954  9.744   1.00 19.49 ? 366 ILE A N   1 
ATOM   2956 C  CA  . ILE A 1 366 ? 6.941   45.234  8.565   1.00 21.12 ? 366 ILE A CA  1 
ATOM   2957 C  C   . ILE A 1 366 ? 5.816   44.453  7.901   1.00 21.10 ? 366 ILE A C   1 
ATOM   2958 O  O   . ILE A 1 366 ? 5.648   44.576  6.660   1.00 23.66 ? 366 ILE A O   1 
ATOM   2959 C  CB  . ILE A 1 366 ? 8.068   44.286  8.997   1.00 20.54 ? 366 ILE A CB  1 
ATOM   2960 C  CG1 . ILE A 1 366 ? 9.259   45.049  9.563   1.00 20.46 ? 366 ILE A CG1 1 
ATOM   2961 C  CG2 . ILE A 1 366 ? 8.439   43.371  7.847   1.00 21.04 ? 366 ILE A CG2 1 
ATOM   2962 C  CD1 . ILE A 1 366 ? 9.946   45.983  8.615   1.00 21.78 ? 366 ILE A CD1 1 
ATOM   2963 N  N   . TRP A 1 367 ? 5.080   43.631  8.642   1.00 18.38 ? 367 TRP A N   1 
ATOM   2964 C  CA  . TRP A 1 367 ? 4.226   42.570  8.069   1.00 19.18 ? 367 TRP A CA  1 
ATOM   2965 C  C   . TRP A 1 367 ? 2.768   42.992  7.974   1.00 18.94 ? 367 TRP A C   1 
ATOM   2966 O  O   . TRP A 1 367 ? 2.031   42.324  7.270   1.00 22.93 ? 367 TRP A O   1 
ATOM   2967 C  CB  . TRP A 1 367 ? 4.340   41.280  8.880   1.00 18.18 ? 367 TRP A CB  1 
ATOM   2968 C  CG  . TRP A 1 367 ? 5.736   40.761  8.917   1.00 16.90 ? 367 TRP A CG  1 
ATOM   2969 C  CD1 . TRP A 1 367 ? 6.638   40.950  9.916   1.00 17.99 ? 367 TRP A CD1 1 
ATOM   2970 C  CD2 . TRP A 1 367 ? 6.383   39.924  7.947   1.00 16.60 ? 367 TRP A CD2 1 
ATOM   2971 N  NE1 . TRP A 1 367 ? 7.817   40.335  9.610   1.00 16.62 ? 367 TRP A NE1 1 
ATOM   2972 C  CE2 . TRP A 1 367 ? 7.691   39.665  8.432   1.00 15.81 ? 367 TRP A CE2 1 
ATOM   2973 C  CE3 . TRP A 1 367 ? 6.003   39.413  6.707   1.00 15.91 ? 367 TRP A CE3 1 
ATOM   2974 C  CZ2 . TRP A 1 367 ? 8.622   38.905  7.722   1.00 15.86 ? 367 TRP A CZ2 1 
ATOM   2975 C  CZ3 . TRP A 1 367 ? 6.911   38.641  6.036   1.00 14.77 ? 367 TRP A CZ3 1 
ATOM   2976 C  CH2 . TRP A 1 367 ? 8.183   38.396  6.524   1.00 16.00 ? 367 TRP A CH2 1 
ATOM   2977 N  N   . GLY A 1 368 ? 2.377   44.075  8.645   1.00 18.24 ? 368 GLY A N   1 
ATOM   2978 C  CA  . GLY A 1 368 ? 0.960   44.493  8.719   1.00 19.42 ? 368 GLY A CA  1 
ATOM   2979 C  C   . GLY A 1 368 ? 0.333   44.017  9.999   1.00 21.37 ? 368 GLY A C   1 
ATOM   2980 O  O   . GLY A 1 368 ? 1.038   43.367  10.791  1.00 22.81 ? 368 GLY A O   1 
ATOM   2981 N  N   . ASP A 1 369 ? -0.958  44.268  10.223  1.00 21.65 ? 369 ASP A N   1 
ATOM   2982 C  CA  . ASP A 1 369 ? -1.557  44.003  11.553  1.00 23.34 ? 369 ASP A CA  1 
ATOM   2983 C  C   . ASP A 1 369 ? -1.951  42.529  11.691  1.00 25.48 ? 369 ASP A C   1 
ATOM   2984 O  O   . ASP A 1 369 ? -2.116  42.085  12.846  1.00 30.31 ? 369 ASP A O   1 
ATOM   2985 C  CB  . ASP A 1 369 ? -2.716  44.969  11.802  1.00 27.35 ? 369 ASP A CB  1 
ATOM   2986 C  CG  . ASP A 1 369 ? -2.242  46.358  12.154  1.00 30.46 ? 369 ASP A CG  1 
ATOM   2987 O  OD1 . ASP A 1 369 ? -1.011  46.555  12.331  1.00 29.67 ? 369 ASP A OD1 1 
ATOM   2988 O  OD2 . ASP A 1 369 ? -3.117  47.253  12.257  1.00 33.95 ? 369 ASP A OD2 1 
ATOM   2989 N  N   . ASP A 1 370 ? -2.069  41.807  10.582  1.00 24.96 ? 370 ASP A N   1 
ATOM   2990 C  CA  . ASP A 1 370 ? -2.560  40.396  10.519  1.00 25.63 ? 370 ASP A CA  1 
ATOM   2991 C  C   . ASP A 1 370 ? -1.411  39.402  10.739  1.00 21.30 ? 370 ASP A C   1 
ATOM   2992 O  O   . ASP A 1 370 ? -1.473  38.294  10.193  1.00 23.38 ? 370 ASP A O   1 
ATOM   2993 C  CB  . ASP A 1 370 ? -3.260  40.129  9.191   1.00 26.53 ? 370 ASP A CB  1 
ATOM   2994 C  CG  . ASP A 1 370 ? -2.318  40.043  7.990   1.00 30.45 ? 370 ASP A CG  1 
ATOM   2995 O  OD1 . ASP A 1 370 ? -1.104  40.413  8.128   1.00 31.45 ? 370 ASP A OD1 1 
ATOM   2996 O  OD2 . ASP A 1 370 ? -2.783  39.568  6.943   1.00 35.69 ? 370 ASP A OD2 1 
ATOM   2997 N  N   . VAL A 1 371 ? -0.423  39.753  11.559  1.00 24.91 ? 371 VAL A N   1 
ATOM   2998 C  CA  . VAL A 1 371 ? 0.826   38.944  11.711  1.00 21.63 ? 371 VAL A CA  1 
ATOM   2999 C  C   . VAL A 1 371 ? 0.524   37.530  12.180  1.00 21.44 ? 371 VAL A C   1 
ATOM   3000 O  O   . VAL A 1 371 ? 1.395   36.639  11.936  1.00 19.07 ? 371 VAL A O   1 
ATOM   3001 C  CB  . VAL A 1 371 ? 1.841   39.557  12.689  1.00 23.26 ? 371 VAL A CB  1 
ATOM   3002 C  CG1 . VAL A 1 371 ? 2.668   40.582  11.960  1.00 25.51 ? 371 VAL A CG1 1 
ATOM   3003 C  CG2 . VAL A 1 371 ? 1.211   40.101  13.962  1.00 25.35 ? 371 VAL A CG2 1 
ATOM   3004 N  N   . GLU A 1 372 ? -0.576  37.285  12.880  1.00 19.70 ? 372 GLU A N   1 
ATOM   3005 C  CA  . GLU A 1 372 ? -0.838  35.943  13.449  1.00 19.42 ? 372 GLU A CA  1 
ATOM   3006 C  C   . GLU A 1 372 ? -1.457  34.987  12.423  1.00 19.46 ? 372 GLU A C   1 
ATOM   3007 O  O   . GLU A 1 372 ? -1.555  33.770  12.709  1.00 20.94 ? 372 GLU A O   1 
ATOM   3008 C  CB  . GLU A 1 372 ? -1.715  36.050  14.707  1.00 22.61 ? 372 GLU A CB  1 
ATOM   3009 C  CG  . GLU A 1 372 ? -1.027  36.654  15.915  1.00 23.45 ? 372 GLU A CG  1 
ATOM   3010 C  CD  . GLU A 1 372 ? 0.232   35.967  16.451  1.00 27.98 ? 372 GLU A CD  1 
ATOM   3011 O  OE1 . GLU A 1 372 ? 0.278   34.692  16.509  1.00 31.18 ? 372 GLU A OE1 1 
ATOM   3012 O  OE2 . GLU A 1 372 ? 1.144   36.715  16.863  1.00 31.05 ? 372 GLU A OE2 1 
ATOM   3013 N  N   . GLU A 1 373 ? -1.878  35.472  11.258  1.00 16.74 ? 373 GLU A N   1 
ATOM   3014 C  CA  . GLU A 1 373 ? -2.527  34.699  10.193  1.00 19.46 ? 373 GLU A CA  1 
ATOM   3015 C  C   . GLU A 1 373 ? -1.457  33.939  9.404   1.00 18.18 ? 373 GLU A C   1 
ATOM   3016 O  O   . GLU A 1 373 ? -0.389  34.508  9.123   1.00 17.16 ? 373 GLU A O   1 
ATOM   3017 C  CB  . GLU A 1 373 ? -3.344  35.606  9.280   1.00 22.30 ? 373 GLU A CB  1 
ATOM   3018 C  CG  . GLU A 1 373 ? -4.515  36.219  10.052  1.00 26.10 ? 373 GLU A CG  1 
ATOM   3019 C  CD  . GLU A 1 373 ? -5.460  37.092  9.250   1.00 35.05 ? 373 GLU A CD  1 
ATOM   3020 O  OE1 . GLU A 1 373 ? -5.277  37.201  8.025   1.00 36.80 ? 373 GLU A OE1 1 
ATOM   3021 O  OE2 . GLU A 1 373 ? -6.367  37.683  9.873   1.00 39.68 ? 373 GLU A OE2 1 
ATOM   3022 N  N   . PHE A 1 374 ? -1.765  32.705  9.045   1.00 16.64 ? 374 PHE A N   1 
ATOM   3023 C  CA  . PHE A 1 374 ? -0.906  31.832  8.228   1.00 16.03 ? 374 PHE A CA  1 
ATOM   3024 C  C   . PHE A 1 374 ? -1.212  32.109  6.756   1.00 17.08 ? 374 PHE A C   1 
ATOM   3025 O  O   . PHE A 1 374 ? -2.250  31.672  6.238   1.00 18.85 ? 374 PHE A O   1 
ATOM   3026 C  CB  . PHE A 1 374 ? -1.088  30.370  8.612   1.00 15.08 ? 374 PHE A CB  1 
ATOM   3027 C  CG  . PHE A 1 374 ? -0.095  29.487  7.912   1.00 16.20 ? 374 PHE A CG  1 
ATOM   3028 C  CD1 . PHE A 1 374 ? 1.191   29.398  8.390   1.00 16.06 ? 374 PHE A CD1 1 
ATOM   3029 C  CD2 . PHE A 1 374 ? -0.425  28.800  6.759   1.00 17.71 ? 374 PHE A CD2 1 
ATOM   3030 C  CE1 . PHE A 1 374 ? 2.133   28.602  7.755   1.00 16.63 ? 374 PHE A CE1 1 
ATOM   3031 C  CE2 . PHE A 1 374 ? 0.526   28.020  6.134   1.00 18.10 ? 374 PHE A CE2 1 
ATOM   3032 C  CZ  . PHE A 1 374 ? 1.793   27.950  6.616   1.00 17.88 ? 374 PHE A CZ  1 
ATOM   3033 N  N   . ARG A 1 375 ? -0.336  32.838  6.082   1.00 13.92 ? 375 ARG A N   1 
ATOM   3034 C  CA  . ARG A 1 375 ? -0.574  33.294  4.680   1.00 15.90 ? 375 ARG A CA  1 
ATOM   3035 C  C   . ARG A 1 375 ? 0.705   33.107  3.875   1.00 14.29 ? 375 ARG A C   1 
ATOM   3036 O  O   . ARG A 1 375 ? 1.563   33.990  3.829   1.00 14.48 ? 375 ARG A O   1 
ATOM   3037 C  CB  . ARG A 1 375 ? -0.977  34.769  4.693   1.00 18.73 ? 375 ARG A CB  1 
ATOM   3038 C  CG  . ARG A 1 375 ? -2.353  35.075  5.281   1.00 25.40 ? 375 ARG A CG  1 
ATOM   3039 C  CD  . ARG A 1 375 ? -2.663  36.588  5.278   1.00 32.06 ? 375 ARG A CD  1 
ATOM   3040 N  NE  . ARG A 1 375 ? -2.411  37.174  3.966   1.00 40.85 ? 375 ARG A NE  1 
ATOM   3041 C  CZ  . ARG A 1 375 ? -1.850  38.367  3.724   1.00 48.14 ? 375 ARG A CZ  1 
ATOM   3042 N  NH1 . ARG A 1 375 ? -1.501  39.191  4.701   1.00 49.49 ? 375 ARG A NH1 1 
ATOM   3043 N  NH2 . ARG A 1 375 ? -1.658  38.740  2.471   1.00 56.66 ? 375 ARG A NH2 1 
ATOM   3044 N  N   . PRO A 1 376 ? 0.890   31.947  3.216   1.00 13.72 ? 376 PRO A N   1 
ATOM   3045 C  CA  . PRO A 1 376 ? 2.110   31.704  2.443   1.00 13.88 ? 376 PRO A CA  1 
ATOM   3046 C  C   . PRO A 1 376 ? 2.371   32.735  1.338   1.00 15.61 ? 376 PRO A C   1 
ATOM   3047 O  O   . PRO A 1 376 ? 3.480   32.937  0.956   1.00 15.62 ? 376 PRO A O   1 
ATOM   3048 C  CB  . PRO A 1 376 ? 1.885   30.304  1.867   1.00 15.81 ? 376 PRO A CB  1 
ATOM   3049 C  CG  . PRO A 1 376 ? 0.977   29.643  2.862   1.00 15.84 ? 376 PRO A CG  1 
ATOM   3050 C  CD  . PRO A 1 376 ? 0.015   30.757  3.274   1.00 15.76 ? 376 PRO A CD  1 
ATOM   3051 N  N   . GLU A 1 377 ? 1.315   33.406  0.896   1.00 17.75 ? 377 GLU A N   1 
ATOM   3052 C  CA  . GLU A 1 377 ? 1.416   34.388  -0.215  1.00 18.87 ? 377 GLU A CA  1 
ATOM   3053 C  C   . GLU A 1 377 ? 2.253   35.577  0.213   1.00 18.60 ? 377 GLU A C   1 
ATOM   3054 O  O   . GLU A 1 377 ? 2.700   36.344  -0.669  1.00 19.33 ? 377 GLU A O   1 
ATOM   3055 C  CB  . GLU A 1 377 ? 0.003   34.769  -0.625  1.00 19.42 ? 377 GLU A CB  1 
ATOM   3056 C  CG  . GLU A 1 377 ? -0.792  33.596  -1.212  1.00 24.18 ? 377 GLU A CG  1 
ATOM   3057 C  CD  . GLU A 1 377 ? -1.396  32.565  -0.222  1.00 29.27 ? 377 GLU A CD  1 
ATOM   3058 O  OE1 . GLU A 1 377 ? -1.438  32.871  1.009   1.00 29.10 ? 377 GLU A OE1 1 
ATOM   3059 O  OE2 . GLU A 1 377 ? -1.889  31.458  -0.690  1.00 25.13 ? 377 GLU A OE2 1 
ATOM   3060 N  N   . ARG A 1 378 ? 2.534   35.774  1.502   1.00 16.62 ? 378 ARG A N   1 
ATOM   3061 C  CA  . ARG A 1 378 ? 3.504   36.813  1.919   1.00 17.12 ? 378 ARG A CA  1 
ATOM   3062 C  C   . ARG A 1 378 ? 4.837   36.579  1.202   1.00 18.03 ? 378 ARG A C   1 
ATOM   3063 O  O   . ARG A 1 378 ? 5.624   37.548  1.049   1.00 18.85 ? 378 ARG A O   1 
ATOM   3064 C  CB  . ARG A 1 378 ? 3.780   36.777  3.423   1.00 17.53 ? 378 ARG A CB  1 
ATOM   3065 C  CG  . ARG A 1 378 ? 2.578   37.034  4.315   1.00 18.54 ? 378 ARG A CG  1 
ATOM   3066 C  CD  . ARG A 1 378 ? 2.959   36.873  5.768   1.00 19.43 ? 378 ARG A CD  1 
ATOM   3067 N  NE  . ARG A 1 378 ? 1.815   36.595  6.615   1.00 19.22 ? 378 ARG A NE  1 
ATOM   3068 C  CZ  . ARG A 1 378 ? 1.057   37.496  7.203   1.00 20.21 ? 378 ARG A CZ  1 
ATOM   3069 N  NH1 . ARG A 1 378 ? 1.276   38.789  6.985   1.00 21.25 ? 378 ARG A NH1 1 
ATOM   3070 N  NH2 . ARG A 1 378 ? 0.055   37.116  7.963   1.00 19.93 ? 378 ARG A NH2 1 
ATOM   3071 N  N   . PHE A 1 379 ? 5.127   35.337  0.831   1.00 16.42 ? 379 PHE A N   1 
ATOM   3072 C  CA  . PHE A 1 379 ? 6.418   34.913  0.227   1.00 17.24 ? 379 PHE A CA  1 
ATOM   3073 C  C   . PHE A 1 379 ? 6.297   34.667  -1.292  1.00 19.41 ? 379 PHE A C   1 
ATOM   3074 O  O   . PHE A 1 379 ? 7.233   34.067  -1.852  1.00 22.04 ? 379 PHE A O   1 
ATOM   3075 C  CB  . PHE A 1 379 ? 6.931   33.702  1.001   1.00 17.21 ? 379 PHE A CB  1 
ATOM   3076 C  CG  . PHE A 1 379 ? 7.324   34.032  2.413   1.00 15.43 ? 379 PHE A CG  1 
ATOM   3077 C  CD1 . PHE A 1 379 ? 8.592   34.511  2.686   1.00 14.84 ? 379 PHE A CD1 1 
ATOM   3078 C  CD2 . PHE A 1 379 ? 6.440   33.861  3.502   1.00 15.48 ? 379 PHE A CD2 1 
ATOM   3079 C  CE1 . PHE A 1 379 ? 8.945   34.888  3.972   1.00 16.99 ? 379 PHE A CE1 1 
ATOM   3080 C  CE2 . PHE A 1 379 ? 6.822   34.186  4.781   1.00 17.59 ? 379 PHE A CE2 1 
ATOM   3081 C  CZ  . PHE A 1 379 ? 8.074   34.698  5.023   1.00 17.09 ? 379 PHE A CZ  1 
ATOM   3082 N  N   . GLU A 1 380 ? 5.204   35.081  -1.930  1.00 21.03 ? 380 GLU A N   1 
ATOM   3083 C  CA  . GLU A 1 380 ? 4.985   34.873  -3.396  1.00 25.13 ? 380 GLU A CA  1 
ATOM   3084 C  C   . GLU A 1 380 ? 5.988   35.688  -4.231  1.00 32.31 ? 380 GLU A C   1 
ATOM   3085 O  O   . GLU A 1 380 ? 6.429   35.139  -5.280  1.00 35.26 ? 380 GLU A O   1 
ATOM   3086 C  CB  . GLU A 1 380 ? 3.533   35.126  -3.839  1.00 27.14 ? 380 GLU A CB  1 
ATOM   3087 C  CG  . GLU A 1 380 ? 2.986   36.550  -3.671  1.00 32.98 ? 380 GLU A CG  1 
ATOM   3088 C  CD  . GLU A 1 380 ? 1.470   36.756  -3.822  1.00 34.42 ? 380 GLU A CD  1 
ATOM   3089 O  OE1 . GLU A 1 380 ? 0.697   35.771  -3.831  1.00 32.09 ? 380 GLU A OE1 1 
ATOM   3090 O  OE2 . GLU A 1 380 ? 1.056   37.921  -3.922  1.00 40.31 ? 380 GLU A OE2 1 
ATOM   3091 N  N   . ASN A 1 381 ? 6.361   36.884  -3.756  1.00 31.00 ? 381 ASN A N   1 
ATOM   3092 C  CA  . ASN A 1 381 ? 7.196   37.927  -4.446  1.00 30.10 ? 381 ASN A CA  1 
ATOM   3093 C  C   . ASN A 1 381 ? 8.264   38.350  -3.436  1.00 31.49 ? 381 ASN A C   1 
ATOM   3094 O  O   . ASN A 1 381 ? 8.239   39.453  -2.879  1.00 34.49 ? 381 ASN A O   1 
ATOM   3095 C  CB  . ASN A 1 381 ? 6.338   39.087  -4.987  1.00 26.58 ? 381 ASN A CB  1 
ATOM   3096 C  CG  . ASN A 1 381 ? 6.851   39.750  -6.249  1.00 23.50 ? 381 ASN A CG  1 
ATOM   3097 O  OD1 . ASN A 1 381 ? 7.931   39.443  -6.737  1.00 21.48 ? 381 ASN A OD1 1 
ATOM   3098 N  ND2 . ASN A 1 381 ? 6.101   40.706  -6.761  1.00 22.46 ? 381 ASN A ND2 1 
ATOM   3099 N  N   . PRO A 1 382 ? 9.223   37.432  -3.194  1.00 36.05 ? 382 PRO A N   1 
ATOM   3100 C  CA  . PRO A 1 382 ? 10.150  37.495  -2.062  1.00 39.96 ? 382 PRO A CA  1 
ATOM   3101 C  C   . PRO A 1 382 ? 11.032  38.748  -1.951  1.00 35.19 ? 382 PRO A C   1 
ATOM   3102 O  O   . PRO A 1 382 ? 11.354  39.143  -0.840  1.00 38.68 ? 382 PRO A O   1 
ATOM   3103 C  CB  . PRO A 1 382 ? 11.041  36.251  -2.250  1.00 42.12 ? 382 PRO A CB  1 
ATOM   3104 C  CG  . PRO A 1 382 ? 10.854  35.829  -3.703  1.00 41.95 ? 382 PRO A CG  1 
ATOM   3105 C  CD  . PRO A 1 382 ? 9.441   36.254  -4.047  1.00 38.21 ? 382 PRO A CD  1 
ATOM   3106 N  N   . SER A 1 383 ? 11.355  39.407  -3.072  1.00 31.46 ? 383 SER A N   1 
ATOM   3107 C  CA  . SER A 1 383 ? 12.081  40.703  -2.993  1.00 27.36 ? 383 SER A CA  1 
ATOM   3108 C  C   . SER A 1 383 ? 11.257  41.762  -2.252  1.00 25.46 ? 383 SER A C   1 
ATOM   3109 O  O   . SER A 1 383 ? 11.804  42.844  -1.952  1.00 23.89 ? 383 SER A O   1 
ATOM   3110 C  CB  . SER A 1 383 ? 12.456  41.172  -4.380  1.00 22.81 ? 383 SER A CB  1 
ATOM   3111 O  OG  . SER A 1 383 ? 13.463  40.333  -4.909  1.00 24.17 ? 383 SER A OG  1 
ATOM   3112 N  N   . ALA A 1 384 ? 9.954   41.530  -1.979  1.00 25.80 ? 384 ALA A N   1 
ATOM   3113 C  CA  . ALA A 1 384 ? 9.110   42.524  -1.266  1.00 29.24 ? 384 ALA A CA  1 
ATOM   3114 C  C   . ALA A 1 384 ? 9.453   42.616  0.240   1.00 30.44 ? 384 ALA A C   1 
ATOM   3115 O  O   . ALA A 1 384 ? 9.193   43.686  0.846   1.00 30.22 ? 384 ALA A O   1 
ATOM   3116 C  CB  . ALA A 1 384 ? 7.637   42.223  -1.481  1.00 29.40 ? 384 ALA A CB  1 
ATOM   3117 N  N   . ILE A 1 385 ? 10.130  41.618  0.799   1.00 30.43 ? 385 ILE A N   1 
ATOM   3118 C  CA  . ILE A 1 385 ? 10.431  41.574  2.270   1.00 32.18 ? 385 ILE A CA  1 
ATOM   3119 C  C   . ILE A 1 385 ? 11.592  42.505  2.587   1.00 29.54 ? 385 ILE A C   1 
ATOM   3120 O  O   . ILE A 1 385 ? 12.635  42.359  1.962   1.00 28.95 ? 385 ILE A O   1 
ATOM   3121 C  CB  . ILE A 1 385 ? 10.718  40.120  2.666   1.00 33.79 ? 385 ILE A CB  1 
ATOM   3122 C  CG1 . ILE A 1 385 ? 9.507   39.228  2.371   1.00 35.40 ? 385 ILE A CG1 1 
ATOM   3123 C  CG2 . ILE A 1 385 ? 11.141  40.034  4.130   1.00 34.46 ? 385 ILE A CG2 1 
ATOM   3124 C  CD1 . ILE A 1 385 ? 9.864   37.803  2.066   1.00 35.12 ? 385 ILE A CD1 1 
ATOM   3125 N  N   . PRO A 1 386 ? 11.494  43.473  3.525   1.00 27.21 ? 386 PRO A N   1 
ATOM   3126 C  CA  . PRO A 1 386 ? 12.624  44.361  3.793   1.00 29.85 ? 386 PRO A CA  1 
ATOM   3127 C  C   . PRO A 1 386 ? 13.846  43.534  4.221   1.00 27.63 ? 386 PRO A C   1 
ATOM   3128 O  O   . PRO A 1 386 ? 13.693  42.392  4.693   1.00 25.43 ? 386 PRO A O   1 
ATOM   3129 C  CB  . PRO A 1 386 ? 12.109  45.343  4.851   1.00 30.87 ? 386 PRO A CB  1 
ATOM   3130 C  CG  . PRO A 1 386 ? 10.593  45.300  4.651   1.00 31.55 ? 386 PRO A CG  1 
ATOM   3131 C  CD  . PRO A 1 386 ? 10.269  43.884  4.246   1.00 27.22 ? 386 PRO A CD  1 
ATOM   3132 N  N   . GLN A 1 387 ? 15.016  44.122  4.016   1.00 28.51 ? 387 GLN A N   1 
ATOM   3133 C  CA  . GLN A 1 387 ? 16.297  43.603  4.528   1.00 28.00 ? 387 GLN A CA  1 
ATOM   3134 C  C   . GLN A 1 387 ? 16.163  43.353  6.033   1.00 26.38 ? 387 GLN A C   1 
ATOM   3135 O  O   . GLN A 1 387 ? 15.683  44.227  6.762   1.00 25.97 ? 387 GLN A O   1 
ATOM   3136 C  CB  . GLN A 1 387 ? 17.419  44.608  4.220   1.00 33.16 ? 387 GLN A CB  1 
ATOM   3137 C  CG  . GLN A 1 387 ? 17.581  44.902  2.730   1.00 36.90 ? 387 GLN A CG  1 
ATOM   3138 C  CD  . GLN A 1 387 ? 18.012  43.676  1.963   1.00 38.87 ? 387 GLN A CD  1 
ATOM   3139 O  OE1 . GLN A 1 387 ? 17.234  43.067  1.224   1.00 40.60 ? 387 GLN A OE1 1 
ATOM   3140 N  NE2 . GLN A 1 387 ? 19.274  43.300  2.124   1.00 38.78 ? 387 GLN A NE2 1 
ATOM   3141 N  N   . HIS A 1 388 ? 16.542  42.176  6.490   1.00 22.09 ? 388 HIS A N   1 
ATOM   3142 C  CA  . HIS A 1 388 ? 16.694  41.837  7.925   1.00 21.88 ? 388 HIS A CA  1 
ATOM   3143 C  C   . HIS A 1 388 ? 15.326  41.717  8.609   1.00 20.00 ? 388 HIS A C   1 
ATOM   3144 O  O   . HIS A 1 388 ? 15.283  41.613  9.797   1.00 19.22 ? 388 HIS A O   1 
ATOM   3145 C  CB  . HIS A 1 388 ? 17.627  42.842  8.626   1.00 24.95 ? 388 HIS A CB  1 
ATOM   3146 C  CG  . HIS A 1 388 ? 19.020  42.808  8.102   1.00 24.16 ? 388 HIS A CG  1 
ATOM   3147 N  ND1 . HIS A 1 388 ? 19.732  41.638  8.020   1.00 28.15 ? 388 HIS A ND1 1 
ATOM   3148 C  CD2 . HIS A 1 388 ? 19.793  43.765  7.531   1.00 31.31 ? 388 HIS A CD2 1 
ATOM   3149 C  CE1 . HIS A 1 388 ? 20.917  41.880  7.497   1.00 31.38 ? 388 HIS A CE1 1 
ATOM   3150 N  NE2 . HIS A 1 388 ? 20.980  43.169  7.199   1.00 31.02 ? 388 HIS A NE2 1 
ATOM   3151 N  N   . ALA A 1 389 ? 14.235  41.586  7.893   1.00 17.86 ? 389 ALA A N   1 
ATOM   3152 C  CA  . ALA A 1 389 ? 12.903  41.360  8.463   1.00 16.91 ? 389 ALA A CA  1 
ATOM   3153 C  C   . ALA A 1 389 ? 12.633  39.869  8.727   1.00 15.02 ? 389 ALA A C   1 
ATOM   3154 O  O   . ALA A 1 389 ? 11.766  39.533  9.503   1.00 15.45 ? 389 ALA A O   1 
ATOM   3155 C  CB  . ALA A 1 389 ? 11.883  41.903  7.510   1.00 19.14 ? 389 ALA A CB  1 
ATOM   3156 N  N   . PHE A 1 390 ? 13.332  38.965  8.045   1.00 13.92 ? 390 PHE A N   1 
ATOM   3157 C  CA  . PHE A 1 390 ? 12.971  37.512  8.084   1.00 13.83 ? 390 PHE A CA  1 
ATOM   3158 C  C   . PHE A 1 390 ? 14.280  36.748  8.281   1.00 14.38 ? 390 PHE A C   1 
ATOM   3159 O  O   . PHE A 1 390 ? 15.179  36.763  7.367   1.00 16.85 ? 390 PHE A O   1 
ATOM   3160 C  CB  . PHE A 1 390 ? 12.279  37.095  6.779   1.00 12.22 ? 390 PHE A CB  1 
ATOM   3161 C  CG  . PHE A 1 390 ? 11.906  35.630  6.678   1.00 12.00 ? 390 PHE A CG  1 
ATOM   3162 C  CD1 . PHE A 1 390 ? 10.975  35.081  7.536   1.00 13.78 ? 390 PHE A CD1 1 
ATOM   3163 C  CD2 . PHE A 1 390 ? 12.440  34.828  5.706   1.00 12.96 ? 390 PHE A CD2 1 
ATOM   3164 C  CE1 . PHE A 1 390 ? 10.592  33.760  7.420   1.00 13.16 ? 390 PHE A CE1 1 
ATOM   3165 C  CE2 . PHE A 1 390 ? 12.065  33.493  5.594   1.00 13.59 ? 390 PHE A CE2 1 
ATOM   3166 C  CZ  . PHE A 1 390 ? 11.126  32.976  6.447   1.00 12.16 ? 390 PHE A CZ  1 
ATOM   3167 N  N   . LYS A 1 391 ? 14.511  36.194  9.477   1.00 12.88 ? 391 LYS A N   1 
ATOM   3168 C  CA  . LYS A 1 391 ? 15.858  35.709  9.827   1.00 12.72 ? 391 LYS A CA  1 
ATOM   3169 C  C   . LYS A 1 391 ? 15.780  34.347  10.500  1.00 11.04 ? 391 LYS A C   1 
ATOM   3170 O  O   . LYS A 1 391 ? 16.447  34.114  11.522  1.00 12.32 ? 391 LYS A O   1 
ATOM   3171 C  CB  . LYS A 1 391 ? 16.545  36.688  10.775  1.00 15.59 ? 391 LYS A CB  1 
ATOM   3172 C  CG  . LYS A 1 391 ? 16.722  38.071  10.177  1.00 18.20 ? 391 LYS A CG  1 
ATOM   3173 C  CD  . LYS A 1 391 ? 17.629  38.130  9.039   1.00 26.08 ? 391 LYS A CD  1 
ATOM   3174 C  CE  . LYS A 1 391 ? 19.062  38.190  9.485   1.00 27.62 ? 391 LYS A CE  1 
ATOM   3175 N  NZ  . LYS A 1 391 ? 19.846  38.767  8.379   1.00 30.08 ? 391 LYS A NZ  1 
ATOM   3176 N  N   . PRO A 1 392 ? 15.014  33.371  9.972   1.00 10.80 ? 392 PRO A N   1 
ATOM   3177 C  CA  . PRO A 1 392 ? 14.932  32.066  10.622  1.00 10.91 ? 392 PRO A CA  1 
ATOM   3178 C  C   . PRO A 1 392 ? 16.250  31.267  10.561  1.00 11.39 ? 392 PRO A C   1 
ATOM   3179 O  O   . PRO A 1 392 ? 16.375  30.331  11.331  1.00 11.32 ? 392 PRO A O   1 
ATOM   3180 C  CB  . PRO A 1 392 ? 13.847  31.336  9.823   1.00 11.98 ? 392 PRO A CB  1 
ATOM   3181 C  CG  . PRO A 1 392 ? 13.966  31.923  8.431   1.00 11.83 ? 392 PRO A CG  1 
ATOM   3182 C  CD  . PRO A 1 392 ? 14.267  33.362  8.702   1.00 12.42 ? 392 PRO A CD  1 
ATOM   3183 N  N   . PHE A 1 393 ? 17.176  31.652  9.681   1.00 10.59 ? 393 PHE A N   1 
ATOM   3184 C  CA  . PHE A 1 393 ? 18.509  30.985  9.551   1.00 11.09 ? 393 PHE A CA  1 
ATOM   3185 C  C   . PHE A 1 393 ? 19.631  31.876  10.049  1.00 10.80 ? 393 PHE A C   1 
ATOM   3186 O  O   . PHE A 1 393 ? 20.814  31.596  9.805   1.00 11.82 ? 393 PHE A O   1 
ATOM   3187 C  CB  . PHE A 1 393 ? 18.739  30.542  8.101   1.00 10.99 ? 393 PHE A CB  1 
ATOM   3188 C  CG  . PHE A 1 393 ? 17.776  29.450  7.678   1.00 10.60 ? 393 PHE A CG  1 
ATOM   3189 C  CD1 . PHE A 1 393 ? 17.891  28.150  8.120   1.00 10.95 ? 393 PHE A CD1 1 
ATOM   3190 C  CD2 . PHE A 1 393 ? 16.705  29.749  6.836   1.00 11.07 ? 393 PHE A CD2 1 
ATOM   3191 C  CE1 . PHE A 1 393 ? 17.013  27.157  7.733   1.00 12.54 ? 393 PHE A CE1 1 
ATOM   3192 C  CE2 . PHE A 1 393 ? 15.783  28.770  6.454   1.00 12.36 ? 393 PHE A CE2 1 
ATOM   3193 C  CZ  . PHE A 1 393 ? 15.932  27.472  6.919   1.00 12.37 ? 393 PHE A CZ  1 
ATOM   3194 N  N   . GLY A 1 394 ? 19.301  32.870  10.859  1.00 10.63 ? 394 GLY A N   1 
ATOM   3195 C  CA  . GLY A 1 394 ? 20.375  33.676  11.456  1.00 11.27 ? 394 GLY A CA  1 
ATOM   3196 C  C   . GLY A 1 394 ? 20.865  34.767  10.524  1.00 12.03 ? 394 GLY A C   1 
ATOM   3197 O  O   . GLY A 1 394 ? 20.155  35.152  9.641   1.00 12.76 ? 394 GLY A O   1 
ATOM   3198 N  N   . ASN A 1 395 ? 22.105  35.177  10.742  1.00 11.49 ? 395 ASN A N   1 
ATOM   3199 C  CA  . ASN A 1 395 ? 22.620  36.377  10.066  1.00 12.12 ? 395 ASN A CA  1 
ATOM   3200 C  C   . ASN A 1 395 ? 24.058  36.243  9.569   1.00 13.03 ? 395 ASN A C   1 
ATOM   3201 O  O   . ASN A 1 395 ? 24.916  35.775  10.302  1.00 11.77 ? 395 ASN A O   1 
ATOM   3202 C  CB  . ASN A 1 395 ? 22.578  37.581  10.989  1.00 12.61 ? 395 ASN A CB  1 
ATOM   3203 C  CG  . ASN A 1 395 ? 22.983  38.852  10.261  1.00 13.48 ? 395 ASN A CG  1 
ATOM   3204 O  OD1 . ASN A 1 395 ? 22.286  39.264  9.347   1.00 15.58 ? 395 ASN A OD1 1 
ATOM   3205 N  ND2 . ASN A 1 395 ? 24.106  39.407  10.670  1.00 14.72 ? 395 ASN A ND2 1 
ATOM   3206 N  N   . GLY A 1 396 ? 24.287  36.735  8.364   1.00 13.26 ? 396 GLY A N   1 
ATOM   3207 C  CA  . GLY A 1 396 ? 25.626  36.980  7.815   1.00 14.39 ? 396 GLY A CA  1 
ATOM   3208 C  C   . GLY A 1 396 ? 26.491  35.749  7.744   1.00 13.89 ? 396 GLY A C   1 
ATOM   3209 O  O   . GLY A 1 396 ? 25.993  34.664  7.387   1.00 13.21 ? 396 GLY A O   1 
ATOM   3210 N  N   . GLN A 1 397 ? 27.772  35.914  8.045   1.00 12.76 ? 397 GLN A N   1 
ATOM   3211 C  CA  . GLN A 1 397 ? 28.700  34.781  7.864   1.00 12.69 ? 397 GLN A CA  1 
ATOM   3212 C  C   . GLN A 1 397 ? 28.430  33.714  8.907   1.00 12.63 ? 397 GLN A C   1 
ATOM   3213 O  O   . GLN A 1 397 ? 28.872  32.589  8.688   1.00 13.75 ? 397 GLN A O   1 
ATOM   3214 C  CB  . GLN A 1 397 ? 30.158  35.236  7.895   1.00 14.02 ? 397 GLN A CB  1 
ATOM   3215 C  CG  . GLN A 1 397 ? 30.617  35.723  9.242   1.00 14.13 ? 397 GLN A CG  1 
ATOM   3216 C  CD  . GLN A 1 397 ? 32.012  36.314  9.181   1.00 16.99 ? 397 GLN A CD  1 
ATOM   3217 O  OE1 . GLN A 1 397 ? 32.823  35.947  8.304   1.00 19.15 ? 397 GLN A OE1 1 
ATOM   3218 N  NE2 . GLN A 1 397 ? 32.262  37.179  10.150  1.00 17.50 ? 397 GLN A NE2 1 
ATOM   3219 N  N   . ARG A 1 398 ? 27.696  34.040  9.978   1.00 12.15 ? 398 ARG A N   1 
ATOM   3220 C  CA  . ARG A 1 398 ? 27.334  33.047  11.018  1.00 11.31 ? 398 ARG A CA  1 
ATOM   3221 C  C   . ARG A 1 398 ? 25.895  32.570  10.825  1.00 11.27 ? 398 ARG A C   1 
ATOM   3222 O  O   . ARG A 1 398 ? 25.318  31.968  11.747  1.00 12.42 ? 398 ARG A O   1 
ATOM   3223 C  CB  . ARG A 1 398 ? 27.590  33.659  12.398  1.00 11.07 ? 398 ARG A CB  1 
ATOM   3224 C  CG  . ARG A 1 398 ? 29.037  34.052  12.600  1.00 11.20 ? 398 ARG A CG  1 
ATOM   3225 C  CD  . ARG A 1 398 ? 30.009  32.902  12.465  1.00 10.54 ? 398 ARG A CD  1 
ATOM   3226 N  NE  . ARG A 1 398 ? 29.746  31.707  13.221  1.00 11.03 ? 398 ARG A NE  1 
ATOM   3227 C  CZ  . ARG A 1 398 ? 30.176  31.409  14.448  1.00 11.89 ? 398 ARG A CZ  1 
ATOM   3228 N  NH1 . ARG A 1 398 ? 30.915  32.266  15.147  1.00 11.77 ? 398 ARG A NH1 1 
ATOM   3229 N  NH2 . ARG A 1 398 ? 29.826  30.258  14.996  1.00 10.86 ? 398 ARG A NH2 1 
ATOM   3230 N  N   . ALA A 1 399 ? 25.346  32.729  9.631   1.00 10.60 ? 399 ALA A N   1 
ATOM   3231 C  CA  . ALA A 1 399 ? 24.046  32.131  9.303   1.00 10.24 ? 399 ALA A CA  1 
ATOM   3232 C  C   . ALA A 1 399 ? 24.161  30.603  9.187   1.00 9.86  ? 399 ALA A C   1 
ATOM   3233 O  O   . ALA A 1 399 ? 25.246  30.059  9.029   1.00 11.66 ? 399 ALA A O   1 
ATOM   3234 C  CB  . ALA A 1 399 ? 23.463  32.699  8.036   1.00 10.98 ? 399 ALA A CB  1 
ATOM   3235 N  N   . CYS A 1 400 ? 23.034  29.942  9.297   1.00 11.06 ? 400 CYS A N   1 
ATOM   3236 C  CA  . CYS A 1 400 ? 22.923  28.483  9.153   1.00 11.18 ? 400 CYS A CA  1 
ATOM   3237 C  C   . CYS A 1 400 ? 23.677  28.002  7.916   1.00 11.13 ? 400 CYS A C   1 
ATOM   3238 O  O   . CYS A 1 400 ? 23.236  28.283  6.791   1.00 12.30 ? 400 CYS A O   1 
ATOM   3239 C  CB  . CYS A 1 400 ? 21.460  28.112  9.029   1.00 12.78 ? 400 CYS A CB  1 
ATOM   3240 S  SG  . CYS A 1 400 ? 21.241  26.318  9.028   1.00 12.59 ? 400 CYS A SG  1 
ATOM   3241 N  N   . ILE A 1 401 ? 24.632  27.138  8.077   1.00 11.38 ? 401 ILE A N   1 
ATOM   3242 C  CA  . ILE A 1 401 ? 25.271  26.472  6.901   1.00 10.69 ? 401 ILE A CA  1 
ATOM   3243 C  C   . ILE A 1 401 ? 24.340  25.444  6.288   1.00 11.04 ? 401 ILE A C   1 
ATOM   3244 O  O   . ILE A 1 401 ? 24.497  25.128  5.046   1.00 12.67 ? 401 ILE A O   1 
ATOM   3245 C  CB  . ILE A 1 401 ? 26.647  25.880  7.269   1.00 11.77 ? 401 ILE A CB  1 
ATOM   3246 C  CG1 . ILE A 1 401 ? 27.539  25.796  6.015   1.00 12.33 ? 401 ILE A CG1 1 
ATOM   3247 C  CG2 . ILE A 1 401 ? 26.500  24.564  7.988   1.00 12.59 ? 401 ILE A CG2 1 
ATOM   3248 C  CD1 . ILE A 1 401 ? 28.969  25.355  6.312   1.00 13.07 ? 401 ILE A CD1 1 
ATOM   3249 N  N   . GLY A 1 402 ? 23.405  24.903  7.052   1.00 11.05 ? 402 GLY A N   1 
ATOM   3250 C  CA  . GLY A 1 402 ? 22.478  23.849  6.620   1.00 10.24 ? 402 GLY A CA  1 
ATOM   3251 C  C   . GLY A 1 402 ? 21.228  24.364  5.953   1.00 11.22 ? 402 GLY A C   1 
ATOM   3252 O  O   . GLY A 1 402 ? 20.371  23.549  5.658   1.00 12.52 ? 402 GLY A O   1 
ATOM   3253 N  N   . GLN A 1 403 ? 21.107  25.648  5.644   1.00 11.11 ? 403 GLN A N   1 
ATOM   3254 C  CA  . GLN A 1 403 ? 19.810  26.196  5.153   1.00 11.11 ? 403 GLN A CA  1 
ATOM   3255 C  C   . GLN A 1 403 ? 19.324  25.498  3.871   1.00 11.83 ? 403 GLN A C   1 
ATOM   3256 O  O   . GLN A 1 403 ? 18.165  25.130  3.801   1.00 11.83 ? 403 GLN A O   1 
ATOM   3257 C  CB  . GLN A 1 403 ? 19.944  27.708  4.924   1.00 13.03 ? 403 GLN A CB  1 
ATOM   3258 C  CG  . GLN A 1 403 ? 18.761  28.302  4.215   1.00 15.66 ? 403 GLN A CG  1 
ATOM   3259 C  CD  . GLN A 1 403 ? 18.840  29.800  4.109   1.00 17.81 ? 403 GLN A CD  1 
ATOM   3260 O  OE1 . GLN A 1 403 ? 19.595  30.491  4.787   1.00 16.79 ? 403 GLN A OE1 1 
ATOM   3261 N  NE2 . GLN A 1 403 ? 17.982  30.312  3.263   1.00 20.40 ? 403 GLN A NE2 1 
ATOM   3262 N  N   A GLN A 1 404 ? 20.208  25.278  2.887   0.50 11.82 ? 404 GLN A N   1 
ATOM   3263 N  N   B GLN A 1 404 ? 20.215  25.305  2.879   0.50 11.80 ? 404 GLN A N   1 
ATOM   3264 C  CA  A GLN A 1 404 ? 19.779  24.666  1.600   0.50 12.01 ? 404 GLN A CA  1 
ATOM   3265 C  CA  B GLN A 1 404 ? 19.830  24.654  1.593   0.50 12.00 ? 404 GLN A CA  1 
ATOM   3266 C  C   A GLN A 1 404 ? 19.481  23.176  1.793   0.50 12.21 ? 404 GLN A C   1 
ATOM   3267 C  C   B GLN A 1 404 ? 19.438  23.201  1.850   0.50 12.14 ? 404 GLN A C   1 
ATOM   3268 O  O   A GLN A 1 404 ? 18.555  22.668  1.157   0.50 12.86 ? 404 GLN A O   1 
ATOM   3269 O  O   B GLN A 1 404 ? 18.415  22.757  1.326   0.50 12.03 ? 404 GLN A O   1 
ATOM   3270 C  CB  A GLN A 1 404 ? 20.857  24.853  0.530   0.50 13.51 ? 404 GLN A CB  1 
ATOM   3271 C  CB  B GLN A 1 404 ? 20.973  24.627  0.569   0.50 13.58 ? 404 GLN A CB  1 
ATOM   3272 C  CG  A GLN A 1 404 ? 21.060  26.284  0.078   0.50 15.77 ? 404 GLN A CG  1 
ATOM   3273 C  CG  B GLN A 1 404 ? 21.700  25.941  0.358   0.50 15.60 ? 404 GLN A CG  1 
ATOM   3274 C  CD  A GLN A 1 404 ? 21.865  27.076  1.073   0.50 17.96 ? 404 GLN A CD  1 
ATOM   3275 C  CD  B GLN A 1 404 ? 20.763  27.053  -0.015  0.50 16.74 ? 404 GLN A CD  1 
ATOM   3276 O  OE1 A GLN A 1 404 ? 22.827  26.597  1.690   0.50 23.14 ? 404 GLN A OE1 1 
ATOM   3277 O  OE1 B GLN A 1 404 ? 19.814  26.882  -0.776  0.50 19.26 ? 404 GLN A OE1 1 
ATOM   3278 N  NE2 A GLN A 1 404 ? 21.433  28.305  1.266   0.50 21.47 ? 404 GLN A NE2 1 
ATOM   3279 N  NE2 B GLN A 1 404 ? 21.007  28.201  0.584   0.50 18.17 ? 404 GLN A NE2 1 
ATOM   3280 N  N   . PHE A 1 405 ? 20.199  22.508  2.691   1.00 11.34 ? 405 PHE A N   1 
ATOM   3281 C  CA  . PHE A 1 405 ? 19.937  21.096  3.040   1.00 11.11 ? 405 PHE A CA  1 
ATOM   3282 C  C   . PHE A 1 405 ? 18.571  20.984  3.695   1.00 12.30 ? 405 PHE A C   1 
ATOM   3283 O  O   . PHE A 1 405 ? 17.748  20.169  3.295   1.00 12.39 ? 405 PHE A O   1 
ATOM   3284 C  CB  . PHE A 1 405 ? 21.048  20.606  3.968   1.00 13.47 ? 405 PHE A CB  1 
ATOM   3285 C  CG  . PHE A 1 405 ? 21.045  19.130  4.261   1.00 14.11 ? 405 PHE A CG  1 
ATOM   3286 C  CD1 . PHE A 1 405 ? 20.193  18.599  5.205   1.00 15.44 ? 405 PHE A CD1 1 
ATOM   3287 C  CD2 . PHE A 1 405 ? 21.885  18.269  3.573   1.00 15.52 ? 405 PHE A CD2 1 
ATOM   3288 C  CE1 . PHE A 1 405 ? 20.224  17.251  5.503   1.00 15.44 ? 405 PHE A CE1 1 
ATOM   3289 C  CE2 . PHE A 1 405 ? 21.893  16.922  3.849   1.00 15.53 ? 405 PHE A CE2 1 
ATOM   3290 C  CZ  . PHE A 1 405 ? 21.066  16.404  4.813   1.00 15.65 ? 405 PHE A CZ  1 
ATOM   3291 N  N   . ALA A 1 406 ? 18.342  21.805  4.736   1.00 11.90 ? 406 ALA A N   1 
ATOM   3292 C  CA  . ALA A 1 406 ? 17.068  21.731  5.494   1.00 12.56 ? 406 ALA A CA  1 
ATOM   3293 C  C   . ALA A 1 406 ? 15.909  22.008  4.543   1.00 11.06 ? 406 ALA A C   1 
ATOM   3294 O  O   . ALA A 1 406 ? 14.886  21.295  4.609   1.00 12.40 ? 406 ALA A O   1 
ATOM   3295 C  CB  . ALA A 1 406 ? 17.099  22.713  6.653   1.00 12.28 ? 406 ALA A CB  1 
ATOM   3296 N  N   . LEU A 1 407 ? 15.984  23.057  3.733   1.00 11.78 ? 407 LEU A N   1 
ATOM   3297 C  CA  . LEU A 1 407 ? 14.830  23.386  2.859   1.00 11.48 ? 407 LEU A CA  1 
ATOM   3298 C  C   . LEU A 1 407 ? 14.676  22.352  1.740   1.00 13.06 ? 407 LEU A C   1 
ATOM   3299 O  O   . LEU A 1 407 ? 13.507  22.108  1.365   1.00 12.20 ? 407 LEU A O   1 
ATOM   3300 C  CB  . LEU A 1 407 ? 14.974  24.807  2.305   1.00 13.09 ? 407 LEU A CB  1 
ATOM   3301 C  CG  . LEU A 1 407 ? 14.846  25.913  3.351   1.00 13.72 ? 407 LEU A CG  1 
ATOM   3302 C  CD1 . LEU A 1 407 ? 15.140  27.265  2.741   1.00 16.99 ? 407 LEU A CD1 1 
ATOM   3303 C  CD2 . LEU A 1 407 ? 13.484  25.915  4.058   1.00 16.30 ? 407 LEU A CD2 1 
ATOM   3304 N  N   . HIS A 1 408 ? 15.738  21.739  1.228   1.00 11.27 ? 408 HIS A N   1 
ATOM   3305 C  CA  . HIS A 1 408 ? 15.552  20.705  0.186   1.00 12.56 ? 408 HIS A CA  1 
ATOM   3306 C  C   . HIS A 1 408 ? 14.834  19.529  0.825   1.00 11.94 ? 408 HIS A C   1 
ATOM   3307 O  O   . HIS A 1 408 ? 13.851  19.027  0.275   1.00 12.79 ? 408 HIS A O   1 
ATOM   3308 C  CB  . HIS A 1 408 ? 16.885  20.317  -0.451  1.00 11.54 ? 408 HIS A CB  1 
ATOM   3309 C  CG  . HIS A 1 408 ? 16.695  19.485  -1.662  1.00 13.23 ? 408 HIS A CG  1 
ATOM   3310 N  ND1 . HIS A 1 408 ? 16.355  20.047  -2.867  1.00 14.64 ? 408 HIS A ND1 1 
ATOM   3311 C  CD2 . HIS A 1 408 ? 16.761  18.146  -1.813  1.00 12.80 ? 408 HIS A CD2 1 
ATOM   3312 C  CE1 . HIS A 1 408 ? 16.212  19.049  -3.736  1.00 13.97 ? 408 HIS A CE1 1 
ATOM   3313 N  NE2 . HIS A 1 408 ? 16.437  17.876  -3.119  1.00 13.64 ? 408 HIS A NE2 1 
ATOM   3314 N  N   . GLU A 1 409 ? 15.343  19.031  1.937   1.00 11.34 ? 409 GLU A N   1 
ATOM   3315 C  CA  . GLU A 1 409 ? 14.724  17.890  2.622   1.00 12.36 ? 409 GLU A CA  1 
ATOM   3316 C  C   . GLU A 1 409 ? 13.262  18.249  2.926   1.00 12.01 ? 409 GLU A C   1 
ATOM   3317 O  O   . GLU A 1 409 ? 12.370  17.423  2.681   1.00 12.76 ? 409 GLU A O   1 
ATOM   3318 C  CB  . GLU A 1 409 ? 15.444  17.584  3.946   1.00 15.33 ? 409 GLU A CB  1 
ATOM   3319 C  CG  . GLU A 1 409 ? 14.844  16.384  4.645   1.00 18.16 ? 409 GLU A CG  1 
ATOM   3320 C  CD  . GLU A 1 409 ? 15.468  15.931  5.924   1.00 24.10 ? 409 GLU A CD  1 
ATOM   3321 O  OE1 . GLU A 1 409 ? 16.275  16.702  6.495   1.00 25.54 ? 409 GLU A OE1 1 
ATOM   3322 O  OE2 . GLU A 1 409 ? 15.126  14.781  6.314   1.00 28.98 ? 409 GLU A OE2 1 
ATOM   3323 N  N   . ALA A 1 410 ? 12.986  19.399  3.542   1.00 11.20 ? 410 ALA A N   1 
ATOM   3324 C  CA  . ALA A 1 410 ? 11.621  19.723  4.002   1.00 11.03 ? 410 ALA A CA  1 
ATOM   3325 C  C   . ALA A 1 410 ? 10.681  19.813  2.807   1.00 11.57 ? 410 ALA A C   1 
ATOM   3326 O  O   . ALA A 1 410 ? 9.509   19.444  2.917   1.00 12.39 ? 410 ALA A O   1 
ATOM   3327 C  CB  . ALA A 1 410 ? 11.617  20.994  4.819   1.00 10.55 ? 410 ALA A CB  1 
ATOM   3328 N  N   . THR A 1 411 ? 11.163  20.359  1.692   1.00 11.87 ? 411 THR A N   1 
ATOM   3329 C  CA  . THR A 1 411 ? 10.299  20.545  0.519   1.00 11.49 ? 411 THR A CA  1 
ATOM   3330 C  C   . THR A 1 411 ? 10.005  19.174  -0.096  1.00 11.91 ? 411 THR A C   1 
ATOM   3331 O  O   . THR A 1 411 ? 8.873   18.880  -0.490  1.00 11.79 ? 411 THR A O   1 
ATOM   3332 C  CB  . THR A 1 411 ? 10.968  21.484  -0.473  1.00 11.06 ? 411 THR A CB  1 
ATOM   3333 O  OG1 . THR A 1 411 ? 11.251  22.750  0.114   1.00 13.42 ? 411 THR A OG1 1 
ATOM   3334 C  CG2 . THR A 1 411 ? 10.076  21.709  -1.671  1.00 12.83 ? 411 THR A CG2 1 
ATOM   3335 N  N   . LEU A 1 412 ? 11.013  18.337  -0.200  1.00 11.23 ? 412 LEU A N   1 
ATOM   3336 C  CA  . LEU A 1 412 ? 10.861  16.967  -0.733  1.00 11.45 ? 412 LEU A CA  1 
ATOM   3337 C  C   . LEU A 1 412 ? 9.826   16.226  0.089   1.00 11.83 ? 412 LEU A C   1 
ATOM   3338 O  O   . LEU A 1 412 ? 8.892   15.629  -0.430  1.00 12.37 ? 412 LEU A O   1 
ATOM   3339 C  CB  . LEU A 1 412 ? 12.214  16.283  -0.712  1.00 13.45 ? 412 LEU A CB  1 
ATOM   3340 C  CG  . LEU A 1 412 ? 12.157  14.783  -0.933  1.00 15.04 ? 412 LEU A CG  1 
ATOM   3341 C  CD1 . LEU A 1 412 ? 11.695  14.475  -2.343  1.00 15.42 ? 412 LEU A CD1 1 
ATOM   3342 C  CD2 . LEU A 1 412 ? 13.533  14.194  -0.673  1.00 17.89 ? 412 LEU A CD2 1 
ATOM   3343 N  N   . VAL A 1 413 ? 10.000  16.217  1.390   1.00 12.81 ? 413 VAL A N   1 
ATOM   3344 C  CA  . VAL A 1 413 ? 9.158   15.384  2.275   1.00 13.93 ? 413 VAL A CA  1 
ATOM   3345 C  C   . VAL A 1 413 ? 7.740   15.934  2.314   1.00 12.41 ? 413 VAL A C   1 
ATOM   3346 O  O   . VAL A 1 413 ? 6.792   15.138  2.257   1.00 12.44 ? 413 VAL A O   1 
ATOM   3347 C  CB  . VAL A 1 413 ? 9.810   15.365  3.670   1.00 15.40 ? 413 VAL A CB  1 
ATOM   3348 C  CG1 . VAL A 1 413 ? 8.863   14.812  4.720   1.00 17.02 ? 413 VAL A CG1 1 
ATOM   3349 C  CG2 . VAL A 1 413 ? 11.146  14.635  3.582   1.00 17.09 ? 413 VAL A CG2 1 
ATOM   3350 N  N   . LEU A 1 414 ? 7.592   17.235  2.479   1.00 11.73 ? 414 LEU A N   1 
ATOM   3351 C  CA  . LEU A 1 414 ? 6.234   17.799  2.545   1.00 12.14 ? 414 LEU A CA  1 
ATOM   3352 C  C   . LEU A 1 414 ? 5.547   17.582  1.195   1.00 11.68 ? 414 LEU A C   1 
ATOM   3353 O  O   . LEU A 1 414 ? 4.347   17.210  1.191   1.00 12.04 ? 414 LEU A O   1 
ATOM   3354 C  CB  . LEU A 1 414 ? 6.283   19.245  3.008   1.00 12.90 ? 414 LEU A CB  1 
ATOM   3355 C  CG  . LEU A 1 414 ? 4.933   19.907  3.199   1.00 14.72 ? 414 LEU A CG  1 
ATOM   3356 C  CD1 . LEU A 1 414 ? 4.075   19.129  4.201   1.00 16.95 ? 414 LEU A CD1 1 
ATOM   3357 C  CD2 . LEU A 1 414 ? 5.130   21.333  3.671   1.00 17.15 ? 414 LEU A CD2 1 
ATOM   3358 N  N   . GLY A 1 415 ? 6.291   17.727  0.082   1.00 12.05 ? 415 GLY A N   1 
ATOM   3359 C  CA  . GLY A 1 415 ? 5.683   17.468  -1.225  1.00 13.09 ? 415 GLY A CA  1 
ATOM   3360 C  C   . GLY A 1 415 ? 5.202   16.020  -1.298  1.00 12.36 ? 415 GLY A C   1 
ATOM   3361 O  O   . GLY A 1 415 ? 4.104   15.731  -1.812  1.00 12.31 ? 415 GLY A O   1 
ATOM   3362 N  N   . MET A 1 416 ? 6.022   15.053  -0.891  1.00 12.04 ? 416 MET A N   1 
ATOM   3363 C  CA  . MET A 1 416 ? 5.626   13.638  -0.956  1.00 12.42 ? 416 MET A CA  1 
ATOM   3364 C  C   . MET A 1 416 ? 4.454   13.367  -0.019  1.00 12.61 ? 416 MET A C   1 
ATOM   3365 O  O   . MET A 1 416 ? 3.516   12.618  -0.395  1.00 13.08 ? 416 MET A O   1 
ATOM   3366 C  CB  . MET A 1 416 ? 6.786   12.684  -0.647  1.00 14.29 ? 416 MET A CB  1 
ATOM   3367 C  CG  . MET A 1 416 ? 7.844   12.735  -1.712  1.00 14.17 ? 416 MET A CG  1 
ATOM   3368 S  SD  . MET A 1 416 ? 9.241   11.578  -1.381  1.00 18.87 ? 416 MET A SD  1 
ATOM   3369 C  CE  . MET A 1 416 ? 8.442   10.020  -1.682  1.00 22.20 ? 416 MET A CE  1 
ATOM   3370 N  N   . MET A 1 417 ? 4.428   13.964  1.175   1.00 11.32 ? 417 MET A N   1 
ATOM   3371 C  CA  . MET A 1 417 ? 3.317   13.742  2.130   1.00 12.62 ? 417 MET A CA  1 
ATOM   3372 C  C   . MET A 1 417 ? 2.019   14.239  1.482   1.00 12.36 ? 417 MET A C   1 
ATOM   3373 O  O   . MET A 1 417 ? 1.023   13.532  1.591   1.00 13.20 ? 417 MET A O   1 
ATOM   3374 C  CB  . MET A 1 417 ? 3.573   14.482  3.436   1.00 13.02 ? 417 MET A CB  1 
ATOM   3375 C  CG  . MET A 1 417 ? 4.711   13.885  4.274   1.00 14.17 ? 417 MET A CG  1 
ATOM   3376 S  SD  . MET A 1 417 ? 5.222   15.005  5.623   1.00 19.29 ? 417 MET A SD  1 
ATOM   3377 C  CE  . MET A 1 417 ? 3.674   15.640  6.251   1.00 20.85 ? 417 MET A CE  1 
ATOM   3378 N  N   . LEU A 1 418 ? 2.059   15.418  0.854   1.00 11.82 ? 418 LEU A N   1 
ATOM   3379 C  CA  . LEU A 1 418 ? 0.841   16.010  0.241   1.00 12.83 ? 418 LEU A CA  1 
ATOM   3380 C  C   . LEU A 1 418 ? 0.463   15.234  -1.009  1.00 13.97 ? 418 LEU A C   1 
ATOM   3381 O  O   . LEU A 1 418 ? -0.714  15.257  -1.361  1.00 14.31 ? 418 LEU A O   1 
ATOM   3382 C  CB  . LEU A 1 418 ? 1.119   17.470  -0.068  1.00 14.45 ? 418 LEU A CB  1 
ATOM   3383 C  CG  . LEU A 1 418 ? 1.303   18.326  1.173   1.00 17.13 ? 418 LEU A CG  1 
ATOM   3384 C  CD1 . LEU A 1 418 ? 1.777   19.718  0.785   1.00 19.81 ? 418 LEU A CD1 1 
ATOM   3385 C  CD2 . LEU A 1 418 ? 0.022   18.352  1.978   1.00 21.61 ? 418 LEU A CD2 1 
ATOM   3386 N  N   . LYS A 1 419 ? 1.390   14.627  -1.730  1.00 12.54 ? 419 LYS A N   1 
ATOM   3387 C  CA  . LYS A 1 419 ? 1.025   13.840  -2.925  1.00 12.92 ? 419 LYS A CA  1 
ATOM   3388 C  C   . LYS A 1 419 ? 0.300   12.566  -2.498  1.00 13.43 ? 419 LYS A C   1 
ATOM   3389 O  O   . LYS A 1 419 ? -0.621  12.120  -3.176  1.00 14.29 ? 419 LYS A O   1 
ATOM   3390 C  CB  . LYS A 1 419 ? 2.290   13.419  -3.664  1.00 12.84 ? 419 LYS A CB  1 
ATOM   3391 C  CG  . LYS A 1 419 ? 2.045   12.413  -4.765  1.00 14.78 ? 419 LYS A CG  1 
ATOM   3392 C  CD  . LYS A 1 419 ? 3.247   12.196  -5.587  1.00 16.59 ? 419 LYS A CD  1 
ATOM   3393 C  CE  . LYS A 1 419 ? 3.084   11.109  -6.615  1.00 18.29 ? 419 LYS A CE  1 
ATOM   3394 N  NZ  . LYS A 1 419 ? 4.355   10.788  -7.308  1.00 21.46 ? 419 LYS A NZ  1 
ATOM   3395 N  N   . HIS A 1 420 ? 0.747   11.914  -1.414  1.00 12.51 ? 420 HIS A N   1 
ATOM   3396 C  CA  . HIS A 1 420 ? 0.334   10.542  -1.083  1.00 12.31 ? 420 HIS A CA  1 
ATOM   3397 C  C   . HIS A 1 420 ? -0.837  10.437  -0.141  1.00 11.86 ? 420 HIS A C   1 
ATOM   3398 O  O   . HIS A 1 420 ? -1.435  9.342   -0.104  1.00 13.05 ? 420 HIS A O   1 
ATOM   3399 C  CB  . HIS A 1 420 ? 1.569   9.772   -0.595  1.00 12.25 ? 420 HIS A CB  1 
ATOM   3400 C  CG  . HIS A 1 420 ? 2.480   9.404   -1.729  1.00 12.67 ? 420 HIS A CG  1 
ATOM   3401 N  ND1 . HIS A 1 420 ? 2.170   8.374   -2.613  1.00 15.86 ? 420 HIS A ND1 1 
ATOM   3402 C  CD2 . HIS A 1 420 ? 3.611   9.971   -2.189  1.00 13.43 ? 420 HIS A CD2 1 
ATOM   3403 C  CE1 . HIS A 1 420 ? 3.114   8.332   -3.541  1.00 15.50 ? 420 HIS A CE1 1 
ATOM   3404 N  NE2 . HIS A 1 420 ? 4.015   9.301   -3.310  1.00 14.57 ? 420 HIS A NE2 1 
ATOM   3405 N  N   . PHE A 1 421 ? -1.158  11.476  0.625   1.00 12.25 ? 421 PHE A N   1 
ATOM   3406 C  CA  . PHE A 1 421 ? -2.146  11.390  1.722   1.00 12.83 ? 421 PHE A CA  1 
ATOM   3407 C  C   . PHE A 1 421 ? -3.051  12.625  1.776   1.00 12.47 ? 421 PHE A C   1 
ATOM   3408 O  O   . PHE A 1 421 ? -2.534  13.701  1.604   1.00 14.48 ? 421 PHE A O   1 
ATOM   3409 C  CB  . PHE A 1 421 ? -1.512  11.212  3.117   1.00 13.15 ? 421 PHE A CB  1 
ATOM   3410 C  CG  . PHE A 1 421 ? -0.546  10.057  3.190   1.00 13.12 ? 421 PHE A CG  1 
ATOM   3411 C  CD1 . PHE A 1 421 ? -0.977  8.771   3.408   1.00 12.24 ? 421 PHE A CD1 1 
ATOM   3412 C  CD2 . PHE A 1 421 ? 0.805   10.284  2.987   1.00 12.85 ? 421 PHE A CD2 1 
ATOM   3413 C  CE1 . PHE A 1 421 ? -0.080  7.710   3.382   1.00 13.52 ? 421 PHE A CE1 1 
ATOM   3414 C  CE2 . PHE A 1 421 ? 1.701   9.230   2.983   1.00 13.55 ? 421 PHE A CE2 1 
ATOM   3415 C  CZ  . PHE A 1 421 ? 1.243   7.954   3.213   1.00 14.45 ? 421 PHE A CZ  1 
ATOM   3416 N  N   . ASP A 1 422 ? -4.305  12.403  2.151   1.00 14.92 ? 422 ASP A N   1 
ATOM   3417 C  CA  . ASP A 1 422 ? -5.177  13.417  2.804   1.00 15.03 ? 422 ASP A CA  1 
ATOM   3418 C  C   . ASP A 1 422 ? -4.949  13.396  4.306   1.00 17.34 ? 422 ASP A C   1 
ATOM   3419 O  O   . ASP A 1 422 ? -4.648  12.350  4.869   1.00 19.88 ? 422 ASP A O   1 
ATOM   3420 C  CB  . ASP A 1 422 ? -6.638  13.196  2.438   1.00 17.51 ? 422 ASP A CB  1 
ATOM   3421 C  CG  . ASP A 1 422 ? -6.906  13.338  0.954   1.00 22.08 ? 422 ASP A CG  1 
ATOM   3422 O  OD1 . ASP A 1 422 ? -6.393  14.255  0.318   1.00 25.69 ? 422 ASP A OD1 1 
ATOM   3423 O  OD2 . ASP A 1 422 ? -7.619  12.491  0.441   1.00 29.99 ? 422 ASP A OD2 1 
ATOM   3424 N  N   . PHE A 1 423 ? -5.102  14.538  4.955   1.00 16.71 ? 423 PHE A N   1 
ATOM   3425 C  CA  . PHE A 1 423 ? -4.826  14.672  6.389   1.00 15.71 ? 423 PHE A CA  1 
ATOM   3426 C  C   . PHE A 1 423 ? -6.043  15.172  7.149   1.00 15.94 ? 423 PHE A C   1 
ATOM   3427 O  O   . PHE A 1 423 ? -6.741  16.047  6.635   1.00 21.27 ? 423 PHE A O   1 
ATOM   3428 C  CB  . PHE A 1 423 ? -3.644  15.593  6.601   1.00 15.74 ? 423 PHE A CB  1 
ATOM   3429 C  CG  . PHE A 1 423 ? -2.354  15.000  6.144   1.00 15.46 ? 423 PHE A CG  1 
ATOM   3430 C  CD1 . PHE A 1 423 ? -1.662  14.097  6.921   1.00 16.83 ? 423 PHE A CD1 1 
ATOM   3431 C  CD2 . PHE A 1 423 ? -1.857  15.315  4.893   1.00 16.48 ? 423 PHE A CD2 1 
ATOM   3432 C  CE1 . PHE A 1 423 ? -0.505  13.499  6.450   1.00 15.65 ? 423 PHE A CE1 1 
ATOM   3433 C  CE2 . PHE A 1 423 ? -0.683  14.733  4.427   1.00 16.76 ? 423 PHE A CE2 1 
ATOM   3434 C  CZ  . PHE A 1 423 ? -0.018  13.809  5.204   1.00 15.50 ? 423 PHE A CZ  1 
ATOM   3435 N  N   . GLU A 1 424 ? -6.247  14.666  8.348   1.00 15.53 ? 424 GLU A N   1 
ATOM   3436 C  CA  . GLU A 1 424 ? -7.377  15.068  9.217   1.00 15.87 ? 424 GLU A CA  1 
ATOM   3437 C  C   . GLU A 1 424 ? -6.785  15.439  10.575  1.00 14.44 ? 424 GLU A C   1 
ATOM   3438 O  O   . GLU A 1 424 ? -6.055  14.625  11.157  1.00 15.92 ? 424 GLU A O   1 
ATOM   3439 C  CB  . GLU A 1 424 ? -8.395  13.928  9.317   1.00 17.15 ? 424 GLU A CB  1 
ATOM   3440 C  CG  . GLU A 1 424 ? -9.578  14.248  10.202  1.00 21.74 ? 424 GLU A CG  1 
ATOM   3441 C  CD  . GLU A 1 424 ? -10.490 13.081  10.586  1.00 25.12 ? 424 GLU A CD  1 
ATOM   3442 O  OE1 . GLU A 1 424 ? -10.239 11.915  10.182  1.00 30.05 ? 424 GLU A OE1 1 
ATOM   3443 O  OE2 . GLU A 1 424 ? -11.459 13.335  11.313  1.00 30.11 ? 424 GLU A OE2 1 
ATOM   3444 N  N   . ASP A 1 425 ? -7.203  16.622  11.073  1.00 14.38 ? 425 ASP A N   1 
ATOM   3445 C  CA  . ASP A 1 425 ? -6.952  17.069  12.459  1.00 13.91 ? 425 ASP A CA  1 
ATOM   3446 C  C   . ASP A 1 425 ? -8.050  16.453  13.329  1.00 15.66 ? 425 ASP A C   1 
ATOM   3447 O  O   . ASP A 1 425 ? -8.973  17.180  13.748  1.00 17.07 ? 425 ASP A O   1 
ATOM   3448 C  CB  . ASP A 1 425 ? -6.950  18.568  12.487  1.00 15.14 ? 425 ASP A CB  1 
ATOM   3449 C  CG  . ASP A 1 425 ? -6.819  19.198  13.840  1.00 14.93 ? 425 ASP A CG  1 
ATOM   3450 O  OD1 . ASP A 1 425 ? -6.303  18.544  14.786  1.00 15.03 ? 425 ASP A OD1 1 
ATOM   3451 O  OD2 . ASP A 1 425 ? -7.233  20.359  13.961  1.00 15.72 ? 425 ASP A OD2 1 
ATOM   3452 N  N   . HIS A 1 426 ? -7.983  15.162  13.578  1.00 15.23 ? 426 HIS A N   1 
ATOM   3453 C  CA  . HIS A 1 426 ? -9.088  14.362  14.139  1.00 16.14 ? 426 HIS A CA  1 
ATOM   3454 C  C   . HIS A 1 426 ? -9.322  14.708  15.602  1.00 17.53 ? 426 HIS A C   1 
ATOM   3455 O  O   . HIS A 1 426 ? -10.451 14.437  16.054  1.00 20.78 ? 426 HIS A O   1 
ATOM   3456 C  CB  . HIS A 1 426 ? -8.818  12.873  13.905  1.00 16.25 ? 426 HIS A CB  1 
ATOM   3457 C  CG  . HIS A 1 426 ? -7.670  12.325  14.664  1.00 17.12 ? 426 HIS A CG  1 
ATOM   3458 N  ND1 . HIS A 1 426 ? -6.373  12.712  14.364  1.00 16.96 ? 426 HIS A ND1 1 
ATOM   3459 C  CD2 . HIS A 1 426 ? -7.602  11.492  15.717  1.00 15.64 ? 426 HIS A CD2 1 
ATOM   3460 C  CE1 . HIS A 1 426 ? -5.559  12.143  15.223  1.00 15.94 ? 426 HIS A CE1 1 
ATOM   3461 N  NE2 . HIS A 1 426 ? -6.287  11.335  16.048  1.00 17.46 ? 426 HIS A NE2 1 
ATOM   3462 N  N   . THR A 1 427 ? -8.354  15.286  16.318  1.00 15.56 ? 427 THR A N   1 
ATOM   3463 C  CA  . THR A 1 427 ? -8.504  15.687  17.726  1.00 16.96 ? 427 THR A CA  1 
ATOM   3464 C  C   . THR A 1 427 ? -8.817  17.183  17.881  1.00 16.26 ? 427 THR A C   1 
ATOM   3465 O  O   . THR A 1 427 ? -8.883  17.641  19.053  1.00 18.45 ? 427 THR A O   1 
ATOM   3466 C  CB  . THR A 1 427 ? -7.297  15.263  18.570  1.00 16.61 ? 427 THR A CB  1 
ATOM   3467 O  OG1 . THR A 1 427 ? -6.192  16.117  18.281  1.00 17.38 ? 427 THR A OG1 1 
ATOM   3468 C  CG2 . THR A 1 427 ? -6.878  13.832  18.343  1.00 17.39 ? 427 THR A CG2 1 
ATOM   3469 N  N   . ASN A 1 428 ? -8.854  17.972  16.799  1.00 16.45 ? 428 ASN A N   1 
ATOM   3470 C  CA  . ASN A 1 428 ? -8.862  19.455  16.883  1.00 16.49 ? 428 ASN A CA  1 
ATOM   3471 C  C   . ASN A 1 428 ? -7.730  19.887  17.840  1.00 16.16 ? 428 ASN A C   1 
ATOM   3472 O  O   . ASN A 1 428 ? -7.932  20.504  18.884  1.00 15.96 ? 428 ASN A O   1 
ATOM   3473 C  CB  . ASN A 1 428 ? -10.240 19.968  17.293  1.00 19.04 ? 428 ASN A CB  1 
ATOM   3474 C  CG  . ASN A 1 428 ? -10.269 21.469  17.187  1.00 22.19 ? 428 ASN A CG  1 
ATOM   3475 O  OD1 . ASN A 1 428 ? -9.452  22.089  16.511  1.00 23.10 ? 428 ASN A OD1 1 
ATOM   3476 N  ND2 . ASN A 1 428 ? -11.173 22.068  17.942  1.00 27.15 ? 428 ASN A ND2 1 
ATOM   3477 N  N   . TYR A 1 429 ? -6.515  19.565  17.433  1.00 14.66 ? 429 TYR A N   1 
ATOM   3478 C  CA  . TYR A 1 429 ? -5.333  19.671  18.314  1.00 13.61 ? 429 TYR A CA  1 
ATOM   3479 C  C   . TYR A 1 429 ? -5.107  21.110  18.724  1.00 13.44 ? 429 TYR A C   1 
ATOM   3480 O  O   . TYR A 1 429 ? -5.122  22.020  17.890  1.00 14.78 ? 429 TYR A O   1 
ATOM   3481 C  CB  . TYR A 1 429 ? -4.120  19.142  17.565  1.00 13.29 ? 429 TYR A CB  1 
ATOM   3482 C  CG  . TYR A 1 429 ? -2.775  19.503  18.139  1.00 12.74 ? 429 TYR A CG  1 
ATOM   3483 C  CD1 . TYR A 1 429 ? -2.331  18.916  19.317  1.00 13.57 ? 429 TYR A CD1 1 
ATOM   3484 C  CD2 . TYR A 1 429 ? -1.983  20.476  17.573  1.00 13.53 ? 429 TYR A CD2 1 
ATOM   3485 C  CE1 . TYR A 1 429 ? -1.096  19.242  19.867  1.00 12.87 ? 429 TYR A CE1 1 
ATOM   3486 C  CE2 . TYR A 1 429 ? -0.749  20.799  18.092  1.00 12.98 ? 429 TYR A CE2 1 
ATOM   3487 C  CZ  . TYR A 1 429 ? -0.280  20.165  19.233  1.00 13.38 ? 429 TYR A CZ  1 
ATOM   3488 O  OH  . TYR A 1 429 ? 0.916   20.566  19.791  1.00 13.67 ? 429 TYR A OH  1 
ATOM   3489 N  N   A GLU A 1 430 ? -4.805  21.297  20.009  0.50 14.67 ? 430 GLU A N   1 
ATOM   3490 N  N   B GLU A 1 430 ? -4.839  21.328  20.012  0.50 14.54 ? 430 GLU A N   1 
ATOM   3491 C  CA  A GLU A 1 430 ? -4.479  22.614  20.601  0.50 15.48 ? 430 GLU A CA  1 
ATOM   3492 C  CA  B GLU A 1 430 ? -4.498  22.669  20.544  0.50 15.21 ? 430 GLU A CA  1 
ATOM   3493 C  C   A GLU A 1 430 ? -2.954  22.769  20.634  0.50 14.56 ? 430 GLU A C   1 
ATOM   3494 C  C   B GLU A 1 430 ? -2.974  22.777  20.624  0.50 14.53 ? 430 GLU A C   1 
ATOM   3495 O  O   A GLU A 1 430 ? -2.291  22.009  21.361  0.50 15.08 ? 430 GLU A O   1 
ATOM   3496 O  O   B GLU A 1 430 ? -2.341  21.995  21.357  0.50 15.20 ? 430 GLU A O   1 
ATOM   3497 C  CB  A GLU A 1 430 ? -5.046  22.715  22.021  0.50 17.98 ? 430 GLU A CB  1 
ATOM   3498 C  CB  B GLU A 1 430 ? -5.143  22.906  21.911  0.50 17.76 ? 430 GLU A CB  1 
ATOM   3499 C  CG  A GLU A 1 430 ? -4.883  24.098  22.627  0.50 20.44 ? 430 GLU A CG  1 
ATOM   3500 C  CG  B GLU A 1 430 ? -6.657  22.993  21.832  0.50 20.35 ? 430 GLU A CG  1 
ATOM   3501 C  CD  A GLU A 1 430 ? -5.283  24.301  24.086  0.50 25.65 ? 430 GLU A CD  1 
ATOM   3502 C  CD  B GLU A 1 430 ? -7.346  23.151  23.171  0.50 25.26 ? 430 GLU A CD  1 
ATOM   3503 O  OE1 A GLU A 1 430 ? -5.806  23.358  24.706  0.50 26.96 ? 430 GLU A OE1 1 
ATOM   3504 O  OE1 B GLU A 1 430 ? -6.897  24.011  23.979  0.50 30.48 ? 430 GLU A OE1 1 
ATOM   3505 O  OE2 A GLU A 1 430 ? -5.037  25.414  24.604  0.50 29.09 ? 430 GLU A OE2 1 
ATOM   3506 O  OE2 B GLU A 1 430 ? -8.338  22.418  23.386  0.50 31.20 ? 430 GLU A OE2 1 
ATOM   3507 N  N   . LEU A 1 431 ? -2.435  23.762  19.923  1.00 14.70 ? 431 LEU A N   1 
ATOM   3508 C  CA  . LEU A 1 431 ? -0.982  23.928  19.815  1.00 14.19 ? 431 LEU A CA  1 
ATOM   3509 C  C   . LEU A 1 431 ? -0.393  24.000  21.231  1.00 14.81 ? 431 LEU A C   1 
ATOM   3510 O  O   . LEU A 1 431 ? -0.808  24.844  22.046  1.00 15.80 ? 431 LEU A O   1 
ATOM   3511 C  CB  . LEU A 1 431 ? -0.683  25.146  18.965  1.00 14.94 ? 431 LEU A CB  1 
ATOM   3512 C  CG  . LEU A 1 431 ? 0.799   25.424  18.728  1.00 15.07 ? 431 LEU A CG  1 
ATOM   3513 C  CD1 . LEU A 1 431 ? 1.457   24.224  18.043  1.00 14.83 ? 431 LEU A CD1 1 
ATOM   3514 C  CD2 . LEU A 1 431 ? 0.949   26.675  17.889  1.00 16.77 ? 431 LEU A CD2 1 
ATOM   3515 N  N   . ASP A 1 432 ? 0.613   23.187  21.462  1.00 13.81 ? 432 ASP A N   1 
ATOM   3516 C  CA  . ASP A 1 432 ? 1.389   23.102  22.725  1.00 14.41 ? 432 ASP A CA  1 
ATOM   3517 C  C   . ASP A 1 432 ? 2.837   23.001  22.260  1.00 15.15 ? 432 ASP A C   1 
ATOM   3518 O  O   . ASP A 1 432 ? 3.196   22.013  21.612  1.00 16.45 ? 432 ASP A O   1 
ATOM   3519 C  CB  . ASP A 1 432 ? 0.920   21.932  23.573  1.00 16.21 ? 432 ASP A CB  1 
ATOM   3520 C  CG  . ASP A 1 432 ? 1.592   21.845  24.923  1.00 21.88 ? 432 ASP A CG  1 
ATOM   3521 O  OD1 . ASP A 1 432 ? 2.561   22.558  25.124  1.00 23.47 ? 432 ASP A OD1 1 
ATOM   3522 O  OD2 . ASP A 1 432 ? 1.245   20.921  25.687  1.00 26.46 ? 432 ASP A OD2 1 
ATOM   3523 N  N   . ILE A 1 433 ? 3.629   24.030  22.530  1.00 13.24 ? 433 ILE A N   1 
ATOM   3524 C  CA  . ILE A 1 433 ? 4.991   24.103  21.986  1.00 13.47 ? 433 ILE A CA  1 
ATOM   3525 C  C   . ILE A 1 433 ? 6.000   23.719  23.061  1.00 13.29 ? 433 ILE A C   1 
ATOM   3526 O  O   . ILE A 1 433 ? 6.179   24.471  24.034  1.00 14.60 ? 433 ILE A O   1 
ATOM   3527 C  CB  . ILE A 1 433 ? 5.272   25.482  21.397  1.00 13.24 ? 433 ILE A CB  1 
ATOM   3528 C  CG1 . ILE A 1 433 ? 4.336   25.779  20.223  1.00 15.06 ? 433 ILE A CG1 1 
ATOM   3529 C  CG2 . ILE A 1 433 ? 6.747   25.525  21.009  1.00 13.57 ? 433 ILE A CG2 1 
ATOM   3530 C  CD1 . ILE A 1 433 ? 4.424   27.196  19.711  1.00 17.43 ? 433 ILE A CD1 1 
ATOM   3531 N  N   . LYS A 1 434 ? 6.687   22.630  22.817  1.00 12.78 ? 434 LYS A N   1 
ATOM   3532 C  CA  . LYS A 1 434 ? 7.760   22.142  23.713  1.00 13.61 ? 434 LYS A CA  1 
ATOM   3533 C  C   . LYS A 1 434 ? 9.086   22.782  23.256  1.00 14.97 ? 434 LYS A C   1 
ATOM   3534 O  O   . LYS A 1 434 ? 9.371   22.869  22.040  1.00 14.57 ? 434 LYS A O   1 
ATOM   3535 C  CB  . LYS A 1 434 ? 7.890   20.627  23.573  1.00 15.57 ? 434 LYS A CB  1 
ATOM   3536 C  CG  . LYS A 1 434 ? 9.056   20.016  24.331  1.00 18.57 ? 434 LYS A CG  1 
ATOM   3537 C  CD  . LYS A 1 434 ? 8.954   18.504  24.375  1.00 21.26 ? 434 LYS A CD  1 
ATOM   3538 C  CE  . LYS A 1 434 ? 10.168  17.906  25.042  1.00 26.52 ? 434 LYS A CE  1 
ATOM   3539 N  NZ  . LYS A 1 434 ? 9.917   17.882  26.493  1.00 36.11 ? 434 LYS A NZ  1 
ATOM   3540 N  N   . GLU A 1 435 ? 9.908   23.156  24.220  1.00 13.10 ? 435 GLU A N   1 
ATOM   3541 C  CA  . GLU A 1 435 ? 11.167  23.841  23.926  1.00 13.94 ? 435 GLU A CA  1 
ATOM   3542 C  C   . GLU A 1 435 ? 12.333  22.984  24.358  1.00 14.37 ? 435 GLU A C   1 
ATOM   3543 O  O   . GLU A 1 435 ? 12.380  22.574  25.540  1.00 16.54 ? 435 GLU A O   1 
ATOM   3544 C  CB  . GLU A 1 435 ? 11.201  25.193  24.632  1.00 13.39 ? 435 GLU A CB  1 
ATOM   3545 C  CG  . GLU A 1 435 ? 10.014  26.073  24.394  1.00 13.48 ? 435 GLU A CG  1 
ATOM   3546 C  CD  . GLU A 1 435 ? 10.224  27.529  24.774  1.00 13.73 ? 435 GLU A CD  1 
ATOM   3547 O  OE1 . GLU A 1 435 ? 11.405  27.909  25.035  1.00 16.20 ? 435 GLU A OE1 1 
ATOM   3548 O  OE2 . GLU A 1 435 ? 9.251   28.308  24.757  1.00 14.66 ? 435 GLU A OE2 1 
ATOM   3549 N  N   . THR A 1 436 ? 13.241  22.697  23.441  1.00 15.87 ? 436 THR A N   1 
ATOM   3550 C  CA  . THR A 1 436 ? 14.537  22.072  23.718  1.00 16.02 ? 436 THR A CA  1 
ATOM   3551 C  C   . THR A 1 436 ? 15.548  23.101  23.244  1.00 15.09 ? 436 THR A C   1 
ATOM   3552 O  O   . THR A 1 436 ? 15.403  24.264  23.568  1.00 18.19 ? 436 THR A O   1 
ATOM   3553 C  CB  . THR A 1 436 ? 14.578  20.690  23.046  1.00 17.92 ? 436 THR A CB  1 
ATOM   3554 O  OG1 . THR A 1 436 ? 14.267  20.842  21.647  1.00 18.66 ? 436 THR A OG1 1 
ATOM   3555 C  CG2 . THR A 1 436 ? 13.627  19.691  23.649  1.00 18.23 ? 436 THR A CG2 1 
ATOM   3556 N  N   . LEU A 1 437 ? 16.508  22.690  22.418  1.00 17.07 ? 437 LEU A N   1 
ATOM   3557 C  CA  . LEU A 1 437 ? 17.278  23.698  21.700  1.00 16.90 ? 437 LEU A CA  1 
ATOM   3558 C  C   . LEU A 1 437 ? 16.322  24.435  20.754  1.00 15.25 ? 437 LEU A C   1 
ATOM   3559 O  O   . LEU A 1 437 ? 16.532  25.605  20.434  1.00 17.00 ? 437 LEU A O   1 
ATOM   3560 C  CB  . LEU A 1 437 ? 18.395  22.980  20.936  1.00 19.42 ? 437 LEU A CB  1 
ATOM   3561 C  CG  . LEU A 1 437 ? 19.403  23.894  20.265  1.00 23.35 ? 437 LEU A CG  1 
ATOM   3562 C  CD1 . LEU A 1 437 ? 20.234  24.638  21.300  1.00 24.31 ? 437 LEU A CD1 1 
ATOM   3563 C  CD2 . LEU A 1 437 ? 20.318  23.080  19.380  1.00 27.19 ? 437 LEU A CD2 1 
ATOM   3564 N  N   . THR A 1 438 ? 15.262  23.744  20.336  1.00 14.33 ? 438 THR A N   1 
ATOM   3565 C  CA  . THR A 1 438 ? 14.344  24.263  19.319  1.00 14.65 ? 438 THR A CA  1 
ATOM   3566 C  C   . THR A 1 438 ? 12.886  24.148  19.759  1.00 15.14 ? 438 THR A C   1 
ATOM   3567 O  O   . THR A 1 438 ? 12.589  23.630  20.829  1.00 15.02 ? 438 THR A O   1 
ATOM   3568 C  CB  . THR A 1 438 ? 14.536  23.504  18.007  1.00 14.75 ? 438 THR A CB  1 
ATOM   3569 O  OG1 . THR A 1 438 ? 14.300  22.126  18.348  1.00 14.72 ? 438 THR A OG1 1 
ATOM   3570 C  CG2 . THR A 1 438 ? 15.913  23.715  17.385  1.00 14.86 ? 438 THR A CG2 1 
ATOM   3571 N  N   . LEU A 1 439 ? 11.987  24.640  18.915  1.00 14.19 ? 439 LEU A N   1 
ATOM   3572 C  CA  . LEU A 1 439 ? 10.529  24.578  19.162  1.00 14.17 ? 439 LEU A CA  1 
ATOM   3573 C  C   . LEU A 1 439 ? 9.895   23.462  18.354  1.00 16.00 ? 439 LEU A C   1 
ATOM   3574 O  O   . LEU A 1 439 ? 10.213  23.392  17.132  1.00 16.90 ? 439 LEU A O   1 
ATOM   3575 C  CB  . LEU A 1 439 ? 9.896   25.901  18.753  1.00 15.55 ? 439 LEU A CB  1 
ATOM   3576 C  CG  . LEU A 1 439 ? 10.495  27.154  19.362  1.00 16.19 ? 439 LEU A CG  1 
ATOM   3577 C  CD1 . LEU A 1 439 ? 9.718   28.384  18.919  1.00 17.18 ? 439 LEU A CD1 1 
ATOM   3578 C  CD2 . LEU A 1 439 ? 10.511  27.089  20.867  1.00 16.21 ? 439 LEU A CD2 1 
ATOM   3579 N  N   . LYS A 1 440 ? 8.996   22.697  18.978  1.00 14.60 ? 440 LYS A N   1 
ATOM   3580 C  CA  . LYS A 1 440 ? 8.212   21.664  18.253  1.00 15.12 ? 440 LYS A CA  1 
ATOM   3581 C  C   . LYS A 1 440 ? 6.821   21.577  18.858  1.00 16.04 ? 440 LYS A C   1 
ATOM   3582 O  O   . LYS A 1 440 ? 6.632   21.834  20.054  1.00 16.08 ? 440 LYS A O   1 
ATOM   3583 C  CB  . LYS A 1 440 ? 8.876   20.297  18.395  1.00 17.11 ? 440 LYS A CB  1 
ATOM   3584 C  CG  . LYS A 1 440 ? 10.241  20.167  17.753  1.00 19.98 ? 440 LYS A CG  1 
ATOM   3585 C  CD  . LYS A 1 440 ? 10.760  18.736  17.826  1.00 20.34 ? 440 LYS A CD  1 
ATOM   3586 C  CE  . LYS A 1 440 ? 12.100  18.624  17.156  1.00 19.78 ? 440 LYS A CE  1 
ATOM   3587 N  NZ  . LYS A 1 440 ? 12.672  17.252  17.245  1.00 20.96 ? 440 LYS A NZ  1 
ATOM   3588 N  N   . PRO A 1 441 ? 5.797   21.258  18.073  1.00 13.60 ? 441 PRO A N   1 
ATOM   3589 C  CA  . PRO A 1 441 ? 4.454   21.059  18.580  1.00 14.03 ? 441 PRO A CA  1 
ATOM   3590 C  C   . PRO A 1 441 ? 4.215   19.714  19.271  1.00 18.56 ? 441 PRO A C   1 
ATOM   3591 O  O   . PRO A 1 441 ? 3.746   18.763  18.605  1.00 20.39 ? 441 PRO A O   1 
ATOM   3592 C  CB  . PRO A 1 441 ? 3.556   21.148  17.352  1.00 16.93 ? 441 PRO A CB  1 
ATOM   3593 C  CG  . PRO A 1 441 ? 4.453   20.917  16.171  1.00 17.30 ? 441 PRO A CG  1 
ATOM   3594 C  CD  . PRO A 1 441 ? 5.870   21.237  16.588  1.00 14.76 ? 441 PRO A CD  1 
ATOM   3595 N  N   . GLU A 1 442 ? 4.211   19.706  20.598  1.00 14.33 ? 442 GLU A N   1 
ATOM   3596 C  CA  . GLU A 1 442 ? 4.193   18.481  21.399  1.00 14.89 ? 442 GLU A CA  1 
ATOM   3597 C  C   . GLU A 1 442 ? 2.776   17.880  21.334  1.00 13.38 ? 442 GLU A C   1 
ATOM   3598 O  O   . GLU A 1 442 ? 1.780   18.620  21.484  1.00 13.68 ? 442 GLU A O   1 
ATOM   3599 C  CB  . GLU A 1 442 ? 4.536   18.809  22.871  1.00 16.58 ? 442 GLU A CB  1 
ATOM   3600 C  CG  . GLU A 1 442 ? 4.647   17.534  23.717  1.00 20.85 ? 442 GLU A CG  1 
ATOM   3601 C  CD  . GLU A 1 442 ? 5.166   17.714  25.119  1.00 25.13 ? 442 GLU A CD  1 
ATOM   3602 O  OE1 . GLU A 1 442 ? 5.056   18.810  25.626  1.00 28.67 ? 442 GLU A OE1 1 
ATOM   3603 O  OE2 . GLU A 1 442 ? 5.637   16.718  25.691  1.00 31.31 ? 442 GLU A OE2 1 
ATOM   3604 N  N   . GLY A 1 443 ? 2.661   16.576  21.107  1.00 12.80 ? 443 GLY A N   1 
ATOM   3605 C  CA  . GLY A 1 443 ? 1.336   15.924  21.151  1.00 14.50 ? 443 GLY A CA  1 
