data_8WN6
# 
_entry.id   8WN6 
# 
_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   8WN6         pdb_00008wn6 10.2210/pdb8wn6/pdb 
WWPDB D_1300041555 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_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                        8WN6 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-05 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              asfushi@mail.ecc.u-tokyo.ac.jp 
_pdbx_contact_author.name_first         Shinya 
_pdbx_contact_author.name_last          Fushinobu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1346-6435 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lin, C.C.'     1 0000-0002-0681-6655 
'Lu, T.J.'      2 0000-0002-3956-8272 
'Fushinobu, S.' 3 0000-0003-1346-6435 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Structural Basis for Specific Hydrolysis and Synthesis of beta-1-2-glucosidic
linkage by Glucose-tolerant beta-glucosidase Td2F2
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_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 'Lin, C.C.'     1 0000-0002-0681-6655 
primary 'Lu, T.J.'      2 0000-0002-3956-8272 
primary 'Fushinobu, S.' 3 0000-0003-1346-6435 
# 
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 'beta-glucosidase Td2F2'                          51561.605 1   3.2.1.21 E352Q ? ? 
2 branched    man 'beta-D-glucopyranose-(1-2)-beta-D-glucopyranose' 342.297   2   ?        ?     ? ? 
3 non-polymer man '2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID'       207.290   1   ?        ?     ? ? 
4 non-polymer syn 'SODIUM ION'                                      22.990    1   ?        ?     ? ? 
5 non-polymer syn 'MALONIC ACID'                                    104.061   2   ?        ?     ? ? 
6 water       nat water                                             18.015    231 ?        ?     ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMAGERFPADFVWGAATAAYQIEGAVREDGRGVSIWDTFSHTPGKIADGTTGDVACDSYHR
YGEDIGLLNALGMNAYRFSIAWPRIVPLGAGPINQAGLDHYSRMVDALLGAGLQPFVTLYHWDLPQPLEDRLGWGSRATA
TVFAEYADIVVRQLGDRVTHWATLNEPWCSAMLGYYLGVHAPGHTDLKRGLEASHNLLLGHGLAVQAMRAAAPQPLQIGI
VLNLTPTYPASDSPEDVAAARRFDGFVNRWFLDPLAGRGYPQDMLDYYGAAAPQANPEDLTQIAAPLDWLGVNYYERMRA
VDAPDASLPQAQRLDDPDLPHTADREVYPEGLYDILLRLHNDYPFRPLYITQNGCALHDEIAEDGGIHDGQRQAFFEAHL
AQLQRALAAGVPLKGYFAWSLLDNFEWAMGLSMRYGICYTNFETLERRIKDSGYWLRDFIAGQRG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMAGERFPADFVWGAATAAYQIEGAVREDGRGVSIWDTFSHTPGKIADGTTGDVACDSYHR
YGEDIGLLNALGMNAYRFSIAWPRIVPLGAGPINQAGLDHYSRMVDALLGAGLQPFVTLYHWDLPQPLEDRLGWGSRATA
TVFAEYADIVVRQLGDRVTHWATLNEPWCSAMLGYYLGVHAPGHTDLKRGLEASHNLLLGHGLAVQAMRAAAPQPLQIGI
VLNLTPTYPASDSPEDVAAARRFDGFVNRWFLDPLAGRGYPQDMLDYYGAAAPQANPEDLTQIAAPLDWLGVNYYERMRA
VDAPDASLPQAQRLDDPDLPHTADREVYPEGLYDILLRLHNDYPFRPLYITQNGCALHDEIAEDGGIHDGQRQAFFEAHL
AQLQRALAAGVPLKGYFAWSLLDNFEWAMGLSMRYGICYTNFETLERRIKDSGYWLRDFIAGQRG
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID' NHE 
4 'SODIUM ION'                                NA  
5 'MALONIC ACID'                              MLA 
6 water                                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  ALA n 
1 23  GLY n 
1 24  GLU n 
1 25  ARG n 
1 26  PHE n 
1 27  PRO n 
1 28  ALA n 
1 29  ASP n 
1 30  PHE n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  ALA n 
1 35  ALA n 
1 36  THR n 
1 37  ALA n 
1 38  ALA n 
1 39  TYR n 
1 40  GLN n 
1 41  ILE n 
1 42  GLU n 
1 43  GLY n 
1 44  ALA n 
1 45  VAL n 
1 46  ARG n 
1 47  GLU n 
1 48  ASP n 
1 49  GLY n 
1 50  ARG n 
1 51  GLY n 
1 52  VAL n 
1 53  SER n 
1 54  ILE n 
1 55  TRP n 
1 56  ASP n 
1 57  THR n 
1 58  PHE n 
1 59  SER n 
1 60  HIS n 
1 61  THR n 
1 62  PRO n 
1 63  GLY n 
1 64  LYS n 
1 65  ILE n 
1 66  ALA n 
1 67  ASP n 
1 68  GLY n 
1 69  THR n 
1 70  THR n 
1 71  GLY n 
1 72  ASP n 
1 73  VAL n 
1 74  ALA n 
1 75  CYS n 
1 76  ASP n 
1 77  SER n 
1 78  TYR n 
1 79  HIS n 
1 80  ARG n 
1 81  TYR n 
1 82  GLY n 
1 83  GLU n 
1 84  ASP n 
1 85  ILE n 
1 86  GLY n 
1 87  LEU n 
1 88  LEU n 
1 89  ASN n 
1 90  ALA n 
1 91  LEU n 
1 92  GLY n 
1 93  MET n 
1 94  ASN n 
1 95  ALA n 
1 96  TYR n 
1 97  ARG n 
1 98  PHE n 
1 99  SER n 
1 100 ILE n 
1 101 ALA n 
1 102 TRP n 
1 103 PRO n 
1 104 ARG n 
1 105 ILE n 
1 106 VAL n 
1 107 PRO n 
1 108 LEU n 
1 109 GLY n 
1 110 ALA n 
1 111 GLY n 
1 112 PRO n 
1 113 ILE n 
1 114 ASN n 
1 115 GLN n 
1 116 ALA n 
1 117 GLY n 
1 118 LEU n 
1 119 ASP n 
1 120 HIS n 
1 121 TYR n 
1 122 SER n 
1 123 ARG n 
1 124 MET n 
1 125 VAL n 
1 126 ASP n 
1 127 ALA n 
1 128 LEU n 
1 129 LEU n 
1 130 GLY n 
1 131 ALA n 
1 132 GLY n 
1 133 LEU n 
1 134 GLN n 
1 135 PRO n 
1 136 PHE n 
1 137 VAL n 
1 138 THR n 
1 139 LEU n 
1 140 TYR n 
1 141 HIS n 
1 142 TRP n 
1 143 ASP n 
1 144 LEU n 
1 145 PRO n 
1 146 GLN n 
1 147 PRO n 
1 148 LEU n 
1 149 GLU n 
1 150 ASP n 
1 151 ARG n 
1 152 LEU n 
1 153 GLY n 
1 154 TRP n 
1 155 GLY n 
1 156 SER n 
1 157 ARG n 
1 158 ALA n 
1 159 THR n 
1 160 ALA n 
1 161 THR n 
1 162 VAL n 
1 163 PHE n 
1 164 ALA n 
1 165 GLU n 
1 166 TYR n 
1 167 ALA n 
1 168 ASP n 
1 169 ILE n 
1 170 VAL n 
1 171 VAL n 
1 172 ARG n 
1 173 GLN n 
1 174 LEU n 
1 175 GLY n 
1 176 ASP n 
1 177 ARG n 
1 178 VAL n 
1 179 THR n 
1 180 HIS n 
1 181 TRP n 
1 182 ALA n 
1 183 THR n 
1 184 LEU n 
1 185 ASN n 
1 186 GLU n 
1 187 PRO n 
1 188 TRP n 
1 189 CYS n 
1 190 SER n 
1 191 ALA n 
1 192 MET n 
1 193 LEU n 
1 194 GLY n 
1 195 TYR n 
1 196 TYR n 
1 197 LEU n 
1 198 GLY n 
1 199 VAL n 
1 200 HIS n 
1 201 ALA n 
1 202 PRO n 
1 203 GLY n 
1 204 HIS n 
1 205 THR n 
1 206 ASP n 
1 207 LEU n 
1 208 LYS n 
1 209 ARG n 
1 210 GLY n 
1 211 LEU n 
1 212 GLU n 
1 213 ALA n 
1 214 SER n 
1 215 HIS n 
1 216 ASN n 
1 217 LEU n 
1 218 LEU n 
1 219 LEU n 
1 220 GLY n 
1 221 HIS n 
1 222 GLY n 
1 223 LEU n 
1 224 ALA n 
1 225 VAL n 
1 226 GLN n 
1 227 ALA n 
1 228 MET n 
1 229 ARG n 
1 230 ALA n 
1 231 ALA n 
1 232 ALA n 
1 233 PRO n 
1 234 GLN n 
1 235 PRO n 
1 236 LEU n 
1 237 GLN n 
1 238 ILE n 
1 239 GLY n 
1 240 ILE n 
1 241 VAL n 
1 242 LEU n 
1 243 ASN n 
1 244 LEU n 
1 245 THR n 
1 246 PRO n 
1 247 THR n 
1 248 TYR n 
1 249 PRO n 
1 250 ALA n 
1 251 SER n 
1 252 ASP n 
1 253 SER n 
1 254 PRO n 
1 255 GLU n 
1 256 ASP n 
1 257 VAL n 
1 258 ALA n 
1 259 ALA n 
1 260 ALA n 
1 261 ARG n 
1 262 ARG n 
1 263 PHE n 
1 264 ASP n 
1 265 GLY n 
1 266 PHE n 
1 267 VAL n 
1 268 ASN n 
1 269 ARG n 
1 270 TRP n 
1 271 PHE n 
1 272 LEU n 
1 273 ASP n 
1 274 PRO n 
1 275 LEU n 
1 276 ALA n 
1 277 GLY n 
1 278 ARG n 
1 279 GLY n 
1 280 TYR n 
1 281 PRO n 
1 282 GLN n 
1 283 ASP n 
1 284 MET n 
1 285 LEU n 
1 286 ASP n 
1 287 TYR n 
1 288 TYR n 
1 289 GLY n 
1 290 ALA n 
1 291 ALA n 
1 292 ALA n 
1 293 PRO n 
1 294 GLN n 
1 295 ALA n 
1 296 ASN n 
1 297 PRO n 
1 298 GLU n 
1 299 ASP n 
1 300 LEU n 
1 301 THR n 
1 302 GLN n 
1 303 ILE n 
1 304 ALA n 
1 305 ALA n 
1 306 PRO n 
1 307 LEU n 
1 308 ASP n 
1 309 TRP n 
1 310 LEU n 
1 311 GLY n 
1 312 VAL n 
1 313 ASN n 
1 314 TYR n 
1 315 TYR n 
1 316 GLU n 
1 317 ARG n 
1 318 MET n 
1 319 ARG n 
1 320 ALA n 
1 321 VAL n 
1 322 ASP n 
1 323 ALA n 
1 324 PRO n 
1 325 ASP n 
1 326 ALA n 
1 327 SER n 
1 328 LEU n 
1 329 PRO n 
1 330 GLN n 
1 331 ALA n 
1 332 GLN n 
1 333 ARG n 
1 334 LEU n 
1 335 ASP n 
1 336 ASP n 
1 337 PRO n 
1 338 ASP n 
1 339 LEU n 
1 340 PRO n 
1 341 HIS n 
1 342 THR n 
1 343 ALA n 
1 344 ASP n 
1 345 ARG n 
1 346 GLU n 
1 347 VAL n 
1 348 TYR n 
1 349 PRO n 
1 350 GLU n 
1 351 GLY n 
1 352 LEU n 
1 353 TYR n 
1 354 ASP n 
1 355 ILE n 
1 356 LEU n 
1 357 LEU n 
1 358 ARG n 
1 359 LEU n 
1 360 HIS n 
1 361 ASN n 
1 362 ASP n 
1 363 TYR n 
1 364 PRO n 
1 365 PHE n 
1 366 ARG n 
1 367 PRO n 
1 368 LEU n 
1 369 TYR n 
1 370 ILE n 
1 371 THR n 
1 372 GLN n 
1 373 ASN n 
1 374 GLY n 
1 375 CYS n 
1 376 ALA n 
1 377 LEU n 
1 378 HIS n 
1 379 ASP n 
1 380 GLU n 
1 381 ILE n 
1 382 ALA n 
1 383 GLU n 
1 384 ASP n 
1 385 GLY n 
1 386 GLY n 
1 387 ILE n 
1 388 HIS n 
1 389 ASP n 
1 390 GLY n 
1 391 GLN n 
1 392 ARG n 
1 393 GLN n 
1 394 ALA n 
1 395 PHE n 
1 396 PHE n 
1 397 GLU n 
1 398 ALA n 
1 399 HIS n 
1 400 LEU n 
1 401 ALA n 
1 402 GLN n 
1 403 LEU n 
1 404 GLN n 
1 405 ARG n 
1 406 ALA n 
1 407 LEU n 
1 408 ALA n 
1 409 ALA n 
1 410 GLY n 
1 411 VAL n 
1 412 PRO n 
1 413 LEU n 
1 414 LYS n 
1 415 GLY n 
1 416 TYR n 
1 417 PHE n 
1 418 ALA n 
1 419 TRP n 
1 420 SER n 
1 421 LEU n 
1 422 LEU n 
1 423 ASP n 
1 424 ASN n 
1 425 PHE n 
1 426 GLU n 
1 427 TRP n 
1 428 ALA n 
1 429 MET n 
1 430 GLY n 
1 431 LEU n 
1 432 SER n 
1 433 MET n 
1 434 ARG n 
1 435 TYR n 
1 436 GLY n 
1 437 ILE n 
1 438 CYS n 
1 439 TYR n 
1 440 THR n 
1 441 ASN n 
1 442 PHE n 
1 443 GLU n 
1 444 THR n 
1 445 LEU n 
1 446 GLU n 
1 447 ARG n 
1 448 ARG n 
1 449 ILE n 
1 450 LYS n 
1 451 ASP n 
1 452 SER n 
1 453 GLY n 
1 454 TYR n 
1 455 TRP n 
1 456 LEU n 
1 457 ARG n 
1 458 ASP n 
1 459 PHE n 
1 460 ILE n 
1 461 ALA n 
1 462 GLY n 
1 463 GLN n 
1 464 ARG n 
1 465 GLY 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                   465 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      metagenomes 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     408169 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DGlcpb1-2DGlcpb1-ROH                        'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,2,1/[a2122h-1b_1-5]/1-1/a2-b1' WURCS                       PDB2Glycan 1.1.0 
3 2 '[][b-D-Glcp]{[(2+1)][b-D-Glcp]{}}'         LINUCS                      PDB-CARE   ?     
# 
_pdbx_entity_branch_link.link_id                    1 
_pdbx_entity_branch_link.entity_id                  2 
_pdbx_entity_branch_link.entity_branch_list_num_1   2 
_pdbx_entity_branch_link.comp_id_1                  BGC 
_pdbx_entity_branch_link.atom_id_1                  C1 
_pdbx_entity_branch_link.leaving_atom_id_1          O1 
_pdbx_entity_branch_link.entity_branch_list_num_2   1 
_pdbx_entity_branch_link.comp_id_2                  BGC 
_pdbx_entity_branch_link.atom_id_2                  O2 
_pdbx_entity_branch_link.leaving_atom_id_2          HO2 
_pdbx_entity_branch_link.value_order                sing 
_pdbx_entity_branch_link.details                    ? 
# 
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 
BGC 'D-saccharide, beta linking' . beta-D-glucopyranose                        'beta-D-glucose; D-glucose; glucose' 'C6 H12 O6' 
180.156 
CYS 'L-peptide linking'          y CYSTEINE                                    ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                   ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                             ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                     ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE                                   ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                  . WATER                                       ? 'H2 O'           18.015  
ILE 'L-peptide linking'          y ISOLEUCINE                                  ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                                     ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                                      ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE                                  ? 'C5 H11 N O2 S'  149.211 
MLA non-polymer                  . 'MALONIC ACID'                              
'DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID; METHANEDICARBOXYLIC ACID' 'C3 H4 O4'       104.061 
NA  non-polymer                  . 'SODIUM ION'                                ? 'Na 1'           22.990  
NHE non-polymer                  . '2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID' 'N-CYCLOHEXYLTAURINE; CHES' 'C8 H17 N O3 S'  
207.290 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BGC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpb            
BGC 'COMMON NAME'                         GMML     1.0 b-D-glucopyranose 
BGC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Glcp          
BGC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
# 
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   MET 1   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  LEU 14  -6  ?   ?   ?   A . n 
A 1 15  VAL 15  -5  ?   ?   ?   A . n 
A 1 16  PRO 16  -4  ?   ?   ?   A . n 
A 1 17  ARG 17  -3  ?   ?   ?   A . n 
A 1 18  GLY 18  -2  ?   ?   ?   A . n 
A 1 19  SER 19  -1  ?   ?   ?   A . n 
A 1 20  HIS 20  0   ?   ?   ?   A . n 
A 1 21  MET 21  1   ?   ?   ?   A . n 
A 1 22  ALA 22  2   ?   ?   ?   A . n 
A 1 23  GLY 23  3   3   GLY GLY A . n 
A 1 24  GLU 24  4   4   GLU GLU A . n 
A 1 25  ARG 25  5   5   ARG ARG A . n 
A 1 26  PHE 26  6   6   PHE PHE A . n 
A 1 27  PRO 27  7   7   PRO PRO A . n 
A 1 28  ALA 28  8   8   ALA ALA A . n 
A 1 29  ASP 29  9   9   ASP ASP A . n 
A 1 30  PHE 30  10  10  PHE PHE A . n 
A 1 31  VAL 31  11  11  VAL VAL A . n 
A 1 32  TRP 32  12  12  TRP TRP A . n 
A 1 33  GLY 33  13  13  GLY GLY A . n 
A 1 34  ALA 34  14  14  ALA ALA A . n 
A 1 35  ALA 35  15  15  ALA ALA A . n 
A 1 36  THR 36  16  16  THR THR A . n 
A 1 37  ALA 37  17  17  ALA ALA A . n 
A 1 38  ALA 38  18  18  ALA ALA A . n 
A 1 39  TYR 39  19  19  TYR TYR A . n 
A 1 40  GLN 40  20  20  GLN GLN A . n 
A 1 41  ILE 41  21  21  ILE ILE A . n 
A 1 42  GLU 42  22  22  GLU GLU A . n 
A 1 43  GLY 43  23  23  GLY GLY A . n 
A 1 44  ALA 44  24  24  ALA ALA A . n 
A 1 45  VAL 45  25  25  VAL VAL A . n 
A 1 46  ARG 46  26  26  ARG ARG A . n 
A 1 47  GLU 47  27  27  GLU GLU A . n 
A 1 48  ASP 48  28  28  ASP ASP A . n 
A 1 49  GLY 49  29  29  GLY GLY A . n 
A 1 50  ARG 50  30  30  ARG ARG A . n 
A 1 51  GLY 51  31  31  GLY GLY A . n 
A 1 52  VAL 52  32  32  VAL VAL A . n 
A 1 53  SER 53  33  33  SER SER A . n 
A 1 54  ILE 54  34  34  ILE ILE A . n 
A 1 55  TRP 55  35  35  TRP TRP A . n 
A 1 56  ASP 56  36  36  ASP ASP A . n 
A 1 57  THR 57  37  37  THR THR A . n 
A 1 58  PHE 58  38  38  PHE PHE A . n 
A 1 59  SER 59  39  39  SER SER A . n 
A 1 60  HIS 60  40  40  HIS HIS A . n 
A 1 61  THR 61  41  41  THR THR A . n 
A 1 62  PRO 62  42  42  PRO PRO A . n 
A 1 63  GLY 63  43  43  GLY GLY A . n 
A 1 64  LYS 64  44  44  LYS LYS A . n 
A 1 65  ILE 65  45  45  ILE ILE A . n 
A 1 66  ALA 66  46  46  ALA ALA A . n 
A 1 67  ASP 67  47  47  ASP ASP A . n 
A 1 68  GLY 68  48  48  GLY GLY A . n 
A 1 69  THR 69  49  49  THR THR A . n 
A 1 70  THR 70  50  50  THR THR A . n 
A 1 71  GLY 71  51  51  GLY GLY A . n 
A 1 72  ASP 72  52  52  ASP ASP A . n 
A 1 73  VAL 73  53  53  VAL VAL A . n 
A 1 74  ALA 74  54  54  ALA ALA A . n 
A 1 75  CYS 75  55  55  CYS CYS A . n 
A 1 76  ASP 76  56  56  ASP ASP A . n 
A 1 77  SER 77  57  57  SER SER A . n 
A 1 78  TYR 78  58  58  TYR TYR A . n 
A 1 79  HIS 79  59  59  HIS HIS A . n 
A 1 80  ARG 80  60  60  ARG ARG A . n 
A 1 81  TYR 81  61  61  TYR TYR A . n 
A 1 82  GLY 82  62  62  GLY GLY A . n 
A 1 83  GLU 83  63  63  GLU GLU A . n 
A 1 84  ASP 84  64  64  ASP ASP A . n 
A 1 85  ILE 85  65  65  ILE ILE A . n 
A 1 86  GLY 86  66  66  GLY GLY A . n 
A 1 87  LEU 87  67  67  LEU LEU A . n 
A 1 88  LEU 88  68  68  LEU LEU A . n 
A 1 89  ASN 89  69  69  ASN ASN A . n 
A 1 90  ALA 90  70  70  ALA ALA A . n 
A 1 91  LEU 91  71  71  LEU LEU A . n 
A 1 92  GLY 92  72  72  GLY GLY A . n 
A 1 93  MET 93  73  73  MET MET A . n 
A 1 94  ASN 94  74  74  ASN ASN A . n 
A 1 95  ALA 95  75  75  ALA ALA A . n 
A 1 96  TYR 96  76  76  TYR TYR A . n 
A 1 97  ARG 97  77  77  ARG ARG A . n 
A 1 98  PHE 98  78  78  PHE PHE A . n 
A 1 99  SER 99  79  79  SER SER A . n 
A 1 100 ILE 100 80  80  ILE ILE A . n 
A 1 101 ALA 101 81  81  ALA ALA A . n 
A 1 102 TRP 102 82  82  TRP TRP A . n 
A 1 103 PRO 103 83  83  PRO PRO A . n 
A 1 104 ARG 104 84  84  ARG ARG A . n 
A 1 105 ILE 105 85  85  ILE ILE A . n 
A 1 106 VAL 106 86  86  VAL VAL A . n 
A 1 107 PRO 107 87  87  PRO PRO A . n 
A 1 108 LEU 108 88  88  LEU LEU A . n 
A 1 109 GLY 109 89  89  GLY GLY A . n 
A 1 110 ALA 110 90  90  ALA ALA A . n 
A 1 111 GLY 111 91  91  GLY GLY A . n 
A 1 112 PRO 112 92  92  PRO PRO A . n 
A 1 113 ILE 113 93  93  ILE ILE A . n 
A 1 114 ASN 114 94  94  ASN ASN A . n 
A 1 115 GLN 115 95  95  GLN GLN A . n 
A 1 116 ALA 116 96  96  ALA ALA A . n 
A 1 117 GLY 117 97  97  GLY GLY A . n 
A 1 118 LEU 118 98  98  LEU LEU A . n 
A 1 119 ASP 119 99  99  ASP ASP A . n 
A 1 120 HIS 120 100 100 HIS HIS A . n 
A 1 121 TYR 121 101 101 TYR TYR A . n 
A 1 122 SER 122 102 102 SER SER A . n 
A 1 123 ARG 123 103 103 ARG ARG A . n 
A 1 124 MET 124 104 104 MET MET A . n 
A 1 125 VAL 125 105 105 VAL VAL A . n 
A 1 126 ASP 126 106 106 ASP ASP A . n 
A 1 127 ALA 127 107 107 ALA ALA A . n 
A 1 128 LEU 128 108 108 LEU LEU A . n 
A 1 129 LEU 129 109 109 LEU LEU A . n 
A 1 130 GLY 130 110 110 GLY GLY A . n 
A 1 131 ALA 131 111 111 ALA ALA A . n 
A 1 132 GLY 132 112 112 GLY GLY A . n 
A 1 133 LEU 133 113 113 LEU LEU A . n 
A 1 134 GLN 134 114 114 GLN GLN A . n 
A 1 135 PRO 135 115 115 PRO PRO A . n 
A 1 136 PHE 136 116 116 PHE PHE A . n 
A 1 137 VAL 137 117 117 VAL VAL A . n 
A 1 138 THR 138 118 118 THR THR A . n 
A 1 139 LEU 139 119 119 LEU LEU A . n 
A 1 140 TYR 140 120 120 TYR TYR A . n 
A 1 141 HIS 141 121 121 HIS HIS A . n 
A 1 142 TRP 142 122 122 TRP TRP A . n 
A 1 143 ASP 143 123 123 ASP ASP A . n 
A 1 144 LEU 144 124 124 LEU LEU A . n 
A 1 145 PRO 145 125 125 PRO PRO A . n 
A 1 146 GLN 146 126 126 GLN GLN A . n 
A 1 147 PRO 147 127 127 PRO PRO A . n 
A 1 148 LEU 148 128 128 LEU LEU A . n 
A 1 149 GLU 149 129 129 GLU GLU A . n 
A 1 150 ASP 150 130 130 ASP ASP A . n 
A 1 151 ARG 151 131 131 ARG ARG A . n 
A 1 152 LEU 152 132 132 LEU LEU A . n 
A 1 153 GLY 153 133 133 GLY GLY A . n 
A 1 154 TRP 154 134 134 TRP TRP A . n 
A 1 155 GLY 155 135 135 GLY GLY A . n 
A 1 156 SER 156 136 136 SER SER A . n 
A 1 157 ARG 157 137 137 ARG ARG A . n 
A 1 158 ALA 158 138 138 ALA ALA A . n 
A 1 159 THR 159 139 139 THR THR A . n 
A 1 160 ALA 160 140 140 ALA ALA A . n 
A 1 161 THR 161 141 141 THR THR A . n 
A 1 162 VAL 162 142 142 VAL VAL A . n 
A 1 163 PHE 163 143 143 PHE PHE A . n 
A 1 164 ALA 164 144 144 ALA ALA A . n 
A 1 165 GLU 165 145 145 GLU GLU A . n 
A 1 166 TYR 166 146 146 TYR TYR A . n 
A 1 167 ALA 167 147 147 ALA ALA A . n 
A 1 168 ASP 168 148 148 ASP ASP A . n 
A 1 169 ILE 169 149 149 ILE ILE A . n 
A 1 170 VAL 170 150 150 VAL VAL A . n 
A 1 171 VAL 171 151 151 VAL VAL A . n 
A 1 172 ARG 172 152 152 ARG ARG A . n 
A 1 173 GLN 173 153 153 GLN GLN A . n 
A 1 174 LEU 174 154 154 LEU LEU A . n 
A 1 175 GLY 175 155 155 GLY GLY A . n 
A 1 176 ASP 176 156 156 ASP ASP A . n 
A 1 177 ARG 177 157 157 ARG ARG A . n 
A 1 178 VAL 178 158 158 VAL VAL A . n 
A 1 179 THR 179 159 159 THR THR A . n 
A 1 180 HIS 180 160 160 HIS HIS A . n 
A 1 181 TRP 181 161 161 TRP TRP A . n 
A 1 182 ALA 182 162 162 ALA ALA A . n 
A 1 183 THR 183 163 163 THR THR A . n 
A 1 184 LEU 184 164 164 LEU LEU A . n 
A 1 185 ASN 185 165 165 ASN ASN A . n 
A 1 186 GLU 186 166 166 GLU GLU A . n 
A 1 187 PRO 187 167 167 PRO PRO A . n 
A 1 188 TRP 188 168 168 TRP TRP A . n 
A 1 189 CYS 189 169 169 CYS CYS A . n 
A 1 190 SER 190 170 170 SER SER A . n 
A 1 191 ALA 191 171 171 ALA ALA A . n 
A 1 192 MET 192 172 172 MET MET A . n 
A 1 193 LEU 193 173 173 LEU LEU A . n 
A 1 194 GLY 194 174 174 GLY GLY A . n 
A 1 195 TYR 195 175 175 TYR TYR A . n 
A 1 196 TYR 196 176 176 TYR TYR A . n 
A 1 197 LEU 197 177 177 LEU LEU A . n 
A 1 198 GLY 198 178 178 GLY GLY A . n 
A 1 199 VAL 199 179 179 VAL VAL A . n 
A 1 200 HIS 200 180 180 HIS HIS A . n 
A 1 201 ALA 201 181 181 ALA ALA A . n 
A 1 202 PRO 202 182 182 PRO PRO A . n 
A 1 203 GLY 203 183 183 GLY GLY A . n 
A 1 204 HIS 204 184 184 HIS HIS A . n 
A 1 205 THR 205 185 185 THR THR A . n 
A 1 206 ASP 206 186 186 ASP ASP A . n 
A 1 207 LEU 207 187 187 LEU LEU A . n 
A 1 208 LYS 208 188 188 LYS LYS A . n 
A 1 209 ARG 209 189 189 ARG ARG A . n 
A 1 210 GLY 210 190 190 GLY GLY A . n 
A 1 211 LEU 211 191 191 LEU LEU A . n 
A 1 212 GLU 212 192 192 GLU GLU A . n 
A 1 213 ALA 213 193 193 ALA ALA A . n 
A 1 214 SER 214 194 194 SER SER A . n 
A 1 215 HIS 215 195 195 HIS HIS A . n 
A 1 216 ASN 216 196 196 ASN ASN A . n 
A 1 217 LEU 217 197 197 LEU LEU A . n 
A 1 218 LEU 218 198 198 LEU LEU A . n 
A 1 219 LEU 219 199 199 LEU LEU A . n 
A 1 220 GLY 220 200 200 GLY GLY A . n 
A 1 221 HIS 221 201 201 HIS HIS A . n 
A 1 222 GLY 222 202 202 GLY GLY A . n 
A 1 223 LEU 223 203 203 LEU LEU A . n 
A 1 224 ALA 224 204 204 ALA ALA A . n 
A 1 225 VAL 225 205 205 VAL VAL A . n 
A 1 226 GLN 226 206 206 GLN GLN A . n 
A 1 227 ALA 227 207 207 ALA ALA A . n 
A 1 228 MET 228 208 208 MET MET A . n 
A 1 229 ARG 229 209 209 ARG ARG A . n 
A 1 230 ALA 230 210 210 ALA ALA A . n 
A 1 231 ALA 231 211 211 ALA ALA A . n 
A 1 232 ALA 232 212 212 ALA ALA A . n 
A 1 233 PRO 233 213 213 PRO PRO A . n 
A 1 234 GLN 234 214 214 GLN GLN A . n 
A 1 235 PRO 235 215 215 PRO PRO A . n 
A 1 236 LEU 236 216 216 LEU LEU A . n 
A 1 237 GLN 237 217 217 GLN GLN A . n 
A 1 238 ILE 238 218 218 ILE ILE A . n 
A 1 239 GLY 239 219 219 GLY GLY A . n 
A 1 240 ILE 240 220 220 ILE ILE A . n 
A 1 241 VAL 241 221 221 VAL VAL A . n 
A 1 242 LEU 242 222 222 LEU LEU A . n 
A 1 243 ASN 243 223 223 ASN ASN A . n 
A 1 244 LEU 244 224 224 LEU LEU A . n 
A 1 245 THR 245 225 225 THR THR A . n 
A 1 246 PRO 246 226 226 PRO PRO A . n 
A 1 247 THR 247 227 227 THR THR A . n 
A 1 248 TYR 248 228 228 TYR TYR A . n 
A 1 249 PRO 249 229 229 PRO PRO A . n 
A 1 250 ALA 250 230 230 ALA ALA A . n 
A 1 251 SER 251 231 231 SER SER A . n 
A 1 252 ASP 252 232 232 ASP ASP A . n 
A 1 253 SER 253 233 233 SER SER A . n 
A 1 254 PRO 254 234 234 PRO PRO A . n 
A 1 255 GLU 255 235 235 GLU GLU A . n 
A 1 256 ASP 256 236 236 ASP ASP A . n 
A 1 257 VAL 257 237 237 VAL VAL A . n 
A 1 258 ALA 258 238 238 ALA ALA A . n 
A 1 259 ALA 259 239 239 ALA ALA A . n 
A 1 260 ALA 260 240 240 ALA ALA A . n 
A 1 261 ARG 261 241 241 ARG ARG A . n 
A 1 262 ARG 262 242 242 ARG ARG A . n 
A 1 263 PHE 263 243 243 PHE PHE A . n 
A 1 264 ASP 264 244 244 ASP ASP A . n 
A 1 265 GLY 265 245 245 GLY GLY A . n 
A 1 266 PHE 266 246 246 PHE PHE A . n 
A 1 267 VAL 267 247 247 VAL VAL A . n 
A 1 268 ASN 268 248 248 ASN ASN A . n 
A 1 269 ARG 269 249 249 ARG ARG A . n 
A 1 270 TRP 270 250 250 TRP TRP A . n 
A 1 271 PHE 271 251 251 PHE PHE A . n 
A 1 272 LEU 272 252 252 LEU LEU A . n 
A 1 273 ASP 273 253 253 ASP ASP A . n 
A 1 274 PRO 274 254 254 PRO PRO A . n 
A 1 275 LEU 275 255 255 LEU LEU A . n 
A 1 276 ALA 276 256 256 ALA ALA A . n 
A 1 277 GLY 277 257 257 GLY GLY A . n 
A 1 278 ARG 278 258 258 ARG ARG A . n 
A 1 279 GLY 279 259 259 GLY GLY A . n 
A 1 280 TYR 280 260 260 TYR TYR A . n 
A 1 281 PRO 281 261 261 PRO PRO A . n 
A 1 282 GLN 282 262 262 GLN GLN A . n 
A 1 283 ASP 283 263 263 ASP ASP A . n 
A 1 284 MET 284 264 264 MET MET A . n 
A 1 285 LEU 285 265 265 LEU LEU A . n 
A 1 286 ASP 286 266 266 ASP ASP A . n 
A 1 287 TYR 287 267 267 TYR TYR A . n 
A 1 288 TYR 288 268 268 TYR TYR A . n 
A 1 289 GLY 289 269 269 GLY GLY A . n 
A 1 290 ALA 290 270 270 ALA ALA A . n 
A 1 291 ALA 291 271 271 ALA ALA A . n 
A 1 292 ALA 292 272 272 ALA ALA A . n 
A 1 293 PRO 293 273 273 PRO PRO A . n 
A 1 294 GLN 294 274 274 GLN GLN A . n 
A 1 295 ALA 295 275 275 ALA ALA A . n 
A 1 296 ASN 296 276 276 ASN ASN A . n 
A 1 297 PRO 297 277 277 PRO PRO A . n 
A 1 298 GLU 298 278 278 GLU GLU A . n 
A 1 299 ASP 299 279 279 ASP ASP A . n 
A 1 300 LEU 300 280 280 LEU LEU A . n 
A 1 301 THR 301 281 281 THR THR A . n 
A 1 302 GLN 302 282 282 GLN GLN A . n 
A 1 303 ILE 303 283 283 ILE ILE A . n 
A 1 304 ALA 304 284 284 ALA ALA A . n 
A 1 305 ALA 305 285 285 ALA ALA A . n 
A 1 306 PRO 306 286 286 PRO PRO A . n 
A 1 307 LEU 307 287 287 LEU LEU A . n 
A 1 308 ASP 308 288 288 ASP ASP A . n 
A 1 309 TRP 309 289 289 TRP TRP A . n 
A 1 310 LEU 310 290 290 LEU LEU A . n 
A 1 311 GLY 311 291 291 GLY GLY A . n 
A 1 312 VAL 312 292 292 VAL VAL A . n 
A 1 313 ASN 313 293 293 ASN ASN A . n 
A 1 314 TYR 314 294 294 TYR TYR A . n 
A 1 315 TYR 315 295 295 TYR TYR A . n 
A 1 316 GLU 316 296 296 GLU GLU A . n 
A 1 317 ARG 317 297 297 ARG ARG A . n 
A 1 318 MET 318 298 298 MET MET A . n 
A 1 319 ARG 319 299 299 ARG ARG A . n 
A 1 320 ALA 320 300 300 ALA ALA A . n 
A 1 321 VAL 321 301 301 VAL VAL A . n 
A 1 322 ASP 322 302 302 ASP ASP A . n 
A 1 323 ALA 323 303 303 ALA ALA A . n 
A 1 324 PRO 324 304 304 PRO PRO A . n 
A 1 325 ASP 325 305 305 ASP ASP A . n 
A 1 326 ALA 326 306 306 ALA ALA A . n 
A 1 327 SER 327 307 307 SER SER A . n 
A 1 328 LEU 328 308 308 LEU LEU A . n 
A 1 329 PRO 329 309 309 PRO PRO A . n 
A 1 330 GLN 330 310 310 GLN GLN A . n 
A 1 331 ALA 331 311 311 ALA ALA A . n 
A 1 332 GLN 332 312 312 GLN GLN A . n 
A 1 333 ARG 333 313 313 ARG ARG A . n 
A 1 334 LEU 334 314 314 LEU LEU A . n 
A 1 335 ASP 335 315 315 ASP ASP A . n 
A 1 336 ASP 336 316 316 ASP ASP A . n 
A 1 337 PRO 337 317 317 PRO PRO A . n 
A 1 338 ASP 338 318 318 ASP ASP A . n 
A 1 339 LEU 339 319 319 LEU LEU A . n 
A 1 340 PRO 340 320 320 PRO PRO A . n 
A 1 341 HIS 341 321 321 HIS HIS A . n 
A 1 342 THR 342 322 322 THR THR A . n 
A 1 343 ALA 343 323 323 ALA ALA A . n 
A 1 344 ASP 344 324 324 ASP ASP A . n 
A 1 345 ARG 345 325 325 ARG ARG A . n 
A 1 346 GLU 346 326 326 GLU GLU A . n 
A 1 347 VAL 347 327 327 VAL VAL A . n 
A 1 348 TYR 348 328 328 TYR TYR A . n 
A 1 349 PRO 349 329 329 PRO PRO A . n 
A 1 350 GLU 350 330 330 GLU GLU A . n 
A 1 351 GLY 351 331 331 GLY GLY A . n 
A 1 352 LEU 352 332 332 LEU LEU A . n 
A 1 353 TYR 353 333 333 TYR TYR A . n 
A 1 354 ASP 354 334 334 ASP ASP A . n 
A 1 355 ILE 355 335 335 ILE ILE A . n 
A 1 356 LEU 356 336 336 LEU LEU A . n 
A 1 357 LEU 357 337 337 LEU LEU A . n 
A 1 358 ARG 358 338 338 ARG ARG A . n 
A 1 359 LEU 359 339 339 LEU LEU A . n 
A 1 360 HIS 360 340 340 HIS HIS A . n 
A 1 361 ASN 361 341 341 ASN ASN A . n 
A 1 362 ASP 362 342 342 ASP ASP A . n 
A 1 363 TYR 363 343 343 TYR TYR A . n 
A 1 364 PRO 364 344 344 PRO PRO A . n 
A 1 365 PHE 365 345 345 PHE PHE A . n 
A 1 366 ARG 366 346 346 ARG ARG A . n 
A 1 367 PRO 367 347 347 PRO PRO A . n 
A 1 368 LEU 368 348 348 LEU LEU A . n 
A 1 369 TYR 369 349 349 TYR TYR A . n 
A 1 370 ILE 370 350 350 ILE ILE A . n 
A 1 371 THR 371 351 351 THR THR A . n 
A 1 372 GLN 372 352 352 GLN GLN A . n 
A 1 373 ASN 373 353 353 ASN ASN A . n 
A 1 374 GLY 374 354 354 GLY GLY A . n 
A 1 375 CYS 375 355 355 CYS CYS A . n 
A 1 376 ALA 376 356 356 ALA ALA A . n 
A 1 377 LEU 377 357 357 LEU LEU A . n 
A 1 378 HIS 378 358 358 HIS HIS A . n 
A 1 379 ASP 379 359 359 ASP ASP A . n 
A 1 380 GLU 380 360 360 GLU GLU A . n 
A 1 381 ILE 381 361 361 ILE ILE A . n 
A 1 382 ALA 382 362 362 ALA ALA A . n 
A 1 383 GLU 383 363 363 GLU GLU A . n 
A 1 384 ASP 384 364 364 ASP ASP A . n 
A 1 385 GLY 385 365 365 GLY GLY A . n 
A 1 386 GLY 386 366 366 GLY GLY A . n 
A 1 387 ILE 387 367 367 ILE ILE A . n 
A 1 388 HIS 388 368 368 HIS HIS A . n 
A 1 389 ASP 389 369 369 ASP ASP A . n 
A 1 390 GLY 390 370 370 GLY GLY A . n 
A 1 391 GLN 391 371 371 GLN GLN A . n 
A 1 392 ARG 392 372 372 ARG ARG A . n 
A 1 393 GLN 393 373 373 GLN GLN A . n 
A 1 394 ALA 394 374 374 ALA ALA A . n 
A 1 395 PHE 395 375 375 PHE PHE A . n 
A 1 396 PHE 396 376 376 PHE PHE A . n 
A 1 397 GLU 397 377 377 GLU GLU A . n 
A 1 398 ALA 398 378 378 ALA ALA A . n 
A 1 399 HIS 399 379 379 HIS HIS A . n 
A 1 400 LEU 400 380 380 LEU LEU A . n 
A 1 401 ALA 401 381 381 ALA ALA A . n 
A 1 402 GLN 402 382 382 GLN GLN A . n 
A 1 403 LEU 403 383 383 LEU LEU A . n 
A 1 404 GLN 404 384 384 GLN GLN A . n 
A 1 405 ARG 405 385 385 ARG ARG A . n 
A 1 406 ALA 406 386 386 ALA ALA A . n 
A 1 407 LEU 407 387 387 LEU LEU A . n 
A 1 408 ALA 408 388 388 ALA ALA A . n 
A 1 409 ALA 409 389 389 ALA ALA A . n 
A 1 410 GLY 410 390 390 GLY GLY A . n 
A 1 411 VAL 411 391 391 VAL VAL A . n 
A 1 412 PRO 412 392 392 PRO PRO A . n 
A 1 413 LEU 413 393 393 LEU LEU A . n 
A 1 414 LYS 414 394 394 LYS LYS A . n 
A 1 415 GLY 415 395 395 GLY GLY A . n 
A 1 416 TYR 416 396 396 TYR TYR A . n 
A 1 417 PHE 417 397 397 PHE PHE A . n 
A 1 418 ALA 418 398 398 ALA ALA A . n 
A 1 419 TRP 419 399 399 TRP TRP A . n 
A 1 420 SER 420 400 400 SER SER A . n 
A 1 421 LEU 421 401 401 LEU LEU A . n 
A 1 422 LEU 422 402 402 LEU LEU A . n 
A 1 423 ASP 423 403 403 ASP ASP A . n 
A 1 424 ASN 424 404 404 ASN ASN A . n 
A 1 425 PHE 425 405 405 PHE PHE A . n 
A 1 426 GLU 426 406 406 GLU GLU A . n 
A 1 427 TRP 427 407 407 TRP TRP A . n 
A 1 428 ALA 428 408 408 ALA ALA A . n 
A 1 429 MET 429 409 409 MET MET A . n 
A 1 430 GLY 430 410 410 GLY GLY A . n 
A 1 431 LEU 431 411 411 LEU LEU A . n 
A 1 432 SER 432 412 412 SER SER A . n 
A 1 433 MET 433 413 413 MET MET A . n 
A 1 434 ARG 434 414 414 ARG ARG A . n 
A 1 435 TYR 435 415 415 TYR TYR A . n 
A 1 436 GLY 436 416 416 GLY GLY A . n 
A 1 437 ILE 437 417 417 ILE ILE A . n 
A 1 438 CYS 438 418 418 CYS CYS A . n 
A 1 439 TYR 439 419 419 TYR TYR A . n 
A 1 440 THR 440 420 420 THR THR A . n 
A 1 441 ASN 441 421 421 ASN ASN A . n 
A 1 442 PHE 442 422 422 PHE PHE A . n 
A 1 443 GLU 443 423 423 GLU GLU A . n 
A 1 444 THR 444 424 424 THR THR A . n 
A 1 445 LEU 445 425 425 LEU LEU A . n 
A 1 446 GLU 446 426 426 GLU GLU A . n 
A 1 447 ARG 447 427 427 ARG ARG A . n 
A 1 448 ARG 448 428 428 ARG ARG A . n 
A 1 449 ILE 449 429 429 ILE ILE A . n 
A 1 450 LYS 450 430 430 LYS LYS A . n 
A 1 451 ASP 451 431 431 ASP ASP A . n 
A 1 452 SER 452 432 432 SER SER A . n 
A 1 453 GLY 453 433 433 GLY GLY A . n 
A 1 454 TYR 454 434 434 TYR TYR A . n 
A 1 455 TRP 455 435 435 TRP TRP A . n 
A 1 456 LEU 456 436 436 LEU LEU A . n 
A 1 457 ARG 457 437 437 ARG ARG A . n 
A 1 458 ASP 458 438 438 ASP ASP A . n 
A 1 459 PHE 459 439 439 PHE PHE A . n 
A 1 460 ILE 460 440 440 ILE ILE A . n 
A 1 461 ALA 461 441 441 ALA ALA A . n 
A 1 462 GLY 462 442 442 GLY GLY A . n 
A 1 463 GLN 463 443 443 GLN GLN A . n 
A 1 464 ARG 464 444 ?   ?   ?   A . n 
A 1 465 GLY 465 445 ?   ?   ?   A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 BGC 1 C BGC 1 C BGC 1 n 
B 2 BGC 2 C BGC 2 C BGC 2 n 
C 2 BGC 1 B BGC 1 B BGC 1 n 
C 2 BGC 2 B BGC 2 B BGC 2 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        BGC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   BGC 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 3 NHE 1   501 1   NHE NHE A . 
E 4 NA  1   502 3   NA  NA  A . 
F 5 MLA 1   503 10  MLA MLA A . 
G 5 MLA 1   504 11  MLA MLA A . 
H 6 HOH 1   601 94  HOH HOH A . 
H 6 HOH 2   602 133 HOH HOH A . 
H 6 HOH 3   603 106 HOH HOH A . 
H 6 HOH 4   604 189 HOH HOH A . 
H 6 HOH 5   605 250 HOH HOH A . 
H 6 HOH 6   606 194 HOH HOH A . 
H 6 HOH 7   607 104 HOH HOH A . 
H 6 HOH 8   608 205 HOH HOH A . 
H 6 HOH 9   609 34  HOH HOH A . 
H 6 HOH 10  610 243 HOH HOH A . 
H 6 HOH 11  611 72  HOH HOH A . 
H 6 HOH 12  612 46  HOH HOH A . 
H 6 HOH 13  613 44  HOH HOH A . 
H 6 HOH 14  614 53  HOH HOH A . 
H 6 HOH 15  615 208 HOH HOH A . 
H 6 HOH 16  616 172 HOH HOH A . 
H 6 HOH 17  617 210 HOH HOH A . 
H 6 HOH 18  618 193 HOH HOH A . 
H 6 HOH 19  619 137 HOH HOH A . 
H 6 HOH 20  620 241 HOH HOH A . 
H 6 HOH 21  621 162 HOH HOH A . 
H 6 HOH 22  622 235 HOH HOH A . 
H 6 HOH 23  623 32  HOH HOH A . 
H 6 HOH 24  624 28  HOH HOH A . 
H 6 HOH 25  625 183 HOH HOH A . 
H 6 HOH 26  626 213 HOH HOH A . 
H 6 HOH 27  627 134 HOH HOH A . 
H 6 HOH 28  628 198 HOH HOH A . 
H 6 HOH 29  629 109 HOH HOH A . 
H 6 HOH 30  630 153 HOH HOH A . 
H 6 HOH 31  631 211 HOH HOH A . 
H 6 HOH 32  632 140 HOH HOH A . 
H 6 HOH 33  633 76  HOH HOH A . 
H 6 HOH 34  634 221 HOH HOH A . 
H 6 HOH 35  635 5   HOH HOH A . 
H 6 HOH 36  636 18  HOH HOH A . 
H 6 HOH 37  637 242 HOH HOH A . 
H 6 HOH 38  638 13  HOH HOH A . 
H 6 HOH 39  639 47  HOH HOH A . 
H 6 HOH 40  640 168 HOH HOH A . 
H 6 HOH 41  641 82  HOH HOH A . 
H 6 HOH 42  642 73  HOH HOH A . 
H 6 HOH 43  643 248 HOH HOH A . 
H 6 HOH 44  644 152 HOH HOH A . 
H 6 HOH 45  645 234 HOH HOH A . 
H 6 HOH 46  646 16  HOH HOH A . 
H 6 HOH 47  647 74  HOH HOH A . 
H 6 HOH 48  648 63  HOH HOH A . 
H 6 HOH 49  649 111 HOH HOH A . 
H 6 HOH 50  650 77  HOH HOH A . 
H 6 HOH 51  651 107 HOH HOH A . 
H 6 HOH 52  652 181 HOH HOH A . 
H 6 HOH 53  653 136 HOH HOH A . 
H 6 HOH 54  654 90  HOH HOH A . 
H 6 HOH 55  655 29  HOH HOH A . 
H 6 HOH 56  656 238 HOH HOH A . 
H 6 HOH 57  657 80  HOH HOH A . 
H 6 HOH 58  658 130 HOH HOH A . 
H 6 HOH 59  659 61  HOH HOH A . 
H 6 HOH 60  660 244 HOH HOH A . 
H 6 HOH 61  661 25  HOH HOH A . 
H 6 HOH 62  662 184 HOH HOH A . 
H 6 HOH 63  663 24  HOH HOH A . 
H 6 HOH 64  664 200 HOH HOH A . 
H 6 HOH 65  665 110 HOH HOH A . 
H 6 HOH 66  666 186 HOH HOH A . 
H 6 HOH 67  667 67  HOH HOH A . 
H 6 HOH 68  668 132 HOH HOH A . 
H 6 HOH 69  669 86  HOH HOH A . 
H 6 HOH 70  670 245 HOH HOH A . 
H 6 HOH 71  671 93  HOH HOH A . 
H 6 HOH 72  672 92  HOH HOH A . 
H 6 HOH 73  673 192 HOH HOH A . 
H 6 HOH 74  674 42  HOH HOH A . 
H 6 HOH 75  675 8   HOH HOH A . 
H 6 HOH 76  676 223 HOH HOH A . 
H 6 HOH 77  677 139 HOH HOH A . 
H 6 HOH 78  678 37  HOH HOH A . 
H 6 HOH 79  679 252 HOH HOH A . 
H 6 HOH 80  680 52  HOH HOH A . 
H 6 HOH 81  681 48  HOH HOH A . 
H 6 HOH 82  682 36  HOH HOH A . 
H 6 HOH 83  683 116 HOH HOH A . 
H 6 HOH 84  684 102 HOH HOH A . 
H 6 HOH 85  685 145 HOH HOH A . 
H 6 HOH 86  686 196 HOH HOH A . 
H 6 HOH 87  687 51  HOH HOH A . 
H 6 HOH 88  688 113 HOH HOH A . 
H 6 HOH 89  689 33  HOH HOH A . 
H 6 HOH 90  690 128 HOH HOH A . 
H 6 HOH 91  691 126 HOH HOH A . 
H 6 HOH 92  692 166 HOH HOH A . 
H 6 HOH 93  693 173 HOH HOH A . 
H 6 HOH 94  694 27  HOH HOH A . 
H 6 HOH 95  695 40  HOH HOH A . 
H 6 HOH 96  696 21  HOH HOH A . 
H 6 HOH 97  697 97  HOH HOH A . 
H 6 HOH 98  698 39  HOH HOH A . 
H 6 HOH 99  699 12  HOH HOH A . 
H 6 HOH 100 700 4   HOH HOH A . 
H 6 HOH 101 701 83  HOH HOH A . 
H 6 HOH 102 702 91  HOH HOH A . 
H 6 HOH 103 703 149 HOH HOH A . 
H 6 HOH 104 704 105 HOH HOH A . 
H 6 HOH 105 705 69  HOH HOH A . 
H 6 HOH 106 706 165 HOH HOH A . 
H 6 HOH 107 707 55  HOH HOH A . 
H 6 HOH 108 708 1   HOH HOH A . 
H 6 HOH 109 709 108 HOH HOH A . 
H 6 HOH 110 710 50  HOH HOH A . 
H 6 HOH 111 711 151 HOH HOH A . 
H 6 HOH 112 712 123 HOH HOH A . 
H 6 HOH 113 713 121 HOH HOH A . 
H 6 HOH 114 714 9   HOH HOH A . 
H 6 HOH 115 715 23  HOH HOH A . 
H 6 HOH 116 716 190 HOH HOH A . 
H 6 HOH 117 717 219 HOH HOH A . 
H 6 HOH 118 718 96  HOH HOH A . 
H 6 HOH 119 719 232 HOH HOH A . 
H 6 HOH 120 720 89  HOH HOH A . 
H 6 HOH 121 721 147 HOH HOH A . 
H 6 HOH 122 722 3   HOH HOH A . 
H 6 HOH 123 723 22  HOH HOH A . 
H 6 HOH 124 724 11  HOH HOH A . 
H 6 HOH 125 725 201 HOH HOH A . 
H 6 HOH 126 726 144 HOH HOH A . 
H 6 HOH 127 727 160 HOH HOH A . 
H 6 HOH 128 728 10  HOH HOH A . 
H 6 HOH 129 729 85  HOH HOH A . 
H 6 HOH 130 730 38  HOH HOH A . 
H 6 HOH 131 731 15  HOH HOH A . 
H 6 HOH 132 732 103 HOH HOH A . 
H 6 HOH 133 733 202 HOH HOH A . 
H 6 HOH 134 734 178 HOH HOH A . 
H 6 HOH 135 735 216 HOH HOH A . 
H 6 HOH 136 736 122 HOH HOH A . 
H 6 HOH 137 737 70  HOH HOH A . 
H 6 HOH 138 738 117 HOH HOH A . 
H 6 HOH 139 739 66  HOH HOH A . 
H 6 HOH 140 740 62  HOH HOH A . 
H 6 HOH 141 741 20  HOH HOH A . 
H 6 HOH 142 742 88  HOH HOH A . 
H 6 HOH 143 743 156 HOH HOH A . 
H 6 HOH 144 744 19  HOH HOH A . 
H 6 HOH 145 745 56  HOH HOH A . 
H 6 HOH 146 746 226 HOH HOH A . 
H 6 HOH 147 747 101 HOH HOH A . 
H 6 HOH 148 748 225 HOH HOH A . 
H 6 HOH 149 749 57  HOH HOH A . 
H 6 HOH 150 750 79  HOH HOH A . 
H 6 HOH 151 751 119 HOH HOH A . 
H 6 HOH 152 752 45  HOH HOH A . 
H 6 HOH 153 753 240 HOH HOH A . 
H 6 HOH 154 754 87  HOH HOH A . 
H 6 HOH 155 755 174 HOH HOH A . 
H 6 HOH 156 756 84  HOH HOH A . 
H 6 HOH 157 757 2   HOH HOH A . 
H 6 HOH 158 758 203 HOH HOH A . 
H 6 HOH 159 759 17  HOH HOH A . 
H 6 HOH 160 760 141 HOH HOH A . 
H 6 HOH 161 761 81  HOH HOH A . 
H 6 HOH 162 762 14  HOH HOH A . 
H 6 HOH 163 763 7   HOH HOH A . 
H 6 HOH 164 764 129 HOH HOH A . 
H 6 HOH 165 765 115 HOH HOH A . 
H 6 HOH 166 766 60  HOH HOH A . 
H 6 HOH 167 767 43  HOH HOH A . 
H 6 HOH 168 768 191 HOH HOH A . 
H 6 HOH 169 769 59  HOH HOH A . 
H 6 HOH 170 770 220 HOH HOH A . 
H 6 HOH 171 771 199 HOH HOH A . 
H 6 HOH 172 772 155 HOH HOH A . 
H 6 HOH 173 773 247 HOH HOH A . 
H 6 HOH 174 774 251 HOH HOH A . 
H 6 HOH 175 775 135 HOH HOH A . 
H 6 HOH 176 776 68  HOH HOH A . 
H 6 HOH 177 777 228 HOH HOH A . 
H 6 HOH 178 778 143 HOH HOH A . 
H 6 HOH 179 779 185 HOH HOH A . 
H 6 HOH 180 780 98  HOH HOH A . 
H 6 HOH 181 781 65  HOH HOH A . 
H 6 HOH 182 782 131 HOH HOH A . 
H 6 HOH 183 783 229 HOH HOH A . 
H 6 HOH 184 784 154 HOH HOH A . 
H 6 HOH 185 785 100 HOH HOH A . 
H 6 HOH 186 786 95  HOH HOH A . 
H 6 HOH 187 787 49  HOH HOH A . 
H 6 HOH 188 788 35  HOH HOH A . 
H 6 HOH 189 789 170 HOH HOH A . 
H 6 HOH 190 790 58  HOH HOH A . 
H 6 HOH 191 791 175 HOH HOH A . 
H 6 HOH 192 792 158 HOH HOH A . 
H 6 HOH 193 793 148 HOH HOH A . 
H 6 HOH 194 794 179 HOH HOH A . 
H 6 HOH 195 795 78  HOH HOH A . 
H 6 HOH 196 796 161 HOH HOH A . 
H 6 HOH 197 797 217 HOH HOH A . 
H 6 HOH 198 798 176 HOH HOH A . 
H 6 HOH 199 799 125 HOH HOH A . 
H 6 HOH 200 800 207 HOH HOH A . 
H 6 HOH 201 801 212 HOH HOH A . 
H 6 HOH 202 802 112 HOH HOH A . 
H 6 HOH 203 803 253 HOH HOH A . 
H 6 HOH 204 804 206 HOH HOH A . 
H 6 HOH 205 805 64  HOH HOH A . 
H 6 HOH 206 806 146 HOH HOH A . 
H 6 HOH 207 807 224 HOH HOH A . 
H 6 HOH 208 808 177 HOH HOH A . 
H 6 HOH 209 809 227 HOH HOH A . 
H 6 HOH 210 810 215 HOH HOH A . 
H 6 HOH 211 811 239 HOH HOH A . 
H 6 HOH 212 812 138 HOH HOH A . 
H 6 HOH 213 813 204 HOH HOH A . 
H 6 HOH 214 814 99  HOH HOH A . 
H 6 HOH 215 815 195 HOH HOH A . 
H 6 HOH 216 816 54  HOH HOH A . 
H 6 HOH 217 817 75  HOH HOH A . 
H 6 HOH 218 818 127 HOH HOH A . 
H 6 HOH 219 819 159 HOH HOH A . 
H 6 HOH 220 820 169 HOH HOH A . 
H 6 HOH 221 821 214 HOH HOH A . 
H 6 HOH 222 822 120 HOH HOH A . 
H 6 HOH 223 823 236 HOH HOH A . 
H 6 HOH 224 824 124 HOH HOH A . 
H 6 HOH 225 825 249 HOH HOH A . 
H 6 HOH 226 826 197 HOH HOH A . 
H 6 HOH 227 827 142 HOH HOH A . 
H 6 HOH 228 828 114 HOH HOH A . 
H 6 HOH 229 829 231 HOH HOH A . 
H 6 HOH 230 830 188 HOH HOH A . 
H 6 HOH 231 831 218 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0411 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8WN6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.542 
_cell.length_a_esd                 ? 
_cell.length_b                     68.978 
_cell.length_b_esd                 ? 
_cell.length_c                     96.389 
_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                         8WN6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8WN6 
_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             2.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.34 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              9.5 
_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    'CHES, K/Na tartrate, LiSO4' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            303 
# 
_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 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         2023-04-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_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 
_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                                       8WN6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.64 
_reflns.d_resolution_low                               48.31 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     55824 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.66 
_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                                0.03 
_reflns.pdbx_Rpim_I_all                                0.021 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.021 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.64 
_reflns_shell.d_res_low                                     1.67 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           11.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2703 
_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                               1.9 
_reflns_shell.pdbx_chi_squared                              0.42 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.056 
_reflns_shell.pdbx_Rpim_I_all                               0.039 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.993 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.039 
_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]                            1.72 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.79 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.93 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               12.183 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.957 
_refine.correlation_coeff_Fo_to_Fc_free          0.945 
_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                                 8WN6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.64 
_refine.ls_d_res_low                             48.31 
_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                     52974 
_refine.ls_number_reflns_R_free                  2850 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.90 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16621 
_refine.ls_R_factor_R_free                       0.19259 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16475 
_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                       0.087 
_refine.pdbx_overall_ESU_R_Free                  0.086 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             1.452 
_refine.overall_SU_ML                            0.051 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.64 
_refine_hist.d_res_low                        48.31 
_refine_hist.number_atoms_solvent             231 
_refine_hist.number_atoms_total               3767 
_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        3462 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         74 
_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' ? 0.011  0.012  3660 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3282 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.753  1.652  5000 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.607  1.571  7537 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.611  5.000  446  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 6.188  5.000  29   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.921 10.000 512  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.093  0.200  527  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  4388 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  896  ? 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' ? 1.399  1.124  1778 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.379  1.124  1778 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.039  2.014  2226 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.040  2.016  2227 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.250  1.375  1882 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.250  1.376  1883 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.518  2.410  2775 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.329  12.33  4197 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.328  12.33  4197 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.640 
_refine_ls_shell.d_res_low                        1.683 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             200 
_refine_ls_shell.number_reflns_R_work             3823 
_refine_ls_shell.percent_reflns_obs               99.04 
_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                  0.180 
_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                  0.223 
# 
_struct.entry_id                     8WN6 
_struct.title                        'Crystal structure of GH1 beta-glucosidase Td2F2 E352Q sophorose complex' 
_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        8WN6 
_struct_keywords.text            'beta-Glucosidase, E352Q nucleophile mutants, Sophorose complex, Hydrolase' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8WN6 
_struct_ref.pdbx_db_accession          8WN6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8WN6 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 465 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             8WN6 
_struct_ref_seq.db_align_beg                  -19 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  445 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       -19 
_struct_ref_seq.pdbx_auth_seq_align_end       445 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 ALA A 37  ? GLU A 42  ? ALA A 17  GLU A 22  1 ? 6  
HELX_P HELX_P2  AA2 ARG A 46  ? ARG A 50  ? ARG A 26  ARG A 30  5 ? 5  
HELX_P HELX_P3  AA3 SER A 53  ? HIS A 60  ? SER A 33  HIS A 40  1 ? 8  
HELX_P HELX_P4  AA4 ASP A 76  ? LEU A 91  ? ASP A 56  LEU A 71  1 ? 16 
HELX_P HELX_P5  AA5 ALA A 101 ? VAL A 106 ? ALA A 81  VAL A 86  1 ? 6  
HELX_P HELX_P6  AA6 ASN A 114 ? ALA A 131 ? ASN A 94  ALA A 111 1 ? 18 
HELX_P HELX_P7  AA7 PRO A 145 ? ASP A 150 ? PRO A 125 ASP A 130 1 ? 6  
HELX_P HELX_P8  AA8 ARG A 151 ? GLY A 155 ? ARG A 131 GLY A 135 5 ? 5  
HELX_P HELX_P9  AA9 SER A 156 ? GLY A 175 ? SER A 136 GLY A 155 1 ? 20 
HELX_P HELX_P10 AB1 GLU A 186 ? TYR A 196 ? GLU A 166 TYR A 176 1 ? 11 
HELX_P HELX_P11 AB2 ASP A 206 ? ALA A 232 ? ASP A 186 ALA A 212 1 ? 27 
HELX_P HELX_P12 AB3 SER A 253 ? ASN A 268 ? SER A 233 ASN A 248 1 ? 16 
HELX_P HELX_P13 AB4 ASN A 268 ? ALA A 276 ? ASN A 248 ALA A 256 1 ? 9  
HELX_P HELX_P14 AB5 PRO A 281 ? GLY A 289 ? PRO A 261 GLY A 269 1 ? 9  
HELX_P HELX_P15 AB6 ALA A 290 ? ALA A 292 ? ALA A 270 ALA A 272 5 ? 3  
HELX_P HELX_P16 AB7 ASN A 296 ? ALA A 304 ? ASN A 276 ALA A 284 1 ? 9  
HELX_P HELX_P17 AB8 PRO A 349 ? TYR A 363 ? PRO A 329 TYR A 343 1 ? 15 
HELX_P HELX_P18 AB9 ASP A 389 ? ALA A 409 ? ASP A 369 ALA A 389 1 ? 21 
HELX_P HELX_P19 AC1 GLU A 426 ? MET A 433 ? GLU A 406 MET A 413 5 ? 8  
HELX_P HELX_P20 AC2 LYS A 450 ? GLY A 462 ? LYS A 430 GLY A 442 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? B BGC .   O2 ? ? ? 1_555 B BGC . C1 ? ? C BGC 1   C BGC 2   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale2 covale both ? C BGC .   O2 ? ? ? 1_555 C BGC . C1 ? ? B BGC 1   B BGC 2   1_555 ? ? ? ? ? ? ? 1.493 ? ? 
metalc1 metalc ?    ? A HIS 341 O  ? ? ? 1_555 E NA  . NA ? ? A HIS 321 A NA  502 1_555 ? ? ? ? ? ? ? 2.537 ? ? 
metalc2 metalc ?    ? E NA  .   NA ? ? ? 1_555 H HOH . O  ? ? A NA  502 A HOH 614 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc3 metalc ?    ? E NA  .   NA ? ? ? 1_555 H HOH . O  ? ? A NA  502 A HOH 742 4_545 ? ? ? ? ? ? ? 2.947 ? ? 
metalc4 metalc ?    ? E NA  .   NA ? ? ? 1_555 H HOH . O  ? ? A NA  502 A HOH 776 1_555 ? ? ? ? ? ? ? 2.918 ? ? 
metalc5 metalc ?    ? E NA  .   NA ? ? ? 1_555 H HOH . O  ? ? A NA  502 A HOH 806 4_545 ? ? ? ? ? ? ? 2.457 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O ? A HIS 341 ? A HIS 321 ? 1_555 NA ? E NA . ? A NA 502 ? 1_555 O ? H HOH . ? A HOH 614 ? 1_555 82.8  ? 
2  O ? A HIS 341 ? A HIS 321 ? 1_555 NA ? E NA . ? A NA 502 ? 1_555 O ? H HOH . ? A HOH 742 ? 4_545 75.6  ? 
3  O ? H HOH .   ? A HOH 614 ? 1_555 NA ? E NA . ? A NA 502 ? 1_555 O ? H HOH . ? A HOH 742 ? 4_545 86.1  ? 
4  O ? A HIS 341 ? A HIS 321 ? 1_555 NA ? E NA . ? A NA 502 ? 1_555 O ? H HOH . ? A HOH 776 ? 1_555 79.1  ? 
5  O ? H HOH .   ? A HOH 614 ? 1_555 NA ? E NA . ? A NA 502 ? 1_555 O ? H HOH . ? A HOH 776 ? 1_555 151.6 ? 
6  O ? H HOH .   ? A HOH 742 ? 4_545 NA ? E NA . ? A NA 502 ? 1_555 O ? H HOH . ? A HOH 776 ? 1_555 68.3  ? 
7  O ? A HIS 341 ? A HIS 321 ? 1_555 NA ? E NA . ? A NA 502 ? 1_555 O ? H HOH . ? A HOH 806 ? 4_545 151.9 ? 
8  O ? H HOH .   ? A HOH 614 ? 1_555 NA ? E NA . ? A NA 502 ? 1_555 O ? H HOH . ? A HOH 806 ? 4_545 98.1  ? 
9  O ? H HOH .   ? A HOH 742 ? 4_545 NA ? E NA . ? A NA 502 ? 1_555 O ? H HOH . ? A HOH 806 ? 4_545 76.4  ? 
10 O ? H HOH .   ? A HOH 776 ? 1_555 NA ? E NA . ? A NA 502 ? 1_555 O ? H HOH . ? A HOH 806 ? 4_545 88.1  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 201 A . ? ALA 181 A PRO 202 A ? PRO 182 A 1 5.92  
2 LEU 328 A . ? LEU 308 A PRO 329 A ? PRO 309 A 1 10.47 
3 ARG 366 A . ? ARG 346 A PRO 367 A ? PRO 347 A 1 -7.14 
4 TRP 419 A . ? TRP 399 A SER 420 A ? SER 400 A 1 -8.66 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 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 VAL A 31  ? ALA A 35  ? VAL A 11  ALA A 15  
AA1 2 ALA A 95  ? SER A 99  ? ALA A 75  SER A 79  
AA1 3 GLN A 134 ? TYR A 140 ? GLN A 114 TYR A 120 
AA1 4 HIS A 180 ? ASN A 185 ? HIS A 160 ASN A 165 
AA1 5 GLN A 237 ? ASN A 243 ? GLN A 217 ASN A 223 
AA1 6 TRP A 309 ? ASN A 313 ? TRP A 289 ASN A 293 
AA1 7 LEU A 368 ? ASN A 373 ? LEU A 348 ASN A 353 
AA1 8 LEU A 413 ? TRP A 419 ? LEU A 393 TRP A 399 
AA1 9 VAL A 31  ? ALA A 35  ? VAL A 11  ALA A 15  
AA2 1 THR A 247 ? PRO A 249 ? THR A 227 PRO A 229 
AA2 2 MET A 318 ? ASP A 322 ? MET A 298 ASP A 302 
AA2 3 ALA A 331 ? ARG A 333 ? ALA A 311 ARG A 313 
AA3 1 CYS A 438 ? THR A 440 ? CYS A 418 THR A 420 
AA3 2 ARG A 447 ? ILE A 449 ? ARG A 427 ILE A 429 
# 
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 ALA A 34  ? N ALA A 14  O ARG A 97  ? O ARG A 77  
AA1 2 3 N PHE A 98  ? N PHE A 78  O THR A 138 ? O THR A 118 
AA1 3 4 N LEU A 139 ? N LEU A 119 O ALA A 182 ? O ALA A 162 
AA1 4 5 N TRP A 181 ? N TRP A 161 O GLY A 239 ? O GLY A 219 
AA1 5 6 N ILE A 240 ? N ILE A 220 O GLY A 311 ? O GLY A 291 
AA1 6 7 N VAL A 312 ? N VAL A 292 O TYR A 369 ? O TYR A 349 
AA1 7 8 N LEU A 368 ? N LEU A 348 O LYS A 414 ? O LYS A 394 
AA1 8 9 O TYR A 416 ? O TYR A 396 N VAL A 31  ? N VAL A 11  
AA2 1 2 N TYR A 248 ? N TYR A 228 O MET A 318 ? O MET A 298 
AA2 2 3 N VAL A 321 ? N VAL A 301 O GLN A 332 ? O GLN A 312 
AA3 1 2 N TYR A 439 ? N TYR A 419 O ARG A 448 ? O ARG A 428 
# 
_pdbx_entry_details.entry_id                   8WN6 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 54  ? ? 53.87   -121.35 
2 1 TRP A 122 ? ? 97.99   -0.13   
3 1 ASP A 123 ? ? -99.35  58.59   
4 1 LEU A 132 ? ? 90.74   -7.14   
5 1 THR A 163 ? ? -68.12  -72.65  
6 1 ASN A 248 ? ? -101.98 -61.34  
7 1 THR A 322 ? ? -88.09  -153.84 
8 1 ASP A 324 ? ? -140.07 -7.42   
9 1 TRP A 407 ? ? 58.61   -126.93 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     77 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.095 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -19 ? A MET 1   
2  1 Y 1 A GLY -18 ? A GLY 2   
3  1 Y 1 A SER -17 ? A SER 3   
4  1 Y 1 A SER -16 ? A SER 4   
5  1 Y 1 A HIS -15 ? A HIS 5   
6  1 Y 1 A HIS -14 ? A HIS 6   
7  1 Y 1 A HIS -13 ? A HIS 7   
8  1 Y 1 A HIS -12 ? A HIS 8   
9  1 Y 1 A HIS -11 ? A HIS 9   
10 1 Y 1 A HIS -10 ? A HIS 10  
11 1 Y 1 A SER -9  ? A SER 11  
12 1 Y 1 A SER -8  ? A SER 12  
13 1 Y 1 A GLY -7  ? A GLY 13  
14 1 Y 1 A LEU -6  ? A LEU 14  
15 1 Y 1 A VAL -5  ? A VAL 15  
16 1 Y 1 A PRO -4  ? A PRO 16  
17 1 Y 1 A ARG -3  ? A ARG 17  
18 1 Y 1 A GLY -2  ? A GLY 18  
19 1 Y 1 A SER -1  ? A SER 19  
20 1 Y 1 A HIS 0   ? A HIS 20  
21 1 Y 1 A MET 1   ? A MET 21  
22 1 Y 1 A ALA 2   ? A ALA 22  
23 1 Y 1 A ARG 444 ? A ARG 464 
24 1 Y 1 A GLY 445 ? A GLY 465 
25 1 N 0 A NA  502 ? E NA  ?   
