data_9IST
# 
_entry.id   9IST 
# 
_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   9IST         pdb_00009ist 10.2210/pdb9ist/pdb 
WWPDB D_1300048450 ?            ?                   
# 
_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                        9IST 
_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 
'Sugimoto, H.' 2 0000-0002-3140-8362 
'Shoji, O.'    3 0000-0003-3522-0065 
# 
_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' 52224.555 2   1.14.14.1,1.6.2.4 
'P25V, 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    7   ?                 ? ? ? 
6 water       nat water                                                18.015    358 ?                 ? ? ? 
# 
_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       
;TIKEMPQPKTFGELKNLPLLNTDKVVQALMKIADELGEIFKFEAPGWVLRYLSSQRLIKEACDESRFDKNLSQVLKFVRD
FAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKPQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TIKEMPQPKTFGELKNLPLLNTDKVVQALMKIADELGEIFKFEAPGWVLRYLSSQRLIKEACDESRFDKNLSQVLKFVRD
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  VAL 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   1   THR THR 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  VAL 25  25  25  VAL VAL 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   1   THR THR 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  VAL 25  25  25  VAL VAL 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 5 GOL 1   506 605 GOL GOL B . 
N 5 GOL 1   507 606 GOL GOL B . 
O 5 GOL 1   508 607 GOL GOL B . 
P 6 HOH 1   601 63  HOH HOH A . 
P 6 HOH 2   602 58  HOH HOH A . 
P 6 HOH 3   603 295 HOH HOH A . 
P 6 HOH 4   604 151 HOH HOH A . 
P 6 HOH 5   605 185 HOH HOH A . 
P 6 HOH 6   606 339 HOH HOH A . 
P 6 HOH 7   607 191 HOH HOH A . 
P 6 HOH 8   608 194 HOH HOH A . 
P 6 HOH 9   609 112 HOH HOH A . 
P 6 HOH 10  610 71  HOH HOH A . 
P 6 HOH 11  611 317 HOH HOH A . 
P 6 HOH 12  612 77  HOH HOH A . 
P 6 HOH 13  613 41  HOH HOH A . 
P 6 HOH 14  614 348 HOH HOH A . 
P 6 HOH 15  615 82  HOH HOH A . 
P 6 HOH 16  616 199 HOH HOH A . 
P 6 HOH 17  617 335 HOH HOH A . 
P 6 HOH 18  618 217 HOH HOH A . 
P 6 HOH 19  619 68  HOH HOH A . 
P 6 HOH 20  620 318 HOH HOH A . 
P 6 HOH 21  621 8   HOH HOH A . 
P 6 HOH 22  622 282 HOH HOH A . 
P 6 HOH 23  623 237 HOH HOH A . 
P 6 HOH 24  624 3   HOH HOH A . 
P 6 HOH 25  625 219 HOH HOH A . 
P 6 HOH 26  626 1   HOH HOH A . 
P 6 HOH 27  627 48  HOH HOH A . 
P 6 HOH 28  628 205 HOH HOH A . 
P 6 HOH 29  629 279 HOH HOH A . 
P 6 HOH 30  630 320 HOH HOH A . 
P 6 HOH 31  631 193 HOH HOH A . 
P 6 HOH 32  632 17  HOH HOH A . 
P 6 HOH 33  633 93  HOH HOH A . 
P 6 HOH 34  634 81  HOH HOH A . 
P 6 HOH 35  635 215 HOH HOH A . 
P 6 HOH 36  636 181 HOH HOH A . 
P 6 HOH 37  637 131 HOH HOH A . 
P 6 HOH 38  638 323 HOH HOH A . 
P 6 HOH 39  639 211 HOH HOH A . 
P 6 HOH 40  640 30  HOH HOH A . 
P 6 HOH 41  641 23  HOH HOH A . 
P 6 HOH 42  642 101 HOH HOH A . 
P 6 HOH 43  643 85  HOH HOH A . 
P 6 HOH 44  644 43  HOH HOH A . 
P 6 HOH 45  645 299 HOH HOH A . 
P 6 HOH 46  646 337 HOH HOH A . 
P 6 HOH 47  647 46  HOH HOH A . 
P 6 HOH 48  648 12  HOH HOH A . 
P 6 HOH 49  649 55  HOH HOH A . 
P 6 HOH 50  650 189 HOH HOH A . 
P 6 HOH 51  651 186 HOH HOH A . 
P 6 HOH 52  652 158 HOH HOH A . 
P 6 HOH 53  653 115 HOH HOH A . 
P 6 HOH 54  654 289 HOH HOH A . 
P 6 HOH 55  655 152 HOH HOH A . 
P 6 HOH 56  656 40  HOH HOH A . 
P 6 HOH 57  657 16  HOH HOH A . 
P 6 HOH 58  658 96  HOH HOH A . 
P 6 HOH 59  659 206 HOH HOH A . 
P 6 HOH 60  660 328 HOH HOH A . 
P 6 HOH 61  661 336 HOH HOH A . 
P 6 HOH 62  662 91  HOH HOH A . 
P 6 HOH 63  663 331 HOH HOH A . 
P 6 HOH 64  664 200 HOH HOH A . 
P 6 HOH 65  665 260 HOH HOH A . 
P 6 HOH 66  666 35  HOH HOH A . 
P 6 HOH 67  667 226 HOH HOH A . 
P 6 HOH 68  668 311 HOH HOH A . 
P 6 HOH 69  669 107 HOH HOH A . 
P 6 HOH 70  670 94  HOH HOH A . 
P 6 HOH 71  671 104 HOH HOH A . 
P 6 HOH 72  672 327 HOH HOH A . 
P 6 HOH 73  673 80  HOH HOH A . 
P 6 HOH 74  674 44  HOH HOH A . 
P 6 HOH 75  675 114 HOH HOH A . 
P 6 HOH 76  676 284 HOH HOH A . 
P 6 HOH 77  677 165 HOH HOH A . 
P 6 HOH 78  678 149 HOH HOH A . 
P 6 HOH 79  679 305 HOH HOH A . 
P 6 HOH 80  680 164 HOH HOH A . 
P 6 HOH 81  681 280 HOH HOH A . 
P 6 HOH 82  682 242 HOH HOH A . 
P 6 HOH 83  683 274 HOH HOH A . 
P 6 HOH 84  684 307 HOH HOH A . 
P 6 HOH 85  685 51  HOH HOH A . 
P 6 HOH 86  686 209 HOH HOH A . 
P 6 HOH 87  687 37  HOH HOH A . 
P 6 HOH 88  688 296 HOH HOH A . 
P 6 HOH 89  689 179 HOH HOH A . 
P 6 HOH 90  690 89  HOH HOH A . 
P 6 HOH 91  691 76  HOH HOH A . 
P 6 HOH 92  692 156 HOH HOH A . 
P 6 HOH 93  693 177 HOH HOH A . 
P 6 HOH 94  694 298 HOH HOH A . 
P 6 HOH 95  695 183 HOH HOH A . 
P 6 HOH 96  696 315 HOH HOH A . 
P 6 HOH 97  697 291 HOH HOH A . 
P 6 HOH 98  698 201 HOH HOH A . 
P 6 HOH 99  699 116 HOH HOH A . 
P 6 HOH 100 700 36  HOH HOH A . 
P 6 HOH 101 701 286 HOH HOH A . 
P 6 HOH 102 702 155 HOH HOH A . 
P 6 HOH 103 703 27  HOH HOH A . 
P 6 HOH 104 704 338 HOH HOH A . 
P 6 HOH 105 705 278 HOH HOH A . 
P 6 HOH 106 706 62  HOH HOH A . 
P 6 HOH 107 707 69  HOH HOH A . 
P 6 HOH 108 708 354 HOH HOH A . 
P 6 HOH 109 709 33  HOH HOH A . 
P 6 HOH 110 710 144 HOH HOH A . 
P 6 HOH 111 711 208 HOH HOH A . 
P 6 HOH 112 712 92  HOH HOH A . 
P 6 HOH 113 713 170 HOH HOH A . 
P 6 HOH 114 714 272 HOH HOH A . 
P 6 HOH 115 715 178 HOH HOH A . 
P 6 HOH 116 716 39  HOH HOH A . 
P 6 HOH 117 717 88  HOH HOH A . 
P 6 HOH 118 718 120 HOH HOH A . 
P 6 HOH 119 719 83  HOH HOH A . 
P 6 HOH 120 720 300 HOH HOH A . 
P 6 HOH 121 721 53  HOH HOH A . 
P 6 HOH 122 722 167 HOH HOH A . 
P 6 HOH 123 723 65  HOH HOH A . 
P 6 HOH 124 724 261 HOH HOH A . 
P 6 HOH 125 725 216 HOH HOH A . 
P 6 HOH 126 726 28  HOH HOH A . 
P 6 HOH 127 727 316 HOH HOH A . 
P 6 HOH 128 728 78  HOH HOH A . 
P 6 HOH 129 729 184 HOH HOH A . 
P 6 HOH 130 730 329 HOH HOH A . 
P 6 HOH 131 731 275 HOH HOH A . 
P 6 HOH 132 732 309 HOH HOH A . 
P 6 HOH 133 733 154 HOH HOH A . 
P 6 HOH 134 734 269 HOH HOH A . 
P 6 HOH 135 735 258 HOH HOH A . 
P 6 HOH 136 736 56  HOH HOH A . 
P 6 HOH 137 737 175 HOH HOH A . 
P 6 HOH 138 738 266 HOH HOH A . 
P 6 HOH 139 739 10  HOH HOH A . 
P 6 HOH 140 740 163 HOH HOH A . 
P 6 HOH 141 741 301 HOH HOH A . 
P 6 HOH 142 742 359 HOH HOH A . 
P 6 HOH 143 743 161 HOH HOH A . 
P 6 HOH 144 744 57  HOH HOH A . 
P 6 HOH 145 745 363 HOH HOH A . 
P 6 HOH 146 746 111 HOH HOH A . 
P 6 HOH 147 747 182 HOH HOH A . 
P 6 HOH 148 748 70  HOH HOH A . 
P 6 HOH 149 749 192 HOH HOH A . 
P 6 HOH 150 750 123 HOH HOH A . 
P 6 HOH 151 751 139 HOH HOH A . 
P 6 HOH 152 752 72  HOH HOH A . 
P 6 HOH 153 753 259 HOH HOH A . 
P 6 HOH 154 754 361 HOH HOH A . 
P 6 HOH 155 755 210 HOH HOH A . 
P 6 HOH 156 756 148 HOH HOH A . 
P 6 HOH 157 757 187 HOH HOH A . 
P 6 HOH 158 758 332 HOH HOH A . 
P 6 HOH 159 759 146 HOH HOH A . 
P 6 HOH 160 760 119 HOH HOH A . 
P 6 HOH 161 761 145 HOH HOH A . 
P 6 HOH 162 762 360 HOH HOH A . 
P 6 HOH 163 763 126 HOH HOH A . 
P 6 HOH 164 764 343 HOH HOH A . 
P 6 HOH 165 765 238 HOH HOH A . 
P 6 HOH 166 766 277 HOH HOH A . 
P 6 HOH 167 767 173 HOH HOH A . 
P 6 HOH 168 768 230 HOH HOH A . 
P 6 HOH 169 769 366 HOH HOH A . 
P 6 HOH 170 770 150 HOH HOH A . 
P 6 HOH 171 771 265 HOH HOH A . 
P 6 HOH 172 772 250 HOH HOH A . 
P 6 HOH 173 773 231 HOH HOH A . 
P 6 HOH 174 774 239 HOH HOH A . 
P 6 HOH 175 775 257 HOH HOH A . 
P 6 HOH 176 776 255 HOH HOH A . 
P 6 HOH 177 777 147 HOH HOH A . 
P 6 HOH 178 778 267 HOH HOH A . 
P 6 HOH 179 779 333 HOH HOH A . 
P 6 HOH 180 780 356 HOH HOH A . 
P 6 HOH 181 781 353 HOH HOH A . 
P 6 HOH 182 782 342 HOH HOH A . 
Q 6 HOH 1   601 121 HOH HOH B . 
Q 6 HOH 2   602 198 HOH HOH B . 
Q 6 HOH 3   603 334 HOH HOH B . 
Q 6 HOH 4   604 133 HOH HOH B . 
Q 6 HOH 5   605 213 HOH HOH B . 
Q 6 HOH 6   606 19  HOH HOH B . 
Q 6 HOH 7   607 109 HOH HOH B . 
Q 6 HOH 8   608 324 HOH HOH B . 
Q 6 HOH 9   609 73  HOH HOH B . 
Q 6 HOH 10  610 136 HOH HOH B . 
Q 6 HOH 11  611 341 HOH HOH B . 
Q 6 HOH 12  612 130 HOH HOH B . 
Q 6 HOH 13  613 137 HOH HOH B . 
Q 6 HOH 14  614 38  HOH HOH B . 
Q 6 HOH 15  615 221 HOH HOH B . 
Q 6 HOH 16  616 248 HOH HOH B . 
Q 6 HOH 17  617 273 HOH HOH B . 
Q 6 HOH 18  618 344 HOH HOH B . 
Q 6 HOH 19  619 281 HOH HOH B . 
Q 6 HOH 20  620 245 HOH HOH B . 
Q 6 HOH 21  621 358 HOH HOH B . 
Q 6 HOH 22  622 64  HOH HOH B . 
Q 6 HOH 23  623 222 HOH HOH B . 
Q 6 HOH 24  624 172 HOH HOH B . 
Q 6 HOH 25  625 294 HOH HOH B . 
Q 6 HOH 26  626 195 HOH HOH B . 
Q 6 HOH 27  627 129 HOH HOH B . 
Q 6 HOH 28  628 204 HOH HOH B . 
Q 6 HOH 29  629 2   HOH HOH B . 
Q 6 HOH 30  630 60  HOH HOH B . 
Q 6 HOH 31  631 108 HOH HOH B . 
Q 6 HOH 32  632 26  HOH HOH B . 
Q 6 HOH 33  633 326 HOH HOH B . 
Q 6 HOH 34  634 34  HOH HOH B . 
Q 6 HOH 35  635 15  HOH HOH B . 
Q 6 HOH 36  636 13  HOH HOH B . 
Q 6 HOH 37  637 138 HOH HOH B . 
Q 6 HOH 38  638 322 HOH HOH B . 
Q 6 HOH 39  639 223 HOH HOH B . 
Q 6 HOH 40  640 6   HOH HOH B . 
Q 6 HOH 41  641 330 HOH HOH B . 
Q 6 HOH 42  642 118 HOH HOH B . 
Q 6 HOH 43  643 362 HOH HOH B . 
Q 6 HOH 44  644 50  HOH HOH B . 
Q 6 HOH 45  645 7   HOH HOH B . 
Q 6 HOH 46  646 197 HOH HOH B . 
Q 6 HOH 47  647 14  HOH HOH B . 
Q 6 HOH 48  648 5   HOH HOH B . 
Q 6 HOH 49  649 319 HOH HOH B . 
Q 6 HOH 50  650 59  HOH HOH B . 
Q 6 HOH 51  651 132 HOH HOH B . 
Q 6 HOH 52  652 176 HOH HOH B . 
Q 6 HOH 53  653 105 HOH HOH B . 
Q 6 HOH 54  654 21  HOH HOH B . 
Q 6 HOH 55  655 24  HOH HOH B . 
Q 6 HOH 56  656 243 HOH HOH B . 
Q 6 HOH 57  657 102 HOH HOH B . 
Q 6 HOH 58  658 90  HOH HOH B . 
Q 6 HOH 59  659 190 HOH HOH B . 
Q 6 HOH 60  660 32  HOH HOH B . 
Q 6 HOH 61  661 174 HOH HOH B . 
Q 6 HOH 62  662 287 HOH HOH B . 
Q 6 HOH 63  663 283 HOH HOH B . 
Q 6 HOH 64  664 122 HOH HOH B . 
Q 6 HOH 65  665 61  HOH HOH B . 
Q 6 HOH 66  666 84  HOH HOH B . 
Q 6 HOH 67  667 292 HOH HOH B . 
Q 6 HOH 68  668 117 HOH HOH B . 
Q 6 HOH 69  669 29  HOH HOH B . 
Q 6 HOH 70  670 214 HOH HOH B . 
Q 6 HOH 71  671 166 HOH HOH B . 
Q 6 HOH 72  672 196 HOH HOH B . 
Q 6 HOH 73  673 256 HOH HOH B . 
Q 6 HOH 74  674 312 HOH HOH B . 
Q 6 HOH 75  675 11  HOH HOH B . 
Q 6 HOH 76  676 110 HOH HOH B . 
Q 6 HOH 77  677 207 HOH HOH B . 
Q 6 HOH 78  678 9   HOH HOH B . 
Q 6 HOH 79  679 97  HOH HOH B . 
Q 6 HOH 80  680 262 HOH HOH B . 
Q 6 HOH 81  681 349 HOH HOH B . 
Q 6 HOH 82  682 31  HOH HOH B . 
Q 6 HOH 83  683 313 HOH HOH B . 
Q 6 HOH 84  684 171 HOH HOH B . 
Q 6 HOH 85  685 218 HOH HOH B . 
Q 6 HOH 86  686 290 HOH HOH B . 
Q 6 HOH 87  687 106 HOH HOH B . 
Q 6 HOH 88  688 225 HOH HOH B . 
Q 6 HOH 89  689 325 HOH HOH B . 
Q 6 HOH 90  690 4   HOH HOH B . 
Q 6 HOH 91  691 285 HOH HOH B . 
Q 6 HOH 92  692 168 HOH HOH B . 
Q 6 HOH 93  693 42  HOH HOH B . 
Q 6 HOH 94  694 306 HOH HOH B . 
Q 6 HOH 95  695 308 HOH HOH B . 
Q 6 HOH 96  696 45  HOH HOH B . 
Q 6 HOH 97  697 268 HOH HOH B . 
Q 6 HOH 98  698 271 HOH HOH B . 
Q 6 HOH 99  699 18  HOH HOH B . 
Q 6 HOH 100 700 140 HOH HOH B . 
Q 6 HOH 101 701 47  HOH HOH B . 
Q 6 HOH 102 702 276 HOH HOH B . 
Q 6 HOH 103 703 66  HOH HOH B . 
Q 6 HOH 104 704 355 HOH HOH B . 
Q 6 HOH 105 705 293 HOH HOH B . 
Q 6 HOH 106 706 79  HOH HOH B . 
Q 6 HOH 107 707 212 HOH HOH B . 
Q 6 HOH 108 708 98  HOH HOH B . 
Q 6 HOH 109 709 288 HOH HOH B . 
Q 6 HOH 110 710 95  HOH HOH B . 
Q 6 HOH 111 711 75  HOH HOH B . 
Q 6 HOH 112 712 180 HOH HOH B . 
Q 6 HOH 113 713 20  HOH HOH B . 
Q 6 HOH 114 714 303 HOH HOH B . 
Q 6 HOH 115 715 253 HOH HOH B . 
Q 6 HOH 116 716 141 HOH HOH B . 
Q 6 HOH 117 717 135 HOH HOH B . 
Q 6 HOH 118 718 357 HOH HOH B . 
Q 6 HOH 119 719 127 HOH HOH B . 
Q 6 HOH 120 720 157 HOH HOH B . 
Q 6 HOH 121 721 169 HOH HOH B . 
Q 6 HOH 122 722 297 HOH HOH B . 
Q 6 HOH 123 723 128 HOH HOH B . 
Q 6 HOH 124 724 49  HOH HOH B . 
Q 6 HOH 125 725 302 HOH HOH B . 
Q 6 HOH 126 726 100 HOH HOH B . 
Q 6 HOH 127 727 153 HOH HOH B . 
Q 6 HOH 128 728 220 HOH HOH B . 
Q 6 HOH 129 729 113 HOH HOH B . 
Q 6 HOH 130 730 99  HOH HOH B . 
Q 6 HOH 131 731 25  HOH HOH B . 
Q 6 HOH 132 732 270 HOH HOH B . 
Q 6 HOH 133 733 74  HOH HOH B . 
Q 6 HOH 134 734 364 HOH HOH B . 
Q 6 HOH 135 735 22  HOH HOH B . 
Q 6 HOH 136 736 52  HOH HOH B . 
Q 6 HOH 137 737 188 HOH HOH B . 
Q 6 HOH 138 738 252 HOH HOH B . 
Q 6 HOH 139 739 314 HOH HOH B . 
Q 6 HOH 140 740 224 HOH HOH B . 
Q 6 HOH 141 741 67  HOH HOH B . 
Q 6 HOH 142 742 249 HOH HOH B . 
Q 6 HOH 143 743 103 HOH HOH B . 
Q 6 HOH 144 744 347 HOH HOH B . 
Q 6 HOH 145 745 365 HOH HOH B . 
Q 6 HOH 146 746 228 HOH HOH B . 
Q 6 HOH 147 747 346 HOH HOH B . 
Q 6 HOH 148 748 124 HOH HOH B . 
Q 6 HOH 149 749 236 HOH HOH B . 
Q 6 HOH 150 750 160 HOH HOH B . 
Q 6 HOH 151 751 142 HOH HOH B . 
Q 6 HOH 152 752 235 HOH HOH B . 
Q 6 HOH 153 753 134 HOH HOH B . 
Q 6 HOH 154 754 125 HOH HOH B . 
Q 6 HOH 155 755 264 HOH HOH B . 
Q 6 HOH 156 756 351 HOH HOH B . 
Q 6 HOH 157 757 229 HOH HOH B . 
Q 6 HOH 158 758 227 HOH HOH B . 
Q 6 HOH 159 759 241 HOH HOH B . 
Q 6 HOH 160 760 233 HOH HOH B . 
Q 6 HOH 161 761 350 HOH HOH B . 
Q 6 HOH 162 762 159 HOH HOH B . 
Q 6 HOH 163 763 352 HOH HOH B . 
Q 6 HOH 164 764 86  HOH HOH B . 
Q 6 HOH 165 765 240 HOH HOH B . 
Q 6 HOH 166 766 340 HOH HOH B . 
Q 6 HOH 167 767 143 HOH HOH B . 
Q 6 HOH 168 768 244 HOH HOH B . 
Q 6 HOH 169 769 87  HOH HOH B . 
Q 6 HOH 170 770 246 HOH HOH B . 
Q 6 HOH 171 771 202 HOH HOH B . 
Q 6 HOH 172 772 247 HOH HOH B . 
Q 6 HOH 173 773 234 HOH HOH B . 
Q 6 HOH 174 774 232 HOH HOH B . 
Q 6 HOH 175 775 254 HOH HOH B . 
Q 6 HOH 176 776 345 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                   98.91 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IST 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.482 
_cell.length_a_esd                 ? 
_cell.length_b                     148.785 
_cell.length_b_esd                 ? 
_cell.length_c                     61.374 
_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                         9IST 
_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                   9IST 
_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             2.60 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.69 
_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         2022-01-19 
_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                                       9IST 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.27 
_reflns.d_resolution_low                               47.00 
_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                                     46574 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.5 
_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                                0.351 
_reflns.pdbx_Rpim_I_all                                0.141 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       282581 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.970 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.319 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.27 
_reflns_shell.d_res_low                                     2.34 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4291 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.2 
_reflns_shell.pdbx_chi_squared                              0.99 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.453 
_reflns_shell.pdbx_Rpim_I_all                               0.582 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.539 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.327 
_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]                            -2.01 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.79 
_refine.aniso_B[2][2]                            -0.45 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            2.58 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               24.172 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.942 
_refine.correlation_coeff_Fo_to_Fc_free          0.888 
_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                                 9IST 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.27 
_refine.ls_d_res_low                             47.00 
_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                     44238 
_refine.ls_number_reflns_R_free                  2326 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.46 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19227 
_refine.ls_R_factor_R_free                       0.25946 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18883 
_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                       0.346 
_refine.pdbx_overall_ESU_R_Free                  0.255 
_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                             9.496 
_refine.overall_SU_ML                            0.218 
_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                       2.27 
_refine_hist.d_res_low                        47.00 
_refine_hist.number_atoms_solvent             358 
_refine_hist.number_atoms_total               7882 
_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        7352 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         172 
_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' ? 0.009  0.013  7703  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  7330  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.698  1.667  10430 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.275  1.593  16936 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.993  5.000  908   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 34.825 23.463 410   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.765 15.000 1356  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 21.130 15.000 38    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.076  0.200  952   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  8626  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  1722  ? 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' ? 1.816  2.416  3638  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.814  2.415  3637  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.811  3.617  4544  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.811  3.619  4545  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.257  2.651  4065  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.256  2.651  4066  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.620  3.875  5888  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.826  27.950 8671  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.804  27.929 8638  ? 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                       2.270 
_refine_ls_shell.d_res_low                        2.329 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             196 
_refine_ls_shell.number_reflns_R_work             3263 
_refine_ls_shell.percent_reflns_obs               98.10 
_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                  0.288 
_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                  0.360 
# 
_struct.entry_id                     9IST 
_struct.title                        
'Crystal Structure of Cytochrome P450BM3 VI-18A12 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        9IST 
_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 5 ? 
N N N 5 ? 
O N N 5 ? 
P N N 6 ? 
Q 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 9IST A 1 ? 455 ? P14779 2 ? 456 ? 1 455 
2 1 9IST 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 9IST VAL A 25  ? UNP P14779 PRO 26  'engineered mutation' 25  1  
1 9IST TRP A 47  ? UNP P14779 ARG 48  'engineered mutation' 47  2  
1 9IST LEU A 49  ? UNP P14779 THR 50  'engineered mutation' 49  3  
1 9IST VAL A 74  ? UNP P14779 ALA 75  'engineered mutation' 74  4  
1 9IST PRO A 188 ? UNP P14779 LEU 189 'engineered mutation' 188 5  
2 9IST VAL B 25  ? UNP P14779 PRO 26  'engineered mutation' 25  6  
2 9IST TRP B 47  ? UNP P14779 ARG 48  'engineered mutation' 47  7  
2 9IST LEU B 49  ? UNP P14779 THR 50  'engineered mutation' 49  8  
2 9IST VAL B 74  ? UNP P14779 ALA 75  'engineered mutation' 74  9  
2 9IST PRO B 188 ? UNP P14779 LEU 189 'engineered mutation' 188 10 
# 
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)'  19020 ? 
2 'ABSA (A^2)' 1220  ? 
2 MORE         -21   ? 
2 'SSA (A^2)'  19040 ? 
# 
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,P       
2 1 B,H,I,J,K,L,M,N,O,Q 
# 
_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 ALA A 111 ? ARG A 132 ? ALA A 111 ARG A 132 1 ? 22 
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 ? ASN A 239 ? ASP A 232 ASN A 239 1 ? 8  
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 ? LYS A 282 ? THR A 268 LYS A 282 1 ? 15 
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 ? PHE B 107 ? PRO B 105 PHE B 107 5 ? 3  
HELX_P HELX_P34 AD7 SER B 108 ? ARG B 132 ? SER B 108 ARG B 132 1 ? 25 
HELX_P HELX_P35 AD8 VAL B 141 ? ASN B 159 ? VAL B 141 ASN B 159 1 ? 19 
HELX_P HELX_P36 AD9 HIS B 171 ? LYS B 187 ? HIS B 171 LYS B 187 1 ? 17 
HELX_P HELX_P37 AE1 PRO B 188 ? ARG B 190 ? PRO B 188 ARG B 190 5 ? 3  
HELX_P HELX_P38 AE2 ASP B 195 ? ALA B 197 ? ASP B 195 ALA B 197 5 ? 3  
HELX_P HELX_P39 AE3 TYR B 198 ? GLY B 227 ? TYR B 198 GLY B 227 1 ? 30 
HELX_P HELX_P40 AE4 ASP B 232 ? GLY B 240 ? ASP B 232 GLY B 240 1 ? 9  
HELX_P HELX_P41 AE5 ASP B 250 ? THR B 268 ? ASP B 250 THR B 268 1 ? 19 
HELX_P HELX_P42 AE6 THR B 268 ? ASN B 283 ? THR B 268 ASN B 283 1 ? 16 
HELX_P HELX_P43 AE7 ASN B 283 ? LEU B 298 ? ASN B 283 LEU B 298 1 ? 16 
HELX_P HELX_P44 AE8 SER B 304 ? LYS B 309 ? SER B 304 LYS B 309 1 ? 6  
HELX_P HELX_P45 AE9 LEU B 311 ? TRP B 325 ? LEU B 311 TRP B 325 1 ? 15 
HELX_P HELX_P46 AF1 GLY B 342 ? GLU B 344 ? GLY B 342 GLU B 344 5 ? 3  
HELX_P HELX_P47 AF2 ILE B 357 ? HIS B 361 ? ILE B 357 HIS B 361 1 ? 5  
HELX_P HELX_P48 AF3 ASP B 363 ? GLY B 368 ? ASP B 363 GLY B 368 1 ? 6  
HELX_P HELX_P49 AF4 ARG B 375 ? GLU B 380 ? ARG B 375 GLU B 380 5 ? 6  
HELX_P HELX_P50 AF5 ASN B 381 ? ILE B 385 ? ASN B 381 ILE B 385 5 ? 5  
HELX_P HELX_P51 AF6 ASN B 395 ? ALA B 399 ? ASN B 395 ALA B 399 5 ? 5  
HELX_P HELX_P52 AF7 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 ? ? ? ? ? ? ? 2.315 ? ? 
metalc2 metalc ? ? C HEM .   FE ? ? ? 1_555 E DMS . S  ? ? A HEM 501 A DMS 503 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc3 metalc ? ? C HEM .   FE ? ? ? 1_555 E DMS . O  ? ? A HEM 501 A DMS 503 1_555 ? ? ? ? ? ? ? 2.681 ? ? 
metalc4 metalc ? ? B CYS 400 SG ? ? ? 1_555 H HEM . FE ? ? B CYS 400 B HEM 501 1_555 ? ? ? ? ? ? ? 2.414 ? ? 
metalc5 metalc ? ? H HEM .   FE ? ? ? 1_555 J DMS . S  ? ? B HEM 501 B DMS 503 1_555 ? ? ? ? ? ? ? 2.473 ? ? 
metalc6 metalc ? ? H HEM .   FE ? ? ? 1_555 J DMS . O  ? ? B HEM 501 B DMS 503 1_555 ? ? ? ? ? ? ? 2.687 ? ? 
# 
_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 96.1  ? 
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 85.8  ? 
3  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 88.7  ? 
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 80.9  ? 
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 88.5  ? 
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 92.6  ? 
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 93.3  ? 
9  NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 177.5 ? 
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 89.4  ? 
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_555 177.2 ? 
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 84.0  ? 
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 97.0  ? 
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 99.1  ? 
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 84.6  ? 
16 SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E DMS . ? A DMS 503 ? 1_555 148.7 ? 
17 NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E DMS . ? A DMS 503 ? 1_555 108.3 ? 
18 NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E DMS . ? A DMS 503 ? 1_555 75.7  ? 
19 NC ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E DMS . ? A DMS 503 ? 1_555 73.7  ? 
20 ND ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E DMS . ? A DMS 503 ? 1_555 104.9 ? 
21 S  ? E DMS .   ? A DMS 503 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E DMS . ? A DMS 503 ? 1_555 33.0  ? 
22 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 95.0  ? 
23 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 87.3  ? 
24 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NB ? H HEM . ? B HEM 501 ? 1_555 89.6  ? 
25 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 83.0  ? 
26 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 176.2 ? 
27 NB ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 87.1  ? 
28 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 93.9  ? 
29 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 90.2  ? 
30 NB ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 178.8 ? 
31 NC ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 93.2  ? 
32 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 S  ? J DMS . ? B DMS 503 ? 1_555 175.2 ? 
33 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 S  ? J DMS . ? B DMS 503 ? 1_555 81.1  ? 
34 NB ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 S  ? J DMS . ? B DMS 503 ? 1_555 95.5  ? 
35 NC ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 S  ? J DMS . ? B DMS 503 ? 1_555 101.1 ? 
36 ND ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 S  ? J DMS . ? B DMS 503 ? 1_555 83.3  ? 
37 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 O  ? J DMS . ? B DMS 503 ? 1_555 152.2 ? 
38 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 O  ? J DMS . ? B DMS 503 ? 1_555 105.4 ? 
39 NB ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 O  ? J DMS . ? B DMS 503 ? 1_555 74.5  ? 
40 NC ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 O  ? J DMS . ? B DMS 503 ? 1_555 75.4  ? 
41 ND ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 O  ? J DMS . ? B DMS 503 ? 1_555 104.5 ? 
42 S  ? J DMS .   ? B DMS 503 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 O  ? J DMS . ? B DMS 503 ? 1_555 32.6  ? 
# 
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  ? GLU B 43  ? ILE B 39  GLU B 43  
AA5 2 VAL B 48  ? LEU B 52  ? VAL B 48  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 LEU A 353 ? O LEU A 353 N LEU A 333 ? N LEU A 333 
AA1 4 5 O TYR A 334 ? O TYR A 334 N ASP A 68  ? N ASP A 68  
AA2 1 2 N ILE A 139 ? N ILE A 139 O VAL A 446 ? O VAL A 446 
AA2 2 3 O LYS A 449 ? O LYS A 449 N ASP A 422 ? N ASP A 422 
AA3 1 2 N THR A 339 ? N THR A 339 O LEU A 347 ? O LEU A 347 
AA4 1 2 N LYS A 434 ? N LYS A 434 O LYS A 440 ? O LYS A 440 
AA5 1 2 N PHE B 40  ? N PHE B 40  O TYR B 51  ? O TYR B 51  
AA5 2 3 N ARG B 50  ? N ARG B 50  O MET B 354 ? O MET B 354 
AA5 3 4 O LEU B 353 ? O LEU B 353 N LEU B 333 ? N LEU B 333 
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 LEU B 341 ? N LEU B 341 O TYR B 345 ? O TYR B 345 
AA8 1 2 N LYS B 434 ? N LYS B 434 O LYS B 440 ? O LYS B 440 
# 
_pdbx_entry_details.entry_id                   9IST 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE2 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    137 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    601 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.17 
# 
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 PRO A 8   ? ? -68.85  -179.88 
2  1 LYS A 15  ? ? 52.48   -119.73 
3  1 SER A 72  ? ? -56.02  170.26  
4  1 ASP A 84  ? ? -99.36  38.80   
5  1 ASP A 136 ? ? -95.27  33.32   
6  1 PHE A 158 ? ? -144.48 30.97   
7  1 GLN A 229 ? ? -110.09 71.66   
8  1 THR A 268 ? ? -98.76  -68.56  
9  1 LYS A 349 ? ? -36.20  126.73  
10 1 ASP A 370 ? ? -85.32  41.69   
11 1 THR A 436 ? ? -108.52 -123.19 
12 1 LYS B 15  ? ? 56.05   -127.44 
13 1 ASP B 84  ? ? -97.00  41.71   
14 1 ASP B 136 ? ? -87.27  30.53   
15 1 PHE B 158 ? ? -157.17 33.37   
16 1 ASP B 168 ? ? -108.11 -63.26  
17 1 GLN B 169 ? ? -33.55  119.61  
18 1 GLN B 229 ? ? -111.96 63.16   
19 1 THR B 268 ? ? -95.50  -65.88  
20 1 GLU B 344 ? ? -139.36 -38.10  
21 1 THR B 436 ? ? -113.39 -133.89 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ARG 
_pdbx_validate_main_chain_plane.auth_asym_id             B 
_pdbx_validate_main_chain_plane.auth_seq_id              378 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   11.56 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 780 ? 5.82 . 
2 1 O ? A HOH 781 ? 6.62 . 
3 1 O ? A HOH 782 ? 8.13 . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
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                    9IST 
_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]   0.017099 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002680 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006721 
_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]   0.016492 
_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   . THR A 1 1   ? -12.694 61.660  20.246  1.00 55.37 ? 1   THR A N   1 
ATOM   2    C  CA  . THR A 1 1   ? -12.851 61.477  21.704  1.00 54.61 ? 1   THR A CA  1 
ATOM   3    C  C   . THR A 1 1   ? -12.320 60.097  22.086  1.00 53.05 ? 1   THR A C   1 
ATOM   4    O  O   . THR A 1 1   ? -12.794 59.086  21.521  1.00 54.02 ? 1   THR A O   1 
ATOM   5    C  CB  . THR A 1 1   ? -14.310 61.651  22.157  1.00 60.35 ? 1   THR A CB  1 
ATOM   6    O  OG1 . THR A 1 1   ? -14.541 63.036  22.426  1.00 66.37 ? 1   THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 1   ? -14.667 60.864  23.401  1.00 60.32 ? 1   THR A CG2 1 
ATOM   8    N  N   . ILE A 1 2   ? -11.370 60.080  23.014  1.00 49.16 ? 2   ILE A N   1 
ATOM   9    C  CA  . ILE A 1 2   ? -10.930 58.869  23.763  1.00 44.18 ? 2   ILE A CA  1 
ATOM   10   C  C   . ILE A 1 2   ? -12.048 58.492  24.744  1.00 45.84 ? 2   ILE A C   1 
ATOM   11   O  O   . ILE A 1 2   ? -12.508 59.377  25.484  1.00 41.54 ? 2   ILE A O   1 
ATOM   12   C  CB  . ILE A 1 2   ? -9.587  59.181  24.450  1.00 42.34 ? 2   ILE A CB  1 
ATOM   13   C  CG1 . ILE A 1 2   ? -8.504  59.457  23.406  1.00 42.32 ? 2   ILE A CG1 1 
ATOM   14   C  CG2 . ILE A 1 2   ? -9.178  58.095  25.429  1.00 42.44 ? 2   ILE A CG2 1 
ATOM   15   C  CD1 . ILE A 1 2   ? -8.423  58.428  22.290  1.00 42.99 ? 2   ILE A CD1 1 
ATOM   16   N  N   . LYS A 1 3   ? -12.512 57.240  24.720  1.00 44.08 ? 3   LYS A N   1 
ATOM   17   C  CA  . LYS A 1 3   ? -13.584 56.792  25.642  1.00 44.84 ? 3   LYS A CA  1 
ATOM   18   C  C   . LYS A 1 3   ? -13.080 55.603  26.449  1.00 40.06 ? 3   LYS A C   1 
ATOM   19   O  O   . LYS A 1 3   ? -12.190 54.894  25.969  1.00 38.45 ? 3   LYS A O   1 
ATOM   20   C  CB  . LYS A 1 3   ? -14.899 56.502  24.906  1.00 47.17 ? 3   LYS A CB  1 
ATOM   21   C  CG  . LYS A 1 3   ? -14.770 55.882  23.527  1.00 52.97 ? 3   LYS A CG  1 
ATOM   22   C  CD  . LYS A 1 3   ? -16.101 55.431  22.943  1.00 56.57 ? 3   LYS A CD  1 
ATOM   23   C  CE  . LYS A 1 3   ? -17.135 56.534  22.870  1.00 61.07 ? 3   LYS A CE  1 
ATOM   24   N  NZ  . LYS A 1 3   ? -16.560 57.800  22.353  1.00 60.19 ? 3   LYS A NZ  1 
ATOM   25   N  N   . GLU A 1 4   ? -13.582 55.489  27.677  1.00 41.27 ? 4   GLU A N   1 
ATOM   26   C  CA  . GLU A 1 4   ? -13.441 54.296  28.544  1.00 41.49 ? 4   GLU A CA  1 
ATOM   27   C  C   . GLU A 1 4   ? -14.241 53.177  27.879  1.00 41.17 ? 4   GLU A C   1 
ATOM   28   O  O   . GLU A 1 4   ? -15.323 53.487  27.353  1.00 38.55 ? 4   GLU A O   1 
ATOM   29   C  CB  . GLU A 1 4   ? -13.989 54.617  29.937  1.00 44.61 ? 4   GLU A CB  1 
ATOM   30   C  CG  . GLU A 1 4   ? -14.178 53.393  30.819  1.00 49.02 ? 4   GLU A CG  1 
ATOM   31   C  CD  . GLU A 1 4   ? -14.800 53.689  32.174  1.00 51.43 ? 4   GLU A CD  1 
ATOM   32   O  OE1 . GLU A 1 4   ? -14.794 54.879  32.566  1.00 42.57 ? 4   GLU A OE1 1 
ATOM   33   O  OE2 . GLU A 1 4   ? -15.300 52.721  32.829  1.00 55.96 ? 4   GLU A OE2 1 
ATOM   34   N  N   . MET A 1 5   ? -13.763 51.929  27.876  1.00 38.00 ? 5   MET A N   1 
ATOM   35   C  CA  . MET A 1 5   ? -14.593 50.838  27.302  1.00 34.08 ? 5   MET A CA  1 
ATOM   36   C  C   . MET A 1 5   ? -15.363 50.172  28.434  1.00 31.79 ? 5   MET A C   1 
ATOM   37   O  O   . MET A 1 5   ? -14.918 50.174  29.575  1.00 32.98 ? 5   MET A O   1 
ATOM   38   C  CB  . MET A 1 5   ? -13.806 49.831  26.451  1.00 32.79 ? 5   MET A CB  1 
ATOM   39   C  CG  . MET A 1 5   ? -12.812 48.980  27.160  1.00 33.23 ? 5   MET A CG  1 
ATOM   40   S  SD  . MET A 1 5   ? -11.938 47.889  25.971  1.00 31.94 ? 5   MET A SD  1 
ATOM   41   C  CE  . MET A 1 5   ? -10.889 49.050  25.095  1.00 31.44 ? 5   MET A CE  1 
ATOM   42   N  N   . PRO A 1 6   ? -16.599 49.699  28.160  1.00 29.37 ? 6   PRO A N   1 
ATOM   43   C  CA  . PRO A 1 6   ? -17.410 49.036  29.172  1.00 27.05 ? 6   PRO A CA  1 
ATOM   44   C  C   . PRO A 1 6   ? -16.828 47.689  29.594  1.00 25.74 ? 6   PRO A C   1 
ATOM   45   O  O   . PRO A 1 6   ? -16.052 47.130  28.869  1.00 26.13 ? 6   PRO A O   1 
ATOM   46   C  CB  . PRO A 1 6   ? -18.766 48.801  28.503  1.00 27.82 ? 6   PRO A CB  1 
ATOM   47   C  CG  . PRO A 1 6   ? -18.507 48.930  27.022  1.00 28.33 ? 6   PRO A CG  1 
ATOM   48   C  CD  . PRO A 1 6   ? -17.307 49.840  26.877  1.00 28.04 ? 6   PRO A CD  1 
ATOM   49   N  N   . GLN A 1 7   ? -17.279 47.196  30.739  1.00 23.89 ? 7   GLN A N   1 
ATOM   50   C  CA  . GLN A 1 7   ? -16.809 45.929  31.345  1.00 24.18 ? 7   GLN A CA  1 
ATOM   51   C  C   . GLN A 1 7   ? -18.008 45.238  31.978  1.00 23.82 ? 7   GLN A C   1 
ATOM   52   O  O   . GLN A 1 7   ? -18.815 45.881  32.645  1.00 22.06 ? 7   GLN A O   1 
ATOM   53   C  CB  . GLN A 1 7   ? -15.736 46.235  32.387  1.00 23.85 ? 7   GLN A CB  1 
ATOM   54   C  CG  . GLN A 1 7   ? -15.351 45.040  33.241  1.00 24.70 ? 7   GLN A CG  1 
ATOM   55   C  CD  . GLN A 1 7   ? -14.213 45.361  34.174  1.00 23.55 ? 7   GLN A CD  1 
ATOM   56   O  OE1 . GLN A 1 7   ? -13.876 46.521  34.408  1.00 23.72 ? 7   GLN A OE1 1 
ATOM   57   N  NE2 . GLN A 1 7   ? -13.612 44.316  34.713  1.00 24.24 ? 7   GLN A NE2 1 
ATOM   58   N  N   . PRO A 1 8   ? -18.145 43.913  31.789  1.00 24.02 ? 8   PRO A N   1 
ATOM   59   C  CA  . PRO A 1 8   ? -19.207 43.148  32.431  1.00 24.25 ? 8   PRO A CA  1 
ATOM   60   C  C   . PRO A 1 8   ? -19.036 43.023  33.953  1.00 24.01 ? 8   PRO A C   1 
ATOM   61   O  O   . PRO A 1 8   ? -18.091 43.576  34.482  1.00 23.62 ? 8   PRO A O   1 
ATOM   62   C  CB  . PRO A 1 8   ? -19.131 41.779  31.739  1.00 24.54 ? 8   PRO A CB  1 
ATOM   63   C  CG  . PRO A 1 8   ? -17.712 41.676  31.244  1.00 24.23 ? 8   PRO A CG  1 
ATOM   64   C  CD  . PRO A 1 8   ? -17.317 43.094  30.897  1.00 24.65 ? 8   PRO A CD  1 
ATOM   65   N  N   . LYS A 1 9   ? -19.979 42.330  34.594  1.00 22.26 ? 9   LYS A N   1 
ATOM   66   C  CA  . LYS A 1 9   ? -20.161 42.308  36.067  1.00 22.32 ? 9   LYS A CA  1 
ATOM   67   C  C   . LYS A 1 9   ? -18.924 41.669  36.726  1.00 24.00 ? 9   LYS A C   1 
ATOM   68   O  O   . LYS A 1 9   ? -18.439 40.595  36.257  1.00 22.57 ? 9   LYS A O   1 
ATOM   69   C  CB  . LYS A 1 9   ? -21.484 41.621  36.423  1.00 21.05 ? 9   LYS A CB  1 
ATOM   70   C  CG  . LYS A 1 9   ? -21.603 40.143  36.071  1.00 21.40 ? 9   LYS A CG  1 
ATOM   71   C  CD  . LYS A 1 9   ? -23.009 39.576  36.266  1.00 22.10 ? 9   LYS A CD  1 
ATOM   72   C  CE  . LYS A 1 9   ? -23.060 38.064  36.409  1.00 23.83 ? 9   LYS A CE  1 
ATOM   73   N  NZ  . LYS A 1 9   ? -24.013 37.583  37.464  1.00 24.80 ? 9   LYS A NZ  1 
ATOM   74   N  N   . THR A 1 10  ? -18.399 42.317  37.766  1.00 23.92 ? 10  THR A N   1 
ATOM   75   C  CA  . THR A 1 10  ? -17.182 41.833  38.459  1.00 24.53 ? 10  THR A CA  1 
ATOM   76   C  C   . THR A 1 10  ? -17.596 41.033  39.693  1.00 22.93 ? 10  THR A C   1 
ATOM   77   O  O   . THR A 1 10  ? -18.772 41.108  40.110  1.00 19.76 ? 10  THR A O   1 
ATOM   78   C  CB  . THR A 1 10  ? -16.193 42.952  38.795  1.00 23.84 ? 10  THR A CB  1 
ATOM   79   O  OG1 . THR A 1 10  ? -16.847 43.838  39.692  1.00 24.32 ? 10  THR A OG1 1 
ATOM   80   C  CG2 . THR A 1 10  ? -15.694 43.675  37.561  1.00 24.18 ? 10  THR A CG2 1 
ATOM   81   N  N   . PHE A 1 11  ? -16.636 40.255  40.185  1.00 23.39 ? 11  PHE A N   1 
ATOM   82   C  CA  . PHE A 1 11  ? -16.731 39.394  41.382  1.00 24.35 ? 11  PHE A CA  1 
ATOM   83   C  C   . PHE A 1 11  ? -15.562 39.703  42.314  1.00 24.38 ? 11  PHE A C   1 
ATOM   84   O  O   . PHE A 1 11  ? -14.692 38.848  42.430  1.00 23.90 ? 11  PHE A O   1 
ATOM   85   C  CB  . PHE A 1 11  ? -16.692 37.928  40.965  1.00 23.93 ? 11  PHE A CB  1 
ATOM   86   C  CG  . PHE A 1 11  ? -17.860 37.484  40.125  1.00 23.38 ? 11  PHE A CG  1 
ATOM   87   C  CD1 . PHE A 1 11  ? -18.000 37.921  38.814  1.00 22.79 ? 11  PHE A CD1 1 
ATOM   88   C  CD2 . PHE A 1 11  ? -18.793 36.592  40.638  1.00 22.74 ? 11  PHE A CD2 1 
ATOM   89   C  CE1 . PHE A 1 11  ? -19.068 37.487  38.046  1.00 21.60 ? 11  PHE A CE1 1 
ATOM   90   C  CE2 . PHE A 1 11  ? -19.861 36.164  39.867  1.00 20.94 ? 11  PHE A CE2 1 
ATOM   91   C  CZ  . PHE A 1 11  ? -19.983 36.603  38.573  1.00 22.05 ? 11  PHE A CZ  1 
ATOM   92   N  N   . GLY A 1 12  ? -15.555 40.875  42.951  1.00 25.42 ? 12  GLY A N   1 
ATOM   93   C  CA  . GLY A 1 12  ? -14.514 41.222  43.939  1.00 26.64 ? 12  GLY A CA  1 
ATOM   94   C  C   . GLY A 1 12  ? -13.122 41.079  43.330  1.00 28.88 ? 12  GLY A C   1 
ATOM   95   O  O   . GLY A 1 12  ? -12.921 41.558  42.194  1.00 26.38 ? 12  GLY A O   1 
ATOM   96   N  N   . GLU A 1 13  ? -12.201 40.395  44.010  1.00 32.17 ? 13  GLU A N   1 
ATOM   97   C  CA  . GLU A 1 13  ? -10.779 40.324  43.572  1.00 36.80 ? 13  GLU A CA  1 
ATOM   98   C  C   . GLU A 1 13  ? -10.606 39.327  42.405  1.00 34.11 ? 13  GLU A C   1 
ATOM   99   O  O   . GLU A 1 13  ? -9.496  39.308  41.793  1.00 31.06 ? 13  GLU A O   1 
ATOM   100  C  CB  . GLU A 1 13  ? -9.886  40.047  44.787  1.00 44.85 ? 13  GLU A CB  1 
ATOM   101  C  CG  . GLU A 1 13  ? -9.553  41.317  45.588  1.00 50.63 ? 13  GLU A CG  1 
ATOM   102  C  CD  . GLU A 1 13  ? -8.873  42.470  44.840  1.00 52.70 ? 13  GLU A CD  1 
ATOM   103  O  OE1 . GLU A 1 13  ? -8.136  42.218  43.851  1.00 51.31 ? 13  GLU A OE1 1 
ATOM   104  O  OE2 . GLU A 1 13  ? -9.073  43.636  45.250  1.00 58.00 ? 13  GLU A OE2 1 
ATOM   105  N  N   . LEU A 1 14  ? -11.652 38.567  42.043  1.00 29.12 ? 14  LEU A N   1 
ATOM   106  C  CA  . LEU A 1 14  ? -11.606 37.650  40.871  1.00 27.09 ? 14  LEU A CA  1 
ATOM   107  C  C   . LEU A 1 14  ? -12.017 38.398  39.592  1.00 26.51 ? 14  LEU A C   1 
ATOM   108  O  O   . LEU A 1 14  ? -11.929 37.793  38.502  1.00 24.47 ? 14  LEU A O   1 
ATOM   109  C  CB  . LEU A 1 14  ? -12.514 36.456  41.143  1.00 25.67 ? 14  LEU A CB  1 
ATOM   110  C  CG  . LEU A 1 14  ? -12.154 35.634  42.374  1.00 26.61 ? 14  LEU A CG  1 
ATOM   111  C  CD1 . LEU A 1 14  ? -13.161 34.511  42.587  1.00 26.72 ? 14  LEU A CD1 1 
ATOM   112  C  CD2 . LEU A 1 14  ? -10.751 35.076  42.237  1.00 27.01 ? 14  LEU A CD2 1 
ATOM   113  N  N   . LYS A 1 15  ? -12.431 39.665  39.720  1.00 26.41 ? 15  LYS A N   1 
ATOM   114  C  CA  . LYS A 1 15  ? -12.842 40.552  38.594  1.00 28.20 ? 15  LYS A CA  1 
ATOM   115  C  C   . LYS A 1 15  ? -13.903 39.814  37.763  1.00 25.48 ? 15  LYS A C   1 
ATOM   116  O  O   . LYS A 1 15  ? -14.916 39.402  38.353  1.00 24.32 ? 15  LYS A O   1 
ATOM   117  C  CB  . LYS A 1 15  ? -11.589 41.004  37.832  1.00 30.35 ? 15  LYS A CB  1 
ATOM   118  C  CG  . LYS A 1 15  ? -10.659 41.885  38.655  1.00 33.48 ? 15  LYS A CG  1 
ATOM   119  C  CD  . LYS A 1 15  ? -9.207  41.671  38.384  1.00 38.17 ? 15  LYS A CD  1 
ATOM   120  C  CE  . LYS A 1 15  ? -8.416  42.965  38.303  1.00 43.90 ? 15  LYS A CE  1 
ATOM   121  N  NZ  . LYS A 1 15  ? -7.113  42.757  37.618  1.00 45.77 ? 15  LYS A NZ  1 
ATOM   122  N  N   . ASN A 1 16  ? -13.644 39.567  36.482  1.00 22.58 ? 16  ASN A N   1 
ATOM   123  C  CA  . ASN A 1 16  ? -14.625 38.950  35.553  1.00 24.02 ? 16  ASN A CA  1 
ATOM   124  C  C   . ASN A 1 16  ? -14.548 37.427  35.574  1.00 24.08 ? 16  ASN A C   1 
ATOM   125  O  O   . ASN A 1 16  ? -15.450 36.802  35.006  1.00 30.12 ? 16  ASN A O   1 
ATOM   126  C  CB  . ASN A 1 16  ? -14.428 39.458  34.126  1.00 23.84 ? 16  ASN A CB  1 
ATOM   127  C  CG  . ASN A 1 16  ? -14.793 40.916  34.044  1.00 22.75 ? 16  ASN A CG  1 
ATOM   128  O  OD1 . ASN A 1 16  ? -13.986 41.758  33.651  1.00 25.33 ? 16  ASN A OD1 1 
ATOM   129  N  ND2 . ASN A 1 16  ? -15.987 41.215  34.511  1.00 21.94 ? 16  ASN A ND2 1 
ATOM   130  N  N   . LEU A 1 17  ? -13.512 36.857  36.184  1.00 23.95 ? 17  LEU A N   1 
ATOM   131  C  CA  . LEU A 1 17  ? -13.098 35.443  35.981  1.00 23.64 ? 17  LEU A CA  1 
ATOM   132  C  C   . LEU A 1 17  ? -14.278 34.485  36.125  1.00 24.33 ? 17  LEU A C   1 
ATOM   133  O  O   . LEU A 1 17  ? -14.424 33.565  35.319  1.00 25.51 ? 17  LEU A O   1 
ATOM   134  C  CB  . LEU A 1 17  ? -11.975 35.089  36.963  1.00 23.18 ? 17  LEU A CB  1 
ATOM   135  C  CG  . LEU A 1 17  ? -11.365 33.705  36.756  1.00 23.21 ? 17  LEU A CG  1 
ATOM   136  C  CD1 . LEU A 1 17  ? -10.651 33.629  35.416  1.00 23.39 ? 17  LEU A CD1 1 
ATOM   137  C  CD2 . LEU A 1 17  ? -10.425 33.354  37.888  1.00 23.02 ? 17  LEU A CD2 1 
ATOM   138  N  N   . PRO A 1 18  ? -15.130 34.602  37.168  1.00 24.52 ? 18  PRO A N   1 
ATOM   139  C  CA  . PRO A 1 18  ? -16.155 33.585  37.395  1.00 24.08 ? 18  PRO A CA  1 
ATOM   140  C  C   . PRO A 1 18  ? -17.171 33.503  36.248  1.00 23.65 ? 18  PRO A C   1 
ATOM   141  O  O   . PRO A 1 18  ? -17.873 32.526  36.178  1.00 20.96 ? 18  PRO A O   1 
ATOM   142  C  CB  . PRO A 1 18  ? -16.783 34.046  38.715  1.00 25.28 ? 18  PRO A CB  1 
ATOM   143  C  CG  . PRO A 1 18  ? -15.653 34.821  39.385  1.00 24.13 ? 18  PRO A CG  1 
ATOM   144  C  CD  . PRO A 1 18  ? -15.098 35.616  38.233  1.00 23.55 ? 18  PRO A CD  1 
ATOM   145  N  N   . LEU A 1 19  ? -17.203 34.515  35.377  1.00 24.50 ? 19  LEU A N   1 
ATOM   146  C  CA  . LEU A 1 19  ? -18.057 34.517  34.156  1.00 25.31 ? 19  LEU A CA  1 
ATOM   147  C  C   . LEU A 1 19  ? -17.624 33.409  33.184  1.00 25.12 ? 19  LEU A C   1 
ATOM   148  O  O   . LEU A 1 19  ? -18.445 33.047  32.345  1.00 26.97 ? 19  LEU A O   1 
ATOM   149  C  CB  . LEU A 1 19  ? -17.987 35.877  33.467  1.00 25.35 ? 19  LEU A CB  1 
ATOM   150  C  CG  . LEU A 1 19  ? -18.599 37.057  34.216  1.00 25.21 ? 19  LEU A CG  1 
ATOM   151  C  CD1 . LEU A 1 19  ? -18.437 38.325  33.385  1.00 26.56 ? 19  LEU A CD1 1 
ATOM   152  C  CD2 . LEU A 1 19  ? -20.068 36.826  34.538  1.00 24.58 ? 19  LEU A CD2 1 
ATOM   153  N  N   . LEU A 1 20  ? -16.419 32.861  33.339  1.00 27.22 ? 20  LEU A N   1 
ATOM   154  C  CA  . LEU A 1 20  ? -15.867 31.733  32.542  1.00 29.38 ? 20  LEU A CA  1 
ATOM   155  C  C   . LEU A 1 20  ? -16.262 30.382  33.145  1.00 29.31 ? 20  LEU A C   1 
ATOM   156  O  O   . LEU A 1 20  ? -15.936 29.332  32.526  1.00 24.74 ? 20  LEU A O   1 
ATOM   157  C  CB  . LEU A 1 20  ? -14.345 31.847  32.554  1.00 31.23 ? 20  LEU A CB  1 
ATOM   158  C  CG  . LEU A 1 20  ? -13.816 33.145  31.977  1.00 32.54 ? 20  LEU A CG  1 
ATOM   159  C  CD1 . LEU A 1 20  ? -12.307 33.239  32.171  1.00 34.13 ? 20  LEU A CD1 1 
ATOM   160  C  CD2 . LEU A 1 20  ? -14.205 33.233  30.501  1.00 34.37 ? 20  LEU A CD2 1 
ATOM   161  N  N   . ASN A 1 21  ? -16.874 30.400  34.329  1.00 30.16 ? 21  ASN A N   1 
ATOM   162  C  CA  . ASN A 1 21  ? -17.293 29.172  35.053  1.00 31.66 ? 21  ASN A CA  1 
ATOM   163  C  C   . ASN A 1 21  ? -18.627 28.660  34.470  1.00 29.66 ? 21  ASN A C   1 
ATOM   164  O  O   . ASN A 1 21  ? -19.642 28.597  35.202  1.00 26.54 ? 21  ASN A O   1 
ATOM   165  C  CB  . ASN A 1 21  ? -17.353 29.413  36.562  1.00 32.19 ? 21  ASN A CB  1 
ATOM   166  C  CG  . ASN A 1 21  ? -17.357 28.098  37.298  1.00 34.67 ? 21  ASN A CG  1 
ATOM   167  O  OD1 . ASN A 1 21  ? -17.041 27.069  36.711  1.00 37.02 ? 21  ASN A OD1 1 
ATOM   168  N  ND2 . ASN A 1 21  ? -17.731 28.112  38.563  1.00 37.94 ? 21  ASN A ND2 1 
ATOM   169  N  N   . THR A 1 22  ? -18.595 28.273  33.195  1.00 26.95 ? 22  THR A N   1 
ATOM   170  C  CA  . THR A 1 22  ? -19.728 27.761  32.389  1.00 27.47 ? 22  THR A CA  1 
ATOM   171  C  C   . THR A 1 22  ? -19.147 26.859  31.288  1.00 26.18 ? 22  THR A C   1 
ATOM   172  O  O   . THR A 1 22  ? -17.983 27.088  30.911  1.00 23.72 ? 22  THR A O   1 
ATOM   173  C  CB  . THR A 1 22  ? -20.558 28.941  31.855  1.00 28.44 ? 22  THR A CB  1 
ATOM   174  O  OG1 . THR A 1 22  ? -21.534 28.414  30.959  1.00 28.37 ? 22  THR A OG1 1 
ATOM   175  C  CG2 . THR A 1 22  ? -19.745 29.990  31.128  1.00 28.30 ? 22  THR A CG2 1 
ATOM   176  N  N   . ASP A 1 23  ? -19.911 25.909  30.744  1.00 27.20 ? 23  ASP A N   1 
ATOM   177  C  CA  . ASP A 1 23  ? -19.453 25.092  29.586  1.00 29.49 ? 23  ASP A CA  1 
ATOM   178  C  C   . ASP A 1 23  ? -19.949 25.737  28.278  1.00 27.28 ? 23  ASP A C   1 
ATOM   179  O  O   . ASP A 1 23  ? -19.822 25.084  27.210  1.00 25.57 ? 23  ASP A O   1 
ATOM   180  C  CB  . ASP A 1 23  ? -19.860 23.629  29.762  1.00 36.20 ? 23  ASP A CB  1 
ATOM   181  C  CG  . ASP A 1 23  ? -21.320 23.462  30.140  1.00 44.61 ? 23  ASP A CG  1 
ATOM   182  O  OD1 . ASP A 1 23  ? -22.042 24.475  30.117  1.00 49.93 ? 23  ASP A OD1 1 
ATOM   183  O  OD2 . ASP A 1 23  ? -21.724 22.328  30.482  1.00 53.80 ? 23  ASP A OD2 1 
ATOM   184  N  N   . LYS A 1 24  ? -20.461 26.981  28.341  1.00 25.77 ? 24  LYS A N   1 
ATOM   185  C  CA  . LYS A 1 24  ? -21.034 27.728  27.186  1.00 25.98 ? 24  LYS A CA  1 
ATOM   186  C  C   . LYS A 1 24  ? -20.528 29.166  27.229  1.00 24.13 ? 24  LYS A C   1 
ATOM   187  O  O   . LYS A 1 24  ? -21.345 30.091  27.247  1.00 23.71 ? 24  LYS A O   1 
ATOM   188  C  CB  . LYS A 1 24  ? -22.572 27.707  27.216  1.00 27.03 ? 24  LYS A CB  1 
ATOM   189  C  CG  . LYS A 1 24  ? -23.206 26.382  26.829  1.00 27.67 ? 24  LYS A CG  1 
ATOM   190  C  CD  . LYS A 1 24  ? -24.705 26.477  26.633  1.00 28.56 ? 24  LYS A CD  1 
ATOM   191  C  CE  . LYS A 1 24  ? -25.328 25.136  26.342  1.00 29.03 ? 24  LYS A CE  1 
ATOM   192  N  NZ  . LYS A 1 24  ? -26.633 25.001  27.023  1.00 32.62 ? 24  LYS A NZ  1 
ATOM   193  N  N   . VAL A 1 25  ? -19.215 29.337  27.191  1.00 28.23 ? 25  VAL A N   1 
ATOM   194  C  CA  . VAL A 1 25  ? -18.515 30.628  27.460  1.00 27.88 ? 25  VAL A CA  1 
ATOM   195  C  C   . VAL A 1 25  ? -18.649 31.572  26.252  1.00 27.26 ? 25  VAL A C   1 
ATOM   196  O  O   . VAL A 1 25  ? -18.827 32.778  26.490  1.00 28.53 ? 25  VAL A O   1 
ATOM   197  C  CB  . VAL A 1 25  ? -17.053 30.365  27.867  1.00 30.95 ? 25  VAL A CB  1 
ATOM   198  C  CG1 . VAL A 1 25  ? -16.090 30.438  26.700  1.00 33.30 ? 25  VAL A CG1 1 
ATOM   199  C  CG2 . VAL A 1 25  ? -16.617 31.309  28.968  1.00 33.83 ? 25  VAL A CG2 1 
ATOM   200  N  N   . VAL A 1 26  ? -18.599 31.072  25.009  1.00 25.73 ? 26  VAL A N   1 
ATOM   201  C  CA  . VAL A 1 26  ? -18.810 31.900  23.775  1.00 25.01 ? 26  VAL A CA  1 
ATOM   202  C  C   . VAL A 1 26  ? -20.216 32.491  23.810  1.00 24.28 ? 26  VAL A C   1 
ATOM   203  O  O   . VAL A 1 26  ? -20.413 33.669  23.481  1.00 22.19 ? 26  VAL A O   1 
ATOM   204  C  CB  . VAL A 1 26  ? -18.623 31.080  22.481  1.00 25.27 ? 26  VAL A CB  1 
ATOM   205  C  CG1 . VAL A 1 26  ? -19.045 31.870  21.255  1.00 24.47 ? 26  VAL A CG1 1 
ATOM   206  C  CG2 . VAL A 1 26  ? -17.199 30.571  22.319  1.00 26.19 ? 26  VAL A CG2 1 
ATOM   207  N  N   . GLN A 1 27  ? -21.185 31.643  24.111  1.00 26.66 ? 27  GLN A N   1 
ATOM   208  C  CA  . GLN A 1 27  ? -22.615 32.029  24.140  1.00 28.30 ? 27  GLN A CA  1 
ATOM   209  C  C   . GLN A 1 27  ? -22.798 33.139  25.183  1.00 26.71 ? 27  GLN A C   1 
ATOM   210  O  O   . GLN A 1 27  ? -23.401 34.140  24.839  1.00 27.97 ? 27  GLN A O   1 
ATOM   211  C  CB  . GLN A 1 27  ? -23.454 30.778  24.391  1.00 28.23 ? 27  GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 27  ? -23.429 29.830  23.199  1.00 28.76 ? 27  GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 27  ? -24.097 28.507  23.466  1.00 27.52 ? 27  GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 27  ? -23.437 27.492  23.702  1.00 26.58 ? 27  GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 27  ? -25.423 28.523  23.434  1.00 29.21 ? 27  GLN A NE2 1 
ATOM   216  N  N   . ALA A 1 28  ? -22.245 32.980  26.383  1.00 25.14 ? 28  ALA A N   1 
ATOM   217  C  CA  . ALA A 1 28  ? -22.252 34.004  27.459  1.00 25.90 ? 28  ALA A CA  1 
ATOM   218  C  C   . ALA A 1 28  ? -21.599 35.307  26.960  1.00 24.99 ? 28  ALA A C   1 
ATOM   219  O  O   . ALA A 1 28  ? -22.141 36.394  27.244  1.00 24.38 ? 28  ALA A O   1 
ATOM   220  C  CB  . ALA A 1 28  ? -21.556 33.452  28.674  1.00 25.33 ? 28  ALA A CB  1 
ATOM   221  N  N   . LEU A 1 29  ? -20.483 35.204  26.232  1.00 24.98 ? 29  LEU A N   1 
ATOM   222  C  CA  . LEU A 1 29  ? -19.693 36.370  25.730  1.00 24.52 ? 29  LEU A CA  1 
ATOM   223  C  C   . LEU A 1 29  ? -20.491 37.104  24.645  1.00 24.00 ? 29  LEU A C   1 
ATOM   224  O  O   . LEU A 1 29  ? -20.421 38.358  24.590  1.00 23.14 ? 29  LEU A O   1 
ATOM   225  C  CB  . LEU A 1 29  ? -18.367 35.880  25.148  1.00 23.45 ? 29  LEU A CB  1 
ATOM   226  C  CG  . LEU A 1 29  ? -17.294 35.539  26.165  1.00 23.82 ? 29  LEU A CG  1 
ATOM   227  C  CD1 . LEU A 1 29  ? -16.257 34.631  25.535  1.00 23.25 ? 29  LEU A CD1 1 
ATOM   228  C  CD2 . LEU A 1 29  ? -16.648 36.805  26.741  1.00 24.43 ? 29  LEU A CD2 1 
ATOM   229  N  N   . MET A 1 30  ? -21.204 36.341  23.808  1.00 24.79 ? 30  MET A N   1 
ATOM   230  C  CA  . MET A 1 30  ? -22.166 36.876  22.806  1.00 25.55 ? 30  MET A CA  1 
ATOM   231  C  C   . MET A 1 30  ? -23.270 37.653  23.552  1.00 25.36 ? 30  MET A C   1 
ATOM   232  O  O   . MET A 1 30  ? -23.632 38.752  23.077  1.00 27.30 ? 30  MET A O   1 
ATOM   233  C  CB  . MET A 1 30  ? -22.770 35.755  21.951  1.00 24.92 ? 30  MET A CB  1 
ATOM   234  C  CG  . MET A 1 30  ? -21.779 35.107  20.975  1.00 26.15 ? 30  MET A CG  1 
ATOM   235  S  SD  . MET A 1 30  ? -22.492 33.618  20.166  1.00 25.87 ? 30  MET A SD  1 
ATOM   236  C  CE  . MET A 1 30  ? -23.758 34.425  19.198  1.00 26.18 ? 30  MET A CE  1 
ATOM   237  N  N   . LYS A 1 31  ? -23.786 37.126  24.669  1.00 25.00 ? 31  LYS A N   1 
ATOM   238  C  CA  . LYS A 1 31  ? -24.864 37.785  25.464  1.00 28.36 ? 31  LYS A CA  1 
ATOM   239  C  C   . LYS A 1 31  ? -24.258 39.059  26.056  1.00 25.46 ? 31  LYS A C   1 
ATOM   240  O  O   . LYS A 1 31  ? -24.887 40.118  26.011  1.00 23.07 ? 31  LYS A O   1 
ATOM   241  C  CB  . LYS A 1 31  ? -25.456 36.826  26.508  1.00 33.53 ? 31  LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 31  ? -26.474 37.414  27.484  1.00 39.58 ? 31  LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 31  ? -27.672 38.102  26.831  1.00 46.39 ? 31  LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 31  ? -28.876 38.244  27.749  1.00 51.11 ? 31  LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 31  ? -29.613 39.515  27.516  1.00 49.33 ? 31  LYS A NZ  1 
ATOM   246  N  N   . ILE A 1 32  ? -23.020 38.983  26.520  1.00 24.33 ? 32  ILE A N   1 
ATOM   247  C  CA  . ILE A 1 32  ? -22.350 40.182  27.080  1.00 22.68 ? 32  ILE A CA  1 
ATOM   248  C  C   . ILE A 1 32  ? -22.190 41.184  25.945  1.00 22.93 ? 32  ILE A C   1 
ATOM   249  O  O   . ILE A 1 32  ? -22.560 42.330  26.185  1.00 24.71 ? 32  ILE A O   1 
ATOM   250  C  CB  . ILE A 1 32  ? -21.041 39.803  27.771  1.00 22.16 ? 32  ILE A CB  1 
ATOM   251  C  CG1 . ILE A 1 32  ? -21.333 39.090  29.090  1.00 20.53 ? 32  ILE A CG1 1 
ATOM   252  C  CG2 . ILE A 1 32  ? -20.146 41.015  27.967  1.00 24.20 ? 32  ILE A CG2 1 
ATOM   253  C  CD1 . ILE A 1 32  ? -20.206 38.234  29.532  1.00 19.81 ? 32  ILE A CD1 1 
ATOM   254  N  N   . ALA A 1 33  ? -21.754 40.756  24.747  1.00 22.25 ? 33  ALA A N   1 
ATOM   255  C  CA  . ALA A 1 33  ? -21.584 41.651  23.573  1.00 21.17 ? 33  ALA A CA  1 
ATOM   256  C  C   . ALA A 1 33  ? -22.920 42.342  23.241  1.00 21.25 ? 33  ALA A C   1 
ATOM   257  O  O   . ALA A 1 33  ? -22.909 43.565  22.983  1.00 20.38 ? 33  ALA A O   1 
ATOM   258  C  CB  . ALA A 1 33  ? -21.003 40.911  22.392  1.00 19.89 ? 33  ALA A CB  1 
ATOM   259  N  N   . ASP A 1 34  ? -24.041 41.616  23.277  1.00 23.84 ? 34  ASP A N   1 
ATOM   260  C  CA  . ASP A 1 34  ? -25.385 42.188  22.997  1.00 26.36 ? 34  ASP A CA  1 
ATOM   261  C  C   . ASP A 1 34  ? -25.613 43.342  23.972  1.00 25.30 ? 34  ASP A C   1 
ATOM   262  O  O   . ASP A 1 34  ? -26.104 44.384  23.538  1.00 25.37 ? 34  ASP A O   1 
ATOM   263  C  CB  . ASP A 1 34  ? -26.533 41.178  23.123  1.00 29.68 ? 34  ASP A CB  1 
ATOM   264  C  CG  . ASP A 1 34  ? -26.681 40.136  22.016  1.00 34.90 ? 34  ASP A CG  1 
ATOM   265  O  OD1 . ASP A 1 34  ? -26.217 40.382  20.852  1.00 34.53 ? 34  ASP A OD1 1 
ATOM   266  O  OD2 . ASP A 1 34  ? -27.268 39.062  22.335  1.00 37.80 ? 34  ASP A OD2 1 
ATOM   267  N  N   . GLU A 1 35  ? -25.225 43.184  25.234  1.00 26.25 ? 35  GLU A N   1 
ATOM   268  C  CA  . GLU A 1 35  ? -25.517 44.190  26.288  1.00 27.29 ? 35  GLU A CA  1 
ATOM   269  C  C   . GLU A 1 35  ? -24.584 45.394  26.151  1.00 27.08 ? 35  GLU A C   1 
ATOM   270  O  O   . GLU A 1 35  ? -25.097 46.521  26.200  1.00 31.57 ? 35  GLU A O   1 
ATOM   271  C  CB  . GLU A 1 35  ? -25.424 43.561  27.673  1.00 28.81 ? 35  GLU A CB  1 
ATOM   272  C  CG  . GLU A 1 35  ? -26.609 42.674  27.967  1.00 31.14 ? 35  GLU A CG  1 
ATOM   273  C  CD  . GLU A 1 35  ? -26.643 42.123  29.382  1.00 36.29 ? 35  GLU A CD  1 
ATOM   274  O  OE1 . GLU A 1 35  ? -27.360 41.121  29.605  1.00 38.71 ? 35  GLU A OE1 1 
ATOM   275  O  OE2 . GLU A 1 35  ? -25.958 42.695  30.262  1.00 40.81 ? 35  GLU A OE2 1 
ATOM   276  N  N   . LEU A 1 36  ? -23.276 45.174  25.991  1.00 24.76 ? 36  LEU A N   1 
ATOM   277  C  CA  . LEU A 1 36  ? -22.249 46.244  26.134  1.00 24.08 ? 36  LEU A CA  1 
ATOM   278  C  C   . LEU A 1 36  ? -21.839 46.832  24.772  1.00 23.46 ? 36  LEU A C   1 
ATOM   279  O  O   . LEU A 1 36  ? -21.406 48.018  24.761  1.00 21.37 ? 36  LEU A O   1 
ATOM   280  C  CB  . LEU A 1 36  ? -21.041 45.656  26.853  1.00 24.23 ? 36  LEU A CB  1 
ATOM   281  C  CG  . LEU A 1 36  ? -21.334 45.093  28.238  1.00 24.11 ? 36  LEU A CG  1 
ATOM   282  C  CD1 . LEU A 1 36  ? -20.037 44.753  28.966  1.00 21.70 ? 36  LEU A CD1 1 
ATOM   283  C  CD2 . LEU A 1 36  ? -22.202 46.076  29.029  1.00 24.51 ? 36  LEU A CD2 1 
ATOM   284  N  N   . GLY A 1 37  ? -21.928 46.048  23.691  1.00 21.35 ? 37  GLY A N   1 
ATOM   285  C  CA  . GLY A 1 37  ? -21.750 46.545  22.315  1.00 21.93 ? 37  GLY A CA  1 
ATOM   286  C  C   . GLY A 1 37  ? -20.423 46.154  21.687  1.00 21.35 ? 37  GLY A C   1 
ATOM   287  O  O   . GLY A 1 37  ? -19.916 45.034  21.944  1.00 22.33 ? 37  GLY A O   1 
ATOM   288  N  N   . GLU A 1 38  ? -19.879 47.046  20.868  1.00 20.62 ? 38  GLU A N   1 
ATOM   289  C  CA  . GLU A 1 38  ? -18.863 46.693  19.848  1.00 21.43 ? 38  GLU A CA  1 
ATOM   290  C  C   . GLU A 1 38  ? -17.541 46.295  20.529  1.00 22.68 ? 38  GLU A C   1 
ATOM   291  O  O   . GLU A 1 38  ? -16.755 45.557  19.893  1.00 21.25 ? 38  GLU A O   1 
ATOM   292  C  CB  . GLU A 1 38  ? -18.746 47.817  18.818  1.00 20.89 ? 38  GLU A CB  1 
ATOM   293  C  CG  . GLU A 1 38  ? -18.174 49.111  19.340  1.00 20.69 ? 38  GLU A CG  1 
ATOM   294  C  CD  . GLU A 1 38  ? -17.828 50.112  18.242  1.00 22.50 ? 38  GLU A CD  1 
ATOM   295  O  OE1 . GLU A 1 38  ? -17.533 49.692  17.080  1.00 21.62 ? 38  GLU A OE1 1 
ATOM   296  O  OE2 . GLU A 1 38  ? -17.822 51.329  18.550  1.00 25.18 ? 38  GLU A OE2 1 
ATOM   297  N  N   . ILE A 1 39  ? -17.316 46.686  21.790  1.00 23.23 ? 39  ILE A N   1 
ATOM   298  C  CA  . ILE A 1 39  ? -16.048 46.393  22.527  1.00 22.89 ? 39  ILE A CA  1 
ATOM   299  C  C   . ILE A 1 39  ? -16.294 46.448  24.041  1.00 23.27 ? 39  ILE A C   1 
ATOM   300  O  O   . ILE A 1 39  ? -16.935 47.422  24.520  1.00 20.72 ? 39  ILE A O   1 
ATOM   301  C  CB  . ILE A 1 39  ? -14.940 47.357  22.076  1.00 25.25 ? 39  ILE A CB  1 
ATOM   302  C  CG1 . ILE A 1 39  ? -13.609 47.059  22.770  1.00 26.37 ? 39  ILE A CG1 1 
ATOM   303  C  CG2 . ILE A 1 39  ? -15.366 48.809  22.267  1.00 27.92 ? 39  ILE A CG2 1 
ATOM   304  C  CD1 . ILE A 1 39  ? -12.393 47.634  22.068  1.00 26.53 ? 39  ILE A CD1 1 
ATOM   305  N  N   . PHE A 1 40  ? -15.833 45.411  24.759  1.00 22.49 ? 40  PHE A N   1 
ATOM   306  C  CA  . PHE A 1 40  ? -15.739 45.376  26.241  1.00 22.17 ? 40  PHE A CA  1 
ATOM   307  C  C   . PHE A 1 40  ? -14.412 44.728  26.698  1.00 22.73 ? 40  PHE A C   1 
ATOM   308  O  O   . PHE A 1 40  ? -13.834 43.853  26.017  1.00 20.83 ? 40  PHE A O   1 
ATOM   309  C  CB  . PHE A 1 40  ? -16.979 44.709  26.846  1.00 21.41 ? 40  PHE A CB  1 
ATOM   310  C  CG  . PHE A 1 40  ? -17.194 43.258  26.485  1.00 21.71 ? 40  PHE A CG  1 
ATOM   311  C  CD1 . PHE A 1 40  ? -16.617 42.239  27.232  1.00 21.54 ? 40  PHE A CD1 1 
ATOM   312  C  CD2 . PHE A 1 40  ? -17.971 42.905  25.392  1.00 21.82 ? 40  PHE A CD2 1 
ATOM   313  C  CE1 . PHE A 1 40  ? -16.837 40.908  26.909  1.00 20.83 ? 40  PHE A CE1 1 
ATOM   314  C  CE2 . PHE A 1 40  ? -18.174 41.575  25.066  1.00 21.31 ? 40  PHE A CE2 1 
ATOM   315  C  CZ  . PHE A 1 40  ? -17.605 40.580  25.820  1.00 20.56 ? 40  PHE A CZ  1 
ATOM   316  N  N   . LYS A 1 41  ? -13.929 45.168  27.859  1.00 23.21 ? 41  LYS A N   1 
ATOM   317  C  CA  . LYS A 1 41  ? -12.697 44.641  28.486  1.00 25.56 ? 41  LYS A CA  1 
ATOM   318  C  C   . LYS A 1 41  ? -13.128 43.591  29.512  1.00 25.23 ? 41  LYS A C   1 
ATOM   319  O  O   . LYS A 1 41  ? -14.181 43.786  30.189  1.00 23.86 ? 41  LYS A O   1 
ATOM   320  C  CB  . LYS A 1 41  ? -11.827 45.776  29.042  1.00 28.90 ? 41  LYS A CB  1 
ATOM   321  C  CG  . LYS A 1 41  ? -12.353 46.505  30.266  1.00 33.83 ? 41  LYS A CG  1 
ATOM   322  C  CD  . LYS A 1 41  ? -11.653 47.826  30.507  1.00 39.94 ? 41  LYS A CD  1 
ATOM   323  C  CE  . LYS A 1 41  ? -12.373 48.725  31.498  1.00 45.35 ? 41  LYS A CE  1 
ATOM   324  N  NZ  . LYS A 1 41  ? -11.816 50.101  31.490  1.00 47.02 ? 41  LYS A NZ  1 
ATOM   325  N  N   . PHE A 1 42  ? -12.399 42.474  29.513  1.00 23.82 ? 42  PHE A N   1 
ATOM   326  C  CA  . PHE A 1 42  ? -12.599 41.294  30.384  1.00 24.00 ? 42  PHE A CA  1 
ATOM   327  C  C   . PHE A 1 42  ? -11.287 41.107  31.133  1.00 24.99 ? 42  PHE A C   1 
ATOM   328  O  O   . PHE A 1 42  ? -10.224 40.906  30.468  1.00 23.80 ? 42  PHE A O   1 
ATOM   329  C  CB  . PHE A 1 42  ? -13.016 40.068  29.570  1.00 23.69 ? 42  PHE A CB  1 
ATOM   330  C  CG  . PHE A 1 42  ? -13.518 38.906  30.393  1.00 23.68 ? 42  PHE A CG  1 
ATOM   331  C  CD1 . PHE A 1 42  ? -12.693 38.274  31.310  1.00 22.87 ? 42  PHE A CD1 1 
ATOM   332  C  CD2 . PHE A 1 42  ? -14.820 38.452  30.262  1.00 23.71 ? 42  PHE A CD2 1 
ATOM   333  C  CE1 . PHE A 1 42  ? -13.155 37.213  32.071  1.00 23.10 ? 42  PHE A CE1 1 
ATOM   334  C  CE2 . PHE A 1 42  ? -15.278 37.382  31.020  1.00 24.45 ? 42  PHE A CE2 1 
ATOM   335  C  CZ  . PHE A 1 42  ? -14.447 36.764  31.919  1.00 23.43 ? 42  PHE A CZ  1 
ATOM   336  N  N   . GLU A 1 43  ? -11.372 41.257  32.452  1.00 26.69 ? 43  GLU A N   1 
ATOM   337  C  CA  . GLU A 1 43  ? -10.228 41.255  33.389  1.00 28.72 ? 43  GLU A CA  1 
ATOM   338  C  C   . GLU A 1 43  ? -10.286 40.043  34.315  1.00 27.21 ? 43  GLU A C   1 
ATOM   339  O  O   . GLU A 1 43  ? -11.307 39.828  34.995  1.00 23.08 ? 43  GLU A O   1 
ATOM   340  C  CB  . GLU A 1 43  ? -10.246 42.516  34.237  1.00 31.53 ? 43  GLU A CB  1 
ATOM   341  C  CG  . GLU A 1 43  ? -9.814  43.746  33.473  1.00 37.05 ? 43  GLU A CG  1 
ATOM   342  C  CD  . GLU A 1 43  ? -9.538  44.946  34.367  1.00 44.00 ? 43  GLU A CD  1 
ATOM   343  O  OE1 . GLU A 1 43  ? -9.544  44.781  35.621  1.00 47.24 ? 43  GLU A OE1 1 
ATOM   344  O  OE2 . GLU A 1 43  ? -9.333  46.043  33.810  1.00 50.43 ? 43  GLU A OE2 1 
ATOM   345  N  N   . ALA A 1 44  ? -9.189  39.301  34.355  1.00 26.99 ? 44  ALA A N   1 
ATOM   346  C  CA  . ALA A 1 44  ? -8.938  38.241  35.343  1.00 26.55 ? 44  ALA A CA  1 
ATOM   347  C  C   . ALA A 1 44  ? -7.714  38.674  36.134  1.00 28.31 ? 44  ALA A C   1 
ATOM   348  O  O   . ALA A 1 44  ? -7.010  39.570  35.664  1.00 28.11 ? 44  ALA A O   1 
ATOM   349  C  CB  . ALA A 1 44  ? -8.747  36.932  34.634  1.00 26.15 ? 44  ALA A CB  1 
ATOM   350  N  N   . PRO A 1 45  ? -7.468  38.090  37.343  1.00 27.87 ? 45  PRO A N   1 
ATOM   351  C  CA  . PRO A 1 45  ? -6.201  38.262  38.073  1.00 27.13 ? 45  PRO A CA  1 
ATOM   352  C  C   . PRO A 1 45  ? -4.940  38.169  37.189  1.00 27.66 ? 45  PRO A C   1 
ATOM   353  O  O   . PRO A 1 45  ? -4.101  39.064  37.272  1.00 30.37 ? 45  PRO A O   1 
ATOM   354  C  CB  . PRO A 1 45  ? -6.260  37.112  39.083  1.00 24.87 ? 45  PRO A CB  1 
ATOM   355  C  CG  . PRO A 1 45  ? -7.719  37.027  39.399  1.00 25.07 ? 45  PRO A CG  1 
ATOM   356  C  CD  . PRO A 1 45  ? -8.399  37.196  38.057  1.00 24.92 ? 45  PRO A CD  1 
ATOM   357  N  N   . GLY A 1 46  ? -4.864  37.182  36.297  1.00 26.45 ? 46  GLY A N   1 
ATOM   358  C  CA  . GLY A 1 46  ? -3.683  36.987  35.427  1.00 31.77 ? 46  GLY A CA  1 
ATOM   359  C  C   . GLY A 1 46  ? -3.530  37.957  34.245  1.00 32.24 ? 46  GLY A C   1 
ATOM   360  O  O   . GLY A 1 46  ? -2.376  38.173  33.854  1.00 32.77 ? 46  GLY A O   1 
ATOM   361  N  N   . TRP A 1 47  ? -4.612  38.470  33.641  1.00 32.11 ? 47  TRP A N   1 
ATOM   362  C  CA  . TRP A 1 47  ? -4.619  38.979  32.236  1.00 31.48 ? 47  TRP A CA  1 
ATOM   363  C  C   . TRP A 1 47  ? -5.859  39.832  31.938  1.00 32.05 ? 47  TRP A C   1 
ATOM   364  O  O   . TRP A 1 47  ? -6.832  39.812  32.725  1.00 36.48 ? 47  TRP A O   1 
ATOM   365  C  CB  . TRP A 1 47  ? -4.561  37.800  31.251  1.00 32.19 ? 47  TRP A CB  1 
ATOM   366  C  CG  . TRP A 1 47  ? -5.580  36.743  31.567  1.00 35.35 ? 47  TRP A CG  1 
ATOM   367  C  CD1 . TRP A 1 47  ? -5.404  35.645  32.363  1.00 34.85 ? 47  TRP A CD1 1 
ATOM   368  C  CD2 . TRP A 1 47  ? -6.965  36.723  31.170  1.00 32.18 ? 47  TRP A CD2 1 
ATOM   369  N  NE1 . TRP A 1 47  ? -6.575  34.945  32.477  1.00 33.61 ? 47  TRP A NE1 1 
ATOM   370  C  CE2 . TRP A 1 47  ? -7.545  35.571  31.746  1.00 32.58 ? 47  TRP A CE2 1 
ATOM   371  C  CE3 . TRP A 1 47  ? -7.765  37.561  30.390  1.00 31.25 ? 47  TRP A CE3 1 
ATOM   372  C  CZ2 . TRP A 1 47  ? -8.880  35.222  31.540  1.00 33.84 ? 47  TRP A CZ2 1 
ATOM   373  C  CZ3 . TRP A 1 47  ? -9.080  37.209  30.173  1.00 32.96 ? 47  TRP A CZ3 1 
ATOM   374  C  CH2 . TRP A 1 47  ? -9.633  36.062  30.748  1.00 33.28 ? 47  TRP A CH2 1 
ATOM   375  N  N   . VAL A 1 48  ? -5.838  40.506  30.786  1.00 30.53 ? 48  VAL A N   1 
ATOM   376  C  CA  . VAL A 1 48  ? -6.943  41.355  30.263  1.00 26.66 ? 48  VAL A CA  1 
ATOM   377  C  C   . VAL A 1 48  ? -7.160  40.979  28.802  1.00 26.70 ? 48  VAL A C   1 
ATOM   378  O  O   . VAL A 1 48  ? -6.172  40.891  28.055  1.00 24.94 ? 48  VAL A O   1 
ATOM   379  C  CB  . VAL A 1 48  ? -6.611  42.845  30.429  1.00 25.47 ? 48  VAL A CB  1 
ATOM   380  C  CG1 . VAL A 1 48  ? -7.656  43.750  29.797  1.00 24.66 ? 48  VAL A CG1 1 
ATOM   381  C  CG2 . VAL A 1 48  ? -6.401  43.177  31.903  1.00 27.12 ? 48  VAL A CG2 1 
ATOM   382  N  N   . LEU A 1 49  ? -8.417  40.760  28.426  1.00 26.73 ? 49  LEU A N   1 
ATOM   383  C  CA  . LEU A 1 49  ? -8.809  40.499  27.021  1.00 25.75 ? 49  LEU A CA  1 
ATOM   384  C  C   . LEU A 1 49  ? -9.814  41.565  26.616  1.00 27.08 ? 49  LEU A C   1 
ATOM   385  O  O   . LEU A 1 49  ? -10.732 41.809  27.403  1.00 28.29 ? 49  LEU A O   1 
ATOM   386  C  CB  . LEU A 1 49  ? -9.458  39.123  26.922  1.00 25.26 ? 49  LEU A CB  1 
ATOM   387  C  CG  . LEU A 1 49  ? -8.639  38.037  26.242  1.00 25.17 ? 49  LEU A CG  1 
ATOM   388  C  CD1 . LEU A 1 49  ? -9.508  36.807  26.052  1.00 24.96 ? 49  LEU A CD1 1 
ATOM   389  C  CD2 . LEU A 1 49  ? -8.086  38.511  24.903  1.00 24.74 ? 49  LEU A CD2 1 
ATOM   390  N  N   . ARG A 1 50  ? -9.645  42.171  25.446  1.00 24.66 ? 50  ARG A N   1 
ATOM   391  C  CA  . ARG A 1 50  ? -10.677 43.083  24.910  1.00 26.22 ? 50  ARG A CA  1 
ATOM   392  C  C   . ARG A 1 50  ? -11.434 42.335  23.806  1.00 25.11 ? 50  ARG A C   1 
ATOM   393  O  O   . ARG A 1 50  ? -10.773 41.919  22.843  1.00 22.65 ? 50  ARG A O   1 
ATOM   394  C  CB  . ARG A 1 50  ? -10.018 44.384  24.444  1.00 26.26 ? 50  ARG A CB  1 
ATOM   395  C  CG  . ARG A 1 50  ? -9.314  45.135  25.562  1.00 25.63 ? 50  ARG A CG  1 
ATOM   396  C  CD  . ARG A 1 50  ? -7.965  45.607  25.104  1.00 25.89 ? 50  ARG A CD  1 
ATOM   397  N  NE  . ARG A 1 50  ? -7.143  46.118  26.186  1.00 27.22 ? 50  ARG A NE  1 
ATOM   398  C  CZ  . ARG A 1 50  ? -6.202  45.446  26.856  1.00 29.34 ? 50  ARG A CZ  1 
ATOM   399  N  NH1 . ARG A 1 50  ? -5.903  44.182  26.574  1.00 29.07 ? 50  ARG A NH1 1 
ATOM   400  N  NH2 . ARG A 1 50  ? -5.544  46.071  27.823  1.00 30.30 ? 50  ARG A NH2 1 
ATOM   401  N  N   . TYR A 1 51  ? -12.763 42.207  23.948  1.00 23.88 ? 51  TYR A N   1 
ATOM   402  C  CA  . TYR A 1 51  ? -13.662 41.473  23.018  1.00 21.43 ? 51  TYR A CA  1 
ATOM   403  C  C   . TYR A 1 51  ? -14.224 42.427  21.969  1.00 21.21 ? 51  TYR A C   1 
ATOM   404  O  O   . TYR A 1 51  ? -14.824 43.442  22.364  1.00 20.14 ? 51  TYR A O   1 
ATOM   405  C  CB  . TYR A 1 51  ? -14.764 40.773  23.799  1.00 19.96 ? 51  TYR A CB  1 
ATOM   406  C  CG  . TYR A 1 51  ? -14.255 39.541  24.493  1.00 20.21 ? 51  TYR A CG  1 
ATOM   407  C  CD1 . TYR A 1 51  ? -14.140 38.335  23.825  1.00 19.91 ? 51  TYR A CD1 1 
ATOM   408  C  CD2 . TYR A 1 51  ? -13.806 39.605  25.800  1.00 19.52 ? 51  TYR A CD2 1 
ATOM   409  C  CE1 . TYR A 1 51  ? -13.664 37.201  24.459  1.00 19.96 ? 51  TYR A CE1 1 
ATOM   410  C  CE2 . TYR A 1 51  ? -13.323 38.485  26.446  1.00 20.33 ? 51  TYR A CE2 1 
ATOM   411  C  CZ  . TYR A 1 51  ? -13.248 37.273  25.779  1.00 20.50 ? 51  TYR A CZ  1 
ATOM   412  O  OH  . TYR A 1 51  ? -12.796 36.171  26.462  1.00 20.24 ? 51  TYR A OH  1 
ATOM   413  N  N   . LEU A 1 52  ? -13.993 42.112  20.690  1.00 20.79 ? 52  LEU A N   1 
ATOM   414  C  CA  . LEU A 1 52  ? -14.436 42.930  19.525  1.00 22.38 ? 52  LEU A CA  1 
ATOM   415  C  C   . LEU A 1 52  ? -15.603 42.224  18.812  1.00 22.16 ? 52  LEU A C   1 
ATOM   416  O  O   . LEU A 1 52  ? -15.464 41.010  18.488  1.00 25.49 ? 52  LEU A O   1 
ATOM   417  C  CB  . LEU A 1 52  ? -13.257 43.133  18.567  1.00 23.57 ? 52  LEU A CB  1 
ATOM   418  C  CG  . LEU A 1 52  ? -12.086 43.978  19.077  1.00 24.39 ? 52  LEU A CG  1 
ATOM   419  C  CD1 . LEU A 1 52  ? -11.066 44.144  17.977  1.00 24.34 ? 52  LEU A CD1 1 
ATOM   420  C  CD2 . LEU A 1 52  ? -12.531 45.347  19.563  1.00 25.68 ? 52  LEU A CD2 1 
ATOM   421  N  N   . SER A 1 53  ? -16.697 42.951  18.547  1.00 22.06 ? 53  SER A N   1 
ATOM   422  C  CA  . SER A 1 53  ? -17.967 42.444  17.936  1.00 22.49 ? 53  SER A CA  1 
ATOM   423  C  C   . SER A 1 53  ? -18.388 43.209  16.655  1.00 21.63 ? 53  SER A C   1 
ATOM   424  O  O   . SER A 1 53  ? -19.288 42.696  15.972  1.00 21.71 ? 53  SER A O   1 
ATOM   425  C  CB  . SER A 1 53  ? -19.057 42.487  18.979  1.00 22.07 ? 53  SER A CB  1 
ATOM   426  O  OG  . SER A 1 53  ? -18.774 41.536  20.006  1.00 22.02 ? 53  SER A OG  1 
ATOM   427  N  N   . SER A 1 54  ? -17.806 44.381  16.340  1.00 19.74 ? 54  SER A N   1 
ATOM   428  C  CA  . SER A 1 54  ? -18.198 45.226  15.177  1.00 19.44 ? 54  SER A CA  1 
ATOM   429  C  C   . SER A 1 54  ? -17.215 45.062  14.015  1.00 18.96 ? 54  SER A C   1 
ATOM   430  O  O   . SER A 1 54  ? -16.013 44.877  14.239  1.00 18.20 ? 54  SER A O   1 
ATOM   431  C  CB  . SER A 1 54  ? -18.324 46.669  15.549  1.00 19.48 ? 54  SER A CB  1 
ATOM   432  O  OG  . SER A 1 54  ? -17.070 47.200  15.934  1.00 21.26 ? 54  SER A OG  1 
ATOM   433  N  N   . GLN A 1 55  ? -17.737 45.130  12.801  1.00 19.74 ? 55  GLN A N   1 
ATOM   434  C  CA  . GLN A 1 55  ? -16.923 45.179  11.571  1.00 20.57 ? 55  GLN A CA  1 
ATOM   435  C  C   . GLN A 1 55  ? -15.969 46.359  11.706  1.00 19.32 ? 55  GLN A C   1 
ATOM   436  O  O   . GLN A 1 55  ? -14.834 46.226  11.324  1.00 19.89 ? 55  GLN A O   1 
ATOM   437  C  CB  . GLN A 1 55  ? -17.806 45.324  10.334  1.00 22.11 ? 55  GLN A CB  1 
ATOM   438  C  CG  . GLN A 1 55  ? -17.416 46.512  9.448   1.00 24.04 ? 55  GLN A CG  1 
ATOM   439  C  CD  . GLN A 1 55  ? -16.400 46.107  8.419   1.00 25.78 ? 55  GLN A CD  1 
ATOM   440  O  OE1 . GLN A 1 55  ? -16.146 44.934  8.181   1.00 33.36 ? 55  GLN A OE1 1 
ATOM   441  N  NE2 . GLN A 1 55  ? -15.803 47.082  7.790   1.00 29.27 ? 55  GLN A NE2 1 
ATOM   442  N  N   . ARG A 1 56  ? -16.467 47.496  12.152  1.00 20.86 ? 56  ARG A N   1 
ATOM   443  C  CA  . ARG A 1 56  ? -15.717 48.780  12.178  1.00 23.78 ? 56  ARG A CA  1 
ATOM   444  C  C   . ARG A 1 56  ? -14.347 48.516  12.823  1.00 23.57 ? 56  ARG A C   1 
ATOM   445  O  O   . ARG A 1 56  ? -13.300 48.801  12.197  1.00 27.09 ? 56  ARG A O   1 
ATOM   446  C  CB  . ARG A 1 56  ? -16.604 49.797  12.910  1.00 26.36 ? 56  ARG A CB  1 
ATOM   447  C  CG  . ARG A 1 56  ? -16.017 51.177  13.181  1.00 28.61 ? 56  ARG A CG  1 
ATOM   448  C  CD  . ARG A 1 56  ? -16.596 51.668  14.506  1.00 31.57 ? 56  ARG A CD  1 
ATOM   449  N  NE  . ARG A 1 56  ? -15.774 52.720  15.075  1.00 33.82 ? 56  ARG A NE  1 
ATOM   450  C  CZ  . ARG A 1 56  ? -15.523 52.913  16.361  1.00 35.07 ? 56  ARG A CZ  1 
ATOM   451  N  NH1 . ARG A 1 56  ? -16.000 52.117  17.302  1.00 36.47 ? 56  ARG A NH1 1 
ATOM   452  N  NH2 . ARG A 1 56  ? -14.754 53.922  16.707  1.00 38.67 ? 56  ARG A NH2 1 
ATOM   453  N  N   . LEU A 1 57  ? -14.361 47.915  14.007  1.00 22.08 ? 57  LEU A N   1 
ATOM   454  C  CA  . LEU A 1 57  ? -13.175 47.704  14.864  1.00 20.61 ? 57  LEU A CA  1 
ATOM   455  C  C   . LEU A 1 57  ? -12.385 46.486  14.382  1.00 20.00 ? 57  LEU A C   1 
ATOM   456  O  O   . LEU A 1 57  ? -11.132 46.530  14.399  1.00 17.12 ? 57  LEU A O   1 
ATOM   457  C  CB  . LEU A 1 57  ? -13.676 47.501  16.297  1.00 21.12 ? 57  LEU A CB  1 
ATOM   458  C  CG  . LEU A 1 57  ? -14.255 48.742  16.971  1.00 22.17 ? 57  LEU A CG  1 
ATOM   459  C  CD1 . LEU A 1 57  ? -14.633 48.451  18.406  1.00 22.38 ? 57  LEU A CD1 1 
ATOM   460  C  CD2 . LEU A 1 57  ? -13.256 49.888  16.923  1.00 22.92 ? 57  LEU A CD2 1 
ATOM   461  N  N   . ILE A 1 58  ? -13.091 45.409  14.019  1.00 20.23 ? 58  ILE A N   1 
ATOM   462  C  CA  . ILE A 1 58  ? -12.436 44.125  13.645  1.00 19.78 ? 58  ILE A CA  1 
ATOM   463  C  C   . ILE A 1 58  ? -11.635 44.333  12.363  1.00 19.87 ? 58  ILE A C   1 
ATOM   464  O  O   . ILE A 1 58  ? -10.614 43.651  12.233  1.00 18.25 ? 58  ILE A O   1 
ATOM   465  C  CB  . ILE A 1 58  ? -13.435 42.955  13.586  1.00 19.88 ? 58  ILE A CB  1 
ATOM   466  C  CG1 . ILE A 1 58  ? -13.879 42.556  14.998  1.00 20.97 ? 58  ILE A CG1 1 
ATOM   467  C  CG2 . ILE A 1 58  ? -12.854 41.767  12.841  1.00 20.01 ? 58  ILE A CG2 1 
ATOM   468  C  CD1 . ILE A 1 58  ? -15.223 41.847  15.084  1.00 20.91 ? 58  ILE A CD1 1 
ATOM   469  N  N   . LYS A 1 59  ? -12.036 45.251  11.478  1.00 22.32 ? 59  LYS A N   1 
ATOM   470  C  CA  . LYS A 1 59  ? -11.287 45.500  10.218  1.00 26.34 ? 59  LYS A CA  1 
ATOM   471  C  C   . LYS A 1 59  ? -9.947  46.171  10.571  1.00 26.15 ? 59  LYS A C   1 
ATOM   472  O  O   . LYS A 1 59  ? -8.941  45.919  9.866   1.00 24.77 ? 59  LYS A O   1 
ATOM   473  C  CB  . LYS A 1 59  ? -12.118 46.304  9.209   1.00 31.79 ? 59  LYS A CB  1 
ATOM   474  C  CG  . LYS A 1 59  ? -11.989 47.818  9.305   1.00 35.50 ? 59  LYS A CG  1 
ATOM   475  C  CD  . LYS A 1 59  ? -13.137 48.550  8.681   1.00 36.74 ? 59  LYS A CD  1 
ATOM   476  C  CE  . LYS A 1 59  ? -13.033 50.044  8.891   1.00 39.07 ? 59  LYS A CE  1 
ATOM   477  N  NZ  . LYS A 1 59  ? -14.100 50.757  8.144   1.00 42.25 ? 59  LYS A NZ  1 
ATOM   478  N  N   . GLU A 1 60  ? -9.907  46.966  11.641  1.00 24.43 ? 60  GLU A N   1 
ATOM   479  C  CA  . GLU A 1 60  ? -8.639  47.563  12.126  1.00 24.35 ? 60  GLU A CA  1 
ATOM   480  C  C   . GLU A 1 60  ? -7.757  46.452  12.698  1.00 23.18 ? 60  GLU A C   1 
ATOM   481  O  O   . GLU A 1 60  ? -6.590  46.338  12.308  1.00 24.24 ? 60  GLU A O   1 
ATOM   482  C  CB  . GLU A 1 60  ? -8.905  48.645  13.171  1.00 26.35 ? 60  GLU A CB  1 
ATOM   483  C  CG  . GLU A 1 60  ? -8.925  50.045  12.595  1.00 28.30 ? 60  GLU A CG  1 
ATOM   484  C  CD  . GLU A 1 60  ? -8.898  51.136  13.645  1.00 27.79 ? 60  GLU A CD  1 
ATOM   485  O  OE1 . GLU A 1 60  ? -9.860  51.872  13.719  1.00 33.56 ? 60  GLU A OE1 1 
ATOM   486  O  OE2 . GLU A 1 60  ? -7.917  51.244  14.374  1.00 29.03 ? 60  GLU A OE2 1 
ATOM   487  N  N   . ALA A 1 61  ? -8.316  45.632  13.573  1.00 23.03 ? 61  ALA A N   1 
ATOM   488  C  CA  . ALA A 1 61  ? -7.593  44.568  14.287  1.00 22.52 ? 61  ALA A CA  1 
ATOM   489  C  C   . ALA A 1 61  ? -7.041  43.591  13.251  1.00 24.13 ? 61  ALA A C   1 
ATOM   490  O  O   . ALA A 1 61  ? -6.024  42.975  13.528  1.00 29.52 ? 61  ALA A O   1 
ATOM   491  C  CB  . ALA A 1 61  ? -8.511  43.903  15.277  1.00 22.60 ? 61  ALA A CB  1 
ATOM   492  N  N   . CYS A 1 62  ? -7.652  43.493  12.072  1.00 24.32 ? 62  CYS A N   1 
ATOM   493  C  CA  . CYS A 1 62  ? -7.190  42.593  10.972  1.00 24.08 ? 62  CYS A CA  1 
ATOM   494  C  C   . CYS A 1 62  ? -6.103  43.250  10.101  1.00 22.14 ? 62  CYS A C   1 
ATOM   495  O  O   . CYS A 1 62  ? -5.699  42.623  9.071   1.00 22.78 ? 62  CYS A O   1 
ATOM   496  C  CB  . CYS A 1 62  ? -8.371  42.130  10.125  1.00 23.66 ? 62  CYS A CB  1 
ATOM   497  S  SG  . CYS A 1 62  ? -9.315  40.811  10.931  1.00 24.04 ? 62  CYS A SG  1 
ATOM   498  N  N   . ASP A 1 63  ? -5.635  44.435  10.485  1.00 20.89 ? 63  ASP A N   1 
ATOM   499  C  CA  . ASP A 1 63  ? -4.434  45.092  9.904   1.00 22.70 ? 63  ASP A CA  1 
ATOM   500  C  C   . ASP A 1 63  ? -3.182  44.376  10.439  1.00 23.04 ? 63  ASP A C   1 
ATOM   501  O  O   . ASP A 1 63  ? -2.827  44.573  11.621  1.00 24.65 ? 63  ASP A O   1 
ATOM   502  C  CB  . ASP A 1 63  ? -4.457  46.596  10.205  1.00 24.24 ? 63  ASP A CB  1 
ATOM   503  C  CG  . ASP A 1 63  ? -3.446  47.426  9.441   1.00 25.26 ? 63  ASP A CG  1 
ATOM   504  O  OD1 . ASP A 1 63  ? -2.392  46.868  9.057   1.00 27.51 ? 63  ASP A OD1 1 
ATOM   505  O  OD2 . ASP A 1 63  ? -3.708  48.636  9.253   1.00 28.08 ? 63  ASP A OD2 1 
ATOM   506  N  N   . GLU A 1 64  ? -2.534  43.569  9.593   1.00 23.67 ? 64  GLU A N   1 
ATOM   507  C  CA  . GLU A 1 64  ? -1.334  42.749  9.922   1.00 25.04 ? 64  GLU A CA  1 
ATOM   508  C  C   . GLU A 1 64  ? -0.112  43.623  10.215  1.00 24.41 ? 64  GLU A C   1 
ATOM   509  O  O   . GLU A 1 64  ? 0.800   43.108  10.832  1.00 26.89 ? 64  GLU A O   1 
ATOM   510  C  CB  . GLU A 1 64  ? -0.989  41.802  8.777   1.00 25.52 ? 64  GLU A CB  1 
ATOM   511  C  CG  . GLU A 1 64  ? -1.945  40.638  8.733   1.00 27.85 ? 64  GLU A CG  1 
ATOM   512  C  CD  . GLU A 1 64  ? -1.705  39.694  7.579   1.00 28.64 ? 64  GLU A CD  1 
ATOM   513  O  OE1 . GLU A 1 64  ? -1.955  40.111  6.419   1.00 29.37 ? 64  GLU A OE1 1 
ATOM   514  O  OE2 . GLU A 1 64  ? -1.278  38.550  7.856   1.00 28.33 ? 64  GLU A OE2 1 
ATOM   515  N  N   . SER A 1 65  ? -0.083  44.875  9.779   1.00 23.58 ? 65  SER A N   1 
ATOM   516  C  CA  . SER A 1 65  ? 1.015   45.816  10.090  1.00 24.37 ? 65  SER A CA  1 
ATOM   517  C  C   . SER A 1 65  ? 0.831   46.378  11.509  1.00 25.14 ? 65  SER A C   1 
ATOM   518  O  O   . SER A 1 65  ? 1.777   46.988  12.026  1.00 27.48 ? 65  SER A O   1 
ATOM   519  C  CB  . SER A 1 65  ? 1.073   46.906  9.041   1.00 26.22 ? 65  SER A CB  1 
ATOM   520  O  OG  . SER A 1 65  ? -0.054  47.762  9.129   1.00 26.11 ? 65  SER A OG  1 
ATOM   521  N  N   . ARG A 1 66  ? -0.331  46.167  12.139  1.00 24.50 ? 66  ARG A N   1 
ATOM   522  C  CA  . ARG A 1 66  ? -0.646  46.722  13.482  1.00 23.93 ? 66  ARG A CA  1 
ATOM   523  C  C   . ARG A 1 66  ? -0.891  45.604  14.493  1.00 23.18 ? 66  ARG A C   1 
ATOM   524  O  O   . ARG A 1 66  ? -0.619  45.819  15.676  1.00 22.92 ? 66  ARG A O   1 
ATOM   525  C  CB  . ARG A 1 66  ? -1.882  47.621  13.398  1.00 25.31 ? 66  ARG A CB  1 
ATOM   526  C  CG  . ARG A 1 66  ? -1.724  48.815  12.456  1.00 27.29 ? 66  ARG A CG  1 
ATOM   527  C  CD  . ARG A 1 66  ? -2.990  49.648  12.429  1.00 27.84 ? 66  ARG A CD  1 
ATOM   528  N  NE  . ARG A 1 66  ? -3.285  50.197  13.754  1.00 30.15 ? 66  ARG A NE  1 
ATOM   529  C  CZ  . ARG A 1 66  ? -4.489  50.602  14.192  1.00 32.35 ? 66  ARG A CZ  1 
ATOM   530  N  NH1 . ARG A 1 66  ? -5.562  50.528  13.418  1.00 30.28 ? 66  ARG A NH1 1 
ATOM   531  N  NH2 . ARG A 1 66  ? -4.616  51.088  15.424  1.00 34.48 ? 66  ARG A NH2 1 
ATOM   532  N  N   . PHE A 1 67  ? -1.419  44.459  14.060  1.00 24.08 ? 67  PHE A N   1 
ATOM   533  C  CA  . PHE A 1 67  ? -1.807  43.353  14.970  1.00 23.56 ? 67  PHE A CA  1 
ATOM   534  C  C   . PHE A 1 67  ? -1.322  42.027  14.394  1.00 22.30 ? 67  PHE A C   1 
ATOM   535  O  O   . PHE A 1 67  ? -1.176  41.902  13.183  1.00 22.11 ? 67  PHE A O   1 
ATOM   536  C  CB  . PHE A 1 67  ? -3.313  43.377  15.230  1.00 24.03 ? 67  PHE A CB  1 
ATOM   537  C  CG  . PHE A 1 67  ? -3.810  44.665  15.844  1.00 24.59 ? 67  PHE A CG  1 
ATOM   538  C  CD1 . PHE A 1 67  ? -4.228  45.721  15.041  1.00 25.01 ? 67  PHE A CD1 1 
ATOM   539  C  CD2 . PHE A 1 67  ? -3.887  44.815  17.219  1.00 23.19 ? 67  PHE A CD2 1 
ATOM   540  C  CE1 . PHE A 1 67  ? -4.674  46.907  15.601  1.00 24.87 ? 67  PHE A CE1 1 
ATOM   541  C  CE2 . PHE A 1 67  ? -4.335  46.002  17.773  1.00 24.32 ? 67  PHE A CE2 1 
ATOM   542  C  CZ  . PHE A 1 67  ? -4.738  47.042  16.969  1.00 23.90 ? 67  PHE A CZ  1 
ATOM   543  N  N   . ASP A 1 68  ? -1.071  41.081  15.290  1.00 22.21 ? 68  ASP A N   1 
ATOM   544  C  CA  . ASP A 1 68  ? -0.530  39.740  14.978  1.00 21.63 ? 68  ASP A CA  1 
ATOM   545  C  C   . ASP A 1 68  ? -1.346  38.745  15.790  1.00 20.82 ? 68  ASP A C   1 
ATOM   546  O  O   . ASP A 1 68  ? -1.921  39.149  16.810  1.00 20.34 ? 68  ASP A O   1 
ATOM   547  C  CB  . ASP A 1 68  ? 0.969   39.654  15.288  1.00 22.06 ? 68  ASP A CB  1 
ATOM   548  C  CG  . ASP A 1 68  ? 1.628   38.358  14.836  1.00 22.62 ? 68  ASP A CG  1 
ATOM   549  O  OD1 . ASP A 1 68  ? 1.128   37.749  13.917  1.00 21.70 ? 68  ASP A OD1 1 
ATOM   550  O  OD2 . ASP A 1 68  ? 2.620   37.957  15.432  1.00 23.36 ? 68  ASP A OD2 1 
ATOM   551  N  N   . LYS A 1 69  ? -1.380  37.494  15.340  1.00 20.22 ? 69  LYS A N   1 
ATOM   552  C  CA  . LYS A 1 69  ? -2.041  36.390  16.066  1.00 20.89 ? 69  LYS A CA  1 
ATOM   553  C  C   . LYS A 1 69  ? -1.453  36.273  17.468  1.00 21.31 ? 69  LYS A C   1 
ATOM   554  O  O   . LYS A 1 69  ? -0.218  36.196  17.583  1.00 24.06 ? 69  LYS A O   1 
ATOM   555  C  CB  . LYS A 1 69  ? -1.891  35.034  15.369  1.00 20.40 ? 69  LYS A CB  1 
ATOM   556  C  CG  . LYS A 1 69  ? -2.376  33.884  16.237  1.00 19.23 ? 69  LYS A CG  1 
ATOM   557  C  CD  . LYS A 1 69  ? -2.726  32.667  15.474  1.00 18.83 ? 69  LYS A CD  1 
ATOM   558  C  CE  . LYS A 1 69  ? -3.038  31.536  16.412  1.00 19.08 ? 69  LYS A CE  1 
ATOM   559  N  NZ  . LYS A 1 69  ? -3.490  30.342  15.671  1.00 20.69 ? 69  LYS A NZ  1 
ATOM   560  N  N   . ASN A 1 70  ? -2.335  36.194  18.459  1.00 20.54 ? 70  ASN A N   1 
ATOM   561  C  CA  . ASN A 1 70  ? -2.028  35.918  19.878  1.00 20.55 ? 70  ASN A CA  1 
ATOM   562  C  C   . ASN A 1 70  ? -2.521  34.503  20.197  1.00 22.87 ? 70  ASN A C   1 
ATOM   563  O  O   . ASN A 1 70  ? -3.524  34.047  19.576  1.00 23.98 ? 70  ASN A O   1 
ATOM   564  C  CB  . ASN A 1 70  ? -2.669  36.994  20.759  1.00 21.69 ? 70  ASN A CB  1 
ATOM   565  C  CG  . ASN A 1 70  ? -2.481  36.815  22.253  1.00 20.93 ? 70  ASN A CG  1 
ATOM   566  O  OD1 . ASN A 1 70  ? -1.363  36.832  22.767  1.00 22.56 ? 70  ASN A OD1 1 
ATOM   567  N  ND2 . ASN A 1 70  ? -3.580  36.701  22.967  1.00 19.39 ? 70  ASN A ND2 1 
ATOM   568  N  N   . LEU A 1 71  ? -1.827  33.819  21.112  1.00 22.27 ? 71  LEU A N   1 
ATOM   569  C  CA  . LEU A 1 71  ? -2.292  32.576  21.764  1.00 21.57 ? 71  LEU A CA  1 
ATOM   570  C  C   . LEU A 1 71  ? -3.051  32.960  23.028  1.00 21.18 ? 71  LEU A C   1 
ATOM   571  O  O   . LEU A 1 71  ? -2.416  33.472  23.940  1.00 23.98 ? 71  LEU A O   1 
ATOM   572  C  CB  . LEU A 1 71  ? -1.073  31.729  22.108  1.00 22.91 ? 71  LEU A CB  1 
ATOM   573  C  CG  . LEU A 1 71  ? -0.672  30.709  21.055  1.00 24.74 ? 71  LEU A CG  1 
ATOM   574  C  CD1 . LEU A 1 71  ? -0.685  31.306  19.650  1.00 23.83 ? 71  LEU A CD1 1 
ATOM   575  C  CD2 . LEU A 1 71  ? 0.665   30.088  21.417  1.00 24.06 ? 71  LEU A CD2 1 
ATOM   576  N  N   . SER A 1 72  ? -4.362  32.782  23.050  1.00 19.54 ? 72  SER A N   1 
ATOM   577  C  CA  . SER A 1 72  ? -5.188  32.930  24.267  1.00 21.24 ? 72  SER A CA  1 
ATOM   578  C  C   . SER A 1 72  ? -4.629  31.995  25.346  1.00 20.89 ? 72  SER A C   1 
ATOM   579  O  O   . SER A 1 72  ? -3.787  31.143  25.003  1.00 19.91 ? 72  SER A O   1 
ATOM   580  C  CB  . SER A 1 72  ? -6.650  32.634  23.991  1.00 21.07 ? 72  SER A CB  1 
ATOM   581  O  OG  . SER A 1 72  ? -6.856  31.247  23.771  1.00 21.53 ? 72  SER A OG  1 
ATOM   582  N  N   . GLN A 1 73  ? -5.110  32.123  26.583  1.00 20.48 ? 73  GLN A N   1 
ATOM   583  C  CA  . GLN A 1 73  ? -4.818  31.135  27.659  1.00 21.79 ? 73  GLN A CA  1 
ATOM   584  C  C   . GLN A 1 73  ? -5.081  29.713  27.134  1.00 21.20 ? 73  GLN A C   1 
ATOM   585  O  O   . GLN A 1 73  ? -4.254  28.841  27.340  1.00 19.63 ? 73  GLN A O   1 
ATOM   586  C  CB  . GLN A 1 73  ? -5.688  31.438  28.875  1.00 22.93 ? 73  GLN A CB  1 
ATOM   587  C  CG  . GLN A 1 73  ? -5.327  32.743  29.552  1.00 27.21 ? 73  GLN A CG  1 
ATOM   588  C  CD  . GLN A 1 73  ? -3.938  32.674  30.149  1.00 30.98 ? 73  GLN A CD  1 
ATOM   589  O  OE1 . GLN A 1 73  ? -3.722  31.978  31.141  1.00 37.41 ? 73  GLN A OE1 1 
ATOM   590  N  NE2 . GLN A 1 73  ? -2.982  33.371  29.540  1.00 30.16 ? 73  GLN A NE2 1 
ATOM   591  N  N   . VAL A 1 74  ? -6.204  29.497  26.446  1.00 22.42 ? 74  VAL A N   1 
ATOM   592  C  CA  . VAL A 1 74  ? -6.626  28.157  25.933  1.00 21.77 ? 74  VAL A CA  1 
ATOM   593  C  C   . VAL A 1 74  ? -5.589  27.639  24.928  1.00 20.12 ? 74  VAL A C   1 
ATOM   594  O  O   . VAL A 1 74  ? -5.175  26.483  25.032  1.00 19.70 ? 74  VAL A O   1 
ATOM   595  C  CB  . VAL A 1 74  ? -8.023  28.235  25.299  1.00 23.00 ? 74  VAL A CB  1 
ATOM   596  C  CG1 . VAL A 1 74  ? -8.194  27.222  24.185  1.00 23.32 ? 74  VAL A CG1 1 
ATOM   597  C  CG2 . VAL A 1 74  ? -9.116  28.116  26.348  1.00 23.60 ? 74  VAL A CG2 1 
ATOM   598  N  N   . LEU A 1 75  ? -5.184  28.448  23.970  1.00 20.39 ? 75  LEU A N   1 
ATOM   599  C  CA  . LEU A 1 75  ? -4.225  27.982  22.943  1.00 21.41 ? 75  LEU A CA  1 
ATOM   600  C  C   . LEU A 1 75  ? -2.886  27.704  23.625  1.00 21.13 ? 75  LEU A C   1 
ATOM   601  O  O   . LEU A 1 75  ? -2.229  26.705  23.267  1.00 21.06 ? 75  LEU A O   1 
ATOM   602  C  CB  . LEU A 1 75  ? -4.095  29.017  21.825  1.00 22.73 ? 75  LEU A CB  1 
ATOM   603  C  CG  . LEU A 1 75  ? -4.840  28.668  20.543  1.00 23.56 ? 75  LEU A CG  1 
ATOM   604  C  CD1 . LEU A 1 75  ? -6.267  28.244  20.829  1.00 22.65 ? 75  LEU A CD1 1 
ATOM   605  C  CD2 . LEU A 1 75  ? -4.790  29.809  19.542  1.00 22.36 ? 75  LEU A CD2 1 
ATOM   606  N  N   . LYS A 1 76  ? -2.522  28.525  24.606  1.00 21.26 ? 76  LYS A N   1 
ATOM   607  C  CA  . LYS A 1 76  ? -1.268  28.318  25.366  1.00 22.10 ? 76  LYS A CA  1 
ATOM   608  C  C   . LYS A 1 76  ? -1.324  26.960  26.070  1.00 21.92 ? 76  LYS A C   1 
ATOM   609  O  O   . LYS A 1 76  ? -0.259  26.335  26.155  1.00 22.80 ? 76  LYS A O   1 
ATOM   610  C  CB  . LYS A 1 76  ? -1.004  29.460  26.343  1.00 22.05 ? 76  LYS A CB  1 
ATOM   611  C  CG  . LYS A 1 76  ? -0.673  30.771  25.669  1.00 21.96 ? 76  LYS A CG  1 
ATOM   612  C  CD  . LYS A 1 76  ? -0.503  31.908  26.649  1.00 23.28 ? 76  LYS A CD  1 
ATOM   613  C  CE  . LYS A 1 76  ? 0.270   33.057  26.043  1.00 24.11 ? 76  LYS A CE  1 
ATOM   614  N  NZ  . LYS A 1 76  ? 0.229   34.247  26.928  1.00 26.39 ? 76  LYS A NZ  1 
ATOM   615  N  N   . PHE A 1 77  ? -2.501  26.495  26.512  1.00 21.38 ? 77  PHE A N   1 
ATOM   616  C  CA  . PHE A 1 77  ? -2.647  25.176  27.195  1.00 21.05 ? 77  PHE A CA  1 
ATOM   617  C  C   . PHE A 1 77  ? -2.777  24.065  26.153  1.00 20.97 ? 77  PHE A C   1 
ATOM   618  O  O   . PHE A 1 77  ? -2.333  22.954  26.406  1.00 21.49 ? 77  PHE A O   1 
ATOM   619  C  CB  . PHE A 1 77  ? -3.789  25.187  28.212  1.00 20.11 ? 77  PHE A CB  1 
ATOM   620  C  CG  . PHE A 1 77  ? -3.490  25.983  29.461  1.00 20.26 ? 77  PHE A CG  1 
ATOM   621  C  CD1 . PHE A 1 77  ? -2.310  25.795  30.164  1.00 21.96 ? 77  PHE A CD1 1 
ATOM   622  C  CD2 . PHE A 1 77  ? -4.402  26.902  29.961  1.00 19.95 ? 77  PHE A CD2 1 
ATOM   623  C  CE1 . PHE A 1 77  ? -2.042  26.535  31.310  1.00 22.26 ? 77  PHE A CE1 1 
ATOM   624  C  CE2 . PHE A 1 77  ? -4.132  27.634  31.108  1.00 20.08 ? 77  PHE A CE2 1 
ATOM   625  C  CZ  . PHE A 1 77  ? -2.956  27.448  31.781  1.00 20.47 ? 77  PHE A CZ  1 
ATOM   626  N  N   . VAL A 1 78  ? -3.313  24.378  24.981  1.00 21.78 ? 78  VAL A N   1 
ATOM   627  C  CA  . VAL A 1 78  ? -3.363  23.424  23.837  1.00 21.64 ? 78  VAL A CA  1 
ATOM   628  C  C   . VAL A 1 78  ? -1.932  23.147  23.385  1.00 21.15 ? 78  VAL A C   1 
ATOM   629  O  O   . VAL A 1 78  ? -1.687  22.029  22.950  1.00 22.98 ? 78  VAL A O   1 
ATOM   630  C  CB  . VAL A 1 78  ? -4.201  23.972  22.668  1.00 21.17 ? 78  VAL A CB  1 
ATOM   631  C  CG1 . VAL A 1 78  ? -4.071  23.124  21.416  1.00 21.01 ? 78  VAL A CG1 1 
ATOM   632  C  CG2 . VAL A 1 78  ? -5.662  24.071  23.052  1.00 23.70 ? 78  VAL A CG2 1 
ATOM   633  N  N   . ARG A 1 79  ? -1.067  24.160  23.422  1.00 22.98 ? 79  ARG A N   1 
ATOM   634  C  CA  . ARG A 1 79  ? 0.363   24.099  23.001  1.00 24.66 ? 79  ARG A CA  1 
ATOM   635  C  C   . ARG A 1 79  ? 1.090   22.990  23.773  1.00 24.69 ? 79  ARG A C   1 
ATOM   636  O  O   . ARG A 1 79  ? 2.023   22.433  23.223  1.00 25.98 ? 79  ARG A O   1 
ATOM   637  C  CB  . ARG A 1 79  ? 1.029   25.465  23.200  1.00 23.94 ? 79  ARG A CB  1 
ATOM   638  C  CG  . ARG A 1 79  ? 2.507   25.513  22.837  1.00 25.41 ? 79  ARG A CG  1 
ATOM   639  C  CD  . ARG A 1 79  ? 2.868   26.950  22.523  1.00 27.66 ? 79  ARG A CD  1 
ATOM   640  N  NE  . ARG A 1 79  ? 4.271   27.335  22.550  1.00 28.21 ? 79  ARG A NE  1 
ATOM   641  C  CZ  . ARG A 1 79  ? 4.993   27.660  21.479  1.00 29.24 ? 79  ARG A CZ  1 
ATOM   642  N  NH1 . ARG A 1 79  ? 4.466   27.617  20.267  1.00 29.11 ? 79  ARG A NH1 1 
ATOM   643  N  NH2 . ARG A 1 79  ? 6.251   28.035  21.621  1.00 29.34 ? 79  ARG A NH2 1 
ATOM   644  N  N   . ASP A 1 80  ? 0.663   22.672  24.992  1.00 24.78 ? 80  ASP A N   1 
ATOM   645  C  CA  . ASP A 1 80  ? 1.266   21.578  25.791  1.00 26.59 ? 80  ASP A CA  1 
ATOM   646  C  C   . ASP A 1 80  ? 1.173   20.241  25.040  1.00 29.50 ? 80  ASP A C   1 
ATOM   647  O  O   . ASP A 1 80  ? 1.974   19.341  25.390  1.00 33.12 ? 80  ASP A O   1 
ATOM   648  C  CB  . ASP A 1 80  ? 0.623   21.464  27.177  1.00 28.27 ? 80  ASP A CB  1 
ATOM   649  C  CG  . ASP A 1 80  ? 0.937   22.632  28.095  1.00 27.32 ? 80  ASP A CG  1 
ATOM   650  O  OD1 . ASP A 1 80  ? 1.946   23.337  27.863  1.00 26.15 ? 80  ASP A OD1 1 
ATOM   651  O  OD2 . ASP A 1 80  ? 0.149   22.842  29.009  1.00 31.97 ? 80  ASP A OD2 1 
ATOM   652  N  N   . PHE A 1 81  ? 0.255   20.060  24.077  1.00 26.98 ? 81  PHE A N   1 
ATOM   653  C  CA  . PHE A 1 81  ? 0.269   18.845  23.214  1.00 25.16 ? 81  PHE A CA  1 
ATOM   654  C  C   . PHE A 1 81  ? 0.322   19.146  21.710  1.00 25.28 ? 81  PHE A C   1 
ATOM   655  O  O   . PHE A 1 81  ? 0.702   18.234  20.984  1.00 27.95 ? 81  PHE A O   1 
ATOM   656  C  CB  . PHE A 1 81  ? -0.897  17.918  23.543  1.00 26.05 ? 81  PHE A CB  1 
ATOM   657  C  CG  . PHE A 1 81  ? -2.263  18.549  23.623  1.00 23.58 ? 81  PHE A CG  1 
ATOM   658  C  CD1 . PHE A 1 81  ? -2.726  19.066  24.819  1.00 22.74 ? 81  PHE A CD1 1 
ATOM   659  C  CD2 . PHE A 1 81  ? -3.104  18.564  22.514  1.00 22.95 ? 81  PHE A CD2 1 
ATOM   660  C  CE1 . PHE A 1 81  ? -4.007  19.584  24.905  1.00 22.57 ? 81  PHE A CE1 1 
ATOM   661  C  CE2 . PHE A 1 81  ? -4.378  19.109  22.597  1.00 22.47 ? 81  PHE A CE2 1 
ATOM   662  C  CZ  . PHE A 1 81  ? -4.825  19.615  23.796  1.00 21.91 ? 81  PHE A CZ  1 
ATOM   663  N  N   . ALA A 1 82  ? -0.014  20.352  21.246  1.00 25.46 ? 82  ALA A N   1 
ATOM   664  C  CA  . ALA A 1 82  ? 0.054   20.729  19.812  1.00 25.42 ? 82  ALA A CA  1 
ATOM   665  C  C   . ALA A 1 82  ? 1.373   21.449  19.547  1.00 24.66 ? 82  ALA A C   1 
ATOM   666  O  O   . ALA A 1 82  ? 1.687   21.702  18.368  1.00 25.88 ? 82  ALA A O   1 
ATOM   667  C  CB  . ALA A 1 82  ? -1.150  21.575  19.422  1.00 25.92 ? 82  ALA A CB  1 
ATOM   668  N  N   . GLY A 1 83  ? 2.121   21.761  20.608  1.00 25.64 ? 83  GLY A N   1 
ATOM   669  C  CA  . GLY A 1 83  ? 3.474   22.350  20.546  1.00 23.65 ? 83  GLY A CA  1 
ATOM   670  C  C   . GLY A 1 83  ? 3.522   23.548  19.626  1.00 23.69 ? 83  GLY A C   1 
ATOM   671  O  O   . GLY A 1 83  ? 2.630   24.381  19.691  1.00 25.10 ? 83  GLY A O   1 
ATOM   672  N  N   . ASP A 1 84  ? 4.525   23.613  18.763  1.00 23.44 ? 84  ASP A N   1 
ATOM   673  C  CA  . ASP A 1 84  ? 4.692   24.718  17.789  1.00 21.47 ? 84  ASP A CA  1 
ATOM   674  C  C   . ASP A 1 84  ? 4.162   24.230  16.445  1.00 20.33 ? 84  ASP A C   1 
ATOM   675  O  O   . ASP A 1 84  ? 4.764   24.577  15.440  1.00 21.56 ? 84  ASP A O   1 
ATOM   676  C  CB  . ASP A 1 84  ? 6.153   25.195  17.737  1.00 21.20 ? 84  ASP A CB  1 
ATOM   677  C  CG  . ASP A 1 84  ? 7.213   24.150  17.369  1.00 21.59 ? 84  ASP A CG  1 
ATOM   678  O  OD1 . ASP A 1 84  ? 6.853   22.978  17.062  1.00 24.82 ? 84  ASP A OD1 1 
ATOM   679  O  OD2 . ASP A 1 84  ? 8.409   24.499  17.386  1.00 19.54 ? 84  ASP A OD2 1 
ATOM   680  N  N   . GLY A 1 85  ? 3.060   23.469  16.431  1.00 20.84 ? 85  GLY A N   1 
ATOM   681  C  CA  . GLY A 1 85  ? 2.264   23.196  15.213  1.00 18.44 ? 85  GLY A CA  1 
ATOM   682  C  C   . GLY A 1 85  ? 1.738   24.493  14.613  1.00 18.09 ? 85  GLY A C   1 
ATOM   683  O  O   . GLY A 1 85  ? 1.885   25.551  15.236  1.00 19.93 ? 85  GLY A O   1 
ATOM   684  N  N   . LEU A 1 86  ? 1.156   24.474  13.422  1.00 17.77 ? 86  LEU A N   1 
ATOM   685  C  CA  . LEU A 1 86  ? 0.781   25.745  12.739  1.00 17.33 ? 86  LEU A CA  1 
ATOM   686  C  C   . LEU A 1 86  ? -0.242  26.516  13.574  1.00 19.08 ? 86  LEU A C   1 
ATOM   687  O  O   . LEU A 1 86  ? -0.211  27.758  13.525  1.00 20.54 ? 86  LEU A O   1 
ATOM   688  C  CB  . LEU A 1 86  ? 0.254   25.447  11.341  1.00 16.25 ? 86  LEU A CB  1 
ATOM   689  C  CG  . LEU A 1 86  ? 1.362   25.192  10.338  1.00 15.67 ? 86  LEU A CG  1 
ATOM   690  C  CD1 . LEU A 1 86  ? 0.825   24.492  9.107   1.00 16.24 ? 86  LEU A CD1 1 
ATOM   691  C  CD2 . LEU A 1 86  ? 2.062   26.495  9.969   1.00 15.66 ? 86  LEU A CD2 1 
ATOM   692  N  N   . PHE A 1 87  ? -1.079  25.820  14.346  1.00 19.83 ? 87  PHE A N   1 
ATOM   693  C  CA  . PHE A 1 87  ? -2.230  26.412  15.070  1.00 19.95 ? 87  PHE A CA  1 
ATOM   694  C  C   . PHE A 1 87  ? -1.769  27.077  16.384  1.00 19.39 ? 87  PHE A C   1 
ATOM   695  O  O   . PHE A 1 87  ? -2.331  28.163  16.727  1.00 18.21 ? 87  PHE A O   1 
ATOM   696  C  CB  . PHE A 1 87  ? -3.306  25.340  15.273  1.00 21.07 ? 87  PHE A CB  1 
ATOM   697  C  CG  . PHE A 1 87  ? -4.560  25.799  15.977  1.00 20.51 ? 87  PHE A CG  1 
ATOM   698  C  CD1 . PHE A 1 87  ? -5.318  26.843  15.473  1.00 20.11 ? 87  PHE A CD1 1 
ATOM   699  C  CD2 . PHE A 1 87  ? -4.977  25.179  17.141  1.00 20.47 ? 87  PHE A CD2 1 
ATOM   700  C  CE1 . PHE A 1 87  ? -6.463  27.259  16.128  1.00 20.75 ? 87  PHE A CE1 1 
ATOM   701  C  CE2 . PHE A 1 87  ? -6.135  25.578  17.776  1.00 21.19 ? 87  PHE A CE2 1 