ATOM   3606 C  C   . GLY A 1 443 ? 0.537   16.093  19.882  1.00 15.58 ? 443 GLY A C   1 
ATOM   3607 O  O   . GLY A 1 443 ? -0.627  15.709  19.847  1.00 16.99 ? 443 GLY A O   1 
ATOM   3608 N  N   . PHE A 1 444 ? 1.125   16.713  18.862  1.00 14.71 ? 444 PHE A N   1 
ATOM   3609 C  CA  . PHE A 1 444 ? 0.446   16.910  17.564  1.00 12.86 ? 444 PHE A CA  1 
ATOM   3610 C  C   . PHE A 1 444 ? 0.256   15.563  16.864  1.00 12.82 ? 444 PHE A C   1 
ATOM   3611 O  O   . PHE A 1 444 ? 1.240   14.840  16.639  1.00 12.54 ? 444 PHE A O   1 
ATOM   3612 C  CB  . PHE A 1 444 ? 1.199   17.924  16.729  1.00 12.72 ? 444 PHE A CB  1 
ATOM   3613 C  CG  . PHE A 1 444 ? 0.621   18.194  15.364  1.00 12.11 ? 444 PHE A CG  1 
ATOM   3614 C  CD1 . PHE A 1 444 ? -0.747  18.229  15.170  1.00 13.28 ? 444 PHE A CD1 1 
ATOM   3615 C  CD2 . PHE A 1 444 ? 1.454   18.395  14.265  1.00 13.16 ? 444 PHE A CD2 1 
ATOM   3616 C  CE1 . PHE A 1 444 ? -1.263  18.447  13.909  1.00 12.73 ? 444 PHE A CE1 1 
ATOM   3617 C  CE2 . PHE A 1 444 ? 0.915   18.653  13.034  1.00 12.75 ? 444 PHE A CE2 1 
ATOM   3618 C  CZ  . PHE A 1 444 ? -0.448  18.628  12.831  1.00 12.64 ? 444 PHE A CZ  1 
ATOM   3619 N  N   . VAL A 1 445 ? -1.009  15.192  16.610  1.00 12.48 ? 445 VAL A N   1 
ATOM   3620 C  CA  . VAL A 1 445 ? -1.403  13.919  15.972  1.00 13.40 ? 445 VAL A CA  1 
ATOM   3621 C  C   . VAL A 1 445 ? -2.363  14.235  14.843  1.00 13.92 ? 445 VAL A C   1 
ATOM   3622 O  O   . VAL A 1 445 ? -3.127  15.241  14.950  1.00 14.16 ? 445 VAL A O   1 
ATOM   3623 C  CB  . VAL A 1 445 ? -2.035  12.931  16.958  1.00 13.81 ? 445 VAL A CB  1 
ATOM   3624 C  CG1 . VAL A 1 445 ? -1.011  12.484  17.992  1.00 14.44 ? 445 VAL A CG1 1 
ATOM   3625 C  CG2 . VAL A 1 445 ? -3.240  13.541  17.640  1.00 15.72 ? 445 VAL A CG2 1 
ATOM   3626 N  N   . VAL A 1 446 ? -2.301  13.446  13.782  1.00 12.50 ? 446 VAL A N   1 
ATOM   3627 C  CA  . VAL A 1 446 ? -3.250  13.546  12.646  1.00 12.33 ? 446 VAL A CA  1 
ATOM   3628 C  C   . VAL A 1 446 ? -3.590  12.131  12.212  1.00 13.46 ? 446 VAL A C   1 
ATOM   3629 O  O   . VAL A 1 446 ? -2.872  11.175  12.539  1.00 14.08 ? 446 VAL A O   1 
ATOM   3630 C  CB  . VAL A 1 446 ? -2.671  14.333  11.469  1.00 13.92 ? 446 VAL A CB  1 
ATOM   3631 C  CG1 . VAL A 1 446 ? -2.401  15.763  11.877  1.00 14.48 ? 446 VAL A CG1 1 
ATOM   3632 C  CG2 . VAL A 1 446 ? -1.457  13.640  10.856  1.00 13.31 ? 446 VAL A CG2 1 
ATOM   3633 N  N   . LYS A 1 447 ? -4.640  12.037  11.414  1.00 14.00 ? 447 LYS A N   1 
ATOM   3634 C  CA  . LYS A 1 447 ? -4.905  10.801  10.658  1.00 14.98 ? 447 LYS A CA  1 
ATOM   3635 C  C   . LYS A 1 447 ? -4.641  11.081  9.202   1.00 16.42 ? 447 LYS A C   1 
ATOM   3636 O  O   . LYS A 1 447 ? -4.950  12.155  8.720   1.00 17.37 ? 447 LYS A O   1 
ATOM   3637 C  CB  . LYS A 1 447 ? -6.353  10.383  10.847  1.00 17.69 ? 447 LYS A CB  1 
ATOM   3638 C  CG  . LYS A 1 447 ? -6.610  9.665   12.151  1.00 19.81 ? 447 LYS A CG  1 
ATOM   3639 C  CD  . LYS A 1 447 ? -8.082  9.321   12.275  1.00 25.07 ? 447 LYS A CD  1 
ATOM   3640 C  CE  . LYS A 1 447 ? -8.329  8.302   13.347  1.00 31.40 ? 447 LYS A CE  1 
ATOM   3641 N  NZ  . LYS A 1 447 ? -9.797  8.159   13.543  1.00 36.83 ? 447 LYS A NZ  1 
ATOM   3642 N  N   . ALA A 1 448 ? -4.079  10.104  8.526   1.00 17.24 ? 448 ALA A N   1 
ATOM   3643 C  CA  . ALA A 1 448 ? -3.820  10.202  7.094   1.00 17.90 ? 448 ALA A CA  1 
ATOM   3644 C  C   . ALA A 1 448 ? -4.772  9.234   6.379   1.00 19.41 ? 448 ALA A C   1 
ATOM   3645 O  O   . ALA A 1 448 ? -5.246  8.185   6.985   1.00 23.47 ? 448 ALA A O   1 
ATOM   3646 C  CB  . ALA A 1 448 ? -2.373  9.980   6.796   1.00 18.94 ? 448 ALA A CB  1 
ATOM   3647 N  N   . LYS A 1 449 ? -5.206  9.626   5.216   1.00 16.82 ? 449 LYS A N   1 
ATOM   3648 C  CA  . LYS A 1 449 ? -5.950  8.699   4.318   1.00 20.30 ? 449 LYS A CA  1 
ATOM   3649 C  C   . LYS A 1 449 ? -5.148  8.637   3.038   1.00 15.62 ? 449 LYS A C   1 
ATOM   3650 O  O   . LYS A 1 449 ? -4.950  9.679   2.400   1.00 17.10 ? 449 LYS A O   1 
ATOM   3651 C  CB  . LYS A 1 449 ? -7.396  9.136   4.087   1.00 24.31 ? 449 LYS A CB  1 
ATOM   3652 C  CG  . LYS A 1 449 ? -8.408  8.084   4.508   1.00 34.27 ? 449 LYS A CG  1 
ATOM   3653 C  CD  . LYS A 1 449 ? -9.704  8.114   3.717   1.00 40.39 ? 449 LYS A CD  1 
ATOM   3654 C  CE  . LYS A 1 449 ? -10.205 6.719   3.388   1.00 43.85 ? 449 LYS A CE  1 
ATOM   3655 N  NZ  . LYS A 1 449 ? -10.604 6.622   1.965   1.00 47.00 ? 449 LYS A NZ  1 
ATOM   3656 N  N   . SER A 1 450 ? -4.682  7.443   2.699   1.00 16.47 ? 450 SER A N   1 
ATOM   3657 C  CA  . SER A 1 450 ? -3.866  7.245   1.490   1.00 16.97 ? 450 SER A CA  1 
ATOM   3658 C  C   . SER A 1 450 ? -4.665  7.629   0.243   1.00 17.83 ? 450 SER A C   1 
ATOM   3659 O  O   . SER A 1 450 ? -5.872  7.233   0.128   1.00 19.28 ? 450 SER A O   1 
ATOM   3660 C  CB  . SER A 1 450 ? -3.437  5.838   1.442   1.00 19.60 ? 450 SER A CB  1 
ATOM   3661 O  OG  . SER A 1 450 ? -2.683  5.619   0.287   1.00 17.89 ? 450 SER A OG  1 
ATOM   3662 N  N   . LYS A 1 451 ? -4.011  8.323   -0.693  1.00 16.53 ? 451 LYS A N   1 
ATOM   3663 C  CA  . LYS A 1 451 ? -4.551  8.540   -2.045  1.00 17.49 ? 451 LYS A CA  1 
ATOM   3664 C  C   . LYS A 1 451 ? -4.295  7.302   -2.908  1.00 19.25 ? 451 LYS A C   1 
ATOM   3665 O  O   . LYS A 1 451 ? -4.710  7.307   -4.055  1.00 21.65 ? 451 LYS A O   1 
ATOM   3666 C  CB  . LYS A 1 451 ? -3.933  9.824   -2.582  1.00 21.21 ? 451 LYS A CB  1 
ATOM   3667 C  CG  . LYS A 1 451 ? -4.371  11.069  -1.829  1.00 19.68 ? 451 LYS A CG  1 
ATOM   3668 C  CD  . LYS A 1 451 ? -3.775  12.356  -2.398  1.00 23.40 ? 451 LYS A CD  1 
ATOM   3669 C  CE  . LYS A 1 451 ? -4.361  13.623  -1.864  1.00 26.70 ? 451 LYS A CE  1 
ATOM   3670 N  NZ  . LYS A 1 451 ? -5.762  13.777  -2.328  1.00 28.59 ? 451 LYS A NZ  1 
ATOM   3671 N  N   . LYS A 1 452 ? -3.632  6.284   -2.381  1.00 17.70 ? 452 LYS A N   1 
ATOM   3672 C  CA  . LYS A 1 452 ? -3.395  4.976   -3.060  1.00 20.97 ? 452 LYS A CA  1 
ATOM   3673 C  C   . LYS A 1 452 ? -2.557  5.173   -4.327  1.00 23.46 ? 452 LYS A C   1 
ATOM   3674 O  O   . LYS A 1 452 ? -2.884  4.588   -5.407  1.00 23.91 ? 452 LYS A O   1 
ATOM   3675 C  CB  . LYS A 1 452 ? -4.765  4.320   -3.283  1.00 24.66 ? 452 LYS A CB  1 
ATOM   3676 C  CG  . LYS A 1 452 ? -5.397  3.825   -1.988  1.00 28.50 ? 452 LYS A CG  1 
ATOM   3677 C  CD  . LYS A 1 452 ? -4.524  2.806   -1.211  1.00 33.27 ? 452 LYS A CD  1 
ATOM   3678 C  CE  . LYS A 1 452 ? -5.316  1.989   -0.204  1.00 35.58 ? 452 LYS A CE  1 
ATOM   3679 N  NZ  . LYS A 1 452 ? -4.582  1.770   1.072   1.00 36.47 ? 452 LYS A NZ  1 
ATOM   3680 N  N   . ILE A 1 453 ? -1.548  6.026   -4.253  1.00 18.42 ? 453 ILE A N   1 
ATOM   3681 C  CA  . ILE A 1 453 ? -0.649  6.333   -5.387  1.00 20.48 ? 453 ILE A CA  1 
ATOM   3682 C  C   . ILE A 1 453 ? 0.641   5.586   -5.146  1.00 20.34 ? 453 ILE A C   1 
ATOM   3683 O  O   . ILE A 1 453 ? 1.309   5.804   -4.145  1.00 18.74 ? 453 ILE A O   1 
ATOM   3684 C  CB  . ILE A 1 453 ? -0.410  7.832   -5.558  1.00 20.41 ? 453 ILE A CB  1 
ATOM   3685 C  CG1 . ILE A 1 453 ? -1.722  8.557   -5.844  1.00 21.56 ? 453 ILE A CG1 1 
ATOM   3686 C  CG2 . ILE A 1 453 ? 0.667   8.095   -6.605  1.00 19.21 ? 453 ILE A CG2 1 
ATOM   3687 C  CD1 . ILE A 1 453 ? -1.615  10.011  -5.567  1.00 23.41 ? 453 ILE A CD1 1 
ATOM   3688 N  N   . PRO A 1 454 ? 0.982   4.613   -6.001  1.00 23.23 ? 454 PRO A N   1 
ATOM   3689 C  CA  . PRO A 1 454 ? 2.158   3.779   -5.790  1.00 24.02 ? 454 PRO A CA  1 
ATOM   3690 C  C   . PRO A 1 454 ? 3.469   4.560   -5.807  1.00 23.75 ? 454 PRO A C   1 
ATOM   3691 O  O   . PRO A 1 454 ? 3.564   5.608   -6.463  1.00 25.54 ? 454 PRO A O   1 
ATOM   3692 C  CB  . PRO A 1 454 ? 2.178   2.836   -7.013  1.00 27.62 ? 454 PRO A CB  1 
ATOM   3693 C  CG  . PRO A 1 454 ? 0.754   2.826   -7.499  1.00 28.54 ? 454 PRO A CG  1 
ATOM   3694 C  CD  . PRO A 1 454 ? 0.186   4.191   -7.177  1.00 24.75 ? 454 PRO A CD  1 
ATOM   3695 N  N   . LEU A 1 455 ? 4.454   4.007   -5.092  1.00 24.18 ? 455 LEU A N   1 
ATOM   3696 C  CA  . LEU A 1 455 ? 5.874   4.423   -5.175  1.00 27.18 ? 455 LEU A CA  1 
ATOM   3697 C  C   . LEU A 1 455 ? 6.589   3.515   -6.187  1.00 33.69 ? 455 LEU A C   1 
ATOM   3698 O  O   . LEU A 1 455 ? 5.994   2.590   -6.744  1.00 38.56 ? 455 LEU A O   1 
ATOM   3699 C  CB  . LEU A 1 455 ? 6.538   4.302   -3.800  1.00 27.89 ? 455 LEU A CB  1 
ATOM   3700 C  CG  . LEU A 1 455 ? 5.984   5.223   -2.727  1.00 27.72 ? 455 LEU A CG  1 
ATOM   3701 C  CD1 . LEU A 1 455 ? 6.342   4.710   -1.352  1.00 28.35 ? 455 LEU A CD1 1 
ATOM   3702 C  CD2 . LEU A 1 455 ? 6.518   6.649   -2.885  1.00 29.76 ? 455 LEU A CD2 1 
ATOM   3703 O  OXT . LEU A 1 455 ? 7.767   3.738   -6.438  1.00 36.78 ? 455 LEU A OXT 1 
ATOM   3704 N  N   . ILE B 1 2   ? 2.234   -59.047 26.856  1.00 37.79 ? 2   ILE B N   1 
ATOM   3705 C  CA  . ILE B 1 2   ? 1.723   -57.965 27.768  1.00 37.42 ? 2   ILE B CA  1 
ATOM   3706 C  C   . ILE B 1 2   ? 2.829   -57.621 28.775  1.00 40.67 ? 2   ILE B C   1 
ATOM   3707 O  O   . ILE B 1 2   ? 3.333   -58.529 29.463  1.00 39.73 ? 2   ILE B O   1 
ATOM   3708 C  CB  . ILE B 1 2   ? 0.393   -58.331 28.462  1.00 38.72 ? 2   ILE B CB  1 
ATOM   3709 C  CG1 . ILE B 1 2   ? -0.755  -58.547 27.470  1.00 39.63 ? 2   ILE B CG1 1 
ATOM   3710 C  CG2 . ILE B 1 2   ? 0.033   -57.290 29.521  1.00 40.31 ? 2   ILE B CG2 1 
ATOM   3711 C  CD1 . ILE B 1 2   ? -1.011  -57.394 26.531  1.00 40.92 ? 2   ILE B CD1 1 
ATOM   3712 N  N   . LYS B 1 3   ? 3.214   -56.347 28.840  1.00 35.36 ? 3   LYS B N   1 
ATOM   3713 C  CA  . LYS B 1 3   ? 4.408   -55.886 29.581  1.00 36.29 ? 3   LYS B CA  1 
ATOM   3714 C  C   . LYS B 1 3   ? 4.016   -54.651 30.388  1.00 33.43 ? 3   LYS B C   1 
ATOM   3715 O  O   . LYS B 1 3   ? 3.087   -53.923 29.935  1.00 32.57 ? 3   LYS B O   1 
ATOM   3716 C  CB  . LYS B 1 3   ? 5.530   -55.540 28.605  1.00 39.99 ? 3   LYS B CB  1 
ATOM   3717 C  CG  . LYS B 1 3   ? 5.830   -56.610 27.562  1.00 45.35 ? 3   LYS B CG  1 
ATOM   3718 C  CD  . LYS B 1 3   ? 7.216   -56.496 26.955  1.00 49.93 ? 3   LYS B CD  1 
ATOM   3719 C  CE  . LYS B 1 3   ? 7.741   -55.077 26.929  1.00 49.51 ? 3   LYS B CE  1 
ATOM   3720 N  NZ  . LYS B 1 3   ? 9.108   -55.018 26.360  1.00 57.19 ? 3   LYS B NZ  1 
ATOM   3721 N  N   . GLU B 1 4   ? 4.652   -54.436 31.547  1.00 30.26 ? 4   GLU B N   1 
ATOM   3722 C  CA  . GLU B 1 4   ? 4.493   -53.166 32.283  1.00 31.70 ? 4   GLU B CA  1 
ATOM   3723 C  C   . GLU B 1 4   ? 5.370   -52.136 31.562  1.00 27.26 ? 4   GLU B C   1 
ATOM   3724 O  O   . GLU B 1 4   ? 6.463   -52.491 31.071  1.00 29.26 ? 4   GLU B O   1 
ATOM   3725 C  CB  . GLU B 1 4   ? 4.837   -53.307 33.768  1.00 36.63 ? 4   GLU B CB  1 
ATOM   3726 C  CG  . GLU B 1 4   ? 5.250   -51.992 34.414  1.00 44.53 ? 4   GLU B CG  1 
ATOM   3727 C  CD  . GLU B 1 4   ? 5.087   -51.875 35.928  1.00 49.75 ? 4   GLU B CD  1 
ATOM   3728 O  OE1 . GLU B 1 4   ? 6.096   -52.060 36.653  1.00 55.82 ? 4   GLU B OE1 1 
ATOM   3729 O  OE2 . GLU B 1 4   ? 3.970   -51.534 36.385  1.00 59.59 ? 4   GLU B OE2 1 
ATOM   3730 N  N   . MET B 1 5   ? 4.911   -50.903 31.510  1.00 25.29 ? 5   MET B N   1 
ATOM   3731 C  CA  . MET B 1 5   ? 5.735   -49.871 30.870  1.00 23.84 ? 5   MET B CA  1 
ATOM   3732 C  C   . MET B 1 5   ? 6.630   -49.225 31.922  1.00 19.83 ? 5   MET B C   1 
ATOM   3733 O  O   . MET B 1 5   ? 6.248   -49.068 33.072  1.00 20.09 ? 5   MET B O   1 
ATOM   3734 C  CB  . MET B 1 5   ? 4.893   -48.866 30.086  1.00 27.73 ? 5   MET B CB  1 
ATOM   3735 C  CG  . MET B 1 5   ? 4.151   -47.841 30.827  1.00 25.78 ? 5   MET B CG  1 
ATOM   3736 S  SD  . MET B 1 5   ? 3.250   -46.895 29.532  1.00 24.61 ? 5   MET B SD  1 
ATOM   3737 C  CE  . MET B 1 5   ? 2.258   -48.188 28.810  1.00 27.19 ? 5   MET B CE  1 
ATOM   3738 N  N   . PRO B 1 6   ? 7.808   -48.743 31.500  1.00 18.09 ? 6   PRO B N   1 
ATOM   3739 C  CA  . PRO B 1 6   ? 8.717   -48.026 32.373  1.00 16.94 ? 6   PRO B CA  1 
ATOM   3740 C  C   . PRO B 1 6   ? 8.118   -46.716 32.848  1.00 16.08 ? 6   PRO B C   1 
ATOM   3741 O  O   . PRO B 1 6   ? 7.191   -46.205 32.234  1.00 16.68 ? 6   PRO B O   1 
ATOM   3742 C  CB  . PRO B 1 6   ? 9.946   -47.755 31.463  1.00 19.54 ? 6   PRO B CB  1 
ATOM   3743 C  CG  . PRO B 1 6   ? 9.790   -48.672 30.312  1.00 22.39 ? 6   PRO B CG  1 
ATOM   3744 C  CD  . PRO B 1 6   ? 8.326   -48.907 30.142  1.00 20.71 ? 6   PRO B CD  1 
ATOM   3745 N  N   . GLN B 1 7   ? 8.647   -46.165 33.930  1.00 15.24 ? 7   GLN B N   1 
ATOM   3746 C  CA  . GLN B 1 7   ? 8.134   -44.930 34.530  1.00 16.22 ? 7   GLN B CA  1 
ATOM   3747 C  C   . GLN B 1 7   ? 9.339   -44.178 35.082  1.00 16.19 ? 7   GLN B C   1 
ATOM   3748 O  O   . GLN B 1 7   ? 10.209  -44.797 35.715  1.00 17.54 ? 7   GLN B O   1 
ATOM   3749 C  CB  . GLN B 1 7   ? 7.115   -45.230 35.621  1.00 16.98 ? 7   GLN B CB  1 
ATOM   3750 C  CG  . GLN B 1 7   ? 6.635   -43.973 36.319  1.00 17.86 ? 7   GLN B CG  1 
ATOM   3751 C  CD  . GLN B 1 7   ? 5.576   -44.267 37.351  1.00 20.94 ? 7   GLN B CD  1 
ATOM   3752 O  OE1 . GLN B 1 7   ? 5.389   -45.402 37.759  1.00 25.90 ? 7   GLN B OE1 1 
ATOM   3753 N  NE2 . GLN B 1 7   ? 4.942   -43.231 37.855  1.00 18.89 ? 7   GLN B NE2 1 
ATOM   3754 N  N   . PRO B 1 8   ? 9.470   -42.865 34.862  1.00 14.79 ? 8   PRO B N   1 
ATOM   3755 C  CA  . PRO B 1 8   ? 10.564  -42.086 35.423  1.00 13.82 ? 8   PRO B CA  1 
ATOM   3756 C  C   . PRO B 1 8   ? 10.419  -41.914 36.938  1.00 13.90 ? 8   PRO B C   1 
ATOM   3757 O  O   . PRO B 1 8   ? 9.434   -42.350 37.545  1.00 14.25 ? 8   PRO B O   1 
ATOM   3758 C  CB  . PRO B 1 8   ? 10.543  -40.744 34.651  1.00 14.06 ? 8   PRO B CB  1 
ATOM   3759 C  CG  . PRO B 1 8   ? 9.077   -40.628 34.244  1.00 14.90 ? 8   PRO B CG  1 
ATOM   3760 C  CD  . PRO B 1 8   ? 8.600   -42.039 33.983  1.00 15.14 ? 8   PRO B CD  1 
ATOM   3761 N  N   . LYS B 1 9   ? 11.464  -41.331 37.516  1.00 13.98 ? 9   LYS B N   1 
ATOM   3762 C  CA  . LYS B 1 9   ? 11.574  -41.193 39.004  1.00 14.04 ? 9   LYS B CA  1 
ATOM   3763 C  C   . LYS B 1 9   ? 10.371  -40.452 39.582  1.00 14.19 ? 9   LYS B C   1 
ATOM   3764 O  O   . LYS B 1 9   ? 9.858   -39.477 38.988  1.00 14.73 ? 9   LYS B O   1 
ATOM   3765 C  CB  . LYS B 1 9   ? 12.889  -40.512 39.360  1.00 13.79 ? 9   LYS B CB  1 
ATOM   3766 C  CG  . LYS B 1 9   ? 13.031  -39.064 38.895  1.00 13.48 ? 9   LYS B CG  1 
ATOM   3767 C  CD  . LYS B 1 9   ? 14.475  -38.577 38.984  1.00 17.12 ? 9   LYS B CD  1 
ATOM   3768 C  CE  . LYS B 1 9   ? 14.649  -37.164 38.505  1.00 20.89 ? 9   LYS B CE  1 
ATOM   3769 N  NZ  . LYS B 1 9   ? 16.090  -36.795 38.413  1.00 22.54 ? 9   LYS B NZ  1 
ATOM   3770 N  N   . THR B 1 10  ? 9.934   -40.905 40.750  1.00 14.88 ? 10  THR B N   1 
ATOM   3771 C  CA  . THR B 1 10  ? 8.755   -40.374 41.464  1.00 14.67 ? 10  THR B CA  1 
ATOM   3772 C  C   . THR B 1 10  ? 9.156   -39.628 42.739  1.00 14.36 ? 10  THR B C   1 
ATOM   3773 O  O   . THR B 1 10  ? 10.314  -39.746 43.224  1.00 14.25 ? 10  THR B O   1 
ATOM   3774 C  CB  . THR B 1 10  ? 7.769   -41.489 41.818  1.00 15.18 ? 10  THR B CB  1 
ATOM   3775 O  OG1 . THR B 1 10  ? 8.491   -42.431 42.609  1.00 18.65 ? 10  THR B OG1 1 
ATOM   3776 C  CG2 . THR B 1 10  ? 7.217   -42.152 40.591  1.00 17.47 ? 10  THR B CG2 1 
ATOM   3777 N  N   . PHE B 1 11  ? 8.225   -38.806 43.202  1.00 14.91 ? 11  PHE B N   1 
ATOM   3778 C  CA  . PHE B 1 11  ? 8.363   -37.830 44.311  1.00 15.33 ? 11  PHE B CA  1 
ATOM   3779 C  C   . PHE B 1 11  ? 7.232   -38.116 45.312  1.00 15.93 ? 11  PHE B C   1 
ATOM   3780 O  O   . PHE B 1 11  ? 6.413   -37.201 45.613  1.00 17.81 ? 11  PHE B O   1 
ATOM   3781 C  CB  . PHE B 1 11  ? 8.326   -36.399 43.755  1.00 16.34 ? 11  PHE B CB  1 
ATOM   3782 C  CG  . PHE B 1 11  ? 9.450   -36.025 42.832  1.00 14.67 ? 11  PHE B CG  1 
ATOM   3783 C  CD1 . PHE B 1 11  ? 9.447   -36.496 41.520  1.00 15.11 ? 11  PHE B CD1 1 
ATOM   3784 C  CD2 . PHE B 1 11  ? 10.481  -35.221 43.243  1.00 14.96 ? 11  PHE B CD2 1 
ATOM   3785 C  CE1 . PHE B 1 11  ? 10.490  -36.206 40.646  1.00 15.53 ? 11  PHE B CE1 1 
ATOM   3786 C  CE2 . PHE B 1 11  ? 11.513  -34.897 42.360  1.00 14.68 ? 11  PHE B CE2 1 
ATOM   3787 C  CZ  . PHE B 1 11  ? 11.529  -35.405 41.079  1.00 15.22 ? 11  PHE B CZ  1 
ATOM   3788 N  N   . GLY B 1 12  ? 7.170   -39.356 45.790  1.00 17.01 ? 12  GLY B N   1 
ATOM   3789 C  CA  . GLY B 1 12  ? 6.123   -39.816 46.718  1.00 20.77 ? 12  GLY B CA  1 
ATOM   3790 C  C   . GLY B 1 12  ? 4.751   -39.473 46.180  1.00 20.76 ? 12  GLY B C   1 
ATOM   3791 O  O   . GLY B 1 12  ? 4.453   -39.807 45.018  1.00 19.42 ? 12  GLY B O   1 
ATOM   3792 N  N   . GLU B 1 13  ? 3.915   -38.782 46.952  1.00 21.67 ? 13  GLU B N   1 
ATOM   3793 C  CA  . GLU B 1 13  ? 2.502   -38.563 46.559  1.00 26.23 ? 13  GLU B CA  1 
ATOM   3794 C  C   . GLU B 1 13  ? 2.407   -37.575 45.391  1.00 21.45 ? 13  GLU B C   1 
ATOM   3795 O  O   . GLU B 1 13  ? 1.340   -37.551 44.765  1.00 24.38 ? 13  GLU B O   1 
ATOM   3796 C  CB  . GLU B 1 13  ? 1.673   -38.163 47.785  1.00 30.63 ? 13  GLU B CB  1 
ATOM   3797 C  CG  . GLU B 1 13  ? 1.411   -39.376 48.697  1.00 35.19 ? 13  GLU B CG  1 
ATOM   3798 C  CD  . GLU B 1 13  ? 0.721   -40.582 48.044  1.00 43.94 ? 13  GLU B CD  1 
ATOM   3799 O  OE1 . GLU B 1 13  ? -0.389  -40.413 47.503  1.00 48.15 ? 13  GLU B OE1 1 
ATOM   3800 O  OE2 . GLU B 1 13  ? 1.310   -41.706 48.039  1.00 49.38 ? 13  GLU B OE2 1 
ATOM   3801 N  N   . LEU B 1 14  ? 3.476   -36.840 45.031  1.00 18.96 ? 14  LEU B N   1 
ATOM   3802 C  CA  . LEU B 1 14  ? 3.428   -35.978 43.832  1.00 19.30 ? 14  LEU B CA  1 
ATOM   3803 C  C   . LEU B 1 14  ? 3.735   -36.811 42.573  1.00 18.26 ? 14  LEU B C   1 
ATOM   3804 O  O   . LEU B 1 14  ? 3.598   -36.274 41.473  1.00 17.76 ? 14  LEU B O   1 
ATOM   3805 C  CB  . LEU B 1 14  ? 4.383   -34.798 44.001  1.00 20.89 ? 14  LEU B CB  1 
ATOM   3806 C  CG  . LEU B 1 14  ? 4.015   -33.748 45.059  1.00 22.99 ? 14  LEU B CG  1 
ATOM   3807 C  CD1 . LEU B 1 14  ? 5.071   -32.637 45.108  1.00 25.72 ? 14  LEU B CD1 1 
ATOM   3808 C  CD2 . LEU B 1 14  ? 2.619   -33.158 44.815  1.00 28.19 ? 14  LEU B CD2 1 
ATOM   3809 N  N   . LYS B 1 15  ? 4.021   -38.094 42.707  1.00 17.14 ? 15  LYS B N   1 
ATOM   3810 C  CA  . LYS B 1 15  ? 4.244   -39.006 41.560  1.00 16.10 ? 15  LYS B CA  1 
ATOM   3811 C  C   . LYS B 1 15  ? 5.335   -38.405 40.655  1.00 16.15 ? 15  LYS B C   1 
ATOM   3812 O  O   . LYS B 1 15  ? 6.388   -38.010 41.181  1.00 15.71 ? 15  LYS B O   1 
ATOM   3813 C  CB  . LYS B 1 15  ? 2.896   -39.330 40.919  1.00 20.53 ? 15  LYS B CB  1 
ATOM   3814 C  CG  . LYS B 1 15  ? 1.938   -39.927 41.965  1.00 21.35 ? 15  LYS B CG  1 
ATOM   3815 C  CD  . LYS B 1 15  ? 0.594   -40.280 41.444  1.00 26.37 ? 15  LYS B CD  1 
ATOM   3816 C  CE  . LYS B 1 15  ? -0.057  -41.331 42.321  1.00 30.43 ? 15  LYS B CE  1 
ATOM   3817 N  NZ  . LYS B 1 15  ? -1.266  -41.844 41.655  1.00 36.83 ? 15  LYS B NZ  1 
ATOM   3818 N  N   . ASN B 1 16  ? 5.099   -38.275 39.350  1.00 13.96 ? 16  ASN B N   1 
ATOM   3819 C  CA  . ASN B 1 16  ? 6.109   -37.703 38.436  1.00 14.59 ? 16  ASN B CA  1 
ATOM   3820 C  C   . ASN B 1 16  ? 5.965   -36.190 38.280  1.00 14.25 ? 16  ASN B C   1 
ATOM   3821 O  O   . ASN B 1 16  ? 6.771   -35.612 37.526  1.00 14.37 ? 16  ASN B O   1 
ATOM   3822 C  CB  . ASN B 1 16  ? 5.990   -38.368 37.067  1.00 12.91 ? 16  ASN B CB  1 
ATOM   3823 C  CG  . ASN B 1 16  ? 6.271   -39.854 37.092  1.00 14.98 ? 16  ASN B CG  1 
ATOM   3824 O  OD1 . ASN B 1 16  ? 5.446   -40.673 36.673  1.00 14.15 ? 16  ASN B OD1 1 
ATOM   3825 N  ND2 . ASN B 1 16  ? 7.450   -40.249 37.631  1.00 15.61 ? 16  ASN B ND2 1 
ATOM   3826 N  N   . LEU B 1 17  ? 4.901   -35.570 38.798  1.00 15.59 ? 17  LEU B N   1 
ATOM   3827 C  CA  . LEU B 1 17  ? 4.596   -34.155 38.463  1.00 16.12 ? 17  LEU B CA  1 
ATOM   3828 C  C   . LEU B 1 17  ? 5.797   -33.230 38.618  1.00 15.94 ? 17  LEU B C   1 
ATOM   3829 O  O   . LEU B 1 17  ? 5.983   -32.336 37.779  1.00 16.00 ? 17  LEU B O   1 
ATOM   3830 C  CB  . LEU B 1 17  ? 3.446   -33.647 39.329  1.00 19.90 ? 17  LEU B CB  1 
ATOM   3831 C  CG  . LEU B 1 17  ? 2.970   -32.244 38.967  1.00 22.49 ? 17  LEU B CG  1 
ATOM   3832 C  CD1 . LEU B 1 17  ? 2.439   -32.188 37.573  1.00 22.54 ? 17  LEU B CD1 1 
ATOM   3833 C  CD2 . LEU B 1 17  ? 1.894   -31.777 39.935  1.00 25.33 ? 17  LEU B CD2 1 
ATOM   3834 N  N   . PRO B 1 18  ? 6.669   -33.336 39.643  1.00 13.96 ? 18  PRO B N   1 
ATOM   3835 C  CA  . PRO B 1 18  ? 7.793   -32.393 39.769  1.00 15.31 ? 18  PRO B CA  1 
ATOM   3836 C  C   . PRO B 1 18  ? 8.749   -32.430 38.568  1.00 14.77 ? 18  PRO B C   1 
ATOM   3837 O  O   . PRO B 1 18  ? 9.518   -31.470 38.444  1.00 16.68 ? 18  PRO B O   1 
ATOM   3838 C  CB  . PRO B 1 18  ? 8.482   -32.788 41.101  1.00 15.55 ? 18  PRO B CB  1 
ATOM   3839 C  CG  . PRO B 1 18  ? 7.326   -33.396 41.859  1.00 15.62 ? 18  PRO B CG  1 
ATOM   3840 C  CD  . PRO B 1 18  ? 6.573   -34.204 40.825  1.00 15.13 ? 18  PRO B CD  1 
ATOM   3841 N  N   . LEU B 1 19  ? 8.756   -33.482 37.760  1.00 15.70 ? 19  LEU B N   1 
ATOM   3842 C  CA  . LEU B 1 19  ? 9.623   -33.478 36.546  1.00 14.61 ? 19  LEU B CA  1 
ATOM   3843 C  C   . LEU B 1 19  ? 9.206   -32.401 35.546  1.00 16.11 ? 19  LEU B C   1 
ATOM   3844 O  O   . LEU B 1 19  ? 10.073  -32.068 34.706  1.00 17.12 ? 19  LEU B O   1 
ATOM   3845 C  CB  . LEU B 1 19  ? 9.589   -34.863 35.923  1.00 15.18 ? 19  LEU B CB  1 
ATOM   3846 C  CG  . LEU B 1 19  ? 10.116  -35.978 36.833  1.00 15.35 ? 19  LEU B CG  1 
ATOM   3847 C  CD1 . LEU B 1 19  ? 9.975   -37.340 36.181  1.00 16.38 ? 19  LEU B CD1 1 
ATOM   3848 C  CD2 . LEU B 1 19  ? 11.561  -35.745 37.258  1.00 16.52 ? 19  LEU B CD2 1 
ATOM   3849 N  N   . LEU B 1 20  ? 7.978   -31.891 35.644  1.00 15.22 ? 20  LEU B N   1 
ATOM   3850 C  CA  . LEU B 1 20  ? 7.528   -30.805 34.726  1.00 17.28 ? 20  LEU B CA  1 
ATOM   3851 C  C   . LEU B 1 20  ? 7.756   -29.442 35.374  1.00 18.89 ? 20  LEU B C   1 
ATOM   3852 O  O   . LEU B 1 20  ? 7.497   -28.426 34.698  1.00 19.48 ? 20  LEU B O   1 
ATOM   3853 C  CB  . LEU B 1 20  ? 6.050   -30.998 34.396  1.00 20.60 ? 20  LEU B CB  1 
ATOM   3854 C  CG  . LEU B 1 20  ? 5.751   -32.285 33.645  1.00 23.66 ? 20  LEU B CG  1 
ATOM   3855 C  CD1 . LEU B 1 20  ? 4.238   -32.450 33.512  1.00 29.60 ? 20  LEU B CD1 1 
ATOM   3856 C  CD2 . LEU B 1 20  ? 6.456   -32.387 32.332  1.00 26.97 ? 20  LEU B CD2 1 
ATOM   3857 N  N   . ASN B 1 21  ? 8.331   -29.382 36.568  1.00 16.68 ? 21  ASN B N   1 
ATOM   3858 C  CA  . ASN B 1 21  ? 8.676   -28.098 37.215  1.00 19.03 ? 21  ASN B CA  1 
ATOM   3859 C  C   . ASN B 1 21  ? 10.032  -27.654 36.692  1.00 19.47 ? 21  ASN B C   1 
ATOM   3860 O  O   . ASN B 1 21  ? 11.027  -27.712 37.415  1.00 20.68 ? 21  ASN B O   1 
ATOM   3861 C  CB  . ASN B 1 21  ? 8.651   -28.191 38.750  1.00 20.14 ? 21  ASN B CB  1 
ATOM   3862 C  CG  . ASN B 1 21  ? 8.811   -26.838 39.397  1.00 25.16 ? 21  ASN B CG  1 
ATOM   3863 O  OD1 . ASN B 1 21  ? 8.863   -25.807 38.717  1.00 29.39 ? 21  ASN B OD1 1 
ATOM   3864 N  ND2 . ASN B 1 21  ? 8.906   -26.827 40.713  1.00 30.46 ? 21  ASN B ND2 1 
ATOM   3865 N  N   . THR B 1 22  ? 10.046  -27.232 35.424  1.00 18.68 ? 22  THR B N   1 
ATOM   3866 C  CA  . THR B 1 22  ? 11.246  -26.831 34.651  1.00 19.11 ? 22  THR B CA  1 
ATOM   3867 C  C   . THR B 1 22  ? 10.769  -25.872 33.560  1.00 19.37 ? 22  THR B C   1 
ATOM   3868 O  O   . THR B 1 22  ? 9.596   -25.999 33.136  1.00 22.09 ? 22  THR B O   1 
ATOM   3869 C  CB  . THR B 1 22  ? 11.953  -28.025 34.018  1.00 18.51 ? 22  THR B CB  1 
ATOM   3870 O  OG1 . THR B 1 22  ? 12.983  -27.525 33.145  1.00 20.73 ? 22  THR B OG1 1 
ATOM   3871 C  CG2 . THR B 1 22  ? 10.990  -28.901 33.251  1.00 16.90 ? 22  THR B CG2 1 
ATOM   3872 N  N   . ASP B 1 23  ? 11.614  -24.939 33.112  1.00 19.73 ? 23  ASP B N   1 
ATOM   3873 C  CA  . ASP B 1 23  ? 11.184  -24.128 31.952  1.00 21.90 ? 23  ASP B CA  1 
ATOM   3874 C  C   . ASP B 1 23  ? 11.469  -24.890 30.654  1.00 18.64 ? 23  ASP B C   1 
ATOM   3875 O  O   . ASP B 1 23  ? 11.095  -24.313 29.651  1.00 18.67 ? 23  ASP B O   1 
ATOM   3876 C  CB  . ASP B 1 23  ? 11.783  -22.717 31.952  1.00 27.08 ? 23  ASP B CB  1 
ATOM   3877 C  CG  . ASP B 1 23  ? 13.253  -22.663 32.239  1.00 33.57 ? 23  ASP B CG  1 
ATOM   3878 O  OD1 . ASP B 1 23  ? 13.927  -23.678 32.056  1.00 29.33 ? 23  ASP B OD1 1 
ATOM   3879 O  OD2 . ASP B 1 23  ? 13.698  -21.573 32.708  1.00 49.17 ? 23  ASP B OD2 1 
ATOM   3880 N  N   . LYS B 1 24  ? 12.045  -26.105 30.660  1.00 16.41 ? 24  LYS B N   1 
ATOM   3881 C  CA  . LYS B 1 24  ? 12.330  -26.879 29.403  1.00 14.71 ? 24  LYS B CA  1 
ATOM   3882 C  C   . LYS B 1 24  ? 11.735  -28.287 29.525  1.00 13.30 ? 24  LYS B C   1 
ATOM   3883 O  O   . LYS B 1 24  ? 12.462  -29.271 29.486  1.00 14.95 ? 24  LYS B O   1 
ATOM   3884 C  CB  . LYS B 1 24  ? 13.821  -26.931 29.063  1.00 15.58 ? 24  LYS B CB  1 
ATOM   3885 C  CG  . LYS B 1 24  ? 14.462  -25.561 28.812  1.00 17.04 ? 24  LYS B CG  1 
ATOM   3886 C  CD  . LYS B 1 24  ? 15.920  -25.579 28.535  1.00 16.77 ? 24  LYS B CD  1 
ATOM   3887 C  CE  . LYS B 1 24  ? 16.517  -24.206 28.228  1.00 20.24 ? 24  LYS B CE  1 
ATOM   3888 N  NZ  . LYS B 1 24  ? 17.936  -24.308 27.880  1.00 21.44 ? 24  LYS B NZ  1 
ATOM   3889 N  N   . PRO B 1 25  ? 10.398  -28.396 29.649  1.00 13.73 ? 25  PRO B N   1 
ATOM   3890 C  CA  . PRO B 1 25  ? 9.796   -29.711 29.881  1.00 15.19 ? 25  PRO B CA  1 
ATOM   3891 C  C   . PRO B 1 25  ? 9.961   -30.697 28.733  1.00 14.11 ? 25  PRO B C   1 
ATOM   3892 O  O   . PRO B 1 25  ? 10.180  -31.871 28.923  1.00 14.27 ? 25  PRO B O   1 
ATOM   3893 C  CB  . PRO B 1 25  ? 8.337   -29.372 30.208  1.00 15.98 ? 25  PRO B CB  1 
ATOM   3894 C  CG  . PRO B 1 25  ? 8.094   -28.052 29.513  1.00 16.66 ? 25  PRO B CG  1 
ATOM   3895 C  CD  . PRO B 1 25  ? 9.404   -27.317 29.728  1.00 15.26 ? 25  PRO B CD  1 
ATOM   3896 N  N   . VAL B 1 26  ? 9.802   -30.230 27.500  1.00 13.48 ? 26  VAL B N   1 
ATOM   3897 C  CA  . VAL B 1 26  ? 9.981   -31.137 26.341  1.00 14.45 ? 26  VAL B CA  1 
ATOM   3898 C  C   . VAL B 1 26  ? 11.405  -31.696 26.309  1.00 13.42 ? 26  VAL B C   1 
ATOM   3899 O  O   . VAL B 1 26  ? 11.596  -32.870 26.036  1.00 13.87 ? 26  VAL B O   1 
ATOM   3900 C  CB  . VAL B 1 26  ? 9.615   -30.402 25.036  1.00 15.50 ? 26  VAL B CB  1 
ATOM   3901 C  CG1 . VAL B 1 26  ? 9.998   -31.215 23.822  1.00 17.43 ? 26  VAL B CG1 1 
ATOM   3902 C  CG2 . VAL B 1 26  ? 8.105   -30.115 25.019  1.00 17.16 ? 26  VAL B CG2 1 
ATOM   3903 N  N   . GLN B 1 27  ? 12.411  -30.858 26.511  1.00 13.87 ? 27  GLN B N   1 
ATOM   3904 C  CA  . GLN B 1 27  ? 13.805  -31.352 26.491  1.00 13.81 ? 27  GLN B CA  1 
ATOM   3905 C  C   . GLN B 1 27  ? 14.021  -32.303 27.679  1.00 12.82 ? 27  GLN B C   1 
ATOM   3906 O  O   . GLN B 1 27  ? 14.739  -33.315 27.497  1.00 15.45 ? 27  GLN B O   1 
ATOM   3907 C  CB  . GLN B 1 27  ? 14.734  -30.144 26.500  1.00 13.00 ? 27  GLN B CB  1 
ATOM   3908 C  CG  . GLN B 1 27  ? 14.740  -29.410 25.160  1.00 13.93 ? 27  GLN B CG  1 
ATOM   3909 C  CD  . GLN B 1 27  ? 15.268  -28.006 25.265  1.00 14.21 ? 27  GLN B CD  1 
ATOM   3910 O  OE1 . GLN B 1 27  ? 14.537  -27.035 25.475  1.00 16.33 ? 27  GLN B OE1 1 
ATOM   3911 N  NE2 . GLN B 1 27  ? 16.549  -27.922 25.096  1.00 15.20 ? 27  GLN B NE2 1 
ATOM   3912 N  N   . ALA B 1 28  ? 13.325  -32.056 28.789  1.00 14.14 ? 28  ALA B N   1 
ATOM   3913 C  CA  . ALA B 1 28  ? 13.400  -33.001 29.933  1.00 13.68 ? 28  ALA B CA  1 
ATOM   3914 C  C   . ALA B 1 28  ? 12.769  -34.361 29.558  1.00 13.13 ? 28  ALA B C   1 
ATOM   3915 O  O   . ALA B 1 28  ? 13.345  -35.473 29.847  1.00 14.19 ? 28  ALA B O   1 
ATOM   3916 C  CB  . ALA B 1 28  ? 12.758  -32.408 31.158  1.00 14.41 ? 28  ALA B CB  1 
ATOM   3917 N  N   . LEU B 1 29  ? 11.626  -34.315 28.864  1.00 12.17 ? 29  LEU B N   1 
ATOM   3918 C  CA  . LEU B 1 29  ? 10.940  -35.554 28.435  1.00 13.31 ? 29  LEU B CA  1 
ATOM   3919 C  C   . LEU B 1 29  ? 11.758  -36.304 27.378  1.00 13.11 ? 29  LEU B C   1 
ATOM   3920 O  O   . LEU B 1 29  ? 11.719  -37.536 27.329  1.00 13.52 ? 29  LEU B O   1 
ATOM   3921 C  CB  . LEU B 1 29  ? 9.541   -35.184 27.953  1.00 12.71 ? 29  LEU B CB  1 
ATOM   3922 C  CG  . LEU B 1 29  ? 8.568   -34.778 29.059  1.00 13.67 ? 29  LEU B CG  1 
ATOM   3923 C  CD1 . LEU B 1 29  ? 7.378   -33.989 28.501  1.00 14.89 ? 29  LEU B CD1 1 
ATOM   3924 C  CD2 . LEU B 1 29  ? 8.049   -35.977 29.855  1.00 13.39 ? 29  LEU B CD2 1 
ATOM   3925 N  N   . MET B 1 30  ? 12.434  -35.572 26.502  1.00 12.34 ? 30  MET B N   1 
ATOM   3926 C  CA  . MET B 1 30  ? 13.322  -36.217 25.494  1.00 14.62 ? 30  MET B CA  1 
ATOM   3927 C  C   . MET B 1 30  ? 14.440  -37.011 26.178  1.00 12.72 ? 30  MET B C   1 
ATOM   3928 O  O   . MET B 1 30  ? 14.711  -38.113 25.814  1.00 13.20 ? 30  MET B O   1 
ATOM   3929 C  CB  . MET B 1 30  ? 13.983  -35.193 24.585  1.00 14.23 ? 30  MET B CB  1 
ATOM   3930 C  CG  . MET B 1 30  ? 12.973  -34.604 23.551  1.00 13.86 ? 30  MET B CG  1 
ATOM   3931 S  SD  . MET B 1 30  ? 13.632  -33.171 22.699  1.00 16.32 ? 30  MET B SD  1 
ATOM   3932 C  CE  . MET B 1 30  ? 14.902  -33.994 21.766  1.00 17.11 ? 30  MET B CE  1 
ATOM   3933 N  N   . LYS B 1 31  ? 14.960  -36.480 27.288  1.00 14.95 ? 31  LYS B N   1 
ATOM   3934 C  CA  . LYS B 1 31  ? 16.075  -37.157 27.995  1.00 15.56 ? 31  LYS B CA  1 
ATOM   3935 C  C   . LYS B 1 31  ? 15.491  -38.380 28.710  1.00 14.39 ? 31  LYS B C   1 
ATOM   3936 O  O   . LYS B 1 31  ? 16.107  -39.440 28.740  1.00 15.10 ? 31  LYS B O   1 
ATOM   3937 C  CB  . LYS B 1 31  ? 16.778  -36.164 28.908  1.00 20.41 ? 31  LYS B CB  1 
ATOM   3938 C  CG  . LYS B 1 31  ? 17.732  -35.228 28.183  1.00 26.35 ? 31  LYS B CG  1 
ATOM   3939 C  CD  . LYS B 1 31  ? 18.573  -34.376 29.141  1.00 35.72 ? 31  LYS B CD  1 
ATOM   3940 C  CE  . LYS B 1 31  ? 18.848  -32.969 28.638  1.00 43.62 ? 31  LYS B CE  1 
ATOM   3941 N  NZ  . LYS B 1 31  ? 20.210  -32.515 29.016  1.00 45.95 ? 31  LYS B NZ  1 
ATOM   3942 N  N   . ILE B 1 32  ? 14.282  -38.249 29.255  1.00 13.72 ? 32  ILE B N   1 
ATOM   3943 C  CA  . ILE B 1 32  ? 13.606  -39.412 29.867  1.00 12.85 ? 32  ILE B CA  1 
ATOM   3944 C  C   . ILE B 1 32  ? 13.420  -40.482 28.810  1.00 14.64 ? 32  ILE B C   1 
ATOM   3945 O  O   . ILE B 1 32  ? 13.657  -41.673 29.075  1.00 13.90 ? 32  ILE B O   1 
ATOM   3946 C  CB  . ILE B 1 32  ? 12.302  -39.033 30.587  1.00 14.44 ? 32  ILE B CB  1 
ATOM   3947 C  CG1 . ILE B 1 32  ? 12.631  -38.185 31.825  1.00 14.75 ? 32  ILE B CG1 1 
ATOM   3948 C  CG2 . ILE B 1 32  ? 11.474  -40.258 30.960  1.00 13.87 ? 32  ILE B CG2 1 
ATOM   3949 C  CD1 . ILE B 1 32  ? 11.455  -37.466 32.376  1.00 15.40 ? 32  ILE B CD1 1 
ATOM   3950 N  N   . ALA B 1 33  ? 12.906  -40.107 27.649  1.00 13.05 ? 33  ALA B N   1 
ATOM   3951 C  CA  . ALA B 1 33  ? 12.745  -41.093 26.575  1.00 14.37 ? 33  ALA B CA  1 
ATOM   3952 C  C   . ALA B 1 33  ? 14.064  -41.745 26.169  1.00 14.83 ? 33  ALA B C   1 
ATOM   3953 O  O   . ALA B 1 33  ? 14.058  -42.981 25.922  1.00 15.59 ? 33  ALA B O   1 
ATOM   3954 C  CB  . ALA B 1 33  ? 12.099  -40.366 25.410  1.00 14.41 ? 33  ALA B CB  1 
ATOM   3955 N  N   . ASP B 1 34  ? 15.152  -40.990 26.109  1.00 15.89 ? 34  ASP B N   1 
ATOM   3956 C  CA  . ASP B 1 34  ? 16.476  -41.607 25.833  1.00 17.34 ? 34  ASP B CA  1 
ATOM   3957 C  C   . ASP B 1 34  ? 16.783  -42.696 26.871  1.00 16.78 ? 34  ASP B C   1 
ATOM   3958 O  O   . ASP B 1 34  ? 17.401  -43.686 26.517  1.00 20.33 ? 34  ASP B O   1 
ATOM   3959 C  CB  . ASP B 1 34  ? 17.553  -40.531 25.792  1.00 18.80 ? 34  ASP B CB  1 
ATOM   3960 C  CG  . ASP B 1 34  ? 17.538  -39.699 24.538  1.00 21.57 ? 34  ASP B CG  1 
ATOM   3961 O  OD1 . ASP B 1 34  ? 17.030  -40.197 23.532  1.00 24.81 ? 34  ASP B OD1 1 
ATOM   3962 O  OD2 . ASP B 1 34  ? 17.925  -38.501 24.590  1.00 27.24 ? 34  ASP B OD2 1 
ATOM   3963 N  N   . GLU B 1 35  ? 16.478  -42.443 28.130  1.00 16.41 ? 35  GLU B N   1 
ATOM   3964 C  CA  . GLU B 1 35  ? 16.806  -43.389 29.220  1.00 17.42 ? 35  GLU B CA  1 
ATOM   3965 C  C   . GLU B 1 35  ? 15.829  -44.570 29.162  1.00 17.84 ? 35  GLU B C   1 
ATOM   3966 O  O   . GLU B 1 35  ? 16.244  -45.688 29.467  1.00 20.17 ? 35  GLU B O   1 
ATOM   3967 C  CB  . GLU B 1 35  ? 16.734  -42.661 30.555  1.00 19.46 ? 35  GLU B CB  1 
ATOM   3968 C  CG  . GLU B 1 35  ? 17.761  -41.551 30.746  1.00 23.67 ? 35  GLU B CG  1 
ATOM   3969 C  CD  . GLU B 1 35  ? 17.782  -40.888 32.119  1.00 30.08 ? 35  GLU B CD  1 
ATOM   3970 O  OE1 . GLU B 1 35  ? 17.056  -41.385 33.006  1.00 39.13 ? 35  GLU B OE1 1 
ATOM   3971 O  OE2 . GLU B 1 35  ? 18.553  -39.894 32.326  1.00 32.16 ? 35  GLU B OE2 1 
ATOM   3972 N  N   . LEU B 1 36  ? 14.523  -44.359 28.932  1.00 15.11 ? 36  LEU B N   1 
ATOM   3973 C  CA  . LEU B 1 36  ? 13.524  -45.405 29.201  1.00 15.77 ? 36  LEU B CA  1 
ATOM   3974 C  C   . LEU B 1 36  ? 13.034  -46.083 27.914  1.00 15.02 ? 36  LEU B C   1 
ATOM   3975 O  O   . LEU B 1 36  ? 12.411  -47.118 28.037  1.00 16.58 ? 36  LEU B O   1 
ATOM   3976 C  CB  . LEU B 1 36  ? 12.337  -44.802 29.952  1.00 15.04 ? 36  LEU B CB  1 
ATOM   3977 C  CG  . LEU B 1 36  ? 12.595  -44.173 31.311  1.00 16.36 ? 36  LEU B CG  1 
ATOM   3978 C  CD1 . LEU B 1 36  ? 11.289  -43.785 31.974  1.00 16.51 ? 36  LEU B CD1 1 
ATOM   3979 C  CD2 . LEU B 1 36  ? 13.326  -45.154 32.238  1.00 17.18 ? 36  LEU B CD2 1 
ATOM   3980 N  N   . GLY B 1 37  ? 13.180  -45.455 26.744  1.00 16.05 ? 37  GLY B N   1 
ATOM   3981 C  CA  . GLY B 1 37  ? 12.876  -46.092 25.451  1.00 15.22 ? 37  GLY B CA  1 
ATOM   3982 C  C   . GLY B 1 37  ? 11.567  -45.606 24.833  1.00 15.68 ? 37  GLY B C   1 
ATOM   3983 O  O   . GLY B 1 37  ? 11.168  -44.452 25.042  1.00 15.88 ? 37  GLY B O   1 
ATOM   3984 N  N   . GLU B 1 38  ? 10.964  -46.453 24.039  1.00 15.21 ? 38  GLU B N   1 
ATOM   3985 C  CA  . GLU B 1 38  ? 9.869   -46.088 23.121  1.00 15.25 ? 38  GLU B CA  1 
ATOM   3986 C  C   . GLU B 1 38  ? 8.599   -45.653 23.852  1.00 15.02 ? 38  GLU B C   1 
ATOM   3987 O  O   . GLU B 1 38  ? 7.741   -45.028 23.181  1.00 13.04 ? 38  GLU B O   1 
ATOM   3988 C  CB  . GLU B 1 38  ? 9.585   -47.203 22.140  1.00 17.09 ? 38  GLU B CB  1 
ATOM   3989 C  CG  . GLU B 1 38  ? 9.104   -48.453 22.800  1.00 16.63 ? 38  GLU B CG  1 
ATOM   3990 C  CD  . GLU B 1 38  ? 8.778   -49.558 21.792  1.00 23.58 ? 38  GLU B CD  1 
ATOM   3991 O  OE1 . GLU B 1 38  ? 8.689   -49.296 20.548  1.00 21.64 ? 38  GLU B OE1 1 
ATOM   3992 O  OE2 . GLU B 1 38  ? 8.650   -50.703 22.275  1.00 25.88 ? 38  GLU B OE2 1 
ATOM   3993 N  N   . ILE B 1 39  ? 8.388   -46.014 25.105  1.00 12.94 ? 39  ILE B N   1 
ATOM   3994 C  CA  . ILE B 1 39  ? 7.118   -45.691 25.802  1.00 13.66 ? 39  ILE B CA  1 
ATOM   3995 C  C   . ILE B 1 39  ? 7.419   -45.589 27.277  1.00 14.02 ? 39  ILE B C   1 
ATOM   3996 O  O   . ILE B 1 39  ? 8.167   -46.429 27.796  1.00 16.01 ? 39  ILE B O   1 
ATOM   3997 C  CB  . ILE B 1 39  ? 6.004   -46.703 25.494  1.00 15.34 ? 39  ILE B CB  1 
ATOM   3998 C  CG1 . ILE B 1 39  ? 4.664   -46.234 26.051  1.00 17.19 ? 39  ILE B CG1 1 
ATOM   3999 C  CG2 . ILE B 1 39  ? 6.383   -48.112 25.914  1.00 15.49 ? 39  ILE B CG2 1 
ATOM   4000 C  CD1 . ILE B 1 39  ? 3.492   -47.073 25.587  1.00 19.00 ? 39  ILE B CD1 1 
ATOM   4001 N  N   . PHE B 1 40  ? 6.854   -44.603 27.922  1.00 12.22 ? 40  PHE B N   1 
ATOM   4002 C  CA  . PHE B 1 40  ? 6.888   -44.520 29.400  1.00 12.48 ? 40  PHE B CA  1 
ATOM   4003 C  C   . PHE B 1 40  ? 5.601   -43.914 29.906  1.00 13.44 ? 40  PHE B C   1 
ATOM   4004 O  O   . PHE B 1 40  ? 4.939   -43.134 29.187  1.00 13.65 ? 40  PHE B O   1 
ATOM   4005 C  CB  . PHE B 1 40  ? 8.146   -43.842 29.917  1.00 12.77 ? 40  PHE B CB  1 
ATOM   4006 C  CG  . PHE B 1 40  ? 8.282   -42.391 29.551  1.00 11.68 ? 40  PHE B CG  1 
ATOM   4007 C  CD1 . PHE B 1 40  ? 7.711   -41.379 30.293  1.00 12.22 ? 40  PHE B CD1 1 
ATOM   4008 C  CD2 . PHE B 1 40  ? 9.028   -42.048 28.415  1.00 11.50 ? 40  PHE B CD2 1 
ATOM   4009 C  CE1 . PHE B 1 40  ? 7.911   -40.040 29.921  1.00 12.50 ? 40  PHE B CE1 1 
ATOM   4010 C  CE2 . PHE B 1 40  ? 9.232   -40.713 28.069  1.00 12.06 ? 40  PHE B CE2 1 
ATOM   4011 C  CZ  . PHE B 1 40  ? 8.667   -39.707 28.807  1.00 12.05 ? 40  PHE B CZ  1 
ATOM   4012 N  N   . LYS B 1 41  ? 5.200   -44.348 31.097  1.00 14.10 ? 41  LYS B N   1 
ATOM   4013 C  CA  . LYS B 1 41  ? 4.038   -43.779 31.799  1.00 15.12 ? 41  LYS B CA  1 
ATOM   4014 C  C   . LYS B 1 41  ? 4.491   -42.633 32.667  1.00 15.54 ? 41  LYS B C   1 
ATOM   4015 O  O   . LYS B 1 41  ? 5.555   -42.707 33.267  1.00 16.97 ? 41  LYS B O   1 
ATOM   4016 C  CB  . LYS B 1 41  ? 3.357   -44.894 32.597  1.00 21.25 ? 41  LYS B CB  1 
ATOM   4017 C  CG  . LYS B 1 41  ? 2.323   -44.552 33.651  1.00 27.73 ? 41  LYS B CG  1 
ATOM   4018 C  CD  . LYS B 1 41  ? 2.358   -45.641 34.754  1.00 33.19 ? 41  LYS B CD  1 
ATOM   4019 C  CE  . LYS B 1 41  ? 2.770   -47.015 34.254  1.00 36.55 ? 41  LYS B CE  1 
ATOM   4020 N  NZ  . LYS B 1 41  ? 3.935   -47.600 34.981  1.00 37.80 ? 41  LYS B NZ  1 
ATOM   4021 N  N   . PHE B 1 42  ? 3.732   -41.576 32.660  1.00 14.79 ? 42  PHE B N   1 
ATOM   4022 C  CA  . PHE B 1 42  ? 3.958   -40.350 33.448  1.00 13.45 ? 42  PHE B CA  1 
ATOM   4023 C  C   . PHE B 1 42  ? 2.714   -40.093 34.296  1.00 16.02 ? 42  PHE B C   1 
ATOM   4024 O  O   . PHE B 1 42  ? 1.631   -39.842 33.729  1.00 16.59 ? 42  PHE B O   1 
ATOM   4025 C  CB  . PHE B 1 42  ? 4.254   -39.159 32.543  1.00 14.97 ? 42  PHE B CB  1 
ATOM   4026 C  CG  . PHE B 1 42  ? 4.746   -37.932 33.246  1.00 13.81 ? 42  PHE B CG  1 
ATOM   4027 C  CD1 . PHE B 1 42  ? 3.916   -37.141 34.011  1.00 15.83 ? 42  PHE B CD1 1 
ATOM   4028 C  CD2 . PHE B 1 42  ? 6.091   -37.625 33.183  1.00 15.18 ? 42  PHE B CD2 1 
ATOM   4029 C  CE1 . PHE B 1 42  ? 4.422   -36.015 34.657  1.00 14.89 ? 42  PHE B CE1 1 
ATOM   4030 C  CE2 . PHE B 1 42  ? 6.587   -36.486 33.788  1.00 15.15 ? 42  PHE B CE2 1 
ATOM   4031 C  CZ  . PHE B 1 42  ? 5.750   -35.695 34.531  1.00 15.88 ? 42  PHE B CZ  1 
ATOM   4032 N  N   . GLU B 1 43  ? 2.839   -40.202 35.603  1.00 15.90 ? 43  GLU B N   1 
ATOM   4033 C  CA  . GLU B 1 43  ? 1.670   -40.105 36.526  1.00 16.75 ? 43  GLU B CA  1 
ATOM   4034 C  C   . GLU B 1 43  ? 1.750   -38.780 37.259  1.00 18.67 ? 43  GLU B C   1 
ATOM   4035 O  O   . GLU B 1 43  ? 2.854   -38.383 37.739  1.00 17.39 ? 43  GLU B O   1 
ATOM   4036 C  CB  . GLU B 1 43  ? 1.688   -41.292 37.495  1.00 19.74 ? 43  GLU B CB  1 
ATOM   4037 C  CG  . GLU B 1 43  ? 1.412   -42.606 36.835  1.00 23.52 ? 43  GLU B CG  1 
ATOM   4038 C  CD  . GLU B 1 43  ? 1.400   -43.814 37.763  1.00 30.50 ? 43  GLU B CD  1 
ATOM   4039 O  OE1 . GLU B 1 43  ? 1.881   -43.679 38.902  1.00 33.02 ? 43  GLU B OE1 1 
ATOM   4040 O  OE2 . GLU B 1 43  ? 0.905   -44.875 37.332  1.00 40.49 ? 43  GLU B OE2 1 
ATOM   4041 N  N   . ALA B 1 44  ? 0.602   -38.104 37.401  1.00 19.74 ? 44  ALA B N   1 
ATOM   4042 C  CA  . ALA B 1 44  ? 0.476   -36.954 38.310  1.00 19.41 ? 44  ALA B CA  1 
ATOM   4043 C  C   . ALA B 1 44  ? -0.708  -37.244 39.213  1.00 20.83 ? 44  ALA B C   1 
ATOM   4044 O  O   . ALA B 1 44  ? -1.467  -38.145 38.950  1.00 20.92 ? 44  ALA B O   1 
ATOM   4045 C  CB  . ALA B 1 44  ? 0.308   -35.689 37.527  1.00 22.06 ? 44  ALA B CB  1 
ATOM   4046 N  N   . PRO B 1 45  ? -0.884  -36.558 40.354  1.00 22.69 ? 45  PRO B N   1 
ATOM   4047 C  CA  . PRO B 1 45  ? -2.079  -36.832 41.168  1.00 25.63 ? 45  PRO B CA  1 
ATOM   4048 C  C   . PRO B 1 45  ? -3.382  -36.722 40.332  1.00 26.72 ? 45  PRO B C   1 
ATOM   4049 O  O   . PRO B 1 45  ? -4.198  -37.619 40.418  1.00 29.80 ? 45  PRO B O   1 
ATOM   4050 C  CB  . PRO B 1 45  ? -1.944  -35.849 42.342  1.00 26.97 ? 45  PRO B CB  1 
ATOM   4051 C  CG  . PRO B 1 45  ? -0.450  -35.524 42.378  1.00 24.94 ? 45  PRO B CG  1 
ATOM   4052 C  CD  . PRO B 1 45  ? -0.010  -35.510 40.922  1.00 23.74 ? 45  PRO B CD  1 
ATOM   4053 N  N   . GLY B 1 46  ? -3.511  -35.774 39.410  1.00 27.99 ? 46  GLY B N   1 
ATOM   4054 C  CA  . GLY B 1 46  ? -4.781  -35.655 38.638  1.00 30.94 ? 46  GLY B CA  1 
ATOM   4055 C  C   . GLY B 1 46  ? -4.958  -36.580 37.416  1.00 32.49 ? 46  GLY B C   1 
ATOM   4056 O  O   . GLY B 1 46  ? -6.082  -36.577 36.840  1.00 32.80 ? 46  GLY B O   1 
ATOM   4057 N  N   . TRP B 1 47  ? -3.940  -37.333 36.968  1.00 26.60 ? 47  TRP B N   1 
ATOM   4058 C  CA  . TRP B 1 47  ? -3.928  -37.806 35.551  1.00 22.92 ? 47  TRP B CA  1 
ATOM   4059 C  C   . TRP B 1 47  ? -2.734  -38.715 35.218  1.00 22.14 ? 47  TRP B C   1 
ATOM   4060 O  O   . TRP B 1 47  ? -1.782  -38.755 35.972  1.00 21.49 ? 47  TRP B O   1 
ATOM   4061 C  CB  . TRP B 1 47  ? -3.944  -36.622 34.582  1.00 23.16 ? 47  TRP B CB  1 
ATOM   4062 C  CG  . TRP B 1 47  ? -2.889  -35.568 34.762  1.00 25.09 ? 47  TRP B CG  1 
ATOM   4063 C  CD1 . TRP B 1 47  ? -3.018  -34.380 35.425  1.00 29.54 ? 47  TRP B CD1 1 
ATOM   4064 C  CD2 . TRP B 1 47  ? -1.536  -35.573 34.249  1.00 22.21 ? 47  TRP B CD2 1 
ATOM   4065 N  NE1 . TRP B 1 47  ? -1.863  -33.646 35.344  1.00 29.55 ? 47  TRP B NE1 1 
ATOM   4066 C  CE2 . TRP B 1 47  ? -0.940  -34.343 34.604  1.00 25.38 ? 47  TRP B CE2 1 
ATOM   4067 C  CE3 . TRP B 1 47  ? -0.798  -36.462 33.469  1.00 21.63 ? 47  TRP B CE3 1 
ATOM   4068 C  CZ2 . TRP B 1 47  ? 0.377   -34.021 34.299  1.00 23.29 ? 47  TRP B CZ2 1 
ATOM   4069 C  CZ3 . TRP B 1 47  ? 0.500   -36.118 33.124  1.00 21.50 ? 47  TRP B CZ3 1 
ATOM   4070 C  CH2 . TRP B 1 47  ? 1.080   -34.921 33.535  1.00 24.49 ? 47  TRP B CH2 1 
ATOM   4071 N  N   . VAL B 1 48  ? -2.797  -39.393 34.063  1.00 18.15 ? 48  VAL B N   1 
ATOM   4072 C  CA  . VAL B 1 48  ? -1.715  -40.269 33.532  1.00 17.73 ? 48  VAL B CA  1 
ATOM   4073 C  C   . VAL B 1 48  ? -1.552  -39.991 32.047  1.00 16.90 ? 48  VAL B C   1 
ATOM   4074 O  O   . VAL B 1 48  ? -2.570  -39.868 31.348  1.00 17.29 ? 48  VAL B O   1 
ATOM   4075 C  CB  . VAL B 1 48  ? -1.989  -41.754 33.747  1.00 19.89 ? 48  VAL B CB  1 
ATOM   4076 C  CG1 . VAL B 1 48  ? -0.893  -42.635 33.196  1.00 20.08 ? 48  VAL B CG1 1 
ATOM   4077 C  CG2 . VAL B 1 48  ? -2.178  -41.986 35.221  1.00 23.44 ? 48  VAL B CG2 1 
ATOM   4078 N  N   . LEU B 1 49  ? -0.331  -39.847 31.585  1.00 16.61 ? 49  LEU B N   1 
ATOM   4079 C  CA  . LEU B 1 49  ? -0.016  -39.755 30.136  1.00 15.98 ? 49  LEU B CA  1 
ATOM   4080 C  C   . LEU B 1 49  ? 0.944   -40.882 29.805  1.00 18.61 ? 49  LEU B C   1 
ATOM   4081 O  O   . LEU B 1 49  ? 1.821   -41.200 30.628  1.00 19.29 ? 49  LEU B O   1 
ATOM   4082 C  CB  . LEU B 1 49  ? 0.645   -38.420 29.777  1.00 20.77 ? 49  LEU B CB  1 
ATOM   4083 C  CG  . LEU B 1 49  ? -0.198  -37.276 29.262  1.00 22.25 ? 49  LEU B CG  1 
ATOM   4084 C  CD1 . LEU B 1 49  ? 0.641   -36.044 28.960  1.00 20.02 ? 49  LEU B CD1 1 
ATOM   4085 C  CD2 . LEU B 1 49  ? -0.957  -37.702 28.004  1.00 21.54 ? 49  LEU B CD2 1 
ATOM   4086 N  N   . ARG B 1 50  ? 0.839   -41.458 28.632  1.00 14.14 ? 50  ARG B N   1 
ATOM   4087 C  CA  . ARG B 1 50  ? 1.845   -42.388 28.113  1.00 14.10 ? 50  ARG B CA  1 
ATOM   4088 C  C   . ARG B 1 50  ? 2.574   -41.676 27.001  1.00 13.53 ? 50  ARG B C   1 
ATOM   4089 O  O   . ARG B 1 50  ? 1.917   -41.275 26.018  1.00 13.92 ? 50  ARG B O   1 
ATOM   4090 C  CB  . ARG B 1 50  ? 1.265   -43.721 27.676  1.00 16.00 ? 50  ARG B CB  1 
ATOM   4091 C  CG  . ARG B 1 50  ? 0.562   -44.477 28.801  1.00 19.09 ? 50  ARG B CG  1 
ATOM   4092 C  CD  . ARG B 1 50  ? -0.821  -44.935 28.407  1.00 21.69 ? 50  ARG B CD  1 
ATOM   4093 N  NE  . ARG B 1 50  ? -1.647  -45.291 29.559  1.00 21.73 ? 50  ARG B NE  1 
ATOM   4094 C  CZ  . ARG B 1 50  ? -2.485  -44.463 30.163  1.00 20.33 ? 50  ARG B CZ  1 
ATOM   4095 N  NH1 . ARG B 1 50  ? -2.673  -43.220 29.721  1.00 18.47 ? 50  ARG B NH1 1 
ATOM   4096 N  NH2 . ARG B 1 50  ? -3.144  -44.909 31.209  1.00 24.28 ? 50  ARG B NH2 1 
ATOM   4097 N  N   . TYR B 1 51  ? 3.866   -41.515 27.123  1.00 11.87 ? 51  TYR B N   1 
ATOM   4098 C  CA  . TYR B 1 51  ? 4.695   -40.760 26.153  1.00 11.86 ? 51  TYR B CA  1 
ATOM   4099 C  C   . TYR B 1 51  ? 5.318   -41.752 25.185  1.00 12.63 ? 51  TYR B C   1 
ATOM   4100 O  O   . TYR B 1 51  ? 6.019   -42.688 25.602  1.00 12.94 ? 51  TYR B O   1 
ATOM   4101 C  CB  . TYR B 1 51  ? 5.783   -39.969 26.883  1.00 11.55 ? 51  TYR B CB  1 
ATOM   4102 C  CG  . TYR B 1 51  ? 5.309   -38.711 27.539  1.00 11.38 ? 51  TYR B CG  1 
ATOM   4103 C  CD1 . TYR B 1 51  ? 4.843   -38.726 28.853  1.00 13.27 ? 51  TYR B CD1 1 
ATOM   4104 C  CD2 . TYR B 1 51  ? 5.364   -37.499 26.856  1.00 12.94 ? 51  TYR B CD2 1 
ATOM   4105 C  CE1 . TYR B 1 51  ? 4.412   -37.540 29.427  1.00 13.25 ? 51  TYR B CE1 1 
ATOM   4106 C  CE2 . TYR B 1 51  ? 4.909   -36.326 27.411  1.00 12.57 ? 51  TYR B CE2 1 
ATOM   4107 C  CZ  . TYR B 1 51  ? 4.426   -36.363 28.698  1.00 14.29 ? 51  TYR B CZ  1 
ATOM   4108 O  OH  . TYR B 1 51  ? 4.040   -35.185 29.284  1.00 16.15 ? 51  TYR B OH  1 
ATOM   4109 N  N   A LEU B 1 52  ? 5.068   -41.562 23.886  0.50 12.43 ? 52  LEU B N   1 
ATOM   4110 N  N   B LEU B 1 52  ? 5.100   -41.540 23.885  0.50 12.46 ? 52  LEU B N   1 
ATOM   4111 C  CA  A LEU B 1 52  ? 5.578   -42.430 22.796  0.50 11.91 ? 52  LEU B CA  1 
ATOM   4112 C  CA  B LEU B 1 52  ? 5.532   -42.434 22.779  0.50 11.93 ? 52  LEU B CA  1 
ATOM   4113 C  C   A LEU B 1 52  ? 6.718   -41.747 22.038  0.50 12.85 ? 52  LEU B C   1 
ATOM   4114 C  C   B LEU B 1 52  ? 6.646   -41.793 21.948  0.50 12.54 ? 52  LEU B C   1 
ATOM   4115 O  O   A LEU B 1 52  ? 6.674   -40.508 21.838  0.50 13.83 ? 52  LEU B O   1 
ATOM   4116 O  O   B LEU B 1 52  ? 6.465   -40.638 21.547  0.50 12.52 ? 52  LEU B O   1 
ATOM   4117 C  CB  A LEU B 1 52  ? 4.445   -42.764 21.824  0.50 11.60 ? 52  LEU B CB  1 
ATOM   4118 C  CB  B LEU B 1 52  ? 4.333   -42.676 21.862  0.50 11.88 ? 52  LEU B CB  1 
ATOM   4119 C  CG  A LEU B 1 52  ? 3.169   -43.266 22.463  0.50 11.37 ? 52  LEU B CG  1 
ATOM   4120 C  CG  B LEU B 1 52  ? 3.414   -43.824 22.216  0.50 12.05 ? 52  LEU B CG  1 
ATOM   4121 C  CD1 A LEU B 1 52  ? 2.100   -43.526 21.395  0.50 11.32 ? 52  LEU B CD1 1 
ATOM   4122 C  CD1 B LEU B 1 52  ? 2.632   -43.526 23.473  0.50 12.22 ? 52  LEU B CD1 1 
ATOM   4123 C  CD2 A LEU B 1 52  ? 3.469   -44.513 23.268  0.50 11.83 ? 52  LEU B CD2 1 
ATOM   4124 C  CD2 B LEU B 1 52  ? 2.455   -44.088 21.065  0.50 12.12 ? 52  LEU B CD2 1 
ATOM   4125 N  N   . SER B 1 53  ? 7.724   -42.532 21.639  1.00 11.81 ? 53  SER B N   1 
ATOM   4126 C  CA  . SER B 1 53  ? 8.924   -42.047 20.927  1.00 12.42 ? 53  SER B CA  1 
ATOM   4127 C  C   . SER B 1 53  ? 9.277   -42.857 19.690  1.00 12.86 ? 53  SER B C   1 
ATOM   4128 O  O   . SER B 1 53  ? 10.145  -42.416 18.960  1.00 16.48 ? 53  SER B O   1 
ATOM   4129 C  CB  . SER B 1 53  ? 10.085  -42.063 21.901  1.00 13.64 ? 53  SER B CB  1 
ATOM   4130 O  OG  . SER B 1 53  ? 9.882   -41.042 22.848  1.00 14.84 ? 53  SER B OG  1 
ATOM   4131 N  N   . SER B 1 54  ? 8.725   -44.065 19.515  1.00 12.24 ? 54  SER B N   1 
ATOM   4132 C  CA  . SER B 1 54  ? 9.137   -44.907 18.380  1.00 14.08 ? 54  SER B CA  1 
ATOM   4133 C  C   . SER B 1 54  ? 8.115   -44.828 17.240  1.00 12.01 ? 54  SER B C   1 
ATOM   4134 O  O   . SER B 1 54  ? 6.884   -44.751 17.505  1.00 12.64 ? 54  SER B O   1 
ATOM   4135 C  CB  . SER B 1 54  ? 9.356   -46.356 18.794  1.00 13.62 ? 54  SER B CB  1 
ATOM   4136 O  OG  . SER B 1 54  ? 8.135   -46.994 19.131  1.00 14.37 ? 54  SER B OG  1 
ATOM   4137 N  N   . GLN B 1 55  ? 8.606   -44.934 16.016  1.00 12.14 ? 55  GLN B N   1 
ATOM   4138 C  CA  . GLN B 1 55  ? 7.704   -45.057 14.848  1.00 12.54 ? 55  GLN B CA  1 
ATOM   4139 C  C   . GLN B 1 55  ? 6.859   -46.318 15.015  1.00 11.76 ? 55  GLN B C   1 
ATOM   4140 O  O   . GLN B 1 55  ? 5.674   -46.324 14.610  1.00 12.06 ? 55  GLN B O   1 
ATOM   4141 C  CB  . GLN B 1 55  ? 8.543   -45.013 13.593  1.00 12.56 ? 55  GLN B CB  1 
ATOM   4142 C  CG  . GLN B 1 55  ? 7.713   -44.925 12.317  1.00 14.18 ? 55  GLN B CG  1 
ATOM   4143 C  CD  . GLN B 1 55  ? 7.278   -46.240 11.714  1.00 14.93 ? 55  GLN B CD  1 
ATOM   4144 O  OE1 . GLN B 1 55  ? 7.644   -47.324 12.138  1.00 15.22 ? 55  GLN B OE1 1 
ATOM   4145 N  NE2 . GLN B 1 55  ? 6.334   -46.164 10.792  1.00 15.91 ? 55  GLN B NE2 1 
ATOM   4146 N  N   . ARG B 1 56  ? 7.419   -47.384 15.593  1.00 12.90 ? 56  ARG B N   1 
ATOM   4147 C  CA  . ARG B 1 56  ? 6.630   -48.648 15.729  1.00 14.76 ? 56  ARG B CA  1 
ATOM   4148 C  C   . ARG B 1 56  ? 5.309   -48.391 16.471  1.00 13.89 ? 56  ARG B C   1 
ATOM   4149 O  O   . ARG B 1 56  ? 4.291   -49.002 16.161  1.00 14.68 ? 56  ARG B O   1 
ATOM   4150 C  CB  . ARG B 1 56  ? 7.483   -49.692 16.478  1.00 18.39 ? 56  ARG B CB  1 
ATOM   4151 C  CG  . ARG B 1 56  ? 6.781   -51.003 16.818  1.00 20.92 ? 56  ARG B CG  1 
ATOM   4152 C  CD  . ARG B 1 56  ? 7.699   -51.921 17.633  1.00 21.94 ? 56  ARG B CD  1 
ATOM   4153 N  NE  . ARG B 1 56  ? 7.538   -51.752 19.071  1.00 24.63 ? 56  ARG B NE  1 
ATOM   4154 C  CZ  . ARG B 1 56  ? 6.685   -52.406 19.854  1.00 22.35 ? 56  ARG B CZ  1 
ATOM   4155 N  NH1 . ARG B 1 56  ? 5.848   -53.299 19.347  1.00 23.22 ? 56  ARG B NH1 1 
ATOM   4156 N  NH2 . ARG B 1 56  ? 6.682   -52.171 21.160  1.00 26.79 ? 56  ARG B NH2 1 
ATOM   4157 N  N   . LEU B 1 57  ? 5.332   -47.577 17.535  1.00 12.26 ? 57  LEU B N   1 
ATOM   4158 C  CA  . LEU B 1 57  ? 4.124   -47.375 18.372  1.00 13.07 ? 57  LEU B CA  1 
ATOM   4159 C  C   . LEU B 1 57  ? 3.365   -46.181 17.839  1.00 12.55 ? 57  LEU B C   1 
ATOM   4160 O  O   . LEU B 1 57  ? 2.122   -46.168 17.883  1.00 12.92 ? 57  LEU B O   1 
ATOM   4161 C  CB  . LEU B 1 57  ? 4.508   -47.161 19.833  1.00 13.02 ? 57  LEU B CB  1 
ATOM   4162 C  CG  . LEU B 1 57  ? 5.148   -48.346 20.538  1.00 13.27 ? 57  LEU B CG  1 
ATOM   4163 C  CD1 . LEU B 1 57  ? 5.398   -48.037 22.009  1.00 15.10 ? 57  LEU B CD1 1 
ATOM   4164 C  CD2 . LEU B 1 57  ? 4.304   -49.600 20.373  1.00 15.42 ? 57  LEU B CD2 1 
ATOM   4165 N  N   . ILE B 1 58  ? 4.078   -45.168 17.346  1.00 12.53 ? 58  ILE B N   1 
ATOM   4166 C  CA  . ILE B 1 58  ? 3.377   -43.959 16.826  1.00 12.64 ? 58  ILE B CA  1 
ATOM   4167 C  C   . ILE B 1 58  ? 2.548   -44.291 15.595  1.00 12.60 ? 58  ILE B C   1 
ATOM   4168 O  O   . ILE B 1 58  ? 1.462   -43.679 15.434  1.00 13.38 ? 58  ILE B O   1 
ATOM   4169 C  CB  . ILE B 1 58  ? 4.387   -42.814 16.684  1.00 12.03 ? 58  ILE B CB  1 
ATOM   4170 C  CG1 . ILE B 1 58  ? 4.806   -42.372 18.092  1.00 12.53 ? 58  ILE B CG1 1 
ATOM   4171 C  CG2 . ILE B 1 58  ? 3.805   -41.643 15.899  1.00 13.89 ? 58  ILE B CG2 1 
ATOM   4172 C  CD1 . ILE B 1 58  ? 6.047   -41.520 18.132  1.00 12.65 ? 58  ILE B CD1 1 
ATOM   4173 N  N   . LYS B 1 59  ? 2.961   -45.235 14.784  1.00 12.37 ? 59  LYS B N   1 
ATOM   4174 C  CA  . LYS B 1 59  ? 2.164   -45.570 13.585  1.00 14.21 ? 59  LYS B CA  1 
ATOM   4175 C  C   . LYS B 1 59  ? 0.806   -46.130 14.027  1.00 14.44 ? 59  LYS B C   1 
ATOM   4176 O  O   . LYS B 1 59  ? -0.169  -46.015 13.274  1.00 15.73 ? 59  LYS B O   1 
ATOM   4177 C  CB  . LYS B 1 59  ? 2.946   -46.507 12.680  1.00 14.03 ? 59  LYS B CB  1 
ATOM   4178 C  CG  . LYS B 1 59  ? 3.090   -47.929 13.213  1.00 15.08 ? 59  LYS B CG  1 
ATOM   4179 C  CD  . LYS B 1 59  ? 3.925   -48.761 12.264  1.00 16.82 ? 59  LYS B CD  1 
ATOM   4180 C  CE  . LYS B 1 59  ? 4.104   -50.193 12.718  1.00 17.91 ? 59  LYS B CE  1 
ATOM   4181 N  NZ  . LYS B 1 59  ? 4.879   -50.955 11.686  1.00 20.89 ? 59  LYS B NZ  1 
ATOM   4182 N  N   . GLU B 1 60  ? 0.746   -46.824 15.133  1.00 12.60 ? 60  GLU B N   1 
ATOM   4183 C  CA  . GLU B 1 60  ? -0.541  -47.290 15.713  1.00 12.64 ? 60  GLU B CA  1 
ATOM   4184 C  C   . GLU B 1 60  ? -1.337  -46.112 16.290  1.00 12.56 ? 60  GLU B C   1 
ATOM   4185 O  O   . GLU B 1 60  ? -2.596  -46.034 16.141  1.00 12.89 ? 60  GLU B O   1 
ATOM   4186 C  CB  . GLU B 1 60  ? -0.301  -48.348 16.797  1.00 13.31 ? 60  GLU B CB  1 
ATOM   4187 C  CG  . GLU B 1 60  ? 0.153   -49.682 16.231  1.00 16.13 ? 60  GLU B CG  1 
ATOM   4188 C  CD  . GLU B 1 60  ? 0.162   -50.784 17.277  1.00 20.92 ? 60  GLU B CD  1 
ATOM   4189 O  OE1 . GLU B 1 60  ? -0.803  -50.874 18.066  1.00 20.29 ? 60  GLU B OE1 1 
ATOM   4190 O  OE2 . GLU B 1 60  ? 1.185   -51.517 17.346  1.00 23.26 ? 60  GLU B OE2 1 
ATOM   4191 N  N   . ALA B 1 61  ? -0.690  -45.220 17.033  1.00 12.58 ? 61  ALA B N   1 
ATOM   4192 C  CA  . ALA B 1 61  ? -1.329  -44.045 17.660  1.00 13.10 ? 61  ALA B CA  1 
ATOM   4193 C  C   . ALA B 1 61  ? -1.997  -43.183 16.595  1.00 13.04 ? 61  ALA B C   1 
ATOM   4194 O  O   . ALA B 1 61  ? -3.007  -42.504 16.870  1.00 12.89 ? 61  ALA B O   1 
ATOM   4195 C  CB  . ALA B 1 61  ? -0.356  -43.251 18.504  1.00 14.31 ? 61  ALA B CB  1 
ATOM   4196 N  N   . CYS B 1 62  ? -1.456  -43.181 15.400  1.00 12.12 ? 62  CYS B N   1 
ATOM   4197 C  CA  . CYS B 1 62  ? -1.921  -42.345 14.258  1.00 12.82 ? 62  CYS B CA  1 
ATOM   4198 C  C   . CYS B 1 62  ? -3.075  -43.013 13.472  1.00 12.36 ? 62  CYS B C   1 
ATOM   4199 O  O   . CYS B 1 62  ? -3.537  -42.429 12.456  1.00 13.78 ? 62  CYS B O   1 
ATOM   4200 C  CB  . CYS B 1 62  ? -0.766  -42.029 13.356  1.00 12.89 ? 62  CYS B CB  1 
ATOM   4201 S  SG  . CYS B 1 62  ? 0.337   -40.777 14.061  1.00 14.70 ? 62  CYS B SG  1 
ATOM   4202 N  N   . ASP B 1 63  ? -3.485  -44.205 13.885  1.00 12.28 ? 63  ASP B N   1 
ATOM   4203 C  CA  . ASP B 1 63  ? -4.644  -44.906 13.313  1.00 11.96 ? 63  ASP B CA  1 
ATOM   4204 C  C   . ASP B 1 63  ? -5.915  -44.245 13.843  1.00 12.10 ? 63  ASP B C   1 
ATOM   4205 O  O   . ASP B 1 63  ? -6.260  -44.391 15.060  1.00 12.49 ? 63  ASP B O   1 
ATOM   4206 C  CB  . ASP B 1 63  ? -4.583  -46.396 13.627  1.00 12.84 ? 63  ASP B CB  1 
ATOM   4207 C  CG  . ASP B 1 63  ? -5.728  -47.205 13.088  1.00 14.93 ? 63  ASP B CG  1 
ATOM   4208 O  OD1 . ASP B 1 63  ? -6.781  -46.617 12.724  1.00 14.54 ? 63  ASP B OD1 1 
ATOM   4209 O  OD2 . ASP B 1 63  ? -5.559  -48.474 13.096  1.00 17.07 ? 63  ASP B OD2 1 
ATOM   4210 N  N   . GLU B 1 64  ? -6.606  -43.466 13.000  1.00 12.91 ? 64  GLU B N   1 
ATOM   4211 C  CA  . GLU B 1 64  ? -7.761  -42.653 13.437  1.00 12.64 ? 64  GLU B CA  1 
ATOM   4212 C  C   . GLU B 1 64  ? -8.969  -43.528 13.770  1.00 12.46 ? 64  GLU B C   1 
ATOM   4213 O  O   . GLU B 1 64  ? -9.913  -43.010 14.403  1.00 14.19 ? 64  GLU B O   1 
ATOM   4214 C  CB  . GLU B 1 64  ? -8.107  -41.691 12.314  1.00 13.91 ? 64  GLU B CB  1 
ATOM   4215 C  CG  . GLU B 1 64  ? -7.018  -40.647 12.134  1.00 16.94 ? 64  GLU B CG  1 
ATOM   4216 C  CD  . GLU B 1 64  ? -7.255  -39.751 10.935  1.00 21.05 ? 64  GLU B CD  1 
ATOM   4217 O  OE1 . GLU B 1 64  ? -7.097  -40.262 9.779   1.00 26.34 ? 64  GLU B OE1 1 
ATOM   4218 O  OE2 . GLU B 1 64  ? -7.641  -38.632 11.161  1.00 16.61 ? 64  GLU B OE2 1 
ATOM   4219 N  N   . SER B 1 65  ? -8.970  -44.815 13.355  1.00 13.76 ? 65  SER B N   1 
ATOM   4220 C  CA  . SER B 1 65  ? -10.063 -45.732 13.814  1.00 13.58 ? 65  SER B CA  1 
ATOM   4221 C  C   . SER B 1 65  ? -9.900  -46.041 15.300  1.00 13.88 ? 65  SER B C   1 
ATOM   4222 O  O   . SER B 1 65  ? -10.884 -46.496 15.903  1.00 15.67 ? 65  SER B O   1 
ATOM   4223 C  CB  . SER B 1 65  ? -10.117 -46.972 13.021  1.00 15.88 ? 65  SER B CB  1 
ATOM   4224 O  OG  . SER B 1 65  ? -9.071  -47.836 13.357  1.00 20.22 ? 65  SER B OG  1 
ATOM   4225 N  N   . ARG B 1 66  ? -8.693  -45.919 15.836  1.00 12.91 ? 66  ARG B N   1 
ATOM   4226 C  CA  . ARG B 1 66  ? -8.368  -46.374 17.209  1.00 13.04 ? 66  ARG B CA  1 
ATOM   4227 C  C   . ARG B 1 66  ? -8.131  -45.214 18.164  1.00 12.47 ? 66  ARG B C   1 
ATOM   4228 O  O   . ARG B 1 66  ? -8.333  -45.371 19.345  1.00 14.05 ? 66  ARG B O   1 
ATOM   4229 C  CB  . ARG B 1 66  ? -7.123  -47.259 17.229  1.00 14.60 ? 66  ARG B CB  1 
ATOM   4230 C  CG  . ARG B 1 66  ? -7.253  -48.519 16.368  1.00 15.97 ? 66  ARG B CG  1 
ATOM   4231 C  CD  . ARG B 1 66  ? -5.902  -49.257 16.213  1.00 15.80 ? 66  ARG B CD  1 
ATOM   4232 N  NE  . ARG B 1 66  ? -5.492  -49.803 17.508  1.00 17.27 ? 66  ARG B NE  1 
ATOM   4233 C  CZ  . ARG B 1 66  ? -4.272  -50.209 17.781  1.00 17.75 ? 66  ARG B CZ  1 
ATOM   4234 N  NH1 . ARG B 1 66  ? -3.320  -50.137 16.872  1.00 18.54 ? 66  ARG B NH1 1 
ATOM   4235 N  NH2 . ARG B 1 66  ? -4.013  -50.686 18.982  1.00 20.83 ? 66  ARG B NH2 1 
ATOM   4236 N  N   . PHE B 1 67  ? -7.658  -44.062 17.651  1.00 12.08 ? 67  PHE B N   1 
ATOM   4237 C  CA  . PHE B 1 67  ? -7.260  -42.926 18.508  1.00 10.59 ? 67  PHE B CA  1 
ATOM   4238 C  C   . PHE B 1 67  ? -7.714  -41.633 17.825  1.00 10.51 ? 67  PHE B C   1 
ATOM   4239 O  O   . PHE B 1 67  ? -7.641  -41.511 16.583  1.00 11.75 ? 67  PHE B O   1 
ATOM   4240 C  CB  . PHE B 1 67  ? -5.727  -42.886 18.635  1.00 12.22 ? 67  PHE B CB  1 
ATOM   4241 C  CG  . PHE B 1 67  ? -5.173  -44.115 19.300  1.00 12.91 ? 67  PHE B CG  1 
ATOM   4242 C  CD1 . PHE B 1 67  ? -5.075  -44.171 20.671  1.00 14.30 ? 67  PHE B CD1 1 
ATOM   4243 C  CD2 . PHE B 1 67  ? -4.676  -45.152 18.531  1.00 13.27 ? 67  PHE B CD2 1 
ATOM   4244 C  CE1 . PHE B 1 67  ? -4.578  -45.321 21.279  1.00 14.45 ? 67  PHE B CE1 1 
ATOM   4245 C  CE2 . PHE B 1 67  ? -4.183  -46.299 19.147  1.00 13.98 ? 67  PHE B CE2 1 
ATOM   4246 C  CZ  . PHE B 1 67  ? -4.143  -46.366 20.511  1.00 14.47 ? 67  PHE B CZ  1 
ATOM   4247 N  N   . ASP B 1 68  ? -8.120  -40.692 18.648  1.00 10.28 ? 68  ASP B N   1 
ATOM   4248 C  CA  . ASP B 1 68  ? -8.517  -39.340 18.195  1.00 10.45 ? 68  ASP B CA  1 
ATOM   4249 C  C   . ASP B 1 68  ? -7.684  -38.300 18.935  1.00 11.35 ? 68  ASP B C   1 
ATOM   4250 O  O   . ASP B 1 68  ? -7.059  -38.586 19.974  1.00 10.98 ? 68  ASP B O   1 
ATOM   4251 C  CB  . ASP B 1 68  ? -10.020 -39.152 18.396  1.00 12.82 ? 68  ASP B CB  1 
ATOM   4252 C  CG  . ASP B 1 68  ? -10.644 -37.829 17.979  1.00 12.69 ? 68  ASP B CG  1 
ATOM   4253 O  OD1 . ASP B 1 68  ? -10.102 -37.188 17.014  1.00 12.40 ? 68  ASP B OD1 1 
ATOM   4254 O  OD2 . ASP B 1 68  ? -11.661 -37.454 18.641  1.00 14.01 ? 68  ASP B OD2 1 
ATOM   4255 N  N   . LYS B 1 69  ? -7.660  -37.071 18.423  1.00 11.06 ? 69  LYS B N   1 
ATOM   4256 C  CA  . LYS B 1 69  ? -6.944  -35.980 19.086  1.00 10.67 ? 69  LYS B CA  1 
