data_8WN5
# 
_entry.id   8WN5 
# 
_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   8WN5         pdb_00008wn5 10.2210/pdb8wn5/pdb 
WWPDB D_1300041470 ?            ?                   
# 
_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                        8WN5 
_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 non-polymer nat 'MALONIC ACID'                              104.061   1   ?        ?     ? ? 
3 non-polymer syn beta-D-glucopyranose                        180.156   1   ?        ?     ? ? 
4 non-polymer syn '2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID' 207.290   1   ?        ?     ? ? 
5 water       nat water                                       18.015    295 ?        ?     ? ? 
# 
_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 
2 'MALONIC ACID'                              MLA 
3 beta-D-glucopyranose                        BGC 
4 '2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID' NHE 
5 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                   ? 
# 
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 
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   1   MET MET A . n 
A 1 22  ALA 22  2   2   ALA ALA 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 
# 
_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 
B 2 MLA 1   501 1   MLA MLA A . 
C 3 BGC 1   502 60  BGC BGC A . 
D 4 NHE 1   503 64  NHE NHE A . 
E 5 HOH 1   601 230 HOH HOH A . 
E 5 HOH 2   602 273 HOH HOH A . 
E 5 HOH 3   603 125 HOH HOH A . 
E 5 HOH 4   604 315 HOH HOH A . 
E 5 HOH 5   605 300 HOH HOH A . 
E 5 HOH 6   606 110 HOH HOH A . 
E 5 HOH 7   607 176 HOH HOH A . 
E 5 HOH 8   608 205 HOH HOH A . 
E 5 HOH 9   609 307 HOH HOH A . 
E 5 HOH 10  610 298 HOH HOH A . 
E 5 HOH 11  611 280 HOH HOH A . 
E 5 HOH 12  612 241 HOH HOH A . 
E 5 HOH 13  613 146 HOH HOH A . 
E 5 HOH 14  614 310 HOH HOH A . 
E 5 HOH 15  615 122 HOH HOH A . 
E 5 HOH 16  616 85  HOH HOH A . 
E 5 HOH 17  617 329 HOH HOH A . 
E 5 HOH 18  618 170 HOH HOH A . 
E 5 HOH 19  619 191 HOH HOH A . 
E 5 HOH 20  620 63  HOH HOH A . 
E 5 HOH 21  621 290 HOH HOH A . 
E 5 HOH 22  622 96  HOH HOH A . 
E 5 HOH 23  623 47  HOH HOH A . 
E 5 HOH 24  624 328 HOH HOH A . 
E 5 HOH 25  625 56  HOH HOH A . 
E 5 HOH 26  626 196 HOH HOH A . 
E 5 HOH 27  627 210 HOH HOH A . 
E 5 HOH 28  628 128 HOH HOH A . 
E 5 HOH 29  629 270 HOH HOH A . 
E 5 HOH 30  630 209 HOH HOH A . 
E 5 HOH 31  631 260 HOH HOH A . 
E 5 HOH 32  632 344 HOH HOH A . 
E 5 HOH 33  633 23  HOH HOH A . 
E 5 HOH 34  634 348 HOH HOH A . 
E 5 HOH 35  635 202 HOH HOH A . 
E 5 HOH 36  636 118 HOH HOH A . 
E 5 HOH 37  637 274 HOH HOH A . 
E 5 HOH 38  638 256 HOH HOH A . 
E 5 HOH 39  639 91  HOH HOH A . 
E 5 HOH 40  640 117 HOH HOH A . 
E 5 HOH 41  641 265 HOH HOH A . 
E 5 HOH 42  642 168 HOH HOH A . 
E 5 HOH 43  643 136 HOH HOH A . 
E 5 HOH 44  644 90  HOH HOH A . 
E 5 HOH 45  645 141 HOH HOH A . 
E 5 HOH 46  646 25  HOH HOH A . 
E 5 HOH 47  647 199 HOH HOH A . 
E 5 HOH 48  648 71  HOH HOH A . 
E 5 HOH 49  649 281 HOH HOH A . 
E 5 HOH 50  650 97  HOH HOH A . 
E 5 HOH 51  651 157 HOH HOH A . 
E 5 HOH 52  652 160 HOH HOH A . 
E 5 HOH 53  653 252 HOH HOH A . 
E 5 HOH 54  654 13  HOH HOH A . 
E 5 HOH 55  655 320 HOH HOH A . 
E 5 HOH 56  656 59  HOH HOH A . 
E 5 HOH 57  657 203 HOH HOH A . 
E 5 HOH 58  658 173 HOH HOH A . 
E 5 HOH 59  659 195 HOH HOH A . 
E 5 HOH 60  660 7   HOH HOH A . 
E 5 HOH 61  661 231 HOH HOH A . 
E 5 HOH 62  662 74  HOH HOH A . 
E 5 HOH 63  663 30  HOH HOH A . 
E 5 HOH 64  664 26  HOH HOH A . 
E 5 HOH 65  665 237 HOH HOH A . 
E 5 HOH 66  666 67  HOH HOH A . 
E 5 HOH 67  667 164 HOH HOH A . 
E 5 HOH 68  668 134 HOH HOH A . 
E 5 HOH 69  669 80  HOH HOH A . 
E 5 HOH 70  670 216 HOH HOH A . 
E 5 HOH 71  671 88  HOH HOH A . 
E 5 HOH 72  672 5   HOH HOH A . 
E 5 HOH 73  673 187 HOH HOH A . 
E 5 HOH 74  674 254 HOH HOH A . 
E 5 HOH 75  675 218 HOH HOH A . 
E 5 HOH 76  676 220 HOH HOH A . 
E 5 HOH 77  677 264 HOH HOH A . 
E 5 HOH 78  678 82  HOH HOH A . 
E 5 HOH 79  679 20  HOH HOH A . 
E 5 HOH 80  680 243 HOH HOH A . 
E 5 HOH 81  681 22  HOH HOH A . 
E 5 HOH 82  682 44  HOH HOH A . 
E 5 HOH 83  683 68  HOH HOH A . 
E 5 HOH 84  684 207 HOH HOH A . 
E 5 HOH 85  685 183 HOH HOH A . 
E 5 HOH 86  686 239 HOH HOH A . 
E 5 HOH 87  687 178 HOH HOH A . 
E 5 HOH 88  688 21  HOH HOH A . 
E 5 HOH 89  689 14  HOH HOH A . 
E 5 HOH 90  690 103 HOH HOH A . 
E 5 HOH 91  691 113 HOH HOH A . 
E 5 HOH 92  692 69  HOH HOH A . 
E 5 HOH 93  693 120 HOH HOH A . 
E 5 HOH 94  694 309 HOH HOH A . 
E 5 HOH 95  695 179 HOH HOH A . 
E 5 HOH 96  696 111 HOH HOH A . 
E 5 HOH 97  697 64  HOH HOH A . 
E 5 HOH 98  698 169 HOH HOH A . 
E 5 HOH 99  699 66  HOH HOH A . 
E 5 HOH 100 700 3   HOH HOH A . 
E 5 HOH 101 701 60  HOH HOH A . 
E 5 HOH 102 702 116 HOH HOH A . 
E 5 HOH 103 703 247 HOH HOH A . 
E 5 HOH 104 704 133 HOH HOH A . 
E 5 HOH 105 705 65  HOH HOH A . 
E 5 HOH 106 706 50  HOH HOH A . 
E 5 HOH 107 707 167 HOH HOH A . 
E 5 HOH 108 708 29  HOH HOH A . 
E 5 HOH 109 709 166 HOH HOH A . 
E 5 HOH 110 710 347 HOH HOH A . 
E 5 HOH 111 711 236 HOH HOH A . 
E 5 HOH 112 712 159 HOH HOH A . 
E 5 HOH 113 713 19  HOH HOH A . 
E 5 HOH 114 714 188 HOH HOH A . 
E 5 HOH 115 715 235 HOH HOH A . 
E 5 HOH 116 716 189 HOH HOH A . 
E 5 HOH 117 717 72  HOH HOH A . 
E 5 HOH 118 718 204 HOH HOH A . 
E 5 HOH 119 719 102 HOH HOH A . 
E 5 HOH 120 720 288 HOH HOH A . 
E 5 HOH 121 721 33  HOH HOH A . 
E 5 HOH 122 722 81  HOH HOH A . 
E 5 HOH 123 723 98  HOH HOH A . 
E 5 HOH 124 724 149 HOH HOH A . 
E 5 HOH 125 725 130 HOH HOH A . 
E 5 HOH 126 726 144 HOH HOH A . 
E 5 HOH 127 727 327 HOH HOH A . 
E 5 HOH 128 728 57  HOH HOH A . 
E 5 HOH 129 729 234 HOH HOH A . 
E 5 HOH 130 730 147 HOH HOH A . 
E 5 HOH 131 731 123 HOH HOH A . 
E 5 HOH 132 732 49  HOH HOH A . 
E 5 HOH 133 733 109 HOH HOH A . 
E 5 HOH 134 734 275 HOH HOH A . 
E 5 HOH 135 735 45  HOH HOH A . 
E 5 HOH 136 736 292 HOH HOH A . 
E 5 HOH 137 737 137 HOH HOH A . 
E 5 HOH 138 738 251 HOH HOH A . 
E 5 HOH 139 739 70  HOH HOH A . 
E 5 HOH 140 740 244 HOH HOH A . 
E 5 HOH 141 741 75  HOH HOH A . 
E 5 HOH 142 742 299 HOH HOH A . 
E 5 HOH 143 743 194 HOH HOH A . 
E 5 HOH 144 744 16  HOH HOH A . 
E 5 HOH 145 745 52  HOH HOH A . 
E 5 HOH 146 746 42  HOH HOH A . 
E 5 HOH 147 747 11  HOH HOH A . 
E 5 HOH 148 748 99  HOH HOH A . 
E 5 HOH 149 749 9   HOH HOH A . 
E 5 HOH 150 750 37  HOH HOH A . 
E 5 HOH 151 751 184 HOH HOH A . 
E 5 HOH 152 752 215 HOH HOH A . 
E 5 HOH 153 753 106 HOH HOH A . 
E 5 HOH 154 754 10  HOH HOH A . 
E 5 HOH 155 755 36  HOH HOH A . 
E 5 HOH 156 756 316 HOH HOH A . 
E 5 HOH 157 757 31  HOH HOH A . 
E 5 HOH 158 758 2   HOH HOH A . 
E 5 HOH 159 759 54  HOH HOH A . 
E 5 HOH 160 760 261 HOH HOH A . 
E 5 HOH 161 761 100 HOH HOH A . 
E 5 HOH 162 762 108 HOH HOH A . 
E 5 HOH 163 763 55  HOH HOH A . 
E 5 HOH 164 764 17  HOH HOH A . 
E 5 HOH 165 765 158 HOH HOH A . 
E 5 HOH 166 766 39  HOH HOH A . 
E 5 HOH 167 767 227 HOH HOH A . 
E 5 HOH 168 768 114 HOH HOH A . 
E 5 HOH 169 769 78  HOH HOH A . 
E 5 HOH 170 770 83  HOH HOH A . 
E 5 HOH 171 771 145 HOH HOH A . 
E 5 HOH 172 772 32  HOH HOH A . 
E 5 HOH 173 773 77  HOH HOH A . 
E 5 HOH 174 774 76  HOH HOH A . 
E 5 HOH 175 775 12  HOH HOH A . 
E 5 HOH 176 776 332 HOH HOH A . 
E 5 HOH 177 777 229 HOH HOH A . 
E 5 HOH 178 778 232 HOH HOH A . 
E 5 HOH 179 779 127 HOH HOH A . 
E 5 HOH 180 780 28  HOH HOH A . 
E 5 HOH 181 781 297 HOH HOH A . 
E 5 HOH 182 782 246 HOH HOH A . 
E 5 HOH 183 783 250 HOH HOH A . 
E 5 HOH 184 784 27  HOH HOH A . 
E 5 HOH 185 785 79  HOH HOH A . 
E 5 HOH 186 786 53  HOH HOH A . 
E 5 HOH 187 787 304 HOH HOH A . 
E 5 HOH 188 788 8   HOH HOH A . 
E 5 HOH 189 789 132 HOH HOH A . 
E 5 HOH 190 790 121 HOH HOH A . 
E 5 HOH 191 791 324 HOH HOH A . 
E 5 HOH 192 792 18  HOH HOH A . 
E 5 HOH 193 793 172 HOH HOH A . 
E 5 HOH 194 794 1   HOH HOH A . 
E 5 HOH 195 795 15  HOH HOH A . 
E 5 HOH 196 796 6   HOH HOH A . 
E 5 HOH 197 797 139 HOH HOH A . 
E 5 HOH 198 798 151 HOH HOH A . 
E 5 HOH 199 799 228 HOH HOH A . 
E 5 HOH 200 800 345 HOH HOH A . 
E 5 HOH 201 801 101 HOH HOH A . 
E 5 HOH 202 802 331 HOH HOH A . 
E 5 HOH 203 803 255 HOH HOH A . 
E 5 HOH 204 804 212 HOH HOH A . 
E 5 HOH 205 805 129 HOH HOH A . 
E 5 HOH 206 806 4   HOH HOH A . 
E 5 HOH 207 807 163 HOH HOH A . 
E 5 HOH 208 808 279 HOH HOH A . 
E 5 HOH 209 809 140 HOH HOH A . 
E 5 HOH 210 810 38  HOH HOH A . 
E 5 HOH 211 811 138 HOH HOH A . 
E 5 HOH 212 812 263 HOH HOH A . 
E 5 HOH 213 813 24  HOH HOH A . 
E 5 HOH 214 814 150 HOH HOH A . 
E 5 HOH 215 815 84  HOH HOH A . 
E 5 HOH 216 816 224 HOH HOH A . 
E 5 HOH 217 817 213 HOH HOH A . 
E 5 HOH 218 818 73  HOH HOH A . 
E 5 HOH 219 819 245 HOH HOH A . 
E 5 HOH 220 820 211 HOH HOH A . 
E 5 HOH 221 821 107 HOH HOH A . 
E 5 HOH 222 822 200 HOH HOH A . 
E 5 HOH 223 823 43  HOH HOH A . 
E 5 HOH 224 824 126 HOH HOH A . 
E 5 HOH 225 825 283 HOH HOH A . 
E 5 HOH 226 826 175 HOH HOH A . 
E 5 HOH 227 827 291 HOH HOH A . 
E 5 HOH 228 828 58  HOH HOH A . 
E 5 HOH 229 829 152 HOH HOH A . 
E 5 HOH 230 830 93  HOH HOH A . 
E 5 HOH 231 831 105 HOH HOH A . 
E 5 HOH 232 832 104 HOH HOH A . 
E 5 HOH 233 833 135 HOH HOH A . 
E 5 HOH 234 834 171 HOH HOH A . 
E 5 HOH 235 835 335 HOH HOH A . 
E 5 HOH 236 836 342 HOH HOH A . 
E 5 HOH 237 837 34  HOH HOH A . 
E 5 HOH 238 838 271 HOH HOH A . 
E 5 HOH 239 839 219 HOH HOH A . 
E 5 HOH 240 840 87  HOH HOH A . 
E 5 HOH 241 841 306 HOH HOH A . 
E 5 HOH 242 842 222 HOH HOH A . 
E 5 HOH 243 843 61  HOH HOH A . 
E 5 HOH 244 844 269 HOH HOH A . 
E 5 HOH 245 845 161 HOH HOH A . 
E 5 HOH 246 846 238 HOH HOH A . 
E 5 HOH 247 847 276 HOH HOH A . 
E 5 HOH 248 848 337 HOH HOH A . 
E 5 HOH 249 849 142 HOH HOH A . 
E 5 HOH 250 850 94  HOH HOH A . 
E 5 HOH 251 851 112 HOH HOH A . 
E 5 HOH 252 852 89  HOH HOH A . 
E 5 HOH 253 853 92  HOH HOH A . 
E 5 HOH 254 854 86  HOH HOH A . 
E 5 HOH 255 855 124 HOH HOH A . 
E 5 HOH 256 856 301 HOH HOH A . 
E 5 HOH 257 857 148 HOH HOH A . 
E 5 HOH 258 858 302 HOH HOH A . 
E 5 HOH 259 859 193 HOH HOH A . 
E 5 HOH 260 860 285 HOH HOH A . 
E 5 HOH 261 861 214 HOH HOH A . 
E 5 HOH 262 862 317 HOH HOH A . 
E 5 HOH 263 863 278 HOH HOH A . 
E 5 HOH 264 864 262 HOH HOH A . 
E 5 HOH 265 865 249 HOH HOH A . 
E 5 HOH 266 866 314 HOH HOH A . 
E 5 HOH 267 867 226 HOH HOH A . 
E 5 HOH 268 868 143 HOH HOH A . 
E 5 HOH 269 869 208 HOH HOH A . 
E 5 HOH 270 870 201 HOH HOH A . 
E 5 HOH 271 871 182 HOH HOH A . 
E 5 HOH 272 872 277 HOH HOH A . 
E 5 HOH 273 873 295 HOH HOH A . 
E 5 HOH 274 874 155 HOH HOH A . 
E 5 HOH 275 875 330 HOH HOH A . 
E 5 HOH 276 876 185 HOH HOH A . 
E 5 HOH 277 877 225 HOH HOH A . 
E 5 HOH 278 878 322 HOH HOH A . 
E 5 HOH 279 879 286 HOH HOH A . 
E 5 HOH 280 880 62  HOH HOH A . 
E 5 HOH 281 881 51  HOH HOH A . 
E 5 HOH 282 882 198 HOH HOH A . 
E 5 HOH 283 883 181 HOH HOH A . 
E 5 HOH 284 884 257 HOH HOH A . 
E 5 HOH 285 885 282 HOH HOH A . 
E 5 HOH 286 886 349 HOH HOH A . 
E 5 HOH 287 887 259 HOH HOH A . 
E 5 HOH 288 888 233 HOH HOH A . 
E 5 HOH 289 889 248 HOH HOH A . 
E 5 HOH 290 890 156 HOH HOH A . 
E 5 HOH 291 891 240 HOH HOH A . 
E 5 HOH 292 892 186 HOH HOH A . 
E 5 HOH 293 893 95  HOH HOH A . 
E 5 HOH 294 894 253 HOH HOH A . 
E 5 HOH 295 895 294 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                     8WN5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.608 
_cell.length_a_esd                 ? 
_cell.length_b                     69.240 
_cell.length_b_esd                 ? 
_cell.length_c                     96.683 
_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                         8WN5 
_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                   8WN5 
_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             2.28 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.07 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'CHES, K/Na tartrate, LiSO4' 
_exptl_crystal_grow.pdbx_pH_range   8.5-9.5 
_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         2023-07-01 
_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                                       8WN5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.5 
_reflns.d_resolution_low                               48.42 
_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                                     73302 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.97 
_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                                0.035 
_reflns.pdbx_Rpim_I_all                                0.025 
_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                              0.025 
_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                                    1.50 
_reflns_shell.d_res_low                                     1.53 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           9.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3592 
_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                              0.68 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.096 
_reflns_shell.pdbx_Rpim_I_all                               0.068 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.977 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.068 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.79 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.01 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.80 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               8.278 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.953 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_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                                 8WN5 
_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                            1.50 
_refine.ls_d_res_low                             48.42 
_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                     69515 
_refine.ls_number_reflns_R_free                  3786 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17138 
_refine.ls_R_factor_R_free                       0.18541 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17060 
_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                       0.069 
_refine.pdbx_overall_ESU_R_Free                  0.067 
_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                             1.003 
_refine.overall_SU_ML                            0.038 
_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                       1.50 
_refine_hist.d_res_low                        48.42 
_refine_hist.number_atoms_solvent             295 
_refine_hist.number_atoms_total               3802 
_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        3475 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_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' ? 0.012  0.012  3661 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3304 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.843  1.649  5006 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.631  1.570  7581 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.481  5.000  454  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 6.688  5.000  29   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.647 10.000 522  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.095  0.200  521  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  4441 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  907  ? 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' ? 1.166  0.736  1798 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.165  0.736  1798 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.832  1.323  2255 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.832  1.323  2256 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.026  0.936  1863 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.026  0.937  1864 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.048  1.628  2751 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.111  8.82   4257 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.111  8.82   4258 ? 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                       1.500 
_refine_ls_shell.d_res_low                        1.539 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             299 
_refine_ls_shell.number_reflns_R_work             5082 
_refine_ls_shell.percent_reflns_obs               99.98 
_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                  0.232 
_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                  0.232 
# 
_struct.entry_id                     8WN5 
_struct.title                        'Crystal structure of GH1 beta-glucosidase Td2F2 E352Q glucose 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        8WN5 
_struct_keywords.text            'beta-Glucosidase, E352Q nucleophile mutants, Glucose 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 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8WN5 
_struct_ref.pdbx_db_accession          8WN5 
_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              8WN5 
_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             8WN5 
_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 
# 
_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_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 4.72  
2 LEU 328 A . ? LEU 308 A PRO 329 A ? PRO 309 A 1 5.66  
3 ARG 366 A . ? ARG 346 A PRO 367 A ? PRO 347 A 1 -6.66 
4 TRP 419 A . ? TRP 399 A SER 420 A ? SER 400 A 1 -7.38 
# 
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 TYR A 96  ? N TYR A 76  O PHE A 136 ? O PHE A 116 
AA1 3 4 N VAL A 137 ? N VAL A 117 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                   8WN5 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             406 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             406 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.330 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            0.078 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 84  ? ? CZ A ARG 84  ? ? NH2 A ARG 84  ? ? 115.94 120.30 -4.36 0.50 N 
2 1 NE A ARG 209 ? ? CZ A ARG 209 ? ? NH2 A ARG 209 ? ? 116.96 120.30 -3.34 0.50 N 
3 1 NE A ARG 372 ? ? CZ A ARG 372 ? ? NH1 A ARG 372 ? ? 123.37 120.30 3.07  0.50 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  ? ? 56.55   -123.44 
2  1 TRP A 122 ? ? 95.43   -3.73   
3  1 LEU A 132 ? ? 89.35   -3.43   
4  1 THR A 163 ? ? -73.38  -72.32  
5  1 ASN A 248 ? ? -97.07  -61.27  
6  1 THR A 322 ? ? -89.04  -156.28 
7  1 ASP A 324 ? ? -140.09 -7.44   
8  1 TYR A 328 ? ? -150.93 80.18   
9  1 ARG A 346 ? ? -173.89 147.16  
10 1 GLU A 406 ? ? -92.53  58.93   
11 1 TRP A 407 ? ? 52.74   -129.73 
# 
_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 ARG 444 ? A ARG 464 
22 1 Y 1 A GLY 445 ? A GLY 465 
# 
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 
NHE "C3'"  C N N 285 
NHE "C2'"  C N N 286 
NHE "C1'"  C N N 287 
NHE "C6'"  C N N 288 
NHE N      N N N 289 
NHE C1     C N N 290 
NHE C2     C N N 291 
NHE S      S N N 292 
NHE O1     O N N 293 
NHE O2     O N N 294 
NHE O3     O N N 295 
NHE "C5'"  C N N 296 
NHE "C4'"  C N N 297 
NHE "H3'1" H N N 298 
NHE "H3'2" H N N 299 
NHE "H2'1" H N N 300 
NHE "H2'2" H N N 301 
NHE "HC'1" H N N 302 
NHE "H6'1" H N N 303 
NHE "H6'2" H N N 304 
NHE HN     H N N 305 
NHE HC11   H N N 306 
NHE HC12   H N N 307 
NHE HC21   H N N 308 
NHE HC22   H N N 309 
NHE HO3    H N N 310 
NHE "H5'1" H N N 311 
NHE "H5'2" H N N 312 
NHE "H4'1" H N N 313 
NHE "H4'2" H N N 314 
PHE N      N N N 315 
PHE CA     C N S 316 
PHE C      C N N 317 
PHE O      O N N 318 
PHE CB     C N N 319 
PHE CG     C Y N 320 
PHE CD1    C Y N 321 
PHE CD2    C Y N 322 
PHE CE1    C Y N 323 
PHE CE2    C Y N 324 
PHE CZ     C Y N 325 
PHE OXT    O N N 326 
PHE H      H N N 327 
PHE H2     H N N 328 
PHE HA     H N N 329 
PHE HB2    H N N 330 
PHE HB3    H N N 331 
PHE HD1    H N N 332 
PHE HD2    H N N 333 
PHE HE1    H N N 334 
PHE HE2    H N N 335 
PHE HZ     H N N 336 
PHE HXT    H N N 337 
PRO N      N N N 338 
PRO CA     C N S 339 
PRO C      C N N 340 
PRO O      O N N 341 
PRO CB     C N N 342 
PRO CG     C N N 343 
PRO CD     C N N 344 
PRO OXT    O N N 345 
PRO H      H N N 346 
PRO HA     H N N 347 
PRO HB2    H N N 348 
PRO HB3    H N N 349 
PRO HG2    H N N 350 
PRO HG3    H N N 351 
PRO HD2    H N N 352 
PRO HD3    H N N 353 
PRO HXT    H N N 354 
SER N      N N N 355 
SER CA     C N S 356 
SER C      C N N 357 
SER O      O N N 358 
SER CB     C N N 359 
SER OG     O N N 360 
SER OXT    O N N 361 
SER H      H N N 362 
SER H2     H N N 363 
SER HA     H N N 364 
SER HB2    H N N 365 
SER HB3    H N N 366 
SER HG     H N N 367 
SER HXT    H N N 368 
THR N      N N N 369 
THR CA     C N S 370 
THR C      C N N 371 
THR O      O N N 372 
THR CB     C N R 373 
THR OG1    O N N 374 
THR CG2    C N N 375 
THR OXT    O N N 376 
THR H      H N N 377 
THR H2     H N N 378 
THR HA     H N N 379 
THR HB     H N N 380 
THR HG1    H N N 381 
THR HG21   H N N 382 
THR HG22   H N N 383 
THR HG23   H N N 384 
THR HXT    H N N 385 
TRP N      N N N 386 
TRP CA     C N S 387 
TRP C      C N N 388 
TRP O      O N N 389 
TRP CB     C N N 390 
TRP CG     C Y N 391 
TRP CD1    C Y N 392 
TRP CD2    C Y N 393 
TRP NE1    N Y N 394 
TRP CE2    C Y N 395 
TRP CE3    C Y N 396 
TRP CZ2    C Y N 397 
TRP CZ3    C Y N 398 
TRP CH2    C Y N 399 
TRP OXT    O N N 400 
TRP H      H N N 401 
TRP H2     H N N 402 
TRP HA     H N N 403 
TRP HB2    H N N 404 
TRP HB3    H N N 405 
TRP HD1    H N N 406 
TRP HE1    H N N 407 
TRP HE3    H N N 408 
TRP HZ2    H N N 409 
TRP HZ3    H N N 410 
TRP HH2    H N N 411 
TRP HXT    H N N 412 
TYR N      N N N 413 
TYR CA     C N S 414 
TYR C      C N N 415 
TYR O      O N N 416 
TYR CB     C N N 417 
TYR CG     C Y N 418 
TYR CD1    C Y N 419 
TYR CD2    C Y N 420 
TYR CE1    C Y N 421 
TYR CE2    C Y N 422 
TYR CZ     C Y N 423 
TYR OH     O N N 424 
TYR OXT    O N N 425 
TYR H      H N N 426 
TYR H2     H N N 427 
TYR HA     H N N 428 
TYR HB2    H N N 429 
TYR HB3    H N N 430 
TYR HD1    H N N 431 
TYR HD2    H N N 432 
TYR HE1    H N N 433 
TYR HE2    H N N 434 
TYR HH     H N N 435 
TYR HXT    H N N 436 
VAL N      N N N 437 
VAL CA     C N S 438 
VAL C      C N N 439 
VAL O      O N N 440 
VAL CB     C N N 441 
VAL CG1    C N N 442 
VAL CG2    C N N 443 
VAL OXT    O N N 444 
VAL H      H N N 445 
VAL H2     H N N 446 
VAL HA     H N N 447 
VAL HB     H N N 448 
VAL HG11   H N N 449 
VAL HG12   H N N 450 
VAL HG13   H N N 451 
VAL HG21   H N N 452 
VAL HG22   H N N 453 
VAL HG23   H N N 454 
VAL HXT    H N N 455 
# 
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 
# 
_atom_sites.entry_id                    8WN5 
_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]   0.014791 
_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]   0.014443 
_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]   0.010343 
_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 
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     . MET A 1 21  ? 5.698   -0.021  10.444  1.00 20.56 ? 1   MET A N     1 
ATOM   2    C CA    . MET A 1 21  ? 5.625   -0.655  11.788  1.00 17.45 ? 1   MET A CA    1 
ATOM   3    C C     . MET A 1 21  ? 7.009   -1.247  12.107  1.00 12.68 ? 1   MET A C     1 
ATOM   4    O O     . MET A 1 21  ? 7.938   -1.312  11.266  1.00 10.63 ? 1   MET A O     1 
ATOM   5    C CB    . MET A 1 21  ? 4.520   -1.720  11.873  1.00 27.56 ? 1   MET A CB    1 
ATOM   6    C CG    . MET A 1 21  ? 3.476   -1.528  12.995  1.00 25.89 ? 1   MET A CG    1 
ATOM   7    S SD    . MET A 1 21  ? 3.369   0.082   13.812  1.00 41.15 ? 1   MET A SD    1 
ATOM   8    C CE    . MET A 1 21  ? 3.122   -0.406  15.523  1.00 33.51 ? 1   MET A CE    1 
ATOM   9    N N     . ALA A 1 22  ? 7.134   -1.736  13.333  1.00 10.44 ? 2   ALA A N     1 
ATOM   10   C CA    . ALA A 1 22  ? 8.435   -2.103  13.859  1.00 10.41 ? 2   ALA A CA    1 
ATOM   11   C C     . ALA A 1 22  ? 9.002   -3.272  13.087  1.00 10.85 ? 2   ALA A C     1 
ATOM   12   O O     . ALA A 1 22  ? 8.338   -4.306  13.007  1.00 10.10 ? 2   ALA A O     1 
ATOM   13   C CB    . ALA A 1 22  ? 8.332   -2.450  15.323  1.00 9.67  ? 2   ALA A CB    1 
ATOM   14   N N     . GLY A 1 23  ? 10.229  -3.113  12.572  1.00 11.40 ? 3   GLY A N     1 
ATOM   15   C CA    . GLY A 1 23  ? 10.860  -4.183  11.824  1.00 11.63 ? 3   GLY A CA    1 
ATOM   16   C C     . GLY A 1 23  ? 10.342  -4.291  10.391  1.00 12.95 ? 3   GLY A C     1 
ATOM   17   O O     . GLY A 1 23  ? 10.672  -5.243  9.692   1.00 14.62 ? 3   GLY A O     1 
ATOM   18   N N     . GLU A 1 24  ? 9.399   -3.417  9.998   1.00 11.55 ? 4   GLU A N     1 
ATOM   19   C CA    . GLU A 1 24  ? 8.761   -3.525  8.692   1.00 12.59 ? 4   GLU A CA    1 
ATOM   20   C C     . GLU A 1 24  ? 9.109   -2.341  7.816   1.00 10.93 ? 4   GLU A C     1 
ATOM   21   O O     . GLU A 1 24  ? 8.589   -2.205  6.692   1.00 12.08 ? 4   GLU A O     1 
ATOM   22   C CB    . GLU A 1 24  ? 7.248   -3.569  8.810   1.00 14.80 ? 4   GLU A CB    1 
ATOM   23   C CG    . GLU A 1 24  ? 6.758   -4.734  9.622   1.00 17.50 ? 4   GLU A CG    1 
ATOM   24   C CD    . GLU A 1 24  ? 5.251   -4.666  9.674   1.00 23.68 ? 4   GLU A CD    1 
ATOM   25   O OE1   . GLU A 1 24  ? 4.624   -4.878  8.602   1.00 28.55 ? 4   GLU A OE1   1 
ATOM   26   O OE2   . GLU A 1 24  ? 4.745   -4.269  10.730  1.00 29.27 ? 4   GLU A OE2   1 
ATOM   27   N N     . ARG A 1 25  ? 9.975   -1.441  8.275   1.00 8.61  ? 5   ARG A N     1 
ATOM   28   C CA    . ARG A 1 25  ? 10.263  -0.279  7.475   1.00 8.70  ? 5   ARG A CA    1 
ATOM   29   C C     . ARG A 1 25  ? 11.471  -0.476  6.572   1.00 8.11  ? 5   ARG A C     1 
ATOM   30   O O     . ARG A 1 25  ? 12.511  -1.060  6.893   1.00 8.49  ? 5   ARG A O     1 
ATOM   31   C CB    . ARG A 1 25  ? 10.514  0.939   8.359   1.00 8.20  ? 5   ARG A CB    1 
ATOM   32   C CG    . ARG A 1 25  ? 9.281   1.365   9.123   1.00 8.62  ? 5   ARG A CG    1 
ATOM   33   C CD    . ARG A 1 25  ? 9.489   2.712   9.755   1.00 8.60  ? 5   ARG A CD    1 
ATOM   34   N NE    . ARG A 1 25  ? 8.301   3.050   10.505  1.00 9.81  ? 5   ARG A NE    1 
ATOM   35   C CZ    . ARG A 1 25  ? 7.207   3.615   10.019  1.00 11.51 ? 5   ARG A CZ    1 
ATOM   36   N NH1   . ARG A 1 25  ? 7.187   3.984   8.738   1.00 15.83 ? 5   ARG A NH1   1 
ATOM   37   N NH2   . ARG A 1 25  ? 6.166   3.793   10.820  1.00 13.79 ? 5   ARG A NH2   1 
ATOM   38   N N     . PHE A 1 26  ? 11.312  0.023   5.356   1.00 8.29  ? 6   PHE A N     1 
ATOM   39   C CA    . PHE A 1 26  ? 12.325  0.096   4.345   1.00 7.87  ? 6   PHE A CA    1 
ATOM   40   C C     . PHE A 1 26  ? 12.923  1.500   4.303   1.00 7.17  ? 6   PHE A C     1 
ATOM   41   O O     . PHE A 1 26  ? 12.309  2.449   4.792   1.00 8.28  ? 6   PHE A O     1 
ATOM   42   C CB    . PHE A 1 26  ? 11.690  -0.327  3.021   1.00 7.53  ? 6   PHE A CB    1 
ATOM   43   C CG    . PHE A 1 26  ? 11.399  -1.796  2.893   1.00 7.58  ? 6   PHE A CG    1 
ATOM   44   C CD1   . PHE A 1 26  ? 10.331  -2.370  3.533   1.00 7.54  ? 6   PHE A CD1   1 
ATOM   45   C CD2   . PHE A 1 26  ? 12.280  -2.625  2.234   1.00 7.44  ? 6   PHE A CD2   1 
ATOM   46   C CE1   . PHE A 1 26  ? 10.049  -3.721  3.422   1.00 8.02  ? 6   PHE A CE1   1 
ATOM   47   C CE2   . PHE A 1 26  ? 12.012  -3.973  2.124   1.00 7.54  ? 6   PHE A CE2   1 
ATOM   48   C CZ    . PHE A 1 26  ? 10.931  -4.525  2.743   1.00 7.00  ? 6   PHE A CZ    1 
ATOM   49   N N     . PRO A 1 27  ? 14.079  1.707   3.668   1.00 7.78  ? 7   PRO A N     1 
ATOM   50   C CA    . PRO A 1 27  ? 14.640  3.053   3.590   1.00 7.93  ? 7   PRO A CA    1 
ATOM   51   C C     . PRO A 1 27  ? 13.693  4.013   2.877   1.00 8.75  ? 7   PRO A C     1 
ATOM   52   O O     . PRO A 1 27  ? 12.914  3.628   2.012   1.00 8.14  ? 7   PRO A O     1 
ATOM   53   C CB    . PRO A 1 27  ? 15.932  2.880   2.820   1.00 9.20  ? 7   PRO A CB    1 
ATOM   54   C CG    . PRO A 1 27  ? 16.258  1.412   2.993   1.00 9.38  ? 7   PRO A CG    1 
ATOM   55   C CD    . PRO A 1 27  ? 14.958  0.682   3.084   1.00 8.27  ? 7   PRO A CD    1 
ATOM   56   N N     . ALA A 1 28  ? 13.745  5.304   3.217   1.00 9.17  ? 8   ALA A N     1 
ATOM   57   C CA    . ALA A 1 28  ? 12.838  6.269   2.665   1.00 9.62  ? 8   ALA A CA    1 
ATOM   58   C C     . ALA A 1 28  ? 13.078  6.448   1.171   1.00 10.09 ? 8   ALA A C     1 
ATOM   59   O O     . ALA A 1 28  ? 12.193  6.932   0.487   1.00 11.36 ? 8   ALA A O     1 
ATOM   60   C CB    . ALA A 1 28  ? 13.048  7.602   3.365   1.00 10.98 ? 8   ALA A CB    1 
ATOM   61   N N     . ASP A 1 29  ? 14.273  6.131   0.691   1.00 9.65  ? 9   ASP A N     1 
ATOM   62   C CA    . ASP A 1 29  ? 14.642  6.267   -0.724  1.00 9.55  ? 9   ASP A CA    1 
ATOM   63   C C     . ASP A 1 29  ? 14.562  4.926   -1.478  1.00 7.81  ? 9   ASP A C     1 
ATOM   64   O O     . ASP A 1 29  ? 14.984  4.808   -2.631  1.00 8.65  ? 9   ASP A O     1 
ATOM   65   C CB    . ASP A 1 29  ? 15.981  6.946   -0.916  1.00 12.72 ? 9   ASP A CB    1 
ATOM   66   C CG    . ASP A 1 29  ? 17.146  6.150   -0.376  1.00 13.55 ? 9   ASP A CG    1 
ATOM   67   O OD1   . ASP A 1 29  ? 16.908  5.161   0.330   1.00 15.47 ? 9   ASP A OD1   1 
ATOM   68   O OD2   . ASP A 1 29  ? 18.289  6.525   -0.656  1.00 23.40 ? 9   ASP A OD2   1 
ATOM   69   N N     . PHE A 1 30  ? 13.930  3.948   -0.862  1.00 6.66  ? 10  PHE A N     1 
ATOM   70   C CA    . PHE A 1 30  ? 13.772  2.629   -1.475  1.00 5.60  ? 10  PHE A CA    1 
ATOM   71   C C     . PHE A 1 30  ? 12.949  2.777   -2.750  1.00 5.59  ? 10  PHE A C     1 
ATOM   72   O O     . PHE A 1 30  ? 11.961  3.508   -2.779  1.00 6.42  ? 10  PHE A O     1 
ATOM   73   C CB    . PHE A 1 30  ? 13.153  1.657   -0.475  1.00 5.74  ? 10  PHE A CB    1 
ATOM   74   C CG    . PHE A 1 30  ? 13.316  0.203   -0.765  1.00 5.50  ? 10  PHE A CG    1 
ATOM   75   C CD1   . PHE A 1 30  ? 14.543  -0.392  -0.546  1.00 5.81  ? 10  PHE A CD1   1 
ATOM   76   C CD2   . PHE A 1 30  ? 12.252  -0.589  -1.166  1.00 5.57  ? 10  PHE A CD2   1 
ATOM   77   C CE1   . PHE A 1 30  ? 14.696  -1.753  -0.718  1.00 5.39  ? 10  PHE A CE1   1 
ATOM   78   C CE2   . PHE A 1 30  ? 12.429  -1.952  -1.363  1.00 5.55  ? 10  PHE A CE2   1 
ATOM   79   C CZ    . PHE A 1 30  ? 13.647  -2.530  -1.104  1.00 5.52  ? 10  PHE A CZ    1 
ATOM   80   N N     . VAL A 1 31  ? 13.304  2.007   -3.759  1.00 4.81  ? 11  VAL A N     1 
ATOM   81   C CA    . VAL A 1 31  ? 12.520  1.979   -4.989  1.00 4.58  ? 11  VAL A CA    1 
ATOM   82   C C     . VAL A 1 31  ? 11.435  0.922   -4.867  1.00 4.26  ? 11  VAL A C     1 
ATOM   83   O O     . VAL A 1 31  ? 11.683  -0.227  -4.513  1.00 4.57  ? 11  VAL A O     1 
ATOM   84   C CB    . VAL A 1 31  ? 13.505  1.694   -6.133  1.00 5.23  ? 11  VAL A CB    1 
ATOM   85   C CG1   . VAL A 1 31  ? 12.772  1.354   -7.400  1.00 5.74  ? 11  VAL A CG1   1 
ATOM   86   C CG2   . VAL A 1 31  ? 14.486  2.812   -6.392  1.00 5.65  ? 11  VAL A CG2   1 
ATOM   87   N N     . TRP A 1 32  ? 10.195  1.311   -5.163  1.00 3.36  ? 12  TRP A N     1 
ATOM   88   C CA    . TRP A 1 32  ? 9.014   0.495   -5.072  1.00 3.27  ? 12  TRP A CA    1 
ATOM   89   C C     . TRP A 1 32  ? 8.340   0.545   -6.431  1.00 2.89  ? 12  TRP A C     1 
ATOM   90   O O     . TRP A 1 32  ? 7.852   1.613   -6.825  1.00 3.00  ? 12  TRP A O     1 
ATOM   91   C CB    . TRP A 1 32  ? 8.033   1.047   -4.041  1.00 3.71  ? 12  TRP A CB    1 
ATOM   92   C CG    . TRP A 1 32  ? 8.456   0.834   -2.621  1.00 4.35  ? 12  TRP A CG    1 
ATOM   93   C CD1   . TRP A 1 32  ? 8.869   1.803   -1.750  1.00 4.74  ? 12  TRP A CD1   1 
ATOM   94   C CD2   . TRP A 1 32  ? 8.472   -0.408  -1.909  1.00 5.27  ? 12  TRP A CD2   1 
ATOM   95   N NE1   . TRP A 1 32  ? 9.101   1.256   -0.514  1.00 5.37  ? 12  TRP A NE1   1 
ATOM   96   C CE2   . TRP A 1 32  ? 8.860   -0.089  -0.579  1.00 5.43  ? 12  TRP A CE2   1 
ATOM   97   C CE3   . TRP A 1 32  ? 8.202   -1.744  -2.255  1.00 5.39  ? 12  TRP A CE3   1 
ATOM   98   C CZ2   . TRP A 1 32  ? 9.013   -1.094  0.383   1.00 5.77  ? 12  TRP A CZ2   1 
ATOM   99   C CZ3   . TRP A 1 32  ? 8.318   -2.735  -1.295  1.00 6.07  ? 12  TRP A CZ3   1 
ATOM   100  C CH2   . TRP A 1 32  ? 8.721   -2.403  0.016   1.00 5.96  ? 12  TRP A CH2   1 
ATOM   101  N N     . GLY A 1 33  ? 8.290   -0.573  -7.128  1.00 2.54  ? 13  GLY A N     1 
ATOM   102  C CA    . GLY A 1 33  ? 7.669   -0.592  -8.434  1.00 2.32  ? 13  GLY A CA    1 
ATOM   103  C C     . GLY A 1 33  ? 6.995   -1.914  -8.732  1.00 2.09  ? 13  GLY A C     1 
ATOM   104  O O     . GLY A 1 33  ? 6.820   -2.819  -7.905  1.00 2.23  ? 13  GLY A O     1 
ATOM   105  N N     . ALA A 1 34  ? 6.480   -1.958  -9.962  1.00 1.94  ? 14  ALA A N     1 
ATOM   106  C CA    . ALA A 1 34  ? 6.030   -3.174  -10.582 1.00 1.84  ? 14  ALA A CA    1 
ATOM   107  C C     . ALA A 1 34  ? 6.706   -3.253  -11.947 1.00 1.70  ? 14  ALA A C     1 
ATOM   108  O O     . ALA A 1 34  ? 7.258   -2.257  -12.427 1.00 1.66  ? 14  ALA A O     1 
ATOM   109  C CB    . ALA A 1 34  ? 4.528   -3.219  -10.677 1.00 1.91  ? 14  ALA A CB    1 
ATOM   110  N N     . ALA A 1 35  ? 6.726   -4.455  -12.515 1.00 1.56  ? 15  ALA A N     1 
ATOM   111  C CA    . ALA A 1 35  ? 7.525   -4.729  -13.715 1.00 1.45  ? 15  ALA A CA    1 
ATOM   112  C C     . ALA A 1 35  ? 6.661   -5.396  -14.780 1.00 1.35  ? 15  ALA A C     1 
ATOM   113  O O     . ALA A 1 35  ? 5.720   -6.130  -14.498 1.00 1.48  ? 15  ALA A O     1 
ATOM   114  C CB    . ALA A 1 35  ? 8.685   -5.626  -13.386 1.00 1.51  ? 15  ALA A CB    1 
ATOM   115  N N     . THR A 1 36  ? 7.060   -5.168  -16.032 1.00 1.20  ? 16  THR A N     1 
ATOM   116  C CA    . THR A 1 36  ? 6.499   -5.769  -17.227 1.00 1.11  ? 16  THR A CA    1 
ATOM   117  C C     . THR A 1 36  ? 7.621   -5.975  -18.262 1.00 1.02  ? 16  THR A C     1 
ATOM   118  O O     . THR A 1 36  ? 8.764   -5.534  -18.077 1.00 1.05  ? 16  THR A O     1 
ATOM   119  C CB    . THR A 1 36  ? 5.438   -4.889  -17.882 1.00 1.12  ? 16  THR A CB    1 
ATOM   120  O OG1   . THR A 1 36  ? 6.053   -3.671  -18.265 1.00 1.10  ? 16  THR A OG1   1 
ATOM   121  C CG2   . THR A 1 36  ? 4.253   -4.624  -16.980 1.00 1.19  ? 16  THR A CG2   1 
ATOM   122  N N     . ALA A 1 37  ? 7.270   -6.673  -19.341 1.00 0.91  ? 17  ALA A N     1 
ATOM   123  C CA    . ALA A 1 37  ? 8.097   -6.887  -20.530 1.00 0.86  ? 17  ALA A CA    1 
ATOM   124  C C     . ALA A 1 37  ? 7.292   -6.529  -21.753 1.00 0.84  ? 17  ALA A C     1 
ATOM   125  O O     . ALA A 1 37  ? 6.103   -6.828  -21.830 1.00 0.81  ? 17  ALA A O     1 
ATOM   126  C CB    . ALA A 1 37  ? 8.528   -8.316  -20.665 1.00 0.85  ? 17  ALA A CB    1 
ATOM   127  N N     . ALA A 1 38  ? 7.940   -5.987  -22.769 1.00 0.82  ? 18  ALA A N     1 
ATOM   128  C CA    . ALA A 1 38  ? 7.260   -5.403  -23.930 1.00 0.84  ? 18  ALA A CA    1 
ATOM   129  C C     . ALA A 1 38  ? 6.392   -6.407  -24.643 1.00 0.89  ? 18  ALA A C     1 
ATOM   130  O O     . ALA A 1 38  ? 5.229   -6.113  -24.931 1.00 0.87  ? 18  ALA A O     1 
ATOM   131  C CB    . ALA A 1 38  ? 8.250   -4.796  -24.882 1.00 0.82  ? 18  ALA A CB    1 
ATOM   132  N N     . TYR A 1 39  ? 6.923   -7.584  -25.002 1.00 0.93  ? 19  TYR A N     1 
ATOM   133  C CA    . TYR A 1 39  ? 6.094   -8.488  -25.813 1.00 1.05  ? 19  TYR A CA    1 
ATOM   134  C C     . TYR A 1 39  ? 4.906   -8.996  -25.007 1.00 1.07  ? 19  TYR A C     1 
ATOM   135  O O     . TYR A 1 39  ? 3.864   -9.362  -25.543 1.00 1.02  ? 19  TYR A O     1 
ATOM   136  C CB    . TYR A 1 39  ? 6.904   -9.663  -26.398 1.00 1.20  ? 19  TYR A CB    1 
ATOM   137  C CG    . TYR A 1 39  ? 6.115   -10.485 -27.366 1.00 1.39  ? 19  TYR A CG    1 
ATOM   138  C CD1   . TYR A 1 39  ? 5.887   -10.024 -28.658 1.00 1.55  ? 19  TYR A CD1   1 
ATOM   139  C CD2   . TYR A 1 39  ? 5.510   -11.658 -26.987 1.00 1.47  ? 19  TYR A CD2   1 
ATOM   140  C CE1   . TYR A 1 39  ? 5.094   -10.723 -29.559 1.00 1.67  ? 19  TYR A CE1   1 
ATOM   141  C CE2   . TYR A 1 39  ? 4.734   -12.384 -27.886 1.00 1.68  ? 19  TYR A CE2   1 
ATOM   142  C CZ    . TYR A 1 39  ? 4.481   -11.884 -29.146 1.00 1.87  ? 19  TYR A CZ    1 
ATOM   143  O OH    . TYR A 1 39  ? 3.645   -12.588 -30.016 1.00 2.57  ? 19  TYR A OH    1 
ATOM   144  N N     . GLN A 1 40  ? 5.060   -9.057  -23.699 1.00 1.12  ? 20  GLN A N     1 
ATOM   145  C CA    . GLN A 1 40  ? 4.014   -9.615  -22.860 1.00 1.23  ? 20  GLN A CA    1 
ATOM   146  C C     . GLN A 1 40  ? 2.799   -8.682  -22.813 1.00 1.22  ? 20  GLN A C     1 
ATOM   147  O O     . GLN A 1 40  ? 1.691   -9.161  -22.498 1.00 1.26  ? 20  GLN A O     1 
ATOM   148  C CB    . GLN A 1 40  ? 4.508   -9.911  -21.454 1.00 1.39  ? 20  GLN A CB    1 
ATOM   149  C CG    . GLN A 1 40  ? 5.619   -10.955 -21.496 1.00 1.56  ? 20  GLN A CG    1 
ATOM   150  C CD    . GLN A 1 40  ? 5.920   -11.441 -20.085 1.00 1.92  ? 20  GLN A CD    1 
ATOM   151  O OE1   . GLN A 1 40  ? 6.772   -10.903 -19.372 1.00 2.49  ? 20  GLN A OE1   1 
ATOM   152  N NE2   . GLN A 1 40  ? 5.244   -12.501 -19.699 1.00 2.17  ? 20  GLN A NE2   1 
ATOM   153  N N     . ILE A 1 41  ? 3.007   -7.374  -22.953 1.00 1.20  ? 21  ILE A N     1 
ATOM   154  C CA    . ILE A 1 41  ? 1.963   -6.390  -22.696 1.00 1.19  ? 21  ILE A CA    1 
ATOM   155  C C     . ILE A 1 41  ? 1.600   -5.524  -23.900 1.00 1.27  ? 21  ILE A C     1 
ATOM   156  O O     . ILE A 1 41  ? 0.487   -5.026  -23.957 1.00 1.31  ? 21  ILE A O     1 
ATOM   157  C CB    . ILE A 1 41  ? 2.243   -5.474  -21.493 1.00 1.16  ? 21  ILE A CB    1 
ATOM   158  C CG1   . ILE A 1 41  ? 3.438   -4.530  -21.708 1.00 1.17  ? 21  ILE A CG1   1 
ATOM   159  C CG2   . ILE A 1 41  ? 2.467   -6.276  -20.227 1.00 1.13  ? 21  ILE A CG2   1 
ATOM   160  C CD1   . ILE A 1 41  ? 3.506   -3.442  -20.670 1.00 1.17  ? 21  ILE A CD1   1 
ATOM   161  N N     . GLU A 1 42  ? 2.509   -5.233  -24.820 1.00 1.31  ? 22  GLU A N     1 
ATOM   162  C CA    . GLU A 1 42  ? 2.275   -4.087  -25.711 1.00 1.42  ? 22  GLU A CA    1 
ATOM   163  C C     . GLU A 1 42  ? 1.229   -4.307  -26.797 1.00 1.48  ? 22  GLU A C     1 
ATOM   164  O O     . GLU A 1 42  ? 0.523   -3.336  -27.145 1.00 1.63  ? 22  GLU A O     1 
ATOM   165  C CB    . GLU A 1 42  ? 3.568   -3.652  -26.392 1.00 1.47  ? 22  GLU A CB    1 
ATOM   166  C CG    . GLU A 1 42  ? 4.535   -2.937  -25.486 1.00 1.56  ? 22  GLU A CG    1 
ATOM   167  C CD    . GLU A 1 42  ? 5.790   -2.430  -26.166 1.00 1.71  ? 22  GLU A CD    1 
ATOM   168  O OE1   . GLU A 1 42  ? 5.968   -2.673  -27.383 1.00 2.19  ? 22  GLU A OE1   1 
ATOM   169  O OE2   . GLU A 1 42  ? 6.558   -1.677  -25.474 1.00 1.76  ? 22  GLU A OE2   1 
ATOM   170  N N     . GLY A 1 43  ? 1.252   -5.488  -27.415 1.00 1.52  ? 23  GLY A N     1 
ATOM   171  C CA    . GLY A 1 43  ? 0.441   -5.601  -28.626 1.00 1.63  ? 23  GLY A CA    1 
ATOM   172  C C     . GLY A 1 43  ? 0.965   -4.715  -29.739 1.00 1.84  ? 23  GLY A C     1 
ATOM   173  O O     . GLY A 1 43  ? 2.165   -4.431  -29.801 1.00 1.99  ? 23  GLY A O     1 
ATOM   174  N N     . ALA A 1 44  ? 0.077   -4.230  -30.625 1.00 2.04  ? 24  ALA A N     1 
ATOM   175  C CA    . ALA A 1 44  ? 0.484   -3.338  -31.700 1.00 2.34  ? 24  ALA A CA    1 
ATOM   176  C C     . ALA A 1 44  ? 1.729   -3.867  -32.426 1.00 2.65  ? 24  ALA A C     1 
ATOM   177  O O     . ALA A 1 44  ? 2.690   -3.134  -32.689 1.00 2.54  ? 24  ALA A O     1 
ATOM   178  C CB    . ALA A 1 44  ? 0.691   -1.949  -31.160 1.00 2.39  ? 24  ALA A CB    1 
ATOM   179  N N     . VAL A 1 45  ? 1.722   -5.151  -32.754 1.00 3.27  ? 25  VAL A N     1 
ATOM   180  C CA    . VAL A 1 45  ? 2.915   -5.873  -33.187 1.00 3.79  ? 25  VAL A CA    1 
ATOM   181  C C     . VAL A 1 45  ? 3.430   -5.408  -34.544 1.00 4.70  ? 25  VAL A C     1 
ATOM   182  O O     . VAL A 1 45  ? 4.586   -5.612  -34.812 1.00 4.44  ? 25  VAL A O     1 
ATOM   183  C CB    . VAL A 1 45  ? 2.782   -7.402  -33.107 1.00 3.90  ? 25  VAL A CB    1 
ATOM   184  C CG1   . VAL A 1 45  ? 2.693   -7.931  -31.681 1.00 3.89  ? 25  VAL A CG1   1 
ATOM   185  C CG2   . VAL A 1 45  ? 1.562   -7.877  -33.905 1.00 4.07  ? 25  VAL A CG2   1 
ATOM   186  N N     . ARG A 1 46  ? 2.547   -4.891  -35.384 1.00 6.59  ? 26  ARG A N     1 
ATOM   187  C CA    . ARG A 1 46  ? 2.959   -4.434  -36.701 1.00 9.16  ? 26  ARG A CA    1 
ATOM   188  C C     . ARG A 1 46  ? 2.841   -2.924  -36.840 1.00 9.18  ? 26  ARG A C     1 
ATOM   189  O O     . ARG A 1 46  ? 3.056   -2.401  -37.939 1.00 11.63 ? 26  ARG A O     1 
ATOM   190  C CB    . ARG A 1 46  ? 2.020   -4.955  -37.797 1.00 13.06 ? 26  ARG A CB    1 
ATOM   191  C CG    . ARG A 1 46  ? 1.588   -6.400  -37.660 1.00 18.45 ? 26  ARG A CG    1 
ATOM   192  C CD    . ARG A 1 46  ? 2.826   -7.220  -37.521 1.00 22.18 ? 26  ARG A CD    1 
ATOM   193  N NE    . ARG A 1 46  ? 3.901   -6.670  -38.333 1.00 28.42 ? 26  ARG A NE    1 
ATOM   194  C CZ    . ARG A 1 46  ? 5.191   -6.667  -38.003 1.00 25.58 ? 26  ARG A CZ    1 
ATOM   195  N NH1   . ARG A 1 46  ? 6.072   -6.253  -38.894 1.00 25.93 ? 26  ARG A NH1   1 
ATOM   196  N NH2   . ARG A 1 46  ? 5.586   -7.186  -36.848 1.00 22.74 ? 26  ARG A NH2   1 
ATOM   197  N N     . GLU A 1 47  ? 2.574   -2.217  -35.764 1.00 6.77  ? 27  GLU A N     1 
ATOM   198  C CA    . GLU A 1 47  ? 2.292   -0.803  -35.828 1.00 6.91  ? 27  GLU A CA    1 
ATOM   199  C C     . GLU A 1 47  ? 3.573   0.020   -35.785 1.00 5.61  ? 27  GLU A C     1 
ATOM   200  O O     . GLU A 1 47  ? 4.571   -0.355  -35.130 1.00 5.29  ? 27  GLU A O     1 
ATOM   201  C CB    . GLU A 1 47  ? 1.343   -0.375  -34.725 1.00 8.45  ? 27  GLU A CB    1 
ATOM   202  C CG    . GLU A 1 47  ? -0.015  -1.002  -34.893 1.00 10.19 ? 27  GLU A CG    1 
ATOM   203  C CD    . GLU A 1 47  ? -1.094  -0.371  -34.029 1.00 13.92 ? 27  GLU A CD    1 
ATOM   204  O OE1   . GLU A 1 47  ? -0.955  0.796   -33.703 1.00 14.86 ? 27  GLU A OE1   1 
ATOM   205  O OE2   . GLU A 1 47  ? -2.021  -1.134  -33.621 1.00 23.34 ? 27  GLU A OE2   1 
ATOM   206  N N     . ASP A 1 48  ? 3.537   1.191   -36.446 1.00 6.07  ? 28  ASP A N     1 
ATOM   207  C CA    . ASP A 1 48  ? 4.559   2.217   -36.307 1.00 6.35  ? 28  ASP A CA    1 
ATOM   208  C C     . ASP A 1 48  ? 5.954   1.639   -36.538 1.00 5.35  ? 28  ASP A C     1 
ATOM   209  O O     . ASP A 1 48  ? 6.912   1.969   -35.808 1.00 5.81  ? 28  ASP A O     1 
ATOM   210  C CB    . ASP A 1 48  ? 4.487   2.926   -34.954 1.00 8.25  ? 28  ASP A CB    1 
ATOM   211  C CG    . ASP A 1 48  ? 3.230   3.751   -34.811 1.00 11.13 ? 28  ASP A CG    1 
ATOM   212  O OD1   . ASP A 1 48  ? 2.634   4.075   -35.854 1.00 13.79 ? 28  ASP A OD1   1 
ATOM   213  O OD2   . ASP A 1 48  ? 2.833   4.004   -33.661 1.00 13.14 ? 28  ASP A OD2   1 
ATOM   214  N N     . GLY A 1 49  ? 6.062   0.801   -37.560 1.00 4.52  ? 29  GLY A N     1 
ATOM   215  C CA    . GLY A 1 49  ? 7.328   0.304   -38.066 1.00 4.37  ? 29  GLY A CA    1 
ATOM   216  C C     . GLY A 1 49  ? 7.922   -0.888  -37.323 1.00 3.82  ? 29  GLY A C     1 
ATOM   217  O O     . GLY A 1 49  ? 9.006   -1.317  -37.656 1.00 4.07  ? 29  GLY A O     1 
ATOM   218  N N     . ARG A 1 50  ? 7.230   -1.454  -36.345 1.00 3.10  ? 30  ARG A N     1 
ATOM   219  C CA    . ARG A 1 50  ? 7.805   -2.556  -35.601 1.00 2.80  ? 30  ARG A CA    1 
ATOM   220  C C     . ARG A 1 50  ? 8.088   -3.728  -36.519 1.00 3.05  ? 30  ARG A C     1 
ATOM   221  O O     . ARG A 1 50  ? 7.242   -4.098  -37.343 1.00 3.47  ? 30  ARG A O     1 
ATOM   222  C CB    . ARG A 1 50  ? 6.874   -3.007  -34.467 1.00 2.40  ? 30  ARG A CB    1 
ATOM   223  C CG    . ARG A 1 50  ? 7.475   -4.076  -33.571 1.00 2.23  ? 30  ARG A CG    1 
ATOM   224  C CD    . ARG A 1 50  ? 6.601   -4.467  -32.375 1.00 2.16  ? 30  ARG A CD    1 
ATOM   225  N NE    . ARG A 1 50  ? 7.089   -5.585  -31.622 1.00 2.12  ? 30  ARG A NE    1 
ATOM   226  C CZ    . ARG A 1 50  ? 6.957   -6.849  -31.985 1.00 2.36  ? 30  ARG A CZ    1 
ATOM   227  N NH1   . ARG A 1 50  ? 6.294   -7.179  -33.069 1.00 2.43  ? 30  ARG A NH1   1 
ATOM   228  N NH2   . ARG A 1 50  ? 7.466   -7.783  -31.200 1.00 2.54  ? 30  ARG A NH2   1 
ATOM   229  N N     . GLY A 1 51  ? 9.265   -4.330  -36.322 1.00 2.92  ? 31  GLY A N     1 
ATOM   230  C CA    . GLY A 1 51  ? 9.625   -5.525  -37.065 1.00 3.11  ? 31  GLY A CA    1 
ATOM   231  C C     . GLY A 1 51  ? 9.048   -6.804  -36.481 1.00 3.61  ? 31  GLY A C     1 
ATOM   232  O O     . GLY A 1 51  ? 8.263   -6.739  -35.555 1.00 5.13  ? 31  GLY A O     1 
ATOM   233  N N     . VAL A 1 52  ? 9.496   -7.939  -36.968 1.00 3.65  ? 32  VAL A N     1 
ATOM   234  C CA    . VAL A 1 52  ? 9.089   -9.228  -36.473 1.00 3.42  ? 32  VAL A CA    1 
ATOM   235  C C     . VAL A 1 52  ? 10.128  -9.736  -35.473 1.00 3.03  ? 32  VAL A C     1 
ATOM   236  O O     . VAL A 1 52  ? 11.318  -9.706  -35.740 1.00 3.07  ? 32  VAL A O     1 
ATOM   237  C CB    . VAL A 1 52  ? 8.936   -10.207 -37.629 1.00 3.85  ? 32  VAL A CB    1 
ATOM   238  C CG1   . VAL A 1 52  ? 8.519   -11.579 -37.148 1.00 4.04  ? 32  VAL A CG1   1 
ATOM   239  C CG2   . VAL A 1 52  ? 7.959   -9.656  -38.667 1.00 3.81  ? 32  VAL A CG2   1 
ATOM   240  N N     . SER A 1 53  ? 9.678   -10.167 -34.288 1.00 2.46  ? 33  SER A N     1 
ATOM   241  C CA    . SER A 1 53  ? 10.544  -10.755 -33.292 1.00 2.27  ? 33  SER A CA    1 
ATOM   242  C C     . SER A 1 53  ? 10.446  -12.276 -33.353 1.00 1.97  ? 33  SER A C     1 
ATOM   243  O O     . SER A 1 53  ? 9.470   -12.851 -33.865 1.00 1.79  ? 33  SER A O     1 
ATOM   244  C CB    . SER A 1 53  ? 10.244  -10.263 -31.880 1.00 2.42  ? 33  SER A CB    1 
ATOM   245  O OG    . SER A 1 53  ? 9.205   -11.013 -31.291 1.00 2.68  ? 33  SER A OG    1 
ATOM   246  N N     . ILE A 1 54  ? 11.400  -12.942 -32.697 1.00 1.79  ? 34  ILE A N     1 
ATOM   247  C CA    . ILE A 1 54  ? 11.318  -14.389 -32.542 1.00 1.75  ? 34  ILE A CA    1 
ATOM   248  C C     . ILE A 1 54  ? 10.045  -14.805 -31.844 1.00 1.83  ? 34  ILE A C     1 
ATOM   249  O O     . ILE A 1 54  ? 9.626   -15.952 -32.031 1.00 1.92  ? 34  ILE A O     1 
ATOM   250  C CB    . ILE A 1 54  ? 12.554  -14.944 -31.823 1.00 1.68  ? 34  ILE A CB    1 
ATOM   251  C CG1   . ILE A 1 54  ? 12.787  -14.369 -30.425 1.00 1.68  ? 34  ILE A CG1   1 
ATOM   252  C CG2   . ILE A 1 54  ? 13.778  -14.782 -32.728 1.00 1.67  ? 34  ILE A CG2   1 
ATOM   253  C CD1   . ILE A 1 54  ? 13.942  -15.058 -29.713 1.00 1.70  ? 34  ILE A CD1   1 