ATOM   702  C  CZ  . PHE A 1 87  ? -6.880  26.615  17.266  1.00 21.27 ? 87  PHE A CZ  1 
ATOM   703  N  N   . THR A 1 88  ? -0.768  26.515  17.078  1.00 18.53 ? 88  THR A N   1 
ATOM   704  C  CA  . THR A 1 88  ? -0.349  26.975  18.438  1.00 17.71 ? 88  THR A CA  1 
ATOM   705  C  C   . THR A 1 88  ? 1.050   27.629  18.411  1.00 16.58 ? 88  THR A C   1 
ATOM   706  O  O   . THR A 1 88  ? 1.609   27.868  19.491  1.00 15.21 ? 88  THR A O   1 
ATOM   707  C  CB  . THR A 1 88  ? -0.490  25.843  19.472  1.00 17.87 ? 88  THR A CB  1 
ATOM   708  O  OG1 . THR A 1 88  ? 0.115   24.627  19.028  1.00 16.50 ? 88  THR A OG1 1 
ATOM   709  C  CG2 . THR A 1 88  ? -1.943  25.535  19.751  1.00 18.49 ? 88  THR A CG2 1 
ATOM   710  N  N   . SER A 1 89  ? 1.573   27.986  17.246  1.00 15.99 ? 89  SER A N   1 
ATOM   711  C  CA  . SER A 1 89  ? 2.887   28.655  17.145  1.00 17.51 ? 89  SER A CA  1 
ATOM   712  C  C   . SER A 1 89  ? 2.671   30.153  16.968  1.00 17.79 ? 89  SER A C   1 
ATOM   713  O  O   . SER A 1 89  ? 1.605   30.556  16.462  1.00 18.07 ? 89  SER A O   1 
ATOM   714  C  CB  . SER A 1 89  ? 3.746   28.063  16.056  1.00 18.90 ? 89  SER A CB  1 
ATOM   715  O  OG  . SER A 1 89  ? 3.074   28.104  14.812  1.00 23.25 ? 89  SER A OG  1 
ATOM   716  N  N   . TRP A 1 90  ? 3.636   30.952  17.417  1.00 17.15 ? 90  TRP A N   1 
ATOM   717  C  CA  . TRP A 1 90  ? 3.611   32.402  17.164  1.00 17.90 ? 90  TRP A CA  1 
ATOM   718  C  C   . TRP A 1 90  ? 4.147   32.609  15.748  1.00 18.06 ? 90  TRP A C   1 
ATOM   719  O  O   . TRP A 1 90  ? 4.891   31.742  15.254  1.00 18.59 ? 90  TRP A O   1 
ATOM   720  C  CB  . TRP A 1 90  ? 4.405   33.180  18.220  1.00 18.64 ? 90  TRP A CB  1 
ATOM   721  C  CG  . TRP A 1 90  ? 3.987   32.919  19.631  1.00 18.62 ? 90  TRP A CG  1 
ATOM   722  C  CD1 . TRP A 1 90  ? 4.380   31.892  20.439  1.00 19.33 ? 90  TRP A CD1 1 
ATOM   723  C  CD2 . TRP A 1 90  ? 3.071   33.705  20.405  1.00 18.71 ? 90  TRP A CD2 1 
ATOM   724  N  NE1 . TRP A 1 90  ? 3.764   31.979  21.666  1.00 19.55 ? 90  TRP A NE1 1 
ATOM   725  C  CE2 . TRP A 1 90  ? 2.962   33.086  21.675  1.00 18.96 ? 90  TRP A CE2 1 
ATOM   726  C  CE3 . TRP A 1 90  ? 2.320   34.852  20.136  1.00 19.75 ? 90  TRP A CE3 1 
ATOM   727  C  CZ2 . TRP A 1 90  ? 2.170   33.603  22.689  1.00 19.62 ? 90  TRP A CZ2 1 
ATOM   728  C  CZ3 . TRP A 1 90  ? 1.521   35.361  21.139  1.00 21.12 ? 90  TRP A CZ3 1 
ATOM   729  C  CH2 . TRP A 1 90  ? 1.456   34.749  22.397  1.00 21.44 ? 90  TRP A CH2 1 
ATOM   730  N  N   . THR A 1 91  ? 3.783   33.726  15.128  1.00 17.95 ? 91  THR A N   1 
ATOM   731  C  CA  . THR A 1 91  ? 4.087   34.020  13.708  1.00 18.02 ? 91  THR A CA  1 
ATOM   732  C  C   . THR A 1 91  ? 5.605   34.152  13.502  1.00 17.90 ? 91  THR A C   1 
ATOM   733  O  O   . THR A 1 91  ? 6.090   33.675  12.466  1.00 19.16 ? 91  THR A O   1 
ATOM   734  C  CB  . THR A 1 91  ? 3.337   35.281  13.292  1.00 17.44 ? 91  THR A CB  1 
ATOM   735  O  OG1 . THR A 1 91  ? 1.954   34.975  13.477  1.00 16.16 ? 91  THR A OG1 1 
ATOM   736  C  CG2 . THR A 1 91  ? 3.682   35.704  11.882  1.00 18.10 ? 91  THR A CG2 1 
ATOM   737  N  N   . HIS A 1 92  ? 6.290   34.796  14.452  1.00 18.50 ? 92  HIS A N   1 
ATOM   738  C  CA  . HIS A 1 92  ? 7.754   35.097  14.484  1.00 18.38 ? 92  HIS A CA  1 
ATOM   739  C  C   . HIS A 1 92  ? 8.573   33.850  14.865  1.00 17.84 ? 92  HIS A C   1 
ATOM   740  O  O   . HIS A 1 92  ? 9.777   33.939  14.757  1.00 16.89 ? 92  HIS A O   1 
ATOM   741  C  CB  . HIS A 1 92  ? 8.032   36.252  15.472  1.00 18.10 ? 92  HIS A CB  1 
ATOM   742  C  CG  . HIS A 1 92  ? 7.431   36.030  16.828  1.00 18.11 ? 92  HIS A CG  1 
ATOM   743  N  ND1 . HIS A 1 92  ? 7.972   35.144  17.738  1.00 18.42 ? 92  HIS A ND1 1 
ATOM   744  C  CD2 . HIS A 1 92  ? 6.311   36.526  17.411  1.00 18.16 ? 92  HIS A CD2 1 
ATOM   745  C  CE1 . HIS A 1 92  ? 7.233   35.142  18.843  1.00 18.99 ? 92  HIS A CE1 1 
ATOM   746  N  NE2 . HIS A 1 92  ? 6.213   35.984  18.674  1.00 18.04 ? 92  HIS A NE2 1 
ATOM   747  N  N   . GLU A 1 93  ? 7.958   32.756  15.343  1.00 18.72 ? 93  GLU A N   1 
ATOM   748  C  CA  . GLU A 1 93  ? 8.674   31.463  15.556  1.00 19.45 ? 93  GLU A CA  1 
ATOM   749  C  C   . GLU A 1 93  ? 9.090   30.893  14.194  1.00 20.85 ? 93  GLU A C   1 
ATOM   750  O  O   . GLU A 1 93  ? 8.234   30.765  13.310  1.00 19.17 ? 93  GLU A O   1 
ATOM   751  C  CB  . GLU A 1 93  ? 7.859   30.401  16.291  1.00 18.06 ? 93  GLU A CB  1 
ATOM   752  C  CG  . GLU A 1 93  ? 7.693   30.697  17.765  1.00 18.11 ? 93  GLU A CG  1 
ATOM   753  C  CD  . GLU A 1 93  ? 6.993   29.607  18.565  1.00 16.73 ? 93  GLU A CD  1 
ATOM   754  O  OE1 . GLU A 1 93  ? 5.753   29.507  18.532  1.00 15.92 ? 93  GLU A OE1 1 
ATOM   755  O  OE2 . GLU A 1 93  ? 7.694   28.891  19.268  1.00 17.56 ? 93  GLU A OE2 1 
ATOM   756  N  N   . LYS A 1 94  ? 10.369  30.541  14.068  1.00 22.48 ? 94  LYS A N   1 
ATOM   757  C  CA  . LYS A 1 94  ? 10.983  29.897  12.879  1.00 23.26 ? 94  LYS A CA  1 
ATOM   758  C  C   . LYS A 1 94  ? 10.083  28.766  12.392  1.00 21.45 ? 94  LYS A C   1 
ATOM   759  O  O   . LYS A 1 94  ? 9.910   28.672  11.194  1.00 23.57 ? 94  LYS A O   1 
ATOM   760  C  CB  . LYS A 1 94  ? 12.376  29.365  13.217  1.00 24.78 ? 94  LYS A CB  1 
ATOM   761  C  CG  . LYS A 1 94  ? 13.062  28.557  12.129  1.00 28.04 ? 94  LYS A CG  1 
ATOM   762  C  CD  . LYS A 1 94  ? 14.282  27.847  12.663  1.00 30.67 ? 94  LYS A CD  1 
ATOM   763  C  CE  . LYS A 1 94  ? 15.370  27.722  11.626  1.00 34.63 ? 94  LYS A CE  1 
ATOM   764  N  NZ  . LYS A 1 94  ? 16.524  26.938  12.144  1.00 35.65 ? 94  LYS A NZ  1 
ATOM   765  N  N   . ASN A 1 95  ? 9.537   27.949  13.279  1.00 20.73 ? 95  ASN A N   1 
ATOM   766  C  CA  . ASN A 1 95  ? 8.793   26.726  12.887  1.00 22.31 ? 95  ASN A CA  1 
ATOM   767  C  C   . ASN A 1 95  ? 7.416   27.064  12.296  1.00 23.09 ? 95  ASN A C   1 
ATOM   768  O  O   . ASN A 1 95  ? 6.839   26.189  11.598  1.00 22.65 ? 95  ASN A O   1 
ATOM   769  C  CB  . ASN A 1 95  ? 8.673   25.755  14.061  1.00 24.09 ? 95  ASN A CB  1 
ATOM   770  C  CG  . ASN A 1 95  ? 9.796   24.746  14.074  1.00 25.14 ? 95  ASN A CG  1 
ATOM   771  O  OD1 . ASN A 1 95  ? 10.407  24.492  13.041  1.00 30.80 ? 95  ASN A OD1 1 
ATOM   772  N  ND2 . ASN A 1 95  ? 10.061  24.162  15.229  1.00 24.78 ? 95  ASN A ND2 1 
ATOM   773  N  N   . TRP A 1 96  ? 6.845   28.238  12.579  1.00 23.68 ? 96  TRP A N   1 
ATOM   774  C  CA  . TRP A 1 96  ? 5.574   28.627  11.921  1.00 22.46 ? 96  TRP A CA  1 
ATOM   775  C  C   . TRP A 1 96  ? 5.842   28.778  10.405  1.00 22.24 ? 96  TRP A C   1 
ATOM   776  O  O   . TRP A 1 96  ? 5.202   28.075  9.580   1.00 19.01 ? 96  TRP A O   1 
ATOM   777  C  CB  . TRP A 1 96  ? 4.940   29.881  12.534  1.00 21.53 ? 96  TRP A CB  1 
ATOM   778  C  CG  . TRP A 1 96  ? 3.703   30.178  11.753  1.00 22.14 ? 96  TRP A CG  1 
ATOM   779  C  CD1 . TRP A 1 96  ? 2.525   29.494  11.817  1.00 22.32 ? 96  TRP A CD1 1 
ATOM   780  C  CD2 . TRP A 1 96  ? 3.584   31.083  10.642  1.00 21.92 ? 96  TRP A CD2 1 
ATOM   781  N  NE1 . TRP A 1 96  ? 1.670   29.942  10.845  1.00 23.17 ? 96  TRP A NE1 1 
ATOM   782  C  CE2 . TRP A 1 96  ? 2.285   30.924  10.119  1.00 21.75 ? 96  TRP A CE2 1 
ATOM   783  C  CE3 . TRP A 1 96  ? 4.436   32.024  10.051  1.00 21.66 ? 96  TRP A CE3 1 
ATOM   784  C  CZ2 . TRP A 1 96  ? 1.822   31.671  9.040   1.00 22.58 ? 96  TRP A CZ2 1 
ATOM   785  C  CZ3 . TRP A 1 96  ? 3.976   32.764  8.983   1.00 21.42 ? 96  TRP A CZ3 1 
ATOM   786  C  CH2 . TRP A 1 96  ? 2.688   32.591  8.487   1.00 21.81 ? 96  TRP A CH2 1 
ATOM   787  N  N   . LYS A 1 97  ? 6.800   29.620  10.053  1.00 22.53 ? 97  LYS A N   1 
ATOM   788  C  CA  . LYS A 1 97  ? 7.074   30.014  8.650   1.00 27.81 ? 97  LYS A CA  1 
ATOM   789  C  C   . LYS A 1 97  ? 7.547   28.780  7.851   1.00 26.12 ? 97  LYS A C   1 
ATOM   790  O  O   . LYS A 1 97  ? 7.179   28.646  6.662   1.00 24.12 ? 97  LYS A O   1 
ATOM   791  C  CB  . LYS A 1 97  ? 8.089   31.168  8.663   1.00 32.59 ? 97  LYS A CB  1 
ATOM   792  C  CG  . LYS A 1 97  ? 8.471   31.719  7.298   1.00 36.96 ? 97  LYS A CG  1 
ATOM   793  C  CD  . LYS A 1 97  ? 7.285   32.193  6.473   1.00 41.31 ? 97  LYS A CD  1 
ATOM   794  C  CE  . LYS A 1 97  ? 6.899   33.634  6.728   1.00 45.49 ? 97  LYS A CE  1 
ATOM   795  N  NZ  . LYS A 1 97  ? 6.211   34.201  5.544   1.00 47.29 ? 97  LYS A NZ  1 
ATOM   796  N  N   . LYS A 1 98  ? 8.322   27.903  8.486   1.00 23.14 ? 98  LYS A N   1 
ATOM   797  C  CA  . LYS A 1 98  ? 8.837   26.662  7.869   1.00 22.89 ? 98  LYS A CA  1 
ATOM   798  C  C   . LYS A 1 98  ? 7.672   25.772  7.456   1.00 21.58 ? 98  LYS A C   1 
ATOM   799  O  O   . LYS A 1 98  ? 7.643   25.345  6.298   1.00 23.13 ? 98  LYS A O   1 
ATOM   800  C  CB  . LYS A 1 98  ? 9.707   25.878  8.847   1.00 22.83 ? 98  LYS A CB  1 
ATOM   801  C  CG  . LYS A 1 98  ? 11.190  26.172  8.744   1.00 24.34 ? 98  LYS A CG  1 
ATOM   802  C  CD  . LYS A 1 98  ? 11.967  25.473  9.825   1.00 24.52 ? 98  LYS A CD  1 
ATOM   803  C  CE  . LYS A 1 98  ? 12.087  23.989  9.567   1.00 23.73 ? 98  LYS A CE  1 
ATOM   804  N  NZ  . LYS A 1 98  ? 13.129  23.410  10.426  1.00 22.64 ? 98  LYS A NZ  1 
ATOM   805  N  N   . ALA A 1 99  ? 6.825   25.429  8.417   1.00 21.10 ? 99  ALA A N   1 
ATOM   806  C  CA  . ALA A 1 99  ? 5.678   24.512  8.238   1.00 22.63 ? 99  ALA A CA  1 
ATOM   807  C  C   . ALA A 1 99  ? 4.695   25.158  7.263   1.00 21.66 ? 99  ALA A C   1 
ATOM   808  O  O   . ALA A 1 99  ? 4.274   24.472  6.306   1.00 24.83 ? 99  ALA A O   1 
ATOM   809  C  CB  . ALA A 1 99  ? 5.036   24.180  9.570   1.00 22.08 ? 99  ALA A CB  1 
ATOM   810  N  N   . HIS A 1 100 ? 4.419   26.448  7.452   1.00 22.01 ? 100 HIS A N   1 
ATOM   811  C  CA  . HIS A 1 100 ? 3.535   27.259  6.576   1.00 21.29 ? 100 HIS A CA  1 
ATOM   812  C  C   . HIS A 1 100 ? 3.962   27.088  5.112   1.00 20.89 ? 100 HIS A C   1 
ATOM   813  O  O   . HIS A 1 100 ? 3.113   26.673  4.289   1.00 17.99 ? 100 HIS A O   1 
ATOM   814  C  CB  . HIS A 1 100 ? 3.532   28.719  7.035   1.00 23.89 ? 100 HIS A CB  1 
ATOM   815  C  CG  . HIS A 1 100 ? 2.780   29.628  6.123   1.00 26.43 ? 100 HIS A CG  1 
ATOM   816  N  ND1 . HIS A 1 100 ? 3.425   30.463  5.219   1.00 28.00 ? 100 HIS A ND1 1 
ATOM   817  C  CD2 . HIS A 1 100 ? 1.451   29.818  5.951   1.00 27.75 ? 100 HIS A CD2 1 
ATOM   818  C  CE1 . HIS A 1 100 ? 2.520   31.152  4.543   1.00 29.43 ? 100 HIS A CE1 1 
ATOM   819  N  NE2 . HIS A 1 100 ? 1.303   30.763  4.963   1.00 29.46 ? 100 HIS A NE2 1 
ATOM   820  N  N   . ASN A 1 101 ? 5.240   27.347  4.793   1.00 19.79 ? 101 ASN A N   1 
ATOM   821  C  CA  . ASN A 1 101 ? 5.725   27.314  3.388   1.00 19.95 ? 101 ASN A CA  1 
ATOM   822  C  C   . ASN A 1 101 ? 5.743   25.885  2.843   1.00 20.95 ? 101 ASN A C   1 
ATOM   823  O  O   . ASN A 1 101 ? 5.549   25.716  1.610   1.00 20.22 ? 101 ASN A O   1 
ATOM   824  C  CB  . ASN A 1 101 ? 7.132   27.861  3.237   1.00 19.31 ? 101 ASN A CB  1 
ATOM   825  C  CG  . ASN A 1 101 ? 7.220   29.312  3.607   1.00 19.64 ? 101 ASN A CG  1 
ATOM   826  O  OD1 . ASN A 1 101 ? 6.245   30.062  3.476   1.00 20.75 ? 101 ASN A OD1 1 
ATOM   827  N  ND2 . ASN A 1 101 ? 8.393   29.691  4.077   1.00 19.24 ? 101 ASN A ND2 1 
ATOM   828  N  N   . ILE A 1 102 ? 6.043   24.912  3.701   1.00 20.41 ? 102 ILE A N   1 
ATOM   829  C  CA  . ILE A 1 102 ? 6.186   23.501  3.259   1.00 21.61 ? 102 ILE A CA  1 
ATOM   830  C  C   . ILE A 1 102 ? 4.789   22.935  2.989   1.00 20.09 ? 102 ILE A C   1 
ATOM   831  O  O   . ILE A 1 102 ? 4.640   22.242  2.008   1.00 18.23 ? 102 ILE A O   1 
ATOM   832  C  CB  . ILE A 1 102 ? 6.983   22.676  4.289   1.00 23.23 ? 102 ILE A CB  1 
ATOM   833  C  CG1 . ILE A 1 102 ? 8.477   22.995  4.198   1.00 22.83 ? 102 ILE A CG1 1 
ATOM   834  C  CG2 . ILE A 1 102 ? 6.713   21.174  4.113   1.00 23.77 ? 102 ILE A CG2 1 
ATOM   835  C  CD1 . ILE A 1 102 ? 9.336   22.236  5.202   1.00 22.60 ? 102 ILE A CD1 1 
ATOM   836  N  N   . LEU A 1 103 ? 3.808   23.255  3.835   1.00 21.18 ? 103 LEU A N   1 
ATOM   837  C  CA  . LEU A 1 103 ? 2.466   22.610  3.838   1.00 21.30 ? 103 LEU A CA  1 
ATOM   838  C  C   . LEU A 1 103 ? 1.466   23.333  2.914   1.00 20.04 ? 103 LEU A C   1 
ATOM   839  O  O   . LEU A 1 103 ? 0.492   22.689  2.483   1.00 19.97 ? 103 LEU A O   1 
ATOM   840  C  CB  . LEU A 1 103 ? 1.984   22.578  5.288   1.00 20.89 ? 103 LEU A CB  1 
ATOM   841  C  CG  . LEU A 1 103 ? 2.488   21.359  6.053   1.00 22.97 ? 103 LEU A CG  1 
ATOM   842  C  CD1 . LEU A 1 103 ? 2.211   21.448  7.554   1.00 21.79 ? 103 LEU A CD1 1 
ATOM   843  C  CD2 . LEU A 1 103 ? 1.869   20.096  5.462   1.00 23.93 ? 103 LEU A CD2 1 
ATOM   844  N  N   . LEU A 1 104 ? 1.681   24.609  2.613   1.00 20.52 ? 104 LEU A N   1 
ATOM   845  C  CA  . LEU A 1 104 ? 0.718   25.450  1.845   1.00 24.66 ? 104 LEU A CA  1 
ATOM   846  C  C   . LEU A 1 104 ? 0.326   24.786  0.516   1.00 25.42 ? 104 LEU A C   1 
ATOM   847  O  O   . LEU A 1 104 ? -0.860  24.794  0.194   1.00 26.00 ? 104 LEU A O   1 
ATOM   848  C  CB  . LEU A 1 104 ? 1.340   26.835  1.627   1.00 26.43 ? 104 LEU A CB  1 
ATOM   849  C  CG  . LEU A 1 104 ? 0.390   28.007  1.425   1.00 28.63 ? 104 LEU A CG  1 
ATOM   850  C  CD1 . LEU A 1 104 ? -0.546  28.150  2.604   1.00 28.87 ? 104 LEU A CD1 1 
ATOM   851  C  CD2 . LEU A 1 104 ? 1.182   29.294  1.228   1.00 29.43 ? 104 LEU A CD2 1 
ATOM   852  N  N   . PRO A 1 105 ? 1.257   24.235  -0.319  1.00 25.39 ? 105 PRO A N   1 
ATOM   853  C  CA  . PRO A 1 105 ? 0.869   23.519  -1.545  1.00 26.41 ? 105 PRO A CA  1 
ATOM   854  C  C   . PRO A 1 105 ? 0.107   22.188  -1.312  1.00 28.51 ? 105 PRO A C   1 
ATOM   855  O  O   . PRO A 1 105 ? -0.678  21.755  -2.184  1.00 26.96 ? 105 PRO A O   1 
ATOM   856  C  CB  . PRO A 1 105 ? 2.179   23.247  -2.308  1.00 26.49 ? 105 PRO A CB  1 
ATOM   857  C  CG  . PRO A 1 105 ? 3.308   23.616  -1.375  1.00 26.85 ? 105 PRO A CG  1 
ATOM   858  C  CD  . PRO A 1 105 ? 2.716   24.351  -0.188  1.00 25.62 ? 105 PRO A CD  1 
ATOM   859  N  N   . SER A 1 106 ? 0.300   21.578  -0.138  1.00 25.27 ? 106 SER A N   1 
ATOM   860  C  CA  . SER A 1 106 ? -0.493  20.428  0.356   1.00 25.28 ? 106 SER A CA  1 
ATOM   861  C  C   . SER A 1 106 ? -1.960  20.802  0.594   1.00 23.13 ? 106 SER A C   1 
ATOM   862  O  O   . SER A 1 106 ? -2.751  19.907  0.557   1.00 21.92 ? 106 SER A O   1 
ATOM   863  C  CB  . SER A 1 106 ? 0.116   19.849  1.612   1.00 26.71 ? 106 SER A CB  1 
ATOM   864  O  OG  . SER A 1 106 ? 1.411   19.339  1.339   1.00 27.28 ? 106 SER A OG  1 
ATOM   865  N  N   . PHE A 1 107 ? -2.295  22.070  0.838   1.00 23.84 ? 107 PHE A N   1 
ATOM   866  C  CA  . PHE A 1 107 ? -3.659  22.533  1.242   1.00 23.89 ? 107 PHE A CA  1 
ATOM   867  C  C   . PHE A 1 107 ? -4.319  23.430  0.176   1.00 21.75 ? 107 PHE A C   1 
ATOM   868  O  O   . PHE A 1 107 ? -5.454  23.918  0.432   1.00 19.87 ? 107 PHE A O   1 
ATOM   869  C  CB  . PHE A 1 107 ? -3.586  23.259  2.586   1.00 22.01 ? 107 PHE A CB  1 
ATOM   870  C  CG  . PHE A 1 107 ? -3.535  22.341  3.774   1.00 21.84 ? 107 PHE A CG  1 
ATOM   871  C  CD1 . PHE A 1 107 ? -4.642  21.607  4.143   1.00 23.31 ? 107 PHE A CD1 1 
ATOM   872  C  CD2 . PHE A 1 107 ? -2.391  22.221  4.538   1.00 24.07 ? 107 PHE A CD2 1 
ATOM   873  C  CE1 . PHE A 1 107 ? -4.610  20.758  5.237   1.00 23.19 ? 107 PHE A CE1 1 
ATOM   874  C  CE2 . PHE A 1 107 ? -2.358  21.387  5.648   1.00 24.16 ? 107 PHE A CE2 1 
ATOM   875  C  CZ  . PHE A 1 107 ? -3.465  20.646  5.985   1.00 24.61 ? 107 PHE A CZ  1 
ATOM   876  N  N   . SER A 1 108 ? -3.670  23.603  -0.978  1.00 20.51 ? 108 SER A N   1 
ATOM   877  C  CA  . SER A 1 108 ? -4.198  24.378  -2.133  1.00 21.48 ? 108 SER A CA  1 
ATOM   878  C  C   . SER A 1 108 ? -5.441  23.693  -2.715  1.00 23.44 ? 108 SER A C   1 
ATOM   879  O  O   . SER A 1 108 ? -5.635  22.461  -2.486  1.00 22.42 ? 108 SER A O   1 
ATOM   880  C  CB  . SER A 1 108 ? -3.144  24.586  -3.204  1.00 19.86 ? 108 SER A CB  1 
ATOM   881  O  OG  . SER A 1 108 ? -2.748  23.351  -3.794  1.00 19.64 ? 108 SER A OG  1 
ATOM   882  N  N   . GLN A 1 109 ? -6.245  24.466  -3.453  1.00 26.64 ? 109 GLN A N   1 
ATOM   883  C  CA  . GLN A 1 109 ? -7.407  23.951  -4.230  1.00 30.03 ? 109 GLN A CA  1 
ATOM   884  C  C   . GLN A 1 109 ? -6.918  22.830  -5.158  1.00 30.86 ? 109 GLN A C   1 
ATOM   885  O  O   . GLN A 1 109 ? -7.523  21.763  -5.120  1.00 37.44 ? 109 GLN A O   1 
ATOM   886  C  CB  . GLN A 1 109 ? -8.120  25.084  -4.977  1.00 29.93 ? 109 GLN A CB  1 
ATOM   887  C  CG  . GLN A 1 109 ? -9.394  24.650  -5.689  1.00 30.98 ? 109 GLN A CG  1 
ATOM   888  C  CD  . GLN A 1 109 ? -10.314 23.847  -4.800  1.00 31.75 ? 109 GLN A CD  1 
ATOM   889  O  OE1 . GLN A 1 109 ? -10.852 22.800  -5.188  1.00 30.96 ? 109 GLN A OE1 1 
ATOM   890  N  NE2 . GLN A 1 109 ? -10.489 24.329  -3.580  1.00 30.83 ? 109 GLN A NE2 1 
ATOM   891  N  N   . GLN A 1 110 ? -5.807  23.005  -5.876  1.00 32.37 ? 110 GLN A N   1 
ATOM   892  C  CA  . GLN A 1 110 ? -5.263  21.954  -6.798  1.00 35.19 ? 110 GLN A CA  1 
ATOM   893  C  C   . GLN A 1 110 ? -5.103  20.620  -6.044  1.00 31.66 ? 110 GLN A C   1 
ATOM   894  O  O   . GLN A 1 110 ? -5.414  19.589  -6.640  1.00 28.10 ? 110 GLN A O   1 
ATOM   895  C  CB  . GLN A 1 110 ? -3.944  22.398  -7.448  1.00 39.29 ? 110 GLN A CB  1 
ATOM   896  C  CG  . GLN A 1 110 ? -3.193  21.311  -8.226  1.00 44.89 ? 110 GLN A CG  1 
ATOM   897  C  CD  . GLN A 1 110 ? -3.844  20.887  -9.530  1.00 51.24 ? 110 GLN A CD  1 
ATOM   898  O  OE1 . GLN A 1 110 ? -4.830  21.467  -9.992  1.00 51.52 ? 110 GLN A OE1 1 
ATOM   899  N  NE2 . GLN A 1 110 ? -3.294  19.851  -10.145 1.00 49.10 ? 110 GLN A NE2 1 
ATOM   900  N  N   . ALA A 1 111 ? -4.626  20.646  -4.791  1.00 29.40 ? 111 ALA A N   1 
ATOM   901  C  CA  . ALA A 1 111 ? -4.247  19.449  -3.990  1.00 29.03 ? 111 ALA A CA  1 
ATOM   902  C  C   . ALA A 1 111 ? -5.506  18.669  -3.632  1.00 26.42 ? 111 ALA A C   1 
ATOM   903  O  O   . ALA A 1 111 ? -5.393  17.452  -3.367  1.00 27.33 ? 111 ALA A O   1 
ATOM   904  C  CB  . ALA A 1 111 ? -3.494  19.828  -2.726  1.00 28.41 ? 111 ALA A CB  1 
ATOM   905  N  N   . MET A 1 112 ? -6.644  19.359  -3.605  1.00 22.86 ? 112 MET A N   1 
ATOM   906  C  CA  . MET A 1 112 ? -7.929  18.742  -3.238  1.00 23.39 ? 112 MET A CA  1 
ATOM   907  C  C   . MET A 1 112 ? -8.305  17.640  -4.240  1.00 22.74 ? 112 MET A C   1 
ATOM   908  O  O   . MET A 1 112 ? -9.003  16.704  -3.847  1.00 23.82 ? 112 MET A O   1 
ATOM   909  C  CB  . MET A 1 112 ? -8.998  19.829  -3.149  1.00 24.02 ? 112 MET A CB  1 
ATOM   910  C  CG  . MET A 1 112 ? -8.736  20.814  -2.018  1.00 25.11 ? 112 MET A CG  1 
ATOM   911  S  SD  . MET A 1 112 ? -8.527  20.021  -0.386  1.00 24.18 ? 112 MET A SD  1 
ATOM   912  C  CE  . MET A 1 112 ? -6.776  20.238  -0.080  1.00 25.26 ? 112 MET A CE  1 
ATOM   913  N  N   . LYS A 1 113 ? -7.827  17.740  -5.481  1.00 24.09 ? 113 LYS A N   1 
ATOM   914  C  CA  . LYS A 1 113 ? -7.994  16.737  -6.569  1.00 23.86 ? 113 LYS A CA  1 
ATOM   915  C  C   . LYS A 1 113 ? -7.425  15.382  -6.133  1.00 25.83 ? 113 LYS A C   1 
ATOM   916  O  O   . LYS A 1 113 ? -8.037  14.326  -6.485  1.00 25.62 ? 113 LYS A O   1 
ATOM   917  C  CB  . LYS A 1 113 ? -7.276  17.218  -7.830  1.00 23.69 ? 113 LYS A CB  1 
ATOM   918  C  CG  . LYS A 1 113 ? -7.905  18.448  -8.456  1.00 24.89 ? 113 LYS A CG  1 
ATOM   919  C  CD  . LYS A 1 113 ? -7.199  18.948  -9.686  1.00 26.07 ? 113 LYS A CD  1 
ATOM   920  C  CE  . LYS A 1 113 ? -7.996  20.065  -10.328 1.00 28.60 ? 113 LYS A CE  1 
ATOM   921  N  NZ  . LYS A 1 113 ? -7.248  20.769  -11.389 1.00 29.55 ? 113 LYS A NZ  1 
ATOM   922  N  N   . GLY A 1 114 ? -6.309  15.414  -5.396  1.00 24.04 ? 114 GLY A N   1 
ATOM   923  C  CA  . GLY A 1 114 ? -5.701  14.244  -4.741  1.00 24.45 ? 114 GLY A CA  1 
ATOM   924  C  C   . GLY A 1 114 ? -6.514  13.725  -3.563  1.00 24.89 ? 114 GLY A C   1 
ATOM   925  O  O   . GLY A 1 114 ? -6.702  12.504  -3.465  1.00 28.00 ? 114 GLY A O   1 
ATOM   926  N  N   . TYR A 1 115 ? -6.992  14.582  -2.669  1.00 24.47 ? 115 TYR A N   1 
ATOM   927  C  CA  . TYR A 1 115 ? -7.650  14.098  -1.424  1.00 23.64 ? 115 TYR A CA  1 
ATOM   928  C  C   . TYR A 1 115 ? -9.047  13.598  -1.757  1.00 22.41 ? 115 TYR A C   1 
ATOM   929  O  O   . TYR A 1 115 ? -9.567  12.781  -0.958  1.00 18.92 ? 115 TYR A O   1 
ATOM   930  C  CB  . TYR A 1 115 ? -7.689  15.175  -0.344  1.00 24.40 ? 115 TYR A CB  1 
ATOM   931  C  CG  . TYR A 1 115 ? -6.322  15.669  0.051   1.00 24.54 ? 115 TYR A CG  1 
ATOM   932  C  CD1 . TYR A 1 115 ? -5.362  14.820  0.588   1.00 26.86 ? 115 TYR A CD1 1 
ATOM   933  C  CD2 . TYR A 1 115 ? -5.975  16.987  -0.145  1.00 24.85 ? 115 TYR A CD2 1 
ATOM   934  C  CE1 . TYR A 1 115 ? -4.111  15.292  0.959   1.00 27.77 ? 115 TYR A CE1 1 
ATOM   935  C  CE2 . TYR A 1 115 ? -4.734  17.471  0.209   1.00 24.95 ? 115 TYR A CE2 1 
ATOM   936  C  CZ  . TYR A 1 115 ? -3.798  16.630  0.770   1.00 26.73 ? 115 TYR A CZ  1 
ATOM   937  O  OH  . TYR A 1 115 ? -2.587  17.154  1.121   1.00 27.62 ? 115 TYR A OH  1 
ATOM   938  N  N   . HIS A 1 116 ? -9.584  14.033  -2.910  1.00 21.39 ? 116 HIS A N   1 
ATOM   939  C  CA  . HIS A 1 116 ? -10.980 13.743  -3.339  1.00 23.95 ? 116 HIS A CA  1 
ATOM   940  C  C   . HIS A 1 116 ? -11.344 12.260  -3.125  1.00 25.25 ? 116 HIS A C   1 
ATOM   941  O  O   . HIS A 1 116 ? -12.245 11.999  -2.293  1.00 26.71 ? 116 HIS A O   1 
ATOM   942  C  CB  . HIS A 1 116 ? -11.232 14.167  -4.789  1.00 22.79 ? 116 HIS A CB  1 
ATOM   943  C  CG  . HIS A 1 116 ? -12.664 14.022  -5.158  1.00 21.89 ? 116 HIS A CG  1 
ATOM   944  N  ND1 . HIS A 1 116 ? -13.631 14.899  -4.682  1.00 20.90 ? 116 HIS A ND1 1 
ATOM   945  C  CD2 . HIS A 1 116 ? -13.302 13.082  -5.898  1.00 21.31 ? 116 HIS A CD2 1 
ATOM   946  C  CE1 . HIS A 1 116 ? -14.808 14.506  -5.119  1.00 21.75 ? 116 HIS A CE1 1 
ATOM   947  N  NE2 . HIS A 1 116 ? -14.634 13.386  -5.870  1.00 21.03 ? 116 HIS A NE2 1 
ATOM   948  N  N   . ALA A 1 117 ? -10.668 11.328  -3.813  1.00 23.26 ? 117 ALA A N   1 
ATOM   949  C  CA  . ALA A 1 117 ? -10.952 9.873   -3.739  1.00 23.86 ? 117 ALA A CA  1 
ATOM   950  C  C   . ALA A 1 117 ? -11.034 9.379   -2.280  1.00 23.80 ? 117 ALA A C   1 
ATOM   951  O  O   . ALA A 1 117 ? -11.846 8.477   -1.963  1.00 23.95 ? 117 ALA A O   1 
ATOM   952  C  CB  . ALA A 1 117 ? -9.915  9.107   -4.512  1.00 23.29 ? 117 ALA A CB  1 
ATOM   953  N  N   . MET A 1 118 ? -10.247 9.939   -1.379  1.00 24.83 ? 118 MET A N   1 
ATOM   954  C  CA  . MET A 1 118 ? -10.233 9.441   0.019   1.00 26.42 ? 118 MET A CA  1 
ATOM   955  C  C   . MET A 1 118 ? -11.391 10.052  0.808   1.00 23.79 ? 118 MET A C   1 
ATOM   956  O  O   . MET A 1 118 ? -11.917 9.350   1.699   1.00 22.03 ? 118 MET A O   1 
ATOM   957  C  CB  . MET A 1 118 ? -8.898  9.746   0.700   1.00 29.15 ? 118 MET A CB  1 
ATOM   958  C  CG  . MET A 1 118 ? -7.835  8.819   0.215   1.00 31.65 ? 118 MET A CG  1 
ATOM   959  S  SD  . MET A 1 118 ? -6.264  9.397   0.755   1.00 40.53 ? 118 MET A SD  1 
ATOM   960  C  CE  . MET A 1 118 ? -6.215  11.047  0.055   1.00 38.18 ? 118 MET A CE  1 
ATOM   961  N  N   . MET A 1 119 ? -11.752 11.300  0.498   1.00 21.97 ? 119 MET A N   1 
ATOM   962  C  CA  . MET A 1 119 ? -12.924 11.976  1.101   1.00 22.81 ? 119 MET A CA  1 
ATOM   963  C  C   . MET A 1 119 ? -14.198 11.199  0.724   1.00 23.77 ? 119 MET A C   1 
ATOM   964  O  O   . MET A 1 119 ? -15.043 10.947  1.658   1.00 21.41 ? 119 MET A O   1 
ATOM   965  C  CB  . MET A 1 119 ? -13.019 13.422  0.627   1.00 22.13 ? 119 MET A CB  1 
ATOM   966  C  CG  . MET A 1 119 ? -11.907 14.283  1.158   1.00 21.95 ? 119 MET A CG  1 
ATOM   967  S  SD  . MET A 1 119 ? -12.257 16.023  0.831   1.00 22.37 ? 119 MET A SD  1 
ATOM   968  C  CE  . MET A 1 119 ? -10.866 16.739  1.688   1.00 24.01 ? 119 MET A CE  1 
ATOM   969  N  N   . VAL A 1 120 ? -14.291 10.804  -0.559  1.00 21.32 ? 120 VAL A N   1 
ATOM   970  C  CA  . VAL A 1 120 ? -15.418 10.023  -1.148  1.00 21.35 ? 120 VAL A CA  1 
ATOM   971  C  C   . VAL A 1 120 ? -15.530 8.670   -0.435  1.00 22.25 ? 120 VAL A C   1 
ATOM   972  O  O   . VAL A 1 120 ? -16.668 8.227   -0.214  1.00 21.98 ? 120 VAL A O   1 
ATOM   973  C  CB  . VAL A 1 120 ? -15.231 9.839   -2.664  1.00 21.74 ? 120 VAL A CB  1 
ATOM   974  C  CG1 . VAL A 1 120 ? -16.234 8.867   -3.255  1.00 22.14 ? 120 VAL A CG1 1 
ATOM   975  C  CG2 . VAL A 1 120 ? -15.307 11.163  -3.410  1.00 22.13 ? 120 VAL A CG2 1 
ATOM   976  N  N   . ASP A 1 121 ? -14.404 8.014   -0.134  1.00 21.96 ? 121 ASP A N   1 
ATOM   977  C  CA  . ASP A 1 121 ? -14.376 6.711   0.579   1.00 21.50 ? 121 ASP A CA  1 
ATOM   978  C  C   . ASP A 1 121 ? -15.182 6.846   1.873   1.00 19.30 ? 121 ASP A C   1 
ATOM   979  O  O   . ASP A 1 121 ? -16.112 6.055   2.060   1.00 18.48 ? 121 ASP A O   1 
ATOM   980  C  CB  . ASP A 1 121 ? -12.939 6.271   0.874   1.00 23.80 ? 121 ASP A CB  1 
ATOM   981  C  CG  . ASP A 1 121 ? -12.824 4.974   1.666   1.00 24.32 ? 121 ASP A CG  1 
ATOM   982  O  OD1 . ASP A 1 121 ? -13.366 4.908   2.807   1.00 23.43 ? 121 ASP A OD1 1 
ATOM   983  O  OD2 . ASP A 1 121 ? -12.196 4.034   1.142   1.00 23.86 ? 121 ASP A OD2 1 
ATOM   984  N  N   . ILE A 1 122 ? -14.871 7.848   2.702   1.00 18.78 ? 122 ILE A N   1 
ATOM   985  C  CA  . ILE A 1 122 ? -15.553 8.069   4.021   1.00 18.81 ? 122 ILE A CA  1 
ATOM   986  C  C   . ILE A 1 122 ? -16.998 8.571   3.810   1.00 19.51 ? 122 ILE A C   1 
ATOM   987  O  O   . ILE A 1 122 ? -17.895 8.162   4.587   1.00 20.24 ? 122 ILE A O   1 
ATOM   988  C  CB  . ILE A 1 122 ? -14.769 9.027   4.940   1.00 19.00 ? 122 ILE A CB  1 
ATOM   989  C  CG1 . ILE A 1 122 ? -13.263 8.733   5.005   1.00 18.01 ? 122 ILE A CG1 1 
ATOM   990  C  CG2 . ILE A 1 122 ? -15.406 9.016   6.321   1.00 18.96 ? 122 ILE A CG2 1 
ATOM   991  C  CD1 . ILE A 1 122 ? -12.899 7.425   5.662   1.00 18.02 ? 122 ILE A CD1 1 
ATOM   992  N  N   . ALA A 1 123 ? -17.234 9.449   2.831   1.00 18.95 ? 123 ALA A N   1 
ATOM   993  C  CA  . ALA A 1 123 ? -18.581 9.938   2.475   1.00 20.25 ? 123 ALA A CA  1 
ATOM   994  C  C   . ALA A 1 123 ? -19.497 8.740   2.208   1.00 20.01 ? 123 ALA A C   1 
ATOM   995  O  O   . ALA A 1 123 ? -20.557 8.660   2.839   1.00 20.92 ? 123 ALA A O   1 
ATOM   996  C  CB  . ALA A 1 123 ? -18.509 10.850  1.269   1.00 21.83 ? 123 ALA A CB  1 
ATOM   997  N  N   . VAL A 1 124 ? -19.095 7.846   1.298   1.00 19.53 ? 124 VAL A N   1 
ATOM   998  C  CA  . VAL A 1 124 ? -19.864 6.621   0.939   1.00 18.94 ? 124 VAL A CA  1 
ATOM   999  C  C   . VAL A 1 124 ? -20.099 5.781   2.206   1.00 18.82 ? 124 VAL A C   1 
ATOM   1000 O  O   . VAL A 1 124 ? -21.192 5.251   2.362   1.00 19.77 ? 124 VAL A O   1 
ATOM   1001 C  CB  . VAL A 1 124 ? -19.159 5.833   -0.176  1.00 17.70 ? 124 VAL A CB  1 
ATOM   1002 C  CG1 . VAL A 1 124 ? -19.737 4.433   -0.338  1.00 16.16 ? 124 VAL A CG1 1 
ATOM   1003 C  CG2 . VAL A 1 124 ? -19.181 6.594   -1.498  1.00 17.27 ? 124 VAL A CG2 1 
ATOM   1004 N  N   . GLN A 1 125 ? -19.129 5.667   3.105   1.00 20.07 ? 125 GLN A N   1 
ATOM   1005 C  CA  . GLN A 1 125 ? -19.343 4.951   4.398   1.00 20.74 ? 125 GLN A CA  1 
ATOM   1006 C  C   . GLN A 1 125 ? -20.523 5.556   5.168   1.00 19.63 ? 125 GLN A C   1 
ATOM   1007 O  O   . GLN A 1 125 ? -21.343 4.795   5.661   1.00 20.74 ? 125 GLN A O   1 
ATOM   1008 C  CB  . GLN A 1 125 ? -18.100 4.979   5.285   1.00 21.08 ? 125 GLN A CB  1 
ATOM   1009 C  CG  . GLN A 1 125 ? -16.980 4.131   4.728   1.00 22.49 ? 125 GLN A CG  1 
ATOM   1010 C  CD  . GLN A 1 125 ? -15.930 3.837   5.761   1.00 24.21 ? 125 GLN A CD  1 
ATOM   1011 O  OE1 . GLN A 1 125 ? -16.217 3.314   6.851   1.00 25.59 ? 125 GLN A OE1 1 
ATOM   1012 N  NE2 . GLN A 1 125 ? -14.700 4.164   5.397   1.00 23.22 ? 125 GLN A NE2 1 
ATOM   1013 N  N   . LEU A 1 126 ? -20.591 6.872   5.300   1.00 21.54 ? 126 LEU A N   1 
ATOM   1014 C  CA  . LEU A 1 126 ? -21.745 7.542   5.952   1.00 21.96 ? 126 LEU A CA  1 
ATOM   1015 C  C   . LEU A 1 126 ? -23.035 7.227   5.202   1.00 19.95 ? 126 LEU A C   1 
ATOM   1016 O  O   . LEU A 1 126 ? -23.989 6.791   5.840   1.00 21.05 ? 126 LEU A O   1 
ATOM   1017 C  CB  . LEU A 1 126 ? -21.556 9.056   5.969   1.00 22.58 ? 126 LEU A CB  1 
ATOM   1018 C  CG  . LEU A 1 126 ? -22.689 9.770   6.694   1.00 23.63 ? 126 LEU A CG  1 
ATOM   1019 C  CD1 . LEU A 1 126 ? -22.460 9.722   8.194   1.00 23.85 ? 126 LEU A CD1 1 
ATOM   1020 C  CD2 . LEU A 1 126 ? -22.839 11.190  6.200   1.00 24.83 ? 126 LEU A CD2 1 
ATOM   1021 N  N   . VAL A 1 127 ? -23.074 7.490   3.904   1.00 18.89 ? 127 VAL A N   1 
ATOM   1022 C  CA  . VAL A 1 127 ? -24.309 7.282   3.107   1.00 20.47 ? 127 VAL A CA  1 
ATOM   1023 C  C   . VAL A 1 127 ? -24.789 5.854   3.354   1.00 20.46 ? 127 VAL A C   1 
ATOM   1024 O  O   . VAL A 1 127 ? -25.972 5.700   3.745   1.00 20.19 ? 127 VAL A O   1 
ATOM   1025 C  CB  . VAL A 1 127 ? -24.079 7.574   1.616   1.00 22.54 ? 127 VAL A CB  1 
ATOM   1026 C  CG1 . VAL A 1 127 ? -25.262 7.148   0.749   1.00 21.86 ? 127 VAL A CG1 1 
ATOM   1027 C  CG2 . VAL A 1 127 ? -23.718 9.038   1.411   1.00 23.59 ? 127 VAL A CG2 1 
ATOM   1028 N  N   . GLN A 1 128 ? -23.899 4.867   3.204   1.00 20.78 ? 128 GLN A N   1 
ATOM   1029 C  CA  . GLN A 1 128 ? -24.237 3.425   3.393   1.00 21.89 ? 128 GLN A CA  1 
ATOM   1030 C  C   . GLN A 1 128 ? -24.673 3.173   4.835   1.00 20.61 ? 128 GLN A C   1 
ATOM   1031 O  O   . GLN A 1 128 ? -25.615 2.375   5.027   1.00 21.40 ? 128 GLN A O   1 
ATOM   1032 C  CB  . GLN A 1 128 ? -23.088 2.527   2.941   1.00 22.90 ? 128 GLN A CB  1 
ATOM   1033 C  CG  . GLN A 1 128 ? -22.870 2.674   1.443   1.00 25.56 ? 128 GLN A CG  1 
ATOM   1034 C  CD  . GLN A 1 128 ? -22.183 1.517   0.762   1.00 29.49 ? 128 GLN A CD  1 
ATOM   1035 O  OE1 . GLN A 1 128 ? -21.060 1.148   1.089   1.00 34.30 ? 128 GLN A OE1 1 
ATOM   1036 N  NE2 . GLN A 1 128 ? -22.836 0.977   -0.258  1.00 31.80 ? 128 GLN A NE2 1 
ATOM   1037 N  N   . LYS A 1 129 ? -24.065 3.841   5.812   1.00 20.39 ? 129 LYS A N   1 
ATOM   1038 C  CA  . LYS A 1 129 ? -24.496 3.694   7.230   1.00 21.72 ? 129 LYS A CA  1 
ATOM   1039 C  C   . LYS A 1 129 ? -25.998 4.013   7.283   1.00 21.54 ? 129 LYS A C   1 
ATOM   1040 O  O   . LYS A 1 129 ? -26.759 3.220   7.794   1.00 21.21 ? 129 LYS A O   1 
ATOM   1041 C  CB  . LYS A 1 129 ? -23.714 4.596   8.200   1.00 21.19 ? 129 LYS A CB  1 
ATOM   1042 C  CG  . LYS A 1 129 ? -24.160 4.418   9.648   1.00 22.59 ? 129 LYS A CG  1 
ATOM   1043 C  CD  . LYS A 1 129 ? -23.445 5.213   10.727  1.00 21.81 ? 129 LYS A CD  1 
ATOM   1044 C  CE  . LYS A 1 129 ? -23.920 4.773   12.096  1.00 22.21 ? 129 LYS A CE  1 
ATOM   1045 N  NZ  . LYS A 1 129 ? -23.659 5.799   13.132  1.00 24.17 ? 129 LYS A NZ  1 
ATOM   1046 N  N   . TRP A 1 130 ? -26.369 5.175   6.752   1.00 22.56 ? 130 TRP A N   1 
ATOM   1047 C  CA  . TRP A 1 130 ? -27.712 5.780   6.852   1.00 21.57 ? 130 TRP A CA  1 
ATOM   1048 C  C   . TRP A 1 130 ? -28.710 5.006   5.999   1.00 20.23 ? 130 TRP A C   1 
ATOM   1049 O  O   . TRP A 1 130 ? -29.805 4.814   6.470   1.00 21.74 ? 130 TRP A O   1 
ATOM   1050 C  CB  . TRP A 1 130 ? -27.606 7.245   6.439   1.00 22.79 ? 130 TRP A CB  1 
ATOM   1051 C  CG  . TRP A 1 130 ? -26.938 8.090   7.479   1.00 21.56 ? 130 TRP A CG  1 
ATOM   1052 C  CD1 . TRP A 1 130 ? -26.319 7.655   8.609   1.00 21.55 ? 130 TRP A CD1 1 
ATOM   1053 C  CD2 . TRP A 1 130 ? -26.843 9.526   7.485   1.00 21.07 ? 130 TRP A CD2 1 
ATOM   1054 N  NE1 . TRP A 1 130 ? -25.832 8.724   9.312   1.00 23.81 ? 130 TRP A NE1 1 
ATOM   1055 C  CE2 . TRP A 1 130 ? -26.143 9.886   8.654   1.00 22.38 ? 130 TRP A CE2 1 
ATOM   1056 C  CE3 . TRP A 1 130 ? -27.260 10.536  6.615   1.00 20.42 ? 130 TRP A CE3 1 
ATOM   1057 C  CZ2 . TRP A 1 130 ? -25.848 11.210  8.971   1.00 21.15 ? 130 TRP A CZ2 1 
ATOM   1058 C  CZ3 . TRP A 1 130 ? -26.958 11.843  6.918   1.00 21.72 ? 130 TRP A CZ3 1 
ATOM   1059 C  CH2 . TRP A 1 130 ? -26.268 12.174  8.086   1.00 22.28 ? 130 TRP A CH2 1 
ATOM   1060 N  N   . GLU A 1 131 ? -28.316 4.545   4.821   1.00 19.76 ? 131 GLU A N   1 
ATOM   1061 C  CA  . GLU A 1 131 ? -29.140 3.640   3.966   1.00 20.27 ? 131 GLU A CA  1 
ATOM   1062 C  C   . GLU A 1 131 ? -29.563 2.394   4.761   1.00 19.72 ? 131 GLU A C   1 
ATOM   1063 O  O   . GLU A 1 131 ? -30.637 1.855   4.478   1.00 22.01 ? 131 GLU A O   1 
ATOM   1064 C  CB  . GLU A 1 131 ? -28.388 3.201   2.697   1.00 20.87 ? 131 GLU A CB  1 
ATOM   1065 C  CG  . GLU A 1 131 ? -28.132 4.306   1.666   1.00 23.11 ? 131 GLU A CG  1 
ATOM   1066 C  CD  . GLU A 1 131 ? -29.306 4.658   0.755   1.00 27.09 ? 131 GLU A CD  1 
ATOM   1067 O  OE1 . GLU A 1 131 ? -30.460 4.510   1.216   1.00 30.28 ? 131 GLU A OE1 1 
ATOM   1068 O  OE2 . GLU A 1 131 ? -29.077 5.062   -0.429  1.00 30.59 ? 131 GLU A OE2 1 
ATOM   1069 N  N   . ARG A 1 132 ? -28.741 1.895   5.673   1.00 19.66 ? 132 ARG A N   1 
ATOM   1070 C  CA  . ARG A 1 132 ? -28.961 0.586   6.332   1.00 20.26 ? 132 ARG A CA  1 
ATOM   1071 C  C   . ARG A 1 132 ? -29.711 0.768   7.658   1.00 20.27 ? 132 ARG A C   1 
ATOM   1072 O  O   . ARG A 1 132 ? -30.022 -0.251  8.257   1.00 21.44 ? 132 ARG A O   1 
ATOM   1073 C  CB  . ARG A 1 132 ? -27.617 -0.140  6.489   1.00 21.71 ? 132 ARG A CB  1 
ATOM   1074 C  CG  . ARG A 1 132 ? -27.046 -0.684  5.175   1.00 23.19 ? 132 ARG A CG  1 
ATOM   1075 C  CD  . ARG A 1 132 ? -25.519 -0.896  5.203   1.00 24.02 ? 132 ARG A CD  1 
ATOM   1076 N  NE  . ARG A 1 132 ? -24.891 -1.395  3.967   1.00 22.58 ? 132 ARG A NE  1 
ATOM   1077 C  CZ  . ARG A 1 132 ? -23.578 -1.468  3.735   1.00 21.03 ? 132 ARG A CZ  1 
ATOM   1078 N  NH1 . ARG A 1 132 ? -22.697 -1.054  4.633   1.00 20.51 ? 132 ARG A NH1 1 
ATOM   1079 N  NH2 . ARG A 1 132 ? -23.145 -1.924  2.575   1.00 20.71 ? 132 ARG A NH2 1 
ATOM   1080 N  N   . LEU A 1 133 ? -30.018 2.000   8.101   1.00 21.61 ? 133 LEU A N   1 
ATOM   1081 C  CA  . LEU A 1 133 ? -30.798 2.244   9.351   1.00 22.54 ? 133 LEU A CA  1 
ATOM   1082 C  C   . LEU A 1 133 ? -32.228 1.733   9.127   1.00 23.43 ? 133 LEU A C   1 
ATOM   1083 O  O   . LEU A 1 133 ? -32.737 1.835   8.006   1.00 23.58 ? 133 LEU A O   1 
ATOM   1084 C  CB  . LEU A 1 133 ? -30.837 3.726   9.736   1.00 22.22 ? 133 LEU A CB  1 
ATOM   1085 C  CG  . LEU A 1 133 ? -29.535 4.360   10.208  1.00 24.61 ? 133 LEU A CG  1 
ATOM   1086 C  CD1 . LEU A 1 133 ? -29.708 5.856   10.475  1.00 23.82 ? 133 LEU A CD1 1 
ATOM   1087 C  CD2 . LEU A 1 133 ? -29.005 3.658   11.443  1.00 25.52 ? 133 LEU A CD2 1 
ATOM   1088 N  N   . ASN A 1 134 ? -32.866 1.207   10.160  1.00 22.46 ? 134 ASN A N   1 
ATOM   1089 C  CA  . ASN A 1 134 ? -34.257 0.713   10.029  1.00 22.71 ? 134 ASN A CA  1 
ATOM   1090 C  C   . ASN A 1 134 ? -35.210 1.909   10.167  1.00 24.49 ? 134 ASN A C   1 
ATOM   1091 O  O   . ASN A 1 134 ? -34.775 2.953   10.688  1.00 23.44 ? 134 ASN A O   1 
ATOM   1092 C  CB  . ASN A 1 134 ? -34.489 -0.428  11.012  1.00 21.54 ? 134 ASN A CB  1 
ATOM   1093 C  CG  . ASN A 1 134 ? -33.478 -1.540  10.811  1.00 21.72 ? 134 ASN A CG  1 
ATOM   1094 O  OD1 . ASN A 1 134 ? -33.560 -2.321  9.861   1.00 20.32 ? 134 ASN A OD1 1 
ATOM   1095 N  ND2 . ASN A 1 134 ? -32.526 -1.638  11.716  1.00 22.42 ? 134 ASN A ND2 1 
ATOM   1096 N  N   . ALA A 1 135 ? -36.457 1.743   9.724   1.00 24.74 ? 135 ALA A N   1 
ATOM   1097 C  CA  . ALA A 1 135 ? -37.493 2.792   9.625   1.00 28.47 ? 135 ALA A CA  1 
ATOM   1098 C  C   . ALA A 1 135 ? -37.733 3.472   10.986  1.00 31.56 ? 135 ALA A C   1 
ATOM   1099 O  O   . ALA A 1 135 ? -38.025 4.688   11.001  1.00 32.96 ? 135 ALA A O   1 
ATOM   1100 C  CB  . ALA A 1 135 ? -38.765 2.175   9.067   1.00 29.81 ? 135 ALA A CB  1 
ATOM   1101 N  N   . ASP A 1 136 ? -37.625 2.762   12.104  1.00 31.49 ? 136 ASP A N   1 
ATOM   1102 C  CA  . ASP A 1 136 ? -37.995 3.356   13.422  1.00 37.00 ? 136 ASP A CA  1 
ATOM   1103 C  C   . ASP A 1 136 ? -36.760 3.928   14.135  1.00 36.25 ? 136 ASP A C   1 
ATOM   1104 O  O   . ASP A 1 136 ? -36.734 3.871   15.367  1.00 38.83 ? 136 ASP A O   1 
ATOM   1105 C  CB  . ASP A 1 136 ? -38.702 2.328   14.312  1.00 39.19 ? 136 ASP A CB  1 
ATOM   1106 C  CG  . ASP A 1 136 ? -37.803 1.197   14.790  1.00 44.20 ? 136 ASP A CG  1 
ATOM   1107 O  OD1 . ASP A 1 136 ? -36.725 0.985   14.172  1.00 47.07 ? 136 ASP A OD1 1 
ATOM   1108 O  OD2 . ASP A 1 136 ? -38.182 0.537   15.791  1.00 51.07 ? 136 ASP A OD2 1 
ATOM   1109 N  N   . GLU A 1 137 ? -35.783 4.457   13.402  1.00 34.79 ? 137 GLU A N   1 
ATOM   1110 C  CA  . GLU A 1 137 ? -34.448 4.839   13.953  1.00 35.25 ? 137 GLU A CA  1 
ATOM   1111 C  C   . GLU A 1 137 ? -34.106 6.268   13.524  1.00 32.70 ? 137 GLU A C   1 
ATOM   1112 O  O   . GLU A 1 137 ? -34.558 6.710   12.446  1.00 37.29 ? 137 GLU A O   1 
ATOM   1113 C  CB  . GLU A 1 137 ? -33.353 3.863   13.491  1.00 34.96 ? 137 GLU A CB  1 
ATOM   1114 C  CG  . GLU A 1 137 ? -33.704 2.402   13.751  1.00 35.74 ? 137 GLU A CG  1 
ATOM   1115 C  CD  . GLU A 1 137 ? -32.592 1.375   13.597  1.00 35.36 ? 137 GLU A CD  1 
ATOM   1116 O  OE1 . GLU A 1 137 ? -31.574 1.687   12.938  1.00 30.99 ? 137 GLU A OE1 1 
ATOM   1117 O  OE2 . GLU A 1 137 ? -32.776 0.230   14.102  1.00 33.67 ? 137 GLU A OE2 1 
ATOM   1118 N  N   . HIS A 1 138 ? -33.289 6.955   14.307  1.00 29.47 ? 138 HIS A N   1 
ATOM   1119 C  CA  . HIS A 1 138 ? -32.849 8.332   13.969  1.00 28.17 ? 138 HIS A CA  1 
ATOM   1120 C  C   . HIS A 1 138 ? -31.318 8.415   13.822  1.00 24.64 ? 138 HIS A C   1 
ATOM   1121 O  O   . HIS A 1 138 ? -30.619 7.420   14.092  1.00 22.63 ? 138 HIS A O   1 
ATOM   1122 C  CB  . HIS A 1 138 ? -33.448 9.295   14.988  1.00 27.79 ? 138 HIS A CB  1 
ATOM   1123 C  CG  . HIS A 1 138 ? -33.041 9.005   16.376  1.00 28.22 ? 138 HIS A CG  1 
ATOM   1124 N  ND1 . HIS A 1 138 ? -31.766 9.269   16.820  1.00 29.83 ? 138 HIS A ND1 1 
ATOM   1125 C  CD2 . HIS A 1 138 ? -33.740 8.547   17.428  1.00 30.67 ? 138 HIS A CD2 1 
ATOM   1126 C  CE1 . HIS A 1 138 ? -31.677 8.967   18.099  1.00 30.30 ? 138 HIS A CE1 1 
ATOM   1127 N  NE2 . HIS A 1 138 ? -32.877 8.524   18.497  1.00 34.34 ? 138 HIS A NE2 1 
ATOM   1128 N  N   . ILE A 1 139 ? -30.837 9.566   13.355  1.00 21.71 ? 139 ILE A N   1 
ATOM   1129 C  CA  . ILE A 1 139 ? -29.394 9.873   13.132  1.00 20.54 ? 139 ILE A CA  1 
ATOM   1130 C  C   . ILE A 1 139 ? -28.934 10.786  14.264  1.00 19.41 ? 139 ILE A C   1 
ATOM   1131 O  O   . ILE A 1 139 ? -29.591 11.787  14.521  1.00 18.39 ? 139 ILE A O   1 
ATOM   1132 C  CB  . ILE A 1 139 ? -29.178 10.514  11.748  1.00 19.91 ? 139 ILE A CB  1 
ATOM   1133 C  CG1 . ILE A 1 139 ? -29.358 9.489   10.622  1.00 20.07 ? 139 ILE A CG1 1 
ATOM   1134 C  CG2 . ILE A 1 139 ? -27.829 11.189  11.672  1.00 20.00 ? 139 ILE A CG2 1 
ATOM   1135 C  CD1 . ILE A 1 139 ? -29.656 10.086  9.274   1.00 19.67 ? 139 ILE A CD1 1 
ATOM   1136 N  N   . GLU A 1 140 ? -27.827 10.445  14.908  1.00 21.34 ? 140 GLU A N   1 
ATOM   1137 C  CA  . GLU A 1 140 ? -27.136 11.348  15.867  1.00 22.50 ? 140 GLU A CA  1 
ATOM   1138 C  C   . GLU A 1 140 ? -26.157 12.191  15.046  1.00 20.95 ? 140 GLU A C   1 
ATOM   1139 O  O   . GLU A 1 140 ? -25.063 11.686  14.745  1.00 22.54 ? 140 GLU A O   1 
ATOM   1140 C  CB  . GLU A 1 140 ? -26.526 10.514  16.993  1.00 23.02 ? 140 GLU A CB  1 
ATOM   1141 C  CG  . GLU A 1 140 ? -27.604 9.780   17.771  1.00 25.26 ? 140 GLU A CG  1 
ATOM   1142 C  CD  . GLU A 1 140 ? -27.132 9.023   18.990  1.00 25.02 ? 140 GLU A CD  1 
ATOM   1143 O  OE1 . GLU A 1 140 ? -25.933 8.802   19.082  1.00 25.59 ? 140 GLU A OE1 1 
ATOM   1144 O  OE2 . GLU A 1 140 ? -27.979 8.635   19.812  1.00 27.30 ? 140 GLU A OE2 1 
ATOM   1145 N  N   . VAL A 1 141 ? -26.555 13.414  14.691  1.00 19.48 ? 141 VAL A N   1 
ATOM   1146 C  CA  . VAL A 1 141 ? -25.907 14.212  13.612  1.00 19.02 ? 141 VAL A CA  1 
ATOM   1147 C  C   . VAL A 1 141 ? -24.472 14.586  13.980  1.00 18.47 ? 141 VAL A C   1 
ATOM   1148 O  O   . VAL A 1 141 ? -23.552 14.231  13.250  1.00 17.89 ? 141 VAL A O   1 
ATOM   1149 C  CB  . VAL A 1 141 ? -26.710 15.468  13.258  1.00 18.63 ? 141 VAL A CB  1 
ATOM   1150 C  CG1 . VAL A 1 141 ? -25.910 16.330  12.273  1.00 18.56 ? 141 VAL A CG1 1 
ATOM   1151 C  CG2 . VAL A 1 141 ? -28.080 15.107  12.736  1.00 17.87 ? 141 VAL A CG2 1 
ATOM   1152 N  N   . PRO A 1 142 ? -24.214 15.364  15.055  1.00 17.07 ? 142 PRO A N   1 
ATOM   1153 C  CA  . PRO A 1 142 ? -22.852 15.763  15.364  1.00 17.58 ? 142 PRO A CA  1 
ATOM   1154 C  C   . PRO A 1 142 ? -22.011 14.502  15.572  1.00 19.15 ? 142 PRO A C   1 
ATOM   1155 O  O   . PRO A 1 142 ? -20.895 14.494  15.089  1.00 20.99 ? 142 PRO A O   1 
ATOM   1156 C  CB  . PRO A 1 142 ? -22.956 16.647  16.622  1.00 17.35 ? 142 PRO A CB  1 
ATOM   1157 C  CG  . PRO A 1 142 ? -24.327 16.347  17.183  1.00 17.48 ? 142 PRO A CG  1 
ATOM   1158 C  CD  . PRO A 1 142 ? -25.175 15.935  15.997  1.00 16.99 ? 142 PRO A CD  1 
ATOM   1159 N  N   . GLU A 1 143 ? -22.574 13.467  16.215  1.00 19.56 ? 143 GLU A N   1 
ATOM   1160 C  CA  . GLU A 1 143 ? -21.867 12.194  16.485  1.00 18.87 ? 143 GLU A CA  1 
ATOM   1161 C  C   . GLU A 1 143 ? -21.402 11.620  15.155  1.00 18.04 ? 143 GLU A C   1 
ATOM   1162 O  O   . GLU A 1 143 ? -20.221 11.477  14.985  1.00 16.15 ? 143 GLU A O   1 
ATOM   1163 C  CB  . GLU A 1 143 ? -22.740 11.216  17.273  1.00 20.32 ? 143 GLU A CB  1 
ATOM   1164 C  CG  . GLU A 1 143 ? -22.911 11.625  18.731  1.00 20.99 ? 143 GLU A CG  1 
ATOM   1165 C  CD  . GLU A 1 143 ? -23.997 12.666  18.963  1.00 21.94 ? 143 GLU A CD  1 
ATOM   1166 O  OE1 . GLU A 1 143 ? -24.592 13.101  17.972  1.00 23.20 ? 143 GLU A OE1 1 
ATOM   1167 O  OE2 . GLU A 1 143 ? -24.293 12.998  20.136  1.00 23.55 ? 143 GLU A OE2 1 
ATOM   1168 N  N   . ASP A 1 144 ? -22.300 11.343  14.222  1.00 18.92 ? 144 ASP A N   1 
ATOM   1169 C  CA  . ASP A 1 144 ? -21.886 10.740  12.922  1.00 21.35 ? 144 ASP A CA  1 
ATOM   1170 C  C   . ASP A 1 144 ? -21.018 11.706  12.094  1.00 20.02 ? 144 ASP A C   1 
ATOM   1171 O  O   . ASP A 1 144 ? -20.181 11.204  11.355  1.00 19.45 ? 144 ASP A O   1 
ATOM   1172 C  CB  . ASP A 1 144 ? -23.072 10.284  12.058  1.00 22.72 ? 144 ASP A CB  1 
ATOM   1173 C  CG  . ASP A 1 144 ? -23.694 8.961   12.472  1.00 25.05 ? 144 ASP A CG  1 
ATOM   1174 O  OD1 . ASP A 1 144 ? -23.063 8.218   13.271  1.00 25.28 ? 144 ASP A OD1 1 
ATOM   1175 O  OD2 . ASP A 1 144 ? -24.818 8.685   11.992  1.00 26.64 ? 144 ASP A OD2 1 
ATOM   1176 N  N   . MET A 1 145 ? -21.231 13.025  12.141  1.00 19.66 ? 145 MET A N   1 
ATOM   1177 C  CA  . MET A 1 145 ? -20.425 13.960  11.312  1.00 19.59 ? 145 MET A CA  1 
ATOM   1178 C  C   . MET A 1 145 ? -18.991 13.993  11.855  1.00 21.21 ? 145 MET A C   1 
ATOM   1179 O  O   . MET A 1 145 ? -18.054 14.181  11.039  1.00 21.40 ? 145 MET A O   1 
ATOM   1180 C  CB  . MET A 1 145 ? -20.979 15.387  11.303  1.00 18.88 ? 145 MET A CB  1 
ATOM   1181 C  CG  . MET A 1 145 ? -22.355 15.520  10.736  1.00 18.75 ? 145 MET A CG  1 
ATOM   1182 S  SD  . MET A 1 145 ? -22.453 15.151  8.989   1.00 20.31 ? 145 MET A SD  1 
ATOM   1183 C  CE  . MET A 1 145 ? -23.069 13.470  9.079   1.00 22.00 ? 145 MET A CE  1 
ATOM   1184 N  N   . THR A 1 146 ? -18.827 13.891  13.181  1.00 21.01 ? 146 THR A N   1 
ATOM   1185 C  CA  . THR A 1 146 ? -17.504 13.902  13.861  1.00 20.69 ? 146 THR A CA  1 
ATOM   1186 C  C   . THR A 1 146 ? -16.780 12.591  13.533  1.00 21.66 ? 146 THR A C   1 
ATOM   1187 O  O   . THR A 1 146 ? -15.555 12.628  13.368  1.00 21.12 ? 146 THR A O   1 
ATOM   1188 C  CB  . THR A 1 146 ? -17.645 14.089  15.374  1.00 20.81 ? 146 THR A CB  1 
ATOM   1189 O  OG1 . THR A 1 146 ? -18.287 15.342  15.577  1.00 20.58 ? 146 THR A OG1 1 
ATOM   1190 C  CG2 . THR A 1 146 ? -16.324 14.069  16.117  1.00 20.97 ? 146 THR A CG2 1 
ATOM   1191 N  N   . ARG A 1 147 ? -17.524 11.487  13.412  1.00 20.39 ? 147 ARG A N   1 
ATOM   1192 C  CA  . ARG A 1 147 ? -17.007 10.222  12.843  1.00 21.02 ? 147 ARG A CA  1 
ATOM   1193 C  C   . ARG A 1 147 ? -16.476 10.467  11.418  1.00 20.00 ? 147 ARG A C   1 
ATOM   1194 O  O   . ARG A 1 147 ? -15.331 10.058  11.141  1.00 18.70 ? 147 ARG A O   1 
ATOM   1195 C  CB  . ARG A 1 147 ? -18.084 9.133   12.866  1.00 23.91 ? 147 ARG A CB  1 
ATOM   1196 C  CG  . ARG A 1 147 ? -18.487 8.659   14.262  1.00 25.27 ? 147 ARG A CG  1 
ATOM   1197 C  CD  . ARG A 1 147 ? -19.441 7.475   14.220  1.00 25.94 ? 147 ARG A CD  1 
ATOM   1198 N  NE  . ARG A 1 147 ? -19.812 7.076   15.575  1.00 27.68 ? 147 ARG A NE  1 
ATOM   1199 C  CZ  . ARG A 1 147 ? -20.967 7.356   16.177  1.00 27.52 ? 147 ARG A CZ  1 
ATOM   1200 N  NH1 . ARG A 1 147 ? -21.914 8.045   15.563  1.00 28.18 ? 147 ARG A NH1 1 
ATOM   1201 N  NH2 . ARG A 1 147 ? -21.165 6.962   17.419  1.00 28.13 ? 147 ARG A NH2 1 
ATOM   1202 N  N   . LEU A 1 148 ? -17.262 11.084  10.532  1.00 19.81 ? 148 LEU A N   1 
ATOM   1203 C  CA  . LEU A 1 148 ? -16.881 11.252  9.101   1.00 20.59 ? 148 LEU A CA  1 
ATOM   1204 C  C   . LEU A 1 148 ? -15.583 12.087  9.011   1.00 19.53 ? 148 LEU A C   1 
ATOM   1205 O  O   . LEU A 1 148 ? -14.646 11.645  8.327   1.00 17.14 ? 148 LEU A O   1 
ATOM   1206 C  CB  . LEU A 1 148 ? -18.045 11.885  8.320   1.00 21.20 ? 148 LEU A CB  1 
ATOM   1207 C  CG  . LEU A 1 148 ? -17.809 12.078  6.816   1.00 21.77 ? 148 LEU A CG  1 
ATOM   1208 C  CD1 . LEU A 1 148 ? -19.102 12.129  6.029   1.00 22.21 ? 148 LEU A CD1 1 
ATOM   1209 C  CD2 . LEU A 1 148 ? -17.018 13.325  6.532   1.00 22.09 ? 148 LEU A CD2 1 
ATOM   1210 N  N   . THR A 1 149 ? -15.504 13.227  9.712   1.00 19.62 ? 149 THR A N   1 
ATOM   1211 C  CA  . THR A 1 149 ? -14.448 14.260  9.515   1.00 19.28 ? 149 THR A CA  1 
ATOM   1212 C  C   . THR A 1 149 ? -13.135 13.796  10.158  1.00 20.83 ? 149 THR A C   1 
ATOM   1213 O  O   . THR A 1 149 ? -12.049 13.972  9.545   1.00 21.57 ? 149 THR A O   1 
ATOM   1214 C  CB  . THR A 1 149 ? -14.933 15.609  10.046  1.00 18.67 ? 149 THR A CB  1 
ATOM   1215 O  OG1 . THR A 1 149 ? -15.282 15.404  11.414  1.00 17.98 ? 149 THR A OG1 1 
ATOM   1216 C  CG2 . THR A 1 149 ? -16.104 16.149  9.254   1.00 19.37 ? 149 THR A CG2 1 
ATOM   1217 N  N   . LEU A 1 150 ? -13.219 13.198  11.341  1.00 20.70 ? 150 LEU A N   1 
ATOM   1218 C  CA  . LEU A 1 150 ? -12.044 12.540  11.932  1.00 20.57 ? 150 LEU A CA  1 
ATOM   1219 C  C   . LEU A 1 150 ? -11.455 11.557  10.917  1.00 20.61 ? 150 LEU A C   1 
ATOM   1220 O  O   . LEU A 1 150 ? -10.256 11.564  10.728  1.00 22.40 ? 150 LEU A O   1 
ATOM   1221 C  CB  . LEU A 1 150 ? -12.412 11.779  13.196  1.00 19.33 ? 150 LEU A CB  1 
ATOM   1222 C  CG  . LEU A 1 150 ? -11.257 10.915  13.682  1.00 18.64 ? 150 LEU A CG  1 
ATOM   1223 C  CD1 . LEU A 1 150 ? -10.092 11.807  14.034  1.00 18.43 ? 150 LEU A CD1 1 
ATOM   1224 C  CD2 . LEU A 1 150 ? -11.671 10.057  14.864  1.00 19.67 ? 150 LEU A CD2 1 
ATOM   1225 N  N   . ASP A 1 151 ? -12.272 10.691  10.344  1.00 21.14 ? 151 ASP A N   1 
ATOM   1226 C  CA  . ASP A 1 151 ? -11.785 9.571   9.508   1.00 21.33 ? 151 ASP A CA  1 
ATOM   1227 C  C   . ASP A 1 151 ? -11.156 10.171  8.249   1.00 19.31 ? 151 ASP A C   1 
ATOM   1228 O  O   . ASP A 1 151 ? -10.164 9.615   7.740   1.00 16.70 ? 151 ASP A O   1 
ATOM   1229 C  CB  . ASP A 1 151 ? -12.900 8.537   9.288   1.00 25.01 ? 151 ASP A CB  1 
ATOM   1230 C  CG  . ASP A 1 151 ? -13.024 7.503   10.423  1.00 28.39 ? 151 ASP A CG  1 
ATOM   1231 O  OD1 . ASP A 1 151 ? -12.912 7.906   11.615  1.00 28.77 ? 151 ASP A OD1 1 
ATOM   1232 O  OD2 . ASP A 1 151 ? -13.246 6.295   10.122  1.00 31.37 ? 151 ASP A OD2 1 
ATOM   1233 N  N   . THR A 1 152 ? -11.683 11.312  7.802   1.00 18.40 ? 152 THR A N   1 
ATOM   1234 C  CA  . THR A 1 152 ? -11.253 11.963  6.550   1.00 17.41 ? 152 THR A CA  1 
ATOM   1235 C  C   . THR A 1 152 ? -9.818  12.444  6.738   1.00 18.21 ? 152 THR A C   1 
ATOM   1236 O  O   . THR A 1 152 ? -9.006  12.320  5.791   1.00 18.30 ? 152 THR A O   1 
ATOM   1237 C  CB  . THR A 1 152 ? -12.229 13.055  6.122   1.00 17.24 ? 152 THR A CB  1 
ATOM   1238 O  OG1 . THR A 1 152 ? -13.504 12.428  5.965   1.00 16.39 ? 152 THR A OG1 1 
ATOM   1239 C  CG2 . THR A 1 152 ? -11.834 13.720  4.819   1.00 18.14 ? 152 THR A CG2 1 
ATOM   1240 N  N   . ILE A 1 153 ? -9.483  12.926  7.925   1.00 17.81 ? 153 ILE A N   1 
ATOM   1241 C  CA  . ILE A 1 153 ? -8.155  13.561  8.102   1.00 18.03 ? 153 ILE A CA  1 
ATOM   1242 C  C   . ILE A 1 153 ? -7.153  12.473  8.455   1.00 19.27 ? 153 ILE A C   1 
ATOM   1243 O  O   . ILE A 1 153 ? -5.970  12.610  8.050   1.00 18.40 ? 153 ILE A O   1 
ATOM   1244 C  CB  . ILE A 1 153 ? -8.186  14.731  9.093   1.00 18.50 ? 153 ILE A CB  1 
ATOM   1245 C  CG1 . ILE A 1 153 ? -6.833  15.444  9.058   1.00 20.69 ? 153 ILE A CG1 1 
ATOM   1246 C  CG2 . ILE A 1 153 ? -8.590  14.289  10.484  1.00 17.94 ? 153 ILE A CG2 1 
ATOM   1247 C  CD1 . ILE A 1 153 ? -6.403  15.881  7.664   1.00 21.08 ? 153 ILE A CD1 1 
ATOM   1248 N  N   . GLY A 1 154 ? -7.624  11.402  9.107   1.00 19.20 ? 154 GLY A N   1 
ATOM   1249 C  CA  . GLY A 1 154 ? -6.825  10.180  9.288   1.00 19.68 ? 154 GLY A CA  1 
ATOM   1250 C  C   . GLY A 1 154 ? -6.286  9.661   7.964   1.00 19.10 ? 154 GLY A C   1 
ATOM   1251 O  O   . GLY A 1 154 ? -5.090  9.338   7.854   1.00 19.43 ? 154 GLY A O   1 
ATOM   1252 N  N   . LEU A 1 155 ? -7.162  9.507   7.002   1.00 19.69 ? 155 LEU A N   1 
ATOM   1253 C  CA  . LEU A 1 155 ? -6.830  8.862   5.721   1.00 21.12 ? 155 LEU A CA  1 
ATOM   1254 C  C   . LEU A 1 155 ? -5.915  9.831   4.950   1.00 22.98 ? 155 LEU A C   1 
ATOM   1255 O  O   . LEU A 1 155 ? -4.770  9.466   4.670   1.00 23.77 ? 155 LEU A O   1 
ATOM   1256 C  CB  . LEU A 1 155 ? -8.168  8.541   5.047   1.00 21.40 ? 155 LEU A CB  1 
ATOM   1257 C  CG  . LEU A 1 155 ? -8.129  7.521   3.912   1.00 22.88 ? 155 LEU A CG  1 
ATOM   1258 C  CD1 . LEU A 1 155 ? -7.393  6.254   4.329   1.00 22.55 ? 155 LEU A CD1 1 
ATOM   1259 C  CD2 . LEU A 1 155 ? -9.537  7.205   3.420   1.00 22.11 ? 155 LEU A CD2 1 
ATOM   1260 N  N   . CYS A 1 156 ? -6.331  11.084  4.763   1.00 24.86 ? 156 CYS A N   1 
ATOM   1261 C  CA  . CYS A 1 156 ? -5.583  12.142  4.026   1.00 24.41 ? 156 CYS A CA  1 
ATOM   1262 C  C   . CYS A 1 156 ? -4.305  12.558  4.770   1.00 25.34 ? 156 CYS A C   1 
ATOM   1263 O  O   . CYS A 1 156 ? -3.309  12.889  4.098   1.00 27.76 ? 156 CYS A O   1 
ATOM   1264 C  CB  . CYS A 1 156 ? -6.468  13.363  3.801   1.00 24.12 ? 156 CYS A CB  1 
ATOM   1265 S  SG  . CYS A 1 156 ? -7.887  13.005  2.734   1.00 24.83 ? 156 CYS A SG  1 
ATOM   1266 N  N   . GLY A 1 157 ? -4.329  12.609  6.100   1.00 25.59 ? 157 GLY A N   1 
ATOM   1267 C  CA  . GLY A 1 157 ? -3.180  13.078  6.890   1.00 25.70 ? 157 GLY A CA  1 
ATOM   1268 C  C   . GLY A 1 157 ? -2.052  12.067  6.825   1.00 28.38 ? 157 GLY A C   1 
ATOM   1269 O  O   . GLY A 1 157 ? -0.933  12.425  6.356   1.00 28.88 ? 157 GLY A O   1 
ATOM   1270 N  N   . PHE A 1 158 ? -2.318  10.823  7.236   1.00 26.36 ? 158 PHE A N   1 
ATOM   1271 C  CA  . PHE A 1 158 ? -1.250  9.796   7.337   1.00 26.04 ? 158 PHE A CA  1 
ATOM   1272 C  C   . PHE A 1 158 ? -1.756  8.400   6.965   1.00 25.34 ? 158 PHE A C   1 
ATOM   1273 O  O   . PHE A 1 158 ? -1.178  7.416   7.468   1.00 24.46 ? 158 PHE A O   1 
ATOM   1274 C  CB  . PHE A 1 158 ? -0.610  9.867   8.721   1.00 25.50 ? 158 PHE A CB  1 
ATOM   1275 C  CG  . PHE A 1 158 ? -1.582  9.874   9.866   1.00 26.30 ? 158 PHE A CG  1 
ATOM   1276 C  CD1 . PHE A 1 158 ? -2.304  11.014  10.169  1.00 27.90 ? 158 PHE A CD1 1 
ATOM   1277 C  CD2 . PHE A 1 158 ? -1.754  8.747   10.655  1.00 27.63 ? 158 PHE A CD2 1 
ATOM   1278 C  CE1 . PHE A 1 158 ? -3.179  11.024  11.245  1.00 29.21 ? 158 PHE A CE1 1 
ATOM   1279 C  CE2 . PHE A 1 158 ? -2.606  8.769   11.749  1.00 28.24 ? 158 PHE A CE2 1 
ATOM   1280 C  CZ  . PHE A 1 158 ? -3.317  9.909   12.039  1.00 28.53 ? 158 PHE A CZ  1 
ATOM   1281 N  N   . ASN A 1 159 ? -2.737  8.305   6.056   1.00 25.99 ? 159 ASN A N   1 
ATOM   1282 C  CA  . ASN A 1 159 ? -3.144  7.016   5.438   1.00 25.95 ? 159 ASN A CA  1 
ATOM   1283 C  C   . ASN A 1 159 ? -3.503  5.985   6.513   1.00 24.89 ? 159 ASN A C   1 
ATOM   1284 O  O   . ASN A 1 159 ? -3.239  4.812   6.266   1.00 27.31 ? 159 ASN A O   1 
ATOM   1285 C  CB  . ASN A 1 159 ? -2.020  6.452   4.567   1.00 28.02 ? 159 ASN A CB  1 
ATOM   1286 C  CG  . ASN A 1 159 ? -2.486  5.340   3.658   1.00 30.23 ? 159 ASN A CG  1 
ATOM   1287 O  OD1 . ASN A 1 159 ? -3.676  5.215   3.414   1.00 28.66 ? 159 ASN A OD1 1 
ATOM   1288 N  ND2 . ASN A 1 159 ? -1.560  4.527   3.165   1.00 34.04 ? 159 ASN A ND2 1 
ATOM   1289 N  N   . TYR A 1 160 ? -4.091  6.416   7.633   1.00 21.87 ? 160 TYR A N   1 
ATOM   1290 C  CA  . TYR A 1 160 ? -4.566  5.588   8.770   1.00 20.18 ? 160 TYR A CA  1 
ATOM   1291 C  C   . TYR A 1 160 ? -6.093  5.628   8.856   1.00 19.63 ? 160 TYR A C   1 
ATOM   1292 O  O   . TYR A 1 160 ? -6.646  6.740   8.795   1.00 21.29 ? 160 TYR A O   1 
ATOM   1293 C  CB  . TYR A 1 160 ? -4.048  6.155   10.083  1.00 18.97 ? 160 TYR A CB  1 
ATOM   1294 C  CG  . TYR A 1 160 ? -4.411  5.341   11.293  1.00 18.80 ? 160 TYR A CG  1 
ATOM   1295 C  CD1 . TYR A 1 160 ? -3.648  4.254   11.695  1.00 18.93 ? 160 TYR A CD1 1 
ATOM   1296 C  CD2 . TYR A 1 160 ? -5.487  5.699   12.086  1.00 18.90 ? 160 TYR A CD2 1 
ATOM   1297 C  CE1 . TYR A 1 160 ? -3.964  3.527   12.837  1.00 18.73 ? 160 TYR A CE1 1 
ATOM   1298 C  CE2 . TYR A 1 160 ? -5.825  4.972   13.215  1.00 19.41 ? 160 TYR A CE2 1 
ATOM   1299 C  CZ  . TYR A 1 160 ? -5.066  3.879   13.593  1.00 18.81 ? 160 TYR A CZ  1 
ATOM   1300 O  OH  . TYR A 1 160 ? -5.439  3.170   14.701  1.00 19.99 ? 160 TYR A OH  1 
ATOM   1301 N  N   . ARG A 1 161 ? -6.736  4.479   9.076   1.00 17.98 ? 161 ARG A N   1 
ATOM   1302 C  CA  . ARG A 1 161 ? -8.214  4.370   9.186   1.00 18.08 ? 161 ARG A CA  1 
ATOM   1303 C  C   . ARG A 1 161 ? -8.625  4.235   10.659  1.00 18.18 ? 161 ARG A C   1 
ATOM   1304 O  O   . ARG A 1 161 ? -8.486  3.161   11.236  1.00 18.51 ? 161 ARG A O   1 
ATOM   1305 C  CB  . ARG A 1 161 ? -8.696  3.207   8.324   1.00 18.62 ? 161 ARG A CB  1 
ATOM   1306 C  CG  . ARG A 1 161 ? -8.572  3.473   6.826   1.00 18.06 ? 161 ARG A CG  1 
ATOM   1307 C  CD  . ARG A 1 161 ? -9.109  2.324   5.995   1.00 17.38 ? 161 ARG A CD  1 
ATOM   1308 N  NE  . ARG A 1 161 ? -8.990  2.628   4.579   1.00 16.37 ? 161 ARG A NE  1 
ATOM   1309 C  CZ  . ARG A 1 161 ? -9.926  3.208   3.859   1.00 15.57 ? 161 ARG A CZ  1 
ATOM   1310 N  NH1 . ARG A 1 161 ? -11.076 3.535   4.412   1.00 15.40 ? 161 ARG A NH1 1 
ATOM   1311 N  NH2 . ARG A 1 161 ? -9.707  3.470   2.585   1.00 15.73 ? 161 ARG A NH2 1 
ATOM   1312 N  N   . PHE A 1 162 ? -9.139  5.295   11.255  1.00 17.98 ? 162 PHE A N   1 
ATOM   1313 C  CA  . PHE A 1 162 ? -9.758  5.233   12.607  1.00 19.51 ? 162 PHE A CA  1 
ATOM   1314 C  C   . PHE A 1 162 ? -10.923 4.237   12.652  1.00 19.70 ? 162 PHE A C   1 
ATOM   1315 O  O   . PHE A 1 162 ? -11.191 3.675   13.757  1.00 20.70 ? 162 PHE A O   1 
ATOM   1316 C  CB  . PHE A 1 162 ? -10.207 6.623   13.049  1.00 19.52 ? 162 PHE A CB  1 
ATOM   1317 C  CG  . PHE A 1 162 ? -9.041  7.449   13.491  1.00 19.93 ? 162 PHE A CG  1 
ATOM   1318 C  CD1 . PHE A 1 162 ? -8.501  7.263   14.760  1.00 20.59 ? 162 PHE A CD1 1 
ATOM   1319 C  CD2 . PHE A 1 162 ? -8.452  8.354   12.622  1.00 19.54 ? 162 PHE A CD2 1 
ATOM   1320 C  CE1 . PHE A 1 162 ? -7.396  7.997   15.159  1.00 21.17 ? 162 PHE A CE1 1 
ATOM   1321 C  CE2 . PHE A 1 162 ? -7.346  9.079   13.025  1.00 20.26 ? 162 PHE A CE2 1 
ATOM   1322 C  CZ  . PHE A 1 162 ? -6.817  8.900   14.286  1.00 20.32 ? 162 PHE A CZ  1 
ATOM   1323 N  N   . ASN A 1 163 ? -11.596 4.024   11.517  1.00 17.91 ? 163 ASN A N   1 
ATOM   1324 C  CA  . ASN A 1 163 ? -12.774 3.119   11.421  1.00 18.33 ? 163 ASN A CA  1 
ATOM   1325 C  C   . ASN A 1 163 ? -13.851 3.565   12.426  1.00 17.70 ? 163 ASN A C   1 
ATOM   1326 O  O   . ASN A 1 163 ? -14.430 2.696   13.039  1.00 16.38 ? 163 ASN A O   1 
ATOM   1327 C  CB  . ASN A 1 163 ? -12.333 1.652   11.550  1.00 16.98 ? 163 ASN A CB  1 
ATOM   1328 C  CG  . ASN A 1 163 ? -11.563 1.233   10.322  1.00 17.17 ? 163 ASN A CG  1 
ATOM   1329 O  OD1 . ASN A 1 163 ? -11.941 1.622   9.218   1.00 16.62 ? 163 ASN A OD1 1 
ATOM   1330 N  ND2 . ASN A 1 163 ? -10.456 0.523   10.495  1.00 16.80 ? 163 ASN A ND2 1 
ATOM   1331 N  N   . SER A 1 164 ? -14.148 4.872   12.506  1.00 19.53 ? 164 SER A N   1 
ATOM   1332 C  CA  . SER A 1 164 ? -15.063 5.510   13.501  1.00 20.78 ? 164 SER A CA  1 
ATOM   1333 C  C   . SER A 1 164 ? -16.477 4.907   13.436  1.00 20.36 ? 164 SER A C   1 
ATOM   1334 O  O   . SER A 1 164 ? -17.124 4.791   14.507  1.00 19.44 ? 164 SER A O   1 
ATOM   1335 C  CB  . SER A 1 164 ? -15.131 6.992   13.299  1.00 21.63 ? 164 SER A CB  1 
ATOM   1336 O  OG  . SER A 1 164 ? -13.897 7.612   13.627  1.00 23.54 ? 164 SER A OG  1 
ATOM   1337 N  N   . PHE A 1 165 ? -16.924 4.541   12.234  1.00 19.12 ? 165 PHE A N   1 
ATOM   1338 C  CA  . PHE A 1 165 ? -18.286 4.020   11.952  1.00 21.12 ? 165 PHE A CA  1 
ATOM   1339 C  C   . PHE A 1 165 ? -18.375 2.545   12.337  1.00 20.85 ? 165 PHE A C   1 
ATOM   1340 O  O   . PHE A 1 165 ? -19.496 2.007   12.279  1.00 21.32 ? 165 PHE A O   1 
ATOM   1341 C  CB  . PHE A 1 165 ? -18.695 4.191   10.477  1.00 20.70 ? 165 PHE A CB  1 
ATOM   1342 C  CG  . PHE A 1 165 ? -18.932 5.619   10.041  1.00 21.06 ? 165 PHE A CG  1 
ATOM   1343 C  CD1 . PHE A 1 165 ? -19.749 6.467   10.768  1.00 20.67 ? 165 PHE A CD1 1 
ATOM   1344 C  CD2 . PHE A 1 165 ? -18.320 6.127   8.896   1.00 22.85 ? 165 PHE A CD2 1 
ATOM   1345 C  CE1 . PHE A 1 165 ? -19.929 7.788   10.375  1.00 21.48 ? 165 PHE A CE1 1 
ATOM   1346 C  CE2 . PHE A 1 165 ? -18.497 7.446   8.510   1.00 21.04 ? 165 PHE A CE2 1 
ATOM   1347 C  CZ  . PHE A 1 165 ? -19.303 8.276   9.252   1.00 21.31 ? 165 PHE A CZ  1 
ATOM   1348 N  N   . TYR A 1 166 ? -17.252 1.917   12.680  1.00 22.14 ? 166 TYR A N   1 
ATOM   1349 C  CA  . TYR A 1 166 ? -17.161 0.466   12.984  1.00 24.78 ? 166 TYR A CA  1 
ATOM   1350 C  C   . TYR A 1 166 ? -17.003 0.238   14.493  1.00 29.48 ? 166 TYR A C   1 
ATOM   1351 O  O   . TYR A 1 166 ? -16.666 -0.889  14.878  1.00 33.54 ? 166 TYR A O   1 
ATOM   1352 C  CB  . TYR A 1 166 ? -15.986 -0.170  12.248  1.00 23.25 ? 166 TYR A CB  1 
ATOM   1353 C  CG  . TYR A 1 166 ? -16.139 -0.372  10.762  1.00 22.96 ? 166 TYR A CG  1 
ATOM   1354 C  CD1 . TYR A 1 166 ? -16.757 -1.505  10.249  1.00 24.40 ? 166 TYR A CD1 1 
ATOM   1355 C  CD2 . TYR A 1 166 ? -15.611 0.527   9.861   1.00 22.05 ? 166 TYR A CD2 1 
ATOM   1356 C  CE1 . TYR A 1 166 ? -16.869 -1.723  8.884   1.00 23.54 ? 166 TYR A CE1 1 
ATOM   1357 C  CE2 . TYR A 1 166 ? -15.679 0.307   8.492   1.00 24.13 ? 166 TYR A CE2 1 
ATOM   1358 C  CZ  . TYR A 1 166 ? -16.317 -0.816  7.999   1.00 23.38 ? 166 TYR A CZ  1 
ATOM   1359 O  OH  . TYR A 1 166 ? -16.422 -0.991  6.656   1.00 21.24 ? 166 TYR A OH  1 
ATOM   1360 N  N   . ARG A 1 167 ? -17.291 1.245   15.322  1.00 37.30 ? 167 ARG A N   1 
ATOM   1361 C  CA  . ARG A 1 167 ? -17.163 1.172   16.809  1.00 41.51 ? 167 ARG A CA  1 
ATOM   1362 C  C   . ARG A 1 167 ? -17.988 2.287   17.479  1.00 50.75 ? 167 ARG A C   1 
ATOM   1363 O  O   . ARG A 1 167 ? -18.070 3.414   16.912  1.00 51.86 ? 167 ARG A O   1 
ATOM   1364 C  CB  . ARG A 1 167 ? -15.689 1.254   17.226  1.00 39.84 ? 167 ARG A CB  1 
ATOM   1365 C  CG  . ARG A 1 167 ? -14.799 2.068   16.291  1.00 39.23 ? 167 ARG A CG  1 
ATOM   1366 C  CD  . ARG A 1 167 ? -13.714 2.888   17.001  1.00 39.80 ? 167 ARG A CD  1 
ATOM   1367 N  NE  . ARG A 1 167 ? -12.445 2.786   16.287  1.00 36.38 ? 167 ARG A NE  1 
ATOM   1368 C  CZ  . ARG A 1 167 ? -11.275 2.459   16.819  1.00 36.31 ? 167 ARG A CZ  1 
ATOM   1369 N  NH1 . ARG A 1 167 ? -11.150 2.250   18.119  1.00 37.33 ? 167 ARG A NH1 1 
ATOM   1370 N  NH2 . ARG A 1 167 ? -10.214 2.354   16.039  1.00 36.27 ? 167 ARG A NH2 1 
ATOM   1371 N  N   . ASP A 1 168 ? -18.587 1.964   18.636  1.00 61.83 ? 168 ASP A N   1 
ATOM   1372 C  CA  . ASP A 1 168 ? -19.215 2.904   19.612  1.00 69.01 ? 168 ASP A CA  1 
ATOM   1373 C  C   . ASP A 1 168 ? -18.089 3.516   20.469  1.00 68.50 ? 168 ASP A C   1 
ATOM   1374 O  O   . ASP A 1 168 ? -18.117 4.746   20.707  1.00 64.41 ? 168 ASP A O   1 
ATOM   1375 C  CB  . ASP A 1 168 ? -20.277 2.199   20.488  1.00 71.07 ? 168 ASP A CB  1 
ATOM   1376 C  CG  . ASP A 1 168 ? -21.541 1.703   19.782  1.00 68.34 ? 168 ASP A CG  1 
ATOM   1377 O  OD1 . ASP A 1 168 ? -22.234 2.530   19.170  1.00 73.14 ? 168 ASP A OD1 1 
ATOM   1378 O  OD2 . ASP A 1 168 ? -21.844 0.492   19.871  1.00 66.98 ? 168 ASP A OD2 1 
ATOM   1379 N  N   . GLN A 1 169 ? -17.113 2.676   20.854  1.00 72.45 ? 169 GLN A N   1 
ATOM   1380 C  CA  . GLN A 1 169 ? -15.999 2.941   21.817  1.00 73.78 ? 169 GLN A CA  1 
ATOM   1381 C  C   . GLN A 1 169 ? -14.828 3.642   21.116  1.00 66.80 ? 169 GLN A C   1 
ATOM   1382 O  O   . GLN A 1 169 ? -14.245 3.079   20.189  1.00 57.62 ? 169 GLN A O   1 
ATOM   1383 C  CB  . GLN A 1 169 ? -15.555 1.629   22.484  1.00 76.38 ? 169 GLN A CB  1 
ATOM   1384 C  CG  . GLN A 1 169 ? -14.967 0.569   21.547  1.00 78.11 ? 169 GLN A CG  1 
ATOM   1385 C  CD  . GLN A 1 169 ? -15.969 -0.081  20.619  1.00 78.32 ? 169 GLN A CD  1 
ATOM   1386 O  OE1 . GLN A 1 169 ? -17.175 0.136   20.712  1.00 69.53 ? 169 GLN A OE1 1 
ATOM   1387 N  NE2 . GLN A 1 169 ? -15.470 -0.890  19.698  1.00 77.60 ? 169 GLN A NE2 1 
ATOM   1388 N  N   . PRO A 1 170 ? -14.425 4.871   21.548  1.00 60.51 ? 170 PRO A N   1 
ATOM   1389 C  CA  . PRO A 1 170 ? -13.445 5.677   20.807  1.00 53.83 ? 170 PRO A CA  1 
ATOM   1390 C  C   . PRO A 1 170 ? -12.015 5.102   20.743  1.00 43.50 ? 170 PRO A C   1 
ATOM   1391 O  O   . PRO A 1 170 ? -11.635 4.312   21.562  1.00 36.04 ? 170 PRO A O   1 
ATOM   1392 C  CB  . PRO A 1 170 ? -13.450 7.030   21.557  1.00 57.58 ? 170 PRO A CB  1 
ATOM   1393 C  CG  . PRO A 1 170 ? -14.760 7.034   22.328  1.00 57.08 ? 170 PRO A CG  1 
ATOM   1394 C  CD  . PRO A 1 170 ? -14.919 5.586   22.742  1.00 58.94 ? 170 PRO A CD  1 
ATOM   1395 N  N   . HIS A 1 171 ? -11.241 5.525   19.747  1.00 36.78 ? 171 HIS A N   1 
ATOM   1396 C  CA  . HIS A 1 171 ? -9.806  5.166   19.614  1.00 35.71 ? 171 HIS A CA  1 
ATOM   1397 C  C   . HIS A 1 171 ? -9.035  5.767   20.798  1.00 33.34 ? 171 HIS A C   1 
ATOM   1398 O  O   . HIS A 1 171 ? -9.302  6.901   21.207  1.00 27.86 ? 171 HIS A O   1 
ATOM   1399 C  CB  . HIS A 1 171 ? -9.322  5.613   18.229  1.00 35.20 ? 171 HIS A CB  1 
ATOM   1400 C  CG  . HIS A 1 171 ? -7.946  5.166   17.862  1.00 35.85 ? 171 HIS A CG  1 
ATOM   1401 N  ND1 . HIS A 1 171 ? -6.834  5.513   18.605  1.00 37.61 ? 171 HIS A ND1 1 
ATOM   1402 C  CD2 . HIS A 1 171 ? -7.496  4.450   16.809  1.00 35.62 ? 171 HIS A CD2 1 
ATOM   1403 C  CE1 . HIS A 1 171 ? -5.755  5.001   18.037  1.00 37.23 ? 171 HIS A CE1 1 
ATOM   1404 N  NE2 . HIS A 1 171 ? -6.138  4.350   16.928  1.00 35.66 ? 171 HIS A NE2 1 
ATOM   1405 N  N   . PRO A 1 172 ? -8.081  5.030   21.418  1.00 32.77 ? 172 PRO A N   1 
ATOM   1406 C  CA  . PRO A 1 172 ? -7.342  5.541   22.583  1.00 31.88 ? 172 PRO A CA  1 
ATOM   1407 C  C   . PRO A 1 172 ? -6.665  6.904   22.353  1.00 30.14 ? 172 PRO A C   1 
ATOM   1408 O  O   . PRO A 1 172 ? -6.605  7.705   23.276  1.00 29.89 ? 172 PRO A O   1 
ATOM   1409 C  CB  . PRO A 1 172 ? -6.314  4.425   22.870  1.00 31.56 ? 172 PRO A CB  1 
ATOM   1410 C  CG  . PRO A 1 172 ? -7.014  3.175   22.372  1.00 31.47 ? 172 PRO A CG  1 
ATOM   1411 C  CD  . PRO A 1 172 ? -7.714  3.636   21.105  1.00 32.63 ? 172 PRO A CD  1 
ATOM   1412 N  N   . PHE A 1 173 ? -6.175  7.155   21.133  1.00 27.90 ? 173 PHE A N   1 
ATOM   1413 C  CA  . PHE A 1 173 ? -5.681  8.494   20.734  1.00 23.66 ? 173 PHE A CA  1 
ATOM   1414 C  C   . PHE A 1 173 ? -6.750  9.540   21.042  1.00 22.26 ? 173 PHE A C   1 
ATOM   1415 O  O   . PHE A 1 173 ? -6.425  10.574  21.629  1.00 22.00 ? 173 PHE A O   1 
ATOM   1416 C  CB  . PHE A 1 173 ? -5.361  8.590   19.247  1.00 23.45 ? 173 PHE A CB  1 
ATOM   1417 C  CG  . PHE A 1 173 ? -4.821  9.948   18.906  1.00 23.60 ? 173 PHE A CG  1 
ATOM   1418 C  CD1 . PHE A 1 173 ? -3.493  10.247  19.130  1.00 24.50 ? 173 PHE A CD1 1 
ATOM   1419 C  CD2 . PHE A 1 173 ? -5.659  10.948  18.455  1.00 26.10 ? 173 PHE A CD2 1 
ATOM   1420 C  CE1 . PHE A 1 173 ? -2.999  11.511  18.859  1.00 26.67 ? 173 PHE A CE1 1 
ATOM   1421 C  CE2 . PHE A 1 173 ? -5.168  12.210  18.178  1.00 27.60 ? 173 PHE A CE2 1 
ATOM   1422 C  CZ  . PHE A 1 173 ? -3.834  12.493  18.384  1.00 28.00 ? 173 PHE A CZ  1 
ATOM   1423 N  N   . ILE A 1 174 ? -7.984  9.261   20.619  1.00 21.46 ? 174 ILE A N   1 
ATOM   1424 C  CA  . ILE A 1 174 ? -9.134  10.212  20.599  1.00 21.52 ? 174 ILE A CA  1 
ATOM   1425 C  C   . ILE A 1 174 ? -9.638  10.414  22.040  1.00 21.92 ? 174 ILE A C   1 
ATOM   1426 O  O   . ILE A 1 174 ? -9.987  11.539  22.385  1.00 22.37 ? 174 ILE A O   1 
ATOM   1427 C  CB  . ILE A 1 174 ? -10.233 9.711   19.627  1.00 21.08 ? 174 ILE A CB  1 
ATOM   1428 C  CG1 . ILE A 1 174 ? -9.716  9.549   18.190  1.00 21.54 ? 174 ILE A CG1 1 
ATOM   1429 C  CG2 . ILE A 1 174 ? -11.464 10.588  19.667  1.00 20.07 ? 174 ILE A CG2 1 
ATOM   1430 C  CD1 . ILE A 1 174 ? -9.232  10.838  17.542  1.00 22.24 ? 174 ILE A CD1 1 
ATOM   1431 N  N   . THR A 1 175 ? -9.655  9.386   22.882  1.00 22.23 ? 175 THR A N   1 
ATOM   1432 C  CA  . THR A 1 175 ? -10.047 9.575   24.304  1.00 22.78 ? 175 THR A CA  1 
ATOM   1433 C  C   . THR A 1 175 ? -9.118  10.637  24.894  1.00 21.88 ? 175 THR A C   1 
ATOM   1434 O  O   . THR A 1 175 ? -9.620  11.646  25.427  1.00 20.57 ? 175 THR A O   1 
ATOM   1435 C  CB  . THR A 1 175 ? -10.048 8.252   25.082  1.00 23.19 ? 175 THR A CB  1 
ATOM   1436 O  OG1 . THR A 1 175 ? -11.019 7.428   24.448  1.00 23.27 ? 175 THR A OG1 1 
ATOM   1437 C  CG2 . THR A 1 175 ? -10.391 8.424   26.548  1.00 24.47 ? 175 THR A CG2 1 
ATOM   1438 N  N   . SER A 1 176 ? -7.810  10.445  24.712  1.00 23.47 ? 176 SER A N   1 
ATOM   1439 C  CA  . SER A 1 176 ? -6.736  11.311  25.262  1.00 22.78 ? 176 SER A CA  1 
ATOM   1440 C  C   . SER A 1 176 ? -6.811  12.705  24.654  1.00 23.10 ? 176 SER A C   1 
ATOM   1441 O  O   . SER A 1 176 ? -6.692  13.687  25.426  1.00 23.39 ? 176 SER A O   1 
ATOM   1442 C  CB  . SER A 1 176 ? -5.401  10.702  25.043  1.00 22.68 ? 176 SER A CB  1 
ATOM   1443 O  OG  . SER A 1 176 ? -5.244  9.624   25.929  1.00 22.61 ? 176 SER A OG  1 
ATOM   1444 N  N   . MET A 1 177 ? -7.014  12.792  23.339  1.00 22.66 ? 177 MET A N   1 
ATOM   1445 C  CA  . MET A 1 177 ? -7.089  14.092  22.618  1.00 22.01 ? 177 MET A CA  1 
ATOM   1446 C  C   . MET A 1 177 ? -8.273  14.913  23.152  1.00 20.91 ? 177 MET A C   1 
ATOM   1447 O  O   . MET A 1 177 ? -8.100  16.126  23.425  1.00 22.48 ? 177 MET A O   1 
ATOM   1448 C  CB  . MET A 1 177 ? -7.258  13.897  21.110  1.00 21.99 ? 177 MET A CB  1 
ATOM   1449 C  CG  . MET A 1 177 ? -7.156  15.200  20.363  1.00 23.17 ? 177 MET A CG  1 
ATOM   1450 S  SD  . MET A 1 177 ? -7.575  15.045  18.623  1.00 26.19 ? 177 MET A SD  1 
ATOM   1451 C  CE  . MET A 1 177 ? -9.330  14.780  18.834  1.00 27.10 ? 177 MET A CE  1 
ATOM   1452 N  N   . VAL A 1 178 ? -9.431  14.278  23.276  1.00 18.84 ? 178 VAL A N   1 
ATOM   1453 C  CA  . VAL A 1 178 ? -10.691 14.917  23.755  1.00 20.21 ? 178 VAL A CA  1 
ATOM   1454 C  C   . VAL A 1 178 ? -10.568 15.330  25.245  1.00 21.70 ? 178 VAL A C   1 
ATOM   1455 O  O   . VAL A 1 178 ? -10.985 16.471  25.578  1.00 20.88 ? 178 VAL A O   1 
ATOM   1456 C  CB  . VAL A 1 178 ? -11.879 13.973  23.477  1.00 20.05 ? 178 VAL A CB  1 
ATOM   1457 C  CG1 . VAL A 1 178 ? -13.148 14.372  24.225  1.00 20.24 ? 178 VAL A CG1 1 
ATOM   1458 C  CG2 . VAL A 1 178 ? -12.137 13.860  21.972  1.00 19.77 ? 178 VAL A CG2 1 
ATOM   1459 N  N   . ARG A 1 179 ? -9.971  14.486  26.098  1.00 21.72 ? 179 ARG A N   1 
ATOM   1460 C  CA  . ARG A 1 179 ? -9.760  14.774  27.546  1.00 22.99 ? 179 ARG A CA  1 
ATOM   1461 C  C   . ARG A 1 179 ? -8.701  15.885  27.733  1.00 21.78 ? 179 ARG A C   1 
ATOM   1462 O  O   . ARG A 1 179 ? -8.823  16.711  28.665  1.00 21.89 ? 179 ARG A O   1 
ATOM   1463 C  CB  . ARG A 1 179 ? -9.415  13.470  28.263  1.00 23.82 ? 179 ARG A CB  1 
ATOM   1464 C  CG  . ARG A 1 179 ? -9.603  13.533  29.773  1.00 25.95 ? 179 ARG A CG  1 
ATOM   1465 C  CD  . ARG A 1 179 ? -9.745  12.135  30.361  1.00 27.46 ? 179 ARG A CD  1 
ATOM   1466 N  NE  . ARG A 1 179 ? -8.630  11.263  29.996  1.00 27.87 ? 179 ARG A NE  1 
ATOM   1467 C  CZ  . ARG A 1 179 ? -8.715  9.951   29.773  1.00 30.51 ? 179 ARG A CZ  1 
ATOM   1468 N  NH1 . ARG A 1 179 ? -9.859  9.291   29.891  1.00 31.79 ? 179 ARG A NH1 1 
ATOM   1469 N  NH2 . ARG A 1 179 ? -7.633  9.288   29.431  1.00 29.86 ? 179 ARG A NH2 1 
ATOM   1470 N  N   . ALA A 1 180 ? -7.731  15.986  26.836  1.00 21.48 ? 180 ALA A N   1 
ATOM   1471 C  CA  . ALA A 1 180 ? -6.665  17.014  26.894  1.00 20.94 ? 180 ALA A CA  1 
ATOM   1472 C  C   . ALA A 1 180 ? -7.229  18.363  26.450  1.00 20.88 ? 180 ALA A C   1 
ATOM   1473 O  O   . ALA A 1 180 ? -6.926  19.403  27.071  1.00 19.32 ? 180 ALA A O   1 
ATOM   1474 C  CB  . ALA A 1 180 ? -5.523  16.601  25.996  1.00 21.43 ? 180 ALA A CB  1 
ATOM   1475 N  N   . LEU A 1 181 ? -7.983  18.343  25.352  1.00 21.06 ? 181 LEU A N   1 
ATOM   1476 C  CA  . LEU A 1 181 ? -8.735  19.534  24.895  1.00 20.85 ? 181 LEU A CA  1 
ATOM   1477 C  C   . LEU A 1 181 ? -9.682  20.013  26.007  1.00 21.01 ? 181 LEU A C   1 
ATOM   1478 O  O   . LEU A 1 181 ? -9.731  21.217  26.202  1.00 19.27 ? 181 LEU A O   1 
ATOM   1479 C  CB  . LEU A 1 181 ? -9.491  19.185  23.622  1.00 20.19 ? 181 LEU A CB  1 
ATOM   1480 C  CG  . LEU A 1 181 ? -8.692  19.296  22.339  1.00 22.06 ? 181 LEU A CG  1 
ATOM   1481 C  CD1 . LEU A 1 181 ? -9.620  19.006  21.172  1.00 24.47 ? 181 LEU A CD1 1 
ATOM   1482 C  CD2 . LEU A 1 181 ? -8.037  20.674  22.185  1.00 22.49 ? 181 LEU A CD2 1 
ATOM   1483 N  N   . ASP A 1 182 ? -10.351 19.104  26.731  1.00 23.08 ? 182 ASP A N   1 
ATOM   1484 C  CA  . ASP A 1 182 ? -11.312 19.467  27.804  1.00 26.14 ? 182 ASP A CA  1 
ATOM   1485 C  C   . ASP A 1 182 ? -10.530 20.195  28.894  1.00 25.52 ? 182 ASP A C   1 
ATOM   1486 O  O   . ASP A 1 182 ? -10.952 21.279  29.263  1.00 25.91 ? 182 ASP A O   1 
ATOM   1487 C  CB  . ASP A 1 182 ? -12.118 18.259  28.302  1.00 29.14 ? 182 ASP A CB  1 
ATOM   1488 C  CG  . ASP A 1 182 ? -13.319 18.602  29.186  1.00 34.88 ? 182 ASP A CG  1 
ATOM   1489 O  OD1 . ASP A 1 182 ? -13.905 19.676  29.005  1.00 38.24 ? 182 ASP A OD1 1 
ATOM   1490 O  OD2 . ASP A 1 182 ? -13.662 17.798  30.081  1.00 44.16 ? 182 ASP A OD2 1 
ATOM   1491 N  N   . GLU A 1 183 ? -9.409  19.625  29.338  1.00 27.89 ? 183 GLU A N   1 
ATOM   1492 C  CA  . GLU A 1 183 ? -8.545  20.133  30.450  1.00 27.94 ? 183 GLU A CA  1 
ATOM   1493 C  C   . GLU A 1 183 ? -7.910  21.472  30.052  1.00 26.70 ? 183 GLU A C   1 
ATOM   1494 O  O   . GLU A 1 183 ? -7.934  22.421  30.861  1.00 23.85 ? 183 GLU A O   1 
ATOM   1495 C  CB  . GLU A 1 183 ? -7.477  19.081  30.787  1.00 28.58 ? 183 GLU A CB  1 
ATOM   1496 C  CG  . GLU A 1 183 ? -6.458  19.510  31.836  1.00 29.13 ? 183 GLU A CG  1 
ATOM   1497 C  CD  . GLU A 1 183 ? -7.013  19.887  33.200  1.00 29.19 ? 183 GLU A CD  1 
ATOM   1498 O  OE1 . GLU A 1 183 ? -8.102  19.373  33.574  1.00 29.30 ? 183 GLU A OE1 1 
ATOM   1499 O  OE2 . GLU A 1 183 ? -6.362  20.710  33.882  1.00 28.19 ? 183 GLU A OE2 1 
ATOM   1500 N  N   . ALA A 1 184 ? -7.376  21.550  28.833  1.00 27.25 ? 184 ALA A N   1 
ATOM   1501 C  CA  . ALA A 1 184 ? -6.863  22.804  28.232  1.00 27.62 ? 184 ALA A CA  1 
ATOM   1502 C  C   . ALA A 1 184 ? -7.928  23.912  28.313  1.00 26.97 ? 184 ALA A C   1 
ATOM   1503 O  O   . ALA A 1 184 ? -7.621  25.037  28.720  1.00 25.43 ? 184 ALA A O   1 
ATOM   1504 C  CB  . ALA A 1 184 ? -6.453  22.527  26.808  1.00 28.49 ? 184 ALA A CB  1 
ATOM   1505 N  N   . MET A 1 185 ? -9.162  23.601  27.941  1.00 28.76 ? 185 MET A N   1 
ATOM   1506 C  CA  . MET A 1 185 ? -10.259 24.598  27.851  1.00 32.26 ? 185 MET A CA  1 
ATOM   1507 C  C   . MET A 1 185 ? -10.781 24.940  29.252  1.00 31.49 ? 185 MET A C   1 
ATOM   1508 O  O   . MET A 1 185 ? -11.389 26.008  29.397  1.00 31.25 ? 185 MET A O   1 
ATOM   1509 C  CB  . MET A 1 185 ? -11.417 24.061  27.005  1.00 35.67 ? 185 MET A CB  1 
ATOM   1510 C  CG  . MET A 1 185 ? -11.754 24.940  25.838  1.00 43.20 ? 185 MET A CG  1 
ATOM   1511 S  SD  . MET A 1 185 ? -11.051 24.338  24.297  1.00 53.41 ? 185 MET A SD  1 
ATOM   1512 C  CE  . MET A 1 185 ? -9.323  24.177  24.729  1.00 54.53 ? 185 MET A CE  1 
ATOM   1513 N  N   . ASN A 1 186 ? -10.582 24.065  30.239  1.00 31.08 ? 186 ASN A N   1 
ATOM   1514 C  CA  . ASN A 1 186 ? -11.128 24.271  31.606  1.00 33.65 ? 186 ASN A CA  1 
ATOM   1515 C  C   . ASN A 1 186 ? -10.112 24.976  32.508  1.00 33.61 ? 186 ASN A C   1 
ATOM   1516 O  O   . ASN A 1 186 ? -10.567 25.534  33.515  1.00 30.94 ? 186 ASN A O   1 
ATOM   1517 C  CB  . ASN A 1 186 ? -11.557 22.962  32.265  1.00 34.56 ? 186 ASN A CB  1 
ATOM   1518 C  CG  . ASN A 1 186 ? -12.960 22.535  31.904  1.00 36.64 ? 186 ASN A CG  1 
ATOM   1519 O  OD1 . ASN A 1 186 ? -13.763 23.321  31.406  1.00 33.14 ? 186 ASN A OD1 1 
ATOM   1520 N  ND2 . ASN A 1 186 ? -13.257 21.275  32.172  1.00 42.48 ? 186 ASN A ND2 1 
ATOM   1521 N  N   . LYS A 1 187 ? -8.803  24.884  32.210  1.00 32.58 ? 187 LYS A N   1 
ATOM   1522 C  CA  . LYS A 1 187 ? -7.721  25.407  33.098  1.00 30.55 ? 187 LYS A CA  1 
ATOM   1523 C  C   . LYS A 1 187 ? -7.937  26.903  33.337  1.00 29.10 ? 187 LYS A C   1 
ATOM   1524 O  O   . LYS A 1 187 ? -7.934  27.320  34.491  1.00 26.56 ? 187 LYS A O   1 
ATOM   1525 C  CB  . LYS A 1 187 ? -6.318  25.143  32.534  1.00 32.69 ? 187 LYS A CB  1 
ATOM   1526 C  CG  . LYS A 1 187 ? -5.683  23.790  32.876  1.00 35.40 ? 187 LYS A CG  1 
ATOM   1527 C  CD  . LYS A 1 187 ? -4.262  23.611  32.310  1.00 36.06 ? 187 LYS A CD  1 
ATOM   1528 C  CE  . LYS A 1 187 ? -3.775  22.172  32.197  1.00 35.89 ? 187 LYS A CE  1 
ATOM   1529 N  NZ  . LYS A 1 187 ? -3.593  21.523  33.525  1.00 35.31 ? 187 LYS A NZ  1 
ATOM   1530 N  N   . PRO A 1 188 ? -8.157  27.749  32.291  1.00 26.36 ? 188 PRO A N   1 
ATOM   1531 C  CA  . PRO A 1 188 ? -8.160  29.201  32.463  1.00 26.09 ? 188 PRO A CA  1 
ATOM   1532 C  C   . PRO A 1 188 ? -9.240  29.744  33.412  1.00 29.97 ? 188 PRO A C   1 
ATOM   1533 O  O   . PRO A 1 188 ? -9.100  30.907  33.818  1.00 34.87 ? 188 PRO A O   1 
ATOM   1534 C  CB  . PRO A 1 188 ? -8.421  29.768  31.055  1.00 25.08 ? 188 PRO A CB  1 
ATOM   1535 C  CG  . PRO A 1 188 ? -8.044  28.630  30.119  1.00 24.85 ? 188 PRO A CG  1 
ATOM   1536 C  CD  . PRO A 1 188 ? -8.394  27.372  30.885  1.00 25.68 ? 188 PRO A CD  1 
ATOM   1537 N  N   . GLN A 1 189 ? -10.252 28.941  33.763  1.00 28.19 ? 189 GLN A N   1 
ATOM   1538 C  CA  . GLN A 1 189 ? -11.383 29.405  34.615  1.00 31.55 ? 189 GLN A CA  1 
ATOM   1539 C  C   . GLN A 1 189 ? -11.071 29.179  36.108  1.00 30.59 ? 189 GLN A C   1 
ATOM   1540 O  O   . GLN A 1 189 ? -11.859 29.665  36.963  1.00 28.66 ? 189 GLN A O   1 
ATOM   1541 C  CB  . GLN A 1 189 ? -12.700 28.764  34.148  1.00 32.71 ? 189 GLN A CB  1 
ATOM   1542 C  CG  . GLN A 1 189 ? -13.042 27.445  34.827  1.00 33.41 ? 189 GLN A CG  1 
ATOM   1543 C  CD  . GLN A 1 189 ? -14.125 26.674  34.109  1.00 35.91 ? 189 GLN A CD  1 
ATOM   1544 O  OE1 . GLN A 1 189 ? -14.181 26.587  32.880  1.00 29.56 ? 189 GLN A OE1 1 
ATOM   1545 N  NE2 . GLN A 1 189 ? -15.014 26.100  34.901  1.00 40.32 ? 189 GLN A NE2 1 
ATOM   1546 N  N   . ARG A 1 190 ? -9.956  28.521  36.438  1.00 31.32 ? 190 ARG A N   1 
ATOM   1547 C  CA  . ARG A 1 190 ? -9.569  28.220  37.850  1.00 31.32 ? 190 ARG A CA  1 
ATOM   1548 C  C   . ARG A 1 190 ? -8.886  29.432  38.496  1.00 31.26 ? 190 ARG A C   1 
ATOM   1549 O  O   . ARG A 1 190 ? -7.791  29.811  38.042  1.00 31.16 ? 190 ARG A O   1 
ATOM   1550 C  CB  . ARG A 1 190 ? -8.655  27.000  37.918  1.00 29.62 ? 190 ARG A CB  1 
ATOM   1551 C  CG  . ARG A 1 190 ? -9.278  25.773  37.276  1.00 30.45 ? 190 ARG A CG  1 
ATOM   1552 C  CD  . ARG A 1 190 ? -8.297  24.643  37.088  1.00 29.47 ? 190 ARG A CD  1 
ATOM   1553 N  NE  . ARG A 1 190 ? -9.006  23.567  36.427  1.00 30.75 ? 190 ARG A NE  1 
ATOM   1554 C  CZ  . ARG A 1 190 ? -8.440  22.511  35.871  1.00 30.60 ? 190 ARG A CZ  1 
ATOM   1555 N  NH1 . ARG A 1 190 ? -7.129  22.340  35.895  1.00 26.87 ? 190 ARG A NH1 1 
ATOM   1556 N  NH2 . ARG A 1 190 ? -9.210  21.620  35.279  1.00 34.00 ? 190 ARG A NH2 1 
ATOM   1557 N  N   . ALA A 1 191 ? -9.518  29.992  39.535  1.00 31.12 ? 191 ALA A N   1 
ATOM   1558 C  CA  . ALA A 1 191 ? -8.945  31.051  40.388  1.00 32.90 ? 191 ALA A CA  1 
ATOM   1559 C  C   . ALA A 1 191 ? -7.580  30.588  40.878  1.00 32.96 ? 191 ALA A C   1 
ATOM   1560 O  O   . ALA A 1 191 ? -6.652  31.357  40.717  1.00 32.63 ? 191 ALA A O   1 
ATOM   1561 C  CB  . ALA A 1 191 ? -9.850  31.350  41.552  1.00 34.96 ? 191 ALA A CB  1 
ATOM   1562 N  N   . ASN A 1 192 ? -7.481  29.377  41.454  1.00 36.69 ? 192 ASN A N   1 
ATOM   1563 C  CA  . ASN A 1 192 ? -6.193  28.814  41.972  1.00 36.00 ? 192 ASN A CA  1 
ATOM   1564 C  C   . ASN A 1 192 ? -5.814  27.539  41.222  1.00 35.72 ? 192 ASN A C   1 
ATOM   1565 O  O   . ASN A 1 192 ? -6.046  26.426  41.727  1.00 35.52 ? 192 ASN A O   1 
ATOM   1566 C  CB  . ASN A 1 192 ? -6.197  28.512  43.472  1.00 33.41 ? 192 ASN A CB  1 
ATOM   1567 C  CG  . ASN A 1 192 ? -4.807  28.162  43.977  1.00 37.67 ? 192 ASN A CG  1 
ATOM   1568 O  OD1 . ASN A 1 192 ? -3.812  28.206  43.228  1.00 33.31 ? 192 ASN A OD1 1 
ATOM   1569 N  ND2 . ASN A 1 192 ? -4.721  27.848  45.263  1.00 38.56 ? 192 ASN A ND2 1 
ATOM   1570 N  N   . PRO A 1 193 ? -5.158  27.668  40.042  1.00 32.97 ? 193 PRO A N   1 
ATOM   1571 C  CA  . PRO A 1 193 ? -4.725  26.506  39.264  1.00 34.94 ? 193 PRO A CA  1 
ATOM   1572 C  C   . PRO A 1 193 ? -3.997  25.463  40.123  1.00 35.16 ? 193 PRO A C   1 
ATOM   1573 O  O   . PRO A 1 193 ? -4.156  24.306  39.840  1.00 32.80 ? 193 PRO A O   1 
ATOM   1574 C  CB  . PRO A 1 193 ? -3.773  27.066  38.192  1.00 34.65 ? 193 PRO A CB  1 
ATOM   1575 C  CG  . PRO A 1 193 ? -4.162  28.533  38.075  1.00 33.92 ? 193 PRO A CG  1 
ATOM   1576 C  CD  . PRO A 1 193 ? -4.793  28.936  39.395  1.00 32.67 ? 193 PRO A CD  1 
ATOM   1577 N  N   . ASP A 1 194 ? -3.270  25.891  41.163  1.00 36.97 ? 194 ASP A N   1 
ATOM   1578 C  CA  . ASP A 1 194 ? -2.362  25.005  41.948  1.00 40.10 ? 194 ASP A CA  1 
ATOM   1579 C  C   . ASP A 1 194 ? -3.053  24.431  43.206  1.00 39.91 ? 194 ASP A C   1 
ATOM   1580 O  O   . ASP A 1 194 ? -2.325  23.964  44.096  1.00 42.05 ? 194 ASP A O   1 
ATOM   1581 C  CB  . ASP A 1 194 ? -1.054  25.745  42.258  1.00 42.03 ? 194 ASP A CB  1 
ATOM   1582 C  CG  . ASP A 1 194 ? -0.382  26.350  41.023  1.00 44.31 ? 194 ASP A CG  1 
ATOM   1583 O  OD1 . ASP A 1 194 ? -0.202  25.605  40.016  1.00 41.38 ? 194 ASP A OD1 1 
ATOM   1584 O  OD2 . ASP A 1 194 ? -0.054  27.573  41.069  1.00 42.18 ? 194 ASP A OD2 1 
ATOM   1585 N  N   . ASP A 1 195 ? -4.387  24.356  43.276  1.00 38.41 ? 195 ASP A N   1 
ATOM   1586 C  CA  . ASP A 1 195 ? -5.095  23.648  44.385  1.00 40.74 ? 195 ASP A CA  1 
ATOM   1587 C  C   . ASP A 1 195 ? -4.962  22.137  44.171  1.00 42.76 ? 195 ASP A C   1 
ATOM   1588 O  O   . ASP A 1 195 ? -5.024  21.679  43.031  1.00 47.23 ? 195 ASP A O   1 
ATOM   1589 C  CB  . ASP A 1 195 ? -6.540  24.143  44.507  1.00 39.94 ? 195 ASP A CB  1 
ATOM   1590 C  CG  . ASP A 1 195 ? -7.436  23.382  45.473  1.00 38.46 ? 195 ASP A CG  1 
ATOM   1591 O  OD1 . ASP A 1 195 ? -7.218  22.183  45.676  1.00 43.71 ? 195 ASP A OD1 1 
ATOM   1592 O  OD2 . ASP A 1 195 ? -8.375  23.986  45.981  1.00 37.29 ? 195 ASP A OD2 1 
ATOM   1593 N  N   . PRO A 1 196 ? -4.699  21.327  45.237  1.00 45.56 ? 196 PRO A N   1 
ATOM   1594 C  CA  . PRO A 1 196 ? -4.666  19.860  45.146  1.00 41.55 ? 196 PRO A CA  1 
ATOM   1595 C  C   . PRO A 1 196 ? -5.911  19.170  44.572  1.00 41.29 ? 196 PRO A C   1 
ATOM   1596 O  O   . PRO A 1 196 ? -5.842  17.957  44.325  1.00 39.44 ? 196 PRO A O   1 
ATOM   1597 C  CB  . PRO A 1 196 ? -4.546  19.385  46.607  1.00 43.50 ? 196 PRO A CB  1 
ATOM   1598 C  CG  . PRO A 1 196 ? -3.865  20.532  47.322  1.00 46.03 ? 196 PRO A CG  1 
ATOM   1599 C  CD  . PRO A 1 196 ? -4.301  21.787  46.584  1.00 46.59 ? 196 PRO A CD  1 
ATOM   1600 N  N   . ALA A 1 197 ? -7.016  19.913  44.423  1.00 35.23 ? 197 ALA A N   1 
ATOM   1601 C  CA  . ALA A 1 197 ? -8.246  19.441  43.760  1.00 34.55 ? 197 ALA A CA  1 
ATOM   1602 C  C   . ALA A 1 197 ? -8.063  19.437  42.239  1.00 34.75 ? 197 ALA A C   1 
ATOM   1603 O  O   . ALA A 1 197 ? -9.047  19.108  41.569  1.00 38.04 ? 197 ALA A O   1 
ATOM   1604 C  CB  . ALA A 1 197 ? -9.429  20.283  44.162  1.00 34.79 ? 197 ALA A CB  1 
ATOM   1605 N  N   . TYR A 1 198 ? -6.888  19.807  41.707  1.00 35.39 ? 198 TYR A N   1 
ATOM   1606 C  CA  . TYR A 1 198 ? -6.578  19.773  40.247  1.00 37.14 ? 198 TYR A CA  1 
ATOM   1607 C  C   . TYR A 1 198 ? -5.319  18.943  39.971  1.00 38.79 ? 198 TYR A C   1 
ATOM   1608 O  O   . TYR A 1 198 ? -4.790  18.956  38.813  1.00 34.10 ? 198 TYR A O   1 
ATOM   1609 C  CB  . TYR A 1 198 ? -6.388  21.174  39.663  1.00 34.60 ? 198 TYR A CB  1 
ATOM   1610 C  CG  . TYR A 1 198 ? -7.537  22.123  39.873  1.00 33.82 ? 198 TYR A CG  1 
ATOM   1611 C  CD1 . TYR A 1 198 ? -8.780  21.907  39.291  1.00 33.19 ? 198 TYR A CD1 1 
ATOM   1612 C  CD2 . TYR A 1 198 ? -7.364  23.261  40.642  1.00 34.31 ? 198 TYR A CD2 1 
ATOM   1613 C  CE1 . TYR A 1 198 ? -9.832  22.792  39.479  1.00 32.06 ? 198 TYR A CE1 1 
ATOM   1614 C  CE2 . TYR A 1 198 ? -8.406  24.150  40.843  1.00 36.70 ? 198 TYR A CE2 1 
ATOM   1615 C  CZ  . TYR A 1 198 ? -9.640  23.915  40.263  1.00 32.53 ? 198 TYR A CZ  1 
ATOM   1616 O  OH  . TYR A 1 198 ? -10.615 24.832  40.478  1.00 29.84 ? 198 TYR A OH  1 
ATOM   1617 N  N   . ASP A 1 199 ? -4.861  18.217  40.988  1.00 39.47 ? 199 ASP A N   1 
ATOM   1618 C  CA  . ASP A 1 199 ? -3.645  17.374  40.878  1.00 42.34 ? 199 ASP A CA  1 
ATOM   1619 C  C   . ASP A 1 199 ? -3.989  16.124  40.054  1.00 38.25 ? 199 ASP A C   1 
ATOM   1620 O  O   . ASP A 1 199 ? -3.121  15.666  39.289  1.00 37.57 ? 199 ASP A O   1 
ATOM   1621 C  CB  . ASP A 1 199 ? -3.028  17.146  42.264  1.00 45.57 ? 199 ASP A CB  1 
ATOM   1622 C  CG  . ASP A 1 199 ? -2.037  18.243  42.648  1.00 48.00 ? 199 ASP A CG  1 
ATOM   1623 O  OD1 . ASP A 1 199 ? -2.316  19.444  42.363  1.00 51.83 ? 199 ASP A OD1 1 
ATOM   1624 O  OD2 . ASP A 1 199 ? -0.975  17.893  43.187  1.00 52.34 ? 199 ASP A OD2 1 
ATOM   1625 N  N   . GLU A 1 200 ? -5.213  15.614  40.157  1.00 36.24 ? 200 GLU A N   1 
ATOM   1626 C  CA  . GLU A 1 200 ? -5.656  14.417  39.391  1.00 38.54 ? 200 GLU A CA  1 
ATOM   1627 C  C   . GLU A 1 200 ? -5.799  14.853  37.919  1.00 32.16 ? 200 GLU A C   1 
ATOM   1628 O  O   . GLU A 1 200 ? -5.286  14.146  37.057  1.00 26.40 ? 200 GLU A O   1 
ATOM   1629 C  CB  . GLU A 1 200 ? -6.865  13.773  40.097  1.00 41.75 ? 200 GLU A CB  1 
ATOM   1630 C  CG  . GLU A 1 200 ? -8.065  13.417  39.216  1.00 51.42 ? 200 GLU A CG  1 
ATOM   1631 C  CD  . GLU A 1 200 ? -9.440  13.457  39.901  1.00 58.35 ? 200 GLU A CD  1 
ATOM   1632 O  OE1 . GLU A 1 200 ? -10.210 12.474  39.770  1.00 56.89 ? 200 GLU A OE1 1 
ATOM   1633 O  OE2 . GLU A 1 200 ? -9.767  14.489  40.544  1.00 65.15 ? 200 GLU A OE2 1 
ATOM   1634 N  N   . ASN A 1 201 ? -6.399  16.018  37.662  1.00 31.24 ? 201 ASN A N   1 
ATOM   1635 C  CA  . ASN A 1 201 ? -6.528  16.623  36.303  1.00 31.15 ? 201 ASN A CA  1 
ATOM   1636 C  C   . ASN A 1 201 ? -5.137  16.840  35.697  1.00 30.41 ? 201 ASN A C   1 
ATOM   1637 O  O   . ASN A 1 201 ? -4.951  16.547  34.492  1.00 31.34 ? 201 ASN A O   1 
ATOM   1638 C  CB  . ASN A 1 201 ? -7.233  17.984  36.299  1.00 29.64 ? 201 ASN A CB  1 
ATOM   1639 C  CG  . ASN A 1 201 ? -8.586  18.002  36.973  1.00 29.86 ? 201 ASN A CG  1 
ATOM   1640 O  OD1 . ASN A 1 201 ? -8.682  17.864  38.178  1.00 29.28 ? 201 ASN A OD1 1 
ATOM   1641 N  ND2 . ASN A 1 201 ? -9.637  18.233  36.213  1.00 31.89 ? 201 ASN A ND2 1 
ATOM   1642 N  N   . LYS A 1 202 ? -4.199  17.337  36.503  1.00 31.23 ? 202 LYS A N   1 
ATOM   1643 C  CA  . LYS A 1 202 ? -2.795  17.562  36.078  1.00 33.49 ? 202 LYS A CA  1 
ATOM   1644 C  C   . LYS A 1 202 ? -2.173  16.207  35.715  1.00 33.63 ? 202 LYS A C   1 
ATOM   1645 O  O   . LYS A 1 202 ? -1.589  16.106  34.618  1.00 37.34 ? 202 LYS A O   1 
ATOM   1646 C  CB  . LYS A 1 202 ? -2.015  18.317  37.157  1.00 34.83 ? 202 LYS A CB  1 
ATOM   1647 C  CG  . LYS A 1 202 ? -2.339  19.804  37.257  1.00 35.90 ? 202 LYS A CG  1 
ATOM   1648 C  CD  . LYS A 1 202 ? -1.584  20.554  38.358  1.00 36.61 ? 202 LYS A CD  1 
ATOM   1649 C  CE  . LYS A 1 202 ? -2.282  21.835  38.793  1.00 37.34 ? 202 LYS A CE  1 
ATOM   1650 N  NZ  . LYS A 1 202 ? -1.411  23.036  38.709  1.00 36.01 ? 202 LYS A NZ  1 
ATOM   1651 N  N   . ARG A 1 203 ? -2.343  15.186  36.554  1.00 31.93 ? 203 ARG A N   1 
ATOM   1652 C  CA  . ARG A 1 203 ? -1.771  13.836  36.293  1.00 32.50 ? 203 ARG A CA  1 
ATOM   1653 C  C   . ARG A 1 203 ? -2.360  13.316  34.980  1.00 27.53 ? 203 ARG A C   1 
ATOM   1654 O  O   . ARG A 1 203 ? -1.599  12.957  34.114  1.00 25.53 ? 203 ARG A O   1 
ATOM   1655 C  CB  . ARG A 1 203 ? -2.027  12.883  37.470  1.00 36.14 ? 203 ARG A CB  1 
ATOM   1656 C  CG  . ARG A 1 203 ? -0.767  12.277  38.072  1.00 39.84 ? 203 ARG A CG  1 
ATOM   1657 C  CD  . ARG A 1 203 ? -0.640  12.566  39.559  1.00 43.14 ? 203 ARG A CD  1 
ATOM   1658 N  NE  . ARG A 1 203 ? -1.839  12.140  40.275  1.00 48.98 ? 203 ARG A NE  1 
ATOM   1659 C  CZ  . ARG A 1 203 ? -2.363  12.732  41.363  1.00 50.23 ? 203 ARG A CZ  1 
ATOM   1660 N  NH1 . ARG A 1 203 ? -1.797  13.805  41.899  1.00 46.27 ? 203 ARG A NH1 1 
ATOM   1661 N  NH2 . ARG A 1 203 ? -3.486  12.259  41.890  1.00 49.81 ? 203 ARG A NH2 1 
ATOM   1662 N  N   . GLN A 1 204 ? -3.679  13.338  34.838  1.00 26.79 ? 204 GLN A N   1 
ATOM   1663 C  CA  . GLN A 1 204 ? -4.422  12.774  33.677  1.00 27.76 ? 204 GLN A CA  1 
ATOM   1664 C  C   . GLN A 1 204 ? -4.001  13.470  32.371  1.00 28.12 ? 204 GLN A C   1 
ATOM   1665 O  O   . GLN A 1 204 ? -3.939  12.805  31.308  1.00 27.03 ? 204 GLN A O   1 
ATOM   1666 C  CB  . GLN A 1 204 ? -5.917  12.949  33.943  1.00 30.31 ? 204 GLN A CB  1 
ATOM   1667 C  CG  . GLN A 1 204 ? -6.811  12.420  32.837  1.00 31.96 ? 204 GLN A CG  1 
ATOM   1668 C  CD  . GLN A 1 204 ? -6.422  11.008  32.481  1.00 33.03 ? 204 GLN A CD  1 
ATOM   1669 O  OE1 . GLN A 1 204 ? -5.746  10.777  31.485  1.00 37.97 ? 204 GLN A OE1 1 
ATOM   1670 N  NE2 . GLN A 1 204 ? -6.794  10.061  33.323  1.00 31.74 ? 204 GLN A NE2 1 
ATOM   1671 N  N   . PHE A 1 205 ? -3.741  14.775  32.440  1.00 28.03 ? 205 PHE A N   1 
ATOM   1672 C  CA  . PHE A 1 205 ? -3.301  15.619  31.302  1.00 26.86 ? 205 PHE A CA  1 
ATOM   1673 C  C   . PHE A 1 205 ? -1.911  15.168  30.847  1.00 31.83 ? 205 PHE A C   1 
ATOM   1674 O  O   . PHE A 1 205 ? -1.707  14.910  29.625  1.00 33.90 ? 205 PHE A O   1 
ATOM   1675 C  CB  . PHE A 1 205 ? -3.311  17.074  31.748  1.00 26.02 ? 205 PHE A CB  1 
ATOM   1676 C  CG  . PHE A 1 205 ? -3.132  18.080  30.656  1.00 24.02 ? 205 PHE A CG  1 
ATOM   1677 C  CD1 . PHE A 1 205 ? -3.992  18.094  29.576  1.00 23.72 ? 205 PHE A CD1 1 
ATOM   1678 C  CD2 . PHE A 1 205 ? -2.126  19.026  30.727  1.00 24.43 ? 205 PHE A CD2 1 
ATOM   1679 C  CE1 . PHE A 1 205 ? -3.839  19.027  28.567  1.00 24.03 ? 205 PHE A CE1 1 
ATOM   1680 C  CE2 . PHE A 1 205 ? -1.987  19.975  29.724  1.00 27.08 ? 205 PHE A CE2 1 
ATOM   1681 C  CZ  . PHE A 1 205 ? -2.846  19.979  28.648  1.00 24.57 ? 205 PHE A CZ  1 
ATOM   1682 N  N   . GLN A 1 206 ? -0.965  15.071  31.788  1.00 31.87 ? 206 GLN A N   1 
ATOM   1683 C  CA  . GLN A 1 206 ? 0.401   14.584  31.464  1.00 34.31 ? 206 GLN A CA  1 
ATOM   1684 C  C   . GLN A 1 206 ? 0.271   13.215  30.775  1.00 31.40 ? 206 GLN A C   1 
ATOM   1685 O  O   . GLN A 1 206 ? 0.881   13.069  29.731  1.00 28.20 ? 206 GLN A O   1 
ATOM   1686 C  CB  . GLN A 1 206 ? 1.324   14.470  32.685  1.00 39.68 ? 206 GLN A CB  1 
ATOM   1687 C  CG  . GLN A 1 206 ? 1.431   15.704  33.586  1.00 45.42 ? 206 GLN A CG  1 
ATOM   1688 C  CD  . GLN A 1 206 ? 1.408   17.048  32.892  1.00 52.60 ? 206 GLN A CD  1 
ATOM   1689 O  OE1 . GLN A 1 206 ? 0.775   17.990  33.369  1.00 57.04 ? 206 GLN A OE1 1 
ATOM   1690 N  NE2 . GLN A 1 206 ? 2.125   17.163  31.782  1.00 54.30 ? 206 GLN A NE2 1 
ATOM   1691 N  N   . GLU A 1 207 ? -0.517  12.284  31.326  1.00 28.96 ? 207 GLU A N   1 
ATOM   1692 C  CA  . GLU A 1 207 ? -0.723  10.913  30.774  1.00 34.34 ? 207 GLU A CA  1 
ATOM   1693 C  C   . GLU A 1 207 ? -1.266  10.998  29.341  1.00 32.61 ? 207 GLU A C   1 
ATOM   1694 O  O   . GLU A 1 207 ? -0.750  10.269  28.447  1.00 30.08 ? 207 GLU A O   1 
ATOM   1695 C  CB  . GLU A 1 207 ? -1.647  10.077  31.672  1.00 38.78 ? 207 GLU A CB  1 
ATOM   1696 C  CG  . GLU A 1 207 ? -0.890  9.337   32.779  1.00 47.95 ? 207 GLU A CG  1 
ATOM   1697 C  CD  . GLU A 1 207 ? -1.676  8.877   34.008  1.00 56.39 ? 207 GLU A CD  1 
ATOM   1698 O  OE1 . GLU A 1 207 ? -1.069  8.797   35.116  1.00 58.85 ? 207 GLU A OE1 1 
ATOM   1699 O  OE2 . GLU A 1 207 ? -2.884  8.586   33.871  1.00 61.95 ? 207 GLU A OE2 1 
ATOM   1700 N  N   . ASP A 1 208 ? -2.250  11.873  29.130  1.00 31.33 ? 208 ASP A N   1 
ATOM   1701 C  CA  . ASP A 1 208 ? -2.949  12.046  27.835  1.00 29.26 ? 208 ASP A CA  1 
ATOM   1702 C  C   . ASP A 1 208 ? -1.970  12.631  26.804  1.00 29.45 ? 208 ASP A C   1 
ATOM   1703 O  O   . ASP A 1 208 ? -1.993  12.173  25.608  1.00 26.86 ? 208 ASP A O   1 
ATOM   1704 C  CB  . ASP A 1 208 ? -4.215  12.874  28.037  1.00 28.55 ? 208 ASP A CB  1 
ATOM   1705 C  CG  . ASP A 1 208 ? -5.394  12.075  28.582  1.00 29.41 ? 208 ASP A CG  1 
ATOM   1706 O  OD1 . ASP A 1 208 ? -5.400  10.845  28.395  1.00 29.74 ? 208 ASP A OD1 1 
ATOM   1707 O  OD2 . ASP A 1 208 ? -6.314  12.693  29.176  1.00 27.78 ? 208 ASP A OD2 1 
ATOM   1708 N  N   . ILE A 1 209 ? -1.134  13.586  27.226  1.00 25.85 ? 209 ILE A N   1 
ATOM   1709 C  CA  . ILE A 1 209 ? -0.052  14.129  26.359  1.00 26.61 ? 209 ILE A CA  1 
ATOM   1710 C  C   . ILE A 1 209 ? 0.872   12.985  25.907  1.00 27.77 ? 209 ILE A C   1 
ATOM   1711 O  O   . ILE A 1 209 ? 1.173   12.911  24.705  1.00 27.51 ? 209 ILE A O   1 
ATOM   1712 C  CB  . ILE A 1 209 ? 0.726   15.236  27.080  1.00 26.05 ? 209 ILE A CB  1 
ATOM   1713 C  CG1 . ILE A 1 209 ? -0.130  16.495  27.250  1.00 25.45 ? 209 ILE A CG1 1 
ATOM   1714 C  CG2 . ILE A 1 209 ? 2.021   15.516  26.333  1.00 26.93 ? 209 ILE A CG2 1 
ATOM   1715 C  CD1 . ILE A 1 209 ? 0.498   17.559  28.119  1.00 23.65 ? 209 ILE A CD1 1 
ATOM   1716 N  N   . LYS A 1 210 ? 1.303   12.138  26.841  1.00 29.29 ? 210 LYS A N   1 
ATOM   1717 C  CA  . LYS A 1 210 ? 2.255   11.018  26.614  1.00 33.13 ? 210 LYS A CA  1 
ATOM   1718 C  C   . LYS A 1 210 ? 1.628   10.002  25.658  1.00 30.17 ? 210 LYS A C   1 
ATOM   1719 O  O   . LYS A 1 210 ? 2.333   9.498   24.775  1.00 28.29 ? 210 LYS A O   1 
ATOM   1720 C  CB  . LYS A 1 210 ? 2.639   10.352  27.941  1.00 38.04 ? 210 LYS A CB  1 
ATOM   1721 C  CG  . LYS A 1 210 ? 3.950   10.829  28.580  1.00 47.27 ? 210 LYS A CG  1 
ATOM   1722 C  CD  . LYS A 1 210 ? 4.412   12.262  28.231  1.00 54.35 ? 210 LYS A CD  1 
ATOM   1723 C  CE  . LYS A 1 210 ? 5.235   12.956  29.306  1.00 52.79 ? 210 LYS A CE  1 
ATOM   1724 N  NZ  . LYS A 1 210 ? 4.579   14.214  29.744  1.00 53.05 ? 210 LYS A NZ  1 
ATOM   1725 N  N   . VAL A 1 211 ? 0.350   9.701   25.860  1.00 28.95 ? 211 VAL A N   1 
ATOM   1726 C  CA  . VAL A 1 211 ? -0.399  8.719   25.042  1.00 27.49 ? 211 VAL A CA  1 
ATOM   1727 C  C   . VAL A 1 211 ? -0.390  9.230   23.591  1.00 28.70 ? 211 VAL A C   1 