ATOM   4257 C  C   . LYS B 1 69  ? -7.506  -35.748 20.477  1.00 10.17 ? 69  LYS B C   1 
ATOM   4258 O  O   . LYS B 1 69  ? -8.742  -35.650 20.708  1.00 11.08 ? 69  LYS B O   1 
ATOM   4259 C  CB  . LYS B 1 69  ? -7.032  -34.675 18.280  1.00 11.13 ? 69  LYS B CB  1 
ATOM   4260 C  CG  . LYS B 1 69  ? -6.659  -33.426 19.072  1.00 11.47 ? 69  LYS B CG  1 
ATOM   4261 C  CD  . LYS B 1 69  ? -6.173  -32.277 18.197  1.00 12.13 ? 69  LYS B CD  1 
ATOM   4262 C  CE  . LYS B 1 69  ? -6.081  -31.028 19.070  1.00 12.02 ? 69  LYS B CE  1 
ATOM   4263 N  NZ  . LYS B 1 69  ? -5.259  -29.957 18.427  1.00 12.86 ? 69  LYS B NZ  1 
ATOM   4264 N  N   . ASN B 1 70  ? -6.588  -35.663 21.415  1.00 9.66  ? 70  ASN B N   1 
ATOM   4265 C  CA  . ASN B 1 70  ? -6.855  -35.250 22.789  1.00 11.07 ? 70  ASN B CA  1 
ATOM   4266 C  C   . ASN B 1 70  ? -6.435  -33.813 23.030  1.00 11.39 ? 70  ASN B C   1 
ATOM   4267 O  O   . ASN B 1 70  ? -5.422  -33.380 22.457  1.00 11.91 ? 70  ASN B O   1 
ATOM   4268 C  CB  . ASN B 1 70  ? -6.137  -36.211 23.724  1.00 12.25 ? 70  ASN B CB  1 
ATOM   4269 C  CG  . ASN B 1 70  ? -6.436  -35.976 25.181  1.00 14.17 ? 70  ASN B CG  1 
ATOM   4270 O  OD1 . ASN B 1 70  ? -7.589  -35.866 25.593  1.00 17.10 ? 70  ASN B OD1 1 
ATOM   4271 N  ND2 . ASN B 1 70  ? -5.363  -35.848 25.950  1.00 15.91 ? 70  ASN B ND2 1 
ATOM   4272 N  N   . LEU B 1 71  ? -7.117  -33.151 23.948  1.00 12.85 ? 71  LEU B N   1 
ATOM   4273 C  CA  . LEU B 1 71  ? -6.635  -31.836 24.480  1.00 13.97 ? 71  LEU B CA  1 
ATOM   4274 C  C   . LEU B 1 71  ? -5.854  -32.097 25.755  1.00 16.09 ? 71  LEU B C   1 
ATOM   4275 O  O   . LEU B 1 71  ? -6.477  -32.515 26.731  1.00 15.85 ? 71  LEU B O   1 
ATOM   4276 C  CB  . LEU B 1 71  ? -7.804  -30.901 24.740  1.00 14.25 ? 71  LEU B CB  1 
ATOM   4277 C  CG  . LEU B 1 71  ? -8.723  -30.568 23.558  1.00 14.80 ? 71  LEU B CG  1 
ATOM   4278 C  CD1 . LEU B 1 71  ? -9.698  -29.469 23.936  1.00 16.33 ? 71  LEU B CD1 1 
ATOM   4279 C  CD2 . LEU B 1 71  ? -7.934  -30.136 22.333  1.00 16.18 ? 71  LEU B CD2 1 
ATOM   4280 N  N   . SER B 1 72  ? -4.552  -31.935 25.696  1.00 16.25 ? 72  SER B N   1 
ATOM   4281 C  CA  . SER B 1 72  ? -3.705  -31.969 26.909  1.00 18.22 ? 72  SER B CA  1 
ATOM   4282 C  C   . SER B 1 72  ? -4.186  -30.886 27.859  1.00 17.27 ? 72  SER B C   1 
ATOM   4283 O  O   . SER B 1 72  ? -4.931  -29.985 27.472  1.00 17.29 ? 72  SER B O   1 
ATOM   4284 C  CB  . SER B 1 72  ? -2.296  -31.761 26.563  1.00 20.70 ? 72  SER B CB  1 
ATOM   4285 O  OG  . SER B 1 72  ? -2.105  -30.370 26.249  1.00 24.88 ? 72  SER B OG  1 
ATOM   4286 N  N   . GLN B 1 73  ? -3.661  -30.932 29.081  1.00 20.83 ? 73  GLN B N   1 
ATOM   4287 C  CA  . GLN B 1 73  ? -3.983  -29.885 30.075  1.00 20.61 ? 73  GLN B CA  1 
ATOM   4288 C  C   . GLN B 1 73  ? -3.623  -28.510 29.501  1.00 20.05 ? 73  GLN B C   1 
ATOM   4289 O  O   . GLN B 1 73  ? -4.432  -27.611 29.688  1.00 22.34 ? 73  GLN B O   1 
ATOM   4290 C  CB  . GLN B 1 73  ? -3.211  -30.144 31.379  1.00 26.51 ? 73  GLN B CB  1 
ATOM   4291 C  CG  . GLN B 1 73  ? -3.429  -31.533 31.947  1.00 30.58 ? 73  GLN B CG  1 
ATOM   4292 C  CD  . GLN B 1 73  ? -4.802  -31.653 32.543  1.00 34.68 ? 73  GLN B CD  1 
ATOM   4293 O  OE1 . GLN B 1 73  ? -5.239  -30.762 33.277  1.00 41.67 ? 73  GLN B OE1 1 
ATOM   4294 N  NE2 . GLN B 1 73  ? -5.512  -32.726 32.201  1.00 41.13 ? 73  GLN B NE2 1 
ATOM   4295 N  N   . VAL B 1 74  ? -2.473  -28.405 28.836  1.00 19.39 ? 74  VAL B N   1 
ATOM   4296 C  CA  . VAL B 1 74  ? -2.033  -27.104 28.234  1.00 21.27 ? 74  VAL B CA  1 
ATOM   4297 C  C   . VAL B 1 74  ? -3.133  -26.665 27.243  1.00 20.01 ? 74  VAL B C   1 
ATOM   4298 O  O   . VAL B 1 74  ? -3.604  -25.525 27.352  1.00 21.33 ? 74  VAL B O   1 
ATOM   4299 C  CB  . VAL B 1 74  ? -0.661  -27.206 27.556  1.00 25.66 ? 74  VAL B CB  1 
ATOM   4300 C  CG1 . VAL B 1 74  ? -0.416  -25.987 26.689  1.00 29.69 ? 74  VAL B CG1 1 
ATOM   4301 C  CG2 . VAL B 1 74  ? 0.449   -27.382 28.599  1.00 25.57 ? 74  VAL B CG2 1 
ATOM   4302 N  N   . LEU B 1 75  ? -3.646  -27.554 26.393  1.00 16.81 ? 75  LEU B N   1 
ATOM   4303 C  CA  . LEU B 1 75  ? -4.622  -27.107 25.353  1.00 15.74 ? 75  LEU B CA  1 
ATOM   4304 C  C   . LEU B 1 75  ? -5.976  -26.758 25.975  1.00 14.67 ? 75  LEU B C   1 
ATOM   4305 O  O   . LEU B 1 75  ? -6.676  -25.873 25.490  1.00 15.94 ? 75  LEU B O   1 
ATOM   4306 C  CB  . LEU B 1 75  ? -4.780  -28.121 24.219  1.00 17.05 ? 75  LEU B CB  1 
ATOM   4307 C  CG  . LEU B 1 75  ? -3.579  -28.253 23.307  1.00 20.50 ? 75  LEU B CG  1 
ATOM   4308 C  CD1 . LEU B 1 75  ? -3.967  -28.950 22.009  1.00 18.41 ? 75  LEU B CD1 1 
ATOM   4309 C  CD2 . LEU B 1 75  ? -2.908  -26.894 23.121  1.00 23.63 ? 75  LEU B CD2 1 
ATOM   4310 N  N   . LYS B 1 76  ? -6.353  -27.461 27.035  1.00 15.96 ? 76  LYS B N   1 
ATOM   4311 C  CA  . LYS B 1 76  ? -7.592  -27.126 27.755  1.00 18.32 ? 76  LYS B CA  1 
ATOM   4312 C  C   . LYS B 1 76  ? -7.494  -25.694 28.307  1.00 19.50 ? 76  LYS B C   1 
ATOM   4313 O  O   . LYS B 1 76  ? -8.477  -25.009 28.286  1.00 19.26 ? 76  LYS B O   1 
ATOM   4314 C  CB  . LYS B 1 76  ? -7.783  -28.135 28.879  1.00 19.86 ? 76  LYS B CB  1 
ATOM   4315 C  CG  . LYS B 1 76  ? -8.070  -29.535 28.377  1.00 19.74 ? 76  LYS B CG  1 
ATOM   4316 C  CD  . LYS B 1 76  ? -8.471  -30.500 29.458  1.00 21.30 ? 76  LYS B CD  1 
ATOM   4317 C  CE  . LYS B 1 76  ? -8.935  -31.791 28.835  1.00 23.85 ? 76  LYS B CE  1 
ATOM   4318 N  NZ  . LYS B 1 76  ? -9.139  -32.836 29.862  1.00 29.43 ? 76  LYS B NZ  1 
ATOM   4319 N  N   . PHE B 1 77  ? -6.312  -25.281 28.740  1.00 19.92 ? 77  PHE B N   1 
ATOM   4320 C  CA  . PHE B 1 77  ? -6.089  -23.920 29.265  1.00 21.42 ? 77  PHE B CA  1 
ATOM   4321 C  C   . PHE B 1 77  ? -5.999  -22.904 28.116  1.00 20.29 ? 77  PHE B C   1 
ATOM   4322 O  O   . PHE B 1 77  ? -6.614  -21.819 28.225  1.00 19.34 ? 77  PHE B O   1 
ATOM   4323 C  CB  . PHE B 1 77  ? -4.879  -23.957 30.213  1.00 21.79 ? 77  PHE B CB  1 
ATOM   4324 C  CG  . PHE B 1 77  ? -5.185  -24.671 31.511  1.00 23.42 ? 77  PHE B CG  1 
ATOM   4325 C  CD1 . PHE B 1 77  ? -6.372  -24.440 32.185  1.00 28.20 ? 77  PHE B CD1 1 
ATOM   4326 C  CD2 . PHE B 1 77  ? -4.269  -25.572 32.040  1.00 25.58 ? 77  PHE B CD2 1 
ATOM   4327 C  CE1 . PHE B 1 77  ? -6.652  -25.113 33.369  1.00 28.94 ? 77  PHE B CE1 1 
ATOM   4328 C  CE2 . PHE B 1 77  ? -4.532  -26.202 33.251  1.00 24.53 ? 77  PHE B CE2 1 
ATOM   4329 C  CZ  . PHE B 1 77  ? -5.735  -25.994 33.880  1.00 25.83 ? 77  PHE B CZ  1 
ATOM   4330 N  N   . VAL B 1 78  ? -5.363  -23.264 26.991  1.00 17.25 ? 78  VAL B N   1 
ATOM   4331 C  CA  . VAL B 1 78  ? -5.347  -22.393 25.774  1.00 17.47 ? 78  VAL B CA  1 
ATOM   4332 C  C   . VAL B 1 78  ? -6.789  -22.203 25.284  1.00 17.01 ? 78  VAL B C   1 
ATOM   4333 O  O   . VAL B 1 78  ? -7.115  -21.115 24.803  1.00 16.22 ? 78  VAL B O   1 
ATOM   4334 C  CB  . VAL B 1 78  ? -4.421  -22.949 24.684  1.00 16.75 ? 78  VAL B CB  1 
ATOM   4335 C  CG1 . VAL B 1 78  ? -4.488  -22.101 23.411  1.00 17.42 ? 78  VAL B CG1 1 
ATOM   4336 C  CG2 . VAL B 1 78  ? -2.977  -23.027 25.197  1.00 18.68 ? 78  VAL B CG2 1 
ATOM   4337 N  N   . ARG B 1 79  ? -7.640  -23.208 25.437  1.00 17.15 ? 79  ARG B N   1 
ATOM   4338 C  CA  . ARG B 1 79  ? -9.065  -23.091 25.042  1.00 15.99 ? 79  ARG B CA  1 
ATOM   4339 C  C   . ARG B 1 79  ? -9.776  -21.948 25.767  1.00 18.45 ? 79  ARG B C   1 
ATOM   4340 O  O   . ARG B 1 79  ? -10.747 -21.448 25.241  1.00 18.45 ? 79  ARG B O   1 
ATOM   4341 C  CB  . ARG B 1 79  ? -9.729  -24.440 25.256  1.00 16.85 ? 79  ARG B CB  1 
ATOM   4342 C  CG  . ARG B 1 79  ? -11.174 -24.475 24.800  1.00 17.70 ? 79  ARG B CG  1 
ATOM   4343 C  CD  . ARG B 1 79  ? -11.700 -25.869 24.785  1.00 19.17 ? 79  ARG B CD  1 
ATOM   4344 N  NE  . ARG B 1 79  ? -13.165 -25.807 24.639  1.00 22.14 ? 79  ARG B NE  1 
ATOM   4345 C  CZ  . ARG B 1 79  ? -13.866 -26.387 23.650  1.00 21.04 ? 79  ARG B CZ  1 
ATOM   4346 N  NH1 . ARG B 1 79  ? -13.229 -27.060 22.721  1.00 15.80 ? 79  ARG B NH1 1 
ATOM   4347 N  NH2 . ARG B 1 79  ? -15.188 -26.278 23.560  1.00 21.57 ? 79  ARG B NH2 1 
ATOM   4348 N  N   . ASP B 1 80  ? -9.300  -21.540 26.940  1.00 19.56 ? 80  ASP B N   1 
ATOM   4349 C  CA  . ASP B 1 80  ? -9.923  -20.392 27.634  1.00 21.11 ? 80  ASP B CA  1 
ATOM   4350 C  C   . ASP B 1 80  ? -9.827  -19.104 26.803  1.00 21.36 ? 80  ASP B C   1 
ATOM   4351 O  O   . ASP B 1 80  ? -10.710 -18.221 26.993  1.00 22.10 ? 80  ASP B O   1 
ATOM   4352 C  CB  . ASP B 1 80  ? -9.327  -20.233 29.041  1.00 24.91 ? 80  ASP B CB  1 
ATOM   4353 C  CG  . ASP B 1 80  ? -9.710  -21.410 29.931  1.00 28.74 ? 80  ASP B CG  1 
ATOM   4354 O  OD1 . ASP B 1 80  ? -10.778 -21.954 29.709  1.00 29.72 ? 80  ASP B OD1 1 
ATOM   4355 O  OD2 . ASP B 1 80  ? -8.935  -21.776 30.848  1.00 36.42 ? 80  ASP B OD2 1 
ATOM   4356 N  N   . PHE B 1 81  ? -8.855  -18.965 25.874  1.00 17.04 ? 81  PHE B N   1 
ATOM   4357 C  CA  . PHE B 1 81  ? -8.879  -17.826 24.917  1.00 18.05 ? 81  PHE B CA  1 
ATOM   4358 C  C   . PHE B 1 81  ? -8.996  -18.245 23.441  1.00 17.34 ? 81  PHE B C   1 
ATOM   4359 O  O   . PHE B 1 81  ? -9.441  -17.418 22.665  1.00 19.83 ? 81  PHE B O   1 
ATOM   4360 C  CB  . PHE B 1 81  ? -7.673  -16.885 25.104  1.00 18.39 ? 81  PHE B CB  1 
ATOM   4361 C  CG  . PHE B 1 81  ? -6.322  -17.543 25.183  1.00 17.29 ? 81  PHE B CG  1 
ATOM   4362 C  CD1 . PHE B 1 81  ? -5.898  -18.109 26.381  1.00 19.51 ? 81  PHE B CD1 1 
ATOM   4363 C  CD2 . PHE B 1 81  ? -5.462  -17.578 24.095  1.00 17.68 ? 81  PHE B CD2 1 
ATOM   4364 C  CE1 . PHE B 1 81  ? -4.664  -18.721 26.472  1.00 20.06 ? 81  PHE B CE1 1 
ATOM   4365 C  CE2 . PHE B 1 81  ? -4.214  -18.166 24.201  1.00 17.79 ? 81  PHE B CE2 1 
ATOM   4366 C  CZ  . PHE B 1 81  ? -3.828  -18.736 25.391  1.00 18.57 ? 81  PHE B CZ  1 
ATOM   4367 N  N   . ALA B 1 82  ? -8.646  -19.458 23.037  1.00 14.99 ? 82  ALA B N   1 
ATOM   4368 C  CA  . ALA B 1 82  ? -8.768  -19.908 21.633  1.00 14.50 ? 82  ALA B CA  1 
ATOM   4369 C  C   . ALA B 1 82  ? -10.095 -20.654 21.436  1.00 14.50 ? 82  ALA B C   1 
ATOM   4370 O  O   . ALA B 1 82  ? -10.383 -21.075 20.305  1.00 13.53 ? 82  ALA B O   1 
ATOM   4371 C  CB  . ALA B 1 82  ? -7.598  -20.777 21.253  1.00 14.88 ? 82  ALA B CB  1 
ATOM   4372 N  N   . GLY B 1 83  ? -10.884 -20.867 22.483  1.00 14.39 ? 83  GLY B N   1 
ATOM   4373 C  CA  . GLY B 1 83  ? -12.270 -21.363 22.393  1.00 14.43 ? 83  GLY B CA  1 
ATOM   4374 C  C   . GLY B 1 83  ? -12.403 -22.639 21.576  1.00 13.50 ? 83  GLY B C   1 
ATOM   4375 O  O   . GLY B 1 83  ? -11.534 -23.561 21.719  1.00 13.93 ? 83  GLY B O   1 
ATOM   4376 N  N   . ASP B 1 84  ? -13.417 -22.724 20.712  1.00 13.54 ? 84  ASP B N   1 
ATOM   4377 C  CA  . ASP B 1 84  ? -13.633 -23.887 19.853  1.00 14.14 ? 84  ASP B CA  1 
ATOM   4378 C  C   . ASP B 1 84  ? -13.172 -23.544 18.437  1.00 13.00 ? 84  ASP B C   1 
ATOM   4379 O  O   . ASP B 1 84  ? -13.723 -24.073 17.471  1.00 15.22 ? 84  ASP B O   1 
ATOM   4380 C  CB  . ASP B 1 84  ? -15.079 -24.361 19.902  1.00 14.25 ? 84  ASP B CB  1 
ATOM   4381 C  CG  . ASP B 1 84  ? -16.122 -23.356 19.541  1.00 14.18 ? 84  ASP B CG  1 
ATOM   4382 O  OD1 . ASP B 1 84  ? -15.768 -22.195 19.317  1.00 16.11 ? 84  ASP B OD1 1 
ATOM   4383 O  OD2 . ASP B 1 84  ? -17.291 -23.782 19.504  1.00 18.63 ? 84  ASP B OD2 1 
ATOM   4384 N  N   . GLY B 1 85  ? -12.059 -22.812 18.372  1.00 13.13 ? 85  GLY B N   1 
ATOM   4385 C  CA  . GLY B 1 85  ? -11.268 -22.712 17.142  1.00 12.46 ? 85  GLY B CA  1 
ATOM   4386 C  C   . GLY B 1 85  ? -10.696 -24.070 16.774  1.00 13.95 ? 85  GLY B C   1 
ATOM   4387 O  O   . GLY B 1 85  ? -10.815 -25.065 17.564  1.00 12.90 ? 85  GLY B O   1 
ATOM   4388 N  N   . LEU B 1 86  ? -10.121 -24.207 15.603  1.00 11.43 ? 86  LEU B N   1 
ATOM   4389 C  CA  . LEU B 1 86  ? -9.758  -25.550 15.078  1.00 11.47 ? 86  LEU B CA  1 
ATOM   4390 C  C   . LEU B 1 86  ? -8.746  -26.280 15.970  1.00 11.54 ? 86  LEU B C   1 
ATOM   4391 O  O   . LEU B 1 86  ? -8.786  -27.507 16.002  1.00 12.76 ? 86  LEU B O   1 
ATOM   4392 C  CB  . LEU B 1 86  ? -9.177  -25.403 13.676  1.00 11.99 ? 86  LEU B CB  1 
ATOM   4393 C  CG  . LEU B 1 86  ? -10.185 -25.132 12.553  1.00 12.77 ? 86  LEU B CG  1 
ATOM   4394 C  CD1 . LEU B 1 86  ? -9.427  -24.757 11.288  1.00 14.70 ? 86  LEU B CD1 1 
ATOM   4395 C  CD2 . LEU B 1 86  ? -11.054 -26.342 12.312  1.00 13.99 ? 86  LEU B CD2 1 
ATOM   4396 N  N   . PHE B 1 87  ? -7.837  -25.554 16.627  1.00 10.95 ? 87  PHE B N   1 
ATOM   4397 C  CA  . PHE B 1 87  ? -6.730  -26.205 17.375  1.00 11.34 ? 87  PHE B CA  1 
ATOM   4398 C  C   . PHE B 1 87  ? -7.177  -26.718 18.731  1.00 11.96 ? 87  PHE B C   1 
ATOM   4399 O  O   . PHE B 1 87  ? -6.614  -27.667 19.197  1.00 12.52 ? 87  PHE B O   1 
ATOM   4400 C  CB  . PHE B 1 87  ? -5.587  -25.179 17.435  1.00 12.82 ? 87  PHE B CB  1 
ATOM   4401 C  CG  . PHE B 1 87  ? -4.380  -25.573 18.237  1.00 12.75 ? 87  PHE B CG  1 
ATOM   4402 C  CD1 . PHE B 1 87  ? -3.652  -26.698 17.919  1.00 13.22 ? 87  PHE B CD1 1 
ATOM   4403 C  CD2 . PHE B 1 87  ? -3.923  -24.734 19.237  1.00 15.45 ? 87  PHE B CD2 1 
ATOM   4404 C  CE1 . PHE B 1 87  ? -2.516  -27.015 18.649  1.00 14.67 ? 87  PHE B CE1 1 
ATOM   4405 C  CE2 . PHE B 1 87  ? -2.784  -25.049 19.952  1.00 16.56 ? 87  PHE B CE2 1 
ATOM   4406 C  CZ  . PHE B 1 87  ? -2.081  -26.191 19.642  1.00 15.28 ? 87  PHE B CZ  1 
ATOM   4407 N  N   . THR B 1 88  ? -8.139  -26.052 19.359  1.00 12.74 ? 88  THR B N   1 
ATOM   4408 C  CA  . THR B 1 88  ? -8.562  -26.343 20.754  1.00 11.61 ? 88  THR B CA  1 
ATOM   4409 C  C   . THR B 1 88  ? -9.967  -26.924 20.776  1.00 12.37 ? 88  THR B C   1 
ATOM   4410 O  O   . THR B 1 88  ? -10.575 -26.955 21.855  1.00 13.45 ? 88  THR B O   1 
ATOM   4411 C  CB  . THR B 1 88  ? -8.367  -25.121 21.650  1.00 12.54 ? 88  THR B CB  1 
ATOM   4412 O  OG1 . THR B 1 88  ? -8.990  -23.980 21.074  1.00 12.98 ? 88  THR B OG1 1 
ATOM   4413 C  CG2 . THR B 1 88  ? -6.919  -24.820 21.912  1.00 13.45 ? 88  THR B CG2 1 
ATOM   4414 N  N   . SER B 1 89  ? -10.449 -27.413 19.649  1.00 11.36 ? 89  SER B N   1 
ATOM   4415 C  CA  . SER B 1 89  ? -11.739 -28.108 19.604  1.00 11.96 ? 89  SER B CA  1 
ATOM   4416 C  C   . SER B 1 89  ? -11.528 -29.631 19.585  1.00 11.32 ? 89  SER B C   1 
ATOM   4417 O  O   . SER B 1 89  ? -10.507 -30.167 19.084  1.00 13.20 ? 89  SER B O   1 
ATOM   4418 C  CB  . SER B 1 89  ? -12.625 -27.645 18.456  1.00 14.66 ? 89  SER B CB  1 
ATOM   4419 O  OG  . SER B 1 89  ? -11.954 -27.683 17.240  1.00 18.07 ? 89  SER B OG  1 
ATOM   4420 N  N   . TRP B 1 90  ? -12.537 -30.321 20.116  1.00 11.91 ? 90  TRP B N   1 
ATOM   4421 C  CA  . TRP B 1 90  ? -12.606 -31.780 19.981  1.00 12.03 ? 90  TRP B CA  1 
ATOM   4422 C  C   . TRP B 1 90  ? -13.186 -32.101 18.603  1.00 11.03 ? 90  TRP B C   1 
ATOM   4423 O  O   . TRP B 1 90  ? -14.085 -31.383 18.093  1.00 12.35 ? 90  TRP B O   1 
ATOM   4424 C  CB  . TRP B 1 90  ? -13.498 -32.367 21.076  1.00 11.86 ? 90  TRP B CB  1 
ATOM   4425 C  CG  . TRP B 1 90  ? -13.031 -32.047 22.452  1.00 12.31 ? 90  TRP B CG  1 
ATOM   4426 C  CD1 . TRP B 1 90  ? -13.390 -30.973 23.221  1.00 14.02 ? 90  TRP B CD1 1 
ATOM   4427 C  CD2 . TRP B 1 90  ? -12.107 -32.826 23.249  1.00 12.53 ? 90  TRP B CD2 1 
ATOM   4428 N  NE1 . TRP B 1 90  ? -12.772 -31.054 24.437  1.00 15.23 ? 90  TRP B NE1 1 
ATOM   4429 C  CE2 . TRP B 1 90  ? -11.947 -32.131 24.461  1.00 13.11 ? 90  TRP B CE2 1 
ATOM   4430 C  CE3 . TRP B 1 90  ? -11.353 -33.996 23.041  1.00 14.41 ? 90  TRP B CE3 1 
ATOM   4431 C  CZ2 . TRP B 1 90  ? -11.151 -32.622 25.505  1.00 13.82 ? 90  TRP B CZ2 1 
ATOM   4432 C  CZ3 . TRP B 1 90  ? -10.559 -34.469 24.074  1.00 13.62 ? 90  TRP B CZ3 1 
ATOM   4433 C  CH2 . TRP B 1 90  ? -10.417 -33.752 25.256  1.00 14.81 ? 90  TRP B CH2 1 
ATOM   4434 N  N   . THR B 1 91  ? -12.788 -33.204 18.006  1.00 10.51 ? 91  THR B N   1 
ATOM   4435 C  CA  . THR B 1 91  ? -13.199 -33.606 16.647  1.00 11.00 ? 91  THR B CA  1 
ATOM   4436 C  C   . THR B 1 91  ? -14.722 -33.699 16.560  1.00 11.99 ? 91  THR B C   1 
ATOM   4437 O  O   . THR B 1 91  ? -15.313 -33.527 15.476  1.00 12.79 ? 91  THR B O   1 
ATOM   4438 C  CB  . THR B 1 91  ? -12.491 -34.914 16.293  1.00 10.96 ? 91  THR B CB  1 
ATOM   4439 O  OG1 . THR B 1 91  ? -11.089 -34.732 16.472  1.00 10.92 ? 91  THR B OG1 1 
ATOM   4440 C  CG2 . THR B 1 91  ? -12.813 -35.386 14.903  1.00 11.66 ? 91  THR B CG2 1 
ATOM   4441 N  N   . HIS B 1 92  ? -15.367 -34.104 17.657  1.00 11.44 ? 92  HIS B N   1 
ATOM   4442 C  CA  . HIS B 1 92  ? -16.825 -34.364 17.688  1.00 11.32 ? 92  HIS B CA  1 
ATOM   4443 C  C   . HIS B 1 92  ? -17.628 -33.090 17.865  1.00 12.33 ? 92  HIS B C   1 
ATOM   4444 O  O   . HIS B 1 92  ? -18.905 -33.191 17.788  1.00 13.86 ? 92  HIS B O   1 
ATOM   4445 C  CB  . HIS B 1 92  ? -17.144 -35.413 18.736  1.00 11.51 ? 92  HIS B CB  1 
ATOM   4446 C  CG  . HIS B 1 92  ? -16.549 -35.125 20.080  1.00 11.51 ? 92  HIS B CG  1 
ATOM   4447 N  ND1 . HIS B 1 92  ? -17.064 -34.178 20.927  1.00 12.42 ? 92  HIS B ND1 1 
ATOM   4448 C  CD2 . HIS B 1 92  ? -15.483 -35.687 20.713  1.00 13.50 ? 92  HIS B CD2 1 
ATOM   4449 C  CE1 . HIS B 1 92  ? -16.356 -34.193 22.071  1.00 12.60 ? 92  HIS B CE1 1 
ATOM   4450 N  NE2 . HIS B 1 92  ? -15.362 -35.089 21.921  1.00 14.05 ? 92  HIS B NE2 1 
ATOM   4451 N  N   . GLU B 1 93  ? -17.006 -31.947 18.106  1.00 11.48 ? 93  GLU B N   1 
ATOM   4452 C  CA  . GLU B 1 93  ? -17.768 -30.667 18.269  1.00 12.15 ? 93  GLU B CA  1 
ATOM   4453 C  C   . GLU B 1 93  ? -18.192 -30.220 16.874  1.00 14.20 ? 93  GLU B C   1 
ATOM   4454 O  O   . GLU B 1 93  ? -17.406 -30.242 15.973  1.00 14.20 ? 93  GLU B O   1 
ATOM   4455 C  CB  . GLU B 1 93  ? -16.937 -29.634 18.999  1.00 13.56 ? 93  GLU B CB  1 
ATOM   4456 C  CG  . GLU B 1 93  ? -16.756 -29.933 20.478  1.00 13.99 ? 93  GLU B CG  1 
ATOM   4457 C  CD  . GLU B 1 93  ? -16.009 -28.805 21.108  1.00 15.11 ? 93  GLU B CD  1 
ATOM   4458 O  OE1 . GLU B 1 93  ? -14.748 -28.815 21.038  1.00 14.87 ? 93  GLU B OE1 1 
ATOM   4459 O  OE2 . GLU B 1 93  ? -16.629 -27.861 21.637  1.00 15.68 ? 93  GLU B OE2 1 
ATOM   4460 N  N   . LYS B 1 94  ? -19.473 -29.852 16.729  1.00 13.40 ? 94  LYS B N   1 
ATOM   4461 C  CA  . LYS B 1 94  ? -19.991 -29.338 15.451  1.00 13.47 ? 94  LYS B CA  1 
ATOM   4462 C  C   . LYS B 1 94  ? -19.079 -28.279 14.851  1.00 13.34 ? 94  LYS B C   1 
ATOM   4463 O  O   . LYS B 1 94  ? -18.873 -28.302 13.610  1.00 13.55 ? 94  LYS B O   1 
ATOM   4464 C  CB  . LYS B 1 94  ? -21.407 -28.822 15.662  1.00 14.48 ? 94  LYS B CB  1 
ATOM   4465 C  CG  . LYS B 1 94  ? -22.009 -28.165 14.446  1.00 15.73 ? 94  LYS B CG  1 
ATOM   4466 C  CD  . LYS B 1 94  ? -23.484 -27.777 14.707  1.00 18.72 ? 94  LYS B CD  1 
ATOM   4467 C  CE  . LYS B 1 94  ? -24.098 -27.117 13.512  1.00 20.72 ? 94  LYS B CE  1 
ATOM   4468 N  NZ  . LYS B 1 94  ? -25.528 -26.859 13.820  1.00 23.86 ? 94  LYS B NZ  1 
ATOM   4469 N  N   . ASN B 1 95  ? -18.585 -27.358 15.653  1.00 12.62 ? 95  ASN B N   1 
ATOM   4470 C  CA  . ASN B 1 95  ? -17.806 -26.222 15.125  1.00 12.07 ? 95  ASN B CA  1 
ATOM   4471 C  C   . ASN B 1 95  ? -16.444 -26.689 14.597  1.00 12.21 ? 95  ASN B C   1 
ATOM   4472 O  O   . ASN B 1 95  ? -15.843 -25.937 13.844  1.00 13.25 ? 95  ASN B O   1 
ATOM   4473 C  CB  . ASN B 1 95  ? -17.650 -25.104 16.146  1.00 14.56 ? 95  ASN B CB  1 
ATOM   4474 C  CG  . ASN B 1 95  ? -18.782 -24.103 16.118  1.00 18.30 ? 95  ASN B CG  1 
ATOM   4475 O  OD1 . ASN B 1 95  ? -19.467 -23.945 15.101  1.00 23.03 ? 95  ASN B OD1 1 
ATOM   4476 N  ND2 . ASN B 1 95  ? -18.931 -23.394 17.204  1.00 17.77 ? 95  ASN B ND2 1 
ATOM   4477 N  N   . TRP B 1 96  ? -15.962 -27.852 15.012  1.00 11.55 ? 96  TRP B N   1 
ATOM   4478 C  CA  . TRP B 1 96  ? -14.684 -28.324 14.407  1.00 10.49 ? 96  TRP B CA  1 
ATOM   4479 C  C   . TRP B 1 96  ? -14.896 -28.691 12.940  1.00 11.57 ? 96  TRP B C   1 
ATOM   4480 O  O   . TRP B 1 96  ? -14.198 -28.154 12.082  1.00 11.75 ? 96  TRP B O   1 
ATOM   4481 C  CB  . TRP B 1 96  ? -14.047 -29.495 15.184  1.00 11.19 ? 96  TRP B CB  1 
ATOM   4482 C  CG  . TRP B 1 96  ? -12.804 -29.933 14.462  1.00 10.72 ? 96  TRP B CG  1 
ATOM   4483 C  CD1 . TRP B 1 96  ? -11.600 -29.274 14.481  1.00 12.88 ? 96  TRP B CD1 1 
ATOM   4484 C  CD2 . TRP B 1 96  ? -12.707 -30.940 13.450  1.00 11.61 ? 96  TRP B CD2 1 
ATOM   4485 N  NE1 . TRP B 1 96  ? -10.754 -29.840 13.594  1.00 13.05 ? 96  TRP B NE1 1 
ATOM   4486 C  CE2 . TRP B 1 96  ? -11.397 -30.847 12.921  1.00 12.28 ? 96  TRP B CE2 1 
ATOM   4487 C  CE3 . TRP B 1 96  ? -13.562 -31.906 12.937  1.00 12.22 ? 96  TRP B CE3 1 
ATOM   4488 C  CZ2 . TRP B 1 96  ? -10.946 -31.717 11.914  1.00 12.23 ? 96  TRP B CZ2 1 
ATOM   4489 C  CZ3 . TRP B 1 96  ? -13.123 -32.754 11.948  1.00 11.74 ? 96  TRP B CZ3 1 
ATOM   4490 C  CH2 . TRP B 1 96  ? -11.820 -32.653 11.444  1.00 13.43 ? 96  TRP B CH2 1 
ATOM   4491 N  N   . LYS B 1 97  ? -15.842 -29.566 12.668  1.00 12.02 ? 97  LYS B N   1 
ATOM   4492 C  CA  . LYS B 1 97  ? -16.012 -30.028 11.288  1.00 13.07 ? 97  LYS B CA  1 
ATOM   4493 C  C   . LYS B 1 97  ? -16.499 -28.877 10.411  1.00 12.22 ? 97  LYS B C   1 
ATOM   4494 O  O   . LYS B 1 97  ? -16.043 -28.796 9.266   1.00 13.74 ? 97  LYS B O   1 
ATOM   4495 C  CB  . LYS B 1 97  ? -16.979 -31.206 11.222  1.00 15.79 ? 97  LYS B CB  1 
ATOM   4496 C  CG  . LYS B 1 97  ? -16.989 -31.914 9.875   1.00 18.50 ? 97  LYS B CG  1 
ATOM   4497 C  CD  . LYS B 1 97  ? -15.642 -32.455 9.448   1.00 23.72 ? 97  LYS B CD  1 
ATOM   4498 C  CE  . LYS B 1 97  ? -15.656 -33.225 8.147   1.00 25.44 ? 97  LYS B CE  1 
ATOM   4499 N  NZ  . LYS B 1 97  ? -16.889 -34.024 8.014   1.00 34.05 ? 97  LYS B NZ  1 
ATOM   4500 N  N   . LYS B 1 98  ? -17.355 -28.014 10.939  1.00 12.04 ? 98  LYS B N   1 
ATOM   4501 C  CA  . LYS B 1 98  ? -17.820 -26.874 10.121  1.00 12.79 ? 98  LYS B CA  1 
ATOM   4502 C  C   . LYS B 1 98  ? -16.626 -26.025 9.743   1.00 12.25 ? 98  LYS B C   1 
ATOM   4503 O  O   . LYS B 1 98  ? -16.432 -25.727 8.548   1.00 11.92 ? 98  LYS B O   1 
ATOM   4504 C  CB  . LYS B 1 98  ? -18.770 -25.958 10.901  1.00 16.86 ? 98  LYS B CB  1 
ATOM   4505 C  CG  . LYS B 1 98  ? -20.210 -26.396 10.967  1.00 19.66 ? 98  LYS B CG  1 
ATOM   4506 C  CD  . LYS B 1 98  ? -21.068 -25.482 11.842  1.00 20.14 ? 98  LYS B CD  1 
ATOM   4507 C  CE  . LYS B 1 98  ? -20.938 -24.028 11.552  1.00 21.30 ? 98  LYS B CE  1 
ATOM   4508 N  NZ  . LYS B 1 98  ? -22.097 -23.222 12.085  1.00 20.86 ? 98  LYS B NZ  1 
ATOM   4509 N  N   . ALA B 1 99  ? -15.789 -25.645 10.679  1.00 12.19 ? 99  ALA B N   1 
ATOM   4510 C  CA  . ALA B 1 99  ? -14.647 -24.757 10.342  1.00 11.89 ? 99  ALA B CA  1 
ATOM   4511 C  C   . ALA B 1 99  ? -13.648 -25.488 9.439   1.00 13.01 ? 99  ALA B C   1 
ATOM   4512 O  O   . ALA B 1 99  ? -13.069 -24.854 8.564   1.00 14.24 ? 99  ALA B O   1 
ATOM   4513 C  CB  . ALA B 1 99  ? -13.994 -24.206 11.608  1.00 13.53 ? 99  ALA B CB  1 
ATOM   4514 N  N   . HIS B 1 100 ? -13.414 -26.765 9.694   1.00 12.11 ? 100 HIS B N   1 
ATOM   4515 C  CA  . HIS B 1 100 ? -12.491 -27.591 8.891   1.00 11.86 ? 100 HIS B CA  1 
ATOM   4516 C  C   . HIS B 1 100 ? -12.938 -27.515 7.423   1.00 13.63 ? 100 HIS B C   1 
ATOM   4517 O  O   . HIS B 1 100 ? -12.117 -27.254 6.532   1.00 14.55 ? 100 HIS B O   1 
ATOM   4518 C  CB  . HIS B 1 100 ? -12.517 -28.983 9.483   1.00 13.63 ? 100 HIS B CB  1 
ATOM   4519 C  CG  . HIS B 1 100 ? -11.788 -30.044 8.764   1.00 13.72 ? 100 HIS B CG  1 
ATOM   4520 N  ND1 . HIS B 1 100 ? -10.403 -30.172 8.865   1.00 14.72 ? 100 HIS B ND1 1 
ATOM   4521 C  CD2 . HIS B 1 100 ? -12.214 -31.106 8.074   1.00 14.27 ? 100 HIS B CD2 1 
ATOM   4522 C  CE1 . HIS B 1 100 ? -10.044 -31.261 8.218   1.00 14.86 ? 100 HIS B CE1 1 
ATOM   4523 N  NE2 . HIS B 1 100 ? -11.125 -31.851 7.721   1.00 17.23 ? 100 HIS B NE2 1 
ATOM   4524 N  N   . ASN B 1 101 ? -14.217 -27.777 7.195   1.00 13.42 ? 101 ASN B N   1 
ATOM   4525 C  CA  . ASN B 1 101 ? -14.703 -27.868 5.804   1.00 13.25 ? 101 ASN B CA  1 
ATOM   4526 C  C   . ASN B 1 101 ? -14.663 -26.481 5.174   1.00 14.33 ? 101 ASN B C   1 
ATOM   4527 O  O   . ASN B 1 101 ? -14.443 -26.397 3.938   1.00 16.52 ? 101 ASN B O   1 
ATOM   4528 C  CB  . ASN B 1 101 ? -16.137 -28.388 5.787   1.00 13.88 ? 101 ASN B CB  1 
ATOM   4529 C  CG  . ASN B 1 101 ? -16.264 -29.855 6.084   1.00 14.21 ? 101 ASN B CG  1 
ATOM   4530 O  OD1 . ASN B 1 101 ? -15.284 -30.615 6.022   1.00 15.93 ? 101 ASN B OD1 1 
ATOM   4531 N  ND2 . ASN B 1 101 ? -17.479 -30.297 6.318   1.00 15.07 ? 101 ASN B ND2 1 
ATOM   4532 N  N   . ILE B 1 102 ? -14.971 -25.454 5.928   1.00 12.90 ? 102 ILE B N   1 
ATOM   4533 C  CA  . ILE B 1 102 ? -14.998 -24.050 5.388   1.00 12.70 ? 102 ILE B CA  1 
ATOM   4534 C  C   . ILE B 1 102 ? -13.571 -23.586 5.087   1.00 16.11 ? 102 ILE B C   1 
ATOM   4535 O  O   . ILE B 1 102 ? -13.359 -22.866 4.059   1.00 18.54 ? 102 ILE B O   1 
ATOM   4536 C  CB  . ILE B 1 102 ? -15.741 -23.106 6.334   1.00 14.14 ? 102 ILE B CB  1 
ATOM   4537 C  CG1 . ILE B 1 102 ? -17.256 -23.382 6.334   1.00 15.57 ? 102 ILE B CG1 1 
ATOM   4538 C  CG2 . ILE B 1 102 ? -15.492 -21.649 6.023   1.00 17.06 ? 102 ILE B CG2 1 
ATOM   4539 C  CD1 . ILE B 1 102 ? -17.982 -22.818 7.474   1.00 15.53 ? 102 ILE B CD1 1 
ATOM   4540 N  N   . LEU B 1 103 ? -12.620 -23.876 5.965   1.00 14.72 ? 103 LEU B N   1 
ATOM   4541 C  CA  . LEU B 1 103 ? -11.274 -23.240 5.867   1.00 13.63 ? 103 LEU B CA  1 
ATOM   4542 C  C   . LEU B 1 103 ? -10.312 -24.088 5.058   1.00 15.66 ? 103 LEU B C   1 
ATOM   4543 O  O   . LEU B 1 103 ? -9.338  -23.505 4.507   1.00 16.04 ? 103 LEU B O   1 
ATOM   4544 C  CB  . LEU B 1 103 ? -10.750 -23.020 7.300   1.00 14.25 ? 103 LEU B CB  1 
ATOM   4545 C  CG  . LEU B 1 103 ? -11.359 -21.811 7.986   1.00 14.84 ? 103 LEU B CG  1 
ATOM   4546 C  CD1 . LEU B 1 103 ? -11.191 -21.881 9.490   1.00 19.00 ? 103 LEU B CD1 1 
ATOM   4547 C  CD2 . LEU B 1 103 ? -10.769 -20.515 7.407   1.00 17.56 ? 103 LEU B CD2 1 
ATOM   4548 N  N   . LEU B 1 104 ? -10.455 -25.406 4.925   1.00 16.29 ? 104 LEU B N   1 
ATOM   4549 C  CA  . LEU B 1 104 ? -9.397  -26.229 4.263   1.00 18.61 ? 104 LEU B CA  1 
ATOM   4550 C  C   . LEU B 1 104 ? -9.134  -25.762 2.827   1.00 23.23 ? 104 LEU B C   1 
ATOM   4551 O  O   . LEU B 1 104 ? -7.969  -25.574 2.458   1.00 20.40 ? 104 LEU B O   1 
ATOM   4552 C  CB  . LEU B 1 104 ? -9.758  -27.729 4.387   1.00 22.06 ? 104 LEU B CB  1 
ATOM   4553 C  CG  . LEU B 1 104 ? -8.970  -28.537 5.383   1.00 25.91 ? 104 LEU B CG  1 
ATOM   4554 C  CD1 . LEU B 1 104 ? -9.444  -29.987 5.379   1.00 30.16 ? 104 LEU B CD1 1 
ATOM   4555 C  CD2 . LEU B 1 104 ? -7.486  -28.488 5.139   1.00 25.45 ? 104 LEU B CD2 1 
ATOM   4556 N  N   . PRO B 1 105 ? -10.165 -25.468 2.021   1.00 26.92 ? 105 PRO B N   1 
ATOM   4557 C  CA  . PRO B 1 105 ? -9.994  -24.790 0.725   1.00 33.60 ? 105 PRO B CA  1 
ATOM   4558 C  C   . PRO B 1 105 ? -9.117  -23.524 0.745   1.00 33.24 ? 105 PRO B C   1 
ATOM   4559 O  O   . PRO B 1 105 ? -8.271  -23.424 -0.193  1.00 39.71 ? 105 PRO B O   1 
ATOM   4560 C  CB  . PRO B 1 105 ? -11.440 -24.399 0.318   1.00 35.17 ? 105 PRO B CB  1 
ATOM   4561 C  CG  . PRO B 1 105 ? -12.259 -24.635 1.592   1.00 34.60 ? 105 PRO B CG  1 
ATOM   4562 C  CD  . PRO B 1 105 ? -11.576 -25.803 2.274   1.00 29.95 ? 105 PRO B CD  1 
ATOM   4563 N  N   . SER B 1 106 ? -9.302  -22.637 1.746   1.00 25.70 ? 106 SER B N   1 
ATOM   4564 C  CA  . SER B 1 106 ? -8.570  -21.354 1.959   1.00 24.64 ? 106 SER B CA  1 
ATOM   4565 C  C   . SER B 1 106 ? -7.080  -21.638 2.231   1.00 22.12 ? 106 SER B C   1 
ATOM   4566 O  O   . SER B 1 106 ? -6.282  -20.653 2.259   1.00 20.61 ? 106 SER B O   1 
ATOM   4567 C  CB  . SER B 1 106 ? -9.149  -20.543 3.073   1.00 32.83 ? 106 SER B CB  1 
ATOM   4568 O  OG  . SER B 1 106 ? -10.489 -20.154 2.797   1.00 43.73 ? 106 SER B OG  1 
ATOM   4569 N  N   . PHE B 1 107 ? -6.675  -22.878 2.454   1.00 19.84 ? 107 PHE B N   1 
ATOM   4570 C  CA  . PHE B 1 107 ? -5.286  -23.154 2.974   1.00 21.21 ? 107 PHE B CA  1 
ATOM   4571 C  C   . PHE B 1 107 ? -4.514  -24.100 2.067   1.00 21.25 ? 107 PHE B C   1 
ATOM   4572 O  O   . PHE B 1 107 ? -3.375  -24.567 2.459   1.00 22.10 ? 107 PHE B O   1 
ATOM   4573 C  CB  . PHE B 1 107 ? -5.333  -23.681 4.400   1.00 19.03 ? 107 PHE B CB  1 
ATOM   4574 C  CG  . PHE B 1 107 ? -5.354  -22.674 5.508   1.00 19.79 ? 107 PHE B CG  1 
ATOM   4575 C  CD1 . PHE B 1 107 ? -4.205  -21.956 5.866   1.00 17.88 ? 107 PHE B CD1 1 
ATOM   4576 C  CD2 . PHE B 1 107 ? -6.514  -22.383 6.168   1.00 17.25 ? 107 PHE B CD2 1 
ATOM   4577 C  CE1 . PHE B 1 107 ? -4.251  -21.027 6.879   1.00 20.10 ? 107 PHE B CE1 1 
ATOM   4578 C  CE2 . PHE B 1 107 ? -6.553  -21.494 7.226   1.00 19.70 ? 107 PHE B CE2 1 
ATOM   4579 C  CZ  . PHE B 1 107 ? -5.410  -20.802 7.570   1.00 22.97 ? 107 PHE B CZ  1 
ATOM   4580 N  N   . SER B 1 108 ? -5.040  -24.330 0.845   1.00 20.84 ? 108 SER B N   1 
ATOM   4581 C  CA  . SER B 1 108 ? -4.487  -25.279 -0.136  1.00 25.63 ? 108 SER B CA  1 
ATOM   4582 C  C   . SER B 1 108 ? -3.133  -24.771 -0.626  1.00 28.67 ? 108 SER B C   1 
ATOM   4583 O  O   . SER B 1 108 ? -2.931  -23.534 -0.650  1.00 27.39 ? 108 SER B O   1 
ATOM   4584 C  CB  . SER B 1 108 ? -5.435  -25.474 -1.345  1.00 26.69 ? 108 SER B CB  1 
ATOM   4585 O  OG  . SER B 1 108 ? -6.005  -24.256 -1.804  1.00 30.96 ? 108 SER B OG  1 
ATOM   4586 N  N   . GLN B 1 109 ? -2.281  -25.684 -1.076  1.00 27.75 ? 109 GLN B N   1 
ATOM   4587 C  CA  . GLN B 1 109 ? -1.089  -25.280 -1.860  1.00 30.59 ? 109 GLN B CA  1 
ATOM   4588 C  C   . GLN B 1 109 ? -1.541  -24.253 -2.914  1.00 29.48 ? 109 GLN B C   1 
ATOM   4589 O  O   . GLN B 1 109 ? -0.847  -23.229 -3.131  1.00 25.58 ? 109 GLN B O   1 
ATOM   4590 C  CB  . GLN B 1 109 ? -0.464  -26.511 -2.520  1.00 29.58 ? 109 GLN B CB  1 
ATOM   4591 C  CG  . GLN B 1 109 ? 0.815   -26.206 -3.262  1.00 30.11 ? 109 GLN B CG  1 
ATOM   4592 C  CD  . GLN B 1 109 ? 1.724   -25.274 -2.500  1.00 32.18 ? 109 GLN B CD  1 
ATOM   4593 O  OE1 . GLN B 1 109 ? 2.270   -24.314 -3.057  1.00 32.66 ? 109 GLN B OE1 1 
ATOM   4594 N  NE2 . GLN B 1 109 ? 1.910   -25.557 -1.217  1.00 35.68 ? 109 GLN B NE2 1 
ATOM   4595 N  N   . GLN B 1 110 ? -2.684  -24.476 -3.567  1.00 28.87 ? 110 GLN B N   1 
ATOM   4596 C  CA  . GLN B 1 110 ? -3.136  -23.611 -4.680  1.00 29.94 ? 110 GLN B CA  1 
ATOM   4597 C  C   . GLN B 1 110 ? -3.624  -22.265 -4.145  1.00 26.99 ? 110 GLN B C   1 
ATOM   4598 O  O   . GLN B 1 110 ? -3.357  -21.198 -4.835  1.00 19.93 ? 110 GLN B O   1 
ATOM   4599 C  CB  . GLN B 1 110 ? -4.083  -24.404 -5.572  1.00 34.57 ? 110 GLN B CB  1 
ATOM   4600 C  CG  . GLN B 1 110 ? -3.330  -25.503 -6.299  1.00 37.56 ? 110 GLN B CG  1 
ATOM   4601 C  CD  . GLN B 1 110 ? -2.365  -24.906 -7.300  1.00 39.15 ? 110 GLN B CD  1 
ATOM   4602 O  OE1 . GLN B 1 110 ? -2.781  -24.194 -8.210  1.00 44.48 ? 110 GLN B OE1 1 
ATOM   4603 N  NE2 . GLN B 1 110 ? -1.068  -25.116 -7.093  1.00 46.73 ? 110 GLN B NE2 1 
ATOM   4604 N  N   . ALA B 1 111 ? -4.188  -22.229 -2.915  1.00 26.73 ? 111 ALA B N   1 
ATOM   4605 C  CA  . ALA B 1 111 ? -4.681  -20.964 -2.333  1.00 26.56 ? 111 ALA B CA  1 
ATOM   4606 C  C   . ALA B 1 111 ? -3.517  -19.995 -2.053  1.00 20.39 ? 111 ALA B C   1 
ATOM   4607 O  O   . ALA B 1 111 ? -3.747  -18.797 -1.966  1.00 24.54 ? 111 ALA B O   1 
ATOM   4608 C  CB  . ALA B 1 111 ? -5.432  -21.284 -1.060  1.00 27.55 ? 111 ALA B CB  1 
ATOM   4609 N  N   . MET B 1 112 ? -2.309  -20.553 -1.886  1.00 24.24 ? 112 MET B N   1 
ATOM   4610 C  CA  . MET B 1 112 ? -1.134  -19.733 -1.597  1.00 23.33 ? 112 MET B CA  1 
ATOM   4611 C  C   . MET B 1 112 ? -0.916  -18.705 -2.710  1.00 19.39 ? 112 MET B C   1 
ATOM   4612 O  O   . MET B 1 112 ? -0.276  -17.781 -2.444  1.00 19.48 ? 112 MET B O   1 
ATOM   4613 C  CB  . MET B 1 112 ? 0.101   -20.609 -1.397  1.00 21.59 ? 112 MET B CB  1 
ATOM   4614 C  CG  . MET B 1 112 ? -0.042  -21.567 -0.244  1.00 22.80 ? 112 MET B CG  1 
ATOM   4615 S  SD  . MET B 1 112 ? -0.507  -20.704 1.260   1.00 22.11 ? 112 MET B SD  1 
ATOM   4616 C  CE  . MET B 1 112 ? -2.106  -21.437 1.552   1.00 26.50 ? 112 MET B CE  1 
ATOM   4617 N  N   . LYS B 1 113 ? -1.425  -18.934 -3.955  1.00 20.23 ? 113 LYS B N   1 
ATOM   4618 C  CA  . LYS B 1 113 ? -1.153  -17.993 -5.066  1.00 17.89 ? 113 LYS B CA  1 
ATOM   4619 C  C   . LYS B 1 113 ? -1.715  -16.627 -4.706  1.00 18.88 ? 113 LYS B C   1 
ATOM   4620 O  O   . LYS B 1 113 ? -1.091  -15.641 -5.069  1.00 19.24 ? 113 LYS B O   1 
ATOM   4621 C  CB  . LYS B 1 113 ? -1.727  -18.518 -6.398  1.00 18.17 ? 113 LYS B CB  1 
ATOM   4622 C  CG  . LYS B 1 113 ? -1.020  -19.744 -6.920  1.00 20.86 ? 113 LYS B CG  1 
ATOM   4623 C  CD  . LYS B 1 113 ? -1.728  -20.348 -8.162  1.00 22.56 ? 113 LYS B CD  1 
ATOM   4624 C  CE  . LYS B 1 113 ? -1.044  -21.589 -8.639  1.00 24.66 ? 113 LYS B CE  1 
ATOM   4625 N  NZ  . LYS B 1 113 ? -1.759  -22.211 -9.784  1.00 29.42 ? 113 LYS B NZ  1 
ATOM   4626 N  N   . GLY B 1 114 ? -2.869  -16.599 -4.059  1.00 19.38 ? 114 GLY B N   1 
ATOM   4627 C  CA  . GLY B 1 114 ? -3.518  -15.375 -3.633  1.00 19.41 ? 114 GLY B CA  1 
ATOM   4628 C  C   . GLY B 1 114 ? -2.810  -14.724 -2.465  1.00 19.27 ? 114 GLY B C   1 
ATOM   4629 O  O   . GLY B 1 114 ? -2.916  -13.525 -2.363  1.00 24.94 ? 114 GLY B O   1 
ATOM   4630 N  N   . TYR B 1 115 ? -2.195  -15.486 -1.556  1.00 15.23 ? 115 TYR B N   1 
ATOM   4631 C  CA  . TYR B 1 115 ? -1.501  -14.924 -0.367  1.00 15.00 ? 115 TYR B CA  1 
ATOM   4632 C  C   . TYR B 1 115 ? -0.100  -14.475 -0.759  1.00 15.75 ? 115 TYR B C   1 
ATOM   4633 O  O   . TYR B 1 115 ? 0.525   -13.720 -0.006  1.00 14.87 ? 115 TYR B O   1 
ATOM   4634 C  CB  . TYR B 1 115 ? -1.398  -15.931 0.793   1.00 14.58 ? 115 TYR B CB  1 
ATOM   4635 C  CG  . TYR B 1 115 ? -2.742  -16.431 1.291   1.00 14.99 ? 115 TYR B CG  1 
ATOM   4636 C  CD1 . TYR B 1 115 ? -3.785  -15.576 1.624   1.00 16.90 ? 115 TYR B CD1 1 
ATOM   4637 C  CD2 . TYR B 1 115 ? -2.992  -17.787 1.350   1.00 16.15 ? 115 TYR B CD2 1 
ATOM   4638 C  CE1 . TYR B 1 115 ? -5.016  -16.062 2.058   1.00 18.54 ? 115 TYR B CE1 1 
ATOM   4639 C  CE2 . TYR B 1 115 ? -4.224  -18.281 1.764   1.00 15.63 ? 115 TYR B CE2 1 
ATOM   4640 C  CZ  . TYR B 1 115 ? -5.255  -17.425 2.074   1.00 18.99 ? 115 TYR B CZ  1 
ATOM   4641 O  OH  . TYR B 1 115 ? -6.495  -17.922 2.452   1.00 21.62 ? 115 TYR B OH  1 
ATOM   4642 N  N   . HIS B 1 116 ? 0.433   -14.974 -1.863  1.00 14.71 ? 116 HIS B N   1 
ATOM   4643 C  CA  . HIS B 1 116 ? 1.885   -14.851 -2.153  1.00 13.89 ? 116 HIS B CA  1 
ATOM   4644 C  C   . HIS B 1 116 ? 2.267   -13.369 -2.121  1.00 14.46 ? 116 HIS B C   1 
ATOM   4645 O  O   . HIS B 1 116 ? 3.337   -13.032 -1.532  1.00 14.26 ? 116 HIS B O   1 
ATOM   4646 C  CB  . HIS B 1 116 ? 2.203   -15.529 -3.494  1.00 14.45 ? 116 HIS B CB  1 
ATOM   4647 C  CG  . HIS B 1 116 ? 3.627   -15.395 -3.920  1.00 13.43 ? 116 HIS B CG  1 
ATOM   4648 N  ND1 . HIS B 1 116 ? 4.610   -16.292 -3.538  1.00 13.70 ? 116 HIS B ND1 1 
ATOM   4649 C  CD2 . HIS B 1 116 ? 4.239   -14.435 -4.645  1.00 14.12 ? 116 HIS B CD2 1 
ATOM   4650 C  CE1 . HIS B 1 116 ? 5.761   -15.856 -4.001  1.00 14.02 ? 116 HIS B CE1 1 
ATOM   4651 N  NE2 . HIS B 1 116 ? 5.555   -14.731 -4.717  1.00 14.60 ? 116 HIS B NE2 1 
ATOM   4652 N  N   . ALA B 1 117 ? 1.556   -12.462 -2.774  1.00 14.00 ? 117 ALA B N   1 
ATOM   4653 C  CA  . ALA B 1 117 ? 1.943   -11.038 -2.817  1.00 14.77 ? 117 ALA B CA  1 
ATOM   4654 C  C   . ALA B 1 117 ? 2.025   -10.439 -1.413  1.00 14.86 ? 117 ALA B C   1 
ATOM   4655 O  O   . ALA B 1 117 ? 2.965   -9.642  -1.194  1.00 16.84 ? 117 ALA B O   1 
ATOM   4656 C  CB  . ALA B 1 117 ? 1.026   -10.235 -3.694  1.00 16.17 ? 117 ALA B CB  1 
ATOM   4657 N  N   . MET B 1 118 ? 1.109   -10.770 -0.517  1.00 15.00 ? 118 MET B N   1 
ATOM   4658 C  CA  . MET B 1 118 ? 1.135   -10.237 0.875   1.00 16.02 ? 118 MET B CA  1 
ATOM   4659 C  C   . MET B 1 118 ? 2.360   -10.840 1.585   1.00 13.67 ? 118 MET B C   1 
ATOM   4660 O  O   . MET B 1 118 ? 3.029   -10.135 2.381   1.00 13.63 ? 118 MET B O   1 
ATOM   4661 C  CB  . MET B 1 118 ? -0.172  -10.554 1.614   1.00 20.36 ? 118 MET B CB  1 
ATOM   4662 C  CG  . MET B 1 118 ? -1.346  -9.684  1.134   1.00 23.41 ? 118 MET B CG  1 
ATOM   4663 S  SD  . MET B 1 118 ? -2.897  -10.170 2.010   1.00 29.47 ? 118 MET B SD  1 
ATOM   4664 C  CE  . MET B 1 118 ? -3.193  -11.775 1.270   1.00 21.56 ? 118 MET B CE  1 
ATOM   4665 N  N   . MET B 1 119 ? 2.710   -12.104 1.348   1.00 11.89 ? 119 MET B N   1 
ATOM   4666 C  CA  . MET B 1 119 ? 3.909   -12.705 1.960   1.00 13.11 ? 119 MET B CA  1 
ATOM   4667 C  C   . MET B 1 119 ? 5.148   -11.981 1.454   1.00 11.83 ? 119 MET B C   1 
ATOM   4668 O  O   . MET B 1 119 ? 6.069   -11.705 2.285   1.00 12.39 ? 119 MET B O   1 
ATOM   4669 C  CB  . MET B 1 119 ? 4.025   -14.192 1.644   1.00 12.55 ? 119 MET B CB  1 
ATOM   4670 C  CG  . MET B 1 119 ? 2.900   -15.024 2.293   1.00 13.80 ? 119 MET B CG  1 
ATOM   4671 S  SD  . MET B 1 119 ? 3.299   -16.758 1.981   1.00 17.35 ? 119 MET B SD  1 
ATOM   4672 C  CE  . MET B 1 119 ? 1.916   -17.671 2.687   1.00 16.06 ? 119 MET B CE  1 
ATOM   4673 N  N   . VAL B 1 120 ? 5.210   -11.632 0.165   1.00 12.37 ? 120 VAL B N   1 
ATOM   4674 C  CA  . VAL B 1 120 ? 6.379   -10.902 -0.397  1.00 12.14 ? 120 VAL B CA  1 
ATOM   4675 C  C   . VAL B 1 120 ? 6.466   -9.532  0.270   1.00 12.28 ? 120 VAL B C   1 
ATOM   4676 O  O   . VAL B 1 120 ? 7.572   -9.055  0.499   1.00 13.25 ? 120 VAL B O   1 
ATOM   4677 C  CB  . VAL B 1 120 ? 6.247   -10.792 -1.919  1.00 14.13 ? 120 VAL B CB  1 
ATOM   4678 C  CG1 . VAL B 1 120 ? 7.245   -9.789  -2.479  1.00 14.32 ? 120 VAL B CG1 1 
ATOM   4679 C  CG2 . VAL B 1 120 ? 6.380   -12.161 -2.567  1.00 13.77 ? 120 VAL B CG2 1 
ATOM   4680 N  N   . ASP B 1 121 ? 5.360   -8.860  0.546   1.00 12.65 ? 121 ASP B N   1 
ATOM   4681 C  CA  . ASP B 1 121 ? 5.365   -7.540  1.199   1.00 13.32 ? 121 ASP B CA  1 
ATOM   4682 C  C   . ASP B 1 121 ? 6.147   -7.603  2.509   1.00 13.26 ? 121 ASP B C   1 
ATOM   4683 O  O   . ASP B 1 121 ? 7.052   -6.798  2.767   1.00 14.37 ? 121 ASP B O   1 
ATOM   4684 C  CB  . ASP B 1 121 ? 3.922   -7.080  1.423   1.00 14.98 ? 121 ASP B CB  1 
ATOM   4685 C  CG  . ASP B 1 121 ? 3.778   -5.711  2.071   1.00 16.70 ? 121 ASP B CG  1 
ATOM   4686 O  OD1 . ASP B 1 121 ? 4.268   -5.546  3.221   1.00 16.46 ? 121 ASP B OD1 1 
ATOM   4687 O  OD2 . ASP B 1 121 ? 3.064   -4.851  1.452   1.00 16.39 ? 121 ASP B OD2 1 
ATOM   4688 N  N   . ILE B 1 122 ? 5.865   -8.606  3.315   1.00 10.63 ? 122 ILE B N   1 
ATOM   4689 C  CA  . ILE B 1 122 ? 6.553   -8.718  4.628   1.00 11.63 ? 122 ILE B CA  1 
ATOM   4690 C  C   . ILE B 1 122 ? 7.980   -9.184  4.402   1.00 11.57 ? 122 ILE B C   1 
ATOM   4691 O  O   . ILE B 1 122 ? 8.863   -8.686  5.138   1.00 11.87 ? 122 ILE B O   1 
ATOM   4692 C  CB  . ILE B 1 122 ? 5.753   -9.616  5.590   1.00 11.17 ? 122 ILE B CB  1 
ATOM   4693 C  CG1 . ILE B 1 122 ? 4.279   -9.205  5.709   1.00 11.90 ? 122 ILE B CG1 1 
ATOM   4694 C  CG2 . ILE B 1 122 ? 6.395   -9.632  6.972   1.00 11.65 ? 122 ILE B CG2 1 
ATOM   4695 C  CD1 . ILE B 1 122 ? 4.051   -7.749  5.978   1.00 13.67 ? 122 ILE B CD1 1 
ATOM   4696 N  N   . ALA B 1 123 ? 8.226   -10.128 3.527   1.00 11.33 ? 123 ALA B N   1 
ATOM   4697 C  CA  . ALA B 1 123 ? 9.570   -10.649 3.280   1.00 11.53 ? 123 ALA B CA  1 
ATOM   4698 C  C   . ALA B 1 123 ? 10.491  -9.524  2.798   1.00 12.34 ? 123 ALA B C   1 
ATOM   4699 O  O   . ALA B 1 123 ? 11.660  -9.444  3.241   1.00 13.12 ? 123 ALA B O   1 
ATOM   4700 C  CB  . ALA B 1 123 ? 9.527   -11.821 2.326   1.00 12.12 ? 123 ALA B CB  1 
ATOM   4701 N  N   . VAL B 1 124 ? 9.980   -8.648  1.952   1.00 13.04 ? 124 VAL B N   1 
ATOM   4702 C  CA  . VAL B 1 124 ? 10.783  -7.479  1.481   1.00 12.71 ? 124 VAL B CA  1 
ATOM   4703 C  C   . VAL B 1 124 ? 11.061  -6.564  2.666   1.00 13.18 ? 124 VAL B C   1 
ATOM   4704 O  O   . VAL B 1 124 ? 12.211  -6.027  2.748   1.00 12.62 ? 124 VAL B O   1 
ATOM   4705 C  CB  . VAL B 1 124 ? 10.075  -6.767  0.332   1.00 12.78 ? 124 VAL B CB  1 
ATOM   4706 C  CG1 . VAL B 1 124 ? 10.654  -5.390  0.064   1.00 14.33 ? 124 VAL B CG1 1 
ATOM   4707 C  CG2 . VAL B 1 124 ? 10.115  -7.636  -0.896  1.00 13.62 ? 124 VAL B CG2 1 
ATOM   4708 N  N   . GLN B 1 125 ? 10.126  -6.397  3.580   1.00 11.58 ? 125 GLN B N   1 
ATOM   4709 C  CA  . GLN B 1 125 ? 10.419  -5.592  4.791   1.00 11.63 ? 125 GLN B CA  1 
ATOM   4710 C  C   . GLN B 1 125 ? 11.579  -6.214  5.576   1.00 12.89 ? 125 GLN B C   1 
ATOM   4711 O  O   . GLN B 1 125 ? 12.449  -5.453  6.094   1.00 12.34 ? 125 GLN B O   1 
ATOM   4712 C  CB  . GLN B 1 125 ? 9.192   -5.417  5.670   1.00 12.99 ? 125 GLN B CB  1 
ATOM   4713 C  CG  . GLN B 1 125 ? 8.082   -4.584  5.057   1.00 12.59 ? 125 GLN B CG  1 
ATOM   4714 C  CD  . GLN B 1 125 ? 7.029   -4.253  6.084   1.00 13.62 ? 125 GLN B CD  1 
ATOM   4715 O  OE1 . GLN B 1 125 ? 7.303   -3.782  7.194   1.00 14.29 ? 125 GLN B OE1 1 
ATOM   4716 N  NE2 . GLN B 1 125 ? 5.762   -4.442  5.735   1.00 13.76 ? 125 GLN B NE2 1 
ATOM   4717 N  N   A LEU B 1 126 ? 11.641  -7.551  5.700   0.50 11.50 ? 126 LEU B N   1 
ATOM   4718 N  N   B LEU B 1 126 ? 11.630  -7.549  5.689   0.50 12.36 ? 126 LEU B N   1 
ATOM   4719 C  CA  A LEU B 1 126 ? 12.797  -8.157  6.419   0.50 10.95 ? 126 LEU B CA  1 
ATOM   4720 C  CA  B LEU B 1 126 ? 12.747  -8.187  6.435   0.50 12.41 ? 126 LEU B CA  1 
ATOM   4721 C  C   A LEU B 1 126 ? 14.083  -7.864  5.653   0.50 11.52 ? 126 LEU B C   1 
ATOM   4722 C  C   B LEU B 1 126 ? 14.063  -7.948  5.680   0.50 12.39 ? 126 LEU B C   1 
ATOM   4723 O  O   A LEU B 1 126 ? 15.090  -7.439  6.267   0.50 12.13 ? 126 LEU B O   1 
ATOM   4724 O  O   B LEU B 1 126 ? 15.063  -7.571  6.334   0.50 13.16 ? 126 LEU B O   1 
ATOM   4725 C  CB  A LEU B 1 126 ? 12.603  -9.669  6.531   0.50 10.79 ? 126 LEU B CB  1 
ATOM   4726 C  CB  B LEU B 1 126 ? 12.410  -9.673  6.614   0.50 12.98 ? 126 LEU B CB  1 
ATOM   4727 C  CG  A LEU B 1 126 ? 13.806  -10.424 7.101   0.50 10.20 ? 126 LEU B CG  1 
ATOM   4728 C  CG  B LEU B 1 126 ? 13.433  -10.517 7.380   0.50 14.24 ? 126 LEU B CG  1 
ATOM   4729 C  CD1 A LEU B 1 126 ? 13.857  -10.282 8.621   0.50 10.53 ? 126 LEU B CD1 1 
ATOM   4730 C  CD1 B LEU B 1 126 ? 14.624  -10.907 6.524   0.50 13.19 ? 126 LEU B CD1 1 
ATOM   4731 C  CD2 A LEU B 1 126 ? 13.691  -11.901 6.778   0.50 11.22 ? 126 LEU B CD2 1 
ATOM   4732 C  CD2 B LEU B 1 126 ? 13.862  -9.827  8.652   0.50 15.53 ? 126 LEU B CD2 1 
ATOM   4733 N  N   . VAL B 1 127 ? 14.085  -8.150  4.363   1.00 11.49 ? 127 VAL B N   1 
ATOM   4734 C  CA  . VAL B 1 127 ? 15.312  -7.968  3.545   1.00 12.52 ? 127 VAL B CA  1 
ATOM   4735 C  C   . VAL B 1 127 ? 15.787  -6.521  3.671   1.00 12.12 ? 127 VAL B C   1 
ATOM   4736 O  O   . VAL B 1 127 ? 17.005  -6.276  3.860   1.00 12.05 ? 127 VAL B O   1 
ATOM   4737 C  CB  . VAL B 1 127 ? 15.107  -8.390  2.091   1.00 12.30 ? 127 VAL B CB  1 
ATOM   4738 C  CG1 . VAL B 1 127 ? 16.309  -8.036  1.223   1.00 14.13 ? 127 VAL B CG1 1 
ATOM   4739 C  CG2 . VAL B 1 127 ? 14.845  -9.898  2.033   1.00 14.81 ? 127 VAL B CG2 1 
ATOM   4740 N  N   . GLN B 1 128 ? 14.878  -5.564  3.569   1.00 12.66 ? 128 GLN B N   1 
ATOM   4741 C  CA  . GLN B 1 128 ? 15.271  -4.129  3.636   1.00 14.18 ? 128 GLN B CA  1 
ATOM   4742 C  C   . GLN B 1 128 ? 15.810  -3.823  5.027   1.00 13.02 ? 128 GLN B C   1 
ATOM   4743 O  O   . GLN B 1 128 ? 16.824  -3.073  5.121   1.00 13.51 ? 128 GLN B O   1 
ATOM   4744 C  CB  . GLN B 1 128 ? 14.091  -3.235  3.272   1.00 14.95 ? 128 GLN B CB  1 
ATOM   4745 C  CG  . GLN B 1 128 ? 13.750  -3.287  1.795   1.00 17.14 ? 128 GLN B CG  1 
ATOM   4746 C  CD  . GLN B 1 128 ? 12.568  -2.422  1.476   1.00 24.88 ? 128 GLN B CD  1 
ATOM   4747 O  OE1 . GLN B 1 128 ? 11.562  -2.416  2.201   1.00 30.62 ? 128 GLN B OE1 1 
ATOM   4748 N  NE2 . GLN B 1 128 ? 12.708  -1.676  0.401   1.00 30.93 ? 128 GLN B NE2 1 
ATOM   4749 N  N   . LYS B 1 129 ? 15.232  -4.346  6.104   1.00 11.49 ? 129 LYS B N   1 
ATOM   4750 C  CA  . LYS B 1 129 ? 15.782  -4.130  7.440   1.00 11.96 ? 129 LYS B CA  1 
ATOM   4751 C  C   . LYS B 1 129 ? 17.232  -4.599  7.499   1.00 11.79 ? 129 LYS B C   1 
ATOM   4752 O  O   . LYS B 1 129 ? 18.083  -3.830  7.958   1.00 12.91 ? 129 LYS B O   1 
ATOM   4753 C  CB  . LYS B 1 129 ? 15.012  -4.903  8.508   1.00 12.49 ? 129 LYS B CB  1 
ATOM   4754 C  CG  . LYS B 1 129 ? 15.574  -4.745  9.894   1.00 13.36 ? 129 LYS B CG  1 
ATOM   4755 C  CD  . LYS B 1 129 ? 14.798  -5.356  11.058  1.00 14.89 ? 129 LYS B CD  1 
ATOM   4756 C  CE  . LYS B 1 129 ? 15.545  -5.130  12.366  1.00 17.91 ? 129 LYS B CE  1 
ATOM   4757 N  NZ  . LYS B 1 129 ? 14.756  -5.584  13.527  1.00 20.54 ? 129 LYS B NZ  1 
ATOM   4758 N  N   . TRP B 1 130 ? 17.524  -5.792  7.001   1.00 11.08 ? 130 TRP B N   1 
ATOM   4759 C  CA  . TRP B 1 130 ? 18.908  -6.314  7.111   1.00 10.98 ? 130 TRP B CA  1 
ATOM   4760 C  C   . TRP B 1 130 ? 19.837  -5.547  6.163   1.00 11.96 ? 130 TRP B C   1 
ATOM   4761 O  O   . TRP B 1 130 ? 21.031  -5.369  6.508   1.00 13.22 ? 130 TRP B O   1 
ATOM   4762 C  CB  . TRP B 1 130 ? 18.858  -7.832  6.842   1.00 11.65 ? 130 TRP B CB  1 
ATOM   4763 C  CG  . TRP B 1 130 ? 18.227  -8.594  7.952   1.00 10.99 ? 130 TRP B CG  1 
ATOM   4764 C  CD1 . TRP B 1 130 ? 17.637  -8.128  9.081   1.00 11.90 ? 130 TRP B CD1 1 
ATOM   4765 C  CD2 . TRP B 1 130 ? 18.043  -10.018 7.968   1.00 12.40 ? 130 TRP B CD2 1 
ATOM   4766 N  NE1 . TRP B 1 130 ? 17.145  -9.162  9.832   1.00 11.63 ? 130 TRP B NE1 1 
ATOM   4767 C  CE2 . TRP B 1 130 ? 17.415  -10.331 9.176   1.00 12.23 ? 130 TRP B CE2 1 
ATOM   4768 C  CE3 . TRP B 1 130 ? 18.451  -11.019 7.093   1.00 12.99 ? 130 TRP B CE3 1 
ATOM   4769 C  CZ2 . TRP B 1 130 ? 17.088  -11.654 9.521   1.00 12.36 ? 130 TRP B CZ2 1 
ATOM   4770 C  CZ3 . TRP B 1 130 ? 18.161  -12.327 7.440   1.00 13.13 ? 130 TRP B CZ3 1 
ATOM   4771 C  CH2 . TRP B 1 130 ? 17.465  -12.618 8.619   1.00 13.89 ? 130 TRP B CH2 1 
ATOM   4772 N  N   . GLU B 1 131 ? 19.360  -5.128  5.008   1.00 12.17 ? 131 GLU B N   1 
ATOM   4773 C  CA  . GLU B 1 131 ? 20.190  -4.311  4.090   1.00 12.47 ? 131 GLU B CA  1 
ATOM   4774 C  C   . GLU B 1 131 ? 20.567  -2.994  4.771   1.00 13.38 ? 131 GLU B C   1 
ATOM   4775 O  O   . GLU B 1 131 ? 21.612  -2.434  4.395   1.00 15.79 ? 131 GLU B O   1 
ATOM   4776 C  CB  . GLU B 1 131 ? 19.431  -3.967  2.814   1.00 12.96 ? 131 GLU B CB  1 
ATOM   4777 C  CG  . GLU B 1 131 ? 19.159  -5.152  1.888   1.00 15.43 ? 131 GLU B CG  1 
ATOM   4778 C  CD  . GLU B 1 131 ? 20.335  -5.652  1.080   1.00 17.75 ? 131 GLU B CD  1 
ATOM   4779 O  OE1 . GLU B 1 131 ? 21.486  -5.335  1.415   1.00 19.71 ? 131 GLU B OE1 1 
ATOM   4780 O  OE2 . GLU B 1 131 ? 20.105  -6.364  0.094   1.00 20.55 ? 131 GLU B OE2 1 
ATOM   4781 N  N   . ARG B 1 132 ? 19.766  -2.512  5.692   1.00 12.65 ? 132 ARG B N   1 
ATOM   4782 C  CA  . ARG B 1 132 ? 19.950  -1.183  6.312   1.00 12.08 ? 132 ARG B CA  1 
ATOM   4783 C  C   . ARG B 1 132 ? 20.785  -1.233  7.590   1.00 12.08 ? 132 ARG B C   1 
ATOM   4784 O  O   . ARG B 1 132 ? 21.034  -0.199  8.196   1.00 13.62 ? 132 ARG B O   1 
ATOM   4785 C  CB  . ARG B 1 132 ? 18.580  -0.533  6.489   1.00 12.38 ? 132 ARG B CB  1 
ATOM   4786 C  CG  . ARG B 1 132 ? 17.964  -0.082  5.178   1.00 12.57 ? 132 ARG B CG  1 
ATOM   4787 C  CD  . ARG B 1 132 ? 16.489  0.260   5.313   1.00 12.96 ? 132 ARG B CD  1 
ATOM   4788 N  NE  . ARG B 1 132 ? 15.967  0.716   4.043   1.00 12.97 ? 132 ARG B NE  1 
ATOM   4789 C  CZ  . ARG B 1 132 ? 14.680  0.831   3.756   1.00 13.06 ? 132 ARG B CZ  1 
ATOM   4790 N  NH1 . ARG B 1 132 ? 13.772  0.491   4.654   1.00 13.77 ? 132 ARG B NH1 1 
ATOM   4791 N  NH2 . ARG B 1 132 ? 14.336  1.252   2.566   1.00 16.30 ? 132 ARG B NH2 1 
ATOM   4792 N  N   . LEU B 1 133 ? 21.173  -2.433  8.041   1.00 13.81 ? 133 LEU B N   1 
ATOM   4793 C  CA  . LEU B 1 133 ? 22.051  -2.512  9.212   1.00 14.30 ? 133 LEU B CA  1 
ATOM   4794 C  C   . LEU B 1 133 ? 23.439  -1.962  8.850   1.00 13.20 ? 133 LEU B C   1 
ATOM   4795 O  O   . LEU B 1 133 ? 23.897  -2.060  7.701   1.00 15.62 ? 133 LEU B O   1 
ATOM   4796 C  CB  . LEU B 1 133 ? 22.152  -3.962  9.684   1.00 14.42 ? 133 LEU B CB  1 
ATOM   4797 C  CG  . LEU B 1 133 ? 20.838  -4.566  10.146  1.00 16.04 ? 133 LEU B CG  1 
ATOM   4798 C  CD1 . LEU B 1 133 ? 21.057  -6.008  10.612  1.00 15.89 ? 133 LEU B CD1 1 
ATOM   4799 C  CD2 . LEU B 1 133 ? 20.213  -3.753  11.248  1.00 17.68 ? 133 LEU B CD2 1 
ATOM   4800 N  N   . ASN B 1 134 ? 24.075  -1.393  9.856   1.00 13.95 ? 134 ASN B N   1 
ATOM   4801 C  CA  . ASN B 1 134 ? 25.441  -0.856  9.734   1.00 15.25 ? 134 ASN B CA  1 
ATOM   4802 C  C   . ASN B 1 134 ? 26.455  -1.989  9.962   1.00 18.41 ? 134 ASN B C   1 
ATOM   4803 O  O   . ASN B 1 134 ? 26.090  -3.048  10.467  1.00 17.65 ? 134 ASN B O   1 
ATOM   4804 C  CB  . ASN B 1 134 ? 25.665  0.292   10.721  1.00 14.97 ? 134 ASN B CB  1 
ATOM   4805 C  CG  . ASN B 1 134 ? 24.636  1.394   10.567  1.00 15.07 ? 134 ASN B CG  1 
ATOM   4806 O  OD1 . ASN B 1 134 ? 24.675  2.138   9.578   1.00 15.68 ? 134 ASN B OD1 1 
ATOM   4807 N  ND2 . ASN B 1 134 ? 23.733  1.478   11.537  1.00 17.81 ? 134 ASN B ND2 1 
ATOM   4808 N  N   . ALA B 1 135 ? 27.705  -1.743  9.607   1.00 21.83 ? 135 ALA B N   1 
ATOM   4809 C  CA  . ALA B 1 135 ? 28.744  -2.810  9.569   1.00 23.48 ? 135 ALA B CA  1 
ATOM   4810 C  C   . ALA B 1 135 ? 28.931  -3.481  10.934  1.00 27.48 ? 135 ALA B C   1 
ATOM   4811 O  O   . ALA B 1 135 ? 29.205  -4.726  10.963  1.00 26.95 ? 135 ALA B O   1 
ATOM   4812 C  CB  . ALA B 1 135 ? 30.048  -2.217  9.101   1.00 25.87 ? 135 ALA B CB  1 
ATOM   4813 N  N   . ASP B 1 136 ? 28.839  -2.747  12.035  1.00 25.90 ? 136 ASP B N   1 
ATOM   4814 C  CA  . ASP B 1 136 ? 29.181  -3.338  13.372  1.00 31.68 ? 136 ASP B CA  1 
ATOM   4815 C  C   . ASP B 1 136 ? 27.971  -4.063  14.018  1.00 29.04 ? 136 ASP B C   1 
ATOM   4816 O  O   . ASP B 1 136 ? 28.035  -4.424  15.226  1.00 30.95 ? 136 ASP B O   1 
ATOM   4817 C  CB  . ASP B 1 136 ? 29.740  -2.280  14.340  1.00 37.22 ? 136 ASP B CB  1 
ATOM   4818 C  CG  . ASP B 1 136 ? 28.940  -0.995  14.516  1.00 48.53 ? 136 ASP B CG  1 
ATOM   4819 O  OD1 . ASP B 1 136 ? 28.095  -0.666  13.629  1.00 53.17 ? 136 ASP B OD1 1 
ATOM   4820 O  OD2 . ASP B 1 136 ? 29.204  -0.288  15.521  1.00 57.73 ? 136 ASP B OD2 1 
ATOM   4821 N  N   . GLU B 1 137 ? 26.880  -4.249  13.281  1.00 22.44 ? 137 GLU B N   1 
ATOM   4822 C  CA  . GLU B 1 137 ? 25.604  -4.680  13.882  1.00 19.54 ? 137 GLU B CA  1 
ATOM   4823 C  C   . GLU B 1 137 ? 25.379  -6.156  13.577  1.00 17.29 ? 137 GLU B C   1 
ATOM   4824 O  O   . GLU B 1 137 ? 25.920  -6.707  12.629  1.00 23.58 ? 137 GLU B O   1 
ATOM   4825 C  CB  . GLU B 1 137 ? 24.478  -3.790  13.360  1.00 18.69 ? 137 GLU B CB  1 
ATOM   4826 C  CG  . GLU B 1 137 ? 24.568  -2.414  14.001  1.00 20.27 ? 137 GLU B CG  1 
ATOM   4827 C  CD  . GLU B 1 137 ? 23.730  -1.304  13.422  1.00 24.06 ? 137 GLU B CD  1 
ATOM   4828 O  OE1 . GLU B 1 137 ? 22.891  -1.545  12.530  1.00 19.25 ? 137 GLU B OE1 1 
ATOM   4829 O  OE2 . GLU B 1 137 ? 23.991  -0.141  13.845  1.00 27.03 ? 137 GLU B OE2 1 
ATOM   4830 N  N   . HIS B 1 138 ? 24.488  -6.740  14.348  1.00 16.68 ? 138 HIS B N   1 
ATOM   4831 C  CA  . HIS B 1 138 ? 24.061  -8.124  14.158  1.00 15.15 ? 138 HIS B CA  1 
ATOM   4832 C  C   . HIS B 1 138 ? 22.546  -8.212  14.135  1.00 15.81 ? 138 HIS B C   1 
ATOM   4833 O  O   . HIS B 1 138 ? 21.826  -7.236  14.371  1.00 15.45 ? 138 HIS B O   1 
ATOM   4834 C  CB  . HIS B 1 138 ? 24.700  -8.984  15.241  1.00 17.38 ? 138 HIS B CB  1 
ATOM   4835 C  CG  . HIS B 1 138 ? 24.176  -8.659  16.573  1.00 18.86 ? 138 HIS B CG  1 
ATOM   4836 N  ND1 . HIS B 1 138 ? 24.851  -7.818  17.476  1.00 23.22 ? 138 HIS B ND1 1 
ATOM   4837 C  CD2 . HIS B 1 138 ? 23.088  -9.103  17.232  1.00 21.31 ? 138 HIS B CD2 1 
ATOM   4838 C  CE1 . HIS B 1 138 ? 24.154  -7.744  18.591  1.00 27.37 ? 138 HIS B CE1 1 
ATOM   4839 N  NE2 . HIS B 1 138 ? 23.092  -8.565  18.495  1.00 23.10 ? 138 HIS B NE2 1 
ATOM   4840 N  N   . ILE B 1 139 ? 22.118  -9.412  13.777  1.00 13.61 ? 139 ILE B N   1 
ATOM   4841 C  CA  . ILE B 1 139 ? 20.696  -9.818  13.660  1.00 13.82 ? 139 ILE B CA  1 
ATOM   4842 C  C   . ILE B 1 139 ? 20.321  -10.649 14.878  1.00 13.18 ? 139 ILE B C   1 
ATOM   4843 O  O   . ILE B 1 139 ? 21.013  -11.611 15.166  1.00 13.87 ? 139 ILE B O   1 
ATOM   4844 C  CB  . ILE B 1 139 ? 20.472  -10.529 12.345  1.00 13.36 ? 139 ILE B CB  1 
ATOM   4845 C  CG1 . ILE B 1 139 ? 20.689  -9.593  11.147  1.00 14.49 ? 139 ILE B CG1 1 
ATOM   4846 C  CG2 . ILE B 1 139 ? 19.099  -11.142 12.308  1.00 13.66 ? 139 ILE B CG2 1 
ATOM   4847 C  CD1 . ILE B 1 139 ? 21.001  -10.284 9.852   1.00 16.18 ? 139 ILE B CD1 1 
ATOM   4848 N  N   . GLU B 1 140 ? 19.193  -10.314 15.476  1.00 13.78 ? 140 GLU B N   1 
ATOM   4849 C  CA  . GLU B 1 140 ? 18.569  -11.119 16.539  1.00 13.93 ? 140 GLU B CA  1 
ATOM   4850 C  C   . GLU B 1 140 ? 17.566  -12.055 15.860  1.00 12.26 ? 140 GLU B C   1 
ATOM   4851 O  O   . GLU B 1 140 ? 16.511  -11.571 15.434  1.00 13.03 ? 140 GLU B O   1 
ATOM   4852 C  CB  . GLU B 1 140 ? 17.894  -10.250 17.578  1.00 16.00 ? 140 GLU B CB  1 
ATOM   4853 C  CG  . GLU B 1 140 ? 18.848  -9.258  18.259  1.00 17.64 ? 140 GLU B CG  1 
ATOM   4854 C  CD  . GLU B 1 140 ? 18.203  -8.448  19.352  1.00 23.96 ? 140 GLU B CD  1 
ATOM   4855 O  OE1 . GLU B 1 140 ? 17.025  -8.071  19.214  1.00 25.76 ? 140 GLU B OE1 1 
ATOM   4856 O  OE2 . GLU B 1 140 ? 18.912  -8.184  20.351  1.00 30.20 ? 140 GLU B OE2 1 
ATOM   4857 N  N   . VAL B 1 141 ? 17.949  -13.312 15.628  1.00 12.54 ? 141 VAL B N   1 
ATOM   4858 C  CA  . VAL B 1 141 ? 17.259  -14.135 14.613  1.00 12.22 ? 141 VAL B CA  1 
ATOM   4859 C  C   . VAL B 1 141 ? 15.834  -14.430 15.041  1.00 12.24 ? 141 VAL B C   1 
ATOM   4860 O  O   . VAL B 1 141 ? 14.895  -14.126 14.293  1.00 11.81 ? 141 VAL B O   1 
ATOM   4861 C  CB  . VAL B 1 141 ? 18.086  -15.368 14.260  1.00 12.45 ? 141 VAL B CB  1 
ATOM   4862 C  CG1 . VAL B 1 141 ? 17.268  -16.293 13.358  1.00 12.14 ? 141 VAL B CG1 1 
ATOM   4863 C  CG2 . VAL B 1 141 ? 19.378  -14.963 13.584  1.00 12.25 ? 141 VAL B CG2 1 
ATOM   4864 N  N   . PRO B 1 142 ? 15.574  -15.126 16.145  1.00 12.11 ? 142 PRO B N   1 
ATOM   4865 C  CA  . PRO B 1 142 ? 14.174  -15.438 16.439  1.00 11.80 ? 142 PRO B CA  1 
ATOM   4866 C  C   . PRO B 1 142 ? 13.306  -14.197 16.574  1.00 12.80 ? 142 PRO B C   1 
ATOM   4867 O  O   . PRO B 1 142 ? 12.135  -14.205 16.214  1.00 11.76 ? 142 PRO B O   1 
ATOM   4868 C  CB  . PRO B 1 142 ? 14.217  -16.284 17.692  1.00 13.45 ? 142 PRO B CB  1 
ATOM   4869 C  CG  . PRO B 1 142 ? 15.564  -16.043 18.285  1.00 14.90 ? 142 PRO B CG  1 
ATOM   4870 C  CD  . PRO B 1 142 ? 16.509  -15.700 17.134  1.00 13.15 ? 142 PRO B CD  1 
ATOM   4871 N  N   . GLU B 1 143 ? 13.874  -13.099 17.061  1.00 12.13 ? 143 GLU B N   1 
ATOM   4872 C  CA  . GLU B 1 143 ? 13.124  -11.829 17.202  1.00 11.98 ? 143 GLU B CA  1 
ATOM   4873 C  C   . GLU B 1 143 ? 12.682  -11.360 15.818  1.00 11.46 ? 143 GLU B C   1 
ATOM   4874 O  O   . GLU B 1 143 ? 11.463  -11.098 15.631  1.00 12.11 ? 143 GLU B O   1 
ATOM   4875 C  CB  . GLU B 1 143 ? 14.011  -10.775 17.873  1.00 13.61 ? 143 GLU B CB  1 
ATOM   4876 C  CG  . GLU B 1 143 ? 14.322  -11.080 19.333  1.00 14.78 ? 143 GLU B CG  1 
ATOM   4877 C  CD  . GLU B 1 143 ? 15.380  -12.104 19.698  1.00 15.93 ? 143 GLU B CD  1 
ATOM   4878 O  OE1 . GLU B 1 143 ? 16.019  -12.705 18.836  1.00 16.06 ? 143 GLU B OE1 1 
ATOM   4879 O  OE2 . GLU B 1 143 ? 15.530  -12.347 20.936  1.00 20.76 ? 143 GLU B OE2 1 
ATOM   4880 N  N   . ASP B 1 144 ? 13.564  -11.358 14.825  1.00 10.97 ? 144 ASP B N   1 
ATOM   4881 C  CA  . ASP B 1 144 ? 13.168  -10.858 13.471  1.00 11.64 ? 144 ASP B CA  1 
ATOM   4882 C  C   . ASP B 1 144 ? 12.261  -11.878 12.779  1.00 13.27 ? 144 ASP B C   1 
ATOM   4883 O  O   . ASP B 1 144 ? 11.351  -11.473 12.017  1.00 13.00 ? 144 ASP B O   1 
ATOM   4884 C  CB  . ASP B 1 144 ? 14.376  -10.470 12.624  1.00 11.89 ? 144 ASP B CB  1 
ATOM   4885 C  CG  . ASP B 1 144 ? 14.866  -9.053  12.872  1.00 13.96 ? 144 ASP B CG  1 
ATOM   4886 O  OD1 . ASP B 1 144 ? 14.088  -8.275  13.506  1.00 13.63 ? 144 ASP B OD1 1 
ATOM   4887 O  OD2 . ASP B 1 144 ? 16.034  -8.783  12.432  1.00 13.99 ? 144 ASP B OD2 1 
ATOM   4888 N  N   . MET B 1 145 ? 12.514  -13.180 12.951  1.00 11.85 ? 145 MET B N   1 
ATOM   4889 C  CA  . MET B 1 145 ? 11.635  -14.182 12.329  1.00 11.22 ? 145 MET B CA  1 
ATOM   4890 C  C   . MET B 1 145 ? 10.229  -14.092 12.932  1.00 11.27 ? 145 MET B C   1 
ATOM   4891 O  O   . MET B 1 145 ? 9.271   -14.272 12.170  1.00 11.63 ? 145 MET B O   1 
ATOM   4892 C  CB  . MET B 1 145 ? 12.206  -15.581 12.489  1.00 10.99 ? 145 MET B CB  1 
ATOM   4893 C  CG  . MET B 1 145 ? 13.540  -15.830 11.795  1.00 12.06 ? 145 MET B CG  1 
ATOM   4894 S  SD  . MET B 1 145 ? 13.537  -15.443 10.048  1.00 14.07 ? 145 MET B SD  1 
ATOM   4895 C  CE  . MET B 1 145 ? 14.249  -13.803 10.049  1.00 16.98 ? 145 MET B CE  1 
ATOM   4896 N  N   . THR B 1 146 ? 10.064  -13.755 14.199  1.00 11.68 ? 146 THR B N   1 
ATOM   4897 C  CA  . THR B 1 146 ? 8.732   -13.663 14.829  1.00 12.25 ? 146 THR B CA  1 
ATOM   4898 C  C   . THR B 1 146 ? 8.066   -12.385 14.317  1.00 14.21 ? 146 THR B C   1 
ATOM   4899 O  O   . THR B 1 146 ? 6.837   -12.408 14.034  1.00 13.79 ? 146 THR B O   1 
ATOM   4900 C  CB  . THR B 1 146 ? 8.870   -13.714 16.360  1.00 13.65 ? 146 THR B CB  1 
ATOM   4901 O  OG1 . THR B 1 146 ? 9.536   -14.934 16.684  1.00 12.92 ? 146 THR B OG1 1 
ATOM   4902 C  CG2 . THR B 1 146 ? 7.500   -13.577 16.971  1.00 13.50 ? 146 THR B CG2 1 
ATOM   4903 N  N   . ARG B 1 147 ? 8.845   -11.315 14.090  1.00 11.68 ? 147 ARG B N   1 
ATOM   4904 C  CA  . ARG B 1 147 ? 8.284   -10.078 13.494  1.00 12.64 ? 147 ARG B CA  1 
ATOM   4905 C  C   . ARG B 1 147 ? 7.685   -10.440 12.149  1.00 12.80 ? 147 ARG B C   1 
ATOM   4906 O  O   . ARG B 1 147 ? 6.512   -10.056 11.859  1.00 13.34 ? 147 ARG B O   1 
ATOM   4907 C  CB  . ARG B 1 147 ? 9.351   -8.972  13.328  1.00 12.36 ? 147 ARG B CB  1 