# 
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  
BGC C2     C  N R 74  
BGC C3     C  N S 75  
BGC C4     C  N S 76  
BGC C5     C  N R 77  
BGC C6     C  N N 78  
BGC C1     C  N R 79  
BGC O1     O  N N 80  
BGC O2     O  N N 81  
BGC O3     O  N N 82  
BGC O4     O  N N 83  
BGC O5     O  N N 84  
BGC O6     O  N N 85  
BGC H2     H  N N 86  
BGC H3     H  N N 87  
BGC H4     H  N N 88  
BGC H5     H  N N 89  
BGC H61    H  N N 90  
BGC H62    H  N N 91  
BGC H1     H  N N 92  
BGC HO1    H  N N 93  
BGC HO2    H  N N 94  
BGC HO3    H  N N 95  
BGC HO4    H  N N 96  
BGC HO6    H  N N 97  
CYS N      N  N N 98  
CYS CA     C  N R 99  
CYS C      C  N N 100 
CYS O      O  N N 101 
CYS CB     C  N N 102 
CYS SG     S  N N 103 
CYS OXT    O  N N 104 
CYS H      H  N N 105 
CYS H2     H  N N 106 
CYS HA     H  N N 107 
CYS HB2    H  N N 108 
CYS HB3    H  N N 109 
CYS HG     H  N N 110 
CYS HXT    H  N N 111 
GLN N      N  N N 112 
GLN CA     C  N S 113 
GLN C      C  N N 114 
GLN O      O  N N 115 
GLN CB     C  N N 116 
GLN CG     C  N N 117 
GLN CD     C  N N 118 
GLN OE1    O  N N 119 
GLN NE2    N  N N 120 
GLN OXT    O  N N 121 
GLN H      H  N N 122 
GLN H2     H  N N 123 
GLN HA     H  N N 124 
GLN HB2    H  N N 125 
GLN HB3    H  N N 126 
GLN HG2    H  N N 127 
GLN HG3    H  N N 128 
GLN HE21   H  N N 129 
GLN HE22   H  N N 130 
GLN HXT    H  N N 131 
GLU N      N  N N 132 
GLU CA     C  N S 133 
GLU C      C  N N 134 
GLU O      O  N N 135 
GLU CB     C  N N 136 
GLU CG     C  N N 137 
GLU CD     C  N N 138 
GLU OE1    O  N N 139 
GLU OE2    O  N N 140 
GLU OXT    O  N N 141 
GLU H      H  N N 142 
GLU H2     H  N N 143 
GLU HA     H  N N 144 
GLU HB2    H  N N 145 
GLU HB3    H  N N 146 
GLU HG2    H  N N 147 
GLU HG3    H  N N 148 
GLU HE2    H  N N 149 
GLU HXT    H  N N 150 
GLY N      N  N N 151 
GLY CA     C  N N 152 
GLY C      C  N N 153 
GLY O      O  N N 154 
GLY OXT    O  N N 155 
GLY H      H  N N 156 
GLY H2     H  N N 157 
GLY HA2    H  N N 158 
GLY HA3    H  N N 159 
GLY HXT    H  N N 160 
HIS N      N  N N 161 
HIS CA     C  N S 162 
HIS C      C  N N 163 
HIS O      O  N N 164 
HIS CB     C  N N 165 
HIS CG     C  Y N 166 
HIS ND1    N  Y N 167 
HIS CD2    C  Y N 168 
HIS CE1    C  Y N 169 
HIS NE2    N  Y N 170 
HIS OXT    O  N N 171 
HIS H      H  N N 172 
HIS H2     H  N N 173 
HIS HA     H  N N 174 
HIS HB2    H  N N 175 
HIS HB3    H  N N 176 
HIS HD1    H  N N 177 
HIS HD2    H  N N 178 
HIS HE1    H  N N 179 
HIS HE2    H  N N 180 
HIS HXT    H  N N 181 
HOH O      O  N N 182 
HOH H1     H  N N 183 
HOH H2     H  N N 184 
ILE N      N  N N 185 
ILE CA     C  N S 186 
ILE C      C  N N 187 
ILE O      O  N N 188 
ILE CB     C  N S 189 
ILE CG1    C  N N 190 
ILE CG2    C  N N 191 
ILE CD1    C  N N 192 
ILE OXT    O  N N 193 
ILE H      H  N N 194 
ILE H2     H  N N 195 
ILE HA     H  N N 196 
ILE HB     H  N N 197 
ILE HG12   H  N N 198 
ILE HG13   H  N N 199 
ILE HG21   H  N N 200 
ILE HG22   H  N N 201 
ILE HG23   H  N N 202 
ILE HD11   H  N N 203 
ILE HD12   H  N N 204 
ILE HD13   H  N N 205 
ILE HXT    H  N N 206 
LEU N      N  N N 207 
LEU CA     C  N S 208 
LEU C      C  N N 209 
LEU O      O  N N 210 
LEU CB     C  N N 211 
LEU CG     C  N N 212 
LEU CD1    C  N N 213 
LEU CD2    C  N N 214 
LEU OXT    O  N N 215 
LEU H      H  N N 216 
LEU H2     H  N N 217 
LEU HA     H  N N 218 
LEU HB2    H  N N 219 
LEU HB3    H  N N 220 
LEU HG     H  N N 221 
LEU HD11   H  N N 222 
LEU HD12   H  N N 223 
LEU HD13   H  N N 224 
LEU HD21   H  N N 225 
LEU HD22   H  N N 226 
LEU HD23   H  N N 227 
LEU HXT    H  N N 228 
LYS N      N  N N 229 
LYS CA     C  N S 230 
LYS C      C  N N 231 
LYS O      O  N N 232 
LYS CB     C  N N 233 
LYS CG     C  N N 234 
LYS CD     C  N N 235 
LYS CE     C  N N 236 
LYS NZ     N  N N 237 
LYS OXT    O  N N 238 
LYS H      H  N N 239 
LYS H2     H  N N 240 
LYS HA     H  N N 241 
LYS HB2    H  N N 242 
LYS HB3    H  N N 243 
LYS HG2    H  N N 244 
LYS HG3    H  N N 245 
LYS HD2    H  N N 246 
LYS HD3    H  N N 247 
LYS HE2    H  N N 248 
LYS HE3    H  N N 249 
LYS HZ1    H  N N 250 
LYS HZ2    H  N N 251 
LYS HZ3    H  N N 252 
LYS HXT    H  N N 253 
MET N      N  N N 254 
MET CA     C  N S 255 
MET C      C  N N 256 
MET O      O  N N 257 
MET CB     C  N N 258 
MET CG     C  N N 259 
MET SD     S  N N 260 
MET CE     C  N N 261 
MET OXT    O  N N 262 
MET H      H  N N 263 
MET H2     H  N N 264 
MET HA     H  N N 265 
MET HB2    H  N N 266 
MET HB3    H  N N 267 
MET HG2    H  N N 268 
MET HG3    H  N N 269 
MET HE1    H  N N 270 
MET HE2    H  N N 271 
MET HE3    H  N N 272 
MET HXT    H  N N 273 
MLA C1     C  N N 274 
MLA O1A    O  N N 275 
MLA O1B    O  N N 276 
MLA C2     C  N N 277 
MLA C3     C  N N 278 
MLA O3A    O  N N 279 
MLA O3B    O  N N 280 
MLA H1A    H  N N 281 
MLA HC21   H  N N 282 
MLA HC22   H  N N 283 
MLA H3B    H  N N 284 
NA  NA     NA N N 285 
NHE "C3'"  C  N N 286 
NHE "C2'"  C  N N 287 
NHE "C1'"  C  N N 288 
NHE "C6'"  C  N N 289 
NHE N      N  N N 290 
NHE C1     C  N N 291 
NHE C2     C  N N 292 
NHE S      S  N N 293 
NHE O1     O  N N 294 
NHE O2     O  N N 295 
NHE O3     O  N N 296 
NHE "C5'"  C  N N 297 
NHE "C4'"  C  N N 298 
NHE "H3'1" H  N N 299 
NHE "H3'2" H  N N 300 
NHE "H2'1" H  N N 301 
NHE "H2'2" H  N N 302 
NHE "HC'1" H  N N 303 
NHE "H6'1" H  N N 304 
NHE "H6'2" H  N N 305 
NHE HN     H  N N 306 
NHE HC11   H  N N 307 
NHE HC12   H  N N 308 
NHE HC21   H  N N 309 
NHE HC22   H  N N 310 
NHE HO3    H  N N 311 
NHE "H5'1" H  N N 312 
NHE "H5'2" H  N N 313 
NHE "H4'1" H  N N 314 
NHE "H4'2" H  N N 315 
PHE N      N  N N 316 
PHE CA     C  N S 317 
PHE C      C  N N 318 
PHE O      O  N N 319 
PHE CB     C  N N 320 
PHE CG     C  Y N 321 
PHE CD1    C  Y N 322 
PHE CD2    C  Y N 323 
PHE CE1    C  Y N 324 
PHE CE2    C  Y N 325 
PHE CZ     C  Y N 326 
PHE OXT    O  N N 327 
PHE H      H  N N 328 
PHE H2     H  N N 329 
PHE HA     H  N N 330 
PHE HB2    H  N N 331 
PHE HB3    H  N N 332 
PHE HD1    H  N N 333 
PHE HD2    H  N N 334 
PHE HE1    H  N N 335 
PHE HE2    H  N N 336 
PHE HZ     H  N N 337 
PHE HXT    H  N N 338 
PRO N      N  N N 339 
PRO CA     C  N S 340 
PRO C      C  N N 341 
PRO O      O  N N 342 
PRO CB     C  N N 343 
PRO CG     C  N N 344 
PRO CD     C  N N 345 
PRO OXT    O  N N 346 
PRO H      H  N N 347 
PRO HA     H  N N 348 
PRO HB2    H  N N 349 
PRO HB3    H  N N 350 
PRO HG2    H  N N 351 
PRO HG3    H  N N 352 
PRO HD2    H  N N 353 
PRO HD3    H  N N 354 
PRO HXT    H  N N 355 
SER N      N  N N 356 
SER CA     C  N S 357 
SER C      C  N N 358 
SER O      O  N N 359 
SER CB     C  N N 360 
SER OG     O  N N 361 
SER OXT    O  N N 362 
SER H      H  N N 363 
SER H2     H  N N 364 
SER HA     H  N N 365 
SER HB2    H  N N 366 
SER HB3    H  N N 367 
SER HG     H  N N 368 
SER HXT    H  N N 369 
THR N      N  N N 370 
THR CA     C  N S 371 
THR C      C  N N 372 
THR O      O  N N 373 
THR CB     C  N R 374 
THR OG1    O  N N 375 
THR CG2    C  N N 376 
THR OXT    O  N N 377 
THR H      H  N N 378 
THR H2     H  N N 379 
THR HA     H  N N 380 
THR HB     H  N N 381 
THR HG1    H  N N 382 
THR HG21   H  N N 383 
THR HG22   H  N N 384 
THR HG23   H  N N 385 
THR HXT    H  N N 386 
TRP N      N  N N 387 
TRP CA     C  N S 388 
TRP C      C  N N 389 
TRP O      O  N N 390 
TRP CB     C  N N 391 
TRP CG     C  Y N 392 
TRP CD1    C  Y N 393 
TRP CD2    C  Y N 394 
TRP NE1    N  Y N 395 
TRP CE2    C  Y N 396 
TRP CE3    C  Y N 397 
TRP CZ2    C  Y N 398 
TRP CZ3    C  Y N 399 
TRP CH2    C  Y N 400 
TRP OXT    O  N N 401 
TRP H      H  N N 402 
TRP H2     H  N N 403 
TRP HA     H  N N 404 
TRP HB2    H  N N 405 
TRP HB3    H  N N 406 
TRP HD1    H  N N 407 
TRP HE1    H  N N 408 
TRP HE3    H  N N 409 
TRP HZ2    H  N N 410 
TRP HZ3    H  N N 411 
TRP HH2    H  N N 412 
TRP HXT    H  N N 413 
TYR N      N  N N 414 
TYR CA     C  N S 415 
TYR C      C  N N 416 
TYR O      O  N N 417 
TYR CB     C  N N 418 
TYR CG     C  Y N 419 
TYR CD1    C  Y N 420 
TYR CD2    C  Y N 421 
TYR CE1    C  Y N 422 
TYR CE2    C  Y N 423 
TYR CZ     C  Y N 424 
TYR OH     O  N N 425 
TYR OXT    O  N N 426 
TYR H      H  N N 427 
TYR H2     H  N N 428 
TYR HA     H  N N 429 
TYR HB2    H  N N 430 
TYR HB3    H  N N 431 
TYR HD1    H  N N 432 
TYR HD2    H  N N 433 
TYR HE1    H  N N 434 
TYR HE2    H  N N 435 
TYR HH     H  N N 436 
TYR HXT    H  N N 437 
VAL N      N  N N 438 
VAL CA     C  N S 439 
VAL C      C  N N 440 
VAL O      O  N N 441 
VAL CB     C  N N 442 
VAL CG1    C  N N 443 
VAL CG2    C  N N 444 
VAL OXT    O  N N 445 
VAL H      H  N N 446 
VAL H2     H  N N 447 
VAL HA     H  N N 448 
VAL HB     H  N N 449 
VAL HG11   H  N N 450 
VAL HG12   H  N N 451 
VAL HG13   H  N N 452 
VAL HG21   H  N N 453 
VAL HG22   H  N N 454 
VAL HG23   H  N N 455 
VAL HXT    H  N N 456 
# 
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  
BGC C2    C3     sing N N 70  
BGC C2    C1     sing N N 71  
BGC C2    O2     sing N N 72  
BGC C2    H2     sing N N 73  
BGC C3    C4     sing N N 74  
BGC C3    O3     sing N N 75  
BGC C3    H3     sing N N 76  
BGC C4    C5     sing N N 77  
BGC C4    O4     sing N N 78  
BGC C4    H4     sing N N 79  
BGC C5    C6     sing N N 80  
BGC C5    O5     sing N N 81  
BGC C5    H5     sing N N 82  
BGC C6    O6     sing N N 83  
BGC C6    H61    sing N N 84  
BGC C6    H62    sing N N 85  
BGC C1    O1     sing N N 86  
BGC C1    O5     sing N N 87  
BGC C1    H1     sing N N 88  
BGC O1    HO1    sing N N 89  
BGC O2    HO2    sing N N 90  
BGC O3    HO3    sing N N 91  
BGC O4    HO4    sing N N 92  
BGC O6    HO6    sing N N 93  
CYS N     CA     sing N N 94  
CYS N     H      sing N N 95  
CYS N     H2     sing N N 96  
CYS CA    C      sing N N 97  
CYS CA    CB     sing N N 98  
CYS CA    HA     sing N N 99  
CYS C     O      doub N N 100 
CYS C     OXT    sing N N 101 
CYS CB    SG     sing N N 102 
CYS CB    HB2    sing N N 103 
CYS CB    HB3    sing N N 104 
CYS SG    HG     sing N N 105 
CYS OXT   HXT    sing N N 106 
GLN N     CA     sing N N 107 
GLN N     H      sing N N 108 
GLN N     H2     sing N N 109 
GLN CA    C      sing N N 110 
GLN CA    CB     sing N N 111 
GLN CA    HA     sing N N 112 
GLN C     O      doub N N 113 
GLN C     OXT    sing N N 114 
GLN CB    CG     sing N N 115 
GLN CB    HB2    sing N N 116 
GLN CB    HB3    sing N N 117 
GLN CG    CD     sing N N 118 
GLN CG    HG2    sing N N 119 
GLN CG    HG3    sing N N 120 
GLN CD    OE1    doub N N 121 
GLN CD    NE2    sing N N 122 
GLN NE2   HE21   sing N N 123 
GLN NE2   HE22   sing N N 124 
GLN OXT   HXT    sing N N 125 
GLU N     CA     sing N N 126 
GLU N     H      sing N N 127 
GLU N     H2     sing N N 128 
GLU CA    C      sing N N 129 
GLU CA    CB     sing N N 130 
GLU CA    HA     sing N N 131 
GLU C     O      doub N N 132 
GLU C     OXT    sing N N 133 
GLU CB    CG     sing N N 134 
GLU CB    HB2    sing N N 135 
GLU CB    HB3    sing N N 136 
GLU CG    CD     sing N N 137 
GLU CG    HG2    sing N N 138 
GLU CG    HG3    sing N N 139 
GLU CD    OE1    doub N N 140 
GLU CD    OE2    sing N N 141 
GLU OE2   HE2    sing N N 142 
GLU OXT   HXT    sing N N 143 
GLY N     CA     sing N N 144 
GLY N     H      sing N N 145 
GLY N     H2     sing N N 146 
GLY CA    C      sing N N 147 
GLY CA    HA2    sing N N 148 
GLY CA    HA3    sing N N 149 
GLY C     O      doub N N 150 
GLY C     OXT    sing N N 151 
GLY OXT   HXT    sing N N 152 
HIS N     CA     sing N N 153 
HIS N     H      sing N N 154 
HIS N     H2     sing N N 155 
HIS CA    C      sing N N 156 
HIS CA    CB     sing N N 157 
HIS CA    HA     sing N N 158 
HIS C     O      doub N N 159 
HIS C     OXT    sing N N 160 
HIS CB    CG     sing N N 161 
HIS CB    HB2    sing N N 162 
HIS CB    HB3    sing N N 163 
HIS CG    ND1    sing Y N 164 
HIS CG    CD2    doub Y N 165 
HIS ND1   CE1    doub Y N 166 
HIS ND1   HD1    sing N N 167 
HIS CD2   NE2    sing Y N 168 
HIS CD2   HD2    sing N N 169 
HIS CE1   NE2    sing Y N 170 
HIS CE1   HE1    sing N N 171 
HIS NE2   HE2    sing N N 172 
HIS OXT   HXT    sing N N 173 
HOH O     H1     sing N N 174 
HOH O     H2     sing N N 175 
ILE N     CA     sing N N 176 
ILE N     H      sing N N 177 
ILE N     H2     sing N N 178 
ILE CA    C      sing N N 179 
ILE CA    CB     sing N N 180 
ILE CA    HA     sing N N 181 
ILE C     O      doub N N 182 
ILE C     OXT    sing N N 183 
ILE CB    CG1    sing N N 184 
ILE CB    CG2    sing N N 185 
ILE CB    HB     sing N N 186 
ILE CG1   CD1    sing N N 187 
ILE CG1   HG12   sing N N 188 
ILE CG1   HG13   sing N N 189 
ILE CG2   HG21   sing N N 190 
ILE CG2   HG22   sing N N 191 
ILE CG2   HG23   sing N N 192 
ILE CD1   HD11   sing N N 193 
ILE CD1   HD12   sing N N 194 
ILE CD1   HD13   sing N N 195 
ILE OXT   HXT    sing N N 196 
LEU N     CA     sing N N 197 
LEU N     H      sing N N 198 
LEU N     H2     sing N N 199 
LEU CA    C      sing N N 200 
LEU CA    CB     sing N N 201 
LEU CA    HA     sing N N 202 
LEU C     O      doub N N 203 
LEU C     OXT    sing N N 204 
LEU CB    CG     sing N N 205 
LEU CB    HB2    sing N N 206 
LEU CB    HB3    sing N N 207 
LEU CG    CD1    sing N N 208 
LEU CG    CD2    sing N N 209 
LEU CG    HG     sing N N 210 
LEU CD1   HD11   sing N N 211 
LEU CD1   HD12   sing N N 212 
LEU CD1   HD13   sing N N 213 
LEU CD2   HD21   sing N N 214 
LEU CD2   HD22   sing N N 215 
LEU CD2   HD23   sing N N 216 
LEU OXT   HXT    sing N N 217 
LYS N     CA     sing N N 218 
LYS N     H      sing N N 219 
LYS N     H2     sing N N 220 
LYS CA    C      sing N N 221 
LYS CA    CB     sing N N 222 
LYS CA    HA     sing N N 223 
LYS C     O      doub N N 224 
LYS C     OXT    sing N N 225 
LYS CB    CG     sing N N 226 
LYS CB    HB2    sing N N 227 
LYS CB    HB3    sing N N 228 
LYS CG    CD     sing N N 229 
LYS CG    HG2    sing N N 230 
LYS CG    HG3    sing N N 231 
LYS CD    CE     sing N N 232 
LYS CD    HD2    sing N N 233 
LYS CD    HD3    sing N N 234 
LYS CE    NZ     sing N N 235 
LYS CE    HE2    sing N N 236 
LYS CE    HE3    sing N N 237 
LYS NZ    HZ1    sing N N 238 
LYS NZ    HZ2    sing N N 239 
LYS NZ    HZ3    sing N N 240 
LYS OXT   HXT    sing N N 241 
MET N     CA     sing N N 242 
MET N     H      sing N N 243 
MET N     H2     sing N N 244 
MET CA    C      sing N N 245 
MET CA    CB     sing N N 246 
MET CA    HA     sing N N 247 
MET C     O      doub N N 248 
MET C     OXT    sing N N 249 
MET CB    CG     sing N N 250 
MET CB    HB2    sing N N 251 
MET CB    HB3    sing N N 252 
MET CG    SD     sing N N 253 
MET CG    HG2    sing N N 254 
MET CG    HG3    sing N N 255 
MET SD    CE     sing N N 256 
MET CE    HE1    sing N N 257 
MET CE    HE2    sing N N 258 
MET CE    HE3    sing N N 259 
MET OXT   HXT    sing N N 260 
MLA C1    O1A    sing N N 261 
MLA C1    O1B    doub N N 262 
MLA C1    C2     sing N N 263 
MLA O1A   H1A    sing N N 264 
MLA C2    C3     sing N N 265 
MLA C2    HC21   sing N N 266 
MLA C2    HC22   sing N N 267 
MLA C3    O3A    doub N N 268 
MLA C3    O3B    sing N N 269 
MLA O3B   H3B    sing N N 270 
NHE "C3'" "C2'"  sing N N 271 
NHE "C3'" "C4'"  sing N N 272 
NHE "C3'" "H3'1" sing N N 273 
NHE "C3'" "H3'2" sing N N 274 
NHE "C2'" "C1'"  sing N N 275 
NHE "C2'" "H2'1" sing N N 276 
NHE "C2'" "H2'2" sing N N 277 
NHE "C1'" "C6'"  sing N N 278 
NHE "C1'" N      sing N N 279 
NHE "C1'" "HC'1" sing N N 280 
NHE "C6'" "C5'"  sing N N 281 
NHE "C6'" "H6'1" sing N N 282 
NHE "C6'" "H6'2" sing N N 283 
NHE N     C1     sing N N 284 
NHE N     HN     sing N N 285 
NHE C1    C2     sing N N 286 
NHE C1    HC11   sing N N 287 
NHE C1    HC12   sing N N 288 
NHE C2    S      sing N N 289 
NHE C2    HC21   sing N N 290 
NHE C2    HC22   sing N N 291 
NHE S     O1     doub N N 292 
NHE S     O2     doub N N 293 
NHE S     O3     sing N N 294 
NHE O3    HO3    sing N N 295 
NHE "C5'" "C4'"  sing N N 296 
NHE "C5'" "H5'1" sing N N 297 
NHE "C5'" "H5'2" sing N N 298 
NHE "C4'" "H4'1" sing N N 299 
NHE "C4'" "H4'2" sing N N 300 
PHE N     CA     sing N N 301 
PHE N     H      sing N N 302 
PHE N     H2     sing N N 303 
PHE CA    C      sing N N 304 
PHE CA    CB     sing N N 305 
PHE CA    HA     sing N N 306 
PHE C     O      doub N N 307 
PHE C     OXT    sing N N 308 
PHE CB    CG     sing N N 309 
PHE CB    HB2    sing N N 310 
PHE CB    HB3    sing N N 311 
PHE CG    CD1    doub Y N 312 
PHE CG    CD2    sing Y N 313 
PHE CD1   CE1    sing Y N 314 
PHE CD1   HD1    sing N N 315 
PHE CD2   CE2    doub Y N 316 
PHE CD2   HD2    sing N N 317 
PHE CE1   CZ     doub Y N 318 
PHE CE1   HE1    sing N N 319 
PHE CE2   CZ     sing Y N 320 
PHE CE2   HE2    sing N N 321 
PHE CZ    HZ     sing N N 322 
PHE OXT   HXT    sing N N 323 
PRO N     CA     sing N N 324 
PRO N     CD     sing N N 325 
PRO N     H      sing N N 326 
PRO CA    C      sing N N 327 
PRO CA    CB     sing N N 328 
PRO CA    HA     sing N N 329 
PRO C     O      doub N N 330 
PRO C     OXT    sing N N 331 
PRO CB    CG     sing N N 332 
PRO CB    HB2    sing N N 333 
PRO CB    HB3    sing N N 334 
PRO CG    CD     sing N N 335 
PRO CG    HG2    sing N N 336 
PRO CG    HG3    sing N N 337 
PRO CD    HD2    sing N N 338 
PRO CD    HD3    sing N N 339 
PRO OXT   HXT    sing N N 340 
SER N     CA     sing N N 341 
SER N     H      sing N N 342 
SER N     H2     sing N N 343 
SER CA    C      sing N N 344 
SER CA    CB     sing N N 345 
SER CA    HA     sing N N 346 
SER C     O      doub N N 347 
SER C     OXT    sing N N 348 
SER CB    OG     sing N N 349 
SER CB    HB2    sing N N 350 
SER CB    HB3    sing N N 351 
SER OG    HG     sing N N 352 
SER OXT   HXT    sing N N 353 
THR N     CA     sing N N 354 
THR N     H      sing N N 355 
THR N     H2     sing N N 356 
THR CA    C      sing N N 357 
THR CA    CB     sing N N 358 
THR CA    HA     sing N N 359 
THR C     O      doub N N 360 
THR C     OXT    sing N N 361 
THR CB    OG1    sing N N 362 
THR CB    CG2    sing N N 363 
THR CB    HB     sing N N 364 
THR OG1   HG1    sing N N 365 
THR CG2   HG21   sing N N 366 
THR CG2   HG22   sing N N 367 
THR CG2   HG23   sing N N 368 
THR OXT   HXT    sing N N 369 
TRP N     CA     sing N N 370 
TRP N     H      sing N N 371 
TRP N     H2     sing N N 372 
TRP CA    C      sing N N 373 
TRP CA    CB     sing N N 374 
TRP CA    HA     sing N N 375 
TRP C     O      doub N N 376 
TRP C     OXT    sing N N 377 
TRP CB    CG     sing N N 378 
TRP CB    HB2    sing N N 379 
TRP CB    HB3    sing N N 380 
TRP CG    CD1    doub Y N 381 
TRP CG    CD2    sing Y N 382 
TRP CD1   NE1    sing Y N 383 
TRP CD1   HD1    sing N N 384 
TRP CD2   CE2    doub Y N 385 
TRP CD2   CE3    sing Y N 386 
TRP NE1   CE2    sing Y N 387 
TRP NE1   HE1    sing N N 388 
TRP CE2   CZ2    sing Y N 389 
TRP CE3   CZ3    doub Y N 390 
TRP CE3   HE3    sing N N 391 
TRP CZ2   CH2    doub Y N 392 
TRP CZ2   HZ2    sing N N 393 
TRP CZ3   CH2    sing Y N 394 
TRP CZ3   HZ3    sing N N 395 
TRP CH2   HH2    sing N N 396 
TRP OXT   HXT    sing N N 397 
TYR N     CA     sing N N 398 
TYR N     H      sing N N 399 
TYR N     H2     sing N N 400 
TYR CA    C      sing N N 401 
TYR CA    CB     sing N N 402 
TYR CA    HA     sing N N 403 
TYR C     O      doub N N 404 
TYR C     OXT    sing N N 405 
TYR CB    CG     sing N N 406 
TYR CB    HB2    sing N N 407 
TYR CB    HB3    sing N N 408 
TYR CG    CD1    doub Y N 409 
TYR CG    CD2    sing Y N 410 
TYR CD1   CE1    sing Y N 411 
TYR CD1   HD1    sing N N 412 
TYR CD2   CE2    doub Y N 413 
TYR CD2   HD2    sing N N 414 
TYR CE1   CZ     doub Y N 415 
TYR CE1   HE1    sing N N 416 
TYR CE2   CZ     sing Y N 417 
TYR CE2   HE2    sing N N 418 
TYR CZ    OH     sing N N 419 
TYR OH    HH     sing N N 420 
TYR OXT   HXT    sing N N 421 
VAL N     CA     sing N N 422 
VAL N     H      sing N N 423 
VAL N     H2     sing N N 424 
VAL CA    C      sing N N 425 
VAL CA    CB     sing N N 426 
VAL CA    HA     sing N N 427 
VAL C     O      doub N N 428 
VAL C     OXT    sing N N 429 
VAL CB    CG1    sing N N 430 
VAL CB    CG2    sing N N 431 
VAL CB    HB     sing N N 432 
VAL CG1   HG11   sing N N 433 
VAL CG1   HG12   sing N N 434 
VAL CG1   HG13   sing N N 435 
VAL CG2   HG21   sing N N 436 
VAL CG2   HG22   sing N N 437 
VAL CG2   HG23   sing N N 438 
VAL OXT   HXT    sing N N 439 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 BGC 1 n 
2 BGC 2 n 
# 
_atom_sites.entry_id                    8WN6 
_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]   0.014806 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014497 
_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]   0.010375 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
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     . GLY A 1 23  ? -10.179 -3.050  -12.525 1.00 21.81 ? 3   GLY A N     1 
ATOM   2    C  CA    . GLY A 1 23  ? -10.827 -4.156  -11.789 1.00 23.16 ? 3   GLY A CA    1 
ATOM   3    C  C     . GLY A 1 23  ? -10.218 -4.348  -10.397 1.00 28.50 ? 3   GLY A C     1 
ATOM   4    O  O     . GLY A 1 23  ? -10.551 -5.270  -9.668  1.00 29.37 ? 3   GLY A O     1 
ATOM   5    N  N     . GLU A 1 24  ? -9.410  -3.352  -10.044 1.00 23.75 ? 4   GLU A N     1 
ATOM   6    C  CA    . GLU A 1 24  ? -8.407  -3.272  -9.002  1.00 25.35 ? 4   GLU A CA    1 
ATOM   7    C  C     . GLU A 1 24  ? -8.935  -2.331  -7.910  1.00 22.48 ? 4   GLU A C     1 
ATOM   8    O  O     . GLU A 1 24  ? -8.470  -2.295  -6.765  1.00 21.88 ? 4   GLU A O     1 
ATOM   9    C  CB    . GLU A 1 24  ? -7.223  -2.632  -9.750  1.00 30.85 ? 4   GLU A CB    1 
ATOM   10   C  CG    . GLU A 1 24  ? -7.674  -1.588  -10.849 1.00 29.47 ? 4   GLU A CG    1 
ATOM   11   C  CD    . GLU A 1 24  ? -6.767  -1.369  -12.047 1.00 29.42 ? 4   GLU A CD    1 
ATOM   12   O  OE1   . GLU A 1 24  ? -7.161  -1.806  -13.180 1.00 27.27 ? 4   GLU A OE1   1 
ATOM   13   O  OE2   . GLU A 1 24  ? -5.622  -0.773  -11.858 1.00 33.41 ? 4   GLU A OE2   1 
ATOM   14   N  N     . ARG A 1 25  ? -9.859  -1.443  -8.310  1.00 16.88 ? 5   ARG A N     1 
ATOM   15   C  CA    . ARG A 1 25  ? -10.109 -0.253  -7.548  1.00 14.57 ? 5   ARG A CA    1 
ATOM   16   C  C     . ARG A 1 25  ? -11.299 -0.459  -6.631  1.00 14.27 ? 5   ARG A C     1 
ATOM   17   O  O     . ARG A 1 25  ? -12.351 -1.019  -6.965  1.00 14.39 ? 5   ARG A O     1 
ATOM   18   C  CB    . ARG A 1 25  ? -10.317 0.954   -8.480  1.00 15.27 ? 5   ARG A CB    1 
ATOM   19   C  CG    . ARG A 1 25  ? -9.016  1.454   -9.066  1.00 16.12 ? 5   ARG A CG    1 
ATOM   20   C  CD    . ARG A 1 25  ? -9.285  2.761   -9.788  1.00 16.68 ? 5   ARG A CD    1 
ATOM   21   N  NE    . ARG A 1 25  ? -8.113  3.051   -10.576 1.00 18.34 ? 5   ARG A NE    1 
ATOM   22   C  CZ    . ARG A 1 25  ? -7.000  3.654   -10.146 1.00 21.58 ? 5   ARG A CZ    1 
ATOM   23   N  NH1   . ARG A 1 25  ? -6.921  4.123   -8.908  1.00 24.22 ? 5   ARG A NH1   1 
ATOM   24   N  NH2   . ARG A 1 25  ? -5.999  3.829   -10.990 1.00 21.84 ? 5   ARG A NH2   1 
ATOM   25   N  N     . PHE A 1 26  ? -11.065 0.011   -5.414  1.00 14.86 ? 6   PHE A N     1 
ATOM   26   C  CA    . PHE A 1 26  ? -12.039 0.077   -4.379  1.00 14.97 ? 6   PHE A CA    1 
ATOM   27   C  C     . PHE A 1 26  ? -12.612 1.493   -4.353  1.00 13.76 ? 6   PHE A C     1 
ATOM   28   O  O     . PHE A 1 26  ? -12.009 2.403   -4.916  1.00 15.33 ? 6   PHE A O     1 
ATOM   29   C  CB    . PHE A 1 26  ? -11.413 -0.384  -3.050  1.00 14.46 ? 6   PHE A CB    1 
ATOM   30   C  CG    . PHE A 1 26  ? -11.114 -1.868  -2.976  1.00 12.96 ? 6   PHE A CG    1 
ATOM   31   C  CD1   . PHE A 1 26  ? -9.983  -2.398  -3.586  1.00 14.48 ? 6   PHE A CD1   1 
ATOM   32   C  CD2   . PHE A 1 26  ? -11.955 -2.722  -2.278  1.00 15.47 ? 6   PHE A CD2   1 
ATOM   33   C  CE1   . PHE A 1 26  ? -9.699  -3.756  -3.541  1.00 14.65 ? 6   PHE A CE1   1 
ATOM   34   C  CE2   . PHE A 1 26  ? -11.665 -4.080  -2.223  1.00 12.62 ? 6   PHE A CE2   1 
ATOM   35   C  CZ    . PHE A 1 26  ? -10.582 -4.597  -2.884  1.00 13.19 ? 6   PHE A CZ    1 
ATOM   36   N  N     . PRO A 1 27  ? -13.779 1.700   -3.743  1.00 14.36 ? 7   PRO A N     1 
ATOM   37   C  CA    . PRO A 1 27  ? -14.370 3.023   -3.605  1.00 15.30 ? 7   PRO A CA    1 
ATOM   38   C  C     . PRO A 1 27  ? -13.408 3.957   -2.879  1.00 16.19 ? 7   PRO A C     1 
ATOM   39   O  O     . PRO A 1 27  ? -12.603 3.530   -2.034  1.00 14.57 ? 7   PRO A O     1 
ATOM   40   C  CB    . PRO A 1 27  ? -15.675 2.823   -2.839  1.00 16.41 ? 7   PRO A CB    1 
ATOM   41   C  CG    . PRO A 1 27  ? -15.955 1.348   -2.975  1.00 16.10 ? 7   PRO A CG    1 
ATOM   42   C  CD    . PRO A 1 27  ? -14.614 0.669   -3.115  1.00 15.51 ? 7   PRO A CD    1 
ATOM   43   N  N     . ALA A 1 28  ? -13.416 5.239   -3.279  1.00 16.91 ? 8   ALA A N     1 
ATOM   44   C  CA    . ALA A 1 28  ? -12.503 6.194   -2.685  1.00 17.67 ? 8   ALA A CA    1 
ATOM   45   C  C     . ALA A 1 28  ? -12.751 6.379   -1.185  1.00 16.82 ? 8   ALA A C     1 
ATOM   46   O  O     . ALA A 1 28  ? -11.836 6.764   -0.488  1.00 20.35 ? 8   ALA A O     1 
ATOM   47   C  CB    . ALA A 1 28  ? -12.606 7.520   -3.436  1.00 19.22 ? 8   ALA A CB    1 
ATOM   48   N  N     . ASP A 1 29  ? -13.959 6.097   -0.697  1.00 15.37 ? 9   ASP A N     1 
ATOM   49   C  CA    . ASP A 1 29  ? -14.329 6.223   0.702   1.00 16.00 ? 9   ASP A CA    1 
ATOM   50   C  C     . ASP A 1 29  ? -14.230 4.882   1.457   1.00 12.84 ? 9   ASP A C     1 
ATOM   51   O  O     . ASP A 1 29  ? -14.685 4.777   2.596   1.00 14.21 ? 9   ASP A O     1 
ATOM   52   C  CB    . ASP A 1 29  ? -15.706 6.866   0.831   1.00 17.21 ? 9   ASP A CB    1 
ATOM   53   C  CG    . ASP A 1 29  ? -16.866 6.050   0.290   1.00 19.81 ? 9   ASP A CG    1 
ATOM   54   O  OD1   . ASP A 1 29  ? -16.615 5.076   -0.416  1.00 23.30 ? 9   ASP A OD1   1 
ATOM   55   O  OD2   . ASP A 1 29  ? -18.022 6.343   0.682   1.00 27.73 ? 9   ASP A OD2   1 
ATOM   56   N  N     . PHE A 1 30  ? -13.598 3.901   0.837   1.00 11.87 ? 10  PHE A N     1 
ATOM   57   C  CA    . PHE A 1 30  ? -13.484 2.565   1.431   1.00 10.98 ? 10  PHE A CA    1 
ATOM   58   C  C     . PHE A 1 30  ? -12.640 2.687   2.706   1.00 11.24 ? 10  PHE A C     1 
ATOM   59   O  O     . PHE A 1 30  ? -11.641 3.415   2.723   1.00 12.99 ? 10  PHE A O     1 
ATOM   60   C  CB    . PHE A 1 30  ? -12.850 1.606   0.422   1.00 11.01 ? 10  PHE A CB    1 
ATOM   61   C  CG    . PHE A 1 30  ? -13.045 0.144   0.690   1.00 10.48 ? 10  PHE A CG    1 
ATOM   62   C  CD1   . PHE A 1 30  ? -14.292 -0.437  0.473   1.00 9.08  ? 10  PHE A CD1   1 
ATOM   63   C  CD2   . PHE A 1 30  ? -12.011 -0.647  1.149   1.00 9.83  ? 10  PHE A CD2   1 
ATOM   64   C  CE1   . PHE A 1 30  ? -14.475 -1.784  0.705   1.00 9.33  ? 10  PHE A CE1   1 
ATOM   65   C  CE2   . PHE A 1 30  ? -12.188 -2.010  1.318   1.00 9.95  ? 10  PHE A CE2   1 
ATOM   66   C  CZ    . PHE A 1 30  ? -13.419 -2.566  1.096   1.00 9.61  ? 10  PHE A CZ    1 
ATOM   67   N  N     . VAL A 1 31  ? -13.037 1.937   3.732   1.00 9.86  ? 11  VAL A N     1 
ATOM   68   C  CA    . VAL A 1 31  ? -12.278 1.869   4.975   1.00 10.03 ? 11  VAL A CA    1 
ATOM   69   C  C     . VAL A 1 31  ? -11.167 0.844   4.822   1.00 9.28  ? 11  VAL A C     1 
ATOM   70   O  O     . VAL A 1 31  ? -11.405 -0.317  4.446   1.00 9.98  ? 11  VAL A O     1 
ATOM   71   C  CB    . VAL A 1 31  ? -13.256 1.596   6.130   1.00 10.78 ? 11  VAL A CB    1 
ATOM   72   C  CG1   . VAL A 1 31  ? -12.525 1.289   7.412   1.00 11.36 ? 11  VAL A CG1   1 
ATOM   73   C  CG2   . VAL A 1 31  ? -14.218 2.747   6.359   1.00 11.28 ? 11  VAL A CG2   1 
ATOM   74   N  N     . TRP A 1 32  ? -9.927  1.271   5.104   1.00 8.26  ? 12  TRP A N     1 
ATOM   75   C  CA    . TRP A 1 32  ? -8.760  0.427   5.043   1.00 8.20  ? 12  TRP A CA    1 
ATOM   76   C  C     . TRP A 1 32  ? -8.103  0.466   6.407   1.00 7.94  ? 12  TRP A C     1 
ATOM   77   O  O     . TRP A 1 32  ? -7.619  1.509   6.826   1.00 8.26  ? 12  TRP A O     1 
ATOM   78   C  CB    . TRP A 1 32  ? -7.726  0.897   4.016   1.00 9.29  ? 12  TRP A CB    1 
ATOM   79   C  CG    . TRP A 1 32  ? -8.167  0.730   2.592   1.00 9.54  ? 12  TRP A CG    1 
ATOM   80   C  CD1   . TRP A 1 32  ? -8.579  1.709   1.728   1.00 10.57 ? 12  TRP A CD1   1 
ATOM   81   C  CD2   . TRP A 1 32  ? -8.194  -0.504  1.882   1.00 10.15 ? 12  TRP A CD2   1 
ATOM   82   N  NE1   . TRP A 1 32  ? -8.843  1.152   0.509   1.00 11.79 ? 12  TRP A NE1   1 
ATOM   83   C  CE2   . TRP A 1 32  ? -8.583  -0.190  0.553   1.00 11.02 ? 12  TRP A CE2   1 
ATOM   84   C  CE3   . TRP A 1 32  ? -7.930  -1.834  2.245   1.00 10.25 ? 12  TRP A CE3   1 
ATOM   85   C  CZ2   . TRP A 1 32  ? -8.736  -1.188  -0.404  1.00 11.04 ? 12  TRP A CZ2   1 
ATOM   86   C  CZ3   . TRP A 1 32  ? -8.057  -2.809  1.270   1.00 11.88 ? 12  TRP A CZ3   1 
ATOM   87   C  CH2   . TRP A 1 32  ? -8.491  -2.482  -0.012  1.00 10.85 ? 12  TRP A CH2   1 
ATOM   88   N  N     . GLY A 1 33  ? -8.012  -0.700  7.044   1.00 7.25  ? 13  GLY A N     1 
ATOM   89   C  CA    . GLY A 1 33  ? -7.536  -0.713  8.417   1.00 6.88  ? 13  GLY A CA    1 
ATOM   90   C  C     . GLY A 1 33  ? -6.801  -2.003  8.753   1.00 6.32  ? 13  GLY A C     1 
ATOM   91   O  O     . GLY A 1 33  ? -6.618  -2.924  7.951   1.00 7.41  ? 13  GLY A O     1 
ATOM   92   N  N     . ALA A 1 34  ? -6.294  -2.043  9.988   1.00 6.12  ? 14  ALA A N     1 
ATOM   93   C  CA    . ALA A 1 34  ? -5.881  -3.273  10.614  1.00 5.44  ? 14  ALA A CA    1 
ATOM   94   C  C     . ALA A 1 34  ? -6.550  -3.352  11.984  1.00 5.02  ? 14  ALA A C     1 
ATOM   95   O  O     . ALA A 1 34  ? -7.095  -2.343  12.445  1.00 4.66  ? 14  ALA A O     1 
ATOM   96   C  CB    . ALA A 1 34  ? -4.381  -3.377  10.693  1.00 5.92  ? 14  ALA A CB    1 
ATOM   97   N  N     . ALA A 1 35  ? -6.646  -4.576  12.504  1.00 5.00  ? 15  ALA A N     1 
ATOM   98   C  CA    . ALA A 1 35  ? -7.428  -4.866  13.693  1.00 4.68  ? 15  ALA A CA    1 
ATOM   99   C  C     . ALA A 1 35  ? -6.580  -5.523  14.753  1.00 4.70  ? 15  ALA A C     1 
ATOM   100  O  O     . ALA A 1 35  ? -5.615  -6.239  14.448  1.00 5.73  ? 15  ALA A O     1 
ATOM   101  C  CB    . ALA A 1 35  ? -8.555  -5.753  13.349  1.00 4.51  ? 15  ALA A CB    1 
ATOM   102  N  N     . THR A 1 36  ? -6.952  -5.244  16.004  1.00 4.52  ? 16  THR A N     1 
ATOM   103  C  CA    . THR A 1 36  ? -6.437  -5.864  17.209  1.00 4.44  ? 16  THR A CA    1 
ATOM   104  C  C     . THR A 1 36  ? -7.569  -6.034  18.224  1.00 4.28  ? 16  THR A C     1 
ATOM   105  O  O     . THR A 1 36  ? -8.692  -5.581  18.022  1.00 3.77  ? 16  THR A O     1 
ATOM   106  C  CB    . THR A 1 36  ? -5.350  -4.984  17.849  1.00 4.45  ? 16  THR A CB    1 
ATOM   107  O  OG1   . THR A 1 36  ? -5.957  -3.743  18.225  1.00 4.83  ? 16  THR A OG1   1 
ATOM   108  C  CG2   . THR A 1 36  ? -4.156  -4.716  16.964  1.00 4.96  ? 16  THR A CG2   1 
ATOM   109  N  N     . ALA A 1 37  ? -7.255  -6.713  19.339  1.00 4.00  ? 17  ALA A N     1 
ATOM   110  C  CA    . ALA A 1 37  ? -8.121  -6.887  20.512  1.00 4.13  ? 17  ALA A CA    1 
ATOM   111  C  C     . ALA A 1 37  ? -7.299  -6.546  21.752  1.00 3.99  ? 17  ALA A C     1 
ATOM   112  O  O     . ALA A 1 37  ? -6.084  -6.818  21.817  1.00 4.28  ? 17  ALA A O     1 
ATOM   113  C  CB    . ALA A 1 37  ? -8.610  -8.262  20.609  1.00 4.25  ? 17  ALA A CB    1 
ATOM   114  N  N     . ALA A 1 38  ? -7.942  -5.973  22.760  1.00 3.87  ? 18  ALA A N     1 
ATOM   115  C  CA    . ALA A 1 38  ? -7.240  -5.415  23.905  1.00 4.05  ? 18  ALA A CA    1 
ATOM   116  C  C     . ALA A 1 38  ? -6.364  -6.430  24.630  1.00 3.99  ? 18  ALA A C     1 
ATOM   117  O  O     . ALA A 1 38  ? -5.168  -6.144  24.899  1.00 4.26  ? 18  ALA A O     1 
ATOM   118  C  CB    . ALA A 1 38  ? -8.228  -4.773  24.881  1.00 4.09  ? 18  ALA A CB    1 
ATOM   119  N  N     . TYR A 1 39  ? -6.903  -7.595  24.994  1.00 4.12  ? 19  TYR A N     1 
ATOM   120  C  CA    . TYR A 1 39  ? -6.115  -8.552  25.776  1.00 4.08  ? 19  TYR A CA    1 
ATOM   121  C  C     . TYR A 1 39  ? -4.918  -9.050  24.967  1.00 4.16  ? 19  TYR A C     1 
ATOM   122  O  O     . TYR A 1 39  ? -3.878  -9.398  25.532  1.00 4.21  ? 19  TYR A O     1 
ATOM   123  C  CB    . TYR A 1 39  ? -6.972  -9.662  26.379  1.00 4.35  ? 19  TYR A CB    1 
ATOM   124  C  CG    . TYR A 1 39  ? -6.189  -10.528 27.341  1.00 4.24  ? 19  TYR A CG    1 
ATOM   125  C  CD1   . TYR A 1 39  ? -5.979  -10.049 28.628  1.00 4.72  ? 19  TYR A CD1   1 
ATOM   126  C  CD2   . TYR A 1 39  ? -5.570  -11.693 26.951  1.00 4.35  ? 19  TYR A CD2   1 
ATOM   127  C  CE1   . TYR A 1 39  ? -5.178  -10.743 29.520  1.00 5.18  ? 19  TYR A CE1   1 
ATOM   128  C  CE2   . TYR A 1 39  ? -4.798  -12.445 27.854  1.00 4.80  ? 19  TYR A CE2   1 
ATOM   129  C  CZ    . TYR A 1 39  ? -4.579  -11.931 29.124  1.00 5.10  ? 19  TYR A CZ    1 
ATOM   130  O  OH    . TYR A 1 39  ? -3.753  -12.648 30.013  1.00 5.66  ? 19  TYR A OH    1 
ATOM   131  N  N     . GLN A 1 40  ? -5.070  -9.070  23.646  1.00 4.31  ? 20  GLN A N     1 
ATOM   132  C  CA    . GLN A 1 40  ? -4.043  -9.633  22.792  1.00 4.53  ? 20  GLN A CA    1 
ATOM   133  C  C     . GLN A 1 40  ? -2.824  -8.727  22.749  1.00 4.64  ? 20  GLN A C     1 
ATOM   134  O  O     . GLN A 1 40  ? -1.741  -9.265  22.449  1.00 4.63  ? 20  GLN A O     1 
ATOM   135  C  CB    . GLN A 1 40  ? -4.566  -9.896  21.394  1.00 4.91  ? 20  GLN A CB    1 
ATOM   136  C  CG    . GLN A 1 40  ? -5.707  -10.891 21.420  1.00 5.05  ? 20  GLN A CG    1 
ATOM   137  C  CD    . GLN A 1 40  ? -6.077  -11.391 20.039  1.00 6.52  ? 20  GLN A CD    1 
ATOM   138  O  OE1   . GLN A 1 40  ? -6.944  -10.830 19.344  1.00 7.72  ? 20  GLN A OE1   1 
ATOM   139  N  NE2   . GLN A 1 40  ? -5.385  -12.423 19.622  1.00 7.38  ? 20  GLN A NE2   1 
ATOM   140  N  N     . ILE A 1 41  ? -2.988  -7.415  22.975  1.00 4.23  ? 21  ILE A N     1 
ATOM   141  C  CA    . ILE A 1 41  ? -1.900  -6.477  22.714  1.00 4.38  ? 21  ILE A CA    1 
ATOM   142  C  C     . ILE A 1 41  ? -1.524  -5.623  23.925  1.00 4.21  ? 21  ILE A C     1 
ATOM   143  O  O     . ILE A 1 41  ? -0.420  -5.083  23.937  1.00 4.32  ? 21  ILE A O     1 
ATOM   144  C  CB    . ILE A 1 41  ? -2.193  -5.565  21.510  1.00 4.59  ? 21  ILE A CB    1 
ATOM   145  C  CG1   . ILE A 1 41  ? -3.368  -4.587  21.721  1.00 5.66  ? 21  ILE A CG1   1 
ATOM   146  C  CG2   . ILE A 1 41  ? -2.367  -6.390  20.262  1.00 4.50  ? 21  ILE A CG2   1 
ATOM   147  C  CD1   . ILE A 1 41  ? -3.393  -3.457  20.676  1.00 5.73  ? 21  ILE A CD1   1 
ATOM   148  N  N     . GLU A 1 42  ? -2.457  -5.304  24.830  1.00 3.86  ? 22  GLU A N     1 
ATOM   149  C  CA    . GLU A 1 42  ? -2.274  -4.152  25.708  1.00 4.32  ? 22  GLU A CA    1 
ATOM   150  C  C     . GLU A 1 42  ? -1.229  -4.361  26.820  1.00 4.33  ? 22  GLU A C     1 
ATOM   151  O  O     . GLU A 1 42  ? -0.507  -3.429  27.145  1.00 5.36  ? 22  GLU A O     1 
ATOM   152  C  CB    . GLU A 1 42  ? -3.581  -3.765  26.381  1.00 4.51  ? 22  GLU A CB    1 
ATOM   153  C  CG    . GLU A 1 42  ? -4.464  -2.932  25.493  1.00 4.66  ? 22  GLU A CG    1 
ATOM   154  C  CD    . GLU A 1 42  ? -5.706  -2.376  26.160  1.00 5.85  ? 22  GLU A CD    1 
ATOM   155  O  OE1   . GLU A 1 42  ? -5.887  -2.699  27.363  1.00 7.60  ? 22  GLU A OE1   1 
ATOM   156  O  OE2   . GLU A 1 42  ? -6.475  -1.643  25.458  1.00 5.31  ? 22  GLU A OE2   1 
ATOM   157  N  N     . GLY A 1 43  ? -1.197  -5.529  27.428  1.00 4.91  ? 23  GLY A N     1 
ATOM   158  C  CA    . GLY A 1 43  ? -0.476  -5.705  28.679  1.00 4.91  ? 23  GLY A CA    1 
ATOM   159  C  C     . GLY A 1 43  ? -0.992  -4.778  29.784  1.00 5.11  ? 23  GLY A C     1 
ATOM   160  O  O     . GLY A 1 43  ? -2.186  -4.469  29.851  1.00 5.59  ? 23  GLY A O     1 
ATOM   161  N  N     . ALA A 1 44  ? -0.078  -4.328  30.663  1.00 5.49  ? 24  ALA A N     1 
ATOM   162  C  CA    . ALA A 1 44  ? -0.472  -3.429  31.762  1.00 5.68  ? 24  ALA A CA    1 
ATOM   163  C  C     . ALA A 1 44  ? -1.739  -3.940  32.471  1.00 6.31  ? 24  ALA A C     1 
ATOM   164  O  O     . ALA A 1 44  ? -2.694  -3.211  32.687  1.00 6.31  ? 24  ALA A O     1 
ATOM   165  C  CB    . ALA A 1 44  ? -0.618  -2.016  31.236  1.00 6.05  ? 24  ALA A CB    1 
ATOM   166  N  N     . VAL A 1 45  ? -1.733  -5.212  32.864  1.00 6.60  ? 25  VAL A N     1 
ATOM   167  C  CA    . VAL A 1 45  ? -2.966  -5.913  33.201  1.00 7.20  ? 25  VAL A CA    1 
ATOM   168  C  C     . VAL A 1 45  ? -3.499  -5.489  34.553  1.00 7.81  ? 25  VAL A C     1 
ATOM   169  O  O     . VAL A 1 45  ? -4.683  -5.652  34.771  1.00 8.26  ? 25  VAL A O     1 
ATOM   170  C  CB    . VAL A 1 45  ? -2.865  -7.433  33.115  1.00 7.56  ? 25  VAL A CB    1 
ATOM   171  C  CG1   . VAL A 1 45  ? -2.767  -7.938  31.664  1.00 7.41  ? 25  VAL A CG1   1 
ATOM   172  C  CG2   . VAL A 1 45  ? -1.661  -7.958  33.895  1.00 8.24  ? 25  VAL A CG2   1 
ATOM   173  N  N     . ARG A 1 46  ? -2.636  -5.008  35.437  1.00 10.82 ? 26  ARG A N     1 
ATOM   174  C  CA    . ARG A 1 46  ? -3.095  -4.510  36.730  1.00 14.78 ? 26  ARG A CA    1 
ATOM   175  C  C     . ARG A 1 46  ? -2.953  -2.999  36.853  1.00 16.64 ? 26  ARG A C     1 
ATOM   176  O  O     . ARG A 1 46  ? -3.232  -2.441  37.934  1.00 16.00 ? 26  ARG A O     1 
ATOM   177  C  CB    . ARG A 1 46  ? -2.284  -5.186  37.843  1.00 19.88 ? 26  ARG A CB    1 
ATOM   178  C  CG    . ARG A 1 46  ? -2.521  -6.689  37.942  1.00 27.11 ? 26  ARG A CG    1 
ATOM   179  C  CD    . ARG A 1 46  ? -1.507  -7.315  38.898  1.00 36.14 ? 26  ARG A CD    1 
ATOM   180  N  NE    . ARG A 1 46  ? -0.129  -6.964  38.523  1.00 42.39 ? 26  ARG A NE    1 
ATOM   181  C  CZ    . ARG A 1 46  ? 0.575   -7.524  37.536  1.00 46.06 ? 26  ARG A CZ    1 
ATOM   182  N  NH1   . ARG A 1 46  ? 0.164   -8.643  36.957  1.00 49.65 ? 26  ARG A NH1   1 
ATOM   183  N  NH2   . ARG A 1 46  ? 1.742   -7.007  37.192  1.00 43.52 ? 26  ARG A NH2   1 
ATOM   184  N  N     . GLU A 1 47  ? -2.596  -2.310  35.767  1.00 11.35 ? 27  GLU A N     1 
ATOM   185  C  CA    . GLU A 1 47  ? -2.332  -0.890  35.843  1.00 11.24 ? 27  GLU A CA    1 
ATOM   186  C  C     . GLU A 1 47  ? -3.605  -0.033  35.752  1.00 10.77 ? 27  GLU A C     1 
ATOM   187  O  O     . GLU A 1 47  ? -4.607  -0.369  35.115  1.00 8.90  ? 27  GLU A O     1 
ATOM   188  C  CB    . GLU A 1 47  ? -1.330  -0.477  34.771  1.00 11.58 ? 27  GLU A CB    1 
ATOM   189  C  CG    . GLU A 1 47  ? 0.010   -1.181  34.950  1.00 13.88 ? 27  GLU A CG    1 
ATOM   190  C  CD    . GLU A 1 47  ? 1.113   -0.618  34.079  1.00 18.50 ? 27  GLU A CD    1 
ATOM   191  O  OE1   . GLU A 1 47  ? 0.989   0.539   33.720  1.00 18.94 ? 27  GLU A OE1   1 
ATOM   192  O  OE2   . GLU A 1 47  ? 2.020   -1.407  33.699  1.00 24.83 ? 27  GLU A OE2   1 
ATOM   193  N  N     . ASP A 1 48  ? -3.554  1.136   36.402  1.00 9.92  ? 28  ASP A N     1 
ATOM   194  C  CA    . ASP A 1 48  ? -4.552  2.178   36.240  1.00 9.89  ? 28  ASP A CA    1 
ATOM   195  C  C     . ASP A 1 48  ? -5.960  1.617   36.483  1.00 9.68  ? 28  ASP A C     1 
ATOM   196  O  O     . ASP A 1 48  ? -6.889  1.951   35.744  1.00 11.29 ? 28  ASP A O     1 
ATOM   197  C  CB    . ASP A 1 48  ? -4.421  2.881   34.885  1.00 11.74 ? 28  ASP A CB    1 
ATOM   198  C  CG    . ASP A 1 48  ? -3.155  3.700   34.753  1.00 16.86 ? 28  ASP A CG    1 
ATOM   199  O  OD1   . ASP A 1 48  ? -2.535  3.966   35.792  1.00 18.79 ? 28  ASP A OD1   1 
ATOM   200  O  OD2   . ASP A 1 48  ? -2.778  4.007   33.611  1.00 19.21 ? 28  ASP A OD2   1 
ATOM   201  N  N     . GLY A 1 49  ? -6.071  0.783   37.525  1.00 9.19  ? 29  GLY A N     1 
ATOM   202  C  CA    . GLY A 1 49  ? -7.368  0.348   38.031  1.00 8.91  ? 29  GLY A CA    1 
ATOM   203  C  C     . GLY A 1 49  ? -7.947  -0.866  37.308  1.00 8.48  ? 29  GLY A C     1 
ATOM   204  O  O     . GLY A 1 49  ? -9.037  -1.332  37.660  1.00 9.33  ? 29  GLY A O     1 
ATOM   205  N  N     . ARG A 1 50  ? -7.240  -1.424  36.317  1.00 6.92  ? 30  ARG A N     1 
ATOM   206  C  CA    . ARG A 1 50  ? -7.808  -2.537  35.556  1.00 6.07  ? 30  ARG A CA    1 
ATOM   207  C  C     . ARG A 1 50  ? -8.093  -3.706  36.493  1.00 6.38  ? 30  ARG A C     1 
ATOM   208  O  O     . ARG A 1 50  ? -7.274  -4.082  37.327  1.00 7.57  ? 30  ARG A O     1 
ATOM   209  C  CB    . ARG A 1 50  ? -6.912  -3.008  34.410  1.00 6.03  ? 30  ARG A CB    1 
ATOM   210  C  CG    . ARG A 1 50  ? -7.498  -4.118  33.562  1.00 5.61  ? 30  ARG A CG    1 
ATOM   211  C  CD    . ARG A 1 50  ? -6.630  -4.454  32.375  1.00 5.48  ? 30  ARG A CD    1 
ATOM   212  N  NE    . ARG A 1 50  ? -7.106  -5.579  31.615  1.00 5.80  ? 30  ARG A NE    1 
ATOM   213  C  CZ    . ARG A 1 50  ? -6.987  -6.850  31.936  1.00 6.48  ? 30  ARG A CZ    1 
ATOM   214  N  NH1   . ARG A 1 50  ? -6.335  -7.214  33.038  1.00 6.53  ? 30  ARG A NH1   1 
ATOM   215  N  NH2   . ARG A 1 50  ? -7.504  -7.775  31.131  1.00 7.68  ? 30  ARG A NH2   1 
ATOM   216  N  N     . GLY A 1 51  ? -9.259  -4.314  36.331  1.00 6.84  ? 31  GLY A N     1 
ATOM   217  C  CA    . GLY A 1 51  ? -9.617  -5.502  37.078  1.00 7.04  ? 31  GLY A CA    1 
ATOM   218  C  C     . GLY A 1 51  ? -9.128  -6.793  36.426  1.00 7.98  ? 31  GLY A C     1 
ATOM   219  O  O     . GLY A 1 51  ? -8.357  -6.720  35.473  1.00 10.11 ? 31  GLY A O     1 
ATOM   220  N  N     . VAL A 1 52  ? -9.449  -7.937  37.013  1.00 8.05  ? 32  VAL A N     1 
ATOM   221  C  CA    . VAL A 1 52  ? -9.081  -9.231  36.477  1.00 7.68  ? 32  VAL A CA    1 
ATOM   222  C  C     . VAL A 1 52  ? -10.132 -9.692  35.485  1.00 7.71  ? 32  VAL A C     1 
ATOM   223  O  O     . VAL A 1 52  ? -11.329 -9.616  35.807  1.00 7.25  ? 32  VAL A O     1 
ATOM   224  C  CB    . VAL A 1 52  ? -8.993  -10.234 37.638  1.00 9.01  ? 32  VAL A CB    1 
ATOM   225  C  CG1   . VAL A 1 52  ? -8.631  -11.635 37.201  1.00 8.62  ? 32  VAL A CG1   1 
ATOM   226  C  CG2   . VAL A 1 52  ? -7.991  -9.739  38.662  1.00 9.30  ? 32  VAL A CG2   1 
ATOM   227  N  N     . SER A 1 53  ? -9.690  -10.140 34.305  1.00 6.68  ? 33  SER A N     1 
ATOM   228  C  CA    . SER A 1 53  ? -10.581 -10.692 33.293  1.00 6.58  ? 33  SER A CA    1 
ATOM   229  C  C     . SER A 1 53  ? -10.465 -12.217 33.285  1.00 5.81  ? 33  SER A C     1 
ATOM   230  O  O     . SER A 1 53  ? -9.544  -12.808 33.839  1.00 5.36  ? 33  SER A O     1 
ATOM   231  C  CB    . SER A 1 53  ? -10.290 -10.163 31.911  1.00 6.67  ? 33  SER A CB    1 
ATOM   232  O  OG    . SER A 1 53  ? -9.265  -10.951 31.283  1.00 7.50  ? 33  SER A OG    1 
ATOM   233  N  N     . ILE A 1 54  ? -11.449 -12.890 32.682  1.00 5.32  ? 34  ILE A N     1 
ATOM   234  C  CA    . ILE A 1 54  ? -11.400 -14.330 32.512  1.00 5.10  ? 34  ILE A CA    1 
ATOM   235  C  C     . ILE A 1 54  ? -10.114 -14.772 31.830  1.00 4.87  ? 34  ILE A C     1 
ATOM   236  O  O     . ILE A 1 54  ? -9.707  -15.905 32.048  1.00 5.61  ? 34  ILE A O     1 
ATOM   237  C  CB    . ILE A 1 54  ? -12.634 -14.910 31.815  1.00 5.27  ? 34  ILE A CB    1 
ATOM   238  C  CG1   . ILE A 1 54  ? -12.866 -14.298 30.442  1.00 5.32  ? 34  ILE A CG1   1 
ATOM   239  C  CG2   . ILE A 1 54  ? -13.836 -14.700 32.730  1.00 5.31  ? 34  ILE A CG2   1 
ATOM   240  C  CD1   . ILE A 1 54  ? -14.014 -14.949 29.708  1.00 5.64  ? 34  ILE A CD1   1 
ATOM   241  N  N     . TRP A 1 55  ? -9.563  -13.949 30.943  1.00 4.66  ? 35  TRP A N     1 
ATOM   242  C  CA    . TRP A 1 55  ? -8.366  -14.333 30.213  1.00 4.90  ? 35  TRP A CA    1 
ATOM   243  C  C     . TRP A 1 55  ? -7.127  -14.195 31.092  1.00 5.14  ? 35  TRP A C     1 
ATOM   244  O  O     . TRP A 1 55  ? -6.117  -14.871 30.825  1.00 6.53  ? 35  TRP A O     1 
ATOM   245  C  CB    . TRP A 1 55  ? -8.221  -13.578 28.895  1.00 4.66  ? 35  TRP A CB    1 
ATOM   246  C  CG    . TRP A 1 55  ? -8.899  -14.286 27.767  1.00 4.86  ? 35  TRP A CG    1 
ATOM   247  C  CD1   . TRP A 1 55  ? -10.203 -14.170 27.358  1.00 4.97  ? 35  TRP A CD1   1 
ATOM   248  C  CD2   . TRP A 1 55  ? -8.406  -15.461 27.097  1.00 4.80  ? 35  TRP A CD2   1 
ATOM   249  N  NE1   . TRP A 1 55  ? -10.499 -15.098 26.390  1.00 5.43  ? 35  TRP A NE1   1 
ATOM   250  C  CE2   . TRP A 1 55  ? -9.407  -15.928 26.213  1.00 5.15  ? 35  TRP A CE2   1 
ATOM   251  C  CE3   . TRP A 1 55  ? -7.177  -16.130 27.116  1.00 4.66  ? 35  TRP A CE3   1 
ATOM   252  C  CZ2   . TRP A 1 55  ? -9.226  -17.008 25.350  1.00 5.40  ? 35  TRP A CZ2   1 
ATOM   253  C  CZ3   . TRP A 1 55  ? -6.990  -17.174 26.237  1.00 4.88  ? 35  TRP A CZ3   1 
ATOM   254  C  CH2   . TRP A 1 55  ? -8.006  -17.640 25.404  1.00 5.07  ? 35  TRP A CH2   1 
ATOM   255  N  N     . ASP A 1 56  ? -7.170  -13.291 32.054  1.00 5.07  ? 36  ASP A N     1 
ATOM   256  C  CA    . ASP A 1 56  ? -6.102  -13.274 33.074  1.00 5.57  ? 36  ASP A CA    1 
ATOM   257  C  C     . ASP A 1 56  ? -6.146  -14.576 33.855  1.00 5.76  ? 36  ASP A C     1 
ATOM   258  O  O     . ASP A 1 56  ? -5.131  -15.260 34.022  1.00 6.57  ? 36  ASP A O     1 
ATOM   259  C  CB    . ASP A 1 56  ? -6.239  -12.087 34.028  1.00 6.02  ? 36  ASP A CB    1 
ATOM   260  C  CG    . ASP A 1 56  ? -6.162  -10.727 33.371  1.00 7.03  ? 36  ASP A CG    1 
ATOM   261  O  OD1   . ASP A 1 56  ? -7.210  -10.240 32.881  1.00 7.52  ? 36  ASP A OD1   1 
ATOM   262  O  OD2   . ASP A 1 56  ? -5.031  -10.133 33.342  1.00 10.16 ? 36  ASP A OD2   1 
ATOM   263  N  N     . THR A 1 57  ? -7.334  -14.950 34.320  1.00 5.84  ? 37  THR A N     1 
ATOM   264  C  CA    . THR A 1 57  ? -7.466  -16.200 35.067  1.00 6.19  ? 37  THR A CA    1 
ATOM   265  C  C     . THR A 1 57  ? -7.034  -17.407 34.227  1.00 6.79  ? 37  THR A C     1 
ATOM   266  O  O     . THR A 1 57  ? -6.274  -18.281 34.679  1.00 6.93  ? 37  THR A O     1 
ATOM   267  C  CB    . THR A 1 57  ? -8.926  -16.351 35.499  1.00 7.16  ? 37  THR A CB    1 
ATOM   268  O  OG1   . THR A 1 57  ? -9.294  -15.193 36.281  1.00 8.24  ? 37  THR A OG1   1 
ATOM   269  C  CG2   . THR A 1 57  ? -9.103  -17.621 36.305  1.00 7.96  ? 37  THR A CG2   1 
ATOM   270  N  N     . PHE A 1 58  ? -7.501  -17.438 32.977  1.00 6.12  ? 38  PHE A N     1 
ATOM   271  C  CA    . PHE A 1 58  ? -7.257  -18.576 32.106  1.00 6.33  ? 38  PHE A CA    1 
ATOM   272  C  C     . PHE A 1 58  ? -5.792  -18.705 31.687  1.00 6.89  ? 38  PHE A C     1 
ATOM   273  O  O     . PHE A 1 58  ? -5.235  -19.806 31.778  1.00 6.88  ? 38  PHE A O     1 
ATOM   274  C  CB    . PHE A 1 58  ? -8.146  -18.468 30.876  1.00 6.25  ? 38  PHE A CB    1 
ATOM   275  C  CG    . PHE A 1 58  ? -8.233  -19.687 30.005  1.00 5.84  ? 38  PHE A CG    1 
ATOM   276  C  CD1   . PHE A 1 58  ? -8.968  -20.808 30.415  1.00 6.19  ? 38  PHE A CD1   1 
ATOM   277  C  CD2   . PHE A 1 58  ? -7.731  -19.674 28.726  1.00 5.81  ? 38  PHE A CD2   1 
ATOM   278  C  CE1   . PHE A 1 58  ? -9.097  -21.898 29.589  1.00 6.10  ? 38  PHE A CE1   1 
ATOM   279  C  CE2   . PHE A 1 58  ? -7.923  -20.756 27.878  1.00 5.99  ? 38  PHE A CE2   1 
ATOM   280  C  CZ    . PHE A 1 58  ? -8.632  -21.848 28.303  1.00 6.04  ? 38  PHE A CZ    1 
ATOM   281  N  N     A SER A 1 59  ? -5.190  -17.586 31.279  0.50 7.61  ? 39  SER A N     1 
ATOM   282  N  N     B SER A 1 59  ? -5.126  -17.612 31.307  0.50 5.81  ? 39  SER A N     1 
ATOM   283  C  CA    A SER A 1 59  ? -3.798  -17.552 30.860  0.50 8.46  ? 39  SER A CA    1 
ATOM   284  C  CA    B SER A 1 59  ? -3.743  -17.705 30.844  0.50 5.32  ? 39  SER A CA    1 
ATOM   285  C  C     A SER A 1 59  ? -2.898  -18.021 31.991  0.50 7.77  ? 39  SER A C     1 
ATOM   286  C  C     B SER A 1 59  ? -2.783  -17.904 32.016  0.50 6.21  ? 39  SER A C     1 
ATOM   287  O  O     A SER A 1 59  ? -1.950  -18.773 31.733  0.50 7.64  ? 39  SER A O     1 
ATOM   288  O  O     B SER A 1 59  ? -1.619  -18.300 31.856  0.50 6.56  ? 39  SER A O     1 
ATOM   289  C  CB    A SER A 1 59  ? -3.423  -16.165 30.374  0.50 9.95  ? 39  SER A CB    1 
ATOM   290  C  CB    B SER A 1 59  ? -3.361  -16.487 30.039  0.50 4.53  ? 39  SER A CB    1 
ATOM   291  O  OG    A SER A 1 59  ? -4.219  -15.864 29.232  0.50 15.02 ? 39  SER A OG    1 
ATOM   292  O  OG    B SER A 1 59  ? -3.260  -15.345 30.875  0.50 3.54  ? 39  SER A OG    1 
ATOM   293  N  N     . HIS A 1 60  ? -3.259  -17.622 33.235  1.00 6.79  ? 40  HIS A N     1 
ATOM   294  C  CA    . HIS A 1 60  ? -2.486  -17.944 34.422  1.00 7.98  ? 40  HIS A CA    1 
ATOM   295  C  C     . HIS A 1 60  ? -2.814  -19.331 34.954  1.00 8.01  ? 40  HIS A C     1 
ATOM   296  O  O     . HIS A 1 60  ? -2.367  -19.636 36.068  1.00 11.58 ? 40  HIS A O     1 
ATOM   297  C  CB    . HIS A 1 60  ? -2.629  -16.868 35.495  1.00 9.20  ? 40  HIS A CB    1 
ATOM   298  C  CG    . HIS A 1 60  ? -1.839  -15.656 35.101  1.00 10.91 ? 40  HIS A CG    1 
ATOM   299  N  ND1   . HIS A 1 60  ? -0.534  -15.505 35.562  1.00 15.22 ? 40  HIS A ND1   1 
ATOM   300  C  CD2   . HIS A 1 60  ? -2.082  -14.585 34.311  1.00 10.59 ? 40  HIS A CD2   1 
ATOM   301  C  CE1   . HIS A 1 60  ? -0.033  -14.368 35.040  1.00 15.13 ? 40  HIS A CE1   1 
ATOM   302  N  NE2   . HIS A 1 60  ? -0.973  -13.764 34.306  1.00 11.08 ? 40  HIS A NE2   1 
ATOM   303  N  N     . THR A 1 61  ? -3.630  -20.133 34.255  1.00 7.17  ? 41  THR A N     1 
ATOM   304  C  CA    . THR A 1 61  ? -3.931  -21.492 34.662  1.00 7.80  ? 41  THR A CA    1 
ATOM   305  C  C     . THR A 1 61  ? -2.986  -22.427 33.902  1.00 7.96  ? 41  THR A C     1 
ATOM   306  O  O     . THR A 1 61  ? -2.954  -22.447 32.673  1.00 7.24  ? 41  THR A O     1 
ATOM   307  C  CB    . THR A 1 61  ? -5.365  -21.854 34.342  1.00 7.57  ? 41  THR A CB    1 
ATOM   308  O  OG1   . THR A 1 61  ? -6.280  -20.982 35.018  1.00 8.35  ? 41  THR A OG1   1 
ATOM   309  C  CG2   . THR A 1 61  ? -5.685  -23.262 34.777  1.00 8.26  ? 41  THR A CG2   1 
ATOM   310  N  N     . PRO A 1 62  ? -2.121  -23.185 34.613  1.00 8.30  ? 42  PRO A N     1 
ATOM   311  C  CA    . PRO A 1 62  ? -1.165  -24.045 33.927  1.00 8.67  ? 42  PRO A CA    1 
ATOM   312  C  C     . PRO A 1 62  ? -1.791  -24.947 32.879  1.00 8.16  ? 42  PRO A C     1 
ATOM   313  O  O     . PRO A 1 62  ? -2.850  -25.601 33.082  1.00 9.38  ? 42  PRO A O     1 
ATOM   314  C  CB    . PRO A 1 62  ? -0.634  -24.896 35.080  1.00 9.02  ? 42  PRO A CB    1 
ATOM   315  C  CG    . PRO A 1 62  ? -0.632  -23.923 36.225  1.00 9.51  ? 42  PRO A CG    1 
ATOM   316  C  CD    . PRO A 1 62  ? -1.945  -23.192 36.059  1.00 9.75  ? 42  PRO A CD    1 
ATOM   317  N  N     . GLY A 1 63  ? -1.156  -24.917 31.716  1.00 7.73  ? 43  GLY A N     1 
ATOM   318  C  CA    . GLY A 1 63  ? -1.489  -25.791 30.622  1.00 7.52  ? 43  GLY A CA    1 
ATOM   319  C  C     . GLY A 1 63  ? -2.533  -25.262 29.643  1.00 8.02  ? 43  GLY A C     1 
ATOM   320  O  O     . GLY A 1 63  ? -2.753  -25.911 28.606  1.00 9.46  ? 43  GLY A O     1 
ATOM   321  N  N     . LYS A 1 64  ? -3.207  -24.144 29.976  1.00 7.19  ? 44  LYS A N     1 
ATOM   322  C  CA    . LYS A 1 64  ? -4.230  -23.633 29.071  1.00 6.93  ? 44  LYS A CA    1 
ATOM   323  C  C     . LYS A 1 64  ? -3.653  -22.985 27.817  1.00 7.12  ? 44  LYS A C     1 
ATOM   324  O  O     . LYS A 1 64  ? -4.343  -23.014 26.801  1.00 8.41  ? 44  LYS A O     1 
ATOM   325  C  CB    . LYS A 1 64  ? -5.112  -22.641 29.821  1.00 6.82  ? 44  LYS A CB    1 
ATOM   326  C  CG    . LYS A 1 64  ? -5.912  -23.288 30.943  1.00 7.82  ? 44  LYS A CG    1 
ATOM   327  C  CD    . LYS A 1 64  ? -6.716  -24.485 30.549  1.00 9.54  ? 44  LYS A CD    1 
ATOM   328  C  CE    . LYS A 1 64  ? -7.607  -24.959 31.688  1.00 11.16 ? 44  LYS A CE    1 
ATOM   329  N  NZ    . LYS A 1 64  ? -8.360  -26.181 31.303  1.00 13.91 ? 44  LYS A NZ    1 
ATOM   330  N  N     . ILE A 1 65  ? -2.459  -22.378 27.888  1.00 6.49  ? 45  ILE A N     1 
ATOM   331  C  CA    . ILE A 1 65  ? -1.856  -21.690 26.744  1.00 6.84  ? 45  ILE A CA    1 
ATOM   332  C  C     . ILE A 1 65  ? -0.693  -22.557 26.275  1.00 7.49  ? 45  ILE A C     1 
ATOM   333  O  O     . ILE A 1 65  ? 0.078   -23.033 27.092  1.00 8.20  ? 45  ILE A O     1 
ATOM   334  C  CB    . ILE A 1 65  ? -1.358  -20.292 27.155  1.00 6.90  ? 45  ILE A CB    1 
ATOM   335  C  CG1   . ILE A 1 65  ? -2.418  -19.487 27.912  1.00 7.22  ? 45  ILE A CG1   1 
ATOM   336  C  CG2   . ILE A 1 65  ? -0.818  -19.486 25.945  1.00 7.35  ? 45  ILE A CG2   1 
ATOM   337  C  CD1   . ILE A 1 65  ? -3.748  -19.388 27.225  1.00 7.14  ? 45  ILE A CD1   1 
ATOM   338  N  N     . ALA A 1 66  ? -0.559  -22.722 24.961  1.00 7.46  ? 46  ALA A N     1 
ATOM   339  C  CA    . ALA A 1 66  ? 0.375   -23.666 24.368  1.00 7.80  ? 46  ALA A CA    1 
ATOM   340  C  C     . ALA A 1 66  ? 1.805   -23.469 24.847  1.00 7.54  ? 46  ALA A C     1 
ATOM   341  O  O     . ALA A 1 66  ? 2.573   -24.446 24.891  1.00 7.60  ? 46  ALA A O     1 
ATOM   342  C  CB    . ALA A 1 66  ? 0.291   -23.534 22.876  1.00 8.72  ? 46  ALA A CB    1 
ATOM   343  N  N     . ASP A 1 67  ? 2.207   -22.225 25.067  1.00 7.91  ? 47  ASP A N     1 
ATOM   344  C  CA    . ASP A 1 67  ? 3.633   -21.912 25.210  1.00 7.87  ? 47  ASP A CA    1 
ATOM   345  C  C     . ASP A 1 67  ? 3.915   -21.208 26.525  1.00 8.80  ? 47  ASP A C     1 
ATOM   346  O  O     . ASP A 1 67  ? 4.959   -20.585 26.723  1.00 8.82  ? 47  ASP A O     1 
ATOM   347  C  CB    . ASP A 1 67  ? 4.101   -21.015 24.064  1.00 8.52  ? 47  ASP A CB    1 
ATOM   348  C  CG    . ASP A 1 67  ? 3.352   -19.684 23.986  1.00 8.53  ? 47  ASP A CG    1 
ATOM   349  O  OD1   . ASP A 1 67  ? 2.499   -19.456 24.870  1.00 7.78  ? 47  ASP A OD1   1 