ATOM   1728 O  O   . VAL A 1 211 ? -0.031  8.443   22.673  1.00 31.61 ? 211 VAL A O   1 
ATOM   1729 C  CB  . VAL A 1 211 ? -1.804  8.523   25.644  1.00 28.73 ? 211 VAL A CB  1 
ATOM   1730 C  CG1 . VAL A 1 211 ? -2.756  7.777   24.717  1.00 29.11 ? 211 VAL A CG1 1 
ATOM   1731 C  CG2 . VAL A 1 211 ? -1.723  7.821   26.990  1.00 28.43 ? 211 VAL A CG2 1 
ATOM   1732 N  N   . MET A 1 212 ? -0.695  10.515  23.392  1.00 25.55 ? 212 MET A N   1 
ATOM   1733 C  CA  . MET A 1 212 ? -0.808  11.131  22.046  1.00 23.42 ? 212 MET A CA  1 
ATOM   1734 C  C   . MET A 1 212 ? 0.564   11.101  21.362  1.00 23.62 ? 212 MET A C   1 
ATOM   1735 O  O   . MET A 1 212 ? 0.626   10.682  20.185  1.00 21.40 ? 212 MET A O   1 
ATOM   1736 C  CB  . MET A 1 212 ? -1.328  12.569  22.143  1.00 22.43 ? 212 MET A CB  1 
ATOM   1737 C  CG  . MET A 1 212 ? -2.840  12.670  22.319  1.00 21.89 ? 212 MET A CG  1 
ATOM   1738 S  SD  . MET A 1 212 ? -3.509  14.344  22.091  1.00 23.38 ? 212 MET A SD  1 
ATOM   1739 C  CE  . MET A 1 212 ? -3.259  15.075  23.709  1.00 21.10 ? 212 MET A CE  1 
ATOM   1740 N  N   . ASN A 1 213 ? 1.610   11.518  22.088  1.00 23.96 ? 213 ASN A N   1 
ATOM   1741 C  CA  . ASN A 1 213 ? 3.024   11.529  21.627  1.00 25.68 ? 213 ASN A CA  1 
ATOM   1742 C  C   . ASN A 1 213 ? 3.497   10.126  21.233  1.00 27.10 ? 213 ASN A C   1 
ATOM   1743 O  O   . ASN A 1 213 ? 3.950   9.964   20.079  1.00 27.99 ? 213 ASN A O   1 
ATOM   1744 C  CB  . ASN A 1 213 ? 3.945   12.129  22.679  1.00 25.91 ? 213 ASN A CB  1 
ATOM   1745 C  CG  . ASN A 1 213 ? 3.809   13.630  22.677  1.00 27.86 ? 213 ASN A CG  1 
ATOM   1746 O  OD1 . ASN A 1 213 ? 3.144   14.183  21.803  1.00 27.11 ? 213 ASN A OD1 1 
ATOM   1747 N  ND2 . ASN A 1 213 ? 4.433   14.284  23.639  1.00 26.90 ? 213 ASN A ND2 1 
ATOM   1748 N  N   . ASP A 1 214 ? 3.414   9.156   22.143  1.00 28.40 ? 214 ASP A N   1 
ATOM   1749 C  CA  . ASP A 1 214 ? 3.756   7.739   21.847  1.00 28.85 ? 214 ASP A CA  1 
ATOM   1750 C  C   . ASP A 1 214 ? 3.151   7.314   20.505  1.00 28.00 ? 214 ASP A C   1 
ATOM   1751 O  O   . ASP A 1 214 ? 3.910   6.819   19.684  1.00 27.91 ? 214 ASP A O   1 
ATOM   1752 C  CB  . ASP A 1 214 ? 3.284   6.798   22.952  1.00 30.27 ? 214 ASP A CB  1 
ATOM   1753 C  CG  . ASP A 1 214 ? 4.193   6.811   24.164  1.00 31.97 ? 214 ASP A CG  1 
ATOM   1754 O  OD1 . ASP A 1 214 ? 5.221   7.557   24.139  1.00 29.12 ? 214 ASP A OD1 1 
ATOM   1755 O  OD2 . ASP A 1 214 ? 3.871   6.073   25.116  1.00 32.44 ? 214 ASP A OD2 1 
ATOM   1756 N  N   . LEU A 1 215 ? 1.842   7.499   20.292  1.00 28.11 ? 215 LEU A N   1 
ATOM   1757 C  CA  . LEU A 1 215 ? 1.130   6.874   19.141  1.00 28.59 ? 215 LEU A CA  1 
ATOM   1758 C  C   . LEU A 1 215 ? 1.488   7.593   17.815  1.00 25.95 ? 215 LEU A C   1 
ATOM   1759 O  O   . LEU A 1 215 ? 1.695   6.899   16.790  1.00 23.20 ? 215 LEU A O   1 
ATOM   1760 C  CB  . LEU A 1 215 ? -0.377  6.802   19.437  1.00 31.62 ? 215 LEU A CB  1 
ATOM   1761 C  CG  . LEU A 1 215 ? -0.751  5.977   20.686  1.00 36.96 ? 215 LEU A CG  1 
ATOM   1762 C  CD1 . LEU A 1 215 ? -2.208  6.183   21.095  1.00 40.03 ? 215 LEU A CD1 1 
ATOM   1763 C  CD2 . LEU A 1 215 ? -0.487  4.479   20.518  1.00 34.89 ? 215 LEU A CD2 1 
ATOM   1764 N  N   . VAL A 1 216 ? 1.672   8.910   17.820  1.00 22.45 ? 216 VAL A N   1 
ATOM   1765 C  CA  . VAL A 1 216 ? 2.017   9.659   16.581  1.00 22.18 ? 216 VAL A CA  1 
ATOM   1766 C  C   . VAL A 1 216 ? 3.510   9.450   16.250  1.00 21.17 ? 216 VAL A C   1 
ATOM   1767 O  O   . VAL A 1 216 ? 3.852   9.371   15.034  1.00 18.96 ? 216 VAL A O   1 
ATOM   1768 C  CB  . VAL A 1 216 ? 1.598   11.141  16.711  1.00 21.96 ? 216 VAL A CB  1 
ATOM   1769 C  CG1 . VAL A 1 216 ? 2.001   11.977  15.502  1.00 21.03 ? 216 VAL A CG1 1 
ATOM   1770 C  CG2 . VAL A 1 216 ? 0.095   11.248  16.944  1.00 21.84 ? 216 VAL A CG2 1 
ATOM   1771 N  N   . ASP A 1 217 ? 4.371   9.315   17.262  1.00 21.79 ? 217 ASP A N   1 
ATOM   1772 C  CA  . ASP A 1 217 ? 5.827   9.060   17.049  1.00 23.35 ? 217 ASP A CA  1 
ATOM   1773 C  C   . ASP A 1 217 ? 5.995   7.694   16.369  1.00 23.80 ? 217 ASP A C   1 
ATOM   1774 O  O   . ASP A 1 217 ? 6.798   7.595   15.428  1.00 22.10 ? 217 ASP A O   1 
ATOM   1775 C  CB  . ASP A 1 217 ? 6.614   9.192   18.352  1.00 22.51 ? 217 ASP A CB  1 
ATOM   1776 C  CG  . ASP A 1 217 ? 6.702   10.626  18.852  1.00 25.25 ? 217 ASP A CG  1 
ATOM   1777 O  OD1 . ASP A 1 217 ? 6.407   11.536  18.063  1.00 29.28 ? 217 ASP A OD1 1 
ATOM   1778 O  OD2 . ASP A 1 217 ? 7.070   10.827  20.026  1.00 25.84 ? 217 ASP A OD2 1 
ATOM   1779 N  N   . LYS A 1 218 ? 5.197   6.710   16.785  1.00 24.84 ? 218 LYS A N   1 
ATOM   1780 C  CA  . LYS A 1 218 ? 5.168   5.349   16.184  1.00 28.61 ? 218 LYS A CA  1 
ATOM   1781 C  C   . LYS A 1 218 ? 4.787   5.430   14.706  1.00 26.00 ? 218 LYS A C   1 
ATOM   1782 O  O   . LYS A 1 218 ? 5.418   4.714   13.893  1.00 24.19 ? 218 LYS A O   1 
ATOM   1783 C  CB  . LYS A 1 218 ? 4.170   4.468   16.939  1.00 33.41 ? 218 LYS A CB  1 
ATOM   1784 C  CG  . LYS A 1 218 ? 3.893   3.099   16.339  1.00 36.50 ? 218 LYS A CG  1 
ATOM   1785 C  CD  . LYS A 1 218 ? 4.987   2.093   16.582  1.00 41.41 ? 218 LYS A CD  1 
ATOM   1786 C  CE  . LYS A 1 218 ? 4.583   0.710   16.118  1.00 45.97 ? 218 LYS A CE  1 
ATOM   1787 N  NZ  . LYS A 1 218 ? 5.769   -0.092  15.738  1.00 45.67 ? 218 LYS A NZ  1 
ATOM   1788 N  N   . ILE A 1 219 ? 3.767   6.234   14.390  1.00 26.09 ? 219 ILE A N   1 
ATOM   1789 C  CA  . ILE A 1 219 ? 3.261   6.444   12.997  1.00 28.07 ? 219 ILE A CA  1 
ATOM   1790 C  C   . ILE A 1 219 ? 4.395   7.035   12.162  1.00 25.76 ? 219 ILE A C   1 
ATOM   1791 O  O   . ILE A 1 219 ? 4.636   6.548   11.039  1.00 23.67 ? 219 ILE A O   1 
ATOM   1792 C  CB  . ILE A 1 219 ? 2.022   7.366   12.981  1.00 29.63 ? 219 ILE A CB  1 
ATOM   1793 C  CG1 . ILE A 1 219 ? 0.787   6.658   13.556  1.00 29.72 ? 219 ILE A CG1 1 
ATOM   1794 C  CG2 . ILE A 1 219 ? 1.777   7.934   11.582  1.00 27.98 ? 219 ILE A CG2 1 
ATOM   1795 C  CD1 . ILE A 1 219 ? 0.211   5.582   12.668  1.00 29.81 ? 219 ILE A CD1 1 
ATOM   1796 N  N   . ILE A 1 220 ? 5.046   8.062   12.707  1.00 25.52 ? 220 ILE A N   1 
ATOM   1797 C  CA  . ILE A 1 220 ? 6.145   8.791   12.015  1.00 26.56 ? 220 ILE A CA  1 
ATOM   1798 C  C   . ILE A 1 220 ? 7.298   7.802   11.806  1.00 26.80 ? 220 ILE A C   1 
ATOM   1799 O  O   . ILE A 1 220 ? 7.777   7.725   10.666  1.00 26.62 ? 220 ILE A O   1 
ATOM   1800 C  CB  . ILE A 1 220 ? 6.547   10.051  12.802  1.00 26.43 ? 220 ILE A CB  1 
ATOM   1801 C  CG1 . ILE A 1 220 ? 5.413   11.076  12.782  1.00 27.96 ? 220 ILE A CG1 1 
ATOM   1802 C  CG2 . ILE A 1 220 ? 7.856   10.639  12.290  1.00 25.85 ? 220 ILE A CG2 1 
ATOM   1803 C  CD1 . ILE A 1 220 ? 5.499   12.108  13.888  1.00 28.68 ? 220 ILE A CD1 1 
ATOM   1804 N  N   . ALA A 1 221 ? 7.656   7.028   12.846  1.00 24.88 ? 221 ALA A N   1 
ATOM   1805 C  CA  . ALA A 1 221 ? 8.750   6.027   12.814  1.00 24.94 ? 221 ALA A CA  1 
ATOM   1806 C  C   . ALA A 1 221 ? 8.424   4.904   11.814  1.00 23.52 ? 221 ALA A C   1 
ATOM   1807 O  O   . ALA A 1 221 ? 9.312   4.549   11.009  1.00 21.19 ? 221 ALA A O   1 
ATOM   1808 C  CB  . ALA A 1 221 ? 9.009   5.511   14.215  1.00 24.56 ? 221 ALA A CB  1 
ATOM   1809 N  N   . ASP A 1 222 ? 7.192   4.387   11.826  1.00 25.35 ? 222 ASP A N   1 
ATOM   1810 C  CA  . ASP A 1 222 ? 6.761   3.309   10.894  1.00 28.11 ? 222 ASP A CA  1 
ATOM   1811 C  C   . ASP A 1 222 ? 6.886   3.819   9.455   1.00 26.17 ? 222 ASP A C   1 
ATOM   1812 O  O   . ASP A 1 222 ? 7.359   3.050   8.596   1.00 27.63 ? 222 ASP A O   1 
ATOM   1813 C  CB  . ASP A 1 222 ? 5.346   2.815   11.206  1.00 31.09 ? 222 ASP A CB  1 
ATOM   1814 C  CG  . ASP A 1 222 ? 5.283   1.994   12.483  1.00 37.19 ? 222 ASP A CG  1 
ATOM   1815 O  OD1 . ASP A 1 222 ? 6.376   1.670   13.017  1.00 37.34 ? 222 ASP A OD1 1 
ATOM   1816 O  OD2 . ASP A 1 222 ? 4.148   1.679   12.941  1.00 37.31 ? 222 ASP A OD2 1 
ATOM   1817 N  N   . ARG A 1 223 ? 6.493   5.066   9.197   1.00 23.20 ? 223 ARG A N   1 
ATOM   1818 C  CA  . ARG A 1 223 ? 6.527   5.643   7.835   1.00 23.00 ? 223 ARG A CA  1 
ATOM   1819 C  C   . ARG A 1 223 ? 7.991   5.802   7.363   1.00 24.41 ? 223 ARG A C   1 
ATOM   1820 O  O   . ARG A 1 223 ? 8.310   5.416   6.185   1.00 23.15 ? 223 ARG A O   1 
ATOM   1821 C  CB  . ARG A 1 223 ? 5.729   6.949   7.802   1.00 22.86 ? 223 ARG A CB  1 
ATOM   1822 C  CG  . ARG A 1 223 ? 5.696   7.596   6.421   1.00 23.60 ? 223 ARG A CG  1 
ATOM   1823 C  CD  . ARG A 1 223 ? 5.121   6.707   5.316   1.00 22.64 ? 223 ARG A CD  1 
ATOM   1824 N  NE  . ARG A 1 223 ? 3.708   6.460   5.555   1.00 23.05 ? 223 ARG A NE  1 
ATOM   1825 C  CZ  . ARG A 1 223 ? 2.729   7.362   5.384   1.00 24.05 ? 223 ARG A CZ  1 
ATOM   1826 N  NH1 . ARG A 1 223 ? 3.010   8.586   4.965   1.00 23.61 ? 223 ARG A NH1 1 
ATOM   1827 N  NH2 . ARG A 1 223 ? 1.465   7.049   5.648   1.00 24.49 ? 223 ARG A NH2 1 
ATOM   1828 N  N   . LYS A 1 224 ? 8.866   6.365   8.206   1.00 25.76 ? 224 LYS A N   1 
ATOM   1829 C  CA  . LYS A 1 224 ? 10.312  6.568   7.889   1.00 27.21 ? 224 LYS A CA  1 
ATOM   1830 C  C   . LYS A 1 224 ? 10.985  5.235   7.550   1.00 25.89 ? 224 LYS A C   1 
ATOM   1831 O  O   . LYS A 1 224 ? 11.809  5.249   6.664   1.00 25.96 ? 224 LYS A O   1 
ATOM   1832 C  CB  . LYS A 1 224 ? 11.048  7.264   9.033   1.00 27.91 ? 224 LYS A CB  1 
ATOM   1833 C  CG  . LYS A 1 224 ? 10.761  8.750   9.084   1.00 28.38 ? 224 LYS A CG  1 
ATOM   1834 C  CD  . LYS A 1 224 ? 11.473  9.447   10.184  1.00 31.42 ? 224 LYS A CD  1 
ATOM   1835 C  CE  . LYS A 1 224 ? 12.959  9.578   9.939   1.00 32.31 ? 224 LYS A CE  1 
ATOM   1836 N  NZ  . LYS A 1 224 ? 13.645  10.049  11.161  1.00 31.51 ? 224 LYS A NZ  1 
ATOM   1837 N  N   . ALA A 1 225 ? 10.610  4.139   8.207   1.00 26.63 ? 225 ALA A N   1 
ATOM   1838 C  CA  . ALA A 1 225 ? 11.189  2.792   8.007   1.00 27.75 ? 225 ALA A CA  1 
ATOM   1839 C  C   . ALA A 1 225 ? 10.665  2.154   6.708   1.00 31.04 ? 225 ALA A C   1 
ATOM   1840 O  O   . ALA A 1 225 ? 11.472  1.511   6.004   1.00 33.70 ? 225 ALA A O   1 
ATOM   1841 C  CB  . ALA A 1 225 ? 10.883  1.922   9.198   1.00 26.29 ? 225 ALA A CB  1 
ATOM   1842 N  N   . SER A 1 226 ? 9.365   2.255   6.418   1.00 28.60 ? 226 SER A N   1 
ATOM   1843 C  CA  . SER A 1 226 ? 8.743   1.619   5.232   1.00 28.78 ? 226 SER A CA  1 
ATOM   1844 C  C   . SER A 1 226 ? 9.223   2.294   3.941   1.00 30.06 ? 226 SER A C   1 
ATOM   1845 O  O   . SER A 1 226 ? 9.137   1.663   2.881   1.00 31.31 ? 226 SER A O   1 
ATOM   1846 C  CB  . SER A 1 226 ? 7.257   1.684   5.333   1.00 28.94 ? 226 SER A CB  1 
ATOM   1847 O  OG  . SER A 1 226 ? 6.814   3.037   5.341   1.00 28.69 ? 226 SER A OG  1 
ATOM   1848 N  N   . GLY A 1 227 ? 9.649   3.557   4.013   1.00 30.77 ? 227 GLY A N   1 
ATOM   1849 C  CA  . GLY A 1 227 ? 9.898   4.411   2.835   1.00 31.01 ? 227 GLY A CA  1 
ATOM   1850 C  C   . GLY A 1 227 ? 8.642   4.635   2.001   1.00 33.78 ? 227 GLY A C   1 
ATOM   1851 O  O   . GLY A 1 227 ? 8.782   5.118   0.853   1.00 35.36 ? 227 GLY A O   1 
ATOM   1852 N  N   . GLU A 1 228 ? 7.456   4.317   2.536   1.00 36.81 ? 228 GLU A N   1 
ATOM   1853 C  CA  . GLU A 1 228 ? 6.194   4.247   1.757   1.00 39.63 ? 228 GLU A CA  1 
ATOM   1854 C  C   . GLU A 1 228 ? 5.853   5.669   1.327   1.00 40.81 ? 228 GLU A C   1 
ATOM   1855 O  O   . GLU A 1 228 ? 5.910   6.570   2.182   1.00 45.75 ? 228 GLU A O   1 
ATOM   1856 C  CB  . GLU A 1 228 ? 5.083   3.603   2.588   1.00 46.08 ? 228 GLU A CB  1 
ATOM   1857 C  CG  . GLU A 1 228 ? 3.817   3.214   1.819   1.00 48.60 ? 228 GLU A CG  1 
ATOM   1858 C  CD  . GLU A 1 228 ? 2.694   2.697   2.725   1.00 50.23 ? 228 GLU A CD  1 
ATOM   1859 O  OE1 . GLU A 1 228 ? 2.920   2.619   3.971   1.00 43.63 ? 228 GLU A OE1 1 
ATOM   1860 O  OE2 . GLU A 1 228 ? 1.590   2.362   2.196   1.00 47.85 ? 228 GLU A OE2 1 
ATOM   1861 N  N   . GLN A 1 229 ? 5.552   5.858   0.041   1.00 41.55 ? 229 GLN A N   1 
ATOM   1862 C  CA  . GLN A 1 229 ? 5.241   7.181   -0.566  1.00 40.41 ? 229 GLN A CA  1 
ATOM   1863 C  C   . GLN A 1 229 ? 3.749   7.189   -0.916  1.00 40.73 ? 229 GLN A C   1 
ATOM   1864 O  O   . GLN A 1 229 ? 3.432   7.053   -2.095  1.00 46.73 ? 229 GLN A O   1 
ATOM   1865 C  CB  . GLN A 1 229 ? 6.152   7.456   -1.775  1.00 39.71 ? 229 GLN A CB  1 
ATOM   1866 C  CG  . GLN A 1 229 ? 7.661   7.395   -1.484  1.00 43.32 ? 229 GLN A CG  1 
ATOM   1867 C  CD  . GLN A 1 229 ? 8.231   8.571   -0.708  1.00 44.52 ? 229 GLN A CD  1 
ATOM   1868 O  OE1 . GLN A 1 229 ? 8.421   8.523   0.508   1.00 49.10 ? 229 GLN A OE1 1 
ATOM   1869 N  NE2 . GLN A 1 229 ? 8.520   9.657   -1.404  1.00 44.58 ? 229 GLN A NE2 1 
ATOM   1870 N  N   . SER A 1 230 ? 2.866   7.257   0.084   1.00 41.38 ? 230 SER A N   1 
ATOM   1871 C  CA  . SER A 1 230 ? 1.422   7.557   -0.092  1.00 40.90 ? 230 SER A CA  1 
ATOM   1872 C  C   . SER A 1 230 ? 1.310   9.067   -0.273  1.00 42.35 ? 230 SER A C   1 
ATOM   1873 O  O   . SER A 1 230 ? 2.196   9.768   0.217   1.00 45.97 ? 230 SER A O   1 
ATOM   1874 C  CB  . SER A 1 230 ? 0.585   7.067   1.068   1.00 41.16 ? 230 SER A CB  1 
ATOM   1875 O  OG  . SER A 1 230 ? 1.309   7.141   2.289   1.00 42.14 ? 230 SER A OG  1 
ATOM   1876 N  N   . ASP A 1 231 ? 0.292   9.539   -0.984  1.00 44.98 ? 231 ASP A N   1 
ATOM   1877 C  CA  . ASP A 1 231 ? 0.085   10.983  -1.261  1.00 46.29 ? 231 ASP A CA  1 
ATOM   1878 C  C   . ASP A 1 231 ? -0.712  11.608  -0.101  1.00 41.23 ? 231 ASP A C   1 
ATOM   1879 O  O   . ASP A 1 231 ? -1.849  12.039  -0.330  1.00 40.90 ? 231 ASP A O   1 
ATOM   1880 C  CB  . ASP A 1 231 ? -0.566  11.157  -2.633  1.00 51.26 ? 231 ASP A CB  1 
ATOM   1881 C  CG  . ASP A 1 231 ? -0.136  12.429  -3.341  1.00 58.70 ? 231 ASP A CG  1 
ATOM   1882 O  OD1 . ASP A 1 231 ? -0.274  13.528  -2.735  1.00 61.07 ? 231 ASP A OD1 1 
ATOM   1883 O  OD2 . ASP A 1 231 ? 0.340   12.309  -4.492  1.00 65.11 ? 231 ASP A OD2 1 
ATOM   1884 N  N   . ASP A 1 232 ? -0.119  11.667  1.097   1.00 32.69 ? 232 ASP A N   1 
ATOM   1885 C  CA  . ASP A 1 232 ? -0.760  12.174  2.336   1.00 29.13 ? 232 ASP A CA  1 
ATOM   1886 C  C   . ASP A 1 232 ? 0.129   13.272  2.967   1.00 25.11 ? 232 ASP A C   1 
ATOM   1887 O  O   . ASP A 1 232 ? 1.279   13.442  2.549   1.00 21.23 ? 232 ASP A O   1 
ATOM   1888 C  CB  . ASP A 1 232 ? -1.062  10.990  3.259   1.00 30.43 ? 232 ASP A CB  1 
ATOM   1889 C  CG  . ASP A 1 232 ? 0.155   10.244  3.792   1.00 32.98 ? 232 ASP A CG  1 
ATOM   1890 O  OD1 . ASP A 1 232 ? 1.284   10.800  3.770   1.00 32.47 ? 232 ASP A OD1 1 
ATOM   1891 O  OD2 . ASP A 1 232 ? -0.033  9.114   4.260   1.00 35.25 ? 232 ASP A OD2 1 
ATOM   1892 N  N   . LEU A 1 233 ? -0.368  14.015  3.955   1.00 22.97 ? 233 LEU A N   1 
ATOM   1893 C  CA  . LEU A 1 233 ? 0.378   15.186  4.507   1.00 22.27 ? 233 LEU A CA  1 
ATOM   1894 C  C   . LEU A 1 233 ? 1.700   14.741  5.150   1.00 21.99 ? 233 LEU A C   1 
ATOM   1895 O  O   . LEU A 1 233 ? 2.611   15.576  5.285   1.00 24.10 ? 233 LEU A O   1 
ATOM   1896 C  CB  . LEU A 1 233 ? -0.494  15.906  5.530   1.00 21.08 ? 233 LEU A CB  1 
ATOM   1897 C  CG  . LEU A 1 233 ? -1.793  16.473  4.980   1.00 21.13 ? 233 LEU A CG  1 
ATOM   1898 C  CD1 . LEU A 1 233 ? -2.693  16.915  6.130   1.00 21.21 ? 233 LEU A CD1 1 
ATOM   1899 C  CD2 . LEU A 1 233 ? -1.521  17.629  4.019   1.00 20.54 ? 233 LEU A CD2 1 
ATOM   1900 N  N   . LEU A 1 234 ? 1.813   13.469  5.531   1.00 23.17 ? 234 LEU A N   1 
ATOM   1901 C  CA  . LEU A 1 234 ? 2.978   12.926  6.273   1.00 22.18 ? 234 LEU A CA  1 
ATOM   1902 C  C   . LEU A 1 234 ? 4.166   12.724  5.309   1.00 21.99 ? 234 LEU A C   1 
ATOM   1903 O  O   . LEU A 1 234 ? 5.246   13.229  5.604   1.00 22.04 ? 234 LEU A O   1 
ATOM   1904 C  CB  . LEU A 1 234 ? 2.543   11.643  6.981   1.00 21.41 ? 234 LEU A CB  1 
ATOM   1905 C  CG  . LEU A 1 234 ? 3.622   10.962  7.817   1.00 21.33 ? 234 LEU A CG  1 
ATOM   1906 C  CD1 . LEU A 1 234 ? 4.370   11.966  8.686   1.00 20.99 ? 234 LEU A CD1 1 
ATOM   1907 C  CD2 . LEU A 1 234 ? 3.025   9.839   8.663   1.00 22.37 ? 234 LEU A CD2 1 
ATOM   1908 N  N   . THR A 1 235 ? 3.987   12.016  4.198   1.00 23.00 ? 235 THR A N   1 
ATOM   1909 C  CA  . THR A 1 235 ? 4.978   11.958  3.087   1.00 24.18 ? 235 THR A CA  1 
ATOM   1910 C  C   . THR A 1 235 ? 5.442   13.396  2.788   1.00 24.15 ? 235 THR A C   1 
ATOM   1911 O  O   . THR A 1 235 ? 6.658   13.642  2.832   1.00 23.86 ? 235 THR A O   1 
ATOM   1912 C  CB  . THR A 1 235 ? 4.380   11.244  1.864   1.00 24.78 ? 235 THR A CB  1 
ATOM   1913 O  OG1 . THR A 1 235 ? 4.104   9.883   2.199   1.00 26.59 ? 235 THR A OG1 1 
ATOM   1914 C  CG2 . THR A 1 235 ? 5.284   11.271  0.652   1.00 24.68 ? 235 THR A CG2 1 
ATOM   1915 N  N   . HIS A 1 236 ? 4.504   14.319  2.544   1.00 23.04 ? 236 HIS A N   1 
ATOM   1916 C  CA  . HIS A 1 236 ? 4.795   15.711  2.113   1.00 23.67 ? 236 HIS A CA  1 
ATOM   1917 C  C   . HIS A 1 236 ? 5.741   16.361  3.123   1.00 23.33 ? 236 HIS A C   1 
ATOM   1918 O  O   . HIS A 1 236 ? 6.700   17.035  2.666   1.00 20.92 ? 236 HIS A O   1 
ATOM   1919 C  CB  . HIS A 1 236 ? 3.519   16.557  1.997   1.00 25.29 ? 236 HIS A CB  1 
ATOM   1920 C  CG  . HIS A 1 236 ? 2.597   16.104  0.920   1.00 29.77 ? 236 HIS A CG  1 
ATOM   1921 N  ND1 . HIS A 1 236 ? 1.221   16.324  0.984   1.00 30.69 ? 236 HIS A ND1 1 
ATOM   1922 C  CD2 . HIS A 1 236 ? 2.840   15.426  -0.231  1.00 30.24 ? 236 HIS A CD2 1 
ATOM   1923 C  CE1 . HIS A 1 236 ? 0.662   15.799  -0.089  1.00 32.05 ? 236 HIS A CE1 1 
ATOM   1924 N  NE2 . HIS A 1 236 ? 1.636   15.227  -0.842  1.00 32.37 ? 236 HIS A NE2 1 
ATOM   1925 N  N   . MET A 1 237 ? 5.438   16.177  4.420   1.00 21.24 ? 237 MET A N   1 
ATOM   1926 C  CA  . MET A 1 237 ? 6.166   16.776  5.569   1.00 22.78 ? 237 MET A CA  1 
ATOM   1927 C  C   . MET A 1 237 ? 7.527   16.064  5.748   1.00 24.26 ? 237 MET A C   1 
ATOM   1928 O  O   . MET A 1 237 ? 8.486   16.683  6.257   1.00 25.05 ? 237 MET A O   1 
ATOM   1929 C  CB  . MET A 1 237 ? 5.335   16.624  6.851   1.00 23.08 ? 237 MET A CB  1 
ATOM   1930 C  CG  . MET A 1 237 ? 4.136   17.570  6.936   1.00 24.04 ? 237 MET A CG  1 
ATOM   1931 S  SD  . MET A 1 237 ? 3.463   17.747  8.608   1.00 23.05 ? 237 MET A SD  1 
ATOM   1932 C  CE  . MET A 1 237 ? 2.380   16.327  8.670   1.00 24.76 ? 237 MET A CE  1 
ATOM   1933 N  N   . LEU A 1 238 ? 7.605   14.789  5.377   1.00 22.89 ? 238 LEU A N   1 
ATOM   1934 C  CA  . LEU A 1 238 ? 8.861   14.019  5.463   1.00 23.56 ? 238 LEU A CA  1 
ATOM   1935 C  C   . LEU A 1 238 ? 9.740   14.424  4.282   1.00 23.08 ? 238 LEU A C   1 
ATOM   1936 O  O   . LEU A 1 238 ? 10.895  14.674  4.509   1.00 22.37 ? 238 LEU A O   1 
ATOM   1937 C  CB  . LEU A 1 238 ? 8.575   12.517  5.539   1.00 21.95 ? 238 LEU A CB  1 
ATOM   1938 C  CG  . LEU A 1 238 ? 8.073   12.047  6.903   1.00 22.38 ? 238 LEU A CG  1 
ATOM   1939 C  CD1 . LEU A 1 238 ? 7.642   10.594  6.856   1.00 22.20 ? 238 LEU A CD1 1 
ATOM   1940 C  CD2 . LEU A 1 238 ? 9.122   12.242  7.983   1.00 23.81 ? 238 LEU A CD2 1 
ATOM   1941 N  N   . ASN A 1 239 ? 9.205   14.587  3.086   1.00 26.20 ? 239 ASN A N   1 
ATOM   1942 C  CA  . ASN A 1 239 ? 10.039  15.030  1.936   1.00 27.72 ? 239 ASN A CA  1 
ATOM   1943 C  C   . ASN A 1 239 ? 10.148  16.555  1.889   1.00 27.71 ? 239 ASN A C   1 
ATOM   1944 O  O   . ASN A 1 239 ? 10.846  17.036  0.994   1.00 25.89 ? 239 ASN A O   1 
ATOM   1945 C  CB  . ASN A 1 239 ? 9.500   14.504  0.614   1.00 28.60 ? 239 ASN A CB  1 
ATOM   1946 C  CG  . ASN A 1 239 ? 9.421   13.005  0.653   1.00 30.45 ? 239 ASN A CG  1 
ATOM   1947 O  OD1 . ASN A 1 239 ? 10.164  12.386  1.402   1.00 33.84 ? 239 ASN A OD1 1 
ATOM   1948 N  ND2 . ASN A 1 239 ? 8.492   12.429  -0.091  1.00 32.99 ? 239 ASN A ND2 1 
ATOM   1949 N  N   . GLY A 1 240 ? 9.499   17.286  2.803   1.00 28.30 ? 240 GLY A N   1 
ATOM   1950 C  CA  . GLY A 1 240 ? 9.400   18.754  2.706   1.00 28.24 ? 240 GLY A CA  1 
ATOM   1951 C  C   . GLY A 1 240 ? 10.730  19.466  2.935   1.00 29.90 ? 240 GLY A C   1 
ATOM   1952 O  O   . GLY A 1 240 ? 11.479  19.039  3.828   1.00 28.13 ? 240 GLY A O   1 
ATOM   1953 N  N   . LYS A 1 241 ? 10.979  20.554  2.185   1.00 33.78 ? 241 LYS A N   1 
ATOM   1954 C  CA  . LYS A 1 241 ? 12.048  21.563  2.423   1.00 33.26 ? 241 LYS A CA  1 
ATOM   1955 C  C   . LYS A 1 241 ? 11.433  22.965  2.359   1.00 29.74 ? 241 LYS A C   1 
ATOM   1956 O  O   . LYS A 1 241 ? 10.813  23.295  1.339   1.00 26.42 ? 241 LYS A O   1 
ATOM   1957 C  CB  . LYS A 1 241 ? 13.187  21.465  1.398   1.00 38.25 ? 241 LYS A CB  1 
ATOM   1958 C  CG  . LYS A 1 241 ? 14.151  20.294  1.576   1.00 48.15 ? 241 LYS A CG  1 
ATOM   1959 C  CD  . LYS A 1 241 ? 14.639  20.027  3.009   1.00 51.14 ? 241 LYS A CD  1 
ATOM   1960 C  CE  . LYS A 1 241 ? 15.805  19.062  3.084   1.00 49.26 ? 241 LYS A CE  1 
ATOM   1961 N  NZ  . LYS A 1 241 ? 15.477  17.763  2.452   1.00 49.04 ? 241 LYS A NZ  1 
ATOM   1962 N  N   . ASP A 1 242 ? 11.661  23.764  3.403   1.00 26.97 ? 242 ASP A N   1 
ATOM   1963 C  CA  . ASP A 1 242 ? 11.316  25.204  3.458   1.00 26.03 ? 242 ASP A CA  1 
ATOM   1964 C  C   . ASP A 1 242 ? 12.227  25.948  2.489   1.00 25.29 ? 242 ASP A C   1 
ATOM   1965 O  O   . ASP A 1 242 ? 13.449  25.929  2.636   1.00 22.70 ? 242 ASP A O   1 
ATOM   1966 C  CB  . ASP A 1 242 ? 11.479  25.799  4.862   1.00 25.08 ? 242 ASP A CB  1 
ATOM   1967 C  CG  . ASP A 1 242 ? 11.285  27.299  4.881   1.00 24.90 ? 242 ASP A CG  1 
ATOM   1968 O  OD1 . ASP A 1 242 ? 10.510  27.783  4.055   1.00 27.52 ? 242 ASP A OD1 1 
ATOM   1969 O  OD2 . ASP A 1 242 ? 11.955  27.980  5.680   1.00 27.76 ? 242 ASP A OD2 1 
ATOM   1970 N  N   . PRO A 1 243 ? 11.657  26.622  1.472   1.00 24.51 ? 243 PRO A N   1 
ATOM   1971 C  CA  . PRO A 1 243 ? 12.465  27.357  0.505   1.00 25.67 ? 243 PRO A CA  1 
ATOM   1972 C  C   . PRO A 1 243 ? 13.269  28.515  1.124   1.00 26.75 ? 243 PRO A C   1 
ATOM   1973 O  O   . PRO A 1 243 ? 14.245  28.917  0.523   1.00 26.19 ? 243 PRO A O   1 
ATOM   1974 C  CB  . PRO A 1 243 ? 11.425  27.910  -0.493  1.00 25.36 ? 243 PRO A CB  1 
ATOM   1975 C  CG  . PRO A 1 243 ? 10.198  27.044  -0.301  1.00 24.96 ? 243 PRO A CG  1 
ATOM   1976 C  CD  . PRO A 1 243 ? 10.218  26.657  1.161   1.00 24.56 ? 243 PRO A CD  1 
ATOM   1977 N  N   . GLU A 1 244 ? 12.802  29.070  2.244   1.00 27.21 ? 244 GLU A N   1 
ATOM   1978 C  CA  . GLU A 1 244 ? 13.424  30.235  2.925   1.00 30.20 ? 244 GLU A CA  1 
ATOM   1979 C  C   . GLU A 1 244 ? 14.673  29.784  3.688   1.00 27.65 ? 244 GLU A C   1 
ATOM   1980 O  O   . GLU A 1 244 ? 15.778  30.273  3.366   1.00 27.68 ? 244 GLU A O   1 
ATOM   1981 C  CB  . GLU A 1 244 ? 12.459  30.868  3.931   1.00 34.77 ? 244 GLU A CB  1 
ATOM   1982 C  CG  . GLU A 1 244 ? 11.228  31.470  3.296   1.00 40.28 ? 244 GLU A CG  1 
ATOM   1983 C  CD  . GLU A 1 244 ? 10.393  32.341  4.223   1.00 46.12 ? 244 GLU A CD  1 
ATOM   1984 O  OE1 . GLU A 1 244 ? 9.345   32.834  3.762   1.00 54.86 ? 244 GLU A OE1 1 
ATOM   1985 O  OE2 . GLU A 1 244 ? 10.793  32.536  5.395   1.00 50.78 ? 244 GLU A OE2 1 
ATOM   1986 N  N   . THR A 1 245 ? 14.492  28.892  4.665   1.00 24.26 ? 245 THR A N   1 
ATOM   1987 C  CA  . THR A 1 245 ? 15.576  28.387  5.541   1.00 23.98 ? 245 THR A CA  1 
ATOM   1988 C  C   . THR A 1 245 ? 16.310  27.216  4.873   1.00 23.34 ? 245 THR A C   1 
ATOM   1989 O  O   . THR A 1 245 ? 17.485  26.977  5.252   1.00 23.28 ? 245 THR A O   1 
ATOM   1990 C  CB  . THR A 1 245 ? 15.051  28.012  6.928   1.00 22.85 ? 245 THR A CB  1 
ATOM   1991 O  OG1 . THR A 1 245 ? 14.241  26.845  6.813   1.00 22.06 ? 245 THR A OG1 1 
ATOM   1992 C  CG2 . THR A 1 245 ? 14.268  29.134  7.577   1.00 23.35 ? 245 THR A CG2 1 
ATOM   1993 N  N   . GLY A 1 246 ? 15.677  26.506  3.930   1.00 21.36 ? 246 GLY A N   1 
ATOM   1994 C  CA  . GLY A 1 246 ? 16.297  25.320  3.308   1.00 21.60 ? 246 GLY A CA  1 
ATOM   1995 C  C   . GLY A 1 246 ? 16.144  24.093  4.189   1.00 21.76 ? 246 GLY A C   1 
ATOM   1996 O  O   . GLY A 1 246 ? 16.531  22.990  3.724   1.00 22.99 ? 246 GLY A O   1 
ATOM   1997 N  N   . GLU A 1 247 ? 15.517  24.247  5.367   1.00 21.20 ? 247 GLU A N   1 
ATOM   1998 C  CA  . GLU A 1 247 ? 15.383  23.178  6.402   1.00 23.63 ? 247 GLU A CA  1 
ATOM   1999 C  C   . GLU A 1 247 ? 14.125  22.329  6.195   1.00 24.48 ? 247 GLU A C   1 
ATOM   2000 O  O   . GLU A 1 247 ? 13.063  22.844  5.857   1.00 25.63 ? 247 GLU A O   1 
ATOM   2001 C  CB  . GLU A 1 247 ? 15.309  23.786  7.803   1.00 22.97 ? 247 GLU A CB  1 
ATOM   2002 C  CG  . GLU A 1 247 ? 16.551  24.548  8.196   1.00 23.20 ? 247 GLU A CG  1 
ATOM   2003 C  CD  . GLU A 1 247 ? 16.439  25.230  9.546   1.00 23.31 ? 247 GLU A CD  1 
ATOM   2004 O  OE1 . GLU A 1 247 ? 15.530  24.879  10.328  1.00 21.55 ? 247 GLU A OE1 1 
ATOM   2005 O  OE2 . GLU A 1 247 ? 17.261  26.115  9.808   1.00 24.74 ? 247 GLU A OE2 1 
ATOM   2006 N  N   . PRO A 1 248 ? 14.171  21.020  6.528   1.00 26.22 ? 248 PRO A N   1 
ATOM   2007 C  CA  . PRO A 1 248 ? 12.966  20.200  6.604   1.00 24.48 ? 248 PRO A CA  1 
ATOM   2008 C  C   . PRO A 1 248 ? 12.352  20.412  8.003   1.00 25.12 ? 248 PRO A C   1 
ATOM   2009 O  O   . PRO A 1 248 ? 12.956  21.101  8.818   1.00 21.56 ? 248 PRO A O   1 
ATOM   2010 C  CB  . PRO A 1 248 ? 13.552  18.802  6.447   1.00 25.87 ? 248 PRO A CB  1 
ATOM   2011 C  CG  . PRO A 1 248 ? 14.813  18.893  7.309   1.00 27.30 ? 248 PRO A CG  1 
ATOM   2012 C  CD  . PRO A 1 248 ? 15.353  20.287  7.024   1.00 27.41 ? 248 PRO A CD  1 
ATOM   2013 N  N   . LEU A 1 249 ? 11.158  19.865  8.248   1.00 24.52 ? 249 LEU A N   1 
ATOM   2014 C  CA  . LEU A 1 249 ? 10.552  19.804  9.596   1.00 24.35 ? 249 LEU A CA  1 
ATOM   2015 C  C   . LEU A 1 249 ? 11.237  18.683  10.380  1.00 24.96 ? 249 LEU A C   1 
ATOM   2016 O  O   . LEU A 1 249 ? 11.439  17.619  9.808   1.00 24.40 ? 249 LEU A O   1 
ATOM   2017 C  CB  . LEU A 1 249 ? 9.063   19.517  9.446   1.00 22.97 ? 249 LEU A CB  1 
ATOM   2018 C  CG  . LEU A 1 249 ? 8.261   20.588  8.728   1.00 22.66 ? 249 LEU A CG  1 
ATOM   2019 C  CD1 . LEU A 1 249 ? 6.779   20.213  8.687   1.00 21.01 ? 249 LEU A CD1 1 
ATOM   2020 C  CD2 . LEU A 1 249 ? 8.464   21.936  9.408   1.00 23.94 ? 249 LEU A CD2 1 
ATOM   2021 N  N   . ASP A 1 250 ? 11.569  18.897  11.652  1.00 28.18 ? 250 ASP A N   1 
ATOM   2022 C  CA  . ASP A 1 250 ? 12.083  17.798  12.508  1.00 29.98 ? 250 ASP A CA  1 
ATOM   2023 C  C   . ASP A 1 250 ? 10.867  16.935  12.871  1.00 28.61 ? 250 ASP A C   1 
ATOM   2024 O  O   . ASP A 1 250 ? 9.719   17.425  12.786  1.00 27.77 ? 250 ASP A O   1 
ATOM   2025 C  CB  . ASP A 1 250 ? 12.932  18.318  13.673  1.00 33.44 ? 250 ASP A CB  1 
ATOM   2026 C  CG  . ASP A 1 250 ? 12.208  19.273  14.606  1.00 41.68 ? 250 ASP A CG  1 
ATOM   2027 O  OD1 . ASP A 1 250 ? 11.132  18.891  15.100  1.00 41.62 ? 250 ASP A OD1 1 
ATOM   2028 O  OD2 . ASP A 1 250 ? 12.726  20.406  14.836  1.00 51.51 ? 250 ASP A OD2 1 
ATOM   2029 N  N   . ASP A 1 251 ? 11.112  15.666  13.193  1.00 27.96 ? 251 ASP A N   1 
ATOM   2030 C  CA  . ASP A 1 251 ? 10.088  14.641  13.529  1.00 25.66 ? 251 ASP A CA  1 
ATOM   2031 C  C   . ASP A 1 251 ? 9.145   15.144  14.628  1.00 21.93 ? 251 ASP A C   1 
ATOM   2032 O  O   . ASP A 1 251 ? 7.967   14.800  14.562  1.00 21.22 ? 251 ASP A O   1 
ATOM   2033 C  CB  . ASP A 1 251 ? 10.769  13.320  13.905  1.00 26.84 ? 251 ASP A CB  1 
ATOM   2034 C  CG  . ASP A 1 251 ? 11.427  12.634  12.716  1.00 30.77 ? 251 ASP A CG  1 
ATOM   2035 O  OD1 . ASP A 1 251 ? 11.364  13.214  11.581  1.00 33.45 ? 251 ASP A OD1 1 
ATOM   2036 O  OD2 . ASP A 1 251 ? 12.026  11.538  12.925  1.00 32.43 ? 251 ASP A OD2 1 
ATOM   2037 N  N   . GLU A 1 252 ? 9.641   15.904  15.593  1.00 20.30 ? 252 GLU A N   1 
ATOM   2038 C  CA  . GLU A 1 252 ? 8.843   16.404  16.737  1.00 23.44 ? 252 GLU A CA  1 
ATOM   2039 C  C   . GLU A 1 252 ? 7.811   17.434  16.242  1.00 23.69 ? 252 GLU A C   1 
ATOM   2040 O  O   . GLU A 1 252 ? 6.687   17.446  16.759  1.00 22.61 ? 252 GLU A O   1 
ATOM   2041 C  CB  . GLU A 1 252 ? 9.770   16.993  17.794  1.00 23.36 ? 252 GLU A CB  1 
ATOM   2042 C  CG  . GLU A 1 252 ? 9.058   17.932  18.741  1.00 28.50 ? 252 GLU A CG  1 
ATOM   2043 C  CD  . GLU A 1 252 ? 9.762   18.229  20.056  1.00 30.64 ? 252 GLU A CD  1 
ATOM   2044 O  OE1 . GLU A 1 252 ? 10.694  17.500  20.397  1.00 35.54 ? 252 GLU A OE1 1 
ATOM   2045 O  OE2 . GLU A 1 252 ? 9.356   19.182  20.743  1.00 34.04 ? 252 GLU A OE2 1 
ATOM   2046 N  N   . ASN A 1 253 ? 8.182   18.288  15.288  1.00 22.26 ? 253 ASN A N   1 
ATOM   2047 C  CA  . ASN A 1 253 ? 7.290   19.348  14.761  1.00 22.62 ? 253 ASN A CA  1 
ATOM   2048 C  C   . ASN A 1 253 ? 6.272   18.690  13.838  1.00 22.82 ? 253 ASN A C   1 
ATOM   2049 O  O   . ASN A 1 253 ? 5.110   19.134  13.841  1.00 22.66 ? 253 ASN A O   1 
ATOM   2050 C  CB  . ASN A 1 253 ? 8.056   20.464  14.059  1.00 22.71 ? 253 ASN A CB  1 
ATOM   2051 C  CG  . ASN A 1 253 ? 7.138   21.546  13.532  1.00 22.13 ? 253 ASN A CG  1 
ATOM   2052 O  OD1 . ASN A 1 253 ? 6.873   21.615  12.334  1.00 20.59 ? 253 ASN A OD1 1 
ATOM   2053 N  ND2 . ASN A 1 253 ? 6.669   22.407  14.419  1.00 21.97 ? 253 ASN A ND2 1 
ATOM   2054 N  N   . ILE A 1 254 ? 6.666   17.623  13.137  1.00 23.92 ? 254 ILE A N   1 
ATOM   2055 C  CA  . ILE A 1 254 ? 5.706   16.793  12.349  1.00 23.92 ? 254 ILE A CA  1 
ATOM   2056 C  C   . ILE A 1 254 ? 4.658   16.174  13.294  1.00 24.02 ? 254 ILE A C   1 
ATOM   2057 O  O   . ILE A 1 254 ? 3.449   16.153  12.930  1.00 24.69 ? 254 ILE A O   1 
ATOM   2058 C  CB  . ILE A 1 254 ? 6.448   15.761  11.495  1.00 24.45 ? 254 ILE A CB  1 
ATOM   2059 C  CG1 . ILE A 1 254 ? 7.373   16.471  10.503  1.00 25.59 ? 254 ILE A CG1 1 
ATOM   2060 C  CG2 . ILE A 1 254 ? 5.457   14.834  10.789  1.00 24.32 ? 254 ILE A CG2 1 
ATOM   2061 C  CD1 . ILE A 1 254 ? 8.021   15.548  9.496   1.00 25.78 ? 254 ILE A CD1 1 
ATOM   2062 N  N   . ARG A 1 255 ? 5.080   15.738  14.488  1.00 24.07 ? 255 ARG A N   1 
ATOM   2063 C  CA  . ARG A 1 255 ? 4.173   15.152  15.505  1.00 21.20 ? 255 ARG A CA  1 
ATOM   2064 C  C   . ARG A 1 255 ? 3.115   16.192  15.858  1.00 18.81 ? 255 ARG A C   1 
ATOM   2065 O  O   . ARG A 1 255 ? 1.939   15.838  15.879  1.00 17.54 ? 255 ARG A O   1 
ATOM   2066 C  CB  . ARG A 1 255 ? 4.936   14.663  16.729  1.00 21.27 ? 255 ARG A CB  1 
ATOM   2067 C  CG  . ARG A 1 255 ? 4.027   14.356  17.902  1.00 22.96 ? 255 ARG A CG  1 
ATOM   2068 C  CD  . ARG A 1 255 ? 4.836   13.777  19.031  1.00 25.98 ? 255 ARG A CD  1 
ATOM   2069 N  NE  . ARG A 1 255 ? 5.169   14.779  20.013  1.00 28.96 ? 255 ARG A NE  1 
ATOM   2070 C  CZ  . ARG A 1 255 ? 6.249   14.746  20.799  1.00 27.99 ? 255 ARG A CZ  1 
ATOM   2071 N  NH1 . ARG A 1 255 ? 7.117   13.749  20.702  1.00 24.88 ? 255 ARG A NH1 1 
ATOM   2072 N  NH2 . ARG A 1 255 ? 6.440   15.721  21.680  1.00 27.48 ? 255 ARG A NH2 1 
ATOM   2073 N  N   . TYR A 1 256 ? 3.538   17.434  16.047  1.00 19.55 ? 256 TYR A N   1 
ATOM   2074 C  CA  . TYR A 1 256 ? 2.682   18.586  16.431  1.00 21.29 ? 256 TYR A CA  1 
ATOM   2075 C  C   . TYR A 1 256 ? 1.696   18.890  15.303  1.00 20.57 ? 256 TYR A C   1 
ATOM   2076 O  O   . TYR A 1 256 ? 0.560   19.248  15.612  1.00 21.70 ? 256 TYR A O   1 
ATOM   2077 C  CB  . TYR A 1 256 ? 3.552   19.796  16.792  1.00 22.29 ? 256 TYR A CB  1 
ATOM   2078 C  CG  . TYR A 1 256 ? 4.354   19.639  18.063  1.00 24.44 ? 256 TYR A CG  1 
ATOM   2079 C  CD1 . TYR A 1 256 ? 3.826   19.007  19.186  1.00 25.37 ? 256 TYR A CD1 1 
ATOM   2080 C  CD2 . TYR A 1 256 ? 5.633   20.166  18.171  1.00 24.75 ? 256 TYR A CD2 1 
ATOM   2081 C  CE1 . TYR A 1 256 ? 4.552   18.887  20.367  1.00 27.32 ? 256 TYR A CE1 1 
ATOM   2082 C  CE2 . TYR A 1 256 ? 6.368   20.048  19.343  1.00 25.30 ? 256 TYR A CE2 1 
ATOM   2083 C  CZ  . TYR A 1 256 ? 5.835   19.401  20.444  1.00 26.11 ? 256 TYR A CZ  1 
ATOM   2084 O  OH  . TYR A 1 256 ? 6.566   19.291  21.599  1.00 26.71 ? 256 TYR A OH  1 
ATOM   2085 N  N   . GLN A 1 257 ? 2.117   18.756  14.044  1.00 19.00 ? 257 GLN A N   1 
ATOM   2086 C  CA  . GLN A 1 257 ? 1.263   19.070  12.870  1.00 18.97 ? 257 GLN A CA  1 
ATOM   2087 C  C   . GLN A 1 257 ? 0.137   18.028  12.778  1.00 19.30 ? 257 GLN A C   1 
ATOM   2088 O  O   . GLN A 1 257 ? -1.038  18.418  12.614  1.00 19.34 ? 257 GLN A O   1 
ATOM   2089 C  CB  . GLN A 1 257 ? 2.086   19.103  11.575  1.00 18.20 ? 257 GLN A CB  1 
ATOM   2090 C  CG  . GLN A 1 257 ? 3.216   20.132  11.565  1.00 17.87 ? 257 GLN A CG  1 
ATOM   2091 C  CD  . GLN A 1 257 ? 2.878   21.557  11.980  1.00 18.01 ? 257 GLN A CD  1 
ATOM   2092 O  OE1 . GLN A 1 257 ? 1.728   21.998  12.065  1.00 15.11 ? 257 GLN A OE1 1 
ATOM   2093 N  NE2 . GLN A 1 257 ? 3.931   22.326  12.212  1.00 18.05 ? 257 GLN A NE2 1 
ATOM   2094 N  N   . ILE A 1 258 ? 0.495   16.750  12.894  1.00 19.55 ? 258 ILE A N   1 
ATOM   2095 C  CA  . ILE A 1 258 ? -0.459  15.606  12.893  1.00 18.48 ? 258 ILE A CA  1 
ATOM   2096 C  C   . ILE A 1 258 ? -1.447  15.794  14.045  1.00 17.32 ? 258 ILE A C   1 
ATOM   2097 O  O   . ILE A 1 258 ? -2.660  15.673  13.813  1.00 14.77 ? 258 ILE A O   1 
ATOM   2098 C  CB  . ILE A 1 258 ? 0.316   14.279  12.986  1.00 20.12 ? 258 ILE A CB  1 
ATOM   2099 C  CG1 . ILE A 1 258 ? 1.115   14.026  11.710  1.00 20.32 ? 258 ILE A CG1 1 
ATOM   2100 C  CG2 . ILE A 1 258 ? -0.614  13.100  13.287  1.00 20.22 ? 258 ILE A CG2 1 
ATOM   2101 C  CD1 . ILE A 1 258 ? 2.091   12.871  11.845  1.00 22.32 ? 258 ILE A CD1 1 
ATOM   2102 N  N   . ILE A 1 259 ? -0.954  16.115  15.240  1.00 16.55 ? 259 ILE A N   1 
ATOM   2103 C  CA  . ILE A 1 259 ? -1.850  16.342  16.402  1.00 17.01 ? 259 ILE A CA  1 
ATOM   2104 C  C   . ILE A 1 259 ? -2.791  17.498  16.065  1.00 17.88 ? 259 ILE A C   1 
ATOM   2105 O  O   . ILE A 1 259 ? -4.039  17.358  16.281  1.00 19.46 ? 259 ILE A O   1 
ATOM   2106 C  CB  . ILE A 1 259 ? -1.047  16.556  17.689  1.00 17.39 ? 259 ILE A CB  1 
ATOM   2107 C  CG1 . ILE A 1 259 ? -0.325  15.258  18.084  1.00 18.04 ? 259 ILE A CG1 1 
ATOM   2108 C  CG2 . ILE A 1 259 ? -1.955  17.082  18.795  1.00 17.97 ? 259 ILE A CG2 1 
ATOM   2109 C  CD1 . ILE A 1 259 ? 0.590   15.389  19.283  1.00 17.80 ? 259 ILE A CD1 1 
ATOM   2110 N  N   . THR A 1 260 ? -2.240  18.578  15.508  1.00 17.98 ? 260 THR A N   1 
ATOM   2111 C  CA  . THR A 1 260 ? -3.011  19.786  15.117  1.00 18.32 ? 260 THR A CA  1 
ATOM   2112 C  C   . THR A 1 260 ? -4.130  19.338  14.159  1.00 18.97 ? 260 THR A C   1 
ATOM   2113 O  O   . THR A 1 260 ? -5.315  19.488  14.519  1.00 20.28 ? 260 THR A O   1 
ATOM   2114 C  CB  . THR A 1 260 ? -2.070  20.867  14.565  1.00 16.94 ? 260 THR A CB  1 
ATOM   2115 O  OG1 . THR A 1 260 ? -1.138  21.233  15.586  1.00 15.79 ? 260 THR A OG1 1 
ATOM   2116 C  CG2 . THR A 1 260 ? -2.820  22.084  14.078  1.00 16.52 ? 260 THR A CG2 1 
ATOM   2117 N  N   . PHE A 1 261 ? -3.762  18.707  13.048  1.00 18.52 ? 261 PHE A N   1 
ATOM   2118 C  CA  . PHE A 1 261 ? -4.696  18.228  11.999  1.00 19.98 ? 261 PHE A CA  1 
ATOM   2119 C  C   . PHE A 1 261 ? -5.806  17.359  12.599  1.00 19.33 ? 261 PHE A C   1 
ATOM   2120 O  O   . PHE A 1 261 ? -6.956  17.508  12.180  1.00 15.88 ? 261 PHE A O   1 
ATOM   2121 C  CB  . PHE A 1 261 ? -3.945  17.467  10.904  1.00 20.43 ? 261 PHE A CB  1 
ATOM   2122 C  CG  . PHE A 1 261 ? -2.914  18.295  10.198  1.00 22.70 ? 261 PHE A CG  1 
ATOM   2123 C  CD1 . PHE A 1 261 ? -3.059  19.669  10.083  1.00 24.95 ? 261 PHE A CD1 1 
ATOM   2124 C  CD2 . PHE A 1 261 ? -1.801  17.702  9.643   1.00 25.24 ? 261 PHE A CD2 1 
ATOM   2125 C  CE1 . PHE A 1 261 ? -2.098  20.425  9.439   1.00 25.77 ? 261 PHE A CE1 1 
ATOM   2126 C  CE2 . PHE A 1 261 ? -0.842  18.461  8.993   1.00 25.58 ? 261 PHE A CE2 1 
ATOM   2127 C  CZ  . PHE A 1 261 ? -0.990  19.818  8.901   1.00 25.49 ? 261 PHE A CZ  1 
ATOM   2128 N  N   . LEU A 1 262 ? -5.462  16.488  13.547  1.00 19.97 ? 262 LEU A N   1 
ATOM   2129 C  CA  . LEU A 1 262 ? -6.422  15.503  14.085  1.00 21.08 ? 262 LEU A CA  1 
ATOM   2130 C  C   . LEU A 1 262 ? -7.392  16.268  14.960  1.00 21.03 ? 262 LEU A C   1 
ATOM   2131 O  O   . LEU A 1 262 ? -8.588  15.949  14.917  1.00 26.49 ? 262 LEU A O   1 
ATOM   2132 C  CB  . LEU A 1 262 ? -5.709  14.379  14.849  1.00 21.12 ? 262 LEU A CB  1 
ATOM   2133 C  CG  . LEU A 1 262 ? -5.117  13.268  13.977  1.00 20.06 ? 262 LEU A CG  1 
ATOM   2134 C  CD1 . LEU A 1 262 ? -4.324  12.284  14.831  1.00 22.31 ? 262 LEU A CD1 1 
ATOM   2135 C  CD2 . LEU A 1 262 ? -6.194  12.539  13.228  1.00 20.39 ? 262 LEU A CD2 1 
ATOM   2136 N  N   . ILE A 1 263 ? -6.918  17.283  15.659  1.00 20.05 ? 263 ILE A N   1 
ATOM   2137 C  CA  . ILE A 1 263 ? -7.830  18.220  16.381  1.00 19.53 ? 263 ILE A CA  1 
ATOM   2138 C  C   . ILE A 1 263 ? -8.767  18.924  15.380  1.00 18.96 ? 263 ILE A C   1 
ATOM   2139 O  O   . ILE A 1 263 ? -10.002 18.906  15.628  1.00 16.54 ? 263 ILE A O   1 
ATOM   2140 C  CB  . ILE A 1 263 ? -7.040  19.222  17.231  1.00 19.10 ? 263 ILE A CB  1 
ATOM   2141 C  CG1 . ILE A 1 263 ? -6.356  18.515  18.411  1.00 19.84 ? 263 ILE A CG1 1 
ATOM   2142 C  CG2 . ILE A 1 263 ? -7.963  20.334  17.677  1.00 19.41 ? 263 ILE A CG2 1 
ATOM   2143 C  CD1 . ILE A 1 263 ? -5.145  19.223  18.955  1.00 19.47 ? 263 ILE A CD1 1 
ATOM   2144 N  N   . ALA A 1 264 ? -8.245  19.508  14.287  1.00 19.87 ? 264 ALA A N   1 
ATOM   2145 C  CA  . ALA A 1 264 ? -9.063  20.285  13.309  1.00 20.34 ? 264 ALA A CA  1 
ATOM   2146 C  C   . ALA A 1 264 ? -10.177 19.393  12.742  1.00 20.43 ? 264 ALA A C   1 
ATOM   2147 O  O   . ALA A 1 264 ? -11.337 19.833  12.752  1.00 21.42 ? 264 ALA A O   1 
ATOM   2148 C  CB  . ALA A 1 264 ? -8.229  20.889  12.213  1.00 20.82 ? 264 ALA A CB  1 
ATOM   2149 N  N   . GLY A 1 265 ? -9.844  18.174  12.324  1.00 20.73 ? 265 GLY A N   1 
ATOM   2150 C  CA  . GLY A 1 265 ? -10.790 17.225  11.708  1.00 23.85 ? 265 GLY A CA  1 
ATOM   2151 C  C   . GLY A 1 265 ? -11.911 16.833  12.676  1.00 24.66 ? 265 GLY A C   1 
ATOM   2152 O  O   . GLY A 1 265 ? -13.075 16.655  12.229  1.00 24.25 ? 265 GLY A O   1 
ATOM   2153 N  N   . HIS A 1 266 ? -11.591 16.679  13.958  1.00 22.10 ? 266 HIS A N   1 
ATOM   2154 C  CA  . HIS A 1 266 ? -12.555 16.161  14.948  1.00 21.77 ? 266 HIS A CA  1 
ATOM   2155 C  C   . HIS A 1 266 ? -13.480 17.300  15.387  1.00 23.24 ? 266 HIS A C   1 
ATOM   2156 O  O   . HIS A 1 266 ? -14.695 17.056  15.538  1.00 25.54 ? 266 HIS A O   1 
ATOM   2157 C  CB  . HIS A 1 266 ? -11.799 15.469  16.064  1.00 21.97 ? 266 HIS A CB  1 
ATOM   2158 C  CG  . HIS A 1 266 ? -12.681 14.969  17.147  1.00 21.60 ? 266 HIS A CG  1 
ATOM   2159 N  ND1 . HIS A 1 266 ? -13.204 15.817  18.093  1.00 20.09 ? 266 HIS A ND1 1 
ATOM   2160 C  CD2 . HIS A 1 266 ? -13.072 13.716  17.467  1.00 20.96 ? 266 HIS A CD2 1 
ATOM   2161 C  CE1 . HIS A 1 266 ? -13.913 15.112  18.950  1.00 21.20 ? 266 HIS A CE1 1 
ATOM   2162 N  NE2 . HIS A 1 266 ? -13.845 13.813  18.582  1.00 20.97 ? 266 HIS A NE2 1 
ATOM   2163 N  N   . GLU A 1 267 ? -12.949 18.511  15.513  1.00 21.65 ? 267 GLU A N   1 
ATOM   2164 C  CA  . GLU A 1 267 ? -13.674 19.643  16.128  1.00 21.82 ? 267 GLU A CA  1 
ATOM   2165 C  C   . GLU A 1 267 ? -14.421 20.516  15.109  1.00 22.29 ? 267 GLU A C   1 
ATOM   2166 O  O   . GLU A 1 267 ? -15.512 20.964  15.472  1.00 20.85 ? 267 GLU A O   1 
ATOM   2167 C  CB  . GLU A 1 267 ? -12.685 20.510  16.897  1.00 23.02 ? 267 GLU A CB  1 
ATOM   2168 C  CG  . GLU A 1 267 ? -12.177 19.843  18.156  1.00 24.23 ? 267 GLU A CG  1 
ATOM   2169 C  CD  . GLU A 1 267 ? -13.304 19.307  19.013  1.00 25.60 ? 267 GLU A CD  1 
ATOM   2170 O  OE1 . GLU A 1 267 ? -13.831 20.077  19.854  1.00 30.05 ? 267 GLU A OE1 1 
ATOM   2171 O  OE2 . GLU A 1 267 ? -13.669 18.143  18.805  1.00 26.24 ? 267 GLU A OE2 1 
ATOM   2172 N  N   . THR A 1 268 ? -13.863 20.804  13.925  1.00 22.19 ? 268 THR A N   1 
ATOM   2173 C  CA  . THR A 1 268 ? -14.295 21.973  13.122  1.00 22.77 ? 268 THR A CA  1 
ATOM   2174 C  C   . THR A 1 268 ? -15.269 21.569  12.023  1.00 22.03 ? 268 THR A C   1 
ATOM   2175 O  O   . THR A 1 268 ? -16.419 22.007  12.103  1.00 22.04 ? 268 THR A O   1 
ATOM   2176 C  CB  . THR A 1 268 ? -13.122 22.766  12.543  1.00 25.16 ? 268 THR A CB  1 
ATOM   2177 O  OG1 . THR A 1 268 ? -12.442 21.913  11.623  1.00 29.97 ? 268 THR A OG1 1 
ATOM   2178 C  CG2 . THR A 1 268 ? -12.189 23.279  13.615  1.00 24.71 ? 268 THR A CG2 1 
ATOM   2179 N  N   . THR A 1 269 ? -14.834 20.833  11.001  1.00 22.62 ? 269 THR A N   1 
ATOM   2180 C  CA  . THR A 1 269 ? -15.669 20.559  9.800   1.00 20.59 ? 269 THR A CA  1 
ATOM   2181 C  C   . THR A 1 269 ? -16.883 19.729  10.212  1.00 19.41 ? 269 THR A C   1 
ATOM   2182 O  O   . THR A 1 269 ? -17.911 19.863  9.562   1.00 18.88 ? 269 THR A O   1 
ATOM   2183 C  CB  . THR A 1 269 ? -14.888 19.910  8.649   1.00 21.84 ? 269 THR A CB  1 
ATOM   2184 O  OG1 . THR A 1 269 ? -13.644 20.583  8.451   1.00 25.52 ? 269 THR A OG1 1 
ATOM   2185 C  CG2 . THR A 1 269 ? -15.646 19.975  7.342   1.00 21.94 ? 269 THR A CG2 1 
ATOM   2186 N  N   . SER A 1 270 ? -16.799 18.942  11.285  1.00 19.61 ? 270 SER A N   1 
ATOM   2187 C  CA  . SER A 1 270 ? -17.968 18.233  11.875  1.00 18.65 ? 270 SER A CA  1 
ATOM   2188 C  C   . SER A 1 270 ? -19.035 19.237  12.321  1.00 17.67 ? 270 SER A C   1 
ATOM   2189 O  O   . SER A 1 270 ? -20.236 18.983  12.105  1.00 18.47 ? 270 SER A O   1 
ATOM   2190 C  CB  . SER A 1 270 ? -17.542 17.367  13.005  1.00 19.18 ? 270 SER A CB  1 
ATOM   2191 O  OG  . SER A 1 270 ? -16.759 18.118  13.912  1.00 19.52 ? 270 SER A OG  1 
ATOM   2192 N  N   . GLY A 1 271 ? -18.616 20.337  12.931  1.00 17.81 ? 271 GLY A N   1 
ATOM   2193 C  CA  . GLY A 1 271 ? -19.532 21.373  13.437  1.00 18.63 ? 271 GLY A CA  1 
ATOM   2194 C  C   . GLY A 1 271 ? -20.209 22.114  12.296  1.00 18.63 ? 271 GLY A C   1 
ATOM   2195 O  O   . GLY A 1 271 ? -21.434 22.313  12.353  1.00 17.31 ? 271 GLY A O   1 
ATOM   2196 N  N   . LEU A 1 272 ? -19.436 22.507  11.287  1.00 18.21 ? 272 LEU A N   1 
ATOM   2197 C  CA  . LEU A 1 272 ? -19.980 23.131  10.063  1.00 19.39 ? 272 LEU A CA  1 
ATOM   2198 C  C   . LEU A 1 272 ? -21.121 22.247  9.521   1.00 21.34 ? 272 LEU A C   1 
ATOM   2199 O  O   . LEU A 1 272 ? -22.228 22.784  9.243   1.00 23.42 ? 272 LEU A O   1 
ATOM   2200 C  CB  . LEU A 1 272 ? -18.843 23.284  9.043   1.00 19.77 ? 272 LEU A CB  1 
ATOM   2201 C  CG  . LEU A 1 272 ? -19.273 23.732  7.645   1.00 19.97 ? 272 LEU A CG  1 
ATOM   2202 C  CD1 . LEU A 1 272 ? -20.173 24.948  7.740   1.00 20.57 ? 272 LEU A CD1 1 
ATOM   2203 C  CD2 . LEU A 1 272 ? -18.078 24.011  6.749   1.00 19.68 ? 272 LEU A CD2 1 
ATOM   2204 N  N   . LEU A 1 273 ? -20.869 20.951  9.343   1.00 19.79 ? 273 LEU A N   1 
ATOM   2205 C  CA  . LEU A 1 273 ? -21.839 20.033  8.699   1.00 20.13 ? 273 LEU A CA  1 
ATOM   2206 C  C   . LEU A 1 273 ? -23.065 19.910  9.597   1.00 20.63 ? 273 LEU A C   1 
ATOM   2207 O  O   . LEU A 1 273 ? -24.174 20.126  9.078   1.00 22.23 ? 273 LEU A O   1 
ATOM   2208 C  CB  . LEU A 1 273 ? -21.192 18.671  8.413   1.00 19.35 ? 273 LEU A CB  1 
ATOM   2209 C  CG  . LEU A 1 273 ? -20.335 18.622  7.146   1.00 18.86 ? 273 LEU A CG  1 
ATOM   2210 C  CD1 . LEU A 1 273 ? -19.552 17.327  7.085   1.00 19.35 ? 273 LEU A CD1 1 
ATOM   2211 C  CD2 . LEU A 1 273 ? -21.189 18.775  5.895   1.00 18.57 ? 273 LEU A CD2 1 
ATOM   2212 N  N   . SER A 1 274 ? -22.888 19.617  10.888  1.00 20.58 ? 274 SER A N   1 
ATOM   2213 C  CA  . SER A 1 274 ? -24.020 19.496  11.849  1.00 19.29 ? 274 SER A CA  1 
ATOM   2214 C  C   . SER A 1 274 ? -24.907 20.744  11.767  1.00 18.73 ? 274 SER A C   1 
ATOM   2215 O  O   . SER A 1 274 ? -26.112 20.556  11.677  1.00 17.43 ? 274 SER A O   1 
ATOM   2216 C  CB  . SER A 1 274 ? -23.562 19.243  13.274  1.00 19.81 ? 274 SER A CB  1 
ATOM   2217 O  OG  . SER A 1 274 ? -22.628 18.166  13.339  1.00 19.21 ? 274 SER A OG  1 
ATOM   2218 N  N   . PHE A 1 275 ? -24.330 21.955  11.820  1.00 18.90 ? 275 PHE A N   1 
ATOM   2219 C  CA  . PHE A 1 275 ? -25.068 23.256  11.804  1.00 18.41 ? 275 PHE A CA  1 
ATOM   2220 C  C   . PHE A 1 275 ? -25.737 23.479  10.441  1.00 18.99 ? 275 PHE A C   1 
ATOM   2221 O  O   . PHE A 1 275 ? -26.862 24.035  10.431  1.00 19.46 ? 275 PHE A O   1 
ATOM   2222 C  CB  . PHE A 1 275 ? -24.185 24.476  12.088  1.00 17.62 ? 275 PHE A CB  1 
ATOM   2223 C  CG  . PHE A 1 275 ? -24.027 24.775  13.558  1.00 17.45 ? 275 PHE A CG  1 
ATOM   2224 C  CD1 . PHE A 1 275 ? -25.124 25.112  14.326  1.00 16.44 ? 275 PHE A CD1 1 
ATOM   2225 C  CD2 . PHE A 1 275 ? -22.790 24.701  14.172  1.00 17.11 ? 275 PHE A CD2 1 
ATOM   2226 C  CE1 . PHE A 1 275 ? -24.997 25.343  15.679  1.00 16.30 ? 275 PHE A CE1 1 
ATOM   2227 C  CE2 . PHE A 1 275 ? -22.664 24.935  15.528  1.00 17.39 ? 275 PHE A CE2 1 
ATOM   2228 C  CZ  . PHE A 1 275 ? -23.773 25.233  16.284  1.00 17.23 ? 275 PHE A CZ  1 
ATOM   2229 N  N   . ALA A 1 276 ? -25.105 23.055  9.340   1.00 18.07 ? 276 ALA A N   1 
ATOM   2230 C  CA  . ALA A 1 276 ? -25.715 23.064  7.988   1.00 18.43 ? 276 ALA A CA  1 
ATOM   2231 C  C   . ALA A 1 276 ? -27.025 22.243  7.999   1.00 18.73 ? 276 ALA A C   1 
ATOM   2232 O  O   . ALA A 1 276 ? -28.092 22.793  7.608   1.00 18.86 ? 276 ALA A O   1 
ATOM   2233 C  CB  . ALA A 1 276 ? -24.728 22.575  6.940   1.00 18.40 ? 276 ALA A CB  1 
ATOM   2234 N  N   . LEU A 1 277 ? -26.972 20.984  8.433   1.00 18.53 ? 277 LEU A N   1 
ATOM   2235 C  CA  . LEU A 1 277 ? -28.158 20.095  8.451   1.00 20.20 ? 277 LEU A CA  1 
ATOM   2236 C  C   . LEU A 1 277 ? -29.248 20.692  9.362   1.00 19.42 ? 277 LEU A C   1 
ATOM   2237 O  O   . LEU A 1 277 ? -30.405 20.650  8.971   1.00 17.20 ? 277 LEU A O   1 
ATOM   2238 C  CB  . LEU A 1 277 ? -27.747 18.696  8.908   1.00 23.03 ? 277 LEU A CB  1 
ATOM   2239 C  CG  . LEU A 1 277 ? -28.784 17.619  8.592   1.00 26.35 ? 277 LEU A CG  1 
ATOM   2240 C  CD1 . LEU A 1 277 ? -28.999 17.510  7.089   1.00 26.91 ? 277 LEU A CD1 1 
ATOM   2241 C  CD2 . LEU A 1 277 ? -28.377 16.270  9.166   1.00 28.28 ? 277 LEU A CD2 1 
ATOM   2242 N  N   . TYR A 1 278 ? -28.879 21.257  10.518  1.00 19.26 ? 278 TYR A N   1 
ATOM   2243 C  CA  . TYR A 1 278 ? -29.808 21.932  11.453  1.00 19.62 ? 278 TYR A CA  1 
ATOM   2244 C  C   . TYR A 1 278 ? -30.570 23.021  10.698  1.00 20.70 ? 278 TYR A C   1 
ATOM   2245 O  O   . TYR A 1 278 ? -31.814 23.056  10.780  1.00 22.58 ? 278 TYR A O   1 
ATOM   2246 C  CB  . TYR A 1 278 ? -29.084 22.490  12.674  1.00 20.01 ? 278 TYR A CB  1 
ATOM   2247 C  CG  . TYR A 1 278 ? -29.938 23.409  13.498  1.00 21.70 ? 278 TYR A CG  1 
ATOM   2248 C  CD1 . TYR A 1 278 ? -30.807 22.904  14.451  1.00 20.83 ? 278 TYR A CD1 1 
ATOM   2249 C  CD2 . TYR A 1 278 ? -29.907 24.782  13.292  1.00 23.23 ? 278 TYR A CD2 1 
ATOM   2250 C  CE1 . TYR A 1 278 ? -31.607 23.746  15.202  1.00 21.75 ? 278 TYR A CE1 1 
ATOM   2251 C  CE2 . TYR A 1 278 ? -30.720 25.640  14.019  1.00 23.95 ? 278 TYR A CE2 1 
ATOM   2252 C  CZ  . TYR A 1 278 ? -31.571 25.113  14.980  1.00 23.98 ? 278 TYR A CZ  1 
ATOM   2253 O  OH  . TYR A 1 278 ? -32.392 25.935  15.696  1.00 24.98 ? 278 TYR A OH  1 
ATOM   2254 N  N   . PHE A 1 279 ? -29.862 23.898  9.996   1.00 21.18 ? 279 PHE A N   1 
ATOM   2255 C  CA  . PHE A 1 279 ? -30.474 25.089  9.350   1.00 20.64 ? 279 PHE A CA  1 
ATOM   2256 C  C   . PHE A 1 279 ? -31.312 24.681  8.161   1.00 20.76 ? 279 PHE A C   1 
ATOM   2257 O  O   . PHE A 1 279 ? -32.236 25.453  7.840   1.00 22.71 ? 279 PHE A O   1 
ATOM   2258 C  CB  . PHE A 1 279 ? -29.441 26.117  8.899   1.00 20.16 ? 279 PHE A CB  1 
ATOM   2259 C  CG  . PHE A 1 279 ? -29.062 27.023  10.031  1.00 19.10 ? 279 PHE A CG  1 
ATOM   2260 C  CD1 . PHE A 1 279 ? -30.042 27.716  10.725  1.00 19.17 ? 279 PHE A CD1 1 
ATOM   2261 C  CD2 . PHE A 1 279 ? -27.750 27.156  10.417  1.00 19.11 ? 279 PHE A CD2 1 
ATOM   2262 C  CE1 . PHE A 1 279 ? -29.714 28.552  11.776  1.00 19.40 ? 279 PHE A CE1 1 
ATOM   2263 C  CE2 . PHE A 1 279 ? -27.424 27.997  11.469  1.00 20.27 ? 279 PHE A CE2 1 
ATOM   2264 C  CZ  . PHE A 1 279 ? -28.404 28.691  12.146  1.00 19.53 ? 279 PHE A CZ  1 
ATOM   2265 N  N   . LEU A 1 280 ? -30.976 23.548  7.542   1.00 20.51 ? 280 LEU A N   1 
ATOM   2266 C  CA  . LEU A 1 280 ? -31.747 22.993  6.405   1.00 20.82 ? 280 LEU A CA  1 
ATOM   2267 C  C   . LEU A 1 280 ? -33.090 22.488  6.928   1.00 19.83 ? 280 LEU A C   1 
ATOM   2268 O  O   . LEU A 1 280 ? -34.096 22.872  6.350   1.00 19.82 ? 280 LEU A O   1 
ATOM   2269 C  CB  . LEU A 1 280 ? -30.953 21.880  5.712   1.00 21.75 ? 280 LEU A CB  1 
ATOM   2270 C  CG  . LEU A 1 280 ? -29.802 22.358  4.824   1.00 21.84 ? 280 LEU A CG  1 
ATOM   2271 C  CD1 . LEU A 1 280 ? -29.174 21.178  4.117   1.00 22.58 ? 280 LEU A CD1 1 
ATOM   2272 C  CD2 . LEU A 1 280 ? -30.252 23.402  3.810   1.00 19.88 ? 280 LEU A CD2 1 
ATOM   2273 N  N   . VAL A 1 281 ? -33.118 21.653  7.975   1.00 19.76 ? 281 VAL A N   1 
ATOM   2274 C  CA  . VAL A 1 281 ? -34.400 21.035  8.412   1.00 19.39 ? 281 VAL A CA  1 
ATOM   2275 C  C   . VAL A 1 281 ? -35.264 22.095  9.083   1.00 19.07 ? 281 VAL A C   1 
ATOM   2276 O  O   . VAL A 1 281 ? -36.474 21.836  9.224   1.00 20.22 ? 281 VAL A O   1 
ATOM   2277 C  CB  . VAL A 1 281 ? -34.209 19.829  9.327   1.00 20.91 ? 281 VAL A CB  1 
ATOM   2278 C  CG1 . VAL A 1 281 ? -33.448 18.744  8.600   1.00 22.33 ? 281 VAL A CG1 1 
ATOM   2279 C  CG2 . VAL A 1 281 ? -33.550 20.216  10.648  1.00 22.64 ? 281 VAL A CG2 1 
ATOM   2280 N  N   . LYS A 1 282 ? -34.682 23.226  9.474   1.00 17.68 ? 282 LYS A N   1 
ATOM   2281 C  CA  . LYS A 1 282 ? -35.454 24.338  10.064  1.00 19.18 ? 282 LYS A CA  1 
ATOM   2282 C  C   . LYS A 1 282 ? -35.852 25.350  8.989   1.00 19.10 ? 282 LYS A C   1 
ATOM   2283 O  O   . LYS A 1 282 ? -36.556 26.283  9.322   1.00 19.92 ? 282 LYS A O   1 
ATOM   2284 C  CB  . LYS A 1 282 ? -34.648 24.979  11.195  1.00 19.12 ? 282 LYS A CB  1 
ATOM   2285 C  CG  . LYS A 1 282 ? -34.341 24.034  12.348  1.00 17.84 ? 282 LYS A CG  1 
ATOM   2286 C  CD  . LYS A 1 282 ? -35.554 23.665  13.162  1.00 17.36 ? 282 LYS A CD  1 
ATOM   2287 C  CE  . LYS A 1 282 ? -35.222 23.116  14.541  1.00 15.98 ? 282 LYS A CE  1 
ATOM   2288 N  NZ  . LYS A 1 282 ? -36.457 22.603  15.168  1.00 15.70 ? 282 LYS A NZ  1 
ATOM   2289 N  N   . ASN A 1 283 ? -35.389 25.187  7.755   1.00 20.43 ? 283 ASN A N   1 
ATOM   2290 C  CA  . ASN A 1 283 ? -35.713 26.099  6.625   1.00 19.70 ? 283 ASN A CA  1 
ATOM   2291 C  C   . ASN A 1 283 ? -35.954 25.231  5.392   1.00 19.96 ? 283 ASN A C   1 
ATOM   2292 O  O   . ASN A 1 283 ? -35.099 25.126  4.510   1.00 19.62 ? 283 ASN A O   1 
ATOM   2293 C  CB  . ASN A 1 283 ? -34.605 27.132  6.428   1.00 20.08 ? 283 ASN A CB  1 
ATOM   2294 C  CG  . ASN A 1 283 ? -34.387 27.989  7.654   1.00 20.60 ? 283 ASN A CG  1 
ATOM   2295 O  OD1 . ASN A 1 283 ? -34.980 29.059  7.761   1.00 19.51 ? 283 ASN A OD1 1 
ATOM   2296 N  ND2 . ASN A 1 283 ? -33.556 27.525  8.581   1.00 19.87 ? 283 ASN A ND2 1 
ATOM   2297 N  N   . PRO A 1 284 ? -37.099 24.513  5.343   1.00 18.93 ? 284 PRO A N   1 
ATOM   2298 C  CA  . PRO A 1 284 ? -37.332 23.496  4.323   1.00 18.44 ? 284 PRO A CA  1 
ATOM   2299 C  C   . PRO A 1 284 ? -37.337 24.026  2.889   1.00 19.05 ? 284 PRO A C   1 
ATOM   2300 O  O   . PRO A 1 284 ? -37.130 23.230  1.998   1.00 20.44 ? 284 PRO A O   1 
ATOM   2301 C  CB  . PRO A 1 284 ? -38.732 22.959  4.614   1.00 18.72 ? 284 PRO A CB  1 
ATOM   2302 C  CG  . PRO A 1 284 ? -38.999 23.345  6.053   1.00 19.33 ? 284 PRO A CG  1 
ATOM   2303 C  CD  . PRO A 1 284 ? -38.203 24.611  6.304   1.00 18.86 ? 284 PRO A CD  1 
ATOM   2304 N  N   . HIS A 1 285 ? -37.606 25.320  2.702   1.00 19.71 ? 285 HIS A N   1 
ATOM   2305 C  CA  . HIS A 1 285 ? -37.485 26.018  1.395   1.00 19.94 ? 285 HIS A CA  1 
ATOM   2306 C  C   . HIS A 1 285 ? -36.026 25.946  0.925   1.00 20.51 ? 285 HIS A C   1 
ATOM   2307 O  O   . HIS A 1 285 ? -35.797 25.631  -0.250  1.00 21.51 ? 285 HIS A O   1 
ATOM   2308 C  CB  . HIS A 1 285 ? -37.983 27.467  1.489   1.00 20.13 ? 285 HIS A CB  1 
ATOM   2309 C  CG  . HIS A 1 285 ? -39.463 27.634  1.378   1.00 20.59 ? 285 HIS A CG  1 
ATOM   2310 N  ND1 . HIS A 1 285 ? -40.242 26.878  0.509   1.00 20.69 ? 285 HIS A ND1 1 
ATOM   2311 C  CD2 . HIS A 1 285 ? -40.303 28.508  1.976   1.00 21.36 ? 285 HIS A CD2 1 
ATOM   2312 C  CE1 . HIS A 1 285 ? -41.496 27.247  0.617   1.00 20.34 ? 285 HIS A CE1 1 
ATOM   2313 N  NE2 . HIS A 1 285 ? -41.557 28.276  1.489   1.00 20.56 ? 285 HIS A NE2 1 
ATOM   2314 N  N   . VAL A 1 286 ? -35.090 26.225  1.838   1.00 20.93 ? 286 VAL A N   1 
ATOM   2315 C  CA  . VAL A 1 286 ? -33.613 26.178  1.614   1.00 19.81 ? 286 VAL A CA  1 
ATOM   2316 C  C   . VAL A 1 286 ? -33.190 24.716  1.440   1.00 20.13 ? 286 VAL A C   1 
ATOM   2317 O  O   . VAL A 1 286 ? -32.421 24.424  0.500   1.00 21.99 ? 286 VAL A O   1 
ATOM   2318 C  CB  . VAL A 1 286 ? -32.847 26.833  2.770   1.00 18.74 ? 286 VAL A CB  1 
ATOM   2319 C  CG1 . VAL A 1 286 ? -31.364 26.854  2.482   1.00 18.29 ? 286 VAL A CG1 1 
ATOM   2320 C  CG2 . VAL A 1 286 ? -33.374 28.231  3.068   1.00 19.68 ? 286 VAL A CG2 1 
ATOM   2321 N  N   . LEU A 1 287 ? -33.760 23.811  2.231   1.00 19.37 ? 287 LEU A N   1 
ATOM   2322 C  CA  . LEU A 1 287 ? -33.453 22.362  2.108   1.00 19.75 ? 287 LEU A CA  1 
ATOM   2323 C  C   . LEU A 1 287 ? -33.842 21.898  0.710   1.00 20.05 ? 287 LEU A C   1 
ATOM   2324 O  O   . LEU A 1 287 ? -33.096 21.098  0.138   1.00 23.26 ? 287 LEU A O   1 
ATOM   2325 C  CB  . LEU A 1 287 ? -34.194 21.568  3.186   1.00 19.70 ? 287 LEU A CB  1 
ATOM   2326 C  CG  . LEU A 1 287 ? -34.318 20.064  2.961   1.00 20.28 ? 287 LEU A CG  1 
ATOM   2327 C  CD1 . LEU A 1 287 ? -32.973 19.410  2.813   1.00 22.07 ? 287 LEU A CD1 1 
ATOM   2328 C  CD2 . LEU A 1 287 ? -35.040 19.433  4.124   1.00 23.01 ? 287 LEU A CD2 1 
ATOM   2329 N  N   . GLN A 1 288 ? -34.985 22.356  0.208   1.00 19.56 ? 288 GLN A N   1 
ATOM   2330 C  CA  . GLN A 1 288 ? -35.559 21.863  -1.059  1.00 20.22 ? 288 GLN A CA  1 
ATOM   2331 C  C   . GLN A 1 288 ? -34.657 22.354  -2.203  1.00 19.60 ? 288 GLN A C   1 
ATOM   2332 O  O   . GLN A 1 288 ? -34.351 21.547  -3.097  1.00 19.43 ? 288 GLN A O   1 
ATOM   2333 C  CB  . GLN A 1 288 ? -37.023 22.296  -1.108  1.00 22.86 ? 288 GLN A CB  1 
ATOM   2334 C  CG  . GLN A 1 288 ? -37.658 22.220  -2.481  1.00 25.32 ? 288 GLN A CG  1 
ATOM   2335 C  CD  . GLN A 1 288 ? -37.499 20.843  -3.051  1.00 28.81 ? 288 GLN A CD  1 
ATOM   2336 O  OE1 . GLN A 1 288 ? -37.601 19.832  -2.346  1.00 32.81 ? 288 GLN A OE1 1 
ATOM   2337 N  NE2 . GLN A 1 288 ? -37.235 20.816  -4.344  1.00 29.88 ? 288 GLN A NE2 1 
ATOM   2338 N  N   . LYS A 1 289 ? -34.202 23.605  -2.131  1.00 18.79 ? 289 LYS A N   1 
ATOM   2339 C  CA  . LYS A 1 289 ? -33.257 24.224  -3.097  1.00 19.64 ? 289 LYS A CA  1 
ATOM   2340 C  C   . LYS A 1 289 ? -31.893 23.506  -3.098  1.00 20.69 ? 289 LYS A C   1 
ATOM   2341 O  O   . LYS A 1 289 ? -31.368 23.198  -4.192  1.00 21.95 ? 289 LYS A O   1 
ATOM   2342 C  CB  . LYS A 1 289 ? -33.082 25.698  -2.732  1.00 19.45 ? 289 LYS A CB  1 
ATOM   2343 C  CG  . LYS A 1 289 ? -34.085 26.631  -3.381  1.00 20.25 ? 289 LYS A CG  1 
ATOM   2344 C  CD  . LYS A 1 289 ? -33.923 28.105  -3.005  1.00 20.03 ? 289 LYS A CD  1 
ATOM   2345 C  CE  . LYS A 1 289 ? -34.551 28.459  -1.674  1.00 19.42 ? 289 LYS A CE  1 
ATOM   2346 N  NZ  . LYS A 1 289 ? -34.667 29.924  -1.487  1.00 19.54 ? 289 LYS A NZ  1 
ATOM   2347 N  N   . ALA A 1 290 ? -31.299 23.277  -1.929  1.00 18.32 ? 290 ALA A N   1 
ATOM   2348 C  CA  . ALA A 1 290 ? -30.036 22.518  -1.798  1.00 18.46 ? 290 ALA A CA  1 
ATOM   2349 C  C   . ALA A 1 290 ? -30.166 21.130  -2.459  1.00 17.63 ? 290 ALA A C   1 
ATOM   2350 O  O   . ALA A 1 290 ? -29.286 20.749  -3.236  1.00 16.08 ? 290 ALA A O   1 
ATOM   2351 C  CB  . ALA A 1 290 ? -29.678 22.406  -0.324  1.00 18.43 ? 290 ALA A CB  1 
ATOM   2352 N  N   . ALA A 1 291 ? -31.239 20.401  -2.130  1.00 18.67 ? 291 ALA A N   1 
ATOM   2353 C  CA  . ALA A 1 291 ? -31.578 19.026  -2.574  1.00 17.87 ? 291 ALA A CA  1 
ATOM   2354 C  C   . ALA A 1 291 ? -31.787 18.928  -4.100  1.00 18.11 ? 291 ALA A C   1 
ATOM   2355 O  O   . ALA A 1 291 ? -31.355 17.936  -4.684  1.00 18.39 ? 291 ALA A O   1 
ATOM   2356 C  CB  . ALA A 1 291 ? -32.802 18.595  -1.821  1.00 17.44 ? 291 ALA A CB  1 
ATOM   2357 N  N   . GLU A 1 292 ? -32.399 19.932  -4.725  1.00 19.23 ? 292 GLU A N   1 
ATOM   2358 C  CA  . GLU A 1 292 ? -32.622 20.015  -6.190  1.00 20.19 ? 292 GLU A CA  1 
ATOM   2359 C  C   . GLU A 1 292 ? -31.261 20.115  -6.885  1.00 18.81 ? 292 GLU A C   1 
ATOM   2360 O  O   . GLU A 1 292 ? -31.026 19.354  -7.835  1.00 18.80 ? 292 GLU A O   1 
ATOM   2361 C  CB  . GLU A 1 292 ? -33.541 21.200  -6.515  1.00 22.41 ? 292 GLU A CB  1 
ATOM   2362 C  CG  . GLU A 1 292 ? -33.806 21.384  -8.007  1.00 22.96 ? 292 GLU A CG  1 
ATOM   2363 C  CD  . GLU A 1 292 ? -32.705 22.041  -8.841  1.00 25.51 ? 292 GLU A CD  1 
ATOM   2364 O  OE1 . GLU A 1 292 ? -31.931 22.924  -8.328  1.00 26.04 ? 292 GLU A OE1 1 
ATOM   2365 O  OE2 . GLU A 1 292 ? -32.624 21.697  -10.038 1.00 28.44 ? 292 GLU A OE2 1 
ATOM   2366 N  N   . GLU A 1 293 ? -30.390 20.995  -6.395  1.00 19.40 ? 293 GLU A N   1 
ATOM   2367 C  CA  . GLU A 1 293 ? -28.981 21.143  -6.856  1.00 19.14 ? 293 GLU A CA  1 
ATOM   2368 C  C   . GLU A 1 293 ? -28.223 19.814  -6.727  1.00 19.48 ? 293 GLU A C   1 
ATOM   2369 O  O   . GLU A 1 293 ? -27.647 19.349  -7.741  1.00 20.21 ? 293 GLU A O   1 
ATOM   2370 C  CB  . GLU A 1 293 ? -28.247 22.232  -6.083  1.00 19.44 ? 293 GLU A CB  1 
ATOM   2371 C  CG  . GLU A 1 293 ? -26.796 22.389  -6.557  1.00 20.55 ? 293 GLU A CG  1 
ATOM   2372 C  CD  . GLU A 1 293 ? -25.960 23.467  -5.885  1.00 21.32 ? 293 GLU A CD  1 
ATOM   2373 O  OE1 . GLU A 1 293 ? -25.443 23.206  -4.754  1.00 20.41 ? 293 GLU A OE1 1 
ATOM   2374 O  OE2 . GLU A 1 293 ? -25.827 24.586  -6.500  1.00 22.04 ? 293 GLU A OE2 1 
ATOM   2375 N  N   . ALA A 1 294 ? -28.222 19.210  -5.542  1.00 18.59 ? 294 ALA A N   1 
ATOM   2376 C  CA  . ALA A 1 294 ? -27.574 17.900  -5.318  1.00 19.26 ? 294 ALA A CA  1 
ATOM   2377 C  C   . ALA A 1 294 ? -28.074 16.925  -6.377  1.00 19.62 ? 294 ALA A C   1 
ATOM   2378 O  O   . ALA A 1 294 ? -27.263 16.141  -6.895  1.00 20.25 ? 294 ALA A O   1 
ATOM   2379 C  CB  . ALA A 1 294 ? -27.899 17.363  -3.948  1.00 19.85 ? 294 ALA A CB  1 
ATOM   2380 N  N   . ALA A 1 295 ? -29.382 16.925  -6.641  1.00 19.11 ? 295 ALA A N   1 
ATOM   2381 C  CA  . ALA A 1 295 ? -30.015 15.912  -7.501  1.00 19.63 ? 295 ALA A CA  1 
ATOM   2382 C  C   . ALA A 1 295 ? -29.577 16.185  -8.941  1.00 20.05 ? 295 ALA A C   1 
ATOM   2383 O  O   . ALA A 1 295 ? -29.148 15.237  -9.633  1.00 18.82 ? 295 ALA A O   1 
ATOM   2384 C  CB  . ALA A 1 295 ? -31.511 15.955  -7.312  1.00 20.76 ? 295 ALA A CB  1 
ATOM   2385 N  N   . ARG A 1 296 ? -29.596 17.458  -9.338  1.00 19.43 ? 296 ARG A N   1 
ATOM   2386 C  CA  . ARG A 1 296 ? -29.309 17.890  -10.726 1.00 20.09 ? 296 ARG A CA  1 
ATOM   2387 C  C   . ARG A 1 296 ? -27.805 17.783  -11.033 1.00 20.91 ? 296 ARG A C   1 
ATOM   2388 O  O   . ARG A 1 296 ? -27.439 17.561  -12.220 1.00 19.37 ? 296 ARG A O   1 
ATOM   2389 C  CB  . ARG A 1 296 ? -29.820 19.320  -10.906 1.00 21.17 ? 296 ARG A CB  1 
ATOM   2390 C  CG  . ARG A 1 296 ? -29.553 19.893  -12.289 1.00 22.85 ? 296 ARG A CG  1 
ATOM   2391 C  CD  . ARG A 1 296 ? -30.084 21.298  -12.466 1.00 23.86 ? 296 ARG A CD  1 
ATOM   2392 N  NE  . ARG A 1 296 ? -30.136 22.014  -11.191 1.00 22.63 ? 296 ARG A NE  1 
ATOM   2393 C  CZ  . ARG A 1 296 ? -29.264 22.927  -10.790 1.00 22.81 ? 296 ARG A CZ  1 
ATOM   2394 N  NH1 . ARG A 1 296 ? -28.232 23.257  -11.555 1.00 21.81 ? 296 ARG A NH1 1 
ATOM   2395 N  NH2 . ARG A 1 296 ? -29.437 23.517  -9.615  1.00 22.16 ? 296 ARG A NH2 1 
ATOM   2396 N  N   . VAL A 1 297 ? -26.931 17.969  -10.042 1.00 19.67 ? 297 VAL A N   1 
ATOM   2397 C  CA  . VAL A 1 297 ? -25.465 18.041  -10.326 1.00 19.20 ? 297 VAL A CA  1 
ATOM   2398 C  C   . VAL A 1 297 ? -24.812 16.657  -10.179 1.00 19.04 ? 297 VAL A C   1 
ATOM   2399 O  O   . VAL A 1 297 ? -24.054 16.284  -11.060 1.00 19.21 ? 297 VAL A O   1 
ATOM   2400 C  CB  . VAL A 1 297 ? -24.785 19.097  -9.452  1.00 18.51 ? 297 VAL A CB  1 
ATOM   2401 C  CG1 . VAL A 1 297 ? -23.278 19.019  -9.578  1.00 19.89 ? 297 VAL A CG1 1 
ATOM   2402 C  CG2 . VAL A 1 297 ? -25.283 20.497  -9.798  1.00 19.41 ? 297 VAL A CG2 1 
ATOM   2403 N  N   . LEU A 1 298 ? -25.132 15.918  -9.121  1.00 20.38 ? 298 LEU A N   1 
ATOM   2404 C  CA  . LEU A 1 298 ? -24.491 14.634  -8.745  1.00 20.04 ? 298 LEU A CA  1 
ATOM   2405 C  C   . LEU A 1 298 ? -25.132 13.480  -9.527  1.00 23.23 ? 298 LEU A C   1 
ATOM   2406 O  O   . LEU A 1 298 ? -25.722 12.541  -8.933  1.00 23.35 ? 298 LEU A O   1 
ATOM   2407 C  CB  . LEU A 1 298 ? -24.617 14.490  -7.233  1.00 18.50 ? 298 LEU A CB  1 
ATOM   2408 C  CG  . LEU A 1 298 ? -23.941 15.625  -6.474  1.00 19.14 ? 298 LEU A CG  1 
ATOM   2409 C  CD1 . LEU A 1 298 ? -24.081 15.469  -4.955  1.00 18.68 ? 298 LEU A CD1 1 
ATOM   2410 C  CD2 . LEU A 1 298 ? -22.475 15.709  -6.890  1.00 19.00 ? 298 LEU A CD2 1 
ATOM   2411 N  N   . VAL A 1 299 ? -24.934 13.497  -10.837 1.00 26.08 ? 299 VAL A N   1 
ATOM   2412 C  CA  . VAL A 1 299 ? -25.630 12.559  -11.757 1.00 29.14 ? 299 VAL A CA  1 
ATOM   2413 C  C   . VAL A 1 299 ? -24.916 11.203  -11.783 1.00 28.25 ? 299 VAL A C   1 
ATOM   2414 O  O   . VAL A 1 299 ? -25.517 10.284  -12.343 1.00 28.39 ? 299 VAL A O   1 
ATOM   2415 C  CB  . VAL A 1 299 ? -25.757 13.175  -13.161 1.00 31.72 ? 299 VAL A CB  1 
ATOM   2416 C  CG1 . VAL A 1 299 ? -26.507 14.502  -13.101 1.00 32.28 ? 299 VAL A CG1 1 
ATOM   2417 C  CG2 . VAL A 1 299 ? -24.398 13.343  -13.841 1.00 33.04 ? 299 VAL A CG2 1 
ATOM   2418 N  N   . ASP A 1 300 ? -23.708 11.077  -11.224 1.00 28.05 ? 300 ASP A N   1 
ATOM   2419 C  CA  . ASP A 1 300 ? -22.954 9.791   -11.176 1.00 28.69 ? 300 ASP A CA  1 
ATOM   2420 C  C   . ASP A 1 300 ? -23.015 9.215   -9.770  1.00 27.85 ? 300 ASP A C   1 
ATOM   2421 O  O   . ASP A 1 300 ? -23.164 9.942   -8.797  1.00 28.76 ? 300 ASP A O   1 
ATOM   2422 C  CB  . ASP A 1 300 ? -21.480 9.918   -11.565 1.00 28.96 ? 300 ASP A CB  1 
ATOM   2423 C  CG  . ASP A 1 300 ? -21.277 10.477  -12.954 1.00 29.71 ? 300 ASP A CG  1 
ATOM   2424 O  OD1 . ASP A 1 300 ? -21.756 9.851   -13.918 1.00 29.55 ? 300 ASP A OD1 1 
ATOM   2425 O  OD2 . ASP A 1 300 ? -20.681 11.555  -13.053 1.00 31.29 ? 300 ASP A OD2 1 
ATOM   2426 N  N   . PRO A 1 301 ? -22.891 7.881   -9.645  1.00 29.70 ? 301 PRO A N   1 
ATOM   2427 C  CA  . PRO A 1 301 ? -22.975 7.206   -8.344  1.00 31.80 ? 301 PRO A CA  1 
ATOM   2428 C  C   . PRO A 1 301 ? -21.989 7.736   -7.287  1.00 31.96 ? 301 PRO A C   1 
ATOM   2429 O  O   . PRO A 1 301 ? -22.323 7.735   -6.091  1.00 28.83 ? 301 PRO A O   1 
ATOM   2430 C  CB  . PRO A 1 301 ? -22.626 5.748   -8.692  1.00 31.91 ? 301 PRO A CB  1 
ATOM   2431 C  CG  . PRO A 1 301 ? -22.974 5.595   -10.168 1.00 32.17 ? 301 PRO A CG  1 
ATOM   2432 C  CD  . PRO A 1 301 ? -22.704 6.950   -10.772 1.00 30.67 ? 301 PRO A CD  1 
ATOM   2433 N  N   . VAL A 1 302 ? -20.799 8.138   -7.761  1.00 32.91 ? 302 VAL A N   1 
ATOM   2434 C  CA  . VAL A 1 302 ? -19.677 8.741   -6.974  1.00 33.84 ? 302 VAL A CA  1 
ATOM   2435 C  C   . VAL A 1 302 ? -19.400 10.151  -7.503  1.00 32.02 ? 302 VAL A C   1 
ATOM   2436 O  O   . VAL A 1 302 ? -19.090 10.330  -8.686  1.00 31.71 ? 302 VAL A O   1 
ATOM   2437 C  CB  . VAL A 1 302 ? -18.431 7.835   -7.056  1.00 35.81 ? 302 VAL A CB  1 
ATOM   2438 C  CG1 . VAL A 1 302 ? -17.145 8.561   -6.715  1.00 36.03 ? 302 VAL A CG1 1 
ATOM   2439 C  CG2 . VAL A 1 302 ? -18.597 6.594   -6.188  1.00 38.96 ? 302 VAL A CG2 1 
ATOM   2440 N  N   . PRO A 1 303 ? -19.511 11.197  -6.646  1.00 27.56 ? 303 PRO A N   1 
ATOM   2441 C  CA  . PRO A 1 303 ? -19.174 12.564  -7.037  1.00 23.57 ? 303 PRO A CA  1 
ATOM   2442 C  C   . PRO A 1 303 ? -17.727 12.732  -7.520  1.00 22.26 ? 303 PRO A C   1 
ATOM   2443 O  O   . PRO A 1 303 ? -16.842 12.282  -6.822  1.00 23.53 ? 303 PRO A O   1 
ATOM   2444 C  CB  . PRO A 1 303 ? -19.305 13.313  -5.707  1.00 24.48 ? 303 PRO A CB  1 
ATOM   2445 C  CG  . PRO A 1 303 ? -20.301 12.538  -4.951  1.00 23.77 ? 303 PRO A CG  1 
ATOM   2446 C  CD  . PRO A 1 303 ? -19.951 11.109  -5.250  1.00 25.27 ? 303 PRO A CD  1 
ATOM   2447 N  N   . SER A 1 304 ? -17.523 13.388  -8.661  1.00 19.68 ? 304 SER A N   1 
ATOM   2448 C  CA  . SER A 1 304 ? -16.200 13.821  -9.166  1.00 18.10 ? 304 SER A CA  1 
ATOM   2449 C  C   . SER A 1 304 ? -15.787 15.107  -8.451  1.00 19.45 ? 304 SER A C   1 
ATOM   2450 O  O   . SER A 1 304 ? -16.673 15.803  -7.970  1.00 19.26 ? 304 SER A O   1 
ATOM   2451 C  CB  . SER A 1 304 ? -16.266 14.079  -10.634 1.00 18.23 ? 304 SER A CB  1 
ATOM   2452 O  OG  . SER A 1 304 ? -17.037 15.260  -10.903 1.00 18.25 ? 304 SER A OG  1 
ATOM   2453 N  N   . TYR A 1 305 ? -14.497 15.466  -8.494  1.00 20.80 ? 305 TYR A N   1 
ATOM   2454 C  CA  . TYR A 1 305 ? -13.960 16.749  -7.979  1.00 22.00 ? 305 TYR A CA  1 
ATOM   2455 C  C   . TYR A 1 305 ? -14.751 17.882  -8.632  1.00 24.17 ? 305 TYR A C   1 
ATOM   2456 O  O   . TYR A 1 305 ? -15.344 18.741  -7.930  1.00 23.18 ? 305 TYR A O   1 
ATOM   2457 C  CB  . TYR A 1 305 ? -12.468 16.890  -8.312  1.00 22.03 ? 305 TYR A CB  1 
ATOM   2458 C  CG  . TYR A 1 305 ? -11.900 18.270  -8.085  1.00 22.35 ? 305 TYR A CG  1 
ATOM   2459 C  CD1 . TYR A 1 305 ? -11.515 18.690  -6.820  1.00 22.99 ? 305 TYR A CD1 1 
ATOM   2460 C  CD2 . TYR A 1 305 ? -11.773 19.176  -9.131  1.00 22.47 ? 305 TYR A CD2 1 
ATOM   2461 C  CE1 . TYR A 1 305 ? -10.996 19.960  -6.602  1.00 22.80 ? 305 TYR A CE1 1 
ATOM   2462 C  CE2 . TYR A 1 305 ? -11.266 20.448  -8.931  1.00 22.43 ? 305 TYR A CE2 1 
ATOM   2463 C  CZ  . TYR A 1 305 ? -10.874 20.840  -7.660  1.00 23.18 ? 305 TYR A CZ  1 
ATOM   2464 O  OH  . TYR A 1 305 ? -10.345 22.081  -7.462  1.00 23.37 ? 305 TYR A OH  1 
ATOM   2465 N  N   . LYS A 1 306 ? -14.740 17.873  -9.969  1.00 27.27 ? 306 LYS A N   1 
ATOM   2466 C  CA  . LYS A 1 306 ? -15.381 18.897  -10.829 1.00 29.18 ? 306 LYS A CA  1 
ATOM   2467 C  C   . LYS A 1 306 ? -16.820 19.085  -10.330 1.00 28.17 ? 306 LYS A C   1 
ATOM   2468 O  O   . LYS A 1 306 ? -17.246 20.248  -10.191 1.00 25.93 ? 306 LYS A O   1 
ATOM   2469 C  CB  . LYS A 1 306 ? -15.304 18.460  -12.297 1.00 31.48 ? 306 LYS A CB  1 
ATOM   2470 C  CG  . LYS A 1 306 ? -15.705 19.497  -13.330 1.00 34.35 ? 306 LYS A CG  1 
ATOM   2471 C  CD  . LYS A 1 306 ? -16.218 18.848  -14.600 1.00 39.32 ? 306 LYS A CD  1 
ATOM   2472 C  CE  . LYS A 1 306 ? -16.616 19.854  -15.659 1.00 43.80 ? 306 LYS A CE  1 
ATOM   2473 N  NZ  . LYS A 1 306 ? -15.465 20.709  -16.044 1.00 47.45 ? 306 LYS A NZ  1 
ATOM   2474 N  N   . GLN A 1 307 ? -17.518 17.978  -10.032 1.00 26.60 ? 307 GLN A N   1 
ATOM   2475 C  CA  . GLN A 1 307 ? -18.954 18.012  -9.662  1.00 25.20 ? 307 GLN A CA  1 
ATOM   2476 C  C   . GLN A 1 307 ? -19.129 18.672  -8.294  1.00 23.58 ? 307 GLN A C   1 
ATOM   2477 O  O   . GLN A 1 307 ? -20.185 19.288  -8.076  1.00 25.65 ? 307 GLN A O   1 
ATOM   2478 C  CB  . GLN A 1 307 ? -19.566 16.624  -9.725  1.00 24.95 ? 307 GLN A CB  1 
ATOM   2479 C  CG  . GLN A 1 307 ? -19.832 16.164  -11.148 1.00 24.35 ? 307 GLN A CG  1 
ATOM   2480 C  CD  . GLN A 1 307 ? -20.229 14.707  -11.142 1.00 25.04 ? 307 GLN A CD  1 
ATOM   2481 O  OE1 . GLN A 1 307 ? -20.040 14.002  -10.147 1.00 23.71 ? 307 GLN A OE1 1 
ATOM   2482 N  NE2 . GLN A 1 307 ? -20.813 14.261  -12.241 1.00 24.13 ? 307 GLN A NE2 1 
ATOM   2483 N  N   . VAL A 1 308 ? -18.133 18.603  -7.424  1.00 21.93 ? 308 VAL A N   1 
ATOM   2484 C  CA  . VAL A 1 308 ? -18.225 19.245  -6.083  1.00 21.31 ? 308 VAL A CA  1 
ATOM   2485 C  C   . VAL A 1 308 ? -18.094 20.756  -6.271  1.00 20.99 ? 308 VAL A C   1 
ATOM   2486 O  O   . VAL A 1 308 ? -18.917 21.498  -5.701  1.00 19.24 ? 308 VAL A O   1 
ATOM   2487 C  CB  . VAL A 1 308 ? -17.198 18.651  -5.097  1.00 21.40 ? 308 VAL A CB  1 
ATOM   2488 C  CG1 . VAL A 1 308 ? -17.202 19.347  -3.745  1.00 20.69 ? 308 VAL A CG1 1 
ATOM   2489 C  CG2 . VAL A 1 308 ? -17.430 17.153  -4.917  1.00 22.21 ? 308 VAL A CG2 1 
ATOM   2490 N  N   . LYS A 1 309 ? -17.151 21.190  -7.105  1.00 23.51 ? 309 LYS A N   1 
ATOM   2491 C  CA  . LYS A 1 309 ? -16.969 22.625  -7.467  1.00 25.30 ? 309 LYS A CA  1 
ATOM   2492 C  C   . LYS A 1 309 ? -18.281 23.224  -7.999  1.00 25.35 ? 309 LYS A C   1 
ATOM   2493 O  O   . LYS A 1 309 ? -18.460 24.428  -7.856  1.00 28.68 ? 309 LYS A O   1 
ATOM   2494 C  CB  . LYS A 1 309 ? -15.876 22.802  -8.524  1.00 24.91 ? 309 LYS A CB  1 
ATOM   2495 C  CG  . LYS A 1 309 ? -14.494 22.339  -8.117  1.00 27.11 ? 309 LYS A CG  1 
ATOM   2496 C  CD  . LYS A 1 309 ? -14.027 22.884  -6.766  1.00 27.30 ? 309 LYS A CD  1 
ATOM   2497 C  CE  . LYS A 1 309 ? -14.270 21.906  -5.628  1.00 28.69 ? 309 LYS A CE  1 
ATOM   2498 N  NZ  . LYS A 1 309 ? -13.503 22.230  -4.392  1.00 26.72 ? 309 LYS A NZ  1 
ATOM   2499 N  N   . GLN A 1 310 ? -19.142 22.433  -8.635  1.00 26.43 ? 310 GLN A N   1 
ATOM   2500 C  CA  . GLN A 1 310 ? -20.372 22.940  -9.308  1.00 25.99 ? 310 GLN A CA  1 
ATOM   2501 C  C   . GLN A 1 310 ? -21.527 23.071  -8.309  1.00 24.19 ? 310 GLN A C   1 
ATOM   2502 O  O   . GLN A 1 310 ? -22.542 23.647  -8.723  1.00 27.38 ? 310 GLN A O   1 
ATOM   2503 C  CB  . GLN A 1 310 ? -20.764 22.021  -10.457 1.00 26.13 ? 310 GLN A CB  1 
ATOM   2504 C  CG  . GLN A 1 310 ? -19.713 21.989  -11.548 1.00 30.54 ? 310 GLN A CG  1 
ATOM   2505 C  CD  . GLN A 1 310 ? -20.034 21.018  -12.668 1.00 33.73 ? 310 GLN A CD  1 
ATOM   2506 O  OE1 . GLN A 1 310 ? -20.806 20.069  -12.505 1.00 32.64 ? 310 GLN A OE1 1 
ATOM   2507 N  NE2 . GLN A 1 310 ? -19.433 21.259  -13.827 1.00 33.55 ? 310 GLN A NE2 1 
ATOM   2508 N  N   . LEU A 1 311 ? -21.376 22.597  -7.058  1.00 22.75 ? 311 LEU A N   1 
ATOM   2509 C  CA  . LEU A 1 311 ? -22.409 22.672  -5.974  1.00 21.19 ? 311 LEU A CA  1 
ATOM   2510 C  C   . LEU A 1 311 ? -22.377 24.048  -5.311  1.00 19.87 ? 311 LEU A C   1 
ATOM   2511 O  O   . LEU A 1 311 ? -22.091 24.128  -4.096  1.00 19.96 ? 311 LEU A O   1 
ATOM   2512 C  CB  . LEU A 1 311 ? -22.184 21.591  -4.915  1.00 20.87 ? 311 LEU A CB  1 
ATOM   2513 C  CG  . LEU A 1 311 ? -22.343 20.148  -5.374  1.00 21.94 ? 311 LEU A CG  1 
ATOM   2514 C  CD1 . LEU A 1 311 ? -21.939 19.185  -4.258  1.00 22.13 ? 311 LEU A CD1 1 
ATOM   2515 C  CD2 . LEU A 1 311 ? -23.765 19.884  -5.863  1.00 21.10 ? 311 LEU A CD2 1 
ATOM   2516 N  N   . LYS A 1 312 ? -22.715 25.078  -6.083  1.00 19.50 ? 312 LYS A N   1 
ATOM   2517 C  CA  . LYS A 1 312 ? -22.639 26.510  -5.697  1.00 19.91 ? 312 LYS A CA  1 
ATOM   2518 C  C   . LYS A 1 312 ? -23.583 26.770  -4.530  1.00 18.42 ? 312 LYS A C   1 
ATOM   2519 O  O   . LYS A 1 312 ? -23.162 27.412  -3.568  1.00 18.33 ? 312 LYS A O   1 
ATOM   2520 C  CB  . LYS A 1 312 ? -22.979 27.404  -6.896  1.00 21.09 ? 312 LYS A CB  1 
ATOM   2521 C  CG  . LYS A 1 312 ? -21.947 27.356  -8.020  1.00 23.64 ? 312 LYS A CG  1 
ATOM   2522 C  CD  . LYS A 1 312 ? -20.532 27.300  -7.470  1.00 25.99 ? 312 LYS A CD  1 
ATOM   2523 C  CE  . LYS A 1 312 ? -19.588 28.297  -8.093  1.00 29.20 ? 312 LYS A CE  1 
ATOM   2524 N  NZ  . LYS A 1 312 ? -18.394 28.494  -7.234  1.00 30.40 ? 312 LYS A NZ  1 
ATOM   2525 N  N   . TYR A 1 313 ? -24.818 26.306  -4.634  1.00 16.70 ? 313 TYR A N   1 
ATOM   2526 C  CA  . TYR A 1 313 ? -25.834 26.622  -3.614  1.00 17.04 ? 313 TYR A CA  1 
ATOM   2527 C  C   . TYR A 1 313 ? -25.447 25.865  -2.346  1.00 16.61 ? 313 TYR A C   1 
ATOM   2528 O  O   . TYR A 1 313 ? -25.572 26.463  -1.258  1.00 14.42 ? 313 TYR A O   1 
ATOM   2529 C  CB  . TYR A 1 313 ? -27.265 26.353  -4.105  1.00 17.11 ? 313 TYR A CB  1 
ATOM   2530 C  CG  . TYR A 1 313 ? -28.303 26.918  -3.170  1.00 17.00 ? 313 TYR A CG  1 
ATOM   2531 C  CD1 . TYR A 1 313 ? -28.770 26.165  -2.106  1.00 17.12 ? 313 TYR A CD1 1 
ATOM   2532 C  CD2 . TYR A 1 313 ? -28.800 28.202  -3.319  1.00 17.01 ? 313 TYR A CD2 1 
ATOM   2533 C  CE1 . TYR A 1 313 ? -29.697 26.676  -1.213  1.00 16.87 ? 313 TYR A CE1 1 
ATOM   2534 C  CE2 . TYR A 1 313 ? -29.743 28.717  -2.440  1.00 17.21 ? 313 TYR A CE2 1 
ATOM   2535 C  CZ  . TYR A 1 313 ? -30.172 27.959  -1.364  1.00 17.21 ? 313 TYR A CZ  1 
ATOM   2536 O  OH  . TYR A 1 313 ? -31.064 28.432  -0.447  1.00 16.73 ? 313 TYR A OH  1 
ATOM   2537 N  N   . VAL A 1 314 ? -24.989 24.605  -2.469  1.00 17.14 ? 314 VAL A N   1 
ATOM   2538 C  CA  . VAL A 1 314 ? -24.533 23.861  -1.257  1.00 16.52 ? 314 VAL A CA  1 
ATOM   2539 C  C   . VAL A 1 314 ? -23.433 24.711  -0.620  1.00 16.64 ? 314 VAL A C   1 
ATOM   2540 O  O   . VAL A 1 314 ? -23.473 24.893  0.582   1.00 17.46 ? 314 VAL A O   1 
ATOM   2541 C  CB  . VAL A 1 314 ? -24.067 22.421  -1.520  1.00 15.83 ? 314 VAL A CB  1 
ATOM   2542 C  CG1 . VAL A 1 314 ? -23.466 21.816  -0.261  1.00 16.12 ? 314 VAL A CG1 1 
ATOM   2543 C  CG2 . VAL A 1 314 ? -25.186 21.532  -2.007  1.00 16.23 ? 314 VAL A CG2 1 
ATOM   2544 N  N   . GLY A 1 315 ? -22.533 25.267  -1.434  1.00 17.68 ? 315 GLY A N   1 
ATOM   2545 C  CA  . GLY A 1 315 ? -21.440 26.145  -0.980  1.00 17.87 ? 315 GLY A CA  1 
ATOM   2546 C  C   . GLY A 1 315 ? -21.996 27.356  -0.259  1.00 19.59 ? 315 GLY A C   1 
ATOM   2547 O  O   . GLY A 1 315 ? -21.411 27.745  0.798   1.00 20.60 ? 315 GLY A O   1 
ATOM   2548 N  N   . MET A 1 316 ? -23.093 27.919  -0.788  1.00 18.25 ? 316 MET A N   1 
ATOM   2549 C  CA  . MET A 1 316 ? -23.788 29.087  -0.197  1.00 19.78 ? 316 MET A CA  1 
ATOM   2550 C  C   . MET A 1 316 ? -24.435 28.726  1.154   1.00 20.16 ? 316 MET A C   1 
ATOM   2551 O  O   . MET A 1 316 ? -24.425 29.576  2.107   1.00 18.33 ? 316 MET A O   1 
ATOM   2552 C  CB  . MET A 1 316 ? -24.856 29.599  -1.162  1.00 20.89 ? 316 MET A CB  1 
ATOM   2553 C  CG  . MET A 1 316 ? -24.282 30.457  -2.275  1.00 21.70 ? 316 MET A CG  1 
ATOM   2554 S  SD  . MET A 1 316 ? -25.466 30.762  -3.593  1.00 22.89 ? 316 MET A SD  1 
ATOM   2555 C  CE  . MET A 1 316 ? -26.898 31.368  -2.688  1.00 21.99 ? 316 MET A CE  1 
ATOM   2556 N  N   . VAL A 1 317 ? -24.999 27.523  1.236   1.00 20.27 ? 317 VAL A N   1 
ATOM   2557 C  CA  . VAL A 1 317 ? -25.600 26.986  2.487   1.00 21.69 ? 317 VAL A CA  1 
ATOM   2558 C  C   . VAL A 1 317 ? -24.513 26.934  3.559   1.00 21.65 ? 317 VAL A C   1 
ATOM   2559 O  O   . VAL A 1 317 ? -24.759 27.420  4.695   1.00 21.68 ? 317 VAL A O   1 
ATOM   2560 C  CB  . VAL A 1 317 ? -26.263 25.615  2.265   1.00 20.75 ? 317 VAL A CB  1 
ATOM   2561 C  CG1 . VAL A 1 317 ? -26.583 24.924  3.583   1.00 19.87 ? 317 VAL A CG1 1 
ATOM   2562 C  CG2 . VAL A 1 317 ? -27.538 25.781  1.449   1.00 20.75 ? 317 VAL A CG2 1 
ATOM   2563 N  N   . LEU A 1 318 ? -23.347 26.411  3.193   1.00 20.62 ? 318 LEU A N   1 
ATOM   2564 C  CA  . LEU A 1 318 ? -22.226 26.232  4.145   1.00 20.61 ? 318 LEU A CA  1 
ATOM   2565 C  C   . LEU A 1 318 ? -21.768 27.596  4.696   1.00 18.94 ? 318 LEU A C   1 
ATOM   2566 O  O   . LEU A 1 318 ? -21.516 27.671  5.938   1.00 16.70 ? 318 LEU A O   1 
ATOM   2567 C  CB  . LEU A 1 318 ? -21.111 25.445  3.453   1.00 19.66 ? 318 LEU A CB  1 
ATOM   2568 C  CG  . LEU A 1 318 ? -21.414 23.963  3.212   1.00 20.03 ? 318 LEU A CG  1 
ATOM   2569 C  CD1 . LEU A 1 318 ? -20.296 23.297  2.405   1.00 20.72 ? 318 LEU A CD1 1 
ATOM   2570 C  CD2 . LEU A 1 318 ? -21.609 23.226  4.527   1.00 20.43 ? 318 LEU A CD2 1 
ATOM   2571 N  N   . ASN A 1 319 ? -21.709 28.629  3.841   1.00 17.57 ? 319 ASN A N   1 
ATOM   2572 C  CA  . ASN A 1 319 ? -21.201 29.977  4.214   1.00 17.06 ? 319 ASN A CA  1 
ATOM   2573 C  C   . ASN A 1 319 ? -22.164 30.635  5.196   1.00 17.35 ? 319 ASN A C   1 
ATOM   2574 O  O   . ASN A 1 319 ? -21.685 31.295  6.105   1.00 16.27 ? 319 ASN A O   1 
ATOM   2575 C  CB  . ASN A 1 319 ? -20.941 30.864  3.000   1.00 16.45 ? 319 ASN A CB  1 
ATOM   2576 C  CG  . ASN A 1 319 ? -19.582 30.594  2.400   1.00 16.34 ? 319 ASN A CG  1 
ATOM   2577 O  OD1 . ASN A 1 319 ? -18.717 30.066  3.085   1.00 16.28 ? 319 ASN A OD1 1 
ATOM   2578 N  ND2 . ASN A 1 319 ? -19.396 30.927  1.133   1.00 15.26 ? 319 ASN A ND2 1 
ATOM   2579 N  N   . GLU A 1 320 ? -23.459 30.376  5.021   1.00 18.16 ? 320 GLU A N   1 
ATOM   2580 C  CA  . GLU A 1 320 ? -24.548 30.995  5.793   1.00 20.02 ? 320 GLU A CA  1 
ATOM   2581 C  C   . GLU A 1 320 ? -24.644 30.283  7.138   1.00 19.83 ? 320 GLU A C   1 
ATOM   2582 O  O   . GLU A 1 320 ? -25.051 30.943  8.093   1.00 22.62 ? 320 GLU A O   1 
ATOM   2583 C  CB  . GLU A 1 320 ? -25.842 30.991  4.967   1.00 21.43 ? 320 GLU A CB  1 
ATOM   2584 C  CG  . GLU A 1 320 ? -27.059 31.597  5.660   1.00 22.53 ? 320 GLU A CG  1 
ATOM   2585 C  CD  . GLU A 1 320 ? -26.995 33.095  5.929   1.00 22.98 ? 320 GLU A CD  1 
ATOM   2586 O  OE1 . GLU A 1 320 ? -25.959 33.699  5.634   1.00 26.15 ? 320 GLU A OE1 1 
ATOM   2587 O  OE2 . GLU A 1 320 ? -27.967 33.657  6.456   1.00 21.12 ? 320 GLU A OE2 1 
ATOM   2588 N  N   . ALA A 1 321 ? -24.278 29.004  7.207   1.00 19.25 ? 321 ALA A N   1 
ATOM   2589 C  CA  . ALA A 1 321 ? -24.115 28.248  8.477   1.00 18.43 ? 321 ALA A CA  1 
ATOM   2590 C  C   . ALA A 1 321 ? -22.878 28.760  9.236   1.00 18.45 ? 321 ALA A C   1 
ATOM   2591 O  O   . ALA A 1 321 ? -22.942 28.880  10.469  1.00 19.08 ? 321 ALA A O   1 
ATOM   2592 C  CB  . ALA A 1 321 ? -24.018 26.770  8.203   1.00 17.37 ? 321 ALA A CB  1 
ATOM   2593 N  N   . LEU A 1 322 ? -21.800 29.070  8.517   1.00 18.89 ? 322 LEU A N   1 
ATOM   2594 C  CA  . LEU A 1 322 ? -20.558 29.632  9.095   1.00 19.94 ? 322 LEU A CA  1 
ATOM   2595 C  C   . LEU A 1 322 ? -20.790 31.075  9.521   1.00 20.45 ? 322 LEU A C   1 
ATOM   2596 O  O   . LEU A 1 322 ? -20.006 31.556  10.369  1.00 21.72 ? 322 LEU A O   1 
ATOM   2597 C  CB  . LEU A 1 322 ? -19.429 29.601  8.064   1.00 21.11 ? 322 LEU A CB  1 
ATOM   2598 C  CG  . LEU A 1 322 ? -18.700 28.279  7.843   1.00 19.69 ? 322 LEU A CG  1 
ATOM   2599 C  CD1 . LEU A 1 322 ? -17.681 28.474  6.739   1.00 19.88 ? 322 LEU A CD1 1 
ATOM   2600 C  CD2 . LEU A 1 322 ? -18.044 27.752  9.108   1.00 19.83 ? 322 LEU A CD2 1 
ATOM   2601 N  N   . ARG A 1 323 ? -21.759 31.767  8.914   1.00 18.74 ? 323 ARG A N   1 
ATOM   2602 C  CA  . ARG A 1 323 ? -22.084 33.143  9.345   1.00 18.77 ? 323 ARG A CA  1 
ATOM   2603 C  C   . ARG A 1 323 ? -22.726 33.061  10.739  1.00 19.21 ? 323 ARG A C   1 
ATOM   2604 O  O   . ARG A 1 323 ? -22.219 33.729  11.661  1.00 18.04 ? 323 ARG A O   1 
ATOM   2605 C  CB  . ARG A 1 323 ? -22.955 33.869  8.319   1.00 18.97 ? 323 ARG A CB  1 
ATOM   2606 C  CG  . ARG A 1 323 ? -23.095 35.361  8.582   1.00 17.83 ? 323 ARG A CG  1 
ATOM   2607 C  CD  . ARG A 1 323 ? -24.028 36.019  7.586   1.00 18.46 ? 323 ARG A CD  1 
ATOM   2608 N  NE  . ARG A 1 323 ? -25.405 35.575  7.773   1.00 18.96 ? 323 ARG A NE  1 
ATOM   2609 C  CZ  . ARG A 1 323 ? -26.231 36.003  8.721   1.00 17.87 ? 323 ARG A CZ  1 
ATOM   2610 N  NH1 . ARG A 1 323 ? -25.852 36.954  9.558   1.00 17.29 ? 323 ARG A NH1 1 
ATOM   2611 N  NH2 . ARG A 1 323 ? -27.453 35.505  8.788   1.00 18.01 ? 323 ARG A NH2 1 
ATOM   2612 N  N   . LEU A 1 324 ? -23.793 32.276  10.895  1.00 19.90 ? 324 LEU A N   1 
ATOM   2613 C  CA  . LEU A 1 324 ? -24.615 32.308  12.127  1.00 21.81 ? 324 LEU A CA  1 
ATOM   2614 C  C   . LEU A 1 324 ? -23.935 31.532  13.242  1.00 21.45 ? 324 LEU A C   1 
ATOM   2615 O  O   . LEU A 1 324 ? -23.972 32.040  14.361  1.00 22.58 ? 324 LEU A O   1 
ATOM   2616 C  CB  . LEU A 1 324 ? -26.012 31.774  11.839  1.00 24.40 ? 324 LEU A CB  1 
ATOM   2617 C  CG  . LEU A 1 324 ? -26.898 32.773  11.100  1.00 25.89 ? 324 LEU A CG  1 
ATOM   2618 C  CD1 . LEU A 1 324 ? -28.095 32.077  10.468  1.00 26.41 ? 324 LEU A CD1 1 
ATOM   2619 C  CD2 . LEU A 1 324 ? -27.334 33.888  12.037  1.00 25.66 ? 324 LEU A CD2 1 
ATOM   2620 N  N   . TRP A 1 325 ? -23.310 30.391  12.955  1.00 21.17 ? 325 TRP A N   1 
ATOM   2621 C  CA  . TRP A 1 325 ? -22.602 29.583  13.988  1.00 22.14 ? 325 TRP A CA  1 
ATOM   2622 C  C   . TRP A 1 325 ? -21.238 29.126  13.474  1.00 23.81 ? 325 TRP A C   1 
ATOM   2623 O  O   . TRP A 1 325 ? -21.021 27.947  13.140  1.00 25.57 ? 325 TRP A O   1 
ATOM   2624 C  CB  . TRP A 1 325 ? -23.492 28.438  14.477  1.00 21.91 ? 325 TRP A CB  1 
ATOM   2625 C  CG  . TRP A 1 325 ? -24.643 28.966  15.274  1.00 21.95 ? 325 TRP A CG  1 
ATOM   2626 C  CD1 . TRP A 1 325 ? -25.961 28.930  14.935  1.00 20.95 ? 325 TRP A CD1 1 
ATOM   2627 C  CD2 . TRP A 1 325 ? -24.571 29.683  16.521  1.00 21.21 ? 325 TRP A CD2 1 
ATOM   2628 N  NE1 . TRP A 1 325 ? -26.714 29.536  15.908  1.00 21.67 ? 325 TRP A NE1 1 
ATOM   2629 C  CE2 . TRP A 1 325 ? -25.894 29.998  16.897  1.00 21.13 ? 325 TRP A CE2 1 
ATOM   2630 C  CE3 . TRP A 1 325 ? -23.535 30.031  17.386  1.00 21.06 ? 325 TRP A CE3 1 
ATOM   2631 C  CZ2 . TRP A 1 325 ? -26.203 30.683  18.073  1.00 21.42 ? 325 TRP A CZ2 1 
ATOM   2632 C  CZ3 . TRP A 1 325 ? -23.836 30.711  18.550  1.00 21.91 ? 325 TRP A CZ3 1 
ATOM   2633 C  CH2 . TRP A 1 325 ? -25.154 31.042  18.885  1.00 21.02 ? 325 TRP A CH2 1 
ATOM   2634 N  N   . PRO A 1 326 ? -20.282 30.084  13.366  1.00 22.84 ? 326 PRO A N   1 
ATOM   2635 C  CA  . PRO A 1 326 ? -18.897 29.759  13.030  1.00 21.27 ? 326 PRO A CA  1 
ATOM   2636 C  C   . PRO A 1 326 ? -18.391 28.755  14.079  1.00 21.28 ? 326 PRO A C   1 
ATOM   2637 O  O   . PRO A 1 326 ? -18.298 29.064  15.281  1.00 19.75 ? 326 PRO A O   1 
ATOM   2638 C  CB  . PRO A 1 326 ? -18.167 31.103  13.064  1.00 21.23 ? 326 PRO A CB  1 
ATOM   2639 C  CG  . PRO A 1 326 ? -19.083 32.014  13.877  1.00 21.16 ? 326 PRO A CG  1 
ATOM   2640 C  CD  . PRO A 1 326 ? -20.480 31.521  13.597  1.00 21.26 ? 326 PRO A CD  1 
ATOM   2641 N  N   . THR A 1 327 ? -18.191 27.524  13.632  1.00 20.09 ? 327 THR A N   1 
ATOM   2642 C  CA  . THR A 1 327 ? -17.902 26.400  14.547  1.00 19.29 ? 327 THR A CA  1 
ATOM   2643 C  C   . THR A 1 327 ? -16.590 26.703  15.289  1.00 19.05 ? 327 THR A C   1 
ATOM   2644 O  O   . THR A 1 327 ? -16.467 26.269  16.440  1.00 17.89 ? 327 THR A O   1 
ATOM   2645 C  CB  . THR A 1 327 ? -17.939 25.087  13.777  1.00 18.19 ? 327 THR A CB  1 
ATOM   2646 O  OG1 . THR A 1 327 ? -17.632 24.100  14.757  1.00 17.43 ? 327 THR A OG1 1 
ATOM   2647 C  CG2 . THR A 1 327 ? -16.962 25.062  12.622  1.00 18.74 ? 327 THR A CG2 1 
ATOM   2648 N  N   . ALA A 1 328 ? -15.653 27.425  14.663  1.00 18.30 ? 328 ALA A N   1 
ATOM   2649 C  CA  . ALA A 1 328 ? -14.480 28.028  15.344  1.00 18.42 ? 328 ALA A CA  1 
ATOM   2650 C  C   . ALA A 1 328 ? -14.838 29.485  15.606  1.00 17.67 ? 328 ALA A C   1 
ATOM   2651 O  O   . ALA A 1 328 ? -14.816 30.294  14.669  1.00 17.59 ? 328 ALA A O   1 
ATOM   2652 C  CB  . ALA A 1 328 ? -13.221 27.876  14.514  1.00 18.52 ? 328 ALA A CB  1 
ATOM   2653 N  N   . PRO A 1 329 ? -15.298 29.821  16.839  1.00 16.22 ? 329 PRO A N   1 
ATOM   2654 C  CA  . PRO A 1 329 ? -15.991 31.085  17.082  1.00 16.88 ? 329 PRO A CA  1 
ATOM   2655 C  C   . PRO A 1 329 ? -15.111 32.316  17.360  1.00 17.21 ? 329 PRO A C   1 
ATOM   2656 O  O   . PRO A 1 329 ? -15.638 33.456  17.459  1.00 16.89 ? 329 PRO A O   1 
ATOM   2657 C  CB  . PRO A 1 329 ? -16.866 30.689  18.307  1.00 17.40 ? 329 PRO A CB  1 
ATOM   2658 C  CG  . PRO A 1 329 ? -16.000 29.745  19.111  1.00 16.56 ? 329 PRO A CG  1 
ATOM   2659 C  CD  . PRO A 1 329 ? -15.281 28.956  18.031  1.00 16.60 ? 329 PRO A CD  1 
ATOM   2660 N  N   . ALA A 1 330 ? -13.803 32.115  17.516  1.00 17.39 ? 330 ALA A N   1 
ATOM   2661 C  CA  . ALA A 1 330 ? -12.918 33.178  18.043  1.00 19.78 ? 330 ALA A CA  1 
ATOM   2662 C  C   . ALA A 1 330 ? -11.479 33.041  17.541  1.00 19.96 ? 330 ALA A C   1 
ATOM   2663 O  O   . ALA A 1 330 ? -11.042 31.927  17.257  1.00 20.06 ? 330 ALA A O   1 
ATOM   2664 C  CB  . ALA A 1 330 ? -12.976 33.197  19.563  1.00 19.94 ? 330 ALA A CB  1 
ATOM   2665 N  N   . PHE A 1 331 ? -10.794 34.180  17.424  1.00 21.21 ? 331 PHE A N   1 
ATOM   2666 C  CA  . PHE A 1 331 ? -9.321  34.287  17.254  1.00 21.97 ? 331 PHE A CA  1 
ATOM   2667 C  C   . PHE A 1 331 ? -8.855  35.517  18.030  1.00 22.41 ? 331 PHE A C   1 
ATOM   2668 O  O   . PHE A 1 331 ? -9.583  36.543  18.103  1.00 23.20 ? 331 PHE A O   1 
ATOM   2669 C  CB  . PHE A 1 331 ? -8.927  34.271  15.771  1.00 21.09 ? 331 PHE A CB  1 
ATOM   2670 C  CG  . PHE A 1 331 ? -9.370  35.419  14.894  1.00 19.31 ? 331 PHE A CG  1 
ATOM   2671 C  CD1 . PHE A 1 331 ? -10.608 35.410  14.272  1.00 19.73 ? 331 PHE A CD1 1 
ATOM   2672 C  CD2 . PHE A 1 331 ? -8.499  36.454  14.577  1.00 19.24 ? 331 PHE A CD2 1 
ATOM   2673 C  CE1 . PHE A 1 331 ? -10.992 36.436  13.412  1.00 18.18 ? 331 PHE A CE1 1 
ATOM   2674 C  CE2 . PHE A 1 331 ? -8.881  37.472  13.707  1.00 18.99 ? 331 PHE A CE2 1 
ATOM   2675 C  CZ  . PHE A 1 331 ? -10.146 37.482  13.166  1.00 17.69 ? 331 PHE A CZ  1 
ATOM   2676 N  N   . SER A 1 332 ? -7.690  35.390  18.647  1.00 23.56 ? 332 SER A N   1 
ATOM   2677 C  CA  . SER A 1 332 ? -7.050  36.435  19.487  1.00 21.28 ? 332 SER A CA  1 
ATOM   2678 C  C   . SER A 1 332 ? -5.940  37.107  18.679  1.00 20.37 ? 332 SER A C   1 
ATOM   2679 O  O   . SER A 1 332 ? -5.284  36.420  17.883  1.00 19.59 ? 332 SER A O   1 
ATOM   2680 C  CB  . SER A 1 332 ? -6.495  35.838  20.762  1.00 19.83 ? 332 SER A CB  1 
ATOM   2681 O  OG  . SER A 1 332 ? -6.105  36.861  21.666  1.00 18.68 ? 332 SER A OG  1 
ATOM   2682 N  N   . LEU A 1 333 ? -5.678  38.374  18.979  1.00 20.22 ? 333 LEU A N   1 
ATOM   2683 C  CA  . LEU A 1 333 ? -4.588  39.185  18.399  1.00 19.36 ? 333 LEU A CA  1 
ATOM   2684 C  C   . LEU A 1 333 ? -3.940  40.029  19.498  1.00 20.37 ? 333 LEU A C   1 
ATOM   2685 O  O   . LEU A 1 333 ? -4.521  40.143  20.616  1.00 18.60 ? 333 LEU A O   1 
ATOM   2686 C  CB  . LEU A 1 333 ? -5.207  40.073  17.327  1.00 19.82 ? 333 LEU A CB  1 
ATOM   2687 C  CG  . LEU A 1 333 ? -5.857  39.319  16.176  1.00 19.71 ? 333 LEU A CG  1 
ATOM   2688 C  CD1 . LEU A 1 333 ? -7.053  40.085  15.685  1.00 19.97 ? 333 LEU A CD1 1 
ATOM   2689 C  CD2 . LEU A 1 333 ? -4.870  39.045  15.055  1.00 19.96 ? 333 LEU A CD2 1 
ATOM   2690 N  N   . TYR A 1 334 ? -2.752  40.570  19.215  1.00 20.08 ? 334 TYR A N   1 
ATOM   2691 C  CA  . TYR A 1 334 ? -2.058  41.488  20.151  1.00 19.37 ? 334 TYR A CA  1 
ATOM   2692 C  C   . TYR A 1 334 ? -1.637  42.691  19.330  1.00 19.17 ? 334 TYR A C   1 
ATOM   2693 O  O   . TYR A 1 334 ? -1.418  42.532  18.097  1.00 19.08 ? 334 TYR A O   1 
ATOM   2694 C  CB  . TYR A 1 334 ? -0.908  40.806  20.912  1.00 18.87 ? 334 TYR A CB  1 
ATOM   2695 C  CG  . TYR A 1 334 ? 0.305   40.467  20.088  1.00 19.37 ? 334 TYR A CG  1 
ATOM   2696 C  CD1 . TYR A 1 334 ? 0.409   39.242  19.449  1.00 20.15 ? 334 TYR A CD1 1 
ATOM   2697 C  CD2 . TYR A 1 334 ? 1.342   41.379  19.917  1.00 20.50 ? 334 TYR A CD2 1 
ATOM   2698 C  CE1 . TYR A 1 334 ? 1.500   38.927  18.657  1.00 20.26 ? 334 TYR A CE1 1 
ATOM   2699 C  CE2 . TYR A 1 334 ? 2.448   41.081  19.135  1.00 19.25 ? 334 TYR A CE2 1 
ATOM   2700 C  CZ  . TYR A 1 334 ? 2.520   39.852  18.497  1.00 20.84 ? 334 TYR A CZ  1 
ATOM   2701 O  OH  . TYR A 1 334 ? 3.595   39.523  17.721  1.00 22.73 ? 334 TYR A OH  1 
ATOM   2702 N  N   . ALA A 1 335 ? -1.608  43.849  19.991  1.00 19.89 ? 335 ALA A N   1 
ATOM   2703 C  CA  . ALA A 1 335 ? -1.019  45.099  19.466  1.00 20.47 ? 335 ALA A CA  1 
ATOM   2704 C  C   . ALA A 1 335 ? 0.493   44.901  19.285  1.00 21.95 ? 335 ALA A C   1 
ATOM   2705 O  O   . ALA A 1 335 ? 1.170   44.590  20.278  1.00 21.16 ? 335 ALA A O   1 
ATOM   2706 C  CB  . ALA A 1 335 ? -1.313  46.241  20.407  1.00 19.81 ? 335 ALA A CB  1 
ATOM   2707 N  N   . LYS A 1 336 ? 0.985   45.085  18.056  1.00 22.91 ? 336 LYS A N   1 
ATOM   2708 C  CA  . LYS A 1 336 ? 2.422   45.016  17.714  1.00 24.78 ? 336 LYS A CA  1 
ATOM   2709 C  C   . LYS A 1 336 ? 3.127   46.246  18.294  1.00 25.63 ? 336 LYS A C   1 
ATOM   2710 O  O   . LYS A 1 336 ? 4.308   46.137  18.612  1.00 26.00 ? 336 LYS A O   1 
ATOM   2711 C  CB  . LYS A 1 336 ? 2.615   44.879  16.198  1.00 25.02 ? 336 LYS A CB  1 
ATOM   2712 C  CG  . LYS A 1 336 ? 2.385   43.468  15.687  1.00 28.05 ? 336 LYS A CG  1 
ATOM   2713 C  CD  . LYS A 1 336 ? 2.058   43.350  14.198  1.00 29.74 ? 336 LYS A CD  1 
ATOM   2714 C  CE  . LYS A 1 336 ? 3.080   43.989  13.285  1.00 30.71 ? 336 LYS A CE  1 
ATOM   2715 N  NZ  . LYS A 1 336 ? 4.454   43.527  13.588  1.00 33.29 ? 336 LYS A NZ  1 
ATOM   2716 N  N   . GLU A 1 337 ? 2.437   47.382  18.402  1.00 29.50 ? 337 GLU A N   1 
ATOM   2717 C  CA  . GLU A 1 337 ? 2.969   48.644  18.984  1.00 31.69 ? 337 GLU A CA  1 
ATOM   2718 C  C   . GLU A 1 337 ? 1.851   49.317  19.789  1.00 30.61 ? 337 GLU A C   1 
ATOM   2719 O  O   . GLU A 1 337 ? 0.695   48.904  19.644  1.00 31.42 ? 337 GLU A O   1 
ATOM   2720 C  CB  . GLU A 1 337 ? 3.454   49.576  17.868  1.00 36.15 ? 337 GLU A CB  1 
ATOM   2721 C  CG  . GLU A 1 337 ? 4.554   49.001  16.982  1.00 38.38 ? 337 GLU A CG  1 
ATOM   2722 C  CD  . GLU A 1 337 ? 5.890   48.767  17.666  1.00 46.19 ? 337 GLU A CD  1 
ATOM   2723 O  OE1 . GLU A 1 337 ? 6.042   49.178  18.857  1.00 48.61 ? 337 GLU A OE1 1 
ATOM   2724 O  OE2 . GLU A 1 337 ? 6.781   48.145  17.017  1.00 52.40 ? 337 GLU A OE2 1 
ATOM   2725 N  N   . ASP A 1 338 ? 2.164   50.347  20.572  1.00 28.66 ? 338 ASP A N   1 
ATOM   2726 C  CA  . ASP A 1 338 ? 1.131   51.243  21.146  1.00 27.45 ? 338 ASP A CA  1 
ATOM   2727 C  C   . ASP A 1 338 ? 0.342   51.814  19.966  1.00 24.64 ? 338 ASP A C   1 
ATOM   2728 O  O   . ASP A 1 338 ? 0.959   52.065  18.937  1.00 22.98 ? 338 ASP A O   1 
ATOM   2729 C  CB  . ASP A 1 338 ? 1.745   52.359  21.990  1.00 29.65 ? 338 ASP A CB  1 
ATOM   2730 C  CG  . ASP A 1 338 ? 2.327   51.936  23.330  1.00 30.84 ? 338 ASP A CG  1 
ATOM   2731 O  OD1 . ASP A 1 338 ? 2.655   50.752  23.477  1.00 33.22 ? 338 ASP A OD1 1 
ATOM   2732 O  OD2 . ASP A 1 338 ? 2.445   52.811  24.226  1.00 33.76 ? 338 ASP A OD2 1 
ATOM   2733 N  N   . THR A 1 339 ? -0.974  51.963  20.093  1.00 24.33 ? 339 THR A N   1 
ATOM   2734 C  CA  . THR A 1 339 ? -1.860  52.416  18.983  1.00 26.68 ? 339 THR A CA  1 
ATOM   2735 C  C   . THR A 1 339 ? -3.282  52.660  19.500  1.00 26.12 ? 339 THR A C   1 
ATOM   2736 O  O   . THR A 1 339 ? -3.584  52.335  20.665  1.00 25.11 ? 339 THR A O   1 
ATOM   2737 C  CB  . THR A 1 339 ? -1.838  51.409  17.813  1.00 26.94 ? 339 THR A CB  1 
ATOM   2738 O  OG1 . THR A 1 339 ? -2.417  51.984  16.639  1.00 27.80 ? 339 THR A OG1 1 
ATOM   2739 C  CG2 . THR A 1 339 ? -2.558  50.120  18.144  1.00 25.74 ? 339 THR A CG2 1 
ATOM   2740 N  N   . VAL A 1 340 ? -4.124  53.209  18.634  1.00 27.80 ? 340 VAL A N   1 
ATOM   2741 C  CA  . VAL A 1 340 ? -5.506  53.621  18.980  1.00 29.16 ? 340 VAL A CA  1 
ATOM   2742 C  C   . VAL A 1 340 ? -6.458  52.889  18.034  1.00 28.69 ? 340 VAL A C   1 
ATOM   2743 O  O   . VAL A 1 340 ? -6.301  53.035  16.809  1.00 26.90 ? 340 VAL A O   1 
ATOM   2744 C  CB  . VAL A 1 340 ? -5.653  55.157  18.937  1.00 30.64 ? 340 VAL A CB  1 
ATOM   2745 C  CG1 . VAL A 1 340 ? -7.081  55.603  19.204  1.00 31.61 ? 340 VAL A CG1 1 
ATOM   2746 C  CG2 . VAL A 1 340 ? -4.716  55.832  19.934  1.00 32.54 ? 340 VAL A CG2 1 
ATOM   2747 N  N   . LEU A 1 341 ? -7.408  52.140  18.605  1.00 28.79 ? 341 LEU A N   1 
ATOM   2748 C  CA  . LEU A 1 341 ? -8.455  51.389  17.859  1.00 29.64 ? 341 LEU A CA  1 
ATOM   2749 C  C   . LEU A 1 341 ? -9.691  52.273  17.652  1.00 28.77 ? 341 LEU A C   1 
ATOM   2750 O  O   . LEU A 1 341 ? -10.173 52.862  18.626  1.00 29.64 ? 341 LEU A O   1 
ATOM   2751 C  CB  . LEU A 1 341 ? -8.805  50.127  18.647  1.00 29.36 ? 341 LEU A CB  1 
ATOM   2752 C  CG  . LEU A 1 341 ? -9.486  49.032  17.835  1.00 29.35 ? 341 LEU A CG  1 
ATOM   2753 C  CD1 . LEU A 1 341 ? -8.567  48.492  16.739  1.00 28.01 ? 341 LEU A CD1 1 