ATOM   4908 C  CG  . ARG B 1 147 ? 9.773   -8.350  14.644  1.00 15.11 ? 147 ARG B CG  1 
ATOM   4909 C  CD  . ARG B 1 147 ? 10.787  -7.264  14.246  1.00 18.15 ? 147 ARG B CD  1 
ATOM   4910 N  NE  . ARG B 1 147 ? 11.115  -6.454  15.407  1.00 20.81 ? 147 ARG B NE  1 
ATOM   4911 C  CZ  . ARG B 1 147 ? 12.187  -6.599  16.172  1.00 21.60 ? 147 ARG B CZ  1 
ATOM   4912 N  NH1 . ARG B 1 147 ? 13.102  -7.513  15.902  1.00 19.43 ? 147 ARG B NH1 1 
ATOM   4913 N  NH2 . ARG B 1 147 ? 12.369  -5.775  17.193  1.00 27.37 ? 147 ARG B NH2 1 
ATOM   4914 N  N   . LEU B 1 148 ? 8.432   -11.208 11.360  1.00 11.32 ? 148 LEU B N   1 
ATOM   4915 C  CA  . LEU B 1 148 ? 7.984   -11.559 10.005  1.00 11.88 ? 148 LEU B CA  1 
ATOM   4916 C  C   . LEU B 1 148 ? 6.720   -12.425 10.076  1.00 12.57 ? 148 LEU B C   1 
ATOM   4917 O  O   . LEU B 1 148 ? 5.761   -12.177 9.304   1.00 11.87 ? 148 LEU B O   1 
ATOM   4918 C  CB  . LEU B 1 148 ? 9.089   -12.290 9.246   1.00 14.09 ? 148 LEU B CB  1 
ATOM   4919 C  CG  . LEU B 1 148 ? 8.640   -12.707 7.842   1.00 16.23 ? 148 LEU B CG  1 
ATOM   4920 C  CD1 . LEU B 1 148 ? 9.572   -12.210 6.788   1.00 20.81 ? 148 LEU B CD1 1 
ATOM   4921 C  CD2 . LEU B 1 148 ? 8.456   -14.198 7.759   1.00 21.52 ? 148 LEU B CD2 1 
ATOM   4922 N  N   . THR B 1 149 ? 6.746   -13.507 10.850  1.00 10.99 ? 149 THR B N   1 
ATOM   4923 C  CA  . THR B 1 149 ? 5.667   -14.528 10.725  1.00 11.06 ? 149 THR B CA  1 
ATOM   4924 C  C   . THR B 1 149 ? 4.385   -14.003 11.363  1.00 13.04 ? 149 THR B C   1 
ATOM   4925 O  O   . THR B 1 149 ? 3.279   -14.232 10.812  1.00 14.03 ? 149 THR B O   1 
ATOM   4926 C  CB  . THR B 1 149 ? 6.092   -15.883 11.270  1.00 12.61 ? 149 THR B CB  1 
ATOM   4927 O  OG1 . THR B 1 149 ? 6.396   -15.772 12.645  1.00 13.73 ? 149 THR B OG1 1 
ATOM   4928 C  CG2 . THR B 1 149 ? 7.265   -16.446 10.518  1.00 11.99 ? 149 THR B CG2 1 
ATOM   4929 N  N   . LEU B 1 150 ? 4.471   -13.229 12.420  1.00 12.16 ? 150 LEU B N   1 
ATOM   4930 C  CA  . LEU B 1 150 ? 3.281   -12.524 12.949  1.00 13.44 ? 150 LEU B CA  1 
ATOM   4931 C  C   . LEU B 1 150 ? 2.714   -11.626 11.865  1.00 12.89 ? 150 LEU B C   1 
ATOM   4932 O  O   . LEU B 1 150 ? 1.454   -11.602 11.625  1.00 12.98 ? 150 LEU B O   1 
ATOM   4933 C  CB  . LEU B 1 150 ? 3.634   -11.714 14.206  1.00 14.44 ? 150 LEU B CB  1 
ATOM   4934 C  CG  . LEU B 1 150 ? 2.500   -10.800 14.681  1.00 16.93 ? 150 LEU B CG  1 
ATOM   4935 C  CD1 . LEU B 1 150 ? 1.298   -11.651 15.078  1.00 17.04 ? 150 LEU B CD1 1 
ATOM   4936 C  CD2 . LEU B 1 150 ? 2.948   -9.875  15.804  1.00 16.58 ? 150 LEU B CD2 1 
ATOM   4937 N  N   . ASP B 1 151 ? 3.549   -10.800 11.237  1.00 12.53 ? 151 ASP B N   1 
ATOM   4938 C  CA  . ASP B 1 151 ? 3.018   -9.804  10.302  1.00 12.82 ? 151 ASP B CA  1 
ATOM   4939 C  C   . ASP B 1 151 ? 2.424   -10.525 9.103   1.00 11.86 ? 151 ASP B C   1 
ATOM   4940 O  O   . ASP B 1 151 ? 1.377   -10.058 8.626   1.00 11.90 ? 151 ASP B O   1 
ATOM   4941 C  CB  . ASP B 1 151 ? 4.075   -8.766  9.936   1.00 13.96 ? 151 ASP B CB  1 
ATOM   4942 C  CG  . ASP B 1 151 ? 4.213   -7.740  11.050  1.00 15.58 ? 151 ASP B CG  1 
ATOM   4943 O  OD1 . ASP B 1 151 ? 3.935   -8.060  12.235  1.00 20.17 ? 151 ASP B OD1 1 
ATOM   4944 O  OD2 . ASP B 1 151 ? 4.682   -6.702  10.717  1.00 25.03 ? 151 ASP B OD2 1 
ATOM   4945 N  N   . THR B 1 152 ? 2.991   -11.647 8.669   1.00 10.81 ? 152 THR B N   1 
ATOM   4946 C  CA  . THR B 1 152 ? 2.453   -12.363 7.495   1.00 10.91 ? 152 THR B CA  1 
ATOM   4947 C  C   . THR B 1 152 ? 1.038   -12.835 7.814   1.00 11.86 ? 152 THR B C   1 
ATOM   4948 O  O   . THR B 1 152 ? 0.177   -12.701 6.945   1.00 11.43 ? 152 THR B O   1 
ATOM   4949 C  CB  . THR B 1 152 ? 3.408   -13.475 7.052   1.00 12.26 ? 152 THR B CB  1 
ATOM   4950 O  OG1 . THR B 1 152 ? 4.683   -12.888 6.739   1.00 12.81 ? 152 THR B OG1 1 
ATOM   4951 C  CG2 . THR B 1 152 ? 2.861   -14.239 5.864   1.00 12.87 ? 152 THR B CG2 1 
ATOM   4952 N  N   . ILE B 1 153 ? 0.843   -13.488 8.917   1.00 12.06 ? 153 ILE B N   1 
ATOM   4953 C  CA  . ILE B 1 153 ? -0.506  -14.042 9.217   1.00 13.29 ? 153 ILE B CA  1 
ATOM   4954 C  C   . ILE B 1 153 ? -1.454  -12.894 9.504   1.00 14.17 ? 153 ILE B C   1 
ATOM   4955 O  O   . ILE B 1 153 ? -2.667  -12.982 9.087   1.00 16.09 ? 153 ILE B O   1 
ATOM   4956 C  CB  . ILE B 1 153 ? -0.500  -15.113 10.317  1.00 13.67 ? 153 ILE B CB  1 
ATOM   4957 C  CG1 . ILE B 1 153 ? -1.830  -15.883 10.349  1.00 14.16 ? 153 ILE B CG1 1 
ATOM   4958 C  CG2 . ILE B 1 153 ? -0.155  -14.534 11.653  1.00 16.31 ? 153 ILE B CG2 1 
ATOM   4959 C  CD1 . ILE B 1 153 ? -2.229  -16.524 9.051   1.00 14.74 ? 153 ILE B CD1 1 
ATOM   4960 N  N   . GLY B 1 154 ? -1.015  -11.788 10.091  1.00 13.39 ? 154 GLY B N   1 
ATOM   4961 C  CA  . GLY B 1 154 ? -1.960  -10.671 10.229  1.00 13.49 ? 154 GLY B CA  1 
ATOM   4962 C  C   . GLY B 1 154 ? -2.444  -10.138 8.916   1.00 13.15 ? 154 GLY B C   1 
ATOM   4963 O  O   . GLY B 1 154 ? -3.643  -9.879  8.783   1.00 13.20 ? 154 GLY B O   1 
ATOM   4964 N  N   . LEU B 1 155 ? -1.543  -10.034 7.906   1.00 13.06 ? 155 LEU B N   1 
ATOM   4965 C  CA  . LEU B 1 155 ? -1.956  -9.413  6.632   1.00 14.67 ? 155 LEU B CA  1 
ATOM   4966 C  C   . LEU B 1 155 ? -2.759  -10.415 5.820   1.00 18.85 ? 155 LEU B C   1 
ATOM   4967 O  O   . LEU B 1 155 ? -3.856  -10.066 5.360   1.00 19.45 ? 155 LEU B O   1 
ATOM   4968 C  CB  . LEU B 1 155 ? -0.647  -8.915  6.000   1.00 16.11 ? 155 LEU B CB  1 
ATOM   4969 C  CG  . LEU B 1 155 ? -0.745  -8.089  4.737   1.00 17.44 ? 155 LEU B CG  1 
ATOM   4970 C  CD1 . LEU B 1 155 ? -1.584  -6.844  4.969   1.00 16.77 ? 155 LEU B CD1 1 
ATOM   4971 C  CD2 . LEU B 1 155 ? 0.644   -7.733  4.245   1.00 16.10 ? 155 LEU B CD2 1 
ATOM   4972 N  N   . CYS B 1 156 ? -2.311  -11.680 5.746   1.00 18.12 ? 156 CYS B N   1 
ATOM   4973 C  CA  . CYS B 1 156 ? -3.085  -12.752 5.039   1.00 18.79 ? 156 CYS B CA  1 
ATOM   4974 C  C   . CYS B 1 156 ? -4.309  -13.203 5.820   1.00 20.36 ? 156 CYS B C   1 
ATOM   4975 O  O   . CYS B 1 156 ? -5.309  -13.661 5.177   1.00 26.49 ? 156 CYS B O   1 
ATOM   4976 C  CB  . CYS B 1 156 ? -2.182  -13.961 4.780   1.00 21.34 ? 156 CYS B CB  1 
ATOM   4977 S  SG  . CYS B 1 156 ? -0.724  -13.642 3.773   1.00 22.25 ? 156 CYS B SG  1 
ATOM   4978 N  N   . GLY B 1 157 ? -4.337  -13.132 7.123   1.00 20.32 ? 157 GLY B N   1 
ATOM   4979 C  CA  . GLY B 1 157 ? -5.489  -13.565 7.932   1.00 21.10 ? 157 GLY B CA  1 
ATOM   4980 C  C   . GLY B 1 157 ? -6.603  -12.555 7.856   1.00 22.67 ? 157 GLY B C   1 
ATOM   4981 O  O   . GLY B 1 157 ? -7.809  -12.951 7.767   1.00 22.77 ? 157 GLY B O   1 
ATOM   4982 N  N   . PHE B 1 158 ? -6.298  -11.265 7.989   1.00 20.05 ? 158 PHE B N   1 
ATOM   4983 C  CA  . PHE B 1 158 ? -7.408  -10.301 8.169   1.00 19.72 ? 158 PHE B CA  1 
ATOM   4984 C  C   . PHE B 1 158 ? -7.017  -8.895  7.717   1.00 17.84 ? 158 PHE B C   1 
ATOM   4985 O  O   . PHE B 1 158 ? -7.649  -7.940  8.185   1.00 16.54 ? 158 PHE B O   1 
ATOM   4986 C  CB  . PHE B 1 158 ? -8.030  -10.353 9.573   1.00 24.66 ? 158 PHE B CB  1 
ATOM   4987 C  CG  . PHE B 1 158 ? -7.043  -10.354 10.702  1.00 28.23 ? 158 PHE B CG  1 
ATOM   4988 C  CD1 . PHE B 1 158 ? -6.290  -11.488 10.973  1.00 31.63 ? 158 PHE B CD1 1 
ATOM   4989 C  CD2 . PHE B 1 158 ? -6.918  -9.259  11.538  1.00 35.19 ? 158 PHE B CD2 1 
ATOM   4990 C  CE1 . PHE B 1 158 ? -5.414  -11.504 12.045  1.00 34.77 ? 158 PHE B CE1 1 
ATOM   4991 C  CE2 . PHE B 1 158 ? -6.037  -9.285  12.618  1.00 33.97 ? 158 PHE B CE2 1 
ATOM   4992 C  CZ  . PHE B 1 158 ? -5.271  -10.393 12.846  1.00 32.14 ? 158 PHE B CZ  1 
ATOM   4993 N  N   . ASN B 1 159 ? -6.016  -8.770  6.871   1.00 17.04 ? 159 ASN B N   1 
ATOM   4994 C  CA  . ASN B 1 159 ? -5.625  -7.492  6.244   1.00 17.43 ? 159 ASN B CA  1 
ATOM   4995 C  C   . ASN B 1 159 ? -5.299  -6.486  7.356   1.00 15.99 ? 159 ASN B C   1 
ATOM   4996 O  O   . ASN B 1 159 ? -5.693  -5.332  7.270   1.00 19.29 ? 159 ASN B O   1 
ATOM   4997 C  CB  . ASN B 1 159 ? -6.726  -6.983  5.308   1.00 20.70 ? 159 ASN B CB  1 
ATOM   4998 C  CG  . ASN B 1 159 ? -6.209  -6.000  4.286   1.00 30.73 ? 159 ASN B CG  1 
ATOM   4999 O  OD1 . ASN B 1 159 ? -5.058  -6.076  3.886   1.00 34.63 ? 159 ASN B OD1 1 
ATOM   5000 N  ND2 . ASN B 1 159 ? -7.025  -5.029  3.907   1.00 34.84 ? 159 ASN B ND2 1 
ATOM   5001 N  N   . TYR B 1 160 ? -4.613  -6.944  8.397   1.00 15.20 ? 160 TYR B N   1 
ATOM   5002 C  CA  . TYR B 1 160 ? -4.231  -6.128  9.568   1.00 14.83 ? 160 TYR B CA  1 
ATOM   5003 C  C   . TYR B 1 160 ? -2.712  -6.094  9.596   1.00 14.26 ? 160 TYR B C   1 
ATOM   5004 O  O   . TYR B 1 160 ? -2.061  -7.149  9.505   1.00 15.23 ? 160 TYR B O   1 
ATOM   5005 C  CB  . TYR B 1 160 ? -4.801  -6.662  10.872  1.00 15.73 ? 160 TYR B CB  1 
ATOM   5006 C  CG  . TYR B 1 160 ? -4.529  -5.790  12.060  1.00 17.26 ? 160 TYR B CG  1 
ATOM   5007 C  CD1 . TYR B 1 160 ? -5.288  -4.656  12.303  1.00 18.64 ? 160 TYR B CD1 1 
ATOM   5008 C  CD2 . TYR B 1 160 ? -3.440  -6.023  12.887  1.00 18.18 ? 160 TYR B CD2 1 
ATOM   5009 C  CE1 . TYR B 1 160 ? -5.037  -3.825  13.375  1.00 18.01 ? 160 TYR B CE1 1 
ATOM   5010 C  CE2 . TYR B 1 160 ? -3.161  -5.177  13.937  1.00 17.79 ? 160 TYR B CE2 1 
ATOM   5011 C  CZ  . TYR B 1 160 ? -3.948  -4.065  14.178  1.00 19.91 ? 160 TYR B CZ  1 
ATOM   5012 O  OH  . TYR B 1 160 ? -3.639  -3.221  15.208  1.00 22.06 ? 160 TYR B OH  1 
ATOM   5013 N  N   . ARG B 1 161 ? -2.166  -4.883  9.732   1.00 13.02 ? 161 ARG B N   1 
ATOM   5014 C  CA  . ARG B 1 161 ? -0.693  -4.732  9.805   1.00 13.04 ? 161 ARG B CA  1 
ATOM   5015 C  C   . ARG B 1 161 ? -0.266  -4.596  11.253  1.00 13.16 ? 161 ARG B C   1 
ATOM   5016 O  O   . ARG B 1 161 ? -0.533  -3.567  11.942  1.00 13.47 ? 161 ARG B O   1 
ATOM   5017 C  CB  . ARG B 1 161 ? -0.218  -3.592  8.900   1.00 13.35 ? 161 ARG B CB  1 
ATOM   5018 C  CG  . ARG B 1 161 ? -0.286  -3.958  7.439   1.00 15.04 ? 161 ARG B CG  1 
ATOM   5019 C  CD  . ARG B 1 161 ? 0.149   -2.901  6.489   1.00 15.69 ? 161 ARG B CD  1 
ATOM   5020 N  NE  . ARG B 1 161 ? 0.026   -3.289  5.102   1.00 14.77 ? 161 ARG B NE  1 
ATOM   5021 C  CZ  . ARG B 1 161 ? 0.968   -3.838  4.368   1.00 13.46 ? 161 ARG B CZ  1 
ATOM   5022 N  NH1 . ARG B 1 161 ? 2.156   -4.140  4.870   1.00 13.94 ? 161 ARG B NH1 1 
ATOM   5023 N  NH2 . ARG B 1 161 ? 0.708   -4.116  3.111   1.00 15.81 ? 161 ARG B NH2 1 
ATOM   5024 N  N   . PHE B 1 162 ? 0.410   -5.602  11.774  1.00 13.09 ? 162 PHE B N   1 
ATOM   5025 C  CA  . PHE B 1 162 ? 1.038   -5.466  13.107  1.00 13.50 ? 162 PHE B CA  1 
ATOM   5026 C  C   . PHE B 1 162 ? 2.245   -4.495  13.040  1.00 12.31 ? 162 PHE B C   1 
ATOM   5027 O  O   . PHE B 1 162 ? 2.587   -3.955  14.127  1.00 13.63 ? 162 PHE B O   1 
ATOM   5028 C  CB  . PHE B 1 162 ? 1.415   -6.838  13.677  1.00 13.25 ? 162 PHE B CB  1 
ATOM   5029 C  CG  . PHE B 1 162 ? 0.216   -7.576  14.181  1.00 14.16 ? 162 PHE B CG  1 
ATOM   5030 C  CD1 . PHE B 1 162 ? -0.290  -7.323  15.427  1.00 14.60 ? 162 PHE B CD1 1 
ATOM   5031 C  CD2 . PHE B 1 162 ? -0.378  -8.550  13.404  1.00 14.07 ? 162 PHE B CD2 1 
ATOM   5032 C  CE1 . PHE B 1 162 ? -1.429  -7.985  15.880  1.00 16.03 ? 162 PHE B CE1 1 
ATOM   5033 C  CE2 . PHE B 1 162 ? -1.497  -9.206  13.860  1.00 14.62 ? 162 PHE B CE2 1 
ATOM   5034 C  CZ  . PHE B 1 162 ? -2.021  -8.930  15.087  1.00 15.23 ? 162 PHE B CZ  1 
ATOM   5035 N  N   . ASN B 1 163 ? 2.816   -4.277  11.876  1.00 12.54 ? 163 ASN B N   1 
ATOM   5036 C  CA  . ASN B 1 163 ? 3.930   -3.309  11.729  1.00 12.84 ? 163 ASN B CA  1 
ATOM   5037 C  C   . ASN B 1 163 ? 5.040   -3.674  12.713  1.00 13.86 ? 163 ASN B C   1 
ATOM   5038 O  O   . ASN B 1 163 ? 5.649   -2.796  13.369  1.00 12.53 ? 163 ASN B O   1 
ATOM   5039 C  CB  . ASN B 1 163 ? 3.366   -1.905  11.853  1.00 13.33 ? 163 ASN B CB  1 
ATOM   5040 C  CG  . ASN B 1 163 ? 2.646   -1.573  10.570  1.00 13.14 ? 163 ASN B CG  1 
ATOM   5041 O  OD1 . ASN B 1 163 ? 3.111   -1.843  9.450   1.00 14.27 ? 163 ASN B OD1 1 
ATOM   5042 N  ND2 . ASN B 1 163 ? 1.483   -0.924  10.743  1.00 14.33 ? 163 ASN B ND2 1 
ATOM   5043 N  N   . SER B 1 164 ? 5.369   -4.959  12.792  1.00 12.33 ? 164 SER B N   1 
ATOM   5044 C  CA  . SER B 1 164 ? 6.353   -5.446  13.780  1.00 14.06 ? 164 SER B CA  1 
ATOM   5045 C  C   . SER B 1 164 ? 7.739   -4.884  13.470  1.00 13.18 ? 164 SER B C   1 
ATOM   5046 O  O   . SER B 1 164 ? 8.528   -4.793  14.428  1.00 13.91 ? 164 SER B O   1 
ATOM   5047 C  CB  . SER B 1 164 ? 6.383   -6.941  13.840  1.00 15.05 ? 164 SER B CB  1 
ATOM   5048 O  OG  . SER B 1 164 ? 5.140   -7.429  14.261  1.00 16.86 ? 164 SER B OG  1 
ATOM   5049 N  N   . PHE B 1 165 ? 8.048   -4.569  12.217  1.00 13.42 ? 165 PHE B N   1 
ATOM   5050 C  CA  . PHE B 1 165 ? 9.414   -4.048  11.906  1.00 13.62 ? 165 PHE B CA  1 
ATOM   5051 C  C   . PHE B 1 165 ? 9.496   -2.565  12.270  1.00 16.15 ? 165 PHE B C   1 
ATOM   5052 O  O   . PHE B 1 165 ? 10.610  -2.015  12.138  1.00 18.59 ? 165 PHE B O   1 
ATOM   5053 C  CB  . PHE B 1 165 ? 9.763   -4.324  10.437  1.00 13.74 ? 165 PHE B CB  1 
ATOM   5054 C  CG  . PHE B 1 165 ? 10.016  -5.782  10.165  1.00 13.76 ? 165 PHE B CG  1 
ATOM   5055 C  CD1 . PHE B 1 165 ? 11.097  -6.431  10.754  1.00 16.19 ? 165 PHE B CD1 1 
ATOM   5056 C  CD2 . PHE B 1 165 ? 9.168   -6.512  9.381   1.00 14.56 ? 165 PHE B CD2 1 
ATOM   5057 C  CE1 . PHE B 1 165 ? 11.337  -7.774  10.532  1.00 15.95 ? 165 PHE B CE1 1 
ATOM   5058 C  CE2 . PHE B 1 165 ? 9.399   -7.863  9.200   1.00 16.19 ? 165 PHE B CE2 1 
ATOM   5059 C  CZ  . PHE B 1 165 ? 10.483  -8.484  9.751   1.00 16.11 ? 165 PHE B CZ  1 
ATOM   5060 N  N   . TYR B 1 166 ? 8.423   -1.922  12.698  1.00 13.64 ? 166 TYR B N   1 
ATOM   5061 C  CA  . TYR B 1 166 ? 8.404   -0.504  13.158  1.00 15.61 ? 166 TYR B CA  1 
ATOM   5062 C  C   . TYR B 1 166 ? 8.486   -0.393  14.676  1.00 17.89 ? 166 TYR B C   1 
ATOM   5063 O  O   . TYR B 1 166 ? 8.362   0.767   15.169  1.00 19.58 ? 166 TYR B O   1 
ATOM   5064 C  CB  . TYR B 1 166 ? 7.185   0.186   12.580  1.00 14.41 ? 166 TYR B CB  1 
ATOM   5065 C  CG  . TYR B 1 166 ? 7.194   0.310   11.104  1.00 13.72 ? 166 TYR B CG  1 
ATOM   5066 C  CD1 . TYR B 1 166 ? 6.666   -0.669  10.285  1.00 14.50 ? 166 TYR B CD1 1 
ATOM   5067 C  CD2 . TYR B 1 166 ? 7.713   1.423   10.477  1.00 13.80 ? 166 TYR B CD2 1 
ATOM   5068 C  CE1 . TYR B 1 166 ? 6.681   -0.562  8.908   1.00 14.12 ? 166 TYR B CE1 1 
ATOM   5069 C  CE2 . TYR B 1 166 ? 7.773   1.526   9.113   1.00 12.84 ? 166 TYR B CE2 1 
ATOM   5070 C  CZ  . TYR B 1 166 ? 7.237   0.549   8.308   1.00 13.19 ? 166 TYR B CZ  1 
ATOM   5071 O  OH  . TYR B 1 166 ? 7.281   0.682   6.970   1.00 13.57 ? 166 TYR B OH  1 
ATOM   5072 N  N   . ARG B 1 167 ? 8.627   -1.525  15.383  1.00 18.10 ? 167 ARG B N   1 
ATOM   5073 C  CA  . ARG B 1 167 ? 8.512   -1.604  16.856  1.00 22.15 ? 167 ARG B CA  1 
ATOM   5074 C  C   . ARG B 1 167 ? 9.649   -2.394  17.482  1.00 22.96 ? 167 ARG B C   1 
ATOM   5075 O  O   . ARG B 1 167 ? 10.104  -3.384  16.881  1.00 21.61 ? 167 ARG B O   1 
ATOM   5076 C  CB  . ARG B 1 167 ? 7.290   -2.423  17.276  1.00 24.75 ? 167 ARG B CB  1 
ATOM   5077 C  CG  . ARG B 1 167 ? 5.990   -1.845  16.757  1.00 24.69 ? 167 ARG B CG  1 
ATOM   5078 C  CD  . ARG B 1 167 ? 4.878   -2.833  17.052  1.00 26.15 ? 167 ARG B CD  1 
ATOM   5079 N  NE  . ARG B 1 167 ? 3.616   -2.519  16.404  1.00 25.97 ? 167 ARG B NE  1 
ATOM   5080 C  CZ  . ARG B 1 167 ? 2.704   -1.713  16.919  1.00 30.53 ? 167 ARG B CZ  1 
ATOM   5081 N  NH1 . ARG B 1 167 ? 2.928   -1.156  18.097  1.00 30.97 ? 167 ARG B NH1 1 
ATOM   5082 N  NH2 . ARG B 1 167 ? 1.566   -1.475  16.278  1.00 32.50 ? 167 ARG B NH2 1 
ATOM   5083 N  N   . ASP B 1 168 ? 10.052  -1.948  18.683  1.00 28.63 ? 168 ASP B N   1 
ATOM   5084 C  CA  . ASP B 1 168 ? 10.816  -2.762  19.665  1.00 35.47 ? 168 ASP B CA  1 
ATOM   5085 C  C   . ASP B 1 168 ? 9.831   -3.449  20.614  1.00 40.85 ? 168 ASP B C   1 
ATOM   5086 O  O   . ASP B 1 168 ? 10.038  -4.619  20.922  1.00 55.38 ? 168 ASP B O   1 
ATOM   5087 C  CB  . ASP B 1 168 ? 11.733  -1.895  20.514  1.00 38.99 ? 168 ASP B CB  1 
ATOM   5088 C  CG  . ASP B 1 168 ? 12.762  -1.116  19.726  1.00 39.97 ? 168 ASP B CG  1 
ATOM   5089 O  OD1 . ASP B 1 168 ? 13.609  -1.757  19.114  1.00 50.71 ? 168 ASP B OD1 1 
ATOM   5090 O  OD2 . ASP B 1 168 ? 12.718  0.127   19.773  1.00 43.31 ? 168 ASP B OD2 1 
ATOM   5091 N  N   . GLN B 1 169 ? 8.800   -2.725  21.042  1.00 40.73 ? 169 GLN B N   1 
ATOM   5092 C  CA  . GLN B 1 169 ? 7.824   -3.139  22.082  1.00 46.26 ? 169 GLN B CA  1 
ATOM   5093 C  C   . GLN B 1 169 ? 6.678   -3.885  21.413  1.00 45.14 ? 169 GLN B C   1 
ATOM   5094 O  O   . GLN B 1 169 ? 6.213   -3.449  20.356  1.00 37.49 ? 169 GLN B O   1 
ATOM   5095 C  CB  . GLN B 1 169 ? 7.329   -1.899  22.823  1.00 56.03 ? 169 GLN B CB  1 
ATOM   5096 C  CG  . GLN B 1 169 ? 8.380   -1.345  23.771  1.00 63.92 ? 169 GLN B CG  1 
ATOM   5097 C  CD  . GLN B 1 169 ? 8.536   -2.234  24.982  1.00 68.41 ? 169 GLN B CD  1 
ATOM   5098 O  OE1 . GLN B 1 169 ? 7.581   -2.469  25.721  1.00 77.85 ? 169 GLN B OE1 1 
ATOM   5099 N  NE2 . GLN B 1 169 ? 9.738   -2.751  25.191  1.00 69.40 ? 169 GLN B NE2 1 
ATOM   5100 N  N   . PRO B 1 170 ? 6.177   -5.011  21.979  1.00 38.91 ? 170 PRO B N   1 
ATOM   5101 C  CA  . PRO B 1 170 ? 5.187   -5.804  21.273  1.00 38.89 ? 170 PRO B CA  1 
ATOM   5102 C  C   . PRO B 1 170 ? 3.946   -4.932  21.122  1.00 32.32 ? 170 PRO B C   1 
ATOM   5103 O  O   . PRO B 1 170 ? 3.712   -4.048  21.905  1.00 30.39 ? 170 PRO B O   1 
ATOM   5104 C  CB  . PRO B 1 170 ? 4.926   -7.056  22.137  1.00 41.63 ? 170 PRO B CB  1 
ATOM   5105 C  CG  . PRO B 1 170 ? 6.009   -7.015  23.205  1.00 43.52 ? 170 PRO B CG  1 
ATOM   5106 C  CD  . PRO B 1 170 ? 6.470   -5.570  23.307  1.00 42.85 ? 170 PRO B CD  1 
ATOM   5107 N  N   . HIS B 1 171 ? 3.185   -5.199  20.075  1.00 32.74 ? 171 HIS B N   1 
ATOM   5108 C  CA  . HIS B 1 171 ? 1.790   -4.734  19.929  1.00 28.21 ? 171 HIS B CA  1 
ATOM   5109 C  C   . HIS B 1 171 ? 1.034   -5.151  21.191  1.00 30.47 ? 171 HIS B C   1 
ATOM   5110 O  O   . HIS B 1 171 ? 1.234   -6.264  21.679  1.00 27.50 ? 171 HIS B O   1 
ATOM   5111 C  CB  . HIS B 1 171 ? 1.260   -5.292  18.606  1.00 27.40 ? 171 HIS B CB  1 
ATOM   5112 C  CG  . HIS B 1 171 ? -0.100  -4.810  18.271  1.00 27.98 ? 171 HIS B CG  1 
ATOM   5113 N  ND1 . HIS B 1 171 ? -1.208  -5.152  19.001  1.00 27.62 ? 171 HIS B ND1 1 
ATOM   5114 C  CD2 . HIS B 1 171 ? -0.545  -4.041  17.254  1.00 24.20 ? 171 HIS B CD2 1 
ATOM   5115 C  CE1 . HIS B 1 171 ? -2.280  -4.608  18.483  1.00 31.48 ? 171 HIS B CE1 1 
ATOM   5116 N  NE2 . HIS B 1 171 ? -1.891  -3.895  17.401  1.00 29.18 ? 171 HIS B NE2 1 
ATOM   5117 N  N   . PRO B 1 172 ? 0.203   -4.293  21.829  1.00 30.07 ? 172 PRO B N   1 
ATOM   5118 C  CA  . PRO B 1 172 ? -0.499  -4.670  23.055  1.00 30.58 ? 172 PRO B CA  1 
ATOM   5119 C  C   . PRO B 1 172 ? -1.302  -5.973  22.949  1.00 30.01 ? 172 PRO B C   1 
ATOM   5120 O  O   . PRO B 1 172 ? -1.426  -6.663  23.937  1.00 31.32 ? 172 PRO B O   1 
ATOM   5121 C  CB  . PRO B 1 172 ? -1.458  -3.494  23.348  1.00 33.32 ? 172 PRO B CB  1 
ATOM   5122 C  CG  . PRO B 1 172 ? -1.484  -2.691  22.064  1.00 33.04 ? 172 PRO B CG  1 
ATOM   5123 C  CD  . PRO B 1 172 ? -0.133  -2.919  21.420  1.00 32.73 ? 172 PRO B CD  1 
ATOM   5124 N  N   . PHE B 1 173 ? -1.849  -6.304  21.781  1.00 27.67 ? 173 PHE B N   1 
ATOM   5125 C  CA  . PHE B 1 173 ? -2.553  -7.594  21.592  1.00 23.34 ? 173 PHE B CA  1 
ATOM   5126 C  C   . PHE B 1 173 ? -1.591  -8.774  21.821  1.00 20.36 ? 173 PHE B C   1 
ATOM   5127 O  O   . PHE B 1 173 ? -1.969  -9.806  22.470  1.00 18.61 ? 173 PHE B O   1 
ATOM   5128 C  CB  . PHE B 1 173 ? -3.166  -7.694  20.190  1.00 22.98 ? 173 PHE B CB  1 
ATOM   5129 C  CG  . PHE B 1 173 ? -3.720  -9.052  19.893  1.00 23.64 ? 173 PHE B CG  1 
ATOM   5130 C  CD1 . PHE B 1 173 ? -2.875  -10.063 19.452  1.00 24.62 ? 173 PHE B CD1 1 
ATOM   5131 C  CD2 . PHE B 1 173 ? -5.065  -9.331  20.034  1.00 24.81 ? 173 PHE B CD2 1 
ATOM   5132 C  CE1 . PHE B 1 173 ? -3.367  -11.334 19.218  1.00 23.85 ? 173 PHE B CE1 1 
ATOM   5133 C  CE2 . PHE B 1 173 ? -5.558  -10.597 19.789  1.00 25.02 ? 173 PHE B CE2 1 
ATOM   5134 C  CZ  . PHE B 1 173 ? -4.713  -11.603 19.370  1.00 26.47 ? 173 PHE B CZ  1 
ATOM   5135 N  N   . ILE B 1 174 ? -0.371  -8.610  21.338  1.00 20.35 ? 174 ILE B N   1 
ATOM   5136 C  CA  . ILE B 1 174 ? 0.677   -9.662  21.409  1.00 20.03 ? 174 ILE B CA  1 
ATOM   5137 C  C   . ILE B 1 174 ? 1.172   -9.768  22.847  1.00 21.18 ? 174 ILE B C   1 
ATOM   5138 O  O   . ILE B 1 174 ? 1.396   -10.867 23.317  1.00 19.76 ? 174 ILE B O   1 
ATOM   5139 C  CB  . ILE B 1 174 ? 1.769   -9.409  20.367  1.00 19.85 ? 174 ILE B CB  1 
ATOM   5140 C  CG1 . ILE B 1 174 ? 1.177   -9.512  18.954  1.00 21.68 ? 174 ILE B CG1 1 
ATOM   5141 C  CG2 . ILE B 1 174 ? 2.968   -10.329 20.533  1.00 21.25 ? 174 ILE B CG2 1 
ATOM   5142 C  CD1 . ILE B 1 174 ? 0.651   -10.885 18.605  1.00 23.06 ? 174 ILE B CD1 1 
ATOM   5143 N  N   . THR B 1 175 ? 1.336   -8.654  23.559  1.00 20.70 ? 175 THR B N   1 
ATOM   5144 C  CA  . THR B 1 175 ? 1.686   -8.712  25.000  1.00 21.63 ? 175 THR B CA  1 
ATOM   5145 C  C   . THR B 1 175 ? 0.662   -9.560  25.743  1.00 18.05 ? 175 THR B C   1 
ATOM   5146 O  O   . THR B 1 175 ? 1.053   -10.429 26.563  1.00 20.90 ? 175 THR B O   1 
ATOM   5147 C  CB  . THR B 1 175 ? 1.723   -7.296  25.583  1.00 21.46 ? 175 THR B CB  1 
ATOM   5148 O  OG1 . THR B 1 175 ? 2.833   -6.656  24.950  1.00 24.52 ? 175 THR B OG1 1 
ATOM   5149 C  CG2 . THR B 1 175 ? 1.904   -7.324  27.090  1.00 23.62 ? 175 THR B CG2 1 
ATOM   5150 N  N   . SER B 1 176 ? -0.608  -9.339  25.489  1.00 17.88 ? 176 SER B N   1 
ATOM   5151 C  CA  . SER B 1 176 ? -1.708  -10.118 26.117  1.00 18.58 ? 176 SER B CA  1 
ATOM   5152 C  C   . SER B 1 176 ? -1.683  -11.586 25.668  1.00 18.07 ? 176 SER B C   1 
ATOM   5153 O  O   . SER B 1 176 ? -1.853  -12.484 26.514  1.00 18.87 ? 176 SER B O   1 
ATOM   5154 C  CB  . SER B 1 176 ? -3.051  -9.480  25.921  1.00 21.27 ? 176 SER B CB  1 
ATOM   5155 O  OG  . SER B 1 176 ? -3.200  -8.413  26.874  1.00 24.40 ? 176 SER B OG  1 
ATOM   5156 N  N   . MET B 1 177 ? -1.488  -11.843 24.387  1.00 18.70 ? 177 MET B N   1 
ATOM   5157 C  CA  . MET B 1 177 ? -1.480  -13.250 23.883  1.00 17.06 ? 177 MET B CA  1 
ATOM   5158 C  C   . MET B 1 177 ? -0.307  -14.040 24.475  1.00 17.12 ? 177 MET B C   1 
ATOM   5159 O  O   . MET B 1 177 ? -0.492  -15.202 24.967  1.00 16.29 ? 177 MET B O   1 
ATOM   5160 C  CB  . MET B 1 177 ? -1.360  -13.225 22.361  1.00 17.40 ? 177 MET B CB  1 
ATOM   5161 C  CG  . MET B 1 177 ? -1.537  -14.592 21.760  1.00 18.44 ? 177 MET B CG  1 
ATOM   5162 S  SD  . MET B 1 177 ? -1.174  -14.623 19.973  1.00 21.46 ? 177 MET B SD  1 
ATOM   5163 C  CE  . MET B 1 177 ? 0.606   -14.510 20.020  1.00 23.65 ? 177 MET B CE  1 
ATOM   5164 N  N   . VAL B 1 178 ? 0.870   -13.433 24.494  1.00 15.51 ? 178 VAL B N   1 
ATOM   5165 C  CA  . VAL B 1 178 ? 2.082   -14.122 25.013  1.00 16.60 ? 178 VAL B CA  1 
ATOM   5166 C  C   . VAL B 1 178 ? 1.877   -14.422 26.505  1.00 17.32 ? 178 VAL B C   1 
ATOM   5167 O  O   . VAL B 1 178 ? 2.226   -15.531 26.949  1.00 17.77 ? 178 VAL B O   1 
ATOM   5168 C  CB  . VAL B 1 178 ? 3.347   -13.290 24.718  1.00 17.73 ? 178 VAL B CB  1 
ATOM   5169 C  CG1 . VAL B 1 178 ? 4.571   -13.811 25.452  1.00 19.30 ? 178 VAL B CG1 1 
ATOM   5170 C  CG2 . VAL B 1 178 ? 3.654   -13.294 23.223  1.00 18.99 ? 178 VAL B CG2 1 
ATOM   5171 N  N   . ARG B 1 179 ? 1.369   -13.471 27.262  1.00 18.43 ? 179 ARG B N   1 
ATOM   5172 C  CA  . ARG B 1 179 ? 1.190   -13.643 28.731  1.00 18.85 ? 179 ARG B CA  1 
ATOM   5173 C  C   . ARG B 1 179 ? 0.057   -14.656 29.000  1.00 19.21 ? 179 ARG B C   1 
ATOM   5174 O  O   . ARG B 1 179 ? 0.162   -15.420 29.986  1.00 20.53 ? 179 ARG B O   1 
ATOM   5175 C  CB  . ARG B 1 179 ? 0.856   -12.296 29.387  1.00 20.64 ? 179 ARG B CB  1 
ATOM   5176 C  CG  . ARG B 1 179 ? 1.008   -12.296 30.908  1.00 22.45 ? 179 ARG B CG  1 
ATOM   5177 C  CD  . ARG B 1 179 ? 1.098   -10.877 31.421  1.00 22.39 ? 179 ARG B CD  1 
ATOM   5178 N  NE  . ARG B 1 179 ? 0.046   -10.021 30.920  1.00 23.73 ? 179 ARG B NE  1 
ATOM   5179 C  CZ  . ARG B 1 179 ? 0.144   -8.700  30.708  1.00 25.97 ? 179 ARG B CZ  1 
ATOM   5180 N  NH1 . ARG B 1 179 ? 1.249   -8.042  31.025  1.00 27.02 ? 179 ARG B NH1 1 
ATOM   5181 N  NH2 . ARG B 1 179 ? -0.890  -8.032  30.237  1.00 27.08 ? 179 ARG B NH2 1 
ATOM   5182 N  N   . ALA B 1 180 ? -0.969  -14.721 28.166  1.00 16.62 ? 180 ALA B N   1 
ATOM   5183 C  CA  . ALA B 1 180 ? -2.044  -15.724 28.302  1.00 19.86 ? 180 ALA B CA  1 
ATOM   5184 C  C   . ALA B 1 180 ? -1.469  -17.118 28.003  1.00 19.40 ? 180 ALA B C   1 
ATOM   5185 O  O   . ALA B 1 180 ? -1.804  -18.083 28.754  1.00 19.95 ? 180 ALA B O   1 
ATOM   5186 C  CB  . ALA B 1 180 ? -3.221  -15.372 27.438  1.00 19.84 ? 180 ALA B CB  1 
ATOM   5187 N  N   . LEU B 1 181 ? -0.676  -17.270 26.942  1.00 17.37 ? 181 LEU B N   1 
ATOM   5188 C  CA  . LEU B 1 181 ? 0.009   -18.556 26.621  1.00 19.05 ? 181 LEU B CA  1 
ATOM   5189 C  C   . LEU B 1 181 ? 0.876   -18.961 27.818  1.00 20.96 ? 181 LEU B C   1 
ATOM   5190 O  O   . LEU B 1 181 ? 0.810   -20.129 28.233  1.00 21.26 ? 181 LEU B O   1 
ATOM   5191 C  CB  . LEU B 1 181 ? 0.822   -18.476 25.326  1.00 18.51 ? 181 LEU B CB  1 
ATOM   5192 C  CG  . LEU B 1 181 ? 0.001   -18.458 24.032  1.00 19.53 ? 181 LEU B CG  1 
ATOM   5193 C  CD1 . LEU B 1 181 ? 0.824   -17.929 22.899  1.00 18.81 ? 181 LEU B CD1 1 
ATOM   5194 C  CD2 . LEU B 1 181 ? -0.527  -19.839 23.735  1.00 20.40 ? 181 LEU B CD2 1 
ATOM   5195 N  N   A ASP B 1 182 ? 1.654   -18.035 28.381  0.50 23.43 ? 182 ASP B N   1 
ATOM   5196 N  N   B ASP B 1 182 ? 1.643   -18.026 28.383  0.50 22.38 ? 182 ASP B N   1 
ATOM   5197 C  CA  A ASP B 1 182 ? 2.568   -18.355 29.514  0.50 23.94 ? 182 ASP B CA  1 
ATOM   5198 C  CA  B ASP B 1 182 ? 2.591   -18.353 29.486  0.50 22.37 ? 182 ASP B CA  1 
ATOM   5199 C  C   A ASP B 1 182 ? 1.774   -18.918 30.690  0.50 24.83 ? 182 ASP B C   1 
ATOM   5200 C  C   B ASP B 1 182 ? 1.802   -18.888 30.691  0.50 23.98 ? 182 ASP B C   1 
ATOM   5201 O  O   A ASP B 1 182 ? 2.190   -19.950 31.260  0.50 25.53 ? 182 ASP B O   1 
ATOM   5202 O  O   B ASP B 1 182 ? 2.238   -19.906 31.268  0.50 25.20 ? 182 ASP B O   1 
ATOM   5203 C  CB  A ASP B 1 182 ? 3.356   -17.120 29.931  0.50 26.07 ? 182 ASP B CB  1 
ATOM   5204 C  CB  B ASP B 1 182 ? 3.495   -17.155 29.791  0.50 22.73 ? 182 ASP B CB  1 
ATOM   5205 C  CG  A ASP B 1 182 ? 4.465   -16.815 28.953  0.50 28.52 ? 182 ASP B CG  1 
ATOM   5206 C  CG  B ASP B 1 182 ? 4.527   -17.451 30.864  0.50 24.37 ? 182 ASP B CG  1 
ATOM   5207 O  OD1 A ASP B 1 182 ? 4.923   -17.768 28.265  0.50 34.29 ? 182 ASP B OD1 1 
ATOM   5208 O  OD1 B ASP B 1 182 ? 5.428   -18.278 30.595  0.50 26.37 ? 182 ASP B OD1 1 
ATOM   5209 O  OD2 A ASP B 1 182 ? 4.866   -15.633 28.879  0.50 31.73 ? 182 ASP B OD2 1 
ATOM   5210 O  OD2 B ASP B 1 182 ? 4.389   -16.898 31.961  0.50 25.27 ? 182 ASP B OD2 1 
ATOM   5211 N  N   . GLU B 1 183 ? 0.678   -18.263 31.045  1.00 22.15 ? 183 GLU B N   1 
ATOM   5212 C  CA  . GLU B 1 183 ? -0.206  -18.718 32.143  1.00 25.16 ? 183 GLU B CA  1 
ATOM   5213 C  C   . GLU B 1 183 ? -0.736  -20.120 31.818  1.00 27.08 ? 183 GLU B C   1 
ATOM   5214 O  O   . GLU B 1 183 ? -0.570  -21.008 32.624  1.00 26.74 ? 183 GLU B O   1 
ATOM   5215 C  CB  . GLU B 1 183 ? -1.304  -17.704 32.417  1.00 26.56 ? 183 GLU B CB  1 
ATOM   5216 C  CG  . GLU B 1 183 ? -2.325  -18.147 33.439  1.00 26.72 ? 183 GLU B CG  1 
ATOM   5217 C  CD  . GLU B 1 183 ? -1.757  -18.370 34.833  1.00 34.41 ? 183 GLU B CD  1 
ATOM   5218 O  OE1 . GLU B 1 183 ? -0.559  -18.102 35.068  1.00 33.85 ? 183 GLU B OE1 1 
ATOM   5219 O  OE2 . GLU B 1 183 ? -2.511  -18.879 35.664  1.00 35.41 ? 183 GLU B OE2 1 
ATOM   5220 N  N   . ALA B 1 184 ? -1.268  -20.360 30.620  1.00 25.84 ? 184 ALA B N   1 
ATOM   5221 C  CA  . ALA B 1 184 ? -1.826  -21.687 30.269  1.00 24.13 ? 184 ALA B CA  1 
ATOM   5222 C  C   . ALA B 1 184 ? -0.782  -22.783 30.464  1.00 27.72 ? 184 ALA B C   1 
ATOM   5223 O  O   . ALA B 1 184 ? -1.125  -23.860 30.999  1.00 28.61 ? 184 ALA B O   1 
ATOM   5224 C  CB  . ALA B 1 184 ? -2.317  -21.609 28.847  1.00 24.89 ? 184 ALA B CB  1 
ATOM   5225 N  N   . MET B 1 185 ? 0.451   -22.505 30.077  1.00 25.85 ? 185 MET B N   1 
ATOM   5226 C  CA  . MET B 1 185 ? 1.599   -23.451 30.095  1.00 32.60 ? 185 MET B CA  1 
ATOM   5227 C  C   . MET B 1 185 ? 2.019   -23.786 31.525  1.00 35.08 ? 185 MET B C   1 
ATOM   5228 O  O   . MET B 1 185 ? 2.649   -24.833 31.693  1.00 36.75 ? 185 MET B O   1 
ATOM   5229 C  CB  . MET B 1 185 ? 2.812   -22.791 29.470  1.00 33.37 ? 185 MET B CB  1 
ATOM   5230 C  CG  . MET B 1 185 ? 3.591   -23.648 28.581  1.00 40.64 ? 185 MET B CG  1 
ATOM   5231 S  SD  . MET B 1 185 ? 3.244   -22.945 26.997  1.00 40.20 ? 185 MET B SD  1 
ATOM   5232 C  CE  . MET B 1 185 ? 2.122   -24.178 26.367  1.00 27.14 ? 185 MET B CE  1 
ATOM   5233 N  N   . ASN B 1 186 ? 1.765   -22.875 32.464  1.00 33.85 ? 186 ASN B N   1 
ATOM   5234 C  CA  . ASN B 1 186 ? 2.237   -22.946 33.876  1.00 35.46 ? 186 ASN B CA  1 
ATOM   5235 C  C   . ASN B 1 186 ? 1.219   -23.646 34.767  1.00 38.39 ? 186 ASN B C   1 
ATOM   5236 O  O   . ASN B 1 186 ? 1.658   -24.287 35.731  1.00 40.71 ? 186 ASN B O   1 
ATOM   5237 C  CB  . ASN B 1 186 ? 2.486   -21.553 34.462  1.00 37.17 ? 186 ASN B CB  1 
ATOM   5238 C  CG  . ASN B 1 186 ? 3.790   -20.952 34.002  1.00 37.11 ? 186 ASN B CG  1 
ATOM   5239 O  OD1 . ASN B 1 186 ? 4.720   -21.662 33.638  1.00 42.98 ? 186 ASN B OD1 1 
ATOM   5240 N  ND2 . ASN B 1 186 ? 3.851   -19.627 33.988  1.00 43.54 ? 186 ASN B ND2 1 
ATOM   5241 N  N   . LYS B 1 187 ? -0.081  -23.493 34.496  1.00 36.44 ? 187 LYS B N   1 
ATOM   5242 C  CA  . LYS B 1 187 ? -1.155  -23.925 35.426  1.00 38.63 ? 187 LYS B CA  1 
ATOM   5243 C  C   . LYS B 1 187 ? -1.063  -25.423 35.722  1.00 42.20 ? 187 LYS B C   1 
ATOM   5244 O  O   . LYS B 1 187 ? -1.402  -25.812 36.836  1.00 48.01 ? 187 LYS B O   1 
ATOM   5245 C  CB  . LYS B 1 187 ? -2.525  -23.544 34.881  1.00 36.02 ? 187 LYS B CB  1 
ATOM   5246 C  CG  . LYS B 1 187 ? -2.714  -22.056 34.699  1.00 39.80 ? 187 LYS B CG  1 
ATOM   5247 C  CD  . LYS B 1 187 ? -3.744  -21.721 33.631  1.00 42.98 ? 187 LYS B CD  1 
ATOM   5248 C  CE  . LYS B 1 187 ? -5.030  -21.163 34.191  1.00 41.74 ? 187 LYS B CE  1 
ATOM   5249 N  NZ  . LYS B 1 187 ? -4.777  -20.355 35.404  1.00 40.96 ? 187 LYS B NZ  1 
ATOM   5250 N  N   . PRO B 1 188 ? -0.662  -26.313 34.781  1.00 41.78 ? 188 PRO B N   1 
ATOM   5251 C  CA  . PRO B 1 188 ? -0.578  -27.740 35.108  1.00 41.84 ? 188 PRO B CA  1 
ATOM   5252 C  C   . PRO B 1 188 ? 0.411   -28.091 36.238  1.00 43.48 ? 188 PRO B C   1 
ATOM   5253 O  O   . PRO B 1 188 ? 0.834   -29.235 36.253  1.00 45.70 ? 188 PRO B O   1 
ATOM   5254 C  CB  . PRO B 1 188 ? -0.138  -28.375 33.787  1.00 40.45 ? 188 PRO B CB  1 
ATOM   5255 C  CG  . PRO B 1 188 ? -0.672  -27.422 32.735  1.00 41.30 ? 188 PRO B CG  1 
ATOM   5256 C  CD  . PRO B 1 188 ? -0.431  -26.058 33.350  1.00 41.29 ? 188 PRO B CD  1 
ATOM   5257 N  N   . GLN B 1 189 ? 0.716   -27.155 37.153  1.00 39.34 ? 189 GLN B N   1 
ATOM   5258 C  CA  . GLN B 1 189 ? 1.614   -27.403 38.325  1.00 31.61 ? 189 GLN B CA  1 
ATOM   5259 C  C   . GLN B 1 189 ? 0.961   -26.967 39.656  1.00 33.41 ? 189 GLN B C   1 
ATOM   5260 O  O   . GLN B 1 189 ? 1.299   -27.570 40.701  1.00 35.54 ? 189 GLN B O   1 
ATOM   5261 C  CB  . GLN B 1 189 ? 2.975   -26.761 38.070  1.00 36.65 ? 189 GLN B CB  1 
ATOM   5262 C  CG  . GLN B 1 189 ? 3.805   -27.446 36.982  1.00 37.06 ? 189 GLN B CG  1 
ATOM   5263 C  CD  . GLN B 1 189 ? 4.470   -28.719 37.455  1.00 45.84 ? 189 GLN B CD  1 
ATOM   5264 O  OE1 . GLN B 1 189 ? 4.469   -29.731 36.757  1.00 44.44 ? 189 GLN B OE1 1 
ATOM   5265 N  NE2 . GLN B 1 189 ? 5.032   -28.701 38.658  1.00 47.06 ? 189 GLN B NE2 1 
ATOM   5266 N  N   . ARG B 1 190 ? 0.030   -26.000 39.634  1.00 35.83 ? 190 ARG B N   1 
ATOM   5267 C  CA  . ARG B 1 190 ? -0.753  -25.567 40.842  1.00 41.73 ? 190 ARG B CA  1 
ATOM   5268 C  C   . ARG B 1 190 ? -1.554  -26.712 41.496  1.00 42.17 ? 190 ARG B C   1 
ATOM   5269 O  O   . ARG B 1 190 ? -2.625  -27.081 40.943  1.00 43.36 ? 190 ARG B O   1 
ATOM   5270 C  CB  . ARG B 1 190 ? -1.738  -24.462 40.449  1.00 40.55 ? 190 ARG B CB  1 
ATOM   5271 C  CG  . ARG B 1 190 ? -1.024  -23.197 39.990  1.00 41.19 ? 190 ARG B CG  1 
ATOM   5272 C  CD  . ARG B 1 190 ? -1.801  -22.267 39.079  1.00 43.41 ? 190 ARG B CD  1 
ATOM   5273 N  NE  . ARG B 1 190 ? -0.788  -21.482 38.363  1.00 42.40 ? 190 ARG B NE  1 
ATOM   5274 C  CZ  . ARG B 1 190 ? -0.993  -20.321 37.796  1.00 39.75 ? 190 ARG B CZ  1 
ATOM   5275 N  NH1 . ARG B 1 190 ? -2.192  -19.759 37.869  1.00 43.06 ? 190 ARG B NH1 1 
ATOM   5276 N  NH2 . ARG B 1 190 ? 0.013   -19.708 37.192  1.00 37.66 ? 190 ARG B NH2 1 
ATOM   5277 N  N   . ALA B 1 191 ? -1.141  -27.174 42.689  1.00 43.40 ? 191 ALA B N   1 
ATOM   5278 C  CA  . ALA B 1 191 ? -1.903  -28.169 43.482  1.00 46.40 ? 191 ALA B CA  1 
ATOM   5279 C  C   . ALA B 1 191 ? -3.281  -27.594 43.887  1.00 42.42 ? 191 ALA B C   1 
ATOM   5280 O  O   . ALA B 1 191 ? -4.266  -28.365 43.917  1.00 41.59 ? 191 ALA B O   1 
ATOM   5281 C  CB  . ALA B 1 191 ? -1.096  -28.601 44.680  1.00 49.42 ? 191 ALA B CB  1 
ATOM   5282 N  N   . ASN B 1 192 ? -3.368  -26.292 44.173  1.00 40.04 ? 192 ASN B N   1 
ATOM   5283 C  CA  . ASN B 1 192 ? -4.587  -25.601 44.702  1.00 38.26 ? 192 ASN B CA  1 
ATOM   5284 C  C   . ASN B 1 192 ? -4.829  -24.310 43.917  1.00 40.56 ? 192 ASN B C   1 
ATOM   5285 O  O   . ASN B 1 192 ? -4.625  -23.190 44.411  1.00 40.34 ? 192 ASN B O   1 
ATOM   5286 C  CB  . ASN B 1 192 ? -4.459  -25.243 46.180  1.00 37.56 ? 192 ASN B CB  1 
ATOM   5287 C  CG  . ASN B 1 192 ? -3.989  -26.407 47.020  1.00 38.16 ? 192 ASN B CG  1 
ATOM   5288 O  OD1 . ASN B 1 192 ? -2.919  -26.350 47.633  1.00 36.34 ? 192 ASN B OD1 1 
ATOM   5289 N  ND2 . ASN B 1 192 ? -4.786  -27.460 47.061  1.00 37.87 ? 192 ASN B ND2 1 
ATOM   5290 N  N   . PRO B 1 193 ? -5.337  -24.428 42.680  1.00 39.44 ? 193 PRO B N   1 
ATOM   5291 C  CA  . PRO B 1 193 ? -5.375  -23.278 41.776  1.00 41.87 ? 193 PRO B CA  1 
ATOM   5292 C  C   . PRO B 1 193 ? -6.428  -22.259 42.232  1.00 44.85 ? 193 PRO B C   1 
ATOM   5293 O  O   . PRO B 1 193 ? -6.466  -21.184 41.657  1.00 44.12 ? 193 PRO B O   1 
ATOM   5294 C  CB  . PRO B 1 193 ? -5.786  -23.888 40.423  1.00 47.06 ? 193 PRO B CB  1 
ATOM   5295 C  CG  . PRO B 1 193 ? -6.547  -25.172 40.792  1.00 45.58 ? 193 PRO B CG  1 
ATOM   5296 C  CD  . PRO B 1 193 ? -5.920  -25.652 42.094  1.00 44.81 ? 193 PRO B CD  1 
ATOM   5297 N  N   . ASP B 1 194 ? -7.254  -22.590 43.231  1.00 42.51 ? 194 ASP B N   1 
ATOM   5298 C  CA  . ASP B 1 194 ? -8.190  -21.597 43.832  1.00 42.28 ? 194 ASP B CA  1 
ATOM   5299 C  C   . ASP B 1 194 ? -7.566  -20.963 45.096  1.00 39.74 ? 194 ASP B C   1 
ATOM   5300 O  O   . ASP B 1 194 ? -8.261  -20.075 45.709  1.00 34.61 ? 194 ASP B O   1 
ATOM   5301 C  CB  . ASP B 1 194 ? -9.577  -22.215 44.054  1.00 48.03 ? 194 ASP B CB  1 
ATOM   5302 C  CG  . ASP B 1 194 ? -10.419 -22.221 42.786  1.00 57.40 ? 194 ASP B CG  1 
ATOM   5303 O  OD1 . ASP B 1 194 ? -10.512 -21.152 42.138  1.00 61.17 ? 194 ASP B OD1 1 
ATOM   5304 O  OD2 . ASP B 1 194 ? -10.947 -23.295 42.437  1.00 58.48 ? 194 ASP B OD2 1 
ATOM   5305 N  N   . ASP B 1 195 ? -6.333  -21.365 45.480  1.00 34.25 ? 195 ASP B N   1 
ATOM   5306 C  CA  . ASP B 1 195 ? -5.465  -20.609 46.444  1.00 41.74 ? 195 ASP B CA  1 
ATOM   5307 C  C   . ASP B 1 195 ? -5.595  -19.112 46.126  1.00 40.90 ? 195 ASP B C   1 
ATOM   5308 O  O   . ASP B 1 195 ? -5.460  -18.720 44.967  1.00 40.49 ? 195 ASP B O   1 
ATOM   5309 C  CB  . ASP B 1 195 ? -4.005  -21.104 46.394  1.00 44.06 ? 195 ASP B CB  1 
ATOM   5310 C  CG  . ASP B 1 195 ? -3.064  -20.544 47.464  1.00 48.42 ? 195 ASP B CG  1 
ATOM   5311 O  OD1 . ASP B 1 195 ? -3.421  -19.538 48.059  1.00 40.89 ? 195 ASP B OD1 1 
ATOM   5312 O  OD2 . ASP B 1 195 ? -1.942  -21.127 47.672  1.00 48.28 ? 195 ASP B OD2 1 
ATOM   5313 N  N   . PRO B 1 196 ? -5.882  -18.207 47.096  1.00 42.17 ? 196 PRO B N   1 
ATOM   5314 C  CA  . PRO B 1 196 ? -5.959  -16.774 46.788  1.00 36.78 ? 196 PRO B CA  1 
ATOM   5315 C  C   . PRO B 1 196 ? -4.628  -16.216 46.241  1.00 36.04 ? 196 PRO B C   1 
ATOM   5316 O  O   . PRO B 1 196 ? -4.694  -15.118 45.675  1.00 34.88 ? 196 PRO B O   1 
ATOM   5317 C  CB  . PRO B 1 196 ? -6.371  -16.080 48.107  1.00 41.87 ? 196 PRO B CB  1 
ATOM   5318 C  CG  . PRO B 1 196 ? -6.732  -17.205 49.083  1.00 39.09 ? 196 PRO B CG  1 
ATOM   5319 C  CD  . PRO B 1 196 ? -6.170  -18.498 48.510  1.00 39.28 ? 196 PRO B CD  1 
ATOM   5320 N  N   . ALA B 1 197 ? -3.526  -16.991 46.320  1.00 33.52 ? 197 ALA B N   1 
ATOM   5321 C  CA  . ALA B 1 197 ? -2.167  -16.676 45.809  1.00 26.80 ? 197 ALA B CA  1 
ATOM   5322 C  C   . ALA B 1 197 ? -2.230  -16.406 44.298  1.00 33.79 ? 197 ALA B C   1 
ATOM   5323 O  O   . ALA B 1 197 ? -1.302  -15.798 43.752  1.00 36.80 ? 197 ALA B O   1 
ATOM   5324 C  CB  . ALA B 1 197 ? -1.211  -17.824 46.080  1.00 27.58 ? 197 ALA B CB  1 
ATOM   5325 N  N   . TYR B 1 198 ? -3.269  -16.894 43.627  1.00 34.02 ? 198 TYR B N   1 
ATOM   5326 C  CA  . TYR B 1 198 ? -3.372  -16.807 42.155  1.00 34.35 ? 198 TYR B CA  1 
ATOM   5327 C  C   . TYR B 1 198 ? -4.493  -15.845 41.779  1.00 34.27 ? 198 TYR B C   1 
ATOM   5328 O  O   . TYR B 1 198 ? -4.773  -15.760 40.562  1.00 38.26 ? 198 TYR B O   1 
ATOM   5329 C  CB  . TYR B 1 198 ? -3.616  -18.189 41.539  1.00 35.35 ? 198 TYR B CB  1 
ATOM   5330 C  CG  . TYR B 1 198 ? -2.624  -19.263 41.916  1.00 34.13 ? 198 TYR B CG  1 
ATOM   5331 C  CD1 . TYR B 1 198 ? -1.310  -19.216 41.486  1.00 34.45 ? 198 TYR B CD1 1 
ATOM   5332 C  CD2 . TYR B 1 198 ? -3.001  -20.339 42.705  1.00 36.12 ? 198 TYR B CD2 1 
ATOM   5333 C  CE1 . TYR B 1 198 ? -0.395  -20.207 41.821  1.00 31.53 ? 198 TYR B CE1 1 
ATOM   5334 C  CE2 . TYR B 1 198 ? -2.101  -21.333 43.056  1.00 36.28 ? 198 TYR B CE2 1 
ATOM   5335 C  CZ  . TYR B 1 198 ? -0.791  -21.265 42.622  1.00 32.96 ? 198 TYR B CZ  1 
ATOM   5336 O  OH  . TYR B 1 198 ? 0.095   -22.257 42.941  1.00 36.58 ? 198 TYR B OH  1 
ATOM   5337 N  N   . ASP B 1 199 ? -5.104  -15.126 42.716  1.00 35.90 ? 199 ASP B N   1 
ATOM   5338 C  CA  . ASP B 1 199 ? -6.165  -14.155 42.326  1.00 43.59 ? 199 ASP B CA  1 
ATOM   5339 C  C   . ASP B 1 199 ? -5.567  -13.212 41.264  1.00 44.89 ? 199 ASP B C   1 
ATOM   5340 O  O   . ASP B 1 199 ? -6.348  -12.775 40.342  1.00 38.96 ? 199 ASP B O   1 
ATOM   5341 C  CB  . ASP B 1 199 ? -6.749  -13.394 43.525  1.00 45.00 ? 199 ASP B CB  1 
ATOM   5342 C  CG  . ASP B 1 199 ? -7.778  -14.178 44.330  1.00 50.74 ? 199 ASP B CG  1 
ATOM   5343 O  OD1 . ASP B 1 199 ? -8.033  -15.358 43.991  1.00 46.37 ? 199 ASP B OD1 1 
ATOM   5344 O  OD2 . ASP B 1 199 ? -8.318  -13.601 45.307  1.00 55.17 ? 199 ASP B OD2 1 
ATOM   5345 N  N   . GLU B 1 200 ? -4.252  -12.934 41.379  1.00 46.05 ? 200 GLU B N   1 
ATOM   5346 C  CA  . GLU B 1 200 ? -3.494  -11.969 40.526  1.00 46.44 ? 200 GLU B CA  1 
ATOM   5347 C  C   . GLU B 1 200 ? -3.358  -12.562 39.120  1.00 38.83 ? 200 GLU B C   1 
ATOM   5348 O  O   . GLU B 1 200 ? -3.740  -11.860 38.156  1.00 39.67 ? 200 GLU B O   1 
ATOM   5349 C  CB  . GLU B 1 200 ? -2.108  -11.652 41.106  1.00 47.74 ? 200 GLU B CB  1 
ATOM   5350 C  CG  . GLU B 1 200 ? -1.279  -10.687 40.257  1.00 53.62 ? 200 GLU B CG  1 
ATOM   5351 C  CD  . GLU B 1 200 ? -2.005  -9.492  39.640  1.00 58.69 ? 200 GLU B CD  1 
ATOM   5352 O  OE1 . GLU B 1 200 ? -3.024  -9.041  40.211  1.00 60.93 ? 200 GLU B OE1 1 
ATOM   5353 O  OE2 . GLU B 1 200 ? -1.552  -9.006  38.572  1.00 63.12 ? 200 GLU B OE2 1 
ATOM   5354 N  N   . ASN B 1 201 ? -2.843  -13.786 39.051  1.00 37.69 ? 201 ASN B N   1 
ATOM   5355 C  CA  . ASN B 1 201 ? -2.708  -14.583 37.796  1.00 39.37 ? 201 ASN B CA  1 
ATOM   5356 C  C   . ASN B 1 201 ? -4.072  -14.794 37.129  1.00 41.97 ? 201 ASN B C   1 
ATOM   5357 O  O   . ASN B 1 201 ? -4.108  -14.689 35.891  1.00 40.47 ? 201 ASN B O   1 
ATOM   5358 C  CB  . ASN B 1 201 ? -2.049  -15.948 37.994  1.00 41.23 ? 201 ASN B CB  1 
ATOM   5359 C  CG  . ASN B 1 201 ? -0.758  -15.918 38.775  1.00 44.88 ? 201 ASN B CG  1 
ATOM   5360 O  OD1 . ASN B 1 201 ? -0.789  -15.749 39.989  1.00 56.29 ? 201 ASN B OD1 1 
ATOM   5361 N  ND2 . ASN B 1 201 ? 0.366   -16.122 38.114  1.00 43.24 ? 201 ASN B ND2 1 
ATOM   5362 N  N   . LYS B 1 202 ? -5.142  -15.104 37.878  1.00 40.85 ? 202 LYS B N   1 
ATOM   5363 C  CA  . LYS B 1 202 ? -6.518  -15.186 37.313  1.00 38.91 ? 202 LYS B CA  1 
ATOM   5364 C  C   . LYS B 1 202 ? -6.954  -13.807 36.835  1.00 39.58 ? 202 LYS B C   1 
ATOM   5365 O  O   . LYS B 1 202 ? -7.511  -13.701 35.718  1.00 42.79 ? 202 LYS B O   1 
ATOM   5366 C  CB  . LYS B 1 202 ? -7.538  -15.688 38.338  1.00 40.74 ? 202 LYS B CB  1 
ATOM   5367 C  CG  . LYS B 1 202 ? -7.361  -17.127 38.797  1.00 41.39 ? 202 LYS B CG  1 
ATOM   5368 C  CD  . LYS B 1 202 ? -8.484  -17.588 39.740  1.00 41.30 ? 202 LYS B CD  1 
ATOM   5369 C  CE  . LYS B 1 202 ? -8.300  -18.978 40.318  1.00 42.58 ? 202 LYS B CE  1 
ATOM   5370 N  NZ  . LYS B 1 202 ? -6.867  -19.361 40.371  1.00 45.54 ? 202 LYS B NZ  1 
ATOM   5371 N  N   . ARG B 1 203 ? -6.759  -12.770 37.660  1.00 32.96 ? 203 ARG B N   1 
ATOM   5372 C  CA  . ARG B 1 203 ? -7.099  -11.383 37.263  1.00 35.34 ? 203 ARG B CA  1 
ATOM   5373 C  C   . ARG B 1 203 ? -6.405  -11.045 35.931  1.00 27.46 ? 203 ARG B C   1 
ATOM   5374 O  O   . ARG B 1 203 ? -7.092  -10.516 35.047  1.00 33.75 ? 203 ARG B O   1 
ATOM   5375 C  CB  . ARG B 1 203 ? -6.681  -10.377 38.340  1.00 39.42 ? 203 ARG B CB  1 
ATOM   5376 C  CG  . ARG B 1 203 ? -7.357  -9.018  38.184  1.00 47.00 ? 203 ARG B CG  1 
ATOM   5377 C  CD  . ARG B 1 203 ? -6.537  -7.830  38.690  1.00 51.31 ? 203 ARG B CD  1 
ATOM   5378 N  NE  . ARG B 1 203 ? -5.331  -7.569  37.907  1.00 54.89 ? 203 ARG B NE  1 
ATOM   5379 C  CZ  . ARG B 1 203 ? -5.307  -7.092  36.661  1.00 55.54 ? 203 ARG B CZ  1 
ATOM   5380 N  NH1 . ARG B 1 203 ? -6.428  -6.821  36.009  1.00 51.80 ? 203 ARG B NH1 1 
ATOM   5381 N  NH2 . ARG B 1 203 ? -4.148  -6.901  36.056  1.00 59.49 ? 203 ARG B NH2 1 
ATOM   5382 N  N   . GLN B 1 204 ? -5.110  -11.323 35.836  1.00 28.27 ? 204 GLN B N   1 
ATOM   5383 C  CA  . GLN B 1 204 ? -4.277  -10.898 34.682  1.00 29.40 ? 204 GLN B CA  1 
ATOM   5384 C  C   . GLN B 1 204 ? -4.751  -11.699 33.456  1.00 27.26 ? 204 GLN B C   1 
ATOM   5385 O  O   . GLN B 1 204 ? -4.817  -11.127 32.363  1.00 27.66 ? 204 GLN B O   1 
ATOM   5386 C  CB  . GLN B 1 204 ? -2.791  -11.085 34.958  1.00 28.60 ? 204 GLN B CB  1 
ATOM   5387 C  CG  . GLN B 1 204 ? -1.886  -10.778 33.777  1.00 29.86 ? 204 GLN B CG  1 
ATOM   5388 C  CD  . GLN B 1 204 ? -1.852  -9.302  33.464  1.00 31.14 ? 204 GLN B CD  1 
ATOM   5389 O  OE1 . GLN B 1 204 ? -0.963  -8.578  33.928  1.00 29.94 ? 204 GLN B OE1 1 
ATOM   5390 N  NE2 . GLN B 1 204 ? -2.788  -8.847  32.644  1.00 29.14 ? 204 GLN B NE2 1 
ATOM   5391 N  N   . PHE B 1 205 ? -5.035  -12.977 33.656  1.00 26.32 ? 205 PHE B N   1 
ATOM   5392 C  CA  . PHE B 1 205 ? -5.509  -13.903 32.581  1.00 27.21 ? 205 PHE B CA  1 
ATOM   5393 C  C   . PHE B 1 205 ? -6.813  -13.354 31.997  1.00 29.84 ? 205 PHE B C   1 
ATOM   5394 O  O   . PHE B 1 205 ? -6.888  -13.226 30.767  1.00 26.75 ? 205 PHE B O   1 
ATOM   5395 C  CB  . PHE B 1 205 ? -5.615  -15.330 33.128  1.00 28.57 ? 205 PHE B CB  1 
ATOM   5396 C  CG  . PHE B 1 205 ? -5.657  -16.461 32.125  1.00 27.37 ? 205 PHE B CG  1 
ATOM   5397 C  CD1 . PHE B 1 205 ? -4.649  -16.640 31.179  1.00 28.93 ? 205 PHE B CD1 1 
ATOM   5398 C  CD2 . PHE B 1 205 ? -6.692  -17.389 32.181  1.00 30.76 ? 205 PHE B CD2 1 
ATOM   5399 C  CE1 . PHE B 1 205 ? -4.677  -17.714 30.289  1.00 24.95 ? 205 PHE B CE1 1 
ATOM   5400 C  CE2 . PHE B 1 205 ? -6.719  -18.453 31.287  1.00 28.32 ? 205 PHE B CE2 1 
ATOM   5401 C  CZ  . PHE B 1 205 ? -5.717  -18.613 30.360  1.00 26.63 ? 205 PHE B CZ  1 
ATOM   5402 N  N   . GLN B 1 206 ? -7.775  -12.923 32.818  1.00 29.13 ? 206 GLN B N   1 
ATOM   5403 C  CA  . GLN B 1 206 ? -9.084  -12.422 32.336  1.00 31.16 ? 206 GLN B CA  1 
ATOM   5404 C  C   . GLN B 1 206 ? -8.872  -11.104 31.610  1.00 30.35 ? 206 GLN B C   1 
ATOM   5405 O  O   . GLN B 1 206 ? -9.528  -10.882 30.597  1.00 35.42 ? 206 GLN B O   1 
ATOM   5406 C  CB  . GLN B 1 206 ? -10.102 -12.270 33.470  1.00 33.13 ? 206 GLN B CB  1 
ATOM   5407 C  CG  . GLN B 1 206 ? -10.380 -13.587 34.158  1.00 34.79 ? 206 GLN B CG  1 
ATOM   5408 C  CD  . GLN B 1 206 ? -10.970 -14.590 33.193  1.00 36.68 ? 206 GLN B CD  1 
ATOM   5409 O  OE1 . GLN B 1 206 ? -11.890 -14.273 32.440  1.00 44.01 ? 206 GLN B OE1 1 
ATOM   5410 N  NE2 . GLN B 1 206 ? -10.443 -15.805 33.221  1.00 36.39 ? 206 GLN B NE2 1 
ATOM   5411 N  N   . GLU B 1 207 ? -7.964  -10.261 32.107  1.00 29.34 ? 207 GLU B N   1 
ATOM   5412 C  CA  . GLU B 1 207 ? -7.669  -8.973  31.447  1.00 31.55 ? 207 GLU B CA  1 
ATOM   5413 C  C   . GLU B 1 207 ? -7.079  -9.275  30.059  1.00 27.43 ? 207 GLU B C   1 
ATOM   5414 O  O   . GLU B 1 207 ? -7.422  -8.550  29.123  1.00 29.69 ? 207 GLU B O   1 
ATOM   5415 C  CB  . GLU B 1 207 ? -6.707  -8.134  32.292  1.00 36.38 ? 207 GLU B CB  1 
ATOM   5416 C  CG  . GLU B 1 207 ? -6.420  -6.755  31.718  1.00 42.20 ? 207 GLU B CG  1 
ATOM   5417 C  CD  . GLU B 1 207 ? -5.172  -6.111  32.301  1.00 48.52 ? 207 GLU B CD  1 
ATOM   5418 O  OE1 . GLU B 1 207 ? -5.053  -6.071  33.556  1.00 53.24 ? 207 GLU B OE1 1 
ATOM   5419 O  OE2 . GLU B 1 207 ? -4.299  -5.694  31.508  1.00 56.45 ? 207 GLU B OE2 1 
ATOM   5420 N  N   . ASP B 1 208 ? -6.158  -10.252 29.965  1.00 28.29 ? 208 ASP B N   1 
ATOM   5421 C  CA  . ASP B 1 208 ? -5.486  -10.609 28.669  1.00 26.10 ? 208 ASP B CA  1 
ATOM   5422 C  C   . ASP B 1 208 ? -6.518  -11.171 27.679  1.00 26.11 ? 208 ASP B C   1 
ATOM   5423 O  O   . ASP B 1 208 ? -6.472  -10.779 26.498  1.00 22.68 ? 208 ASP B O   1 
ATOM   5424 C  CB  . ASP B 1 208 ? -4.311  -11.555 28.916  1.00 26.32 ? 208 ASP B CB  1 
ATOM   5425 C  CG  . ASP B 1 208 ? -3.132  -10.818 29.545  1.00 23.42 ? 208 ASP B CG  1 
ATOM   5426 O  OD1 . ASP B 1 208 ? -3.011  -9.605  29.266  1.00 24.00 ? 208 ASP B OD1 1 
ATOM   5427 O  OD2 . ASP B 1 208 ? -2.315  -11.474 30.225  1.00 23.23 ? 208 ASP B OD2 1 
ATOM   5428 N  N   . ILE B 1 209 ? -7.446  -11.986 28.157  1.00 25.00 ? 209 ILE B N   1 
ATOM   5429 C  CA  . ILE B 1 209 ? -8.566  -12.523 27.327  1.00 28.46 ? 209 ILE B CA  1 
ATOM   5430 C  C   . ILE B 1 209 ? -9.398  -11.349 26.779  1.00 30.32 ? 209 ILE B C   1 
ATOM   5431 O  O   . ILE B 1 209 ? -9.676  -11.335 25.580  1.00 31.03 ? 209 ILE B O   1 
ATOM   5432 C  CB  . ILE B 1 209 ? -9.375  -13.556 28.131  1.00 27.80 ? 209 ILE B CB  1 
ATOM   5433 C  CG1 . ILE B 1 209 ? -8.505  -14.795 28.369  1.00 27.87 ? 209 ILE B CG1 1 
ATOM   5434 C  CG2 . ILE B 1 209 ? -10.685 -13.893 27.429  1.00 30.44 ? 209 ILE B CG2 1 
ATOM   5435 C  CD1 . ILE B 1 209 ? -9.071  -15.827 29.326  1.00 27.10 ? 209 ILE B CD1 1 
ATOM   5436 N  N   . LYS B 1 210 ? -9.711  -10.332 27.602  1.00 30.03 ? 210 LYS B N   1 
ATOM   5437 C  CA  . LYS B 1 210 ? -10.525 -9.166  27.156  1.00 31.05 ? 210 LYS B CA  1 
ATOM   5438 C  C   . LYS B 1 210 ? -9.800  -8.363  26.075  1.00 27.18 ? 210 LYS B C   1 
ATOM   5439 O  O   . LYS B 1 210 ? -10.460 -7.923  25.112  1.00 31.13 ? 210 LYS B O   1 
ATOM   5440 C  CB  . LYS B 1 210 ? -10.886 -8.233  28.322  1.00 35.11 ? 210 LYS B CB  1 
ATOM   5441 C  CG  . LYS B 1 210 ? -11.969 -7.220  27.988  1.00 42.86 ? 210 LYS B CG  1 
ATOM   5442 C  CD  . LYS B 1 210 ? -11.771 -5.833  28.626  1.00 48.09 ? 210 LYS B CD  1 
ATOM   5443 C  CE  . LYS B 1 210 ? -12.822 -4.809  28.233  1.00 52.01 ? 210 LYS B CE  1 
ATOM   5444 N  NZ  . LYS B 1 210 ? -14.139 -5.433  27.950  1.00 53.30 ? 210 LYS B NZ  1 
ATOM   5445 N  N   . VAL B 1 211 ? -8.490  -8.129  26.221  1.00 24.94 ? 211 VAL B N   1 
ATOM   5446 C  CA  . VAL B 1 211 ? -7.697  -7.349  25.237  1.00 25.47 ? 211 VAL B CA  1 
ATOM   5447 C  C   . VAL B 1 211 ? -7.822  -8.053  23.879  1.00 24.41 ? 211 VAL B C   1 
ATOM   5448 O  O   . VAL B 1 211 ? -7.947  -7.364  22.807  1.00 26.48 ? 211 VAL B O   1 
ATOM   5449 C  CB  . VAL B 1 211 ? -6.227  -7.264  25.683  1.00 25.16 ? 211 VAL B CB  1 
ATOM   5450 C  CG1 . VAL B 1 211 ? -5.289  -6.821  24.584  1.00 27.21 ? 211 VAL B CG1 1 
ATOM   5451 C  CG2 . VAL B 1 211 ? -6.089  -6.351  26.896  1.00 27.68 ? 211 VAL B CG2 1 
ATOM   5452 N  N   . MET B 1 212 ? -7.629  -9.376  23.913  1.00 26.35 ? 212 MET B N   1 
ATOM   5453 C  CA  . MET B 1 212 ? -7.578  -10.174 22.651  1.00 23.53 ? 212 MET B CA  1 
ATOM   5454 C  C   . MET B 1 212 ? -8.965  -10.157 22.006  1.00 22.76 ? 212 MET B C   1 
ATOM   5455 O  O   . MET B 1 212 ? -9.050  -9.941  20.813  1.00 22.15 ? 212 MET B O   1 
ATOM   5456 C  CB  . MET B 1 212 ? -7.142  -11.623 22.906  1.00 22.04 ? 212 MET B CB  1 
ATOM   5457 C  CG  . MET B 1 212 ? -5.631  -11.733 23.135  1.00 21.08 ? 212 MET B CG  1 
ATOM   5458 S  SD  . MET B 1 212 ? -5.058  -13.481 23.298  1.00 21.93 ? 212 MET B SD  1 
ATOM   5459 C  CE  . MET B 1 212 ? -5.441  -13.776 25.007  1.00 20.95 ? 212 MET B CE  1 
ATOM   5460 N  N   . ASN B 1 213 ? -10.001 -10.422 22.788  1.00 23.78 ? 213 ASN B N   1 
ATOM   5461 C  CA  . ASN B 1 213 ? -11.411 -10.436 22.314  1.00 25.74 ? 213 ASN B CA  1 
ATOM   5462 C  C   . ASN B 1 213 ? -11.800 -9.064  21.753  1.00 28.77 ? 213 ASN B C   1 
ATOM   5463 O  O   . ASN B 1 213 ? -12.465 -8.998  20.689  1.00 28.32 ? 213 ASN B O   1 
ATOM   5464 C  CB  . ASN B 1 213 ? -12.364 -10.883 23.406  1.00 27.52 ? 213 ASN B CB  1 
ATOM   5465 C  CG  . ASN B 1 213 ? -12.258 -12.356 23.721  1.00 28.93 ? 213 ASN B CG  1 
ATOM   5466 O  OD1 . ASN B 1 213 ? -11.570 -13.111 23.003  1.00 26.71 ? 213 ASN B OD1 1 
ATOM   5467 N  ND2 . ASN B 1 213 ? -12.915 -12.762 24.784  1.00 30.33 ? 213 ASN B ND2 1 
ATOM   5468 N  N   . ASP B 1 214 ? -11.353 -7.998  22.413  1.00 34.31 ? 214 ASP B N   1 
ATOM   5469 C  CA  . ASP B 1 214 ? -11.684 -6.611  22.016  1.00 32.90 ? 214 ASP B CA  1 
ATOM   5470 C  C   . ASP B 1 214 ? -11.146 -6.306  20.626  1.00 31.83 ? 214 ASP B C   1 
ATOM   5471 O  O   . ASP B 1 214 ? -11.976 -5.814  19.837  1.00 31.89 ? 214 ASP B O   1 
ATOM   5472 C  CB  . ASP B 1 214 ? -11.165 -5.585  23.025  1.00 37.16 ? 214 ASP B CB  1 
ATOM   5473 C  CG  . ASP B 1 214 ? -12.021 -5.488  24.265  1.00 39.69 ? 214 ASP B CG  1 
ATOM   5474 O  OD1 . ASP B 1 214 ? -13.057 -6.172  24.325  1.00 41.34 ? 214 ASP B OD1 1 
ATOM   5475 O  OD2 . ASP B 1 214 ? -11.641 -4.713  25.159  1.00 52.51 ? 214 ASP B OD2 1 
ATOM   5476 N  N   . LEU B 1 215 ? -9.840  -6.511  20.354  1.00 24.56 ? 215 LEU B N   1 
ATOM   5477 C  CA  . LEU B 1 215 ? -9.245  -6.168  19.037  1.00 27.58 ? 215 LEU B CA  1 
ATOM   5478 C  C   . LEU B 1 215 ? -9.936  -7.047  18.002  1.00 22.28 ? 215 LEU B C   1 
ATOM   5479 O  O   . LEU B 1 215 ? -10.309 -6.560  16.967  1.00 23.74 ? 215 LEU B O   1 
ATOM   5480 C  CB  . LEU B 1 215 ? -7.730  -6.373  18.966  1.00 27.66 ? 215 LEU B CB  1 
ATOM   5481 C  CG  . LEU B 1 215 ? -7.115  -6.130  17.569  1.00 31.56 ? 215 LEU B CG  1 
ATOM   5482 C  CD1 . LEU B 1 215 ? -7.133  -4.648  17.181  1.00 34.70 ? 215 LEU B CD1 1 
ATOM   5483 C  CD2 . LEU B 1 215 ? -5.697  -6.680  17.455  1.00 34.66 ? 215 LEU B CD2 1 
ATOM   5484 N  N   . VAL B 1 216 ? -10.001 -8.365  18.247  1.00 24.95 ? 216 VAL B N   1 
ATOM   5485 C  CA  . VAL B 1 216 ? -10.443 -9.246  17.138  1.00 21.49 ? 216 VAL B CA  1 
ATOM   5486 C  C   . VAL B 1 216 ? -11.956 -9.017  16.892  1.00 18.83 ? 216 VAL B C   1 
ATOM   5487 O  O   . VAL B 1 216 ? -12.310 -8.996  15.751  1.00 20.13 ? 216 VAL B O   1 
ATOM   5488 C  CB  . VAL B 1 216 ? -10.086 -10.715 17.422  1.00 19.74 ? 216 VAL B CB  1 
ATOM   5489 C  CG1 . VAL B 1 216 ? -10.602 -11.607 16.329  1.00 19.43 ? 216 VAL B CG1 1 
ATOM   5490 C  CG2 . VAL B 1 216 ? -8.600  -10.888 17.554  1.00 21.80 ? 216 VAL B CG2 1 
ATOM   5491 N  N   . ASP B 1 217 ? -12.788 -8.906  17.920  1.00 19.74 ? 217 ASP B N   1 
ATOM   5492 C  CA  . ASP B 1 217 ? -14.261 -8.666  17.723  1.00 21.07 ? 217 ASP B CA  1 
ATOM   5493 C  C   . ASP B 1 217 ? -14.439 -7.347  16.939  1.00 24.84 ? 217 ASP B C   1 
ATOM   5494 O  O   . ASP B 1 217 ? -15.300 -7.292  16.056  1.00 24.56 ? 217 ASP B O   1 
ATOM   5495 C  CB  . ASP B 1 217 ? -15.039 -8.604  19.021  1.00 22.07 ? 217 ASP B CB  1 
ATOM   5496 C  CG  . ASP B 1 217 ? -15.198 -9.929  19.741  1.00 25.44 ? 217 ASP B CG  1 
ATOM   5497 O  OD1 . ASP B 1 217 ? -14.902 -10.945 19.072  1.00 24.38 ? 217 ASP B OD1 1 
ATOM   5498 O  OD2 . ASP B 1 217 ? -15.581 -9.936  20.953  1.00 28.22 ? 217 ASP B OD2 1 
ATOM   5499 N  N   . LYS B 1 218 ? -13.615 -6.338  17.229  1.00 27.02 ? 218 LYS B N   1 
ATOM   5500 C  CA  . LYS B 1 218 ? -13.673 -5.031  16.512  1.00 27.04 ? 218 LYS B CA  1 
ATOM   5501 C  C   . LYS B 1 218 ? -13.192 -5.187  15.065  1.00 24.40 ? 218 LYS B C   1 
ATOM   5502 O  O   . LYS B 1 218 ? -13.889 -4.706  14.106  1.00 25.99 ? 218 LYS B O   1 
ATOM   5503 C  CB  . LYS B 1 218 ? -12.868 -3.985  17.293  1.00 29.67 ? 218 LYS B CB  1 
ATOM   5504 C  CG  . LYS B 1 218 ? -12.831 -2.603  16.652  1.00 36.58 ? 218 LYS B CG  1 
ATOM   5505 C  CD  . LYS B 1 218 ? -12.035 -1.597  17.440  1.00 40.96 ? 218 LYS B CD  1 
ATOM   5506 C  CE  . LYS B 1 218 ? -12.433 -0.163  17.148  1.00 46.15 ? 218 LYS B CE  1 
ATOM   5507 N  NZ  . LYS B 1 218 ? -12.488 0.097   15.688  1.00 50.63 ? 218 LYS B NZ  1 
ATOM   5508 N  N   . ILE B 1 219 ? -12.107 -5.930  14.824  1.00 23.45 ? 219 ILE B N   1 
ATOM   5509 C  CA  . ILE B 1 219 ? -11.697 -6.290  13.434  1.00 26.14 ? 219 ILE B CA  1 
ATOM   5510 C  C   . ILE B 1 219 ? -12.894 -6.882  12.665  1.00 22.77 ? 219 ILE B C   1 
ATOM   5511 O  O   . ILE B 1 219 ? -13.175 -6.510  11.502  1.00 21.76 ? 219 ILE B O   1 
ATOM   5512 C  CB  . ILE B 1 219 ? -10.489 -7.250  13.473  1.00 27.47 ? 219 ILE B CB  1 
ATOM   5513 C  CG1 . ILE B 1 219 ? -9.217  -6.505  13.914  1.00 30.83 ? 219 ILE B CG1 1 
ATOM   5514 C  CG2 . ILE B 1 219 ? -10.312 -7.952  12.131  1.00 30.09 ? 219 ILE B CG2 1 
ATOM   5515 C  CD1 . ILE B 1 219 ? -8.059  -7.406  14.283  1.00 34.41 ? 219 ILE B CD1 1 
ATOM   5516 N  N   . ILE B 1 220 ? -13.533 -7.905  13.216  1.00 21.06 ? 220 ILE B N   1 
ATOM   5517 C  CA  . ILE B 1 220 ? -14.633 -8.584  12.480  1.00 21.44 ? 220 ILE B CA  1 
ATOM   5518 C  C   . ILE B 1 220 ? -15.790 -7.587  12.212  1.00 19.34 ? 220 ILE B C   1 
ATOM   5519 O  O   . ILE B 1 220 ? -16.281 -7.585  11.063  1.00 19.63 ? 220 ILE B O   1 
ATOM   5520 C  CB  . ILE B 1 220 ? -15.078 -9.809  13.295  1.00 21.56 ? 220 ILE B CB  1 
ATOM   5521 C  CG1 . ILE B 1 220 ? -13.933 -10.826 13.408  1.00 20.67 ? 220 ILE B CG1 1 
ATOM   5522 C  CG2 . ILE B 1 220 ? -16.330 -10.415 12.667  1.00 22.89 ? 220 ILE B CG2 1 
ATOM   5523 C  CD1 . ILE B 1 220 ? -14.182 -11.897 14.434  1.00 19.47 ? 220 ILE B CD1 1 
ATOM   5524 N  N   . ALA B 1 221 ? -16.203 -6.848  13.231  1.00 23.71 ? 221 ALA B N   1 
ATOM   5525 C  CA  . ALA B 1 221 ? -17.337 -5.881  13.139  1.00 24.88 ? 221 ALA B CA  1 
ATOM   5526 C  C   . ALA B 1 221 ? -17.033 -4.828  12.041  1.00 23.79 ? 221 ALA B C   1 
ATOM   5527 O  O   . ALA B 1 221 ? -17.928 -4.565  11.167  1.00 22.76 ? 221 ALA B O   1 
ATOM   5528 C  CB  . ALA B 1 221 ? -17.554 -5.276  14.488  1.00 25.03 ? 221 ALA B CB  1 
ATOM   5529 N  N   . ASP B 1 222 ? -15.813 -4.287  12.061  1.00 25.16 ? 222 ASP B N   1 
ATOM   5530 C  CA  . ASP B 1 222 ? -15.354 -3.282  11.066  1.00 26.89 ? 222 ASP B CA  1 
ATOM   5531 C  C   . ASP B 1 222 ? -15.449 -3.884  9.667   1.00 26.59 ? 222 ASP B C   1 
ATOM   5532 O  O   . ASP B 1 222 ? -15.856 -3.212  8.703   1.00 26.59 ? 222 ASP B O   1 
ATOM   5533 C  CB  . ASP B 1 222 ? -13.925 -2.796  11.342  1.00 29.98 ? 222 ASP B CB  1 
ATOM   5534 C  CG  . ASP B 1 222 ? -13.698 -1.933  12.581  1.00 31.74 ? 222 ASP B CG  1 
ATOM   5535 O  OD1 . ASP B 1 222 ? -14.678 -1.466  13.192  1.00 33.94 ? 222 ASP B OD1 1 
ATOM   5536 O  OD2 . ASP B 1 222 ? -12.524 -1.703  12.908  1.00 38.55 ? 222 ASP B OD2 1 
ATOM   5537 N  N   . ARG B 1 223 ? -15.050 -5.159  9.501   1.00 21.90 ? 223 ARG B N   1 
ATOM   5538 C  CA  . ARG B 1 223 ? -15.113 -5.777  8.174   1.00 21.41 ? 223 ARG B CA  1 
ATOM   5539 C  C   . ARG B 1 223 ? -16.567 -5.948  7.764   1.00 23.04 ? 223 ARG B C   1 
ATOM   5540 O  O   . ARG B 1 223 ? -16.859 -5.730  6.597   1.00 24.69 ? 223 ARG B O   1 
ATOM   5541 C  CB  . ARG B 1 223 ? -14.359 -7.120  8.159   1.00 19.25 ? 223 ARG B CB  1 
ATOM   5542 C  CG  . ARG B 1 223 ? -14.325 -7.776  6.782   1.00 20.51 ? 223 ARG B CG  1 
ATOM   5543 C  CD  . ARG B 1 223 ? -13.583 -6.958  5.739   1.00 23.08 ? 223 ARG B CD  1 
ATOM   5544 N  NE  . ARG B 1 223 ? -12.178 -6.943  6.087   1.00 23.56 ? 223 ARG B NE  1 
ATOM   5545 C  CZ  . ARG B 1 223 ? -11.332 -7.977  5.829   1.00 24.81 ? 223 ARG B CZ  1 
ATOM   5546 N  NH1 . ARG B 1 223 ? -11.762 -9.071  5.227   1.00 23.88 ? 223 ARG B NH1 1 
ATOM   5547 N  NH2 . ARG B 1 223 ? -10.062 -7.916  6.165   1.00 25.41 ? 223 ARG B NH2 1 
ATOM   5548 N  N   . LYS B 1 224 ? -17.430 -6.376  8.695   1.00 25.38 ? 224 LYS B N   1 
ATOM   5549 C  CA  . LYS B 1 224 ? -18.867 -6.565  8.362   1.00 27.53 ? 224 LYS B CA  1 
ATOM   5550 C  C   . LYS B 1 224 ? -19.462 -5.187  8.048   1.00 28.21 ? 224 LYS B C   1 
ATOM   5551 O  O   . LYS B 1 224 ? -20.201 -5.133  7.067   1.00 34.16 ? 224 LYS B O   1 
ATOM   5552 C  CB  . LYS B 1 224 ? -19.605 -7.253  9.505   1.00 31.78 ? 224 LYS B CB  1 
ATOM   5553 C  CG  . LYS B 1 224 ? -19.164 -8.690  9.731   1.00 32.79 ? 224 LYS B CG  1 
ATOM   5554 C  CD  . LYS B 1 224 ? -19.942 -9.341  10.855  1.00 33.48 ? 224 LYS B CD  1 
ATOM   5555 C  CE  . LYS B 1 224 ? -21.305 -9.778  10.376  1.00 36.32 ? 224 LYS B CE  1 
ATOM   5556 N  NZ  . LYS B 1 224 ? -22.017 -10.568 11.404  1.00 35.65 ? 224 LYS B NZ  1 
ATOM   5557 N  N   . ALA B 1 225 ? -19.072 -4.155  8.802   1.00 31.82 ? 225 ALA B N   1 
ATOM   5558 C  CA  . ALA B 1 225 ? -19.573 -2.753  8.668   1.00 33.12 ? 225 ALA B CA  1 