ATOM   350  O  OD2   . ASP A 1 67  ? 3.702   -18.872 23.101  1.00 9.10  ? 47  ASP A OD2   1 
ATOM   351  N  N     . GLY A 1 68  ? 2.982   -21.311 27.471  1.00 8.25  ? 48  GLY A N     1 
ATOM   352  C  CA    . GLY A 1 68  ? 3.221   -20.771 28.795  1.00 9.64  ? 48  GLY A CA    1 
ATOM   353  C  C     . GLY A 1 68  ? 3.118   -19.252 28.924  1.00 9.70  ? 48  GLY A C     1 
ATOM   354  O  O     . GLY A 1 68  ? 3.481   -18.687 29.958  1.00 13.80 ? 48  GLY A O     1 
ATOM   355  N  N     . THR A 1 69  ? 2.731   -18.566 27.853  1.00 7.92  ? 49  THR A N     1 
ATOM   356  C  CA    . THR A 1 69  ? 2.675   -17.133 27.861  1.00 7.37  ? 49  THR A CA    1 
ATOM   357  C  C     . THR A 1 69  ? 1.308   -16.657 28.355  1.00 7.37  ? 49  THR A C     1 
ATOM   358  O  O     . THR A 1 69  ? 0.371   -17.437 28.498  1.00 7.01  ? 49  THR A O     1 
ATOM   359  C  CB    . THR A 1 69  ? 2.976   -16.539 26.482  1.00 7.33  ? 49  THR A CB    1 
ATOM   360  O  OG1   . THR A 1 69  ? 2.012   -16.991 25.537  1.00 7.15  ? 49  THR A OG1   1 
ATOM   361  C  CG2   . THR A 1 69  ? 4.348   -16.918 25.981  1.00 8.19  ? 49  THR A CG2   1 
ATOM   362  N  N     . THR A 1 70  ? 1.290   -15.353 28.667  1.00 8.08  ? 50  THR A N     1 
ATOM   363  C  CA    . THR A 1 70  ? 0.086   -14.673 29.122  1.00 7.68  ? 50  THR A CA    1 
ATOM   364  C  C     . THR A 1 70  ? 0.001   -13.358 28.387  1.00 7.14  ? 50  THR A C     1 
ATOM   365  O  O     . THR A 1 70  ? 0.930   -12.950 27.683  1.00 6.93  ? 50  THR A O     1 
ATOM   366  C  CB    . THR A 1 70  ? 0.068   -14.420 30.639  1.00 8.78  ? 50  THR A CB    1 
ATOM   367  O  OG1   . THR A 1 70  ? 1.003   -13.380 30.946  1.00 8.20  ? 50  THR A OG1   1 
ATOM   368  C  CG2   . THR A 1 70  ? 0.427   -15.683 31.393  1.00 10.04 ? 50  THR A CG2   1 
ATOM   369  N  N     . GLY A 1 71  ? -1.112  -12.656 28.621  1.00 6.51  ? 51  GLY A N     1 
ATOM   370  C  CA    . GLY A 1 71  ? -1.306  -11.305 28.173  1.00 6.16  ? 51  GLY A CA    1 
ATOM   371  C  C     . GLY A 1 71  ? -0.736  -10.270 29.134  1.00 5.78  ? 51  GLY A C     1 
ATOM   372  O  O     . GLY A 1 71  ? -0.983  -9.076  28.996  1.00 5.38  ? 51  GLY A O     1 
ATOM   373  N  N     . ASP A 1 72  ? 0.104   -10.684 30.097  1.00 6.25  ? 52  ASP A N     1 
ATOM   374  C  CA    . ASP A 1 72  ? 0.557   -9.726  31.087  1.00 6.67  ? 52  ASP A CA    1 
ATOM   375  C  C     . ASP A 1 72  ? 1.297   -8.524  30.498  1.00 6.48  ? 52  ASP A C     1 
ATOM   376  O  O     . ASP A 1 72  ? 1.134   -7.387  30.988  1.00 7.24  ? 52  ASP A O     1 
ATOM   377  C  CB    . ASP A 1 72  ? 1.428   -10.391 32.143  1.00 7.55  ? 52  ASP A CB    1 
ATOM   378  C  CG    . ASP A 1 72  ? 0.714   -11.225 33.187  1.00 10.24 ? 52  ASP A CG    1 
ATOM   379  O  OD1   . ASP A 1 72  ? -0.501  -11.420 33.095  1.00 10.15 ? 52  ASP A OD1   1 
ATOM   380  O  OD2   . ASP A 1 72  ? 1.451   -11.747 34.113  1.00 13.05 ? 52  ASP A OD2   1 
ATOM   381  N  N     . VAL A 1 73  ? 2.143   -8.777  29.498  1.00 6.87  ? 53  VAL A N     1 
ATOM   382  C  CA    . VAL A 1 73  ? 2.805   -7.726  28.781  1.00 7.42  ? 53  VAL A CA    1 
ATOM   383  C  C     . VAL A 1 73  ? 2.298   -7.621  27.348  1.00 7.03  ? 53  VAL A C     1 
ATOM   384  O  O     . VAL A 1 73  ? 2.048   -6.516  26.871  1.00 7.81  ? 53  VAL A O     1 
ATOM   385  C  CB    . VAL A 1 73  ? 4.328   -7.896  28.844  1.00 8.35  ? 53  VAL A CB    1 
ATOM   386  C  CG1   . VAL A 1 73  ? 4.955   -6.830  27.972  1.00 9.46  ? 53  VAL A CG1   1 
ATOM   387  C  CG2   . VAL A 1 73  ? 4.789   -7.769  30.291  1.00 9.47  ? 53  VAL A CG2   1 
ATOM   388  N  N     . ALA A 1 74  ? 2.217   -8.745  26.638  1.00 6.87  ? 54  ALA A N     1 
ATOM   389  C  CA    . ALA A 1 74  ? 1.812   -8.815  25.258  1.00 6.74  ? 54  ALA A CA    1 
ATOM   390  C  C     . ALA A 1 74  ? 2.669   -7.870  24.419  1.00 7.06  ? 54  ALA A C     1 
ATOM   391  O  O     . ALA A 1 74  ? 3.906   -7.996  24.435  1.00 8.16  ? 54  ALA A O     1 
ATOM   392  C  CB    . ALA A 1 74  ? 0.322   -8.523  25.202  1.00 7.56  ? 54  ALA A CB    1 
ATOM   393  N  N     . CYS A 1 75  ? 2.055   -6.911  23.729  1.00 6.79  ? 55  CYS A N     1 
ATOM   394  C  CA    . CYS A 1 75  ? 2.761   -5.939  22.912  1.00 6.81  ? 55  CYS A CA    1 
ATOM   395  C  C     . CYS A 1 75  ? 3.002   -4.653  23.673  1.00 6.59  ? 55  CYS A C     1 
ATOM   396  O  O     . CYS A 1 75  ? 3.492   -3.682  23.091  1.00 6.45  ? 55  CYS A O     1 
ATOM   397  C  CB    . CYS A 1 75  ? 1.996   -5.657  21.623  1.00 7.19  ? 55  CYS A CB    1 
ATOM   398  S  SG    . CYS A 1 75  ? 1.588   -7.172  20.733  1.00 8.25  ? 55  CYS A SG    1 
ATOM   399  N  N     . ASP A 1 76  ? 2.561   -4.593  24.944  1.00 6.43  ? 56  ASP A N     1 
ATOM   400  C  CA    . ASP A 1 76  ? 2.644   -3.403  25.780  1.00 6.54  ? 56  ASP A CA    1 
ATOM   401  C  C     . ASP A 1 76  ? 1.969   -2.214  25.102  1.00 6.04  ? 56  ASP A C     1 
ATOM   402  O  O     . ASP A 1 76  ? 2.378   -1.072  25.256  1.00 6.57  ? 56  ASP A O     1 
ATOM   403  C  CB    . ASP A 1 76  ? 4.125   -3.101  26.107  1.00 7.94  ? 56  ASP A CB    1 
ATOM   404  C  CG    . ASP A 1 76  ? 4.354   -2.102  27.215  1.00 9.57  ? 56  ASP A CG    1 
ATOM   405  O  OD1   . ASP A 1 76  ? 3.583   -2.104  28.208  1.00 11.27 ? 56  ASP A OD1   1 
ATOM   406  O  OD2   . ASP A 1 76  ? 5.418   -1.385  27.155  1.00 12.88 ? 56  ASP A OD2   1 
ATOM   407  N  N     . SER A 1 77  ? 0.847   -2.484  24.383  1.00 5.58  ? 57  SER A N     1 
ATOM   408  C  CA    . SER A 1 77  ? 0.188   -1.404  23.672  1.00 6.00  ? 57  SER A CA    1 
ATOM   409  C  C     . SER A 1 77  ? -0.565  -0.414  24.566  1.00 5.96  ? 57  SER A C     1 
ATOM   410  O  O     . SER A 1 77  ? -0.929  0.667   24.108  1.00 5.97  ? 57  SER A O     1 
ATOM   411  C  CB    . SER A 1 77  ? -0.714  -1.928  22.570  1.00 6.47  ? 57  SER A CB    1 
ATOM   412  O  OG    . SER A 1 77  ? 0.064   -2.576  21.547  1.00 7.56  ? 57  SER A OG    1 
ATOM   413  N  N     . TYR A 1 78  ? -0.851  -0.761  25.807  1.00 6.10  ? 58  TYR A N     1 
ATOM   414  C  CA    . TYR A 1 78  ? -1.438  0.198   26.727  1.00 6.43  ? 58  TYR A CA    1 
ATOM   415  C  C     . TYR A 1 78  ? -0.512  1.417   26.851  1.00 7.04  ? 58  TYR A C     1 
ATOM   416  O  O     . TYR A 1 78  ? -0.953  2.551   26.799  1.00 6.49  ? 58  TYR A O     1 
ATOM   417  C  CB    . TYR A 1 78  ? -1.703  -0.453  28.079  1.00 7.00  ? 58  TYR A CB    1 
ATOM   418  C  CG    . TYR A 1 78  ? -2.415  0.469   29.034  1.00 7.48  ? 58  TYR A CG    1 
ATOM   419  C  CD1   . TYR A 1 78  ? -3.763  0.736   28.907  1.00 7.78  ? 58  TYR A CD1   1 
ATOM   420  C  CD2   . TYR A 1 78  ? -1.691  1.139   30.007  1.00 8.01  ? 58  TYR A CD2   1 
ATOM   421  C  CE1   . TYR A 1 78  ? -4.415  1.549   29.803  1.00 8.61  ? 58  TYR A CE1   1 
ATOM   422  C  CE2   . TYR A 1 78  ? -2.318  2.016   30.860  1.00 9.16  ? 58  TYR A CE2   1 
ATOM   423  C  CZ    . TYR A 1 78  ? -3.677  2.201   30.766  1.00 9.33  ? 58  TYR A CZ    1 
ATOM   424  O  OH    . TYR A 1 78  ? -4.320  3.100   31.604  1.00 12.22 ? 58  TYR A OH    1 
ATOM   425  N  N     . HIS A 1 79  ? 0.798   1.145   26.865  1.00 6.58  ? 59  HIS A N     1 
ATOM   426  C  CA    . HIS A 1 79  ? 1.785   2.197   26.885  1.00 8.39  ? 59  HIS A CA    1 
ATOM   427  C  C     . HIS A 1 79  ? 2.266   2.600   25.500  1.00 7.24  ? 59  HIS A C     1 
ATOM   428  O  O     . HIS A 1 79  ? 2.725   3.719   25.337  1.00 8.34  ? 59  HIS A O     1 
ATOM   429  C  CB    . HIS A 1 79  ? 2.941   1.795   27.793  1.00 9.05  ? 59  HIS A CB    1 
ATOM   430  C  CG    . HIS A 1 79  ? 2.556   1.695   29.236  1.00 11.12 ? 59  HIS A CG    1 
ATOM   431  N  ND1   . HIS A 1 79  ? 2.024   2.743   29.949  1.00 14.55 ? 59  HIS A ND1   1 
ATOM   432  C  CD2   . HIS A 1 79  ? 2.554   0.640   30.043  1.00 13.92 ? 59  HIS A CD2   1 
ATOM   433  C  CE1   . HIS A 1 79  ? 1.743   2.311   31.171  1.00 14.48 ? 59  HIS A CE1   1 
ATOM   434  N  NE2   . HIS A 1 79  ? 2.078   1.077   31.263  1.00 13.15 ? 59  HIS A NE2   1 
ATOM   435  N  N     . ARG A 1 80  ? 2.223   1.690   24.534  1.00 7.10  ? 60  ARG A N     1 
ATOM   436  C  CA    . ARG A 1 80  ? 2.885   1.880   23.261  1.00 7.17  ? 60  ARG A CA    1 
ATOM   437  C  C     . ARG A 1 80  ? 1.920   2.065   22.099  1.00 6.24  ? 60  ARG A C     1 
ATOM   438  O  O     . ARG A 1 80  ? 2.274   1.891   20.908  1.00 6.56  ? 60  ARG A O     1 
ATOM   439  C  CB    . ARG A 1 80  ? 3.830   0.713   23.026  1.00 8.41  ? 60  ARG A CB    1 
ATOM   440  C  CG    . ARG A 1 80  ? 4.895   0.610   24.094  1.00 9.93  ? 60  ARG A CG    1 
ATOM   441  C  CD    . ARG A 1 80  ? 5.928   -0.402  23.665  1.00 11.71 ? 60  ARG A CD    1 
ATOM   442  N  NE    . ARG A 1 80  ? 6.803   -0.761  24.756  1.00 13.26 ? 60  ARG A NE    1 
ATOM   443  C  CZ    . ARG A 1 80  ? 8.098   -0.490  24.792  1.00 18.58 ? 60  ARG A CZ    1 
ATOM   444  N  NH1   . ARG A 1 80  ? 8.679   0.012   23.730  1.00 19.26 ? 60  ARG A NH1   1 
ATOM   445  N  NH2   . ARG A 1 80  ? 8.784   -0.685  25.894  1.00 21.38 ? 60  ARG A NH2   1 
ATOM   446  N  N     . TYR A 1 81  ? 0.659   2.449   22.398  1.00 5.65  ? 61  TYR A N     1 
ATOM   447  C  CA    . TYR A 1 81  ? -0.312  2.629   21.330  1.00 5.93  ? 61  TYR A CA    1 
ATOM   448  C  C     . TYR A 1 81  ? 0.153   3.683   20.325  1.00 5.97  ? 61  TYR A C     1 
ATOM   449  O  O     . TYR A 1 81  ? -0.272  3.636   19.169  1.00 5.96  ? 61  TYR A O     1 
ATOM   450  C  CB    . TYR A 1 81  ? -1.716  2.921   21.847  1.00 6.28  ? 61  TYR A CB    1 
ATOM   451  C  CG    . TYR A 1 81  ? -1.898  4.222   22.561  1.00 6.02  ? 61  TYR A CG    1 
ATOM   452  C  CD1   . TYR A 1 81  ? -2.191  5.403   21.866  1.00 6.11  ? 61  TYR A CD1   1 
ATOM   453  C  CD2   . TYR A 1 81  ? -1.784  4.283   23.925  1.00 6.93  ? 61  TYR A CD2   1 
ATOM   454  C  CE1   . TYR A 1 81  ? -2.333  6.607   22.538  1.00 6.40  ? 61  TYR A CE1   1 
ATOM   455  C  CE2   . TYR A 1 81  ? -1.927  5.475   24.605  1.00 7.21  ? 61  TYR A CE2   1 
ATOM   456  C  CZ    . TYR A 1 81  ? -2.215  6.641   23.907  1.00 7.46  ? 61  TYR A CZ    1 
ATOM   457  O  OH    . TYR A 1 81  ? -2.336  7.808   24.664  1.00 8.98  ? 61  TYR A OH    1 
ATOM   458  N  N     . GLY A 1 82  ? 0.967   4.653   20.741  1.00 5.54  ? 62  GLY A N     1 
ATOM   459  C  CA    . GLY A 1 82  ? 1.412   5.665   19.800  1.00 6.08  ? 62  GLY A CA    1 
ATOM   460  C  C     . GLY A 1 82  ? 2.335   5.062   18.751  1.00 6.41  ? 62  GLY A C     1 
ATOM   461  O  O     . GLY A 1 82  ? 2.348   5.521   17.609  1.00 6.68  ? 62  GLY A O     1 
ATOM   462  N  N     . GLU A 1 83  ? 3.114   4.051   19.141  1.00 7.02  ? 63  GLU A N     1 
ATOM   463  C  CA    . GLU A 1 83  ? 3.920   3.310   18.197  1.00 8.51  ? 63  GLU A CA    1 
ATOM   464  C  C     . GLU A 1 83  ? 3.003   2.597   17.224  1.00 8.08  ? 63  GLU A C     1 
ATOM   465  O  O     . GLU A 1 83  ? 3.247   2.569   16.007  1.00 8.62  ? 63  GLU A O     1 
ATOM   466  C  CB    . GLU A 1 83  ? 4.797   2.300   18.926  1.00 11.03 ? 63  GLU A CB    1 
ATOM   467  C  CG    . GLU A 1 83  ? 5.798   2.932   19.863  1.00 13.19 ? 63  GLU A CG    1 
ATOM   468  C  CD    . GLU A 1 83  ? 6.824   1.975   20.436  1.00 20.55 ? 63  GLU A CD    1 
ATOM   469  O  OE1   . GLU A 1 83  ? 7.254   1.076   19.674  1.00 23.53 ? 63  GLU A OE1   1 
ATOM   470  O  OE2   . GLU A 1 83  ? 7.212   2.157   21.617  1.00 23.13 ? 63  GLU A OE2   1 
ATOM   471  N  N     . ASP A 1 84  ? 1.888   2.055   17.737  1.00 6.56  ? 64  ASP A N     1 
ATOM   472  C  CA    . ASP A 1 84  ? 0.932   1.359   16.892  1.00 6.44  ? 64  ASP A CA    1 
ATOM   473  C  C     . ASP A 1 84  ? 0.328   2.333   15.867  1.00 5.69  ? 64  ASP A C     1 
ATOM   474  O  O     . ASP A 1 84  ? 0.153   1.990   14.729  1.00 6.03  ? 64  ASP A O     1 
ATOM   475  C  CB    . ASP A 1 84  ? -0.131  0.678   17.759  1.00 7.28  ? 64  ASP A CB    1 
ATOM   476  C  CG    . ASP A 1 84  ? 0.339   -0.425  18.691  1.00 8.58  ? 64  ASP A CG    1 
ATOM   477  O  OD1   . ASP A 1 84  ? 1.540   -0.888  18.556  1.00 9.65  ? 64  ASP A OD1   1 
ATOM   478  O  OD2   . ASP A 1 84  ? -0.478  -0.842  19.575  1.00 9.22  ? 64  ASP A OD2   1 
ATOM   479  N  N     . ILE A 1 85  ? -0.009  3.544   16.304  1.00 5.22  ? 65  ILE A N     1 
ATOM   480  C  CA    . ILE A 1 85  ? -0.500  4.600   15.431  1.00 5.40  ? 65  ILE A CA    1 
ATOM   481  C  C     . ILE A 1 85  ? 0.557   4.916   14.364  1.00 5.89  ? 65  ILE A C     1 
ATOM   482  O  O     . ILE A 1 85  ? 0.262   5.124   13.222  1.00 6.73  ? 65  ILE A O     1 
ATOM   483  C  CB    . ILE A 1 85  ? -0.904  5.849   16.233  1.00 5.55  ? 65  ILE A CB    1 
ATOM   484  C  CG1   . ILE A 1 85  ? -2.148  5.523   17.038  1.00 5.78  ? 65  ILE A CG1   1 
ATOM   485  C  CG2   . ILE A 1 85  ? -1.088  7.047   15.299  1.00 5.64  ? 65  ILE A CG2   1 
ATOM   486  C  CD1   . ILE A 1 85  ? -2.587  6.612   18.021  1.00 6.19  ? 65  ILE A CD1   1 
ATOM   487  N  N     . GLY A 1 86  ? 1.806   4.974   14.777  1.00 6.33  ? 66  GLY A N     1 
ATOM   488  C  CA    . GLY A 1 86  ? 2.895   5.182   13.820  1.00 6.81  ? 66  GLY A CA    1 
ATOM   489  C  C     . GLY A 1 86  ? 2.928   4.113   12.718  1.00 7.25  ? 66  GLY A C     1 
ATOM   490  O  O     . GLY A 1 86  ? 3.179   4.431   11.537  1.00 7.24  ? 66  GLY A O     1 
ATOM   491  N  N     . LEU A 1 87  ? 2.707   2.856   13.101  1.00 6.63  ? 67  LEU A N     1 
ATOM   492  C  CA    . LEU A 1 87  ? 2.628   1.752   12.133  1.00 7.26  ? 67  LEU A CA    1 
ATOM   493  C  C     . LEU A 1 87  ? 1.446   1.977   11.181  1.00 7.15  ? 67  LEU A C     1 
ATOM   494  O  O     . LEU A 1 87  ? 1.569   1.838   9.972   1.00 7.64  ? 67  LEU A O     1 
ATOM   495  C  CB    . LEU A 1 87  ? 2.498   0.431   12.877  1.00 8.44  ? 67  LEU A CB    1 
ATOM   496  C  CG    . LEU A 1 87  ? 3.707   -0.029  13.684  1.00 9.65  ? 67  LEU A CG    1 
ATOM   497  C  CD1   . LEU A 1 87  ? 3.374   -1.253  14.490  1.00 10.73 ? 67  LEU A CD1   1 
ATOM   498  C  CD2   . LEU A 1 87  ? 4.905   -0.289  12.785  1.00 11.69 ? 67  LEU A CD2   1 
ATOM   499  N  N     . LEU A 1 88  ? 0.248   2.251   11.736  1.00 6.96  ? 68  LEU A N     1 
ATOM   500  C  CA    . LEU A 1 88  ? -0.931  2.420   10.910  1.00 7.27  ? 68  LEU A CA    1 
ATOM   501  C  C     . LEU A 1 88  ? -0.738  3.548   9.920   1.00 8.30  ? 68  LEU A C     1 
ATOM   502  O  O     . LEU A 1 88  ? -1.101  3.452   8.758   1.00 8.67  ? 68  LEU A O     1 
ATOM   503  C  CB    . LEU A 1 88  ? -2.084  2.761   11.855  1.00 6.59  ? 68  LEU A CB    1 
ATOM   504  C  CG    . LEU A 1 88  ? -2.580  1.577   12.662  1.00 6.35  ? 68  LEU A CG    1 
ATOM   505  C  CD1   . LEU A 1 88  ? -3.318  2.112   13.898  1.00 6.43  ? 68  LEU A CD1   1 
ATOM   506  C  CD2   . LEU A 1 88  ? -3.500  0.665   11.838  1.00 6.82  ? 68  LEU A CD2   1 
ATOM   507  N  N     . ASN A 1 89  ? -0.082  4.627   10.368  1.00 8.98  ? 69  ASN A N     1 
ATOM   508  C  CA    . ASN A 1 89  ? 0.213   5.744   9.486   1.00 10.26 ? 69  ASN A CA    1 
ATOM   509  C  C     . ASN A 1 89  ? 1.202   5.317   8.397   1.00 10.15 ? 69  ASN A C     1 
ATOM   510  O  O     . ASN A 1 89  ? 1.023   5.689   7.231   1.00 9.31  ? 69  ASN A O     1 
ATOM   511  C  CB    . ASN A 1 89  ? 0.764   6.907   10.302  1.00 12.52 ? 69  ASN A CB    1 
ATOM   512  C  CG    . ASN A 1 89  ? 1.088   8.098   9.434   1.00 17.21 ? 69  ASN A CG    1 
ATOM   513  O  OD1   . ASN A 1 89  ? 0.178   8.694   8.870   1.00 19.66 ? 69  ASN A OD1   1 
ATOM   514  N  ND2   . ASN A 1 89  ? 2.353   8.458   9.411   1.00 18.69 ? 69  ASN A ND2   1 
ATOM   515  N  N     . ALA A 1 90  ? 2.231   4.589   8.773   1.00 8.83  ? 70  ALA A N     1 
ATOM   516  C  CA    . ALA A 1 90  ? 3.214   4.125   7.809   1.00 8.65  ? 70  ALA A CA    1 
ATOM   517  C  C     . ALA A 1 90  ? 2.613   3.218   6.746   1.00 10.32 ? 70  ALA A C     1 
ATOM   518  O  O     . ALA A 1 90  ? 3.075   3.221   5.588   1.00 12.57 ? 70  ALA A O     1 
ATOM   519  C  CB    . ALA A 1 90  ? 4.337   3.433   8.509   1.00 8.89  ? 70  ALA A CB    1 
ATOM   520  N  N     . LEU A 1 91  ? 1.574   2.470   7.118   1.00 10.70 ? 71  LEU A N     1 
ATOM   521  C  CA    . LEU A 1 91  ? 0.884   1.549   6.227   1.00 11.98 ? 71  LEU A CA    1 
ATOM   522  C  C     . LEU A 1 91  ? -0.134  2.282   5.354   1.00 13.46 ? 71  LEU A C     1 
ATOM   523  O  O     . LEU A 1 91  ? -0.714  1.635   4.457   1.00 17.80 ? 71  LEU A O     1 
ATOM   524  C  CB    . LEU A 1 91  ? 0.221   0.470   7.109   1.00 11.17 ? 71  LEU A CB    1 
ATOM   525  C  CG    . LEU A 1 91  ? 1.175   -0.483  7.837   1.00 11.71 ? 71  LEU A CG    1 
ATOM   526  C  CD1   . LEU A 1 91  ? 0.533   -1.164  9.032   1.00 13.67 ? 71  LEU A CD1   1 
ATOM   527  C  CD2   . LEU A 1 91  ? 1.737   -1.538  6.896   1.00 13.43 ? 71  LEU A CD2   1 
ATOM   528  N  N     . GLY A 1 92  ? -0.360  3.581   5.619   1.00 11.87 ? 72  GLY A N     1 
ATOM   529  C  CA    . GLY A 1 92  ? -1.293  4.391   4.873   1.00 12.97 ? 72  GLY A CA    1 
ATOM   530  C  C     . GLY A 1 92  ? -2.737  3.949   5.076   1.00 12.91 ? 72  GLY A C     1 
ATOM   531  O  O     . GLY A 1 92  ? -3.588  4.215   4.234   1.00 14.07 ? 72  GLY A O     1 
ATOM   532  N  N     . MET A 1 93  ? -3.021  3.387   6.250   1.00 10.79 ? 73  MET A N     1 
ATOM   533  C  CA    . MET A 1 93  ? -4.373  3.007   6.623   1.00 10.02 ? 73  MET A CA    1 
ATOM   534  C  C     . MET A 1 93  ? -5.210  4.258   6.908   1.00 8.65  ? 73  MET A C     1 
ATOM   535  O  O     . MET A 1 93  ? -4.660  5.347   7.161   1.00 8.73  ? 73  MET A O     1 
ATOM   536  C  CB    . MET A 1 93  ? -4.321  2.062   7.844   1.00 12.15 ? 73  MET A CB    1 
ATOM   537  C  CG    . MET A 1 93  ? -3.566  0.770   7.654   1.00 19.65 ? 73  MET A CG    1 
ATOM   538  S  SD    . MET A 1 93  ? -4.545  -0.266  6.625   1.00 21.70 ? 73  MET A SD    1 
ATOM   539  C  CE    . MET A 1 93  ? -3.486  -1.729  6.628   1.00 20.30 ? 73  MET A CE    1 
ATOM   540  N  N     . ASN A 1 94  ? -6.537  4.136   6.879   1.00 7.26  ? 74  ASN A N     1 
ATOM   541  C  CA    . ASN A 1 94  ? -7.410  5.237   7.251   1.00 7.80  ? 74  ASN A CA    1 
ATOM   542  C  C     . ASN A 1 94  ? -8.351  4.850   8.380   1.00 6.76  ? 74  ASN A C     1 
ATOM   543  O  O     . ASN A 1 94  ? -9.217  5.643   8.723   1.00 7.36  ? 74  ASN A O     1 
ATOM   544  C  CB    . ASN A 1 94  ? -8.198  5.770   6.047   1.00 8.61  ? 74  ASN A CB    1 
ATOM   545  C  CG    . ASN A 1 94  ? -9.188  4.766   5.490   1.00 10.20 ? 74  ASN A CG    1 
ATOM   546  O  OD1   . ASN A 1 94  ? -9.671  3.883   6.195   1.00 10.11 ? 74  ASN A OD1   1 
ATOM   547  N  ND2   . ASN A 1 94  ? -9.491  4.893   4.211   1.00 11.43 ? 74  ASN A ND2   1 
ATOM   548  N  N     . ALA A 1 95  ? -8.059  3.737   9.090   1.00 6.38  ? 75  ALA A N     1 
ATOM   549  C  CA    . ALA A 1 95  ? -8.917  3.285   10.159  1.00 5.96  ? 75  ALA A CA    1 
ATOM   550  C  C     . ALA A 1 95  ? -8.134  2.299   11.009  1.00 5.57  ? 75  ALA A C     1 
ATOM   551  O  O     . ALA A 1 95  ? -7.159  1.736   10.547  1.00 5.73  ? 75  ALA A O     1 
ATOM   552  C  CB    . ALA A 1 95  ? -10.166 2.613   9.621   1.00 5.65  ? 75  ALA A CB    1 
ATOM   553  N  N     . TYR A 1 96  ? -8.573  2.145   12.248  1.00 5.06  ? 76  TYR A N     1 
ATOM   554  C  CA    . TYR A 1 96  ? -8.049  1.135   13.147  1.00 5.05  ? 76  TYR A CA    1 
ATOM   555  C  C     . TYR A 1 96  ? -9.185  0.539   13.938  1.00 5.04  ? 76  TYR A C     1 
ATOM   556  O  O     . TYR A 1 96  ? -9.980  1.250   14.547  1.00 5.77  ? 76  TYR A O     1 
ATOM   557  C  CB    . TYR A 1 96  ? -7.099  1.781   14.142  1.00 5.03  ? 76  TYR A CB    1 
ATOM   558  C  CG    . TYR A 1 96  ? -6.411  0.887   15.130  1.00 5.36  ? 76  TYR A CG    1 
ATOM   559  C  CD1   . TYR A 1 96  ? -5.967  -0.376  14.807  1.00 5.58  ? 76  TYR A CD1   1 
ATOM   560  C  CD2   . TYR A 1 96  ? -6.188  1.355   16.405  1.00 5.58  ? 76  TYR A CD2   1 
ATOM   561  C  CE1   . TYR A 1 96  ? -5.317  -1.153  15.738  1.00 5.67  ? 76  TYR A CE1   1 
ATOM   562  C  CE2   . TYR A 1 96  ? -5.494  0.607   17.338  1.00 5.78  ? 76  TYR A CE2   1 
ATOM   563  C  CZ    . TYR A 1 96  ? -5.065  -0.654  16.997  1.00 5.73  ? 76  TYR A CZ    1 
ATOM   564  O  OH    . TYR A 1 96  ? -4.357  -1.468  17.875  1.00 7.90  ? 76  TYR A OH    1 
ATOM   565  N  N     . ARG A 1 97  ? -9.244  -0.788  13.863  1.00 4.62  ? 77  ARG A N     1 
ATOM   566  C  CA    . ARG A 1 97  ? -10.200 -1.545  14.631  1.00 4.66  ? 77  ARG A CA    1 
ATOM   567  C  C     . ARG A 1 97  ? -9.495  -2.081  15.857  1.00 4.42  ? 77  ARG A C     1 
ATOM   568  O  O     . ARG A 1 97  ? -8.516  -2.819  15.755  1.00 4.74  ? 77  ARG A O     1 
ATOM   569  C  CB    . ARG A 1 97  ? -10.851 -2.657  13.797  1.00 4.88  ? 77  ARG A CB    1 
ATOM   570  C  CG    . ARG A 1 97  ? -11.793 -3.541  14.611  1.00 5.02  ? 77  ARG A CG    1 
ATOM   571  C  CD    . ARG A 1 97  ? -12.604 -4.441  13.735  1.00 5.62  ? 77  ARG A CD    1 
ATOM   572  N  NE    . ARG A 1 97  ? -13.555 -5.170  14.555  1.00 5.91  ? 77  ARG A NE    1 
ATOM   573  C  CZ    . ARG A 1 97  ? -13.329 -6.402  15.023  1.00 6.06  ? 77  ARG A CZ    1 
ATOM   574  N  NH1   . ARG A 1 97  ? -12.380 -7.173  14.510  1.00 6.27  ? 77  ARG A NH1   1 
ATOM   575  N  NH2   . ARG A 1 97  ? -14.033 -6.825  16.048  1.00 6.78  ? 77  ARG A NH2   1 
ATOM   576  N  N     . PHE A 1 98  ? -10.038 -1.747  17.029  1.00 4.44  ? 78  PHE A N     1 
ATOM   577  C  CA    . PHE A 1 98  ? -9.479  -2.168  18.302  1.00 4.60  ? 78  PHE A CA    1 
ATOM   578  C  C     . PHE A 1 98  ? -10.616 -2.358  19.296  1.00 4.53  ? 78  PHE A C     1 
ATOM   579  O  O     . PHE A 1 98  ? -11.758 -1.939  19.076  1.00 5.26  ? 78  PHE A O     1 
ATOM   580  C  CB    . PHE A 1 98  ? -8.467  -1.131  18.809  1.00 4.79  ? 78  PHE A CB    1 
ATOM   581  C  CG    . PHE A 1 98  ? -9.050  0.195   19.181  1.00 4.69  ? 78  PHE A CG    1 
ATOM   582  C  CD1   . PHE A 1 98  ? -9.298  1.169   18.220  1.00 4.73  ? 78  PHE A CD1   1 
ATOM   583  C  CD2   . PHE A 1 98  ? -9.346  0.474   20.502  1.00 5.07  ? 78  PHE A CD2   1 
ATOM   584  C  CE1   . PHE A 1 98  ? -9.852  2.372   18.617  1.00 5.42  ? 78  PHE A CE1   1 
ATOM   585  C  CE2   . PHE A 1 98  ? -9.908  1.685   20.883  1.00 5.45  ? 78  PHE A CE2   1 
ATOM   586  C  CZ    . PHE A 1 98  ? -10.143 2.623   19.925  1.00 5.09  ? 78  PHE A CZ    1 
ATOM   587  N  N     . SER A 1 99  ? -10.304 -2.985  20.411  1.00 4.35  ? 79  SER A N     1 
ATOM   588  C  CA    . SER A 1 99  ? -11.311 -3.236  21.434  1.00 4.56  ? 79  SER A CA    1 
ATOM   589  C  C     . SER A 1 99  ? -10.990 -2.425  22.694  1.00 5.04  ? 79  SER A C     1 
ATOM   590  O  O     . SER A 1 99  ? -9.846  -2.089  23.038  1.00 5.39  ? 79  SER A O     1 
ATOM   591  C  CB    . SER A 1 99  ? -11.525 -4.682  21.686  1.00 4.52  ? 79  SER A CB    1 
ATOM   592  O  OG    . SER A 1 99  ? -10.661 -5.234  22.663  1.00 4.56  ? 79  SER A OG    1 
ATOM   593  N  N     . ILE A 1 100 ? -12.066 -2.098  23.413  1.00 5.55  ? 80  ILE A N     1 
ATOM   594  C  CA    . ILE A 1 100 ? -11.991 -1.500  24.731  1.00 5.74  ? 80  ILE A CA    1 
ATOM   595  C  C     . ILE A 1 100 ? -12.115 -2.626  25.757  1.00 5.70  ? 80  ILE A C     1 
ATOM   596  O  O     . ILE A 1 100 ? -13.017 -3.455  25.635  1.00 6.39  ? 80  ILE A O     1 
ATOM   597  C  CB    . ILE A 1 100 ? -13.072 -0.405  24.868  1.00 6.94  ? 80  ILE A CB    1 
ATOM   598  C  CG1   . ILE A 1 100 ? -12.620 0.784   23.985  1.00 8.74  ? 80  ILE A CG1   1 
ATOM   599  C  CG2   . ILE A 1 100 ? -13.247 -0.049  26.350  1.00 6.34  ? 80  ILE A CG2   1 
ATOM   600  C  CD1   . ILE A 1 100 ? -13.333 2.033   24.102  1.00 11.04 ? 80  ILE A CD1   1 
ATOM   601  N  N     . ALA A 1 101 ? -11.195 -2.674  26.745  1.00 4.71  ? 81  ALA A N     1 
ATOM   602  C  CA    . ALA A 1 101 ? -11.209 -3.700  27.770  1.00 4.93  ? 81  ALA A CA    1 
ATOM   603  C  C     . ALA A 1 101 ? -12.221 -3.364  28.865  1.00 5.02  ? 81  ALA A C     1 
ATOM   604  O  O     . ALA A 1 101 ? -12.030 -2.407  29.608  1.00 4.84  ? 81  ALA A O     1 
ATOM   605  C  CB    . ALA A 1 101 ? -9.843  -3.842  28.369  1.00 4.99  ? 81  ALA A CB    1 
ATOM   606  N  N     . TRP A 1 102 ? -13.338 -4.107  28.900  1.00 5.09  ? 82  TRP A N     1 
ATOM   607  C  CA    . TRP A 1 102 ? -14.341 -3.945  29.945  1.00 5.40  ? 82  TRP A CA    1 
ATOM   608  C  C     . TRP A 1 102 ? -13.680 -3.899  31.332  1.00 5.48  ? 82  TRP A C     1 
ATOM   609  O  O     . TRP A 1 102 ? -14.032 -3.045  32.164  1.00 5.05  ? 82  TRP A O     1 
ATOM   610  C  CB    . TRP A 1 102 ? -15.384 -5.043  29.779  1.00 5.27  ? 82  TRP A CB    1 
ATOM   611  C  CG    . TRP A 1 102 ? -16.579 -5.056  30.690  1.00 5.72  ? 82  TRP A CG    1 
ATOM   612  C  CD1   . TRP A 1 102 ? -16.882 -4.227  31.733  1.00 6.45  ? 82  TRP A CD1   1 
ATOM   613  C  CD2   . TRP A 1 102 ? -17.674 -5.966  30.551  1.00 5.96  ? 82  TRP A CD2   1 
ATOM   614  N  NE1   . TRP A 1 102 ? -18.123 -4.553  32.234  1.00 6.37  ? 82  TRP A NE1   1 
ATOM   615  C  CE2   . TRP A 1 102 ? -18.637 -5.596  31.512  1.00 6.19  ? 82  TRP A CE2   1 
ATOM   616  C  CE3   . TRP A 1 102 ? -17.962 -6.996  29.659  1.00 6.58  ? 82  TRP A CE3   1 
ATOM   617  C  CZ2   . TRP A 1 102 ? -19.815 -6.321  31.670  1.00 6.33  ? 82  TRP A CZ2   1 
ATOM   618  C  CZ3   . TRP A 1 102 ? -19.131 -7.702  29.815  1.00 6.20  ? 82  TRP A CZ3   1 
ATOM   619  C  CH2   . TRP A 1 102 ? -20.052 -7.322  30.778  1.00 5.83  ? 82  TRP A CH2   1 
ATOM   620  N  N     . PRO A 1 103 ? -12.653 -4.730  31.613  1.00 5.52  ? 83  PRO A N     1 
ATOM   621  C  CA    . PRO A 1 103 ? -11.970 -4.672  32.918  1.00 5.59  ? 83  PRO A CA    1 
ATOM   622  C  C     . PRO A 1 103 ? -11.339 -3.321  33.263  1.00 5.41  ? 83  PRO A C     1 
ATOM   623  O  O     . PRO A 1 103 ? -11.081 -3.025  34.427  1.00 5.43  ? 83  PRO A O     1 
ATOM   624  C  CB    . PRO A 1 103 ? -10.918 -5.779  32.771  1.00 6.07  ? 83  PRO A CB    1 
ATOM   625  C  CG    . PRO A 1 103 ? -11.469 -6.735  31.760  1.00 6.41  ? 83  PRO A CG    1 
ATOM   626  C  CD    . PRO A 1 103 ? -12.198 -5.859  30.776  1.00 6.17  ? 83  PRO A CD    1 
ATOM   627  N  N     . ARG A 1 104 ? -11.014 -2.496  32.259  1.00 4.72  ? 84  ARG A N     1 
ATOM   628  C  CA    . ARG A 1 104 ? -10.484 -1.177  32.534  1.00 5.18  ? 84  ARG A CA    1 
ATOM   629  C  C     . ARG A 1 104 ? -11.587 -0.149  32.783  1.00 5.29  ? 84  ARG A C     1 
ATOM   630  O  O     . ARG A 1 104 ? -11.296 0.899   33.317  1.00 5.93  ? 84  ARG A O     1 
ATOM   631  C  CB    . ARG A 1 104 ? -9.626  -0.626  31.398  1.00 5.21  ? 84  ARG A CB    1 
ATOM   632  C  CG    . ARG A 1 104 ? -8.394  -1.472  31.091  1.00 5.48  ? 84  ARG A CG    1 
ATOM   633  C  CD    . ARG A 1 104 ? -7.458  -0.671  30.216  1.00 5.51  ? 84  ARG A CD    1 
ATOM   634  N  NE    . ARG A 1 104 ? -6.285  -1.442  29.801  1.00 5.85  ? 84  ARG A NE    1 
ATOM   635  C  CZ    . ARG A 1 104 ? -5.230  -1.734  30.564  1.00 7.02  ? 84  ARG A CZ    1 
ATOM   636  N  NH1   . ARG A 1 104 ? -5.121  -1.216  31.768  1.00 8.51  ? 84  ARG A NH1   1 
ATOM   637  N  NH2   . ARG A 1 104 ? -4.325  -2.564  30.075  1.00 7.53  ? 84  ARG A NH2   1 
ATOM   638  N  N     . ILE A 1 105 ? -12.825 -0.442  32.370  1.00 4.80  ? 85  ILE A N     1 
ATOM   639  C  CA    . ILE A 1 105 ? -13.898 0.550   32.408  1.00 5.49  ? 85  ILE A CA    1 
ATOM   640  C  C     . ILE A 1 105 ? -14.793 0.291   33.614  1.00 5.79  ? 85  ILE A C     1 
ATOM   641  O  O     . ILE A 1 105 ? -15.152 1.246   34.332  1.00 6.65  ? 85  ILE A O     1 
ATOM   642  C  CB    . ILE A 1 105 ? -14.724 0.538   31.105  1.00 5.52  ? 85  ILE A CB    1 
ATOM   643  C  CG1   . ILE A 1 105 ? -13.804 0.692   29.870  1.00 5.41  ? 85  ILE A CG1   1 
ATOM   644  C  CG2   . ILE A 1 105 ? -15.856 1.580   31.162  1.00 5.59  ? 85  ILE A CG2   1 
ATOM   645  C  CD1   . ILE A 1 105 ? -12.868 1.859   29.938  1.00 5.64  ? 85  ILE A CD1   1 
ATOM   646  N  N     . VAL A 1 106 ? -15.160 -0.972  33.820  1.00 6.40  ? 86  VAL A N     1 
ATOM   647  C  CA    . VAL A 1 106 ? -15.924 -1.377  35.002  1.00 6.53  ? 86  VAL A CA    1 
ATOM   648  C  C     . VAL A 1 106 ? -15.211 -2.573  35.610  1.00 7.22  ? 86  VAL A C     1 
ATOM   649  O  O     . VAL A 1 106 ? -15.430 -3.717  35.217  1.00 7.08  ? 86  VAL A O     1 
ATOM   650  C  CB    . VAL A 1 106 ? -17.388 -1.676  34.652  1.00 7.67  ? 86  VAL A CB    1 
ATOM   651  C  CG1   . VAL A 1 106 ? -18.139 -1.962  35.943  1.00 8.09  ? 86  VAL A CG1   1 
ATOM   652  C  CG2   . VAL A 1 106 ? -18.061 -0.614  33.839  1.00 7.85  ? 86  VAL A CG2   1 
ATOM   653  N  N     . PRO A 1 107 ? -14.170 -2.351  36.445  1.00 6.75  ? 87  PRO A N     1 
ATOM   654  C  CA    . PRO A 1 107 ? -13.306 -3.449  36.872  1.00 6.90  ? 87  PRO A CA    1 
ATOM   655  C  C     . PRO A 1 107 ? -13.977 -4.648  37.535  1.00 8.28  ? 87  PRO A C     1 
ATOM   656  O  O     . PRO A 1 107 ? -13.495 -5.756  37.413  1.00 9.82  ? 87  PRO A O     1 
ATOM   657  C  CB    . PRO A 1 107 ? -12.359 -2.744  37.830  1.00 6.89  ? 87  PRO A CB    1 
ATOM   658  C  CG    . PRO A 1 107 ? -12.281 -1.312  37.352  1.00 6.87  ? 87  PRO A CG    1 
ATOM   659  C  CD    . PRO A 1 107 ? -13.692 -1.028  36.868  1.00 7.13  ? 87  PRO A CD    1 
ATOM   660  N  N     . LEU A 1 108 ? -15.141 -4.427  38.156  1.00 7.97  ? 88  LEU A N     1 
ATOM   661  C  CA    . LEU A 1 108 ? -15.851 -5.516  38.807  1.00 9.65  ? 88  LEU A CA    1 
ATOM   662  C  C     . LEU A 1 108 ? -16.921 -6.104  37.887  1.00 9.94  ? 88  LEU A C     1 
ATOM   663  O  O     . LEU A 1 108 ? -17.688 -6.967  38.315  1.00 11.63 ? 88  LEU A O     1 
ATOM   664  C  CB    . LEU A 1 108 ? -16.501 -4.973  40.083  1.00 10.90 ? 88  LEU A CB    1 
ATOM   665  C  CG    . LEU A 1 108 ? -15.536 -4.487  41.151  1.00 13.12 ? 88  LEU A CG    1 
ATOM   666  C  CD1   . LEU A 1 108 ? -16.303 -3.889  42.322  1.00 14.31 ? 88  LEU A CD1   1 
ATOM   667  C  CD2   . LEU A 1 108 ? -14.620 -5.597  41.628  1.00 14.21 ? 88  LEU A CD2   1 
ATOM   668  N  N     . GLY A 1 109 ? -17.013 -5.621  36.659  1.00 8.51  ? 89  GLY A N     1 
ATOM   669  C  CA    . GLY A 1 109 ? -18.026 -6.067  35.709  1.00 9.67  ? 89  GLY A CA    1 
ATOM   670  C  C     . GLY A 1 109 ? -19.354 -5.368  35.883  1.00 10.51 ? 89  GLY A C     1 
ATOM   671  O  O     . GLY A 1 109 ? -19.843 -4.749  34.960  1.00 10.98 ? 89  GLY A O     1 
ATOM   672  N  N     . ALA A 1 110 ? -19.843 -5.442  37.113  1.00 11.20 ? 90  ALA A N     1 
ATOM   673  C  CA    . ALA A 1 110 ? -21.010 -4.739  37.597  1.00 12.68 ? 90  ALA A CA    1 
ATOM   674  C  C     . ALA A 1 110 ? -20.566 -3.988  38.837  1.00 13.16 ? 90  ALA A C     1 
ATOM   675  O  O     . ALA A 1 110 ? -20.290 -4.569  39.873  1.00 15.84 ? 90  ALA A O     1 
ATOM   676  C  CB    . ALA A 1 110 ? -22.105 -5.707  37.957  1.00 13.18 ? 90  ALA A CB    1 
ATOM   677  N  N     . GLY A 1 111 ? -20.442 -2.700  38.696  1.00 11.73 ? 91  GLY A N     1 
ATOM   678  C  CA    . GLY A 1 111 ? -19.914 -1.925  39.795  1.00 10.63 ? 91  GLY A CA    1 
ATOM   679  C  C     . GLY A 1 111 ? -19.482 -0.570  39.284  1.00 10.24 ? 91  GLY A C     1 
ATOM   680  O  O     . GLY A 1 111 ? -19.937 -0.114  38.249  1.00 9.43  ? 91  GLY A O     1 
ATOM   681  N  N     . PRO A 1 112 ? -18.693 0.166   40.086  1.00 9.99  ? 92  PRO A N     1 
ATOM   682  C  CA    . PRO A 1 112 ? -18.313 1.510   39.707  1.00 10.58 ? 92  PRO A CA    1 
ATOM   683  C  C     . PRO A 1 112 ? -17.487 1.580   38.440  1.00 9.40  ? 92  PRO A C     1 
ATOM   684  O  O     . PRO A 1 112 ? -16.837 0.616   38.051  1.00 9.16  ? 92  PRO A O     1 
ATOM   685  C  CB    . PRO A 1 112 ? -17.436 1.992   40.875  1.00 11.32 ? 92  PRO A CB    1 
ATOM   686  C  CG    . PRO A 1 112 ? -17.852 1.113   42.040  1.00 14.04 ? 92  PRO A CG    1 
ATOM   687  C  CD    . PRO A 1 112 ? -18.249 -0.219  41.428  1.00 10.46 ? 92  PRO A CD    1 
ATOM   688  N  N     . ILE A 1 113 ? -17.606 2.709   37.792  1.00 9.27  ? 93  ILE A N     1 
ATOM   689  C  CA    . ILE A 1 113 ? -16.758 3.003   36.647  1.00 10.11 ? 93  ILE A CA    1 
ATOM   690  C  C     . ILE A 1 113 ? -15.347 3.328   37.140  1.00 9.75  ? 93  ILE A C     1 
ATOM   691  O  O     . ILE A 1 113 ? -15.088 3.635   38.288  1.00 10.65 ? 93  ILE A O     1 
ATOM   692  C  CB    . ILE A 1 113 ? -17.343 4.102   35.749  1.00 15.25 ? 93  ILE A CB    1 
ATOM   693  C  CG1   . ILE A 1 113 ? -17.217 5.525   36.255  1.00 23.33 ? 93  ILE A CG1   1 
ATOM   694  C  CG2   . ILE A 1 113 ? -18.758 3.794   35.325  1.00 14.86 ? 93  ILE A CG2   1 
ATOM   695  C  CD1   . ILE A 1 113 ? -17.631 6.550   35.196  1.00 25.64 ? 93  ILE A CD1   1 
ATOM   696  N  N     . ASN A 1 114 ? -14.376 3.087   36.265  1.00 7.35  ? 94  ASN A N     1 
ATOM   697  C  CA    . ASN A 1 114 ? -12.983 3.441   36.455  1.00 7.64  ? 94  ASN A CA    1 
ATOM   698  C  C     . ASN A 1 114 ? -12.639 4.548   35.463  1.00 7.67  ? 94  ASN A C     1 
ATOM   699  O  O     . ASN A 1 114 ? -12.386 4.304   34.271  1.00 7.66  ? 94  ASN A O     1 
ATOM   700  C  CB    . ASN A 1 114 ? -12.098 2.221   36.273  1.00 7.93  ? 94  ASN A CB    1 
ATOM   701  C  CG    . ASN A 1 114 ? -10.625 2.489   36.449  1.00 9.12  ? 94  ASN A CG    1 
ATOM   702  O  OD1   . ASN A 1 114 ? -10.200 3.142   37.414  1.00 12.20 ? 94  ASN A OD1   1 
ATOM   703  N  ND2   . ASN A 1 114 ? -9.811  1.995   35.536  1.00 8.64  ? 94  ASN A ND2   1 
ATOM   704  N  N     . GLN A 1 115 ? -12.636 5.788   35.937  1.00 7.73  ? 95  GLN A N     1 
ATOM   705  C  CA    . GLN A 1 115 ? -12.527 6.899   35.005  1.00 7.94  ? 95  GLN A CA    1 
ATOM   706  C  C     . GLN A 1 115 ? -11.141 6.888   34.344  1.00 7.38  ? 95  GLN A C     1 
ATOM   707  O  O     . GLN A 1 115 ? -11.011 7.319   33.194  1.00 7.84  ? 95  GLN A O     1 
ATOM   708  C  CB    . GLN A 1 115 ? -12.775 8.234   35.705  1.00 9.47  ? 95  GLN A CB    1 
ATOM   709  C  CG    . GLN A 1 115 ? -12.903 9.407   34.731  1.00 11.01 ? 95  GLN A CG    1 
ATOM   710  C  CD    . GLN A 1 115 ? -14.033 9.270   33.740  1.00 12.18 ? 95  GLN A CD    1 
ATOM   711  O  OE1   . GLN A 1 115 ? -15.175 8.883   34.054  1.00 12.27 ? 95  GLN A OE1   1 
ATOM   712  N  NE2   . GLN A 1 115 ? -13.698 9.534   32.500  1.00 12.86 ? 95  GLN A NE2   1 
ATOM   713  N  N     . ALA A 1 116 ? -10.133 6.383   35.041  1.00 7.94  ? 96  ALA A N     1 
ATOM   714  C  CA    . ALA A 1 116 ? -8.812  6.303   34.410  1.00 7.86  ? 96  ALA A CA    1 
ATOM   715  C  C     . ALA A 1 116 ? -8.780  5.476   33.117  1.00 8.57  ? 96  ALA A C     1 
ATOM   716  O  O     . ALA A 1 116 ? -7.990  5.789   32.198  1.00 8.39  ? 96  ALA A O     1 
ATOM   717  C  CB    . ALA A 1 116 ? -7.838  5.682   35.357  1.00 8.84  ? 96  ALA A CB    1 
ATOM   718  N  N     . GLY A 1 117 ? -9.576  4.397   33.098  1.00 7.80  ? 97  GLY A N     1 
ATOM   719  C  CA    . GLY A 1 117 ? -9.702  3.560   31.903  1.00 7.26  ? 97  GLY A CA    1 
ATOM   720  C  C     . GLY A 1 117 ? -10.340 4.366   30.771  1.00 6.77  ? 97  GLY A C     1 
ATOM   721  O  O     . GLY A 1 117 ? -9.892  4.335   29.621  1.00 6.36  ? 97  GLY A O     1 
ATOM   722  N  N     . LEU A 1 118 ? -11.491 5.026   31.054  1.00 7.11  ? 98  LEU A N     1 
ATOM   723  C  CA    . LEU A 1 118 ? -12.143 5.817   30.041  1.00 8.04  ? 98  LEU A CA    1 
ATOM   724  C  C     . LEU A 1 118 ? -11.239 6.934   29.534  1.00 7.38  ? 98  LEU A C     1 
ATOM   725  O  O     . LEU A 1 118 ? -11.210 7.205   28.330  1.00 8.66  ? 98  LEU A O     1 
ATOM   726  C  CB    . LEU A 1 118 ? -13.450 6.402   30.597  1.00 9.43  ? 98  LEU A CB    1 
ATOM   727  C  CG    . LEU A 1 118 ? -14.621 5.430   30.729  1.00 11.75 ? 98  LEU A CG    1 
ATOM   728  C  CD1   . LEU A 1 118 ? -15.711 6.042   31.608  1.00 14.51 ? 98  LEU A CD1   1 
ATOM   729  C  CD2   . LEU A 1 118 ? -15.200 5.094   29.396  1.00 12.23 ? 98  LEU A CD2   1 
ATOM   730  N  N     . ASP A 1 119 ? -10.488 7.575   30.412  1.00 7.92  ? 99  ASP A N     1 
ATOM   731  C  CA    . ASP A 1 119 ? -9.613  8.657   30.016  1.00 8.16  ? 99  ASP A CA    1 
ATOM   732  C  C     . ASP A 1 119 ? -8.507  8.140   29.099  1.00 6.86  ? 99  ASP A C     1 
ATOM   733  O  O     . ASP A 1 119 ? -8.119  8.833   28.141  1.00 6.29  ? 99  ASP A O     1 
ATOM   734  C  CB    . ASP A 1 119 ? -9.008  9.347   31.233  1.00 10.73 ? 99  ASP A CB    1 
ATOM   735  C  CG    . ASP A 1 119 ? -9.992  10.167  32.067  1.00 14.38 ? 99  ASP A CG    1 
ATOM   736  O  OD1   . ASP A 1 119 ? -11.132 10.417  31.593  1.00 16.45 ? 99  ASP A OD1   1 
ATOM   737  O  OD2   . ASP A 1 119 ? -9.572  10.525  33.197  1.00 19.17 ? 99  ASP A OD2   1 
ATOM   738  N  N     . HIS A 1 120 ? -8.011  6.948   29.375  1.00 6.39  ? 100 HIS A N     1 
ATOM   739  C  CA    . HIS A 1 120 ? -6.992  6.331   28.521  1.00 5.66  ? 100 HIS A CA    1 
ATOM   740  C  C     . HIS A 1 120 ? -7.509  6.194   27.089  1.00 5.17  ? 100 HIS A C     1 
ATOM   741  O  O     . HIS A 1 120 ? -6.837  6.582   26.090  1.00 4.64  ? 100 HIS A O     1 
ATOM   742  C  CB    . HIS A 1 120 ? -6.576  4.978   29.074  1.00 5.57  ? 100 HIS A CB    1 
ATOM   743  C  CG    . HIS A 1 120 ? -5.785  4.176   28.089  1.00 6.00  ? 100 HIS A CG    1 
ATOM   744  N  ND1   . HIS A 1 120 ? -4.413  4.365   27.929  1.00 6.37  ? 100 HIS A ND1   1 
ATOM   745  C  CD2   . HIS A 1 120 ? -6.145  3.193   27.252  1.00 5.28  ? 100 HIS A CD2   1 
ATOM   746  C  CE1   . HIS A 1 120 ? -3.990  3.511   27.002  1.00 5.84  ? 100 HIS A CE1   1 
ATOM   747  N  NE2   . HIS A 1 120 ? -5.025  2.808   26.527  1.00 5.99  ? 100 HIS A NE2   1 
ATOM   748  N  N     . TYR A 1 121 ? -8.716  5.615   26.949  1.00 4.43  ? 101 TYR A N     1 
ATOM   749  C  CA    . TYR A 1 121 ? -9.235  5.371   25.610  1.00 4.53  ? 101 TYR A CA    1 
ATOM   750  C  C     . TYR A 1 121 ? -9.699  6.672   24.952  1.00 4.70  ? 101 TYR A C     1 
ATOM   751  O  O     . TYR A 1 121 ? -9.638  6.790   23.739  1.00 5.29  ? 101 TYR A O     1 
ATOM   752  C  CB    . TYR A 1 121 ? -10.383 4.352   25.633  1.00 4.47  ? 101 TYR A CB    1 
ATOM   753  C  CG    . TYR A 1 121 ? -9.917  2.962   25.949  1.00 4.16  ? 101 TYR A CG    1 
ATOM   754  C  CD1   . TYR A 1 121 ? -9.133  2.248   25.030  1.00 4.26  ? 101 TYR A CD1   1 
ATOM   755  C  CD2   . TYR A 1 121 ? -10.230 2.338   27.128  1.00 4.54  ? 101 TYR A CD2   1 
ATOM   756  C  CE1   . TYR A 1 121 ? -8.694  0.970   25.304  1.00 4.07  ? 101 TYR A CE1   1 
ATOM   757  C  CE2   . TYR A 1 121 ? -9.798  1.051   27.438  1.00 4.40  ? 101 TYR A CE2   1 
ATOM   758  C  CZ    . TYR A 1 121 ? -9.038  0.341   26.496  1.00 4.34  ? 101 TYR A CZ    1 
ATOM   759  O  OH    . TYR A 1 121 ? -8.648  -0.925  26.781  1.00 4.89  ? 101 TYR A OH    1 
ATOM   760  N  N     . SER A 1 122 ? -10.059 7.665   25.747  1.00 4.88  ? 102 SER A N     1 
ATOM   761  C  CA    . SER A 1 122 ? -10.320 9.010   25.212  1.00 5.82  ? 102 SER A CA    1 
ATOM   762  C  C     . SER A 1 122 ? -9.060  9.586   24.564  1.00 5.72  ? 102 SER A C     1 
ATOM   763  O  O     . SER A 1 122 ? -9.108  10.105  23.456  1.00 5.09  ? 102 SER A O     1 
ATOM   764  C  CB    . SER A 1 122 ? -10.864 9.906   26.283  1.00 7.12  ? 102 SER A CB    1 
ATOM   765  O  OG    . SER A 1 122 ? -11.134 11.198  25.739  1.00 9.23  ? 102 SER A OG    1 
ATOM   766  N  N     . ARG A 1 123 ? -7.929  9.427   25.248  1.00 6.03  ? 103 ARG A N     1 
ATOM   767  C  CA    . ARG A 1 123 ? -6.699  9.949   24.672  1.00 6.41  ? 103 ARG A CA    1 
ATOM   768  C  C     . ARG A 1 123 ? -6.328  9.192   23.397  1.00 6.89  ? 103 ARG A C     1 
ATOM   769  O  O     . ARG A 1 123 ? -5.896  9.794   22.406  1.00 6.04  ? 103 ARG A O     1 
ATOM   770  C  CB    . ARG A 1 123 ? -5.564  9.875   25.695  1.00 6.46  ? 103 ARG A CB    1 
ATOM   771  C  CG    . ARG A 1 123 ? -5.685  10.894  26.824  1.00 7.09  ? 103 ARG A CG    1 
ATOM   772  C  CD    . ARG A 1 123 ? -4.477  10.811  27.694  1.00 7.05  ? 103 ARG A CD    1 
ATOM   773  N  NE    . ARG A 1 123 ? -4.319  9.625   28.487  1.00 7.21  ? 103 ARG A NE    1 
ATOM   774  C  CZ    . ARG A 1 123 ? -4.830  9.404   29.707  1.00 8.20  ? 103 ARG A CZ    1 
ATOM   775  N  NH1   . ARG A 1 123 ? -5.597  10.304  30.314  1.00 9.99  ? 103 ARG A NH1   1 
ATOM   776  N  NH2   . ARG A 1 123 ? -4.565  8.256   30.321  1.00 9.16  ? 103 ARG A NH2   1 
ATOM   777  N  N     . MET A 1 124 ? -6.449  7.867   23.446  1.00 6.58  ? 104 MET A N     1 
ATOM   778  C  CA    . MET A 1 124 ? -6.132  7.034   22.298  1.00 7.01  ? 104 MET A CA    1 
ATOM   779  C  C     . MET A 1 124 ? -7.048  7.405   21.115  1.00 6.20  ? 104 MET A C     1 
ATOM   780  O  O     . MET A 1 124 ? -6.589  7.495   19.978  1.00 5.53  ? 104 MET A O     1 
ATOM   781  C  CB    . MET A 1 124 ? -6.283  5.552   22.645  1.00 8.65  ? 104 MET A CB    1 
ATOM   782  C  CG    . MET A 1 124 ? -6.000  4.619   21.511  1.00 11.24 ? 104 MET A CG    1 
ATOM   783  S  SD    . MET A 1 124 ? -6.176  2.906   22.214  1.00 16.49 ? 104 MET A SD    1 
ATOM   784  C  CE    . MET A 1 124 ? -6.230  1.996   20.683  1.00 17.79 ? 104 MET A CE    1 
ATOM   785  N  N     . VAL A 1 125 ? -8.368  7.602   21.353  1.00 5.46  ? 105 VAL A N     1 
ATOM   786  C  CA    . VAL A 1 125 ? -9.260  8.007   20.280  1.00 5.91  ? 105 VAL A CA    1 
ATOM   787  C  C     . VAL A 1 125 ? -8.814  9.333   19.670  1.00 5.57  ? 105 VAL A C     1 
ATOM   788  O  O     . VAL A 1 125 ? -8.801  9.515   18.468  1.00 5.75  ? 105 VAL A O     1 
ATOM   789  C  CB    . VAL A 1 125 ? -10.714 8.045   20.775  1.00 6.21  ? 105 VAL A CB    1 
ATOM   790  C  CG1   . VAL A 1 125 ? -11.631 8.913   19.927  1.00 7.16  ? 105 VAL A CG1   1 
ATOM   791  C  CG2   . VAL A 1 125 ? -11.226 6.614   20.932  1.00 6.54  ? 105 VAL A CG2   1 
ATOM   792  N  N     . ASP A 1 126 ? -8.389  10.275  20.515  1.00 5.79  ? 106 ASP A N     1 
ATOM   793  C  CA    . ASP A 1 126 ? -7.981  11.580  20.022  1.00 6.07  ? 106 ASP A CA    1 
ATOM   794  C  C     . ASP A 1 126 ? -6.696  11.433  19.212  1.00 5.69  ? 106 ASP A C     1 
ATOM   795  O  O     . ASP A 1 126 ? -6.520  12.141  18.218  1.00 7.06  ? 106 ASP A O     1 
ATOM   796  C  CB    . ASP A 1 126 ? -7.803  12.532  21.194  1.00 7.23  ? 106 ASP A CB    1 
ATOM   797  C  CG    . ASP A 1 126 ? -9.119  13.023  21.790  1.00 9.31  ? 106 ASP A CG    1 
ATOM   798  O  OD1   . ASP A 1 126 ? -10.174 12.842  21.151  1.00 11.24 ? 106 ASP A OD1   1 
ATOM   799  O  OD2   . ASP A 1 126 ? -9.059  13.703  22.839  1.00 11.28 ? 106 ASP A OD2   1 
ATOM   800  N  N     . ALA A 1 127 ? -5.776  10.586  19.685  1.00 5.71  ? 107 ALA A N     1 
ATOM   801  C  CA    . ALA A 1 127 ? -4.543  10.328  18.934  1.00 5.61  ? 107 ALA A CA    1 
ATOM   802  C  C     . ALA A 1 127 ? -4.830  9.729   17.558  1.00 6.09  ? 107 ALA A C     1 
ATOM   803  O  O     . ALA A 1 127 ? -4.199  10.113  16.572  1.00 6.23  ? 107 ALA A O     1 
ATOM   804  C  CB    . ALA A 1 127 ? -3.573  9.507   19.756  1.00 5.65  ? 107 ALA A CB    1 
ATOM   805  N  N     . LEU A 1 128 ? -5.811  8.813   17.478  1.00 6.04  ? 108 LEU A N     1 
ATOM   806  C  CA    . LEU A 1 128 ? -6.195  8.225   16.215  1.00 6.34  ? 108 LEU A CA    1 
ATOM   807  C  C     . LEU A 1 128 ? -6.753  9.309   15.316  1.00 7.12  ? 108 LEU A C     1 
ATOM   808  O  O     . LEU A 1 128 ? -6.358  9.361   14.169  1.00 7.61  ? 108 LEU A O     1 
ATOM   809  C  CB    . LEU A 1 128 ? -7.208  7.102   16.446  1.00 5.95  ? 108 LEU A CB    1 
ATOM   810  C  CG    . LEU A 1 128 ? -6.605  5.842   17.042  1.00 5.89  ? 108 LEU A CG    1 
ATOM   811  C  CD1   . LEU A 1 128 ? -7.659  4.937   17.650  1.00 5.95  ? 108 LEU A CD1   1 
ATOM   812  C  CD2   . LEU A 1 128 ? -5.733  5.090   16.027  1.00 6.15  ? 108 LEU A CD2   1 
ATOM   813  N  N     . LEU A 1 129 ? -7.745  10.058  15.796  1.00 7.74  ? 109 LEU A N     1 
ATOM   814  C  CA    . LEU A 1 129 ? -8.379  11.094  14.987  1.00 8.58  ? 109 LEU A CA    1 
ATOM   815  C  C     . LEU A 1 129 ? -7.367  12.147  14.552  1.00 9.56  ? 109 LEU A C     1 
ATOM   816  O  O     . LEU A 1 129 ? -7.408  12.567  13.396  1.00 11.15 ? 109 LEU A O     1 
ATOM   817  C  CB    . LEU A 1 129 ? -9.550  11.691  15.763  1.00 9.34  ? 109 LEU A CB    1 
ATOM   818  C  CG    . LEU A 1 129 ? -10.722 10.746  15.912  1.00 11.64 ? 109 LEU A CG    1 
ATOM   819  C  CD1   . LEU A 1 129 ? -11.736 11.411  16.807  1.00 13.29 ? 109 LEU A CD1   1 
ATOM   820  C  CD2   . LEU A 1 129 ? -11.358 10.338  14.607  1.00 12.68 ? 109 LEU A CD2   1 
ATOM   821  N  N     . GLY A 1 130 ? -6.431  12.505  15.415  1.00 10.20 ? 110 GLY A N     1 
ATOM   822  C  CA    . GLY A 1 130 ? -5.344  13.417  15.052  1.00 11.59 ? 110 GLY A CA    1 
ATOM   823  C  C     . GLY A 1 130 ? -4.488  12.908  13.902  1.00 11.19 ? 110 GLY A C     1 
ATOM   824  O  O     . GLY A 1 130 ? -3.953  13.717  13.114  1.00 13.29 ? 110 GLY A O     1 
ATOM   825  N  N     . ALA A 1 131 ? -4.361  11.588  13.756  1.00 9.07  ? 111 ALA A N     1 
ATOM   826  C  CA    . ALA A 1 131 ? -3.574  10.944  12.708  1.00 9.64  ? 111 ALA A CA    1 
ATOM   827  C  C     . ALA A 1 131 ? -4.366  10.652  11.419  1.00 10.45 ? 111 ALA A C     1 
ATOM   828  O  O     . ALA A 1 131 ? -3.820  10.072  10.484  1.00 11.16 ? 111 ALA A O     1 
ATOM   829  C  CB    . ALA A 1 131 ? -3.007  9.667   13.274  1.00 10.11 ? 111 ALA A CB    1 
ATOM   830  N  N     . GLY A 1 132 ? -5.642  10.985  11.424  1.00 10.71 ? 112 GLY A N     1 
ATOM   831  C  CA    . GLY A 1 132 ? -6.536  10.715  10.319  1.00 11.29 ? 112 GLY A CA    1 
ATOM   832  C  C     . GLY A 1 132 ? -6.970  9.263   10.246  1.00 12.19 ? 112 GLY A C     1 
ATOM   833  O  O     . GLY A 1 132 ? -7.190  8.741   9.158   1.00 13.73 ? 112 GLY A O     1 
ATOM   834  N  N     . LEU A 1 133 ? -7.021  8.579   11.404  1.00 9.12  ? 113 LEU A N     1 
ATOM   835  C  CA    . LEU A 1 133 ? -7.423  7.185   11.483  1.00 8.97  ? 113 LEU A CA    1 
ATOM   836  C  C     . LEU A 1 133 ? -8.795  7.103   12.163  1.00 9.42  ? 113 LEU A C     1 
ATOM   837  O  O     . LEU A 1 133 ? -8.917  7.454   13.342  1.00 9.98  ? 113 LEU A O     1 
ATOM   838  C  CB    . LEU A 1 133 ? -6.401  6.410   12.296  1.00 8.74  ? 113 LEU A CB    1 
ATOM   839  C  CG    . LEU A 1 133 ? -4.999  6.370   11.700  1.00 8.64  ? 113 LEU A CG    1 
ATOM   840  C  CD1   . LEU A 1 133 ? -3.976  5.901   12.715  1.00 8.99  ? 113 LEU A CD1   1 
ATOM   841  C  CD2   . LEU A 1 133 ? -4.980  5.440   10.487  1.00 9.48  ? 113 LEU A CD2   1 
ATOM   842  N  N     . GLN A 1 134 ? -9.785  6.596   11.450  1.00 7.75  ? 114 GLN A N     1 
ATOM   843  C  CA    . GLN A 1 134 ? -11.100 6.432   12.037  1.00 7.77  ? 114 GLN A CA    1 
ATOM   844  C  C     . GLN A 1 134 ? -11.120 5.249   13.010  1.00 7.74  ? 114 GLN A C     1 
ATOM   845  O  O     . GLN A 1 134 ? -10.752 4.133   12.655  1.00 7.53  ? 114 GLN A O     1 
ATOM   846  C  CB    . GLN A 1 134 ? -12.103 6.163   10.913  1.00 8.53  ? 114 GLN A CB    1 
ATOM   847  C  CG    . GLN A 1 134 ? -13.501 6.000   11.474  1.00 9.87  ? 114 GLN A CG    1 
ATOM   848  C  CD    . GLN A 1 134 ? -14.514 5.745   10.390  1.00 12.22 ? 114 GLN A CD    1 
ATOM   849  O  OE1   . GLN A 1 134 ? -14.203 5.625   9.194   1.00 14.13 ? 114 GLN A OE1   1 
ATOM   850  N  NE2   . GLN A 1 134 ? -15.745 5.584   10.859  1.00 13.42 ? 114 GLN A NE2   1 
ATOM   851  N  N     . PRO A 1 135 ? -11.513 5.458   14.271  1.00 7.81  ? 115 PRO A N     1 
ATOM   852  C  CA    . PRO A 1 135 ? -11.635 4.357   15.236  1.00 8.08  ? 115 PRO A CA    1 
ATOM   853  C  C     . PRO A 1 135 ? -12.891 3.509   14.990  1.00 8.70  ? 115 PRO A C     1 
ATOM   854  O  O     . PRO A 1 135 ? -13.988 4.052   14.880  1.00 10.36 ? 115 PRO A O     1 
ATOM   855  C  CB    . PRO A 1 135 ? -11.650 5.085   16.587  1.00 8.47  ? 115 PRO A CB    1 
ATOM   856  C  CG    . PRO A 1 135 ? -12.136 6.460   16.280  1.00 10.33 ? 115 PRO A CG    1 
ATOM   857  C  CD    . PRO A 1 135 ? -11.724 6.765   14.877  1.00 8.47  ? 115 PRO A CD    1 
ATOM   858  N  N     . PHE A 1 136 ? -12.694 2.211   14.846  1.00 8.66  ? 116 PHE A N     1 
ATOM   859  C  CA    . PHE A 1 136 ? -13.758 1.244   14.765  1.00 8.76  ? 116 PHE A CA    1 
ATOM   860  C  C     . PHE A 1 136 ? -13.653 0.452   16.049  1.00 9.74  ? 116 PHE A C     1 
ATOM   861  O  O     . PHE A 1 136 ? -12.764 -0.378  16.175  1.00 10.49 ? 116 PHE A O     1 
ATOM   862  C  CB    . PHE A 1 136 ? -13.601 0.322   13.558  1.00 11.11 ? 116 PHE A CB    1 
ATOM   863  C  CG    . PHE A 1 136 ? -14.336 0.719   12.312  1.00 12.08 ? 116 PHE A CG    1 
ATOM   864  C  CD1   . PHE A 1 136 ? -13.963 1.868   11.627  1.00 12.93 ? 116 PHE A CD1   1 
ATOM   865  C  CD2   . PHE A 1 136 ? -15.393 -0.031  11.873  1.00 15.01 ? 116 PHE A CD2   1 
ATOM   866  C  CE1   . PHE A 1 136 ? -14.591 2.200   10.435  1.00 13.69 ? 116 PHE A CE1   1 
ATOM   867  C  CE2   . PHE A 1 136 ? -16.061 0.316   10.721  1.00 13.32 ? 116 PHE A CE2   1 
ATOM   868  C  CZ    . PHE A 1 136 ? -15.650 1.426   10.003  1.00 13.66 ? 116 PHE A CZ    1 
ATOM   869  N  N     . VAL A 1 137 ? -14.546 0.720   16.996  1.00 7.77  ? 117 VAL A N     1 
ATOM   870  C  CA    . VAL A 1 137 ? -14.343 0.222   18.342  1.00 7.40  ? 117 VAL A CA    1 
ATOM   871  C  C     . VAL A 1 137 ? -15.208 -0.994  18.558  1.00 7.14  ? 117 VAL A C     1 
ATOM   872  O  O     . VAL A 1 137 ? -16.414 -0.893  18.420  1.00 9.10  ? 117 VAL A O     1 
ATOM   873  C  CB    . VAL A 1 137 ? -14.664 1.287   19.394  1.00 8.68  ? 117 VAL A CB    1 
ATOM   874  C  CG1   . VAL A 1 137 ? -14.521 0.739   20.803  1.00 10.61 ? 117 VAL A CG1   1 
ATOM   875  C  CG2   . VAL A 1 137 ? -13.771 2.505   19.195  1.00 8.71  ? 117 VAL A CG2   1 
ATOM   876  N  N     . THR A 1 138 ? -14.585 -2.051  19.078  1.00 6.21  ? 118 THR A N     1 
ATOM   877  C  CA    . THR A 1 138 ? -15.296 -3.211  19.606  1.00 6.43  ? 118 THR A CA    1 
ATOM   878  C  C     . THR A 1 138 ? -15.440 -3.084  21.122  1.00 6.35  ? 118 THR A C     1 
ATOM   879  O  O     . THR A 1 138 ? -14.449 -2.961  21.866  1.00 6.40  ? 118 THR A O     1 
ATOM   880  C  CB    . THR A 1 138 ? -14.467 -4.466  19.302  1.00 6.73  ? 118 THR A CB    1 
ATOM   881  O  OG1   . THR A 1 138 ? -14.117 -4.536  17.898  1.00 7.45  ? 118 THR A OG1   1 
ATOM   882  C  CG2   . THR A 1 138 ? -15.122 -5.741  19.748  1.00 7.08  ? 118 THR A CG2   1 
ATOM   883  N  N     . LEU A 1 139 ? -16.671 -3.272  21.618  1.00 5.49  ? 119 LEU A N     1 
ATOM   884  C  CA    . LEU A 1 139 ? -16.852 -3.208  23.051  1.00 5.61  ? 119 LEU A CA    1 
ATOM   885  C  C     . LEU A 1 139 ? -16.437 -4.501  23.746  1.00 5.39  ? 119 LEU A C     1 
ATOM   886  O  O     . LEU A 1 139 ? -15.947 -4.440  24.860  1.00 5.79  ? 119 LEU A O     1 
ATOM   887  C  CB    . LEU A 1 139 ? -18.330 -2.873  23.316  1.00 6.04  ? 119 LEU A CB    1 
ATOM   888  C  CG    . LEU A 1 139 ? -18.698 -1.424  23.083  1.00 6.88  ? 119 LEU A CG    1 
ATOM   889  C  CD1   . LEU A 1 139 ? -20.219 -1.247  23.094  1.00 8.09  ? 119 LEU A CD1   1 
ATOM   890  C  CD2   . LEU A 1 139 ? -18.078 -0.518  24.179  1.00 7.90  ? 119 LEU A CD2   1 
ATOM   891  N  N     . TYR A 1 140 ? -16.752 -5.665  23.175  1.00 5.35  ? 120 TYR A N     1 
ATOM   892  C  CA    . TYR A 1 140 ? -16.440 -6.919  23.841  1.00 5.56  ? 120 TYR A CA    1 
ATOM   893  C  C     . TYR A 1 140 ? -15.652 -7.821  22.923  1.00 5.63  ? 120 TYR A C     1 
ATOM   894  O  O     . TYR A 1 140 ? -16.209 -8.395  21.993  1.00 5.96  ? 120 TYR A O     1 
ATOM   895  C  CB    . TYR A 1 140 ? -17.710 -7.641  24.276  1.00 5.64  ? 120 TYR A CB    1 
ATOM   896  C  CG    . TYR A 1 140 ? -17.405 -8.903  25.060  1.00 5.12  ? 120 TYR A CG    1 
ATOM   897  C  CD1   . TYR A 1 140 ? -16.927 -8.802  26.357  1.00 5.03  ? 120 TYR A CD1   1 
ATOM   898  C  CD2   . TYR A 1 140 ? -17.511 -10.169 24.517  1.00 4.91  ? 120 TYR A CD2   1 
ATOM   899  C  CE1   . TYR A 1 140 ? -16.647 -9.919  27.107  1.00 5.13  ? 120 TYR A CE1   1 
ATOM   900  C  CE2   . TYR A 1 140 ? -17.200 -11.310 25.243  1.00 5.39  ? 120 TYR A CE2   1 
ATOM   901  C  CZ    . TYR A 1 140 ? -16.750 -11.178 26.539  1.00 5.33  ? 120 TYR A CZ    1 
ATOM   902  O  OH    . TYR A 1 140 ? -16.451 -12.296 27.267  1.00 6.76  ? 120 TYR A OH    1 
ATOM   903  N  N     . HIS A 1 141 ? -14.371 -8.003  23.262  1.00 5.67  ? 121 HIS A N     1 
ATOM   904  C  CA    . HIS A 1 141 ? -13.505 -8.929  22.553  1.00 5.46  ? 121 HIS A CA    1 
ATOM   905  C  C     . HIS A 1 141 ? -12.910 -9.906  23.553  1.00 5.55  ? 121 HIS A C     1 
ATOM   906  O  O     . HIS A 1 141 ? -11.694 -10.043 23.670  1.00 5.66  ? 121 HIS A O     1 
ATOM   907  C  CB    . HIS A 1 141 ? -12.487 -8.203  21.678  1.00 5.53  ? 121 HIS A CB    1 
ATOM   908  C  CG    . HIS A 1 141 ? -11.931 -9.004  20.547  1.00 5.59  ? 121 HIS A CG    1 
ATOM   909  N  ND1   . HIS A 1 141 ? -11.794 -8.481  19.278  1.00 4.97  ? 121 HIS A ND1   1 
ATOM   910  C  CD2   . HIS A 1 141 ? -11.448 -10.251 20.497  1.00 5.39  ? 121 HIS A CD2   1 
ATOM   911  C  CE1   . HIS A 1 141 ? -11.200 -9.401  18.514  1.00 4.81  ? 121 HIS A CE1   1 
ATOM   912  N  NE2   . HIS A 1 141 ? -10.967 -10.501 19.230  1.00 4.98  ? 121 HIS A NE2   1 
ATOM   913  N  N     . TRP A 1 142 ? -13.778 -10.481 24.398  1.00 4.83  ? 122 TRP A N     1 
ATOM   914  C  CA    . TRP A 1 142 ? -13.608 -11.737 25.095  1.00 5.25  ? 122 TRP A CA    1 
ATOM   915  C  C     . TRP A 1 142 ? -13.121 -11.585 26.534  1.00 5.36  ? 122 TRP A C     1 
ATOM   916  O  O     . TRP A 1 142 ? -13.064 -12.608 27.209  1.00 6.67  ? 122 TRP A O     1 
ATOM   917  C  CB    . TRP A 1 142 ? -12.726 -12.746 24.348  1.00 5.33  ? 122 TRP A CB    1 
ATOM   918  C  CG    . TRP A 1 142 ? -13.155 -13.038 22.951  1.00 5.65  ? 122 TRP A CG    1 
ATOM   919  C  CD1   . TRP A 1 142 ? -14.295 -12.638 22.287  1.00 5.59  ? 122 TRP A CD1   1 
ATOM   920  C  CD2   . TRP A 1 142 ? -12.444 -13.884 22.055  1.00 5.77  ? 122 TRP A CD2   1 
ATOM   921  N  NE1   . TRP A 1 142 ? -14.287 -13.135 21.016  1.00 6.07  ? 122 TRP A NE1   1 
ATOM   922  C  CE2   . TRP A 1 142 ? -13.168 -13.897 20.834  1.00 5.96  ? 122 TRP A CE2   1 