ATOM   254  N N     . TRP A 1 55  ? 9.499   -13.977 -30.970 1.00 1.78  ? 35  TRP A N     1 
ATOM   255  C CA    . TRP A 1 55  ? 8.280   -14.322 -30.247 1.00 1.96  ? 35  TRP A CA    1 
ATOM   256  C C     . TRP A 1 55  ? 7.027   -14.152 -31.094 1.00 2.17  ? 35  TRP A C     1 
ATOM   257  O O     . TRP A 1 55  ? 6.030   -14.848 -30.855 1.00 2.59  ? 35  TRP A O     1 
ATOM   258  C CB    . TRP A 1 55  ? 8.202   -13.580 -28.904 1.00 1.89  ? 35  TRP A CB    1 
ATOM   259  C CG    . TRP A 1 55  ? 8.849   -14.359 -27.808 1.00 1.87  ? 35  TRP A CG    1 
ATOM   260  C CD1   . TRP A 1 55  ? 10.105  -14.212 -27.302 1.00 1.85  ? 35  TRP A CD1   1 
ATOM   261  C CD2   . TRP A 1 55  ? 8.282   -15.513 -27.156 1.00 1.85  ? 35  TRP A CD2   1 
ATOM   262  N NE1   . TRP A 1 55  ? 10.364  -15.183 -26.396 1.00 1.97  ? 35  TRP A NE1   1 
ATOM   263  C CE2   . TRP A 1 55  ? 9.253   -15.987 -26.232 1.00 1.89  ? 35  TRP A CE2   1 
ATOM   264  C CE3   . TRP A 1 55  ? 7.022   -16.147 -27.227 1.00 1.79  ? 35  TRP A CE3   1 
ATOM   265  C CZ2   . TRP A 1 55  ? 9.015   -17.077 -25.397 1.00 1.88  ? 35  TRP A CZ2   1 
ATOM   266  C CZ3   . TRP A 1 55  ? 6.803   -17.199 -26.358 1.00 1.75  ? 35  TRP A CZ3   1 
ATOM   267  C CH2   . TRP A 1 55  ? 7.804   -17.705 -25.527 1.00 1.85  ? 35  TRP A CH2   1 
ATOM   268  N N     . ASP A 1 56  ? 7.062   -13.264 -32.082 1.00 2.29  ? 36  ASP A N     1 
ATOM   269  C CA    . ASP A 1 56  ? 6.020   -13.252 -33.110 1.00 2.61  ? 36  ASP A CA    1 
ATOM   270  C C     . ASP A 1 56  ? 6.048   -14.569 -33.863 1.00 2.65  ? 36  ASP A C     1 
ATOM   271  O O     . ASP A 1 56  ? 5.010   -15.232 -34.005 1.00 2.92  ? 36  ASP A O     1 
ATOM   272  C CB    . ASP A 1 56  ? 6.165   -12.081 -34.082 1.00 2.88  ? 36  ASP A CB    1 
ATOM   273  C CG    . ASP A 1 56  ? 6.119   -10.732 -33.410 1.00 3.20  ? 36  ASP A CG    1 
ATOM   274  O OD1   . ASP A 1 56  ? 7.184   -10.261 -32.857 1.00 3.50  ? 36  ASP A OD1   1 
ATOM   275  O OD2   . ASP A 1 56  ? 5.017   -10.105 -33.396 1.00 3.71  ? 36  ASP A OD2   1 
ATOM   276  N N     . THR A 1 57  ? 7.220   -14.978 -34.334 1.00 2.58  ? 37  THR A N     1 
ATOM   277  C CA    . THR A 1 57  ? 7.372   -16.210 -35.106 1.00 2.73  ? 37  THR A CA    1 
ATOM   278  C C     . THR A 1 57  ? 6.885   -17.392 -34.271 1.00 2.56  ? 37  THR A C     1 
ATOM   279  O O     . THR A 1 57  ? 6.104   -18.249 -34.724 1.00 3.04  ? 37  THR A O     1 
ATOM   280  C CB    . THR A 1 57  ? 8.841   -16.384 -35.480 1.00 2.97  ? 37  THR A CB    1 
ATOM   281  O OG1   . THR A 1 57  ? 9.209   -15.222 -36.250 1.00 3.74  ? 37  THR A OG1   1 
ATOM   282  C CG2   . THR A 1 57  ? 9.104   -17.651 -36.268 1.00 3.09  ? 37  THR A CG2   1 
ATOM   283  N N     . PHE A 1 58  ? 7.370   -17.467 -33.028 1.00 2.38  ? 38  PHE A N     1 
ATOM   284  C CA    . PHE A 1 58  ? 7.122   -18.603 -32.176 1.00 2.48  ? 38  PHE A CA    1 
ATOM   285  C C     . PHE A 1 58  ? 5.659   -18.661 -31.760 1.00 2.67  ? 38  PHE A C     1 
ATOM   286  O O     . PHE A 1 58  ? 5.038   -19.726 -31.830 1.00 2.60  ? 38  PHE A O     1 
ATOM   287  C CB    . PHE A 1 58  ? 8.026   -18.512 -30.941 1.00 2.41  ? 38  PHE A CB    1 
ATOM   288  C CG    . PHE A 1 58  ? 8.108   -19.718 -30.047 1.00 2.44  ? 38  PHE A CG    1 
ATOM   289  C CD1   . PHE A 1 58  ? 8.805   -20.851 -30.414 1.00 2.42  ? 38  PHE A CD1   1 
ATOM   290  C CD2   . PHE A 1 58  ? 7.529   -19.699 -28.795 1.00 2.50  ? 38  PHE A CD2   1 
ATOM   291  C CE1   . PHE A 1 58  ? 8.947   -21.916 -29.540 1.00 2.54  ? 38  PHE A CE1   1 
ATOM   292  C CE2   . PHE A 1 58  ? 7.680   -20.781 -27.947 1.00 2.53  ? 38  PHE A CE2   1 
ATOM   293  C CZ    . PHE A 1 58  ? 8.417   -21.838 -28.311 1.00 2.57  ? 38  PHE A CZ    1 
ATOM   294  N N     . SER A 1 59  ? 5.044   -17.555 -31.375 1.00 2.91  ? 39  SER A N     1 
ATOM   295  C CA    . SER A 1 59  ? 3.666   -17.655 -30.930 1.00 3.36  ? 39  SER A CA    1 
ATOM   296  C C     . SER A 1 59  ? 2.708   -17.936 -32.095 1.00 3.67  ? 39  SER A C     1 
ATOM   297  O O     . SER A 1 59  ? 1.610   -18.452 -31.857 1.00 5.15  ? 39  SER A O     1 
ATOM   298  C CB    . SER A 1 59  ? 3.308   -16.401 -30.141 1.00 3.96  ? 39  SER A CB    1 
ATOM   299  O OG    . SER A 1 59  ? 3.100   -15.311 -30.961 1.00 4.72  ? 39  SER A OG    1 
ATOM   300  N N     . HIS A 1 60  ? 3.109   -17.613 -33.337 1.00 3.75  ? 40  HIS A N     1 
ATOM   301  C CA    . HIS A 1 60  ? 2.317   -17.908 -34.522 1.00 4.20  ? 40  HIS A CA    1 
ATOM   302  C C     . HIS A 1 60  ? 2.652   -19.291 -35.055 1.00 4.38  ? 40  HIS A C     1 
ATOM   303  O O     . HIS A 1 60  ? 2.174   -19.611 -36.135 1.00 6.44  ? 40  HIS A O     1 
ATOM   304  C CB    . HIS A 1 60  ? 2.490   -16.814 -35.570 1.00 4.61  ? 40  HIS A CB    1 
ATOM   305  C CG    . HIS A 1 60  ? 1.702   -15.623 -35.182 1.00 5.30  ? 40  HIS A CG    1 
ATOM   306  N ND1   . HIS A 1 60  ? 0.383   -15.461 -35.569 1.00 7.92  ? 40  HIS A ND1   1 
ATOM   307  C CD2   . HIS A 1 60  ? 1.997   -14.568 -34.406 1.00 5.61  ? 40  HIS A CD2   1 
ATOM   308  C CE1   . HIS A 1 60  ? -0.052  -14.293 -35.079 1.00 7.62  ? 40  HIS A CE1   1 
ATOM   309  N NE2   . HIS A 1 60  ? 0.925   -13.732 -34.373 1.00 6.11  ? 40  HIS A NE2   1 
ATOM   310  N N     . THR A 1 61  ? 3.467   -20.078 -34.375 1.00 3.75  ? 41  THR A N     1 
ATOM   311  C CA    . THR A 1 61  ? 3.793   -21.436 -34.763 1.00 3.81  ? 41  THR A CA    1 
ATOM   312  C C     . THR A 1 61  ? 2.781   -22.345 -34.055 1.00 3.97  ? 41  THR A C     1 
ATOM   313  O O     . THR A 1 61  ? 2.770   -22.415 -32.808 1.00 3.68  ? 41  THR A O     1 
ATOM   314  C CB    . THR A 1 61  ? 5.216   -21.839 -34.400 1.00 3.84  ? 41  THR A CB    1 
ATOM   315  O OG1   . THR A 1 61  ? 6.092   -20.930 -35.078 1.00 4.17  ? 41  THR A OG1   1 
ATOM   316  C CG2   . THR A 1 61  ? 5.538   -23.259 -34.833 1.00 3.94  ? 41  THR A CG2   1 
ATOM   317  N N     . PRO A 1 62  ? 1.990   -23.173 -34.794 1.00 4.35  ? 42  PRO A N     1 
ATOM   318  C CA    . PRO A 1 62  ? 1.057   -24.077 -34.144 1.00 4.62  ? 42  PRO A CA    1 
ATOM   319  C C     . PRO A 1 62  ? 1.657   -24.929 -33.049 1.00 4.21  ? 42  PRO A C     1 
ATOM   320  O O     . PRO A 1 62  ? 2.695   -25.571 -33.269 1.00 5.23  ? 42  PRO A O     1 
ATOM   321  C CB    . PRO A 1 62  ? 0.616   -24.926 -35.346 1.00 4.93  ? 42  PRO A CB    1 
ATOM   322  C CG    . PRO A 1 62  ? 0.487   -23.911 -36.446 1.00 5.31  ? 42  PRO A CG    1 
ATOM   323  C CD    . PRO A 1 62  ? 1.774   -23.126 -36.268 1.00 4.84  ? 42  PRO A CD    1 
ATOM   324  N N     . GLY A 1 63  ? 0.979   -24.936 -31.896 1.00 4.21  ? 43  GLY A N     1 
ATOM   325  C CA    . GLY A 1 63  ? 1.375   -25.827 -30.840 1.00 4.22  ? 43  GLY A CA    1 
ATOM   326  C C     . GLY A 1 63  ? 2.339   -25.264 -29.815 1.00 4.01  ? 43  GLY A C     1 
ATOM   327  O O     . GLY A 1 63  ? 2.531   -25.887 -28.786 1.00 4.95  ? 43  GLY A O     1 
ATOM   328  N N     . LYS A 1 64  ? 3.017   -24.137 -30.114 1.00 3.53  ? 44  LYS A N     1 
ATOM   329  C CA    . LYS A 1 64  ? 4.016   -23.638 -29.193 1.00 3.43  ? 44  LYS A CA    1 
ATOM   330  C C     . LYS A 1 64  ? 3.404   -23.001 -27.957 1.00 3.18  ? 44  LYS A C     1 
ATOM   331  O O     . LYS A 1 64  ? 4.057   -23.049 -26.934 1.00 3.51  ? 44  LYS A O     1 
ATOM   332  C CB    . LYS A 1 64  ? 4.952   -22.665 -29.928 1.00 3.63  ? 44  LYS A CB    1 
ATOM   333  C CG    . LYS A 1 64  ? 5.726   -23.308 -31.067 1.00 4.05  ? 44  LYS A CG    1 
ATOM   334  C CD    . LYS A 1 64  ? 6.576   -24.469 -30.650 1.00 4.53  ? 44  LYS A CD    1 
ATOM   335  C CE    . LYS A 1 64  ? 7.465   -24.961 -31.768 1.00 5.81  ? 44  LYS A CE    1 
ATOM   336  N NZ    . LYS A 1 64  ? 8.175   -26.183 -31.416 1.00 7.06  ? 44  LYS A NZ    1 
ATOM   337  N N     . ILE A 1 65  ? 2.236   -22.427 -28.070 1.00 2.89  ? 45  ILE A N     1 
ATOM   338  C CA    . ILE A 1 65  ? 1.613   -21.731 -26.943 1.00 2.94  ? 45  ILE A CA    1 
ATOM   339  C C     . ILE A 1 65  ? 0.462   -22.605 -26.440 1.00 3.13  ? 45  ILE A C     1 
ATOM   340  O O     . ILE A 1 65  ? -0.342  -23.080 -27.248 1.00 4.01  ? 45  ILE A O     1 
ATOM   341  C CB    . ILE A 1 65  ? 1.118   -20.320 -27.348 1.00 2.83  ? 45  ILE A CB    1 
ATOM   342  C CG1   . ILE A 1 65  ? 2.198   -19.492 -28.070 1.00 2.86  ? 45  ILE A CG1   1 
ATOM   343  C CG2   . ILE A 1 65  ? 0.584   -19.531 -26.171 1.00 3.00  ? 45  ILE A CG2   1 
ATOM   344  C CD1   . ILE A 1 65  ? 3.516   -19.282 -27.313 1.00 2.76  ? 45  ILE A CD1   1 
ATOM   345  N N     . ALA A 1 66  ? 0.306   -22.722 -25.128 1.00 3.01  ? 46  ALA A N     1 
ATOM   346  C CA    . ALA A 1 66  ? -0.619  -23.712 -24.581 1.00 3.21  ? 46  ALA A CA    1 
ATOM   347  C C     . ALA A 1 66  ? -2.051  -23.518 -25.055 1.00 3.33  ? 46  ALA A C     1 
ATOM   348  O O     . ALA A 1 66  ? -2.844  -24.460 -25.113 1.00 3.54  ? 46  ALA A O     1 
ATOM   349  C CB    . ALA A 1 66  ? -0.552  -23.626 -23.091 1.00 3.52  ? 46  ALA A CB    1 
ATOM   350  N N     . ASP A 1 67  ? -2.486  -22.274 -25.239 1.00 3.68  ? 47  ASP A N     1 
ATOM   351  C CA    . ASP A 1 67  ? -3.869  -21.913 -25.436 1.00 4.05  ? 47  ASP A CA    1 
ATOM   352  C C     . ASP A 1 67  ? -4.130  -21.219 -26.763 1.00 4.64  ? 47  ASP A C     1 
ATOM   353  O O     . ASP A 1 67  ? -5.178  -20.593 -26.938 1.00 5.17  ? 47  ASP A O     1 
ATOM   354  C CB    . ASP A 1 67  ? -4.308  -21.045 -24.261 1.00 3.80  ? 47  ASP A CB    1 
ATOM   355  C CG    . ASP A 1 67  ? -3.578  -19.713 -24.184 1.00 4.06  ? 47  ASP A CG    1 
ATOM   356  O OD1   . ASP A 1 67  ? -2.698  -19.502 -25.055 1.00 3.47  ? 47  ASP A OD1   1 
ATOM   357  O OD2   . ASP A 1 67  ? -3.968  -18.907 -23.297 1.00 5.10  ? 47  ASP A OD2   1 
ATOM   358  N N     . GLY A 1 68  ? -3.181  -21.319 -27.702 1.00 5.24  ? 48  GLY A N     1 
ATOM   359  C CA    . GLY A 1 68  ? -3.415  -20.759 -29.023 1.00 6.18  ? 48  GLY A CA    1 
ATOM   360  C C     . GLY A 1 68  ? -3.403  -19.225 -29.062 1.00 6.89  ? 48  GLY A C     1 
ATOM   361  O O     . GLY A 1 68  ? -3.811  -18.644 -30.068 1.00 10.14 ? 48  GLY A O     1 
ATOM   362  N N     . THR A 1 69  ? -2.910  -18.561 -28.009 1.00 5.07  ? 49  THR A N     1 
ATOM   363  C CA    . THR A 1 69  ? -2.875  -17.123 -28.003 1.00 4.43  ? 49  THR A CA    1 
ATOM   364  C C     . THR A 1 69  ? -1.514  -16.662 -28.516 1.00 3.62  ? 49  THR A C     1 
ATOM   365  O O     . THR A 1 69  ? -0.575  -17.437 -28.663 1.00 3.50  ? 49  THR A O     1 
ATOM   366  C CB    . THR A 1 69  ? -3.195  -16.548 -26.620 1.00 3.98  ? 49  THR A CB    1 
ATOM   367  O OG1   . THR A 1 69  ? -2.215  -16.978 -25.674 1.00 3.68  ? 49  THR A OG1   1 
ATOM   368  C CG2   . THR A 1 69  ? -4.600  -16.912 -26.182 1.00 3.98  ? 49  THR A CG2   1 
ATOM   369  N N     . THR A 1 70  ? -1.468  -15.342 -28.782 1.00 3.80  ? 50  THR A N     1 
ATOM   370  C CA    . THR A 1 70  ? -0.261  -14.659 -29.205 1.00 3.79  ? 50  THR A CA    1 
ATOM   371  C C     . THR A 1 70  ? -0.165  -13.350 -28.466 1.00 3.49  ? 50  THR A C     1 
ATOM   372  O O     . THR A 1 70  ? -1.092  -12.935 -27.788 1.00 3.72  ? 50  THR A O     1 
ATOM   373  C CB    . THR A 1 70  ? -0.205  -14.371 -30.710 1.00 3.92  ? 50  THR A CB    1 
ATOM   374  O OG1   . THR A 1 70  ? -1.100  -13.312 -31.022 1.00 4.31  ? 50  THR A OG1   1 
ATOM   375  C CG2   . THR A 1 70  ? -0.610  -15.588 -31.516 1.00 4.51  ? 50  THR A CG2   1 
ATOM   376  N N     . GLY A 1 71  ? 0.982   -12.665 -28.670 1.00 2.98  ? 51  GLY A N     1 
ATOM   377  C CA    . GLY A 1 71  ? 1.144   -11.308 -28.210 1.00 2.93  ? 51  GLY A CA    1 
ATOM   378  C C     . GLY A 1 71  ? 0.610   -10.235 -29.144 1.00 2.78  ? 51  GLY A C     1 
ATOM   379  O O     . GLY A 1 71  ? 0.956   -9.068  -28.991 1.00 2.55  ? 51  GLY A O     1 
ATOM   380  N N     . ASP A 1 72  ? -0.212  -10.612 -30.140 1.00 2.89  ? 52  ASP A N     1 
ATOM   381  C CA    . ASP A 1 72  ? -0.631  -9.621  -31.106 1.00 3.34  ? 52  ASP A CA    1 
ATOM   382  C C     . ASP A 1 72  ? -1.338  -8.407  -30.505 1.00 3.37  ? 52  ASP A C     1 
ATOM   383  O O     . ASP A 1 72  ? -1.090  -7.287  -30.985 1.00 3.40  ? 52  ASP A O     1 
ATOM   384  C CB    . ASP A 1 72  ? -1.500  -10.219 -32.211 1.00 3.85  ? 52  ASP A CB    1 
ATOM   385  C CG    . ASP A 1 72  ? -0.797  -11.087 -33.233 1.00 4.84  ? 52  ASP A CG    1 
ATOM   386  O OD1   . ASP A 1 72  ? 0.399   -11.345 -33.109 1.00 5.48  ? 52  ASP A OD1   1 
ATOM   387  O OD2   . ASP A 1 72  ? -1.542  -11.596 -34.147 1.00 8.23  ? 52  ASP A OD2   1 
ATOM   388  N N     . VAL A 1 73  ? -2.180  -8.646  -29.512 1.00 3.54  ? 53  VAL A N     1 
ATOM   389  C CA    . VAL A 1 73  ? -2.843  -7.584  -28.782 1.00 3.77  ? 53  VAL A CA    1 
ATOM   390  C C     . VAL A 1 73  ? -2.344  -7.493  -27.330 1.00 3.43  ? 53  VAL A C     1 
ATOM   391  O O     . VAL A 1 73  ? -2.028  -6.398  -26.832 1.00 3.35  ? 53  VAL A O     1 
ATOM   392  C CB    . VAL A 1 73  ? -4.362  -7.763  -28.831 1.00 4.57  ? 53  VAL A CB    1 
ATOM   393  C CG1   . VAL A 1 73  ? -5.023  -6.719  -27.955 1.00 4.77  ? 53  VAL A CG1   1 
ATOM   394  C CG2   . VAL A 1 73  ? -4.823  -7.635  -30.279 1.00 5.14  ? 53  VAL A CG2   1 
ATOM   395  N N     . ALA A 1 74  ? -2.297  -8.622  -26.633 1.00 3.10  ? 54  ALA A N     1 
ATOM   396  C CA    . ALA A 1 74  ? -1.805  -8.722  -25.254 1.00 3.20  ? 54  ALA A CA    1 
ATOM   397  C C     . ALA A 1 74  ? -2.627  -7.757  -24.422 1.00 3.19  ? 54  ALA A C     1 
ATOM   398  O O     . ALA A 1 74  ? -3.851  -7.854  -24.436 1.00 3.94  ? 54  ALA A O     1 
ATOM   399  C CB    . ALA A 1 74  ? -0.322  -8.492  -25.223 1.00 3.42  ? 54  ALA A CB    1 
ATOM   400  N N     . CYS A 1 75  ? -2.001  -6.811  -23.723 1.00 2.79  ? 55  CYS A N     1 
ATOM   401  C CA    . CYS A 1 75  ? -2.732  -5.845  -22.905 1.00 2.86  ? 55  CYS A CA    1 
ATOM   402  C C     . CYS A 1 75  ? -2.971  -4.554  -23.663 1.00 2.82  ? 55  CYS A C     1 
ATOM   403  O O     . CYS A 1 75  ? -3.441  -3.580  -23.102 1.00 2.50  ? 55  CYS A O     1 
ATOM   404  C CB    . CYS A 1 75  ? -1.956  -5.543  -21.620 1.00 3.10  ? 55  CYS A CB    1 
ATOM   405  S SG    . CYS A 1 75  ? -1.533  -7.075  -20.735 1.00 3.99  ? 55  CYS A SG    1 
ATOM   406  N N     . ASP A 1 76  ? -2.504  -4.481  -24.913 1.00 2.70  ? 56  ASP A N     1 
ATOM   407  C CA    . ASP A 1 76  ? -2.584  -3.306  -25.745 1.00 3.18  ? 56  ASP A CA    1 
ATOM   408  C C     . ASP A 1 76  ? -1.895  -2.137  -25.065 1.00 2.78  ? 56  ASP A C     1 
ATOM   409  O O     . ASP A 1 76  ? -2.301  -0.984  -25.254 1.00 2.66  ? 56  ASP A O     1 
ATOM   410  C CB    . ASP A 1 76  ? -4.036  -2.933  -26.036 1.00 4.00  ? 56  ASP A CB    1 
ATOM   411  C CG    . ASP A 1 76  ? -4.267  -2.026  -27.223 1.00 5.58  ? 56  ASP A CG    1 
ATOM   412  O OD1   . ASP A 1 76  ? -3.467  -2.002  -28.174 1.00 7.01  ? 56  ASP A OD1   1 
ATOM   413  O OD2   . ASP A 1 76  ? -5.224  -1.212  -27.102 1.00 7.53  ? 56  ASP A OD2   1 
ATOM   414  N N     . SER A 1 77  ? -0.766  -2.389  -24.359 1.00 2.48  ? 57  SER A N     1 
ATOM   415  C CA    . SER A 1 77  ? -0.079  -1.319  -23.640 1.00 2.54  ? 57  SER A CA    1 
ATOM   416  C C     . SER A 1 77  ? 0.647   -0.343  -24.549 1.00 2.58  ? 57  SER A C     1 
ATOM   417  O O     . SER A 1 77  ? 1.012   0.731   -24.099 1.00 2.21  ? 57  SER A O     1 
ATOM   418  C CB    . SER A 1 77  ? 0.799   -1.844  -22.530 1.00 2.63  ? 57  SER A CB    1 
ATOM   419  O OG    . SER A 1 77  ? 0.025   -2.502  -21.535 1.00 3.24  ? 57  SER A OG    1 
ATOM   420  N N     . TYR A 1 78  ? 0.923   -0.708  -25.806 1.00 2.51  ? 58  TYR A N     1 
ATOM   421  C CA    . TYR A 1 78  ? 1.491   0.265   -26.717 1.00 3.01  ? 58  TYR A CA    1 
ATOM   422  C C     . TYR A 1 78  ? 0.582   1.495   -26.766 1.00 3.07  ? 58  TYR A C     1 
ATOM   423  O O     . TYR A 1 78  ? 1.030   2.609   -26.764 1.00 2.91  ? 58  TYR A O     1 
ATOM   424  C CB    . TYR A 1 78  ? 1.722   -0.375  -28.093 1.00 3.30  ? 58  TYR A CB    1 
ATOM   425  C CG    . TYR A 1 78  ? 2.429   0.545   -29.046 1.00 3.84  ? 58  TYR A CG    1 
ATOM   426  C CD1   . TYR A 1 78  ? 3.783   0.787   -28.943 1.00 4.17  ? 58  TYR A CD1   1 
ATOM   427  C CD2   . TYR A 1 78  ? 1.707   1.236   -30.016 1.00 4.25  ? 58  TYR A CD2   1 
ATOM   428  C CE1   . TYR A 1 78  ? 4.427   1.632   -29.837 1.00 4.96  ? 58  TYR A CE1   1 
ATOM   429  C CE2   . TYR A 1 78  ? 2.323   2.087   -30.903 1.00 5.18  ? 58  TYR A CE2   1 
ATOM   430  C CZ    . TYR A 1 78  ? 3.664   2.292   -30.786 1.00 5.46  ? 58  TYR A CZ    1 
ATOM   431  O OH    . TYR A 1 78  ? 4.322   3.160   -31.668 1.00 8.86  ? 58  TYR A OH    1 
ATOM   432  N N     . HIS A 1 79  ? -0.726  1.250   -26.825 1.00 3.43  ? 59  HIS A N     1 
ATOM   433  C CA    . HIS A 1 79  ? -1.729  2.300   -26.849 1.00 4.13  ? 59  HIS A CA    1 
ATOM   434  C C     . HIS A 1 79  ? -2.194  2.708   -25.474 1.00 4.05  ? 59  HIS A C     1 
ATOM   435  O O     . HIS A 1 79  ? -2.672  3.848   -25.350 1.00 4.74  ? 59  HIS A O     1 
ATOM   436  C CB    . HIS A 1 79  ? -2.908  1.878   -27.721 1.00 5.14  ? 59  HIS A CB    1 
ATOM   437  C CG    . HIS A 1 79  ? -2.543  1.729   -29.178 1.00 7.19  ? 59  HIS A CG    1 
ATOM   438  N ND1   . HIS A 1 79  ? -1.986  2.784   -29.877 1.00 10.53 ? 59  HIS A ND1   1 
ATOM   439  C CD2   . HIS A 1 79  ? -2.543  0.679   -29.981 1.00 10.55 ? 59  HIS A CD2   1 
ATOM   440  C CE1   . HIS A 1 79  ? -1.725  2.356   -31.110 1.00 11.15 ? 59  HIS A CE1   1 
ATOM   441  N NE2   . HIS A 1 79  ? -2.078  1.133   -31.204 1.00 10.05 ? 59  HIS A NE2   1 
ATOM   442  N N     . ARG A 1 80  ? -2.119  1.806   -24.492 1.00 3.50  ? 60  ARG A N     1 
ATOM   443  C CA    . ARG A 1 80  ? -2.816  2.012   -23.232 1.00 3.56  ? 60  ARG A CA    1 
ATOM   444  C C     . ARG A 1 80  ? -1.819  2.160   -22.087 1.00 3.00  ? 60  ARG A C     1 
ATOM   445  O O     . ARG A 1 80  ? -2.162  2.010   -20.930 1.00 2.96  ? 60  ARG A O     1 
ATOM   446  C CB    . ARG A 1 80  ? -3.799  0.873   -22.933 1.00 4.57  ? 60  ARG A CB    1 
ATOM   447  C CG    . ARG A 1 80  ? -4.863  0.764   -24.004 1.00 5.32  ? 60  ARG A CG    1 
ATOM   448  C CD    . ARG A 1 80  ? -5.845  -0.320  -23.614 1.00 6.80  ? 60  ARG A CD    1 
ATOM   449  N NE    . ARG A 1 80  ? -6.733  -0.590  -24.717 1.00 9.33  ? 60  ARG A NE    1 
ATOM   450  C CZ    . ARG A 1 80  ? -8.032  -0.342  -24.715 1.00 13.40 ? 60  ARG A CZ    1 
ATOM   451  N NH1   . ARG A 1 80  ? -8.576  0.125   -23.620 1.00 14.77 ? 60  ARG A NH1   1 
ATOM   452  N NH2   . ARG A 1 80  ? -8.714  -0.557  -25.811 1.00 15.12 ? 60  ARG A NH2   1 
ATOM   453  N N     . TYR A 1 81  ? -0.587  2.547   -22.394 1.00 2.60  ? 61  TYR A N     1 
ATOM   454  C CA    . TYR A 1 81  ? 0.388   2.693   -21.316 1.00 2.51  ? 61  TYR A CA    1 
ATOM   455  C C     . TYR A 1 81  ? -0.031  3.763   -20.295 1.00 2.45  ? 61  TYR A C     1 
ATOM   456  O O     . TYR A 1 81  ? 0.420   3.747   -19.159 1.00 2.49  ? 61  TYR A O     1 
ATOM   457  C CB    . TYR A 1 81  ? 1.814   2.975   -21.806 1.00 2.65  ? 61  TYR A CB    1 
ATOM   458  C CG    . TYR A 1 81  ? 2.016   4.285   -22.513 1.00 2.77  ? 61  TYR A CG    1 
ATOM   459  C CD1   . TYR A 1 81  ? 2.265   5.460   -21.810 1.00 2.85  ? 61  TYR A CD1   1 
ATOM   460  C CD2   . TYR A 1 81  ? 1.936   4.369   -23.892 1.00 3.17  ? 61  TYR A CD2   1 
ATOM   461  C CE1   . TYR A 1 81  ? 2.472   6.665   -22.448 1.00 3.05  ? 61  TYR A CE1   1 
ATOM   462  C CE2   . TYR A 1 81  ? 2.073   5.580   -24.553 1.00 3.35  ? 61  TYR A CE2   1 
ATOM   463  C CZ    . TYR A 1 81  ? 2.371   6.724   -23.825 1.00 3.56  ? 61  TYR A CZ    1 
ATOM   464  O OH    . TYR A 1 81  ? 2.502   7.898   -24.535 1.00 4.80  ? 61  TYR A OH    1 
ATOM   465  N N     . GLY A 1 82  ? -0.839  4.750   -20.726 1.00 2.44  ? 62  GLY A N     1 
ATOM   466  C CA    . GLY A 1 82  ? -1.354  5.732   -19.803 1.00 2.48  ? 62  GLY A CA    1 
ATOM   467  C C     . GLY A 1 82  ? -2.235  5.109   -18.735 1.00 2.69  ? 62  GLY A C     1 
ATOM   468  O O     . GLY A 1 82  ? -2.226  5.564   -17.583 1.00 2.70  ? 62  GLY A O     1 
ATOM   469  N N     . GLU A 1 83  ? -3.004  4.085   -19.121 1.00 3.07  ? 63  GLU A N     1 
ATOM   470  C CA    . GLU A 1 83  ? -3.781  3.349   -18.144 1.00 3.85  ? 63  GLU A CA    1 
ATOM   471  C C     . GLU A 1 83  ? -2.855  2.625   -17.183 1.00 3.34  ? 63  GLU A C     1 
ATOM   472  O O     . GLU A 1 83  ? -3.115  2.597   -15.977 1.00 3.44  ? 63  GLU A O     1 
ATOM   473  C CB    . GLU A 1 83  ? -4.733  2.362   -18.800 1.00 5.35  ? 63  GLU A CB    1 
ATOM   474  C CG    . GLU A 1 83  ? -5.744  2.997   -19.721 1.00 7.25  ? 63  GLU A CG    1 
ATOM   475  C CD    . GLU A 1 83  ? -6.680  2.009   -20.364 1.00 10.73 ? 63  GLU A CD    1 
ATOM   476  O OE1   . GLU A 1 83  ? -7.069  1.058   -19.664 1.00 15.03 ? 63  GLU A OE1   1 
ATOM   477  O OE2   . GLU A 1 83  ? -7.086  2.240   -21.544 1.00 15.84 ? 63  GLU A OE2   1 
ATOM   478  N N     . ASP A 1 84  ? -1.756  2.073   -17.693 1.00 2.81  ? 64  ASP A N     1 
ATOM   479  C CA    . ASP A 1 84  ? -0.802  1.394   -16.828 1.00 2.81  ? 64  ASP A CA    1 
ATOM   480  C C     . ASP A 1 84  ? -0.211  2.391   -15.840 1.00 2.52  ? 64  ASP A C     1 
ATOM   481  O O     . ASP A 1 84  ? 0.036   2.067   -14.693 1.00 2.53  ? 64  ASP A O     1 
ATOM   482  C CB    . ASP A 1 84  ? 0.258   0.734   -17.707 1.00 3.05  ? 64  ASP A CB    1 
ATOM   483  C CG    . ASP A 1 84  ? -0.259  -0.330  -18.667 1.00 3.59  ? 64  ASP A CG    1 
ATOM   484  O OD1   . ASP A 1 84  ? -1.432  -0.776  -18.467 1.00 4.36  ? 64  ASP A OD1   1 
ATOM   485  O OD2   . ASP A 1 84  ? 0.534   -0.717  -19.580 1.00 4.01  ? 64  ASP A OD2   1 
ATOM   486  N N     . ILE A 1 85  ? 0.126   3.606   -16.301 1.00 2.21  ? 65  ILE A N     1 
ATOM   487  C CA    . ILE A 1 85  ? 0.605   4.664   -15.405 1.00 2.21  ? 65  ILE A CA    1 
ATOM   488  C C     . ILE A 1 85  ? -0.448  4.971   -14.331 1.00 2.32  ? 65  ILE A C     1 
ATOM   489  O O     . ILE A 1 85  ? -0.112  5.166   -13.168 1.00 2.17  ? 65  ILE A O     1 
ATOM   490  C CB    . ILE A 1 85  ? 1.029   5.908   -16.222 1.00 2.30  ? 65  ILE A CB    1 
ATOM   491  C CG1   . ILE A 1 85  ? 2.263   5.594   -17.028 1.00 2.29  ? 65  ILE A CG1   1 
ATOM   492  C CG2   . ILE A 1 85  ? 1.228   7.107   -15.302 1.00 2.40  ? 65  ILE A CG2   1 
ATOM   493  C CD1   . ILE A 1 85  ? 2.703   6.709   -17.938 1.00 2.22  ? 65  ILE A CD1   1 
ATOM   494  N N     . GLY A 1 86  ? -1.711  5.006   -14.768 1.00 2.56  ? 66  GLY A N     1 
ATOM   495  C CA    . GLY A 1 86  ? -2.774  5.185   -13.787 1.00 2.77  ? 66  GLY A CA    1 
ATOM   496  C C     . GLY A 1 86  ? -2.733  4.120   -12.710 1.00 3.09  ? 66  GLY A C     1 
ATOM   497  O O     . GLY A 1 86  ? -2.972  4.451   -11.544 1.00 3.46  ? 66  GLY A O     1 
ATOM   498  N N     . LEU A 1 87  ? -2.524  2.859   -13.084 1.00 2.97  ? 67  LEU A N     1 
ATOM   499  C CA    . LEU A 1 87  ? -2.458  1.797   -12.089 1.00 3.18  ? 67  LEU A CA    1 
ATOM   500  C C     . LEU A 1 87  ? -1.265  2.004   -11.150 1.00 3.08  ? 67  LEU A C     1 
ATOM   501  O O     . LEU A 1 87  ? -1.363  1.871   -9.943  1.00 2.87  ? 67  LEU A O     1 
ATOM   502  C CB    . LEU A 1 87  ? -2.327  0.463   -12.817 1.00 3.81  ? 67  LEU A CB    1 
ATOM   503  C CG    . LEU A 1 87  ? -3.520  0.016   -13.637 1.00 4.62  ? 67  LEU A CG    1 
ATOM   504  C CD1   . LEU A 1 87  ? -3.181  -1.181  -14.472 1.00 5.24  ? 67  LEU A CD1   1 
ATOM   505  C CD2   . LEU A 1 87  ? -4.712  -0.244  -12.735 1.00 5.50  ? 67  LEU A CD2   1 
ATOM   506  N N     . LEU A 1 88  ? -0.085  2.307   -11.709 1.00 3.03  ? 68  LEU A N     1 
ATOM   507  C CA    . LEU A 1 88  ? 1.118   2.482   -10.919 1.00 3.14  ? 68  LEU A CA    1 
ATOM   508  C C     . LEU A 1 88  ? 0.924   3.614   -9.930  1.00 3.77  ? 68  LEU A C     1 
ATOM   509  O O     . LEU A 1 88  ? 1.322   3.521   -8.774  1.00 3.82  ? 68  LEU A O     1 
ATOM   510  C CB    . LEU A 1 88  ? 2.274   2.820   -11.858 1.00 2.86  ? 68  LEU A CB    1 
ATOM   511  C CG    . LEU A 1 88  ? 2.772   1.617   -12.659 1.00 2.78  ? 68  LEU A CG    1 
ATOM   512  C CD1   . LEU A 1 88  ? 3.449   2.086   -13.959 1.00 2.71  ? 68  LEU A CD1   1 
ATOM   513  C CD2   . LEU A 1 88  ? 3.691   0.725   -11.835 1.00 2.86  ? 68  LEU A CD2   1 
ATOM   514  N N     . ASN A 1 89  ? 0.260   4.702   -10.354 1.00 4.34  ? 69  ASN A N     1 
ATOM   515  C CA    . ASN A 1 89  ? -0.059  5.782   -9.458  1.00 5.40  ? 69  ASN A CA    1 
ATOM   516  C C     . ASN A 1 89  ? -1.050  5.363   -8.364  1.00 5.29  ? 69  ASN A C     1 
ATOM   517  O O     . ASN A 1 89  ? -0.834  5.723   -7.196  1.00 5.91  ? 69  ASN A O     1 
ATOM   518  C CB    . ASN A 1 89  ? -0.676  6.920   -10.273 1.00 6.77  ? 69  ASN A CB    1 
ATOM   519  C CG    . ASN A 1 89  ? -0.997  8.111   -9.403  1.00 9.42  ? 69  ASN A CG    1 
ATOM   520  O OD1   . ASN A 1 89  ? -0.097  8.669   -8.820  1.00 12.48 ? 69  ASN A OD1   1 
ATOM   521  N ND2   . ASN A 1 89  ? -2.243  8.491   -9.386  1.00 11.95 ? 69  ASN A ND2   1 
ATOM   522  N N     . ALA A 1 90  ? -2.094  4.644   -8.746  1.00 4.53  ? 70  ALA A N     1 
ATOM   523  C CA    . ALA A 1 90  ? -3.077  4.165   -7.782  1.00 4.45  ? 70  ALA A CA    1 
ATOM   524  C C     . ALA A 1 90  ? -2.411  3.249   -6.765  1.00 5.21  ? 70  ALA A C     1 
ATOM   525  O O     . ALA A 1 90  ? -2.832  3.242   -5.593  1.00 6.89  ? 70  ALA A O     1 
ATOM   526  C CB    . ALA A 1 90  ? -4.145  3.433   -8.480  1.00 4.28  ? 70  ALA A CB    1 
ATOM   527  N N     . LEU A 1 91  ? -1.383  2.506   -7.158  1.00 5.10  ? 71  LEU A N     1 
ATOM   528  C CA    . LEU A 1 91  ? -0.661  1.638   -6.239  1.00 5.69  ? 71  LEU A CA    1 
ATOM   529  C C     . LEU A 1 91  ? 0.340   2.387   -5.352  1.00 6.24  ? 71  LEU A C     1 
ATOM   530  O O     . LEU A 1 91  ? 0.966   1.777   -4.439  1.00 8.98  ? 71  LEU A O     1 
ATOM   531  C CB    . LEU A 1 91  ? 0.028   0.567   -7.083  1.00 5.84  ? 71  LEU A CB    1 
ATOM   532  C CG    . LEU A 1 91  ? -0.937  -0.403  -7.736  1.00 6.60  ? 71  LEU A CG    1 
ATOM   533  C CD1   . LEU A 1 91  ? -0.314  -1.271  -8.837  1.00 8.01  ? 71  LEU A CD1   1 
ATOM   534  C CD2   . LEU A 1 91  ? -1.529  -1.300  -6.652  1.00 7.92  ? 71  LEU A CD2   1 
ATOM   535  N N     . GLY A 1 92  ? 0.587   3.671   -5.618  1.00 6.06  ? 72  GLY A N     1 
ATOM   536  C CA    . GLY A 1 92  ? 1.528   4.493   -4.869  1.00 6.72  ? 72  GLY A CA    1 
ATOM   537  C C     . GLY A 1 92  ? 2.968   4.077   -5.129  1.00 6.59  ? 72  GLY A C     1 
ATOM   538  O O     . GLY A 1 92  ? 3.841   4.322   -4.287  1.00 7.72  ? 72  GLY A O     1 
ATOM   539  N N     . MET A 1 93  ? 3.240   3.478   -6.287  1.00 5.72  ? 73  MET A N     1 
ATOM   540  C CA    . MET A 1 93  ? 4.618   3.112   -6.614  1.00 5.49  ? 73  MET A CA    1 
ATOM   541  C C     . MET A 1 93  ? 5.447   4.362   -6.923  1.00 4.05  ? 73  MET A C     1 
ATOM   542  O O     . MET A 1 93  ? 4.890   5.447   -7.166  1.00 4.73  ? 73  MET A O     1 
ATOM   543  C CB    . MET A 1 93  ? 4.626   2.191   -7.841  1.00 7.14  ? 73  MET A CB    1 
ATOM   544  C CG    . MET A 1 93  ? 3.868   0.938   -7.639  1.00 11.18 ? 73  MET A CG    1 
ATOM   545  S SD    . MET A 1 93  ? 4.807   -0.127  -6.587  1.00 12.24 ? 73  MET A SD    1 
ATOM   546  C CE    . MET A 1 93  ? 3.781   -1.617  -6.589  1.00 10.60 ? 73  MET A CE    1 
ATOM   547  N N     . ASN A 1 94  ? 6.776   4.241   -6.897  1.00 3.58  ? 74  ASN A N     1 
ATOM   548  C CA    . ASN A 1 94  ? 7.658   5.334   -7.262  1.00 3.24  ? 74  ASN A CA    1 
ATOM   549  C C     . ASN A 1 94  ? 8.549   4.964   -8.443  1.00 2.77  ? 74  ASN A C     1 
ATOM   550  O O     . ASN A 1 94  ? 9.432   5.717   -8.777  1.00 2.75  ? 74  ASN A O     1 
ATOM   551  C CB    . ASN A 1 94  ? 8.485   5.861   -6.076  1.00 3.59  ? 74  ASN A CB    1 
ATOM   552  C CG    . ASN A 1 94  ? 9.406   4.823   -5.509  1.00 4.27  ? 74  ASN A CG    1 
ATOM   553  O OD1   . ASN A 1 94  ? 9.902   3.960   -6.214  1.00 4.74  ? 74  ASN A OD1   1 
ATOM   554  N ND2   . ASN A 1 94  ? 9.656   4.875   -4.221  1.00 5.08  ? 74  ASN A ND2   1 
ATOM   555  N N     . ALA A 1 95  ? 8.300   3.809   -9.088  1.00 2.18  ? 75  ALA A N     1 
ATOM   556  C CA    . ALA A 1 95  ? 9.126   3.357   -10.197 1.00 1.98  ? 75  ALA A CA    1 
ATOM   557  C C     . ALA A 1 95  ? 8.325   2.383   -11.033 1.00 1.84  ? 75  ALA A C     1 
ATOM   558  O O     . ALA A 1 95  ? 7.397   1.749   -10.586 1.00 1.79  ? 75  ALA A O     1 
ATOM   559  C CB    . ALA A 1 95  ? 10.415  2.687   -9.719  1.00 1.96  ? 75  ALA A CB    1 
ATOM   560  N N     . TYR A 1 96  ? 8.773   2.189   -12.272 1.00 1.71  ? 76  TYR A N     1 
ATOM   561  C CA    . TYR A 1 96  ? 8.212   1.222   -13.195 1.00 1.69  ? 76  TYR A CA    1 
ATOM   562  C C     . TYR A 1 96  ? 9.351   0.606   -13.995 1.00 1.65  ? 76  TYR A C     1 
ATOM   563  O O     . TYR A 1 96  ? 10.164  1.323   -14.602 1.00 1.69  ? 76  TYR A O     1 
ATOM   564  C CB    . TYR A 1 96  ? 7.264   1.900   -14.177 1.00 1.75  ? 76  TYR A CB    1 
ATOM   565  C CG    . TYR A 1 96  ? 6.578   1.011   -15.162 1.00 1.76  ? 76  TYR A CG    1 
ATOM   566  C CD1   . TYR A 1 96  ? 6.165   -0.282  -14.853 1.00 1.79  ? 76  TYR A CD1   1 
ATOM   567  C CD2   . TYR A 1 96  ? 6.348   1.454   -16.440 1.00 1.80  ? 76  TYR A CD2   1 
ATOM   568  C CE1   . TYR A 1 96  ? 5.472   -1.049  -15.762 1.00 1.97  ? 76  TYR A CE1   1 
ATOM   569  C CE2   . TYR A 1 96  ? 5.648   0.694   -17.351 1.00 1.92  ? 76  TYR A CE2   1 
ATOM   570  C CZ    . TYR A 1 96  ? 5.260   -0.574  -17.036 1.00 2.05  ? 76  TYR A CZ    1 
ATOM   571  O OH    . TYR A 1 96  ? 4.535   -1.405  -17.876 1.00 2.90  ? 76  TYR A OH    1 
ATOM   572  N N     . ARG A 1 97  ? 9.403   -0.720  -13.937 1.00 1.69  ? 77  ARG A N     1 
ATOM   573  C CA    . ARG A 1 97  ? 10.393  -1.470  -14.695 1.00 1.83  ? 77  ARG A CA    1 
ATOM   574  C C     . ARG A 1 97  ? 9.700   -2.042  -15.909 1.00 1.52  ? 77  ARG A C     1 
ATOM   575  O O     . ARG A 1 97  ? 8.710   -2.781  -15.787 1.00 1.59  ? 77  ARG A O     1 
ATOM   576  C CB    . ARG A 1 97  ? 11.008  -2.596  -13.873 1.00 2.38  ? 77  ARG A CB    1 
ATOM   577  C CG    . ARG A 1 97  ? 11.942  -3.520  -14.635 1.00 3.04  ? 77  ARG A CG    1 
ATOM   578  C CD    . ARG A 1 97  ? 12.873  -4.248  -13.688 1.00 3.50  ? 77  ARG A CD    1 
ATOM   579  N NE    . ARG A 1 97  ? 13.743  -5.099  -14.476 1.00 3.93  ? 77  ARG A NE    1 
ATOM   580  C CZ    . ARG A 1 97  ? 13.439  -6.268  -14.964 1.00 4.22  ? 77  ARG A CZ    1 
ATOM   581  N NH1   . ARG A 1 97  ? 12.501  -7.035  -14.441 1.00 4.64  ? 77  ARG A NH1   1 
ATOM   582  N NH2   . ARG A 1 97  ? 14.176  -6.755  -15.966 1.00 4.69  ? 77  ARG A NH2   1 
ATOM   583  N N     . PHE A 1 98  ? 10.210  -1.690  -17.083 1.00 1.41  ? 78  PHE A N     1 
ATOM   584  C CA    . PHE A 1 98  ? 9.599   -2.103  -18.351 1.00 1.39  ? 78  PHE A CA    1 
ATOM   585  C C     . PHE A 1 98  ? 10.711  -2.344  -19.351 1.00 1.36  ? 78  PHE A C     1 
ATOM   586  O O     . PHE A 1 98  ? 11.842  -1.887  -19.140 1.00 1.26  ? 78  PHE A O     1 
ATOM   587  C CB    . PHE A 1 98  ? 8.599   -1.082  -18.856 1.00 1.47  ? 78  PHE A CB    1 
ATOM   588  C CG    . PHE A 1 98  ? 9.184   0.230   -19.251 1.00 1.57  ? 78  PHE A CG    1 
ATOM   589  C CD1   . PHE A 1 98  ? 9.457   1.201   -18.294 1.00 1.62  ? 78  PHE A CD1   1 
ATOM   590  C CD2   . PHE A 1 98  ? 9.478   0.535   -20.581 1.00 1.70  ? 78  PHE A CD2   1 
ATOM   591  C CE1   . PHE A 1 98  ? 10.008  2.424   -18.659 1.00 1.72  ? 78  PHE A CE1   1 
ATOM   592  C CE2   . PHE A 1 98  ? 10.072  1.741   -20.929 1.00 1.75  ? 78  PHE A CE2   1 
ATOM   593  C CZ    . PHE A 1 98  ? 10.339  2.678   -19.971 1.00 1.76  ? 78  PHE A CZ    1 
ATOM   594  N N     . SER A 1 99  ? 10.413  -3.033  -20.430 1.00 1.30  ? 79  SER A N     1 
ATOM   595  C CA    . SER A 1 99  ? 11.439  -3.259  -21.460 1.00 1.44  ? 79  SER A CA    1 
ATOM   596  C C     . SER A 1 99  ? 11.105  -2.458  -22.718 1.00 1.59  ? 79  SER A C     1 
ATOM   597  O O     . SER A 1 99  ? 9.965   -2.115  -23.054 1.00 1.58  ? 79  SER A O     1 
ATOM   598  C CB    . SER A 1 99  ? 11.678  -4.721  -21.743 1.00 1.51  ? 79  SER A CB    1 
ATOM   599  O OG    . SER A 1 99  ? 10.710  -5.289  -22.659 1.00 1.53  ? 79  SER A OG    1 
ATOM   600  N N     . ILE A 1 100 ? 12.168  -2.158  -23.446 1.00 1.80  ? 80  ILE A N     1 
ATOM   601  C CA    . ILE A 1 100 ? 12.085  -1.569  -24.773 1.00 2.09  ? 80  ILE A CA    1 
ATOM   602  C C     . ILE A 1 100 ? 12.179  -2.685  -25.785 1.00 1.80  ? 80  ILE A C     1 
ATOM   603  O O     . ILE A 1 100 ? 13.010  -3.594  -25.674 1.00 1.81  ? 80  ILE A O     1 
ATOM   604  C CB    . ILE A 1 100 ? 13.183  -0.494  -24.928 1.00 2.96  ? 80  ILE A CB    1 
ATOM   605  C CG1   . ILE A 1 100 ? 12.683  0.721   -24.072 1.00 4.22  ? 80  ILE A CG1   1 
ATOM   606  C CG2   . ILE A 1 100 ? 13.319  -0.117  -26.416 1.00 2.91  ? 80  ILE A CG2   1 
ATOM   607  C CD1   . ILE A 1 100 ? 13.478  1.946   -24.104 1.00 5.50  ? 80  ILE A CD1   1 
ATOM   608  N N     . ALA A 1 101 ? 11.260  -2.688  -26.768 1.00 1.59  ? 81  ALA A N     1 
ATOM   609  C CA    . ALA A 1 101 ? 11.258  -3.719  -27.777 1.00 1.51  ? 81  ALA A CA    1 
ATOM   610  C C     . ALA A 1 101 ? 12.285  -3.369  -28.853 1.00 1.43  ? 81  ALA A C     1 
ATOM   611  O O     . ALA A 1 101 ? 12.041  -2.505  -29.685 1.00 1.43  ? 81  ALA A O     1 
ATOM   612  C CB    . ALA A 1 101 ? 9.875   -3.834  -28.375 1.00 1.48  ? 81  ALA A CB    1 
ATOM   613  N N     . TRP A 1 102 ? 13.350  -4.154  -28.939 1.00 1.37  ? 82  TRP A N     1 
ATOM   614  C CA    . TRP A 1 102 ? 14.340  -4.000  -29.998 1.00 1.38  ? 82  TRP A CA    1 
ATOM   615  C C     . TRP A 1 102 ? 13.673  -3.943  -31.382 1.00 1.34  ? 82  TRP A C     1 
ATOM   616  O O     . TRP A 1 102 ? 14.019  -3.107  -32.219 1.00 1.19  ? 82  TRP A O     1 
ATOM   617  C CB    . TRP A 1 102 ? 15.363  -5.137  -29.844 1.00 1.49  ? 82  TRP A CB    1 
ATOM   618  C CG    . TRP A 1 102 ? 16.564  -5.133  -30.735 1.00 1.67  ? 82  TRP A CG    1 
ATOM   619  C CD1   . TRP A 1 102 ? 16.915  -4.285  -31.751 1.00 1.86  ? 82  TRP A CD1   1 
ATOM   620  C CD2   . TRP A 1 102 ? 17.682  -6.012  -30.566 1.00 1.81  ? 82  TRP A CD2   1 
ATOM   621  N NE1   . TRP A 1 102 ? 18.117  -4.650  -32.298 1.00 1.98  ? 82  TRP A NE1   1 
ATOM   622  C CE2   . TRP A 1 102 ? 18.632  -5.688  -31.565 1.00 1.85  ? 82  TRP A CE2   1 
ATOM   623  C CE3   . TRP A 1 102 ? 17.939  -7.068  -29.702 1.00 1.87  ? 82  TRP A CE3   1 
ATOM   624  C CZ2   . TRP A 1 102 ? 19.814  -6.397  -31.740 1.00 1.97  ? 82  TRP A CZ2   1 
ATOM   625  C CZ3   . TRP A 1 102 ? 19.107  -7.771  -29.882 1.00 1.97  ? 82  TRP A CZ3   1 
ATOM   626  C CH2   . TRP A 1 102 ? 20.047  -7.411  -30.864 1.00 2.03  ? 82  TRP A CH2   1 
ATOM   627  N N     . PRO A 1 103 ? 12.661  -4.774  -31.658 1.00 1.33  ? 83  PRO A N     1 
ATOM   628  C CA    . PRO A 1 103 ? 11.971  -4.698  -32.946 1.00 1.39  ? 83  PRO A CA    1 
ATOM   629  C C     . PRO A 1 103 ? 11.336  -3.356  -33.270 1.00 1.40  ? 83  PRO A C     1 
ATOM   630  O O     . PRO A 1 103 ? 11.100  -3.093  -34.443 1.00 1.34  ? 83  PRO A O     1 
ATOM   631  C CB    . PRO A 1 103 ? 10.867  -5.770  -32.877 1.00 1.53  ? 83  PRO A CB    1 
ATOM   632  C CG    . PRO A 1 103 ? 11.403  -6.765  -31.898 1.00 1.49  ? 83  PRO A CG    1 
ATOM   633  C CD    . PRO A 1 103 ? 12.140  -5.932  -30.879 1.00 1.46  ? 83  PRO A CD    1 
ATOM   634  N N     . ARG A 1 104 ? 11.035  -2.521  -32.268 1.00 1.36  ? 84  ARG A N     1 
ATOM   635  C CA    . ARG A 1 104 ? 10.484  -1.209  -32.561 1.00 1.38  ? 84  ARG A CA    1 
ATOM   636  C C     . ARG A 1 104 ? 11.596  -0.204  -32.848 1.00 1.43  ? 84  ARG A C     1 
ATOM   637  O O     . ARG A 1 104 ? 11.288  0.870   -33.358 1.00 1.56  ? 84  ARG A O     1 
ATOM   638  C CB    . ARG A 1 104 ? 9.636   -0.663  -31.415 1.00 1.46  ? 84  ARG A CB    1 
ATOM   639  C CG    . ARG A 1 104 ? 8.386   -1.473  -31.129 1.00 1.56  ? 84  ARG A CG    1 
ATOM   640  C CD    . ARG A 1 104 ? 7.473   -0.658  -30.224 1.00 1.73  ? 84  ARG A CD    1 
ATOM   641  N NE    . ARG A 1 104 ? 6.289   -1.421  -29.826 1.00 1.98  ? 84  ARG A NE    1 
ATOM   642  C CZ    . ARG A 1 104 ? 5.233   -1.723  -30.552 1.00 2.23  ? 84  ARG A CZ    1 
ATOM   643  N NH1   . ARG A 1 104 ? 5.062   -1.193  -31.733 1.00 2.52  ? 84  ARG A NH1   1 
ATOM   644  N NH2   . ARG A 1 104 ? 4.376   -2.564  -30.003 1.00 2.70  ? 84  ARG A NH2   1 
ATOM   645  N N     . ILE A 1 105 ? 12.828  -0.483  -32.416 1.00 1.37  ? 85  ILE A N     1 
ATOM   646  C CA    . ILE A 1 105 ? 13.942  0.471   -32.455 1.00 1.43  ? 85  ILE A CA    1 
ATOM   647  C C     . ILE A 1 105 ? 14.813  0.206   -33.683 1.00 1.62  ? 85  ILE A C     1 
ATOM   648  O O     . ILE A 1 105 ? 15.195  1.160   -34.364 1.00 2.04  ? 85  ILE A O     1 
ATOM   649  C CB    . ILE A 1 105 ? 14.787  0.448   -31.170 1.00 1.38  ? 85  ILE A CB    1 
ATOM   650  C CG1   . ILE A 1 105 ? 13.934  0.622   -29.934 1.00 1.37  ? 85  ILE A CG1   1 
ATOM   651  C CG2   . ILE A 1 105 ? 15.882  1.475   -31.263 1.00 1.39  ? 85  ILE A CG2   1 
ATOM   652  C CD1   . ILE A 1 105 ? 12.974  1.805   -29.996 1.00 1.38  ? 85  ILE A CD1   1 
ATOM   653  N N     . VAL A 1 106 ? 15.168  -1.048  -33.933 1.00 1.72  ? 86  VAL A N     1 
ATOM   654  C CA    . VAL A 1 106 ? 15.928  -1.443  -35.119 1.00 1.94  ? 86  VAL A CA    1 
ATOM   655  C C     . VAL A 1 106 ? 15.167  -2.623  -35.687 1.00 2.14  ? 86  VAL A C     1 
ATOM   656  O O     . VAL A 1 106 ? 15.438  -3.756  -35.310 1.00 2.18  ? 86  VAL A O     1 
ATOM   657  C CB    . VAL A 1 106 ? 17.400  -1.786  -34.799 1.00 2.17  ? 86  VAL A CB    1 
ATOM   658  C CG1   . VAL A 1 106 ? 18.175  -2.001  -36.094 1.00 2.24  ? 86  VAL A CG1   1 
ATOM   659  C CG2   . VAL A 1 106 ? 18.064  -0.784  -33.929 1.00 2.21  ? 86  VAL A CG2   1 
ATOM   660  N N     . PRO A 1 107 ? 14.127  -2.406  -36.507 1.00 2.38  ? 87  PRO A N     1 
ATOM   661  C CA    . PRO A 1 107 ? 13.237  -3.482  -36.926 1.00 2.77  ? 87  PRO A CA    1 
ATOM   662  C C     . PRO A 1 107 ? 13.927  -4.672  -37.588 1.00 3.73  ? 87  PRO A C     1 
ATOM   663  O O     . PRO A 1 107 ? 13.430  -5.801  -37.418 1.00 5.32  ? 87  PRO A O     1 
ATOM   664  C CB    . PRO A 1 107 ? 12.284  -2.753  -37.863 1.00 2.68  ? 87  PRO A CB    1 
ATOM   665  C CG    . PRO A 1 107 ? 12.245  -1.346  -37.338 1.00 2.56  ? 87  PRO A CG    1 
ATOM   666  C CD    . PRO A 1 107 ? 13.669  -1.085  -36.929 1.00 2.50  ? 87  PRO A CD    1 
ATOM   667  N N     . LEU A 1 108 ? 15.063  -4.468  -38.266 1.00 4.21  ? 88  LEU A N     1 
ATOM   668  C CA    . LEU A 1 108 ? 15.758  -5.582  -38.897 1.00 5.36  ? 88  LEU A CA    1 
ATOM   669  C C     . LEU A 1 108 ? 16.846  -6.147  -37.987 1.00 5.08  ? 88  LEU A C     1 
ATOM   670  O O     . LEU A 1 108 ? 17.580  -7.039  -38.399 1.00 6.15  ? 88  LEU A O     1 
ATOM   671  C CB    . LEU A 1 108 ? 16.374  -5.084  -40.209 1.00 6.50  ? 88  LEU A CB    1 
ATOM   672  C CG    . LEU A 1 108 ? 15.379  -4.592  -41.237 1.00 8.32  ? 88  LEU A CG    1 
ATOM   673  C CD1   . LEU A 1 108 ? 16.122  -3.923  -42.390 1.00 9.27  ? 88  LEU A CD1   1 
ATOM   674  C CD2   . LEU A 1 108 ? 14.530  -5.731  -41.736 1.00 9.55  ? 88  LEU A CD2   1 
ATOM   675  N N     . GLY A 1 109 ? 16.979  -5.668  -36.754 1.00 4.16  ? 89  GLY A N     1 
ATOM   676  C CA    . GLY A 1 109 ? 17.970  -6.166  -35.828 1.00 4.69  ? 89  GLY A CA    1 
ATOM   677  C C     . GLY A 1 109 ? 19.276  -5.435  -36.005 1.00 4.82  ? 89  GLY A C     1 
ATOM   678  O O     . GLY A 1 109 ? 19.767  -4.874  -35.053 1.00 6.07  ? 89  GLY A O     1 
ATOM   679  N N     . ALA A 1 110 ? 19.790  -5.494  -37.233 1.00 5.27  ? 90  ALA A N     1 
ATOM   680  C CA    . ALA A 1 110 ? 20.942  -4.757  -37.707 1.00 6.23  ? 90  ALA A CA    1 
ATOM   681  C C     . ALA A 1 110 ? 20.488  -4.043  -38.962 1.00 6.64  ? 90  ALA A C     1 
ATOM   682  O O     . ALA A 1 110 ? 20.220  -4.650  -40.003 1.00 9.49  ? 90  ALA A O     1 
ATOM   683  C CB    . ALA A 1 110 ? 22.055  -5.728  -38.005 1.00 6.99  ? 90  ALA A CB    1 
ATOM   684  N N     . GLY A 1 111 ? 20.346  -2.737  -38.839 1.00 6.03  ? 91  GLY A N     1 
ATOM   685  C CA    . GLY A 1 111 ? 19.764  -2.000  -39.936 1.00 5.31  ? 91  GLY A CA    1 
ATOM   686  C C     . GLY A 1 111 ? 19.414  -0.620  -39.445 1.00 4.73  ? 91  GLY A C     1 
ATOM   687  O O     . GLY A 1 111 ? 19.880  -0.198  -38.409 1.00 4.98  ? 91  GLY A O     1 
ATOM   688  N N     . PRO A 1 112 ? 18.592  0.111   -40.231 1.00 5.08  ? 92  PRO A N     1 
ATOM   689  C CA    . PRO A 1 112 ? 18.210  1.455   -39.853 1.00 4.95  ? 92  PRO A CA    1 
ATOM   690  C C     . PRO A 1 112 ? 17.464  1.522   -38.533 1.00 4.42  ? 92  PRO A C     1 
ATOM   691  O O     . PRO A 1 112 ? 16.790  0.577   -38.127 1.00 4.49  ? 92  PRO A O     1 
ATOM   692  C CB    . PRO A 1 112 ? 17.278  1.863   -40.991 1.00 5.66  ? 92  PRO A CB    1 
ATOM   693  C CG    . PRO A 1 112 ? 17.761  1.072   -42.153 1.00 6.71  ? 92  PRO A CG    1 
ATOM   694  C CD    . PRO A 1 112 ? 18.069  -0.284  -41.551 1.00 5.49  ? 92  PRO A CD    1 
ATOM   695  N N     . ILE A 1 113 ? 17.589  2.673   -37.908 1.00 4.73  ? 93  ILE A N     1 
ATOM   696  C CA    . ILE A 1 113 ? 16.744  3.000   -36.764 1.00 5.36  ? 93  ILE A CA    1 
ATOM   697  C C     . ILE A 1 113 ? 15.313  3.250   -37.231 1.00 5.21  ? 93  ILE A C     1 
ATOM   698  O O     . ILE A 1 113 ? 15.049  3.590   -38.389 1.00 5.20  ? 93  ILE A O     1 
ATOM   699  C CB    . ILE A 1 113 ? 17.334  4.221   -36.060 1.00 7.20  ? 93  ILE A CB    1 
ATOM   700  C CG1   . ILE A 1 113 ? 18.706  3.887   -35.495 1.00 8.25  ? 93  ILE A CG1   1 
ATOM   701  C CG2   . ILE A 1 113 ? 16.349  4.789   -35.043 1.00 8.65  ? 93  ILE A CG2   1 
ATOM   702  C CD1   . ILE A 1 113 ? 19.485  5.123   -35.066 1.00 11.40 ? 93  ILE A CD1   1 
ATOM   703  N N     . ASN A 1 114 ? 14.372  3.039   -36.312 1.00 4.38  ? 94  ASN A N     1 
ATOM   704  C CA    . ASN A 1 114 ? 12.982  3.411   -36.514 1.00 4.18  ? 94  ASN A CA    1 
ATOM   705  C C     . ASN A 1 114 ? 12.676  4.514   -35.532 1.00 4.16  ? 94  ASN A C     1 
ATOM   706  O O     . ASN A 1 114 ? 12.444  4.242   -34.344 1.00 4.13  ? 94  ASN A O     1 
ATOM   707  C CB    . ASN A 1 114 ? 12.091  2.197   -36.288 1.00 4.32  ? 94  ASN A CB    1 
ATOM   708  C CG    . ASN A 1 114 ? 10.617  2.477   -36.433 1.00 4.99  ? 94  ASN A CG    1 
ATOM   709  O OD1   . ASN A 1 114 ? 10.190  3.111   -37.403 1.00 7.53  ? 94  ASN A OD1   1 
ATOM   710  N ND2   . ASN A 1 114 ? 9.801   1.968   -35.520 1.00 4.60  ? 94  ASN A ND2   1 
ATOM   711  N N     . GLN A 1 115 ? 12.659  5.779   -36.007 1.00 4.06  ? 95  GLN A N     1 
ATOM   712  C CA    . GLN A 1 115 ? 12.554  6.857   -35.057 1.00 3.97  ? 95  GLN A CA    1 
ATOM   713  C C     . GLN A 1 115 ? 11.188  6.858   -34.369 1.00 3.86  ? 95  GLN A C     1 
ATOM   714  O O     . GLN A 1 115 ? 11.106  7.254   -33.197 1.00 3.78  ? 95  GLN A O     1 
ATOM   715  C CB    . GLN A 1 115 ? 12.833  8.192   -35.761 1.00 4.60  ? 95  GLN A CB    1 
ATOM   716  C CG    . GLN A 1 115 ? 12.980  9.379   -34.820 1.00 5.23  ? 95  GLN A CG    1 
ATOM   717  C CD    . GLN A 1 115 ? 14.122  9.262   -33.840 1.00 5.92  ? 95  GLN A CD    1 
ATOM   718  O OE1   . GLN A 1 115 ? 15.214  8.820   -34.166 1.00 7.16  ? 95  GLN A OE1   1 
ATOM   719  N NE2   . GLN A 1 115 ? 13.848  9.483   -32.576 1.00 6.42  ? 95  GLN A NE2   1 
ATOM   720  N N     . ALA A 1 116 ? 10.159  6.369   -35.034 1.00 3.67  ? 96  ALA A N     1 
ATOM   721  C CA    . ALA A 1 116 ? 8.833   6.311   -34.416 1.00 3.54  ? 96  ALA A CA    1 
ATOM   722  C C     . ALA A 1 116 ? 8.867   5.470   -33.149 1.00 3.41  ? 96  ALA A C     1 
ATOM   723  O O     . ALA A 1 116 ? 8.144   5.764   -32.184 1.00 3.35  ? 96  ALA A O     1 
ATOM   724  C CB    . ALA A 1 116 ? 7.837   5.753   -35.389 1.00 3.71  ? 96  ALA A CB    1 
ATOM   725  N N     . GLY A 1 117 ? 9.693   4.424   -33.137 1.00 3.20  ? 97  GLY A N     1 
ATOM   726  C CA    . GLY A 1 117 ? 9.800   3.568   -31.968 1.00 3.14  ? 97  GLY A CA    1 
ATOM   727  C C     . GLY A 1 117 ? 10.482  4.295   -30.811 1.00 3.07  ? 97  GLY A C     1 
ATOM   728  O O     . GLY A 1 117 ? 10.029  4.297   -29.660 1.00 2.89  ? 97  GLY A O     1 
ATOM   729  N N     . LEU A 1 118 ? 11.597  4.990   -31.099 1.00 3.00  ? 98  LEU A N     1 
ATOM   730  C CA    . LEU A 1 118 ? 12.272  5.783   -30.085 1.00 3.39  ? 98  LEU A CA    1 
ATOM   731  C C     . LEU A 1 118 ? 11.361  6.892   -29.550 1.00 3.34  ? 98  LEU A C     1 
ATOM   732  O O     . LEU A 1 118 ? 11.351  7.133   -28.341 1.00 3.40  ? 98  LEU A O     1 
ATOM   733  C CB    . LEU A 1 118 ? 13.551  6.416   -30.655 1.00 4.02  ? 98  LEU A CB    1 
ATOM   734  C CG    . LEU A 1 118 ? 14.660  5.411   -30.893 1.00 4.66  ? 98  LEU A CG    1 
ATOM   735  C CD1   . LEU A 1 118 ? 15.766  5.992   -31.776 1.00 5.45  ? 98  LEU A CD1   1 
ATOM   736  C CD2   . LEU A 1 118 ? 15.293  4.938   -29.601 1.00 4.94  ? 98  LEU A CD2   1 
ATOM   737  N N     . ASP A 1 119 ? 10.592  7.525   -30.423 1.00 3.57  ? 99  ASP A N     1 
ATOM   738  C CA    . ASP A 1 119 ? 9.731   8.624   -30.003 1.00 3.83  ? 99  ASP A CA    1 
ATOM   739  C C     . ASP A 1 119 ? 8.626   8.122   -29.090 1.00 2.75  ? 99  ASP A C     1 
ATOM   740  O O     . ASP A 1 119 ? 8.249   8.800   -28.144 1.00 2.65  ? 99  ASP A O     1 
ATOM   741  C CB    . ASP A 1 119 ? 9.177   9.356   -31.220 1.00 5.49  ? 99  ASP A CB    1 
ATOM   742  C CG    . ASP A 1 119 ? 10.227  10.172  -31.980 1.00 8.23  ? 99  ASP A CG    1 
ATOM   743  O OD1   . ASP A 1 119 ? 11.320  10.387  -31.457 1.00 11.49 ? 99  ASP A OD1   1 
ATOM   744  O OD2   . ASP A 1 119 ? 9.884   10.609  -33.082 1.00 13.02 ? 99  ASP A OD2   1 
ATOM   745  N N     . HIS A 1 120 ? 8.107   6.931   -29.365 1.00 2.18  ? 100 HIS A N     1 
ATOM   746  C CA    . HIS A 1 120 ? 7.112   6.318   -28.494 1.00 1.84  ? 100 HIS A CA    1 
ATOM   747  C C     . HIS A 1 120 ? 7.670   6.197   -27.080 1.00 1.65  ? 100 HIS A C     1 
ATOM   748  O O     . HIS A 1 120 ? 7.023   6.587   -26.091 1.00 1.45  ? 100 HIS A O     1 
ATOM   749  C CB    . HIS A 1 120 ? 6.696   4.953   -29.038 1.00 1.91  ? 100 HIS A CB    1 
ATOM   750  C CG    . HIS A 1 120 ? 5.883   4.144   -28.080 1.00 2.07  ? 100 HIS A CG    1 
ATOM   751  N ND1   . HIS A 1 120 ? 4.537   4.403   -27.872 1.00 2.45  ? 100 HIS A ND1   1 
ATOM   752  C CD2   . HIS A 1 120 ? 6.259   3.143   -27.225 1.00 2.14  ? 100 HIS A CD2   1 
ATOM   753  C CE1   . HIS A 1 120 ? 4.133   3.549   -26.960 1.00 2.24  ? 100 HIS A CE1   1 
ATOM   754  N NE2   . HIS A 1 120 ? 5.136   2.815   -26.490 1.00 2.23  ? 100 HIS A NE2   1 
ATOM   755  N N     . TYR A 1 121 ? 8.841   5.570   -26.941 1.00 1.48  ? 101 TYR A N     1 
ATOM   756  C CA    . TYR A 1 121 ? 9.376   5.374   -25.615 1.00 1.46  ? 101 TYR A CA    1 