ATOM   5559 C  C   . ALA B 1 225 ? -19.034 -2.098  7.388   1.00 39.79 ? 225 ALA B C   1 
ATOM   5560 O  O   . ALA B 1 225 ? -19.599 -1.062  7.015   1.00 37.88 ? 225 ALA B O   1 
ATOM   5561 C  CB  . ALA B 1 225 ? -19.229 -1.952  9.893   1.00 32.25 ? 225 ALA B CB  1 
ATOM   5562 N  N   . SER B 1 226 ? -18.057 -2.691  6.684   1.00 36.32 ? 226 SER B N   1 
ATOM   5563 C  CA  . SER B 1 226 ? -17.463 -2.110  5.443   1.00 37.42 ? 226 SER B CA  1 
ATOM   5564 C  C   . SER B 1 226 ? -18.028 -2.767  4.170   1.00 38.48 ? 226 SER B C   1 
ATOM   5565 O  O   . SER B 1 226 ? -18.073 -2.094  3.114   1.00 45.54 ? 226 SER B O   1 
ATOM   5566 C  CB  . SER B 1 226 ? -15.964 -2.237  5.493   1.00 41.01 ? 226 SER B CB  1 
ATOM   5567 O  OG  . SER B 1 226 ? -15.593 -3.491  4.960   1.00 35.10 ? 226 SER B OG  1 
ATOM   5568 N  N   . GLY B 1 227 ? -18.378 -4.056  4.217   1.00 37.19 ? 227 GLY B N   1 
ATOM   5569 C  CA  . GLY B 1 227 ? -18.700 -4.877  3.035   1.00 38.15 ? 227 GLY B CA  1 
ATOM   5570 C  C   . GLY B 1 227 ? -17.489 -5.231  2.172   1.00 35.34 ? 227 GLY B C   1 
ATOM   5571 O  O   . GLY B 1 227 ? -17.662 -6.030  1.279   1.00 38.19 ? 227 GLY B O   1 
ATOM   5572 N  N   . GLU B 1 228 ? -16.304 -4.677  2.452   1.00 42.10 ? 228 GLU B N   1 
ATOM   5573 C  CA  . GLU B 1 228 ? -15.057 -4.862  1.648   1.00 41.69 ? 228 GLU B CA  1 
ATOM   5574 C  C   . GLU B 1 228 ? -14.782 -6.368  1.483   1.00 38.02 ? 228 GLU B C   1 
ATOM   5575 O  O   . GLU B 1 228 ? -14.889 -7.076  2.473   1.00 39.77 ? 228 GLU B O   1 
ATOM   5576 C  CB  . GLU B 1 228 ? -13.919 -4.075  2.310   1.00 45.79 ? 228 GLU B CB  1 
ATOM   5577 C  CG  . GLU B 1 228 ? -12.532 -4.691  2.173   1.00 52.38 ? 228 GLU B CG  1 
ATOM   5578 C  CD  . GLU B 1 228 ? -11.614 -4.420  3.360   1.00 58.35 ? 228 GLU B CD  1 
ATOM   5579 O  OE1 . GLU B 1 228 ? -11.857 -3.425  4.084   1.00 57.71 ? 228 GLU B OE1 1 
ATOM   5580 O  OE2 . GLU B 1 228 ? -10.671 -5.227  3.582   1.00 67.51 ? 228 GLU B OE2 1 
ATOM   5581 N  N   . GLN B 1 229 ? -14.474 -6.815  0.265   1.00 40.65 ? 229 GLN B N   1 
ATOM   5582 C  CA  . GLN B 1 229 ? -14.096 -8.215  -0.099  1.00 40.12 ? 229 GLN B CA  1 
ATOM   5583 C  C   . GLN B 1 229 ? -12.587 -8.227  -0.385  1.00 44.80 ? 229 GLN B C   1 
ATOM   5584 O  O   . GLN B 1 229 ? -12.184 -7.600  -1.376  1.00 44.75 ? 229 GLN B O   1 
ATOM   5585 C  CB  . GLN B 1 229 ? -14.904 -8.700  -1.318  1.00 45.05 ? 229 GLN B CB  1 
ATOM   5586 C  CG  . GLN B 1 229 ? -15.888 -9.845  -1.054  1.00 46.52 ? 229 GLN B CG  1 
ATOM   5587 C  CD  . GLN B 1 229 ? -16.927 -9.609  0.024   1.00 46.63 ? 229 GLN B CD  1 
ATOM   5588 O  OE1 . GLN B 1 229 ? -17.607 -10.533 0.450   1.00 55.75 ? 229 GLN B OE1 1 
ATOM   5589 N  NE2 . GLN B 1 229 ? -17.101 -8.377  0.462   1.00 50.39 ? 229 GLN B NE2 1 
ATOM   5590 N  N   . SER B 1 230 ? -11.771 -8.889  0.443   1.00 43.94 ? 230 SER B N   1 
ATOM   5591 C  CA  . SER B 1 230 ? -10.296 -8.931  0.273   1.00 40.54 ? 230 SER B CA  1 
ATOM   5592 C  C   . SER B 1 230 ? -9.827  -10.344 -0.069  1.00 38.61 ? 230 SER B C   1 
ATOM   5593 O  O   . SER B 1 230 ? -10.646 -11.259 -0.145  1.00 38.11 ? 230 SER B O   1 
ATOM   5594 C  CB  . SER B 1 230 ? -9.566  -8.398  1.485   1.00 44.45 ? 230 SER B CB  1 
ATOM   5595 O  OG  . SER B 1 230 ? -10.177 -7.220  1.983   1.00 48.95 ? 230 SER B OG  1 
ATOM   5596 N  N   . ASP B 1 231 ? -8.527  -10.511 -0.267  1.00 43.34 ? 231 ASP B N   1 
ATOM   5597 C  CA  . ASP B 1 231 ? -7.927  -11.831 -0.589  1.00 46.51 ? 231 ASP B CA  1 
ATOM   5598 C  C   . ASP B 1 231 ? -7.586  -12.544 0.725   1.00 42.97 ? 231 ASP B C   1 
ATOM   5599 O  O   . ASP B 1 231 ? -6.614  -13.330 0.712   1.00 44.61 ? 231 ASP B O   1 
ATOM   5600 C  CB  . ASP B 1 231 ? -6.687  -11.694 -1.484  1.00 50.14 ? 231 ASP B CB  1 
ATOM   5601 C  CG  . ASP B 1 231 ? -6.933  -11.974 -2.962  1.00 58.79 ? 231 ASP B CG  1 
ATOM   5602 O  OD1 . ASP B 1 231 ? -7.439  -13.080 -3.287  1.00 64.18 ? 231 ASP B OD1 1 
ATOM   5603 O  OD2 . ASP B 1 231 ? -6.593  -11.098 -3.777  1.00 63.79 ? 231 ASP B OD2 1 
ATOM   5604 N  N   . ASP B 1 232 ? -8.358  -12.341 1.806   1.00 40.46 ? 232 ASP B N   1 
ATOM   5605 C  CA  . ASP B 1 232 ? -7.897  -12.829 3.136   1.00 29.92 ? 232 ASP B CA  1 
ATOM   5606 C  C   . ASP B 1 232 ? -8.828  -13.894 3.748   1.00 26.72 ? 232 ASP B C   1 
ATOM   5607 O  O   . ASP B 1 232 ? -9.973  -14.077 3.356   1.00 26.20 ? 232 ASP B O   1 
ATOM   5608 C  CB  . ASP B 1 232 ? -7.634  -11.690 4.114   1.00 27.44 ? 232 ASP B CB  1 
ATOM   5609 C  CG  . ASP B 1 232 ? -8.834  -10.855 4.490   1.00 25.13 ? 232 ASP B CG  1 
ATOM   5610 O  OD1 . ASP B 1 232 ? -9.988  -11.350 4.448   1.00 24.07 ? 232 ASP B OD1 1 
ATOM   5611 O  OD2 . ASP B 1 232 ? -8.612  -9.742  4.867   1.00 26.92 ? 232 ASP B OD2 1 
ATOM   5612 N  N   . LEU B 1 233 ? -8.322  -14.556 4.776   1.00 21.73 ? 233 LEU B N   1 
ATOM   5613 C  CA  . LEU B 1 233 ? -9.105  -15.624 5.471   1.00 21.01 ? 233 LEU B CA  1 
ATOM   5614 C  C   . LEU B 1 233 ? -10.385 -15.056 6.070   1.00 19.50 ? 233 LEU B C   1 
ATOM   5615 O  O   . LEU B 1 233 ? -11.397 -15.791 6.140   1.00 20.37 ? 233 LEU B O   1 
ATOM   5616 C  CB  . LEU B 1 233 ? -8.224  -16.247 6.540   1.00 18.69 ? 233 LEU B CB  1 
ATOM   5617 C  CG  . LEU B 1 233 ? -7.121  -17.118 6.009   1.00 20.45 ? 233 LEU B CG  1 
ATOM   5618 C  CD1 . LEU B 1 233 ? -6.086  -17.422 7.103   1.00 23.70 ? 233 LEU B CD1 1 
ATOM   5619 C  CD2 . LEU B 1 233 ? -7.725  -18.384 5.475   1.00 23.50 ? 233 LEU B CD2 1 
ATOM   5620 N  N   . LEU B 1 234 ? -10.386 -13.826 6.585   1.00 19.13 ? 234 LEU B N   1 
ATOM   5621 C  CA  . LEU B 1 234 ? -11.599 -13.243 7.232   1.00 17.85 ? 234 LEU B CA  1 
ATOM   5622 C  C   . LEU B 1 234 ? -12.752 -13.119 6.199   1.00 20.70 ? 234 LEU B C   1 
ATOM   5623 O  O   . LEU B 1 234 ? -13.887 -13.412 6.559   1.00 19.72 ? 234 LEU B O   1 
ATOM   5624 C  CB  . LEU B 1 234 ? -11.266 -11.888 7.863   1.00 18.28 ? 234 LEU B CB  1 
ATOM   5625 C  CG  . LEU B 1 234 ? -12.430 -11.138 8.498   1.00 18.13 ? 234 LEU B CG  1 
ATOM   5626 C  CD1 . LEU B 1 234 ? -13.279 -12.011 9.435   1.00 19.62 ? 234 LEU B CD1 1 
ATOM   5627 C  CD2 . LEU B 1 234 ? -11.940 -9.894  9.213   1.00 19.57 ? 234 LEU B CD2 1 
ATOM   5628 N  N   . THR B 1 235 ? -12.451 -12.702 4.979   1.00 24.15 ? 235 THR B N   1 
ATOM   5629 C  CA  . THR B 1 235 ? -13.515 -12.619 3.924   1.00 25.30 ? 235 THR B CA  1 
ATOM   5630 C  C   . THR B 1 235 ? -14.110 -14.014 3.737   1.00 26.50 ? 235 THR B C   1 
ATOM   5631 O  O   . THR B 1 235 ? -15.372 -14.115 3.747   1.00 25.57 ? 235 THR B O   1 
ATOM   5632 C  CB  . THR B 1 235 ? -12.969 -12.117 2.593   1.00 29.85 ? 235 THR B CB  1 
ATOM   5633 O  OG1 . THR B 1 235 ? -12.540 -10.785 2.837   1.00 29.21 ? 235 THR B OG1 1 
ATOM   5634 C  CG2 . THR B 1 235 ? -14.011 -12.116 1.488   1.00 29.71 ? 235 THR B CG2 1 
ATOM   5635 N  N   . HIS B 1 236 ? -13.234 -15.016 3.577   1.00 22.10 ? 236 HIS B N   1 
ATOM   5636 C  CA  . HIS B 1 236 ? -13.605 -16.450 3.375   1.00 23.44 ? 236 HIS B CA  1 
ATOM   5637 C  C   . HIS B 1 236 ? -14.490 -16.889 4.543   1.00 23.31 ? 236 HIS B C   1 
ATOM   5638 O  O   . HIS B 1 236 ? -15.511 -17.542 4.313   1.00 23.47 ? 236 HIS B O   1 
ATOM   5639 C  CB  . HIS B 1 236 ? -12.409 -17.369 3.176   1.00 26.66 ? 236 HIS B CB  1 
ATOM   5640 C  CG  . HIS B 1 236 ? -11.409 -16.890 2.176   1.00 37.97 ? 236 HIS B CG  1 
ATOM   5641 N  ND1 . HIS B 1 236 ? -10.071 -17.255 2.247   1.00 36.72 ? 236 HIS B ND1 1 
ATOM   5642 C  CD2 . HIS B 1 236 ? -11.520 -16.054 1.109   1.00 39.58 ? 236 HIS B CD2 1 
ATOM   5643 C  CE1 . HIS B 1 236 ? -9.399  -16.682 1.267   1.00 40.31 ? 236 HIS B CE1 1 
ATOM   5644 N  NE2 . HIS B 1 236 ? -10.269 -15.916 0.562   1.00 44.81 ? 236 HIS B NE2 1 
ATOM   5645 N  N   . MET B 1 237 ? -14.173 -16.533 5.779   1.00 19.63 ? 237 MET B N   1 
ATOM   5646 C  CA  . MET B 1 237 ? -14.969 -16.959 6.927   1.00 19.30 ? 237 MET B CA  1 
ATOM   5647 C  C   . MET B 1 237 ? -16.310 -16.232 6.988   1.00 19.41 ? 237 MET B C   1 
ATOM   5648 O  O   . MET B 1 237 ? -17.309 -16.806 7.483   1.00 20.64 ? 237 MET B O   1 
ATOM   5649 C  CB  . MET B 1 237 ? -14.216 -16.775 8.245   1.00 18.05 ? 237 MET B CB  1 
ATOM   5650 C  CG  . MET B 1 237 ? -13.094 -17.795 8.353   1.00 17.87 ? 237 MET B CG  1 
ATOM   5651 S  SD  . MET B 1 237 ? -12.299 -17.808 9.986   1.00 18.37 ? 237 MET B SD  1 
ATOM   5652 C  CE  . MET B 1 237 ? -11.365 -16.270 9.902   1.00 16.36 ? 237 MET B CE  1 
ATOM   5653 N  N   . LEU B 1 238 ? -16.350 -14.971 6.587   1.00 20.72 ? 238 LEU B N   1 
ATOM   5654 C  CA  . LEU B 1 238 ? -17.624 -14.205 6.673   1.00 22.95 ? 238 LEU B CA  1 
ATOM   5655 C  C   . LEU B 1 238 ? -18.580 -14.690 5.588   1.00 24.53 ? 238 LEU B C   1 
ATOM   5656 O  O   . LEU B 1 238 ? -19.789 -14.560 5.830   1.00 32.04 ? 238 LEU B O   1 
ATOM   5657 C  CB  . LEU B 1 238 ? -17.324 -12.706 6.551   1.00 24.13 ? 238 LEU B CB  1 
ATOM   5658 C  CG  . LEU B 1 238 ? -16.773 -12.079 7.821   1.00 23.47 ? 238 LEU B CG  1 
ATOM   5659 C  CD1 . LEU B 1 238 ? -16.345 -10.634 7.520   1.00 25.82 ? 238 LEU B CD1 1 
ATOM   5660 C  CD2 . LEU B 1 238 ? -17.724 -12.091 8.987   1.00 24.25 ? 238 LEU B CD2 1 
ATOM   5661 N  N   . ASN B 1 239 ? -18.084 -15.239 4.491   1.00 23.04 ? 239 ASN B N   1 
ATOM   5662 C  CA  . ASN B 1 239 ? -18.924 -15.610 3.309   1.00 28.70 ? 239 ASN B CA  1 
ATOM   5663 C  C   . ASN B 1 239 ? -19.109 -17.123 3.154   1.00 31.69 ? 239 ASN B C   1 
ATOM   5664 O  O   . ASN B 1 239 ? -20.087 -17.540 2.483   1.00 32.23 ? 239 ASN B O   1 
ATOM   5665 C  CB  . ASN B 1 239 ? -18.310 -15.113 2.008   1.00 32.28 ? 239 ASN B CB  1 
ATOM   5666 C  CG  . ASN B 1 239 ? -18.305 -13.603 1.923   1.00 33.05 ? 239 ASN B CG  1 
ATOM   5667 O  OD1 . ASN B 1 239 ? -19.059 -12.926 2.635   1.00 34.76 ? 239 ASN B OD1 1 
ATOM   5668 N  ND2 . ASN B 1 239 ? -17.429 -13.099 1.080   1.00 35.19 ? 239 ASN B ND2 1 
ATOM   5669 N  N   . GLY B 1 240 ? -18.186 -17.922 3.673   1.00 23.68 ? 240 GLY B N   1 
ATOM   5670 C  CA  . GLY B 1 240 ? -18.112 -19.367 3.434   1.00 23.30 ? 240 GLY B CA  1 
ATOM   5671 C  C   . GLY B 1 240 ? -19.260 -20.085 4.109   1.00 20.93 ? 240 GLY B C   1 
ATOM   5672 O  O   . GLY B 1 240 ? -19.760 -19.652 5.133   1.00 21.78 ? 240 GLY B O   1 
ATOM   5673 N  N   . LYS B 1 241 ? -19.697 -21.152 3.487   1.00 19.85 ? 241 LYS B N   1 
ATOM   5674 C  CA  . LYS B 1 241 ? -20.757 -22.024 4.030   1.00 20.09 ? 241 LYS B CA  1 
ATOM   5675 C  C   . LYS B 1 241 ? -20.200 -23.442 4.029   1.00 17.48 ? 241 LYS B C   1 
ATOM   5676 O  O   . LYS B 1 241 ? -19.582 -23.903 3.083   1.00 18.81 ? 241 LYS B O   1 
ATOM   5677 C  CB  . LYS B 1 241 ? -22.017 -21.951 3.162   1.00 22.80 ? 241 LYS B CB  1 
ATOM   5678 C  CG  . LYS B 1 241 ? -22.617 -20.556 3.053   1.00 28.77 ? 241 LYS B CG  1 
ATOM   5679 C  CD  . LYS B 1 241 ? -23.428 -20.126 4.220   1.00 34.77 ? 241 LYS B CD  1 
ATOM   5680 C  CE  . LYS B 1 241 ? -24.669 -19.343 3.816   1.00 43.00 ? 241 LYS B CE  1 
ATOM   5681 N  NZ  . LYS B 1 241 ? -24.343 -18.149 3.002   1.00 47.02 ? 241 LYS B NZ  1 
ATOM   5682 N  N   . ASP B 1 242 ? -20.420 -24.140 5.122   1.00 15.12 ? 242 ASP B N   1 
ATOM   5683 C  CA  . ASP B 1 242 ? -20.040 -25.565 5.220   1.00 14.93 ? 242 ASP B CA  1 
ATOM   5684 C  C   . ASP B 1 242 ? -20.865 -26.381 4.217   1.00 16.41 ? 242 ASP B C   1 
ATOM   5685 O  O   . ASP B 1 242 ? -22.089 -26.426 4.362   1.00 17.26 ? 242 ASP B O   1 
ATOM   5686 C  CB  . ASP B 1 242 ? -20.151 -26.025 6.674   1.00 14.75 ? 242 ASP B CB  1 
ATOM   5687 C  CG  . ASP B 1 242 ? -20.098 -27.519 6.850   1.00 15.19 ? 242 ASP B CG  1 
ATOM   5688 O  OD1 . ASP B 1 242 ? -19.433 -28.222 6.022   1.00 15.42 ? 242 ASP B OD1 1 
ATOM   5689 O  OD2 . ASP B 1 242 ? -20.768 -28.004 7.767   1.00 15.96 ? 242 ASP B OD2 1 
ATOM   5690 N  N   . PRO B 1 243 ? -20.258 -27.118 3.264   1.00 18.42 ? 243 PRO B N   1 
ATOM   5691 C  CA  . PRO B 1 243 ? -21.049 -27.973 2.366   1.00 19.77 ? 243 PRO B CA  1 
ATOM   5692 C  C   . PRO B 1 243 ? -21.960 -28.940 3.120   1.00 21.35 ? 243 PRO B C   1 
ATOM   5693 O  O   . PRO B 1 243 ? -23.028 -29.304 2.611   1.00 21.74 ? 243 PRO B O   1 
ATOM   5694 C  CB  . PRO B 1 243 ? -20.024 -28.733 1.503   1.00 21.53 ? 243 PRO B CB  1 
ATOM   5695 C  CG  . PRO B 1 243 ? -18.760 -27.921 1.628   1.00 23.81 ? 243 PRO B CG  1 
ATOM   5696 C  CD  . PRO B 1 243 ? -18.822 -27.217 2.964   1.00 19.81 ? 243 PRO B CD  1 
ATOM   5697 N  N   . GLU B 1 244 ? -21.558 -29.446 4.274   1.00 18.58 ? 244 GLU B N   1 
ATOM   5698 C  CA  . GLU B 1 244 ? -22.268 -30.536 4.983   1.00 20.57 ? 244 GLU B CA  1 
ATOM   5699 C  C   . GLU B 1 244 ? -23.515 -29.964 5.683   1.00 21.61 ? 244 GLU B C   1 
ATOM   5700 O  O   . GLU B 1 244 ? -24.630 -30.356 5.318   1.00 22.17 ? 244 GLU B O   1 
ATOM   5701 C  CB  . GLU B 1 244 ? -21.267 -31.150 5.977   1.00 22.79 ? 244 GLU B CB  1 
ATOM   5702 C  CG  . GLU B 1 244 ? -21.746 -32.332 6.761   1.00 28.17 ? 244 GLU B CG  1 
ATOM   5703 C  CD  . GLU B 1 244 ? -20.643 -32.821 7.709   1.00 33.63 ? 244 GLU B CD  1 
ATOM   5704 O  OE1 . GLU B 1 244 ? -19.442 -32.572 7.441   1.00 35.55 ? 244 GLU B OE1 1 
ATOM   5705 O  OE2 . GLU B 1 244 ? -20.983 -33.390 8.736   1.00 45.63 ? 244 GLU B OE2 1 
ATOM   5706 N  N   . THR B 1 245 ? -23.345 -29.075 6.658   1.00 19.81 ? 245 THR B N   1 
ATOM   5707 C  CA  . THR B 1 245 ? -24.461 -28.471 7.452   1.00 19.97 ? 245 THR B CA  1 
ATOM   5708 C  C   . THR B 1 245 ? -25.149 -27.363 6.643   1.00 20.44 ? 245 THR B C   1 
ATOM   5709 O  O   . THR B 1 245 ? -26.340 -27.090 6.954   1.00 20.99 ? 245 THR B O   1 
ATOM   5710 C  CB  . THR B 1 245 ? -24.006 -27.913 8.802   1.00 19.28 ? 245 THR B CB  1 
ATOM   5711 O  OG1 . THR B 1 245 ? -23.108 -26.830 8.517   1.00 18.11 ? 245 THR B OG1 1 
ATOM   5712 C  CG2 . THR B 1 245 ? -23.351 -28.952 9.700   1.00 19.70 ? 245 THR B CG2 1 
ATOM   5713 N  N   . GLY B 1 246 ? -24.465 -26.762 5.661   1.00 18.79 ? 246 GLY B N   1 
ATOM   5714 C  CA  . GLY B 1 246 ? -24.906 -25.563 4.929   1.00 16.26 ? 246 GLY B CA  1 
ATOM   5715 C  C   . GLY B 1 246 ? -24.830 -24.299 5.763   1.00 16.87 ? 246 GLY B C   1 
ATOM   5716 O  O   . GLY B 1 246 ? -25.300 -23.262 5.338   1.00 17.09 ? 246 GLY B O   1 
ATOM   5717 N  N   . GLU B 1 247 ? -24.211 -24.342 6.948   1.00 16.53 ? 247 GLU B N   1 
ATOM   5718 C  CA  . GLU B 1 247 ? -24.133 -23.194 7.868   1.00 16.58 ? 247 GLU B CA  1 
ATOM   5719 C  C   . GLU B 1 247 ? -22.812 -22.445 7.685   1.00 16.64 ? 247 GLU B C   1 
ATOM   5720 O  O   . GLU B 1 247 ? -21.774 -23.059 7.457   1.00 16.46 ? 247 GLU B O   1 
ATOM   5721 C  CB  . GLU B 1 247 ? -24.222 -23.644 9.312   1.00 17.62 ? 247 GLU B CB  1 
ATOM   5722 C  CG  . GLU B 1 247 ? -25.529 -24.330 9.710   1.00 20.25 ? 247 GLU B CG  1 
ATOM   5723 C  CD  . GLU B 1 247 ? -25.462 -24.958 11.085  1.00 21.94 ? 247 GLU B CD  1 
ATOM   5724 O  OE1 . GLU B 1 247 ? -24.610 -24.528 11.873  1.00 20.93 ? 247 GLU B OE1 1 
ATOM   5725 O  OE2 . GLU B 1 247 ? -26.292 -25.860 11.408  1.00 25.40 ? 247 GLU B OE2 1 
ATOM   5726 N  N   . PRO B 1 248 ? -22.795 -21.126 7.947   1.00 18.82 ? 248 PRO B N   1 
ATOM   5727 C  CA  . PRO B 1 248 ? -21.553 -20.383 8.062   1.00 20.32 ? 248 PRO B CA  1 
ATOM   5728 C  C   . PRO B 1 248 ? -21.054 -20.453 9.495   1.00 20.72 ? 248 PRO B C   1 
ATOM   5729 O  O   . PRO B 1 248 ? -21.767 -20.863 10.352  1.00 19.78 ? 248 PRO B O   1 
ATOM   5730 C  CB  . PRO B 1 248 ? -22.006 -18.966 7.647   1.00 22.45 ? 248 PRO B CB  1 
ATOM   5731 C  CG  . PRO B 1 248 ? -23.388 -18.862 8.249   1.00 23.39 ? 248 PRO B CG  1 
ATOM   5732 C  CD  . PRO B 1 248 ? -23.972 -20.254 8.154   1.00 21.06 ? 248 PRO B CD  1 
ATOM   5733 N  N   . LEU B 1 249 ? -19.821 -19.998 9.726   1.00 17.97 ? 249 LEU B N   1 
ATOM   5734 C  CA  . LEU B 1 249 ? -19.335 -19.793 11.096  1.00 18.10 ? 249 LEU B CA  1 
ATOM   5735 C  C   . LEU B 1 249 ? -20.007 -18.576 11.699  1.00 18.84 ? 249 LEU B C   1 
ATOM   5736 O  O   . LEU B 1 249 ? -20.240 -17.612 10.931  1.00 21.97 ? 249 LEU B O   1 
ATOM   5737 C  CB  . LEU B 1 249 ? -17.829 -19.548 11.085  1.00 18.60 ? 249 LEU B CB  1 
ATOM   5738 C  CG  . LEU B 1 249 ? -17.011 -20.697 10.515  1.00 18.82 ? 249 LEU B CG  1 
ATOM   5739 C  CD1 . LEU B 1 249 ? -15.522 -20.339 10.550  1.00 20.63 ? 249 LEU B CD1 1 
ATOM   5740 C  CD2 . LEU B 1 249 ? -17.293 -21.977 11.258  1.00 19.97 ? 249 LEU B CD2 1 
ATOM   5741 N  N   . ASP B 1 250 ? -20.268 -18.596 12.976  1.00 19.08 ? 250 ASP B N   1 
ATOM   5742 C  CA  . ASP B 1 250 ? -20.746 -17.372 13.659  1.00 20.22 ? 250 ASP B CA  1 
ATOM   5743 C  C   . ASP B 1 250 ? -19.567 -16.488 14.066  1.00 19.82 ? 250 ASP B C   1 
ATOM   5744 O  O   . ASP B 1 250 ? -18.386 -16.940 14.001  1.00 18.39 ? 250 ASP B O   1 
ATOM   5745 C  CB  . ASP B 1 250 ? -21.707 -17.654 14.807  1.00 23.00 ? 250 ASP B CB  1 
ATOM   5746 C  CG  . ASP B 1 250 ? -21.151 -18.403 15.999  1.00 30.51 ? 250 ASP B CG  1 
ATOM   5747 O  OD1 . ASP B 1 250 ? -19.945 -18.412 16.179  1.00 27.99 ? 250 ASP B OD1 1 
ATOM   5748 O  OD2 . ASP B 1 250 ? -21.976 -18.911 16.787  1.00 33.32 ? 250 ASP B OD2 1 
ATOM   5749 N  N   . ASP B 1 251 ? -19.851 -15.237 14.434  1.00 18.80 ? 251 ASP B N   1 
ATOM   5750 C  CA  . ASP B 1 251 ? -18.796 -14.231 14.707  1.00 19.97 ? 251 ASP B CA  1 
ATOM   5751 C  C   . ASP B 1 251 ? -17.902 -14.660 15.879  1.00 18.84 ? 251 ASP B C   1 
ATOM   5752 O  O   . ASP B 1 251 ? -16.692 -14.363 15.799  1.00 19.64 ? 251 ASP B O   1 
ATOM   5753 C  CB  . ASP B 1 251 ? -19.430 -12.862 14.967  1.00 19.84 ? 251 ASP B CB  1 
ATOM   5754 C  CG  . ASP B 1 251 ? -20.009 -12.246 13.715  1.00 22.26 ? 251 ASP B CG  1 
ATOM   5755 O  OD1 . ASP B 1 251 ? -19.839 -12.786 12.627  1.00 25.33 ? 251 ASP B OD1 1 
ATOM   5756 O  OD2 . ASP B 1 251 ? -20.628 -11.166 13.874  1.00 26.81 ? 251 ASP B OD2 1 
ATOM   5757 N  N   . GLU B 1 252 ? -18.442 -15.280 16.918  1.00 19.58 ? 252 GLU B N   1 
ATOM   5758 C  CA  . GLU B 1 252 ? -17.656 -15.752 18.095  1.00 18.54 ? 252 GLU B CA  1 
ATOM   5759 C  C   . GLU B 1 252 ? -16.668 -16.813 17.628  1.00 16.98 ? 252 GLU B C   1 
ATOM   5760 O  O   . GLU B 1 252 ? -15.478 -16.748 17.980  1.00 15.17 ? 252 GLU B O   1 
ATOM   5761 C  CB  . GLU B 1 252 ? -18.530 -16.391 19.179  1.00 19.82 ? 252 GLU B CB  1 
ATOM   5762 C  CG  . GLU B 1 252 ? -17.748 -16.846 20.379  1.00 26.61 ? 252 GLU B CG  1 
ATOM   5763 C  CD  . GLU B 1 252 ? -18.589 -17.403 21.513  1.00 30.55 ? 252 GLU B CD  1 
ATOM   5764 O  OE1 . GLU B 1 252 ? -19.816 -17.202 21.485  1.00 33.81 ? 252 GLU B OE1 1 
ATOM   5765 O  OE2 . GLU B 1 252 ? -18.027 -18.068 22.401  1.00 37.67 ? 252 GLU B OE2 1 
ATOM   5766 N  N   . ASN B 1 253 ? -17.131 -17.745 16.785  1.00 16.48 ? 253 ASN B N   1 
ATOM   5767 C  CA  . ASN B 1 253 ? -16.177 -18.787 16.316  1.00 14.93 ? 253 ASN B CA  1 
ATOM   5768 C  C   . ASN B 1 253 ? -15.133 -18.162 15.389  1.00 15.13 ? 253 ASN B C   1 
ATOM   5769 O  O   . ASN B 1 253 ? -13.930 -18.560 15.426  1.00 13.84 ? 253 ASN B O   1 
ATOM   5770 C  CB  . ASN B 1 253 ? -16.891 -19.966 15.658  1.00 14.77 ? 253 ASN B CB  1 
ATOM   5771 C  CG  . ASN B 1 253 ? -15.928 -21.086 15.270  1.00 14.95 ? 253 ASN B CG  1 
ATOM   5772 O  OD1 . ASN B 1 253 ? -15.517 -21.183 14.111  1.00 15.23 ? 253 ASN B OD1 1 
ATOM   5773 N  ND2 . ASN B 1 253 ? -15.529 -21.868 16.267  1.00 14.85 ? 253 ASN B ND2 1 
ATOM   5774 N  N   . ILE B 1 254 ? -15.519 -17.212 14.519  1.00 14.54 ? 254 ILE B N   1 
ATOM   5775 C  CA  . ILE B 1 254 ? -14.525 -16.521 13.664  1.00 14.64 ? 254 ILE B CA  1 
ATOM   5776 C  C   . ILE B 1 254 ? -13.466 -15.861 14.545  1.00 14.40 ? 254 ILE B C   1 
ATOM   5777 O  O   . ILE B 1 254 ? -12.279 -15.982 14.228  1.00 15.53 ? 254 ILE B O   1 
ATOM   5778 C  CB  . ILE B 1 254 ? -15.201 -15.507 12.731  1.00 15.13 ? 254 ILE B CB  1 
ATOM   5779 C  CG1 . ILE B 1 254 ? -16.077 -16.207 11.719  1.00 16.12 ? 254 ILE B CG1 1 
ATOM   5780 C  CG2 . ILE B 1 254 ? -14.174 -14.662 12.037  1.00 14.73 ? 254 ILE B CG2 1 
ATOM   5781 C  CD1 . ILE B 1 254 ? -17.044 -15.207 11.059  1.00 17.16 ? 254 ILE B CD1 1 
ATOM   5782 N  N   . ARG B 1 255 ? -13.867 -15.242 15.638  1.00 14.71 ? 255 ARG B N   1 
ATOM   5783 C  CA  . ARG B 1 255 ? -12.857 -14.634 16.551  1.00 15.50 ? 255 ARG B CA  1 
ATOM   5784 C  C   . ARG B 1 255 ? -11.885 -15.721 17.046  1.00 13.93 ? 255 ARG B C   1 
ATOM   5785 O  O   . ARG B 1 255 ? -10.657 -15.505 17.049  1.00 13.25 ? 255 ARG B O   1 
ATOM   5786 C  CB  . ARG B 1 255 ? -13.549 -13.986 17.745  1.00 18.63 ? 255 ARG B CB  1 
ATOM   5787 C  CG  . ARG B 1 255 ? -12.612 -13.616 18.891  1.00 19.79 ? 255 ARG B CG  1 
ATOM   5788 C  CD  . ARG B 1 255 ? -13.121 -14.089 20.227  1.00 22.31 ? 255 ARG B CD  1 
ATOM   5789 N  NE  . ARG B 1 255 ? -14.274 -13.295 20.605  1.00 22.54 ? 255 ARG B NE  1 
ATOM   5790 C  CZ  . ARG B 1 255 ? -15.056 -13.571 21.631  1.00 24.87 ? 255 ARG B CZ  1 
ATOM   5791 N  NH1 . ARG B 1 255 ? -14.812 -14.630 22.391  1.00 24.16 ? 255 ARG B NH1 1 
ATOM   5792 N  NH2 . ARG B 1 255 ? -16.064 -12.763 21.922  1.00 27.44 ? 255 ARG B NH2 1 
ATOM   5793 N  N   . TYR B 1 256 ? -12.403 -16.870 17.454  1.00 13.88 ? 256 TYR B N   1 
ATOM   5794 C  CA  . TYR B 1 256 ? -11.524 -17.947 17.964  1.00 13.87 ? 256 TYR B CA  1 
ATOM   5795 C  C   . TYR B 1 256 ? -10.573 -18.419 16.868  1.00 12.19 ? 256 TYR B C   1 
ATOM   5796 O  O   . TYR B 1 256 ? -9.391  -18.685 17.159  1.00 11.88 ? 256 TYR B O   1 
ATOM   5797 C  CB  . TYR B 1 256 ? -12.326 -19.100 18.506  1.00 14.47 ? 256 TYR B CB  1 
ATOM   5798 C  CG  . TYR B 1 256 ? -13.099 -18.804 19.761  1.00 16.66 ? 256 TYR B CG  1 
ATOM   5799 C  CD1 . TYR B 1 256 ? -12.526 -18.077 20.770  1.00 18.02 ? 256 TYR B CD1 1 
ATOM   5800 C  CD2 . TYR B 1 256 ? -14.388 -19.279 19.901  1.00 18.31 ? 256 TYR B CD2 1 
ATOM   5801 C  CE1 . TYR B 1 256 ? -13.238 -17.820 21.946  1.00 21.95 ? 256 TYR B CE1 1 
ATOM   5802 C  CE2 . TYR B 1 256 ? -15.116 -19.034 21.040  1.00 21.22 ? 256 TYR B CE2 1 
ATOM   5803 C  CZ  . TYR B 1 256 ? -14.541 -18.294 22.036  1.00 21.83 ? 256 TYR B CZ  1 
ATOM   5804 O  OH  . TYR B 1 256 ? -15.341 -18.116 23.139  1.00 34.24 ? 256 TYR B OH  1 
ATOM   5805 N  N   . GLN B 1 257 ? -11.009 -18.496 15.606  1.00 11.39 ? 257 GLN B N   1 
ATOM   5806 C  CA  . GLN B 1 257 ? -10.139 -18.907 14.490  1.00 11.76 ? 257 GLN B CA  1 
ATOM   5807 C  C   . GLN B 1 257 ? -9.036  -17.877 14.312  1.00 11.38 ? 257 GLN B C   1 
ATOM   5808 O  O   . GLN B 1 257 ? -7.889  -18.240 14.121  1.00 11.68 ? 257 GLN B O   1 
ATOM   5809 C  CB  . GLN B 1 257 ? -10.865 -19.089 13.145  1.00 11.92 ? 257 GLN B CB  1 
ATOM   5810 C  CG  . GLN B 1 257 ? -12.052 -20.063 13.218  1.00 11.15 ? 257 GLN B CG  1 
ATOM   5811 C  CD  . GLN B 1 257 ? -11.722 -21.451 13.726  1.00 11.66 ? 257 GLN B CD  1 
ATOM   5812 O  OE1 . GLN B 1 257 ? -10.560 -21.843 13.853  1.00 12.39 ? 257 GLN B OE1 1 
ATOM   5813 N  NE2 . GLN B 1 257 ? -12.789 -22.215 13.930  1.00 12.52 ? 257 GLN B NE2 1 
ATOM   5814 N  N   . ILE B 1 258 ? -9.389  -16.594 14.370  1.00 12.78 ? 258 ILE B N   1 
ATOM   5815 C  CA  . ILE B 1 258 ? -8.340  -15.546 14.202  1.00 13.86 ? 258 ILE B CA  1 
ATOM   5816 C  C   . ILE B 1 258 ? -7.359  -15.604 15.361  1.00 12.60 ? 258 ILE B C   1 
ATOM   5817 O  O   . ILE B 1 258 ? -6.135  -15.579 15.079  1.00 12.35 ? 258 ILE B O   1 
ATOM   5818 C  CB  . ILE B 1 258 ? -8.981  -14.164 14.066  1.00 15.21 ? 258 ILE B CB  1 
ATOM   5819 C  CG1 . ILE B 1 258 ? -9.763  -14.063 12.748  1.00 16.86 ? 258 ILE B CG1 1 
ATOM   5820 C  CG2 . ILE B 1 258 ? -7.923  -13.070 14.186  1.00 15.38 ? 258 ILE B CG2 1 
ATOM   5821 C  CD1 . ILE B 1 258 ? -10.615 -12.830 12.651  1.00 21.59 ? 258 ILE B CD1 1 
ATOM   5822 N  N   . ILE B 1 259 ? -7.840  -15.731 16.604  1.00 13.31 ? 259 ILE B N   1 
ATOM   5823 C  CA  . ILE B 1 259 ? -6.892  -15.864 17.745  1.00 13.92 ? 259 ILE B CA  1 
ATOM   5824 C  C   . ILE B 1 259 ? -5.945  -17.044 17.479  1.00 11.60 ? 259 ILE B C   1 
ATOM   5825 O  O   . ILE B 1 259 ? -4.693  -16.949 17.682  1.00 11.50 ? 259 ILE B O   1 
ATOM   5826 C  CB  . ILE B 1 259 ? -7.661  -15.950 19.056  1.00 14.58 ? 259 ILE B CB  1 
ATOM   5827 C  CG1 . ILE B 1 259 ? -8.298  -14.597 19.380  1.00 15.76 ? 259 ILE B CG1 1 
ATOM   5828 C  CG2 . ILE B 1 259 ? -6.752  -16.430 20.158  1.00 15.87 ? 259 ILE B CG2 1 
ATOM   5829 C  CD1 . ILE B 1 259 ? -9.294  -14.621 20.518  1.00 16.98 ? 259 ILE B CD1 1 
ATOM   5830 N  N   . THR B 1 260 ? -6.536  -18.136 17.034  1.00 11.76 ? 260 THR B N   1 
ATOM   5831 C  CA  . THR B 1 260 ? -5.778  -19.389 16.783  1.00 12.20 ? 260 THR B CA  1 
ATOM   5832 C  C   . THR B 1 260 ? -4.660  -19.115 15.741  1.00 12.26 ? 260 THR B C   1 
ATOM   5833 O  O   . THR B 1 260 ? -3.510  -19.560 15.870  1.00 13.06 ? 260 THR B O   1 
ATOM   5834 C  CB  . THR B 1 260 ? -6.719  -20.507 16.351  1.00 12.60 ? 260 THR B CB  1 
ATOM   5835 O  OG1 . THR B 1 260 ? -7.584  -20.734 17.464  1.00 13.70 ? 260 THR B OG1 1 
ATOM   5836 C  CG2 . THR B 1 260 ? -5.977  -21.783 16.018  1.00 13.01 ? 260 THR B CG2 1 
ATOM   5837 N  N   . PHE B 1 261 ? -5.052  -18.493 14.601  1.00 12.39 ? 261 PHE B N   1 
ATOM   5838 C  CA  . PHE B 1 261 ? -4.089  -18.229 13.508  1.00 13.04 ? 261 PHE B CA  1 
ATOM   5839 C  C   . PHE B 1 261 ? -2.964  -17.320 13.979  1.00 11.92 ? 261 PHE B C   1 
ATOM   5840 O  O   . PHE B 1 261 ? -1.823  -17.502 13.542  1.00 12.99 ? 261 PHE B O   1 
ATOM   5841 C  CB  . PHE B 1 261 ? -4.808  -17.636 12.290  1.00 13.89 ? 261 PHE B CB  1 
ATOM   5842 C  CG  . PHE B 1 261 ? -5.840  -18.527 11.642  1.00 16.12 ? 261 PHE B CG  1 
ATOM   5843 C  CD1 . PHE B 1 261 ? -5.684  -19.902 11.591  1.00 19.86 ? 261 PHE B CD1 1 
ATOM   5844 C  CD2 . PHE B 1 261 ? -6.953  -17.963 11.071  1.00 20.96 ? 261 PHE B CD2 1 
ATOM   5845 C  CE1 . PHE B 1 261 ? -6.666  -20.717 11.029  1.00 22.95 ? 261 PHE B CE1 1 
ATOM   5846 C  CE2 . PHE B 1 261 ? -7.909  -18.777 10.472  1.00 19.75 ? 261 PHE B CE2 1 
ATOM   5847 C  CZ  . PHE B 1 261 ? -7.764  -20.139 10.477  1.00 20.01 ? 261 PHE B CZ  1 
ATOM   5848 N  N   . LEU B 1 262 ? -3.281  -16.353 14.861  1.00 12.16 ? 262 LEU B N   1 
ATOM   5849 C  CA  . LEU B 1 262 ? -2.224  -15.432 15.362  1.00 14.04 ? 262 LEU B CA  1 
ATOM   5850 C  C   . LEU B 1 262 ? -1.288  -16.157 16.316  1.00 13.51 ? 262 LEU B C   1 
ATOM   5851 O  O   . LEU B 1 262 ? -0.040  -15.914 16.266  1.00 15.42 ? 262 LEU B O   1 
ATOM   5852 C  CB  . LEU B 1 262 ? -2.892  -14.230 16.041  1.00 14.90 ? 262 LEU B CB  1 
ATOM   5853 C  CG  . LEU B 1 262 ? -3.659  -13.305 15.092  1.00 15.38 ? 262 LEU B CG  1 
ATOM   5854 C  CD1 . LEU B 1 262 ? -4.458  -12.292 15.894  1.00 16.69 ? 262 LEU B CD1 1 
ATOM   5855 C  CD2 . LEU B 1 262 ? -2.727  -12.605 14.118  1.00 18.25 ? 262 LEU B CD2 1 
ATOM   5856 N  N   . ILE B 1 263 ? -1.797  -17.073 17.105  1.00 12.74 ? 263 ILE B N   1 
ATOM   5857 C  CA  . ILE B 1 263 ? -0.944  -17.943 17.958  1.00 13.51 ? 263 ILE B CA  1 
ATOM   5858 C  C   . ILE B 1 263 ? 0.013   -18.686 17.040  1.00 12.99 ? 263 ILE B C   1 
ATOM   5859 O  O   . ILE B 1 263 ? 1.253   -18.682 17.286  1.00 12.89 ? 263 ILE B O   1 
ATOM   5860 C  CB  . ILE B 1 263 ? -1.778  -18.899 18.813  1.00 14.17 ? 263 ILE B CB  1 
ATOM   5861 C  CG1 . ILE B 1 263 ? -2.553  -18.154 19.899  1.00 14.71 ? 263 ILE B CG1 1 
ATOM   5862 C  CG2 . ILE B 1 263 ? -0.864  -19.975 19.384  1.00 16.24 ? 263 ILE B CG2 1 
ATOM   5863 C  CD1 . ILE B 1 263 ? -3.701  -18.948 20.464  1.00 16.84 ? 263 ILE B CD1 1 
ATOM   5864 N  N   . ALA B 1 264 ? -0.523  -19.306 15.990  1.00 14.05 ? 264 ALA B N   1 
ATOM   5865 C  CA  . ALA B 1 264 ? 0.318   -20.141 15.117  1.00 15.23 ? 264 ALA B CA  1 
ATOM   5866 C  C   . ALA B 1 264 ? 1.384   -19.284 14.476  1.00 17.25 ? 264 ALA B C   1 
ATOM   5867 O  O   . ALA B 1 264 ? 2.536   -19.704 14.468  1.00 19.65 ? 264 ALA B O   1 
ATOM   5868 C  CB  . ALA B 1 264 ? -0.532  -20.797 14.044  1.00 15.17 ? 264 ALA B CB  1 
ATOM   5869 N  N   . GLY B 1 265 ? 0.969   -18.159 13.889  1.00 16.63 ? 265 GLY B N   1 
ATOM   5870 C  CA  . GLY B 1 265 ? 1.926   -17.374 13.091  1.00 20.04 ? 265 GLY B CA  1 
ATOM   5871 C  C   . GLY B 1 265 ? 3.029   -16.844 13.982  1.00 21.14 ? 265 GLY B C   1 
ATOM   5872 O  O   . GLY B 1 265 ? 4.169   -16.786 13.510  1.00 25.06 ? 265 GLY B O   1 
ATOM   5873 N  N   . HIS B 1 266 ? 2.716   -16.422 15.204  1.00 16.52 ? 266 HIS B N   1 
ATOM   5874 C  CA  . HIS B 1 266 ? 3.726   -15.925 16.170  1.00 17.04 ? 266 HIS B CA  1 
ATOM   5875 C  C   . HIS B 1 266 ? 4.688   -17.044 16.597  1.00 16.25 ? 266 HIS B C   1 
ATOM   5876 O  O   . HIS B 1 266 ? 5.871   -16.806 16.745  1.00 17.15 ? 266 HIS B O   1 
ATOM   5877 C  CB  . HIS B 1 266 ? 3.050   -15.325 17.390  1.00 16.62 ? 266 HIS B CB  1 
ATOM   5878 C  CG  . HIS B 1 266 ? 3.944   -14.637 18.349  1.00 16.68 ? 266 HIS B CG  1 
ATOM   5879 N  ND1 . HIS B 1 266 ? 4.539   -15.288 19.398  1.00 19.39 ? 266 HIS B ND1 1 
ATOM   5880 C  CD2 . HIS B 1 266 ? 4.278   -13.330 18.467  1.00 16.41 ? 266 HIS B CD2 1 
ATOM   5881 C  CE1 . HIS B 1 266 ? 5.245   -14.410 20.100  1.00 17.98 ? 266 HIS B CE1 1 
ATOM   5882 N  NE2 . HIS B 1 266 ? 5.065   -13.221 19.570  1.00 18.16 ? 266 HIS B NE2 1 
ATOM   5883 N  N   . GLU B 1 267 ? 4.167   -18.223 16.894  1.00 15.46 ? 267 GLU B N   1 
ATOM   5884 C  CA  . GLU B 1 267 ? 4.914   -19.273 17.606  1.00 16.02 ? 267 GLU B CA  1 
ATOM   5885 C  C   . GLU B 1 267 ? 5.614   -20.267 16.699  1.00 16.08 ? 267 GLU B C   1 
ATOM   5886 O  O   . GLU B 1 267 ? 6.706   -20.745 17.105  1.00 17.21 ? 267 GLU B O   1 
ATOM   5887 C  CB  . GLU B 1 267 ? 3.923   -20.017 18.491  1.00 17.60 ? 267 GLU B CB  1 
ATOM   5888 C  CG  . GLU B 1 267 ? 3.436   -19.204 19.675  1.00 18.74 ? 267 GLU B CG  1 
ATOM   5889 C  CD  . GLU B 1 267 ? 4.489   -18.856 20.718  1.00 21.78 ? 267 GLU B CD  1 
ATOM   5890 O  OE1 . GLU B 1 267 ? 4.706   -19.671 21.663  1.00 27.06 ? 267 GLU B OE1 1 
ATOM   5891 O  OE2 . GLU B 1 267 ? 5.090   -17.800 20.592  1.00 24.32 ? 267 GLU B OE2 1 
ATOM   5892 N  N   . THR B 1 268 ? 5.062   -20.658 15.550  1.00 16.77 ? 268 THR B N   1 
ATOM   5893 C  CA  . THR B 1 268 ? 5.554   -21.872 14.850  1.00 16.29 ? 268 THR B CA  1 
ATOM   5894 C  C   . THR B 1 268 ? 6.514   -21.568 13.706  1.00 15.30 ? 268 THR B C   1 
ATOM   5895 O  O   . THR B 1 268 ? 7.677   -22.005 13.755  1.00 14.46 ? 268 THR B O   1 
ATOM   5896 C  CB  . THR B 1 268 ? 4.356   -22.690 14.358  1.00 18.67 ? 268 THR B CB  1 
ATOM   5897 O  OG1 . THR B 1 268 ? 3.617   -21.957 13.379  1.00 22.23 ? 268 THR B OG1 1 
ATOM   5898 C  CG2 . THR B 1 268 ? 3.472   -23.059 15.521  1.00 22.73 ? 268 THR B CG2 1 
ATOM   5899 N  N   . THR B 1 269 ? 6.061   -20.889 12.659  1.00 13.40 ? 269 THR B N   1 
ATOM   5900 C  CA  . THR B 1 269 ? 6.883   -20.711 11.447  1.00 14.28 ? 269 THR B CA  1 
ATOM   5901 C  C   . THR B 1 269 ? 8.177   -19.995 11.856  1.00 12.71 ? 269 THR B C   1 
ATOM   5902 O  O   . THR B 1 269 ? 9.225   -20.209 11.244  1.00 14.32 ? 269 THR B O   1 
ATOM   5903 C  CB  . THR B 1 269 ? 6.152   -19.989 10.303  1.00 14.01 ? 269 THR B CB  1 
ATOM   5904 O  OG1 . THR B 1 269 ? 4.878   -20.647 10.218  1.00 16.45 ? 269 THR B OG1 1 
ATOM   5905 C  CG2 . THR B 1 269 ? 6.887   -20.004 8.974   1.00 14.36 ? 269 THR B CG2 1 
ATOM   5906 N  N   . SER B 1 270 ? 8.066   -19.062 12.819  1.00 13.01 ? 270 SER B N   1 
ATOM   5907 C  CA  . SER B 1 270 ? 9.266   -18.296 13.245  1.00 12.51 ? 270 SER B CA  1 
ATOM   5908 C  C   . SER B 1 270 ? 10.312  -19.246 13.841  1.00 11.66 ? 270 SER B C   1 
ATOM   5909 O  O   . SER B 1 270 ? 11.496  -19.016 13.704  1.00 12.60 ? 270 SER B O   1 
ATOM   5910 C  CB  . SER B 1 270 ? 8.910   -17.234 14.230  1.00 13.33 ? 270 SER B CB  1 
ATOM   5911 O  OG  . SER B 1 270 ? 8.060   -17.753 15.232  1.00 16.29 ? 270 SER B OG  1 
ATOM   5912 N  N   . GLY B 1 271 ? 9.868   -20.219 14.625  1.00 11.39 ? 271 GLY B N   1 
ATOM   5913 C  CA  . GLY B 1 271 ? 10.822  -21.218 15.136  1.00 11.87 ? 271 GLY B CA  1 
ATOM   5914 C  C   . GLY B 1 271 ? 11.466  -21.992 14.022  1.00 11.36 ? 271 GLY B C   1 
ATOM   5915 O  O   . GLY B 1 271 ? 12.702  -22.216 14.072  1.00 11.52 ? 271 GLY B O   1 
ATOM   5916 N  N   . LEU B 1 272 ? 10.680  -22.434 13.032  1.00 10.85 ? 272 LEU B N   1 
ATOM   5917 C  CA  . LEU B 1 272 ? 11.253  -23.184 11.890  1.00 11.25 ? 272 LEU B CA  1 
ATOM   5918 C  C   . LEU B 1 272 ? 12.345  -22.359 11.209  1.00 11.43 ? 272 LEU B C   1 
ATOM   5919 O  O   . LEU B 1 272 ? 13.428  -22.880 10.951  1.00 11.89 ? 272 LEU B O   1 
ATOM   5920 C  CB  . LEU B 1 272 ? 10.117  -23.509 10.933  1.00 12.04 ? 272 LEU B CB  1 
ATOM   5921 C  CG  . LEU B 1 272 ? 10.565  -24.069 9.599   1.00 12.46 ? 272 LEU B CG  1 
ATOM   5922 C  CD1 . LEU B 1 272 ? 11.491  -25.279 9.671   1.00 13.95 ? 272 LEU B CD1 1 
ATOM   5923 C  CD2 . LEU B 1 272 ? 9.358   -24.356 8.743   1.00 13.85 ? 272 LEU B CD2 1 
ATOM   5924 N  N   . LEU B 1 273 ? 12.034  -21.110 10.884  1.00 11.76 ? 273 LEU B N   1 
ATOM   5925 C  CA  . LEU B 1 273 ? 13.009  -20.289 10.146  1.00 12.00 ? 273 LEU B CA  1 
ATOM   5926 C  C   . LEU B 1 273 ? 14.247  -20.134 11.035  1.00 11.84 ? 273 LEU B C   1 
ATOM   5927 O  O   . LEU B 1 273 ? 15.349  -20.135 10.501  1.00 12.36 ? 273 LEU B O   1 
ATOM   5928 C  CB  . LEU B 1 273 ? 12.364  -18.956 9.815   1.00 10.65 ? 273 LEU B CB  1 
ATOM   5929 C  CG  . LEU B 1 273 ? 11.508  -18.988 8.555   1.00 12.04 ? 273 LEU B CG  1 
ATOM   5930 C  CD1 . LEU B 1 273 ? 10.553  -17.788 8.570   1.00 12.29 ? 273 LEU B CD1 1 
ATOM   5931 C  CD2 . LEU B 1 273 ? 12.397  -19.070 7.351   1.00 13.06 ? 273 LEU B CD2 1 
ATOM   5932 N  N   . SER B 1 274 ? 14.080  -19.925 12.351  1.00 10.68 ? 274 SER B N   1 
ATOM   5933 C  CA  . SER B 1 274 ? 15.243  -19.709 13.223  1.00 11.68 ? 274 SER B CA  1 
ATOM   5934 C  C   . SER B 1 274 ? 16.125  -20.962 13.249  1.00 11.66 ? 274 SER B C   1 
ATOM   5935 O  O   . SER B 1 274 ? 17.335  -20.860 13.178  1.00 11.28 ? 274 SER B O   1 
ATOM   5936 C  CB  . SER B 1 274 ? 14.780  -19.306 14.579  1.00 12.23 ? 274 SER B CB  1 
ATOM   5937 O  OG  . SER B 1 274 ? 14.007  -18.092 14.571  1.00 12.29 ? 274 SER B OG  1 
ATOM   5938 N  N   . PHE B 1 275 ? 15.510  -22.136 13.411  1.00 10.89 ? 275 PHE B N   1 
ATOM   5939 C  CA  . PHE B 1 275 ? 16.273  -23.415 13.414  1.00 11.65 ? 275 PHE B CA  1 
ATOM   5940 C  C   . PHE B 1 275 ? 16.938  -23.655 12.061  1.00 11.45 ? 275 PHE B C   1 
ATOM   5941 O  O   . PHE B 1 275 ? 18.071  -24.130 12.001  1.00 12.13 ? 275 PHE B O   1 
ATOM   5942 C  CB  . PHE B 1 275 ? 15.436  -24.635 13.824  1.00 11.35 ? 275 PHE B CB  1 
ATOM   5943 C  CG  . PHE B 1 275 ? 15.211  -24.725 15.300  1.00 12.22 ? 275 PHE B CG  1 
ATOM   5944 C  CD1 . PHE B 1 275 ? 16.241  -25.038 16.163  1.00 12.82 ? 275 PHE B CD1 1 
ATOM   5945 C  CD2 . PHE B 1 275 ? 13.933  -24.611 15.811  1.00 13.93 ? 275 PHE B CD2 1 
ATOM   5946 C  CE1 . PHE B 1 275 ? 16.021  -25.155 17.532  1.00 14.94 ? 275 PHE B CE1 1 
ATOM   5947 C  CE2 . PHE B 1 275 ? 13.710  -24.715 17.179  1.00 14.44 ? 275 PHE B CE2 1 
ATOM   5948 C  CZ  . PHE B 1 275 ? 14.753  -25.014 18.036  1.00 15.50 ? 275 PHE B CZ  1 
ATOM   5949 N  N   . ALA B 1 276 ? 16.241  -23.356 10.969  1.00 11.39 ? 276 ALA B N   1 
ATOM   5950 C  CA  . ALA B 1 276 ? 16.805  -23.549 9.631   1.00 10.95 ? 276 ALA B CA  1 
ATOM   5951 C  C   . ALA B 1 276 ? 18.079  -22.694 9.471   1.00 11.01 ? 276 ALA B C   1 
ATOM   5952 O  O   . ALA B 1 276 ? 19.112  -23.191 9.009   1.00 11.40 ? 276 ALA B O   1 
ATOM   5953 C  CB  . ALA B 1 276 ? 15.778  -23.258 8.568   1.00 12.55 ? 276 ALA B CB  1 
ATOM   5954 N  N   . LEU B 1 277 ? 17.986  -21.412 9.799   1.00 11.05 ? 277 LEU B N   1 
ATOM   5955 C  CA  . LEU B 1 277 ? 19.195  -20.547 9.727   1.00 12.37 ? 277 LEU B CA  1 
ATOM   5956 C  C   . LEU B 1 277 ? 20.294  -21.013 10.698  1.00 12.34 ? 277 LEU B C   1 
ATOM   5957 O  O   . LEU B 1 277 ? 21.473  -21.011 10.279  1.00 12.69 ? 277 LEU B O   1 
ATOM   5958 C  CB  . LEU B 1 277 ? 18.813  -19.094 9.987   1.00 13.34 ? 277 LEU B CB  1 
ATOM   5959 C  CG  . LEU B 1 277 ? 19.960  -18.095 9.759   1.00 15.97 ? 277 LEU B CG  1 
ATOM   5960 C  CD1 . LEU B 1 277 ? 20.432  -18.074 8.307   1.00 18.14 ? 277 LEU B CD1 1 
ATOM   5961 C  CD2 . LEU B 1 277 ? 19.510  -16.720 10.202  1.00 17.18 ? 277 LEU B CD2 1 
ATOM   5962 N  N   . TYR B 1 278 ? 19.937  -21.501 11.878  1.00 11.62 ? 278 TYR B N   1 
ATOM   5963 C  CA  . TYR B 1 278 ? 20.936  -22.107 12.801  1.00 11.80 ? 278 TYR B CA  1 
ATOM   5964 C  C   . TYR B 1 278 ? 21.686  -23.230 12.108  1.00 11.29 ? 278 TYR B C   1 
ATOM   5965 O  O   . TYR B 1 278 ? 22.923  -23.274 12.070  1.00 12.14 ? 278 TYR B O   1 
ATOM   5966 C  CB  . TYR B 1 278 ? 20.242  -22.571 14.087  1.00 13.17 ? 278 TYR B CB  1 
ATOM   5967 C  CG  . TYR B 1 278 ? 21.121  -23.440 14.955  1.00 13.36 ? 278 TYR B CG  1 
ATOM   5968 C  CD1 . TYR B 1 278 ? 22.059  -22.853 15.794  1.00 13.97 ? 278 TYR B CD1 1 
ATOM   5969 C  CD2 . TYR B 1 278 ? 21.083  -24.803 14.863  1.00 15.02 ? 278 TYR B CD2 1 
ATOM   5970 C  CE1 . TYR B 1 278 ? 22.911  -23.633 16.572  1.00 15.27 ? 278 TYR B CE1 1 
ATOM   5971 C  CE2 . TYR B 1 278 ? 21.958  -25.597 15.586  1.00 15.90 ? 278 TYR B CE2 1 
ATOM   5972 C  CZ  . TYR B 1 278 ? 22.859  -25.014 16.454  1.00 15.19 ? 278 TYR B CZ  1 
ATOM   5973 O  OH  . TYR B 1 278 ? 23.683  -25.852 17.169  1.00 16.93 ? 278 TYR B OH  1 
ATOM   5974 N  N   . PHE B 1 279 ? 20.938  -24.177 11.537  1.00 11.00 ? 279 PHE B N   1 
ATOM   5975 C  CA  . PHE B 1 279 ? 21.580  -25.360 10.933  1.00 12.35 ? 279 PHE B CA  1 
ATOM   5976 C  C   . PHE B 1 279 ? 22.388  -24.955 9.702   1.00 12.99 ? 279 PHE B C   1 
ATOM   5977 O  O   . PHE B 1 279 ? 23.475  -25.542 9.420   1.00 13.71 ? 279 PHE B O   1 
ATOM   5978 C  CB  . PHE B 1 279 ? 20.560  -26.454 10.601  1.00 12.56 ? 279 PHE B CB  1 
ATOM   5979 C  CG  . PHE B 1 279 ? 20.147  -27.256 11.781  1.00 12.91 ? 279 PHE B CG  1 
ATOM   5980 C  CD1 . PHE B 1 279 ? 21.093  -27.991 12.471  1.00 13.59 ? 279 PHE B CD1 1 
ATOM   5981 C  CD2 . PHE B 1 279 ? 18.824  -27.251 12.202  1.00 13.40 ? 279 PHE B CD2 1 
ATOM   5982 C  CE1 . PHE B 1 279 ? 20.715  -28.730 13.576  1.00 14.04 ? 279 PHE B CE1 1 
ATOM   5983 C  CE2 . PHE B 1 279 ? 18.452  -27.987 13.331  1.00 13.77 ? 279 PHE B CE2 1 
ATOM   5984 C  CZ  . PHE B 1 279 ? 19.404  -28.706 14.006  1.00 15.29 ? 279 PHE B CZ  1 
ATOM   5985 N  N   . LEU B 1 280 ? 21.923  -23.963 8.934   1.00 12.53 ? 280 LEU B N   1 
ATOM   5986 C  CA  . LEU B 1 280 ? 22.686  -23.465 7.773   1.00 13.39 ? 280 LEU B CA  1 
ATOM   5987 C  C   . LEU B 1 280 ? 24.029  -22.860 8.210   1.00 14.37 ? 280 LEU B C   1 
ATOM   5988 O  O   . LEU B 1 280 ? 25.035  -23.197 7.626   1.00 13.74 ? 280 LEU B O   1 
ATOM   5989 C  CB  . LEU B 1 280 ? 21.827  -22.464 7.009   1.00 14.63 ? 280 LEU B CB  1 
ATOM   5990 C  CG  . LEU B 1 280 ? 20.718  -23.116 6.144   1.00 16.16 ? 280 LEU B CG  1 
ATOM   5991 C  CD1 . LEU B 1 280 ? 19.832  -22.057 5.541   1.00 17.48 ? 280 LEU B CD1 1 
ATOM   5992 C  CD2 . LEU B 1 280 ? 21.301  -24.003 5.058   1.00 18.50 ? 280 LEU B CD2 1 
ATOM   5993 N  N   . VAL B 1 281 ? 24.050  -22.018 9.227   1.00 13.47 ? 281 VAL B N   1 
ATOM   5994 C  CA  . VAL B 1 281 ? 25.348  -21.373 9.596   1.00 13.85 ? 281 VAL B CA  1 
ATOM   5995 C  C   . VAL B 1 281 ? 26.272  -22.405 10.245  1.00 14.17 ? 281 VAL B C   1 
ATOM   5996 O  O   . VAL B 1 281 ? 27.493  -22.227 10.209  1.00 16.78 ? 281 VAL B O   1 
ATOM   5997 C  CB  . VAL B 1 281 ? 25.240  -20.105 10.444  1.00 15.02 ? 281 VAL B CB  1 
ATOM   5998 C  CG1 . VAL B 1 281 ? 24.442  -19.059 9.717   1.00 16.41 ? 281 VAL B CG1 1 
ATOM   5999 C  CG2 . VAL B 1 281 ? 24.701  -20.356 11.821  1.00 13.57 ? 281 VAL B CG2 1 
ATOM   6000 N  N   . LYS B 1 282 ? 25.737  -23.466 10.819  1.00 13.49 ? 282 LYS B N   1 
ATOM   6001 C  CA  . LYS B 1 282 ? 26.575  -24.549 11.409  1.00 13.98 ? 282 LYS B CA  1 
ATOM   6002 C  C   . LYS B 1 282 ? 27.029  -25.566 10.373  1.00 15.10 ? 282 LYS B C   1 
ATOM   6003 O  O   . LYS B 1 282 ? 27.896  -26.405 10.703  1.00 16.85 ? 282 LYS B O   1 
ATOM   6004 C  CB  . LYS B 1 282 ? 25.810  -25.278 12.517  1.00 13.94 ? 282 LYS B CB  1 
ATOM   6005 C  CG  . LYS B 1 282 ? 25.493  -24.390 13.701  1.00 14.09 ? 282 LYS B CG  1 
ATOM   6006 C  CD  . LYS B 1 282 ? 26.711  -23.838 14.422  1.00 14.53 ? 282 LYS B CD  1 
ATOM   6007 C  CE  . LYS B 1 282 ? 26.331  -23.153 15.700  1.00 14.13 ? 282 LYS B CE  1 
ATOM   6008 N  NZ  . LYS B 1 282 ? 27.545  -22.585 16.366  1.00 15.74 ? 282 LYS B NZ  1 
ATOM   6009 N  N   . ASN B 1 283 ? 26.484  -25.519 9.155   1.00 14.04 ? 283 ASN B N   1 
ATOM   6010 C  CA  . ASN B 1 283 ? 26.771  -26.490 8.090   1.00 13.93 ? 283 ASN B CA  1 
ATOM   6011 C  C   . ASN B 1 283 ? 27.032  -25.748 6.789   1.00 14.23 ? 283 ASN B C   1 
ATOM   6012 O  O   . ASN B 1 283 ? 26.202  -25.730 5.883   1.00 15.17 ? 283 ASN B O   1 
ATOM   6013 C  CB  . ASN B 1 283 ? 25.617  -27.490 7.956   1.00 14.58 ? 283 ASN B CB  1 
ATOM   6014 C  CG  . ASN B 1 283 ? 25.496  -28.350 9.186   1.00 15.33 ? 283 ASN B CG  1 
ATOM   6015 O  OD1 . ASN B 1 283 ? 26.144  -29.407 9.258   1.00 18.46 ? 283 ASN B OD1 1 
ATOM   6016 N  ND2 . ASN B 1 283 ? 24.658  -27.931 10.126  1.00 15.22 ? 283 ASN B ND2 1 
ATOM   6017 N  N   . PRO B 1 284 ? 28.179  -25.060 6.661   1.00 14.94 ? 284 PRO B N   1 
ATOM   6018 C  CA  . PRO B 1 284 ? 28.444  -24.198 5.516   1.00 15.87 ? 284 PRO B CA  1 
ATOM   6019 C  C   . PRO B 1 284 ? 28.355  -24.839 4.139   1.00 14.79 ? 284 PRO B C   1 
ATOM   6020 O  O   . PRO B 1 284 ? 28.000  -24.105 3.188   1.00 15.78 ? 284 PRO B O   1 
ATOM   6021 C  CB  . PRO B 1 284 ? 29.899  -23.730 5.710   1.00 18.95 ? 284 PRO B CB  1 
ATOM   6022 C  CG  . PRO B 1 284 ? 30.169  -23.945 7.136   1.00 18.26 ? 284 PRO B CG  1 
ATOM   6023 C  CD  . PRO B 1 284 ? 29.251  -25.027 7.660   1.00 17.21 ? 284 PRO B CD  1 
ATOM   6024 N  N   . HIS B 1 285 ? 28.599  -26.147 3.990   1.00 15.50 ? 285 HIS B N   1 
ATOM   6025 C  CA  . HIS B 1 285 ? 28.451  -26.755 2.655   1.00 15.75 ? 285 HIS B CA  1 
ATOM   6026 C  C   . HIS B 1 285 ? 26.961  -26.797 2.272   1.00 15.23 ? 285 HIS B C   1 
ATOM   6027 O  O   . HIS B 1 285 ? 26.611  -26.693 1.074   1.00 16.09 ? 285 HIS B O   1 
ATOM   6028 C  CB  . HIS B 1 285 ? 29.009  -28.168 2.648   1.00 16.36 ? 285 HIS B CB  1 
ATOM   6029 C  CG  . HIS B 1 285 ? 30.507  -28.256 2.773   1.00 19.40 ? 285 HIS B CG  1 
ATOM   6030 N  ND1 . HIS B 1 285 ? 31.349  -27.508 2.007   1.00 20.68 ? 285 HIS B ND1 1 
ATOM   6031 C  CD2 . HIS B 1 285 ? 31.271  -28.990 3.607   1.00 23.21 ? 285 HIS B CD2 1 
ATOM   6032 C  CE1 . HIS B 1 285 ? 32.616  -27.849 2.309   1.00 19.57 ? 285 HIS B CE1 1 
ATOM   6033 N  NE2 . HIS B 1 285 ? 32.561  -28.721 3.303   1.00 19.65 ? 285 HIS B NE2 1 
ATOM   6034 N  N   . VAL B 1 286 ? 26.086  -27.004 3.261   1.00 14.08 ? 286 VAL B N   1 
ATOM   6035 C  CA  . VAL B 1 286 ? 24.619  -26.984 3.034   1.00 14.37 ? 286 VAL B CA  1 
ATOM   6036 C  C   . VAL B 1 286 ? 24.170  -25.553 2.724   1.00 14.13 ? 286 VAL B C   1 
ATOM   6037 O  O   . VAL B 1 286 ? 23.432  -25.338 1.727   1.00 13.91 ? 286 VAL B O   1 
ATOM   6038 C  CB  . VAL B 1 286 ? 23.878  -27.579 4.249   1.00 14.67 ? 286 VAL B CB  1 
ATOM   6039 C  CG1 . VAL B 1 286 ? 22.372  -27.479 4.057   1.00 14.85 ? 286 VAL B CG1 1 
ATOM   6040 C  CG2 . VAL B 1 286 ? 24.265  -29.012 4.523   1.00 15.04 ? 286 VAL B CG2 1 
ATOM   6041 N  N   . LEU B 1 287 ? 24.629  -24.571 3.487   1.00 14.33 ? 287 LEU B N   1 
ATOM   6042 C  CA  . LEU B 1 287 ? 24.368  -23.146 3.141   1.00 14.78 ? 287 LEU B CA  1 
ATOM   6043 C  C   . LEU B 1 287 ? 24.786  -22.817 1.697   1.00 14.42 ? 287 LEU B C   1 
ATOM   6044 O  O   . LEU B 1 287 ? 23.957  -22.277 0.969   1.00 15.31 ? 287 LEU B O   1 
ATOM   6045 C  CB  . LEU B 1 287 ? 25.031  -22.255 4.191   1.00 14.90 ? 287 LEU B CB  1 
ATOM   6046 C  CG  . LEU B 1 287 ? 24.556  -20.818 4.181   1.00 19.62 ? 287 LEU B CG  1 
ATOM   6047 C  CD1 . LEU B 1 287 ? 24.975  -20.129 5.471   1.00 21.25 ? 287 LEU B CD1 1 
ATOM   6048 C  CD2 . LEU B 1 287 ? 25.131  -20.050 3.026   1.00 22.97 ? 287 LEU B CD2 1 
ATOM   6049 N  N   . GLN B 1 288 ? 25.956  -23.229 1.239   1.00 14.21 ? 288 GLN B N   1 
ATOM   6050 C  CA  . GLN B 1 288 ? 26.408  -22.924 -0.132  1.00 15.81 ? 288 GLN B CA  1 
ATOM   6051 C  C   . GLN B 1 288 ? 25.446  -23.574 -1.128  1.00 14.83 ? 288 GLN B C   1 
ATOM   6052 O  O   . GLN B 1 288 ? 25.101  -22.944 -2.110  1.00 14.82 ? 288 GLN B O   1 
ATOM   6053 C  CB  . GLN B 1 288 ? 27.832  -23.428 -0.307  1.00 18.64 ? 288 GLN B CB  1 
ATOM   6054 C  CG  . GLN B 1 288 ? 28.380  -23.077 -1.674  1.00 23.66 ? 288 GLN B CG  1 
ATOM   6055 C  CD  . GLN B 1 288 ? 29.841  -23.429 -1.796  1.00 28.95 ? 288 GLN B CD  1 
ATOM   6056 O  OE1 . GLN B 1 288 ? 30.600  -23.414 -0.825  1.00 37.44 ? 288 GLN B OE1 1 
ATOM   6057 N  NE2 . GLN B 1 288 ? 30.223  -23.752 -3.008  1.00 33.97 ? 288 GLN B NE2 1 
ATOM   6058 N  N   . LYS B 1 289 ? 25.077  -24.824 -0.934  1.00 14.89 ? 289 LYS B N   1 
ATOM   6059 C  CA  . LYS B 1 289 ? 24.198  -25.541 -1.881  1.00 14.75 ? 289 LYS B CA  1 
ATOM   6060 C  C   . LYS B 1 289 ? 22.851  -24.810 -1.942  1.00 14.36 ? 289 LYS B C   1 
ATOM   6061 O  O   . LYS B 1 289 ? 22.291  -24.647 -3.060  1.00 14.98 ? 289 LYS B O   1 
ATOM   6062 C  CB  . LYS B 1 289 ? 24.031  -27.003 -1.461  1.00 16.55 ? 289 LYS B CB  1 
ATOM   6063 C  CG  . LYS B 1 289 ? 23.287  -27.879 -2.469  1.00 21.95 ? 289 LYS B CG  1 
ATOM   6064 C  CD  . LYS B 1 289 ? 23.507  -29.370 -2.212  1.00 26.07 ? 289 LYS B CD  1 
ATOM   6065 C  CE  . LYS B 1 289 ? 22.636  -30.245 -3.094  1.00 30.26 ? 289 LYS B CE  1 
ATOM   6066 N  NZ  . LYS B 1 289 ? 22.815  -31.688 -2.802  1.00 34.48 ? 289 LYS B NZ  1 
ATOM   6067 N  N   . ALA B 1 290 ? 22.281  -24.423 -0.807  1.00 13.69 ? 290 ALA B N   1 
ATOM   6068 C  CA  . ALA B 1 290 ? 20.992  -23.688 -0.779  1.00 14.23 ? 290 ALA B CA  1 
ATOM   6069 C  C   . ALA B 1 290 ? 21.136  -22.292 -1.423  1.00 14.16 ? 290 ALA B C   1 
ATOM   6070 O  O   . ALA B 1 290 ? 20.243  -21.849 -2.185  1.00 13.78 ? 290 ALA B O   1 
ATOM   6071 C  CB  . ALA B 1 290 ? 20.551  -23.621 0.653   1.00 13.25 ? 290 ALA B CB  1 
ATOM   6072 N  N   . ALA B 1 291 ? 22.221  -21.592 -1.142  1.00 12.74 ? 291 ALA B N   1 
ATOM   6073 C  CA  . ALA B 1 291 ? 22.493  -20.267 -1.729  1.00 13.53 ? 291 ALA B CA  1 
ATOM   6074 C  C   . ALA B 1 291 ? 22.631  -20.401 -3.268  1.00 12.93 ? 291 ALA B C   1 
ATOM   6075 O  O   . ALA B 1 291 ? 22.176  -19.482 -3.991  1.00 14.99 ? 291 ALA B O   1 
ATOM   6076 C  CB  . ALA B 1 291 ? 23.724  -19.629 -1.148  1.00 13.54 ? 291 ALA B CB  1 
ATOM   6077 N  N   . GLU B 1 292 ? 23.264  -21.460 -3.780  1.00 14.94 ? 292 GLU B N   1 
ATOM   6078 C  CA  . GLU B 1 292 ? 23.416  -21.635 -5.239  1.00 16.95 ? 292 GLU B CA  1 
ATOM   6079 C  C   . GLU B 1 292 ? 22.024  -21.834 -5.856  1.00 14.94 ? 292 GLU B C   1 
ATOM   6080 O  O   . GLU B 1 292 ? 21.731  -21.275 -6.933  1.00 17.38 ? 292 GLU B O   1 
ATOM   6081 C  CB  . GLU B 1 292 ? 24.374  -22.775 -5.541  1.00 19.06 ? 292 GLU B CB  1 
ATOM   6082 C  CG  . GLU B 1 292 ? 25.809  -22.435 -5.233  1.00 21.21 ? 292 GLU B CG  1 
ATOM   6083 C  CD  . GLU B 1 292 ? 26.753  -23.635 -5.247  1.00 28.70 ? 292 GLU B CD  1 
ATOM   6084 O  OE1 . GLU B 1 292 ? 26.274  -24.787 -5.266  1.00 33.12 ? 292 GLU B OE1 1 
ATOM   6085 O  OE2 . GLU B 1 292 ? 27.982  -23.412 -5.140  1.00 34.99 ? 292 GLU B OE2 1 
ATOM   6086 N  N   . GLU B 1 293 ? 21.143  -22.582 -5.179  1.00 14.65 ? 293 GLU B N   1 
ATOM   6087 C  CA  . GLU B 1 293 ? 19.800  -22.808 -5.718  1.00 13.90 ? 293 GLU B CA  1 
ATOM   6088 C  C   . GLU B 1 293 ? 19.044  -21.466 -5.728  1.00 14.23 ? 293 GLU B C   1 
ATOM   6089 O  O   . GLU B 1 293 ? 18.351  -21.128 -6.711  1.00 15.38 ? 293 GLU B O   1 
ATOM   6090 C  CB  . GLU B 1 293 ? 19.038  -23.787 -4.829  1.00 13.74 ? 293 GLU B CB  1 
ATOM   6091 C  CG  . GLU B 1 293 ? 17.620  -23.969 -5.318  1.00 14.84 ? 293 GLU B CG  1 
ATOM   6092 C  CD  . GLU B 1 293 ? 16.855  -25.018 -4.534  1.00 16.46 ? 293 GLU B CD  1 
ATOM   6093 O  OE1 . GLU B 1 293 ? 16.354  -24.629 -3.497  1.00 17.61 ? 293 GLU B OE1 1 
ATOM   6094 O  OE2 . GLU B 1 293 ? 16.779  -26.212 -4.999  1.00 17.13 ? 293 GLU B OE2 1 
ATOM   6095 N  N   . ALA B 1 294 ? 19.065  -20.746 -4.623  1.00 13.72 ? 294 ALA B N   1 
ATOM   6096 C  CA  . ALA B 1 294 ? 18.403  -19.412 -4.551  1.00 14.73 ? 294 ALA B CA  1 
ATOM   6097 C  C   . ALA B 1 294 ? 18.885  -18.500 -5.702  1.00 15.27 ? 294 ALA B C   1 
ATOM   6098 O  O   . ALA B 1 294 ? 18.028  -17.855 -6.345  1.00 14.67 ? 294 ALA B O   1 
ATOM   6099 C  CB  . ALA B 1 294 ? 18.645  -18.796 -3.204  1.00 14.22 ? 294 ALA B CB  1 
ATOM   6100 N  N   . ALA B 1 295 ? 20.200  -18.455 -5.969  1.00 15.20 ? 295 ALA B N   1 
ATOM   6101 C  CA  . ALA B 1 295 ? 20.741  -17.576 -7.050  1.00 15.66 ? 295 ALA B CA  1 
ATOM   6102 C  C   . ALA B 1 295 ? 20.253  -18.094 -8.395  1.00 16.59 ? 295 ALA B C   1 
ATOM   6103 O  O   . ALA B 1 295 ? 19.919  -17.246 -9.269  1.00 17.75 ? 295 ALA B O   1 
ATOM   6104 C  CB  . ALA B 1 295 ? 22.233  -17.481 -6.976  1.00 16.34 ? 295 ALA B CB  1 
ATOM   6105 N  N   . ARG B 1 296 ? 20.162  -19.410 -8.597  1.00 17.79 ? 296 ARG B N   1 
ATOM   6106 C  CA  . ARG B 1 296 ? 19.803  -19.967 -9.931  1.00 16.23 ? 296 ARG B CA  1 
ATOM   6107 C  C   . ARG B 1 296 ? 18.309  -19.706 -10.197 1.00 16.66 ? 296 ARG B C   1 
ATOM   6108 O  O   . ARG B 1 296 ? 17.897  -19.419 -11.356 1.00 17.76 ? 296 ARG B O   1 
ATOM   6109 C  CB  . ARG B 1 296 ? 20.135  -21.462 -9.959  1.00 20.30 ? 296 ARG B CB  1 
ATOM   6110 C  CG  . ARG B 1 296 ? 19.670  -22.241 -11.178 1.00 25.29 ? 296 ARG B CG  1 
ATOM   6111 C  CD  . ARG B 1 296 ? 20.252  -23.652 -11.134 1.00 28.71 ? 296 ARG B CD  1 
ATOM   6112 N  NE  . ARG B 1 296 ? 19.901  -24.465 -9.945  1.00 33.02 ? 296 ARG B NE  1 
ATOM   6113 C  CZ  . ARG B 1 296 ? 20.733  -24.798 -8.924  1.00 37.56 ? 296 ARG B CZ  1 
ATOM   6114 N  NH1 . ARG B 1 296 ? 21.994  -24.393 -8.872  1.00 40.06 ? 296 ARG B NH1 1 
ATOM   6115 N  NH2 . ARG B 1 296 ? 20.294  -25.543 -7.926  1.00 32.50 ? 296 ARG B NH2 1 
ATOM   6116 N  N   . VAL B 1 297 ? 17.455  -19.869 -9.190  1.00 15.07 ? 297 VAL B N   1 
ATOM   6117 C  CA  . VAL B 1 297 ? 15.993  -19.854 -9.394  1.00 15.66 ? 297 VAL B CA  1 
ATOM   6118 C  C   . VAL B 1 297 ? 15.437  -18.436 -9.295  1.00 16.33 ? 297 VAL B C   1 
ATOM   6119 O  O   . VAL B 1 297 ? 14.505  -18.105 -10.056 1.00 16.69 ? 297 VAL B O   1 
ATOM   6120 C  CB  . VAL B 1 297 ? 15.361  -20.789 -8.356  1.00 16.27 ? 297 VAL B CB  1 
ATOM   6121 C  CG1 . VAL B 1 297 ? 13.852  -20.669 -8.343  1.00 16.57 ? 297 VAL B CG1 1 
ATOM   6122 C  CG2 . VAL B 1 297 ? 15.775  -22.226 -8.613  1.00 17.08 ? 297 VAL B CG2 1 
ATOM   6123 N  N   . LEU B 1 298 ? 15.858  -17.663 -8.278  1.00 16.12 ? 298 LEU B N   1 
ATOM   6124 C  CA  . LEU B 1 298 ? 15.252  -16.325 -7.993  1.00 16.21 ? 298 LEU B CA  1 
ATOM   6125 C  C   . LEU B 1 298 ? 15.879  -15.233 -8.863  1.00 17.25 ? 298 LEU B C   1 
ATOM   6126 O  O   . LEU B 1 298 ? 16.590  -14.376 -8.367  1.00 17.44 ? 298 LEU B O   1 
ATOM   6127 C  CB  . LEU B 1 298 ? 15.390  -16.029 -6.509  1.00 15.67 ? 298 LEU B CB  1 
ATOM   6128 C  CG  . LEU B 1 298 ? 14.695  -17.044 -5.624  1.00 15.39 ? 298 LEU B CG  1 
ATOM   6129 C  CD1 . LEU B 1 298 ? 14.903  -16.705 -4.160  1.00 15.52 ? 298 LEU B CD1 1 
ATOM   6130 C  CD2 . LEU B 1 298 ? 13.220  -17.139 -5.917  1.00 16.01 ? 298 LEU B CD2 1 
ATOM   6131 N  N   . VAL B 1 299 ? 15.522  -15.277 -10.148 1.00 18.11 ? 299 VAL B N   1 
ATOM   6132 C  CA  . VAL B 1 299 ? 16.148  -14.443 -11.225 1.00 19.50 ? 299 VAL B CA  1 
ATOM   6133 C  C   . VAL B 1 299 ? 15.473  -13.083 -11.316 1.00 21.98 ? 299 VAL B C   1 
ATOM   6134 O  O   . VAL B 1 299 ? 15.993  -12.247 -12.109 1.00 22.51 ? 299 VAL B O   1 
ATOM   6135 C  CB  . VAL B 1 299 ? 16.138  -15.173 -12.579 1.00 22.42 ? 299 VAL B CB  1 
ATOM   6136 C  CG1 . VAL B 1 299 ? 17.015  -16.416 -12.507 1.00 22.31 ? 299 VAL B CG1 1 
ATOM   6137 C  CG2 . VAL B 1 299 ? 14.734  -15.531 -13.069 1.00 22.92 ? 299 VAL B CG2 1 
ATOM   6138 N  N   . ASP B 1 300 ? 14.399  -12.841 -10.555 1.00 19.16 ? 300 ASP B N   1 
ATOM   6139 C  CA  . ASP B 1 300 ? 13.580  -11.616 -10.661 1.00 19.28 ? 300 ASP B CA  1 
ATOM   6140 C  C   . ASP B 1 300 ? 13.749  -10.799 -9.398  1.00 20.68 ? 300 ASP B C   1 
ATOM   6141 O  O   . ASP B 1 300 ? 14.153  -11.329 -8.374  1.00 20.09 ? 300 ASP B O   1 
ATOM   6142 C  CB  . ASP B 1 300 ? 12.109  -11.933 -10.942 1.00 18.89 ? 300 ASP B CB  1 
ATOM   6143 C  CG  . ASP B 1 300 ? 11.874  -12.601 -12.298 1.00 22.04 ? 300 ASP B CG  1 
ATOM   6144 O  OD1 . ASP B 1 300 ? 12.490  -12.154 -13.257 1.00 27.99 ? 300 ASP B OD1 1 
ATOM   6145 O  OD2 . ASP B 1 300 ? 11.043  -13.488 -12.360 1.00 27.65 ? 300 ASP B OD2 1 
ATOM   6146 N  N   . PRO B 1 301 ? 13.408  -9.493  -9.427  1.00 20.16 ? 301 PRO B N   1 
ATOM   6147 C  CA  . PRO B 1 301 ? 13.537  -8.646  -8.258  1.00 21.10 ? 301 PRO B CA  1 
ATOM   6148 C  C   . PRO B 1 301 ? 12.752  -9.185  -7.065  1.00 20.21 ? 301 PRO B C   1 
ATOM   6149 O  O   . PRO B 1 301 ? 13.281  -9.134  -5.970  1.00 22.62 ? 301 PRO B O   1 
ATOM   6150 C  CB  . PRO B 1 301 ? 12.923  -7.314  -8.709  1.00 23.60 ? 301 PRO B CB  1 
ATOM   6151 C  CG  . PRO B 1 301 ? 13.139  -7.308  -10.187 1.00 24.23 ? 301 PRO B CG  1 
ATOM   6152 C  CD  . PRO B 1 301 ? 12.961  -8.737  -10.625 1.00 21.72 ? 301 PRO B CD  1 
ATOM   6153 N  N   . VAL B 1 302 ? 11.540  -9.693  -7.261  1.00 19.85 ? 302 VAL B N   1 
ATOM   6154 C  CA  . VAL B 1 302 ? 10.932  -10.489 -6.154  1.00 21.83 ? 302 VAL B CA  1 
ATOM   6155 C  C   . VAL B 1 302 ? 10.503  -11.845 -6.690  1.00 21.95 ? 302 VAL B C   1 
ATOM   6156 O  O   . VAL B 1 302 ? 10.238  -12.014 -7.874  1.00 23.14 ? 302 VAL B O   1 
ATOM   6157 C  CB  . VAL B 1 302 ? 9.776   -9.774  -5.453  1.00 24.51 ? 302 VAL B CB  1 
ATOM   6158 C  CG1 . VAL B 1 302 ? 10.325  -8.536  -4.747  1.00 23.67 ? 302 VAL B CG1 1 
ATOM   6159 C  CG2 . VAL B 1 302 ? 8.617   -9.439  -6.383  1.00 25.41 ? 302 VAL B CG2 1 
ATOM   6160 N  N   . PRO B 1 303 ? 10.407  -12.825 -5.789  1.00 20.56 ? 303 PRO B N   1 
ATOM   6161 C  CA  . PRO B 1 303 ? 10.074  -14.177 -6.190  1.00 18.65 ? 303 PRO B CA  1 
ATOM   6162 C  C   . PRO B 1 303 ? 8.624   -14.297 -6.647  1.00 17.02 ? 303 PRO B C   1 
ATOM   6163 O  O   . PRO B 1 303 ? 7.739   -13.691 -6.022  1.00 17.56 ? 303 PRO B O   1 
ATOM   6164 C  CB  . PRO B 1 303 ? 10.295  -14.995 -4.923  1.00 20.21 ? 303 PRO B CB  1 
ATOM   6165 C  CG  . PRO B 1 303 ? 11.328  -14.191 -4.176  1.00 21.96 ? 303 PRO B CG  1 
ATOM   6166 C  CD  . PRO B 1 303 ? 10.875  -12.768 -4.392  1.00 20.80 ? 303 PRO B CD  1 
ATOM   6167 N  N   . SER B 1 304 ? 8.422   -15.029 -7.728  1.00 15.78 ? 304 SER B N   1 
ATOM   6168 C  CA  . SER B 1 304 ? 7.066   -15.469 -8.104  1.00 15.14 ? 304 SER B CA  1 
ATOM   6169 C  C   . SER B 1 304 ? 6.620   -16.691 -7.275  1.00 15.09 ? 304 SER B C   1 
ATOM   6170 O  O   . SER B 1 304 ? 7.470   -17.406 -6.678  1.00 14.91 ? 304 SER B O   1 
ATOM   6171 C  CB  . SER B 1 304 ? 6.999   -15.825 -9.566  1.00 16.85 ? 304 SER B CB  1 
ATOM   6172 O  OG  . SER B 1 304 ? 7.746   -16.979 -9.803  1.00 17.73 ? 304 SER B OG  1 
ATOM   6173 N  N   . TYR B 1 305 ? 5.333   -16.971 -7.259  1.00 13.79 ? 305 TYR B N   1 
ATOM   6174 C  CA  . TYR B 1 305 ? 4.796   -18.184 -6.632  1.00 14.98 ? 305 TYR B CA  1 
ATOM   6175 C  C   . TYR B 1 305 ? 5.521   -19.404 -7.201  1.00 14.86 ? 305 TYR B C   1 
ATOM   6176 O  O   . TYR B 1 305 ? 5.966   -20.314 -6.461  1.00 15.66 ? 305 TYR B O   1 
ATOM   6177 C  CB  . TYR B 1 305 ? 3.279   -18.208 -6.804  1.00 16.46 ? 305 TYR B CB  1 
ATOM   6178 C  CG  . TYR B 1 305 ? 2.664   -19.500 -6.373  1.00 18.58 ? 305 TYR B CG  1 
ATOM   6179 C  CD1 . TYR B 1 305 ? 2.276   -19.709 -5.072  1.00 19.16 ? 305 TYR B CD1 1 
ATOM   6180 C  CD2 . TYR B 1 305 ? 2.590   -20.545 -7.277  1.00 22.50 ? 305 TYR B CD2 1 
ATOM   6181 C  CE1 . TYR B 1 305 ? 1.762   -20.932 -4.676  1.00 21.87 ? 305 TYR B CE1 1 
ATOM   6182 C  CE2 . TYR B 1 305 ? 2.061   -21.755 -6.900  1.00 24.40 ? 305 TYR B CE2 1 
ATOM   6183 C  CZ  . TYR B 1 305 ? 1.620   -21.937 -5.621  1.00 24.78 ? 305 TYR B CZ  1 
ATOM   6184 O  OH  . TYR B 1 305 ? 1.169   -23.207 -5.344  1.00 31.73 ? 305 TYR B OH  1 
ATOM   6185 N  N   . LYS B 1 306 ? 5.636   -19.506 -8.520  1.00 15.10 ? 306 LYS B N   1 
ATOM   6186 C  CA  . LYS B 1 306 ? 6.209   -20.710 -9.137  1.00 16.69 ? 306 LYS B CA  1 
ATOM   6187 C  C   . LYS B 1 306 ? 7.680   -20.851 -8.751  1.00 15.51 ? 306 LYS B C   1 
ATOM   6188 O  O   . LYS B 1 306 ? 8.145   -21.964 -8.533  1.00 17.82 ? 306 LYS B O   1 
ATOM   6189 C  CB  . LYS B 1 306 ? 6.032   -20.674 -10.651 1.00 18.68 ? 306 LYS B CB  1 
ATOM   6190 C  CG  . LYS B 1 306 ? 6.561   -21.917 -11.345 1.00 23.11 ? 306 LYS B CG  1 
ATOM   6191 C  CD  . LYS B 1 306 ? 5.879   -23.217 -10.860 1.00 24.81 ? 306 LYS B CD  1 
ATOM   6192 C  CE  . LYS B 1 306 ? 6.186   -24.369 -11.800 1.00 29.10 ? 306 LYS B CE  1 
ATOM   6193 N  NZ  . LYS B 1 306 ? 5.688   -25.667 -11.270 1.00 31.76 ? 306 LYS B NZ  1 
ATOM   6194 N  N   . GLN B 1 307 ? 8.386   -19.726 -8.666  1.00 14.40 ? 307 GLN B N   1 
ATOM   6195 C  CA  . GLN B 1 307 ? 9.822   -19.771 -8.304  1.00 15.58 ? 307 GLN B CA  1 
ATOM   6196 C  C   . GLN B 1 307 ? 9.986   -20.378 -6.922  1.00 16.31 ? 307 GLN B C   1 
ATOM   6197 O  O   . GLN B 1 307 ? 10.876  -21.191 -6.754  1.00 15.68 ? 307 GLN B O   1 
ATOM   6198 C  CB  . GLN B 1 307 ? 10.496  -18.412 -8.400  1.00 15.28 ? 307 GLN B CB  1 
ATOM   6199 C  CG  . GLN B 1 307 ? 10.769  -18.039 -9.861  1.00 15.10 ? 307 GLN B CG  1 
ATOM   6200 C  CD  . GLN B 1 307 ? 11.032  -16.576 -10.008 1.00 18.48 ? 307 GLN B CD  1 
ATOM   6201 O  OE1 . GLN B 1 307 ? 10.851  -15.795 -9.085  1.00 16.95 ? 307 GLN B OE1 1 
ATOM   6202 N  NE2 . GLN B 1 307 ? 11.537  -16.169 -11.153 1.00 19.34 ? 307 GLN B NE2 1 
ATOM   6203 N  N   . VAL B 1 308 ? 9.122   -19.989 -5.973  1.00 15.28 ? 308 VAL B N   1 
ATOM   6204 C  CA  . VAL B 1 308 ? 9.194   -20.565 -4.596  1.00 15.07 ? 308 VAL B CA  1 
ATOM   6205 C  C   . VAL B 1 308 ? 8.958   -22.078 -4.681  1.00 15.89 ? 308 VAL B C   1 
ATOM   6206 O  O   . VAL B 1 308 ? 9.689   -22.840 -4.014  1.00 16.14 ? 308 VAL B O   1 
ATOM   6207 C  CB  . VAL B 1 308 ? 8.198   -19.835 -3.682  1.00 14.02 ? 308 VAL B CB  1 
ATOM   6208 C  CG1 . VAL B 1 308 ? 8.106   -20.534 -2.315  1.00 15.05 ? 308 VAL B CG1 1 
ATOM   6209 C  CG2 . VAL B 1 308 ? 8.598   -18.369 -3.513  1.00 15.49 ? 308 VAL B CG2 1 