ATOM   923  C  CE3   . TRP A 1 142 ? -11.234 -14.592 22.174  1.00 5.50  ? 122 TRP A CE3   1 
ATOM   924  C  CZ2   . TRP A 1 142 ? -12.727 -14.638 19.746  1.00 6.60  ? 122 TRP A CZ2   1 
ATOM   925  C  CZ3   . TRP A 1 142 ? -10.823 -15.323 21.081  1.00 6.10  ? 122 TRP A CZ3   1 
ATOM   926  C  CH2   . TRP A 1 142 ? -11.545 -15.327 19.892  1.00 6.55  ? 122 TRP A CH2   1 
ATOM   927  N  N     . ASP A 1 143 ? -12.897 -10.381 27.019  1.00 5.99  ? 123 ASP A N     1 
ATOM   928  C  CA    . ASP A 1 143 ? -12.241 -10.129 28.296  1.00 6.48  ? 123 ASP A CA    1 
ATOM   929  C  C     . ASP A 1 143 ? -13.295 -9.840  29.359  1.00 6.21  ? 123 ASP A C     1 
ATOM   930  O  O     . ASP A 1 143 ? -13.262 -8.818  30.016  1.00 7.22  ? 123 ASP A O     1 
ATOM   931  C  CB    . ASP A 1 143 ? -11.195 -9.023  28.165  1.00 7.34  ? 123 ASP A CB    1 
ATOM   932  C  CG    . ASP A 1 143 ? -11.562 -7.855  27.264  1.00 9.84  ? 123 ASP A CG    1 
ATOM   933  O  OD1   . ASP A 1 143 ? -12.661 -7.866  26.667  1.00 11.40 ? 123 ASP A OD1   1 
ATOM   934  O  OD2   . ASP A 1 143 ? -10.750 -6.961  27.167  1.00 12.36 ? 123 ASP A OD2   1 
ATOM   935  N  N     . LEU A 1 144 ? -14.190 -10.783 29.564  1.00 6.09  ? 124 LEU A N     1 
ATOM   936  C  CA    . LEU A 1 144 ? -15.229 -10.637 30.585  1.00 6.08  ? 124 LEU A CA    1 
ATOM   937  C  C     . LEU A 1 144 ? -14.584 -10.443 31.949  1.00 5.55  ? 124 LEU A C     1 
ATOM   938  O  O     . LEU A 1 144 ? -13.682 -11.206 32.333  1.00 5.47  ? 124 LEU A O     1 
ATOM   939  C  CB    . LEU A 1 144 ? -16.087 -11.889 30.620  1.00 6.52  ? 124 LEU A CB    1 
ATOM   940  C  CG    . LEU A 1 144 ? -17.237 -11.890 31.618  1.00 6.85  ? 124 LEU A CG    1 
ATOM   941  C  CD1   . LEU A 1 144 ? -18.299 -10.954 31.104  1.00 7.10  ? 124 LEU A CD1   1 
ATOM   942  C  CD2   . LEU A 1 144 ? -17.770 -13.296 31.786  1.00 7.40  ? 124 LEU A CD2   1 
ATOM   943  N  N     . PRO A 1 145 ? -15.021 -9.445  32.762  1.00 5.52  ? 125 PRO A N     1 
ATOM   944  C  CA    . PRO A 1 145 ? -14.505 -9.350  34.122  1.00 5.78  ? 125 PRO A CA    1 
ATOM   945  C  C     . PRO A 1 145 ? -14.723 -10.630 34.911  1.00 6.25  ? 125 PRO A C     1 
ATOM   946  O  O     . PRO A 1 145 ? -15.823 -11.180 34.914  1.00 6.35  ? 125 PRO A O     1 
ATOM   947  C  CB    . PRO A 1 145 ? -15.281 -8.159  34.681  1.00 6.25  ? 125 PRO A CB    1 
ATOM   948  C  CG    . PRO A 1 145 ? -15.416 -7.268  33.444  1.00 6.09  ? 125 PRO A CG    1 
ATOM   949  C  CD    . PRO A 1 145 ? -15.777 -8.257  32.372  1.00 5.94  ? 125 PRO A CD    1 
ATOM   950  N  N     . GLN A 1 146 ? -13.673 -11.083 35.614  1.00 5.91  ? 126 GLN A N     1 
ATOM   951  C  CA    . GLN A 1 146 ? -13.759 -12.325 36.365  1.00 6.26  ? 126 GLN A CA    1 
ATOM   952  C  C     . GLN A 1 146 ? -14.881 -12.300 37.391  1.00 6.33  ? 126 GLN A C     1 
ATOM   953  O  O     . GLN A 1 146 ? -15.507 -13.338 37.577  1.00 6.11  ? 126 GLN A O     1 
ATOM   954  C  CB    . GLN A 1 146 ? -12.410 -12.631 37.019  1.00 6.62  ? 126 GLN A CB    1 
ATOM   955  C  CG    . GLN A 1 146 ? -12.372 -13.955 37.821  1.00 7.06  ? 126 GLN A CG    1 
ATOM   956  C  CD    . GLN A 1 146 ? -12.566 -15.174 36.959  1.00 7.71  ? 126 GLN A CD    1 
ATOM   957  O  OE1   . GLN A 1 146 ? -11.932 -15.324 35.905  1.00 8.13  ? 126 GLN A OE1   1 
ATOM   958  N  NE2   . GLN A 1 146 ? -13.459 -16.069 37.367  1.00 9.52  ? 126 GLN A NE2   1 
ATOM   959  N  N     . PRO A 1 147 ? -15.163 -11.198 38.106  1.00 6.96  ? 127 PRO A N     1 
ATOM   960  C  CA    . PRO A 1 147 ? -16.273 -11.246 39.056  1.00 7.83  ? 127 PRO A CA    1 
ATOM   961  C  C     . PRO A 1 147 ? -17.610 -11.664 38.445  1.00 8.65  ? 127 PRO A C     1 
ATOM   962  O  O     . PRO A 1 147 ? -18.426 -12.262 39.138  1.00 9.17  ? 127 PRO A O     1 
ATOM   963  C  CB    . PRO A 1 147 ? -16.252 -9.852  39.676  1.00 8.44  ? 127 PRO A CB    1 
ATOM   964  C  CG    . PRO A 1 147 ? -14.822 -9.447  39.592  1.00 7.84  ? 127 PRO A CG    1 
ATOM   965  C  CD    . PRO A 1 147 ? -14.392 -9.940  38.224  1.00 7.53  ? 127 PRO A CD    1 
ATOM   966  N  N     . LEU A 1 148 ? -17.852 -11.342 37.173  1.00 8.06  ? 128 LEU A N     1 
ATOM   967  C  CA    . LEU A 1 148 ? -19.076 -11.759 36.517  1.00 7.73  ? 128 LEU A CA    1 
ATOM   968  C  C     . LEU A 1 148 ? -19.032 -13.256 36.261  1.00 8.12  ? 128 LEU A C     1 
ATOM   969  O  O     . LEU A 1 148 ? -20.053 -13.943 36.382  1.00 8.90  ? 128 LEU A O     1 
ATOM   970  C  CB    . LEU A 1 148 ? -19.293 -10.970 35.215  1.00 7.52  ? 128 LEU A CB    1 
ATOM   971  C  CG    . LEU A 1 148 ? -19.465 -9.473  35.402  1.00 8.25  ? 128 LEU A CG    1 
ATOM   972  C  CD1   . LEU A 1 148 ? -19.704 -8.758  34.085  1.00 9.02  ? 128 LEU A CD1   1 
ATOM   973  C  CD2   . LEU A 1 148 ? -20.621 -9.171  36.350  1.00 9.04  ? 128 LEU A CD2   1 
ATOM   974  N  N     . GLU A 1 149 ? -17.879 -13.791 35.809  1.00 7.62  ? 129 GLU A N     1 
ATOM   975  C  CA    . GLU A 1 149 ? -17.726 -15.222 35.669  1.00 8.14  ? 129 GLU A CA    1 
ATOM   976  C  C     . GLU A 1 149 ? -17.927 -15.973 36.993  1.00 9.28  ? 129 GLU A C     1 
ATOM   977  O  O     . GLU A 1 149 ? -18.473 -17.088 36.981  1.00 9.90  ? 129 GLU A O     1 
ATOM   978  C  CB    . GLU A 1 149 ? -16.389 -15.558 34.991  1.00 8.64  ? 129 GLU A CB    1 
ATOM   979  C  CG    . GLU A 1 149 ? -16.218 -17.025 34.722  1.00 8.98  ? 129 GLU A CG    1 
ATOM   980  C  CD    . GLU A 1 149 ? -17.286 -17.681 33.847  1.00 9.37  ? 129 GLU A CD    1 
ATOM   981  O  OE1   . GLU A 1 149 ? -17.788 -17.010 32.947  1.00 10.03 ? 129 GLU A OE1   1 
ATOM   982  O  OE2   . GLU A 1 149 ? -17.488 -18.904 34.010  1.00 12.08 ? 129 GLU A OE2   1 
ATOM   983  N  N     . ASP A 1 150 ? -17.515 -15.388 38.123  1.00 10.29 ? 130 ASP A N     1 
ATOM   984  C  CA    . ASP A 1 150 ? -17.814 -15.992 39.427  1.00 10.42 ? 130 ASP A CA    1 
ATOM   985  C  C     . ASP A 1 150 ? -19.321 -16.159 39.667  1.00 12.01 ? 130 ASP A C     1 
ATOM   986  O  O     . ASP A 1 150 ? -19.696 -16.944 40.536  1.00 13.36 ? 130 ASP A O     1 
ATOM   987  C  CB    . ASP A 1 150 ? -17.105 -15.213 40.526  1.00 11.36 ? 130 ASP A CB    1 
ATOM   988  C  CG    . ASP A 1 150 ? -15.577 -15.244 40.449  1.00 15.37 ? 130 ASP A CG    1 
ATOM   989  O  OD1   . ASP A 1 150 ? -15.033 -16.101 39.799  1.00 16.02 ? 130 ASP A OD1   1 
ATOM   990  O  OD2   . ASP A 1 150 ? -14.960 -14.417 41.088  1.00 19.88 ? 130 ASP A OD2   1 
ATOM   991  N  N     . ARG A 1 151 ? -20.149 -15.373 39.008  1.00 11.28 ? 131 ARG A N     1 
ATOM   992  C  CA    . ARG A 1 151 ? -21.613 -15.458 39.065  1.00 13.07 ? 131 ARG A CA    1 
ATOM   993  C  C     . ARG A 1 151 ? -22.200 -15.986 37.759  1.00 12.82 ? 131 ARG A C     1 
ATOM   994  O  O     . ARG A 1 151 ? -23.267 -15.526 37.353  1.00 13.30 ? 131 ARG A O     1 
ATOM   995  C  CB    . ARG A 1 151 ? -22.173 -14.072 39.383  1.00 15.71 ? 131 ARG A CB    1 
ATOM   996  C  CG    . ARG A 1 151 ? -21.761 -13.489 40.721  1.00 21.60 ? 131 ARG A CG    1 
ATOM   997  C  CD    . ARG A 1 151 ? -21.682 -11.969 40.725  1.00 30.01 ? 131 ARG A CD    1 
ATOM   998  N  NE    . ARG A 1 151 ? -21.252 -11.389 42.006  1.00 38.25 ? 131 ARG A NE    1 
ATOM   999  C  CZ    . ARG A 1 151 ? -20.028 -11.447 42.562  1.00 45.71 ? 131 ARG A CZ    1 
ATOM   1000 N  NH1   . ARG A 1 151 ? -18.963 -11.964 41.937  1.00 35.67 ? 131 ARG A NH1   1 
ATOM   1001 N  NH2   . ARG A 1 151 ? -19.881 -10.939 43.780  1.00 47.40 ? 131 ARG A NH2   1 
ATOM   1002 N  N     . LEU A 1 152 ? -21.473 -16.928 37.132  1.00 11.06 ? 132 LEU A N     1 
ATOM   1003 C  CA    . LEU A 1 152 ? -21.854 -17.774 36.005  1.00 10.95 ? 132 LEU A CA    1 
ATOM   1004 C  C     . LEU A 1 152 ? -21.503 -17.150 34.659  1.00 8.95  ? 132 LEU A C     1 
ATOM   1005 O  O     . LEU A 1 152 ? -21.631 -17.838 33.646  1.00 8.84  ? 132 LEU A O     1 
ATOM   1006 C  CB    . LEU A 1 152 ? -23.330 -18.185 36.036  1.00 14.19 ? 132 LEU A CB    1 
ATOM   1007 C  CG    . LEU A 1 152 ? -23.746 -18.950 37.298  1.00 19.36 ? 132 LEU A CG    1 
ATOM   1008 C  CD1   . LEU A 1 152 ? -25.228 -19.317 37.229  1.00 20.65 ? 132 LEU A CD1   1 
ATOM   1009 C  CD2   . LEU A 1 152 ? -22.880 -20.185 37.508  1.00 21.16 ? 132 LEU A CD2   1 
ATOM   1010 N  N     . GLY A 1 153 ? -21.044 -15.886 34.649  1.00 8.22  ? 133 GLY A N     1 
ATOM   1011 C  CA    . GLY A 1 153 ? -20.601 -15.248 33.416  1.00 7.67  ? 133 GLY A CA    1 
ATOM   1012 C  C     . GLY A 1 153 ? -21.683 -15.213 32.339  1.00 8.00  ? 133 GLY A C     1 
ATOM   1013 O  O     . GLY A 1 153 ? -22.824 -14.900 32.627  1.00 8.50  ? 133 GLY A O     1 
ATOM   1014 N  N     . TRP A 1 154 ? -21.351 -15.624 31.128  1.00 7.25  ? 134 TRP A N     1 
ATOM   1015 C  CA    . TRP A 1 154 ? -22.347 -15.631 30.060  1.00 7.71  ? 134 TRP A CA    1 
ATOM   1016 C  C     . TRP A 1 154 ? -23.438 -16.678 30.293  1.00 8.95  ? 134 TRP A C     1 
ATOM   1017 O  O     . TRP A 1 154 ? -24.435 -16.688 29.560  1.00 9.70  ? 134 TRP A O     1 
ATOM   1018 C  CB    . TRP A 1 154 ? -21.682 -15.724 28.695  1.00 7.87  ? 134 TRP A CB    1 
ATOM   1019 C  CG    . TRP A 1 154 ? -20.900 -14.488 28.353  1.00 7.88  ? 134 TRP A CG    1 
ATOM   1020 C  CD1   . TRP A 1 154 ? -19.540 -14.354 28.282  1.00 7.90  ? 134 TRP A CD1   1 
ATOM   1021 C  CD2   . TRP A 1 154 ? -21.437 -13.176 28.089  1.00 7.46  ? 134 TRP A CD2   1 
ATOM   1022 N  NE1   . TRP A 1 154 ? -19.196 -13.073 27.937  1.00 7.40  ? 134 TRP A NE1   1 
ATOM   1023 C  CE2   . TRP A 1 154 ? -20.345 -12.302 27.865  1.00 7.60  ? 134 TRP A CE2   1 
ATOM   1024 C  CE3   . TRP A 1 154 ? -22.732 -12.646 27.979  1.00 7.01  ? 134 TRP A CE3   1 
ATOM   1025 C  CZ2   . TRP A 1 154 ? -20.501 -10.954 27.536  1.00 7.34  ? 134 TRP A CZ2   1 
ATOM   1026 C  CZ3   . TRP A 1 154 ? -22.886 -11.294 27.707  1.00 7.91  ? 134 TRP A CZ3   1 
ATOM   1027 C  CH2   . TRP A 1 154 ? -21.796 -10.461 27.457  1.00 8.02  ? 134 TRP A CH2   1 
ATOM   1028 N  N     . GLY A 1 155 ? -23.290 -17.527 31.304  1.00 8.82  ? 135 GLY A N     1 
ATOM   1029 C  CA    . GLY A 1 155 ? -24.405 -18.374 31.692  1.00 10.61 ? 135 GLY A CA    1 
ATOM   1030 C  C     . GLY A 1 155 ? -25.529 -17.676 32.439  1.00 13.19 ? 135 GLY A C     1 
ATOM   1031 O  O     . GLY A 1 155 ? -26.513 -18.333 32.772  1.00 14.34 ? 135 GLY A O     1 
ATOM   1032 N  N     . SER A 1 156 ? -25.364 -16.421 32.828  1.00 12.25 ? 136 SER A N     1 
ATOM   1033 C  CA    . SER A 1 156 ? -26.372 -15.658 33.559  1.00 13.08 ? 136 SER A CA    1 
ATOM   1034 C  C     . SER A 1 156 ? -26.929 -14.541 32.679  1.00 12.80 ? 136 SER A C     1 
ATOM   1035 O  O     . SER A 1 156 ? -26.153 -13.754 32.109  1.00 12.01 ? 136 SER A O     1 
ATOM   1036 C  CB    . SER A 1 156 ? -25.749 -15.109 34.819  1.00 13.35 ? 136 SER A CB    1 
ATOM   1037 O  OG    . SER A 1 156 ? -26.667 -14.256 35.523  1.00 15.60 ? 136 SER A OG    1 
ATOM   1038 N  N     . ARG A 1 157 ? -28.270 -14.368 32.646  1.00 12.71 ? 137 ARG A N     1 
ATOM   1039 C  CA    . ARG A 1 157 ? -28.900 -13.224 31.986  1.00 14.15 ? 137 ARG A CA    1 
ATOM   1040 C  C     . ARG A 1 157 ? -28.397 -11.908 32.548  1.00 12.98 ? 137 ARG A C     1 
ATOM   1041 O  O     . ARG A 1 157 ? -28.314 -10.914 31.833  1.00 14.38 ? 137 ARG A O     1 
ATOM   1042 C  CB    . ARG A 1 157 ? -30.421 -13.274 32.188  1.00 17.11 ? 137 ARG A CB    1 
ATOM   1043 C  CG    . ARG A 1 157 ? -31.127 -14.298 31.318  1.00 23.39 ? 137 ARG A CG    1 
ATOM   1044 C  CD    . ARG A 1 157 ? -32.612 -14.209 31.677  1.00 25.31 ? 137 ARG A CD    1 
ATOM   1045 N  NE    . ARG A 1 157 ? -33.231 -12.962 31.244  1.00 25.11 ? 137 ARG A NE    1 
ATOM   1046 C  CZ    . ARG A 1 157 ? -33.723 -12.820 30.014  1.00 24.66 ? 137 ARG A CZ    1 
ATOM   1047 N  NH1   . ARG A 1 157 ? -33.648 -13.858 29.210  1.00 22.57 ? 137 ARG A NH1   1 
ATOM   1048 N  NH2   . ARG A 1 157 ? -34.269 -11.688 29.602  1.00 28.86 ? 137 ARG A NH2   1 
ATOM   1049 N  N     . ALA A 1 158 ? -28.027 -11.864 33.832  1.00 11.40 ? 138 ALA A N     1 
ATOM   1050 C  CA    . ALA A 1 158 ? -27.614 -10.622 34.456  1.00 12.21 ? 138 ALA A CA    1 
ATOM   1051 C  C     . ALA A 1 158 ? -26.327 -10.098 33.817  1.00 11.00 ? 138 ALA A C     1 
ATOM   1052 O  O     . ALA A 1 158 ? -26.114 -8.899  33.771  1.00 10.90 ? 138 ALA A O     1 
ATOM   1053 C  CB    . ALA A 1 158 ? -27.427 -10.768 35.912  1.00 14.79 ? 138 ALA A CB    1 
ATOM   1054 N  N     . THR A 1 159 ? -25.567 -10.983 33.202  1.00 8.87  ? 139 THR A N     1 
ATOM   1055 C  CA    . THR A 1 159 ? -24.354 -10.527 32.525  1.00 8.96  ? 139 THR A CA    1 
ATOM   1056 C  C     . THR A 1 159 ? -24.707 -9.746  31.259  1.00 8.61  ? 139 THR A C     1 
ATOM   1057 O  O     . THR A 1 159 ? -24.085 -8.724  30.947  1.00 8.36  ? 139 THR A O     1 
ATOM   1058 C  CB    . THR A 1 159 ? -23.424 -11.708 32.244  1.00 8.22  ? 139 THR A CB    1 
ATOM   1059 O  OG1   . THR A 1 159 ? -23.031 -12.276 33.481  1.00 9.37  ? 139 THR A OG1   1 
ATOM   1060 C  CG2   . THR A 1 159 ? -22.207 -11.323 31.416  1.00 8.59  ? 139 THR A CG2   1 
ATOM   1061 N  N     . ALA A 1 160 ? -25.755 -10.144 30.540  1.00 8.90  ? 140 ALA A N     1 
ATOM   1062 C  CA    . ALA A 1 160 ? -26.250 -9.350  29.427  1.00 9.77  ? 140 ALA A CA    1 
ATOM   1063 C  C     . ALA A 1 160 ? -26.697 -7.955  29.866  1.00 9.58  ? 140 ALA A C     1 
ATOM   1064 O  O     . ALA A 1 160 ? -26.371 -6.973  29.204  1.00 9.21  ? 140 ALA A O     1 
ATOM   1065 C  CB    . ALA A 1 160 ? -27.372 -10.106 28.719  1.00 9.73  ? 140 ALA A CB    1 
ATOM   1066 N  N     . THR A 1 161 ? -27.385 -7.861  31.003  1.00 10.09 ? 141 THR A N     1 
ATOM   1067 C  CA    . THR A 1 161 ? -27.826 -6.574  31.521  1.00 11.09 ? 141 THR A CA    1 
ATOM   1068 C  C     . THR A 1 161 ? -26.640 -5.648  31.731  1.00 9.62  ? 141 THR A C     1 
ATOM   1069 O  O     . THR A 1 161 ? -26.671 -4.479  31.355  1.00 10.19 ? 141 THR A O     1 
ATOM   1070 C  CB    . THR A 1 161 ? -28.628 -6.748  32.813  1.00 13.13 ? 141 THR A CB    1 
ATOM   1071 O  OG1   . THR A 1 161 ? -29.766 -7.482  32.334  1.00 15.99 ? 141 THR A OG1   1 
ATOM   1072 C  CG2   . THR A 1 161 ? -29.013 -5.443  33.461  1.00 16.61 ? 141 THR A CG2   1 
ATOM   1073 N  N     . VAL A 1 162 ? -25.631 -6.163  32.406  1.00 9.15  ? 142 VAL A N     1 
ATOM   1074 C  CA    . VAL A 1 162 ? -24.544 -5.303  32.830  1.00 8.53  ? 142 VAL A CA    1 
ATOM   1075 C  C     . VAL A 1 162 ? -23.568 -5.058  31.676  1.00 7.18  ? 142 VAL A C     1 
ATOM   1076 O  O     . VAL A 1 162 ? -22.932 -4.015  31.663  1.00 6.89  ? 142 VAL A O     1 
ATOM   1077 C  CB    . VAL A 1 162 ? -23.845 -5.789  34.112  1.00 10.55 ? 142 VAL A CB    1 
ATOM   1078 C  CG1   . VAL A 1 162 ? -24.819 -5.845  35.286  1.00 11.72 ? 142 VAL A CG1   1 
ATOM   1079 C  CG2   . VAL A 1 162 ? -23.138 -7.106  33.935  1.00 11.52 ? 142 VAL A CG2   1 
ATOM   1080 N  N     . PHE A 1 163 ? -23.584 -5.928  30.678  1.00 7.32  ? 143 PHE A N     1 
ATOM   1081 C  CA    . PHE A 1 163 ? -22.874 -5.626  29.441  1.00 6.49  ? 143 PHE A CA    1 
ATOM   1082 C  C     . PHE A 1 163 ? -23.486 -4.408  28.778  1.00 6.97  ? 143 PHE A C     1 
ATOM   1083 O  O     . PHE A 1 163 ? -22.823 -3.494  28.294  1.00 6.02  ? 143 PHE A O     1 
ATOM   1084 C  CB    . PHE A 1 163 ? -22.842 -6.805  28.487  1.00 6.36  ? 143 PHE A CB    1 
ATOM   1085 C  CG    . PHE A 1 163 ? -22.309 -6.433  27.138  1.00 6.46  ? 143 PHE A CG    1 
ATOM   1086 C  CD1   . PHE A 1 163 ? -20.953 -6.124  26.973  1.00 7.11  ? 143 PHE A CD1   1 
ATOM   1087 C  CD2   . PHE A 1 163 ? -23.118 -6.337  26.031  1.00 6.92  ? 143 PHE A CD2   1 
ATOM   1088 C  CE1   . PHE A 1 163 ? -20.493 -5.671  25.762  1.00 6.56  ? 143 PHE A CE1   1 
ATOM   1089 C  CE2   . PHE A 1 163 ? -22.618 -5.980  24.792  1.00 7.25  ? 143 PHE A CE2   1 
ATOM   1090 C  CZ    . PHE A 1 163 ? -21.289 -5.655  24.639  1.00 7.23  ? 143 PHE A CZ    1 
ATOM   1091 N  N     . ALA A 1 164 ? -24.832 -4.331  28.727  1.00 7.58  ? 144 ALA A N     1 
ATOM   1092 C  CA    . ALA A 1 164 ? -25.470 -3.185  28.111  1.00 7.85  ? 144 ALA A CA    1 
ATOM   1093 C  C     . ALA A 1 164 ? -25.165 -1.885  28.880  1.00 7.22  ? 144 ALA A C     1 
ATOM   1094 O  O     . ALA A 1 164 ? -25.087 -0.821  28.289  1.00 7.37  ? 144 ALA A O     1 
ATOM   1095 C  CB    . ALA A 1 164 ? -26.973 -3.458  27.988  1.00 8.30  ? 144 ALA A CB    1 
ATOM   1096 N  N     . GLU A 1 165 ? -25.016 -1.967  30.203  1.00 7.52  ? 145 GLU A N     1 
ATOM   1097 C  CA    . GLU A 1 165 ? -24.685 -0.831  31.054  1.00 7.75  ? 145 GLU A CA    1 
ATOM   1098 C  C     . GLU A 1 165 ? -23.280 -0.352  30.694  1.00 7.84  ? 145 GLU A C     1 
ATOM   1099 O  O     . GLU A 1 165 ? -23.041 0.860   30.602  1.00 7.94  ? 145 GLU A O     1 
ATOM   1100 C  CB    . GLU A 1 165 ? -24.804 -1.168  32.520  1.00 9.09  ? 145 GLU A CB    1 
ATOM   1101 C  CG    . GLU A 1 165 ? -26.229 -1.423  32.979  1.00 9.78  ? 145 GLU A CG    1 
ATOM   1102 C  CD    . GLU A 1 165 ? -26.337 -1.936  34.388  1.00 13.99 ? 145 GLU A CD    1 
ATOM   1103 O  OE1   . GLU A 1 165 ? -25.303 -2.121  35.044  1.00 14.28 ? 145 GLU A OE1   1 
ATOM   1104 O  OE2   . GLU A 1 165 ? -27.531 -2.190  34.807  1.00 15.80 ? 145 GLU A OE2   1 
ATOM   1105 N  N     . TYR A 1 166 ? -22.366 -1.308  30.584  1.00 7.31  ? 146 TYR A N     1 
ATOM   1106 C  CA    . TYR A 1 166 ? -20.992 -0.979  30.165  1.00 7.21  ? 146 TYR A CA    1 
ATOM   1107 C  C     . TYR A 1 166 ? -20.990 -0.263  28.812  1.00 7.10  ? 146 TYR A C     1 
ATOM   1108 O  O     . TYR A 1 166 ? -20.302 0.730   28.587  1.00 6.72  ? 146 TYR A O     1 
ATOM   1109 C  CB    . TYR A 1 166 ? -20.180 -2.269  30.173  1.00 6.74  ? 146 TYR A CB    1 
ATOM   1110 C  CG    . TYR A 1 166 ? -18.972 -2.306  29.264  1.00 6.16  ? 146 TYR A CG    1 
ATOM   1111 C  CD1   . TYR A 1 166 ? -17.884 -1.504  29.503  1.00 6.36  ? 146 TYR A CD1   1 
ATOM   1112 C  CD2   . TYR A 1 166 ? -18.928 -3.183  28.186  1.00 5.90  ? 146 TYR A CD2   1 
ATOM   1113 C  CE1   . TYR A 1 166 ? -16.764 -1.564  28.703  1.00 5.33  ? 146 TYR A CE1   1 
ATOM   1114 C  CE2   . TYR A 1 166 ? -17.817 -3.229  27.359  1.00 5.80  ? 146 TYR A CE2   1 
ATOM   1115 C  CZ    . TYR A 1 166 ? -16.718 -2.447  27.650  1.00 6.21  ? 146 TYR A CZ    1 
ATOM   1116 O  OH    . TYR A 1 166 ? -15.582 -2.483  26.832  1.00 6.31  ? 146 TYR A OH    1 
ATOM   1117 N  N     . ALA A 1 167 ? -21.780 -0.764  27.852  1.00 6.73  ? 147 ALA A N     1 
ATOM   1118 C  CA    . ALA A 1 167 ? -21.888 -0.161  26.530  1.00 6.48  ? 147 ALA A CA    1 
ATOM   1119 C  C     . ALA A 1 167 ? -22.349 1.289   26.613  1.00 7.00  ? 147 ALA A C     1 
ATOM   1120 O  O     . ALA A 1 167 ? -21.782 2.177   25.994  1.00 7.09  ? 147 ALA A O     1 
ATOM   1121 C  CB    . ALA A 1 167 ? -22.773 -1.023  25.666  1.00 6.62  ? 147 ALA A CB    1 
ATOM   1122 N  N     . ASP A 1 168 ? -23.367 1.533   27.435  1.00 7.29  ? 148 ASP A N     1 
ATOM   1123 C  CA    . ASP A 1 168 ? -23.876 2.870   27.696  1.00 8.81  ? 148 ASP A CA    1 
ATOM   1124 C  C     . ASP A 1 168 ? -22.761 3.785   28.200  1.00 8.34  ? 148 ASP A C     1 
ATOM   1125 O  O     . ASP A 1 168 ? -22.552 4.859   27.648  1.00 9.07  ? 148 ASP A O     1 
ATOM   1126 C  CB    . ASP A 1 168 ? -25.060 2.697   28.665  1.00 9.95  ? 148 ASP A CB    1 
ATOM   1127 C  CG    . ASP A 1 168 ? -25.617 3.932   29.345  1.00 13.36 ? 148 ASP A CG    1 
ATOM   1128 O  OD1   . ASP A 1 168 ? -24.831 4.827   29.764  1.00 15.68 ? 148 ASP A OD1   1 
ATOM   1129 O  OD2   . ASP A 1 168 ? -26.874 3.913   29.599  1.00 18.20 ? 148 ASP A OD2   1 
ATOM   1130 N  N     . ILE A 1 169 ? -22.017 3.340   29.212  1.00 8.49  ? 149 ILE A N     1 
ATOM   1131 C  CA    . ILE A 1 169 ? -20.959 4.098   29.859  1.00 7.76  ? 149 ILE A CA    1 
ATOM   1132 C  C     . ILE A 1 169 ? -19.913 4.536   28.829  1.00 6.84  ? 149 ILE A C     1 
ATOM   1133 O  O     . ILE A 1 169 ? -19.533 5.701   28.764  1.00 6.83  ? 149 ILE A O     1 
ATOM   1134 C  CB    . ILE A 1 169 ? -20.326 3.280   31.005  1.00 7.85  ? 149 ILE A CB    1 
ATOM   1135 C  CG1   . ILE A 1 169 ? -21.249 3.148   32.220  1.00 9.02  ? 149 ILE A CG1   1 
ATOM   1136 C  CG2   . ILE A 1 169 ? -19.000 3.873   31.457  1.00 8.37  ? 149 ILE A CG2   1 
ATOM   1137 C  CD1   . ILE A 1 169 ? -20.991 1.961   33.089  1.00 10.46 ? 149 ILE A CD1   1 
ATOM   1138 N  N     . VAL A 1 170 ? -19.503 3.598   27.981  1.00 6.96  ? 150 VAL A N     1 
ATOM   1139 C  CA    . VAL A 1 170 ? -18.443 3.931   27.031  1.00 6.70  ? 150 VAL A CA    1 
ATOM   1140 C  C     . VAL A 1 170 ? -18.953 4.871   25.939  1.00 7.09  ? 150 VAL A C     1 
ATOM   1141 O  O     . VAL A 1 170 ? -18.257 5.807   25.587  1.00 7.55  ? 150 VAL A O     1 
ATOM   1142 C  CB    . VAL A 1 170 ? -17.846 2.632   26.433  1.00 6.74  ? 150 VAL A CB    1 
ATOM   1143 C  CG1   . VAL A 1 170 ? -16.762 2.917   25.417  1.00 7.56  ? 150 VAL A CG1   1 
ATOM   1144 C  CG2   . VAL A 1 170 ? -17.301 1.724   27.523  1.00 6.58  ? 150 VAL A CG2   1 
ATOM   1145 N  N     . VAL A 1 171 ? -20.163 4.638   25.369  1.00 7.69  ? 151 VAL A N     1 
ATOM   1146 C  CA    . VAL A 1 171 ? -20.666 5.500   24.318  1.00 9.28  ? 151 VAL A CA    1 
ATOM   1147 C  C     . VAL A 1 171 ? -20.906 6.910   24.844  1.00 8.96  ? 151 VAL A C     1 
ATOM   1148 O  O     . VAL A 1 171 ? -20.717 7.886   24.114  1.00 8.24  ? 151 VAL A O     1 
ATOM   1149 C  CB    . VAL A 1 171 ? -21.931 4.883   23.692  1.00 10.72 ? 151 VAL A CB    1 
ATOM   1150 C  CG1   . VAL A 1 171 ? -22.768 5.934   22.939  1.00 14.70 ? 151 VAL A CG1   1 
ATOM   1151 C  CG2   . VAL A 1 171 ? -21.529 3.663   22.864  1.00 10.91 ? 151 VAL A CG2   1 
ATOM   1152 N  N     . ARG A 1 172 ? -21.303 7.050   26.106  1.00 9.09  ? 152 ARG A N     1 
ATOM   1153 C  CA    . ARG A 1 172 ? -21.510 8.387   26.640  1.00 12.43 ? 152 ARG A CA    1 
ATOM   1154 C  C     . ARG A 1 172 ? -20.241 9.214   26.616  1.00 13.57 ? 152 ARG A C     1 
ATOM   1155 O  O     . ARG A 1 172 ? -20.304 10.434  26.440  1.00 14.73 ? 152 ARG A O     1 
ATOM   1156 C  CB    . ARG A 1 172 ? -22.015 8.325   28.074  1.00 14.70 ? 152 ARG A CB    1 
ATOM   1157 C  CG    . ARG A 1 172 ? -23.490 8.031   28.119  1.00 17.61 ? 152 ARG A CG    1 
ATOM   1158 C  CD    . ARG A 1 172 ? -23.939 8.231   29.543  1.00 18.24 ? 152 ARG A CD    1 
ATOM   1159 N  NE    . ARG A 1 172 ? -25.219 7.604   29.691  1.00 20.89 ? 152 ARG A NE    1 
ATOM   1160 C  CZ    . ARG A 1 172 ? -26.378 8.167   29.399  1.00 25.98 ? 152 ARG A CZ    1 
ATOM   1161 N  NH1   . ARG A 1 172 ? -26.427 9.444   29.043  1.00 27.24 ? 152 ARG A NH1   1 
ATOM   1162 N  NH2   . ARG A 1 172 ? -27.479 7.453   29.499  1.00 28.21 ? 152 ARG A NH2   1 
ATOM   1163 N  N     . GLN A 1 173 ? -19.104 8.549   26.787  1.00 11.53 ? 153 GLN A N     1 
ATOM   1164 C  CA    . GLN A 1 173 ? -17.842 9.271   26.872  1.00 12.75 ? 153 GLN A CA    1 
ATOM   1165 C  C     . GLN A 1 173 ? -17.160 9.424   25.526  1.00 10.51 ? 153 GLN A C     1 
ATOM   1166 O  O     . GLN A 1 173 ? -16.582 10.481  25.265  1.00 10.76 ? 153 GLN A O     1 
ATOM   1167 C  CB    . GLN A 1 173 ? -16.962 8.595   27.905  1.00 16.25 ? 153 GLN A CB    1 
ATOM   1168 C  CG    . GLN A 1 173 ? -17.653 8.713   29.251  1.00 21.70 ? 153 GLN A CG    1 
ATOM   1169 C  CD    . GLN A 1 173 ? -16.726 9.139   30.357  1.00 24.65 ? 153 GLN A CD    1 
ATOM   1170 O  OE1   . GLN A 1 173 ? -15.611 9.561   30.079  1.00 20.20 ? 153 GLN A OE1   1 
ATOM   1171 N  NE2   . GLN A 1 173 ? -17.180 8.973   31.603  1.00 28.56 ? 153 GLN A NE2   1 
ATOM   1172 N  N     . LEU A 1 174 ? -17.220 8.407   24.673  1.00 8.44  ? 154 LEU A N     1 
ATOM   1173 C  CA    . LEU A 1 174 ? -16.491 8.436   23.417  1.00 8.48  ? 154 LEU A CA    1 
ATOM   1174 C  C     . LEU A 1 174 ? -17.358 8.628   22.172  1.00 9.01  ? 154 LEU A C     1 
ATOM   1175 O  O     . LEU A 1 174 ? -16.822 8.819   21.091  1.00 8.91  ? 154 LEU A O     1 
ATOM   1176 C  CB    . LEU A 1 174 ? -15.735 7.116   23.258  1.00 8.98  ? 154 LEU A CB    1 
ATOM   1177 C  CG    . LEU A 1 174 ? -14.746 6.761   24.358  1.00 11.34 ? 154 LEU A CG    1 
ATOM   1178 C  CD1   . LEU A 1 174 ? -14.056 5.458   23.992  1.00 12.95 ? 154 LEU A CD1   1 
ATOM   1179 C  CD2   . LEU A 1 174 ? -13.731 7.851   24.599  1.00 13.83 ? 154 LEU A CD2   1 
ATOM   1180 N  N     . GLY A 1 175 ? -18.687 8.535   22.323  1.00 9.04  ? 155 GLY A N     1 
ATOM   1181 C  CA    . GLY A 1 175 ? -19.597 8.579   21.185  1.00 8.82  ? 155 GLY A CA    1 
ATOM   1182 C  C     . GLY A 1 175 ? -19.756 9.931   20.493  1.00 9.82  ? 155 GLY A C     1 
ATOM   1183 O  O     . GLY A 1 175 ? -20.347 10.006  19.409  1.00 11.06 ? 155 GLY A O     1 
ATOM   1184 N  N     . ASP A 1 176 ? -19.118 10.955  21.044  1.00 9.41  ? 156 ASP A N     1 
ATOM   1185 C  CA    . ASP A 1 176 ? -19.044 12.235  20.362  1.00 10.91 ? 156 ASP A CA    1 
ATOM   1186 C  C     . ASP A 1 176 ? -17.988 12.215  19.268  1.00 10.66 ? 156 ASP A C     1 
ATOM   1187 O  O     . ASP A 1 176 ? -18.004 13.096  18.391  1.00 12.58 ? 156 ASP A O     1 
ATOM   1188 C  CB    . ASP A 1 176 ? -18.723 13.358  21.347  1.00 12.67 ? 156 ASP A CB    1 
ATOM   1189 C  CG    . ASP A 1 176 ? -17.443 13.225  22.160  1.00 15.14 ? 156 ASP A CG    1 
ATOM   1190 O  OD1   . ASP A 1 176 ? -16.941 12.078  22.349  1.00 13.90 ? 156 ASP A OD1   1 
ATOM   1191 O  OD2   . ASP A 1 176 ? -16.917 14.282  22.574  1.00 21.10 ? 156 ASP A OD2   1 
ATOM   1192 N  N     . ARG A 1 177 ? -17.103 11.214  19.311  1.00 8.66  ? 157 ARG A N     1 
ATOM   1193 C  CA    . ARG A 1 177 ? -15.965 11.097  18.411  1.00 8.21  ? 157 ARG A CA    1 
ATOM   1194 C  C     . ARG A 1 177 ? -15.959 9.815   17.591  1.00 8.62  ? 157 ARG A C     1 
ATOM   1195 O  O     . ARG A 1 177 ? -15.449 9.818   16.456  1.00 11.69 ? 157 ARG A O     1 
ATOM   1196 C  CB    . ARG A 1 177 ? -14.657 11.214  19.196  1.00 8.77  ? 157 ARG A CB    1 
ATOM   1197 C  CG    . ARG A 1 177 ? -14.396 12.651  19.608  1.00 9.07  ? 157 ARG A CG    1 
ATOM   1198 C  CD    . ARG A 1 177 ? -13.452 12.745  20.769  1.00 9.75  ? 157 ARG A CD    1 
ATOM   1199 N  NE    . ARG A 1 177 ? -14.034 12.200  21.983  1.00 10.15 ? 157 ARG A NE    1 
ATOM   1200 C  CZ    . ARG A 1 177 ? -13.368 11.815  23.051  1.00 10.90 ? 157 ARG A CZ    1 
ATOM   1201 N  NH1   . ARG A 1 177 ? -14.026 11.419  24.108  1.00 11.97 ? 157 ARG A NH1   1 
ATOM   1202 N  NH2   . ARG A 1 177 ? -12.053 11.882  23.089  1.00 11.17 ? 157 ARG A NH2   1 
ATOM   1203 N  N     . VAL A 1 178 ? -16.506 8.733   18.139  1.00 7.58  ? 158 VAL A N     1 
ATOM   1204 C  CA    . VAL A 1 178 ? -16.527 7.445   17.485  1.00 7.36  ? 158 VAL A CA    1 
ATOM   1205 C  C     . VAL A 1 178 ? -17.942 7.240   16.972  1.00 8.56  ? 158 VAL A C     1 
ATOM   1206 O  O     . VAL A 1 178 ? -18.836 7.175   17.792  1.00 8.82  ? 158 VAL A O     1 
ATOM   1207 C  CB    . VAL A 1 178 ? -16.139 6.341   18.480  1.00 6.71  ? 158 VAL A CB    1 
ATOM   1208 C  CG1   . VAL A 1 178 ? -16.202 4.969   17.849  1.00 6.32  ? 158 VAL A CG1   1 
ATOM   1209 C  CG2   . VAL A 1 178 ? -14.749 6.580   19.085  1.00 7.16  ? 158 VAL A CG2   1 
ATOM   1210 N  N     . THR A 1 179 ? -18.074 7.055   15.659  1.00 9.09  ? 159 THR A N     1 
ATOM   1211 C  CA    . THR A 1 179 ? -19.384 6.733   15.092  1.00 9.33  ? 159 THR A CA    1 
ATOM   1212 C  C     . THR A 1 179 ? -19.582 5.223   14.944  1.00 9.91  ? 159 THR A C     1 
ATOM   1213 O  O     . THR A 1 179 ? -20.720 4.728   15.018  1.00 9.44  ? 159 THR A O     1 
ATOM   1214 C  CB    . THR A 1 179 ? -19.539 7.398   13.727  1.00 10.34 ? 159 THR A CB    1 
ATOM   1215 O  OG1   . THR A 1 179 ? -18.406 7.109   12.911  1.00 11.32 ? 159 THR A OG1   1 
ATOM   1216 C  CG2   . THR A 1 179 ? -19.641 8.895   13.901  1.00 13.34 ? 159 THR A CG2   1 
ATOM   1217 N  N     . HIS A 1 180 ? -18.513 4.476   14.705  1.00 8.27  ? 160 HIS A N     1 
ATOM   1218 C  CA    . HIS A 1 180 ? -18.635 3.073   14.300  1.00 8.26  ? 160 HIS A CA    1 
ATOM   1219 C  C     . HIS A 1 180 ? -18.233 2.168   15.453  1.00 8.08  ? 160 HIS A C     1 
ATOM   1220 O  O     . HIS A 1 180 ? -17.084 2.133   15.889  1.00 8.18  ? 160 HIS A O     1 
ATOM   1221 C  CB    . HIS A 1 180 ? -17.807 2.721   13.058  1.00 9.69  ? 160 HIS A CB    1 
ATOM   1222 C  CG    . HIS A 1 180 ? -18.471 3.206   11.807  1.00 11.02 ? 160 HIS A CG    1 
ATOM   1223 N  ND1   . HIS A 1 180 ? -18.709 4.556   11.667  1.00 13.70 ? 160 HIS A ND1   1 
ATOM   1224 C  CD2   . HIS A 1 180 ? -19.028 2.605   10.728  1.00 13.28 ? 160 HIS A CD2   1 
ATOM   1225 C  CE1   . HIS A 1 180 ? -19.372 4.756   10.526  1.00 15.01 ? 160 HIS A CE1   1 
ATOM   1226 N  NE2   . HIS A 1 180 ? -19.519 3.608   9.902   1.00 13.96 ? 160 HIS A NE2   1 
ATOM   1227 N  N     . TRP A 1 181 ? -19.240 1.439   15.940  1.00 7.22  ? 161 TRP A N     1 
ATOM   1228 C  CA    . TRP A 1 181 ? -19.130 0.565   17.088  1.00 7.15  ? 161 TRP A CA    1 
ATOM   1229 C  C     . TRP A 1 181 ? -19.564 -0.851  16.743  1.00 7.84  ? 161 TRP A C     1 
ATOM   1230 O  O     . TRP A 1 181 ? -20.606 -1.048  16.111  1.00 8.42  ? 161 TRP A O     1 
ATOM   1231 C  CB    . TRP A 1 181 ? -20.002 1.056   18.238  1.00 7.59  ? 161 TRP A CB    1 
ATOM   1232 C  CG    . TRP A 1 181 ? -19.703 2.439   18.727  1.00 7.68  ? 161 TRP A CG    1 
ATOM   1233 C  CD1   . TRP A 1 181 ? -20.063 3.641   18.188  1.00 7.63  ? 161 TRP A CD1   1 
ATOM   1234 C  CD2   . TRP A 1 181 ? -18.949 2.745   19.913  1.00 8.45  ? 161 TRP A CD2   1 
ATOM   1235 N  NE1   . TRP A 1 181 ? -19.599 4.661   18.986  1.00 8.16  ? 161 TRP A NE1   1 
ATOM   1236 C  CE2   . TRP A 1 181 ? -18.852 4.144   20.004  1.00 8.51  ? 161 TRP A CE2   1 
ATOM   1237 C  CE3   . TRP A 1 181 ? -18.250 1.957   20.812  1.00 9.99  ? 161 TRP A CE3   1 
ATOM   1238 C  CZ2   . TRP A 1 181 ? -18.150 4.761   21.044  1.00 9.66  ? 161 TRP A CZ2   1 
ATOM   1239 C  CZ3   . TRP A 1 181 ? -17.549 2.559   21.835  1.00 11.70 ? 161 TRP A CZ3   1 
ATOM   1240 C  CH2   . TRP A 1 181 ? -17.485 3.956   21.934  1.00 11.64 ? 161 TRP A CH2   1 
ATOM   1241 N  N     . ALA A 1 182 ? -18.888 -1.828  17.330  1.00 6.84  ? 162 ALA A N     1 
ATOM   1242 C  CA    . ALA A 1 182 ? -19.413 -3.183  17.394  1.00 7.53  ? 162 ALA A CA    1 
ATOM   1243 C  C     . ALA A 1 182 ? -19.648 -3.567  18.844  1.00 7.01  ? 162 ALA A C     1 
ATOM   1244 O  O     . ALA A 1 182 ? -18.837 -3.271  19.712  1.00 6.85  ? 162 ALA A O     1 
ATOM   1245 C  CB    . ALA A 1 182 ? -18.472 -4.151  16.740  1.00 8.12  ? 162 ALA A CB    1 
ATOM   1246 N  N     . THR A 1 183 ? -20.763 -4.239  19.118  1.00 6.13  ? 163 THR A N     1 
ATOM   1247 C  CA    . THR A 1 183 ? -21.060 -4.760  20.432  1.00 6.17  ? 163 THR A CA    1 
ATOM   1248 C  C     . THR A 1 183 ? -20.084 -5.890  20.755  1.00 6.43  ? 163 THR A C     1 
ATOM   1249 O  O     . THR A 1 183 ? -19.234 -5.733  21.639  1.00 6.79  ? 163 THR A O     1 
ATOM   1250 C  CB    . THR A 1 183 ? -22.525 -5.196  20.511  1.00 6.22  ? 163 THR A CB    1 
ATOM   1251 O  OG1   . THR A 1 183 ? -22.706 -6.102  19.416  1.00 7.29  ? 163 THR A OG1   1 
ATOM   1252 C  CG2   . THR A 1 183 ? -23.407 -3.974  20.441  1.00 7.09  ? 163 THR A CG2   1 
ATOM   1253 N  N     . LEU A 1 184 ? -20.273 -7.027  20.103  1.00 6.38  ? 164 LEU A N     1 
ATOM   1254 C  CA    . LEU A 1 184 ? -19.500 -8.232  20.335  1.00 6.67  ? 164 LEU A CA    1 
ATOM   1255 C  C     . LEU A 1 184 ? -18.619 -8.548  19.149  1.00 6.92  ? 164 LEU A C     1 
ATOM   1256 O  O     . LEU A 1 184 ? -18.962 -8.302  17.991  1.00 7.26  ? 164 LEU A O     1 
ATOM   1257 C  CB    . LEU A 1 184 ? -20.401 -9.455  20.577  1.00 7.25  ? 164 LEU A CB    1 
ATOM   1258 C  CG    . LEU A 1 184 ? -21.544 -9.324  21.576  1.00 7.60  ? 164 LEU A CG    1 
ATOM   1259 C  CD1   . LEU A 1 184 ? -22.339 -10.629 21.570  1.00 8.56  ? 164 LEU A CD1   1 
ATOM   1260 C  CD2   . LEU A 1 184 ? -21.070 -8.971  22.954  1.00 8.62  ? 164 LEU A CD2   1 
ATOM   1261 N  N     . ASN A 1 185 ? -17.481 -9.177  19.476  1.00 6.27  ? 165 ASN A N     1 
ATOM   1262 C  CA    . ASN A 1 185 ? -16.642 -9.859  18.505  1.00 6.04  ? 165 ASN A CA    1 
ATOM   1263 C  C     . ASN A 1 185 ? -16.840 -11.350 18.699  1.00 6.18  ? 165 ASN A C     1 
ATOM   1264 O  O     . ASN A 1 185 ? -16.459 -11.900 19.734  1.00 6.12  ? 165 ASN A O     1 
ATOM   1265 C  CB    . ASN A 1 185 ? -15.165 -9.468  18.686  1.00 6.12  ? 165 ASN A CB    1 
ATOM   1266 C  CG    . ASN A 1 185 ? -14.275 -10.141 17.680  1.00 6.48  ? 165 ASN A CG    1 
ATOM   1267 O  OD1   . ASN A 1 185 ? -14.206 -9.689  16.543  1.00 6.34  ? 165 ASN A OD1   1 
ATOM   1268 N  ND2   . ASN A 1 185 ? -13.648 -11.232 18.077  1.00 7.59  ? 165 ASN A ND2   1 
ATOM   1269 N  N     . GLU A 1 186 ? -17.381 -12.019 17.660  1.00 6.53  ? 166 GLU A N     1 
ATOM   1270 C  CA    . GLU A 1 186 ? -17.329 -13.477 17.575  1.00 6.91  ? 166 GLU A CA    1 
ATOM   1271 C  C     . GLU A 1 186 ? -17.961 -14.162 18.777  1.00 7.02  ? 166 GLU A C     1 
ATOM   1272 O  O     . GLU A 1 186 ? -17.334 -14.925 19.480  1.00 5.96  ? 166 GLU A O     1 
ATOM   1273 C  CB    . GLU A 1 186 ? -15.936 -14.017 17.357  1.00 7.42  ? 166 GLU A CB    1 
ATOM   1274 C  CG    . GLU A 1 186 ? -15.269 -13.431 16.158  1.00 8.62  ? 166 GLU A CG    1 
ATOM   1275 C  CD    . GLU A 1 186 ? -13.865 -13.974 16.046  1.00 11.21 ? 166 GLU A CD    1 
ATOM   1276 O  OE1   . GLU A 1 186 ? -13.694 -15.206 16.057  1.00 14.69 ? 166 GLU A OE1   1 
ATOM   1277 O  OE2   . GLU A 1 186 ? -12.951 -13.165 15.986  1.00 14.99 ? 166 GLU A OE2   1 
ATOM   1278 N  N     . PRO A 1 187 ? -19.279 -14.046 18.960  1.00 6.82  ? 167 PRO A N     1 
ATOM   1279 C  CA    . PRO A 1 187 ? -19.942 -14.767 20.039  1.00 6.90  ? 167 PRO A CA    1 
ATOM   1280 C  C     . PRO A 1 187 ? -19.833 -16.283 19.950  1.00 6.22  ? 167 PRO A C     1 
ATOM   1281 O  O     . PRO A 1 187 ? -19.872 -16.941 20.977  1.00 6.11  ? 167 PRO A O     1 
ATOM   1282 C  CB    . PRO A 1 187 ? -21.396 -14.252 19.974  1.00 6.84  ? 167 PRO A CB    1 
ATOM   1283 C  CG    . PRO A 1 187 ? -21.534 -13.768 18.540  1.00 7.43  ? 167 PRO A CG    1 
ATOM   1284 C  CD    . PRO A 1 187 ? -20.169 -13.141 18.228  1.00 7.27  ? 167 PRO A CD    1 
ATOM   1285 N  N     . TRP A 1 188 ? -19.697 -16.832 18.745  1.00 6.98  ? 168 TRP A N     1 
ATOM   1286 C  CA    . TRP A 1 188 ? -19.462 -18.276 18.649  1.00 7.54  ? 168 TRP A CA    1 
ATOM   1287 C  C     . TRP A 1 188 ? -18.212 -18.663 19.427  1.00 7.15  ? 168 TRP A C     1 
ATOM   1288 O  O     . TRP A 1 188 ? -18.193 -19.682 20.116  1.00 6.84  ? 168 TRP A O     1 
ATOM   1289 C  CB    . TRP A 1 188 ? -19.284 -18.729 17.204  1.00 8.38  ? 168 TRP A CB    1 
ATOM   1290 C  CG    . TRP A 1 188 ? -19.060 -20.196 17.111  1.00 8.60  ? 168 TRP A CG    1 
ATOM   1291 C  CD1   . TRP A 1 188 ? -20.005 -21.175 16.970  1.00 8.63  ? 168 TRP A CD1   1 
ATOM   1292 C  CD2   . TRP A 1 188 ? -17.790 -20.839 16.977  1.00 7.75  ? 168 TRP A CD2   1 
ATOM   1293 N  NE1   . TRP A 1 188 ? -19.378 -22.391 16.890  1.00 9.00  ? 168 TRP A NE1   1 
ATOM   1294 C  CE2   . TRP A 1 188 ? -18.017 -22.228 16.872  1.00 8.15  ? 168 TRP A CE2   1 
ATOM   1295 C  CE3   . TRP A 1 188 ? -16.464 -20.389 17.006  1.00 8.11  ? 168 TRP A CE3   1 
ATOM   1296 C  CZ2   . TRP A 1 188 ? -16.989 -23.155 16.757  1.00 9.22  ? 168 TRP A CZ2   1 
ATOM   1297 C  CZ3   . TRP A 1 188 ? -15.445 -21.308 16.900  1.00 9.01  ? 168 TRP A CZ3   1 
ATOM   1298 C  CH2   . TRP A 1 188 ? -15.686 -22.689 16.795  1.00 9.23  ? 168 TRP A CH2   1 
ATOM   1299 N  N     . CYS A 1 189 ? -17.126 -17.903 19.261  1.00 6.90  ? 169 CYS A N     1 
ATOM   1300 C  CA    . CYS A 1 189 ? -15.919 -18.256 20.014  1.00 7.42  ? 169 CYS A CA    1 
ATOM   1301 C  C     . CYS A 1 189 ? -16.174 -18.147 21.521  1.00 6.89  ? 169 CYS A C     1 
ATOM   1302 O  O     . CYS A 1 189 ? -15.892 -19.087 22.300  1.00 7.61  ? 169 CYS A O     1 
ATOM   1303 C  CB    . CYS A 1 189 ? -14.767 -17.349 19.597  1.00 7.48  ? 169 CYS A CB    1 
ATOM   1304 S  SG    . CYS A 1 189 ? -14.080 -17.722 17.971  1.00 9.60  ? 169 CYS A SG    1 
ATOM   1305 N  N     . SER A 1 190 ? -16.719 -17.026 21.979  1.00 6.68  ? 170 SER A N     1 
ATOM   1306 C  CA    . SER A 1 190 ? -16.941 -16.829 23.406  1.00 6.37  ? 170 SER A CA    1 
ATOM   1307 C  C     . SER A 1 190 ? -17.804 -17.962 23.960  1.00 7.19  ? 170 SER A C     1 
ATOM   1308 O  O     . SER A 1 190 ? -17.529 -18.510 25.029  1.00 7.39  ? 170 SER A O     1 
ATOM   1309 C  CB    . SER A 1 190 ? -17.608 -15.519 23.707  1.00 6.73  ? 170 SER A CB    1 
ATOM   1310 O  OG    . SER A 1 190 ? -16.779 -14.406 23.366  1.00 6.46  ? 170 SER A OG    1 
ATOM   1311 N  N     . ALA A 1 191 ? -18.880 -18.297 23.248  1.00 6.40  ? 171 ALA A N     1 
ATOM   1312 C  CA    . ALA A 1 191 ? -19.797 -19.324 23.741  1.00 6.94  ? 171 ALA A CA    1 
ATOM   1313 C  C     . ALA A 1 191 ? -19.252 -20.728 23.569  1.00 6.88  ? 171 ALA A C     1 
ATOM   1314 O  O     . ALA A 1 191 ? -19.190 -21.508 24.528  1.00 7.25  ? 171 ALA A O     1 
ATOM   1315 C  CB    . ALA A 1 191 ? -21.148 -19.213 23.092  1.00 7.47  ? 171 ALA A CB    1 
ATOM   1316 N  N     . MET A 1 192 ? -18.887 -21.090 22.342  1.00 6.94  ? 172 MET A N     1 
ATOM   1317 C  CA    . MET A 1 192 ? -18.625 -22.492 22.063  1.00 8.58  ? 172 MET A CA    1 
ATOM   1318 C  C     . MET A 1 192 ? -17.184 -22.837 22.439  1.00 8.58  ? 172 MET A C     1 
ATOM   1319 O  O     . MET A 1 192 ? -16.952 -23.925 22.963  1.00 11.19 ? 172 MET A O     1 
ATOM   1320 C  CB    . MET A 1 192 ? -18.949 -22.809 20.606  1.00 9.90  ? 172 MET A CB    1 
ATOM   1321 C  CG    . MET A 1 192 ? -20.378 -22.618 20.273  1.00 12.25 ? 172 MET A CG    1 
ATOM   1322 S  SD    . MET A 1 192 ? -21.459 -23.487 21.474  1.00 19.48 ? 172 MET A SD    1 
ATOM   1323 C  CE    . MET A 1 192 ? -23.057 -23.358 20.674  1.00 25.41 ? 172 MET A CE    1 
ATOM   1324 N  N     . LEU A 1 193 ? -16.213 -21.966 22.133  1.00 7.41  ? 173 LEU A N     1 
ATOM   1325 C  CA    . LEU A 1 193 ? -14.856 -22.272 22.583  1.00 7.61  ? 173 LEU A CA    1 
ATOM   1326 C  C     . LEU A 1 193 ? -14.688 -22.025 24.086  1.00 7.14  ? 173 LEU A C     1 
ATOM   1327 O  O     . LEU A 1 193 ? -13.884 -22.716 24.744  1.00 7.27  ? 173 LEU A O     1 
ATOM   1328 C  CB    . LEU A 1 193 ? -13.828 -21.484 21.772  1.00 7.59  ? 173 LEU A CB    1 
ATOM   1329 C  CG    . LEU A 1 193 ? -13.887 -21.751 20.278  1.00 7.99  ? 173 LEU A CG    1 
ATOM   1330 C  CD1   . LEU A 1 193 ? -12.783 -20.942 19.618  1.00 8.57  ? 173 LEU A CD1   1 
ATOM   1331 C  CD2   . LEU A 1 193 ? -13.808 -23.236 19.970  1.00 9.16  ? 173 LEU A CD2   1 
ATOM   1332 N  N     . GLY A 1 194 ? -15.430 -21.060 24.662  1.00 6.37  ? 174 GLY A N     1 
ATOM   1333 C  CA    . GLY A 1 194 ? -15.234 -20.734 26.082  1.00 6.30  ? 174 GLY A CA    1 
ATOM   1334 C  C     . GLY A 1 194 ? -16.046 -21.597 27.049  1.00 6.86  ? 174 GLY A C     1 
ATOM   1335 O  O     . GLY A 1 194 ? -15.598 -21.783 28.169  1.00 7.83  ? 174 GLY A O     1 
ATOM   1336 N  N     . TYR A 1 195 ? -17.208 -22.129 26.619  1.00 7.05  ? 175 TYR A N     1 
ATOM   1337 C  CA    . TYR A 1 195 ? -18.092 -22.833 27.543  1.00 7.40  ? 175 TYR A CA    1 
ATOM   1338 C  C     . TYR A 1 195 ? -18.418 -24.261 27.105  1.00 8.06  ? 175 TYR A C     1 
ATOM   1339 O  O     . TYR A 1 195 ? -18.852 -25.027 27.984  1.00 8.75  ? 175 TYR A O     1 
ATOM   1340 C  CB    . TYR A 1 195 ? -19.411 -22.074 27.766  1.00 7.20  ? 175 TYR A CB    1 
ATOM   1341 C  CG    . TYR A 1 195 ? -19.274 -20.783 28.529  1.00 7.27  ? 175 TYR A CG    1 
ATOM   1342 C  CD1   . TYR A 1 195 ? -18.893 -19.598 27.899  1.00 6.81  ? 175 TYR A CD1   1 
ATOM   1343 C  CD2   . TYR A 1 195 ? -19.489 -20.698 29.900  1.00 8.03  ? 175 TYR A CD2   1 
ATOM   1344 C  CE1   . TYR A 1 195 ? -18.783 -18.390 28.577  1.00 7.43  ? 175 TYR A CE1   1 
ATOM   1345 C  CE2   . TYR A 1 195 ? -19.351 -19.512 30.590  1.00 8.73  ? 175 TYR A CE2   1 
ATOM   1346 C  CZ    . TYR A 1 195 ? -18.983 -18.329 29.938  1.00 7.66  ? 175 TYR A CZ    1 
ATOM   1347 O  OH    . TYR A 1 195 ? -18.883 -17.154 30.662  1.00 8.61  ? 175 TYR A OH    1 
ATOM   1348 N  N     . TYR A 1 196 ? -18.249 -24.618 25.826  1.00 8.28  ? 176 TYR A N     1 
ATOM   1349 C  CA    . TYR A 1 196 ? -18.535 -25.973 25.356  1.00 9.29  ? 176 TYR A CA    1 
ATOM   1350 C  C     . TYR A 1 196 ? -17.265 -26.783 25.152  1.00 10.06 ? 176 TYR A C     1 
ATOM   1351 O  O     . TYR A 1 196 ? -17.079 -27.867 25.726  1.00 12.12 ? 176 TYR A O     1 
ATOM   1352 C  CB    . TYR A 1 196 ? -19.378 -25.896 24.092  1.00 9.20  ? 176 TYR A CB    1 
ATOM   1353 C  CG    . TYR A 1 196 ? -19.572 -27.204 23.356  1.00 10.10 ? 176 TYR A CG    1 
ATOM   1354 C  CD1   . TYR A 1 196 ? -19.829 -28.375 24.040  1.00 12.15 ? 176 TYR A CD1   1 
ATOM   1355 C  CD2   . TYR A 1 196 ? -19.535 -27.239 21.983  1.00 12.95 ? 176 TYR A CD2   1 
ATOM   1356 C  CE1   . TYR A 1 196 ? -19.986 -29.571 23.354  1.00 12.38 ? 176 TYR A CE1   1 
ATOM   1357 C  CE2   . TYR A 1 196 ? -19.688 -28.425 21.277  1.00 14.48 ? 176 TYR A CE2   1 
ATOM   1358 C  CZ    . TYR A 1 196 ? -19.948 -29.598 21.974  1.00 14.62 ? 176 TYR A CZ    1 
ATOM   1359 O  OH    . TYR A 1 196 ? -20.129 -30.796 21.268  1.00 16.95 ? 176 TYR A OH    1 
ATOM   1360 N  N     . LEU A 1 197 ? -16.325 -26.263 24.364  1.00 10.26 ? 177 LEU A N     1 
ATOM   1361 C  CA    . LEU A 1 197 ? -15.109 -27.003 24.079  1.00 10.73 ? 177 LEU A CA    1 
ATOM   1362 C  C     . LEU A 1 197 ? -13.968 -26.720 25.056  1.00 12.10 ? 177 LEU A C     1 
ATOM   1363 O  O     . LEU A 1 197 ? -13.016 -27.474 25.115  1.00 12.38 ? 177 LEU A O     1 
ATOM   1364 C  CB    . LEU A 1 197 ? -14.706 -26.721 22.631  1.00 13.00 ? 177 LEU A CB    1 
ATOM   1365 C  CG    . LEU A 1 197 ? -15.722 -27.199 21.590  1.00 14.80 ? 177 LEU A CG    1 
ATOM   1366 C  CD1   . LEU A 1 197 ? -15.225 -26.895 20.196  1.00 16.40 ? 177 LEU A CD1   1 
ATOM   1367 C  CD2   . LEU A 1 197 ? -15.969 -28.692 21.715  1.00 15.53 ? 177 LEU A CD2   1 
ATOM   1368 N  N     . GLY A 1 198 ? -14.086 -25.673 25.854  1.00 10.14 ? 178 GLY A N     1 
ATOM   1369 C  CA    . GLY A 1 198 ? -13.155 -25.383 26.934  1.00 11.26 ? 178 GLY A CA    1 
ATOM   1370 C  C     . GLY A 1 198 ? -11.784 -24.902 26.473  1.00 11.47 ? 178 GLY A C     1 
ATOM   1371 O  O     . GLY A 1 198 ? -10.886 -24.880 27.303  1.00 12.62 ? 178 GLY A O     1 
ATOM   1372 N  N     . VAL A 1 199 ? -11.592 -24.503 25.212  1.00 9.05  ? 179 VAL A N     1 
ATOM   1373 C  CA    . VAL A 1 199 ? -10.238 -24.150 24.773  1.00 9.02  ? 179 VAL A CA    1 
ATOM   1374 C  C     . VAL A 1 199 ? -9.942  -22.660 24.967  1.00 8.24  ? 179 VAL A C     1 
ATOM   1375 O  O     . VAL A 1 199 ? -8.777  -22.283 24.982  1.00 8.69  ? 179 VAL A O     1 
ATOM   1376 C  CB    . VAL A 1 199 ? -9.978  -24.587 23.328  1.00 11.21 ? 179 VAL A CB    1 
ATOM   1377 C  CG1   . VAL A 1 199 ? -10.082 -26.096 23.194  1.00 14.24 ? 179 VAL A CG1   1 
ATOM   1378 C  CG2   . VAL A 1 199 ? -10.867 -23.887 22.352  1.00 11.95 ? 179 VAL A CG2   1 
ATOM   1379 N  N     . HIS A 1 200 ? -10.983 -21.843 25.160  1.00 6.92  ? 180 HIS A N     1 
ATOM   1380 C  CA    . HIS A 1 200 ? -10.886 -20.415 25.463  1.00 6.92  ? 180 HIS A CA    1 
ATOM   1381 C  C     . HIS A 1 200 ? -11.454 -20.141 26.853  1.00 6.52  ? 180 HIS A C     1 
ATOM   1382 O  O     . HIS A 1 200 ? -12.186 -20.954 27.406  1.00 6.11  ? 180 HIS A O     1 
ATOM   1383 C  CB    . HIS A 1 200 ? -11.664 -19.569 24.459  1.00 7.07  ? 180 HIS A CB    1 
ATOM   1384 C  CG    . HIS A 1 200 ? -10.941 -19.430 23.179  1.00 7.50  ? 180 HIS A CG    1 
ATOM   1385 N  ND1   . HIS A 1 200 ? -11.409 -18.694 22.116  1.00 8.22  ? 180 HIS A ND1   1 
ATOM   1386 C  CD2   . HIS A 1 200 ? -9.778  -20.002 22.785  1.00 7.73  ? 180 HIS A CD2   1 
ATOM   1387 C  CE1   . HIS A 1 200 ? -10.540 -18.803 21.120  1.00 8.35  ? 180 HIS A CE1   1 
ATOM   1388 N  NE2   . HIS A 1 200 ? -9.525  -19.552 21.502  1.00 7.84  ? 180 HIS A NE2   1 
ATOM   1389 N  N     . ALA A 1 201 ? -11.074 -18.988 27.421  1.00 5.37  ? 181 ALA A N     1 
ATOM   1390 C  CA    . ALA A 1 201 ? -11.641 -18.627 28.709  1.00 5.12  ? 181 ALA A CA    1 
ATOM   1391 C  C     . ALA A 1 201 ? -13.158 -18.517 28.638  1.00 5.36  ? 181 ALA A C     1 
ATOM   1392 O  O     . ALA A 1 201 ? -13.719 -18.100 27.614  1.00 5.40  ? 181 ALA A O     1 
ATOM   1393 C  CB    . ALA A 1 201 ? -11.033 -17.346 29.146  1.00 5.29  ? 181 ALA A CB    1 
ATOM   1394 N  N     . PRO A 1 202 ? -13.901 -18.928 29.684  1.00 5.72  ? 182 PRO A N     1 
ATOM   1395 C  CA    . PRO A 1 202 ? -13.369 -19.375 30.971  1.00 6.55  ? 182 PRO A CA    1 
ATOM   1396 C  C     . PRO A 1 202 ? -12.968 -20.836 31.061  1.00 7.82  ? 182 PRO A C     1 
ATOM   1397 O  O     . PRO A 1 202 ? -12.429 -21.271 32.094  1.00 9.39  ? 182 PRO A O     1 
ATOM   1398 C  CB    . PRO A 1 202 ? -14.564 -19.158 31.919  1.00 6.39  ? 182 PRO A CB    1 
ATOM   1399 C  CG    . PRO A 1 202 ? -15.748 -19.420 31.010  1.00 6.19  ? 182 PRO A CG    1 
ATOM   1400 C  CD    . PRO A 1 202 ? -15.376 -18.752 29.742  1.00 6.02  ? 182 PRO A CD    1 
ATOM   1401 N  N     . GLY A 1 203 ? -13.199 -21.627 30.001  1.00 7.91  ? 183 GLY A N     1 
ATOM   1402 C  CA    . GLY A 1 203 ? -12.691 -22.991 29.929  1.00 8.01  ? 183 GLY A CA    1 
ATOM   1403 C  C     . GLY A 1 203 ? -13.694 -24.051 30.383  1.00 9.76  ? 183 GLY A C     1 
ATOM   1404 O  O     . GLY A 1 203 ? -13.275 -25.180 30.690  1.00 11.92 ? 183 GLY A O     1 
ATOM   1405 N  N     . HIS A 1 204 ? -15.002 -23.763 30.307  1.00 9.59  ? 184 HIS A N     1 
ATOM   1406 C  CA    . HIS A 1 204 ? -16.016 -24.771 30.619  1.00 11.49 ? 184 HIS A CA    1 
ATOM   1407 C  C     . HIS A 1 204 ? -16.192 -25.734 29.443  1.00 10.22 ? 184 HIS A C     1 
ATOM   1408 O  O     . HIS A 1 204 ? -15.864 -25.431 28.292  1.00 9.28  ? 184 HIS A O     1 
ATOM   1409 C  CB    . HIS A 1 204 ? -17.360 -24.150 31.038  1.00 12.49 ? 184 HIS A CB    1 
ATOM   1410 C  CG    . HIS A 1 204 ? -17.278 -23.473 32.363  1.00 19.10 ? 184 HIS A CG    1 
ATOM   1411 N  ND1   . HIS A 1 204 ? -16.627 -24.103 33.407  1.00 27.26 ? 184 HIS A ND1   1 
ATOM   1412 C  CD2   . HIS A 1 204 ? -17.565 -22.246 32.797  1.00 22.21 ? 184 HIS A CD2   1 
ATOM   1413 C  CE1   . HIS A 1 204 ? -16.567 -23.286 34.449  1.00 27.26 ? 184 HIS A CE1   1 
ATOM   1414 N  NE2   . HIS A 1 204 ? -17.162 -22.174 34.115  1.00 26.33 ? 184 HIS A NE2   1 
ATOM   1415 N  N     . THR A 1 205 ? -16.754 -26.915 29.756  1.00 10.37 ? 185 THR A N     1 
ATOM   1416 C  CA    . THR A 1 205 ? -16.897 -27.980 28.767  1.00 11.18 ? 185 THR A CA    1 
ATOM   1417 C  C     . THR A 1 205 ? -18.291 -28.605 28.873  1.00 13.04 ? 185 THR A C     1 
ATOM   1418 O  O     . THR A 1 205 ? -18.440 -29.787 29.172  1.00 15.43 ? 185 THR A O     1 
ATOM   1419 C  CB    . THR A 1 205 ? -15.789 -29.012 28.898  1.00 13.89 ? 185 THR A CB    1 
ATOM   1420 O  OG1   . THR A 1 205 ? -15.754 -29.444 30.265  1.00 15.65 ? 185 THR A OG1   1 
ATOM   1421 C  CG2   . THR A 1 205 ? -14.426 -28.453 28.527  1.00 14.11 ? 185 THR A CG2   1 
ATOM   1422 N  N     . ASP A 1 206 ? -19.320 -27.856 28.549  1.00 11.48 ? 186 ASP A N     1 
ATOM   1423 C  CA    . ASP A 1 206 ? -20.666 -28.402 28.555  1.00 13.39 ? 186 ASP A CA    1 
ATOM   1424 C  C     . ASP A 1 206 ? -21.489 -27.744 27.447  1.00 13.43 ? 186 ASP A C     1 
ATOM   1425 O  O     . ASP A 1 206 ? -21.545 -26.506 27.359  1.00 12.88 ? 186 ASP A O     1 
ATOM   1426 C  CB    . ASP A 1 206 ? -21.310 -28.102 29.880  1.00 15.08 ? 186 ASP A CB    1 
ATOM   1427 C  CG    . ASP A 1 206 ? -22.711 -28.667 29.967  1.00 19.43 ? 186 ASP A CG    1 
ATOM   1428 O  OD1   . ASP A 1 206 ? -22.822 -29.905 30.009  1.00 22.33 ? 186 ASP A OD1   1 
ATOM   1429 O  OD2   . ASP A 1 206 ? -23.663 -27.854 30.021  1.00 19.88 ? 186 ASP A OD2   1 
ATOM   1430 N  N     . LEU A 1 207 ? -22.175 -28.566 26.642  1.00 13.36 ? 187 LEU A N     1 
ATOM   1431 C  CA    . LEU A 1 207 ? -22.931 -28.038 25.517  1.00 12.73 ? 187 LEU A CA    1 
ATOM   1432 C  C     . LEU A 1 207 ? -24.045 -27.117 25.988  1.00 13.19 ? 187 LEU A C     1 
ATOM   1433 O  O     . LEU A 1 207 ? -24.232 -26.050 25.403  1.00 12.25 ? 187 LEU A O     1 
ATOM   1434 C  CB    . LEU A 1 207 ? -23.532 -29.164 24.672  1.00 14.37 ? 187 LEU A CB    1 
ATOM   1435 C  CG    . LEU A 1 207 ? -24.515 -28.730 23.594  1.00 16.56 ? 187 LEU A CG    1 
ATOM   1436 C  CD1   . LEU A 1 207 ? -23.811 -27.991 22.466  1.00 16.92 ? 187 LEU A CD1   1 
ATOM   1437 C  CD2   . LEU A 1 207 ? -25.309 -29.937 23.093  1.00 19.68 ? 187 LEU A CD2   1 
ATOM   1438 N  N     . LYS A 1 208 ? -24.768 -27.486 27.050  1.00 13.98 ? 188 LYS A N     1 
ATOM   1439 C  CA    . LYS A 1 208 ? -25.864 -26.651 27.515  1.00 14.67 ? 188 LYS A CA    1 
ATOM   1440 C  C     . LYS A 1 208 ? -25.319 -25.292 27.984  1.00 12.48 ? 188 LYS A C     1 
ATOM   1441 O  O     . LYS A 1 208 ? -25.885 -24.265 27.678  1.00 13.58 ? 188 LYS A O     1 
ATOM   1442 C  CB    . LYS A 1 208 ? -26.660 -27.342 28.626  1.00 17.94 ? 188 LYS A CB    1 
ATOM   1443 C  CG    . LYS A 1 208 ? -27.745 -26.469 29.216  1.00 24.03 ? 188 LYS A CG    1 
ATOM   1444 C  CD    . LYS A 1 208 ? -28.704 -27.254 30.108  1.00 30.62 ? 188 LYS A CD    1 
ATOM   1445 C  CE    . LYS A 1 208 ? -30.102 -26.673 30.015  1.00 37.66 ? 188 LYS A CE    1 
ATOM   1446 N  NZ    . LYS A 1 208 ? -31.054 -27.352 30.920  1.00 40.64 ? 188 LYS A NZ    1 
ATOM   1447 N  N     . ARG A 1 209 ? -24.175 -25.280 28.655  1.00 12.76 ? 189 ARG A N     1 
ATOM   1448 C  CA    . ARG A 1 209 ? -23.573 -24.022 29.076  1.00 12.34 ? 189 ARG A CA    1 
ATOM   1449 C  C     . ARG A 1 209 ? -23.187 -23.173 27.859  1.00 10.19 ? 189 ARG A C     1 
ATOM   1450 O  O     . ARG A 1 209 ? -23.348 -21.956 27.893  1.00 9.50  ? 189 ARG A O     1 
ATOM   1451 C  CB    . ARG A 1 209 ? -22.328 -24.247 29.924  1.00 14.71 ? 189 ARG A CB    1 
ATOM   1452 C  CG    . ARG A 1 209 ? -22.603 -24.843 31.291  1.00 18.13 ? 189 ARG A CG    1 
ATOM   1453 C  CD    . ARG A 1 209 ? -21.246 -25.044 31.937  1.00 23.14 ? 189 ARG A CD    1 
ATOM   1454 N  NE    . ARG A 1 209 ? -21.222 -25.600 33.276  1.00 28.36 ? 189 ARG A NE    1 
ATOM   1455 C  CZ    . ARG A 1 209 ? -20.710 -24.942 34.309  1.00 35.73 ? 189 ARG A CZ    1 
ATOM   1456 N  NH1   . ARG A 1 209 ? -20.315 -23.681 34.158  1.00 37.88 ? 189 ARG A NH1   1 
ATOM   1457 N  NH2   . ARG A 1 209 ? -20.611 -25.545 35.483  1.00 39.96 ? 189 ARG A NH2   1 
ATOM   1458 N  N     . GLY A 1 210 ? -22.644 -23.818 26.824  1.00 9.66  ? 190 GLY A N     1 
ATOM   1459 C  CA    . GLY A 1 210 ? -22.287 -23.092 25.607  1.00 8.97  ? 190 GLY A CA    1 
ATOM   1460 C  C     . GLY A 1 210 ? -23.496 -22.466 24.933  1.00 9.35  ? 190 GLY A C     1 
ATOM   1461 O  O     . GLY A 1 210 ? -23.477 -21.315 24.492  1.00 8.27  ? 190 GLY A O     1 
ATOM   1462 N  N     . LEU A 1 211 ? -24.575 -23.235 24.837  1.00 9.44  ? 191 LEU A N     1 
ATOM   1463 C  CA    . LEU A 1 211 ? -25.768 -22.717 24.190  1.00 9.46  ? 191 LEU A CA    1 
ATOM   1464 C  C     . LEU A 1 211 ? -26.431 -21.617 24.993  1.00 9.34  ? 191 LEU A C     1 
ATOM   1465 O  O     . LEU A 1 211 ? -26.969 -20.647 24.448  1.00 10.28 ? 191 LEU A O     1 
ATOM   1466 C  CB    . LEU A 1 211 ? -26.698 -23.914 23.921  1.00 10.72 ? 191 LEU A CB    1 
ATOM   1467 C  CG    . LEU A 1 211 ? -26.229 -24.795 22.774  1.00 13.56 ? 191 LEU A CG    1 
ATOM   1468 C  CD1   . LEU A 1 211 ? -27.147 -25.980 22.620  1.00 14.44 ? 191 LEU A CD1   1 
ATOM   1469 C  CD2   . LEU A 1 211 ? -26.129 -24.075 21.451  1.00 15.53 ? 191 LEU A CD2   1 
ATOM   1470 N  N     . GLU A 1 212 ? -26.435 -21.760 26.306  1.00 9.28  ? 192 GLU A N     1 
ATOM   1471 C  CA    . GLU A 1 212 ? -26.959 -20.749 27.198  1.00 10.32 ? 192 GLU A CA    1 
ATOM   1472 C  C     . GLU A 1 212 ? -26.129 -19.477 27.065  1.00 9.57  ? 192 GLU A C     1 
ATOM   1473 O  O     . GLU A 1 212 ? -26.662 -18.392 26.939  1.00 9.95  ? 192 GLU A O     1 
ATOM   1474 C  CB    . GLU A 1 212 ? -26.920 -21.317 28.606  1.00 13.28 ? 192 GLU A CB    1 
ATOM   1475 C  CG    . GLU A 1 212 ? -27.381 -20.397 29.690  1.00 19.33 ? 192 GLU A CG    1 
ATOM   1476 C  CD    . GLU A 1 212 ? -27.237 -20.988 31.098  1.00 27.90 ? 192 GLU A CD    1 
ATOM   1477 O  OE1   . GLU A 1 212 ? -28.241 -20.890 31.839  1.00 33.21 ? 192 GLU A OE1   1 
ATOM   1478 O  OE2   . GLU A 1 212 ? -26.116 -21.542 31.469  1.00 30.21 ? 192 GLU A OE2   1 
ATOM   1479 N  N     . ALA A 1 213 ? -24.815 -19.670 27.025  1.00 7.83  ? 193 ALA A N     1 
ATOM   1480 C  CA    . ALA A 1 213 ? -23.932 -18.538 26.832  1.00 7.44  ? 193 ALA A CA    1 
ATOM   1481 C  C     . ALA A 1 213 ? -24.226 -17.839 25.518  1.00 7.25  ? 193 ALA A C     1 
ATOM   1482 O  O     . ALA A 1 213 ? -24.210 -16.614 25.452  1.00 7.48  ? 193 ALA A O     1 
ATOM   1483 C  CB    . ALA A 1 213 ? -22.474 -18.932 26.874  1.00 7.09  ? 193 ALA A CB    1 
ATOM   1484 N  N     . SER A 1 214 ? -24.460 -18.607 24.449  1.00 8.75  ? 194 SER A N     1 
ATOM   1485 C  CA    . SER A 1 214 ? -24.700 -18.022 23.140  1.00 8.39  ? 194 SER A CA    1 
ATOM   1486 C  C     . SER A 1 214 ? -25.941 -17.118 23.195  1.00 8.12  ? 194 SER A C     1 
ATOM   1487 O  O     . SER A 1 214 ? -25.969 -16.062 22.590  1.00 7.51  ? 194 SER A O     1 
ATOM   1488 C  CB    . SER A 1 214 ? -24.739 -19.078 22.064  1.00 9.81  ? 194 SER A CB    1 
ATOM   1489 O  OG    . SER A 1 214 ? -26.022 -19.707 22.059  1.00 11.05 ? 194 SER A OG    1 
ATOM   1490 N  N     . HIS A 1 215 ? -26.988 -17.564 23.902  1.00 8.10  ? 195 HIS A N     1 
ATOM   1491 C  CA    . HIS A 1 215 ? -28.197 -16.794 24.016  1.00 9.05  ? 195 HIS A CA    1 
ATOM   1492 C  C     . HIS A 1 215 ? -27.967 -15.508 24.792  1.00 8.56  ? 195 HIS A C     1 
ATOM   1493 O  O     . HIS A 1 215 ? -28.441 -14.464 24.401  1.00 8.59  ? 195 HIS A O     1 
ATOM   1494 C  CB    . HIS A 1 215 ? -29.303 -17.662 24.618  1.00 9.43  ? 195 HIS A CB    1 
ATOM   1495 C  CG    . HIS A 1 215 ? -30.607 -16.938 24.649  1.00 12.16 ? 195 HIS A CG    1 