ATOM   757  C C     . TYR A 1 121 ? 9.795   6.682   -24.959 1.00 1.65  ? 101 TYR A C     1 
ATOM   758  O O     . TYR A 1 121 ? 9.744   6.800   -23.751 1.00 1.65  ? 101 TYR A O     1 
ATOM   759  C CB    . TYR A 1 121 ? 10.482  4.318   -25.635 1.00 1.32  ? 101 TYR A CB    1 
ATOM   760  C CG    . TYR A 1 121 ? 9.964   2.946   -25.977 1.00 1.20  ? 101 TYR A CG    1 
ATOM   761  C CD1   . TYR A 1 121 ? 9.215   2.234   -25.058 1.00 1.17  ? 101 TYR A CD1   1 
ATOM   762  C CD2   . TYR A 1 121 ? 10.303  2.302   -27.153 1.00 1.19  ? 101 TYR A CD2   1 
ATOM   763  C CE1   . TYR A 1 121 ? 8.772   0.955   -25.325 1.00 1.15  ? 101 TYR A CE1   1 
ATOM   764  C CE2   . TYR A 1 121 ? 9.825   1.041   -27.456 1.00 1.17  ? 101 TYR A CE2   1 
ATOM   765  C CZ    . TYR A 1 121 ? 9.099   0.337   -26.517 1.00 1.14  ? 101 TYR A CZ    1 
ATOM   766  O OH    . TYR A 1 121 ? 8.711   -0.952  -26.834 1.00 1.17  ? 101 TYR A OH    1 
ATOM   767  N N     . SER A 1 122 ? 10.211  7.669   -25.746 1.00 1.97  ? 102 SER A N     1 
ATOM   768  C CA    . SER A 1 122 ? 10.514  8.976   -25.202 1.00 2.49  ? 102 SER A CA    1 
ATOM   769  C C     . SER A 1 122 ? 9.282   9.606   -24.556 1.00 2.52  ? 102 SER A C     1 
ATOM   770  O O     . SER A 1 122 ? 9.352   10.159  -23.479 1.00 2.26  ? 102 SER A O     1 
ATOM   771  C CB    . SER A 1 122 ? 11.083  9.813   -26.294 1.00 2.98  ? 102 SER A CB    1 
ATOM   772  O OG    . SER A 1 122 ? 11.424  11.108  -25.780 1.00 4.80  ? 102 SER A OG    1 
ATOM   773  N N     . ARG A 1 123 ? 8.143   9.522   -25.242 1.00 2.56  ? 103 ARG A N     1 
ATOM   774  C CA    . ARG A 1 123 ? 6.909   10.044  -24.672 1.00 2.94  ? 103 ARG A CA    1 
ATOM   775  C C     . ARG A 1 123 ? 6.570   9.274   -23.398 1.00 2.96  ? 103 ARG A C     1 
ATOM   776  O O     . ARG A 1 123 ? 6.111   9.828   -22.426 1.00 2.84  ? 103 ARG A O     1 
ATOM   777  C CB    . ARG A 1 123 ? 5.776   9.942   -25.683 1.00 3.25  ? 103 ARG A CB    1 
ATOM   778  C CG    . ARG A 1 123 ? 5.897   10.914  -26.837 1.00 3.77  ? 103 ARG A CG    1 
ATOM   779  C CD    . ARG A 1 123 ? 4.660   10.900  -27.722 1.00 4.24  ? 103 ARG A CD    1 
ATOM   780  N NE    . ARG A 1 123 ? 4.458   9.712   -28.469 1.00 4.86  ? 103 ARG A NE    1 
ATOM   781  C CZ    . ARG A 1 123 ? 4.977   9.450   -29.660 1.00 4.92  ? 103 ARG A CZ    1 
ATOM   782  N NH1   . ARG A 1 123 ? 5.775   10.318  -30.242 1.00 5.99  ? 103 ARG A NH1   1 
ATOM   783  N NH2   . ARG A 1 123 ? 4.660   8.343   -30.293 1.00 5.29  ? 103 ARG A NH2   1 
ATOM   784  N N     . MET A 1 124 ? 6.709   7.944   -23.427 1.00 2.95  ? 104 MET A N     1 
ATOM   785  C CA    . MET A 1 124 ? 6.346   7.112   -22.291 1.00 3.51  ? 104 MET A CA    1 
ATOM   786  C C     . MET A 1 124 ? 7.243   7.456   -21.092 1.00 2.94  ? 104 MET A C     1 
ATOM   787  O O     . MET A 1 124 ? 6.764   7.594   -19.978 1.00 2.33  ? 104 MET A O     1 
ATOM   788  C CB    . MET A 1 124 ? 6.464   5.645   -22.684 1.00 5.24  ? 104 MET A CB    1 
ATOM   789  C CG    . MET A 1 124 ? 6.061   4.716   -21.612 1.00 6.68  ? 104 MET A CG    1 
ATOM   790  S SD    . MET A 1 124 ? 6.308   2.982   -22.258 1.00 12.39 ? 104 MET A SD    1 
ATOM   791  C CE    . MET A 1 124 ? 6.189   2.022   -20.760 1.00 13.51 ? 104 MET A CE    1 
ATOM   792  N N     . VAL A 1 125 ? 8.543   7.670   -21.323 1.00 2.55  ? 105 VAL A N     1 
ATOM   793  C CA    . VAL A 1 125 ? 9.449   8.087   -20.261 1.00 2.62  ? 105 VAL A CA    1 
ATOM   794  C C     . VAL A 1 125 ? 8.983   9.414   -19.673 1.00 2.64  ? 105 VAL A C     1 
ATOM   795  O O     . VAL A 1 125 ? 8.966   9.566   -18.466 1.00 2.94  ? 105 VAL A O     1 
ATOM   796  C CB    . VAL A 1 125 ? 10.897  8.100   -20.757 1.00 2.56  ? 105 VAL A CB    1 
ATOM   797  C CG1   . VAL A 1 125 ? 11.809  8.970   -19.917 1.00 2.73  ? 105 VAL A CG1   1 
ATOM   798  C CG2   . VAL A 1 125 ? 11.414  6.654   -20.884 1.00 2.70  ? 105 VAL A CG2   1 
ATOM   799  N N     . ASP A 1 126 ? 8.652   10.379  -20.552 1.00 2.69  ? 106 ASP A N     1 
ATOM   800  C CA    . ASP A 1 126 ? 8.220   11.655  -20.034 1.00 3.08  ? 106 ASP A CA    1 
ATOM   801  C C     . ASP A 1 126 ? 6.926   11.510  -19.246 1.00 2.77  ? 106 ASP A C     1 
ATOM   802  O O     . ASP A 1 126 ? 6.782   12.209  -18.262 1.00 2.81  ? 106 ASP A O     1 
ATOM   803  C CB    . ASP A 1 126 ? 8.083   12.637  -21.174 1.00 3.56  ? 106 ASP A CB    1 
ATOM   804  C CG    . ASP A 1 126 ? 9.399   13.100  -21.759 1.00 4.44  ? 106 ASP A CG    1 
ATOM   805  O OD1   . ASP A 1 126 ? 10.438  12.885  -21.109 1.00 5.57  ? 106 ASP A OD1   1 
ATOM   806  O OD2   . ASP A 1 126 ? 9.323   13.747  -22.802 1.00 7.38  ? 106 ASP A OD2   1 
ATOM   807  N N     . ALA A 1 127 ? 5.987   10.674  -19.702 1.00 2.38  ? 107 ALA A N     1 
ATOM   808  C CA    . ALA A 1 127 ? 4.746   10.440  -18.952 1.00 2.32  ? 107 ALA A CA    1 
ATOM   809  C C     . ALA A 1 127 ? 5.058   9.860   -17.568 1.00 2.39  ? 107 ALA A C     1 
ATOM   810  O O     . ALA A 1 127 ? 4.421   10.245  -16.578 1.00 2.62  ? 107 ALA A O     1 
ATOM   811  C CB    . ALA A 1 127 ? 3.794   9.602   -19.727 1.00 2.36  ? 107 ALA A CB    1 
ATOM   812  N N     . LEU A 1 128 ? 5.988   8.913   -17.488 1.00 2.44  ? 108 LEU A N     1 
ATOM   813  C CA    . LEU A 1 128 ? 6.339   8.301   -16.221 1.00 2.53  ? 108 LEU A CA    1 
ATOM   814  C C     . LEU A 1 128 ? 6.976   9.344   -15.314 1.00 2.99  ? 108 LEU A C     1 
ATOM   815  O O     . LEU A 1 128 ? 6.588   9.436   -14.158 1.00 2.94  ? 108 LEU A O     1 
ATOM   816  C CB    . LEU A 1 128 ? 7.337   7.154   -16.475 1.00 2.40  ? 108 LEU A CB    1 
ATOM   817  C CG    . LEU A 1 128 ? 6.719   5.910   -17.085 1.00 2.28  ? 108 LEU A CG    1 
ATOM   818  C CD1   . LEU A 1 128 ? 7.798   5.006   -17.650 1.00 2.38  ? 108 LEU A CD1   1 
ATOM   819  C CD2   . LEU A 1 128 ? 5.853   5.184   -16.077 1.00 2.27  ? 108 LEU A CD2   1 
ATOM   820  N N     . LEU A 1 129 ? 7.966   10.107  -15.800 1.00 3.71  ? 109 LEU A N     1 
ATOM   821  C CA    . LEU A 1 129 ? 8.618   11.123  -14.959 1.00 4.79  ? 109 LEU A CA    1 
ATOM   822  C C     . LEU A 1 129 ? 7.603   12.175  -14.530 1.00 5.40  ? 109 LEU A C     1 
ATOM   823  O O     . LEU A 1 129 ? 7.658   12.574  -13.346 1.00 7.59  ? 109 LEU A O     1 
ATOM   824  C CB    . LEU A 1 129 ? 9.802   11.730  -15.718 1.00 5.94  ? 109 LEU A CB    1 
ATOM   825  C CG    . LEU A 1 129 ? 10.988  10.792  -15.905 1.00 7.89  ? 109 LEU A CG    1 
ATOM   826  C CD1   . LEU A 1 129 ? 11.998  11.459  -16.831 1.00 9.31  ? 109 LEU A CD1   1 
ATOM   827  C CD2   . LEU A 1 129 ? 11.642  10.413  -14.598 1.00 8.41  ? 109 LEU A CD2   1 
ATOM   828  N N     . GLY A 1 130 ? 6.681   12.546  -15.407 1.00 5.51  ? 110 GLY A N     1 
ATOM   829  C CA    . GLY A 1 130 ? 5.657   13.520  -15.018 1.00 6.20  ? 110 GLY A CA    1 
ATOM   830  C C     . GLY A 1 130 ? 4.760   13.009  -13.894 1.00 6.55  ? 110 GLY A C     1 
ATOM   831  O O     . GLY A 1 130 ? 4.206   13.805  -13.104 1.00 9.36  ? 110 GLY A O     1 
ATOM   832  N N     . ALA A 1 131 ? 4.591   11.700  -13.772 1.00 5.51  ? 111 ALA A N     1 
ATOM   833  C CA    . ALA A 1 131 ? 3.818   11.074  -12.701 1.00 5.28  ? 111 ALA A CA    1 
ATOM   834  C C     . ALA A 1 131 ? 4.641   10.731  -11.457 1.00 5.88  ? 111 ALA A C     1 
ATOM   835  O O     . ALA A 1 131 ? 4.101   10.157  -10.510 1.00 6.98  ? 111 ALA A O     1 
ATOM   836  C CB    . ALA A 1 131 ? 3.223   9.819   -13.267 1.00 5.19  ? 111 ALA A CB    1 
ATOM   837  N N     . GLY A 1 132 ? 5.921   11.086  -11.456 1.00 5.96  ? 112 GLY A N     1 
ATOM   838  C CA    . GLY A 1 132 ? 6.773   10.749  -10.326 1.00 6.58  ? 112 GLY A CA    1 
ATOM   839  C C     . GLY A 1 132 ? 7.202   9.291   -10.294 1.00 6.99  ? 112 GLY A C     1 
ATOM   840  O O     . GLY A 1 132 ? 7.499   8.762   -9.225  1.00 8.76  ? 112 GLY A O     1 
ATOM   841  N N     . LEU A 1 133 ? 7.238   8.609   -11.445 1.00 5.37  ? 113 LEU A N     1 
ATOM   842  C CA    . LEU A 1 133 ? 7.633   7.211   -11.538 1.00 4.81  ? 113 LEU A CA    1 
ATOM   843  C C     . LEU A 1 133 ? 8.976   7.116   -12.253 1.00 4.79  ? 113 LEU A C     1 
ATOM   844  O O     . LEU A 1 133 ? 9.111   7.504   -13.412 1.00 6.09  ? 113 LEU A O     1 
ATOM   845  C CB    . LEU A 1 133 ? 6.574   6.434   -12.326 1.00 4.32  ? 113 LEU A CB    1 
ATOM   846  C CG    . LEU A 1 133 ? 5.175   6.404   -11.706 1.00 4.18  ? 113 LEU A CG    1 
ATOM   847  C CD1   . LEU A 1 133 ? 4.121   5.974   -12.711 1.00 4.31  ? 113 LEU A CD1   1 
ATOM   848  C CD2   . LEU A 1 133 ? 5.176   5.445   -10.507 1.00 4.62  ? 113 LEU A CD2   1 
ATOM   849  N N     . GLN A 1 134 ? 9.980   6.645   -11.531 1.00 3.62  ? 114 GLN A N     1 
ATOM   850  C CA    . GLN A 1 134 ? 11.304  6.494   -12.106 1.00 4.16  ? 114 GLN A CA    1 
ATOM   851  C C     . GLN A 1 134 ? 11.303  5.316   -13.083 1.00 3.73  ? 114 GLN A C     1 
ATOM   852  O O     . GLN A 1 134 ? 10.951  4.198   -12.728 1.00 3.49  ? 114 GLN A O     1 
ATOM   853  C CB    . GLN A 1 134 ? 12.324  6.225   -11.008 1.00 4.59  ? 114 GLN A CB    1 
ATOM   854  C CG    . GLN A 1 134 ? 13.734  6.115   -11.555 1.00 5.29  ? 114 GLN A CG    1 
ATOM   855  C CD    . GLN A 1 134 ? 14.768  5.822   -10.498 1.00 6.70  ? 114 GLN A CD    1 
ATOM   856  O OE1   . GLN A 1 134 ? 14.473  5.729   -9.301  1.00 8.84  ? 114 GLN A OE1   1 
ATOM   857  N NE2   . GLN A 1 134 ? 15.972  5.549   -10.965 1.00 8.34  ? 114 GLN A NE2   1 
ATOM   858  N N     . PRO A 1 135 ? 11.697  5.549   -14.342 1.00 4.07  ? 115 PRO A N     1 
ATOM   859  C CA    . PRO A 1 135 ? 11.777  4.455   -15.308 1.00 4.29  ? 115 PRO A CA    1 
ATOM   860  C C     . PRO A 1 135 ? 13.018  3.610   -15.052 1.00 4.53  ? 115 PRO A C     1 
ATOM   861  O O     . PRO A 1 135 ? 14.137  4.129   -15.073 1.00 5.81  ? 115 PRO A O     1 
ATOM   862  C CB    . PRO A 1 135 ? 11.831  5.228   -16.631 1.00 4.85  ? 115 PRO A CB    1 
ATOM   863  C CG    . PRO A 1 135 ? 12.354  6.626   -16.321 1.00 5.58  ? 115 PRO A CG    1 
ATOM   864  C CD    . PRO A 1 135 ? 11.898  6.880   -14.923 1.00 4.39  ? 115 PRO A CD    1 
ATOM   865  N N     . PHE A 1 136 ? 12.830  2.316   -14.920 1.00 3.97  ? 116 PHE A N     1 
ATOM   866  C CA    . PHE A 1 136 ? 13.900  1.347   -14.886 1.00 4.66  ? 116 PHE A CA    1 
ATOM   867  C C     . PHE A 1 136 ? 13.802  0.570   -16.179 1.00 4.46  ? 116 PHE A C     1 
ATOM   868  O O     . PHE A 1 136 ? 12.912  -0.268  -16.289 1.00 5.28  ? 116 PHE A O     1 
ATOM   869  C CB    . PHE A 1 136 ? 13.780  0.398   -13.693 1.00 5.71  ? 116 PHE A CB    1 
ATOM   870  C CG    . PHE A 1 136 ? 14.508  0.822   -12.446 1.00 7.12  ? 116 PHE A CG    1 
ATOM   871  C CD1   . PHE A 1 136 ? 14.056  1.940   -11.755 1.00 8.20  ? 116 PHE A CD1   1 
ATOM   872  C CD2   . PHE A 1 136 ? 15.573  0.107   -11.950 1.00 9.30  ? 116 PHE A CD2   1 
ATOM   873  C CE1   . PHE A 1 136 ? 14.684  2.323   -10.571 1.00 9.14  ? 116 PHE A CE1   1 
ATOM   874  C CE2   . PHE A 1 136 ? 16.187  0.471   -10.769 1.00 9.10  ? 116 PHE A CE2   1 
ATOM   875  C CZ    . PHE A 1 136 ? 15.750  1.591   -10.108 1.00 8.96  ? 116 PHE A CZ    1 
ATOM   876  N N     . VAL A 1 137 ? 14.694  0.809   -17.125 1.00 3.83  ? 117 VAL A N     1 
ATOM   877  C CA    . VAL A 1 137 ? 14.514  0.267   -18.457 1.00 3.93  ? 117 VAL A CA    1 
ATOM   878  C C     . VAL A 1 137 ? 15.361  -0.983  -18.654 1.00 3.63  ? 117 VAL A C     1 
ATOM   879  O O     . VAL A 1 137 ? 16.563  -0.966  -18.409 1.00 4.34  ? 117 VAL A O     1 
ATOM   880  C CB    . VAL A 1 137 ? 14.897  1.322   -19.486 1.00 4.79  ? 117 VAL A CB    1 
ATOM   881  C CG1   . VAL A 1 137 ? 14.822  0.765   -20.884 1.00 6.45  ? 117 VAL A CG1   1 
ATOM   882  C CG2   . VAL A 1 137 ? 13.995  2.549   -19.353 1.00 5.20  ? 117 VAL A CG2   1 
ATOM   883  N N     . THR A 1 138 ? 14.735  -2.043  -19.161 1.00 3.01  ? 118 THR A N     1 
ATOM   884  C CA    . THR A 1 138 ? 15.444  -3.235  -19.599 1.00 3.03  ? 118 THR A CA    1 
ATOM   885  C C     . THR A 1 138 ? 15.581  -3.169  -21.111 1.00 2.50  ? 118 THR A C     1 
ATOM   886  O O     . THR A 1 138 ? 14.570  -2.997  -21.809 1.00 2.26  ? 118 THR A O     1 
ATOM   887  C CB    . THR A 1 138 ? 14.536  -4.426  -19.292 1.00 3.74  ? 118 THR A CB    1 
ATOM   888  O OG1   . THR A 1 138 ? 14.163  -4.509  -17.890 1.00 5.64  ? 118 THR A OG1   1 
ATOM   889  C CG2   . THR A 1 138 ? 15.183  -5.719  -19.683 1.00 4.47  ? 118 THR A CG2   1 
ATOM   890  N N     . LEU A 1 139 ? 16.777  -3.341  -21.672 1.00 2.17  ? 119 LEU A N     1 
ATOM   891  C CA    . LEU A 1 139 ? 16.940  -3.286  -23.119 1.00 2.27  ? 119 LEU A CA    1 
ATOM   892  C C     . LEU A 1 139 ? 16.475  -4.562  -23.808 1.00 2.12  ? 119 LEU A C     1 
ATOM   893  O O     . LEU A 1 139 ? 15.945  -4.495  -24.921 1.00 1.95  ? 119 LEU A O     1 
ATOM   894  C CB    . LEU A 1 139 ? 18.398  -2.999  -23.473 1.00 2.57  ? 119 LEU A CB    1 
ATOM   895  C CG    . LEU A 1 139 ? 18.761  -1.555  -23.237 1.00 3.05  ? 119 LEU A CG    1 
ATOM   896  C CD1   . LEU A 1 139 ? 20.248  -1.361  -23.156 1.00 3.27  ? 119 LEU A CD1   1 
ATOM   897  C CD2   . LEU A 1 139 ? 18.200  -0.640  -24.331 1.00 3.46  ? 119 LEU A CD2   1 
ATOM   898  N N     . TYR A 1 140 ? 16.676  -5.716  -23.202 1.00 1.94  ? 120 TYR A N     1 
ATOM   899  C CA    . TYR A 1 140 ? 16.374  -6.985  -23.842 1.00 1.92  ? 120 TYR A CA    1 
ATOM   900  C C     . TYR A 1 140 ? 15.589  -7.895  -22.900 1.00 1.88  ? 120 TYR A C     1 
ATOM   901  O O     . TYR A 1 140 ? 16.155  -8.471  -21.979 1.00 1.78  ? 120 TYR A O     1 
ATOM   902  C CB    . TYR A 1 140 ? 17.624  -7.712  -24.301 1.00 1.96  ? 120 TYR A CB    1 
ATOM   903  C CG    . TYR A 1 140 ? 17.311  -8.987  -25.025 1.00 1.95  ? 120 TYR A CG    1 
ATOM   904  C CD1   . TYR A 1 140 ? 16.857  -8.896  -26.339 1.00 1.94  ? 120 TYR A CD1   1 
ATOM   905  C CD2   . TYR A 1 140 ? 17.430  -10.256 -24.474 1.00 1.98  ? 120 TYR A CD2   1 
ATOM   906  C CE1   . TYR A 1 140 ? 16.564  -10.013 -27.093 1.00 2.08  ? 120 TYR A CE1   1 
ATOM   907  C CE2   . TYR A 1 140 ? 17.147  -11.386 -25.228 1.00 1.97  ? 120 TYR A CE2   1 
ATOM   908  C CZ    . TYR A 1 140 ? 16.710  -11.266 -26.527 1.00 2.08  ? 120 TYR A CZ    1 
ATOM   909  O OH    . TYR A 1 140 ? 16.379  -12.390 -27.251 1.00 2.45  ? 120 TYR A OH    1 
ATOM   910  N N     . HIS A 1 141 ? 14.301  -8.088  -23.204 1.00 1.77  ? 121 HIS A N     1 
ATOM   911  C CA    . HIS A 1 141 ? 13.463  -9.051  -22.506 1.00 1.75  ? 121 HIS A CA    1 
ATOM   912  C C     . HIS A 1 141 ? 12.872  -9.980  -23.549 1.00 1.96  ? 121 HIS A C     1 
ATOM   913  O O     . HIS A 1 141 ? 11.647  -10.132 -23.638 1.00 2.04  ? 121 HIS A O     1 
ATOM   914  C CB    . HIS A 1 141 ? 12.454  -8.359  -21.601 1.00 1.64  ? 121 HIS A CB    1 
ATOM   915  C CG    . HIS A 1 141 ? 11.903  -9.172  -20.501 1.00 1.57  ? 121 HIS A CG    1 
ATOM   916  N ND1   . HIS A 1 141 ? 11.733  -8.607  -19.239 1.00 1.49  ? 121 HIS A ND1   1 
ATOM   917  C CD2   . HIS A 1 141 ? 11.392  -10.436 -20.463 1.00 1.58  ? 121 HIS A CD2   1 
ATOM   918  C CE1   . HIS A 1 141 ? 11.133  -9.525  -18.485 1.00 1.55  ? 121 HIS A CE1   1 
ATOM   919  N NE2   . HIS A 1 141 ? 10.920  -10.634 -19.181 1.00 1.58  ? 121 HIS A NE2   1 
ATOM   920  N N     . TRP A 1 142 ? 13.770  -10.547 -24.374 1.00 1.96  ? 122 TRP A N     1 
ATOM   921  C CA    . TRP A 1 142 ? 13.567  -11.796 -25.111 1.00 2.04  ? 122 TRP A CA    1 
ATOM   922  C C     . TRP A 1 142 ? 13.070  -11.637 -26.556 1.00 2.36  ? 122 TRP A C     1 
ATOM   923  O O     . TRP A 1 142 ? 13.035  -12.647 -27.270 1.00 2.47  ? 122 TRP A O     1 
ATOM   924  C CB    . TRP A 1 142 ? 12.670  -12.793 -24.366 1.00 1.93  ? 122 TRP A CB    1 
ATOM   925  C CG    . TRP A 1 142 ? 13.132  -13.114 -22.967 1.00 1.86  ? 122 TRP A CG    1 
ATOM   926  C CD1   . TRP A 1 142 ? 14.239  -12.701 -22.290 1.00 1.88  ? 122 TRP A CD1   1 
ATOM   927  C CD2   . TRP A 1 142 ? 12.382  -13.944 -22.083 1.00 1.90  ? 122 TRP A CD2   1 
ATOM   928  N NE1   . TRP A 1 142 ? 14.205  -13.243 -21.038 1.00 1.89  ? 122 TRP A NE1   1 
ATOM   929  C CE2   . TRP A 1 142 ? 13.086  -14.007 -20.868 1.00 1.89  ? 122 TRP A CE2   1 
ATOM   930  C CE3   . TRP A 1 142 ? 11.162  -14.619 -22.206 1.00 1.83  ? 122 TRP A CE3   1 
ATOM   931  C CZ2   . TRP A 1 142 ? 12.620  -14.759 -19.800 1.00 1.92  ? 122 TRP A CZ2   1 
ATOM   932  C CZ3   . TRP A 1 142 ? 10.723  -15.384 -21.153 1.00 1.95  ? 122 TRP A CZ3   1 
ATOM   933  C CH2   . TRP A 1 142 ? 11.447  -15.457 -19.971 1.00 2.04  ? 122 TRP A CH2   1 
ATOM   934  N N     . ASP A 1 143 ? 12.799  -10.431 -26.985 1.00 2.71  ? 123 ASP A N     1 
ATOM   935  C CA    . ASP A 1 143 ? 12.175  -10.171 -28.283 1.00 2.94  ? 123 ASP A CA    1 
ATOM   936  C C     . ASP A 1 143 ? 13.249  -9.858  -29.322 1.00 2.70  ? 123 ASP A C     1 
ATOM   937  O O     . ASP A 1 143 ? 13.244  -8.844  -29.999 1.00 3.35  ? 123 ASP A O     1 
ATOM   938  C CB    . ASP A 1 143 ? 11.151  -9.051  -28.158 1.00 3.55  ? 123 ASP A CB    1 
ATOM   939  C CG    . ASP A 1 143 ? 11.526  -7.845  -27.325 1.00 4.61  ? 123 ASP A CG    1 
ATOM   940  O OD1   . ASP A 1 143 ? 12.492  -7.886  -26.626 1.00 5.24  ? 123 ASP A OD1   1 
ATOM   941  O OD2   . ASP A 1 143 ? 10.731  -6.910  -27.332 1.00 7.18  ? 123 ASP A OD2   1 
ATOM   942  N N     . LEU A 1 144 ? 14.116  -10.836 -29.563 1.00 2.24  ? 124 LEU A N     1 
ATOM   943  C CA    . LEU A 1 144 ? 15.160  -10.724 -30.577 1.00 2.17  ? 124 LEU A CA    1 
ATOM   944  C C     . LEU A 1 144 ? 14.527  -10.521 -31.944 1.00 2.09  ? 124 LEU A C     1 
ATOM   945  O O     . LEU A 1 144 ? 13.627  -11.269 -32.312 1.00 2.03  ? 124 LEU A O     1 
ATOM   946  C CB    . LEU A 1 144 ? 15.956  -12.017 -30.621 1.00 2.12  ? 124 LEU A CB    1 
ATOM   947  C CG    . LEU A 1 144 ? 17.164  -11.993 -31.557 1.00 2.17  ? 124 LEU A CG    1 
ATOM   948  C CD1   . LEU A 1 144 ? 18.277  -11.067 -31.093 1.00 2.22  ? 124 LEU A CD1   1 
ATOM   949  C CD2   . LEU A 1 144 ? 17.713  -13.413 -31.705 1.00 2.32  ? 124 LEU A CD2   1 
ATOM   950  N N     . PRO A 1 145 ? 14.962  -9.537  -32.744 1.00 2.08  ? 125 PRO A N     1 
ATOM   951  C CA    . PRO A 1 145 ? 14.477  -9.422  -34.123 1.00 2.23  ? 125 PRO A CA    1 
ATOM   952  C C     . PRO A 1 145 ? 14.698  -10.707 -34.901 1.00 2.52  ? 125 PRO A C     1 
ATOM   953  O O     . PRO A 1 145 ? 15.780  -11.269 -34.898 1.00 2.40  ? 125 PRO A O     1 
ATOM   954  C CB    . PRO A 1 145 ? 15.319  -8.249  -34.654 1.00 2.27  ? 125 PRO A CB    1 
ATOM   955  C CG    . PRO A 1 145 ? 15.426  -7.380  -33.416 1.00 2.24  ? 125 PRO A CG    1 
ATOM   956  C CD    . PRO A 1 145 ? 15.747  -8.373  -32.329 1.00 2.16  ? 125 PRO A CD    1 
ATOM   957  N N     . GLN A 1 146 ? 13.647  -11.152 -35.614 1.00 2.52  ? 126 GLN A N     1 
ATOM   958  C CA    . GLN A 1 146 ? 13.727  -12.432 -36.340 1.00 2.75  ? 126 GLN A CA    1 
ATOM   959  C C     . GLN A 1 146 ? 14.811  -12.426 -37.406 1.00 2.71  ? 126 GLN A C     1 
ATOM   960  O O     . GLN A 1 146 ? 15.470  -13.467 -37.563 1.00 2.51  ? 126 GLN A O     1 
ATOM   961  C CB    . GLN A 1 146 ? 12.364  -12.744 -36.941 1.00 3.05  ? 126 GLN A CB    1 
ATOM   962  C CG    . GLN A 1 146 ? 12.342  -14.009 -37.785 1.00 3.44  ? 126 GLN A CG    1 
ATOM   963  C CD    . GLN A 1 146 ? 12.496  -15.265 -36.971 1.00 3.82  ? 126 GLN A CD    1 
ATOM   964  O OE1   . GLN A 1 146 ? 11.844  -15.400 -35.925 1.00 4.06  ? 126 GLN A OE1   1 
ATOM   965  N NE2   . GLN A 1 146 ? 13.405  -16.162 -37.338 1.00 4.18  ? 126 GLN A NE2   1 
ATOM   966  N N     . PRO A 1 147 ? 15.101  -11.303 -38.116 1.00 2.95  ? 127 PRO A N     1 
ATOM   967  C CA    . PRO A 1 147 ? 16.214  -11.342 -39.054 1.00 3.20  ? 127 PRO A CA    1 
ATOM   968  C C     . PRO A 1 147 ? 17.531  -11.772 -38.442 1.00 3.54  ? 127 PRO A C     1 
ATOM   969  O O     . PRO A 1 147 ? 18.394  -12.363 -39.112 1.00 4.82  ? 127 PRO A O     1 
ATOM   970  C CB    . PRO A 1 147 ? 16.195  -9.936  -39.659 1.00 3.22  ? 127 PRO A CB    1 
ATOM   971  C CG    . PRO A 1 147 ? 14.788  -9.510  -39.580 1.00 3.31  ? 127 PRO A CG    1 
ATOM   972  C CD    . PRO A 1 147 ? 14.333  -10.056 -38.232 1.00 3.19  ? 127 PRO A CD    1 
ATOM   973  N N     . LEU A 1 148 ? 17.779  -11.443 -37.163 1.00 3.37  ? 128 LEU A N     1 
ATOM   974  C CA    . LEU A 1 148 ? 19.006  -11.882 -36.534 1.00 3.34  ? 128 LEU A CA    1 
ATOM   975  C C     . LEU A 1 148 ? 18.967  -13.377 -36.262 1.00 3.51  ? 128 LEU A C     1 
ATOM   976  O O     . LEU A 1 148 ? 19.984  -14.072 -36.379 1.00 3.69  ? 128 LEU A O     1 
ATOM   977  C CB    . LEU A 1 148 ? 19.272  -11.112 -35.238 1.00 3.40  ? 128 LEU A CB    1 
ATOM   978  C CG    . LEU A 1 148 ? 19.383  -9.605  -35.405 1.00 3.67  ? 128 LEU A CG    1 
ATOM   979  C CD1   . LEU A 1 148 ? 19.614  -8.888  -34.082 1.00 3.78  ? 128 LEU A CD1   1 
ATOM   980  C CD2   . LEU A 1 148 ? 20.433  -9.219  -36.427 1.00 4.02  ? 128 LEU A CD2   1 
ATOM   981  N N     . GLU A 1 149 ? 17.817  -13.894 -35.823 1.00 3.72  ? 129 GLU A N     1 
ATOM   982  C CA    . GLU A 1 149 ? 17.680  -15.338 -35.650 1.00 4.39  ? 129 GLU A CA    1 
ATOM   983  C C     . GLU A 1 149 ? 17.846  -16.103 -36.957 1.00 5.27  ? 129 GLU A C     1 
ATOM   984  O O     . GLU A 1 149 ? 18.429  -17.200 -36.918 1.00 5.21  ? 129 GLU A O     1 
ATOM   985  C CB    . GLU A 1 149 ? 16.357  -15.657 -34.974 1.00 4.34  ? 129 GLU A CB    1 
ATOM   986  C CG    . GLU A 1 149 ? 16.113  -17.163 -34.744 1.00 4.61  ? 129 GLU A CG    1 
ATOM   987  C CD    . GLU A 1 149 ? 17.152  -17.800 -33.821 1.00 5.51  ? 129 GLU A CD    1 
ATOM   988  O OE1   . GLU A 1 149 ? 17.696  -17.103 -32.984 1.00 6.58  ? 129 GLU A OE1   1 
ATOM   989  O OE2   . GLU A 1 149 ? 17.354  -19.041 -33.927 1.00 7.21  ? 129 GLU A OE2   1 
ATOM   990  N N     . ASP A 1 150 ? 17.466  -15.500 -38.070 1.00 5.55  ? 130 ASP A N     1 
ATOM   991  C CA    . ASP A 1 150 ? 17.704  -16.137 -39.371 1.00 6.23  ? 130 ASP A CA    1 
ATOM   992  C C     . ASP A 1 150 ? 19.194  -16.261 -39.667 1.00 7.48  ? 130 ASP A C     1 
ATOM   993  O O     . ASP A 1 150 ? 19.568  -17.070 -40.537 1.00 8.90  ? 130 ASP A O     1 
ATOM   994  C CB    . ASP A 1 150 ? 16.998  -15.376 -40.479 1.00 7.05  ? 130 ASP A CB    1 
ATOM   995  C CG    . ASP A 1 150 ? 15.487  -15.323 -40.407 1.00 8.83  ? 130 ASP A CG    1 
ATOM   996  O OD1   . ASP A 1 150 ? 14.882  -16.210 -39.798 1.00 10.08 ? 130 ASP A OD1   1 
ATOM   997  O OD2   . ASP A 1 150 ? 14.946  -14.388 -41.057 1.00 12.85 ? 130 ASP A OD2   1 
ATOM   998  N N     . ARG A 1 151 ? 20.032  -15.470 -38.990 1.00 7.12  ? 131 ARG A N     1 
ATOM   999  C CA    . ARG A 1 151 ? 21.491  -15.566 -39.066 1.00 7.97  ? 131 ARG A CA    1 
ATOM   1000 C C     . ARG A 1 151 ? 22.096  -16.145 -37.776 1.00 7.93  ? 131 ARG A C     1 
ATOM   1001 O O     . ARG A 1 151 ? 23.174  -15.733 -37.384 1.00 9.19  ? 131 ARG A O     1 
ATOM   1002 C CB    . ARG A 1 151 ? 22.067  -14.182 -39.380 1.00 9.98  ? 131 ARG A CB    1 
ATOM   1003 C CG    . ARG A 1 151 ? 21.509  -13.541 -40.632 1.00 12.79 ? 131 ARG A CG    1 
ATOM   1004 C CD    . ARG A 1 151 ? 21.578  -12.009 -40.666 1.00 18.31 ? 131 ARG A CD    1 
ATOM   1005 N NE    . ARG A 1 151 ? 21.145  -11.482 -41.970 1.00 23.07 ? 131 ARG A NE    1 
ATOM   1006 C CZ    . ARG A 1 151 ? 19.919  -11.551 -42.529 1.00 26.20 ? 131 ARG A CZ    1 
ATOM   1007 N NH1   . ARG A 1 151 ? 18.846  -12.038 -41.888 1.00 21.52 ? 131 ARG A NH1   1 
ATOM   1008 N NH2   . ARG A 1 151 ? 19.780  -11.100 -43.771 1.00 29.92 ? 131 ARG A NH2   1 
ATOM   1009 N N     . LEU A 1 152 ? 21.361  -17.057 -37.142 1.00 7.48  ? 132 LEU A N     1 
ATOM   1010 C CA    . LEU A 1 152 ? 21.752  -17.884 -35.996 1.00 7.33  ? 132 LEU A CA    1 
ATOM   1011 C C     . LEU A 1 152 ? 21.455  -17.229 -34.651 1.00 6.28  ? 132 LEU A C     1 
ATOM   1012 O O     . LEU A 1 152 ? 21.577  -17.895 -33.653 1.00 5.47  ? 132 LEU A O     1 
ATOM   1013 C CB    . LEU A 1 152 ? 23.211  -18.356 -36.024 1.00 9.88  ? 132 LEU A CB    1 
ATOM   1014 C CG    . LEU A 1 152 ? 23.598  -19.160 -37.259 1.00 14.03 ? 132 LEU A CG    1 
ATOM   1015 C CD1   . LEU A 1 152 ? 25.037  -19.606 -37.147 1.00 15.81 ? 132 LEU A CD1   1 
ATOM   1016 C CD2   . LEU A 1 152 ? 22.693  -20.348 -37.484 1.00 15.83 ? 132 LEU A CD2   1 
ATOM   1017 N N     . GLY A 1 153 ? 20.957  -15.992 -34.635 1.00 5.06  ? 133 GLY A N     1 
ATOM   1018 C CA    . GLY A 1 153 ? 20.508  -15.408 -33.379 1.00 4.45  ? 133 GLY A CA    1 
ATOM   1019 C C     . GLY A 1 153 ? 21.630  -15.375 -32.349 1.00 4.03  ? 133 GLY A C     1 
ATOM   1020 O O     . GLY A 1 153 ? 22.730  -14.982 -32.667 1.00 3.76  ? 133 GLY A O     1 
ATOM   1021 N N     . TRP A 1 154 ? 21.323  -15.771 -31.134 1.00 3.71  ? 134 TRP A N     1 
ATOM   1022 C CA    . TRP A 1 154 ? 22.339  -15.745 -30.086 1.00 3.82  ? 134 TRP A CA    1 
ATOM   1023 C C     . TRP A 1 154 ? 23.393  -16.816 -30.311 1.00 4.82  ? 134 TRP A C     1 
ATOM   1024 O O     . TRP A 1 154 ? 24.396  -16.790 -29.602 1.00 5.11  ? 134 TRP A O     1 
ATOM   1025 C CB    . TRP A 1 154 ? 21.679  -15.811 -28.703 1.00 3.33  ? 134 TRP A CB    1 
ATOM   1026 C CG    . TRP A 1 154 ? 20.873  -14.585 -28.376 1.00 3.35  ? 134 TRP A CG    1 
ATOM   1027 C CD1   . TRP A 1 154 ? 19.513  -14.488 -28.308 1.00 3.44  ? 134 TRP A CD1   1 
ATOM   1028 C CD2   . TRP A 1 154 ? 21.393  -13.273 -28.139 1.00 3.42  ? 134 TRP A CD2   1 
ATOM   1029 N NE1   . TRP A 1 154 ? 19.164  -13.196 -27.987 1.00 3.28  ? 134 TRP A NE1   1 
ATOM   1030 C CE2   . TRP A 1 154 ? 20.287  -12.426 -27.865 1.00 3.34  ? 134 TRP A CE2   1 
ATOM   1031 C CE3   . TRP A 1 154 ? 22.682  -12.726 -28.033 1.00 3.67  ? 134 TRP A CE3   1 
ATOM   1032 C CZ2   . TRP A 1 154 ? 20.428  -11.058 -27.591 1.00 3.47  ? 134 TRP A CZ2   1 
ATOM   1033 C CZ3   . TRP A 1 154 ? 22.810  -11.381 -27.715 1.00 3.79  ? 134 TRP A CZ3   1 
ATOM   1034 C CH2   . TRP A 1 154 ? 21.706  -10.559 -27.515 1.00 3.40  ? 134 TRP A CH2   1 
ATOM   1035 N N     . GLY A 1 155 ? 23.235  -17.635 -31.338 1.00 5.53  ? 135 GLY A N     1 
ATOM   1036 C CA    . GLY A 1 155 ? 24.310  -18.527 -31.749 1.00 6.65  ? 135 GLY A CA    1 
ATOM   1037 C C     . GLY A 1 155 ? 25.446  -17.837 -32.477 1.00 8.41  ? 135 GLY A C     1 
ATOM   1038 O O     . GLY A 1 155 ? 26.465  -18.495 -32.767 1.00 8.95  ? 135 GLY A O     1 
ATOM   1039 N N     . SER A 1 156 ? 25.285  -16.566 -32.837 1.00 7.12  ? 136 SER A N     1 
ATOM   1040 C CA    . SER A 1 156 ? 26.279  -15.802 -33.583 1.00 7.62  ? 136 SER A CA    1 
ATOM   1041 C C     . SER A 1 156 ? 26.843  -14.656 -32.742 1.00 8.10  ? 136 SER A C     1 
ATOM   1042 O O     . SER A 1 156 ? 26.098  -13.842 -32.164 1.00 7.08  ? 136 SER A O     1 
ATOM   1043 C CB    . SER A 1 156 ? 25.670  -15.271 -34.855 1.00 8.31  ? 136 SER A CB    1 
ATOM   1044 O OG    . SER A 1 156 ? 26.576  -14.417 -35.558 1.00 10.44 ? 136 SER A OG    1 
ATOM   1045 N N     . ARG A 1 157 ? 28.169  -14.501 -32.735 1.00 8.25  ? 137 ARG A N     1 
ATOM   1046 C CA    . ARG A 1 157 ? 28.837  -13.389 -32.069 1.00 8.95  ? 137 ARG A CA    1 
ATOM   1047 C C     . ARG A 1 157 ? 28.348  -12.070 -32.644 1.00 8.57  ? 137 ARG A C     1 
ATOM   1048 O O     . ARG A 1 157 ? 28.344  -11.038 -31.975 1.00 7.31  ? 137 ARG A O     1 
ATOM   1049 C CB    . ARG A 1 157 ? 30.349  -13.489 -32.287 1.00 12.12 ? 137 ARG A CB    1 
ATOM   1050 C CG    . ARG A 1 157 ? 30.967  -14.693 -31.621 1.00 16.66 ? 137 ARG A CG    1 
ATOM   1051 C CD    . ARG A 1 157 ? 32.473  -14.623 -31.870 1.00 19.41 ? 137 ARG A CD    1 
ATOM   1052 N NE    . ARG A 1 157 ? 33.109  -13.447 -31.276 1.00 19.98 ? 137 ARG A NE    1 
ATOM   1053 C CZ    . ARG A 1 157 ? 33.647  -13.474 -30.055 1.00 16.29 ? 137 ARG A CZ    1 
ATOM   1054 N NH1   . ARG A 1 157 ? 33.482  -14.552 -29.323 1.00 16.76 ? 137 ARG A NH1   1 
ATOM   1055 N NH2   . ARG A 1 157 ? 34.285  -12.431 -29.583 1.00 18.26 ? 137 ARG A NH2   1 
ATOM   1056 N N     . ALA A 1 158 ? 27.959  -12.059 -33.912 1.00 7.29  ? 138 ALA A N     1 
ATOM   1057 C CA    . ALA A 1 158 ? 27.566  -10.809 -34.546 1.00 7.19  ? 138 ALA A CA    1 
ATOM   1058 C C     . ALA A 1 158 ? 26.291  -10.267 -33.902 1.00 6.00  ? 138 ALA A C     1 
ATOM   1059 O O     . ALA A 1 158 ? 26.070  -9.049  -33.942 1.00 6.24  ? 138 ALA A O     1 
ATOM   1060 C CB    . ALA A 1 158 ? 27.345  -10.969 -36.003 1.00 8.48  ? 138 ALA A CB    1 
ATOM   1061 N N     . THR A 1 159 ? 25.477  -11.148 -33.313 1.00 5.15  ? 139 THR A N     1 
ATOM   1062 C CA    . THR A 1 159 ? 24.277  -10.668 -32.626 1.00 4.43  ? 139 THR A CA    1 
ATOM   1063 C C     . THR A 1 159 ? 24.665  -9.843  -31.396 1.00 4.31  ? 139 THR A C     1 
ATOM   1064 O O     . THR A 1 159 ? 24.037  -8.829  -31.075 1.00 3.71  ? 139 THR A O     1 
ATOM   1065 C CB    . THR A 1 159 ? 23.341  -11.821 -32.299 1.00 4.05  ? 139 THR A CB    1 
ATOM   1066 O OG1   . THR A 1 159 ? 22.997  -12.405 -33.538 1.00 4.49  ? 139 THR A OG1   1 
ATOM   1067 C CG2   . THR A 1 159 ? 22.112  -11.422 -31.508 1.00 3.85  ? 139 THR A CG2   1 
ATOM   1068 N N     . ALA A 1 160 ? 25.710  -10.260 -30.697 1.00 4.30  ? 140 ALA A N     1 
ATOM   1069 C CA    . ALA A 1 160 ? 26.244  -9.476  -29.594 1.00 4.38  ? 140 ALA A CA    1 
ATOM   1070 C C     . ALA A 1 160 ? 26.688  -8.080  -30.018 1.00 4.69  ? 140 ALA A C     1 
ATOM   1071 O O     . ALA A 1 160 ? 26.400  -7.106  -29.317 1.00 4.97  ? 140 ALA A O     1 
ATOM   1072 C CB    . ALA A 1 160 ? 27.345  -10.260 -28.912 1.00 4.57  ? 140 ALA A CB    1 
ATOM   1073 N N     . THR A 1 161 ? 27.356  -7.961  -31.168 1.00 5.54  ? 141 THR A N     1 
ATOM   1074 C CA    . THR A 1 161 ? 27.855  -6.685  -31.623 1.00 6.23  ? 141 THR A CA    1 
ATOM   1075 C C     . THR A 1 161 ? 26.677  -5.759  -31.895 1.00 5.13  ? 141 THR A C     1 
ATOM   1076 O O     . THR A 1 161 ? 26.688  -4.595  -31.545 1.00 5.48  ? 141 THR A O     1 
ATOM   1077 C CB    . THR A 1 161 ? 28.699  -6.851  -32.896 1.00 8.84  ? 141 THR A CB    1 
ATOM   1078 O OG1   . THR A 1 161 ? 29.806  -7.637  -32.434 1.00 12.98 ? 141 THR A OG1   1 
ATOM   1079 C CG2   . THR A 1 161 ? 29.114  -5.533  -33.508 1.00 10.58 ? 141 THR A CG2   1 
ATOM   1080 N N     . VAL A 1 162 ? 25.643  -6.292  -32.546 1.00 4.00  ? 142 VAL A N     1 
ATOM   1081 C CA    . VAL A 1 162 ? 24.530  -5.435  -32.967 1.00 4.02  ? 142 VAL A CA    1 
ATOM   1082 C C     . VAL A 1 162 ? 23.601  -5.191  -31.776 1.00 3.45  ? 142 VAL A C     1 
ATOM   1083 O O     . VAL A 1 162 ? 22.943  -4.161  -31.751 1.00 3.09  ? 142 VAL A O     1 
ATOM   1084 C CB    . VAL A 1 162 ? 23.774  -5.884  -34.228 1.00 4.96  ? 142 VAL A CB    1 
ATOM   1085 C CG1   . VAL A 1 162 ? 24.752  -5.936  -35.417 1.00 6.01  ? 142 VAL A CG1   1 
ATOM   1086 C CG2   . VAL A 1 162 ? 23.076  -7.201  -34.046 1.00 5.36  ? 142 VAL A CG2   1 
ATOM   1087 N N     . PHE A 1 163 ? 23.594  -6.075  -30.780 1.00 3.05  ? 143 PHE A N     1 
ATOM   1088 C CA    . PHE A 1 163 ? 22.884  -5.735  -29.531 1.00 2.81  ? 143 PHE A CA    1 
ATOM   1089 C C     . PHE A 1 163 ? 23.519  -4.474  -28.941 1.00 2.82  ? 143 PHE A C     1 
ATOM   1090 O O     . PHE A 1 163 ? 22.850  -3.550  -28.471 1.00 2.60  ? 143 PHE A O     1 
ATOM   1091 C CB    . PHE A 1 163 ? 22.897  -6.914  -28.574 1.00 2.86  ? 143 PHE A CB    1 
ATOM   1092 C CG    . PHE A 1 163 ? 22.333  -6.565  -27.228 1.00 2.72  ? 143 PHE A CG    1 
ATOM   1093 C CD1   . PHE A 1 163 ? 20.985  -6.244  -27.093 1.00 2.71  ? 143 PHE A CD1   1 
ATOM   1094 C CD2   . PHE A 1 163 ? 23.141  -6.462  -26.104 1.00 2.68  ? 143 PHE A CD2   1 
ATOM   1095 C CE1   . PHE A 1 163 ? 20.481  -5.838  -25.870 1.00 2.72  ? 143 PHE A CE1   1 
ATOM   1096 C CE2   . PHE A 1 163 ? 22.605  -6.059  -24.900 1.00 2.86  ? 143 PHE A CE2   1 
ATOM   1097 C CZ    . PHE A 1 163 ? 21.281  -5.753  -24.781 1.00 2.93  ? 143 PHE A CZ    1 
ATOM   1098 N N     . ALA A 1 164 ? 24.883  -4.429  -28.893 1.00 2.98  ? 144 ALA A N     1 
ATOM   1099 C CA    . ALA A 1 164 ? 25.530  -3.272  -28.318 1.00 3.19  ? 144 ALA A CA    1 
ATOM   1100 C C     . ALA A 1 164 ? 25.246  -1.976  -29.083 1.00 3.23  ? 144 ALA A C     1 
ATOM   1101 O O     . ALA A 1 164 ? 25.140  -0.903  -28.463 1.00 3.41  ? 144 ALA A O     1 
ATOM   1102 C CB    . ALA A 1 164 ? 27.017  -3.546  -28.171 1.00 3.32  ? 144 ALA A CB    1 
ATOM   1103 N N     . GLU A 1 165 ? 25.084  -2.078  -30.406 1.00 3.11  ? 145 GLU A N     1 
ATOM   1104 C CA    . GLU A 1 165 ? 24.716  -0.929  -31.202 1.00 3.45  ? 145 GLU A CA    1 
ATOM   1105 C C     . GLU A 1 165 ? 23.300  -0.459  -30.851 1.00 3.02  ? 145 GLU A C     1 
ATOM   1106 O O     . GLU A 1 165 ? 23.046  0.733   -30.717 1.00 3.30  ? 145 GLU A O     1 
ATOM   1107 C CB    . GLU A 1 165 ? 24.831  -1.292  -32.671 1.00 4.54  ? 145 GLU A CB    1 
ATOM   1108 C CG    . GLU A 1 165 ? 26.246  -1.531  -33.155 1.00 5.45  ? 145 GLU A CG    1 
ATOM   1109 C CD    . GLU A 1 165 ? 26.283  -2.005  -34.588 1.00 7.55  ? 145 GLU A CD    1 
ATOM   1110 O OE1   . GLU A 1 165 ? 25.259  -2.243  -35.231 1.00 7.31  ? 145 GLU A OE1   1 
ATOM   1111 O OE2   . GLU A 1 165 ? 27.452  -2.257  -35.033 1.00 8.61  ? 145 GLU A OE2   1 
ATOM   1112 N N     . TYR A 1 166 ? 22.365  -1.413  -30.717 1.00 2.49  ? 146 TYR A N     1 
ATOM   1113 C CA    . TYR A 1 166 ? 21.007  -1.071  -30.271 1.00 2.40  ? 146 TYR A CA    1 
ATOM   1114 C C     . TYR A 1 166 ? 21.017  -0.372  -28.923 1.00 2.34  ? 146 TYR A C     1 
ATOM   1115 O O     . TYR A 1 166 ? 20.326  0.610   -28.720 1.00 2.17  ? 146 TYR A O     1 
ATOM   1116 C CB    . TYR A 1 166 ? 20.196  -2.349  -30.289 1.00 2.23  ? 146 TYR A CB    1 
ATOM   1117 C CG    . TYR A 1 166 ? 18.984  -2.392  -29.377 1.00 2.00  ? 146 TYR A CG    1 
ATOM   1118 C CD1   . TYR A 1 166 ? 17.864  -1.604  -29.575 1.00 1.96  ? 146 TYR A CD1   1 
ATOM   1119 C CD2   . TYR A 1 166 ? 18.949  -3.295  -28.319 1.00 1.94  ? 146 TYR A CD2   1 
ATOM   1120 C CE1   . TYR A 1 166 ? 16.796  -1.636  -28.706 1.00 1.86  ? 146 TYR A CE1   1 
ATOM   1121 C CE2   . TYR A 1 166 ? 17.857  -3.394  -27.484 1.00 1.87  ? 146 TYR A CE2   1 
ATOM   1122 C CZ    . TYR A 1 166 ? 16.774  -2.568  -27.689 1.00 1.84  ? 146 TYR A CZ    1 
ATOM   1123 O OH    . TYR A 1 166 ? 15.647  -2.577  -26.884 1.00 2.03  ? 146 TYR A OH    1 
ATOM   1124 N N     . ALA A 1 167 ? 21.837  -0.851  -27.991 1.00 2.28  ? 147 ALA A N     1 
ATOM   1125 C CA    . ALA A 1 167 ? 21.910  -0.258  -26.665 1.00 2.51  ? 147 ALA A CA    1 
ATOM   1126 C C     . ALA A 1 167 ? 22.412  1.184   -26.741 1.00 3.01  ? 147 ALA A C     1 
ATOM   1127 O O     . ALA A 1 167 ? 21.853  2.087   -26.124 1.00 3.03  ? 147 ALA A O     1 
ATOM   1128 C CB    . ALA A 1 167 ? 22.820  -1.094  -25.820 1.00 2.54  ? 147 ALA A CB    1 
ATOM   1129 N N     . ASP A 1 168 ? 23.403  1.434   -27.607 1.00 3.46  ? 148 ASP A N     1 
ATOM   1130 C CA    . ASP A 1 168 ? 23.910  2.780   -27.870 1.00 4.01  ? 148 ASP A CA    1 
ATOM   1131 C C     . ASP A 1 168 ? 22.800  3.688   -28.376 1.00 3.87  ? 148 ASP A C     1 
ATOM   1132 O O     . ASP A 1 168 ? 22.561  4.758   -27.791 1.00 4.18  ? 148 ASP A O     1 
ATOM   1133 C CB    . ASP A 1 168 ? 25.089  2.603   -28.837 1.00 4.76  ? 148 ASP A CB    1 
ATOM   1134 C CG    . ASP A 1 168 ? 25.619  3.867   -29.489 1.00 6.32  ? 148 ASP A CG    1 
ATOM   1135 O OD1   . ASP A 1 168 ? 24.829  4.794   -29.826 1.00 7.06  ? 148 ASP A OD1   1 
ATOM   1136 O OD2   . ASP A 1 168 ? 26.853  3.841   -29.745 1.00 9.34  ? 148 ASP A OD2   1 
ATOM   1137 N N     . ILE A 1 169 ? 22.031  3.213   -29.359 1.00 3.57  ? 149 ILE A N     1 
ATOM   1138 C CA    . ILE A 1 169 ? 20.994  4.005   -29.992 1.00 3.60  ? 149 ILE A CA    1 
ATOM   1139 C C     . ILE A 1 169 ? 19.968  4.432   -28.933 1.00 3.49  ? 149 ILE A C     1 
ATOM   1140 O O     . ILE A 1 169 ? 19.505  5.573   -28.902 1.00 3.30  ? 149 ILE A O     1 
ATOM   1141 C CB    . ILE A 1 169 ? 20.348  3.189   -31.124 1.00 4.08  ? 149 ILE A CB    1 
ATOM   1142 C CG1   . ILE A 1 169 ? 21.299  3.016   -32.325 1.00 4.64  ? 149 ILE A CG1   1 
ATOM   1143 C CG2   . ILE A 1 169 ? 19.009  3.789   -31.503 1.00 4.25  ? 149 ILE A CG2   1 
ATOM   1144 C CD1   . ILE A 1 169 ? 20.954  1.865   -33.192 1.00 5.01  ? 149 ILE A CD1   1 
ATOM   1145 N N     . VAL A 1 170 ? 19.544  3.495   -28.093 1.00 3.13  ? 150 VAL A N     1 
ATOM   1146 C CA    . VAL A 1 170 ? 18.487  3.841   -27.149 1.00 3.01  ? 150 VAL A CA    1 
ATOM   1147 C C     . VAL A 1 170 ? 18.996  4.794   -26.085 1.00 3.33  ? 150 VAL A C     1 
ATOM   1148 O O     . VAL A 1 170 ? 18.289  5.745   -25.757 1.00 3.12  ? 150 VAL A O     1 
ATOM   1149 C CB    . VAL A 1 170 ? 17.908  2.555   -26.531 1.00 2.68  ? 150 VAL A CB    1 
ATOM   1150 C CG1   . VAL A 1 170 ? 16.837  2.868   -25.523 1.00 2.81  ? 150 VAL A CG1   1 
ATOM   1151 C CG2   . VAL A 1 170 ? 17.324  1.637   -27.587 1.00 2.60  ? 150 VAL A CG2   1 
ATOM   1152 N N     . VAL A 1 171 ? 20.182  4.577   -25.536 1.00 3.75  ? 151 VAL A N     1 
ATOM   1153 C CA    . VAL A 1 171 ? 20.720  5.452   -24.514 1.00 4.98  ? 151 VAL A CA    1 
ATOM   1154 C C     . VAL A 1 171 ? 20.956  6.857   -25.052 1.00 5.20  ? 151 VAL A C     1 
ATOM   1155 O O     . VAL A 1 171 ? 20.828  7.827   -24.324 1.00 4.67  ? 151 VAL A O     1 
ATOM   1156 C CB    . VAL A 1 171 ? 22.016  4.878   -23.925 1.00 6.80  ? 151 VAL A CB    1 
ATOM   1157 C CG1   . VAL A 1 171 ? 22.924  5.941   -23.297 1.00 9.30  ? 151 VAL A CG1   1 
ATOM   1158 C CG2   . VAL A 1 171 ? 21.659  3.712   -23.036 1.00 7.04  ? 151 VAL A CG2   1 
ATOM   1159 N N     . ARG A 1 172 ? 21.326  6.975   -26.330 1.00 6.10  ? 152 ARG A N     1 
ATOM   1160 C CA    . ARG A 1 172 ? 21.520  8.310   -26.881 1.00 7.96  ? 152 ARG A CA    1 
ATOM   1161 C C     . ARG A 1 172 ? 20.240  9.128   -26.788 1.00 8.30  ? 152 ARG A C     1 
ATOM   1162 O O     . ARG A 1 172 ? 20.305  10.332  -26.589 1.00 11.41 ? 152 ARG A O     1 
ATOM   1163 C CB    . ARG A 1 172 ? 21.985  8.227   -28.333 1.00 10.12 ? 152 ARG A CB    1 
ATOM   1164 C CG    . ARG A 1 172 ? 23.440  7.874   -28.445 1.00 12.97 ? 152 ARG A CG    1 
ATOM   1165 C CD    . ARG A 1 172 ? 23.944  8.195   -29.829 1.00 13.50 ? 152 ARG A CD    1 
ATOM   1166 N NE    . ARG A 1 172 ? 25.217  7.567   -29.948 1.00 15.20 ? 152 ARG A NE    1 
ATOM   1167 C CZ    . ARG A 1 172 ? 26.358  8.074   -29.545 1.00 16.85 ? 152 ARG A CZ    1 
ATOM   1168 N NH1   . ARG A 1 172 ? 26.437  9.363   -29.243 1.00 19.37 ? 152 ARG A NH1   1 
ATOM   1169 N NH2   . ARG A 1 172 ? 27.403  7.271   -29.465 1.00 19.50 ? 152 ARG A NH2   1 
ATOM   1170 N N     . GLN A 1 173 ? 19.095  8.490   -26.992 1.00 7.02  ? 153 GLN A N     1 
ATOM   1171 C CA    . GLN A 1 173 ? 17.786  9.150   -27.047 1.00 7.69  ? 153 GLN A CA    1 
ATOM   1172 C C     . GLN A 1 173 ? 17.212  9.344   -25.637 1.00 6.61  ? 153 GLN A C     1 
ATOM   1173 O O     . GLN A 1 173 ? 16.636  10.396  -25.329 1.00 6.70  ? 153 GLN A O     1 
ATOM   1174 C CB    . GLN A 1 173 ? 16.824  8.264   -27.841 1.00 10.74 ? 153 GLN A CB    1 
ATOM   1175 C CG    . GLN A 1 173 ? 15.371  8.737   -27.868 1.00 14.07 ? 153 GLN A CG    1 
ATOM   1176 C CD    . GLN A 1 173 ? 15.092  9.602   -29.072 1.00 16.02 ? 153 GLN A CD    1 
ATOM   1177 O OE1   . GLN A 1 173 ? 15.684  9.470   -30.152 1.00 13.84 ? 153 GLN A OE1   1 
ATOM   1178 N NE2   . GLN A 1 173 ? 14.065  10.421  -28.915 1.00 18.94 ? 153 GLN A NE2   1 
ATOM   1179 N N     . LEU A 1 174 ? 17.356  8.351   -24.752 1.00 5.22  ? 154 LEU A N     1 
ATOM   1180 C CA    . LEU A 1 174 ? 16.657  8.340   -23.477 1.00 4.75  ? 154 LEU A CA    1 
ATOM   1181 C C     . LEU A 1 174 ? 17.541  8.562   -22.255 1.00 4.72  ? 154 LEU A C     1 
ATOM   1182 O O     . LEU A 1 174 ? 17.079  8.769   -21.138 1.00 4.47  ? 154 LEU A O     1 
ATOM   1183 C CB    . LEU A 1 174 ? 15.919  7.011   -23.292 1.00 4.75  ? 154 LEU A CB    1 
ATOM   1184 C CG    . LEU A 1 174 ? 14.856  6.625   -24.316 1.00 5.85  ? 154 LEU A CG    1 
ATOM   1185 C CD1   . LEU A 1 174 ? 14.224  5.295   -23.945 1.00 6.05  ? 154 LEU A CD1   1 
ATOM   1186 C CD2   . LEU A 1 174 ? 13.804  7.695   -24.525 1.00 7.54  ? 154 LEU A CD2   1 
ATOM   1187 N N     . GLY A 1 175 ? 18.856  8.518   -22.442 1.00 4.51  ? 155 GLY A N     1 
ATOM   1188 C CA    . GLY A 1 175 ? 19.795  8.552   -21.338 1.00 5.02  ? 155 GLY A CA    1 
ATOM   1189 C C     . GLY A 1 175 ? 19.949  9.909   -20.667 1.00 5.40  ? 155 GLY A C     1 
ATOM   1190 O O     . GLY A 1 175 ? 20.569  9.988   -19.611 1.00 6.24  ? 155 GLY A O     1 
ATOM   1191 N N     . ASP A 1 176 ? 19.303  10.930  -21.213 1.00 5.37  ? 156 ASP A N     1 
ATOM   1192 C CA    . ASP A 1 176 ? 19.261  12.220  -20.528 1.00 6.27  ? 156 ASP A CA    1 
ATOM   1193 C C     . ASP A 1 176 ? 18.248  12.201  -19.395 1.00 6.17  ? 156 ASP A C     1 
ATOM   1194 O O     . ASP A 1 176 ? 18.261  13.056  -18.507 1.00 7.65  ? 156 ASP A O     1 
ATOM   1195 C CB    . ASP A 1 176 ? 18.897  13.336  -21.490 1.00 7.35  ? 156 ASP A CB    1 
ATOM   1196 C CG    . ASP A 1 176 ? 17.544  13.210  -22.171 1.00 9.82  ? 156 ASP A CG    1 
ATOM   1197 O OD1   . ASP A 1 176 ? 17.088  12.060  -22.452 1.00 8.32  ? 156 ASP A OD1   1 
ATOM   1198 O OD2   . ASP A 1 176 ? 16.922  14.279  -22.493 1.00 18.22 ? 156 ASP A OD2   1 
ATOM   1199 N N     . ARG A 1 177 ? 17.342  11.219  -19.415 1.00 4.66  ? 157 ARG A N     1 
ATOM   1200 C CA    . ARG A 1 177 ? 16.234  11.125  -18.469 1.00 4.75  ? 157 ARG A CA    1 
ATOM   1201 C C     . ARG A 1 177 ? 16.206  9.842   -17.669 1.00 5.21  ? 157 ARG A C     1 
ATOM   1202 O O     . ARG A 1 177 ? 15.672  9.842   -16.572 1.00 6.54  ? 157 ARG A O     1 
ATOM   1203 C CB    . ARG A 1 177 ? 14.920  11.249  -19.243 1.00 4.68  ? 157 ARG A CB    1 
ATOM   1204 C CG    . ARG A 1 177 ? 14.634  12.681  -19.648 1.00 5.03  ? 157 ARG A CG    1 
ATOM   1205 C CD    . ARG A 1 177 ? 13.643  12.773  -20.785 1.00 5.30  ? 157 ARG A CD    1 
ATOM   1206 N NE    . ARG A 1 177 ? 14.186  12.191  -22.008 1.00 6.32  ? 157 ARG A NE    1 
ATOM   1207 C CZ    . ARG A 1 177 ? 13.497  11.771  -23.052 1.00 6.70  ? 157 ARG A CZ    1 
ATOM   1208 N NH1   . ARG A 1 177 ? 14.133  11.307  -24.123 1.00 7.66  ? 157 ARG A NH1   1 
ATOM   1209 N NH2   . ARG A 1 177 ? 12.186  11.857  -23.070 1.00 7.30  ? 157 ARG A NH2   1 
ATOM   1210 N N     . VAL A 1 178 ? 16.721  8.744   -18.214 1.00 4.18  ? 158 VAL A N     1 
ATOM   1211 C CA    . VAL A 1 178 ? 16.721  7.449   -17.556 1.00 4.19  ? 158 VAL A CA    1 
ATOM   1212 C C     . VAL A 1 178 ? 18.142  7.197   -17.051 1.00 4.25  ? 158 VAL A C     1 
ATOM   1213 O O     . VAL A 1 178 ? 19.053  7.130   -17.863 1.00 4.77  ? 158 VAL A O     1 
ATOM   1214 C CB    . VAL A 1 178 ? 16.315  6.346   -18.534 1.00 3.93  ? 158 VAL A CB    1 
ATOM   1215 C CG1   . VAL A 1 178 ? 16.422  4.972   -17.871 1.00 3.85  ? 158 VAL A CG1   1 
ATOM   1216 C CG2   . VAL A 1 178 ? 14.971  6.598   -19.178 1.00 3.95  ? 158 VAL A CG2   1 
ATOM   1217 N N     . THR A 1 179 ? 18.308  7.060   -15.747 1.00 4.60  ? 159 THR A N     1 
ATOM   1218 C CA    . THR A 1 179 ? 19.615  6.745   -15.177 1.00 4.92  ? 159 THR A CA    1 
ATOM   1219 C C     . THR A 1 179 ? 19.808  5.255   -14.996 1.00 4.99  ? 159 THR A C     1 
ATOM   1220 O O     . THR A 1 179 ? 20.930  4.777   -15.086 1.00 4.81  ? 159 THR A O     1 
ATOM   1221 C CB    . THR A 1 179 ? 19.803  7.388   -13.802 1.00 6.01  ? 159 THR A CB    1 
ATOM   1222 O OG1   . THR A 1 179 ? 18.707  7.109   -12.955 1.00 6.87  ? 159 THR A OG1   1 
ATOM   1223 C CG2   . THR A 1 179 ? 19.923  8.872   -13.916 1.00 7.65  ? 159 THR A CG2   1 
ATOM   1224 N N     . HIS A 1 180 ? 18.754  4.490   -14.752 1.00 4.02  ? 160 HIS A N     1 
ATOM   1225 C CA    . HIS A 1 180 ? 18.881  3.090   -14.374 1.00 3.91  ? 160 HIS A CA    1 
ATOM   1226 C C     . HIS A 1 180 ? 18.476  2.180   -15.520 1.00 3.70  ? 160 HIS A C     1 
ATOM   1227 O O     . HIS A 1 180 ? 17.308  2.132   -15.903 1.00 3.94  ? 160 HIS A O     1 
ATOM   1228 C CB    . HIS A 1 180 ? 18.105  2.736   -13.107 1.00 4.27  ? 160 HIS A CB    1 
ATOM   1229 C CG    . HIS A 1 180 ? 18.720  3.275   -11.867 1.00 4.76  ? 160 HIS A CG    1 
ATOM   1230 N ND1   . HIS A 1 180 ? 18.913  4.620   -11.681 1.00 6.12  ? 160 HIS A ND1   1 
ATOM   1231 C CD2   . HIS A 1 180 ? 19.329  2.632   -10.853 1.00 5.42  ? 160 HIS A CD2   1 
ATOM   1232 C CE1   . HIS A 1 180 ? 19.560  4.764   -10.498 1.00 5.92  ? 160 HIS A CE1   1 
ATOM   1233 N NE2   . HIS A 1 180 ? 19.826  3.568   -9.987  1.00 6.63  ? 160 HIS A NE2   1 
ATOM   1234 N N     . TRP A 1 181 ? 19.441  1.410   -15.998 1.00 3.12  ? 161 TRP A N     1 
ATOM   1235 C CA    . TRP A 1 181 ? 19.306  0.569   -17.169 1.00 3.14  ? 161 TRP A CA    1 
ATOM   1236 C C     . TRP A 1 181 ? 19.735  -0.845  -16.850 1.00 3.12  ? 161 TRP A C     1 
ATOM   1237 O O     . TRP A 1 181 ? 20.745  -1.043  -16.178 1.00 3.70  ? 161 TRP A O     1 
ATOM   1238 C CB    . TRP A 1 181 ? 20.197  1.051   -18.282 1.00 3.18  ? 161 TRP A CB    1 
ATOM   1239 C CG    . TRP A 1 181 ? 19.878  2.409   -18.792 1.00 3.43  ? 161 TRP A CG    1 
ATOM   1240 C CD1   . TRP A 1 181 ? 20.211  3.616   -18.248 1.00 3.70  ? 161 TRP A CD1   1 
ATOM   1241 C CD2   . TRP A 1 181 ? 19.120  2.685   -19.976 1.00 4.27  ? 161 TRP A CD2   1 
ATOM   1242 N NE1   . TRP A 1 181 ? 19.697  4.620   -19.035 1.00 3.94  ? 161 TRP A NE1   1 
ATOM   1243 C CE2   . TRP A 1 181 ? 19.046  4.086   -20.102 1.00 4.18  ? 161 TRP A CE2   1 
ATOM   1244 C CE3   . TRP A 1 181 ? 18.526  1.888   -20.926 1.00 5.29  ? 161 TRP A CE3   1 
ATOM   1245 C CZ2   . TRP A 1 181 ? 18.360  4.697   -21.140 1.00 5.23  ? 161 TRP A CZ2   1 
ATOM   1246 C CZ3   . TRP A 1 181 ? 17.826  2.481   -21.942 1.00 6.40  ? 161 TRP A CZ3   1 
ATOM   1247 C CH2   . TRP A 1 181 ? 17.748  3.871   -22.053 1.00 6.23  ? 161 TRP A CH2   1 
ATOM   1248 N N     . ALA A 1 182 ? 19.055  -1.848  -17.387 1.00 2.83  ? 162 ALA A N     1 
ATOM   1249 C CA    . ALA A 1 182 ? 19.575  -3.205  -17.448 1.00 3.02  ? 162 ALA A CA    1 
ATOM   1250 C C     . ALA A 1 182 ? 19.773  -3.564  -18.898 1.00 2.93  ? 162 ALA A C     1 
ATOM   1251 O O     . ALA A 1 182 ? 18.969  -3.209  -19.753 1.00 3.27  ? 162 ALA A O     1 
ATOM   1252 C CB    . ALA A 1 182 ? 18.635  -4.148  -16.826 1.00 3.25  ? 162 ALA A CB    1 
ATOM   1253 N N     . THR A 1 183 ? 20.814  -4.335  -19.205 1.00 2.65  ? 163 THR A N     1 
ATOM   1254 C CA    . THR A 1 183 ? 21.051  -4.863  -20.525 1.00 2.81  ? 163 THR A CA    1 
ATOM   1255 C C     . THR A 1 183 ? 20.073  -5.978  -20.827 1.00 2.86  ? 163 THR A C     1 
ATOM   1256 O O     . THR A 1 183 ? 19.199  -5.839  -21.678 1.00 3.12  ? 163 THR A O     1 
ATOM   1257 C CB    . THR A 1 183 ? 22.516  -5.301  -20.642 1.00 2.88  ? 163 THR A CB    1 
ATOM   1258 O OG1   . THR A 1 183 ? 22.737  -6.191  -19.544 1.00 3.23  ? 163 THR A OG1   1 
ATOM   1259 C CG2   . THR A 1 183 ? 23.452  -4.122  -20.617 1.00 3.16  ? 163 THR A CG2   1 