ATOM   6210 N  N   . LYS B 1 309 ? 8.053   -22.531 -5.556  1.00 15.98 ? 309 LYS B N   1 
ATOM   6211 C  CA  . LYS B 1 309 ? 7.788   -23.993 -5.708  1.00 16.64 ? 309 LYS B CA  1 
ATOM   6212 C  C   . LYS B 1 309 ? 9.019   -24.694 -6.264  1.00 16.17 ? 309 LYS B C   1 
ATOM   6213 O  O   . LYS B 1 309 ? 9.186   -25.900 -6.022  1.00 21.54 ? 309 LYS B O   1 
ATOM   6214 C  CB  . LYS B 1 309 ? 6.589   -24.245 -6.619  1.00 19.37 ? 309 LYS B CB  1 
ATOM   6215 C  CG  . LYS B 1 309 ? 5.265   -23.716 -6.133  1.00 22.67 ? 309 LYS B CG  1 
ATOM   6216 C  CD  . LYS B 1 309 ? 4.895   -24.208 -4.758  1.00 25.63 ? 309 LYS B CD  1 
ATOM   6217 C  CE  . LYS B 1 309 ? 5.070   -23.167 -3.654  1.00 33.42 ? 309 LYS B CE  1 
ATOM   6218 N  NZ  . LYS B 1 309 ? 4.845   -23.676 -2.262  1.00 35.66 ? 309 LYS B NZ  1 
ATOM   6219 N  N   . GLN B 1 310 ? 9.890   -23.983 -6.967  1.00 15.91 ? 310 GLN B N   1 
ATOM   6220 C  CA  . GLN B 1 310 ? 11.094  -24.569 -7.579  1.00 17.35 ? 310 GLN B CA  1 
ATOM   6221 C  C   . GLN B 1 310 ? 12.285  -24.592 -6.634  1.00 16.37 ? 310 GLN B C   1 
ATOM   6222 O  O   . GLN B 1 310 ? 13.335  -25.134 -7.013  1.00 18.78 ? 310 GLN B O   1 
ATOM   6223 C  CB  . GLN B 1 310 ? 11.387  -23.758 -8.837  1.00 19.84 ? 310 GLN B CB  1 
ATOM   6224 C  CG  . GLN B 1 310 ? 10.300  -24.039 -9.861  1.00 21.95 ? 310 GLN B CG  1 
ATOM   6225 C  CD  . GLN B 1 310 ? 10.389  -23.170 -11.094 1.00 31.32 ? 310 GLN B CD  1 
ATOM   6226 O  OE1 . GLN B 1 310 ? 10.719  -21.983 -11.042 1.00 27.48 ? 310 GLN B OE1 1 
ATOM   6227 N  NE2 . GLN B 1 310 ? 10.017  -23.766 -12.219 1.00 35.42 ? 310 GLN B NE2 1 
ATOM   6228 N  N   . LEU B 1 311 ? 12.170  -24.014 -5.409  1.00 14.99 ? 311 LEU B N   1 
ATOM   6229 C  CA  . LEU B 1 311 ? 13.299  -24.023 -4.449  1.00 14.39 ? 311 LEU B CA  1 
ATOM   6230 C  C   . LEU B 1 311 ? 13.330  -25.378 -3.719  1.00 14.76 ? 311 LEU B C   1 
ATOM   6231 O  O   . LEU B 1 311 ? 13.091  -25.482 -2.497  1.00 15.85 ? 311 LEU B O   1 
ATOM   6232 C  CB  . LEU B 1 311 ? 13.164  -22.828 -3.509  1.00 13.31 ? 311 LEU B CB  1 
ATOM   6233 C  CG  . LEU B 1 311 ? 13.348  -21.444 -4.118  1.00 12.85 ? 311 LEU B CG  1 
ATOM   6234 C  CD1 . LEU B 1 311 ? 13.022  -20.365 -3.103  1.00 12.60 ? 311 LEU B CD1 1 
ATOM   6235 C  CD2 . LEU B 1 311 ? 14.767  -21.243 -4.665  1.00 14.98 ? 311 LEU B CD2 1 
ATOM   6236 N  N   . LYS B 1 312 ? 13.651  -26.429 -4.446  1.00 15.44 ? 312 LYS B N   1 
ATOM   6237 C  CA  . LYS B 1 312 ? 13.524  -27.798 -3.897  1.00 15.21 ? 312 LYS B CA  1 
ATOM   6238 C  C   . LYS B 1 312 ? 14.495  -27.975 -2.751  1.00 15.40 ? 312 LYS B C   1 
ATOM   6239 O  O   . LYS B 1 312 ? 14.084  -28.525 -1.724  1.00 15.03 ? 312 LYS B O   1 
ATOM   6240 C  CB  . LYS B 1 312 ? 13.816  -28.807 -5.005  1.00 18.03 ? 312 LYS B CB  1 
ATOM   6241 C  CG  . LYS B 1 312 ? 13.754  -30.276 -4.595  1.00 20.21 ? 312 LYS B CG  1 
ATOM   6242 C  CD  . LYS B 1 312 ? 13.995  -31.149 -5.806  1.00 24.22 ? 312 LYS B CD  1 
ATOM   6243 C  CE  . LYS B 1 312 ? 13.656  -32.609 -5.650  1.00 29.79 ? 312 LYS B CE  1 
ATOM   6244 N  NZ  . LYS B 1 312 ? 14.334  -33.194 -4.477  1.00 32.25 ? 312 LYS B NZ  1 
ATOM   6245 N  N   . TYR B 1 313 ? 15.755  -27.574 -2.892  1.00 13.19 ? 313 TYR B N   1 
ATOM   6246 C  CA  . TYR B 1 313 ? 16.742  -27.802 -1.826  1.00 13.80 ? 313 TYR B CA  1 
ATOM   6247 C  C   . TYR B 1 313 ? 16.397  -26.950 -0.605  1.00 13.38 ? 313 TYR B C   1 
ATOM   6248 O  O   . TYR B 1 313 ? 16.565  -27.375 0.548   1.00 13.13 ? 313 TYR B O   1 
ATOM   6249 C  CB  . TYR B 1 313 ? 18.176  -27.575 -2.333  1.00 13.53 ? 313 TYR B CB  1 
ATOM   6250 C  CG  . TYR B 1 313 ? 19.218  -28.102 -1.368  1.00 14.31 ? 313 TYR B CG  1 
ATOM   6251 C  CD1 . TYR B 1 313 ? 19.455  -29.467 -1.273  1.00 15.34 ? 313 TYR B CD1 1 
ATOM   6252 C  CD2 . TYR B 1 313 ? 19.901  -27.266 -0.522  1.00 16.28 ? 313 TYR B CD2 1 
ATOM   6253 C  CE1 . TYR B 1 313 ? 20.406  -29.966 -0.414  1.00 17.20 ? 313 TYR B CE1 1 
ATOM   6254 C  CE2 . TYR B 1 313 ? 20.882  -27.753 0.331   1.00 17.38 ? 313 TYR B CE2 1 
ATOM   6255 C  CZ  . TYR B 1 313 ? 21.124  -29.113 0.390   1.00 15.90 ? 313 TYR B CZ  1 
ATOM   6256 O  OH  . TYR B 1 313 ? 22.092  -29.598 1.258   1.00 17.32 ? 313 TYR B OH  1 
ATOM   6257 N  N   . VAL B 1 314 ? 15.936  -25.742 -0.804  1.00 13.39 ? 314 VAL B N   1 
ATOM   6258 C  CA  . VAL B 1 314 ? 15.490  -24.919 0.357   1.00 13.42 ? 314 VAL B CA  1 
ATOM   6259 C  C   . VAL B 1 314 ? 14.391  -25.678 1.121   1.00 13.12 ? 314 VAL B C   1 
ATOM   6260 O  O   . VAL B 1 314 ? 14.372  -25.709 2.395   1.00 13.00 ? 314 VAL B O   1 
ATOM   6261 C  CB  . VAL B 1 314 ? 15.007  -23.532 -0.088  1.00 14.24 ? 314 VAL B CB  1 
ATOM   6262 C  CG1 . VAL B 1 314 ? 14.466  -22.720 1.073   1.00 15.62 ? 314 VAL B CG1 1 
ATOM   6263 C  CG2 . VAL B 1 314 ? 16.182  -22.781 -0.721  1.00 15.17 ? 314 VAL B CG2 1 
ATOM   6264 N  N   . GLY B 1 315 ? 13.447  -26.265 0.428   1.00 12.82 ? 315 GLY B N   1 
ATOM   6265 C  CA  . GLY B 1 315 ? 12.397  -27.076 1.059   1.00 13.50 ? 315 GLY B CA  1 
ATOM   6266 C  C   . GLY B 1 315 ? 12.972  -28.258 1.804   1.00 13.48 ? 315 GLY B C   1 
ATOM   6267 O  O   . GLY B 1 315 ? 12.461  -28.638 2.919   1.00 13.98 ? 315 GLY B O   1 
ATOM   6268 N  N   . MET B 1 316 ? 14.027  -28.865 1.284   1.00 13.30 ? 316 MET B N   1 
ATOM   6269 C  CA  . MET B 1 316 ? 14.697  -29.992 1.978   1.00 12.31 ? 316 MET B CA  1 
ATOM   6270 C  C   . MET B 1 316 ? 15.361  -29.512 3.254   1.00 12.46 ? 316 MET B C   1 
ATOM   6271 O  O   . MET B 1 316 ? 15.312  -30.232 4.269   1.00 13.93 ? 316 MET B O   1 
ATOM   6272 C  CB  . MET B 1 316 ? 15.719  -30.640 1.048   1.00 13.29 ? 316 MET B CB  1 
ATOM   6273 C  CG  . MET B 1 316 ? 15.043  -31.382 -0.073  1.00 15.23 ? 316 MET B CG  1 
ATOM   6274 S  SD  . MET B 1 316 ? 16.124  -31.667 -1.511  1.00 17.59 ? 316 MET B SD  1 
ATOM   6275 C  CE  . MET B 1 316 ? 17.479  -32.599 -0.843  1.00 16.58 ? 316 MET B CE  1 
ATOM   6276 N  N   . VAL B 1 317 ? 16.004  -28.355 3.192   1.00 11.63 ? 317 VAL B N   1 
ATOM   6277 C  CA  . VAL B 1 317 ? 16.610  -27.726 4.389   1.00 12.08 ? 317 VAL B CA  1 
ATOM   6278 C  C   . VAL B 1 317 ? 15.504  -27.548 5.439   1.00 12.17 ? 317 VAL B C   1 
ATOM   6279 O  O   . VAL B 1 317 ? 15.749  -27.864 6.620   1.00 12.19 ? 317 VAL B O   1 
ATOM   6280 C  CB  . VAL B 1 317 ? 17.310  -26.401 4.010   1.00 12.31 ? 317 VAL B CB  1 
ATOM   6281 C  CG1 . VAL B 1 317 ? 17.624  -25.599 5.243   1.00 12.88 ? 317 VAL B CG1 1 
ATOM   6282 C  CG2 . VAL B 1 317 ? 18.539  -26.664 3.146   1.00 12.82 ? 317 VAL B CG2 1 
ATOM   6283 N  N   . LEU B 1 318 ? 14.332  -27.035 5.074   1.00 12.16 ? 318 LEU B N   1 
ATOM   6284 C  CA  . LEU B 1 318 ? 13.258  -26.731 6.071   1.00 11.52 ? 318 LEU B CA  1 
ATOM   6285 C  C   . LEU B 1 318 ? 12.773  -28.057 6.668   1.00 11.11 ? 318 LEU B C   1 
ATOM   6286 O  O   . LEU B 1 318 ? 12.571  -28.157 7.889   1.00 12.00 ? 318 LEU B O   1 
ATOM   6287 C  CB  . LEU B 1 318 ? 12.138  -25.944 5.400   1.00 11.57 ? 318 LEU B CB  1 
ATOM   6288 C  CG  . LEU B 1 318 ? 12.517  -24.502 5.040   1.00 12.94 ? 318 LEU B CG  1 
ATOM   6289 C  CD1 . LEU B 1 318 ? 11.489  -23.900 4.122   1.00 15.36 ? 318 LEU B CD1 1 
ATOM   6290 C  CD2 . LEU B 1 318 ? 12.670  -23.618 6.262   1.00 13.81 ? 318 LEU B CD2 1 
ATOM   6291 N  N   . ASN B 1 319 ? 12.611  -29.091 5.855   1.00 12.15 ? 319 ASN B N   1 
ATOM   6292 C  CA  . ASN B 1 319 ? 12.166  -30.417 6.376   1.00 12.15 ? 319 ASN B CA  1 
ATOM   6293 C  C   . ASN B 1 319 ? 13.201  -30.995 7.330   1.00 12.26 ? 319 ASN B C   1 
ATOM   6294 O  O   . ASN B 1 319 ? 12.804  -31.576 8.331   1.00 12.38 ? 319 ASN B O   1 
ATOM   6295 C  CB  . ASN B 1 319 ? 11.845  -31.396 5.250   1.00 14.04 ? 319 ASN B CB  1 
ATOM   6296 C  CG  . ASN B 1 319 ? 10.504  -31.139 4.614   1.00 17.21 ? 319 ASN B CG  1 
ATOM   6297 O  OD1 . ASN B 1 319 ? 9.525   -30.788 5.281   1.00 19.99 ? 319 ASN B OD1 1 
ATOM   6298 N  ND2 . ASN B 1 319 ? 10.443  -31.378 3.303   1.00 23.56 ? 319 ASN B ND2 1 
ATOM   6299 N  N   . GLU B 1 320 ? 14.487  -30.873 7.011   1.00 12.74 ? 320 GLU B N   1 
ATOM   6300 C  CA  . GLU B 1 320 ? 15.534  -31.401 7.906   1.00 13.85 ? 320 GLU B CA  1 
ATOM   6301 C  C   . GLU B 1 320 ? 15.563  -30.600 9.190   1.00 13.39 ? 320 GLU B C   1 
ATOM   6302 O  O   . GLU B 1 320 ? 15.857  -31.232 10.262  1.00 14.97 ? 320 GLU B O   1 
ATOM   6303 C  CB  . GLU B 1 320 ? 16.862  -31.499 7.172   1.00 15.12 ? 320 GLU B CB  1 
ATOM   6304 C  CG  . GLU B 1 320 ? 17.963  -32.108 7.951   1.00 14.20 ? 320 GLU B CG  1 
ATOM   6305 C  CD  . GLU B 1 320 ? 17.905  -33.588 8.294   1.00 16.64 ? 320 GLU B CD  1 
ATOM   6306 O  OE1 . GLU B 1 320 ? 16.804  -34.204 8.113   1.00 15.01 ? 320 GLU B OE1 1 
ATOM   6307 O  OE2 . GLU B 1 320 ? 18.957  -34.174 8.717   1.00 14.69 ? 320 GLU B OE2 1 
ATOM   6308 N  N   . ALA B 1 321 ? 15.280  -29.304 9.185   1.00 12.01 ? 321 ALA B N   1 
ATOM   6309 C  CA  . ALA B 1 321 ? 15.173  -28.531 10.432  1.00 12.22 ? 321 ALA B CA  1 
ATOM   6310 C  C   . ALA B 1 321 ? 13.962  -28.983 11.232  1.00 11.99 ? 321 ALA B C   1 
ATOM   6311 O  O   . ALA B 1 321 ? 14.065  -29.138 12.478  1.00 12.44 ? 321 ALA B O   1 
ATOM   6312 C  CB  . ALA B 1 321 ? 15.041  -27.075 10.135  1.00 13.30 ? 321 ALA B CB  1 
ATOM   6313 N  N   . LEU B 1 322 ? 12.833  -29.271 10.572  1.00 10.84 ? 322 LEU B N   1 
ATOM   6314 C  CA  . LEU B 1 322 ? 11.662  -29.816 11.277  1.00 12.60 ? 322 LEU B CA  1 
ATOM   6315 C  C   . LEU B 1 322 ? 11.964  -31.205 11.796  1.00 13.19 ? 322 LEU B C   1 
ATOM   6316 O  O   . LEU B 1 322 ? 11.301  -31.614 12.781  1.00 12.54 ? 322 LEU B O   1 
ATOM   6317 C  CB  . LEU B 1 322 ? 10.487  -29.900 10.314  1.00 12.24 ? 322 LEU B CB  1 
ATOM   6318 C  CG  . LEU B 1 322 ? 9.880   -28.557 9.943   1.00 14.00 ? 322 LEU B CG  1 
ATOM   6319 C  CD1 . LEU B 1 322 ? 8.846   -28.747 8.892   1.00 15.49 ? 322 LEU B CD1 1 
ATOM   6320 C  CD2 . LEU B 1 322 ? 9.269   -27.857 11.145  1.00 15.41 ? 322 LEU B CD2 1 
ATOM   6321 N  N   . ARG B 1 323 ? 12.820  -31.977 11.130  1.00 10.63 ? 323 ARG B N   1 
ATOM   6322 C  CA  . ARG B 1 323 ? 13.114  -33.326 11.640  1.00 12.02 ? 323 ARG B CA  1 
ATOM   6323 C  C   . ARG B 1 323 ? 13.809  -33.179 13.016  1.00 11.58 ? 323 ARG B C   1 
ATOM   6324 O  O   . ARG B 1 323 ? 13.348  -33.758 14.038  1.00 12.93 ? 323 ARG B O   1 
ATOM   6325 C  CB  . ARG B 1 323 ? 13.931  -34.179 10.670  1.00 11.49 ? 323 ARG B CB  1 
ATOM   6326 C  CG  . ARG B 1 323 ? 14.058  -35.609 11.171  1.00 12.61 ? 323 ARG B CG  1 
ATOM   6327 C  CD  . ARG B 1 323 ? 14.997  -36.461 10.345  1.00 13.69 ? 323 ARG B CD  1 
ATOM   6328 N  NE  . ARG B 1 323 ? 16.379  -35.949 10.334  1.00 14.01 ? 323 ARG B NE  1 
ATOM   6329 C  CZ  . ARG B 1 323 ? 17.261  -36.153 11.313  1.00 15.82 ? 323 ARG B CZ  1 
ATOM   6330 N  NH1 . ARG B 1 323 ? 16.997  -36.978 12.316  1.00 16.27 ? 323 ARG B NH1 1 
ATOM   6331 N  NH2 . ARG B 1 323 ? 18.464  -35.612 11.215  1.00 14.28 ? 323 ARG B NH2 1 
ATOM   6332 N  N   . LEU B 1 324 ? 14.892  -32.404 13.056  1.00 11.72 ? 324 LEU B N   1 
ATOM   6333 C  CA  . LEU B 1 324 ? 15.681  -32.327 14.311  1.00 12.04 ? 324 LEU B CA  1 
ATOM   6334 C  C   . LEU B 1 324 ? 14.960  -31.541 15.371  1.00 12.62 ? 324 LEU B C   1 
ATOM   6335 O  O   . LEU B 1 324 ? 15.023  -31.971 16.582  1.00 12.73 ? 324 LEU B O   1 
ATOM   6336 C  CB  . LEU B 1 324 ? 17.054  -31.744 13.974  1.00 13.37 ? 324 LEU B CB  1 
ATOM   6337 C  CG  . LEU B 1 324 ? 17.995  -32.756 13.335  1.00 15.90 ? 324 LEU B CG  1 
ATOM   6338 C  CD1 . LEU B 1 324 ? 19.209  -32.076 12.747  1.00 18.96 ? 324 LEU B CD1 1 
ATOM   6339 C  CD2 . LEU B 1 324 ? 18.383  -33.833 14.315  1.00 17.74 ? 324 LEU B CD2 1 
ATOM   6340 N  N   . TRP B 1 325 ? 14.332  -30.409 15.053  1.00 12.36 ? 325 TRP B N   1 
ATOM   6341 C  CA  . TRP B 1 325 ? 13.697  -29.555 16.053  1.00 12.86 ? 325 TRP B CA  1 
ATOM   6342 C  C   . TRP B 1 325 ? 12.304  -29.178 15.584  1.00 12.66 ? 325 TRP B C   1 
ATOM   6343 O  O   . TRP B 1 325 ? 12.070  -28.019 15.176  1.00 14.09 ? 325 TRP B O   1 
ATOM   6344 C  CB  . TRP B 1 325 ? 14.568  -28.365 16.469  1.00 12.84 ? 325 TRP B CB  1 
ATOM   6345 C  CG  . TRP B 1 325 ? 15.762  -28.822 17.247  1.00 13.58 ? 325 TRP B CG  1 
ATOM   6346 C  CD1 . TRP B 1 325 ? 17.057  -28.839 16.843  1.00 14.66 ? 325 TRP B CD1 1 
ATOM   6347 C  CD2 . TRP B 1 325 ? 15.721  -29.459 18.539  1.00 13.91 ? 325 TRP B CD2 1 
ATOM   6348 N  NE1 . TRP B 1 325 ? 17.844  -29.390 17.820  1.00 15.64 ? 325 TRP B NE1 1 
ATOM   6349 C  CE2 . TRP B 1 325 ? 17.054  -29.778 18.869  1.00 14.22 ? 325 TRP B CE2 1 
ATOM   6350 C  CE3 . TRP B 1 325 ? 14.693  -29.687 19.454  1.00 15.74 ? 325 TRP B CE3 1 
ATOM   6351 C  CZ2 . TRP B 1 325 ? 17.369  -30.393 20.084  1.00 16.32 ? 325 TRP B CZ2 1 
ATOM   6352 C  CZ3 . TRP B 1 325 ? 15.009  -30.320 20.633  1.00 17.14 ? 325 TRP B CZ3 1 
ATOM   6353 C  CH2 . TRP B 1 325 ? 16.334  -30.613 20.947  1.00 16.43 ? 325 TRP B CH2 1 
ATOM   6354 N  N   . PRO B 1 326 ? 11.340  -30.106 15.641  1.00 12.10 ? 326 PRO B N   1 
ATOM   6355 C  CA  . PRO B 1 326 ? 9.956   -29.808 15.237  1.00 13.84 ? 326 PRO B CA  1 
ATOM   6356 C  C   . PRO B 1 326 ? 9.439   -28.756 16.202  1.00 13.88 ? 326 PRO B C   1 
ATOM   6357 O  O   . PRO B 1 326 ? 9.284   -29.004 17.367  1.00 14.34 ? 326 PRO B O   1 
ATOM   6358 C  CB  . PRO B 1 326 ? 9.250   -31.157 15.286  1.00 13.53 ? 326 PRO B CB  1 
ATOM   6359 C  CG  . PRO B 1 326 ? 10.058  -31.932 16.291  1.00 14.34 ? 326 PRO B CG  1 
ATOM   6360 C  CD  . PRO B 1 326 ? 11.500  -31.486 16.139  1.00 13.35 ? 326 PRO B CD  1 
ATOM   6361 N  N   . THR B 1 327 ? 9.130   -27.577 15.677  1.00 13.65 ? 327 THR B N   1 
ATOM   6362 C  CA  . THR B 1 327 ? 8.916   -26.408 16.527  1.00 15.06 ? 327 THR B CA  1 
ATOM   6363 C  C   . THR B 1 327 ? 7.648   -26.608 17.323  1.00 14.44 ? 327 THR B C   1 
ATOM   6364 O  O   . THR B 1 327 ? 7.613   -26.066 18.427  1.00 15.90 ? 327 THR B O   1 
ATOM   6365 C  CB  . THR B 1 327 ? 8.966   -25.136 15.698  1.00 17.20 ? 327 THR B CB  1 
ATOM   6366 O  OG1 . THR B 1 327 ? 8.823   -24.008 16.543  1.00 24.15 ? 327 THR B OG1 1 
ATOM   6367 C  CG2 . THR B 1 327 ? 7.877   -25.108 14.676  1.00 14.99 ? 327 THR B CG2 1 
ATOM   6368 N  N   . ALA B 1 328 ? 6.641   -27.335 16.825  1.00 13.22 ? 328 ALA B N   1 
ATOM   6369 C  CA  . ALA B 1 328 ? 5.503   -27.783 17.642  1.00 14.01 ? 328 ALA B CA  1 
ATOM   6370 C  C   . ALA B 1 328 ? 5.856   -29.199 18.040  1.00 16.70 ? 328 ALA B C   1 
ATOM   6371 O  O   . ALA B 1 328 ? 5.791   -30.104 17.193  1.00 20.85 ? 328 ALA B O   1 
ATOM   6372 C  CB  . ALA B 1 328 ? 4.205   -27.714 16.839  1.00 14.72 ? 328 ALA B CB  1 
ATOM   6373 N  N   . PRO B 1 329 ? 6.376   -29.472 19.247  1.00 12.40 ? 329 PRO B N   1 
ATOM   6374 C  CA  . PRO B 1 329 ? 7.047   -30.760 19.492  1.00 12.34 ? 329 PRO B CA  1 
ATOM   6375 C  C   . PRO B 1 329 ? 6.221   -31.955 19.973  1.00 11.53 ? 329 PRO B C   1 
ATOM   6376 O  O   . PRO B 1 329 ? 6.753   -32.996 20.131  1.00 13.30 ? 329 PRO B O   1 
ATOM   6377 C  CB  . PRO B 1 329 ? 8.017   -30.353 20.622  1.00 13.46 ? 329 PRO B CB  1 
ATOM   6378 C  CG  . PRO B 1 329 ? 7.334   -29.291 21.350  1.00 12.93 ? 329 PRO B CG  1 
ATOM   6379 C  CD  . PRO B 1 329 ? 6.500   -28.519 20.350  1.00 13.71 ? 329 PRO B CD  1 
ATOM   6380 N  N   . ALA B 1 330 ? 4.917   -31.754 20.117  1.00 13.07 ? 330 ALA B N   1 
ATOM   6381 C  CA  . ALA B 1 330 ? 4.094   -32.835 20.696  1.00 12.63 ? 330 ALA B CA  1 
ATOM   6382 C  C   . ALA B 1 330 ? 2.640   -32.677 20.269  1.00 14.40 ? 330 ALA B C   1 
ATOM   6383 O  O   . ALA B 1 330 ? 2.168   -31.572 20.042  1.00 15.89 ? 330 ALA B O   1 
ATOM   6384 C  CB  . ALA B 1 330 ? 4.237   -32.862 22.170  1.00 15.35 ? 330 ALA B CB  1 
ATOM   6385 N  N   . PHE B 1 331 ? 1.944   -33.793 20.248  1.00 11.68 ? 331 PHE B N   1 
ATOM   6386 C  CA  . PHE B 1 331 ? 0.484   -33.820 20.123  1.00 12.18 ? 331 PHE B CA  1 
ATOM   6387 C  C   . PHE B 1 331 ? -0.069  -35.002 20.904  1.00 12.67 ? 331 PHE B C   1 
ATOM   6388 O  O   . PHE B 1 331 ? 0.639   -36.035 21.023  1.00 12.76 ? 331 PHE B O   1 
ATOM   6389 C  CB  . PHE B 1 331 ? 0.013   -33.801 18.693  1.00 13.28 ? 331 PHE B CB  1 
ATOM   6390 C  CG  . PHE B 1 331 ? 0.453   -34.902 17.780  1.00 13.39 ? 331 PHE B CG  1 
ATOM   6391 C  CD1 . PHE B 1 331 ? 1.666   -34.838 17.120  1.00 14.20 ? 331 PHE B CD1 1 
ATOM   6392 C  CD2 . PHE B 1 331 ? -0.373  -35.992 17.543  1.00 13.43 ? 331 PHE B CD2 1 
ATOM   6393 C  CE1 . PHE B 1 331 ? 2.054   -35.835 16.261  1.00 13.72 ? 331 PHE B CE1 1 
ATOM   6394 C  CE2 . PHE B 1 331 ? 0.006   -36.964 16.644  1.00 15.66 ? 331 PHE B CE2 1 
ATOM   6395 C  CZ  . PHE B 1 331 ? 1.234   -36.921 16.035  1.00 15.30 ? 331 PHE B CZ  1 
ATOM   6396 N  N   . SER B 1 332 ? -1.274  -34.854 21.380  1.00 10.83 ? 332 SER B N   1 
ATOM   6397 C  CA  . SER B 1 332 ? -1.886  -35.821 22.320  1.00 10.62 ? 332 SER B CA  1 
ATOM   6398 C  C   . SER B 1 332 ? -3.015  -36.557 21.593  1.00 12.38 ? 332 SER B C   1 
ATOM   6399 O  O   . SER B 1 332 ? -3.755  -35.958 20.804  1.00 11.35 ? 332 SER B O   1 
ATOM   6400 C  CB  . SER B 1 332 ? -2.341  -35.133 23.555  1.00 12.72 ? 332 SER B CB  1 
ATOM   6401 O  OG  . SER B 1 332 ? -2.726  -36.064 24.555  1.00 13.82 ? 332 SER B OG  1 
ATOM   6402 N  N   . LEU B 1 333 ? -3.251  -37.794 22.027  1.00 13.04 ? 333 LEU B N   1 
ATOM   6403 C  CA  . LEU B 1 333 ? -4.312  -38.671 21.504  1.00 11.84 ? 333 LEU B CA  1 
ATOM   6404 C  C   . LEU B 1 333 ? -5.002  -39.347 22.672  1.00 12.48 ? 333 LEU B C   1 
ATOM   6405 O  O   . LEU B 1 333 ? -4.414  -39.479 23.748  1.00 12.77 ? 333 LEU B O   1 
ATOM   6406 C  CB  . LEU B 1 333 ? -3.716  -39.743 20.609  1.00 12.64 ? 333 LEU B CB  1 
ATOM   6407 C  CG  . LEU B 1 333 ? -2.944  -39.175 19.407  1.00 15.92 ? 333 LEU B CG  1 
ATOM   6408 C  CD1 . LEU B 1 333 ? -2.032  -40.183 18.831  1.00 20.15 ? 333 LEU B CD1 1 
ATOM   6409 C  CD2 . LEU B 1 333 ? -3.880  -38.619 18.346  1.00 12.76 ? 333 LEU B CD2 1 
ATOM   6410 N  N   . TYR B 1 334 ? -6.232  -39.771 22.464  1.00 11.73 ? 334 TYR B N   1 
ATOM   6411 C  CA  . TYR B 1 334 ? -6.945  -40.653 23.429  1.00 11.85 ? 334 TYR B CA  1 
ATOM   6412 C  C   . TYR B 1 334 ? -7.410  -41.882 22.672  1.00 11.69 ? 334 TYR B C   1 
ATOM   6413 O  O   . TYR B 1 334 ? -7.747  -41.837 21.493  1.00 12.19 ? 334 TYR B O   1 
ATOM   6414 C  CB  . TYR B 1 334 ? -8.073  -39.925 24.176  1.00 12.64 ? 334 TYR B CB  1 
ATOM   6415 C  CG  . TYR B 1 334 ? -9.258  -39.613 23.305  1.00 12.38 ? 334 TYR B CG  1 
ATOM   6416 C  CD1 . TYR B 1 334 ? -9.313  -38.424 22.618  1.00 14.27 ? 334 TYR B CD1 1 
ATOM   6417 C  CD2 . TYR B 1 334 ? -10.330 -40.486 23.166  1.00 13.70 ? 334 TYR B CD2 1 
ATOM   6418 C  CE1 . TYR B 1 334 ? -10.384 -38.125 21.779  1.00 13.50 ? 334 TYR B CE1 1 
ATOM   6419 C  CE2 . TYR B 1 334 ? -11.419 -40.202 22.356  1.00 14.57 ? 334 TYR B CE2 1 
ATOM   6420 C  CZ  . TYR B 1 334 ? -11.431 -39.024 21.650  1.00 14.46 ? 334 TYR B CZ  1 
ATOM   6421 O  OH  . TYR B 1 334 ? -12.451 -38.729 20.796  1.00 18.01 ? 334 TYR B OH  1 
ATOM   6422 N  N   . ALA B 1 335 ? -7.488  -43.000 23.401  1.00 12.99 ? 335 ALA B N   1 
ATOM   6423 C  CA  . ALA B 1 335 ? -8.021  -44.274 22.892  1.00 13.01 ? 335 ALA B CA  1 
ATOM   6424 C  C   . ALA B 1 335 ? -9.552  -44.193 22.737  1.00 13.37 ? 335 ALA B C   1 
ATOM   6425 O  O   . ALA B 1 335 ? -10.292 -43.928 23.683  1.00 13.61 ? 335 ALA B O   1 
ATOM   6426 C  CB  . ALA B 1 335 ? -7.620  -45.383 23.826  1.00 13.41 ? 335 ALA B CB  1 
ATOM   6427 N  N   . LYS B 1 336 ? -10.016 -44.441 21.538  1.00 13.06 ? 336 LYS B N   1 
ATOM   6428 C  CA  . LYS B 1 336 ? -11.468 -44.419 21.291  1.00 14.03 ? 336 LYS B CA  1 
ATOM   6429 C  C   . LYS B 1 336 ? -12.166 -45.605 21.952  1.00 14.73 ? 336 LYS B C   1 
ATOM   6430 O  O   . LYS B 1 336 ? -13.360 -45.454 22.227  1.00 18.11 ? 336 LYS B O   1 
ATOM   6431 C  CB  . LYS B 1 336 ? -11.692 -44.419 19.791  1.00 14.02 ? 336 LYS B CB  1 
ATOM   6432 C  CG  . LYS B 1 336 ? -11.371 -43.077 19.155  1.00 14.30 ? 336 LYS B CG  1 
ATOM   6433 C  CD  . LYS B 1 336 ? -11.269 -43.178 17.658  1.00 15.66 ? 336 LYS B CD  1 
ATOM   6434 C  CE  . LYS B 1 336 ? -12.497 -43.693 16.972  1.00 18.44 ? 336 LYS B CE  1 
ATOM   6435 N  NZ  . LYS B 1 336 ? -13.607 -42.752 17.175  1.00 20.58 ? 336 LYS B NZ  1 
ATOM   6436 N  N   . GLU B 1 337 ? -11.463 -46.721 22.054  1.00 15.77 ? 337 GLU B N   1 
ATOM   6437 C  CA  . GLU B 1 337 ? -12.014 -47.989 22.617  1.00 17.07 ? 337 GLU B CA  1 
ATOM   6438 C  C   . GLU B 1 337 ? -10.866 -48.651 23.378  1.00 17.73 ? 337 GLU B C   1 
ATOM   6439 O  O   . GLU B 1 337 ? -9.650  -48.341 23.150  1.00 18.57 ? 337 GLU B O   1 
ATOM   6440 C  CB  . GLU B 1 337 ? -12.489 -48.878 21.474  1.00 20.80 ? 337 GLU B CB  1 
ATOM   6441 C  CG  . GLU B 1 337 ? -13.597 -48.274 20.645  1.00 23.86 ? 337 GLU B CG  1 
ATOM   6442 C  CD  . GLU B 1 337 ? -14.921 -48.068 21.348  1.00 28.36 ? 337 GLU B CD  1 
ATOM   6443 O  OE1 . GLU B 1 337 ? -15.096 -48.591 22.472  1.00 30.15 ? 337 GLU B OE1 1 
ATOM   6444 O  OE2 . GLU B 1 337 ? -15.791 -47.351 20.772  1.00 36.50 ? 337 GLU B OE2 1 
ATOM   6445 N  N   . ASP B 1 338 ? -11.166 -49.670 24.166  1.00 17.91 ? 338 ASP B N   1 
ATOM   6446 C  CA  . ASP B 1 338 ? -10.086 -50.530 24.702  1.00 18.98 ? 338 ASP B CA  1 
ATOM   6447 C  C   . ASP B 1 338 ? -9.273  -51.114 23.573  1.00 17.30 ? 338 ASP B C   1 
ATOM   6448 O  O   . ASP B 1 338 ? -9.835  -51.527 22.510  1.00 19.92 ? 338 ASP B O   1 
ATOM   6449 C  CB  . ASP B 1 338 ? -10.653 -51.661 25.550  1.00 19.31 ? 338 ASP B CB  1 
ATOM   6450 C  CG  . ASP B 1 338 ? -11.371 -51.259 26.807  1.00 23.02 ? 338 ASP B CG  1 
ATOM   6451 O  OD1 . ASP B 1 338 ? -11.407 -50.043 27.202  1.00 21.06 ? 338 ASP B OD1 1 
ATOM   6452 O  OD2 . ASP B 1 338 ? -11.903 -52.210 27.447  1.00 26.26 ? 338 ASP B OD2 1 
ATOM   6453 N  N   . THR B 1 339 ? -7.958  -51.161 23.729  1.00 18.62 ? 339 THR B N   1 
ATOM   6454 C  CA  . THR B 1 339 ? -7.122  -51.655 22.623  1.00 20.07 ? 339 THR B CA  1 
ATOM   6455 C  C   . THR B 1 339 ? -5.775  -52.028 23.190  1.00 20.91 ? 339 THR B C   1 
ATOM   6456 O  O   . THR B 1 339 ? -5.468  -51.509 24.286  1.00 26.99 ? 339 THR B O   1 
ATOM   6457 C  CB  . THR B 1 339 ? -7.024  -50.592 21.510  1.00 21.25 ? 339 THR B CB  1 
ATOM   6458 O  OG1 . THR B 1 339 ? -6.456  -51.184 20.344  1.00 22.39 ? 339 THR B OG1 1 
ATOM   6459 C  CG2 . THR B 1 339 ? -6.173  -49.410 21.900  1.00 22.12 ? 339 THR B CG2 1 
ATOM   6460 N  N   . VAL B 1 340 ? -4.982  -52.709 22.411  1.00 21.93 ? 340 VAL B N   1 
ATOM   6461 C  CA  . VAL B 1 340 ? -3.608  -53.075 22.831  1.00 21.85 ? 340 VAL B CA  1 
ATOM   6462 C  C   . VAL B 1 340 ? -2.640  -52.383 21.902  1.00 19.78 ? 340 VAL B C   1 
ATOM   6463 O  O   . VAL B 1 340 ? -2.705  -52.579 20.685  1.00 21.26 ? 340 VAL B O   1 
ATOM   6464 C  CB  . VAL B 1 340 ? -3.379  -54.598 22.841  1.00 22.80 ? 340 VAL B CB  1 
ATOM   6465 C  CG1 . VAL B 1 340 ? -1.944  -54.915 23.184  1.00 24.30 ? 340 VAL B CG1 1 
ATOM   6466 C  CG2 . VAL B 1 340 ? -4.294  -55.230 23.854  1.00 24.18 ? 340 VAL B CG2 1 
ATOM   6467 N  N   . LEU B 1 341 ? -1.728  -51.634 22.480  1.00 19.71 ? 341 LEU B N   1 
ATOM   6468 C  CA  . LEU B 1 341 ? -0.710  -50.920 21.694  1.00 20.73 ? 341 LEU B CA  1 
ATOM   6469 C  C   . LEU B 1 341 ? 0.538   -51.817 21.502  1.00 20.77 ? 341 LEU B C   1 
ATOM   6470 O  O   . LEU B 1 341 ? 1.084   -52.327 22.505  1.00 23.33 ? 341 LEU B O   1 
ATOM   6471 C  CB  . LEU B 1 341 ? -0.481  -49.595 22.439  1.00 20.91 ? 341 LEU B CB  1 
ATOM   6472 C  CG  . LEU B 1 341 ? 0.447   -48.606 21.777  1.00 23.80 ? 341 LEU B CG  1 
ATOM   6473 C  CD1 . LEU B 1 341 ? -0.168  -48.054 20.494  1.00 22.25 ? 341 LEU B CD1 1 
ATOM   6474 C  CD2 . LEU B 1 341 ? 0.786   -47.489 22.736  1.00 22.02 ? 341 LEU B CD2 1 
ATOM   6475 N  N   . GLY B 1 342 ? 0.967   -52.091 20.274  1.00 20.81 ? 342 GLY B N   1 
ATOM   6476 C  CA  . GLY B 1 342 ? 2.250   -52.745 20.001  1.00 21.65 ? 342 GLY B CA  1 
ATOM   6477 C  C   . GLY B 1 342 ? 2.274   -54.203 20.473  1.00 23.69 ? 342 GLY B C   1 
ATOM   6478 O  O   . GLY B 1 342 ? 3.371   -54.760 20.579  1.00 22.70 ? 342 GLY B O   1 
ATOM   6479 N  N   . GLY B 1 343 ? 1.099   -54.794 20.687  1.00 23.35 ? 343 GLY B N   1 
ATOM   6480 C  CA  . GLY B 1 343 ? 0.953   -56.202 21.120  1.00 22.11 ? 343 GLY B CA  1 
ATOM   6481 C  C   . GLY B 1 343 ? 1.346   -56.363 22.560  1.00 25.59 ? 343 GLY B C   1 
ATOM   6482 O  O   . GLY B 1 343 ? 1.304   -57.508 23.072  1.00 28.10 ? 343 GLY B O   1 
ATOM   6483 N  N   . GLU B 1 344 ? 1.686   -55.269 23.239  1.00 21.69 ? 344 GLU B N   1 
ATOM   6484 C  CA  . GLU B 1 344 ? 2.324   -55.341 24.588  1.00 23.27 ? 344 GLU B CA  1 
ATOM   6485 C  C   . GLU B 1 344 ? 1.602   -54.508 25.637  1.00 22.44 ? 344 GLU B C   1 
ATOM   6486 O  O   . GLU B 1 344 ? 1.753   -54.824 26.811  1.00 24.12 ? 344 GLU B O   1 
ATOM   6487 C  CB  . GLU B 1 344 ? 3.778   -54.857 24.486  1.00 25.57 ? 344 GLU B CB  1 
ATOM   6488 C  CG  . GLU B 1 344 ? 4.632   -55.818 23.695  1.00 29.80 ? 344 GLU B CG  1 
ATOM   6489 C  CD  . GLU B 1 344 ? 6.075   -55.458 23.420  1.00 36.21 ? 344 GLU B CD  1 
ATOM   6490 O  OE1 . GLU B 1 344 ? 6.389   -54.274 23.170  1.00 36.44 ? 344 GLU B OE1 1 
ATOM   6491 O  OE2 . GLU B 1 344 ? 6.875   -56.406 23.383  1.00 43.50 ? 344 GLU B OE2 1 
ATOM   6492 N  N   . TYR B 1 345 ? 0.962   -53.388 25.279  1.00 20.44 ? 345 TYR B N   1 
ATOM   6493 C  CA  . TYR B 1 345 ? 0.548   -52.362 26.260  1.00 20.13 ? 345 TYR B CA  1 
ATOM   6494 C  C   . TYR B 1 345 ? -0.965  -52.195 26.192  1.00 21.05 ? 345 TYR B C   1 
ATOM   6495 O  O   . TYR B 1 345 ? -1.482  -51.479 25.347  1.00 19.26 ? 345 TYR B O   1 
ATOM   6496 C  CB  . TYR B 1 345 ? 1.281   -51.033 26.029  1.00 19.75 ? 345 TYR B CB  1 
ATOM   6497 C  CG  . TYR B 1 345 ? 2.777   -51.176 26.093  1.00 19.02 ? 345 TYR B CG  1 
ATOM   6498 C  CD1 . TYR B 1 345 ? 3.397   -51.433 27.313  1.00 21.71 ? 345 TYR B CD1 1 
ATOM   6499 C  CD2 . TYR B 1 345 ? 3.559   -51.132 24.982  1.00 17.93 ? 345 TYR B CD2 1 
ATOM   6500 C  CE1 . TYR B 1 345 ? 4.762   -51.597 27.402  1.00 22.03 ? 345 TYR B CE1 1 
ATOM   6501 C  CE2 . TYR B 1 345 ? 4.931   -51.298 25.048  1.00 20.12 ? 345 TYR B CE2 1 
ATOM   6502 C  CZ  . TYR B 1 345 ? 5.531   -51.565 26.261  1.00 20.66 ? 345 TYR B CZ  1 
ATOM   6503 O  OH  . TYR B 1 345 ? 6.873   -51.746 26.263  1.00 24.71 ? 345 TYR B OH  1 
ATOM   6504 N  N   . PRO B 1 346 ? -1.742  -52.817 27.082  1.00 20.68 ? 346 PRO B N   1 
ATOM   6505 C  CA  . PRO B 1 346 ? -3.191  -52.675 27.090  1.00 21.61 ? 346 PRO B CA  1 
ATOM   6506 C  C   . PRO B 1 346 ? -3.619  -51.266 27.496  1.00 21.68 ? 346 PRO B C   1 
ATOM   6507 O  O   . PRO B 1 346 ? -3.114  -50.700 28.454  1.00 23.24 ? 346 PRO B O   1 
ATOM   6508 C  CB  . PRO B 1 346 ? -3.721  -53.725 28.083  1.00 25.91 ? 346 PRO B CB  1 
ATOM   6509 C  CG  . PRO B 1 346 ? -2.491  -54.469 28.567  1.00 26.75 ? 346 PRO B CG  1 
ATOM   6510 C  CD  . PRO B 1 346 ? -1.249  -53.716 28.152  1.00 24.11 ? 346 PRO B CD  1 
ATOM   6511 N  N   . LEU B 1 347 ? -4.546  -50.709 26.719  1.00 20.21 ? 347 LEU B N   1 
ATOM   6512 C  CA  . LEU B 1 347 ? -5.129  -49.390 27.023  1.00 19.84 ? 347 LEU B CA  1 
ATOM   6513 C  C   . LEU B 1 347 ? -6.631  -49.570 27.188  1.00 19.04 ? 347 LEU B C   1 
ATOM   6514 O  O   . LEU B 1 347 ? -7.245  -50.366 26.446  1.00 21.41 ? 347 LEU B O   1 
ATOM   6515 C  CB  . LEU B 1 347 ? -4.829  -48.406 25.883  1.00 19.43 ? 347 LEU B CB  1 
ATOM   6516 C  CG  . LEU B 1 347 ? -3.362  -48.187 25.521  1.00 18.66 ? 347 LEU B CG  1 
ATOM   6517 C  CD1 . LEU B 1 347 ? -3.263  -47.242 24.314  1.00 18.09 ? 347 LEU B CD1 1 
ATOM   6518 C  CD2 . LEU B 1 347 ? -2.584  -47.599 26.690  1.00 18.49 ? 347 LEU B CD2 1 
ATOM   6519 N  N   . GLU B 1 348 ? -7.180  -48.733 28.023  1.00 18.41 ? 348 GLU B N   1 
ATOM   6520 C  CA  . GLU B 1 348 ? -8.627  -48.579 28.212  1.00 20.27 ? 348 GLU B CA  1 
ATOM   6521 C  C   . GLU B 1 348 ? -9.140  -47.396 27.400  1.00 18.85 ? 348 GLU B C   1 
ATOM   6522 O  O   . GLU B 1 348 ? -8.403  -46.407 27.202  1.00 17.68 ? 348 GLU B O   1 
ATOM   6523 C  CB  . GLU B 1 348 ? -8.957  -48.372 29.682  1.00 25.55 ? 348 GLU B CB  1 
ATOM   6524 C  CG  . GLU B 1 348 ? -8.477  -49.528 30.546  1.00 34.57 ? 348 GLU B CG  1 
ATOM   6525 C  CD  . GLU B 1 348 ? -9.080  -49.608 31.940  1.00 41.25 ? 348 GLU B CD  1 
ATOM   6526 O  OE1 . GLU B 1 348 ? -9.698  -48.610 32.412  1.00 49.68 ? 348 GLU B OE1 1 
ATOM   6527 O  OE2 . GLU B 1 348 ? -8.959  -50.698 32.537  1.00 51.86 ? 348 GLU B OE2 1 
ATOM   6528 N  N   . LYS B 1 349 ? -10.390 -47.462 27.017  1.00 17.42 ? 349 LYS B N   1 
ATOM   6529 C  CA  . LYS B 1 349 ? -11.070 -46.297 26.414  1.00 16.95 ? 349 LYS B CA  1 
ATOM   6530 C  C   . LYS B 1 349 ? -10.794 -45.027 27.210  1.00 15.98 ? 349 LYS B C   1 
ATOM   6531 O  O   . LYS B 1 349 ? -10.916 -45.041 28.470  1.00 17.67 ? 349 LYS B O   1 
ATOM   6532 C  CB  . LYS B 1 349 ? -12.570 -46.586 26.343  1.00 17.76 ? 349 LYS B CB  1 
ATOM   6533 C  CG  . LYS B 1 349 ? -13.403 -45.496 25.734  1.00 18.58 ? 349 LYS B CG  1 
ATOM   6534 C  CD  . LYS B 1 349 ? -14.823 -45.951 25.517  1.00 21.15 ? 349 LYS B CD  1 
ATOM   6535 C  CE  . LYS B 1 349 ? -15.650 -44.833 24.989  1.00 23.82 ? 349 LYS B CE  1 
ATOM   6536 N  NZ  . LYS B 1 349 ? -16.992 -45.386 24.692  1.00 28.55 ? 349 LYS B NZ  1 
ATOM   6537 N  N   . GLY B 1 350 ? -10.340 -43.947 26.546  1.00 14.97 ? 350 GLY B N   1 
ATOM   6538 C  CA  . GLY B 1 350 ? -10.097 -42.684 27.237  1.00 15.83 ? 350 GLY B CA  1 
ATOM   6539 C  C   . GLY B 1 350 ? -8.641  -42.479 27.623  1.00 13.68 ? 350 GLY B C   1 
ATOM   6540 O  O   . GLY B 1 350 ? -8.265  -41.328 27.917  1.00 15.85 ? 350 GLY B O   1 
ATOM   6541 N  N   . ASP B 1 351 ? -7.833  -43.546 27.595  1.00 13.73 ? 351 ASP B N   1 
ATOM   6542 C  CA  . ASP B 1 351 ? -6.403  -43.429 28.006  1.00 13.73 ? 351 ASP B CA  1 
ATOM   6543 C  C   . ASP B 1 351 ? -5.687  -42.442 27.090  1.00 13.74 ? 351 ASP B C   1 
ATOM   6544 O  O   . ASP B 1 351 ? -5.894  -42.471 25.855  1.00 14.56 ? 351 ASP B O   1 
ATOM   6545 C  CB  . ASP B 1 351 ? -5.727  -44.782 28.052  1.00 14.50 ? 351 ASP B CB  1 
ATOM   6546 C  CG  . ASP B 1 351 ? -6.003  -45.593 29.319  1.00 16.83 ? 351 ASP B CG  1 
ATOM   6547 O  OD1 . ASP B 1 351 ? -6.706  -45.104 30.191  1.00 21.08 ? 351 ASP B OD1 1 
ATOM   6548 O  OD2 . ASP B 1 351 ? -5.542  -46.750 29.311  1.00 20.68 ? 351 ASP B OD2 1 
ATOM   6549 N  N   . GLU B 1 352 ? -4.873  -41.605 27.695  1.00 13.82 ? 352 GLU B N   1 
ATOM   6550 C  CA  . GLU B 1 352 ? -4.194  -40.488 26.983  1.00 13.28 ? 352 GLU B CA  1 
ATOM   6551 C  C   . GLU B 1 352 ? -2.750  -40.854 26.620  1.00 13.53 ? 352 GLU B C   1 
ATOM   6552 O  O   . GLU B 1 352 ? -1.999  -41.411 27.453  1.00 14.30 ? 352 GLU B O   1 
ATOM   6553 C  CB  . GLU B 1 352 ? -4.263  -39.226 27.810  1.00 14.94 ? 352 GLU B CB  1 
ATOM   6554 C  CG  . GLU B 1 352 ? -5.680  -38.780 28.174  1.00 17.88 ? 352 GLU B CG  1 
ATOM   6555 C  CD  . GLU B 1 352 ? -5.785  -37.547 29.041  1.00 25.15 ? 352 GLU B CD  1 
ATOM   6556 O  OE1 . GLU B 1 352 ? -5.089  -36.549 28.760  1.00 26.25 ? 352 GLU B OE1 1 
ATOM   6557 O  OE2 . GLU B 1 352 ? -6.615  -37.568 29.967  1.00 39.44 ? 352 GLU B OE2 1 
ATOM   6558 N  N   . LEU B 1 353 ? -2.362  -40.528 25.395  1.00 13.05 ? 353 LEU B N   1 
ATOM   6559 C  CA  . LEU B 1 353 ? -1.026  -40.662 24.823  1.00 13.45 ? 353 LEU B CA  1 
ATOM   6560 C  C   . LEU B 1 353 ? -0.488  -39.280 24.466  1.00 12.53 ? 353 LEU B C   1 
ATOM   6561 O  O   . LEU B 1 353 ? -1.263  -38.374 24.121  1.00 14.47 ? 353 LEU B O   1 
ATOM   6562 C  CB  . LEU B 1 353 ? -1.028  -41.495 23.548  1.00 13.71 ? 353 LEU B CB  1 
ATOM   6563 C  CG  . LEU B 1 353 ? -1.754  -42.830 23.561  1.00 15.75 ? 353 LEU B CG  1 
ATOM   6564 C  CD1 . LEU B 1 353 ? -1.641  -43.532 22.227  1.00 14.97 ? 353 LEU B CD1 1 
ATOM   6565 C  CD2 . LEU B 1 353 ? -1.189  -43.724 24.637  1.00 17.70 ? 353 LEU B CD2 1 
ATOM   6566 N  N   . MET B 1 354 ? 0.830   -39.133 24.497  1.00 11.10 ? 354 MET B N   1 
ATOM   6567 C  CA  . MET B 1 354 ? 1.509   -37.927 23.972  1.00 11.52 ? 354 MET B CA  1 
ATOM   6568 C  C   . MET B 1 354 ? 2.612   -38.390 23.034  1.00 13.88 ? 354 MET B C   1 
ATOM   6569 O  O   . MET B 1 354 ? 3.483   -39.194 23.440  1.00 14.45 ? 354 MET B O   1 
ATOM   6570 C  CB  . MET B 1 354 ? 2.106   -37.072 25.096  1.00 12.89 ? 354 MET B CB  1 
ATOM   6571 C  CG  . MET B 1 354 ? 2.678   -35.744 24.615  1.00 15.29 ? 354 MET B CG  1 
ATOM   6572 S  SD  . MET B 1 354 ? 1.399   -34.585 24.115  1.00 16.33 ? 354 MET B SD  1 
ATOM   6573 C  CE  . MET B 1 354 ? 0.885   -34.035 25.731  1.00 19.72 ? 354 MET B CE  1 
ATOM   6574 N  N   . VAL B 1 355 ? 2.621   -37.881 21.823  1.00 12.65 ? 355 VAL B N   1 
ATOM   6575 C  CA  . VAL B 1 355 ? 3.651   -38.186 20.838  1.00 11.59 ? 355 VAL B CA  1 
ATOM   6576 C  C   . VAL B 1 355 ? 4.772   -37.151 21.039  1.00 11.57 ? 355 VAL B C   1 
ATOM   6577 O  O   . VAL B 1 355 ? 4.543   -35.936 20.876  1.00 12.51 ? 355 VAL B O   1 
ATOM   6578 C  CB  . VAL B 1 355 ? 3.078   -38.127 19.417  1.00 12.21 ? 355 VAL B CB  1 
ATOM   6579 C  CG1 . VAL B 1 355 ? 4.209   -38.292 18.420  1.00 13.35 ? 355 VAL B CG1 1 
ATOM   6580 C  CG2 . VAL B 1 355 ? 1.987   -39.132 19.172  1.00 13.48 ? 355 VAL B CG2 1 
ATOM   6581 N  N   . LEU B 1 356 ? 5.972   -37.631 21.333  1.00 11.34 ? 356 LEU B N   1 
ATOM   6582 C  CA  . LEU B 1 356 ? 7.169   -36.771 21.435  1.00 12.55 ? 356 LEU B CA  1 
ATOM   6583 C  C   . LEU B 1 356 ? 7.848   -36.716 20.079  1.00 11.08 ? 356 LEU B C   1 
ATOM   6584 O  O   . LEU B 1 356 ? 8.652   -37.564 19.752  1.00 12.03 ? 356 LEU B O   1 
ATOM   6585 C  CB  . LEU B 1 356 ? 8.147   -37.339 22.457  1.00 14.63 ? 356 LEU B CB  1 
ATOM   6586 C  CG  . LEU B 1 356 ? 7.726   -37.259 23.892  1.00 16.96 ? 356 LEU B CG  1 
ATOM   6587 C  CD1 . LEU B 1 356 ? 8.804   -37.988 24.735  1.00 19.45 ? 356 LEU B CD1 1 
ATOM   6588 C  CD2 . LEU B 1 356 ? 7.586   -35.823 24.370  1.00 19.30 ? 356 LEU B CD2 1 
ATOM   6589 N  N   . ILE B 1 357 ? 7.482   -35.712 19.307  1.00 10.89 ? 357 ILE B N   1 
ATOM   6590 C  CA  . ILE B 1 357 ? 7.885   -35.671 17.892  1.00 10.40 ? 357 ILE B CA  1 
ATOM   6591 C  C   . ILE B 1 357 ? 9.406   -35.625 17.769  1.00 10.16 ? 357 ILE B C   1 
ATOM   6592 O  O   . ILE B 1 357 ? 9.951   -36.250 16.849  1.00 11.71 ? 357 ILE B O   1 
ATOM   6593 C  CB  . ILE B 1 357 ? 7.216   -34.508 17.148  1.00 11.54 ? 357 ILE B CB  1 
ATOM   6594 C  CG1 . ILE B 1 357 ? 5.682   -34.524 17.274  1.00 11.43 ? 357 ILE B CG1 1 
ATOM   6595 C  CG2 . ILE B 1 357 ? 7.619   -34.580 15.683  1.00 11.36 ? 357 ILE B CG2 1 
ATOM   6596 C  CD1 . ILE B 1 357 ? 5.027   -33.308 16.675  1.00 10.90 ? 357 ILE B CD1 1 
ATOM   6597 N  N   . PRO B 1 358 ? 10.164  -34.856 18.580  1.00 11.33 ? 358 PRO B N   1 
ATOM   6598 C  CA  . PRO B 1 358 ? 11.615  -34.839 18.394  1.00 12.06 ? 358 PRO B CA  1 
ATOM   6599 C  C   . PRO B 1 358 ? 12.242  -36.223 18.588  1.00 12.60 ? 358 PRO B C   1 
ATOM   6600 O  O   . PRO B 1 358 ? 13.244  -36.556 17.947  1.00 11.64 ? 358 PRO B O   1 
ATOM   6601 C  CB  . PRO B 1 358 ? 12.129  -33.904 19.477  1.00 13.31 ? 358 PRO B CB  1 
ATOM   6602 C  CG  . PRO B 1 358 ? 10.965  -32.981 19.756  1.00 12.93 ? 358 PRO B CG  1 
ATOM   6603 C  CD  . PRO B 1 358 ? 9.761   -33.909 19.626  1.00 11.68 ? 358 PRO B CD  1 
ATOM   6604 N  N   . GLN B 1 359 ? 11.625  -37.041 19.436  1.00 13.30 ? 359 GLN B N   1 
ATOM   6605 C  CA  . GLN B 1 359 ? 12.163  -38.394 19.624  1.00 14.13 ? 359 GLN B CA  1 
ATOM   6606 C  C   . GLN B 1 359 ? 11.761  -39.335 18.497  1.00 12.94 ? 359 GLN B C   1 
ATOM   6607 O  O   . GLN B 1 359 ? 12.608  -40.146 18.007  1.00 13.29 ? 359 GLN B O   1 
ATOM   6608 C  CB  . GLN B 1 359 ? 11.678  -39.007 20.928  1.00 15.68 ? 359 GLN B CB  1 
ATOM   6609 C  CG  . GLN B 1 359 ? 12.225  -38.375 22.156  1.00 17.67 ? 359 GLN B CG  1 
ATOM   6610 C  CD  . GLN B 1 359 ? 13.735  -38.449 22.232  1.00 17.94 ? 359 GLN B CD  1 
ATOM   6611 O  OE1 . GLN B 1 359 ? 14.362  -37.443 22.076  1.00 20.05 ? 359 GLN B OE1 1 
ATOM   6612 N  NE2 . GLN B 1 359 ? 14.292  -39.636 22.406  1.00 20.10 ? 359 GLN B NE2 1 
ATOM   6613 N  N   . LEU B 1 360 ? 10.533  -39.208 17.971  1.00 11.81 ? 360 LEU B N   1 
ATOM   6614 C  CA  . LEU B 1 360 ? 10.123  -39.939 16.772  1.00 11.69 ? 360 LEU B CA  1 
ATOM   6615 C  C   . LEU B 1 360 ? 11.168  -39.700 15.662  1.00 11.50 ? 360 LEU B C   1 
ATOM   6616 O  O   . LEU B 1 360 ? 11.591  -40.617 14.982  1.00 12.46 ? 360 LEU B O   1 
ATOM   6617 C  CB  . LEU B 1 360 ? 8.758   -39.423 16.326  1.00 11.67 ? 360 LEU B CB  1 
ATOM   6618 C  CG  . LEU B 1 360 ? 8.262   -39.975 14.993  1.00 12.77 ? 360 LEU B CG  1 
ATOM   6619 C  CD1 . LEU B 1 360 ? 8.082   -41.482 14.991  1.00 13.85 ? 360 LEU B CD1 1 
ATOM   6620 C  CD2 . LEU B 1 360 ? 6.979   -39.274 14.579  1.00 12.91 ? 360 LEU B CD2 1 
ATOM   6621 N  N   . HIS B 1 361 ? 11.558  -38.442 15.491  1.00 11.48 ? 361 HIS B N   1 
ATOM   6622 C  CA  . HIS B 1 361 ? 12.447  -38.022 14.394  1.00 11.09 ? 361 HIS B CA  1 
ATOM   6623 C  C   . HIS B 1 361 ? 13.909  -38.418 14.642  1.00 11.75 ? 361 HIS B C   1 
ATOM   6624 O  O   . HIS B 1 361 ? 14.732  -38.173 13.760  1.00 13.33 ? 361 HIS B O   1 
ATOM   6625 C  CB  . HIS B 1 361 ? 12.316  -36.526 14.236  1.00 11.27 ? 361 HIS B CB  1 
ATOM   6626 C  CG  . HIS B 1 361 ? 10.997  -36.091 13.672  1.00 11.30 ? 361 HIS B CG  1 
ATOM   6627 N  ND1 . HIS B 1 361 ? 10.693  -34.760 13.550  1.00 10.82 ? 361 HIS B ND1 1 
ATOM   6628 C  CD2 . HIS B 1 361 ? 9.903   -36.789 13.248  1.00 11.25 ? 361 HIS B CD2 1 
ATOM   6629 C  CE1 . HIS B 1 361 ? 9.470   -34.634 13.014  1.00 10.92 ? 361 HIS B CE1 1 
ATOM   6630 N  NE2 . HIS B 1 361 ? 8.965   -35.864 12.790  1.00 10.78 ? 361 HIS B NE2 1 
ATOM   6631 N  N   . ARG B 1 362 ? 14.181  -39.044 15.786  1.00 12.16 ? 362 ARG B N   1 
ATOM   6632 C  CA  . ARG B 1 362 ? 15.528  -39.608 16.117  1.00 11.88 ? 362 ARG B CA  1 
ATOM   6633 C  C   . ARG B 1 362 ? 15.471  -41.139 16.147  1.00 13.92 ? 362 ARG B C   1 
ATOM   6634 O  O   . ARG B 1 362 ? 16.426  -41.785 16.668  1.00 15.98 ? 362 ARG B O   1 
ATOM   6635 C  CB  . ARG B 1 362 ? 15.944  -39.016 17.457  1.00 13.70 ? 362 ARG B CB  1 
ATOM   6636 C  CG  . ARG B 1 362 ? 16.419  -37.567 17.314  1.00 14.27 ? 362 ARG B CG  1 
ATOM   6637 C  CD  . ARG B 1 362 ? 16.495  -36.884 18.663  1.00 13.99 ? 362 ARG B CD  1 
ATOM   6638 N  NE  . ARG B 1 362 ? 17.154  -35.576 18.567  1.00 14.77 ? 362 ARG B NE  1 
ATOM   6639 C  CZ  . ARG B 1 362 ? 16.536  -34.469 18.118  1.00 13.92 ? 362 ARG B CZ  1 
ATOM   6640 N  NH1 . ARG B 1 362 ? 15.280  -34.559 17.660  1.00 13.70 ? 362 ARG B NH1 1 
ATOM   6641 N  NH2 . ARG B 1 362 ? 17.224  -33.339 18.005  1.00 14.90 ? 362 ARG B NH2 1 
ATOM   6642 N  N   . ASP B 1 363 ? 14.405  -41.754 15.653  1.00 12.40 ? 363 ASP B N   1 
ATOM   6643 C  CA  . ASP B 1 363 ? 14.282  -43.243 15.645  1.00 14.15 ? 363 ASP B CA  1 
ATOM   6644 C  C   . ASP B 1 363 ? 15.334  -43.789 14.687  1.00 14.38 ? 363 ASP B C   1 
ATOM   6645 O  O   . ASP B 1 363 ? 15.151  -43.696 13.480  1.00 14.21 ? 363 ASP B O   1 
ATOM   6646 C  CB  . ASP B 1 363 ? 12.844  -43.645 15.344  1.00 13.00 ? 363 ASP B CB  1 
ATOM   6647 C  CG  . ASP B 1 363 ? 12.567  -45.133 15.459  1.00 15.04 ? 363 ASP B CG  1 
ATOM   6648 O  OD1 . ASP B 1 363 ? 13.572  -45.918 15.390  1.00 16.71 ? 363 ASP B OD1 1 
ATOM   6649 O  OD2 . ASP B 1 363 ? 11.398  -45.490 15.652  1.00 13.90 ? 363 ASP B OD2 1 
ATOM   6650 N  N   . LYS B 1 364 ? 16.386  -44.439 15.215  1.00 15.29 ? 364 LYS B N   1 
ATOM   6651 C  CA  . LYS B 1 364 ? 17.463  -44.927 14.324  1.00 16.82 ? 364 LYS B CA  1 
ATOM   6652 C  C   . LYS B 1 364 ? 17.005  -46.062 13.412  1.00 17.31 ? 364 LYS B C   1 
ATOM   6653 O  O   . LYS B 1 364 ? 17.634  -46.257 12.355  1.00 20.16 ? 364 LYS B O   1 
ATOM   6654 C  CB  . LYS B 1 364 ? 18.670  -45.353 15.162  1.00 17.57 ? 364 LYS B CB  1 
ATOM   6655 C  CG  . LYS B 1 364 ? 19.336  -44.165 15.823  1.00 19.70 ? 364 LYS B CG  1 
ATOM   6656 C  CD  . LYS B 1 364 ? 20.524  -44.484 16.781  1.00 21.47 ? 364 LYS B CD  1 
ATOM   6657 C  CE  . LYS B 1 364 ? 21.178  -43.262 17.389  1.00 26.73 ? 364 LYS B CE  1 
ATOM   6658 N  NZ  . LYS B 1 364 ? 22.378  -43.637 18.184  1.00 32.05 ? 364 LYS B NZ  1 
ATOM   6659 N  N   . THR B 1 365 ? 15.950  -46.766 13.770  1.00 16.44 ? 365 THR B N   1 
ATOM   6660 C  CA  . THR B 1 365 ? 15.444  -47.858 12.912  1.00 17.34 ? 365 THR B CA  1 
ATOM   6661 C  C   . THR B 1 365 ? 14.843  -47.289 11.626  1.00 18.45 ? 365 THR B C   1 
ATOM   6662 O  O   . THR B 1 365 ? 14.718  -48.057 10.665  1.00 20.47 ? 365 THR B O   1 
ATOM   6663 C  CB  . THR B 1 365 ? 14.446  -48.770 13.626  1.00 19.29 ? 365 THR B CB  1 
ATOM   6664 O  OG1 . THR B 1 365 ? 13.185  -48.121 13.721  1.00 21.85 ? 365 THR B OG1 1 
ATOM   6665 C  CG2 . THR B 1 365 ? 14.911  -49.248 14.981  1.00 19.66 ? 365 THR B CG2 1 
ATOM   6666 N  N   . ILE B 1 366 ? 14.424  -46.026 11.611  1.00 16.40 ? 366 ILE B N   1 
ATOM   6667 C  CA  . ILE B 1 366 ? 13.903  -45.314 10.413  1.00 15.99 ? 366 ILE B CA  1 
ATOM   6668 C  C   . ILE B 1 366 ? 15.010  -44.556 9.704   1.00 16.15 ? 366 ILE B C   1 
ATOM   6669 O  O   . ILE B 1 366 ? 15.074  -44.603 8.468   1.00 18.72 ? 366 ILE B O   1 
ATOM   6670 C  CB  . ILE B 1 366 ? 12.783  -44.345 10.840  1.00 15.06 ? 366 ILE B CB  1 
ATOM   6671 C  CG1 . ILE B 1 366 ? 11.631  -45.125 11.479  1.00 16.36 ? 366 ILE B CG1 1 
ATOM   6672 C  CG2 . ILE B 1 366 ? 12.320  -43.492 9.690   1.00 15.65 ? 366 ILE B CG2 1 
ATOM   6673 C  CD1 . ILE B 1 366 ? 10.875  -46.028 10.526  1.00 18.63 ? 366 ILE B CD1 1 
ATOM   6674 N  N   . TRP B 1 367 ? 15.787  -43.767 10.421  1.00 15.19 ? 367 TRP B N   1 
ATOM   6675 C  CA  . TRP B 1 367 ? 16.664  -42.745 9.816   1.00 15.77 ? 367 TRP B CA  1 
ATOM   6676 C  C   . TRP B 1 367 ? 18.112  -43.227 9.658   1.00 18.67 ? 367 TRP B C   1 
ATOM   6677 O  O   . TRP B 1 367 ? 18.872  -42.570 8.937   1.00 19.20 ? 367 TRP B O   1 
ATOM   6678 C  CB  . TRP B 1 367 ? 16.558  -41.462 10.638  1.00 16.44 ? 367 TRP B CB  1 
ATOM   6679 C  CG  . TRP B 1 367 ? 15.173  -40.907 10.721  1.00 15.28 ? 367 TRP B CG  1 
ATOM   6680 C  CD1 . TRP B 1 367 ? 14.293  -41.093 11.744  1.00 14.75 ? 367 TRP B CD1 1 
ATOM   6681 C  CD2 . TRP B 1 367 ? 14.479  -40.111 9.744   1.00 14.40 ? 367 TRP B CD2 1 
ATOM   6682 N  NE1 . TRP B 1 367 ? 13.105  -40.452 11.473  1.00 14.79 ? 367 TRP B NE1 1 
ATOM   6683 C  CE2 . TRP B 1 367 ? 13.191  -39.845 10.254  1.00 13.94 ? 367 TRP B CE2 1 
ATOM   6684 C  CE3 . TRP B 1 367 ? 14.802  -39.604 8.494   1.00 13.34 ? 367 TRP B CE3 1 
ATOM   6685 C  CZ2 . TRP B 1 367 ? 12.243  -39.110 9.550   1.00 13.47 ? 367 TRP B CZ2 1 
ATOM   6686 C  CZ3 . TRP B 1 367 ? 13.860  -38.879 7.788   1.00 13.82 ? 367 TRP B CZ3 1 
ATOM   6687 C  CH2 . TRP B 1 367 ? 12.610  -38.588 8.331   1.00 13.58 ? 367 TRP B CH2 1 
ATOM   6688 N  N   . GLY B 1 368 ? 18.471  -44.308 10.342  1.00 19.17 ? 368 GLY B N   1 
ATOM   6689 C  CA  . GLY B 1 368 ? 19.862  -44.782 10.443  1.00 18.44 ? 368 GLY B CA  1 
ATOM   6690 C  C   . GLY B 1 368 ? 20.590  -44.166 11.602  1.00 22.22 ? 368 GLY B C   1 
ATOM   6691 O  O   . GLY B 1 368 ? 20.011  -43.407 12.387  1.00 21.54 ? 368 GLY B O   1 
ATOM   6692 N  N   . ASP B 1 369 ? 21.871  -44.488 11.763  1.00 25.20 ? 369 ASP B N   1 
ATOM   6693 C  CA  . ASP B 1 369 ? 22.576  -44.106 13.007  1.00 29.50 ? 369 ASP B CA  1 
ATOM   6694 C  C   . ASP B 1 369 ? 22.925  -42.618 13.042  1.00 28.31 ? 369 ASP B C   1 
ATOM   6695 O  O   . ASP B 1 369 ? 23.061  -42.104 14.171  1.00 38.58 ? 369 ASP B O   1 
ATOM   6696 C  CB  . ASP B 1 369 ? 23.804  -44.989 13.207  1.00 34.51 ? 369 ASP B CB  1 
ATOM   6697 C  CG  . ASP B 1 369 ? 23.439  -46.364 13.731  1.00 39.49 ? 369 ASP B CG  1 
ATOM   6698 O  OD1 . ASP B 1 369 ? 22.342  -46.516 14.307  1.00 42.45 ? 369 ASP B OD1 1 
ATOM   6699 O  OD2 . ASP B 1 369 ? 24.250  -47.273 13.559  1.00 50.22 ? 369 ASP B OD2 1 
ATOM   6700 N  N   . ASP B 1 370 ? 23.016  -41.951 11.899  1.00 27.97 ? 370 ASP B N   1 
ATOM   6701 C  CA  . ASP B 1 370 ? 23.483  -40.534 11.837  1.00 28.52 ? 370 ASP B CA  1 
ATOM   6702 C  C   . ASP B 1 370 ? 22.337  -39.556 12.172  1.00 25.45 ? 370 ASP B C   1 
ATOM   6703 O  O   . ASP B 1 370 ? 22.393  -38.429 11.636  1.00 26.03 ? 370 ASP B O   1 
ATOM   6704 C  CB  . ASP B 1 370 ? 24.087  -40.257 10.461  1.00 29.62 ? 370 ASP B CB  1 
ATOM   6705 C  CG  . ASP B 1 370 ? 23.086  -40.290 9.325   1.00 31.90 ? 370 ASP B CG  1 
ATOM   6706 O  OD1 . ASP B 1 370 ? 21.910  -40.672 9.576   1.00 34.39 ? 370 ASP B OD1 1 
ATOM   6707 O  OD2 . ASP B 1 370 ? 23.464  -39.898 8.202   1.00 35.74 ? 370 ASP B OD2 1 
ATOM   6708 N  N   . VAL B 1 371 ? 21.381  -39.921 13.032  1.00 24.38 ? 371 VAL B N   1 
ATOM   6709 C  CA  . VAL B 1 371 ? 20.138  -39.110 13.268  1.00 24.18 ? 371 VAL B CA  1 
ATOM   6710 C  C   . VAL B 1 371 ? 20.466  -37.699 13.748  1.00 23.63 ? 371 VAL B C   1 
ATOM   6711 O  O   . VAL B 1 371 ? 19.633  -36.821 13.572  1.00 21.37 ? 371 VAL B O   1 
ATOM   6712 C  CB  . VAL B 1 371 ? 19.147  -39.755 14.263  1.00 26.36 ? 371 VAL B CB  1 
ATOM   6713 C  CG1 . VAL B 1 371 ? 18.568  -41.036 13.710  1.00 29.11 ? 371 VAL B CG1 1 
ATOM   6714 C  CG2 . VAL B 1 371 ? 19.737  -40.012 15.636  1.00 27.21 ? 371 VAL B CG2 1 
ATOM   6715 N  N   . GLU B 1 372 ? 21.602  -37.441 14.400  1.00 20.87 ? 372 GLU B N   1 
ATOM   6716 C  CA  . GLU B 1 372 ? 21.870  -36.083 14.925  1.00 20.72 ? 372 GLU B CA  1 
ATOM   6717 C  C   . GLU B 1 372 ? 22.483  -35.185 13.850  1.00 17.87 ? 372 GLU B C   1 
ATOM   6718 O  O   . GLU B 1 372 ? 22.584  -33.984 14.087  1.00 24.76 ? 372 GLU B O   1 
ATOM   6719 C  CB  . GLU B 1 372 ? 22.809  -36.133 16.141  1.00 24.42 ? 372 GLU B CB  1 
ATOM   6720 C  CG  . GLU B 1 372 ? 22.130  -36.645 17.388  1.00 25.32 ? 372 GLU B CG  1 
ATOM   6721 C  CD  . GLU B 1 372 ? 20.933  -35.849 17.920  1.00 30.34 ? 372 GLU B CD  1 
ATOM   6722 O  OE1 . GLU B 1 372 ? 20.899  -34.601 17.771  1.00 35.70 ? 372 GLU B OE1 1 
ATOM   6723 O  OE2 . GLU B 1 372 ? 20.052  -36.461 18.545  1.00 33.12 ? 372 GLU B OE2 1 
ATOM   6724 N  N   . GLU B 1 373 ? 22.879  -35.723 12.709  1.00 19.00 ? 373 GLU B N   1 
ATOM   6725 C  CA  . GLU B 1 373 ? 23.505  -34.951 11.621  1.00 21.31 ? 373 GLU B CA  1 
ATOM   6726 C  C   . GLU B 1 373 ? 22.420  -34.216 10.840  1.00 21.27 ? 373 GLU B C   1 
ATOM   6727 O  O   . GLU B 1 373 ? 21.333  -34.767 10.630  1.00 16.91 ? 373 GLU B O   1 
ATOM   6728 C  CB  . GLU B 1 373 ? 24.333  -35.839 10.709  1.00 25.76 ? 373 GLU B CB  1 
ATOM   6729 C  CG  . GLU B 1 373 ? 25.636  -36.239 11.386  1.00 30.65 ? 373 GLU B CG  1 
ATOM   6730 C  CD  . GLU B 1 373 ? 26.388  -37.346 10.680  1.00 38.91 ? 373 GLU B CD  1 
ATOM   6731 O  OE1 . GLU B 1 373 ? 26.455  -37.274 9.442   1.00 42.68 ? 373 GLU B OE1 1 
ATOM   6732 O  OE2 . GLU B 1 373 ? 26.903  -38.273 11.385  1.00 45.33 ? 373 GLU B OE2 1 
ATOM   6733 N  N   . PHE B 1 374 ? 22.720  -33.003 10.410  1.00 17.15 ? 374 PHE B N   1 
ATOM   6734 C  CA  . PHE B 1 374 ? 21.849  -32.180 9.543   1.00 17.00 ? 374 PHE B CA  1 
ATOM   6735 C  C   . PHE B 1 374 ? 22.143  -32.508 8.078   1.00 18.36 ? 374 PHE B C   1 
ATOM   6736 O  O   . PHE B 1 374 ? 23.220  -32.102 7.525   1.00 19.11 ? 374 PHE B O   1 
ATOM   6737 C  CB  . PHE B 1 374 ? 22.082  -30.710 9.814   1.00 15.30 ? 374 PHE B CB  1 
ATOM   6738 C  CG  . PHE B 1 374 ? 21.081  -29.838 9.133   1.00 16.31 ? 374 PHE B CG  1 
ATOM   6739 C  CD1 . PHE B 1 374 ? 19.838  -29.685 9.689   1.00 15.81 ? 374 PHE B CD1 1 
ATOM   6740 C  CD2 . PHE B 1 374 ? 21.366  -29.144 7.956   1.00 18.07 ? 374 PHE B CD2 1 
ATOM   6741 C  CE1 . PHE B 1 374 ? 18.853  -28.948 9.083   1.00 15.36 ? 374 PHE B CE1 1 
ATOM   6742 C  CE2 . PHE B 1 374 ? 20.375  -28.366 7.360   1.00 17.13 ? 374 PHE B CE2 1 
ATOM   6743 C  CZ  . PHE B 1 374 ? 19.127  -28.307 7.909   1.00 17.53 ? 374 PHE B CZ  1 
ATOM   6744 N  N   . ARG B 1 375 ? 21.288  -33.305 7.457   1.00 16.38 ? 375 ARG B N   1 
ATOM   6745 C  CA  . ARG B 1 375 ? 21.500  -33.820 6.083   1.00 17.73 ? 375 ARG B CA  1 
ATOM   6746 C  C   . ARG B 1 375 ? 20.202  -33.635 5.305   1.00 17.56 ? 375 ARG B C   1 
ATOM   6747 O  O   . ARG B 1 375 ? 19.358  -34.526 5.295   1.00 15.86 ? 375 ARG B O   1 
ATOM   6748 C  CB  . ARG B 1 375 ? 22.011  -35.263 6.145   1.00 20.18 ? 375 ARG B CB  1 
ATOM   6749 C  CG  . ARG B 1 375 ? 22.374  -35.872 4.799   1.00 28.08 ? 375 ARG B CG  1 
ATOM   6750 C  CD  . ARG B 1 375 ? 23.224  -37.159 4.935   1.00 33.84 ? 375 ARG B CD  1 
ATOM   6751 N  NE  . ARG B 1 375 ? 22.498  -38.331 5.459   1.00 40.29 ? 375 ARG B NE  1 
ATOM   6752 C  CZ  . ARG B 1 375 ? 21.619  -39.091 4.779   1.00 47.65 ? 375 ARG B CZ  1 
ATOM   6753 N  NH1 . ARG B 1 375 ? 21.332  -38.836 3.506   1.00 46.17 ? 375 ARG B NH1 1 
ATOM   6754 N  NH2 . ARG B 1 375 ? 21.030  -40.118 5.384   1.00 47.03 ? 375 ARG B NH2 1 
ATOM   6755 N  N   . PRO B 1 376 ? 19.987  -32.486 4.622   1.00 15.90 ? 376 PRO B N   1 
ATOM   6756 C  CA  . PRO B 1 376 ? 18.782  -32.242 3.822   1.00 15.43 ? 376 PRO B CA  1 
ATOM   6757 C  C   . PRO B 1 376 ? 18.488  -33.302 2.753   1.00 15.11 ? 376 PRO B C   1 
ATOM   6758 O  O   . PRO B 1 376 ? 17.314  -33.583 2.454   1.00 14.37 ? 376 PRO B O   1 
ATOM   6759 C  CB  . PRO B 1 376 ? 19.008  -30.857 3.223   1.00 15.83 ? 376 PRO B CB  1 
ATOM   6760 C  CG  . PRO B 1 376 ? 19.935  -30.202 4.224   1.00 17.92 ? 376 PRO B CG  1 
ATOM   6761 C  CD  . PRO B 1 376 ? 20.841  -31.299 4.732   1.00 16.43 ? 376 PRO B CD  1 
ATOM   6762 N  N   . GLU B 1 377 ? 19.524  -33.981 2.337   1.00 16.46 ? 377 GLU B N   1 
ATOM   6763 C  CA  . GLU B 1 377 ? 19.452  -35.020 1.271   1.00 18.02 ? 377 GLU B CA  1 
ATOM   6764 C  C   . GLU B 1 377 ? 18.567  -36.184 1.755   1.00 16.80 ? 377 GLU B C   1 
ATOM   6765 O  O   . GLU B 1 377 ? 18.073  -36.927 0.884   1.00 17.52 ? 377 GLU B O   1 
ATOM   6766 C  CB  . GLU B 1 377 ? 20.864  -35.422 0.839   1.00 19.33 ? 377 GLU B CB  1 
ATOM   6767 C  CG  . GLU B 1 377 ? 21.600  -34.263 0.136   1.00 23.85 ? 377 GLU B CG  1 
ATOM   6768 C  CD  . GLU B 1 377 ? 22.245  -33.227 1.074   1.00 25.62 ? 377 GLU B CD  1 
ATOM   6769 O  OE1 . GLU B 1 377 ? 22.336  -33.501 2.297   1.00 25.79 ? 377 GLU B OE1 1 
ATOM   6770 O  OE2 . GLU B 1 377 ? 22.720  -32.162 0.585   1.00 24.85 ? 377 GLU B OE2 1 
ATOM   6771 N  N   . ARG B 1 378 ? 18.276  -36.326 3.051   1.00 15.66 ? 378 ARG B N   1 
ATOM   6772 C  CA  . ARG B 1 378 ? 17.278  -37.330 3.531   1.00 16.04 ? 378 ARG B CA  1 
ATOM   6773 C  C   . ARG B 1 378 ? 15.940  -37.113 2.822   1.00 15.98 ? 378 ARG B C   1 
ATOM   6774 O  O   . ARG B 1 378 ? 15.109  -38.031 2.745   1.00 17.49 ? 378 ARG B O   1 
ATOM   6775 C  CB  . ARG B 1 378 ? 17.044  -37.236 5.049   1.00 15.25 ? 378 ARG B CB  1 
ATOM   6776 C  CG  . ARG B 1 378 ? 18.276  -37.504 5.875   1.00 16.64 ? 378 ARG B CG  1 
ATOM   6777 C  CD  . ARG B 1 378 ? 17.880  -37.335 7.319   1.00 17.08 ? 378 ARG B CD  1 
ATOM   6778 N  NE  . ARG B 1 378 ? 18.990  -36.948 8.161   1.00 19.01 ? 378 ARG B NE  1 
ATOM   6779 C  CZ  . ARG B 1 378 ? 19.833  -37.800 8.746   1.00 19.12 ? 378 ARG B CZ  1 
ATOM   6780 N  NH1 . ARG B 1 378 ? 19.656  -39.118 8.621   1.00 19.37 ? 378 ARG B NH1 1 
ATOM   6781 N  NH2 . ARG B 1 378 ? 20.825  -37.343 9.487   1.00 20.25 ? 378 ARG B NH2 1 
ATOM   6782 N  N   . PHE B 1 379 ? 15.660  -35.890 2.420   1.00 15.18 ? 379 PHE B N   1 
ATOM   6783 C  CA  . PHE B 1 379 ? 14.382  -35.438 1.829   1.00 14.63 ? 379 PHE B CA  1 
ATOM   6784 C  C   . PHE B 1 379 ? 14.458  -35.255 0.300   1.00 16.28 ? 379 PHE B C   1 
ATOM   6785 O  O   . PHE B 1 379 ? 13.564  -34.631 -0.220  1.00 17.98 ? 379 PHE B O   1 
ATOM   6786 C  CB  . PHE B 1 379 ? 13.905  -34.201 2.618   1.00 14.00 ? 379 PHE B CB  1 
ATOM   6787 C  CG  . PHE B 1 379 ? 13.499  -34.487 4.046   1.00 14.32 ? 379 PHE B CG  1 
ATOM   6788 C  CD1 . PHE B 1 379 ? 12.222  -34.959 4.328   1.00 15.40 ? 379 PHE B CD1 1 
ATOM   6789 C  CD2 . PHE B 1 379 ? 14.373  -34.335 5.098   1.00 14.58 ? 379 PHE B CD2 1 
ATOM   6790 C  CE1 . PHE B 1 379 ? 11.845  -35.227 5.644   1.00 14.21 ? 379 PHE B CE1 1 
ATOM   6791 C  CE2 . PHE B 1 379 ? 14.005  -34.648 6.393   1.00 15.37 ? 379 PHE B CE2 1 
ATOM   6792 C  CZ  . PHE B 1 379 ? 12.742  -35.087 6.672   1.00 15.53 ? 379 PHE B CZ  1 
ATOM   6793 N  N   . GLU B 1 380 ? 15.446  -35.850 -0.372  1.00 16.47 ? 380 GLU B N   1 
ATOM   6794 C  CA  . GLU B 1 380 ? 15.535  -35.787 -1.850  1.00 18.54 ? 380 GLU B CA  1 
ATOM   6795 C  C   . GLU B 1 380 ? 14.193  -36.245 -2.426  1.00 18.67 ? 380 GLU B C   1 
ATOM   6796 O  O   . GLU B 1 380 ? 13.699  -35.651 -3.341  1.00 19.83 ? 380 GLU B O   1 
ATOM   6797 C  CB  . GLU B 1 380 ? 16.671  -36.657 -2.383  1.00 23.10 ? 380 GLU B CB  1 
ATOM   6798 C  CG  . GLU B 1 380 ? 17.040  -36.297 -3.823  1.00 30.49 ? 380 GLU B CG  1 
ATOM   6799 C  CD  . GLU B 1 380 ? 17.755  -34.951 -3.962  1.00 32.50 ? 380 GLU B CD  1 
ATOM   6800 O  OE1 . GLU B 1 380 ? 18.874  -34.795 -3.358  1.00 42.56 ? 380 GLU B OE1 1 
ATOM   6801 O  OE2 . GLU B 1 380 ? 17.226  -34.066 -4.675  1.00 47.52 ? 380 GLU B OE2 1 
ATOM   6802 N  N   . ASN B 1 381 ? 13.676  -37.357 -1.924  1.00 16.67 ? 381 ASN B N   1 
ATOM   6803 C  CA  . ASN B 1 381 ? 12.365  -37.934 -2.282  1.00 18.17 ? 381 ASN B CA  1 
ATOM   6804 C  C   . ASN B 1 381 ? 11.593  -38.197 -1.006  1.00 19.10 ? 381 ASN B C   1 
ATOM   6805 O  O   . ASN B 1 381 ? 11.799  -39.206 -0.320  1.00 18.95 ? 381 ASN B O   1 
ATOM   6806 C  CB  . ASN B 1 381 ? 12.536  -39.223 -3.051  1.00 17.59 ? 381 ASN B CB  1 
ATOM   6807 C  CG  . ASN B 1 381 ? 11.197  -39.735 -3.528  1.00 19.39 ? 381 ASN B CG  1 
ATOM   6808 O  OD1 . ASN B 1 381 ? 10.173  -39.137 -3.214  1.00 19.55 ? 381 ASN B OD1 1 
ATOM   6809 N  ND2 . ASN B 1 381 ? 11.209  -40.847 -4.238  1.00 21.60 ? 381 ASN B ND2 1 
ATOM   6810 N  N   . PRO B 1 382 ? 10.790  -37.209 -0.564  1.00 21.94 ? 382 PRO B N   1 
ATOM   6811 C  CA  . PRO B 1 382 ? 10.050  -37.366 0.694   1.00 22.92 ? 382 PRO B CA  1 
ATOM   6812 C  C   . PRO B 1 382 ? 9.141   -38.597 0.724   1.00 23.01 ? 382 PRO B C   1 
ATOM   6813 O  O   . PRO B 1 382 ? 8.884   -39.117 1.801   1.00 24.31 ? 382 PRO B O   1 
ATOM   6814 C  CB  . PRO B 1 382 ? 9.251   -36.062 0.786   1.00 24.68 ? 382 PRO B CB  1 
ATOM   6815 C  CG  . PRO B 1 382 ? 10.100  -35.108 0.019   1.00 26.41 ? 382 PRO B CG  1 
ATOM   6816 C  CD  . PRO B 1 382 ? 10.636  -35.883 -1.180  1.00 24.93 ? 382 PRO B CD  1 
ATOM   6817 N  N   . SER B 1 383 ? 8.707   -39.081 -0.444  1.00 20.44 ? 383 SER B N   1 
ATOM   6818 C  CA  . SER B 1 383 ? 7.922   -40.341 -0.551  1.00 19.99 ? 383 SER B CA  1 
ATOM   6819 C  C   . SER B 1 383 ? 8.675   -41.575 0.032   1.00 19.03 ? 383 SER B C   1 
ATOM   6820 O  O   . SER B 1 383 ? 8.040   -42.548 0.441   1.00 17.68 ? 383 SER B O   1 
ATOM   6821 C  CB  . SER B 1 383 ? 7.446   -40.500 -2.018  1.00 21.10 ? 383 SER B CB  1 
ATOM   6822 O  OG  . SER B 1 383 ? 8.260   -41.355 -2.760  1.00 29.27 ? 383 SER B OG  1 
ATOM   6823 N  N   . ALA B 1 384 ? 10.017  -41.547 0.157   1.00 16.27 ? 384 ALA B N   1 
ATOM   6824 C  CA  . ALA B 1 384 ? 10.822  -42.621 0.733   1.00 16.15 ? 384 ALA B CA  1 
ATOM   6825 C  C   . ALA B 1 384 ? 10.668  -42.773 2.243   1.00 17.51 ? 384 ALA B C   1 
ATOM   6826 O  O   . ALA B 1 384 ? 10.995  -43.831 2.801   1.00 21.29 ? 384 ALA B O   1 
ATOM   6827 C  CB  . ALA B 1 384 ? 12.286  -42.412 0.436   1.00 17.06 ? 384 ALA B CB  1 
ATOM   6828 N  N   . ILE B 1 385 ? 10.086  -41.785 2.903   1.00 17.16 ? 385 ILE B N   1 
ATOM   6829 C  CA  . ILE B 1 385 ? 9.868   -41.869 4.352   1.00 17.55 ? 385 ILE B CA  1 
ATOM   6830 C  C   . ILE B 1 385 ? 8.636   -42.721 4.613   1.00 16.10 ? 385 ILE B C   1 
ATOM   6831 O  O   . ILE B 1 385 ? 7.559   -42.422 4.110   1.00 15.14 ? 385 ILE B O   1 
ATOM   6832 C  CB  . ILE B 1 385 ? 9.729   -40.450 4.900   1.00 19.23 ? 385 ILE B CB  1 
ATOM   6833 C  CG1 . ILE B 1 385 ? 10.970  -39.637 4.542   1.00 24.35 ? 385 ILE B CG1 1 
ATOM   6834 C  CG2 . ILE B 1 385 ? 9.471   -40.455 6.403   1.00 20.00 ? 385 ILE B CG2 1 
ATOM   6835 C  CD1 . ILE B 1 385 ? 10.737  -38.157 4.713   1.00 28.46 ? 385 ILE B CD1 1 
ATOM   6836 N  N   . PRO B 1 386 ? 8.714   -43.679 5.558   1.00 17.09 ? 386 PRO B N   1 
ATOM   6837 C  CA  . PRO B 1 386 ? 7.563   -44.503 5.918   1.00 16.98 ? 386 PRO B CA  1 
ATOM   6838 C  C   . PRO B 1 386 ? 6.424   -43.662 6.492   1.00 16.56 ? 386 PRO B C   1 
ATOM   6839 O  O   . PRO B 1 386 ? 6.631   -42.541 7.001   1.00 16.38 ? 386 PRO B O   1 
ATOM   6840 C  CB  . PRO B 1 386 ? 8.108   -45.463 6.999   1.00 17.73 ? 386 PRO B CB  1 
ATOM   6841 C  CG  . PRO B 1 386 ? 9.580   -45.476 6.736   1.00 20.52 ? 386 PRO B CG  1 
ATOM   6842 C  CD  . PRO B 1 386 ? 9.932   -44.091 6.241   1.00 19.41 ? 386 PRO B CD  1 
ATOM   6843 N  N   . GLN B 1 387 ? 5.223   -44.207 6.499   1.00 15.39 ? 387 GLN B N   1 
ATOM   6844 C  CA  . GLN B 1 387 ? 4.083   -43.519 7.126   1.00 15.32 ? 387 GLN B CA  1 
ATOM   6845 C  C   . GLN B 1 387 ? 4.374   -43.290 8.599   1.00 14.62 ? 387 GLN B C   1 
ATOM   6846 O  O   . GLN B 1 387 ? 4.935   -44.172 9.285   1.00 15.05 ? 387 GLN B O   1 
ATOM   6847 C  CB  . GLN B 1 387 ? 2.842   -44.405 7.026   1.00 20.31 ? 387 GLN B CB  1 
ATOM   6848 C  CG  . GLN B 1 387 ? 1.578   -43.638 7.022   1.00 27.09 ? 387 GLN B CG  1 
ATOM   6849 C  CD  . GLN B 1 387 ? 0.384   -44.340 6.429   1.00 25.91 ? 387 GLN B CD  1 
ATOM   6850 O  OE1 . GLN B 1 387 ? 0.241   -45.577 6.391   1.00 29.52 ? 387 GLN B OE1 1 
ATOM   6851 N  NE2 . GLN B 1 387 ? -0.541  -43.471 6.086   1.00 23.08 ? 387 GLN B NE2 1 
ATOM   6852 N  N   . HIS B 1 388 ? 3.934   -42.147 9.128   1.00 14.55 ? 388 HIS B N   1 
ATOM   6853 C  CA  . HIS B 1 388 ? 3.937   -41.838 10.580  1.00 13.89 ? 388 HIS B CA  1 
ATOM   6854 C  C   . HIS B 1 388 ? 5.367   -41.787 11.133  1.00 13.87 ? 388 HIS B C   1 
ATOM   6855 O  O   . HIS B 1 388 ? 5.535   -41.986 12.342  1.00 16.59 ? 388 HIS B O   1 
ATOM   6856 C  CB  . HIS B 1 388 ? 3.006   -42.779 11.327  1.00 13.78 ? 388 HIS B CB  1 
ATOM   6857 C  CG  . HIS B 1 388 ? 1.655   -42.825 10.712  1.00 13.69 ? 388 HIS B CG  1 
ATOM   6858 N  ND1 . HIS B 1 388 ? 1.004   -41.673 10.329  1.00 14.62 ? 388 HIS B ND1 1 
ATOM   6859 C  CD2 . HIS B 1 388 ? 0.846   -43.869 10.510  1.00 14.46 ? 388 HIS B CD2 1 