ATOM   2754 C  CD2 . LEU A 1 341 ? -9.957  47.922  18.762  1.00 29.70 ? 341 LEU A CD2 1 
ATOM   2755 N  N   . GLY A 1 342 ? -10.136 52.400  16.403  1.00 30.39 ? 342 GLY A N   1 
ATOM   2756 C  CA  . GLY A 1 342 ? -11.313 53.192  15.988  1.00 28.43 ? 342 GLY A CA  1 
ATOM   2757 C  C   . GLY A 1 342 ? -11.231 54.638  16.443  1.00 28.37 ? 342 GLY A C   1 
ATOM   2758 O  O   . GLY A 1 342 ? -12.276 55.194  16.754  1.00 27.86 ? 342 GLY A O   1 
ATOM   2759 N  N   . GLY A 1 343 ? -10.040 55.235  16.496  1.00 27.83 ? 343 GLY A N   1 
ATOM   2760 C  CA  . GLY A 1 343 ? -9.849  56.582  17.054  1.00 26.76 ? 343 GLY A CA  1 
ATOM   2761 C  C   . GLY A 1 343 ? -10.458 56.731  18.448  1.00 29.48 ? 343 GLY A C   1 
ATOM   2762 O  O   . GLY A 1 343 ? -10.733 57.881  18.857  1.00 33.36 ? 343 GLY A O   1 
ATOM   2763 N  N   . GLU A 1 344 ? -10.666 55.657  19.209  1.00 29.27 ? 344 GLU A N   1 
ATOM   2764 C  CA  . GLU A 1 344 ? -11.366 55.805  20.520  1.00 31.33 ? 344 GLU A CA  1 
ATOM   2765 C  C   . GLU A 1 344 ? -10.680 55.044  21.648  1.00 29.76 ? 344 GLU A C   1 
ATOM   2766 O  O   . GLU A 1 344 ? -10.850 55.459  22.810  1.00 30.60 ? 344 GLU A O   1 
ATOM   2767 C  CB  . GLU A 1 344 ? -12.797 55.296  20.424  1.00 32.17 ? 344 GLU A CB  1 
ATOM   2768 C  CG  . GLU A 1 344 ? -13.679 56.248  19.658  1.00 36.42 ? 344 GLU A CG  1 
ATOM   2769 C  CD  . GLU A 1 344 ? -15.082 55.735  19.399  1.00 36.31 ? 344 GLU A CD  1 
ATOM   2770 O  OE1 . GLU A 1 344 ? -15.271 54.507  19.339  1.00 36.73 ? 344 GLU A OE1 1 
ATOM   2771 O  OE2 . GLU A 1 344 ? -15.971 56.575  19.267  1.00 38.16 ? 344 GLU A OE2 1 
ATOM   2772 N  N   . TYR A 1 345 ? -10.010 53.936  21.339  1.00 29.67 ? 345 TYR A N   1 
ATOM   2773 C  CA  . TYR A 1 345 ? -9.544  52.960  22.357  1.00 29.90 ? 345 TYR A CA  1 
ATOM   2774 C  C   . TYR A 1 345 ? -8.024  52.851  22.317  1.00 29.76 ? 345 TYR A C   1 
ATOM   2775 O  O   . TYR A 1 345 ? -7.460  52.169  21.464  1.00 29.76 ? 345 TYR A O   1 
ATOM   2776 C  CB  . TYR A 1 345 ? -10.276 51.642  22.147  1.00 29.43 ? 345 TYR A CB  1 
ATOM   2777 C  CG  . TYR A 1 345 ? -11.763 51.775  22.291  1.00 27.67 ? 345 TYR A CG  1 
ATOM   2778 C  CD1 . TYR A 1 345 ? -12.335 51.979  23.538  1.00 28.50 ? 345 TYR A CD1 1 
ATOM   2779 C  CD2 . TYR A 1 345 ? -12.592 51.712  21.184  1.00 27.24 ? 345 TYR A CD2 1 
ATOM   2780 C  CE1 . TYR A 1 345 ? -13.705 52.093  23.693  1.00 28.47 ? 345 TYR A CE1 1 
ATOM   2781 C  CE2 . TYR A 1 345 ? -13.966 51.827  21.322  1.00 30.38 ? 345 TYR A CE2 1 
ATOM   2782 C  CZ  . TYR A 1 345 ? -14.519 52.021  22.581  1.00 30.43 ? 345 TYR A CZ  1 
ATOM   2783 O  OH  . TYR A 1 345 ? -15.864 52.139  22.724  1.00 35.46 ? 345 TYR A OH  1 
ATOM   2784 N  N   . PRO A 1 346 ? -7.332  53.546  23.241  1.00 30.96 ? 346 PRO A N   1 
ATOM   2785 C  CA  . PRO A 1 346 ? -5.878  53.468  23.361  1.00 31.27 ? 346 PRO A CA  1 
ATOM   2786 C  C   . PRO A 1 346 ? -5.445  52.051  23.729  1.00 29.31 ? 346 PRO A C   1 
ATOM   2787 O  O   . PRO A 1 346 ? -6.029  51.462  24.634  1.00 27.64 ? 346 PRO A O   1 
ATOM   2788 C  CB  . PRO A 1 346 ? -5.516  54.388  24.537  1.00 33.30 ? 346 PRO A CB  1 
ATOM   2789 C  CG  . PRO A 1 346 ? -6.736  55.268  24.710  1.00 34.61 ? 346 PRO A CG  1 
ATOM   2790 C  CD  . PRO A 1 346 ? -7.918  54.446  24.241  1.00 32.51 ? 346 PRO A CD  1 
ATOM   2791 N  N   . LEU A 1 347 ? -4.444  51.553  23.017  1.00 28.06 ? 347 LEU A N   1 
ATOM   2792 C  CA  . LEU A 1 347 ? -3.873  50.211  23.249  1.00 28.24 ? 347 LEU A CA  1 
ATOM   2793 C  C   . LEU A 1 347 ? -2.371  50.361  23.437  1.00 30.40 ? 347 LEU A C   1 
ATOM   2794 O  O   . LEU A 1 347 ? -1.759  51.243  22.792  1.00 33.72 ? 347 LEU A O   1 
ATOM   2795 C  CB  . LEU A 1 347 ? -4.183  49.304  22.054  1.00 29.18 ? 347 LEU A CB  1 
ATOM   2796 C  CG  . LEU A 1 347 ? -5.657  48.956  21.830  1.00 27.98 ? 347 LEU A CG  1 
ATOM   2797 C  CD1 . LEU A 1 347 ? -5.778  47.860  20.773  1.00 27.76 ? 347 LEU A CD1 1 
ATOM   2798 C  CD2 . LEU A 1 347 ? -6.311  48.513  23.133  1.00 27.03 ? 347 LEU A CD2 1 
ATOM   2799 N  N   . GLU A 1 348 ? -1.830  49.519  24.310  1.00 31.45 ? 348 GLU A N   1 
ATOM   2800 C  CA  . GLU A 1 348 ? -0.383  49.328  24.538  1.00 29.10 ? 348 GLU A CA  1 
ATOM   2801 C  C   . GLU A 1 348 ? 0.112   48.111  23.755  1.00 27.66 ? 348 GLU A C   1 
ATOM   2802 O  O   . GLU A 1 348 ? -0.627  47.112  23.638  1.00 24.14 ? 348 GLU A O   1 
ATOM   2803 C  CB  . GLU A 1 348 ? -0.130  49.100  26.020  1.00 28.38 ? 348 GLU A CB  1 
ATOM   2804 C  CG  . GLU A 1 348 ? -0.303  50.348  26.840  1.00 30.55 ? 348 GLU A CG  1 
ATOM   2805 C  CD  . GLU A 1 348 ? 0.142   50.095  28.263  1.00 32.73 ? 348 GLU A CD  1 
ATOM   2806 O  OE1 . GLU A 1 348 ? -0.597  49.345  28.974  1.00 33.01 ? 348 GLU A OE1 1 
ATOM   2807 O  OE2 . GLU A 1 348 ? 1.254   50.593  28.634  1.00 32.56 ? 348 GLU A OE2 1 
ATOM   2808 N  N   . LYS A 1 349 ? 1.340   48.207  23.254  1.00 26.92 ? 349 LYS A N   1 
ATOM   2809 C  CA  . LYS A 1 349 ? 2.110   47.053  22.754  1.00 26.34 ? 349 LYS A CA  1 
ATOM   2810 C  C   . LYS A 1 349 ? 1.786   45.854  23.651  1.00 24.31 ? 349 LYS A C   1 
ATOM   2811 O  O   . LYS A 1 349 ? 1.908   45.998  24.882  1.00 22.34 ? 349 LYS A O   1 
ATOM   2812 C  CB  . LYS A 1 349 ? 3.598   47.412  22.772  1.00 28.03 ? 349 LYS A CB  1 
ATOM   2813 C  CG  . LYS A 1 349 ? 4.507   46.349  22.188  1.00 30.70 ? 349 LYS A CG  1 
ATOM   2814 C  CD  . LYS A 1 349 ? 5.943   46.793  22.048  1.00 33.38 ? 349 LYS A CD  1 
ATOM   2815 C  CE  . LYS A 1 349 ? 6.775   45.724  21.380  1.00 33.78 ? 349 LYS A CE  1 
ATOM   2816 N  NZ  . LYS A 1 349 ? 8.007   46.300  20.802  1.00 40.38 ? 349 LYS A NZ  1 
ATOM   2817 N  N   . GLY A 1 350 ? 1.371   44.735  23.052  1.00 23.46 ? 350 GLY A N   1 
ATOM   2818 C  CA  . GLY A 1 350 ? 1.205   43.434  23.732  1.00 22.99 ? 350 GLY A CA  1 
ATOM   2819 C  C   . GLY A 1 350 ? -0.216  43.206  24.227  1.00 23.00 ? 350 GLY A C   1 
ATOM   2820 O  O   . GLY A 1 350 ? -0.481  42.058  24.650  1.00 23.05 ? 350 GLY A O   1 
ATOM   2821 N  N   . ASP A 1 351 ? -1.091  44.235  24.184  1.00 22.62 ? 351 ASP A N   1 
ATOM   2822 C  CA  . ASP A 1 351 ? -2.511  44.174  24.646  1.00 20.95 ? 351 ASP A CA  1 
ATOM   2823 C  C   . ASP A 1 351 ? -3.242  43.138  23.796  1.00 22.36 ? 351 ASP A C   1 
ATOM   2824 O  O   . ASP A 1 351 ? -3.134  43.205  22.533  1.00 21.81 ? 351 ASP A O   1 
ATOM   2825 C  CB  . ASP A 1 351 ? -3.226  45.526  24.581  1.00 21.19 ? 351 ASP A CB  1 
ATOM   2826 C  CG  . ASP A 1 351 ? -2.978  46.441  25.785  1.00 21.42 ? 351 ASP A CG  1 
ATOM   2827 O  OD1 . ASP A 1 351 ? -2.285  46.022  26.719  1.00 20.22 ? 351 ASP A OD1 1 
ATOM   2828 O  OD2 . ASP A 1 351 ? -3.474  47.574  25.770  1.00 19.63 ? 351 ASP A OD2 1 
ATOM   2829 N  N   . GLU A 1 352 ? -3.948  42.229  24.470  1.00 22.21 ? 352 GLU A N   1 
ATOM   2830 C  CA  . GLU A 1 352 ? -4.619  41.066  23.854  1.00 24.25 ? 352 GLU A CA  1 
ATOM   2831 C  C   . GLU A 1 352 ? -6.053  41.438  23.436  1.00 25.93 ? 352 GLU A C   1 
ATOM   2832 O  O   . GLU A 1 352 ? -6.769  42.094  24.233  1.00 27.00 ? 352 GLU A O   1 
ATOM   2833 C  CB  . GLU A 1 352 ? -4.625  39.906  24.839  1.00 25.89 ? 352 GLU A CB  1 
ATOM   2834 C  CG  . GLU A 1 352 ? -3.254  39.519  25.350  1.00 28.45 ? 352 GLU A CG  1 
ATOM   2835 C  CD  . GLU A 1 352 ? -3.304  38.265  26.198  1.00 30.24 ? 352 GLU A CD  1 
ATOM   2836 O  OE1 . GLU A 1 352 ? -3.135  38.384  27.433  1.00 33.70 ? 352 GLU A OE1 1 
ATOM   2837 O  OE2 . GLU A 1 352 ? -3.561  37.179  25.625  1.00 29.36 ? 352 GLU A OE2 1 
ATOM   2838 N  N   . LEU A 1 353 ? -6.465  41.018  22.235  1.00 24.88 ? 353 LEU A N   1 
ATOM   2839 C  CA  . LEU A 1 353 ? -7.843  41.201  21.717  1.00 24.72 ? 353 LEU A CA  1 
ATOM   2840 C  C   . LEU A 1 353 ? -8.429  39.826  21.382  1.00 24.60 ? 353 LEU A C   1 
ATOM   2841 O  O   . LEU A 1 353 ? -7.651  38.863  21.171  1.00 24.48 ? 353 LEU A O   1 
ATOM   2842 C  CB  . LEU A 1 353 ? -7.839  42.083  20.463  1.00 24.80 ? 353 LEU A CB  1 
ATOM   2843 C  CG  . LEU A 1 353 ? -7.136  43.434  20.559  1.00 24.73 ? 353 LEU A CG  1 
ATOM   2844 C  CD1 . LEU A 1 353 ? -7.266  44.149  19.235  1.00 25.90 ? 353 LEU A CD1 1 
ATOM   2845 C  CD2 . LEU A 1 353 ? -7.690  44.302  21.678  1.00 25.91 ? 353 LEU A CD2 1 
ATOM   2846 N  N   . MET A 1 354 ? -9.757  39.747  21.358  1.00 22.63 ? 354 MET A N   1 
ATOM   2847 C  CA  . MET A 1 354 ? -10.518 38.538  20.983  1.00 22.30 ? 354 MET A CA  1 
ATOM   2848 C  C   . MET A 1 354 ? -11.692 38.964  20.098  1.00 22.51 ? 354 MET A C   1 
ATOM   2849 O  O   . MET A 1 354 ? -12.529 39.789  20.527  1.00 21.53 ? 354 MET A O   1 
ATOM   2850 C  CB  . MET A 1 354 ? -11.022 37.781  22.210  1.00 22.45 ? 354 MET A CB  1 
ATOM   2851 C  CG  . MET A 1 354 ? -11.527 36.379  21.869  1.00 23.49 ? 354 MET A CG  1 
ATOM   2852 S  SD  . MET A 1 354 ? -10.225 35.234  21.300  1.00 25.13 ? 354 MET A SD  1 
ATOM   2853 C  CE  . MET A 1 354 ? -9.668  34.650  22.900  1.00 24.21 ? 354 MET A CE  1 
ATOM   2854 N  N   . VAL A 1 355 ? -11.699 38.452  18.876  1.00 21.41 ? 355 VAL A N   1 
ATOM   2855 C  CA  . VAL A 1 355 ? -12.788 38.662  17.889  1.00 21.13 ? 355 VAL A CA  1 
ATOM   2856 C  C   . VAL A 1 355 ? -13.856 37.608  18.158  1.00 21.18 ? 355 VAL A C   1 
ATOM   2857 O  O   . VAL A 1 355 ? -13.545 36.448  17.918  1.00 21.98 ? 355 VAL A O   1 
ATOM   2858 C  CB  . VAL A 1 355 ? -12.235 38.511  16.460  1.00 20.85 ? 355 VAL A CB  1 
ATOM   2859 C  CG1 . VAL A 1 355 ? -13.318 38.759  15.417  1.00 21.71 ? 355 VAL A CG1 1 
ATOM   2860 C  CG2 . VAL A 1 355 ? -11.018 39.390  16.237  1.00 21.28 ? 355 VAL A CG2 1 
ATOM   2861 N  N   . LEU A 1 356 ? -15.057 37.987  18.614  1.00 23.91 ? 356 LEU A N   1 
ATOM   2862 C  CA  . LEU A 1 356 ? -16.235 37.080  18.652  1.00 23.50 ? 356 LEU A CA  1 
ATOM   2863 C  C   . LEU A 1 356 ? -16.830 37.038  17.251  1.00 22.04 ? 356 LEU A C   1 
ATOM   2864 O  O   . LEU A 1 356 ? -17.634 37.950  16.927  1.00 17.83 ? 356 LEU A O   1 
ATOM   2865 C  CB  . LEU A 1 356 ? -17.281 37.564  19.652  1.00 27.45 ? 356 LEU A CB  1 
ATOM   2866 C  CG  . LEU A 1 356 ? -16.793 37.674  21.088  1.00 31.93 ? 356 LEU A CG  1 
ATOM   2867 C  CD1 . LEU A 1 356 ? -17.823 38.389  21.948  1.00 34.15 ? 356 LEU A CD1 1 
ATOM   2868 C  CD2 . LEU A 1 356 ? -16.491 36.289  21.642  1.00 34.51 ? 356 LEU A CD2 1 
ATOM   2869 N  N   . ILE A 1 357 ? -16.447 36.014  16.474  1.00 21.91 ? 357 ILE A N   1 
ATOM   2870 C  CA  . ILE A 1 357 ? -16.862 35.850  15.044  1.00 23.26 ? 357 ILE A CA  1 
ATOM   2871 C  C   . ILE A 1 357 ? -18.385 35.802  14.945  1.00 22.04 ? 357 ILE A C   1 
ATOM   2872 O  O   . ILE A 1 357 ? -18.931 36.409  14.024  1.00 21.59 ? 357 ILE A O   1 
ATOM   2873 C  CB  . ILE A 1 357 ? -16.234 34.625  14.356  1.00 25.01 ? 357 ILE A CB  1 
ATOM   2874 C  CG1 . ILE A 1 357 ? -14.726 34.514  14.587  1.00 25.01 ? 357 ILE A CG1 1 
ATOM   2875 C  CG2 . ILE A 1 357 ? -16.550 34.669  12.870  1.00 26.97 ? 357 ILE A CG2 1 
ATOM   2876 C  CD1 . ILE A 1 357 ? -14.120 33.252  14.040  1.00 25.62 ? 357 ILE A CD1 1 
ATOM   2877 N  N   . PRO A 1 358 ? -19.108 35.118  15.875  1.00 21.62 ? 358 PRO A N   1 
ATOM   2878 C  CA  . PRO A 1 358 ? -20.571 35.111  15.876  1.00 21.27 ? 358 PRO A CA  1 
ATOM   2879 C  C   . PRO A 1 358 ? -21.193 36.512  15.966  1.00 21.67 ? 358 PRO A C   1 
ATOM   2880 O  O   . PRO A 1 358 ? -22.257 36.698  15.372  1.00 20.76 ? 358 PRO A O   1 
ATOM   2881 C  CB  . PRO A 1 358 ? -20.953 34.300  17.121  1.00 21.70 ? 358 PRO A CB  1 
ATOM   2882 C  CG  . PRO A 1 358 ? -19.772 33.395  17.320  1.00 21.46 ? 358 PRO A CG  1 
ATOM   2883 C  CD  . PRO A 1 358 ? -18.585 34.274  16.961  1.00 22.39 ? 358 PRO A CD  1 
ATOM   2884 N  N   . GLN A 1 359 ? -20.531 37.461  16.644  1.00 20.61 ? 359 GLN A N   1 
ATOM   2885 C  CA  . GLN A 1 359 ? -21.049 38.850  16.761  1.00 20.42 ? 359 GLN A CA  1 
ATOM   2886 C  C   . GLN A 1 359 ? -20.678 39.641  15.501  1.00 20.49 ? 359 GLN A C   1 
ATOM   2887 O  O   . GLN A 1 359 ? -21.540 40.372  14.989  1.00 19.32 ? 359 GLN A O   1 
ATOM   2888 C  CB  . GLN A 1 359 ? -20.529 39.534  18.021  1.00 20.85 ? 359 GLN A CB  1 
ATOM   2889 C  CG  . GLN A 1 359 ? -20.987 38.897  19.326  1.00 21.67 ? 359 GLN A CG  1 
ATOM   2890 C  CD  . GLN A 1 359 ? -22.490 38.818  19.487  1.00 22.48 ? 359 GLN A CD  1 
ATOM   2891 O  OE1 . GLN A 1 359 ? -23.059 37.736  19.659  1.00 21.98 ? 359 GLN A OE1 1 
ATOM   2892 N  NE2 . GLN A 1 359 ? -23.152 39.967  19.456  1.00 22.68 ? 359 GLN A NE2 1 
ATOM   2893 N  N   . LEU A 1 360 ? -19.432 39.553  15.034  1.00 20.47 ? 360 LEU A N   1 
ATOM   2894 C  CA  . LEU A 1 360 ? -19.059 40.201  13.758  1.00 20.42 ? 360 LEU A CA  1 
ATOM   2895 C  C   . LEU A 1 360 ? -20.116 39.817  12.701  1.00 19.39 ? 360 LEU A C   1 
ATOM   2896 O  O   . LEU A 1 360 ? -20.599 40.717  11.972  1.00 18.65 ? 360 LEU A O   1 
ATOM   2897 C  CB  . LEU A 1 360 ? -17.669 39.736  13.326  1.00 22.04 ? 360 LEU A CB  1 
ATOM   2898 C  CG  . LEU A 1 360 ? -17.336 40.105  11.881  1.00 22.49 ? 360 LEU A CG  1 
ATOM   2899 C  CD1 . LEU A 1 360 ? -17.267 41.619  11.739  1.00 23.55 ? 360 LEU A CD1 1 
ATOM   2900 C  CD2 . LEU A 1 360 ? -16.036 39.467  11.429  1.00 23.22 ? 360 LEU A CD2 1 
ATOM   2901 N  N   . HIS A 1 361 ? -20.502 38.538  12.641  1.00 18.19 ? 361 HIS A N   1 
ATOM   2902 C  CA  . HIS A 1 361 ? -21.424 38.016  11.595  1.00 18.98 ? 361 HIS A CA  1 
ATOM   2903 C  C   . HIS A 1 361 ? -22.874 38.406  11.862  1.00 19.03 ? 361 HIS A C   1 
ATOM   2904 O  O   . HIS A 1 361 ? -23.695 38.080  11.011  1.00 19.20 ? 361 HIS A O   1 
ATOM   2905 C  CB  . HIS A 1 361 ? -21.335 36.511  11.453  1.00 18.12 ? 361 HIS A CB  1 
ATOM   2906 C  CG  . HIS A 1 361 ? -20.034 36.087  10.901  1.00 17.65 ? 361 HIS A CG  1 
ATOM   2907 N  ND1 . HIS A 1 361 ? -19.646 34.769  10.881  1.00 17.81 ? 361 HIS A ND1 1 
ATOM   2908 C  CD2 . HIS A 1 361 ? -19.009 36.815  10.421  1.00 18.23 ? 361 HIS A CD2 1 
ATOM   2909 C  CE1 . HIS A 1 361 ? -18.440 34.689  10.366  1.00 18.50 ? 361 HIS A CE1 1 
ATOM   2910 N  NE2 . HIS A 1 361 ? -18.013 35.943  10.097  1.00 18.81 ? 361 HIS A NE2 1 
ATOM   2911 N  N   . ARG A 1 362 ? -23.152 39.111  12.953  1.00 20.24 ? 362 ARG A N   1 
ATOM   2912 C  CA  . ARG A 1 362 ? -24.512 39.624  13.265  1.00 22.14 ? 362 ARG A CA  1 
ATOM   2913 C  C   . ARG A 1 362 ? -24.537 41.151  13.100  1.00 23.96 ? 362 ARG A C   1 
ATOM   2914 O  O   . ARG A 1 362 ? -25.532 41.763  13.517  1.00 25.77 ? 362 ARG A O   1 
ATOM   2915 C  CB  . ARG A 1 362 ? -24.929 39.129  14.657  1.00 20.67 ? 362 ARG A CB  1 
ATOM   2916 C  CG  . ARG A 1 362 ? -25.453 37.699  14.646  1.00 21.69 ? 362 ARG A CG  1 
ATOM   2917 C  CD  . ARG A 1 362 ? -25.505 37.045  16.024  1.00 23.84 ? 362 ARG A CD  1 
ATOM   2918 N  NE  . ARG A 1 362 ? -26.164 35.738  16.047  1.00 23.88 ? 362 ARG A NE  1 
ATOM   2919 C  CZ  . ARG A 1 362 ? -25.601 34.583  15.687  1.00 24.51 ? 362 ARG A CZ  1 
ATOM   2920 N  NH1 . ARG A 1 362 ? -24.359 34.550  15.237  1.00 26.96 ? 362 ARG A NH1 1 
ATOM   2921 N  NH2 . ARG A 1 362 ? -26.284 33.456  15.742  1.00 23.22 ? 362 ARG A NH2 1 
ATOM   2922 N  N   . ASP A 1 363 ? -23.491 41.761  12.537  1.00 25.36 ? 363 ASP A N   1 
ATOM   2923 C  CA  . ASP A 1 363 ? -23.395 43.244  12.469  1.00 26.94 ? 363 ASP A CA  1 
ATOM   2924 C  C   . ASP A 1 363 ? -24.448 43.765  11.490  1.00 26.34 ? 363 ASP A C   1 
ATOM   2925 O  O   . ASP A 1 363 ? -24.216 43.695  10.267  1.00 22.97 ? 363 ASP A O   1 
ATOM   2926 C  CB  . ASP A 1 363 ? -22.002 43.765  12.085  1.00 28.90 ? 363 ASP A CB  1 
ATOM   2927 C  CG  . ASP A 1 363 ? -21.855 45.291  12.116  1.00 29.33 ? 363 ASP A CG  1 
ATOM   2928 O  OD1 . ASP A 1 363 ? -22.836 46.019  11.776  1.00 28.14 ? 363 ASP A OD1 1 
ATOM   2929 O  OD2 . ASP A 1 363 ? -20.752 45.752  12.474  1.00 30.40 ? 363 ASP A OD2 1 
ATOM   2930 N  N   . LYS A 1 364 ? -25.503 44.356  12.054  1.00 27.05 ? 364 LYS A N   1 
ATOM   2931 C  CA  . LYS A 1 364 ? -26.678 44.885  11.320  1.00 28.51 ? 364 LYS A CA  1 
ATOM   2932 C  C   . LYS A 1 364 ? -26.228 45.935  10.287  1.00 26.71 ? 364 LYS A C   1 
ATOM   2933 O  O   . LYS A 1 364 ? -26.825 45.946  9.210   1.00 24.62 ? 364 LYS A O   1 
ATOM   2934 C  CB  . LYS A 1 364 ? -27.729 45.379  12.320  1.00 29.76 ? 364 LYS A CB  1 
ATOM   2935 C  CG  . LYS A 1 364 ? -28.726 44.302  12.720  1.00 33.04 ? 364 LYS A CG  1 
ATOM   2936 C  CD  . LYS A 1 364 ? -29.652 44.653  13.882  1.00 38.41 ? 364 LYS A CD  1 
ATOM   2937 C  CE  . LYS A 1 364 ? -28.987 44.589  15.254  1.00 43.85 ? 364 LYS A CE  1 
ATOM   2938 N  NZ  . LYS A 1 364 ? -28.154 43.373  15.449  1.00 46.24 ? 364 LYS A NZ  1 
ATOM   2939 N  N   . THR A 1 365 ? -25.193 46.737  10.550  1.00 24.29 ? 365 THR A N   1 
ATOM   2940 C  CA  . THR A 1 365 ? -24.681 47.735  9.560   1.00 25.90 ? 365 THR A CA  1 
ATOM   2941 C  C   . THR A 1 365 ? -24.113 47.018  8.307   1.00 25.86 ? 365 THR A C   1 
ATOM   2942 O  O   . THR A 1 365 ? -24.198 47.565  7.200   1.00 24.53 ? 365 THR A O   1 
ATOM   2943 C  CB  . THR A 1 365 ? -23.697 48.712  10.217  1.00 25.54 ? 365 THR A CB  1 
ATOM   2944 O  OG1 . THR A 1 365 ? -22.440 48.067  10.464  1.00 27.68 ? 365 THR A OG1 1 
ATOM   2945 C  CG2 . THR A 1 365 ? -24.255 49.288  11.502  1.00 26.09 ? 365 THR A CG2 1 
ATOM   2946 N  N   . ILE A 1 366 ? -23.598 45.803  8.461   1.00 26.59 ? 366 ILE A N   1 
ATOM   2947 C  CA  . ILE A 1 366 ? -23.040 44.996  7.344   1.00 25.92 ? 366 ILE A CA  1 
ATOM   2948 C  C   . ILE A 1 366 ? -24.137 44.143  6.723   1.00 24.31 ? 366 ILE A C   1 
ATOM   2949 O  O   . ILE A 1 366 ? -24.180 44.057  5.505   1.00 23.46 ? 366 ILE A O   1 
ATOM   2950 C  CB  . ILE A 1 366 ? -21.889 44.096  7.840   1.00 27.78 ? 366 ILE A CB  1 
ATOM   2951 C  CG1 . ILE A 1 366 ? -20.700 44.939  8.302   1.00 27.96 ? 366 ILE A CG1 1 
ATOM   2952 C  CG2 . ILE A 1 366 ? -21.509 43.072  6.769   1.00 27.62 ? 366 ILE A CG2 1 
ATOM   2953 C  CD1 . ILE A 1 366 ? -20.167 45.875  7.231   1.00 28.78 ? 366 ILE A CD1 1 
ATOM   2954 N  N   . TRP A 1 367 ? -24.940 43.447  7.513   1.00 24.10 ? 367 TRP A N   1 
ATOM   2955 C  CA  . TRP A 1 367 ? -25.809 42.382  6.935   1.00 25.09 ? 367 TRP A CA  1 
ATOM   2956 C  C   . TRP A 1 367 ? -27.265 42.832  6.817   1.00 25.25 ? 367 TRP A C   1 
ATOM   2957 O  O   . TRP A 1 367 ? -28.046 42.048  6.233   1.00 26.13 ? 367 TRP A O   1 
ATOM   2958 C  CB  . TRP A 1 367 ? -25.688 41.082  7.746   1.00 23.55 ? 367 TRP A CB  1 
ATOM   2959 C  CG  . TRP A 1 367 ? -24.285 40.559  7.816   1.00 21.28 ? 367 TRP A CG  1 
ATOM   2960 C  CD1 . TRP A 1 367 ? -23.384 40.770  8.816   1.00 21.19 ? 367 TRP A CD1 1 
ATOM   2961 C  CD2 . TRP A 1 367 ? -23.632 39.728  6.846   1.00 20.64 ? 367 TRP A CD2 1 
ATOM   2962 N  NE1 . TRP A 1 367 ? -22.209 40.137  8.535   1.00 21.21 ? 367 TRP A NE1 1 
ATOM   2963 C  CE2 . TRP A 1 367 ? -22.326 39.491  7.329   1.00 21.51 ? 367 TRP A CE2 1 
ATOM   2964 C  CE3 . TRP A 1 367 ? -24.020 39.165  5.618   1.00 22.18 ? 367 TRP A CE3 1 
ATOM   2965 C  CZ2 . TRP A 1 367 ? -21.404 38.699  6.632   1.00 20.68 ? 367 TRP A CZ2 1 
ATOM   2966 C  CZ3 . TRP A 1 367 ? -23.109 38.388  4.924   1.00 22.28 ? 367 TRP A CZ3 1 
ATOM   2967 C  CH2 . TRP A 1 367 ? -21.816 38.161  5.428   1.00 22.15 ? 367 TRP A CH2 1 
ATOM   2968 N  N   . GLY A 1 368 ? -27.624 44.006  7.352   1.00 25.74 ? 368 GLY A N   1 
ATOM   2969 C  CA  . GLY A 1 368 ? -29.005 44.534  7.324   1.00 27.09 ? 368 GLY A CA  1 
ATOM   2970 C  C   . GLY A 1 368 ? -29.872 43.931  8.415   1.00 28.26 ? 368 GLY A C   1 
ATOM   2971 O  O   . GLY A 1 368 ? -29.305 43.254  9.291   1.00 26.89 ? 368 GLY A O   1 
ATOM   2972 N  N   . ASP A 1 369 ? -31.192 44.167  8.364   1.00 30.73 ? 369 ASP A N   1 
ATOM   2973 C  CA  . ASP A 1 369 ? -32.123 43.973  9.512   1.00 35.62 ? 369 ASP A CA  1 
ATOM   2974 C  C   . ASP A 1 369 ? -32.470 42.488  9.679   1.00 38.06 ? 369 ASP A C   1 
ATOM   2975 O  O   . ASP A 1 369 ? -32.797 42.098  10.816  1.00 41.76 ? 369 ASP A O   1 
ATOM   2976 C  CB  . ASP A 1 369 ? -33.407 44.804  9.370   1.00 38.72 ? 369 ASP A CB  1 
ATOM   2977 C  CG  . ASP A 1 369 ? -33.273 46.249  9.833   1.00 42.61 ? 369 ASP A CG  1 
ATOM   2978 O  OD1 . ASP A 1 369 ? -32.294 46.542  10.547  1.00 42.46 ? 369 ASP A OD1 1 
ATOM   2979 O  OD2 . ASP A 1 369 ? -34.157 47.077  9.478   1.00 44.07 ? 369 ASP A OD2 1 
ATOM   2980 N  N   . ASP A 1 370 ? -32.404 41.694  8.605   1.00 36.66 ? 370 ASP A N   1 
ATOM   2981 C  CA  . ASP A 1 370 ? -32.769 40.252  8.613   1.00 36.64 ? 370 ASP A CA  1 
ATOM   2982 C  C   . ASP A 1 370 ? -31.562 39.408  9.068   1.00 36.91 ? 370 ASP A C   1 
ATOM   2983 O  O   . ASP A 1 370 ? -31.366 38.313  8.531   1.00 34.25 ? 370 ASP A O   1 
ATOM   2984 C  CB  . ASP A 1 370 ? -33.325 39.822  7.245   1.00 38.02 ? 370 ASP A CB  1 
ATOM   2985 C  CG  . ASP A 1 370 ? -32.320 39.726  6.106   1.00 39.47 ? 370 ASP A CG  1 
ATOM   2986 O  OD1 . ASP A 1 370 ? -31.253 40.356  6.214   1.00 42.12 ? 370 ASP A OD1 1 
ATOM   2987 O  OD2 . ASP A 1 370 ? -32.610 39.007  5.110   1.00 42.29 ? 370 ASP A OD2 1 
ATOM   2988 N  N   . VAL A 1 371 ? -30.825 39.853  10.083  1.00 33.11 ? 371 VAL A N   1 
ATOM   2989 C  CA  . VAL A 1 371 ? -29.477 39.317  10.420  1.00 30.17 ? 371 VAL A CA  1 
ATOM   2990 C  C   . VAL A 1 371 ? -29.571 37.882  10.981  1.00 30.93 ? 371 VAL A C   1 
ATOM   2991 O  O   . VAL A 1 371 ? -28.612 37.089  10.719  1.00 26.51 ? 371 VAL A O   1 
ATOM   2992 C  CB  . VAL A 1 371 ? -28.779 40.294  11.386  1.00 31.46 ? 371 VAL A CB  1 
ATOM   2993 C  CG1 . VAL A 1 371 ? -29.038 39.980  12.852  1.00 31.97 ? 371 VAL A CG1 1 
ATOM   2994 C  CG2 . VAL A 1 371 ? -27.291 40.355  11.119  1.00 32.31 ? 371 VAL A CG2 1 
ATOM   2995 N  N   . GLU A 1 372 ? -30.635 37.561  11.747  1.00 30.73 ? 372 GLU A N   1 
ATOM   2996 C  CA  . GLU A 1 372 ? -30.842 36.243  12.416  1.00 32.98 ? 372 GLU A CA  1 
ATOM   2997 C  C   . GLU A 1 372 ? -31.552 35.278  11.456  1.00 30.04 ? 372 GLU A C   1 
ATOM   2998 O  O   . GLU A 1 372 ? -31.722 34.108  11.806  1.00 32.44 ? 372 GLU A O   1 
ATOM   2999 C  CB  . GLU A 1 372 ? -31.643 36.357  13.719  1.00 36.69 ? 372 GLU A CB  1 
ATOM   3000 C  CG  . GLU A 1 372 ? -31.009 37.243  14.794  1.00 41.97 ? 372 GLU A CG  1 
ATOM   3001 C  CD  . GLU A 1 372 ? -29.732 36.768  15.497  1.00 51.56 ? 372 GLU A CD  1 
ATOM   3002 O  OE1 . GLU A 1 372 ? -29.397 35.548  15.442  1.00 45.70 ? 372 GLU A OE1 1 
ATOM   3003 O  OE2 . GLU A 1 372 ? -29.047 37.634  16.119  1.00 58.61 ? 372 GLU A OE2 1 
ATOM   3004 N  N   . GLU A 1 373 ? -31.910 35.728  10.262  1.00 28.60 ? 373 GLU A N   1 
ATOM   3005 C  CA  . GLU A 1 373 ? -32.543 34.875  9.226   1.00 30.06 ? 373 GLU A CA  1 
ATOM   3006 C  C   . GLU A 1 373 ? -31.461 33.997  8.587   1.00 28.39 ? 373 GLU A C   1 
ATOM   3007 O  O   . GLU A 1 373 ? -30.349 34.517  8.328   1.00 28.06 ? 373 GLU A O   1 
ATOM   3008 C  CB  . GLU A 1 373 ? -33.233 35.758  8.178   1.00 35.87 ? 373 GLU A CB  1 
ATOM   3009 C  CG  . GLU A 1 373 ? -34.468 35.137  7.542   1.00 42.96 ? 373 GLU A CG  1 
ATOM   3010 C  CD  . GLU A 1 373 ? -35.314 36.074  6.690   1.00 45.89 ? 373 GLU A CD  1 
ATOM   3011 O  OE1 . GLU A 1 373 ? -35.893 37.022  7.272   1.00 52.67 ? 373 GLU A OE1 1 
ATOM   3012 O  OE2 . GLU A 1 373 ? -35.412 35.842  5.452   1.00 45.47 ? 373 GLU A OE2 1 
ATOM   3013 N  N   . PHE A 1 374 ? -31.773 32.730  8.307   1.00 24.75 ? 374 PHE A N   1 
ATOM   3014 C  CA  . PHE A 1 374 ? -30.911 31.823  7.512   1.00 22.30 ? 374 PHE A CA  1 
ATOM   3015 C  C   . PHE A 1 374 ? -31.241 32.017  6.031   1.00 20.35 ? 374 PHE A C   1 
ATOM   3016 O  O   . PHE A 1 374 ? -32.178 31.373  5.598   1.00 20.28 ? 374 PHE A O   1 
ATOM   3017 C  CB  . PHE A 1 374 ? -31.076 30.360  7.944   1.00 21.04 ? 374 PHE A CB  1 
ATOM   3018 C  CG  . PHE A 1 374 ? -30.085 29.422  7.296   1.00 21.55 ? 374 PHE A CG  1 
ATOM   3019 C  CD1 . PHE A 1 374 ? -28.817 29.257  7.835   1.00 21.35 ? 374 PHE A CD1 1 
ATOM   3020 C  CD2 . PHE A 1 374 ? -30.396 28.739  6.120   1.00 20.78 ? 374 PHE A CD2 1 
ATOM   3021 C  CE1 . PHE A 1 374 ? -27.894 28.418  7.227   1.00 21.55 ? 374 PHE A CE1 1 
ATOM   3022 C  CE2 . PHE A 1 374 ? -29.473 27.895  5.518   1.00 20.58 ? 374 PHE A CE2 1 
ATOM   3023 C  CZ  . PHE A 1 374 ? -28.230 27.730  6.078   1.00 21.45 ? 374 PHE A CZ  1 
ATOM   3024 N  N   . ARG A 1 375 ? -30.493 32.855  5.303   1.00 20.84 ? 375 ARG A N   1 
ATOM   3025 C  CA  . ARG A 1 375 ? -30.643 33.107  3.832   1.00 21.39 ? 375 ARG A CA  1 
ATOM   3026 C  C   . ARG A 1 375 ? -29.299 32.901  3.146   1.00 17.50 ? 375 ARG A C   1 
ATOM   3027 O  O   . ARG A 1 375 ? -28.425 33.770  3.142   1.00 14.83 ? 375 ARG A O   1 
ATOM   3028 C  CB  . ARG A 1 375 ? -31.087 34.535  3.485   1.00 25.59 ? 375 ARG A CB  1 
ATOM   3029 C  CG  . ARG A 1 375 ? -32.231 35.098  4.314   1.00 31.87 ? 375 ARG A CG  1 
ATOM   3030 C  CD  . ARG A 1 375 ? -33.548 35.303  3.566   1.00 38.81 ? 375 ARG A CD  1 
ATOM   3031 N  NE  . ARG A 1 375 ? -33.438 35.816  2.204   1.00 43.42 ? 375 ARG A NE  1 
ATOM   3032 C  CZ  . ARG A 1 375 ? -33.680 35.117  1.083   1.00 52.04 ? 375 ARG A CZ  1 
ATOM   3033 N  NH1 . ARG A 1 375 ? -34.030 33.838  1.150   1.00 56.57 ? 375 ARG A NH1 1 
ATOM   3034 N  NH2 . ARG A 1 375 ? -33.566 35.701  -0.107  1.00 47.30 ? 375 ARG A NH2 1 
ATOM   3035 N  N   . PRO A 1 376 ? -29.080 31.716  2.560   1.00 17.63 ? 376 PRO A N   1 
ATOM   3036 C  CA  . PRO A 1 376 ? -27.895 31.468  1.739   1.00 18.19 ? 376 PRO A CA  1 
ATOM   3037 C  C   . PRO A 1 376 ? -27.739 32.475  0.599   1.00 18.09 ? 376 PRO A C   1 
ATOM   3038 O  O   . PRO A 1 376 ? -26.627 32.723  0.209   1.00 19.01 ? 376 PRO A O   1 
ATOM   3039 C  CB  . PRO A 1 376 ? -28.132 30.034  1.235   1.00 18.06 ? 376 PRO A CB  1 
ATOM   3040 C  CG  . PRO A 1 376 ? -28.891 29.389  2.374   1.00 17.21 ? 376 PRO A CG  1 
ATOM   3041 C  CD  . PRO A 1 376 ? -29.857 30.487  2.780   1.00 18.27 ? 376 PRO A CD  1 
ATOM   3042 N  N   . GLU A 1 377 ? -28.854 33.049  0.152   1.00 19.80 ? 377 GLU A N   1 
ATOM   3043 C  CA  . GLU A 1 377 ? -28.955 33.992  -0.997  1.00 21.09 ? 377 GLU A CA  1 
ATOM   3044 C  C   . GLU A 1 377 ? -28.101 35.234  -0.698  1.00 21.35 ? 377 GLU A C   1 
ATOM   3045 O  O   . GLU A 1 377 ? -27.651 35.863  -1.646  1.00 18.96 ? 377 GLU A O   1 
ATOM   3046 C  CB  . GLU A 1 377 ? -30.433 34.314  -1.269  1.00 21.26 ? 377 GLU A CB  1 
ATOM   3047 C  CG  . GLU A 1 377 ? -31.198 33.151  -1.917  1.00 21.91 ? 377 GLU A CG  1 
ATOM   3048 C  CD  . GLU A 1 377 ? -31.580 31.983  -1.002  1.00 23.52 ? 377 GLU A CD  1 
ATOM   3049 O  OE1 . GLU A 1 377 ? -31.539 32.178  0.250   1.00 23.04 ? 377 GLU A OE1 1 
ATOM   3050 O  OE2 . GLU A 1 377 ? -31.901 30.859  -1.527  1.00 21.86 ? 377 GLU A OE2 1 
ATOM   3051 N  N   . ARG A 1 378 ? -27.864 35.551  0.580   1.00 20.43 ? 378 ARG A N   1 
ATOM   3052 C  CA  . ARG A 1 378 ? -26.890 36.593  1.002   1.00 20.94 ? 378 ARG A CA  1 
ATOM   3053 C  C   . ARG A 1 378 ? -25.534 36.436  0.325   1.00 20.29 ? 378 ARG A C   1 
ATOM   3054 O  O   . ARG A 1 378 ? -24.860 37.448  0.182   1.00 21.62 ? 378 ARG A O   1 
ATOM   3055 C  CB  . ARG A 1 378 ? -26.512 36.452  2.473   1.00 21.20 ? 378 ARG A CB  1 
ATOM   3056 C  CG  . ARG A 1 378 ? -27.541 37.046  3.402   1.00 21.42 ? 378 ARG A CG  1 
ATOM   3057 C  CD  . ARG A 1 378 ? -27.009 36.809  4.784   1.00 21.35 ? 378 ARG A CD  1 
ATOM   3058 N  NE  . ARG A 1 378 ? -28.134 36.401  5.587   1.00 20.68 ? 378 ARG A NE  1 
ATOM   3059 C  CZ  . ARG A 1 378 ? -29.018 37.217  6.099   1.00 19.22 ? 378 ARG A CZ  1 
ATOM   3060 N  NH1 . ARG A 1 378 ? -28.934 38.512  5.868   1.00 19.35 ? 378 ARG A NH1 1 
ATOM   3061 N  NH2 . ARG A 1 378 ? -29.976 36.727  6.862   1.00 20.16 ? 378 ARG A NH2 1 
ATOM   3062 N  N   . PHE A 1 379 ? -25.123 35.210  0.018   1.00 19.98 ? 379 PHE A N   1 
ATOM   3063 C  CA  . PHE A 1 379 ? -23.790 34.907  -0.561  1.00 21.56 ? 379 PHE A CA  1 
ATOM   3064 C  C   . PHE A 1 379 ? -23.892 34.660  -2.070  1.00 21.38 ? 379 PHE A C   1 
ATOM   3065 O  O   . PHE A 1 379 ? -22.851 34.324  -2.672  1.00 22.53 ? 379 PHE A O   1 
ATOM   3066 C  CB  . PHE A 1 379 ? -23.161 33.717  0.177   1.00 20.71 ? 379 PHE A CB  1 
ATOM   3067 C  CG  . PHE A 1 379 ? -22.805 34.020  1.609   1.00 20.88 ? 379 PHE A CG  1 
ATOM   3068 C  CD1 . PHE A 1 379 ? -21.628 34.690  1.911   1.00 21.05 ? 379 PHE A CD1 1 
ATOM   3069 C  CD2 . PHE A 1 379 ? -23.668 33.685  2.646   1.00 20.51 ? 379 PHE A CD2 1 
ATOM   3070 C  CE1 . PHE A 1 379 ? -21.305 34.986  3.228   1.00 21.22 ? 379 PHE A CE1 1 
ATOM   3071 C  CE2 . PHE A 1 379 ? -23.341 33.987  3.958   1.00 21.00 ? 379 PHE A CE2 1 
ATOM   3072 C  CZ  . PHE A 1 379 ? -22.167 34.647  4.246   1.00 21.35 ? 379 PHE A CZ  1 
ATOM   3073 N  N   . GLU A 1 380 ? -25.067 34.842  -2.665  1.00 22.80 ? 380 GLU A N   1 
ATOM   3074 C  CA  . GLU A 1 380 ? -25.299 34.525  -4.102  1.00 26.60 ? 380 GLU A CA  1 
ATOM   3075 C  C   . GLU A 1 380 ? -24.323 35.348  -4.954  1.00 27.09 ? 380 GLU A C   1 
ATOM   3076 O  O   . GLU A 1 380 ? -23.699 34.776  -5.851  1.00 26.26 ? 380 GLU A O   1 
ATOM   3077 C  CB  . GLU A 1 380 ? -26.764 34.707  -4.520  1.00 27.36 ? 380 GLU A CB  1 
ATOM   3078 C  CG  . GLU A 1 380 ? -27.206 33.661  -5.543  1.00 30.52 ? 380 GLU A CG  1 
ATOM   3079 C  CD  . GLU A 1 380 ? -28.668 33.713  -5.971  1.00 32.01 ? 380 GLU A CD  1 
ATOM   3080 O  OE1 . GLU A 1 380 ? -29.434 32.738  -5.676  1.00 32.45 ? 380 GLU A OE1 1 
ATOM   3081 O  OE2 . GLU A 1 380 ? -29.021 34.705  -6.654  1.00 33.91 ? 380 GLU A OE2 1 
ATOM   3082 N  N   . ASN A 1 381 ? -24.180 36.630  -4.645  1.00 26.08 ? 381 ASN A N   1 
ATOM   3083 C  CA  . ASN A 1 381 ? -23.101 37.497  -5.176  1.00 28.81 ? 381 ASN A CA  1 
ATOM   3084 C  C   . ASN A 1 381 ? -21.918 37.398  -4.202  1.00 30.60 ? 381 ASN A C   1 
ATOM   3085 O  O   . ASN A 1 381 ? -21.935 38.029  -3.151  1.00 30.77 ? 381 ASN A O   1 
ATOM   3086 C  CB  . ASN A 1 381 ? -23.632 38.920  -5.442  1.00 26.42 ? 381 ASN A CB  1 
ATOM   3087 C  CG  . ASN A 1 381 ? -22.533 39.885  -5.841  1.00 27.37 ? 381 ASN A CG  1 
ATOM   3088 O  OD1 . ASN A 1 381 ? -21.368 39.489  -5.910  1.00 29.82 ? 381 ASN A OD1 1 
ATOM   3089 N  ND2 . ASN A 1 381 ? -22.872 41.138  -6.118  1.00 24.48 ? 381 ASN A ND2 1 
ATOM   3090 N  N   . PRO A 1 382 ? -20.866 36.588  -4.484  1.00 35.17 ? 382 PRO A N   1 
ATOM   3091 C  CA  . PRO A 1 382 ? -19.745 36.433  -3.552  1.00 35.46 ? 382 PRO A CA  1 
ATOM   3092 C  C   . PRO A 1 382 ? -18.921 37.708  -3.309  1.00 36.22 ? 382 PRO A C   1 
ATOM   3093 O  O   . PRO A 1 382 ? -18.309 37.775  -2.260  1.00 37.10 ? 382 PRO A O   1 
ATOM   3094 C  CB  . PRO A 1 382 ? -18.840 35.354  -4.181  1.00 37.04 ? 382 PRO A CB  1 
ATOM   3095 C  CG  . PRO A 1 382 ? -19.272 35.256  -5.638  1.00 39.09 ? 382 PRO A CG  1 
ATOM   3096 C  CD  . PRO A 1 382 ? -20.709 35.747  -5.686  1.00 38.14 ? 382 PRO A CD  1 
ATOM   3097 N  N   . SER A 1 383 ? -18.954 38.676  -4.243  1.00 36.46 ? 383 SER A N   1 
ATOM   3098 C  CA  . SER A 1 383 ? -18.135 39.925  -4.261  1.00 34.58 ? 383 SER A CA  1 
ATOM   3099 C  C   . SER A 1 383 ? -18.882 41.115  -3.627  1.00 31.31 ? 383 SER A C   1 
ATOM   3100 O  O   . SER A 1 383 ? -18.383 42.245  -3.729  1.00 32.13 ? 383 SER A O   1 
ATOM   3101 C  CB  . SER A 1 383 ? -17.702 40.244  -5.689  1.00 36.45 ? 383 SER A CB  1 
ATOM   3102 O  OG  . SER A 1 383 ? -16.801 39.252  -6.179  1.00 37.53 ? 383 SER A OG  1 
ATOM   3103 N  N   . ALA A 1 384 ? -20.045 40.903  -3.018  1.00 28.11 ? 384 ALA A N   1 
ATOM   3104 C  CA  . ALA A 1 384 ? -20.839 41.972  -2.368  1.00 26.37 ? 384 ALA A CA  1 
ATOM   3105 C  C   . ALA A 1 384 ? -20.513 42.036  -0.871  1.00 25.75 ? 384 ALA A C   1 
ATOM   3106 O  O   . ALA A 1 384 ? -20.956 42.993  -0.217  1.00 24.71 ? 384 ALA A O   1 
ATOM   3107 C  CB  . ALA A 1 384 ? -22.310 41.726  -2.601  1.00 26.25 ? 384 ALA A CB  1 
ATOM   3108 N  N   . ILE A 1 385 ? -19.772 41.055  -0.351  1.00 27.51 ? 385 ILE A N   1 
ATOM   3109 C  CA  . ILE A 1 385 ? -19.411 40.933  1.095   1.00 29.90 ? 385 ILE A CA  1 
ATOM   3110 C  C   . ILE A 1 385 ? -18.311 41.963  1.344   1.00 30.51 ? 385 ILE A C   1 
ATOM   3111 O  O   . ILE A 1 385 ? -17.316 41.958  0.626   1.00 30.54 ? 385 ILE A O   1 
ATOM   3112 C  CB  . ILE A 1 385 ? -18.971 39.485  1.453   1.00 32.93 ? 385 ILE A CB  1 
ATOM   3113 C  CG1 . ILE A 1 385 ? -20.116 38.540  1.849   1.00 32.86 ? 385 ILE A CG1 1 
ATOM   3114 C  CG2 . ILE A 1 385 ? -17.937 39.500  2.567   1.00 35.11 ? 385 ILE A CG2 1 
ATOM   3115 C  CD1 . ILE A 1 385 ? -21.469 38.842  1.250   1.00 34.27 ? 385 ILE A CD1 1 
ATOM   3116 N  N   . PRO A 1 386 ? -18.467 42.924  2.293   1.00 30.02 ? 386 PRO A N   1 
ATOM   3117 C  CA  . PRO A 1 386 ? -17.401 43.873  2.594   1.00 29.15 ? 386 PRO A CA  1 
ATOM   3118 C  C   . PRO A 1 386 ? -16.148 43.213  3.175   1.00 29.77 ? 386 PRO A C   1 
ATOM   3119 O  O   . PRO A 1 386 ? -16.201 42.119  3.755   1.00 27.93 ? 386 PRO A O   1 
ATOM   3120 C  CB  . PRO A 1 386 ? -18.022 44.823  3.628   1.00 29.32 ? 386 PRO A CB  1 
ATOM   3121 C  CG  . PRO A 1 386 ? -19.504 44.712  3.349   1.00 29.94 ? 386 PRO A CG  1 
ATOM   3122 C  CD  . PRO A 1 386 ? -19.699 43.244  3.030   1.00 30.08 ? 386 PRO A CD  1 
ATOM   3123 N  N   . GLN A 1 387 ? -15.039 43.925  3.022   1.00 30.04 ? 387 GLN A N   1 
ATOM   3124 C  CA  . GLN A 1 387 ? -13.725 43.516  3.561   1.00 30.09 ? 387 GLN A CA  1 
ATOM   3125 C  C   . GLN A 1 387 ? -13.862 43.362  5.083   1.00 28.94 ? 387 GLN A C   1 
ATOM   3126 O  O   . GLN A 1 387 ? -14.411 44.265  5.754   1.00 27.72 ? 387 GLN A O   1 
ATOM   3127 C  CB  . GLN A 1 387 ? -12.687 44.536  3.125   1.00 32.91 ? 387 GLN A CB  1 
ATOM   3128 C  CG  . GLN A 1 387 ? -11.346 43.925  2.775   1.00 37.83 ? 387 GLN A CG  1 
ATOM   3129 C  CD  . GLN A 1 387 ? -10.393 45.039  2.418   1.00 43.50 ? 387 GLN A CD  1 
ATOM   3130 O  OE1 . GLN A 1 387 ? -10.811 46.091  1.917   1.00 45.02 ? 387 GLN A OE1 1 
ATOM   3131 N  NE2 . GLN A 1 387 ? -9.111  44.814  2.676   1.00 41.24 ? 387 GLN A NE2 1 
ATOM   3132 N  N   . HIS A 1 388 ? -13.450 42.203  5.583   1.00 29.41 ? 388 HIS A N   1 
ATOM   3133 C  CA  . HIS A 1 388 ? -13.305 41.879  7.026   1.00 29.44 ? 388 HIS A CA  1 
ATOM   3134 C  C   . HIS A 1 388 ? -14.672 41.694  7.696   1.00 27.09 ? 388 HIS A C   1 
ATOM   3135 O  O   . HIS A 1 388 ? -14.716 41.658  8.916   1.00 28.34 ? 388 HIS A O   1 
ATOM   3136 C  CB  . HIS A 1 388 ? -12.436 42.935  7.705   1.00 30.71 ? 388 HIS A CB  1 
ATOM   3137 C  CG  . HIS A 1 388 ? -11.066 43.029  7.120   1.00 31.38 ? 388 HIS A CG  1 
ATOM   3138 N  ND1 . HIS A 1 388 ? -10.231 41.933  7.030   1.00 32.45 ? 388 HIS A ND1 1 
ATOM   3139 C  CD2 . HIS A 1 388 ? -10.381 44.073  6.610   1.00 32.01 ? 388 HIS A CD2 1 
ATOM   3140 C  CE1 . HIS A 1 388 ? -9.080  42.297  6.508   1.00 32.26 ? 388 HIS A CE1 1 
ATOM   3141 N  NE2 . HIS A 1 388 ? -9.151  43.605  6.236   1.00 33.52 ? 388 HIS A NE2 1 
ATOM   3142 N  N   . ALA A 1 389 ? -15.738 41.486  6.924   1.00 27.55 ? 389 ALA A N   1 
ATOM   3143 C  CA  . ALA A 1 389 ? -17.103 41.287  7.465   1.00 24.34 ? 389 ALA A CA  1 
ATOM   3144 C  C   . ALA A 1 389 ? -17.354 39.812  7.797   1.00 21.31 ? 389 ALA A C   1 
ATOM   3145 O  O   . ALA A 1 389 ? -18.070 39.583  8.747   1.00 20.73 ? 389 ALA A O   1 
ATOM   3146 C  CB  . ALA A 1 389 ? -18.126 41.841  6.509   1.00 24.75 ? 389 ALA A CB  1 
ATOM   3147 N  N   . PHE A 1 390 ? -16.767 38.862  7.054   1.00 20.76 ? 390 PHE A N   1 
ATOM   3148 C  CA  . PHE A 1 390 ? -16.996 37.395  7.187   1.00 19.38 ? 390 PHE A CA  1 
ATOM   3149 C  C   . PHE A 1 390 ? -15.644 36.716  7.447   1.00 19.06 ? 390 PHE A C   1 
ATOM   3150 O  O   . PHE A 1 390 ? -14.821 36.666  6.530   1.00 17.96 ? 390 PHE A O   1 
ATOM   3151 C  CB  . PHE A 1 390 ? -17.728 36.901  5.929   1.00 18.61 ? 390 PHE A CB  1 
ATOM   3152 C  CG  . PHE A 1 390 ? -18.117 35.443  5.871   1.00 18.11 ? 390 PHE A CG  1 
ATOM   3153 C  CD1 . PHE A 1 390 ? -18.976 34.889  6.817   1.00 18.26 ? 390 PHE A CD1 1 
ATOM   3154 C  CD2 . PHE A 1 390 ? -17.649 34.619  4.842   1.00 17.71 ? 390 PHE A CD2 1 
ATOM   3155 C  CE1 . PHE A 1 390 ? -19.336 33.543  6.749   1.00 17.77 ? 390 PHE A CE1 1 
ATOM   3156 C  CE2 . PHE A 1 390 ? -18.010 33.279  4.777   1.00 17.06 ? 390 PHE A CE2 1 
ATOM   3157 C  CZ  . PHE A 1 390 ? -18.875 32.752  5.714   1.00 17.48 ? 390 PHE A CZ  1 
ATOM   3158 N  N   . LYS A 1 391 ? -15.390 36.240  8.670   1.00 19.65 ? 391 LYS A N   1 
ATOM   3159 C  CA  . LYS A 1 391 ? -14.048 35.733  9.067   1.00 19.74 ? 391 LYS A CA  1 
ATOM   3160 C  C   . LYS A 1 391 ? -14.147 34.349  9.691   1.00 18.87 ? 391 LYS A C   1 
ATOM   3161 O  O   . LYS A 1 391 ? -13.441 34.014  10.636  1.00 19.25 ? 391 LYS A O   1 
ATOM   3162 C  CB  . LYS A 1 391 ? -13.387 36.737  10.011  1.00 22.08 ? 391 LYS A CB  1 
ATOM   3163 C  CG  . LYS A 1 391 ? -13.368 38.170  9.502   1.00 23.88 ? 391 LYS A CG  1 
ATOM   3164 C  CD  . LYS A 1 391 ? -12.499 38.358  8.289   1.00 27.19 ? 391 LYS A CD  1 
ATOM   3165 C  CE  . LYS A 1 391 ? -11.025 38.472  8.638   1.00 29.65 ? 391 LYS A CE  1 
ATOM   3166 N  NZ  . LYS A 1 391 ? -10.190 38.775  7.454   1.00 31.09 ? 391 LYS A NZ  1 
ATOM   3167 N  N   . PRO A 1 392 ? -14.923 33.420  9.109   1.00 18.15 ? 392 PRO A N   1 
ATOM   3168 C  CA  . PRO A 1 392 ? -15.082 32.120  9.737   1.00 16.65 ? 392 PRO A CA  1 
ATOM   3169 C  C   . PRO A 1 392 ? -13.756 31.355  9.779   1.00 15.91 ? 392 PRO A C   1 
ATOM   3170 O  O   . PRO A 1 392 ? -13.689 30.443  10.518  1.00 15.37 ? 392 PRO A O   1 
ATOM   3171 C  CB  . PRO A 1 392 ? -16.077 31.446  8.798   1.00 17.34 ? 392 PRO A CB  1 
ATOM   3172 C  CG  . PRO A 1 392 ? -15.727 32.012  7.455   1.00 16.90 ? 392 PRO A CG  1 
ATOM   3173 C  CD  . PRO A 1 392 ? -15.503 33.475  7.754   1.00 17.37 ? 392 PRO A CD  1 
ATOM   3174 N  N   . PHE A 1 393 ? -12.758 31.743  8.981   1.00 15.98 ? 393 PHE A N   1 
ATOM   3175 C  CA  . PHE A 1 393 ? -11.454 31.036  8.892   1.00 17.00 ? 393 PHE A CA  1 
ATOM   3176 C  C   . PHE A 1 393 ? -10.310 31.931  9.416   1.00 18.62 ? 393 PHE A C   1 
ATOM   3177 O  O   . PHE A 1 393 ? -9.129  31.653  9.114   1.00 22.24 ? 393 PHE A O   1 
ATOM   3178 C  CB  . PHE A 1 393 ? -11.217 30.553  7.450   1.00 16.56 ? 393 PHE A CB  1 
ATOM   3179 C  CG  . PHE A 1 393 ? -12.138 29.449  6.989   1.00 16.28 ? 393 PHE A CG  1 
ATOM   3180 C  CD1 . PHE A 1 393 ? -12.009 28.154  7.470   1.00 17.06 ? 393 PHE A CD1 1 
ATOM   3181 C  CD2 . PHE A 1 393 ? -13.154 29.704  6.093   1.00 15.86 ? 393 PHE A CD2 1 
ATOM   3182 C  CE1 . PHE A 1 393 ? -12.860 27.140  7.045   1.00 17.17 ? 393 PHE A CE1 1 
ATOM   3183 C  CE2 . PHE A 1 393 ? -14.005 28.691  5.670   1.00 16.45 ? 393 PHE A CE2 1 
ATOM   3184 C  CZ  . PHE A 1 393 ? -13.864 27.413  6.150   1.00 16.35 ? 393 PHE A CZ  1 
ATOM   3185 N  N   . GLY A 1 394 ? -10.601 32.978  10.190  1.00 18.52 ? 394 GLY A N   1 
ATOM   3186 C  CA  . GLY A 1 394 ? -9.568  33.867  10.778  1.00 18.68 ? 394 GLY A CA  1 
ATOM   3187 C  C   . GLY A 1 394 ? -9.085  34.923  9.783   1.00 19.18 ? 394 GLY A C   1 
ATOM   3188 O  O   . GLY A 1 394 ? -9.838  35.224  8.836   1.00 17.76 ? 394 GLY A O   1 
ATOM   3189 N  N   . ASN A 1 395 ? -7.827  35.391  9.922   1.00 20.62 ? 395 ASN A N   1 
ATOM   3190 C  CA  . ASN A 1 395 ? -7.320  36.583  9.196   1.00 18.79 ? 395 ASN A CA  1 
ATOM   3191 C  C   . ASN A 1 395 ? -5.882  36.412  8.673   1.00 19.02 ? 395 ASN A C   1 
ATOM   3192 O  O   . ASN A 1 395 ? -5.018  35.873  9.410   1.00 16.79 ? 395 ASN A O   1 
ATOM   3193 C  CB  . ASN A 1 395 ? -7.444  37.801  10.086  1.00 19.88 ? 395 ASN A CB  1 
ATOM   3194 C  CG  . ASN A 1 395 ? -7.081  39.027  9.297   1.00 21.34 ? 395 ASN A CG  1 
ATOM   3195 O  OD1 . ASN A 1 395 ? -7.798  39.402  8.364   1.00 20.69 ? 395 ASN A OD1 1 
ATOM   3196 N  ND2 . ASN A 1 395 ? -5.935  39.599  9.632   1.00 22.11 ? 395 ASN A ND2 1 
ATOM   3197 N  N   . GLY A 1 396 ? -5.661  36.847  7.413   1.00 19.27 ? 396 GLY A N   1 
ATOM   3198 C  CA  . GLY A 1 396 ? -4.348  37.045  6.761   1.00 18.35 ? 396 GLY A CA  1 
ATOM   3199 C  C   . GLY A 1 396 ? -3.527  35.774  6.739   1.00 19.23 ? 396 GLY A C   1 
ATOM   3200 O  O   . GLY A 1 396 ? -4.133  34.673  6.529   1.00 18.14 ? 396 GLY A O   1 
ATOM   3201 N  N   . GLN A 1 397 ? -2.217  35.887  7.011   1.00 18.33 ? 397 GLN A N   1 
ATOM   3202 C  CA  . GLN A 1 397 ? -1.261  34.748  6.888   1.00 18.35 ? 397 GLN A CA  1 
ATOM   3203 C  C   . GLN A 1 397 ? -1.547  33.717  7.996   1.00 17.07 ? 397 GLN A C   1 
ATOM   3204 O  O   . GLN A 1 397 ? -1.278  32.516  7.777   1.00 19.07 ? 397 GLN A O   1 
ATOM   3205 C  CB  . GLN A 1 397 ? 0.191   35.255  6.836   1.00 17.39 ? 397 GLN A CB  1 
ATOM   3206 C  CG  . GLN A 1 397 ? 0.753   35.652  8.185   1.00 18.35 ? 397 GLN A CG  1 
ATOM   3207 C  CD  . GLN A 1 397 ? 2.004   36.481  8.066   1.00 19.59 ? 397 GLN A CD  1 
ATOM   3208 O  OE1 . GLN A 1 397 ? 2.749   36.416  7.083   1.00 24.80 ? 397 GLN A OE1 1 
ATOM   3209 N  NE2 . GLN A 1 397 ? 2.243   37.289  9.078   1.00 19.81 ? 397 GLN A NE2 1 
ATOM   3210 N  N   . ARG A 1 398 ? -2.161  34.114  9.100   1.00 16.66 ? 398 ARG A N   1 
ATOM   3211 C  CA  . ARG A 1 398 ? -2.630  33.149  10.145  1.00 16.48 ? 398 ARG A CA  1 
ATOM   3212 C  C   . ARG A 1 398 ? -4.080  32.673  9.927   1.00 16.95 ? 398 ARG A C   1 
ATOM   3213 O  O   . ARG A 1 398 ? -4.653  32.038  10.843  1.00 18.91 ? 398 ARG A O   1 
ATOM   3214 C  CB  . ARG A 1 398 ? -2.464  33.771  11.533  1.00 15.74 ? 398 ARG A CB  1 
ATOM   3215 C  CG  . ARG A 1 398 ? -1.022  34.131  11.852  1.00 16.18 ? 398 ARG A CG  1 
ATOM   3216 C  CD  . ARG A 1 398 ? -0.027  33.018  11.559  1.00 15.10 ? 398 ARG A CD  1 
ATOM   3217 N  NE  . ARG A 1 398 ? -0.254  31.798  12.335  1.00 14.71 ? 398 ARG A NE  1 
ATOM   3218 C  CZ  . ARG A 1 398 ? 0.208   31.585  13.562  1.00 15.00 ? 398 ARG A CZ  1 
ATOM   3219 N  NH1 . ARG A 1 398 ? 0.898   32.526  14.165  1.00 15.59 ? 398 ARG A NH1 1 
ATOM   3220 N  NH2 . ARG A 1 398 ? -0.011  30.443  14.198  1.00 15.71 ? 398 ARG A NH2 1 
ATOM   3221 N  N   . ALA A 1 399 ? -4.682  32.891  8.766   1.00 17.19 ? 399 ALA A N   1 
ATOM   3222 C  CA  . ALA A 1 399 ? -5.952  32.215  8.415   1.00 16.73 ? 399 ALA A CA  1 
ATOM   3223 C  C   . ALA A 1 399 ? -5.735  30.691  8.319   1.00 16.26 ? 399 ALA A C   1 
ATOM   3224 O  O   . ALA A 1 399 ? -4.560  30.240  8.152   1.00 14.85 ? 399 ALA A O   1 
ATOM   3225 C  CB  . ALA A 1 399 ? -6.494  32.773  7.125   1.00 16.73 ? 399 ALA A CB  1 
ATOM   3226 N  N   . CYS A 1 400 ? -6.844  29.939  8.405   1.00 15.68 ? 400 CYS A N   1 
ATOM   3227 C  CA  . CYS A 1 400 ? -6.924  28.455  8.350   1.00 16.39 ? 400 CYS A CA  1 
ATOM   3228 C  C   . CYS A 1 400 ? -6.254  27.893  7.079   1.00 16.92 ? 400 CYS A C   1 
ATOM   3229 O  O   . CYS A 1 400 ? -6.728  28.128  5.976   1.00 14.54 ? 400 CYS A O   1 
ATOM   3230 C  CB  . CYS A 1 400 ? -8.385  28.026  8.383   1.00 15.66 ? 400 CYS A CB  1 
ATOM   3231 S  SG  . CYS A 1 400 ? -8.634  26.239  8.498   1.00 15.11 ? 400 CYS A SG  1 
ATOM   3232 N  N   . ILE A 1 401 ? -5.209  27.094  7.235   1.00 19.33 ? 401 ILE A N   1 
ATOM   3233 C  CA  . ILE A 1 401 ? -4.515  26.455  6.073   1.00 19.75 ? 401 ILE A CA  1 
ATOM   3234 C  C   . ILE A 1 401 ? -5.440  25.368  5.482   1.00 19.06 ? 401 ILE A C   1 
ATOM   3235 O  O   . ILE A 1 401 ? -5.353  25.150  4.267   1.00 17.40 ? 401 ILE A O   1 
ATOM   3236 C  CB  . ILE A 1 401 ? -3.121  25.937  6.489   1.00 19.49 ? 401 ILE A CB  1 
ATOM   3237 C  CG1 . ILE A 1 401 ? -2.188  25.761  5.284   1.00 19.53 ? 401 ILE A CG1 1 
ATOM   3238 C  CG2 . ILE A 1 401 ? -3.222  24.672  7.330   1.00 18.99 ? 401 ILE A CG2 1 
ATOM   3239 C  CD1 . ILE A 1 401 ? -0.756  25.393  5.643   1.00 20.42 ? 401 ILE A CD1 1 
ATOM   3240 N  N   . GLY A 1 402 ? -6.346  24.801  6.299   1.00 19.30 ? 402 GLY A N   1 
ATOM   3241 C  CA  . GLY A 1 402 ? -7.324  23.746  5.933   1.00 18.72 ? 402 GLY A CA  1 
ATOM   3242 C  C   . GLY A 1 402 ? -8.631  24.246  5.327   1.00 17.83 ? 402 GLY A C   1 
ATOM   3243 O  O   . GLY A 1 402 ? -9.516  23.426  5.116   1.00 18.05 ? 402 GLY A O   1 
ATOM   3244 N  N   . GLN A 1 403 ? -8.764  25.533  5.012   1.00 18.89 ? 403 GLN A N   1 
ATOM   3245 C  CA  . GLN A 1 403 ? -10.027 26.129  4.502   1.00 19.13 ? 403 GLN A CA  1 
ATOM   3246 C  C   . GLN A 1 403 ? -10.504 25.430  3.213   1.00 20.01 ? 403 GLN A C   1 
ATOM   3247 O  O   . GLN A 1 403 ? -11.715 25.174  3.105   1.00 19.26 ? 403 GLN A O   1 
ATOM   3248 C  CB  . GLN A 1 403 ? -9.839  27.618  4.253   1.00 19.70 ? 403 GLN A CB  1 
ATOM   3249 C  CG  . GLN A 1 403 ? -11.100 28.265  3.709   1.00 19.50 ? 403 GLN A CG  1 
ATOM   3250 C  CD  . GLN A 1 403 ? -10.885 29.712  3.369   1.00 20.56 ? 403 GLN A CD  1 
ATOM   3251 O  OE1 . GLN A 1 403 ? -10.077 30.404  3.992   1.00 20.01 ? 403 GLN A OE1 1 
ATOM   3252 N  NE2 . GLN A 1 403 ? -11.639 30.186  2.387   1.00 21.69 ? 403 GLN A NE2 1 
ATOM   3253 N  N   . GLN A 1 404 ? -9.613  25.179  2.252   1.00 20.43 ? 404 GLN A N   1 
ATOM   3254 C  CA  . GLN A 1 404 ? -9.950  24.492  0.968   1.00 22.04 ? 404 GLN A CA  1 
ATOM   3255 C  C   . GLN A 1 404 ? -10.356 23.041  1.274   1.00 21.81 ? 404 GLN A C   1 
ATOM   3256 O  O   . GLN A 1 404 ? -11.332 22.534  0.695   1.00 21.61 ? 404 GLN A O   1 
ATOM   3257 C  CB  . GLN A 1 404 ? -8.750  24.474  0.003   1.00 24.61 ? 404 GLN A CB  1 
ATOM   3258 C  CG  . GLN A 1 404 ? -8.019  25.806  -0.175  1.00 24.22 ? 404 GLN A CG  1 
ATOM   3259 C  CD  . GLN A 1 404 ? -8.953  26.867  -0.696  1.00 25.17 ? 404 GLN A CD  1 
ATOM   3260 O  OE1 . GLN A 1 404 ? -9.722  26.638  -1.621  1.00 25.42 ? 404 GLN A OE1 1 
ATOM   3261 N  NE2 . GLN A 1 404 ? -8.919  28.035  -0.080  1.00 25.86 ? 404 GLN A NE2 1 
ATOM   3262 N  N   . PHE A 1 405 ? -9.609  22.390  2.160   1.00 21.68 ? 405 PHE A N   1 
ATOM   3263 C  CA  . PHE A 1 405 ? -9.854  21.004  2.604   1.00 21.98 ? 405 PHE A CA  1 
ATOM   3264 C  C   . PHE A 1 405 ? -11.252 20.925  3.223   1.00 22.88 ? 405 PHE A C   1 
ATOM   3265 O  O   . PHE A 1 405 ? -12.044 20.053  2.805   1.00 23.58 ? 405 PHE A O   1 
ATOM   3266 C  CB  . PHE A 1 405 ? -8.751  20.565  3.556   1.00 22.12 ? 405 PHE A CB  1 
ATOM   3267 C  CG  . PHE A 1 405 ? -8.771  19.098  3.868   1.00 24.41 ? 405 PHE A CG  1 
ATOM   3268 C  CD1 . PHE A 1 405 ? -9.600  18.593  4.860   1.00 26.22 ? 405 PHE A CD1 1 
ATOM   3269 C  CD2 . PHE A 1 405 ? -7.958  18.211  3.177   1.00 25.62 ? 405 PHE A CD2 1 
ATOM   3270 C  CE1 . PHE A 1 405 ? -9.619  17.232  5.146   1.00 25.22 ? 405 PHE A CE1 1 
ATOM   3271 C  CE2 . PHE A 1 405 ? -7.961  16.854  3.482   1.00 25.33 ? 405 PHE A CE2 1 
ATOM   3272 C  CZ  . PHE A 1 405 ? -8.791  16.366  4.464   1.00 24.30 ? 405 PHE A CZ  1 
ATOM   3273 N  N   . ALA A 1 406 ? -11.563 21.803  4.178   1.00 22.85 ? 406 ALA A N   1 
ATOM   3274 C  CA  . ALA A 1 406 ? -12.825 21.753  4.956   1.00 21.64 ? 406 ALA A CA  1 
ATOM   3275 C  C   . ALA A 1 406 ? -14.009 22.020  4.010   1.00 21.25 ? 406 ALA A C   1 
ATOM   3276 O  O   . ALA A 1 406 ? -14.975 21.249  3.991   1.00 21.04 ? 406 ALA A O   1 
ATOM   3277 C  CB  . ALA A 1 406 ? -12.768 22.738  6.089   1.00 21.54 ? 406 ALA A CB  1 
ATOM   3278 N  N   . LEU A 1 407 ? -13.946 23.054  3.192   1.00 20.99 ? 407 LEU A N   1 
ATOM   3279 C  CA  . LEU A 1 407 ? -15.112 23.380  2.335   1.00 20.70 ? 407 LEU A CA  1 
ATOM   3280 C  C   . LEU A 1 407 ? -15.278 22.301  1.254   1.00 20.68 ? 407 LEU A C   1 
ATOM   3281 O  O   . LEU A 1 407 ? -16.423 22.038  0.872   1.00 18.62 ? 407 LEU A O   1 
ATOM   3282 C  CB  . LEU A 1 407 ? -14.948 24.779  1.756   1.00 19.19 ? 407 LEU A CB  1 
ATOM   3283 C  CG  . LEU A 1 407 ? -15.071 25.903  2.772   1.00 19.10 ? 407 LEU A CG  1 
ATOM   3284 C  CD1 . LEU A 1 407 ? -14.916 27.237  2.081   1.00 19.58 ? 407 LEU A CD1 1 
ATOM   3285 C  CD2 . LEU A 1 407 ? -16.401 25.834  3.523   1.00 19.53 ? 407 LEU A CD2 1 
ATOM   3286 N  N   . HIS A 1 408 ? -14.215 21.615  0.840   1.00 21.48 ? 408 HIS A N   1 
ATOM   3287 C  CA  . HIS A 1 408 ? -14.353 20.537  -0.180  1.00 20.66 ? 408 HIS A CA  1 
ATOM   3288 C  C   . HIS A 1 408 ? -15.141 19.386  0.423   1.00 20.90 ? 408 HIS A C   1 
ATOM   3289 O  O   . HIS A 1 408 ? -16.174 18.992  -0.174  1.00 18.47 ? 408 HIS A O   1 
ATOM   3290 C  CB  . HIS A 1 408 ? -13.017 20.035  -0.719  1.00 19.96 ? 408 HIS A CB  1 
ATOM   3291 C  CG  . HIS A 1 408 ? -13.193 19.242  -1.966  1.00 19.49 ? 408 HIS A CG  1 
ATOM   3292 N  ND1 . HIS A 1 408 ? -13.372 19.841  -3.217  1.00 19.80 ? 408 HIS A ND1 1 
ATOM   3293 C  CD2 . HIS A 1 408 ? -13.282 17.915  -2.164  1.00 18.77 ? 408 HIS A CD2 1 
ATOM   3294 C  CE1 . HIS A 1 408 ? -13.476 18.899  -4.133  1.00 19.31 ? 408 HIS A CE1 1 
ATOM   3295 N  NE2 . HIS A 1 408 ? -13.451 17.709  -3.509  1.00 18.74 ? 408 HIS A NE2 1 
ATOM   3296 N  N   . GLU A 1 409 ? -14.651 18.901  1.570   1.00 22.94 ? 409 GLU A N   1 
ATOM   3297 C  CA  . GLU A 1 409 ? -15.242 17.774  2.329   1.00 23.49 ? 409 GLU A CA  1 
ATOM   3298 C  C   . GLU A 1 409 ? -16.700 18.115  2.637   1.00 21.88 ? 409 GLU A C   1 
ATOM   3299 O  O   . GLU A 1 409 ? -17.554 17.288  2.356   1.00 19.05 ? 409 GLU A O   1 
ATOM   3300 C  CB  . GLU A 1 409 ? -14.464 17.482  3.613   1.00 26.73 ? 409 GLU A CB  1 
ATOM   3301 C  CG  . GLU A 1 409 ? -15.021 16.276  4.354   1.00 29.71 ? 409 GLU A CG  1 
ATOM   3302 C  CD  . GLU A 1 409 ? -14.334 15.871  5.650   1.00 32.54 ? 409 GLU A CD  1 
ATOM   3303 O  OE1 . GLU A 1 409 ? -13.470 16.635  6.161   1.00 36.02 ? 409 GLU A OE1 1 
ATOM   3304 O  OE2 . GLU A 1 409 ? -14.682 14.789  6.157   1.00 31.61 ? 409 GLU A OE2 1 
ATOM   3305 N  N   . ALA A 1 410 ? -16.950 19.293  3.213   1.00 22.74 ? 410 ALA A N   1 
ATOM   3306 C  CA  . ALA A 1 410 ? -18.294 19.755  3.640   1.00 22.23 ? 410 ALA A CA  1 
ATOM   3307 C  C   . ALA A 1 410 ? -19.228 19.706  2.428   1.00 21.14 ? 410 ALA A C   1 
ATOM   3308 O  O   . ALA A 1 410 ? -20.326 19.180  2.558   1.00 22.32 ? 410 ALA A O   1 
ATOM   3309 C  CB  . ALA A 1 410 ? -18.239 21.155  4.227   1.00 22.02 ? 410 ALA A CB  1 
ATOM   3310 N  N   . THR A 1 411 ? -18.804 20.262  1.295   1.00 20.13 ? 411 THR A N   1 
ATOM   3311 C  CA  . THR A 1 411 ? -19.642 20.394  0.080   1.00 18.16 ? 411 THR A CA  1 
ATOM   3312 C  C   . THR A 1 411 ? -19.890 18.975  -0.443  1.00 17.88 ? 411 THR A C   1 
ATOM   3313 O  O   . THR A 1 411 ? -21.061 18.630  -0.725  1.00 17.87 ? 411 THR A O   1 
ATOM   3314 C  CB  . THR A 1 411 ? -19.006 21.357  -0.936  1.00 17.39 ? 411 THR A CB  1 
ATOM   3315 O  OG1 . THR A 1 411 ? -18.612 22.559  -0.272  1.00 16.31 ? 411 THR A OG1 1 
ATOM   3316 C  CG2 . THR A 1 411 ? -19.932 21.708  -2.084  1.00 17.07 ? 411 THR A CG2 1 
ATOM   3317 N  N   . LEU A 1 412 ? -18.846 18.164  -0.527  1.00 17.34 ? 412 LEU A N   1 
ATOM   3318 C  CA  . LEU A 1 412 ? -18.975 16.772  -0.999  1.00 19.43 ? 412 LEU A CA  1 
ATOM   3319 C  C   . LEU A 1 412 ? -20.029 16.044  -0.171  1.00 20.24 ? 412 LEU A C   1 
ATOM   3320 O  O   . LEU A 1 412 ? -20.870 15.361  -0.772  1.00 21.87 ? 412 LEU A O   1 
ATOM   3321 C  CB  . LEU A 1 412 ? -17.653 16.003  -0.880  1.00 21.50 ? 412 LEU A CB  1 
ATOM   3322 C  CG  . LEU A 1 412 ? -17.838 14.506  -1.132  1.00 23.24 ? 412 LEU A CG  1 
ATOM   3323 C  CD1 . LEU A 1 412 ? -18.289 14.279  -2.571  1.00 23.47 ? 412 LEU A CD1 1 
ATOM   3324 C  CD2 . LEU A 1 412 ? -16.581 13.716  -0.794  1.00 25.00 ? 412 LEU A CD2 1 
ATOM   3325 N  N   . VAL A 1 413 ? -19.885 16.064  1.154   1.00 20.29 ? 413 VAL A N   1 
ATOM   3326 C  CA  . VAL A 1 413 ? -20.696 15.242  2.098   1.00 20.27 ? 413 VAL A CA  1 
ATOM   3327 C  C   . VAL A 1 413 ? -22.142 15.759  2.095   1.00 19.43 ? 413 VAL A C   1 
ATOM   3328 O  O   . VAL A 1 413 ? -23.072 14.949  1.977   1.00 17.32 ? 413 VAL A O   1 
ATOM   3329 C  CB  . VAL A 1 413 ? -20.057 15.269  3.496   1.00 22.26 ? 413 VAL A CB  1 
ATOM   3330 C  CG1 . VAL A 1 413 ? -21.033 14.844  4.582   1.00 22.95 ? 413 VAL A CG1 1 
ATOM   3331 C  CG2 . VAL A 1 413 ? -18.796 14.408  3.527   1.00 22.58 ? 413 VAL A CG2 1 
ATOM   3332 N  N   . LEU A 1 414 ? -22.331 17.074  2.192   1.00 19.36 ? 414 LEU A N   1 
ATOM   3333 C  CA  . LEU A 1 414 ? -23.691 17.674  2.220   1.00 19.45 ? 414 LEU A CA  1 
ATOM   3334 C  C   . LEU A 1 414 ? -24.417 17.384  0.886   1.00 18.84 ? 414 LEU A C   1 
ATOM   3335 O  O   . LEU A 1 414 ? -25.569 16.925  0.901   1.00 15.61 ? 414 LEU A O   1 
ATOM   3336 C  CB  . LEU A 1 414 ? -23.579 19.167  2.509   1.00 19.56 ? 414 LEU A CB  1 
ATOM   3337 C  CG  . LEU A 1 414 ? -24.914 19.833  2.827   1.00 20.70 ? 414 LEU A CG  1 
ATOM   3338 C  CD1 . LEU A 1 414 ? -25.720 18.989  3.818   1.00 21.44 ? 414 LEU A CD1 1 
ATOM   3339 C  CD2 . LEU A 1 414 ? -24.688 21.232  3.357   1.00 21.29 ? 414 LEU A CD2 1 
ATOM   3340 N  N   . GLY A 1 415 ? -23.725 17.575  -0.235  1.00 19.72 ? 415 GLY A N   1 
ATOM   3341 C  CA  . GLY A 1 415 ? -24.188 17.147  -1.568  1.00 20.11 ? 415 GLY A CA  1 
ATOM   3342 C  C   . GLY A 1 415 ? -24.716 15.729  -1.548  1.00 19.52 ? 415 GLY A C   1 
ATOM   3343 O  O   . GLY A 1 415 ? -25.880 15.551  -1.918  1.00 18.67 ? 415 GLY A O   1 
ATOM   3344 N  N   . MET A 1 416 ? -23.910 14.758  -1.104  1.00 20.25 ? 416 MET A N   1 
ATOM   3345 C  CA  . MET A 1 416 ? -24.312 13.323  -1.088  1.00 21.68 ? 416 MET A CA  1 
ATOM   3346 C  C   . MET A 1 416 ? -25.471 13.099  -0.090  1.00 22.24 ? 416 MET A C   1 
ATOM   3347 O  O   . MET A 1 416 ? -26.439 12.354  -0.426  1.00 19.91 ? 416 MET A O   1 
ATOM   3348 C  CB  . MET A 1 416 ? -23.108 12.436  -0.759  1.00 24.36 ? 416 MET A CB  1 
ATOM   3349 C  CG  . MET A 1 416 ? -22.045 12.469  -1.872  1.00 26.47 ? 416 MET A CG  1 
ATOM   3350 S  SD  . MET A 1 416 ? -20.688 11.271  -1.729  1.00 28.18 ? 416 MET A SD  1 
ATOM   3351 C  CE  . MET A 1 416 ? -21.657 9.765   -1.703  1.00 28.11 ? 416 MET A CE  1 
ATOM   3352 N  N   . MET A 1 417 ? -25.428 13.726  1.090   1.00 21.36 ? 417 MET A N   1 
ATOM   3353 C  CA  . MET A 1 417 ? -26.548 13.639  2.067   1.00 21.74 ? 417 MET A CA  1 
ATOM   3354 C  C   . MET A 1 417 ? -27.857 14.070  1.361   1.00 21.94 ? 417 MET A C   1 
ATOM   3355 O  O   . MET A 1 417 ? -28.885 13.330  1.442   1.00 19.86 ? 417 MET A O   1 
ATOM   3356 C  CB  . MET A 1 417 ? -26.258 14.500  3.309   1.00 21.89 ? 417 MET A CB  1 
ATOM   3357 C  CG  . MET A 1 417 ? -25.155 13.933  4.215   1.00 22.29 ? 417 MET A CG  1 
ATOM   3358 S  SD  . MET A 1 417 ? -24.566 15.093  5.509   1.00 20.86 ? 417 MET A SD  1 
ATOM   3359 C  CE  . MET A 1 417 ? -26.142 15.627  6.174   1.00 23.76 ? 417 MET A CE  1 
ATOM   3360 N  N   . LEU A 1 418 ? -27.822 15.177  0.608   1.00 21.22 ? 418 LEU A N   1 
ATOM   3361 C  CA  . LEU A 1 418 ? -29.049 15.775  0.027   1.00 20.00 ? 418 LEU A CA  1 
ATOM   3362 C  C   . LEU A 1 418 ? -29.525 14.958  -1.183  1.00 22.18 ? 418 LEU A C   1 
ATOM   3363 O  O   . LEU A 1 418 ? -30.771 14.853  -1.391  1.00 20.84 ? 418 LEU A O   1 
ATOM   3364 C  CB  . LEU A 1 418 ? -28.743 17.227  -0.306  1.00 19.73 ? 418 LEU A CB  1 
ATOM   3365 C  CG  . LEU A 1 418 ? -28.436 18.094  0.902   1.00 20.49 ? 418 LEU A CG  1 
ATOM   3366 C  CD1 . LEU A 1 418 ? -28.047 19.509  0.487   1.00 21.94 ? 418 LEU A CD1 1 
ATOM   3367 C  CD2 . LEU A 1 418 ? -29.612 18.117  1.848   1.00 22.28 ? 418 LEU A CD2 1 
ATOM   3368 N  N   . LYS A 1 419 ? -28.602 14.324  -1.913  1.00 22.13 ? 419 LYS A N   1 
ATOM   3369 C  CA  . LYS A 1 419 ? -28.943 13.423  -3.050  1.00 22.59 ? 419 LYS A CA  1 
ATOM   3370 C  C   . LYS A 1 419 ? -29.658 12.163  -2.550  1.00 23.33 ? 419 LYS A C   1 
ATOM   3371 O  O   . LYS A 1 419 ? -30.633 11.779  -3.185  1.00 21.15 ? 419 LYS A O   1 
ATOM   3372 C  CB  . LYS A 1 419 ? -27.686 13.030  -3.835  1.00 23.72 ? 419 LYS A CB  1 
ATOM   3373 C  CG  . LYS A 1 419 ? -27.845 11.896  -4.845  1.00 23.19 ? 419 LYS A CG  1 
ATOM   3374 C  CD  . LYS A 1 419 ? -26.676 11.866  -5.798  1.00 23.70 ? 419 LYS A CD  1 
ATOM   3375 C  CE  . LYS A 1 419 ? -26.598 10.637  -6.670  1.00 24.64 ? 419 LYS A CE  1 
ATOM   3376 N  NZ  . LYS A 1 419 ? -25.186 10.343  -7.032  1.00 26.81 ? 419 LYS A NZ  1 
ATOM   3377 N  N   . HIS A 1 420 ? -29.179 11.532  -1.471  1.00 24.45 ? 420 HIS A N   1 
ATOM   3378 C  CA  . HIS A 1 420 ? -29.555 10.142  -1.091  1.00 24.44 ? 420 HIS A CA  1 
ATOM   3379 C  C   . HIS A 1 420 ? -30.728 10.085  -0.092  1.00 23.75 ? 420 HIS A C   1 
ATOM   3380 O  O   . HIS A 1 420 ? -31.247 8.972   0.139   1.00 21.60 ? 420 HIS A O   1 
ATOM   3381 C  CB  . HIS A 1 420 ? -28.311 9.393   -0.583  1.00 24.17 ? 420 HIS A CB  1 
ATOM   3382 C  CG  . HIS A 1 420 ? -27.404 9.031   -1.703  1.00 23.55 ? 420 HIS A CG  1 
ATOM   3383 N  ND1 . HIS A 1 420 ? -27.751 8.073   -2.631  1.00 23.07 ? 420 HIS A ND1 1 
ATOM   3384 C  CD2 . HIS A 1 420 ? -26.211 9.529   -2.089  1.00 24.80 ? 420 HIS A CD2 1 
ATOM   3385 C  CE1 . HIS A 1 420 ? -26.794 7.974   -3.533  1.00 24.19 ? 420 HIS A CE1 1 
ATOM   3386 N  NE2 . HIS A 1 420 ? -25.833 8.854   -3.223  1.00 25.37 ? 420 HIS A NE2 1 
ATOM   3387 N  N   . PHE A 1 421 ? -31.093 11.195  0.544   1.00 24.20 ? 421 PHE A N   1 
ATOM   3388 C  CA  . PHE A 1 421 ? -32.118 11.194  1.619   1.00 24.57 ? 421 PHE A CA  1 
ATOM   3389 C  C   . PHE A 1 421 ? -32.868 12.531  1.717   1.00 25.21 ? 421 PHE A C   1 
ATOM   3390 O  O   . PHE A 1 421 ? -32.256 13.600  1.571   1.00 21.82 ? 421 PHE A O   1 
ATOM   3391 C  CB  . PHE A 1 421 ? -31.512 10.957  3.004   1.00 23.51 ? 421 PHE A CB  1 
ATOM   3392 C  CG  . PHE A 1 421 ? -30.522 9.834   3.112   1.00 23.09 ? 421 PHE A CG  1 
ATOM   3393 C  CD1 . PHE A 1 421 ? -30.939 8.552   3.408   1.00 22.98 ? 421 PHE A CD1 1 
ATOM   3394 C  CD2 . PHE A 1 421 ? -29.164 10.069  2.944   1.00 24.00 ? 421 PHE A CD2 1 
ATOM   3395 C  CE1 . PHE A 1 421 ? -30.024 7.515   3.500   1.00 22.41 ? 421 PHE A CE1 1 
ATOM   3396 C  CE2 . PHE A 1 421 ? -28.248 9.035   3.059   1.00 23.52 ? 421 PHE A CE2 1 
ATOM   3397 C  CZ  . PHE A 1 421 ? -28.683 7.760   3.336   1.00 22.89 ? 421 PHE A CZ  1 
ATOM   3398 N  N   . ASP A 1 422 ? -34.166 12.428  2.008   1.00 27.20 ? 422 ASP A N   1 
ATOM   3399 C  CA  . ASP A 1 422 ? -34.976 13.460  2.700   1.00 30.32 ? 422 ASP A CA  1 
ATOM   3400 C  C   . ASP A 1 422 ? -34.720 13.369  4.196   1.00 29.11 ? 422 ASP A C   1 
ATOM   3401 O  O   . ASP A 1 422 ? -34.513 12.240  4.685   1.00 28.87 ? 422 ASP A O   1 
ATOM   3402 C  CB  . ASP A 1 422 ? -36.477 13.258  2.506   1.00 34.58 ? 422 ASP A CB  1 
ATOM   3403 C  CG  . ASP A 1 422 ? -36.917 13.891  1.217   1.00 38.84 ? 422 ASP A CG  1 
ATOM   3404 O  OD1 . ASP A 1 422 ? -37.070 15.127  1.233   1.00 45.33 ? 422 ASP A OD1 1 
ATOM   3405 O  OD2 . ASP A 1 422 ? -36.999 13.152  0.201   1.00 38.57 ? 422 ASP A OD2 1 
ATOM   3406 N  N   . PHE A 1 423 ? -34.865 14.504  4.873   1.00 25.39 ? 423 PHE A N   1 
ATOM   3407 C  CA  . PHE A 1 423 ? -34.596 14.673  6.311   1.00 25.25 ? 423 PHE A CA  1 
ATOM   3408 C  C   . PHE A 1 423 ? -35.824 15.247  7.016   1.00 25.87 ? 423 PHE A C   1 
ATOM   3409 O  O   . PHE A 1 423 ? -36.342 16.281  6.628   1.00 29.73 ? 423 PHE A O   1 
ATOM   3410 C  CB  . PHE A 1 423 ? -33.381 15.578  6.471   1.00 24.54 ? 423 PHE A CB  1 
ATOM   3411 C  CG  . PHE A 1 423 ? -32.112 14.963  5.965   1.00 22.67 ? 423 PHE A CG  1 
ATOM   3412 C  CD1 . PHE A 1 423 ? -31.419 14.050  6.738   1.00 22.39 ? 423 PHE A CD1 1 
ATOM   3413 C  CD2 . PHE A 1 423 ? -31.620 15.295  4.715   1.00 23.49 ? 423 PHE A CD2 1 
ATOM   3414 C  CE1 . PHE A 1 423 ? -30.272 13.446  6.250   1.00 22.56 ? 423 PHE A CE1 1 
ATOM   3415 C  CE2 . PHE A 1 423 ? -30.456 14.713  4.240   1.00 23.24 ? 423 PHE A CE2 1 
ATOM   3416 C  CZ  . PHE A 1 423 ? -29.790 13.782  5.003   1.00 22.76 ? 423 PHE A CZ  1 
ATOM   3417 N  N   . GLU A 1 424 ? -36.240 14.608  8.091   1.00 27.04 ? 424 GLU A N   1 
ATOM   3418 C  CA  . GLU A 1 424 ? -37.339 15.115  8.940   1.00 30.01 ? 424 GLU A CA  1 
ATOM   3419 C  C   . GLU A 1 424 ? -36.738 15.476  10.303  1.00 26.68 ? 424 GLU A C   1 
ATOM   3420 O  O   . GLU A 1 424 ? -36.003 14.618  10.867  1.00 25.18 ? 424 GLU A O   1 
ATOM   3421 C  CB  . GLU A 1 424 ? -38.468 14.080  9.023   1.00 34.25 ? 424 GLU A CB  1 
ATOM   3422 C  CG  . GLU A 1 424 ? -39.258 14.147  10.319  1.00 40.30 ? 424 GLU A CG  1 
ATOM   3423 C  CD  . GLU A 1 424 ? -40.509 13.278  10.390  1.00 44.37 ? 424 GLU A CD  1 
ATOM   3424 O  OE1 . GLU A 1 424 ? -40.455 12.108  9.941   1.00 41.38 ? 424 GLU A OE1 1 
ATOM   3425 O  OE2 . GLU A 1 424 ? -41.539 13.785  10.908  1.00 50.04 ? 424 GLU A OE2 1 
ATOM   3426 N  N   . ASP A 1 425 ? -37.049 16.690  10.782  1.00 22.93 ? 425 ASP A N   1 
ATOM   3427 C  CA  . ASP A 1 425 ? -36.867 17.155  12.180  1.00 21.05 ? 425 ASP A CA  1 
ATOM   3428 C  C   . ASP A 1 425 ? -37.980 16.524  13.030  1.00 21.13 ? 425 ASP A C   1 
ATOM   3429 O  O   . ASP A 1 425 ? -38.795 17.240  13.584  1.00 19.83 ? 425 ASP A O   1 
ATOM   3430 C  CB  . ASP A 1 425 ? -36.829 18.690  12.188  1.00 20.86 ? 425 ASP A CB  1 
ATOM   3431 C  CG  . ASP A 1 425 ? -36.738 19.385  13.538  1.00 20.60 ? 425 ASP A CG  1 
ATOM   3432 O  OD1 . ASP A 1 425 ? -36.405 18.738  14.557  1.00 18.77 ? 425 ASP A OD1 1 
ATOM   3433 O  OD2 . ASP A 1 425 ? -37.015 20.597  13.553  1.00 22.95 ? 425 ASP A OD2 1 
ATOM   3434 N  N   . HIS A 1 426 ? -38.008 15.203  13.147  1.00 22.33 ? 426 HIS A N   1 
ATOM   3435 C  CA  . HIS A 1 426 ? -39.133 14.474  13.794  1.00 23.03 ? 426 HIS A CA  1 
ATOM   3436 C  C   . HIS A 1 426 ? -39.358 14.916  15.244  1.00 22.11 ? 426 HIS A C   1 
ATOM   3437 O  O   . HIS A 1 426 ? -40.457 14.697  15.703  1.00 23.81 ? 426 HIS A O   1 
ATOM   3438 C  CB  . HIS A 1 426 ? -38.935 12.958  13.707  1.00 24.25 ? 426 HIS A CB  1 
ATOM   3439 C  CG  . HIS A 1 426 ? -37.708 12.479  14.387  1.00 24.11 ? 426 HIS A CG  1 
ATOM   3440 N  ND1 . HIS A 1 426 ? -36.470 12.924  14.022  1.00 24.44 ? 426 HIS A ND1 1 
ATOM   3441 C  CD2 . HIS A 1 426 ? -37.532 11.603  15.409  1.00 25.78 ? 426 HIS A CD2 1 
ATOM   3442 C  CE1 . HIS A 1 426 ? -35.565 12.360  14.803  1.00 26.42 ? 426 HIS A CE1 1 
ATOM   3443 N  NE2 . HIS A 1 426 ? -36.196 11.526  15.666  1.00 25.30 ? 426 HIS A NE2 1 
ATOM   3444 N  N   . THR A 1 427 ? -38.385 15.462  15.974  1.00 21.45 ? 427 THR A N   1 
ATOM   3445 C  CA  . THR A 1 427 ? -38.541 15.706  17.435  1.00 21.32 ? 427 THR A CA  1 
ATOM   3446 C  C   . THR A 1 427 ? -38.737 17.193  17.692  1.00 23.75 ? 427 THR A C   1 
ATOM   3447 O  O   . THR A 1 427 ? -38.821 17.592  18.859  1.00 23.23 ? 427 THR A O   1 
ATOM   3448 C  CB  . THR A 1 427 ? -37.327 15.249  18.239  1.00 20.17 ? 427 THR A CB  1 
ATOM   3449 O  OG1 . THR A 1 427 ? -36.261 16.153  17.966  1.00 22.26 ? 427 THR A OG1 1 
ATOM   3450 C  CG2 . THR A 1 427 ? -36.916 13.836  17.928  1.00 20.33 ? 427 THR A CG2 1 
ATOM   3451 N  N   . ASN A 1 428 ? -38.721 17.981  16.625  1.00 27.61 ? 428 ASN A N   1 
ATOM   3452 C  CA  . ASN A 1 428 ? -38.803 19.453  16.703  1.00 29.67 ? 428 ASN A CA  1 
ATOM   3453 C  C   . ASN A 1 428 ? -37.637 19.947  17.572  1.00 29.62 ? 428 ASN A C   1 
ATOM   3454 O  O   . ASN A 1 428 ? -37.878 20.577  18.625  1.00 30.35 ? 428 ASN A O   1 
ATOM   3455 C  CB  . ASN A 1 428 ? -40.184 19.863  17.195  1.00 31.65 ? 428 ASN A CB  1 
ATOM   3456 C  CG  . ASN A 1 428 ? -40.554 21.214  16.639  1.00 39.03 ? 428 ASN A CG  1 
ATOM   3457 O  OD1 . ASN A 1 428 ? -40.394 21.445  15.444  1.00 51.82 ? 428 ASN A OD1 1 
ATOM   3458 N  ND2 . ASN A 1 428 ? -41.006 22.121  17.489  1.00 41.24 ? 428 ASN A ND2 1 
ATOM   3459 N  N   . TYR A 1 429 ? -36.410 19.630  17.161  1.00 26.57 ? 429 TYR A N   1 
ATOM   3460 C  CA  . TYR A 1 429 ? -35.167 19.853  17.949  1.00 24.79 ? 429 TYR A CA  1 
ATOM   3461 C  C   . TYR A 1 429 ? -35.010 21.343  18.294  1.00 24.26 ? 429 TYR A C   1 
ATOM   3462 O  O   . TYR A 1 429 ? -35.198 22.240  17.441  1.00 23.24 ? 429 TYR A O   1 
ATOM   3463 C  CB  . TYR A 1 429 ? -33.943 19.324  17.197  1.00 23.24 ? 429 TYR A CB  1 
ATOM   3464 C  CG  . TYR A 1 429 ? -32.611 19.718  17.787  1.00 22.30 ? 429 TYR A CG  1 
ATOM   3465 C  CD1 . TYR A 1 429 ? -32.174 19.172  18.988  1.00 21.34 ? 429 TYR A CD1 1 
ATOM   3466 C  CD2 . TYR A 1 429 ? -31.791 20.627  17.136  1.00 19.86 ? 429 TYR A CD2 1 
ATOM   3467 C  CE1 . TYR A 1 429 ? -30.949 19.512  19.526  1.00 20.15 ? 429 TYR A CE1 1 
ATOM   3468 C  CE2 . TYR A 1 429 ? -30.572 20.989  17.666  1.00 19.66 ? 429 TYR A CE2 1 
ATOM   3469 C  CZ  . TYR A 1 429 ? -30.142 20.408  18.848  1.00 20.49 ? 429 TYR A CZ  1 
ATOM   3470 O  OH  . TYR A 1 429 ? -28.942 20.769  19.367  1.00 19.81 ? 429 TYR A OH  1 
ATOM   3471 N  N   . GLU A 1 430 ? -34.687 21.585  19.557  1.00 24.85 ? 430 GLU A N   1 
ATOM   3472 C  CA  . GLU A 1 430 ? -34.375 22.908  20.147  1.00 28.45 ? 430 GLU A CA  1 
ATOM   3473 C  C   . GLU A 1 430 ? -32.842 23.063  20.225  1.00 26.67 ? 430 GLU A C   1 
ATOM   3474 O  O   . GLU A 1 430 ? -32.197 22.300  20.990  1.00 22.20 ? 430 GLU A O   1 
ATOM   3475 C  CB  . GLU A 1 430 ? -35.076 22.950  21.500  1.00 33.44 ? 430 GLU A CB  1 
ATOM   3476 C  CG  . GLU A 1 430 ? -34.781 24.178  22.329  1.00 41.45 ? 430 GLU A CG  1 
ATOM   3477 C  CD  . GLU A 1 430 ? -35.547 24.185  23.643  1.00 48.06 ? 430 GLU A CD  1 
ATOM   3478 O  OE1 . GLU A 1 430 ? -36.380 23.267  23.847  1.00 51.81 ? 430 GLU A OE1 1 
ATOM   3479 O  OE2 . GLU A 1 430 ? -35.305 25.098  24.461  1.00 55.94 ? 430 GLU A OE2 1 
ATOM   3480 N  N   . LEU A 1 431 ? -32.273 23.974  19.425  1.00 24.66 ? 431 LEU A N   1 
ATOM   3481 C  CA  . LEU A 1 431 ? -30.809 24.224  19.381  1.00 24.62 ? 431 LEU A CA  1 
ATOM   3482 C  C   . LEU A 1 431 ? -30.225 24.319  20.809  1.00 24.44 ? 431 LEU A C   1 
ATOM   3483 O  O   . LEU A 1 431 ? -30.678 25.165  21.618  1.00 26.15 ? 431 LEU A O   1 
ATOM   3484 C  CB  . LEU A 1 431 ? -30.525 25.490  18.573  1.00 23.08 ? 431 LEU A CB  1 
ATOM   3485 C  CG  . LEU A 1 431 ? -29.044 25.745  18.313  1.00 22.74 ? 431 LEU A CG  1 
ATOM   3486 C  CD1 . LEU A 1 431 ? -28.392 24.539  17.667  1.00 22.09 ? 431 LEU A CD1 1 
ATOM   3487 C  CD2 . LEU A 1 431 ? -28.845 26.978  17.452  1.00 23.00 ? 431 LEU A CD2 1 
ATOM   3488 N  N   . ASP A 1 432 ? -29.278 23.425  21.094  1.00 24.31 ? 432 ASP A N   1 
ATOM   3489 C  CA  . ASP A 1 432 ? -28.436 23.337  22.315  1.00 25.09 ? 432 ASP A CA  1 
ATOM   3490 C  C   . ASP A 1 432 ? -27.009 23.243  21.768  1.00 24.99 ? 432 ASP A C   1 
ATOM   3491 O  O   . ASP A 1 432 ? -26.755 22.369  20.901  1.00 22.19 ? 432 ASP A O   1 
ATOM   3492 C  CB  . ASP A 1 432 ? -28.893 22.166  23.191  1.00 25.44 ? 432 ASP A CB  1 
ATOM   3493 C  CG  . ASP A 1 432 ? -28.170 21.928  24.509  1.00 28.24 ? 432 ASP A CG  1 
ATOM   3494 O  OD1 . ASP A 1 432 ? -27.143 22.576  24.756  1.00 29.11 ? 432 ASP A OD1 1 
ATOM   3495 O  OD2 . ASP A 1 432 ? -28.628 21.037  25.272  1.00 30.35 ? 432 ASP A OD2 1 
ATOM   3496 N  N   . ILE A 1 433 ? -26.151 24.188  22.156  1.00 23.78 ? 433 ILE A N   1 
ATOM   3497 C  CA  . ILE A 1 433 ? -24.795 24.354  21.571  1.00 22.17 ? 433 ILE A CA  1 
ATOM   3498 C  C   . ILE A 1 433 ? -23.792 23.941  22.638  1.00 20.53 ? 433 ILE A C   1 
ATOM   3499 O  O   . ILE A 1 433 ? -23.632 24.700  23.628  1.00 17.44 ? 433 ILE A O   1 
ATOM   3500 C  CB  . ILE A 1 433 ? -24.578 25.784  21.047  1.00 21.50 ? 433 ILE A CB  1 
ATOM   3501 C  CG1 . ILE A 1 433 ? -25.446 26.046  19.825  1.00 22.74 ? 433 ILE A CG1 1 
ATOM   3502 C  CG2 . ILE A 1 433 ? -23.120 26.050  20.729  1.00 22.49 ? 433 ILE A CG2 1 
ATOM   3503 C  CD1 . ILE A 1 433 ? -25.328 27.452  19.297  1.00 23.58 ? 433 ILE A CD1 1 
ATOM   3504 N  N   . LYS A 1 434 ? -23.157 22.794  22.389  1.00 20.85 ? 434 LYS A N   1 
ATOM   3505 C  CA  . LYS A 1 434 ? -22.021 22.242  23.162  1.00 23.63 ? 434 LYS A CA  1 
ATOM   3506 C  C   . LYS A 1 434 ? -20.765 22.940  22.648  1.00 23.32 ? 434 LYS A C   1 
ATOM   3507 O  O   . LYS A 1 434 ? -20.592 22.967  21.424  1.00 24.07 ? 434 LYS A O   1 
ATOM   3508 C  CB  . LYS A 1 434 ? -21.957 20.720  23.000  1.00 28.29 ? 434 LYS A CB  1 
ATOM   3509 C  CG  . LYS A 1 434 ? -20.670 20.057  23.490  1.00 33.57 ? 434 LYS A CG  1 
ATOM   3510 C  CD  . LYS A 1 434 ? -20.411 18.675  22.884  1.00 38.94 ? 434 LYS A CD  1 
ATOM   3511 C  CE  . LYS A 1 434 ? -20.801 17.508  23.782  1.00 43.11 ? 434 LYS A CE  1 
ATOM   3512 N  NZ  . LYS A 1 434 ? -19.784 17.247  24.835  1.00 44.87 ? 434 LYS A NZ  1 
ATOM   3513 N  N   . GLU A 1 435 ? -19.977 23.521  23.557  1.00 23.50 ? 435 GLU A N   1 
ATOM   3514 C  CA  . GLU A 1 435 ? -18.677 24.189  23.268  1.00 23.69 ? 435 GLU A CA  1 
ATOM   3515 C  C   . GLU A 1 435 ? -17.515 23.297  23.731  1.00 21.40 ? 435 GLU A C   1 
ATOM   3516 O  O   . GLU A 1 435 ? -17.411 22.998  24.918  1.00 22.82 ? 435 GLU A O   1 
ATOM   3517 C  CB  . GLU A 1 435 ? -18.627 25.574  23.926  1.00 23.44 ? 435 GLU A CB  1 
ATOM   3518 C  CG  . GLU A 1 435 ? -19.852 26.417  23.653  1.00 22.48 ? 435 GLU A CG  1 
ATOM   3519 C  CD  . GLU A 1 435 ? -19.711 27.883  24.030  1.00 23.40 ? 435 GLU A CD  1 
ATOM   3520 O  OE1 . GLU A 1 435 ? -20.740 28.605  24.031  1.00 23.30 ? 435 GLU A OE1 1 
ATOM   3521 O  OE2 . GLU A 1 435 ? -18.583 28.301  24.328  1.00 21.66 ? 435 GLU A OE2 1 
ATOM   3522 N  N   . THR A 1 436 ? -16.670 22.855  22.804  1.00 22.03 ? 436 THR A N   1 
ATOM   3523 C  CA  . THR A 1 436 ? -15.347 22.239  23.107  1.00 21.20 ? 436 THR A CA  1 
ATOM   3524 C  C   . THR A 1 436 ? -14.298 23.271  22.679  1.00 22.26 ? 436 THR A C   1 
ATOM   3525 O  O   . THR A 1 436 ? -14.364 24.431  23.130  1.00 23.82 ? 436 THR A O   1 
ATOM   3526 C  CB  . THR A 1 436 ? -15.273 20.840  22.475  1.00 20.95 ? 436 THR A CB  1 
ATOM   3527 O  OG1 . THR A 1 436 ? -15.579 20.927  21.076  1.00 20.13 ? 436 THR A OG1 1 
ATOM   3528 C  CG2 . THR A 1 436 ? -16.220 19.859  23.142  1.00 20.07 ? 436 THR A CG2 1 
ATOM   3529 N  N   . LEU A 1 437 ? -13.378 22.915  21.797  1.00 24.03 ? 437 LEU A N   1 
ATOM   3530 C  CA  . LEU A 1 437 ? -12.563 23.933  21.093  1.00 23.32 ? 437 LEU A CA  1 
ATOM   3531 C  C   . LEU A 1 437 ? -13.530 24.679  20.167  1.00 23.08 ? 437 LEU A C   1 
ATOM   3532 O  O   . LEU A 1 437 ? -13.314 25.889  19.903  1.00 20.56 ? 437 LEU A O   1 
ATOM   3533 C  CB  . LEU A 1 437 ? -11.437 23.210  20.335  1.00 25.12 ? 437 LEU A CB  1 
ATOM   3534 C  CG  . LEU A 1 437 ? -10.488 24.106  19.535  1.00 25.67 ? 437 LEU A CG  1 
ATOM   3535 C  CD1 . LEU A 1 437 ? -9.550  24.893  20.453  1.00 25.02 ? 437 LEU A CD1 1 
ATOM   3536 C  CD2 . LEU A 1 437 ? -9.693  23.296  18.515  1.00 25.82 ? 437 LEU A CD2 1 
ATOM   3537 N  N   . THR A 1 438 ? -14.588 23.965  19.728  1.00 21.44 ? 438 THR A N   1 
ATOM   3538 C  CA  . THR A 1 438 ? -15.548 24.415  18.695  1.00 19.15 ? 438 THR A CA  1 
ATOM   3539 C  C   . THR A 1 438 ? -16.997 24.280  19.183  1.00 18.86 ? 438 THR A C   1 
ATOM   3540 O  O   . THR A 1 438 ? -17.258 23.597  20.192  1.00 18.55 ? 438 THR A O   1 
ATOM   3541 C  CB  . THR A 1 438 ? -15.367 23.625  17.401  1.00 18.18 ? 438 THR A CB  1 
ATOM   3542 O  OG1 . THR A 1 438 ? -15.559 22.244  17.705  1.00 18.92 ? 438 THR A OG1 1 
ATOM   3543 C  CG2 . THR A 1 438 ? -14.017 23.872  16.770  1.00 18.55 ? 438 THR A CG2 1 
ATOM   3544 N  N   . LEU A 1 439 ? -17.897 24.940  18.465  1.00 18.07 ? 439 LEU A N   1 
ATOM   3545 C  CA  . LEU A 1 439 ? -19.358 24.909  18.693  1.00 17.72 ? 439 LEU A CA  1 
ATOM   3546 C  C   . LEU A 1 439 ? -19.933 23.735  17.896  1.00 17.79 ? 439 LEU A C   1 
ATOM   3547 O  O   . LEU A 1 439 ? -19.599 23.613  16.707  1.00 16.93 ? 439 LEU A O   1 
ATOM   3548 C  CB  . LEU A 1 439 ? -19.953 26.246  18.230  1.00 16.71 ? 439 LEU A CB  1 
ATOM   3549 C  CG  . LEU A 1 439 ? -19.397 27.509  18.877  1.00 15.87 ? 439 LEU A CG  1 
ATOM   3550 C  CD1 . LEU A 1 439 ? -20.180 28.725  18.437  1.00 15.10 ? 439 LEU A CD1 1 
ATOM   3551 C  CD2 . LEU A 1 439 ? -19.392 27.411  20.400  1.00 16.50 ? 439 LEU A CD2 1 
ATOM   3552 N  N   . LYS A 1 440 ? -20.746 22.898  18.535  1.00 20.56 ? 440 LYS A N   1 
ATOM   3553 C  CA  . LYS A 1 440 ? -21.580 21.867  17.851  1.00 23.40 ? 440 LYS A CA  1 
ATOM   3554 C  C   . LYS A 1 440 ? -22.986 21.879  18.448  1.00 23.72 ? 440 LYS A C   1 
ATOM   3555 O  O   . LYS A 1 440 ? -23.159 22.223  19.616  1.00 24.50 ? 440 LYS A O   1 
ATOM   3556 C  CB  . LYS A 1 440 ? -20.984 20.464  18.030  1.00 25.78 ? 440 LYS A CB  1 
ATOM   3557 C  CG  . LYS A 1 440 ? -19.830 20.103  17.102  1.00 26.22 ? 440 LYS A CG  1 
ATOM   3558 C  CD  . LYS A 1 440 ? -19.256 18.731  17.394  1.00 26.20 ? 440 LYS A CD  1 
ATOM   3559 C  CE  . LYS A 1 440 ? -18.057 18.417  16.536  1.00 26.60 ? 440 LYS A CE  1 
ATOM   3560 N  NZ  . LYS A 1 440 ? -17.239 17.340  17.135  1.00 29.17 ? 440 LYS A NZ  1 
ATOM   3561 N  N   . PRO A 1 441 ? -24.014 21.442  17.690  1.00 24.62 ? 441 PRO A N   1 
ATOM   3562 C  CA  . PRO A 1 441 ? -25.345 21.249  18.246  1.00 25.43 ? 441 PRO A CA  1 
ATOM   3563 C  C   . PRO A 1 441 ? -25.312 19.977  19.088  1.00 26.96 ? 441 PRO A C   1 
ATOM   3564 O  O   . PRO A 1 441 ? -24.829 19.020  18.582  1.00 34.83 ? 441 PRO A O   1 
ATOM   3565 C  CB  . PRO A 1 441 ? -26.261 21.091  17.027  1.00 26.42 ? 441 PRO A CB  1 
ATOM   3566 C  CG  . PRO A 1 441 ? -25.350 20.700  15.886  1.00 26.95 ? 441 PRO A CG  1 
ATOM   3567 C  CD  . PRO A 1 441 ? -23.941 21.088  16.266  1.00 25.52 ? 441 PRO A CD  1 
ATOM   3568 N  N   . GLU A 1 442 ? -25.735 20.016  20.350  1.00 26.65 ? 442 GLU A N   1 
ATOM   3569 C  CA  . GLU A 1 442 ? -25.771 18.814  21.215  1.00 25.48 ? 442 GLU A CA  1 
ATOM   3570 C  C   . GLU A 1 442 ? -27.176 18.217  21.114  1.00 23.99 ? 442 GLU A C   1 
ATOM   3571 O  O   . GLU A 1 442 ? -28.132 18.993  21.116  1.00 23.46 ? 442 GLU A O   1 
ATOM   3572 C  CB  . GLU A 1 442 ? -25.397 19.182  22.646  1.00 27.69 ? 442 GLU A CB  1 
ATOM   3573 C  CG  . GLU A 1 442 ? -24.883 18.001  23.454  1.00 31.02 ? 442 GLU A CG  1 
ATOM   3574 C  CD  . GLU A 1 442 ? -24.640 18.327  24.922  1.00 38.75 ? 442 GLU A CD  1 
ATOM   3575 O  OE1 . GLU A 1 442 ? -24.911 19.501  25.365  1.00 41.69 ? 442 GLU A OE1 1 
ATOM   3576 O  OE2 . GLU A 1 442 ? -24.184 17.412  25.629  1.00 45.39 ? 442 GLU A OE2 1 
ATOM   3577 N  N   . GLY A 1 443 ? -27.296 16.892  21.000  1.00 23.15 ? 443 GLY A N   1 
ATOM   3578 C  CA  . GLY A 1 443 ? -28.596 16.184  20.979  1.00 22.45 ? 443 GLY A CA  1 
ATOM   3579 C  C   . GLY A 1 443 ? -29.345 16.308  19.643  1.00 21.13 ? 443 GLY A C   1 
ATOM   3580 O  O   . GLY A 1 443 ? -30.521 15.922  19.604  1.00 18.23 ? 443 GLY A O   1 
ATOM   3581 N  N   . PHE A 1 444 ? -28.724 16.836  18.583  1.00 19.36 ? 444 PHE A N   1 
ATOM   3582 C  CA  . PHE A 1 444 ? -29.398 17.037  17.278  1.00 20.89 ? 444 PHE A CA  1 
ATOM   3583 C  C   . PHE A 1 444 ? -29.587 15.652  16.662  1.00 20.91 ? 444 PHE A C   1 
ATOM   3584 O  O   . PHE A 1 444 ? -28.560 14.977  16.353  1.00 18.98 ? 444 PHE A O   1 
ATOM   3585 C  CB  . PHE A 1 444 ? -28.620 18.002  16.370  1.00 23.00 ? 444 PHE A CB  1 
ATOM   3586 C  CG  . PHE A 1 444 ? -29.255 18.295  15.027  1.00 23.29 ? 444 PHE A CG  1 
ATOM   3587 C  CD1 . PHE A 1 444 ? -30.635 18.391  14.892  1.00 22.60 ? 444 PHE A CD1 1 
ATOM   3588 C  CD2 . PHE A 1 444 ? -28.469 18.512  13.901  1.00 23.71 ? 444 PHE A CD2 1 
ATOM   3589 C  CE1 . PHE A 1 444 ? -31.214 18.679  13.667  1.00 21.79 ? 444 PHE A CE1 1 
ATOM   3590 C  CE2 . PHE A 1 444 ? -29.051 18.775  12.669  1.00 23.10 ? 444 PHE A CE2 1 
ATOM   3591 C  CZ  . PHE A 1 444 ? -30.424 18.854  12.555  1.00 21.86 ? 444 PHE A CZ  1 
ATOM   3592 N  N   . VAL A 1 445 ? -30.857 15.256  16.526  1.00 21.00 ? 445 VAL A N   1 
ATOM   3593 C  CA  . VAL A 1 445 ? -31.312 13.983  15.897  1.00 22.07 ? 445 VAL A CA  1 
ATOM   3594 C  C   . VAL A 1 445 ? -32.236 14.358  14.740  1.00 22.16 ? 445 VAL A C   1 
ATOM   3595 O  O   . VAL A 1 445 ? -33.010 15.322  14.905  1.00 21.05 ? 445 VAL A O   1 
ATOM   3596 C  CB  . VAL A 1 445 ? -32.026 13.032  16.889  1.00 23.19 ? 445 VAL A CB  1 
ATOM   3597 C  CG1 . VAL A 1 445 ? -31.060 12.412  17.888  1.00 23.56 ? 445 VAL A CG1 1 
ATOM   3598 C  CG2 . VAL A 1 445 ? -33.184 13.702  17.624  1.00 21.73 ? 445 VAL A CG2 1 
ATOM   3599 N  N   . VAL A 1 446 ? -32.173 13.606  13.633  1.00 23.88 ? 446 VAL A N   1 
ATOM   3600 C  CA  . VAL A 1 446 ? -33.170 13.668  12.513  1.00 25.35 ? 446 VAL A CA  1 
ATOM   3601 C  C   . VAL A 1 446 ? -33.527 12.249  12.072  1.00 25.77 ? 446 VAL A C   1 
ATOM   3602 O  O   . VAL A 1 446 ? -32.793 11.314  12.460  1.00 23.57 ? 446 VAL A O   1 
ATOM   3603 C  CB  . VAL A 1 446 ? -32.634 14.451  11.306  1.00 24.76 ? 446 VAL A CB  1 
ATOM   3604 C  CG1 . VAL A 1 446 ? -32.405 15.912  11.642  1.00 25.63 ? 446 VAL A CG1 1 
ATOM   3605 C  CG2 . VAL A 1 446 ? -31.383 13.797  10.735  1.00 24.35 ? 446 VAL A CG2 1 
ATOM   3606 N  N   . LYS A 1 447 ? -34.566 12.112  11.243  1.00 25.82 ? 447 LYS A N   1 
ATOM   3607 C  CA  . LYS A 1 447 ? -34.807 10.875  10.461  1.00 27.62 ? 447 LYS A CA  1 
ATOM   3608 C  C   . LYS A 1 447 ? -34.455 11.162  9.009   1.00 26.41 ? 447 LYS A C   1 
ATOM   3609 O  O   . LYS A 1 447 ? -34.754 12.257  8.529   1.00 28.53 ? 447 LYS A O   1 
ATOM   3610 C  CB  . LYS A 1 447 ? -36.233 10.365  10.654  1.00 31.45 ? 447 LYS A CB  1 
ATOM   3611 C  CG  . LYS A 1 447 ? -36.502 9.817   12.053  1.00 35.81 ? 447 LYS A CG  1 
ATOM   3612 C  CD  . LYS A 1 447 ? -37.611 8.765   12.150  1.00 39.97 ? 447 LYS A CD  1 
ATOM   3613 C  CE  . LYS A 1 447 ? -38.082 8.573   13.579  1.00 44.82 ? 447 LYS A CE  1 
ATOM   3614 N  NZ  . LYS A 1 447 ? -39.137 7.540   13.673  1.00 50.82 ? 447 LYS A NZ  1 
ATOM   3615 N  N   . ALA A 1 448 ? -33.726 10.256  8.376   1.00 25.43 ? 448 ALA A N   1 
ATOM   3616 C  CA  . ALA A 1 448 ? -33.433 10.329  6.932   1.00 27.73 ? 448 ALA A CA  1 
ATOM   3617 C  C   . ALA A 1 448 ? -34.315 9.307   6.233   1.00 30.66 ? 448 ALA A C   1 
ATOM   3618 O  O   . ALA A 1 448 ? -34.257 8.133   6.647   1.00 40.78 ? 448 ALA A O   1 
ATOM   3619 C  CB  . ALA A 1 448 ? -31.991 10.040  6.667   1.00 28.11 ? 448 ALA A CB  1 
ATOM   3620 N  N   . LYS A 1 449 ? -35.125 9.721   5.258   1.00 29.48 ? 449 LYS A N   1 
ATOM   3621 C  CA  . LYS A 1 449 ? -35.901 8.759   4.451   1.00 31.09 ? 449 LYS A CA  1 
ATOM   3622 C  C   . LYS A 1 449 ? -35.120 8.548   3.157   1.00 27.26 ? 449 LYS A C   1 
ATOM   3623 O  O   . LYS A 1 449 ? -34.705 9.541   2.552   1.00 26.60 ? 449 LYS A O   1 
ATOM   3624 C  CB  . LYS A 1 449 ? -37.351 9.220   4.267   1.00 37.46 ? 449 LYS A CB  1 
ATOM   3625 C  CG  . LYS A 1 449 ? -38.401 8.184   4.678   1.00 46.20 ? 449 LYS A CG  1 
ATOM   3626 C  CD  . LYS A 1 449 ? -37.886 6.736   4.712   1.00 52.11 ? 449 LYS A CD  1 
ATOM   3627 C  CE  . LYS A 1 449 ? -38.954 5.692   4.961   1.00 55.73 ? 449 LYS A CE  1 
ATOM   3628 N  NZ  . LYS A 1 449 ? -39.823 5.507   3.775   1.00 57.67 ? 449 LYS A NZ  1 
ATOM   3629 N  N   . SER A 1 450 ? -34.842 7.298   2.803   1.00 25.71 ? 450 SER A N   1 
ATOM   3630 C  CA  . SER A 1 450 ? -33.966 6.973   1.654   1.00 24.59 ? 450 SER A CA  1 
ATOM   3631 C  C   . SER A 1 450 ? -34.675 7.355   0.356   1.00 25.02 ? 450 SER A C   1 
ATOM   3632 O  O   . SER A 1 450 ? -35.875 7.081   0.247   1.00 25.29 ? 450 SER A O   1 
ATOM   3633 C  CB  . SER A 1 450 ? -33.560 5.548   1.645   1.00 22.94 ? 450 SER A CB  1 
ATOM   3634 O  OG  . SER A 1 450 ? -32.695 5.337   0.544   1.00 23.21 ? 450 SER A OG  1 
ATOM   3635 N  N   . LYS A 1 451 ? -33.959 7.966   -0.588  1.00 25.26 ? 451 LYS A N   1 
ATOM   3636 C  CA  . LYS A 1 451 ? -34.494 8.308   -1.927  1.00 26.93 ? 451 LYS A CA  1 
ATOM   3637 C  C   . LYS A 1 451 ? -34.141 7.155   -2.864  1.00 28.80 ? 451 LYS A C   1 
ATOM   3638 O  O   . LYS A 1 451 ? -34.429 7.283   -4.050  1.00 31.28 ? 451 LYS A O   1 
ATOM   3639 C  CB  . LYS A 1 451 ? -33.991 9.673   -2.404  1.00 29.08 ? 451 LYS A CB  1 
ATOM   3640 C  CG  . LYS A 1 451 ? -34.473 10.847  -1.554  1.00 31.49 ? 451 LYS A CG  1 
ATOM   3641 C  CD  . LYS A 1 451 ? -33.937 12.213  -1.954  1.00 31.24 ? 451 LYS A CD  1 
ATOM   3642 C  CE  . LYS A 1 451 ? -34.957 13.044  -2.697  1.00 37.38 ? 451 LYS A CE  1 
ATOM   3643 N  NZ  . LYS A 1 451 ? -35.019 14.441  -2.195  1.00 42.77 ? 451 LYS A NZ  1 
ATOM   3644 N  N   . LYS A 1 452 ? -33.585 6.065   -2.324  1.00 28.91 ? 452 LYS A N   1 
ATOM   3645 C  CA  . LYS A 1 452 ? -33.381 4.766   -3.022  1.00 34.45 ? 452 LYS A CA  1 
ATOM   3646 C  C   . LYS A 1 452 ? -32.506 4.976   -4.271  1.00 34.68 ? 452 LYS A C   1 
ATOM   3647 O  O   . LYS A 1 452 ? -32.649 4.227   -5.247  1.00 34.75 ? 452 LYS A O   1 
ATOM   3648 C  CB  . LYS A 1 452 ? -34.724 4.118   -3.379  1.00 39.15 ? 452 LYS A CB  1 
ATOM   3649 C  CG  . LYS A 1 452 ? -35.780 4.095   -2.269  1.00 44.51 ? 452 LYS A CG  1 
ATOM   3650 C  CD  . LYS A 1 452 ? -35.823 2.814   -1.456  1.00 45.82 ? 452 LYS A CD  1 
ATOM   3651 C  CE  . LYS A 1 452 ? -34.615 2.639   -0.563  1.00 48.15 ? 452 LYS A CE  1 
ATOM   3652 N  NZ  . LYS A 1 452 ? -34.955 1.861   0.652   1.00 46.77 ? 452 LYS A NZ  1 
ATOM   3653 N  N   . ILE A 1 453 ? -31.589 5.938   -4.241  1.00 34.52 ? 453 ILE A N   1 
ATOM   3654 C  CA  . ILE A 1 453 ? -30.654 6.152   -5.372  1.00 34.50 ? 453 ILE A CA  1 
ATOM   3655 C  C   . ILE A 1 453 ? -29.441 5.283   -5.095  1.00 34.60 ? 453 ILE A C   1 
ATOM   3656 O  O   . ILE A 1 453 ? -28.796 5.429   -4.060  1.00 32.97 ? 453 ILE A O   1 
ATOM   3657 C  CB  . ILE A 1 453 ? -30.331 7.642   -5.579  1.00 34.19 ? 453 ILE A CB  1 
ATOM   3658 C  CG1 . ILE A 1 453 ? -31.614 8.435   -5.834  1.00 33.72 ? 453 ILE A CG1 1 
ATOM   3659 C  CG2 . ILE A 1 453 ? -29.320 7.816   -6.705  1.00 33.35 ? 453 ILE A CG2 1 
ATOM   3660 C  CD1 . ILE A 1 453 ? -31.592 9.843   -5.308  1.00 35.09 ? 453 ILE A CD1 1 
ATOM   3661 N  N   . PRO A 1 454 ? -29.158 4.301   -5.979  1.00 39.44 ? 454 PRO A N   1 
ATOM   3662 C  CA  . PRO A 1 454 ? -28.002 3.411   -5.809  1.00 40.68 ? 454 PRO A CA  1 
ATOM   3663 C  C   . PRO A 1 454 ? -26.660 4.165   -5.854  1.00 39.39 ? 454 PRO A C   1 
ATOM   3664 O  O   . PRO A 1 454 ? -26.562 5.175   -6.518  1.00 32.52 ? 454 PRO A O   1 
ATOM   3665 C  CB  . PRO A 1 454 ? -28.105 2.438   -6.998  1.00 41.07 ? 454 PRO A CB  1 
ATOM   3666 C  CG  . PRO A 1 454 ? -28.923 3.208   -8.024  1.00 42.61 ? 454 PRO A CG  1 
ATOM   3667 C  CD  . PRO A 1 454 ? -29.922 4.006   -7.204  1.00 38.58 ? 454 PRO A CD  1 
ATOM   3668 N  N   . LEU A 1 455 ? -25.659 3.666   -5.127  1.00 40.75 ? 455 LEU A N   1 
ATOM   3669 C  CA  . LEU A 1 455 ? -24.274 4.204   -5.161  1.00 42.53 ? 455 LEU A CA  1 
ATOM   3670 C  C   . LEU A 1 455 ? -23.484 3.524   -6.292  1.00 51.53 ? 455 LEU A C   1 
ATOM   3671 O  O   . LEU A 1 455 ? -24.049 2.833   -7.156  1.00 61.90 ? 455 LEU A O   1 
ATOM   3672 C  CB  . LEU A 1 455 ? -23.642 4.000   -3.784  1.00 39.51 ? 455 LEU A CB  1 
ATOM   3673 C  CG  . LEU A 1 455 ? -23.959 5.108   -2.787  1.00 38.54 ? 455 LEU A CG  1 
ATOM   3674 C  CD1 . LEU A 1 455 ? -23.387 4.779   -1.424  1.00 39.69 ? 455 LEU A CD1 1 
ATOM   3675 C  CD2 . LEU A 1 455 ? -23.430 6.446   -3.274  1.00 38.74 ? 455 LEU A CD2 1 
ATOM   3676 O  OXT . LEU A 1 455 ? -22.257 3.643   -6.424  1.00 56.55 ? 455 LEU A OXT 1 
ATOM   3677 N  N   . THR B 1 1   ? -25.812 -60.158 22.673  1.00 43.79 ? 1   THR B N   1 
ATOM   3678 C  CA  . THR B 1 1   ? -26.333 -60.616 23.996  1.00 45.14 ? 1   THR B CA  1 
ATOM   3679 C  C   . THR B 1 1   ? -26.745 -59.400 24.838  1.00 46.51 ? 1   THR B C   1 
ATOM   3680 O  O   . THR B 1 1   ? -26.076 -58.348 24.729  1.00 44.13 ? 1   THR B O   1 
ATOM   3681 C  CB  . THR B 1 1   ? -25.282 -61.442 24.746  1.00 44.92 ? 1   THR B CB  1 
ATOM   3682 O  OG1 . THR B 1 1   ? -24.685 -62.317 23.788  1.00 45.77 ? 1   THR B OG1 1 
ATOM   3683 C  CG2 . THR B 1 1   ? -25.851 -62.219 25.916  1.00 42.56 ? 1   THR B CG2 1 
ATOM   3684 N  N   . ILE B 1 2   ? -27.781 -59.563 25.667  1.00 47.11 ? 2   ILE B N   1 
ATOM   3685 C  CA  . ILE B 1 2   ? -28.334 -58.506 26.568  1.00 46.97 ? 2   ILE B CA  1 
ATOM   3686 C  C   . ILE B 1 2   ? -27.233 -58.100 27.551  1.00 46.76 ? 2   ILE B C   1 
ATOM   3687 O  O   . ILE B 1 2   ? -26.923 -58.917 28.424  1.00 49.89 ? 2   ILE B O   1 
ATOM   3688 C  CB  . ILE B 1 2   ? -29.604 -59.004 27.296  1.00 48.28 ? 2   ILE B CB  1 
ATOM   3689 C  CG1 . ILE B 1 2   ? -30.682 -59.497 26.320  1.00 48.07 ? 2   ILE B CG1 1 
ATOM   3690 C  CG2 . ILE B 1 2   ? -30.149 -57.943 28.247  1.00 49.51 ? 2   ILE B CG2 1 
ATOM   3691 C  CD1 . ILE B 1 2   ? -30.979 -58.551 25.180  1.00 46.91 ? 2   ILE B CD1 1 
ATOM   3692 N  N   . LYS B 1 3   ? -26.655 -56.900 27.380  1.00 51.16 ? 3   LYS B N   1 
ATOM   3693 C  CA  . LYS B 1 3   ? -25.567 -56.318 28.227  1.00 49.96 ? 3   LYS B CA  1 
ATOM   3694 C  C   . LYS B 1 3   ? -26.125 -55.189 29.105  1.00 45.46 ? 3   LYS B C   1 
ATOM   3695 O  O   . LYS B 1 3   ? -27.198 -54.615 28.790  1.00 42.56 ? 3   LYS B O   1 
ATOM   3696 C  CB  . LYS B 1 3   ? -24.393 -55.825 27.372  1.00 49.53 ? 3   LYS B CB  1 
ATOM   3697 C  CG  . LYS B 1 3   ? -23.412 -56.924 26.974  1.00 56.27 ? 3   LYS B CG  1 
ATOM   3698 C  CD  . LYS B 1 3   ? -22.784 -56.772 25.598  1.00 57.58 ? 3   LYS B CD  1 
ATOM   3699 C  CE  . LYS B 1 3   ? -21.478 -56.006 25.621  1.00 60.47 ? 3   LYS B CE  1 
ATOM   3700 N  NZ  . LYS B 1 3   ? -21.189 -55.379 24.308  1.00 62.49 ? 3   LYS B NZ  1 
ATOM   3701 N  N   . GLU B 1 4   ? -25.442 -54.926 30.213  1.00 44.69 ? 4   GLU B N   1 
ATOM   3702 C  CA  . GLU B 1 4   ? -25.729 -53.773 31.099  1.00 43.63 ? 4   GLU B CA  1 
ATOM   3703 C  C   . GLU B 1 4   ? -25.059 -52.563 30.452  1.00 39.44 ? 4   GLU B C   1 
ATOM   3704 O  O   . GLU B 1 4   ? -23.941 -52.706 29.913  1.00 33.11 ? 4   GLU B O   1 
ATOM   3705 C  CB  . GLU B 1 4   ? -25.215 -54.024 32.521  1.00 47.65 ? 4   GLU B CB  1 
ATOM   3706 C  CG  . GLU B 1 4   ? -25.998 -53.274 33.592  1.00 55.76 ? 4   GLU B CG  1 
ATOM   3707 C  CD  . GLU B 1 4   ? -25.270 -53.099 34.922  1.00 58.55 ? 4   GLU B CD  1 
ATOM   3708 O  OE1 . GLU B 1 4   ? -24.608 -54.065 35.360  1.00 56.46 ? 4   GLU B OE1 1 
ATOM   3709 O  OE2 . GLU B 1 4   ? -25.354 -51.988 35.514  1.00 59.47 ? 4   GLU B OE2 1 
ATOM   3710 N  N   . MET B 1 5   ? -25.708 -51.409 30.532  1.00 38.33 ? 5   MET B N   1 
ATOM   3711 C  CA  . MET B 1 5   ? -25.170 -50.145 29.980  1.00 35.89 ? 5   MET B CA  1 
ATOM   3712 C  C   . MET B 1 5   ? -24.091 -49.592 30.910  1.00 32.45 ? 5   MET B C   1 
ATOM   3713 O  O   . MET B 1 5   ? -24.355 -49.367 32.085  1.00 39.10 ? 5   MET B O   1 
ATOM   3714 C  CB  . MET B 1 5   ? -26.304 -49.130 29.854  1.00 35.64 ? 5   MET B CB  1 
ATOM   3715 C  CG  . MET B 1 5   ? -26.087 -48.174 28.728  1.00 35.55 ? 5   MET B CG  1 
ATOM   3716 S  SD  . MET B 1 5   ? -27.582 -47.243 28.396  1.00 36.84 ? 5   MET B SD  1 
ATOM   3717 C  CE  . MET B 1 5   ? -28.327 -48.251 27.118  1.00 37.49 ? 5   MET B CE  1 
ATOM   3718 N  N   . PRO B 1 6   ? -22.864 -49.284 30.432  1.00 27.01 ? 6   PRO B N   1 
ATOM   3719 C  CA  . PRO B 1 6   ? -21.888 -48.598 31.273  1.00 25.26 ? 6   PRO B CA  1 
ATOM   3720 C  C   . PRO B 1 6   ? -22.478 -47.334 31.904  1.00 25.85 ? 6   PRO B C   1 
ATOM   3721 O  O   . PRO B 1 6   ? -23.397 -46.769 31.368  1.00 26.37 ? 6   PRO B O   1 
ATOM   3722 C  CB  . PRO B 1 6   ? -20.740 -48.211 30.332  1.00 25.63 ? 6   PRO B CB  1 
ATOM   3723 C  CG  . PRO B 1 6   ? -20.911 -49.116 29.106  1.00 24.63 ? 6   PRO B CG  1 
ATOM   3724 C  CD  . PRO B 1 6   ? -22.368 -49.532 29.067  1.00 25.68 ? 6   PRO B CD  1 
ATOM   3725 N  N   . GLN B 1 7   ? -21.937 -46.922 33.042  1.00 25.95 ? 7   GLN B N   1 
ATOM   3726 C  CA  . GLN B 1 7   ? -22.333 -45.663 33.712  1.00 25.89 ? 7   GLN B CA  1 
ATOM   3727 C  C   . GLN B 1 7   ? -21.057 -44.999 34.200  1.00 26.54 ? 7   GLN B C   1 
ATOM   3728 O  O   . GLN B 1 7   ? -20.163 -45.688 34.668  1.00 27.31 ? 7   GLN B O   1 
ATOM   3729 C  CB  . GLN B 1 7   ? -23.320 -45.992 34.821  1.00 26.89 ? 7   GLN B CB  1 
ATOM   3730 C  CG  . GLN B 1 7   ? -24.061 -44.787 35.356  1.00 27.78 ? 7   GLN B CG  1 
ATOM   3731 C  CD  . GLN B 1 7   ? -24.914 -45.159 36.539  1.00 27.45 ? 7   GLN B CD  1 
ATOM   3732 O  OE1 . GLN B 1 7   ? -24.751 -46.206 37.154  1.00 30.79 ? 7   GLN B OE1 1 
ATOM   3733 N  NE2 . GLN B 1 7   ? -25.815 -44.273 36.894  1.00 29.49 ? 7   GLN B NE2 1 
ATOM   3734 N  N   . PRO B 1 8   ? -20.879 -43.663 34.062  1.00 27.57 ? 8   PRO B N   1 
ATOM   3735 C  CA  . PRO B 1 8   ? -19.664 -43.020 34.543  1.00 27.05 ? 8   PRO B CA  1 
ATOM   3736 C  C   . PRO B 1 8   ? -19.673 -42.999 36.080  1.00 25.79 ? 8   PRO B C   1 
ATOM   3737 O  O   . PRO B 1 8   ? -20.637 -43.492 36.663  1.00 27.02 ? 8   PRO B O   1 
ATOM   3738 C  CB  . PRO B 1 8   ? -19.694 -41.608 33.921  1.00 26.75 ? 8   PRO B CB  1 
ATOM   3739 C  CG  . PRO B 1 8   ? -21.025 -41.457 33.223  1.00 25.34 ? 8   PRO B CG  1 
ATOM   3740 C  CD  . PRO B 1 8   ? -21.838 -42.696 33.522  1.00 26.60 ? 8   PRO B CD  1 
ATOM   3741 N  N   . LYS B 1 9   ? -18.632 -42.411 36.682  1.00 26.36 ? 9   LYS B N   1 
ATOM   3742 C  CA  . LYS B 1 9   ? -18.475 -42.254 38.154  1.00 26.01 ? 9   LYS B CA  1 
ATOM   3743 C  C   . LYS B 1 9   ? -19.733 -41.590 38.736  1.00 24.09 ? 9   LYS B C   1 
ATOM   3744 O  O   . LYS B 1 9   ? -20.219 -40.615 38.152  1.00 21.86 ? 9   LYS B O   1 
ATOM   3745 C  CB  . LYS B 1 9   ? -17.189 -41.502 38.553  1.00 28.50 ? 9   LYS B CB  1 
ATOM   3746 C  CG  . LYS B 1 9   ? -16.693 -40.343 37.679  1.00 30.24 ? 9   LYS B CG  1 
ATOM   3747 C  CD  . LYS B 1 9   ? -15.355 -39.688 38.134  1.00 31.77 ? 9   LYS B CD  1 
ATOM   3748 C  CE  . LYS B 1 9   ? -15.460 -38.219 38.541  1.00 36.03 ? 9   LYS B CE  1 
ATOM   3749 N  NZ  . LYS B 1 9   ? -14.312 -37.670 39.338  1.00 34.75 ? 9   LYS B NZ  1 
ATOM   3750 N  N   . THR B 1 10  ? -20.231 -42.119 39.855  1.00 21.45 ? 10  THR B N   1 
ATOM   3751 C  CA  . THR B 1 10  ? -21.370 -41.561 40.631  1.00 21.31 ? 10  THR B CA  1 
ATOM   3752 C  C   . THR B 1 10  ? -20.903 -40.854 41.917  1.00 21.44 ? 10  THR B C   1 
ATOM   3753 O  O   . THR B 1 10  ? -19.787 -41.144 42.409  1.00 22.51 ? 10  THR B O   1 
ATOM   3754 C  CB  . THR B 1 10  ? -22.375 -42.654 41.000  1.00 19.81 ? 10  THR B CB  1 
ATOM   3755 O  OG1 . THR B 1 10  ? -21.657 -43.662 41.717  1.00 18.51 ? 10  THR B OG1 1 
ATOM   3756 C  CG2 . THR B 1 10  ? -23.046 -43.222 39.782  1.00 19.71 ? 10  THR B CG2 1 
ATOM   3757 N  N   . PHE B 1 11  ? -21.780 -39.991 42.444  1.00 21.77 ? 11  PHE B N   1 
ATOM   3758 C  CA  . PHE B 1 11  ? -21.575 -39.067 43.591  1.00 22.10 ? 11  PHE B CA  1 
ATOM   3759 C  C   . PHE B 1 11  ? -22.749 -39.229 44.571  1.00 23.59 ? 11  PHE B C   1 
ATOM   3760 O  O   . PHE B 1 11  ? -23.469 -38.261 44.844  1.00 22.76 ? 11  PHE B O   1 
ATOM   3761 C  CB  . PHE B 1 11  ? -21.508 -37.610 43.123  1.00 20.06 ? 11  PHE B CB  1 
ATOM   3762 C  CG  . PHE B 1 11  ? -20.392 -37.276 42.172  1.00 18.54 ? 11  PHE B CG  1 
ATOM   3763 C  CD1 . PHE B 1 11  ? -20.444 -37.700 40.862  1.00 17.48 ? 11  PHE B CD1 1 
ATOM   3764 C  CD2 . PHE B 1 11  ? -19.359 -36.425 42.563  1.00 18.37 ? 11  PHE B CD2 1 
ATOM   3765 C  CE1 . PHE B 1 11  ? -19.428 -37.359 39.985  1.00 18.57 ? 11  PHE B CE1 1 
ATOM   3766 C  CE2 . PHE B 1 11  ? -18.345 -36.078 41.688  1.00 17.38 ? 11  PHE B CE2 1 
ATOM   3767 C  CZ  . PHE B 1 11  ? -18.369 -36.568 40.400  1.00 18.43 ? 11  PHE B CZ  1 
ATOM   3768 N  N   . GLY B 1 12  ? -22.943 -40.441 45.087  1.00 26.38 ? 12  GLY B N   1 
ATOM   3769 C  CA  . GLY B 1 12  ? -24.009 -40.722 46.059  1.00 26.60 ? 12  GLY B CA  1 
ATOM   3770 C  C   . GLY B 1 12  ? -25.340 -40.324 45.462  1.00 28.78 ? 12  GLY B C   1 
ATOM   3771 O  O   . GLY B 1 12  ? -25.601 -40.714 44.284  1.00 27.78 ? 12  GLY B O   1 
ATOM   3772 N  N   . GLU B 1 13  ? -26.109 -39.524 46.206  1.00 28.29 ? 13  GLU B N   1 
ATOM   3773 C  CA  . GLU B 1 13  ? -27.520 -39.211 45.886  1.00 31.13 ? 13  GLU B CA  1 
ATOM   3774 C  C   . GLU B 1 13  ? -27.582 -38.360 44.608  1.00 30.57 ? 13  GLU B C   1 
ATOM   3775 O  O   . GLU B 1 13  ? -28.614 -38.437 43.941  1.00 31.99 ? 13  GLU B O   1 
ATOM   3776 C  CB  . GLU B 1 13  ? -28.236 -38.590 47.089  1.00 35.60 ? 13  GLU B CB  1 
ATOM   3777 C  CG  . GLU B 1 13  ? -27.606 -37.309 47.611  1.00 42.62 ? 13  GLU B CG  1 
ATOM   3778 C  CD  . GLU B 1 13  ? -26.329 -37.481 48.429  1.00 49.74 ? 13  GLU B CD  1 
ATOM   3779 O  OE1 . GLU B 1 13  ? -25.831 -38.648 48.551  1.00 47.52 ? 13  GLU B OE1 1 