ATOM   1260 N N     . LEU A 1 184 ? 20.280  -7.105  -20.186 1.00 2.66  ? 164 LEU A N     1 
ATOM   1261 C CA    . LEU A 1 184 ? 19.508  -8.331  -20.393 1.00 2.64  ? 164 LEU A CA    1 
ATOM   1262 C C     . LEU A 1 184 ? 18.638  -8.630  -19.192 1.00 2.63  ? 164 LEU A C     1 
ATOM   1263 O O     . LEU A 1 184 ? 19.028  -8.421  -18.055 1.00 2.71  ? 164 LEU A O     1 
ATOM   1264 C CB    . LEU A 1 184 ? 20.460  -9.526  -20.569 1.00 2.98  ? 164 LEU A CB    1 
ATOM   1265 C CG    . LEU A 1 184 ? 21.520  -9.378  -21.647 1.00 3.25  ? 164 LEU A CG    1 
ATOM   1266 C CD1   . LEU A 1 184 ? 22.305  -10.691 -21.679 1.00 3.57  ? 164 LEU A CD1   1 
ATOM   1267 C CD2   . LEU A 1 184 ? 20.950  -9.023  -23.010 1.00 3.53  ? 164 LEU A CD2   1 
ATOM   1268 N N     . ASN A 1 185 ? 17.500  -9.262  -19.488 1.00 2.57  ? 165 ASN A N     1 
ATOM   1269 C CA    . ASN A 1 185 ? 16.675  -9.912  -18.481 1.00 2.87  ? 165 ASN A CA    1 
ATOM   1270 C C     . ASN A 1 185 ? 16.794  -11.422 -18.644 1.00 2.92  ? 165 ASN A C     1 
ATOM   1271 O O     . ASN A 1 185 ? 16.364  -11.983 -19.637 1.00 2.84  ? 165 ASN A O     1 
ATOM   1272 C CB    . ASN A 1 185 ? 15.191  -9.486  -18.637 1.00 3.34  ? 165 ASN A CB    1 
ATOM   1273 C CG    . ASN A 1 185 ? 14.317  -10.123 -17.582 1.00 4.20  ? 165 ASN A CG    1 
ATOM   1274 O OD1   . ASN A 1 185 ? 14.337  -9.693  -16.448 1.00 6.27  ? 165 ASN A OD1   1 
ATOM   1275 N ND2   . ASN A 1 185 ? 13.652  -11.211 -17.940 1.00 5.42  ? 165 ASN A ND2   1 
ATOM   1276 N N     . GLU A 1 186 ? 17.370  -12.087 -17.635 1.00 3.00  ? 166 GLU A N     1 
ATOM   1277 C CA    . GLU A 1 186 ? 17.360  -13.555 -17.530 1.00 3.33  ? 166 GLU A CA    1 
ATOM   1278 C C     . GLU A 1 186 ? 17.988  -14.224 -18.740 1.00 3.04  ? 166 GLU A C     1 
ATOM   1279 O O     . GLU A 1 186 ? 17.322  -14.977 -19.443 1.00 2.90  ? 166 GLU A O     1 
ATOM   1280 C CB    . GLU A 1 186 ? 15.970  -14.071 -17.292 1.00 3.90  ? 166 GLU A CB    1 
ATOM   1281 C CG    . GLU A 1 186 ? 15.374  -13.567 -15.995 1.00 4.66  ? 166 GLU A CG    1 
ATOM   1282 C CD    . GLU A 1 186 ? 13.956  -14.046 -15.729 1.00 5.93  ? 166 GLU A CD    1 
ATOM   1283 O OE1   . GLU A 1 186 ? 13.307  -14.516 -16.648 1.00 9.43  ? 166 GLU A OE1   1 
ATOM   1284 O OE2   . GLU A 1 186 ? 13.463  -13.932 -14.637 1.00 5.87  ? 166 GLU A OE2   1 
ATOM   1285 N N     . PRO A 1 187 ? 19.295  -14.032 -18.963 1.00 2.96  ? 167 PRO A N     1 
ATOM   1286 C CA    . PRO A 1 187 ? 19.977  -14.761 -20.040 1.00 2.97  ? 167 PRO A CA    1 
ATOM   1287 C C     . PRO A 1 187 ? 19.877  -16.275 -19.920 1.00 3.19  ? 167 PRO A C     1 
ATOM   1288 O O     . PRO A 1 187 ? 19.883  -16.963 -20.927 1.00 3.15  ? 167 PRO A O     1 
ATOM   1289 C CB    . PRO A 1 187 ? 21.423  -14.272 -19.938 1.00 3.08  ? 167 PRO A CB    1 
ATOM   1290 C CG    . PRO A 1 187 ? 21.565  -13.779 -18.555 1.00 3.17  ? 167 PRO A CG    1 
ATOM   1291 C CD    . PRO A 1 187 ? 20.220  -13.164 -18.221 1.00 3.05  ? 167 PRO A CD    1 
ATOM   1292 N N     . TRP A 1 188 ? 19.745  -16.800 -18.695 1.00 2.98  ? 168 TRP A N     1 
ATOM   1293 C CA    . TRP A 1 188 ? 19.549  -18.240 -18.611 1.00 3.31  ? 168 TRP A CA    1 
ATOM   1294 C C     . TRP A 1 188 ? 18.314  -18.683 -19.380 1.00 3.27  ? 168 TRP A C     1 
ATOM   1295 O O     . TRP A 1 188 ? 18.301  -19.724 -20.052 1.00 3.19  ? 168 TRP A O     1 
ATOM   1296 C CB    . TRP A 1 188 ? 19.514  -18.714 -17.148 1.00 3.71  ? 168 TRP A CB    1 
ATOM   1297 C CG    . TRP A 1 188 ? 19.267  -20.195 -17.054 1.00 4.36  ? 168 TRP A CG    1 
ATOM   1298 C CD1   . TRP A 1 188 ? 20.196  -21.197 -16.961 1.00 4.67  ? 168 TRP A CD1   1 
ATOM   1299 C CD2   . TRP A 1 188 ? 17.991  -20.854 -16.975 1.00 4.66  ? 168 TRP A CD2   1 
ATOM   1300 N NE1   . TRP A 1 188 ? 19.573  -22.406 -16.899 1.00 5.08  ? 168 TRP A NE1   1 
ATOM   1301 C CE2   . TRP A 1 188 ? 18.206  -22.247 -16.865 1.00 5.12  ? 168 TRP A CE2   1 
ATOM   1302 C CE3   . TRP A 1 188 ? 16.662  -20.387 -16.962 1.00 5.36  ? 168 TRP A CE3   1 
ATOM   1303 C CZ2   . TRP A 1 188 ? 17.156  -23.160 -16.801 1.00 6.14  ? 168 TRP A CZ2   1 
ATOM   1304 C CZ3   . TRP A 1 188 ? 15.631  -21.288 -16.903 1.00 6.04  ? 168 TRP A CZ3   1 
ATOM   1305 C CH2   . TRP A 1 188 ? 15.870  -22.670 -16.820 1.00 6.42  ? 168 TRP A CH2   1 
ATOM   1306 N N     . CYS A 1 189 ? 17.220  -17.907 -19.215 1.00 3.19  ? 169 CYS A N     1 
ATOM   1307 C CA    . CYS A 1 189 ? 16.004  -18.235 -19.932 1.00 3.53  ? 169 CYS A CA    1 
ATOM   1308 C C     . CYS A 1 189 ? 16.212  -18.152 -21.447 1.00 3.01  ? 169 CYS A C     1 
ATOM   1309 O O     . CYS A 1 189 ? 15.888  -19.083 -22.180 1.00 3.10  ? 169 CYS A O     1 
ATOM   1310 C CB    . CYS A 1 189 ? 14.877  -17.299 -19.515 1.00 3.90  ? 169 CYS A CB    1 
ATOM   1311 S SG    . CYS A 1 189 ? 14.358  -17.647 -17.804 1.00 6.15  ? 169 CYS A SG    1 
ATOM   1312 N N     . SER A 1 190 ? 16.711  -17.023 -21.951 1.00 2.68  ? 170 SER A N     1 
ATOM   1313 C CA    . SER A 1 190 ? 16.934  -16.874 -23.373 1.00 2.69  ? 170 SER A CA    1 
ATOM   1314 C C     . SER A 1 190 ? 17.793  -17.995 -23.943 1.00 2.97  ? 170 SER A C     1 
ATOM   1315 O O     . SER A 1 190 ? 17.430  -18.573 -24.981 1.00 3.27  ? 170 SER A O     1 
ATOM   1316 C CB    . SER A 1 190 ? 17.607  -15.588 -23.674 1.00 2.52  ? 170 SER A CB    1 
ATOM   1317 O OG    . SER A 1 190 ? 16.759  -14.482 -23.393 1.00 2.62  ? 170 SER A OG    1 
ATOM   1318 N N     . ALA A 1 191 ? 18.864  -18.366 -23.226 1.00 2.88  ? 171 ALA A N     1 
ATOM   1319 C CA    . ALA A 1 191 ? 19.775  -19.394 -23.735 1.00 3.13  ? 171 ALA A CA    1 
ATOM   1320 C C     . ALA A 1 191 ? 19.205  -20.783 -23.572 1.00 3.80  ? 171 ALA A C     1 
ATOM   1321 O O     . ALA A 1 191 ? 19.113  -21.568 -24.521 1.00 4.07  ? 171 ALA A O     1 
ATOM   1322 C CB    . ALA A 1 191 ? 21.115  -19.297 -23.037 1.00 3.12  ? 171 ALA A CB    1 
ATOM   1323 N N     . MET A 1 192 ? 18.786  -21.101 -22.370 1.00 3.75  ? 172 MET A N     1 
ATOM   1324 C CA    . MET A 1 192 ? 18.467  -22.478 -22.061 1.00 5.01  ? 172 MET A CA    1 
ATOM   1325 C C     . MET A 1 192 ? 17.048  -22.818 -22.457 1.00 5.05  ? 172 MET A C     1 
ATOM   1326 O O     . MET A 1 192 ? 16.799  -23.878 -23.003 1.00 6.53  ? 172 MET A O     1 
ATOM   1327 C CB    . MET A 1 192 ? 18.792  -22.827 -20.597 1.00 5.98  ? 172 MET A CB    1 
ATOM   1328 C CG    . MET A 1 192 ? 20.225  -22.664 -20.326 1.00 6.81  ? 172 MET A CG    1 
ATOM   1329 S SD    . MET A 1 192 ? 21.292  -23.630 -21.447 1.00 9.98  ? 172 MET A SD    1 
ATOM   1330 C CE    . MET A 1 192 ? 22.906  -23.125 -20.853 1.00 12.16 ? 172 MET A CE    1 
ATOM   1331 N N     . LEU A 1 193 ? 16.079  -21.974 -22.123 1.00 4.27  ? 173 LEU A N     1 
ATOM   1332 C CA    . LEU A 1 193 ? 14.722  -22.259 -22.545 1.00 4.54  ? 173 LEU A CA    1 
ATOM   1333 C C     . LEU A 1 193 ? 14.568  -22.033 -24.046 1.00 4.04  ? 173 LEU A C     1 
ATOM   1334 O O     . LEU A 1 193 ? 13.770  -22.742 -24.652 1.00 4.47  ? 173 LEU A O     1 
ATOM   1335 C CB    . LEU A 1 193 ? 13.703  -21.430 -21.771 1.00 5.38  ? 173 LEU A CB    1 
ATOM   1336 C CG    . LEU A 1 193 ? 13.768  -21.625 -20.260 1.00 6.22  ? 173 LEU A CG    1 
ATOM   1337 C CD1   . LEU A 1 193 ? 12.681  -20.802 -19.597 1.00 6.37  ? 173 LEU A CD1   1 
ATOM   1338 C CD2   . LEU A 1 193 ? 13.631  -23.098 -19.908 1.00 7.11  ? 173 LEU A CD2   1 
ATOM   1339 N N     . GLY A 1 194 ? 15.318  -21.103 -24.639 1.00 3.69  ? 174 GLY A N     1 
ATOM   1340 C CA    . GLY A 1 194 ? 15.119  -20.800 -26.040 1.00 3.36  ? 174 GLY A CA    1 
ATOM   1341 C C     . GLY A 1 194 ? 15.912  -21.698 -27.002 1.00 3.56  ? 174 GLY A C     1 
ATOM   1342 O O     . GLY A 1 194 ? 15.470  -21.863 -28.129 1.00 4.17  ? 174 GLY A O     1 
ATOM   1343 N N     . TYR A 1 195 ? 17.093  -22.185 -26.587 1.00 3.91  ? 175 TYR A N     1 
ATOM   1344 C CA    . TYR A 1 195 ? 17.987  -22.887 -27.495 1.00 3.86  ? 175 TYR A CA    1 
ATOM   1345 C C     . TYR A 1 195 ? 18.308  -24.320 -27.051 1.00 4.56  ? 175 TYR A C     1 
ATOM   1346 O O     . TYR A 1 195 ? 18.762  -25.071 -27.907 1.00 4.92  ? 175 TYR A O     1 
ATOM   1347 C CB    . TYR A 1 195 ? 19.300  -22.125 -27.725 1.00 3.95  ? 175 TYR A CB    1 
ATOM   1348 C CG    . TYR A 1 195 ? 19.176  -20.820 -28.473 1.00 3.98  ? 175 TYR A CG    1 
ATOM   1349 C CD1   . TYR A 1 195 ? 18.816  -19.639 -27.840 1.00 3.94  ? 175 TYR A CD1   1 
ATOM   1350 C CD2   . TYR A 1 195 ? 19.447  -20.757 -29.831 1.00 4.20  ? 175 TYR A CD2   1 
ATOM   1351 C CE1   . TYR A 1 195 ? 18.668  -18.468 -28.545 1.00 3.94  ? 175 TYR A CE1   1 
ATOM   1352 C CE2   . TYR A 1 195 ? 19.292  -19.591 -30.547 1.00 4.03  ? 175 TYR A CE2   1 
ATOM   1353 C CZ    . TYR A 1 195 ? 18.920  -18.435 -29.900 1.00 4.00  ? 175 TYR A CZ    1 
ATOM   1354 O OH    . TYR A 1 195 ? 18.796  -17.258 -30.601 1.00 4.53  ? 175 TYR A OH    1 
ATOM   1355 N N     . TYR A 1 196 ? 18.129  -24.670 -25.776 1.00 5.02  ? 176 TYR A N     1 
ATOM   1356 C CA    . TYR A 1 196 ? 18.420  -26.020 -25.302 1.00 5.81  ? 176 TYR A CA    1 
ATOM   1357 C C     . TYR A 1 196 ? 17.141  -26.814 -25.082 1.00 6.62  ? 176 TYR A C     1 
ATOM   1358 O O     . TYR A 1 196 ? 17.029  -27.923 -25.599 1.00 7.97  ? 176 TYR A O     1 
ATOM   1359 C CB    . TYR A 1 196 ? 19.306  -25.950 -24.049 1.00 6.09  ? 176 TYR A CB    1 
ATOM   1360 C CG    . TYR A 1 196 ? 19.559  -27.252 -23.313 1.00 7.12  ? 176 TYR A CG    1 
ATOM   1361 C CD1   . TYR A 1 196 ? 19.775  -28.427 -23.998 1.00 8.37  ? 176 TYR A CD1   1 
ATOM   1362 C CD2   . TYR A 1 196 ? 19.582  -27.280 -21.935 1.00 7.99  ? 176 TYR A CD2   1 
ATOM   1363 C CE1   . TYR A 1 196 ? 19.994  -29.615 -23.331 1.00 9.23  ? 176 TYR A CE1   1 
ATOM   1364 C CE2   . TYR A 1 196 ? 19.787  -28.458 -21.251 1.00 9.94  ? 176 TYR A CE2   1 
ATOM   1365 C CZ    . TYR A 1 196 ? 20.020  -29.612 -21.960 1.00 10.07 ? 176 TYR A CZ    1 
ATOM   1366 O OH    . TYR A 1 196 ? 20.218  -30.782 -21.240 1.00 12.12 ? 176 TYR A OH    1 
ATOM   1367 N N     . LEU A 1 197 ? 16.179  -26.286 -24.310 1.00 6.59  ? 177 LEU A N     1 
ATOM   1368 C CA    . LEU A 1 197 ? 14.989  -27.006 -23.936 1.00 7.16  ? 177 LEU A CA    1 
ATOM   1369 C C     . LEU A 1 197 ? 13.838  -26.761 -24.900 1.00 6.86  ? 177 LEU A C     1 
ATOM   1370 O O     . LEU A 1 197 ? 12.914  -27.557 -24.972 1.00 8.85  ? 177 LEU A O     1 
ATOM   1371 C CB    . LEU A 1 197 ? 14.649  -26.713 -22.468 1.00 9.44  ? 177 LEU A CB    1 
ATOM   1372 C CG    . LEU A 1 197 ? 15.780  -27.061 -21.497 1.00 11.86 ? 177 LEU A CG    1 
ATOM   1373 C CD1   . LEU A 1 197 ? 15.450  -26.627 -20.092 1.00 14.65 ? 177 LEU A CD1   1 
ATOM   1374 C CD2   . LEU A 1 197 ? 16.094  -28.554 -21.549 1.00 13.05 ? 177 LEU A CD2   1 
ATOM   1375 N N     . GLY A 1 198 ? 13.916  -25.695 -25.711 1.00 6.95  ? 178 GLY A N     1 
ATOM   1376 C CA    . GLY A 1 198 ? 12.989  -25.477 -26.803 1.00 8.08  ? 178 GLY A CA    1 
ATOM   1377 C C     . GLY A 1 198 ? 11.616  -24.971 -26.401 1.00 7.53  ? 178 GLY A C     1 
ATOM   1378 O O     . GLY A 1 198 ? 10.727  -24.884 -27.260 1.00 8.76  ? 178 GLY A O     1 
ATOM   1379 N N     . VAL A 1 199 ? 11.448  -24.562 -25.141 1.00 5.96  ? 179 VAL A N     1 
ATOM   1380 C CA    . VAL A 1 199 ? 10.111  -24.202 -24.690 1.00 6.77  ? 179 VAL A CA    1 
ATOM   1381 C C     . VAL A 1 199 ? 9.802   -22.734 -24.937 1.00 5.35  ? 179 VAL A C     1 
ATOM   1382 O O     . VAL A 1 199 ? 8.629   -22.373 -25.020 1.00 5.25  ? 179 VAL A O     1 
ATOM   1383 C CB    . VAL A 1 199 ? 9.885   -24.580 -23.216 1.00 8.52  ? 179 VAL A CB    1 
ATOM   1384 C CG1   . VAL A 1 199 ? 9.987   -26.084 -23.017 1.00 10.75 ? 179 VAL A CG1   1 
ATOM   1385 C CG2   . VAL A 1 199 ? 10.792  -23.860 -22.277 1.00 8.88  ? 179 VAL A CG2   1 
ATOM   1386 N N     . HIS A 1 200 ? 10.835  -21.922 -25.134 1.00 4.22  ? 180 HIS A N     1 
ATOM   1387 C CA    . HIS A 1 200 ? 10.680  -20.511 -25.457 1.00 4.03  ? 180 HIS A CA    1 
ATOM   1388 C C     . HIS A 1 200 ? 11.273  -20.245 -26.832 1.00 3.56  ? 180 HIS A C     1 
ATOM   1389 O O     . HIS A 1 200 ? 12.080  -21.013 -27.345 1.00 2.91  ? 180 HIS A O     1 
ATOM   1390 C CB    . HIS A 1 200 ? 11.469  -19.665 -24.465 1.00 4.05  ? 180 HIS A CB    1 
ATOM   1391 C CG    . HIS A 1 200 ? 10.724  -19.513 -23.192 1.00 4.47  ? 180 HIS A CG    1 
ATOM   1392 N ND1   . HIS A 1 200 ? 11.191  -18.752 -22.161 1.00 5.03  ? 180 HIS A ND1   1 
ATOM   1393 C CD2   . HIS A 1 200 ? 9.550   -20.045 -22.808 1.00 5.09  ? 180 HIS A CD2   1 
ATOM   1394 C CE1   . HIS A 1 200 ? 10.278  -18.815 -21.185 1.00 4.86  ? 180 HIS A CE1   1 
ATOM   1395 N NE2   . HIS A 1 200 ? 9.253   -19.547 -21.557 1.00 5.06  ? 180 HIS A NE2   1 
ATOM   1396 N N     . ALA A 1 201 ? 10.934  -19.097 -27.415 1.00 2.93  ? 181 ALA A N     1 
ATOM   1397 C CA    . ALA A 1 201 ? 11.513  -18.725 -28.686 1.00 2.76  ? 181 ALA A CA    1 
ATOM   1398 C C     . ALA A 1 201 ? 13.024  -18.617 -28.617 1.00 2.63  ? 181 ALA A C     1 
ATOM   1399 O O     . ALA A 1 201 ? 13.594  -18.152 -27.594 1.00 2.39  ? 181 ALA A O     1 
ATOM   1400 C CB    . ALA A 1 201 ? 10.950  -17.409 -29.104 1.00 2.66  ? 181 ALA A CB    1 
ATOM   1401 N N     . PRO A 1 202 ? 13.777  -19.008 -29.677 1.00 2.88  ? 182 PRO A N     1 
ATOM   1402 C CA    . PRO A 1 202 ? 13.244  -19.453 -30.965 1.00 3.26  ? 182 PRO A CA    1 
ATOM   1403 C C     . PRO A 1 202 ? 12.841  -20.926 -31.021 1.00 4.08  ? 182 PRO A C     1 
ATOM   1404 O O     . PRO A 1 202 ? 12.296  -21.336 -32.054 1.00 5.34  ? 182 PRO A O     1 
ATOM   1405 C CB    . PRO A 1 202 ? 14.474  -19.174 -31.859 1.00 3.30  ? 182 PRO A CB    1 
ATOM   1406 C CG    . PRO A 1 202 ? 15.641  -19.460 -30.974 1.00 3.22  ? 182 PRO A CG    1 
ATOM   1407 C CD    . PRO A 1 202 ? 15.241  -18.854 -29.669 1.00 3.10  ? 182 PRO A CD    1 
ATOM   1408 N N     . GLY A 1 203 ? 13.130  -21.706 -29.982 1.00 4.20  ? 183 GLY A N     1 
ATOM   1409 C CA    . GLY A 1 203 ? 12.607  -23.063 -29.921 1.00 4.77  ? 183 GLY A CA    1 
ATOM   1410 C C     . GLY A 1 203 ? 13.613  -24.136 -30.325 1.00 5.49  ? 183 GLY A C     1 
ATOM   1411 O O     . GLY A 1 203 ? 13.196  -25.269 -30.580 1.00 7.71  ? 183 GLY A O     1 
ATOM   1412 N N     . HIS A 1 204 ? 14.906  -23.869 -30.228 1.00 5.70  ? 184 HIS A N     1 
ATOM   1413 C CA    . HIS A 1 204 ? 15.894  -24.888 -30.546 1.00 6.70  ? 184 HIS A CA    1 
ATOM   1414 C C     . HIS A 1 204 ? 16.078  -25.826 -29.361 1.00 6.40  ? 184 HIS A C     1 
ATOM   1415 O O     . HIS A 1 204 ? 15.752  -25.519 -28.207 1.00 4.92  ? 184 HIS A O     1 
ATOM   1416 C CB    . HIS A 1 204 ? 17.206  -24.224 -30.951 1.00 8.04  ? 184 HIS A CB    1 
ATOM   1417 C CG    . HIS A 1 204 ? 17.211  -23.642 -32.316 1.00 12.26 ? 184 HIS A CG    1 
ATOM   1418 N ND1   . HIS A 1 204 ? 17.493  -24.539 -33.337 1.00 17.69 ? 184 HIS A ND1   1 
ATOM   1419 C CD2   . HIS A 1 204 ? 17.197  -22.407 -32.881 1.00 16.41 ? 184 HIS A CD2   1 
ATOM   1420 C CE1   . HIS A 1 204 ? 17.551  -23.865 -34.501 1.00 19.24 ? 184 HIS A CE1   1 
ATOM   1421 N NE2   . HIS A 1 204 ? 17.318  -22.590 -34.248 1.00 19.87 ? 184 HIS A NE2   1 
ATOM   1422 N N     . THR A 1 205 ? 16.612  -27.023 -29.650 1.00 7.53  ? 185 THR A N     1 
ATOM   1423 C CA    . THR A 1 205 ? 16.780  -28.063 -28.651 1.00 8.28  ? 185 THR A CA    1 
ATOM   1424 C C     . THR A 1 205 ? 18.162  -28.697 -28.728 1.00 9.85  ? 185 THR A C     1 
ATOM   1425 O O     . THR A 1 205 ? 18.289  -29.888 -28.974 1.00 12.35 ? 185 THR A O     1 
ATOM   1426 C CB    . THR A 1 205 ? 15.706  -29.139 -28.794 1.00 9.72  ? 185 THR A CB    1 
ATOM   1427 O OG1   . THR A 1 205 ? 15.713  -29.553 -30.170 1.00 10.66 ? 185 THR A OG1   1 
ATOM   1428 C CG2   . THR A 1 205 ? 14.335  -28.628 -28.422 1.00 10.29 ? 185 THR A CG2   1 
ATOM   1429 N N     . ASP A 1 206 ? 19.188  -27.962 -28.390 1.00 9.35  ? 186 ASP A N     1 
ATOM   1430 C CA    . ASP A 1 206 ? 20.535  -28.515 -28.388 1.00 9.64  ? 186 ASP A CA    1 
ATOM   1431 C C     . ASP A 1 206 ? 21.387  -27.849 -27.308 1.00 9.07  ? 186 ASP A C     1 
ATOM   1432 O O     . ASP A 1 206 ? 21.456  -26.611 -27.223 1.00 8.00  ? 186 ASP A O     1 
ATOM   1433 C CB    . ASP A 1 206 ? 21.141  -28.315 -29.767 1.00 11.21 ? 186 ASP A CB    1 
ATOM   1434 C CG    . ASP A 1 206 ? 22.557  -28.809 -29.879 1.00 14.01 ? 186 ASP A CG    1 
ATOM   1435 O OD1   . ASP A 1 206 ? 22.738  -30.047 -29.928 1.00 17.99 ? 186 ASP A OD1   1 
ATOM   1436 O OD2   . ASP A 1 206 ? 23.471  -27.968 -29.925 1.00 14.60 ? 186 ASP A OD2   1 
ATOM   1437 N N     . LEU A 1 207 ? 22.079  -28.651 -26.496 1.00 9.11  ? 187 LEU A N     1 
ATOM   1438 C CA    . LEU A 1 207 ? 22.874  -28.107 -25.418 1.00 8.99  ? 187 LEU A CA    1 
ATOM   1439 C C     . LEU A 1 207 ? 23.949  -27.149 -25.925 1.00 8.76  ? 187 LEU A C     1 
ATOM   1440 O O     . LEU A 1 207 ? 24.179  -26.078 -25.374 1.00 7.85  ? 187 LEU A O     1 
ATOM   1441 C CB    . LEU A 1 207 ? 23.536  -29.246 -24.636 1.00 11.00 ? 187 LEU A CB    1 
ATOM   1442 C CG    . LEU A 1 207 ? 24.471  -28.805 -23.514 1.00 13.34 ? 187 LEU A CG    1 
ATOM   1443 C CD1   . LEU A 1 207 ? 23.721  -28.053 -22.431 1.00 12.87 ? 187 LEU A CD1   1 
ATOM   1444 C CD2   . LEU A 1 207 ? 25.222  -30.014 -22.964 1.00 16.48 ? 187 LEU A CD2   1 
ATOM   1445 N N     . LYS A 1 208 ? 24.684  -27.537 -26.951 1.00 8.65  ? 188 LYS A N     1 
ATOM   1446 C CA    . LYS A 1 208 ? 25.777  -26.724 -27.451 1.00 9.02  ? 188 LYS A CA    1 
ATOM   1447 C C     . LYS A 1 208 ? 25.202  -25.387 -27.927 1.00 7.82  ? 188 LYS A C     1 
ATOM   1448 O O     . LYS A 1 208 ? 25.813  -24.361 -27.693 1.00 7.61  ? 188 LYS A O     1 
ATOM   1449 C CB    . LYS A 1 208 ? 26.571  -27.446 -28.545 1.00 11.61 ? 188 LYS A CB    1 
ATOM   1450 C CG    . LYS A 1 208 ? 27.738  -26.668 -29.105 1.00 15.77 ? 188 LYS A CG    1 
ATOM   1451 C CD    . LYS A 1 208 ? 28.503  -27.445 -30.188 1.00 19.51 ? 188 LYS A CD    1 
ATOM   1452 C CE    . LYS A 1 208 ? 29.767  -26.711 -30.602 1.00 26.19 ? 188 LYS A CE    1 
ATOM   1453 N NZ    . LYS A 1 208 ? 30.608  -27.486 -31.550 1.00 31.48 ? 188 LYS A NZ    1 
ATOM   1454 N N     . ARG A 1 209 ? 24.045  -25.410 -28.608 1.00 7.65  ? 189 ARG A N     1 
ATOM   1455 C CA    . ARG A 1 209 ? 23.416  -24.160 -29.034 1.00 7.71  ? 189 ARG A CA    1 
ATOM   1456 C C     . ARG A 1 209 ? 23.082  -23.296 -27.818 1.00 6.22  ? 189 ARG A C     1 
ATOM   1457 O O     . ARG A 1 209 ? 23.305  -22.072 -27.819 1.00 5.90  ? 189 ARG A O     1 
ATOM   1458 C CB    . ARG A 1 209 ? 22.124  -24.407 -29.815 1.00 9.70  ? 189 ARG A CB    1 
ATOM   1459 C CG    . ARG A 1 209 ? 22.327  -24.988 -31.206 1.00 12.26 ? 189 ARG A CG    1 
ATOM   1460 C CD    . ARG A 1 209 ? 20.950  -25.268 -31.798 1.00 16.38 ? 189 ARG A CD    1 
ATOM   1461 N NE    . ARG A 1 209 ? 20.907  -25.944 -33.087 1.00 20.56 ? 189 ARG A NE    1 
ATOM   1462 C CZ    . ARG A 1 209 ? 21.034  -25.334 -34.258 1.00 24.66 ? 189 ARG A CZ    1 
ATOM   1463 N NH1   . ARG A 1 209 ? 21.306  -24.046 -34.311 1.00 26.65 ? 189 ARG A NH1   1 
ATOM   1464 N NH2   . ARG A 1 209 ? 20.903  -26.020 -35.379 1.00 28.71 ? 189 ARG A NH2   1 
ATOM   1465 N N     . GLY A 1 210 ? 22.571  -23.918 -26.767 1.00 6.08  ? 190 GLY A N     1 
ATOM   1466 C CA    . GLY A 1 210 ? 22.237  -23.146 -25.573 1.00 5.15  ? 190 GLY A CA    1 
ATOM   1467 C C     . GLY A 1 210 ? 23.466  -22.521 -24.929 1.00 5.42  ? 190 GLY A C     1 
ATOM   1468 O O     . GLY A 1 210 ? 23.456  -21.367 -24.501 1.00 4.86  ? 190 GLY A O     1 
ATOM   1469 N N     . LEU A 1 211 ? 24.543  -23.290 -24.819 1.00 5.70  ? 191 LEU A N     1 
ATOM   1470 C CA    . LEU A 1 211 ? 25.743  -22.763 -24.203 1.00 5.77  ? 191 LEU A CA    1 
ATOM   1471 C C     . LEU A 1 211 ? 26.418  -21.705 -25.035 1.00 5.62  ? 191 LEU A C     1 
ATOM   1472 O O     . LEU A 1 211 ? 26.968  -20.766 -24.504 1.00 6.00  ? 191 LEU A O     1 
ATOM   1473 C CB    . LEU A 1 211 ? 26.673  -23.957 -23.914 1.00 6.67  ? 191 LEU A CB    1 
ATOM   1474 C CG    . LEU A 1 211 ? 26.243  -24.857 -22.777 1.00 8.39  ? 191 LEU A CG    1 
ATOM   1475 C CD1   . LEU A 1 211 ? 27.213  -26.044 -22.666 1.00 8.90  ? 191 LEU A CD1   1 
ATOM   1476 C CD2   . LEU A 1 211 ? 26.247  -24.113 -21.447 1.00 9.39  ? 191 LEU A CD2   1 
ATOM   1477 N N     . GLU A 1 212 ? 26.395  -21.864 -26.357 1.00 6.33  ? 192 GLU A N     1 
ATOM   1478 C CA    . GLU A 1 212 ? 26.917  -20.846 -27.226 1.00 6.95  ? 192 GLU A CA    1 
ATOM   1479 C C     . GLU A 1 212 ? 26.082  -19.564 -27.086 1.00 5.45  ? 192 GLU A C     1 
ATOM   1480 O O     . GLU A 1 212 ? 26.614  -18.482 -27.008 1.00 5.72  ? 192 GLU A O     1 
ATOM   1481 C CB    . GLU A 1 212 ? 26.852  -21.443 -28.637 1.00 10.49 ? 192 GLU A CB    1 
ATOM   1482 C CG    . GLU A 1 212 ? 27.261  -20.536 -29.769 1.00 16.40 ? 192 GLU A CG    1 
ATOM   1483 C CD    . GLU A 1 212 ? 27.066  -21.204 -31.144 1.00 22.37 ? 192 GLU A CD    1 
ATOM   1484 O OE1   . GLU A 1 212 ? 28.077  -21.385 -31.819 1.00 28.93 ? 192 GLU A OE1   1 
ATOM   1485 O OE2   . GLU A 1 212 ? 25.892  -21.569 -31.551 1.00 25.32 ? 192 GLU A OE2   1 
ATOM   1486 N N     . ALA A 1 213 ? 24.769  -19.749 -27.057 1.00 4.76  ? 193 ALA A N     1 
ATOM   1487 C CA    . ALA A 1 213 ? 23.889  -18.596 -26.866 1.00 4.51  ? 193 ALA A CA    1 
ATOM   1488 C C     . ALA A 1 213 ? 24.206  -17.936 -25.541 1.00 4.45  ? 193 ALA A C     1 
ATOM   1489 O O     . ALA A 1 213 ? 24.220  -16.700 -25.468 1.00 4.28  ? 193 ALA A O     1 
ATOM   1490 C CB    . ALA A 1 213 ? 22.448  -19.011 -26.935 1.00 4.28  ? 193 ALA A CB    1 
ATOM   1491 N N     . SER A 1 214 ? 24.419  -18.719 -24.470 1.00 4.40  ? 194 SER A N     1 
ATOM   1492 C CA    . SER A 1 214 ? 24.701  -18.111 -23.166 1.00 4.77  ? 194 SER A CA    1 
ATOM   1493 C C     . SER A 1 214 ? 25.941  -17.206 -23.221 1.00 4.24  ? 194 SER A C     1 
ATOM   1494 O O     . SER A 1 214 ? 25.981  -16.123 -22.632 1.00 4.15  ? 194 SER A O     1 
ATOM   1495 C CB    . SER A 1 214 ? 24.777  -19.159 -22.080 1.00 5.49  ? 194 SER A CB    1 
ATOM   1496 O OG    . SER A 1 214 ? 26.021  -19.872 -22.101 1.00 7.67  ? 194 SER A OG    1 
ATOM   1497 N N     . HIS A 1 215 ? 26.989  -17.645 -23.966 1.00 4.06  ? 195 HIS A N     1 
ATOM   1498 C CA    . HIS A 1 215 ? 28.208  -16.885 -24.093 1.00 4.86  ? 195 HIS A CA    1 
ATOM   1499 C C     . HIS A 1 215 ? 27.969  -15.595 -24.864 1.00 4.27  ? 195 HIS A C     1 
ATOM   1500 O O     . HIS A 1 215 ? 28.491  -14.545 -24.515 1.00 4.86  ? 195 HIS A O     1 
ATOM   1501 C CB    . HIS A 1 215 ? 29.303  -17.745 -24.741 1.00 5.40  ? 195 HIS A CB    1 
ATOM   1502 C CG    . HIS A 1 215 ? 30.639  -17.070 -24.794 1.00 6.46  ? 195 HIS A CG    1 
ATOM   1503 N ND1   . HIS A 1 215 ? 31.378  -16.890 -23.651 1.00 7.63  ? 195 HIS A ND1   1 
ATOM   1504 C CD2   . HIS A 1 215 ? 31.297  -16.466 -25.794 1.00 7.63  ? 195 HIS A CD2   1 
ATOM   1505 C CE1   . HIS A 1 215 ? 32.468  -16.174 -23.975 1.00 8.69  ? 195 HIS A CE1   1 
ATOM   1506 N NE2   . HIS A 1 215 ? 32.465  -15.947 -25.265 1.00 9.11  ? 195 HIS A NE2   1 
ATOM   1507 N N     . ASN A 1 216 ? 27.229  -15.682 -25.992 1.00 4.44  ? 196 ASN A N     1 
ATOM   1508 C CA    . ASN A 1 216 ? 27.036  -14.507 -26.815 1.00 4.62  ? 196 ASN A CA    1 
ATOM   1509 C C     . ASN A 1 216 ? 26.091  -13.506 -26.148 1.00 3.88  ? 196 ASN A C     1 
ATOM   1510 O O     . ASN A 1 216 ? 26.234  -12.311 -26.392 1.00 4.03  ? 196 ASN A O     1 
ATOM   1511 C CB    . ASN A 1 216 ? 26.576  -14.893 -28.207 1.00 5.38  ? 196 ASN A CB    1 
ATOM   1512 C CG    . ASN A 1 216 ? 27.693  -15.609 -28.955 1.00 6.88  ? 196 ASN A CG    1 
ATOM   1513 O OD1   . ASN A 1 216 ? 28.859  -15.228 -28.851 1.00 9.30  ? 196 ASN A OD1   1 
ATOM   1514 N ND2   . ASN A 1 216 ? 27.307  -16.548 -29.767 1.00 7.16  ? 196 ASN A ND2   1 
ATOM   1515 N N     . LEU A 1 217 ? 25.164  -13.997 -25.342 1.00 3.52  ? 197 LEU A N     1 
ATOM   1516 C CA    . LEU A 1 217 ? 24.364  -13.102 -24.509 1.00 3.34  ? 197 LEU A CA    1 
ATOM   1517 C C     . LEU A 1 217 ? 25.248  -12.354 -23.530 1.00 3.58  ? 197 LEU A C     1 
ATOM   1518 O O     . LEU A 1 217 ? 25.160  -11.140 -23.431 1.00 3.36  ? 197 LEU A O     1 
ATOM   1519 C CB    . LEU A 1 217 ? 23.292  -13.937 -23.789 1.00 3.33  ? 197 LEU A CB    1 
ATOM   1520 C CG    . LEU A 1 217 ? 22.064  -14.295 -24.614 1.00 3.68  ? 197 LEU A CG    1 
ATOM   1521 C CD1   . LEU A 1 217 ? 21.355  -15.521 -24.091 1.00 3.68  ? 197 LEU A CD1   1 
ATOM   1522 C CD2   . LEU A 1 217 ? 21.062  -13.143 -24.691 1.00 3.58  ? 197 LEU A CD2   1 
ATOM   1523 N N     . LEU A 1 218 ? 26.118  -13.091 -22.786 1.00 3.89  ? 198 LEU A N     1 
ATOM   1524 C CA    . LEU A 1 218 ? 26.995  -12.419 -21.850 1.00 4.33  ? 198 LEU A CA    1 
ATOM   1525 C C     . LEU A 1 218 ? 27.920  -11.445 -22.568 1.00 4.27  ? 198 LEU A C     1 
ATOM   1526 O O     . LEU A 1 218 ? 28.192  -10.362 -22.067 1.00 4.15  ? 198 LEU A O     1 
ATOM   1527 C CB    . LEU A 1 218 ? 27.808  -13.459 -21.090 1.00 4.87  ? 198 LEU A CB    1 
ATOM   1528 C CG    . LEU A 1 218 ? 27.044  -14.175 -19.984 1.00 5.60  ? 198 LEU A CG    1 
ATOM   1529 C CD1   . LEU A 1 218 ? 27.830  -15.365 -19.417 1.00 6.16  ? 198 LEU A CD1   1 
ATOM   1530 C CD2   . LEU A 1 218 ? 26.676  -13.195 -18.897 1.00 6.73  ? 198 LEU A CD2   1 
ATOM   1531 N N     . LEU A 1 219 ? 28.439  -11.833 -23.738 1.00 4.45  ? 199 LEU A N     1 
ATOM   1532 C CA    . LEU A 1 219 ? 29.310  -10.949 -24.495 1.00 5.42  ? 199 LEU A CA    1 
ATOM   1533 C C     . LEU A 1 219 ? 28.554  -9.698  -24.956 1.00 5.20  ? 199 LEU A C     1 
ATOM   1534 O O     . LEU A 1 219 ? 29.049  -8.585  -24.865 1.00 6.05  ? 199 LEU A O     1 
ATOM   1535 C CB    . LEU A 1 219 ? 29.916  -11.749 -25.674 1.00 7.12  ? 199 LEU A CB    1 
ATOM   1536 C CG    . LEU A 1 219 ? 30.836  -10.945 -26.593 1.00 9.30  ? 199 LEU A CG    1 
ATOM   1537 C CD1   . LEU A 1 219 ? 32.089  -10.510 -25.856 1.00 10.60 ? 199 LEU A CD1   1 
ATOM   1538 C CD2   . LEU A 1 219 ? 31.184  -11.745 -27.825 1.00 10.80 ? 199 LEU A CD2   1 
ATOM   1539 N N     . GLY A 1 220 ? 27.333  -9.895  -25.461 1.00 4.56  ? 200 GLY A N     1 
ATOM   1540 C CA    . GLY A 1 220 ? 26.450  -8.797  -25.823 1.00 4.20  ? 200 GLY A CA    1 
ATOM   1541 C C     . GLY A 1 220 ? 26.232  -7.834  -24.664 1.00 3.94  ? 200 GLY A C     1 
ATOM   1542 O O     . GLY A 1 220 ? 26.353  -6.621  -24.836 1.00 3.43  ? 200 GLY A O     1 
ATOM   1543 N N     . HIS A 1 221 ? 25.933  -8.401  -23.487 1.00 3.56  ? 201 HIS A N     1 
ATOM   1544 C CA    . HIS A 1 221 ? 25.858  -7.629  -22.264 1.00 3.61  ? 201 HIS A CA    1 
ATOM   1545 C C     . HIS A 1 221 ? 27.096  -6.759  -22.110 1.00 3.76  ? 201 HIS A C     1 
ATOM   1546 O O     . HIS A 1 221 ? 27.003  -5.563  -21.876 1.00 3.89  ? 201 HIS A O     1 
ATOM   1547 C CB    . HIS A 1 221 ? 25.646  -8.536  -21.072 1.00 3.41  ? 201 HIS A CB    1 
ATOM   1548 C CG    . HIS A 1 221 ? 26.036  -7.898  -19.803 1.00 3.42  ? 201 HIS A CG    1 
ATOM   1549 N ND1   . HIS A 1 221 ? 25.257  -6.957  -19.154 1.00 3.42  ? 201 HIS A ND1   1 
ATOM   1550 C CD2   . HIS A 1 221 ? 27.151  -8.040  -19.055 1.00 3.45  ? 201 HIS A CD2   1 
ATOM   1551 C CE1   . HIS A 1 221 ? 25.895  -6.537  -18.062 1.00 3.55  ? 201 HIS A CE1   1 
ATOM   1552 N NE2   . HIS A 1 221 ? 27.093  -7.211  -17.997 1.00 3.69  ? 201 HIS A NE2   1 
ATOM   1553 N N     . GLY A 1 222 ? 28.291  -7.387  -22.122 1.00 4.12  ? 202 GLY A N     1 
ATOM   1554 C CA    . GLY A 1 222 ? 29.503  -6.633  -21.822 1.00 4.55  ? 202 GLY A CA    1 
ATOM   1555 C C     . GLY A 1 222 ? 29.814  -5.559  -22.845 1.00 4.31  ? 202 GLY A C     1 
ATOM   1556 O O     . GLY A 1 222 ? 30.259  -4.450  -22.498 1.00 4.63  ? 202 GLY A O     1 
ATOM   1557 N N     . LEU A 1 223 ? 29.640  -5.875  -24.131 1.00 4.46  ? 203 LEU A N     1 
ATOM   1558 C CA    . LEU A 1 223 ? 29.810  -4.902  -25.164 1.00 4.78  ? 203 LEU A CA    1 
ATOM   1559 C C     . LEU A 1 223 ? 28.821  -3.751  -25.003 1.00 4.25  ? 203 LEU A C     1 
ATOM   1560 O O     . LEU A 1 223 ? 29.158  -2.612  -25.245 1.00 4.74  ? 203 LEU A O     1 
ATOM   1561 C CB    . LEU A 1 223 ? 29.661  -5.538  -26.535 1.00 5.95  ? 203 LEU A CB    1 
ATOM   1562 C CG    . LEU A 1 223 ? 30.744  -6.550  -26.899 1.00 7.06  ? 203 LEU A CG    1 
ATOM   1563 C CD1   . LEU A 1 223 ? 30.382  -7.192  -28.213 1.00 7.49  ? 203 LEU A CD1   1 
ATOM   1564 C CD2   . LEU A 1 223 ? 32.089  -5.836  -27.020 1.00 8.98  ? 203 LEU A CD2   1 
ATOM   1565 N N     . ALA A 1 224 ? 27.570  -4.077  -24.637 1.00 4.13  ? 204 ALA A N     1 
ATOM   1566 C CA    . ALA A 1 224 ? 26.539  -3.050  -24.469 1.00 4.05  ? 204 ALA A CA    1 
ATOM   1567 C C     . ALA A 1 224 ? 26.849  -2.122  -23.312 1.00 4.12  ? 204 ALA A C     1 
ATOM   1568 O O     . ALA A 1 224 ? 26.690  -0.936  -23.473 1.00 4.11  ? 204 ALA A O     1 
ATOM   1569 C CB    . ALA A 1 224 ? 25.195  -3.715  -24.299 1.00 3.80  ? 204 ALA A CB    1 
ATOM   1570 N N     . VAL A 1 225 ? 27.362  -2.659  -22.200 1.00 4.60  ? 205 VAL A N     1 
ATOM   1571 C CA    . VAL A 1 225 ? 27.726  -1.793  -21.091 1.00 5.27  ? 205 VAL A CA    1 
ATOM   1572 C C     . VAL A 1 225 ? 28.686  -0.718  -21.572 1.00 6.04  ? 205 VAL A C     1 
ATOM   1573 O O     . VAL A 1 225 ? 28.531  0.456   -21.283 1.00 5.78  ? 205 VAL A O     1 
ATOM   1574 C CB    . VAL A 1 225 ? 28.295  -2.587  -19.908 1.00 5.58  ? 205 VAL A CB    1 
ATOM   1575 C CG1   . VAL A 1 225 ? 28.842  -1.635  -18.881 1.00 5.82  ? 205 VAL A CG1   1 
ATOM   1576 C CG2   . VAL A 1 225 ? 27.290  -3.540  -19.295 1.00 5.32  ? 205 VAL A CG2   1 
ATOM   1577 N N     . GLN A 1 226 ? 29.719  -1.170  -22.284 1.00 7.42  ? 206 GLN A N     1 
ATOM   1578 C CA    . GLN A 1 226 ? 30.754  -0.228  -22.676 1.00 9.01  ? 206 GLN A CA    1 
ATOM   1579 C C     . GLN A 1 226 ? 30.216  0.767   -23.707 1.00 7.63  ? 206 GLN A C     1 
ATOM   1580 O O     . GLN A 1 226 ? 30.481  1.972   -23.618 1.00 7.97  ? 206 GLN A O     1 
ATOM   1581 C CB    . GLN A 1 226 ? 31.985  -1.005  -23.161 1.00 12.58 ? 206 GLN A CB    1 
ATOM   1582 C CG    . GLN A 1 226 ? 32.603  -1.957  -22.126 1.00 18.99 ? 206 GLN A CG    1 
ATOM   1583 C CD    . GLN A 1 226 ? 33.249  -1.435  -20.846 1.00 30.03 ? 206 GLN A CD    1 
ATOM   1584 O OE1   . GLN A 1 226 ? 34.440  -1.680  -20.629 1.00 41.42 ? 206 GLN A OE1   1 
ATOM   1585 N NE2   . GLN A 1 226 ? 32.492  -0.865  -19.901 1.00 26.32 ? 206 GLN A NE2   1 
ATOM   1586 N N     . ALA A 1 227 ? 29.391  0.290   -24.663 1.00 5.99  ? 207 ALA A N     1 
ATOM   1587 C CA    . ALA A 1 227 ? 28.802  1.182   -25.658 1.00 5.44  ? 207 ALA A CA    1 
ATOM   1588 C C     . ALA A 1 227 ? 27.876  2.201   -24.979 1.00 5.17  ? 207 ALA A C     1 
ATOM   1589 O O     . ALA A 1 227 ? 27.784  3.344   -25.405 1.00 5.23  ? 207 ALA A O     1 
ATOM   1590 C CB    . ALA A 1 227 ? 28.050  0.379   -26.706 1.00 5.60  ? 207 ALA A CB    1 
ATOM   1591 N N     . MET A 1 228 ? 27.117  1.755   -23.993 1.00 5.06  ? 208 MET A N     1 
ATOM   1592 C CA    . MET A 1 228 ? 26.194  2.618   -23.275 1.00 5.17  ? 208 MET A CA    1 
ATOM   1593 C C     . MET A 1 228 ? 26.917  3.717   -22.508 1.00 6.03  ? 208 MET A C     1 
ATOM   1594 O O     . MET A 1 228 ? 26.490  4.846   -22.570 1.00 7.39  ? 208 MET A O     1 
ATOM   1595 C CB    . MET A 1 228 ? 25.370  1.811   -22.280 1.00 4.64  ? 208 MET A CB    1 
ATOM   1596 C CG    . MET A 1 228 ? 24.370  0.874   -22.948 1.00 4.40  ? 208 MET A CG    1 
ATOM   1597 S SD    . MET A 1 228 ? 23.731  -0.464  -21.927 1.00 4.24  ? 208 MET A SD    1 
ATOM   1598 C CE    . MET A 1 228 ? 22.633  0.444   -20.854 1.00 4.38  ? 208 MET A CE    1 
ATOM   1599 N N     . ARG A 1 229 ? 28.026  3.378   -21.854 1.00 7.57  ? 209 ARG A N     1 
ATOM   1600 C CA    . ARG A 1 229 ? 28.741  4.429   -21.126 1.00 8.90  ? 209 ARG A CA    1 
ATOM   1601 C C     . ARG A 1 229 ? 29.297  5.467   -22.085 1.00 9.54  ? 209 ARG A C     1 
ATOM   1602 O O     . ARG A 1 229 ? 29.196  6.686   -21.812 1.00 12.08 ? 209 ARG A O     1 
ATOM   1603 C CB    . ARG A 1 229 ? 29.792  3.834   -20.217 1.00 10.17 ? 209 ARG A CB    1 
ATOM   1604 C CG    . ARG A 1 229 ? 29.085  3.119   -19.080 1.00 10.91 ? 209 ARG A CG    1 
ATOM   1605 C CD    . ARG A 1 229 ? 30.021  2.833   -17.984 1.00 9.61  ? 209 ARG A CD    1 
ATOM   1606 N NE    . ARG A 1 229 ? 29.610  1.781   -17.117 1.00 8.64  ? 209 ARG A NE    1 
ATOM   1607 C CZ    . ARG A 1 229 ? 28.711  1.863   -16.155 1.00 7.75  ? 209 ARG A CZ    1 
ATOM   1608 N NH1   . ARG A 1 229 ? 27.973  2.972   -15.986 1.00 8.19  ? 209 ARG A NH1   1 
ATOM   1609 N NH2   . ARG A 1 229 ? 28.548  0.794   -15.394 1.00 7.93  ? 209 ARG A NH2   1 
ATOM   1610 N N     . ALA A 1 230 ? 29.735  5.001   -23.245 1.00 8.41  ? 210 ALA A N     1 
ATOM   1611 C CA    . ALA A 1 230 ? 30.263  5.921   -24.249 1.00 9.18  ? 210 ALA A CA    1 
ATOM   1612 C C     . ALA A 1 230 ? 29.191  6.829   -24.842 1.00 10.31 ? 210 ALA A C     1 
ATOM   1613 O O     . ALA A 1 230 ? 29.416  8.013   -25.087 1.00 12.84 ? 210 ALA A O     1 
ATOM   1614 C CB    . ALA A 1 230 ? 30.986  5.151   -25.311 1.00 9.23  ? 210 ALA A CB    1 
ATOM   1615 N N     . ALA A 1 231 ? 27.980  6.299   -25.075 1.00 8.86  ? 211 ALA A N     1 
ATOM   1616 C CA    . ALA A 1 231 ? 26.926  7.022   -25.760 1.00 9.34  ? 211 ALA A CA    1 
ATOM   1617 C C     . ALA A 1 231 ? 26.147  7.915   -24.807 1.00 10.09 ? 211 ALA A C     1 
ATOM   1618 O O     . ALA A 1 231 ? 25.460  8.825   -25.266 1.00 11.97 ? 211 ALA A O     1 
ATOM   1619 C CB    . ALA A 1 231 ? 25.970  6.009   -26.363 1.00 9.24  ? 211 ALA A CB    1 
ATOM   1620 N N     . ALA A 1 232 ? 26.197  7.633   -23.528 1.00 12.15 ? 212 ALA A N     1 
ATOM   1621 C CA    . ALA A 1 232 ? 25.258  8.271   -22.602 1.00 14.37 ? 212 ALA A CA    1 
ATOM   1622 C C     . ALA A 1 232 ? 25.590  9.737   -22.408 1.00 14.54 ? 212 ALA A C     1 
ATOM   1623 O O     . ALA A 1 232 ? 26.768  10.087  -22.309 1.00 13.45 ? 212 ALA A O     1 
ATOM   1624 C CB    . ALA A 1 232 ? 25.323  7.577   -21.288 1.00 16.28 ? 212 ALA A CB    1 
ATOM   1625 N N     . PRO A 1 233 ? 24.600  10.659  -22.336 1.00 13.14 ? 213 PRO A N     1 
ATOM   1626 C CA    . PRO A 1 233 ? 24.970  12.035  -22.053 1.00 14.28 ? 213 PRO A CA    1 
ATOM   1627 C C     . PRO A 1 233 ? 25.221  12.339  -20.585 1.00 14.86 ? 213 PRO A C     1 
ATOM   1628 O O     . PRO A 1 233 ? 25.587  13.473  -20.290 1.00 16.89 ? 213 PRO A O     1 
ATOM   1629 C CB    . PRO A 1 233 ? 23.771  12.803  -22.583 1.00 14.93 ? 213 PRO A CB    1 
ATOM   1630 C CG    . PRO A 1 233 ? 22.626  11.858  -22.177 1.00 13.99 ? 213 PRO A CG    1 
ATOM   1631 C CD    . PRO A 1 233 ? 23.151  10.498  -22.591 1.00 14.80 ? 213 PRO A CD    1 
ATOM   1632 N N     . GLN A 1 234 ? 24.972  11.392  -19.658 1.00 13.33 ? 214 GLN A N     1 
ATOM   1633 C CA    . GLN A 1 234 ? 25.246  11.576  -18.249 1.00 12.34 ? 214 GLN A CA    1 
ATOM   1634 C C     . GLN A 1 234 ? 25.667  10.230  -17.674 1.00 11.55 ? 214 GLN A C     1 
ATOM   1635 O O     . GLN A 1 234 ? 25.396  9.217   -18.282 1.00 10.91 ? 214 GLN A O     1 
ATOM   1636 C CB    . GLN A 1 234 ? 24.031  12.096  -17.486 1.00 12.54 ? 214 GLN A CB    1 
ATOM   1637 C CG    . GLN A 1 234 ? 22.889  11.101  -17.370 1.00 13.41 ? 214 GLN A CG    1 
ATOM   1638 C CD    . GLN A 1 234 ? 21.703  11.573  -16.562 1.00 14.85 ? 214 GLN A CD    1 
ATOM   1639 O OE1   . GLN A 1 234 ? 21.836  12.179  -15.497 1.00 16.90 ? 214 GLN A OE1   1 
ATOM   1640 N NE2   . GLN A 1 234 ? 20.510  11.247  -17.026 1.00 15.09 ? 214 GLN A NE2   1 
ATOM   1641 N N     . PRO A 1 235 ? 26.296  10.151  -16.501 1.00 11.81 ? 215 PRO A N     1 
ATOM   1642 C CA    . PRO A 1 235 ? 26.606  8.856   -15.902 1.00 11.99 ? 215 PRO A CA    1 
ATOM   1643 C C     . PRO A 1 235 ? 25.351  8.028   -15.682 1.00 9.26  ? 215 PRO A C     1 
ATOM   1644 O O     . PRO A 1 235 ? 24.310  8.557   -15.299 1.00 9.87  ? 215 PRO A O     1 
ATOM   1645 C CB    . PRO A 1 235 ? 27.224  9.208   -14.550 1.00 13.86 ? 215 PRO A CB    1 
ATOM   1646 C CG    . PRO A 1 235 ? 27.886  10.556  -14.861 1.00 14.55 ? 215 PRO A CG    1 
ATOM   1647 C CD    . PRO A 1 235 ? 26.882  11.286  -15.730 1.00 14.14 ? 215 PRO A CD    1 
ATOM   1648 N N     . LEU A 1 236 ? 25.465  6.739   -16.014 1.00 7.54  ? 216 LEU A N     1 
ATOM   1649 C CA    . LEU A 1 236 ? 24.338  5.814   -15.863 1.00 6.53  ? 216 LEU A CA    1 
ATOM   1650 C C     . LEU A 1 236 ? 24.619  4.820   -14.757 1.00 6.34  ? 216 LEU A C     1 
ATOM   1651 O O     . LEU A 1 236 ? 25.799  4.492   -14.441 1.00 7.25  ? 216 LEU A O     1 
ATOM   1652 C CB    . LEU A 1 236 ? 24.125  5.078   -17.179 1.00 6.69  ? 216 LEU A CB    1 
ATOM   1653 C CG    . LEU A 1 236 ? 23.841  5.884   -18.449 1.00 6.64  ? 216 LEU A CG    1 
ATOM   1654 C CD1   . LEU A 1 236 ? 23.585  4.921   -19.610 1.00 7.29  ? 216 LEU A CD1   1 
ATOM   1655 C CD2   . LEU A 1 236 ? 22.667  6.832   -18.274 1.00 7.21  ? 216 LEU A CD2   1 
ATOM   1656 N N     . GLN A 1 237 ? 23.534  4.217   -14.228 1.00 5.22  ? 217 GLN A N     1 
ATOM   1657 C CA    . GLN A 1 237 ? 23.612  3.094   -13.326 1.00 5.22  ? 217 GLN A CA    1 
ATOM   1658 C C     . GLN A 1 237 ? 23.149  1.872   -14.114 1.00 4.54  ? 217 GLN A C     1 
ATOM   1659 O O     . GLN A 1 237 ? 21.938  1.685   -14.314 1.00 3.97  ? 217 GLN A O     1 
ATOM   1660 C CB    . GLN A 1 237 ? 22.737  3.302   -12.085 1.00 6.36  ? 217 GLN A CB    1 
ATOM   1661 C CG    . GLN A 1 237 ? 23.050  4.593   -11.334 1.00 7.77  ? 217 GLN A CG    1 
ATOM   1662 C CD    . GLN A 1 237 ? 24.502  4.754   -10.948 1.00 9.83  ? 217 GLN A CD    1 
ATOM   1663 O OE1   . GLN A 1 237 ? 25.097  3.866   -10.343 1.00 11.95 ? 217 GLN A OE1   1 
ATOM   1664 N NE2   . GLN A 1 237 ? 25.027  5.932   -11.256 1.00 12.68 ? 217 GLN A NE2   1 
ATOM   1665 N N     . ILE A 1 238 ? 24.102  1.058   -14.553 1.00 4.32  ? 218 ILE A N     1 
ATOM   1666 C CA    . ILE A 1 238 ? 23.842  -0.056  -15.447 1.00 4.30  ? 218 ILE A CA    1 
ATOM   1667 C C     . ILE A 1 238 ? 23.977  -1.356  -14.706 1.00 4.26  ? 218 ILE A C     1 
ATOM   1668 O O     . ILE A 1 238 ? 24.955  -1.561  -13.963 1.00 4.30  ? 218 ILE A O     1 
ATOM   1669 C CB    . ILE A 1 238 ? 24.776  -0.045  -16.666 1.00 4.16  ? 218 ILE A CB    1 
ATOM   1670 C CG1   . ILE A 1 238 ? 24.754  1.305   -17.381 1.00 4.65  ? 218 ILE A CG1   1 
ATOM   1671 C CG2   . ILE A 1 238 ? 24.437  -1.209  -17.599 1.00 4.09  ? 218 ILE A CG2   1 
ATOM   1672 C CD1   . ILE A 1 238 ? 25.670  1.417   -18.558 1.00 4.94  ? 218 ILE A CD1   1 
ATOM   1673 N N     . GLY A 1 239 ? 22.980  -2.220  -14.892 1.00 3.59  ? 219 GLY A N     1 
ATOM   1674 C CA    . GLY A 1 239 ? 22.927  -3.552  -14.297 1.00 3.38  ? 219 GLY A CA    1 
ATOM   1675 C C     . GLY A 1 239 ? 22.594  -4.608  -15.346 1.00 3.15  ? 219 GLY A C     1 
ATOM   1676 O O     . GLY A 1 239 ? 22.448  -4.299  -16.513 1.00 3.26  ? 219 GLY A O     1 
ATOM   1677 N N     . ILE A 1 240 ? 22.539  -5.837  -14.858 1.00 2.78  ? 220 ILE A N     1 
ATOM   1678 C CA    . ILE A 1 240 ? 21.980  -6.976  -15.567 1.00 2.61  ? 220 ILE A CA    1 
ATOM   1679 C C     . ILE A 1 240 ? 21.017  -7.625  -14.603 1.00 2.74  ? 220 ILE A C     1 
ATOM   1680 O O     . ILE A 1 240 ? 21.112  -7.467  -13.364 1.00 2.84  ? 220 ILE A O     1 
ATOM   1681 C CB    . ILE A 1 240 ? 23.082  -7.957  -16.035 1.00 2.66  ? 220 ILE A CB    1 
ATOM   1682 C CG1   . ILE A 1 240 ? 22.525  -9.021  -16.982 1.00 2.73  ? 220 ILE A CG1   1 
ATOM   1683 C CG2   . ILE A 1 240 ? 23.795  -8.614  -14.869 1.00 2.63  ? 220 ILE A CG2   1 
ATOM   1684 C CD1   . ILE A 1 240 ? 23.582  -9.931  -17.634 1.00 2.97  ? 220 ILE A CD1   1 
ATOM   1685 N N     . VAL A 1 241 ? 20.020  -8.321  -15.130 1.00 2.58  ? 221 VAL A N     1 
ATOM   1686 C CA    . VAL A 1 241 ? 19.008  -8.954  -14.321 1.00 2.73  ? 221 VAL A CA    1 
ATOM   1687 C C     . VAL A 1 241 ? 19.092  -10.464 -14.542 1.00 2.77  ? 221 VAL A C     1 
ATOM   1688 O O     . VAL A 1 241 ? 19.031  -10.948 -15.675 1.00 2.70  ? 221 VAL A O     1 
ATOM   1689 C CB    . VAL A 1 241 ? 17.608  -8.436  -14.685 1.00 2.88  ? 221 VAL A CB    1 
ATOM   1690 C CG1   . VAL A 1 241 ? 16.542  -9.310  -14.052 1.00 3.06  ? 221 VAL A CG1   1 
ATOM   1691 C CG2   . VAL A 1 241 ? 17.442  -6.952  -14.298 1.00 3.06  ? 221 VAL A CG2   1 
ATOM   1692 N N     . LEU A 1 242 ? 19.289  -11.211 -13.454 1.00 3.17  ? 222 LEU A N     1 
ATOM   1693 C CA    . LEU A 1 242 ? 19.378  -12.660 -13.506 1.00 3.33  ? 222 LEU A CA    1 
ATOM   1694 C C     . LEU A 1 242 ? 18.239  -13.278 -12.715 1.00 3.26  ? 222 LEU A C     1 
ATOM   1695 O O     . LEU A 1 242 ? 17.971  -12.858 -11.581 1.00 3.51  ? 222 LEU A O     1 
ATOM   1696 C CB    . LEU A 1 242 ? 20.691  -13.149 -12.866 1.00 3.63  ? 222 LEU A CB    1 
ATOM   1697 C CG    . LEU A 1 242 ? 21.962  -12.581 -13.458 1.00 4.17  ? 222 LEU A CG    1 
ATOM   1698 C CD1   . LEU A 1 242 ? 23.219  -13.112 -12.722 1.00 4.61  ? 222 LEU A CD1   1 
ATOM   1699 C CD2   . LEU A 1 242 ? 22.104  -12.873 -14.958 1.00 4.14  ? 222 LEU A CD2   1 
ATOM   1700 N N     . ASN A 1 243 ? 17.641  -14.327 -13.245 1.00 3.48  ? 223 ASN A N     1 
ATOM   1701 C CA    . ASN A 1 243 ? 16.848  -15.233 -12.423 1.00 3.95  ? 223 ASN A CA    1 
ATOM   1702 C C     . ASN A 1 243 ? 17.797  -16.127 -11.632 1.00 4.27  ? 223 ASN A C     1 
ATOM   1703 O O     . ASN A 1 243 ? 18.739  -16.681 -12.184 1.00 5.20  ? 223 ASN A O     1 
ATOM   1704 C CB    . ASN A 1 243 ? 15.894  -16.109 -13.233 1.00 4.55  ? 223 ASN A CB    1 
ATOM   1705 C CG    . ASN A 1 243 ? 16.572  -16.921 -14.294 1.00 5.43  ? 223 ASN A CG    1 
ATOM   1706 O OD1   . ASN A 1 243 ? 17.197  -16.405 -15.214 1.00 5.40  ? 223 ASN A OD1   1 
ATOM   1707 N ND2   . ASN A 1 243 ? 16.475  -18.243 -14.168 1.00 7.34  ? 223 ASN A ND2   1 
ATOM   1708 N N     . LEU A 1 244 ? 17.565  -16.198 -10.326 1.00 4.48  ? 224 LEU A N     1 
ATOM   1709 C CA    . LEU A 1 244 ? 18.374  -17.072 -9.478  1.00 4.84  ? 224 LEU A CA    1 
ATOM   1710 C C     . LEU A 1 244 ? 17.460  -18.033 -8.760  1.00 5.67  ? 224 LEU A C     1 
ATOM   1711 O O     . LEU A 1 244 ? 16.412  -17.670 -8.232  1.00 5.70  ? 224 LEU A O     1 
ATOM   1712 C CB    . LEU A 1 244 ? 19.198  -16.232 -8.513  1.00 4.81  ? 224 LEU A CB    1 
ATOM   1713 C CG    . LEU A 1 244 ? 20.201  -15.291 -9.160  1.00 5.01  ? 224 LEU A CG    1 
ATOM   1714 C CD1   . LEU A 1 244 ? 20.930  -14.430 -8.108  1.00 5.48  ? 224 LEU A CD1   1 
ATOM   1715 C CD2   . LEU A 1 244 ? 21.258  -16.014 -9.981  1.00 4.85  ? 224 LEU A CD2   1 
ATOM   1716 N N     . THR A 1 245 ? 17.858  -19.309 -8.764  1.00 6.86  ? 225 THR A N     1 
ATOM   1717 C CA    . THR A 1 245 ? 17.108  -20.369 -8.137  1.00 7.46  ? 225 THR A CA    1 
ATOM   1718 C C     . THR A 1 245 ? 17.965  -21.014 -7.050  1.00 7.72  ? 225 THR A C     1 
ATOM   1719 O O     . THR A 1 245 ? 18.831  -21.840 -7.352  1.00 7.41  ? 225 THR A O     1 
ATOM   1720 C CB    . THR A 1 245 ? 16.660  -21.453 -9.119  1.00 8.99  ? 225 THR A CB    1 
ATOM   1721 O OG1   . THR A 1 245 ? 15.817  -20.792 -10.069 1.00 11.09 ? 225 THR A OG1   1 
ATOM   1722 C CG2   . THR A 1 245 ? 15.875  -22.543 -8.427  1.00 9.36  ? 225 THR A CG2   1 
ATOM   1723 N N     . PRO A 1 246 ? 17.743  -20.676 -5.769  1.00 7.78  ? 226 PRO A N     1 
ATOM   1724 C CA    . PRO A 1 246 ? 18.501  -21.358 -4.700  1.00 8.49  ? 226 PRO A CA    1 
ATOM   1725 C C     . PRO A 1 246 ? 18.156  -22.842 -4.736  1.00 7.42  ? 226 PRO A C     1 
ATOM   1726 O O     . PRO A 1 246 ? 16.986  -23.205 -4.844  1.00 8.63  ? 226 PRO A O     1 
ATOM   1727 C CB    . PRO A 1 246 ? 17.987  -20.678 -3.428  1.00 8.86  ? 226 PRO A CB    1 
ATOM   1728 C CG    . PRO A 1 246 ? 16.620  -20.153 -3.775  1.00 8.29  ? 226 PRO A CG    1 
ATOM   1729 C CD    . PRO A 1 246 ? 16.731  -19.742 -5.238  1.00 8.08  ? 226 PRO A CD    1 
ATOM   1730 N N     . THR A 1 247 ? 19.217  -23.669 -4.584  1.00 8.49  ? 227 THR A N     1 
ATOM   1731 C CA    . THR A 1 247 ? 19.086  -25.102 -4.804  1.00 8.52  ? 227 THR A CA    1 
ATOM   1732 C C     . THR A 1 247 ? 19.502  -25.823 -3.528  1.00 8.07  ? 227 THR A C     1 
ATOM   1733 O O     . THR A 1 247 ? 20.409  -25.373 -2.854  1.00 8.88  ? 227 THR A O     1 
ATOM   1734 C CB    . THR A 1 247 ? 19.947  -25.538 -5.989  1.00 10.06 ? 227 THR A CB    1 
ATOM   1735 O OG1   . THR A 1 247 ? 19.584  -24.747 -7.141  1.00 12.76 ? 227 THR A OG1   1 
ATOM   1736 C CG2   . THR A 1 247 ? 19.778  -26.979 -6.390  1.00 10.98 ? 227 THR A CG2   1 
ATOM   1737 N N     . TYR A 1 248 ? 18.745  -26.841 -3.195  1.00 8.25  ? 228 TYR A N     1 
ATOM   1738 C CA    . TYR A 1 248 ? 18.959  -27.532 -1.927  1.00 8.66  ? 228 TYR A CA    1 
ATOM   1739 C C     . TYR A 1 248 ? 18.941  -29.013 -2.268  1.00 8.48  ? 228 TYR A C     1 
ATOM   1740 O O     . TYR A 1 248 ? 17.994  -29.508 -2.868  1.00 9.67  ? 228 TYR A O     1 
ATOM   1741 C CB    . TYR A 1 248 ? 17.849  -27.206 -0.934  1.00 8.23  ? 228 TYR A CB    1 
ATOM   1742 C CG    . TYR A 1 248 ? 17.637  -25.746 -0.679  1.00 8.66  ? 228 TYR A CG    1 
ATOM   1743 C CD1   . TYR A 1 248 ? 16.903  -25.016 -1.573  1.00 10.16 ? 228 TYR A CD1   1 
ATOM   1744 C CD2   . TYR A 1 248 ? 18.181  -25.097 0.413   1.00 8.37  ? 228 TYR A CD2   1 
ATOM   1745 C CE1   . TYR A 1 248 ? 16.735  -23.656 -1.410  1.00 10.31 ? 228 TYR A CE1   1 
ATOM   1746 C CE2   . TYR A 1 248 ? 18.012  -23.739 0.598   1.00 9.43  ? 228 TYR A CE2   1 
ATOM   1747 C CZ    . TYR A 1 248 ? 17.290  -23.019 -0.330  1.00 10.49 ? 228 TYR A CZ    1 
ATOM   1748 O OH    . TYR A 1 248 ? 17.085  -21.679 -0.088  1.00 12.16 ? 228 TYR A OH    1 
ATOM   1749 N N     . PRO A 1 249 ? 19.900  -29.821 -1.785  1.00 8.83  ? 229 PRO A N     1 
ATOM   1750 C CA    . PRO A 1 249 ? 19.766  -31.252 -2.058  1.00 9.49  ? 229 PRO A CA    1 
ATOM   1751 C C     . PRO A 1 249 ? 18.644  -31.837 -1.223  1.00 9.33  ? 229 PRO A C     1 
ATOM   1752 O O     . PRO A 1 249 ? 18.476  -31.480 -0.060  1.00 8.95  ? 229 PRO A O     1 
ATOM   1753 C CB    . PRO A 1 249 ? 21.144  -31.766 -1.663  1.00 10.22 ? 229 PRO A CB    1 
ATOM   1754 C CG    . PRO A 1 249 ? 21.566  -30.827 -0.607  1.00 10.22 ? 229 PRO A CG    1 
ATOM   1755 C CD    . PRO A 1 249 ? 21.039  -29.440 -0.972  1.00 9.55  ? 229 PRO A CD    1 
ATOM   1756 N N     . ALA A 1 250 ? 17.937  -32.806 -1.820  1.00 9.76  ? 230 ALA A N     1 
ATOM   1757 C CA    . ALA A 1 250 ? 16.809  -33.461 -1.207  1.00 11.49 ? 230 ALA A CA    1 
ATOM   1758 C C     . ALA A 1 250 ? 17.233  -34.344 -0.037  1.00 11.36 ? 230 ALA A C     1 
ATOM   1759 O O     . ALA A 1 250 ? 16.481  -34.523 0.917   1.00 14.67 ? 230 ALA A O     1 
ATOM   1760 C CB    . ALA A 1 250 ? 16.128  -34.276 -2.268  1.00 13.70 ? 230 ALA A CB    1 
ATOM   1761 N N     . SER A 1 251 ? 18.472  -34.858 -0.084  1.00 10.29 ? 231 SER A N     1 
ATOM   1762 C CA    . SER A 1 251 ? 19.088  -35.584 1.022   1.00 10.07 ? 231 SER A CA    1 