ATOM   1496 N  ND1   . HIS A 1 215 ? -31.363 -16.702 23.519  1.00 13.79 ? 195 HIS A ND1   1 
ATOM   1497 C  CD2   . HIS A 1 215 ? -31.272 -16.409 25.694  1.00 13.31 ? 195 HIS A CD2   1 
ATOM   1498 C  CE1   . HIS A 1 215 ? -32.452 -16.030 23.897  1.00 13.95 ? 195 HIS A CE1   1 
ATOM   1499 N  NE2   . HIS A 1 215 ? -32.430 -15.835 25.207  1.00 14.59 ? 195 HIS A NE2   1 
ATOM   1500 N  N     . ASN A 1 216 ? -27.240 -15.581 25.905  1.00 8.80  ? 196 ASN A N     1 
ATOM   1501 C  CA    . ASN A 1 216 ? -27.028 -14.413 26.730  1.00 8.95  ? 196 ASN A CA    1 
ATOM   1502 C  C     . ASN A 1 216 ? -26.058 -13.412 26.084  1.00 7.77  ? 196 ASN A C     1 
ATOM   1503 O  O     . ASN A 1 216 ? -26.201 -12.207 26.278  1.00 7.95  ? 196 ASN A O     1 
ATOM   1504 C  CB    . ASN A 1 216 ? -26.566 -14.788 28.114  1.00 9.50  ? 196 ASN A CB    1 
ATOM   1505 C  CG    . ASN A 1 216 ? -27.664 -15.433 28.943  1.00 11.89 ? 196 ASN A CG    1 
ATOM   1506 O  OD1   . ASN A 1 216 ? -28.852 -15.112 28.793  1.00 12.63 ? 196 ASN A OD1   1 
ATOM   1507 N  ND2   . ASN A 1 216 ? -27.281 -16.384 29.753  1.00 12.62 ? 196 ASN A ND2   1 
ATOM   1508 N  N     . LEU A 1 217 ? -25.149 -13.903 25.253  1.00 7.80  ? 197 LEU A N     1 
ATOM   1509 C  CA    . LEU A 1 217 ? -24.309 -13.033 24.429  1.00 7.34  ? 197 LEU A CA    1 
ATOM   1510 C  C     . LEU A 1 217 ? -25.185 -12.267 23.437  1.00 7.85  ? 197 LEU A C     1 
ATOM   1511 O  O     . LEU A 1 217 ? -25.072 -11.064 23.320  1.00 7.84  ? 197 LEU A O     1 
ATOM   1512 C  CB    . LEU A 1 217 ? -23.225 -13.839 23.691  1.00 7.22  ? 197 LEU A CB    1 
ATOM   1513 C  CG    . LEU A 1 217 ? -22.048 -14.264 24.551  1.00 7.38  ? 197 LEU A CG    1 
ATOM   1514 C  CD1   . LEU A 1 217 ? -21.395 -15.518 24.008  1.00 7.44  ? 197 LEU A CD1   1 
ATOM   1515 C  CD2   . LEU A 1 217 ? -21.012 -13.139 24.640  1.00 7.50  ? 197 LEU A CD2   1 
ATOM   1516 N  N     . LEU A 1 218 ? -26.032 -13.002 22.690  1.00 8.50  ? 198 LEU A N     1 
ATOM   1517 C  CA    . LEU A 1 218 ? -26.932 -12.360 21.744  1.00 9.12  ? 198 LEU A CA    1 
ATOM   1518 C  C     . LEU A 1 218 ? -27.868 -11.390 22.441  1.00 8.47  ? 198 LEU A C     1 
ATOM   1519 O  O     . LEU A 1 218 ? -28.148 -10.301 21.886  1.00 8.28  ? 198 LEU A O     1 
ATOM   1520 C  CB    . LEU A 1 218 ? -27.696 -13.422 20.961  1.00 9.41  ? 198 LEU A CB    1 
ATOM   1521 C  CG    . LEU A 1 218 ? -26.908 -14.145 19.890  1.00 11.29 ? 198 LEU A CG    1 
ATOM   1522 C  CD1   . LEU A 1 218 ? -27.663 -15.342 19.318  1.00 12.31 ? 198 LEU A CD1   1 
ATOM   1523 C  CD2   . LEU A 1 218 ? -26.550 -13.174 18.783  1.00 13.07 ? 198 LEU A CD2   1 
ATOM   1524 N  N     . LEU A 1 219 ? -28.387 -11.752 23.618  1.00 8.77  ? 199 LEU A N     1 
ATOM   1525 C  CA    . LEU A 1 219 ? -29.255 -10.857 24.380  1.00 9.98  ? 199 LEU A CA    1 
ATOM   1526 C  C     . LEU A 1 219 ? -28.492 -9.621  24.853  1.00 9.57  ? 199 LEU A C     1 
ATOM   1527 O  O     . LEU A 1 219 ? -28.953 -8.526  24.671  1.00 10.40 ? 199 LEU A O     1 
ATOM   1528 C  CB    . LEU A 1 219 ? -29.878 -11.627 25.541  1.00 12.40 ? 199 LEU A CB    1 
ATOM   1529 C  CG    . LEU A 1 219 ? -30.800 -10.815 26.450  1.00 16.30 ? 199 LEU A CG    1 
ATOM   1530 C  CD1   . LEU A 1 219 ? -32.047 -10.346 25.719  1.00 16.97 ? 199 LEU A CD1   1 
ATOM   1531 C  CD2   . LEU A 1 219 ? -31.199 -11.666 27.661  1.00 17.94 ? 199 LEU A CD2   1 
ATOM   1532 N  N     . GLY A 1 220 ? -27.241 -9.808  25.289  1.00 9.11  ? 200 GLY A N     1 
ATOM   1533 C  CA    . GLY A 1 220 ? -26.387 -8.692  25.625  1.00 8.63  ? 200 GLY A CA    1 
ATOM   1534 C  C     . GLY A 1 220 ? -26.202 -7.740  24.458  1.00 8.11  ? 200 GLY A C     1 
ATOM   1535 O  O     . GLY A 1 220 ? -26.282 -6.538  24.633  1.00 8.45  ? 200 GLY A O     1 
ATOM   1536 N  N     . HIS A 1 221 ? -25.886 -8.275  23.283  1.00 8.03  ? 201 HIS A N     1 
ATOM   1537 C  CA    . HIS A 1 221 ? -25.830 -7.519  22.054  1.00 7.46  ? 201 HIS A CA    1 
ATOM   1538 C  C     . HIS A 1 221 ? -27.098 -6.682  21.872  1.00 8.16  ? 201 HIS A C     1 
ATOM   1539 O  O     . HIS A 1 221 ? -27.020 -5.480  21.670  1.00 8.12  ? 201 HIS A O     1 
ATOM   1540 C  CB    . HIS A 1 221 ? -25.593 -8.435  20.858  1.00 7.80  ? 201 HIS A CB    1 
ATOM   1541 C  CG    . HIS A 1 221 ? -25.957 -7.773  19.596  1.00 8.00  ? 201 HIS A CG    1 
ATOM   1542 N  ND1   . HIS A 1 221 ? -25.204 -6.817  18.952  1.00 7.30  ? 201 HIS A ND1   1 
ATOM   1543 C  CD2   . HIS A 1 221 ? -27.095 -7.935  18.841  1.00 7.68  ? 201 HIS A CD2   1 
ATOM   1544 C  CE1   . HIS A 1 221 ? -25.859 -6.438  17.846  1.00 8.44  ? 201 HIS A CE1   1 
ATOM   1545 N  NE2   . HIS A 1 221 ? -27.029 -7.139  17.769  1.00 8.00  ? 201 HIS A NE2   1 
ATOM   1546 N  N     . GLY A 1 222 ? -28.275 -7.328  21.879  1.00 9.35  ? 202 GLY A N     1 
ATOM   1547 C  CA    . GLY A 1 222 ? -29.511 -6.582  21.656  1.00 9.11  ? 202 GLY A CA    1 
ATOM   1548 C  C     . GLY A 1 222 ? -29.791 -5.494  22.691  1.00 8.74  ? 202 GLY A C     1 
ATOM   1549 O  O     . GLY A 1 222 ? -30.220 -4.369  22.364  1.00 10.54 ? 202 GLY A O     1 
ATOM   1550 N  N     . LEU A 1 223 ? -29.604 -5.823  23.959  1.00 8.04  ? 203 LEU A N     1 
ATOM   1551 C  CA    . LEU A 1 223 ? -29.778 -4.840  24.989  1.00 8.40  ? 203 LEU A CA    1 
ATOM   1552 C  C     . LEU A 1 223 ? -28.792 -3.679  24.810  1.00 8.15  ? 203 LEU A C     1 
ATOM   1553 O  O     . LEU A 1 223 ? -29.119 -2.551  25.070  1.00 8.36  ? 203 LEU A O     1 
ATOM   1554 C  CB    . LEU A 1 223 ? -29.635 -5.478  26.344  1.00 10.00 ? 203 LEU A CB    1 
ATOM   1555 C  CG    . LEU A 1 223 ? -30.700 -6.495  26.735  1.00 12.21 ? 203 LEU A CG    1 
ATOM   1556 C  CD1   . LEU A 1 223 ? -30.280 -7.097  28.056  1.00 12.76 ? 203 LEU A CD1   1 
ATOM   1557 C  CD2   . LEU A 1 223 ? -32.051 -5.793  26.822  1.00 14.62 ? 203 LEU A CD2   1 
ATOM   1558 N  N     . ALA A 1 224 ? -27.532 -3.993  24.477  1.00 7.77  ? 204 ALA A N     1 
ATOM   1559 C  CA    . ALA A 1 224 ? -26.517 -2.979  24.279  1.00 7.47  ? 204 ALA A CA    1 
ATOM   1560 C  C     . ALA A 1 224 ? -26.828 -2.047  23.128  1.00 7.73  ? 204 ALA A C     1 
ATOM   1561 O  O     . ALA A 1 224 ? -26.645 -0.855  23.276  1.00 10.24 ? 204 ALA A O     1 
ATOM   1562 C  CB    . ALA A 1 224 ? -25.167 -3.638  24.109  1.00 7.04  ? 204 ALA A CB    1 
ATOM   1563 N  N     . VAL A 1 225 ? -27.354 -2.556  22.012  1.00 8.07  ? 205 VAL A N     1 
ATOM   1564 C  CA    . VAL A 1 225 ? -27.679 -1.713  20.881  1.00 9.89  ? 205 VAL A CA    1 
ATOM   1565 C  C     . VAL A 1 225 ? -28.671 -0.652  21.360  1.00 11.20 ? 205 VAL A C     1 
ATOM   1566 O  O     . VAL A 1 225 ? -28.499 0.519   21.054  1.00 10.59 ? 205 VAL A O     1 
ATOM   1567 C  CB    . VAL A 1 225 ? -28.228 -2.532  19.698  1.00 10.51 ? 205 VAL A CB    1 
ATOM   1568 C  CG1   . VAL A 1 225 ? -28.659 -1.581  18.607  1.00 12.98 ? 205 VAL A CG1   1 
ATOM   1569 C  CG2   . VAL A 1 225 ? -27.212 -3.526  19.153  1.00 10.06 ? 205 VAL A CG2   1 
ATOM   1570 N  N     . GLN A 1 226 ? -29.727 -1.085  22.065  1.00 12.77 ? 206 GLN A N     1 
ATOM   1571 C  CA    . GLN A 1 226 ? -30.779 -0.168  22.484  1.00 14.90 ? 206 GLN A CA    1 
ATOM   1572 C  C     . GLN A 1 226 ? -30.187 0.850   23.470  1.00 13.19 ? 206 GLN A C     1 
ATOM   1573 O  O     . GLN A 1 226 ? -30.465 2.044   23.413  1.00 12.94 ? 206 GLN A O     1 
ATOM   1574 C  CB    . GLN A 1 226 ? -31.940 -0.980  23.073  1.00 20.36 ? 206 GLN A CB    1 
ATOM   1575 C  CG    . GLN A 1 226 ? -33.315 -0.527  22.597  1.00 33.95 ? 206 GLN A CG    1 
ATOM   1576 C  CD    . GLN A 1 226 ? -33.796 0.775   23.214  1.00 44.78 ? 206 GLN A CD    1 
ATOM   1577 O  OE1   . GLN A 1 226 ? -33.220 1.852   23.007  1.00 48.19 ? 206 GLN A OE1   1 
ATOM   1578 N  NE2   . GLN A 1 226 ? -34.891 0.696   23.967  1.00 41.02 ? 206 GLN A NE2   1 
ATOM   1579 N  N     . ALA A 1 227 ? -29.331 0.390   24.404  1.00 10.67 ? 207 ALA A N     1 
ATOM   1580 C  CA    . ALA A 1 227 ? -28.750 1.257   25.413  1.00 10.35 ? 207 ALA A CA    1 
ATOM   1581 C  C     . ALA A 1 227 ? -27.812 2.258   24.728  1.00 9.09  ? 207 ALA A C     1 
ATOM   1582 O  O     . ALA A 1 227 ? -27.748 3.417   25.136  1.00 9.98  ? 207 ALA A O     1 
ATOM   1583 C  CB    . ALA A 1 227 ? -28.011 0.433   26.462  1.00 10.19 ? 207 ALA A CB    1 
ATOM   1584 N  N     . MET A 1 228 ? -27.028 1.803   23.747  1.00 9.58  ? 208 MET A N     1 
ATOM   1585 C  CA    . MET A 1 228 ? -26.125 2.678   23.021  1.00 9.37  ? 208 MET A CA    1 
ATOM   1586 C  C     . MET A 1 228 ? -26.858 3.767   22.235  1.00 10.66 ? 208 MET A C     1 
ATOM   1587 O  O     . MET A 1 228 ? -26.442 4.904   22.261  1.00 12.25 ? 208 MET A O     1 
ATOM   1588 C  CB    . MET A 1 228 ? -25.223 1.865   22.086  1.00 9.40  ? 208 MET A CB    1 
ATOM   1589 C  CG    . MET A 1 228 ? -24.306 0.942   22.857  1.00 9.39  ? 208 MET A CG    1 
ATOM   1590 S  SD    . MET A 1 228 ? -23.660 -0.351  21.820  1.00 9.33  ? 208 MET A SD    1 
ATOM   1591 C  CE    . MET A 1 228 ? -22.496 0.576   20.823  1.00 12.01 ? 208 MET A CE    1 
ATOM   1592 N  N     . ARG A 1 229 ? -27.951 3.410   21.557  1.00 11.45 ? 209 ARG A N     1 
ATOM   1593 C  CA    . ARG A 1 229 ? -28.752 4.373   20.797  1.00 13.06 ? 209 ARG A CA    1 
ATOM   1594 C  C     . ARG A 1 229 ? -29.335 5.422   21.741  1.00 13.85 ? 209 ARG A C     1 
ATOM   1595 O  O     . ARG A 1 229 ? -29.415 6.604   21.355  1.00 16.71 ? 209 ARG A O     1 
ATOM   1596 C  CB    . ARG A 1 229 ? -29.794 3.623   19.948  1.00 14.04 ? 209 ARG A CB    1 
ATOM   1597 C  CG    . ARG A 1 229 ? -29.155 2.936   18.744  1.00 14.72 ? 209 ARG A CG    1 
ATOM   1598 C  CD    . ARG A 1 229 ? -29.973 2.095   17.804  1.00 15.11 ? 209 ARG A CD    1 
ATOM   1599 N  NE    . ARG A 1 229 ? -29.175 1.696   16.686  1.00 15.46 ? 209 ARG A NE    1 
ATOM   1600 C  CZ    . ARG A 1 229 ? -29.376 0.632   15.931  1.00 20.03 ? 209 ARG A CZ    1 
ATOM   1601 N  NH1   . ARG A 1 229 ? -30.398 -0.205  16.174  1.00 24.07 ? 209 ARG A NH1   1 
ATOM   1602 N  NH2   . ARG A 1 229 ? -28.548 0.425   14.924  1.00 18.82 ? 209 ARG A NH2   1 
ATOM   1603 N  N     . ALA A 1 230 ? -29.753 5.026   22.948  1.00 13.90 ? 210 ALA A N     1 
ATOM   1604 C  CA    . ALA A 1 230 ? -30.297 5.941   23.944  1.00 15.73 ? 210 ALA A CA    1 
ATOM   1605 C  C     . ALA A 1 230 ? -29.219 6.862   24.535  1.00 19.39 ? 210 ALA A C     1 
ATOM   1606 O  O     . ALA A 1 230 ? -29.475 8.039   24.813  1.00 21.83 ? 210 ALA A O     1 
ATOM   1607 C  CB    . ALA A 1 230 ? -31.009 5.120   24.986  1.00 16.09 ? 210 ALA A CB    1 
ATOM   1608 N  N     . ALA A 1 231 ? -27.998 6.339   24.758  1.00 14.81 ? 211 ALA A N     1 
ATOM   1609 C  CA    . ALA A 1 231 ? -26.942 7.059   25.453  1.00 14.95 ? 211 ALA A CA    1 
ATOM   1610 C  C     . ALA A 1 231 ? -26.146 7.938   24.486  1.00 16.78 ? 211 ALA A C     1 
ATOM   1611 O  O     . ALA A 1 231 ? -25.436 8.821   24.965  1.00 18.39 ? 211 ALA A O     1 
ATOM   1612 C  CB    . ALA A 1 231 ? -26.017 6.073   26.141  1.00 14.48 ? 211 ALA A CB    1 
ATOM   1613 N  N     . ALA A 1 232 ? -26.296 7.711   23.174  1.00 19.67 ? 212 ALA A N     1 
ATOM   1614 C  CA    . ALA A 1 232 ? -25.449 8.282   22.126  1.00 21.63 ? 212 ALA A CA    1 
ATOM   1615 C  C     . ALA A 1 232 ? -25.574 9.796   22.076  1.00 18.90 ? 212 ALA A C     1 
ATOM   1616 O  O     . ALA A 1 232 ? -26.680 10.311  21.962  1.00 16.53 ? 212 ALA A O     1 
ATOM   1617 C  CB    . ALA A 1 232 ? -25.887 7.760   20.802  1.00 21.84 ? 212 ALA A CB    1 
ATOM   1618 N  N     . PRO A 1 233 ? -24.492 10.599  22.097  1.00 18.77 ? 213 PRO A N     1 
ATOM   1619 C  CA    . PRO A 1 233 ? -24.692 12.020  21.825  1.00 19.23 ? 213 PRO A CA    1 
ATOM   1620 C  C     . PRO A 1 233 ? -24.812 12.393  20.351  1.00 22.01 ? 213 PRO A C     1 
ATOM   1621 O  O     . PRO A 1 233 ? -24.978 13.571  20.043  1.00 22.32 ? 213 PRO A O     1 
ATOM   1622 C  CB    . PRO A 1 233 ? -23.414 12.637  22.412  1.00 22.76 ? 213 PRO A CB    1 
ATOM   1623 C  CG    . PRO A 1 233 ? -22.394 11.574  22.113  1.00 18.86 ? 213 PRO A CG    1 
ATOM   1624 C  CD    . PRO A 1 233 ? -23.091 10.267  22.441  1.00 21.46 ? 213 PRO A CD    1 
ATOM   1625 N  N     . GLN A 1 234 ? -24.684 11.431  19.426  1.00 18.39 ? 214 GLN A N     1 
ATOM   1626 C  CA    . GLN A 1 234 ? -24.883 11.695  18.018  1.00 18.22 ? 214 GLN A CA    1 
ATOM   1627 C  C     . GLN A 1 234 ? -25.314 10.369  17.395  1.00 18.93 ? 214 GLN A C     1 
ATOM   1628 O  O     . GLN A 1 234 ? -25.138 9.338   18.029  1.00 16.27 ? 214 GLN A O     1 
ATOM   1629 C  CB    . GLN A 1 234 ? -23.606 12.216  17.351  1.00 21.13 ? 214 GLN A CB    1 
ATOM   1630 C  CG    . GLN A 1 234 ? -22.564 11.133  17.077  1.00 20.52 ? 214 GLN A CG    1 
ATOM   1631 C  CD    . GLN A 1 234 ? -21.350 11.637  16.340  1.00 22.58 ? 214 GLN A CD    1 
ATOM   1632 O  OE1   . GLN A 1 234 ? -21.451 12.334  15.334  1.00 24.99 ? 214 GLN A OE1   1 
ATOM   1633 N  NE2   . GLN A 1 234 ? -20.172 11.307  16.845  1.00 20.66 ? 214 GLN A NE2   1 
ATOM   1634 N  N     . PRO A 1 235 ? -25.935 10.347  16.208  1.00 21.52 ? 215 PRO A N     1 
ATOM   1635 C  CA    . PRO A 1 235 ? -26.193 9.083   15.513  1.00 20.30 ? 215 PRO A CA    1 
ATOM   1636 C  C     . PRO A 1 235 ? -24.948 8.204   15.397  1.00 15.59 ? 215 PRO A C     1 
ATOM   1637 O  O     . PRO A 1 235 ? -23.897 8.667   14.934  1.00 15.65 ? 215 PRO A O     1 
ATOM   1638 C  CB    . PRO A 1 235 ? -26.615 9.540   14.109  1.00 22.50 ? 215 PRO A CB    1 
ATOM   1639 C  CG    . PRO A 1 235 ? -27.283 10.893  14.363  1.00 24.39 ? 215 PRO A CG    1 
ATOM   1640 C  CD    . PRO A 1 235 ? -26.494 11.517  15.496  1.00 22.91 ? 215 PRO A CD    1 
ATOM   1641 N  N     . LEU A 1 236 ? -25.127 6.917   15.722  1.00 15.55 ? 216 LEU A N     1 
ATOM   1642 C  CA    . LEU A 1 236 ? -24.049 5.923   15.634  1.00 11.73 ? 216 LEU A CA    1 
ATOM   1643 C  C     . LEU A 1 236 ? -24.325 4.872   14.563  1.00 11.23 ? 216 LEU A C     1 
ATOM   1644 O  O     . LEU A 1 236 ? -25.501 4.625   14.215  1.00 12.57 ? 216 LEU A O     1 
ATOM   1645 C  CB    . LEU A 1 236 ? -23.935 5.203   16.974  1.00 11.29 ? 216 LEU A CB    1 
ATOM   1646 C  CG    . LEU A 1 236 ? -23.656 6.050   18.211  1.00 11.94 ? 216 LEU A CG    1 
ATOM   1647 C  CD1   . LEU A 1 236 ? -23.492 5.146   19.399  1.00 12.66 ? 216 LEU A CD1   1 
ATOM   1648 C  CD2   . LEU A 1 236 ? -22.435 6.943   17.988  1.00 13.52 ? 216 LEU A CD2   1 
ATOM   1649 N  N     . GLN A 1 237 ? -23.241 4.218   14.104  1.00 9.15  ? 217 GLN A N     1 
ATOM   1650 C  CA    . GLN A 1 237 ? -23.323 3.089   13.190  1.00 9.02  ? 217 GLN A CA    1 
ATOM   1651 C  C     . GLN A 1 237 ? -22.918 1.871   14.015  1.00 8.55  ? 217 GLN A C     1 
ATOM   1652 O  O     . GLN A 1 237 ? -21.730 1.663   14.213  1.00 7.89  ? 217 GLN A O     1 
ATOM   1653 C  CB    . GLN A 1 237 ? -22.435 3.271   11.957  1.00 10.34 ? 217 GLN A CB    1 
ATOM   1654 C  CG    . GLN A 1 237 ? -22.750 4.540   11.157  1.00 12.65 ? 217 GLN A CG    1 
ATOM   1655 C  CD    . GLN A 1 237 ? -24.199 4.631   10.740  1.00 14.87 ? 217 GLN A CD    1 
ATOM   1656 O  OE1   . GLN A 1 237 ? -24.754 3.735   10.107  1.00 17.69 ? 217 GLN A OE1   1 
ATOM   1657 N  NE2   . GLN A 1 237 ? -24.793 5.765   11.054  1.00 17.24 ? 217 GLN A NE2   1 
ATOM   1658 N  N     . ILE A 1 238 ? -23.903 1.130   14.520  1.00 8.64  ? 218 ILE A N     1 
ATOM   1659 C  CA    . ILE A 1 238 ? -23.669 0.022   15.431  1.00 8.37  ? 218 ILE A CA    1 
ATOM   1660 C  C     . ILE A 1 238 ? -23.821 -1.287  14.667  1.00 9.64  ? 218 ILE A C     1 
ATOM   1661 O  O     . ILE A 1 238 ? -24.837 -1.537  14.001  1.00 9.63  ? 218 ILE A O     1 
ATOM   1662 C  CB    . ILE A 1 238 ? -24.628 0.039   16.621  1.00 9.01  ? 218 ILE A CB    1 
ATOM   1663 C  CG1   . ILE A 1 238 ? -24.633 1.366   17.374  1.00 9.20  ? 218 ILE A CG1   1 
ATOM   1664 C  CG2   . ILE A 1 238 ? -24.314 -1.136  17.547  1.00 9.52  ? 218 ILE A CG2   1 
ATOM   1665 C  CD1   . ILE A 1 238 ? -25.686 1.466   18.446  1.00 9.57  ? 218 ILE A CD1   1 
ATOM   1666 N  N     . GLY A 1 239 ? -22.822 -2.150  14.850  1.00 7.46  ? 219 GLY A N     1 
ATOM   1667 C  CA    . GLY A 1 239 ? -22.895 -3.495  14.306  1.00 7.37  ? 219 GLY A CA    1 
ATOM   1668 C  C     . GLY A 1 239 ? -22.468 -4.554  15.336  1.00 7.21  ? 219 GLY A C     1 
ATOM   1669 O  O     . GLY A 1 239 ? -22.306 -4.269  16.519  1.00 6.98  ? 219 GLY A O     1 
ATOM   1670 N  N     . ILE A 1 240 ? -22.359 -5.766  14.809  1.00 7.06  ? 220 ILE A N     1 
ATOM   1671 C  CA    . ILE A 1 240 ? -21.827 -6.931  15.507  1.00 6.75  ? 220 ILE A CA    1 
ATOM   1672 C  C     . ILE A 1 240 ? -20.868 -7.591  14.544  1.00 6.92  ? 220 ILE A C     1 
ATOM   1673 O  O     . ILE A 1 240 ? -20.921 -7.387  13.326  1.00 6.43  ? 220 ILE A O     1 
ATOM   1674 C  CB    . ILE A 1 240 ? -22.925 -7.872  16.000  1.00 7.97  ? 220 ILE A CB    1 
ATOM   1675 C  CG1   . ILE A 1 240 ? -22.424 -8.945  16.975  1.00 8.22  ? 220 ILE A CG1   1 
ATOM   1676 C  CG2   . ILE A 1 240 ? -23.639 -8.515  14.815  1.00 7.80  ? 220 ILE A CG2   1 
ATOM   1677 C  CD1   . ILE A 1 240 ? -23.499 -9.830  17.525  1.00 9.12  ? 220 ILE A CD1   1 
ATOM   1678 N  N     . VAL A 1 241 ? -19.875 -8.262  15.110  1.00 6.24  ? 221 VAL A N     1 
ATOM   1679 C  CA    . VAL A 1 241 ? -18.845 -8.914  14.318  1.00 6.44  ? 221 VAL A CA    1 
ATOM   1680 C  C     . VAL A 1 241 ? -18.964 -10.427 14.553  1.00 6.49  ? 221 VAL A C     1 
ATOM   1681 O  O     . VAL A 1 241 ? -18.928 -10.888 15.704  1.00 6.46  ? 221 VAL A O     1 
ATOM   1682 C  CB    . VAL A 1 241 ? -17.437 -8.417  14.664  1.00 6.07  ? 221 VAL A CB    1 
ATOM   1683 C  CG1   . VAL A 1 241 ? -16.378 -9.264  14.008  1.00 6.31  ? 221 VAL A CG1   1 
ATOM   1684 C  CG2   . VAL A 1 241 ? -17.270 -6.930  14.251  1.00 6.56  ? 221 VAL A CG2   1 
ATOM   1685 N  N     . LEU A 1 242 ? -19.129 -11.185 13.461  1.00 7.31  ? 222 LEU A N     1 
ATOM   1686 C  CA    . LEU A 1 242 ? -19.218 -12.638 13.503  1.00 7.12  ? 222 LEU A CA    1 
ATOM   1687 C  C     . LEU A 1 242 ? -18.047 -13.259 12.759  1.00 7.24  ? 222 LEU A C     1 
ATOM   1688 O  O     . LEU A 1 242 ? -17.680 -12.860 11.649  1.00 7.85  ? 222 LEU A O     1 
ATOM   1689 C  CB    . LEU A 1 242 ? -20.524 -13.098 12.823  1.00 7.59  ? 222 LEU A CB    1 
ATOM   1690 C  CG    . LEU A 1 242 ? -21.804 -12.548 13.429  1.00 8.44  ? 222 LEU A CG    1 
ATOM   1691 C  CD1   . LEU A 1 242 ? -23.007 -13.125 12.674  1.00 8.82  ? 222 LEU A CD1   1 
ATOM   1692 C  CD2   . LEU A 1 242 ? -21.974 -12.821 14.898  1.00 8.73  ? 222 LEU A CD2   1 
ATOM   1693 N  N     . ASN A 1 243 ? -17.469 -14.330 13.328  1.00 7.69  ? 223 ASN A N     1 
ATOM   1694 C  CA    . ASN A 1 243 ? -16.638 -15.244 12.544  1.00 7.93  ? 223 ASN A CA    1 
ATOM   1695 C  C     . ASN A 1 243 ? -17.592 -16.096 11.723  1.00 9.49  ? 223 ASN A C     1 
ATOM   1696 O  O     . ASN A 1 243 ? -18.555 -16.605 12.275  1.00 10.00 ? 223 ASN A O     1 
ATOM   1697 C  CB    . ASN A 1 243 ? -15.722 -16.109 13.394  1.00 8.02  ? 223 ASN A CB    1 
ATOM   1698 C  CG    . ASN A 1 243 ? -16.446 -16.903 14.464  1.00 8.68  ? 223 ASN A CG    1 
ATOM   1699 O  OD1   . ASN A 1 243 ? -17.158 -16.386 15.336  1.00 9.23  ? 223 ASN A OD1   1 
ATOM   1700 N  ND2   . ASN A 1 243 ? -16.298 -18.203 14.343  1.00 9.43  ? 223 ASN A ND2   1 
ATOM   1701 N  N     . LEU A 1 244 ? -17.346 -16.224 10.427  1.00 10.16 ? 224 LEU A N     1 
ATOM   1702 C  CA    . LEU A 1 244 ? -18.131 -17.103 9.580   1.00 9.82  ? 224 LEU A CA    1 
ATOM   1703 C  C     . LEU A 1 244 ? -17.173 -18.041 8.851   1.00 10.60 ? 224 LEU A C     1 
ATOM   1704 O  O     . LEU A 1 244 ? -16.102 -17.647 8.373   1.00 11.81 ? 224 LEU A O     1 
ATOM   1705 C  CB    . LEU A 1 244 ? -18.904 -16.243 8.579   1.00 9.41  ? 224 LEU A CB    1 
ATOM   1706 C  CG    . LEU A 1 244 ? -19.913 -15.295 9.199   1.00 8.58  ? 224 LEU A CG    1 
ATOM   1707 C  CD1   . LEU A 1 244 ? -20.553 -14.429 8.113   1.00 10.04 ? 224 LEU A CD1   1 
ATOM   1708 C  CD2   . LEU A 1 244 ? -21.001 -16.020 9.967   1.00 9.05  ? 224 LEU A CD2   1 
ATOM   1709 N  N     . THR A 1 245 ? -17.556 -19.330 8.780   1.00 10.16 ? 225 THR A N     1 
ATOM   1710 C  CA    . THR A 1 245 ? -16.768 -20.344 8.132   1.00 11.46 ? 225 THR A CA    1 
ATOM   1711 C  C     . THR A 1 245 ? -17.658 -21.009 7.098   1.00 11.06 ? 225 THR A C     1 
ATOM   1712 O  O     . THR A 1 245 ? -18.528 -21.807 7.444   1.00 11.99 ? 225 THR A O     1 
ATOM   1713 C  CB    . THR A 1 245 ? -16.280 -21.408 9.138   1.00 11.80 ? 225 THR A CB    1 
ATOM   1714 O  OG1   . THR A 1 245 ? -15.397 -20.779 10.069  1.00 13.31 ? 225 THR A OG1   1 
ATOM   1715 C  CG2   . THR A 1 245 ? -15.489 -22.502 8.484   1.00 12.15 ? 225 THR A CG2   1 
ATOM   1716 N  N     . PRO A 1 246 ? -17.470 -20.692 5.809   1.00 11.08 ? 226 PRO A N     1 
ATOM   1717 C  CA    . PRO A 1 246 ? -18.281 -21.350 4.771   1.00 11.32 ? 226 PRO A CA    1 
ATOM   1718 C  C     . PRO A 1 246 ? -17.918 -22.822 4.807   1.00 10.49 ? 226 PRO A C     1 
ATOM   1719 O  O     . PRO A 1 246 ? -16.729 -23.190 4.912   1.00 11.59 ? 226 PRO A O     1 
ATOM   1720 C  CB    . PRO A 1 246 ? -17.827 -20.644 3.497   1.00 11.69 ? 226 PRO A CB    1 
ATOM   1721 C  CG    . PRO A 1 246 ? -16.416 -20.272 3.768   1.00 11.19 ? 226 PRO A CG    1 
ATOM   1722 C  CD    . PRO A 1 246 ? -16.470 -19.799 5.223   1.00 11.07 ? 226 PRO A CD    1 
ATOM   1723 N  N     . THR A 1 247 ? -18.948 -23.643 4.635   1.00 12.18 ? 227 THR A N     1 
ATOM   1724 C  CA    . THR A 1 247 ? -18.834 -25.073 4.859   1.00 12.02 ? 227 THR A CA    1 
ATOM   1725 C  C     . THR A 1 247 ? -19.225 -25.789 3.570   1.00 11.90 ? 227 THR A C     1 
ATOM   1726 O  O     . THR A 1 247 ? -20.221 -25.395 2.953   1.00 13.98 ? 227 THR A O     1 
ATOM   1727 C  CB    . THR A 1 247 ? -19.702 -25.496 6.044   1.00 13.88 ? 227 THR A CB    1 
ATOM   1728 O  OG1   . THR A 1 247 ? -19.300 -24.694 7.184   1.00 16.59 ? 227 THR A OG1   1 
ATOM   1729 C  CG2   . THR A 1 247 ? -19.531 -26.953 6.393   1.00 14.77 ? 227 THR A CG2   1 
ATOM   1730 N  N     . TYR A 1 248 ? -18.444 -26.807 3.227   1.00 11.22 ? 228 TYR A N     1 
ATOM   1731 C  CA    . TYR A 1 248 ? -18.658 -27.539 1.985   1.00 12.67 ? 228 TYR A CA    1 
ATOM   1732 C  C     . TYR A 1 248 ? -18.622 -29.026 2.276   1.00 12.39 ? 228 TYR A C     1 
ATOM   1733 O  O     . TYR A 1 248 ? -17.665 -29.485 2.915   1.00 13.59 ? 228 TYR A O     1 
ATOM   1734 C  CB    . TYR A 1 248 ? -17.553 -27.207 0.994   1.00 12.42 ? 228 TYR A CB    1 
ATOM   1735 C  CG    . TYR A 1 248 ? -17.386 -25.734 0.736   1.00 12.54 ? 228 TYR A CG    1 
ATOM   1736 C  CD1   . TYR A 1 248 ? -16.621 -24.972 1.595   1.00 13.59 ? 228 TYR A CD1   1 
ATOM   1737 C  CD2   . TYR A 1 248 ? -17.930 -25.108 -0.370  1.00 12.04 ? 228 TYR A CD2   1 
ATOM   1738 C  CE1   . TYR A 1 248 ? -16.477 -23.606 1.414   1.00 14.16 ? 228 TYR A CE1   1 
ATOM   1739 C  CE2   . TYR A 1 248 ? -17.776 -23.751 -0.573  1.00 12.51 ? 228 TYR A CE2   1 
ATOM   1740 C  CZ    . TYR A 1 248 ? -17.033 -22.999 0.315   1.00 14.13 ? 228 TYR A CZ    1 
ATOM   1741 O  OH    . TYR A 1 248 ? -16.825 -21.654 0.072   1.00 13.25 ? 228 TYR A OH    1 
ATOM   1742 N  N     . PRO A 1 249 ? -19.587 -29.819 1.770   1.00 13.00 ? 229 PRO A N     1 
ATOM   1743 C  CA    . PRO A 1 249 ? -19.537 -31.258 1.997   1.00 11.89 ? 229 PRO A CA    1 
ATOM   1744 C  C     . PRO A 1 249 ? -18.406 -31.845 1.165   1.00 13.57 ? 229 PRO A C     1 
ATOM   1745 O  O     . PRO A 1 249 ? -18.236 -31.470 -0.001  1.00 12.92 ? 229 PRO A O     1 
ATOM   1746 C  CB    . PRO A 1 249 ? -20.922 -31.765 1.551   1.00 13.17 ? 229 PRO A CB    1 
ATOM   1747 C  CG    . PRO A 1 249 ? -21.467 -30.695 0.678   1.00 12.44 ? 229 PRO A CG    1 
ATOM   1748 C  CD    . PRO A 1 249 ? -20.801 -29.384 1.074   1.00 12.11 ? 229 PRO A CD    1 
ATOM   1749 N  N     . ALA A 1 250 ? -17.621 -32.759 1.763   1.00 13.12 ? 230 ALA A N     1 
ATOM   1750 C  CA    . ALA A 1 250 ? -16.490 -33.362 1.068   1.00 15.41 ? 230 ALA A CA    1 
ATOM   1751 C  C     . ALA A 1 250 ? -16.963 -34.268 -0.062  1.00 15.07 ? 230 ALA A C     1 
ATOM   1752 O  O     . ALA A 1 250 ? -16.194 -34.541 -0.990  1.00 18.79 ? 230 ALA A O     1 
ATOM   1753 C  CB    . ALA A 1 250 ? -15.650 -34.148 2.030   1.00 18.93 ? 230 ALA A CB    1 
ATOM   1754 N  N     . SER A 1 251 ? -18.224 -34.733 0.029   1.00 13.73 ? 231 SER A N     1 
ATOM   1755 C  CA    . SER A 1 251 ? -18.865 -35.483 -1.043  1.00 12.30 ? 231 SER A CA    1 
ATOM   1756 C  C     . SER A 1 251 ? -20.339 -35.110 -1.058  1.00 13.46 ? 231 SER A C     1 
ATOM   1757 O  O     . SER A 1 251 ? -20.824 -34.499 -0.114  1.00 12.56 ? 231 SER A O     1 
ATOM   1758 C  CB    . SER A 1 251 ? -18.724 -36.996 -0.878  1.00 11.78 ? 231 SER A CB    1 
ATOM   1759 O  OG    . SER A 1 251 ? -19.626 -37.529 0.056   1.00 13.16 ? 231 SER A OG    1 
ATOM   1760 N  N     . ASP A 1 252 ? -21.075 -35.621 -2.048  1.00 13.80 ? 232 ASP A N     1 
ATOM   1761 C  CA    . ASP A 1 252 ? -22.472 -35.257 -2.155  1.00 14.82 ? 232 ASP A CA    1 
ATOM   1762 C  C     . ASP A 1 252 ? -23.333 -36.324 -1.499  1.00 13.10 ? 232 ASP A C     1 
ATOM   1763 O  O     . ASP A 1 252 ? -24.542 -36.264 -1.599  1.00 13.98 ? 232 ASP A O     1 
ATOM   1764 C  CB    . ASP A 1 252 ? -22.834 -35.003 -3.620  1.00 19.27 ? 232 ASP A CB    1 
ATOM   1765 C  CG    . ASP A 1 252 ? -22.030 -33.902 -4.316  1.00 24.68 ? 232 ASP A CG    1 
ATOM   1766 O  OD1   . ASP A 1 252 ? -21.803 -32.794 -3.729  1.00 25.20 ? 232 ASP A OD1   1 
ATOM   1767 O  OD2   . ASP A 1 252 ? -21.674 -34.121 -5.484  1.00 33.10 ? 232 ASP A OD2   1 
ATOM   1768 N  N     . SER A 1 253 ? -22.726 -37.216 -0.722  1.00 12.65 ? 233 SER A N     1 
ATOM   1769 C  CA    . SER A 1 253 ? -23.452 -38.225 0.015   1.00 13.81 ? 233 SER A CA    1 
ATOM   1770 C  C     . SER A 1 253 ? -24.343 -37.542 1.040   1.00 14.67 ? 233 SER A C     1 
ATOM   1771 O  O     . SER A 1 253 ? -23.951 -36.524 1.650   1.00 13.25 ? 233 SER A O     1 
ATOM   1772 C  CB    . SER A 1 253 ? -22.548 -39.219 0.682   1.00 18.60 ? 233 SER A CB    1 
ATOM   1773 O  OG    . SER A 1 253 ? -22.036 -38.690 1.927   1.00 20.70 ? 233 SER A OG    1 
ATOM   1774 N  N     . PRO A 1 254 ? -25.556 -38.055 1.308   1.00 13.67 ? 234 PRO A N     1 
ATOM   1775 C  CA    . PRO A 1 254 ? -26.417 -37.507 2.366   1.00 13.15 ? 234 PRO A CA    1 
ATOM   1776 C  C     . PRO A 1 254 ? -25.739 -37.254 3.721   1.00 13.16 ? 234 PRO A C     1 
ATOM   1777 O  O     . PRO A 1 254 ? -26.021 -36.263 4.413   1.00 12.50 ? 234 PRO A O     1 
ATOM   1778 C  CB    . PRO A 1 254 ? -27.520 -38.571 2.484   1.00 17.47 ? 234 PRO A CB    1 
ATOM   1779 C  CG    . PRO A 1 254 ? -27.627 -39.163 1.098   1.00 16.10 ? 234 PRO A CG    1 
ATOM   1780 C  CD    . PRO A 1 254 ? -26.211 -39.167 0.571   1.00 15.60 ? 234 PRO A CD    1 
ATOM   1781 N  N     . GLU A 1 255 ? -24.887 -38.185 4.130   1.00 14.10 ? 235 GLU A N     1 
ATOM   1782 C  CA    . GLU A 1 255 ? -24.221 -38.094 5.423   1.00 16.45 ? 235 GLU A CA    1 
ATOM   1783 C  C     . GLU A 1 255 ? -23.285 -36.883 5.456   1.00 14.10 ? 235 GLU A C     1 
ATOM   1784 O  O     . GLU A 1 255 ? -23.216 -36.203 6.480   1.00 12.42 ? 235 GLU A O     1 
ATOM   1785 C  CB    . GLU A 1 255 ? -23.473 -39.406 5.699   1.00 20.51 ? 235 GLU A CB    1 
ATOM   1786 C  CG    . GLU A 1 255 ? -24.426 -40.595 5.775   1.00 27.49 ? 235 GLU A CG    1 
ATOM   1787 C  CD    . GLU A 1 255 ? -24.953 -41.254 4.494   1.00 30.61 ? 235 GLU A CD    1 
ATOM   1788 O  OE1   . GLU A 1 255 ? -24.481 -40.941 3.365   1.00 24.15 ? 235 GLU A OE1   1 
ATOM   1789 O  OE2   . GLU A 1 255 ? -25.871 -42.104 4.627   1.00 39.93 ? 235 GLU A OE2   1 
ATOM   1790 N  N     . ASP A 1 256 ? -22.572 -36.637 4.365   1.00 13.54 ? 236 ASP A N     1 
ATOM   1791 C  CA    . ASP A 1 256 ? -21.599 -35.549 4.337   1.00 13.87 ? 236 ASP A CA    1 
ATOM   1792 C  C     . ASP A 1 256 ? -22.300 -34.208 4.138   1.00 13.47 ? 236 ASP A C     1 
ATOM   1793 O  O     . ASP A 1 256 ? -21.875 -33.187 4.675   1.00 12.45 ? 236 ASP A O     1 
ATOM   1794 C  CB    . ASP A 1 256 ? -20.539 -35.744 3.261   1.00 13.41 ? 236 ASP A CB    1 
ATOM   1795 C  CG    . ASP A 1 256 ? -19.567 -36.880 3.578   1.00 15.13 ? 236 ASP A CG    1 
ATOM   1796 O  OD1   . ASP A 1 256 ? -19.513 -37.323 4.784   1.00 15.44 ? 236 ASP A OD1   1 
ATOM   1797 O  OD2   . ASP A 1 256 ? -18.890 -37.347 2.615   1.00 17.41 ? 236 ASP A OD2   1 
ATOM   1798 N  N     . VAL A 1 257 ? -23.350 -34.191 3.312   1.00 11.71 ? 237 VAL A N     1 
ATOM   1799 C  CA    . VAL A 1 257 ? -24.111 -32.972 3.147   1.00 11.26 ? 237 VAL A CA    1 
ATOM   1800 C  C     . VAL A 1 257 ? -24.753 -32.586 4.468   1.00 10.77 ? 237 VAL A C     1 
ATOM   1801 O  O     . VAL A 1 257 ? -24.732 -31.415 4.831   1.00 10.83 ? 237 VAL A O     1 
ATOM   1802 C  CB    . VAL A 1 257 ? -25.130 -33.115 2.010   1.00 12.70 ? 237 VAL A CB    1 
ATOM   1803 C  CG1   . VAL A 1 257 ? -25.982 -31.867 1.902   1.00 14.39 ? 237 VAL A CG1   1 
ATOM   1804 C  CG2   . VAL A 1 257 ? -24.409 -33.345 0.684   1.00 12.96 ? 237 VAL A CG2   1 
ATOM   1805 N  N     . ALA A 1 258 ? -25.283 -33.548 5.222   1.00 10.74 ? 238 ALA A N     1 
ATOM   1806 C  CA    . ALA A 1 258 ? -25.905 -33.254 6.505   1.00 10.38 ? 238 ALA A CA    1 
ATOM   1807 C  C     . ALA A 1 258 ? -24.871 -32.709 7.480   1.00 11.57 ? 238 ALA A C     1 
ATOM   1808 O  O     . ALA A 1 258 ? -25.147 -31.792 8.251   1.00 10.82 ? 238 ALA A O     1 
ATOM   1809 C  CB    . ALA A 1 258 ? -26.550 -34.491 7.065   1.00 11.50 ? 238 ALA A CB    1 
ATOM   1810 N  N     . ALA A 1 259 ? -23.676 -33.301 7.431   1.00 11.80 ? 239 ALA A N     1 
ATOM   1811 C  CA    . ALA A 1 259 ? -22.606 -32.863 8.315   1.00 12.41 ? 239 ALA A CA    1 
ATOM   1812 C  C     . ALA A 1 259 ? -22.247 -31.411 8.005   1.00 12.16 ? 239 ALA A C     1 
ATOM   1813 O  O     . ALA A 1 259 ? -22.087 -30.611 8.940   1.00 11.49 ? 239 ALA A O     1 
ATOM   1814 C  CB    . ALA A 1 259 ? -21.401 -33.737 8.162   1.00 12.59 ? 239 ALA A CB    1 
ATOM   1815 N  N     . ALA A 1 260 ? -22.122 -31.093 6.716   1.00 11.37 ? 240 ALA A N     1 
ATOM   1816 C  CA    . ALA A 1 260 ? -21.855 -29.714 6.325   1.00 11.45 ? 240 ALA A CA    1 
ATOM   1817 C  C     . ALA A 1 260 ? -22.979 -28.821 6.858   1.00 10.76 ? 240 ALA A C     1 
ATOM   1818 O  O     . ALA A 1 260 ? -22.758 -27.737 7.415   1.00 11.16 ? 240 ALA A O     1 
ATOM   1819 C  CB    . ALA A 1 260 ? -21.662 -29.612 4.824   1.00 11.67 ? 240 ALA A CB    1 
ATOM   1820 N  N     . ARG A 1 261 ? -24.238 -29.241 6.719   1.00 9.99  ? 241 ARG A N     1 
ATOM   1821 C  CA    . ARG A 1 261 ? -25.346 -28.427 7.232   1.00 11.32 ? 241 ARG A CA    1 
ATOM   1822 C  C     . ARG A 1 261 ? -25.299 -28.216 8.748   1.00 11.74 ? 241 ARG A C     1 
ATOM   1823 O  O     . ARG A 1 261 ? -25.570 -27.110 9.218   1.00 11.56 ? 241 ARG A O     1 
ATOM   1824 C  CB    . ARG A 1 261 ? -26.723 -28.982 6.883   1.00 13.14 ? 241 ARG A CB    1 
ATOM   1825 C  CG    . ARG A 1 261 ? -26.958 -29.068 5.393   1.00 15.57 ? 241 ARG A CG    1 
ATOM   1826 C  CD    . ARG A 1 261 ? -28.394 -29.446 5.108   1.00 20.02 ? 241 ARG A CD    1 
ATOM   1827 N  NE    . ARG A 1 261 ? -28.544 -29.631 3.670   1.00 21.92 ? 241 ARG A NE    1 
ATOM   1828 C  CZ    . ARG A 1 261 ? -28.821 -30.816 3.128   1.00 22.08 ? 241 ARG A CZ    1 
ATOM   1829 N  NH1   . ARG A 1 261 ? -29.029 -31.843 3.928   1.00 21.74 ? 241 ARG A NH1   1 
ATOM   1830 N  NH2   . ARG A 1 261 ? -28.860 -30.959 1.809   1.00 23.78 ? 241 ARG A NH2   1 
ATOM   1831 N  N     . ARG A 1 262 ? -24.986 -29.257 9.521   1.00 11.60 ? 242 ARG A N     1 
ATOM   1832 C  CA    . ARG A 1 262 ? -24.916 -29.118 10.970  1.00 11.26 ? 242 ARG A CA    1 
ATOM   1833 C  C     . ARG A 1 262 ? -23.758 -28.185 11.338  1.00 11.24 ? 242 ARG A C     1 
ATOM   1834 O  O     . ARG A 1 262 ? -23.919 -27.393 12.252  1.00 11.52 ? 242 ARG A O     1 
ATOM   1835 C  CB    . ARG A 1 262 ? -24.705 -30.469 11.668  1.00 12.21 ? 242 ARG A CB    1 
ATOM   1836 C  CG    . ARG A 1 262 ? -25.884 -31.436 11.577  1.00 13.02 ? 242 ARG A CG    1 
ATOM   1837 C  CD    . ARG A 1 262 ? -25.612 -32.627 12.483  1.00 13.04 ? 242 ARG A CD    1 
ATOM   1838 N  NE    . ARG A 1 262 ? -24.417 -33.427 12.176  1.00 13.06 ? 242 ARG A NE    1 
ATOM   1839 C  CZ    . ARG A 1 262 ? -24.347 -34.421 11.293  1.00 13.17 ? 242 ARG A CZ    1 
ATOM   1840 N  NH1   . ARG A 1 262 ? -25.421 -34.744 10.569  1.00 13.16 ? 242 ARG A NH1   1 
ATOM   1841 N  NH2   . ARG A 1 262 ? -23.186 -34.990 11.032  1.00 13.95 ? 242 ARG A NH2   1 
ATOM   1842 N  N     . PHE A 1 263 ? -22.594 -28.309 10.700  1.00 11.21 ? 243 PHE A N     1 
ATOM   1843 C  CA    . PHE A 1 263 ? -21.496 -27.413 11.053  1.00 11.11 ? 243 PHE A CA    1 
ATOM   1844 C  C     . PHE A 1 263 ? -21.803 -25.976 10.680  1.00 10.67 ? 243 PHE A C     1 
ATOM   1845 O  O     . PHE A 1 263 ? -21.506 -25.025 11.407  1.00 10.82 ? 243 PHE A O     1 
ATOM   1846 C  CB    . PHE A 1 263 ? -20.193 -27.870 10.423  1.00 11.17 ? 243 PHE A CB    1 
ATOM   1847 C  CG    . PHE A 1 263 ? -18.978 -27.120 10.878  1.00 12.48 ? 243 PHE A CG    1 
ATOM   1848 C  CD1   . PHE A 1 263 ? -18.578 -25.986 10.209  1.00 13.63 ? 243 PHE A CD1   1 
ATOM   1849 C  CD2   . PHE A 1 263 ? -18.235 -27.555 11.962  1.00 15.93 ? 243 PHE A CD2   1 
ATOM   1850 C  CE1   . PHE A 1 263 ? -17.446 -25.299 10.604  1.00 14.34 ? 243 PHE A CE1   1 
ATOM   1851 C  CE2   . PHE A 1 263 ? -17.125 -26.838 12.374  1.00 15.69 ? 243 PHE A CE2   1 
ATOM   1852 C  CZ    . PHE A 1 263 ? -16.740 -25.718 11.696  1.00 15.25 ? 243 PHE A CZ    1 
ATOM   1853 N  N     . ASP A 1 264 ? -22.430 -25.782 9.514   1.00 11.41 ? 244 ASP A N     1 
ATOM   1854 C  CA    . ASP A 1 264 ? -22.865 -24.467 9.100   1.00 11.31 ? 244 ASP A CA    1 
ATOM   1855 C  C     . ASP A 1 264 ? -23.851 -23.886 10.112  1.00 11.14 ? 244 ASP A C     1 
ATOM   1856 O  O     . ASP A 1 264 ? -23.851 -22.678 10.361  1.00 11.59 ? 244 ASP A O     1 
ATOM   1857 C  CB    . ASP A 1 264 ? -23.469 -24.549 7.698   1.00 12.24 ? 244 ASP A CB    1 
ATOM   1858 C  CG    . ASP A 1 264 ? -24.009 -23.222 7.187   1.00 12.91 ? 244 ASP A CG    1 
ATOM   1859 O  OD1   . ASP A 1 264 ? -23.183 -22.304 6.905   1.00 14.79 ? 244 ASP A OD1   1 
ATOM   1860 O  OD2   . ASP A 1 264 ? -25.233 -23.102 7.095   1.00 11.91 ? 244 ASP A OD2   1 
ATOM   1861 N  N     . GLY A 1 265 ? -24.755 -24.712 10.663  1.00 10.50 ? 245 GLY A N     1 
ATOM   1862 C  CA    . GLY A 1 265 ? -25.686 -24.239 11.680  1.00 9.26  ? 245 GLY A CA    1 
ATOM   1863 C  C     . GLY A 1 265 ? -24.987 -23.888 12.993  1.00 10.02 ? 245 GLY A C     1 
ATOM   1864 O  O     . GLY A 1 265 ? -25.389 -22.904 13.630  1.00 10.62 ? 245 GLY A O     1 
ATOM   1865 N  N     . PHE A 1 266 ? -23.979 -24.703 13.338  1.00 10.36 ? 246 PHE A N     1 
ATOM   1866 C  CA    . PHE A 1 266 ? -23.266 -24.611 14.614  1.00 10.26 ? 246 PHE A CA    1 
ATOM   1867 C  C     . PHE A 1 266 ? -22.534 -23.279 14.688  1.00 9.71  ? 246 PHE A C     1 
ATOM   1868 O  O     . PHE A 1 266 ? -22.642 -22.606 15.732  1.00 9.00  ? 246 PHE A O     1 
ATOM   1869 C  CB    . PHE A 1 266 ? -22.298 -25.787 14.701  1.00 10.20 ? 246 PHE A CB    1 
ATOM   1870 C  CG    . PHE A 1 266 ? -21.336 -25.803 15.869  1.00 10.14 ? 246 PHE A CG    1 
ATOM   1871 C  CD1   . PHE A 1 266 ? -21.780 -25.762 17.172  1.00 11.94 ? 246 PHE A CD1   1 
ATOM   1872 C  CD2   . PHE A 1 266 ? -19.977 -25.979 15.629  1.00 12.08 ? 246 PHE A CD2   1 
ATOM   1873 C  CE1   . PHE A 1 266 ? -20.873 -25.813 18.217  1.00 12.13 ? 246 PHE A CE1   1 
ATOM   1874 C  CE2   . PHE A 1 266 ? -19.082 -26.071 16.685  1.00 12.07 ? 246 PHE A CE2   1 
ATOM   1875 C  CZ    . PHE A 1 266 ? -19.530 -25.959 17.953  1.00 11.23 ? 246 PHE A CZ    1 
ATOM   1876 N  N     . VAL A 1 267 ? -21.855 -22.923 13.585  1.00 9.39  ? 247 VAL A N     1 
ATOM   1877 C  CA    . VAL A 1 267 ? -20.989 -21.732 13.566  1.00 10.05 ? 247 VAL A CA    1 
ATOM   1878 C  C     . VAL A 1 267 ? -21.790 -20.530 13.052  1.00 11.36 ? 247 VAL A C     1 
ATOM   1879 O  O     . VAL A 1 267 ? -21.757 -19.447 13.646  1.00 12.02 ? 247 VAL A O     1 
ATOM   1880 C  CB    . VAL A 1 267 ? -19.691 -21.941 12.745  1.00 10.81 ? 247 VAL A CB    1 
ATOM   1881 C  CG1   . VAL A 1 267 ? -18.823 -20.698 12.748  1.00 11.64 ? 247 VAL A CG1   1 
ATOM   1882 C  CG2   . VAL A 1 267 ? -18.868 -23.119 13.201  1.00 11.36 ? 247 VAL A CG2   1 
ATOM   1883 N  N     . ASN A 1 268 ? -22.523 -20.678 11.933  1.00 10.71 ? 248 ASN A N     1 
ATOM   1884 C  CA    . ASN A 1 268 ? -22.948 -19.511 11.197  1.00 9.90  ? 248 ASN A CA    1 
ATOM   1885 C  C     . ASN A 1 268 ? -24.407 -19.204 11.488  1.00 10.14 ? 248 ASN A C     1 
ATOM   1886 O  O     . ASN A 1 268 ? -24.754 -18.117 11.940  1.00 9.78  ? 248 ASN A O     1 
ATOM   1887 C  CB    . ASN A 1 268 ? -22.684 -19.658 9.692   1.00 10.48 ? 248 ASN A CB    1 
ATOM   1888 C  CG    . ASN A 1 268 ? -21.255 -20.041 9.359   1.00 11.61 ? 248 ASN A CG    1 
ATOM   1889 O  OD1   . ASN A 1 268 ? -20.270 -19.507 9.894   1.00 10.81 ? 248 ASN A OD1   1 
ATOM   1890 N  ND2   . ASN A 1 268 ? -21.100 -21.033 8.500   1.00 12.52 ? 248 ASN A ND2   1 
ATOM   1891 N  N     . ARG A 1 269 ? -25.323 -20.141 11.158  1.00 9.36  ? 249 ARG A N     1 
ATOM   1892 C  CA    . ARG A 1 269 ? -26.732 -19.805 11.171  1.00 9.52  ? 249 ARG A CA    1 
ATOM   1893 C  C     . ARG A 1 269 ? -27.272 -19.627 12.582  1.00 8.64  ? 249 ARG A C     1 
ATOM   1894 O  O     . ARG A 1 269 ? -28.206 -18.887 12.816  1.00 9.61  ? 249 ARG A O     1 
ATOM   1895 C  CB    . ARG A 1 269 ? -27.546 -20.887 10.452  1.00 9.63  ? 249 ARG A CB    1 
ATOM   1896 C  CG    . ARG A 1 269 ? -27.154 -21.039 8.997   1.00 10.31 ? 249 ARG A CG    1 
ATOM   1897 C  CD    . ARG A 1 269 ? -27.962 -22.111 8.282   1.00 11.06 ? 249 ARG A CD    1 
ATOM   1898 N  NE    . ARG A 1 269 ? -27.631 -23.471 8.721   1.00 12.48 ? 249 ARG A NE    1 
ATOM   1899 C  CZ    . ARG A 1 269 ? -28.489 -24.325 9.264   1.00 10.96 ? 249 ARG A CZ    1 
ATOM   1900 N  NH1   . ARG A 1 269 ? -29.665 -23.936 9.729   1.00 12.14 ? 249 ARG A NH1   1 
ATOM   1901 N  NH2   . ARG A 1 269 ? -28.069 -25.556 9.473   1.00 12.61 ? 249 ARG A NH2   1 
ATOM   1902 N  N     . TRP A 1 270 ? -26.636 -20.291 13.543  1.00 8.92  ? 250 TRP A N     1 
ATOM   1903 C  CA    . TRP A 1 270 ? -27.040 -20.134 14.934  1.00 8.40  ? 250 TRP A CA    1 
ATOM   1904 C  C     . TRP A 1 270 ? -27.068 -18.667 15.361  1.00 8.36  ? 250 TRP A C     1 
ATOM   1905 O  O     . TRP A 1 270 ? -27.878 -18.274 16.175  1.00 9.12  ? 250 TRP A O     1 
ATOM   1906 C  CB    . TRP A 1 270 ? -26.154 -20.967 15.889  1.00 8.90  ? 250 TRP A CB    1 
ATOM   1907 C  CG    . TRP A 1 270 ? -26.687 -20.993 17.285  1.00 8.64  ? 250 TRP A CG    1 
ATOM   1908 C  CD1   . TRP A 1 270 ? -26.216 -20.314 18.383  1.00 9.29  ? 250 TRP A CD1   1 
ATOM   1909 C  CD2   . TRP A 1 270 ? -27.838 -21.718 17.743  1.00 9.33  ? 250 TRP A CD2   1 
ATOM   1910 N  NE1   . TRP A 1 270 ? -26.983 -20.578 19.485  1.00 10.09 ? 250 TRP A NE1   1 
ATOM   1911 C  CE2   . TRP A 1 270 ? -27.983 -21.432 19.121  1.00 10.03 ? 250 TRP A CE2   1 
ATOM   1912 C  CE3   . TRP A 1 270 ? -28.724 -22.608 17.128  1.00 9.93  ? 250 TRP A CE3   1 
ATOM   1913 C  CZ2   . TRP A 1 270 ? -29.008 -21.974 19.902  1.00 10.90 ? 250 TRP A CZ2   1 
ATOM   1914 C  CZ3   . TRP A 1 270 ? -29.762 -23.109 17.887  1.00 10.68 ? 250 TRP A CZ3   1 
ATOM   1915 C  CH2   . TRP A 1 270 ? -29.904 -22.790 19.245  1.00 11.12 ? 250 TRP A CH2   1 
ATOM   1916 N  N     . PHE A 1 271 ? -26.113 -17.867 14.835  1.00 8.63  ? 251 PHE A N     1 
ATOM   1917 C  CA    . PHE A 1 271 ? -26.005 -16.454 15.122  1.00 8.98  ? 251 PHE A CA    1 
ATOM   1918 C  C     . PHE A 1 271 ? -26.686 -15.588 14.055  1.00 8.16  ? 251 PHE A C     1 
ATOM   1919 O  O     . PHE A 1 271 ? -27.409 -14.693 14.418  1.00 9.26  ? 251 PHE A O     1 
ATOM   1920 C  CB    . PHE A 1 271 ? -24.524 -16.098 15.337  1.00 8.73  ? 251 PHE A CB    1 
ATOM   1921 C  CG    . PHE A 1 271 ? -23.983 -16.767 16.559  1.00 8.99  ? 251 PHE A CG    1 
ATOM   1922 C  CD1   . PHE A 1 271 ? -24.179 -16.209 17.805  1.00 8.91  ? 251 PHE A CD1   1 
ATOM   1923 C  CD2   . PHE A 1 271 ? -23.336 -17.980 16.464  1.00 9.08  ? 251 PHE A CD2   1 
ATOM   1924 C  CE1   . PHE A 1 271 ? -23.761 -16.883 18.939  1.00 9.55  ? 251 PHE A CE1   1 
ATOM   1925 C  CE2   . PHE A 1 271 ? -22.890 -18.633 17.609  1.00 9.81  ? 251 PHE A CE2   1 
ATOM   1926 C  CZ    . PHE A 1 271 ? -23.102 -18.062 18.832  1.00 8.70  ? 251 PHE A CZ    1 
ATOM   1927 N  N     . LEU A 1 272 ? -26.508 -15.888 12.779  1.00 9.00  ? 252 LEU A N     1 
ATOM   1928 C  CA    . LEU A 1 272 ? -27.065 -15.044 11.717  1.00 10.05 ? 252 LEU A CA    1 
ATOM   1929 C  C     . LEU A 1 272 ? -28.590 -15.039 11.774  1.00 10.70 ? 252 LEU A C     1 
ATOM   1930 O  O     . LEU A 1 272 ? -29.231 -13.993 11.665  1.00 12.13 ? 252 LEU A O     1 
ATOM   1931 C  CB    . LEU A 1 272 ? -26.630 -15.572 10.359  1.00 11.21 ? 252 LEU A CB    1 
ATOM   1932 C  CG    . LEU A 1 272 ? -25.181 -15.346 9.976   1.00 12.40 ? 252 LEU A CG    1 
ATOM   1933 C  CD1   . LEU A 1 272 ? -24.829 -16.206 8.770   1.00 15.12 ? 252 LEU A CD1   1 
ATOM   1934 C  CD2   . LEU A 1 272 ? -24.958 -13.859 9.705   1.00 11.84 ? 252 LEU A CD2   1 
ATOM   1935 N  N     . ASP A 1 273 ? -29.198 -16.214 11.969  1.00 10.85 ? 253 ASP A N     1 
ATOM   1936 C  CA    . ASP A 1 273 ? -30.654 -16.275 11.890  1.00 11.89 ? 253 ASP A CA    1 
ATOM   1937 C  C     . ASP A 1 273 ? -31.326 -15.444 12.963  1.00 11.64 ? 253 ASP A C     1 
ATOM   1938 O  O     . ASP A 1 273 ? -32.231 -14.658 12.675  1.00 13.05 ? 253 ASP A O     1 
ATOM   1939 C  CB    . ASP A 1 273 ? -31.182 -17.704 11.946  1.00 11.89 ? 253 ASP A CB    1 
ATOM   1940 C  CG    . ASP A 1 273 ? -31.006 -18.479 10.655  1.00 15.29 ? 253 ASP A CG    1 
ATOM   1941 O  OD1   . ASP A 1 273 ? -30.392 -17.944 9.689   1.00 17.31 ? 253 ASP A OD1   1 
ATOM   1942 O  OD2   . ASP A 1 273 ? -31.429 -19.668 10.638  1.00 16.71 ? 253 ASP A OD2   1 
ATOM   1943 N  N     . PRO A 1 274 ? -31.020 -15.590 14.268  1.00 11.06 ? 254 PRO A N     1 
ATOM   1944 C  CA    . PRO A 1 274 ? -31.711 -14.762 15.263  1.00 11.41 ? 254 PRO A CA    1 
ATOM   1945 C  C     . PRO A 1 274 ? -31.417 -13.269 15.084  1.00 10.93 ? 254 PRO A C     1 
ATOM   1946 O  O     . PRO A 1 274 ? -32.291 -12.421 15.303  1.00 11.55 ? 254 PRO A O     1 
ATOM   1947 C  CB    . PRO A 1 274 ? -31.228 -15.285 16.617  1.00 12.74 ? 254 PRO A CB    1 
ATOM   1948 C  CG    . PRO A 1 274 ? -30.012 -16.080 16.303  1.00 11.72 ? 254 PRO A CG    1 
ATOM   1949 C  CD    . PRO A 1 274 ? -30.125 -16.591 14.879  1.00 10.94 ? 254 PRO A CD    1 
ATOM   1950 N  N     . LEU A 1 275 ? -30.184 -12.936 14.655  1.00 10.75 ? 255 LEU A N     1 
ATOM   1951 C  CA    . LEU A 1 275 ? -29.880 -11.550 14.349  1.00 10.77 ? 255 LEU A CA    1 
ATOM   1952 C  C     . LEU A 1 275 ? -30.770 -11.009 13.224  1.00 11.02 ? 255 LEU A C     1 
ATOM   1953 O  O     . LEU A 1 275 ? -31.085 -9.812  13.204  1.00 12.89 ? 255 LEU A O     1 
ATOM   1954 C  CB    . LEU A 1 275 ? -28.398 -11.408 14.037  1.00 10.33 ? 255 LEU A CB    1 
ATOM   1955 C  CG    . LEU A 1 275 ? -27.448 -11.533 15.245  1.00 10.58 ? 255 LEU A CG    1 
ATOM   1956 C  CD1   . LEU A 1 275 ? -26.045 -11.648 14.701  1.00 10.39 ? 255 LEU A CD1   1 
ATOM   1957 C  CD2   . LEU A 1 275 ? -27.574 -10.341 16.189  1.00 10.46 ? 255 LEU A CD2   1 
ATOM   1958 N  N     . ALA A 1 276 ? -31.139 -11.885 12.282  1.00 12.34 ? 256 ALA A N     1 
ATOM   1959 C  CA    . ALA A 1 276 ? -31.912 -11.514 11.110  1.00 12.49 ? 256 ALA A CA    1 
ATOM   1960 C  C     . ALA A 1 276 ? -33.405 -11.528 11.400  1.00 13.96 ? 256 ALA A C     1 
ATOM   1961 O  O     . ALA A 1 276 ? -34.163 -11.307 10.443  1.00 14.80 ? 256 ALA A O     1 
ATOM   1962 C  CB    . ALA A 1 276 ? -31.605 -12.457 9.991   1.00 13.55 ? 256 ALA A CB    1 
ATOM   1963 N  N     . GLY A 1 277 ? -33.809 -11.794 12.628  1.00 13.78 ? 257 GLY A N     1 
ATOM   1964 C  CA    . GLY A 1 277 ? -35.228 -11.862 12.990  1.00 15.33 ? 257 GLY A CA    1 
ATOM   1965 C  C     . GLY A 1 277 ? -35.905 -13.178 12.593  1.00 17.24 ? 257 GLY A C     1 
ATOM   1966 O  O     . GLY A 1 277 ? -37.149 -13.225 12.487  1.00 16.39 ? 257 GLY A O     1 
ATOM   1967 N  N     . ARG A 1 278 ? -35.093 -14.234 12.396  1.00 14.27 ? 258 ARG A N     1 
ATOM   1968 C  CA    . ARG A 1 278 ? -35.567 -15.526 11.892  1.00 13.67 ? 258 ARG A CA    1 
ATOM   1969 C  C     . ARG A 1 278 ? -35.644 -16.558 13.008  1.00 14.54 ? 258 ARG A C     1 
ATOM   1970 O  O     . ARG A 1 278 ? -35.966 -17.724 12.719  1.00 14.98 ? 258 ARG A O     1 
ATOM   1971 C  CB    . ARG A 1 278 ? -34.679 -16.043 10.766  1.00 13.93 ? 258 ARG A CB    1 
ATOM   1972 C  CG    . ARG A 1 278 ? -34.690 -15.137 9.546   1.00 14.51 ? 258 ARG A CG    1 
ATOM   1973 C  CD    . ARG A 1 278 ? -33.820 -15.609 8.427   1.00 15.04 ? 258 ARG A CD    1 
ATOM   1974 N  NE    . ARG A 1 278 ? -33.820 -14.605 7.398   1.00 14.16 ? 258 ARG A NE    1 
ATOM   1975 C  CZ    . ARG A 1 278 ? -33.038 -14.626 6.342   1.00 14.24 ? 258 ARG A CZ    1 
ATOM   1976 N  NH1   . ARG A 1 278 ? -32.232 -15.642 6.121   1.00 15.19 ? 258 ARG A NH1   1 
ATOM   1977 N  NH2   . ARG A 1 278 ? -33.104 -13.622 5.491   1.00 16.17 ? 258 ARG A NH2   1 
ATOM   1978 N  N     . GLY A 1 279 ? -35.461 -16.126 14.266  1.00 13.54 ? 259 GLY A N     1 
ATOM   1979 C  CA    . GLY A 1 279 ? -35.351 -17.040 15.388  1.00 14.27 ? 259 GLY A CA    1 
ATOM   1980 C  C     . GLY A 1 279 ? -34.115 -17.932 15.252  1.00 12.30 ? 259 GLY A C     1 
ATOM   1981 O  O     . GLY A 1 279 ? -33.337 -17.771 14.318  1.00 13.95 ? 259 GLY A O     1 
ATOM   1982 N  N     . TYR A 1 280 ? -33.935 -18.879 16.177  1.00 13.05 ? 260 TYR A N     1 
ATOM   1983 C  CA    . TYR A 1 280 ? -32.871 -19.864 16.059  1.00 11.05 ? 260 TYR A CA    1 
ATOM   1984 C  C     . TYR A 1 280 ? -33.206 -20.859 14.949  1.00 12.12 ? 260 TYR A C     1 
ATOM   1985 O  O     . TYR A 1 280 ? -34.393 -21.163 14.732  1.00 13.89 ? 260 TYR A O     1 
ATOM   1986 C  CB    . TYR A 1 280 ? -32.604 -20.591 17.377  1.00 12.14 ? 260 TYR A CB    1 
ATOM   1987 C  CG    . TYR A 1 280 ? -31.931 -19.753 18.433  1.00 12.40 ? 260 TYR A CG    1 
ATOM   1988 C  CD1   . TYR A 1 280 ? -30.604 -19.364 18.283  1.00 11.72 ? 260 TYR A CD1   1 
ATOM   1989 C  CD2   . TYR A 1 280 ? -32.588 -19.305 19.550  1.00 12.26 ? 260 TYR A CD2   1 
ATOM   1990 C  CE1   . TYR A 1 280 ? -29.990 -18.553 19.213  1.00 11.73 ? 260 TYR A CE1   1 
ATOM   1991 C  CE2   . TYR A 1 280 ? -31.992 -18.459 20.482  1.00 13.61 ? 260 TYR A CE2   1 
ATOM   1992 C  CZ    . TYR A 1 280 ? -30.647 -18.135 20.346  1.00 12.40 ? 260 TYR A CZ    1 
ATOM   1993 O  OH    . TYR A 1 280 ? -30.032 -17.306 21.267  1.00 12.74 ? 260 TYR A OH    1 
ATOM   1994 N  N     . PRO A 1 281 ? -32.229 -21.359 14.183  1.00 12.04 ? 261 PRO A N     1 
ATOM   1995 C  CA    . PRO A 1 281 ? -32.524 -22.313 13.107  1.00 12.24 ? 261 PRO A CA    1 
ATOM   1996 C  C     . PRO A 1 281 ? -33.155 -23.602 13.654  1.00 14.50 ? 261 PRO A C     1 
ATOM   1997 O  O     . PRO A 1 281 ? -32.643 -24.217 14.571  1.00 13.58 ? 261 PRO A O     1 
ATOM   1998 C  CB    . PRO A 1 281 ? -31.190 -22.593 12.453  1.00 13.54 ? 261 PRO A CB    1 
ATOM   1999 C  CG    . PRO A 1 281 ? -30.128 -22.012 13.369  1.00 13.47 ? 261 PRO A CG    1 
ATOM   2000 C  CD    . PRO A 1 281 ? -30.794 -21.017 14.261  1.00 11.54 ? 261 PRO A CD    1 
ATOM   2001 N  N     . GLN A 1 282 ? -34.303 -23.987 13.104  1.00 15.10 ? 262 GLN A N     1 
ATOM   2002 C  CA    . GLN A 1 282 ? -35.059 -25.074 13.726  1.00 16.58 ? 262 GLN A CA    1 
ATOM   2003 C  C     . GLN A 1 282 ? -34.326 -26.414 13.619  1.00 14.12 ? 262 GLN A C     1 
ATOM   2004 O  O     . GLN A 1 282 ? -34.466 -27.269 14.510  1.00 14.81 ? 262 GLN A O     1 
ATOM   2005 C  CB    . GLN A 1 282 ? -36.467 -25.136 13.101  1.00 18.93 ? 262 GLN A CB    1 
ATOM   2006 C  CG    . GLN A 1 282 ? -37.450 -26.032 13.871  1.00 22.03 ? 262 GLN A CG    1 
ATOM   2007 C  CD    . GLN A 1 282 ? -37.756 -25.526 15.260  1.00 24.47 ? 262 GLN A CD    1 
ATOM   2008 O  OE1   . GLN A 1 282 ? -38.182 -24.387 15.447  1.00 26.65 ? 262 GLN A OE1   1 
ATOM   2009 N  NE2   . GLN A 1 282 ? -37.504 -26.348 16.272  1.00 28.28 ? 262 GLN A NE2   1 
ATOM   2010 N  N     . ASP A 1 283 ? -33.537 -26.631 12.564  1.00 13.20 ? 263 ASP A N     1 
ATOM   2011 C  CA    . ASP A 1 283 ? -32.801 -27.878 12.398  1.00 13.47 ? 263 ASP A CA    1 
ATOM   2012 C  C     . ASP A 1 283 ? -31.831 -28.019 13.568  1.00 14.37 ? 263 ASP A C     1 
ATOM   2013 O  O     . ASP A 1 283 ? -31.651 -29.098 14.122  1.00 15.34 ? 263 ASP A O     1 
ATOM   2014 C  CB    . ASP A 1 283 ? -32.141 -27.995 11.035  1.00 14.58 ? 263 ASP A CB    1 
ATOM   2015 C  CG    . ASP A 1 283 ? -31.053 -26.977 10.730  1.00 14.99 ? 263 ASP A CG    1 
ATOM   2016 O  OD1   . ASP A 1 283 ? -31.225 -25.828 11.180  1.00 18.69 ? 263 ASP A OD1   1 
ATOM   2017 O  OD2   . ASP A 1 283 ? -30.083 -27.353 10.045  1.00 16.06 ? 263 ASP A OD2   1 
ATOM   2018 N  N     . MET A 1 284 ? -31.237 -26.896 13.964  1.00 12.80 ? 264 MET A N     1 
ATOM   2019 C  CA    . MET A 1 284 ? -30.281 -26.948 15.062  1.00 12.91 ? 264 MET A CA    1 
ATOM   2020 C  C     . MET A 1 284 ? -31.012 -27.043 16.391  1.00 12.59 ? 264 MET A C     1 
ATOM   2021 O  O     . MET A 1 284 ? -30.567 -27.736 17.275  1.00 12.89 ? 264 MET A O     1 
ATOM   2022 C  CB    . MET A 1 284 ? -29.338 -25.747 15.051  1.00 13.00 ? 264 MET A CB    1 
ATOM   2023 C  CG    . MET A 1 284 ? -28.598 -25.630 13.764  1.00 14.09 ? 264 MET A CG    1 
ATOM   2024 S  SD    . MET A 1 284 ? -27.618 -27.034 13.316  1.00 14.92 ? 264 MET A SD    1 
ATOM   2025 C  CE    . MET A 1 284 ? -26.407 -27.078 14.644  1.00 17.12 ? 264 MET A CE    1 
ATOM   2026 N  N     . LEU A 1 285 ? -32.161 -26.390 16.540  1.00 15.43 ? 265 LEU A N     1 
ATOM   2027 C  CA    . LEU A 1 285 ? -32.910 -26.515 17.771  1.00 15.03 ? 265 LEU A CA    1 
ATOM   2028 C  C     . LEU A 1 285 ? -33.260 -27.986 18.008  1.00 16.01 ? 265 LEU A C     1 
ATOM   2029 O  O     . LEU A 1 285 ? -33.119 -28.515 19.106  1.00 18.83 ? 265 LEU A O     1 
ATOM   2030 C  CB    . LEU A 1 285 ? -34.172 -25.657 17.673  1.00 16.15 ? 265 LEU A CB    1 
ATOM   2031 C  CG    . LEU A 1 285 ? -33.982 -24.171 17.897  1.00 15.44 ? 265 LEU A CG    1 
ATOM   2032 C  CD1   . LEU A 1 285 ? -35.299 -23.452 17.680  1.00 17.72 ? 265 LEU A CD1   1 
ATOM   2033 C  CD2   . LEU A 1 285 ? -33.428 -23.884 19.270  1.00 15.89 ? 265 LEU A CD2   1 
ATOM   2034 N  N     . ASP A 1 286 ? -33.721 -28.657 16.958  1.00 17.72 ? 266 ASP A N     1 
ATOM   2035 C  CA    . ASP A 1 286 ? -34.179 -30.033 17.119  1.00 19.85 ? 266 ASP A CA    1 
ATOM   2036 C  C     . ASP A 1 286 ? -32.994 -30.938 17.435  1.00 20.64 ? 266 ASP A C     1 
ATOM   2037 O  O     . ASP A 1 286 ? -33.125 -31.859 18.254  1.00 22.08 ? 266 ASP A O     1 
ATOM   2038 C  CB    . ASP A 1 286 ? -34.906 -30.490 15.860  1.00 20.49 ? 266 ASP A CB    1 
ATOM   2039 C  CG    . ASP A 1 286 ? -36.258 -29.814 15.659  1.00 22.86 ? 266 ASP A CG    1 
ATOM   2040 O  OD1   . ASP A 1 286 ? -36.858 -29.286 16.653  1.00 26.32 ? 266 ASP A OD1   1 
ATOM   2041 O  OD2   . ASP A 1 286 ? -36.684 -29.782 14.488  1.00 26.81 ? 266 ASP A OD2   1 
ATOM   2042 N  N     . TYR A 1 287 ? -31.834 -30.638 16.804  1.00 16.73 ? 267 TYR A N     1 
ATOM   2043 C  CA    . TYR A 1 287 ? -30.603 -31.383 16.984  1.00 17.22 ? 267 TYR A CA    1 
ATOM   2044 C  C     . TYR A 1 287 ? -30.076 -31.232 18.411  1.00 17.60 ? 267 TYR A C     1 
ATOM   2045 O  O     . TYR A 1 287 ? -29.687 -32.212 19.029  1.00 19.44 ? 267 TYR A O     1 
ATOM   2046 C  CB    . TYR A 1 287 ? -29.577 -30.938 15.944  1.00 17.18 ? 267 TYR A CB    1 
ATOM   2047 C  CG    . TYR A 1 287 ? -28.210 -31.574 15.995  1.00 17.34 ? 267 TYR A CG    1 
ATOM   2048 C  CD1   . TYR A 1 287 ? -28.020 -32.941 15.856  1.00 18.52 ? 267 TYR A CD1   1 
ATOM   2049 C  CD2   . TYR A 1 287 ? -27.083 -30.796 16.124  1.00 16.68 ? 267 TYR A CD2   1 
ATOM   2050 C  CE1   . TYR A 1 287 ? -26.753 -33.515 15.827  1.00 16.98 ? 267 TYR A CE1   1 
ATOM   2051 C  CE2   . TYR A 1 287 ? -25.809 -31.345 16.111  1.00 16.92 ? 267 TYR A CE2   1 
ATOM   2052 C  CZ    . TYR A 1 287 ? -25.641 -32.719 16.025  1.00 16.95 ? 267 TYR A CZ    1 
ATOM   2053 O  OH    . TYR A 1 287 ? -24.397 -33.272 15.997  1.00 16.15 ? 267 TYR A OH    1 
ATOM   2054 N  N     . TYR A 1 288 ? -30.025 -29.997 18.921  1.00 14.20 ? 268 TYR A N     1 
ATOM   2055 C  CA    . TYR A 1 288 ? -29.611 -29.748 20.289  1.00 15.06 ? 268 TYR A CA    1 
ATOM   2056 C  C     . TYR A 1 288 ? -30.609 -30.241 21.343  1.00 15.89 ? 268 TYR A C     1 
ATOM   2057 O  O     . TYR A 1 288 ? -30.236 -30.488 22.494  1.00 19.41 ? 268 TYR A O     1 
ATOM   2058 C  CB    . TYR A 1 288 ? -29.387 -28.245 20.475  1.00 14.13 ? 268 TYR A CB    1 
ATOM   2059 C  CG    . TYR A 1 288 ? -28.249 -27.664 19.683  1.00 13.51 ? 268 TYR A CG    1 
ATOM   2060 C  CD1   . TYR A 1 288 ? -27.079 -28.355 19.434  1.00 14.24 ? 268 TYR A CD1   1 
ATOM   2061 C  CD2   . TYR A 1 288 ? -28.332 -26.363 19.210  1.00 12.68 ? 268 TYR A CD2   1 
ATOM   2062 C  CE1   . TYR A 1 288 ? -26.026 -27.770 18.752  1.00 15.29 ? 268 TYR A CE1   1 
ATOM   2063 C  CE2   . TYR A 1 288 ? -27.308 -25.789 18.491  1.00 14.37 ? 268 TYR A CE2   1 
ATOM   2064 C  CZ    . TYR A 1 288 ? -26.131 -26.481 18.270  1.00 14.34 ? 268 TYR A CZ    1 
ATOM   2065 O  OH    . TYR A 1 288 ? -25.089 -25.870 17.574  1.00 14.58 ? 268 TYR A OH    1 
ATOM   2066 N  N     . GLY A 1 289 ? -31.889 -30.307 20.991  1.00 17.56 ? 269 GLY A N     1 
ATOM   2067 C  CA    . GLY A 1 289 ? -32.902 -30.664 21.973  1.00 18.61 ? 269 GLY A CA    1 
ATOM   2068 C  C     . GLY A 1 289 ? -32.906 -29.747 23.186  1.00 18.06 ? 269 GLY A C     1 