ATOM   3780 O  OE2 . GLU B 1 13  ? -25.812 -36.441 48.933  1.00 56.34 ? 13  GLU B OE2 1 
ATOM   3781 N  N   . LEU B 1 14  ? -26.511 -37.646 44.226  1.00 30.85 ? 14  LEU B N   1 
ATOM   3782 C  CA  . LEU B 1 14  ? -26.465 -36.793 42.996  1.00 28.56 ? 14  LEU B CA  1 
ATOM   3783 C  C   . LEU B 1 14  ? -26.117 -37.640 41.757  1.00 27.64 ? 14  LEU B C   1 
ATOM   3784 O  O   . LEU B 1 14  ? -26.116 -37.104 40.651  1.00 25.34 ? 14  LEU B O   1 
ATOM   3785 C  CB  . LEU B 1 14  ? -25.468 -35.642 43.196  1.00 27.91 ? 14  LEU B CB  1 
ATOM   3786 C  CG  . LEU B 1 14  ? -25.790 -34.688 44.351  1.00 28.43 ? 14  LEU B CG  1 
ATOM   3787 C  CD1 . LEU B 1 14  ? -24.674 -33.670 44.564  1.00 26.39 ? 14  LEU B CD1 1 
ATOM   3788 C  CD2 . LEU B 1 14  ? -27.127 -33.993 44.114  1.00 28.86 ? 14  LEU B CD2 1 
ATOM   3789 N  N   . LYS B 1 15  ? -25.851 -38.929 41.908  1.00 28.27 ? 15  LYS B N   1 
ATOM   3790 C  CA  . LYS B 1 15  ? -25.694 -39.831 40.732  1.00 29.15 ? 15  LYS B CA  1 
ATOM   3791 C  C   . LYS B 1 15  ? -24.593 -39.242 39.831  1.00 26.26 ? 15  LYS B C   1 
ATOM   3792 O  O   . LYS B 1 15  ? -23.514 -38.964 40.373  1.00 24.77 ? 15  LYS B O   1 
ATOM   3793 C  CB  . LYS B 1 15  ? -27.088 -40.054 40.131  1.00 29.88 ? 15  LYS B CB  1 
ATOM   3794 C  CG  . LYS B 1 15  ? -28.095 -40.591 41.146  1.00 33.38 ? 15  LYS B CG  1 
ATOM   3795 C  CD  . LYS B 1 15  ? -29.442 -40.978 40.575  1.00 39.42 ? 15  LYS B CD  1 
ATOM   3796 C  CE  . LYS B 1 15  ? -30.268 -41.904 41.451  1.00 43.30 ? 15  LYS B CE  1 
ATOM   3797 N  NZ  . LYS B 1 15  ? -30.901 -43.002 40.662  1.00 43.92 ? 15  LYS B NZ  1 
ATOM   3798 N  N   . ASN B 1 16  ? -24.828 -39.033 38.530  1.00 24.32 ? 16  ASN B N   1 
ATOM   3799 C  CA  . ASN B 1 16  ? -23.782 -38.538 37.588  1.00 23.23 ? 16  ASN B CA  1 
ATOM   3800 C  C   . ASN B 1 16  ? -23.753 -36.992 37.533  1.00 23.53 ? 16  ASN B C   1 
ATOM   3801 O  O   . ASN B 1 16  ? -22.765 -36.444 37.024  1.00 22.81 ? 16  ASN B O   1 
ATOM   3802 C  CB  . ASN B 1 16  ? -23.936 -39.157 36.187  1.00 22.43 ? 16  ASN B CB  1 
ATOM   3803 C  CG  . ASN B 1 16  ? -23.815 -40.670 36.173  1.00 22.53 ? 16  ASN B CG  1 
ATOM   3804 O  OD1 . ASN B 1 16  ? -24.730 -41.376 35.743  1.00 23.22 ? 16  ASN B OD1 1 
ATOM   3805 N  ND2 . ASN B 1 16  ? -22.696 -41.196 36.650  1.00 23.34 ? 16  ASN B ND2 1 
ATOM   3806 N  N   . LEU B 1 17  ? -24.763 -36.287 38.068  1.00 24.21 ? 17  LEU B N   1 
ATOM   3807 C  CA  . LEU B 1 17  ? -25.037 -34.841 37.776  1.00 22.76 ? 17  LEU B CA  1 
ATOM   3808 C  C   . LEU B 1 17  ? -23.777 -33.980 37.934  1.00 24.44 ? 17  LEU B C   1 
ATOM   3809 O  O   . LEU B 1 17  ? -23.567 -33.044 37.162  1.00 30.16 ? 17  LEU B O   1 
ATOM   3810 C  CB  . LEU B 1 17  ? -26.180 -34.345 38.682  1.00 21.65 ? 17  LEU B CB  1 
ATOM   3811 C  CG  . LEU B 1 17  ? -26.845 -33.041 38.234  1.00 20.47 ? 17  LEU B CG  1 
ATOM   3812 C  CD1 . LEU B 1 17  ? -27.210 -33.079 36.763  1.00 20.00 ? 17  LEU B CD1 1 
ATOM   3813 C  CD2 . LEU B 1 17  ? -28.068 -32.735 39.045  1.00 20.36 ? 17  LEU B CD2 1 
ATOM   3814 N  N   . PRO B 1 18  ? -22.936 -34.176 38.977  1.00 22.42 ? 18  PRO B N   1 
ATOM   3815 C  CA  . PRO B 1 18  ? -21.794 -33.302 39.203  1.00 22.18 ? 18  PRO B CA  1 
ATOM   3816 C  C   . PRO B 1 18  ? -20.796 -33.368 38.057  1.00 23.13 ? 18  PRO B C   1 
ATOM   3817 O  O   . PRO B 1 18  ? -20.059 -32.409 37.877  1.00 21.16 ? 18  PRO B O   1 
ATOM   3818 C  CB  . PRO B 1 18  ? -21.168 -33.846 40.491  1.00 21.78 ? 18  PRO B CB  1 
ATOM   3819 C  CG  . PRO B 1 18  ? -22.355 -34.434 41.211  1.00 22.32 ? 18  PRO B CG  1 
ATOM   3820 C  CD  . PRO B 1 18  ? -23.114 -35.117 40.092  1.00 22.84 ? 18  PRO B CD  1 
ATOM   3821 N  N   . LEU B 1 19  ? -20.768 -34.486 37.327  1.00 24.08 ? 19  LEU B N   1 
ATOM   3822 C  CA  . LEU B 1 19  ? -19.879 -34.598 36.140  1.00 22.79 ? 19  LEU B CA  1 
ATOM   3823 C  C   . LEU B 1 19  ? -20.188 -33.430 35.206  1.00 24.53 ? 19  LEU B C   1 
ATOM   3824 O  O   . LEU B 1 19  ? -19.296 -33.065 34.452  1.00 31.08 ? 19  LEU B O   1 
ATOM   3825 C  CB  . LEU B 1 19  ? -20.079 -35.936 35.425  1.00 21.76 ? 19  LEU B CB  1 
ATOM   3826 C  CG  . LEU B 1 19  ? -19.585 -37.171 36.176  1.00 21.28 ? 19  LEU B CG  1 
ATOM   3827 C  CD1 . LEU B 1 19  ? -19.923 -38.433 35.411  1.00 21.47 ? 19  LEU B CD1 1 
ATOM   3828 C  CD2 . LEU B 1 19  ? -18.079 -37.105 36.421  1.00 22.12 ? 19  LEU B CD2 1 
ATOM   3829 N  N   . LEU B 1 20  ? -21.402 -32.868 35.221  1.00 24.12 ? 20  LEU B N   1 
ATOM   3830 C  CA  . LEU B 1 20  ? -21.773 -31.805 34.239  1.00 25.48 ? 20  LEU B CA  1 
ATOM   3831 C  C   . LEU B 1 20  ? -21.757 -30.422 34.896  1.00 24.93 ? 20  LEU B C   1 
ATOM   3832 O  O   . LEU B 1 20  ? -22.206 -29.436 34.271  1.00 27.64 ? 20  LEU B O   1 
ATOM   3833 C  CB  . LEU B 1 20  ? -23.112 -32.167 33.600  1.00 25.43 ? 20  LEU B CB  1 
ATOM   3834 C  CG  . LEU B 1 20  ? -22.995 -33.091 32.382  1.00 25.38 ? 20  LEU B CG  1 
ATOM   3835 C  CD1 . LEU B 1 20  ? -21.871 -34.099 32.508  1.00 26.17 ? 20  LEU B CD1 1 
ATOM   3836 C  CD2 . LEU B 1 20  ? -24.295 -33.818 32.107  1.00 24.91 ? 20  LEU B CD2 1 
ATOM   3837 N  N   . ASN B 1 21  ? -21.129 -30.335 36.062  1.00 25.63 ? 21  ASN B N   1 
ATOM   3838 C  CA  . ASN B 1 21  ? -20.940 -29.074 36.828  1.00 24.83 ? 21  ASN B CA  1 
ATOM   3839 C  C   . ASN B 1 21  ? -19.684 -28.371 36.293  1.00 25.30 ? 21  ASN B C   1 
ATOM   3840 O  O   . ASN B 1 21  ? -18.620 -28.429 36.940  1.00 22.71 ? 21  ASN B O   1 
ATOM   3841 C  CB  . ASN B 1 21  ? -20.924 -29.358 38.324  1.00 24.19 ? 21  ASN B CB  1 
ATOM   3842 C  CG  . ASN B 1 21  ? -20.967 -28.090 39.127  1.00 25.21 ? 21  ASN B CG  1 
ATOM   3843 O  OD1 . ASN B 1 21  ? -21.307 -27.025 38.610  1.00 25.94 ? 21  ASN B OD1 1 
ATOM   3844 N  ND2 . ASN B 1 21  ? -20.625 -28.203 40.388  1.00 25.54 ? 21  ASN B ND2 1 
ATOM   3845 N  N   . THR B 1 22  ? -19.830 -27.755 35.117  1.00 25.56 ? 22  THR B N   1 
ATOM   3846 C  CA  . THR B 1 22  ? -18.742 -27.166 34.303  1.00 26.63 ? 22  THR B CA  1 
ATOM   3847 C  C   . THR B 1 22  ? -19.399 -26.176 33.339  1.00 26.37 ? 22  THR B C   1 
ATOM   3848 O  O   . THR B 1 22  ? -20.629 -26.315 33.093  1.00 30.12 ? 22  THR B O   1 
ATOM   3849 C  CB  . THR B 1 22  ? -17.952 -28.283 33.608  1.00 28.36 ? 22  THR B CB  1 
ATOM   3850 O  OG1 . THR B 1 22  ? -17.066 -27.712 32.648  1.00 27.93 ? 22  THR B OG1 1 
ATOM   3851 C  CG2 . THR B 1 22  ? -18.853 -29.267 32.895  1.00 31.31 ? 22  THR B CG2 1 
ATOM   3852 N  N   . ASP B 1 23  ? -18.646 -25.216 32.799  1.00 24.48 ? 23  ASP B N   1 
ATOM   3853 C  CA  . ASP B 1 23  ? -19.175 -24.316 31.736  1.00 22.69 ? 23  ASP B CA  1 
ATOM   3854 C  C   . ASP B 1 23  ? -18.799 -24.900 30.378  1.00 21.40 ? 23  ASP B C   1 
ATOM   3855 O  O   . ASP B 1 23  ? -18.896 -24.161 29.402  1.00 23.72 ? 23  ASP B O   1 
ATOM   3856 C  CB  . ASP B 1 23  ? -18.730 -22.868 31.918  1.00 21.61 ? 23  ASP B CB  1 
ATOM   3857 C  CG  . ASP B 1 23  ? -17.245 -22.662 31.738  1.00 22.57 ? 23  ASP B CG  1 
ATOM   3858 O  OD1 . ASP B 1 23  ? -16.513 -23.651 31.581  1.00 21.80 ? 23  ASP B OD1 1 
ATOM   3859 O  OD2 . ASP B 1 23  ? -16.831 -21.501 31.755  1.00 27.65 ? 23  ASP B OD2 1 
ATOM   3860 N  N   . LYS B 1 24  ? -18.413 -26.181 30.323  1.00 21.36 ? 24  LYS B N   1 
ATOM   3861 C  CA  . LYS B 1 24  ? -18.134 -26.917 29.056  1.00 21.68 ? 24  LYS B CA  1 
ATOM   3862 C  C   . LYS B 1 24  ? -18.731 -28.327 29.120  1.00 21.53 ? 24  LYS B C   1 
ATOM   3863 O  O   . LYS B 1 24  ? -17.969 -29.318 29.098  1.00 21.71 ? 24  LYS B O   1 
ATOM   3864 C  CB  . LYS B 1 24  ? -16.633 -26.967 28.789  1.00 21.38 ? 24  LYS B CB  1 
ATOM   3865 C  CG  . LYS B 1 24  ? -16.079 -25.639 28.325  1.00 21.67 ? 24  LYS B CG  1 
ATOM   3866 C  CD  . LYS B 1 24  ? -14.583 -25.593 28.318  1.00 21.70 ? 24  LYS B CD  1 
ATOM   3867 C  CE  . LYS B 1 24  ? -14.097 -24.195 28.023  1.00 22.92 ? 24  LYS B CE  1 
ATOM   3868 N  NZ  . LYS B 1 24  ? -12.664 -24.190 27.646  1.00 24.06 ? 24  LYS B NZ  1 
ATOM   3869 N  N   . VAL B 1 25  ? -20.063 -28.399 29.146  1.00 21.87 ? 25  VAL B N   1 
ATOM   3870 C  CA  . VAL B 1 25  ? -20.842 -29.655 29.361  1.00 20.93 ? 25  VAL B CA  1 
ATOM   3871 C  C   . VAL B 1 25  ? -20.566 -30.628 28.216  1.00 19.56 ? 25  VAL B C   1 
ATOM   3872 O  O   . VAL B 1 25  ? -20.285 -31.813 28.494  1.00 20.77 ? 25  VAL B O   1 
ATOM   3873 C  CB  . VAL B 1 25  ? -22.340 -29.349 29.509  1.00 22.62 ? 25  VAL B CB  1 
ATOM   3874 C  CG1 . VAL B 1 25  ? -23.156 -30.623 29.568  1.00 25.48 ? 25  VAL B CG1 1 
ATOM   3875 C  CG2 . VAL B 1 25  ? -22.623 -28.494 30.742  1.00 22.63 ? 25  VAL B CG2 1 
ATOM   3876 N  N   . VAL B 1 26  ? -20.615 -30.152 26.975  1.00 17.54 ? 26  VAL B N   1 
ATOM   3877 C  CA  . VAL B 1 26  ? -20.412 -31.019 25.779  1.00 18.62 ? 26  VAL B CA  1 
ATOM   3878 C  C   . VAL B 1 26  ? -19.023 -31.642 25.832  1.00 19.73 ? 26  VAL B C   1 
ATOM   3879 O  O   . VAL B 1 26  ? -18.915 -32.845 25.517  1.00 20.70 ? 26  VAL B O   1 
ATOM   3880 C  CB  . VAL B 1 26  ? -20.598 -30.277 24.450  1.00 17.24 ? 26  VAL B CB  1 
ATOM   3881 C  CG1 . VAL B 1 26  ? -20.155 -31.135 23.287  1.00 16.86 ? 26  VAL B CG1 1 
ATOM   3882 C  CG2 . VAL B 1 26  ? -22.031 -29.843 24.290  1.00 17.39 ? 26  VAL B CG2 1 
ATOM   3883 N  N   . GLN B 1 27  ? -18.002 -30.856 26.175  1.00 21.59 ? 27  GLN B N   1 
ATOM   3884 C  CA  . GLN B 1 27  ? -16.601 -31.353 26.204  1.00 22.55 ? 27  GLN B CA  1 
ATOM   3885 C  C   . GLN B 1 27  ? -16.430 -32.303 27.395  1.00 21.48 ? 27  GLN B C   1 
ATOM   3886 O  O   . GLN B 1 27  ? -15.666 -33.258 27.268  1.00 24.80 ? 27  GLN B O   1 
ATOM   3887 C  CB  . GLN B 1 27  ? -15.631 -30.170 26.182  1.00 24.90 ? 27  GLN B CB  1 
ATOM   3888 C  CG  . GLN B 1 27  ? -15.651 -29.439 24.837  1.00 24.79 ? 27  GLN B CG  1 
ATOM   3889 C  CD  . GLN B 1 27  ? -15.052 -28.067 24.931  1.00 23.42 ? 27  GLN B CD  1 
ATOM   3890 O  OE1 . GLN B 1 27  ? -13.835 -27.912 24.864  1.00 24.40 ? 27  GLN B OE1 1 
ATOM   3891 N  NE2 . GLN B 1 27  ? -15.901 -27.073 25.134  1.00 22.29 ? 27  GLN B NE2 1 
ATOM   3892 N  N   . ALA B 1 28  ? -17.147 -32.099 28.495  1.00 19.67 ? 28  ALA B N   1 
ATOM   3893 C  CA  . ALA B 1 28  ? -17.133 -33.066 29.610  1.00 18.24 ? 28  ALA B CA  1 
ATOM   3894 C  C   . ALA B 1 28  ? -17.800 -34.349 29.114  1.00 18.84 ? 28  ALA B C   1 
ATOM   3895 O  O   . ALA B 1 28  ? -17.235 -35.422 29.336  1.00 20.06 ? 28  ALA B O   1 
ATOM   3896 C  CB  . ALA B 1 28  ? -17.800 -32.497 30.822  1.00 17.82 ? 28  ALA B CB  1 
ATOM   3897 N  N   . LEU B 1 29  ? -18.909 -34.257 28.380  1.00 18.39 ? 29  LEU B N   1 
ATOM   3898 C  CA  . LEU B 1 29  ? -19.577 -35.475 27.862  1.00 19.18 ? 29  LEU B CA  1 
ATOM   3899 C  C   . LEU B 1 29  ? -18.633 -36.209 26.886  1.00 20.05 ? 29  LEU B C   1 
ATOM   3900 O  O   . LEU B 1 29  ? -18.590 -37.463 26.895  1.00 21.35 ? 29  LEU B O   1 
ATOM   3901 C  CB  . LEU B 1 29  ? -20.953 -35.100 27.290  1.00 18.78 ? 29  LEU B CB  1 
ATOM   3902 C  CG  . LEU B 1 29  ? -22.018 -34.871 28.369  1.00 18.74 ? 29  LEU B CG  1 
ATOM   3903 C  CD1 . LEU B 1 29  ? -23.213 -34.077 27.846  1.00 19.16 ? 29  LEU B CD1 1 
ATOM   3904 C  CD2 . LEU B 1 29  ? -22.457 -36.179 29.022  1.00 17.37 ? 29  LEU B CD2 1 
ATOM   3905 N  N   . MET B 1 30  ? -17.812 -35.495 26.132  1.00 20.45 ? 30  MET B N   1 
ATOM   3906 C  CA  . MET B 1 30  ? -16.869 -36.141 25.177  1.00 22.86 ? 30  MET B CA  1 
ATOM   3907 C  C   . MET B 1 30  ? -15.763 -36.923 25.923  1.00 24.31 ? 30  MET B C   1 
ATOM   3908 O  O   . MET B 1 30  ? -15.380 -38.040 25.419  1.00 21.71 ? 30  MET B O   1 
ATOM   3909 C  CB  . MET B 1 30  ? -16.238 -35.094 24.252  1.00 22.07 ? 30  MET B CB  1 
ATOM   3910 C  CG  . MET B 1 30  ? -17.236 -34.507 23.284  1.00 22.45 ? 30  MET B CG  1 
ATOM   3911 S  SD  . MET B 1 30  ? -16.566 -33.165 22.309  1.00 23.05 ? 30  MET B SD  1 
ATOM   3912 C  CE  . MET B 1 30  ? -15.332 -34.027 21.332  1.00 21.21 ? 30  MET B CE  1 
ATOM   3913 N  N   . LYS B 1 31  ? -15.217 -36.374 27.026  1.00 24.61 ? 31  LYS B N   1 
ATOM   3914 C  CA  . LYS B 1 31  ? -14.196 -37.088 27.844  1.00 26.88 ? 31  LYS B CA  1 
ATOM   3915 C  C   . LYS B 1 31  ? -14.831 -38.369 28.414  1.00 24.65 ? 31  LYS B C   1 
ATOM   3916 O  O   . LYS B 1 31  ? -14.194 -39.414 28.273  1.00 23.21 ? 31  LYS B O   1 
ATOM   3917 C  CB  . LYS B 1 31  ? -13.540 -36.154 28.864  1.00 30.27 ? 31  LYS B CB  1 
ATOM   3918 C  CG  . LYS B 1 31  ? -12.715 -35.044 28.212  1.00 38.07 ? 31  LYS B CG  1 
ATOM   3919 C  CD  . LYS B 1 31  ? -12.047 -34.051 29.171  1.00 44.82 ? 31  LYS B CD  1 
ATOM   3920 C  CE  . LYS B 1 31  ? -12.950 -33.540 30.283  1.00 51.10 ? 31  LYS B CE  1 
ATOM   3921 N  NZ  . LYS B 1 31  ? -12.271 -32.535 31.137  1.00 54.41 ? 31  LYS B NZ  1 
ATOM   3922 N  N   . ILE B 1 32  ? -16.083 -38.331 28.902  1.00 25.10 ? 32  ILE B N   1 
ATOM   3923 C  CA  . ILE B 1 32  ? -16.791 -39.533 29.449  1.00 25.85 ? 32  ILE B CA  1 
ATOM   3924 C  C   . ILE B 1 32  ? -16.961 -40.563 28.332  1.00 25.75 ? 32  ILE B C   1 
ATOM   3925 O  O   . ILE B 1 32  ? -16.863 -41.779 28.603  1.00 27.31 ? 32  ILE B O   1 
ATOM   3926 C  CB  . ILE B 1 32  ? -18.156 -39.194 30.075  1.00 27.11 ? 32  ILE B CB  1 
ATOM   3927 C  CG1 . ILE B 1 32  ? -18.047 -38.256 31.282  1.00 25.37 ? 32  ILE B CG1 1 
ATOM   3928 C  CG2 . ILE B 1 32  ? -18.870 -40.488 30.438  1.00 28.83 ? 32  ILE B CG2 1 
ATOM   3929 C  CD1 . ILE B 1 32  ? -19.341 -37.600 31.654  1.00 25.19 ? 32  ILE B CD1 1 
ATOM   3930 N  N   . ALA B 1 33  ? -17.239 -40.101 27.119  1.00 25.60 ? 33  ALA B N   1 
ATOM   3931 C  CA  . ALA B 1 33  ? -17.437 -40.990 25.956  1.00 25.32 ? 33  ALA B CA  1 
ATOM   3932 C  C   . ALA B 1 33  ? -16.083 -41.602 25.589  1.00 25.54 ? 33  ALA B C   1 
ATOM   3933 O  O   . ALA B 1 33  ? -16.056 -42.781 25.257  1.00 24.51 ? 33  ALA B O   1 
ATOM   3934 C  CB  . ALA B 1 33  ? -18.061 -40.227 24.820  1.00 25.98 ? 33  ALA B CB  1 
ATOM   3935 N  N   . ASP B 1 34  ? -14.996 -40.834 25.693  1.00 28.29 ? 34  ASP B N   1 
ATOM   3936 C  CA  . ASP B 1 34  ? -13.617 -41.330 25.437  1.00 30.14 ? 34  ASP B CA  1 
ATOM   3937 C  C   . ASP B 1 34  ? -13.309 -42.474 26.405  1.00 29.98 ? 34  ASP B C   1 
ATOM   3938 O  O   . ASP B 1 34  ? -12.624 -43.427 25.981  1.00 29.01 ? 34  ASP B O   1 
ATOM   3939 C  CB  . ASP B 1 34  ? -12.565 -40.229 25.577  1.00 34.25 ? 34  ASP B CB  1 
ATOM   3940 C  CG  . ASP B 1 34  ? -12.247 -39.490 24.293  1.00 42.03 ? 34  ASP B CG  1 
ATOM   3941 O  OD1 . ASP B 1 34  ? -12.760 -39.903 23.215  1.00 43.56 ? 34  ASP B OD1 1 
ATOM   3942 O  OD2 . ASP B 1 34  ? -11.481 -38.496 24.383  1.00 52.20 ? 34  ASP B OD2 1 
ATOM   3943 N  N   . GLU B 1 35  ? -13.830 -42.389 27.634  1.00 31.02 ? 35  GLU B N   1 
ATOM   3944 C  CA  . GLU B 1 35  ? -13.554 -43.348 28.735  1.00 31.94 ? 35  GLU B CA  1 
ATOM   3945 C  C   . GLU B 1 35  ? -14.525 -44.536 28.702  1.00 30.71 ? 35  GLU B C   1 
ATOM   3946 O  O   . GLU B 1 35  ? -14.023 -45.668 28.857  1.00 31.32 ? 35  GLU B O   1 
ATOM   3947 C  CB  . GLU B 1 35  ? -13.536 -42.588 30.059  1.00 34.26 ? 35  GLU B CB  1 
ATOM   3948 C  CG  . GLU B 1 35  ? -12.285 -41.732 30.162  1.00 35.92 ? 35  GLU B CG  1 
ATOM   3949 C  CD  . GLU B 1 35  ? -12.087 -40.953 31.441  1.00 38.51 ? 35  GLU B CD  1 
ATOM   3950 O  OE1 . GLU B 1 35  ? -13.021 -40.887 32.272  1.00 40.24 ? 35  GLU B OE1 1 
ATOM   3951 O  OE2 . GLU B 1 35  ? -10.986 -40.405 31.590  1.00 42.87 ? 35  GLU B OE2 1 
ATOM   3952 N  N   . LEU B 1 36  ? -15.830 -44.332 28.479  1.00 27.21 ? 36  LEU B N   1 
ATOM   3953 C  CA  . LEU B 1 36  ? -16.831 -45.428 28.646  1.00 27.30 ? 36  LEU B CA  1 
ATOM   3954 C  C   . LEU B 1 36  ? -17.156 -46.119 27.313  1.00 25.20 ? 36  LEU B C   1 
ATOM   3955 O  O   . LEU B 1 36  ? -17.714 -47.209 27.368  1.00 24.77 ? 36  LEU B O   1 
ATOM   3956 C  CB  . LEU B 1 36  ? -18.105 -44.883 29.308  1.00 26.95 ? 36  LEU B CB  1 
ATOM   3957 C  CG  . LEU B 1 36  ? -17.970 -44.455 30.771  1.00 26.52 ? 36  LEU B CG  1 
ATOM   3958 C  CD1 . LEU B 1 36  ? -19.266 -44.644 31.519  1.00 25.05 ? 36  LEU B CD1 1 
ATOM   3959 C  CD2 . LEU B 1 36  ? -16.854 -45.216 31.479  1.00 28.17 ? 36  LEU B CD2 1 
ATOM   3960 N  N   . GLY B 1 37  ? -16.853 -45.508 26.171  1.00 24.82 ? 37  GLY B N   1 
ATOM   3961 C  CA  . GLY B 1 37  ? -17.087 -46.106 24.845  1.00 24.69 ? 37  GLY B CA  1 
ATOM   3962 C  C   . GLY B 1 37  ? -18.374 -45.590 24.214  1.00 26.41 ? 37  GLY B C   1 
ATOM   3963 O  O   . GLY B 1 37  ? -18.806 -44.461 24.536  1.00 28.16 ? 37  GLY B O   1 
ATOM   3964 N  N   . GLU B 1 38  ? -18.987 -46.428 23.381  1.00 23.87 ? 38  GLU B N   1 
ATOM   3965 C  CA  . GLU B 1 38  ? -20.015 -46.070 22.384  1.00 23.59 ? 38  GLU B CA  1 
ATOM   3966 C  C   . GLU B 1 38  ? -21.357 -45.760 23.048  1.00 22.66 ? 38  GLU B C   1 
ATOM   3967 O  O   . GLU B 1 38  ? -22.221 -45.176 22.367  1.00 21.71 ? 38  GLU B O   1 
ATOM   3968 C  CB  . GLU B 1 38  ? -20.184 -47.220 21.384  1.00 25.21 ? 38  GLU B CB  1 
ATOM   3969 C  CG  . GLU B 1 38  ? -20.690 -48.517 21.983  1.00 24.52 ? 38  GLU B CG  1 
ATOM   3970 C  CD  . GLU B 1 38  ? -20.937 -49.579 20.938  1.00 26.31 ? 38  GLU B CD  1 
ATOM   3971 O  OE1 . GLU B 1 38  ? -20.864 -49.261 19.726  1.00 26.44 ? 38  GLU B OE1 1 
ATOM   3972 O  OE2 . GLU B 1 38  ? -21.219 -50.721 21.339  1.00 29.18 ? 38  GLU B OE2 1 
ATOM   3973 N  N   . ILE B 1 39  ? -21.558 -46.185 24.290  1.00 20.02 ? 39  ILE B N   1 
ATOM   3974 C  CA  . ILE B 1 39  ? -22.838 -45.928 24.999  1.00 19.84 ? 39  ILE B CA  1 
ATOM   3975 C  C   . ILE B 1 39  ? -22.583 -45.881 26.505  1.00 18.57 ? 39  ILE B C   1 
ATOM   3976 O  O   . ILE B 1 39  ? -21.915 -46.796 27.051  1.00 17.38 ? 39  ILE B O   1 
ATOM   3977 C  CB  . ILE B 1 39  ? -23.916 -46.970 24.633  1.00 21.23 ? 39  ILE B CB  1 
ATOM   3978 C  CG1 . ILE B 1 39  ? -25.286 -46.580 25.194  1.00 21.35 ? 39  ILE B CG1 1 
ATOM   3979 C  CG2 . ILE B 1 39  ? -23.533 -48.375 25.089  1.00 21.66 ? 39  ILE B CG2 1 
ATOM   3980 C  CD1 . ILE B 1 39  ? -26.455 -47.180 24.449  1.00 21.65 ? 39  ILE B CD1 1 
ATOM   3981 N  N   . PHE B 1 40  ? -23.163 -44.879 27.147  1.00 17.82 ? 40  PHE B N   1 
ATOM   3982 C  CA  . PHE B 1 40  ? -23.255 -44.808 28.622  1.00 18.29 ? 40  PHE B CA  1 
ATOM   3983 C  C   . PHE B 1 40  ? -24.583 -44.162 29.027  1.00 18.69 ? 40  PHE B C   1 
ATOM   3984 O  O   . PHE B 1 40  ? -25.072 -43.190 28.378  1.00 17.73 ? 40  PHE B O   1 
ATOM   3985 C  CB  . PHE B 1 40  ? -22.024 -44.109 29.194  1.00 18.22 ? 40  PHE B CB  1 
ATOM   3986 C  CG  . PHE B 1 40  ? -21.884 -42.659 28.815  1.00 18.03 ? 40  PHE B CG  1 
ATOM   3987 C  CD1 . PHE B 1 40  ? -22.539 -41.675 29.536  1.00 18.31 ? 40  PHE B CD1 1 
ATOM   3988 C  CD2 . PHE B 1 40  ? -21.116 -42.285 27.721  1.00 18.78 ? 40  PHE B CD2 1 
ATOM   3989 C  CE1 . PHE B 1 40  ? -22.437 -40.341 29.172  1.00 18.29 ? 40  PHE B CE1 1 
ATOM   3990 C  CE2 . PHE B 1 40  ? -21.009 -40.949 27.358  1.00 18.73 ? 40  PHE B CE2 1 
ATOM   3991 C  CZ  . PHE B 1 40  ? -21.656 -39.982 28.099  1.00 18.49 ? 40  PHE B CZ  1 
ATOM   3992 N  N   . LYS B 1 41  ? -25.175 -44.762 30.056  1.00 20.82 ? 41  LYS B N   1 
ATOM   3993 C  CA  . LYS B 1 41  ? -26.335 -44.260 30.833  1.00 23.88 ? 41  LYS B CA  1 
ATOM   3994 C  C   . LYS B 1 41  ? -25.841 -43.095 31.695  1.00 22.57 ? 41  LYS B C   1 
ATOM   3995 O  O   . LYS B 1 41  ? -24.833 -43.281 32.355  1.00 22.09 ? 41  LYS B O   1 
ATOM   3996 C  CB  . LYS B 1 41  ? -26.884 -45.404 31.693  1.00 28.21 ? 41  LYS B CB  1 
ATOM   3997 C  CG  . LYS B 1 41  ? -27.997 -45.030 32.663  1.00 37.65 ? 41  LYS B CG  1 
ATOM   3998 C  CD  . LYS B 1 41  ? -28.763 -46.231 33.193  1.00 42.65 ? 41  LYS B CD  1 
ATOM   3999 C  CE  . LYS B 1 41  ? -27.850 -47.361 33.618  1.00 50.48 ? 41  LYS B CE  1 
ATOM   4000 N  NZ  . LYS B 1 41  ? -28.620 -48.466 34.236  1.00 56.86 ? 41  LYS B NZ  1 
ATOM   4001 N  N   . PHE B 1 42  ? -26.487 -41.925 31.645  1.00 22.31 ? 42  PHE B N   1 
ATOM   4002 C  CA  . PHE B 1 42  ? -26.236 -40.776 32.557  1.00 21.31 ? 42  PHE B CA  1 
ATOM   4003 C  C   . PHE B 1 42  ? -27.488 -40.592 33.421  1.00 22.74 ? 42  PHE B C   1 
ATOM   4004 O  O   . PHE B 1 42  ? -28.565 -40.348 32.854  1.00 24.33 ? 42  PHE B O   1 
ATOM   4005 C  CB  . PHE B 1 42  ? -25.889 -39.509 31.761  1.00 20.45 ? 42  PHE B CB  1 
ATOM   4006 C  CG  . PHE B 1 42  ? -25.345 -38.369 32.587  1.00 19.11 ? 42  PHE B CG  1 
ATOM   4007 C  CD1 . PHE B 1 42  ? -26.164 -37.649 33.446  1.00 19.91 ? 42  PHE B CD1 1 
ATOM   4008 C  CD2 . PHE B 1 42  ? -24.002 -38.050 32.551  1.00 18.95 ? 42  PHE B CD2 1 
ATOM   4009 C  CE1 . PHE B 1 42  ? -25.655 -36.625 34.235  1.00 19.31 ? 42  PHE B CE1 1 
ATOM   4010 C  CE2 . PHE B 1 42  ? -23.492 -37.024 33.331  1.00 19.04 ? 42  PHE B CE2 1 
ATOM   4011 C  CZ  . PHE B 1 42  ? -24.314 -36.320 34.180  1.00 19.42 ? 42  PHE B CZ  1 
ATOM   4012 N  N   . GLU B 1 43  ? -27.357 -40.703 34.741  1.00 24.95 ? 43  GLU B N   1 
ATOM   4013 C  CA  . GLU B 1 43  ? -28.471 -40.536 35.713  1.00 27.10 ? 43  GLU B CA  1 
ATOM   4014 C  C   . GLU B 1 43  ? -28.267 -39.225 36.474  1.00 25.14 ? 43  GLU B C   1 
ATOM   4015 O  O   . GLU B 1 43  ? -27.230 -39.053 37.096  1.00 23.33 ? 43  GLU B O   1 
ATOM   4016 C  CB  . GLU B 1 43  ? -28.536 -41.710 36.695  1.00 31.87 ? 43  GLU B CB  1 
ATOM   4017 C  CG  . GLU B 1 43  ? -28.850 -43.057 36.059  1.00 36.33 ? 43  GLU B CG  1 
ATOM   4018 C  CD  . GLU B 1 43  ? -28.842 -44.257 37.005  1.00 43.57 ? 43  GLU B CD  1 
ATOM   4019 O  OE1 . GLU B 1 43  ? -29.009 -44.060 38.237  1.00 46.65 ? 43  GLU B OE1 1 
ATOM   4020 O  OE2 . GLU B 1 43  ? -28.666 -45.405 36.505  1.00 53.31 ? 43  GLU B OE2 1 
ATOM   4021 N  N   . ALA B 1 44  ? -29.217 -38.303 36.361  1.00 28.40 ? 44  ALA B N   1 
ATOM   4022 C  CA  . ALA B 1 44  ? -29.433 -37.164 37.286  1.00 26.16 ? 44  ALA B CA  1 
ATOM   4023 C  C   . ALA B 1 44  ? -30.572 -37.578 38.221  1.00 26.64 ? 44  ALA B C   1 
ATOM   4024 O  O   . ALA B 1 44  ? -31.239 -38.569 37.952  1.00 27.14 ? 44  ALA B O   1 
ATOM   4025 C  CB  . ALA B 1 44  ? -29.736 -35.921 36.490  1.00 23.22 ? 44  ALA B CB  1 
ATOM   4026 N  N   . PRO B 1 45  ? -30.797 -36.934 39.387  1.00 29.18 ? 45  PRO B N   1 
ATOM   4027 C  CA  . PRO B 1 45  ? -32.008 -37.202 40.176  1.00 32.63 ? 45  PRO B CA  1 
ATOM   4028 C  C   . PRO B 1 45  ? -33.295 -36.892 39.386  1.00 32.39 ? 45  PRO B C   1 
ATOM   4029 O  O   . PRO B 1 45  ? -34.180 -37.692 39.420  1.00 28.66 ? 45  PRO B O   1 
ATOM   4030 C  CB  . PRO B 1 45  ? -31.835 -36.302 41.404  1.00 32.04 ? 45  PRO B CB  1 
ATOM   4031 C  CG  . PRO B 1 45  ? -30.334 -36.148 41.502  1.00 31.22 ? 45  PRO B CG  1 
ATOM   4032 C  CD  . PRO B 1 45  ? -29.882 -36.007 40.063  1.00 29.13 ? 45  PRO B CD  1 
ATOM   4033 N  N   . GLY B 1 46  ? -33.318 -35.786 38.638  1.00 36.02 ? 46  GLY B N   1 
ATOM   4034 C  CA  . GLY B 1 46  ? -34.428 -35.416 37.740  1.00 39.09 ? 46  GLY B CA  1 
ATOM   4035 C  C   . GLY B 1 46  ? -34.582 -36.413 36.602  1.00 42.98 ? 46  GLY B C   1 
ATOM   4036 O  O   . GLY B 1 46  ? -35.601 -37.150 36.570  1.00 46.85 ? 46  GLY B O   1 
ATOM   4037 N  N   . TRP B 1 47  ? -33.574 -36.508 35.736  1.00 42.38 ? 47  TRP B N   1 
ATOM   4038 C  CA  . TRP B 1 47  ? -33.695 -37.200 34.425  1.00 38.53 ? 47  TRP B CA  1 
ATOM   4039 C  C   . TRP B 1 47  ? -32.683 -38.338 34.264  1.00 39.66 ? 47  TRP B C   1 
ATOM   4040 O  O   . TRP B 1 47  ? -31.771 -38.471 35.114  1.00 41.82 ? 47  TRP B O   1 
ATOM   4041 C  CB  . TRP B 1 47  ? -33.529 -36.169 33.324  1.00 37.08 ? 47  TRP B CB  1 
ATOM   4042 C  CG  . TRP B 1 47  ? -32.339 -35.296 33.530  1.00 37.53 ? 47  TRP B CG  1 
ATOM   4043 C  CD1 . TRP B 1 47  ? -32.288 -34.108 34.202  1.00 40.10 ? 47  TRP B CD1 1 
ATOM   4044 C  CD2 . TRP B 1 47  ? -31.008 -35.546 33.056  1.00 37.86 ? 47  TRP B CD2 1 
ATOM   4045 N  NE1 . TRP B 1 47  ? -31.020 -33.591 34.163  1.00 39.78 ? 47  TRP B NE1 1 
ATOM   4046 C  CE2 . TRP B 1 47  ? -30.211 -34.456 33.471  1.00 37.29 ? 47  TRP B CE2 1 
ATOM   4047 C  CE3 . TRP B 1 47  ? -30.418 -36.582 32.327  1.00 37.19 ? 47  TRP B CE3 1 
ATOM   4048 C  CZ2 . TRP B 1 47  ? -28.853 -34.373 33.170  1.00 37.12 ? 47  TRP B CZ2 1 
ATOM   4049 C  CZ3 . TRP B 1 47  ? -29.081 -36.482 32.008  1.00 38.10 ? 47  TRP B CZ3 1 
ATOM   4050 C  CH2 . TRP B 1 47  ? -28.311 -35.395 32.428  1.00 38.60 ? 47  TRP B CH2 1 
ATOM   4051 N  N   . VAL B 1 48  ? -32.862 -39.137 33.207  1.00 36.36 ? 48  VAL B N   1 
ATOM   4052 C  CA  . VAL B 1 48  ? -31.852 -40.102 32.685  1.00 32.60 ? 48  VAL B CA  1 
ATOM   4053 C  C   . VAL B 1 48  ? -31.713 -39.931 31.167  1.00 30.02 ? 48  VAL B C   1 
ATOM   4054 O  O   . VAL B 1 48  ? -32.664 -39.614 30.481  1.00 29.94 ? 48  VAL B O   1 
ATOM   4055 C  CB  . VAL B 1 48  ? -32.175 -41.550 33.090  1.00 32.38 ? 48  VAL B CB  1 
ATOM   4056 C  CG1 . VAL B 1 48  ? -31.263 -42.572 32.418  1.00 31.17 ? 48  VAL B CG1 1 
ATOM   4057 C  CG2 . VAL B 1 48  ? -32.113 -41.702 34.595  1.00 33.11 ? 48  VAL B CG2 1 
ATOM   4058 N  N   . LEU B 1 49  ? -30.517 -40.136 30.661  1.00 27.49 ? 49  LEU B N   1 
ATOM   4059 C  CA  . LEU B 1 49  ? -30.200 -39.853 29.250  1.00 27.16 ? 49  LEU B CA  1 
ATOM   4060 C  C   . LEU B 1 49  ? -29.161 -40.885 28.854  1.00 25.39 ? 49  LEU B C   1 
ATOM   4061 O  O   . LEU B 1 49  ? -28.270 -41.119 29.648  1.00 26.22 ? 49  LEU B O   1 
ATOM   4062 C  CB  . LEU B 1 49  ? -29.692 -38.411 29.186  1.00 26.10 ? 49  LEU B CB  1 
ATOM   4063 C  CG  . LEU B 1 49  ? -29.845 -37.648 27.877  1.00 27.15 ? 49  LEU B CG  1 
ATOM   4064 C  CD1 . LEU B 1 49  ? -31.219 -37.843 27.227  1.00 27.07 ? 49  LEU B CD1 1 
ATOM   4065 C  CD2 . LEU B 1 49  ? -29.583 -36.173 28.135  1.00 26.35 ? 49  LEU B CD2 1 
ATOM   4066 N  N   . ARG B 1 50  ? -29.351 -41.556 27.731  1.00 25.31 ? 50  ARG B N   1 
ATOM   4067 C  CA  . ARG B 1 50  ? -28.354 -42.516 27.210  1.00 25.11 ? 50  ARG B CA  1 
ATOM   4068 C  C   . ARG B 1 50  ? -27.567 -41.813 26.101  1.00 22.62 ? 50  ARG B C   1 
ATOM   4069 O  O   . ARG B 1 50  ? -28.186 -41.339 25.142  1.00 21.31 ? 50  ARG B O   1 
ATOM   4070 C  CB  . ARG B 1 50  ? -29.048 -43.798 26.751  1.00 25.68 ? 50  ARG B CB  1 
ATOM   4071 C  CG  . ARG B 1 50  ? -29.835 -44.483 27.856  1.00 26.70 ? 50  ARG B CG  1 
ATOM   4072 C  CD  . ARG B 1 50  ? -31.251 -44.822 27.451  1.00 27.79 ? 50  ARG B CD  1 
ATOM   4073 N  NE  . ARG B 1 50  ? -32.053 -45.266 28.584  1.00 29.07 ? 50  ARG B NE  1 
ATOM   4074 C  CZ  . ARG B 1 50  ? -32.781 -44.491 29.383  1.00 30.64 ? 50  ARG B CZ  1 
ATOM   4075 N  NH1 . ARG B 1 50  ? -32.819 -43.175 29.229  1.00 29.40 ? 50  ARG B NH1 1 
ATOM   4076 N  NH2 . ARG B 1 50  ? -33.482 -45.055 30.355  1.00 33.51 ? 50  ARG B NH2 1 
ATOM   4077 N  N   . TYR B 1 51  ? -26.246 -41.779 26.244  1.00 20.67 ? 51  TYR B N   1 
ATOM   4078 C  CA  . TYR B 1 51  ? -25.327 -41.011 25.371  1.00 19.66 ? 51  TYR B CA  1 
ATOM   4079 C  C   . TYR B 1 51  ? -24.694 -41.998 24.410  1.00 18.39 ? 51  TYR B C   1 
ATOM   4080 O  O   . TYR B 1 51  ? -24.085 -42.948 24.919  1.00 18.05 ? 51  TYR B O   1 
ATOM   4081 C  CB  . TYR B 1 51  ? -24.305 -40.224 26.195  1.00 18.65 ? 51  TYR B CB  1 
ATOM   4082 C  CG  . TYR B 1 51  ? -24.843 -38.935 26.763  1.00 18.95 ? 51  TYR B CG  1 
ATOM   4083 C  CD1 . TYR B 1 51  ? -24.900 -37.784 25.989  1.00 19.29 ? 51  TYR B CD1 1 
ATOM   4084 C  CD2 . TYR B 1 51  ? -25.309 -38.867 28.064  1.00 18.73 ? 51  TYR B CD2 1 
ATOM   4085 C  CE1 . TYR B 1 51  ? -25.355 -36.585 26.506  1.00 19.05 ? 51  TYR B CE1 1 
ATOM   4086 C  CE2 . TYR B 1 51  ? -25.783 -37.677 28.598  1.00 19.54 ? 51  TYR B CE2 1 
ATOM   4087 C  CZ  . TYR B 1 51  ? -25.810 -36.537 27.814  1.00 20.69 ? 51  TYR B CZ  1 
ATOM   4088 O  OH  . TYR B 1 51  ? -26.305 -35.373 28.324  1.00 24.04 ? 51  TYR B OH  1 
ATOM   4089 N  N   . LEU B 1 52  ? -24.916 -41.785 23.107  1.00 16.89 ? 52  LEU B N   1 
ATOM   4090 C  CA  . LEU B 1 52  ? -24.440 -42.646 22.005  1.00 16.64 ? 52  LEU B CA  1 
ATOM   4091 C  C   . LEU B 1 52  ? -23.281 -41.922 21.321  1.00 16.63 ? 52  LEU B C   1 
ATOM   4092 O  O   . LEU B 1 52  ? -23.437 -40.736 21.025  1.00 16.69 ? 52  LEU B O   1 
ATOM   4093 C  CB  . LEU B 1 52  ? -25.576 -42.867 21.001  1.00 16.67 ? 52  LEU B CB  1 
ATOM   4094 C  CG  . LEU B 1 52  ? -26.669 -43.856 21.383  1.00 17.10 ? 52  LEU B CG  1 
ATOM   4095 C  CD1 . LEU B 1 52  ? -27.264 -43.556 22.726  1.00 17.95 ? 52  LEU B CD1 1 
ATOM   4096 C  CD2 . LEU B 1 52  ? -27.770 -43.833 20.346  1.00 17.54 ? 52  LEU B CD2 1 
ATOM   4097 N  N   . SER B 1 53  ? -22.200 -42.639 21.010  1.00 17.59 ? 53  SER B N   1 
ATOM   4098 C  CA  . SER B 1 53  ? -20.959 -42.115 20.382  1.00 18.02 ? 53  SER B CA  1 
ATOM   4099 C  C   . SER B 1 53  ? -20.527 -42.901 19.131  1.00 18.53 ? 53  SER B C   1 
ATOM   4100 O  O   . SER B 1 53  ? -19.683 -42.382 18.395  1.00 19.30 ? 53  SER B O   1 
ATOM   4101 C  CB  . SER B 1 53  ? -19.883 -42.103 21.396  1.00 17.30 ? 53  SER B CB  1 
ATOM   4102 O  OG  . SER B 1 53  ? -20.200 -41.175 22.407  1.00 16.84 ? 53  SER B OG  1 
ATOM   4103 N  N   . SER B 1 54  ? -21.056 -44.095 18.862  1.00 19.61 ? 54  SER B N   1 
ATOM   4104 C  CA  . SER B 1 54  ? -20.612 -44.898 17.688  1.00 20.14 ? 54  SER B CA  1 
ATOM   4105 C  C   . SER B 1 54  ? -21.678 -44.862 16.580  1.00 20.72 ? 54  SER B C   1 
ATOM   4106 O  O   . SER B 1 54  ? -22.871 -44.813 16.915  1.00 19.00 ? 54  SER B O   1 
ATOM   4107 C  CB  . SER B 1 54  ? -20.287 -46.294 18.118  1.00 20.07 ? 54  SER B CB  1 
ATOM   4108 O  OG  . SER B 1 54  ? -21.479 -47.013 18.389  1.00 20.94 ? 54  SER B OG  1 
ATOM   4109 N  N   . GLN B 1 55  ? -21.278 -44.890 15.301  1.00 21.08 ? 55  GLN B N   1 
ATOM   4110 C  CA  . GLN B 1 55  ? -22.247 -44.956 14.185  1.00 20.47 ? 55  GLN B CA  1 
ATOM   4111 C  C   . GLN B 1 55  ? -22.975 -46.299 14.261  1.00 20.15 ? 55  GLN B C   1 
ATOM   4112 O  O   . GLN B 1 55  ? -24.145 -46.354 13.897  1.00 18.11 ? 55  GLN B O   1 
ATOM   4113 C  CB  . GLN B 1 55  ? -21.591 -44.635 12.834  1.00 23.19 ? 55  GLN B CB  1 
ATOM   4114 C  CG  . GLN B 1 55  ? -21.117 -45.814 12.010  1.00 23.95 ? 55  GLN B CG  1 
ATOM   4115 C  CD  . GLN B 1 55  ? -22.154 -46.745 11.445  1.00 22.11 ? 55  GLN B CD  1 
ATOM   4116 O  OE1 . GLN B 1 55  ? -22.180 -47.918 11.795  1.00 25.59 ? 55  GLN B OE1 1 
ATOM   4117 N  NE2 . GLN B 1 55  ? -22.927 -46.279 10.486  1.00 21.51 ? 55  GLN B NE2 1 
ATOM   4118 N  N   . ARG B 1 56  ? -22.345 -47.343 14.785  1.00 21.87 ? 56  ARG B N   1 
ATOM   4119 C  CA  . ARG B 1 56  ? -23.017 -48.650 14.987  1.00 22.98 ? 56  ARG B CA  1 
ATOM   4120 C  C   . ARG B 1 56  ? -24.370 -48.398 15.665  1.00 24.94 ? 56  ARG B C   1 
ATOM   4121 O  O   . ARG B 1 56  ? -25.418 -48.859 15.139  1.00 24.83 ? 56  ARG B O   1 
ATOM   4122 C  CB  . ARG B 1 56  ? -22.111 -49.573 15.797  1.00 25.41 ? 56  ARG B CB  1 
ATOM   4123 C  CG  . ARG B 1 56  ? -22.800 -50.809 16.354  1.00 29.52 ? 56  ARG B CG  1 
ATOM   4124 C  CD  . ARG B 1 56  ? -21.904 -51.619 17.285  1.00 31.27 ? 56  ARG B CD  1 
ATOM   4125 N  NE  . ARG B 1 56  ? -22.760 -52.671 17.791  1.00 34.29 ? 56  ARG B NE  1 
ATOM   4126 C  CZ  . ARG B 1 56  ? -23.148 -52.830 19.051  1.00 35.04 ? 56  ARG B CZ  1 
ATOM   4127 N  NH1 . ARG B 1 56  ? -22.702 -52.042 20.008  1.00 34.69 ? 56  ARG B NH1 1 
ATOM   4128 N  NH2 . ARG B 1 56  ? -23.983 -53.807 19.347  1.00 38.92 ? 56  ARG B NH2 1 
ATOM   4129 N  N   . LEU B 1 57  ? -24.372 -47.665 16.780  1.00 23.76 ? 57  LEU B N   1 
ATOM   4130 C  CA  . LEU B 1 57  ? -25.600 -47.471 17.584  1.00 22.75 ? 57  LEU B CA  1 
ATOM   4131 C  C   . LEU B 1 57  ? -26.385 -46.269 17.075  1.00 22.32 ? 57  LEU B C   1 
ATOM   4132 O  O   . LEU B 1 57  ? -27.632 -46.304 17.175  1.00 20.04 ? 57  LEU B O   1 
ATOM   4133 C  CB  . LEU B 1 57  ? -25.218 -47.321 19.054  1.00 22.95 ? 57  LEU B CB  1 
ATOM   4134 C  CG  . LEU B 1 57  ? -24.649 -48.593 19.682  1.00 22.80 ? 57  LEU B CG  1 
ATOM   4135 C  CD1 . LEU B 1 57  ? -24.483 -48.426 21.188  1.00 25.31 ? 57  LEU B CD1 1 
ATOM   4136 C  CD2 . LEU B 1 57  ? -25.539 -49.775 19.401  1.00 22.53 ? 57  LEU B CD2 1 
ATOM   4137 N  N   . ILE B 1 58  ? -25.702 -45.232 16.586  1.00 21.48 ? 58  ILE B N   1 
ATOM   4138 C  CA  . ILE B 1 58  ? -26.405 -44.000 16.126  1.00 22.11 ? 58  ILE B CA  1 
ATOM   4139 C  C   . ILE B 1 58  ? -27.218 -44.335 14.864  1.00 22.25 ? 58  ILE B C   1 
ATOM   4140 O  O   . ILE B 1 58  ? -28.323 -43.780 14.714  1.00 24.63 ? 58  ILE B O   1 
ATOM   4141 C  CB  . ILE B 1 58  ? -25.438 -42.803 15.994  1.00 20.91 ? 58  ILE B CB  1 
ATOM   4142 C  CG1 . ILE B 1 58  ? -25.082 -42.300 17.395  1.00 19.77 ? 58  ILE B CG1 1 
ATOM   4143 C  CG2 . ILE B 1 58  ? -26.025 -41.691 15.117  1.00 21.74 ? 58  ILE B CG2 1 
ATOM   4144 C  CD1 . ILE B 1 58  ? -23.796 -41.530 17.525  1.00 19.67 ? 58  ILE B CD1 1 
ATOM   4145 N  N   . LYS B 1 59  ? -26.785 -45.280 14.040  1.00 21.78 ? 59  LYS B N   1 
ATOM   4146 C  CA  . LYS B 1 59  ? -27.540 -45.591 12.802  1.00 22.40 ? 59  LYS B CA  1 
ATOM   4147 C  C   . LYS B 1 59  ? -28.863 -46.259 13.205  1.00 22.62 ? 59  LYS B C   1 
ATOM   4148 O  O   . LYS B 1 59  ? -29.879 -46.015 12.559  1.00 26.04 ? 59  LYS B O   1 
ATOM   4149 C  CB  . LYS B 1 59  ? -26.685 -46.393 11.820  1.00 22.35 ? 59  LYS B CB  1 
ATOM   4150 C  CG  . LYS B 1 59  ? -26.940 -47.887 11.821  1.00 23.77 ? 59  LYS B CG  1 
ATOM   4151 C  CD  . LYS B 1 59  ? -25.843 -48.724 11.185  1.00 24.10 ? 59  LYS B CD  1 
ATOM   4152 C  CE  . LYS B 1 59  ? -25.638 -50.014 11.948  1.00 23.27 ? 59  LYS B CE  1 
ATOM   4153 N  NZ  . LYS B 1 59  ? -24.564 -50.841 11.362  1.00 25.61 ? 59  LYS B NZ  1 
ATOM   4154 N  N   . GLU B 1 60  ? -28.882 -47.041 14.269  1.00 22.79 ? 60  GLU B N   1 
ATOM   4155 C  CA  . GLU B 1 60  ? -30.138 -47.646 14.770  1.00 23.33 ? 60  GLU B CA  1 
ATOM   4156 C  C   . GLU B 1 60  ? -31.044 -46.553 15.329  1.00 22.18 ? 60  GLU B C   1 
ATOM   4157 O  O   . GLU B 1 60  ? -32.238 -46.583 15.047  1.00 22.80 ? 60  GLU B O   1 
ATOM   4158 C  CB  . GLU B 1 60  ? -29.840 -48.724 15.815  1.00 25.26 ? 60  GLU B CB  1 
ATOM   4159 C  CG  . GLU B 1 60  ? -29.262 -49.963 15.174  1.00 28.29 ? 60  GLU B CG  1 
ATOM   4160 C  CD  . GLU B 1 60  ? -29.311 -51.220 16.009  1.00 30.92 ? 60  GLU B CD  1 
ATOM   4161 O  OE1 . GLU B 1 60  ? -28.391 -52.049 15.855  1.00 30.56 ? 60  GLU B OE1 1 
ATOM   4162 O  OE2 . GLU B 1 60  ? -30.273 -51.365 16.790  1.00 36.23 ? 60  GLU B OE2 1 
ATOM   4163 N  N   . ALA B 1 61  ? -30.497 -45.616 16.095  1.00 20.18 ? 61  ALA B N   1 
ATOM   4164 C  CA  . ALA B 1 61  ? -31.296 -44.596 16.781  1.00 19.70 ? 61  ALA B CA  1 
ATOM   4165 C  C   . ALA B 1 61  ? -31.837 -43.598 15.752  1.00 20.77 ? 61  ALA B C   1 
ATOM   4166 O  O   . ALA B 1 61  ? -32.742 -42.834 16.124  1.00 21.93 ? 61  ALA B O   1 
ATOM   4167 C  CB  . ALA B 1 61  ? -30.464 -43.938 17.847  1.00 20.71 ? 61  ALA B CB  1 
ATOM   4168 N  N   . CYS B 1 62  ? -31.341 -43.606 14.506  1.00 20.44 ? 62  CYS B N   1 
ATOM   4169 C  CA  . CYS B 1 62  ? -31.809 -42.691 13.418  1.00 21.27 ? 62  CYS B CA  1 
ATOM   4170 C  C   . CYS B 1 62  ? -32.935 -43.340 12.604  1.00 21.37 ? 62  CYS B C   1 
ATOM   4171 O  O   . CYS B 1 62  ? -33.337 -42.746 11.585  1.00 21.59 ? 62  CYS B O   1 
ATOM   4172 C  CB  . CYS B 1 62  ? -30.649 -42.228 12.535  1.00 20.62 ? 62  CYS B CB  1 
ATOM   4173 S  SG  . CYS B 1 62  ? -29.653 -40.966 13.387  1.00 21.25 ? 62  CYS B SG  1 
ATOM   4174 N  N   . ASP B 1 63  ? -33.454 -44.483 13.061  1.00 20.59 ? 63  ASP B N   1 
ATOM   4175 C  CA  . ASP B 1 63  ? -34.474 -45.293 12.345  1.00 21.11 ? 63  ASP B CA  1 
ATOM   4176 C  C   . ASP B 1 63  ? -35.834 -44.727 12.726  1.00 21.87 ? 63  ASP B C   1 
ATOM   4177 O  O   . ASP B 1 63  ? -36.160 -44.810 13.933  1.00 19.79 ? 63  ASP B O   1 
ATOM   4178 C  CB  . ASP B 1 63  ? -34.314 -46.775 12.699  1.00 23.09 ? 63  ASP B CB  1 
ATOM   4179 C  CG  . ASP B 1 63  ? -35.461 -47.669 12.278  1.00 23.88 ? 63  ASP B CG  1 
ATOM   4180 O  OD1 . ASP B 1 63  ? -36.239 -47.243 11.371  1.00 23.11 ? 63  ASP B OD1 1 
ATOM   4181 O  OD2 . ASP B 1 63  ? -35.589 -48.758 12.894  1.00 22.54 ? 63  ASP B OD2 1 
ATOM   4182 N  N   . GLU B 1 64  ? -36.552 -44.110 11.773  1.00 22.55 ? 64  GLU B N   1 
ATOM   4183 C  CA  . GLU B 1 64  ? -37.785 -43.339 12.099  1.00 25.46 ? 64  GLU B CA  1 
ATOM   4184 C  C   . GLU B 1 64  ? -38.901 -44.315 12.489  1.00 22.32 ? 64  GLU B C   1 
ATOM   4185 O  O   . GLU B 1 64  ? -39.895 -43.854 13.047  1.00 18.72 ? 64  GLU B O   1 
ATOM   4186 C  CB  . GLU B 1 64  ? -38.176 -42.339 11.010  1.00 27.20 ? 64  GLU B CB  1 
ATOM   4187 C  CG  . GLU B 1 64  ? -38.818 -42.937 9.780   1.00 32.91 ? 64  GLU B CG  1 
ATOM   4188 C  CD  . GLU B 1 64  ? -39.408 -41.913 8.803   1.00 39.92 ? 64  GLU B CD  1 
ATOM   4189 O  OE1 . GLU B 1 64  ? -39.079 -40.680 8.892   1.00 41.33 ? 64  GLU B OE1 1 
ATOM   4190 O  OE2 . GLU B 1 64  ? -40.207 -42.342 7.944   1.00 47.27 ? 64  GLU B OE2 1 
ATOM   4191 N  N   . SER B 1 65  ? -38.713 -45.617 12.275  1.00 21.99 ? 65  SER B N   1 
ATOM   4192 C  CA  . SER B 1 65  ? -39.715 -46.639 12.650  1.00 24.22 ? 65  SER B CA  1 
ATOM   4193 C  C   . SER B 1 65  ? -39.616 -46.899 14.155  1.00 25.06 ? 65  SER B C   1 
ATOM   4194 O  O   . SER B 1 65  ? -40.592 -47.367 14.732  1.00 24.40 ? 65  SER B O   1 
ATOM   4195 C  CB  . SER B 1 65  ? -39.580 -47.904 11.835  1.00 26.35 ? 65  SER B CB  1 
ATOM   4196 O  OG  . SER B 1 65  ? -38.578 -48.765 12.369  1.00 29.71 ? 65  SER B OG  1 
ATOM   4197 N  N   . ARG B 1 66  ? -38.497 -46.581 14.803  1.00 27.11 ? 66  ARG B N   1 
ATOM   4198 C  CA  . ARG B 1 66  ? -38.375 -46.872 16.261  1.00 27.20 ? 66  ARG B CA  1 
ATOM   4199 C  C   . ARG B 1 66  ? -38.136 -45.614 17.094  1.00 23.78 ? 66  ARG B C   1 
ATOM   4200 O  O   . ARG B 1 66  ? -38.414 -45.677 18.292  1.00 26.75 ? 66  ARG B O   1 
ATOM   4201 C  CB  . ARG B 1 66  ? -37.304 -47.936 16.480  1.00 29.08 ? 66  ARG B CB  1 
ATOM   4202 C  CG  . ARG B 1 66  ? -37.684 -49.280 15.881  1.00 30.84 ? 66  ARG B CG  1 
ATOM   4203 C  CD  . ARG B 1 66  ? -36.657 -50.301 16.290  1.00 32.54 ? 66  ARG B CD  1 
ATOM   4204 N  NE  . ARG B 1 66  ? -35.449 -50.157 15.503  1.00 34.73 ? 66  ARG B NE  1 
ATOM   4205 C  CZ  . ARG B 1 66  ? -34.218 -50.398 15.952  1.00 35.49 ? 66  ARG B CZ  1 
ATOM   4206 N  NH1 . ARG B 1 66  ? -34.036 -50.811 17.202  1.00 37.15 ? 66  ARG B NH1 1 
ATOM   4207 N  NH2 . ARG B 1 66  ? -33.182 -50.242 15.142  1.00 31.12 ? 66  ARG B NH2 1 
ATOM   4208 N  N   . PHE B 1 67  ? -37.673 -44.515 16.499  1.00 22.48 ? 67  PHE B N   1 
ATOM   4209 C  CA  . PHE B 1 67  ? -37.211 -43.311 17.241  1.00 20.50 ? 67  PHE B CA  1 
ATOM   4210 C  C   . PHE B 1 67  ? -37.835 -42.046 16.647  1.00 18.43 ? 67  PHE B C   1 
ATOM   4211 O  O   . PHE B 1 67  ? -38.092 -41.986 15.436  1.00 18.88 ? 67  PHE B O   1 
ATOM   4212 C  CB  . PHE B 1 67  ? -35.677 -43.302 17.252  1.00 21.00 ? 67  PHE B CB  1 
ATOM   4213 C  CG  . PHE B 1 67  ? -35.107 -44.458 18.036  1.00 20.43 ? 67  PHE B CG  1 
ATOM   4214 C  CD1 . PHE B 1 67  ? -35.198 -44.474 19.417  1.00 18.56 ? 67  PHE B CD1 1 
ATOM   4215 C  CD2 . PHE B 1 67  ? -34.563 -45.560 17.390  1.00 19.54 ? 67  PHE B CD2 1 
ATOM   4216 C  CE1 . PHE B 1 67  ? -34.729 -45.557 20.140  1.00 19.83 ? 67  PHE B CE1 1 
ATOM   4217 C  CE2 . PHE B 1 67  ? -34.093 -46.641 18.121  1.00 19.76 ? 67  PHE B CE2 1 
ATOM   4218 C  CZ  . PHE B 1 67  ? -34.172 -46.636 19.494  1.00 19.25 ? 67  PHE B CZ  1 
ATOM   4219 N  N   . ASP B 1 68  ? -38.122 -41.073 17.500  1.00 17.47 ? 68  ASP B N   1 
ATOM   4220 C  CA  . ASP B 1 68  ? -38.568 -39.726 17.069  1.00 17.53 ? 68  ASP B CA  1 
ATOM   4221 C  C   . ASP B 1 68  ? -37.754 -38.690 17.842  1.00 17.98 ? 68  ASP B C   1 
ATOM   4222 O  O   . ASP B 1 68  ? -37.198 -39.034 18.904  1.00 18.56 ? 68  ASP B O   1 
ATOM   4223 C  CB  . ASP B 1 68  ? -40.067 -39.540 17.260  1.00 18.05 ? 68  ASP B CB  1 
ATOM   4224 C  CG  . ASP B 1 68  ? -40.619 -38.214 16.747  1.00 18.59 ? 68  ASP B CG  1 
ATOM   4225 O  OD1 . ASP B 1 68  ? -40.125 -37.721 15.692  1.00 17.70 ? 68  ASP B OD1 1 
ATOM   4226 O  OD2 . ASP B 1 68  ? -41.564 -37.704 17.402  1.00 18.87 ? 68  ASP B OD2 1 
ATOM   4227 N  N   . LYS B 1 69  ? -37.665 -37.481 17.307  1.00 17.23 ? 69  LYS B N   1 
ATOM   4228 C  CA  . LYS B 1 69  ? -36.959 -36.365 17.967  1.00 19.02 ? 69  LYS B CA  1 
ATOM   4229 C  C   . LYS B 1 69  ? -37.512 -36.194 19.385  1.00 18.76 ? 69  LYS B C   1 
ATOM   4230 O  O   . LYS B 1 69  ? -38.750 -36.206 19.576  1.00 17.92 ? 69  LYS B O   1 
ATOM   4231 C  CB  . LYS B 1 69  ? -37.107 -35.078 17.147  1.00 19.50 ? 69  LYS B CB  1 
ATOM   4232 C  CG  . LYS B 1 69  ? -36.820 -33.829 17.957  1.00 19.65 ? 69  LYS B CG  1 
ATOM   4233 C  CD  . LYS B 1 69  ? -36.483 -32.632 17.137  1.00 20.13 ? 69  LYS B CD  1 
ATOM   4234 C  CE  . LYS B 1 69  ? -36.207 -31.442 18.036  1.00 20.37 ? 69  LYS B CE  1 
ATOM   4235 N  NZ  . LYS B 1 69  ? -35.535 -30.353 17.303  1.00 20.55 ? 69  LYS B NZ  1 
ATOM   4236 N  N   . ASN B 1 70  ? -36.613 -36.069 20.346  1.00 19.43 ? 70  ASN B N   1 
ATOM   4237 C  CA  . ASN B 1 70  ? -36.978 -35.831 21.763  1.00 21.10 ? 70  ASN B CA  1 
ATOM   4238 C  C   . ASN B 1 70  ? -36.623 -34.381 22.080  1.00 20.33 ? 70  ASN B C   1 
ATOM   4239 O  O   . ASN B 1 70  ? -35.630 -33.862 21.510  1.00 20.54 ? 70  ASN B O   1 
ATOM   4240 C  CB  . ASN B 1 70  ? -36.310 -36.826 22.724  1.00 21.64 ? 70  ASN B CB  1 
ATOM   4241 C  CG  . ASN B 1 70  ? -36.658 -36.552 24.178  1.00 23.47 ? 70  ASN B CG  1 
ATOM   4242 O  OD1 . ASN B 1 70  ? -37.836 -36.588 24.573  1.00 26.02 ? 70  ASN B OD1 1 
ATOM   4243 N  ND2 . ASN B 1 70  ? -35.647 -36.267 24.990  1.00 23.72 ? 70  ASN B ND2 1 
ATOM   4244 N  N   . LEU B 1 71  ? -37.415 -33.746 22.937  1.00 19.48 ? 71  LEU B N   1 
ATOM   4245 C  CA  . LEU B 1 71  ? -37.016 -32.461 23.550  1.00 19.58 ? 71  LEU B CA  1 
ATOM   4246 C  C   . LEU B 1 71  ? -36.275 -32.809 24.844  1.00 20.93 ? 71  LEU B C   1 
ATOM   4247 O  O   . LEU B 1 71  ? -36.922 -33.265 25.784  1.00 22.55 ? 71  LEU B O   1 
ATOM   4248 C  CB  . LEU B 1 71  ? -38.252 -31.586 23.779  1.00 18.70 ? 71  LEU B CB  1 
ATOM   4249 C  CG  . LEU B 1 71  ? -39.119 -31.312 22.555  1.00 18.16 ? 71  LEU B CG  1 
ATOM   4250 C  CD1 . LEU B 1 71  ? -40.231 -30.346 22.920  1.00 18.90 ? 71  LEU B CD1 1 
ATOM   4251 C  CD2 . LEU B 1 71  ? -38.298 -30.748 21.393  1.00 18.86 ? 71  LEU B CD2 1 
ATOM   4252 N  N   . SER B 1 72  ? -34.943 -32.702 24.831  1.00 22.33 ? 72  SER B N   1 
ATOM   4253 C  CA  . SER B 1 72  ? -34.060 -32.666 26.024  1.00 21.92 ? 72  SER B CA  1 
ATOM   4254 C  C   . SER B 1 72  ? -34.490 -31.526 26.959  1.00 22.79 ? 72  SER B C   1 
ATOM   4255 O  O   . SER B 1 72  ? -35.144 -30.580 26.503  1.00 25.28 ? 72  SER B O   1 
ATOM   4256 C  CB  . SER B 1 72  ? -32.651 -32.491 25.583  1.00 21.78 ? 72  SER B CB  1 
ATOM   4257 O  OG  . SER B 1 72  ? -32.537 -31.328 24.777  1.00 22.90 ? 72  SER B OG  1 
ATOM   4258 N  N   . GLN B 1 73  ? -34.145 -31.611 28.236  1.00 23.64 ? 73  GLN B N   1 
ATOM   4259 C  CA  . GLN B 1 73  ? -34.366 -30.528 29.222  1.00 24.52 ? 73  GLN B CA  1 
ATOM   4260 C  C   . GLN B 1 73  ? -33.954 -29.181 28.604  1.00 23.01 ? 73  GLN B C   1 
ATOM   4261 O  O   . GLN B 1 73  ? -34.681 -28.199 28.776  1.00 24.82 ? 73  GLN B O   1 
ATOM   4262 C  CB  . GLN B 1 73  ? -33.559 -30.804 30.495  1.00 27.04 ? 73  GLN B CB  1 
ATOM   4263 C  CG  . GLN B 1 73  ? -34.004 -32.040 31.261  1.00 31.53 ? 73  GLN B CG  1 
ATOM   4264 C  CD  . GLN B 1 73  ? -35.400 -31.860 31.802  1.00 34.07 ? 73  GLN B CD  1 
ATOM   4265 O  OE1 . GLN B 1 73  ? -36.347 -32.549 31.413  1.00 32.25 ? 73  GLN B OE1 1 
ATOM   4266 N  NE2 . GLN B 1 73  ? -35.534 -30.875 32.669  1.00 37.39 ? 73  GLN B NE2 1 
ATOM   4267 N  N   . VAL B 1 74  ? -32.804 -29.112 27.938  1.00 21.24 ? 74  VAL B N   1 
ATOM   4268 C  CA  . VAL B 1 74  ? -32.342 -27.850 27.276  1.00 21.25 ? 74  VAL B CA  1 
ATOM   4269 C  C   . VAL B 1 74  ? -33.433 -27.349 26.317  1.00 19.40 ? 74  VAL B C   1 
ATOM   4270 O  O   . VAL B 1 74  ? -33.812 -26.168 26.401  1.00 20.35 ? 74  VAL B O   1 
ATOM   4271 C  CB  . VAL B 1 74  ? -30.997 -28.032 26.541  1.00 21.00 ? 74  VAL B CB  1 
ATOM   4272 C  CG1 . VAL B 1 74  ? -30.696 -26.867 25.613  1.00 20.23 ? 74  VAL B CG1 1 
ATOM   4273 C  CG2 . VAL B 1 74  ? -29.843 -28.279 27.510  1.00 20.27 ? 74  VAL B CG2 1 
ATOM   4274 N  N   . LEU B 1 75  ? -33.907 -28.201 25.418  1.00 18.03 ? 75  LEU B N   1 
ATOM   4275 C  CA  . LEU B 1 75  ? -34.911 -27.782 24.403  1.00 18.77 ? 75  LEU B CA  1 
ATOM   4276 C  C   . LEU B 1 75  ? -36.260 -27.503 25.063  1.00 18.05 ? 75  LEU B C   1 
ATOM   4277 O  O   . LEU B 1 75  ? -36.980 -26.673 24.506  1.00 17.64 ? 75  LEU B O   1 
ATOM   4278 C  CB  . LEU B 1 75  ? -35.055 -28.839 23.293  1.00 17.77 ? 75  LEU B CB  1 
ATOM   4279 C  CG  . LEU B 1 75  ? -33.864 -28.956 22.346  1.00 16.46 ? 75  LEU B CG  1 
ATOM   4280 C  CD1 . LEU B 1 75  ? -34.292 -29.550 21.025  1.00 16.47 ? 75  LEU B CD1 1 
ATOM   4281 C  CD2 . LEU B 1 75  ? -33.191 -27.621 22.126  1.00 17.35 ? 75  LEU B CD2 1 
ATOM   4282 N  N   . LYS B 1 76  ? -36.596 -28.174 26.171  1.00 18.17 ? 76  LYS B N   1 
ATOM   4283 C  CA  . LYS B 1 76  ? -37.817 -27.841 26.957  1.00 18.80 ? 76  LYS B CA  1 
ATOM   4284 C  C   . LYS B 1 76  ? -37.683 -26.442 27.567  1.00 17.25 ? 76  LYS B C   1 
ATOM   4285 O  O   . LYS B 1 76  ? -38.689 -25.776 27.691  1.00 16.91 ? 76  LYS B O   1 
ATOM   4286 C  CB  . LYS B 1 76  ? -38.089 -28.895 28.026  1.00 20.48 ? 76  LYS B CB  1 
ATOM   4287 C  CG  . LYS B 1 76  ? -38.820 -30.118 27.509  1.00 21.70 ? 76  LYS B CG  1 
ATOM   4288 C  CD  . LYS B 1 76  ? -38.771 -31.301 28.441  1.00 23.04 ? 76  LYS B CD  1 
ATOM   4289 C  CE  . LYS B 1 76  ? -39.230 -32.551 27.725  1.00 24.19 ? 76  LYS B CE  1 
ATOM   4290 N  NZ  . LYS B 1 76  ? -39.856 -33.489 28.675  1.00 26.11 ? 76  LYS B NZ  1 
ATOM   4291 N  N   . PHE B 1 77  ? -36.478 -25.989 27.878  1.00 16.62 ? 77  PHE B N   1 
ATOM   4292 C  CA  . PHE B 1 77  ? -36.243 -24.620 28.410  1.00 16.68 ? 77  PHE B CA  1 
ATOM   4293 C  C   . PHE B 1 77  ? -36.113 -23.589 27.274  1.00 16.40 ? 77  PHE B C   1 
ATOM   4294 O  O   . PHE B 1 77  ? -36.568 -22.443 27.482  1.00 16.95 ? 77  PHE B O   1 
ATOM   4295 C  CB  . PHE B 1 77  ? -35.076 -24.644 29.400  1.00 16.24 ? 77  PHE B CB  1 
ATOM   4296 C  CG  . PHE B 1 77  ? -35.452 -25.257 30.727  1.00 16.80 ? 77  PHE B CG  1 
ATOM   4297 C  CD1 . PHE B 1 77  ? -36.557 -24.796 31.431  1.00 17.48 ? 77  PHE B CD1 1 
ATOM   4298 C  CD2 . PHE B 1 77  ? -34.700 -26.283 31.287  1.00 18.16 ? 77  PHE B CD2 1 
ATOM   4299 C  CE1 . PHE B 1 77  ? -36.906 -25.342 32.659  1.00 17.30 ? 77  PHE B CE1 1 
ATOM   4300 C  CE2 . PHE B 1 77  ? -35.052 -26.839 32.514  1.00 17.64 ? 77  PHE B CE2 1 
ATOM   4301 C  CZ  . PHE B 1 77  ? -36.148 -26.356 33.202  1.00 17.59 ? 77  PHE B CZ  1 
ATOM   4302 N  N   . VAL B 1 78  ? -35.559 -23.939 26.110  1.00 14.99 ? 78  VAL B N   1 
ATOM   4303 C  CA  . VAL B 1 78  ? -35.551 -23.019 24.928  1.00 15.15 ? 78  VAL B CA  1 
ATOM   4304 C  C   . VAL B 1 78  ? -37.010 -22.732 24.501  1.00 16.26 ? 78  VAL B C   1 
ATOM   4305 O  O   . VAL B 1 78  ? -37.305 -21.592 24.019  1.00 18.03 ? 78  VAL B O   1 
ATOM   4306 C  CB  . VAL B 1 78  ? -34.718 -23.622 23.782  1.00 15.08 ? 78  VAL B CB  1 
ATOM   4307 C  CG1 . VAL B 1 78  ? -34.887 -22.896 22.465  1.00 15.62 ? 78  VAL B CG1 1 
ATOM   4308 C  CG2 . VAL B 1 78  ? -33.247 -23.640 24.139  1.00 16.64 ? 78  VAL B CG2 1 
ATOM   4309 N  N   . ARG B 1 79  ? -37.894 -23.728 24.642  1.00 16.15 ? 79  ARG B N   1 
ATOM   4310 C  CA  . ARG B 1 79  ? -39.354 -23.670 24.347  1.00 15.84 ? 79  ARG B CA  1 
ATOM   4311 C  C   . ARG B 1 79  ? -40.074 -22.614 25.188  1.00 15.68 ? 79  ARG B C   1 
ATOM   4312 O  O   . ARG B 1 79  ? -41.076 -22.074 24.712  1.00 14.79 ? 79  ARG B O   1 
ATOM   4313 C  CB  . ARG B 1 79  ? -39.988 -25.032 24.618  1.00 16.16 ? 79  ARG B CB  1 
ATOM   4314 C  CG  . ARG B 1 79  ? -41.474 -25.082 24.298  1.00 16.13 ? 79  ARG B CG  1 
ATOM   4315 C  CD  . ARG B 1 79  ? -41.888 -26.455 23.865  1.00 16.42 ? 79  ARG B CD  1 
ATOM   4316 N  NE  . ARG B 1 79  ? -43.320 -26.478 23.669  1.00 16.79 ? 79  ARG B NE  1 
ATOM   4317 C  CZ  . ARG B 1 79  ? -43.956 -27.154 22.730  1.00 16.94 ? 79  ARG B CZ  1 
ATOM   4318 N  NH1 . ARG B 1 79  ? -43.303 -27.876 21.828  1.00 16.26 ? 79  ARG B NH1 1 
ATOM   4319 N  NH2 . ARG B 1 79  ? -45.268 -27.035 22.656  1.00 17.60 ? 79  ARG B NH2 1 
ATOM   4320 N  N   . ASP B 1 80  ? -39.592 -22.300 26.386  1.00 17.17 ? 80  ASP B N   1 
ATOM   4321 C  CA  . ASP B 1 80  ? -40.208 -21.209 27.181  1.00 18.12 ? 80  ASP B CA  1 
ATOM   4322 C  C   . ASP B 1 80  ? -40.109 -19.890 26.382  1.00 17.76 ? 80  ASP B C   1 
ATOM   4323 O  O   . ASP B 1 80  ? -40.914 -18.996 26.679  1.00 18.22 ? 80  ASP B O   1 
ATOM   4324 C  CB  . ASP B 1 80  ? -39.682 -21.220 28.619  1.00 19.39 ? 80  ASP B CB  1 
ATOM   4325 C  CG  . ASP B 1 80  ? -40.007 -22.493 29.396  1.00 20.19 ? 80  ASP B CG  1 
ATOM   4326 O  OD1 . ASP B 1 80  ? -40.989 -23.209 29.034  1.00 20.45 ? 80  ASP B OD1 1 
ATOM   4327 O  OD2 . ASP B 1 80  ? -39.237 -22.802 30.341  1.00 20.42 ? 80  ASP B OD2 1 
ATOM   4328 N  N   . PHE B 1 81  ? -39.227 -19.774 25.373  1.00 16.84 ? 81  PHE B N   1 
ATOM   4329 C  CA  . PHE B 1 81  ? -39.169 -18.607 24.454  1.00 16.96 ? 81  PHE B CA  1 
ATOM   4330 C  C   . PHE B 1 81  ? -39.244 -18.975 22.955  1.00 17.31 ? 81  PHE B C   1 
ATOM   4331 O  O   . PHE B 1 81  ? -39.479 -18.054 22.149  1.00 17.40 ? 81  PHE B O   1 
ATOM   4332 C  CB  . PHE B 1 81  ? -37.939 -17.730 24.711  1.00 18.51 ? 81  PHE B CB  1 
ATOM   4333 C  CG  . PHE B 1 81  ? -36.568 -18.377 24.763  1.00 19.28 ? 81  PHE B CG  1 
ATOM   4334 C  CD1 . PHE B 1 81  ? -36.129 -19.032 25.902  1.00 19.69 ? 81  PHE B CD1 1 
ATOM   4335 C  CD2 . PHE B 1 81  ? -35.677 -18.228 23.713  1.00 20.09 ? 81  PHE B CD2 1 
ATOM   4336 C  CE1 . PHE B 1 81  ? -34.855 -19.564 25.971  1.00 19.26 ? 81  PHE B CE1 1 
ATOM   4337 C  CE2 . PHE B 1 81  ? -34.406 -18.776 23.766  1.00 19.88 ? 81  PHE B CE2 1 
ATOM   4338 C  CZ  . PHE B 1 81  ? -33.998 -19.437 24.902  1.00 20.04 ? 81  PHE B CZ  1 
ATOM   4339 N  N   . ALA B 1 82  ? -39.004 -20.209 22.529  1.00 16.59 ? 82  ALA B N   1 
ATOM   4340 C  CA  . ALA B 1 82  ? -39.099 -20.534 21.087  1.00 18.32 ? 82  ALA B CA  1 
ATOM   4341 C  C   . ALA B 1 82  ? -40.347 -21.375 20.845  1.00 18.63 ? 82  ALA B C   1 
ATOM   4342 O  O   . ALA B 1 82  ? -40.573 -21.768 19.685  1.00 19.05 ? 82  ALA B O   1 
ATOM   4343 C  CB  . ALA B 1 82  ? -37.855 -21.218 20.585  1.00 18.74 ? 82  ALA B CB  1 
ATOM   4344 N  N   . GLY B 1 83  ? -41.110 -21.623 21.911  1.00 19.87 ? 83  GLY B N   1 
ATOM   4345 C  CA  . GLY B 1 83  ? -42.484 -22.166 21.867  1.00 20.35 ? 83  GLY B CA  1 
ATOM   4346 C  C   . GLY B 1 83  ? -42.569 -23.399 20.990  1.00 20.69 ? 83  GLY B C   1 
ATOM   4347 O  O   . GLY B 1 83  ? -41.622 -24.221 21.016  1.00 22.28 ? 83  GLY B O   1 
ATOM   4348 N  N   . ASP B 1 84  ? -43.654 -23.537 20.224  1.00 20.90 ? 84  ASP B N   1 
ATOM   4349 C  CA  . ASP B 1 84  ? -43.840 -24.699 19.316  1.00 20.48 ? 84  ASP B CA  1 
ATOM   4350 C  C   . ASP B 1 84  ? -43.400 -24.290 17.905  1.00 20.17 ? 84  ASP B C   1 
ATOM   4351 O  O   . ASP B 1 84  ? -44.083 -24.709 16.937  1.00 19.01 ? 84  ASP B O   1 
ATOM   4352 C  CB  . ASP B 1 84  ? -45.261 -25.257 19.378  1.00 20.73 ? 84  ASP B CB  1 
ATOM   4353 C  CG  . ASP B 1 84  ? -46.351 -24.304 18.916  1.00 23.32 ? 84  ASP B CG  1 
ATOM   4354 O  OD1 . ASP B 1 84  ? -46.083 -23.056 18.875  1.00 21.34 ? 84  ASP B OD1 1 
ATOM   4355 O  OD2 . ASP B 1 84  ? -47.482 -24.818 18.609  1.00 24.11 ? 84  ASP B OD2 1 
ATOM   4356 N  N   . GLY B 1 85  ? -42.281 -23.555 17.801  1.00 18.84 ? 85  GLY B N   1 
ATOM   4357 C  CA  . GLY B 1 85  ? -41.550 -23.370 16.534  1.00 19.44 ? 85  GLY B CA  1 
ATOM   4358 C  C   . GLY B 1 85  ? -40.945 -24.692 16.073  1.00 19.24 ? 85  GLY B C   1 
ATOM   4359 O  O   . GLY B 1 85  ? -41.012 -25.673 16.854  1.00 21.39 ? 85  GLY B O   1 
ATOM   4360 N  N   . LEU B 1 86  ? -40.348 -24.729 14.877  1.00 18.00 ? 86  LEU B N   1 
ATOM   4361 C  CA  . LEU B 1 86  ? -39.897 -25.978 14.215  1.00 17.74 ? 86  LEU B CA  1 
ATOM   4362 C  C   . LEU B 1 86  ? -38.897 -26.743 15.085  1.00 18.48 ? 86  LEU B C   1 
ATOM   4363 O  O   . LEU B 1 86  ? -38.905 -27.972 15.039  1.00 18.99 ? 86  LEU B O   1 
ATOM   4364 C  CB  . LEU B 1 86  ? -39.266 -25.615 12.880  1.00 18.48 ? 86  LEU B CB  1 
ATOM   4365 C  CG  . LEU B 1 86  ? -40.260 -25.183 11.812  1.00 19.56 ? 86  LEU B CG  1 
ATOM   4366 C  CD1 . LEU B 1 86  ? -39.538 -24.751 10.542  1.00 20.75 ? 86  LEU B CD1 1 
ATOM   4367 C  CD2 . LEU B 1 86  ? -41.281 -26.279 11.508  1.00 20.31 ? 86  LEU B CD2 1 
ATOM   4368 N  N   . PHE B 1 87  ? -38.069 -26.019 15.837  1.00 19.66 ? 87  PHE B N   1 
ATOM   4369 C  CA  . PHE B 1 87  ? -36.880 -26.513 16.567  1.00 17.90 ? 87  PHE B CA  1 
ATOM   4370 C  C   . PHE B 1 87  ? -37.326 -27.115 17.896  1.00 18.82 ? 87  PHE B C   1 
ATOM   4371 O  O   . PHE B 1 87  ? -36.668 -28.090 18.346  1.00 19.37 ? 87  PHE B O   1 
ATOM   4372 C  CB  . PHE B 1 87  ? -35.901 -25.349 16.774  1.00 17.72 ? 87  PHE B CB  1 
ATOM   4373 C  CG  . PHE B 1 87  ? -34.616 -25.663 17.504  1.00 17.33 ? 87  PHE B CG  1 
ATOM   4374 C  CD1 . PHE B 1 87  ? -33.877 -26.798 17.214  1.00 18.77 ? 87  PHE B CD1 1 
ATOM   4375 C  CD2 . PHE B 1 87  ? -34.111 -24.795 18.448  1.00 17.93 ? 87  PHE B CD2 1 
ATOM   4376 C  CE1 . PHE B 1 87  ? -32.679 -27.073 17.855  1.00 19.29 ? 87  PHE B CE1 1 
ATOM   4377 C  CE2 . PHE B 1 87  ? -32.926 -25.081 19.111  1.00 19.04 ? 87  PHE B CE2 1 
ATOM   4378 C  CZ  . PHE B 1 87  ? -32.210 -26.219 18.817  1.00 19.30 ? 87  PHE B CZ  1 
ATOM   4379 N  N   . THR B 1 88  ? -38.355 -26.545 18.540  1.00 17.94 ? 88  THR B N   1 
ATOM   4380 C  CA  . THR B 1 88  ? -38.752 -26.936 19.933  1.00 18.19 ? 88  THR B CA  1 
ATOM   4381 C  C   . THR B 1 88  ? -40.157 -27.553 19.971  1.00 17.77 ? 88  THR B C   1 
ATOM   4382 O  O   . THR B 1 88  ? -40.704 -27.719 21.064  1.00 17.99 ? 88  THR B O   1 
ATOM   4383 C  CB  . THR B 1 88  ? -38.612 -25.748 20.892  1.00 16.87 ? 88  THR B CB  1 
ATOM   4384 O  OG1 . THR B 1 88  ? -39.219 -24.631 20.262  1.00 14.62 ? 88  THR B OG1 1 
ATOM   4385 C  CG2 . THR B 1 88  ? -37.160 -25.463 21.206  1.00 16.97 ? 88  THR B CG2 1 
ATOM   4386 N  N   . SER B 1 89  ? -40.713 -27.889 18.813  1.00 18.20 ? 89  SER B N   1 
ATOM   4387 C  CA  . SER B 1 89  ? -42.022 -28.567 18.681  1.00 18.63 ? 89  SER B CA  1 
ATOM   4388 C  C   . SER B 1 89  ? -41.779 -30.078 18.612  1.00 18.46 ? 89  SER B C   1 
ATOM   4389 O  O   . SER B 1 89  ? -40.678 -30.495 18.159  1.00 18.66 ? 89  SER B O   1 
ATOM   4390 C  CB  . SER B 1 89  ? -42.780 -28.041 17.487  1.00 18.80 ? 89  SER B CB  1 
ATOM   4391 O  OG  . SER B 1 89  ? -42.126 -28.382 16.279  1.00 18.81 ? 89  SER B OG  1 
ATOM   4392 N  N   . TRP B 1 90  ? -42.735 -30.871 19.097  1.00 17.08 ? 90  TRP B N   1 
ATOM   4393 C  CA  . TRP B 1 90  ? -42.746 -32.336 18.871  1.00 17.40 ? 90  TRP B CA  1 
ATOM   4394 C  C   . TRP B 1 90  ? -43.238 -32.594 17.442  1.00 17.19 ? 90  TRP B C   1 
ATOM   4395 O  O   . TRP B 1 90  ? -44.078 -31.801 16.963  1.00 16.71 ? 90  TRP B O   1 
ATOM   4396 C  CB  . TRP B 1 90  ? -43.670 -33.010 19.875  1.00 17.36 ? 90  TRP B CB  1 
ATOM   4397 C  CG  . TRP B 1 90  ? -43.289 -32.778 21.291  1.00 17.57 ? 90  TRP B CG  1 
ATOM   4398 C  CD1 . TRP B 1 90  ? -43.725 -31.781 22.111  1.00 18.75 ? 90  TRP B CD1 1 
ATOM   4399 C  CD2 . TRP B 1 90  ? -42.377 -33.574 22.058  1.00 18.88 ? 90  TRP B CD2 1 
ATOM   4400 N  NE1 . TRP B 1 90  ? -43.126 -31.884 23.344  1.00 20.02 ? 90  TRP B NE1 1 
ATOM   4401 C  CE2 . TRP B 1 90  ? -42.318 -32.998 23.352  1.00 19.36 ? 90  TRP B CE2 1 
ATOM   4402 C  CE3 . TRP B 1 90  ? -41.610 -34.714 21.781  1.00 19.14 ? 90  TRP B CE3 1 
ATOM   4403 C  CZ2 . TRP B 1 90  ? -41.519 -33.529 24.363  1.00 18.28 ? 90  TRP B CZ2 1 
ATOM   4404 C  CZ3 . TRP B 1 90  ? -40.824 -35.240 22.783  1.00 19.60 ? 90  TRP B CZ3 1 
ATOM   4405 C  CH2 . TRP B 1 90  ? -40.794 -34.661 24.057  1.00 19.02 ? 90  TRP B CH2 1 
ATOM   4406 N  N   . THR B 1 91  ? -42.767 -33.669 16.816  1.00 17.71 ? 91  THR B N   1 
ATOM   4407 C  CA  . THR B 1 91  ? -43.155 -34.138 15.456  1.00 19.84 ? 91  THR B CA  1 
ATOM   4408 C  C   . THR B 1 91  ? -44.695 -34.289 15.330  1.00 21.78 ? 91  THR B C   1 
ATOM   4409 O  O   . THR B 1 91  ? -45.222 -33.938 14.251  1.00 23.79 ? 91  THR B O   1 
ATOM   4410 C  CB  . THR B 1 91  ? -42.352 -35.410 15.124  1.00 21.01 ? 91  THR B CB  1 
ATOM   4411 O  OG1 . THR B 1 91  ? -40.998 -35.217 15.569  1.00 20.11 ? 91  THR B OG1 1 
ATOM   4412 C  CG2 . THR B 1 91  ? -42.378 -35.767 13.649  1.00 20.64 ? 91  THR B CG2 1 
ATOM   4413 N  N   . HIS B 1 92  ? -45.402 -34.745 16.380  1.00 22.30 ? 92  HIS B N   1 
ATOM   4414 C  CA  . HIS B 1 92  ? -46.860 -35.087 16.401  1.00 21.61 ? 92  HIS B CA  1 
ATOM   4415 C  C   . HIS B 1 92  ? -47.742 -33.877 16.743  1.00 20.99 ? 92  HIS B C   1 
ATOM   4416 O  O   . HIS B 1 92  ? -49.009 -34.026 16.729  1.00 21.04 ? 92  HIS B O   1 
ATOM   4417 C  CB  . HIS B 1 92  ? -47.139 -36.192 17.437  1.00 22.19 ? 92  HIS B CB  1 
ATOM   4418 C  CG  . HIS B 1 92  ? -46.567 -35.896 18.786  1.00 22.36 ? 92  HIS B CG  1 
ATOM   4419 N  ND1 . HIS B 1 92  ? -47.121 -34.965 19.637  1.00 21.68 ? 92  HIS B ND1 1 
ATOM   4420 C  CD2 . HIS B 1 92  ? -45.473 -36.372 19.426  1.00 22.93 ? 92  HIS B CD2 1 
ATOM   4421 C  CE1 . HIS B 1 92  ? -46.424 -34.910 20.765  1.00 20.52 ? 92  HIS B CE1 1 
ATOM   4422 N  NE2 . HIS B 1 92  ? -45.407 -35.767 20.667  1.00 21.20 ? 92  HIS B NE2 1 
ATOM   4423 N  N   . GLU B 1 93  ? -47.131 -32.747 17.105  1.00 20.93 ? 93  GLU B N   1 
ATOM   4424 C  CA  . GLU B 1 93  ? -47.858 -31.472 17.337  1.00 21.58 ? 93  GLU B CA  1 
ATOM   4425 C  C   . GLU B 1 93  ? -48.283 -30.929 15.970  1.00 22.46 ? 93  GLU B C   1 
ATOM   4426 O  O   . GLU B 1 93  ? -47.437 -30.950 15.023  1.00 18.16 ? 93  GLU B O   1 
ATOM   4427 C  CB  . GLU B 1 93  ? -47.009 -30.431 18.052  1.00 21.17 ? 93  GLU B CB  1 
ATOM   4428 C  CG  . GLU B 1 93  ? -47.063 -30.540 19.557  1.00 22.07 ? 93  GLU B CG  1 
ATOM   4429 C  CD  . GLU B 1 93  ? -46.278 -29.446 20.243  1.00 22.70 ? 93  GLU B CD  1 
ATOM   4430 O  OE1 . GLU B 1 93  ? -45.072 -29.315 19.970  1.00 25.12 ? 93  GLU B OE1 1 
ATOM   4431 O  OE2 . GLU B 1 93  ? -46.883 -28.705 21.013  1.00 25.23 ? 93  GLU B OE2 1 
ATOM   4432 N  N   . LYS B 1 94  ? -49.541 -30.475 15.876  1.00 23.36 ? 94  LYS B N   1 
ATOM   4433 C  CA  . LYS B 1 94  ? -50.120 -29.941 14.612  1.00 24.15 ? 94  LYS B CA  1 
ATOM   4434 C  C   . LYS B 1 94  ? -49.173 -28.901 14.014  1.00 20.63 ? 94  LYS B C   1 
ATOM   4435 O  O   . LYS B 1 94  ? -49.013 -28.888 12.790  1.00 17.69 ? 94  LYS B O   1 
ATOM   4436 C  CB  . LYS B 1 94  ? -51.491 -29.296 14.835  1.00 27.10 ? 94  LYS B CB  1 
ATOM   4437 C  CG  . LYS B 1 94  ? -52.313 -29.096 13.567  1.00 27.46 ? 94  LYS B CG  1 
ATOM   4438 C  CD  . LYS B 1 94  ? -53.479 -28.193 13.797  1.00 30.62 ? 94  LYS B CD  1 
ATOM   4439 C  CE  . LYS B 1 94  ? -54.355 -28.004 12.582  1.00 35.59 ? 94  LYS B CE  1 
ATOM   4440 N  NZ  . LYS B 1 94  ? -55.675 -27.432 12.970  1.00 38.77 ? 94  LYS B NZ  1 
ATOM   4441 N  N   . ASN B 1 95  ? -48.601 -28.037 14.846  1.00 19.83 ? 95  ASN B N   1 
ATOM   4442 C  CA  . ASN B 1 95  ? -47.882 -26.851 14.325  1.00 19.75 ? 95  ASN B CA  1 
ATOM   4443 C  C   . ASN B 1 95  ? -46.557 -27.277 13.685  1.00 19.30 ? 95  ASN B C   1 
ATOM   4444 O  O   . ASN B 1 95  ? -46.058 -26.498 12.865  1.00 19.46 ? 95  ASN B O   1 
ATOM   4445 C  CB  . ASN B 1 95  ? -47.734 -25.779 15.398  1.00 20.50 ? 95  ASN B CB  1 
ATOM   4446 C  CG  . ASN B 1 95  ? -48.870 -24.779 15.381  1.00 19.95 ? 95  ASN B CG  1 
ATOM   4447 O  OD1 . ASN B 1 95  ? -49.548 -24.629 14.382  1.00 21.70 ? 95  ASN B OD1 1 
ATOM   4448 N  ND2 . ASN B 1 95  ? -49.071 -24.072 16.475  1.00 20.49 ? 95  ASN B ND2 1 
ATOM   4449 N  N   . TRP B 1 96  ? -46.001 -28.452 14.013  1.00 19.05 ? 96  TRP B N   1 
ATOM   4450 C  CA  . TRP B 1 96  ? -44.733 -28.891 13.387  1.00 18.64 ? 96  TRP B CA  1 
ATOM   4451 C  C   . TRP B 1 96  ? -44.969 -29.072 11.875  1.00 20.36 ? 96  TRP B C   1 
ATOM   4452 O  O   . TRP B 1 96  ? -44.260 -28.398 11.080  1.00 19.84 ? 96  TRP B O   1 
ATOM   4453 C  CB  . TRP B 1 96  ? -44.077 -30.143 14.021  1.00 18.05 ? 96  TRP B CB  1 
ATOM   4454 C  CG  . TRP B 1 96  ? -42.836 -30.447 13.232  1.00 16.72 ? 96  TRP B CG  1 
ATOM   4455 C  CD1 . TRP B 1 96  ? -41.673 -29.730 13.262  1.00 16.65 ? 96  TRP B CD1 1 
ATOM   4456 C  CD2 . TRP B 1 96  ? -42.720 -31.361 12.123  1.00 16.39 ? 96  TRP B CD2 1 
ATOM   4457 N  NE1 . TRP B 1 96  ? -40.811 -30.192 12.306  1.00 17.35 ? 96  TRP B NE1 1 
ATOM   4458 C  CE2 . TRP B 1 96  ? -41.437 -31.166 11.566  1.00 17.26 ? 96  TRP B CE2 1 
ATOM   4459 C  CE3 . TRP B 1 96  ? -43.555 -32.339 11.561  1.00 15.68 ? 96  TRP B CE3 1 
ATOM   4460 C  CZ2 . TRP B 1 96  ? -40.988 -31.910 10.468  1.00 16.54 ? 96  TRP B CZ2 1 
ATOM   4461 C  CZ3 . TRP B 1 96  ? -43.100 -33.087 10.507  1.00 15.38 ? 96  TRP B CZ3 1 
ATOM   4462 C  CH2 . TRP B 1 96  ? -41.842 -32.859 9.953   1.00 15.89 ? 96  TRP B CH2 1 
ATOM   4463 N  N   . LYS B 1 97  ? -45.891 -29.958 11.476  1.00 23.27 ? 97  LYS B N   1 
ATOM   4464 C  CA  . LYS B 1 97  ? -46.069 -30.341 10.047  1.00 25.70 ? 97  LYS B CA  1 
ATOM   4465 C  C   . LYS B 1 97  ? -46.629 -29.139 9.275   1.00 25.28 ? 97  LYS B C   1 
ATOM   4466 O  O   . LYS B 1 97  ? -46.193 -28.924 8.117   1.00 26.65 ? 97  LYS B O   1 
ATOM   4467 C  CB  . LYS B 1 97  ? -46.962 -31.574 9.873   1.00 27.62 ? 97  LYS B CB  1 
ATOM   4468 C  CG  . LYS B 1 97  ? -47.073 -32.055 8.420   1.00 28.61 ? 97  LYS B CG  1 
ATOM   4469 C  CD  . LYS B 1 97  ? -46.015 -33.052 8.004   1.00 30.57 ? 97  LYS B CD  1 
ATOM   4470 C  CE  . LYS B 1 97  ? -45.622 -32.942 6.543   1.00 33.71 ? 97  LYS B CE  1 
ATOM   4471 N  NZ  . LYS B 1 97  ? -45.221 -34.241 5.960   1.00 32.87 ? 97  LYS B NZ  1 
ATOM   4472 N  N   . LYS B 1 98  ? -47.510 -28.368 9.913   1.00 22.26 ? 98  LYS B N   1 
ATOM   4473 C  CA  . LYS B 1 98  ? -48.053 -27.090 9.388   1.00 24.09 ? 98  LYS B CA  1 
ATOM   4474 C  C   . LYS B 1 98  ? -46.908 -26.139 9.006   1.00 22.79 ? 98  LYS B C   1 
ATOM   4475 O  O   . LYS B 1 98  ? -46.785 -25.799 7.806   1.00 19.77 ? 98  LYS B O   1 
ATOM   4476 C  CB  . LYS B 1 98  ? -48.944 -26.449 10.455  1.00 24.94 ? 98  LYS B CB  1 
ATOM   4477 C  CG  . LYS B 1 98  ? -49.726 -25.242 9.984   1.00 27.19 ? 98  LYS B CG  1 
ATOM   4478 C  CD  . LYS B 1 98  ? -51.087 -25.113 10.645  1.00 29.34 ? 98  LYS B CD  1 
ATOM   4479 C  CE  . LYS B 1 98  ? -51.095 -24.150 11.809  1.00 31.29 ? 98  LYS B CE  1 
ATOM   4480 N  NZ  . LYS B 1 98  ? -52.396 -23.452 11.896  1.00 32.62 ? 98  LYS B NZ  1 
ATOM   4481 N  N   . ALA B 1 99  ? -46.097 -25.737 9.994   1.00 21.50 ? 99  ALA B N   1 
ATOM   4482 C  CA  . ALA B 1 99  ? -44.973 -24.798 9.807   1.00 21.10 ? 99  ALA B CA  1 
ATOM   4483 C  C   . ALA B 1 99  ? -43.992 -25.408 8.806   1.00 21.29 ? 99  ALA B C   1 
ATOM   4484 O  O   . ALA B 1 99  ? -43.530 -24.668 7.929   1.00 19.41 ? 99  ALA B O   1 
ATOM   4485 C  CB  . ALA B 1 99  ? -44.315 -24.502 11.118  1.00 21.31 ? 99  ALA B CB  1 
ATOM   4486 N  N   . HIS B 1 100 ? -43.733 -26.720 8.907   1.00 21.89 ? 100 HIS B N   1 
ATOM   4487 C  CA  . HIS B 1 100 ? -42.769 -27.435 8.026   1.00 23.12 ? 100 HIS B CA  1 
ATOM   4488 C  C   . HIS B 1 100 ? -43.243 -27.298 6.580   1.00 22.04 ? 100 HIS B C   1 
ATOM   4489 O  O   . HIS B 1 100 ? -42.443 -26.858 5.716   1.00 20.21 ? 100 HIS B O   1 
ATOM   4490 C  CB  . HIS B 1 100 ? -42.588 -28.905 8.410   1.00 24.55 ? 100 HIS B CB  1 
ATOM   4491 C  CG  . HIS B 1 100 ? -41.687 -29.607 7.455   1.00 28.30 ? 100 HIS B CG  1 
ATOM   4492 N  ND1 . HIS B 1 100 ? -40.311 -29.682 7.648   1.00 27.53 ? 100 HIS B ND1 1 
ATOM   4493 C  CD2 . HIS B 1 100 ? -41.955 -30.204 6.272   1.00 30.91 ? 100 HIS B CD2 1 
ATOM   4494 C  CE1 . HIS B 1 100 ? -39.779 -30.325 6.630   1.00 33.26 ? 100 HIS B CE1 1 
ATOM   4495 N  NE2 . HIS B 1 100 ? -40.774 -30.655 5.763   1.00 32.94 ? 100 HIS B NE2 1 
ATOM   4496 N  N   . ASN B 1 101 ? -44.527 -27.586 6.361   1.00 20.54 ? 101 ASN B N   1 
ATOM   4497 C  CA  . ASN B 1 101 ? -45.126 -27.615 5.013   1.00 20.65 ? 101 ASN B CA  1 
ATOM   4498 C  C   . ASN B 1 101 ? -45.038 -26.214 4.410   1.00 19.49 ? 101 ASN B C   1 
ATOM   4499 O  O   . ASN B 1 101 ? -44.663 -26.124 3.262   1.00 18.35 ? 101 ASN B O   1 
ATOM   4500 C  CB  . ASN B 1 101 ? -46.539 -28.187 5.081   1.00 21.59 ? 101 ASN B CB  1 
ATOM   4501 C  CG  . ASN B 1 101 ? -46.568 -29.693 5.173   1.00 18.34 ? 101 ASN B CG  1 
ATOM   4502 O  OD1 . ASN B 1 101 ? -45.557 -30.343 4.970   1.00 20.65 ? 101 ASN B OD1 1 
ATOM   4503 N  ND2 . ASN B 1 101 ? -47.728 -30.246 5.457   1.00 18.41 ? 101 ASN B ND2 1 
ATOM   4504 N  N   . ILE B 1 102 ? -45.265 -25.170 5.209   1.00 20.54 ? 102 ILE B N   1 
ATOM   4505 C  CA  . ILE B 1 102 ? -45.279 -23.741 4.750   1.00 20.53 ? 102 ILE B CA  1 
ATOM   4506 C  C   . ILE B 1 102 ? -43.852 -23.224 4.496   1.00 20.15 ? 102 ILE B C   1 
ATOM   4507 O  O   . ILE B 1 102 ? -43.653 -22.479 3.522   1.00 20.24 ? 102 ILE B O   1 
ATOM   4508 C  CB  . ILE B 1 102 ? -46.040 -22.853 5.763   1.00 20.73 ? 102 ILE B CB  1 
ATOM   4509 C  CG1 . ILE B 1 102 ? -47.530 -23.227 5.847   1.00 19.89 ? 102 ILE B CG1 1 
ATOM   4510 C  CG2 . ILE B 1 102 ? -45.850 -21.378 5.415   1.00 21.66 ? 102 ILE B CG2 1 
ATOM   4511 C  CD1 . ILE B 1 102 ? -48.297 -22.625 7.039   1.00 18.25 ? 102 ILE B CD1 1 
ATOM   4512 N  N   . LEU B 1 103 ? -42.884 -23.597 5.334   1.00 20.57 ? 103 LEU B N   1 
ATOM   4513 C  CA  . LEU B 1 103 ? -41.504 -23.023 5.296   1.00 19.99 ? 103 LEU B CA  1 
ATOM   4514 C  C   . LEU B 1 103 ? -40.607 -23.796 4.317   1.00 20.21 ? 103 LEU B C   1 
ATOM   4515 O  O   . LEU B 1 103 ? -39.653 -23.191 3.840   1.00 21.54 ? 103 LEU B O   1 
ATOM   4516 C  CB  . LEU B 1 103 ? -40.905 -22.976 6.714   1.00 19.14 ? 103 LEU B CB  1 
ATOM   4517 C  CG  . LEU B 1 103 ? -41.490 -21.910 7.647   1.00 20.08 ? 103 LEU B CG  1 
ATOM   4518 C  CD1 . LEU B 1 103 ? -40.987 -22.082 9.080   1.00 21.85 ? 103 LEU B CD1 1 
ATOM   4519 C  CD2 . LEU B 1 103 ? -41.199 -20.494 7.144   1.00 20.82 ? 103 LEU B CD2 1 
ATOM   4520 N  N   . LEU B 1 104 ? -40.886 -25.056 3.988   1.00 20.37 ? 104 LEU B N   1 
ATOM   4521 C  CA  . LEU B 1 104 ? -40.020 -25.824 3.047   1.00 21.84 ? 104 LEU B CA  1 
ATOM   4522 C  C   . LEU B 1 104 ? -39.769 -25.011 1.766   1.00 21.28 ? 104 LEU B C   1 
ATOM   4523 O  O   . LEU B 1 104 ? -38.614 -24.841 1.378   1.00 19.92 ? 104 LEU B O   1 
ATOM   4524 C  CB  . LEU B 1 104 ? -40.619 -27.210 2.776   1.00 23.17 ? 104 LEU B CB  1 
ATOM   4525 C  CG  . LEU B 1 104 ? -39.733 -28.151 1.955   1.00 24.82 ? 104 LEU B CG  1 
ATOM   4526 C  CD1 . LEU B 1 104 ? -38.566 -28.672 2.790   1.00 26.75 ? 104 LEU B CD1 1 
ATOM   4527 C  CD2 . LEU B 1 104 ? -40.529 -29.315 1.381   1.00 24.03 ? 104 LEU B CD2 1 
ATOM   4528 N  N   . PRO B 1 105 ? -40.787 -24.451 1.064   1.00 21.96 ? 105 PRO B N   1 
ATOM   4529 C  CA  . PRO B 1 105 ? -40.534 -23.696 -0.164  1.00 22.10 ? 105 PRO B CA  1 
ATOM   4530 C  C   . PRO B 1 105 ? -39.689 -22.444 0.107   1.00 22.17 ? 105 PRO B C   1 
ATOM   4531 O  O   . PRO B 1 105 ? -39.036 -21.994 -0.805  1.00 21.30 ? 105 PRO B O   1 
ATOM   4532 C  CB  . PRO B 1 105 ? -41.886 -23.305 -0.750  1.00 20.19 ? 105 PRO B CB  1 
ATOM   4533 C  CG  . PRO B 1 105 ? -42.916 -23.817 0.222   1.00 21.48 ? 105 PRO B CG  1 
ATOM   4534 C  CD  . PRO B 1 105 ? -42.223 -24.564 1.341   1.00 22.56 ? 105 PRO B CD  1 
ATOM   4535 N  N   . SER B 1 106 ? -39.691 -21.958 1.346   1.00 22.20 ? 106 SER B N   1 
ATOM   4536 C  CA  . SER B 1 106 ? -38.864 -20.813 1.797   1.00 24.06 ? 106 SER B CA  1 
ATOM   4537 C  C   . SER B 1 106 ? -37.373 -21.184 1.762   1.00 22.76 ? 106 SER B C   1 
ATOM   4538 O  O   . SER B 1 106 ? -36.573 -20.279 1.857   1.00 25.34 ? 106 SER B O   1 
ATOM   4539 C  CB  . SER B 1 106 ? -39.278 -20.326 3.185   1.00 25.09 ? 106 SER B CB  1 
ATOM   4540 O  OG  . SER B 1 106 ? -40.605 -19.851 3.205   1.00 24.81 ? 106 SER B OG  1 
ATOM   4541 N  N   . PHE B 1 107 ? -37.009 -22.462 1.668   1.00 24.50 ? 107 PHE B N   1 
ATOM   4542 C  CA  . PHE B 1 107 ? -35.601 -22.936 1.711   1.00 25.28 ? 107 PHE B CA  1 
ATOM   4543 C  C   . PHE B 1 107 ? -35.178 -23.601 0.394   1.00 28.20 ? 107 PHE B C   1 
ATOM   4544 O  O   . PHE B 1 107 ? -34.154 -24.267 0.337   1.00 32.47 ? 107 PHE B O   1 
ATOM   4545 C  CB  . PHE B 1 107 ? -35.481 -23.813 2.941   1.00 24.30 ? 107 PHE B CB  1 
ATOM   4546 C  CG  . PHE B 1 107 ? -35.595 -23.002 4.200   1.00 24.32 ? 107 PHE B CG  1 
ATOM   4547 C  CD1 . PHE B 1 107 ? -34.581 -22.139 4.577   1.00 24.79 ? 107 PHE B CD1 1 
ATOM   4548 C  CD2 . PHE B 1 107 ? -36.712 -23.085 5.004   1.00 24.34 ? 107 PHE B CD2 1 
ATOM   4549 C  CE1 . PHE B 1 107 ? -34.679 -21.402 5.749   1.00 24.64 ? 107 PHE B CE1 1 
ATOM   4550 C  CE2 . PHE B 1 107 ? -36.809 -22.348 6.171   1.00 23.22 ? 107 PHE B CE2 1 
ATOM   4551 C  CZ  . PHE B 1 107 ? -35.797 -21.508 6.542   1.00 24.48 ? 107 PHE B CZ  1 
ATOM   4552 N  N   . SER B 1 108 ? -35.936 -23.346 -0.664  1.00 33.87 ? 108 SER B N   1 
ATOM   4553 C  CA  . SER B 1 108 ? -35.726 -23.844 -2.046  1.00 33.53 ? 108 SER B CA  1 
ATOM   4554 C  C   . SER B 1 108 ? -34.809 -22.887 -2.818  1.00 35.25 ? 108 SER B C   1 
ATOM   4555 O  O   . SER B 1 108 ? -34.809 -21.661 -2.531  1.00 32.36 ? 108 SER B O   1 
ATOM   4556 C  CB  . SER B 1 108 ? -37.042 -23.932 -2.757  1.00 33.61 ? 108 SER B CB  1 
ATOM   4557 O  OG  . SER B 1 108 ? -37.437 -22.621 -3.166  1.00 33.90 ? 108 SER B OG  1 
ATOM   4558 N  N   . GLN B 1 109 ? -34.150 -23.426 -3.840  1.00 35.61 ? 109 GLN B N   1 
ATOM   4559 C  CA  . GLN B 1 109 ? -33.198 -22.702 -4.705  1.00 35.96 ? 109 GLN B CA  1 
ATOM   4560 C  C   . GLN B 1 109 ? -33.794 -21.348 -5.111  1.00 35.82 ? 109 GLN B C   1 
ATOM   4561 O  O   . GLN B 1 109 ? -33.090 -20.334 -5.021  1.00 32.77 ? 109 GLN B O   1 
ATOM   4562 C  CB  . GLN B 1 109 ? -32.876 -23.586 -5.903  1.00 40.86 ? 109 GLN B CB  1 
ATOM   4563 C  CG  . GLN B 1 109 ? -32.106 -24.846 -5.527  1.00 43.43 ? 109 GLN B CG  1 
ATOM   4564 C  CD  . GLN B 1 109 ? -31.558 -25.551 -6.746  1.00 49.58 ? 109 GLN B CD  1 
ATOM   4565 O  OE1 . GLN B 1 109 ? -31.241 -24.929 -7.766  1.00 44.90 ? 109 GLN B OE1 1 
ATOM   4566 N  NE2 . GLN B 1 109 ? -31.452 -26.870 -6.648  1.00 50.75 ? 109 GLN B NE2 1 
ATOM   4567 N  N   . GLN B 1 110 ? -35.051 -21.312 -5.533  1.00 38.22 ? 110 GLN B N   1 
ATOM   4568 C  CA  . GLN B 1 110 ? -35.684 -20.045 -5.971  1.00 42.29 ? 110 GLN B CA  1 
ATOM   4569 C  C   . GLN B 1 110 ? -35.649 -19.035 -4.818  1.00 44.89 ? 110 GLN B C   1 
ATOM   4570 O  O   . GLN B 1 110 ? -35.532 -17.831 -5.097  1.00 44.12 ? 110 GLN B O   1 
ATOM   4571 C  CB  . GLN B 1 110 ? -37.125 -20.280 -6.408  1.00 47.50 ? 110 GLN B CB  1 
ATOM   4572 C  CG  . GLN B 1 110 ? -37.751 -19.060 -7.064  1.00 50.28 ? 110 GLN B CG  1 
ATOM   4573 C  CD  . GLN B 1 110 ? -38.727 -19.503 -8.126  1.00 56.48 ? 110 GLN B CD  1 
ATOM   4574 O  OE1 . GLN B 1 110 ? -38.354 -20.159 -9.102  1.00 51.71 ? 110 GLN B OE1 1 
ATOM   4575 N  NE2 . GLN B 1 110 ? -39.992 -19.158 -7.938  1.00 58.76 ? 110 GLN B NE2 1 
ATOM   4576 N  N   . ALA B 1 111 ? -35.799 -19.522 -3.579  1.00 46.05 ? 111 ALA B N   1 
ATOM   4577 C  CA  . ALA B 1 111 ? -35.734 -18.732 -2.324  1.00 39.88 ? 111 ALA B CA  1 
ATOM   4578 C  C   . ALA B 1 111 ? -34.283 -18.307 -2.071  1.00 33.29 ? 111 ALA B C   1 
ATOM   4579 O  O   . ALA B 1 111 ? -34.027 -17.094 -1.782  1.00 31.83 ? 111 ALA B O   1 
ATOM   4580 C  CB  . ALA B 1 111 ? -36.278 -19.554 -1.180  1.00 39.31 ? 111 ALA B CB  1 
ATOM   4581 N  N   . MET B 1 112 ? -33.368 -19.264 -2.197  1.00 29.31 ? 112 MET B N   1 
ATOM   4582 C  CA  . MET B 1 112 ? -31.919 -19.062 -1.920  1.00 29.71 ? 112 MET B CA  1 
ATOM   4583 C  C   . MET B 1 112 ? -31.296 -18.093 -2.937  1.00 30.59 ? 112 MET B C   1 
ATOM   4584 O  O   . MET B 1 112 ? -30.393 -17.333 -2.534  1.00 26.81 ? 112 MET B O   1 
ATOM   4585 C  CB  . MET B 1 112 ? -31.170 -20.388 -1.963  1.00 29.17 ? 112 MET B CB  1 
ATOM   4586 C  CG  . MET B 1 112 ? -30.110 -20.476 -0.904  1.00 30.88 ? 112 MET B CG  1 
ATOM   4587 S  SD  . MET B 1 112 ? -30.784 -20.551 0.789   1.00 28.89 ? 112 MET B SD  1 
ATOM   4588 C  CE  . MET B 1 112 ? -31.398 -22.234 0.823   1.00 30.93 ? 112 MET B CE  1 
ATOM   4589 N  N   . LYS B 1 113 ? -31.731 -18.125 -4.207  1.00 31.79 ? 113 LYS B N   1 
ATOM   4590 C  CA  . LYS B 1 113 ? -31.299 -17.138 -5.234  1.00 30.82 ? 113 LYS B CA  1 
ATOM   4591 C  C   . LYS B 1 113 ? -31.807 -15.770 -4.761  1.00 30.88 ? 113 LYS B C   1 
ATOM   4592 O  O   . LYS B 1 113 ? -31.084 -14.740 -4.960  1.00 32.49 ? 113 LYS B O   1 
ATOM   4593 C  CB  . LYS B 1 113 ? -31.791 -17.522 -6.636  1.00 32.67 ? 113 LYS B CB  1 
ATOM   4594 C  CG  . LYS B 1 113 ? -31.123 -18.745 -7.257  1.00 34.06 ? 113 LYS B CG  1 
ATOM   4595 C  CD  . LYS B 1 113 ? -32.047 -19.690 -8.054  1.00 37.44 ? 113 LYS B CD  1 
ATOM   4596 C  CE  . LYS B 1 113 ? -31.861 -19.681 -9.565  1.00 40.66 ? 113 LYS B CE  1 
ATOM   4597 N  NZ  . LYS B 1 113 ? -32.167 -21.017 -10.147 1.00 41.79 ? 113 LYS B NZ  1 
ATOM   4598 N  N   . GLY B 1 114 ? -32.967 -15.768 -4.091  1.00 26.63 ? 114 GLY B N   1 
ATOM   4599 C  CA  . GLY B 1 114 ? -33.586 -14.565 -3.502  1.00 24.62 ? 114 GLY B CA  1 
ATOM   4600 C  C   . GLY B 1 114 ? -32.821 -14.038 -2.314  1.00 24.32 ? 114 GLY B C   1 
ATOM   4601 O  O   . GLY B 1 114 ? -32.605 -12.825 -2.278  1.00 28.40 ? 114 GLY B O   1 
ATOM   4602 N  N   . TYR B 1 115 ? -32.429 -14.907 -1.375  1.00 21.85 ? 115 TYR B N   1 
ATOM   4603 C  CA  . TYR B 1 115 ? -31.667 -14.534 -0.148  1.00 20.97 ? 115 TYR B CA  1 
ATOM   4604 C  C   . TYR B 1 115 ? -30.202 -14.149 -0.452  1.00 19.37 ? 115 TYR B C   1 
ATOM   4605 O  O   . TYR B 1 115 ? -29.593 -13.357 0.328   1.00 16.64 ? 115 TYR B O   1 
ATOM   4606 C  CB  . TYR B 1 115 ? -31.651 -15.694 0.854   1.00 22.01 ? 115 TYR B CB  1 
ATOM   4607 C  CG  . TYR B 1 115 ? -32.999 -16.202 1.297   1.00 23.29 ? 115 TYR B CG  1 
ATOM   4608 C  CD1 . TYR B 1 115 ? -34.013 -15.336 1.665   1.00 22.69 ? 115 TYR B CD1 1 
ATOM   4609 C  CD2 . TYR B 1 115 ? -33.247 -17.564 1.381   1.00 23.69 ? 115 TYR B CD2 1 
ATOM   4610 C  CE1 . TYR B 1 115 ? -35.253 -15.811 2.067   1.00 24.21 ? 115 TYR B CE1 1 
ATOM   4611 C  CE2 . TYR B 1 115 ? -34.470 -18.056 1.811   1.00 23.54 ? 115 TYR B CE2 1 
ATOM   4612 C  CZ  . TYR B 1 115 ? -35.474 -17.175 2.164   1.00 23.35 ? 115 TYR B CZ  1 
ATOM   4613 O  OH  . TYR B 1 115 ? -36.685 -17.641 2.571   1.00 22.98 ? 115 TYR B OH  1 
ATOM   4614 N  N   . HIS B 1 116 ? -29.635 -14.740 -1.508  1.00 18.18 ? 116 HIS B N   1 
ATOM   4615 C  CA  . HIS B 1 116 ? -28.221 -14.600 -1.928  1.00 18.73 ? 116 HIS B CA  1 
ATOM   4616 C  C   . HIS B 1 116 ? -27.843 -13.118 -1.998  1.00 18.95 ? 116 HIS B C   1 
ATOM   4617 O  O   . HIS B 1 116 ? -26.742 -12.732 -1.584  1.00 19.27 ? 116 HIS B O   1 
ATOM   4618 C  CB  . HIS B 1 116 ? -27.970 -15.303 -3.276  1.00 18.39 ? 116 HIS B CB  1 
ATOM   4619 C  CG  . HIS B 1 116 ? -26.617 -14.976 -3.817  1.00 18.31 ? 116 HIS B CG  1 
ATOM   4620 N  ND1 . HIS B 1 116 ? -25.492 -15.740 -3.524  1.00 17.78 ? 116 HIS B ND1 1 
ATOM   4621 C  CD2 . HIS B 1 116 ? -26.184 -13.894 -4.501  1.00 17.61 ? 116 HIS B CD2 1 
ATOM   4622 C  CE1 . HIS B 1 116 ? -24.440 -15.156 -4.051  1.00 17.93 ? 116 HIS B CE1 1 
ATOM   4623 N  NE2 . HIS B 1 116 ? -24.847 -14.040 -4.677  1.00 17.67 ? 116 HIS B NE2 1 
ATOM   4624 N  N   . ALA B 1 117 ? -28.728 -12.320 -2.553  1.00 19.95 ? 117 ALA B N   1 
ATOM   4625 C  CA  . ALA B 1 117 ? -28.561 -10.862 -2.669  1.00 20.61 ? 117 ALA B CA  1 
ATOM   4626 C  C   . ALA B 1 117 ? -28.388 -10.286 -1.266  1.00 22.17 ? 117 ALA B C   1 
ATOM   4627 O  O   . ALA B 1 117 ? -27.584 -9.355  -1.112  1.00 22.63 ? 117 ALA B O   1 
ATOM   4628 C  CB  . ALA B 1 117 ? -29.756 -10.278 -3.361  1.00 19.85 ? 117 ALA B CB  1 
ATOM   4629 N  N   . MET B 1 118 ? -29.102 -10.811 -0.272  1.00 23.98 ? 118 MET B N   1 
ATOM   4630 C  CA  . MET B 1 118 ? -29.016 -10.257 1.106   1.00 25.49 ? 118 MET B CA  1 
ATOM   4631 C  C   . MET B 1 118 ? -27.764 -10.800 1.808   1.00 22.86 ? 118 MET B C   1 
ATOM   4632 O  O   . MET B 1 118 ? -27.130 -10.029 2.549   1.00 21.41 ? 118 MET B O   1 
ATOM   4633 C  CB  . MET B 1 118 ? -30.300 -10.533 1.889   1.00 29.51 ? 118 MET B CB  1 
ATOM   4634 C  CG  . MET B 1 118 ? -31.438 -9.596  1.450   1.00 34.60 ? 118 MET B CG  1 
ATOM   4635 S  SD  . MET B 1 118 ? -32.974 -9.914  2.369   1.00 49.16 ? 118 MET B SD  1 
ATOM   4636 C  CE  . MET B 1 118 ? -33.311 -11.604 1.877   1.00 41.72 ? 118 MET B CE  1 
ATOM   4637 N  N   . MET B 1 119 ? -27.374 -12.046 1.534   1.00 22.33 ? 119 MET B N   1 
ATOM   4638 C  CA  . MET B 1 119 ? -26.152 -12.649 2.117   1.00 22.72 ? 119 MET B CA  1 
ATOM   4639 C  C   . MET B 1 119 ? -24.936 -11.844 1.642   1.00 21.79 ? 119 MET B C   1 
ATOM   4640 O  O   . MET B 1 119 ? -24.090 -11.488 2.492   1.00 20.46 ? 119 MET B O   1 
ATOM   4641 C  CB  . MET B 1 119 ? -26.017 -14.119 1.712   1.00 25.40 ? 119 MET B CB  1 
ATOM   4642 C  CG  . MET B 1 119 ? -27.059 -15.023 2.370   1.00 26.55 ? 119 MET B CG  1 
ATOM   4643 S  SD  . MET B 1 119 ? -27.072 -16.725 1.744   1.00 27.50 ? 119 MET B SD  1 
ATOM   4644 C  CE  . MET B 1 119 ? -28.612 -17.306 2.444   1.00 26.61 ? 119 MET B CE  1 
ATOM   4645 N  N   . VAL B 1 120 ? -24.912 -11.484 0.358   1.00 20.74 ? 120 VAL B N   1 
ATOM   4646 C  CA  . VAL B 1 120 ? -23.747 -10.829 -0.305  1.00 22.01 ? 120 VAL B CA  1 
ATOM   4647 C  C   . VAL B 1 120 ? -23.663 -9.393  0.216   1.00 20.23 ? 120 VAL B C   1 
ATOM   4648 O  O   . VAL B 1 120 ? -22.548 -8.873  0.339   1.00 17.29 ? 120 VAL B O   1 
ATOM   4649 C  CB  . VAL B 1 120 ? -23.836 -10.912 -1.850  1.00 24.16 ? 120 VAL B CB  1 
ATOM   4650 C  CG1 . VAL B 1 120 ? -24.568 -9.730  -2.476  1.00 26.64 ? 120 VAL B CG1 1 
ATOM   4651 C  CG2 . VAL B 1 120 ? -22.462 -11.022 -2.481  1.00 25.74 ? 120 VAL B CG2 1 
ATOM   4652 N  N   . ASP B 1 121 ? -24.814 -8.782  0.515   1.00 20.50 ? 121 ASP B N   1 
ATOM   4653 C  CA  . ASP B 1 121 ? -24.878 -7.458  1.183   1.00 20.14 ? 121 ASP B CA  1 
ATOM   4654 C  C   . ASP B 1 121 ? -24.011 -7.523  2.446   1.00 19.65 ? 121 ASP B C   1 
ATOM   4655 O  O   . ASP B 1 121 ? -23.070 -6.709  2.596   1.00 17.71 ? 121 ASP B O   1 
ATOM   4656 C  CB  . ASP B 1 121 ? -26.314 -7.035  1.466   1.00 20.15 ? 121 ASP B CB  1 
ATOM   4657 C  CG  . ASP B 1 121 ? -26.379 -5.617  2.021   1.00 22.55 ? 121 ASP B CG  1 
ATOM   4658 O  OD1 . ASP B 1 121 ? -25.876 -5.402  3.139   1.00 21.72 ? 121 ASP B OD1 1 
ATOM   4659 O  OD2 . ASP B 1 121 ? -26.922 -4.731  1.336   1.00 25.03 ? 121 ASP B OD2 1 
ATOM   4660 N  N   . ILE B 1 122 ? -24.238 -8.531  3.283   1.00 20.31 ? 122 ILE B N   1 
ATOM   4661 C  CA  . ILE B 1 122 ? -23.473 -8.656  4.557   1.00 20.38 ? 122 ILE B CA  1 
ATOM   4662 C  C   . ILE B 1 122 ? -22.045 -9.165  4.284   1.00 19.57 ? 122 ILE B C   1 
ATOM   4663 O  O   . ILE B 1 122 ? -21.116 -8.717  4.980   1.00 19.24 ? 122 ILE B O   1 
ATOM   4664 C  CB  . ILE B 1 122 ? -24.241 -9.517  5.559   1.00 19.24 ? 122 ILE B CB  1 
ATOM   4665 C  CG1 . ILE B 1 122 ? -25.682 -9.030  5.715   1.00 20.68 ? 122 ILE B CG1 1 
ATOM   4666 C  CG2 . ILE B 1 122 ? -23.502 -9.527  6.863   1.00 19.17 ? 122 ILE B CG2 1 
ATOM   4667 C  CD1 . ILE B 1 122 ? -25.829 -7.541  6.003   1.00 20.50 ? 122 ILE B CD1 1 
ATOM   4668 N  N   . ALA B 1 123 ? -21.836 -10.044 3.311   1.00 19.11 ? 123 ALA B N   1 
ATOM   4669 C  CA  . ALA B 1 123 ? -20.480 -10.579 3.023   1.00 19.77 ? 123 ALA B CA  1 
ATOM   4670 C  C   . ALA B 1 123 ? -19.521 -9.433  2.662   1.00 19.48 ? 123 ALA B C   1 
ATOM   4671 O  O   . ALA B 1 123 ? -18.387 -9.431  3.178   1.00 22.35 ? 123 ALA B O   1 
ATOM   4672 C  CB  . ALA B 1 123 ? -20.517 -11.653 1.950   1.00 19.65 ? 123 ALA B CB  1 
ATOM   4673 N  N   . VAL B 1 124 ? -19.941 -8.502  1.808   1.00 19.54 ? 124 VAL B N   1 
ATOM   4674 C  CA  . VAL B 1 124 ? -19.138 -7.327  1.352   1.00 19.67 ? 124 VAL B CA  1 
ATOM   4675 C  C   . VAL B 1 124 ? -18.825 -6.398  2.541   1.00 20.61 ? 124 VAL B C   1 
ATOM   4676 O  O   . VAL B 1 124 ? -17.651 -6.016  2.695   1.00 20.90 ? 124 VAL B O   1 
ATOM   4677 C  CB  . VAL B 1 124 ? -19.896 -6.627  0.217   1.00 21.36 ? 124 VAL B CB  1 
ATOM   4678 C  CG1 . VAL B 1 124 ? -19.396 -5.222  -0.062  1.00 21.67 ? 124 VAL B CG1 1 
ATOM   4679 C  CG2 . VAL B 1 124 ? -19.893 -7.481  -1.054  1.00 21.66 ? 124 VAL B CG2 1 
ATOM   4680 N  N   . GLN B 1 125 ? -19.804 -6.075  3.392   1.00 20.32 ? 125 GLN B N   1 
ATOM   4681 C  CA  . GLN B 1 125 ? -19.567 -5.325  4.660   1.00 20.65 ? 125 GLN B CA  1 
ATOM   4682 C  C   . GLN B 1 125 ? -18.428 -5.971  5.467   1.00 21.51 ? 125 GLN B C   1 
ATOM   4683 O  O   . GLN B 1 125 ? -17.570 -5.234  5.990   1.00 21.25 ? 125 GLN B O   1 
ATOM   4684 C  CB  . GLN B 1 125 ? -20.842 -5.270  5.495   1.00 21.31 ? 125 GLN B CB  1 
ATOM   4685 C  CG  . GLN B 1 125 ? -21.837 -4.211  5.047   1.00 21.49 ? 125 GLN B CG  1 
ATOM   4686 C  CD  . GLN B 1 125 ? -22.996 -4.087  6.014   1.00 21.89 ? 125 GLN B CD  1 
ATOM   4687 O  OE1 . GLN B 1 125 ? -22.827 -3.707  7.174   1.00 21.61 ? 125 GLN B OE1 1 
ATOM   4688 N  NE2 . GLN B 1 125 ? -24.199 -4.354  5.528   1.00 21.93 ? 125 GLN B NE2 1 
ATOM   4689 N  N   . LEU B 1 126 ? -18.400 -7.301  5.580   1.00 22.11 ? 126 LEU B N   1 
ATOM   4690 C  CA  . LEU B 1 126 ? -17.272 -7.998  6.242   1.00 23.20 ? 126 LEU B CA  1 
ATOM   4691 C  C   . LEU B 1 126 ? -16.001 -7.764  5.425   1.00 22.40 ? 126 LEU B C   1 
ATOM   4692 O  O   . LEU B 1 126 ? -15.043 -7.276  6.019   1.00 23.74 ? 126 LEU B O   1 
ATOM   4693 C  CB  . LEU B 1 126 ? -17.546 -9.495  6.410   1.00 25.44 ? 126 LEU B CB  1 
ATOM   4694 C  CG  . LEU B 1 126 ? -16.482 -10.240 7.224   1.00 26.05 ? 126 LEU B CG  1 
ATOM   4695 C  CD1 . LEU B 1 126 ? -16.811 -10.259 8.714   1.00 25.20 ? 126 LEU B CD1 1 
ATOM   4696 C  CD2 . LEU B 1 126 ? -16.309 -11.653 6.704   1.00 27.14 ? 126 LEU B CD2 1 
ATOM   4697 N  N   . VAL B 1 127 ? -15.980 -8.112  4.137   1.00 21.78 ? 127 VAL B N   1 
ATOM   4698 C  CA  . VAL B 1 127 ? -14.750 -7.974  3.306   1.00 22.88 ? 127 VAL B CA  1 
ATOM   4699 C  C   . VAL B 1 127 ? -14.181 -6.566  3.472   1.00 22.75 ? 127 VAL B C   1 
ATOM   4700 O  O   . VAL B 1 127 ? -12.976 -6.469  3.675   1.00 25.65 ? 127 VAL B O   1 
ATOM   4701 C  CB  . VAL B 1 127 ? -14.990 -8.304  1.827   1.00 23.86 ? 127 VAL B CB  1 
ATOM   4702 C  CG1 . VAL B 1 127 ? -13.827 -7.874  0.927   1.00 23.34 ? 127 VAL B CG1 1 
ATOM   4703 C  CG2 . VAL B 1 127 ? -15.274 -9.786  1.683   1.00 24.20 ? 127 VAL B CG2 1 
ATOM   4704 N  N   . GLN B 1 128 ? -15.018 -5.531  3.426   1.00 23.84 ? 128 GLN B N   1 
ATOM   4705 C  CA  . GLN B 1 128 ? -14.621 -4.094  3.526   1.00 22.65 ? 128 GLN B CA  1 
ATOM   4706 C  C   . GLN B 1 128 ? -14.133 -3.732  4.951   1.00 21.20 ? 128 GLN B C   1 
ATOM   4707 O  O   . GLN B 1 128 ? -13.116 -3.019  5.059   1.00 18.66 ? 128 GLN B O   1 
ATOM   4708 C  CB  . GLN B 1 128 ? -15.793 -3.229  3.053   1.00 24.32 ? 128 GLN B CB  1 
ATOM   4709 C  CG  . GLN B 1 128 ? -16.002 -3.326  1.550   1.00 26.92 ? 128 GLN B CG  1 
ATOM   4710 C  CD  . GLN B 1 128 ? -16.996 -2.337  0.985   1.00 30.85 ? 128 GLN B CD  1 
ATOM   4711 O  OE1 . GLN B 1 128 ? -18.095 -2.123  1.522   1.00 32.02 ? 128 GLN B OE1 1 
ATOM   4712 N  NE2 . GLN B 1 128 ? -16.618 -1.748  -0.143  1.00 32.32 ? 128 GLN B NE2 1 
ATOM   4713 N  N   . LYS B 1 129 ? -14.813 -4.176  6.014   1.00 19.66 ? 129 LYS B N   1 
ATOM   4714 C  CA  . LYS B 1 129 ? -14.324 -4.022  7.415   1.00 19.50 ? 129 LYS B CA  1 
ATOM   4715 C  C   . LYS B 1 129 ? -12.857 -4.470  7.500   1.00 19.54 ? 129 LYS B C   1 
ATOM   4716 O  O   . LYS B 1 129 ? -12.008 -3.744  8.067   1.00 17.15 ? 129 LYS B O   1 
ATOM   4717 C  CB  . LYS B 1 129 ? -15.152 -4.866  8.389   1.00 20.14 ? 129 LYS B CB  1 
ATOM   4718 C  CG  . LYS B 1 129 ? -14.535 -4.959  9.769   1.00 21.65 ? 129 LYS B CG  1 
ATOM   4719 C  CD  . LYS B 1 129 ? -15.447 -5.423  10.878  1.00 23.17 ? 129 LYS B CD  1 
ATOM   4720 C  CE  . LYS B 1 129 ? -14.897 -4.980  12.222  1.00 24.43 ? 129 LYS B CE  1 
ATOM   4721 N  NZ  . LYS B 1 129 ? -15.345 -5.856  13.326  1.00 25.97 ? 129 LYS B NZ  1 
ATOM   4722 N  N   . TRP B 1 130 ? -12.582 -5.653  6.950   1.00 19.14 ? 130 TRP B N   1 
ATOM   4723 C  CA  . TRP B 1 130 ? -11.261 -6.308  7.011   1.00 18.05 ? 130 TRP B CA  1 
ATOM   4724 C  C   . TRP B 1 130 ? -10.309 -5.572  6.073   1.00 19.34 ? 130 TRP B C   1 
ATOM   4725 O  O   . TRP B 1 130 ? -9.128  -5.452  6.431   1.00 20.45 ? 130 TRP B O   1 
ATOM   4726 C  CB  . TRP B 1 130 ? -11.401 -7.797  6.679   1.00 16.92 ? 130 TRP B CB  1 
ATOM   4727 C  CG  . TRP B 1 130 ? -11.972 -8.581  7.817   1.00 16.77 ? 130 TRP B CG  1 
ATOM   4728 C  CD1 . TRP B 1 130 ? -12.480 -8.091  8.983   1.00 15.43 ? 130 TRP B CD1 1 
ATOM   4729 C  CD2 . TRP B 1 130 ? -12.120 -10.003 7.877   1.00 15.67 ? 130 TRP B CD2 1 
ATOM   4730 N  NE1 . TRP B 1 130 ? -12.901 -9.112  9.773   1.00 15.60 ? 130 TRP B NE1 1 
ATOM   4731 C  CE2 . TRP B 1 130 ? -12.682 -10.299 9.129   1.00 15.86 ? 130 TRP B CE2 1 
ATOM   4732 C  CE3 . TRP B 1 130 ? -11.771 -11.050 7.018   1.00 15.54 ? 130 TRP B CE3 1 
ATOM   4733 C  CZ2 . TRP B 1 130 ? -12.977 -11.606 9.521   1.00 15.37 ? 130 TRP B CZ2 1 
ATOM   4734 C  CZ3 . TRP B 1 130 ? -12.009 -12.339 7.422   1.00 15.05 ? 130 TRP B CZ3 1 
ATOM   4735 C  CH2 . TRP B 1 130 ? -12.625 -12.611 8.652   1.00 15.62 ? 130 TRP B CH2 1 
ATOM   4736 N  N   . GLU B 1 131 ? -10.784 -5.111  4.921   1.00 19.67 ? 131 GLU B N   1 
ATOM   4737 C  CA  . GLU B 1 131 ? -9.924  -4.356  3.974   1.00 22.03 ? 131 GLU B CA  1 
ATOM   4738 C  C   . GLU B 1 131 ? -9.527  -3.056  4.699   1.00 20.70 ? 131 GLU B C   1 
ATOM   4739 O  O   . GLU B 1 131 ? -8.435  -2.590  4.517   1.00 18.95 ? 131 GLU B O   1 
ATOM   4740 C  CB  . GLU B 1 131 ? -10.608 -4.259  2.596   1.00 25.50 ? 131 GLU B CB  1 
ATOM   4741 C  CG  . GLU B 1 131 ? -9.666  -4.591  1.432   1.00 33.35 ? 131 GLU B CG  1 
ATOM   4742 C  CD  . GLU B 1 131 ? -10.052 -5.629  0.377   1.00 38.25 ? 131 GLU B CD  1 
ATOM   4743 O  OE1 . GLU B 1 131 ? -11.082 -5.450  -0.319  1.00 44.27 ? 131 GLU B OE1 1 
ATOM   4744 O  OE2 . GLU B 1 131 ? -9.280  -6.600  0.203   1.00 40.33 ? 131 GLU B OE2 1 
ATOM   4745 N  N   . ARG B 1 132 ? -10.331 -2.575  5.643   1.00 21.48 ? 132 ARG B N   1 
ATOM   4746 C  CA  . ARG B 1 132 ? -10.155 -1.230  6.245   1.00 21.34 ? 132 ARG B CA  1 
ATOM   4747 C  C   . ARG B 1 132 ? -9.330  -1.307  7.527   1.00 19.83 ? 132 ARG B C   1 
ATOM   4748 O  O   . ARG B 1 132 ? -9.123  -0.235  8.097   1.00 18.59 ? 132 ARG B O   1 
ATOM   4749 C  CB  . ARG B 1 132 ? -11.516 -0.567  6.495   1.00 20.85 ? 132 ARG B CB  1 
ATOM   4750 C  CG  . ARG B 1 132 ? -12.146 -0.064  5.206   1.00 21.37 ? 132 ARG B CG  1 
ATOM   4751 C  CD  . ARG B 1 132 ? -13.629 0.197   5.266   1.00 21.86 ? 132 ARG B CD  1 
ATOM   4752 N  NE  . ARG B 1 132 ? -14.082 0.702   3.976   1.00 22.13 ? 132 ARG B NE  1 
ATOM   4753 C  CZ  . ARG B 1 132 ? -15.357 0.836   3.631   1.00 22.18 ? 132 ARG B CZ  1 
ATOM   4754 N  NH1 . ARG B 1 132 ? -16.325 0.448   4.439   1.00 20.54 ? 132 ARG B NH1 1 
ATOM   4755 N  NH2 . ARG B 1 132 ? -15.663 1.337   2.454   1.00 23.40 ? 132 ARG B NH2 1 
ATOM   4756 N  N   . LEU B 1 133 ? -8.875  -2.494  7.942   1.00 19.20 ? 133 LEU B N   1 
ATOM   4757 C  CA  . LEU B 1 133 ? -8.026  -2.643  9.156   1.00 21.93 ? 133 LEU B CA  1 
ATOM   4758 C  C   . LEU B 1 133 ? -6.633  -2.090  8.837   1.00 23.77 ? 133 LEU B C   1 
ATOM   4759 O  O   . LEU B 1 133 ? -6.187  -2.228  7.677   1.00 23.56 ? 133 LEU B O   1 
ATOM   4760 C  CB  . LEU B 1 133 ? -7.950  -4.107  9.604   1.00 21.42 ? 133 LEU B CB  1 
ATOM   4761 C  CG  . LEU B 1 133 ? -9.224  -4.693  10.217  1.00 22.51 ? 133 LEU B CG  1 
ATOM   4762 C  CD1 . LEU B 1 133 ? -8.992  -6.102  10.757  1.00 21.90 ? 133 LEU B CD1 1 
ATOM   4763 C  CD2 . LEU B 1 133 ? -9.779  -3.791  11.316  1.00 22.78 ? 133 LEU B CD2 1 
ATOM   4764 N  N   . ASN B 1 134 ? -5.971  -1.483  9.820   1.00 25.00 ? 134 ASN B N   1 
ATOM   4765 C  CA  . ASN B 1 134 ? -4.560  -1.022  9.677   1.00 27.29 ? 134 ASN B CA  1 
ATOM   4766 C  C   . ASN B 1 134 ? -3.623  -2.200  9.966   1.00 29.46 ? 134 ASN B C   1 
ATOM   4767 O  O   . ASN B 1 134 ? -4.054  -3.146  10.651  1.00 32.72 ? 134 ASN B O   1 
ATOM   4768 C  CB  . ASN B 1 134 ? -4.252  0.154   10.605  1.00 25.82 ? 134 ASN B CB  1 
ATOM   4769 C  CG  . ASN B 1 134 ? -5.265  1.270   10.477  1.00 23.60 ? 134 ASN B CG  1 
ATOM   4770 O  OD1 . ASN B 1 134 ? -5.302  1.942   9.454   1.00 23.18 ? 134 ASN B OD1 1 
ATOM   4771 N  ND2 . ASN B 1 134 ? -6.080  1.471   11.498  1.00 21.46 ? 134 ASN B ND2 1 
ATOM   4772 N  N   . ALA B 1 135 ? -2.381  -2.114  9.502   1.00 30.85 ? 135 ALA B N   1 
ATOM   4773 C  CA  . ALA B 1 135 ? -1.337  -3.166  9.570   1.00 34.25 ? 135 ALA B CA  1 
ATOM   4774 C  C   . ALA B 1 135 ? -1.258  -3.819  10.965  1.00 35.29 ? 135 ALA B C   1 
ATOM   4775 O  O   . ALA B 1 135 ? -1.347  -5.068  11.054  1.00 36.77 ? 135 ALA B O   1 
ATOM   4776 C  CB  . ALA B 1 135 ? -0.021  -2.539  9.162   1.00 35.15 ? 135 ALA B CB  1 
ATOM   4777 N  N   . ASP B 1 136 ? -1.133  -3.025  12.031  1.00 37.75 ? 136 ASP B N   1 
ATOM   4778 C  CA  . ASP B 1 136 ? -0.759  -3.548  13.378  1.00 48.37 ? 136 ASP B CA  1 
ATOM   4779 C  C   . ASP B 1 136 ? -2.033  -3.991  14.128  1.00 47.88 ? 136 ASP B C   1 
ATOM   4780 O  O   . ASP B 1 136 ? -2.034  -3.914  15.390  1.00 51.01 ? 136 ASP B O   1 
ATOM   4781 C  CB  . ASP B 1 136 ? 0.135   -2.546  14.143  1.00 53.82 ? 136 ASP B CB  1 
ATOM   4782 C  CG  . ASP B 1 136 ? 1.657   -2.775  14.052  1.00 60.17 ? 136 ASP B CG  1 
ATOM   4783 O  OD1 . ASP B 1 136 ? 2.137   -3.292  13.005  1.00 56.80 ? 136 ASP B OD1 1 
ATOM   4784 O  OD2 . ASP B 1 136 ? 2.377   -2.433  15.037  1.00 61.14 ? 136 ASP B OD2 1 
ATOM   4785 N  N   . GLU B 1 137 ? -3.072  -4.452  13.402  1.00 42.31 ? 137 GLU B N   1 
ATOM   4786 C  CA  . GLU B 1 137 ? -4.403  -4.838  13.965  1.00 35.20 ? 137 GLU B CA  1 
ATOM   4787 C  C   . GLU B 1 137 ? -4.785  -6.254  13.524  1.00 32.71 ? 137 GLU B C   1 
ATOM   4788 O  O   . GLU B 1 137 ? -4.398  -6.689  12.392  1.00 37.81 ? 137 GLU B O   1 
ATOM   4789 C  CB  . GLU B 1 137 ? -5.531  -3.925  13.504  1.00 30.88 ? 137 GLU B CB  1 
ATOM   4790 C  CG  . GLU B 1 137 ? -5.378  -2.518  13.970  1.00 32.00 ? 137 GLU B CG  1 
ATOM   4791 C  CD  . GLU B 1 137 ? -6.412  -1.552  13.430  1.00 33.47 ? 137 GLU B CD  1 
ATOM   4792 O  OE1 . GLU B 1 137 ? -7.153  -1.935  12.498  1.00 31.59 ? 137 GLU B OE1 1 
ATOM   4793 O  OE2 . GLU B 1 137 ? -6.452  -0.407  13.943  1.00 33.99 ? 137 GLU B OE2 1 
ATOM   4794 N  N   . HIS B 1 138 ? -5.562  -6.919  14.370  1.00 26.48 ? 138 HIS B N   1 
ATOM   4795 C  CA  . HIS B 1 138 ? -5.981  -8.329  14.182  1.00 25.23 ? 138 HIS B CA  1 
ATOM   4796 C  C   . HIS B 1 138 ? -7.512  -8.399  14.076  1.00 22.62 ? 138 HIS B C   1 
ATOM   4797 O  O   . HIS B 1 138 ? -8.179  -7.390  14.299  1.00 22.38 ? 138 HIS B O   1 
ATOM   4798 C  CB  . HIS B 1 138 ? -5.385  -9.204  15.293  1.00 23.94 ? 138 HIS B CB  1 
ATOM   4799 C  CG  . HIS B 1 138 ? -6.034  -9.022  16.619  1.00 24.27 ? 138 HIS B CG  1 
ATOM   4800 N  ND1 . HIS B 1 138 ? -5.394  -8.423  17.668  1.00 28.03 ? 138 HIS B ND1 1 
ATOM   4801 C  CD2 . HIS B 1 138 ? -7.263  -9.360  17.071  1.00 25.37 ? 138 HIS B CD2 1 
ATOM   4802 C  CE1 . HIS B 1 138 ? -6.199  -8.393  18.722  1.00 28.82 ? 138 HIS B CE1 1 
ATOM   4803 N  NE2 . HIS B 1 138 ? -7.345  -8.982  18.385  1.00 24.96 ? 138 HIS B NE2 1 
ATOM   4804 N  N   . ILE B 1 139 ? -8.007  -9.578  13.718  1.00 20.12 ? 139 ILE B N   1 
ATOM   4805 C  CA  . ILE B 1 139 ? -9.438  -9.929  13.516  1.00 19.76 ? 139 ILE B CA  1 