ATOM   1763 C C     . SER A 1 251 ? 20.554  -35.179 1.038   1.00 10.01 ? 231 SER A C     1 
ATOM   1764 O O     . SER A 1 251 ? 21.016  -34.503 0.136   1.00 9.22  ? 231 SER A O     1 
ATOM   1765 C CB    . SER A 1 251 ? 18.992  -37.103 0.875   1.00 9.35  ? 231 SER A CB    1 
ATOM   1766 O OG    . SER A 1 251 ? 19.851  -37.583 -0.134  1.00 10.50 ? 231 SER A OG    1 
ATOM   1767 N N     . ASP A 1 252 ? 21.300  -35.681 2.014   1.00 10.51 ? 232 ASP A N     1 
ATOM   1768 C CA    . ASP A 1 252 ? 22.712  -35.378 2.153   1.00 11.62 ? 232 ASP A CA    1 
ATOM   1769 C C     . ASP A 1 252 ? 23.558  -36.443 1.454   1.00 9.27  ? 232 ASP A C     1 
ATOM   1770 O O     . ASP A 1 252 ? 24.776  -36.413 1.560   1.00 9.07  ? 232 ASP A O     1 
ATOM   1771 C CB    . ASP A 1 252 ? 23.043  -35.226 3.638   1.00 15.70 ? 232 ASP A CB    1 
ATOM   1772 C CG    . ASP A 1 252 ? 23.160  -36.515 4.450   1.00 21.94 ? 232 ASP A CG    1 
ATOM   1773 O OD1   . ASP A 1 252 ? 22.807  -37.612 3.939   1.00 26.96 ? 232 ASP A OD1   1 
ATOM   1774 O OD2   . ASP A 1 252 ? 23.636  -36.421 5.613   1.00 32.09 ? 232 ASP A OD2   1 
ATOM   1775 N N     . SER A 1 253 ? 22.958  -37.322 0.638   1.00 8.74  ? 233 SER A N     1 
ATOM   1776 C CA    . SER A 1 253 ? 23.698  -38.296 -0.124  1.00 9.89  ? 233 SER A CA    1 
ATOM   1777 C C     . SER A 1 253 ? 24.646  -37.598 -1.081  1.00 9.59  ? 233 SER A C     1 
ATOM   1778 O O     . SER A 1 253 ? 24.314  -36.556 -1.676  1.00 8.54  ? 233 SER A O     1 
ATOM   1779 C CB    . SER A 1 253 ? 22.797  -39.232 -0.878  1.00 12.16 ? 233 SER A CB    1 
ATOM   1780 O OG    . SER A 1 253 ? 22.224  -38.596 -2.028  1.00 15.68 ? 233 SER A OG    1 
ATOM   1781 N N     . PRO A 1 254 ? 25.828  -38.146 -1.385  1.00 9.14  ? 234 PRO A N     1 
ATOM   1782 C CA    . PRO A 1 254 ? 26.694  -37.569 -2.407  1.00 9.11  ? 234 PRO A CA    1 
ATOM   1783 C C     . PRO A 1 254 ? 26.008  -37.298 -3.754  1.00 9.55  ? 234 PRO A C     1 
ATOM   1784 O O     . PRO A 1 254 ? 26.300  -36.300 -4.415  1.00 9.74  ? 234 PRO A O     1 
ATOM   1785 C CB    . PRO A 1 254 ? 27.795  -38.641 -2.509  1.00 10.01 ? 234 PRO A CB    1 
ATOM   1786 C CG    . PRO A 1 254 ? 27.882  -39.162 -1.106  1.00 10.57 ? 234 PRO A CG    1 
ATOM   1787 C CD    . PRO A 1 254 ? 26.442  -39.296 -0.675  1.00 10.21 ? 234 PRO A CD    1 
ATOM   1788 N N     . GLU A 1 255 ? 25.116  -38.189 -4.169  1.00 9.80  ? 235 GLU A N     1 
ATOM   1789 C CA    . GLU A 1 255 ? 24.452  -38.072 -5.457  1.00 10.94 ? 235 GLU A CA    1 
ATOM   1790 C C     . GLU A 1 255 ? 23.519  -36.861 -5.458  1.00 9.33  ? 235 GLU A C     1 
ATOM   1791 O O     . GLU A 1 255 ? 23.485  -36.135 -6.447  1.00 9.62  ? 235 GLU A O     1 
ATOM   1792 C CB    . GLU A 1 255 ? 23.676  -39.359 -5.768  1.00 15.06 ? 235 GLU A CB    1 
ATOM   1793 C CG    . GLU A 1 255 ? 24.569  -40.596 -5.894  1.00 20.33 ? 235 GLU A CG    1 
ATOM   1794 C CD    . GLU A 1 255 ? 25.090  -41.269 -4.622  1.00 23.17 ? 235 GLU A CD    1 
ATOM   1795 O OE1   . GLU A 1 255 ? 24.680  -40.933 -3.493  1.00 18.32 ? 235 GLU A OE1   1 
ATOM   1796 O OE2   . GLU A 1 255 ? 25.977  -42.147 -4.775  1.00 33.77 ? 235 GLU A OE2   1 
ATOM   1797 N N     . ASP A 1 256 ? 22.794  -36.661 -4.368  1.00 8.66  ? 236 ASP A N     1 
ATOM   1798 C CA    . ASP A 1 256 ? 21.846  -35.534 -4.352  1.00 8.84  ? 236 ASP A CA    1 
ATOM   1799 C C     . ASP A 1 256 ? 22.580  -34.218 -4.139  1.00 9.05  ? 236 ASP A C     1 
ATOM   1800 O O     . ASP A 1 256 ? 22.212  -33.171 -4.688  1.00 8.51  ? 236 ASP A O     1 
ATOM   1801 C CB    . ASP A 1 256 ? 20.768  -35.701 -3.294  1.00 8.78  ? 236 ASP A CB    1 
ATOM   1802 C CG    . ASP A 1 256 ? 19.827  -36.855 -3.599  1.00 10.64 ? 236 ASP A CG    1 
ATOM   1803 O OD1   . ASP A 1 256 ? 19.794  -37.281 -4.796  1.00 11.55 ? 236 ASP A OD1   1 
ATOM   1804 O OD2   . ASP A 1 256 ? 19.140  -37.275 -2.660  1.00 12.58 ? 236 ASP A OD2   1 
ATOM   1805 N N     . VAL A 1 257 ? 23.610  -34.198 -3.291  1.00 7.59  ? 237 VAL A N     1 
ATOM   1806 C CA    . VAL A 1 257 ? 24.405  -32.985 -3.148  1.00 7.01  ? 237 VAL A CA    1 
ATOM   1807 C C     . VAL A 1 257 ? 25.035  -32.586 -4.481  1.00 7.61  ? 237 VAL A C     1 
ATOM   1808 O O     . VAL A 1 257 ? 25.081  -31.402 -4.829  1.00 7.03  ? 237 VAL A O     1 
ATOM   1809 C CB    . VAL A 1 257 ? 25.435  -33.165 -2.030  1.00 8.11  ? 237 VAL A CB    1 
ATOM   1810 C CG1   . VAL A 1 257 ? 26.353  -31.973 -1.924  1.00 9.58  ? 237 VAL A CG1   1 
ATOM   1811 C CG2   . VAL A 1 257 ? 24.714  -33.373 -0.705  1.00 7.84  ? 237 VAL A CG2   1 
ATOM   1812 N N     . ALA A 1 258 ? 25.583  -33.544 -5.230  1.00 6.66  ? 238 ALA A N     1 
ATOM   1813 C CA    . ALA A 1 258 ? 26.198  -33.237 -6.497  1.00 6.70  ? 238 ALA A CA    1 
ATOM   1814 C C     . ALA A 1 258 ? 25.149  -32.716 -7.469  1.00 6.70  ? 238 ALA A C     1 
ATOM   1815 O O     . ALA A 1 258 ? 25.483  -31.810 -8.207  1.00 6.81  ? 238 ALA A O     1 
ATOM   1816 C CB    . ALA A 1 258 ? 26.917  -34.481 -7.039  1.00 7.67  ? 238 ALA A CB    1 
ATOM   1817 N N     . ALA A 1 259 ? 23.968  -33.320 -7.453  1.00 6.80  ? 239 ALA A N     1 
ATOM   1818 C CA    . ALA A 1 259 ? 22.918  -32.835 -8.351  1.00 7.11  ? 239 ALA A CA    1 
ATOM   1819 C C     . ALA A 1 259 ? 22.605  -31.375 -8.026  1.00 7.66  ? 239 ALA A C     1 
ATOM   1820 O O     . ALA A 1 259 ? 22.438  -30.541 -8.927  1.00 6.82  ? 239 ALA A O     1 
ATOM   1821 C CB    . ALA A 1 259 ? 21.691  -33.678 -8.229  1.00 7.72  ? 239 ALA A CB    1 
ATOM   1822 N N     . ALA A 1 260 ? 22.476  -31.064 -6.736  1.00 6.47  ? 240 ALA A N     1 
ATOM   1823 C CA    . ALA A 1 260 ? 22.222  -29.678 -6.356  1.00 6.23  ? 240 ALA A CA    1 
ATOM   1824 C C     . ALA A 1 260 ? 23.315  -28.766 -6.867  1.00 6.32  ? 240 ALA A C     1 
ATOM   1825 O O     . ALA A 1 260 ? 23.048  -27.660 -7.371  1.00 6.61  ? 240 ALA A O     1 
ATOM   1826 C CB    . ALA A 1 260 ? 22.030  -29.600 -4.859  1.00 6.36  ? 240 ALA A CB    1 
ATOM   1827 N N     . ARG A 1 261 ? 24.569  -29.175 -6.759  1.00 6.43  ? 241 ARG A N     1 
ATOM   1828 C CA    . ARG A 1 261 ? 25.677  -28.366 -7.217  1.00 7.10  ? 241 ARG A CA    1 
ATOM   1829 C C     . ARG A 1 261 ? 25.572  -28.161 -8.721  1.00 6.86  ? 241 ARG A C     1 
ATOM   1830 O O     . ARG A 1 261 ? 25.832  -27.076 -9.210  1.00 6.86  ? 241 ARG A O     1 
ATOM   1831 C CB    . ARG A 1 261 ? 27.028  -28.985 -6.848  1.00 8.15  ? 241 ARG A CB    1 
ATOM   1832 C CG    . ARG A 1 261 ? 27.280  -28.946 -5.358  1.00 11.88 ? 241 ARG A CG    1 
ATOM   1833 C CD    . ARG A 1 261 ? 28.706  -29.367 -5.086  1.00 15.00 ? 241 ARG A CD    1 
ATOM   1834 N NE    . ARG A 1 261 ? 28.804  -29.595 -3.643  1.00 18.85 ? 241 ARG A NE    1 
ATOM   1835 C CZ    . ARG A 1 261 ? 28.993  -30.786 -3.093  1.00 20.39 ? 241 ARG A CZ    1 
ATOM   1836 N NH1   . ARG A 1 261 ? 29.159  -31.843 -3.863  1.00 22.37 ? 241 ARG A NH1   1 
ATOM   1837 N NH2   . ARG A 1 261 ? 29.019  -30.913 -1.773  1.00 20.17 ? 241 ARG A NH2   1 
ATOM   1838 N N     . ARG A 1 262 ? 25.252  -29.217 -9.455  1.00 6.48  ? 242 ARG A N     1 
ATOM   1839 C CA    . ARG A 1 262 ? 25.204  -29.075 -10.906 1.00 7.25  ? 242 ARG A CA    1 
ATOM   1840 C C     . ARG A 1 262 ? 24.060  -28.137 -11.306 1.00 7.07  ? 242 ARG A C     1 
ATOM   1841 O O     . ARG A 1 262 ? 24.273  -27.340 -12.231 1.00 6.61  ? 242 ARG A O     1 
ATOM   1842 C CB    . ARG A 1 262 ? 25.002  -30.401 -11.624 1.00 8.16  ? 242 ARG A CB    1 
ATOM   1843 C CG    . ARG A 1 262 ? 26.206  -31.344 -11.537 1.00 8.42  ? 242 ARG A CG    1 
ATOM   1844 C CD    . ARG A 1 262 ? 25.950  -32.527 -12.459 1.00 9.49  ? 242 ARG A CD    1 
ATOM   1845 N NE    . ARG A 1 262 ? 24.772  -33.330 -12.170 1.00 9.77  ? 242 ARG A NE    1 
ATOM   1846 C CZ    . ARG A 1 262 ? 24.704  -34.308 -11.276 1.00 10.65 ? 242 ARG A CZ    1 
ATOM   1847 N NH1   . ARG A 1 262 ? 25.801  -34.680 -10.636 1.00 10.70 ? 242 ARG A NH1   1 
ATOM   1848 N NH2   . ARG A 1 262 ? 23.578  -34.964 -11.046 1.00 11.94 ? 242 ARG A NH2   1 
ATOM   1849 N N     . PHE A 1 263 ? 22.885  -28.310 -10.691 1.00 6.76  ? 243 PHE A N     1 
ATOM   1850 C CA    . PHE A 1 263 ? 21.751  -27.419 -11.016 1.00 6.55  ? 243 PHE A CA    1 
ATOM   1851 C C     . PHE A 1 263 ? 22.072  -25.971 -10.650 1.00 6.86  ? 243 PHE A C     1 
ATOM   1852 O O     . PHE A 1 263 ? 21.834  -25.027 -11.405 1.00 5.55  ? 243 PHE A O     1 
ATOM   1853 C CB    . PHE A 1 263 ? 20.453  -27.879 -10.378 1.00 7.10  ? 243 PHE A CB    1 
ATOM   1854 C CG    . PHE A 1 263 ? 19.250  -27.133 -10.886 1.00 8.02  ? 243 PHE A CG    1 
ATOM   1855 C CD1   . PHE A 1 263 ? 18.824  -25.962 -10.272 1.00 9.34  ? 243 PHE A CD1   1 
ATOM   1856 C CD2   . PHE A 1 263 ? 18.593  -27.599 -12.007 1.00 10.77 ? 243 PHE A CD2   1 
ATOM   1857 C CE1   . PHE A 1 263 ? 17.746  -25.261 -10.804 1.00 10.06 ? 243 PHE A CE1   1 
ATOM   1858 C CE2   . PHE A 1 263 ? 17.506  -26.897 -12.508 1.00 11.00 ? 243 PHE A CE2   1 
ATOM   1859 C CZ    . PHE A 1 263 ? 17.108  -25.736 -11.911 1.00 11.54 ? 243 PHE A CZ    1 
ATOM   1860 N N     . ASP A 1 264 ? 22.699  -25.740 -9.488  1.00 6.63  ? 244 ASP A N     1 
ATOM   1861 C CA    . ASP A 1 264 ? 23.170  -24.434 -9.092  1.00 6.45  ? 244 ASP A CA    1 
ATOM   1862 C C     . ASP A 1 264 ? 24.132  -23.840 -10.120 1.00 6.32  ? 244 ASP A C     1 
ATOM   1863 O O     . ASP A 1 264 ? 24.180  -22.620 -10.378 1.00 6.11  ? 244 ASP A O     1 
ATOM   1864 C CB    . ASP A 1 264 ? 23.856  -24.548 -7.732  1.00 7.43  ? 244 ASP A CB    1 
ATOM   1865 C CG    . ASP A 1 264 ? 24.352  -23.234 -7.200  1.00 7.09  ? 244 ASP A CG    1 
ATOM   1866 O OD1   . ASP A 1 264 ? 23.439  -22.303 -6.968  1.00 8.23  ? 244 ASP A OD1   1 
ATOM   1867 O OD2   . ASP A 1 264 ? 25.580  -23.022 -7.104  1.00 8.11  ? 244 ASP A OD2   1 
ATOM   1868 N N     . GLY A 1 265 ? 25.047  -24.649 -10.643 1.00 5.76  ? 245 GLY A N     1 
ATOM   1869 C CA    . GLY A 1 265 ? 25.955  -24.248 -11.711 1.00 5.43  ? 245 GLY A CA    1 
ATOM   1870 C C     . GLY A 1 265 ? 25.255  -23.867 -13.016 1.00 5.57  ? 245 GLY A C     1 
ATOM   1871 O O     . GLY A 1 265 ? 25.591  -22.844 -13.634 1.00 6.97  ? 245 GLY A O     1 
ATOM   1872 N N     . PHE A 1 266 ? 24.314  -24.707 -13.386 1.00 5.77  ? 246 PHE A N     1 
ATOM   1873 C CA    . PHE A 1 266 ? 23.536  -24.587 -14.627 1.00 5.44  ? 246 PHE A CA    1 
ATOM   1874 C C     . PHE A 1 266 ? 22.775  -23.266 -14.680 1.00 6.08  ? 246 PHE A C     1 
ATOM   1875 O O     . PHE A 1 266 ? 22.837  -22.579 -15.698 1.00 4.98  ? 246 PHE A O     1 
ATOM   1876 C CB    . PHE A 1 266 ? 22.584  -25.772 -14.723 1.00 5.76  ? 246 PHE A CB    1 
ATOM   1877 C CG    . PHE A 1 266 ? 21.585  -25.770 -15.849 1.00 6.26  ? 246 PHE A CG    1 
ATOM   1878 C CD1   . PHE A 1 266 ? 21.976  -25.712 -17.168 1.00 7.75  ? 246 PHE A CD1   1 
ATOM   1879 C CD2   . PHE A 1 266 ? 20.257  -25.969 -15.550 1.00 6.28  ? 246 PHE A CD2   1 
ATOM   1880 C CE1   . PHE A 1 266 ? 21.018  -25.787 -18.169 1.00 7.08  ? 246 PHE A CE1   1 
ATOM   1881 C CE2   . PHE A 1 266 ? 19.311  -26.098 -16.564 1.00 6.66  ? 246 PHE A CE2   1 
ATOM   1882 C CZ    . PHE A 1 266 ? 19.699  -26.006 -17.855 1.00 7.00  ? 246 PHE A CZ    1 
ATOM   1883 N N     . VAL A 1 267 ? 22.097  -22.924 -13.587 1.00 5.45  ? 247 VAL A N     1 
ATOM   1884 C CA    . VAL A 1 267 ? 21.262  -21.719 -13.571 1.00 6.48  ? 247 VAL A CA    1 
ATOM   1885 C C     . VAL A 1 267 ? 22.048  -20.521 -13.085 1.00 6.50  ? 247 VAL A C     1 
ATOM   1886 O O     . VAL A 1 267 ? 21.980  -19.462 -13.671 1.00 7.27  ? 247 VAL A O     1 
ATOM   1887 C CB    . VAL A 1 267 ? 19.993  -21.918 -12.727 1.00 6.85  ? 247 VAL A CB    1 
ATOM   1888 C CG1   . VAL A 1 267 ? 19.126  -20.647 -12.678 1.00 7.37  ? 247 VAL A CG1   1 
ATOM   1889 C CG2   . VAL A 1 267 ? 19.189  -23.115 -13.130 1.00 7.43  ? 247 VAL A CG2   1 
ATOM   1890 N N     . ASN A 1 268 ? 22.718  -20.625 -11.936 1.00 5.89  ? 248 ASN A N     1 
ATOM   1891 C CA    . ASN A 1 268 ? 23.191  -19.474 -11.206 1.00 5.76  ? 248 ASN A CA    1 
ATOM   1892 C C     . ASN A 1 268 ? 24.641  -19.188 -11.514 1.00 5.60  ? 248 ASN A C     1 
ATOM   1893 O O     . ASN A 1 268 ? 25.013  -18.127 -11.953 1.00 5.88  ? 248 ASN A O     1 
ATOM   1894 C CB    . ASN A 1 268 ? 23.023  -19.659 -9.694  1.00 5.77  ? 248 ASN A CB    1 
ATOM   1895 C CG    . ASN A 1 268 ? 21.609  -20.008 -9.308  1.00 6.52  ? 248 ASN A CG    1 
ATOM   1896 O OD1   . ASN A 1 268 ? 20.648  -19.405 -9.830  1.00 6.39  ? 248 ASN A OD1   1 
ATOM   1897 N ND2   . ASN A 1 268 ? 21.412  -21.031 -8.479  1.00 7.06  ? 248 ASN A ND2   1 
ATOM   1898 N N     . ARG A 1 269 ? 25.566  -20.138 -11.211 1.00 5.50  ? 249 ARG A N     1 
ATOM   1899 C CA    . ARG A 1 269 ? 26.978  -19.786 -11.268 1.00 5.21  ? 249 ARG A CA    1 
ATOM   1900 C C     . ARG A 1 269 ? 27.505  -19.592 -12.683 1.00 4.40  ? 249 ARG A C     1 
ATOM   1901 O O     . ARG A 1 269 ? 28.468  -18.869 -12.898 1.00 4.46  ? 249 ARG A O     1 
ATOM   1902 C CB    . ARG A 1 269 ? 27.870  -20.818 -10.548 1.00 5.35  ? 249 ARG A CB    1 
ATOM   1903 C CG    . ARG A 1 269 ? 27.479  -21.006 -9.091  1.00 5.68  ? 249 ARG A CG    1 
ATOM   1904 C CD    . ARG A 1 269 ? 28.351  -22.051 -8.380  1.00 6.19  ? 249 ARG A CD    1 
ATOM   1905 N NE    . ARG A 1 269 ? 27.952  -23.386 -8.707  1.00 7.01  ? 249 ARG A NE    1 
ATOM   1906 C CZ    . ARG A 1 269 ? 28.773  -24.275 -9.305  1.00 6.09  ? 249 ARG A CZ    1 
ATOM   1907 N NH1   . ARG A 1 269 ? 29.960  -23.891 -9.744  1.00 7.51  ? 249 ARG A NH1   1 
ATOM   1908 N NH2   . ARG A 1 269 ? 28.350  -25.488 -9.547  1.00 7.12  ? 249 ARG A NH2   1 
ATOM   1909 N N     . TRP A 1 270 ? 26.882  -20.240 -13.663 1.00 4.40  ? 250 TRP A N     1 
ATOM   1910 C CA    . TRP A 1 270 ? 27.310  -20.093 -15.034 1.00 4.37  ? 250 TRP A CA    1 
ATOM   1911 C C     . TRP A 1 270 ? 27.270  -18.619 -15.459 1.00 4.17  ? 250 TRP A C     1 
ATOM   1912 O O     . TRP A 1 270 ? 28.051  -18.218 -16.282 1.00 4.68  ? 250 TRP A O     1 
ATOM   1913 C CB    . TRP A 1 270 ? 26.398  -20.929 -15.946 1.00 4.67  ? 250 TRP A CB    1 
ATOM   1914 C CG    . TRP A 1 270 ? 26.884  -20.976 -17.358 1.00 5.18  ? 250 TRP A CG    1 
ATOM   1915 C CD1   . TRP A 1 270 ? 26.358  -20.317 -18.445 1.00 5.53  ? 250 TRP A CD1   1 
ATOM   1916 C CD2   . TRP A 1 270 ? 27.997  -21.728 -17.839 1.00 5.77  ? 250 TRP A CD2   1 
ATOM   1917 N NE1   . TRP A 1 270 ? 27.105  -20.583 -19.555 1.00 5.87  ? 250 TRP A NE1   1 
ATOM   1918 C CE2   . TRP A 1 270 ? 28.116  -21.449 -19.220 1.00 6.34  ? 250 TRP A CE2   1 
ATOM   1919 C CE3   . TRP A 1 270 ? 28.906  -22.583 -17.225 1.00 6.60  ? 250 TRP A CE3   1 
ATOM   1920 C CZ2   . TRP A 1 270 ? 29.121  -22.015 -19.998 1.00 6.45  ? 250 TRP A CZ2   1 
ATOM   1921 C CZ3   . TRP A 1 270 ? 29.932  -23.115 -17.988 1.00 6.95  ? 250 TRP A CZ3   1 
ATOM   1922 C CH2   . TRP A 1 270 ? 30.043  -22.794 -19.339 1.00 6.73  ? 250 TRP A CH2   1 
ATOM   1923 N N     . PHE A 1 271 ? 26.322  -17.821 -14.882 1.00 4.92  ? 251 PHE A N     1 
ATOM   1924 C CA    . PHE A 1 271 ? 26.232  -16.412 -15.190 1.00 4.94  ? 251 PHE A CA    1 
ATOM   1925 C C     . PHE A 1 271 ? 26.937  -15.554 -14.130 1.00 4.95  ? 251 PHE A C     1 
ATOM   1926 O O     . PHE A 1 271 ? 27.633  -14.638 -14.515 1.00 5.70  ? 251 PHE A O     1 
ATOM   1927 C CB    . PHE A 1 271 ? 24.745  -16.054 -15.387 1.00 4.92  ? 251 PHE A CB    1 
ATOM   1928 C CG    . PHE A 1 271 ? 24.147  -16.762 -16.588 1.00 5.08  ? 251 PHE A CG    1 
ATOM   1929 C CD1   . PHE A 1 271 ? 24.327  -16.222 -17.844 1.00 5.43  ? 251 PHE A CD1   1 
ATOM   1930 C CD2   . PHE A 1 271 ? 23.493  -17.975 -16.489 1.00 5.00  ? 251 PHE A CD2   1 
ATOM   1931 C CE1   . PHE A 1 271 ? 23.871  -16.867 -18.982 1.00 5.67  ? 251 PHE A CE1   1 
ATOM   1932 C CE2   . PHE A 1 271 ? 22.998  -18.596 -17.637 1.00 5.86  ? 251 PHE A CE2   1 
ATOM   1933 C CZ    . PHE A 1 271 ? 23.206  -18.050 -18.870 1.00 5.77  ? 251 PHE A CZ    1 
ATOM   1934 N N     . LEU A 1 272 ? 26.733  -15.857 -12.849 1.00 5.79  ? 252 LEU A N     1 
ATOM   1935 C CA    . LEU A 1 272 ? 27.324  -15.049 -11.780 1.00 6.48  ? 252 LEU A CA    1 
ATOM   1936 C C     . LEU A 1 272 ? 28.840  -14.999 -11.885 1.00 6.45  ? 252 LEU A C     1 
ATOM   1937 O O     . LEU A 1 272 ? 29.463  -13.954 -11.762 1.00 7.44  ? 252 LEU A O     1 
ATOM   1938 C CB    . LEU A 1 272 ? 26.889  -15.574 -10.416 1.00 6.71  ? 252 LEU A CB    1 
ATOM   1939 C CG    . LEU A 1 272 ? 25.438  -15.337 -10.012 1.00 6.79  ? 252 LEU A CG    1 
ATOM   1940 C CD1   . LEU A 1 272 ? 25.088  -16.162 -8.788  1.00 7.72  ? 252 LEU A CD1   1 
ATOM   1941 C CD2   . LEU A 1 272 ? 25.179  -13.881 -9.766  1.00 6.11  ? 252 LEU A CD2   1 
ATOM   1942 N N     . ASP A 1 273 ? 29.453  -16.172 -12.123 1.00 6.88  ? 253 ASP A N     1 
ATOM   1943 C CA    . ASP A 1 273 ? 30.893  -16.239 -12.013 1.00 7.69  ? 253 ASP A CA    1 
ATOM   1944 C C     . ASP A 1 273 ? 31.560  -15.404 -13.087 1.00 6.62  ? 253 ASP A C     1 
ATOM   1945 O O     . ASP A 1 273 ? 32.471  -14.620 -12.810 1.00 6.97  ? 253 ASP A O     1 
ATOM   1946 C CB    . ASP A 1 273 ? 31.386  -17.687 -12.067 1.00 8.63  ? 253 ASP A CB    1 
ATOM   1947 C CG    . ASP A 1 273 ? 31.261  -18.433 -10.758 1.00 10.15 ? 253 ASP A CG    1 
ATOM   1948 O OD1   . ASP A 1 273 ? 30.673  -17.906 -9.762  1.00 11.53 ? 253 ASP A OD1   1 
ATOM   1949 O OD2   . ASP A 1 273 ? 31.784  -19.559 -10.714 1.00 11.93 ? 253 ASP A OD2   1 
ATOM   1950 N N     . PRO A 1 274 ? 31.224  -15.532 -14.387 1.00 6.26  ? 254 PRO A N     1 
ATOM   1951 C CA    . PRO A 1 274 ? 31.878  -14.724 -15.411 1.00 7.10  ? 254 PRO A CA    1 
ATOM   1952 C C     . PRO A 1 274 ? 31.609  -13.225 -15.245 1.00 6.84  ? 254 PRO A C     1 
ATOM   1953 O O     . PRO A 1 274 ? 32.484  -12.386 -15.453 1.00 8.02  ? 254 PRO A O     1 
ATOM   1954 C CB    . PRO A 1 274 ? 31.372  -15.225 -16.758 1.00 7.26  ? 254 PRO A CB    1 
ATOM   1955 C CG    . PRO A 1 274 ? 30.218  -16.123 -16.405 1.00 6.87  ? 254 PRO A CG    1 
ATOM   1956 C CD    . PRO A 1 274 ? 30.313  -16.542 -14.954 1.00 6.44  ? 254 PRO A CD    1 
ATOM   1957 N N     . LEU A 1 275 ? 30.375  -12.892 -14.800 1.00 7.58  ? 255 LEU A N     1 
ATOM   1958 C CA    . LEU A 1 275 ? 30.077  -11.494 -14.498 1.00 7.65  ? 255 LEU A CA    1 
ATOM   1959 C C     . LEU A 1 275 ? 30.973  -10.954 -13.386 1.00 8.28  ? 255 LEU A C     1 
ATOM   1960 O O     . LEU A 1 275 ? 31.286  -9.765  -13.367 1.00 9.22  ? 255 LEU A O     1 
ATOM   1961 C CB    . LEU A 1 275 ? 28.603  -11.356 -14.149 1.00 6.86  ? 255 LEU A CB    1 
ATOM   1962 C CG    . LEU A 1 275 ? 27.638  -11.490 -15.331 1.00 7.14  ? 255 LEU A CG    1 
ATOM   1963 C CD1   . LEU A 1 275 ? 26.228  -11.649 -14.813 1.00 6.43  ? 255 LEU A CD1   1 
ATOM   1964 C CD2   . LEU A 1 275 ? 27.772  -10.303 -16.283 1.00 6.65  ? 255 LEU A CD2   1 
ATOM   1965 N N     . ALA A 1 276 ? 31.324  -11.833 -12.449 1.00 9.17  ? 256 ALA A N     1 
ATOM   1966 C CA    . ALA A 1 276 ? 32.142  -11.496 -11.272 1.00 10.88 ? 256 ALA A CA    1 
ATOM   1967 C C     . ALA A 1 276 ? 33.638  -11.494 -11.602 1.00 12.13 ? 256 ALA A C     1 
ATOM   1968 O O     . ALA A 1 276 ? 34.457  -11.266 -10.693 1.00 14.37 ? 256 ALA A O     1 
ATOM   1969 C CB    . ALA A 1 276 ? 31.834  -12.450 -10.155 1.00 11.81 ? 256 ALA A CB    1 
ATOM   1970 N N     . GLY A 1 277 ? 34.019  -11.789 -12.836 1.00 11.75 ? 257 GLY A N     1 
ATOM   1971 C CA    . GLY A 1 277 ? 35.409  -11.834 -13.246 1.00 11.36 ? 257 GLY A CA    1 
ATOM   1972 C C     . GLY A 1 277 ? 36.111  -13.131 -12.875 1.00 12.85 ? 257 GLY A C     1 
ATOM   1973 O O     . GLY A 1 277 ? 37.338  -13.115 -12.771 1.00 14.04 ? 257 GLY A O     1 
ATOM   1974 N N     . ARG A 1 278 ? 35.350  -14.192 -12.597 1.00 10.96 ? 258 ARG A N     1 
ATOM   1975 C CA    . ARG A 1 278 ? 35.863  -15.459 -12.077 1.00 11.78 ? 258 ARG A CA    1 
ATOM   1976 C C     . ARG A 1 278 ? 35.947  -16.528 -13.166 1.00 12.55 ? 258 ARG A C     1 
ATOM   1977 O O     . ARG A 1 278 ? 36.231  -17.708 -12.859 1.00 13.08 ? 258 ARG A O     1 
ATOM   1978 C CB    . ARG A 1 278 ? 34.992  -15.966 -10.935 1.00 11.90 ? 258 ARG A CB    1 
ATOM   1979 C CG    . ARG A 1 278 ? 34.927  -15.004 -9.747  1.00 11.56 ? 258 ARG A CG    1 
ATOM   1980 C CD    . ARG A 1 278 ? 34.101  -15.466 -8.579  1.00 11.97 ? 258 ARG A CD    1 
ATOM   1981 N NE    . ARG A 1 278 ? 34.052  -14.522 -7.462  1.00 11.88 ? 258 ARG A NE    1 
ATOM   1982 C CZ    . ARG A 1 278 ? 33.222  -14.591 -6.440  1.00 11.90 ? 258 ARG A CZ    1 
ATOM   1983 N NH1   . ARG A 1 278 ? 32.442  -15.638 -6.241  1.00 12.69 ? 258 ARG A NH1   1 
ATOM   1984 N NH2   . ARG A 1 278 ? 33.242  -13.600 -5.568  1.00 14.25 ? 258 ARG A NH2   1 
ATOM   1985 N N     . GLY A 1 279 ? 35.685  -16.122 -14.413 1.00 11.25 ? 259 GLY A N     1 
ATOM   1986 C CA    . GLY A 1 279 ? 35.564  -17.061 -15.522 1.00 10.63 ? 259 GLY A CA    1 
ATOM   1987 C C     . GLY A 1 279 ? 34.297  -17.887 -15.370 1.00 9.11  ? 259 GLY A C     1 
ATOM   1988 O O     . GLY A 1 279 ? 33.556  -17.735 -14.400 1.00 11.20 ? 259 GLY A O     1 
ATOM   1989 N N     . TYR A 1 280 ? 34.109  -18.841 -16.280 1.00 8.29  ? 260 TYR A N     1 
ATOM   1990 C CA    . TYR A 1 280 ? 33.065  -19.828 -16.129 1.00 8.06  ? 260 TYR A CA    1 
ATOM   1991 C C     . TYR A 1 280 ? 33.426  -20.820 -15.033 1.00 8.97  ? 260 TYR A C     1 
ATOM   1992 O O     . TYR A 1 280 ? 34.605  -21.173 -14.901 1.00 10.67 ? 260 TYR A O     1 
ATOM   1993 C CB    . TYR A 1 280 ? 32.817  -20.563 -17.440 1.00 7.88  ? 260 TYR A CB    1 
ATOM   1994 C CG    . TYR A 1 280 ? 32.116  -19.726 -18.475 1.00 7.49  ? 260 TYR A CG    1 
ATOM   1995 C CD1   . TYR A 1 280 ? 30.787  -19.360 -18.303 1.00 8.39  ? 260 TYR A CD1   1 
ATOM   1996 C CD2   . TYR A 1 280 ? 32.755  -19.270 -19.606 1.00 8.32  ? 260 TYR A CD2   1 
ATOM   1997 C CE1   . TYR A 1 280 ? 30.115  -18.599 -19.235 1.00 8.54  ? 260 TYR A CE1   1 
ATOM   1998 C CE2   . TYR A 1 280 ? 32.100  -18.498 -20.559 1.00 10.04 ? 260 TYR A CE2   1 
ATOM   1999 C CZ    . TYR A 1 280 ? 30.773  -18.153 -20.361 1.00 9.32  ? 260 TYR A CZ    1 
ATOM   2000 O OH    . TYR A 1 280 ? 30.129  -17.388 -21.312 1.00 10.76 ? 260 TYR A OH    1 
ATOM   2001 N N     . PRO A 1 281 ? 32.461  -21.341 -14.273 1.00 7.74  ? 261 PRO A N     1 
ATOM   2002 C CA    . PRO A 1 281 ? 32.776  -22.283 -13.202 1.00 8.38  ? 261 PRO A CA    1 
ATOM   2003 C C     . PRO A 1 281 ? 33.388  -23.563 -13.782 1.00 7.90  ? 261 PRO A C     1 
ATOM   2004 O O     . PRO A 1 281 ? 32.815  -24.188 -14.673 1.00 8.36  ? 261 PRO A O     1 
ATOM   2005 C CB    . PRO A 1 281 ? 31.422  -22.615 -12.581 1.00 8.47  ? 261 PRO A CB    1 
ATOM   2006 C CG    . PRO A 1 281 ? 30.367  -22.151 -13.594 1.00 8.78  ? 261 PRO A CG    1 
ATOM   2007 C CD    . PRO A 1 281 ? 31.018  -21.044 -14.361 1.00 7.76  ? 261 PRO A CD    1 
ATOM   2008 N N     . GLN A 1 282 ? 34.534  -23.956 -13.225 1.00 8.25  ? 262 GLN A N     1 
ATOM   2009 C CA    . GLN A 1 282 ? 35.321  -25.031 -13.807 1.00 8.83  ? 262 GLN A CA    1 
ATOM   2010 C C     . GLN A 1 282 ? 34.590  -26.370 -13.708 1.00 7.60  ? 262 GLN A C     1 
ATOM   2011 O O     . GLN A 1 282 ? 34.690  -27.195 -14.622 1.00 7.48  ? 262 GLN A O     1 
ATOM   2012 C CB    . GLN A 1 282 ? 36.686  -25.051 -13.128 1.00 10.32 ? 262 GLN A CB    1 
ATOM   2013 C CG    . GLN A 1 282 ? 37.688  -25.924 -13.882 1.00 12.53 ? 262 GLN A CG    1 
ATOM   2014 C CD    . GLN A 1 282 ? 37.924  -25.444 -15.293 1.00 14.97 ? 262 GLN A CD    1 
ATOM   2015 O OE1   . GLN A 1 282 ? 38.282  -24.286 -15.518 1.00 17.70 ? 262 GLN A OE1   1 
ATOM   2016 N NE2   . GLN A 1 282 ? 37.674  -26.317 -16.256 1.00 16.86 ? 262 GLN A NE2   1 
ATOM   2017 N N     . ASP A 1 283 ? 33.830  -26.626 -12.640 1.00 8.07  ? 263 ASP A N     1 
ATOM   2018 C CA    . ASP A 1 283 ? 33.073  -27.858 -12.551 1.00 7.68  ? 263 ASP A CA    1 
ATOM   2019 C C     . ASP A 1 283 ? 32.090  -28.007 -13.703 1.00 8.42  ? 263 ASP A C     1 
ATOM   2020 O O     . ASP A 1 283 ? 31.925  -29.067 -14.252 1.00 8.85  ? 263 ASP A O     1 
ATOM   2021 C CB    . ASP A 1 283 ? 32.358  -28.021 -11.218 1.00 8.30  ? 263 ASP A CB    1 
ATOM   2022 C CG    . ASP A 1 283 ? 31.292  -26.985 -10.873 1.00 9.46  ? 263 ASP A CG    1 
ATOM   2023 O OD1   . ASP A 1 283 ? 31.439  -25.863 -11.284 1.00 10.39 ? 263 ASP A OD1   1 
ATOM   2024 O OD2   . ASP A 1 283 ? 30.376  -27.352 -10.128 1.00 10.19 ? 263 ASP A OD2   1 
ATOM   2025 N N     . MET A 1 284 ? 31.460  -26.900 -14.095 1.00 6.94  ? 264 MET A N     1 
ATOM   2026 C CA    . MET A 1 284 ? 30.523  -26.963 -15.186 1.00 7.08  ? 264 MET A CA    1 
ATOM   2027 C C     . MET A 1 284 ? 31.231  -27.061 -16.533 1.00 7.44  ? 264 MET A C     1 
ATOM   2028 O O     . MET A 1 284 ? 30.725  -27.744 -17.407 1.00 7.31  ? 264 MET A O     1 
ATOM   2029 C CB    . MET A 1 284 ? 29.617  -25.728 -15.160 1.00 7.32  ? 264 MET A CB    1 
ATOM   2030 C CG    . MET A 1 284 ? 28.826  -25.588 -13.859 1.00 8.22  ? 264 MET A CG    1 
ATOM   2031 S SD    . MET A 1 284 ? 27.866  -27.020 -13.379 1.00 8.98  ? 264 MET A SD    1 
ATOM   2032 C CE    . MET A 1 284 ? 26.709  -27.101 -14.745 1.00 9.90  ? 264 MET A CE    1 
ATOM   2033 N N     . LEU A 1 285 ? 32.323  -26.319 -16.726 1.00 7.87  ? 265 LEU A N     1 
ATOM   2034 C CA    . LEU A 1 285 ? 33.118  -26.486 -17.940 1.00 7.83  ? 265 LEU A CA    1 
ATOM   2035 C C     . LEU A 1 285 ? 33.485  -27.957 -18.130 1.00 9.33  ? 265 LEU A C     1 
ATOM   2036 O O     . LEU A 1 285 ? 33.391  -28.487 -19.234 1.00 10.44 ? 265 LEU A O     1 
ATOM   2037 C CB    . LEU A 1 285 ? 34.386  -25.629 -17.876 1.00 8.30  ? 265 LEU A CB    1 
ATOM   2038 C CG    . LEU A 1 285 ? 34.180  -24.131 -18.051 1.00 8.34  ? 265 LEU A CG    1 
ATOM   2039 C CD1   . LEU A 1 285 ? 35.471  -23.399 -17.738 1.00 9.13  ? 265 LEU A CD1   1 
ATOM   2040 C CD2   . LEU A 1 285 ? 33.652  -23.814 -19.437 1.00 9.00  ? 265 LEU A CD2   1 
ATOM   2041 N N     . ASP A 1 286 ? 33.971  -28.583 -17.073 1.00 9.53  ? 266 ASP A N     1 
ATOM   2042 C CA    . ASP A 1 286 ? 34.455  -29.957 -17.218 1.00 9.98  ? 266 ASP A CA    1 
ATOM   2043 C C     . ASP A 1 286 ? 33.293  -30.895 -17.502 1.00 10.91 ? 266 ASP A C     1 
ATOM   2044 O O     . ASP A 1 286 ? 33.431  -31.815 -18.290 1.00 14.43 ? 266 ASP A O     1 
ATOM   2045 C CB    . ASP A 1 286 ? 35.203  -30.431 -15.971 1.00 11.15 ? 266 ASP A CB    1 
ATOM   2046 C CG    . ASP A 1 286 ? 36.554  -29.762 -15.708 1.00 12.48 ? 266 ASP A CG    1 
ATOM   2047 O OD1   . ASP A 1 286 ? 37.155  -29.143 -16.633 1.00 14.34 ? 266 ASP A OD1   1 
ATOM   2048 O OD2   . ASP A 1 286 ? 36.966  -29.787 -14.531 1.00 13.59 ? 266 ASP A OD2   1 
ATOM   2049 N N     . TYR A 1 287 ? 32.131  -30.636 -16.876 1.00 10.02 ? 267 TYR A N     1 
ATOM   2050 C CA    . TYR A 1 287 ? 30.925  -31.421 -17.068 1.00 9.95  ? 267 TYR A CA    1 
ATOM   2051 C C     . TYR A 1 287 ? 30.381  -31.269 -18.495 1.00 11.14 ? 267 TYR A C     1 
ATOM   2052 O O     . TYR A 1 287 ? 30.031  -32.245 -19.146 1.00 12.15 ? 267 TYR A O     1 
ATOM   2053 C CB    . TYR A 1 287 ? 29.890  -30.973 -16.042 1.00 11.02 ? 267 TYR A CB    1 
ATOM   2054 C CG    . TYR A 1 287 ? 28.524  -31.620 -16.089 1.00 10.89 ? 267 TYR A CG    1 
ATOM   2055 C CD1   . TYR A 1 287 ? 28.346  -32.995 -16.003 1.00 12.26 ? 267 TYR A CD1   1 
ATOM   2056 C CD2   . TYR A 1 287 ? 27.378  -30.849 -16.111 1.00 12.19 ? 267 TYR A CD2   1 
ATOM   2057 C CE1   . TYR A 1 287 ? 27.075  -33.571 -15.950 1.00 11.92 ? 267 TYR A CE1   1 
ATOM   2058 C CE2   . TYR A 1 287 ? 26.109  -31.402 -16.082 1.00 12.50 ? 267 TYR A CE2   1 
ATOM   2059 C CZ    . TYR A 1 287 ? 25.946  -32.779 -16.021 1.00 12.72 ? 267 TYR A CZ    1 
ATOM   2060 O OH    . TYR A 1 287 ? 24.658  -33.252 -15.961 1.00 12.65 ? 267 TYR A OH    1 
ATOM   2061 N N     . TYR A 1 288 ? 30.261  -30.034 -18.982 1.00 9.04  ? 268 TYR A N     1 
ATOM   2062 C CA    . TYR A 1 288 ? 29.769  -29.769 -20.322 1.00 9.78  ? 268 TYR A CA    1 
ATOM   2063 C C     . TYR A 1 288 ? 30.765  -30.222 -21.396 1.00 9.96  ? 268 TYR A C     1 
ATOM   2064 O O     . TYR A 1 288 ? 30.394  -30.460 -22.539 1.00 10.84 ? 268 TYR A O     1 
ATOM   2065 C CB    . TYR A 1 288 ? 29.515  -28.266 -20.486 1.00 9.22  ? 268 TYR A CB    1 
ATOM   2066 C CG    . TYR A 1 288 ? 28.405  -27.665 -19.662 1.00 8.38  ? 268 TYR A CG    1 
ATOM   2067 C CD1   . TYR A 1 288 ? 27.263  -28.369 -19.344 1.00 8.30  ? 268 TYR A CD1   1 
ATOM   2068 C CD2   . TYR A 1 288 ? 28.507  -26.351 -19.254 1.00 7.30  ? 268 TYR A CD2   1 
ATOM   2069 C CE1   . TYR A 1 288 ? 26.226  -27.776 -18.640 1.00 9.70  ? 268 TYR A CE1   1 
ATOM   2070 C CE2   . TYR A 1 288 ? 27.477  -25.739 -18.547 1.00 8.19  ? 268 TYR A CE2   1 
ATOM   2071 C CZ    . TYR A 1 288 ? 26.358  -26.467 -18.229 1.00 8.63  ? 268 TYR A CZ    1 
ATOM   2072 O OH    . TYR A 1 288 ? 25.308  -25.888 -17.527 1.00 9.15  ? 268 TYR A OH    1 
ATOM   2073 N N     . GLY A 1 289 ? 32.049  -30.211 -21.056 1.00 10.23 ? 269 GLY A N     1 
ATOM   2074 C CA    . GLY A 1 289 ? 33.078  -30.552 -22.040 1.00 10.88 ? 269 GLY A CA    1 
ATOM   2075 C C     . GLY A 1 289 ? 33.028  -29.676 -23.294 1.00 11.33 ? 269 GLY A C     1 
ATOM   2076 O O     . GLY A 1 289 ? 32.861  -28.451 -23.199 1.00 12.84 ? 269 GLY A O     1 
ATOM   2077 N N     . ALA A 1 290 ? 33.209  -30.276 -24.489 1.00 13.39 ? 270 ALA A N     1 
ATOM   2078 C CA    . ALA A 1 290 ? 33.330  -29.515 -25.725 1.00 16.97 ? 270 ALA A CA    1 
ATOM   2079 C C     . ALA A 1 290 ? 32.031  -28.804 -26.115 1.00 15.81 ? 270 ALA A C     1 
ATOM   2080 O O     . ALA A 1 290 ? 32.062  -27.918 -26.975 1.00 17.64 ? 270 ALA A O     1 
ATOM   2081 C CB    . ALA A 1 290 ? 33.794  -30.412 -26.869 1.00 18.20 ? 270 ALA A CB    1 
ATOM   2082 N N     . ALA A 1 291 ? 30.900  -29.164 -25.477 1.00 15.02 ? 271 ALA A N     1 
ATOM   2083 C CA    . ALA A 1 291 ? 29.674  -28.406 -25.725 1.00 13.84 ? 271 ALA A CA    1 
ATOM   2084 C C     . ALA A 1 291 ? 29.762  -26.955 -25.246 1.00 14.60 ? 271 ALA A C     1 
ATOM   2085 O O     . ALA A 1 291 ? 29.086  -26.081 -25.783 1.00 15.29 ? 271 ALA A O     1 
ATOM   2086 C CB    . ALA A 1 291 ? 28.505  -29.106 -25.129 1.00 13.63 ? 271 ALA A CB    1 
ATOM   2087 N N     . ALA A 1 292 ? 30.670  -26.656 -24.333 1.00 13.36 ? 272 ALA A N     1 
ATOM   2088 C CA    . ALA A 1 292 ? 30.773  -25.307 -23.823 1.00 14.55 ? 272 ALA A CA    1 
ATOM   2089 C C     . ALA A 1 292 ? 31.606  -24.495 -24.791 1.00 16.61 ? 272 ALA A C     1 
ATOM   2090 O O     . ALA A 1 292 ? 32.443  -25.034 -25.513 1.00 14.72 ? 272 ALA A O     1 
ATOM   2091 C CB    . ALA A 1 292 ? 31.395  -25.328 -22.452 1.00 15.28 ? 272 ALA A CB    1 
ATOM   2092 N N     . PRO A 1 293 ? 31.406  -23.174 -24.824 1.00 17.00 ? 273 PRO A N     1 
ATOM   2093 C CA    . PRO A 1 293 ? 32.190  -22.317 -25.699 1.00 20.72 ? 273 PRO A CA    1 
ATOM   2094 C C     . PRO A 1 293 ? 33.624  -22.334 -25.184 1.00 20.35 ? 273 PRO A C     1 
ATOM   2095 O O     . PRO A 1 293 ? 33.852  -22.527 -23.992 1.00 18.93 ? 273 PRO A O     1 
ATOM   2096 C CB    . PRO A 1 293 ? 31.503  -20.950 -25.523 1.00 22.91 ? 273 PRO A CB    1 
ATOM   2097 C CG    . PRO A 1 293 ? 30.972  -21.005 -24.079 1.00 23.06 ? 273 PRO A CG    1 
ATOM   2098 C CD    . PRO A 1 293 ? 30.479  -22.431 -23.947 1.00 21.21 ? 273 PRO A CD    1 
ATOM   2099 N N     . GLN A 1 294 ? 34.573  -22.142 -26.099 1.00 23.94 ? 274 GLN A N     1 
ATOM   2100 C CA    . GLN A 1 294 ? 35.924  -21.762 -25.707 1.00 31.02 ? 274 GLN A CA    1 
ATOM   2101 C C     . GLN A 1 294 ? 35.856  -20.281 -25.369 1.00 31.21 ? 274 GLN A C     1 
ATOM   2102 O O     . GLN A 1 294 ? 35.472  -19.458 -26.191 1.00 36.07 ? 274 GLN A O     1 
ATOM   2103 C CB    . GLN A 1 294 ? 36.969  -22.097 -26.779 1.00 39.40 ? 274 GLN A CB    1 
ATOM   2104 C CG    . GLN A 1 294 ? 36.584  -21.731 -28.217 1.00 49.02 ? 274 GLN A CG    1 
ATOM   2105 C CD    . GLN A 1 294 ? 35.647  -22.724 -28.881 1.00 56.20 ? 274 GLN A CD    1 
ATOM   2106 O OE1   . GLN A 1 294 ? 34.433  -22.718 -28.658 1.00 54.51 ? 274 GLN A OE1   1 
ATOM   2107 N NE2   . GLN A 1 294 ? 36.199  -23.578 -29.734 1.00 59.14 ? 274 GLN A NE2   1 
ATOM   2108 N N     . ALA A 1 295 ? 36.110  -19.955 -24.110 1.00 30.25 ? 275 ALA A N     1 
ATOM   2109 C CA    . ALA A 1 295 ? 35.982  -18.583 -23.666 1.00 31.27 ? 275 ALA A CA    1 
ATOM   2110 C C     . ALA A 1 295 ? 37.371  -17.965 -23.612 1.00 29.42 ? 275 ALA A C     1 
ATOM   2111 O O     . ALA A 1 295 ? 38.063  -18.106 -22.614 1.00 33.80 ? 275 ALA A O     1 
ATOM   2112 C CB    . ALA A 1 295 ? 35.293  -18.582 -22.328 1.00 32.64 ? 275 ALA A CB    1 
ATOM   2113 N N     . ASN A 1 296 ? 37.767  -17.288 -24.689 1.00 31.80 ? 276 ASN A N     1 
ATOM   2114 C CA    . ASN A 1 296 ? 39.074  -16.657 -24.713 1.00 35.42 ? 276 ASN A CA    1 
ATOM   2115 C C     . ASN A 1 296 ? 39.074  -15.533 -23.671 1.00 33.74 ? 276 ASN A C     1 
ATOM   2116 O O     . ASN A 1 296 ? 38.035  -14.922 -23.379 1.00 30.14 ? 276 ASN A O     1 
ATOM   2117 C CB    . ASN A 1 296 ? 39.493  -16.239 -26.125 1.00 36.38 ? 276 ASN A CB    1 
ATOM   2118 C CG    . ASN A 1 296 ? 38.590  -15.194 -26.740 1.00 42.97 ? 276 ASN A CG    1 
ATOM   2119 O OD1   . ASN A 1 296 ? 38.256  -14.194 -26.100 1.00 40.36 ? 276 ASN A OD1   1 
ATOM   2120 N ND2   . ASN A 1 296 ? 38.168  -15.431 -27.971 1.00 43.35 ? 276 ASN A ND2   1 
ATOM   2121 N N     . PRO A 1 297 ? 40.228  -15.272 -23.028 1.00 29.69 ? 277 PRO A N     1 
ATOM   2122 C CA    . PRO A 1 297 ? 40.366  -14.191 -22.047 1.00 29.91 ? 277 PRO A CA    1 
ATOM   2123 C C     . PRO A 1 297 ? 39.770  -12.825 -22.409 1.00 25.48 ? 277 PRO A C     1 
ATOM   2124 O O     . PRO A 1 297 ? 39.290  -12.103 -21.528 1.00 24.22 ? 277 PRO A O     1 
ATOM   2125 C CB    . PRO A 1 297 ? 41.898  -14.027 -21.969 1.00 29.72 ? 277 PRO A CB    1 
ATOM   2126 C CG    . PRO A 1 297 ? 42.418  -15.430 -22.193 1.00 31.15 ? 277 PRO A CG    1 
ATOM   2127 C CD    . PRO A 1 297 ? 41.486  -16.025 -23.221 1.00 30.91 ? 277 PRO A CD    1 
ATOM   2128 N N     . GLU A 1 298 ? 39.854  -12.461 -23.691 1.00 22.72 ? 278 GLU A N     1 
ATOM   2129 C CA    . GLU A 1 298 ? 39.383  -11.166 -24.173 1.00 21.72 ? 278 GLU A CA    1 
ATOM   2130 C C     . GLU A 1 298 ? 37.870  -11.061 -23.944 1.00 17.48 ? 278 GLU A C     1 
ATOM   2131 O O     . GLU A 1 298 ? 37.360  -10.033 -23.496 1.00 15.45 ? 278 GLU A O     1 
ATOM   2132 C CB    . GLU A 1 298 ? 39.678  -10.978 -25.667 1.00 26.91 ? 278 GLU A CB    1 
ATOM   2133 C CG    . GLU A 1 298 ? 41.153  -11.106 -26.058 1.00 37.63 ? 278 GLU A CG    1 
ATOM   2134 C CD    . GLU A 1 298 ? 41.734  -12.508 -26.259 1.00 46.88 ? 278 GLU A CD    1 
ATOM   2135 O OE1   . GLU A 1 298 ? 41.021  -13.519 -26.035 1.00 51.12 ? 278 GLU A OE1   1 
ATOM   2136 O OE2   . GLU A 1 298 ? 42.923  -12.596 -26.650 1.00 57.28 ? 278 GLU A OE2   1 
ATOM   2137 N N     . ASP A 1 299 ? 37.163  -12.131 -24.305 1.00 16.56 ? 279 ASP A N     1 
ATOM   2138 C CA    . ASP A 1 299 ? 35.716  -12.154 -24.126 1.00 13.90 ? 279 ASP A CA    1 
ATOM   2139 C C     . ASP A 1 299 ? 35.351  -12.087 -22.642 1.00 13.40 ? 279 ASP A C     1 
ATOM   2140 O O     . ASP A 1 299 ? 34.441  -11.347 -22.268 1.00 12.21 ? 279 ASP A O     1 
ATOM   2141 C CB    . ASP A 1 299 ? 35.114  -13.426 -24.728 1.00 14.31 ? 279 ASP A CB    1 
ATOM   2142 C CG    . ASP A 1 299 ? 34.978  -13.450 -26.244 1.00 14.26 ? 279 ASP A CG    1 
ATOM   2143 O OD1   . ASP A 1 299 ? 35.398  -12.518 -26.916 1.00 14.95 ? 279 ASP A OD1   1 
ATOM   2144 O OD2   . ASP A 1 299 ? 34.418  -14.407 -26.738 1.00 15.83 ? 279 ASP A OD2   1 
ATOM   2145 N N     . LEU A 1 300 ? 36.017  -12.869 -21.775 1.00 12.42 ? 280 LEU A N     1 
ATOM   2146 C CA    . LEU A 1 300 ? 35.767  -12.846 -20.335 1.00 12.10 ? 280 LEU A CA    1 
ATOM   2147 C C     . LEU A 1 300 ? 35.972  -11.449 -19.759 1.00 11.73 ? 280 LEU A C     1 
ATOM   2148 O O     . LEU A 1 300 ? 35.215  -11.017 -18.873 1.00 9.78  ? 280 LEU A O     1 
ATOM   2149 C CB    . LEU A 1 300 ? 36.665  -13.857 -19.622 1.00 15.25 ? 280 LEU A CB    1 
ATOM   2150 C CG    . LEU A 1 300 ? 36.253  -15.293 -19.902 1.00 16.78 ? 280 LEU A CG    1 
ATOM   2151 C CD1   . LEU A 1 300 ? 37.288  -16.298 -19.389 1.00 17.91 ? 280 LEU A CD1   1 
ATOM   2152 C CD2   . LEU A 1 300 ? 34.897  -15.560 -19.326 1.00 16.65 ? 280 LEU A CD2   1 
ATOM   2153 N N     . THR A 1 301 ? 36.977  -10.735 -20.262 1.00 12.84 ? 281 THR A N     1 
ATOM   2154 C CA    . THR A 1 301 ? 37.220  -9.366  -19.821 1.00 13.59 ? 281 THR A CA    1 
ATOM   2155 C C     . THR A 1 301 ? 36.003  -8.482  -20.121 1.00 12.11 ? 281 THR A C     1 
ATOM   2156 O O     . THR A 1 301 ? 35.533  -7.721  -19.250 1.00 12.10 ? 281 THR A O     1 
ATOM   2157 C CB    . THR A 1 301 ? 38.516  -8.816  -20.428 1.00 16.17 ? 281 THR A CB    1 
ATOM   2158 O OG1   . THR A 1 301 ? 39.523  -9.612  -19.808 1.00 18.90 ? 281 THR A OG1   1 
ATOM   2159 C CG2   . THR A 1 301 ? 38.698  -7.354  -20.110 1.00 16.70 ? 281 THR A CG2   1 
ATOM   2160 N N     . GLN A 1 302 ? 35.496  -8.645  -21.347 1.00 11.35 ? 282 GLN A N     1 
ATOM   2161 C CA    . GLN A 1 302 ? 34.372  -7.850  -21.835 1.00 11.58 ? 282 GLN A CA    1 
ATOM   2162 C C     . GLN A 1 302 ? 33.135  -8.188  -21.005 1.00 9.67  ? 282 GLN A C     1 
ATOM   2163 O O     . GLN A 1 302 ? 32.378  -7.295  -20.615 1.00 8.14  ? 282 GLN A O     1 
ATOM   2164 C CB    . GLN A 1 302 ? 34.142  -8.069  -23.326 1.00 14.22 ? 282 GLN A CB    1 
ATOM   2165 C CG    . GLN A 1 302 ? 35.151  -7.337  -24.203 1.00 19.50 ? 282 GLN A CG    1 
ATOM   2166 C CD    . GLN A 1 302 ? 34.826  -5.875  -24.462 1.00 20.63 ? 282 GLN A CD    1 
ATOM   2167 O OE1   . GLN A 1 302 ? 35.439  -5.269  -25.324 1.00 33.58 ? 282 GLN A OE1   1 
ATOM   2168 N NE2   . GLN A 1 302 ? 33.831  -5.289  -23.782 1.00 26.53 ? 282 GLN A NE2   1 
ATOM   2169 N N     . ILE A 1 303 ? 32.896  -9.472  -20.783 1.00 8.01  ? 283 ILE A N     1 
ATOM   2170 C CA    . ILE A 1 303 ? 31.755  -9.928  -20.002 1.00 7.44  ? 283 ILE A CA    1 
ATOM   2171 C C     . ILE A 1 303 ? 31.709  -9.309  -18.610 1.00 7.90  ? 283 ILE A C     1 
ATOM   2172 O O     . ILE A 1 303 ? 30.634  -8.936  -18.097 1.00 8.37  ? 283 ILE A O     1 
ATOM   2173 C CB    . ILE A 1 303 ? 31.693  -11.455 -19.962 1.00 7.76  ? 283 ILE A CB    1 
ATOM   2174 C CG1   . ILE A 1 303 ? 31.370  -11.986 -21.358 1.00 7.63  ? 283 ILE A CG1   1 
ATOM   2175 C CG2   . ILE A 1 303 ? 30.729  -11.940 -18.913 1.00 7.23  ? 283 ILE A CG2   1 
ATOM   2176 C CD1   . ILE A 1 303 ? 31.519  -13.488 -21.503 1.00 8.39  ? 283 ILE A CD1   1 
ATOM   2177 N N     . ALA A 1 304 ? 32.883  -9.097  -18.010 1.00 8.17  ? 284 ALA A N     1 
ATOM   2178 C CA    . ALA A 1 304 ? 32.966  -8.546  -16.663 1.00 9.27  ? 284 ALA A CA    1 
ATOM   2179 C C     . ALA A 1 304 ? 33.042  -7.025  -16.644 1.00 9.96  ? 284 ALA A C     1 
ATOM   2180 O O     . ALA A 1 304 ? 33.465  -6.483  -15.613 1.00 11.59 ? 284 ALA A O     1 
ATOM   2181 C CB    . ALA A 1 304 ? 34.161  -9.162  -15.955 1.00 9.96  ? 284 ALA A CB    1 
ATOM   2182 N N     . ALA A 1 305 ? 32.575  -6.337  -17.701 1.00 9.38  ? 285 ALA A N     1 
ATOM   2183 C CA    . ALA A 1 305 ? 32.512  -4.880  -17.710 1.00 9.77  ? 285 ALA A CA    1 
ATOM   2184 C C     . ALA A 1 305 ? 31.888  -4.424  -16.410 1.00 10.41 ? 285 ALA A C     1 
ATOM   2185 O O     . ALA A 1 305 ? 30.814  -4.867  -16.026 1.00 10.79 ? 285 ALA A O     1 
ATOM   2186 C CB    . ALA A 1 305 ? 31.659  -4.387  -18.855 1.00 9.71  ? 285 ALA A CB    1 
ATOM   2187 N N     . PRO A 1 306 ? 32.478  -3.470  -15.664 1.00 10.19 ? 286 PRO A N     1 
ATOM   2188 C CA    . PRO A 1 306 ? 31.910  -3.118  -14.367 1.00 9.12  ? 286 PRO A CA    1 
ATOM   2189 C C     . PRO A 1 306 ? 30.454  -2.656  -14.402 1.00 7.94  ? 286 PRO A C     1 
ATOM   2190 O O     . PRO A 1 306 ? 30.092  -1.837  -15.260 1.00 9.67  ? 286 PRO A O     1 
ATOM   2191 C CB    . PRO A 1 306 ? 32.792  -1.944  -13.936 1.00 10.62 ? 286 PRO A CB    1 
ATOM   2192 C CG    . PRO A 1 306 ? 34.107  -2.256  -14.574 1.00 11.25 ? 286 PRO A CG    1 
ATOM   2193 C CD    . PRO A 1 306 ? 33.790  -2.847  -15.925 1.00 11.14 ? 286 PRO A CD    1 
ATOM   2194 N N     A LEU A 1 307 ? 29.693  -3.232  -13.456 0.50 7.49  ? 287 LEU A N     1 
ATOM   2195 N N     B LEU A 1 307 ? 29.679  -3.224  -13.507 0.50 7.32  ? 287 LEU A N     1 
ATOM   2196 C CA    A LEU A 1 307 ? 28.265  -2.992  -13.238 0.50 7.41  ? 287 LEU A CA    1 
ATOM   2197 C CA    B LEU A 1 307 ? 28.299  -2.810  -13.386 0.50 7.09  ? 287 LEU A CA    1 
ATOM   2198 C C     A LEU A 1 307 ? 28.013  -2.164  -11.986 0.50 6.78  ? 287 LEU A C     1 
ATOM   2199 C C     B LEU A 1 307 ? 28.151  -1.962  -12.141 0.50 6.82  ? 287 LEU A C     1 
ATOM   2200 O O     A LEU A 1 307 ? 28.606  -2.374  -10.904 0.50 5.98  ? 287 LEU A O     1 
ATOM   2201 O O     B LEU A 1 307 ? 29.055  -1.856  -11.290 0.50 6.90  ? 287 LEU A O     1 
ATOM   2202 C CB    A LEU A 1 307 ? 27.519  -4.303  -12.999 0.50 7.92  ? 287 LEU A CB    1 
ATOM   2203 C CB    B LEU A 1 307 ? 27.425  -4.053  -13.323 0.50 7.18  ? 287 LEU A CB    1 
ATOM   2204 C CG    A LEU A 1 307 ? 27.406  -5.233  -14.195 0.50 8.26  ? 287 LEU A CG    1 
ATOM   2205 C CG    B LEU A 1 307 ? 27.566  -4.906  -14.570 0.50 7.01  ? 287 LEU A CG    1 
ATOM   2206 C CD1   A LEU A 1 307 ? 26.406  -6.322  -13.904 0.50 8.52  ? 287 LEU A CD1   1 
ATOM   2207 C CD1   B LEU A 1 307 ? 26.715  -6.147  -14.458 0.50 6.91  ? 287 LEU A CD1   1 
ATOM   2208 C CD2   A LEU A 1 307 ? 27.061  -4.472  -15.462 0.50 8.73  ? 287 LEU A CD2   1 
ATOM   2209 C CD2   B LEU A 1 307 ? 27.248  -4.109  -15.838 0.50 7.12  ? 287 LEU A CD2   1 
ATOM   2210 N N     . ASP A 1 308 ? 26.993  -1.310  -12.080 1.00 6.63  ? 288 ASP A N     1 
ATOM   2211 C CA    . ASP A 1 308 ? 26.592  -0.492  -10.965 1.00 6.52  ? 288 ASP A CA    1 
ATOM   2212 C C     . ASP A 1 308 ? 25.618  -1.172  -10.040 1.00 6.63  ? 288 ASP A C     1 
ATOM   2213 O O     . ASP A 1 308 ? 25.488  -0.727  -8.907  1.00 9.23  ? 288 ASP A O     1 
ATOM   2214 C CB    . ASP A 1 308 ? 26.000  0.818   -11.474 1.00 6.83  ? 288 ASP A CB    1 
ATOM   2215 C CG    . ASP A 1 308 ? 26.977  1.505   -12.378 1.00 7.13  ? 288 ASP A CG    1 
ATOM   2216 O OD1   . ASP A 1 308 ? 28.066  1.951   -11.845 1.00 10.51 ? 288 ASP A OD1   1 
ATOM   2217 O OD2   . ASP A 1 308 ? 26.760  1.649   -13.579 1.00 6.37  ? 288 ASP A OD2   1 
ATOM   2218 N N     . TRP A 1 309 ? 24.868  -2.188  -10.499 1.00 4.98  ? 289 TRP A N     1 
ATOM   2219 C CA    . TRP A 1 309 ? 23.929  -2.889  -9.663  1.00 4.83  ? 289 TRP A CA    1 
ATOM   2220 C C     . TRP A 1 309 ? 23.645  -4.252  -10.292 1.00 4.25  ? 289 TRP A C     1 
ATOM   2221 O O     . TRP A 1 309 ? 23.945  -4.451  -11.478 1.00 4.58  ? 289 TRP A O     1 
ATOM   2222 C CB    . TRP A 1 309 ? 22.655  -2.044  -9.445  1.00 4.63  ? 289 TRP A CB    1 
ATOM   2223 C CG    . TRP A 1 309 ? 21.913  -1.647  -10.683 1.00 4.72  ? 289 TRP A CG    1 
ATOM   2224 C CD1   . TRP A 1 309 ? 22.100  -0.502  -11.376 1.00 4.78  ? 289 TRP A CD1   1 
ATOM   2225 C CD2   . TRP A 1 309 ? 20.844  -2.347  -11.320 1.00 4.70  ? 289 TRP A CD2   1 
ATOM   2226 N NE1   . TRP A 1 309 ? 21.241  -0.423  -12.456 1.00 4.98  ? 289 TRP A NE1   1 
ATOM   2227 C CE2   . TRP A 1 309 ? 20.456  -1.525  -12.414 1.00 4.65  ? 289 TRP A CE2   1 
ATOM   2228 C CE3   . TRP A 1 309 ? 20.153  -3.525  -11.080 1.00 5.01  ? 289 TRP A CE3   1 
ATOM   2229 C CZ2   . TRP A 1 309 ? 19.432  -1.891  -13.256 1.00 5.23  ? 289 TRP A CZ2   1 
ATOM   2230 C CZ3   . TRP A 1 309 ? 19.145  -3.908  -11.936 1.00 5.53  ? 289 TRP A CZ3   1 
ATOM   2231 C CH2   . TRP A 1 309 ? 18.779  -3.051  -12.993 1.00 5.23  ? 289 TRP A CH2   1 
ATOM   2232 N N     . LEU A 1 310 ? 23.056  -5.144  -9.514  1.00 4.07  ? 290 LEU A N     1 
ATOM   2233 C CA    . LEU A 1 310 ? 22.578  -6.421  -10.023 1.00 4.57  ? 290 LEU A CA    1 
ATOM   2234 C C     . LEU A 1 310 ? 21.109  -6.550  -9.673  1.00 4.44  ? 290 LEU A C     1 
ATOM   2235 O O     . LEU A 1 310 ? 20.707  -6.344  -8.533  1.00 4.39  ? 290 LEU A O     1 
ATOM   2236 C CB    . LEU A 1 310 ? 23.372  -7.608  -9.417  1.00 5.32  ? 290 LEU A CB    1 
ATOM   2237 C CG    . LEU A 1 310 ? 22.815  -9.001  -9.709  1.00 5.89  ? 290 LEU A CG    1 
ATOM   2238 C CD1   . LEU A 1 310 ? 23.083  -9.314  -11.133 1.00 6.35  ? 290 LEU A CD1   1 
ATOM   2239 C CD2   . LEU A 1 310 ? 23.461  -10.082 -8.837  1.00 6.94  ? 290 LEU A CD2   1 
ATOM   2240 N N     . GLY A 1 311 ? 20.307  -7.013  -10.638 1.00 3.83  ? 291 GLY A N     1 
ATOM   2241 C CA    . GLY A 1 311 ? 18.922  -7.301  -10.429 1.00 3.80  ? 291 GLY A CA    1 
ATOM   2242 C C     . GLY A 1 311 ? 18.695  -8.798  -10.249 1.00 3.66  ? 291 GLY A C     1 
ATOM   2243 O O     . GLY A 1 311 ? 19.231  -9.574  -11.039 1.00 3.75  ? 291 GLY A O     1 
ATOM   2244 N N     . VAL A 1 312 ? 17.955  -9.146  -9.205  1.00 4.20  ? 292 VAL A N     1 
ATOM   2245 C CA    . VAL A 1 312 ? 17.609  -10.511 -8.897  1.00 4.49  ? 292 VAL A CA    1 
ATOM   2246 C C     . VAL A 1 312 ? 16.136  -10.752 -9.151  1.00 4.16  ? 292 VAL A C     1 
ATOM   2247 O O     . VAL A 1 312 ? 15.295  -10.006 -8.639  1.00 3.82  ? 292 VAL A O     1 
ATOM   2248 C CB    . VAL A 1 312 ? 17.924  -10.801 -7.421  1.00 5.69  ? 292 VAL A CB    1 
ATOM   2249 C CG1   . VAL A 1 312 ? 17.507  -12.216 -7.074  1.00 6.31  ? 292 VAL A CG1   1 
ATOM   2250 C CG2   . VAL A 1 312 ? 19.385  -10.531 -7.130  1.00 6.40  ? 292 VAL A CG2   1 
ATOM   2251 N N     . ASN A 1 313 ? 15.825  -11.724 -9.994  1.00 3.81  ? 293 ASN A N     1 
ATOM   2252 C CA    . ASN A 1 313 ? 14.469  -12.200 -10.175 1.00 3.83  ? 293 ASN A CA    1 
ATOM   2253 C C     . ASN A 1 313 ? 14.344  -13.503 -9.403  1.00 4.45  ? 293 ASN A C     1 
ATOM   2254 O O     . ASN A 1 313 ? 15.184  -14.389 -9.587  1.00 4.65  ? 293 ASN A O     1 
ATOM   2255 C CB    . ASN A 1 313 ? 14.144  -12.435 -11.646 1.00 3.83  ? 293 ASN A CB    1 
ATOM   2256 C CG    . ASN A 1 313 ? 14.104  -11.146 -12.440 1.00 4.04  ? 293 ASN A CG    1 
ATOM   2257 O OD1   . ASN A 1 313 ? 14.272  -10.047 -11.911 1.00 4.04  ? 293 ASN A OD1   1 
ATOM   2258 N ND2   . ASN A 1 313 ? 13.953  -11.305 -13.729 1.00 3.90  ? 293 ASN A ND2   1 
ATOM   2259 N N     . TYR A 1 314 ? 13.361  -13.582 -8.534  1.00 4.33  ? 294 TYR A N     1 
ATOM   2260 C CA    . TYR A 1 314 ? 13.186  -14.722 -7.640  1.00 4.81  ? 294 TYR A CA    1 
ATOM   2261 C C     . TYR A 1 314 ? 11.743  -15.202 -7.644  1.00 4.77  ? 294 TYR A C     1 
ATOM   2262 O O     . TYR A 1 314 ? 10.817  -14.398 -7.408  1.00 3.84  ? 294 TYR A O     1 
ATOM   2263 C CB    . TYR A 1 314 ? 13.561  -14.404 -6.173  1.00 5.51  ? 294 TYR A CB    1 
ATOM   2264 C CG    . TYR A 1 314 ? 13.347  -15.591 -5.268  1.00 5.92  ? 294 TYR A CG    1 
ATOM   2265 C CD1   . TYR A 1 314 ? 14.191  -16.686 -5.347  1.00 7.31  ? 294 TYR A CD1   1 