ATOM   6860 C  CE1 . HIS B 1 388 ? -0.196  -42.038 9.872   1.00 14.35 ? 388 HIS B CE1 1 
ATOM   6861 N  NE2 . HIS B 1 388 ? -0.321  -43.383 9.970   1.00 16.39 ? 388 HIS B NE2 1 
ATOM   6862 N  N   . ALA B 1 389 ? 6.341   -41.517 10.290  1.00 13.24 ? 389 ALA B N   1 
ATOM   6863 C  CA  . ALA B 1 389 ? 7.753   -41.413 10.727  1.00 12.84 ? 389 ALA B CA  1 
ATOM   6864 C  C   . ALA B 1 389 ? 8.208   -39.974 10.819  1.00 11.63 ? 389 ALA B C   1 
ATOM   6865 O  O   . ALA B 1 389 ? 9.151   -39.696 11.550  1.00 13.06 ? 389 ALA B O   1 
ATOM   6866 C  CB  . ALA B 1 389 ? 8.649   -42.157 9.765   1.00 13.05 ? 389 ALA B CB  1 
ATOM   6867 N  N   . PHE B 1 390 ? 7.605   -39.080 10.027  1.00 11.72 ? 390 PHE B N   1 
ATOM   6868 C  CA  . PHE B 1 390 ? 7.969   -37.656 9.981   1.00 11.41 ? 390 PHE B CA  1 
ATOM   6869 C  C   . PHE B 1 390 ? 6.679   -36.878 10.201  1.00 11.70 ? 390 PHE B C   1 
ATOM   6870 O  O   . PHE B 1 390 ? 5.806   -36.897 9.308   1.00 12.44 ? 390 PHE B O   1 
ATOM   6871 C  CB  . PHE B 1 390 ? 8.606   -37.305 8.647   1.00 11.76 ? 390 PHE B CB  1 
ATOM   6872 C  CG  . PHE B 1 390 ? 8.968   -35.859 8.479   1.00 11.73 ? 390 PHE B CG  1 
ATOM   6873 C  CD1 . PHE B 1 390 ? 9.908   -35.256 9.303   1.00 11.62 ? 390 PHE B CD1 1 
ATOM   6874 C  CD2 . PHE B 1 390 ? 8.461   -35.127 7.440   1.00 11.75 ? 390 PHE B CD2 1 
ATOM   6875 C  CE1 . PHE B 1 390 ? 10.277  -33.953 9.115   1.00 11.84 ? 390 PHE B CE1 1 
ATOM   6876 C  CE2 . PHE B 1 390 ? 8.836   -33.798 7.237   1.00 11.76 ? 390 PHE B CE2 1 
ATOM   6877 C  CZ  . PHE B 1 390 ? 9.738   -33.207 8.111   1.00 12.31 ? 390 PHE B CZ  1 
ATOM   6878 N  N   . LYS B 1 391 ? 6.472   -36.345 11.398  1.00 10.97 ? 391 LYS B N   1 
ATOM   6879 C  CA  . LYS B 1 391 ? 5.139   -35.853 11.771  1.00 11.35 ? 391 LYS B CA  1 
ATOM   6880 C  C   . LYS B 1 391 ? 5.174   -34.451 12.374  1.00 9.81  ? 391 LYS B C   1 
ATOM   6881 O  O   . LYS B 1 391 ? 4.519   -34.190 13.378  1.00 10.31 ? 391 LYS B O   1 
ATOM   6882 C  CB  . LYS B 1 391 ? 4.446   -36.844 12.706  1.00 12.09 ? 391 LYS B CB  1 
ATOM   6883 C  CG  . LYS B 1 391 ? 4.250   -38.200 12.070  1.00 12.79 ? 391 LYS B CG  1 
ATOM   6884 C  CD  . LYS B 1 391 ? 3.291   -38.220 10.946  1.00 15.42 ? 391 LYS B CD  1 
ATOM   6885 C  CE  . LYS B 1 391 ? 1.872   -38.410 11.430  1.00 16.77 ? 391 LYS B CE  1 
ATOM   6886 N  NZ  . LYS B 1 391 ? 1.043   -38.701 10.245  1.00 16.73 ? 391 LYS B NZ  1 
ATOM   6887 N  N   . PRO B 1 392 ? 5.918   -33.470 11.794  1.00 9.91  ? 392 PRO B N   1 
ATOM   6888 C  CA  . PRO B 1 392 ? 5.974   -32.153 12.388  1.00 9.56  ? 392 PRO B CA  1 
ATOM   6889 C  C   . PRO B 1 392 ? 4.660   -31.392 12.319  1.00 9.32  ? 392 PRO B C   1 
ATOM   6890 O  O   . PRO B 1 392 ? 4.536   -30.345 12.945  1.00 9.89  ? 392 PRO B O   1 
ATOM   6891 C  CB  . PRO B 1 392 ? 7.082   -31.457 11.561  1.00 10.63 ? 392 PRO B CB  1 
ATOM   6892 C  CG  . PRO B 1 392 ? 6.966   -32.105 10.231  1.00 10.81 ? 392 PRO B CG  1 
ATOM   6893 C  CD  . PRO B 1 392 ? 6.664   -33.548 10.533  1.00 11.17 ? 392 PRO B CD  1 
ATOM   6894 N  N   . PHE B 1 393 ? 3.737   -31.844 11.459  1.00 10.21 ? 393 PHE B N   1 
ATOM   6895 C  CA  . PHE B 1 393 ? 2.399   -31.179 11.330  1.00 10.41 ? 393 PHE B CA  1 
ATOM   6896 C  C   . PHE B 1 393 ? 1.272   -32.026 11.883  1.00 10.67 ? 393 PHE B C   1 
ATOM   6897 O  O   . PHE B 1 393 ? 0.121   -31.749 11.552  1.00 11.58 ? 393 PHE B O   1 
ATOM   6898 C  CB  . PHE B 1 393 ? 2.185   -30.801 9.859   1.00 10.71 ? 393 PHE B CB  1 
ATOM   6899 C  CG  . PHE B 1 393 ? 3.163   -29.782 9.339   1.00 11.03 ? 393 PHE B CG  1 
ATOM   6900 C  CD1 . PHE B 1 393 ? 3.057   -28.443 9.697   1.00 11.26 ? 393 PHE B CD1 1 
ATOM   6901 C  CD2 . PHE B 1 393 ? 4.207   -30.175 8.525   1.00 11.57 ? 393 PHE B CD2 1 
ATOM   6902 C  CE1 . PHE B 1 393 ? 3.985   -27.510 9.227   1.00 11.70 ? 393 PHE B CE1 1 
ATOM   6903 C  CE2 . PHE B 1 393 ? 5.137   -29.242 8.083   1.00 12.09 ? 393 PHE B CE2 1 
ATOM   6904 C  CZ  . PHE B 1 393 ? 5.024   -27.935 8.433   1.00 11.64 ? 393 PHE B CZ  1 
ATOM   6905 N  N   . GLY B 1 394 ? 1.560   -32.961 12.779  1.00 10.31 ? 394 GLY B N   1 
ATOM   6906 C  CA  . GLY B 1 394 ? 0.515   -33.778 13.388  1.00 10.42 ? 394 GLY B CA  1 
ATOM   6907 C  C   . GLY B 1 394 ? 0.004   -34.839 12.465  1.00 11.75 ? 394 GLY B C   1 
ATOM   6908 O  O   . GLY B 1 394 ? 0.713   -35.285 11.568  1.00 12.29 ? 394 GLY B O   1 
ATOM   6909 N  N   . ASN B 1 395 ? -1.271  -35.207 12.659  1.00 11.21 ? 395 ASN B N   1 
ATOM   6910 C  CA  . ASN B 1 395 ? -1.792  -36.428 12.024  1.00 11.19 ? 395 ASN B CA  1 
ATOM   6911 C  C   . ASN B 1 395 ? -3.213  -36.282 11.498  1.00 11.68 ? 395 ASN B C   1 
ATOM   6912 O  O   . ASN B 1 395 ? -4.084  -35.841 12.232  1.00 12.03 ? 395 ASN B O   1 
ATOM   6913 C  CB  . ASN B 1 395 ? -1.758  -37.589 13.007  1.00 12.01 ? 395 ASN B CB  1 
ATOM   6914 C  CG  . ASN B 1 395 ? -2.158  -38.872 12.324  1.00 11.23 ? 395 ASN B CG  1 
ATOM   6915 O  OD1 . ASN B 1 395 ? -1.491  -39.335 11.400  1.00 12.05 ? 395 ASN B OD1 1 
ATOM   6916 N  ND2 . ASN B 1 395 ? -3.256  -39.476 12.803  1.00 12.68 ? 395 ASN B ND2 1 
ATOM   6917 N  N   . GLY B 1 396 ? -3.436  -36.861 10.324  1.00 11.23 ? 396 GLY B N   1 
ATOM   6918 C  CA  . GLY B 1 396 ? -4.774  -37.150 9.793   1.00 12.38 ? 396 GLY B CA  1 
ATOM   6919 C  C   . GLY B 1 396 ? -5.645  -35.918 9.697   1.00 11.22 ? 396 GLY B C   1 
ATOM   6920 O  O   . GLY B 1 396 ? -5.166  -34.842 9.268   1.00 11.62 ? 396 GLY B O   1 
ATOM   6921 N  N   . GLN B 1 397 ? -6.914  -36.077 10.059  1.00 11.27 ? 397 GLN B N   1 
ATOM   6922 C  CA  . GLN B 1 397 ? -7.860  -34.954 9.852   1.00 10.96 ? 397 GLN B CA  1 
ATOM   6923 C  C   . GLN B 1 397 ? -7.582  -33.840 10.841  1.00 11.26 ? 397 GLN B C   1 
ATOM   6924 O  O   . GLN B 1 397 ? -8.014  -32.711 10.591  1.00 11.89 ? 397 GLN B O   1 
ATOM   6925 C  CB  . GLN B 1 397 ? -9.327  -35.389 9.909   1.00 11.02 ? 397 GLN B CB  1 
ATOM   6926 C  CG  . GLN B 1 397 ? -9.799  -35.776 11.276  1.00 12.02 ? 397 GLN B CG  1 
ATOM   6927 C  CD  . GLN B 1 397 ? -11.165 -36.442 11.257  1.00 13.93 ? 397 GLN B CD  1 
ATOM   6928 O  OE1 . GLN B 1 397 ? -12.016 -36.144 10.415  1.00 16.56 ? 397 GLN B OE1 1 
ATOM   6929 N  NE2 . GLN B 1 397 ? -11.402 -37.274 12.249  1.00 16.43 ? 397 GLN B NE2 1 
ATOM   6930 N  N   . ARG B 1 398 ? -6.827  -34.117 11.895  1.00 10.69 ? 398 ARG B N   1 
ATOM   6931 C  CA  . ARG B 1 398 ? -6.419  -33.099 12.867  1.00 9.91  ? 398 ARG B CA  1 
ATOM   6932 C  C   . ARG B 1 398 ? -4.984  -32.614 12.593  1.00 10.00 ? 398 ARG B C   1 
ATOM   6933 O  O   . ARG B 1 398 ? -4.384  -32.009 13.495  1.00 10.90 ? 398 ARG B O   1 
ATOM   6934 C  CB  . ARG B 1 398 ? -6.573  -33.620 14.291  1.00 10.64 ? 398 ARG B CB  1 
ATOM   6935 C  CG  . ARG B 1 398 ? -7.999  -34.052 14.614  1.00 10.47 ? 398 ARG B CG  1 
ATOM   6936 C  CD  . ARG B 1 398 ? -9.017  -32.970 14.416  1.00 10.88 ? 398 ARG B CD  1 
ATOM   6937 N  NE  . ARG B 1 398 ? -8.737  -31.752 15.098  1.00 10.84 ? 398 ARG B NE  1 
ATOM   6938 C  CZ  . ARG B 1 398 ? -9.136  -31.392 16.308  1.00 11.50 ? 398 ARG B CZ  1 
ATOM   6939 N  NH1 . ARG B 1 398 ? -9.889  -32.187 17.049  1.00 11.32 ? 398 ARG B NH1 1 
ATOM   6940 N  NH2 . ARG B 1 398 ? -8.844  -30.194 16.763  1.00 11.93 ? 398 ARG B NH2 1 
ATOM   6941 N  N   . ALA B 1 399 ? -4.436  -32.854 11.414  1.00 9.99  ? 399 ALA B N   1 
ATOM   6942 C  CA  . ALA B 1 399 ? -3.139  -32.271 11.049  1.00 10.14 ? 399 ALA B CA  1 
ATOM   6943 C  C   . ALA B 1 399 ? -3.240  -30.768 10.837  1.00 10.95 ? 399 ALA B C   1 
ATOM   6944 O  O   . ALA B 1 399 ? -4.332  -30.191 10.712  1.00 11.51 ? 399 ALA B O   1 
ATOM   6945 C  CB  . ALA B 1 399 ? -2.646  -32.913 9.780   1.00 11.28 ? 399 ALA B CB  1 
ATOM   6946 N  N   . CYS B 1 400 ? -2.095  -30.137 10.873  1.00 10.44 ? 400 CYS B N   1 
ATOM   6947 C  CA  . CYS B 1 400 ? -1.996  -28.677 10.727  1.00 11.02 ? 400 CYS B CA  1 
ATOM   6948 C  C   . CYS B 1 400 ? -2.695  -28.179 9.493   1.00 10.78 ? 400 CYS B C   1 
ATOM   6949 O  O   . CYS B 1 400 ? -2.300  -28.521 8.380   1.00 12.69 ? 400 CYS B O   1 
ATOM   6950 C  CB  . CYS B 1 400 ? -0.542  -28.314 10.689  1.00 11.31 ? 400 CYS B CB  1 
ATOM   6951 S  SG  . CYS B 1 400 ? -0.271  -26.536 10.514  1.00 12.85 ? 400 CYS B SG  1 
ATOM   6952 N  N   . ILE B 1 401 ? -3.654  -27.279 9.650   1.00 10.88 ? 401 ILE B N   1 
ATOM   6953 C  CA  . ILE B 1 401 ? -4.317  -26.699 8.446   1.00 11.86 ? 401 ILE B CA  1 
ATOM   6954 C  C   . ILE B 1 401 ? -3.356  -25.745 7.728   1.00 11.46 ? 401 ILE B C   1 
ATOM   6955 O  O   . ILE B 1 401 ? -3.563  -25.537 6.491   1.00 13.51 ? 401 ILE B O   1 
ATOM   6956 C  CB  . ILE B 1 401 ? -5.649  -26.028 8.814   1.00 12.98 ? 401 ILE B CB  1 
ATOM   6957 C  CG1 . ILE B 1 401 ? -6.542  -25.892 7.595   1.00 12.78 ? 401 ILE B CG1 1 
ATOM   6958 C  CG2 . ILE B 1 401 ? -5.414  -24.703 9.485   1.00 13.68 ? 401 ILE B CG2 1 
ATOM   6959 C  CD1 . ILE B 1 401 ? -7.964  -25.444 7.872   1.00 13.66 ? 401 ILE B CD1 1 
ATOM   6960 N  N   . GLY B 1 402 ? -2.403  -25.194 8.457   1.00 12.57 ? 402 GLY B N   1 
ATOM   6961 C  CA  . GLY B 1 402 ? -1.488  -24.160 7.923   1.00 12.50 ? 402 GLY B CA  1 
ATOM   6962 C  C   . GLY B 1 402 ? -0.227  -24.731 7.314   1.00 13.06 ? 402 GLY B C   1 
ATOM   6963 O  O   . GLY B 1 402 ? 0.661   -23.914 7.014   1.00 12.98 ? 402 GLY B O   1 
ATOM   6964 N  N   . GLN B 1 403 ? -0.109  -26.029 7.090   1.00 11.97 ? 403 GLN B N   1 
ATOM   6965 C  CA  . GLN B 1 403 ? 1.179   -26.615 6.677   1.00 12.49 ? 403 GLN B CA  1 
ATOM   6966 C  C   . GLN B 1 403 ? 1.676   -25.984 5.360   1.00 12.14 ? 403 GLN B C   1 
ATOM   6967 O  O   . GLN B 1 403 ? 2.885   -25.647 5.232   1.00 12.48 ? 403 GLN B O   1 
ATOM   6968 C  CB  . GLN B 1 403 ? 1.032   -28.132 6.514   1.00 12.63 ? 403 GLN B CB  1 
ATOM   6969 C  CG  . GLN B 1 403 ? 2.257   -28.776 5.883   1.00 14.09 ? 403 GLN B CG  1 
ATOM   6970 C  CD  . GLN B 1 403 ? 2.191   -30.268 5.771   1.00 17.48 ? 403 GLN B CD  1 
ATOM   6971 O  OE1 . GLN B 1 403 ? 1.354   -30.950 6.353   1.00 17.57 ? 403 GLN B OE1 1 
ATOM   6972 N  NE2 . GLN B 1 403 ? 3.138   -30.817 5.022   1.00 20.65 ? 403 GLN B NE2 1 
ATOM   6973 N  N   . GLN B 1 404 ? 0.827   -25.927 4.351   1.00 12.97 ? 404 GLN B N   1 
ATOM   6974 C  CA  . GLN B 1 404 ? 1.237   -25.319 3.054   1.00 14.77 ? 404 GLN B CA  1 
ATOM   6975 C  C   . GLN B 1 404 ? 1.539   -23.831 3.186   1.00 13.54 ? 404 GLN B C   1 
ATOM   6976 O  O   . GLN B 1 404 ? 2.561   -23.390 2.596   1.00 13.30 ? 404 GLN B O   1 
ATOM   6977 C  CB  . GLN B 1 404 ? 0.155   -25.436 1.987   1.00 17.78 ? 404 GLN B CB  1 
ATOM   6978 C  CG  . GLN B 1 404 ? -0.470  -26.783 1.841   1.00 24.95 ? 404 GLN B CG  1 
ATOM   6979 C  CD  . GLN B 1 404 ? 0.569   -27.842 1.691   1.00 28.83 ? 404 GLN B CD  1 
ATOM   6980 O  OE1 . GLN B 1 404 ? 1.489   -27.720 0.881   1.00 35.33 ? 404 GLN B OE1 1 
ATOM   6981 N  NE2 . GLN B 1 404 ? 0.432   -28.880 2.505   1.00 35.35 ? 404 GLN B NE2 1 
ATOM   6982 N  N   . PHE B 1 405 ? 0.807   -23.083 3.970   1.00 12.70 ? 405 PHE B N   1 
ATOM   6983 C  CA  . PHE B 1 405 ? 1.036   -21.655 4.229   1.00 13.23 ? 405 PHE B CA  1 
ATOM   6984 C  C   . PHE B 1 405 ? 2.403   -21.482 4.874   1.00 13.67 ? 405 PHE B C   1 
ATOM   6985 O  O   . PHE B 1 405 ? 3.239   -20.678 4.427   1.00 14.00 ? 405 PHE B O   1 
ATOM   6986 C  CB  . PHE B 1 405 ? -0.091  -21.147 5.113   1.00 13.01 ? 405 PHE B CB  1 
ATOM   6987 C  CG  . PHE B 1 405 ? -0.080  -19.667 5.377   1.00 14.83 ? 405 PHE B CG  1 
ATOM   6988 C  CD1 . PHE B 1 405 ? 0.774   -19.083 6.296   1.00 14.88 ? 405 PHE B CD1 1 
ATOM   6989 C  CD2 . PHE B 1 405 ? -0.935  -18.841 4.636   1.00 15.23 ? 405 PHE B CD2 1 
ATOM   6990 C  CE1 . PHE B 1 405 ? 0.751   -17.710 6.517   1.00 15.19 ? 405 PHE B CE1 1 
ATOM   6991 C  CE2 . PHE B 1 405 ? -0.974  -17.480 4.887   1.00 15.42 ? 405 PHE B CE2 1 
ATOM   6992 C  CZ  . PHE B 1 405 ? -0.125  -16.914 5.805   1.00 15.32 ? 405 PHE B CZ  1 
ATOM   6993 N  N   . ALA B 1 406 ? 2.672   -22.251 5.915   1.00 12.18 ? 406 ALA B N   1 
ATOM   6994 C  CA  . ALA B 1 406 ? 3.923   -22.093 6.680   1.00 12.26 ? 406 ALA B CA  1 
ATOM   6995 C  C   . ALA B 1 406 ? 5.107   -22.448 5.770   1.00 11.81 ? 406 ALA B C   1 
ATOM   6996 O  O   . ALA B 1 406 ? 6.160   -21.752 5.799   1.00 11.54 ? 406 ALA B O   1 
ATOM   6997 C  CB  . ALA B 1 406 ? 3.867   -22.961 7.909   1.00 13.27 ? 406 ALA B CB  1 
ATOM   6998 N  N   . LEU B 1 407 ? 5.010   -23.535 5.016   1.00 11.86 ? 407 LEU B N   1 
ATOM   6999 C  CA  . LEU B 1 407 ? 6.141   -23.965 4.163   1.00 11.73 ? 407 LEU B CA  1 
ATOM   7000 C  C   . LEU B 1 407 ? 6.320   -22.988 3.004   1.00 12.88 ? 407 LEU B C   1 
ATOM   7001 O  O   . LEU B 1 407 ? 7.483   -22.755 2.617   1.00 12.83 ? 407 LEU B O   1 
ATOM   7002 C  CB  . LEU B 1 407 ? 5.983   -25.406 3.722   1.00 12.70 ? 407 LEU B CB  1 
ATOM   7003 C  CG  . LEU B 1 407 ? 6.112   -26.440 4.838   1.00 14.79 ? 407 LEU B CG  1 
ATOM   7004 C  CD1 . LEU B 1 407 ? 5.800   -27.809 4.298   1.00 16.32 ? 407 LEU B CD1 1 
ATOM   7005 C  CD2 . LEU B 1 407 ? 7.486   -26.421 5.499   1.00 15.89 ? 407 LEU B CD2 1 
ATOM   7006 N  N   . HIS B 1 408 ? 5.248   -22.414 2.489   1.00 11.98 ? 408 HIS B N   1 
ATOM   7007 C  CA  . HIS B 1 408 ? 5.413   -21.436 1.393   1.00 12.52 ? 408 HIS B CA  1 
ATOM   7008 C  C   . HIS B 1 408 ? 6.124   -20.219 1.963   1.00 12.77 ? 408 HIS B C   1 
ATOM   7009 O  O   . HIS B 1 408 ? 7.097   -19.681 1.309   1.00 13.37 ? 408 HIS B O   1 
ATOM   7010 C  CB  . HIS B 1 408 ? 4.075   -21.105 0.745   1.00 11.90 ? 408 HIS B CB  1 
ATOM   7011 C  CG  . HIS B 1 408 ? 4.249   -20.327 -0.510  1.00 12.30 ? 408 HIS B CG  1 
ATOM   7012 N  ND1 . HIS B 1 408 ? 4.561   -20.970 -1.668  1.00 14.58 ? 408 HIS B ND1 1 
ATOM   7013 C  CD2 . HIS B 1 408 ? 4.167   -19.010 -0.758  1.00 13.02 ? 408 HIS B CD2 1 
ATOM   7014 C  CE1 . HIS B 1 408 ? 4.653   -20.020 -2.621  1.00 14.33 ? 408 HIS B CE1 1 
ATOM   7015 N  NE2 . HIS B 1 408 ? 4.408   -18.830 -2.119  1.00 13.40 ? 408 HIS B NE2 1 
ATOM   7016 N  N   . GLU B 1 409 ? 5.608   -19.635 3.037   1.00 13.00 ? 409 GLU B N   1 
ATOM   7017 C  CA  . GLU B 1 409 ? 6.244   -18.452 3.656   1.00 13.38 ? 409 GLU B CA  1 
ATOM   7018 C  C   . GLU B 1 409 ? 7.710   -18.741 3.970   1.00 12.68 ? 409 GLU B C   1 
ATOM   7019 O  O   . GLU B 1 409 ? 8.586   -17.921 3.695   1.00 12.39 ? 409 GLU B O   1 
ATOM   7020 C  CB  . GLU B 1 409 ? 5.527   -18.082 4.965   1.00 15.17 ? 409 GLU B CB  1 
ATOM   7021 C  CG  . GLU B 1 409 ? 6.191   -16.900 5.647   1.00 19.85 ? 409 GLU B CG  1 
ATOM   7022 C  CD  . GLU B 1 409 ? 5.534   -16.363 6.897   1.00 25.86 ? 409 GLU B CD  1 
ATOM   7023 O  OE1 . GLU B 1 409 ? 4.663   -17.058 7.489   1.00 29.48 ? 409 GLU B OE1 1 
ATOM   7024 O  OE2 . GLU B 1 409 ? 5.908   -15.214 7.244   1.00 29.97 ? 409 GLU B OE2 1 
ATOM   7025 N  N   . ALA B 1 410 ? 7.996   -19.857 4.640   1.00 11.71 ? 410 ALA B N   1 
ATOM   7026 C  CA  . ALA B 1 410 ? 9.374   -20.150 5.088   1.00 12.00 ? 410 ALA B CA  1 
ATOM   7027 C  C   . ALA B 1 410 ? 10.286  -20.355 3.880   1.00 11.24 ? 410 ALA B C   1 
ATOM   7028 O  O   . ALA B 1 410 ? 11.461  -19.894 3.864   1.00 12.39 ? 410 ALA B O   1 
ATOM   7029 C  CB  . ALA B 1 410 ? 9.376   -21.340 5.997   1.00 12.46 ? 410 ALA B CB  1 
ATOM   7030 N  N   . THR B 1 411 ? 9.796   -20.976 2.797   1.00 11.44 ? 411 THR B N   1 
ATOM   7031 C  CA  . THR B 1 411 ? 10.653  -21.184 1.611   1.00 11.50 ? 411 THR B CA  1 
ATOM   7032 C  C   . THR B 1 411 ? 10.918  -19.843 0.896   1.00 10.96 ? 411 THR B C   1 
ATOM   7033 O  O   . THR B 1 411 ? 12.050  -19.588 0.478   1.00 11.62 ? 411 THR B O   1 
ATOM   7034 C  CB  . THR B 1 411 ? 9.989   -22.181 0.664   1.00 11.58 ? 411 THR B CB  1 
ATOM   7035 O  OG1 . THR B 1 411 ? 9.673   -23.414 1.335   1.00 11.72 ? 411 THR B OG1 1 
ATOM   7036 C  CG2 . THR B 1 411 ? 10.880  -22.521 -0.512  1.00 12.50 ? 411 THR B CG2 1 
ATOM   7037 N  N   . LEU B 1 412 ? 9.891   -19.013 0.770   1.00 11.54 ? 412 LEU B N   1 
ATOM   7038 C  CA  . LEU B 1 412 ? 10.043  -17.664 0.166   1.00 12.58 ? 412 LEU B CA  1 
ATOM   7039 C  C   . LEU B 1 412 ? 11.103  -16.874 0.933   1.00 12.35 ? 412 LEU B C   1 
ATOM   7040 O  O   . LEU B 1 412 ? 12.070  -16.364 0.333   1.00 12.52 ? 412 LEU B O   1 
ATOM   7041 C  CB  . LEU B 1 412 ? 8.684   -16.954 0.226   1.00 12.90 ? 412 LEU B CB  1 
ATOM   7042 C  CG  . LEU B 1 412 ? 8.743   -15.464 -0.086  1.00 14.74 ? 412 LEU B CG  1 
ATOM   7043 C  CD1 . LEU B 1 412 ? 9.128   -15.303 -1.539  1.00 16.96 ? 412 LEU B CD1 1 
ATOM   7044 C  CD2 . LEU B 1 412 ? 7.402   -14.822 0.242   1.00 18.75 ? 412 LEU B CD2 1 
ATOM   7045 N  N   . VAL B 1 413 ? 10.938  -16.783 2.227   1.00 11.71 ? 413 VAL B N   1 
ATOM   7046 C  CA  . VAL B 1 413 ? 11.800  -15.928 3.097   1.00 13.84 ? 413 VAL B CA  1 
ATOM   7047 C  C   . VAL B 1 413 ? 13.212  -16.506 3.094   1.00 12.06 ? 413 VAL B C   1 
ATOM   7048 O  O   . VAL B 1 413 ? 14.174  -15.728 2.929   1.00 12.31 ? 413 VAL B O   1 
ATOM   7049 C  CB  . VAL B 1 413 ? 11.225  -15.869 4.516   1.00 16.13 ? 413 VAL B CB  1 
ATOM   7050 C  CG1 . VAL B 1 413 ? 12.200  -15.283 5.513   1.00 17.99 ? 413 VAL B CG1 1 
ATOM   7051 C  CG2 . VAL B 1 413 ? 9.898   -15.126 4.548   1.00 18.14 ? 413 VAL B CG2 1 
ATOM   7052 N  N   . LEU B 1 414 ? 13.383  -17.784 3.302   1.00 11.58 ? 414 LEU B N   1 
ATOM   7053 C  CA  . LEU B 1 414 ? 14.752  -18.354 3.358   1.00 12.08 ? 414 LEU B CA  1 
ATOM   7054 C  C   . LEU B 1 414 ? 15.391  -18.225 1.969   1.00 12.67 ? 414 LEU B C   1 
ATOM   7055 O  O   . LEU B 1 414 ? 16.584  -17.889 1.898   1.00 12.10 ? 414 LEU B O   1 
ATOM   7056 C  CB  . LEU B 1 414 ? 14.648  -19.789 3.901   1.00 14.80 ? 414 LEU B CB  1 
ATOM   7057 C  CG  . LEU B 1 414 ? 15.969  -20.468 4.155   1.00 14.98 ? 414 LEU B CG  1 
ATOM   7058 C  CD1 . LEU B 1 414 ? 16.839  -19.639 5.090   1.00 15.55 ? 414 LEU B CD1 1 
ATOM   7059 C  CD2 . LEU B 1 414 ? 15.738  -21.858 4.704   1.00 15.92 ? 414 LEU B CD2 1 
ATOM   7060 N  N   . GLY B 1 415 ? 14.633  -18.405 0.885   1.00 12.22 ? 415 GLY B N   1 
ATOM   7061 C  CA  . GLY B 1 415 ? 15.223  -18.209 -0.454  1.00 13.28 ? 415 GLY B CA  1 
ATOM   7062 C  C   . GLY B 1 415 ? 15.701  -16.786 -0.636  1.00 12.12 ? 415 GLY B C   1 
ATOM   7063 O  O   . GLY B 1 415 ? 16.834  -16.561 -1.169  1.00 12.40 ? 415 GLY B O   1 
ATOM   7064 N  N   . MET B 1 416 ? 14.905  -15.806 -0.204  1.00 11.73 ? 416 MET B N   1 
ATOM   7065 C  CA  . MET B 1 416 ? 15.326  -14.387 -0.346  1.00 12.85 ? 416 MET B CA  1 
ATOM   7066 C  C   . MET B 1 416 ? 16.542  -14.128 0.539   1.00 12.86 ? 416 MET B C   1 
ATOM   7067 O  O   . MET B 1 416 ? 17.464  -13.398 0.107   1.00 13.19 ? 416 MET B O   1 
ATOM   7068 C  CB  . MET B 1 416 ? 14.185  -13.446 -0.007  1.00 13.60 ? 416 MET B CB  1 
ATOM   7069 C  CG  . MET B 1 416 ? 13.110  -13.474 -1.069  1.00 13.67 ? 416 MET B CG  1 
ATOM   7070 S  SD  . MET B 1 416 ? 11.780  -12.324 -0.768  1.00 19.70 ? 416 MET B SD  1 
ATOM   7071 C  CE  . MET B 1 416 ? 12.576  -10.799 -1.248  1.00 23.04 ? 416 MET B CE  1 
ATOM   7072 N  N   . MET B 1 417 ? 16.561  -14.641 1.762   1.00 11.64 ? 417 MET B N   1 
ATOM   7073 C  CA  . MET B 1 417 ? 17.694  -14.412 2.672   1.00 13.06 ? 417 MET B CA  1 
ATOM   7074 C  C   . MET B 1 417 ? 18.945  -14.951 1.986   1.00 13.32 ? 417 MET B C   1 
ATOM   7075 O  O   . MET B 1 417 ? 19.993  -14.256 2.005   1.00 14.41 ? 417 MET B O   1 
ATOM   7076 C  CB  . MET B 1 417 ? 17.463  -15.119 4.003   1.00 13.57 ? 417 MET B CB  1 
ATOM   7077 C  CG  . MET B 1 417 ? 16.410  -14.505 4.851   1.00 15.26 ? 417 MET B CG  1 
ATOM   7078 S  SD  . MET B 1 417 ? 15.856  -15.546 6.239   1.00 18.74 ? 417 MET B SD  1 
ATOM   7079 C  CE  . MET B 1 417 ? 17.397  -16.207 6.883   1.00 19.18 ? 417 MET B CE  1 
ATOM   7080 N  N   . LEU B 1 418 ? 18.858  -16.134 1.376   1.00 13.54 ? 418 LEU B N   1 
ATOM   7081 C  CA  . LEU B 1 418 ? 20.033  -16.781 0.789   1.00 13.81 ? 418 LEU B CA  1 
ATOM   7082 C  C   . LEU B 1 418 ? 20.472  -16.111 -0.512  1.00 12.95 ? 418 LEU B C   1 
ATOM   7083 O  O   . LEU B 1 418 ? 21.645  -16.192 -0.872  1.00 14.17 ? 418 LEU B O   1 
ATOM   7084 C  CB  . LEU B 1 418 ? 19.677  -18.238 0.525   1.00 15.92 ? 418 LEU B CB  1 
ATOM   7085 C  CG  . LEU B 1 418 ? 19.585  -19.110 1.778   1.00 17.02 ? 418 LEU B CG  1 
ATOM   7086 C  CD1 . LEU B 1 418 ? 18.905  -20.395 1.412   1.00 19.90 ? 418 LEU B CD1 1 
ATOM   7087 C  CD2 . LEU B 1 418 ? 20.950  -19.394 2.371   1.00 22.28 ? 418 LEU B CD2 1 
ATOM   7088 N  N   . LYS B 1 419 ? 19.536  -15.517 -1.228  1.00 12.23 ? 419 LYS B N   1 
ATOM   7089 C  CA  . LYS B 1 419 ? 19.849  -14.732 -2.448  1.00 13.67 ? 419 LYS B CA  1 
ATOM   7090 C  C   . LYS B 1 419 ? 20.604  -13.480 -2.064  1.00 13.44 ? 419 LYS B C   1 
ATOM   7091 O  O   . LYS B 1 419 ? 21.576  -13.114 -2.765  1.00 15.15 ? 419 LYS B O   1 
ATOM   7092 C  CB  . LYS B 1 419 ? 18.575  -14.334 -3.179  1.00 13.62 ? 419 LYS B CB  1 
ATOM   7093 C  CG  . LYS B 1 419 ? 18.819  -13.422 -4.368  1.00 15.56 ? 419 LYS B CG  1 
ATOM   7094 C  CD  . LYS B 1 419 ? 17.554  -13.137 -5.101  1.00 15.90 ? 419 LYS B CD  1 
ATOM   7095 C  CE  . LYS B 1 419 ? 17.774  -12.152 -6.216  1.00 19.50 ? 419 LYS B CE  1 
ATOM   7096 N  NZ  . LYS B 1 419 ? 16.526  -11.881 -6.969  1.00 20.24 ? 419 LYS B NZ  1 
ATOM   7097 N  N   . HIS B 1 420 ? 20.180  -12.807 -0.995  1.00 11.65 ? 420 HIS B N   1 
ATOM   7098 C  CA  . HIS B 1 420 ? 20.565  -11.389 -0.728  1.00 12.18 ? 420 HIS B CA  1 
ATOM   7099 C  C   . HIS B 1 420 ? 21.748  -11.233 0.230   1.00 13.29 ? 420 HIS B C   1 
ATOM   7100 O  O   . HIS B 1 420 ? 22.364  -10.169 0.183   1.00 13.38 ? 420 HIS B O   1 
ATOM   7101 C  CB  . HIS B 1 420 ? 19.366  -10.587 -0.289  1.00 12.32 ? 420 HIS B CB  1 
ATOM   7102 C  CG  . HIS B 1 420 ? 18.440  -10.283 -1.434  1.00 12.11 ? 420 HIS B CG  1 
ATOM   7103 N  ND1 . HIS B 1 420 ? 18.731  -9.270  -2.354  1.00 14.61 ? 420 HIS B ND1 1 
ATOM   7104 C  CD2 . HIS B 1 420 ? 17.242  -10.787 -1.782  1.00 13.57 ? 420 HIS B CD2 1 
ATOM   7105 C  CE1 . HIS B 1 420 ? 17.733  -9.246  -3.253  1.00 15.74 ? 420 HIS B CE1 1 
ATOM   7106 N  NE2 . HIS B 1 420 ? 16.840  -10.168 -2.933  1.00 15.66 ? 420 HIS B NE2 1 
ATOM   7107 N  N   . PHE B 1 421 ? 22.090  -12.235 1.039   1.00 12.71 ? 421 PHE B N   1 
ATOM   7108 C  CA  . PHE B 1 421 ? 23.125  -12.092 2.095   1.00 13.66 ? 421 PHE B CA  1 
ATOM   7109 C  C   . PHE B 1 421 ? 23.992  -13.346 2.193   1.00 14.31 ? 421 PHE B C   1 
ATOM   7110 O  O   . PHE B 1 421 ? 23.529  -14.457 2.022   1.00 14.46 ? 421 PHE B O   1 
ATOM   7111 C  CB  . PHE B 1 421 ? 22.518  -11.874 3.478   1.00 12.62 ? 421 PHE B CB  1 
ATOM   7112 C  CG  . PHE B 1 421 ? 21.515  -10.745 3.501   1.00 12.74 ? 421 PHE B CG  1 
ATOM   7113 C  CD1 . PHE B 1 421 ? 21.926  -9.436  3.660   1.00 13.44 ? 421 PHE B CD1 1 
ATOM   7114 C  CD2 . PHE B 1 421 ? 20.177  -10.983 3.303   1.00 14.09 ? 421 PHE B CD2 1 
ATOM   7115 C  CE1 . PHE B 1 421 ? 21.013  -8.380  3.668   1.00 13.30 ? 421 PHE B CE1 1 
ATOM   7116 C  CE2 . PHE B 1 421 ? 19.260  -9.936  3.311   1.00 12.76 ? 421 PHE B CE2 1 
ATOM   7117 C  CZ  . PHE B 1 421 ? 19.672  -8.644  3.477   1.00 13.70 ? 421 PHE B CZ  1 
ATOM   7118 N  N   . ASP B 1 422 ? 25.230  -13.116 2.637   1.00 15.32 ? 422 ASP B N   1 
ATOM   7119 C  CA  . ASP B 1 422 ? 26.062  -14.147 3.286   1.00 15.88 ? 422 ASP B CA  1 
ATOM   7120 C  C   . ASP B 1 422 ? 25.881  -14.010 4.795   1.00 16.96 ? 422 ASP B C   1 
ATOM   7121 O  O   . ASP B 1 422 ? 25.547  -12.909 5.288   1.00 18.60 ? 422 ASP B O   1 
ATOM   7122 C  CB  . ASP B 1 422 ? 27.543  -13.990 2.892   1.00 17.62 ? 422 ASP B CB  1 
ATOM   7123 C  CG  . ASP B 1 422 ? 27.798  -14.154 1.402   1.00 21.83 ? 422 ASP B CG  1 
ATOM   7124 O  OD1 . ASP B 1 422 ? 27.301  -15.131 0.819   1.00 29.06 ? 422 ASP B OD1 1 
ATOM   7125 O  OD2 . ASP B 1 422 ? 28.407  -13.230 0.810   1.00 30.44 ? 422 ASP B OD2 1 
ATOM   7126 N  N   . PHE B 1 423 ? 26.031  -15.095 5.528   1.00 16.63 ? 423 PHE B N   1 
ATOM   7127 C  CA  . PHE B 1 423 ? 25.808  -15.136 6.977   1.00 16.71 ? 423 PHE B CA  1 
ATOM   7128 C  C   . PHE B 1 423 ? 27.067  -15.596 7.706   1.00 16.66 ? 423 PHE B C   1 
ATOM   7129 O  O   . PHE B 1 423 ? 27.763  -16.507 7.241   1.00 21.40 ? 423 PHE B O   1 
ATOM   7130 C  CB  . PHE B 1 423 ? 24.618  -16.038 7.295   1.00 16.91 ? 423 PHE B CB  1 
ATOM   7131 C  CG  . PHE B 1 423 ? 23.322  -15.476 6.758   1.00 16.00 ? 423 PHE B CG  1 
ATOM   7132 C  CD1 . PHE B 1 423 ? 22.642  -14.492 7.460   1.00 17.26 ? 423 PHE B CD1 1 
ATOM   7133 C  CD2 . PHE B 1 423 ? 22.822  -15.862 5.524   1.00 17.27 ? 423 PHE B CD2 1 
ATOM   7134 C  CE1 . PHE B 1 423 ? 21.466  -13.943 6.976   1.00 16.53 ? 423 PHE B CE1 1 
ATOM   7135 C  CE2 . PHE B 1 423 ? 21.644  -15.288 5.032   1.00 16.34 ? 423 PHE B CE2 1 
ATOM   7136 C  CZ  . PHE B 1 423 ? 20.999  -14.298 5.723   1.00 15.44 ? 423 PHE B CZ  1 
ATOM   7137 N  N   . GLU B 1 424 ? 27.276  -15.031 8.878   1.00 16.65 ? 424 GLU B N   1 
ATOM   7138 C  CA  . GLU B 1 424 ? 28.401  -15.369 9.771   1.00 16.79 ? 424 GLU B CA  1 
ATOM   7139 C  C   . GLU B 1 424 ? 27.850  -15.677 11.153  1.00 16.36 ? 424 GLU B C   1 
ATOM   7140 O  O   . GLU B 1 424 ? 27.108  -14.885 11.711  1.00 16.51 ? 424 GLU B O   1 
ATOM   7141 C  CB  . GLU B 1 424 ? 29.395  -14.210 9.805   1.00 17.54 ? 424 GLU B CB  1 
ATOM   7142 C  CG  . GLU B 1 424 ? 30.580  -14.505 10.691  1.00 21.99 ? 424 GLU B CG  1 
ATOM   7143 C  CD  . GLU B 1 424 ? 31.495  -13.323 10.938  1.00 29.15 ? 424 GLU B CD  1 
ATOM   7144 O  OE1 . GLU B 1 424 ? 31.079  -12.152 10.685  1.00 32.23 ? 424 GLU B OE1 1 
ATOM   7145 O  OE2 . GLU B 1 424 ? 32.600  -13.564 11.449  1.00 35.34 ? 424 GLU B OE2 1 
ATOM   7146 N  N   . ASP B 1 425 ? 28.273  -16.842 11.668  1.00 16.07 ? 425 ASP B N   1 
ATOM   7147 C  CA  . ASP B 1 425 ? 28.004  -17.242 13.059  1.00 15.18 ? 425 ASP B CA  1 
ATOM   7148 C  C   . ASP B 1 425 ? 29.103  -16.586 13.906  1.00 16.99 ? 425 ASP B C   1 
ATOM   7149 O  O   . ASP B 1 425 ? 30.046  -17.311 14.324  1.00 17.42 ? 425 ASP B O   1 
ATOM   7150 C  CB  . ASP B 1 425 ? 27.997  -18.770 13.127  1.00 14.93 ? 425 ASP B CB  1 
ATOM   7151 C  CG  . ASP B 1 425 ? 27.882  -19.324 14.539  1.00 15.05 ? 425 ASP B CG  1 
ATOM   7152 O  OD1 . ASP B 1 425 ? 27.352  -18.621 15.433  1.00 15.13 ? 425 ASP B OD1 1 
ATOM   7153 O  OD2 . ASP B 1 425 ? 28.238  -20.514 14.695  1.00 15.60 ? 425 ASP B OD2 1 
ATOM   7154 N  N   . HIS B 1 426 ? 29.027  -15.269 14.119  1.00 16.44 ? 426 HIS B N   1 
ATOM   7155 C  CA  . HIS B 1 426 ? 30.156  -14.457 14.643  1.00 17.89 ? 426 HIS B CA  1 
ATOM   7156 C  C   . HIS B 1 426 ? 30.420  -14.759 16.126  1.00 18.78 ? 426 HIS B C   1 
ATOM   7157 O  O   . HIS B 1 426 ? 31.522  -14.421 16.634  1.00 21.10 ? 426 HIS B O   1 
ATOM   7158 C  CB  . HIS B 1 426 ? 29.871  -12.967 14.355  1.00 17.17 ? 426 HIS B CB  1 
ATOM   7159 C  CG  . HIS B 1 426 ? 28.717  -12.411 15.093  1.00 18.38 ? 426 HIS B CG  1 
ATOM   7160 N  ND1 . HIS B 1 426 ? 27.418  -12.825 14.842  1.00 15.66 ? 426 HIS B ND1 1 
ATOM   7161 C  CD2 . HIS B 1 426 ? 28.635  -11.468 16.058  1.00 17.64 ? 426 HIS B CD2 1 
ATOM   7162 C  CE1 . HIS B 1 426 ? 26.607  -12.172 15.613  1.00 15.87 ? 426 HIS B CE1 1 
ATOM   7163 N  NE2 . HIS B 1 426 ? 27.309  -11.322 16.402  1.00 18.52 ? 426 HIS B NE2 1 
ATOM   7164 N  N   . THR B 1 427 ? 29.470  -15.330 16.854  1.00 16.57 ? 427 THR B N   1 
ATOM   7165 C  CA  . THR B 1 427 ? 29.591  -15.651 18.303  1.00 15.61 ? 427 THR B CA  1 
ATOM   7166 C  C   . THR B 1 427 ? 29.874  -17.148 18.537  1.00 16.06 ? 427 THR B C   1 
ATOM   7167 O  O   . THR B 1 427 ? 30.015  -17.531 19.755  1.00 18.93 ? 427 THR B O   1 
ATOM   7168 C  CB  . THR B 1 427 ? 28.400  -15.181 19.118  1.00 16.90 ? 427 THR B CB  1 
ATOM   7169 O  OG1 . THR B 1 427 ? 27.277  -16.052 18.863  1.00 17.50 ? 427 THR B OG1 1 
ATOM   7170 C  CG2 . THR B 1 427 ? 28.028  -13.746 18.823  1.00 16.79 ? 427 THR B CG2 1 
ATOM   7171 N  N   . ASN B 1 428 ? 29.918  -17.974 17.491  1.00 15.65 ? 428 ASN B N   1 
ATOM   7172 C  CA  . ASN B 1 428 ? 29.928  -19.450 17.642  1.00 15.39 ? 428 ASN B CA  1 
ATOM   7173 C  C   . ASN B 1 428 ? 28.818  -19.842 18.633  1.00 16.68 ? 428 ASN B C   1 
ATOM   7174 O  O   . ASN B 1 428 ? 29.026  -20.379 19.704  1.00 17.06 ? 428 ASN B O   1 
ATOM   7175 C  CB  . ASN B 1 428 ? 31.315  -19.951 18.055  1.00 17.29 ? 428 ASN B CB  1 
ATOM   7176 C  CG  . ASN B 1 428 ? 31.366  -21.451 17.979  1.00 24.33 ? 428 ASN B CG  1 
ATOM   7177 O  OD1 . ASN B 1 428 ? 30.583  -22.078 17.274  1.00 25.30 ? 428 ASN B OD1 1 
ATOM   7178 N  ND2 . ASN B 1 428 ? 32.307  -22.049 18.687  1.00 30.18 ? 428 ASN B ND2 1 
ATOM   7179 N  N   . TYR B 1 429 ? 27.599  -19.535 18.239  1.00 15.40 ? 429 TYR B N   1 
ATOM   7180 C  CA  . TYR B 1 429 ? 26.414  -19.616 19.092  1.00 14.61 ? 429 TYR B CA  1 
ATOM   7181 C  C   . TYR B 1 429 ? 26.217  -21.041 19.579  1.00 14.49 ? 429 TYR B C   1 
ATOM   7182 O  O   . TYR B 1 429 ? 26.257  -22.010 18.784  1.00 13.88 ? 429 TYR B O   1 
ATOM   7183 C  CB  . TYR B 1 429 ? 25.199  -19.112 18.318  1.00 13.96 ? 429 TYR B CB  1 
ATOM   7184 C  CG  . TYR B 1 429 ? 23.895  -19.469 18.961  1.00 12.89 ? 429 TYR B CG  1 
ATOM   7185 C  CD1 . TYR B 1 429 ? 23.429  -18.821 20.070  1.00 13.00 ? 429 TYR B CD1 1 
ATOM   7186 C  CD2 . TYR B 1 429 ? 23.086  -20.453 18.427  1.00 11.96 ? 429 TYR B CD2 1 
ATOM   7187 C  CE1 . TYR B 1 429 ? 22.223  -19.100 20.672  1.00 13.51 ? 429 TYR B CE1 1 
ATOM   7188 C  CE2 . TYR B 1 429 ? 21.859  -20.745 19.014  1.00 12.13 ? 429 TYR B CE2 1 
ATOM   7189 C  CZ  . TYR B 1 429 ? 21.424  -20.090 20.161  1.00 12.84 ? 429 TYR B CZ  1 
ATOM   7190 O  OH  . TYR B 1 429 ? 20.226  -20.412 20.793  1.00 15.11 ? 429 TYR B OH  1 
ATOM   7191 N  N   . GLU B 1 430 ? 25.990  -21.151 20.871  1.00 15.13 ? 430 GLU B N   1 
ATOM   7192 C  CA  . GLU B 1 430 ? 25.649  -22.423 21.547  1.00 16.69 ? 430 GLU B CA  1 
ATOM   7193 C  C   . GLU B 1 430 ? 24.123  -22.537 21.639  1.00 14.28 ? 430 GLU B C   1 
ATOM   7194 O  O   . GLU B 1 430 ? 23.486  -21.729 22.305  1.00 15.15 ? 430 GLU B O   1 
ATOM   7195 C  CB  . GLU B 1 430 ? 26.291  -22.503 22.936  1.00 20.25 ? 430 GLU B CB  1 
ATOM   7196 C  CG  . GLU B 1 430 ? 26.083  -23.827 23.641  1.00 27.69 ? 430 GLU B CG  1 
ATOM   7197 C  CD  . GLU B 1 430 ? 26.797  -24.020 24.977  1.00 34.44 ? 430 GLU B CD  1 
ATOM   7198 O  OE1 . GLU B 1 430 ? 27.312  -23.024 25.534  1.00 42.34 ? 430 GLU B OE1 1 
ATOM   7199 O  OE2 . GLU B 1 430 ? 26.809  -25.181 25.473  1.00 42.48 ? 430 GLU B OE2 1 
ATOM   7200 N  N   . LEU B 1 431 ? 23.591  -23.581 21.019  1.00 14.72 ? 431 LEU B N   1 
ATOM   7201 C  CA  . LEU B 1 431 ? 22.127  -23.776 20.950  1.00 14.88 ? 431 LEU B CA  1 
ATOM   7202 C  C   . LEU B 1 431 ? 21.537  -23.815 22.362  1.00 15.67 ? 431 LEU B C   1 
ATOM   7203 O  O   . LEU B 1 431 ? 21.999  -24.632 23.202  1.00 17.52 ? 431 LEU B O   1 
ATOM   7204 C  CB  . LEU B 1 431 ? 21.826  -25.019 20.151  1.00 16.17 ? 431 LEU B CB  1 
ATOM   7205 C  CG  . LEU B 1 431 ? 20.349  -25.269 19.885  1.00 16.64 ? 431 LEU B CG  1 
ATOM   7206 C  CD1 . LEU B 1 431 ? 19.703  -24.130 19.158  1.00 17.10 ? 431 LEU B CD1 1 
ATOM   7207 C  CD2 . LEU B 1 431 ? 20.193  -26.564 19.102  1.00 17.20 ? 431 LEU B CD2 1 
ATOM   7208 N  N   . ASP B 1 432 ? 20.559  -22.956 22.602  1.00 14.45 ? 432 ASP B N   1 
ATOM   7209 C  CA  . ASP B 1 432 ? 19.792  -22.828 23.849  1.00 16.37 ? 432 ASP B CA  1 
ATOM   7210 C  C   . ASP B 1 432 ? 18.334  -22.740 23.441  1.00 14.54 ? 432 ASP B C   1 
ATOM   7211 O  O   . ASP B 1 432 ? 17.974  -21.791 22.745  1.00 16.00 ? 432 ASP B O   1 
ATOM   7212 C  CB  . ASP B 1 432 ? 20.229  -21.593 24.624  1.00 16.53 ? 432 ASP B CB  1 
ATOM   7213 C  CG  . ASP B 1 432 ? 19.577  -21.405 25.968  1.00 23.27 ? 432 ASP B CG  1 
ATOM   7214 O  OD1 . ASP B 1 432 ? 18.753  -22.247 26.355  1.00 23.94 ? 432 ASP B OD1 1 
ATOM   7215 O  OD2 . ASP B 1 432 ? 19.851  -20.350 26.611  1.00 28.26 ? 432 ASP B OD2 1 
ATOM   7216 N  N   . ILE B 1 433 ? 17.564  -23.777 23.707  1.00 13.00 ? 433 ILE B N   1 
ATOM   7217 C  CA  . ILE B 1 433 ? 16.192  -23.846 23.156  1.00 13.26 ? 433 ILE B CA  1 
ATOM   7218 C  C   . ILE B 1 433 ? 15.187  -23.413 24.211  1.00 14.44 ? 433 ILE B C   1 
ATOM   7219 O  O   . ILE B 1 433 ? 15.046  -24.110 25.230  1.00 14.40 ? 433 ILE B O   1 
ATOM   7220 C  CB  . ILE B 1 433 ? 15.883  -25.256 22.603  1.00 13.32 ? 433 ILE B CB  1 
ATOM   7221 C  CG1 . ILE B 1 433 ? 16.818  -25.599 21.430  1.00 15.03 ? 433 ILE B CG1 1 
ATOM   7222 C  CG2 . ILE B 1 433 ? 14.406  -25.323 22.221  1.00 13.99 ? 433 ILE B CG2 1 
ATOM   7223 C  CD1 . ILE B 1 433 ? 16.795  -27.023 20.950  1.00 16.67 ? 433 ILE B CD1 1 
ATOM   7224 N  N   . LYS B 1 434 ? 14.506  -22.307 23.970  1.00 14.09 ? 434 LYS B N   1 
ATOM   7225 C  CA  . LYS B 1 434 ? 13.438  -21.791 24.843  1.00 15.53 ? 434 LYS B CA  1 
ATOM   7226 C  C   . LYS B 1 434 ? 12.120  -22.433 24.470  1.00 15.37 ? 434 LYS B C   1 
ATOM   7227 O  O   . LYS B 1 434 ? 11.833  -22.588 23.255  1.00 14.72 ? 434 LYS B O   1 
ATOM   7228 C  CB  . LYS B 1 434 ? 13.294  -20.273 24.707  1.00 17.26 ? 434 LYS B CB  1 
ATOM   7229 C  CG  . LYS B 1 434 ? 12.155  -19.649 25.481  1.00 20.08 ? 434 LYS B CG  1 
ATOM   7230 C  CD  . LYS B 1 434 ? 12.289  -18.122 25.530  1.00 23.59 ? 434 LYS B CD  1 
ATOM   7231 C  CE  . LYS B 1 434 ? 11.067  -17.485 26.144  1.00 26.04 ? 434 LYS B CE  1 
ATOM   7232 N  NZ  . LYS B 1 434 ? 11.204  -16.008 26.161  1.00 32.80 ? 434 LYS B NZ  1 
ATOM   7233 N  N   . GLU B 1 435 ? 11.359  -22.815 25.485  1.00 14.42 ? 435 GLU B N   1 
ATOM   7234 C  CA  . GLU B 1 435 ? 10.080  -23.501 25.239  1.00 14.99 ? 435 GLU B CA  1 
ATOM   7235 C  C   . GLU B 1 435 ? 8.928   -22.618 25.655  1.00 15.43 ? 435 GLU B C   1 
ATOM   7236 O  O   . GLU B 1 435 ? 8.870   -22.183 26.817  1.00 17.25 ? 435 GLU B O   1 
ATOM   7237 C  CB  . GLU B 1 435 ? 10.023  -24.814 26.018  1.00 14.96 ? 435 GLU B CB  1 
ATOM   7238 C  CG  . GLU B 1 435 ? 11.204  -25.703 25.803  1.00 15.97 ? 435 GLU B CG  1 
ATOM   7239 C  CD  . GLU B 1 435 ? 11.026  -27.142 26.250  1.00 15.45 ? 435 GLU B CD  1 
ATOM   7240 O  OE1 . GLU B 1 435 ? 9.840   -27.500 26.608  1.00 17.56 ? 435 GLU B OE1 1 
ATOM   7241 O  OE2 . GLU B 1 435 ? 11.983  -27.918 26.225  1.00 15.64 ? 435 GLU B OE2 1 
ATOM   7242 N  N   . THR B 1 436 ? 8.014   -22.387 24.752  1.00 17.41 ? 436 THR B N   1 
ATOM   7243 C  CA  . THR B 1 436 ? 6.732   -21.699 25.038  1.00 19.10 ? 436 THR B CA  1 
ATOM   7244 C  C   . THR B 1 436 ? 5.683   -22.721 24.633  1.00 18.75 ? 436 THR B C   1 
ATOM   7245 O  O   . THR B 1 436 ? 5.815   -23.886 25.019  1.00 20.85 ? 436 THR B O   1 
ATOM   7246 C  CB  . THR B 1 436 ? 6.686   -20.361 24.294  1.00 20.56 ? 436 THR B CB  1 
ATOM   7247 O  OG1 . THR B 1 436 ? 6.929   -20.555 22.902  1.00 22.27 ? 436 THR B OG1 1 
ATOM   7248 C  CG2 . THR B 1 436 ? 7.670   -19.349 24.824  1.00 21.63 ? 436 THR B CG2 1 
ATOM   7249 N  N   . LEU B 1 437 ? 4.727   -22.343 23.788  1.00 18.79 ? 437 LEU B N   1 
ATOM   7250 C  CA  . LEU B 1 437 ? 3.899   -23.375 23.129  1.00 16.74 ? 437 LEU B CA  1 
ATOM   7251 C  C   . LEU B 1 437 ? 4.817   -24.137 22.176  1.00 17.89 ? 437 LEU B C   1 
ATOM   7252 O  O   . LEU B 1 437 ? 4.554   -25.324 21.902  1.00 18.21 ? 437 LEU B O   1 
ATOM   7253 C  CB  . LEU B 1 437 ? 2.738   -22.724 22.379  1.00 20.66 ? 437 LEU B CB  1 
ATOM   7254 C  CG  . LEU B 1 437 ? 1.732   -23.672 21.753  1.00 23.40 ? 437 LEU B CG  1 
ATOM   7255 C  CD1 . LEU B 1 437 ? 0.880   -24.311 22.842  1.00 23.35 ? 437 LEU B CD1 1 
ATOM   7256 C  CD2 . LEU B 1 437 ? 0.863   -22.934 20.748  1.00 24.99 ? 437 LEU B CD2 1 
ATOM   7257 N  N   . THR B 1 438 ? 5.905   -23.496 21.716  1.00 14.60 ? 438 THR B N   1 
ATOM   7258 C  CA  . THR B 1 438 ? 6.769   -24.051 20.674  1.00 13.88 ? 438 THR B CA  1 
ATOM   7259 C  C   . THR B 1 438 ? 8.223   -23.929 21.103  1.00 14.39 ? 438 THR B C   1 
ATOM   7260 O  O   . THR B 1 438 ? 8.529   -23.373 22.216  1.00 15.51 ? 438 THR B O   1 
ATOM   7261 C  CB  . THR B 1 438 ? 6.543   -23.324 19.354  1.00 15.16 ? 438 THR B CB  1 
ATOM   7262 O  OG1 . THR B 1 438 ? 6.737   -21.940 19.620  1.00 16.30 ? 438 THR B OG1 1 
ATOM   7263 C  CG2 . THR B 1 438 ? 5.187   -23.655 18.758  1.00 15.81 ? 438 THR B CG2 1 
ATOM   7264 N  N   . LEU B 1 439 ? 9.114   -24.469 20.277  1.00 15.19 ? 439 LEU B N   1 
ATOM   7265 C  CA  . LEU B 1 439 ? 10.571  -24.411 20.526  1.00 13.59 ? 439 LEU B CA  1 
ATOM   7266 C  C   . LEU B 1 439 ? 11.179  -23.284 19.672  1.00 14.01 ? 439 LEU B C   1 
ATOM   7267 O  O   . LEU B 1 439 ? 10.883  -23.231 18.439  1.00 16.27 ? 439 LEU B O   1 
ATOM   7268 C  CB  . LEU B 1 439 ? 11.185  -25.757 20.174  1.00 13.82 ? 439 LEU B CB  1 
ATOM   7269 C  CG  . LEU B 1 439 ? 10.601  -26.979 20.862  1.00 15.21 ? 439 LEU B CG  1 
ATOM   7270 C  CD1 . LEU B 1 439 ? 11.322  -28.247 20.439  1.00 16.06 ? 439 LEU B CD1 1 
ATOM   7271 C  CD2 . LEU B 1 439 ? 10.622  -26.849 22.372  1.00 16.12 ? 439 LEU B CD2 1 
ATOM   7272 N  N   . LYS B 1 440 ? 12.132  -22.549 20.207  1.00 14.55 ? 440 LYS B N   1 
ATOM   7273 C  CA  . LYS B 1 440 ? 12.888  -21.521 19.437  1.00 15.10 ? 440 LYS B CA  1 
ATOM   7274 C  C   . LYS B 1 440 ? 14.304  -21.461 19.988  1.00 15.40 ? 440 LYS B C   1 
ATOM   7275 O  O   . LYS B 1 440 ? 14.502  -21.609 21.193  1.00 16.36 ? 440 LYS B O   1 
ATOM   7276 C  CB  . LYS B 1 440 ? 12.239  -20.146 19.477  1.00 17.40 ? 440 LYS B CB  1 
ATOM   7277 C  CG  . LYS B 1 440 ? 10.897  -20.030 18.785  1.00 19.59 ? 440 LYS B CG  1 
ATOM   7278 C  CD  . LYS B 1 440 ? 10.389  -18.580 18.682  1.00 20.56 ? 440 LYS B CD  1 
ATOM   7279 C  CE  . LYS B 1 440 ? 8.952   -18.543 18.222  1.00 21.26 ? 440 LYS B CE  1 
ATOM   7280 N  NZ  . LYS B 1 440 ? 8.389   -17.171 18.297  1.00 19.28 ? 440 LYS B NZ  1 
ATOM   7281 N  N   . PRO B 1 441 ? 15.320  -21.189 19.147  1.00 14.11 ? 441 PRO B N   1 
ATOM   7282 C  CA  . PRO B 1 441 ? 16.680  -20.946 19.592  1.00 14.72 ? 441 PRO B CA  1 
ATOM   7283 C  C   . PRO B 1 441 ? 16.970  -19.583 20.218  1.00 18.65 ? 441 PRO B C   1 
ATOM   7284 O  O   . PRO B 1 441 ? 17.389  -18.646 19.498  1.00 21.42 ? 441 PRO B O   1 
ATOM   7285 C  CB  . PRO B 1 441 ? 17.551  -21.077 18.337  1.00 18.07 ? 441 PRO B CB  1 
ATOM   7286 C  CG  . PRO B 1 441 ? 16.611  -20.956 17.143  1.00 16.32 ? 441 PRO B CG  1 
ATOM   7287 C  CD  . PRO B 1 441 ? 15.209  -21.187 17.680  1.00 14.78 ? 441 PRO B CD  1 
ATOM   7288 N  N   . GLU B 1 442 ? 16.929  -19.517 21.546  1.00 14.77 ? 442 GLU B N   1 
ATOM   7289 C  CA  . GLU B 1 442 ? 17.030  -18.284 22.323  1.00 14.62 ? 442 GLU B CA  1 
ATOM   7290 C  C   . GLU B 1 442 ? 18.427  -17.684 22.176  1.00 16.19 ? 442 GLU B C   1 
ATOM   7291 O  O   . GLU B 1 442 ? 19.409  -18.407 22.293  1.00 14.95 ? 442 GLU B O   1 
ATOM   7292 C  CB  . GLU B 1 442 ? 16.711  -18.510 23.804  1.00 17.19 ? 442 GLU B CB  1 
ATOM   7293 C  CG  . GLU B 1 442 ? 16.654  -17.196 24.521  1.00 21.25 ? 442 GLU B CG  1 
ATOM   7294 C  CD  . GLU B 1 442 ? 16.134  -17.201 25.941  1.00 28.41 ? 442 GLU B CD  1 
ATOM   7295 O  OE1 . GLU B 1 442 ? 16.007  -18.284 26.505  1.00 29.71 ? 442 GLU B OE1 1 
ATOM   7296 O  OE2 . GLU B 1 442 ? 15.843  -16.113 26.437  1.00 34.93 ? 442 GLU B OE2 1 
ATOM   7297 N  N   . GLY B 1 443 ? 18.501  -16.382 21.931  1.00 15.15 ? 443 GLY B N   1 
ATOM   7298 C  CA  . GLY B 1 443 ? 19.773  -15.655 21.868  1.00 14.98 ? 443 GLY B CA  1 
ATOM   7299 C  C   . GLY B 1 443 ? 20.564  -15.906 20.591  1.00 14.06 ? 443 GLY B C   1 
ATOM   7300 O  O   . GLY B 1 443 ? 21.718  -15.485 20.461  1.00 16.89 ? 443 GLY B O   1 
ATOM   7301 N  N   . PHE B 1 444 ? 19.978  -16.569 19.604  1.00 14.55 ? 444 PHE B N   1 
ATOM   7302 C  CA  . PHE B 1 444 ? 20.688  -16.835 18.342  1.00 13.34 ? 444 PHE B CA  1 
ATOM   7303 C  C   . PHE B 1 444 ? 20.822  -15.534 17.545  1.00 14.00 ? 444 PHE B C   1 
ATOM   7304 O  O   . PHE B 1 444 ? 19.845  -14.810 17.294  1.00 13.07 ? 444 PHE B O   1 
ATOM   7305 C  CB  . PHE B 1 444 ? 19.937  -17.906 17.538  1.00 13.57 ? 444 PHE B CB  1 
ATOM   7306 C  CG  . PHE B 1 444 ? 20.474  -18.234 16.178  1.00 12.50 ? 444 PHE B CG  1 
ATOM   7307 C  CD1 . PHE B 1 444 ? 21.843  -18.279 15.942  1.00 12.94 ? 444 PHE B CD1 1 
ATOM   7308 C  CD2 . PHE B 1 444 ? 19.639  -18.534 15.132  1.00 13.24 ? 444 PHE B CD2 1 
ATOM   7309 C  CE1 . PHE B 1 444 ? 22.346  -18.587 14.714  1.00 12.73 ? 444 PHE B CE1 1 
ATOM   7310 C  CE2 . PHE B 1 444 ? 20.159  -18.786 13.886  1.00 13.85 ? 444 PHE B CE2 1 
ATOM   7311 C  CZ  . PHE B 1 444 ? 21.513  -18.816 13.662  1.00 12.94 ? 444 PHE B CZ  1 
ATOM   7312 N  N   . VAL B 1 445 ? 22.068  -15.191 17.251  1.00 13.95 ? 445 VAL B N   1 
ATOM   7313 C  CA  . VAL B 1 445 ? 22.452  -13.950 16.549  1.00 14.67 ? 445 VAL B CA  1 
ATOM   7314 C  C   . VAL B 1 445 ? 23.398  -14.334 15.419  1.00 12.70 ? 445 VAL B C   1 
ATOM   7315 O  O   . VAL B 1 445 ? 24.165  -15.324 15.536  1.00 14.04 ? 445 VAL B O   1 
ATOM   7316 C  CB  . VAL B 1 445 ? 23.077  -12.913 17.497  1.00 15.07 ? 445 VAL B CB  1 
ATOM   7317 C  CG1 . VAL B 1 445 ? 22.056  -12.356 18.502  1.00 16.25 ? 445 VAL B CG1 1 
ATOM   7318 C  CG2 . VAL B 1 445 ? 24.313  -13.470 18.222  1.00 16.56 ? 445 VAL B CG2 1 
ATOM   7319 N  N   . VAL B 1 446 ? 23.343  -13.596 14.340  1.00 12.81 ? 446 VAL B N   1 
ATOM   7320 C  CA  . VAL B 1 446 ? 24.267  -13.727 13.186  1.00 14.11 ? 446 VAL B CA  1 
ATOM   7321 C  C   . VAL B 1 446 ? 24.614  -12.329 12.679  1.00 13.61 ? 446 VAL B C   1 
ATOM   7322 O  O   . VAL B 1 446 ? 23.896  -11.365 13.009  1.00 14.47 ? 446 VAL B O   1 
ATOM   7323 C  CB  . VAL B 1 446 ? 23.688  -14.595 12.075  1.00 13.85 ? 446 VAL B CB  1 
ATOM   7324 C  CG1 . VAL B 1 446 ? 23.380  -16.010 12.518  1.00 15.17 ? 446 VAL B CG1 1 
ATOM   7325 C  CG2 . VAL B 1 446 ? 22.461  -13.962 11.444  1.00 14.72 ? 446 VAL B CG2 1 
ATOM   7326 N  N   . LYS B 1 447 ? 25.651  -12.278 11.861  1.00 13.46 ? 447 LYS B N   1 
ATOM   7327 C  CA  . LYS B 1 447 ? 25.923  -11.105 11.019  1.00 14.77 ? 447 LYS B CA  1 
ATOM   7328 C  C   . LYS B 1 447 ? 25.588  -11.447 9.596   1.00 15.27 ? 447 LYS B C   1 
ATOM   7329 O  O   . LYS B 1 447 ? 25.876  -12.579 9.125   1.00 16.78 ? 447 LYS B O   1 
ATOM   7330 C  CB  . LYS B 1 447 ? 27.369  -10.664 11.184  1.00 16.68 ? 447 LYS B CB  1 
ATOM   7331 C  CG  . LYS B 1 447 ? 27.608  -9.953  12.481  1.00 18.95 ? 447 LYS B CG  1 
ATOM   7332 C  CD  . LYS B 1 447 ? 29.048  -9.479  12.586  1.00 22.29 ? 447 LYS B CD  1 
ATOM   7333 C  CE  . LYS B 1 447 ? 29.310  -8.780  13.883  1.00 27.62 ? 447 LYS B CE  1 
ATOM   7334 N  NZ  . LYS B 1 447 ? 30.757  -8.477  14.019  1.00 32.41 ? 447 LYS B NZ  1 
ATOM   7335 N  N   . ALA B 1 448 ? 25.011  -10.491 8.890   1.00 16.50 ? 448 ALA B N   1 
ATOM   7336 C  CA  . ALA B 1 448 ? 24.741  -10.637 7.463   1.00 17.40 ? 448 ALA B CA  1 
ATOM   7337 C  C   . ALA B 1 448 ? 25.746  -9.738  6.718   1.00 20.31 ? 448 ALA B C   1 
ATOM   7338 O  O   . ALA B 1 448 ? 26.273  -8.711  7.262   1.00 24.46 ? 448 ALA B O   1 
ATOM   7339 C  CB  . ALA B 1 448 ? 23.283  -10.415 7.136   1.00 18.92 ? 448 ALA B CB  1 
ATOM   7340 N  N   . LYS B 1 449 ? 26.140  -10.154 5.557   1.00 18.60 ? 449 LYS B N   1 
ATOM   7341 C  CA  . LYS B 1 449 ? 26.877  -9.251  4.634   1.00 20.06 ? 449 LYS B CA  1 
ATOM   7342 C  C   . LYS B 1 449 ? 26.094  -9.263  3.335   1.00 16.87 ? 449 LYS B C   1 
ATOM   7343 O  O   . LYS B 1 449 ? 25.961  -10.350 2.705   1.00 16.22 ? 449 LYS B O   1 
ATOM   7344 C  CB  . LYS B 1 449 ? 28.292  -9.738  4.397   1.00 22.86 ? 449 LYS B CB  1 
ATOM   7345 C  CG  . LYS B 1 449 ? 29.206  -8.786  3.634   1.00 31.05 ? 449 LYS B CG  1 
ATOM   7346 C  CD  . LYS B 1 449 ? 30.525  -9.445  3.243   1.00 36.54 ? 449 LYS B CD  1 
ATOM   7347 C  CE  . LYS B 1 449 ? 31.110  -8.920  1.944   1.00 41.57 ? 449 LYS B CE  1 
ATOM   7348 N  NZ  . LYS B 1 449 ? 31.099  -7.434  1.904   1.00 43.75 ? 449 LYS B NZ  1 
ATOM   7349 N  N   . SER B 1 450 ? 25.618  -8.088  2.947   1.00 16.68 ? 450 SER B N   1 
ATOM   7350 C  CA  . SER B 1 450 ? 24.820  -7.919  1.720   1.00 16.37 ? 450 SER B CA  1 
ATOM   7351 C  C   . SER B 1 450 ? 25.625  -8.355  0.507   1.00 18.22 ? 450 SER B C   1 
ATOM   7352 O  O   . SER B 1 450 ? 26.824  -7.939  0.371   1.00 17.94 ? 450 SER B O   1 
ATOM   7353 C  CB  . SER B 1 450 ? 24.358  -6.528  1.613   1.00 18.13 ? 450 SER B CB  1 
ATOM   7354 O  OG  . SER B 1 450 ? 23.597  -6.392  0.427   1.00 17.61 ? 450 SER B OG  1 
ATOM   7355 N  N   . LYS B 1 451 ? 24.982  -9.077  -0.391  1.00 17.14 ? 451 LYS B N   1 
ATOM   7356 C  CA  . LYS B 1 451 ? 25.494  -9.362  -1.738  1.00 18.35 ? 451 LYS B CA  1 
ATOM   7357 C  C   . LYS B 1 451 ? 25.221  -8.186  -2.686  1.00 18.89 ? 451 LYS B C   1 
ATOM   7358 O  O   . LYS B 1 451 ? 25.659  -8.279  -3.866  1.00 22.80 ? 451 LYS B O   1 
ATOM   7359 C  CB  . LYS B 1 451 ? 24.905  -10.671 -2.241  1.00 18.84 ? 451 LYS B CB  1 
ATOM   7360 C  CG  . LYS B 1 451 ? 25.260  -11.895 -1.409  1.00 22.39 ? 451 LYS B CG  1 
ATOM   7361 C  CD  . LYS B 1 451 ? 24.693  -13.128 -2.078  1.00 24.91 ? 451 LYS B CD  1 
ATOM   7362 C  CE  . LYS B 1 451 ? 25.117  -14.467 -1.535  1.00 25.11 ? 451 LYS B CE  1 
ATOM   7363 N  NZ  . LYS B 1 451 ? 26.538  -14.739 -1.873  1.00 28.45 ? 451 LYS B NZ  1 
ATOM   7364 N  N   . LYS B 1 452 ? 24.478  -7.178  -2.216  1.00 19.38 ? 452 LYS B N   1 
ATOM   7365 C  CA  . LYS B 1 452 ? 24.243  -5.900  -2.931  1.00 19.98 ? 452 LYS B CA  1 
ATOM   7366 C  C   . LYS B 1 452 ? 23.468  -6.187  -4.202  1.00 20.52 ? 452 LYS B C   1 
ATOM   7367 O  O   . LYS B 1 452 ? 23.770  -5.621  -5.270  1.00 23.64 ? 452 LYS B O   1 
ATOM   7368 C  CB  . LYS B 1 452 ? 25.577  -5.189  -3.171  1.00 22.30 ? 452 LYS B CB  1 
ATOM   7369 C  CG  . LYS B 1 452 ? 26.231  -4.680  -1.890  1.00 25.83 ? 452 LYS B CG  1 
ATOM   7370 C  CD  . LYS B 1 452 ? 25.424  -3.607  -1.113  1.00 30.04 ? 452 LYS B CD  1 
ATOM   7371 C  CE  . LYS B 1 452 ? 26.104  -3.163  0.175   1.00 34.91 ? 452 LYS B CE  1 
ATOM   7372 N  NZ  . LYS B 1 452 ? 25.256  -2.275  1.012   1.00 37.36 ? 452 LYS B NZ  1 
ATOM   7373 N  N   . ILE B 1 453 ? 22.419  -6.991  -4.080  1.00 17.43 ? 453 ILE B N   1 
ATOM   7374 C  CA  . ILE B 1 453 ? 21.526  -7.328  -5.206  1.00 19.55 ? 453 ILE B CA  1 
ATOM   7375 C  C   . ILE B 1 453 ? 20.259  -6.535  -4.976  1.00 22.35 ? 453 ILE B C   1 
ATOM   7376 O  O   . ILE B 1 453 ? 19.578  -6.719  -3.985  1.00 19.33 ? 453 ILE B O   1 
ATOM   7377 C  CB  . ILE B 1 453 ? 21.260  -8.840  -5.272  1.00 20.56 ? 453 ILE B CB  1 
ATOM   7378 C  CG1 . ILE B 1 453 ? 22.565  -9.605  -5.475  1.00 21.18 ? 453 ILE B CG1 1 
ATOM   7379 C  CG2 . ILE B 1 453 ? 20.244  -9.119  -6.365  1.00 20.45 ? 453 ILE B CG2 1 
ATOM   7380 C  CD1 . ILE B 1 453 ? 22.434  -11.084 -5.215  1.00 24.24 ? 453 ILE B CD1 1 
ATOM   7381 N  N   . PRO B 1 454 ? 19.892  -5.628  -5.884  1.00 24.99 ? 454 PRO B N   1 
ATOM   7382 C  CA  . PRO B 1 454 ? 18.705  -4.807  -5.680  1.00 25.21 ? 454 PRO B CA  1 
ATOM   7383 C  C   . PRO B 1 454 ? 17.409  -5.624  -5.652  1.00 23.77 ? 454 PRO B C   1 
ATOM   7384 O  O   . PRO B 1 454 ? 17.365  -6.674  -6.295  1.00 24.62 ? 454 PRO B O   1 
ATOM   7385 C  CB  . PRO B 1 454 ? 18.619  -3.913  -6.934  1.00 29.91 ? 454 PRO B CB  1 
ATOM   7386 C  CG  . PRO B 1 454 ? 19.951  -4.049  -7.626  1.00 28.63 ? 454 PRO B CG  1 
ATOM   7387 C  CD  . PRO B 1 454 ? 20.595  -5.332  -7.146  1.00 28.43 ? 454 PRO B CD  1 
ATOM   7388 N  N   . LEU B 1 455 ? 16.412  -5.118  -4.916  1.00 26.17 ? 455 LEU B N   1 
ATOM   7389 C  CA  . LEU B 1 455 ? 14.979  -5.496  -5.030  1.00 29.06 ? 455 LEU B CA  1 
ATOM   7390 C  C   . LEU B 1 455 ? 14.340  -4.595  -6.099  1.00 33.81 ? 455 LEU B C   1 
ATOM   7391 O  O   . LEU B 1 455 ? 15.003  -3.876  -6.820  1.00 39.16 ? 455 LEU B O   1 
ATOM   7392 C  CB  . LEU B 1 455 ? 14.276  -5.272  -3.683  1.00 30.27 ? 455 LEU B CB  1 
ATOM   7393 C  CG  . LEU B 1 455 ? 14.772  -6.139  -2.534  1.00 27.26 ? 455 LEU B CG  1 
ATOM   7394 C  CD1 . LEU B 1 455 ? 14.343  -5.606  -1.162  1.00 27.09 ? 455 LEU B CD1 1 
ATOM   7395 C  CD2 . LEU B 1 455 ? 14.305  -7.557  -2.715  1.00 27.84 ? 455 LEU B CD2 1 
ATOM   7396 O  OXT . LEU B 1 455 ? 13.144  -4.585  -6.251  1.00 42.49 ? 455 LEU B OXT 1 
HETATM 7397 C  CHA . HEM C 2 .   ? 23.423  27.890  12.526  1.00 10.76 ? 501 HEM A CHA 1 
HETATM 7398 C  CHB . HEM C 2 .   ? 18.574  27.646  12.053  1.00 10.65 ? 501 HEM A CHB 1 
HETATM 7399 C  CHC . HEM C 2 .   ? 18.994  23.289  9.984   1.00 10.61 ? 501 HEM A CHC 1 
HETATM 7400 C  CHD . HEM C 2 .   ? 23.751  23.361  10.728  1.00 11.05 ? 501 HEM A CHD 1 
HETATM 7401 C  C1A . HEM C 2 .   ? 22.071  28.204  12.531  1.00 9.45  ? 501 HEM A C1A 1 
HETATM 7402 C  C2A . HEM C 2 .   ? 21.563  29.429  13.127  1.00 10.45 ? 501 HEM A C2A 1 
HETATM 7403 C  C3A . HEM C 2 .   ? 20.196  29.341  12.976  1.00 10.08 ? 501 HEM A C3A 1 
HETATM 7404 C  C4A . HEM C 2 .   ? 19.859  28.090  12.376  1.00 9.84  ? 501 HEM A C4A 1 
HETATM 7405 C  CMA . HEM C 2 .   ? 19.125  30.316  13.453  1.00 11.67 ? 501 HEM A CMA 1 
HETATM 7406 C  CAA . HEM C 2 .   ? 22.317  30.587  13.721  1.00 10.68 ? 501 HEM A CAA 1 
HETATM 7407 C  CBA . HEM C 2 .   ? 22.730  30.325  15.164  1.00 10.31 ? 501 HEM A CBA 1 
HETATM 7408 C  CGA . HEM C 2 .   ? 23.397  31.484  15.914  1.00 10.20 ? 501 HEM A CGA 1 
HETATM 7409 O  O1A . HEM C 2 .   ? 23.729  31.169  17.101  1.00 12.36 ? 501 HEM A O1A 1 
HETATM 7410 O  O2A . HEM C 2 .   ? 23.587  32.562  15.275  1.00 11.09 ? 501 HEM A O2A 1 
HETATM 7411 C  C1B . HEM C 2 .   ? 18.274  26.429  11.440  1.00 9.81  ? 501 HEM A C1B 1 
HETATM 7412 C  C2B . HEM C 2 .   ? 16.939  26.046  11.094  1.00 10.90 ? 501 HEM A C2B 1 
HETATM 7413 C  C3B . HEM C 2 .   ? 17.076  24.852  10.466  1.00 11.61 ? 501 HEM A C3B 1 
HETATM 7414 C  C4B . HEM C 2 .   ? 18.459  24.468  10.496  1.00 9.72  ? 501 HEM A C4B 1 
HETATM 7415 C  CMB . HEM C 2 .   ? 15.706  26.860  11.311  1.00 12.13 ? 501 HEM A CMB 1 
HETATM 7416 C  CAB . HEM C 2 .   ? 16.040  24.002  9.838   1.00 11.81 ? 501 HEM A CAB 1 
HETATM 7417 C  CBB . HEM C 2 .   ? 14.929  24.470  9.381   1.00 20.04 ? 501 HEM A CBB 1 
HETATM 7418 C  C1C . HEM C 2 .   ? 20.290  22.904  10.031  1.00 10.02 ? 501 HEM A C1C 1 
HETATM 7419 C  C2C . HEM C 2 .   ? 20.814  21.703  9.484   1.00 11.34 ? 501 HEM A C2C 1 
HETATM 7420 C  C3C . HEM C 2 .   ? 22.197  21.717  9.706   1.00 11.15 ? 501 HEM A C3C 1 
HETATM 7421 C  C4C . HEM C 2 .   ? 22.480  22.944  10.378  1.00 10.82 ? 501 HEM A C4C 1 
HETATM 7422 C  CMC . HEM C 2 .   ? 19.984  20.617  8.854   1.00 12.46 ? 501 HEM A CMC 1 
HETATM 7423 C  CAC . HEM C 2 .   ? 23.189  20.717  9.378   1.00 13.56 ? 501 HEM A CAC 1 
HETATM 7424 C  CBC . HEM C 2 .   ? 22.975  19.543  8.875   1.00 23.04 ? 501 HEM A CBC 1 
HETATM 7425 C  C1D . HEM C 2 .   ? 24.050  24.594  11.294  1.00 9.79  ? 501 HEM A C1D 1 
HETATM 7426 C  C2D . HEM C 2 .   ? 25.415  25.003  11.672  1.00 10.45 ? 501 HEM A C2D 1 
HETATM 7427 C  C3D . HEM C 2 .   ? 25.323  26.276  12.081  1.00 10.84 ? 501 HEM A C3D 1 
HETATM 7428 C  C4D . HEM C 2 .   ? 23.891  26.634  12.087  1.00 10.19 ? 501 HEM A C4D 1 
HETATM 7429 C  CMD . HEM C 2 .   ? 26.659  24.173  11.564  1.00 10.97 ? 501 HEM A CMD 1 
HETATM 7430 C  CAD . HEM C 2 .   ? 26.489  27.152  12.540  1.00 10.79 ? 501 HEM A CAD 1 
HETATM 7431 C  CBD . HEM C 2 .   ? 26.942  27.927  11.309  1.00 11.40 ? 501 HEM A CBD 1 
HETATM 7432 C  CGD . HEM C 2 .   ? 28.147  28.815  11.566  1.00 12.56 ? 501 HEM A CGD 1 
HETATM 7433 O  O1D . HEM C 2 .   ? 28.149  29.616  12.547  1.00 11.52 ? 501 HEM A O1D 1 
HETATM 7434 O  O2D . HEM C 2 .   ? 29.180  28.638  10.877  1.00 13.35 ? 501 HEM A O2D 1 
HETATM 7435 N  NA  . HEM C 2 .   ? 20.980  27.409  12.114  1.00 9.72  ? 501 HEM A NA  1 
HETATM 7436 N  NB  . HEM C 2 .   ? 19.118  25.431  11.136  1.00 9.16  ? 501 HEM A NB  1 
HETATM 7437 N  NC  . HEM C 2 .   ? 21.332  23.658  10.474  1.00 9.43  ? 501 HEM A NC  1 
HETATM 7438 N  ND  . HEM C 2 .   ? 23.147  25.604  11.581  1.00 9.52  ? 501 HEM A ND  1 
HETATM 7439 FE FE  . HEM C 2 .   ? 21.192  25.569  11.245  1.00 10.99 ? 501 HEM A FE  1 
HETATM 7440 N  N   A HL0 D 3 .   ? 18.469  31.846  27.594  0.50 27.87 ? 502 HL0 A N   1 
HETATM 7441 C  C1  A HL0 D 3 .   ? 19.685  28.161  17.853  0.50 18.66 ? 502 HL0 A C1  1 
HETATM 7442 O  O1  A HL0 D 3 .   ? 17.464  33.346  26.269  0.50 19.61 ? 502 HL0 A O1  1 
HETATM 7443 C  C2  A HL0 D 3 .   ? 18.620  28.338  18.929  0.50 21.59 ? 502 HL0 A C2  1 
HETATM 7444 O  O2  A HL0 D 3 .   ? 21.785  32.267  28.619  0.50 31.22 ? 502 HL0 A O2  1 
HETATM 7445 C  C3  A HL0 D 3 .   ? 19.179  28.348  20.321  0.50 22.70 ? 502 HL0 A C3  1 
HETATM 7446 O  O3  A HL0 D 3 .   ? 21.248  31.236  26.746  0.50 28.15 ? 502 HL0 A O3  1 
HETATM 7447 C  C4  A HL0 D 3 .   ? 18.136  28.320  21.407  0.50 23.91 ? 502 HL0 A C4  1 
HETATM 7448 C  C5  A HL0 D 3 .   ? 18.257  29.415  22.454  0.50 25.80 ? 502 HL0 A C5  1 
HETATM 7449 C  C6  A HL0 D 3 .   ? 16.899  29.858  23.041  0.50 25.36 ? 502 HL0 A C6  1 
HETATM 7450 C  C7  A HL0 D 3 .   ? 16.873  29.899  24.550  0.50 24.87 ? 502 HL0 A C7  1 
HETATM 7451 C  C8  A HL0 D 3 .   ? 16.030  31.002  25.170  0.50 27.34 ? 502 HL0 A C8  1 
HETATM 7452 C  C9  A HL0 D 3 .   ? 16.344  31.239  26.606  0.50 26.47 ? 502 HL0 A C9  1 
HETATM 7453 C  C10 A HL0 D 3 .   ? 17.463  32.244  26.806  0.50 26.26 ? 502 HL0 A C10 1 
HETATM 7454 C  C11 A HL0 D 3 .   ? 19.615  32.688  27.833  0.50 28.55 ? 502 HL0 A C11 1 
HETATM 7455 C  C12 A HL0 D 3 .   ? 19.715  33.233  29.248  0.50 30.37 ? 502 HL0 A C12 1 
HETATM 7456 C  C13 A HL0 D 3 .   ? 21.173  33.148  29.600  0.50 30.31 ? 502 HL0 A C13 1 
HETATM 7457 C  C14 A HL0 D 3 .   ? 20.934  31.963  27.640  0.50 29.69 ? 502 HL0 A C14 1 
HETATM 7458 S  S   . DMS E 4 .   ? 20.958  24.644  13.495  0.70 18.47 ? 503 DMS A S   1 
HETATM 7459 O  O   . DMS E 4 .   ? 20.142  23.387  13.566  0.70 20.01 ? 503 DMS A O   1 
HETATM 7460 C  C1  . DMS E 4 .   ? 22.414  24.269  14.421  0.70 21.21 ? 503 DMS A C1  1 
HETATM 7461 C  C2  . DMS E 4 .   ? 20.277  25.697  14.759  0.70 17.94 ? 503 DMS A C2  1 
HETATM 7462 C  C1  . GOL F 5 .   ? -8.776  26.802  -2.250  1.00 32.26 ? 504 GOL A C1  1 
HETATM 7463 O  O1  . GOL F 5 .   ? -7.350  26.583  -2.253  1.00 22.08 ? 504 GOL A O1  1 
HETATM 7464 C  C2  . GOL F 5 .   ? -9.573  25.511  -2.237  1.00 32.24 ? 504 GOL A C2  1 
HETATM 7465 O  O2  . GOL F 5 .   ? -9.675  24.968  -0.907  1.00 27.32 ? 504 GOL A O2  1 
HETATM 7466 C  C3  . GOL F 5 .   ? -10.955 25.657  -2.837  1.00 34.44 ? 504 GOL A C3  1 
HETATM 7467 O  O3  . GOL F 5 .   ? -11.743 24.480  -2.639  1.00 37.08 ? 504 GOL A O3  1 
HETATM 7468 C  C1  B GOL G 5 .   ? 21.834  33.733  28.650  0.50 18.79 ? 505 GOL A C1  1 
HETATM 7469 O  O1  B GOL G 5 .   ? 23.054  33.870  27.923  0.50 15.92 ? 505 GOL A O1  1 
HETATM 7470 C  C2  B GOL G 5 .   ? 20.831  32.814  27.983  0.50 19.82 ? 505 GOL A C2  1 
HETATM 7471 O  O2  B GOL G 5 .   ? 21.451  31.543  27.772  0.50 18.84 ? 505 GOL A O2  1 
HETATM 7472 C  C3  B GOL G 5 .   ? 19.547  32.664  28.792  0.50 21.19 ? 505 GOL A C3  1 
HETATM 7473 O  O3  B GOL G 5 .   ? 18.669  31.665  28.286  0.50 23.96 ? 505 GOL A O3  1 
HETATM 7474 C  CHA . HEM H 2 .   ? -2.421  -27.884 14.074  1.00 9.80  ? 501 HEM B CHA 1 
HETATM 7475 C  CHB . HEM H 2 .   ? 2.426   -27.712 13.630  1.00 10.05 ? 501 HEM B CHB 1 
HETATM 7476 C  CHC . HEM H 2 .   ? 2.004   -23.504 11.320  1.00 10.40 ? 501 HEM B CHC 1 
HETATM 7477 C  CHD . HEM H 2 .   ? -2.755  -23.514 12.088  1.00 11.06 ? 501 HEM B CHD 1 
HETATM 7478 C  C1A . HEM H 2 .   ? -1.092  -28.250 14.157  1.00 8.97  ? 501 HEM B C1A 1 
HETATM 7479 C  C2A . HEM H 2 .   ? -0.534  -29.440 14.745  1.00 10.29 ? 501 HEM B C2A 1 
HETATM 7480 C  C3A . HEM H 2 .   ? 0.820   -29.344 14.665  1.00 9.70  ? 501 HEM B C3A 1 
HETATM 7481 C  C4A . HEM H 2 .   ? 1.145   -28.145 13.917  1.00 9.48  ? 501 HEM B C4A 1 
HETATM 7482 C  CMA . HEM H 2 .   ? 1.816   -30.344 15.156  1.00 10.66 ? 501 HEM B CMA 1 
HETATM 7483 C  CAA . HEM H 2 .   ? -1.339  -30.547 15.422  1.00 10.20 ? 501 HEM B CAA 1 
HETATM 7484 C  CBA . HEM H 2 .   ? -1.605  -30.208 16.863  1.00 10.02 ? 501 HEM B CBA 1 
HETATM 7485 C  CGA . HEM H 2 .   ? -2.373  -31.316 17.682  1.00 10.40 ? 501 HEM B CGA 1 
HETATM 7486 O  O1A . HEM H 2 .   ? -2.644  -31.022 18.876  1.00 11.85 ? 501 HEM B O1A 1 
HETATM 7487 O  O2A . HEM H 2 .   ? -2.598  -32.418 17.144  1.00 10.68 ? 501 HEM B O2A 1 
HETATM 7488 C  C1B . HEM H 2 .   ? 2.686   -26.494 12.958  1.00 9.61  ? 501 HEM B C1B 1 
HETATM 7489 C  C2B . HEM H 2 .   ? 4.039   -26.183 12.483  1.00 10.14 ? 501 HEM B C2B 1 
HETATM 7490 C  C3B . HEM H 2 .   ? 3.935   -25.011 11.842  1.00 10.18 ? 501 HEM B C3B 1 
HETATM 7491 C  C4B . HEM H 2 .   ? 2.537   -24.616 11.877  1.00 9.94  ? 501 HEM B C4B 1 
HETATM 7492 C  CMB . HEM H 2 .   ? 5.243   -26.985 12.811  1.00 10.94 ? 501 HEM B CMB 1 
HETATM 7493 C  CAB . HEM H 2 .   ? 4.952   -24.200 11.159  1.00 12.75 ? 501 HEM B CAB 1 
HETATM 7494 C  CBB . HEM H 2 .   ? 6.133   -24.651 10.826  1.00 19.11 ? 501 HEM B CBB 1 
HETATM 7495 C  C1C . HEM H 2 .   ? 0.686   -23.113 11.312  1.00 9.88  ? 501 HEM B C1C 1 
HETATM 7496 C  C2C . HEM H 2 .   ? 0.131   -21.945 10.735  1.00 11.01 ? 501 HEM B C2C 1 
HETATM 7497 C  C3C . HEM H 2 .   ? -1.208  -21.930 10.949  1.00 11.83 ? 501 HEM B C3C 1 
HETATM 7498 C  C4C . HEM H 2 .   ? -1.486  -23.129 11.697  1.00 10.79 ? 501 HEM B C4C 1 
HETATM 7499 C  CMC . HEM H 2 .   ? 0.939   -20.893 10.078  1.00 13.76 ? 501 HEM B CMC 1 
HETATM 7500 C  CAC . HEM H 2 .   ? -2.260  -20.993 10.597  1.00 14.06 ? 501 HEM B CAC 1 
HETATM 7501 C  CBC . HEM H 2 .   ? -2.037  -19.891 9.994   1.00 23.62 ? 501 HEM B CBC 1 
HETATM 7502 C  C1D . HEM H 2 .   ? -3.074  -24.700 12.734  1.00 10.40 ? 501 HEM B C1D 1 
HETATM 7503 C  C2D . HEM H 2 .   ? -4.443  -25.111 13.083  1.00 10.10 ? 501 HEM B C2D 1 
HETATM 7504 C  C3D . HEM H 2 .   ? -4.369  -26.367 13.607  1.00 10.52 ? 501 HEM B C3D 1 
HETATM 7505 C  C4D . HEM H 2 .   ? -2.934  -26.681 13.600  1.00 9.15  ? 501 HEM B C4D 1 
HETATM 7506 C  CMD . HEM H 2 .   ? -5.682  -24.243 12.974  1.00 10.67 ? 501 HEM B CMD 1 
HETATM 7507 C  CAD . HEM H 2 .   ? -5.522  -27.218 14.089  1.00 10.48 ? 501 HEM B CAD 1 
HETATM 7508 C  CBD . HEM H 2 .   ? -6.039  -28.027 12.879  1.00 10.53 ? 501 HEM B CBD 1 
HETATM 7509 C  CGD . HEM H 2 .   ? -7.217  -28.904 13.280  1.00 11.97 ? 501 HEM B CGD 1 
HETATM 7510 O  O1D . HEM H 2 .   ? -7.126  -29.643 14.302  1.00 11.40 ? 501 HEM B O1D 1 