ATOM   4806 C  C   . ILE B 1 139 ? -9.867  -10.876 14.637  1.00 18.13 ? 139 ILE B C   1 
ATOM   4807 O  O   . ILE B 1 139 ? -9.210  -11.901 14.803  1.00 17.17 ? 139 ILE B O   1 
ATOM   4808 C  CB  . ILE B 1 139 ? -9.605  -10.586 12.134  1.00 18.72 ? 139 ILE B CB  1 
ATOM   4809 C  CG1 . ILE B 1 139 ? -9.438  -9.553  11.015  1.00 19.44 ? 139 ILE B CG1 1 
ATOM   4810 C  CG2 . ILE B 1 139 ? -10.917 -11.335 12.062  1.00 17.97 ? 139 ILE B CG2 1 
ATOM   4811 C  CD1 . ILE B 1 139 ? -9.007  -10.128 9.683   1.00 20.08 ? 139 ILE B CD1 1 
ATOM   4812 N  N   . GLU B 1 140 ? -10.928 -10.528 15.350  1.00 19.06 ? 140 GLU B N   1 
ATOM   4813 C  CA  . GLU B 1 140 ? -11.550 -11.394 16.381  1.00 21.30 ? 140 GLU B CA  1 
ATOM   4814 C  C   . GLU B 1 140 ? -12.523 -12.277 15.602  1.00 18.94 ? 140 GLU B C   1 
ATOM   4815 O  O   . GLU B 1 140 ? -13.544 -11.772 15.158  1.00 19.45 ? 140 GLU B O   1 
ATOM   4816 C  CB  . GLU B 1 140 ? -12.182 -10.552 17.499  1.00 23.19 ? 140 GLU B CB  1 
ATOM   4817 C  CG  . GLU B 1 140 ? -11.190 -9.629  18.214  1.00 25.01 ? 140 GLU B CG  1 
ATOM   4818 C  CD  . GLU B 1 140 ? -11.763 -8.624  19.214  1.00 27.34 ? 140 GLU B CD  1 
ATOM   4819 O  OE1 . GLU B 1 140 ? -12.992 -8.493  19.293  1.00 27.24 ? 140 GLU B OE1 1 
ATOM   4820 O  OE2 . GLU B 1 140 ? -10.969 -7.946  19.903  1.00 31.35 ? 140 GLU B OE2 1 
ATOM   4821 N  N   . VAL B 1 141 ? -12.162 -13.531 15.357  1.00 17.11 ? 141 VAL B N   1 
ATOM   4822 C  CA  . VAL B 1 141 ? -12.854 -14.359 14.330  1.00 16.03 ? 141 VAL B CA  1 
ATOM   4823 C  C   . VAL B 1 141 ? -14.294 -14.650 14.741  1.00 15.91 ? 141 VAL B C   1 
ATOM   4824 O  O   . VAL B 1 141 ? -15.219 -14.287 14.025  1.00 14.80 ? 141 VAL B O   1 
ATOM   4825 C  CB  . VAL B 1 141 ? -12.098 -15.653 14.049  1.00 14.98 ? 141 VAL B CB  1 
ATOM   4826 C  CG1 . VAL B 1 141 ? -12.952 -16.533 13.155  1.00 15.76 ? 141 VAL B CG1 1 
ATOM   4827 C  CG2 . VAL B 1 141 ? -10.719 -15.396 13.470  1.00 14.55 ? 141 VAL B CG2 1 
ATOM   4828 N  N   . PRO B 1 142 ? -14.549 -15.382 15.848  1.00 16.17 ? 142 PRO B N   1 
ATOM   4829 C  CA  . PRO B 1 142 ? -15.918 -15.750 16.185  1.00 16.87 ? 142 PRO B CA  1 
ATOM   4830 C  C   . PRO B 1 142 ? -16.792 -14.496 16.330  1.00 17.48 ? 142 PRO B C   1 
ATOM   4831 O  O   . PRO B 1 142 ? -17.946 -14.562 16.015  1.00 20.63 ? 142 PRO B O   1 
ATOM   4832 C  CB  . PRO B 1 142 ? -15.808 -16.555 17.497  1.00 16.84 ? 142 PRO B CB  1 
ATOM   4833 C  CG  . PRO B 1 142 ? -14.421 -16.202 18.054  1.00 16.92 ? 142 PRO B CG  1 
ATOM   4834 C  CD  . PRO B 1 142 ? -13.575 -15.904 16.822  1.00 16.46 ? 142 PRO B CD  1 
ATOM   4835 N  N   . GLU B 1 143 ? -16.244 -13.376 16.789  1.00 17.56 ? 143 GLU B N   1 
ATOM   4836 C  CA  . GLU B 1 143 ? -17.047 -12.143 17.005  1.00 17.22 ? 143 GLU B CA  1 
ATOM   4837 C  C   . GLU B 1 143 ? -17.555 -11.604 15.656  1.00 15.66 ? 143 GLU B C   1 
ATOM   4838 O  O   . GLU B 1 143 ? -18.755 -11.318 15.558  1.00 13.24 ? 143 GLU B O   1 
ATOM   4839 C  CB  . GLU B 1 143 ? -16.243 -11.089 17.758  1.00 18.30 ? 143 GLU B CB  1 
ATOM   4840 C  CG  . GLU B 1 143 ? -16.072 -11.410 19.230  1.00 20.84 ? 143 GLU B CG  1 
ATOM   4841 C  CD  . GLU B 1 143 ? -15.005 -12.438 19.601  1.00 22.90 ? 143 GLU B CD  1 
ATOM   4842 O  OE1 . GLU B 1 143 ? -14.264 -12.910 18.697  1.00 24.11 ? 143 GLU B OE1 1 
ATOM   4843 O  OE2 . GLU B 1 143 ? -14.929 -12.782 20.801  1.00 23.88 ? 143 GLU B OE2 1 
ATOM   4844 N  N   . ASP B 1 144 ? -16.664 -11.462 14.674  1.00 15.29 ? 144 ASP B N   1 
ATOM   4845 C  CA  . ASP B 1 144 ? -16.998 -10.926 13.333  1.00 15.32 ? 144 ASP B CA  1 
ATOM   4846 C  C   . ASP B 1 144 ? -17.865 -11.953 12.608  1.00 16.46 ? 144 ASP B C   1 
ATOM   4847 O  O   . ASP B 1 144 ? -18.812 -11.503 11.936  1.00 18.34 ? 144 ASP B O   1 
ATOM   4848 C  CB  . ASP B 1 144 ? -15.761 -10.499 12.539  1.00 15.08 ? 144 ASP B CB  1 
ATOM   4849 C  CG  . ASP B 1 144 ? -15.180 -9.133  12.892  1.00 15.91 ? 144 ASP B CG  1 
ATOM   4850 O  OD1 . ASP B 1 144 ? -15.763 -8.422  13.736  1.00 14.76 ? 144 ASP B OD1 1 
ATOM   4851 O  OD2 . ASP B 1 144 ? -14.129 -8.774  12.305  1.00 17.76 ? 144 ASP B OD2 1 
ATOM   4852 N  N   . MET B 1 145 ? -17.609 -13.261 12.724  1.00 16.68 ? 145 MET B N   1 
ATOM   4853 C  CA  . MET B 1 145 ? -18.483 -14.254 12.026  1.00 17.67 ? 145 MET B CA  1 
ATOM   4854 C  C   . MET B 1 145 ? -19.894 -14.223 12.634  1.00 17.57 ? 145 MET B C   1 
ATOM   4855 O  O   . MET B 1 145 ? -20.844 -14.443 11.870  1.00 18.13 ? 145 MET B O   1 
ATOM   4856 C  CB  . MET B 1 145 ? -17.956 -15.692 12.051  1.00 17.87 ? 145 MET B CB  1 
ATOM   4857 C  CG  . MET B 1 145 ? -16.617 -15.865 11.359  1.00 18.12 ? 145 MET B CG  1 
ATOM   4858 S  SD  . MET B 1 145 ? -16.528 -15.430 9.591   1.00 18.75 ? 145 MET B SD  1 
ATOM   4859 C  CE  . MET B 1 145 ? -16.488 -13.642 9.615   1.00 19.15 ? 145 MET B CE  1 
ATOM   4860 N  N   . THR B 1 146 ? -20.038 -13.978 13.940  1.00 16.68 ? 146 THR B N   1 
ATOM   4861 C  CA  . THR B 1 146 ? -21.365 -13.911 14.605  1.00 16.74 ? 146 THR B CA  1 
ATOM   4862 C  C   . THR B 1 146 ? -22.077 -12.648 14.114  1.00 18.44 ? 146 THR B C   1 
ATOM   4863 O  O   . THR B 1 146 ? -23.261 -12.724 13.742  1.00 16.95 ? 146 THR B O   1 
ATOM   4864 C  CB  . THR B 1 146 ? -21.251 -13.892 16.130  1.00 15.91 ? 146 THR B CB  1 
ATOM   4865 O  OG1 . THR B 1 146 ? -20.609 -15.100 16.520  1.00 14.69 ? 146 THR B OG1 1 
ATOM   4866 C  CG2 . THR B 1 146 ? -22.584 -13.743 16.824  1.00 15.67 ? 146 THR B CG2 1 
ATOM   4867 N  N   . ARG B 1 147 ? -21.380 -11.510 14.153  1.00 20.59 ? 147 ARG B N   1 
ATOM   4868 C  CA  . ARG B 1 147 ? -21.885 -10.225 13.602  1.00 21.19 ? 147 ARG B CA  1 
ATOM   4869 C  C   . ARG B 1 147 ? -22.495 -10.500 12.226  1.00 21.53 ? 147 ARG B C   1 
ATOM   4870 O  O   . ARG B 1 147 ? -23.699 -10.224 12.083  1.00 23.48 ? 147 ARG B O   1 
ATOM   4871 C  CB  . ARG B 1 147 ? -20.774 -9.176  13.569  1.00 22.62 ? 147 ARG B CB  1 
ATOM   4872 C  CG  . ARG B 1 147 ? -20.482 -8.595  14.945  1.00 23.80 ? 147 ARG B CG  1 
ATOM   4873 C  CD  . ARG B 1 147 ? -19.494 -7.447  14.839  1.00 25.65 ? 147 ARG B CD  1 
ATOM   4874 N  NE  . ARG B 1 147 ? -19.075 -7.055  16.170  1.00 25.78 ? 147 ARG B NE  1 
ATOM   4875 C  CZ  . ARG B 1 147 ? -17.907 -7.333  16.732  1.00 28.39 ? 147 ARG B CZ  1 
ATOM   4876 N  NH1 . ARG B 1 147 ? -16.947 -7.984  16.098  1.00 28.41 ? 147 ARG B NH1 1 
ATOM   4877 N  NH2 . ARG B 1 147 ? -17.697 -6.927  17.966  1.00 33.13 ? 147 ARG B NH2 1 
ATOM   4878 N  N   . LEU B 1 148 ? -21.739 -11.122 11.308  1.00 20.93 ? 148 LEU B N   1 
ATOM   4879 C  CA  . LEU B 1 148 ? -22.190 -11.371 9.920   1.00 20.88 ? 148 LEU B CA  1 
ATOM   4880 C  C   . LEU B 1 148 ? -23.459 -12.226 9.867   1.00 19.66 ? 148 LEU B C   1 
ATOM   4881 O  O   . LEU B 1 148 ? -24.344 -11.808 9.089   1.00 17.74 ? 148 LEU B O   1 
ATOM   4882 C  CB  . LEU B 1 148 ? -21.096 -12.032 9.083   1.00 23.73 ? 148 LEU B CB  1 
ATOM   4883 C  CG  . LEU B 1 148 ? -21.536 -12.422 7.669   1.00 25.39 ? 148 LEU B CG  1 
ATOM   4884 C  CD1 . LEU B 1 148 ? -20.590 -11.856 6.623   1.00 28.05 ? 148 LEU B CD1 1 
ATOM   4885 C  CD2 . LEU B 1 148 ? -21.654 -13.932 7.527   1.00 27.60 ? 148 LEU B CD2 1 
ATOM   4886 N  N   . THR B 1 149 ? -23.514 -13.389 10.554  1.00 19.29 ? 149 THR B N   1 
ATOM   4887 C  CA  . THR B 1 149 ? -24.598 -14.408 10.385  1.00 18.66 ? 149 THR B CA  1 
ATOM   4888 C  C   . THR B 1 149 ? -25.902 -13.934 11.039  1.00 18.82 ? 149 THR B C   1 
ATOM   4889 O  O   . THR B 1 149 ? -26.979 -14.316 10.521  1.00 19.71 ? 149 THR B O   1 
ATOM   4890 C  CB  . THR B 1 149 ? -24.234 -15.822 10.868  1.00 19.57 ? 149 THR B CB  1 
ATOM   4891 O  OG1 . THR B 1 149 ? -24.044 -15.874 12.281  1.00 19.43 ? 149 THR B OG1 1 
ATOM   4892 C  CG2 . THR B 1 149 ? -22.996 -16.372 10.181  1.00 20.66 ? 149 THR B CG2 1 
ATOM   4893 N  N   . LEU B 1 150 ? -25.839 -13.160 12.121  1.00 18.65 ? 150 LEU B N   1 
ATOM   4894 C  CA  . LEU B 1 150 ? -27.048 -12.500 12.696  1.00 19.55 ? 150 LEU B CA  1 
ATOM   4895 C  C   . LEU B 1 150 ? -27.547 -11.441 11.710  1.00 18.87 ? 150 LEU B C   1 
ATOM   4896 O  O   . LEU B 1 150 ? -28.755 -11.366 11.522  1.00 17.22 ? 150 LEU B O   1 
ATOM   4897 C  CB  . LEU B 1 150 ? -26.762 -11.854 14.058  1.00 19.32 ? 150 LEU B CB  1 
ATOM   4898 C  CG  . LEU B 1 150 ? -27.924 -11.025 14.623  1.00 19.19 ? 150 LEU B CG  1 
ATOM   4899 C  CD1 . LEU B 1 150 ? -29.078 -11.930 15.025  1.00 18.30 ? 150 LEU B CD1 1 
ATOM   4900 C  CD2 . LEU B 1 150 ? -27.468 -10.169 15.804  1.00 19.25 ? 150 LEU B CD2 1 
ATOM   4901 N  N   . ASP B 1 151 ? -26.643 -10.663 11.098  1.00 20.22 ? 151 ASP B N   1 
ATOM   4902 C  CA  . ASP B 1 151 ? -27.034 -9.614  10.111  1.00 20.48 ? 151 ASP B CA  1 
ATOM   4903 C  C   . ASP B 1 151 ? -27.729 -10.309 8.927   1.00 18.14 ? 151 ASP B C   1 
ATOM   4904 O  O   . ASP B 1 151 ? -28.754 -9.818  8.498   1.00 17.94 ? 151 ASP B O   1 
ATOM   4905 C  CB  . ASP B 1 151 ? -25.865 -8.677  9.748   1.00 21.34 ? 151 ASP B CB  1 
ATOM   4906 C  CG  . ASP B 1 151 ? -25.816 -7.453  10.661  1.00 23.83 ? 151 ASP B CG  1 
ATOM   4907 O  OD1 . ASP B 1 151 ? -26.128 -7.643  11.840  1.00 23.51 ? 151 ASP B OD1 1 
ATOM   4908 O  OD2 . ASP B 1 151 ? -25.529 -6.283  10.178  1.00 25.76 ? 151 ASP B OD2 1 
ATOM   4909 N  N   . THR B 1 152 ? -27.256 -11.464 8.483   1.00 17.30 ? 152 THR B N   1 
ATOM   4910 C  CA  . THR B 1 152 ? -27.871 -12.199 7.354   1.00 18.98 ? 152 THR B CA  1 
ATOM   4911 C  C   . THR B 1 152 ? -29.306 -12.621 7.682   1.00 19.55 ? 152 THR B C   1 
ATOM   4912 O  O   . THR B 1 152 ? -30.230 -12.343 6.853   1.00 18.15 ? 152 THR B O   1 
ATOM   4913 C  CB  . THR B 1 152 ? -27.040 -13.411 6.938   1.00 20.25 ? 152 THR B CB  1 
ATOM   4914 O  OG1 . THR B 1 152 ? -25.826 -12.836 6.454   1.00 22.32 ? 152 THR B OG1 1 
ATOM   4915 C  CG2 . THR B 1 152 ? -27.702 -14.264 5.867   1.00 19.97 ? 152 THR B CG2 1 
ATOM   4916 N  N   . ILE B 1 153 ? -29.510 -13.238 8.842   1.00 18.73 ? 153 ILE B N   1 
ATOM   4917 C  CA  . ILE B 1 153 ? -30.845 -13.795 9.175   1.00 19.70 ? 153 ILE B CA  1 
ATOM   4918 C  C   . ILE B 1 153 ? -31.835 -12.656 9.481   1.00 18.13 ? 153 ILE B C   1 
ATOM   4919 O  O   . ILE B 1 153 ? -32.999 -12.796 9.105   1.00 17.89 ? 153 ILE B O   1 
ATOM   4920 C  CB  . ILE B 1 153 ? -30.741 -14.854 10.287  1.00 21.26 ? 153 ILE B CB  1 
ATOM   4921 C  CG1 . ILE B 1 153 ? -31.884 -15.865 10.153  1.00 22.10 ? 153 ILE B CG1 1 
ATOM   4922 C  CG2 . ILE B 1 153 ? -30.678 -14.200 11.665  1.00 22.36 ? 153 ILE B CG2 1 
ATOM   4923 C  CD1 . ILE B 1 153 ? -31.973 -16.494 8.766   1.00 23.20 ? 153 ILE B CD1 1 
ATOM   4924 N  N   . GLY B 1 154 ? -31.407 -11.544 10.078  1.00 17.84 ? 154 GLY B N   1 
ATOM   4925 C  CA  . GLY B 1 154 ? -32.288 -10.372 10.277  1.00 18.37 ? 154 GLY B CA  1 
ATOM   4926 C  C   . GLY B 1 154 ? -32.913 -9.901  8.969   1.00 18.22 ? 154 GLY B C   1 
ATOM   4927 O  O   . GLY B 1 154 ? -34.133 -9.611  8.941   1.00 16.76 ? 154 GLY B O   1 
ATOM   4928 N  N   . LEU B 1 155 ? -32.079 -9.827  7.937   1.00 18.61 ? 155 LEU B N   1 
ATOM   4929 C  CA  . LEU B 1 155 ? -32.428 -9.391  6.572   1.00 20.59 ? 155 LEU B CA  1 
ATOM   4930 C  C   . LEU B 1 155 ? -33.356 -10.433 5.925   1.00 20.06 ? 155 LEU B C   1 
ATOM   4931 O  O   . LEU B 1 155 ? -34.456 -10.062 5.527   1.00 20.99 ? 155 LEU B O   1 
ATOM   4932 C  CB  . LEU B 1 155 ? -31.116 -9.225  5.801   1.00 22.89 ? 155 LEU B CB  1 
ATOM   4933 C  CG  . LEU B 1 155 ? -30.980 -7.970  4.956   1.00 26.02 ? 155 LEU B CG  1 
ATOM   4934 C  CD1 . LEU B 1 155 ? -31.417 -6.744  5.733   1.00 28.16 ? 155 LEU B CD1 1 
ATOM   4935 C  CD2 . LEU B 1 155 ? -29.546 -7.811  4.469   1.00 26.86 ? 155 LEU B CD2 1 
ATOM   4936 N  N   . CYS B 1 156 ? -32.928 -11.688 5.814   1.00 19.96 ? 156 CYS B N   1 
ATOM   4937 C  CA  . CYS B 1 156 ? -33.679 -12.779 5.125   1.00 20.66 ? 156 CYS B CA  1 
ATOM   4938 C  C   . CYS B 1 156 ? -34.914 -13.152 5.936   1.00 20.43 ? 156 CYS B C   1 
ATOM   4939 O  O   . CYS B 1 156 ? -35.849 -13.644 5.350   1.00 21.07 ? 156 CYS B O   1 
ATOM   4940 C  CB  . CYS B 1 156 ? -32.829 -14.033 4.945   1.00 20.27 ? 156 CYS B CB  1 
ATOM   4941 S  SG  . CYS B 1 156 ? -31.319 -13.757 3.978   1.00 19.56 ? 156 CYS B SG  1 
ATOM   4942 N  N   . GLY B 1 157 ? -34.859 -12.974 7.252   1.00 21.30 ? 157 GLY B N   1 
ATOM   4943 C  CA  . GLY B 1 157 ? -35.941 -13.336 8.180   1.00 22.83 ? 157 GLY B CA  1 
ATOM   4944 C  C   . GLY B 1 157 ? -37.075 -12.336 8.119   1.00 22.82 ? 157 GLY B C   1 
ATOM   4945 O  O   . GLY B 1 157 ? -38.240 -12.758 7.966   1.00 23.52 ? 157 GLY B O   1 
ATOM   4946 N  N   . PHE B 1 158 ? -36.766 -11.047 8.250   1.00 22.87 ? 158 PHE B N   1 
ATOM   4947 C  CA  . PHE B 1 158 ? -37.818 -10.007 8.367   1.00 23.70 ? 158 PHE B CA  1 
ATOM   4948 C  C   . PHE B 1 158 ? -37.261 -8.649  7.943   1.00 23.03 ? 158 PHE B C   1 
ATOM   4949 O  O   . PHE B 1 158 ? -37.713 -7.620  8.458   1.00 20.51 ? 158 PHE B O   1 
ATOM   4950 C  CB  . PHE B 1 158 ? -38.422 -10.057 9.776   1.00 23.73 ? 158 PHE B CB  1 
ATOM   4951 C  CG  . PHE B 1 158 ? -37.407 -10.064 10.885  1.00 23.46 ? 158 PHE B CG  1 
ATOM   4952 C  CD1 . PHE B 1 158 ? -36.732 -11.223 11.213  1.00 24.20 ? 158 PHE B CD1 1 
ATOM   4953 C  CD2 . PHE B 1 158 ? -37.119 -8.910  11.595  1.00 23.99 ? 158 PHE B CD2 1 
ATOM   4954 C  CE1 . PHE B 1 158 ? -35.776 -11.223 12.218  1.00 25.25 ? 158 PHE B CE1 1 
ATOM   4955 C  CE2 . PHE B 1 158 ? -36.176 -8.917  12.614  1.00 23.44 ? 158 PHE B CE2 1 
ATOM   4956 C  CZ  . PHE B 1 158 ? -35.503 -10.069 12.921  1.00 24.27 ? 158 PHE B CZ  1 
ATOM   4957 N  N   . ASN B 1 159 ? -36.344 -8.660  6.974   1.00 24.12 ? 159 ASN B N   1 
ATOM   4958 C  CA  . ASN B 1 159 ? -35.882 -7.435  6.267   1.00 25.10 ? 159 ASN B CA  1 
ATOM   4959 C  C   . ASN B 1 159 ? -35.561 -6.333  7.284   1.00 22.66 ? 159 ASN B C   1 
ATOM   4960 O  O   . ASN B 1 159 ? -35.939 -5.181  7.072   1.00 24.96 ? 159 ASN B O   1 
ATOM   4961 C  CB  . ASN B 1 159 ? -36.915 -7.002  5.229   1.00 27.40 ? 159 ASN B CB  1 
ATOM   4962 C  CG  . ASN B 1 159 ? -36.388 -5.915  4.323   1.00 29.91 ? 159 ASN B CG  1 
ATOM   4963 O  OD1 . ASN B 1 159 ? -35.192 -5.828  4.077   1.00 31.87 ? 159 ASN B OD1 1 
ATOM   4964 N  ND2 . ASN B 1 159 ? -37.272 -5.058  3.846   1.00 32.88 ? 159 ASN B ND2 1 
ATOM   4965 N  N   . TYR B 1 160 ? -34.844 -6.695  8.336   1.00 20.47 ? 160 TYR B N   1 
ATOM   4966 C  CA  . TYR B 1 160 ? -34.353 -5.797  9.396   1.00 19.42 ? 160 TYR B CA  1 
ATOM   4967 C  C   . TYR B 1 160 ? -32.838 -5.905  9.516   1.00 19.71 ? 160 TYR B C   1 
ATOM   4968 O  O   . TYR B 1 160 ? -32.286 -7.007  9.445   1.00 20.29 ? 160 TYR B O   1 
ATOM   4969 C  CB  . TYR B 1 160 ? -34.976 -6.219  10.717  1.00 19.89 ? 160 TYR B CB  1 
ATOM   4970 C  CG  . TYR B 1 160 ? -34.628 -5.370  11.905  1.00 19.17 ? 160 TYR B CG  1 
ATOM   4971 C  CD1 . TYR B 1 160 ? -33.484 -5.609  12.625  1.00 18.72 ? 160 TYR B CD1 1 
ATOM   4972 C  CD2 . TYR B 1 160 ? -35.455 -4.348  12.321  1.00 20.00 ? 160 TYR B CD2 1 
ATOM   4973 C  CE1 . TYR B 1 160 ? -33.168 -4.855  13.741  1.00 20.12 ? 160 TYR B CE1 1 
ATOM   4974 C  CE2 . TYR B 1 160 ? -35.142 -3.574  13.431  1.00 21.14 ? 160 TYR B CE2 1 
ATOM   4975 C  CZ  . TYR B 1 160 ? -33.998 -3.838  14.155  1.00 19.03 ? 160 TYR B CZ  1 
ATOM   4976 O  OH  . TYR B 1 160 ? -33.669 -3.105  15.252  1.00 17.51 ? 160 TYR B OH  1 
ATOM   4977 N  N   . ARG B 1 161 ? -32.185 -4.773  9.765   1.00 21.16 ? 161 ARG B N   1 
ATOM   4978 C  CA  . ARG B 1 161 ? -30.700 -4.668  9.817   1.00 18.73 ? 161 ARG B CA  1 
ATOM   4979 C  C   . ARG B 1 161 ? -30.261 -4.506  11.268  1.00 17.06 ? 161 ARG B C   1 
ATOM   4980 O  O   . ARG B 1 161 ? -30.488 -3.458  11.839  1.00 14.80 ? 161 ARG B O   1 
ATOM   4981 C  CB  . ARG B 1 161 ? -30.251 -3.520  8.907   1.00 18.77 ? 161 ARG B CB  1 
ATOM   4982 C  CG  . ARG B 1 161 ? -30.445 -3.847  7.433   1.00 19.26 ? 161 ARG B CG  1 
ATOM   4983 C  CD  . ARG B 1 161 ? -29.744 -2.867  6.536   1.00 18.73 ? 161 ARG B CD  1 
ATOM   4984 N  NE  . ARG B 1 161 ? -29.890 -3.198  5.133   1.00 19.01 ? 161 ARG B NE  1 
ATOM   4985 C  CZ  . ARG B 1 161 ? -28.990 -3.819  4.379   1.00 19.01 ? 161 ARG B CZ  1 
ATOM   4986 N  NH1 . ARG B 1 161 ? -27.827 -4.224  4.866   1.00 20.66 ? 161 ARG B NH1 1 
ATOM   4987 N  NH2 . ARG B 1 161 ? -29.246 -4.003  3.102   1.00 18.03 ? 161 ARG B NH2 1 
ATOM   4988 N  N   . PHE B 1 162 ? -29.619 -5.523  11.832  1.00 18.22 ? 162 PHE B N   1 
ATOM   4989 C  CA  . PHE B 1 162 ? -28.972 -5.420  13.168  1.00 18.09 ? 162 PHE B CA  1 
ATOM   4990 C  C   . PHE B 1 162 ? -27.758 -4.487  13.085  1.00 18.36 ? 162 PHE B C   1 
ATOM   4991 O  O   . PHE B 1 162 ? -27.322 -3.952  14.116  1.00 16.13 ? 162 PHE B O   1 
ATOM   4992 C  CB  . PHE B 1 162 ? -28.595 -6.793  13.713  1.00 16.99 ? 162 PHE B CB  1 
ATOM   4993 C  CG  . PHE B 1 162 ? -29.795 -7.533  14.221  1.00 16.53 ? 162 PHE B CG  1 
ATOM   4994 C  CD1 . PHE B 1 162 ? -30.291 -7.266  15.492  1.00 16.34 ? 162 PHE B CD1 1 
ATOM   4995 C  CD2 . PHE B 1 162 ? -30.448 -8.446  13.411  1.00 15.70 ? 162 PHE B CD2 1 
ATOM   4996 C  CE1 . PHE B 1 162 ? -31.397 -7.949  15.970  1.00 16.11 ? 162 PHE B CE1 1 
ATOM   4997 C  CE2 . PHE B 1 162 ? -31.561 -9.119  13.888  1.00 16.41 ? 162 PHE B CE2 1 
ATOM   4998 C  CZ  . PHE B 1 162 ? -32.034 -8.861  15.164  1.00 16.62 ? 162 PHE B CZ  1 
ATOM   4999 N  N   . ASN B 1 163 ? -27.237 -4.284  11.879  1.00 19.59 ? 163 ASN B N   1 
ATOM   5000 C  CA  . ASN B 1 163 ? -26.121 -3.339  11.653  1.00 20.89 ? 163 ASN B CA  1 
ATOM   5001 C  C   . ASN B 1 163 ? -24.986 -3.713  12.618  1.00 22.16 ? 163 ASN B C   1 
ATOM   5002 O  O   . ASN B 1 163 ? -24.390 -2.810  13.247  1.00 25.86 ? 163 ASN B O   1 
ATOM   5003 C  CB  . ASN B 1 163 ? -26.631 -1.899  11.754  1.00 21.04 ? 163 ASN B CB  1 
ATOM   5004 C  CG  . ASN B 1 163 ? -27.399 -1.505  10.513  1.00 21.53 ? 163 ASN B CG  1 
ATOM   5005 O  OD1 . ASN B 1 163 ? -26.976 -1.814  9.393   1.00 22.08 ? 163 ASN B OD1 1 
ATOM   5006 N  ND2 . ASN B 1 163 ? -28.519 -0.822  10.700  1.00 21.68 ? 163 ASN B ND2 1 
ATOM   5007 N  N   . SER B 1 164 ? -24.674 -5.002  12.705  1.00 21.03 ? 164 SER B N   1 
ATOM   5008 C  CA  . SER B 1 164 ? -23.777 -5.564  13.740  1.00 23.16 ? 164 SER B CA  1 
ATOM   5009 C  C   . SER B 1 164 ? -22.339 -5.044  13.583  1.00 25.37 ? 164 SER B C   1 
ATOM   5010 O  O   . SER B 1 164 ? -21.564 -5.091  14.577  1.00 25.63 ? 164 SER B O   1 
ATOM   5011 C  CB  . SER B 1 164 ? -23.847 -7.059  13.712  1.00 22.61 ? 164 SER B CB  1 
ATOM   5012 O  OG  . SER B 1 164 ? -25.051 -7.485  14.327  1.00 23.17 ? 164 SER B OG  1 
ATOM   5013 N  N   . PHE B 1 165 ? -21.959 -4.590  12.389  1.00 25.55 ? 165 PHE B N   1 
ATOM   5014 C  CA  . PHE B 1 165 ? -20.596 -4.071  12.138  1.00 25.05 ? 165 PHE B CA  1 
ATOM   5015 C  C   . PHE B 1 165 ? -20.528 -2.580  12.501  1.00 25.13 ? 165 PHE B C   1 
ATOM   5016 O  O   . PHE B 1 165 ? -19.378 -2.047  12.550  1.00 25.33 ? 165 PHE B O   1 
ATOM   5017 C  CB  . PHE B 1 165 ? -20.176 -4.354  10.700  1.00 24.67 ? 165 PHE B CB  1 
ATOM   5018 C  CG  . PHE B 1 165 ? -19.999 -5.815  10.386  1.00 27.03 ? 165 PHE B CG  1 
ATOM   5019 C  CD1 . PHE B 1 165 ? -19.239 -6.633  11.209  1.00 26.44 ? 165 PHE B CD1 1 
ATOM   5020 C  CD2 . PHE B 1 165 ? -20.581 -6.368  9.255   1.00 26.69 ? 165 PHE B CD2 1 
ATOM   5021 C  CE1 . PHE B 1 165 ? -19.081 -7.977  10.917  1.00 26.35 ? 165 PHE B CE1 1 
ATOM   5022 C  CE2 . PHE B 1 165 ? -20.415 -7.708  8.968   1.00 26.78 ? 165 PHE B CE2 1 
ATOM   5023 C  CZ  . PHE B 1 165 ? -19.663 -8.510  9.797   1.00 26.83 ? 165 PHE B CZ  1 
ATOM   5024 N  N   . TYR B 1 166 ? -21.670 -1.949  12.805  1.00 25.21 ? 166 TYR B N   1 
ATOM   5025 C  CA  . TYR B 1 166 ? -21.763 -0.500  13.129  1.00 29.11 ? 166 TYR B CA  1 
ATOM   5026 C  C   . TYR B 1 166 ? -21.831 -0.280  14.642  1.00 32.84 ? 166 TYR B C   1 
ATOM   5027 O  O   . TYR B 1 166 ? -21.770 0.879   15.129  1.00 35.30 ? 166 TYR B O   1 
ATOM   5028 C  CB  . TYR B 1 166 ? -22.958 0.144   12.430  1.00 28.11 ? 166 TYR B CB  1 
ATOM   5029 C  CG  . TYR B 1 166 ? -22.830 0.212   10.933  1.00 28.26 ? 166 TYR B CG  1 
ATOM   5030 C  CD1 . TYR B 1 166 ? -22.176 1.265   10.325  1.00 28.80 ? 166 TYR B CD1 1 
ATOM   5031 C  CD2 . TYR B 1 166 ? -23.350 -0.778  10.122  1.00 29.72 ? 166 TYR B CD2 1 
ATOM   5032 C  CE1 . TYR B 1 166 ? -22.076 1.356   8.945   1.00 29.69 ? 166 TYR B CE1 1 
ATOM   5033 C  CE2 . TYR B 1 166 ? -23.237 -0.716  8.741   1.00 31.95 ? 166 TYR B CE2 1 
ATOM   5034 C  CZ  . TYR B 1 166 ? -22.605 0.363   8.148   1.00 29.07 ? 166 TYR B CZ  1 
ATOM   5035 O  OH  . TYR B 1 166 ? -22.503 0.446   6.797   1.00 25.71 ? 166 TYR B OH  1 
ATOM   5036 N  N   . ARG B 1 167 ? -21.919 -1.353  15.408  1.00 37.75 ? 167 ARG B N   1 
ATOM   5037 C  CA  . ARG B 1 167 ? -21.990 -1.213  16.881  1.00 44.83 ? 167 ARG B CA  1 
ATOM   5038 C  C   . ARG B 1 167 ? -20.971 -2.156  17.503  1.00 50.31 ? 167 ARG B C   1 
ATOM   5039 O  O   . ARG B 1 167 ? -20.404 -3.005  16.780  1.00 56.82 ? 167 ARG B O   1 
ATOM   5040 C  CB  . ARG B 1 167 ? -23.419 -1.476  17.357  1.00 45.96 ? 167 ARG B CB  1 
ATOM   5041 C  CG  . ARG B 1 167 ? -24.111 -2.601  16.606  1.00 45.84 ? 167 ARG B CG  1 
ATOM   5042 C  CD  . ARG B 1 167 ? -25.245 -3.203  17.388  1.00 47.06 ? 167 ARG B CD  1 
ATOM   5043 N  NE  . ARG B 1 167 ? -26.532 -2.674  16.982  1.00 48.19 ? 167 ARG B NE  1 
ATOM   5044 C  CZ  . ARG B 1 167 ? -27.503 -2.309  17.809  1.00 48.07 ? 167 ARG B CZ  1 
ATOM   5045 N  NH1 . ARG B 1 167 ? -27.352 -2.372  19.125  1.00 48.46 ? 167 ARG B NH1 1 
ATOM   5046 N  NH2 . ARG B 1 167 ? -28.630 -1.851  17.304  1.00 50.22 ? 167 ARG B NH2 1 
ATOM   5047 N  N   . ASP B 1 168 ? -20.705 -1.936  18.782  1.00 56.63 ? 168 ASP B N   1 
ATOM   5048 C  CA  . ASP B 1 168 ? -19.940 -2.840  19.677  1.00 60.99 ? 168 ASP B CA  1 
ATOM   5049 C  C   . ASP B 1 168 ? -21.004 -3.427  20.615  1.00 60.25 ? 168 ASP B C   1 
ATOM   5050 O  O   . ASP B 1 168 ? -21.270 -4.648  20.514  1.00 53.65 ? 168 ASP B O   1 
ATOM   5051 C  CB  . ASP B 1 168 ? -18.786 -2.025  20.286  1.00 61.27 ? 168 ASP B CB  1 
ATOM   5052 C  CG  . ASP B 1 168 ? -17.712 -2.799  21.027  1.00 60.77 ? 168 ASP B CG  1 
ATOM   5053 O  OD1 . ASP B 1 168 ? -17.897 -3.037  22.238  1.00 61.92 ? 168 ASP B OD1 1 
ATOM   5054 O  OD2 . ASP B 1 168 ? -16.680 -3.104  20.400  1.00 56.28 ? 168 ASP B OD2 1 
ATOM   5055 N  N   . GLN B 1 169 ? -21.622 -2.523  21.398  1.00 63.38 ? 169 GLN B N   1 
ATOM   5056 C  CA  . GLN B 1 169 ? -22.935 -2.613  22.098  1.00 62.34 ? 169 GLN B CA  1 
ATOM   5057 C  C   . GLN B 1 169 ? -23.937 -3.433  21.297  1.00 59.46 ? 169 GLN B C   1 
ATOM   5058 O  O   . GLN B 1 169 ? -24.327 -3.039  20.201  1.00 56.12 ? 169 GLN B O   1 
ATOM   5059 C  CB  . GLN B 1 169 ? -23.507 -1.205  22.282  1.00 64.98 ? 169 GLN B CB  1 
ATOM   5060 C  CG  . GLN B 1 169 ? -25.028 -1.130  22.329  1.00 63.61 ? 169 GLN B CG  1 
ATOM   5061 C  CD  . GLN B 1 169 ? -25.496 0.245   22.745  1.00 66.94 ? 169 GLN B CD  1 
ATOM   5062 O  OE1 . GLN B 1 169 ? -24.936 1.264   22.343  1.00 73.56 ? 169 GLN B OE1 1 
ATOM   5063 N  NE2 . GLN B 1 169 ? -26.541 0.287   23.555  1.00 65.98 ? 169 GLN B NE2 1 
ATOM   5064 N  N   . PRO B 1 170 ? -24.444 -4.548  21.863  1.00 51.90 ? 170 PRO B N   1 
ATOM   5065 C  CA  . PRO B 1 170 ? -25.456 -5.358  21.195  1.00 47.36 ? 170 PRO B CA  1 
ATOM   5066 C  C   . PRO B 1 170 ? -26.888 -4.785  21.290  1.00 43.82 ? 170 PRO B C   1 
ATOM   5067 O  O   . PRO B 1 170 ? -27.191 -4.028  22.219  1.00 36.23 ? 170 PRO B O   1 
ATOM   5068 C  CB  . PRO B 1 170 ? -25.312 -6.700  21.929  1.00 50.95 ? 170 PRO B CB  1 
ATOM   5069 C  CG  . PRO B 1 170 ? -24.945 -6.302  23.337  1.00 51.52 ? 170 PRO B CG  1 
ATOM   5070 C  CD  . PRO B 1 170 ? -24.091 -5.062  23.194  1.00 52.74 ? 170 PRO B CD  1 
ATOM   5071 N  N   . HIS B 1 171 ? -27.718 -5.156  20.298  1.00 36.70 ? 171 HIS B N   1 
ATOM   5072 C  CA  . HIS B 1 171 ? -29.173 -4.886  20.187  1.00 33.23 ? 171 HIS B CA  1 
ATOM   5073 C  C   . HIS B 1 171 ? -29.902 -5.546  21.366  1.00 34.00 ? 171 HIS B C   1 
ATOM   5074 O  O   . HIS B 1 171 ? -29.561 -6.666  21.755  1.00 29.20 ? 171 HIS B O   1 
ATOM   5075 C  CB  . HIS B 1 171 ? -29.634 -5.359  18.810  1.00 32.06 ? 171 HIS B CB  1 
ATOM   5076 C  CG  . HIS B 1 171 ? -31.036 -4.985  18.482  1.00 33.98 ? 171 HIS B CG  1 
ATOM   5077 N  ND1 . HIS B 1 171 ? -32.105 -5.726  18.921  1.00 31.47 ? 171 HIS B ND1 1 
ATOM   5078 C  CD2 . HIS B 1 171 ? -31.548 -3.966  17.752  1.00 34.95 ? 171 HIS B CD2 1 
ATOM   5079 C  CE1 . HIS B 1 171 ? -33.226 -5.165  18.496  1.00 34.34 ? 171 HIS B CE1 1 
ATOM   5080 N  NE2 . HIS B 1 171 ? -32.913 -4.096  17.766  1.00 35.62 ? 171 HIS B NE2 1 
ATOM   5081 N  N   . PRO B 1 172 ? -30.889 -4.870  22.016  1.00 31.88 ? 172 PRO B N   1 
ATOM   5082 C  CA  . PRO B 1 172 ? -31.463 -5.362  23.279  1.00 31.20 ? 172 PRO B CA  1 
ATOM   5083 C  C   . PRO B 1 172 ? -32.029 -6.793  23.168  1.00 27.91 ? 172 PRO B C   1 
ATOM   5084 O  O   . PRO B 1 172 ? -32.052 -7.523  24.173  1.00 24.67 ? 172 PRO B O   1 
ATOM   5085 C  CB  . PRO B 1 172 ? -32.581 -4.354  23.628  1.00 31.03 ? 172 PRO B CB  1 
ATOM   5086 C  CG  . PRO B 1 172 ? -32.277 -3.118  22.804  1.00 31.89 ? 172 PRO B CG  1 
ATOM   5087 C  CD  . PRO B 1 172 ? -31.489 -3.593  21.596  1.00 32.59 ? 172 PRO B CD  1 
ATOM   5088 N  N   . PHE B 1 173 ? -32.493 -7.165  21.966  1.00 24.31 ? 173 PHE B N   1 
ATOM   5089 C  CA  . PHE B 1 173 ? -33.075 -8.500  21.677  1.00 23.92 ? 173 PHE B CA  1 
ATOM   5090 C  C   . PHE B 1 173 ? -32.015 -9.598  21.869  1.00 24.19 ? 173 PHE B C   1 
ATOM   5091 O  O   . PHE B 1 173 ? -32.316 -10.672 22.450  1.00 23.54 ? 173 PHE B O   1 
ATOM   5092 C  CB  . PHE B 1 173 ? -33.643 -8.563  20.255  1.00 24.96 ? 173 PHE B CB  1 
ATOM   5093 C  CG  . PHE B 1 173 ? -34.191 -9.932  19.937  1.00 24.26 ? 173 PHE B CG  1 
ATOM   5094 C  CD1 . PHE B 1 173 ? -33.345 -10.935 19.501  1.00 21.77 ? 173 PHE B CD1 1 
ATOM   5095 C  CD2 . PHE B 1 173 ? -35.520 -10.242 20.201  1.00 22.51 ? 173 PHE B CD2 1 
ATOM   5096 C  CE1 . PHE B 1 173 ? -33.835 -12.213 19.312  1.00 22.61 ? 173 PHE B CE1 1 
ATOM   5097 C  CE2 . PHE B 1 173 ? -36.007 -11.519 19.988  1.00 21.62 ? 173 PHE B CE2 1 
ATOM   5098 C  CZ  . PHE B 1 173 ? -35.161 -12.503 19.547  1.00 21.44 ? 173 PHE B CZ  1 
ATOM   5099 N  N   . ILE B 1 174 ? -30.800 -9.345  21.379  1.00 23.60 ? 174 ILE B N   1 
ATOM   5100 C  CA  . ILE B 1 174 ? -29.704 -10.358 21.313  1.00 22.51 ? 174 ILE B CA  1 
ATOM   5101 C  C   . ILE B 1 174 ? -29.114 -10.557 22.702  1.00 20.17 ? 174 ILE B C   1 
ATOM   5102 O  O   . ILE B 1 174 ? -28.750 -11.693 23.010  1.00 20.17 ? 174 ILE B O   1 
ATOM   5103 C  CB  . ILE B 1 174 ? -28.652 -9.960  20.267  1.00 23.03 ? 174 ILE B CB  1 
ATOM   5104 C  CG1 . ILE B 1 174 ? -29.274 -9.875  18.868  1.00 24.16 ? 174 ILE B CG1 1 
ATOM   5105 C  CG2 . ILE B 1 174 ? -27.480 -10.914 20.297  1.00 22.40 ? 174 ILE B CG2 1 
ATOM   5106 C  CD1 . ILE B 1 174 ? -29.634 -11.208 18.262  1.00 23.16 ? 174 ILE B CD1 1 
ATOM   5107 N  N   . THR B 1 175 ? -29.035 -9.500  23.503  1.00 19.42 ? 175 THR B N   1 
ATOM   5108 C  CA  . THR B 1 175 ? -28.664 -9.567  24.946  1.00 19.14 ? 175 THR B CA  1 
ATOM   5109 C  C   . THR B 1 175 ? -29.588 -10.590 25.618  1.00 17.93 ? 175 THR B C   1 
ATOM   5110 O  O   . THR B 1 175 ? -29.111 -11.648 26.071  1.00 17.34 ? 175 THR B O   1 
ATOM   5111 C  CB  . THR B 1 175 ? -28.726 -8.175  25.602  1.00 18.96 ? 175 THR B CB  1 
ATOM   5112 O  OG1 . THR B 1 175 ? -27.759 -7.365  24.930  1.00 18.46 ? 175 THR B OG1 1 
ATOM   5113 C  CG2 . THR B 1 175 ? -28.468 -8.182  27.099  1.00 19.18 ? 175 THR B CG2 1 
ATOM   5114 N  N   . SER B 1 176 ? -30.881 -10.316 25.610  1.00 17.79 ? 176 SER B N   1 
ATOM   5115 C  CA  . SER B 1 176 ? -31.906 -11.172 26.252  1.00 18.29 ? 176 SER B CA  1 
ATOM   5116 C  C   . SER B 1 176 ? -31.826 -12.611 25.704  1.00 19.96 ? 176 SER B C   1 
ATOM   5117 O  O   . SER B 1 176 ? -31.894 -13.571 26.548  1.00 19.22 ? 176 SER B O   1 
ATOM   5118 C  CB  . SER B 1 176 ? -33.262 -10.546 26.098  1.00 17.78 ? 176 SER B CB  1 
ATOM   5119 O  OG  . SER B 1 176 ? -33.292 -9.329  26.829  1.00 16.66 ? 176 SER B OG  1 
ATOM   5120 N  N   . MET B 1 177 ? -31.663 -12.781 24.378  1.00 19.39 ? 177 MET B N   1 
ATOM   5121 C  CA  . MET B 1 177 ? -31.667 -14.124 23.719  1.00 20.50 ? 177 MET B CA  1 
ATOM   5122 C  C   . MET B 1 177 ? -30.454 -14.960 24.150  1.00 19.55 ? 177 MET B C   1 
ATOM   5123 O  O   . MET B 1 177 ? -30.613 -16.146 24.550  1.00 17.92 ? 177 MET B O   1 
ATOM   5124 C  CB  . MET B 1 177 ? -31.616 -13.987 22.202  1.00 22.15 ? 177 MET B CB  1 
ATOM   5125 C  CG  . MET B 1 177 ? -31.872 -15.290 21.483  1.00 25.34 ? 177 MET B CG  1 
ATOM   5126 S  SD  . MET B 1 177 ? -31.505 -15.073 19.742  1.00 28.64 ? 177 MET B SD  1 
ATOM   5127 C  CE  . MET B 1 177 ? -29.724 -15.281 19.807  1.00 32.16 ? 177 MET B CE  1 
ATOM   5128 N  N   . VAL B 1 178 ? -29.276 -14.356 24.029  1.00 19.90 ? 178 VAL B N   1 
ATOM   5129 C  CA  . VAL B 1 178 ? -27.963 -14.936 24.427  1.00 20.36 ? 178 VAL B CA  1 
ATOM   5130 C  C   . VAL B 1 178 ? -28.013 -15.408 25.890  1.00 20.23 ? 178 VAL B C   1 
ATOM   5131 O  O   . VAL B 1 178 ? -27.617 -16.586 26.157  1.00 19.82 ? 178 VAL B O   1 
ATOM   5132 C  CB  . VAL B 1 178 ? -26.865 -13.895 24.176  1.00 20.33 ? 178 VAL B CB  1 
ATOM   5133 C  CG1 . VAL B 1 178 ? -25.579 -14.286 24.859  1.00 20.50 ? 178 VAL B CG1 1 
ATOM   5134 C  CG2 . VAL B 1 178 ? -26.655 -13.691 22.680  1.00 21.69 ? 178 VAL B CG2 1 
ATOM   5135 N  N   . ARG B 1 179 ? -28.477 -14.535 26.787  1.00 19.73 ? 179 ARG B N   1 
ATOM   5136 C  CA  . ARG B 1 179 ? -28.663 -14.815 28.239  1.00 20.83 ? 179 ARG B CA  1 
ATOM   5137 C  C   . ARG B 1 179 ? -29.699 -15.944 28.415  1.00 20.48 ? 179 ARG B C   1 
ATOM   5138 O  O   . ARG B 1 179 ? -29.418 -16.954 29.083  1.00 22.13 ? 179 ARG B O   1 
ATOM   5139 C  CB  . ARG B 1 179 ? -29.069 -13.520 28.942  1.00 21.22 ? 179 ARG B CB  1 
ATOM   5140 C  CG  . ARG B 1 179 ? -28.720 -13.456 30.419  1.00 22.87 ? 179 ARG B CG  1 
ATOM   5141 C  CD  . ARG B 1 179 ? -28.561 -12.006 30.826  1.00 23.35 ? 179 ARG B CD  1 
ATOM   5142 N  NE  . ARG B 1 179 ? -29.714 -11.167 30.519  1.00 24.88 ? 179 ARG B NE  1 
ATOM   5143 C  CZ  . ARG B 1 179 ? -29.682 -9.833  30.379  1.00 25.63 ? 179 ARG B CZ  1 
ATOM   5144 N  NH1 . ARG B 1 179 ? -28.545 -9.174  30.498  1.00 24.63 ? 179 ARG B NH1 1 
ATOM   5145 N  NH2 . ARG B 1 179 ? -30.784 -9.148  30.101  1.00 24.65 ? 179 ARG B NH2 1 
ATOM   5146 N  N   . ALA B 1 180 ? -30.847 -15.835 27.775  1.00 19.81 ? 180 ALA B N   1 
ATOM   5147 C  CA  . ALA B 1 180 ? -31.891 -16.879 27.832  1.00 19.69 ? 180 ALA B CA  1 
ATOM   5148 C  C   . ALA B 1 180 ? -31.329 -18.214 27.316  1.00 19.75 ? 180 ALA B C   1 
ATOM   5149 O  O   . ALA B 1 180 ? -31.664 -19.234 27.900  1.00 20.43 ? 180 ALA B O   1 
ATOM   5150 C  CB  . ALA B 1 180 ? -33.099 -16.429 27.050  1.00 19.84 ? 180 ALA B CB  1 
ATOM   5151 N  N   . LEU B 1 181 ? -30.534 -18.240 26.241  1.00 20.94 ? 181 LEU B N   1 
ATOM   5152 C  CA  . LEU B 1 181 ? -29.989 -19.526 25.724  1.00 22.34 ? 181 LEU B CA  1 
ATOM   5153 C  C   . LEU B 1 181 ? -29.055 -20.131 26.778  1.00 24.62 ? 181 LEU B C   1 
ATOM   5154 O  O   . LEU B 1 181 ? -29.035 -21.363 26.949  1.00 22.78 ? 181 LEU B O   1 
ATOM   5155 C  CB  . LEU B 1 181 ? -29.246 -19.302 24.409  1.00 21.42 ? 181 LEU B CB  1 
ATOM   5156 C  CG  . LEU B 1 181 ? -30.143 -19.125 23.188  1.00 20.62 ? 181 LEU B CG  1 
ATOM   5157 C  CD1 . LEU B 1 181 ? -29.405 -18.434 22.052  1.00 19.97 ? 181 LEU B CD1 1 
ATOM   5158 C  CD2 . LEU B 1 181 ? -30.673 -20.467 22.742  1.00 21.56 ? 181 LEU B CD2 1 
ATOM   5159 N  N   . ASP B 1 182 ? -28.306 -19.260 27.443  1.00 27.25 ? 182 ASP B N   1 
ATOM   5160 C  CA  . ASP B 1 182 ? -27.286 -19.628 28.446  1.00 28.14 ? 182 ASP B CA  1 
ATOM   5161 C  C   . ASP B 1 182 ? -27.995 -20.201 29.674  1.00 26.15 ? 182 ASP B C   1 
ATOM   5162 O  O   . ASP B 1 182 ? -27.480 -21.180 30.233  1.00 27.07 ? 182 ASP B O   1 
ATOM   5163 C  CB  . ASP B 1 182 ? -26.432 -18.408 28.787  1.00 31.79 ? 182 ASP B CB  1 
ATOM   5164 C  CG  . ASP B 1 182 ? -25.110 -18.799 29.411  1.00 37.29 ? 182 ASP B CG  1 
ATOM   5165 O  OD1 . ASP B 1 182 ? -24.543 -19.865 29.002  1.00 38.52 ? 182 ASP B OD1 1 
ATOM   5166 O  OD2 . ASP B 1 182 ? -24.665 -18.052 30.308  1.00 40.93 ? 182 ASP B OD2 1 
ATOM   5167 N  N   . GLU B 1 183 ? -29.133 -19.619 30.062  1.00 23.29 ? 183 GLU B N   1 
ATOM   5168 C  CA  . GLU B 1 183 ? -29.933 -20.094 31.219  1.00 22.14 ? 183 GLU B CA  1 
ATOM   5169 C  C   . GLU B 1 183 ? -30.475 -21.486 30.903  1.00 21.87 ? 183 GLU B C   1 
ATOM   5170 O  O   . GLU B 1 183 ? -30.374 -22.383 31.752  1.00 20.91 ? 183 GLU B O   1 
ATOM   5171 C  CB  . GLU B 1 183 ? -31.053 -19.101 31.539  1.00 20.91 ? 183 GLU B CB  1 
ATOM   5172 C  CG  . GLU B 1 183 ? -31.976 -19.578 32.653  1.00 19.84 ? 183 GLU B CG  1 
ATOM   5173 C  CD  . GLU B 1 183 ? -31.341 -19.722 34.030  1.00 19.34 ? 183 GLU B CD  1 
ATOM   5174 O  OE1 . GLU B 1 183 ? -30.131 -19.454 34.172  1.00 19.30 ? 183 GLU B OE1 1 
ATOM   5175 O  OE2 . GLU B 1 183 ? -32.052 -20.112 34.957  1.00 17.75 ? 183 GLU B OE2 1 
ATOM   5176 N  N   . ALA B 1 184 ? -31.014 -21.667 29.703  1.00 23.15 ? 184 ALA B N   1 
ATOM   5177 C  CA  . ALA B 1 184 ? -31.622 -22.948 29.280  1.00 23.86 ? 184 ALA B CA  1 
ATOM   5178 C  C   . ALA B 1 184 ? -30.536 -24.028 29.172  1.00 25.23 ? 184 ALA B C   1 
ATOM   5179 O  O   . ALA B 1 184 ? -30.833 -25.208 29.509  1.00 28.27 ? 184 ALA B O   1 
ATOM   5180 C  CB  . ALA B 1 184 ? -32.385 -22.784 27.987  1.00 23.29 ? 184 ALA B CB  1 
ATOM   5181 N  N   . MET B 1 185 ? -29.328 -23.681 28.711  1.00 24.83 ? 185 MET B N   1 
ATOM   5182 C  CA  . MET B 1 185 ? -28.222 -24.674 28.620  1.00 25.50 ? 185 MET B CA  1 
ATOM   5183 C  C   . MET B 1 185 ? -27.813 -25.105 30.035  1.00 25.09 ? 185 MET B C   1 
ATOM   5184 O  O   . MET B 1 185 ? -27.519 -26.283 30.217  1.00 25.50 ? 185 MET B O   1 
ATOM   5185 C  CB  . MET B 1 185 ? -27.013 -24.103 27.880  1.00 27.67 ? 185 MET B CB  1 
ATOM   5186 C  CG  . MET B 1 185 ? -27.211 -24.078 26.388  1.00 30.37 ? 185 MET B CG  1 
ATOM   5187 S  SD  . MET B 1 185 ? -27.362 -25.730 25.650  1.00 37.71 ? 185 MET B SD  1 
ATOM   5188 C  CE  . MET B 1 185 ? -25.819 -26.534 26.088  1.00 36.74 ? 185 MET B CE  1 
ATOM   5189 N  N   . ASN B 1 186 ? -27.871 -24.179 30.996  1.00 25.05 ? 186 ASN B N   1 
ATOM   5190 C  CA  . ASN B 1 186 ? -27.384 -24.333 32.395  1.00 24.43 ? 186 ASN B CA  1 
ATOM   5191 C  C   . ASN B 1 186 ? -28.384 -25.075 33.284  1.00 24.82 ? 186 ASN B C   1 
ATOM   5192 O  O   . ASN B 1 186 ? -27.914 -25.840 34.161  1.00 27.78 ? 186 ASN B O   1 
ATOM   5193 C  CB  . ASN B 1 186 ? -27.077 -22.978 33.034  1.00 22.76 ? 186 ASN B CB  1 
ATOM   5194 C  CG  . ASN B 1 186 ? -25.667 -22.554 32.731  1.00 23.90 ? 186 ASN B CG  1 
ATOM   5195 O  OD1 . ASN B 1 186 ? -24.733 -23.346 32.819  1.00 24.37 ? 186 ASN B OD1 1 
ATOM   5196 N  ND2 . ASN B 1 186 ? -25.502 -21.309 32.355  1.00 26.47 ? 186 ASN B ND2 1 
ATOM   5197 N  N   . LYS B 1 187 ? -29.687 -24.842 33.109  1.00 24.09 ? 187 LYS B N   1 
ATOM   5198 C  CA  . LYS B 1 187 ? -30.720 -25.268 34.095  1.00 24.32 ? 187 LYS B CA  1 
ATOM   5199 C  C   . LYS B 1 187 ? -30.594 -26.768 34.353  1.00 22.05 ? 187 LYS B C   1 
ATOM   5200 O  O   . LYS B 1 187 ? -30.709 -27.206 35.480  1.00 19.34 ? 187 LYS B O   1 
ATOM   5201 C  CB  . LYS B 1 187 ? -32.136 -24.920 33.619  1.00 25.34 ? 187 LYS B CB  1 
ATOM   5202 C  CG  . LYS B 1 187 ? -32.683 -23.549 34.003  1.00 25.55 ? 187 LYS B CG  1 
ATOM   5203 C  CD  . LYS B 1 187 ? -33.772 -23.076 33.060  1.00 25.83 ? 187 LYS B CD  1 
ATOM   5204 C  CE  . LYS B 1 187 ? -34.936 -22.411 33.740  1.00 27.83 ? 187 LYS B CE  1 
ATOM   5205 N  NZ  . LYS B 1 187 ? -34.491 -21.292 34.605  1.00 29.53 ? 187 LYS B NZ  1 
ATOM   5206 N  N   . PRO B 1 188 ? -30.426 -27.628 33.328  1.00 22.46 ? 188 PRO B N   1 
ATOM   5207 C  CA  . PRO B 1 188 ? -30.440 -29.076 33.562  1.00 21.97 ? 188 PRO B CA  1 
ATOM   5208 C  C   . PRO B 1 188 ? -29.355 -29.606 34.513  1.00 21.88 ? 188 PRO B C   1 
ATOM   5209 O  O   . PRO B 1 188 ? -29.560 -30.695 35.040  1.00 20.50 ? 188 PRO B O   1 
ATOM   5210 C  CB  . PRO B 1 188 ? -30.252 -29.685 32.164  1.00 22.56 ? 188 PRO B CB  1 
ATOM   5211 C  CG  . PRO B 1 188 ? -30.717 -28.600 31.213  1.00 22.85 ? 188 PRO B CG  1 
ATOM   5212 C  CD  . PRO B 1 188 ? -30.370 -27.287 31.900  1.00 22.91 ? 188 PRO B CD  1 
ATOM   5213 N  N   . GLN B 1 189 ? -28.285 -28.823 34.740  1.00 21.28 ? 189 GLN B N   1 
ATOM   5214 C  CA  . GLN B 1 189 ? -27.083 -29.234 35.508  1.00 21.39 ? 189 GLN B CA  1 
ATOM   5215 C  C   . GLN B 1 189 ? -27.178 -28.795 36.973  1.00 21.75 ? 189 GLN B C   1 
ATOM   5216 O  O   . GLN B 1 189 ? -26.253 -29.073 37.683  1.00 21.21 ? 189 GLN B O   1 
ATOM   5217 C  CB  . GLN B 1 189 ? -25.823 -28.710 34.832  1.00 21.44 ? 189 GLN B CB  1 
ATOM   5218 C  CG  . GLN B 1 189 ? -25.534 -29.449 33.530  1.00 22.43 ? 189 GLN B CG  1 
ATOM   5219 C  CD  . GLN B 1 189 ? -26.171 -28.840 32.299  1.00 23.95 ? 189 GLN B CD  1 
ATOM   5220 O  OE1 . GLN B 1 189 ? -26.887 -29.498 31.538  1.00 24.45 ? 189 GLN B OE1 1 
ATOM   5221 N  NE2 . GLN B 1 189 ? -25.894 -27.565 32.087  1.00 24.13 ? 189 GLN B NE2 1 
ATOM   5222 N  N   . ARG B 1 190 ? -28.298 -28.242 37.424  1.00 24.19 ? 190 ARG B N   1 
ATOM   5223 C  CA  . ARG B 1 190 ? -28.478 -27.747 38.819  1.00 26.17 ? 190 ARG B CA  1 
ATOM   5224 C  C   . ARG B 1 190 ? -29.094 -28.863 39.673  1.00 27.10 ? 190 ARG B C   1 
ATOM   5225 O  O   . ARG B 1 190 ? -30.253 -29.250 39.436  1.00 30.74 ? 190 ARG B O   1 
ATOM   5226 C  CB  . ARG B 1 190 ? -29.336 -26.476 38.826  1.00 25.24 ? 190 ARG B CB  1 
ATOM   5227 C  CG  . ARG B 1 190 ? -28.667 -25.295 38.139  1.00 25.20 ? 190 ARG B CG  1 
ATOM   5228 C  CD  . ARG B 1 190 ? -29.611 -24.148 37.868  1.00 24.92 ? 190 ARG B CD  1 
ATOM   5229 N  NE  . ARG B 1 190 ? -28.975 -23.084 37.113  1.00 24.42 ? 190 ARG B NE  1 
ATOM   5230 C  CZ  . ARG B 1 190 ? -29.607 -22.010 36.642  1.00 24.28 ? 190 ARG B CZ  1 
ATOM   5231 N  NH1 . ARG B 1 190 ? -30.906 -21.846 36.837  1.00 23.54 ? 190 ARG B NH1 1 
ATOM   5232 N  NH2 . ARG B 1 190 ? -28.929 -21.085 35.983  1.00 23.38 ? 190 ARG B NH2 1 
ATOM   5233 N  N   . ALA B 1 191 ? -28.322 -29.375 40.623  1.00 29.64 ? 191 ALA B N   1 
ATOM   5234 C  CA  . ALA B 1 191 ? -28.745 -30.417 41.586  1.00 30.26 ? 191 ALA B CA  1 
ATOM   5235 C  C   . ALA B 1 191 ? -30.007 -29.923 42.302  1.00 29.07 ? 191 ALA B C   1 
ATOM   5236 O  O   . ALA B 1 191 ? -31.014 -30.688 42.375  1.00 29.54 ? 191 ALA B O   1 
ATOM   5237 C  CB  . ALA B 1 191 ? -27.618 -30.725 42.551  1.00 30.79 ? 191 ALA B CB  1 
ATOM   5238 N  N   . ASN B 1 192 ? -29.995 -28.663 42.725  1.00 26.34 ? 192 ASN B N   1 
ATOM   5239 C  CA  . ASN B 1 192 ? -31.160 -28.075 43.418  1.00 27.93 ? 192 ASN B CA  1 
ATOM   5240 C  C   . ASN B 1 192 ? -31.601 -26.827 42.665  1.00 27.46 ? 192 ASN B C   1 
ATOM   5241 O  O   . ASN B 1 192 ? -31.072 -25.739 42.903  1.00 25.29 ? 192 ASN B O   1 
ATOM   5242 C  CB  . ASN B 1 192 ? -30.882 -27.818 44.899  1.00 27.20 ? 192 ASN B CB  1 
ATOM   5243 C  CG  . ASN B 1 192 ? -32.096 -27.201 45.556  1.00 26.99 ? 192 ASN B CG  1 
ATOM   5244 O  OD1 . ASN B 1 192 ? -33.211 -27.368 45.068  1.00 23.18 ? 192 ASN B OD1 1 
ATOM   5245 N  ND2 . ASN B 1 192 ? -31.880 -26.460 46.626  1.00 26.74 ? 192 ASN B ND2 1 
ATOM   5246 N  N   . PRO B 1 193 ? -32.609 -26.950 41.767  1.00 27.58 ? 193 PRO B N   1 
ATOM   5247 C  CA  . PRO B 1 193 ? -33.077 -25.814 40.978  1.00 26.80 ? 193 PRO B CA  1 
ATOM   5248 C  C   . PRO B 1 193 ? -33.617 -24.623 41.785  1.00 25.43 ? 193 PRO B C   1 
ATOM   5249 O  O   . PRO B 1 193 ? -33.546 -23.561 41.256  1.00 26.78 ? 193 PRO B O   1 
ATOM   5250 C  CB  . PRO B 1 193 ? -34.197 -26.404 40.101  1.00 29.53 ? 193 PRO B CB  1 
ATOM   5251 C  CG  . PRO B 1 193 ? -33.921 -27.905 40.082  1.00 29.54 ? 193 PRO B CG  1 
ATOM   5252 C  CD  . PRO B 1 193 ? -33.342 -28.188 41.451  1.00 28.85 ? 193 PRO B CD  1 
ATOM   5253 N  N   . ASP B 1 194 ? -34.117 -24.802 43.013  1.00 27.52 ? 194 ASP B N   1 
ATOM   5254 C  CA  . ASP B 1 194 ? -34.677 -23.690 43.839  1.00 29.73 ? 194 ASP B CA  1 
ATOM   5255 C  C   . ASP B 1 194 ? -33.626 -23.192 44.843  1.00 31.07 ? 194 ASP B C   1 
ATOM   5256 O  O   . ASP B 1 194 ? -34.007 -22.484 45.802  1.00 34.55 ? 194 ASP B O   1 
ATOM   5257 C  CB  . ASP B 1 194 ? -35.951 -24.100 44.588  1.00 32.90 ? 194 ASP B CB  1 
ATOM   5258 C  CG  . ASP B 1 194 ? -36.952 -24.924 43.786  1.00 37.79 ? 194 ASP B CG  1 
ATOM   5259 O  OD1 . ASP B 1 194 ? -36.978 -24.801 42.529  1.00 36.96 ? 194 ASP B OD1 1 
ATOM   5260 O  OD2 . ASP B 1 194 ? -37.704 -25.704 44.426  1.00 45.18 ? 194 ASP B OD2 1 
ATOM   5261 N  N   . ASP B 1 195 ? -32.354 -23.568 44.677  1.00 29.09 ? 195 ASP B N   1 
ATOM   5262 C  CA  . ASP B 1 195 ? -31.241 -22.941 45.432  1.00 28.43 ? 195 ASP B CA  1 
ATOM   5263 C  C   . ASP B 1 195 ? -31.322 -21.435 45.215  1.00 27.11 ? 195 ASP B C   1 
ATOM   5264 O  O   . ASP B 1 195 ? -31.347 -20.987 44.071  1.00 26.60 ? 195 ASP B O   1 
ATOM   5265 C  CB  . ASP B 1 195 ? -29.881 -23.470 44.977  1.00 30.09 ? 195 ASP B CB  1 
ATOM   5266 C  CG  . ASP B 1 195 ? -28.718 -23.062 45.863  1.00 28.24 ? 195 ASP B CG  1 
ATOM   5267 O  OD1 . ASP B 1 195 ? -28.614 -21.876 46.174  1.00 28.38 ? 195 ASP B OD1 1 
ATOM   5268 O  OD2 . ASP B 1 195 ? -27.935 -23.949 46.229  1.00 31.63 ? 195 ASP B OD2 1 
ATOM   5269 N  N   . PRO B 1 196 ? -31.296 -20.598 46.278  1.00 25.45 ? 196 PRO B N   1 
ATOM   5270 C  CA  . PRO B 1 196 ? -31.349 -19.149 46.096  1.00 23.60 ? 196 PRO B CA  1 
ATOM   5271 C  C   . PRO B 1 196 ? -30.291 -18.624 45.109  1.00 22.33 ? 196 PRO B C   1 
ATOM   5272 O  O   . PRO B 1 196 ? -30.467 -17.552 44.583  1.00 19.24 ? 196 PRO B O   1 
ATOM   5273 C  CB  . PRO B 1 196 ? -31.071 -18.582 47.495  1.00 23.55 ? 196 PRO B CB  1 
ATOM   5274 C  CG  . PRO B 1 196 ? -30.466 -19.733 48.265  1.00 24.30 ? 196 PRO B CG  1 
ATOM   5275 C  CD  . PRO B 1 196 ? -31.114 -20.978 47.694  1.00 26.00 ? 196 PRO B CD  1 
ATOM   5276 N  N   . ALA B 1 197 ? -29.200 -19.362 44.894  1.00 22.10 ? 197 ALA B N   1 
ATOM   5277 C  CA  . ALA B 1 197 ? -28.172 -18.965 43.902  1.00 23.43 ? 197 ALA B CA  1 
ATOM   5278 C  C   . ALA B 1 197 ? -28.848 -18.748 42.543  1.00 21.75 ? 197 ALA B C   1 
ATOM   5279 O  O   . ALA B 1 197 ? -28.327 -17.995 41.757  1.00 22.57 ? 197 ALA B O   1 
ATOM   5280 C  CB  . ALA B 1 197 ? -27.045 -19.987 43.808  1.00 23.10 ? 197 ALA B CB  1 
ATOM   5281 N  N   . TYR B 1 198 ? -29.971 -19.386 42.253  1.00 21.30 ? 198 TYR B N   1 
ATOM   5282 C  CA  . TYR B 1 198 ? -30.561 -19.299 40.895  1.00 22.97 ? 198 TYR B CA  1 
ATOM   5283 C  C   . TYR B 1 198 ? -31.697 -18.263 40.863  1.00 24.22 ? 198 TYR B C   1 
ATOM   5284 O  O   . TYR B 1 198 ? -32.257 -18.018 39.760  1.00 24.19 ? 198 TYR B O   1 
ATOM   5285 C  CB  . TYR B 1 198 ? -30.926 -20.699 40.423  1.00 21.63 ? 198 TYR B CB  1 
ATOM   5286 C  CG  . TYR B 1 198 ? -29.812 -21.705 40.576  1.00 24.60 ? 198 TYR B CG  1 
ATOM   5287 C  CD1 . TYR B 1 198 ? -28.578 -21.548 39.949  1.00 25.64 ? 198 TYR B CD1 1 
ATOM   5288 C  CD2 . TYR B 1 198 ? -30.001 -22.849 41.332  1.00 26.70 ? 198 TYR B CD2 1 
ATOM   5289 C  CE1 . TYR B 1 198 ? -27.565 -22.489 40.082  1.00 24.46 ? 198 TYR B CE1 1 
ATOM   5290 C  CE2 . TYR B 1 198 ? -29.014 -23.814 41.449  1.00 27.13 ? 198 TYR B CE2 1 
ATOM   5291 C  CZ  . TYR B 1 198 ? -27.791 -23.629 40.831  1.00 26.79 ? 198 TYR B CZ  1 
ATOM   5292 O  OH  . TYR B 1 198 ? -26.856 -24.615 40.973  1.00 26.55 ? 198 TYR B OH  1 
ATOM   5293 N  N   . ASP B 1 199 ? -32.007 -17.624 41.995  1.00 24.29 ? 199 ASP B N   1 
ATOM   5294 C  CA  . ASP B 1 199 ? -33.175 -16.713 42.082  1.00 25.90 ? 199 ASP B CA  1 
ATOM   5295 C  C   . ASP B 1 199 ? -33.052 -15.642 40.995  1.00 26.00 ? 199 ASP B C   1 
ATOM   5296 O  O   . ASP B 1 199 ? -34.055 -15.453 40.310  1.00 25.98 ? 199 ASP B O   1 
ATOM   5297 C  CB  . ASP B 1 199 ? -33.388 -16.134 43.482  1.00 28.30 ? 199 ASP B CB  1 
ATOM   5298 C  CG  . ASP B 1 199 ? -34.088 -17.094 44.442  1.00 31.30 ? 199 ASP B CG  1 
ATOM   5299 O  OD1 . ASP B 1 199 ? -34.399 -18.237 44.040  1.00 31.74 ? 199 ASP B OD1 1 
ATOM   5300 O  OD2 . ASP B 1 199 ? -34.301 -16.702 45.603  1.00 36.39 ? 199 ASP B OD2 1 
ATOM   5301 N  N   . GLU B 1 200 ? -31.901 -14.977 40.825  1.00 25.61 ? 200 GLU B N   1 
ATOM   5302 C  CA  . GLU B 1 200 ? -31.784 -13.851 39.853  1.00 30.01 ? 200 GLU B CA  1 
ATOM   5303 C  C   . GLU B 1 200 ? -31.794 -14.408 38.422  1.00 28.51 ? 200 GLU B C   1 
ATOM   5304 O  O   . GLU B 1 200 ? -32.304 -13.710 37.528  1.00 29.75 ? 200 GLU B O   1 
ATOM   5305 C  CB  . GLU B 1 200 ? -30.550 -12.975 40.103  1.00 33.80 ? 200 GLU B CB  1 
ATOM   5306 C  CG  . GLU B 1 200 ? -30.460 -11.748 39.188  1.00 38.57 ? 200 GLU B CG  1 
ATOM   5307 C  CD  . GLU B 1 200 ? -31.615 -10.742 39.227  1.00 45.70 ? 200 GLU B CD  1 
ATOM   5308 O  OE1 . GLU B 1 200 ? -32.253 -10.591 40.309  1.00 51.81 ? 200 GLU B OE1 1 
ATOM   5309 O  OE2 . GLU B 1 200 ? -31.880 -10.087 38.176  1.00 49.09 ? 200 GLU B OE2 1 
ATOM   5310 N  N   . ASN B 1 201 ? -31.182 -15.573 38.202  1.00 26.83 ? 201 ASN B N   1 
ATOM   5311 C  CA  . ASN B 1 201 ? -31.141 -16.249 36.881  1.00 26.77 ? 201 ASN B CA  1 
ATOM   5312 C  C   . ASN B 1 201 ? -32.581 -16.412 36.386  1.00 25.29 ? 201 ASN B C   1 
ATOM   5313 O  O   . ASN B 1 201 ? -32.835 -16.114 35.204  1.00 23.54 ? 201 ASN B O   1 
ATOM   5314 C  CB  . ASN B 1 201 ? -30.452 -17.614 36.954  1.00 28.01 ? 201 ASN B CB  1 
ATOM   5315 C  CG  . ASN B 1 201 ? -29.045 -17.515 37.487  1.00 29.76 ? 201 ASN B CG  1 
ATOM   5316 O  OD1 . ASN B 1 201 ? -28.838 -17.651 38.686  1.00 38.24 ? 201 ASN B OD1 1 
ATOM   5317 N  ND2 . ASN B 1 201 ? -28.096 -17.169 36.635  1.00 29.08 ? 201 ASN B ND2 1 
ATOM   5318 N  N   . LYS B 1 202 ? -33.474 -16.839 37.292  1.00 23.98 ? 202 LYS B N   1 
ATOM   5319 C  CA  . LYS B 1 202 ? -34.909 -17.136 37.020  1.00 24.77 ? 202 LYS B CA  1 
ATOM   5320 C  C   . LYS B 1 202 ? -35.680 -15.835 36.761  1.00 24.71 ? 202 LYS B C   1 
ATOM   5321 O  O   . LYS B 1 202 ? -36.437 -15.811 35.779  1.00 22.95 ? 202 LYS B O   1 
ATOM   5322 C  CB  . LYS B 1 202 ? -35.488 -17.979 38.159  1.00 25.54 ? 202 LYS B CB  1 
ATOM   5323 C  CG  . LYS B 1 202 ? -34.631 -19.190 38.517  1.00 28.36 ? 202 LYS B CG  1 
ATOM   5324 C  CD  . LYS B 1 202 ? -35.367 -20.444 38.897  1.00 28.22 ? 202 LYS B CD  1 
ATOM   5325 C  CE  . LYS B 1 202 ? -35.976 -20.398 40.276  1.00 28.58 ? 202 LYS B CE  1 
ATOM   5326 N  NZ  . LYS B 1 202 ? -35.819 -21.716 40.939  1.00 29.67 ? 202 LYS B NZ  1 
ATOM   5327 N  N   . ARG B 1 203 ? -35.501 -14.795 37.589  1.00 26.09 ? 203 ARG B N   1 
ATOM   5328 C  CA  . ARG B 1 203 ? -36.122 -13.468 37.353  1.00 29.42 ? 203 ARG B CA  1 
ATOM   5329 C  C   . ARG B 1 203 ? -35.661 -12.973 35.983  1.00 27.20 ? 203 ARG B C   1 
ATOM   5330 O  O   . ARG B 1 203 ? -36.529 -12.639 35.170  1.00 23.71 ? 203 ARG B O   1 
ATOM   5331 C  CB  . ARG B 1 203 ? -35.739 -12.440 38.421  1.00 35.24 ? 203 ARG B CB  1 
ATOM   5332 C  CG  . ARG B 1 203 ? -36.357 -12.679 39.793  1.00 40.97 ? 203 ARG B CG  1 
ATOM   5333 C  CD  . ARG B 1 203 ? -35.544 -11.966 40.864  1.00 45.32 ? 203 ARG B CD  1 
ATOM   5334 N  NE  . ARG B 1 203 ? -35.662 -12.531 42.205  1.00 47.89 ? 203 ARG B NE  1 
ATOM   5335 C  CZ  . ARG B 1 203 ? -34.696 -12.525 43.127  1.00 48.25 ? 203 ARG B CZ  1 
ATOM   5336 N  NH1 . ARG B 1 203 ? -33.504 -12.009 42.863  1.00 46.73 ? 203 ARG B NH1 1 
ATOM   5337 N  NH2 . ARG B 1 203 ? -34.927 -13.055 44.316  1.00 51.72 ? 203 ARG B NH2 1 
ATOM   5338 N  N   . GLN B 1 204 ? -34.343 -12.973 35.744  1.00 26.93 ? 204 GLN B N   1 
ATOM   5339 C  CA  . GLN B 1 204 ? -33.730 -12.486 34.474  1.00 29.10 ? 204 GLN B CA  1 
ATOM   5340 C  C   . GLN B 1 204 ? -34.372 -13.223 33.295  1.00 26.60 ? 204 GLN B C   1 
ATOM   5341 O  O   . GLN B 1 204 ? -34.769 -12.549 32.330  1.00 22.98 ? 204 GLN B O   1 
ATOM   5342 C  CB  . GLN B 1 204 ? -32.208 -12.670 34.452  1.00 30.57 ? 204 GLN B CB  1 
ATOM   5343 C  CG  . GLN B 1 204 ? -31.521 -12.055 33.237  1.00 30.91 ? 204 GLN B CG  1 
ATOM   5344 C  CD  . GLN B 1 204 ? -31.820 -10.581 33.086  1.00 34.11 ? 204 GLN B CD  1 
ATOM   5345 O  OE1 . GLN B 1 204 ? -32.775 -10.170 32.435  1.00 36.81 ? 204 GLN B OE1 1 
ATOM   5346 N  NE2 . GLN B 1 204 ? -31.011 -9.748  33.707  1.00 37.52 ? 204 GLN B NE2 1 
ATOM   5347 N  N   . PHE B 1 205 ? -34.477 -14.553 33.413  1.00 26.24 ? 205 PHE B N   1 
ATOM   5348 C  CA  . PHE B 1 205 ? -34.949 -15.481 32.350  1.00 25.24 ? 205 PHE B CA  1 
ATOM   5349 C  C   . PHE B 1 205 ? -36.310 -14.993 31.865  1.00 24.30 ? 205 PHE B C   1 
ATOM   5350 O  O   . PHE B 1 205 ? -36.517 -14.812 30.663  1.00 23.20 ? 205 PHE B O   1 
ATOM   5351 C  CB  . PHE B 1 205 ? -35.032 -16.921 32.869  1.00 24.48 ? 205 PHE B CB  1 
ATOM   5352 C  CG  . PHE B 1 205 ? -35.280 -17.973 31.810  1.00 24.64 ? 205 PHE B CG  1 
ATOM   5353 C  CD1 . PHE B 1 205 ? -34.495 -18.031 30.663  1.00 22.68 ? 205 PHE B CD1 1 
ATOM   5354 C  CD2 . PHE B 1 205 ? -36.276 -18.928 31.973  1.00 24.37 ? 205 PHE B CD2 1 
ATOM   5355 C  CE1 . PHE B 1 205 ? -34.695 -19.014 29.713  1.00 21.68 ? 205 PHE B CE1 1 
ATOM   5356 C  CE2 . PHE B 1 205 ? -36.463 -19.925 31.025  1.00 24.41 ? 205 PHE B CE2 1 
ATOM   5357 C  CZ  . PHE B 1 205 ? -35.671 -19.963 29.895  1.00 22.86 ? 205 PHE B CZ  1 
ATOM   5358 N  N   . GLN B 1 206 ? -37.186 -14.757 32.834  1.00 26.67 ? 206 GLN B N   1 
ATOM   5359 C  CA  . GLN B 1 206 ? -38.584 -14.334 32.635  1.00 28.01 ? 206 GLN B CA  1 
ATOM   5360 C  C   . GLN B 1 206 ? -38.570 -12.974 31.959  1.00 25.85 ? 206 GLN B C   1 
ATOM   5361 O  O   . GLN B 1 206 ? -39.372 -12.779 31.052  1.00 24.80 ? 206 GLN B O   1 
ATOM   5362 C  CB  . GLN B 1 206 ? -39.322 -14.324 33.975  1.00 30.86 ? 206 GLN B CB  1 
ATOM   5363 C  CG  . GLN B 1 206 ? -39.681 -15.714 34.485  1.00 32.83 ? 206 GLN B CG  1 
ATOM   5364 C  CD  . GLN B 1 206 ? -40.501 -16.496 33.481  1.00 37.57 ? 206 GLN B CD  1 
ATOM   5365 O  OE1 . GLN B 1 206 ? -41.259 -15.934 32.679  1.00 39.21 ? 206 GLN B OE1 1 
ATOM   5366 N  NE2 . GLN B 1 206 ? -40.337 -17.813 33.501  1.00 38.33 ? 206 GLN B NE2 1 
ATOM   5367 N  N   . GLU B 1 207 ? -37.696 -12.077 32.405  1.00 28.94 ? 207 GLU B N   1 
ATOM   5368 C  CA  . GLU B 1 207 ? -37.596 -10.706 31.850  1.00 33.07 ? 207 GLU B CA  1 
ATOM   5369 C  C   . GLU B 1 207 ? -37.145 -10.809 30.373  1.00 32.26 ? 207 GLU B C   1 
ATOM   5370 O  O   . GLU B 1 207 ? -37.694 -10.081 29.527  1.00 28.17 ? 207 GLU B O   1 
ATOM   5371 C  CB  . GLU B 1 207 ? -36.682 -9.862  32.735  1.00 39.33 ? 207 GLU B CB  1 
ATOM   5372 C  CG  . GLU B 1 207 ? -36.877 -8.364  32.573  1.00 47.06 ? 207 GLU B CG  1 
ATOM   5373 C  CD  . GLU B 1 207 ? -35.807 -7.522  33.261  1.00 55.14 ? 207 GLU B CD  1 
ATOM   5374 O  OE1 . GLU B 1 207 ? -35.582 -7.720  34.492  1.00 61.32 ? 207 GLU B OE1 1 
ATOM   5375 O  OE2 . GLU B 1 207 ? -35.180 -6.686  32.565  1.00 59.58 ? 207 GLU B OE2 1 
ATOM   5376 N  N   . ASP B 1 208 ? -36.249 -11.744 30.057  1.00 28.30 ? 208 ASP B N   1 
ATOM   5377 C  CA  . ASP B 1 208 ? -35.663 -11.911 28.702  1.00 28.45 ? 208 ASP B CA  1 
ATOM   5378 C  C   . ASP B 1 208 ? -36.722 -12.468 27.739  1.00 27.38 ? 208 ASP B C   1 
ATOM   5379 O  O   . ASP B 1 208 ? -36.830 -11.972 26.589  1.00 25.06 ? 208 ASP B O   1 
ATOM   5380 C  CB  . ASP B 1 208 ? -34.410 -12.791 28.775  1.00 28.43 ? 208 ASP B CB  1 
ATOM   5381 C  CG  . ASP B 1 208 ? -33.225 -12.090 29.422  1.00 26.55 ? 208 ASP B CG  1 
ATOM   5382 O  OD1 . ASP B 1 208 ? -33.087 -10.879 29.238  1.00 26.31 ? 208 ASP B OD1 1 
ATOM   5383 O  OD2 . ASP B 1 208 ? -32.447 -12.761 30.095  1.00 28.33 ? 208 ASP B OD2 1 
ATOM   5384 N  N   . ILE B 1 209 ? -37.477 -13.472 28.175  1.00 26.46 ? 209 ILE B N   1 
ATOM   5385 C  CA  . ILE B 1 209 ? -38.634 -13.993 27.390  1.00 26.22 ? 209 ILE B CA  1 
ATOM   5386 C  C   . ILE B 1 209 ? -39.572 -12.830 27.022  1.00 25.85 ? 209 ILE B C   1 
ATOM   5387 O  O   . ILE B 1 209 ? -39.936 -12.722 25.805  1.00 25.21 ? 209 ILE B O   1 
ATOM   5388 C  CB  . ILE B 1 209 ? -39.358 -15.108 28.151  1.00 26.21 ? 209 ILE B CB  1 
ATOM   5389 C  CG1 . ILE B 1 209 ? -38.464 -16.345 28.296  1.00 26.23 ? 209 ILE B CG1 1 
ATOM   5390 C  CG2 . ILE B 1 209 ? -40.691 -15.446 27.484  1.00 25.19 ? 209 ILE B CG2 1 
ATOM   5391 C  CD1 . ILE B 1 209 ? -38.764 -17.166 29.543  1.00 26.21 ? 209 ILE B CD1 1 
ATOM   5392 N  N   . LYS B 1 210 ? -39.929 -11.994 28.002  1.00 24.43 ? 210 LYS B N   1 
ATOM   5393 C  CA  . LYS B 1 210 ? -40.852 -10.847 27.804  1.00 24.77 ? 210 LYS B CA  1 
ATOM   5394 C  C   . LYS B 1 210 ? -40.279 -9.889  26.751  1.00 22.78 ? 210 LYS B C   1 
ATOM   5395 O  O   . LYS B 1 210 ? -41.056 -9.528  25.865  1.00 23.81 ? 210 LYS B O   1 
ATOM   5396 C  CB  . LYS B 1 210 ? -41.158 -10.117 29.116  1.00 26.91 ? 210 LYS B CB  1 
ATOM   5397 C  CG  . LYS B 1 210 ? -42.280 -10.750 29.937  1.00 33.04 ? 210 LYS B CG  1 
ATOM   5398 C  CD  . LYS B 1 210 ? -42.145 -10.605 31.458  1.00 34.68 ? 210 LYS B CD  1 
ATOM   5399 C  CE  . LYS B 1 210 ? -42.951 -11.627 32.232  1.00 37.37 ? 210 LYS B CE  1 
ATOM   5400 N  NZ  . LYS B 1 210 ? -42.439 -11.781 33.617  1.00 40.83 ? 210 LYS B NZ  1 
ATOM   5401 N  N   . VAL B 1 211 ? -39.001 -9.495  26.849  1.00 21.48 ? 211 VAL B N   1 
ATOM   5402 C  CA  . VAL B 1 211 ? -38.293 -8.587  25.890  1.00 21.90 ? 211 VAL B CA  1 
ATOM   5403 C  C   . VAL B 1 211 ? -38.324 -9.193  24.480  1.00 23.32 ? 211 VAL B C   1 
ATOM   5404 O  O   . VAL B 1 211 ? -38.705 -8.461  23.540  1.00 25.86 ? 211 VAL B O   1 
ATOM   5405 C  CB  . VAL B 1 211 ? -36.846 -8.264  26.332  1.00 23.16 ? 211 VAL B CB  1 
ATOM   5406 C  CG1 . VAL B 1 211 ? -36.012 -7.664  25.204  1.00 24.76 ? 211 VAL B CG1 1 
ATOM   5407 C  CG2 . VAL B 1 211 ? -36.803 -7.314  27.521  1.00 22.44 ? 211 VAL B CG2 1 
ATOM   5408 N  N   . MET B 1 212 ? -37.917 -10.458 24.313  1.00 23.91 ? 212 MET B N   1 
ATOM   5409 C  CA  . MET B 1 212 ? -37.926 -11.147 22.996  1.00 24.06 ? 212 MET B CA  1 
ATOM   5410 C  C   . MET B 1 212 ? -39.364 -11.179 22.445  1.00 26.94 ? 212 MET B C   1 
ATOM   5411 O  O   . MET B 1 212 ? -39.561 -10.933 21.199  1.00 24.19 ? 212 MET B O   1 
ATOM   5412 C  CB  . MET B 1 212 ? -37.376 -12.570 23.099  1.00 23.01 ? 212 MET B CB  1 
ATOM   5413 C  CG  . MET B 1 212 ? -35.893 -12.621 23.420  1.00 22.57 ? 212 MET B CG  1 
ATOM   5414 S  SD  . MET B 1 212 ? -35.235 -14.300 23.271  1.00 22.23 ? 212 MET B SD  1 
ATOM   5415 C  CE  . MET B 1 212 ? -35.422 -14.909 24.948  1.00 20.98 ? 212 MET B CE  1 
ATOM   5416 N  N   . ASN B 1 213 ? -40.361 -11.439 23.304  1.00 27.83 ? 213 ASN B N   1 
ATOM   5417 C  CA  . ASN B 1 213 ? -41.769 -11.584 22.837  1.00 25.91 ? 213 ASN B CA  1 
ATOM   5418 C  C   . ASN B 1 213 ? -42.344 -10.245 22.381  1.00 25.17 ? 213 ASN B C   1 
ATOM   5419 O  O   . ASN B 1 213 ? -43.017 -10.204 21.328  1.00 24.73 ? 213 ASN B O   1 
ATOM   5420 C  CB  . ASN B 1 213 ? -42.657 -12.160 23.916  1.00 25.78 ? 213 ASN B CB  1 
ATOM   5421 C  CG  . ASN B 1 213 ? -42.462 -13.647 24.037  1.00 25.47 ? 213 ASN B CG  1 
ATOM   5422 O  OD1 . ASN B 1 213 ? -41.861 -14.292 23.171  1.00 26.29 ? 213 ASN B OD1 1 
ATOM   5423 N  ND2 . ASN B 1 213 ? -42.943 -14.178 25.145  1.00 25.48 ? 213 ASN B ND2 1 
ATOM   5424 N  N   . ASP B 1 214 ? -42.085 -9.203  23.160  1.00 24.64 ? 214 ASP B N   1 
ATOM   5425 C  CA  . ASP B 1 214 ? -42.469 -7.811  22.855  1.00 25.07 ? 214 ASP B CA  1 
ATOM   5426 C  C   . ASP B 1 214 ? -41.912 -7.397  21.491  1.00 23.49 ? 214 ASP B C   1 
ATOM   5427 O  O   . ASP B 1 214 ? -42.663 -6.820  20.700  1.00 21.14 ? 214 ASP B O   1 
ATOM   5428 C  CB  . ASP B 1 214 ? -41.985 -6.890  23.968  1.00 27.09 ? 214 ASP B CB  1 
ATOM   5429 C  CG  . ASP B 1 214 ? -42.911 -6.900  25.172  1.00 32.45 ? 214 ASP B CG  1 
ATOM   5430 O  OD1 . ASP B 1 214 ? -43.843 -7.759  25.224  1.00 35.97 ? 214 ASP B OD1 1 
ATOM   5431 O  OD2 . ASP B 1 214 ? -42.698 -6.052  26.062  1.00 41.05 ? 214 ASP B OD2 1 
ATOM   5432 N  N   . LEU B 1 215 ? -40.626 -7.647  21.266  1.00 23.99 ? 215 LEU B N   1 
ATOM   5433 C  CA  . LEU B 1 215 ? -39.845 -7.050  20.155  1.00 24.30 ? 215 LEU B CA  1 
ATOM   5434 C  C   . LEU B 1 215 ? -40.233 -7.776  18.866  1.00 22.82 ? 215 LEU B C   1 
ATOM   5435 O  O   . LEU B 1 215 ? -40.422 -7.106  17.831  1.00 24.16 ? 215 LEU B O   1 
ATOM   5436 C  CB  . LEU B 1 215 ? -38.333 -7.118  20.440  1.00 25.06 ? 215 LEU B CB  1 
ATOM   5437 C  CG  . LEU B 1 215 ? -37.773 -6.173  21.513  1.00 27.76 ? 215 LEU B CG  1 
ATOM   5438 C  CD1 . LEU B 1 215 ? -36.260 -6.312  21.574  1.00 28.66 ? 215 LEU B CD1 1 
ATOM   5439 C  CD2 . LEU B 1 215 ? -38.124 -4.703  21.289  1.00 27.15 ? 215 LEU B CD2 1 
ATOM   5440 N  N   . VAL B 1 216 ? -40.424 -9.086  18.922  1.00 22.91 ? 216 VAL B N   1 
ATOM   5441 C  CA  . VAL B 1 216 ? -40.873 -9.832  17.718  1.00 21.90 ? 216 VAL B CA  1 
ATOM   5442 C  C   . VAL B 1 216 ? -42.351 -9.500  17.468  1.00 23.13 ? 216 VAL B C   1 
ATOM   5443 O  O   . VAL B 1 216 ? -42.693 -9.271  16.276  1.00 23.96 ? 216 VAL B O   1 
ATOM   5444 C  CB  . VAL B 1 216 ? -40.542 -11.325 17.839  1.00 22.22 ? 216 VAL B CB  1 
ATOM   5445 C  CG1 . VAL B 1 216 ? -41.211 -12.171 16.758  1.00 22.31 ? 216 VAL B CG1 1 
ATOM   5446 C  CG2 . VAL B 1 216 ? -39.030 -11.524 17.820  1.00 21.40 ? 216 VAL B CG2 1 
ATOM   5447 N  N   . ASP B 1 217 ? -43.180 -9.372  18.518  1.00 24.27 ? 217 ASP B N   1 
ATOM   5448 C  CA  . ASP B 1 217 ? -44.632 -9.048  18.364  1.00 24.57 ? 217 ASP B CA  1 
ATOM   5449 C  C   . ASP B 1 217 ? -44.776 -7.686  17.629  1.00 25.30 ? 217 ASP B C   1 
ATOM   5450 O  O   . ASP B 1 217 ? -45.673 -7.576  16.733  1.00 23.83 ? 217 ASP B O   1 
ATOM   5451 C  CB  . ASP B 1 217 ? -45.394 -9.155  19.698  1.00 24.68 ? 217 ASP B CB  1 
ATOM   5452 C  CG  . ASP B 1 217 ? -45.689 -10.584 20.187  1.00 25.60 ? 217 ASP B CG  1 
ATOM   5453 O  OD1 . ASP B 1 217 ? -45.452 -11.535 19.441  1.00 26.42 ? 217 ASP B OD1 1 
ATOM   5454 O  OD2 . ASP B 1 217 ? -46.172 -10.750 21.320  1.00 25.56 ? 217 ASP B OD2 1 
ATOM   5455 N  N   . LYS B 1 218 ? -43.905 -6.711  17.910  1.00 24.52 ? 218 LYS B N   1 
ATOM   5456 C  CA  . LYS B 1 218 ? -43.930 -5.370  17.263  1.00 28.26 ? 218 LYS B CA  1 
ATOM   5457 C  C   . LYS B 1 218 ? -43.428 -5.475  15.809  1.00 26.64 ? 218 LYS B C   1 
ATOM   5458 O  O   . LYS B 1 218 ? -43.890 -4.718  14.964  1.00 24.62 ? 218 LYS B O   1 
ATOM   5459 C  CB  . LYS B 1 218 ? -43.107 -4.345  18.060  1.00 31.15 ? 218 LYS B CB  1 
ATOM   5460 C  CG  . LYS B 1 218 ? -43.395 -2.887  17.717  1.00 34.81 ? 218 LYS B CG  1 
ATOM   5461 C  CD  . LYS B 1 218 ? -42.691 -1.860  18.618  1.00 38.94 ? 218 LYS B CD  1 
ATOM   5462 C  CE  . LYS B 1 218 ? -41.422 -1.275  18.017  1.00 40.68 ? 218 LYS B CE  1 
ATOM   5463 N  NZ  . LYS B 1 218 ? -41.696 -0.270  16.955  1.00 42.40 ? 218 LYS B NZ  1 
ATOM   5464 N  N   . ILE B 1 219 ? -42.505 -6.384  15.509  1.00 29.31 ? 219 ILE B N   1 
ATOM   5465 C  CA  . ILE B 1 219 ? -42.053 -6.613  14.107  1.00 28.74 ? 219 ILE B CA  1 
ATOM   5466 C  C   . ILE B 1 219 ? -43.230 -7.187  13.298  1.00 25.08 ? 219 ILE B C   1 
ATOM   5467 O  O   . ILE B 1 219 ? -43.408 -6.732  12.180  1.00 22.35 ? 219 ILE B O   1 
ATOM   5468 C  CB  . ILE B 1 219 ? -40.768 -7.470  14.065  1.00 31.35 ? 219 ILE B CB  1 
ATOM   5469 C  CG1 . ILE B 1 219 ? -39.532 -6.569  14.134  1.00 34.43 ? 219 ILE B CG1 1 
ATOM   5470 C  CG2 . ILE B 1 219 ? -40.727 -8.365  12.834  1.00 31.30 ? 219 ILE B CG2 1 
ATOM   5471 C  CD1 . ILE B 1 219 ? -38.290 -7.277  14.608  1.00 39.76 ? 219 ILE B CD1 1 
ATOM   5472 N  N   . ILE B 1 220 ? -44.021 -8.108  13.860  1.00 22.14 ? 220 ILE B N   1 
ATOM   5473 C  CA  . ILE B 1 220 ? -45.163 -8.772  13.159  1.00 22.54 ? 220 ILE B CA  1 
ATOM   5474 C  C   . ILE B 1 220 ? -46.293 -7.741  12.986  1.00 24.13 ? 220 ILE B C   1 
ATOM   5475 O  O   . ILE B 1 220 ? -46.789 -7.567  11.852  1.00 22.72 ? 220 ILE B O   1 
ATOM   5476 C  CB  . ILE B 1 220 ? -45.579 -10.069 13.897  1.00 22.11 ? 220 ILE B CB  1 
ATOM   5477 C  CG1 . ILE B 1 220 ? -44.485 -11.146 13.777  1.00 23.72 ? 220 ILE B CG1 1 
ATOM   5478 C  CG2 . ILE B 1 220 ? -46.918 -10.608 13.418  1.00 20.95 ? 220 ILE B CG2 1 
ATOM   5479 C  CD1 . ILE B 1 220 ? -44.587 -12.270 14.802  1.00 23.29 ? 220 ILE B CD1 1 
ATOM   5480 N  N   . ALA B 1 221 ? -46.632 -7.016  14.051  1.00 25.69 ? 221 ALA B N   1 
ATOM   5481 C  CA  . ALA B 1 221 ? -47.680 -5.971  14.052  1.00 24.71 ? 221 ALA B CA  1 
ATOM   5482 C  C   . ALA B 1 221 ? -47.329 -4.910  13.005  1.00 24.27 ? 221 ALA B C   1 
ATOM   5483 O  O   . ALA B 1 221 ? -48.227 -4.513  12.265  1.00 28.41 ? 221 ALA B O   1 
ATOM   5484 C  CB  . ALA B 1 221 ? -47.824 -5.385  15.436  1.00 24.89 ? 221 ALA B CB  1 
ATOM   5485 N  N   . ASP B 1 222 ? -46.069 -4.484  12.936  1.00 23.38 ? 222 ASP B N   1 
ATOM   5486 C  CA  . ASP B 1 222 ? -45.589 -3.428  12.003  1.00 23.10 ? 222 ASP B CA  1 
ATOM   5487 C  C   . ASP B 1 222 ? -45.643 -3.949  10.559  1.00 22.83 ? 222 ASP B C   1 
ATOM   5488 O  O   . ASP B 1 222 ? -46.039 -3.183  9.641   1.00 22.48 ? 222 ASP B O   1 
ATOM   5489 C  CB  . ASP B 1 222 ? -44.173 -2.957  12.366  1.00 23.76 ? 222 ASP B CB  1 
ATOM   5490 C  CG  . ASP B 1 222 ? -44.067 -2.175  13.667  1.00 25.63 ? 222 ASP B CG  1 
ATOM   5491 O  OD1 . ASP B 1 222 ? -45.113 -1.995  14.336  1.00 31.52 ? 222 ASP B OD1 1 
ATOM   5492 O  OD2 . ASP B 1 222 ? -42.939 -1.757  14.024  1.00 23.10 ? 222 ASP B OD2 1 
ATOM   5493 N  N   . ARG B 1 223 ? -45.252 -5.203  10.329  1.00 23.97 ? 223 ARG B N   1 
ATOM   5494 C  CA  . ARG B 1 223 ? -45.279 -5.779  8.961   1.00 24.37 ? 223 ARG B CA  1 
ATOM   5495 C  C   . ARG B 1 223 ? -46.733 -5.803  8.480   1.00 25.75 ? 223 ARG B C   1 
ATOM   5496 O  O   . ARG B 1 223 ? -46.966 -5.312  7.374   1.00 26.89 ? 223 ARG B O   1 
ATOM   5497 C  CB  . ARG B 1 223 ? -44.660 -7.173  8.905   1.00 23.07 ? 223 ARG B CB  1 
ATOM   5498 C  CG  . ARG B 1 223 ? -44.687 -7.763  7.499   1.00 23.39 ? 223 ARG B CG  1 
ATOM   5499 C  CD  . ARG B 1 223 ? -43.955 -6.908  6.473   1.00 23.51 ? 223 ARG B CD  1 
ATOM   5500 N  NE  . ARG B 1 223 ? -42.531 -6.912  6.780   1.00 25.30 ? 223 ARG B NE  1 
ATOM   5501 C  CZ  . ARG B 1 223 ? -41.670 -7.861  6.424   1.00 26.16 ? 223 ARG B CZ  1 
ATOM   5502 N  NH1 . ARG B 1 223 ? -42.046 -8.880  5.669   1.00 28.61 ? 223 ARG B NH1 1 
ATOM   5503 N  NH2 . ARG B 1 223 ? -40.414 -7.778  6.812   1.00 27.47 ? 223 ARG B NH2 1 
ATOM   5504 N  N   . LYS B 1 224 ? -47.661 -6.312  9.313   1.00 27.11 ? 224 LYS B N   1 
ATOM   5505 C  CA  . LYS B 1 224 ? -49.132 -6.391  9.055   1.00 27.41 ? 224 LYS B CA  1 
ATOM   5506 C  C   . LYS B 1 224 ? -49.696 -4.999  8.746   1.00 27.32 ? 224 LYS B C   1 
ATOM   5507 O  O   . LYS B 1 224 ? -50.413 -4.890  7.725   1.00 24.47 ? 224 LYS B O   1 
ATOM   5508 C  CB  . LYS B 1 224 ? -49.878 -7.023  10.234  1.00 28.44 ? 224 LYS B CB  1 
ATOM   5509 C  CG  . LYS B 1 224 ? -49.874 -8.550  10.223  1.00 30.89 ? 224 LYS B CG  1 
ATOM   5510 C  CD  . LYS B 1 224 ? -49.958 -9.154  11.614  1.00 34.19 ? 224 LYS B CD  1 
ATOM   5511 C  CE  . LYS B 1 224 ? -51.344 -9.124  12.229  1.00 35.65 ? 224 LYS B CE  1 
ATOM   5512 N  NZ  . LYS B 1 224 ? -52.143 -10.304 11.817  1.00 36.19 ? 224 LYS B NZ  1 
ATOM   5513 N  N   . ALA B 1 225 ? -49.358 -3.987  9.556   1.00 24.37 ? 225 ALA B N   1 
ATOM   5514 C  CA  . ALA B 1 225 ? -49.797 -2.587  9.361   1.00 26.87 ? 225 ALA B CA  1 
ATOM   5515 C  C   . ALA B 1 225 ? -49.161 -1.976  8.095   1.00 29.21 ? 225 ALA B C   1 
ATOM   5516 O  O   . ALA B 1 225 ? -49.787 -1.089  7.471   1.00 32.61 ? 225 ALA B O   1 
ATOM   5517 C  CB  . ALA B 1 225 ? -49.483 -1.759  10.590  1.00 26.96 ? 225 ALA B CB  1 
ATOM   5518 N  N   . SER B 1 226 ? -47.951 -2.364  7.716   1.00 28.46 ? 226 SER B N   1 
ATOM   5519 C  CA  . SER B 1 226 ? -47.299 -1.827  6.493   1.00 29.73 ? 226 SER B CA  1 
ATOM   5520 C  C   . SER B 1 226 ? -47.934 -2.468  5.249   1.00 30.30 ? 226 SER B C   1 
ATOM   5521 O  O   . SER B 1 226 ? -48.097 -1.782  4.234   1.00 29.66 ? 226 SER B O   1 
ATOM   5522 C  CB  . SER B 1 226 ? -45.813 -2.032  6.532   1.00 28.81 ? 226 SER B CB  1 
ATOM   5523 O  OG  . SER B 1 226 ? -45.472 -3.284  5.963   1.00 32.46 ? 226 SER B OG  1 
ATOM   5524 N  N   . GLY B 1 227 ? -48.317 -3.737  5.332   1.00 35.46 ? 227 GLY B N   1 
ATOM   5525 C  CA  . GLY B 1 227 ? -48.747 -4.523  4.159   1.00 38.02 ? 227 GLY B CA  1 
ATOM   5526 C  C   . GLY B 1 227 ? -47.614 -4.667  3.146   1.00 42.08 ? 227 GLY B C   1 
ATOM   5527 O  O   . GLY B 1 227 ? -47.915 -4.908  1.957   1.00 39.44 ? 227 GLY B O   1 
ATOM   5528 N  N   . GLU B 1 228 ? -46.350 -4.537  3.582   1.00 45.49 ? 228 GLU B N   1 
ATOM   5529 C  CA  . GLU B 1 228 ? -45.171 -4.521  2.673   1.00 42.13 ? 228 GLU B CA  1 
ATOM   5530 C  C   . GLU B 1 228 ? -44.871 -5.966  2.259   1.00 39.18 ? 228 GLU B C   1 
ATOM   5531 O  O   . GLU B 1 228 ? -45.011 -6.859  3.091   1.00 40.12 ? 228 GLU B O   1 
ATOM   5532 C  CB  . GLU B 1 228 ? -43.973 -3.843  3.345   1.00 45.54 ? 228 GLU B CB  1 
ATOM   5533 C  CG  . GLU B 1 228 ? -42.888 -3.436  2.356   1.00 49.60 ? 228 GLU B CG  1 
ATOM   5534 C  CD  . GLU B 1 228 ? -41.480 -3.228  2.899   1.00 50.58 ? 228 GLU B CD  1 
ATOM   5535 O  OE1 . GLU B 1 228 ? -41.084 -3.942  3.844   1.00 46.00 ? 228 GLU B OE1 1 
ATOM   5536 O  OE2 . GLU B 1 228 ? -40.763 -2.356  2.347   1.00 58.93 ? 228 GLU B OE2 1 
ATOM   5537 N  N   . GLN B 1 229 ? -44.457 -6.174  1.013   1.00 39.21 ? 229 GLN B N   1 
ATOM   5538 C  CA  . GLN B 1 229 ? -44.245 -7.516  0.418   1.00 39.38 ? 229 GLN B CA  1 
ATOM   5539 C  C   . GLN B 1 229 ? -42.752 -7.721  0.174   1.00 36.15 ? 229 GLN B C   1 
ATOM   5540 O  O   . GLN B 1 229 ? -42.360 -7.849  -0.981  1.00 36.14 ? 229 GLN B O   1 
ATOM   5541 C  CB  . GLN B 1 229 ? -45.064 -7.642  -0.873  1.00 41.11 ? 229 GLN B CB  1 
ATOM   5542 C  CG  . GLN B 1 229 ? -46.573 -7.594  -0.653  1.00 40.60 ? 229 GLN B CG  1 
ATOM   5543 C  CD  . GLN B 1 229 ? -47.055 -8.728  0.226   1.00 43.94 ? 229 GLN B CD  1 
ATOM   5544 O  OE1 . GLN B 1 229 ? -46.816 -9.906  -0.050  1.00 44.45 ? 229 GLN B OE1 1 
ATOM   5545 N  NE2 . GLN B 1 229 ? -47.736 -8.380  1.306   1.00 40.06 ? 229 GLN B NE2 1 
ATOM   5546 N  N   . SER B 1 230 ? -41.944 -7.731  1.231   1.00 35.61 ? 230 SER B N   1 
ATOM   5547 C  CA  . SER B 1 230 ? -40.497 -8.039  1.138   1.00 37.03 ? 230 SER B CA  1 
ATOM   5548 C  C   . SER B 1 230 ? -40.356 -9.534  0.842   1.00 38.61 ? 230 SER B C   1 
ATOM   5549 O  O   . SER B 1 230 ? -41.247 -10.310 1.250   1.00 39.49 ? 230 SER B O   1 
ATOM   5550 C  CB  . SER B 1 230 ? -39.742 -7.646  2.378   1.00 38.20 ? 230 SER B CB  1 
ATOM   5551 O  OG  . SER B 1 230 ? -40.427 -6.640  3.105   1.00 39.45 ? 230 SER B OG  1 
ATOM   5552 N  N   . ASP B 1 231 ? -39.295 -9.927  0.141   1.00 39.89 ? 231 ASP B N   1 
ATOM   5553 C  CA  . ASP B 1 231 ? -39.049 -11.349 -0.200  1.00 42.88 ? 231 ASP B CA  1 
ATOM   5554 C  C   . ASP B 1 231 ? -38.262 -11.954 0.975   1.00 39.15 ? 231 ASP B C   1 
ATOM   5555 O  O   . ASP B 1 231 ? -37.054 -12.246 0.832   1.00 37.89 ? 231 ASP B O   1 
ATOM   5556 C  CB  . ASP B 1 231 ? -38.429 -11.475 -1.600  1.00 50.26 ? 231 ASP B CB  1 
ATOM   5557 C  CG  . ASP B 1 231 ? -38.992 -12.634 -2.405  1.00 56.11 ? 231 ASP B CG  1 
ATOM   5558 O  OD1 . ASP B 1 231 ? -39.890 -13.353 -1.879  1.00 53.58 ? 231 ASP B OD1 1 
ATOM   5559 O  OD2 . ASP B 1 231 ? -38.525 -12.815 -3.551  1.00 68.91 ? 231 ASP B OD2 1 
ATOM   5560 N  N   . ASP B 1 232 ? -38.946 -12.121 2.109   1.00 30.82 ? 232 ASP B N   1 
ATOM   5561 C  CA  . ASP B 1 232 ? -38.348 -12.548 3.389   1.00 25.99 ? 232 ASP B CA  1 
ATOM   5562 C  C   . ASP B 1 232 ? -39.295 -13.549 4.050   1.00 24.15 ? 232 ASP B C   1 
ATOM   5563 O  O   . ASP B 1 232 ? -40.487 -13.576 3.678   1.00 23.90 ? 232 ASP B O   1 
ATOM   5564 C  CB  . ASP B 1 232 ? -38.030 -11.333 4.253   1.00 26.96 ? 232 ASP B CB  1 
ATOM   5565 C  CG  . ASP B 1 232 ? -39.210 -10.555 4.826   1.00 28.70 ? 232 ASP B CG  1 
ATOM   5566 O  OD1 . ASP B 1 232 ? -40.252 -11.171 5.149   1.00 30.24 ? 232 ASP B OD1 1 
ATOM   5567 O  OD2 . ASP B 1 232 ? -39.064 -9.322  4.994   1.00 31.22 ? 232 ASP B OD2 1 
ATOM   5568 N  N   . LEU B 1 233 ? -38.779 -14.292 5.028   1.00 21.54 ? 233 LEU B N   1 
ATOM   5569 C  CA  . LEU B 1 233 ? -39.461 -15.427 5.715   1.00 19.79 ? 233 LEU B CA  1 
ATOM   5570 C  C   . LEU B 1 233 ? -40.759 -14.964 6.379   1.00 17.52 ? 233 LEU B C   1 
ATOM   5571 O  O   . LEU B 1 233 ? -41.712 -15.700 6.357   1.00 14.89 ? 233 LEU B O   1 
ATOM   5572 C  CB  . LEU B 1 233 ? -38.496 -16.051 6.728   1.00 18.72 ? 233 LEU B CB  1 
ATOM   5573 C  CG  . LEU B 1 233 ? -37.444 -16.969 6.112   1.00 18.57 ? 233 LEU B CG  1 
ATOM   5574 C  CD1 . LEU B 1 233 ? -36.291 -17.187 7.066   1.00 19.33 ? 233 LEU B CD1 1 
ATOM   5575 C  CD2 . LEU B 1 233 ? -38.043 -18.305 5.727   1.00 19.05 ? 233 LEU B CD2 1 
ATOM   5576 N  N   . LEU B 1 234 ? -40.801 -13.751 6.907   1.00 20.01 ? 234 LEU B N   1 
ATOM   5577 C  CA  . LEU B 1 234 ? -42.017 -13.192 7.567   1.00 20.30 ? 234 LEU B CA  1 
ATOM   5578 C  C   . LEU B 1 234 ? -43.142 -13.003 6.542   1.00 19.64 ? 234 LEU B C   1 
ATOM   5579 O  O   . LEU B 1 234 ? -44.287 -13.216 6.899   1.00 19.90 ? 234 LEU B O   1 
ATOM   5580 C  CB  . LEU B 1 234 ? -41.663 -11.858 8.219   1.00 18.88 ? 234 LEU B CB  1 
ATOM   5581 C  CG  . LEU B 1 234 ? -42.809 -11.152 8.920   1.00 18.44 ? 234 LEU B CG  1 
ATOM   5582 C  CD1 . LEU B 1 234 ? -43.486 -12.049 9.948   1.00 18.85 ? 234 LEU B CD1 1 
ATOM   5583 C  CD2 . LEU B 1 234 ? -42.283 -9.886  9.570   1.00 19.14 ? 234 LEU B CD2 1 
ATOM   5584 N  N   . THR B 1 235 ? -42.821 -12.597 5.320   1.00 21.35 ? 235 THR B N   1 
ATOM   5585 C  CA  . THR B 1 235 ? -43.829 -12.463 4.237   1.00 21.87 ? 235 THR B CA  1 
ATOM   5586 C  C   . THR B 1 235 ? -44.339 -13.867 3.908   1.00 23.43 ? 235 THR B C   1 
ATOM   5587 O  O   . THR B 1 235 ? -45.566 -14.019 3.950   1.00 26.01 ? 235 THR B O   1 
ATOM   5588 C  CB  . THR B 1 235 ? -43.303 -11.721 3.004   1.00 20.53 ? 235 THR B CB  1 
ATOM   5589 O  OG1 . THR B 1 235 ? -42.797 -10.475 3.470   1.00 19.43 ? 235 THR B OG1 1 
ATOM   5590 C  CG2 . THR B 1 235 ? -44.391 -11.484 1.979   1.00 22.04 ? 235 THR B CG2 1 
ATOM   5591 N  N   . HIS B 1 236 ? -43.456 -14.842 3.637   1.00 23.41 ? 236 HIS B N   1 
ATOM   5592 C  CA  . HIS B 1 236 ? -43.850 -16.247 3.317   1.00 26.66 ? 236 HIS B CA  1 
ATOM   5593 C  C   . HIS B 1 236 ? -44.756 -16.787 4.436   1.00 23.17 ? 236 HIS B C   1 
ATOM   5594 O  O   . HIS B 1 236 ? -45.756 -17.450 4.104   1.00 23.57 ? 236 HIS B O   1 
ATOM   5595 C  CB  . HIS B 1 236 ? -42.634 -17.150 2.988   1.00 30.49 ? 236 HIS B CB  1 
ATOM   5596 C  CG  . HIS B 1 236 ? -41.795 -16.606 1.867   1.00 38.26 ? 236 HIS B CG  1 
ATOM   5597 N  ND1 . HIS B 1 236 ? -40.435 -16.871 1.739   1.00 39.31 ? 236 HIS B ND1 1 
ATOM   5598 C  CD2 . HIS B 1 236 ? -42.101 -15.747 0.862   1.00 41.40 ? 236 HIS B CD2 1 
ATOM   5599 C  CE1 . HIS B 1 236 ? -39.958 -16.219 0.693   1.00 42.33 ? 236 HIS B CE1 1 
ATOM   5600 N  NE2 . HIS B 1 236 ? -40.960 -15.529 0.135   1.00 43.14 ? 236 HIS B NE2 1 
ATOM   5601 N  N   . MET B 1 237 ? -44.479 -16.451 5.700   1.00 22.01 ? 237 MET B N   1 
ATOM   5602 C  CA  . MET B 1 237 ? -45.243 -16.956 6.873   1.00 22.59 ? 237 MET B CA  1 
ATOM   5603 C  C   . MET B 1 237 ? -46.612 -16.256 6.993   1.00 23.21 ? 237 MET B C   1 
ATOM   5604 O  O   . MET B 1 237 ? -47.597 -16.940 7.318   1.00 24.59 ? 237 MET B O   1 
ATOM   5605 C  CB  . MET B 1 237 ? -44.435 -16.821 8.170   1.00 21.05 ? 237 MET B CB  1 
ATOM   5606 C  CG  . MET B 1 237 ? -43.382 -17.899 8.291   1.00 20.83 ? 237 MET B CG  1 
ATOM   5607 S  SD  . MET B 1 237 ? -42.627 -17.992 9.916   1.00 22.64 ? 237 MET B SD  1 
ATOM   5608 C  CE  . MET B 1 237 ? -41.562 -16.552 9.843   1.00 21.83 ? 237 MET B CE  1 
ATOM   5609 N  N   . LEU B 1 238 ? -46.699 -14.961 6.714   1.00 22.89 ? 238 LEU B N   1 
ATOM   5610 C  CA  . LEU B 1 238 ? -47.978 -14.212 6.813   1.00 24.05 ? 238 LEU B CA  1 
ATOM   5611 C  C   . LEU B 1 238 ? -48.905 -14.534 5.626   1.00 23.83 ? 238 LEU B C   1 
ATOM   5612 O  O   . LEU B 1 238 ? -50.126 -14.410 5.803   1.00 21.97 ? 238 LEU B O   1 
ATOM   5613 C  CB  . LEU B 1 238 ? -47.651 -12.717 6.907   1.00 24.00 ? 238 LEU B CB  1 
ATOM   5614 C  CG  . LEU B 1 238 ? -47.099 -12.273 8.256   1.00 23.89 ? 238 LEU B CG  1 
ATOM   5615 C  CD1 . LEU B 1 238 ? -46.538 -10.864 8.174   1.00 25.04 ? 238 LEU B CD1 1 
ATOM   5616 C  CD2 . LEU B 1 238 ? -48.163 -12.356 9.341   1.00 22.83 ? 238 LEU B CD2 1 
ATOM   5617 N  N   . ASN B 1 239 ? -48.373 -14.916 4.464   1.00 23.35 ? 239 ASN B N   1 
ATOM   5618 C  CA  . ASN B 1 239 ? -49.191 -15.240 3.259   1.00 26.48 ? 239 ASN B CA  1 
ATOM   5619 C  C   . ASN B 1 239 ? -49.415 -16.750 3.117   1.00 24.31 ? 239 ASN B C   1 
ATOM   5620 O  O   . ASN B 1 239 ? -50.299 -17.118 2.346   1.00 21.77 ? 239 ASN B O   1 
ATOM   5621 C  CB  . ASN B 1 239 ? -48.587 -14.698 1.952   1.00 26.86 ? 239 ASN B CB  1 
ATOM   5622 C  CG  . ASN B 1 239 ? -48.454 -13.195 2.017   1.00 28.10 ? 239 ASN B CG  1 
ATOM   5623 O  OD1 . ASN B 1 239 ? -49.105 -12.578 2.850   1.00 28.86 ? 239 ASN B OD1 1 
ATOM   5624 N  ND2 . ASN B 1 239 ? -47.563 -12.614 1.225   1.00 30.50 ? 239 ASN B ND2 1 
ATOM   5625 N  N   . GLY B 1 240 ? -48.638 -17.573 3.816   1.00 23.97 ? 240 GLY B N   1 
ATOM   5626 C  CA  . GLY B 1 240 ? -48.562 -19.019 3.551   1.00 24.13 ? 240 GLY B CA  1 
ATOM   5627 C  C   . GLY B 1 240 ? -49.809 -19.738 4.018   1.00 23.95 ? 240 GLY B C   1 
ATOM   5628 O  O   . GLY B 1 240 ? -50.414 -19.279 5.002   1.00 25.85 ? 240 GLY B O   1 
ATOM   5629 N  N   . LYS B 1 241 ? -50.164 -20.823 3.330   1.00 25.63 ? 241 LYS B N   1 
ATOM   5630 C  CA  . LYS B 1 241 ? -51.254 -21.758 3.707   1.00 27.35 ? 241 LYS B CA  1 
ATOM   5631 C  C   . LYS B 1 241 ? -50.662 -23.155 3.649   1.00 23.37 ? 241 LYS B C   1 
ATOM   5632 O  O   . LYS B 1 241 ? -49.986 -23.454 2.658   1.00 23.71 ? 241 LYS B O   1 
ATOM   5633 C  CB  . LYS B 1 241 ? -52.451 -21.712 2.752   1.00 31.86 ? 241 LYS B CB  1 
ATOM   5634 C  CG  . LYS B 1 241 ? -53.144 -20.366 2.596   1.00 40.45 ? 241 LYS B CG  1 
ATOM   5635 C  CD  . LYS B 1 241 ? -53.704 -19.769 3.889   1.00 46.82 ? 241 LYS B CD  1 
ATOM   5636 C  CE  . LYS B 1 241 ? -54.078 -18.297 3.773   1.00 51.32 ? 241 LYS B CE  1 
ATOM   5637 N  NZ  . LYS B 1 241 ? -55.534 -18.084 3.587   1.00 51.11 ? 241 LYS B NZ  1 
ATOM   5638 N  N   . ASP B 1 242 ? -50.917 -23.960 4.669   1.00 21.73 ? 242 ASP B N   1 
ATOM   5639 C  CA  . ASP B 1 242 ? -50.446 -25.361 4.750   1.00 21.30 ? 242 ASP B CA  1 
ATOM   5640 C  C   . ASP B 1 242 ? -51.207 -26.129 3.674   1.00 21.71 ? 242 ASP B C   1 
ATOM   5641 O  O   . ASP B 1 242 ? -52.425 -26.172 3.708   1.00 21.88 ? 242 ASP B O   1 
ATOM   5642 C  CB  . ASP B 1 242 ? -50.678 -25.925 6.156   1.00 20.08 ? 242 ASP B CB  1 
ATOM   5643 C  CG  . ASP B 1 242 ? -50.460 -27.426 6.244   1.00 20.28 ? 242 ASP B CG  1 
ATOM   5644 O  OD1 . ASP B 1 242 ? -49.743 -27.963 5.369   1.00 18.36 ? 242 ASP B OD1 1 
ATOM   5645 O  OD2 . ASP B 1 242 ? -50.975 -28.048 7.209   1.00 19.66 ? 242 ASP B OD2 1 
ATOM   5646 N  N   . PRO B 1 243 ? -50.569 -26.786 2.688   1.00 23.54 ? 243 PRO B N   1 
ATOM   5647 C  CA  . PRO B 1 243 ? -51.350 -27.482 1.662   1.00 24.76 ? 243 PRO B CA  1 
ATOM   5648 C  C   . PRO B 1 243 ? -52.240 -28.584 2.254   1.00 25.31 ? 243 PRO B C   1 
ATOM   5649 O  O   . PRO B 1 243 ? -53.317 -28.765 1.722   1.00 26.37 ? 243 PRO B O   1 
ATOM   5650 C  CB  . PRO B 1 243 ? -50.300 -28.049 0.704   1.00 25.38 ? 243 PRO B CB  1 
ATOM   5651 C  CG  . PRO B 1 243 ? -49.075 -27.161 0.981   1.00 27.34 ? 243 PRO B CG  1 
ATOM   5652 C  CD  . PRO B 1 243 ? -49.120 -26.895 2.479   1.00 24.22 ? 243 PRO B CD  1 
ATOM   5653 N  N   . GLU B 1 244 ? -51.821 -29.221 3.357   1.00 25.72 ? 244 GLU B N   1 
ATOM   5654 C  CA  . GLU B 1 244 ? -52.498 -30.407 3.953   1.00 26.85 ? 244 GLU B CA  1 
ATOM   5655 C  C   . GLU B 1 244 ? -53.713 -29.961 4.778   1.00 26.13 ? 244 GLU B C   1 
ATOM   5656 O  O   . GLU B 1 244 ? -54.846 -30.294 4.361   1.00 27.47 ? 244 GLU B O   1 
ATOM   5657 C  CB  . GLU B 1 244 ? -51.504 -31.222 4.774   1.00 28.48 ? 244 GLU B CB  1 
ATOM   5658 C  CG  . GLU B 1 244 ? -52.169 -32.253 5.648   1.00 33.87 ? 244 GLU B CG  1 
ATOM   5659 C  CD  . GLU B 1 244 ? -51.200 -33.044 6.506   1.00 39.11 ? 244 GLU B CD  1 
ATOM   5660 O  OE1 . GLU B 1 244 ? -50.180 -32.474 6.918   1.00 45.10 ? 244 GLU B OE1 1 
ATOM   5661 O  OE2 . GLU B 1 244 ? -51.464 -34.231 6.745   1.00 45.00 ? 244 GLU B OE2 1 
ATOM   5662 N  N   . THR B 1 245 ? -53.529 -29.207 5.864   1.00 23.66 ? 245 THR B N   1 
ATOM   5663 C  CA  . THR B 1 245 ? -54.668 -28.702 6.690   1.00 23.86 ? 245 THR B CA  1 
ATOM   5664 C  C   . THR B 1 245 ? -55.352 -27.494 6.032   1.00 23.68 ? 245 THR B C   1 
ATOM   5665 O  O   . THR B 1 245 ? -56.414 -27.091 6.499   1.00 24.59 ? 245 THR B O   1 
ATOM   5666 C  CB  . THR B 1 245 ? -54.276 -28.270 8.107   1.00 23.14 ? 245 THR B CB  1 
ATOM   5667 O  OG1 . THR B 1 245 ? -53.538 -27.049 8.015   1.00 21.65 ? 245 THR B OG1 1 
ATOM   5668 C  CG2 . THR B 1 245 ? -53.525 -29.335 8.871   1.00 22.67 ? 245 THR B CG2 1 
ATOM   5669 N  N   . GLY B 1 246 ? -54.751 -26.909 5.000   1.00 27.15 ? 246 GLY B N   1 
ATOM   5670 C  CA  . GLY B 1 246 ? -55.301 -25.727 4.305   1.00 23.86 ? 246 GLY B CA  1 
ATOM   5671 C  C   . GLY B 1 246 ? -55.125 -24.461 5.124   1.00 23.73 ? 246 GLY B C   1 
ATOM   5672 O  O   . GLY B 1 246 ? -55.471 -23.383 4.581   1.00 27.76 ? 246 GLY B O   1 
ATOM   5673 N  N   . GLU B 1 247 ? -54.567 -24.544 6.337   1.00 20.53 ? 247 GLU B N   1 
ATOM   5674 C  CA  . GLU B 1 247 ? -54.554 -23.409 7.298   1.00 22.48 ? 247 GLU B CA  1 
ATOM   5675 C  C   . GLU B 1 247 ? -53.289 -22.566 7.196   1.00 23.80 ? 247 GLU B C   1 
ATOM   5676 O  O   . GLU B 1 247 ? -52.206 -23.063 6.865   1.00 24.04 ? 247 GLU B O   1 
ATOM   5677 C  CB  . GLU B 1 247 ? -54.570 -23.883 8.749   1.00 21.66 ? 247 GLU B CB  1 
ATOM   5678 C  CG  . GLU B 1 247 ? -55.848 -24.560 9.159   1.00 21.82 ? 247 GLU B CG  1 
ATOM   5679 C  CD  . GLU B 1 247 ? -55.714 -25.264 10.488  1.00 23.45 ? 247 GLU B CD  1 
ATOM   5680 O  OE1 . GLU B 1 247 ? -56.418 -26.271 10.692  1.00 24.81 ? 247 GLU B OE1 1 
ATOM   5681 O  OE2 . GLU B 1 247 ? -54.848 -24.840 11.293  1.00 22.86 ? 247 GLU B OE2 1 
ATOM   5682 N  N   . PRO B 1 248 ? -53.391 -21.268 7.571   1.00 25.03 ? 248 PRO B N   1 
ATOM   5683 C  CA  . PRO B 1 248 ? -52.216 -20.431 7.816   1.00 23.74 ? 248 PRO B CA  1 
ATOM   5684 C  C   . PRO B 1 248 ? -51.663 -20.580 9.245   1.00 22.17 ? 248 PRO B C   1 
ATOM   5685 O  O   . PRO B 1 248 ? -52.338 -21.094 10.104  1.00 20.76 ? 248 PRO B O   1 
ATOM   5686 C  CB  . PRO B 1 248 ? -52.784 -19.024 7.588   1.00 23.21 ? 248 PRO B CB  1 
ATOM   5687 C  CG  . PRO B 1 248 ? -54.201 -19.122 8.107   1.00 23.51 ? 248 PRO B CG  1 
ATOM   5688 C  CD  . PRO B 1 248 ? -54.650 -20.525 7.761   1.00 23.69 ? 248 PRO B CD  1 
ATOM   5689 N  N   . LEU B 1 249 ? -50.434 -20.110 9.449   1.00 22.45 ? 249 LEU B N   1 
ATOM   5690 C  CA  . LEU B 1 249 ? -49.787 -19.970 10.776  1.00 22.66 ? 249 LEU B CA  1 
ATOM   5691 C  C   . LEU B 1 249 ? -50.463 -18.842 11.552  1.00 23.09 ? 249 LEU B C   1 
ATOM   5692 O  O   . LEU B 1 249 ? -50.696 -17.803 10.923  1.00 21.81 ? 249 LEU B O   1 
ATOM   5693 C  CB  . LEU B 1 249 ? -48.304 -19.640 10.565  1.00 23.93 ? 249 LEU B CB  1 
ATOM   5694 C  CG  . LEU B 1 249 ? -47.433 -20.782 10.050  1.00 23.95 ? 249 LEU B CG  1 
ATOM   5695 C  CD1 . LEU B 1 249 ? -45.952 -20.408 10.093  1.00 24.53 ? 249 LEU B CD1 1 
ATOM   5696 C  CD2 . LEU B 1 249 ? -47.688 -22.053 10.847  1.00 23.51 ? 249 LEU B CD2 1 
ATOM   5697 N  N   . ASP B 1 250 ? -50.726 -19.041 12.849  1.00 22.19 ? 250 ASP B N   1 
ATOM   5698 C  CA  . ASP B 1 250 ? -51.071 -17.961 13.810  1.00 25.66 ? 250 ASP B CA  1 
ATOM   5699 C  C   . ASP B 1 250 ? -49.889 -17.002 13.973  1.00 24.84 ? 250 ASP B C   1 
ATOM   5700 O  O   . ASP B 1 250 ? -48.739 -17.465 13.951  1.00 23.77 ? 250 ASP B O   1 
ATOM   5701 C  CB  . ASP B 1 250 ? -51.323 -18.491 15.231  1.00 29.84 ? 250 ASP B CB  1 
ATOM   5702 C  CG  . ASP B 1 250 ? -52.274 -19.657 15.248  1.00 37.04 ? 250 ASP B CG  1 
ATOM   5703 O  OD1 . ASP B 1 250 ? -53.454 -19.443 14.878  1.00 41.48 ? 250 ASP B OD1 1 
ATOM   5704 O  OD2 . ASP B 1 250 ? -51.816 -20.781 15.562  1.00 49.89 ? 250 ASP B OD2 1 
ATOM   5705 N  N   . ASP B 1 251 ? -50.166 -15.752 14.328  1.00 24.90 ? 251 ASP B N   1 
ATOM   5706 C  CA  . ASP B 1 251 ? -49.125 -14.752 14.669  1.00 24.95 ? 251 ASP B CA  1 
ATOM   5707 C  C   . ASP B 1 251 ? -48.273 -15.252 15.841  1.00 23.67 ? 251 ASP B C   1 
ATOM   5708 O  O   . ASP B 1 251 ? -47.081 -14.923 15.883  1.00 25.92 ? 251 ASP B O   1 
ATOM   5709 C  CB  . ASP B 1 251 ? -49.749 -13.389 14.969  1.00 25.63 ? 251 ASP B CB  1 
ATOM   5710 C  CG  . ASP B 1 251 ? -50.266 -12.667 13.736  1.00 27.28 ? 251 ASP B CG  1 
ATOM   5711 O  OD1 . ASP B 1 251 ? -49.912 -13.086 12.578  1.00 28.54 ? 251 ASP B OD1 1 
ATOM   5712 O  OD2 . ASP B 1 251 ? -51.011 -11.683 13.933  1.00 26.98 ? 251 ASP B OD2 1 
ATOM   5713 N  N   . GLU B 1 252 ? -48.838 -16.005 16.778  1.00 21.78 ? 252 GLU B N   1 
ATOM   5714 C  CA  . GLU B 1 252 ? -48.053 -16.562 17.912  1.00 20.07 ? 252 GLU B CA  1 
ATOM   5715 C  C   . GLU B 1 252 ? -46.975 -17.531 17.409  1.00 18.10 ? 252 GLU B C   1 
ATOM   5716 O  O   . GLU B 1 252 ? -45.837 -17.419 17.817  1.00 18.40 ? 252 GLU B O   1 
ATOM   5717 C  CB  . GLU B 1 252 ? -48.943 -17.259 18.925  1.00 19.05 ? 252 GLU B CB  1 
ATOM   5718 C  CG  . GLU B 1 252 ? -48.174 -17.592 20.183  1.00 20.98 ? 252 GLU B CG  1 
ATOM   5719 C  CD  . GLU B 1 252 ? -48.996 -18.287 21.245  1.00 21.48 ? 252 GLU B CD  1 
ATOM   5720 O  OE1 . GLU B 1 252 ? -50.205 -18.243 21.136  1.00 22.35 ? 252 GLU B OE1 1 
ATOM   5721 O  OE2 . GLU B 1 252 ? -48.414 -18.881 22.156  1.00 23.23 ? 252 GLU B OE2 1 
ATOM   5722 N  N   . ASN B 1 253 ? -47.328 -18.479 16.567  1.00 18.15 ? 253 ASN B N   1 
ATOM   5723 C  CA  . ASN B 1 253 ? -46.366 -19.435 15.966  1.00 17.91 ? 253 ASN B CA  1 
ATOM   5724 C  C   . ASN B 1 253 ? -45.324 -18.668 15.148  1.00 17.50 ? 253 ASN B C   1 
ATOM   5725 O  O   . ASN B 1 253 ? -44.145 -18.999 15.252  1.00 17.48 ? 253 ASN B O   1 
ATOM   5726 C  CB  . ASN B 1 253 ? -47.066 -20.474 15.090  1.00 18.33 ? 253 ASN B CB  1 
ATOM   5727 C  CG  . ASN B 1 253 ? -46.086 -21.514 14.601  1.00 20.14 ? 253 ASN B CG  1 
ATOM   5728 O  OD1 . ASN B 1 253 ? -45.650 -21.468 13.436  1.00 21.34 ? 253 ASN B OD1 1 
ATOM   5729 N  ND2 . ASN B 1 253 ? -45.661 -22.377 15.514  1.00 18.62 ? 253 ASN B ND2 1 
ATOM   5730 N  N   . ILE B 1 254 ? -45.747 -17.682 14.360  1.00 16.97 ? 254 ILE B N   1 
ATOM   5731 C  CA  . ILE B 1 254 ? -44.842 -16.901 13.479  1.00 17.78 ? 254 ILE B CA  1 
ATOM   5732 C  C   . ILE B 1 254 ? -43.768 -16.291 14.372  1.00 18.26 ? 254 ILE B C   1 
ATOM   5733 O  O   . ILE B 1 254 ? -42.571 -16.361 14.015  1.00 18.38 ? 254 ILE B O   1 
ATOM   5734 C  CB  . ILE B 1 254 ? -45.621 -15.834 12.679  1.00 18.62 ? 254 ILE B CB  1 
ATOM   5735 C  CG1 . ILE B 1 254 ? -46.595 -16.477 11.692  1.00 19.35 ? 254 ILE B CG1 1 
ATOM   5736 C  CG2 . ILE B 1 254 ? -44.659 -14.875 12.003  1.00 18.57 ? 254 ILE B CG2 1 
ATOM   5737 C  CD1 . ILE B 1 254 ? -47.313 -15.504 10.785  1.00 20.46 ? 254 ILE B CD1 1 
ATOM   5738 N  N   . ARG B 1 255 ? -44.180 -15.731 15.508  1.00 18.10 ? 255 ARG B N   1 
ATOM   5739 C  CA  . ARG B 1 255 ? -43.220 -15.105 16.437  1.00 18.76 ? 255 ARG B CA  1 
ATOM   5740 C  C   . ARG B 1 255 ? -42.238 -16.191 16.890  1.00 18.53 ? 255 ARG B C   1 
ATOM   5741 O  O   . ARG B 1 255 ? -41.008 -15.903 16.916  1.00 17.42 ? 255 ARG B O   1 
ATOM   5742 C  CB  . ARG B 1 255 ? -43.939 -14.400 17.584  1.00 19.92 ? 255 ARG B CB  1 
ATOM   5743 C  CG  . ARG B 1 255 ? -43.123 -14.352 18.870  1.00 22.10 ? 255 ARG B CG  1 
ATOM   5744 C  CD  . ARG B 1 255 ? -43.977 -13.725 19.921  1.00 24.97 ? 255 ARG B CD  1 
ATOM   5745 N  NE  . ARG B 1 255 ? -44.267 -14.677 20.964  1.00 30.92 ? 255 ARG B NE  1 
ATOM   5746 C  CZ  . ARG B 1 255 ? -45.270 -14.589 21.829  1.00 32.00 ? 255 ARG B CZ  1 
ATOM   5747 N  NH1 . ARG B 1 255 ? -45.389 -15.526 22.752  1.00 34.37 ? 255 ARG B NH1 1 
ATOM   5748 N  NH2 . ARG B 1 255 ? -46.148 -13.598 21.763  1.00 31.50 ? 255 ARG B NH2 1 
ATOM   5749 N  N   . TYR B 1 256 ? -42.729 -17.383 17.240  1.00 17.07 ? 256 TYR B N   1 
ATOM   5750 C  CA  . TYR B 1 256 ? -41.854 -18.511 17.655  1.00 17.91 ? 256 TYR B CA  1 
ATOM   5751 C  C   . TYR B 1 256 ? -40.849 -18.824 16.535  1.00 18.53 ? 256 TYR B C   1 
ATOM   5752 O  O   . TYR B 1 256 ? -39.645 -18.905 16.825  1.00 19.15 ? 256 TYR B O   1 
ATOM   5753 C  CB  . TYR B 1 256 ? -42.685 -19.734 18.035  1.00 18.44 ? 256 TYR B CB  1 
ATOM   5754 C  CG  . TYR B 1 256 ? -43.536 -19.542 19.268  1.00 19.55 ? 256 TYR B CG  1 
ATOM   5755 C  CD1 . TYR B 1 256 ? -43.129 -18.728 20.314  1.00 18.17 ? 256 TYR B CD1 1 
ATOM   5756 C  CD2 . TYR B 1 256 ? -44.748 -20.194 19.393  1.00 19.71 ? 256 TYR B CD2 1 
ATOM   5757 C  CE1 . TYR B 1 256 ? -43.906 -18.572 21.443  1.00 19.36 ? 256 TYR B CE1 1 
ATOM   5758 C  CE2 . TYR B 1 256 ? -45.525 -20.067 20.532  1.00 20.02 ? 256 TYR B CE2 1 
ATOM   5759 C  CZ  . TYR B 1 256 ? -45.111 -19.243 21.559  1.00 20.04 ? 256 TYR B CZ  1 
ATOM   5760 O  OH  . TYR B 1 256 ? -45.890 -19.104 22.682  1.00 20.99 ? 256 TYR B OH  1 
ATOM   5761 N  N   . GLN B 1 257 ? -41.309 -18.956 15.286  1.00 17.88 ? 257 GLN B N   1 
ATOM   5762 C  CA  . GLN B 1 257 ? -40.424 -19.284 14.133  1.00 18.39 ? 257 GLN B CA  1 
ATOM   5763 C  C   . GLN B 1 257 ? -39.374 -18.173 13.989  1.00 17.85 ? 257 GLN B C   1 
ATOM   5764 O  O   . GLN B 1 257 ? -38.229 -18.478 13.696  1.00 18.12 ? 257 GLN B O   1 
ATOM   5765 C  CB  . GLN B 1 257 ? -41.202 -19.441 12.815  1.00 18.10 ? 257 GLN B CB  1 
ATOM   5766 C  CG  . GLN B 1 257 ? -42.384 -20.404 12.824  1.00 17.43 ? 257 GLN B CG  1 
ATOM   5767 C  CD  . GLN B 1 257 ? -42.058 -21.805 13.282  1.00 17.94 ? 257 GLN B CD  1 
ATOM   5768 O  OE1 . GLN B 1 257 ? -40.932 -22.114 13.652  1.00 17.30 ? 257 GLN B OE1 1 
ATOM   5769 N  NE2 . GLN B 1 257 ? -43.062 -22.672 13.274  1.00 18.30 ? 257 GLN B NE2 1 
ATOM   5770 N  N   . ILE B 1 258 ? -39.737 -16.914 14.214  1.00 17.72 ? 258 ILE B N   1 
ATOM   5771 C  CA  . ILE B 1 258 ? -38.757 -15.810 14.025  1.00 17.93 ? 258 ILE B CA  1 
ATOM   5772 C  C   . ILE B 1 258 ? -37.704 -15.915 15.130  1.00 18.65 ? 258 ILE B C   1 
ATOM   5773 O  O   . ILE B 1 258 ? -36.502 -15.821 14.807  1.00 19.29 ? 258 ILE B O   1 
ATOM   5774 C  CB  . ILE B 1 258 ? -39.468 -14.448 13.921  1.00 17.99 ? 258 ILE B CB  1 
ATOM   5775 C  CG1 . ILE B 1 258 ? -40.070 -14.312 12.520  1.00 19.48 ? 258 ILE B CG1 1 
ATOM   5776 C  CG2 . ILE B 1 258 ? -38.542 -13.284 14.246  1.00 17.87 ? 258 ILE B CG2 1 
ATOM   5777 C  CD1 . ILE B 1 258 ? -40.486 -12.914 12.164  1.00 21.67 ? 258 ILE B CD1 1 
ATOM   5778 N  N   . ILE B 1 259 ? -38.117 -16.159 16.370  1.00 17.56 ? 259 ILE B N   1 
ATOM   5779 C  CA  . ILE B 1 259 ? -37.162 -16.316 17.492  1.00 18.09 ? 259 ILE B CA  1 
ATOM   5780 C  C   . ILE B 1 259 ? -36.232 -17.478 17.147  1.00 17.62 ? 259 ILE B C   1 
ATOM   5781 O  O   . ILE B 1 259 ? -35.028 -17.345 17.342  1.00 18.04 ? 259 ILE B O   1 
ATOM   5782 C  CB  . ILE B 1 259 ? -37.918 -16.492 18.814  1.00 19.65 ? 259 ILE B CB  1 
ATOM   5783 C  CG1 . ILE B 1 259 ? -38.632 -15.187 19.201  1.00 20.01 ? 259 ILE B CG1 1 
ATOM   5784 C  CG2 . ILE B 1 259 ? -36.979 -16.987 19.913  1.00 19.85 ? 259 ILE B CG2 1 
ATOM   5785 C  CD1 . ILE B 1 259 ? -39.531 -15.305 20.437  1.00 19.64 ? 259 ILE B CD1 1 
ATOM   5786 N  N   . THR B 1 260 ? -36.778 -18.550 16.586  1.00 17.59 ? 260 THR B N   1 
ATOM   5787 C  CA  . THR B 1 260 ? -36.034 -19.779 16.242  1.00 17.80 ? 260 THR B CA  1 
ATOM   5788 C  C   . THR B 1 260 ? -34.967 -19.449 15.191  1.00 17.82 ? 260 THR B C   1 
ATOM   5789 O  O   . THR B 1 260 ? -33.839 -19.991 15.307  1.00 15.38 ? 260 THR B O   1 
ATOM   5790 C  CB  . THR B 1 260 ? -36.983 -20.904 15.796  1.00 17.94 ? 260 THR B CB  1 
ATOM   5791 O  OG1 . THR B 1 260 ? -37.890 -21.148 16.865  1.00 17.68 ? 260 THR B OG1 1 
ATOM   5792 C  CG2 . THR B 1 260 ? -36.264 -22.195 15.451  1.00 17.33 ? 260 THR B CG2 1 
ATOM   5793 N  N   . PHE B 1 261 ? -35.310 -18.650 14.176  1.00 17.73 ? 261 PHE B N   1 
ATOM   5794 C  CA  . PHE B 1 261 ? -34.372 -18.314 13.067  1.00 18.09 ? 261 PHE B CA  1 
ATOM   5795 C  C   . PHE B 1 261 ? -33.227 -17.433 13.577  1.00 17.93 ? 261 PHE B C   1 
ATOM   5796 O  O   . PHE B 1 261 ? -32.078 -17.581 13.060  1.00 17.93 ? 261 PHE B O   1 
ATOM   5797 C  CB  . PHE B 1 261 ? -35.106 -17.652 11.902  1.00 18.49 ? 261 PHE B CB  1 
ATOM   5798 C  CG  . PHE B 1 261 ? -36.063 -18.576 11.198  1.00 18.74 ? 261 PHE B CG  1 
ATOM   5799 C  CD1 . PHE B 1 261 ? -35.713 -19.896 10.945  1.00 19.18 ? 261 PHE B CD1 1 
ATOM   5800 C  CD2 . PHE B 1 261 ? -37.306 -18.120 10.773  1.00 19.44 ? 261 PHE B CD2 1 
ATOM   5801 C  CE1 . PHE B 1 261 ? -36.593 -20.744 10.287  1.00 19.79 ? 261 PHE B CE1 1 
ATOM   5802 C  CE2 . PHE B 1 261 ? -38.179 -18.972 10.112  1.00 19.10 ? 261 PHE B CE2 1 
ATOM   5803 C  CZ  . PHE B 1 261 ? -37.828 -20.285 9.886   1.00 19.42 ? 261 PHE B CZ  1 
ATOM   5804 N  N   . LEU B 1 262 ? -33.511 -16.572 14.558  1.00 17.11 ? 262 LEU B N   1 
ATOM   5805 C  CA  . LEU B 1 262 ? -32.508 -15.648 15.133  1.00 17.51 ? 262 LEU B CA  1 
ATOM   5806 C  C   . LEU B 1 262 ? -31.521 -16.439 15.991  1.00 17.98 ? 262 LEU B C   1 
ATOM   5807 O  O   . LEU B 1 262 ? -30.329 -16.161 15.881  1.00 17.75 ? 262 LEU B O   1 
ATOM   5808 C  CB  . LEU B 1 262 ? -33.226 -14.571 15.941  1.00 18.29 ? 262 LEU B CB  1 
ATOM   5809 C  CG  . LEU B 1 262 ? -33.965 -13.523 15.108  1.00 18.77 ? 262 LEU B CG  1 
ATOM   5810 C  CD1 . LEU B 1 262 ? -34.767 -12.574 15.997  1.00 18.89 ? 262 LEU B CD1 1 
ATOM   5811 C  CD2 . LEU B 1 262 ? -32.981 -12.759 14.252  1.00 19.09 ? 262 LEU B CD2 1 
ATOM   5812 N  N   . ILE B 1 263 ? -32.005 -17.390 16.799  1.00 18.23 ? 263 ILE B N   1 
ATOM   5813 C  CA  . ILE B 1 263 ? -31.164 -18.418 17.481  1.00 19.24 ? 263 ILE B CA  1 
ATOM   5814 C  C   . ILE B 1 263 ? -30.237 -19.092 16.449  1.00 19.70 ? 263 ILE B C   1 
ATOM   5815 O  O   . ILE B 1 263 ? -29.013 -19.080 16.637  1.00 19.89 ? 263 ILE B O   1 
ATOM   5816 C  CB  . ILE B 1 263 ? -32.036 -19.447 18.223  1.00 19.40 ? 263 ILE B CB  1 
ATOM   5817 C  CG1 . ILE B 1 263 ? -32.738 -18.798 19.416  1.00 19.13 ? 263 ILE B CG1 1 
ATOM   5818 C  CG2 . ILE B 1 263 ? -31.207 -20.663 18.630  1.00 19.23 ? 263 ILE B CG2 1 
ATOM   5819 C  CD1 . ILE B 1 263 ? -33.959 -19.544 19.839  1.00 19.96 ? 263 ILE B CD1 1 
ATOM   5820 N  N   . ALA B 1 264 ? -30.782 -19.653 15.385  1.00 20.13 ? 264 ALA B N   1 
ATOM   5821 C  CA  . ALA B 1 264 ? -29.969 -20.381 14.395  1.00 23.05 ? 264 ALA B CA  1 
ATOM   5822 C  C   . ALA B 1 264 ? -28.943 -19.403 13.802  1.00 24.24 ? 264 ALA B C   1 
ATOM   5823 O  O   . ALA B 1 264 ? -27.777 -19.772 13.748  1.00 26.31 ? 264 ALA B O   1 
ATOM   5824 C  CB  . ALA B 1 264 ? -30.840 -21.076 13.356  1.00 22.32 ? 264 ALA B CB  1 
ATOM   5825 N  N   . GLY B 1 265 ? -29.339 -18.176 13.436  1.00 28.21 ? 265 GLY B N   1 
ATOM   5826 C  CA  . GLY B 1 265 ? -28.454 -17.201 12.754  1.00 27.15 ? 265 GLY B CA  1 
ATOM   5827 C  C   . GLY B 1 265 ? -27.253 -16.823 13.613  1.00 28.04 ? 265 GLY B C   1 
ATOM   5828 O  O   . GLY B 1 265 ? -26.098 -16.827 13.125  1.00 31.60 ? 265 GLY B O   1 
ATOM   5829 N  N   . HIS B 1 266 ? -27.515 -16.550 14.877  1.00 24.54 ? 266 HIS B N   1 
ATOM   5830 C  CA  . HIS B 1 266 ? -26.500 -16.190 15.883  1.00 23.36 ? 266 HIS B CA  1 