ATOM   2069 O  O     . GLY A 1 289 ? -32.814 -28.512 23.079  1.00 22.39 ? 269 GLY A O     1 
ATOM   2070 N  N     . ALA A 1 290 ? -33.084 -30.327 24.382  1.00 18.94 ? 270 ALA A N     1 
ATOM   2071 C  CA    . ALA A 1 290 ? -33.354 -29.537 25.572  1.00 21.24 ? 270 ALA A CA    1 
ATOM   2072 C  C     . ALA A 1 290 ? -32.106 -28.767 25.989  1.00 21.31 ? 270 ALA A C     1 
ATOM   2073 O  O     . ALA A 1 290 ? -32.205 -27.896 26.853  1.00 21.30 ? 270 ALA A O     1 
ATOM   2074 C  CB    . ALA A 1 290 ? -33.863 -30.393 26.720  1.00 22.67 ? 270 ALA A CB    1 
ATOM   2075 N  N     . ALA A 1 291 ? -30.971 -29.070 25.353  1.00 22.15 ? 271 ALA A N     1 
ATOM   2076 C  CA    . ALA A 1 291 ? -29.744 -28.334 25.655  1.00 22.83 ? 271 ALA A CA    1 
ATOM   2077 C  C     . ALA A 1 291 ? -29.819 -26.888 25.148  1.00 24.58 ? 271 ALA A C     1 
ATOM   2078 O  O     . ALA A 1 291 ? -29.183 -25.992 25.711  1.00 22.63 ? 271 ALA A O     1 
ATOM   2079 C  CB    . ALA A 1 291 ? -28.562 -29.055 25.088  1.00 23.23 ? 271 ALA A CB    1 
ATOM   2080 N  N     . ALA A 1 292 ? -30.645 -26.647 24.117  1.00 21.27 ? 272 ALA A N     1 
ATOM   2081 C  CA    . ALA A 1 292 ? -30.829 -25.294 23.613  1.00 22.77 ? 272 ALA A CA    1 
ATOM   2082 C  C     . ALA A 1 292 ? -31.601 -24.456 24.623  1.00 21.75 ? 272 ALA A C     1 
ATOM   2083 O  O     . ALA A 1 292 ? -32.446 -24.947 25.391  1.00 20.07 ? 272 ALA A O     1 
ATOM   2084 C  CB    . ALA A 1 292 ? -31.543 -25.329 22.286  1.00 24.67 ? 272 ALA A CB    1 
ATOM   2085 N  N     . PRO A 1 293 ? -31.382 -23.131 24.643  1.00 22.87 ? 273 PRO A N     1 
ATOM   2086 C  CA    . PRO A 1 293 ? -32.039 -22.288 25.632  1.00 27.72 ? 273 PRO A CA    1 
ATOM   2087 C  C     . PRO A 1 293 ? -33.508 -22.167 25.242  1.00 26.39 ? 273 PRO A C     1 
ATOM   2088 O  O     . PRO A 1 293 ? -33.851 -22.417 24.091  1.00 21.04 ? 273 PRO A O     1 
ATOM   2089 C  CB    . PRO A 1 293 ? -31.271 -20.970 25.519  1.00 31.34 ? 273 PRO A CB    1 
ATOM   2090 C  CG    . PRO A 1 293 ? -30.787 -20.938 24.065  1.00 29.59 ? 273 PRO A CG    1 
ATOM   2091 C  CD    . PRO A 1 293 ? -30.558 -22.382 23.680  1.00 28.81 ? 273 PRO A CD    1 
ATOM   2092 N  N     . GLN A 1 294 ? -34.334 -21.808 26.225  1.00 35.23 ? 274 GLN A N     1 
ATOM   2093 C  CA    . GLN A 1 294 ? -35.754 -21.546 26.023  1.00 48.05 ? 274 GLN A CA    1 
ATOM   2094 C  C     . GLN A 1 294 ? -35.896 -20.099 25.576  1.00 50.17 ? 274 GLN A C     1 
ATOM   2095 O  O     . GLN A 1 294 ? -36.083 -19.197 26.389  1.00 60.46 ? 274 GLN A O     1 
ATOM   2096 C  CB    . GLN A 1 294 ? -36.584 -21.814 27.287  1.00 60.43 ? 274 GLN A CB    1 
ATOM   2097 C  CG    . GLN A 1 294 ? -35.993 -21.283 28.597  1.00 66.62 ? 274 GLN A CG    1 
ATOM   2098 C  CD    . GLN A 1 294 ? -34.913 -22.168 29.185  1.00 76.14 ? 274 GLN A CD    1 
ATOM   2099 O  OE1   . GLN A 1 294 ? -33.730 -22.033 28.874  1.00 73.64 ? 274 GLN A OE1   1 
ATOM   2100 N  NE2   . GLN A 1 294 ? -35.305 -23.067 30.076  1.00 78.20 ? 274 GLN A NE2   1 
ATOM   2101 N  N     . ALA A 1 295 ? -35.757 -19.885 24.273  1.00 43.61 ? 275 ALA A N     1 
ATOM   2102 C  CA    . ALA A 1 295 ? -35.729 -18.540 23.738  1.00 42.32 ? 275 ALA A CA    1 
ATOM   2103 C  C     . ALA A 1 295 ? -37.153 -17.994 23.659  1.00 42.37 ? 275 ALA A C     1 
ATOM   2104 O  O     . ALA A 1 295 ? -37.874 -18.239 22.691  1.00 40.61 ? 275 ALA A O     1 
ATOM   2105 C  CB    . ALA A 1 295 ? -35.066 -18.569 22.389  1.00 41.59 ? 275 ALA A CB    1 
ATOM   2106 N  N     . ASN A 1 296 ? -37.554 -17.213 24.658  1.00 38.84 ? 276 ASN A N     1 
ATOM   2107 C  CA    . ASN A 1 296 ? -38.884 -16.640 24.609  1.00 41.92 ? 276 ASN A CA    1 
ATOM   2108 C  C     . ASN A 1 296 ? -38.915 -15.551 23.527  1.00 41.14 ? 276 ASN A C     1 
ATOM   2109 O  O     . ASN A 1 296 ? -37.876 -15.012 23.116  1.00 37.62 ? 276 ASN A O     1 
ATOM   2110 C  CB    . ASN A 1 296 ? -39.338 -16.208 26.000  1.00 43.91 ? 276 ASN A CB    1 
ATOM   2111 C  CG    . ASN A 1 296 ? -38.464 -15.115 26.556  1.00 47.98 ? 276 ASN A CG    1 
ATOM   2112 O  OD1   . ASN A 1 296 ? -38.206 -14.131 25.866  1.00 46.54 ? 276 ASN A OD1   1 
ATOM   2113 N  ND2   . ASN A 1 296 ? -37.979 -15.300 27.773  1.00 50.31 ? 276 ASN A ND2   1 
ATOM   2114 N  N     . PRO A 1 297 ? -40.109 -15.208 22.999  1.00 34.53 ? 277 PRO A N     1 
ATOM   2115 C  CA    . PRO A 1 297 ? -40.220 -14.247 21.896  1.00 34.26 ? 277 PRO A CA    1 
ATOM   2116 C  C     . PRO A 1 297 ? -39.641 -12.853 22.161  1.00 29.53 ? 277 PRO A C     1 
ATOM   2117 O  O     . PRO A 1 297 ? -39.097 -12.227 21.249  1.00 32.73 ? 277 PRO A O     1 
ATOM   2118 C  CB    . PRO A 1 297 ? -41.737 -14.069 21.672  1.00 36.51 ? 277 PRO A CB    1 
ATOM   2119 C  CG    . PRO A 1 297 ? -42.431 -15.146 22.495  1.00 35.82 ? 277 PRO A CG    1 
ATOM   2120 C  CD    . PRO A 1 297 ? -41.416 -15.732 23.448  1.00 36.73 ? 277 PRO A CD    1 
ATOM   2121 N  N     . GLU A 1 298 ? -39.772 -12.394 23.410  1.00 26.23 ? 278 GLU A N     1 
ATOM   2122 C  CA    . GLU A 1 298 ? -39.325 -11.075 23.841  1.00 27.57 ? 278 GLU A CA    1 
ATOM   2123 C  C     . GLU A 1 298 ? -37.803 -10.963 23.665  1.00 25.03 ? 278 GLU A C     1 
ATOM   2124 O  O     . GLU A 1 298 ? -37.302 -9.915  23.277  1.00 19.49 ? 278 GLU A O     1 
ATOM   2125 C  CB    . GLU A 1 298 ? -39.674 -10.816 25.313  1.00 33.43 ? 278 GLU A CB    1 
ATOM   2126 C  CG    . GLU A 1 298 ? -41.155 -10.993 25.676  1.00 45.84 ? 278 GLU A CG    1 
ATOM   2127 C  CD    . GLU A 1 298 ? -41.713 -12.417 25.661  1.00 50.96 ? 278 GLU A CD    1 
ATOM   2128 O  OE1   . GLU A 1 298 ? -41.080 -13.321 26.274  1.00 52.95 ? 278 GLU A OE1   1 
ATOM   2129 O  OE2   . GLU A 1 298 ? -42.782 -12.634 25.030  1.00 58.92 ? 278 GLU A OE2   1 
ATOM   2130 N  N     . ASP A 1 299 ? -37.078 -12.042 23.980  1.00 22.41 ? 279 ASP A N     1 
ATOM   2131 C  CA    . ASP A 1 299 ? -35.626 -12.035 23.839  1.00 19.13 ? 279 ASP A CA    1 
ATOM   2132 C  C     . ASP A 1 299 ? -35.268 -11.948 22.364  1.00 17.16 ? 279 ASP A C     1 
ATOM   2133 O  O     . ASP A 1 299 ? -34.343 -11.225 21.985  1.00 17.77 ? 279 ASP A O     1 
ATOM   2134 C  CB    . ASP A 1 299 ? -34.987 -13.277 24.471  1.00 19.68 ? 279 ASP A CB    1 
ATOM   2135 C  CG    . ASP A 1 299 ? -34.943 -13.247 25.982  1.00 20.39 ? 279 ASP A CG    1 
ATOM   2136 O  OD1   . ASP A 1 299 ? -35.503 -12.324 26.573  1.00 22.97 ? 279 ASP A OD1   1 
ATOM   2137 O  OD2   . ASP A 1 299 ? -34.366 -14.167 26.569  1.00 24.10 ? 279 ASP A OD2   1 
ATOM   2138 N  N     . LEU A 1 300 ? -35.969 -12.720 21.528  1.00 17.56 ? 280 LEU A N     1 
ATOM   2139 C  CA    . LEU A 1 300 ? -35.603 -12.815 20.128  1.00 18.39 ? 280 LEU A CA    1 
ATOM   2140 C  C     . LEU A 1 300 ? -35.856 -11.457 19.488  1.00 17.65 ? 280 LEU A C     1 
ATOM   2141 O  O     . LEU A 1 300 ? -35.132 -11.067 18.585  1.00 15.81 ? 280 LEU A O     1 
ATOM   2142 C  CB    . LEU A 1 300 ? -36.418 -13.913 19.432  1.00 22.32 ? 280 LEU A CB    1 
ATOM   2143 C  CG    . LEU A 1 300 ? -36.053 -15.334 19.827  1.00 24.93 ? 280 LEU A CG    1 
ATOM   2144 C  CD1   . LEU A 1 300 ? -37.044 -16.319 19.222  1.00 29.83 ? 280 LEU A CD1   1 
ATOM   2145 C  CD2   . LEU A 1 300 ? -34.635 -15.672 19.423  1.00 27.92 ? 280 LEU A CD2   1 
ATOM   2146 N  N     . THR A 1 301 ? -36.906 -10.758 19.930  1.00 18.93 ? 281 THR A N     1 
ATOM   2147 C  CA    . THR A 1 301 ? -37.175 -9.412  19.430  1.00 20.19 ? 281 THR A CA    1 
ATOM   2148 C  C     . THR A 1 301 ? -36.000 -8.476  19.749  1.00 18.93 ? 281 THR A C     1 
ATOM   2149 O  O     . THR A 1 301 ? -35.571 -7.705  18.895  1.00 18.87 ? 281 THR A O     1 
ATOM   2150 C  CB    . THR A 1 301 ? -38.484 -8.867  20.022  1.00 24.03 ? 281 THR A CB    1 
ATOM   2151 O  OG1   . THR A 1 301 ? -39.441 -9.696  19.391  1.00 25.13 ? 281 THR A OG1   1 
ATOM   2152 C  CG2   . THR A 1 301 ? -38.743 -7.409  19.726  1.00 26.92 ? 281 THR A CG2   1 
ATOM   2153 N  N     . GLN A 1 302 ? -35.479 -8.606  20.961  1.00 18.51 ? 282 GLN A N     1 
ATOM   2154 C  CA    . GLN A 1 302 ? -34.365 -7.756  21.405  1.00 19.29 ? 282 GLN A CA    1 
ATOM   2155 C  C     . GLN A 1 302 ? -33.077 -8.078  20.619  1.00 15.72 ? 282 GLN A C     1 
ATOM   2156 O  O     . GLN A 1 302 ? -32.337 -7.169  20.187  1.00 14.95 ? 282 GLN A O     1 
ATOM   2157 C  CB    . GLN A 1 302 ? -34.226 -7.883  22.918  1.00 22.20 ? 282 GLN A CB    1 
ATOM   2158 C  CG    . GLN A 1 302 ? -33.319 -6.838  23.552  1.00 29.67 ? 282 GLN A CG    1 
ATOM   2159 C  CD    . GLN A 1 302 ? -34.001 -5.496  23.737  1.00 32.09 ? 282 GLN A CD    1 
ATOM   2160 O  OE1   . GLN A 1 302 ? -35.055 -5.429  24.375  1.00 31.84 ? 282 GLN A OE1   1 
ATOM   2161 N  NE2   . GLN A 1 302 ? -33.390 -4.441  23.203  1.00 29.78 ? 282 GLN A NE2   1 
ATOM   2162 N  N     . ILE A 1 303 ? -32.857 -9.366  20.364  1.00 13.94 ? 283 ILE A N     1 
ATOM   2163 C  CA    . ILE A 1 303 ? -31.662 -9.821  19.645  1.00 12.54 ? 283 ILE A CA    1 
ATOM   2164 C  C     . ILE A 1 303 ? -31.642 -9.264  18.229  1.00 15.98 ? 283 ILE A C     1 
ATOM   2165 O  O     . ILE A 1 303 ? -30.591 -8.899  17.681  1.00 15.47 ? 283 ILE A O     1 
ATOM   2166 C  CB    . ILE A 1 303 ? -31.578 -11.355 19.705  1.00 12.68 ? 283 ILE A CB    1 
ATOM   2167 C  CG1   . ILE A 1 303 ? -31.327 -11.804 21.159  1.00 12.42 ? 283 ILE A CG1   1 
ATOM   2168 C  CG2   . ILE A 1 303 ? -30.611 -11.920 18.692  1.00 12.49 ? 283 ILE A CG2   1 
ATOM   2169 C  CD1   . ILE A 1 303 ? -31.394 -13.262 21.400  1.00 14.38 ? 283 ILE A CD1   1 
ATOM   2170 N  N     . ALA A 1 304 ? -32.842 -9.134  17.626  1.00 13.38 ? 284 ALA A N     1 
ATOM   2171 C  CA    . ALA A 1 304 ? -32.963 -8.796  16.216  1.00 15.47 ? 284 ALA A CA    1 
ATOM   2172 C  C     . ALA A 1 304 ? -33.038 -7.291  15.971  1.00 18.69 ? 284 ALA A C     1 
ATOM   2173 O  O     . ALA A 1 304 ? -33.503 -6.902  14.900  1.00 18.40 ? 284 ALA A O     1 
ATOM   2174 C  CB    . ALA A 1 304 ? -34.154 -9.495  15.605  1.00 16.57 ? 284 ALA A CB    1 
ATOM   2175 N  N     . ALA A 1 305 ? -32.507 -6.475  16.892  1.00 19.37 ? 285 ALA A N     1 
ATOM   2176 C  CA    . ALA A 1 305 ? -32.379 -5.033  16.650  1.00 21.62 ? 285 ALA A CA    1 
ATOM   2177 C  C     . ALA A 1 305 ? -31.679 -4.779  15.309  1.00 21.88 ? 285 ALA A C     1 
ATOM   2178 O  O     . ALA A 1 305 ? -30.806 -5.550  14.869  1.00 19.99 ? 285 ALA A O     1 
ATOM   2179 C  CB    . ALA A 1 305 ? -31.691 -4.391  17.816  1.00 23.79 ? 285 ALA A CB    1 
ATOM   2180 N  N     . PRO A 1 306 ? -32.147 -3.783  14.508  1.00 20.25 ? 286 PRO A N     1 
ATOM   2181 C  CA    . PRO A 1 306 ? -31.592 -3.556  13.172  1.00 19.25 ? 286 PRO A CA    1 
ATOM   2182 C  C     . PRO A 1 306 ? -30.127 -3.171  13.349  1.00 16.95 ? 286 PRO A C     1 
ATOM   2183 O  O     . PRO A 1 306 ? -29.847 -2.407  14.249  1.00 16.79 ? 286 PRO A O     1 
ATOM   2184 C  CB    . PRO A 1 306 ? -32.440 -2.407  12.582  1.00 23.31 ? 286 PRO A CB    1 
ATOM   2185 C  CG    . PRO A 1 306 ? -33.111 -1.774  13.798  1.00 25.03 ? 286 PRO A CG    1 
ATOM   2186 C  CD    . PRO A 1 306 ? -33.277 -2.886  14.820  1.00 28.90 ? 286 PRO A CD    1 
ATOM   2187 N  N     . LEU A 1 307 ? -29.266 -3.737  12.506  1.00 14.96 ? 287 LEU A N     1 
ATOM   2188 C  CA    . LEU A 1 307 ? -27.858 -3.390  12.587  1.00 17.28 ? 287 LEU A CA    1 
ATOM   2189 C  C     . LEU A 1 307 ? -27.588 -2.314  11.550  1.00 16.36 ? 287 LEU A C     1 
ATOM   2190 O  O     . LEU A 1 307 ? -28.001 -2.414  10.399  1.00 15.42 ? 287 LEU A O     1 
ATOM   2191 C  CB    . LEU A 1 307 ? -26.994 -4.597  12.244  1.00 17.95 ? 287 LEU A CB    1 
ATOM   2192 C  CG    . LEU A 1 307 ? -27.080 -5.847  13.130  1.00 21.05 ? 287 LEU A CG    1 
ATOM   2193 C  CD1   . LEU A 1 307 ? -26.125 -6.878  12.567  1.00 22.07 ? 287 LEU A CD1   1 
ATOM   2194 C  CD2   . LEU A 1 307 ? -26.764 -5.562  14.575  1.00 22.70 ? 287 LEU A CD2   1 
ATOM   2195 N  N     . ASP A 1 308 ? -26.701 -1.385  11.887  1.00 12.38 ? 288 ASP A N     1 
ATOM   2196 C  CA    . ASP A 1 308 ? -26.208 -0.454  10.886  1.00 11.58 ? 288 ASP A CA    1 
ATOM   2197 C  C     . ASP A 1 308 ? -25.195 -1.077  9.949   1.00 11.34 ? 288 ASP A C     1 
ATOM   2198 O  O     . ASP A 1 308 ? -24.929 -0.544  8.871   1.00 13.08 ? 288 ASP A O     1 
ATOM   2199 C  CB    . ASP A 1 308 ? -25.676 0.786   11.617  1.00 11.90 ? 288 ASP A CB    1 
ATOM   2200 C  CG    . ASP A 1 308 ? -26.743 1.476   12.410  1.00 12.47 ? 288 ASP A CG    1 
ATOM   2201 O  OD1   . ASP A 1 308 ? -27.819 1.818   11.776  1.00 14.44 ? 288 ASP A OD1   1 
ATOM   2202 O  OD2   . ASP A 1 308 ? -26.581 1.666   13.637  1.00 11.32 ? 288 ASP A OD2   1 
ATOM   2203 N  N     . TRP A 1 309 ? -24.521 -2.144  10.404  1.00 11.03 ? 289 TRP A N     1 
ATOM   2204 C  CA    . TRP A 1 309 ? -23.532 -2.845  9.620   1.00 9.14  ? 289 TRP A CA    1 
ATOM   2205 C  C     . TRP A 1 309 ? -23.278 -4.201  10.274  1.00 8.38  ? 289 TRP A C     1 
ATOM   2206 O  O     . TRP A 1 309 ? -23.643 -4.389  11.428  1.00 10.39 ? 289 TRP A O     1 
ATOM   2207 C  CB    . TRP A 1 309 ? -22.242 -2.044  9.412   1.00 9.10  ? 289 TRP A CB    1 
ATOM   2208 C  CG    . TRP A 1 309 ? -21.556 -1.658  10.684  1.00 9.41  ? 289 TRP A CG    1 
ATOM   2209 C  CD1   . TRP A 1 309 ? -21.791 -0.557  11.457  1.00 10.25 ? 289 TRP A CD1   1 
ATOM   2210 C  CD2   . TRP A 1 309 ? -20.480 -2.363  11.333  1.00 10.95 ? 289 TRP A CD2   1 
ATOM   2211 N  NE1   . TRP A 1 309 ? -20.945 -0.521  12.540  1.00 11.04 ? 289 TRP A NE1   1 
ATOM   2212 C  CE2   . TRP A 1 309 ? -20.106 -1.590  12.469  1.00 10.27 ? 289 TRP A CE2   1 
ATOM   2213 C  CE3   . TRP A 1 309 ? -19.773 -3.530  11.044  1.00 11.48 ? 289 TRP A CE3   1 
ATOM   2214 C  CZ2   . TRP A 1 309 ? -19.121 -2.012  13.336  1.00 11.29 ? 289 TRP A CZ2   1 
ATOM   2215 C  CZ3   . TRP A 1 309 ? -18.752 -3.923  11.879  1.00 13.34 ? 289 TRP A CZ3   1 
ATOM   2216 C  CH2   . TRP A 1 309 ? -18.443 -3.168  13.022  1.00 12.58 ? 289 TRP A CH2   1 
ATOM   2217 N  N     . LEU A 1 310 ? -22.790 -5.139  9.485   1.00 8.83  ? 290 LEU A N     1 
ATOM   2218 C  CA    . LEU A 1 310 ? -22.295 -6.425  9.989   1.00 9.58  ? 290 LEU A CA    1 
ATOM   2219 C  C     . LEU A 1 310 ? -20.853 -6.602  9.607   1.00 9.27  ? 290 LEU A C     1 
ATOM   2220 O  O     . LEU A 1 310 ? -20.427 -6.342  8.469   1.00 8.89  ? 290 LEU A O     1 
ATOM   2221 C  CB    . LEU A 1 310 ? -23.129 -7.569  9.393   1.00 10.83 ? 290 LEU A CB    1 
ATOM   2222 C  CG    . LEU A 1 310 ? -22.614 -8.977  9.682   1.00 11.52 ? 290 LEU A CG    1 
ATOM   2223 C  CD1   . LEU A 1 310 ? -22.908 -9.309  11.086  1.00 11.83 ? 290 LEU A CD1   1 
ATOM   2224 C  CD2   . LEU A 1 310 ? -23.288 -9.985  8.771   1.00 14.45 ? 290 LEU A CD2   1 
ATOM   2225 N  N     . GLY A 1 311 ? -20.023 -7.053  10.583  1.00 8.01  ? 291 GLY A N     1 
ATOM   2226 C  CA    . GLY A 1 311 ? -18.646 -7.353  10.340  1.00 8.00  ? 291 GLY A CA    1 
ATOM   2227 C  C     . GLY A 1 311 ? -18.437 -8.855  10.223  1.00 7.57  ? 291 GLY A C     1 
ATOM   2228 O  O     . GLY A 1 311 ? -19.034 -9.618  10.998  1.00 8.16  ? 291 GLY A O     1 
ATOM   2229 N  N     . VAL A 1 312 ? -17.584 -9.232  9.271   1.00 8.41  ? 292 VAL A N     1 
ATOM   2230 C  CA    . VAL A 1 312 ? -17.265 -10.610 8.989   1.00 8.45  ? 292 VAL A CA    1 
ATOM   2231 C  C     . VAL A 1 312 ? -15.807 -10.835 9.263   1.00 8.28  ? 292 VAL A C     1 
ATOM   2232 O  O     . VAL A 1 312 ? -14.984 -10.123 8.700   1.00 8.06  ? 292 VAL A O     1 
ATOM   2233 C  CB    . VAL A 1 312 ? -17.564 -10.948 7.524   1.00 11.17 ? 292 VAL A CB    1 
ATOM   2234 C  CG1   . VAL A 1 312 ? -17.127 -12.376 7.208   1.00 12.45 ? 292 VAL A CG1   1 
ATOM   2235 C  CG2   . VAL A 1 312 ? -19.025 -10.682 7.240   1.00 12.61 ? 292 VAL A CG2   1 
ATOM   2236 N  N     . ASN A 1 313 ? -15.526 -11.819 10.123  1.00 7.89  ? 293 ASN A N     1 
ATOM   2237 C  CA    . ASN A 1 313 ? -14.182 -12.289 10.351  1.00 7.47  ? 293 ASN A CA    1 
ATOM   2238 C  C     . ASN A 1 313 ? -14.013 -13.608 9.589   1.00 9.27  ? 293 ASN A C     1 
ATOM   2239 O  O     . ASN A 1 313 ? -14.784 -14.500 9.833   1.00 10.23 ? 293 ASN A O     1 
ATOM   2240 C  CB    . ASN A 1 313 ? -13.935 -12.462 11.841  1.00 7.88  ? 293 ASN A CB    1 
ATOM   2241 C  CG    . ASN A 1 313 ? -13.897 -11.151 12.601  1.00 7.43  ? 293 ASN A CG    1 
ATOM   2242 O  OD1   . ASN A 1 313 ? -13.997 -10.077 12.025  1.00 7.52  ? 293 ASN A OD1   1 
ATOM   2243 N  ND2   . ASN A 1 313 ? -13.671 -11.240 13.890  1.00 7.84  ? 293 ASN A ND2   1 
ATOM   2244 N  N     . TYR A 1 314 ? -13.080 -13.680 8.659   1.00 7.85  ? 294 TYR A N     1 
ATOM   2245 C  CA    . TYR A 1 314 ? -12.913 -14.809 7.726   1.00 8.57  ? 294 TYR A CA    1 
ATOM   2246 C  C     . TYR A 1 314 ? -11.459 -15.258 7.733   1.00 9.92  ? 294 TYR A C     1 
ATOM   2247 O  O     . TYR A 1 314 ? -10.563 -14.446 7.485   1.00 8.79  ? 294 TYR A O     1 
ATOM   2248 C  CB    . TYR A 1 314 ? -13.344 -14.463 6.282   1.00 9.00  ? 294 TYR A CB    1 
ATOM   2249 C  CG    . TYR A 1 314 ? -13.084 -15.631 5.356   1.00 9.89  ? 294 TYR A CG    1 
ATOM   2250 C  CD1   . TYR A 1 314 ? -13.912 -16.759 5.397   1.00 11.03 ? 294 TYR A CD1   1 
ATOM   2251 C  CD2   . TYR A 1 314 ? -11.981 -15.673 4.516   1.00 9.90  ? 294 TYR A CD2   1 
ATOM   2252 C  CE1   . TYR A 1 314 ? -13.620 -17.878 4.636   1.00 10.77 ? 294 TYR A CE1   1 
ATOM   2253 C  CE2   . TYR A 1 314 ? -11.681 -16.800 3.758   1.00 10.78 ? 294 TYR A CE2   1 
ATOM   2254 C  CZ    . TYR A 1 314 ? -12.509 -17.905 3.817   1.00 10.31 ? 294 TYR A CZ    1 
ATOM   2255 O  OH    . TYR A 1 314 ? -12.144 -19.048 3.076   1.00 10.77 ? 294 TYR A OH    1 
ATOM   2256 N  N     . TYR A 1 315 ? -11.238 -16.570 8.017   1.00 9.74  ? 295 TYR A N     1 
ATOM   2257 C  CA    . TYR A 1 315 ? -9.912  -17.165 7.935   1.00 10.93 ? 295 TYR A CA    1 
ATOM   2258 C  C     . TYR A 1 315 ? -9.882  -18.386 7.024   1.00 12.34 ? 295 TYR A C     1 
ATOM   2259 O  O     . TYR A 1 315 ? -8.921  -18.539 6.277   1.00 14.18 ? 295 TYR A O     1 
ATOM   2260 C  CB    . TYR A 1 315 ? -9.408  -17.546 9.327   1.00 10.61 ? 295 TYR A CB    1 
ATOM   2261 C  CG    . TYR A 1 315 ? -9.150  -16.348 10.206  1.00 10.73 ? 295 TYR A CG    1 
ATOM   2262 C  CD1   . TYR A 1 315 ? -10.150 -15.806 10.963  1.00 10.15 ? 295 TYR A CD1   1 
ATOM   2263 C  CD2   . TYR A 1 315 ? -7.891  -15.759 10.266  1.00 10.51 ? 295 TYR A CD2   1 
ATOM   2264 C  CE1   . TYR A 1 315 ? -9.960  -14.658 11.708  1.00 10.12 ? 295 TYR A CE1   1 
ATOM   2265 C  CE2   . TYR A 1 315 ? -7.680  -14.614 11.018  1.00 10.90 ? 295 TYR A CE2   1 
ATOM   2266 C  CZ    . TYR A 1 315 ? -8.708  -14.105 11.789  1.00 9.91  ? 295 TYR A CZ    1 
ATOM   2267 O  OH    . TYR A 1 315 ? -8.510  -12.997 12.563  1.00 10.09 ? 295 TYR A OH    1 
ATOM   2268 N  N     . GLU A 1 316 ? -10.944 -19.196 7.061   1.00 13.32 ? 296 GLU A N     1 
ATOM   2269 C  CA    . GLU A 1 316 ? -10.844 -20.530 6.477   1.00 11.73 ? 296 GLU A CA    1 
ATOM   2270 C  C     . GLU A 1 316 ? -12.236 -21.026 6.118   1.00 10.89 ? 296 GLU A C     1 
ATOM   2271 O  O     . GLU A 1 316 ? -13.221 -20.564 6.667   1.00 12.63 ? 296 GLU A O     1 
ATOM   2272 C  CB    . GLU A 1 316 ? -10.203 -21.525 7.469   1.00 12.06 ? 296 GLU A CB    1 
ATOM   2273 C  CG    . GLU A 1 316 ? -10.983 -21.684 8.757   1.00 13.27 ? 296 GLU A CG    1 
ATOM   2274 C  CD    . GLU A 1 316 ? -10.351 -22.563 9.818   1.00 15.28 ? 296 GLU A CD    1 
ATOM   2275 O  OE1   . GLU A 1 316 ? -11.120 -22.967 10.758  1.00 19.66 ? 296 GLU A OE1   1 
ATOM   2276 O  OE2   . GLU A 1 316 ? -9.093  -22.795 9.747   1.00 15.08 ? 296 GLU A OE2   1 
ATOM   2277 N  N     . ARG A 1 317 ? -12.263 -22.088 5.284   1.00 12.06 ? 297 ARG A N     1 
ATOM   2278 C  CA    . ARG A 1 317 ? -13.505 -22.814 5.083   1.00 12.59 ? 297 ARG A CA    1 
ATOM   2279 C  C     . ARG A 1 317 ? -13.482 -24.077 5.945   1.00 13.01 ? 297 ARG A C     1 
ATOM   2280 O  O     . ARG A 1 317 ? -12.492 -24.419 6.587   1.00 12.67 ? 297 ARG A O     1 
ATOM   2281 C  CB    . ARG A 1 317 ? -13.678 -23.230 3.622   1.00 12.20 ? 297 ARG A CB    1 
ATOM   2282 C  CG    . ARG A 1 317 ? -12.606 -24.190 3.203   1.00 13.25 ? 297 ARG A CG    1 
ATOM   2283 C  CD    . ARG A 1 317 ? -13.040 -24.992 1.982   1.00 15.66 ? 297 ARG A CD    1 
ATOM   2284 N  NE    . ARG A 1 317 ? -11.973 -25.889 1.715   1.00 18.54 ? 297 ARG A NE    1 
ATOM   2285 C  CZ    . ARG A 1 317 ? -11.961 -26.743 0.693   1.00 22.55 ? 297 ARG A CZ    1 
ATOM   2286 N  NH1   . ARG A 1 317 ? -12.844 -26.596 -0.255  1.00 24.32 ? 297 ARG A NH1   1 
ATOM   2287 N  NH2   . ARG A 1 317 ? -11.079 -27.715 0.629   1.00 23.68 ? 297 ARG A NH2   1 
ATOM   2288 N  N     . MET A 1 318 ? -14.595 -24.805 5.925   1.00 12.52 ? 298 MET A N     1 
ATOM   2289 C  CA    . MET A 1 318 ? -14.631 -26.137 6.510   1.00 13.06 ? 298 MET A CA    1 
ATOM   2290 C  C     . MET A 1 318 ? -15.122 -27.069 5.400   1.00 13.03 ? 298 MET A C     1 
ATOM   2291 O  O     . MET A 1 318 ? -16.240 -26.910 4.936   1.00 12.84 ? 298 MET A O     1 
ATOM   2292 C  CB    . MET A 1 318 ? -15.614 -26.180 7.682   1.00 13.28 ? 298 MET A CB    1 
ATOM   2293 C  CG    . MET A 1 318 ? -15.972 -27.576 8.238   1.00 16.91 ? 298 MET A CG    1 
ATOM   2294 S  SD    . MET A 1 318 ? -14.530 -28.402 8.936   1.00 21.56 ? 298 MET A SD    1 
ATOM   2295 C  CE    . MET A 1 318 ? -15.408 -29.649 9.893   1.00 24.04 ? 298 MET A CE    1 
ATOM   2296 N  N     . ARG A 1 319 ? -14.260 -27.974 4.970   1.00 14.49 ? 299 ARG A N     1 
ATOM   2297 C  CA    . ARG A 1 319 ? -14.709 -29.061 4.103   1.00 14.42 ? 299 ARG A CA    1 
ATOM   2298 C  C     . ARG A 1 319 ? -15.028 -30.288 4.954   1.00 14.08 ? 299 ARG A C     1 
ATOM   2299 O  O     . ARG A 1 319 ? -14.105 -30.847 5.529   1.00 14.90 ? 299 ARG A O     1 
ATOM   2300 C  CB    . ARG A 1 319 ? -13.618 -29.428 3.115   1.00 16.22 ? 299 ARG A CB    1 
ATOM   2301 C  CG    . ARG A 1 319 ? -14.079 -30.457 2.094   1.00 19.81 ? 299 ARG A CG    1 
ATOM   2302 C  CD    . ARG A 1 319 ? -13.203 -30.413 0.879   1.00 25.31 ? 299 ARG A CD    1 
ATOM   2303 N  NE    . ARG A 1 319 ? -11.998 -31.147 1.153   1.00 34.23 ? 299 ARG A NE    1 
ATOM   2304 C  CZ    . ARG A 1 319 ? -11.694 -32.294 0.559   1.00 39.24 ? 299 ARG A CZ    1 
ATOM   2305 N  NH1   . ARG A 1 319 ? -12.553 -32.856 -0.269  1.00 43.44 ? 299 ARG A NH1   1 
ATOM   2306 N  NH2   . ARG A 1 319 ? -10.534 -32.870 0.804   1.00 37.64 ? 299 ARG A NH2   1 
ATOM   2307 N  N     . ALA A 1 320 ? -16.322 -30.634 5.064   1.00 14.01 ? 300 ALA A N     1 
ATOM   2308 C  CA    . ALA A 1 320 ? -16.892 -31.481 6.108   1.00 13.28 ? 300 ALA A CA    1 
ATOM   2309 C  C     . ALA A 1 320 ? -17.174 -32.907 5.625   1.00 15.69 ? 300 ALA A C     1 
ATOM   2310 O  O     . ALA A 1 320 ? -17.720 -33.121 4.535   1.00 13.89 ? 300 ALA A O     1 
ATOM   2311 C  CB    . ALA A 1 320 ? -18.152 -30.844 6.631   1.00 14.63 ? 300 ALA A CB    1 
ATOM   2312 N  N     . VAL A 1 321 ? -16.818 -33.862 6.487   1.00 14.48 ? 301 VAL A N     1 
ATOM   2313 C  CA    . VAL A 1 321 ? -17.276 -35.239 6.412   1.00 16.17 ? 301 VAL A CA    1 
ATOM   2314 C  C     . VAL A 1 321 ? -17.996 -35.552 7.705   1.00 15.70 ? 301 VAL A C     1 
ATOM   2315 O  O     . VAL A 1 321 ? -17.754 -34.945 8.742   1.00 15.13 ? 301 VAL A O     1 
ATOM   2316 C  CB    . VAL A 1 321 ? -16.147 -36.255 6.181   1.00 19.82 ? 301 VAL A CB    1 
ATOM   2317 C  CG1   . VAL A 1 321 ? -15.650 -36.197 4.752   1.00 24.13 ? 301 VAL A CG1   1 
ATOM   2318 C  CG2   . VAL A 1 321 ? -15.023 -36.115 7.187   1.00 20.81 ? 301 VAL A CG2   1 
ATOM   2319 N  N     . ASP A 1 322 ? -18.966 -36.463 7.597   1.00 13.93 ? 302 ASP A N     1 
ATOM   2320 C  CA    . ASP A 1 322 ? -19.680 -36.951 8.755   1.00 15.24 ? 302 ASP A CA    1 
ATOM   2321 C  C     . ASP A 1 322 ? -18.707 -37.568 9.769   1.00 15.82 ? 302 ASP A C     1 
ATOM   2322 O  O     . ASP A 1 322 ? -17.766 -38.261 9.393   1.00 16.19 ? 302 ASP A O     1 
ATOM   2323 C  CB    . ASP A 1 322 ? -20.678 -38.006 8.281   1.00 16.55 ? 302 ASP A CB    1 
ATOM   2324 C  CG    . ASP A 1 322 ? -21.718 -38.402 9.316   1.00 18.40 ? 302 ASP A CG    1 
ATOM   2325 O  OD1   . ASP A 1 322 ? -21.984 -37.617 10.247  1.00 19.93 ? 302 ASP A OD1   1 
ATOM   2326 O  OD2   . ASP A 1 322 ? -22.253 -39.531 9.171   1.00 20.65 ? 302 ASP A OD2   1 
ATOM   2327 N  N     . ALA A 1 323 ? -18.971 -37.333 11.056  1.00 17.56 ? 303 ALA A N     1 
ATOM   2328 C  CA    . ALA A 1 323 ? -18.176 -37.924 12.133  1.00 18.10 ? 303 ALA A CA    1 
ATOM   2329 C  C     . ALA A 1 323 ? -19.115 -38.323 13.256  1.00 17.80 ? 303 ALA A C     1 
ATOM   2330 O  O     . ALA A 1 323 ? -19.256 -37.611 14.269  1.00 17.54 ? 303 ALA A O     1 
ATOM   2331 C  CB    . ALA A 1 323 ? -17.153 -36.930 12.588  1.00 19.67 ? 303 ALA A CB    1 
ATOM   2332 N  N     . PRO A 1 324 ? -19.813 -39.459 13.081  1.00 20.02 ? 304 PRO A N     1 
ATOM   2333 C  CA    . PRO A 1 324 ? -20.884 -39.838 13.996  1.00 23.02 ? 304 PRO A CA    1 
ATOM   2334 C  C     . PRO A 1 324 ? -20.388 -39.992 15.425  1.00 23.15 ? 304 PRO A C     1 
ATOM   2335 O  O     . PRO A 1 324 ? -21.133 -39.753 16.352  1.00 26.92 ? 304 PRO A O     1 
ATOM   2336 C  CB    . PRO A 1 324 ? -21.431 -41.155 13.426  1.00 23.23 ? 304 PRO A CB    1 
ATOM   2337 C  CG    . PRO A 1 324 ? -20.956 -41.195 11.997  1.00 24.28 ? 304 PRO A CG    1 
ATOM   2338 C  CD    . PRO A 1 324 ? -19.668 -40.396 11.950  1.00 21.06 ? 304 PRO A CD    1 
ATOM   2339 N  N     . ASP A 1 325 ? -19.093 -40.277 15.594  1.00 27.52 ? 305 ASP A N     1 
ATOM   2340 C  CA    . ASP A 1 325 ? -18.576 -40.622 16.911  1.00 31.69 ? 305 ASP A CA    1 
ATOM   2341 C  C     . ASP A 1 325 ? -18.007 -39.389 17.612  1.00 33.76 ? 305 ASP A C     1 
ATOM   2342 O  O     . ASP A 1 325 ? -17.618 -39.474 18.775  1.00 30.78 ? 305 ASP A O     1 
ATOM   2343 C  CB    . ASP A 1 325 ? -17.532 -41.744 16.814  1.00 35.73 ? 305 ASP A CB    1 
ATOM   2344 C  CG    . ASP A 1 325 ? -18.128 -43.093 16.442  1.00 40.00 ? 305 ASP A CG    1 
ATOM   2345 O  OD1   . ASP A 1 325 ? -19.350 -43.295 16.682  1.00 42.43 ? 305 ASP A OD1   1 
ATOM   2346 O  OD2   . ASP A 1 325 ? -17.375 -43.930 15.881  1.00 48.00 ? 305 ASP A OD2   1 
ATOM   2347 N  N     . ALA A 1 326 ? -17.940 -38.249 16.910  1.00 27.48 ? 306 ALA A N     1 
ATOM   2348 C  CA    . ALA A 1 326 ? -17.352 -37.049 17.474  1.00 25.96 ? 306 ALA A CA    1 
ATOM   2349 C  C     . ALA A 1 326 ? -18.400 -36.282 18.277  1.00 24.98 ? 306 ALA A C     1 
ATOM   2350 O  O     . ALA A 1 326 ? -19.593 -36.544 18.186  1.00 25.66 ? 306 ALA A O     1 
ATOM   2351 C  CB    . ALA A 1 326 ? -16.736 -36.224 16.372  1.00 27.40 ? 306 ALA A CB    1 
ATOM   2352 N  N     . SER A 1 327 ? -17.930 -35.312 19.060  1.00 25.12 ? 307 SER A N     1 
ATOM   2353 C  CA    . SER A 1 327 ? -18.791 -34.334 19.697  1.00 27.13 ? 307 SER A CA    1 
ATOM   2354 C  C     . SER A 1 327 ? -19.632 -33.618 18.641  1.00 21.96 ? 307 SER A C     1 
ATOM   2355 O  O     . SER A 1 327 ? -19.212 -33.417 17.508  1.00 22.47 ? 307 SER A O     1 
ATOM   2356 C  CB    . SER A 1 327 ? -17.972 -33.340 20.464  1.00 29.73 ? 307 SER A CB    1 
ATOM   2357 O  OG    . SER A 1 327 ? -17.014 -34.013 21.268  1.00 32.26 ? 307 SER A OG    1 
ATOM   2358 N  N     . LEU A 1 328 ? -20.826 -33.249 19.056  1.00 22.39 ? 308 LEU A N     1 
ATOM   2359 C  CA    . LEU A 1 328 ? -21.675 -32.368 18.290  1.00 22.02 ? 308 LEU A CA    1 
ATOM   2360 C  C     . LEU A 1 328 ? -20.839 -31.181 17.793  1.00 20.46 ? 308 LEU A C     1 
ATOM   2361 O  O     . LEU A 1 328 ? -19.964 -30.663 18.482  1.00 19.57 ? 308 LEU A O     1 
ATOM   2362 C  CB    . LEU A 1 328 ? -22.782 -32.107 19.304  1.00 26.71 ? 308 LEU A CB    1 
ATOM   2363 C  CG    . LEU A 1 328 ? -23.891 -31.152 18.970  1.00 32.12 ? 308 LEU A CG    1 
ATOM   2364 C  CD1   . LEU A 1 328 ? -25.177 -31.621 19.677  1.00 30.09 ? 308 LEU A CD1   1 
ATOM   2365 C  CD2   . LEU A 1 328 ? -23.465 -29.750 19.400  1.00 39.84 ? 308 LEU A CD2   1 
ATOM   2366 N  N     . PRO A 1 329 ? -20.930 -30.747 16.509  1.00 16.97 ? 309 PRO A N     1 
ATOM   2367 C  CA    . PRO A 1 329 ? -21.958 -31.196 15.558  1.00 16.92 ? 309 PRO A CA    1 
ATOM   2368 C  C     . PRO A 1 329 ? -21.630 -32.381 14.642  1.00 16.61 ? 309 PRO A C     1 
ATOM   2369 O  O     . PRO A 1 329 ? -22.167 -32.482 13.537  1.00 14.49 ? 309 PRO A O     1 
ATOM   2370 C  CB    . PRO A 1 329 ? -22.095 -29.893 14.741  1.00 15.44 ? 309 PRO A CB    1 
ATOM   2371 C  CG    . PRO A 1 329 ? -20.676 -29.406 14.597  1.00 17.38 ? 309 PRO A CG    1 
ATOM   2372 C  CD    . PRO A 1 329 ? -20.077 -29.686 15.949  1.00 17.29 ? 309 PRO A CD    1 
ATOM   2373 N  N     . GLN A 1 330 ? -20.735 -33.273 15.070  1.00 15.50 ? 310 GLN A N     1 
ATOM   2374 C  CA    . GLN A 1 330 ? -20.509 -34.536 14.397  1.00 15.65 ? 310 GLN A CA    1 
ATOM   2375 C  C     . GLN A 1 330 ? -20.055 -34.295 12.959  1.00 16.05 ? 310 GLN A C     1 
ATOM   2376 O  O     . GLN A 1 330 ? -20.586 -34.876 12.013  1.00 15.39 ? 310 GLN A O     1 
ATOM   2377 C  CB    . GLN A 1 330 ? -21.771 -35.389 14.532  1.00 17.00 ? 310 GLN A CB    1 
ATOM   2378 C  CG    . GLN A 1 330 ? -22.015 -35.861 15.961  1.00 17.57 ? 310 GLN A CG    1 
ATOM   2379 C  CD    . GLN A 1 330 ? -23.315 -36.601 16.046  1.00 20.75 ? 310 GLN A CD    1 
ATOM   2380 O  OE1   . GLN A 1 330 ? -23.335 -37.821 16.242  1.00 25.48 ? 310 GLN A OE1   1 
ATOM   2381 N  NE2   . GLN A 1 330 ? -24.405 -35.868 15.929  1.00 17.97 ? 310 GLN A NE2   1 
ATOM   2382 N  N     . ALA A 1 331 ? -19.068 -33.409 12.804  1.00 16.31 ? 311 ALA A N     1 
ATOM   2383 C  CA    . ALA A 1 331 ? -18.505 -33.080 11.510  1.00 18.70 ? 311 ALA A CA    1 
ATOM   2384 C  C     . ALA A 1 331 ? -17.000 -33.010 11.671  1.00 19.77 ? 311 ALA A C     1 
ATOM   2385 O  O     . ALA A 1 331 ? -16.510 -32.452 12.638  1.00 25.11 ? 311 ALA A O     1 
ATOM   2386 C  CB    . ALA A 1 331 ? -19.032 -31.774 11.010  1.00 18.20 ? 311 ALA A CB    1 
ATOM   2387 N  N     . GLN A 1 332 ? -16.273 -33.574 10.742  1.00 17.40 ? 312 GLN A N     1 
ATOM   2388 C  CA    . GLN A 1 332 ? -14.823 -33.481 10.797  1.00 21.50 ? 312 GLN A CA    1 
ATOM   2389 C  C     . GLN A 1 332 ? -14.302 -32.797 9.545   1.00 21.02 ? 312 GLN A C     1 
ATOM   2390 O  O     . GLN A 1 332 ? -14.906 -32.857 8.468   1.00 18.01 ? 312 GLN A O     1 
ATOM   2391 C  CB    . GLN A 1 332 ? -14.182 -34.856 10.835  1.00 27.99 ? 312 GLN A CB    1 
ATOM   2392 C  CG    . GLN A 1 332 ? -14.068 -35.440 12.232  1.00 37.05 ? 312 GLN A CG    1 
ATOM   2393 C  CD    . GLN A 1 332 ? -13.350 -36.765 12.141  1.00 43.14 ? 312 GLN A CD    1 
ATOM   2394 O  OE1   . GLN A 1 332 ? -12.841 -37.145 11.079  1.00 45.14 ? 312 GLN A OE1   1 
ATOM   2395 N  NE2   . GLN A 1 332 ? -13.303 -37.471 13.259  1.00 46.10 ? 312 GLN A NE2   1 
ATOM   2396 N  N     . ARG A 1 333 ? -13.149 -32.151 9.706   1.00 20.15 ? 313 ARG A N     1 
ATOM   2397 C  CA    . ARG A 1 333 ? -12.526 -31.435 8.610   1.00 22.00 ? 313 ARG A CA    1 
ATOM   2398 C  C     . ARG A 1 333 ? -11.808 -32.451 7.742   1.00 21.59 ? 313 ARG A C     1 
ATOM   2399 O  O     . ARG A 1 333 ? -11.121 -33.302 8.289   1.00 21.88 ? 313 ARG A O     1 
ATOM   2400 C  CB    . ARG A 1 333 ? -11.551 -30.395 9.182   1.00 26.72 ? 313 ARG A CB    1 
ATOM   2401 C  CG    . ARG A 1 333 ? -10.552 -29.840 8.179   1.00 33.14 ? 313 ARG A CG    1 
ATOM   2402 C  CD    . ARG A 1 333 ? -9.775  -28.654 8.736   1.00 35.64 ? 313 ARG A CD    1 
ATOM   2403 N  NE    . ARG A 1 333 ? -10.473 -27.404 8.477   1.00 41.20 ? 313 ARG A NE    1 
ATOM   2404 C  CZ    . ARG A 1 333 ? -11.153 -26.733 9.390   1.00 36.53 ? 313 ARG A CZ    1 
ATOM   2405 N  NH1   . ARG A 1 333 ? -11.213 -27.180 10.629  1.00 40.89 ? 313 ARG A NH1   1 
ATOM   2406 N  NH2   . ARG A 1 333 ? -11.747 -25.604 9.079   1.00 31.80 ? 313 ARG A NH2   1 
ATOM   2407 N  N     . LEU A 1 334 ? -12.015 -32.431 6.421   1.00 20.36 ? 314 LEU A N     1 
ATOM   2408 C  CA    . LEU A 1 334 ? -11.216 -33.263 5.528   1.00 23.33 ? 314 LEU A CA    1 
ATOM   2409 C  C     . LEU A 1 334 ? -10.295 -32.357 4.723   1.00 25.60 ? 314 LEU A C     1 
ATOM   2410 O  O     . LEU A 1 334 ? -10.761 -31.583 3.901   1.00 26.08 ? 314 LEU A O     1 
ATOM   2411 C  CB    . LEU A 1 334 ? -12.105 -34.092 4.605   1.00 24.19 ? 314 LEU A CB    1 
ATOM   2412 C  CG    . LEU A 1 334 ? -11.353 -34.972 3.608   1.00 27.36 ? 314 LEU A CG    1 
ATOM   2413 C  CD1   . LEU A 1 334 ? -10.678 -36.151 4.311   1.00 28.58 ? 314 LEU A CD1   1 
ATOM   2414 C  CD2   . LEU A 1 334 ? -12.290 -35.453 2.512   1.00 29.68 ? 314 LEU A CD2   1 
ATOM   2415 N  N     . ASP A 1 335 ? -8.993  -32.454 4.969   1.00 35.99 ? 315 ASP A N     1 
ATOM   2416 C  CA    . ASP A 1 335 ? -8.074  -31.545 4.310   1.00 40.72 ? 315 ASP A CA    1 
ATOM   2417 C  C     . ASP A 1 335 ? -8.023  -31.949 2.844   1.00 39.48 ? 315 ASP A C     1 
ATOM   2418 O  O     . ASP A 1 335 ? -8.261  -33.100 2.509   1.00 36.41 ? 315 ASP A O     1 
ATOM   2419 C  CB    . ASP A 1 335 ? -6.739  -31.466 5.048   1.00 48.86 ? 315 ASP A CB    1 
ATOM   2420 C  CG    . ASP A 1 335 ? -6.905  -30.648 6.318   1.00 51.31 ? 315 ASP A CG    1 
ATOM   2421 O  OD1   . ASP A 1 335 ? -7.166  -29.414 6.200   1.00 51.16 ? 315 ASP A OD1   1 
ATOM   2422 O  OD2   . ASP A 1 335 ? -6.887  -31.258 7.405   1.00 60.76 ? 315 ASP A OD2   1 
ATOM   2423 N  N     . ASP A 1 336 ? -7.798  -30.947 1.998   1.00 39.25 ? 316 ASP A N     1 
ATOM   2424 C  CA    . ASP A 1 336 ? -7.851  -31.068 0.557   1.00 34.61 ? 316 ASP A CA    1 
ATOM   2425 C  C     . ASP A 1 336 ? -6.419  -30.922 0.063   1.00 36.09 ? 316 ASP A C     1 
ATOM   2426 O  O     . ASP A 1 336 ? -5.816  -29.881 0.299   1.00 27.52 ? 316 ASP A O     1 
ATOM   2427 C  CB    . ASP A 1 336 ? -8.766  -29.981 -0.005  1.00 32.96 ? 316 ASP A CB    1 
ATOM   2428 C  CG    . ASP A 1 336 ? -8.905  -29.948 -1.513  1.00 33.04 ? 316 ASP A CG    1 
ATOM   2429 O  OD1   . ASP A 1 336 ? -8.121  -30.641 -2.218  1.00 29.44 ? 316 ASP A OD1   1 
ATOM   2430 O  OD2   . ASP A 1 336 ? -9.778  -29.224 -1.973  1.00 32.19 ? 316 ASP A OD2   1 
ATOM   2431 N  N     . PRO A 1 337 ? -5.833  -31.943 -0.613  1.00 32.12 ? 317 PRO A N     1 
ATOM   2432 C  CA    . PRO A 1 337 ? -4.417  -31.886 -1.016  1.00 32.81 ? 317 PRO A CA    1 
ATOM   2433 C  C     . PRO A 1 337 ? -4.107  -30.740 -1.982  1.00 28.91 ? 317 PRO A C     1 
ATOM   2434 O  O     . PRO A 1 337 ? -2.962  -30.316 -2.100  1.00 28.93 ? 317 PRO A O     1 
ATOM   2435 C  CB    . PRO A 1 337 ? -4.146  -33.213 -1.757  1.00 34.90 ? 317 PRO A CB    1 
ATOM   2436 C  CG    . PRO A 1 337 ? -5.514  -33.946 -1.871  1.00 35.22 ? 317 PRO A CG    1 
ATOM   2437 C  CD    . PRO A 1 337 ? -6.522  -33.186 -1.031  1.00 35.89 ? 317 PRO A CD    1 
ATOM   2438 N  N     . ASP A 1 338 ? -5.148  -30.299 -2.695  1.00 27.26 ? 318 ASP A N     1 
ATOM   2439 C  CA    . ASP A 1 338 ? -5.051  -29.275 -3.730  1.00 31.14 ? 318 ASP A CA    1 
ATOM   2440 C  C     . ASP A 1 338 ? -4.927  -27.858 -3.157  1.00 26.65 ? 318 ASP A C     1 
ATOM   2441 O  O     . ASP A 1 338 ? -4.715  -26.917 -3.920  1.00 27.26 ? 318 ASP A O     1 
ATOM   2442 C  CB    . ASP A 1 338 ? -6.270  -29.282 -4.661  1.00 33.73 ? 318 ASP A CB    1 
ATOM   2443 C  CG    . ASP A 1 338 ? -6.287  -30.471 -5.599  1.00 36.63 ? 318 ASP A CG    1 
ATOM   2444 O  OD1   . ASP A 1 338 ? -5.209  -31.056 -5.811  1.00 32.54 ? 318 ASP A OD1   1 
ATOM   2445 O  OD2   . ASP A 1 338 ? -7.385  -30.822 -6.073  1.00 40.44 ? 318 ASP A OD2   1 
ATOM   2446 N  N     . LEU A 1 339 ? -5.143  -27.668 -1.846  1.00 21.93 ? 319 LEU A N     1 
ATOM   2447 C  CA    . LEU A 1 339 ? -5.059  -26.342 -1.259  1.00 21.79 ? 319 LEU A CA    1 
ATOM   2448 C  C     . LEU A 1 339 ? -3.840  -26.293 -0.367  1.00 18.48 ? 319 LEU A C     1 
ATOM   2449 O  O     . LEU A 1 339 ? -3.611  -27.188 0.437   1.00 19.11 ? 319 LEU A O     1 
ATOM   2450 C  CB    . LEU A 1 339 ? -6.296  -26.013 -0.429  1.00 21.37 ? 319 LEU A CB    1 
ATOM   2451 C  CG    . LEU A 1 339 ? -7.589  -26.082 -1.219  1.00 24.35 ? 319 LEU A CG    1 
ATOM   2452 C  CD1   . LEU A 1 339 ? -8.751  -25.789 -0.299  1.00 29.81 ? 319 LEU A CD1   1 
ATOM   2453 C  CD2   . LEU A 1 339 ? -7.557  -25.139 -2.403  1.00 26.35 ? 319 LEU A CD2   1 
ATOM   2454 N  N     . PRO A 1 340 ? -3.041  -25.224 -0.464  1.00 18.62 ? 320 PRO A N     1 
ATOM   2455 C  CA    . PRO A 1 340 ? -1.953  -25.013 0.480   1.00 17.41 ? 320 PRO A CA    1 
ATOM   2456 C  C     . PRO A 1 340 ? -2.419  -24.551 1.873   1.00 17.76 ? 320 PRO A C     1 
ATOM   2457 O  O     . PRO A 1 340 ? -3.531  -24.087 2.017   1.00 18.01 ? 320 PRO A O     1 
ATOM   2458 C  CB    . PRO A 1 340 ? -1.186  -23.871 -0.189  1.00 17.41 ? 320 PRO A CB    1 
ATOM   2459 C  CG    . PRO A 1 340 ? -2.200  -23.102 -0.975  1.00 16.69 ? 320 PRO A CG    1 
ATOM   2460 C  CD    . PRO A 1 340 ? -3.249  -24.104 -1.387  1.00 18.77 ? 320 PRO A CD    1 
ATOM   2461 N  N     . HIS A 1 341 ? -1.539  -24.719 2.857   1.00 17.26 ? 321 HIS A N     1 
ATOM   2462 C  CA    . HIS A 1 341 ? -1.804  -24.387 4.244   1.00 17.24 ? 321 HIS A CA    1 
ATOM   2463 C  C     . HIS A 1 341 ? -0.853  -23.278 4.645   1.00 15.12 ? 321 HIS A C     1 
ATOM   2464 O  O     . HIS A 1 341 ? 0.204   -23.160 4.079   1.00 14.86 ? 321 HIS A O     1 
ATOM   2465 C  CB    . HIS A 1 341 ? -1.557  -25.606 5.147   1.00 19.51 ? 321 HIS A CB    1 
ATOM   2466 C  CG    . HIS A 1 341 ? -2.650  -26.594 4.995   1.00 25.15 ? 321 HIS A CG    1 
ATOM   2467 N  ND1   . HIS A 1 341 ? -3.500  -26.889 6.036   1.00 28.27 ? 321 HIS A ND1   1 
ATOM   2468 C  CD2   . HIS A 1 341 ? -3.141  -27.222 3.920   1.00 29.04 ? 321 HIS A CD2   1 
ATOM   2469 C  CE1   . HIS A 1 341 ? -4.424  -27.737 5.606   1.00 29.17 ? 321 HIS A CE1   1 
ATOM   2470 N  NE2   . HIS A 1 341 ? -4.232  -27.950 4.338   1.00 28.28 ? 321 HIS A NE2   1 
ATOM   2471 N  N     . THR A 1 342 ? -1.239  -22.469 5.637   1.00 16.33 ? 322 THR A N     1 
ATOM   2472 C  CA    . THR A 1 342 ? -0.322  -21.601 6.367   1.00 14.63 ? 322 THR A CA    1 
ATOM   2473 C  C     . THR A 1 342 ? 0.291   -22.336 7.553   1.00 17.86 ? 322 THR A C     1 
ATOM   2474 O  O     . THR A 1 342 ? 0.385   -23.559 7.530   1.00 17.64 ? 322 THR A O     1 
ATOM   2475 C  CB    . THR A 1 342 ? -1.098  -20.355 6.839   1.00 14.95 ? 322 THR A CB    1 
ATOM   2476 O  OG1   . THR A 1 342 ? -2.026  -20.809 7.840   1.00 14.46 ? 322 THR A OG1   1 
ATOM   2477 C  CG2   . THR A 1 342 ? -1.822  -19.658 5.712   1.00 14.61 ? 322 THR A CG2   1 
ATOM   2478 N  N     . ALA A 1 343 ? 0.707   -21.608 8.609   1.00 14.48 ? 323 ALA A N     1 
ATOM   2479 C  CA    . ALA A 1 343 ? 1.234   -22.230 9.802   1.00 15.62 ? 323 ALA A CA    1 
ATOM   2480 C  C     . ALA A 1 343 ? 0.125   -22.985 10.543  1.00 16.37 ? 323 ALA A C     1 
ATOM   2481 O  O     . ALA A 1 343 ? 0.435   -23.899 11.314  1.00 17.46 ? 323 ALA A O     1 
ATOM   2482 C  CB    . ALA A 1 343 ? 1.883   -21.240 10.687  1.00 14.14 ? 323 ALA A CB    1 
ATOM   2483 N  N     . ASP A 1 344 ? -1.126  -22.585 10.351  1.00 13.63 ? 324 ASP A N     1 
ATOM   2484 C  CA    . ASP A 1 344 ? -2.214  -23.156 11.143  1.00 14.26 ? 324 ASP A CA    1 
ATOM   2485 C  C     . ASP A 1 344 ? -3.501  -23.432 10.371  1.00 13.92 ? 324 ASP A C     1 
ATOM   2486 O  O     . ASP A 1 344 ? -4.445  -24.030 10.955  1.00 13.91 ? 324 ASP A O     1 
ATOM   2487 C  CB    . ASP A 1 344 ? -2.484  -22.321 12.409  1.00 13.35 ? 324 ASP A CB    1 
ATOM   2488 C  CG    . ASP A 1 344 ? -3.008  -20.921 12.181  1.00 14.28 ? 324 ASP A CG    1 
ATOM   2489 O  OD1   . ASP A 1 344 ? -2.900  -20.445 11.024  1.00 13.48 ? 324 ASP A OD1   1 
ATOM   2490 O  OD2   . ASP A 1 344 ? -3.606  -20.353 13.169  1.00 13.02 ? 324 ASP A OD2   1 
ATOM   2491 N  N     . ARG A 1 345 ? -3.644  -23.021 9.092   1.00 15.08 ? 325 ARG A N     1 
ATOM   2492 C  CA    . ARG A 1 345 ? -4.881  -23.216 8.384   1.00 15.02 ? 325 ARG A CA    1 
ATOM   2493 C  C     . ARG A 1 345 ? -4.670  -23.508 6.895   1.00 15.96 ? 325 ARG A C     1 
ATOM   2494 O  O     . ARG A 1 345 ? -3.608  -23.248 6.327   1.00 20.15 ? 325 ARG A O     1 
ATOM   2495 C  CB    . ARG A 1 345 ? -5.795  -21.984 8.469   1.00 14.94 ? 325 ARG A CB    1 
ATOM   2496 C  CG    . ARG A 1 345 ? -5.988  -21.449 9.881   1.00 14.22 ? 325 ARG A CG    1 
ATOM   2497 C  CD    . ARG A 1 345 ? -6.927  -20.259 9.860   1.00 13.00 ? 325 ARG A CD    1 
ATOM   2498 N  NE    . ARG A 1 345 ? -6.933  -19.602 11.178  1.00 11.41 ? 325 ARG A NE    1 
ATOM   2499 C  CZ    . ARG A 1 345 ? -7.674  -19.991 12.187  1.00 12.84 ? 325 ARG A CZ    1 
ATOM   2500 N  NH1   . ARG A 1 345 ? -8.611  -20.908 12.019  1.00 13.44 ? 325 ARG A NH1   1 
ATOM   2501 N  NH2   . ARG A 1 345 ? -7.563  -19.368 13.342  1.00 12.75 ? 325 ARG A NH2   1 
ATOM   2502 N  N     . GLU A 1 346 ? -5.723  -24.051 6.305   1.00 15.98 ? 326 GLU A N     1 
ATOM   2503 C  CA    . GLU A 1 346 ? -5.846  -24.178 4.859   1.00 16.43 ? 326 GLU A CA    1 
ATOM   2504 C  C     . GLU A 1 346 ? -6.185  -22.806 4.285   1.00 16.84 ? 326 GLU A C     1 
ATOM   2505 O  O     . GLU A 1 346 ? -7.076  -22.122 4.820   1.00 18.54 ? 326 GLU A O     1 
ATOM   2506 C  CB    . GLU A 1 346 ? -6.962  -25.185 4.600   1.00 18.42 ? 326 GLU A CB    1 
ATOM   2507 C  CG    . GLU A 1 346 ? -7.333  -25.493 3.153   1.00 20.58 ? 326 GLU A CG    1 
ATOM   2508 C  CD    . GLU A 1 346 ? -8.636  -26.263 3.036   1.00 26.36 ? 326 GLU A CD    1 
ATOM   2509 O  OE1   . GLU A 1 346 ? -9.724  -25.677 3.293   1.00 21.15 ? 326 GLU A OE1   1 
ATOM   2510 O  OE2   . GLU A 1 346 ? -8.555  -27.483 2.721   1.00 33.04 ? 326 GLU A OE2   1 
ATOM   2511 N  N     . VAL A 1 347 ? -5.579  -22.451 3.133   1.00 15.57 ? 327 VAL A N     1 
ATOM   2512 C  CA    . VAL A 1 347 ? -5.858  -21.197 2.442   1.00 15.35 ? 327 VAL A CA    1 
ATOM   2513 C  C     . VAL A 1 347 ? -6.940  -21.453 1.384   1.00 16.88 ? 327 VAL A C     1 
ATOM   2514 O  O     . VAL A 1 347 ? -6.816  -22.342 0.533   1.00 17.47 ? 327 VAL A O     1 
ATOM   2515 C  CB    . VAL A 1 347 ? -4.567  -20.569 1.865   1.00 15.25 ? 327 VAL A CB    1 
ATOM   2516 C  CG1   . VAL A 1 347 ? -4.855  -19.309 1.060   1.00 17.22 ? 327 VAL A CG1   1 
ATOM   2517 C  CG2   . VAL A 1 347 ? -3.531  -20.290 2.936   1.00 16.17 ? 327 VAL A CG2   1 
ATOM   2518 N  N     . TYR A 1 348 ? -8.052  -20.713 1.465   1.00 14.84 ? 328 TYR A N     1 
ATOM   2519 C  CA    . TYR A 1 348 ? -9.145  -20.859 0.539   1.00 15.09 ? 328 TYR A CA    1 
ATOM   2520 C  C     . TYR A 1 348 ? -9.833  -19.520 0.278   1.00 14.45 ? 328 TYR A C     1 
ATOM   2521 O  O     . TYR A 1 348 ? -10.938 -19.225 0.778   1.00 12.18 ? 328 TYR A O     1 
ATOM   2522 C  CB    . TYR A 1 348 ? -10.136 -21.883 1.046   1.00 16.00 ? 328 TYR A CB    1 
ATOM   2523 C  CG    . TYR A 1 348 ? -11.066 -22.340 -0.034  1.00 15.01 ? 328 TYR A CG    1 
ATOM   2524 C  CD1   . TYR A 1 348 ? -10.569 -23.069 -1.104  1.00 18.70 ? 328 TYR A CD1   1 
ATOM   2525 C  CD2   . TYR A 1 348 ? -12.406 -22.042 -0.006  1.00 16.27 ? 328 TYR A CD2   1 
ATOM   2526 C  CE1   . TYR A 1 348 ? -11.410 -23.527 -2.092  1.00 19.26 ? 328 TYR A CE1   1 
ATOM   2527 C  CE2   . TYR A 1 348 ? -13.266 -22.508 -0.976  1.00 18.03 ? 328 TYR A CE2   1 
ATOM   2528 C  CZ    . TYR A 1 348 ? -12.760 -23.269 -2.010  1.00 20.16 ? 328 TYR A CZ    1 
ATOM   2529 O  OH    . TYR A 1 348 ? -13.543 -23.719 -3.014  1.00 21.91 ? 328 TYR A OH    1 
ATOM   2530 N  N     . PRO A 1 349 ? -9.222  -18.678 -0.591  1.00 14.97 ? 329 PRO A N     1 
ATOM   2531 C  CA    . PRO A 1 349 ? -9.714  -17.307 -0.755  1.00 15.13 ? 329 PRO A CA    1 
ATOM   2532 C  C     . PRO A 1 349 ? -11.126 -17.251 -1.268  1.00 12.63 ? 329 PRO A C     1 
ATOM   2533 O  O     . PRO A 1 349 ? -11.960 -16.399 -0.940  1.00 13.16 ? 329 PRO A O     1 
ATOM   2534 C  CB    . PRO A 1 349 ? -8.737  -16.679 -1.753  1.00 15.75 ? 329 PRO A CB    1 
ATOM   2535 C  CG    . PRO A 1 349 ? -7.498  -17.509 -1.649  1.00 17.77 ? 329 PRO A CG    1 
ATOM   2536 C  CD    . PRO A 1 349 ? -7.970  -18.910 -1.324  1.00 17.31 ? 329 PRO A CD    1 
ATOM   2537 N  N     . GLU A 1 350 ? -11.469 -18.221 -2.134  1.00 13.03 ? 330 GLU A N     1 
ATOM   2538 C  CA    . GLU A 1 350 ? -12.798 -18.279 -2.684  1.00 12.74 ? 330 GLU A CA    1 
ATOM   2539 C  C     . GLU A 1 350 ? -13.903 -18.466 -1.645  1.00 13.65 ? 330 GLU A C     1 
ATOM   2540 O  O     . GLU A 1 350 ? -15.051 -18.109 -1.848  1.00 13.10 ? 330 GLU A O     1 
ATOM   2541 C  CB    . GLU A 1 350 ? -12.793 -19.386 -3.734  1.00 14.94 ? 330 GLU A CB    1 
ATOM   2542 C  CG    . GLU A 1 350 ? -11.772 -19.138 -4.848  1.00 16.65 ? 330 GLU A CG    1 
ATOM   2543 C  CD    . GLU A 1 350 ? -10.307 -19.550 -4.694  1.00 19.92 ? 330 GLU A CD    1 
ATOM   2544 O  OE1   . GLU A 1 350 ? -9.908  -20.181 -3.684  1.00 21.21 ? 330 GLU A OE1   1 
ATOM   2545 O  OE2   . GLU A 1 350 ? -9.551  -19.308 -5.685  1.00 20.47 ? 330 GLU A OE2   1 
ATOM   2546 N  N     . GLY A 1 351 ? -13.564 -18.953 -0.446  1.00 12.51 ? 331 GLY A N     1 
ATOM   2547 C  CA    . GLY A 1 351 ? -14.546 -19.044 0.624   1.00 13.40 ? 331 GLY A CA    1 
ATOM   2548 C  C     . GLY A 1 351 ? -15.100 -17.675 1.058   1.00 11.71 ? 331 GLY A C     1 
ATOM   2549 O  O     . GLY A 1 351 ? -16.242 -17.556 1.451   1.00 12.36 ? 331 GLY A O     1 
ATOM   2550 N  N     . LEU A 1 352 ? -14.257 -16.652 0.936   1.00 13.09 ? 332 LEU A N     1 
ATOM   2551 C  CA    . LEU A 1 352 ? -14.645 -15.280 1.236   1.00 12.86 ? 332 LEU A CA    1 
ATOM   2552 C  C     . LEU A 1 352 ? -15.656 -14.790 0.217   1.00 14.97 ? 332 LEU A C     1 
ATOM   2553 O  O     . LEU A 1 352 ? -16.651 -14.182 0.579   1.00 12.95 ? 332 LEU A O     1 
ATOM   2554 C  CB    . LEU A 1 352 ? -13.400 -14.400 1.261   1.00 15.22 ? 332 LEU A CB    1 
ATOM   2555 C  CG    . LEU A 1 352 ? -13.606 -12.917 1.603   1.00 14.35 ? 332 LEU A CG    1 
ATOM   2556 C  CD1   . LEU A 1 352 ? -14.333 -12.729 2.936   1.00 14.30 ? 332 LEU A CD1   1 
ATOM   2557 C  CD2   . LEU A 1 352 ? -12.252 -12.248 1.639   1.00 13.88 ? 332 LEU A CD2   1 
ATOM   2558 N  N     . TYR A 1 353 ? -15.403 -15.099 -1.060  1.00 15.26 ? 333 TYR A N     1 
ATOM   2559 C  CA    . TYR A 1 353 ? -16.390 -14.755 -2.063  1.00 14.62 ? 333 TYR A CA    1 
ATOM   2560 C  C     . TYR A 1 353 ? -17.692 -15.464 -1.748  1.00 13.47 ? 333 TYR A C     1 
ATOM   2561 O  O     . TYR A 1 353 ? -18.729 -14.849 -1.715  1.00 11.68 ? 333 TYR A O     1 
ATOM   2562 C  CB    . TYR A 1 353 ? -15.857 -15.089 -3.458  1.00 15.35 ? 333 TYR A CB    1 
ATOM   2563 C  CG    . TYR A 1 353 ? -16.860 -14.858 -4.551  1.00 16.28 ? 333 TYR A CG    1 
ATOM   2564 C  CD1   . TYR A 1 353 ? -17.793 -15.820 -4.902  1.00 17.62 ? 333 TYR A CD1   1 
ATOM   2565 C  CD2   . TYR A 1 353 ? -16.924 -13.637 -5.195  1.00 16.13 ? 333 TYR A CD2   1 
ATOM   2566 C  CE1   . TYR A 1 353 ? -18.732 -15.587 -5.893  1.00 18.85 ? 333 TYR A CE1   1 
ATOM   2567 C  CE2   . TYR A 1 353 ? -17.866 -13.389 -6.179  1.00 17.14 ? 333 TYR A CE2   1 
ATOM   2568 C  CZ    . TYR A 1 353 ? -18.760 -14.367 -6.553  1.00 19.50 ? 333 TYR A CZ    1 
ATOM   2569 O  OH    . TYR A 1 353 ? -19.687 -14.040 -7.534  1.00 19.24 ? 333 TYR A OH    1 
ATOM   2570 N  N     . ASP A 1 354 ? -17.645 -16.773 -1.464  1.00 13.38 ? 334 ASP A N     1 
ATOM   2571 C  CA    . ASP A 1 354 ? -18.888 -17.497 -1.278  1.00 13.93 ? 334 ASP A CA    1 
ATOM   2572 C  C     . ASP A 1 354 ? -19.656 -16.937 -0.109  1.00 13.45 ? 334 ASP A C     1 
ATOM   2573 O  O     . ASP A 1 354 ? -20.860 -16.778 -0.181  1.00 11.64 ? 334 ASP A O     1 
ATOM   2574 C  CB    . ASP A 1 354 ? -18.703 -19.011 -1.101  1.00 15.03 ? 334 ASP A CB    1 
ATOM   2575 C  CG    . ASP A 1 354 ? -18.271 -19.754 -2.368  1.00 17.90 ? 334 ASP A CG    1 
ATOM   2576 O  OD1   . ASP A 1 354 ? -18.464 -19.177 -3.496  1.00 16.99 ? 334 ASP A OD1   1 
ATOM   2577 O  OD2   . ASP A 1 354 ? -17.562 -20.778 -2.232  1.00 20.70 ? 334 ASP A OD2   1 
ATOM   2578 N  N     . ILE A 1 355 ? -18.954 -16.711 1.025   1.00 12.79 ? 335 ILE A N     1 
ATOM   2579 C  CA    . ILE A 1 355 ? -19.678 -16.278 2.199   1.00 12.37 ? 335 ILE A CA    1 
ATOM   2580 C  C     . ILE A 1 355 ? -20.305 -14.888 2.013   1.00 11.19 ? 335 ILE A C     1 
ATOM   2581 O  O     . ILE A 1 355 ? -21.350 -14.640 2.543   1.00 9.92  ? 335 ILE A O     1 
ATOM   2582 C  CB    . ILE A 1 355 ? -18.825 -16.412 3.481   1.00 14.01 ? 335 ILE A CB    1 
ATOM   2583 C  CG1   . ILE A 1 355 ? -19.755 -16.481 4.688   1.00 16.53 ? 335 ILE A CG1   1 
ATOM   2584 C  CG2   . ILE A 1 355 ? -17.776 -15.328 3.579   1.00 14.44 ? 335 ILE A CG2   1 
ATOM   2585 C  CD1   . ILE A 1 355 ? -20.330 -17.835 4.898   1.00 19.03 ? 335 ILE A CD1   1 
ATOM   2586 N  N     . LEU A 1 356 ? -19.608 -13.968 1.344   1.00 11.60 ? 336 LEU A N     1 
ATOM   2587 C  CA    . LEU A 1 356 ? -20.156 -12.658 1.047   1.00 11.52 ? 336 LEU A CA    1 
ATOM   2588 C  C     . LEU A 1 356 ? -21.375 -12.771 0.127   1.00 11.16 ? 336 LEU A C     1 
ATOM   2589 O  O     . LEU A 1 356 ? -22.342 -12.066 0.367   1.00 11.50 ? 336 LEU A O     1 
ATOM   2590 C  CB    . LEU A 1 356 ? -19.030 -11.822 0.440   1.00 12.17 ? 336 LEU A CB    1 
ATOM   2591 C  CG    . LEU A 1 356 ? -17.981 -11.360 1.461   1.00 12.98 ? 336 LEU A CG    1 
ATOM   2592 C  CD1   . LEU A 1 356 ? -16.860 -10.609 0.788   1.00 13.20 ? 336 LEU A CD1   1 
ATOM   2593 C  CD2   . LEU A 1 356 ? -18.630 -10.527 2.544   1.00 13.31 ? 336 LEU A CD2   1 
ATOM   2594 N  N     . LEU A 1 357 ? -21.305 -13.646 -0.893  1.00 12.66 ? 337 LEU A N     1 
ATOM   2595 C  CA    . LEU A 1 357 ? -22.424 -13.783 -1.826  1.00 13.57 ? 337 LEU A CA    1 
ATOM   2596 C  C     . LEU A 1 357 ? -23.598 -14.346 -1.052  1.00 12.35 ? 337 LEU A C     1 
ATOM   2597 O  O     . LEU A 1 357 ? -24.747 -13.977 -1.233  1.00 14.94 ? 337 LEU A O     1 
ATOM   2598 C  CB    . LEU A 1 357 ? -22.017 -14.664 -3.016  1.00 13.82 ? 337 LEU A CB    1 
ATOM   2599 C  CG    . LEU A 1 357 ? -21.554 -13.953 -4.299  1.00 15.42 ? 337 LEU A CG    1 
ATOM   2600 C  CD1   . LEU A 1 357 ? -22.714 -13.209 -4.915  1.00 17.56 ? 337 LEU A CD1   1 
ATOM   2601 C  CD2   . LEU A 1 357 ? -20.429 -12.962 -4.048  1.00 14.97 ? 337 LEU A CD2   1 
ATOM   2602 N  N     . ARG A 1 358 ? -23.328 -15.267 -0.102  1.00 11.64 ? 338 ARG A N     1 
ATOM   2603 C  CA    . ARG A 1 358 ? -24.415 -15.758 0.718   1.00 12.22 ? 338 ARG A CA    1 
ATOM   2604 C  C     . ARG A 1 358 ? -25.050 -14.667 1.570   1.00 12.08 ? 338 ARG A C     1 
ATOM   2605 O  O     . ARG A 1 358 ? -26.250 -14.520 1.696   1.00 11.66 ? 338 ARG A O     1 
ATOM   2606 C  CB    . ARG A 1 358 ? -23.910 -16.853 1.653   1.00 13.27 ? 338 ARG A CB    1 
ATOM   2607 C  CG    . ARG A 1 358 ? -25.003 -17.360 2.576   1.00 15.96 ? 338 ARG A CG    1 
ATOM   2608 C  CD    . ARG A 1 358 ? -24.386 -18.440 3.388   1.00 17.60 ? 338 ARG A CD    1 
ATOM   2609 N  NE    . ARG A 1 358 ? -25.413 -19.092 4.157   1.00 19.95 ? 338 ARG A NE    1 
ATOM   2610 C  CZ    . ARG A 1 358 ? -25.138 -19.990 5.085   1.00 20.76 ? 338 ARG A CZ    1 
ATOM   2611 N  NH1   . ARG A 1 358 ? -23.881 -20.320 5.304   1.00 20.22 ? 338 ARG A NH1   1 
ATOM   2612 N  NH2   . ARG A 1 358 ? -26.125 -20.518 5.780   1.00 20.16 ? 338 ARG A NH2   1 
ATOM   2613 N  N     . LEU A 1 359 ? -24.215 -13.866 2.248   1.00 12.72 ? 339 LEU A N     1 
ATOM   2614 C  CA    . LEU A 1 359 ? -24.782 -12.783 3.008   1.00 12.03 ? 339 LEU A CA    1 
ATOM   2615 C  C     . LEU A 1 359 ? -25.581 -11.819 2.144   1.00 12.24 ? 339 LEU A C     1 
ATOM   2616 O  O     . LEU A 1 359 ? -26.647 -11.398 2.578   1.00 12.84 ? 339 LEU A O     1 
ATOM   2617 C  CB    . LEU A 1 359 ? -23.619 -12.044 3.684   1.00 12.07 ? 339 LEU A CB    1 
ATOM   2618 C  CG    . LEU A 1 359 ? -23.011 -12.777 4.891   1.00 12.44 ? 339 LEU A CG    1 
ATOM   2619 C  CD1   . LEU A 1 359 ? -21.741 -12.070 5.367   1.00 12.20 ? 339 LEU A CD1   1 
ATOM   2620 C  CD2   . LEU A 1 359 ? -24.008 -12.958 6.039   1.00 11.93 ? 339 LEU A CD2   1 
ATOM   2621 N  N     . HIS A 1 360 ? -25.005 -11.472 0.989   1.00 12.43 ? 340 HIS A N     1 
ATOM   2622 C  CA    . HIS A 1 360 ? -25.633 -10.550 0.068   1.00 12.92 ? 340 HIS A CA    1 
ATOM   2623 C  C     . HIS A 1 360 ? -27.006 -11.086 -0.336  1.00 13.08 ? 340 HIS A C     1 
ATOM   2624 O  O     . HIS A 1 360 ? -28.015 -10.414 -0.244  1.00 11.35 ? 340 HIS A O     1 
ATOM   2625 C  CB    . HIS A 1 360 ? -24.735 -10.338 -1.145  1.00 13.58 ? 340 HIS A CB    1 
ATOM   2626 C  CG    . HIS A 1 360 ? -25.336 -9.412  -2.160  1.00 15.98 ? 340 HIS A CG    1 
ATOM   2627 N  ND1   . HIS A 1 360 ? -25.876 -8.167  -1.882  1.00 15.17 ? 340 HIS A ND1   1 
ATOM   2628 C  CD2   . HIS A 1 360 ? -25.539 -9.643  -3.463  1.00 17.06 ? 340 HIS A CD2   1 
ATOM   2629 C  CE1   . HIS A 1 360 ? -26.326 -7.638  -3.027  1.00 16.60 ? 340 HIS A CE1   1 
ATOM   2630 N  NE2   . HIS A 1 360 ? -26.123 -8.523  -4.005  1.00 16.51 ? 340 HIS A NE2   1 
ATOM   2631 N  N     . ASN A 1 361 ? -27.064 -12.336 -0.765  1.00 13.42 ? 341 ASN A N     1 
ATOM   2632 C  CA    . ASN A 1 361 ? -28.310 -12.847 -1.329  1.00 13.05 ? 341 ASN A CA    1 
ATOM   2633 C  C     . ASN A 1 361 ? -29.256 -13.440 -0.288  1.00 14.95 ? 341 ASN A C     1 
ATOM   2634 O  O     . ASN A 1 361 ? -30.461 -13.385 -0.503  1.00 16.47 ? 341 ASN A O     1 
ATOM   2635 C  CB    . ASN A 1 361 ? -28.006 -13.853 -2.429  1.00 13.55 ? 341 ASN A CB    1 
ATOM   2636 C  CG    . ASN A 1 361 ? -27.378 -13.164 -3.614  1.00 14.44 ? 341 ASN A CG    1 
ATOM   2637 O  OD1   . ASN A 1 361 ? -27.912 -12.150 -4.051  1.00 16.08 ? 341 ASN A OD1   1 
ATOM   2638 N  ND2   . ASN A 1 361 ? -26.243 -13.643 -4.111  1.00 14.30 ? 341 ASN A ND2   1 
ATOM   2639 N  N     . ASP A 1 362 ? -28.764 -14.035 0.814   1.00 14.50 ? 342 ASP A N     1 
ATOM   2640 C  CA    . ASP A 1 362 ? -29.584 -14.880 1.681   1.00 13.48 ? 342 ASP A CA    1 
ATOM   2641 C  C     . ASP A 1 362 ? -29.970 -14.184 2.985   1.00 13.77 ? 342 ASP A C     1 