ATOM   2266 C CD2   . TYR A 1 314 ? 12.223  -15.701 -4.461  1.00 6.18  ? 294 TYR A CD2   1 
ATOM   2267 C CE1   . TYR A 1 314 ? 13.906  -17.841 -4.636  1.00 8.04  ? 294 TYR A CE1   1 
ATOM   2268 C CE2   . TYR A 1 314 ? 11.953  -16.851 -3.724  1.00 6.39  ? 294 TYR A CE2   1 
ATOM   2269 C CZ    . TYR A 1 314 ? 12.818  -17.918 -3.798  1.00 7.70  ? 294 TYR A CZ    1 
ATOM   2270 O OH    . TYR A 1 314 ? 12.538  -19.090 -3.084  1.00 8.61  ? 294 TYR A OH    1 
ATOM   2271 N N     . TYR A 1 315 ? 11.515  -16.492 -7.913  1.00 5.43  ? 295 TYR A N     1 
ATOM   2272 C CA    . TYR A 1 315 ? 10.202  -17.103 -7.870  1.00 6.49  ? 295 TYR A CA    1 
ATOM   2273 C C     . TYR A 1 315 ? 10.152  -18.315 -6.938  1.00 7.44  ? 295 TYR A C     1 
ATOM   2274 O O     . TYR A 1 315 ? 9.124   -18.555 -6.315  1.00 8.51  ? 295 TYR A O     1 
ATOM   2275 C CB    . TYR A 1 315 ? 9.734   -17.494 -9.282  1.00 7.85  ? 295 TYR A CB    1 
ATOM   2276 C CG    . TYR A 1 315 ? 9.504   -16.295 -10.166 1.00 10.16 ? 295 TYR A CG    1 
ATOM   2277 C CD1   . TYR A 1 315 ? 8.255   -15.664 -10.191 1.00 12.35 ? 295 TYR A CD1   1 
ATOM   2278 C CD2   . TYR A 1 315 ? 10.505  -15.765 -10.903 1.00 11.59 ? 295 TYR A CD2   1 
ATOM   2279 C CE1   . TYR A 1 315 ? 8.025   -14.521 -10.946 1.00 11.96 ? 295 TYR A CE1   1 
ATOM   2280 C CE2   . TYR A 1 315 ? 10.313  -14.608 -11.660 1.00 9.72  ? 295 TYR A CE2   1 
ATOM   2281 C CZ    . TYR A 1 315 ? 9.084   -13.990 -11.665 1.00 11.61 ? 295 TYR A CZ    1 
ATOM   2282 O OH    . TYR A 1 315 ? 8.854   -12.873 -12.437 1.00 12.83 ? 295 TYR A OH    1 
ATOM   2283 N N     . GLU A 1 316 ? 11.171  -19.167 -6.966  1.00 8.07  ? 296 GLU A N     1 
ATOM   2284 C CA    . GLU A 1 316 ? 11.050  -20.514 -6.416  1.00 9.51  ? 296 GLU A CA    1 
ATOM   2285 C C     . GLU A 1 316 ? 12.454  -20.995 -6.046  1.00 10.15 ? 296 GLU A C     1 
ATOM   2286 O O     . GLU A 1 316 ? 13.439  -20.510 -6.570  1.00 11.38 ? 296 GLU A O     1 
ATOM   2287 C CB    . GLU A 1 316 ? 10.403  -21.438 -7.457  1.00 12.07 ? 296 GLU A CB    1 
ATOM   2288 C CG    . GLU A 1 316 ? 11.304  -21.640 -8.664  1.00 14.66 ? 296 GLU A CG    1 
ATOM   2289 C CD    . GLU A 1 316 ? 10.709  -22.360 -9.868  1.00 18.55 ? 296 GLU A CD    1 
ATOM   2290 O OE1   . GLU A 1 316 ? 11.487  -22.495 -10.891 1.00 28.30 ? 296 GLU A OE1   1 
ATOM   2291 O OE2   . GLU A 1 316 ? 9.534   -22.846 -9.792  1.00 18.21 ? 296 GLU A OE2   1 
ATOM   2292 N N     . ARG A 1 317 ? 12.509  -22.049 -5.239  1.00 9.93  ? 297 ARG A N     1 
ATOM   2293 C CA    . ARG A 1 317 ? 13.760  -22.772 -5.051  1.00 10.13 ? 297 ARG A CA    1 
ATOM   2294 C C     . ARG A 1 317 ? 13.736  -24.012 -5.924  1.00 9.97  ? 297 ARG A C     1 
ATOM   2295 O O     . ARG A 1 317 ? 12.748  -24.319 -6.603  1.00 11.36 ? 297 ARG A O     1 
ATOM   2296 C CB    . ARG A 1 317 ? 13.889  -23.232 -3.592  1.00 11.64 ? 297 ARG A CB    1 
ATOM   2297 C CG    . ARG A 1 317 ? 12.820  -24.210 -3.156  1.00 12.83 ? 297 ARG A CG    1 
ATOM   2298 C CD    . ARG A 1 317 ? 13.049  -24.980 -1.854  1.00 15.24 ? 297 ARG A CD    1 
ATOM   2299 N NE    . ARG A 1 317 ? 11.959  -25.905 -1.750  1.00 18.31 ? 297 ARG A NE    1 
ATOM   2300 C CZ    . ARG A 1 317 ? 11.869  -26.862 -0.839  1.00 23.03 ? 297 ARG A CZ    1 
ATOM   2301 N NH1   . ARG A 1 317 ? 12.735  -26.860 0.138   1.00 22.21 ? 297 ARG A NH1   1 
ATOM   2302 N NH2   . ARG A 1 317 ? 10.880  -27.739 -0.879  1.00 27.59 ? 297 ARG A NH2   1 
ATOM   2303 N N     . MET A 1 318 ? 14.846  -24.750 -5.877  1.00 9.47  ? 298 MET A N     1 
ATOM   2304 C CA    . MET A 1 318 ? 14.881  -26.095 -6.433  1.00 10.53 ? 298 MET A CA    1 
ATOM   2305 C C     . MET A 1 318 ? 15.378  -27.023 -5.324  1.00 10.94 ? 298 MET A C     1 
ATOM   2306 O O     . MET A 1 318 ? 16.508  -26.885 -4.898  1.00 11.10 ? 298 MET A O     1 
ATOM   2307 C CB    . MET A 1 318 ? 15.830  -26.172 -7.634  1.00 12.62 ? 298 MET A CB    1 
ATOM   2308 C CG    . MET A 1 318 ? 16.183  -27.588 -8.127  1.00 17.17 ? 298 MET A CG    1 
ATOM   2309 S SD    . MET A 1 318 ? 14.787  -28.339 -8.932  1.00 22.06 ? 298 MET A SD    1 
ATOM   2310 C CE    . MET A 1 318 ? 15.684  -29.595 -9.859  1.00 25.35 ? 298 MET A CE    1 
ATOM   2311 N N     . ARG A 1 319 ? 14.538  -27.967 -4.927  1.00 12.02 ? 299 ARG A N     1 
ATOM   2312 C CA    . ARG A 1 319 ? 14.989  -29.072 -4.091  1.00 11.54 ? 299 ARG A CA    1 
ATOM   2313 C C     . ARG A 1 319 ? 15.304  -30.268 -4.983  1.00 11.86 ? 299 ARG A C     1 
ATOM   2314 O O     . ARG A 1 319 ? 14.404  -30.811 -5.624  1.00 14.01 ? 299 ARG A O     1 
ATOM   2315 C CB    . ARG A 1 319 ? 13.904  -29.435 -3.090  1.00 13.70 ? 299 ARG A CB    1 
ATOM   2316 C CG    . ARG A 1 319 ? 14.409  -30.419 -2.046  1.00 18.14 ? 299 ARG A CG    1 
ATOM   2317 C CD    . ARG A 1 319 ? 13.505  -30.437 -0.844  1.00 23.82 ? 299 ARG A CD    1 
ATOM   2318 N NE    . ARG A 1 319 ? 12.286  -31.131 -1.189  1.00 31.27 ? 299 ARG A NE    1 
ATOM   2319 C CZ    . ARG A 1 319 ? 11.836  -32.217 -0.575  1.00 35.80 ? 299 ARG A CZ    1 
ATOM   2320 N NH1   . ARG A 1 319 ? 12.551  -32.792 0.372   1.00 39.75 ? 299 ARG A NH1   1 
ATOM   2321 N NH2   . ARG A 1 319 ? 10.666  -32.719 -0.926  1.00 37.16 ? 299 ARG A NH2   1 
ATOM   2322 N N     . ALA A 1 320 ? 16.592  -30.614 -5.065  1.00 11.62 ? 300 ALA A N     1 
ATOM   2323 C CA    . ALA A 1 320 ? 17.148  -31.407 -6.144  1.00 10.62 ? 300 ALA A CA    1 
ATOM   2324 C C     . ALA A 1 320 ? 17.442  -32.837 -5.718  1.00 11.53 ? 300 ALA A C     1 
ATOM   2325 O O     . ALA A 1 320 ? 18.021  -33.101 -4.652  1.00 10.85 ? 300 ALA A O     1 
ATOM   2326 C CB    . ALA A 1 320 ? 18.411  -30.763 -6.658  1.00 10.66 ? 300 ALA A CB    1 
ATOM   2327 N N     . VAL A 1 321 ? 17.035  -33.752 -6.592  1.00 11.65 ? 301 VAL A N     1 
ATOM   2328 C CA    . VAL A 1 321 ? 17.505  -35.125 -6.531  1.00 12.46 ? 301 VAL A CA    1 
ATOM   2329 C C     . VAL A 1 321 ? 18.272  -35.452 -7.796  1.00 12.33 ? 301 VAL A C     1 
ATOM   2330 O O     . VAL A 1 321 ? 17.970  -34.959 -8.878  1.00 12.28 ? 301 VAL A O     1 
ATOM   2331 C CB    . VAL A 1 321 ? 16.383  -36.154 -6.362  1.00 15.68 ? 301 VAL A CB    1 
ATOM   2332 C CG1   . VAL A 1 321 ? 15.780  -36.075 -4.972  1.00 18.50 ? 301 VAL A CG1   1 
ATOM   2333 C CG2   . VAL A 1 321 ? 15.337  -36.039 -7.453  1.00 16.54 ? 301 VAL A CG2   1 
ATOM   2334 N N     . ASP A 1 322 ? 19.174  -36.435 -7.640  1.00 11.50 ? 302 ASP A N     1 
ATOM   2335 C CA    . ASP A 1 322 ? 19.931  -36.898 -8.778  1.00 12.14 ? 302 ASP A CA    1 
ATOM   2336 C C     . ASP A 1 322 ? 18.970  -37.508 -9.799  1.00 12.95 ? 302 ASP A C     1 
ATOM   2337 O O     . ASP A 1 322 ? 18.042  -38.211 -9.418  1.00 14.53 ? 302 ASP A O     1 
ATOM   2338 C CB    . ASP A 1 322 ? 20.947  -37.947 -8.321  1.00 13.51 ? 302 ASP A CB    1 
ATOM   2339 C CG    . ASP A 1 322 ? 21.998  -38.340 -9.341  1.00 15.90 ? 302 ASP A CG    1 
ATOM   2340 O OD1   . ASP A 1 322 ? 22.329  -37.536 -10.233 1.00 16.87 ? 302 ASP A OD1   1 
ATOM   2341 O OD2   . ASP A 1 322 ? 22.483  -39.506 -9.210  1.00 18.11 ? 302 ASP A OD2   1 
ATOM   2342 N N     . ALA A 1 323 ? 19.269  -37.296 -11.078 1.00 14.40 ? 303 ALA A N     1 
ATOM   2343 C CA    . ALA A 1 323 ? 18.461  -37.848 -12.167 1.00 14.78 ? 303 ALA A CA    1 
ATOM   2344 C C     . ALA A 1 323 ? 19.410  -38.284 -13.278 1.00 15.30 ? 303 ALA A C     1 
ATOM   2345 O O     . ALA A 1 323 ? 19.575  -37.604 -14.283 1.00 15.53 ? 303 ALA A O     1 
ATOM   2346 C CB    . ALA A 1 323 ? 17.467  -36.810 -12.652 1.00 15.23 ? 303 ALA A CB    1 
ATOM   2347 N N     . PRO A 1 324 ? 20.112  -39.423 -13.085 1.00 16.97 ? 304 PRO A N     1 
ATOM   2348 C CA    . PRO A 1 324 ? 21.198  -39.798 -13.992 1.00 18.92 ? 304 PRO A CA    1 
ATOM   2349 C C     . PRO A 1 324 ? 20.684  -39.963 -15.420 1.00 20.67 ? 304 PRO A C     1 
ATOM   2350 O O     . PRO A 1 324 ? 21.360  -39.592 -16.367 1.00 25.00 ? 304 PRO A O     1 
ATOM   2351 C CB    . PRO A 1 324 ? 21.743  -41.123 -13.441 1.00 19.15 ? 304 PRO A CB    1 
ATOM   2352 C CG    . PRO A 1 324 ? 21.123  -41.298 -12.055 1.00 18.88 ? 304 PRO A CG    1 
ATOM   2353 C CD    . PRO A 1 324 ? 19.952  -40.338 -11.939 1.00 16.95 ? 304 PRO A CD    1 
ATOM   2354 N N     . ASP A 1 325 ? 19.438  -40.404 -15.569 1.00 21.90 ? 305 ASP A N     1 
ATOM   2355 C CA    . ASP A 1 325 ? 18.933  -40.714 -16.896 1.00 27.43 ? 305 ASP A CA    1 
ATOM   2356 C C     . ASP A 1 325 ? 18.370  -39.472 -17.591 1.00 25.58 ? 305 ASP A C     1 
ATOM   2357 O O     . ASP A 1 325 ? 18.063  -39.537 -18.774 1.00 26.51 ? 305 ASP A O     1 
ATOM   2358 C CB    . ASP A 1 325 ? 17.913  -41.849 -16.821 1.00 29.93 ? 305 ASP A CB    1 
ATOM   2359 C CG    . ASP A 1 325 ? 18.525  -43.153 -16.334 1.00 34.60 ? 305 ASP A CG    1 
ATOM   2360 O OD1   . ASP A 1 325 ? 19.634  -43.499 -16.815 1.00 35.39 ? 305 ASP A OD1   1 
ATOM   2361 O OD2   . ASP A 1 325 ? 17.880  -43.825 -15.492 1.00 41.97 ? 305 ASP A OD2   1 
ATOM   2362 N N     . ALA A 1 326 ? 18.247  -38.338 -16.884 1.00 24.34 ? 306 ALA A N     1 
ATOM   2363 C CA    . ALA A 1 326 ? 17.683  -37.127 -17.463 1.00 22.46 ? 306 ALA A CA    1 
ATOM   2364 C C     . ALA A 1 326 ? 18.745  -36.349 -18.237 1.00 21.90 ? 306 ALA A C     1 
ATOM   2365 O O     . ALA A 1 326 ? 19.923  -36.679 -18.192 1.00 20.18 ? 306 ALA A O     1 
ATOM   2366 C CB    . ALA A 1 326 ? 17.053  -36.292 -16.382 1.00 23.62 ? 306 ALA A CB    1 
ATOM   2367 N N     . SER A 1 327 ? 18.309  -35.313 -18.968 1.00 21.93 ? 307 SER A N     1 
ATOM   2368 C CA    . SER A 1 327 ? 19.218  -34.434 -19.700 1.00 22.63 ? 307 SER A CA    1 
ATOM   2369 C C     . SER A 1 327 ? 20.051  -33.610 -18.715 1.00 18.00 ? 307 SER A C     1 
ATOM   2370 O O     . SER A 1 327 ? 19.630  -33.437 -17.569 1.00 19.47 ? 307 SER A O     1 
ATOM   2371 C CB    . SER A 1 327 ? 18.483  -33.510 -20.649 1.00 24.43 ? 307 SER A CB    1 
ATOM   2372 O OG    . SER A 1 327 ? 17.351  -34.160 -21.224 1.00 29.57 ? 307 SER A OG    1 
ATOM   2373 N N     . LEU A 1 328 ? 21.211  -33.126 -19.171 1.00 17.74 ? 308 LEU A N     1 
ATOM   2374 C CA    . LEU A 1 328 ? 22.049  -32.263 -18.346 1.00 16.29 ? 308 LEU A CA    1 
ATOM   2375 C C     . LEU A 1 328 ? 21.128  -31.163 -17.813 1.00 16.14 ? 308 LEU A C     1 
ATOM   2376 O O     . LEU A 1 328 ? 20.247  -30.675 -18.520 1.00 15.05 ? 308 LEU A O     1 
ATOM   2377 C CB    . LEU A 1 328 ? 23.269  -31.698 -19.111 1.00 18.40 ? 308 LEU A CB    1 
ATOM   2378 C CG    . LEU A 1 328 ? 24.279  -32.663 -19.773 1.00 20.98 ? 308 LEU A CG    1 
ATOM   2379 C CD1   . LEU A 1 328 ? 25.631  -31.979 -19.958 1.00 21.09 ? 308 LEU A CD1   1 
ATOM   2380 C CD2   . LEU A 1 328 ? 24.487  -33.985 -19.041 1.00 22.55 ? 308 LEU A CD2   1 
ATOM   2381 N N     . PRO A 1 329 ? 21.214  -30.741 -16.527 1.00 13.57 ? 309 PRO A N     1 
ATOM   2382 C CA    . PRO A 1 329 ? 22.244  -31.194 -15.587 1.00 13.64 ? 309 PRO A CA    1 
ATOM   2383 C C     . PRO A 1 329 ? 21.964  -32.391 -14.672 1.00 12.87 ? 309 PRO A C     1 
ATOM   2384 O O     . PRO A 1 329 ? 22.527  -32.480 -13.565 1.00 11.07 ? 309 PRO A O     1 
ATOM   2385 C CB    . PRO A 1 329 ? 22.405  -29.933 -14.715 1.00 13.40 ? 309 PRO A CB    1 
ATOM   2386 C CG    . PRO A 1 329 ? 21.026  -29.379 -14.632 1.00 13.72 ? 309 PRO A CG    1 
ATOM   2387 C CD    . PRO A 1 329 ? 20.436  -29.600 -16.011 1.00 14.20 ? 309 PRO A CD    1 
ATOM   2388 N N     . GLN A 1 330 ? 21.092  -33.295 -15.110 1.00 12.05 ? 310 GLN A N     1 
ATOM   2389 C CA    . GLN A 1 330 ? 20.849  -34.549 -14.420 1.00 12.51 ? 310 GLN A CA    1 
ATOM   2390 C C     . GLN A 1 330 ? 20.392  -34.291 -12.989 1.00 13.12 ? 310 GLN A C     1 
ATOM   2391 O O     . GLN A 1 330 ? 20.914  -34.895 -12.040 1.00 10.22 ? 310 GLN A O     1 
ATOM   2392 C CB    . GLN A 1 330 ? 22.118  -35.402 -14.500 1.00 12.84 ? 310 GLN A CB    1 
ATOM   2393 C CG    . GLN A 1 330 ? 22.359  -35.973 -15.894 1.00 13.30 ? 310 GLN A CG    1 
ATOM   2394 C CD    . GLN A 1 330 ? 23.729  -36.581 -16.033 1.00 16.41 ? 310 GLN A CD    1 
ATOM   2395 O OE1   . GLN A 1 330 ? 24.746  -35.903 -15.964 1.00 17.16 ? 310 GLN A OE1   1 
ATOM   2396 N NE2   . GLN A 1 330 ? 23.790  -37.895 -16.254 1.00 19.31 ? 310 GLN A NE2   1 
ATOM   2397 N N     . ALA A 1 331 ? 19.390  -33.411 -12.848 1.00 13.05 ? 311 ALA A N     1 
ATOM   2398 C CA    . ALA A 1 331 ? 18.889  -33.055 -11.528 1.00 15.45 ? 311 ALA A CA    1 
ATOM   2399 C C     . ALA A 1 331 ? 17.409  -32.754 -11.629 1.00 16.89 ? 311 ALA A C     1 
ATOM   2400 O O     . ALA A 1 331 ? 17.054  -31.908 -12.450 1.00 20.87 ? 311 ALA A O     1 
ATOM   2401 C CB    . ALA A 1 331 ? 19.637  -31.841 -11.017 1.00 14.84 ? 311 ALA A CB    1 
ATOM   2402 N N     . GLN A 1 332 ? 16.577  -33.440 -10.854 1.00 17.12 ? 312 GLN A N     1 
ATOM   2403 C CA    . GLN A 1 332 ? 15.149  -33.175 -10.933 1.00 20.22 ? 312 GLN A CA    1 
ATOM   2404 C C     . GLN A 1 332 ? 14.589  -32.652 -9.620  1.00 19.92 ? 312 GLN A C     1 
ATOM   2405 O O     . GLN A 1 332 ? 15.127  -32.859 -8.532  1.00 15.13 ? 312 GLN A O     1 
ATOM   2406 C CB    . GLN A 1 332 ? 14.414  -34.423 -11.401 1.00 27.85 ? 312 GLN A CB    1 
ATOM   2407 C CG    . GLN A 1 332 ? 14.651  -34.676 -12.886 1.00 35.23 ? 312 GLN A CG    1 
ATOM   2408 C CD    . GLN A 1 332 ? 14.060  -35.984 -13.356 1.00 39.92 ? 312 GLN A CD    1 
ATOM   2409 O OE1   . GLN A 1 332 ? 13.395  -36.699 -12.604 1.00 41.33 ? 312 GLN A OE1   1 
ATOM   2410 N NE2   . GLN A 1 332 ? 14.311  -36.303 -14.617 1.00 39.80 ? 312 GLN A NE2   1 
ATOM   2411 N N     . ARG A 1 333 ? 13.475  -31.940 -9.756  1.00 19.54 ? 313 ARG A N     1 
ATOM   2412 C CA    . ARG A 1 333 ? 12.817  -31.304 -8.636  1.00 21.68 ? 313 ARG A CA    1 
ATOM   2413 C C     . ARG A 1 333 ? 12.069  -32.362 -7.834  1.00 21.30 ? 313 ARG A C     1 
ATOM   2414 O O     . ARG A 1 333 ? 11.393  -33.209 -8.407  1.00 22.29 ? 313 ARG A O     1 
ATOM   2415 C CB    . ARG A 1 333 ? 11.864  -30.227 -9.179  1.00 25.13 ? 313 ARG A CB    1 
ATOM   2416 C CG    . ARG A 1 333 ? 10.890  -29.676 -8.148  1.00 30.27 ? 313 ARG A CG    1 
ATOM   2417 C CD    . ARG A 1 333 ? 10.104  -28.487 -8.688  1.00 30.73 ? 313 ARG A CD    1 
ATOM   2418 N NE    . ARG A 1 333 ? 10.816  -27.241 -8.431  1.00 35.68 ? 313 ARG A NE    1 
ATOM   2419 C CZ    . ARG A 1 333 ? 11.487  -26.571 -9.358  1.00 32.79 ? 313 ARG A CZ    1 
ATOM   2420 N NH1   . ARG A 1 333 ? 11.543  -27.031 -10.596 1.00 40.35 ? 313 ARG A NH1   1 
ATOM   2421 N NH2   . ARG A 1 333 ? 12.116  -25.456 -9.059  1.00 29.13 ? 313 ARG A NH2   1 
ATOM   2422 N N     . LEU A 1 334 ? 12.238  -32.357 -6.506  1.00 20.94 ? 314 LEU A N     1 
ATOM   2423 C CA    . LEU A 1 334 ? 11.397  -33.158 -5.631  1.00 24.85 ? 314 LEU A CA    1 
ATOM   2424 C C     . LEU A 1 334 ? 10.492  -32.220 -4.836  1.00 28.28 ? 314 LEU A C     1 
ATOM   2425 O O     . LEU A 1 334 ? 10.961  -31.489 -3.980  1.00 27.27 ? 314 LEU A O     1 
ATOM   2426 C CB    . LEU A 1 334 ? 12.290  -33.998 -4.723  1.00 26.00 ? 314 LEU A CB    1 
ATOM   2427 C CG    . LEU A 1 334 ? 11.567  -34.952 -3.783  1.00 27.28 ? 314 LEU A CG    1 
ATOM   2428 C CD1   . LEU A 1 334 ? 10.958  -36.122 -4.553  1.00 28.93 ? 314 LEU A CD1   1 
ATOM   2429 C CD2   . LEU A 1 334 ? 12.525  -35.440 -2.716  1.00 25.93 ? 314 LEU A CD2   1 
ATOM   2430 N N     . ASP A 1 335 ? 9.191   -32.226 -5.145  1.00 41.16 ? 315 ASP A N     1 
ATOM   2431 C CA    . ASP A 1 335 ? 8.298   -31.247 -4.548  1.00 49.12 ? 315 ASP A CA    1 
ATOM   2432 C C     . ASP A 1 335 ? 8.034   -31.677 -3.109  1.00 50.54 ? 315 ASP A C     1 
ATOM   2433 O O     . ASP A 1 335 ? 7.818   -32.856 -2.838  1.00 49.31 ? 315 ASP A O     1 
ATOM   2434 C CB    . ASP A 1 335 ? 7.064   -31.002 -5.422  1.00 55.13 ? 315 ASP A CB    1 
ATOM   2435 C CG    . ASP A 1 335 ? 7.379   -30.139 -6.638  1.00 57.12 ? 315 ASP A CG    1 
ATOM   2436 O OD1   . ASP A 1 335 ? 7.634   -28.902 -6.452  1.00 47.75 ? 315 ASP A OD1   1 
ATOM   2437 O OD2   . ASP A 1 335 ? 7.417   -30.709 -7.758  1.00 56.13 ? 315 ASP A OD2   1 
ATOM   2438 N N     . ASP A 1 336 ? 8.190   -30.706 -2.200  1.00 58.73 ? 316 ASP A N     1 
ATOM   2439 C CA    . ASP A 1 336 ? 7.910   -30.847 -0.780  1.00 55.16 ? 316 ASP A CA    1 
ATOM   2440 C C     . ASP A 1 336 ? 6.425   -30.534 -0.605  1.00 57.95 ? 316 ASP A C     1 
ATOM   2441 O O     . ASP A 1 336 ? 6.035   -29.370 -0.627  1.00 52.89 ? 316 ASP A O     1 
ATOM   2442 C CB    . ASP A 1 336 ? 8.864   -29.926 -0.009  1.00 51.11 ? 316 ASP A CB    1 
ATOM   2443 C CG    . ASP A 1 336 ? 8.889   -30.016 1.509   1.00 49.25 ? 316 ASP A CG    1 
ATOM   2444 O OD1   . ASP A 1 336 ? 8.022   -30.693 2.080   1.00 42.44 ? 316 ASP A OD1   1 
ATOM   2445 O OD2   . ASP A 1 336 ? 9.791   -29.391 2.112   1.00 45.17 ? 316 ASP A OD2   1 
ATOM   2446 N N     . PRO A 1 337 ? 5.539   -31.555 -0.488  1.00 67.99 ? 317 PRO A N     1 
ATOM   2447 C CA    . PRO A 1 337 ? 4.093   -31.317 -0.479  1.00 66.41 ? 317 PRO A CA    1 
ATOM   2448 C C     . PRO A 1 337 ? 3.623   -30.704 0.838   1.00 59.68 ? 317 PRO A C     1 
ATOM   2449 O O     . PRO A 1 337 ? 2.462   -30.319 0.948   1.00 58.01 ? 317 PRO A O     1 
ATOM   2450 C CB    . PRO A 1 337 ? 3.496   -32.712 -0.713  1.00 68.83 ? 317 PRO A CB    1 
ATOM   2451 C CG    . PRO A 1 337 ? 4.528   -33.660 -0.123  1.00 70.68 ? 317 PRO A CG    1 
ATOM   2452 C CD    . PRO A 1 337 ? 5.869   -32.983 -0.326  1.00 69.51 ? 317 PRO A CD    1 
ATOM   2453 N N     . ASP A 1 338 ? 4.534   -30.627 1.826   1.00 52.22 ? 318 ASP A N     1 
ATOM   2454 C CA    . ASP A 1 338 ? 4.336   -29.765 2.979   1.00 50.83 ? 318 ASP A CA    1 
ATOM   2455 C C     . ASP A 1 338 ? 4.150   -28.332 2.488   1.00 44.99 ? 318 ASP A C     1 
ATOM   2456 O O     . ASP A 1 338 ? 3.093   -27.736 2.697   1.00 51.67 ? 318 ASP A O     1 
ATOM   2457 C CB    . ASP A 1 338 ? 5.490   -29.859 3.983   1.00 52.90 ? 318 ASP A CB    1 
ATOM   2458 C CG    . ASP A 1 338 ? 5.381   -31.036 4.937   1.00 56.41 ? 318 ASP A CG    1 
ATOM   2459 O OD1   . ASP A 1 338 ? 4.298   -31.667 4.980   1.00 58.75 ? 318 ASP A OD1   1 
ATOM   2460 O OD2   . ASP A 1 338 ? 6.380   -31.318 5.623   1.00 54.68 ? 318 ASP A OD2   1 
ATOM   2461 N N     . LEU A 1 339 ? 5.153   -27.819 1.766   1.00 34.98 ? 319 LEU A N     1 
ATOM   2462 C CA    . LEU A 1 339 ? 5.077   -26.471 1.230   1.00 30.53 ? 319 LEU A CA    1 
ATOM   2463 C C     . LEU A 1 339 ? 3.912   -26.369 0.256   1.00 25.66 ? 319 LEU A C     1 
ATOM   2464 O O     . LEU A 1 339 ? 3.675   -27.266 -0.570  1.00 27.00 ? 319 LEU A O     1 
ATOM   2465 C CB    . LEU A 1 339 ? 6.385   -26.100 0.538   1.00 28.57 ? 319 LEU A CB    1 
ATOM   2466 C CG    . LEU A 1 339 ? 7.584   -26.064 1.474   1.00 31.63 ? 319 LEU A CG    1 
ATOM   2467 C CD1   . LEU A 1 339 ? 8.834   -25.751 0.691   1.00 33.94 ? 319 LEU A CD1   1 
ATOM   2468 C CD2   . LEU A 1 339 ? 7.375   -25.074 2.615   1.00 32.73 ? 319 LEU A CD2   1 
ATOM   2469 N N     . PRO A 1 340 ? 3.181   -25.236 0.320   1.00 21.08 ? 320 PRO A N     1 
ATOM   2470 C CA    . PRO A 1 340 ? 2.129   -24.932 -0.635  1.00 20.68 ? 320 PRO A CA    1 
ATOM   2471 C C     . PRO A 1 340 ? 2.610   -24.427 -2.007  1.00 20.10 ? 320 PRO A C     1 
ATOM   2472 O O     . PRO A 1 340 ? 3.749   -24.001 -2.150  1.00 17.52 ? 320 PRO A O     1 
ATOM   2473 C CB    . PRO A 1 340 ? 1.392   -23.779 0.054   1.00 21.20 ? 320 PRO A CB    1 
ATOM   2474 C CG    . PRO A 1 340 ? 2.463   -23.046 0.835   1.00 20.14 ? 320 PRO A CG    1 
ATOM   2475 C CD    . PRO A 1 340 ? 3.451   -24.117 1.244   1.00 20.28 ? 320 PRO A CD    1 
ATOM   2476 N N     . HIS A 1 341 ? 1.702   -24.508 -2.981  1.00 20.29 ? 321 HIS A N     1 
ATOM   2477 C CA    . HIS A 1 341 ? 1.988   -24.280 -4.386  1.00 19.85 ? 321 HIS A CA    1 
ATOM   2478 C C     . HIS A 1 341 ? 1.038   -23.210 -4.883  1.00 17.78 ? 321 HIS A C     1 
ATOM   2479 O O     . HIS A 1 341 ? -0.072  -23.082 -4.377  1.00 16.83 ? 321 HIS A O     1 
ATOM   2480 C CB    . HIS A 1 341 ? 1.801   -25.567 -5.211  1.00 19.65 ? 321 HIS A CB    1 
ATOM   2481 C CG    . HIS A 1 341 ? 2.938   -26.524 -5.061  1.00 22.55 ? 321 HIS A CG    1 
ATOM   2482 N ND1   . HIS A 1 341 ? 3.765   -26.855 -6.111  1.00 24.96 ? 321 HIS A ND1   1 
ATOM   2483 C CD2   . HIS A 1 341 ? 3.405   -27.193 -3.983  1.00 22.72 ? 321 HIS A CD2   1 
ATOM   2484 C CE1   . HIS A 1 341 ? 4.683   -27.708 -5.687  1.00 27.71 ? 321 HIS A CE1   1 
ATOM   2485 N NE2   . HIS A 1 341 ? 4.496   -27.920 -4.407  1.00 25.73 ? 321 HIS A NE2   1 
ATOM   2486 N N     . THR A 1 342 ? 1.490   -22.419 -5.871  1.00 18.40 ? 322 THR A N     1 
ATOM   2487 C CA    . THR A 1 342 ? 0.611   -21.515 -6.596  1.00 16.33 ? 322 THR A CA    1 
ATOM   2488 C C     . THR A 1 342 ? 0.009   -22.242 -7.791  1.00 16.51 ? 322 THR A C     1 
ATOM   2489 O O     . THR A 1 342 ? -0.079  -23.481 -7.746  1.00 17.55 ? 322 THR A O     1 
ATOM   2490 C CB    . THR A 1 342 ? 1.397   -20.273 -7.032  1.00 14.33 ? 322 THR A CB    1 
ATOM   2491 O OG1   . THR A 1 342 ? 2.241   -20.756 -8.092  1.00 14.72 ? 322 THR A OG1   1 
ATOM   2492 C CG2   . THR A 1 342 ? 2.156   -19.654 -5.892  1.00 15.02 ? 322 THR A CG2   1 
ATOM   2493 N N     . ALA A 1 343 ? -0.421  -21.517 -8.835  1.00 16.18 ? 323 ALA A N     1 
ATOM   2494 C CA    . ALA A 1 343 ? -0.935  -22.148 -10.036 1.00 15.21 ? 323 ALA A CA    1 
ATOM   2495 C C     . ALA A 1 343 ? 0.174   -22.945 -10.736 1.00 18.41 ? 323 ALA A C     1 
ATOM   2496 O O     . ALA A 1 343 ? -0.117  -23.872 -11.492 1.00 18.26 ? 323 ALA A O     1 
ATOM   2497 C CB    . ALA A 1 343 ? -1.634  -21.172 -10.965 1.00 16.08 ? 323 ALA A CB    1 
ATOM   2498 N N     . ASP A 1 344 ? 1.440   -22.544 -10.592 1.00 14.34 ? 324 ASP A N     1 
ATOM   2499 C CA    . ASP A 1 344 ? 2.477   -23.171 -11.407 1.00 14.20 ? 324 ASP A CA    1 
ATOM   2500 C C     . ASP A 1 344 ? 3.758   -23.416 -10.619 1.00 12.82 ? 324 ASP A C     1 
ATOM   2501 O O     . ASP A 1 344 ? 4.654   -24.069 -11.175 1.00 14.57 ? 324 ASP A O     1 
ATOM   2502 C CB    . ASP A 1 344 ? 2.821   -22.354 -12.652 1.00 13.69 ? 324 ASP A CB    1 
ATOM   2503 C CG    . ASP A 1 344 ? 3.299   -20.927 -12.383 1.00 15.03 ? 324 ASP A CG    1 
ATOM   2504 O OD1   . ASP A 1 344 ? 3.120   -20.466 -11.239 1.00 13.98 ? 324 ASP A OD1   1 
ATOM   2505 O OD2   . ASP A 1 344 ? 3.893   -20.333 -13.335 1.00 15.68 ? 324 ASP A OD2   1 
ATOM   2506 N N     . ARG A 1 345 ? 3.884   -22.932 -9.381  1.00 13.97 ? 325 ARG A N     1 
ATOM   2507 C CA    . ARG A 1 345 ? 5.113   -23.058 -8.628  1.00 12.65 ? 325 ARG A CA    1 
ATOM   2508 C C     . ARG A 1 345 ? 4.934   -23.372 -7.142  1.00 15.30 ? 325 ARG A C     1 
ATOM   2509 O O     . ARG A 1 345 ? 3.890   -23.140 -6.527  1.00 16.21 ? 325 ARG A O     1 
ATOM   2510 C CB    . ARG A 1 345 ? 5.965   -21.783 -8.697  1.00 12.86 ? 325 ARG A CB    1 
ATOM   2511 C CG    . ARG A 1 345 ? 6.294   -21.362 -10.115 1.00 14.52 ? 325 ARG A CG    1 
ATOM   2512 C CD    . ARG A 1 345 ? 7.196   -20.135 -10.094 1.00 15.31 ? 325 ARG A CD    1 
ATOM   2513 N NE    . ARG A 1 345 ? 7.343   -19.557 -11.426 1.00 15.52 ? 325 ARG A NE    1 
ATOM   2514 C CZ    . ARG A 1 345 ? 8.261   -19.922 -12.302 1.00 21.90 ? 325 ARG A CZ    1 
ATOM   2515 N NH1   . ARG A 1 345 ? 9.298   -20.628 -11.911 1.00 22.86 ? 325 ARG A NH1   1 
ATOM   2516 N NH2   . ARG A 1 345 ? 8.160   -19.533 -13.559 1.00 24.78 ? 325 ARG A NH2   1 
ATOM   2517 N N     . GLU A 1 346 ? 6.002   -23.902 -6.553  1.00 15.00 ? 326 GLU A N     1 
ATOM   2518 C CA    . GLU A 1 346 ? 6.131   -24.081 -5.113  1.00 16.47 ? 326 GLU A CA    1 
ATOM   2519 C C     . GLU A 1 346 ? 6.477   -22.750 -4.452  1.00 16.02 ? 326 GLU A C     1 
ATOM   2520 O O     . GLU A 1 346 ? 7.430   -22.063 -4.853  1.00 15.51 ? 326 GLU A O     1 
ATOM   2521 C CB    . GLU A 1 346 ? 7.252   -25.083 -4.830  1.00 17.69 ? 326 GLU A CB    1 
ATOM   2522 C CG    . GLU A 1 346 ? 7.481   -25.411 -3.379  1.00 20.17 ? 326 GLU A CG    1 
ATOM   2523 C CD    . GLU A 1 346 ? 8.783   -26.147 -3.140  1.00 22.64 ? 326 GLU A CD    1 
ATOM   2524 O OE1   . GLU A 1 346 ? 9.872   -25.546 -3.277  1.00 19.76 ? 326 GLU A OE1   1 
ATOM   2525 O OE2   . GLU A 1 346 ? 8.692   -27.351 -2.819  1.00 25.62 ? 326 GLU A OE2   1 
ATOM   2526 N N     . VAL A 1 347 ? 5.775   -22.408 -3.366  1.00 13.36 ? 327 VAL A N     1 
ATOM   2527 C CA    . VAL A 1 347 ? 6.079   -21.173 -2.656  1.00 14.24 ? 327 VAL A CA    1 
ATOM   2528 C C     . VAL A 1 347 ? 7.144   -21.459 -1.600  1.00 13.83 ? 327 VAL A C     1 
ATOM   2529 O O     . VAL A 1 347 ? 7.007   -22.353 -0.761  1.00 17.68 ? 327 VAL A O     1 
ATOM   2530 C CB    . VAL A 1 347 ? 4.819   -20.548 -2.035  1.00 13.88 ? 327 VAL A CB    1 
ATOM   2531 C CG1   . VAL A 1 347 ? 5.154   -19.279 -1.246  1.00 14.65 ? 327 VAL A CG1   1 
ATOM   2532 C CG2   . VAL A 1 347 ? 3.718   -20.277 -3.053  1.00 14.99 ? 327 VAL A CG2   1 
ATOM   2533 N N     . TYR A 1 348 ? 8.219   -20.671 -1.586  1.00 12.86 ? 328 TYR A N     1 
ATOM   2534 C CA    . TYR A 1 348 ? 9.288   -20.871 -0.632  1.00 11.82 ? 328 TYR A CA    1 
ATOM   2535 C C     . TYR A 1 348 ? 9.968   -19.531 -0.336  1.00 11.10 ? 328 TYR A C     1 
ATOM   2536 O O     . TYR A 1 348 ? 11.048  -19.211 -0.849  1.00 9.93  ? 328 TYR A O     1 
ATOM   2537 C CB    . TYR A 1 348 ? 10.282  -21.913 -1.134  1.00 12.95 ? 328 TYR A CB    1 
ATOM   2538 C CG    . TYR A 1 348 ? 11.223  -22.372 -0.053  1.00 12.56 ? 328 TYR A CG    1 
ATOM   2539 C CD1   . TYR A 1 348 ? 10.740  -23.115 1.011   1.00 15.02 ? 328 TYR A CD1   1 
ATOM   2540 C CD2   . TYR A 1 348 ? 12.555  -22.016 -0.042  1.00 13.24 ? 328 TYR A CD2   1 
ATOM   2541 C CE1   . TYR A 1 348 ? 11.597  -23.582 1.997   1.00 13.87 ? 328 TYR A CE1   1 
ATOM   2542 C CE2   . TYR A 1 348 ? 13.406  -22.400 0.972   1.00 13.69 ? 328 TYR A CE2   1 
ATOM   2543 C CZ    . TYR A 1 348 ? 12.926  -23.222 1.971   1.00 15.28 ? 328 TYR A CZ    1 
ATOM   2544 O OH    . TYR A 1 348 ? 13.719  -23.632 2.987   1.00 16.94 ? 328 TYR A OH    1 
ATOM   2545 N N     . PRO A 1 349 ? 9.374   -18.694 0.539   1.00 12.12 ? 329 PRO A N     1 
ATOM   2546 C CA    . PRO A 1 349 ? 9.920   -17.342 0.720   1.00 11.27 ? 329 PRO A CA    1 
ATOM   2547 C C     . PRO A 1 349 ? 11.340  -17.292 1.231   1.00 10.43 ? 329 PRO A C     1 
ATOM   2548 O O     . PRO A 1 349 ? 12.146  -16.420 0.928   1.00 9.85  ? 329 PRO A O     1 
ATOM   2549 C CB    . PRO A 1 349 ? 8.953   -16.736 1.731   1.00 12.34 ? 329 PRO A CB    1 
ATOM   2550 C CG    . PRO A 1 349 ? 7.674   -17.498 1.514   1.00 14.08 ? 329 PRO A CG    1 
ATOM   2551 C CD    . PRO A 1 349 ? 8.137   -18.921 1.282   1.00 13.56 ? 329 PRO A CD    1 
ATOM   2552 N N     . GLU A 1 350 ? 11.710  -18.266 2.078   1.00 11.26 ? 330 GLU A N     1 
ATOM   2553 C CA    . GLU A 1 350 ? 13.012  -18.260 2.683   1.00 9.86  ? 330 GLU A CA    1 
ATOM   2554 C C     . GLU A 1 350 ? 14.173  -18.399 1.685   1.00 10.53 ? 330 GLU A C     1 
ATOM   2555 O O     . GLU A 1 350 ? 15.306  -18.035 1.933   1.00 11.68 ? 330 GLU A O     1 
ATOM   2556 C CB    . GLU A 1 350 ? 13.038  -19.400 3.711   1.00 10.93 ? 330 GLU A CB    1 
ATOM   2557 C CG    . GLU A 1 350 ? 12.083  -19.156 4.870   1.00 12.18 ? 330 GLU A CG    1 
ATOM   2558 C CD    . GLU A 1 350 ? 10.622  -19.573 4.726   1.00 14.52 ? 330 GLU A CD    1 
ATOM   2559 O OE1   . GLU A 1 350 ? 10.222  -20.083 3.638   1.00 16.00 ? 330 GLU A OE1   1 
ATOM   2560 O OE2   . GLU A 1 350 ? 9.853   -19.352 5.733   1.00 17.69 ? 330 GLU A OE2   1 
ATOM   2561 N N     . GLY A 1 351 ? 13.880  -18.912 0.476   1.00 10.04 ? 331 GLY A N     1 
ATOM   2562 C CA    . GLY A 1 351 ? 14.913  -19.000 -0.556  1.00 9.89  ? 331 GLY A CA    1 
ATOM   2563 C C     . GLY A 1 351 ? 15.432  -17.635 -1.031  1.00 7.76  ? 331 GLY A C     1 
ATOM   2564 O O     . GLY A 1 351 ? 16.577  -17.478 -1.392  1.00 8.81  ? 331 GLY A O     1 
ATOM   2565 N N     . LEU A 1 352 ? 14.558  -16.627 -0.897  1.00 9.42  ? 332 LEU A N     1 
ATOM   2566 C CA    . LEU A 1 352 ? 14.951  -15.265 -1.224  1.00 9.21  ? 332 LEU A CA    1 
ATOM   2567 C C     . LEU A 1 352 ? 15.974  -14.731 -0.225  1.00 9.21  ? 332 LEU A C     1 
ATOM   2568 O O     . LEU A 1 352 ? 16.976  -14.163 -0.609  1.00 8.27  ? 332 LEU A O     1 
ATOM   2569 C CB    . LEU A 1 352 ? 13.733  -14.355 -1.257  1.00 9.11  ? 332 LEU A CB    1 
ATOM   2570 C CG    . LEU A 1 352 ? 13.965  -12.872 -1.621  1.00 8.46  ? 332 LEU A CG    1 
ATOM   2571 C CD1   . LEU A 1 352 ? 14.670  -12.700 -2.952  1.00 8.75  ? 332 LEU A CD1   1 
ATOM   2572 C CD2   . LEU A 1 352 ? 12.644  -12.148 -1.691  1.00 9.04  ? 332 LEU A CD2   1 
ATOM   2573 N N     . TYR A 1 353 ? 15.708  -15.062 1.060   1.00 10.28 ? 333 TYR A N     1 
ATOM   2574 C CA    . TYR A 1 353 ? 16.693  -14.737 2.064   1.00 11.29 ? 333 TYR A CA    1 
ATOM   2575 C C     . TYR A 1 353 ? 18.011  -15.438 1.749   1.00 9.94  ? 333 TYR A C     1 
ATOM   2576 O O     . TYR A 1 353 ? 19.050  -14.840 1.745   1.00 9.69  ? 333 TYR A O     1 
ATOM   2577 C CB    . TYR A 1 353 ? 16.172  -15.052 3.472   1.00 11.68 ? 333 TYR A CB    1 
ATOM   2578 C CG    . TYR A 1 353 ? 17.187  -14.799 4.555   1.00 12.24 ? 333 TYR A CG    1 
ATOM   2579 C CD1   . TYR A 1 353 ? 18.140  -15.745 4.903   1.00 12.96 ? 333 TYR A CD1   1 
ATOM   2580 C CD2   . TYR A 1 353 ? 17.185  -13.601 5.243   1.00 13.16 ? 333 TYR A CD2   1 
ATOM   2581 C CE1   . TYR A 1 353 ? 19.106  -15.474 5.859   1.00 14.38 ? 333 TYR A CE1   1 
ATOM   2582 C CE2   . TYR A 1 353 ? 18.107  -13.346 6.243   1.00 13.17 ? 333 TYR A CE2   1 
ATOM   2583 C CZ    . TYR A 1 353 ? 19.071  -14.288 6.552   1.00 14.75 ? 333 TYR A CZ    1 
ATOM   2584 O OH    . TYR A 1 353 ? 19.992  -14.022 7.539   1.00 14.83 ? 333 TYR A OH    1 
ATOM   2585 N N     . ASP A 1 354 ? 17.945  -16.741 1.503   1.00 9.73  ? 334 ASP A N     1 
ATOM   2586 C CA    . ASP A 1 354 ? 19.160  -17.512 1.300   1.00 10.45 ? 334 ASP A CA    1 
ATOM   2587 C C     . ASP A 1 354 ? 19.951  -16.960 0.118   1.00 9.20  ? 334 ASP A C     1 
ATOM   2588 O O     . ASP A 1 354 ? 21.132  -16.781 0.179   1.00 9.01  ? 334 ASP A O     1 
ATOM   2589 C CB    . ASP A 1 354 ? 18.822  -18.998 1.130   1.00 10.55 ? 334 ASP A CB    1 
ATOM   2590 C CG    . ASP A 1 354 ? 18.354  -19.740 2.391   1.00 12.67 ? 334 ASP A CG    1 
ATOM   2591 O OD1   . ASP A 1 354 ? 18.498  -19.177 3.555   1.00 13.17 ? 334 ASP A OD1   1 
ATOM   2592 O OD2   . ASP A 1 354 ? 17.689  -20.803 2.250   1.00 14.50 ? 334 ASP A OD2   1 
ATOM   2593 N N     . ILE A 1 355 ? 19.274  -16.680 -1.021  1.00 8.75  ? 335 ILE A N     1 
ATOM   2594 C CA    . ILE A 1 355 ? 20.025  -16.271 -2.186  1.00 9.13  ? 335 ILE A CA    1 
ATOM   2595 C C     . ILE A 1 355 ? 20.639  -14.873 -2.035  1.00 7.59  ? 335 ILE A C     1 
ATOM   2596 O O     . ILE A 1 355 ? 21.703  -14.589 -2.519  1.00 7.64  ? 335 ILE A O     1 
ATOM   2597 C CB    . ILE A 1 355 ? 19.134  -16.428 -3.448  1.00 9.47  ? 335 ILE A CB    1 
ATOM   2598 C CG1   . ILE A 1 355 ? 20.020  -16.540 -4.679  1.00 10.04 ? 335 ILE A CG1   1 
ATOM   2599 C CG2   . ILE A 1 355 ? 18.108  -15.334 -3.610  1.00 9.45  ? 335 ILE A CG2   1 
ATOM   2600 C CD1   . ILE A 1 355 ? 20.583  -17.896 -4.883  1.00 12.16 ? 335 ILE A CD1   1 
ATOM   2601 N N     . LEU A 1 356 ? 19.924  -13.974 -1.337  1.00 9.11  ? 336 LEU A N     1 
ATOM   2602 C CA    . LEU A 1 356 ? 20.467  -12.667 -1.057  1.00 8.52  ? 336 LEU A CA    1 
ATOM   2603 C C     . LEU A 1 356 ? 21.664  -12.747 -0.102  1.00 8.32  ? 336 LEU A C     1 
ATOM   2604 O O     . LEU A 1 356 ? 22.595  -12.026 -0.344  1.00 7.79  ? 336 LEU A O     1 
ATOM   2605 C CB    . LEU A 1 356 ? 19.357  -11.778 -0.468  1.00 8.60  ? 336 LEU A CB    1 
ATOM   2606 C CG    . LEU A 1 356 ? 18.265  -11.400 -1.475  1.00 9.44  ? 336 LEU A CG    1 
ATOM   2607 C CD1   . LEU A 1 356 ? 17.127  -10.664 -0.834  1.00 9.41  ? 336 LEU A CD1   1 
ATOM   2608 C CD2   . LEU A 1 356 ? 18.883  -10.593 -2.593  1.00 10.18 ? 336 LEU A CD2   1 
ATOM   2609 N N     . LEU A 1 357 ? 21.575  -13.606 0.917   1.00 8.67  ? 337 LEU A N     1 
ATOM   2610 C CA    . LEU A 1 357 ? 22.704  -13.775 1.849   1.00 10.64 ? 337 LEU A CA    1 
ATOM   2611 C C     . LEU A 1 357 ? 23.908  -14.323 1.091   1.00 10.46 ? 337 LEU A C     1 
ATOM   2612 O O     . LEU A 1 357 ? 25.033  -13.863 1.235   1.00 11.32 ? 337 LEU A O     1 
ATOM   2613 C CB    . LEU A 1 357 ? 22.315  -14.691 3.015   1.00 11.17 ? 337 LEU A CB    1 
ATOM   2614 C CG    . LEU A 1 357 ? 21.829  -13.984 4.286   1.00 12.70 ? 337 LEU A CG    1 
ATOM   2615 C CD1   . LEU A 1 357 ? 22.979  -13.228 4.911   1.00 14.29 ? 337 LEU A CD1   1 
ATOM   2616 C CD2   . LEU A 1 357 ? 20.698  -12.996 3.995   1.00 13.93 ? 337 LEU A CD2   1 
ATOM   2617 N N     . ARG A 1 358 ? 23.647  -15.231 0.147   1.00 9.86  ? 338 ARG A N     1 
ATOM   2618 C CA    . ARG A 1 358 ? 24.712  -15.761 -0.673  1.00 9.46  ? 338 ARG A CA    1 
ATOM   2619 C C     . ARG A 1 358 ? 25.355  -14.659 -1.508  1.00 9.49  ? 338 ARG A C     1 
ATOM   2620 O O     . ARG A 1 358 ? 26.542  -14.513 -1.646  1.00 9.01  ? 338 ARG A O     1 
ATOM   2621 C CB    . ARG A 1 358 ? 24.172  -16.845 -1.602  1.00 10.01 ? 338 ARG A CB    1 
ATOM   2622 C CG    . ARG A 1 358 ? 25.242  -17.362 -2.546  1.00 10.66 ? 338 ARG A CG    1 
ATOM   2623 C CD    . ARG A 1 358 ? 24.588  -18.428 -3.354  1.00 12.27 ? 338 ARG A CD    1 
ATOM   2624 N NE    . ARG A 1 358 ? 25.622  -19.038 -4.149  1.00 13.60 ? 338 ARG A NE    1 
ATOM   2625 C CZ    . ARG A 1 358 ? 25.375  -19.960 -5.044  1.00 13.04 ? 338 ARG A CZ    1 
ATOM   2626 N NH1   . ARG A 1 358 ? 24.131  -20.279 -5.299  1.00 12.92 ? 338 ARG A NH1   1 
ATOM   2627 N NH2   . ARG A 1 358 ? 26.398  -20.420 -5.747  1.00 13.53 ? 338 ARG A NH2   1 
ATOM   2628 N N     . LEU A 1 359 ? 24.519  -13.865 -2.202  1.00 8.97  ? 339 LEU A N     1 
ATOM   2629 C CA    . LEU A 1 359 ? 25.097  -12.795 -2.981  1.00 8.62  ? 339 LEU A CA    1 
ATOM   2630 C C     . LEU A 1 359 ? 25.876  -11.785 -2.148  1.00 9.12  ? 339 LEU A C     1 
ATOM   2631 O O     . LEU A 1 359 ? 26.913  -11.365 -2.587  1.00 8.41  ? 339 LEU A O     1 
ATOM   2632 C CB    . LEU A 1 359 ? 23.965  -12.066 -3.732  1.00 8.28  ? 339 LEU A CB    1 
ATOM   2633 C CG    . LEU A 1 359 ? 23.329  -12.822 -4.902  1.00 7.63  ? 339 LEU A CG    1 
ATOM   2634 C CD1   . LEU A 1 359 ? 22.105  -12.057 -5.374  1.00 7.77  ? 339 LEU A CD1   1 
ATOM   2635 C CD2   . LEU A 1 359 ? 24.320  -13.018 -6.032  1.00 7.53  ? 339 LEU A CD2   1 
ATOM   2636 N N     . HIS A 1 360 ? 25.326  -11.433 -0.972  1.00 10.48 ? 340 HIS A N     1 
ATOM   2637 C CA    . HIS A 1 360 ? 25.962  -10.514 -0.048  1.00 11.14 ? 340 HIS A CA    1 
ATOM   2638 C C     . HIS A 1 360 ? 27.347  -11.046 0.340   1.00 10.68 ? 340 HIS A C     1 
ATOM   2639 O O     . HIS A 1 360 ? 28.295  -10.291 0.265   1.00 9.48  ? 340 HIS A O     1 
ATOM   2640 C CB    . HIS A 1 360 ? 25.019  -10.247 1.120   1.00 11.54 ? 340 HIS A CB    1 
ATOM   2641 C CG    . HIS A 1 360 ? 25.594  -9.332  2.148   1.00 13.11 ? 340 HIS A CG    1 
ATOM   2642 N ND1   . HIS A 1 360 ? 26.169  -8.115  1.845   1.00 12.87 ? 340 HIS A ND1   1 
ATOM   2643 C CD2   . HIS A 1 360 ? 25.716  -9.524  3.470   1.00 15.22 ? 340 HIS A CD2   1 
ATOM   2644 C CE1   . HIS A 1 360 ? 26.608  -7.577  2.992   1.00 13.67 ? 340 HIS A CE1   1 
ATOM   2645 N NE2   . HIS A 1 360 ? 26.306  -8.393  3.980   1.00 14.72 ? 340 HIS A NE2   1 
ATOM   2646 N N     . ASN A 1 361 ? 27.417  -12.314 0.739   1.00 11.58 ? 341 ASN A N     1 
ATOM   2647 C CA    . ASN A 1 361 ? 28.630  -12.861 1.358   1.00 11.50 ? 341 ASN A CA    1 
ATOM   2648 C C     . ASN A 1 361 ? 29.594  -13.434 0.325   1.00 12.89 ? 341 ASN A C     1 
ATOM   2649 O O     . ASN A 1 361 ? 30.793  -13.377 0.535   1.00 14.62 ? 341 ASN A O     1 
ATOM   2650 C CB    . ASN A 1 361 ? 28.300  -13.900 2.438   1.00 12.43 ? 341 ASN A CB    1 
ATOM   2651 C CG    . ASN A 1 361 ? 27.650  -13.236 3.626   1.00 12.31 ? 341 ASN A CG    1 
ATOM   2652 O OD1   . ASN A 1 361 ? 28.185  -12.240 4.094   1.00 14.08 ? 341 ASN A OD1   1 
ATOM   2653 N ND2   . ASN A 1 361 ? 26.544  -13.757 4.141   1.00 12.50 ? 341 ASN A ND2   1 
ATOM   2654 N N     . ASP A 1 362 ? 29.111  -13.890 -0.834  1.00 13.52 ? 342 ASP A N     1 
ATOM   2655 C CA    . ASP A 1 362 ? 29.901  -14.783 -1.683  1.00 11.78 ? 342 ASP A CA    1 
ATOM   2656 C C     . ASP A 1 362 ? 30.251  -14.121 -3.014  1.00 11.58 ? 342 ASP A C     1 
ATOM   2657 O O     . ASP A 1 362 ? 31.085  -14.652 -3.734  1.00 12.78 ? 342 ASP A O     1 
ATOM   2658 C CB    . ASP A 1 362 ? 29.164  -16.088 -1.969  1.00 12.72 ? 342 ASP A CB    1 
ATOM   2659 C CG    . ASP A 1 362 ? 28.699  -16.912 -0.769  1.00 12.91 ? 342 ASP A CG    1 
ATOM   2660 O OD1   . ASP A 1 362 ? 28.665  -16.379 0.369   1.00 13.85 ? 342 ASP A OD1   1 
ATOM   2661 O OD2   . ASP A 1 362 ? 28.170  -18.022 -0.998  1.00 14.29 ? 342 ASP A OD2   1 
ATOM   2662 N N     . TYR A 1 363 ? 29.586  -12.998 -3.377  1.00 11.02 ? 343 TYR A N     1 
ATOM   2663 C CA    . TYR A 1 363 ? 29.811  -12.337 -4.651  1.00 9.66  ? 343 TYR A CA    1 
ATOM   2664 C C     . TYR A 1 363 ? 29.970  -10.837 -4.447  1.00 10.77 ? 343 TYR A C     1 
ATOM   2665 O O     . TYR A 1 363 ? 29.608  -10.320 -3.384  1.00 10.50 ? 343 TYR A O     1 
ATOM   2666 C CB    . TYR A 1 363 ? 28.589  -12.570 -5.567  1.00 8.82  ? 343 TYR A CB    1 
ATOM   2667 C CG    . TYR A 1 363 ? 28.593  -13.957 -6.152  1.00 8.03  ? 343 TYR A CG    1 
ATOM   2668 C CD1   . TYR A 1 363 ? 29.388  -14.192 -7.264  1.00 8.25  ? 343 TYR A CD1   1 
ATOM   2669 C CD2   . TYR A 1 363 ? 27.902  -14.988 -5.570  1.00 8.44  ? 343 TYR A CD2   1 
ATOM   2670 C CE1   . TYR A 1 363 ? 29.451  -15.473 -7.836  1.00 8.02  ? 343 TYR A CE1   1 
ATOM   2671 C CE2   . TYR A 1 363 ? 27.979  -16.278 -6.107  1.00 9.59  ? 343 TYR A CE2   1 
ATOM   2672 C CZ    . TYR A 1 363 ? 28.730  -16.484 -7.254  1.00 9.36  ? 343 TYR A CZ    1 
ATOM   2673 O OH    . TYR A 1 363 ? 28.901  -17.721 -7.856  1.00 10.99 ? 343 TYR A OH    1 
ATOM   2674 N N     . PRO A 1 364 ? 30.518  -10.145 -5.459  1.00 11.01 ? 344 PRO A N     1 
ATOM   2675 C CA    . PRO A 1 364 ? 30.873  -8.728  -5.347  1.00 12.17 ? 344 PRO A CA    1 
ATOM   2676 C C     . PRO A 1 364 ? 29.833  -7.688  -5.785  1.00 11.93 ? 344 PRO A C     1 
ATOM   2677 O O     . PRO A 1 364 ? 30.091  -6.496  -5.706  1.00 14.12 ? 344 PRO A O     1 
ATOM   2678 C CB    . PRO A 1 364 ? 32.060  -8.646  -6.275  1.00 13.16 ? 344 PRO A CB    1 
ATOM   2679 C CG    . PRO A 1 364 ? 31.720  -9.621  -7.396  1.00 12.75 ? 344 PRO A CG    1 
ATOM   2680 C CD    . PRO A 1 364 ? 31.036  -10.760 -6.699  1.00 13.10 ? 344 PRO A CD    1 
ATOM   2681 N N     . PHE A 1 365 ? 28.665  -8.141  -6.223  1.00 10.72 ? 345 PHE A N     1 
ATOM   2682 C CA    . PHE A 1 365 ? 27.684  -7.222  -6.779  1.00 9.68  ? 345 PHE A CA    1 
ATOM   2683 C C     . PHE A 1 365 ? 26.985  -6.474  -5.664  1.00 8.32  ? 345 PHE A C     1 
ATOM   2684 O O     . PHE A 1 365 ? 26.479  -7.074  -4.741  1.00 9.44  ? 345 PHE A O     1 
ATOM   2685 C CB    . PHE A 1 365 ? 26.654  -8.011  -7.580  1.00 8.78  ? 345 PHE A CB    1 
ATOM   2686 C CG    . PHE A 1 365 ? 27.298  -8.924  -8.606  1.00 9.86  ? 345 PHE A CG    1 
ATOM   2687 C CD1   . PHE A 1 365 ? 27.871  -8.435  -9.782  1.00 10.15 ? 345 PHE A CD1   1 
ATOM   2688 C CD2   . PHE A 1 365 ? 27.290  -10.291 -8.388  1.00 9.02  ? 345 PHE A CD2   1 
ATOM   2689 C CE1   . PHE A 1 365 ? 28.468  -9.319  -10.685 1.00 10.48 ? 345 PHE A CE1   1 
ATOM   2690 C CE2   . PHE A 1 365 ? 27.845  -11.160 -9.312  1.00 8.93  ? 345 PHE A CE2   1 
ATOM   2691 C CZ    . PHE A 1 365 ? 28.442  -10.672 -10.430 1.00 9.13  ? 345 PHE A CZ    1 
ATOM   2692 N N     . ARG A 1 366 ? 26.845  -5.172  -5.880  1.00 9.14  ? 346 ARG A N     1 
ATOM   2693 C CA    . ARG A 1 366 ? 26.092  -4.346  -4.938  1.00 9.00  ? 346 ARG A CA    1 
ATOM   2694 C C     . ARG A 1 366 ? 25.986  -2.954  -5.539  1.00 7.34  ? 346 ARG A C     1 
ATOM   2695 O O     . ARG A 1 366 ? 26.855  -2.476  -6.259  1.00 8.81  ? 346 ARG A O     1 
ATOM   2696 C CB    . ARG A 1 366 ? 26.746  -4.232  -3.552  1.00 11.21 ? 346 ARG A CB    1 
ATOM   2697 C CG    . ARG A 1 366 ? 28.227  -3.924  -3.596  1.00 14.07 ? 346 ARG A CG    1 
ATOM   2698 C CD    . ARG A 1 366 ? 28.751  -4.063  -2.168  1.00 18.26 ? 346 ARG A CD    1 
ATOM   2699 N NE    . ARG A 1 366 ? 30.170  -3.795  -2.032  1.00 23.07 ? 346 ARG A NE    1 
ATOM   2700 C CZ    . ARG A 1 366 ? 31.153  -4.680  -2.213  1.00 25.79 ? 346 ARG A CZ    1 
ATOM   2701 N NH1   . ARG A 1 366 ? 32.405  -4.268  -2.081  1.00 29.64 ? 346 ARG A NH1   1 
ATOM   2702 N NH2   . ARG A 1 366 ? 30.902  -5.960  -2.488  1.00 23.31 ? 346 ARG A NH2   1 
ATOM   2703 N N     . PRO A 1 367 ? 24.881  -2.198  -5.305  1.00 6.91  ? 347 PRO A N     1 
ATOM   2704 C CA    . PRO A 1 367 ? 23.720  -2.693  -4.621  1.00 6.27  ? 347 PRO A CA    1 
ATOM   2705 C C     . PRO A 1 367 ? 22.920  -3.703  -5.463  1.00 5.84  ? 347 PRO A C     1 
ATOM   2706 O O     . PRO A 1 367 ? 23.236  -3.934  -6.643  1.00 5.62  ? 347 PRO A O     1 
ATOM   2707 C CB    . PRO A 1 367 ? 22.855  -1.433  -4.424  1.00 6.75  ? 347 PRO A CB    1 
ATOM   2708 C CG    . PRO A 1 367 ? 23.310  -0.498  -5.498  1.00 7.21  ? 347 PRO A CG    1 
ATOM   2709 C CD    . PRO A 1 367 ? 24.758  -0.814  -5.760  1.00 7.02  ? 347 PRO A CD    1 
ATOM   2710 N N     . LEU A 1 368 ? 21.909  -4.254  -4.812  1.00 5.62  ? 348 LEU A N     1 
ATOM   2711 C CA    . LEU A 1 368 ? 21.008  -5.248  -5.371  1.00 5.48  ? 348 LEU A CA    1 
ATOM   2712 C C     . LEU A 1 368 ? 19.621  -4.637  -5.462  1.00 5.41  ? 348 LEU A C     1 
ATOM   2713 O O     . LEU A 1 368 ? 19.174  -3.928  -4.570  1.00 5.30  ? 348 LEU A O     1 
ATOM   2714 C CB    . LEU A 1 368 ? 20.982  -6.522  -4.500  1.00 6.07  ? 348 LEU A CB    1 
ATOM   2715 C CG    . LEU A 1 368 ? 22.318  -7.226  -4.241  1.00 6.91  ? 348 LEU A CG    1 
ATOM   2716 C CD1   . LEU A 1 368 ? 22.111  -8.406  -3.324  1.00 7.73  ? 348 LEU A CD1   1 
ATOM   2717 C CD2   . LEU A 1 368 ? 22.954  -7.621  -5.568  1.00 7.42  ? 348 LEU A CD2   1 
ATOM   2718 N N     . TYR A 1 369 ? 18.880  -5.016  -6.512  1.00 4.52  ? 349 TYR A N     1 
ATOM   2719 C CA    . TYR A 1 369 ? 17.451  -4.784  -6.622  1.00 4.91  ? 349 TYR A CA    1 
ATOM   2720 C C     . TYR A 1 369 ? 16.717  -6.097  -6.815  1.00 4.50  ? 349 TYR A C     1 
ATOM   2721 O O     . TYR A 1 369 ? 17.216  -6.955  -7.546  1.00 5.32  ? 349 TYR A O     1 
ATOM   2722 C CB    . TYR A 1 369 ? 17.137  -3.876  -7.802  1.00 4.47  ? 349 TYR A CB    1 
ATOM   2723 C CG    . TYR A 1 369 ? 17.643  -2.478  -7.674  1.00 4.64  ? 349 TYR A CG    1 
ATOM   2724 C CD1   . TYR A 1 369 ? 18.939  -2.135  -7.979  1.00 5.13  ? 349 TYR A CD1   1 
ATOM   2725 C CD2   . TYR A 1 369 ? 16.810  -1.471  -7.232  1.00 4.81  ? 349 TYR A CD2   1 
ATOM   2726 C CE1   . TYR A 1 369 ? 19.407  -0.844  -7.854  1.00 5.67  ? 349 TYR A CE1   1 
ATOM   2727 C CE2   . TYR A 1 369 ? 17.253  -0.186  -7.128  1.00 5.33  ? 349 TYR A CE2   1 
ATOM   2728 C CZ    . TYR A 1 369 ? 18.543  0.155   -7.414  1.00 5.64  ? 349 TYR A CZ    1 
ATOM   2729 O OH    . TYR A 1 369 ? 19.038  1.460   -7.292  1.00 7.57  ? 349 TYR A OH    1 
ATOM   2730 N N     . ILE A 1 370 ? 15.577  -6.279  -6.213  1.00 4.18  ? 350 ILE A N     1 
ATOM   2731 C CA    . ILE A 1 370 ? 14.707  -7.381  -6.593  1.00 4.18  ? 350 ILE A CA    1 
ATOM   2732 C C     . ILE A 1 370 ? 13.891  -6.900  -7.793  1.00 3.82  ? 350 ILE A C     1 
ATOM   2733 O O     . ILE A 1 370 ? 13.015  -6.054  -7.636  1.00 4.17  ? 350 ILE A O     1 
ATOM   2734 C CB    . ILE A 1 370 ? 13.773  -7.864  -5.464  1.00 5.48  ? 350 ILE A CB    1 
ATOM   2735 C CG1   . ILE A 1 370 ? 14.578  -8.217  -4.209  1.00 6.45  ? 350 ILE A CG1   1 
ATOM   2736 C CG2   . ILE A 1 370 ? 12.913  -8.992  -5.897  1.00 5.75  ? 350 ILE A CG2   1 
ATOM   2737 C CD1   . ILE A 1 370 ? 15.717  -9.135  -4.467  1.00 7.42  ? 350 ILE A CD1   1 
ATOM   2738 N N     . THR A 1 371 ? 14.249  -7.318  -8.997  1.00 3.18  ? 351 THR A N     1 
ATOM   2739 C CA    . THR A 1 371 ? 13.651  -6.751  -10.197 1.00 3.02  ? 351 THR A CA    1 
ATOM   2740 C C     . THR A 1 371 ? 12.386  -7.487  -10.639 1.00 3.01  ? 351 THR A C     1 
ATOM   2741 O O     . THR A 1 371 ? 11.625  -6.913  -11.425 1.00 2.86  ? 351 THR A O     1 
ATOM   2742 C CB    . THR A 1 371 ? 14.703  -6.673  -11.295 1.00 3.01  ? 351 THR A CB    1 
ATOM   2743 O OG1   . THR A 1 371 ? 15.568  -7.828  -11.234 1.00 2.99  ? 351 THR A OG1   1 
ATOM   2744 C CG2   . THR A 1 371 ? 15.590  -5.467  -11.132 1.00 3.11  ? 351 THR A CG2   1 
ATOM   2745 N N     . GLN A 1 372 ? 12.111  -8.709  -10.161 1.00 2.87  ? 352 GLN A N     1 
ATOM   2746 C CA    . GLN A 1 372 ? 10.849  -9.411  -10.356 1.00 3.16  ? 352 GLN A CA    1 
ATOM   2747 C C     . GLN A 1 372 ? 10.656  -10.368 -9.180  1.00 3.15  ? 352 GLN A C     1 
ATOM   2748 O O     . GLN A 1 372 ? 11.530  -11.214 -8.949  1.00 3.39  ? 352 GLN A O     1 
ATOM   2749 C CB    . GLN A 1 372 ? 10.798  -10.241 -11.660 1.00 3.35  ? 352 GLN A CB    1 
ATOM   2750 C CG    . GLN A 1 372 ? 11.146  -9.437  -12.909 1.00 3.39  ? 352 GLN A CG    1 
ATOM   2751 C CD    . GLN A 1 372 ? 11.062  -10.073 -14.286 1.00 3.69  ? 352 GLN A CD    1 
ATOM   2752 O OE1   . GLN A 1 372 ? 11.535  -9.433  -15.218 1.00 4.57  ? 352 GLN A OE1   1 
ATOM   2753 N NE2   . GLN A 1 372 ? 10.599  -11.305 -14.411 1.00 4.08  ? 352 GLN A NE2   1 
ATOM   2754 N N     . ASN A 1 373 ? 9.479   -10.379 -8.589  1.00 3.50  ? 353 ASN A N     1 
ATOM   2755 C CA    . ASN A 1 373 ? 9.085   -11.362 -7.587  1.00 4.09  ? 353 ASN A CA    1 
ATOM   2756 C C     . ASN A 1 373 ? 7.568   -11.365 -7.601  1.00 3.97  ? 353 ASN A C     1 
ATOM   2757 O O     . ASN A 1 373 ? 6.937   -10.307 -7.497  1.00 3.92  ? 353 ASN A O     1 
ATOM   2758 C CB    . ASN A 1 373 ? 9.623   -10.983 -6.210  1.00 4.67  ? 353 ASN A CB    1 
ATOM   2759 C CG    . ASN A 1 373 ? 9.172   -11.874 -5.080  1.00 5.50  ? 353 ASN A CG    1 
ATOM   2760 O OD1   . ASN A 1 373 ? 8.569   -11.410 -4.115  1.00 6.09  ? 353 ASN A OD1   1 
ATOM   2761 N ND2   . ASN A 1 373 ? 9.409   -13.177 -5.184  1.00 6.90  ? 353 ASN A ND2   1 
ATOM   2762 N N     . GLY A 1 374 ? 6.902   -12.509 -7.811  1.00 4.64  ? 354 GLY A N     1 
ATOM   2763 C CA    . GLY A 1 374 ? 5.466   -12.591 -7.801  1.00 4.99  ? 354 GLY A CA    1 
ATOM   2764 C C     . GLY A 1 374 ? 5.016   -14.014 -8.099  1.00 5.35  ? 354 GLY A C     1 
ATOM   2765 O O     . GLY A 1 374 ? 5.858   -14.908 -8.124  1.00 6.08  ? 354 GLY A O     1 
ATOM   2766 N N     . CYS A 1 375 ? 3.742   -14.153 -8.321  1.00 5.20  ? 355 CYS A N     1 
ATOM   2767 C CA    . CYS A 1 375 ? 3.164   -15.490 -8.485  1.00 6.29  ? 355 CYS A CA    1 
ATOM   2768 C C     . CYS A 1 375 ? 1.903   -15.483 -9.343  1.00 6.15  ? 355 CYS A C     1 