HETATM 7511 O  O2D . HEM H 2 .   ? -8.266  -28.840 12.595  1.00 12.94 ? 501 HEM B O2D 1 
HETATM 7512 N  NA  . HEM H 2 .   ? -0.061  -27.426 13.680  1.00 9.15  ? 501 HEM B NA  1 
HETATM 7513 N  NB  . HEM H 2 .   ? 1.837   -25.555 12.583  1.00 9.34  ? 501 HEM B NB  1 
HETATM 7514 N  NC  . HEM H 2 .   ? -0.314  -23.833 11.827  1.00 10.10 ? 501 HEM B NC  1 
HETATM 7515 N  ND  . HEM H 2 .   ? -2.188  -25.686 13.030  1.00 9.32  ? 501 HEM B ND  1 
HETATM 7516 FE FE  . HEM H 2 .   ? -0.213  -25.678 12.699  1.00 11.14 ? 501 HEM B FE  1 
HETATM 7517 N  N   A HL0 I 3 .   ? 2.919   -31.312 29.357  0.50 22.98 ? 502 HL0 B N   1 
HETATM 7518 C  C1  A HL0 I 3 .   ? 1.621   -27.325 19.538  0.50 22.45 ? 502 HL0 B C1  1 
HETATM 7519 O  O1  A HL0 I 3 .   ? 3.778   -32.905 28.010  0.50 20.39 ? 502 HL0 B O1  1 
HETATM 7520 C  C2  A HL0 I 3 .   ? 2.548   -27.923 20.593  0.50 23.12 ? 502 HL0 B C2  1 
HETATM 7521 O  O2  A HL0 I 3 .   ? -0.330  -31.461 30.569  0.50 29.55 ? 502 HL0 B O2  1 
HETATM 7522 C  C3  A HL0 I 3 .   ? 1.933   -28.100 21.968  0.50 23.81 ? 502 HL0 B C3  1 
HETATM 7523 O  O3  A HL0 I 3 .   ? 0.094   -30.748 28.499  0.50 28.67 ? 502 HL0 B O3  1 
HETATM 7524 C  C4  A HL0 I 3 .   ? 2.923   -28.007 23.126  0.50 24.10 ? 502 HL0 B C4  1 
HETATM 7525 C  C5  A HL0 I 3 .   ? 2.977   -29.219 24.036  0.50 22.79 ? 502 HL0 B C5  1 
HETATM 7526 C  C6  A HL0 I 3 .   ? 4.337   -29.464 24.720  0.50 19.55 ? 502 HL0 B C6  1 
HETATM 7527 C  C7  A HL0 I 3 .   ? 4.234   -29.631 26.250  0.50 18.30 ? 502 HL0 B C7  1 
HETATM 7528 C  C8  A HL0 I 3 .   ? 5.303   -30.511 26.878  0.50 20.85 ? 502 HL0 B C8  1 
HETATM 7529 C  C9  A HL0 I 3 .   ? 5.058   -30.851 28.298  0.50 20.99 ? 502 HL0 B C9  1 
HETATM 7530 C  C10 A HL0 I 3 .   ? 3.865   -31.790 28.532  0.50 23.21 ? 502 HL0 B C10 1 
HETATM 7531 C  C11 A HL0 I 3 .   ? 1.751   -32.091 29.697  0.50 26.85 ? 502 HL0 B C11 1 
HETATM 7532 C  C12 A HL0 I 3 .   ? 1.656   -32.533 31.142  0.50 27.11 ? 502 HL0 B C12 1 
HETATM 7533 C  C13 A HL0 I 3 .   ? 0.175   -32.552 31.386  0.50 28.54 ? 502 HL0 B C13 1 
HETATM 7534 C  C14 A HL0 I 3 .   ? 0.443   -31.344 29.479  0.50 27.30 ? 502 HL0 B C14 1 
HETATM 7535 S  S   . DMS J 4 .   ? 0.038   -24.677 14.907  0.70 18.68 ? 503 DMS B S   1 
HETATM 7536 O  O   . DMS J 4 .   ? 0.914   -23.441 14.905  0.70 22.16 ? 503 DMS B O   1 
HETATM 7537 C  C1  . DMS J 4 .   ? 0.621   -25.623 16.274  0.70 17.85 ? 503 DMS B C1  1 
HETATM 7538 C  C2  . DMS J 4 .   ? -1.393  -24.105 15.739  0.70 20.71 ? 503 DMS B C2  1 
HETATM 7539 C  C1  . GOL K 5 .   ? 0.484   -34.156 7.647   1.00 32.91 ? 504 GOL B C1  1 
HETATM 7540 O  O1  . GOL K 5 .   ? 1.630   -33.811 6.871   1.00 37.52 ? 504 GOL B O1  1 
HETATM 7541 C  C2  . GOL K 5 .   ? 0.254   -35.653 7.666   1.00 29.69 ? 504 GOL B C2  1 
HETATM 7542 O  O2  . GOL K 5 .   ? 1.322   -36.377 8.281   1.00 27.02 ? 504 GOL B O2  1 
HETATM 7543 C  C3  . GOL K 5 .   ? -1.052  -36.046 8.306   1.00 30.13 ? 504 GOL B C3  1 
HETATM 7544 O  O3  . GOL K 5 .   ? -1.179  -37.448 8.572   1.00 20.05 ? 504 GOL B O3  1 
HETATM 7545 C  C1  B GOL L 5 .   ? 1.276   -32.445 29.117  0.50 25.12 ? 505 GOL B C1  1 
HETATM 7546 O  O1  B GOL L 5 .   ? 2.354   -31.518 28.930  0.50 29.10 ? 505 GOL B O1  1 
HETATM 7547 C  C2  B GOL L 5 .   ? 0.198   -31.877 30.012  0.50 25.16 ? 505 GOL B C2  1 
HETATM 7548 O  O2  B GOL L 5 .   ? -0.407  -30.755 29.370  0.50 21.90 ? 505 GOL B O2  1 
HETATM 7549 C  C3  B GOL L 5 .   ? -0.814  -32.907 30.490  0.50 21.53 ? 505 GOL B C3  1 
HETATM 7550 O  O3  B GOL L 5 .   ? -1.784  -33.299 29.515  0.50 20.74 ? 505 GOL B O3  1 
HETATM 7551 O  O   . HOH M 6 .   ? -6.687  19.264  0.108   1.00 25.11 ? 601 HOH A O   1 
HETATM 7552 O  O   . HOH M 6 .   ? 11.783  1.812   1.529   1.00 22.71 ? 602 HOH A O   1 
HETATM 7553 O  O   . HOH M 6 .   ? 20.338  30.702  24.574  1.00 35.40 ? 603 HOH A O   1 
HETATM 7554 O  O   . HOH M 6 .   ? 1.448   33.047  17.883  1.00 30.73 ? 604 HOH A O   1 
HETATM 7555 O  O   . HOH M 6 .   ? 17.403  18.738  7.250   1.00 24.32 ? 605 HOH A O   1 
HETATM 7556 O  O   . HOH M 6 .   ? 38.029  31.914  12.257  1.00 23.45 ? 606 HOH A O   1 
HETATM 7557 O  O   . HOH M 6 .   ? 19.665  17.718  33.308  1.00 37.62 ? 607 HOH A O   1 
HETATM 7558 O  O   . HOH M 6 .   ? 42.930  23.790  13.362  1.00 35.82 ? 608 HOH A O   1 
HETATM 7559 O  O   . HOH M 6 .   ? 21.979  30.420  5.575   1.00 20.14 ? 609 HOH A O   1 
HETATM 7560 O  O   . HOH M 6 .   ? -2.587  15.344  21.389  1.00 26.98 ? 610 HOH A O   1 
HETATM 7561 O  O   . HOH M 6 .   ? 28.077  36.290  29.578  1.00 35.95 ? 611 HOH A O   1 
HETATM 7562 O  O   . HOH M 6 .   ? 48.951  28.254  6.603   1.00 25.43 ? 612 HOH A O   1 
HETATM 7563 O  O   . HOH M 6 .   ? 10.786  1.029   4.179   1.00 15.85 ? 613 HOH A O   1 
HETATM 7564 O  O   . HOH M 6 .   ? 22.918  31.741  34.781  1.00 23.31 ? 614 HOH A O   1 
HETATM 7565 O  O   . HOH M 6 .   ? 4.930   21.364  25.614  1.00 25.22 ? 615 HOH A O   1 
HETATM 7566 O  O   . HOH M 6 .   ? 32.909  35.003  5.926   1.00 29.67 ? 616 HOH A O   1 
HETATM 7567 O  O   . HOH M 6 .   ? 33.641  50.185  27.132  1.00 31.07 ? 617 HOH A O   1 
HETATM 7568 O  O   . HOH M 6 .   ? 20.939  54.175  14.634  1.00 36.08 ? 618 HOH A O   1 
HETATM 7569 O  O   . HOH M 6 .   ? -6.691  6.868   8.665   1.00 37.04 ? 619 HOH A O   1 
HETATM 7570 O  O   . HOH M 6 .   ? 17.109  6.915   -3.421  1.00 28.90 ? 620 HOH A O   1 
HETATM 7571 O  O   . HOH M 6 .   ? -2.132  2.671   2.205   1.00 28.29 ? 621 HOH A O   1 
HETATM 7572 O  O   . HOH M 6 .   ? 2.601   4.812   -1.851  1.00 25.10 ? 622 HOH A O   1 
HETATM 7573 O  O   . HOH M 6 .   ? -7.442  9.903   0.413   1.00 34.09 ? 623 HOH A O   1 
HETATM 7574 O  O   . HOH M 6 .   ? 22.474  10.760  -2.265  1.00 21.50 ? 624 HOH A O   1 
HETATM 7575 O  O   . HOH M 6 .   ? 26.638  19.976  42.228  1.00 36.23 ? 625 HOH A O   1 
HETATM 7576 O  O   . HOH M 6 .   ? 39.230  26.474  18.851  1.00 20.40 ? 626 HOH A O   1 
HETATM 7577 O  O   . HOH M 6 .   ? 26.029  30.262  13.923  1.00 11.40 ? 627 HOH A O   1 
HETATM 7578 O  O   . HOH M 6 .   ? -4.251  31.876  4.572   1.00 26.80 ? 628 HOH A O   1 
HETATM 7579 O  O   . HOH M 6 .   ? 27.471  30.306  7.683   1.00 19.34 ? 629 HOH A O   1 
HETATM 7580 O  O   . HOH M 6 .   ? 39.367  18.828  6.292   1.00 19.52 ? 630 HOH A O   1 
HETATM 7581 O  O   . HOH M 6 .   ? 1.400   13.455  -9.206  1.00 24.02 ? 631 HOH A O   1 
HETATM 7582 O  O   . HOH M 6 .   ? 4.987   14.962  21.260  1.00 23.00 ? 632 HOH A O   1 
HETATM 7583 O  O   . HOH M 6 .   ? 4.253   37.250  20.898  1.00 20.64 ? 633 HOH A O   1 
HETATM 7584 O  O   . HOH M 6 .   ? -2.060  24.960  -6.134  1.00 18.47 ? 634 HOH A O   1 
HETATM 7585 O  O   . HOH M 6 .   ? 13.155  22.695  -11.466 1.00 26.90 ? 635 HOH A O   1 
HETATM 7586 O  O   . HOH M 6 .   ? 39.901  28.946  21.273  1.00 19.46 ? 636 HOH A O   1 
HETATM 7587 O  O   . HOH M 6 .   ? 22.678  54.767  16.819  1.00 34.95 ? 637 HOH A O   1 
HETATM 7588 O  O   . HOH M 6 .   ? -4.968  -0.762  15.224  1.00 27.57 ? 638 HOH A O   1 
HETATM 7589 O  O   . HOH M 6 .   ? 12.168  42.823  23.008  1.00 16.21 ? 639 HOH A O   1 
HETATM 7590 O  O   . HOH M 6 .   ? 38.837  20.772  17.817  1.00 28.93 ? 640 HOH A O   1 
HETATM 7591 O  O   . HOH M 6 .   ? 11.858  -2.806  6.250   1.00 13.80 ? 641 HOH A O   1 
HETATM 7592 O  O   . HOH M 6 .   ? 8.685   33.101  33.342  1.00 23.45 ? 642 HOH A O   1 
HETATM 7593 O  O   . HOH M 6 .   ? -0.483  7.247   -1.724  1.00 15.26 ? 643 HOH A O   1 
HETATM 7594 O  O   . HOH M 6 .   ? 11.219  48.478  24.680  1.00 19.29 ? 644 HOH A O   1 
HETATM 7595 O  O   . HOH M 6 .   ? 0.446   0.140   13.212  1.00 27.82 ? 645 HOH A O   1 
HETATM 7596 O  O   . HOH M 6 .   ? 34.304  21.098  24.767  1.00 34.44 ? 646 HOH A O   1 
HETATM 7597 O  O   . HOH M 6 .   ? 12.745  15.403  -13.331 1.00 23.60 ? 647 HOH A O   1 
HETATM 7598 O  O   . HOH M 6 .   ? 24.687  35.837  28.645  1.00 45.66 ? 648 HOH A O   1 
HETATM 7599 O  O   . HOH M 6 .   ? 29.203  28.358  8.235   1.00 15.00 ? 649 HOH A O   1 
HETATM 7600 O  O   . HOH M 6 .   ? -2.568  20.013  23.112  1.00 21.53 ? 650 HOH A O   1 
HETATM 7601 O  O   . HOH M 6 .   ? -6.235  6.638   16.446  1.00 36.30 ? 651 HOH A O   1 
HETATM 7602 O  O   . HOH M 6 .   ? -0.243  9.070   20.201  1.00 32.90 ? 652 HOH A O   1 
HETATM 7603 O  O   . HOH M 6 .   ? 2.887   26.342  24.196  1.00 17.64 ? 653 HOH A O   1 
HETATM 7604 O  O   . HOH M 6 .   ? -5.635  16.103  15.672  1.00 15.93 ? 654 HOH A O   1 
HETATM 7605 O  O   . HOH M 6 .   ? 23.535  33.787  12.902  1.00 13.38 ? 655 HOH A O   1 
HETATM 7606 O  O   . HOH M 6 .   ? 27.990  37.086  11.290  1.00 17.56 ? 656 HOH A O   1 
HETATM 7607 O  O   . HOH M 6 .   ? 32.619  16.194  22.336  1.00 28.48 ? 657 HOH A O   1 
HETATM 7608 O  O   . HOH M 6 .   ? 7.061   26.146  -9.950  1.00 29.24 ? 658 HOH A O   1 
HETATM 7609 O  O   . HOH M 6 .   ? 14.006  30.798  3.714   1.00 19.67 ? 659 HOH A O   1 
HETATM 7610 O  O   . HOH M 6 .   ? 14.462  29.484  13.136  1.00 20.53 ? 660 HOH A O   1 
HETATM 7611 O  O   . HOH M 6 .   ? -0.695  32.450  14.874  1.00 27.48 ? 661 HOH A O   1 
HETATM 7612 O  O   . HOH M 6 .   ? -4.085  25.253  18.165  1.00 19.47 ? 662 HOH A O   1 
HETATM 7613 O  O   . HOH M 6 .   ? 16.306  42.758  41.907  1.00 30.85 ? 663 HOH A O   1 
HETATM 7614 O  O   . HOH M 6 .   ? 24.145  32.918  19.095  1.00 12.47 ? 664 HOH A O   1 
HETATM 7615 O  O   . HOH M 6 .   ? 5.155   4.574   15.527  1.00 24.15 ? 665 HOH A O   1 
HETATM 7616 O  O   . HOH M 6 .   ? 40.993  15.832  7.816   1.00 26.48 ? 666 HOH A O   1 
HETATM 7617 O  O   . HOH M 6 .   ? 11.555  25.184  -0.993  1.00 22.99 ? 667 HOH A O   1 
HETATM 7618 O  O   . HOH M 6 .   ? 20.458  7.446   9.162   1.00 13.85 ? 668 HOH A O   1 
HETATM 7619 O  O   . HOH M 6 .   ? 15.172  28.198  30.841  1.00 25.99 ? 669 HOH A O   1 
HETATM 7620 O  O   . HOH M 6 .   ? 3.565   7.984   14.222  1.00 14.83 ? 670 HOH A O   1 
HETATM 7621 O  O   . HOH M 6 .   ? -2.655  16.158  0.494   1.00 17.49 ? 671 HOH A O   1 
HETATM 7622 O  O   . HOH M 6 .   ? 10.687  47.902  13.447  1.00 18.47 ? 672 HOH A O   1 
HETATM 7623 O  O   . HOH M 6 .   ? 26.491  48.701  29.199  1.00 29.87 ? 673 HOH A O   1 
HETATM 7624 O  O   . HOH M 6 .   ? 36.818  0.218   8.338   1.00 28.31 ? 674 HOH A O   1 
HETATM 7625 O  O   . HOH M 6 .   ? 14.043  27.456  24.662  1.00 24.49 ? 675 HOH A O   1 
HETATM 7626 O  O   . HOH M 6 .   ? 27.332  34.480  27.269  1.00 29.08 ? 676 HOH A O   1 
HETATM 7627 O  O   . HOH M 6 .   ? 25.029  30.224  33.527  1.00 32.13 ? 677 HOH A O   1 
HETATM 7628 O  O   . HOH M 6 .   ? 29.320  23.335  17.063  1.00 14.18 ? 678 HOH A O   1 
HETATM 7629 O  O   . HOH M 6 .   ? 10.226  41.516  10.525  1.00 20.95 ? 679 HOH A O   1 
HETATM 7630 O  O   . HOH M 6 .   ? 24.399  49.755  11.504  1.00 23.16 ? 680 HOH A O   1 
HETATM 7631 O  O   . HOH M 6 .   ? 8.651   26.286  11.766  1.00 22.28 ? 681 HOH A O   1 
HETATM 7632 O  O   . HOH M 6 .   ? 18.180  16.259  8.405   1.00 20.55 ? 682 HOH A O   1 
HETATM 7633 O  O   . HOH M 6 .   ? 25.931  41.980  28.450  1.00 18.54 ? 683 HOH A O   1 
HETATM 7634 O  O   . HOH M 6 .   ? -4.953  3.205   7.060   1.00 31.99 ? 684 HOH A O   1 
HETATM 7635 O  O   . HOH M 6 .   ? 34.331  24.941  13.461  1.00 14.17 ? 685 HOH A O   1 
HETATM 7636 O  O   . HOH M 6 .   ? 9.060   29.052  -2.811  1.00 23.03 ? 686 HOH A O   1 
HETATM 7637 O  O   . HOH M 6 .   ? 9.096   22.666  26.951  1.00 15.88 ? 687 HOH A O   1 
HETATM 7638 O  O   . HOH M 6 .   ? 40.546  29.834  7.461   1.00 18.74 ? 688 HOH A O   1 
HETATM 7639 O  O   . HOH M 6 .   ? 21.555  50.596  26.624  1.00 26.97 ? 689 HOH A O   1 
HETATM 7640 O  O   . HOH M 6 .   ? -3.626  27.817  14.383  1.00 32.70 ? 690 HOH A O   1 
HETATM 7641 O  O   . HOH M 6 .   ? 13.525  17.448  19.825  1.00 31.22 ? 691 HOH A O   1 
HETATM 7642 O  O   . HOH M 6 .   ? 18.428  5.423   8.943   1.00 14.53 ? 692 HOH A O   1 
HETATM 7643 O  O   . HOH M 6 .   ? 37.744  11.771  16.369  1.00 24.66 ? 693 HOH A O   1 
HETATM 7644 O  O   . HOH M 6 .   ? 30.237  48.083  17.687  1.00 25.93 ? 694 HOH A O   1 
HETATM 7645 O  O   . HOH M 6 .   ? 23.353  14.669  30.385  1.00 20.84 ? 695 HOH A O   1 
HETATM 7646 O  O   . HOH M 6 .   ? 7.256   18.198  -12.846 1.00 15.93 ? 696 HOH A O   1 
HETATM 7647 O  O   . HOH M 6 .   ? 26.787  39.722  30.457  1.00 22.14 ? 697 HOH A O   1 
HETATM 7648 O  O   . HOH M 6 .   ? 38.423  8.981   15.594  1.00 26.99 ? 698 HOH A O   1 
HETATM 7649 O  O   . HOH M 6 .   ? 30.301  44.746  28.198  1.00 30.24 ? 699 HOH A O   1 
HETATM 7650 O  O   . HOH M 6 .   ? 32.235  35.256  17.672  1.00 14.32 ? 700 HOH A O   1 
HETATM 7651 O  O   . HOH M 6 .   ? 10.143  27.076  -7.131  1.00 36.59 ? 701 HOH A O   1 
HETATM 7652 O  O   . HOH M 6 .   ? -2.032  28.537  16.193  1.00 31.10 ? 702 HOH A O   1 
HETATM 7653 O  O   . HOH M 6 .   ? 21.632  2.260   14.035  1.00 23.97 ? 703 HOH A O   1 
HETATM 7654 O  O   . HOH M 6 .   ? 22.842  23.882  3.203   1.00 13.00 ? 704 HOH A O   1 
HETATM 7655 O  O   . HOH M 6 .   ? 5.253   7.295   16.420  1.00 18.90 ? 705 HOH A O   1 
HETATM 7656 O  O   . HOH M 6 .   ? 17.312  1.606   1.743   1.00 17.53 ? 706 HOH A O   1 
HETATM 7657 O  O   . HOH M 6 .   ? 22.139  48.315  28.225  1.00 37.86 ? 707 HOH A O   1 
HETATM 7658 O  O   . HOH M 6 .   ? 2.610   13.663  18.847  1.00 17.92 ? 708 HOH A O   1 
HETATM 7659 O  O   . HOH M 6 .   ? 22.746  15.159  33.027  1.00 25.42 ? 709 HOH A O   1 
HETATM 7660 O  O   . HOH M 6 .   ? 33.399  47.263  27.839  1.00 28.25 ? 710 HOH A O   1 
HETATM 7661 O  O   . HOH M 6 .   ? 13.590  3.904   0.845   1.00 18.73 ? 711 HOH A O   1 
HETATM 7662 O  O   . HOH M 6 .   ? 34.615  37.087  21.593  1.00 27.24 ? 712 HOH A O   1 
HETATM 7663 O  O   . HOH M 6 .   ? 26.800  16.480  -2.768  1.00 31.20 ? 713 HOH A O   1 
HETATM 7664 O  O   . HOH M 6 .   ? -7.786  20.844  2.215   1.00 23.96 ? 714 HOH A O   1 
HETATM 7665 O  O   . HOH M 6 .   ? 14.089  24.454  -3.708  1.00 32.94 ? 715 HOH A O   1 
HETATM 7666 O  O   . HOH M 6 .   ? 8.000   49.541  27.675  1.00 30.20 ? 716 HOH A O   1 
HETATM 7667 O  O   . HOH M 6 .   ? 34.706  27.740  0.652   1.00 28.36 ? 717 HOH A O   1 
HETATM 7668 O  O   . HOH M 6 .   ? 2.794   40.510  5.332   1.00 21.56 ? 718 HOH A O   1 
HETATM 7669 O  O   . HOH M 6 .   ? 6.690   46.361  4.827   1.00 32.15 ? 719 HOH A O   1 
HETATM 7670 O  O   . HOH M 6 .   ? 14.562  11.330  19.691  1.00 23.60 ? 720 HOH A O   1 
HETATM 7671 O  O   . HOH M 6 .   ? -9.328  21.484  12.549  1.00 35.41 ? 721 HOH A O   1 
HETATM 7672 O  O   . HOH M 6 .   ? 31.335  40.440  12.799  1.00 23.05 ? 722 HOH A O   1 
HETATM 7673 O  O   . HOH M 6 .   ? 30.413  37.758  25.249  1.00 33.85 ? 723 HOH A O   1 
HETATM 7674 O  O   . HOH M 6 .   ? -1.657  13.436  -5.383  1.00 17.56 ? 724 HOH A O   1 
HETATM 7675 O  O   . HOH M 6 .   ? 23.078  6.287   25.938  1.00 31.66 ? 725 HOH A O   1 
HETATM 7676 O  O   . HOH M 6 .   ? -4.854  16.513  20.676  1.00 21.43 ? 726 HOH A O   1 
HETATM 7677 O  O   . HOH M 6 .   ? 13.272  42.833  43.446  1.00 12.44 ? 727 HOH A O   1 
HETATM 7678 O  O   . HOH M 6 .   ? 6.151   9.938   -5.000  1.00 19.74 ? 728 HOH A O   1 
HETATM 7679 O  O   . HOH M 6 .   ? -1.849  15.800  -3.915  1.00 17.23 ? 729 HOH A O   1 
HETATM 7680 O  O   . HOH M 6 .   ? 14.268  44.105  -2.191  1.00 24.18 ? 730 HOH A O   1 
HETATM 7681 O  O   . HOH M 6 .   ? 16.986  29.545  28.930  1.00 31.66 ? 731 HOH A O   1 
HETATM 7682 O  O   . HOH M 6 .   ? 40.373  8.671   13.696  1.00 26.59 ? 732 HOH A O   1 
HETATM 7683 O  O   . HOH M 6 .   ? 28.665  19.547  34.333  1.00 34.01 ? 733 HOH A O   1 
HETATM 7684 O  O   . HOH M 6 .   ? 24.696  34.889  16.342  1.00 12.69 ? 734 HOH A O   1 
HETATM 7685 O  O   . HOH M 6 .   ? 3.190   30.569  23.375  1.00 31.56 ? 735 HOH A O   1 
HETATM 7686 O  O   . HOH M 6 .   ? 0.983   47.822  10.556  1.00 32.26 ? 736 HOH A O   1 
HETATM 7687 O  O   . HOH M 6 .   ? -6.435  24.737  -4.143  1.00 18.68 ? 737 HOH A O   1 
HETATM 7688 O  O   . HOH M 6 .   ? 17.343  24.039  -0.957  1.00 19.21 ? 738 HOH A O   1 
HETATM 7689 O  O   . HOH M 6 .   ? 7.708   13.002  -8.905  1.00 19.95 ? 739 HOH A O   1 
HETATM 7690 O  O   . HOH M 6 .   ? 4.795   50.446  8.780   1.00 25.24 ? 740 HOH A O   1 
HETATM 7691 O  O   . HOH M 6 .   ? 41.451  4.459   12.015  1.00 34.25 ? 741 HOH A O   1 
HETATM 7692 O  O   . HOH M 6 .   ? -7.511  5.294   1.321   1.00 29.99 ? 742 HOH A O   1 
HETATM 7693 O  O   . HOH M 6 .   ? 25.289  26.968  3.081   1.00 24.38 ? 743 HOH A O   1 
HETATM 7694 O  O   . HOH M 6 .   ? -2.058  6.494   7.450   1.00 24.49 ? 744 HOH A O   1 
HETATM 7695 O  O   . HOH M 6 .   ? -9.599  20.178  21.120  1.00 33.73 ? 745 HOH A O   1 
HETATM 7696 O  O   . HOH M 6 .   ? -3.957  32.170  2.037   1.00 34.85 ? 746 HOH A O   1 
HETATM 7697 O  O   . HOH M 6 .   ? 9.026   30.941  -0.433  1.00 27.10 ? 747 HOH A O   1 
HETATM 7698 O  O   . HOH M 6 .   ? 3.663   9.035   -9.399  1.00 28.26 ? 748 HOH A O   1 
HETATM 7699 O  O   . HOH M 6 .   ? 41.780  23.778  -0.653  1.00 35.47 ? 749 HOH A O   1 
HETATM 7700 O  O   . HOH M 6 .   ? -7.292  -0.906  8.247   1.00 32.38 ? 750 HOH A O   1 
HETATM 7701 O  O   . HOH M 6 .   ? 11.411  1.829   7.470   1.00 16.07 ? 751 HOH A O   1 
HETATM 7702 O  O   . HOH M 6 .   ? 23.799  40.363  7.240   1.00 35.77 ? 752 HOH A O   1 
HETATM 7703 O  O   . HOH M 6 .   ? 34.969  50.429  22.263  1.00 26.21 ? 753 HOH A O   1 
HETATM 7704 O  O   . HOH M 6 .   ? 11.179  27.550  1.703   1.00 27.86 ? 754 HOH A O   1 
HETATM 7705 O  O   . HOH M 6 .   ? 24.292  34.662  5.134   1.00 29.08 ? 755 HOH A O   1 
HETATM 7706 O  O   . HOH M 6 .   ? 6.255   35.943  30.385  1.00 19.98 ? 756 HOH A O   1 
HETATM 7707 O  O   . HOH M 6 .   ? 4.423   33.185  24.004  1.00 30.66 ? 757 HOH A O   1 
HETATM 7708 O  O   . HOH M 6 .   ? 18.670  33.048  5.556   1.00 31.76 ? 758 HOH A O   1 
HETATM 7709 O  O   . HOH M 6 .   ? 26.815  26.523  0.971   1.00 20.47 ? 759 HOH A O   1 
HETATM 7710 O  O   . HOH M 6 .   ? 30.399  37.985  12.272  1.00 18.39 ? 760 HOH A O   1 
HETATM 7711 O  O   . HOH M 6 .   ? 21.302  12.074  -5.697  1.00 19.28 ? 761 HOH A O   1 
HETATM 7712 O  O   . HOH M 6 .   ? 27.157  54.702  17.917  1.00 36.73 ? 762 HOH A O   1 
HETATM 7713 O  O   . HOH M 6 .   ? 6.333   30.145  29.357  1.00 27.44 ? 763 HOH A O   1 
HETATM 7714 O  O   . HOH M 6 .   ? 24.837  22.783  38.029  1.00 33.18 ? 764 HOH A O   1 
HETATM 7715 O  O   . HOH M 6 .   ? 17.509  3.426   7.212   1.00 14.65 ? 765 HOH A O   1 
HETATM 7716 O  O   . HOH M 6 .   ? 40.650  27.402  16.699  1.00 21.84 ? 766 HOH A O   1 
HETATM 7717 O  O   . HOH M 6 .   ? -5.188  16.831  0.502   1.00 27.52 ? 767 HOH A O   1 
HETATM 7718 O  O   . HOH M 6 .   ? 21.532  30.423  18.757  1.00 19.06 ? 768 HOH A O   1 
HETATM 7719 O  O   . HOH M 6 .   ? -2.472  -0.071  5.461   1.00 27.53 ? 769 HOH A O   1 
HETATM 7720 O  O   . HOH M 6 .   ? -3.037  7.729   9.729   1.00 21.57 ? 770 HOH A O   1 
HETATM 7721 O  O   . HOH M 6 .   ? 35.602  36.004  8.981   1.00 32.77 ? 771 HOH A O   1 
HETATM 7722 O  O   . HOH M 6 .   ? 14.492  12.974  3.689   1.00 22.33 ? 772 HOH A O   1 
HETATM 7723 O  O   . HOH M 6 .   ? -6.199  16.593  3.293   1.00 21.29 ? 773 HOH A O   1 
HETATM 7724 O  O   . HOH M 6 .   ? 17.224  11.269  26.736  1.00 25.71 ? 774 HOH A O   1 
HETATM 7725 O  O   . HOH M 6 .   ? 23.785  32.094  21.732  1.00 20.85 ? 775 HOH A O   1 
HETATM 7726 O  O   . HOH M 6 .   ? 14.726  4.195   9.487   1.00 13.94 ? 776 HOH A O   1 
HETATM 7727 O  O   . HOH M 6 .   ? -0.199  18.490  23.555  1.00 30.18 ? 777 HOH A O   1 
HETATM 7728 O  O   . HOH M 6 .   ? 22.815  14.910  43.334  1.00 33.31 ? 778 HOH A O   1 
HETATM 7729 O  O   . HOH M 6 .   ? 18.010  33.969  8.147   1.00 14.71 ? 779 HOH A O   1 
HETATM 7730 O  O   . HOH M 6 .   ? 11.636  51.093  24.662  1.00 35.83 ? 780 HOH A O   1 
HETATM 7731 O  O   . HOH M 6 .   ? 14.456  26.772  22.039  1.00 36.80 ? 781 HOH A O   1 
HETATM 7732 O  O   . HOH M 6 .   ? 41.163  30.141  10.146  1.00 21.60 ? 782 HOH A O   1 
HETATM 7733 O  O   . HOH M 6 .   ? 3.660   1.451   9.758   1.00 18.23 ? 783 HOH A O   1 
HETATM 7734 O  O   . HOH M 6 .   ? 1.806   5.871   13.854  1.00 22.58 ? 784 HOH A O   1 
HETATM 7735 O  O   . HOH M 6 .   ? 26.008  40.982  13.402  1.00 15.52 ? 785 HOH A O   1 
HETATM 7736 O  O   . HOH M 6 .   ? 23.586  33.996  36.873  1.00 27.90 ? 786 HOH A O   1 
HETATM 7737 O  O   . HOH M 6 .   ? -5.862  9.844   18.478  1.00 35.36 ? 787 HOH A O   1 
HETATM 7738 O  O   . HOH M 6 .   ? -9.200  18.070  9.576   1.00 25.39 ? 788 HOH A O   1 
HETATM 7739 O  O   . HOH M 6 .   ? 17.909  40.561  4.524   1.00 36.56 ? 789 HOH A O   1 
HETATM 7740 O  O   . HOH M 6 .   ? 13.005  6.019   16.701  1.00 34.44 ? 790 HOH A O   1 
HETATM 7741 O  O   . HOH M 6 .   ? 13.044  24.338  27.956  1.00 30.19 ? 791 HOH A O   1 
HETATM 7742 O  O   . HOH M 6 .   ? 41.145  20.979  16.550  1.00 28.07 ? 792 HOH A O   1 
HETATM 7743 O  O   . HOH M 6 .   ? 2.672   41.582  17.040  1.00 30.08 ? 793 HOH A O   1 
HETATM 7744 O  O   . HOH M 6 .   ? 19.218  16.029  31.499  1.00 29.78 ? 794 HOH A O   1 
HETATM 7745 O  O   . HOH M 6 .   ? 16.838  17.876  24.898  1.00 22.43 ? 795 HOH A O   1 
HETATM 7746 O  O   . HOH M 6 .   ? 16.811  38.333  47.575  1.00 29.93 ? 796 HOH A O   1 
HETATM 7747 O  O   . HOH M 6 .   ? 8.576   3.594   13.503  1.00 21.55 ? 797 HOH A O   1 
HETATM 7748 O  O   . HOH M 6 .   ? 33.746  40.147  14.012  1.00 25.91 ? 798 HOH A O   1 
HETATM 7749 O  O   . HOH M 6 .   ? -8.928  10.383  8.064   1.00 32.67 ? 799 HOH A O   1 
HETATM 7750 O  O   . HOH M 6 .   ? 6.185   19.980  -14.934 1.00 27.88 ? 800 HOH A O   1 
HETATM 7751 O  O   . HOH M 6 .   ? 25.893  38.309  12.714  1.00 16.05 ? 801 HOH A O   1 
HETATM 7752 O  O   . HOH M 6 .   ? 36.039  18.852  1.127   1.00 34.93 ? 802 HOH A O   1 
HETATM 7753 O  O   . HOH M 6 .   ? 34.510  46.789  12.117  1.00 36.15 ? 803 HOH A O   1 
HETATM 7754 O  O   . HOH M 6 .   ? 26.776  43.161  7.876   1.00 29.24 ? 804 HOH A O   1 
HETATM 7755 O  O   . HOH M 6 .   ? 8.085   43.064  16.805  1.00 27.47 ? 805 HOH A O   1 
HETATM 7756 O  O   . HOH M 6 .   ? 20.101  14.830  -8.423  1.00 29.65 ? 806 HOH A O   1 
HETATM 7757 O  O   . HOH M 6 .   ? 11.371  20.779  21.115  1.00 20.96 ? 807 HOH A O   1 
HETATM 7758 O  O   . HOH M 6 .   ? 11.138  10.261  17.396  1.00 24.01 ? 808 HOH A O   1 
HETATM 7759 O  O   . HOH M 6 .   ? 32.218  4.853   9.381   1.00 34.96 ? 809 HOH A O   1 
HETATM 7760 O  O   . HOH M 6 .   ? 7.621   41.358  33.939  1.00 20.51 ? 810 HOH A O   1 
HETATM 7761 O  O   . HOH M 6 .   ? -11.279 22.572  -0.275  1.00 33.05 ? 811 HOH A O   1 
HETATM 7762 O  O   . HOH M 6 .   ? 43.650  14.140  13.326  1.00 30.51 ? 812 HOH A O   1 
HETATM 7763 O  O   . HOH M 6 .   ? 14.976  25.325  26.292  1.00 35.98 ? 813 HOH A O   1 
HETATM 7764 O  O   . HOH M 6 .   ? 15.871  17.129  22.361  1.00 23.93 ? 814 HOH A O   1 
HETATM 7765 O  O   . HOH M 6 .   ? 41.033  21.231  12.952  1.00 23.75 ? 815 HOH A O   1 
HETATM 7766 O  O   . HOH M 6 .   ? 8.800   49.351  21.471  1.00 27.22 ? 816 HOH A O   1 
HETATM 7767 O  O   . HOH M 6 .   ? -5.023  19.017  21.888  1.00 19.13 ? 817 HOH A O   1 
HETATM 7768 O  O   . HOH M 6 .   ? 0.381   29.994  15.958  1.00 25.24 ? 818 HOH A O   1 
HETATM 7769 O  O   . HOH M 6 .   ? -2.482  39.324  13.906  1.00 33.89 ? 819 HOH A O   1 
HETATM 7770 O  O   . HOH M 6 .   ? 3.777   20.325  -13.859 1.00 30.51 ? 820 HOH A O   1 
HETATM 7771 O  O   . HOH M 6 .   ? 27.559  2.797   8.760   1.00 36.15 ? 821 HOH A O   1 
HETATM 7772 O  O   . HOH M 6 .   ? -4.419  31.522  9.713   1.00 24.62 ? 822 HOH A O   1 
HETATM 7773 O  O   . HOH M 6 .   ? 14.829  39.453  5.511   1.00 28.22 ? 823 HOH A O   1 
HETATM 7774 O  O   . HOH M 6 .   ? 4.453   45.087  16.245  1.00 25.61 ? 824 HOH A O   1 
HETATM 7775 O  O   . HOH M 6 .   ? 34.327  29.959  25.095  1.00 32.90 ? 825 HOH A O   1 
HETATM 7776 O  O   . HOH M 6 .   ? -4.784  30.351  0.571   1.00 31.38 ? 826 HOH A O   1 
HETATM 7777 O  O   . HOH M 6 .   ? 25.230  26.186  -5.561  1.00 27.82 ? 827 HOH A O   1 
HETATM 7778 O  O   . HOH M 6 .   ? 5.023   38.242  31.161  1.00 34.80 ? 828 HOH A O   1 
HETATM 7779 O  O   . HOH M 6 .   ? 21.913  37.312  6.598   1.00 22.16 ? 829 HOH A O   1 
HETATM 7780 O  O   . HOH M 6 .   ? -7.399  27.867  4.868   1.00 20.50 ? 830 HOH A O   1 
HETATM 7781 O  O   . HOH M 6 .   ? 11.094  48.751  33.427  1.00 31.65 ? 831 HOH A O   1 
HETATM 7782 O  O   . HOH M 6 .   ? 33.694  16.733  24.529  1.00 30.03 ? 832 HOH A O   1 
HETATM 7783 O  O   . HOH M 6 .   ? 8.767   16.480  -14.291 1.00 21.27 ? 833 HOH A O   1 
HETATM 7784 O  O   . HOH M 6 .   ? 17.407  13.853  -9.342  1.00 20.36 ? 834 HOH A O   1 
HETATM 7785 O  O   . HOH M 6 .   ? 6.824   5.422   19.191  1.00 37.33 ? 835 HOH A O   1 
HETATM 7786 O  O   B HOH M 6 .   ? 16.998  33.207  25.818  0.50 21.19 ? 836 HOH A O   1 
HETATM 7787 O  O   . HOH M 6 .   ? -7.961  26.870  12.378  1.00 31.10 ? 837 HOH A O   1 
HETATM 7788 O  O   . HOH M 6 .   ? -3.419  29.025  11.697  1.00 20.02 ? 838 HOH A O   1 
HETATM 7789 O  O   . HOH M 6 .   ? 38.026  15.377  23.604  1.00 39.30 ? 839 HOH A O   1 
HETATM 7790 O  O   . HOH M 6 .   ? 17.351  27.107  27.995  1.00 34.54 ? 840 HOH A O   1 
HETATM 7791 O  O   . HOH M 6 .   ? 7.903   43.229  20.939  1.00 28.70 ? 841 HOH A O   1 
HETATM 7792 O  O   . HOH M 6 .   ? 24.158  27.801  -2.378  1.00 27.67 ? 842 HOH A O   1 
HETATM 7793 O  O   . HOH M 6 .   ? 9.428   31.157  38.215  1.00 40.64 ? 843 HOH A O   1 
HETATM 7794 O  O   . HOH M 6 .   ? 16.725  26.638  -0.741  1.00 35.47 ? 844 HOH A O   1 
HETATM 7795 O  O   . HOH M 6 .   ? 30.630  4.871   7.366   1.00 42.19 ? 845 HOH A O   1 
HETATM 7796 O  O   . HOH M 6 .   ? 7.246   25.306  33.551  1.00 34.94 ? 846 HOH A O   1 
HETATM 7797 O  O   . HOH M 6 .   ? 14.668  48.690  6.618   1.00 33.50 ? 847 HOH A O   1 
HETATM 7798 O  O   . HOH M 6 .   ? 42.578  15.338  16.652  1.00 28.27 ? 848 HOH A O   1 
HETATM 7799 O  O   . HOH M 6 .   ? 16.866  16.248  -11.412 1.00 19.54 ? 849 HOH A O   1 
HETATM 7800 O  O   . HOH M 6 .   ? -5.768  15.099  -5.217  1.00 36.11 ? 850 HOH A O   1 
HETATM 7801 O  O   . HOH M 6 .   ? 10.673  7.655   -10.550 1.00 35.94 ? 851 HOH A O   1 
HETATM 7802 O  O   . HOH M 6 .   ? 17.502  28.859  0.441   1.00 31.84 ? 852 HOH A O   1 
HETATM 7803 O  O   . HOH M 6 .   ? -1.739  4.832   16.355  1.00 32.26 ? 853 HOH A O   1 
HETATM 7804 O  O   . HOH M 6 .   ? -7.008  19.177  7.316   1.00 38.16 ? 854 HOH A O   1 
HETATM 7805 O  O   . HOH M 6 .   ? 6.399   34.609  37.172  1.00 35.57 ? 855 HOH A O   1 
HETATM 7806 O  O   . HOH M 6 .   ? 35.446  38.584  15.038  1.00 41.11 ? 856 HOH A O   1 
HETATM 7807 O  O   . HOH M 6 .   ? -6.773  24.955  17.615  1.00 37.99 ? 857 HOH A O   1 
HETATM 7808 O  O   . HOH M 6 .   ? 32.096  27.891  26.754  1.00 40.19 ? 858 HOH A O   1 
HETATM 7809 O  O   . HOH M 6 .   ? 12.019  24.379  34.343  1.00 41.17 ? 859 HOH A O   1 
HETATM 7810 O  O   . HOH M 6 .   ? 2.910   40.166  -5.996  1.00 28.39 ? 860 HOH A O   1 
HETATM 7811 O  O   . HOH M 6 .   ? 19.074  51.046  30.875  1.00 32.07 ? 861 HOH A O   1 
HETATM 7812 O  O   . HOH M 6 .   ? -3.436  4.569   5.602   1.00 39.64 ? 862 HOH A O   1 
HETATM 7813 O  O   . HOH M 6 .   ? 23.497  8.416   -3.294  1.00 32.05 ? 863 HOH A O   1 
HETATM 7814 O  O   . HOH M 6 .   ? 12.738  25.352  -10.658 1.00 33.52 ? 864 HOH A O   1 
HETATM 7815 O  O   . HOH M 6 .   ? 15.302  30.417  0.992   1.00 31.29 ? 865 HOH A O   1 
HETATM 7816 O  O   . HOH M 6 .   ? 17.023  20.474  25.520  1.00 27.82 ? 866 HOH A O   1 
HETATM 7817 O  O   . HOH M 6 .   ? 37.816  5.378   18.181  1.00 38.33 ? 867 HOH A O   1 
HETATM 7818 O  O   . HOH M 6 .   ? 24.890  36.128  13.870  1.00 15.13 ? 868 HOH A O   1 
HETATM 7819 O  O   . HOH M 6 .   ? 9.947   14.712  19.099  1.00 38.06 ? 869 HOH A O   1 
HETATM 7820 O  O   . HOH M 6 .   ? 23.241  10.212  -5.847  1.00 31.31 ? 870 HOH A O   1 
HETATM 7821 O  O   . HOH M 6 .   ? 15.721  43.916  44.000  1.00 32.80 ? 871 HOH A O   1 
HETATM 7822 O  O   . HOH M 6 .   ? 8.914   44.906  19.064  1.00 28.95 ? 872 HOH A O   1 
HETATM 7823 O  O   . HOH M 6 .   ? 15.431  15.067  -13.559 1.00 32.80 ? 873 HOH A O   1 
HETATM 7824 O  O   . HOH M 6 .   ? 21.096  31.133  21.338  1.00 43.59 ? 874 HOH A O   1 
HETATM 7825 O  O   . HOH M 6 .   ? 15.655  32.890  4.776   1.00 26.98 ? 875 HOH A O   1 
HETATM 7826 O  O   . HOH M 6 .   ? 16.612  13.275  28.435  1.00 39.42 ? 876 HOH A O   1 
HETATM 7827 O  O   . HOH M 6 .   ? 17.645  -1.763  12.717  1.00 26.06 ? 877 HOH A O   1 
HETATM 7828 O  O   . HOH M 6 .   ? 37.151  22.752  22.088  1.00 39.94 ? 878 HOH A O   1 
HETATM 7829 O  O   . HOH M 6 .   ? 6.576   31.519  32.062  1.00 33.66 ? 879 HOH A O   1 
HETATM 7830 O  O   . HOH M 6 .   ? 1.505   11.964  20.698  1.00 25.28 ? 880 HOH A O   1 
HETATM 7831 O  O   . HOH M 6 .   ? 6.668   21.710  27.727  1.00 22.76 ? 881 HOH A O   1 
HETATM 7832 O  O   . HOH M 6 .   ? 2.749   3.714   14.443  1.00 34.14 ? 882 HOH A O   1 
HETATM 7833 O  O   . HOH M 6 .   ? 9.666   49.756  15.076  1.00 33.19 ? 883 HOH A O   1 
HETATM 7834 O  O   . HOH M 6 .   ? -0.797  12.615  -7.900  1.00 27.62 ? 884 HOH A O   1 
HETATM 7835 O  O   . HOH M 6 .   ? 40.386  32.492  11.101  1.00 30.82 ? 885 HOH A O   1 
HETATM 7836 O  O   . HOH M 6 .   ? 31.260  49.899  16.258  1.00 39.37 ? 886 HOH A O   1 
HETATM 7837 O  O   . HOH M 6 .   ? 3.446   2.264   -1.341  1.00 30.93 ? 887 HOH A O   1 
HETATM 7838 O  O   . HOH M 6 .   ? 11.273  17.404  -14.455 1.00 27.94 ? 888 HOH A O   1 
HETATM 7839 O  O   . HOH M 6 .   ? 14.077  37.549  3.271   1.00 37.50 ? 889 HOH A O   1 
HETATM 7840 O  O   . HOH M 6 .   ? 14.399  17.056  26.156  1.00 39.38 ? 890 HOH A O   1 
HETATM 7841 O  O   . HOH M 6 .   ? 15.465  10.520  24.727  1.00 34.96 ? 891 HOH A O   1 
HETATM 7842 O  O   . HOH M 6 .   ? 13.909  15.600  22.419  1.00 34.67 ? 892 HOH A O   1 
HETATM 7843 O  O   . HOH M 6 .   ? 10.792  18.161  21.524  1.00 29.09 ? 893 HOH A O   1 
HETATM 7844 O  O   . HOH M 6 .   ? -4.155  13.083  -6.364  1.00 30.24 ? 894 HOH A O   1 
HETATM 7845 O  O   . HOH M 6 .   ? 7.839   17.137  20.617  1.00 24.88 ? 895 HOH A O   1 
HETATM 7846 O  O   . HOH M 6 .   ? 16.693  7.873   -6.070  1.00 42.01 ? 896 HOH A O   1 
HETATM 7847 O  O   . HOH M 6 .   ? 15.310  9.030   18.273  1.00 34.58 ? 897 HOH A O   1 
HETATM 7848 O  O   . HOH M 6 .   ? 19.008  17.766  -12.034 1.00 30.84 ? 898 HOH A O   1 
HETATM 7849 O  O   . HOH M 6 .   ? 41.950  6.547   13.500  1.00 29.54 ? 899 HOH A O   1 
HETATM 7850 O  O   . HOH M 6 .   ? 7.417   35.767  32.784  1.00 25.82 ? 900 HOH A O   1 
HETATM 7851 O  O   . HOH M 6 .   ? 0.504   29.455  20.895  1.00 39.00 ? 901 HOH A O   1 
HETATM 7852 O  O   . HOH N 6 .   ? 8.483   -51.546 24.671  1.00 32.86 ? 601 HOH B O   1 
HETATM 7853 O  O   . HOH N 6 .   ? -1.763  -24.711 43.720  1.00 41.35 ? 602 HOH B O   1 
HETATM 7854 O  O   . HOH N 6 .   ? 2.230   -22.955 42.270  1.00 38.49 ? 603 HOH B O   1 
HETATM 7855 O  O   . HOH N 6 .   ? 28.277  -10.877 0.696   1.00 30.14 ? 604 HOH B O   1 
HETATM 7856 O  O   . HOH N 6 .   ? 9.216   -2.503  1.620   1.00 20.47 ? 605 HOH B O   1 
HETATM 7857 O  O   . HOH N 6 .   ? 3.566   -19.069 8.317   1.00 22.74 ? 606 HOH B O   1 
HETATM 7858 O  O   B HOH N 6 .   ? 3.841   -32.860 27.540  0.50 20.81 ? 607 HOH B O   1 
HETATM 7859 O  O   . HOH N 6 .   ? 19.725  -33.018 19.237  1.00 30.93 ? 608 HOH B O   1 
HETATM 7860 O  O   . HOH N 6 .   ? 4.272   -17.412 25.889  1.00 23.91 ? 609 HOH B O   1 
HETATM 7861 O  O   . HOH N 6 .   ? 3.268   -51.575 15.979  1.00 23.43 ? 610 HOH B O   1 
HETATM 7862 O  O   . HOH N 6 .   ? 26.031  0.856   14.887  1.00 29.59 ? 611 HOH B O   1 
HETATM 7863 O  O   . HOH N 6 .   ? -18.212 -25.995 20.305  1.00 19.39 ? 612 HOH B O   1 
HETATM 7864 O  O   . HOH N 6 .   ? -9.563  -39.170 28.152  1.00 31.66 ? 613 HOH B O   1 
HETATM 7865 O  O   . HOH N 6 .   ? 25.143  -32.537 5.932   1.00 30.81 ? 614 HOH B O   1 
HETATM 7866 O  O   . HOH N 6 .   ? 27.577  -7.302  8.932   1.00 32.20 ? 615 HOH B O   1 
HETATM 7867 O  O   . HOH N 6 .   ? 21.577  -32.540 16.417  1.00 28.92 ? 616 HOH B O   1 
HETATM 7868 O  O   . HOH N 6 .   ? 29.803  -21.801 13.115  1.00 36.93 ? 617 HOH B O   1 
HETATM 7869 O  O   . HOH N 6 .   ? 10.223  -1.569  4.236   1.00 16.26 ? 618 HOH B O   1 
HETATM 7870 O  O   . HOH N 6 .   ? -17.057 -32.022 14.137  1.00 24.58 ? 619 HOH B O   1 
HETATM 7871 O  O   . HOH N 6 .   ? 21.238  -42.420 7.798   1.00 34.80 ? 620 HOH B O   1 
HETATM 7872 O  O   . HOH N 6 .   ? -5.392  -48.172 31.473  1.00 34.93 ? 621 HOH B O   1 
HETATM 7873 O  O   . HOH N 6 .   ? -12.143 -52.485 21.816  1.00 37.31 ? 622 HOH B O   1 
HETATM 7874 O  O   . HOH N 6 .   ? 23.675  -14.996 22.094  1.00 26.99 ? 623 HOH B O   1 
HETATM 7875 O  O   . HOH N 6 .   ? 2.827   -16.545 9.260   1.00 20.80 ? 624 HOH B O   1 
HETATM 7876 O  O   . HOH N 6 .   ? -1.438  -54.569 19.585  1.00 33.72 ? 625 HOH B O   1 
HETATM 7877 O  O   . HOH N 6 .   ? -2.093  -5.923  26.350  1.00 29.21 ? 626 HOH B O   1 
HETATM 7878 O  O   . HOH N 6 .   ? -18.256 -19.239 7.406   1.00 21.51 ? 627 HOH B O   1 
HETATM 7879 O  O   . HOH N 6 .   ? 23.589  -16.887 1.059   1.00 17.30 ? 628 HOH B O   1 
HETATM 7880 O  O   . HOH N 6 .   ? 12.368  -26.403 13.141  1.00 21.85 ? 629 HOH B O   1 
HETATM 7881 O  O   . HOH N 6 .   ? 24.494  -32.439 3.327   1.00 32.90 ? 630 HOH B O   1 
HETATM 7882 O  O   . HOH N 6 .   ? 16.893  -37.068 22.656  1.00 24.54 ? 631 HOH B O   1 
HETATM 7883 O  O   . HOH N 6 .   ? 13.936  -19.288 -12.323 1.00 28.81 ? 632 HOH B O   1 
HETATM 7884 O  O   . HOH N 6 .   ? 0.586   -7.770  9.628   1.00 13.68 ? 633 HOH B O   1 
HETATM 7885 O  O   . HOH N 6 .   ? 16.228  -14.681 21.902  1.00 23.36 ? 634 HOH B O   1 
HETATM 7886 O  O   . HOH N 6 .   ? 23.748  -19.629 23.854  1.00 22.02 ? 635 HOH B O   1 
HETATM 7887 O  O   . HOH N 6 .   ? -18.771 -28.392 23.058  1.00 18.78 ? 636 HOH B O   1 
HETATM 7888 O  O   . HOH N 6 .   ? -4.965  -30.256 15.660  1.00 11.72 ? 637 HOH B O   1 
HETATM 7889 O  O   . HOH N 6 .   ? 18.200  -5.818  -1.630  1.00 22.70 ? 638 HOH B O   1 
HETATM 7890 O  O   . HOH N 6 .   ? -1.405  -11.514 -1.606  1.00 26.65 ? 639 HOH B O   1 
HETATM 7891 O  O   . HOH N 6 .   ? 3.916   -6.003  16.099  1.00 27.36 ? 640 HOH B O   1 
HETATM 7892 O  O   . HOH N 6 .   ? 25.271  -25.069 19.121  1.00 20.65 ? 641 HOH B O   1 
HETATM 7893 O  O   . HOH N 6 .   ? 8.696   -12.470 -9.962  1.00 31.88 ? 642 HOH B O   1 
HETATM 7894 O  O   . HOH N 6 .   ? 3.882   -42.244 47.834  1.00 34.80 ? 643 HOH B O   1 
HETATM 7895 O  O   . HOH N 6 .   ? -14.625 -36.130 10.807  1.00 36.56 ? 644 HOH B O   1 
HETATM 7896 O  O   . HOH N 6 .   ? 9.144   2.341   6.109   1.00 14.36 ? 645 HOH B O   1 
HETATM 7897 O  O   . HOH N 6 .   ? -11.244 -15.656 23.628  1.00 35.92 ? 646 HOH B O   1 
HETATM 7898 O  O   . HOH N 6 .   ? 21.358  -9.091  20.774  1.00 30.48 ? 647 HOH B O   1 
HETATM 7899 O  O   . HOH N 6 .   ? 13.170  -48.896 29.840  1.00 28.90 ? 648 HOH B O   1 
HETATM 7900 O  O   . HOH N 6 .   ? -12.897 -49.533 29.327  1.00 34.34 ? 649 HOH B O   1 
HETATM 7901 O  O   . HOH N 6 .   ? -10.525 -40.464 14.801  1.00 19.22 ? 650 HOH B O   1 
HETATM 7902 O  O   . HOH N 6 .   ? -1.099  -30.832 7.350   1.00 19.11 ? 651 HOH B O   1 
HETATM 7903 O  O   . HOH N 6 .   ? 20.643  -0.245  13.068  1.00 22.52 ? 652 HOH B O   1 
HETATM 7904 O  O   . HOH N 6 .   ? 26.694  -16.186 16.265  1.00 15.23 ? 653 HOH B O   1 
HETATM 7905 O  O   . HOH N 6 .   ? -7.033  -37.231 13.343  1.00 13.92 ? 654 HOH B O   1 
HETATM 7906 O  O   . HOH N 6 .   ? 12.710  -32.407 34.891  1.00 24.49 ? 655 HOH B O   1 
HETATM 7907 O  O   . HOH N 6 .   ? -1.792  -24.452 4.600   1.00 16.95 ? 656 HOH B O   1 
HETATM 7908 O  O   . HOH N 6 .   ? 3.627   -2.290  1.929   1.00 21.17 ? 657 HOH B O   1 
HETATM 7909 O  O   . HOH N 6 .   ? -14.898 -42.601 19.502  1.00 29.37 ? 658 HOH B O   1 
HETATM 7910 O  O   . HOH N 6 .   ? 9.450   -48.889 13.329  1.00 25.94 ? 659 HOH B O   1 
HETATM 7911 O  O   . HOH N 6 .   ? 3.843   -24.817 0.481   1.00 22.50 ? 660 HOH B O   1 
HETATM 7912 O  O   . HOH N 6 .   ? 19.325  -14.699 -8.689  1.00 23.54 ? 661 HOH B O   1 
HETATM 7913 O  O   . HOH N 6 .   ? -8.381  -28.649 9.925   1.00 15.23 ? 662 HOH B O   1 
HETATM 7914 O  O   . HOH N 6 .   ? 10.058  -48.063 26.825  1.00 17.44 ? 663 HOH B O   1 
HETATM 7915 O  O   . HOH N 6 .   ? 3.769   -7.838  -3.008  1.00 28.34 ? 664 HOH B O   1 
HETATM 7916 O  O   . HOH N 6 .   ? -19.927 -16.250 8.642   1.00 24.90 ? 665 HOH B O   1 
HETATM 7917 O  O   . HOH N 6 .   ? -10.571 -34.996 29.162  1.00 33.68 ? 666 HOH B O   1 
HETATM 7918 O  O   . HOH N 6 .   ? -0.498  -13.025 -4.919  1.00 22.76 ? 667 HOH B O   1 
HETATM 7919 O  O   . HOH N 6 .   ? 23.088  -3.335  2.236   1.00 27.85 ? 668 HOH B O   1 
HETATM 7920 O  O   . HOH N 6 .   ? 26.181  -17.560 1.118   1.00 26.35 ? 669 HOH B O   1 
HETATM 7921 O  O   . HOH N 6 .   ? -8.240  -23.159 18.430  1.00 12.96 ? 670 HOH B O   1 
HETATM 7922 O  O   . HOH N 6 .   ? 10.290  -47.947 15.619  1.00 15.25 ? 671 HOH B O   1 
HETATM 7923 O  O   . HOH N 6 .   ? -20.431 -4.672  12.169  1.00 28.65 ? 672 HOH B O   1 
HETATM 7924 O  O   . HOH N 6 .   ? -3.022  -32.693 20.963  1.00 11.69 ? 673 HOH B O   1 
HETATM 7925 O  O   . HOH N 6 .   ? -9.037  -47.817 20.256  1.00 20.18 ? 674 HOH B O   1 
HETATM 7926 O  O   . HOH N 6 .   ? 18.267  -25.887 25.570  1.00 18.99 ? 675 HOH B O   1 
HETATM 7927 O  O   . HOH N 6 .   ? 29.065  -22.981 20.444  1.00 32.60 ? 676 HOH B O   1 
HETATM 7928 O  O   . HOH N 6 .   ? -0.411  -2.210  14.281  1.00 27.08 ? 677 HOH B O   1 
HETATM 7929 O  O   . HOH N 6 .   ? -4.661  -41.431 30.623  1.00 18.19 ? 678 HOH B O   1 
HETATM 7930 O  O   . HOH N 6 .   ? -1.035  -47.809 30.352  1.00 32.83 ? 679 HOH B O   1 
HETATM 7931 O  O   . HOH N 6 .   ? -6.619  -30.667 9.335   1.00 14.11 ? 680 HOH B O   1 
HETATM 7932 O  O   . HOH N 6 .   ? 22.991  -6.902  7.592   1.00 26.72 ? 681 HOH B O   1 
HETATM 7933 O  O   . HOH N 6 .   ? 6.496   -29.455 14.653  1.00 16.70 ? 682 HOH B O   1 
HETATM 7934 O  O   . HOH N 6 .   ? -12.219 -35.671 7.749   1.00 35.38 ? 683 HOH B O   1 
HETATM 7935 O  O   . HOH N 6 .   ? 9.294   -25.816 0.127   1.00 23.91 ? 684 HOH B O   1 
HETATM 7936 O  O   . HOH N 6 .   ? -3.285  -49.729 13.888  1.00 19.17 ? 685 HOH B O   1 
HETATM 7937 O  O   . HOH N 6 .   ? 16.312  -20.969 26.774  1.00 24.37 ? 686 HOH B O   1 
HETATM 7938 O  O   . HOH N 6 .   ? 4.923   -42.030 43.530  1.00 28.05 ? 687 HOH B O   1 
HETATM 7939 O  O   . HOH N 6 .   ? 8.101   -17.552 -12.435 1.00 24.50 ? 688 HOH B O   1 
HETATM 7940 O  O   . HOH N 6 .   ? -17.691 -20.276 19.277  1.00 25.84 ? 689 HOH B O   1 
HETATM 7941 O  O   . HOH N 6 .   ? 19.584  -18.784 -13.390 1.00 29.95 ? 690 HOH B O   1 
HETATM 7942 O  O   . HOH N 6 .   ? 7.171   -49.578 10.692  1.00 29.74 ? 691 HOH B O   1 
HETATM 7943 O  O   . HOH N 6 .   ? 18.517  -13.524 19.535  1.00 17.41 ? 692 HOH B O   1 
HETATM 7944 O  O   . HOH N 6 .   ? 6.540   -11.111 20.454  1.00 24.16 ? 693 HOH B O   1 
HETATM 7945 O  O   . HOH N 6 .   ? 13.501  -11.865 22.686  1.00 38.73 ? 694 HOH B O   1 
HETATM 7946 O  O   . HOH N 6 .   ? -19.314 -8.792  14.102  1.00 29.90 ? 695 HOH B O   1 
HETATM 7947 O  O   . HOH N 6 .   ? 23.020  -28.441 17.691  1.00 29.63 ? 696 HOH B O   1 
HETATM 7948 O  O   . HOH N 6 .   ? 10.664  -41.723 12.564  1.00 15.84 ? 697 HOH B O   1 
HETATM 7949 O  O   . HOH N 6 .   ? -17.512 -8.884  16.088  1.00 26.96 ? 698 HOH B O   1 
HETATM 7950 O  O   . HOH N 6 .   ? -9.273  -44.156 30.458  1.00 27.91 ? 699 HOH B O   1 
HETATM 7951 O  O   . HOH N 6 .   ? 2.578   -5.744  9.269   1.00 15.12 ? 700 HOH B O   1 
HETATM 7952 O  O   . HOH N 6 .   ? 14.600  -11.037 -4.525  1.00 23.87 ? 701 HOH B O   1 
HETATM 7953 O  O   . HOH N 6 .   ? -12.458 -18.071 29.086  1.00 36.05 ? 702 HOH B O   1 
HETATM 7954 O  O   . HOH N 6 .   ? -4.125  -27.529 4.707   1.00 29.22 ? 703 HOH B O   1 
HETATM 7955 O  O   . HOH N 6 .   ? -20.778 -13.717 10.234  1.00 39.36 ? 704 HOH B O   1 
HETATM 7956 O  O   . HOH N 6 .   ? 7.647   -16.972 21.098  1.00 35.23 ? 705 HOH B O   1 
HETATM 7957 O  O   . HOH N 6 .   ? 28.178  -27.114 -1.128  1.00 26.99 ? 706 HOH B O   1 
HETATM 7958 O  O   . HOH N 6 .   ? 22.745  -16.761 -3.312  1.00 19.59 ? 707 HOH B O   1 
HETATM 7959 O  O   . HOH N 6 .   ? 3.674   -10.642 27.320  1.00 26.31 ? 708 HOH B O   1 
HETATM 7960 O  O   . HOH N 6 .   ? 12.152  -22.261 28.181  1.00 19.73 ? 709 HOH B O   1 
HETATM 7961 O  O   . HOH N 6 .   ? 22.183  -26.056 -5.407  1.00 24.64 ? 710 HOH B O   1 
HETATM 7962 O  O   . HOH N 6 .   ? 6.831   -31.275 5.148   1.00 23.74 ? 711 HOH B O   1 
HETATM 7963 O  O   . HOH N 6 .   ? -2.626  -33.773 14.761  1.00 10.67 ? 712 HOH B O   1 
HETATM 7964 O  O   . HOH N 6 .   ? -2.375  -14.009 31.267  1.00 23.83 ? 713 HOH B O   1 
HETATM 7965 O  O   . HOH N 6 .   ? -0.509  -50.171 29.129  1.00 25.42 ? 714 HOH B O   1 
HETATM 7966 O  O   . HOH N 6 .   ? -2.774  -31.675 23.623  1.00 24.54 ? 715 HOH B O   1 
HETATM 7967 O  O   . HOH N 6 .   ? 17.606  -8.031  14.553  1.00 15.40 ? 716 HOH B O   1 
HETATM 7968 O  O   . HOH N 6 .   ? 18.131  -30.095 24.523  1.00 33.03 ? 717 HOH B O   1 
HETATM 7969 O  O   . HOH N 6 .   ? -27.996 -27.446 9.944   1.00 29.41 ? 718 HOH B O   1 
HETATM 7970 O  O   . HOH N 6 .   ? 11.586  -30.333 39.857  1.00 37.36 ? 719 HOH B O   1 
HETATM 7971 O  O   . HOH N 6 .   ? 22.494  -14.453 -4.986  1.00 17.95 ? 720 HOH B O   1 
HETATM 7972 O  O   . HOH N 6 .   ? -14.981 -39.729 21.221  1.00 28.81 ? 721 HOH B O   1 
HETATM 7973 O  O   . HOH N 6 .   ? -2.694  -3.171  4.685   1.00 40.41 ? 722 HOH B O   1 
HETATM 7974 O  O   . HOH N 6 .   ? 17.591  -37.549 36.230  1.00 35.34 ? 723 HOH B O   1 
HETATM 7975 O  O   . HOH N 6 .   ? 23.821  -20.508 -8.560  1.00 24.86 ? 724 HOH B O   1 
HETATM 7976 O  O   . HOH N 6 .   ? 21.474  -8.109  -1.546  1.00 15.05 ? 725 HOH B O   1 
HETATM 7977 O  O   . HOH N 6 .   ? -20.546 -35.260 16.981  1.00 36.84 ? 726 HOH B O   1 
HETATM 7978 O  O   . HOH N 6 .   ? 9.025   -42.526 25.015  1.00 13.37 ? 727 HOH B O   1 
HETATM 7979 O  O   . HOH N 6 .   ? -11.205 -34.931 19.674  1.00 12.04 ? 728 HOH B O   1 
HETATM 7980 O  O   . HOH N 6 .   ? 17.163  -10.114 -8.997  1.00 37.63 ? 729 HOH B O   1 
HETATM 7981 O  O   . HOH N 6 .   ? 12.996  -14.196 -8.375  1.00 16.34 ? 730 HOH B O   1 
HETATM 7982 O  O   . HOH N 6 .   ? -10.646 -33.990 6.026   1.00 24.85 ? 731 HOH B O   1 
HETATM 7983 O  O   . HOH N 6 .   ? 25.977  -16.234 21.304  1.00 21.69 ? 732 HOH B O   1 
HETATM 7984 O  O   . HOH N 6 .   ? 29.886  -11.118 8.406   1.00 34.21 ? 733 HOH B O   1 
HETATM 7985 O  O   . HOH N 6 .   ? -13.294 -24.965 14.878  1.00 13.19 ? 734 HOH B O   1 
HETATM 7986 O  O   . HOH N 6 .   ? 7.163   -26.853 26.248  1.00 24.49 ? 735 HOH B O   1 
HETATM 7987 O  O   . HOH N 6 .   ? 9.763   -28.084 3.288   1.00 29.33 ? 736 HOH B O   1 
HETATM 7988 O  O   . HOH N 6 .   ? -19.815 -30.137 9.276   1.00 17.82 ? 737 HOH B O   1 
HETATM 7989 O  O   . HOH N 6 .   ? 6.065   -27.678 32.429  1.00 26.30 ? 738 HOH B O   1 
HETATM 7990 O  O   . HOH N 6 .   ? -3.659  -34.730 18.287  1.00 12.75 ? 739 HOH B O   1 
HETATM 7991 O  O   . HOH N 6 .   ? 24.066  -8.109  9.993   1.00 19.77 ? 740 HOH B O   1 
HETATM 7992 O  O   . HOH N 6 .   ? 27.314  -6.661  16.848  1.00 29.69 ? 741 HOH B O   1 
HETATM 7993 O  O   . HOH N 6 .   ? -5.950  -33.923 29.173  1.00 27.95 ? 742 HOH B O   1 
HETATM 7994 O  O   . HOH N 6 .   ? 19.317  -6.056  14.024  1.00 21.49 ? 743 HOH B O   1 
HETATM 7995 O  O   . HOH N 6 .   ? -9.536  -38.033 14.411  1.00 16.48 ? 744 HOH B O   1 
HETATM 7996 O  O   . HOH N 6 .   ? 4.589   -37.736 49.455  1.00 33.44 ? 745 HOH B O   1 
HETATM 7997 O  O   . HOH N 6 .   ? 17.975  -40.833 6.938   1.00 19.87 ? 746 HOH B O   1 
HETATM 7998 O  O   . HOH N 6 .   ? 7.063   -16.336 27.174  1.00 33.69 ? 747 HOH B O   1 
HETATM 7999 O  O   . HOH N 6 .   ? 9.941   -10.372 17.863  1.00 24.80 ? 748 HOH B O   1 
HETATM 8000 O  O   . HOH N 6 .   ? -7.745  -4.670  22.079  1.00 35.93 ? 749 HOH B O   1 
HETATM 8001 O  O   . HOH N 6 .   ? 18.508  -41.586 18.528  1.00 34.53 ? 750 HOH B O   1 
HETATM 8002 O  O   . HOH N 6 .   ? 8.134   -42.151 45.371  1.00 13.59 ? 751 HOH B O   1 
HETATM 8003 O  O   . HOH N 6 .   ? -0.462  -30.232 20.447  1.00 17.78 ? 752 HOH B O   1 
HETATM 8004 O  O   . HOH N 6 .   ? -13.625 -36.628 23.492  1.00 27.85 ? 753 HOH B O   1 
HETATM 8005 O  O   . HOH N 6 .   ? 3.453   -3.835  7.508   1.00 15.39 ? 754 HOH B O   1 
HETATM 8006 O  O   . HOH N 6 .   ? -16.740 -11.640 17.072  1.00 30.76 ? 755 HOH B O   1 
HETATM 8007 O  O   . HOH N 6 .   ? 11.852  -30.194 -1.410  1.00 21.95 ? 756 HOH B O   1 
HETATM 8008 O  O   . HOH N 6 .   ? 28.748  -21.412 2.928   1.00 21.50 ? 757 HOH B O   1 
HETATM 8009 O  O   . HOH N 6 .   ? -13.388 -20.959 26.061  1.00 33.24 ? 758 HOH B O   1 
HETATM 8010 O  O   . HOH N 6 .   ? 12.864  -43.092 18.761  1.00 27.14 ? 759 HOH B O   1 
HETATM 8011 O  O   . HOH N 6 .   ? 9.604   -2.200  7.526   1.00 16.05 ? 760 HOH B O   1 
HETATM 8012 O  O   . HOH N 6 .   ? 11.768  -31.738 0.847   1.00 31.59 ? 761 HOH B O   1 
HETATM 8013 O  O   . HOH N 6 .   ? 15.069  -35.414 32.074  1.00 20.59 ? 762 HOH B O   1 
HETATM 8014 O  O   . HOH N 6 .   ? -4.939  -38.311 14.740  1.00 14.50 ? 763 HOH B O   1 
HETATM 8015 O  O   . HOH N 6 .   ? -5.017  -40.996 15.574  1.00 13.13 ? 764 HOH B O   1 
HETATM 8016 O  O   . HOH N 6 .   ? -3.602  -35.022 6.919   1.00 29.01 ? 765 HOH B O   1 
HETATM 8017 O  O   . HOH N 6 .   ? 2.866   -34.219 10.075  1.00 12.81 ? 766 HOH B O   1 
HETATM 8018 O  O   . HOH N 6 .   ? 7.388   -4.566  1.055   1.00 17.29 ? 767 HOH B O   1 
HETATM 8019 O  O   . HOH N 6 .   ? 14.885  -29.669 30.912  1.00 30.71 ? 768 HOH B O   1 
HETATM 8020 O  O   . HOH N 6 .   ? 17.462  -1.741  9.780   1.00 17.78 ? 769 HOH B O   1 
HETATM 8021 O  O   . HOH N 6 .   ? -12.740 -3.814  6.757   1.00 40.21 ? 770 HOH B O   1 
HETATM 8022 O  O   . HOH N 6 .   ? 27.216  -26.972 -3.712  1.00 38.39 ? 771 HOH B O   1 
HETATM 8023 O  O   . HOH N 6 .   ? -7.970  -22.545 -2.946  1.00 32.73 ? 772 HOH B O   1 
HETATM 8024 O  O   . HOH N 6 .   ? -20.148 -21.375 14.088  1.00 22.06 ? 773 HOH B O   1 
HETATM 8025 O  O   . HOH N 6 .   ? -1.940  -45.743 11.056  1.00 30.02 ? 774 HOH B O   1 
HETATM 8026 O  O   . HOH N 6 .   ? -6.231  -43.669 10.180  1.00 27.48 ? 775 HOH B O   1 
HETATM 8027 O  O   . HOH N 6 .   ? 7.184   -25.235 31.816  1.00 32.10 ? 776 HOH B O   1 
HETATM 8028 O  O   . HOH N 6 .   ? 16.911  -32.951 25.681  1.00 29.78 ? 777 HOH B O   1 
HETATM 8029 O  O   . HOH N 6 .   ? 6.447   -13.565 4.420   1.00 22.04 ? 778 HOH B O   1 
HETATM 8030 O  O   . HOH N 6 .   ? 1.178   -51.840 30.377  1.00 32.64 ? 779 HOH B O   1 
HETATM 8031 O  O   . HOH N 6 .   ? -19.828 -20.525 18.109  1.00 27.00 ? 780 HOH B O   1 
HETATM 8032 O  O   . HOH N 6 .   ? 7.375   -49.698 35.629  1.00 34.45 ? 781 HOH B O   1 
HETATM 8033 O  O   . HOH N 6 .   ? 6.297   -4.482  9.787   1.00 16.21 ? 782 HOH B O   1 
HETATM 8034 O  O   . HOH N 6 .   ? 30.256  -18.290 10.183  1.00 28.48 ? 783 HOH B O   1 
HETATM 8035 O  O   . HOH N 6 .   ? 8.361   -5.987  17.032  1.00 32.28 ? 784 HOH B O   1 
HETATM 8036 O  O   . HOH N 6 .   ? 16.748  -44.969 18.012  1.00 24.01 ? 785 HOH B O   1 
HETATM 8037 O  O   . HOH N 6 .   ? 28.165  0.488   7.857   1.00 32.61 ? 786 HOH B O   1 
HETATM 8038 O  O   . HOH N 6 .   ? 16.905  -2.453  -3.959  1.00 31.63 ? 787 HOH B O   1 
HETATM 8039 O  O   . HOH N 6 .   ? -13.956 -50.044 24.773  1.00 21.75 ? 788 HOH B O   1 
HETATM 8040 O  O   . HOH N 6 .   ? 4.001   -19.893 26.554  1.00 34.92 ? 789 HOH B O   1 
HETATM 8041 O  O   . HOH N 6 .   ? 0.903   -15.669 -7.152  1.00 32.71 ? 790 HOH B O   1 
HETATM 8042 O  O   . HOH N 6 .   ? 6.464   -24.800 27.676  1.00 39.31 ? 791 HOH B O   1 
HETATM 8043 O  O   . HOH N 6 .   ? -19.709 -27.135 18.300  1.00 19.63 ? 792 HOH B O   1 
HETATM 8044 O  O   . HOH N 6 .   ? 15.946  -4.594  15.965  1.00 23.69 ? 793 HOH B O   1 
HETATM 8045 O  O   . HOH N 6 .   ? 3.506   -14.979 -8.277  1.00 26.45 ? 794 HOH B O   1 
HETATM 8046 O  O   . HOH N 6 .   ? -1.934  -3.486  2.120   1.00 41.36 ? 795 HOH B O   1 
HETATM 8047 O  O   . HOH N 6 .   ? -4.728  -50.574 30.857  1.00 35.99 ? 796 HOH B O   1 
HETATM 8048 O  O   . HOH N 6 .   ? 12.462  -3.705  13.593  1.00 20.48 ? 797 HOH B O   1 
HETATM 8049 O  O   . HOH N 6 .   ? 27.089  -17.238 3.882   1.00 21.40 ? 798 HOH B O   1 
HETATM 8050 O  O   . HOH N 6 .   ? 15.632  -34.549 36.631  1.00 34.90 ? 799 HOH B O   1 
HETATM 8051 O  O   . HOH N 6 .   ? 22.893  -46.209 9.659   1.00 38.60 ? 800 HOH B O   1 
HETATM 8052 O  O   . HOH N 6 .   ? -17.011 -22.974 2.079   1.00 35.14 ? 801 HOH B O   1 
HETATM 8053 O  O   . HOH N 6 .   ? 5.879   -39.829 7.753   1.00 18.23 ? 802 HOH B O   1 
HETATM 8054 O  O   . HOH N 6 .   ? 4.827   -47.082 6.197   1.00 18.91 ? 803 HOH B O   1 
HETATM 8055 O  O   . HOH N 6 .   ? 8.967   -41.912 -5.777  1.00 30.43 ? 804 HOH B O   1 
HETATM 8056 O  O   . HOH N 6 .   ? 5.275   -16.784 23.324  1.00 25.45 ? 805 HOH B O   1 
HETATM 8057 O  O   . HOH N 6 .   ? -20.434 -30.142 11.964  1.00 21.36 ? 806 HOH B O   1 
HETATM 8058 O  O   . HOH N 6 .   ? 14.701  -26.556 35.302  1.00 34.00 ? 807 HOH B O   1 
HETATM 8059 O  O   . HOH N 6 .   ? 23.687  -39.321 15.218  1.00 29.34 ? 808 HOH B O   1 
HETATM 8060 O  O   . HOH N 6 .   ? -1.486  -31.016 36.566  1.00 28.23 ? 809 HOH B O   1 
HETATM 8061 O  O   . HOH N 6 .   ? -12.824 -40.110 16.191  1.00 24.52 ? 810 HOH B O   1 
HETATM 8062 O  O   . HOH N 6 .   ? 12.488  -32.704 -2.142  1.00 27.21 ? 811 HOH B O   1 
HETATM 8063 O  O   . HOH N 6 .   ? -16.112 -35.017 13.087  1.00 31.19 ? 812 HOH B O   1 
HETATM 8064 O  O   . HOH N 6 .   ? 9.735   -44.886 38.975  1.00 29.00 ? 813 HOH B O   1 
HETATM 8065 O  O   . HOH N 6 .   ? 15.903  -7.152  16.671  1.00 22.12 ? 814 HOH B O   1 
HETATM 8066 O  O   . HOH N 6 .   ? -3.339  -40.517 9.458   1.00 30.20 ? 815 HOH B O   1 
HETATM 8067 O  O   . HOH N 6 .   ? 13.728  -40.722 35.754  1.00 20.32 ? 816 HOH B O   1 
HETATM 8068 O  O   . HOH N 6 .   ? -13.361 -29.507 26.858  1.00 26.73 ? 817 HOH B O   1 
HETATM 8069 O  O   . HOH N 6 .   ? 14.995  -39.160 -0.020  1.00 29.98 ? 818 HOH B O   1 
HETATM 8070 O  O   . HOH N 6 .   ? -26.678 -20.724 5.866   1.00 37.92 ? 819 HOH B O   1 
HETATM 8071 O  O   . HOH N 6 .   ? 26.665  -9.824  18.844  1.00 38.38 ? 820 HOH B O   1 
HETATM 8072 O  O   . HOH N 6 .   ? 26.211  -18.781 22.597  1.00 20.81 ? 821 HOH B O   1 
HETATM 8073 O  O   . HOH N 6 .   ? -5.825  -54.560 20.283  1.00 33.42 ? 822 HOH B O   1 
HETATM 8074 O  O   . HOH N 6 .   ? 9.501   -19.977 -12.820 1.00 29.92 ? 823 HOH B O   1 
HETATM 8075 O  O   . HOH N 6 .   ? -8.186  -5.449  9.665   1.00 34.83 ? 824 HOH B O   1 
HETATM 8076 O  O   . HOH N 6 .   ? 1.345   -25.886 43.654  1.00 33.49 ? 825 HOH B O   1 
HETATM 8077 O  O   . HOH N 6 .   ? 11.701  -18.200 -13.305 1.00 26.77 ? 826 HOH B O   1 
HETATM 8078 O  O   . HOH N 6 .   ? 9.833   -20.544 22.252  1.00 20.14 ? 827 HOH B O   1 
HETATM 8079 O  O   . HOH N 6 .   ? 25.418  -31.827 10.861  1.00 23.40 ? 828 HOH B O   1 
HETATM 8080 O  O   . HOH N 6 .   ? 2.536   -40.025 7.576   1.00 20.96 ? 829 HOH B O   1 
HETATM 8081 O  O   . HOH N 6 .   ? 10.446  -48.039 35.386  1.00 31.40 ? 830 HOH B O   1 
HETATM 8082 O  O   . HOH N 6 .   ? 4.619   -53.647 16.652  1.00 24.48 ? 831 HOH B O   1 
HETATM 8083 O  O   . HOH N 6 .   ? 24.466  -29.264 12.788  1.00 21.30 ? 832 HOH B O   1 
HETATM 8084 O  O   . HOH N 6 .   ? 20.734  -30.008 17.384  1.00 26.21 ? 833 HOH B O   1 
HETATM 8085 O  O   . HOH N 6 .   ? 12.467  -49.012 23.686  1.00 24.02 ? 834 HOH B O   1 
HETATM 8086 O  O   . HOH N 6 .   ? -5.450  -39.272 32.690  1.00 26.73 ? 835 HOH B O   1 
HETATM 8087 O  O   . HOH N 6 .   ? -11.200 -5.081  9.763   1.00 31.56 ? 836 HOH B O   1 
HETATM 8088 O  O   . HOH N 6 .   ? 8.128   -23.853 29.441  1.00 32.24 ? 837 HOH B O   1 
HETATM 8089 O  O   . HOH N 6 .   ? -22.671 -14.250 14.041  1.00 30.32 ? 838 HOH B O   1 
HETATM 8090 O  O   . HOH N 6 .   ? 28.416  -28.335 6.057   1.00 21.71 ? 839 HOH B O   1 
HETATM 8091 O  O   . HOH N 6 .   ? 5.259   -30.791 2.876   1.00 31.73 ? 840 HOH B O   1 
HETATM 8092 O  O   . HOH N 6 .   ? -2.032  -33.151 39.030  1.00 38.18 ? 841 HOH B O   1 
HETATM 8093 O  O   . HOH N 6 .   ? 5.582   -48.393 8.869   1.00 30.67 ? 842 HOH B O   1 
HETATM 8094 O  O   . HOH N 6 .   ? 25.263  -27.669 15.313  1.00 40.05 ? 843 HOH B O   1 
HETATM 8095 O  O   . HOH N 6 .   ? 23.172  -4.927  16.412  1.00 27.13 ? 844 HOH B O   1 
HETATM 8096 O  O   . HOH N 6 .   ? -3.933  -42.656 9.438   1.00 33.33 ? 845 HOH B O   1 
HETATM 8097 O  O   . HOH N 6 .   ? -6.295  -15.614 -1.306  1.00 33.97 ? 846 HOH B O   1 
HETATM 8098 O  O   . HOH N 6 .   ? 3.943   -17.805 -10.437 1.00 19.96 ? 847 HOH B O   1 
HETATM 8099 O  O   . HOH N 6 .   ? -1.737  -14.420 33.954  1.00 32.42 ? 848 HOH B O   1 
HETATM 8100 O  O   . HOH N 6 .   ? 28.113  -25.228 17.834  1.00 37.78 ? 849 HOH B O   1 
HETATM 8101 O  O   . HOH N 6 .   ? 14.027  -41.762 33.573  1.00 29.41 ? 850 HOH B O   1 
HETATM 8102 O  O   . HOH N 6 .   ? 4.624   -29.086 30.695  1.00 38.42 ? 851 HOH B O   1 
HETATM 8103 O  O   . HOH N 6 .   ? -16.758 -14.775 24.811  1.00 38.66 ? 852 HOH B O   1 
HETATM 8104 O  O   . HOH N 6 .   ? 21.512  -18.214 24.576  1.00 38.21 ? 853 HOH B O   1 
HETATM 8105 O  O   . HOH N 6 .   ? 9.757   -9.238  -9.770  1.00 31.95 ? 854 HOH B O   1 
HETATM 8106 O  O   . HOH N 6 .   ? 25.574  -5.510  4.716   1.00 36.04 ? 855 HOH B O   1 
HETATM 8107 O  O   . HOH N 6 .   ? -21.513 -15.268 17.507  1.00 31.22 ? 856 HOH B O   1 
HETATM 8108 O  O   . HOH N 6 .   ? -11.064 -26.798 28.275  1.00 36.79 ? 857 HOH B O   1 
HETATM 8109 O  O   . HOH N 6 .   ? 7.072   -26.373 23.490  1.00 32.35 ? 858 HOH B O   1 
HETATM 8110 O  O   . HOH N 6 .   ? 2.124   -50.499 32.936  1.00 23.22 ? 859 HOH B O   1 
HETATM 8111 O  O   . HOH N 6 .   ? 13.414  -42.855 22.828  1.00 28.88 ? 860 HOH B O   1 
HETATM 8112 O  O   . HOH N 6 .   ? 7.888   -24.504 -1.837  1.00 36.86 ? 861 HOH B O   1 
HETATM 8113 O  O   . HOH N 6 .   ? -5.390  -27.448 2.575   1.00 31.74 ? 862 HOH B O   1 
HETATM 8114 O  O   . HOH N 6 .   ? -12.715 -16.286 25.431  1.00 34.54 ? 863 HOH B O   1 
HETATM 8115 O  O   . HOH N 6 .   ? -5.297  -18.582 -4.831  1.00 28.54 ? 864 HOH B O   1 
HETATM 8116 O  O   . HOH N 6 .   ? 10.564  -0.176  9.389   1.00 16.06 ? 865 HOH B O   1 
HETATM 8117 O  O   . HOH N 6 .   ? 10.566  -20.242 28.909  1.00 37.77 ? 866 HOH B O   1 
HETATM 8118 O  O   . HOH N 6 .   ? 5.369   -33.415 5.928   1.00 32.06 ? 867 HOH B O   1 
HETATM 8119 O  O   . HOH N 6 .   ? 17.525  -33.538 38.804  1.00 42.81 ? 868 HOH B O   1 
HETATM 8120 O  O   . HOH N 6 .   ? 12.167  -44.758 21.122  1.00 27.79 ? 869 HOH B O   1 
HETATM 8121 O  O   . HOH N 6 .   ? 10.322  -50.574 26.353  1.00 37.25 ? 870 HOH B O   1 
HETATM 8122 O  O   . HOH N 6 .   ? 27.640  -19.970 0.979   1.00 29.03 ? 871 HOH B O   1 
HETATM 8123 O  O   . HOH N 6 .   ? 26.071  -31.061 1.708   1.00 40.05 ? 872 HOH B O   1 
HETATM 8124 O  O   . HOH N 6 .   ? 5.946   -4.048  -0.730  1.00 38.21 ? 873 HOH B O   1 
HETATM 8125 O  O   . HOH N 6 .   ? 17.754  -34.849 23.910  1.00 33.54 ? 874 HOH B O   1 
HETATM 8126 O  O   . HOH N 6 .   ? -0.559  -31.062 22.932  1.00 35.99 ? 875 HOH B O   1 
HETATM 8127 O  O   . HOH N 6 .   ? 3.234   1.624   12.820  1.00 28.61 ? 876 HOH B O   1 
HETATM 8128 O  O   . HOH N 6 .   ? -3.954  -36.054 15.960  1.00 13.50 ? 877 HOH B O   1 
HETATM 8129 O  O   . HOH N 6 .   ? 25.371  -22.709 -9.401  1.00 38.97 ? 878 HOH B O   1 
HETATM 8130 O  O   . HOH N 6 .   ? 5.686   -43.275 46.019  1.00 26.68 ? 879 HOH B O   1 
HETATM 8131 O  O   . HOH N 6 .   ? 5.128   -40.823 49.948  1.00 37.17 ? 880 HOH B O   1 
HETATM 8132 O  O   . HOH N 6 .   ? 19.745  -11.840 21.232  1.00 23.71 ? 881 HOH B O   1 
HETATM 8133 O  O   . HOH N 6 .   ? 11.285  -14.245 20.096  1.00 38.73 ? 882 HOH B O   1 
HETATM 8134 O  O   . HOH N 6 .   ? 25.796  -17.930 -4.176  1.00 46.48 ? 883 HOH B O   1 
HETATM 8135 O  O   . HOH N 6 .   ? -20.290 -24.950 21.791  1.00 34.60 ? 884 HOH B O   1 
HETATM 8136 O  O   . HOH N 6 .   ? -13.089 -41.069 26.149  1.00 39.09 ? 885 HOH B O   1 
HETATM 8137 O  O   . HOH N 6 .   ? 14.540  -21.307 28.803  1.00 26.39 ? 886 HOH B O   1 
HETATM 8138 O  O   . HOH N 6 .   ? 11.547  -49.959 16.995  1.00 24.90 ? 887 HOH B O   1 
HETATM 8139 O  O   . HOH N 6 .   ? 1.657   -12.595 -6.869  1.00 31.41 ? 888 HOH B O   1 
HETATM 8140 O  O   . HOH N 6 .   ? 7.832   -49.028 8.266   1.00 39.48 ? 889 HOH B O   1 
HETATM 8141 O  O   . HOH N 6 .   ? 14.961  -41.731 4.792   1.00 41.86 ? 890 HOH B O   1 
HETATM 8142 O  O   . HOH N 6 .   ? 21.546  -13.750 -7.517  1.00 27.83 ? 891 HOH B O   1 
HETATM 8143 O  O   . HOH N 6 .   ? 8.591   -27.980 1.291   1.00 31.23 ? 892 HOH B O   1 
HETATM 8144 O  O   . HOH N 6 .   ? 18.497  -3.787  14.592  1.00 30.60 ? 893 HOH B O   1 
HETATM 8145 O  O   . HOH N 6 .   ? 17.386  -3.188  -1.179  1.00 30.43 ? 894 HOH B O   1 
HETATM 8146 O  O   . HOH N 6 .   ? -19.600 -32.591 13.087  1.00 27.47 ? 895 HOH B O   1 
HETATM 8147 O  O   . HOH N 6 .   ? 10.451  -18.045 22.403  1.00 27.16 ? 896 HOH B O   1 
HETATM 8148 O  O   . HOH N 6 .   ? -26.976 -20.928 9.099   1.00 35.88 ? 897 HOH B O   1 
HETATM 8149 O  O   . HOH N 6 .   ? 5.861   -8.996  18.871  1.00 38.74 ? 898 HOH B O   1 
HETATM 8150 O  O   . HOH N 6 .   ? -3.632  -3.535  26.121  1.00 39.15 ? 899 HOH B O   1 
HETATM 8151 O  O   . HOH N 6 .   ? 13.308  -16.946 21.554  1.00 25.42 ? 900 HOH B O   1 
HETATM 8152 O  O   . HOH N 6 .   ? -4.471  -29.112 0.709   1.00 39.47 ? 901 HOH B O   1 
HETATM 8153 O  O   . HOH N 6 .   ? -20.893 -6.673  13.874  1.00 31.33 ? 902 HOH B O   1 
HETATM 8154 O  O   . HOH N 6 .   ? 5.762   -10.046 25.411  1.00 33.43 ? 903 HOH B O   1 
HETATM 8155 O  O   . HOH N 6 .   ? 1.617   -19.332 -10.559 1.00 29.79 ? 904 HOH B O   1 
HETATM 8156 O  O   . HOH N 6 .   ? 24.927  -14.166 -6.071  1.00 30.19 ? 905 HOH B O   1 
HETATM 8157 O  O   . HOH N 6 .   ? -22.969 -31.066 12.172  1.00 35.55 ? 906 HOH B O   1 
HETATM 8158 O  O   . HOH N 6 .   ? 25.617  -18.795 -6.994  1.00 40.89 ? 907 HOH B O   1 
HETATM 8159 O  O   . HOH N 6 .   ? 16.668  -33.080 32.147  1.00 28.87 ? 908 HOH B O   1 
HETATM 8160 O  O   . HOH N 6 .   ? 13.886  -35.039 34.602  1.00 27.73 ? 909 HOH B O   1 
HETATM 8161 O  O   . HOH N 6 .   ? 20.431  -29.540 22.709  1.00 42.78 ? 910 HOH B O   1 
# 