ATOM   5831 C  C   . HIS B 1 266 ? -25.554 -17.360 16.172  1.00 23.14 ? 266 HIS B C   1 
ATOM   5832 O  O   . HIS B 1 266 ? -24.331 -17.102 16.218  1.00 26.47 ? 266 HIS B O   1 
ATOM   5833 C  CB  . HIS B 1 266 ? -27.218 -15.694 17.130  1.00 22.95 ? 266 HIS B CB  1 
ATOM   5834 C  CG  . HIS B 1 266 ? -26.330 -14.949 18.053  1.00 23.57 ? 266 HIS B CG  1 
ATOM   5835 N  ND1 . HIS B 1 266 ? -25.579 -15.595 19.021  1.00 23.85 ? 266 HIS B ND1 1 
ATOM   5836 C  CD2 . HIS B 1 266 ? -26.096 -13.627 18.187  1.00 22.73 ? 266 HIS B CD2 1 
ATOM   5837 C  CE1 . HIS B 1 266 ? -24.917 -14.699 19.718  1.00 23.15 ? 266 HIS B CE1 1 
ATOM   5838 N  NE2 . HIS B 1 266 ? -25.210 -13.488 19.220  1.00 25.06 ? 266 HIS B NE2 1 
ATOM   5839 N  N   . GLU B 1 267 ? -26.055 -18.583 16.370  1.00 20.85 ? 267 GLU B N   1 
ATOM   5840 C  CA  . GLU B 1 267 ? -25.307 -19.642 17.110  1.00 19.86 ? 267 GLU B CA  1 
ATOM   5841 C  C   . GLU B 1 267 ? -24.560 -20.610 16.188  1.00 19.17 ? 267 GLU B C   1 
ATOM   5842 O  O   . GLU B 1 267 ? -23.467 -21.069 16.581  1.00 19.17 ? 267 GLU B O   1 
ATOM   5843 C  CB  . GLU B 1 267 ? -26.259 -20.469 17.961  1.00 20.81 ? 267 GLU B CB  1 
ATOM   5844 C  CG  . GLU B 1 267 ? -26.862 -19.685 19.099  1.00 23.20 ? 267 GLU B CG  1 
ATOM   5845 C  CD  . GLU B 1 267 ? -25.812 -19.222 20.085  1.00 24.77 ? 267 GLU B CD  1 
ATOM   5846 O  OE1 . GLU B 1 267 ? -25.573 -19.956 21.067  1.00 27.22 ? 267 GLU B OE1 1 
ATOM   5847 O  OE2 . GLU B 1 267 ? -25.223 -18.158 19.846  1.00 26.21 ? 267 GLU B OE2 1 
ATOM   5848 N  N   . THR B 1 268 ? -25.130 -20.984 15.045  1.00 18.17 ? 268 THR B N   1 
ATOM   5849 C  CA  . THR B 1 268 ? -24.642 -22.142 14.257  1.00 17.66 ? 268 THR B CA  1 
ATOM   5850 C  C   . THR B 1 268 ? -23.679 -21.679 13.152  1.00 16.85 ? 268 THR B C   1 
ATOM   5851 O  O   . THR B 1 268 ? -22.505 -22.067 13.235  1.00 17.77 ? 268 THR B O   1 
ATOM   5852 C  CB  . THR B 1 268 ? -25.816 -22.991 13.759  1.00 19.79 ? 268 THR B CB  1 
ATOM   5853 O  OG1 . THR B 1 268 ? -26.668 -22.194 12.933  1.00 20.60 ? 268 THR B OG1 1 
ATOM   5854 C  CG2 . THR B 1 268 ? -26.653 -23.540 14.889  1.00 21.38 ? 268 THR B CG2 1 
ATOM   5855 N  N   . THR B 1 269 ? -24.122 -20.922 12.147  1.00 15.19 ? 269 THR B N   1 
ATOM   5856 C  CA  . THR B 1 269 ? -23.332 -20.732 10.901  1.00 16.04 ? 269 THR B CA  1 
ATOM   5857 C  C   . THR B 1 269 ? -22.059 -19.953 11.217  1.00 16.13 ? 269 THR B C   1 
ATOM   5858 O  O   . THR B 1 269 ? -21.038 -20.227 10.558  1.00 14.85 ? 269 THR B O   1 
ATOM   5859 C  CB  . THR B 1 269 ? -24.117 -20.053 9.777   1.00 16.60 ? 269 THR B CB  1 
ATOM   5860 O  OG1 . THR B 1 269 ? -25.338 -20.778 9.704   1.00 17.80 ? 269 THR B OG1 1 
ATOM   5861 C  CG2 . THR B 1 269 ? -23.394 -20.097 8.449   1.00 17.38 ? 269 THR B CG2 1 
ATOM   5862 N  N   . SER B 1 270 ? -22.137 -19.055 12.206  1.00 15.76 ? 270 SER B N   1 
ATOM   5863 C  CA  . SER B 1 270 ? -20.995 -18.347 12.821  1.00 15.70 ? 270 SER B CA  1 
ATOM   5864 C  C   . SER B 1 270 ? -19.985 -19.369 13.347  1.00 17.44 ? 270 SER B C   1 
ATOM   5865 O  O   . SER B 1 270 ? -18.786 -19.169 13.130  1.00 19.60 ? 270 SER B O   1 
ATOM   5866 C  CB  . SER B 1 270 ? -21.493 -17.397 13.899  1.00 16.14 ? 270 SER B CB  1 
ATOM   5867 O  OG  . SER B 1 270 ? -22.313 -18.066 14.867  1.00 15.37 ? 270 SER B OG  1 
ATOM   5868 N  N   . GLY B 1 271 ? -20.461 -20.431 14.008  1.00 19.15 ? 271 GLY B N   1 
ATOM   5869 C  CA  . GLY B 1 271 ? -19.645 -21.520 14.579  1.00 18.43 ? 271 GLY B CA  1 
ATOM   5870 C  C   . GLY B 1 271 ? -18.892 -22.255 13.481  1.00 18.84 ? 271 GLY B C   1 
ATOM   5871 O  O   . GLY B 1 271 ? -17.661 -22.416 13.607  1.00 18.69 ? 271 GLY B O   1 
ATOM   5872 N  N   . LEU B 1 272 ? -19.584 -22.668 12.421  1.00 17.90 ? 272 LEU B N   1 
ATOM   5873 C  CA  . LEU B 1 272 ? -18.949 -23.345 11.258  1.00 18.23 ? 272 LEU B CA  1 
ATOM   5874 C  C   . LEU B 1 272 ? -17.842 -22.457 10.666  1.00 17.90 ? 272 LEU B C   1 
ATOM   5875 O  O   . LEU B 1 272 ? -16.712 -22.956 10.442  1.00 18.10 ? 272 LEU B O   1 
ATOM   5876 C  CB  . LEU B 1 272 ? -20.026 -23.618 10.208  1.00 19.25 ? 272 LEU B CB  1 
ATOM   5877 C  CG  . LEU B 1 272 ? -19.522 -24.167 8.875   1.00 20.16 ? 272 LEU B CG  1 
ATOM   5878 C  CD1 . LEU B 1 272 ? -18.597 -25.346 9.099   1.00 19.91 ? 272 LEU B CD1 1 
ATOM   5879 C  CD2 . LEU B 1 272 ? -20.704 -24.562 7.991   1.00 20.59 ? 272 LEU B CD2 1 
ATOM   5880 N  N   . LEU B 1 273 ? -18.154 -21.193 10.367  1.00 17.33 ? 273 LEU B N   1 
ATOM   5881 C  CA  . LEU B 1 273 ? -17.193 -20.276 9.695   1.00 17.18 ? 273 LEU B CA  1 
ATOM   5882 C  C   . LEU B 1 273 ? -15.925 -20.110 10.552  1.00 16.78 ? 273 LEU B C   1 
ATOM   5883 O  O   . LEU B 1 273 ? -14.838 -20.151 9.961   1.00 16.06 ? 273 LEU B O   1 
ATOM   5884 C  CB  . LEU B 1 273 ? -17.854 -18.926 9.399   1.00 16.65 ? 273 LEU B CB  1 
ATOM   5885 C  CG  . LEU B 1 273 ? -18.646 -18.934 8.093   1.00 16.15 ? 273 LEU B CG  1 
ATOM   5886 C  CD1 . LEU B 1 273 ? -19.688 -17.830 8.073   1.00 15.17 ? 273 LEU B CD1 1 
ATOM   5887 C  CD2 . LEU B 1 273 ? -17.703 -18.847 6.895   1.00 16.30 ? 273 LEU B CD2 1 
ATOM   5888 N  N   . SER B 1 274 ? -16.087 -19.903 11.868  1.00 15.93 ? 274 SER B N   1 
ATOM   5889 C  CA  . SER B 1 274 ? -15.016 -19.754 12.885  1.00 15.65 ? 274 SER B CA  1 
ATOM   5890 C  C   . SER B 1 274 ? -14.106 -20.975 12.877  1.00 16.39 ? 274 SER B C   1 
ATOM   5891 O  O   . SER B 1 274 ? -12.875 -20.786 12.818  1.00 16.71 ? 274 SER B O   1 
ATOM   5892 C  CB  . SER B 1 274 ? -15.614 -19.538 14.229  1.00 14.93 ? 274 SER B CB  1 
ATOM   5893 O  OG  . SER B 1 274 ? -16.336 -18.322 14.225  1.00 13.92 ? 274 SER B OG  1 
ATOM   5894 N  N   . PHE B 1 275 ? -14.702 -22.174 12.885  1.00 17.08 ? 275 PHE B N   1 
ATOM   5895 C  CA  . PHE B 1 275 ? -13.951 -23.450 12.917  1.00 17.22 ? 275 PHE B CA  1 
ATOM   5896 C  C   . PHE B 1 275 ? -13.300 -23.698 11.556  1.00 18.50 ? 275 PHE B C   1 
ATOM   5897 O  O   . PHE B 1 275 ? -12.164 -24.231 11.531  1.00 21.03 ? 275 PHE B O   1 
ATOM   5898 C  CB  . PHE B 1 275 ? -14.815 -24.630 13.352  1.00 16.32 ? 275 PHE B CB  1 
ATOM   5899 C  CG  . PHE B 1 275 ? -15.006 -24.760 14.845  1.00 16.00 ? 275 PHE B CG  1 
ATOM   5900 C  CD1 . PHE B 1 275 ? -13.933 -25.013 15.674  1.00 16.47 ? 275 PHE B CD1 1 
ATOM   5901 C  CD2 . PHE B 1 275 ? -16.269 -24.678 15.407  1.00 15.29 ? 275 PHE B CD2 1 
ATOM   5902 C  CE1 . PHE B 1 275 ? -14.111 -25.164 17.038  1.00 16.90 ? 275 PHE B CE1 1 
ATOM   5903 C  CE2 . PHE B 1 275 ? -16.444 -24.787 16.768  1.00 16.23 ? 275 PHE B CE2 1 
ATOM   5904 C  CZ  . PHE B 1 275 ? -15.364 -25.040 17.582  1.00 17.44 ? 275 PHE B CZ  1 
ATOM   5905 N  N   . ALA B 1 276 ? -13.959 -23.331 10.462  1.00 19.44 ? 276 ALA B N   1 
ATOM   5906 C  CA  . ALA B 1 276 ? -13.393 -23.516 9.099   1.00 20.33 ? 276 ALA B CA  1 
ATOM   5907 C  C   . ALA B 1 276 ? -12.130 -22.652 8.954   1.00 19.47 ? 276 ALA B C   1 
ATOM   5908 O  O   . ALA B 1 276 ? -11.109 -23.181 8.459   1.00 19.85 ? 276 ALA B O   1 
ATOM   5909 C  CB  . ALA B 1 276 ? -14.417 -23.231 8.031   1.00 20.38 ? 276 ALA B CB  1 
ATOM   5910 N  N   . LEU B 1 277 ? -12.150 -21.419 9.457   1.00 19.59 ? 277 LEU B N   1 
ATOM   5911 C  CA  . LEU B 1 277 ? -10.954 -20.537 9.415   1.00 20.71 ? 277 LEU B CA  1 
ATOM   5912 C  C   . LEU B 1 277 ? -9.855  -21.084 10.336  1.00 19.55 ? 277 LEU B C   1 
ATOM   5913 O  O   . LEU B 1 277 ? -8.686  -21.100 9.898   1.00 18.33 ? 277 LEU B O   1 
ATOM   5914 C  CB  . LEU B 1 277 ? -11.320 -19.102 9.778   1.00 23.87 ? 277 LEU B CB  1 
ATOM   5915 C  CG  . LEU B 1 277 ? -10.296 -18.078 9.276   1.00 27.56 ? 277 LEU B CG  1 
ATOM   5916 C  CD1 . LEU B 1 277 ? -10.122 -18.185 7.768   1.00 26.88 ? 277 LEU B CD1 1 
ATOM   5917 C  CD2 . LEU B 1 277 ? -10.681 -16.659 9.681   1.00 29.07 ? 277 LEU B CD2 1 
ATOM   5918 N  N   . TYR B 1 278 ? -10.206 -21.574 11.535  1.00 19.14 ? 278 TYR B N   1 
ATOM   5919 C  CA  . TYR B 1 278 ? -9.258  -22.271 12.440  1.00 18.67 ? 278 TYR B CA  1 
ATOM   5920 C  C   . TYR B 1 278 ? -8.540  -23.373 11.642  1.00 20.73 ? 278 TYR B C   1 
ATOM   5921 O  O   . TYR B 1 278 ? -7.274  -23.365 11.603  1.00 20.81 ? 278 TYR B O   1 
ATOM   5922 C  CB  . TYR B 1 278 ? -9.952  -22.820 13.687  1.00 19.08 ? 278 TYR B CB  1 
ATOM   5923 C  CG  . TYR B 1 278 ? -9.088  -23.763 14.485  1.00 17.85 ? 278 TYR B CG  1 
ATOM   5924 C  CD1 . TYR B 1 278 ? -8.138  -23.258 15.348  1.00 18.66 ? 278 TYR B CD1 1 
ATOM   5925 C  CD2 . TYR B 1 278 ? -9.152  -25.135 14.327  1.00 18.36 ? 278 TYR B CD2 1 
ATOM   5926 C  CE1 . TYR B 1 278 ? -7.279  -24.079 16.050  1.00 18.62 ? 278 TYR B CE1 1 
ATOM   5927 C  CE2 . TYR B 1 278 ? -8.309  -25.977 15.039  1.00 19.31 ? 278 TYR B CE2 1 
ATOM   5928 C  CZ  . TYR B 1 278 ? -7.359  -25.442 15.897  1.00 18.81 ? 278 TYR B CZ  1 
ATOM   5929 O  OH  . TYR B 1 278 ? -6.481  -26.198 16.615  1.00 19.57 ? 278 TYR B OH  1 
ATOM   5930 N  N   . PHE B 1 279 ? -9.281  -24.283 10.992  1.00 20.48 ? 279 PHE B N   1 
ATOM   5931 C  CA  . PHE B 1 279 ? -8.649  -25.467 10.346  1.00 20.77 ? 279 PHE B CA  1 
ATOM   5932 C  C   . PHE B 1 279 ? -7.781  -24.988 9.172   1.00 20.34 ? 279 PHE B C   1 
ATOM   5933 O  O   . PHE B 1 279 ? -6.665  -25.507 8.971   1.00 22.08 ? 279 PHE B O   1 
ATOM   5934 C  CB  . PHE B 1 279 ? -9.670  -26.560 10.000  1.00 20.27 ? 279 PHE B CB  1 
ATOM   5935 C  CG  . PHE B 1 279 ? -10.105 -27.372 11.201  1.00 19.22 ? 279 PHE B CG  1 
ATOM   5936 C  CD1 . PHE B 1 279 ? -9.185  -28.126 11.922  1.00 19.57 ? 279 PHE B CD1 1 
ATOM   5937 C  CD2 . PHE B 1 279 ? -11.426 -27.355 11.635  1.00 18.14 ? 279 PHE B CD2 1 
ATOM   5938 C  CE1 . PHE B 1 279 ? -9.586  -28.850 13.043  1.00 20.18 ? 279 PHE B CE1 1 
ATOM   5939 C  CE2 . PHE B 1 279 ? -11.815 -28.064 12.760  1.00 18.62 ? 279 PHE B CE2 1 
ATOM   5940 C  CZ  . PHE B 1 279 ? -10.901 -28.817 13.461  1.00 18.16 ? 279 PHE B CZ  1 
ATOM   5941 N  N   . LEU B 1 280 ? -8.240  -23.994 8.434   1.00 19.97 ? 280 LEU B N   1 
ATOM   5942 C  CA  . LEU B 1 280 ? -7.495  -23.494 7.250   1.00 20.32 ? 280 LEU B CA  1 
ATOM   5943 C  C   . LEU B 1 280 ? -6.148  -22.906 7.683   1.00 19.75 ? 280 LEU B C   1 
ATOM   5944 O  O   . LEU B 1 280 ? -5.153  -23.284 7.078   1.00 20.37 ? 280 LEU B O   1 
ATOM   5945 C  CB  . LEU B 1 280 ? -8.358  -22.460 6.529   1.00 20.81 ? 280 LEU B CB  1 
ATOM   5946 C  CG  . LEU B 1 280 ? -9.538  -23.037 5.744   1.00 21.94 ? 280 LEU B CG  1 
ATOM   5947 C  CD1 . LEU B 1 280 ? -10.446 -21.913 5.267   1.00 22.80 ? 280 LEU B CD1 1 
ATOM   5948 C  CD2 . LEU B 1 280 ? -9.073  -23.888 4.561   1.00 21.24 ? 280 LEU B CD2 1 
ATOM   5949 N  N   . VAL B 1 281 ? -6.100  -22.026 8.696   1.00 20.67 ? 281 VAL B N   1 
ATOM   5950 C  CA  . VAL B 1 281 ? -4.820  -21.393 9.147   1.00 20.04 ? 281 VAL B CA  1 
ATOM   5951 C  C   . VAL B 1 281 ? -3.898  -22.480 9.712   1.00 20.07 ? 281 VAL B C   1 
ATOM   5952 O  O   . VAL B 1 281 ? -2.701  -22.341 9.554   1.00 22.23 ? 281 VAL B O   1 
ATOM   5953 C  CB  . VAL B 1 281 ? -5.002  -20.222 10.132  1.00 19.77 ? 281 VAL B CB  1 
ATOM   5954 C  CG1 . VAL B 1 281 ? -5.711  -19.058 9.473   1.00 21.11 ? 281 VAL B CG1 1 
ATOM   5955 C  CG2 . VAL B 1 281 ? -5.682  -20.602 11.435  1.00 19.99 ? 281 VAL B CG2 1 
ATOM   5956 N  N   . LYS B 1 282 ? -4.456  -23.557 10.263  1.00 20.51 ? 282 LYS B N   1 
ATOM   5957 C  CA  . LYS B 1 282 ? -3.706  -24.695 10.853  1.00 20.15 ? 282 LYS B CA  1 
ATOM   5958 C  C   . LYS B 1 282 ? -3.289  -25.709 9.777   1.00 20.19 ? 282 LYS B C   1 
ATOM   5959 O  O   . LYS B 1 282 ? -2.476  -26.613 10.091  1.00 22.50 ? 282 LYS B O   1 
ATOM   5960 C  CB  . LYS B 1 282 ? -4.560  -25.356 11.940  1.00 19.16 ? 282 LYS B CB  1 
ATOM   5961 C  CG  . LYS B 1 282 ? -4.757  -24.487 13.174  1.00 18.91 ? 282 LYS B CG  1 
ATOM   5962 C  CD  . LYS B 1 282 ? -3.466  -24.067 13.879  1.00 18.78 ? 282 LYS B CD  1 
ATOM   5963 C  CE  . LYS B 1 282 ? -3.749  -23.507 15.261  1.00 19.31 ? 282 LYS B CE  1 
ATOM   5964 N  NZ  . LYS B 1 282 ? -2.578  -22.837 15.869  1.00 19.04 ? 282 LYS B NZ  1 
ATOM   5965 N  N   . ASN B 1 283 ? -3.801  -25.597 8.557   1.00 19.35 ? 283 ASN B N   1 
ATOM   5966 C  CA  . ASN B 1 283 ? -3.500  -26.577 7.479   1.00 19.05 ? 283 ASN B CA  1 
ATOM   5967 C  C   . ASN B 1 283 ? -3.226  -25.790 6.210   1.00 18.92 ? 283 ASN B C   1 
ATOM   5968 O  O   . ASN B 1 283 ? -4.086  -25.723 5.343   1.00 18.57 ? 283 ASN B O   1 
ATOM   5969 C  CB  . ASN B 1 283 ? -4.630  -27.590 7.357   1.00 17.83 ? 283 ASN B CB  1 
ATOM   5970 C  CG  . ASN B 1 283 ? -4.818  -28.334 8.661   1.00 18.49 ? 283 ASN B CG  1 
ATOM   5971 O  OD1 . ASN B 1 283 ? -4.237  -29.396 8.849   1.00 19.48 ? 283 ASN B OD1 1 
ATOM   5972 N  ND2 . ASN B 1 283 ? -5.596  -27.784 9.584   1.00 19.09 ? 283 ASN B ND2 1 
ATOM   5973 N  N   . PRO B 1 284 ? -2.056  -25.115 6.117   1.00 18.90 ? 284 PRO B N   1 
ATOM   5974 C  CA  . PRO B 1 284 ? -1.764  -24.216 5.009   1.00 20.90 ? 284 PRO B CA  1 
ATOM   5975 C  C   . PRO B 1 284 ? -1.922  -24.864 3.635   1.00 21.40 ? 284 PRO B C   1 
ATOM   5976 O  O   . PRO B 1 284 ? -2.334  -24.148 2.781   1.00 23.25 ? 284 PRO B O   1 
ATOM   5977 C  CB  . PRO B 1 284 ? -0.305  -23.783 5.212   1.00 19.72 ? 284 PRO B CB  1 
ATOM   5978 C  CG  . PRO B 1 284 ? -0.117  -23.903 6.720   1.00 19.77 ? 284 PRO B CG  1 
ATOM   5979 C  CD  . PRO B 1 284 ? -0.981  -25.082 7.119   1.00 19.36 ? 284 PRO B CD  1 
ATOM   5980 N  N   . HIS B 1 285 ? -1.574  -26.137 3.448   1.00 21.01 ? 285 HIS B N   1 
ATOM   5981 C  CA  . HIS B 1 285 ? -1.822  -26.816 2.152   1.00 22.50 ? 285 HIS B CA  1 
ATOM   5982 C  C   . HIS B 1 285 ? -3.316  -26.763 1.782   1.00 23.43 ? 285 HIS B C   1 
ATOM   5983 O  O   . HIS B 1 285 ? -3.614  -26.442 0.604   1.00 23.18 ? 285 HIS B O   1 
ATOM   5984 C  CB  . HIS B 1 285 ? -1.246  -28.223 2.159   1.00 24.13 ? 285 HIS B CB  1 
ATOM   5985 C  CG  . HIS B 1 285 ? 0.225   -28.210 1.935   1.00 25.80 ? 285 HIS B CG  1 
ATOM   5986 N  ND1 . HIS B 1 285 ? 0.837   -27.261 1.125   1.00 26.08 ? 285 HIS B ND1 1 
ATOM   5987 C  CD2 . HIS B 1 285 ? 1.206   -28.988 2.422   1.00 25.20 ? 285 HIS B CD2 1 
ATOM   5988 C  CE1 . HIS B 1 285 ? 2.127   -27.476 1.112   1.00 25.24 ? 285 HIS B CE1 1 
ATOM   5989 N  NE2 . HIS B 1 285 ? 2.373   -28.544 1.874   1.00 25.49 ? 285 HIS B NE2 1 
ATOM   5990 N  N   . VAL B 1 286 ? -4.229  -26.998 2.735   1.00 22.54 ? 286 VAL B N   1 
ATOM   5991 C  CA  . VAL B 1 286 ? -5.707  -26.990 2.480   1.00 20.66 ? 286 VAL B CA  1 
ATOM   5992 C  C   . VAL B 1 286 ? -6.158  -25.583 2.085   1.00 18.97 ? 286 VAL B C   1 
ATOM   5993 O  O   . VAL B 1 286 ? -6.963  -25.465 1.139   1.00 17.23 ? 286 VAL B O   1 
ATOM   5994 C  CB  . VAL B 1 286 ? -6.485  -27.545 3.685   1.00 21.10 ? 286 VAL B CB  1 
ATOM   5995 C  CG1 . VAL B 1 286 ? -8.001  -27.456 3.487   1.00 20.37 ? 286 VAL B CG1 1 
ATOM   5996 C  CG2 . VAL B 1 286 ? -6.043  -28.987 3.975   1.00 21.53 ? 286 VAL B CG2 1 
ATOM   5997 N  N   . LEU B 1 287 ? -5.626  -24.573 2.776   1.00 18.97 ? 287 LEU B N   1 
ATOM   5998 C  CA  . LEU B 1 287 ? -6.028  -23.154 2.650   1.00 19.92 ? 287 LEU B CA  1 
ATOM   5999 C  C   . LEU B 1 287 ? -5.615  -22.665 1.253   1.00 21.31 ? 287 LEU B C   1 
ATOM   6000 O  O   . LEU B 1 287 ? -6.482  -22.106 0.548   1.00 19.02 ? 287 LEU B O   1 
ATOM   6001 C  CB  . LEU B 1 287 ? -5.406  -22.376 3.816   1.00 20.50 ? 287 LEU B CB  1 
ATOM   6002 C  CG  . LEU B 1 287 ? -5.272  -20.865 3.665   1.00 21.63 ? 287 LEU B CG  1 
ATOM   6003 C  CD1 . LEU B 1 287 ? -6.546  -20.234 3.198   1.00 22.45 ? 287 LEU B CD1 1 
ATOM   6004 C  CD2 . LEU B 1 287 ? -4.863  -20.245 4.978   1.00 23.52 ? 287 LEU B CD2 1 
ATOM   6005 N  N   . GLN B 1 288 ? -4.381  -22.958 0.834   1.00 21.04 ? 288 GLN B N   1 
ATOM   6006 C  CA  . GLN B 1 288 ? -3.872  -22.708 -0.543  1.00 23.67 ? 288 GLN B CA  1 
ATOM   6007 C  C   . GLN B 1 288 ? -4.836  -23.268 -1.607  1.00 23.45 ? 288 GLN B C   1 
ATOM   6008 O  O   . GLN B 1 288 ? -5.118  -22.574 -2.580  1.00 23.05 ? 288 GLN B O   1 
ATOM   6009 C  CB  . GLN B 1 288 ? -2.490  -23.354 -0.687  1.00 25.30 ? 288 GLN B CB  1 
ATOM   6010 C  CG  . GLN B 1 288 ? -1.855  -23.196 -2.063  1.00 27.96 ? 288 GLN B CG  1 
ATOM   6011 C  CD  . GLN B 1 288 ? -1.758  -21.734 -2.407  1.00 31.05 ? 288 GLN B CD  1 
ATOM   6012 O  OE1 . GLN B 1 288 ? -1.747  -20.893 -1.515  1.00 39.07 ? 288 GLN B OE1 1 
ATOM   6013 N  NE2 . GLN B 1 288 ? -1.740  -21.414 -3.691  1.00 30.37 ? 288 GLN B NE2 1 
ATOM   6014 N  N   . LYS B 1 289 ? -5.261  -24.523 -1.471  1.00 25.19 ? 289 LYS B N   1 
ATOM   6015 C  CA  . LYS B 1 289 ? -6.106  -25.225 -2.476  1.00 25.47 ? 289 LYS B CA  1 
ATOM   6016 C  C   . LYS B 1 289 ? -7.451  -24.486 -2.589  1.00 24.77 ? 289 LYS B C   1 
ATOM   6017 O  O   . LYS B 1 289 ? -7.843  -24.159 -3.734  1.00 23.51 ? 289 LYS B O   1 
ATOM   6018 C  CB  . LYS B 1 289 ? -6.202  -26.704 -2.086  1.00 26.60 ? 289 LYS B CB  1 
ATOM   6019 C  CG  . LYS B 1 289 ? -6.797  -27.643 -3.128  1.00 29.71 ? 289 LYS B CG  1 
ATOM   6020 C  CD  . LYS B 1 289 ? -6.817  -29.100 -2.676  1.00 29.71 ? 289 LYS B CD  1 
ATOM   6021 C  CE  . LYS B 1 289 ? -7.590  -30.014 -3.609  1.00 30.06 ? 289 LYS B CE  1 
ATOM   6022 N  NZ  . LYS B 1 289 ? -7.329  -31.449 -3.313  1.00 29.40 ? 289 LYS B NZ  1 
ATOM   6023 N  N   . ALA B 1 290 ? -8.093  -24.185 -1.444  1.00 24.22 ? 290 ALA B N   1 
ATOM   6024 C  CA  . ALA B 1 290 ? -9.415  -23.519 -1.338  1.00 21.94 ? 290 ALA B CA  1 
ATOM   6025 C  C   . ALA B 1 290 ? -9.288  -22.086 -1.862  1.00 22.07 ? 290 ALA B C   1 
ATOM   6026 O  O   . ALA B 1 290 ? -10.175 -21.663 -2.592  1.00 24.76 ? 290 ALA B O   1 
ATOM   6027 C  CB  . ALA B 1 290 ? -9.927  -23.560 0.076   1.00 20.34 ? 290 ALA B CB  1 
ATOM   6028 N  N   . ALA B 1 291 ? -8.182  -21.411 -1.556  1.00 21.93 ? 291 ALA B N   1 
ATOM   6029 C  CA  . ALA B 1 291 ? -7.804  -20.072 -2.064  1.00 23.13 ? 291 ALA B CA  1 
ATOM   6030 C  C   . ALA B 1 291 ? -7.698  -20.089 -3.599  1.00 22.96 ? 291 ALA B C   1 
ATOM   6031 O  O   . ALA B 1 291 ? -8.237  -19.158 -4.237  1.00 22.90 ? 291 ALA B O   1 
ATOM   6032 C  CB  . ALA B 1 291 ? -6.513  -19.610 -1.412  1.00 22.35 ? 291 ALA B CB  1 
ATOM   6033 N  N   . GLU B 1 292 ? -7.060  -21.104 -4.184  1.00 24.42 ? 292 GLU B N   1 
ATOM   6034 C  CA  . GLU B 1 292 ? -6.966  -21.243 -5.665  1.00 26.98 ? 292 GLU B CA  1 
ATOM   6035 C  C   . GLU B 1 292 ? -8.382  -21.399 -6.254  1.00 24.59 ? 292 GLU B C   1 
ATOM   6036 O  O   . GLU B 1 292 ? -8.717  -20.653 -7.201  1.00 22.24 ? 292 GLU B O   1 
ATOM   6037 C  CB  . GLU B 1 292 ? -6.001  -22.365 -6.053  1.00 31.22 ? 292 GLU B CB  1 
ATOM   6038 C  CG  . GLU B 1 292 ? -4.603  -21.838 -6.352  1.00 38.56 ? 292 GLU B CG  1 
ATOM   6039 C  CD  . GLU B 1 292 ? -3.454  -22.794 -6.067  1.00 45.13 ? 292 GLU B CD  1 
ATOM   6040 O  OE1 . GLU B 1 292 ? -2.324  -22.295 -5.862  1.00 43.61 ? 292 GLU B OE1 1 
ATOM   6041 O  OE2 . GLU B 1 292 ? -3.685  -24.034 -6.057  1.00 47.81 ? 292 GLU B OE2 1 
ATOM   6042 N  N   . GLU B 1 293 ? -9.219  -22.265 -5.686  1.00 22.23 ? 293 GLU B N   1 
ATOM   6043 C  CA  . GLU B 1 293 ? -10.640 -22.371 -6.122  1.00 22.15 ? 293 GLU B CA  1 
ATOM   6044 C  C   . GLU B 1 293 ? -11.296 -20.987 -5.999  1.00 20.46 ? 293 GLU B C   1 
ATOM   6045 O  O   . GLU B 1 293 ? -11.859 -20.494 -7.017  1.00 18.15 ? 293 GLU B O   1 
ATOM   6046 C  CB  . GLU B 1 293 ? -11.399 -23.446 -5.338  1.00 22.04 ? 293 GLU B CB  1 
ATOM   6047 C  CG  . GLU B 1 293 ? -12.791 -23.750 -5.896  1.00 22.16 ? 293 GLU B CG  1 
ATOM   6048 C  CD  . GLU B 1 293 ? -13.552 -24.783 -5.084  1.00 21.78 ? 293 GLU B CD  1 
ATOM   6049 O  OE1 . GLU B 1 293 ? -13.969 -24.444 -3.951  1.00 21.45 ? 293 GLU B OE1 1 
ATOM   6050 O  OE2 . GLU B 1 293 ? -13.643 -25.953 -5.551  1.00 21.87 ? 293 GLU B OE2 1 
ATOM   6051 N  N   . ALA B 1 294 ? -11.196 -20.352 -4.833  1.00 18.83 ? 294 ALA B N   1 
ATOM   6052 C  CA  . ALA B 1 294 ? -11.819 -19.036 -4.609  1.00 20.88 ? 294 ALA B CA  1 
ATOM   6053 C  C   . ALA B 1 294 ? -11.481 -18.118 -5.794  1.00 21.75 ? 294 ALA B C   1 
ATOM   6054 O  O   . ALA B 1 294 ? -12.435 -17.596 -6.406  1.00 21.93 ? 294 ALA B O   1 
ATOM   6055 C  CB  . ALA B 1 294 ? -11.405 -18.457 -3.285  1.00 22.12 ? 294 ALA B CB  1 
ATOM   6056 N  N   . ALA B 1 295 ? -10.199 -18.000 -6.165  1.00 22.86 ? 295 ALA B N   1 
ATOM   6057 C  CA  . ALA B 1 295 ? -9.706  -17.104 -7.243  1.00 22.93 ? 295 ALA B CA  1 
ATOM   6058 C  C   . ALA B 1 295 ? -10.191 -17.539 -8.623  1.00 23.00 ? 295 ALA B C   1 
ATOM   6059 O  O   . ALA B 1 295 ? -10.583 -16.677 -9.403  1.00 25.08 ? 295 ALA B O   1 
ATOM   6060 C  CB  . ALA B 1 295 ? -8.206  -17.075 -7.242  1.00 24.35 ? 295 ALA B CB  1 
ATOM   6061 N  N   . ARG B 1 296 ? -10.090 -18.819 -8.944  1.00 22.92 ? 296 ARG B N   1 
ATOM   6062 C  CA  . ARG B 1 296 ? -10.574 -19.379 -10.231 1.00 25.76 ? 296 ARG B CA  1 
ATOM   6063 C  C   . ARG B 1 296 ? -12.048 -18.999 -10.468 1.00 25.75 ? 296 ARG B C   1 
ATOM   6064 O  O   . ARG B 1 296 ? -12.368 -18.542 -11.592 1.00 22.66 ? 296 ARG B O   1 
ATOM   6065 C  CB  . ARG B 1 296 ? -10.370 -20.898 -10.238 1.00 29.76 ? 296 ARG B CB  1 
ATOM   6066 C  CG  . ARG B 1 296 ? -10.771 -21.595 -11.534 1.00 34.82 ? 296 ARG B CG  1 
ATOM   6067 C  CD  . ARG B 1 296 ? -10.330 -23.057 -11.616 1.00 40.47 ? 296 ARG B CD  1 
ATOM   6068 N  NE  . ARG B 1 296 ? -10.625 -23.912 -10.454 1.00 45.71 ? 296 ARG B NE  1 
ATOM   6069 C  CZ  . ARG B 1 296 ? -9.823  -24.107 -9.384  1.00 50.94 ? 296 ARG B CZ  1 
ATOM   6070 N  NH1 . ARG B 1 296 ? -8.652  -23.485 -9.267  1.00 50.50 ? 296 ARG B NH1 1 
ATOM   6071 N  NH2 . ARG B 1 296 ? -10.213 -24.928 -8.417  1.00 47.05 ? 296 ARG B NH2 1 
ATOM   6072 N  N   . VAL B 1 297 ? -12.901 -19.170 -9.449  1.00 25.77 ? 297 VAL B N   1 
ATOM   6073 C  CA  . VAL B 1 297 ? -14.387 -19.221 -9.584  1.00 25.59 ? 297 VAL B CA  1 
ATOM   6074 C  C   . VAL B 1 297 ? -14.993 -17.818 -9.440  1.00 25.18 ? 297 VAL B C   1 
ATOM   6075 O  O   . VAL B 1 297 ? -15.896 -17.506 -10.238 1.00 25.29 ? 297 VAL B O   1 
ATOM   6076 C  CB  . VAL B 1 297 ? -15.014 -20.188 -8.562  1.00 25.55 ? 297 VAL B CB  1 
ATOM   6077 C  CG1 . VAL B 1 297 ? -16.521 -20.013 -8.469  1.00 25.72 ? 297 VAL B CG1 1 
ATOM   6078 C  CG2 . VAL B 1 297 ? -14.668 -21.623 -8.873  1.00 25.66 ? 297 VAL B CG2 1 
ATOM   6079 N  N   . LEU B 1 298 ? -14.590 -17.044 -8.428  1.00 24.81 ? 298 LEU B N   1 
ATOM   6080 C  CA  . LEU B 1 298 ? -15.245 -15.747 -8.074  1.00 25.61 ? 298 LEU B CA  1 
ATOM   6081 C  C   . LEU B 1 298 ? -14.590 -14.611 -8.880  1.00 25.43 ? 298 LEU B C   1 
ATOM   6082 O  O   . LEU B 1 298 ? -13.920 -13.757 -8.278  1.00 22.89 ? 298 LEU B O   1 
ATOM   6083 C  CB  . LEU B 1 298 ? -15.132 -15.510 -6.560  1.00 26.12 ? 298 LEU B CB  1 
ATOM   6084 C  CG  . LEU B 1 298 ? -15.778 -16.578 -5.686  1.00 25.71 ? 298 LEU B CG  1 
ATOM   6085 C  CD1 . LEU B 1 298 ? -15.647 -16.223 -4.212  1.00 26.82 ? 298 LEU B CD1 1 
ATOM   6086 C  CD2 . LEU B 1 298 ? -17.228 -16.765 -6.065  1.00 25.52 ? 298 LEU B CD2 1 
ATOM   6087 N  N   . VAL B 1 299 ? -14.834 -14.573 -10.195 1.00 26.91 ? 299 VAL B N   1 
ATOM   6088 C  CA  . VAL B 1 299 ? -14.108 -13.693 -11.163 1.00 28.00 ? 299 VAL B CA  1 
ATOM   6089 C  C   . VAL B 1 299 ? -14.706 -12.281 -11.126 1.00 29.36 ? 299 VAL B C   1 
ATOM   6090 O  O   . VAL B 1 299 ? -14.078 -11.373 -11.740 1.00 26.86 ? 299 VAL B O   1 
ATOM   6091 C  CB  . VAL B 1 299 ? -14.113 -14.286 -12.586 1.00 28.64 ? 299 VAL B CB  1 
ATOM   6092 C  CG1 . VAL B 1 299 ? -13.256 -15.527 -12.631 1.00 31.28 ? 299 VAL B CG1 1 
ATOM   6093 C  CG2 . VAL B 1 299 ? -15.503 -14.592 -13.125 1.00 28.18 ? 299 VAL B CG2 1 
ATOM   6094 N  N   . ASP B 1 300 ? -15.834 -12.116 -10.410 1.00 29.38 ? 300 ASP B N   1 
ATOM   6095 C  CA  . ASP B 1 300 ? -16.607 -10.850 -10.296 1.00 30.26 ? 300 ASP B CA  1 
ATOM   6096 C  C   . ASP B 1 300 ? -16.593 -10.327 -8.866  1.00 29.05 ? 300 ASP B C   1 
ATOM   6097 O  O   . ASP B 1 300 ? -16.589 -11.087 -7.896  1.00 29.17 ? 300 ASP B O   1 
ATOM   6098 C  CB  . ASP B 1 300 ? -18.047 -11.072 -10.754 1.00 33.35 ? 300 ASP B CB  1 
ATOM   6099 C  CG  . ASP B 1 300 ? -18.106 -11.613 -12.172 1.00 34.59 ? 300 ASP B CG  1 
ATOM   6100 O  OD1 . ASP B 1 300 ? -17.226 -11.251 -12.950 1.00 39.75 ? 300 ASP B OD1 1 
ATOM   6101 O  OD2 . ASP B 1 300 ? -18.980 -12.441 -12.462 1.00 33.81 ? 300 ASP B OD2 1 
ATOM   6102 N  N   . PRO B 1 301 ? -16.615 -8.995  -8.701  1.00 30.68 ? 301 PRO B N   1 
ATOM   6103 C  CA  . PRO B 1 301 ? -16.631 -8.362  -7.381  1.00 31.32 ? 301 PRO B CA  1 
ATOM   6104 C  C   . PRO B 1 301 ? -17.745 -8.827  -6.432  1.00 35.08 ? 301 PRO B C   1 
ATOM   6105 O  O   . PRO B 1 301 ? -17.482 -9.030  -5.251  1.00 41.27 ? 301 PRO B O   1 
ATOM   6106 C  CB  . PRO B 1 301 ? -16.886 -6.888  -7.711  1.00 32.33 ? 301 PRO B CB  1 
ATOM   6107 C  CG  . PRO B 1 301 ? -16.278 -6.701  -9.077  1.00 33.27 ? 301 PRO B CG  1 
ATOM   6108 C  CD  . PRO B 1 301 ? -16.545 -8.012  -9.794  1.00 33.81 ? 301 PRO B CD  1 
ATOM   6109 N  N   . VAL B 1 302 ? -18.965 -8.937  -6.956  1.00 32.66 ? 302 VAL B N   1 
ATOM   6110 C  CA  . VAL B 1 302 ? -20.162 -9.400  -6.199  1.00 30.33 ? 302 VAL B CA  1 
ATOM   6111 C  C   . VAL B 1 302 ? -20.498 -10.784 -6.736  1.00 28.92 ? 302 VAL B C   1 
ATOM   6112 O  O   . VAL B 1 302 ? -20.991 -10.917 -7.847  1.00 30.19 ? 302 VAL B O   1 
ATOM   6113 C  CB  . VAL B 1 302 ? -21.341 -8.410  -6.304  1.00 28.12 ? 302 VAL B CB  1 
ATOM   6114 C  CG1 . VAL B 1 302 ? -22.485 -8.814  -5.388  1.00 29.75 ? 302 VAL B CG1 1 
ATOM   6115 C  CG2 . VAL B 1 302 ? -20.905 -6.991  -5.982  1.00 29.16 ? 302 VAL B CG2 1 
ATOM   6116 N  N   . PRO B 1 303 ? -20.171 -11.864 -5.997  1.00 28.64 ? 303 PRO B N   1 
ATOM   6117 C  CA  . PRO B 1 303 ? -20.487 -13.217 -6.446  1.00 26.35 ? 303 PRO B CA  1 
ATOM   6118 C  C   . PRO B 1 303 ? -21.993 -13.435 -6.664  1.00 23.86 ? 303 PRO B C   1 
ATOM   6119 O  O   . PRO B 1 303 ? -22.774 -12.945 -5.878  1.00 21.44 ? 303 PRO B O   1 
ATOM   6120 C  CB  . PRO B 1 303 ? -19.999 -14.132 -5.310  1.00 26.80 ? 303 PRO B CB  1 
ATOM   6121 C  CG  . PRO B 1 303 ? -18.999 -13.284 -4.552  1.00 28.99 ? 303 PRO B CG  1 
ATOM   6122 C  CD  . PRO B 1 303 ? -19.483 -11.855 -4.694  1.00 29.16 ? 303 PRO B CD  1 
ATOM   6123 N  N   . SER B 1 304 ? -22.330 -14.146 -7.740  1.00 20.39 ? 304 SER B N   1 
ATOM   6124 C  CA  . SER B 1 304 ? -23.684 -14.638 -8.045  1.00 20.92 ? 304 SER B CA  1 
ATOM   6125 C  C   . SER B 1 304 ? -23.943 -15.926 -7.262  1.00 22.54 ? 304 SER B C   1 
ATOM   6126 O  O   . SER B 1 304 ? -22.949 -16.643 -6.893  1.00 21.53 ? 304 SER B O   1 
ATOM   6127 C  CB  . SER B 1 304 ? -23.841 -14.887 -9.514  1.00 20.25 ? 304 SER B CB  1 
ATOM   6128 O  OG  . SER B 1 304 ? -22.945 -15.908 -9.924  1.00 21.26 ? 304 SER B OG  1 
ATOM   6129 N  N   . TYR B 1 305 ? -25.232 -16.227 -7.087  1.00 22.33 ? 305 TYR B N   1 
ATOM   6130 C  CA  . TYR B 1 305 ? -25.770 -17.519 -6.585  1.00 25.18 ? 305 TYR B CA  1 
ATOM   6131 C  C   . TYR B 1 305 ? -25.049 -18.727 -7.230  1.00 24.56 ? 305 TYR B C   1 
ATOM   6132 O  O   . TYR B 1 305 ? -24.686 -19.661 -6.488  1.00 25.29 ? 305 TYR B O   1 
ATOM   6133 C  CB  . TYR B 1 305 ? -27.287 -17.586 -6.804  1.00 23.87 ? 305 TYR B CB  1 
ATOM   6134 C  CG  . TYR B 1 305 ? -27.868 -18.950 -6.527  1.00 25.65 ? 305 TYR B CG  1 
ATOM   6135 C  CD1 . TYR B 1 305 ? -28.169 -19.351 -5.233  1.00 26.08 ? 305 TYR B CD1 1 
ATOM   6136 C  CD2 . TYR B 1 305 ? -28.072 -19.859 -7.559  1.00 25.59 ? 305 TYR B CD2 1 
ATOM   6137 C  CE1 . TYR B 1 305 ? -28.680 -20.613 -4.973  1.00 27.06 ? 305 TYR B CE1 1 
ATOM   6138 C  CE2 . TYR B 1 305 ? -28.590 -21.123 -7.316  1.00 25.99 ? 305 TYR B CE2 1 
ATOM   6139 C  CZ  . TYR B 1 305 ? -28.904 -21.498 -6.020  1.00 27.41 ? 305 TYR B CZ  1 
ATOM   6140 O  OH  . TYR B 1 305 ? -29.430 -22.736 -5.775  1.00 28.54 ? 305 TYR B OH  1 
ATOM   6141 N  N   . LYS B 1 306 ? -24.839 -18.718 -8.543  1.00 22.07 ? 306 LYS B N   1 
ATOM   6142 C  CA  . LYS B 1 306 ? -24.371 -19.911 -9.297  1.00 22.19 ? 306 LYS B CA  1 
ATOM   6143 C  C   . LYS B 1 306 ? -22.865 -20.103 -9.114  1.00 21.58 ? 306 LYS B C   1 
ATOM   6144 O  O   . LYS B 1 306 ? -22.403 -21.266 -9.060  1.00 23.73 ? 306 LYS B O   1 
ATOM   6145 C  CB  . LYS B 1 306 ? -24.737 -19.791 -10.779 1.00 23.09 ? 306 LYS B CB  1 
ATOM   6146 C  CG  . LYS B 1 306 ? -26.181 -20.158 -11.118 1.00 23.23 ? 306 LYS B CG  1 
ATOM   6147 C  CD  . LYS B 1 306 ? -26.382 -20.561 -12.595 1.00 24.62 ? 306 LYS B CD  1 
ATOM   6148 C  CE  . LYS B 1 306 ? -25.949 -19.505 -13.595 1.00 23.21 ? 306 LYS B CE  1 
ATOM   6149 N  NZ  . LYS B 1 306 ? -26.038 -20.015 -14.976 1.00 23.04 ? 306 LYS B NZ  1 
ATOM   6150 N  N   . GLN B 1 307 ? -22.108 -19.021 -8.986  1.00 21.45 ? 307 GLN B N   1 
ATOM   6151 C  CA  . GLN B 1 307 ? -20.651 -19.119 -8.722  1.00 20.58 ? 307 GLN B CA  1 
ATOM   6152 C  C   . GLN B 1 307 ? -20.445 -19.748 -7.339  1.00 20.77 ? 307 GLN B C   1 
ATOM   6153 O  O   . GLN B 1 307 ? -19.523 -20.593 -7.207  1.00 18.39 ? 307 GLN B O   1 
ATOM   6154 C  CB  . GLN B 1 307 ? -19.993 -17.742 -8.766  1.00 21.63 ? 307 GLN B CB  1 
ATOM   6155 C  CG  . GLN B 1 307 ? -20.136 -17.023 -10.093 1.00 21.93 ? 307 GLN B CG  1 
ATOM   6156 C  CD  . GLN B 1 307 ? -19.698 -15.585 -9.964  1.00 22.37 ? 307 GLN B CD  1 
ATOM   6157 O  OE1 . GLN B 1 307 ? -19.940 -14.919 -8.953  1.00 19.83 ? 307 GLN B OE1 1 
ATOM   6158 N  NE2 . GLN B 1 307 ? -19.009 -15.112 -10.988 1.00 22.54 ? 307 GLN B NE2 1 
ATOM   6159 N  N   . VAL B 1 308 ? -21.255 -19.342 -6.344  1.00 19.90 ? 308 VAL B N   1 
ATOM   6160 C  CA  . VAL B 1 308 ? -21.201 -19.953 -4.985  1.00 20.85 ? 308 VAL B CA  1 
ATOM   6161 C  C   . VAL B 1 308 ? -21.322 -21.482 -5.133  1.00 20.62 ? 308 VAL B C   1 
ATOM   6162 O  O   . VAL B 1 308 ? -20.557 -22.191 -4.500  1.00 18.82 ? 308 VAL B O   1 
ATOM   6163 C  CB  . VAL B 1 308 ? -22.256 -19.374 -4.021  1.00 21.13 ? 308 VAL B CB  1 
ATOM   6164 C  CG1 . VAL B 1 308 ? -22.327 -20.188 -2.728  1.00 21.95 ? 308 VAL B CG1 1 
ATOM   6165 C  CG2 . VAL B 1 308 ? -22.007 -17.914 -3.710  1.00 20.47 ? 308 VAL B CG2 1 
ATOM   6166 N  N   . LYS B 1 309 ? -22.221 -21.974 -5.986  1.00 24.05 ? 309 LYS B N   1 
ATOM   6167 C  CA  . LYS B 1 309 ? -22.514 -23.431 -6.157  1.00 24.46 ? 309 LYS B CA  1 
ATOM   6168 C  C   . LYS B 1 309 ? -21.309 -24.185 -6.749  1.00 23.46 ? 309 LYS B C   1 
ATOM   6169 O  O   . LYS B 1 309 ? -21.308 -25.409 -6.666  1.00 23.51 ? 309 LYS B O   1 
ATOM   6170 C  CB  . LYS B 1 309 ? -23.769 -23.605 -7.020  1.00 26.27 ? 309 LYS B CB  1 
ATOM   6171 C  CG  . LYS B 1 309 ? -25.040 -22.979 -6.449  1.00 28.74 ? 309 LYS B CG  1 
ATOM   6172 C  CD  . LYS B 1 309 ? -25.569 -23.737 -5.258  1.00 31.54 ? 309 LYS B CD  1 
ATOM   6173 C  CE  . LYS B 1 309 ? -26.372 -22.912 -4.264  1.00 34.02 ? 309 LYS B CE  1 
ATOM   6174 N  NZ  . LYS B 1 309 ? -26.170 -23.355 -2.856  1.00 31.51 ? 309 LYS B NZ  1 
ATOM   6175 N  N   . GLN B 1 310 ? -20.345 -23.479 -7.349  1.00 24.33 ? 310 GLN B N   1 
ATOM   6176 C  CA  . GLN B 1 310 ? -19.135 -24.027 -8.031  1.00 25.22 ? 310 GLN B CA  1 
ATOM   6177 C  C   . GLN B 1 310 ? -17.946 -24.168 -7.070  1.00 23.49 ? 310 GLN B C   1 
ATOM   6178 O  O   . GLN B 1 310 ? -16.956 -24.799 -7.470  1.00 23.79 ? 310 GLN B O   1 
ATOM   6179 C  CB  . GLN B 1 310 ? -18.689 -23.080 -9.152  1.00 26.07 ? 310 GLN B CB  1 
ATOM   6180 C  CG  . GLN B 1 310 ? -19.599 -23.084 -10.347 1.00 26.85 ? 310 GLN B CG  1 
ATOM   6181 C  CD  . GLN B 1 310 ? -19.538 -24.469 -10.921 1.00 28.33 ? 310 GLN B CD  1 
ATOM   6182 O  OE1 . GLN B 1 310 ? -18.549 -24.864 -11.520 1.00 34.39 ? 310 GLN B OE1 1 
ATOM   6183 N  NE2 . GLN B 1 310 ? -20.574 -25.239 -10.671 1.00 30.30 ? 310 GLN B NE2 1 
ATOM   6184 N  N   . LEU B 1 311 ? -18.017 -23.550 -5.889  1.00 22.56 ? 311 LEU B N   1 
ATOM   6185 C  CA  . LEU B 1 311 ? -16.972 -23.590 -4.829  1.00 23.27 ? 311 LEU B CA  1 
ATOM   6186 C  C   . LEU B 1 311 ? -16.995 -24.974 -4.142  1.00 25.31 ? 311 LEU B C   1 
ATOM   6187 O  O   . LEU B 1 311 ? -17.207 -25.061 -2.888  1.00 21.58 ? 311 LEU B O   1 
ATOM   6188 C  CB  . LEU B 1 311 ? -17.195 -22.425 -3.855  1.00 22.05 ? 311 LEU B CB  1 
ATOM   6189 C  CG  . LEU B 1 311 ? -17.013 -21.032 -4.465  1.00 21.84 ? 311 LEU B CG  1 
ATOM   6190 C  CD1 . LEU B 1 311 ? -17.351 -19.938 -3.465  1.00 20.69 ? 311 LEU B CD1 1 
ATOM   6191 C  CD2 . LEU B 1 311 ? -15.595 -20.860 -5.001  1.00 22.48 ? 311 LEU B CD2 1 
ATOM   6192 N  N   . LYS B 1 312 ? -16.726 -26.026 -4.930  1.00 25.11 ? 312 LYS B N   1 
ATOM   6193 C  CA  . LYS B 1 312 ? -16.932 -27.424 -4.487  1.00 26.42 ? 312 LYS B CA  1 
ATOM   6194 C  C   . LYS B 1 312 ? -15.982 -27.697 -3.323  1.00 23.91 ? 312 LYS B C   1 
ATOM   6195 O  O   . LYS B 1 312 ? -16.453 -28.204 -2.278  1.00 23.01 ? 312 LYS B O   1 
ATOM   6196 C  CB  . LYS B 1 312 ? -16.736 -28.385 -5.662  1.00 31.13 ? 312 LYS B CB  1 
ATOM   6197 C  CG  . LYS B 1 312 ? -17.730 -28.219 -6.811  1.00 36.61 ? 312 LYS B CG  1 
ATOM   6198 C  CD  . LYS B 1 312 ? -19.208 -28.183 -6.354  1.00 42.64 ? 312 LYS B CD  1 
ATOM   6199 C  CE  . LYS B 1 312 ? -20.206 -28.254 -7.500  1.00 45.31 ? 312 LYS B CE  1 
ATOM   6200 N  NZ  . LYS B 1 312 ? -21.615 -28.157 -7.035  1.00 49.09 ? 312 LYS B NZ  1 
ATOM   6201 N  N   . TYR B 1 313 ? -14.696 -27.362 -3.497  1.00 21.82 ? 313 TYR B N   1 
ATOM   6202 C  CA  . TYR B 1 313 ? -13.642 -27.676 -2.512  1.00 20.14 ? 313 TYR B CA  1 
ATOM   6203 C  C   . TYR B 1 313 ? -13.928 -26.921 -1.212  1.00 18.74 ? 313 TYR B C   1 
ATOM   6204 O  O   . TYR B 1 313 ? -13.692 -27.470 -0.109  1.00 19.29 ? 313 TYR B O   1 
ATOM   6205 C  CB  . TYR B 1 313 ? -12.242 -27.384 -3.043  1.00 20.48 ? 313 TYR B CB  1 
ATOM   6206 C  CG  . TYR B 1 313 ? -11.177 -27.897 -2.115  1.00 19.75 ? 313 TYR B CG  1 
ATOM   6207 C  CD1 . TYR B 1 313 ? -10.912 -29.251 -2.028  1.00 20.71 ? 313 TYR B CD1 1 
ATOM   6208 C  CD2 . TYR B 1 313 ? -10.522 -27.050 -1.239  1.00 20.14 ? 313 TYR B CD2 1 
ATOM   6209 C  CE1 . TYR B 1 313 ? -9.975  -29.742 -1.128  1.00 21.51 ? 313 TYR B CE1 1 
ATOM   6210 C  CE2 . TYR B 1 313 ? -9.575  -27.525 -0.341  1.00 20.50 ? 313 TYR B CE2 1 
ATOM   6211 C  CZ  . TYR B 1 313 ? -9.286  -28.874 -0.298  1.00 20.54 ? 313 TYR B CZ  1 
ATOM   6212 O  OH  . TYR B 1 313 ? -8.345  -29.361 0.565   1.00 21.09 ? 313 TYR B OH  1 
ATOM   6213 N  N   . VAL B 1 314 ? -14.432 -25.706 -1.316  1.00 16.46 ? 314 VAL B N   1 
ATOM   6214 C  CA  . VAL B 1 314 ? -14.758 -24.912 -0.100  1.00 16.62 ? 314 VAL B CA  1 
ATOM   6215 C  C   . VAL B 1 314 ? -15.888 -25.614 0.649   1.00 17.07 ? 314 VAL B C   1 
ATOM   6216 O  O   . VAL B 1 314 ? -15.819 -25.697 1.882   1.00 18.25 ? 314 VAL B O   1 
ATOM   6217 C  CB  . VAL B 1 314 ? -15.104 -23.473 -0.480  1.00 16.85 ? 314 VAL B CB  1 
ATOM   6218 C  CG1 . VAL B 1 314 ? -15.811 -22.747 0.643   1.00 17.36 ? 314 VAL B CG1 1 
ATOM   6219 C  CG2 . VAL B 1 314 ? -13.861 -22.733 -0.941  1.00 17.48 ? 314 VAL B CG2 1 
ATOM   6220 N  N   . GLY B 1 315 ? -16.860 -26.156 -0.086  1.00 17.40 ? 315 GLY B N   1 
ATOM   6221 C  CA  . GLY B 1 315 ? -17.910 -27.037 0.459   1.00 17.81 ? 315 GLY B CA  1 
ATOM   6222 C  C   . GLY B 1 315 ? -17.330 -28.188 1.255   1.00 16.86 ? 315 GLY B C   1 
ATOM   6223 O  O   . GLY B 1 315 ? -17.837 -28.515 2.341   1.00 17.46 ? 315 GLY B O   1 
ATOM   6224 N  N   . MET B 1 316 ? -16.325 -28.836 0.707   1.00 16.66 ? 316 MET B N   1 
ATOM   6225 C  CA  . MET B 1 316 ? -15.707 -30.000 1.370   1.00 18.11 ? 316 MET B CA  1 
ATOM   6226 C  C   . MET B 1 316 ? -14.998 -29.518 2.633   1.00 16.95 ? 316 MET B C   1 
ATOM   6227 O  O   . MET B 1 316 ? -14.983 -30.255 3.658   1.00 15.65 ? 316 MET B O   1 
ATOM   6228 C  CB  . MET B 1 316 ? -14.746 -30.668 0.396   1.00 20.08 ? 316 MET B CB  1 
ATOM   6229 C  CG  . MET B 1 316 ? -15.499 -31.373 -0.714  1.00 22.64 ? 316 MET B CG  1 
ATOM   6230 S  SD  . MET B 1 316 ? -14.470 -31.750 -2.148  1.00 25.38 ? 316 MET B SD  1 
ATOM   6231 C  CE  . MET B 1 316 ? -13.214 -32.779 -1.391  1.00 26.18 ? 316 MET B CE  1 
ATOM   6232 N  N   . VAL B 1 317 ? -14.469 -28.294 2.579   1.00 17.65 ? 317 VAL B N   1 
ATOM   6233 C  CA  . VAL B 1 317 ? -13.742 -27.687 3.727   1.00 18.42 ? 317 VAL B CA  1 
ATOM   6234 C  C   . VAL B 1 317 ? -14.764 -27.503 4.854   1.00 18.45 ? 317 VAL B C   1 
ATOM   6235 O  O   . VAL B 1 317 ? -14.403 -27.774 6.031   1.00 16.69 ? 317 VAL B O   1 
ATOM   6236 C  CB  . VAL B 1 317 ? -13.022 -26.378 3.338   1.00 19.02 ? 317 VAL B CB  1 
ATOM   6237 C  CG1 . VAL B 1 317 ? -12.760 -25.494 4.551   1.00 18.31 ? 317 VAL B CG1 1 
ATOM   6238 C  CG2 . VAL B 1 317 ? -11.727 -26.655 2.571   1.00 18.90 ? 317 VAL B CG2 1 
ATOM   6239 N  N   . LEU B 1 318 ? -15.980 -27.073 4.483   1.00 18.62 ? 318 LEU B N   1 
ATOM   6240 C  CA  . LEU B 1 318 ? -17.085 -26.780 5.434   1.00 19.03 ? 318 LEU B CA  1 
ATOM   6241 C  C   . LEU B 1 318 ? -17.549 -28.086 6.067   1.00 18.38 ? 318 LEU B C   1 
ATOM   6242 O  O   . LEU B 1 318 ? -17.725 -28.104 7.291   1.00 18.85 ? 318 LEU B O   1 
ATOM   6243 C  CB  . LEU B 1 318 ? -18.241 -26.058 4.740   1.00 18.61 ? 318 LEU B CB  1 
ATOM   6244 C  CG  . LEU B 1 318 ? -17.973 -24.611 4.338   1.00 19.13 ? 318 LEU B CG  1 
ATOM   6245 C  CD1 . LEU B 1 318 ? -19.233 -23.977 3.778   1.00 19.48 ? 318 LEU B CD1 1 
ATOM   6246 C  CD2 . LEU B 1 318 ? -17.460 -23.793 5.507   1.00 19.71 ? 318 LEU B CD2 1 
ATOM   6247 N  N   . ASN B 1 319 ? -17.682 -29.145 5.272   1.00 17.97 ? 319 ASN B N   1 
ATOM   6248 C  CA  . ASN B 1 319 ? -18.124 -30.470 5.779   1.00 17.62 ? 319 ASN B CA  1 
ATOM   6249 C  C   . ASN B 1 319 ? -17.091 -31.059 6.728   1.00 17.29 ? 319 ASN B C   1 
ATOM   6250 O  O   . ASN B 1 319 ? -17.493 -31.609 7.770   1.00 16.00 ? 319 ASN B O   1 
ATOM   6251 C  CB  . ASN B 1 319 ? -18.404 -31.441 4.637   1.00 19.01 ? 319 ASN B CB  1 
ATOM   6252 C  CG  . ASN B 1 319 ? -19.774 -31.177 4.055   1.00 20.16 ? 319 ASN B CG  1 
ATOM   6253 O  OD1 . ASN B 1 319 ? -20.678 -30.744 4.764   1.00 18.69 ? 319 ASN B OD1 1 
ATOM   6254 N  ND2 . ASN B 1 319 ? -19.916 -31.393 2.761   1.00 20.90 ? 319 ASN B ND2 1 
ATOM   6255 N  N   . GLU B 1 320 ? -15.813 -30.983 6.353   1.00 18.48 ? 320 GLU B N   1 
ATOM   6256 C  CA  . GLU B 1 320 ? -14.691 -31.499 7.181   1.00 18.66 ? 320 GLU B CA  1 
ATOM   6257 C  C   . GLU B 1 320 ? -14.651 -30.764 8.534   1.00 18.71 ? 320 GLU B C   1 
ATOM   6258 O  O   . GLU B 1 320 ? -14.313 -31.432 9.538   1.00 20.11 ? 320 GLU B O   1 
ATOM   6259 C  CB  . GLU B 1 320 ? -13.383 -31.372 6.406   1.00 19.12 ? 320 GLU B CB  1 
ATOM   6260 C  CG  . GLU B 1 320 ? -12.192 -32.046 7.064   1.00 19.75 ? 320 GLU B CG  1 
ATOM   6261 C  CD  . GLU B 1 320 ? -12.339 -33.528 7.409   1.00 20.97 ? 320 GLU B CD  1 
ATOM   6262 O  OE1 . GLU B 1 320 ? -13.462 -34.069 7.254   1.00 20.16 ? 320 GLU B OE1 1 
ATOM   6263 O  OE2 . GLU B 1 320 ? -11.319 -34.151 7.827   1.00 20.11 ? 320 GLU B OE2 1 
ATOM   6264 N  N   . ALA B 1 321 ? -14.965 -29.460 8.558   1.00 17.61 ? 321 ALA B N   1 
ATOM   6265 C  CA  . ALA B 1 321 ? -15.069 -28.609 9.771   1.00 18.12 ? 321 ALA B CA  1 
ATOM   6266 C  C   . ALA B 1 321 ? -16.299 -28.996 10.600  1.00 19.21 ? 321 ALA B C   1 
ATOM   6267 O  O   . ALA B 1 321 ? -16.202 -28.990 11.840  1.00 18.98 ? 321 ALA B O   1 
ATOM   6268 C  CB  . ALA B 1 321 ? -15.148 -27.149 9.391   1.00 17.90 ? 321 ALA B CB  1 
ATOM   6269 N  N   . LEU B 1 322 ? -17.418 -29.316 9.940   1.00 19.55 ? 322 LEU B N   1 
ATOM   6270 C  CA  . LEU B 1 322 ? -18.596 -29.917 10.617  1.00 19.97 ? 322 LEU B CA  1 
ATOM   6271 C  C   . LEU B 1 322 ? -18.215 -31.281 11.212  1.00 19.12 ? 322 LEU B C   1 
ATOM   6272 O  O   . LEU B 1 322 ? -18.662 -31.559 12.357  1.00 18.16 ? 322 LEU B O   1 
ATOM   6273 C  CB  . LEU B 1 322 ? -19.756 -30.046 9.629   1.00 20.60 ? 322 LEU B CB  1 
ATOM   6274 C  CG  . LEU B 1 322 ? -20.386 -28.729 9.192   1.00 22.08 ? 322 LEU B CG  1 
ATOM   6275 C  CD1 . LEU B 1 322 ? -21.548 -29.004 8.241   1.00 23.36 ? 322 LEU B CD1 1 
ATOM   6276 C  CD2 . LEU B 1 322 ? -20.857 -27.909 10.387  1.00 21.26 ? 322 LEU B CD2 1 
ATOM   6277 N  N   . ARG B 1 323 ? -17.433 -32.101 10.497  1.00 17.54 ? 323 ARG B N   1 
ATOM   6278 C  CA  . ARG B 1 323 ? -17.005 -33.422 11.029  1.00 17.50 ? 323 ARG B CA  1 
ATOM   6279 C  C   . ARG B 1 323 ? -16.330 -33.212 12.390  1.00 17.83 ? 323 ARG B C   1 
ATOM   6280 O  O   . ARG B 1 323 ? -16.943 -33.643 13.400  1.00 17.72 ? 323 ARG B O   1 
ATOM   6281 C  CB  . ARG B 1 323 ? -16.086 -34.221 10.110  1.00 17.49 ? 323 ARG B CB  1 
ATOM   6282 C  CG  . ARG B 1 323 ? -15.952 -35.675 10.568  1.00 19.19 ? 323 ARG B CG  1 
ATOM   6283 C  CD  . ARG B 1 323 ? -15.093 -36.547 9.658   1.00 19.50 ? 323 ARG B CD  1 
ATOM   6284 N  NE  . ARG B 1 323 ? -13.737 -36.014 9.528   1.00 18.73 ? 323 ARG B NE  1 
ATOM   6285 C  CZ  . ARG B 1 323 ? -12.781 -36.160 10.426  1.00 19.68 ? 323 ARG B CZ  1 
ATOM   6286 N  NH1 . ARG B 1 323 ? -13.001 -36.824 11.552  1.00 21.00 ? 323 ARG B NH1 1 
ATOM   6287 N  NH2 . ARG B 1 323 ? -11.609 -35.594 10.229  1.00 20.45 ? 323 ARG B NH2 1 
ATOM   6288 N  N   . LEU B 1 324 ? -15.163 -32.553 12.419  1.00 17.76 ? 324 LEU B N   1 
ATOM   6289 C  CA  . LEU B 1 324 ? -14.266 -32.447 13.617  1.00 19.20 ? 324 LEU B CA  1 
ATOM   6290 C  C   . LEU B 1 324 ? -14.909 -31.595 14.718  1.00 18.92 ? 324 LEU B C   1 
ATOM   6291 O  O   . LEU B 1 324 ? -14.820 -31.978 15.855  1.00 20.15 ? 324 LEU B O   1 
ATOM   6292 C  CB  . LEU B 1 324 ? -12.903 -31.878 13.207  1.00 20.69 ? 324 LEU B CB  1 
ATOM   6293 C  CG  . LEU B 1 324 ? -11.910 -32.887 12.607  1.00 23.16 ? 324 LEU B CG  1 
ATOM   6294 C  CD1 . LEU B 1 324 ? -10.708 -32.191 11.954  1.00 24.39 ? 324 LEU B CD1 1 
ATOM   6295 C  CD2 . LEU B 1 324 ? -11.420 -33.876 13.660  1.00 22.61 ? 324 LEU B CD2 1 
ATOM   6296 N  N   . TRP B 1 325 ? -15.593 -30.503 14.403  1.00 19.45 ? 325 TRP B N   1 
ATOM   6297 C  CA  . TRP B 1 325 ? -16.330 -29.721 15.441  1.00 21.48 ? 325 TRP B CA  1 
ATOM   6298 C  C   . TRP B 1 325 ? -17.698 -29.308 14.917  1.00 20.28 ? 325 TRP B C   1 
ATOM   6299 O  O   . TRP B 1 325 ? -17.848 -28.209 14.389  1.00 19.45 ? 325 TRP B O   1 
ATOM   6300 C  CB  . TRP B 1 325 ? -15.535 -28.509 15.953  1.00 21.45 ? 325 TRP B CB  1 
ATOM   6301 C  CG  . TRP B 1 325 ? -14.364 -28.930 16.775  1.00 23.35 ? 325 TRP B CG  1 
ATOM   6302 C  CD1 . TRP B 1 325 ? -13.043 -28.842 16.434  1.00 23.97 ? 325 TRP B CD1 1 
ATOM   6303 C  CD2 . TRP B 1 325 ? -14.409 -29.577 18.058  1.00 24.06 ? 325 TRP B CD2 1 
ATOM   6304 N  NE1 . TRP B 1 325 ? -12.261 -29.370 17.425  1.00 24.06 ? 325 TRP B NE1 1 
ATOM   6305 C  CE2 . TRP B 1 325 ? -13.066 -29.813 18.442  1.00 23.93 ? 325 TRP B CE2 1 
ATOM   6306 C  CE3 . TRP B 1 325 ? -15.443 -29.923 18.942  1.00 24.34 ? 325 TRP B CE3 1 
ATOM   6307 C  CZ2 . TRP B 1 325 ? -12.739 -30.398 19.666  1.00 23.40 ? 325 TRP B CZ2 1 
ATOM   6308 C  CZ3 . TRP B 1 325 ? -15.120 -30.515 20.147  1.00 24.63 ? 325 TRP B CZ3 1 
ATOM   6309 C  CH2 . TRP B 1 325 ? -13.783 -30.758 20.493  1.00 24.35 ? 325 TRP B CH2 1 
ATOM   6310 N  N   . PRO B 1 326 ? -18.712 -30.187 15.091  1.00 19.64 ? 326 PRO B N   1 
ATOM   6311 C  CA  . PRO B 1 326 ? -20.076 -29.905 14.652  1.00 18.70 ? 326 PRO B CA  1 
ATOM   6312 C  C   . PRO B 1 326 ? -20.625 -28.878 15.647  1.00 18.63 ? 326 PRO B C   1 
ATOM   6313 O  O   . PRO B 1 326 ? -20.778 -29.201 16.799  1.00 18.71 ? 326 PRO B O   1 
ATOM   6314 C  CB  . PRO B 1 326 ? -20.791 -31.262 14.700  1.00 18.33 ? 326 PRO B CB  1 
ATOM   6315 C  CG  . PRO B 1 326 ? -19.976 -32.097 15.706  1.00 19.06 ? 326 PRO B CG  1 
ATOM   6316 C  CD  . PRO B 1 326 ? -18.587 -31.500 15.744  1.00 19.32 ? 326 PRO B CD  1 
ATOM   6317 N  N   . THR B 1 327 ? -20.858 -27.665 15.170  1.00 17.97 ? 327 THR B N   1 
ATOM   6318 C  CA  . THR B 1 327 ? -21.101 -26.488 16.021  1.00 18.65 ? 327 THR B CA  1 
ATOM   6319 C  C   . THR B 1 327 ? -22.377 -26.730 16.827  1.00 19.57 ? 327 THR B C   1 
ATOM   6320 O  O   . THR B 1 327 ? -22.448 -26.266 18.011  1.00 19.23 ? 327 THR B O   1 
ATOM   6321 C  CB  . THR B 1 327 ? -21.097 -25.207 15.189  1.00 19.15 ? 327 THR B CB  1 
ATOM   6322 O  OG1 . THR B 1 327 ? -21.369 -24.149 16.104  1.00 20.07 ? 327 THR B OG1 1 
ATOM   6323 C  CG2 . THR B 1 327 ? -22.123 -25.184 14.081  1.00 19.46 ? 327 THR B CG2 1 
ATOM   6324 N  N   . ALA B 1 328 ? -23.361 -27.385 16.211  1.00 19.56 ? 328 ALA B N   1 
ATOM   6325 C  CA  . ALA B 1 328 ? -24.551 -27.892 16.920  1.00 20.47 ? 328 ALA B CA  1 
ATOM   6326 C  C   . ALA B 1 328 ? -24.174 -29.314 17.296  1.00 19.86 ? 328 ALA B C   1 
ATOM   6327 O  O   . ALA B 1 328 ? -24.065 -30.165 16.419  1.00 20.86 ? 328 ALA B O   1 
ATOM   6328 C  CB  . ALA B 1 328 ? -25.814 -27.787 16.086  1.00 20.26 ? 328 ALA B CB  1 
ATOM   6329 N  N   . PRO B 1 329 ? -23.828 -29.559 18.582  1.00 17.63 ? 329 PRO B N   1 
ATOM   6330 C  CA  . PRO B 1 329 ? -23.058 -30.742 18.943  1.00 18.00 ? 329 PRO B CA  1 
ATOM   6331 C  C   . PRO B 1 329 ? -23.902 -31.968 19.337  1.00 16.40 ? 329 PRO B C   1 
ATOM   6332 O  O   . PRO B 1 329 ? -23.332 -32.980 19.689  1.00 16.07 ? 329 PRO B O   1 
ATOM   6333 C  CB  . PRO B 1 329 ? -22.245 -30.159 20.119  1.00 17.40 ? 329 PRO B CB  1 
ATOM   6334 C  CG  . PRO B 1 329 ? -23.221 -29.272 20.827  1.00 17.23 ? 329 PRO B CG  1 
ATOM   6335 C  CD  . PRO B 1 329 ? -24.088 -28.691 19.735  1.00 16.76 ? 329 PRO B CD  1 
ATOM   6336 N  N   . ALA B 1 330 ? -25.222 -31.874 19.318  1.00 15.72 ? 330 ALA B N   1 
ATOM   6337 C  CA  . ALA B 1 330 ? -26.044 -33.002 19.816  1.00 18.94 ? 330 ALA B CA  1 
ATOM   6338 C  C   . ALA B 1 330 ? -27.527 -32.855 19.452  1.00 19.00 ? 330 ALA B C   1 
ATOM   6339 O  O   . ALA B 1 330 ? -28.011 -31.729 19.227  1.00 20.71 ? 330 ALA B O   1 
ATOM   6340 C  CB  . ALA B 1 330 ? -25.849 -33.179 21.314  1.00 17.58 ? 330 ALA B CB  1 
ATOM   6341 N  N   . PHE B 1 331 ? -28.224 -33.985 19.420  1.00 18.90 ? 331 PHE B N   1 
ATOM   6342 C  CA  . PHE B 1 331 ? -29.687 -34.029 19.183  1.00 19.08 ? 331 PHE B CA  1 
ATOM   6343 C  C   . PHE B 1 331 ? -30.250 -35.233 19.933  1.00 18.74 ? 331 PHE B C   1 
ATOM   6344 O  O   . PHE B 1 331 ? -29.503 -36.234 20.086  1.00 17.19 ? 331 PHE B O   1 
ATOM   6345 C  CB  . PHE B 1 331 ? -29.987 -34.009 17.687  1.00 18.66 ? 331 PHE B CB  1 
ATOM   6346 C  CG  . PHE B 1 331 ? -29.515 -35.175 16.862  1.00 19.46 ? 331 PHE B CG  1 
ATOM   6347 C  CD1 . PHE B 1 331 ? -30.311 -36.297 16.692  1.00 19.93 ? 331 PHE B CD1 1 
ATOM   6348 C  CD2 . PHE B 1 331 ? -28.355 -35.078 16.112  1.00 19.99 ? 331 PHE B CD2 1 
ATOM   6349 C  CE1 . PHE B 1 331 ? -29.926 -37.328 15.849  1.00 19.22 ? 331 PHE B CE1 1 
ATOM   6350 C  CE2 . PHE B 1 331 ? -27.960 -36.119 15.281  1.00 20.63 ? 331 PHE B CE2 1 
ATOM   6351 C  CZ  . PHE B 1 331 ? -28.737 -37.245 15.160  1.00 19.61 ? 331 PHE B CZ  1 
ATOM   6352 N  N   . SER B 1 332 ? -31.484 -35.119 20.439  1.00 16.63 ? 332 SER B N   1 
ATOM   6353 C  CA  . SER B 1 332 ? -32.060 -36.150 21.338  1.00 16.17 ? 332 SER B CA  1 
ATOM   6354 C  C   . SER B 1 332 ? -33.126 -36.974 20.598  1.00 17.42 ? 332 SER B C   1 
ATOM   6355 O  O   . SER B 1 332 ? -33.812 -36.445 19.723  1.00 18.69 ? 332 SER B O   1 
ATOM   6356 C  CB  . SER B 1 332 ? -32.574 -35.522 22.597  1.00 15.06 ? 332 SER B CB  1 
ATOM   6357 O  OG  . SER B 1 332 ? -32.953 -36.510 23.537  1.00 15.24 ? 332 SER B OG  1 
ATOM   6358 N  N   . LEU B 1 333 ? -33.264 -38.248 20.953  1.00 19.32 ? 333 LEU B N   1 
ATOM   6359 C  CA  . LEU B 1 333 ? -34.293 -39.161 20.392  1.00 20.23 ? 333 LEU B CA  1 
ATOM   6360 C  C   . LEU B 1 333 ? -35.036 -39.834 21.556  1.00 19.62 ? 333 LEU B C   1 
ATOM   6361 O  O   . LEU B 1 333 ? -34.472 -39.869 22.688  1.00 18.01 ? 333 LEU B O   1 
ATOM   6362 C  CB  . LEU B 1 333 ? -33.604 -40.186 19.488  1.00 22.01 ? 333 LEU B CB  1 
ATOM   6363 C  CG  . LEU B 1 333 ? -32.614 -39.610 18.472  1.00 23.97 ? 333 LEU B CG  1 
ATOM   6364 C  CD1 . LEU B 1 333 ? -31.673 -40.677 17.967  1.00 25.26 ? 333 LEU B CD1 1 
ATOM   6365 C  CD2 . LEU B 1 333 ? -33.360 -38.986 17.306  1.00 25.15 ? 333 LEU B CD2 1 
ATOM   6366 N  N   . TYR B 1 334 ? -36.280 -40.270 21.322  1.00 18.57 ? 334 TYR B N   1 
ATOM   6367 C  CA  . TYR B 1 334 ? -37.005 -41.157 22.270  1.00 19.72 ? 334 TYR B CA  1 
ATOM   6368 C  C   . TYR B 1 334 ? -37.420 -42.413 21.508  1.00 18.91 ? 334 TYR B C   1 
ATOM   6369 O  O   . TYR B 1 334 ? -37.643 -42.296 20.274  1.00 17.73 ? 334 TYR B O   1 
ATOM   6370 C  CB  . TYR B 1 334 ? -38.153 -40.449 23.011  1.00 19.52 ? 334 TYR B CB  1 
ATOM   6371 C  CG  . TYR B 1 334 ? -39.382 -40.128 22.198  1.00 18.62 ? 334 TYR B CG  1 
ATOM   6372 C  CD1 . TYR B 1 334 ? -39.474 -38.929 21.519  1.00 19.37 ? 334 TYR B CD1 1 
ATOM   6373 C  CD2 . TYR B 1 334 ? -40.437 -41.011 22.105  1.00 17.96 ? 334 TYR B CD2 1 
ATOM   6374 C  CE1 . TYR B 1 334 ? -40.568 -38.625 20.737  1.00 19.80 ? 334 TYR B CE1 1 
ATOM   6375 C  CE2 . TYR B 1 334 ? -41.549 -40.720 21.337  1.00 19.51 ? 334 TYR B CE2 1 
ATOM   6376 C  CZ  . TYR B 1 334 ? -41.623 -39.517 20.647  1.00 20.22 ? 334 TYR B CZ  1 
ATOM   6377 O  OH  . TYR B 1 334 ? -42.724 -39.167 19.898  1.00 19.69 ? 334 TYR B OH  1 
ATOM   6378 N  N   . ALA B 1 335 ? -37.455 -43.544 22.229  1.00 18.20 ? 335 ALA B N   1 
ATOM   6379 C  CA  . ALA B 1 335 ? -37.978 -44.839 21.749  1.00 20.72 ? 335 ALA B CA  1 
ATOM   6380 C  C   . ALA B 1 335 ? -39.507 -44.739 21.670  1.00 22.94 ? 335 ALA B C   1 
ATOM   6381 O  O   . ALA B 1 335 ? -40.143 -44.434 22.696  1.00 23.27 ? 335 ALA B O   1 
ATOM   6382 C  CB  . ALA B 1 335 ? -37.546 -45.962 22.653  1.00 20.86 ? 335 ALA B CB  1 
ATOM   6383 N  N   . LYS B 1 336 ? -40.091 -44.967 20.502  1.00 22.03 ? 336 LYS B N   1 
ATOM   6384 C  CA  . LYS B 1 336 ? -41.560 -44.809 20.381  1.00 26.86 ? 336 LYS B CA  1 
ATOM   6385 C  C   . LYS B 1 336 ? -42.248 -46.146 20.721  1.00 26.83 ? 336 LYS B C   1 
ATOM   6386 O  O   . LYS B 1 336 ? -43.455 -46.140 21.023  1.00 25.31 ? 336 LYS B O   1 
ATOM   6387 C  CB  . LYS B 1 336 ? -41.903 -44.179 19.028  1.00 25.68 ? 336 LYS B CB  1 
ATOM   6388 C  CG  . LYS B 1 336 ? -41.503 -44.990 17.829  1.00 26.69 ? 336 LYS B CG  1 
ATOM   6389 C  CD  . LYS B 1 336 ? -40.841 -44.084 16.868  1.00 28.52 ? 336 LYS B CD  1 
ATOM   6390 C  CE  . LYS B 1 336 ? -41.825 -43.105 16.302  1.00 25.97 ? 336 LYS B CE  1 
ATOM   6391 N  NZ  . LYS B 1 336 ? -42.220 -43.584 14.971  1.00 25.98 ? 336 LYS B NZ  1 
ATOM   6392 N  N   . GLU B 1 337 ? -41.474 -47.228 20.764  1.00 30.41 ? 337 GLU B N   1 
ATOM   6393 C  CA  . GLU B 1 337 ? -41.901 -48.574 21.237  1.00 31.85 ? 337 GLU B CA  1 
ATOM   6394 C  C   . GLU B 1 337 ? -40.750 -49.131 22.096  1.00 28.65 ? 337 GLU B C   1 
ATOM   6395 O  O   . GLU B 1 337 ? -39.637 -48.612 21.973  1.00 28.60 ? 337 GLU B O   1 
ATOM   6396 C  CB  . GLU B 1 337 ? -42.262 -49.436 20.012  1.00 34.57 ? 337 GLU B CB  1 
ATOM   6397 C  CG  . GLU B 1 337 ? -41.137 -49.567 18.974  1.00 39.24 ? 337 GLU B CG  1 
ATOM   6398 C  CD  . GLU B 1 337 ? -41.277 -50.674 17.925  1.00 44.11 ? 337 GLU B CD  1 
ATOM   6399 O  OE1 . GLU B 1 337 ? -42.418 -51.066 17.646  1.00 43.64 ? 337 GLU B OE1 1 
ATOM   6400 O  OE2 . GLU B 1 337 ? -40.238 -51.159 17.387  1.00 47.36 ? 337 GLU B OE2 1 
ATOM   6401 N  N   . ASP B 1 338 ? -40.998 -50.114 22.959  1.00 27.29 ? 338 ASP B N   1 
ATOM   6402 C  CA  . ASP B 1 338 ? -39.926 -50.986 23.499  1.00 26.04 ? 338 ASP B CA  1 
ATOM   6403 C  C   . ASP B 1 338 ? -39.175 -51.583 22.302  1.00 27.17 ? 338 ASP B C   1 
ATOM   6404 O  O   . ASP B 1 338 ? -39.816 -51.932 21.307  1.00 30.96 ? 338 ASP B O   1 
ATOM   6405 C  CB  . ASP B 1 338 ? -40.451 -52.158 24.331  1.00 25.96 ? 338 ASP B CB  1 
ATOM   6406 C  CG  . ASP B 1 338 ? -41.145 -51.849 25.646  1.00 27.74 ? 338 ASP B CG  1 
ATOM   6407 O  OD1 . ASP B 1 338 ? -41.378 -50.648 25.984  1.00 26.82 ? 338 ASP B OD1 1 
ATOM   6408 O  OD2 . ASP B 1 338 ? -41.496 -52.839 26.318  1.00 30.66 ? 338 ASP B OD2 1 
ATOM   6409 N  N   . THR B 1 339 ? -37.861 -51.722 22.398  1.00 26.17 ? 339 THR B N   1 
ATOM   6410 C  CA  . THR B 1 339 ? -36.986 -52.194 21.297  1.00 27.46 ? 339 THR B CA  1 
ATOM   6411 C  C   . THR B 1 339 ? -35.656 -52.560 21.962  1.00 27.52 ? 339 THR B C   1 
ATOM   6412 O  O   . THR B 1 339 ? -35.579 -52.458 23.187  1.00 28.03 ? 339 THR B O   1 
ATOM   6413 C  CB  . THR B 1 339 ? -36.920 -51.146 20.163  1.00 27.60 ? 339 THR B CB  1 
ATOM   6414 O  OG1 . THR B 1 339 ? -36.254 -51.620 18.992  1.00 29.17 ? 339 THR B OG1 1 
ATOM   6415 C  CG2 . THR B 1 339 ? -36.217 -49.869 20.564  1.00 25.69 ? 339 THR B CG2 1 
ATOM   6416 N  N   . VAL B 1 340 ? -34.658 -52.937 21.175  1.00 28.16 ? 340 VAL B N   1 
ATOM   6417 C  CA  . VAL B 1 340 ? -33.325 -53.384 21.650  1.00 30.64 ? 340 VAL B CA  1 
ATOM   6418 C  C   . VAL B 1 340 ? -32.302 -52.684 20.764  1.00 33.21 ? 340 VAL B C   1 
ATOM   6419 O  O   . VAL B 1 340 ? -32.389 -52.836 19.523  1.00 36.17 ? 340 VAL B O   1 
ATOM   6420 C  CB  . VAL B 1 340 ? -33.184 -54.913 21.548  1.00 32.20 ? 340 VAL B CB  1 
ATOM   6421 C  CG1 . VAL B 1 340 ? -31.855 -55.368 22.098  1.00 32.83 ? 340 VAL B CG1 1 
ATOM   6422 C  CG2 . VAL B 1 340 ? -34.344 -55.655 22.213  1.00 32.11 ? 340 VAL B CG2 1 
ATOM   6423 N  N   . LEU B 1 341 ? -31.392 -51.919 21.352  1.00 31.65 ? 341 LEU B N   1 
ATOM   6424 C  CA  . LEU B 1 341 ? -30.395 -51.174 20.558  1.00 31.43 ? 341 LEU B CA  1 
ATOM   6425 C  C   . LEU B 1 341 ? -29.203 -52.104 20.358  1.00 30.27 ? 341 LEU B C   1 
ATOM   6426 O  O   . LEU B 1 341 ? -28.807 -52.736 21.341  1.00 30.44 ? 341 LEU B O   1 
ATOM   6427 C  CB  . LEU B 1 341 ? -30.051 -49.887 21.310  1.00 31.58 ? 341 LEU B CB  1 
ATOM   6428 C  CG  . LEU B 1 341 ? -29.457 -48.754 20.480  1.00 32.36 ? 341 LEU B CG  1 
ATOM   6429 C  CD1 . LEU B 1 341 ? -30.380 -48.337 19.340  1.00 31.69 ? 341 LEU B CD1 1 
ATOM   6430 C  CD2 . LEU B 1 341 ? -29.149 -47.562 21.381  1.00 35.59 ? 341 LEU B CD2 1 
ATOM   6431 N  N   . GLY B 1 342 ? -28.720 -52.246 19.123  1.00 29.27 ? 342 GLY B N   1 
ATOM   6432 C  CA  . GLY B 1 342 ? -27.451 -52.937 18.828  1.00 29.29 ? 342 GLY B CA  1 
ATOM   6433 C  C   . GLY B 1 342 ? -27.493 -54.393 19.254  1.00 30.93 ? 342 GLY B C   1 
ATOM   6434 O  O   . GLY B 1 342 ? -26.414 -54.961 19.540  1.00 29.95 ? 342 GLY B O   1 
ATOM   6435 N  N   . GLY B 1 343 ? -28.696 -54.979 19.288  1.00 31.72 ? 343 GLY B N   1 
ATOM   6436 C  CA  . GLY B 1 343 ? -28.957 -56.350 19.764  1.00 31.17 ? 343 GLY B CA  1 
ATOM   6437 C  C   . GLY B 1 343 ? -28.411 -56.614 21.161  1.00 31.96 ? 343 GLY B C   1 
ATOM   6438 O  O   . GLY B 1 343 ? -28.119 -57.794 21.455  1.00 32.93 ? 343 GLY B O   1 
ATOM   6439 N  N   . GLU B 1 344 ? -28.278 -55.582 22.004  1.00 33.78 ? 344 GLU B N   1 
ATOM   6440 C  CA  . GLU B 1 344 ? -27.633 -55.690 23.344  1.00 35.36 ? 344 GLU B CA  1 
ATOM   6441 C  C   . GLU B 1 344 ? -28.387 -54.885 24.409  1.00 33.74 ? 344 GLU B C   1 
ATOM   6442 O  O   . GLU B 1 344 ? -28.449 -55.361 25.544  1.00 33.42 ? 344 GLU B O   1 
ATOM   6443 C  CB  . GLU B 1 344 ? -26.189 -55.194 23.292  1.00 38.30 ? 344 GLU B CB  1 
ATOM   6444 C  CG  . GLU B 1 344 ? -25.267 -56.014 22.405  1.00 40.84 ? 344 GLU B CG  1 
ATOM   6445 C  CD  . GLU B 1 344 ? -23.843 -55.471 22.292  1.00 43.64 ? 344 GLU B CD  1 
ATOM   6446 O  OE1 . GLU B 1 344 ? -23.675 -54.215 22.217  1.00 44.28 ? 344 GLU B OE1 1 
ATOM   6447 O  OE2 . GLU B 1 344 ? -22.898 -56.296 22.269  1.00 41.13 ? 344 GLU B OE2 1 
ATOM   6448 N  N   . TYR B 1 345 ? -28.911 -53.703 24.080  1.00 31.90 ? 345 TYR B N   1 
ATOM   6449 C  CA  . TYR B 1 345 ? -29.393 -52.725 25.083  1.00 32.02 ? 345 TYR B CA  1 
ATOM   6450 C  C   . TYR B 1 345 ? -30.898 -52.578 24.954  1.00 34.92 ? 345 TYR B C   1 
ATOM   6451 O  O   . TYR B 1 345 ? -31.400 -51.840 24.110  1.00 35.96 ? 345 TYR B O   1 
ATOM   6452 C  CB  . TYR B 1 345 ? -28.635 -51.408 24.966  1.00 30.84 ? 345 TYR B CB  1 
ATOM   6453 C  CG  . TYR B 1 345 ? -27.144 -51.576 25.094  1.00 31.58 ? 345 TYR B CG  1 
ATOM   6454 C  CD1 . TYR B 1 345 ? -26.546 -51.798 26.330  1.00 32.07 ? 345 TYR B CD1 1 
ATOM   6455 C  CD2 . TYR B 1 345 ? -26.340 -51.588 23.965  1.00 29.76 ? 345 TYR B CD2 1 
ATOM   6456 C  CE1 . TYR B 1 345 ? -25.170 -51.947 26.442  1.00 32.65 ? 345 TYR B CE1 1 
ATOM   6457 C  CE2 . TYR B 1 345 ? -24.971 -51.762 24.061  1.00 31.30 ? 345 TYR B CE2 1 
ATOM   6458 C  CZ  . TYR B 1 345 ? -24.385 -51.928 25.300  1.00 30.83 ? 345 TYR B CZ  1 
ATOM   6459 O  OH  . TYR B 1 345 ? -23.040 -52.076 25.354  1.00 30.68 ? 345 TYR B OH  1 
ATOM   6460 N  N   . PRO B 1 346 ? -31.655 -53.302 25.802  1.00 36.18 ? 346 PRO B N   1 
ATOM   6461 C  CA  . PRO B 1 346 ? -33.109 -53.178 25.810  1.00 34.80 ? 346 PRO B CA  1 
ATOM   6462 C  C   . PRO B 1 346 ? -33.537 -51.765 26.232  1.00 30.42 ? 346 PRO B C   1 
ATOM   6463 O  O   . PRO B 1 346 ? -32.941 -51.212 27.124  1.00 29.81 ? 346 PRO B O   1 
ATOM   6464 C  CB  . PRO B 1 346 ? -33.576 -54.264 26.800  1.00 37.66 ? 346 PRO B CB  1 
ATOM   6465 C  CG  . PRO B 1 346 ? -32.343 -54.579 27.652  1.00 40.32 ? 346 PRO B CG  1 
ATOM   6466 C  CD  . PRO B 1 346 ? -31.150 -54.311 26.757  1.00 37.13 ? 346 PRO B CD  1 
ATOM   6467 N  N   . LEU B 1 347 ? -34.563 -51.232 25.566  1.00 27.29 ? 347 LEU B N   1 
ATOM   6468 C  CA  . LEU B 1 347 ? -35.122 -49.880 25.796  1.00 25.17 ? 347 LEU B CA  1 
ATOM   6469 C  C   . LEU B 1 347 ? -36.626 -50.014 26.041  1.00 25.24 ? 347 LEU B C   1 
ATOM   6470 O  O   . LEU B 1 347 ? -37.260 -50.902 25.411  1.00 24.44 ? 347 LEU B O   1 
ATOM   6471 C  CB  . LEU B 1 347 ? -34.834 -49.031 24.554  1.00 24.13 ? 347 LEU B CB  1 
ATOM   6472 C  CG  . LEU B 1 347 ? -33.362 -48.701 24.324  1.00 23.15 ? 347 LEU B CG  1 
ATOM   6473 C  CD1 . LEU B 1 347 ? -33.150 -48.017 22.991  1.00 22.41 ? 347 LEU B CD1 1 
ATOM   6474 C  CD2 . LEU B 1 347 ? -32.833 -47.830 25.441  1.00 23.39 ? 347 LEU B CD2 1 
ATOM   6475 N  N   . GLU B 1 348 ? -37.162 -49.165 26.917  1.00 24.80 ? 348 GLU B N   1 
ATOM   6476 C  CA  . GLU B 1 348 ? -38.614 -48.971 27.145  1.00 26.48 ? 348 GLU B CA  1 
ATOM   6477 C  C   . GLU B 1 348 ? -39.136 -47.832 26.236  1.00 28.61 ? 348 GLU B C   1 
ATOM   6478 O  O   . GLU B 1 348 ? -38.375 -46.876 25.927  1.00 28.28 ? 348 GLU B O   1 
ATOM   6479 C  CB  . GLU B 1 348 ? -38.887 -48.604 28.604  1.00 28.34 ? 348 GLU B CB  1 
ATOM   6480 C  CG  . GLU B 1 348 ? -38.640 -49.691 29.636  1.00 31.53 ? 348 GLU B CG  1 
ATOM   6481 C  CD  . GLU B 1 348 ? -39.293 -49.300 30.960  1.00 35.61 ? 348 GLU B CD  1 
ATOM   6482 O  OE1 . GLU B 1 348 ? -38.688 -48.486 31.724  1.00 34.50 ? 348 GLU B OE1 1 
ATOM   6483 O  OE2 . GLU B 1 348 ? -40.456 -49.730 31.179  1.00 38.37 ? 348 GLU B OE2 1 
ATOM   6484 N  N   . LYS B 1 349 ? -40.406 -47.914 25.829  1.00 27.44 ? 349 LYS B N   1 
ATOM   6485 C  CA  . LYS B 1 349 ? -41.153 -46.789 25.231  1.00 27.06 ? 349 LYS B CA  1 
ATOM   6486 C  C   . LYS B 1 349 ? -40.870 -45.530 26.052  1.00 25.38 ? 349 LYS B C   1 
ATOM   6487 O  O   . LYS B 1 349 ? -41.090 -45.586 27.262  1.00 25.21 ? 349 LYS B O   1 
ATOM   6488 C  CB  . LYS B 1 349 ? -42.641 -47.117 25.239  1.00 28.40 ? 349 LYS B CB  1 
ATOM   6489 C  CG  . LYS B 1 349 ? -43.492 -46.095 24.518  1.00 29.40 ? 349 LYS B CG  1 
ATOM   6490 C  CD  . LYS B 1 349 ? -44.844 -46.643 24.176  1.00 29.18 ? 349 LYS B CD  1 
ATOM   6491 C  CE  . LYS B 1 349 ? -45.704 -45.605 23.509  1.00 29.86 ? 349 LYS B CE  1 
ATOM   6492 N  NZ  . LYS B 1 349 ? -47.095 -46.084 23.378  1.00 33.09 ? 349 LYS B NZ  1 
ATOM   6493 N  N   . GLY B 1 350 ? -40.354 -44.471 25.415  1.00 24.06 ? 350 GLY B N   1 
ATOM   6494 C  CA  . GLY B 1 350 ? -40.166 -43.133 26.010  1.00 24.01 ? 350 GLY B CA  1 
ATOM   6495 C  C   . GLY B 1 350 ? -38.734 -42.898 26.481  1.00 23.54 ? 350 GLY B C   1 
ATOM   6496 O  O   . GLY B 1 350 ? -38.412 -41.764 26.811  1.00 22.42 ? 350 GLY B O   1 
ATOM   6497 N  N   . ASP B 1 351 ? -37.908 -43.939 26.561  1.00 23.73 ? 351 ASP B N   1 
ATOM   6498 C  CA  . ASP B 1 351 ? -36.479 -43.807 26.929  1.00 24.40 ? 351 ASP B CA  1 
ATOM   6499 C  C   . ASP B 1 351 ? -35.809 -42.796 25.990  1.00 26.73 ? 351 ASP B C   1 
ATOM   6500 O  O   . ASP B 1 351 ? -36.022 -42.881 24.739  1.00 25.78 ? 351 ASP B O   1 
ATOM   6501 C  CB  . ASP B 1 351 ? -35.761 -45.148 26.847  1.00 24.80 ? 351 ASP B CB  1 
ATOM   6502 C  CG  . ASP B 1 351 ? -36.010 -46.039 28.043  1.00 25.32 ? 351 ASP B CG  1 
ATOM   6503 O  OD1 . ASP B 1 351 ? -36.591 -45.561 29.036  1.00 25.85 ? 351 ASP B OD1 1 
ATOM   6504 O  OD2 . ASP B 1 351 ? -35.587 -47.187 27.980  1.00 27.69 ? 351 ASP B OD2 1 
ATOM   6505 N  N   . GLU B 1 352 ? -35.030 -41.874 26.571  1.00 27.69 ? 352 GLU B N   1 
ATOM   6506 C  CA  . GLU B 1 352 ? -34.393 -40.755 25.838  1.00 26.42 ? 352 GLU B CA  1 
ATOM   6507 C  C   . GLU B 1 352 ? -32.921 -41.105 25.607  1.00 24.81 ? 352 GLU B C   1 
ATOM   6508 O  O   . GLU B 1 352 ? -32.270 -41.626 26.566  1.00 21.75 ? 352 GLU B O   1 
ATOM   6509 C  CB  . GLU B 1 352 ? -34.522 -39.443 26.602  1.00 29.48 ? 352 GLU B CB  1 
ATOM   6510 C  CG  . GLU B 1 352 ? -35.906 -39.161 27.159  1.00 30.89 ? 352 GLU B CG  1 
ATOM   6511 C  CD  . GLU B 1 352 ? -35.946 -37.970 28.107  1.00 32.47 ? 352 GLU B CD  1 
ATOM   6512 O  OE1 . GLU B 1 352 ? -36.209 -38.191 29.318  1.00 32.72 ? 352 GLU B OE1 1 
ATOM   6513 O  OE2 . GLU B 1 352 ? -35.713 -36.829 27.633  1.00 28.16 ? 352 GLU B OE2 1 
ATOM   6514 N  N   . LEU B 1 353 ? -32.475 -40.884 24.361  1.00 22.12 ? 353 LEU B N   1 
ATOM   6515 C  CA  . LEU B 1 353 ? -31.075 -40.959 23.888  1.00 22.34 ? 353 LEU B CA  1 
ATOM   6516 C  C   . LEU B 1 353 ? -30.583 -39.541 23.606  1.00 22.73 ? 353 LEU B C   1 
ATOM   6517 O  O   . LEU B 1 353 ? -31.400 -38.651 23.380  1.00 22.79 ? 353 LEU B O   1 
ATOM   6518 C  CB  . LEU B 1 353 ? -30.998 -41.789 22.607  1.00 22.77 ? 353 LEU B CB  1 
ATOM   6519 C  CG  . LEU B 1 353 ? -31.884 -43.027 22.599  1.00 25.12 ? 353 LEU B CG  1 
ATOM   6520 C  CD1 . LEU B 1 353 ? -31.840 -43.703 21.238  1.00 26.99 ? 353 LEU B CD1 1 
ATOM   6521 C  CD2 . LEU B 1 353 ? -31.457 -43.978 23.695  1.00 25.38 ? 353 LEU B CD2 1 
ATOM   6522 N  N   . MET B 1 354 ? -29.272 -39.353 23.639  1.00 23.43 ? 354 MET B N   1 
ATOM   6523 C  CA  . MET B 1 354 ? -28.604 -38.130 23.155  1.00 24.39 ? 354 MET B CA  1 
ATOM   6524 C  C   . MET B 1 354 ? -27.427 -38.577 22.281  1.00 24.25 ? 354 MET B C   1 
ATOM   6525 O  O   . MET B 1 354 ? -26.620 -39.408 22.759  1.00 25.39 ? 354 MET B O   1 
ATOM   6526 C  CB  . MET B 1 354 ? -28.130 -37.246 24.313  1.00 24.18 ? 354 MET B CB  1 
ATOM   6527 C  CG  . MET B 1 354 ? -27.581 -35.917 23.827  1.00 25.64 ? 354 MET B CG  1 
ATOM   6528 S  SD  . MET B 1 354 ? -28.850 -34.819 23.116  1.00 23.44 ? 354 MET B SD  1 
ATOM   6529 C  CE  . MET B 1 354 ? -29.135 -33.747 24.524  1.00 23.45 ? 354 MET B CE  1 
ATOM   6530 N  N   . VAL B 1 355 ? -27.413 -38.129 21.021  1.00 22.02 ? 355 VAL B N   1 
ATOM   6531 C  CA  . VAL B 1 355 ? -26.297 -38.333 20.054  1.00 19.53 ? 355 VAL B CA  1 
ATOM   6532 C  C   . VAL B 1 355 ? -25.241 -37.250 20.321  1.00 19.22 ? 355 VAL B C   1 
ATOM   6533 O  O   . VAL B 1 355 ? -25.535 -36.069 20.167  1.00 17.10 ? 355 VAL B O   1 
ATOM   6534 C  CB  . VAL B 1 355 ? -26.761 -38.303 18.586  1.00 18.26 ? 355 VAL B CB  1 
ATOM   6535 C  CG1 . VAL B 1 355 ? -25.601 -38.594 17.654  1.00 17.47 ? 355 VAL B CG1 1 
ATOM   6536 C  CG2 . VAL B 1 355 ? -27.927 -39.252 18.320  1.00 19.38 ? 355 VAL B CG2 1 
ATOM   6537 N  N   . LEU B 1 356 ? -24.047 -37.683 20.710  1.00 20.55 ? 356 LEU B N   1 
ATOM   6538 C  CA  . LEU B 1 356 ? -22.831 -36.845 20.823  1.00 22.35 ? 356 LEU B CA  1 
ATOM   6539 C  C   . LEU B 1 356 ? -22.158 -36.734 19.459  1.00 20.40 ? 356 LEU B C   1 
ATOM   6540 O  O   . LEU B 1 356 ? -21.348 -37.594 19.132  1.00 19.70 ? 356 LEU B O   1 
ATOM   6541 C  CB  . LEU B 1 356 ? -21.892 -37.510 21.829  1.00 25.53 ? 356 LEU B CB  1 
ATOM   6542 C  CG  . LEU B 1 356 ? -22.098 -37.092 23.277  1.00 31.29 ? 356 LEU B CG  1 
ATOM   6543 C  CD1 . LEU B 1 356 ? -21.060 -37.765 24.165  1.00 34.75 ? 356 LEU B CD1 1 
ATOM   6544 C  CD2 . LEU B 1 356 ? -22.038 -35.568 23.419  1.00 33.18 ? 356 LEU B CD2 1 
ATOM   6545 N  N   . ILE B 1 357 ? -22.438 -35.685 18.705  1.00 19.52 ? 357 ILE B N   1 
ATOM   6546 C  CA  . ILE B 1 357 ? -22.020 -35.637 17.277  1.00 18.91 ? 357 ILE B CA  1 
ATOM   6547 C  C   . ILE B 1 357 ? -20.487 -35.609 17.174  1.00 18.78 ? 357 ILE B C   1 
ATOM   6548 O  O   . ILE B 1 357 ? -19.916 -36.221 16.259  1.00 17.88 ? 357 ILE B O   1 
ATOM   6549 C  CB  . ILE B 1 357 ? -22.698 -34.465 16.546  1.00 18.77 ? 357 ILE B CB  1 
ATOM   6550 C  CG1 . ILE B 1 357 ? -24.220 -34.452 16.758  1.00 19.44 ? 357 ILE B CG1 1 
ATOM   6551 C  CG2 . ILE B 1 357 ? -22.333 -34.548 15.078  1.00 19.55 ? 357 ILE B CG2 1 
ATOM   6552 C  CD1 . ILE B 1 357 ? -24.924 -33.234 16.233  1.00 18.73 ? 357 ILE B CD1 1 
ATOM   6553 N  N   . PRO B 1 358 ? -19.763 -34.858 18.041  1.00 18.08 ? 358 PRO B N   1 
ATOM   6554 C  CA  . PRO B 1 358 ? -18.305 -34.817 17.973  1.00 19.03 ? 358 PRO B CA  1 
ATOM   6555 C  C   . PRO B 1 358 ? -17.692 -36.213 18.109  1.00 20.05 ? 358 PRO B C   1 
ATOM   6556 O  O   . PRO B 1 358 ? -16.697 -36.426 17.468  1.00 22.90 ? 358 PRO B O   1 
ATOM   6557 C  CB  . PRO B 1 358 ? -17.895 -33.887 19.128  1.00 18.83 ? 358 PRO B CB  1 
ATOM   6558 C  CG  . PRO B 1 358 ? -19.088 -32.975 19.278  1.00 18.81 ? 358 PRO B CG  1 
ATOM   6559 C  CD  . PRO B 1 358 ? -20.277 -33.892 19.021  1.00 18.86 ? 358 PRO B CD  1 
ATOM   6560 N  N   . GLN B 1 359 ? -18.331 -37.120 18.860  1.00 20.43 ? 359 GLN B N   1 
ATOM   6561 C  CA  . GLN B 1 359 ? -17.815 -38.491 19.106  1.00 21.44 ? 359 GLN B CA  1 
ATOM   6562 C  C   . GLN B 1 359 ? -18.065 -39.395 17.889  1.00 22.28 ? 359 GLN B C   1 
ATOM   6563 O  O   . GLN B 1 359 ? -17.125 -40.134 17.482  1.00 25.27 ? 359 GLN B O   1 
ATOM   6564 C  CB  . GLN B 1 359 ? -18.425 -39.047 20.389  1.00 21.74 ? 359 GLN B CB  1 
ATOM   6565 C  CG  . GLN B 1 359 ? -17.892 -38.364 21.636  1.00 21.55 ? 359 GLN B CG  1 
ATOM   6566 C  CD  . GLN B 1 359 ? -16.379 -38.390 21.721  1.00 21.71 ? 359 GLN B CD  1 
ATOM   6567 O  OE1 . GLN B 1 359 ? -15.711 -37.353 21.752  1.00 21.26 ? 359 GLN B OE1 1 
ATOM   6568 N  NE2 . GLN B 1 359 ? -15.818 -39.584 21.792  1.00 22.41 ? 359 GLN B NE2 1 
ATOM   6569 N  N   . LEU B 1 360 ? -19.259 -39.330 17.312  1.00 21.51 ? 360 LEU B N   1 
ATOM   6570 C  CA  . LEU B 1 360 ? -19.646 -40.071 16.079  1.00 21.96 ? 360 LEU B CA  1 
ATOM   6571 C  C   . LEU B 1 360 ? -18.685 -39.729 14.943  1.00 21.24 ? 360 LEU B C   1 
ATOM   6572 O  O   . LEU B 1 360 ? -18.327 -40.608 14.144  1.00 22.87 ? 360 LEU B O   1 
ATOM   6573 C  CB  . LEU B 1 360 ? -21.075 -39.650 15.726  1.00 22.35 ? 360 LEU B CB  1 
ATOM   6574 C  CG  . LEU B 1 360 ? -21.585 -40.104 14.366  1.00 22.64 ? 360 LEU B CG  1 
ATOM   6575 C  CD1 . LEU B 1 360 ? -21.817 -41.595 14.384  1.00 22.66 ? 360 LEU B CD1 1 
ATOM   6576 C  CD2 . LEU B 1 360 ? -22.862 -39.356 14.000  1.00 23.33 ? 360 LEU B CD2 1 
ATOM   6577 N  N   . HIS B 1 361 ? -18.363 -38.451 14.832  1.00 21.37 ? 361 HIS B N   1 
ATOM   6578 C  CA  . HIS B 1 361 ? -17.472 -37.900 13.789  1.00 20.40 ? 361 HIS B CA  1 
ATOM   6579 C  C   . HIS B 1 361 ? -16.028 -38.365 14.039  1.00 20.75 ? 361 HIS B C   1 
ATOM   6580 O  O   . HIS B 1 361 ? -15.205 -38.237 13.124  1.00 19.65 ? 361 HIS B O   1 
ATOM   6581 C  CB  . HIS B 1 361 ? -17.667 -36.387 13.776  1.00 20.81 ? 361 HIS B CB  1 
ATOM   6582 C  CG  . HIS B 1 361 ? -18.993 -35.983 13.233  1.00 20.19 ? 361 HIS B CG  1 
ATOM   6583 N  ND1 . HIS B 1 361 ? -19.337 -34.657 13.040  1.00 19.40 ? 361 HIS B ND1 1 
ATOM   6584 C  CD2 . HIS B 1 361 ? -20.044 -36.721 12.790  1.00 20.83 ? 361 HIS B CD2 1 
ATOM   6585 C  CE1 . HIS B 1 361 ? -20.548 -34.602 12.486  1.00 20.33 ? 361 HIS B CE1 1 
ATOM   6586 N  NE2 . HIS B 1 361 ? -21.008 -35.860 12.334  1.00 19.12 ? 361 HIS B NE2 1 
ATOM   6587 N  N   . ARG B 1 362 ? -15.726 -38.926 15.217  1.00 21.81 ? 362 ARG B N   1 
ATOM   6588 C  CA  . ARG B 1 362 ? -14.372 -39.477 15.511  1.00 21.52 ? 362 ARG B CA  1 
ATOM   6589 C  C   . ARG B 1 362 ? -14.399 -41.013 15.633  1.00 21.89 ? 362 ARG B C   1 
ATOM   6590 O  O   . ARG B 1 362 ? -13.383 -41.576 16.083  1.00 21.17 ? 362 ARG B O   1 
ATOM   6591 C  CB  . ARG B 1 362 ? -13.798 -38.814 16.767  1.00 21.44 ? 362 ARG B CB  1 
ATOM   6592 C  CG  . ARG B 1 362 ? -13.541 -37.318 16.639  1.00 20.79 ? 362 ARG B CG  1 
ATOM   6593 C  CD  . ARG B 1 362 ? -13.353 -36.667 18.017  1.00 20.69 ? 362 ARG B CD  1 
ATOM   6594 N  NE  . ARG B 1 362 ? -12.759 -35.348 17.901  1.00 20.31 ? 362 ARG B NE  1 
ATOM   6595 C  CZ  . ARG B 1 362 ? -13.422 -34.254 17.535  1.00 20.81 ? 362 ARG B CZ  1 
ATOM   6596 N  NH1 . ARG B 1 362 ? -14.723 -34.306 17.265  1.00 20.04 ? 362 ARG B NH1 1 
ATOM   6597 N  NH2 . ARG B 1 362 ? -12.770 -33.110 17.436  1.00 21.39 ? 362 ARG B NH2 1 
ATOM   6598 N  N   . ASP B 1 363 ? -15.466 -41.685 15.168  1.00 23.92 ? 363 ASP B N   1 
ATOM   6599 C  CA  . ASP B 1 363 ? -15.567 -43.176 15.144  1.00 24.33 ? 363 ASP B CA  1 
ATOM   6600 C  C   . ASP B 1 363 ? -14.492 -43.710 14.174  1.00 26.21 ? 363 ASP B C   1 
ATOM   6601 O  O   . ASP B 1 363 ? -14.649 -43.476 12.928  1.00 23.42 ? 363 ASP B O   1 
ATOM   6602 C  CB  . ASP B 1 363 ? -16.998 -43.622 14.816  1.00 23.26 ? 363 ASP B CB  1 
ATOM   6603 C  CG  . ASP B 1 363 ? -17.273 -45.105 15.013  1.00 25.53 ? 363 ASP B CG  1 
ATOM   6604 O  OD1 . ASP B 1 363 ? -16.355 -45.935 14.726  1.00 27.62 ? 363 ASP B OD1 1 
ATOM   6605 O  OD2 . ASP B 1 363 ? -18.410 -45.441 15.453  1.00 24.06 ? 363 ASP B OD2 1 
ATOM   6606 N  N   . LYS B 1 364 ? -13.412 -44.312 14.717  1.00 25.21 ? 364 LYS B N   1 
ATOM   6607 C  CA  . LYS B 1 364 ? -12.206 -44.725 13.939  1.00 26.73 ? 364 LYS B CA  1 
ATOM   6608 C  C   . LYS B 1 364 ? -12.566 -45.856 12.980  1.00 25.65 ? 364 LYS B C   1 
ATOM   6609 O  O   . LYS B 1 364 ? -11.900 -45.952 11.940  1.00 23.15 ? 364 LYS B O   1 
ATOM   6610 C  CB  . LYS B 1 364 ? -11.090 -45.334 14.787  1.00 29.80 ? 364 LYS B CB  1 
ATOM   6611 C  CG  . LYS B 1 364 ? -9.934  -44.427 15.175  1.00 32.87 ? 364 LYS B CG  1 
ATOM   6612 C  CD  . LYS B 1 364 ? -9.999  -43.922 16.621  1.00 34.92 ? 364 LYS B CD  1 
ATOM   6613 C  CE  . LYS B 1 364 ? -8.715  -44.126 17.399  1.00 35.53 ? 364 LYS B CE  1 
ATOM   6614 N  NZ  . LYS B 1 364 ? -7.535  -43.587 16.684  1.00 35.24 ? 364 LYS B NZ  1 
ATOM   6615 N  N   . THR B 1 365 ? -13.554 -46.684 13.346  1.00 25.08 ? 365 THR B N   1 
ATOM   6616 C  CA  . THR B 1 365 ? -14.011 -47.839 12.532  1.00 26.15 ? 365 THR B CA  1 
ATOM   6617 C  C   . THR B 1 365 ? -14.619 -47.316 11.235  1.00 25.65 ? 365 THR B C   1 
ATOM   6618 O  O   . THR B 1 365 ? -14.632 -48.059 10.244  1.00 24.03 ? 365 THR B O   1 
ATOM   6619 C  CB  . THR B 1 365 ? -15.038 -48.708 13.249  1.00 26.47 ? 365 THR B CB  1 
ATOM   6620 O  OG1 . THR B 1 365 ? -16.228 -47.922 13.348  1.00 30.32 ? 365 THR B OG1 1 
ATOM   6621 C  CG2 . THR B 1 365 ? -14.528 -49.180 14.592  1.00 26.19 ? 365 THR B CG2 1 
ATOM   6622 N  N   . ILE B 1 366 ? -15.085 -46.071 11.261  1.00 25.79 ? 366 ILE B N   1 
ATOM   6623 C  CA  . ILE B 1 366 ? -15.712 -45.400 10.092  1.00 25.17 ? 366 ILE B CA  1 
ATOM   6624 C  C   . ILE B 1 366 ? -14.629 -44.625 9.360   1.00 25.38 ? 366 ILE B C   1 
ATOM   6625 O  O   . ILE B 1 366 ? -14.406 -44.901 8.173   1.00 26.41 ? 366 ILE B O   1 
ATOM   6626 C  CB  . ILE B 1 366 ? -16.865 -44.483 10.535  1.00 23.70 ? 366 ILE B CB  1 
ATOM   6627 C  CG1 . ILE B 1 366 ? -17.940 -45.286 11.260  1.00 23.17 ? 366 ILE B CG1 1 
ATOM   6628 C  CG2 . ILE B 1 366 ? -17.422 -43.707 9.345   1.00 25.19 ? 366 ILE B CG2 1 
ATOM   6629 C  CD1 . ILE B 1 366 ? -18.569 -46.367 10.403  1.00 23.27 ? 366 ILE B CD1 1 
ATOM   6630 N  N   . TRP B 1 367 ? -13.992 -43.703 10.066  1.00 25.04 ? 367 TRP B N   1 
ATOM   6631 C  CA  . TRP B 1 367 ? -13.171 -42.641 9.440   1.00 26.04 ? 367 TRP B CA  1 
ATOM   6632 C  C   . TRP B 1 367 ? -11.733 -43.119 9.215   1.00 27.10 ? 367 TRP B C   1 
ATOM   6633 O  O   . TRP B 1 367 ? -11.089 -42.528 8.371   1.00 28.94 ? 367 TRP B O   1 
ATOM   6634 C  CB  . TRP B 1 367 ? -13.275 -41.351 10.274  1.00 24.79 ? 367 TRP B CB  1 
ATOM   6635 C  CG  . TRP B 1 367 ? -14.674 -40.807 10.266  1.00 24.04 ? 367 TRP B CG  1 
ATOM   6636 C  CD1 . TRP B 1 367 ? -15.600 -40.913 11.262  1.00 23.66 ? 367 TRP B CD1 1 
ATOM   6637 C  CD2 . TRP B 1 367 ? -15.349 -40.172 9.166   1.00 22.70 ? 367 TRP B CD2 1 
ATOM   6638 N  NE1 . TRP B 1 367 ? -16.791 -40.369 10.871  1.00 21.56 ? 367 TRP B NE1 1 
ATOM   6639 C  CE2 . TRP B 1 367 ? -16.669 -39.905 9.591   1.00 21.81 ? 367 TRP B CE2 1 
ATOM   6640 C  CE3 . TRP B 1 367 ? -14.974 -39.803 7.871   1.00 23.35 ? 367 TRP B CE3 1 
ATOM   6641 C  CZ2 . TRP B 1 367 ? -17.606 -39.278 8.771   1.00 22.86 ? 367 TRP B CZ2 1 
ATOM   6642 C  CZ3 . TRP B 1 367 ? -15.906 -39.184 7.060   1.00 23.84 ? 367 TRP B CZ3 1 
ATOM   6643 C  CH2 . TRP B 1 367 ? -17.205 -38.935 7.500   1.00 22.30 ? 367 TRP B CH2 1 
ATOM   6644 N  N   . GLY B 1 368 ? -11.227 -44.113 9.951   1.00 30.13 ? 368 GLY B N   1 
ATOM   6645 C  CA  . GLY B 1 368 ? -9.833  -44.577 9.788   1.00 32.56 ? 368 GLY B CA  1 
ATOM   6646 C  C   . GLY B 1 368 ? -8.869  -43.977 10.802  1.00 35.81 ? 368 GLY B C   1 
ATOM   6647 O  O   . GLY B 1 368 ? -9.322  -43.255 11.701  1.00 33.98 ? 368 GLY B O   1 
ATOM   6648 N  N   . ASP B 1 369 ? -7.575  -44.295 10.656  1.00 43.62 ? 369 ASP B N   1 
ATOM   6649 C  CA  . ASP B 1 369 ? -6.471  -43.981 11.609  1.00 47.01 ? 369 ASP B CA  1 
ATOM   6650 C  C   . ASP B 1 369 ? -6.215  -42.467 11.625  1.00 46.76 ? 369 ASP B C   1 
ATOM   6651 O  O   . ASP B 1 369 ? -5.797  -41.958 12.675  1.00 44.13 ? 369 ASP B O   1 
ATOM   6652 C  CB  . ASP B 1 369 ? -5.151  -44.670 11.232  1.00 51.40 ? 369 ASP B CB  1 
ATOM   6653 C  CG  . ASP B 1 369 ? -5.298  -46.118 10.796  1.00 60.73 ? 369 ASP B CG  1 
ATOM   6654 O  OD1 . ASP B 1 369 ? -5.917  -46.892 11.561  1.00 60.43 ? 369 ASP B OD1 1 
ATOM   6655 O  OD2 . ASP B 1 369 ? -4.812  -46.457 9.678   1.00 62.58 ? 369 ASP B OD2 1 
ATOM   6656 N  N   . ASP B 1 370 ? -6.437  -41.779 10.502  1.00 45.30 ? 370 ASP B N   1 
ATOM   6657 C  CA  . ASP B 1 370 ? -6.249  -40.308 10.383  1.00 45.02 ? 370 ASP B CA  1 
ATOM   6658 C  C   . ASP B 1 370 ? -7.504  -39.542 10.863  1.00 39.82 ? 370 ASP B C   1 
ATOM   6659 O  O   . ASP B 1 370 ? -7.712  -38.415 10.403  1.00 42.12 ? 370 ASP B O   1 
ATOM   6660 C  CB  . ASP B 1 370 ? -5.877  -39.954 8.934   1.00 46.18 ? 370 ASP B CB  1 
ATOM   6661 C  CG  . ASP B 1 370 ? -6.995  -40.190 7.928   1.00 47.39 ? 370 ASP B CG  1 
ATOM   6662 O  OD1 . ASP B 1 370 ? -8.026  -40.786 8.331   1.00 46.68 ? 370 ASP B OD1 1 
ATOM   6663 O  OD2 . ASP B 1 370 ? -6.844  -39.758 6.751   1.00 43.99 ? 370 ASP B OD2 1 
ATOM   6664 N  N   . VAL B 1 371 ? -8.328  -40.083 11.759  1.00 37.68 ? 371 VAL B N   1 
ATOM   6665 C  CA  . VAL B 1 371 ? -9.644  -39.456 12.122  1.00 37.58 ? 371 VAL B CA  1 
ATOM   6666 C  C   . VAL B 1 371 ? -9.427  -38.008 12.593  1.00 33.80 ? 371 VAL B C   1 
ATOM   6667 O  O   . VAL B 1 371 ? -10.299 -37.158 12.341  1.00 33.91 ? 371 VAL B O   1 
ATOM   6668 C  CB  . VAL B 1 371 ? -10.424 -40.271 13.182  1.00 38.32 ? 371 VAL B CB  1 
ATOM   6669 C  CG1 . VAL B 1 371 ? -9.740  -40.289 14.543  1.00 37.22 ? 371 VAL B CG1 1 
ATOM   6670 C  CG2 . VAL B 1 371 ? -11.845 -39.754 13.334  1.00 39.01 ? 371 VAL B CG2 1 
ATOM   6671 N  N   . GLU B 1 372 ? -8.328  -37.733 13.294  1.00 32.41 ? 372 GLU B N   1 
ATOM   6672 C  CA  . GLU B 1 372 ? -8.102  -36.424 13.950  1.00 30.90 ? 372 GLU B CA  1 
ATOM   6673 C  C   . GLU B 1 372 ? -7.484  -35.440 12.942  1.00 27.48 ? 372 GLU B C   1 
ATOM   6674 O  O   . GLU B 1 372 ? -7.402  -34.269 13.272  1.00 26.70 ? 372 GLU B O   1 
ATOM   6675 C  CB  . GLU B 1 372 ? -7.284  -36.617 15.230  1.00 34.11 ? 372 GLU B CB  1 
ATOM   6676 C  CG  . GLU B 1 372 ? -8.111  -37.097 16.411  1.00 37.11 ? 372 GLU B CG  1 
ATOM   6677 C  CD  . GLU B 1 372 ? -9.070  -36.084 17.028  1.00 41.81 ? 372 GLU B CD  1 
ATOM   6678 O  OE1 . GLU B 1 372 ? -8.767  -34.867 17.008  1.00 45.88 ? 372 GLU B OE1 1 
ATOM   6679 O  OE2 . GLU B 1 372 ? -10.125 -36.511 17.541  1.00 43.19 ? 372 GLU B OE2 1 
ATOM   6680 N  N   . GLU B 1 373 ? -7.131  -35.884 11.736  1.00 28.32 ? 373 GLU B N   1 
ATOM   6681 C  CA  . GLU B 1 373 ? -6.564  -35.034 10.642  1.00 30.42 ? 373 GLU B CA  1 
ATOM   6682 C  C   . GLU B 1 373 ? -7.668  -34.264 9.887   1.00 26.72 ? 373 GLU B C   1 
ATOM   6683 O  O   . GLU B 1 373 ? -8.763  -34.815 9.686   1.00 21.69 ? 373 GLU B O   1 
ATOM   6684 C  CB  . GLU B 1 373 ? -5.710  -35.895 9.702   1.00 35.16 ? 373 GLU B CB  1 
ATOM   6685 C  CG  . GLU B 1 373 ? -4.499  -36.472 10.426  1.00 42.32 ? 373 GLU B CG  1 
ATOM   6686 C  CD  . GLU B 1 373 ? -3.444  -37.139 9.561   1.00 49.97 ? 373 GLU B CD  1 
ATOM   6687 O  OE1 . GLU B 1 373 ? -3.680  -37.262 8.328   1.00 54.62 ? 373 GLU B OE1 1 
ATOM   6688 O  OE2 . GLU B 1 373 ? -2.393  -37.556 10.134  1.00 55.98 ? 373 GLU B OE2 1 
ATOM   6689 N  N   . PHE B 1 374 ? -7.393  -33.005 9.517   1.00 24.37 ? 374 PHE B N   1 
ATOM   6690 C  CA  . PHE B 1 374 ? -8.286  -32.157 8.677   1.00 22.24 ? 374 PHE B CA  1 
ATOM   6691 C  C   . PHE B 1 374 ? -8.030  -32.427 7.190   1.00 23.18 ? 374 PHE B C   1 
ATOM   6692 O  O   . PHE B 1 374 ? -7.140  -31.793 6.632   1.00 20.73 ? 374 PHE B O   1 
ATOM   6693 C  CB  . PHE B 1 374 ? -8.048  -30.670 8.914   1.00 19.47 ? 374 PHE B CB  1 
ATOM   6694 C  CG  . PHE B 1 374 ? -9.123  -29.821 8.308   1.00 18.33 ? 374 PHE B CG  1 
ATOM   6695 C  CD1 . PHE B 1 374 ? -10.326 -29.671 8.962   1.00 16.31 ? 374 PHE B CD1 1 
ATOM   6696 C  CD2 . PHE B 1 374 ? -8.941  -29.189 7.086   1.00 18.17 ? 374 PHE B CD2 1 
ATOM   6697 C  CE1 . PHE B 1 374 ? -11.334 -28.910 8.406   1.00 16.57 ? 374 PHE B CE1 1 
ATOM   6698 C  CE2 . PHE B 1 374 ? -9.955  -28.416 6.538   1.00 18.43 ? 374 PHE B CE2 1 
ATOM   6699 C  CZ  . PHE B 1 374 ? -11.158 -28.288 7.195   1.00 16.43 ? 374 PHE B CZ  1 
ATOM   6700 N  N   . ARG B 1 375 ? -8.837  -33.286 6.570   1.00 25.89 ? 375 ARG B N   1 
ATOM   6701 C  CA  . ARG B 1 375 ? -8.668  -33.748 5.170   1.00 28.28 ? 375 ARG B CA  1 
ATOM   6702 C  C   . ARG B 1 375 ? -10.020 -33.637 4.473   1.00 25.00 ? 375 ARG B C   1 
ATOM   6703 O  O   . ARG B 1 375 ? -10.817 -34.571 4.473   1.00 23.08 ? 375 ARG B O   1 
ATOM   6704 C  CB  . ARG B 1 375 ? -8.090  -35.165 5.184   1.00 35.28 ? 375 ARG B CB  1 
ATOM   6705 C  CG  . ARG B 1 375 ? -7.828  -35.711 3.789   1.00 44.75 ? 375 ARG B CG  1 
ATOM   6706 C  CD  . ARG B 1 375 ? -7.066  -37.018 3.784   1.00 52.26 ? 375 ARG B CD  1 
ATOM   6707 N  NE  . ARG B 1 375 ? -7.625  -37.964 2.813   1.00 62.84 ? 375 ARG B NE  1 
ATOM   6708 C  CZ  . ARG B 1 375 ? -8.196  -39.143 3.104   1.00 67.83 ? 375 ARG B CZ  1 
ATOM   6709 N  NH1 . ARG B 1 375 ? -8.300  -39.570 4.356   1.00 70.62 ? 375 ARG B NH1 1 
ATOM   6710 N  NH2 . ARG B 1 375 ? -8.653  -39.905 2.124   1.00 66.98 ? 375 ARG B NH2 1 
ATOM   6711 N  N   . PRO B 1 376 ? -10.345 -32.453 3.915   1.00 23.91 ? 376 PRO B N   1 
ATOM   6712 C  CA  . PRO B 1 376 ? -11.611 -32.229 3.204   1.00 23.12 ? 376 PRO B CA  1 
ATOM   6713 C  C   . PRO B 1 376 ? -11.868 -33.206 2.053   1.00 25.02 ? 376 PRO B C   1 
ATOM   6714 O  O   . PRO B 1 376 ? -13.029 -33.436 1.636   1.00 20.89 ? 376 PRO B O   1 
ATOM   6715 C  CB  . PRO B 1 376 ? -11.423 -30.838 2.585   1.00 23.49 ? 376 PRO B CB  1 
ATOM   6716 C  CG  . PRO B 1 376 ? -10.443 -30.153 3.509   1.00 23.78 ? 376 PRO B CG  1 
ATOM   6717 C  CD  . PRO B 1 376 ? -9.503  -31.245 3.974   1.00 23.18 ? 376 PRO B CD  1 
ATOM   6718 N  N   . GLU B 1 377 ? -10.765 -33.768 1.554   1.00 26.42 ? 377 GLU B N   1 
ATOM   6719 C  CA  . GLU B 1 377 ? -10.767 -34.808 0.497   1.00 27.99 ? 377 GLU B CA  1 
ATOM   6720 C  C   . GLU B 1 377 ? -11.608 -36.010 0.985   1.00 26.36 ? 377 GLU B C   1 
ATOM   6721 O  O   . GLU B 1 377 ? -12.101 -36.747 0.114   1.00 27.60 ? 377 GLU B O   1 
ATOM   6722 C  CB  . GLU B 1 377 ? -9.312  -35.094 0.087   1.00 28.25 ? 377 GLU B CB  1 
ATOM   6723 C  CG  . GLU B 1 377 ? -8.608  -33.914 -0.587  1.00 28.68 ? 377 GLU B CG  1 
ATOM   6724 C  CD  . GLU B 1 377 ? -7.925  -32.844 0.280   1.00 31.04 ? 377 GLU B CD  1 
ATOM   6725 O  OE1 . GLU B 1 377 ? -7.888  -32.986 1.547   1.00 28.44 ? 377 GLU B OE1 1 
ATOM   6726 O  OE2 . GLU B 1 377 ? -7.411  -31.841 -0.313  1.00 27.72 ? 377 GLU B OE2 1 
ATOM   6727 N  N   . ARG B 1 378 ? -11.879 -36.149 2.298   1.00 26.20 ? 378 ARG B N   1 
ATOM   6728 C  CA  . ARG B 1 378 ? -12.800 -37.206 2.845   1.00 26.65 ? 378 ARG B CA  1 
ATOM   6729 C  C   . ARG B 1 378 ? -13.983 -37.327 1.907   1.00 24.76 ? 378 ARG B C   1 
ATOM   6730 O  O   . ARG B 1 378 ? -14.572 -38.375 1.883   1.00 28.09 ? 378 ARG B O   1 
ATOM   6731 C  CB  . ARG B 1 378 ? -13.211 -37.076 4.306   1.00 24.81 ? 378 ARG B CB  1 
ATOM   6732 C  CG  . ARG B 1 378 ? -12.124 -37.583 5.226   1.00 25.37 ? 378 ARG B CG  1 
ATOM   6733 C  CD  . ARG B 1 378 ? -12.457 -37.193 6.651   1.00 26.79 ? 378 ARG B CD  1 
ATOM   6734 N  NE  . ARG B 1 378 ? -11.253 -36.782 7.344   1.00 26.00 ? 378 ARG B NE  1 
ATOM   6735 C  CZ  . ARG B 1 378 ? -10.336 -37.612 7.794   1.00 28.19 ? 378 ARG B CZ  1 
ATOM   6736 N  NH1 . ARG B 1 378 ? -10.475 -38.923 7.622   1.00 27.97 ? 378 ARG B NH1 1 
ATOM   6737 N  NH2 . ARG B 1 378 ? -9.273  -37.117 8.411   1.00 28.83 ? 378 ARG B NH2 1 
ATOM   6738 N  N   . PHE B 1 379 ? -14.497 -36.140 1.572   1.00 24.99 ? 379 PHE B N   1 
ATOM   6739 C  CA  . PHE B 1 379 ? -15.870 -35.841 1.095   1.00 24.09 ? 379 PHE B CA  1 
ATOM   6740 C  C   . PHE B 1 379 ? -15.892 -35.761 -0.431  1.00 23.16 ? 379 PHE B C   1 
ATOM   6741 O  O   . PHE B 1 379 ? -16.957 -35.377 -0.961  1.00 19.63 ? 379 PHE B O   1 
ATOM   6742 C  CB  . PHE B 1 379 ? -16.352 -34.535 1.743   1.00 24.46 ? 379 PHE B CB  1 
ATOM   6743 C  CG  . PHE B 1 379 ? -16.682 -34.671 3.206   1.00 24.02 ? 379 PHE B CG  1 
ATOM   6744 C  CD1 . PHE B 1 379 ? -17.953 -35.048 3.617   1.00 24.36 ? 379 PHE B CD1 1 
ATOM   6745 C  CD2 . PHE B 1 379 ? -15.714 -34.464 4.167   1.00 21.97 ? 379 PHE B CD2 1 
ATOM   6746 C  CE1 . PHE B 1 379 ? -18.260 -35.179 4.968   1.00 24.84 ? 379 PHE B CE1 1 
ATOM   6747 C  CE2 . PHE B 1 379 ? -16.019 -34.613 5.509   1.00 23.94 ? 379 PHE B CE2 1 
ATOM   6748 C  CZ  . PHE B 1 379 ? -17.284 -34.976 5.914   1.00 22.91 ? 379 PHE B CZ  1 
ATOM   6749 N  N   . GLU B 1 380 ? -14.780 -36.108 -1.100  1.00 24.15 ? 380 GLU B N   1 
ATOM   6750 C  CA  . GLU B 1 380 ? -14.715 -36.134 -2.588  1.00 26.96 ? 380 GLU B CA  1 
ATOM   6751 C  C   . GLU B 1 380 ? -15.787 -37.147 -2.999  1.00 23.93 ? 380 GLU B C   1 
ATOM   6752 O  O   . GLU B 1 380 ? -16.523 -36.851 -3.936  1.00 24.17 ? 380 GLU B O   1 
ATOM   6753 C  CB  . GLU B 1 380 ? -13.284 -36.370 -3.132  1.00 32.37 ? 380 GLU B CB  1 
ATOM   6754 C  CG  . GLU B 1 380 ? -12.638 -35.175 -3.901  1.00 35.29 ? 380 GLU B CG  1 
ATOM   6755 C  CD  . GLU B 1 380 ? -11.102 -34.964 -3.862  1.00 38.12 ? 380 GLU B CD  1 
ATOM   6756 O  OE1 . GLU B 1 380 ? -10.337 -35.961 -3.901  1.00 38.94 ? 380 GLU B OE1 1 
ATOM   6757 O  OE2 . GLU B 1 380 ? -10.635 -33.776 -3.821  1.00 39.62 ? 380 GLU B OE2 1 
ATOM   6758 N  N   . ASN B 1 381 ? -15.996 -38.201 -2.214  1.00 23.17 ? 381 ASN B N   1 
ATOM   6759 C  CA  . ASN B 1 381 ? -16.968 -39.273 -2.557  1.00 25.50 ? 381 ASN B CA  1 
ATOM   6760 C  C   . ASN B 1 381 ? -17.867 -39.531 -1.355  1.00 25.21 ? 381 ASN B C   1 
ATOM   6761 O  O   . ASN B 1 381 ? -17.605 -40.431 -0.578  1.00 25.70 ? 381 ASN B O   1 
ATOM   6762 C  CB  . ASN B 1 381 ? -16.278 -40.568 -3.004  1.00 26.67 ? 381 ASN B CB  1 
ATOM   6763 C  CG  . ASN B 1 381 ? -15.013 -40.337 -3.810  1.00 30.38 ? 381 ASN B CG  1 
ATOM   6764 O  OD1 . ASN B 1 381 ? -15.075 -39.918 -4.964  1.00 39.67 ? 381 ASN B OD1 1 
ATOM   6765 N  ND2 . ASN B 1 381 ? -13.851 -40.587 -3.221  1.00 28.99 ? 381 ASN B ND2 1 
ATOM   6766 N  N   . PRO B 1 382 ? -18.989 -38.803 -1.183  1.00 27.94 ? 382 PRO B N   1 
ATOM   6767 C  CA  . PRO B 1 382 ? -19.803 -38.938 0.029   1.00 30.08 ? 382 PRO B CA  1 
ATOM   6768 C  C   . PRO B 1 382 ? -20.608 -40.251 0.082   1.00 29.05 ? 382 PRO B C   1 
ATOM   6769 O  O   . PRO B 1 382 ? -21.029 -40.624 1.171   1.00 28.77 ? 382 PRO B O   1 
ATOM   6770 C  CB  . PRO B 1 382 ? -20.740 -37.718 -0.026  1.00 29.90 ? 382 PRO B CB  1 
ATOM   6771 C  CG  . PRO B 1 382 ? -20.899 -37.487 -1.523  1.00 29.44 ? 382 PRO B CG  1 
ATOM   6772 C  CD  . PRO B 1 382 ? -19.553 -37.833 -2.131  1.00 27.87 ? 382 PRO B CD  1 
ATOM   6773 N  N   . SER B 1 383 ? -20.787 -40.952 -1.045  1.00 27.31 ? 383 SER B N   1 
ATOM   6774 C  CA  . SER B 1 383 ? -21.517 -42.250 -1.069  1.00 27.61 ? 383 SER B CA  1 
ATOM   6775 C  C   . SER B 1 383 ? -20.720 -43.325 -0.310  1.00 25.52 ? 383 SER B C   1 
ATOM   6776 O  O   . SER B 1 383 ? -21.314 -44.336 0.090   1.00 26.64 ? 383 SER B O   1 
ATOM   6777 C  CB  . SER B 1 383 ? -21.805 -42.671 -2.466  1.00 30.74 ? 383 SER B CB  1 
ATOM   6778 O  OG  . SER B 1 383 ? -20.568 -42.867 -3.136  1.00 36.89 ? 383 SER B OG  1 
ATOM   6779 N  N   . ALA B 1 384 ? -19.421 -43.132 -0.101  1.00 23.44 ? 384 ALA B N   1 
ATOM   6780 C  CA  . ALA B 1 384 ? -18.600 -44.034 0.738   1.00 23.92 ? 384 ALA B CA  1 
ATOM   6781 C  C   . ALA B 1 384 ? -18.929 -43.860 2.227   1.00 24.28 ? 384 ALA B C   1 
ATOM   6782 O  O   . ALA B 1 384 ? -18.658 -44.802 2.993   1.00 25.93 ? 384 ALA B O   1 
ATOM   6783 C  CB  . ALA B 1 384 ? -17.144 -43.790 0.473   1.00 24.85 ? 384 ALA B CB  1 
ATOM   6784 N  N   . ILE B 1 385 ? -19.513 -42.733 2.647   1.00 22.98 ? 385 ILE B N   1 
ATOM   6785 C  CA  . ILE B 1 385 ? -19.883 -42.527 4.074   1.00 23.14 ? 385 ILE B CA  1 
ATOM   6786 C  C   . ILE B 1 385 ? -20.995 -43.506 4.450   1.00 22.67 ? 385 ILE B C   1 
ATOM   6787 O  O   . ILE B 1 385 ? -22.076 -43.429 3.888   1.00 23.44 ? 385 ILE B O   1 
ATOM   6788 C  CB  . ILE B 1 385 ? -20.322 -41.074 4.329   1.00 25.83 ? 385 ILE B CB  1 
ATOM   6789 C  CG1 . ILE B 1 385 ? -19.242 -40.068 3.925   1.00 28.27 ? 385 ILE B CG1 1 
ATOM   6790 C  CG2 . ILE B 1 385 ? -20.750 -40.894 5.781   1.00 23.75 ? 385 ILE B CG2 1 
ATOM   6791 C  CD1 . ILE B 1 385 ? -19.755 -38.672 3.685   1.00 29.06 ? 385 ILE B CD1 1 
ATOM   6792 N  N   . PRO B 1 386 ? -20.818 -44.391 5.460   1.00 21.81 ? 386 PRO B N   1 
ATOM   6793 C  CA  . PRO B 1 386 ? -21.882 -45.302 5.887   1.00 22.21 ? 386 PRO B CA  1 
ATOM   6794 C  C   . PRO B 1 386 ? -23.073 -44.559 6.514   1.00 21.94 ? 386 PRO B C   1 
ATOM   6795 O  O   . PRO B 1 386 ? -22.925 -43.382 6.828   1.00 20.24 ? 386 PRO B O   1 
ATOM   6796 C  CB  . PRO B 1 386 ? -21.219 -46.242 6.921   1.00 22.63 ? 386 PRO B CB  1 
ATOM   6797 C  CG  . PRO B 1 386 ? -19.712 -46.072 6.684   1.00 21.89 ? 386 PRO B CG  1 
ATOM   6798 C  CD  . PRO B 1 386 ? -19.573 -44.639 6.201   1.00 21.79 ? 386 PRO B CD  1 
ATOM   6799 N  N   . GLN B 1 387 ? -24.212 -45.256 6.636   1.00 20.41 ? 387 GLN B N   1 
ATOM   6800 C  CA  . GLN B 1 387 ? -25.505 -44.687 7.103   1.00 20.87 ? 387 GLN B CA  1 
ATOM   6801 C  C   . GLN B 1 387 ? -25.264 -43.953 8.415   1.00 21.49 ? 387 GLN B C   1 
ATOM   6802 O  O   . GLN B 1 387 ? -24.673 -44.561 9.339   1.00 19.60 ? 387 GLN B O   1 
ATOM   6803 C  CB  . GLN B 1 387 ? -26.565 -45.753 7.369   1.00 21.65 ? 387 GLN B CB  1 
ATOM   6804 C  CG  . GLN B 1 387 ? -27.273 -46.271 6.124   1.00 22.61 ? 387 GLN B CG  1 
ATOM   6805 C  CD  . GLN B 1 387 ? -28.621 -46.822 6.505   1.00 23.72 ? 387 GLN B CD  1 
ATOM   6806 O  OE1 . GLN B 1 387 ? -28.739 -47.973 6.909   1.00 26.64 ? 387 GLN B OE1 1 
ATOM   6807 N  NE2 . GLN B 1 387 ? -29.641 -45.979 6.433   1.00 25.63 ? 387 GLN B NE2 1 
ATOM   6808 N  N   . HIS B 1 388 ? -25.679 -42.691 8.474   1.00 21.22 ? 388 HIS B N   1 
ATOM   6809 C  CA  . HIS B 1 388 ? -25.710 -41.897 9.723   1.00 21.02 ? 388 HIS B CA  1 
ATOM   6810 C  C   . HIS B 1 388 ? -24.313 -41.847 10.370  1.00 19.51 ? 388 HIS B C   1 
ATOM   6811 O  O   . HIS B 1 388 ? -24.253 -41.805 11.591  1.00 19.11 ? 388 HIS B O   1 
ATOM   6812 C  CB  . HIS B 1 388 ? -26.781 -42.480 10.658  1.00 21.19 ? 388 HIS B CB  1 
ATOM   6813 C  CG  . HIS B 1 388 ? -28.122 -42.666 10.030  1.00 22.02 ? 388 HIS B CG  1 
ATOM   6814 N  ND1 . HIS B 1 388 ? -28.818 -41.623 9.422   1.00 21.71 ? 388 HIS B ND1 1 
ATOM   6815 C  CD2 . HIS B 1 388 ? -28.916 -43.755 9.941   1.00 22.86 ? 388 HIS B CD2 1 
ATOM   6816 C  CE1 . HIS B 1 388 ? -29.966 -42.071 8.963   1.00 21.78 ? 388 HIS B CE1 1 
ATOM   6817 N  NE2 . HIS B 1 388 ? -30.050 -43.385 9.261   1.00 22.85 ? 388 HIS B NE2 1 
ATOM   6818 N  N   . ALA B 1 389 ? -23.234 -41.826 9.581   1.00 18.24 ? 389 ALA B N   1 
ATOM   6819 C  CA  . ALA B 1 389 ? -21.853 -41.570 10.055  1.00 17.69 ? 389 ALA B CA  1 
ATOM   6820 C  C   . ALA B 1 389 ? -21.589 -40.071 10.235  1.00 17.71 ? 389 ALA B C   1 
ATOM   6821 O  O   . ALA B 1 389 ? -20.616 -39.752 10.959  1.00 19.74 ? 389 ALA B O   1 
ATOM   6822 C  CB  . ALA B 1 389 ? -20.845 -42.133 9.103   1.00 17.10 ? 389 ALA B CB  1 
ATOM   6823 N  N   . PHE B 1 390 ? -22.362 -39.213 9.564   1.00 16.04 ? 390 PHE B N   1 
ATOM   6824 C  CA  . PHE B 1 390 ? -22.138 -37.754 9.445   1.00 15.74 ? 390 PHE B CA  1 
ATOM   6825 C  C   . PHE B 1 390 ? -23.480 -37.052 9.606   1.00 15.71 ? 390 PHE B C   1 
ATOM   6826 O  O   . PHE B 1 390 ? -24.261 -37.142 8.705   1.00 16.85 ? 390 PHE B O   1 
ATOM   6827 C  CB  . PHE B 1 390 ? -21.513 -37.453 8.080   1.00 16.27 ? 390 PHE B CB  1 
ATOM   6828 C  CG  . PHE B 1 390 ? -21.114 -36.016 7.850   1.00 16.19 ? 390 PHE B CG  1 
ATOM   6829 C  CD1 . PHE B 1 390 ? -20.074 -35.439 8.565   1.00 16.24 ? 390 PHE B CD1 1 
ATOM   6830 C  CD2 . PHE B 1 390 ? -21.749 -35.248 6.886   1.00 16.65 ? 390 PHE B CD2 1 
ATOM   6831 C  CE1 . PHE B 1 390 ? -19.688 -34.130 8.319   1.00 16.85 ? 390 PHE B CE1 1 
ATOM   6832 C  CE2 . PHE B 1 390 ? -21.375 -33.931 6.661   1.00 17.48 ? 390 PHE B CE2 1 
ATOM   6833 C  CZ  . PHE B 1 390 ? -20.340 -33.375 7.377   1.00 16.82 ? 390 PHE B CZ  1 
ATOM   6834 N  N   . LYS B 1 391 ? -23.734 -36.449 10.761  1.00 17.36 ? 391 LYS B N   1 
ATOM   6835 C  CA  . LYS B 1 391 ? -25.066 -35.981 11.224  1.00 18.26 ? 391 LYS B CA  1 
ATOM   6836 C  C   . LYS B 1 391 ? -24.975 -34.578 11.805  1.00 18.39 ? 391 LYS B C   1 
ATOM   6837 O  O   . LYS B 1 391 ? -25.565 -34.333 12.853  1.00 21.65 ? 391 LYS B O   1 
ATOM   6838 C  CB  . LYS B 1 391 ? -25.580 -36.909 12.327  1.00 18.89 ? 391 LYS B CB  1 
ATOM   6839 C  CG  . LYS B 1 391 ? -25.771 -38.355 11.906  1.00 20.06 ? 391 LYS B CG  1 
ATOM   6840 C  CD  . LYS B 1 391 ? -26.494 -38.493 10.554  1.00 21.98 ? 391 LYS B CD  1 
ATOM   6841 C  CE  . LYS B 1 391 ? -27.980 -38.772 10.641  1.00 22.48 ? 391 LYS B CE  1 
ATOM   6842 N  NZ  . LYS B 1 391 ? -28.633 -38.692 9.304   1.00 23.56 ? 391 LYS B NZ  1 
ATOM   6843 N  N   . PRO B 1 392 ? -24.274 -33.616 11.159  1.00 17.84 ? 392 PRO B N   1 
ATOM   6844 C  CA  . PRO B 1 392 ? -24.108 -32.293 11.746  1.00 17.59 ? 392 PRO B CA  1 
ATOM   6845 C  C   . PRO B 1 392 ? -25.395 -31.457 11.631  1.00 18.19 ? 392 PRO B C   1 
ATOM   6846 O  O   . PRO B 1 392 ? -25.432 -30.445 12.291  1.00 20.43 ? 392 PRO B O   1 
ATOM   6847 C  CB  . PRO B 1 392 ? -22.918 -31.743 10.934  1.00 17.47 ? 392 PRO B CB  1 
ATOM   6848 C  CG  . PRO B 1 392 ? -23.118 -32.338 9.546   1.00 16.80 ? 392 PRO B CG  1 
ATOM   6849 C  CD  . PRO B 1 392 ? -23.646 -33.719 9.824   1.00 17.58 ? 392 PRO B CD  1 
ATOM   6850 N  N   . PHE B 1 393 ? -26.382 -31.869 10.810  1.00 17.36 ? 393 PHE B N   1 
ATOM   6851 C  CA  . PHE B 1 393 ? -27.708 -31.204 10.658  1.00 17.67 ? 393 PHE B CA  1 
ATOM   6852 C  C   . PHE B 1 393 ? -28.803 -32.124 11.222  1.00 17.24 ? 393 PHE B C   1 
ATOM   6853 O  O   . PHE B 1 393 ? -29.992 -31.958 10.909  1.00 17.81 ? 393 PHE B O   1 
ATOM   6854 C  CB  . PHE B 1 393 ? -27.950 -30.779 9.201   1.00 17.48 ? 393 PHE B CB  1 
ATOM   6855 C  CG  . PHE B 1 393 ? -27.030 -29.680 8.720   1.00 17.40 ? 393 PHE B CG  1 
ATOM   6856 C  CD1 . PHE B 1 393 ? -27.191 -28.375 9.149   1.00 18.41 ? 393 PHE B CD1 1 