ATOM   2642 O  O     . ASP A 1 362 ? -30.867 -14.654 3.681   1.00 13.94 ? 342 ASP A O     1 
ATOM   2643 C  CB    . ASP A 1 362 ? -28.865 -16.184 1.998   1.00 15.85 ? 342 ASP A CB    1 
ATOM   2644 C  CG    . ASP A 1 362 ? -28.301 -16.907 0.780   1.00 18.92 ? 342 ASP A CG    1 
ATOM   2645 O  OD1   . ASP A 1 362 ? -28.307 -16.302 -0.414  1.00 21.12 ? 342 ASP A OD1   1 
ATOM   2646 O  OD2   . ASP A 1 362 ? -27.777 -18.061 0.974   1.00 19.66 ? 342 ASP A OD2   1 
ATOM   2647 N  N     . TYR A 1 363 ? -29.239 -13.099 3.336   1.00 14.08 ? 343 TYR A N     1 
ATOM   2648 C  CA    . TYR A 1 363 ? -29.525 -12.367 4.570   1.00 12.85 ? 343 TYR A CA    1 
ATOM   2649 C  C     . TYR A 1 363 ? -29.711 -10.876 4.297   1.00 14.52 ? 343 TYR A C     1 
ATOM   2650 O  O     . TYR A 1 363 ? -29.241 -10.380 3.289   1.00 12.70 ? 343 TYR A O     1 
ATOM   2651 C  CB    . TYR A 1 363 ? -28.322 -12.555 5.518   1.00 12.36 ? 343 TYR A CB    1 
ATOM   2652 C  CG    . TYR A 1 363 ? -28.280 -13.929 6.141   1.00 12.03 ? 343 TYR A CG    1 
ATOM   2653 C  CD1   . TYR A 1 363 ? -29.106 -14.182 7.221   1.00 12.79 ? 343 TYR A CD1   1 
ATOM   2654 C  CD2   . TYR A 1 363 ? -27.592 -14.994 5.573   1.00 12.30 ? 343 TYR A CD2   1 
ATOM   2655 C  CE1   . TYR A 1 363 ? -29.164 -15.432 7.824   1.00 12.44 ? 343 TYR A CE1   1 
ATOM   2656 C  CE2   . TYR A 1 363 ? -27.674 -16.268 6.139   1.00 13.26 ? 343 TYR A CE2   1 
ATOM   2657 C  CZ    . TYR A 1 363 ? -28.474 -16.476 7.246   1.00 13.86 ? 343 TYR A CZ    1 
ATOM   2658 O  OH    . TYR A 1 363 ? -28.588 -17.714 7.865   1.00 16.47 ? 343 TYR A OH    1 
ATOM   2659 N  N     . PRO A 1 364 ? -30.331 -10.133 5.239   1.00 12.83 ? 344 PRO A N     1 
ATOM   2660 C  CA    . PRO A 1 364 ? -30.608 -8.713  5.050   1.00 13.78 ? 344 PRO A CA    1 
ATOM   2661 C  C     . PRO A 1 364 ? -29.509 -7.720  5.432   1.00 14.80 ? 344 PRO A C     1 
ATOM   2662 O  O     . PRO A 1 364 ? -29.590 -6.554  5.061   1.00 16.15 ? 344 PRO A O     1 
ATOM   2663 C  CB    . PRO A 1 364 ? -31.772 -8.492  6.015   1.00 13.96 ? 344 PRO A CB    1 
ATOM   2664 C  CG    . PRO A 1 364 ? -31.486 -9.470  7.159   1.00 12.37 ? 344 PRO A CG    1 
ATOM   2665 C  CD    . PRO A 1 364 ? -30.913 -10.683 6.480   1.00 13.65 ? 344 PRO A CD    1 
ATOM   2666 N  N     . PHE A 1 365 ? -28.476 -8.181  6.122   1.00 12.99 ? 345 PHE A N     1 
ATOM   2667 C  CA    . PHE A 1 365 ? -27.534 -7.220  6.691   1.00 13.06 ? 345 PHE A CA    1 
ATOM   2668 C  C     . PHE A 1 365 ? -26.768 -6.482  5.613   1.00 11.18 ? 345 PHE A C     1 
ATOM   2669 O  O     . PHE A 1 365 ? -26.312 -7.062  4.639   1.00 14.05 ? 345 PHE A O     1 
ATOM   2670 C  CB    . PHE A 1 365 ? -26.520 -7.958  7.563   1.00 11.59 ? 345 PHE A CB    1 
ATOM   2671 C  CG    . PHE A 1 365 ? -27.162 -8.917  8.538   1.00 11.53 ? 345 PHE A CG    1 
ATOM   2672 C  CD1   . PHE A 1 365 ? -27.836 -8.464  9.662   1.00 11.93 ? 345 PHE A CD1   1 
ATOM   2673 C  CD2   . PHE A 1 365 ? -27.120 -10.283 8.330   1.00 11.29 ? 345 PHE A CD2   1 
ATOM   2674 C  CE1   . PHE A 1 365 ? -28.416 -9.359  10.556  1.00 12.54 ? 345 PHE A CE1   1 
ATOM   2675 C  CE2   . PHE A 1 365 ? -27.685 -11.166 9.242   1.00 10.99 ? 345 PHE A CE2   1 
ATOM   2676 C  CZ    . PHE A 1 365 ? -28.332 -10.700 10.341  1.00 11.54 ? 345 PHE A CZ    1 
ATOM   2677 N  N     . ARG A 1 366 ? -26.627 -5.177  5.832   1.00 13.13 ? 346 ARG A N     1 
ATOM   2678 C  CA    . ARG A 1 366 ? -25.832 -4.333  4.956   1.00 13.13 ? 346 ARG A CA    1 
ATOM   2679 C  C     . ARG A 1 366 ? -25.740 -2.957  5.592   1.00 10.81 ? 346 ARG A C     1 
ATOM   2680 O  O     . ARG A 1 366 ? -26.629 -2.517  6.306   1.00 11.57 ? 346 ARG A O     1 
ATOM   2681 C  CB    . ARG A 1 366 ? -26.400 -4.225  3.532   1.00 14.86 ? 346 ARG A CB    1 
ATOM   2682 C  CG    . ARG A 1 366 ? -27.863 -3.887  3.509   1.00 16.68 ? 346 ARG A CG    1 
ATOM   2683 C  CD    . ARG A 1 366 ? -28.281 -3.775  2.040   1.00 18.23 ? 346 ARG A CD    1 
ATOM   2684 N  NE    . ARG A 1 366 ? -29.669 -3.386  1.898   1.00 21.17 ? 346 ARG A NE    1 
ATOM   2685 C  CZ    . ARG A 1 366 ? -30.721 -4.195  1.977   1.00 24.71 ? 346 ARG A CZ    1 
ATOM   2686 N  NH1   . ARG A 1 366 ? -31.927 -3.678  1.806   1.00 26.60 ? 346 ARG A NH1   1 
ATOM   2687 N  NH2   . ARG A 1 366 ? -30.598 -5.497  2.228   1.00 25.02 ? 346 ARG A NH2   1 
ATOM   2688 N  N     . PRO A 1 367 ? -24.648 -2.225  5.356   1.00 9.64  ? 347 PRO A N     1 
ATOM   2689 C  CA    . PRO A 1 367 ? -23.479 -2.714  4.654   1.00 10.00 ? 347 PRO A CA    1 
ATOM   2690 C  C     . PRO A 1 367 ? -22.634 -3.693  5.461   1.00 10.11 ? 347 PRO A C     1 
ATOM   2691 O  O     . PRO A 1 367 ? -22.957 -3.986  6.613   1.00 10.40 ? 347 PRO A O     1 
ATOM   2692 C  CB    . PRO A 1 367 ? -22.695 -1.437  4.401   1.00 10.94 ? 347 PRO A CB    1 
ATOM   2693 C  CG    . PRO A 1 367 ? -23.094 -0.576  5.563   1.00 10.16 ? 347 PRO A CG    1 
ATOM   2694 C  CD    . PRO A 1 367 ? -24.553 -0.829  5.776   1.00 10.27 ? 347 PRO A CD    1 
ATOM   2695 N  N     . LEU A 1 368 ? -21.668 -4.271  4.783   1.00 9.87  ? 348 LEU A N     1 
ATOM   2696 C  CA    . LEU A 1 368 ? -20.773 -5.240  5.389   1.00 10.36 ? 348 LEU A CA    1 
ATOM   2697 C  C     . LEU A 1 368 ? -19.372 -4.683  5.426   1.00 10.30 ? 348 LEU A C     1 
ATOM   2698 O  O     . LEU A 1 368 ? -18.922 -3.991  4.505   1.00 10.14 ? 348 LEU A O     1 
ATOM   2699 C  CB    . LEU A 1 368 ? -20.751 -6.527  4.547   1.00 10.76 ? 348 LEU A CB    1 
ATOM   2700 C  CG    . LEU A 1 368 ? -22.082 -7.189  4.268   1.00 11.33 ? 348 LEU A CG    1 
ATOM   2701 C  CD1   . LEU A 1 368 ? -21.869 -8.376  3.319   1.00 10.94 ? 348 LEU A CD1   1 
ATOM   2702 C  CD2   . LEU A 1 368 ? -22.759 -7.629  5.558   1.00 12.00 ? 348 LEU A CD2   1 
ATOM   2703 N  N     . TYR A 1 369 ? -18.635 -5.105  6.470   1.00 8.56  ? 349 TYR A N     1 
ATOM   2704 C  CA    . TYR A 1 369 ? -17.207 -4.859  6.571   1.00 9.31  ? 349 TYR A CA    1 
ATOM   2705 C  C     . TYR A 1 369 ? -16.514 -6.191  6.783   1.00 8.79  ? 349 TYR A C     1 
ATOM   2706 O  O     . TYR A 1 369 ? -17.066 -7.029  7.507   1.00 10.25 ? 349 TYR A O     1 
ATOM   2707 C  CB    . TYR A 1 369 ? -16.883 -3.938  7.767   1.00 8.70  ? 349 TYR A CB    1 
ATOM   2708 C  CG    . TYR A 1 369 ? -17.365 -2.525  7.651   1.00 9.29  ? 349 TYR A CG    1 
ATOM   2709 C  CD1   . TYR A 1 369 ? -18.675 -2.164  7.906   1.00 10.72 ? 349 TYR A CD1   1 
ATOM   2710 C  CD2   . TYR A 1 369 ? -16.502 -1.553  7.178   1.00 10.28 ? 349 TYR A CD2   1 
ATOM   2711 C  CE1   . TYR A 1 369 ? -19.098 -0.849  7.774   1.00 11.19 ? 349 TYR A CE1   1 
ATOM   2712 C  CE2   . TYR A 1 369 ? -16.907 -0.237  7.046   1.00 10.83 ? 349 TYR A CE2   1 
ATOM   2713 C  CZ    . TYR A 1 369 ? -18.218 0.111   7.302   1.00 10.96 ? 349 TYR A CZ    1 
ATOM   2714 O  OH    . TYR A 1 369 ? -18.724 1.413   7.207   1.00 12.97 ? 349 TYR A OH    1 
ATOM   2715 N  N     . ILE A 1 370 ? -15.299 -6.351  6.263   1.00 8.76  ? 350 ILE A N     1 
ATOM   2716 C  CA    . ILE A 1 370 ? -14.450 -7.457  6.645   1.00 8.63  ? 350 ILE A CA    1 
ATOM   2717 C  C     . ILE A 1 370 ? -13.637 -6.941  7.823   1.00 8.09  ? 350 ILE A C     1 
ATOM   2718 O  O     . ILE A 1 370 ? -12.744 -6.131  7.603   1.00 8.27  ? 350 ILE A O     1 
ATOM   2719 C  CB    . ILE A 1 370 ? -13.529 -7.963  5.523   1.00 9.46  ? 350 ILE A CB    1 
ATOM   2720 C  CG1   . ILE A 1 370 ? -14.292 -8.418  4.259   1.00 10.48 ? 350 ILE A CG1   1 
ATOM   2721 C  CG2   . ILE A 1 370 ? -12.650 -9.056  6.037   1.00 10.24 ? 350 ILE A CG2   1 
ATOM   2722 C  CD1   . ILE A 1 370 ? -15.474 -9.257  4.537   1.00 11.26 ? 350 ILE A CD1   1 
ATOM   2723 N  N     . THR A 1 371 ? -13.982 -7.397  9.043   1.00 7.14  ? 351 THR A N     1 
ATOM   2724 C  CA    . THR A 1 371 ? -13.389 -6.832  10.240  1.00 7.05  ? 351 THR A CA    1 
ATOM   2725 C  C     . THR A 1 371 ? -12.130 -7.578  10.694  1.00 7.28  ? 351 THR A C     1 
ATOM   2726 O  O     . THR A 1 371 ? -11.377 -7.034  11.508  1.00 6.75  ? 351 THR A O     1 
ATOM   2727 C  CB    . THR A 1 371 ? -14.469 -6.674  11.305  1.00 7.07  ? 351 THR A CB    1 
ATOM   2728 O  OG1   . THR A 1 371 ? -15.276 -7.849  11.264  1.00 7.63  ? 351 THR A OG1   1 
ATOM   2729 C  CG2   . THR A 1 371 ? -15.364 -5.477  11.104  1.00 7.57  ? 351 THR A CG2   1 
ATOM   2730 N  N     . GLN A 1 372 ? -11.858 -8.784  10.177  1.00 6.55  ? 352 GLN A N     1 
ATOM   2731 C  CA    . GLN A 1 372 ? -10.626 -9.508  10.395  1.00 6.65  ? 352 GLN A CA    1 
ATOM   2732 C  C     . GLN A 1 372 ? -10.426 -10.476 9.229   1.00 7.28  ? 352 GLN A C     1 
ATOM   2733 O  O     . GLN A 1 372 ? -11.316 -11.265 8.912   1.00 7.77  ? 352 GLN A O     1 
ATOM   2734 C  CB    . GLN A 1 372 ? -10.613 -10.346 11.684  1.00 6.30  ? 352 GLN A CB    1 
ATOM   2735 C  CG    . GLN A 1 372 ? -10.913 -9.538  12.937  1.00 6.44  ? 352 GLN A CG    1 
ATOM   2736 C  CD    . GLN A 1 372 ? -10.818 -10.227 14.294  1.00 7.52  ? 352 GLN A CD    1 
ATOM   2737 O  OE1   . GLN A 1 372 ? -11.273 -9.650  15.296  1.00 8.10  ? 352 GLN A OE1   1 
ATOM   2738 N  NE2   . GLN A 1 372 ? -10.250 -11.429 14.334  1.00 7.01  ? 352 GLN A NE2   1 
ATOM   2739 N  N     . ASN A 1 373 ? -9.225  -10.474 8.681   1.00 7.69  ? 353 ASN A N     1 
ATOM   2740 C  CA    . ASN A 1 373 ? -8.838  -11.439 7.649   1.00 7.62  ? 353 ASN A CA    1 
ATOM   2741 C  C     . ASN A 1 373 ? -7.324  -11.394 7.605   1.00 7.19  ? 353 ASN A C     1 
ATOM   2742 O  O     . ASN A 1 373 ? -6.738  -10.332 7.424   1.00 8.32  ? 353 ASN A O     1 
ATOM   2743 C  CB    . ASN A 1 373 ? -9.462  -11.074 6.294   1.00 8.07  ? 353 ASN A CB    1 
ATOM   2744 C  CG    . ASN A 1 373 ? -8.984  -11.937 5.131   1.00 9.67  ? 353 ASN A CG    1 
ATOM   2745 O  OD1   . ASN A 1 373 ? -8.418  -11.464 4.135   1.00 10.24 ? 353 ASN A OD1   1 
ATOM   2746 N  ND2   . ASN A 1 373 ? -9.199  -13.234 5.266   1.00 9.61  ? 353 ASN A ND2   1 
ATOM   2747 N  N     . GLY A 1 374 ? -6.668  -12.519 7.751   1.00 8.17  ? 354 GLY A N     1 
ATOM   2748 C  CA    . GLY A 1 374 ? -5.223  -12.601 7.747   1.00 8.04  ? 354 GLY A CA    1 
ATOM   2749 C  C     . GLY A 1 374 ? -4.755  -14.037 8.005   1.00 8.79  ? 354 GLY A C     1 
ATOM   2750 O  O     . GLY A 1 374 ? -5.580  -14.936 8.025   1.00 10.02 ? 354 GLY A O     1 
ATOM   2751 N  N     . CYS A 1 375 ? -3.488  -14.193 8.153   1.00 9.45  ? 355 CYS A N     1 
ATOM   2752 C  CA    . CYS A 1 375 ? -2.895  -15.510 8.302   1.00 10.82 ? 355 CYS A CA    1 
ATOM   2753 C  C     . CYS A 1 375 ? -1.625  -15.496 9.144   1.00 9.59  ? 355 CYS A C     1 
ATOM   2754 O  O     . CYS A 1 375 ? -0.937  -14.504 9.376   1.00 8.45  ? 355 CYS A O     1 
ATOM   2755 C  CB    . CYS A 1 375 ? -2.672  -16.155 6.941   1.00 13.42 ? 355 CYS A CB    1 
ATOM   2756 S  SG    . CYS A 1 375 ? -1.344  -15.417 5.958   1.00 14.29 ? 355 CYS A SG    1 
ATOM   2757 N  N     . ALA A 1 376 ? -1.330  -16.720 9.620   1.00 9.34  ? 356 ALA A N     1 
ATOM   2758 C  CA    . ALA A 1 376 ? -0.201  -16.973 10.464  1.00 9.65  ? 356 ALA A CA    1 
ATOM   2759 C  C     . ALA A 1 376 ? 0.866   -17.740 9.695   1.00 10.14 ? 356 ALA A C     1 
ATOM   2760 O  O     . ALA A 1 376 ? 0.527   -18.608 8.869   1.00 12.28 ? 356 ALA A O     1 
ATOM   2761 C  CB    . ALA A 1 376 ? -0.654  -17.779 11.654  1.00 9.77  ? 356 ALA A CB    1 
ATOM   2762 N  N     . LEU A 1 377 ? 2.084   -17.326 9.913   1.00 11.26 ? 357 LEU A N     1 
ATOM   2763 C  CA    . LEU A 1 377 ? 3.247   -17.954 9.288   1.00 12.49 ? 357 LEU A CA    1 
ATOM   2764 C  C     . LEU A 1 377 ? 4.349   -18.089 10.309  1.00 12.20 ? 357 LEU A C     1 
ATOM   2765 O  O     . LEU A 1 377 ? 4.408   -17.434 11.362  1.00 12.91 ? 357 LEU A O     1 
ATOM   2766 C  CB    . LEU A 1 377 ? 3.752   -17.125 8.090   1.00 11.89 ? 357 LEU A CB    1 
ATOM   2767 C  CG    . LEU A 1 377 ? 2.780   -16.936 6.932   1.00 12.06 ? 357 LEU A CG    1 
ATOM   2768 C  CD1   . LEU A 1 377 ? 3.345   -15.951 5.922   1.00 12.54 ? 357 LEU A CD1   1 
ATOM   2769 C  CD2   . LEU A 1 377 ? 2.434   -18.246 6.227   1.00 12.28 ? 357 LEU A CD2   1 
ATOM   2770 N  N     . HIS A 1 378 ? 5.365   -18.857 9.921   1.00 12.61 ? 358 HIS A N     1 
ATOM   2771 C  CA    . HIS A 1 378 ? 6.537   -18.971 10.748  1.00 14.25 ? 358 HIS A CA    1 
ATOM   2772 C  C     . HIS A 1 378 ? 7.455   -17.799 10.408  1.00 15.17 ? 358 HIS A C     1 
ATOM   2773 O  O     . HIS A 1 378 ? 8.557   -18.007 9.920   1.00 15.19 ? 358 HIS A O     1 
ATOM   2774 C  CB    . HIS A 1 378 ? 7.165   -20.366 10.524  1.00 15.10 ? 358 HIS A CB    1 
ATOM   2775 C  CG    . HIS A 1 378 ? 6.256   -21.479 10.878  1.00 19.11 ? 358 HIS A CG    1 
ATOM   2776 N  ND1   . HIS A 1 378 ? 5.714   -22.464 10.057  1.00 23.19 ? 358 HIS A ND1   1 
ATOM   2777 C  CD2   . HIS A 1 378 ? 5.771   -21.705 12.124  1.00 18.16 ? 358 HIS A CD2   1 
ATOM   2778 C  CE1   . HIS A 1 378 ? 4.895   -23.238 10.793  1.00 19.10 ? 358 HIS A CE1   1 
ATOM   2779 N  NE2   . HIS A 1 378 ? 4.939   -22.786 12.046  1.00 22.75 ? 358 HIS A NE2   1 
ATOM   2780 N  N     . ASP A 1 379 ? 7.028   -16.571 10.744  1.00 14.79 ? 359 ASP A N     1 
ATOM   2781 C  CA    . ASP A 1 379 ? 7.750   -15.371 10.366  1.00 14.88 ? 359 ASP A CA    1 
ATOM   2782 C  C     . ASP A 1 379 ? 9.066   -15.269 11.100  1.00 14.47 ? 359 ASP A C     1 
ATOM   2783 O  O     . ASP A 1 379 ? 9.160   -15.583 12.285  1.00 16.01 ? 359 ASP A O     1 
ATOM   2784 C  CB    . ASP A 1 379 ? 6.969   -14.078 10.639  1.00 13.55 ? 359 ASP A CB    1 
ATOM   2785 C  CG    . ASP A 1 379 ? 5.676   -14.014 9.884   1.00 14.76 ? 359 ASP A CG    1 
ATOM   2786 O  OD1   . ASP A 1 379 ? 5.695   -14.144 8.648   1.00 17.05 ? 359 ASP A OD1   1 
ATOM   2787 O  OD2   . ASP A 1 379 ? 4.639   -13.962 10.546  1.00 15.32 ? 359 ASP A OD2   1 
ATOM   2788 N  N     . GLU A 1 380 ? 10.111  -14.873 10.365  1.00 15.79 ? 360 GLU A N     1 
ATOM   2789 C  CA    . GLU A 1 380 ? 11.413  -14.680 10.938  1.00 17.13 ? 360 GLU A CA    1 
ATOM   2790 C  C     . GLU A 1 380 ? 12.008  -13.420 10.325  1.00 16.32 ? 360 GLU A C     1 
ATOM   2791 O  O     . GLU A 1 380 ? 11.695  -13.058 9.196   1.00 15.48 ? 360 GLU A O     1 
ATOM   2792 C  CB    . GLU A 1 380 ? 12.309  -15.911 10.724  1.00 23.29 ? 360 GLU A CB    1 
ATOM   2793 C  CG    . GLU A 1 380 ? 12.497  -16.340 9.277   1.00 25.98 ? 360 GLU A CG    1 
ATOM   2794 C  CD    . GLU A 1 380 ? 13.024  -17.767 9.086   1.00 27.07 ? 360 GLU A CD    1 
ATOM   2795 O  OE1   . GLU A 1 380 ? 13.983  -18.122 9.808   1.00 27.30 ? 360 GLU A OE1   1 
ATOM   2796 O  OE2   . GLU A 1 380 ? 12.411  -18.560 8.278   1.00 22.22 ? 360 GLU A OE2   1 
ATOM   2797 N  N     . ILE A 1 381 ? 12.770  -12.721 11.144  1.00 14.99 ? 361 ILE A N     1 
ATOM   2798 C  CA    . ILE A 1 381 ? 13.571  -11.625 10.656  1.00 16.18 ? 361 ILE A CA    1 
ATOM   2799 C  C     . ILE A 1 381 ? 14.718  -12.188 9.837   1.00 16.12 ? 361 ILE A C     1 
ATOM   2800 O  O     . ILE A 1 381 ? 15.547  -12.975 10.326  1.00 18.30 ? 361 ILE A O     1 
ATOM   2801 C  CB    . ILE A 1 381 ? 14.051  -10.753 11.816  1.00 17.03 ? 361 ILE A CB    1 
ATOM   2802 C  CG1   . ILE A 1 381 ? 12.832  -10.104 12.488  1.00 18.55 ? 361 ILE A CG1   1 
ATOM   2803 C  CG2   . ILE A 1 381 ? 15.056  -9.733  11.319  1.00 19.80 ? 361 ILE A CG2   1 
ATOM   2804 C  CD1   . ILE A 1 381 ? 13.153  -9.172  13.625  1.00 19.68 ? 361 ILE A CD1   1 
ATOM   2805 N  N     . ALA A 1 382 ? 14.779  -11.715 8.594   1.00 15.85 ? 362 ALA A N     1 
ATOM   2806 C  CA    . ALA A 1 382 ? 15.807  -12.203 7.684   1.00 16.22 ? 362 ALA A CA    1 
ATOM   2807 C  C     . ALA A 1 382 ? 17.119  -11.451 7.879   1.00 17.92 ? 362 ALA A C     1 
ATOM   2808 O  O     . ALA A 1 382 ? 17.299  -10.532 8.684   1.00 15.52 ? 362 ALA A O     1 
ATOM   2809 C  CB    . ALA A 1 382 ? 15.287  -12.100 6.280   1.00 18.45 ? 362 ALA A CB    1 
ATOM   2810 N  N     . GLU A 1 383 ? 18.133  -11.929 7.153   1.00 17.47 ? 363 GLU A N     1 
ATOM   2811 C  CA    . GLU A 1 383 ? 19.468  -11.378 7.245   1.00 19.28 ? 363 GLU A CA    1 
ATOM   2812 C  C     . GLU A 1 383 ? 19.483  -9.871  6.980   1.00 18.36 ? 363 GLU A C     1 
ATOM   2813 O  O     . GLU A 1 383 ? 20.288  -9.151  7.571   1.00 18.79 ? 363 GLU A O     1 
ATOM   2814 C  CB    . GLU A 1 383 ? 20.301  -12.117 6.200   1.00 21.09 ? 363 GLU A CB    1 
ATOM   2815 C  CG    . GLU A 1 383 ? 21.743  -11.691 6.200   1.00 23.55 ? 363 GLU A CG    1 
ATOM   2816 C  CD    . GLU A 1 383 ? 22.536  -12.069 7.430   1.00 25.90 ? 363 GLU A CD    1 
ATOM   2817 O  OE1   . GLU A 1 383 ? 22.066  -12.925 8.218   1.00 27.66 ? 363 GLU A OE1   1 
ATOM   2818 O  OE2   . GLU A 1 383 ? 23.628  -11.525 7.572   1.00 30.03 ? 363 GLU A OE2   1 
ATOM   2819 N  N     . ASP A 1 384 ? 18.614  -9.417  6.071   1.00 16.51 ? 364 ASP A N     1 
ATOM   2820 C  CA    . ASP A 1 384 ? 18.530  -8.020  5.677   1.00 16.24 ? 364 ASP A CA    1 
ATOM   2821 C  C     . ASP A 1 384 ? 17.717  -7.217  6.697   1.00 17.16 ? 364 ASP A C     1 
ATOM   2822 O  O     . ASP A 1 384 ? 17.631  -6.007  6.596   1.00 17.79 ? 364 ASP A O     1 
ATOM   2823 C  CB    . ASP A 1 384 ? 17.867  -7.873  4.317   1.00 17.48 ? 364 ASP A CB    1 
ATOM   2824 C  CG    . ASP A 1 384 ? 16.487  -8.504  4.253   1.00 19.43 ? 364 ASP A CG    1 
ATOM   2825 O  OD1   . ASP A 1 384 ? 16.383  -9.760  4.009   1.00 20.55 ? 364 ASP A OD1   1 
ATOM   2826 O  OD2   . ASP A 1 384 ? 15.521  -7.780  4.468   1.00 20.77 ? 364 ASP A OD2   1 
ATOM   2827 N  N     . GLY A 1 385 ? 17.020  -7.896  7.603   1.00 15.85 ? 365 GLY A N     1 
ATOM   2828 C  CA    . GLY A 1 385 ? 16.244  -7.179  8.612   1.00 16.34 ? 365 GLY A CA    1 
ATOM   2829 C  C     . GLY A 1 385 ? 14.752  -7.118  8.342   1.00 17.67 ? 365 GLY A C     1 
ATOM   2830 O  O     . GLY A 1 385 ? 13.988  -6.808  9.257   1.00 19.73 ? 365 GLY A O     1 
ATOM   2831 N  N     . GLY A 1 386 ? 14.326  -7.449  7.124   1.00 15.90 ? 366 GLY A N     1 
ATOM   2832 C  CA    . GLY A 1 386 ? 12.910  -7.510  6.811   1.00 15.26 ? 366 GLY A CA    1 
ATOM   2833 C  C     . GLY A 1 386 ? 12.335  -8.868  7.163   1.00 14.15 ? 366 GLY A C     1 
ATOM   2834 O  O     . GLY A 1 386 ? 13.044  -9.787  7.599   1.00 15.16 ? 366 GLY A O     1 
ATOM   2835 N  N     . ILE A 1 387 ? 11.027  -8.988  6.965   1.00 12.60 ? 367 ILE A N     1 
ATOM   2836 C  CA    . ILE A 1 387 ? 10.322  -10.233 7.091   1.00 11.93 ? 367 ILE A CA    1 
ATOM   2837 C  C     . ILE A 1 387 ? 9.706   -10.543 5.747   1.00 11.99 ? 367 ILE A C     1 
ATOM   2838 O  O     . ILE A 1 387 ? 8.825   -9.835  5.281   1.00 10.82 ? 367 ILE A O     1 
ATOM   2839 C  CB    . ILE A 1 387 ? 9.225   -10.168 8.185   1.00 11.85 ? 367 ILE A CB    1 
ATOM   2840 C  CG1   . ILE A 1 387 ? 9.765   -9.770  9.559   1.00 12.04 ? 367 ILE A CG1   1 
ATOM   2841 C  CG2   . ILE A 1 387 ? 8.536   -11.509 8.255   1.00 13.16 ? 367 ILE A CG2   1 
ATOM   2842 C  CD1   . ILE A 1 387 ? 10.005  -8.338  9.812   1.00 12.39 ? 367 ILE A CD1   1 
ATOM   2843 N  N     . HIS A 1 388 ? 10.223  -11.591 5.078   1.00 12.85 ? 368 HIS A N     1 
ATOM   2844 C  CA    . HIS A 1 388 ? 9.757   -11.928 3.739   1.00 14.01 ? 368 HIS A CA    1 
ATOM   2845 C  C     . HIS A 1 388 ? 8.602   -12.919 3.766   1.00 14.94 ? 368 HIS A C     1 
ATOM   2846 O  O     . HIS A 1 388 ? 8.751   -14.116 3.496   1.00 14.78 ? 368 HIS A O     1 
ATOM   2847 C  CB    . HIS A 1 388 ? 10.949  -12.406 2.909   1.00 14.82 ? 368 HIS A CB    1 
ATOM   2848 C  CG    . HIS A 1 388 ? 12.088  -11.456 3.071   1.00 14.22 ? 368 HIS A CG    1 
ATOM   2849 N  ND1   . HIS A 1 388 ? 11.960  -10.110 2.807   1.00 14.01 ? 368 HIS A ND1   1 
ATOM   2850 C  CD2   . HIS A 1 388 ? 13.351  -11.646 3.441   1.00 17.33 ? 368 HIS A CD2   1 
ATOM   2851 C  CE1   . HIS A 1 388 ? 13.098  -9.512  3.127   1.00 14.76 ? 368 HIS A CE1   1 
ATOM   2852 N  NE2   . HIS A 1 388 ? 13.974  -10.434 3.503   1.00 15.64 ? 368 HIS A NE2   1 
ATOM   2853 N  N     . ASP A 1 389 ? 7.414   -12.404 4.063   1.00 12.68 ? 369 ASP A N     1 
ATOM   2854 C  CA    . ASP A 1 389 ? 6.203   -13.181 4.218   1.00 12.59 ? 369 ASP A CA    1 
ATOM   2855 C  C     . ASP A 1 389 ? 5.395   -13.210 2.926   1.00 12.79 ? 369 ASP A C     1 
ATOM   2856 O  O     . ASP A 1 389 ? 4.203   -12.900 2.880   1.00 10.79 ? 369 ASP A O     1 
ATOM   2857 C  CB    . ASP A 1 389 ? 5.421   -12.655 5.430   1.00 12.52 ? 369 ASP A CB    1 
ATOM   2858 C  CG    . ASP A 1 389 ? 4.957   -11.211 5.332   1.00 15.29 ? 369 ASP A CG    1 
ATOM   2859 O  OD1   . ASP A 1 389 ? 5.550   -10.474 4.549   1.00 14.18 ? 369 ASP A OD1   1 
ATOM   2860 O  OD2   . ASP A 1 389 ? 3.900   -10.888 5.960   1.00 13.58 ? 369 ASP A OD2   1 
ATOM   2861 N  N     . GLY A 1 390 ? 5.988   -13.770 1.851   1.00 11.67 ? 370 GLY A N     1 
ATOM   2862 C  CA    . GLY A 1 390 ? 5.269   -13.770 0.598   1.00 12.61 ? 370 GLY A CA    1 
ATOM   2863 C  C     . GLY A 1 390 ? 3.942   -14.492 0.620   1.00 11.70 ? 370 GLY A C     1 
ATOM   2864 O  O     . GLY A 1 390 ? 3.023   -14.121 -0.116  1.00 13.24 ? 370 GLY A O     1 
ATOM   2865 N  N     . GLN A 1 391 ? 3.828   -15.578 1.408   1.00 11.53 ? 371 GLN A N     1 
ATOM   2866 C  CA    . GLN A 1 391 ? 2.552   -16.269 1.399   1.00 11.67 ? 371 GLN A CA    1 
ATOM   2867 C  C     . GLN A 1 391 ? 1.448   -15.393 1.984   1.00 10.73 ? 371 GLN A C     1 
ATOM   2868 O  O     . GLN A 1 391 ? 0.294   -15.524 1.605   1.00 11.42 ? 371 GLN A O     1 
ATOM   2869 C  CB    . GLN A 1 391 ? 2.656   -17.600 2.165   1.00 12.42 ? 371 GLN A CB    1 
ATOM   2870 C  CG    . GLN A 1 391 ? 1.440   -18.483 1.974   1.00 12.73 ? 371 GLN A CG    1 
ATOM   2871 C  CD    . GLN A 1 391 ? 1.520   -19.804 2.710   1.00 13.12 ? 371 GLN A CD    1 
ATOM   2872 O  OE1   . GLN A 1 391 ? 2.412   -19.997 3.522   1.00 12.69 ? 371 GLN A OE1   1 
ATOM   2873 N  NE2   . GLN A 1 391 ? 0.546   -20.660 2.442   1.00 15.37 ? 371 GLN A NE2   1 
ATOM   2874 N  N     . ARG A 1 392 ? 1.811   -14.548 2.948   1.00 12.48 ? 372 ARG A N     1 
ATOM   2875 C  CA    . ARG A 1 392 ? 0.846   -13.610 3.514   1.00 11.04 ? 372 ARG A CA    1 
ATOM   2876 C  C     . ARG A 1 392 ? 0.516   -12.482 2.534   1.00 10.08 ? 372 ARG A C     1 
ATOM   2877 O  O     . ARG A 1 392 ? -0.639  -12.151 2.389   1.00 9.95  ? 372 ARG A O     1 
ATOM   2878 C  CB    . ARG A 1 392 ? 1.370   -13.014 4.827   1.00 11.03 ? 372 ARG A CB    1 
ATOM   2879 C  CG    . ARG A 1 392 ? 0.389   -12.054 5.468   1.00 10.13 ? 372 ARG A CG    1 
ATOM   2880 C  CD    . ARG A 1 392 ? 0.734   -11.538 6.845   1.00 10.70 ? 372 ARG A CD    1 
ATOM   2881 N  NE    . ARG A 1 392 ? 0.827   -12.616 7.845   1.00 10.61 ? 372 ARG A NE    1 
ATOM   2882 C  CZ    . ARG A 1 392 ? 1.973   -13.062 8.390   1.00 9.88  ? 372 ARG A CZ    1 
ATOM   2883 N  NH1   . ARG A 1 392 ? 3.155   -12.700 7.937   1.00 11.15 ? 372 ARG A NH1   1 
ATOM   2884 N  NH2   . ARG A 1 392 ? 1.945   -13.913 9.404   1.00 11.13 ? 372 ARG A NH2   1 
ATOM   2885 N  N     . GLN A 1 393 ? 1.500   -11.962 1.806   1.00 10.26 ? 373 GLN A N     1 
ATOM   2886 C  CA    . GLN A 1 393 ? 1.215   -11.059 0.709   1.00 12.03 ? 373 GLN A CA    1 
ATOM   2887 C  C     . GLN A 1 393 ? 0.231   -11.673 -0.277  1.00 12.63 ? 373 GLN A C     1 
ATOM   2888 O  O     . GLN A 1 393 ? -0.776  -11.076 -0.632  1.00 12.72 ? 373 GLN A O     1 
ATOM   2889 C  CB    . GLN A 1 393 ? 2.496   -10.611 0.008   1.00 13.54 ? 373 GLN A CB    1 
ATOM   2890 C  CG    . GLN A 1 393 ? 2.152   -9.684  -1.160  1.00 16.67 ? 373 GLN A CG    1 
ATOM   2891 C  CD    . GLN A 1 393 ? 3.375   -9.264  -1.913  1.00 22.74 ? 373 GLN A CD    1 
ATOM   2892 O  OE1   . GLN A 1 393 ? 4.361   -8.843  -1.324  1.00 26.23 ? 373 GLN A OE1   1 
ATOM   2893 N  NE2   . GLN A 1 393 ? 3.324   -9.401  -3.234  1.00 29.61 ? 373 GLN A NE2   1 
ATOM   2894 N  N     . ALA A 1 394 ? 0.531   -12.895 -0.735  1.00 13.53 ? 374 ALA A N     1 
ATOM   2895 C  CA    . ALA A 1 394 ? -0.363  -13.631 -1.629  1.00 14.71 ? 374 ALA A CA    1 
ATOM   2896 C  C     . ALA A 1 394 ? -1.732  -13.860 -0.999  1.00 12.75 ? 374 ALA A C     1 
ATOM   2897 O  O     . ALA A 1 394 ? -2.758  -13.814 -1.667  1.00 11.51 ? 374 ALA A O     1 
ATOM   2898 C  CB    . ALA A 1 394 ? 0.314   -14.934 -1.995  1.00 16.81 ? 374 ALA A CB    1 
ATOM   2899 N  N     . PHE A 1 395 ? -1.777  -14.117 0.333   1.00 13.48 ? 375 PHE A N     1 
ATOM   2900 C  CA    . PHE A 1 395 ? -3.052  -14.266 1.020   1.00 12.59 ? 375 PHE A CA    1 
ATOM   2901 C  C     . PHE A 1 395 ? -3.919  -13.018 0.872   1.00 10.68 ? 375 PHE A C     1 
ATOM   2902 O  O     . PHE A 1 395 ? -5.115  -13.054 0.535   1.00 11.14 ? 375 PHE A O     1 
ATOM   2903 C  CB    . PHE A 1 395 ? -2.749  -14.648 2.482   1.00 12.14 ? 375 PHE A CB    1 
ATOM   2904 C  CG    . PHE A 1 395 ? -3.964  -14.978 3.295   1.00 13.18 ? 375 PHE A CG    1 
ATOM   2905 C  CD1   . PHE A 1 395 ? -4.727  -13.975 3.864   1.00 13.13 ? 375 PHE A CD1   1 
ATOM   2906 C  CD2   . PHE A 1 395 ? -4.315  -16.295 3.536   1.00 13.98 ? 375 PHE A CD2   1 
ATOM   2907 C  CE1   . PHE A 1 395 ? -5.860  -14.278 4.586   1.00 13.30 ? 375 PHE A CE1   1 
ATOM   2908 C  CE2   . PHE A 1 395 ? -5.432  -16.595 4.289   1.00 14.10 ? 375 PHE A CE2   1 
ATOM   2909 C  CZ    . PHE A 1 395 ? -6.195  -15.588 4.822   1.00 13.19 ? 375 PHE A CZ    1 
ATOM   2910 N  N     . PHE A 1 396 ? -3.323  -11.853 1.155   1.00 11.33 ? 376 PHE A N     1 
ATOM   2911 C  CA    . PHE A 1 396 ? -4.027  -10.588 1.012   1.00 10.83 ? 376 PHE A CA    1 
ATOM   2912 C  C     . PHE A 1 396 ? -4.405  -10.328 -0.451  1.00 10.16 ? 376 PHE A C     1 
ATOM   2913 O  O     . PHE A 1 396 ? -5.525  -9.946  -0.717  1.00 11.45 ? 376 PHE A O     1 
ATOM   2914 C  CB    . PHE A 1 396 ? -3.237  -9.381  1.572   1.00 10.60 ? 376 PHE A CB    1 
ATOM   2915 C  CG    . PHE A 1 396 ? -3.102  -9.415  3.078   1.00 11.04 ? 376 PHE A CG    1 
ATOM   2916 C  CD1   . PHE A 1 396 ? -4.228  -9.423  3.871   1.00 11.37 ? 376 PHE A CD1   1 
ATOM   2917 C  CD2   . PHE A 1 396 ? -1.879  -9.326  3.674   1.00 12.71 ? 376 PHE A CD2   1 
ATOM   2918 C  CE1   . PHE A 1 396 ? -4.117  -9.486  5.249   1.00 12.12 ? 376 PHE A CE1   1 
ATOM   2919 C  CE2   . PHE A 1 396 ? -1.764  -9.325  5.060   1.00 13.78 ? 376 PHE A CE2   1 
ATOM   2920 C  CZ    . PHE A 1 396 ? -2.887  -9.441  5.825   1.00 11.42 ? 376 PHE A CZ    1 
ATOM   2921 N  N     . GLU A 1 397 ? -3.460  -10.490 -1.369  1.00 11.86 ? 377 GLU A N     1 
ATOM   2922 C  CA    . GLU A 1 397 ? -3.752  -10.271 -2.789  1.00 14.10 ? 377 GLU A CA    1 
ATOM   2923 C  C     . GLU A 1 397 ? -4.937  -11.119 -3.236  1.00 13.80 ? 377 GLU A C     1 
ATOM   2924 O  O     . GLU A 1 397 ? -5.892  -10.626 -3.847  1.00 14.76 ? 377 GLU A O     1 
ATOM   2925 C  CB    . GLU A 1 397 ? -2.581  -10.694 -3.672  1.00 18.71 ? 377 GLU A CB    1 
ATOM   2926 C  CG    . GLU A 1 397 ? -1.383  -9.793  -3.686  1.00 25.07 ? 377 GLU A CG    1 
ATOM   2927 C  CD    . GLU A 1 397 ? -0.650  -9.924  -5.020  1.00 32.95 ? 377 GLU A CD    1 
ATOM   2928 O  OE1   . GLU A 1 397 ? -1.315  -9.768  -6.063  1.00 40.14 ? 377 GLU A OE1   1 
ATOM   2929 O  OE2   . GLU A 1 397 ? 0.564   -10.205 -5.010  1.00 37.11 ? 377 GLU A OE2   1 
ATOM   2930 N  N     . ALA A 1 398 ? -4.963  -12.398 -2.815  1.00 14.03 ? 378 ALA A N     1 
ATOM   2931 C  CA    . ALA A 1 398 ? -6.005  -13.282 -3.285  1.00 13.61 ? 378 ALA A CA    1 
ATOM   2932 C  C     . ALA A 1 398 ? -7.342  -12.978 -2.654  1.00 12.34 ? 378 ALA A C     1 
ATOM   2933 O  O     . ALA A 1 398 ? -8.392  -13.068 -3.263  1.00 14.60 ? 378 ALA A O     1 
ATOM   2934 C  CB    . ALA A 1 398 ? -5.612  -14.712 -3.043  1.00 14.54 ? 378 ALA A CB    1 
ATOM   2935 N  N     . HIS A 1 399 ? -7.329  -12.604 -1.357  1.00 11.88 ? 379 HIS A N     1 
ATOM   2936 C  CA    . HIS A 1 399 ? -8.576  -12.329 -0.711  1.00 10.70 ? 379 HIS A CA    1 
ATOM   2937 C  C     . HIS A 1 399 ? -9.181  -11.011 -1.228  1.00 9.68  ? 379 HIS A C     1 
ATOM   2938 O  O     . HIS A 1 399 ? -10.376 -10.878 -1.317  1.00 10.62 ? 379 HIS A O     1 
ATOM   2939 C  CB    . HIS A 1 399 ? -8.423  -12.429 0.825   1.00 10.24 ? 379 HIS A CB    1 
ATOM   2940 C  CG    . HIS A 1 399 ? -8.328  -13.853 1.310   1.00 9.93  ? 379 HIS A CG    1 
ATOM   2941 N  ND1   . HIS A 1 399 ? -7.124  -14.507 1.280   1.00 11.06 ? 379 HIS A ND1   1 
ATOM   2942 C  CD2   . HIS A 1 399 ? -9.237  -14.693 1.879   1.00 10.73 ? 379 HIS A CD2   1 
ATOM   2943 C  CE1   . HIS A 1 399 ? -7.308  -15.736 1.789   1.00 11.09 ? 379 HIS A CE1   1 
ATOM   2944 N  NE2   . HIS A 1 399 ? -8.598  -15.880 2.113   1.00 10.54 ? 379 HIS A NE2   1 
ATOM   2945 N  N     . LEU A 1 400 ? -8.316  -10.012 -1.437  1.00 12.02 ? 380 LEU A N     1 
ATOM   2946 C  CA    . LEU A 1 400 ? -8.751  -8.719  -1.957  1.00 12.31 ? 380 LEU A CA    1 
ATOM   2947 C  C     . LEU A 1 400 ? -9.283  -8.891  -3.375  1.00 12.13 ? 380 LEU A C     1 
ATOM   2948 O  O     . LEU A 1 400 ? -10.282 -8.264  -3.683  1.00 12.74 ? 380 LEU A O     1 
ATOM   2949 C  CB    . LEU A 1 400 ? -7.610  -7.705  -1.867  1.00 12.42 ? 380 LEU A CB    1 
ATOM   2950 C  CG    . LEU A 1 400 ? -7.312  -7.237  -0.431  1.00 12.95 ? 380 LEU A CG    1 
ATOM   2951 C  CD1   . LEU A 1 400 ? -6.028  -6.389  -0.405  1.00 14.21 ? 380 LEU A CD1   1 
ATOM   2952 C  CD2   . LEU A 1 400 ? -8.501  -6.507  0.109   1.00 13.95 ? 380 LEU A CD2   1 
ATOM   2953 N  N     . ALA A 1 401 ? -8.726  -9.840  -4.120  1.00 13.75 ? 381 ALA A N     1 
ATOM   2954 C  CA    . ALA A 1 401 ? -9.288  -10.153 -5.435  1.00 14.84 ? 381 ALA A CA    1 
ATOM   2955 C  C     . ALA A 1 401 ? -10.717 -10.666 -5.330  1.00 14.78 ? 381 ALA A C     1 
ATOM   2956 O  O     . ALA A 1 401 ? -11.589 -10.331 -6.129  1.00 14.67 ? 381 ALA A O     1 
ATOM   2957 C  CB    . ALA A 1 401 ? -8.380  -11.109 -6.168  1.00 15.47 ? 381 ALA A CB    1 
ATOM   2958 N  N     . GLN A 1 402 ? -10.968 -11.569 -4.361  1.00 12.62 ? 382 GLN A N     1 
ATOM   2959 C  CA    . GLN A 1 402 ? -12.303 -12.058 -4.117  1.00 13.21 ? 382 GLN A CA    1 
ATOM   2960 C  C     . GLN A 1 402 ? -13.228 -10.953 -3.641  1.00 12.41 ? 382 GLN A C     1 
ATOM   2961 O  O     . GLN A 1 402 ? -14.391 -10.942 -3.972  1.00 12.88 ? 382 GLN A O     1 
ATOM   2962 C  CB    . GLN A 1 402 ? -12.225 -13.281 -3.181  1.00 14.14 ? 382 GLN A CB    1 
ATOM   2963 C  CG    . GLN A 1 402 ? -11.311 -14.376 -3.709  1.00 15.47 ? 382 GLN A CG    1 
ATOM   2964 C  CD    . GLN A 1 402 ? -11.901 -14.995 -4.949  1.00 16.59 ? 382 GLN A CD    1 
ATOM   2965 O  OE1   . GLN A 1 402 ? -13.105 -15.088 -5.054  1.00 18.18 ? 382 GLN A OE1   1 
ATOM   2966 N  NE2   . GLN A 1 402 ? -11.045 -15.385 -5.878  1.00 24.00 ? 382 GLN A NE2   1 
ATOM   2967 N  N     . LEU A 1 403 ? -12.712 -9.956  -2.869  1.00 11.99 ? 383 LEU A N     1 
ATOM   2968 C  CA    . LEU A 1 403 ? -13.538 -8.845  -2.484  1.00 13.04 ? 383 LEU A CA    1 
ATOM   2969 C  C     . LEU A 1 403 ? -13.917 -7.998  -3.707  1.00 11.26 ? 383 LEU A C     1 
ATOM   2970 O  O     . LEU A 1 403 ? -15.022 -7.548  -3.701  1.00 12.31 ? 383 LEU A O     1 
ATOM   2971 C  CB    . LEU A 1 403 ? -12.775 -7.959  -1.498  1.00 14.41 ? 383 LEU A CB    1 
ATOM   2972 C  CG    . LEU A 1 403 ? -12.524 -8.561  -0.126  1.00 19.27 ? 383 LEU A CG    1 
ATOM   2973 C  CD1   . LEU A 1 403 ? -11.995 -7.480  0.784   1.00 20.96 ? 383 LEU A CD1   1 
ATOM   2974 C  CD2   . LEU A 1 403 ? -13.796 -9.153  0.429   1.00 19.28 ? 383 LEU A CD2   1 
ATOM   2975 N  N     . GLN A 1 404 ? -13.012 -7.834  -4.672  1.00 12.66 ? 384 GLN A N     1 
ATOM   2976 C  CA    . GLN A 1 404 ? -13.323 -7.110  -5.918  1.00 13.13 ? 384 GLN A CA    1 
ATOM   2977 C  C     . GLN A 1 404 ? -14.453 -7.858  -6.638  1.00 13.21 ? 384 GLN A C     1 
ATOM   2978 O  O     . GLN A 1 404 ? -15.438 -7.238  -7.087  1.00 14.70 ? 384 GLN A O     1 
ATOM   2979 C  CB    . GLN A 1 404 ? -12.089 -6.991  -6.815  1.00 16.45 ? 384 GLN A CB    1 
ATOM   2980 C  CG    . GLN A 1 404 ? -11.035 -5.975  -6.356  1.00 21.12 ? 384 GLN A CG    1 
ATOM   2981 C  CD    . GLN A 1 404 ? -9.625  -6.440  -6.700  1.00 28.85 ? 384 GLN A CD    1 
ATOM   2982 O  OE1   . GLN A 1 404 ? -9.374  -7.176  -7.662  1.00 29.28 ? 384 GLN A OE1   1 
ATOM   2983 N  NE2   . GLN A 1 404 ? -8.657  -6.072  -5.871  1.00 34.38 ? 384 GLN A NE2   1 
ATOM   2984 N  N     . ARG A 1 405 ? -14.362 -9.189  -6.674  1.00 14.54 ? 385 ARG A N     1 
ATOM   2985 C  CA    . ARG A 1 405 ? -15.389 -9.998  -7.334  1.00 14.19 ? 385 ARG A CA    1 
ATOM   2986 C  C     . ARG A 1 405 ? -16.740 -9.833  -6.654  1.00 13.62 ? 385 ARG A C     1 
ATOM   2987 O  O     . ARG A 1 405 ? -17.815 -9.756  -7.277  1.00 14.19 ? 385 ARG A O     1 
ATOM   2988 C  CB    . ARG A 1 405 ? -15.019 -11.489 -7.413  1.00 16.35 ? 385 ARG A CB    1 
ATOM   2989 C  CG    . ARG A 1 405 ? -13.819 -11.829 -8.294  1.00 21.39 ? 385 ARG A CG    1 
ATOM   2990 C  CD    . ARG A 1 405 ? -13.549 -13.335 -8.406  1.00 27.63 ? 385 ARG A CD    1 
ATOM   2991 N  NE    . ARG A 1 405 ? -14.734 -14.082 -8.848  1.00 28.18 ? 385 ARG A NE    1 
ATOM   2992 C  CZ    . ARG A 1 405 ? -15.274 -15.189 -8.294  1.00 31.14 ? 385 ARG A CZ    1 
ATOM   2993 N  NH1   . ARG A 1 405 ? -14.742 -15.794 -7.248  1.00 26.07 ? 385 ARG A NH1   1 
ATOM   2994 N  NH2   . ARG A 1 405 ? -16.382 -15.703 -8.806  1.00 32.08 ? 385 ARG A NH2   1 
ATOM   2995 N  N     . ALA A 1 406 ? -16.726 -9.836  -5.296  1.00 11.44 ? 386 ALA A N     1 
ATOM   2996 C  CA    . ALA A 1 406 ? -17.932 -9.652  -4.523  1.00 10.96 ? 386 ALA A CA    1 
ATOM   2997 C  C     . ALA A 1 406 ? -18.551 -8.260  -4.714  1.00 10.99 ? 386 ALA A C     1 
ATOM   2998 O  O     . ALA A 1 406 ? -19.771 -8.092  -4.887  1.00 12.01 ? 386 ALA A O     1 
ATOM   2999 C  CB    . ALA A 1 406 ? -17.595 -10.025 -3.085  1.00 11.47 ? 386 ALA A CB    1 
ATOM   3000 N  N     . LEU A 1 407 ? -17.713 -7.216  -4.752  1.00 11.44 ? 387 LEU A N     1 
ATOM   3001 C  CA    . LEU A 1 407 ? -18.211 -5.885  -5.029  1.00 12.05 ? 387 LEU A CA    1 
ATOM   3002 C  C     . LEU A 1 407 ? -18.859 -5.872  -6.430  1.00 10.73 ? 387 LEU A C     1 
ATOM   3003 O  O     . LEU A 1 407 ? -19.917 -5.272  -6.547  1.00 11.55 ? 387 LEU A O     1 
ATOM   3004 C  CB    . LEU A 1 407 ? -17.065 -4.881  -4.908  1.00 13.61 ? 387 LEU A CB    1 
ATOM   3005 C  CG    . LEU A 1 407 ? -16.724 -4.465  -3.473  1.00 13.65 ? 387 LEU A CG    1 
ATOM   3006 C  CD1   . LEU A 1 407 ? -15.319 -3.933  -3.401  1.00 14.55 ? 387 LEU A CD1   1 
ATOM   3007 C  CD2   . LEU A 1 407 ? -17.690 -3.459  -2.949  1.00 13.07 ? 387 LEU A CD2   1 
ATOM   3008 N  N     . ALA A 1 408 ? -18.229 -6.546  -7.380  1.00 13.92 ? 388 ALA A N     1 
ATOM   3009 C  CA    . ALA A 1 408 ? -18.716 -6.604  -8.774  1.00 12.10 ? 388 ALA A CA    1 
ATOM   3010 C  C     . ALA A 1 408 ? -20.103 -7.241  -8.780  1.00 13.91 ? 388 ALA A C     1 
ATOM   3011 O  O     . ALA A 1 408 ? -20.990 -6.838  -9.526  1.00 10.57 ? 388 ALA A O     1 
ATOM   3012 C  CB    . ALA A 1 408 ? -17.700 -7.356  -9.624  1.00 14.56 ? 388 ALA A CB    1 
ATOM   3013 N  N     . ALA A 1 409 ? -20.335 -8.220  -7.899  1.00 12.72 ? 389 ALA A N     1 
ATOM   3014 C  CA    . ALA A 1 409 ? -21.624 -8.890  -7.809  1.00 13.54 ? 389 ALA A CA    1 
ATOM   3015 C  C     . ALA A 1 409 ? -22.677 -8.096  -7.050  1.00 13.13 ? 389 ALA A C     1 
ATOM   3016 O  O     . ALA A 1 409 ? -23.819 -8.515  -6.852  1.00 16.34 ? 389 ALA A O     1 
ATOM   3017 C  CB    . ALA A 1 409 ? -21.379 -10.254 -7.186  1.00 13.32 ? 389 ALA A CB    1 
ATOM   3018 N  N     . GLY A 1 410 ? -22.312 -6.937  -6.500  1.00 11.25 ? 390 GLY A N     1 
ATOM   3019 C  CA    . GLY A 1 410 ? -23.273 -6.079  -5.854  1.00 11.50 ? 390 GLY A CA    1 
ATOM   3020 C  C     . GLY A 1 410 ? -23.181 -6.135  -4.317  1.00 11.60 ? 390 GLY A C     1 
ATOM   3021 O  O     . GLY A 1 410 ? -23.990 -5.520  -3.666  1.00 12.97 ? 390 GLY A O     1 
ATOM   3022 N  N     . VAL A 1 411 ? -22.180 -6.840  -3.776  1.00 13.52 ? 391 VAL A N     1 
ATOM   3023 C  CA    . VAL A 1 411 ? -22.110 -6.952  -2.315  1.00 13.56 ? 391 VAL A CA    1 
ATOM   3024 C  C     . VAL A 1 411 ? -21.760 -5.560  -1.774  1.00 14.06 ? 391 VAL A C     1 
ATOM   3025 O  O     . VAL A 1 411 ? -20.774 -4.977  -2.233  1.00 12.93 ? 391 VAL A O     1 
ATOM   3026 C  CB    . VAL A 1 411 ? -21.088 -7.991  -1.856  1.00 14.97 ? 391 VAL A CB    1 
ATOM   3027 C  CG1   . VAL A 1 411 ? -21.016 -8.048  -0.322  1.00 15.82 ? 391 VAL A CG1   1 
ATOM   3028 C  CG2   . VAL A 1 411 ? -21.374 -9.363  -2.463  1.00 15.10 ? 391 VAL A CG2   1 
ATOM   3029 N  N     . PRO A 1 412 ? -22.514 -5.051  -0.777  1.00 13.60 ? 392 PRO A N     1 
ATOM   3030 C  CA    . PRO A 1 412 ? -22.297 -3.730  -0.199  1.00 12.67 ? 392 PRO A CA    1 
ATOM   3031 C  C     . PRO A 1 412 ? -21.190 -3.715  0.844   1.00 11.37 ? 392 PRO A C     1 
ATOM   3032 O  O     . PRO A 1 412 ? -21.484 -3.431  2.000   1.00 12.83 ? 392 PRO A O     1 
ATOM   3033 C  CB    . PRO A 1 412 ? -23.630 -3.356  0.445   1.00 13.49 ? 392 PRO A CB    1 
ATOM   3034 C  CG    . PRO A 1 412 ? -24.235 -4.703  0.809   1.00 15.31 ? 392 PRO A CG    1 
ATOM   3035 C  CD    . PRO A 1 412 ? -23.686 -5.709  -0.186  1.00 15.69 ? 392 PRO A CD    1 
ATOM   3036 N  N     . LEU A 1 413 ? -19.996 -3.959  0.365   1.00 11.59 ? 393 LEU A N     1 
ATOM   3037 C  CA    . LEU A 1 413 ? -18.800 -3.989  1.201   1.00 12.55 ? 393 LEU A CA    1 
ATOM   3038 C  C     . LEU A 1 413 ? -18.240 -2.574  1.323   1.00 12.80 ? 393 LEU A C     1 
ATOM   3039 O  O     . LEU A 1 413 ? -18.042 -1.908  0.311   1.00 12.47 ? 393 LEU A O     1 
ATOM   3040 C  CB    . LEU A 1 413 ? -17.819 -4.960  0.562   1.00 13.65 ? 393 LEU A CB    1 
ATOM   3041 C  CG    . LEU A 1 413 ? -16.542 -5.264  1.340   1.00 17.45 ? 393 LEU A CG    1 
ATOM   3042 C  CD1   . LEU A 1 413 ? -16.849 -6.105  2.579   1.00 18.75 ? 393 LEU A CD1   1 
ATOM   3043 C  CD2   . LEU A 1 413 ? -15.521 -5.978  0.485   1.00 18.43 ? 393 LEU A CD2   1 
ATOM   3044 N  N     . LYS A 1 414 ? -17.952 -2.134  2.554   1.00 11.31 ? 394 LYS A N     1 
ATOM   3045 C  CA    . LYS A 1 414 ? -17.531 -0.762  2.811   1.00 11.12 ? 394 LYS A CA    1 
ATOM   3046 C  C     . LYS A 1 414 ? -16.141 -0.694  3.449   1.00 10.11 ? 394 LYS A C     1 
ATOM   3047 O  O     . LYS A 1 414 ? -15.601 0.392   3.572   1.00 9.64  ? 394 LYS A O     1 
ATOM   3048 C  CB    . LYS A 1 414 ? -18.579 -0.021  3.638   1.00 14.07 ? 394 LYS A CB    1 
ATOM   3049 C  CG    . LYS A 1 414 ? -19.841 0.365   2.852   1.00 16.08 ? 394 LYS A CG    1 
ATOM   3050 C  CD    . LYS A 1 414 ? -20.642 1.408   3.550   1.00 21.82 ? 394 LYS A CD    1 
ATOM   3051 C  CE    . LYS A 1 414 ? -21.875 1.835   2.773   1.00 29.08 ? 394 LYS A CE    1 
ATOM   3052 N  NZ    . LYS A 1 414 ? -21.551 2.608   1.549   1.00 34.35 ? 394 LYS A NZ    1 
ATOM   3053 N  N     . GLY A 1 415 ? -15.539 -1.817  3.806   1.00 9.22  ? 395 GLY A N     1 
ATOM   3054 C  CA    . GLY A 1 415 ? -14.189 -1.733  4.335   1.00 8.90  ? 395 GLY A CA    1 
ATOM   3055 C  C     . GLY A 1 415 ? -13.534 -3.079  4.594   1.00 8.95  ? 395 GLY A C     1 
ATOM   3056 O  O     . GLY A 1 415 ? -14.197 -4.139  4.575   1.00 8.13  ? 395 GLY A O     1 
ATOM   3057 N  N     . TYR A 1 416 ? -12.247 -3.006  4.867   1.00 8.12  ? 396 TYR A N     1 
ATOM   3058 C  CA    . TYR A 1 416 ? -11.439 -4.193  5.048   1.00 8.11  ? 396 TYR A CA    1 
ATOM   3059 C  C     . TYR A 1 416 ? -10.420 -3.925  6.138   1.00 7.61  ? 396 TYR A C     1 
ATOM   3060 O  O     . TYR A 1 416 ? -9.668  -2.964  6.008   1.00 8.14  ? 396 TYR A O     1 
ATOM   3061 C  CB    . TYR A 1 416 ? -10.733 -4.578  3.760   1.00 9.01  ? 396 TYR A CB    1 
ATOM   3062 C  CG    . TYR A 1 416 ? -9.848  -5.779  3.884   1.00 8.52  ? 396 TYR A CG    1 
ATOM   3063 C  CD1   . TYR A 1 416 ? -10.356 -7.070  3.771   1.00 9.42  ? 396 TYR A CD1   1 
ATOM   3064 C  CD2   . TYR A 1 416 ? -8.494  -5.650  4.126   1.00 8.31  ? 396 TYR A CD2   1 
ATOM   3065 C  CE1   . TYR A 1 416 ? -9.519  -8.155  3.788   1.00 8.49  ? 396 TYR A CE1   1 
ATOM   3066 C  CE2   . TYR A 1 416 ? -7.651  -6.744  4.192   1.00 8.57  ? 396 TYR A CE2   1 
ATOM   3067 C  CZ    . TYR A 1 416 ? -8.169  -8.011  4.022   1.00 8.87  ? 396 TYR A CZ    1 
ATOM   3068 O  OH    . TYR A 1 416 ? -7.316  -9.067  4.132   1.00 11.20 ? 396 TYR A OH    1 
ATOM   3069 N  N     . PHE A 1 417 ? -10.384 -4.804  7.137   1.00 6.62  ? 397 PHE A N     1 
ATOM   3070 C  CA    . PHE A 1 417 ? -9.335  -4.717  8.153   1.00 6.93  ? 397 PHE A CA    1 
ATOM   3071 C  C     . PHE A 1 417 ? -8.512  -5.982  8.181   1.00 6.79  ? 397 PHE A C     1 
ATOM   3072 O  O     . PHE A 1 417 ? -9.028  -7.075  8.433   1.00 7.68  ? 397 PHE A O     1 
ATOM   3073 C  CB    . PHE A 1 417 ? -9.954  -4.566  9.555   1.00 6.89  ? 397 PHE A CB    1 
ATOM   3074 C  CG    . PHE A 1 417 ? -10.695 -3.284  9.791   1.00 6.79  ? 397 PHE A CG    1 
ATOM   3075 C  CD1   . PHE A 1 417 ? -12.008 -3.112  9.348   1.00 6.52  ? 397 PHE A CD1   1 
ATOM   3076 C  CD2   . PHE A 1 417 ? -10.058 -2.203  10.386  1.00 6.47  ? 397 PHE A CD2   1 
ATOM   3077 C  CE1   . PHE A 1 417 ? -12.689 -1.916  9.554   1.00 6.63  ? 397 PHE A CE1   1 
ATOM   3078 C  CE2   . PHE A 1 417 ? -10.744 -1.020  10.582  1.00 6.53  ? 397 PHE A CE2   1 
ATOM   3079 C  CZ    . PHE A 1 417 ? -12.043 -0.864  10.136  1.00 6.31  ? 397 PHE A CZ    1 
ATOM   3080 N  N     . ALA A 1 418 ? -7.215  -5.826  7.979   1.00 6.85  ? 398 ALA A N     1 
ATOM   3081 C  CA    . ALA A 1 418 ? -6.269  -6.912  8.073   1.00 7.08  ? 398 ALA A CA    1 
ATOM   3082 C  C     . ALA A 1 418 ? -6.124  -7.346  9.518   1.00 7.20  ? 398 ALA A C     1 
ATOM   3083 O  O     . ALA A 1 418 ? -5.963  -6.511  10.424  1.00 7.49  ? 398 ALA A O     1 
ATOM   3084 C  CB    . ALA A 1 418 ? -4.930  -6.468  7.547   1.00 7.76  ? 398 ALA A CB    1 
ATOM   3085 N  N     . TRP A 1 419 ? -6.179  -8.641  9.708   1.00 7.68  ? 399 TRP A N     1 
ATOM   3086 C  CA    . TRP A 1 419 ? -5.755  -9.248  10.972  1.00 7.99  ? 399 TRP A CA    1 
ATOM   3087 C  C     . TRP A 1 419 ? -4.319  -9.662  10.817  1.00 8.22  ? 399 TRP A C     1 
ATOM   3088 O  O     . TRP A 1 419 ? -4.042  -10.413 9.876   1.00 9.52  ? 399 TRP A O     1 
ATOM   3089 C  CB    . TRP A 1 419 ? -6.575  -10.482 11.318  1.00 8.67  ? 399 TRP A CB    1 
ATOM   3090 C  CG    . TRP A 1 419 ? -6.250  -10.927 12.712  1.00 8.50  ? 399 TRP A CG    1 
ATOM   3091 C  CD1   . TRP A 1 419 ? -5.436  -11.946 13.097  1.00 9.55  ? 399 TRP A CD1   1 
ATOM   3092 C  CD2   . TRP A 1 419 ? -6.715  -10.288 13.892  1.00 8.07  ? 399 TRP A CD2   1 
ATOM   3093 N  NE1   . TRP A 1 419 ? -5.348  -11.992 14.464  1.00 9.57  ? 399 TRP A NE1   1 
ATOM   3094 C  CE2   . TRP A 1 419 ? -6.150  -10.992 14.983  1.00 8.63  ? 399 TRP A CE2   1 
ATOM   3095 C  CE3   . TRP A 1 419 ? -7.570  -9.214  14.154  1.00 8.12  ? 399 TRP A CE3   1 
ATOM   3096 C  CZ2   . TRP A 1 419 ? -6.420  -10.634 16.306  1.00 8.91  ? 399 TRP A CZ2   1 
ATOM   3097 C  CZ3   . TRP A 1 419 ? -7.841  -8.871  15.461  1.00 8.19  ? 399 TRP A CZ3   1 
ATOM   3098 C  CH2   . TRP A 1 419 ? -7.275  -9.569  16.518  1.00 8.11  ? 399 TRP A CH2   1 
ATOM   3099 N  N     . SER A 1 420 ? -3.409  -9.248  11.681  1.00 6.51  ? 400 SER A N     1 
ATOM   3100 C  CA    . SER A 1 420 ? -3.595  -8.250  12.733  1.00 6.83  ? 400 SER A CA    1 
ATOM   3101 C  C     . SER A 1 420 ? -2.602  -7.134  12.438  1.00 6.55  ? 400 SER A C     1 
ATOM   3102 O  O     . SER A 1 420 ? -1.646  -7.338  11.705  1.00 7.23  ? 400 SER A O     1 
ATOM   3103 C  CB    . SER A 1 420 ? -3.333  -8.891  14.096  1.00 7.26  ? 400 SER A CB    1 
ATOM   3104 O  OG    . SER A 1 420 ? -3.401  -7.942  15.166  1.00 7.28  ? 400 SER A OG    1 
ATOM   3105 N  N     . LEU A 1 421 ? -2.736  -5.987  13.119  1.00 6.39  ? 401 LEU A N     1 
ATOM   3106 C  CA    . LEU A 1 421 ? -1.735  -4.961  12.976  1.00 6.09  ? 401 LEU A CA    1 
ATOM   3107 C  C     . LEU A 1 421 ? -0.379  -5.534  13.350  1.00 6.51  ? 401 LEU A C     1 
ATOM   3108 O  O     . LEU A 1 421 ? 0.596   -5.196  12.706  1.00 7.95  ? 401 LEU A O     1 
ATOM   3109 C  CB    . LEU A 1 421 ? -2.109  -3.768  13.871  1.00 5.89  ? 401 LEU A CB    1 
ATOM   3110 C  CG    . LEU A 1 421 ? -1.070  -2.643  13.886  1.00 6.81  ? 401 LEU A CG    1 
ATOM   3111 C  CD1   . LEU A 1 421 ? -0.895  -2.120  12.451  1.00 7.13  ? 401 LEU A CD1   1 
ATOM   3112 C  CD2   . LEU A 1 421 ? -1.462  -1.564  14.877  1.00 6.50  ? 401 LEU A CD2   1 
ATOM   3113 N  N     . LEU A 1 422 ? -0.304  -6.289  14.444  1.00 6.73  ? 402 LEU A N     1 
ATOM   3114 C  CA    . LEU A 1 422 ? 0.997   -6.791  14.839  1.00 7.86  ? 402 LEU A CA    1 
ATOM   3115 C  C     . LEU A 1 422 ? 0.834   -8.144  15.497  1.00 7.65  ? 402 LEU A C     1 
ATOM   3116 O  O     . LEU A 1 422 ? -0.255  -8.575  15.861  1.00 7.17  ? 402 LEU A O     1 
ATOM   3117 C  CB    . LEU A 1 422 ? 1.735   -5.807  15.731  1.00 9.02  ? 402 LEU A CB    1 
ATOM   3118 C  CG    . LEU A 1 422 ? 1.129   -5.536  17.128  1.00 10.33 ? 402 LEU A CG    1 
ATOM   3119 C  CD1   . LEU A 1 422 ? 2.053   -4.620  17.954  1.00 11.23 ? 402 LEU A CD1   1 
ATOM   3120 C  CD2   . LEU A 1 422 ? -0.208  -4.839  17.081  1.00 12.49 ? 402 LEU A CD2   1 
ATOM   3121 N  N     . ASP A 1 423 ? 1.957   -8.866  15.520  1.00 6.39  ? 403 ASP A N     1 
ATOM   3122 C  CA    . ASP A 1 423 ? 1.988   -10.153 16.175  1.00 6.72  ? 403 ASP A CA    1 
ATOM   3123 C  C     . ASP A 1 423 ? 1.556   -9.936  17.629  1.00 5.95  ? 403 ASP A C     1 
ATOM   3124 O  O     . ASP A 1 423 ? 1.992   -8.989  18.301  1.00 6.18  ? 403 ASP A O     1 
ATOM   3125 C  CB    . ASP A 1 423 ? 3.377   -10.785 16.106  1.00 7.37  ? 403 ASP A CB    1 
ATOM   3126 C  CG    . ASP A 1 423 ? 3.846   -11.033 14.679  1.00 7.68  ? 403 ASP A CG    1 
ATOM   3127 O  OD1   . ASP A 1 423 ? 3.023   -11.311 13.822  1.00 8.48  ? 403 ASP A OD1   1 
ATOM   3128 O  OD2   . ASP A 1 423 ? 5.074   -10.985 14.504  1.00 8.04  ? 403 ASP A OD2   1 
ATOM   3129 N  N     . ASN A 1 424 ? 0.760   -10.877 18.126  1.00 5.78  ? 404 ASN A N     1 
ATOM   3130 C  CA    . ASN A 1 424 ? 0.132   -10.660 19.425  1.00 6.19  ? 404 ASN A CA    1 
ATOM   3131 C  C     . ASN A 1 424 ? -0.046  -11.957 20.196  1.00 6.32  ? 404 ASN A C     1 
ATOM   3132 O  O     . ASN A 1 424 ? 0.365   -13.023 19.751  1.00 6.64  ? 404 ASN A O     1 
ATOM   3133 C  CB    . ASN A 1 424 ? -1.154  -9.881  19.181  1.00 7.24  ? 404 ASN A CB    1 
ATOM   3134 C  CG    . ASN A 1 424 ? -2.163  -10.699 18.429  1.00 7.42  ? 404 ASN A CG    1 
ATOM   3135 O  OD1   . ASN A 1 424 ? -2.576  -11.748 18.875  1.00 8.12  ? 404 ASN A OD1   1 
ATOM   3136 N  ND2   . ASN A 1 424 ? -2.536  -10.276 17.231  1.00 10.05 ? 404 ASN A ND2   1 
ATOM   3137 N  N     . PHE A 1 425 ? -0.704  -11.849 21.358  1.00 5.37  ? 405 PHE A N     1 
ATOM   3138 C  CA    . PHE A 1 425 ? -1.090  -13.020 22.128  1.00 5.11  ? 405 PHE A CA    1 
ATOM   3139 C  C     . PHE A 1 425 ? -2.329  -13.636 21.495  1.00 5.41  ? 405 PHE A C     1 
ATOM   3140 O  O     . PHE A 1 425 ? -3.444  -13.151 21.729  1.00 5.46  ? 405 PHE A O     1 
ATOM   3141 C  CB    . PHE A 1 425 ? -1.337  -12.591 23.574  1.00 4.79  ? 405 PHE A CB    1 
ATOM   3142 C  CG    . PHE A 1 425 ? -1.799  -13.687 24.483  1.00 4.88  ? 405 PHE A CG    1 
ATOM   3143 C  CD1   . PHE A 1 425 ? -0.872  -14.547 25.082  1.00 5.25  ? 405 PHE A CD1   1 
ATOM   3144 C  CD2   . PHE A 1 425 ? -3.149  -13.914 24.774  1.00 5.17  ? 405 PHE A CD2   1 
ATOM   3145 C  CE1   . PHE A 1 425 ? -1.276  -15.595 25.889  1.00 5.39  ? 405 PHE A CE1   1 
ATOM   3146 C  CE2   . PHE A 1 425 ? -3.538  -14.991 25.572  1.00 5.65  ? 405 PHE A CE2   1 
ATOM   3147 C  CZ    . PHE A 1 425 ? -2.625  -15.811 26.165  1.00 5.69  ? 405 PHE A CZ    1 
ATOM   3148 N  N     . GLU A 1 426 ? -2.172  -14.723 20.721  1.00 5.40  ? 406 GLU A N     1 
ATOM   3149 C  CA    . GLU A 1 426 ? -3.256  -15.377 20.014  1.00 6.14  ? 406 GLU A CA    1 
ATOM   3150 C  C     . GLU A 1 426 ? -3.919  -16.454 20.878  1.00 6.05  ? 406 GLU A C     1 
ATOM   3151 O  O     . GLU A 1 426 ? -3.952  -17.648 20.563  1.00 6.91  ? 406 GLU A O     1 
ATOM   3152 C  CB    . GLU A 1 426 ? -2.743  -15.947 18.690  1.00 7.07  ? 406 GLU A CB    1 
ATOM   3153 C  CG    . GLU A 1 426 ? -2.517  -14.855 17.675  1.00 8.09  ? 406 GLU A CG    1 
ATOM   3154 C  CD    . GLU A 1 426 ? -3.665  -14.119 17.017  1.00 9.14  ? 406 GLU A CD    1 
ATOM   3155 O  OE1   . GLU A 1 426 ? -4.867  -14.390 17.288  1.00 8.34  ? 406 GLU A OE1   1 
ATOM   3156 O  OE2   . GLU A 1 426 ? -3.317  -13.205 16.250  1.00 9.23  ? 406 GLU A OE2   1 
ATOM   3157 N  N     . TRP A 1 427 ? -4.466  -15.995 22.014  1.00 5.38  ? 407 TRP A N     1 
ATOM   3158 C  CA    . TRP A 1 427 ? -5.378  -16.795 22.811  1.00 5.95  ? 407 TRP A CA    1 
ATOM   3159 C  C     . TRP A 1 427 ? -4.689  -18.091 23.243  1.00 6.25  ? 407 TRP A C     1 
ATOM   3160 O  O     . TRP A 1 427 ? -3.604  -18.000 23.828  1.00 5.71  ? 407 TRP A O     1 
ATOM   3161 C  CB    . TRP A 1 427 ? -6.709  -16.947 22.059  1.00 5.75  ? 407 TRP A CB    1 
ATOM   3162 C  CG    . TRP A 1 427 ? -7.253  -15.641 21.594  1.00 5.79  ? 407 TRP A CG    1 
ATOM   3163 C  CD1   . TRP A 1 427 ? -7.497  -15.246 20.304  1.00 5.93  ? 407 TRP A CD1   1 
ATOM   3164 C  CD2   . TRP A 1 427 ? -7.660  -14.544 22.422  1.00 5.39  ? 407 TRP A CD2   1 
ATOM   3165 N  NE1   . TRP A 1 427 ? -8.039  -14.001 20.277  1.00 5.95  ? 407 TRP A NE1   1 
ATOM   3166 C  CE2   . TRP A 1 427 ? -8.153  -13.534 21.564  1.00 5.28  ? 407 TRP A CE2   1 
ATOM   3167 C  CE3   . TRP A 1 427 ? -7.737  -14.334 23.799  1.00 5.35  ? 407 TRP A CE3   1 
ATOM   3168 C  CZ2   . TRP A 1 427 ? -8.671  -12.353 22.059  1.00 5.42  ? 407 TRP A CZ2   1 
ATOM   3169 C  CZ3   . TRP A 1 427 ? -8.207  -13.126 24.279  1.00 5.58  ? 407 TRP A CZ3   1 
ATOM   3170 C  CH2   . TRP A 1 427 ? -8.687  -12.150 23.413  1.00 5.46  ? 407 TRP A CH2   1 
ATOM   3171 N  N     . ALA A 1 428 ? -5.286  -19.254 22.990  1.00 6.85  ? 408 ALA A N     1 
ATOM   3172 C  CA    . ALA A 1 428 ? -4.738  -20.523 23.470  1.00 7.03  ? 408 ALA A CA    1 
ATOM   3173 C  C     . ALA A 1 428 ? -3.397  -20.826 22.810  1.00 7.26  ? 408 ALA A C     1 
ATOM   3174 O  O     . ALA A 1 428 ? -2.691  -21.726 23.283  1.00 7.89  ? 408 ALA A O     1 
ATOM   3175 C  CB    . ALA A 1 428 ? -5.701  -21.645 23.275  1.00 7.78  ? 408 ALA A CB    1 
ATOM   3176 N  N     A MET A 1 429 ? -3.043  -20.156 21.710  0.50 7.98  ? 409 MET A N     1 
ATOM   3177 N  N     B MET A 1 429 ? -3.069  -20.138 21.723  0.50 6.63  ? 409 MET A N     1 
ATOM   3178 C  CA    A MET A 1 429 ? -1.759  -20.412 21.062  0.50 9.66  ? 409 MET A CA    1 
ATOM   3179 C  CA    B MET A 1 429 ? -1.817  -20.395 21.032  0.50 6.95  ? 409 MET A CA    1 
ATOM   3180 C  C     A MET A 1 429 ? -0.658  -19.523 21.634  0.50 8.53  ? 409 MET A C     1 
ATOM   3181 C  C     B MET A 1 429 ? -0.702  -19.495 21.565  0.50 7.14  ? 409 MET A C     1 
ATOM   3182 O  O     A MET A 1 429 ? 0.536   -19.692 21.365  0.50 8.44  ? 409 MET A O     1 
ATOM   3183 O  O     B MET A 1 429 ? 0.463   -19.649 21.201  0.50 7.29  ? 409 MET A O     1 
ATOM   3184 C  CB    A MET A 1 429 ? -1.844  -20.178 19.549  0.50 12.86 ? 409 MET A CB    1 
ATOM   3185 C  CB    B MET A 1 429 ? -2.011  -20.191 19.523  0.50 7.04  ? 409 MET A CB    1 
ATOM   3186 C  CG    A MET A 1 429 ? -2.657  -21.235 18.821  0.50 16.47 ? 409 MET A CG    1 
ATOM   3187 C  CG    B MET A 1 429 ? -2.952  -21.219 18.903  0.50 7.16  ? 409 MET A CG    1 
ATOM   3188 S  SD    A MET A 1 429 ? -2.262  -22.926 19.323  0.50 23.93 ? 409 MET A SD    1 
ATOM   3189 S  SD    B MET A 1 429 ? -3.115  -21.070 17.084  0.50 6.78  ? 409 MET A SD    1 
ATOM   3190 C  CE    A MET A 1 429 ? -0.489  -23.040 19.060  0.50 24.85 ? 409 MET A CE    1 
ATOM   3191 C  CE    B MET A 1 429 ? -4.034  -19.552 16.906  0.50 6.39  ? 409 MET A CE    1 
ATOM   3192 N  N     . GLY A 1 430 ? -1.028  -18.529 22.428  1.00 7.39  ? 410 GLY A N     1 
ATOM   3193 C  CA    . GLY A 1 430 ? -0.017  -17.696 23.049  1.00 7.56  ? 410 GLY A CA    1 
ATOM   3194 C  C     . GLY A 1 430 ? 0.653   -16.770 22.058  1.00 8.29  ? 410 GLY A C     1 
ATOM   3195 O  O     . GLY A 1 430 ? 0.082   -16.403 21.047  1.00 9.48  ? 410 GLY A O     1 
ATOM   3196 N  N     . LEU A 1 431 ? 1.896   -16.447 22.348  1.00 9.63  ? 411 LEU A N     1 
ATOM   3197 C  CA    . LEU A 1 431 ? 2.682   -15.588 21.482  1.00 11.12 ? 411 LEU A CA    1 
ATOM   3198 C  C     . LEU A 1 431 ? 3.266   -16.376 20.303  1.00 12.53 ? 411 LEU A C     1 
ATOM   3199 O  O     . LEU A 1 431 ? 3.942   -15.773 19.451  1.00 15.20 ? 411 LEU A O     1 
ATOM   3200 C  CB    . LEU A 1 431 ? 3.821   -14.991 22.304  1.00 10.40 ? 411 LEU A CB    1 
ATOM   3201 C  CG    . LEU A 1 431 ? 3.380   -14.122 23.481  1.00 11.59 ? 411 LEU A CG    1 
ATOM   3202 C  CD1   . LEU A 1 431 ? 4.543   -13.622 24.323  1.00 12.69 ? 411 LEU A CD1   1 
ATOM   3203 C  CD2   . LEU A 1 431 ? 2.554   -12.952 22.974  1.00 11.96 ? 411 LEU A CD2   1 
ATOM   3204 N  N     A SER A 1 432 ? 3.075   -17.691 20.227  0.50 12.21 ? 412 SER A N     1 
ATOM   3205 N  N     B SER A 1 432 ? 2.999   -17.686 20.275  0.50 12.01 ? 412 SER A N     1 
ATOM   3206 C  CA    A SER A 1 432 ? 3.796   -18.489 19.240  0.50 12.77 ? 412 SER A CA    1 
ATOM   3207 C  CA    B SER A 1 432 ? 3.650   -18.608 19.358  0.50 12.47 ? 412 SER A CA    1 
ATOM   3208 C  C     A SER A 1 432 ? 3.076   -18.604 17.899  0.50 12.09 ? 412 SER A C     1 
ATOM   3209 C  C     B SER A 1 432 ? 3.220   -18.376 17.912  0.50 12.10 ? 412 SER A C     1 
ATOM   3210 O  O     A SER A 1 432 ? 3.468   -19.405 17.050  0.50 11.51 ? 412 SER A O     1 
ATOM   3211 O  O     B SER A 1 432 ? 4.026   -18.603 17.022  0.50 12.39 ? 412 SER A O     1 
ATOM   3212 C  CB    A SER A 1 432 ? 4.044   -19.878 19.762  0.50 12.81 ? 412 SER A CB    1 
ATOM   3213 C  CB    B SER A 1 432 ? 3.483   -20.093 19.800  0.50 12.01 ? 412 SER A CB    1 
ATOM   3214 O  OG    A SER A 1 432 ? 4.747   -19.825 20.969  0.50 14.40 ? 412 SER A OG    1 