ATOM   2769 O O     . CYS A 1 375 ? 1.213   -14.500 -9.505  1.00 6.00  ? 355 CYS A O     1 
ATOM   2770 C CB    . CYS A 1 375 ? 2.914   -16.167 -7.143  1.00 7.79  ? 355 CYS A CB    1 
ATOM   2771 S SG    . CYS A 1 375 ? 1.613   -15.397 -6.147  1.00 10.32 ? 355 CYS A SG    1 
ATOM   2772 N N     . ALA A 1 376 ? 1.578   -16.713 -9.827  1.00 7.14  ? 356 ALA A N     1 
ATOM   2773 C CA    . ALA A 1 376 ? 0.459   -16.964 -10.695 1.00 8.15  ? 356 ALA A CA    1 
ATOM   2774 C C     . ALA A 1 376 ? -0.611  -17.705 -9.899  1.00 9.15  ? 356 ALA A C     1 
ATOM   2775 O O     . ALA A 1 376 ? -0.260  -18.599 -9.126  1.00 11.19 ? 356 ALA A O     1 
ATOM   2776 C CB    . ALA A 1 376 ? 0.869   -17.770 -11.882 1.00 8.65  ? 356 ALA A CB    1 
ATOM   2777 N N     . LEU A 1 377 ? -1.844  -17.312 -10.105 1.00 10.09 ? 357 LEU A N     1 
ATOM   2778 C CA    . LEU A 1 377 ? -2.961  -17.953 -9.425  1.00 10.87 ? 357 LEU A CA    1 
ATOM   2779 C C     . LEU A 1 377 ? -4.070  -18.086 -10.444 1.00 11.90 ? 357 LEU A C     1 
ATOM   2780 O O     . LEU A 1 377 ? -4.090  -17.458 -11.488 1.00 11.25 ? 357 LEU A O     1 
ATOM   2781 C CB    . LEU A 1 377 ? -3.444  -17.125 -8.220  1.00 10.66 ? 357 LEU A CB    1 
ATOM   2782 C CG    . LEU A 1 377 ? -2.455  -16.961 -7.079  1.00 11.55 ? 357 LEU A CG    1 
ATOM   2783 C CD1   . LEU A 1 377 ? -3.014  -16.019 -6.050  1.00 12.16 ? 357 LEU A CD1   1 
ATOM   2784 C CD2   . LEU A 1 377 ? -2.157  -18.313 -6.423  1.00 12.67 ? 357 LEU A CD2   1 
ATOM   2785 N N     . HIS A 1 378 ? -5.095  -18.876 -10.079 1.00 12.11 ? 358 HIS A N     1 
ATOM   2786 C CA    . HIS A 1 378 ? -6.289  -18.993 -10.893 1.00 13.52 ? 358 HIS A CA    1 
ATOM   2787 C C     . HIS A 1 378 ? -7.232  -17.853 -10.561 1.00 13.58 ? 358 HIS A C     1 
ATOM   2788 O O     . HIS A 1 378 ? -8.303  -18.049 -9.969  1.00 16.16 ? 358 HIS A O     1 
ATOM   2789 C CB    . HIS A 1 378 ? -6.947  -20.358 -10.649 1.00 13.64 ? 358 HIS A CB    1 
ATOM   2790 C CG    . HIS A 1 378 ? -6.022  -21.494 -10.924 1.00 16.09 ? 358 HIS A CG    1 
ATOM   2791 N ND1   . HIS A 1 378 ? -5.514  -21.675 -12.205 1.00 17.35 ? 358 HIS A ND1   1 
ATOM   2792 C CD2   . HIS A 1 378 ? -5.459  -22.448 -10.138 1.00 16.68 ? 358 HIS A CD2   1 
ATOM   2793 C CE1   . HIS A 1 378 ? -4.725  -22.730 -12.197 1.00 17.44 ? 358 HIS A CE1   1 
ATOM   2794 N NE2   . HIS A 1 378 ? -4.643  -23.209 -10.949 1.00 18.05 ? 358 HIS A NE2   1 
ATOM   2795 N N     . ASP A 1 379 ? -6.778  -16.611 -10.836 1.00 12.42 ? 359 ASP A N     1 
ATOM   2796 C CA    . ASP A 1 379 ? -7.517  -15.444 -10.398 1.00 12.63 ? 359 ASP A CA    1 
ATOM   2797 C C     . ASP A 1 379 ? -8.850  -15.347 -11.107 1.00 12.80 ? 359 ASP A C     1 
ATOM   2798 O O     . ASP A 1 379 ? -8.967  -15.602 -12.306 1.00 14.87 ? 359 ASP A O     1 
ATOM   2799 C CB    . ASP A 1 379 ? -6.761  -14.136 -10.659 1.00 10.49 ? 359 ASP A CB    1 
ATOM   2800 C CG    . ASP A 1 379 ? -5.460  -14.077 -9.919  1.00 11.58 ? 359 ASP A CG    1 
ATOM   2801 O OD1   . ASP A 1 379 ? -5.490  -14.209 -8.675  1.00 11.95 ? 359 ASP A OD1   1 
ATOM   2802 O OD2   . ASP A 1 379 ? -4.396  -14.000 -10.570 1.00 10.58 ? 359 ASP A OD2   1 
ATOM   2803 N N     . GLU A 1 380 ? -9.881  -14.971 -10.353 1.00 15.22 ? 360 GLU A N     1 
ATOM   2804 C CA    . GLU A 1 380 ? -11.173 -14.766 -10.941 1.00 16.49 ? 360 GLU A CA    1 
ATOM   2805 C C     . GLU A 1 380 ? -11.778 -13.491 -10.352 1.00 14.12 ? 360 GLU A C     1 
ATOM   2806 O O     . GLU A 1 380 ? -11.537 -13.149 -9.199  1.00 14.02 ? 360 GLU A O     1 
ATOM   2807 C CB    . GLU A 1 380 ? -12.066 -16.007 -10.752 1.00 21.97 ? 360 GLU A CB    1 
ATOM   2808 C CG    . GLU A 1 380 ? -12.117 -16.583 -9.347  1.00 24.81 ? 360 GLU A CG    1 
ATOM   2809 C CD    . GLU A 1 380 ? -12.598 -18.036 -9.206  1.00 25.99 ? 360 GLU A CD    1 
ATOM   2810 O OE1   . GLU A 1 380 ? -13.353 -18.507 -10.083 1.00 25.09 ? 360 GLU A OE1   1 
ATOM   2811 O OE2   . GLU A 1 380 ? -12.142 -18.730 -8.239  1.00 19.24 ? 360 GLU A OE2   1 
ATOM   2812 N N     . ILE A 1 381 ? -12.554 -12.826 -11.176 1.00 12.57 ? 361 ILE A N     1 
ATOM   2813 C CA    . ILE A 1 381 ? -13.380 -11.728 -10.701 1.00 14.07 ? 361 ILE A CA    1 
ATOM   2814 C C     . ILE A 1 381 ? -14.528 -12.315 -9.885  1.00 14.37 ? 361 ILE A C     1 
ATOM   2815 O O     . ILE A 1 381 ? -15.291 -13.153 -10.384 1.00 17.10 ? 361 ILE A O     1 
ATOM   2816 C CB    . ILE A 1 381 ? -13.850 -10.817 -11.846 1.00 14.12 ? 361 ILE A CB    1 
ATOM   2817 C CG1   . ILE A 1 381 ? -12.661 -10.202 -12.599 1.00 16.25 ? 361 ILE A CG1   1 
ATOM   2818 C CG2   . ILE A 1 381 ? -14.779 -9.738  -11.288 1.00 15.12 ? 361 ILE A CG2   1 
ATOM   2819 C CD1   . ILE A 1 381 ? -13.003 -9.260  -13.732 1.00 17.66 ? 361 ILE A CD1   1 
ATOM   2820 N N     . ALA A 1 382 ? -14.642 -11.855 -8.643  1.00 14.58 ? 362 ALA A N     1 
ATOM   2821 C CA    . ALA A 1 382 ? -15.625 -12.373 -7.693  1.00 13.81 ? 362 ALA A CA    1 
ATOM   2822 C C     . ALA A 1 382 ? -16.964 -11.698 -7.916  1.00 15.17 ? 362 ALA A C     1 
ATOM   2823 O O     . ALA A 1 382 ? -17.118 -10.750 -8.662  1.00 14.76 ? 362 ALA A O     1 
ATOM   2824 C CB    . ALA A 1 382 ? -15.126 -12.144 -6.298  1.00 16.20 ? 362 ALA A CB    1 
ATOM   2825 N N     . GLU A 1 383 ? -17.968 -12.146 -7.167  1.00 13.32 ? 363 GLU A N     1 
ATOM   2826 C CA    . GLU A 1 383 ? -19.279 -11.557 -7.293  1.00 14.33 ? 363 GLU A CA    1 
ATOM   2827 C C     . GLU A 1 383 ? -19.284 -10.047 -7.013  1.00 13.75 ? 363 GLU A C     1 
ATOM   2828 O O     . GLU A 1 383 ? -20.049 -9.315  -7.626  1.00 14.48 ? 363 GLU A O     1 
ATOM   2829 C CB    . GLU A 1 383 ? -20.176 -12.349 -6.332  1.00 16.84 ? 363 GLU A CB    1 
ATOM   2830 C CG    . GLU A 1 383 ? -21.576 -11.828 -6.259  1.00 19.97 ? 363 GLU A CG    1 
ATOM   2831 C CD    . GLU A 1 383 ? -22.368 -12.061 -7.527  1.00 22.93 ? 363 GLU A CD    1 
ATOM   2832 O OE1   . GLU A 1 383 ? -21.888 -12.836 -8.410  1.00 24.76 ? 363 GLU A OE1   1 
ATOM   2833 O OE2   . GLU A 1 383 ? -23.469 -11.470 -7.631  1.00 28.98 ? 363 GLU A OE2   1 
ATOM   2834 N N     . ASP A 1 384 ? -18.489 -9.598  -6.044  1.00 12.95 ? 364 ASP A N     1 
ATOM   2835 C CA    . ASP A 1 384 ? -18.373 -8.194  -5.655  1.00 14.02 ? 364 ASP A CA    1 
ATOM   2836 C C     . ASP A 1 384 ? -17.590 -7.365  -6.677  1.00 13.71 ? 364 ASP A C     1 
ATOM   2837 O O     . ASP A 1 384 ? -17.620 -6.130  -6.609  1.00 15.44 ? 364 ASP A O     1 
ATOM   2838 C CB    . ASP A 1 384 ? -17.658 -8.035  -4.311  1.00 15.07 ? 364 ASP A CB    1 
ATOM   2839 C CG    . ASP A 1 384 ? -16.288 -8.698  -4.244  1.00 16.52 ? 364 ASP A CG    1 
ATOM   2840 O OD1   . ASP A 1 384 ? -16.213 -9.936  -3.966  1.00 15.27 ? 364 ASP A OD1   1 
ATOM   2841 O OD2   . ASP A 1 384 ? -15.276 -7.991  -4.404  1.00 15.86 ? 364 ASP A OD2   1 
ATOM   2842 N N     . GLY A 1 385 ? -16.853 -8.032  -7.565  1.00 13.12 ? 365 GLY A N     1 
ATOM   2843 C CA    . GLY A 1 385 ? -16.116 -7.363  -8.645  1.00 13.53 ? 365 GLY A CA    1 
ATOM   2844 C C     . GLY A 1 385 ? -14.614 -7.275  -8.380  1.00 13.78 ? 365 GLY A C     1 
ATOM   2845 O O     . GLY A 1 385 ? -13.834 -6.917  -9.283  1.00 14.15 ? 365 GLY A O     1 
ATOM   2846 N N     . GLY A 1 386 ? -14.166 -7.596  -7.169  1.00 11.67 ? 366 GLY A N     1 
ATOM   2847 C CA    . GLY A 1 386 ? -12.757 -7.648  -6.848  1.00 10.85 ? 366 GLY A CA    1 
ATOM   2848 C C     . GLY A 1 386 ? -12.146 -9.002  -7.174  1.00 11.32 ? 366 GLY A C     1 
ATOM   2849 O O     . GLY A 1 386 ? -12.845 -9.939  -7.591  1.00 13.17 ? 366 GLY A O     1 
ATOM   2850 N N     . ILE A 1 387 ? -10.846 -9.098  -6.957  1.00 8.22  ? 367 ILE A N     1 
ATOM   2851 C CA    . ILE A 1 387 ? -10.112 -10.326 -7.135  1.00 8.00  ? 367 ILE A CA    1 
ATOM   2852 C C     . ILE A 1 387 ? -9.498  -10.647 -5.790  1.00 8.79  ? 367 ILE A C     1 
ATOM   2853 O O     . ILE A 1 387 ? -8.608  -9.932  -5.324  1.00 8.12  ? 367 ILE A O     1 
ATOM   2854 C CB    . ILE A 1 387 ? -9.035  -10.231 -8.250  1.00 8.55  ? 367 ILE A CB    1 
ATOM   2855 C CG1   . ILE A 1 387 ? -9.640  -9.828  -9.585  1.00 8.58  ? 367 ILE A CG1   1 
ATOM   2856 C CG2   . ILE A 1 387 ? -8.295  -11.541 -8.350  1.00 9.42  ? 367 ILE A CG2   1 
ATOM   2857 C CD1   . ILE A 1 387 ? -9.912  -8.387  -9.858  1.00 9.00  ? 367 ILE A CD1   1 
ATOM   2858 N N     . HIS A 1 388 ? -9.991  -11.710 -5.111  1.00 9.03  ? 368 HIS A N     1 
ATOM   2859 C CA    . HIS A 1 388 ? -9.520  -12.024 -3.776  1.00 9.77  ? 368 HIS A CA    1 
ATOM   2860 C C     . HIS A 1 388 ? -8.339  -12.978 -3.824  1.00 9.90  ? 368 HIS A C     1 
ATOM   2861 O O     . HIS A 1 388 ? -8.456  -14.190 -3.525  1.00 11.65 ? 368 HIS A O     1 
ATOM   2862 C CB    . HIS A 1 388 ? -10.686 -12.579 -2.936  1.00 9.61  ? 368 HIS A CB    1 
ATOM   2863 C CG    . HIS A 1 388 ? -11.843 -11.628 -3.061  1.00 10.44 ? 368 HIS A CG    1 
ATOM   2864 N ND1   . HIS A 1 388 ? -11.722 -10.267 -2.834  1.00 10.24 ? 368 HIS A ND1   1 
ATOM   2865 C CD2   . HIS A 1 388 ? -13.107 -11.795 -3.446  1.00 10.65 ? 368 HIS A CD2   1 
ATOM   2866 C CE1   . HIS A 1 388 ? -12.853 -9.663  -3.123  1.00 9.21  ? 368 HIS A CE1   1 
ATOM   2867 N NE2   . HIS A 1 388 ? -13.743 -10.589 -3.484  1.00 11.30 ? 368 HIS A NE2   1 
ATOM   2868 N N     . ASP A 1 389 ? -7.159  -12.445 -4.162  1.00 9.77  ? 369 ASP A N     1 
ATOM   2869 C CA    . ASP A 1 389 ? -5.972  -13.261 -4.316  1.00 9.24  ? 369 ASP A CA    1 
ATOM   2870 C C     . ASP A 1 389 ? -5.130  -13.290 -3.054  1.00 9.10  ? 369 ASP A C     1 
ATOM   2871 O O     . ASP A 1 389 ? -3.965  -12.920 -2.969  1.00 8.59  ? 369 ASP A O     1 
ATOM   2872 C CB    . ASP A 1 389 ? -5.185  -12.744 -5.516  1.00 8.78  ? 369 ASP A CB    1 
ATOM   2873 C CG    . ASP A 1 389 ? -4.746  -11.290 -5.401  1.00 10.00 ? 369 ASP A CG    1 
ATOM   2874 O OD1   . ASP A 1 389 ? -5.399  -10.546 -4.621  1.00 8.87  ? 369 ASP A OD1   1 
ATOM   2875 O OD2   . ASP A 1 389 ? -3.734  -10.974 -6.069  1.00 9.21  ? 369 ASP A OD2   1 
ATOM   2876 N N     . GLY A 1 390 ? -5.736  -13.817 -1.964  1.00 8.56  ? 370 GLY A N     1 
ATOM   2877 C CA    . GLY A 1 390 ? -5.000  -13.824 -0.715  1.00 9.34  ? 370 GLY A CA    1 
ATOM   2878 C C     . GLY A 1 390 ? -3.675  -14.559 -0.692  1.00 8.28  ? 370 GLY A C     1 
ATOM   2879 O O     . GLY A 1 390 ? -2.751  -14.186 0.044   1.00 11.01 ? 370 GLY A O     1 
ATOM   2880 N N     . GLN A 1 391 ? -3.524  -15.613 -1.522  1.00 9.65  ? 371 GLN A N     1 
ATOM   2881 C CA    . GLN A 1 391 ? -2.285  -16.344 -1.547  1.00 10.28 ? 371 GLN A CA    1 
ATOM   2882 C C     . GLN A 1 391 ? -1.171  -15.445 -2.104  1.00 8.18  ? 371 GLN A C     1 
ATOM   2883 O O     . GLN A 1 391 ? -0.016  -15.537 -1.694  1.00 9.15  ? 371 GLN A O     1 
ATOM   2884 C CB    . GLN A 1 391 ? -2.401  -17.661 -2.328  1.00 11.69 ? 371 GLN A CB    1 
ATOM   2885 C CG    . GLN A 1 391 ? -1.167  -18.540 -2.153  1.00 13.73 ? 371 GLN A CG    1 
ATOM   2886 C CD    . GLN A 1 391 ? -1.269  -19.854 -2.896  1.00 12.61 ? 371 GLN A CD    1 
ATOM   2887 O OE1   . GLN A 1 391 ? -2.199  -20.078 -3.661  1.00 11.26 ? 371 GLN A OE1   1 
ATOM   2888 N NE2   . GLN A 1 391 ? -0.293  -20.721 -2.638  1.00 13.37 ? 371 GLN A NE2   1 
ATOM   2889 N N     . ARG A 1 392 ? -1.563  -14.575 -3.048  1.00 9.02  ? 372 ARG A N     1 
ATOM   2890 C CA    . ARG A 1 392 ? -0.604  -13.627 -3.624  1.00 8.45  ? 372 ARG A CA    1 
ATOM   2891 C C     . ARG A 1 392 ? -0.281  -12.514 -2.623  1.00 7.12  ? 372 ARG A C     1 
ATOM   2892 O O     . ARG A 1 392 ? 0.878   -12.170 -2.518  1.00 7.52  ? 372 ARG A O     1 
ATOM   2893 C CB    . ARG A 1 392 ? -1.099  -13.056 -4.954  1.00 8.19  ? 372 ARG A CB    1 
ATOM   2894 C CG    . ARG A 1 392 ? -0.137  -12.055 -5.575  1.00 7.84  ? 372 ARG A CG    1 
ATOM   2895 C CD    . ARG A 1 392 ? -0.561  -11.573 -6.957  1.00 7.71  ? 372 ARG A CD    1 
ATOM   2896 N NE    . ARG A 1 392 ? -0.615  -12.639 -7.974  1.00 7.59  ? 372 ARG A NE    1 
ATOM   2897 C CZ    . ARG A 1 392 ? -1.743  -13.136 -8.488  1.00 7.43  ? 372 ARG A CZ    1 
ATOM   2898 N NH1   . ARG A 1 392 ? -2.952  -12.769 -8.085  1.00 7.45  ? 372 ARG A NH1   1 
ATOM   2899 N NH2   . ARG A 1 392 ? -1.667  -13.980 -9.504  1.00 8.55  ? 372 ARG A NH2   1 
ATOM   2900 N N     A GLN A 1 393 ? -1.292  -12.026 -1.869  0.50 8.33  ? 373 GLN A N     1 
ATOM   2901 N N     B GLN A 1 393 ? -1.264  -12.018 -1.848  0.50 7.66  ? 373 GLN A N     1 
ATOM   2902 C CA    A GLN A 1 393 ? -1.052  -11.099 -0.772  0.50 9.06  ? 373 GLN A CA    1 
ATOM   2903 C CA    B GLN A 1 393 ? -0.909  -11.094 -0.786  0.50 7.83  ? 373 GLN A CA    1 
ATOM   2904 C C     A GLN A 1 393 ? -0.035  -11.714 0.202   0.50 8.67  ? 373 GLN A C     1 
ATOM   2905 C C     B GLN A 1 393 ? 0.068   -11.751 0.185   0.50 7.90  ? 373 GLN A C     1 
ATOM   2906 O O     A GLN A 1 393 ? 0.964   -11.092 0.572   0.50 8.67  ? 373 GLN A O     1 
ATOM   2907 O O     B GLN A 1 393 ? 1.100   -11.184 0.573   0.50 7.58  ? 373 GLN A O     1 
ATOM   2908 C CB    A GLN A 1 393 ? -2.411  -10.709 -0.177  0.50 10.50 ? 373 GLN A CB    1 
ATOM   2909 C CB    B GLN A 1 393 ? -2.139  -10.638 -0.023  0.50 8.06  ? 373 GLN A CB    1 
ATOM   2910 C CG    A GLN A 1 393 ? -2.350  -9.687  0.959   0.50 12.10 ? 373 GLN A CG    1 
ATOM   2911 C CG    B GLN A 1 393 ? -1.748  -9.753  1.148   0.50 8.25  ? 373 GLN A CG    1 
ATOM   2912 C CD    A GLN A 1 393 ? -1.962  -10.279 2.298   0.50 14.31 ? 373 GLN A CD    1 
ATOM   2913 C CD    B GLN A 1 393 ? -2.968  -9.392  1.942   0.50 8.38  ? 373 GLN A CD    1 
ATOM   2914 O OE1   A GLN A 1 393 ? -2.368  -11.385 2.651   0.50 15.09 ? 373 GLN A OE1   1 
ATOM   2915 O OE1   B GLN A 1 393 ? -2.973  -9.525  3.160   0.50 9.84  ? 373 GLN A OE1   1 
ATOM   2916 N NE2   A GLN A 1 393 ? -1.151  -9.552  3.058   0.50 16.73 ? 373 GLN A NE2   1 
ATOM   2917 N NE2   B GLN A 1 393 ? -3.989  -8.974  1.228   0.50 8.05  ? 373 GLN A NE2   1 
ATOM   2918 N N     . ALA A 1 394 ? -0.275  -12.982 0.605   1.00 9.58  ? 374 ALA A N     1 
ATOM   2919 C CA    . ALA A 1 394 ? 0.609   -13.697 1.510   1.00 10.04 ? 374 ALA A CA    1 
ATOM   2920 C C     . ALA A 1 394 ? 1.981   -13.954 0.913   1.00 7.92  ? 374 ALA A C     1 
ATOM   2921 O O     . ALA A 1 394 ? 3.012   -13.849 1.559   1.00 9.03  ? 374 ALA A O     1 
ATOM   2922 C CB    . ALA A 1 394 ? -0.025  -15.004 1.873   1.00 10.64 ? 374 ALA A CB    1 
ATOM   2923 N N     . PHE A 1 395 ? 2.010   -14.142 -0.423  1.00 7.61  ? 375 PHE A N     1 
ATOM   2924 C CA    . PHE A 1 395 ? 3.276   -14.271 -1.111  1.00 7.57  ? 375 PHE A CA    1 
ATOM   2925 C C     . PHE A 1 395 ? 4.125   -13.002 -0.959  1.00 7.15  ? 375 PHE A C     1 
ATOM   2926 O O     . PHE A 1 395 ? 5.278   -13.046 -0.584  1.00 8.02  ? 375 PHE A O     1 
ATOM   2927 C CB    . PHE A 1 395 ? 3.019   -14.620 -2.576  1.00 7.56  ? 375 PHE A CB    1 
ATOM   2928 C CG    . PHE A 1 395 ? 4.234   -14.923 -3.393  1.00 8.63  ? 375 PHE A CG    1 
ATOM   2929 C CD1   . PHE A 1 395 ? 5.042   -13.918 -3.922  1.00 8.29  ? 375 PHE A CD1   1 
ATOM   2930 C CD2   . PHE A 1 395 ? 4.539   -16.235 -3.687  1.00 9.66  ? 375 PHE A CD2   1 
ATOM   2931 C CE1   . PHE A 1 395 ? 6.142   -14.211 -4.691  1.00 9.72  ? 375 PHE A CE1   1 
ATOM   2932 C CE2   . PHE A 1 395 ? 5.632   -16.513 -4.473  1.00 9.60  ? 375 PHE A CE2   1 
ATOM   2933 C CZ    . PHE A 1 395 ? 6.427   -15.516 -4.968  1.00 9.17  ? 375 PHE A CZ    1 
ATOM   2934 N N     . PHE A 1 396 ? 3.501   -11.844 -1.217  1.00 7.12  ? 376 PHE A N     1 
ATOM   2935 C CA    . PHE A 1 396 ? 4.232   -10.606 -1.079  1.00 7.14  ? 376 PHE A CA    1 
ATOM   2936 C C     . PHE A 1 396 ? 4.628   -10.347 0.385   1.00 6.85  ? 376 PHE A C     1 
ATOM   2937 O O     . PHE A 1 396 ? 5.740   -9.933  0.652   1.00 7.85  ? 376 PHE A O     1 
ATOM   2938 C CB    . PHE A 1 396 ? 3.429   -9.411  -1.622  1.00 7.37  ? 376 PHE A CB    1 
ATOM   2939 C CG    . PHE A 1 396 ? 3.310   -9.424  -3.126  1.00 6.93  ? 376 PHE A CG    1 
ATOM   2940 C CD1   . PHE A 1 396 ? 4.450   -9.444  -3.908  1.00 7.06  ? 376 PHE A CD1   1 
ATOM   2941 C CD2   . PHE A 1 396 ? 2.084   -9.340  -3.724  1.00 7.55  ? 376 PHE A CD2   1 
ATOM   2942 C CE1   . PHE A 1 396 ? 4.344   -9.509  -5.296  1.00 7.40  ? 376 PHE A CE1   1 
ATOM   2943 C CE2   . PHE A 1 396 ? 1.975   -9.342  -5.100  1.00 8.57  ? 376 PHE A CE2   1 
ATOM   2944 C CZ    . PHE A 1 396 ? 3.107   -9.464  -5.871  1.00 6.96  ? 376 PHE A CZ    1 
ATOM   2945 N N     . GLU A 1 397 ? 3.687   -10.584 1.307   1.00 8.12  ? 377 GLU A N     1 
ATOM   2946 C CA    . GLU A 1 397 ? 3.984   -10.327 2.722   1.00 10.80 ? 377 GLU A CA    1 
ATOM   2947 C C     . GLU A 1 397 ? 5.189   -11.153 3.184   1.00 8.41  ? 377 GLU A C     1 
ATOM   2948 O O     . GLU A 1 397 ? 6.150   -10.657 3.764   1.00 10.86 ? 377 GLU A O     1 
ATOM   2949 C CB    . GLU A 1 397 ? 2.728   -10.614 3.535   1.00 14.12 ? 377 GLU A CB    1 
ATOM   2950 C CG    . GLU A 1 397 ? 2.727   -9.991  4.916   1.00 23.02 ? 377 GLU A CG    1 
ATOM   2951 C CD    . GLU A 1 397 ? 1.360   -9.862  5.574   1.00 28.13 ? 377 GLU A CD    1 
ATOM   2952 O OE1   . GLU A 1 397 ? 1.324   -9.332  6.710   1.00 44.36 ? 377 GLU A OE1   1 
ATOM   2953 O OE2   . GLU A 1 397 ? 0.335   -10.291 4.969   1.00 34.75 ? 377 GLU A OE2   1 
ATOM   2954 N N     . ALA A 1 398 ? 5.200   -12.445 2.795   1.00 8.85  ? 378 ALA A N     1 
ATOM   2955 C CA    . ALA A 1 398 ? 6.278   -13.304 3.225   1.00 8.80  ? 378 ALA A CA    1 
ATOM   2956 C C     . ALA A 1 398 ? 7.626   -12.996 2.584   1.00 8.57  ? 378 ALA A C     1 
ATOM   2957 O O     . ALA A 1 398 ? 8.683   -13.039 3.192   1.00 11.10 ? 378 ALA A O     1 
ATOM   2958 C CB    . ALA A 1 398 ? 5.868   -14.729 2.986   1.00 8.99  ? 378 ALA A CB    1 
ATOM   2959 N N     . HIS A 1 399 ? 7.620   -12.634 1.269   1.00 7.82  ? 379 HIS A N     1 
ATOM   2960 C CA    . HIS A 1 399 ? 8.855   -12.300 0.622   1.00 7.07  ? 379 HIS A CA    1 
ATOM   2961 C C     . HIS A 1 399 ? 9.427   -10.977 1.143   1.00 6.17  ? 379 HIS A C     1 
ATOM   2962 O O     . HIS A 1 399 ? 10.610  -10.842 1.289   1.00 6.89  ? 379 HIS A O     1 
ATOM   2963 C CB    . HIS A 1 399 ? 8.741   -12.419 -0.915  1.00 6.57  ? 379 HIS A CB    1 
ATOM   2964 C CG    . HIS A 1 399 ? 8.584   -13.833 -1.403  1.00 6.62  ? 379 HIS A CG    1 
ATOM   2965 N ND1   . HIS A 1 399 ? 7.394   -14.489 -1.354  1.00 7.09  ? 379 HIS A ND1   1 
ATOM   2966 C CD2   . HIS A 1 399 ? 9.502   -14.683 -1.899  1.00 6.68  ? 379 HIS A CD2   1 
ATOM   2967 C CE1   . HIS A 1 399 ? 7.593   -15.731 -1.856  1.00 7.27  ? 379 HIS A CE1   1 
ATOM   2968 N NE2   . HIS A 1 399 ? 8.844   -15.862 -2.184  1.00 6.76  ? 379 HIS A NE2   1 
ATOM   2969 N N     . LEU A 1 400 ? 8.539   -9.986  1.351   1.00 6.88  ? 380 LEU A N     1 
ATOM   2970 C CA    . LEU A 1 400 ? 9.023   -8.706  1.899   1.00 7.24  ? 380 LEU A CA    1 
ATOM   2971 C C     . LEU A 1 400 ? 9.538   -8.860  3.338   1.00 7.02  ? 380 LEU A C     1 
ATOM   2972 O O     . LEU A 1 400 ? 10.528  -8.233  3.669   1.00 8.30  ? 380 LEU A O     1 
ATOM   2973 C CB    . LEU A 1 400 ? 7.864   -7.708  1.802   1.00 7.20  ? 380 LEU A CB    1 
ATOM   2974 C CG    . LEU A 1 400 ? 7.545   -7.231  0.371   1.00 7.80  ? 380 LEU A CG    1 
ATOM   2975 C CD1   . LEU A 1 400 ? 6.331   -6.313  0.414   1.00 9.45  ? 380 LEU A CD1   1 
ATOM   2976 C CD2   . LEU A 1 400 ? 8.720   -6.469  -0.204  1.00 8.71  ? 380 LEU A CD2   1 
ATOM   2977 N N     . ALA A 1 401 ? 8.971   -9.825  4.067   1.00 8.91  ? 381 ALA A N     1 
ATOM   2978 C CA    . ALA A 1 401 ? 9.507   -10.114 5.398   1.00 9.77  ? 381 ALA A CA    1 
ATOM   2979 C C     . ALA A 1 401 ? 10.920  -10.673 5.301   1.00 10.54 ? 381 ALA A C     1 
ATOM   2980 O O     . ALA A 1 401 ? 11.832  -10.338 6.050   1.00 10.90 ? 381 ALA A O     1 
ATOM   2981 C CB    . ALA A 1 401 ? 8.589   -11.046 6.120   1.00 9.85  ? 381 ALA A CB    1 
ATOM   2982 N N     . GLN A 1 402 ? 11.179  -11.521 4.294   1.00 9.25  ? 382 GLN A N     1 
ATOM   2983 C CA    . GLN A 1 402 ? 12.515  -12.016 4.104   1.00 10.09 ? 382 GLN A CA    1 
ATOM   2984 C C     . GLN A 1 402 ? 13.462  -10.909 3.654   1.00 8.48  ? 382 GLN A C     1 
ATOM   2985 O O     . GLN A 1 402 ? 14.653  -10.892 3.910   1.00 8.93  ? 382 GLN A O     1 
ATOM   2986 C CB    . GLN A 1 402 ? 12.460  -13.208 3.134   1.00 10.81 ? 382 GLN A CB    1 
ATOM   2987 C CG    . GLN A 1 402 ? 11.657  -14.382 3.653   1.00 12.04 ? 382 GLN A CG    1 
ATOM   2988 C CD    . GLN A 1 402 ? 12.253  -14.998 4.893   1.00 13.19 ? 382 GLN A CD    1 
ATOM   2989 O OE1   . GLN A 1 402 ? 13.461  -15.053 5.041   1.00 15.34 ? 382 GLN A OE1   1 
ATOM   2990 N NE2   . GLN A 1 402 ? 11.383  -15.351 5.813   1.00 17.84 ? 382 GLN A NE2   1 
ATOM   2991 N N     . LEU A 1 403 ? 12.962  -9.915  2.857   1.00 7.79  ? 383 LEU A N     1 
ATOM   2992 C CA    . LEU A 1 403 ? 13.813  -8.818  2.471   1.00 8.59  ? 383 LEU A CA    1 
ATOM   2993 C C     . LEU A 1 403 ? 14.176  -7.930  3.678   1.00 7.75  ? 383 LEU A C     1 
ATOM   2994 O O     . LEU A 1 403 ? 15.272  -7.420  3.694   1.00 8.41  ? 383 LEU A O     1 
ATOM   2995 C CB    . LEU A 1 403 ? 13.085  -8.001  1.383   1.00 10.16 ? 383 LEU A CB    1 
ATOM   2996 C CG    . LEU A 1 403 ? 12.950  -8.707  0.031   1.00 12.09 ? 383 LEU A CG    1 
ATOM   2997 C CD1   . LEU A 1 403 ? 12.249  -7.772  -0.945  1.00 13.95 ? 383 LEU A CD1   1 
ATOM   2998 C CD2   . LEU A 1 403 ? 14.307  -9.094  -0.497  1.00 12.45 ? 383 LEU A CD2   1 
ATOM   2999 N N     A GLN A 1 404 ? 13.254  -7.744  4.618   0.50 8.21  ? 384 GLN A N     1 
ATOM   3000 N N     B GLN A 1 404 ? 13.213  -7.736  4.599   0.50 8.30  ? 384 GLN A N     1 
ATOM   3001 C CA    A GLN A 1 404 ? 13.613  -7.017  5.829   0.50 8.32  ? 384 GLN A CA    1 
ATOM   3002 C CA    B GLN A 1 404 ? 13.465  -7.078  5.885   0.50 8.53  ? 384 GLN A CA    1 
ATOM   3003 C C     A GLN A 1 404 ? 14.633  -7.792  6.658   0.50 8.21  ? 384 GLN A C     1 
ATOM   3004 C C     B GLN A 1 404 ? 14.660  -7.771  6.564   0.50 8.26  ? 384 GLN A C     1 
ATOM   3005 O O     A GLN A 1 404 ? 15.489  -7.178  7.258   0.50 8.59  ? 384 GLN A O     1 
ATOM   3006 O O     B GLN A 1 404 ? 15.691  -7.095  6.831   0.50 7.84  ? 384 GLN A O     1 
ATOM   3007 C CB    A GLN A 1 404 ? 12.413  -6.789  6.719   0.50 8.17  ? 384 GLN A CB    1 
ATOM   3008 C CB    B GLN A 1 404 ? 12.202  -7.095  6.753   0.50 8.78  ? 384 GLN A CB    1 
ATOM   3009 C CG    A GLN A 1 404 ? 11.628  -5.536  6.360   0.50 8.68  ? 384 GLN A CG    1 
ATOM   3010 C CG    B GLN A 1 404 ? 11.017  -6.276  6.203   0.50 9.21  ? 384 GLN A CG    1 
ATOM   3011 C CD    A GLN A 1 404 ? 12.336  -4.260  6.757   0.50 9.15  ? 384 GLN A CD    1 
ATOM   3012 C CD    B GLN A 1 404 ? 9.638   -6.623  6.736   0.50 9.97  ? 384 GLN A CD    1 
ATOM   3013 O OE1   A GLN A 1 404 ? 12.694  -4.030  7.908   0.50 7.70  ? 384 GLN A OE1   1 
ATOM   3014 O OE1   B GLN A 1 404 ? 9.451   -7.375  7.689   0.50 10.45 ? 384 GLN A OE1   1 
ATOM   3015 N NE2   A GLN A 1 404 ? 12.500  -3.372  5.798   0.50 10.23 ? 384 GLN A NE2   1 
ATOM   3016 N NE2   B GLN A 1 404 ? 8.615   -6.134  6.057   0.50 10.99 ? 384 GLN A NE2   1 
ATOM   3017 N N     . ARG A 1 405 ? 14.547  -9.119  6.682   1.00 8.71  ? 385 ARG A N     1 
ATOM   3018 C CA    . ARG A 1 405 ? 15.596  -9.926  7.344   1.00 9.63  ? 385 ARG A CA    1 
ATOM   3019 C C     . ARG A 1 405 ? 16.934  -9.742  6.643   1.00 8.69  ? 385 ARG A C     1 
ATOM   3020 O O     . ARG A 1 405 ? 18.015  -9.602  7.213   1.00 9.31  ? 385 ARG A O     1 
ATOM   3021 C CB    . ARG A 1 405 ? 15.226  -11.405 7.361   1.00 12.49 ? 385 ARG A CB    1 
ATOM   3022 C CG    . ARG A 1 405 ? 14.107  -11.809 8.321   1.00 18.63 ? 385 ARG A CG    1 
ATOM   3023 C CD    . ARG A 1 405 ? 13.891  -13.331 8.380   1.00 25.44 ? 385 ARG A CD    1 
ATOM   3024 N NE    . ARG A 1 405 ? 15.133  -14.070 8.673   1.00 30.25 ? 385 ARG A NE    1 
ATOM   3025 C CZ    . ARG A 1 405 ? 15.558  -15.212 8.109   1.00 33.58 ? 385 ARG A CZ    1 
ATOM   3026 N NH1   . ARG A 1 405 ? 14.795  -15.900 7.274   1.00 31.63 ? 385 ARG A NH1   1 
ATOM   3027 N NH2   . ARG A 1 405 ? 16.758  -15.684 8.409   1.00 33.09 ? 385 ARG A NH2   1 
ATOM   3028 N N     . ALA A 1 406 ? 16.894  -9.738  5.290   1.00 7.48  ? 386 ALA A N     1 
ATOM   3029 C CA    . ALA A 1 406 ? 18.099  -9.572  4.530   1.00 7.00  ? 386 ALA A CA    1 
ATOM   3030 C C     . ALA A 1 406 ? 18.732  -8.194  4.725   1.00 7.14  ? 386 ALA A C     1 
ATOM   3031 O O     . ALA A 1 406 ? 19.928  -8.021  4.927   1.00 7.86  ? 386 ALA A O     1 
ATOM   3032 C CB    . ALA A 1 406 ? 17.750  -9.913  3.064   1.00 7.31  ? 386 ALA A CB    1 
ATOM   3033 N N     . LEU A 1 407 ? 17.892  -7.139  4.718   1.00 7.37  ? 387 LEU A N     1 
ATOM   3034 C CA    . LEU A 1 407 ? 18.385  -5.806  5.012   1.00 7.80  ? 387 LEU A CA    1 
ATOM   3035 C C     . LEU A 1 407 ? 19.027  -5.780  6.420   1.00 6.88  ? 387 LEU A C     1 
ATOM   3036 O O     . LEU A 1 407 ? 20.050  -5.139  6.558   1.00 7.26  ? 387 LEU A O     1 
ATOM   3037 C CB    . LEU A 1 407 ? 17.215  -4.811  4.900   1.00 8.24  ? 387 LEU A CB    1 
ATOM   3038 C CG    . LEU A 1 407 ? 16.868  -4.419  3.455   1.00 8.20  ? 387 LEU A CG    1 
ATOM   3039 C CD1   . LEU A 1 407 ? 15.468  -3.835  3.396   1.00 9.00  ? 387 LEU A CD1   1 
ATOM   3040 C CD2   . LEU A 1 407 ? 17.881  -3.449  2.934   1.00 8.70  ? 387 LEU A CD2   1 
ATOM   3041 N N     . ALA A 1 408 ? 18.374  -6.421  7.371   1.00 7.07  ? 388 ALA A N     1 
ATOM   3042 C CA    . ALA A 1 408 ? 18.909  -6.460  8.753   1.00 7.07  ? 388 ALA A CA    1 
ATOM   3043 C C     . ALA A 1 408 ? 20.291  -7.145  8.801   1.00 8.60  ? 388 ALA A C     1 
ATOM   3044 O O     . ALA A 1 408 ? 21.171  -6.745  9.588   1.00 7.31  ? 388 ALA A O     1 
ATOM   3045 C CB    . ALA A 1 408 ? 17.941  -7.135  9.648   1.00 7.81  ? 388 ALA A CB    1 
ATOM   3046 N N     . ALA A 1 409 ? 20.550  -8.127  7.920   1.00 8.25  ? 389 ALA A N     1 
ATOM   3047 C CA    . ALA A 1 409 ? 21.847  -8.777  7.818   1.00 8.97  ? 389 ALA A CA    1 
ATOM   3048 C C     . ALA A 1 409 ? 22.898  -7.970  7.068   1.00 8.36  ? 389 ALA A C     1 
ATOM   3049 O O     . ALA A 1 409 ? 24.017  -8.456  6.887   1.00 11.84 ? 389 ALA A O     1 
ATOM   3050 C CB    . ALA A 1 409 ? 21.640  -10.135 7.155   1.00 8.56  ? 389 ALA A CB    1 
ATOM   3051 N N     . GLY A 1 410 ? 22.607  -6.758  6.538   1.00 8.17  ? 390 GLY A N     1 
ATOM   3052 C CA    . GLY A 1 410 ? 23.577  -5.941  5.858   1.00 8.35  ? 390 GLY A CA    1 
ATOM   3053 C C     . GLY A 1 410 ? 23.490  -6.010  4.312   1.00 7.43  ? 390 GLY A C     1 
ATOM   3054 O O     . GLY A 1 410 ? 24.314  -5.399  3.677   1.00 9.05  ? 390 GLY A O     1 
ATOM   3055 N N     . VAL A 1 411 ? 22.506  -6.731  3.784   1.00 8.23  ? 391 VAL A N     1 
ATOM   3056 C CA    . VAL A 1 411 ? 22.447  -6.843  2.315   1.00 8.24  ? 391 VAL A CA    1 
ATOM   3057 C C     . VAL A 1 411 ? 22.059  -5.482  1.756   1.00 8.49  ? 391 VAL A C     1 
ATOM   3058 O O     . VAL A 1 411 ? 21.047  -4.901  2.185   1.00 7.76  ? 391 VAL A O     1 
ATOM   3059 C CB    . VAL A 1 411 ? 21.461  -7.894  1.854   1.00 8.71  ? 391 VAL A CB    1 
ATOM   3060 C CG1   . VAL A 1 411 ? 21.377  -7.913  0.331   1.00 9.10  ? 391 VAL A CG1   1 
ATOM   3061 C CG2   . VAL A 1 411 ? 21.851  -9.271  2.388   1.00 8.64  ? 391 VAL A CG2   1 
ATOM   3062 N N     . PRO A 1 412 ? 22.804  -4.984  0.755   1.00 8.38  ? 392 PRO A N     1 
ATOM   3063 C CA    . PRO A 1 412 ? 22.566  -3.647  0.206   1.00 8.01  ? 392 PRO A CA    1 
ATOM   3064 C C     . PRO A 1 412 ? 21.457  -3.607  -0.841  1.00 6.93  ? 392 PRO A C     1 
ATOM   3065 O O     . PRO A 1 412 ? 21.766  -3.401  -2.027  1.00 8.00  ? 392 PRO A O     1 
ATOM   3066 C CB    . PRO A 1 412 ? 23.894  -3.255  -0.434  1.00 8.52  ? 392 PRO A CB    1 
ATOM   3067 C CG    . PRO A 1 412 ? 24.499  -4.578  -0.864  1.00 9.76  ? 392 PRO A CG    1 
ATOM   3068 C CD    . PRO A 1 412 ? 24.028  -5.571  0.171   1.00 9.22  ? 392 PRO A CD    1 
ATOM   3069 N N     A LEU A 1 413 ? 20.241  -3.815  -0.381  0.50 6.44  ? 393 LEU A N     1 
ATOM   3070 N N     B LEU A 1 413 ? 20.251  -3.902  -0.380  0.50 7.17  ? 393 LEU A N     1 
ATOM   3071 C CA    A LEU A 1 413 ? 19.093  -3.916  -1.259  0.50 5.95  ? 393 LEU A CA    1 
ATOM   3072 C CA    B LEU A 1 413 ? 19.079  -3.847  -1.230  0.50 7.17  ? 393 LEU A CA    1 
ATOM   3073 C C     A LEU A 1 413 ? 18.402  -2.558  -1.378  0.50 5.91  ? 393 LEU A C     1 
ATOM   3074 C C     B LEU A 1 413 ? 18.670  -2.385  -1.408  0.50 6.68  ? 393 LEU A C     1 
ATOM   3075 O O     A LEU A 1 413 ? 17.903  -2.054  -0.365  0.50 5.08  ? 393 LEU A O     1 
ATOM   3076 O O     B LEU A 1 413 ? 18.606  -1.579  -0.480  0.50 6.81  ? 393 LEU A O     1 
ATOM   3077 C CB    A LEU A 1 413 ? 18.148  -4.936  -0.645  0.50 5.97  ? 393 LEU A CB    1 
ATOM   3078 C CB    B LEU A 1 413 ? 17.960  -4.677  -0.604  0.50 8.01  ? 393 LEU A CB    1 
ATOM   3079 C CG    A LEU A 1 413 ? 16.866  -5.145  -1.425  0.50 6.00  ? 393 LEU A CG    1 
ATOM   3080 C CG    B LEU A 1 413 ? 18.227  -6.178  -0.555  0.50 9.03  ? 393 LEU A CG    1 
ATOM   3081 C CD1   A LEU A 1 413 ? 17.175  -5.901  -2.712  0.50 5.83  ? 393 LEU A CD1   1 
ATOM   3082 C CD1   B LEU A 1 413 ? 17.355  -6.862  0.493   0.50 9.65  ? 393 LEU A CD1   1 
ATOM   3083 C CD2   A LEU A 1 413 ? 15.840  -5.834  -0.564  0.50 6.18  ? 393 LEU A CD2   1 
ATOM   3084 C CD2   B LEU A 1 413 ? 17.979  -6.813  -1.915  0.50 9.53  ? 393 LEU A CD2   1 
ATOM   3085 N N     . LYS A 1 414 ? 18.277  -2.043  -2.634  1.00 5.93  ? 394 LYS A N     1 
ATOM   3086 C CA    . LYS A 1 414 ? 17.804  -0.685  -2.893  1.00 5.96  ? 394 LYS A CA    1 
ATOM   3087 C C     . LYS A 1 414 ? 16.420  -0.641  -3.535  1.00 5.17  ? 394 LYS A C     1 
ATOM   3088 O O     . LYS A 1 414 ? 15.881  0.458   -3.685  1.00 4.68  ? 394 LYS A O     1 
ATOM   3089 C CB    . LYS A 1 414 ? 18.824  0.079   -3.721  1.00 7.89  ? 394 LYS A CB    1 
ATOM   3090 C CG    . LYS A 1 414 ? 20.057  0.455   -2.900  1.00 10.06 ? 394 LYS A CG    1 
ATOM   3091 C CD    . LYS A 1 414 ? 20.900  1.471   -3.557  1.00 14.50 ? 394 LYS A CD    1 
ATOM   3092 C CE    . LYS A 1 414 ? 20.430  2.893   -3.378  1.00 19.14 ? 394 LYS A CE    1 
ATOM   3093 N NZ    . LYS A 1 414 ? 21.408  3.828   -3.986  1.00 24.85 ? 394 LYS A NZ    1 
ATOM   3094 N N     . GLY A 1 415 ? 15.816  -1.769  -3.845  1.00 4.47  ? 395 GLY A N     1 
ATOM   3095 C CA    . GLY A 1 415 ? 14.465  -1.674  -4.361  1.00 4.04  ? 395 GLY A CA    1 
ATOM   3096 C C     . GLY A 1 415 ? 13.804  -3.011  -4.601  1.00 3.82  ? 395 GLY A C     1 
ATOM   3097 O O     . GLY A 1 415 ? 14.461  -4.069  -4.572  1.00 3.90  ? 395 GLY A O     1 
ATOM   3098 N N     . TYR A 1 416 ? 12.521  -2.956  -4.909  1.00 3.31  ? 396 TYR A N     1 
ATOM   3099 C CA    . TYR A 1 416 ? 11.661  -4.111  -5.054  1.00 3.29  ? 396 TYR A CA    1 
ATOM   3100 C C     . TYR A 1 416 ? 10.654  -3.820  -6.146  1.00 3.11  ? 396 TYR A C     1 
ATOM   3101 O O     . TYR A 1 416 ? 9.909   -2.842  -6.035  1.00 3.50  ? 396 TYR A O     1 
ATOM   3102 C CB    . TYR A 1 416 ? 10.929  -4.475  -3.763  1.00 3.69  ? 396 TYR A CB    1 
ATOM   3103 C CG    . TYR A 1 416 ? 10.067  -5.689  -3.877  1.00 3.91  ? 396 TYR A CG    1 
ATOM   3104 C CD1   . TYR A 1 416 ? 10.601  -6.960  -3.730  1.00 4.15  ? 396 TYR A CD1   1 
ATOM   3105 C CD2   . TYR A 1 416 ? 8.722   -5.575  -4.164  1.00 4.20  ? 396 TYR A CD2   1 
ATOM   3106 C CE1   . TYR A 1 416 ? 9.769   -8.061  -3.788  1.00 4.08  ? 396 TYR A CE1   1 
ATOM   3107 C CE2   . TYR A 1 416 ? 7.889   -6.674  -4.236  1.00 4.15  ? 396 TYR A CE2   1 
ATOM   3108 C CZ    . TYR A 1 416 ? 8.422   -7.940  -4.052  1.00 4.38  ? 396 TYR A CZ    1 
ATOM   3109 O OH    . TYR A 1 416 ? 7.542   -8.968  -4.158  1.00 5.70  ? 396 TYR A OH    1 
ATOM   3110 N N     . PHE A 1 417 ? 10.566  -4.713  -7.130  1.00 2.83  ? 397 PHE A N     1 
ATOM   3111 C CA    . PHE A 1 417 ? 9.530   -4.621  -8.146  1.00 2.65  ? 397 PHE A CA    1 
ATOM   3112 C C     . PHE A 1 417 ? 8.679   -5.876  -8.160  1.00 2.75  ? 397 PHE A C     1 
ATOM   3113 O O     . PHE A 1 417 ? 9.173   -7.007  -8.384  1.00 3.19  ? 397 PHE A O     1 
ATOM   3114 C CB    . PHE A 1 417 ? 10.155  -4.505  -9.542  1.00 2.52  ? 397 PHE A CB    1 
ATOM   3115 C CG    . PHE A 1 417 ? 10.912  -3.237  -9.797  1.00 2.43  ? 397 PHE A CG    1 
ATOM   3116 C CD1   . PHE A 1 417 ? 12.191  -3.064  -9.327  1.00 2.65  ? 397 PHE A CD1   1 
ATOM   3117 C CD2   . PHE A 1 417 ? 10.290  -2.150  -10.362 1.00 2.40  ? 397 PHE A CD2   1 
ATOM   3118 C CE1   . PHE A 1 417 ? 12.890  -1.885  -9.535  1.00 2.61  ? 397 PHE A CE1   1 
ATOM   3119 C CE2   . PHE A 1 417 ? 10.984  -0.975  -10.570 1.00 2.51  ? 397 PHE A CE2   1 
ATOM   3120 C CZ    . PHE A 1 417 ? 12.280  -0.814  -10.147 1.00 2.55  ? 397 PHE A CZ    1 
ATOM   3121 N N     . ALA A 1 418 ? 7.394   -5.725  -7.944  1.00 2.80  ? 398 ALA A N     1 
ATOM   3122 C CA    . ALA A 1 418 ? 6.413   -6.782  -8.030  1.00 3.01  ? 398 ALA A CA    1 
ATOM   3123 C C     . ALA A 1 418 ? 6.265   -7.225  -9.474  1.00 3.36  ? 398 ALA A C     1 
ATOM   3124 O O     . ALA A 1 418 ? 6.113   -6.389  -10.374 1.00 3.29  ? 398 ALA A O     1 
ATOM   3125 C CB    . ALA A 1 418 ? 5.080   -6.336  -7.527  1.00 3.40  ? 398 ALA A CB    1 
ATOM   3126 N N     . TRP A 1 419 ? 6.356   -8.524  -9.662  1.00 3.57  ? 399 TRP A N     1 
ATOM   3127 C CA    . TRP A 1 419 ? 6.028   -9.150  -10.927 1.00 3.94  ? 399 TRP A CA    1 
ATOM   3128 C C     . TRP A 1 419 ? 4.602   -9.632  -10.885 1.00 3.92  ? 399 TRP A C     1 
ATOM   3129 O O     . TRP A 1 419 ? 4.301   -10.403 -9.964  1.00 4.50  ? 399 TRP A O     1 
ATOM   3130 C CB    . TRP A 1 419 ? 6.953   -10.338 -11.219 1.00 4.38  ? 399 TRP A CB    1 
ATOM   3131 C CG    . TRP A 1 419 ? 6.694   -10.817 -12.610 1.00 4.74  ? 399 TRP A CG    1 
ATOM   3132 C CD1   . TRP A 1 419 ? 5.942   -11.877 -13.009 1.00 5.58  ? 399 TRP A CD1   1 
ATOM   3133 C CD2   . TRP A 1 419 ? 7.054   -10.122 -13.814 1.00 4.68  ? 399 TRP A CD2   1 
ATOM   3134 N NE1   . TRP A 1 419 ? 5.823   -11.890 -14.375 1.00 6.08  ? 399 TRP A NE1   1 
ATOM   3135 C CE2   . TRP A 1 419 ? 6.527   -10.845 -14.899 1.00 4.82  ? 399 TRP A CE2   1 
ATOM   3136 C CE3   . TRP A 1 419 ? 7.813   -8.980  -14.056 1.00 4.20  ? 399 TRP A CE3   1 
ATOM   3137 C CZ2   . TRP A 1 419 ? 6.709   -10.464 -16.212 1.00 4.73  ? 399 TRP A CZ2   1 
ATOM   3138 C CZ3   . TRP A 1 419 ? 8.039   -8.633  -15.368 1.00 4.32  ? 399 TRP A CZ3   1 
ATOM   3139 C CH2   . TRP A 1 419 ? 7.475   -9.350  -16.405 1.00 3.92  ? 399 TRP A CH2   1 
ATOM   3140 N N     . SER A 1 420 ? 3.698   -9.264  -11.777 1.00 3.68  ? 400 SER A N     1 
ATOM   3141 C CA    . SER A 1 420 ? 3.801   -8.264  -12.842 1.00 3.57  ? 400 SER A CA    1 
ATOM   3142 C C     . SER A 1 420 ? 2.797   -7.175  -12.541 1.00 3.04  ? 400 SER A C     1 
ATOM   3143 O O     . SER A 1 420 ? 1.877   -7.365  -11.772 1.00 2.69  ? 400 SER A O     1 
ATOM   3144 C CB    . SER A 1 420 ? 3.502   -8.904  -14.185 1.00 4.36  ? 400 SER A CB    1 
ATOM   3145 O OG    . SER A 1 420 ? 3.571   -7.929  -15.232 1.00 5.39  ? 400 SER A OG    1 
ATOM   3146 N N     . LEU A 1 421 ? 2.941   -5.987  -13.131 1.00 2.55  ? 401 LEU A N     1 
ATOM   3147 C CA    . LEU A 1 421 ? 1.917   -4.975  -12.942 1.00 2.59  ? 401 LEU A CA    1 
ATOM   3148 C C     . LEU A 1 421 ? 0.546   -5.514  -13.321 1.00 2.86  ? 401 LEU A C     1 
ATOM   3149 O O     . LEU A 1 421 ? -0.423  -5.201  -12.625 1.00 3.17  ? 401 LEU A O     1 
ATOM   3150 C CB    . LEU A 1 421 ? 2.277   -3.748  -13.800 1.00 2.46  ? 401 LEU A CB    1 
ATOM   3151 C CG    . LEU A 1 421 ? 1.242   -2.614  -13.796 1.00 2.54  ? 401 LEU A CG    1 
ATOM   3152 C CD1   . LEU A 1 421 ? 1.100   -2.040  -12.404 1.00 2.65  ? 401 LEU A CD1   1 
ATOM   3153 C CD2   . LEU A 1 421 ? 1.626   -1.534  -14.810 1.00 2.71  ? 401 LEU A CD2   1 
ATOM   3154 N N     . LEU A 1 422 ? 0.444   -6.217  -14.446 1.00 3.12  ? 402 LEU A N     1 
ATOM   3155 C CA    . LEU A 1 422 ? -0.876  -6.691  -14.831 1.00 3.58  ? 402 LEU A CA    1 
ATOM   3156 C C     . LEU A 1 422 ? -0.739  -8.028  -15.513 1.00 3.18  ? 402 LEU A C     1 
ATOM   3157 O O     . LEU A 1 422 ? 0.332   -8.460  -15.859 1.00 3.50  ? 402 LEU A O     1 
ATOM   3158 C CB    . LEU A 1 422 ? -1.648  -5.675  -15.670 1.00 4.13  ? 402 LEU A CB    1 
ATOM   3159 C CG    . LEU A 1 422 ? -1.082  -5.424  -17.086 1.00 4.67  ? 402 LEU A CG    1 
ATOM   3160 C CD1   . LEU A 1 422 ? -1.998  -4.507  -17.906 1.00 5.25  ? 402 LEU A CD1   1 
ATOM   3161 C CD2   . LEU A 1 422 ? 0.300   -4.820  -17.132 1.00 5.53  ? 402 LEU A CD2   1 
ATOM   3162 N N     . ASP A 1 423 ? -1.860  -8.755  -15.546 1.00 3.10  ? 403 ASP A N     1 
ATOM   3163 C CA    . ASP A 1 423 ? -1.871  -10.058 -16.189 1.00 3.45  ? 403 ASP A CA    1 
ATOM   3164 C C     . ASP A 1 423 ? -1.488  -9.853  -17.656 1.00 3.19  ? 403 ASP A C     1 
ATOM   3165 O O     . ASP A 1 423 ? -1.901  -8.897  -18.283 1.00 3.08  ? 403 ASP A O     1 
ATOM   3166 C CB    . ASP A 1 423 ? -3.245  -10.708 -16.110 1.00 3.76  ? 403 ASP A CB    1 
ATOM   3167 C CG    . ASP A 1 423 ? -3.715  -10.988 -14.700 1.00 3.96  ? 403 ASP A CG    1 
ATOM   3168 O OD1   . ASP A 1 423 ? -2.883  -11.277 -13.861 1.00 4.37  ? 403 ASP A OD1   1 
ATOM   3169 O OD2   . ASP A 1 423 ? -4.957  -10.960 -14.555 1.00 4.65  ? 403 ASP A OD2   1 
ATOM   3170 N N     . ASN A 1 424 ? -0.752  -10.791 -18.223 1.00 3.15  ? 404 ASN A N     1 
ATOM   3171 C CA    . ASN A 1 424 ? -0.253  -10.559 -19.569 1.00 3.64  ? 404 ASN A CA    1 
ATOM   3172 C C     . ASN A 1 424 ? -0.080  -11.852 -20.350 1.00 3.31  ? 404 ASN A C     1 
ATOM   3173 O O     . ASN A 1 424 ? -0.534  -12.899 -19.928 1.00 3.16  ? 404 ASN A O     1 
ATOM   3174 C CB    . ASN A 1 424 ? 0.974   -9.679  -19.436 1.00 4.55  ? 404 ASN A CB    1 
ATOM   3175 C CG    . ASN A 1 424 ? 2.005   -10.409 -18.628 1.00 5.79  ? 404 ASN A CG    1 
ATOM   3176 O OD1   . ASN A 1 424 ? 2.385   -11.503 -18.957 1.00 5.74  ? 404 ASN A OD1   1 
ATOM   3177 N ND2   . ASN A 1 424 ? 2.459   -9.809  -17.566 1.00 8.57  ? 404 ASN A ND2   1 
ATOM   3178 N N     . PHE A 1 425 ? 0.554   -11.725 -21.515 1.00 2.74  ? 405 PHE A N     1 
ATOM   3179 C CA    . PHE A 1 425 ? 0.908   -12.888 -22.334 1.00 2.79  ? 405 PHE A CA    1 
ATOM   3180 C C     . PHE A 1 425 ? 2.099   -13.595 -21.690 1.00 2.92  ? 405 PHE A C     1 
ATOM   3181 O O     . PHE A 1 425 ? 3.232   -13.130 -21.807 1.00 2.80  ? 405 PHE A O     1 
ATOM   3182 C CB    . PHE A 1 425 ? 1.181   -12.446 -23.779 1.00 2.79  ? 405 PHE A CB    1 
ATOM   3183 C CG    . PHE A 1 425 ? 1.597   -13.594 -24.654 1.00 2.66  ? 405 PHE A CG    1 
ATOM   3184 C CD1   . PHE A 1 425 ? 0.633   -14.437 -25.187 1.00 2.82  ? 405 PHE A CD1   1 
ATOM   3185 C CD2   . PHE A 1 425 ? 2.935   -13.864 -24.946 1.00 2.87  ? 405 PHE A CD2   1 
ATOM   3186 C CE1   . PHE A 1 425 ? 1.012   -15.518 -25.955 1.00 2.83  ? 405 PHE A CE1   1 
ATOM   3187 C CE2   . PHE A 1 425 ? 3.292   -14.956 -25.729 1.00 2.76  ? 405 PHE A CE2   1 
ATOM   3188 C CZ    . PHE A 1 425 ? 2.308   -15.772 -26.219 1.00 2.88  ? 405 PHE A CZ    1 
ATOM   3189 N N     . GLU A 1 426 ? 1.867   -14.726 -21.023 1.00 2.97  ? 406 GLU A N     1 
ATOM   3190 C CA    . GLU A 1 426 ? 2.836   -15.421 -20.208 1.00 3.55  ? 406 GLU A CA    1 
ATOM   3191 C C     . GLU A 1 426 ? 3.545   -16.471 -21.070 1.00 3.11  ? 406 GLU A C     1 
ATOM   3192 O O     . GLU A 1 426 ? 3.559   -17.675 -20.792 1.00 3.25  ? 406 GLU A O     1 
ATOM   3193 C CB    . GLU A 1 426 ? 2.124   -16.036 -18.990 1.00 4.62  ? 406 GLU A CB    1 
ATOM   3194 C CG    . GLU A 1 426 ? 2.994   -16.811 -18.009 1.00 6.56  ? 406 GLU A CG    1 
ATOM   3195 C CD    . GLU A 1 426 ? 4.358   -16.252 -17.621 1.00 9.08  ? 406 GLU A CD    1 
ATOM   3196 O OE1   . GLU A 1 426 ? 4.440   -15.018 -17.468 1.00 7.10  ? 406 GLU A OE1   1 
ATOM   3197 O OE2   . GLU A 1 426 ? 5.348   -17.101 -17.360 1.00 13.17 ? 406 GLU A OE2   1 
ATOM   3198 N N     . TRP A 1 427 ? 4.175   -15.981 -22.130 1.00 2.73  ? 407 TRP A N     1 
ATOM   3199 C CA    . TRP A 1 427 ? 5.078   -16.781 -22.932 1.00 2.74  ? 407 TRP A CA    1 
ATOM   3200 C C     . TRP A 1 427 ? 4.383   -18.069 -23.368 1.00 2.78  ? 407 TRP A C     1 
ATOM   3201 O O     . TRP A 1 427 ? 3.323   -18.003 -23.994 1.00 2.40  ? 407 TRP A O     1 
ATOM   3202 C CB    . TRP A 1 427 ? 6.411   -16.971 -22.195 1.00 2.62  ? 407 TRP A CB    1 
ATOM   3203 C CG    . TRP A 1 427 ? 7.027   -15.685 -21.732 1.00 2.34  ? 407 TRP A CG    1 
ATOM   3204 C CD1   . TRP A 1 427 ? 7.353   -15.329 -20.441 1.00 2.30  ? 407 TRP A CD1   1 
ATOM   3205 C CD2   . TRP A 1 427 ? 7.486   -14.593 -22.580 1.00 2.12  ? 407 TRP A CD2   1 
ATOM   3206 N NE1   . TRP A 1 427 ? 7.889   -14.083 -20.437 1.00 2.19  ? 407 TRP A NE1   1 
ATOM   3207 C CE2   . TRP A 1 427 ? 8.002   -13.597 -21.707 1.00 2.09  ? 407 TRP A CE2   1 
ATOM   3208 C CE3   . TRP A 1 427 ? 7.489   -14.311 -23.964 1.00 2.15  ? 407 TRP A CE3   1 
ATOM   3209 C CZ2   . TRP A 1 427 ? 8.587   -12.434 -22.178 1.00 2.07  ? 407 TRP A CZ2   1 
ATOM   3210 C CZ3   . TRP A 1 427 ? 8.024   -13.120 -24.411 1.00 2.19  ? 407 TRP A CZ3   1 
ATOM   3211 C CH2   . TRP A 1 427 ? 8.567   -12.192 -23.522 1.00 2.09  ? 407 TRP A CH2   1 
ATOM   3212 N N     . ALA A 1 428 ? 5.013   -19.217 -23.166 1.00 3.15  ? 408 ALA A N     1 
ATOM   3213 C CA    . ALA A 1 428 ? 4.447   -20.475 -23.641 1.00 3.77  ? 408 ALA A CA    1 
ATOM   3214 C C     . ALA A 1 428 ? 3.133   -20.840 -22.981 1.00 4.10  ? 408 ALA A C     1 
ATOM   3215 O O     . ALA A 1 428 ? 2.442   -21.752 -23.487 1.00 3.81  ? 408 ALA A O     1 
ATOM   3216 C CB    . ALA A 1 428 ? 5.463   -21.585 -23.516 1.00 4.36  ? 408 ALA A CB    1 
ATOM   3217 N N     . MET A 1 429 ? 2.773   -20.187 -21.890 1.00 4.74  ? 409 MET A N     1 
ATOM   3218 C CA    A MET A 1 429 ? 1.485   -20.472 -21.261 0.50 5.51  ? 409 MET A CA    1 
ATOM   3219 C CA    B MET A 1 429 ? 1.498   -20.434 -21.221 0.50 5.22  ? 409 MET A CA    1 
ATOM   3220 C C     . MET A 1 429 ? 0.390   -19.557 -21.805 1.00 5.23  ? 409 MET A C     1 
ATOM   3221 O O     . MET A 1 429 ? -0.785  -19.691 -21.442 1.00 5.68  ? 409 MET A O     1 
ATOM   3222 C CB    A MET A 1 429 ? 1.540   -20.326 -19.738 0.50 7.19  ? 409 MET A CB    1 
ATOM   3223 C CB    B MET A 1 429 ? 1.621   -20.136 -19.721 0.50 6.34  ? 409 MET A CB    1 
ATOM   3224 C CG    A MET A 1 429 ? 2.192   -21.498 -19.052 0.50 8.90  ? 409 MET A CG    1 
ATOM   3225 C CG    B MET A 1 429 ? 2.785   -20.852 -19.089 0.50 7.30  ? 409 MET A CG    1 
ATOM   3226 S SD    A MET A 1 429 ? 1.789   -23.132 -19.703 0.50 13.80 ? 409 MET A SD    1 
ATOM   3227 S SD    B MET A 1 429 ? 2.658   -22.640 -19.203 0.50 10.52 ? 409 MET A SD    1 
ATOM   3228 C CE    A MET A 1 429 ? -0.003  -23.168 -19.672 0.50 13.58 ? 409 MET A CE    1 
ATOM   3229 C CE    B MET A 1 429 ? 1.066   -22.975 -18.464 0.50 11.61 ? 409 MET A CE    1 
ATOM   3230 N N     . GLY A 1 430 ? 0.725   -18.572 -22.636 1.00 4.68  ? 410 GLY A N     1 
ATOM   3231 C CA    . GLY A 1 430 ? -0.311  -17.739 -23.210 1.00 4.95  ? 410 GLY A CA    1 
ATOM   3232 C C     . GLY A 1 430 ? -0.964  -16.829 -22.188 1.00 5.62  ? 410 GLY A C     1 
ATOM   3233 O O     . GLY A 1 430 ? -0.379  -16.490 -21.167 1.00 5.23  ? 410 GLY A O     1 
ATOM   3234 N N     . LEU A 1 431 ? -2.202  -16.483 -22.483 1.00 6.98  ? 411 LEU A N     1 
ATOM   3235 C CA    . LEU A 1 431 ? -3.000  -15.618 -21.627 1.00 8.06  ? 411 LEU A CA    1 
ATOM   3236 C C     . LEU A 1 431 ? -3.543  -16.378 -20.425 1.00 8.78  ? 411 LEU A C     1 
ATOM   3237 O O     . LEU A 1 431 ? -4.101  -15.724 -19.511 1.00 11.57 ? 411 LEU A O     1 
ATOM   3238 C CB    . LEU A 1 431 ? -4.101  -14.993 -22.482 1.00 8.00  ? 411 LEU A CB    1 
ATOM   3239 C CG    . LEU A 1 431 ? -3.603  -14.114 -23.614 1.00 8.76  ? 411 LEU A CG    1 
ATOM   3240 C CD1   . LEU A 1 431 ? -4.800  -13.599 -24.436 1.00 9.03  ? 411 LEU A CD1   1 
ATOM   3241 C CD2   . LEU A 1 431 ? -2.736  -12.967 -23.113 1.00 9.24  ? 411 LEU A CD2   1 
ATOM   3242 N N     A SER A 1 432 ? -3.295  -17.697 -20.362 0.50 8.65  ? 412 SER A N     1 
ATOM   3243 N N     B SER A 1 432 ? -3.295  -17.694 -20.324 0.50 9.07  ? 412 SER A N     1 
ATOM   3244 C CA    A SER A 1 432 ? -3.938  -18.586 -19.416 0.50 8.71  ? 412 SER A CA    1 
ATOM   3245 C CA    B SER A 1 432 ? -3.964  -18.570 -19.376 0.50 9.55  ? 412 SER A CA    1 
ATOM   3246 C C     A SER A 1 432 ? -3.425  -18.393 -17.992 0.50 8.75  ? 412 SER A C     1 
ATOM   3247 C C     B SER A 1 432 ? -3.233  -18.701 -18.035 0.50 8.97  ? 412 SER A C     1 
ATOM   3248 O O     A SER A 1 432 ? -4.164  -18.662 -17.056 0.50 9.53  ? 412 SER A O     1 
ATOM   3249 O O     B SER A 1 432 ? -3.594  -19.516 -17.168 0.50 8.88  ? 412 SER A O     1 
ATOM   3250 C CB    A SER A 1 432 ? -3.869  -20.043 -19.842 0.50 8.10  ? 412 SER A CB    1 
ATOM   3251 C CB    B SER A 1 432 ? -4.166  -19.915 -19.993 0.50 9.45  ? 412 SER A CB    1 
ATOM   3252 O OG    A SER A 1 432 ? -2.577  -20.641 -19.699 0.50 7.96  ? 412 SER A OG    1 
ATOM   3253 O OG    B SER A 1 432 ? -5.121  -19.864 -21.048 0.50 11.25 ? 412 SER A OG    1 
ATOM   3254 N N     . MET A 1 433 ? -2.197  -17.882 -17.814 1.00 8.15  ? 413 MET A N     1 
ATOM   3255 C CA    . MET A 1 433 ? -1.484  -17.965 -16.567 1.00 7.95  ? 413 MET A CA    1 
ATOM   3256 C C     . MET A 1 433 ? -1.251  -16.532 -16.060 1.00 7.43  ? 413 MET A C     1 
ATOM   3257 O O     . MET A 1 433 ? -0.483  -15.773 -16.652 1.00 8.92  ? 413 MET A O     1 
ATOM   3258 C CB    . MET A 1 433 ? -0.148  -18.689 -16.798 1.00 9.55  ? 413 MET A CB    1 
ATOM   3259 C CG    . MET A 1 433 ? 0.614   -18.908 -15.564 1.00 10.93 ? 413 MET A CG    1 
ATOM   3260 S SD    . MET A 1 433 ? -0.172  -20.127 -14.471 1.00 15.59 ? 413 MET A SD    1 
ATOM   3261 C CE    . MET A 1 433 ? 0.095   -21.651 -15.382 1.00 16.30 ? 413 MET A CE    1 
ATOM   3262 N N     . ARG A 1 434 ? -1.937  -16.160 -14.966 1.00 6.40  ? 414 ARG A N     1 
ATOM   3263 C CA    . ARG A 1 434 ? -2.078  -14.773 -14.527 1.00 5.75  ? 414 ARG A CA    1 
ATOM   3264 C C     . ARG A 1 434 ? -1.136  -14.451 -13.385 1.00 5.31  ? 414 ARG A C     1 
ATOM   3265 O O     . ARG A 1 434 ? -1.279  -14.949 -12.267 1.00 5.50  ? 414 ARG A O     1 
ATOM   3266 C CB    . ARG A 1 434 ? -3.511  -14.522 -14.069 1.00 5.38  ? 414 ARG A CB    1 
ATOM   3267 C CG    . ARG A 1 434 ? -4.528  -14.519 -15.189 1.00 5.61  ? 414 ARG A CG    1 
ATOM   3268 C CD    . ARG A 1 434 ? -5.945  -14.283 -14.737 1.00 5.83  ? 414 ARG A CD    1 
ATOM   3269 N NE    . ARG A 1 434 ? -6.878  -14.321 -15.842 1.00 6.81  ? 414 ARG A NE    1 
ATOM   3270 C CZ    . ARG A 1 434 ? -7.158  -13.340 -16.678 1.00 6.66  ? 414 ARG A CZ    1 
ATOM   3271 N NH1   . ARG A 1 434 ? -6.668  -12.114 -16.471 1.00 6.45  ? 414 ARG A NH1   1 