ATOM   6857 C  CD2 . PHE B 1 393 ? -25.965 -29.957 7.885   1.00 17.89 ? 393 PHE B CD2 1 
ATOM   6858 C  CE1 . PHE B 1 393 ? -26.333 -27.366 8.728   1.00 18.40 ? 393 PHE B CE1 1 
ATOM   6859 C  CE2 . PHE B 1 393 ? -25.118 -28.948 7.443   1.00 17.88 ? 393 PHE B CE2 1 
ATOM   6860 C  CZ  . PHE B 1 393 ? -25.314 -27.651 7.853   1.00 17.57 ? 393 PHE B CZ  1 
ATOM   6861 N  N   . GLY B 1 394 ? -28.425 -33.084 12.057  1.00 17.32 ? 394 GLY B N   1 
ATOM   6862 C  CA  . GLY B 1 394 ? -29.389 -34.012 12.675  1.00 17.61 ? 394 GLY B CA  1 
ATOM   6863 C  C   . GLY B 1 394 ? -29.934 -35.001 11.666  1.00 17.36 ? 394 GLY B C   1 
ATOM   6864 O  O   . GLY B 1 394 ? -29.195 -35.378 10.728  1.00 16.84 ? 394 GLY B O   1 
ATOM   6865 N  N   . ASN B 1 395 ? -31.187 -35.425 11.844  1.00 18.41 ? 395 ASN B N   1 
ATOM   6866 C  CA  . ASN B 1 395 ? -31.671 -36.674 11.208  1.00 19.10 ? 395 ASN B CA  1 
ATOM   6867 C  C   . ASN B 1 395 ? -33.154 -36.638 10.817  1.00 19.46 ? 395 ASN B C   1 
ATOM   6868 O  O   . ASN B 1 395 ? -34.019 -36.177 11.655  1.00 18.47 ? 395 ASN B O   1 
ATOM   6869 C  CB  . ASN B 1 395 ? -31.454 -37.858 12.129  1.00 19.93 ? 395 ASN B CB  1 
ATOM   6870 C  CG  . ASN B 1 395 ? -31.790 -39.135 11.406  1.00 20.75 ? 395 ASN B CG  1 
ATOM   6871 O  OD1 . ASN B 1 395 ? -31.062 -39.510 10.487  1.00 22.72 ? 395 ASN B OD1 1 
ATOM   6872 N  ND2 . ASN B 1 395 ? -32.889 -39.770 11.797  1.00 19.48 ? 395 ASN B ND2 1 
ATOM   6873 N  N   . GLY B 1 396 ? -33.411 -37.123 9.589   1.00 18.76 ? 396 GLY B N   1 
ATOM   6874 C  CA  . GLY B 1 396 ? -34.734 -37.443 9.019   1.00 18.56 ? 396 GLY B CA  1 
ATOM   6875 C  C   . GLY B 1 396 ? -35.641 -36.234 8.928   1.00 18.18 ? 396 GLY B C   1 
ATOM   6876 O  O   . GLY B 1 396 ? -35.157 -35.163 8.571   1.00 19.24 ? 396 GLY B O   1 
ATOM   6877 N  N   . GLN B 1 397 ? -36.922 -36.399 9.250   1.00 18.34 ? 397 GLN B N   1 
ATOM   6878 C  CA  . GLN B 1 397 ? -37.946 -35.330 9.104   1.00 18.63 ? 397 GLN B CA  1 
ATOM   6879 C  C   . GLN B 1 397 ? -37.520 -34.095 9.895   1.00 17.63 ? 397 GLN B C   1 
ATOM   6880 O  O   . GLN B 1 397 ? -37.929 -32.966 9.531   1.00 16.06 ? 397 GLN B O   1 
ATOM   6881 C  CB  . GLN B 1 397 ? -39.272 -35.751 9.723   1.00 21.07 ? 397 GLN B CB  1 
ATOM   6882 C  CG  . GLN B 1 397 ? -39.997 -36.863 8.999   1.00 24.35 ? 397 GLN B CG  1 
ATOM   6883 C  CD  . GLN B 1 397 ? -41.390 -36.907 9.572   1.00 26.34 ? 397 GLN B CD  1 
ATOM   6884 O  OE1 . GLN B 1 397 ? -41.617 -37.399 10.676  1.00 30.76 ? 397 GLN B OE1 1 
ATOM   6885 N  NE2 . GLN B 1 397 ? -42.319 -36.304 8.858   1.00 28.27 ? 397 GLN B NE2 1 
ATOM   6886 N  N   . ARG B 1 398 ? -36.841 -34.312 11.025  1.00 15.69 ? 398 ARG B N   1 
ATOM   6887 C  CA  . ARG B 1 398 ? -36.541 -33.213 11.961  1.00 15.45 ? 398 ARG B CA  1 
ATOM   6888 C  C   . ARG B 1 398 ? -35.102 -32.729 11.725  1.00 15.74 ? 398 ARG B C   1 
ATOM   6889 O  O   . ARG B 1 398 ? -34.519 -32.027 12.601  1.00 14.19 ? 398 ARG B O   1 
ATOM   6890 C  CB  . ARG B 1 398 ? -36.884 -33.699 13.371  1.00 15.93 ? 398 ARG B CB  1 
ATOM   6891 C  CG  . ARG B 1 398 ? -38.369 -33.976 13.595  1.00 15.09 ? 398 ARG B CG  1 
ATOM   6892 C  CD  . ARG B 1 398 ? -39.246 -32.767 13.342  1.00 14.50 ? 398 ARG B CD  1 
ATOM   6893 N  NE  . ARG B 1 398 ? -38.960 -31.637 14.215  1.00 15.36 ? 398 ARG B NE  1 
ATOM   6894 C  CZ  . ARG B 1 398 ? -39.394 -31.484 15.479  1.00 14.67 ? 398 ARG B CZ  1 
ATOM   6895 N  NH1 . ARG B 1 398 ? -40.107 -32.429 16.072  1.00 14.17 ? 398 ARG B NH1 1 
ATOM   6896 N  NH2 . ARG B 1 398 ? -39.116 -30.371 16.142  1.00 14.11 ? 398 ARG B NH2 1 
ATOM   6897 N  N   . ALA B 1 399 ? -34.544 -33.059 10.562  1.00 16.32 ? 399 ALA B N   1 
ATOM   6898 C  CA  . ALA B 1 399 ? -33.243 -32.516 10.120  1.00 16.84 ? 399 ALA B CA  1 
ATOM   6899 C  C   . ALA B 1 399 ? -33.403 -31.002 9.927   1.00 17.36 ? 399 ALA B C   1 
ATOM   6900 O  O   . ALA B 1 399 ? -34.549 -30.498 9.885   1.00 17.21 ? 399 ALA B O   1 
ATOM   6901 C  CB  . ALA B 1 399 ? -32.758 -33.227 8.886   1.00 17.29 ? 399 ALA B CB  1 
ATOM   6902 N  N   . CYS B 1 400 ? -32.284 -30.287 9.977   1.00 16.39 ? 400 CYS B N   1 
ATOM   6903 C  CA  . CYS B 1 400 ? -32.214 -28.818 9.857   1.00 16.77 ? 400 CYS B CA  1 
ATOM   6904 C  C   . CYS B 1 400 ? -32.849 -28.381 8.530   1.00 17.63 ? 400 CYS B C   1 
ATOM   6905 O  O   . CYS B 1 400 ? -32.359 -28.795 7.457   1.00 15.52 ? 400 CYS B O   1 
ATOM   6906 C  CB  . CYS B 1 400 ? -30.753 -28.385 9.918   1.00 17.11 ? 400 CYS B CB  1 
ATOM   6907 S  SG  . CYS B 1 400 ? -30.508 -26.604 9.776   1.00 16.07 ? 400 CYS B SG  1 
ATOM   6908 N  N   . ILE B 1 401 ? -33.884 -27.547 8.603   1.00 19.84 ? 401 ILE B N   1 
ATOM   6909 C  CA  . ILE B 1 401 ? -34.526 -26.912 7.411   1.00 20.20 ? 401 ILE B CA  1 
ATOM   6910 C  C   . ILE B 1 401 ? -33.592 -25.853 6.813   1.00 19.70 ? 401 ILE B C   1 
ATOM   6911 O  O   . ILE B 1 401 ? -33.663 -25.640 5.595   1.00 20.08 ? 401 ILE B O   1 
ATOM   6912 C  CB  . ILE B 1 401 ? -35.898 -26.337 7.786   1.00 21.11 ? 401 ILE B CB  1 
ATOM   6913 C  CG1 . ILE B 1 401 ? -36.763 -26.148 6.540   1.00 21.22 ? 401 ILE B CG1 1 
ATOM   6914 C  CG2 . ILE B 1 401 ? -35.778 -25.061 8.613   1.00 22.36 ? 401 ILE B CG2 1 
ATOM   6915 C  CD1 . ILE B 1 401 ? -38.205 -25.815 6.840   1.00 21.24 ? 401 ILE B CD1 1 
ATOM   6916 N  N   . GLY B 1 402 ? -32.722 -25.253 7.630   1.00 18.91 ? 402 GLY B N   1 
ATOM   6917 C  CA  . GLY B 1 402 ? -31.748 -24.238 7.186   1.00 18.94 ? 402 GLY B CA  1 
ATOM   6918 C  C   . GLY B 1 402 ? -30.422 -24.812 6.713   1.00 17.41 ? 402 GLY B C   1 
ATOM   6919 O  O   . GLY B 1 402 ? -29.524 -24.022 6.462   1.00 18.34 ? 402 GLY B O   1 
ATOM   6920 N  N   . GLN B 1 403 ? -30.287 -26.120 6.579   1.00 17.40 ? 403 GLN B N   1 
ATOM   6921 C  CA  . GLN B 1 403 ? -29.044 -26.752 6.081   1.00 19.73 ? 403 GLN B CA  1 
ATOM   6922 C  C   . GLN B 1 403 ? -28.588 -26.094 4.766   1.00 20.61 ? 403 GLN B C   1 
ATOM   6923 O  O   . GLN B 1 403 ? -27.403 -25.779 4.694   1.00 19.99 ? 403 GLN B O   1 
ATOM   6924 C  CB  . GLN B 1 403 ? -29.242 -28.247 5.865   1.00 20.77 ? 403 GLN B CB  1 
ATOM   6925 C  CG  . GLN B 1 403 ? -27.985 -28.939 5.373   1.00 22.02 ? 403 GLN B CG  1 
ATOM   6926 C  CD  . GLN B 1 403 ? -28.139 -30.437 5.232   1.00 23.12 ? 403 GLN B CD  1 
ATOM   6927 O  OE1 . GLN B 1 403 ? -29.009 -31.061 5.825   1.00 26.41 ? 403 GLN B OE1 1 
ATOM   6928 N  NE2 . GLN B 1 403 ? -27.277 -31.040 4.440   1.00 23.10 ? 403 GLN B NE2 1 
ATOM   6929 N  N   . GLN B 1 404 ? -29.461 -25.905 3.767   1.00 21.36 ? 404 GLN B N   1 
ATOM   6930 C  CA  . GLN B 1 404 ? -29.047 -25.375 2.432   1.00 25.06 ? 404 GLN B CA  1 
ATOM   6931 C  C   . GLN B 1 404 ? -28.596 -23.936 2.627   1.00 22.34 ? 404 GLN B C   1 
ATOM   6932 O  O   . GLN B 1 404 ? -27.619 -23.524 1.985   1.00 23.39 ? 404 GLN B O   1 
ATOM   6933 C  CB  . GLN B 1 404 ? -30.175 -25.308 1.391   1.00 31.30 ? 404 GLN B CB  1 
ATOM   6934 C  CG  . GLN B 1 404 ? -30.840 -26.632 1.071   1.00 35.26 ? 404 GLN B CG  1 
ATOM   6935 C  CD  . GLN B 1 404 ? -29.742 -27.611 0.820   1.00 39.11 ? 404 GLN B CD  1 
ATOM   6936 O  OE1 . GLN B 1 404 ? -29.562 -28.578 1.556   1.00 49.28 ? 404 GLN B OE1 1 
ATOM   6937 N  NE2 . GLN B 1 404 ? -28.924 -27.278 -0.158  1.00 49.46 ? 404 GLN B NE2 1 
ATOM   6938 N  N   . PHE B 1 405 ? -29.323 -23.224 3.477   1.00 19.91 ? 405 PHE B N   1 
ATOM   6939 C  CA  . PHE B 1 405 ? -29.156 -21.780 3.746   1.00 18.84 ? 405 PHE B CA  1 
ATOM   6940 C  C   . PHE B 1 405 ? -27.784 -21.591 4.376   1.00 19.50 ? 405 PHE B C   1 
ATOM   6941 O  O   . PHE B 1 405 ? -27.004 -20.746 3.896   1.00 21.56 ? 405 PHE B O   1 
ATOM   6942 C  CB  . PHE B 1 405 ? -30.314 -21.269 4.612   1.00 17.42 ? 405 PHE B CB  1 
ATOM   6943 C  CG  . PHE B 1 405 ? -30.309 -19.789 4.922   1.00 17.36 ? 405 PHE B CG  1 
ATOM   6944 C  CD1 . PHE B 1 405 ? -29.427 -19.259 5.865   1.00 15.88 ? 405 PHE B CD1 1 
ATOM   6945 C  CD2 . PHE B 1 405 ? -31.221 -18.929 4.316   1.00 17.86 ? 405 PHE B CD2 1 
ATOM   6946 C  CE1 . PHE B 1 405 ? -29.433 -17.911 6.161   1.00 15.60 ? 405 PHE B CE1 1 
ATOM   6947 C  CE2 . PHE B 1 405 ? -31.237 -17.573 4.628   1.00 17.45 ? 405 PHE B CE2 1 
ATOM   6948 C  CZ  . PHE B 1 405 ? -30.338 -17.067 5.546   1.00 17.53 ? 405 PHE B CZ  1 
ATOM   6949 N  N   . ALA B 1 406 ? -27.499 -22.363 5.420   1.00 20.17 ? 406 ALA B N   1 
ATOM   6950 C  CA  . ALA B 1 406 ? -26.224 -22.296 6.174   1.00 18.18 ? 406 ALA B CA  1 
ATOM   6951 C  C   . ALA B 1 406 ? -25.055 -22.628 5.240   1.00 17.25 ? 406 ALA B C   1 
ATOM   6952 O  O   . ALA B 1 406 ? -24.015 -22.002 5.356   1.00 18.01 ? 406 ALA B O   1 
ATOM   6953 C  CB  . ALA B 1 406 ? -26.271 -23.206 7.379   1.00 16.23 ? 406 ALA B CB  1 
ATOM   6954 N  N   . LEU B 1 407 ? -25.189 -23.612 4.363   1.00 17.45 ? 407 LEU B N   1 
ATOM   6955 C  CA  . LEU B 1 407 ? -24.030 -24.063 3.551   1.00 18.74 ? 407 LEU B CA  1 
ATOM   6956 C  C   . LEU B 1 407 ? -23.781 -23.052 2.411   1.00 18.85 ? 407 LEU B C   1 
ATOM   6957 O  O   . LEU B 1 407 ? -22.592 -22.765 2.081   1.00 17.81 ? 407 LEU B O   1 
ATOM   6958 C  CB  . LEU B 1 407 ? -24.292 -25.497 3.073   1.00 19.68 ? 407 LEU B CB  1 
ATOM   6959 C  CG  . LEU B 1 407 ? -24.191 -26.567 4.165   1.00 20.91 ? 407 LEU B CG  1 
ATOM   6960 C  CD1 . LEU B 1 407 ? -24.599 -27.937 3.652   1.00 20.20 ? 407 LEU B CD1 1 
ATOM   6961 C  CD2 . LEU B 1 407 ? -22.780 -26.628 4.744   1.00 22.79 ? 407 LEU B CD2 1 
ATOM   6962 N  N   . HIS B 1 408 ? -24.855 -22.493 1.850   1.00 20.11 ? 408 HIS B N   1 
ATOM   6963 C  CA  . HIS B 1 408 ? -24.785 -21.367 0.885   1.00 19.91 ? 408 HIS B CA  1 
ATOM   6964 C  C   . HIS B 1 408 ? -24.069 -20.155 1.510   1.00 20.44 ? 408 HIS B C   1 
ATOM   6965 O  O   . HIS B 1 408 ? -23.060 -19.702 0.920   1.00 21.63 ? 408 HIS B O   1 
ATOM   6966 C  CB  . HIS B 1 408 ? -26.166 -20.994 0.348   1.00 20.63 ? 408 HIS B CB  1 
ATOM   6967 C  CG  . HIS B 1 408 ? -26.051 -20.095 -0.837  1.00 20.85 ? 408 HIS B CG  1 
ATOM   6968 N  ND1 . HIS B 1 408 ? -25.762 -20.577 -2.109  1.00 21.20 ? 408 HIS B ND1 1 
ATOM   6969 C  CD2 . HIS B 1 408 ? -26.101 -18.752 -0.936  1.00 20.85 ? 408 HIS B CD2 1 
ATOM   6970 C  CE1 . HIS B 1 408 ? -25.683 -19.565 -2.939  1.00 21.88 ? 408 HIS B CE1 1 
ATOM   6971 N  NE2 . HIS B 1 408 ? -25.893 -18.431 -2.247  1.00 22.34 ? 408 HIS B NE2 1 
ATOM   6972 N  N   . GLU B 1 409 ? -24.579 -19.607 2.608   1.00 19.73 ? 409 GLU B N   1 
ATOM   6973 C  CA  . GLU B 1 409 ? -24.007 -18.394 3.249   1.00 21.87 ? 409 GLU B CA  1 
ATOM   6974 C  C   . GLU B 1 409 ? -22.533 -18.678 3.551   1.00 21.70 ? 409 GLU B C   1 
ATOM   6975 O  O   . GLU B 1 409 ? -21.684 -17.840 3.187   1.00 23.98 ? 409 GLU B O   1 
ATOM   6976 C  CB  . GLU B 1 409 ? -24.791 -18.004 4.514   1.00 24.94 ? 409 GLU B CB  1 
ATOM   6977 C  CG  . GLU B 1 409 ? -24.144 -16.887 5.314   1.00 28.21 ? 409 GLU B CG  1 
ATOM   6978 C  CD  . GLU B 1 409 ? -24.890 -16.355 6.540   1.00 32.97 ? 409 GLU B CD  1 
ATOM   6979 O  OE1 . GLU B 1 409 ? -25.735 -17.087 7.166   1.00 41.85 ? 409 GLU B OE1 1 
ATOM   6980 O  OE2 . GLU B 1 409 ? -24.605 -15.191 6.894   1.00 36.26 ? 409 GLU B OE2 1 
ATOM   6981 N  N   . ALA B 1 410 ? -22.234 -19.838 4.143   1.00 18.96 ? 410 ALA B N   1 
ATOM   6982 C  CA  . ALA B 1 410 ? -20.875 -20.189 4.596   1.00 18.37 ? 410 ALA B CA  1 
ATOM   6983 C  C   . ALA B 1 410 ? -19.961 -20.332 3.367   1.00 18.09 ? 410 ALA B C   1 
ATOM   6984 O  O   . ALA B 1 410 ? -18.826 -19.812 3.401   1.00 17.19 ? 410 ALA B O   1 
ATOM   6985 C  CB  . ALA B 1 410 ? -20.923 -21.425 5.458   1.00 17.68 ? 410 ALA B CB  1 
ATOM   6986 N  N   . THR B 1 411 ? -20.409 -21.012 2.312   1.00 17.31 ? 411 THR B N   1 
ATOM   6987 C  CA  . THR B 1 411 ? -19.573 -21.181 1.099   1.00 17.11 ? 411 THR B CA  1 
ATOM   6988 C  C   . THR B 1 411 ? -19.257 -19.768 0.575   1.00 17.47 ? 411 THR B C   1 
ATOM   6989 O  O   . THR B 1 411 ? -18.045 -19.446 0.355   1.00 18.62 ? 411 THR B O   1 
ATOM   6990 C  CB  . THR B 1 411 ? -20.227 -22.126 0.079   1.00 17.00 ? 411 THR B CB  1 
ATOM   6991 O  OG1 . THR B 1 411 ? -20.457 -23.394 0.698   1.00 16.49 ? 411 THR B OG1 1 
ATOM   6992 C  CG2 . THR B 1 411 ? -19.386 -22.330 -1.162  1.00 16.38 ? 411 THR B CG2 1 
ATOM   6993 N  N   . LEU B 1 412 ? -20.275 -18.919 0.452   1.00 17.61 ? 412 LEU B N   1 
ATOM   6994 C  CA  . LEU B 1 412 ? -20.124 -17.551 -0.093  1.00 17.98 ? 412 LEU B CA  1 
ATOM   6995 C  C   . LEU B 1 412 ? -19.119 -16.785 0.770   1.00 17.88 ? 412 LEU B C   1 
ATOM   6996 O  O   . LEU B 1 412 ? -18.143 -16.249 0.227   1.00 19.05 ? 412 LEU B O   1 
ATOM   6997 C  CB  . LEU B 1 412 ? -21.481 -16.839 -0.136  1.00 19.74 ? 412 LEU B CB  1 
ATOM   6998 C  CG  . LEU B 1 412 ? -21.399 -15.324 -0.355  1.00 19.57 ? 412 LEU B CG  1 
ATOM   6999 C  CD1 . LEU B 1 412 ? -21.029 -15.018 -1.790  1.00 20.54 ? 412 LEU B CD1 1 
ATOM   7000 C  CD2 . LEU B 1 412 ? -22.682 -14.631 0.043   1.00 19.59 ? 412 LEU B CD2 1 
ATOM   7001 N  N   . VAL B 1 413 ? -19.332 -16.745 2.069   1.00 17.79 ? 413 VAL B N   1 
ATOM   7002 C  CA  . VAL B 1 413 ? -18.465 -15.940 2.975   1.00 19.54 ? 413 VAL B CA  1 
ATOM   7003 C  C   . VAL B 1 413 ? -17.034 -16.481 2.954   1.00 19.68 ? 413 VAL B C   1 
ATOM   7004 O  O   . VAL B 1 413 ? -16.101 -15.680 2.729   1.00 20.44 ? 413 VAL B O   1 
ATOM   7005 C  CB  . VAL B 1 413 ? -19.034 -15.872 4.402   1.00 18.36 ? 413 VAL B CB  1 
ATOM   7006 C  CG1 . VAL B 1 413 ? -18.005 -15.290 5.362   1.00 18.73 ? 413 VAL B CG1 1 
ATOM   7007 C  CG2 . VAL B 1 413 ? -20.322 -15.062 4.400   1.00 18.30 ? 413 VAL B CG2 1 
ATOM   7008 N  N   . LEU B 1 414 ? -16.858 -17.782 3.149   1.00 20.46 ? 414 LEU B N   1 
ATOM   7009 C  CA  . LEU B 1 414 ? -15.489 -18.366 3.124   1.00 21.21 ? 414 LEU B CA  1 
ATOM   7010 C  C   . LEU B 1 414 ? -14.854 -18.114 1.742   1.00 19.26 ? 414 LEU B C   1 
ATOM   7011 O  O   . LEU B 1 414 ? -13.686 -17.632 1.705   1.00 18.53 ? 414 LEU B O   1 
ATOM   7012 C  CB  . LEU B 1 414 ? -15.533 -19.847 3.508   1.00 20.90 ? 414 LEU B CB  1 
ATOM   7013 C  CG  . LEU B 1 414 ? -14.167 -20.501 3.705   1.00 22.88 ? 414 LEU B CG  1 
ATOM   7014 C  CD1 . LEU B 1 414 ? -13.326 -19.731 4.707   1.00 22.86 ? 414 LEU B CD1 1 
ATOM   7015 C  CD2 . LEU B 1 414 ? -14.322 -21.947 4.154   1.00 23.65 ? 414 LEU B CD2 1 
ATOM   7016 N  N   . GLY B 1 415 ? -15.601 -18.354 0.658   1.00 17.99 ? 415 GLY B N   1 
ATOM   7017 C  CA  . GLY B 1 415 ? -15.129 -18.089 -0.711  1.00 18.16 ? 415 GLY B CA  1 
ATOM   7018 C  C   . GLY B 1 415 ? -14.544 -16.696 -0.808  1.00 19.59 ? 415 GLY B C   1 
ATOM   7019 O  O   . GLY B 1 415 ? -13.350 -16.530 -1.185  1.00 18.94 ? 415 GLY B O   1 
ATOM   7020 N  N   . MET B 1 416 ? -15.328 -15.701 -0.399  1.00 21.14 ? 416 MET B N   1 
ATOM   7021 C  CA  . MET B 1 416 ? -14.910 -14.286 -0.533  1.00 21.98 ? 416 MET B CA  1 
ATOM   7022 C  C   . MET B 1 416 ? -13.705 -14.003 0.365   1.00 21.14 ? 416 MET B C   1 
ATOM   7023 O  O   . MET B 1 416 ? -12.844 -13.205 -0.049  1.00 21.85 ? 416 MET B O   1 
ATOM   7024 C  CB  . MET B 1 416 ? -16.066 -13.353 -0.192  1.00 23.32 ? 416 MET B CB  1 
ATOM   7025 C  CG  . MET B 1 416 ? -17.176 -13.453 -1.224  1.00 23.50 ? 416 MET B CG  1 
ATOM   7026 S  SD  . MET B 1 416 ? -18.444 -12.233 -0.906  1.00 23.77 ? 416 MET B SD  1 
ATOM   7027 C  CE  . MET B 1 416 ? -17.546 -10.725 -1.263  1.00 24.60 ? 416 MET B CE  1 
ATOM   7028 N  N   . MET B 1 417 ? -13.634 -14.645 1.526   1.00 20.12 ? 417 MET B N   1 
ATOM   7029 C  CA  . MET B 1 417 ? -12.557 -14.387 2.507   1.00 20.88 ? 417 MET B CA  1 
ATOM   7030 C  C   . MET B 1 417 ? -11.253 -14.873 1.871   1.00 20.44 ? 417 MET B C   1 
ATOM   7031 O  O   . MET B 1 417 ? -10.242 -14.127 1.950   1.00 20.30 ? 417 MET B O   1 
ATOM   7032 C  CB  . MET B 1 417 ? -12.816 -15.093 3.848   1.00 21.60 ? 417 MET B CB  1 
ATOM   7033 C  CG  . MET B 1 417 ? -13.944 -14.471 4.666   1.00 22.09 ? 417 MET B CG  1 
ATOM   7034 S  SD  . MET B 1 417 ? -14.439 -15.503 6.106   1.00 25.92 ? 417 MET B SD  1 
ATOM   7035 C  CE  . MET B 1 417 ? -12.864 -15.958 6.811   1.00 25.42 ? 417 MET B CE  1 
ATOM   7036 N  N   . LEU B 1 418 ? -11.294 -16.048 1.231   1.00 20.53 ? 418 LEU B N   1 
ATOM   7037 C  CA  . LEU B 1 418 ? -10.110 -16.683 0.586   1.00 20.71 ? 418 LEU B CA  1 
ATOM   7038 C  C   . LEU B 1 418 ? -9.726  -15.890 -0.671  1.00 20.52 ? 418 LEU B C   1 
ATOM   7039 O  O   . LEU B 1 418 ? -8.512  -15.720 -0.926  1.00 21.63 ? 418 LEU B O   1 
ATOM   7040 C  CB  . LEU B 1 418 ? -10.401 -18.155 0.270   1.00 21.57 ? 418 LEU B CB  1 
ATOM   7041 C  CG  . LEU B 1 418 ? -10.634 -19.070 1.476   1.00 22.04 ? 418 LEU B CG  1 
ATOM   7042 C  CD1 . LEU B 1 418 ? -11.070 -20.453 1.048   1.00 22.23 ? 418 LEU B CD1 1 
ATOM   7043 C  CD2 . LEU B 1 418 ? -9.383  -19.179 2.317   1.00 23.22 ? 418 LEU B CD2 1 
ATOM   7044 N  N   . LYS B 1 419 ? -10.693 -15.356 -1.410  1.00 19.91 ? 419 LYS B N   1 
ATOM   7045 C  CA  . LYS B 1 419 ? -10.377 -14.517 -2.600  1.00 19.75 ? 419 LYS B CA  1 
ATOM   7046 C  C   . LYS B 1 419 ? -9.594  -13.273 -2.182  1.00 19.86 ? 419 LYS B C   1 
ATOM   7047 O  O   . LYS B 1 419 ? -8.657  -12.899 -2.916  1.00 21.25 ? 419 LYS B O   1 
ATOM   7048 C  CB  . LYS B 1 419 ? -11.643 -14.066 -3.330  1.00 20.58 ? 419 LYS B CB  1 
ATOM   7049 C  CG  . LYS B 1 419 ? -11.432 -13.041 -4.432  1.00 19.71 ? 419 LYS B CG  1 
ATOM   7050 C  CD  . LYS B 1 419 ? -12.706 -12.749 -5.141  1.00 19.95 ? 419 LYS B CD  1 
ATOM   7051 C  CE  . LYS B 1 419 ? -12.613 -11.604 -6.116  1.00 21.05 ? 419 LYS B CE  1 
ATOM   7052 N  NZ  . LYS B 1 419 ? -13.935 -11.295 -6.714  1.00 21.97 ? 419 LYS B NZ  1 
ATOM   7053 N  N   . HIS B 1 420 ? -9.970  -12.629 -1.081  1.00 19.62 ? 420 HIS B N   1 
ATOM   7054 C  CA  . HIS B 1 420 ? -9.609  -11.214 -0.821  1.00 21.22 ? 420 HIS B CA  1 
ATOM   7055 C  C   . HIS B 1 420 ? -8.391  -11.092 0.104   1.00 22.03 ? 420 HIS B C   1 
ATOM   7056 O  O   . HIS B 1 420 ? -7.771  -10.009 0.089   1.00 21.50 ? 420 HIS B O   1 
ATOM   7057 C  CB  . HIS B 1 420 ? -10.838 -10.432 -0.326  1.00 22.00 ? 420 HIS B CB  1 
ATOM   7058 C  CG  . HIS B 1 420 ? -11.726 -10.005 -1.444  1.00 23.12 ? 420 HIS B CG  1 
ATOM   7059 N  ND1 . HIS B 1 420 ? -11.453 -8.881  -2.210  1.00 23.70 ? 420 HIS B ND1 1 
ATOM   7060 C  CD2 . HIS B 1 420 ? -12.853 -10.553 -1.959  1.00 23.34 ? 420 HIS B CD2 1 
ATOM   7061 C  CE1 . HIS B 1 420 ? -12.384 -8.745  -3.133  1.00 21.63 ? 420 HIS B CE1 1 
ATOM   7062 N  NE2 . HIS B 1 420 ? -13.233 -9.779  -3.022  1.00 22.46 ? 420 HIS B NE2 1 
ATOM   7063 N  N   . PHE B 1 421 ? -8.031  -12.144 0.850   1.00 23.16 ? 421 PHE B N   1 
ATOM   7064 C  CA  . PHE B 1 421 ? -7.077  -12.033 1.979   1.00 22.79 ? 421 PHE B CA  1 
ATOM   7065 C  C   . PHE B 1 421 ? -6.168  -13.260 2.111   1.00 23.23 ? 421 PHE B C   1 
ATOM   7066 O  O   . PHE B 1 421 ? -6.640  -14.391 1.986   1.00 20.88 ? 421 PHE B O   1 
ATOM   7067 C  CB  . PHE B 1 421 ? -7.847  -11.875 3.296   1.00 23.59 ? 421 PHE B CB  1 
ATOM   7068 C  CG  . PHE B 1 421 ? -8.743  -10.668 3.397   1.00 21.92 ? 421 PHE B CG  1 
ATOM   7069 C  CD1 . PHE B 1 421 ? -8.209  -9.414  3.636   1.00 20.31 ? 421 PHE B CD1 1 
ATOM   7070 C  CD2 . PHE B 1 421 ? -10.119 -10.798 3.262   1.00 21.76 ? 421 PHE B CD2 1 
ATOM   7071 C  CE1 . PHE B 1 421 ? -9.027  -8.300  3.696   1.00 20.67 ? 421 PHE B CE1 1 
ATOM   7072 C  CE2 . PHE B 1 421 ? -10.934 -9.675  3.319   1.00 22.86 ? 421 PHE B CE2 1 
ATOM   7073 C  CZ  . PHE B 1 421 ? -10.382 -8.429  3.556   1.00 20.94 ? 421 PHE B CZ  1 
ATOM   7074 N  N   . ASP B 1 422 ? -4.897  -13.020 2.449   1.00 24.85 ? 422 ASP B N   1 
ATOM   7075 C  CA  . ASP B 1 422 ? -4.001  -14.053 3.026   1.00 28.27 ? 422 ASP B CA  1 
ATOM   7076 C  C   . ASP B 1 422 ? -4.196  -13.994 4.545   1.00 27.29 ? 422 ASP B C   1 
ATOM   7077 O  O   . ASP B 1 422 ? -4.416  -12.896 5.080   1.00 23.72 ? 422 ASP B O   1 
ATOM   7078 C  CB  . ASP B 1 422 ? -2.548  -13.851 2.593   1.00 30.92 ? 422 ASP B CB  1 
ATOM   7079 C  CG  . ASP B 1 422 ? -2.326  -13.967 1.086   1.00 37.03 ? 422 ASP B CG  1 
ATOM   7080 O  OD1 . ASP B 1 422 ? -3.025  -14.792 0.446   1.00 37.36 ? 422 ASP B OD1 1 
ATOM   7081 O  OD2 . ASP B 1 422 ? -1.443  -13.239 0.554   1.00 39.43 ? 422 ASP B OD2 1 
ATOM   7082 N  N   . PHE B 1 423 ? -4.184  -15.142 5.201   1.00 26.42 ? 423 PHE B N   1 
ATOM   7083 C  CA  . PHE B 1 423 ? -4.443  -15.239 6.652   1.00 28.29 ? 423 PHE B CA  1 
ATOM   7084 C  C   . PHE B 1 423 ? -3.166  -15.652 7.374   1.00 29.33 ? 423 PHE B C   1 
ATOM   7085 O  O   . PHE B 1 423 ? -2.370  -16.423 6.847   1.00 29.47 ? 423 PHE B O   1 
ATOM   7086 C  CB  . PHE B 1 423 ? -5.615  -16.182 6.901   1.00 28.35 ? 423 PHE B CB  1 
ATOM   7087 C  CG  . PHE B 1 423 ? -6.907  -15.542 6.500   1.00 27.40 ? 423 PHE B CG  1 
ATOM   7088 C  CD1 . PHE B 1 423 ? -7.484  -14.577 7.305   1.00 29.87 ? 423 PHE B CD1 1 
ATOM   7089 C  CD2 . PHE B 1 423 ? -7.484  -15.830 5.284   1.00 28.18 ? 423 PHE B CD2 1 
ATOM   7090 C  CE1 . PHE B 1 423 ? -8.637  -13.924 6.902   1.00 31.34 ? 423 PHE B CE1 1 
ATOM   7091 C  CE2 . PHE B 1 423 ? -8.643  -15.189 4.887   1.00 29.83 ? 423 PHE B CE2 1 
ATOM   7092 C  CZ  . PHE B 1 423 ? -9.218  -14.239 5.695   1.00 31.34 ? 423 PHE B CZ  1 
ATOM   7093 N  N   . GLU B 1 424 ? -2.999  -15.137 8.578   1.00 29.26 ? 424 GLU B N   1 
ATOM   7094 C  CA  . GLU B 1 424 ? -1.822  -15.424 9.415   1.00 30.98 ? 424 GLU B CA  1 
ATOM   7095 C  C   . GLU B 1 424 ? -2.352  -15.803 10.802  1.00 28.94 ? 424 GLU B C   1 
ATOM   7096 O  O   . GLU B 1 424 ? -3.142  -15.028 11.357  1.00 27.37 ? 424 GLU B O   1 
ATOM   7097 C  CB  . GLU B 1 424 ? -0.902  -14.205 9.396   1.00 30.95 ? 424 GLU B CB  1 
ATOM   7098 C  CG  . GLU B 1 424 ? 0.497   -14.514 9.875   1.00 35.07 ? 424 GLU B CG  1 
ATOM   7099 C  CD  . GLU B 1 424 ? 1.245   -13.333 10.472  1.00 36.73 ? 424 GLU B CD  1 
ATOM   7100 O  OE1 . GLU B 1 424 ? 1.002   -12.183 10.028  1.00 40.74 ? 424 GLU B OE1 1 
ATOM   7101 O  OE2 . GLU B 1 424 ? 2.056   -13.567 11.381  1.00 34.09 ? 424 GLU B OE2 1 
ATOM   7102 N  N   . ASP B 1 425 ? -1.974  -16.987 11.297  1.00 26.95 ? 425 ASP B N   1 
ATOM   7103 C  CA  . ASP B 1 425 ? -2.200  -17.439 12.695  1.00 24.93 ? 425 ASP B CA  1 
ATOM   7104 C  C   . ASP B 1 425 ? -1.076  -16.864 13.559  1.00 24.67 ? 425 ASP B C   1 
ATOM   7105 O  O   . ASP B 1 425 ? -0.272  -17.646 14.077  1.00 26.19 ? 425 ASP B O   1 
ATOM   7106 C  CB  . ASP B 1 425 ? -2.232  -18.964 12.742  1.00 25.49 ? 425 ASP B CB  1 
ATOM   7107 C  CG  . ASP B 1 425 ? -2.273  -19.550 14.134  1.00 26.34 ? 425 ASP B CG  1 
ATOM   7108 O  OD1 . ASP B 1 425 ? -2.838  -18.885 15.050  1.00 25.74 ? 425 ASP B OD1 1 
ATOM   7109 O  OD2 . ASP B 1 425 ? -1.751  -20.682 14.277  1.00 26.99 ? 425 ASP B OD2 1 
ATOM   7110 N  N   . HIS B 1 426 ? -1.035  -15.541 13.706  1.00 22.15 ? 426 HIS B N   1 
ATOM   7111 C  CA  . HIS B 1 426 ? 0.109   -14.787 14.267  1.00 22.37 ? 426 HIS B CA  1 
ATOM   7112 C  C   . HIS B 1 426 ? 0.315   -15.103 15.760  1.00 23.28 ? 426 HIS B C   1 
ATOM   7113 O  O   . HIS B 1 426 ? 1.405   -14.785 16.243  1.00 24.90 ? 426 HIS B O   1 
ATOM   7114 C  CB  . HIS B 1 426 ? -0.043  -13.277 14.026  1.00 22.20 ? 426 HIS B CB  1 
ATOM   7115 C  CG  . HIS B 1 426 ? -1.210  -12.653 14.724  1.00 21.95 ? 426 HIS B CG  1 
ATOM   7116 N  ND1 . HIS B 1 426 ? -2.512  -12.946 14.392  1.00 21.11 ? 426 HIS B ND1 1 
ATOM   7117 C  CD2 . HIS B 1 426 ? -1.274  -11.767 15.738  1.00 21.02 ? 426 HIS B CD2 1 
ATOM   7118 C  CE1 . HIS B 1 426 ? -3.324  -12.282 15.181  1.00 20.30 ? 426 HIS B CE1 1 
ATOM   7119 N  NE2 . HIS B 1 426 ? -2.585  -11.541 16.000  1.00 20.81 ? 426 HIS B NE2 1 
ATOM   7120 N  N   . THR B 1 427 ? -0.673  -15.643 16.480  1.00 20.97 ? 427 THR B N   1 
ATOM   7121 C  CA  . THR B 1 427 ? -0.551  -15.984 17.924  1.00 19.08 ? 427 THR B CA  1 
ATOM   7122 C  C   . THR B 1 427 ? -0.282  -17.482 18.126  1.00 18.70 ? 427 THR B C   1 
ATOM   7123 O  O   . THR B 1 427 ? -0.148  -17.867 19.282  1.00 18.63 ? 427 THR B O   1 
ATOM   7124 C  CB  . THR B 1 427 ? -1.789  -15.559 18.722  1.00 18.09 ? 427 THR B CB  1 
ATOM   7125 O  OG1 . THR B 1 427 ? -2.936  -16.196 18.162  1.00 16.93 ? 427 THR B OG1 1 
ATOM   7126 C  CG2 . THR B 1 427 ? -1.968  -14.059 18.747  1.00 18.98 ? 427 THR B CG2 1 
ATOM   7127 N  N   . ASN B 1 428 ? -0.196  -18.291 17.065  1.00 20.34 ? 428 ASN B N   1 
ATOM   7128 C  CA  . ASN B 1 428 ? -0.173  -19.779 17.140  1.00 22.33 ? 428 ASN B CA  1 
ATOM   7129 C  C   . ASN B 1 428 ? -1.307  -20.224 18.085  1.00 22.17 ? 428 ASN B C   1 
ATOM   7130 O  O   . ASN B 1 428 ? -1.038  -20.859 19.110  1.00 21.46 ? 428 ASN B O   1 
ATOM   7131 C  CB  . ASN B 1 428 ? 1.203   -20.325 17.543  1.00 23.84 ? 428 ASN B CB  1 
ATOM   7132 C  CG  . ASN B 1 428 ? 2.313   -19.899 16.603  1.00 27.95 ? 428 ASN B CG  1 
ATOM   7133 O  OD1 . ASN B 1 428 ? 3.328   -19.359 17.039  1.00 32.05 ? 428 ASN B OD1 1 
ATOM   7134 N  ND2 . ASN B 1 428 ? 2.130   -20.095 15.307  1.00 31.42 ? 428 ASN B ND2 1 
ATOM   7135 N  N   . TYR B 1 429 ? -2.545  -19.880 17.735  1.00 22.44 ? 429 TYR B N   1 
ATOM   7136 C  CA  . TYR B 1 429 ? -3.781  -20.103 18.528  1.00 21.20 ? 429 TYR B CA  1 
ATOM   7137 C  C   . TYR B 1 429 ? -3.931  -21.572 18.966  1.00 22.49 ? 429 TYR B C   1 
ATOM   7138 O  O   . TYR B 1 429 ? -3.990  -22.496 18.103  1.00 22.64 ? 429 TYR B O   1 
ATOM   7139 C  CB  . TYR B 1 429 ? -4.977  -19.621 17.710  1.00 19.80 ? 429 TYR B CB  1 
ATOM   7140 C  CG  . TYR B 1 429 ? -6.286  -19.859 18.404  1.00 17.73 ? 429 TYR B CG  1 
ATOM   7141 C  CD1 . TYR B 1 429 ? -6.565  -19.256 19.612  1.00 17.01 ? 429 TYR B CD1 1 
ATOM   7142 C  CD2 . TYR B 1 429 ? -7.215  -20.727 17.872  1.00 16.32 ? 429 TYR B CD2 1 
ATOM   7143 C  CE1 . TYR B 1 429 ? -7.749  -19.519 20.283  1.00 16.93 ? 429 TYR B CE1 1 
ATOM   7144 C  CE2 . TYR B 1 429 ? -8.410  -20.979 18.513  1.00 16.41 ? 429 TYR B CE2 1 
ATOM   7145 C  CZ  . TYR B 1 429 ? -8.679  -20.373 19.725  1.00 16.21 ? 429 TYR B CZ  1 
ATOM   7146 O  OH  . TYR B 1 429 ? -9.847  -20.639 20.365  1.00 15.19 ? 429 TYR B OH  1 
ATOM   7147 N  N   . GLU B 1 430 ? -3.988  -21.769 20.287  1.00 24.00 ? 430 GLU B N   1 
ATOM   7148 C  CA  . GLU B 1 430 ? -4.398  -23.018 20.973  1.00 27.80 ? 430 GLU B CA  1 
ATOM   7149 C  C   . GLU B 1 430 ? -5.921  -22.989 21.061  1.00 26.00 ? 430 GLU B C   1 
ATOM   7150 O  O   . GLU B 1 430 ? -6.455  -22.125 21.806  1.00 25.02 ? 430 GLU B O   1 
ATOM   7151 C  CB  . GLU B 1 430 ? -3.831  -23.118 22.399  1.00 36.06 ? 430 GLU B CB  1 
ATOM   7152 C  CG  . GLU B 1 430 ? -4.431  -24.261 23.252  1.00 46.19 ? 430 GLU B CG  1 
ATOM   7153 C  CD  . GLU B 1 430 ? -4.821  -24.014 24.725  1.00 57.55 ? 430 GLU B CD  1 
ATOM   7154 O  OE1 . GLU B 1 430 ? -5.396  -22.929 25.057  1.00 67.46 ? 430 GLU B OE1 1 
ATOM   7155 O  OE2 . GLU B 1 430 ? -4.594  -24.934 25.562  1.00 58.06 ? 430 GLU B OE2 1 
ATOM   7156 N  N   . LEU B 1 431 ? -6.581  -23.934 20.386  1.00 25.02 ? 431 LEU B N   1 
ATOM   7157 C  CA  . LEU B 1 431 ? -8.055  -24.046 20.332  1.00 22.40 ? 431 LEU B CA  1 
ATOM   7158 C  C   . LEU B 1 431 ? -8.577  -24.146 21.762  1.00 23.75 ? 431 LEU B C   1 
ATOM   7159 O  O   . LEU B 1 431 ? -8.168  -25.069 22.478  1.00 23.54 ? 431 LEU B O   1 
ATOM   7160 C  CB  . LEU B 1 431 ? -8.463  -25.260 19.494  1.00 22.09 ? 431 LEU B CB  1 
ATOM   7161 C  CG  . LEU B 1 431 ? -9.971  -25.516 19.427  1.00 21.03 ? 431 LEU B CG  1 
ATOM   7162 C  CD1 . LEU B 1 431 ? -10.650 -24.490 18.540  1.00 21.02 ? 431 LEU B CD1 1 
ATOM   7163 C  CD2 . LEU B 1 431 ? -10.253 -26.917 18.942  1.00 20.36 ? 431 LEU B CD2 1 
ATOM   7164 N  N   . ASP B 1 432 ? -9.428  -23.191 22.134  1.00 26.18 ? 432 ASP B N   1 
ATOM   7165 C  CA  . ASP B 1 432 ? -10.269 -23.173 23.359  1.00 27.03 ? 432 ASP B CA  1 
ATOM   7166 C  C   . ASP B 1 432 ? -11.711 -23.039 22.848  1.00 25.76 ? 432 ASP B C   1 
ATOM   7167 O  O   . ASP B 1 432 ? -11.941 -22.215 21.925  1.00 25.35 ? 432 ASP B O   1 
ATOM   7168 C  CB  . ASP B 1 432 ? -9.822  -22.038 24.293  1.00 29.16 ? 432 ASP B CB  1 
ATOM   7169 C  CG  . ASP B 1 432 ? -10.464 -22.066 25.669  1.00 32.44 ? 432 ASP B CG  1 
ATOM   7170 O  OD1 . ASP B 1 432 ? -11.192 -23.018 25.944  1.00 39.02 ? 432 ASP B OD1 1 
ATOM   7171 O  OD2 . ASP B 1 432 ? -10.225 -21.145 26.458  1.00 33.98 ? 432 ASP B OD2 1 
ATOM   7172 N  N   . ILE B 1 433 ? -12.640 -23.827 23.380  1.00 23.07 ? 433 ILE B N   1 
ATOM   7173 C  CA  . ILE B 1 433 ? -14.003 -23.963 22.802  1.00 22.25 ? 433 ILE B CA  1 
ATOM   7174 C  C   . ILE B 1 433 ? -15.048 -23.509 23.822  1.00 25.43 ? 433 ILE B C   1 
ATOM   7175 O  O   . ILE B 1 433 ? -15.183 -24.152 24.904  1.00 24.03 ? 433 ILE B O   1 
ATOM   7176 C  CB  . ILE B 1 433 ? -14.229 -25.392 22.308  1.00 20.77 ? 433 ILE B CB  1 
ATOM   7177 C  CG1 . ILE B 1 433 ? -13.523 -25.574 20.965  1.00 21.33 ? 433 ILE B CG1 1 
ATOM   7178 C  CG2 . ILE B 1 433 ? -15.707 -25.695 22.202  1.00 21.23 ? 433 ILE B CG2 1 
ATOM   7179 C  CD1 . ILE B 1 433 ? -13.559 -26.969 20.422  1.00 21.35 ? 433 ILE B CD1 1 
ATOM   7180 N  N   . LYS B 1 434 ? -15.766 -22.444 23.464  1.00 25.20 ? 434 LYS B N   1 
ATOM   7181 C  CA  . LYS B 1 434 ? -16.863 -21.883 24.278  1.00 26.72 ? 434 LYS B CA  1 
ATOM   7182 C  C   . LYS B 1 434 ? -18.187 -22.492 23.798  1.00 25.87 ? 434 LYS B C   1 
ATOM   7183 O  O   . LYS B 1 434 ? -18.345 -22.766 22.581  1.00 23.52 ? 434 LYS B O   1 
ATOM   7184 C  CB  . LYS B 1 434 ? -16.886 -20.356 24.227  1.00 28.97 ? 434 LYS B CB  1 
ATOM   7185 C  CG  . LYS B 1 434 ? -17.955 -19.697 25.093  1.00 31.03 ? 434 LYS B CG  1 
ATOM   7186 C  CD  . LYS B 1 434 ? -18.646 -18.558 24.398  1.00 36.93 ? 434 LYS B CD  1 
ATOM   7187 C  CE  . LYS B 1 434 ? -17.834 -17.290 24.430  1.00 40.10 ? 434 LYS B CE  1 
ATOM   7188 N  NZ  . LYS B 1 434 ? -18.203 -16.493 25.622  1.00 46.94 ? 434 LYS B NZ  1 
ATOM   7189 N  N   . GLU B 1 435 ? -19.064 -22.709 24.777  1.00 23.94 ? 435 GLU B N   1 
ATOM   7190 C  CA  . GLU B 1 435 ? -20.317 -23.468 24.697  1.00 23.08 ? 435 GLU B CA  1 
ATOM   7191 C  C   . GLU B 1 435 ? -21.444 -22.564 25.177  1.00 24.73 ? 435 GLU B C   1 
ATOM   7192 O  O   . GLU B 1 435 ? -21.411 -22.109 26.335  1.00 22.57 ? 435 GLU B O   1 
ATOM   7193 C  CB  . GLU B 1 435 ? -20.278 -24.697 25.589  1.00 22.78 ? 435 GLU B CB  1 
ATOM   7194 C  CG  . GLU B 1 435 ? -19.136 -25.645 25.288  1.00 22.28 ? 435 GLU B CG  1 
ATOM   7195 C  CD  . GLU B 1 435 ? -19.397 -27.023 25.853  1.00 20.54 ? 435 GLU B CD  1 
ATOM   7196 O  OE1 . GLU B 1 435 ? -20.576 -27.271 26.192  1.00 19.08 ? 435 GLU B OE1 1 
ATOM   7197 O  OE2 . GLU B 1 435 ? -18.433 -27.832 25.945  1.00 20.04 ? 435 GLU B OE2 1 
ATOM   7198 N  N   . THR B 1 436 ? -22.357 -22.310 24.249  1.00 26.51 ? 436 THR B N   1 
ATOM   7199 C  CA  . THR B 1 436 ? -23.702 -21.732 24.421  1.00 25.78 ? 436 THR B CA  1 
ATOM   7200 C  C   . THR B 1 436 ? -24.634 -22.882 24.047  1.00 25.40 ? 436 THR B C   1 
ATOM   7201 O  O   . THR B 1 436 ? -24.350 -24.017 24.506  1.00 27.46 ? 436 THR B O   1 
ATOM   7202 C  CB  . THR B 1 436 ? -23.790 -20.458 23.571  1.00 27.21 ? 436 THR B CB  1 
ATOM   7203 O  OG1 . THR B 1 436 ? -23.480 -20.746 22.196  1.00 26.11 ? 436 THR B OG1 1 
ATOM   7204 C  CG2 . THR B 1 436 ? -22.853 -19.394 24.100  1.00 25.30 ? 436 THR B CG2 1 
ATOM   7205 N  N   . LEU B 1 437 ? -25.660 -22.640 23.233  1.00 23.48 ? 437 LEU B N   1 
ATOM   7206 C  CA  . LEU B 1 437 ? -26.377 -23.747 22.552  1.00 23.33 ? 437 LEU B CA  1 
ATOM   7207 C  C   . LEU B 1 437 ? -25.365 -24.467 21.638  1.00 21.79 ? 437 LEU B C   1 
ATOM   7208 O  O   . LEU B 1 437 ? -25.497 -25.677 21.487  1.00 20.18 ? 437 LEU B O   1 
ATOM   7209 C  CB  . LEU B 1 437 ? -27.563 -23.176 21.770  1.00 23.50 ? 437 LEU B CB  1 
ATOM   7210 C  CG  . LEU B 1 437 ? -28.448 -24.218 21.084  1.00 24.04 ? 437 LEU B CG  1 
ATOM   7211 C  CD1 . LEU B 1 437 ? -29.456 -24.819 22.060  1.00 24.48 ? 437 LEU B CD1 1 
ATOM   7212 C  CD2 . LEU B 1 437 ? -29.149 -23.635 19.864  1.00 22.63 ? 437 LEU B CD2 1 
ATOM   7213 N  N   . THR B 1 438 ? -24.360 -23.739 21.122  1.00 20.14 ? 438 THR B N   1 
ATOM   7214 C  CA  . THR B 1 438 ? -23.374 -24.211 20.110  1.00 19.97 ? 438 THR B CA  1 
ATOM   7215 C  C   . THR B 1 438 ? -21.936 -24.057 20.620  1.00 18.54 ? 438 THR B C   1 
ATOM   7216 O  O   . THR B 1 438 ? -21.727 -23.362 21.631  1.00 17.23 ? 438 THR B O   1 
ATOM   7217 C  CB  . THR B 1 438 ? -23.504 -23.458 18.776  1.00 19.63 ? 438 THR B CB  1 
ATOM   7218 O  OG1 . THR B 1 438 ? -23.435 -22.045 18.980  1.00 18.46 ? 438 THR B OG1 1 
ATOM   7219 C  CG2 . THR B 1 438 ? -24.801 -23.761 18.071  1.00 22.10 ? 438 THR B CG2 1 
ATOM   7220 N  N   . LEU B 1 439 ? -21.011 -24.670 19.875  1.00 19.13 ? 439 LEU B N   1 
ATOM   7221 C  CA  . LEU B 1 439 ? -19.534 -24.678 20.061  1.00 19.24 ? 439 LEU B CA  1 
ATOM   7222 C  C   . LEU B 1 439 ? -18.919 -23.602 19.176  1.00 20.43 ? 439 LEU B C   1 
ATOM   7223 O  O   . LEU B 1 439 ? -19.295 -23.531 17.993  1.00 21.22 ? 439 LEU B O   1 
ATOM   7224 C  CB  . LEU B 1 439 ? -18.978 -26.037 19.629  1.00 18.39 ? 439 LEU B CB  1 
ATOM   7225 C  CG  . LEU B 1 439 ? -19.576 -27.254 20.321  1.00 18.79 ? 439 LEU B CG  1 
ATOM   7226 C  CD1 . LEU B 1 439 ? -18.813 -28.498 19.908  1.00 18.80 ? 439 LEU B CD1 1 
ATOM   7227 C  CD2 . LEU B 1 439 ? -19.540 -27.086 21.838  1.00 20.06 ? 439 LEU B CD2 1 
ATOM   7228 N  N   . LYS B 1 440 ? -17.952 -22.869 19.715  1.00 21.03 ? 440 LYS B N   1 
ATOM   7229 C  CA  . LYS B 1 440 ? -17.295 -21.736 19.024  1.00 21.20 ? 440 LYS B CA  1 
ATOM   7230 C  C   . LYS B 1 440 ? -15.881 -21.621 19.568  1.00 21.40 ? 440 LYS B C   1 
ATOM   7231 O  O   . LYS B 1 440 ? -15.694 -21.740 20.780  1.00 19.01 ? 440 LYS B O   1 
ATOM   7232 C  CB  . LYS B 1 440 ? -18.047 -20.418 19.235  1.00 21.85 ? 440 LYS B CB  1 
ATOM   7233 C  CG  . LYS B 1 440 ? -19.201 -20.178 18.277  1.00 22.26 ? 440 LYS B CG  1 
ATOM   7234 C  CD  . LYS B 1 440 ? -19.947 -18.878 18.498  1.00 21.58 ? 440 LYS B CD  1 
ATOM   7235 C  CE  . LYS B 1 440 ? -21.157 -18.755 17.589  1.00 21.54 ? 440 LYS B CE  1 
ATOM   7236 N  NZ  . LYS B 1 440 ? -21.853 -17.455 17.755  1.00 21.87 ? 440 LYS B NZ  1 
ATOM   7237 N  N   . PRO B 1 441 ? -14.887 -21.409 18.667  1.00 21.26 ? 441 PRO B N   1 
ATOM   7238 C  CA  . PRO B 1 441 ? -13.521 -21.106 19.049  1.00 22.00 ? 441 PRO B CA  1 
ATOM   7239 C  C   . PRO B 1 441 ? -13.537 -19.865 19.932  1.00 22.26 ? 441 PRO B C   1 
ATOM   7240 O  O   . PRO B 1 441 ? -14.112 -18.901 19.548  1.00 28.75 ? 441 PRO B O   1 
ATOM   7241 C  CB  . PRO B 1 441 ? -12.795 -20.767 17.738  1.00 21.93 ? 441 PRO B CB  1 
ATOM   7242 C  CG  . PRO B 1 441 ? -13.637 -21.376 16.662  1.00 22.93 ? 441 PRO B CG  1 
ATOM   7243 C  CD  . PRO B 1 441 ? -15.047 -21.400 17.210  1.00 22.06 ? 441 PRO B CD  1 
ATOM   7244 N  N   . GLU B 1 442 ? -12.923 -19.923 21.089  1.00 22.49 ? 442 GLU B N   1 
ATOM   7245 C  CA  . GLU B 1 442 ? -12.876 -18.741 21.973  1.00 23.38 ? 442 GLU B CA  1 
ATOM   7246 C  C   . GLU B 1 442 ? -11.511 -18.048 21.828  1.00 19.99 ? 442 GLU B C   1 
ATOM   7247 O  O   . GLU B 1 442 ? -10.463 -18.723 21.850  1.00 16.33 ? 442 GLU B O   1 
ATOM   7248 C  CB  . GLU B 1 442 ? -13.185 -19.202 23.388  1.00 25.03 ? 442 GLU B CB  1 
ATOM   7249 C  CG  . GLU B 1 442 ? -13.060 -18.090 24.380  1.00 28.92 ? 442 GLU B CG  1 
ATOM   7250 C  CD  . GLU B 1 442 ? -13.842 -18.358 25.651  1.00 32.82 ? 442 GLU B CD  1 
ATOM   7251 O  OE1 . GLU B 1 442 ? -13.928 -19.567 26.081  1.00 30.42 ? 442 GLU B OE1 1 
ATOM   7252 O  OE2 . GLU B 1 442 ? -14.389 -17.357 26.176  1.00 33.68 ? 442 GLU B OE2 1 
ATOM   7253 N  N   . GLY B 1 443 ? -11.516 -16.732 21.680  1.00 17.97 ? 443 GLY B N   1 
ATOM   7254 C  CA  . GLY B 1 443 ? -10.259 -15.977 21.693  1.00 18.45 ? 443 GLY B CA  1 
ATOM   7255 C  C   . GLY B 1 443 ? -9.454  -16.249 20.445  1.00 17.86 ? 443 GLY B C   1 
ATOM   7256 O  O   . GLY B 1 443 ? -8.284  -15.893 20.435  1.00 18.37 ? 443 GLY B O   1 
ATOM   7257 N  N   . PHE B 1 444 ? -10.064 -16.817 19.408  1.00 16.76 ? 444 PHE B N   1 
ATOM   7258 C  CA  . PHE B 1 444 ? -9.388  -17.063 18.107  1.00 17.29 ? 444 PHE B CA  1 
ATOM   7259 C  C   . PHE B 1 444 ? -9.236  -15.717 17.380  1.00 18.31 ? 444 PHE B C   1 
ATOM   7260 O  O   . PHE B 1 444 ? -10.236 -15.042 17.034  1.00 17.41 ? 444 PHE B O   1 
ATOM   7261 C  CB  . PHE B 1 444 ? -10.160 -18.134 17.336  1.00 16.29 ? 444 PHE B CB  1 
ATOM   7262 C  CG  . PHE B 1 444 ? -9.728  -18.402 15.921  1.00 15.30 ? 444 PHE B CG  1 
ATOM   7263 C  CD1 . PHE B 1 444 ? -8.390  -18.455 15.578  1.00 15.49 ? 444 PHE B CD1 1 
ATOM   7264 C  CD2 . PHE B 1 444 ? -10.677 -18.640 14.938  1.00 15.38 ? 444 PHE B CD2 1 
ATOM   7265 C  CE1 . PHE B 1 444 ? -8.002  -18.726 14.272  1.00 15.16 ? 444 PHE B CE1 1 
ATOM   7266 C  CE2 . PHE B 1 444 ? -10.297 -18.910 13.633  1.00 16.01 ? 444 PHE B CE2 1 
ATOM   7267 C  CZ  . PHE B 1 444 ? -8.949  -18.940 13.298  1.00 15.72 ? 444 PHE B CZ  1 
ATOM   7268 N  N   . VAL B 1 445 ? -7.987  -15.309 17.186  1.00 19.52 ? 445 VAL B N   1 
ATOM   7269 C  CA  . VAL B 1 445 ? -7.624  -14.066 16.455  1.00 20.10 ? 445 VAL B CA  1 
ATOM   7270 C  C   . VAL B 1 445 ? -6.765  -14.459 15.260  1.00 21.80 ? 445 VAL B C   1 
ATOM   7271 O  O   . VAL B 1 445 ? -6.152  -15.537 15.310  1.00 22.20 ? 445 VAL B O   1 
ATOM   7272 C  CB  . VAL B 1 445 ? -6.910  -13.074 17.381  1.00 20.44 ? 445 VAL B CB  1 
ATOM   7273 C  CG1 . VAL B 1 445 ? -7.912  -12.438 18.337  1.00 20.03 ? 445 VAL B CG1 1 
ATOM   7274 C  CG2 . VAL B 1 445 ? -5.749  -13.713 18.131  1.00 20.43 ? 445 VAL B CG2 1 
ATOM   7275 N  N   . VAL B 1 446 ? -6.800  -13.665 14.189  1.00 24.46 ? 446 VAL B N   1 
ATOM   7276 C  CA  . VAL B 1 446 ? -5.875  -13.809 13.025  1.00 26.53 ? 446 VAL B CA  1 
ATOM   7277 C  C   . VAL B 1 446 ? -5.539  -12.425 12.460  1.00 27.31 ? 446 VAL B C   1 
ATOM   7278 O  O   . VAL B 1 446 ? -6.222  -11.448 12.796  1.00 28.64 ? 446 VAL B O   1 
ATOM   7279 C  CB  . VAL B 1 446 ? -6.472  -14.682 11.912  1.00 28.56 ? 446 VAL B CB  1 
ATOM   7280 C  CG1 . VAL B 1 446 ? -6.868  -16.058 12.419  1.00 28.31 ? 446 VAL B CG1 1 
ATOM   7281 C  CG2 . VAL B 1 446 ? -7.624  -13.981 11.202  1.00 29.35 ? 446 VAL B CG2 1 
ATOM   7282 N  N   . LYS B 1 447 ? -4.505  -12.370 11.630  1.00 27.13 ? 447 LYS B N   1 
ATOM   7283 C  CA  . LYS B 1 447 ? -4.142  -11.196 10.815  1.00 27.89 ? 447 LYS B CA  1 
ATOM   7284 C  C   . LYS B 1 447 ? -4.526  -11.558 9.383   1.00 27.98 ? 447 LYS B C   1 
ATOM   7285 O  O   . LYS B 1 447 ? -4.410  -12.747 9.028   1.00 24.38 ? 447 LYS B O   1 
ATOM   7286 C  CB  . LYS B 1 447 ? -2.662  -10.847 10.999  1.00 32.62 ? 447 LYS B CB  1 
ATOM   7287 C  CG  . LYS B 1 447 ? -2.304  -10.191 12.328  1.00 33.20 ? 447 LYS B CG  1 
ATOM   7288 C  CD  . LYS B 1 447 ? -1.068  -9.337  12.277  1.00 36.65 ? 447 LYS B CD  1 
ATOM   7289 C  CE  . LYS B 1 447 ? -1.196  -8.081  13.116  1.00 42.28 ? 447 LYS B CE  1 
ATOM   7290 N  NZ  . LYS B 1 447 ? -0.835  -8.330  14.535  1.00 45.86 ? 447 LYS B NZ  1 
ATOM   7291 N  N   . ALA B 1 448 ? -5.040  -10.583 8.636   1.00 27.99 ? 448 ALA B N   1 
ATOM   7292 C  CA  . ALA B 1 448 ? -5.442  -10.752 7.231   1.00 29.21 ? 448 ALA B CA  1 
ATOM   7293 C  C   . ALA B 1 448 ? -4.665  -9.756  6.392   1.00 30.25 ? 448 ALA B C   1 
ATOM   7294 O  O   . ALA B 1 448 ? -4.897  -8.573  6.558   1.00 35.28 ? 448 ALA B O   1 
ATOM   7295 C  CB  . ALA B 1 448 ? -6.925  -10.563 7.071   1.00 28.08 ? 448 ALA B CB  1 
ATOM   7296 N  N   . LYS B 1 449 ? -3.818  -10.250 5.496   1.00 33.08 ? 449 LYS B N   1 
ATOM   7297 C  CA  . LYS B 1 449 ? -3.064  -9.418  4.520   1.00 33.81 ? 449 LYS B CA  1 
ATOM   7298 C  C   . LYS B 1 449 ? -3.921  -9.355  3.236   1.00 29.55 ? 449 LYS B C   1 
ATOM   7299 O  O   . LYS B 1 449 ? -4.184  -10.422 2.618   1.00 25.16 ? 449 LYS B O   1 
ATOM   7300 C  CB  . LYS B 1 449 ? -1.631  -9.955  4.345   1.00 38.28 ? 449 LYS B CB  1 
ATOM   7301 C  CG  . LYS B 1 449 ? -1.138  -10.922 5.434   1.00 44.93 ? 449 LYS B CG  1 
ATOM   7302 C  CD  . LYS B 1 449 ? 0.090   -10.506 6.248   1.00 49.39 ? 449 LYS B CD  1 
ATOM   7303 C  CE  . LYS B 1 449 ? -0.211  -9.616  7.441   1.00 51.68 ? 449 LYS B CE  1 
ATOM   7304 N  NZ  . LYS B 1 449 ? 0.070   -8.184  7.160   1.00 48.06 ? 449 LYS B NZ  1 
ATOM   7305 N  N   . SER B 1 450 ? -4.391  -8.158  2.878   1.00 25.12 ? 450 SER B N   1 
ATOM   7306 C  CA  . SER B 1 450 ? -5.182  -7.919  1.653   1.00 26.23 ? 450 SER B CA  1 
ATOM   7307 C  C   . SER B 1 450 ? -4.384  -8.373  0.415   1.00 27.54 ? 450 SER B C   1 
ATOM   7308 O  O   . SER B 1 450 ? -3.192  -8.075  0.324   1.00 26.50 ? 450 SER B O   1 
ATOM   7309 C  CB  . SER B 1 450 ? -5.595  -6.472  1.611   1.00 27.26 ? 450 SER B CB  1 
ATOM   7310 O  OG  . SER B 1 450 ? -6.183  -6.118  0.371   1.00 29.04 ? 450 SER B OG  1 
ATOM   7311 N  N   . LYS B 1 451 ? -5.010  -9.135  -0.484  1.00 28.99 ? 451 LYS B N   1 
ATOM   7312 C  CA  . LYS B 1 451 ? -4.493  -9.418  -1.851  1.00 31.12 ? 451 LYS B CA  1 
ATOM   7313 C  C   . LYS B 1 451 ? -4.840  -8.249  -2.780  1.00 32.65 ? 451 LYS B C   1 
ATOM   7314 O  O   . LYS B 1 451 ? -4.680  -8.396  -3.994  1.00 32.59 ? 451 LYS B O   1 
ATOM   7315 C  CB  . LYS B 1 451 ? -5.067  -10.732 -2.387  1.00 31.72 ? 451 LYS B CB  1 
ATOM   7316 C  CG  . LYS B 1 451 ? -4.580  -11.986 -1.676  1.00 34.31 ? 451 LYS B CG  1 
ATOM   7317 C  CD  . LYS B 1 451 ? -5.462  -13.171 -1.954  1.00 36.75 ? 451 LYS B CD  1 
ATOM   7318 C  CE  . LYS B 1 451 ? -4.941  -14.488 -1.423  1.00 39.06 ? 451 LYS B CE  1 
ATOM   7319 N  NZ  . LYS B 1 451 ? -3.769  -14.951 -2.205  1.00 42.23 ? 451 LYS B NZ  1 
ATOM   7320 N  N   . LYS B 1 452 ? -5.318  -7.138  -2.222  1.00 36.28 ? 452 LYS B N   1 
ATOM   7321 C  CA  . LYS B 1 452 ? -5.558  -5.865  -2.944  1.00 41.50 ? 452 LYS B CA  1 
ATOM   7322 C  C   . LYS B 1 452 ? -6.423  -6.132  -4.188  1.00 41.51 ? 452 LYS B C   1 
ATOM   7323 O  O   . LYS B 1 452 ? -6.004  -5.721  -5.284  1.00 36.76 ? 452 LYS B O   1 
ATOM   7324 C  CB  . LYS B 1 452 ? -4.205  -5.213  -3.263  1.00 46.82 ? 452 LYS B CB  1 
ATOM   7325 C  CG  . LYS B 1 452 ? -3.438  -4.676  -2.052  1.00 49.63 ? 452 LYS B CG  1 
ATOM   7326 C  CD  . LYS B 1 452 ? -4.102  -3.474  -1.372  1.00 56.20 ? 452 LYS B CD  1 
ATOM   7327 C  CE  . LYS B 1 452 ? -3.707  -3.280  0.084   1.00 60.43 ? 452 LYS B CE  1 
ATOM   7328 N  NZ  . LYS B 1 452 ? -4.853  -2.841  0.919   1.00 56.41 ? 452 LYS B NZ  1 
ATOM   7329 N  N   . ILE B 1 453 ? -7.579  -6.801  -4.020  1.00 42.09 ? 453 ILE B N   1 
ATOM   7330 C  CA  . ILE B 1 453 ? -8.572  -7.071  -5.110  1.00 39.77 ? 453 ILE B CA  1 
ATOM   7331 C  C   . ILE B 1 453 ? -9.798  -6.181  -4.875  1.00 41.46 ? 453 ILE B C   1 
ATOM   7332 O  O   . ILE B 1 453 ? -10.344 -6.119  -3.775  1.00 36.09 ? 453 ILE B O   1 
ATOM   7333 C  CB  . ILE B 1 453 ? -8.927  -8.573  -5.226  1.00 35.98 ? 453 ILE B CB  1 
ATOM   7334 C  CG1 . ILE B 1 453 ? -7.685  -9.461  -5.357  1.00 34.96 ? 453 ILE B CG1 1 
ATOM   7335 C  CG2 . ILE B 1 453 ? -9.890  -8.813  -6.378  1.00 34.20 ? 453 ILE B CG2 1 
ATOM   7336 C  CD1 . ILE B 1 453 ? -7.988  -10.935 -5.569  1.00 33.15 ? 453 ILE B CD1 1 
ATOM   7337 N  N   . PRO B 1 454 ? -10.253 -5.430  -5.905  1.00 48.66 ? 454 PRO B N   1 
ATOM   7338 C  CA  . PRO B 1 454 ? -11.385 -4.513  -5.747  1.00 51.98 ? 454 PRO B CA  1 
ATOM   7339 C  C   . PRO B 1 454 ? -12.758 -5.199  -5.619  1.00 52.98 ? 454 PRO B C   1 
ATOM   7340 O  O   . PRO B 1 454 ? -12.916 -6.383  -5.976  1.00 47.16 ? 454 PRO B O   1 
ATOM   7341 C  CB  . PRO B 1 454 ? -11.346 -3.645  -7.026  1.00 49.01 ? 454 PRO B CB  1 
ATOM   7342 C  CG  . PRO B 1 454 ? -10.654 -4.515  -8.057  1.00 47.59 ? 454 PRO B CG  1 
ATOM   7343 C  CD  . PRO B 1 454 ? -9.708  -5.411  -7.278  1.00 47.66 ? 454 PRO B CD  1 
ATOM   7344 N  N   . LEU B 1 455 ? -13.706 -4.428  -5.077  1.00 53.57 ? 455 LEU B N   1 
ATOM   7345 C  CA  . LEU B 1 455 ? -15.165 -4.719  -5.057  1.00 56.02 ? 455 LEU B CA  1 
ATOM   7346 C  C   . LEU B 1 455 ? -15.887 -3.725  -5.994  1.00 59.95 ? 455 LEU B C   1 
ATOM   7347 O  O   . LEU B 1 455 ? -15.222 -3.108  -6.846  1.00 56.15 ? 455 LEU B O   1 
ATOM   7348 C  CB  . LEU B 1 455 ? -15.653 -4.644  -3.604  1.00 49.61 ? 455 LEU B CB  1 
ATOM   7349 C  CG  . LEU B 1 455 ? -15.194 -5.796  -2.712  1.00 43.07 ? 455 LEU B CG  1 
ATOM   7350 C  CD1 . LEU B 1 455 ? -15.440 -5.490  -1.244  1.00 39.44 ? 455 LEU B CD1 1 
ATOM   7351 C  CD2 . LEU B 1 455 ? -15.894 -7.086  -3.115  1.00 44.27 ? 455 LEU B CD2 1 
ATOM   7352 O  OXT . LEU B 1 455 ? -17.123 -3.504  -5.975  1.00 59.77 ? 455 LEU B OXT 1 
HETATM 7353 C  CHA . HEM C 2 .   ? -6.535  27.942  11.756  1.00 19.38 ? 501 HEM A CHA 1 
HETATM 7354 C  CHB . HEM C 2 .   ? -11.411 27.745  11.379  1.00 17.95 ? 501 HEM A CHB 1 
HETATM 7355 C  CHC . HEM C 2 .   ? -10.898 23.319  9.324   1.00 19.44 ? 501 HEM A CHC 1 
HETATM 7356 C  CHD . HEM C 2 .   ? -6.223  23.440  10.166  1.00 18.97 ? 501 HEM A CHD 1 
HETATM 7357 C  C1A . HEM C 2 .   ? -7.893  28.250  11.801  1.00 18.16 ? 501 HEM A C1A 1 
HETATM 7358 C  C2A . HEM C 2 .   ? -8.388  29.473  12.297  1.00 18.00 ? 501 HEM A C2A 1 
HETATM 7359 C  C3A . HEM C 2 .   ? -9.766  29.424  12.208  1.00 18.17 ? 501 HEM A C3A 1 
HETATM 7360 C  C4A . HEM C 2 .   ? -10.123 28.189  11.648  1.00 17.17 ? 501 HEM A C4A 1 
HETATM 7361 C  CMA . HEM C 2 .   ? -10.732 30.523  12.638  1.00 19.20 ? 501 HEM A CMA 1 
HETATM 7362 C  CAA . HEM C 2 .   ? -7.522  30.595  12.836  1.00 16.72 ? 501 HEM A CAA 1 
HETATM 7363 C  CBA . HEM C 2 .   ? -7.238  30.416  14.346  1.00 16.86 ? 501 HEM A CBA 1 
HETATM 7364 C  CGA . HEM C 2 .   ? -6.601  31.639  15.034  1.00 16.85 ? 501 HEM A CGA 1 
HETATM 7365 O  O1A . HEM C 2 .   ? -6.269  31.458  16.231  1.00 15.94 ? 501 HEM A O1A 1 
HETATM 7366 O  O2A . HEM C 2 .   ? -6.401  32.782  14.433  1.00 15.47 ? 501 HEM A O2A 1 
HETATM 7367 C  C1B . HEM C 2 .   ? -11.703 26.510  10.753  1.00 18.07 ? 501 HEM A C1B 1 
HETATM 7368 C  C2B . HEM C 2 .   ? -12.999 26.082  10.351  1.00 18.64 ? 501 HEM A C2B 1 
HETATM 7369 C  C3B . HEM C 2 .   ? -12.844 24.823  9.774   1.00 18.82 ? 501 HEM A C3B 1 
HETATM 7370 C  C4B . HEM C 2 .   ? -11.419 24.517  9.849   1.00 18.40 ? 501 HEM A C4B 1 
HETATM 7371 C  CMB . HEM C 2 .   ? -14.275 26.869  10.554  1.00 18.22 ? 501 HEM A CMB 1 
HETATM 7372 C  CAB . HEM C 2 .   ? -13.763 23.867  9.104   1.00 19.15 ? 501 HEM A CAB 1 
HETATM 7373 C  CBB . HEM C 2 .   ? -14.987 24.225  8.780   1.00 20.36 ? 501 HEM A CBB 1 
HETATM 7374 C  C1C . HEM C 2 .   ? -9.582  22.929  9.366   1.00 19.88 ? 501 HEM A C1C 1 
HETATM 7375 C  C2C . HEM C 2 .   ? -9.072  21.679  8.974   1.00 21.26 ? 501 HEM A C2C 1 
HETATM 7376 C  C3C . HEM C 2 .   ? -7.705  21.766  9.199   1.00 20.80 ? 501 HEM A C3C 1 
HETATM 7377 C  C4C . HEM C 2 .   ? -7.459  23.029  9.783   1.00 19.54 ? 501 HEM A C4C 1 
HETATM 7378 C  CMC . HEM C 2 .   ? -9.832  20.501  8.353   1.00 22.42 ? 501 HEM A CMC 1 
HETATM 7379 C  CAC . HEM C 2 .   ? -6.644  20.749  9.024   1.00 23.72 ? 501 HEM A CAC 1 
HETATM 7380 C  CBC . HEM C 2 .   ? -6.836  19.463  8.722   1.00 25.53 ? 501 HEM A CBC 1 
HETATM 7381 C  C1D . HEM C 2 .   ? -5.967  24.700  10.677  1.00 18.12 ? 501 HEM A C1D 1 
HETATM 7382 C  C2D . HEM C 2 .   ? -4.583  25.099  10.907  1.00 18.05 ? 501 HEM A C2D 1 
HETATM 7383 C  C3D . HEM C 2 .   ? -4.651  26.353  11.347  1.00 19.48 ? 501 HEM A C3D 1 
HETATM 7384 C  C4D . HEM C 2 .   ? -6.083  26.693  11.353  1.00 18.62 ? 501 HEM A C4D 1 
HETATM 7385 C  CMD . HEM C 2 .   ? -3.333  24.268  10.728  1.00 17.83 ? 501 HEM A CMD 1 
HETATM 7386 C  CAD . HEM C 2 .   ? -3.463  27.222  11.749  1.00 21.32 ? 501 HEM A CAD 1 
HETATM 7387 C  CBD . HEM C 2 .   ? -2.984  27.936  10.474  1.00 23.42 ? 501 HEM A CBD 1 
HETATM 7388 C  CGD . HEM C 2 .   ? -1.817  28.880  10.676  1.00 24.65 ? 501 HEM A CGD 1 
HETATM 7389 O  O1D . HEM C 2 .   ? -1.864  29.823  11.485  1.00 24.18 ? 501 HEM A O1D 1 
HETATM 7390 O  O2D . HEM C 2 .   ? -0.792  28.742  9.967   1.00 29.32 ? 501 HEM A O2D 1 
HETATM 7391 N  NA  . HEM C 2 .   ? -8.972  27.471  11.430  1.00 17.04 ? 501 HEM A NA  1 
HETATM 7392 N  NB  . HEM C 2 .   ? -10.822 25.550  10.440  1.00 18.16 ? 501 HEM A NB  1 
HETATM 7393 N  NC  . HEM C 2 .   ? -8.607  23.731  9.883   1.00 18.64 ? 501 HEM A NC  1 
HETATM 7394 N  ND  . HEM C 2 .   ? -6.837  25.673  10.932  1.00 17.85 ? 501 HEM A ND  1 
HETATM 7395 FE FE  . HEM C 2 .   ? -8.751  25.639  10.731  1.00 15.92 ? 501 HEM A FE  1 
HETATM 7396 N  N   . HL0 D 3 .   ? -11.879 32.300  26.179  1.00 47.18 ? 502 HL0 A N   1 
HETATM 7397 C  C1  . HL0 D 3 .   ? -10.321 28.344  16.989  1.00 61.59 ? 502 HL0 A C1  1 
HETATM 7398 O  O1  . HL0 D 3 .   ? -12.293 33.989  24.719  1.00 31.25 ? 502 HL0 A O1  1 
HETATM 7399 C  C2  . HL0 D 3 .   ? -11.263 27.746  18.011  1.00 61.64 ? 502 HL0 A C2  1 
HETATM 7400 O  O2  . HL0 D 3 .   ? -8.597  32.867  27.591  1.00 51.25 ? 502 HL0 A O2  1 
HETATM 7401 C  C3  . HL0 D 3 .   ? -10.959 28.136  19.445  1.00 61.71 ? 502 HL0 A C3  1 
HETATM 7402 O  O3  . HL0 D 3 .   ? -9.016  31.681  25.771  1.00 53.72 ? 502 HL0 A O3  1 
HETATM 7403 C  C4  . HL0 D 3 .   ? -11.553 29.455  19.893  1.00 60.20 ? 502 HL0 A C4  1 
HETATM 7404 C  C5  . HL0 D 3 .   ? -10.699 30.216  20.884  1.00 58.95 ? 502 HL0 A C5  1 
HETATM 7405 C  C6  . HL0 D 3 .   ? -10.949 29.822  22.324  1.00 59.99 ? 502 HL0 A C6  1 
HETATM 7406 C  C7  . HL0 D 3 .   ? -11.410 30.953  23.231  1.00 55.67 ? 502 HL0 A C7  1 
HETATM 7407 C  C8  . HL0 D 3 .   ? -12.883 31.352  23.095  1.00 50.58 ? 502 HL0 A C8  1 
HETATM 7408 C  C9  . HL0 D 3 .   ? -13.470 31.939  24.350  1.00 43.52 ? 502 HL0 A C9  1 
HETATM 7409 C  C10 . HL0 D 3 .   ? -12.504 32.840  25.101  1.00 42.70 ? 502 HL0 A C10 1 
HETATM 7410 C  C11 . HL0 D 3 .   ? -10.801 32.970  26.880  1.00 50.09 ? 502 HL0 A C11 1 
HETATM 7411 C  C12 . HL0 D 3 .   ? -10.849 32.916  28.391  1.00 47.36 ? 502 HL0 A C12 1 
HETATM 7412 C  C13 . HL0 D 3 .   ? -9.408  33.257  28.741  1.00 51.23 ? 502 HL0 A C13 1 
HETATM 7413 C  C14 . HL0 D 3 .   ? -9.405  32.409  26.637  1.00 50.20 ? 502 HL0 A C14 1 
HETATM 7414 S  S   . DMS E 4 .   ? -8.755  25.030  13.027  1.00 25.32 ? 503 DMS A S   1 
HETATM 7415 O  O   . DMS E 4 .   ? -9.608  23.918  12.600  1.00 24.56 ? 503 DMS A O   1 
HETATM 7416 C  C1  . DMS E 4 .   ? -9.600  25.978  14.264  1.00 25.74 ? 503 DMS A C1  1 
HETATM 7417 C  C2  . DMS E 4 .   ? -7.522  24.342  14.065  1.00 24.94 ? 503 DMS A C2  1 
HETATM 7418 C  C1  . GOL F 5 .   ? -38.625 26.830  -2.877  1.00 39.18 ? 504 GOL A C1  1 
HETATM 7419 O  O1  . GOL F 5 .   ? -37.412 26.334  -3.417  1.00 39.21 ? 504 GOL A O1  1 
HETATM 7420 C  C2  . GOL F 5 .   ? -39.614 25.708  -2.689  1.00 42.22 ? 504 GOL A C2  1 
HETATM 7421 O  O2  . GOL F 5 .   ? -39.569 25.250  -1.340  1.00 37.72 ? 504 GOL A O2  1 
HETATM 7422 C  C3  . GOL F 5 .   ? -41.033 26.097  -3.037  1.00 46.35 ? 504 GOL A C3  1 
HETATM 7423 O  O3  . GOL F 5 .   ? -41.918 24.996  -2.839  1.00 50.99 ? 504 GOL A O3  1 
HETATM 7424 C  C1  . GOL G 5 .   ? -27.546 27.046  -10.114 1.00 28.45 ? 505 GOL A C1  1 
HETATM 7425 O  O1  . GOL G 5 .   ? -26.908 28.264  -10.487 1.00 26.81 ? 505 GOL A O1  1 
HETATM 7426 C  C2  . GOL G 5 .   ? -26.735 26.310  -9.064  1.00 30.05 ? 505 GOL A C2  1 
HETATM 7427 O  O2  . GOL G 5 .   ? -27.563 25.394  -8.328  1.00 26.68 ? 505 GOL A O2  1 
HETATM 7428 C  C3  . GOL G 5 .   ? -25.523 25.613  -9.661  1.00 31.10 ? 505 GOL A C3  1 
HETATM 7429 O  O3  . GOL G 5 .   ? -25.876 24.709  -10.709 1.00 31.68 ? 505 GOL A O3  1 
HETATM 7430 C  CHA . HEM H 2 .   ? -32.576 -28.123 13.324  1.00 16.12 ? 501 HEM B CHA 1 
HETATM 7431 C  CHB . HEM H 2 .   ? -27.793 -27.825 12.835  1.00 16.23 ? 501 HEM B CHB 1 
HETATM 7432 C  CHC . HEM H 2 .   ? -28.189 -23.553 10.627  1.00 16.26 ? 501 HEM B CHC 1 
HETATM 7433 C  CHD . HEM H 2 .   ? -32.952 -23.700 11.304  1.00 17.69 ? 501 HEM B CHD 1 
HETATM 7434 C  C1A . HEM H 2 .   ? -31.253 -28.406 13.368  1.00 15.98 ? 501 HEM B C1A 1 
HETATM 7435 C  C2A . HEM H 2 .   ? -30.730 -29.579 13.973  1.00 16.30 ? 501 HEM B C2A 1 
HETATM 7436 C  C3A . HEM H 2 .   ? -29.354 -29.484 13.843  1.00 16.21 ? 501 HEM B C3A 1 
HETATM 7437 C  C4A . HEM H 2 .   ? -29.057 -28.270 13.152  1.00 15.66 ? 501 HEM B C4A 1 
HETATM 7438 C  CMA . HEM H 2 .   ? -28.304 -30.480 14.336  1.00 15.30 ? 501 HEM B CMA 1 
HETATM 7439 C  CAA . HEM H 2 .   ? -31.513 -30.709 14.652  1.00 16.23 ? 501 HEM B CAA 1 
HETATM 7440 C  CBA . HEM H 2 .   ? -31.917 -30.336 16.083  1.00 16.46 ? 501 HEM B CBA 1 
HETATM 7441 C  CGA . HEM H 2 .   ? -32.491 -31.504 16.874  1.00 17.27 ? 501 HEM B CGA 1 
HETATM 7442 O  O1A . HEM H 2 .   ? -32.795 -31.229 18.056  1.00 17.63 ? 501 HEM B O1A 1 
HETATM 7443 O  O2A . HEM H 2 .   ? -32.672 -32.707 16.430  1.00 16.85 ? 501 HEM B O2A 1 
HETATM 7444 C  C1B . HEM H 2 .   ? -27.479 -26.627 12.176  1.00 15.83 ? 501 HEM B C1B 1 
HETATM 7445 C  C2B . HEM H 2 .   ? -26.143 -26.232 11.822  1.00 16.69 ? 501 HEM B C2B 1 
HETATM 7446 C  C3B . HEM H 2 .   ? -26.241 -25.016 11.204  1.00 16.87 ? 501 HEM B C3B 1 
HETATM 7447 C  C4B . HEM H 2 .   ? -27.689 -24.712 11.203  1.00 16.04 ? 501 HEM B C4B 1 
HETATM 7448 C  CMB . HEM H 2 .   ? -24.887 -27.039 12.081  1.00 16.80 ? 501 HEM B CMB 1 
HETATM 7449 C  CAB . HEM H 2 .   ? -25.246 -24.152 10.532  1.00 17.27 ? 501 HEM B CAB 1 
HETATM 7450 C  CBB . HEM H 2 .   ? -24.083 -24.629 10.084  1.00 18.01 ? 501 HEM B CBB 1 
HETATM 7451 C  C1C . HEM H 2 .   ? -29.515 -23.213 10.597  1.00 16.38 ? 501 HEM B C1C 1 
HETATM 7452 C  C2C . HEM H 2 .   ? -30.008 -22.067 9.983   1.00 17.18 ? 501 HEM B C2C 1 
HETATM 7453 C  C3C . HEM H 2 .   ? -31.388 -22.102 10.173  1.00 17.73 ? 501 HEM B C3C 1 
HETATM 7454 C  C4C . HEM H 2 .   ? -31.688 -23.292 10.898  1.00 17.31 ? 501 HEM B C4C 1 
HETATM 7455 C  CMC . HEM H 2 .   ? -29.155 -21.060 9.252   1.00 16.33 ? 501 HEM B CMC 1 
HETATM 7456 C  CAC . HEM H 2 .   ? -32.408 -21.176 9.667   1.00 20.13 ? 501 HEM B CAC 1 
HETATM 7457 C  CBC . HEM H 2 .   ? -32.170 -20.294 8.687   1.00 22.46 ? 501 HEM B CBC 1 
HETATM 7458 C  C1D . HEM H 2 .   ? -33.175 -24.930 11.943  1.00 17.52 ? 501 HEM B C1D 1 
HETATM 7459 C  C2D . HEM H 2 .   ? -34.541 -25.373 12.276  1.00 18.77 ? 501 HEM B C2D 1 
HETATM 7460 C  C3D . HEM H 2 .   ? -34.444 -26.589 12.828  1.00 17.00 ? 501 HEM B C3D 1 
HETATM 7461 C  C4D . HEM H 2 .   ? -33.013 -26.916 12.827  1.00 15.93 ? 501 HEM B C4D 1 
HETATM 7462 C  CMD . HEM H 2 .   ? -35.837 -24.641 12.069  1.00 19.09 ? 501 HEM B CMD 1 
HETATM 7463 C  CAD . HEM H 2 .   ? -35.642 -27.380 13.279  1.00 17.13 ? 501 HEM B CAD 1 
HETATM 7464 C  CBD . HEM H 2 .   ? -36.037 -28.259 12.073  1.00 16.28 ? 501 HEM B CBD 1 
HETATM 7465 C  CGD . HEM H 2 .   ? -37.313 -29.057 12.280  1.00 16.18 ? 501 HEM B CGD 1 
HETATM 7466 O  O1D . HEM H 2 .   ? -37.434 -29.838 13.243  1.00 15.93 ? 501 HEM B O1D 1 
HETATM 7467 O  O2D . HEM H 2 .   ? -38.247 -28.985 11.455  1.00 14.87 ? 501 HEM B O2D 1 
HETATM 7468 N  NA  . HEM H 2 .   ? -30.216 -27.610 12.866  1.00 15.68 ? 501 HEM B NA  1 
HETATM 7469 N  NB  . HEM H 2 .   ? -28.340 -25.686 11.827  1.00 15.60 ? 501 HEM B NB  1 
HETATM 7470 N  NC  . HEM H 2 .   ? -30.518 -23.948 11.134  1.00 15.70 ? 501 HEM B NC  1 
HETATM 7471 N  ND  . HEM H 2 .   ? -32.298 -25.901 12.294  1.00 16.46 ? 501 HEM B ND  1 
HETATM 7472 FE FE  . HEM H 2 .   ? -30.421 -25.803 12.052  1.00 14.40 ? 501 HEM B FE  1 
HETATM 7473 N  N   . HL0 I 3 .   ? -27.255 -31.739 27.986  1.00 28.23 ? 502 HL0 B N   1 
HETATM 7474 C  C1  . HL0 I 3 .   ? -29.002 -28.158 18.550  1.00 41.36 ? 502 HL0 B C1  1 
HETATM 7475 O  O1  . HL0 I 3 .   ? -26.538 -33.340 26.525  1.00 25.53 ? 502 HL0 B O1  1 
HETATM 7476 C  C2  . HL0 I 3 .   ? -27.880 -27.606 19.404  1.00 43.63 ? 502 HL0 B C2  1 
HETATM 7477 O  O2  . HL0 I 3 .   ? -30.395 -32.347 29.460  1.00 30.06 ? 502 HL0 B O2  1 
HETATM 7478 C  C3  . HL0 I 3 .   ? -27.701 -28.324 20.721  1.00 45.56 ? 502 HL0 B C3  1 
HETATM 7479 O  O3  . HL0 I 3 .   ? -30.077 -31.653 27.363  1.00 35.53 ? 502 HL0 B O3  1 
HETATM 7480 C  C4  . HL0 I 3 .   ? -28.966 -28.670 21.476  1.00 44.75 ? 502 HL0 B C4  1 
HETATM 7481 C  C5  . HL0 I 3 .   ? -28.746 -28.899 22.957  1.00 46.80 ? 502 HL0 B C5  1 
HETATM 7482 C  C6  . HL0 I 3 .   ? -27.798 -30.035 23.280  1.00 44.42 ? 502 HL0 B C6  1 
HETATM 7483 C  C7  . HL0 I 3 .   ? -27.357 -30.115 24.727  1.00 40.49 ? 502 HL0 B C7  1 
HETATM 7484 C  C8  . HL0 I 3 .   ? -26.018 -30.814 24.889  1.00 38.12 ? 502 HL0 B C8  1 
HETATM 7485 C  C9  . HL0 I 3 .   ? -25.664 -31.123 26.291  1.00 33.34 ? 502 HL0 B C9  1 
HETATM 7486 C  C10 . HL0 I 3 .   ? -26.534 -32.169 26.925  1.00 30.55 ? 502 HL0 B C10 1 
HETATM 7487 C  C11 . HL0 I 3 .   ? -28.226 -32.578 28.642  1.00 31.21 ? 502 HL0 B C11 1 
HETATM 7488 C  C12 . HL0 I 3 .   ? -28.186 -32.659 30.162  1.00 31.06 ? 502 HL0 B C12 1 
HETATM 7489 C  C13 . HL0 I 3 .   ? -29.608 -33.076 30.443  1.00 30.49 ? 502 HL0 B C13 1 
HETATM 7490 C  C14 . HL0 I 3 .   ? -29.643 -32.114 28.381  1.00 30.75 ? 502 HL0 B C14 1 
HETATM 7491 S  S   . DMS J 4 .   ? -30.438 -25.154 14.438  1.00 27.25 ? 503 DMS B S   1 
HETATM 7492 O  O   . DMS J 4 .   ? -29.590 -24.073 13.933  1.00 25.89 ? 503 DMS B O   1 
HETATM 7493 C  C1  . DMS J 4 .   ? -29.824 -25.624 16.031  1.00 26.40 ? 503 DMS B C1  1 
HETATM 7494 C  C2  . DMS J 4 .   ? -31.942 -24.416 15.005  1.00 28.86 ? 503 DMS B C2  1 
HETATM 7495 C  C1  . GOL K 5 .   ? -29.661 -33.986 6.413   1.00 28.71 ? 504 GOL B C1  1 
HETATM 7496 O  O1  . GOL K 5 .   ? -28.325 -33.527 6.587   1.00 25.89 ? 504 GOL B O1  1 
HETATM 7497 C  C2  . GOL K 5 .   ? -29.766 -35.496 6.585   1.00 31.36 ? 504 GOL B C2  1 
HETATM 7498 O  O2  . GOL K 5 .   ? -28.912 -35.935 7.648   1.00 31.94 ? 504 GOL B O2  1 
HETATM 7499 C  C3  . GOL K 5 .   ? -31.181 -35.988 6.851   1.00 28.38 ? 504 GOL B C3  1 
HETATM 7500 O  O3  . GOL K 5 .   ? -31.176 -37.089 7.765   1.00 27.39 ? 504 GOL B O3  1 
HETATM 7501 C  C1  . GOL L 5 .   ? -22.754 -24.527 30.639  1.00 21.48 ? 505 GOL B C1  1 
HETATM 7502 O  O1  . GOL L 5 .   ? -22.405 -23.345 31.355  1.00 19.72 ? 505 GOL B O1  1 
HETATM 7503 C  C2  . GOL L 5 .   ? -22.949 -24.228 29.175  1.00 22.10 ? 505 GOL B C2  1 
HETATM 7504 O  O2  . GOL L 5 .   ? -21.939 -23.306 28.777  1.00 25.00 ? 505 GOL B O2  1 
HETATM 7505 C  C3  . GOL L 5 .   ? -22.902 -25.452 28.291  1.00 21.20 ? 505 GOL B C3  1 
HETATM 7506 O  O3  . GOL L 5 .   ? -21.586 -25.984 28.219  1.00 20.07 ? 505 GOL B O3  1 
HETATM 7507 C  C1  . GOL M 5 .   ? -34.972 -43.079 6.838   1.00 30.97 ? 506 GOL B C1  1 
HETATM 7508 O  O1  . GOL M 5 .   ? -35.520 -42.135 5.914   1.00 31.03 ? 506 GOL B O1  1 
HETATM 7509 C  C2  . GOL M 5 .   ? -35.514 -42.864 8.243   1.00 31.43 ? 506 GOL B C2  1 
HETATM 7510 O  O2  . GOL M 5 .   ? -35.218 -43.991 9.066   1.00 29.13 ? 506 GOL B O2  1 
HETATM 7511 C  C3  . GOL M 5 .   ? -35.020 -41.597 8.916   1.00 30.95 ? 506 GOL B C3  1 
HETATM 7512 O  O3  . GOL M 5 .   ? -33.652 -41.322 8.620   1.00 38.21 ? 506 GOL B O3  1 
HETATM 7513 C  C1  . GOL N 5 .   ? -23.019 -11.576 20.300  1.00 38.25 ? 507 GOL B C1  1 
HETATM 7514 O  O1  . GOL N 5 .   ? -23.749 -10.677 19.464  1.00 38.21 ? 507 GOL B O1  1 
HETATM 7515 C  C2  . GOL N 5 .   ? -23.519 -11.598 21.738  1.00 39.83 ? 507 GOL B C2  1 
HETATM 7516 O  O2  . GOL N 5 .   ? -22.634 -12.403 22.524  1.00 34.89 ? 507 GOL B O2  1 
HETATM 7517 C  C3  . GOL N 5 .   ? -23.667 -10.219 22.376  1.00 40.25 ? 507 GOL B C3  1 
HETATM 7518 O  O3  . GOL N 5 .   ? -24.123 -10.291 23.728  1.00 41.07 ? 507 GOL B O3  1 
HETATM 7519 C  C1  . GOL O 5 .   ? -34.236 -37.567 14.867  1.00 27.60 ? 508 GOL B C1  1 
HETATM 7520 O  O1  . GOL O 5 .   ? -33.877 -36.185 14.709  1.00 25.22 ? 508 GOL B O1  1 
HETATM 7521 C  C2  . GOL O 5 .   ? -35.111 -38.155 13.759  1.00 25.64 ? 508 GOL B C2  1 
HETATM 7522 O  O2  . GOL O 5 .   ? -35.309 -39.554 13.942  1.00 26.77 ? 508 GOL B O2  1 
HETATM 7523 C  C3  . GOL O 5 .   ? -36.480 -37.524 13.614  1.00 22.53 ? 508 GOL B C3  1 
HETATM 7524 O  O3  . GOL O 5 .   ? -36.632 -36.985 12.303  1.00 20.34 ? 508 GOL B O3  1 
HETATM 7525 O  O   . HOH P 6 .   ? -8.451  12.207  -5.878  1.00 25.31 ? 601 HOH A O   1 
HETATM 7526 O  O   . HOH P 6 .   ? -20.687 23.228  26.258  1.00 21.73 ? 602 HOH A O   1 
HETATM 7527 O  O   . HOH P 6 .   ? -18.853 48.361  23.665  1.00 21.01 ? 603 HOH A O   1 
HETATM 7528 O  O   . HOH P 6 .   ? -24.939 6.329   15.034  1.00 28.18 ? 604 HOH A O   1 
HETATM 7529 O  O   . HOH P 6 .   ? 2.830   52.253  29.294  1.00 20.31 ? 605 HOH A O   1 
HETATM 7530 O  O   . HOH P 6 .   ? -34.807 -0.597  15.067  1.00 23.59 ? 606 HOH A O   1 
HETATM 7531 O  O   . HOH P 6 .   ? -11.474 5.286   8.847   1.00 18.76 ? 607 HOH A O   1 
HETATM 7532 O  O   . HOH P 6 .   ? -37.515 22.136  -6.376  1.00 22.57 ? 608 HOH A O   1 
HETATM 7533 O  O   . HOH P 6 .   ? -20.873 28.295  -3.487  1.00 25.39 ? 609 HOH A O   1 
HETATM 7534 O  O   . HOH P 6 .   ? -18.273 2.131   7.533   1.00 15.84 ? 610 HOH A O   1 
HETATM 7535 O  O   . HOH P 6 .   ? -7.153  32.334  34.341  1.00 30.58 ? 611 HOH A O   1 
HETATM 7536 O  O   . HOH P 6 .   ? 9.979   29.434  20.063  1.00 19.63 ? 612 HOH A O   1 
HETATM 7537 O  O   . HOH P 6 .   ? -19.439 47.850  12.257  1.00 17.29 ? 613 HOH A O   1 
HETATM 7538 O  O   . HOH P 6 .   ? 0.462   45.194  26.740  1.00 20.31 ? 614 HOH A O   1 
HETATM 7539 O  O   . HOH P 6 .   ? -23.855 9.678   -5.032  1.00 16.53 ? 615 HOH A O   1 
HETATM 7540 O  O   . HOH P 6 .   ? 3.341   51.018  27.295  1.00 25.33 ? 616 HOH A O   1 
HETATM 7541 O  O   . HOH P 6 .   ? -18.174 -2.743  6.183   1.00 15.03 ? 617 HOH A O   1 
HETATM 7542 O  O   . HOH P 6 .   ? 1.977   35.401  16.613  1.00 19.16 ? 618 HOH A O   1 
HETATM 7543 O  O   . HOH P 6 .   ? -26.938 26.524  23.824  1.00 14.87 ? 619 HOH A O   1 
HETATM 7544 O  O   . HOH P 6 .   ? -11.578 15.967  8.041   1.00 24.50 ? 620 HOH A O   1 
HETATM 7545 O  O   . HOH P 6 .   ? -11.751 34.222  7.475   1.00 11.71 ? 621 HOH A O   1 
HETATM 7546 O  O   . HOH P 6 .   ? -32.159 24.691  -6.486  1.00 9.64  ? 622 HOH A O   1 
HETATM 7547 O  O   . HOH P 6 .   ? -3.855  30.497  12.971  1.00 12.86 ? 623 HOH A O   1 
HETATM 7548 O  O   . HOH P 6 .   ? -6.416  33.915  12.115  1.00 10.99 ? 624 HOH A O   1 
HETATM 7549 O  O   . HOH P 6 .   ? -17.784 42.972  21.913  1.00 12.02 ? 625 HOH A O   1 
HETATM 7550 O  O   . HOH P 6 .   ? -16.734 43.791  42.283  1.00 4.74  ? 626 HOH A O   1 
HETATM 7551 O  O   . HOH P 6 .   ? -14.975 11.548  19.222  1.00 30.78 ? 627 HOH A O   1 
HETATM 7552 O  O   . HOH P 6 .   ? -5.829  34.772  36.018  1.00 28.61 ? 628 HOH A O   1 
HETATM 7553 O  O   . HOH P 6 .   ? -15.531 29.589  12.173  1.00 24.75 ? 629 HOH A O   1 
HETATM 7554 O  O   . HOH P 6 .   ? 3.798   2.296   6.419   1.00 38.25 ? 630 HOH A O   1 
HETATM 7555 O  O   . HOH P 6 .   ? -16.945 6.189   16.723  1.00 26.10 ? 631 HOH A O   1 
HETATM 7556 O  O   . HOH P 6 .   ? -7.062  23.867  2.711   1.00 13.33 ? 632 HOH A O   1 
HETATM 7557 O  O   . HOH P 6 .   ? -8.559  51.111  25.329  1.00 20.30 ? 633 HOH A O   1 
HETATM 7558 O  O   . HOH P 6 .   ? -36.235 24.667  -5.117  1.00 26.10 ? 634 HOH A O   1 
HETATM 7559 O  O   . HOH P 6 .   ? -34.004 25.403  17.745  1.00 22.85 ? 635 HOH A O   1 
HETATM 7560 O  O   . HOH P 6 .   ? -10.552 18.669  32.801  1.00 34.00 ? 636 HOH A O   1 
HETATM 7561 O  O   . HOH P 6 .   ? -9.265  54.467  13.450  1.00 30.03 ? 637 HOH A O   1 
HETATM 7562 O  O   . HOH P 6 .   ? -15.057 28.894  30.033  1.00 20.52 ? 638 HOH A O   1 
HETATM 7563 O  O   . HOH P 6 .   ? 12.335  13.886  9.172   1.00 31.43 ? 639 HOH A O   1 
HETATM 7564 O  O   . HOH P 6 .   ? -19.748 41.523  9.543   1.00 17.83 ? 640 HOH A O   1 
HETATM 7565 O  O   . HOH P 6 .   ? -0.605  23.912  16.437  1.00 19.68 ? 641 HOH A O   1 
HETATM 7566 O  O   . HOH P 6 .   ? -24.934 15.621  20.798  1.00 19.64 ? 642 HOH A O   1 
HETATM 7567 O  O   . HOH P 6 .   ? -16.310 3.696   0.779   1.00 18.35 ? 643 HOH A O   1 
HETATM 7568 O  O   . HOH P 6 .   ? -10.997 51.457  29.313  1.00 9.03  ? 644 HOH A O   1 
HETATM 7569 O  O   . HOH P 6 .   ? -2.202  37.383  10.118  1.00 26.63 ? 645 HOH A O   1 
HETATM 7570 O  O   . HOH P 6 .   ? -26.109 1.331   9.629   1.00 21.25 ? 646 HOH A O   1 
HETATM 7571 O  O   . HOH P 6 .   ? -3.233  40.533  29.090  1.00 14.07 ? 647 HOH A O   1 
HETATM 7572 O  O   . HOH P 6 .   ? -5.756  33.137  18.320  1.00 18.60 ? 648 HOH A O   1 
HETATM 7573 O  O   . HOH P 6 .   ? 4.556   25.180  12.685  1.00 22.04 ? 649 HOH A O   1 
HETATM 7574 O  O   . HOH P 6 .   ? -7.398  54.841  15.086  1.00 33.12 ? 650 HOH A O   1 
HETATM 7575 O  O   . HOH P 6 .   ? -35.245 6.397   9.824   1.00 29.11 ? 651 HOH A O   1 
HETATM 7576 O  O   . HOH P 6 .   ? 6.097   27.242  -0.600  1.00 39.41 ? 652 HOH A O   1 
HETATM 7577 O  O   . HOH P 6 .   ? -31.811 33.921  -6.359  1.00 13.14 ? 653 HOH A O   1 
HETATM 7578 O  O   . HOH P 6 .   ? -0.046  48.247  16.839  1.00 29.23 ? 654 HOH A O   1 
HETATM 7579 O  O   . HOH P 6 .   ? -3.065  29.803  5.873   1.00 15.84 ? 655 HOH A O   1 
HETATM 7580 O  O   . HOH P 6 .   ? -2.879  26.681  0.182   1.00 19.29 ? 656 HOH A O   1 
HETATM 7581 O  O   . HOH P 6 .   ? -5.317  35.157  15.424  1.00 19.02 ? 657 HOH A O   1 
HETATM 7582 O  O   . HOH P 6 .   ? -8.337  2.347   13.998  1.00 23.24 ? 658 HOH A O   1 
HETATM 7583 O  O   . HOH P 6 .   ? -26.619 8.026   14.258  1.00 14.00 ? 659 HOH A O   1 
HETATM 7584 O  O   . HOH P 6 .   ? -33.828 30.825  1.097   1.00 26.76 ? 660 HOH A O   1 
HETATM 7585 O  O   . HOH P 6 .   ? -12.221 3.387   7.072   1.00 12.16 ? 661 HOH A O   1 
HETATM 7586 O  O   . HOH P 6 .   ? -32.261 20.039  22.638  1.00 22.33 ? 662 HOH A O   1 
HETATM 7587 O  O   . HOH P 6 .   ? -31.512 13.124  -5.481  1.00 24.98 ? 663 HOH A O   1 
HETATM 7588 O  O   . HOH P 6 .   ? 0.973   39.664  24.472  1.00 29.25 ? 664 HOH A O   1 
HETATM 7589 O  O   . HOH P 6 .   ? -32.146 15.364  -3.794  1.00 21.22 ? 665 HOH A O   1 
HETATM 7590 O  O   . HOH P 6 .   ? -9.411  7.378   9.282   1.00 15.60 ? 666 HOH A O   1 
HETATM 7591 O  O   . HOH P 6 .   ? 3.164   25.741  28.701  1.00 35.16 ? 667 HOH A O   1 
HETATM 7592 O  O   . HOH P 6 .   ? -22.310 12.610  -9.144  1.00 18.96 ? 668 HOH A O   1 
HETATM 7593 O  O   . HOH P 6 .   ? -12.483 23.508  -1.757  1.00 20.49 ? 669 HOH A O   1 
HETATM 7594 O  O   . HOH P 6 .   ? -7.031  16.000  32.642  1.00 28.12 ? 670 HOH A O   1 
HETATM 7595 O  O   . HOH P 6 .   ? -25.844 45.021  14.796  1.00 31.02 ? 671 HOH A O   1 
HETATM 7596 O  O   . HOH P 6 .   ? 1.203   5.389   25.825  1.00 34.21 ? 672 HOH A O   1 
HETATM 7597 O  O   . HOH P 6 .   ? 10.657  27.776  15.888  1.00 24.01 ? 673 HOH A O   1 
HETATM 7598 O  O   . HOH P 6 .   ? -18.403 21.017  20.555  1.00 20.66 ? 674 HOH A O   1 
HETATM 7599 O  O   . HOH P 6 .   ? 5.051   51.215  20.582  1.00 15.84 ? 675 HOH A O   1 
HETATM 7600 O  O   . HOH P 6 .   ? 12.079  4.748   11.684  1.00 23.60 ? 676 HOH A O   1 
HETATM 7601 O  O   . HOH P 6 .   ? -15.296 39.464  4.293   1.00 30.80 ? 677 HOH A O   1 
HETATM 7602 O  O   . HOH P 6 .   ? -12.372 1.185   1.250   1.00 21.35 ? 678 HOH A O   1 
HETATM 7603 O  O   . HOH P 6 .   ? -8.031  36.930  5.812   1.00 21.80 ? 679 HOH A O   1 
HETATM 7604 O  O   . HOH P 6 .   ? -7.201  15.974  42.746  1.00 32.22 ? 680 HOH A O   1 
HETATM 7605 O  O   . HOH P 6 .   ? -38.150 27.442  4.584   1.00 23.87 ? 681 HOH A O   1 
HETATM 7606 O  O   . HOH P 6 .   ? -27.153 40.118  4.250   1.00 15.35 ? 682 HOH A O   1 
HETATM 7607 O  O   . HOH P 6 .   ? -27.358 13.603  18.658  1.00 14.03 ? 683 HOH A O   1 
HETATM 7608 O  O   . HOH P 6 .   ? 1.509   40.453  11.760  1.00 32.89 ? 684 HOH A O   1 
HETATM 7609 O  O   . HOH P 6 .   ? -15.297 4.335   9.510   1.00 23.26 ? 685 HOH A O   1 
HETATM 7610 O  O   . HOH P 6 .   ? -6.356  1.705   3.767   1.00 36.38 ? 686 HOH A O   1 
HETATM 7611 O  O   . HOH P 6 .   ? -33.326 7.535   9.931   1.00 11.64 ? 687 HOH A O   1 
HETATM 7612 O  O   . HOH P 6 .   ? -25.945 37.413  20.058  1.00 33.88 ? 688 HOH A O   1 
HETATM 7613 O  O   . HOH P 6 .   ? -19.559 0.595   -1.368  1.00 33.29 ? 689 HOH A O   1 
HETATM 7614 O  O   . HOH P 6 .   ? -9.785  27.580  41.695  1.00 16.64 ? 690 HOH A O   1 
HETATM 7615 O  O   . HOH P 6 .   ? -22.210 43.074  15.909  1.00 26.96 ? 691 HOH A O   1 
HETATM 7616 O  O   . HOH P 6 .   ? -16.938 15.219  -13.840 1.00 21.97 ? 692 HOH A O   1 
HETATM 7617 O  O   . HOH P 6 .   ? -34.416 -2.219  7.048   1.00 30.94 ? 693 HOH A O   1 
HETATM 7618 O  O   . HOH P 6 .   ? -22.674 25.720  32.707  1.00 27.20 ? 694 HOH A O   1 
HETATM 7619 O  O   . HOH P 6 .   ? -35.890 16.854  -3.645  1.00 34.02 ? 695 HOH A O   1 
HETATM 7620 O  O   . HOH P 6 .   ? -5.449  41.497  6.349   1.00 38.11 ? 696 HOH A O   1 
HETATM 7621 O  O   . HOH P 6 .   ? -42.118 16.603  11.613  1.00 25.93 ? 697 HOH A O   1 
HETATM 7622 O  O   . HOH P 6 .   ? -22.336 49.661  27.055  1.00 28.27 ? 698 HOH A O   1 
HETATM 7623 O  O   . HOH P 6 .   ? -3.041  23.852  35.291  1.00 23.16 ? 699 HOH A O   1 
HETATM 7624 O  O   . HOH P 6 .   ? -3.648  42.418  27.578  1.00 26.65 ? 700 HOH A O   1 
HETATM 7625 O  O   . HOH P 6 .   ? 14.028  14.994  13.225  1.00 33.80 ? 701 HOH A O   1 
HETATM 7626 O  O   . HOH P 6 .   ? -0.245  51.172  14.719  1.00 33.88 ? 702 HOH A O   1 
HETATM 7627 O  O   . HOH P 6 .   ? -12.988 18.207  24.148  1.00 14.56 ? 703 HOH A O   1 
HETATM 7628 O  O   . HOH P 6 .   ? -8.162  30.920  18.515  1.00 39.20 ? 704 HOH A O   1 
HETATM 7629 O  O   . HOH P 6 .   ? -15.560 13.210  3.582   1.00 28.83 ? 705 HOH A O   1 
HETATM 7630 O  O   . HOH P 6 .   ? -13.181 16.040  -11.793 1.00 13.36 ? 706 HOH A O   1 
HETATM 7631 O  O   . HOH P 6 .   ? -15.364 46.219  1.069   1.00 22.51 ? 707 HOH A O   1 
HETATM 7632 O  O   . HOH P 6 .   ? 7.654   35.216  10.366  1.00 26.78 ? 708 HOH A O   1 
HETATM 7633 O  O   . HOH P 6 .   ? -3.919  41.130  12.097  1.00 23.78 ? 709 HOH A O   1 
HETATM 7634 O  O   . HOH P 6 .   ? -23.176 34.651  37.639  1.00 25.14 ? 710 HOH A O   1 
HETATM 7635 O  O   . HOH P 6 .   ? -19.756 31.500  38.374  1.00 36.08 ? 711 HOH A O   1 
HETATM 7636 O  O   . HOH P 6 .   ? -4.541  25.809  -5.938  1.00 18.43 ? 712 HOH A O   1 
HETATM 7637 O  O   . HOH P 6 .   ? 15.039  28.158  -2.362  1.00 38.23 ? 713 HOH A O   1 
HETATM 7638 O  O   . HOH P 6 .   ? -28.896 0.414   13.797  1.00 25.08 ? 714 HOH A O   1 
HETATM 7639 O  O   . HOH P 6 .   ? -2.606  15.564  -2.819  1.00 31.01 ? 715 HOH A O   1 
HETATM 7640 O  O   . HOH P 6 .   ? -22.481 41.675  32.867  1.00 16.24 ? 716 HOH A O   1 
HETATM 7641 O  O   . HOH P 6 .   ? -5.422  27.469  -3.531  1.00 27.48 ? 717 HOH A O   1 
HETATM 7642 O  O   . HOH P 6 .   ? -21.541 15.822  -14.840 1.00 28.23 ? 718 HOH A O   1 
HETATM 7643 O  O   . HOH P 6 .   ? -35.056 19.256  21.599  1.00 23.31 ? 719 HOH A O   1 
HETATM 7644 O  O   . HOH P 6 .   ? -34.476 17.038  20.370  1.00 21.78 ? 720 HOH A O   1 
HETATM 7645 O  O   . HOH P 6 .   ? -3.329  43.361  6.570   1.00 23.57 ? 721 HOH A O   1 
HETATM 7646 O  O   . HOH P 6 .   ? -25.872 47.759  23.428  1.00 31.18 ? 722 HOH A O   1 
HETATM 7647 O  O   . HOH P 6 .   ? -12.465 13.320  -9.540  1.00 15.66 ? 723 HOH A O   1 
HETATM 7648 O  O   . HOH P 6 .   ? -29.669 18.418  23.866  1.00 36.26 ? 724 HOH A O   1 
HETATM 7649 O  O   . HOH P 6 .   ? 4.021   19.492  27.785  1.00 22.29 ? 725 HOH A O   1 
HETATM 7650 O  O   . HOH P 6 .   ? -4.113  38.268  11.843  1.00 17.43 ? 726 HOH A O   1 
HETATM 7651 O  O   . HOH P 6 .   ? 0.770   26.491  29.156  1.00 26.43 ? 727 HOH A O   1 
HETATM 7652 O  O   . HOH P 6 .   ? -33.671 49.098  11.907  1.00 26.50 ? 728 HOH A O   1 
HETATM 7653 O  O   . HOH P 6 .   ? -3.916  54.982  15.900  1.00 38.71 ? 729 HOH A O   1 
HETATM 7654 O  O   . HOH P 6 .   ? -13.958 17.361  21.907  1.00 23.68 ? 730 HOH A O   1 
HETATM 7655 O  O   . HOH P 6 .   ? -19.412 49.206  32.079  1.00 26.81 ? 731 HOH A O   1 
HETATM 7656 O  O   . HOH P 6 .   ? -23.237 36.109  30.270  1.00 35.43 ? 732 HOH A O   1 
HETATM 7657 O  O   . HOH P 6 .   ? -0.107  4.720   8.954   1.00 28.52 ? 733 HOH A O   1 
HETATM 7658 O  O   . HOH P 6 .   ? -37.964 18.763  8.409   1.00 37.76 ? 734 HOH A O   1 
HETATM 7659 O  O   . HOH P 6 .   ? 6.309   28.921  24.783  1.00 29.42 ? 735 HOH A O   1 
HETATM 7660 O  O   . HOH P 6 .   ? -29.907 30.080  15.298  1.00 22.01 ? 736 HOH A O   1 
HETATM 7661 O  O   . HOH P 6 .   ? -41.787 23.213  0.046   1.00 31.51 ? 737 HOH A O   1 
HETATM 7662 O  O   . HOH P 6 .   ? -13.104 29.697  40.038  1.00 37.43 ? 738 HOH A O   1 
HETATM 7663 O  O   . HOH P 6 .   ? -5.186  36.218  12.706  1.00 13.70 ? 739 HOH A O   1 
HETATM 7664 O  O   . HOH P 6 .   ? 0.604   21.788  -5.247  1.00 33.06 ? 740 HOH A O   1 
HETATM 7665 O  O   . HOH P 6 .   ? 12.880  16.030  16.353  1.00 21.52 ? 741 HOH A O   1 
HETATM 7666 O  O   . HOH P 6 .   ? 4.824   20.637  24.214  1.00 32.72 ? 742 HOH A O   1 
HETATM 7667 O  O   . HOH P 6 .   ? -30.739 4.792   16.205  1.00 28.60 ? 743 HOH A O   1 
HETATM 7668 O  O   . HOH P 6 .   ? -21.412 50.035  20.549  1.00 26.50 ? 744 HOH A O   1 
HETATM 7669 O  O   . HOH P 6 .   ? -30.257 39.594  20.854  1.00 28.70 ? 745 HOH A O   1 
HETATM 7670 O  O   . HOH P 6 .   ? 4.514   30.277  24.487  1.00 26.04 ? 746 HOH A O   1 
HETATM 7671 O  O   . HOH P 6 .   ? -1.089  54.332  23.987  1.00 27.76 ? 747 HOH A O   1 
HETATM 7672 O  O   . HOH P 6 .   ? 8.002   22.091  -0.126  1.00 27.26 ? 748 HOH A O   1 
HETATM 7673 O  O   . HOH P 6 .   ? -18.337 25.576  -4.654  1.00 25.39 ? 749 HOH A O   1 
HETATM 7674 O  O   . HOH P 6 .   ? -24.644 40.457  1.851   1.00 31.14 ? 750 HOH A O   1 
HETATM 7675 O  O   . HOH P 6 .   ? -34.196 4.649   4.925   1.00 29.38 ? 751 HOH A O   1 
HETATM 7676 O  O   . HOH P 6 .   ? -33.314 29.584  11.348  1.00 24.59 ? 752 HOH A O   1 
HETATM 7677 O  O   . HOH P 6 .   ? 9.873   21.305  17.415  1.00 29.92 ? 753 HOH A O   1 
HETATM 7678 O  O   . HOH P 6 .   ? -19.420 54.357  17.962  1.00 36.55 ? 754 HOH A O   1 
HETATM 7679 O  O   . HOH P 6 .   ? -12.518 22.253  36.256  1.00 31.23 ? 755 HOH A O   1 
HETATM 7680 O  O   . HOH P 6 .   ? -14.221 27.927  22.668  1.00 27.51 ? 756 HOH A O   1 
HETATM 7681 O  O   . HOH P 6 .   ? -12.561 29.311  27.949  1.00 32.65 ? 757 HOH A O   1 
HETATM 7682 O  O   . HOH P 6 .   ? -9.520  34.883  5.279   1.00 32.44 ? 758 HOH A O   1 
HETATM 7683 O  O   . HOH P 6 .   ? -4.886  27.668  1.727   1.00 29.49 ? 759 HOH A O   1 
HETATM 7684 O  O   . HOH P 6 .   ? -28.116 12.185  20.468  1.00 29.44 ? 760 HOH A O   1 
HETATM 7685 O  O   . HOH P 6 .   ? 5.379   39.218  13.407  1.00 30.05 ? 761 HOH A O   1 
HETATM 7686 O  O   . HOH P 6 .   ? -20.539 50.596  15.192  1.00 31.99 ? 762 HOH A O   1 
HETATM 7687 O  O   . HOH P 6 .   ? -39.369 22.656  11.395  1.00 22.90 ? 763 HOH A O   1 
HETATM 7688 O  O   . HOH P 6 .   ? -1.482  4.908   16.569  1.00 39.02 ? 764 HOH A O   1 
HETATM 7689 O  O   . HOH P 6 .   ? -22.377 43.614  18.906  1.00 30.83 ? 765 HOH A O   1 
HETATM 7690 O  O   . HOH P 6 .   ? -19.188 20.953  27.538  1.00 28.00 ? 766 HOH A O   1 
HETATM 7691 O  O   . HOH P 6 .   ? -33.821 18.165  -10.756 1.00 30.33 ? 767 HOH A O   1 
HETATM 7692 O  O   . HOH P 6 .   ? 6.330   36.255  8.765   1.00 31.03 ? 768 HOH A O   1 
HETATM 7693 O  O   . HOH P 6 .   ? 0.063   22.851  33.709  1.00 29.37 ? 769 HOH A O   1 
HETATM 7694 O  O   . HOH P 6 .   ? -17.810 47.142  36.341  1.00 26.39 ? 770 HOH A O   1 
HETATM 7695 O  O   . HOH P 6 .   ? -19.992 15.514  19.449  1.00 27.73 ? 771 HOH A O   1 
HETATM 7696 O  O   . HOH P 6 .   ? -28.096 46.749  29.091  1.00 38.84 ? 772 HOH A O   1 
HETATM 7697 O  O   . HOH P 6 .   ? -15.529 25.313  27.982  1.00 28.65 ? 773 HOH A O   1 
HETATM 7698 O  O   . HOH P 6 .   ? -7.316  31.883  1.005   1.00 31.61 ? 774 HOH A O   1 
HETATM 7699 O  O   . HOH P 6 .   ? 8.281   24.221  22.015  1.00 25.93 ? 775 HOH A O   1 
HETATM 7700 O  O   . HOH P 6 .   ? -12.859 -2.117  13.001  1.00 24.37 ? 776 HOH A O   1 
HETATM 7701 O  O   . HOH P 6 .   ? -2.994  7.284   16.164  1.00 28.29 ? 777 HOH A O   1 
HETATM 7702 O  O   . HOH P 6 .   ? -29.295 29.320  20.919  1.00 30.11 ? 778 HOH A O   1 
HETATM 7703 O  O   . HOH P 6 .   ? -15.945 15.925  22.174  1.00 20.46 ? 779 HOH A O   1 
HETATM 7704 O  O   . HOH P 6 .   ? -16.878 32.326  42.491  1.00 30.51 ? 780 HOH A O   1 
HETATM 7705 O  O   . HOH P 6 .   ? -9.424  8.234   -9.532  1.00 30.07 ? 781 HOH A O   1 
HETATM 7706 O  O   . HOH P 6 .   ? -36.043 4.407   -12.629 1.00 29.94 ? 782 HOH A O   1 
HETATM 7707 O  O   . HOH Q 6 .   ? -4.582  0.612   14.357  1.00 26.48 ? 601 HOH B O   1 
HETATM 7708 O  O   . HOH Q 6 .   ? -16.103 -11.946 22.483  1.00 20.00 ? 602 HOH B O   1 
HETATM 7709 O  O   . HOH Q 6 .   ? -8.648  -7.917  -1.502  1.00 13.61 ? 603 HOH B O   1 
HETATM 7710 O  O   . HOH Q 6 .   ? -27.410 -5.567  9.085   1.00 25.31 ? 604 HOH B O   1 
HETATM 7711 O  O   . HOH Q 6 .   ? -36.344 -34.569 28.078  1.00 21.62 ? 605 HOH B O   1 
HETATM 7712 O  O   . HOH Q 6 .   ? -41.375 -35.663 18.644  1.00 6.07  ? 606 HOH B O   1 
HETATM 7713 O  O   . HOH Q 6 .   ? -32.025 -15.060 30.637  1.00 20.90 ? 607 HOH B O   1 
HETATM 7714 O  O   . HOH Q 6 .   ? -41.060 -26.167 27.901  1.00 24.08 ? 608 HOH B O   1 
HETATM 7715 O  O   . HOH Q 6 .   ? -19.823 -47.788 26.306  1.00 19.59 ? 609 HOH B O   1 
HETATM 7716 O  O   . HOH Q 6 .   ? -38.571 -52.905 17.715  1.00 26.97 ? 610 HOH B O   1 
HETATM 7717 O  O   . HOH Q 6 .   ? -8.941  -9.128  20.575  1.00 24.45 ? 611 HOH B O   1 
HETATM 7718 O  O   . HOH Q 6 .   ? -32.055 -45.601 6.514   1.00 31.37 ? 612 HOH B O   1 
HETATM 7719 O  O   . HOH Q 6 .   ? -19.364 -40.898 -4.014  1.00 25.11 ? 613 HOH B O   1 
HETATM 7720 O  O   . HOH Q 6 .   ? -20.563 -2.038  1.572   1.00 23.61 ? 614 HOH B O   1 
HETATM 7721 O  O   . HOH Q 6 .   ? -38.351 -28.725 8.984   1.00 22.91 ? 615 HOH B O   1 
HETATM 7722 O  O   . HOH Q 6 .   ? -50.538 -21.243 17.663  1.00 31.19 ? 616 HOH B O   1 
HETATM 7723 O  O   . HOH Q 6 .   ? -19.406 -47.695 15.007  1.00 19.02 ? 617 HOH B O   1 
HETATM 7724 O  O   . HOH Q 6 .   ? -42.691 -50.710 30.613  1.00 30.37 ? 618 HOH B O   1 
HETATM 7725 O  O   . HOH Q 6 .   ? -44.978 -27.411 1.132   1.00 23.98 ? 619 HOH B O   1 
HETATM 7726 O  O   . HOH Q 6 .   ? -32.761 -24.681 -2.169  1.00 26.28 ? 620 HOH B O   1 
HETATM 7727 O  O   . HOH Q 6 .   ? -16.792 -18.316 -12.440 1.00 17.37 ? 621 HOH B O   1 
HETATM 7728 O  O   . HOH Q 6 .   ? -15.537 -10.549 -4.760  1.00 26.15 ? 622 HOH B O   1 
HETATM 7729 O  O   . HOH Q 6 .   ? -32.410 -6.963  26.814  1.00 17.30 ? 623 HOH B O   1 
HETATM 7730 O  O   . HOH Q 6 .   ? -24.157 -22.292 28.093  1.00 21.43 ? 624 HOH B O   1 
HETATM 7731 O  O   . HOH Q 6 .   ? -26.185 -51.569 14.677  1.00 22.67 ? 625 HOH B O   1 
HETATM 7732 O  O   . HOH Q 6 .   ? -47.327 -32.733 13.199  1.00 23.08 ? 626 HOH B O   1 
HETATM 7733 O  O   . HOH Q 6 .   ? -32.718 -44.400 8.698   1.00 21.61 ? 627 HOH B O   1 
HETATM 7734 O  O   . HOH Q 6 .   ? -40.569 -24.917 30.894  1.00 22.57 ? 628 HOH B O   1 
HETATM 7735 O  O   . HOH Q 6 .   ? -32.700 -34.011 14.026  1.00 14.15 ? 629 HOH B O   1 
HETATM 7736 O  O   . HOH Q 6 .   ? -18.138 -26.563 12.430  1.00 18.97 ? 630 HOH B O   1 
HETATM 7737 O  O   . HOH Q 6 .   ? -13.208 -36.920 22.186  1.00 21.81 ? 631 HOH B O   1 
HETATM 7738 O  O   . HOH Q 6 .   ? -23.769 -4.427  9.859   1.00 14.53 ? 632 HOH B O   1 
HETATM 7739 O  O   . HOH Q 6 .   ? -47.302 -15.771 24.478  1.00 32.42 ? 633 HOH B O   1 
HETATM 7740 O  O   . HOH Q 6 .   ? -38.622 -23.406 17.914  1.00 20.14 ? 634 HOH B O   1 
HETATM 7741 O  O   . HOH Q 6 .   ? -23.292 -29.606 14.003  1.00 12.52 ? 635 HOH B O   1 
HETATM 7742 O  O   . HOH Q 6 .   ? -35.317 -30.595 14.620  1.00 13.18 ? 636 HOH B O   1 
HETATM 7743 O  O   . HOH Q 6 .   ? 0.094   -21.973 12.948  1.00 16.20 ? 637 HOH B O   1 
HETATM 7744 O  O   . HOH Q 6 .   ? -26.998 -29.174 28.945  1.00 20.64 ? 638 HOH B O   1 
HETATM 7745 O  O   . HOH Q 6 .   ? -42.622 -15.035 30.632  1.00 33.18 ? 639 HOH B O   1 
HETATM 7746 O  O   . HOH Q 6 .   ? -33.264 -32.938 19.995  1.00 5.50  ? 640 HOH B O   1 
HETATM 7747 O  O   . HOH Q 6 .   ? -13.206 -40.006 34.761  1.00 32.17 ? 641 HOH B O   1 
HETATM 7748 O  O   . HOH Q 6 .   ? -25.260 -42.793 42.680  1.00 35.07 ? 642 HOH B O   1 
HETATM 7749 O  O   . HOH Q 6 .   ? -28.691 -5.072  -0.624  1.00 29.08 ? 643 HOH B O   1 
HETATM 7750 O  O   . HOH Q 6 .   ? -20.951 -42.517 24.588  1.00 18.52 ? 644 HOH B O   1 
HETATM 7751 O  O   . HOH Q 6 .   ? -7.632  -14.226 -4.997  1.00 18.56 ? 645 HOH B O   1 
HETATM 7752 O  O   . HOH Q 6 .   ? -3.605  -17.394 0.705   1.00 21.06 ? 646 HOH B O   1 
HETATM 7753 O  O   . HOH Q 6 .   ? -27.168 -34.026 9.412   1.00 11.44 ? 647 HOH B O   1 
HETATM 7754 O  O   . HOH Q 6 .   ? -33.779 -35.107 17.385  1.00 21.01 ? 648 HOH B O   1 
HETATM 7755 O  O   . HOH Q 6 .   ? -22.588 -17.579 20.345  1.00 29.52 ? 649 HOH B O   1 
HETATM 7756 O  O   . HOH Q 6 .   ? -4.944  -25.690 18.775  1.00 20.28 ? 650 HOH B O   1 
HETATM 7757 O  O   . HOH Q 6 .   ? -49.585 -30.191 8.241   1.00 20.45 ? 651 HOH B O   1 
HETATM 7758 O  O   . HOH Q 6 .   ? -16.571 -42.700 18.148  1.00 27.59 ? 652 HOH B O   1 
HETATM 7759 O  O   . HOH Q 6 .   ? -12.994 -10.452 -9.431  1.00 30.11 ? 653 HOH B O   1 
HETATM 7760 O  O   . HOH Q 6 .   ? -43.695 -25.350 14.330  1.00 12.77 ? 654 HOH B O   1 
HETATM 7761 O  O   . HOH Q 6 .   ? -29.659 -7.602  9.788   1.00 16.51 ? 655 HOH B O   1 
HETATM 7762 O  O   . HOH Q 6 .   ? -31.867 -24.516 3.896   1.00 17.54 ? 656 HOH B O   1 
HETATM 7763 O  O   . HOH Q 6 .   ? -21.520 -25.576 -0.547  1.00 28.34 ? 657 HOH B O   1 
HETATM 7764 O  O   . HOH Q 6 .   ? -4.020  -16.353 20.661  1.00 19.78 ? 658 HOH B O   1 
HETATM 7765 O  O   . HOH Q 6 .   ? -36.619 -53.727 25.369  1.00 26.32 ? 659 HOH B O   1 
HETATM 7766 O  O   . HOH Q 6 .   ? -17.503 -13.640 -8.244  1.00 20.54 ? 660 HOH B O   1 
HETATM 7767 O  O   . HOH Q 6 .   ? -31.130 -15.882 33.077  1.00 27.90 ? 661 HOH B O   1 
HETATM 7768 O  O   . HOH Q 6 .   ? -13.786 -15.105 21.686  1.00 24.37 ? 662 HOH B O   1 
HETATM 7769 O  O   . HOH Q 6 .   ? -12.205 -25.685 25.352  1.00 15.15 ? 663 HOH B O   1 
HETATM 7770 O  O   . HOH Q 6 .   ? -19.933 -8.178  -9.418  1.00 31.21 ? 664 HOH B O   1 
HETATM 7771 O  O   . HOH Q 6 .   ? -31.342 -54.673 17.761  1.00 29.86 ? 665 HOH B O   1 
HETATM 7772 O  O   . HOH Q 6 .   ? -24.307 -41.838 4.244   1.00 26.08 ? 666 HOH B O   1 
HETATM 7773 O  O   . HOH Q 6 .   ? -26.815 -24.720 -0.538  1.00 24.57 ? 667 HOH B O   1 
HETATM 7774 O  O   . HOH Q 6 .   ? -48.239 -21.392 18.386  1.00 28.44 ? 668 HOH B O   1 
HETATM 7775 O  O   . HOH Q 6 .   ? -48.892 -29.144 22.867  1.00 19.06 ? 669 HOH B O   1 
HETATM 7776 O  O   . HOH Q 6 .   ? -23.670 -23.183 -10.606 1.00 28.19 ? 670 HOH B O   1 
HETATM 7777 O  O   . HOH Q 6 .   ? -6.656  0.179   16.657  1.00 31.81 ? 671 HOH B O   1 
HETATM 7778 O  O   . HOH Q 6 .   ? -6.289  -19.954 23.571  1.00 26.40 ? 672 HOH B O   1 
HETATM 7779 O  O   . HOH Q 6 .   ? -52.528 -24.161 14.620  1.00 35.83 ? 673 HOH B O   1 
HETATM 7780 O  O   . HOH Q 6 .   ? -42.774 -49.766 28.269  1.00 32.93 ? 674 HOH B O   1 
HETATM 7781 O  O   . HOH Q 6 .   ? -21.883 -43.115 44.482  1.00 9.56  ? 675 HOH B O   1 
HETATM 7782 O  O   . HOH Q 6 .   ? -27.448 -27.064 42.261  1.00 26.59 ? 676 HOH B O   1 
HETATM 7783 O  O   . HOH Q 6 .   ? -51.913 -13.124 10.577  1.00 27.44 ? 677 HOH B O   1 
HETATM 7784 O  O   . HOH Q 6 .   ? -12.261 -8.001  14.304  1.00 17.26 ? 678 HOH B O   1 
HETATM 7785 O  O   . HOH Q 6 .   ? -4.899  -31.577 10.549  1.00 26.50 ? 679 HOH B O   1 
HETATM 7786 O  O   . HOH Q 6 .   ? -31.932 -31.383 36.453  1.00 28.01 ? 680 HOH B O   1 
HETATM 7787 O  O   . HOH Q 6 .   ? -27.228 -33.940 3.973   1.00 25.30 ? 681 HOH B O   1 
HETATM 7788 O  O   . HOH Q 6 .   ? -11.706 -14.028 19.346  1.00 17.72 ? 682 HOH B O   1 
HETATM 7789 O  O   . HOH Q 6 .   ? -13.735 -24.356 31.493  1.00 26.46 ? 683 HOH B O   1 
HETATM 7790 O  O   . HOH Q 6 .   ? -35.031 -23.291 36.594  1.00 13.44 ? 684 HOH B O   1 
HETATM 7791 O  O   . HOH Q 6 .   ? -56.422 -23.271 1.873   1.00 32.55 ? 685 HOH B O   1 
HETATM 7792 O  O   . HOH Q 6 .   ? -4.940  -49.567 11.131  1.00 26.00 ? 686 HOH B O   1 
HETATM 7793 O  O   . HOH Q 6 .   ? -28.284 -50.956 31.746  1.00 20.47 ? 687 HOH B O   1 
HETATM 7794 O  O   . HOH Q 6 .   ? -49.458 -27.621 17.569  1.00 26.64 ? 688 HOH B O   1 
HETATM 7795 O  O   . HOH Q 6 .   ? -27.681 -18.261 33.208  1.00 30.74 ? 689 HOH B O   1 
HETATM 7796 O  O   . HOH Q 6 .   ? -26.737 -1.848  1.509   1.00 23.59 ? 690 HOH B O   1 
HETATM 7797 O  O   . HOH Q 6 .   ? -14.645 -34.978 38.249  1.00 31.70 ? 691 HOH B O   1 
HETATM 7798 O  O   . HOH Q 6 .   ? -10.354 -22.199 29.183  1.00 23.55 ? 692 HOH B O   1 
HETATM 7799 O  O   . HOH Q 6 .   ? -5.563  -8.041  9.989   1.00 18.28 ? 693 HOH B O   1 
HETATM 7800 O  O   . HOH Q 6 .   ? -9.052  -38.294 26.006  1.00 39.40 ? 694 HOH B O   1 
HETATM 7801 O  O   . HOH Q 6 .   ? -8.505  -25.893 -6.001  1.00 29.66 ? 695 HOH B O   1 
HETATM 7802 O  O   . HOH Q 6 .   ? -17.613 -3.889  14.000  1.00 25.14 ? 696 HOH B O   1 
HETATM 7803 O  O   . HOH Q 6 .   ? -43.237 -17.077 25.569  1.00 21.24 ? 697 HOH B O   1 
HETATM 7804 O  O   . HOH Q 6 .   ? -9.519  -0.344  13.283  1.00 23.16 ? 698 HOH B O   1 
HETATM 7805 O  O   . HOH Q 6 .   ? -19.560 -1.381  3.984   1.00 11.93 ? 699 HOH B O   1 
HETATM 7806 O  O   . HOH Q 6 .   ? -23.362 -49.481 9.016   1.00 25.79 ? 700 HOH B O   1 
HETATM 7807 O  O   . HOH Q 6 .   ? -16.270 -42.438 34.887  1.00 18.06 ? 701 HOH B O   1 
HETATM 7808 O  O   . HOH Q 6 .   ? -12.227 -31.680 -5.199  1.00 35.06 ? 702 HOH B O   1 
HETATM 7809 O  O   . HOH Q 6 .   ? -1.660  -28.345 5.457   1.00 17.36 ? 703 HOH B O   1 
HETATM 7810 O  O   . HOH Q 6 .   ? -26.484 2.514   20.103  1.00 32.77 ? 704 HOH B O   1 
HETATM 7811 O  O   . HOH Q 6 .   ? -31.693 -52.483 13.815  1.00 28.03 ? 705 HOH B O   1 
HETATM 7812 O  O   . HOH Q 6 .   ? -23.822 -25.996 33.941  1.00 19.29 ? 706 HOH B O   1 
HETATM 7813 O  O   . HOH Q 6 .   ? -3.766  -17.343 -4.060  1.00 30.18 ? 707 HOH B O   1 
HETATM 7814 O  O   . HOH Q 6 .   ? -6.827  -16.582 -3.492  1.00 25.00 ? 708 HOH B O   1 
HETATM 7815 O  O   . HOH Q 6 .   ? -12.492 -40.693 6.184   1.00 26.59 ? 709 HOH B O   1 
HETATM 7816 O  O   . HOH Q 6 .   ? -44.030 -50.415 23.005  1.00 24.44 ? 710 HOH B O   1 
HETATM 7817 O  O   . HOH Q 6 .   ? -13.147 -45.258 17.614  1.00 25.60 ? 711 HOH B O   1 
HETATM 7818 O  O   . HOH Q 6 .   ? -25.929 -23.072 36.678  1.00 42.02 ? 712 HOH B O   1 
HETATM 7819 O  O   . HOH Q 6 .   ? -5.547  -29.364 12.231  1.00 14.81 ? 713 HOH B O   1 
HETATM 7820 O  O   . HOH Q 6 .   ? -45.041 -41.039 20.694  1.00 25.67 ? 714 HOH B O   1 
HETATM 7821 O  O   . HOH Q 6 .   ? -36.577 -8.491  0.424   1.00 32.97 ? 715 HOH B O   1 
HETATM 7822 O  O   . HOH Q 6 .   ? -41.392 -4.548  8.414   1.00 35.46 ? 716 HOH B O   1 
HETATM 7823 O  O   . HOH Q 6 .   ? -53.109 -14.803 14.645  1.00 38.47 ? 717 HOH B O   1 
HETATM 7824 O  O   . HOH Q 6 .   ? -1.497  -25.352 17.346  1.00 33.81 ? 718 HOH B O   1 
HETATM 7825 O  O   . HOH Q 6 .   ? -26.730 -17.065 -10.379 1.00 11.35 ? 719 HOH B O   1 
HETATM 7826 O  O   . HOH Q 6 .   ? -22.191 -5.944  17.504  1.00 30.20 ? 720 HOH B O   1 
HETATM 7827 O  O   . HOH Q 6 .   ? -2.954  -7.104  9.329   1.00 30.73 ? 721 HOH B O   1 
HETATM 7828 O  O   . HOH Q 6 .   ? -15.659 -40.448 33.885  1.00 26.39 ? 722 HOH B O   1 
HETATM 7829 O  O   . HOH Q 6 .   ? -16.327 -17.272 21.044  1.00 19.73 ? 723 HOH B O   1 
HETATM 7830 O  O   . HOH Q 6 .   ? -20.354 -20.372 21.903  1.00 33.10 ? 724 HOH B O   1 
HETATM 7831 O  O   . HOH Q 6 .   ? -11.504 -46.065 30.742  1.00 32.10 ? 725 HOH B O   1 
HETATM 7832 O  O   . HOH Q 6 .   ? -37.184 -19.663 35.016  1.00 13.98 ? 726 HOH B O   1 
HETATM 7833 O  O   . HOH Q 6 .   ? -40.072 -38.400 25.926  1.00 31.90 ? 727 HOH B O   1 
HETATM 7834 O  O   . HOH Q 6 .   ? -35.549 -41.585 29.777  1.00 25.97 ? 728 HOH B O   1 
HETATM 7835 O  O   . HOH Q 6 .   ? -47.381 -22.301 1.186   1.00 31.61 ? 729 HOH B O   1 
HETATM 7836 O  O   . HOH Q 6 .   ? -17.286 -49.148 23.152  1.00 18.22 ? 730 HOH B O   1 
HETATM 7837 O  O   . HOH Q 6 .   ? -24.039 -48.469 6.889   1.00 13.95 ? 731 HOH B O   1 
HETATM 7838 O  O   . HOH Q 6 .   ? -44.503 -20.161 25.401  1.00 31.80 ? 732 HOH B O   1 
HETATM 7839 O  O   . HOH Q 6 .   ? -43.369 -30.047 25.998  1.00 21.07 ? 733 HOH B O   1 
HETATM 7840 O  O   . HOH Q 6 .   ? -50.352 -36.824 15.737  1.00 31.70 ? 734 HOH B O   1 
HETATM 7841 O  O   . HOH Q 6 .   ? -3.854  -19.084 22.136  1.00 17.00 ? 735 HOH B O   1 
HETATM 7842 O  O   . HOH Q 6 .   ? -19.525 1.037   4.011   1.00 19.35 ? 736 HOH B O   1 
HETATM 7843 O  O   . HOH Q 6 .   ? -13.197 -1.996  10.608  1.00 40.58 ? 737 HOH B O   1 
HETATM 7844 O  O   . HOH Q 6 .   ? -33.523 -3.037  4.702   1.00 25.15 ? 738 HOH B O   1 
HETATM 7845 O  O   . HOH Q 6 .   ? -14.855 -30.513 30.647  1.00 34.62 ? 739 HOH B O   1 
HETATM 7846 O  O   . HOH Q 6 .   ? -16.713 -49.298 29.798  1.00 30.93 ? 740 HOH B O   1 
HETATM 7847 O  O   . HOH Q 6 .   ? -24.476 -40.130 6.635   1.00 22.25 ? 741 HOH B O   1 
HETATM 7848 O  O   . HOH Q 6 .   ? -34.344 -52.923 13.449  1.00 31.60 ? 742 HOH B O   1 
HETATM 7849 O  O   . HOH Q 6 .   ? -10.954 -5.381  14.235  1.00 21.61 ? 743 HOH B O   1 
HETATM 7850 O  O   . HOH Q 6 .   ? -36.695 -14.946 -1.536  1.00 34.45 ? 744 HOH B O   1 
HETATM 7851 O  O   . HOH Q 6 .   ? -44.248 -39.287 15.935  1.00 30.09 ? 745 HOH B O   1 
HETATM 7852 O  O   . HOH Q 6 .   ? -31.917 -13.842 45.821  1.00 25.40 ? 746 HOH B O   1 
HETATM 7853 O  O   . HOH Q 6 .   ? -45.294 -14.992 -0.049  1.00 30.81 ? 747 HOH B O   1 
HETATM 7854 O  O   . HOH Q 6 .   ? -9.029  -30.158 16.210  1.00 20.73 ? 748 HOH B O   1 
HETATM 7855 O  O   . HOH Q 6 .   ? -45.371 -36.945 10.547  1.00 34.17 ? 749 HOH B O   1 
HETATM 7856 O  O   . HOH Q 6 .   ? -34.649 -28.467 3.679   1.00 32.60 ? 750 HOH B O   1 
HETATM 7857 O  O   . HOH Q 6 .   ? -31.551 -32.443 38.527  1.00 27.96 ? 751 HOH B O   1 
HETATM 7858 O  O   . HOH Q 6 .   ? -25.198 -10.738 -7.350  1.00 34.26 ? 752 HOH B O   1 
HETATM 7859 O  O   . HOH Q 6 .   ? -18.186 -14.095 -15.583 1.00 26.55 ? 753 HOH B O   1 
HETATM 7860 O  O   . HOH Q 6 .   ? -17.609 -45.078 20.312  1.00 25.22 ? 754 HOH B O   1 
HETATM 7861 O  O   . HOH Q 6 .   ? -24.481 -41.990 48.955  1.00 32.10 ? 755 HOH B O   1 
HETATM 7862 O  O   . HOH Q 6 .   ? -8.944  -3.025  -2.300  1.00 37.93 ? 756 HOH B O   1 
HETATM 7863 O  O   . HOH Q 6 .   ? -36.846 -54.833 17.209  1.00 31.45 ? 757 HOH B O   1 
HETATM 7864 O  O   . HOH Q 6 .   ? -19.854 -15.573 20.338  1.00 33.40 ? 758 HOH B O   1 
HETATM 7865 O  O   . HOH Q 6 .   ? -4.966  -4.994  5.349   1.00 19.31 ? 759 HOH B O   1 
HETATM 7866 O  O   . HOH Q 6 .   ? -47.333 -23.933 23.528  1.00 20.49 ? 760 HOH B O   1 
HETATM 7867 O  O   . HOH Q 6 .   ? -59.153 -26.826 14.603  1.00 31.93 ? 761 HOH B O   1 
HETATM 7868 O  O   . HOH Q 6 .   ? -40.026 -25.374 -4.180  1.00 32.46 ? 762 HOH B O   1 
HETATM 7869 O  O   . HOH Q 6 .   ? -14.444 -37.453 33.676  1.00 31.92 ? 763 HOH B O   1 
HETATM 7870 O  O   . HOH Q 6 .   ? -26.002 1.767   12.408  1.00 28.98 ? 764 HOH B O   1 
HETATM 7871 O  O   . HOH Q 6 .   ? -31.945 0.115   18.360  1.00 32.63 ? 765 HOH B O   1 
HETATM 7872 O  O   . HOH Q 6 .   ? -19.391 -50.244 25.309  1.00 31.78 ? 766 HOH B O   1 
HETATM 7873 O  O   . HOH Q 6 .   ? -14.438 -41.671 4.403   1.00 32.94 ? 767 HOH B O   1 
HETATM 7874 O  O   . HOH Q 6 .   ? -22.379 -34.821 1.938   1.00 23.86 ? 768 HOH B O   1 
HETATM 7875 O  O   . HOH Q 6 .   ? -10.535 -12.152 21.050  1.00 23.89 ? 769 HOH B O   1 
HETATM 7876 O  O   . HOH Q 6 .   ? -35.715 -7.385  16.989  1.00 24.20 ? 770 HOH B O   1 
HETATM 7877 O  O   . HOH Q 6 .   ? -9.805  -44.410 30.004  1.00 35.59 ? 771 HOH B O   1 
HETATM 7878 O  O   . HOH Q 6 .   ? -26.604 1.148   14.644  1.00 28.96 ? 772 HOH B O   1 
HETATM 7879 O  O   . HOH Q 6 .   ? -24.257 -5.218  -2.243  1.00 37.32 ? 773 HOH B O   1 
HETATM 7880 O  O   . HOH Q 6 .   ? -9.984  -29.215 22.151  1.00 33.14 ? 774 HOH B O   1 
HETATM 7881 O  O   . HOH Q 6 .   ? -31.776 -33.500 3.016   1.00 34.74 ? 775 HOH B O   1 
HETATM 7882 O  O   . HOH Q 6 .   ? -47.842 -17.850 -2.226  1.00 28.47 ? 776 HOH B O   1 
# 