ATOM   3215 O  OG    B SER A 1 432 ? 2.192   -20.657 19.530  0.50 11.57 ? 412 SER A OG    1 
ATOM   3216 N  N     . MET A 1 433 ? 2.007   -17.835 17.668  1.00 11.40 ? 413 MET A N     1 
ATOM   3217 C  CA    . MET A 1 433 ? 1.336   -17.920 16.396  1.00 11.44 ? 413 MET A CA    1 
ATOM   3218 C  C     . MET A 1 433 ? 1.190   -16.488 15.861  1.00 11.67 ? 413 MET A C     1 
ATOM   3219 O  O     . MET A 1 433 ? 0.406   -15.703 16.384  1.00 11.87 ? 413 MET A O     1 
ATOM   3220 C  CB    . MET A 1 433 ? -0.044  -18.602 16.501  1.00 13.82 ? 413 MET A CB    1 
ATOM   3221 C  CG    . MET A 1 433 ? -0.631  -18.963 15.169  1.00 14.41 ? 413 MET A CG    1 
ATOM   3222 S  SD    . MET A 1 433 ? 0.322   -20.193 14.188  1.00 17.79 ? 413 MET A SD    1 
ATOM   3223 C  CE    . MET A 1 433 ? 0.207   -21.608 15.265  1.00 18.99 ? 413 MET A CE    1 
ATOM   3224 N  N     . ARG A 1 434 ? 2.019   -16.129 14.865  1.00 9.41  ? 414 ARG A N     1 
ATOM   3225 C  CA    . ARG A 1 434 ? 2.223   -14.762 14.401  1.00 8.51  ? 414 ARG A CA    1 
ATOM   3226 C  C     . ARG A 1 434 ? 1.308   -14.437 13.232  1.00 8.73  ? 414 ARG A C     1 
ATOM   3227 O  O     . ARG A 1 434 ? 1.435   -15.017 12.139  1.00 9.70  ? 414 ARG A O     1 
ATOM   3228 C  CB    . ARG A 1 434 ? 3.680   -14.555 13.977  1.00 9.00  ? 414 ARG A CB    1 
ATOM   3229 C  CG    . ARG A 1 434 ? 4.653   -14.506 15.126  1.00 8.70  ? 414 ARG A CG    1 
ATOM   3230 C  CD    . ARG A 1 434 ? 6.078   -14.370 14.669  1.00 8.91  ? 414 ARG A CD    1 
ATOM   3231 N  NE    . ARG A 1 434 ? 6.976   -14.413 15.802  1.00 9.78  ? 414 ARG A NE    1 
ATOM   3232 C  CZ    . ARG A 1 434 ? 7.265   -13.389 16.614  1.00 11.11 ? 414 ARG A CZ    1 
ATOM   3233 N  NH1   . ARG A 1 434 ? 6.703   -12.191 16.434  1.00 10.63 ? 414 ARG A NH1   1 
ATOM   3234 N  NH2   . ARG A 1 434 ? 8.059   -13.561 17.655  1.00 12.61 ? 414 ARG A NH2   1 
ATOM   3235 N  N     . TYR A 1 435 ? 0.329   -13.542 13.471  1.00 7.36  ? 415 TYR A N     1 
ATOM   3236 C  CA    . TYR A 1 435 ? -0.623  -13.138 12.465  1.00 7.87  ? 415 TYR A CA    1 
ATOM   3237 C  C     . TYR A 1 435 ? -0.425  -11.681 12.029  1.00 8.05  ? 415 TYR A C     1 
ATOM   3238 O  O     . TYR A 1 435 ? -1.228  -11.216 11.249  1.00 7.62  ? 415 TYR A O     1 
ATOM   3239 C  CB    . TYR A 1 435 ? -2.063  -13.242 12.979  1.00 7.92  ? 415 TYR A CB    1 
ATOM   3240 C  CG    . TYR A 1 435 ? -2.717  -14.590 12.865  1.00 7.62  ? 415 TYR A CG    1 
ATOM   3241 C  CD1   . TYR A 1 435 ? -2.625  -15.559 13.839  1.00 8.59  ? 415 TYR A CD1   1 
ATOM   3242 C  CD2   . TYR A 1 435 ? -3.574  -14.860 11.805  1.00 7.95  ? 415 TYR A CD2   1 
ATOM   3243 C  CE1   . TYR A 1 435 ? -3.300  -16.771 13.733  1.00 8.33  ? 415 TYR A CE1   1 
ATOM   3244 C  CE2   . TYR A 1 435 ? -4.237  -16.071 11.676  1.00 8.16  ? 415 TYR A CE2   1 
ATOM   3245 C  CZ    . TYR A 1 435 ? -4.127  -17.034 12.654  1.00 7.93  ? 415 TYR A CZ    1 
ATOM   3246 O  OH    . TYR A 1 435 ? -4.794  -18.240 12.512  1.00 10.07 ? 415 TYR A OH    1 
ATOM   3247 N  N     . GLY A 1 436 ? 0.579   -10.996 12.551  1.00 8.60  ? 416 GLY A N     1 
ATOM   3248 C  CA    . GLY A 1 436 ? 0.790   -9.584  12.247  1.00 7.88  ? 416 GLY A CA    1 
ATOM   3249 C  C     . GLY A 1 436 ? 1.149   -9.276  10.800  1.00 9.40  ? 416 GLY A C     1 
ATOM   3250 O  O     . GLY A 1 436 ? 1.783   -10.098 10.148  1.00 9.50  ? 416 GLY A O     1 
ATOM   3251 N  N     . ILE A 1 437 ? 0.765   -8.070  10.355  1.00 8.37  ? 417 ILE A N     1 
ATOM   3252 C  CA    . ILE A 1 437 ? 1.396   -7.457  9.189   1.00 9.26  ? 417 ILE A CA    1 
ATOM   3253 C  C     . ILE A 1 437 ? 2.660   -6.706  9.602   1.00 9.04  ? 417 ILE A C     1 
ATOM   3254 O  O     . ILE A 1 437 ? 3.470   -6.302  8.739   1.00 10.81 ? 417 ILE A O     1 
ATOM   3255 C  CB    . ILE A 1 437 ? 0.402   -6.607  8.384   1.00 8.51  ? 417 ILE A CB    1 
ATOM   3256 C  CG1   . ILE A 1 437 ? -0.100  -5.387  9.178   1.00 9.28  ? 417 ILE A CG1   1 
ATOM   3257 C  CG2   . ILE A 1 437 ? -0.715  -7.508  7.887   1.00 8.33  ? 417 ILE A CG2   1 
ATOM   3258 C  CD1   . ILE A 1 437 ? -1.216  -4.580  8.450   1.00 10.46 ? 417 ILE A CD1   1 
ATOM   3259 N  N     . CYS A 1 438 ? 2.851   -6.531  10.915  1.00 8.79  ? 418 CYS A N     1 
ATOM   3260 C  CA    . CYS A 1 438 ? 4.056   -6.071  11.550  1.00 8.50  ? 418 CYS A CA    1 
ATOM   3261 C  C     . CYS A 1 438 ? 4.533   -7.146  12.522  1.00 8.13  ? 418 CYS A C     1 
ATOM   3262 O  O     . CYS A 1 438 ? 3.760   -7.744  13.272  1.00 8.72  ? 418 CYS A O     1 
ATOM   3263 C  CB    . CYS A 1 438 ? 3.867   -4.761  12.284  1.00 8.60  ? 418 CYS A CB    1 
ATOM   3264 S  SG    . CYS A 1 438 ? 3.140   -3.441  11.276  1.00 10.68 ? 418 CYS A SG    1 
ATOM   3265 N  N     . TYR A 1 439 ? 5.843   -7.376  12.540  1.00 7.65  ? 419 TYR A N     1 
ATOM   3266 C  CA    . TYR A 1 439 ? 6.469   -8.325  13.426  1.00 8.79  ? 419 TYR A CA    1 
ATOM   3267 C  C     . TYR A 1 439 ? 6.654   -7.682  14.786  1.00 8.35  ? 419 TYR A C     1 
ATOM   3268 O  O     . TYR A 1 439 ? 7.116   -6.555  14.870  1.00 10.01 ? 419 TYR A O     1 
ATOM   3269 C  CB    . TYR A 1 439 ? 7.857   -8.675  12.877  1.00 9.14  ? 419 TYR A CB    1 
ATOM   3270 C  CG    . TYR A 1 439 ? 8.568   -9.784  13.602  1.00 9.98  ? 419 TYR A CG    1 
ATOM   3271 C  CD1   . TYR A 1 439 ? 9.355   -9.493  14.684  1.00 10.81 ? 419 TYR A CD1   1 
ATOM   3272 C  CD2   . TYR A 1 439 ? 8.438   -11.094 13.172  1.00 10.71 ? 419 TYR A CD2   1 
ATOM   3273 C  CE1   . TYR A 1 439 ? 10.052  -10.513 15.335  1.00 12.48 ? 419 TYR A CE1   1 
ATOM   3274 C  CE2   . TYR A 1 439 ? 9.129   -12.113 13.805  1.00 12.29 ? 419 TYR A CE2   1 
ATOM   3275 C  CZ    . TYR A 1 439 ? 9.932   -11.809 14.875  1.00 11.92 ? 419 TYR A CZ    1 
ATOM   3276 O  OH    . TYR A 1 439 ? 10.589  -12.873 15.492  1.00 16.76 ? 419 TYR A OH    1 
ATOM   3277 N  N     . THR A 1 440 ? 6.325   -8.410  15.869  1.00 8.41  ? 420 THR A N     1 
ATOM   3278 C  CA    . THR A 1 440 ? 6.569   -7.915  17.205  1.00 7.78  ? 420 THR A CA    1 
ATOM   3279 C  C     . THR A 1 440 ? 7.681   -8.740  17.872  1.00 8.29  ? 420 THR A C     1 
ATOM   3280 O  O     . THR A 1 440 ? 7.546   -9.955  18.046  1.00 8.37  ? 420 THR A O     1 
ATOM   3281 C  CB    . THR A 1 440 ? 5.341   -8.062  18.116  1.00 8.58  ? 420 THR A CB    1 
ATOM   3282 O  OG1   . THR A 1 440 ? 4.206   -7.463  17.472  1.00 7.81  ? 420 THR A OG1   1 
ATOM   3283 C  CG2   . THR A 1 440 ? 5.544   -7.385  19.458  1.00 8.46  ? 420 THR A CG2   1 
ATOM   3284 N  N     . ASN A 1 441 ? 8.758   -8.057  18.262  1.00 9.11  ? 421 ASN A N     1 
ATOM   3285 C  CA    . ASN A 1 441 ? 9.756   -8.681  19.119  1.00 10.66 ? 421 ASN A CA    1 
ATOM   3286 C  C     . ASN A 1 441 ? 9.214   -8.677  20.542  1.00 10.27 ? 421 ASN A C     1 
ATOM   3287 O  O     . ASN A 1 441 ? 9.062   -7.617  21.130  1.00 9.94  ? 421 ASN A O     1 
ATOM   3288 C  CB    . ASN A 1 441 ? 11.111  -7.995  18.974  1.00 11.60 ? 421 ASN A CB    1 
ATOM   3289 C  CG    . ASN A 1 441 ? 12.181  -8.675  19.794  1.00 15.26 ? 421 ASN A CG    1 
ATOM   3290 O  OD1   . ASN A 1 441 ? 11.951  -9.106  20.918  1.00 13.13 ? 421 ASN A OD1   1 
ATOM   3291 N  ND2   . ASN A 1 441 ? 13.369  -8.780  19.211  1.00 16.80 ? 421 ASN A ND2   1 
ATOM   3292 N  N     . PHE A 1 442 ? 8.774   -9.834  21.068  1.00 11.63 ? 422 PHE A N     1 
ATOM   3293 C  CA    . PHE A 1 442 ? 8.142   -9.829  22.389  1.00 12.52 ? 422 PHE A CA    1 
ATOM   3294 C  C     . PHE A 1 442 ? 9.103   -9.577  23.541  1.00 14.66 ? 422 PHE A C     1 
ATOM   3295 O  O     . PHE A 1 442 ? 8.642   -9.239  24.620  1.00 15.23 ? 422 PHE A O     1 
ATOM   3296 C  CB    . PHE A 1 442 ? 7.341   -11.111 22.604  1.00 10.65 ? 422 PHE A CB    1 
ATOM   3297 C  CG    . PHE A 1 442 ? 6.221   -11.233 21.615  1.00 10.14 ? 422 PHE A CG    1 
ATOM   3298 C  CD1   . PHE A 1 442 ? 5.169   -10.330 21.674  1.00 10.61 ? 422 PHE A CD1   1 
ATOM   3299 C  CD2   . PHE A 1 442 ? 6.205   -12.209 20.638  1.00 10.24 ? 422 PHE A CD2   1 
ATOM   3300 C  CE1   . PHE A 1 442 ? 4.111   -10.430 20.795  1.00 9.27  ? 422 PHE A CE1   1 
ATOM   3301 C  CE2   . PHE A 1 442 ? 5.127   -12.326 19.778  1.00 9.96  ? 422 PHE A CE2   1 
ATOM   3302 C  CZ    . PHE A 1 442 ? 4.084   -11.408 19.857  1.00 10.45 ? 422 PHE A CZ    1 
ATOM   3303 N  N     . GLU A 1 443 ? 10.414  -9.649  23.297  1.00 15.79 ? 423 GLU A N     1 
ATOM   3304 C  CA    . GLU A 1 443 ? 11.368  -9.378  24.360  1.00 18.45 ? 423 GLU A CA    1 
ATOM   3305 C  C     . GLU A 1 443 ? 11.675  -7.893  24.447  1.00 16.00 ? 423 GLU A C     1 
ATOM   3306 O  O     . GLU A 1 443 ? 11.659  -7.332  25.532  1.00 17.94 ? 423 GLU A O     1 
ATOM   3307 C  CB    . GLU A 1 443 ? 12.666  -10.147 24.131  1.00 24.52 ? 423 GLU A CB    1 
ATOM   3308 C  CG    . GLU A 1 443 ? 12.474  -11.646 24.125  1.00 32.83 ? 423 GLU A CG    1 
ATOM   3309 C  CD    . GLU A 1 443 ? 13.793  -12.406 24.225  1.00 51.09 ? 423 GLU A CD    1 
ATOM   3310 O  OE1   . GLU A 1 443 ? 14.869  -11.753 24.067  1.00 55.52 ? 423 GLU A OE1   1 
ATOM   3311 O  OE2   . GLU A 1 443 ? 13.755  -13.640 24.494  1.00 55.88 ? 423 GLU A OE2   1 
ATOM   3312 N  N     . THR A 1 444 ? 11.870  -7.238  23.304  1.00 13.38 ? 424 THR A N     1 
ATOM   3313 C  CA    . THR A 1 444 ? 12.228  -5.837  23.282  1.00 13.07 ? 424 THR A CA    1 
ATOM   3314 C  C     . THR A 1 444 ? 11.047  -4.903  23.013  1.00 12.27 ? 424 THR A C     1 
ATOM   3315 O  O     . THR A 1 444 ? 11.151  -3.689  23.232  1.00 12.74 ? 424 THR A O     1 
ATOM   3316 C  CB    . THR A 1 444 ? 13.218  -5.566  22.156  1.00 13.81 ? 424 THR A CB    1 
ATOM   3317 O  OG1   . THR A 1 444 ? 12.616  -5.761  20.885  1.00 12.48 ? 424 THR A OG1   1 
ATOM   3318 C  CG2   . THR A 1 444 ? 14.432  -6.484  22.227  1.00 14.75 ? 424 THR A CG2   1 
ATOM   3319 N  N     . LEU A 1 445 ? 9.990   -5.500  22.487  1.00 11.81 ? 425 LEU A N     1 
ATOM   3320 C  CA    . LEU A 1 445 ? 8.750   -4.815  22.102  1.00 11.73 ? 425 LEU A CA    1 
ATOM   3321 C  C     . LEU A 1 445 ? 8.909   -3.946  20.857  1.00 11.38 ? 425 LEU A C     1 
ATOM   3322 O  O     . LEU A 1 445 ? 8.007   -3.189  20.459  1.00 11.09 ? 425 LEU A O     1 
ATOM   3323 C  CB    . LEU A 1 445 ? 8.157   -4.046  23.279  1.00 13.00 ? 425 LEU A CB    1 
ATOM   3324 C  CG    . LEU A 1 445 ? 7.816   -4.983  24.433  1.00 15.79 ? 425 LEU A CG    1 
ATOM   3325 C  CD1   . LEU A 1 445 ? 7.731   -4.250  25.760  1.00 18.63 ? 425 LEU A CD1   1 
ATOM   3326 C  CD2   . LEU A 1 445 ? 6.564   -5.779  24.080  1.00 16.49 ? 425 LEU A CD2   1 
ATOM   3327 N  N     . GLU A 1 446 ? 10.022  -4.094  20.145  1.00 11.61 ? 426 GLU A N     1 
ATOM   3328 C  CA    . GLU A 1 446 ? 10.129  -3.458  18.839  1.00 11.48 ? 426 GLU A CA    1 
ATOM   3329 C  C     . GLU A 1 446 ? 9.149   -4.071  17.841  1.00 11.11 ? 426 GLU A C     1 
ATOM   3330 O  O     . GLU A 1 446 ? 8.917   -5.266  17.820  1.00 12.10 ? 426 GLU A O     1 
ATOM   3331 C  CB    . GLU A 1 446 ? 11.569  -3.669  18.331  1.00 13.87 ? 426 GLU A CB    1 
ATOM   3332 C  CG    . GLU A 1 446 ? 11.860  -3.042  16.972  1.00 16.20 ? 426 GLU A CG    1 
ATOM   3333 C  CD    . GLU A 1 446 ? 13.190  -3.409  16.312  1.00 20.39 ? 426 GLU A CD    1 
ATOM   3334 O  OE1   . GLU A 1 446 ? 13.982  -4.213  16.880  1.00 24.46 ? 426 GLU A OE1   1 
ATOM   3335 O  OE2   . GLU A 1 446 ? 13.425  -2.869  15.227  1.00 23.50 ? 426 GLU A OE2   1 
ATOM   3336 N  N     . ARG A 1 447 ? 8.615   -3.223  16.963  1.00 10.68 ? 427 ARG A N     1 
ATOM   3337 C  CA    . ARG A 1 447 ? 7.779   -3.625  15.859  1.00 9.65  ? 427 ARG A CA    1 
ATOM   3338 C  C     . ARG A 1 447 ? 8.469   -3.286  14.550  1.00 9.97  ? 427 ARG A C     1 
ATOM   3339 O  O     . ARG A 1 447 ? 9.112   -2.254  14.450  1.00 10.66 ? 427 ARG A O     1 
ATOM   3340 C  CB    . ARG A 1 447 ? 6.425   -2.900  15.852  1.00 9.85  ? 427 ARG A CB    1 
ATOM   3341 C  CG    . ARG A 1 447 ? 5.539   -3.028  17.084  1.00 10.21 ? 427 ARG A CG    1 
ATOM   3342 C  CD    . ARG A 1 447 ? 5.655   -1.922  18.108  1.00 10.32 ? 427 ARG A CD    1 
ATOM   3343 N  NE    . ARG A 1 447 ? 4.387   -1.771  18.858  1.00 10.76 ? 427 ARG A NE    1 
ATOM   3344 C  CZ    . ARG A 1 447 ? 4.132   -2.326  20.036  1.00 9.44  ? 427 ARG A CZ    1 
ATOM   3345 N  NH1   . ARG A 1 447 ? 5.071   -3.014  20.693  1.00 10.52 ? 427 ARG A NH1   1 
ATOM   3346 N  NH2   . ARG A 1 447 ? 2.936   -2.182  20.589  1.00 8.57  ? 427 ARG A NH2   1 
ATOM   3347 N  N     . ARG A 1 448 ? 8.343   -4.179  13.569  1.00 11.50 ? 428 ARG A N     1 
ATOM   3348 C  CA    . ARG A 1 448 ? 8.895   -3.991  12.234  1.00 11.53 ? 428 ARG A CA    1 
ATOM   3349 C  C     . ARG A 1 448 ? 7.856   -4.414  11.209  1.00 10.13 ? 428 ARG A C     1 
ATOM   3350 O  O     . ARG A 1 448 ? 7.276   -5.476  11.341  1.00 11.17 ? 428 ARG A O     1 
ATOM   3351 C  CB    . ARG A 1 448 ? 10.119  -4.918  12.157  1.00 16.42 ? 428 ARG A CB    1 
ATOM   3352 C  CG    . ARG A 1 448 ? 11.197  -4.530  11.184  1.00 24.70 ? 428 ARG A CG    1 
ATOM   3353 C  CD    . ARG A 1 448 ? 12.388  -5.413  11.505  1.00 24.03 ? 428 ARG A CD    1 
ATOM   3354 N  NE    . ARG A 1 448 ? 13.168  -5.011  12.668  1.00 26.10 ? 428 ARG A NE    1 
ATOM   3355 C  CZ    . ARG A 1 448 ? 14.449  -5.335  12.820  1.00 26.11 ? 428 ARG A CZ    1 
ATOM   3356 N  NH1   . ARG A 1 448 ? 15.026  -6.094  11.902  1.00 23.66 ? 428 ARG A NH1   1 
ATOM   3357 N  NH2   . ARG A 1 448 ? 15.155  -4.908  13.846  1.00 26.88 ? 428 ARG A NH2   1 
ATOM   3358 N  N     . ILE A 1 449 ? 7.625   -3.589  10.172  1.00 9.01  ? 429 ILE A N     1 
ATOM   3359 C  CA    . ILE A 1 449 ? 6.654   -3.883  9.160   1.00 8.95  ? 429 ILE A CA    1 
ATOM   3360 C  C     . ILE A 1 449 ? 7.179   -5.053  8.322   1.00 9.51  ? 429 ILE A C     1 
ATOM   3361 O  O     . ILE A 1 449 ? 8.342   -5.036  7.885   1.00 11.00 ? 429 ILE A O     1 
ATOM   3362 C  CB    . ILE A 1 449 ? 6.331   -2.621  8.324   1.00 9.29  ? 429 ILE A CB    1 
ATOM   3363 C  CG1   . ILE A 1 449 ? 5.802   -1.473  9.197   1.00 9.15  ? 429 ILE A CG1   1 
ATOM   3364 C  CG2   . ILE A 1 449 ? 5.406   -2.961  7.195   1.00 9.83  ? 429 ILE A CG2   1 
ATOM   3365 C  CD1   . ILE A 1 449 ? 5.630   -0.175  8.461   1.00 9.95  ? 429 ILE A CD1   1 
ATOM   3366 N  N     . LYS A 1 450 ? 6.323   -6.033  8.102   1.00 9.44  ? 430 LYS A N     1 
ATOM   3367 C  CA    . LYS A 1 450 ? 6.643   -7.172  7.244   1.00 9.54  ? 430 LYS A CA    1 
ATOM   3368 C  C     . LYS A 1 450 ? 6.418   -6.785  5.786   1.00 9.59  ? 430 LYS A C     1 
ATOM   3369 O  O     . LYS A 1 450 ? 5.674   -5.867  5.430   1.00 8.67  ? 430 LYS A O     1 
ATOM   3370 C  CB    . LYS A 1 450 ? 5.778   -8.381  7.600   1.00 9.57  ? 430 LYS A CB    1 
ATOM   3371 C  CG    . LYS A 1 450 ? 5.815   -8.775  9.073   1.00 8.65  ? 430 LYS A CG    1 
ATOM   3372 C  CD    . LYS A 1 450 ? 5.002   -9.990  9.382   1.00 8.40  ? 430 LYS A CD    1 
ATOM   3373 C  CE    . LYS A 1 450 ? 4.977   -10.357 10.870  1.00 8.16  ? 430 LYS A CE    1 
ATOM   3374 N  NZ    . LYS A 1 450 ? 3.962   -11.398 11.176  1.00 7.81  ? 430 LYS A NZ    1 
ATOM   3375 N  N     . ASP A 1 451 ? 6.931   -7.615  4.859   1.00 10.57 ? 431 ASP A N     1 
ATOM   3376 C  CA    . ASP A 1 451 ? 6.726   -7.287  3.461   1.00 11.36 ? 431 ASP A CA    1 
ATOM   3377 C  C     . ASP A 1 451 ? 5.272   -7.202  3.046   1.00 11.17 ? 431 ASP A C     1 
ATOM   3378 O  O     . ASP A 1 451 ? 4.909   -6.379  2.191   1.00 13.00 ? 431 ASP A O     1 
ATOM   3379 C  CB    . ASP A 1 451 ? 7.425   -8.289  2.546   1.00 12.09 ? 431 ASP A CB    1 
ATOM   3380 C  CG    . ASP A 1 451 ? 8.931   -8.193  2.585   1.00 13.57 ? 431 ASP A CG    1 
ATOM   3381 O  OD1   . ASP A 1 451 ? 9.473   -7.220  3.108   1.00 12.95 ? 431 ASP A OD1   1 
ATOM   3382 O  OD2   . ASP A 1 451 ? 9.582   -9.124  1.984   1.00 13.38 ? 431 ASP A OD2   1 
ATOM   3383 N  N     . SER A 1 452 ? 4.416   -8.029  3.634   1.00 9.04  ? 432 SER A N     1 
ATOM   3384 C  CA    . SER A 1 452 ? 3.006   -7.981  3.333   1.00 10.08 ? 432 SER A CA    1 
ATOM   3385 C  C     . SER A 1 452 ? 2.442   -6.618  3.739   1.00 9.56  ? 432 SER A C     1 
ATOM   3386 O  O     . SER A 1 452 ? 1.535   -6.117  3.082   1.00 11.47 ? 432 SER A O     1 
ATOM   3387 C  CB    . SER A 1 452 ? 2.258   -9.109  3.950   1.00 11.26 ? 432 SER A CB    1 
ATOM   3388 O  OG    . SER A 1 452 ? 2.320   -9.078  5.378   1.00 11.57 ? 432 SER A OG    1 
ATOM   3389 N  N     . GLY A 1 453 ? 2.935   -6.062  4.838   1.00 9.64  ? 433 GLY A N     1 
ATOM   3390 C  CA    . GLY A 1 453 ? 2.480   -4.745  5.264   1.00 10.73 ? 433 GLY A CA    1 
ATOM   3391 C  C     . GLY A 1 453 ? 2.824   -3.689  4.204   1.00 10.93 ? 433 GLY A C     1 
ATOM   3392 O  O     . GLY A 1 453 ? 2.004   -2.831  3.893   1.00 10.22 ? 433 GLY A O     1 
ATOM   3393 N  N     . TYR A 1 454 ? 4.063   -3.736  3.683   1.00 10.68 ? 434 TYR A N     1 
ATOM   3394 C  CA    . TYR A 1 454 ? 4.441   -2.773  2.656   1.00 11.55 ? 434 TYR A CA    1 
ATOM   3395 C  C     . TYR A 1 454 ? 3.636   -3.005  1.382   1.00 10.86 ? 434 TYR A C     1 
ATOM   3396 O  O     . TYR A 1 454 ? 3.381   -2.045  0.628   1.00 11.05 ? 434 TYR A O     1 
ATOM   3397 C  CB    . TYR A 1 454 ? 5.931   -2.792  2.355   1.00 12.53 ? 434 TYR A CB    1 
ATOM   3398 C  CG    . TYR A 1 454 ? 6.768   -2.206  3.445   1.00 12.40 ? 434 TYR A CG    1 
ATOM   3399 C  CD1   . TYR A 1 454 ? 6.579   -0.903  3.879   1.00 12.69 ? 434 TYR A CD1   1 
ATOM   3400 C  CD2   . TYR A 1 454 ? 7.706   -2.989  4.106   1.00 13.22 ? 434 TYR A CD2   1 
ATOM   3401 C  CE1   . TYR A 1 454 ? 7.355   -0.373  4.890   1.00 14.89 ? 434 TYR A CE1   1 
ATOM   3402 C  CE2   . TYR A 1 454 ? 8.487   -2.465  5.128   1.00 13.28 ? 434 TYR A CE2   1 
ATOM   3403 C  CZ    . TYR A 1 454 ? 8.310   -1.152  5.505   1.00 14.29 ? 434 TYR A CZ    1 
ATOM   3404 O  OH    . TYR A 1 454 ? 9.004   -0.588  6.521   1.00 17.89 ? 434 TYR A OH    1 
ATOM   3405 N  N     . TRP A 1 455 ? 3.264   -4.261  1.096   1.00 10.35 ? 435 TRP A N     1 
ATOM   3406 C  CA    . TRP A 1 455 ? 2.426   -4.520  -0.061  1.00 9.69  ? 435 TRP A CA    1 
ATOM   3407 C  C     . TRP A 1 455 ? 1.072   -3.849  0.137   1.00 9.35  ? 435 TRP A C     1 
ATOM   3408 O  O     . TRP A 1 455 ? 0.524   -3.164  -0.723  1.00 10.23 ? 435 TRP A O     1 
ATOM   3409 C  CB    . TRP A 1 455 ? 2.325   -6.025  -0.422  1.00 10.71 ? 435 TRP A CB    1 
ATOM   3410 C  CG    . TRP A 1 455 ? 1.453   -6.223  -1.623  1.00 11.09 ? 435 TRP A CG    1 
ATOM   3411 C  CD1   . TRP A 1 455 ? 1.875   -6.179  -2.921  1.00 12.56 ? 435 TRP A CD1   1 
ATOM   3412 C  CD2   . TRP A 1 455 ? 0.027   -6.353  -1.685  1.00 11.94 ? 435 TRP A CD2   1 
ATOM   3413 N  NE1   . TRP A 1 455 ? 0.825   -6.281  -3.767  1.00 14.06 ? 435 TRP A NE1   1 
ATOM   3414 C  CE2   . TRP A 1 455 ? -0.337  -6.374  -3.048  1.00 12.80 ? 435 TRP A CE2   1 
ATOM   3415 C  CE3   . TRP A 1 455 ? -1.002  -6.452  -0.744  1.00 11.37 ? 435 TRP A CE3   1 
ATOM   3416 C  CZ2   . TRP A 1 455 ? -1.650  -6.477  -3.479  1.00 14.45 ? 435 TRP A CZ2   1 
ATOM   3417 C  CZ3   . TRP A 1 455 ? -2.305  -6.561  -1.160  1.00 12.89 ? 435 TRP A CZ3   1 
ATOM   3418 C  CH2   . TRP A 1 455 ? -2.636  -6.566  -2.520  1.00 15.12 ? 435 TRP A CH2   1 
ATOM   3419 N  N     . LEU A 1 456 ? 0.469   -4.012  1.328   1.00 9.27  ? 436 LEU A N     1 
ATOM   3420 C  CA    . LEU A 1 456 ? -0.814  -3.399  1.597   1.00 9.51  ? 436 LEU A CA    1 
ATOM   3421 C  C     . LEU A 1 456 ? -0.695  -1.870  1.487   1.00 9.53  ? 436 LEU A C     1 
ATOM   3422 O  O     . LEU A 1 456 ? -1.556  -1.229  0.916   1.00 9.49  ? 436 LEU A O     1 
ATOM   3423 C  CB    . LEU A 1 456 ? -1.266  -3.785  3.014   1.00 11.00 ? 436 LEU A CB    1 
ATOM   3424 C  CG    . LEU A 1 456 ? -1.863  -5.185  3.151   1.00 13.16 ? 436 LEU A CG    1 
ATOM   3425 C  CD1   . LEU A 1 456 ? -2.086  -5.540  4.628   1.00 14.49 ? 436 LEU A CD1   1 
ATOM   3426 C  CD2   . LEU A 1 456 ? -3.176  -5.317  2.405   1.00 14.79 ? 436 LEU A CD2   1 
ATOM   3427 N  N     . ARG A 1 457 ? 0.385   -1.293  2.015   1.00 8.88  ? 437 ARG A N     1 
ATOM   3428 C  CA    . ARG A 1 457 ? 0.596   0.148   1.946   1.00 8.89  ? 437 ARG A CA    1 
ATOM   3429 C  C     . ARG A 1 457 ? 0.484   0.598   0.494   1.00 9.27  ? 437 ARG A C     1 
ATOM   3430 O  O     . ARG A 1 457 ? -0.214  1.563   0.183   1.00 8.75  ? 437 ARG A O     1 
ATOM   3431 C  CB    . ARG A 1 457 ? 1.936   0.520   2.554   1.00 9.39  ? 437 ARG A CB    1 
ATOM   3432 C  CG    . ARG A 1 457 ? 2.331   1.977   2.430   1.00 8.88  ? 437 ARG A CG    1 
ATOM   3433 C  CD    . ARG A 1 457 ? 3.799   2.270   2.667   1.00 9.22  ? 437 ARG A CD    1 
ATOM   3434 N  NE    . ARG A 1 457 ? 4.614   1.693   1.617   1.00 9.91  ? 437 ARG A NE    1 
ATOM   3435 C  CZ    . ARG A 1 457 ? 5.933   1.744   1.592   1.00 10.74 ? 437 ARG A CZ    1 
ATOM   3436 N  NH1   . ARG A 1 457 ? 6.613   2.337   2.556   1.00 10.42 ? 437 ARG A NH1   1 
ATOM   3437 N  NH2   . ARG A 1 457 ? 6.572   1.124   0.602   1.00 12.45 ? 437 ARG A NH2   1 
ATOM   3438 N  N     . ASP A 1 458 ? 1.215   -0.118  -0.373  1.00 10.07 ? 438 ASP A N     1 
ATOM   3439 C  CA    . ASP A 1 458 ? 1.318   0.340   -1.748  1.00 11.23 ? 438 ASP A CA    1 
ATOM   3440 C  C     . ASP A 1 458 ? 0.045   0.082   -2.526  1.00 11.08 ? 438 ASP A C     1 
ATOM   3441 O  O     . ASP A 1 458 ? -0.293  0.877   -3.415  1.00 12.20 ? 438 ASP A O     1 
ATOM   3442 C  CB    . ASP A 1 458 ? 2.566   -0.265  -2.357  1.00 12.48 ? 438 ASP A CB    1 
ATOM   3443 C  CG    . ASP A 1 458 ? 3.834   0.250   -1.701  1.00 15.06 ? 438 ASP A CG    1 
ATOM   3444 O  OD1   . ASP A 1 458 ? 3.778   1.350   -1.084  1.00 16.72 ? 438 ASP A OD1   1 
ATOM   3445 O  OD2   . ASP A 1 458 ? 4.876   -0.466  -1.803  1.00 17.44 ? 438 ASP A OD2   1 
ATOM   3446 N  N     . PHE A 1 459 ? -0.651  -1.018  -2.204  1.00 11.07 ? 439 PHE A N     1 
ATOM   3447 C  CA    . PHE A 1 459 ? -1.922  -1.330  -2.832  1.00 11.87 ? 439 PHE A CA    1 
ATOM   3448 C  C     . PHE A 1 459 ? -2.945  -0.262  -2.468  1.00 12.47 ? 439 PHE A C     1 
ATOM   3449 O  O     . PHE A 1 459 ? -3.632  0.281   -3.338  1.00 12.43 ? 439 PHE A O     1 
ATOM   3450 C  CB    . PHE A 1 459 ? -2.417  -2.733  -2.442  1.00 13.56 ? 439 PHE A CB    1 
ATOM   3451 C  CG    . PHE A 1 459 ? -3.760  -3.058  -3.024  1.00 15.26 ? 439 PHE A CG    1 
ATOM   3452 C  CD1   . PHE A 1 459 ? -3.858  -3.439  -4.359  1.00 18.98 ? 439 PHE A CD1   1 
ATOM   3453 C  CD2   . PHE A 1 459 ? -4.931  -2.903  -2.309  1.00 15.69 ? 439 PHE A CD2   1 
ATOM   3454 C  CE1   . PHE A 1 459 ? -5.079  -3.765  -4.931  1.00 19.18 ? 439 PHE A CE1   1 
ATOM   3455 C  CE2   . PHE A 1 459 ? -6.153  -3.154  -2.911  1.00 16.30 ? 439 PHE A CE2   1 
ATOM   3456 C  CZ    . PHE A 1 459 ? -6.225  -3.594  -4.211  1.00 18.42 ? 439 PHE A CZ    1 
ATOM   3457 N  N     . ILE A 1 460 ? -3.031  0.066   -1.166  1.00 10.54 ? 440 ILE A N     1 
ATOM   3458 C  CA    . ILE A 1 460 ? -3.972  1.069   -0.707  1.00 11.46 ? 440 ILE A CA    1 
ATOM   3459 C  C     . ILE A 1 460 ? -3.634  2.426   -1.314  1.00 14.22 ? 440 ILE A C     1 
ATOM   3460 O  O     . ILE A 1 460 ? -4.516  3.157   -1.726  1.00 15.03 ? 440 ILE A O     1 
ATOM   3461 C  CB    . ILE A 1 460 ? -3.970  1.136   0.827   1.00 11.81 ? 440 ILE A CB    1 
ATOM   3462 C  CG1   . ILE A 1 460 ? -4.481  -0.197  1.368   1.00 12.23 ? 440 ILE A CG1   1 
ATOM   3463 C  CG2   . ILE A 1 460 ? -4.807  2.306   1.295   1.00 12.66 ? 440 ILE A CG2   1 
ATOM   3464 C  CD1   . ILE A 1 460 ? -4.252  -0.402  2.848   1.00 12.82 ? 440 ILE A CD1   1 
ATOM   3465 N  N     . ALA A 1 461 ? -2.351  2.756   -1.417  1.00 13.14 ? 441 ALA A N     1 
ATOM   3466 C  CA    . ALA A 1 461 ? -1.957  4.052   -1.972  1.00 17.12 ? 441 ALA A CA    1 
ATOM   3467 C  C     . ALA A 1 461 ? -2.275  4.130   -3.468  1.00 18.71 ? 441 ALA A C     1 
ATOM   3468 O  O     . ALA A 1 461 ? -2.609  5.193   -3.963  1.00 22.44 ? 441 ALA A O     1 
ATOM   3469 C  CB    . ALA A 1 461 ? -0.499  4.293   -1.677  1.00 17.91 ? 441 ALA A CB    1 
ATOM   3470 N  N     . GLY A 1 462 ? -2.217  3.018   -4.196  1.00 19.84 ? 442 GLY A N     1 
ATOM   3471 C  CA    . GLY A 1 462 ? -2.669  2.983   -5.583  1.00 25.68 ? 442 GLY A CA    1 
ATOM   3472 C  C     . GLY A 1 462 ? -4.140  3.408   -5.728  1.00 31.34 ? 442 GLY A C     1 
ATOM   3473 O  O     . GLY A 1 462 ? -4.583  3.756   -6.825  1.00 32.66 ? 442 GLY A O     1 
ATOM   3474 N  N     . GLN A 1 463 ? -4.894  3.399   -4.620  1.00 29.10 ? 443 GLN A N     1 
ATOM   3475 C  CA    . GLN A 1 463 ? -6.275  3.865   -4.596  1.00 30.02 ? 443 GLN A CA    1 
ATOM   3476 C  C     . GLN A 1 463 ? -6.289  5.394   -4.404  1.00 33.58 ? 443 GLN A C     1 
ATOM   3477 O  O     . GLN A 1 463 ? -7.332  5.996   -4.750  1.00 43.52 ? 443 GLN A O     1 
ATOM   3478 C  CB    . GLN A 1 463 ? -7.093  3.210   -3.467  1.00 27.19 ? 443 GLN A CB    1 
ATOM   3479 C  CG    . GLN A 1 463 ? -6.932  1.695   -3.303  1.00 24.79 ? 443 GLN A CG    1 
ATOM   3480 C  CD    . GLN A 1 463 ? -7.566  0.902   -4.408  1.00 28.34 ? 443 GLN A CD    1 
ATOM   3481 O  OE1   . GLN A 1 463 ? -8.598  1.303   -4.938  1.00 28.20 ? 443 GLN A OE1   1 
ATOM   3482 N  NE2   . GLN A 1 463 ? -6.963  -0.220  -4.765  1.00 26.74 ? 443 GLN A NE2   1 
HETATM 3483 C  C2    . BGC B 2 .   ? -11.182 -19.222 13.932  1.00 12.81 ? 1   BGC C C2    1 
HETATM 3484 C  C3    . BGC B 2 .   ? -12.609 -18.747 13.512  1.00 13.46 ? 1   BGC C C3    1 
HETATM 3485 C  C4    . BGC B 2 .   ? -13.316 -19.833 12.677  1.00 14.71 ? 1   BGC C C4    1 
HETATM 3486 C  C5    . BGC B 2 .   ? -13.238 -21.191 13.432  1.00 14.57 ? 1   BGC C C5    1 
HETATM 3487 C  C6    . BGC B 2 .   ? -13.864 -22.384 12.693  1.00 18.43 ? 1   BGC C C6    1 
HETATM 3488 C  C1    . BGC B 2 .   ? -11.202 -20.638 14.514  1.00 15.13 ? 1   BGC C C1    1 
HETATM 3489 O  O1    . BGC B 2 .   ? -9.910  -21.064 14.699  1.00 15.30 ? 1   BGC C O1    1 
HETATM 3490 O  O2    . BGC B 2 .   ? -10.746 -18.341 15.098  1.00 12.61 ? 1   BGC C O2    1 
HETATM 3491 O  O3    . BGC B 2 .   ? -12.505 -17.530 12.741  1.00 14.03 ? 1   BGC C O3    1 
HETATM 3492 O  O4    . BGC B 2 .   ? -14.666 -19.440 12.387  1.00 14.38 ? 1   BGC C O4    1 
HETATM 3493 O  O5    . BGC B 2 .   ? -11.836 -21.494 13.567  1.00 14.01 ? 1   BGC C O5    1 
HETATM 3494 O  O6    . BGC B 2 .   ? -13.500 -22.365 11.294  1.00 19.06 ? 1   BGC C O6    1 
HETATM 3495 C  C2    . BGC B 2 .   ? -10.636 -16.056 15.397  1.00 12.06 ? 2   BGC C C2    1 
HETATM 3496 C  C3    . BGC B 2 .   ? -9.726  -14.814 15.453  1.00 11.57 ? 2   BGC C C3    1 
HETATM 3497 C  C4    . BGC B 2 .   ? -8.334  -15.186 16.004  1.00 11.49 ? 2   BGC C C4    1 
HETATM 3498 C  C5    . BGC B 2 .   ? -7.753  -16.341 15.197  1.00 12.84 ? 2   BGC C C5    1 
HETATM 3499 C  C6    . BGC B 2 .   ? -6.366  -16.746 15.616  1.00 12.59 ? 2   BGC C C6    1 
HETATM 3500 C  C1    . BGC B 2 .   ? -9.912  -17.261 14.804  1.00 13.47 ? 2   BGC C C1    1 
HETATM 3501 O  O2    . BGC B 2 .   ? -11.771 -15.746 14.577  1.00 13.61 ? 2   BGC C O2    1 
HETATM 3502 O  O3    . BGC B 2 .   ? -10.327 -13.780 16.262  1.00 10.60 ? 2   BGC C O3    1 
HETATM 3503 O  O4    . BGC B 2 .   ? -7.469  -14.034 15.887  1.00 11.38 ? 2   BGC C O4    1 
HETATM 3504 O  O5    . BGC B 2 .   ? -8.610  -17.475 15.376  1.00 11.94 ? 2   BGC C O5    1 
HETATM 3505 O  O6    . BGC B 2 .   ? -6.170  -16.691 17.069  1.00 13.43 ? 2   BGC C O6    1 
HETATM 3506 C  C2    . BGC C 2 .   ? -33.761 -6.651  9.602   1.00 19.79 ? 1   BGC B C2    1 
HETATM 3507 C  C3    . BGC C 2 .   ? -33.842 -7.113  11.052  1.00 21.20 ? 1   BGC B C3    1 
HETATM 3508 C  C4    . BGC C 2 .   ? -35.286 -7.396  11.493  1.00 22.01 ? 1   BGC B C4    1 
HETATM 3509 C  C5    . BGC C 2 .   ? -35.991 -8.247  10.472  1.00 23.06 ? 1   BGC B C5    1 
HETATM 3510 C  C6    . BGC C 2 .   ? -37.461 -8.371  10.767  1.00 25.21 ? 1   BGC B C6    1 
HETATM 3511 C  C1    . BGC C 2 .   ? -34.580 -7.516  8.657   1.00 21.72 ? 1   BGC B C1    1 
HETATM 3512 O  O1    . BGC C 2 .   ? -34.733 -6.930  7.417   1.00 23.05 ? 1   BGC B O1    1 
HETATM 3513 O  O2    . BGC C 2 .   ? -32.395 -6.623  9.175   1.00 18.02 ? 1   BGC B O2    1 
HETATM 3514 O  O3    . BGC C 2 .   ? -33.226 -6.106  11.889  1.00 19.74 ? 1   BGC B O3    1 
HETATM 3515 O  O4    . BGC C 2 .   ? -35.383 -8.132  12.741  1.00 24.75 ? 1   BGC B O4    1 
HETATM 3516 O  O5    . BGC C 2 .   ? -35.902 -7.636  9.160   1.00 22.13 ? 1   BGC B O5    1 
HETATM 3517 O  O6    . BGC C 2 .   ? -38.027 -9.278  9.852   1.00 27.85 ? 1   BGC B O6    1 
HETATM 3518 C  C2    . BGC C 2 .   ? -30.339 -5.422  9.014   1.00 17.81 ? 2   BGC B C2    1 
HETATM 3519 C  C3    . BGC C 2 .   ? -29.608 -4.238  8.473   1.00 18.59 ? 2   BGC B C3    1 
HETATM 3520 C  C4    . BGC C 2 .   ? -30.037 -3.977  7.033   1.00 19.18 ? 2   BGC B C4    1 
HETATM 3521 C  C5    . BGC C 2 .   ? -31.566 -3.862  6.887   1.00 19.70 ? 2   BGC B C5    1 
HETATM 3522 C  C6    . BGC C 2 .   ? -32.008 -3.746  5.448   1.00 21.53 ? 2   BGC B C6    1 
HETATM 3523 C  C1    . BGC C 2 .   ? -31.868 -5.272  8.819   1.00 17.42 ? 2   BGC B C1    1 
HETATM 3524 O  O2    . BGC C 2 .   ? -30.073 -5.650  10.396  1.00 17.29 ? 2   BGC B O2    1 
HETATM 3525 O  O3    . BGC C 2 .   ? -28.180 -4.437  8.506   1.00 17.37 ? 2   BGC B O3    1 
HETATM 3526 O  O4    . BGC C 2 .   ? -29.442 -2.777  6.581   1.00 16.53 ? 2   BGC B O4    1 
HETATM 3527 O  O5    . BGC C 2 .   ? -32.239 -5.055  7.433   1.00 18.94 ? 2   BGC B O5    1 
HETATM 3528 O  O6    . BGC C 2 .   ? -33.427 -3.584  5.377   1.00 22.85 ? 2   BGC B O6    1 
HETATM 3529 C  "C3'" . NHE D 3 .   ? -24.137 -27.198 1.227   1.00 17.11 ? 501 NHE A "C3'" 1 
HETATM 3530 C  "C2'" . NHE D 3 .   ? -23.031 -26.137 1.183   1.00 17.19 ? 501 NHE A "C2'" 1 
HETATM 3531 C  "C1'" . NHE D 3 .   ? -23.375 -24.944 2.068   1.00 17.53 ? 501 NHE A "C1'" 1 
HETATM 3532 C  "C6'" . NHE D 3 .   ? -23.706 -25.357 3.507   1.00 19.69 ? 501 NHE A "C6'" 1 
HETATM 3533 N  N     . NHE D 3 .   ? -22.320 -23.908 2.157   1.00 16.97 ? 501 NHE A N     1 
HETATM 3534 C  C1    . NHE D 3 .   ? -21.734 -23.432 0.866   1.00 16.45 ? 501 NHE A C1    1 
HETATM 3535 C  C2    . NHE D 3 .   ? -20.712 -22.302 1.035   1.00 15.98 ? 501 NHE A C2    1 
HETATM 3536 S  S     . NHE D 3 .   ? -21.529 -20.749 1.390   1.00 15.00 ? 501 NHE A S     1 
HETATM 3537 O  O1    . NHE D 3 .   ? -20.358 -19.811 1.577   1.00 15.52 ? 501 NHE A O1    1 
HETATM 3538 O  O2    . NHE D 3 .   ? -22.390 -20.469 0.254   1.00 16.88 ? 501 NHE A O2    1 
HETATM 3539 O  O3    . NHE D 3 .   ? -22.279 -20.962 2.609   1.00 17.14 ? 501 NHE A O3    1 
HETATM 3540 C  "C5'" . NHE D 3 .   ? -24.745 -26.477 3.584   1.00 22.23 ? 501 NHE A "C5'" 1 
HETATM 3541 C  "C4'" . NHE D 3 .   ? -24.404 -27.639 2.656   1.00 17.77 ? 501 NHE A "C4'" 1 
HETATM 3542 NA NA    . NA  E 4 .   ? 2.484   -24.267 4.190   0.00 21.29 ? 502 NA  A NA    1 
HETATM 3543 C  C1    . MLA F 5 .   ? -35.102 -7.159  4.321   1.00 28.52 ? 503 MLA A C1    1 
HETATM 3544 O  O1A   . MLA F 5 .   ? -35.278 -8.090  5.143   1.00 25.03 ? 503 MLA A O1A   1 
HETATM 3545 O  O1B   . MLA F 5 .   ? -35.072 -5.945  4.631   1.00 23.41 ? 503 MLA A O1B   1 
HETATM 3546 C  C2    . MLA F 5 .   ? -34.980 -7.520  2.845   1.00 24.21 ? 503 MLA A C2    1 
HETATM 3547 C  C3    . MLA F 5 .   ? -33.929 -6.695  2.110   1.00 29.89 ? 503 MLA A C3    1 
HETATM 3548 O  O3A   . MLA F 5 .   ? -32.846 -7.246  1.810   1.00 28.05 ? 503 MLA A O3A   1 
HETATM 3549 O  O3B   . MLA F 5 .   ? -34.184 -5.485  1.895   1.00 29.57 ? 503 MLA A O3B   1 
HETATM 3550 C  C1    . MLA G 5 .   ? -1.831  5.949   29.934  1.00 20.48 ? 504 MLA A C1    1 
HETATM 3551 O  O1A   . MLA G 5 .   ? -1.401  6.683   30.846  1.00 21.86 ? 504 MLA A O1A   1 
HETATM 3552 O  O1B   . MLA G 5 .   ? -2.994  6.042   29.466  1.00 15.26 ? 504 MLA A O1B   1 
HETATM 3553 C  C2    . MLA G 5 .   ? -0.869  4.923   29.332  1.00 21.89 ? 504 MLA A C2    1 
HETATM 3554 C  C3    . MLA G 5 .   ? 0.250   5.620   28.573  1.00 22.94 ? 504 MLA A C3    1 
HETATM 3555 O  O3A   . MLA G 5 .   ? -0.042  6.694   27.979  1.00 25.20 ? 504 MLA A O3A   1 
HETATM 3556 O  O3B   . MLA G 5 .   ? 1.419   5.143   28.661  1.00 22.14 ? 504 MLA A O3B   1 
HETATM 3557 O  O     . HOH H 6 .   ? 1.299   -1.668  28.249  1.00 18.28 ? 601 HOH A O     1 
HETATM 3558 O  O     . HOH H 6 .   ? -15.636 -22.739 -3.434  1.00 21.75 ? 602 HOH A O     1 
HETATM 3559 O  O     . HOH H 6 .   ? 8.809   -16.271 2.535   1.00 14.43 ? 603 HOH A O     1 
HETATM 3560 O  O     . HOH H 6 .   ? -19.053 -32.143 29.105  1.00 24.87 ? 604 HOH A O     1 
HETATM 3561 O  O     . HOH H 6 .   ? -16.801 -38.547 2.209   1.00 31.42 ? 605 HOH A O     1 
HETATM 3562 O  O     . HOH H 6 .   ? 8.628   -0.601  20.894  1.00 28.17 ? 606 HOH A O     1 
HETATM 3563 O  O     . HOH H 6 .   ? 14.596  -5.220  19.071  1.00 23.59 ? 607 HOH A O     1 
HETATM 3564 O  O     . HOH H 6 .   ? -8.030  -21.852 -3.864  1.00 25.79 ? 608 HOH A O     1 
HETATM 3565 O  O     . HOH H 6 .   ? -3.211  -18.780 9.156   1.00 12.39 ? 609 HOH A O     1 
HETATM 3566 O  O     . HOH H 6 .   ? -28.551 2.243   9.393   1.00 27.65 ? 610 HOH A O     1 
HETATM 3567 O  O     . HOH H 6 .   ? -31.416 -21.599 9.005   1.00 14.62 ? 611 HOH A O     1 
HETATM 3568 O  O     . HOH H 6 .   ? -3.026  -11.633 32.249  1.00 9.79  ? 612 HOH A O     1 
HETATM 3569 O  O     . HOH H 6 .   ? -15.817 5.607   13.980  1.00 10.36 ? 613 HOH A O     1 
HETATM 3570 O  O     . HOH H 6 .   ? 3.143   -22.273 4.458   1.00 13.01 ? 614 HOH A O     1 
HETATM 3571 O  O     . HOH H 6 .   ? -2.217  8.205   9.689   1.00 24.24 ? 615 HOH A O     1 
HETATM 3572 O  O     . HOH H 6 .   ? -7.087  15.375  22.843  1.00 21.70 ? 616 HOH A O     1 
HETATM 3573 O  O     . HOH H 6 .   ? 6.289   0.693   28.424  1.00 24.80 ? 617 HOH A O     1 
HETATM 3574 O  O     . HOH H 6 .   ? 6.194   -18.222 22.846  1.00 26.64 ? 618 HOH A O     1 
HETATM 3575 O  O     . HOH H 6 .   ? -21.156 2.233   7.597   1.00 20.72 ? 619 HOH A O     1 
HETATM 3576 O  O     . HOH H 6 .   ? -18.568 -39.712 5.167   1.00 24.09 ? 620 HOH A O     1 
HETATM 3577 O  O     . HOH H 6 .   ? -24.082 5.445   32.175  1.00 26.34 ? 621 HOH A O     1 
HETATM 3578 O  O     . HOH H 6 .   ? -27.917 -19.231 3.302   1.00 24.24 ? 622 HOH A O     1 
HETATM 3579 O  O     . HOH H 6 .   ? -29.234 -7.295  16.121  1.00 13.07 ? 623 HOH A O     1 
HETATM 3580 O  O     . HOH H 6 .   ? -2.984  -0.099  19.746  1.00 8.15  ? 624 HOH A O     1 
HETATM 3581 O  O     . HOH H 6 .   ? 10.428  -3.442  7.982   1.00 24.05 ? 625 HOH A O     1 
HETATM 3582 O  O     . HOH H 6 .   ? -27.545 5.898   13.162  1.00 23.40 ? 626 HOH A O     1 
HETATM 3583 O  O     . HOH H 6 .   ? -8.706  -15.098 38.843  1.00 17.62 ? 627 HOH A O     1 
HETATM 3584 O  O     . HOH H 6 .   ? -10.659 -25.707 29.793  1.00 23.57 ? 628 HOH A O     1 
HETATM 3585 O  O     . HOH H 6 .   ? -2.181  8.097   27.347  1.00 16.72 ? 629 HOH A O     1 
HETATM 3586 O  O     . HOH H 6 .   ? -23.581 -38.297 12.233  1.00 21.14 ? 630 HOH A O     1 
HETATM 3587 O  O     . HOH H 6 .   ? -1.235  3.406   1.770   1.00 22.30 ? 631 HOH A O     1 
HETATM 3588 O  O     . HOH H 6 .   ? 9.964   -19.555 8.185   1.00 23.27 ? 632 HOH A O     1 
HETATM 3589 O  O     . HOH H 6 .   ? 1.791   -6.054  33.177  1.00 18.82 ? 633 HOH A O     1 
HETATM 3590 O  O     . HOH H 6 .   ? -17.649 -32.596 15.532  1.00 30.21 ? 634 HOH A O     1 
HETATM 3591 O  O     . HOH H 6 .   ? -19.594 -15.577 16.006  1.00 8.76  ? 635 HOH A O     1 
HETATM 3592 O  O     . HOH H 6 .   ? -2.852  -7.901  27.524  1.00 4.72  ? 636 HOH A O     1 
HETATM 3593 O  O     . HOH H 6 .   ? -9.384  3.443   -6.296  1.00 31.71 ? 637 HOH A O     1 
HETATM 3594 O  O     . HOH H 6 .   ? -2.073  -11.676 8.622   1.00 7.46  ? 638 HOH A O     1 
HETATM 3595 O  O     . HOH H 6 .   ? 0.209   -19.422 30.282  1.00 13.15 ? 639 HOH A O     1 
HETATM 3596 O  O     . HOH H 6 .   ? 6.299   3.990   23.320  1.00 21.29 ? 640 HOH A O     1 
HETATM 3597 O  O     . HOH H 6 .   ? -6.439  -19.477 6.010   1.00 16.09 ? 641 HOH A O     1 
HETATM 3598 O  O     . HOH H 6 .   ? -5.839  7.306   32.627  1.00 16.81 ? 642 HOH A O     1 
HETATM 3599 O  O     . HOH H 6 .   ? -8.242  12.987  25.277  1.00 25.28 ? 643 HOH A O     1 
HETATM 3600 O  O     . HOH H 6 .   ? -19.306 -40.150 -0.359  1.00 22.12 ? 644 HOH A O     1 
HETATM 3601 O  O     . HOH H 6 .   ? -32.195 -6.728  -0.731  1.00 24.27 ? 645 HOH A O     1 
HETATM 3602 O  O     . HOH H 6 .   ? -24.433 -23.280 17.686  1.00 12.21 ? 646 HOH A O     1 
HETATM 3603 O  O     . HOH H 6 .   ? 5.626   3.713   4.948   1.00 15.91 ? 647 HOH A O     1 
HETATM 3604 O  O     . HOH H 6 .   ? -3.585  -19.580 38.453  1.00 17.80 ? 648 HOH A O     1 
HETATM 3605 O  O     . HOH H 6 .   ? 7.031   -15.394 6.691   1.00 15.64 ? 649 HOH A O     1 
HETATM 3606 O  O     . HOH H 6 .   ? -22.710 -1.683  35.557  1.00 17.81 ? 650 HOH A O     1 
HETATM 3607 O  O     . HOH H 6 .   ? 3.808   -18.185 13.865  1.00 15.93 ? 651 HOH A O     1 
HETATM 3608 O  O     . HOH H 6 .   ? -11.279 15.045  23.548  1.00 25.01 ? 652 HOH A O     1 
HETATM 3609 O  O     . HOH H 6 .   ? -17.670 3.617   6.079   1.00 21.65 ? 653 HOH A O     1 
HETATM 3610 O  O     . HOH H 6 .   ? -19.940 -20.011 33.930  1.00 17.03 ? 654 HOH A O     1 
HETATM 3611 O  O     . HOH H 6 .   ? -8.437  -7.100  28.537  1.00 10.07 ? 655 HOH A O     1 
HETATM 3612 O  O     . HOH H 6 .   ? -19.883 -40.259 2.317   1.00 25.65 ? 656 HOH A O     1 
HETATM 3613 O  O     . HOH H 6 .   ? -12.366 -7.009  35.308  1.00 14.56 ? 657 HOH A O     1 
HETATM 3614 O  O     . HOH H 6 .   ? -32.038 -18.215 7.569   1.00 21.73 ? 658 HOH A O     1 
HETATM 3615 O  O     . HOH H 6 .   ? -15.134 8.272   14.264  1.00 15.29 ? 659 HOH A O     1 
HETATM 3616 O  O     . HOH H 6 .   ? -39.547 -29.311 16.370  1.00 25.26 ? 660 HOH A O     1 
HETATM 3617 O  O     . HOH H 6 .   ? -21.548 -22.497 4.759   1.00 11.96 ? 661 HOH A O     1 
HETATM 3618 O  O     . HOH H 6 .   ? -23.434 -11.622 36.075  1.00 23.73 ? 662 HOH A O     1 
HETATM 3619 O  O     . HOH H 6 .   ? 2.935   -11.165 28.045  1.00 7.05  ? 663 HOH A O     1 
HETATM 3620 O  O     . HOH H 6 .   ? -17.241 2.634   0.581   1.00 23.92 ? 664 HOH A O     1 
HETATM 3621 O  O     . HOH H 6 .   ? -5.412  -21.980 14.373  1.00 22.07 ? 665 HOH A O     1 
HETATM 3622 O  O     . HOH H 6 .   ? -24.906 -13.247 37.323  1.00 22.55 ? 666 HOH A O     1 
HETATM 3623 O  O     . HOH H 6 .   ? -10.086 -0.542  40.034  1.00 18.02 ? 667 HOH A O     1 
HETATM 3624 O  O     . HOH H 6 .   ? -25.296 -10.522 -7.933  1.00 18.64 ? 668 HOH A O     1 
HETATM 3625 O  O     . HOH H 6 .   ? -8.978  -21.300 34.957  1.00 18.09 ? 669 HOH A O     1 
HETATM 3626 O  O     . HOH H 6 .   ? -5.664  8.503   6.922   1.00 29.68 ? 670 HOH A O     1 
HETATM 3627 O  O     . HOH H 6 .   ? -10.224 4.969   0.999   1.00 19.89 ? 671 HOH A O     1 
HETATM 3628 O  O     . HOH H 6 .   ? -22.308 -18.512 -1.699  1.00 17.53 ? 672 HOH A O     1 
HETATM 3629 O  O     . HOH H 6 .   ? 3.618   -14.120 31.101  1.00 26.63 ? 673 HOH A O     1 
HETATM 3630 O  O     . HOH H 6 .   ? -26.312 -9.892  4.821   1.00 17.49 ? 674 HOH A O     1 
HETATM 3631 O  O     . HOH H 6 .   ? -14.569 -5.941  26.944  1.00 7.33  ? 675 HOH A O     1 
HETATM 3632 O  O     . HOH H 6 .   ? -27.851 -31.773 8.647   1.00 23.02 ? 676 HOH A O     1 
HETATM 3633 O  O     . HOH H 6 .   ? -30.598 -7.218  12.491  1.00 18.53 ? 677 HOH A O     1 
HETATM 3634 O  O     . HOH H 6 .   ? -4.734  0.676   24.838  1.00 11.74 ? 678 HOH A O     1 
HETATM 3635 O  O     . HOH H 6 .   ? -13.367 12.103  27.039  1.00 30.21 ? 679 HOH A O     1 
HETATM 3636 O  O     . HOH H 6 .   ? -24.596 -36.963 8.720   1.00 17.26 ? 680 HOH A O     1 
HETATM 3637 O  O     . HOH H 6 .   ? -21.204 -2.830  33.555  1.00 11.90 ? 681 HOH A O     1 
HETATM 3638 O  O     . HOH H 6 .   ? -6.746  -24.044 25.970  1.00 9.26  ? 682 HOH A O     1 
HETATM 3639 O  O     . HOH H 6 .   ? -34.753 -13.598 15.619  1.00 23.19 ? 683 HOH A O     1 
HETATM 3640 O  O     . HOH H 6 .   ? -27.603 -10.435 -6.176  1.00 22.09 ? 684 HOH A O     1 
HETATM 3641 O  O     . HOH H 6 .   ? 8.194   -11.187 0.810   1.00 18.83 ? 685 HOH A O     1 
HETATM 3642 O  O     . HOH H 6 .   ? -16.427 5.411   7.590   1.00 25.96 ? 686 HOH A O     1 
HETATM 3643 O  O     . HOH H 6 .   ? 11.890  -13.529 6.493   1.00 15.29 ? 687 HOH A O     1 
HETATM 3644 O  O     . HOH H 6 .   ? -24.974 -21.283 0.731   1.00 18.89 ? 688 HOH A O     1 
HETATM 3645 O  O     . HOH H 6 .   ? -16.227 -1.871  39.058  1.00 10.16 ? 689 HOH A O     1 
HETATM 3646 O  O     . HOH H 6 .   ? 4.366   6.782   10.736  1.00 19.16 ? 690 HOH A O     1 
HETATM 3647 O  O     . HOH H 6 .   ? -10.592 14.443  18.951  1.00 22.53 ? 691 HOH A O     1 
HETATM 3648 O  O     . HOH H 6 .   ? 6.425   -5.550  0.046   1.00 17.72 ? 692 HOH A O     1 
HETATM 3649 O  O     . HOH H 6 .   ? -5.913  -2.602  39.210  1.00 20.88 ? 693 HOH A O     1 
HETATM 3650 O  O     . HOH H 6 .   ? -7.033  -1.876  22.768  1.00 6.58  ? 694 HOH A O     1 
HETATM 3651 O  O     . HOH H 6 .   ? -5.651  -17.695 7.957   1.00 12.92 ? 695 HOH A O     1 
HETATM 3652 O  O     . HOH H 6 .   ? -15.150 -3.078  15.793  1.00 11.74 ? 696 HOH A O     1 
HETATM 3653 O  O     . HOH H 6 .   ? -16.679 3.007   3.315   1.00 18.41 ? 697 HOH A O     1 
HETATM 3654 O  O     . HOH H 6 .   ? -1.600  11.047  16.540  1.00 11.39 ? 698 HOH A O     1 
HETATM 3655 O  O     . HOH H 6 .   ? -15.506 -14.466 25.842  1.00 6.55  ? 699 HOH A O     1 
HETATM 3656 O  O     . HOH H 6 .   ? -12.511 -6.015  24.564  1.00 7.72  ? 700 HOH A O     1 
HETATM 3657 O  O     . HOH H 6 .   ? -32.704 -13.451 1.124   1.00 15.70 ? 701 HOH A O     1 
HETATM 3658 O  O     . HOH H 6 .   ? -20.981 -3.537  -4.663  1.00 17.97 ? 702 HOH A O     1 
HETATM 3659 O  O     . HOH H 6 .   ? -31.136 -1.776  26.810  1.00 18.56 ? 703 HOH A O     1 
HETATM 3660 O  O     . HOH H 6 .   ? -9.655  -23.141 4.417   1.00 22.67 ? 704 HOH A O     1 
HETATM 3661 O  O     . HOH H 6 .   ? 5.815   -9.656  25.584  1.00 14.23 ? 705 HOH A O     1 
HETATM 3662 O  O     . HOH H 6 .   ? -4.234  -0.002  39.457  1.00 23.78 ? 706 HOH A O     1 
HETATM 3663 O  O     . HOH H 6 .   ? -9.931  2.865   -1.652  1.00 16.02 ? 707 HOH A O     1 
HETATM 3664 O  O     . HOH H 6 .   ? -6.678  -5.017  28.678  1.00 5.46  ? 708 HOH A O     1 
HETATM 3665 O  O     . HOH H 6 .   ? -28.885 3.966   27.677  1.00 17.38 ? 709 HOH A O     1 
HETATM 3666 O  O     . HOH H 6 .   ? -1.296  -21.683 30.573  1.00 12.79 ? 710 HOH A O     1 
HETATM 3667 O  O     . HOH H 6 .   ? -5.846  -21.783 -2.015  1.00 20.55 ? 711 HOH A O     1 
HETATM 3668 O  O     . HOH H 6 .   ? 11.015  -17.245 6.260   1.00 25.18 ? 712 HOH A O     1 
HETATM 3669 O  O     . HOH H 6 .   ? -23.474 -21.075 30.531  1.00 19.75 ? 713 HOH A O     1 
HETATM 3670 O  O     . HOH H 6 .   ? -4.319  -6.106  29.124  1.00 5.52  ? 714 HOH A O     1 
HETATM 3671 O  O     . HOH H 6 .   ? -9.066  -12.256 18.197  1.00 8.99  ? 715 HOH A O     1 
HETATM 3672 O  O     . HOH H 6 .   ? -21.722 -21.758 32.713  1.00 25.42 ? 716 HOH A O     1 
HETATM 3673 O  O     . HOH H 6 .   ? -2.863  5.389   1.807   1.00 24.53 ? 717 HOH A O     1 
HETATM 3674 O  O     . HOH H 6 .   ? -31.557 -9.674  1.299   1.00 15.93 ? 718 HOH A O     1 
HETATM 3675 O  O     . HOH H 6 .   ? -16.722 -30.612 25.325  1.00 28.62 ? 719 HOH A O     1 
HETATM 3676 O  O     . HOH H 6 .   ? 5.887   3.062   15.209  1.00 16.28 ? 720 HOH A O     1 
HETATM 3677 O  O     . HOH H 6 .   ? -15.856 -20.345 35.795  1.00 21.30 ? 721 HOH A O     1 
HETATM 3678 O  O     . HOH H 6 .   ? -18.214 -12.434 21.967  1.00 6.29  ? 722 HOH A O     1 
HETATM 3679 O  O     . HOH H 6 .   ? 2.376   -13.721 17.913  1.00 11.00 ? 723 HOH A O     1 
HETATM 3680 O  O     . HOH H 6 .   ? -16.212 -16.888 26.912  1.00 6.73  ? 724 HOH A O     1 
HETATM 3681 O  O     . HOH H 6 .   ? -32.639 -16.468 2.462   1.00 24.78 ? 725 HOH A O     1 
HETATM 3682 O  O     . HOH H 6 .   ? -28.926 -19.741 5.942   1.00 23.40 ? 726 HOH A O     1 
HETATM 3683 O  O     . HOH H 6 .   ? -27.631 -17.654 -2.793  1.00 19.29 ? 727 HOH A O     1 
HETATM 3684 O  O     . HOH H 6 .   ? -20.911 -16.770 13.900  1.00 8.66  ? 728 HOH A O     1 
HETATM 3685 O  O     . HOH H 6 .   ? 2.006   5.637   23.172  1.00 19.57 ? 729 HOH A O     1 
HETATM 3686 O  O     . HOH H 6 .   ? -8.758  -18.583 3.177   1.00 13.85 ? 730 HOH A O     1 
HETATM 3687 O  O     . HOH H 6 .   ? -11.610 -5.835  18.309  1.00 7.36  ? 731 HOH A O     1 
HETATM 3688 O  O     . HOH H 6 .   ? -34.122 -19.648 11.495  1.00 19.65 ? 732 HOH A O     1 
HETATM 3689 O  O     . HOH H 6 .   ? -8.274  -14.993 -5.478  1.00 24.62 ? 733 HOH A O     1 
HETATM 3690 O  O     . HOH H 6 .   ? 9.085   -0.468  17.415  1.00 22.45 ? 734 HOH A O     1 
HETATM 3691 O  O     . HOH H 6 .   ? 3.967   -13.294 -2.660  1.00 25.18 ? 735 HOH A O     1 
HETATM 3692 O  O     . HOH H 6 .   ? 0.188   -4.753  35.340  1.00 17.15 ? 736 HOH A O     1 
HETATM 3693 O  O     . HOH H 6 .   ? -11.756 -7.441  38.893  1.00 18.70 ? 737 HOH A O     1 
HETATM 3694 O  O     . HOH H 6 .   ? -7.855  14.631  17.897  1.00 17.81 ? 738 HOH A O     1 
HETATM 3695 O  O     . HOH H 6 .   ? -23.739 -6.653  -10.232 1.00 14.43 ? 739 HOH A O     1 
HETATM 3696 O  O     . HOH H 6 .   ? 2.759   -4.214  29.929  1.00 13.22 ? 740 HOH A O     1 
HETATM 3697 O  O     . HOH H 6 .   ? -6.925  -20.129 20.497  1.00 9.22  ? 741 HOH A O     1 
HETATM 3698 O  O     . HOH H 6 .   ? -31.620 -10.926 -1.348  1.00 14.57 ? 742 HOH A O     1 
HETATM 3699 O  O     . HOH H 6 .   ? -10.284 8.223   8.145   1.00 24.20 ? 743 HOH A O     1 
HETATM 3700 O  O     . HOH H 6 .   ? -13.064 -16.175 25.615  1.00 7.45  ? 744 HOH A O     1 
HETATM 3701 O  O     . HOH H 6 .   ? -19.713 7.531   30.945  1.00 18.32 ? 745 HOH A O     1 
HETATM 3702 O  O     . HOH H 6 .   ? -34.586 -27.174 21.161  1.00 26.29 ? 746 HOH A O     1 
HETATM 3703 O  O     . HOH H 6 .   ? -5.063  -27.462 27.947  1.00 17.19 ? 747 HOH A O     1 
HETATM 3704 O  O     . HOH H 6 .   ? -23.051 7.910   12.309  1.00 26.19 ? 748 HOH A O     1 
HETATM 3705 O  O     . HOH H 6 .   ? 9.900   -6.471  5.961   1.00 12.26 ? 749 HOH A O     1 
HETATM 3706 O  O     . HOH H 6 .   ? -24.896 -30.230 28.059  1.00 20.74 ? 750 HOH A O     1 
HETATM 3707 O  O     . HOH H 6 .   ? -29.126 -3.030  31.050  1.00 20.07 ? 751 HOH A O     1 
HETATM 3708 O  O     . HOH H 6 .   ? -12.337 -17.633 34.248  1.00 13.40 ? 752 HOH A O     1 
HETATM 3709 O  O     . HOH H 6 .   ? -12.339 -31.717 12.427  1.00 31.95 ? 753 HOH A O     1 
HETATM 3710 O  O     . HOH H 6 .   ? -5.425  -18.425 37.419  1.00 18.06 ? 754 HOH A O     1 
HETATM 3711 O  O     . HOH H 6 .   ? -11.990 5.782   7.369   1.00 19.03 ? 755 HOH A O     1 
HETATM 3712 O  O     . HOH H 6 .   ? -27.719 5.977   16.542  1.00 18.65 ? 756 HOH A O     1 
HETATM 3713 O  O     . HOH H 6 .   ? -9.718  -8.184  24.637  1.00 5.64  ? 757 HOH A O     1 
HETATM 3714 O  O     . HOH H 6 .   ? -9.688  12.253  11.664  1.00 25.90 ? 758 HOH A O     1 
HETATM 3715 O  O     . HOH H 6 .   ? -13.467 -16.871 22.994  1.00 6.63  ? 759 HOH A O     1 
HETATM 3716 O  O     . HOH H 6 .   ? -36.176 -19.561 17.864  1.00 20.62 ? 760 HOH A O     1 
HETATM 3717 O  O     . HOH H 6 .   ? -28.202 -33.961 10.634  1.00 17.68 ? 761 HOH A O     1 
HETATM 3718 O  O     . HOH H 6 .   ? -7.410  -3.755  20.732  1.00 4.09  ? 762 HOH A O     1 
HETATM 3719 O  O     . HOH H 6 .   ? -0.390  -12.915 16.265  1.00 7.18  ? 763 HOH A O     1 
HETATM 3720 O  O     . HOH H 6 .   ? 9.311   -1.228  10.268  1.00 21.13 ? 764 HOH A O     1 
HETATM 3721 O  O     . HOH H 6 .   ? -17.461 -27.418 32.527  1.00 20.76 ? 765 HOH A O     1 
HETATM 3722 O  O     . HOH H 6 .   ? 9.701   -12.311 19.853  1.00 14.61 ? 766 HOH A O     1 
HETATM 3723 O  O     . HOH H 6 .   ? -10.492 -19.541 33.415  1.00 13.46 ? 767 HOH A O     1 
HETATM 3724 O  O     . HOH H 6 .   ? -19.085 -7.869  40.714  1.00 26.48 ? 768 HOH A O     1 
HETATM 3725 O  O     . HOH H 6 .   ? 5.752   -20.016 7.269   1.00 14.43 ? 769 HOH A O     1 
HETATM 3726 O  O     . HOH H 6 .   ? 13.016  -13.743 13.869  1.00 27.50 ? 770 HOH A O     1 
HETATM 3727 O  O     . HOH H 6 .   ? 0.165   -25.912 27.582  1.00 19.60 ? 771 HOH A O     1 
HETATM 3728 O  O     . HOH H 6 .   ? -26.726 -7.110  -6.492  1.00 22.40 ? 772 HOH A O     1 
HETATM 3729 O  O     . HOH H 6 .   ? -17.922 12.133  15.148  1.00 27.63 ? 773 HOH A O     1 
HETATM 3730 O  O     . HOH H 6 .   ? -1.444  9.598   31.235  1.00 26.37 ? 774 HOH A O     1 
HETATM 3731 O  O     . HOH H 6 .   ? -29.919 -16.467 33.895  1.00 24.37 ? 775 HOH A O     1 
HETATM 3732 O  O     . HOH H 6 .   ? 0.957   -26.294 2.749   1.00 16.64 ? 776 HOH A O     1 
HETATM 3733 O  O     . HOH H 6 .   ? 13.428  -7.099  16.441  1.00 23.91 ? 777 HOH A O     1 
HETATM 3734 O  O     . HOH H 6 .   ? -1.265  1.595   38.244  1.00 22.58 ? 778 HOH A O     1 
HETATM 3735 O  O     . HOH H 6 .   ? -35.728 -22.021 11.378  1.00 22.94 ? 779 HOH A O     1 
HETATM 3736 O  O     . HOH H 6 .   ? 17.569  -14.318 5.462   1.00 21.13 ? 780 HOH A O     1 
HETATM 3737 O  O     . HOH H 6 .   ? -25.582 -13.159 -6.991  1.00 14.06 ? 781 HOH A O     1 
HETATM 3738 O  O     . HOH H 6 .   ? -6.845  12.869  29.390  1.00 21.89 ? 782 HOH A O     1 
HETATM 3739 O  O     . HOH H 6 .   ? -6.139  9.942   33.244  1.00 30.02 ? 783 HOH A O     1 
HETATM 3740 O  O     . HOH H 6 .   ? -3.626  -10.091 35.996  1.00 24.17 ? 784 HOH A O     1 
HETATM 3741 O  O     . HOH H 6 .   ? 4.096   -14.273 28.739  1.00 18.15 ? 785 HOH A O     1 
HETATM 3742 O  O     . HOH H 6 .   ? -13.582 -18.940 36.457  1.00 20.65 ? 786 HOH A O     1 
HETATM 3743 O  O     . HOH H 6 .   ? -14.777 -4.973  -8.968  1.00 15.05 ? 787 HOH A O     1 
HETATM 3744 O  O     . HOH H 6 .   ? -4.943  -8.446  18.461  1.00 11.58 ? 788 HOH A O     1 
HETATM 3745 O  O     . HOH H 6 .   ? 8.814   -4.868  1.325   1.00 20.36 ? 789 HOH A O     1 
HETATM 3746 O  O     . HOH H 6 .   ? -13.516 1.436   39.669  1.00 15.86 ? 790 HOH A O     1 
HETATM 3747 O  O     . HOH H 6 .   ? -3.204  -24.605 24.113  1.00 21.02 ? 791 HOH A O     1 
HETATM 3748 O  O     . HOH H 6 .   ? -21.724 -30.172 -5.282  1.00 30.19 ? 792 HOH A O     1 
HETATM 3749 O  O     . HOH H 6 .   ? -1.277  -19.987 0.044   1.00 18.86 ? 793 HOH A O     1 
HETATM 3750 O  O     . HOH H 6 .   ? -1.658  -26.064 25.713  1.00 26.59 ? 794 HOH A O     1 
HETATM 3751 O  O     . HOH H 6 .   ? -29.607 -7.788  -0.718  1.00 17.94 ? 795 HOH A O     1 
HETATM 3752 O  O     . HOH H 6 .   ? -16.485 -0.917  15.136  1.00 24.73 ? 796 HOH A O     1 
HETATM 3753 O  O     . HOH H 6 .   ? -3.446  -16.895 -1.361  1.00 24.15 ? 797 HOH A O     1 
HETATM 3754 O  O     . HOH H 6 .   ? -24.717 -16.415 -4.394  1.00 25.32 ? 798 HOH A O     1 
HETATM 3755 O  O     . HOH H 6 .   ? 3.508   -21.837 7.126   1.00 21.05 ? 799 HOH A O     1 
HETATM 3756 O  O     . HOH H 6 .   ? -6.618  -24.013 13.310  1.00 26.19 ? 800 HOH A O     1 
HETATM 3757 O  O     . HOH H 6 .   ? -6.231  -28.345 30.257  1.00 22.56 ? 801 HOH A O     1 
HETATM 3758 O  O     . HOH H 6 .   ? 9.571   -15.187 7.213   1.00 16.91 ? 802 HOH A O     1 
HETATM 3759 O  O     . HOH H 6 .   ? -36.878 -11.881 15.998  1.00 29.38 ? 803 HOH A O     1 
HETATM 3760 O  O     . HOH H 6 .   ? 2.019   -20.415 32.296  1.00 25.59 ? 804 HOH A O     1 
HETATM 3761 O  O     . HOH H 6 .   ? -32.382 -11.474 3.094   1.00 17.12 ? 805 HOH A O     1 
HETATM 3762 O  O     . HOH H 6 .   ? -29.258 -9.327  -3.133  1.00 16.52 ? 806 HOH A O     1 
HETATM 3763 O  O     . HOH H 6 .   ? -19.363 1.982   -0.785  1.00 23.49 ? 807 HOH A O     1 
HETATM 3764 O  O     . HOH H 6 .   ? -7.074  -20.869 16.205  1.00 23.17 ? 808 HOH A O     1 
HETATM 3765 O  O     . HOH H 6 .   ? -27.263 -16.515 -5.470  1.00 19.07 ? 809 HOH A O     1 
HETATM 3766 O  O     . HOH H 6 .   ? 4.022   5.117   22.175  1.00 26.50 ? 810 HOH A O     1 
HETATM 3767 O  O     . HOH H 6 .   ? 3.920   -24.283 7.716   1.00 30.69 ? 811 HOH A O     1 
HETATM 3768 O  O     . HOH H 6 .   ? -7.603  -26.203 27.300  1.00 21.30 ? 812 HOH A O     1 
HETATM 3769 O  O     . HOH H 6 .   ? -32.342 0.737   26.450  1.00 24.01 ? 813 HOH A O     1 
HETATM 3770 O  O     . HOH H 6 .   ? -9.877  -19.199 17.856  1.00 19.17 ? 814 HOH A O     1 
HETATM 3771 O  O     . HOH H 6 .   ? -11.842 -19.368 38.129  1.00 24.07 ? 815 HOH A O     1 
HETATM 3772 O  O     . HOH H 6 .   ? -4.279  -0.432  22.366  1.00 13.65 ? 816 HOH A O     1 
HETATM 3773 O  O     . HOH H 6 .   ? -14.212 -0.906  40.815  1.00 15.74 ? 817 HOH A O     1 
HETATM 3774 O  O     . HOH H 6 .   ? -7.220  -18.800 18.151  1.00 19.07 ? 818 HOH A O     1 
HETATM 3775 O  O     . HOH H 6 .   ? 0.788   5.465   2.043   1.00 24.64 ? 819 HOH A O     1 
HETATM 3776 O  O     . HOH H 6 .   ? -11.428 -11.495 40.018  1.00 20.25 ? 820 HOH A O     1 
HETATM 3777 O  O     . HOH H 6 .   ? -30.215 -0.317  6.393   1.00 29.07 ? 821 HOH A O     1 
HETATM 3778 O  O     . HOH H 6 .   ? -5.480  -15.750 38.304  1.00 22.90 ? 822 HOH A O     1 
HETATM 3779 O  O     . HOH H 6 .   ? -3.626  -24.075 15.464  1.00 25.63 ? 823 HOH A O     1 
HETATM 3780 O  O     . HOH H 6 .   ? 5.576   -11.550 27.450  1.00 19.60 ? 824 HOH A O     1 
HETATM 3781 O  O     . HOH H 6 .   ? -19.397 2.719   -3.170  1.00 37.35 ? 825 HOH A O     1 
HETATM 3782 O  O     . HOH H 6 .   ? -6.662  -22.767 19.799  1.00 21.62 ? 826 HOH A O     1 
HETATM 3783 O  O     . HOH H 6 .   ? -24.103 -9.327  37.925  1.00 27.61 ? 827 HOH A O     1 
HETATM 3784 O  O     . HOH H 6 .   ? -11.808 -2.124  41.292  1.00 22.41 ? 828 HOH A O     1 
HETATM 3785 O  O     . HOH H 6 .   ? -9.928  -13.195 40.513  1.00 30.79 ? 829 HOH A O     1 
HETATM 3786 O  O     . HOH H 6 .   ? -34.837 -3.302  8.610   1.00 22.22 ? 830 HOH A O     1 
HETATM 3787 O  O     . HOH H 6 .   ? -9.648  -22.303 17.114  1.00 32.81 ? 831 HOH A O     1 
# 