ATOM   3272 N NH2   . ARG A 1 434 ? -7.974  -13.512 -17.704 1.00 8.96  ? 414 ARG A NH2   1 
ATOM   3273 N N     . TYR A 1 435 ? -0.127  -13.581 -13.663 1.00 4.32  ? 415 TYR A N     1 
ATOM   3274 C CA    . TYR A 1 435 ? 0.873   -13.131 -12.709 1.00 4.58  ? 415 TYR A CA    1 
ATOM   3275 C C     . TYR A 1 435 ? 0.651   -11.709 -12.179 1.00 4.25  ? 415 TYR A C     1 
ATOM   3276 O O     . TYR A 1 435 ? 1.478   -11.236 -11.414 1.00 4.14  ? 415 TYR A O     1 
ATOM   3277 C CB    . TYR A 1 435 ? 2.265   -13.198 -13.346 1.00 5.13  ? 415 TYR A CB    1 
ATOM   3278 C CG    . TYR A 1 435 ? 2.977   -14.520 -13.171 1.00 5.71  ? 415 TYR A CG    1 
ATOM   3279 C CD1   . TYR A 1 435 ? 3.781   -14.740 -12.056 1.00 6.06  ? 415 TYR A CD1   1 
ATOM   3280 C CD2   . TYR A 1 435 ? 2.932   -15.516 -14.131 1.00 6.47  ? 415 TYR A CD2   1 
ATOM   3281 C CE1   . TYR A 1 435 ? 4.449   -15.942 -11.885 1.00 6.74  ? 415 TYR A CE1   1 
ATOM   3282 C CE2   . TYR A 1 435 ? 3.586   -16.726 -13.972 1.00 6.55  ? 415 TYR A CE2   1 
ATOM   3283 C CZ    . TYR A 1 435 ? 4.316   -16.954 -12.817 1.00 6.70  ? 415 TYR A CZ    1 
ATOM   3284 O OH    . TYR A 1 435 ? 5.009   -18.138 -12.570 1.00 9.09  ? 415 TYR A OH    1 
ATOM   3285 N N     . GLY A 1 436 ? -0.390  -11.031 -12.620 1.00 3.82  ? 416 GLY A N     1 
ATOM   3286 C CA    . GLY A 1 436 ? -0.549  -9.607  -12.298 1.00 3.89  ? 416 GLY A CA    1 
ATOM   3287 C C     . GLY A 1 436 ? -0.877  -9.334  -10.833 1.00 4.52  ? 416 GLY A C     1 
ATOM   3288 O O     . GLY A 1 436 ? -1.582  -10.130 -10.199 1.00 4.90  ? 416 GLY A O     1 
ATOM   3289 N N     . ILE A 1 437 ? -0.543  -8.120  -10.378 1.00 4.41  ? 417 ILE A N     1 
ATOM   3290 C CA    . ILE A 1 437 ? -1.177  -7.514  -9.207  1.00 4.64  ? 417 ILE A CA    1 
ATOM   3291 C C     . ILE A 1 437 ? -2.443  -6.773  -9.613  1.00 4.48  ? 417 ILE A C     1 
ATOM   3292 O O     . ILE A 1 437 ? -3.249  -6.400  -8.739  1.00 5.02  ? 417 ILE A O     1 
ATOM   3293 C CB    . ILE A 1 437 ? -0.203  -6.696  -8.370  1.00 4.85  ? 417 ILE A CB    1 
ATOM   3294 C CG1   . ILE A 1 437 ? 0.283   -5.463  -9.144  1.00 4.85  ? 417 ILE A CG1   1 
ATOM   3295 C CG2   . ILE A 1 437 ? 0.928   -7.601  -7.936  1.00 5.19  ? 417 ILE A CG2   1 
ATOM   3296 C CD1   . ILE A 1 437 ? 1.248   -4.587  -8.378  1.00 5.17  ? 417 ILE A CD1   1 
ATOM   3297 N N     . CYS A 1 438 ? -2.635  -6.556  -10.922 1.00 4.30  ? 418 CYS A N     1 
ATOM   3298 C CA    . CYS A 1 438 ? -3.865  -6.086  -11.513 1.00 4.36  ? 418 CYS A CA    1 
ATOM   3299 C C     . CYS A 1 438 ? -4.341  -7.148  -12.525 1.00 4.42  ? 418 CYS A C     1 
ATOM   3300 O O     . CYS A 1 438 ? -3.546  -7.702  -13.289 1.00 4.84  ? 418 CYS A O     1 
ATOM   3301 C CB    . CYS A 1 438 ? -3.684  -4.749  -12.226 1.00 4.71  ? 418 CYS A CB    1 
ATOM   3302 S SG    . CYS A 1 438 ? -2.931  -3.441  -11.227 1.00 6.11  ? 418 CYS A SG    1 
ATOM   3303 N N     . TYR A 1 439 ? -5.658  -7.355  -12.547 1.00 4.49  ? 419 TYR A N     1 
ATOM   3304 C CA    . TYR A 1 439 ? -6.310  -8.284  -13.433 1.00 4.68  ? 419 TYR A CA    1 
ATOM   3305 C C     . TYR A 1 439 ? -6.519  -7.592  -14.775 1.00 4.82  ? 419 TYR A C     1 
ATOM   3306 O O     . TYR A 1 439 ? -7.023  -6.465  -14.854 1.00 5.53  ? 419 TYR A O     1 
ATOM   3307 C CB    . TYR A 1 439 ? -7.654  -8.682  -12.808 1.00 5.52  ? 419 TYR A CB    1 
ATOM   3308 C CG    . TYR A 1 439 ? -8.453  -9.721  -13.556 1.00 6.10  ? 419 TYR A CG    1 
ATOM   3309 C CD1   . TYR A 1 439 ? -9.241  -9.406  -14.648 1.00 6.50  ? 419 TYR A CD1   1 
ATOM   3310 C CD2   . TYR A 1 439 ? -8.315  -11.044 -13.201 1.00 7.01  ? 419 TYR A CD2   1 
ATOM   3311 C CE1   . TYR A 1 439 ? -9.934  -10.392 -15.338 1.00 7.92  ? 419 TYR A CE1   1 
ATOM   3312 C CE2   . TYR A 1 439 ? -8.982  -12.040 -13.897 1.00 7.63  ? 419 TYR A CE2   1 
ATOM   3313 C CZ    . TYR A 1 439 ? -9.819  -11.701 -14.924 1.00 7.64  ? 419 TYR A CZ    1 
ATOM   3314 O OH    . TYR A 1 439 ? -10.527 -12.693 -15.622 1.00 12.04 ? 419 TYR A OH    1 
ATOM   3315 N N     . THR A 1 440 ? -6.205  -8.318  -15.874 1.00 4.59  ? 420 THR A N     1 
ATOM   3316 C CA    . THR A 1 440 ? -6.469  -7.839  -17.206 1.00 4.41  ? 420 THR A CA    1 
ATOM   3317 C C     . THR A 1 440 ? -7.583  -8.660  -17.846 1.00 4.46  ? 420 THR A C     1 
ATOM   3318 O O     . THR A 1 440 ? -7.446  -9.883  -17.969 1.00 5.13  ? 420 THR A O     1 
ATOM   3319 C CB    . THR A 1 440 ? -5.242  -7.966  -18.125 1.00 4.66  ? 420 THR A CB    1 
ATOM   3320 O OG1   . THR A 1 440 ? -4.130  -7.383  -17.429 1.00 4.30  ? 420 THR A OG1   1 
ATOM   3321 C CG2   . THR A 1 440 ? -5.481  -7.287  -19.455 1.00 5.09  ? 420 THR A CG2   1 
ATOM   3322 N N     . ASN A 1 441 ? -8.654  -7.972  -18.216 1.00 4.70  ? 421 ASN A N     1 
ATOM   3323 C CA    . ASN A 1 441 ? -9.681  -8.608  -19.036 1.00 5.99  ? 421 ASN A CA    1 
ATOM   3324 C C     . ASN A 1 441 ? -9.182  -8.553  -20.471 1.00 6.15  ? 421 ASN A C     1 
ATOM   3325 O O     . ASN A 1 441 ? -9.047  -7.481  -21.059 1.00 5.57  ? 421 ASN A O     1 
ATOM   3326 C CB    . ASN A 1 441 ? -10.997 -7.879  -18.873 1.00 7.10  ? 421 ASN A CB    1 
ATOM   3327 C CG    . ASN A 1 441 ? -12.082 -8.541  -19.673 1.00 9.33  ? 421 ASN A CG    1 
ATOM   3328 O OD1   . ASN A 1 441 ? -11.908 -8.962  -20.827 1.00 10.04 ? 421 ASN A OD1   1 
ATOM   3329 N ND2   . ASN A 1 441 ? -13.263 -8.536  -19.062 1.00 12.35 ? 421 ASN A ND2   1 
ATOM   3330 N N     . PHE A 1 442 ? -8.740  -9.698  -21.019 1.00 6.63  ? 422 PHE A N     1 
ATOM   3331 C CA    . PHE A 1 442 ? -8.129  -9.670  -22.343 1.00 7.07  ? 422 PHE A CA    1 
ATOM   3332 C C     . PHE A 1 442 ? -9.099  -9.429  -23.494 1.00 8.77  ? 422 PHE A C     1 
ATOM   3333 O O     . PHE A 1 442 ? -8.675  -9.077  -24.587 1.00 9.47  ? 422 PHE A O     1 
ATOM   3334 C CB    . PHE A 1 442 ? -7.334  -10.948 -22.611 1.00 6.60  ? 422 PHE A CB    1 
ATOM   3335 C CG    . PHE A 1 442 ? -6.166  -11.090 -21.656 1.00 5.76  ? 422 PHE A CG    1 
ATOM   3336 C CD1   . PHE A 1 442 ? -5.110  -10.185 -21.704 1.00 5.74  ? 422 PHE A CD1   1 
ATOM   3337 C CD2   . PHE A 1 442 ? -6.093  -12.100 -20.706 1.00 5.65  ? 422 PHE A CD2   1 
ATOM   3338 C CE1   . PHE A 1 442 ? -4.056  -10.293 -20.815 1.00 5.62  ? 422 PHE A CE1   1 
ATOM   3339 C CE2   . PHE A 1 442 ? -5.065  -12.176 -19.789 1.00 5.84  ? 422 PHE A CE2   1 
ATOM   3340 C CZ    . PHE A 1 442 ? -4.005  -11.290 -19.890 1.00 5.76  ? 422 PHE A CZ    1 
ATOM   3341 N N     . GLU A 1 443 ? -10.408 -9.541  -23.239 1.00 9.54  ? 423 GLU A N     1 
ATOM   3342 C CA    . GLU A 1 443 ? -11.391 -9.209  -24.257 1.00 12.48 ? 423 GLU A CA    1 
ATOM   3343 C C     . GLU A 1 443 ? -11.678 -7.713  -24.318 1.00 10.81 ? 423 GLU A C     1 
ATOM   3344 O O     . GLU A 1 443 ? -11.745 -7.153  -25.399 1.00 13.27 ? 423 GLU A O     1 
ATOM   3345 C CB    . GLU A 1 443 ? -12.710 -9.934  -23.981 1.00 16.47 ? 423 GLU A CB    1 
ATOM   3346 C CG    . GLU A 1 443 ? -12.574 -11.453 -23.958 1.00 23.79 ? 423 GLU A CG    1 
ATOM   3347 C CD    . GLU A 1 443 ? -12.014 -12.083 -25.226 1.00 32.29 ? 423 GLU A CD    1 
ATOM   3348 O OE1   . GLU A 1 443 ? -12.745 -12.112 -26.250 1.00 42.41 ? 423 GLU A OE1   1 
ATOM   3349 O OE2   . GLU A 1 443 ? -10.844 -12.533 -25.200 1.00 41.29 ? 423 GLU A OE2   1 
ATOM   3350 N N     . THR A 1 444 ? -11.835 -7.070  -23.156 1.00 9.04  ? 424 THR A N     1 
ATOM   3351 C CA    . THR A 1 444 ? -12.200 -5.659  -23.132 1.00 8.39  ? 424 THR A CA    1 
ATOM   3352 C C     . THR A 1 444 ? -11.020 -4.728  -22.854 1.00 8.29  ? 424 THR A C     1 
ATOM   3353 O O     . THR A 1 444 ? -11.118 -3.511  -23.084 1.00 9.09  ? 424 THR A O     1 
ATOM   3354 C CB    . THR A 1 444 ? -13.208 -5.363  -22.028 1.00 8.94  ? 424 THR A CB    1 
ATOM   3355 O OG1   . THR A 1 444 ? -12.549 -5.588  -20.779 1.00 9.25  ? 424 THR A OG1   1 
ATOM   3356 C CG2   . THR A 1 444 ? -14.446 -6.234  -22.145 1.00 9.94  ? 424 THR A CG2   1 
ATOM   3357 N N     . LEU A 1 445 ? -9.933  -5.329  -22.385 1.00 7.46  ? 425 LEU A N     1 
ATOM   3358 C CA    . LEU A 1 445 ? -8.692  -4.646  -22.010 1.00 7.39  ? 425 LEU A CA    1 
ATOM   3359 C C     . LEU A 1 445 ? -8.845  -3.798  -20.759 1.00 6.96  ? 425 LEU A C     1 
ATOM   3360 O O     . LEU A 1 445 ? -7.950  -3.077  -20.347 1.00 6.75  ? 425 LEU A O     1 
ATOM   3361 C CB    . LEU A 1 445 ? -8.084  -3.867  -23.175 1.00 8.00  ? 425 LEU A CB    1 
ATOM   3362 C CG    . LEU A 1 445 ? -7.789  -4.775  -24.377 1.00 10.22 ? 425 LEU A CG    1 
ATOM   3363 C CD1   . LEU A 1 445 ? -7.623  -4.019  -25.661 1.00 12.12 ? 425 LEU A CD1   1 
ATOM   3364 C CD2   . LEU A 1 445 ? -6.592  -5.650  -24.064 1.00 9.64  ? 425 LEU A CD2   1 
ATOM   3365 N N     . GLU A 1 446 ? -9.929  -3.981  -20.030 1.00 6.82  ? 426 GLU A N     1 
ATOM   3366 C CA    . GLU A 1 446 ? -10.051 -3.367  -18.714 1.00 7.20  ? 426 GLU A CA    1 
ATOM   3367 C C     . GLU A 1 446 ? -9.055  -3.985  -17.744 1.00 6.12  ? 426 GLU A C     1 
ATOM   3368 O O     . GLU A 1 446 ? -8.836  -5.187  -17.731 1.00 7.27  ? 426 GLU A O     1 
ATOM   3369 C CB    . GLU A 1 446 ? -11.454 -3.653  -18.149 1.00 9.72  ? 426 GLU A CB    1 
ATOM   3370 C CG    . GLU A 1 446 ? -11.731 -3.022  -16.778 1.00 11.63 ? 426 GLU A CG    1 
ATOM   3371 C CD    . GLU A 1 446 ? -13.059 -3.358  -16.102 1.00 15.56 ? 426 GLU A CD    1 
ATOM   3372 O OE1   . GLU A 1 446 ? -13.799 -4.228  -16.605 1.00 18.26 ? 426 GLU A OE1   1 
ATOM   3373 O OE2   . GLU A 1 446 ? -13.327 -2.736  -15.053 1.00 16.26 ? 426 GLU A OE2   1 
ATOM   3374 N N     . ARG A 1 447 ? -8.457  -3.141  -16.900 1.00 6.00  ? 427 ARG A N     1 
ATOM   3375 C CA    . ARG A 1 447 ? -7.623  -3.558  -15.797 1.00 5.23  ? 427 ARG A CA    1 
ATOM   3376 C C     . ARG A 1 447 ? -8.342  -3.251  -14.491 1.00 5.42  ? 427 ARG A C     1 
ATOM   3377 O O     . ARG A 1 447 ? -9.008  -2.232  -14.391 1.00 6.39  ? 427 ARG A O     1 
ATOM   3378 C CB    . ARG A 1 447 ? -6.278  -2.827  -15.777 1.00 5.16  ? 427 ARG A CB    1 
ATOM   3379 C CG    . ARG A 1 447 ? -5.412  -2.994  -17.023 1.00 4.97  ? 427 ARG A CG    1 
ATOM   3380 C CD    . ARG A 1 447 ? -5.496  -1.849  -18.006 1.00 4.67  ? 427 ARG A CD    1 
ATOM   3381 N NE    . ARG A 1 447 ? -4.276  -1.666  -18.812 1.00 4.51  ? 427 ARG A NE    1 
ATOM   3382 C CZ    . ARG A 1 447 ? -4.057  -2.199  -20.003 1.00 4.37  ? 427 ARG A CZ    1 
ATOM   3383 N NH1   . ARG A 1 447 ? -4.992  -2.906  -20.642 1.00 4.99  ? 427 ARG A NH1   1 
ATOM   3384 N NH2   . ARG A 1 447 ? -2.853  -2.078  -20.546 1.00 3.80  ? 427 ARG A NH2   1 
ATOM   3385 N N     . ARG A 1 448 ? -8.143  -4.112  -13.503 1.00 5.92  ? 428 ARG A N     1 
ATOM   3386 C CA    . ARG A 1 448 ? -8.719  -3.927  -12.169 1.00 7.17  ? 428 ARG A CA    1 
ATOM   3387 C C     . ARG A 1 448 ? -7.684  -4.362  -11.150 1.00 6.12  ? 428 ARG A C     1 
ATOM   3388 O O     . ARG A 1 448 ? -7.123  -5.446  -11.248 1.00 6.82  ? 428 ARG A O     1 
ATOM   3389 C CB    . ARG A 1 448 ? -9.904  -4.883  -12.046 1.00 10.78 ? 428 ARG A CB    1 
ATOM   3390 C CG    . ARG A 1 448 ? -11.042 -4.388  -11.189 1.00 17.45 ? 428 ARG A CG    1 
ATOM   3391 C CD    . ARG A 1 448 ? -12.146 -5.381  -11.519 1.00 18.71 ? 428 ARG A CD    1 
ATOM   3392 N NE    . ARG A 1 448 ? -12.953 -5.071  -12.691 1.00 19.10 ? 428 ARG A NE    1 
ATOM   3393 C CZ    . ARG A 1 448 ? -14.249 -5.357  -12.775 1.00 19.68 ? 428 ARG A CZ    1 
ATOM   3394 N NH1   . ARG A 1 448 ? -14.785 -6.177  -11.879 1.00 17.33 ? 428 ARG A NH1   1 
ATOM   3395 N NH2   . ARG A 1 448 ? -14.977 -4.889  -13.766 1.00 22.31 ? 428 ARG A NH2   1 
ATOM   3396 N N     . ILE A 1 449 ? -7.432  -3.578  -10.095 1.00 5.57  ? 429 ILE A N     1 
ATOM   3397 C CA    . ILE A 1 449 ? -6.459  -3.905  -9.090  1.00 5.53  ? 429 ILE A CA    1 
ATOM   3398 C C     . ILE A 1 449 ? -6.952  -5.097  -8.268  1.00 5.45  ? 429 ILE A C     1 
ATOM   3399 O O     . ILE A 1 449 ? -8.096  -5.114  -7.814  1.00 6.71  ? 429 ILE A O     1 
ATOM   3400 C CB    . ILE A 1 449 ? -6.169  -2.649  -8.229  1.00 6.09  ? 429 ILE A CB    1 
ATOM   3401 C CG1   . ILE A 1 449 ? -5.566  -1.550  -9.106  1.00 6.44  ? 429 ILE A CG1   1 
ATOM   3402 C CG2   . ILE A 1 449 ? -5.256  -2.993  -7.089  1.00 6.27  ? 429 ILE A CG2   1 
ATOM   3403 C CD1   . ILE A 1 449 ? -5.416  -0.251  -8.387  1.00 6.79  ? 429 ILE A CD1   1 
ATOM   3404 N N     . LYS A 1 450 ? -6.078  -6.090  -8.106  1.00 5.01  ? 430 LYS A N     1 
ATOM   3405 C CA    . LYS A 1 450 ? -6.439  -7.241  -7.276  1.00 5.04  ? 430 LYS A CA    1 
ATOM   3406 C C     . LYS A 1 450 ? -6.218  -6.881  -5.803  1.00 5.08  ? 430 LYS A C     1 
ATOM   3407 O O     . LYS A 1 450 ? -5.496  -5.954  -5.432  1.00 5.57  ? 430 LYS A O     1 
ATOM   3408 C CB    . LYS A 1 450 ? -5.584  -8.437  -7.664  1.00 5.03  ? 430 LYS A CB    1 
ATOM   3409 C CG    . LYS A 1 450 ? -5.610  -8.856  -9.125  1.00 5.05  ? 430 LYS A CG    1 
ATOM   3410 C CD    . LYS A 1 450 ? -4.686  -10.018 -9.397  1.00 5.35  ? 430 LYS A CD    1 
ATOM   3411 C CE    . LYS A 1 450 ? -4.720  -10.369 -10.900 1.00 5.40  ? 430 LYS A CE    1 
ATOM   3412 N NZ    . LYS A 1 450 ? -3.727  -11.411 -11.270 1.00 5.79  ? 430 LYS A NZ    1 
ATOM   3413 N N     . ASP A 1 451 ? -6.748  -7.701  -4.874  1.00 5.33  ? 431 ASP A N     1 
ATOM   3414 C CA    . ASP A 1 451 ? -6.553  -7.379  -3.462  1.00 6.16  ? 431 ASP A CA    1 
ATOM   3415 C C     . ASP A 1 451 ? -5.090  -7.314  -3.061  1.00 6.12  ? 431 ASP A C     1 
ATOM   3416 O O     . ASP A 1 451 ? -4.717  -6.499  -2.194  1.00 8.27  ? 431 ASP A O     1 
ATOM   3417 C CB    . ASP A 1 451 ? -7.292  -8.403  -2.606  1.00 6.85  ? 431 ASP A CB    1 
ATOM   3418 C CG    . ASP A 1 451 ? -8.791  -8.272  -2.636  1.00 8.21  ? 431 ASP A CG    1 
ATOM   3419 O OD1   . ASP A 1 451 ? -9.339  -7.302  -3.140  1.00 9.33  ? 431 ASP A OD1   1 
ATOM   3420 O OD2   . ASP A 1 451 ? -9.476  -9.217  -2.068  1.00 10.43 ? 431 ASP A OD2   1 
ATOM   3421 N N     . SER A 1 452 ? -4.230  -8.135  -3.649  1.00 6.06  ? 432 SER A N     1 
ATOM   3422 C CA    . SER A 1 452 ? -2.825  -8.106  -3.357  1.00 6.02  ? 432 SER A CA    1 
ATOM   3423 C C     . SER A 1 452 ? -2.227  -6.734  -3.711  1.00 5.82  ? 432 SER A C     1 
ATOM   3424 O O     . SER A 1 452 ? -1.310  -6.264  -3.037  1.00 6.65  ? 432 SER A O     1 
ATOM   3425 C CB    . SER A 1 452 ? -2.125  -9.234  -4.031  1.00 6.93  ? 432 SER A CB    1 
ATOM   3426 O OG    . SER A 1 452 ? -2.226  -9.108  -5.445  1.00 7.26  ? 432 SER A OG    1 
ATOM   3427 N N     . GLY A 1 453 ? -2.695  -6.170  -4.813  1.00 5.30  ? 433 GLY A N     1 
ATOM   3428 C CA    . GLY A 1 453 ? -2.258  -4.827  -5.220  1.00 5.20  ? 433 GLY A CA    1 
ATOM   3429 C C     . GLY A 1 453 ? -2.634  -3.753  -4.201  1.00 5.18  ? 433 GLY A C     1 
ATOM   3430 O O     . GLY A 1 453 ? -1.825  -2.883  -3.898  1.00 4.52  ? 433 GLY A O     1 
ATOM   3431 N N     . TYR A 1 454 ? -3.833  -3.850  -3.638  1.00 5.13  ? 434 TYR A N     1 
ATOM   3432 C CA    . TYR A 1 454 ? -4.240  -2.912  -2.605  1.00 5.65  ? 434 TYR A CA    1 
ATOM   3433 C C     . TYR A 1 454 ? -3.435  -3.134  -1.326  1.00 5.62  ? 434 TYR A C     1 
ATOM   3434 O O     . TYR A 1 454 ? -3.105  -2.172  -0.635  1.00 5.77  ? 434 TYR A O     1 
ATOM   3435 C CB    . TYR A 1 454 ? -5.737  -2.967  -2.342  1.00 6.36  ? 434 TYR A CB    1 
ATOM   3436 C CG    . TYR A 1 454 ? -6.585  -2.395  -3.444  1.00 6.67  ? 434 TYR A CG    1 
ATOM   3437 C CD1   . TYR A 1 454 ? -6.461  -1.073  -3.792  1.00 7.35  ? 434 TYR A CD1   1 
ATOM   3438 C CD2   . TYR A 1 454 ? -7.509  -3.176  -4.126  1.00 7.48  ? 434 TYR A CD2   1 
ATOM   3439 C CE1   . TYR A 1 454 ? -7.238  -0.521  -4.800  1.00 7.89  ? 434 TYR A CE1   1 
ATOM   3440 C CE2   . TYR A 1 454 ? -8.275  -2.652  -5.141  1.00 7.70  ? 434 TYR A CE2   1 
ATOM   3441 C CZ    . TYR A 1 454 ? -8.186  -1.309  -5.428  1.00 8.54  ? 434 TYR A CZ    1 
ATOM   3442 O OH    . TYR A 1 454 ? -8.978  -0.819  -6.438  1.00 12.99 ? 434 TYR A OH    1 
ATOM   3443 N N     . TRP A 1 455 ? -3.053  -4.378  -1.038  1.00 5.75  ? 435 TRP A N     1 
ATOM   3444 C CA    . TRP A 1 455 ? -2.183  -4.620  0.098   1.00 6.01  ? 435 TRP A CA    1 
ATOM   3445 C C     . TRP A 1 455 ? -0.839  -3.946  -0.128  1.00 5.82  ? 435 TRP A C     1 
ATOM   3446 O O     . TRP A 1 455 ? -0.293  -3.282  0.761   1.00 5.58  ? 435 TRP A O     1 
ATOM   3447 C CB    . TRP A 1 455 ? -2.058  -6.126  0.388   1.00 7.03  ? 435 TRP A CB    1 
ATOM   3448 C CG    . TRP A 1 455 ? -1.241  -6.317  1.625   1.00 7.13  ? 435 TRP A CG    1 
ATOM   3449 C CD1   . TRP A 1 455 ? -1.695  -6.280  2.920   1.00 8.23  ? 435 TRP A CD1   1 
ATOM   3450 C CD2   . TRP A 1 455 ? 0.174   -6.442  1.690   1.00 7.46  ? 435 TRP A CD2   1 
ATOM   3451 N NE1   . TRP A 1 455 ? -0.639  -6.414  3.772   1.00 8.56  ? 435 TRP A NE1   1 
ATOM   3452 C CE2   . TRP A 1 455 ? 0.531   -6.437  3.064   1.00 8.13  ? 435 TRP A CE2   1 
ATOM   3453 C CE3   . TRP A 1 455 ? 1.192   -6.495  0.729   1.00 7.72  ? 435 TRP A CE3   1 
ATOM   3454 C CZ2   . TRP A 1 455 ? 1.849   -6.577  3.478   1.00 8.89  ? 435 TRP A CZ2   1 
ATOM   3455 C CZ3   . TRP A 1 455 ? 2.502   -6.588  1.141   1.00 8.43  ? 435 TRP A CZ3   1 
ATOM   3456 C CH2   . TRP A 1 455 ? 2.834   -6.623  2.503   1.00 9.72  ? 435 TRP A CH2   1 
ATOM   3457 N N     . LEU A 1 456 ? -0.250  -4.117  -1.342  1.00 5.26  ? 436 LEU A N     1 
ATOM   3458 C CA    . LEU A 1 456 ? 1.024   -3.490  -1.622  1.00 5.28  ? 436 LEU A CA    1 
ATOM   3459 C C     . LEU A 1 456 ? 0.872   -1.989  -1.484  1.00 4.71  ? 436 LEU A C     1 
ATOM   3460 O O     . LEU A 1 456 ? 1.727   -1.336  -0.926  1.00 4.12  ? 436 LEU A O     1 
ATOM   3461 C CB    . LEU A 1 456 ? 1.541   -3.845  -3.021  1.00 5.97  ? 436 LEU A CB    1 
ATOM   3462 C CG    . LEU A 1 456 ? 2.129   -5.247  -3.178  1.00 7.23  ? 436 LEU A CG    1 
ATOM   3463 C CD1   . LEU A 1 456 ? 2.288   -5.588  -4.667  1.00 7.48  ? 436 LEU A CD1   1 
ATOM   3464 C CD2   . LEU A 1 456 ? 3.446   -5.413  -2.467  1.00 8.12  ? 436 LEU A CD2   1 
ATOM   3465 N N     . ARG A 1 457 ? -0.197  -1.431  -2.039  1.00 4.27  ? 437 ARG A N     1 
ATOM   3466 C CA    . ARG A 1 457 ? -0.404  0.007   -1.952  1.00 4.43  ? 437 ARG A CA    1 
ATOM   3467 C C     . ARG A 1 457 ? -0.328  0.488   -0.511  1.00 4.73  ? 437 ARG A C     1 
ATOM   3468 O O     . ARG A 1 457 ? 0.353   1.463   -0.212  1.00 4.62  ? 437 ARG A O     1 
ATOM   3469 C CB    . ARG A 1 457 ? -1.750  0.385   -2.561  1.00 4.14  ? 437 ARG A CB    1 
ATOM   3470 C CG    . ARG A 1 457 ? -2.128  1.848   -2.419  1.00 4.30  ? 437 ARG A CG    1 
ATOM   3471 C CD    . ARG A 1 457 ? -3.585  2.172   -2.705  1.00 4.77  ? 437 ARG A CD    1 
ATOM   3472 N NE    . ARG A 1 457 ? -4.395  1.626   -1.627  1.00 5.55  ? 437 ARG A NE    1 
ATOM   3473 C CZ    . ARG A 1 457 ? -5.708  1.633   -1.620  1.00 5.40  ? 437 ARG A CZ    1 
ATOM   3474 N NH1   . ARG A 1 457 ? -6.401  2.234   -2.558  1.00 5.54  ? 437 ARG A NH1   1 
ATOM   3475 N NH2   . ARG A 1 457 ? -6.322  1.082   -0.566  1.00 6.30  ? 437 ARG A NH2   1 
ATOM   3476 N N     . ASP A 1 458 ? -1.042  -0.206  0.371   1.00 5.11  ? 438 ASP A N     1 
ATOM   3477 C CA    . ASP A 1 458 ? -1.121  0.288   1.731   1.00 5.68  ? 438 ASP A CA    1 
ATOM   3478 C C     . ASP A 1 458 ? 0.134   0.009   2.514   1.00 5.54  ? 438 ASP A C     1 
ATOM   3479 O O     . ASP A 1 458 ? 0.445   0.795   3.406   1.00 7.38  ? 438 ASP A O     1 
ATOM   3480 C CB    . ASP A 1 458 ? -2.387  -0.291  2.337   1.00 6.67  ? 438 ASP A CB    1 
ATOM   3481 C CG    . ASP A 1 458 ? -3.639  0.262   1.640   1.00 8.94  ? 438 ASP A CG    1 
ATOM   3482 O OD1   . ASP A 1 458 ? -3.597  1.373   1.036   1.00 10.80 ? 438 ASP A OD1   1 
ATOM   3483 O OD2   . ASP A 1 458 ? -4.674  -0.464  1.752   1.00 13.62 ? 438 ASP A OD2   1 
ATOM   3484 N N     . PHE A 1 459 ? 0.863   -1.056  2.163   1.00 5.81  ? 439 PHE A N     1 
ATOM   3485 C CA    . PHE A 1 459 ? 2.112   -1.363  2.812   1.00 5.97  ? 439 PHE A CA    1 
ATOM   3486 C C     . PHE A 1 459 ? 3.130   -0.294  2.450   1.00 6.43  ? 439 PHE A C     1 
ATOM   3487 O O     . PHE A 1 459 ? 3.847   0.233   3.318   1.00 7.98  ? 439 PHE A O     1 
ATOM   3488 C CB    . PHE A 1 459 ? 2.606   -2.759  2.424   1.00 7.13  ? 439 PHE A CB    1 
ATOM   3489 C CG    . PHE A 1 459 ? 3.921   -3.111  3.061   1.00 7.74  ? 439 PHE A CG    1 
ATOM   3490 C CD1   . PHE A 1 459 ? 3.950   -3.528  4.376   1.00 9.09  ? 439 PHE A CD1   1 
ATOM   3491 C CD2   . PHE A 1 459 ? 5.121   -2.939  2.409   1.00 8.16  ? 439 PHE A CD2   1 
ATOM   3492 C CE1   . PHE A 1 459 ? 5.157   -3.832  4.995   1.00 9.56  ? 439 PHE A CE1   1 
ATOM   3493 C CE2   . PHE A 1 459 ? 6.309   -3.241  3.023   1.00 8.93  ? 439 PHE A CE2   1 
ATOM   3494 C CZ    . PHE A 1 459 ? 6.329   -3.668  4.332   1.00 9.20  ? 439 PHE A CZ    1 
ATOM   3495 N N     . ILE A 1 460 ? 3.235   0.017   1.136   1.00 5.95  ? 440 ILE A N     1 
ATOM   3496 C CA    . ILE A 1 460 ? 4.141   1.044   0.664   1.00 6.59  ? 440 ILE A CA    1 
ATOM   3497 C C     . ILE A 1 460 ? 3.771   2.390   1.267   1.00 7.38  ? 440 ILE A C     1 
ATOM   3498 O O     . ILE A 1 460 ? 4.656   3.157   1.645   1.00 8.47  ? 440 ILE A O     1 
ATOM   3499 C CB    . ILE A 1 460 ? 4.128   1.076   -0.876  1.00 6.71  ? 440 ILE A CB    1 
ATOM   3500 C CG1   . ILE A 1 460 ? 4.708   -0.233  -1.399  1.00 7.34  ? 440 ILE A CG1   1 
ATOM   3501 C CG2   . ILE A 1 460 ? 4.887   2.283   -1.393  1.00 6.40  ? 440 ILE A CG2   1 
ATOM   3502 C CD1   . ILE A 1 460 ? 4.467   -0.484  -2.883  1.00 8.27  ? 440 ILE A CD1   1 
ATOM   3503 N N     . ALA A 1 461 ? 2.486   2.710   1.328   1.00 7.69  ? 441 ALA A N     1 
ATOM   3504 C CA    . ALA A 1 461 ? 2.076   4.015   1.852   1.00 9.46  ? 441 ALA A CA    1 
ATOM   3505 C C     . ALA A 1 461 ? 2.440   4.139   3.329   1.00 10.25 ? 441 ALA A C     1 
ATOM   3506 O O     . ALA A 1 461 ? 2.645   5.246   3.823   1.00 12.30 ? 441 ALA A O     1 
ATOM   3507 C CB    . ALA A 1 461 ? 0.594   4.183   1.625   1.00 9.59  ? 441 ALA A CB    1 
ATOM   3508 N N     . GLY A 1 462 ? 2.478   3.042   4.079   1.00 10.00 ? 442 GLY A N     1 
ATOM   3509 C CA    . GLY A 1 462 ? 2.879   3.104   5.482   1.00 11.38 ? 442 GLY A CA    1 
ATOM   3510 C C     . GLY A 1 462 ? 4.362   3.487   5.637   1.00 12.80 ? 442 GLY A C     1 
ATOM   3511 O O     . GLY A 1 462 ? 4.800   3.835   6.741   1.00 17.72 ? 442 GLY A O     1 
ATOM   3512 N N     . GLN A 1 463 ? 5.137   3.474   4.540   1.00 12.59 ? 443 GLN A N     1 
ATOM   3513 C CA    . GLN A 1 463 ? 6.550   3.816   4.608   1.00 12.27 ? 443 GLN A CA    1 
ATOM   3514 C C     . GLN A 1 463 ? 6.788   5.332   4.645   1.00 14.30 ? 443 GLN A C     1 
ATOM   3515 O O     . GLN A 1 463 ? 6.043   6.057   3.891   1.00 16.72 ? 443 GLN A O     1 
ATOM   3516 C CB    . GLN A 1 463 ? 7.336   3.225   3.429   1.00 12.82 ? 443 GLN A CB    1 
ATOM   3517 C CG    . GLN A 1 463 ? 7.220   1.732   3.246   1.00 12.88 ? 443 GLN A CG    1 
ATOM   3518 C CD    . GLN A 1 463 ? 7.727   0.910   4.393   1.00 14.35 ? 443 GLN A CD    1 
ATOM   3519 O OE1   . GLN A 1 463 ? 8.697   1.287   5.044   1.00 14.46 ? 443 GLN A OE1   1 
ATOM   3520 N NE2   . GLN A 1 463 ? 7.104   -0.221  4.633   1.00 13.88 ? 443 GLN A NE2   1 
HETATM 3521 C C1    . MLA B 2 .   ? -1.976  -28.614 -18.497 1.00 18.83 ? 501 MLA A C1    1 
HETATM 3522 O O1A   . MLA B 2 .   ? -1.611  -27.881 -17.575 1.00 20.60 ? 501 MLA A O1A   1 
HETATM 3523 O O1B   . MLA B 2 .   ? -3.103  -28.576 -18.974 1.00 13.64 ? 501 MLA A O1B   1 
HETATM 3524 C C2    . MLA B 2 .   ? -0.959  -29.590 -19.077 1.00 19.70 ? 501 MLA A C2    1 
HETATM 3525 C C3    . MLA B 2 .   ? 0.112   -28.925 -19.917 1.00 23.07 ? 501 MLA A C3    1 
HETATM 3526 O O3A   . MLA B 2 .   ? -0.241  -27.943 -20.594 1.00 29.21 ? 501 MLA A O3A   1 
HETATM 3527 O O3B   . MLA B 2 .   ? 1.308   -29.331 -19.797 1.00 21.29 ? 501 MLA A O3B   1 
HETATM 3528 C C2    . BGC C 3 .   ? 8.615   -13.172 -16.905 1.00 5.77  ? 502 BGC A C2    1 
HETATM 3529 C C3    . BGC C 3 .   ? 9.950   -13.894 -16.815 1.00 5.99  ? 502 BGC A C3    1 
HETATM 3530 C C4    . BGC C 3 .   ? 10.023  -14.790 -15.595 1.00 8.35  ? 502 BGC A C4    1 
HETATM 3531 C C5    . BGC C 3 .   ? 8.826   -15.648 -15.531 1.00 9.26  ? 502 BGC A C5    1 
HETATM 3532 C C6    . BGC C 3 .   ? 8.588   -16.544 -14.353 1.00 13.80 ? 502 BGC A C6    1 
HETATM 3533 C C1    . BGC C 3 .   ? 7.500   -14.149 -16.839 1.00 7.01  ? 502 BGC A C1    1 
HETATM 3534 O O1    . BGC C 3 .   ? 6.314   -13.539 -16.772 1.00 6.52  ? 502 BGC A O1    1 
HETATM 3535 O O2    . BGC C 3 .   ? 8.626   -12.483 -18.160 1.00 4.59  ? 502 BGC A O2    1 
HETATM 3536 O O3    . BGC C 3 .   ? 11.031  -12.944 -16.898 1.00 4.88  ? 502 BGC A O3    1 
HETATM 3537 O O4    . BGC C 3 .   ? 11.097  -15.742 -15.827 1.00 11.96 ? 502 BGC A O4    1 
HETATM 3538 O O5    . BGC C 3 .   ? 7.603   -14.820 -15.623 1.00 9.37  ? 502 BGC A O5    1 
HETATM 3539 O O6    . BGC C 3 .   ? 7.376   -17.300 -14.751 1.00 16.29 ? 502 BGC A O6    1 
HETATM 3540 C "C3'" . NHE D 4 .   ? 25.033  -26.477 -3.419  1.00 16.82 ? 503 NHE A "C3'" 1 
HETATM 3541 C "C2'" . NHE D 4 .   ? 23.983  -25.371 -3.412  1.00 15.61 ? 503 NHE A "C2'" 1 
HETATM 3542 C "C1'" . NHE D 4 .   ? 23.626  -24.970 -1.991  1.00 14.26 ? 503 NHE A "C1'" 1 
HETATM 3543 C "C6'" . NHE D 4 .   ? 23.171  -26.156 -1.145  1.00 14.00 ? 503 NHE A "C6'" 1 
HETATM 3544 N N     . NHE D 4 .   ? 22.577  -23.949 -2.117  1.00 12.32 ? 503 NHE A N     1 
HETATM 3545 C C1    . NHE D 4 .   ? 22.041  -23.478 -0.831  1.00 13.32 ? 503 NHE A C1    1 
HETATM 3546 C C2    . NHE D 4 .   ? 21.011  -22.398 -1.025  1.00 12.05 ? 503 NHE A C2    1 
HETATM 3547 S S     . NHE D 4 .   ? 21.705  -20.802 -1.409  1.00 11.59 ? 503 NHE A S     1 
HETATM 3548 O O1    . NHE D 4 .   ? 22.454  -20.976 -2.642  1.00 11.53 ? 503 NHE A O1    1 
HETATM 3549 O O2    . NHE D 4 .   ? 20.590  -19.879 -1.534  1.00 10.23 ? 503 NHE A O2    1 
HETATM 3550 O O3    . NHE D 4 .   ? 22.616  -20.510 -0.216  1.00 11.12 ? 503 NHE A O3    1 
HETATM 3551 C "C5'" . NHE D 4 .   ? 24.267  -27.218 -1.116  1.00 15.14 ? 503 NHE A "C5'" 1 
HETATM 3552 C "C4'" . NHE D 4 .   ? 24.642  -27.644 -2.524  1.00 16.85 ? 503 NHE A "C4'" 1 
HETATM 3553 O O     . HOH E 5 .   ? 8.517   -24.106 -8.221  1.00 22.79 ? 601 HOH A O     1 
HETATM 3554 O O     . HOH E 5 .   ? 4.204   7.095   2.956   1.00 26.07 ? 602 HOH A O     1 
HETATM 3555 O O     . HOH E 5 .   ? 1.200   -27.647 -22.431 1.00 18.48 ? 603 HOH A O     1 
HETATM 3556 O O     . HOH E 5 .   ? -4.310  -21.454 -15.981 1.00 23.80 ? 604 HOH A O     1 
HETATM 3557 O O     . HOH E 5 .   ? 29.936  10.178  -25.939 1.00 20.29 ? 605 HOH A O     1 
HETATM 3558 O O     . HOH E 5 .   ? -8.782  -16.380 -2.565  1.00 10.84 ? 606 HOH A O     1 
HETATM 3559 O O     . HOH E 5 .   ? 6.692   3.133   -32.142 1.00 17.12 ? 607 HOH A O     1 
HETATM 3560 O O     . HOH E 5 .   ? -3.321  5.697   -26.785 1.00 21.05 ? 608 HOH A O     1 
HETATM 3561 O O     . HOH E 5 .   ? 28.567  -0.705  -6.457  1.00 29.87 ? 609 HOH A O     1 
HETATM 3562 O O     . HOH E 5 .   ? -5.338  -20.338 -14.276 1.00 27.45 ? 610 HOH A O     1 
HETATM 3563 O O     . HOH E 5 .   ? 15.421  -19.228 -11.949 1.00 29.74 ? 611 HOH A O     1 
HETATM 3564 O O     . HOH E 5 .   ? 27.280  3.848   -9.159  1.00 24.74 ? 612 HOH A O     1 
HETATM 3565 O O     . HOH E 5 .   ? 34.385  -32.428 -25.026 1.00 23.60 ? 613 HOH A O     1 
HETATM 3566 O O     . HOH E 5 .   ? 15.980  -22.669 3.538   1.00 18.72 ? 614 HOH A O     1 
HETATM 3567 O O     . HOH E 5 .   ? -8.550  -0.555  -20.914 1.00 18.16 ? 615 HOH A O     1 
HETATM 3568 O O     . HOH E 5 .   ? -14.495 -5.062  -18.885 1.00 17.42 ? 616 HOH A O     1 
HETATM 3569 O O     . HOH E 5 .   ? 11.259  -7.676  10.070  1.00 26.42 ? 617 HOH A O     1 
HETATM 3570 O O     . HOH E 5 .   ? 28.331  -19.052 -3.306  1.00 21.15 ? 618 HOH A O     1 
HETATM 3571 O O     . HOH E 5 .   ? 31.695  -21.550 -9.115  1.00 11.60 ? 619 HOH A O     1 
HETATM 3572 O O     . HOH E 5 .   ? -2.895  -22.378 -4.549  1.00 10.74 ? 620 HOH A O     1 
HETATM 3573 O O     . HOH E 5 .   ? 27.346  -6.722  0.045   1.00 22.34 ? 621 HOH A O     1 
HETATM 3574 O O     . HOH E 5 .   ? 27.112  0.869   -7.710  1.00 19.87 ? 622 HOH A O     1 
HETATM 3575 O O     . HOH E 5 .   ? 3.532   -18.728 -9.372  1.00 11.24 ? 623 HOH A O     1 
HETATM 3576 O O     . HOH E 5 .   ? 29.679  -2.376  -33.697 1.00 32.49 ? 624 HOH A O     1 
HETATM 3577 O O     . HOH E 5 .   ? 14.904  -4.948  8.926   1.00 10.53 ? 625 HOH A O     1 
HETATM 3578 O O     . HOH E 5 .   ? 27.921  5.536   -13.356 1.00 21.01 ? 626 HOH A O     1 
HETATM 3579 O O     . HOH E 5 .   ? 20.332  -0.533  1.166   1.00 22.22 ? 627 HOH A O     1 
HETATM 3580 O O     . HOH E 5 .   ? -6.162  4.087   -23.141 1.00 19.40 ? 628 HOH A O     1 
HETATM 3581 O O     . HOH E 5 .   ? -6.196  0.692   -28.617 1.00 24.97 ? 629 HOH A O     1 
HETATM 3582 O O     . HOH E 5 .   ? 8.245   4.285   -38.713 1.00 23.27 ? 630 HOH A O     1 
HETATM 3583 O O     . HOH E 5 .   ? 19.038  -39.733 -5.345  1.00 23.25 ? 631 HOH A O     1 
HETATM 3584 O O     . HOH E 5 .   ? 29.896  -8.484  1.300   1.00 26.78 ? 632 HOH A O     1 
HETATM 3585 O O     . HOH E 5 .   ? 2.940   -11.605 -32.348 1.00 4.93  ? 633 HOH A O     1 
HETATM 3586 O O     . HOH E 5 .   ? 21.354  -41.676 -8.239  1.00 24.75 ? 634 HOH A O     1 
HETATM 3587 O O     . HOH E 5 .   ? 28.962  1.892   -9.371  1.00 23.31 ? 635 HOH A O     1 
HETATM 3588 O O     . HOH E 5 .   ? -9.726  -19.775 -8.388  1.00 17.53 ? 636 HOH A O     1 
HETATM 3589 O O     . HOH E 5 .   ? 10.973  -18.006 -17.173 1.00 28.13 ? 637 HOH A O     1 
HETATM 3590 O O     . HOH E 5 .   ? 25.558  -10.445 7.680   1.00 25.24 ? 638 HOH A O     1 
HETATM 3591 O O     . HOH E 5 .   ? 1.393   3.268   -1.833  1.00 13.39 ? 639 HOH A O     1 
HETATM 3592 O O     . HOH E 5 .   ? 4.105   0.444   8.387   1.00 22.14 ? 640 HOH A O     1 
HETATM 3593 O O     . HOH E 5 .   ? 20.309  -40.335 -2.578  1.00 25.95 ? 641 HOH A O     1 
HETATM 3594 O O     . HOH E 5 .   ? -1.030  2.444   4.855   1.00 20.74 ? 642 HOH A O     1 
HETATM 3595 O O     . HOH E 5 .   ? 7.372   15.531  -22.880 1.00 17.95 ? 643 HOH A O     1 
HETATM 3596 O O     . HOH E 5 .   ? 6.622   -19.409 -6.188  1.00 12.51 ? 644 HOH A O     1 
HETATM 3597 O O     . HOH E 5 .   ? 25.116  -21.276 -0.633  1.00 17.68 ? 645 HOH A O     1 
HETATM 3598 O O     . HOH E 5 .   ? 16.053  5.621   -13.997 1.00 4.95  ? 646 HOH A O     1 
HETATM 3599 O O     . HOH E 5 .   ? 21.437  -21.993 -32.626 1.00 19.08 ? 647 HOH A O     1 
HETATM 3600 O O     . HOH E 5 .   ? 29.714  -7.645  -13.710 1.00 12.53 ? 648 HOH A O     1 
HETATM 3601 O O     . HOH E 5 .   ? -3.814  -18.134 -14.051 1.00 24.96 ? 649 HOH A O     1 
HETATM 3602 O O     . HOH E 5 .   ? 24.844  -13.487 -37.360 1.00 16.07 ? 650 HOH A O     1 
HETATM 3603 O O     . HOH E 5 .   ? -2.767  -22.449 -17.746 1.00 18.82 ? 651 HOH A O     1 
HETATM 3604 O O     . HOH E 5 .   ? 15.882  -20.374 -35.709 1.00 18.60 ? 652 HOH A O     1 
HETATM 3605 O O     . HOH E 5 .   ? 13.552  12.214  -27.002 1.00 22.27 ? 653 HOH A O     1 
HETATM 3606 O O     . HOH E 5 .   ? 2.303   -11.701 -8.754  1.00 4.21  ? 654 HOH A O     1 
HETATM 3607 O O     . HOH E 5 .   ? 28.491  -15.981 -36.572 1.00 27.56 ? 655 HOH A O     1 
HETATM 3608 O O     . HOH E 5 .   ? -2.399  -26.450 -21.120 1.00 11.85 ? 656 HOH A O     1 
HETATM 3609 O O     . HOH E 5 .   ? 23.844  -38.115 -12.363 1.00 20.60 ? 657 HOH A O     1 
HETATM 3610 O O     . HOH E 5 .   ? 39.824  -29.186 -16.418 1.00 19.27 ? 658 HOH A O     1 
HETATM 3611 O O     . HOH E 5 .   ? 2.430   8.226   -9.697  1.00 20.06 ? 659 HOH A O     1 
HETATM 3612 O O     . HOH E 5 .   ? 19.620  -15.593 -16.025 1.00 4.28  ? 660 HOH A O     1 
HETATM 3613 O O     . HOH E 5 .   ? -11.678 -12.047 -17.957 1.00 22.24 ? 661 HOH A O     1 
HETATM 3614 O O     . HOH E 5 .   ? -1.820  -5.879  -33.149 1.00 13.75 ? 662 HOH A O     1 
HETATM 3615 O O     . HOH E 5 .   ? 8.398   -7.132  -28.639 1.00 6.36  ? 663 HOH A O     1 
HETATM 3616 O O     . HOH E 5 .   ? 29.480  -7.159  -16.447 1.00 6.12  ? 664 HOH A O     1 
HETATM 3617 O O     . HOH E 5 .   ? -0.489  -7.356  6.554   1.00 24.41 ? 665 HOH A O     1 
HETATM 3618 O O     . HOH E 5 .   ? -11.610 -13.632 -6.557  1.00 13.75 ? 666 HOH A O     1 
HETATM 3619 O O     . HOH E 5 .   ? 8.203   -21.864 3.711   1.00 22.19 ? 667 HOH A O     1 
HETATM 3620 O O     . HOH E 5 .   ? 31.099  -16.625 -29.390 1.00 18.07 ? 668 HOH A O     1 
HETATM 3621 O O     . HOH E 5 .   ? -6.766  -15.524 -6.699  1.00 13.14 ? 669 HOH A O     1 
HETATM 3622 O O     . HOH E 5 .   ? 6.220   8.874   -6.854  1.00 22.97 ? 670 HOH A O     1 
HETATM 3623 O O     . HOH E 5 .   ? 21.153  -3.521  4.704   1.00 15.07 ? 671 HOH A O     1 
HETATM 3624 O O     . HOH E 5 .   ? 2.838   -7.825  -27.511 1.00 1.09  ? 672 HOH A O     1 
HETATM 3625 O O     . HOH E 5 .   ? 16.495  -30.546 -25.216 1.00 23.99 ? 673 HOH A O     1 
HETATM 3626 O O     . HOH E 5 .   ? 17.988  -32.652 -15.569 1.00 25.01 ? 674 HOH A O     1 
HETATM 3627 O O     . HOH E 5 .   ? -10.833 -17.387 -6.288  1.00 22.74 ? 675 HOH A O     1 
HETATM 3628 O O     . HOH E 5 .   ? 23.820  10.843  -13.935 1.00 21.24 ? 676 HOH A O     1 
HETATM 3629 O O     . HOH E 5 .   ? 32.829  -16.515 -2.825  1.00 26.55 ? 677 HOH A O     1 
HETATM 3630 O O     . HOH E 5 .   ? 8.368   -15.075 -38.821 1.00 14.91 ? 678 HOH A O     1 
HETATM 3631 O O     . HOH E 5 .   ? 3.164   -0.022  -19.760 1.00 4.20  ? 679 HOH A O     1 
HETATM 3632 O O     . HOH E 5 .   ? -6.588  -18.351 -22.879 1.00 21.74 ? 680 HOH A O     1 
HETATM 3633 O O     . HOH E 5 .   ? -3.001  -11.028 -28.050 1.00 5.26  ? 681 HOH A O     1 
HETATM 3634 O O     . HOH E 5 .   ? 21.837  -22.643 -4.690  1.00 10.17 ? 682 HOH A O     1 
HETATM 3635 O O     . HOH E 5 .   ? 28.903  3.839   -27.969 1.00 12.49 ? 683 HOH A O     1 
HETATM 3636 O O     . HOH E 5 .   ? 4.521   -27.344 -32.331 1.00 21.21 ? 684 HOH A O     1 
HETATM 3637 O O     . HOH E 5 .   ? -3.667  -14.026 -31.536 1.00 22.94 ? 685 HOH A O     1 
HETATM 3638 O O     . HOH E 5 .   ? 11.862  4.742   6.175   1.00 20.18 ? 686 HOH A O     1 
HETATM 3639 O O     . HOH E 5 .   ? 32.570  -31.482 -13.190 1.00 17.67 ? 687 HOH A O     1 
HETATM 3640 O O     . HOH E 5 .   ? 24.695  -23.248 -17.736 1.00 5.95  ? 688 HOH A O     1 
HETATM 3641 O O     . HOH E 5 .   ? 15.416  -14.529 -25.874 1.00 3.50  ? 689 HOH A O     1 
HETATM 3642 O O     . HOH E 5 .   ? 17.958  3.712   -6.211  1.00 15.48 ? 690 HOH A O     1 
HETATM 3643 O O     . HOH E 5 .   ? 10.476  -25.803 -29.812 1.00 16.81 ? 691 HOH A O     1 
HETATM 3644 O O     . HOH E 5 .   ? 10.567  5.107   -1.070  1.00 13.65 ? 692 HOH A O     1 
HETATM 3645 O O     . HOH E 5 .   ? 34.365  -19.621 -11.590 1.00 14.23 ? 693 HOH A O     1 
HETATM 3646 O O     . HOH E 5 .   ? 31.481  -0.204  -17.097 1.00 12.24 ? 694 HOH A O     1 
HETATM 3647 O O     . HOH E 5 .   ? 16.335  9.892   -36.412 1.00 18.26 ? 695 HOH A O     1 
HETATM 3648 O O     . HOH E 5 .   ? 24.856  -36.913 -8.676  1.00 14.32 ? 696 HOH A O     1 
HETATM 3649 O O     . HOH E 5 .   ? 4.845   0.683   -24.809 1.00 10.39 ? 697 HOH A O     1 
HETATM 3650 O O     . HOH E 5 .   ? 11.556  15.186  -23.440 1.00 21.02 ? 698 HOH A O     1 
HETATM 3651 O O     . HOH E 5 .   ? 22.618  -1.714  -35.693 1.00 12.11 ? 699 HOH A O     1 
HETATM 3652 O O     . HOH E 5 .   ? 12.525  -6.099  -24.535 1.00 2.58  ? 700 HOH A O     1 
HETATM 3653 O O     . HOH E 5 .   ? 19.915  -20.039 -33.986 1.00 11.60 ? 701 HOH A O     1 
HETATM 3654 O O     . HOH E 5 .   ? 9.936   -22.955 -4.223  1.00 18.49 ? 702 HOH A O     1 
HETATM 3655 O O     . HOH E 5 .   ? 37.262  -28.464 -19.281 1.00 22.72 ? 703 HOH A O     1 
HETATM 3656 O O     . HOH E 5 .   ? 3.530   -19.565 -38.512 1.00 17.73 ? 704 HOH A O     1 
HETATM 3657 O O     . HOH E 5 .   ? 16.875  3.025   -3.491  1.00 12.46 ? 705 HOH A O     1 
HETATM 3658 O O     . HOH E 5 .   ? 23.794  -6.649  10.366  1.00 11.07 ? 706 HOH A O     1 
HETATM 3659 O O     . HOH E 5 .   ? 32.285  -18.168 -7.564  1.00 18.48 ? 707 HOH A O     1 
HETATM 3660 O O     . HOH E 5 .   ? 21.179  -2.984  -33.660 1.00 7.33  ? 708 HOH A O     1 
HETATM 3661 O O     . HOH E 5 .   ? -4.220  6.746   -10.717 1.00 15.62 ? 709 HOH A O     1 
HETATM 3662 O O     . HOH E 5 .   ? 39.423  -29.522 -13.338 1.00 27.85 ? 710 HOH A O     1 
HETATM 3663 O O     . HOH E 5 .   ? 17.827  8.934   -11.104 1.00 24.56 ? 711 HOH A O     1 
HETATM 3664 O O     . HOH E 5 .   ? 34.397  -27.033 -21.336 1.00 15.72 ? 712 HOH A O     1 
HETATM 3665 O O     . HOH E 5 .   ? 7.159   -1.890  -22.800 1.00 1.44  ? 713 HOH A O     1 
HETATM 3666 O O     . HOH E 5 .   ? 32.984  -13.430 -1.127  1.00 18.26 ? 714 HOH A O     1 
HETATM 3667 O O     . HOH E 5 .   ? 8.676   12.981  -25.367 1.00 23.92 ? 715 HOH A O     1 
HETATM 3668 O O     . HOH E 5 .   ? 26.974  -7.377  6.452   1.00 26.40 ? 716 HOH A O     1 
HETATM 3669 O O     . HOH E 5 .   ? 22.608  -18.523 1.726   1.00 12.84 ? 717 HOH A O     1 
HETATM 3670 O O     . HOH E 5 .   ? 15.570  12.121  -15.022 1.00 19.22 ? 718 HOH A O     1 
HETATM 3671 O O     . HOH E 5 .   ? -6.105  -5.912  0.116   1.00 14.19 ? 719 HOH A O     1 
HETATM 3672 O O     . HOH E 5 .   ? 16.358  -12.593 -42.946 1.00 26.06 ? 720 HOH A O     1 
HETATM 3673 O O     . HOH E 5 .   ? 15.388  8.270   -14.321 1.00 7.86  ? 721 HOH A O     1 
HETATM 3674 O O     . HOH E 5 .   ? 5.888   7.343   -32.559 1.00 15.37 ? 722 HOH A O     1 
HETATM 3675 O O     . HOH E 5 .   ? 10.057  -0.562  -40.099 1.00 15.52 ? 723 HOH A O     1 
HETATM 3676 O O     . HOH E 5 .   ? 5.758   -2.701  -39.213 1.00 15.68 ? 724 HOH A O     1 
HETATM 3677 O O     . HOH E 5 .   ? 24.068  5.597   -32.363 1.00 17.98 ? 725 HOH A O     1 
HETATM 3678 O O     . HOH E 5 .   ? 10.396  8.243   -8.185  1.00 19.91 ? 726 HOH A O     1 
HETATM 3679 O O     . HOH E 5 .   ? 11.705  12.644  -33.560 1.00 31.06 ? 727 HOH A O     1 
HETATM 3680 O O     . HOH E 5 .   ? 8.735   -18.602 -3.360  1.00 12.85 ? 728 HOH A O     1 
HETATM 3681 O O     . HOH E 5 .   ? 7.571   -6.216  14.868  1.00 23.39 ? 729 HOH A O     1 
HETATM 3682 O O     . HOH E 5 .   ? -10.292 -3.425  -7.974  1.00 20.36 ? 730 HOH A O     1 
HETATM 3683 O O     . HOH E 5 .   ? -8.033  -11.266 -0.862  1.00 13.34 ? 731 HOH A O     1 
HETATM 3684 O O     . HOH E 5 .   ? 10.251  2.969   1.545   1.00 10.33 ? 732 HOH A O     1 
HETATM 3685 O O     . HOH E 5 .   ? 17.448  2.567   -0.522  1.00 18.72 ? 733 HOH A O     1 
HETATM 3686 O O     . HOH E 5 .   ? -10.759 -15.323 -14.738 1.00 26.23 ? 734 HOH A O     1 
HETATM 3687 O O     . HOH E 5 .   ? 26.711  -9.844  -4.914  1.00 11.39 ? 735 HOH A O     1 
HETATM 3688 O O     . HOH E 5 .   ? 8.653   -15.014 5.375   1.00 18.91 ? 736 HOH A O     1 
HETATM 3689 O O     . HOH E 5 .   ? 28.016  -10.342 6.126   1.00 20.30 ? 737 HOH A O     1 
HETATM 3690 O O     . HOH E 5 .   ? 17.241  -40.672 -13.875 1.00 25.72 ? 738 HOH A O     1 
HETATM 3691 O O     . HOH E 5 .   ? -5.477  3.786   -4.898  1.00 10.55 ? 739 HOH A O     1 
HETATM 3692 O O     . HOH E 5 .   ? 19.090  -10.485 9.630   1.00 23.66 ? 740 HOH A O     1 
HETATM 3693 O O     . HOH E 5 .   ? 23.318  -21.216 -30.537 1.00 13.59 ? 741 HOH A O     1 
HETATM 3694 O O     . HOH E 5 .   ? 21.176  -18.872 4.276   1.00 24.45 ? 742 HOH A O     1 
HETATM 3695 O O     . HOH E 5 .   ? 10.733  14.668  -18.983 1.00 17.92 ? 743 HOH A O     1 
HETATM 3696 O O     . HOH E 5 .   ? 20.927  -16.784 -13.919 1.00 5.06  ? 744 HOH A O     1 
HETATM 3697 O O     . HOH E 5 .   ? 5.796   -17.702 -8.135  1.00 10.49 ? 745 HOH A O     1 
HETATM 3698 O O     . HOH E 5 .   ? 11.644  -7.310  -38.953 1.00 10.51 ? 746 HOH A O     1 
HETATM 3699 O O     . HOH E 5 .   ? 6.690   -5.033  -28.704 1.00 2.46  ? 747 HOH A O     1 
HETATM 3700 O O     . HOH E 5 .   ? 31.250  -1.925  -26.977 1.00 14.35 ? 748 HOH A O     1 
HETATM 3701 O O     . HOH E 5 .   ? 4.315   -6.088  -29.107 1.00 2.43  ? 749 HOH A O     1 
HETATM 3702 O O     . HOH E 5 .   ? 1.751   11.095  -16.508 1.00 8.13  ? 750 HOH A O     1 
HETATM 3703 O O     . HOH E 5 .   ? 3.949   -26.262 -35.680 1.00 24.79 ? 751 HOH A O     1 
HETATM 3704 O O     . HOH E 5 .   ? 27.911  -17.711 2.719   1.00 20.20 ? 752 HOH A O     1 
HETATM 3705 O O     . HOH E 5 .   ? -5.744  3.078   -15.123 1.00 13.27 ? 753 HOH A O     1 
HETATM 3706 O O     . HOH E 5 .   ? 16.078  -16.986 -26.859 1.00 3.75  ? 754 HOH A O     1 
HETATM 3707 O O     . HOH E 5 .   ? -2.697  -4.070  -29.909 1.00 8.93  ? 755 HOH A O     1 
HETATM 3708 O O     . HOH E 5 .   ? 29.258  -23.372 -30.225 1.00 34.74 ? 756 HOH A O     1 
HETATM 3709 O O     . HOH E 5 .   ? 1.060   -21.704 -30.697 1.00 7.33  ? 757 HOH A O     1 
HETATM 3710 O O     . HOH E 5 .   ? 14.573  -6.040  -27.027 1.00 2.72  ? 758 HOH A O     1 
HETATM 3711 O O     . HOH E 5 .   ? 13.697  -18.177 -8.778  1.00 10.72 ? 759 HOH A O     1 
HETATM 3712 O O     . HOH E 5 .   ? 26.039  -37.327 6.772   1.00 23.70 ? 760 HOH A O     1 
HETATM 3713 O O     . HOH E 5 .   ? 29.140  -19.728 -5.890  1.00 19.14 ? 761 HOH A O     1 
HETATM 3714 O O     . HOH E 5 .   ? 23.408  -11.623 -36.216 1.00 15.28 ? 762 HOH A O     1 
HETATM 3715 O O     . HOH E 5 .   ? 30.528  -5.593  -12.156 1.00 12.31 ? 763 HOH A O     1 
HETATM 3716 O O     . HOH E 5 .   ? 16.135  -1.961  -39.173 1.00 3.65  ? 764 HOH A O     1 
HETATM 3717 O O     . HOH E 5 .   ? 16.799  5.508   -7.718  1.00 19.14 ? 765 HOH A O     1 
HETATM 3718 O O     . HOH E 5 .   ? 19.679  7.399   -31.049 1.00 12.61 ? 766 HOH A O     1 
HETATM 3719 O O     . HOH E 5 .   ? 11.171  -9.798  8.743   1.00 23.47 ? 767 HOH A O     1 
HETATM 3720 O O     . HOH E 5 .   ? 8.885   -21.318 -34.853 1.00 14.92 ? 768 HOH A O     1 
HETATM 3721 O O     . HOH E 5 .   ? 8.033   14.719  -17.881 1.00 14.52 ? 769 HOH A O     1 
HETATM 3722 O O     . HOH E 5 .   ? 9.440   3.634   6.443   1.00 16.76 ? 770 HOH A O     1 
HETATM 3723 O O     . HOH E 5 .   ? 24.755  -30.314 -27.957 1.00 16.32 ? 771 HOH A O     1 
HETATM 3724 O O     . HOH E 5 .   ? -9.660  -6.590  -5.968  1.00 9.43  ? 772 HOH A O     1 
HETATM 3725 O O     . HOH E 5 .   ? -5.973  -9.312  -25.624 1.00 11.51 ? 773 HOH A O     1 
HETATM 3726 O O     . HOH E 5 .   ? -0.271  -4.600  -35.232 1.00 14.80 ? 774 HOH A O     1 
HETATM 3727 O O     . HOH E 5 .   ? 12.920  -16.281 -25.569 1.00 2.32  ? 775 HOH A O     1 
HETATM 3728 O O     . HOH E 5 .   ? 28.286  -31.859 -8.654  1.00 24.78 ? 776 HOH A O     1 
HETATM 3729 O O     . HOH E 5 .   ? 1.707   -17.517 -0.612  1.00 22.94 ? 777 HOH A O     1 
HETATM 3730 O O     . HOH E 5 .   ? 29.598  -30.052 -9.722  1.00 26.28 ? 778 HOH A O     1 
HETATM 3731 O O     . HOH E 5 .   ? 6.086   -21.796 1.867   1.00 18.67 ? 779 HOH A O     1 
HETATM 3732 O O     . HOH E 5 .   ? -2.475  -13.619 -17.983 1.00 7.82  ? 780 HOH A O     1 
HETATM 3733 O O     . HOH E 5 .   ? 10.992  2.192   -39.970 1.00 23.98 ? 781 HOH A O     1 
HETATM 3734 O O     . HOH E 5 .   ? 23.478  7.862   -12.655 1.00 22.79 ? 782 HOH A O     1 
HETATM 3735 O O     . HOH E 5 .   ? 4.020   -9.799  -36.043 1.00 22.45 ? 783 HOH A O     1 
HETATM 3736 O O     . HOH E 5 .   ? 15.371  -3.026  -15.783 1.00 10.42 ? 784 HOH A O     1 
HETATM 3737 O O     . HOH E 5 .   ? -1.884  5.721   -23.189 1.00 12.97 ? 785 HOH A O     1 
HETATM 3738 O O     . HOH E 5 .   ? 6.551   -24.070 -26.005 1.00 7.54  ? 786 HOH A O     1 
HETATM 3739 O O     . HOH E 5 .   ? 6.097   10.532  -33.074 1.00 25.07 ? 787 HOH A O     1 
HETATM 3740 O O     . HOH E 5 .   ? 7.527   -3.739  -20.716 1.00 1.14  ? 788 HOH A O     1 
HETATM 3741 O O     . HOH E 5 .   ? 25.997  -19.009 0.583   1.00 16.29 ? 789 HOH A O     1 
HETATM 3742 O O     . HOH E 5 .   ? 5.299   -18.293 -37.476 1.00 14.74 ? 790 HOH A O     1 
HETATM 3743 O O     . HOH E 5 .   ? 15.546  -18.813 -38.793 1.00 22.82 ? 791 HOH A O     1 
HETATM 3744 O O     . HOH E 5 .   ? 13.346  -17.017 -22.926 1.00 3.32  ? 792 HOH A O     1 
HETATM 3745 O O     . HOH E 5 .   ? 4.133   -0.069  -39.501 1.00 22.23 ? 793 HOH A O     1 
HETATM 3746 O O     . HOH E 5 .   ? 9.743   -8.246  -24.670 1.00 2.22  ? 794 HOH A O     1 
HETATM 3747 O O     . HOH E 5 .   ? 11.647  -5.901  -18.267 1.00 3.95  ? 795 HOH A O     1 
HETATM 3748 O O     . HOH E 5 .   ? 0.269   -12.999 -16.484 1.00 4.15  ? 796 HOH A O     1 
HETATM 3749 O O     . HOH E 5 .   ? 1.321   1.703   -38.212 1.00 18.49 ? 797 HOH A O     1 
HETATM 3750 O O     . HOH E 5 .   ? 35.825  -22.101 -11.439 1.00 20.15 ? 798 HOH A O     1 
HETATM 3751 O O     . HOH E 5 .   ? 21.412  -31.452 -26.667 1.00 24.23 ? 799 HOH A O     1 
HETATM 3752 O O     . HOH E 5 .   ? 12.429  -31.648 -12.433 1.00 28.96 ? 800 HOH A O     1 
HETATM 3753 O O     . HOH E 5 .   ? -0.392  -25.933 -27.703 1.00 14.45 ? 801 HOH A O     1 
HETATM 3754 O O     . HOH E 5 .   ? 0.937   7.780   -6.199  1.00 27.16 ? 802 HOH A O     1 
HETATM 3755 O O     . HOH E 5 .   ? 18.793  5.229   2.522   1.00 26.52 ? 803 HOH A O     1 
HETATM 3756 O O     . HOH E 5 .   ? 18.860  -7.861  -40.862 1.00 24.07 ? 804 HOH A O     1 
HETATM 3757 O O     . HOH E 5 .   ? 36.424  -19.553 -17.876 1.00 18.25 ? 805 HOH A O     1 
HETATM 3758 O O     . HOH E 5 .   ? 18.146  -12.423 -21.885 1.00 3.73  ? 806 HOH A O     1 
HETATM 3759 O O     . HOH E 5 .   ? -9.168  -1.252  -10.096 1.00 18.09 ? 807 HOH A O     1 
HETATM 3760 O O     . HOH E 5 .   ? 33.611  -8.499  -12.176 1.00 26.58 ? 808 HOH A O     1 
HETATM 3761 O O     . HOH E 5 .   ? -13.340 -7.091  -16.444 1.00 20.40 ? 809 HOH A O     1 
HETATM 3762 O O     . HOH E 5 .   ? 28.022  5.693   -17.002 1.00 10.33 ? 810 HOH A O     1 
HETATM 3763 O O     . HOH E 5 .   ? 28.571  -33.815 -10.496 1.00 19.72 ? 811 HOH A O     1 
HETATM 3764 O O     . HOH E 5 .   ? 12.638  -26.122 4.025   1.00 26.85 ? 812 HOH A O     1 
HETATM 3765 O O     . HOH E 5 .   ? 6.541   -20.094 -20.661 1.00 7.61  ? 813 HOH A O     1 
HETATM 3766 O O     . HOH E 5 .   ? -2.145  5.555   -3.968  1.00 18.79 ? 814 HOH A O     1 
HETATM 3767 O O     . HOH E 5 .   ? 12.257  5.794   -7.405  1.00 12.46 ? 815 HOH A O     1 
HETATM 3768 O O     . HOH E 5 .   ? -1.432  -3.213  3.447   1.00 22.13 ? 816 HOH A O     1 
HETATM 3769 O O     . HOH E 5 .   ? 30.506  -8.794  -35.029 1.00 24.18 ? 817 HOH A O     1 
HETATM 3770 O O     . HOH E 5 .   ? 4.938   -27.474 -28.280 1.00 11.94 ? 818 HOH A O     1 
HETATM 3771 O O     . HOH E 5 .   ? 9.897   12.066  -11.529 1.00 22.62 ? 819 HOH A O     1 
HETATM 3772 O O     . HOH E 5 .   ? -1.622  -25.184 -5.929  1.00 21.97 ? 820 HOH A O     1 
HETATM 3773 O O     . HOH E 5 .   ? 17.392  -27.581 -32.419 1.00 16.37 ? 821 HOH A O     1 
HETATM 3774 O O     . HOH E 5 .   ? -8.761  -5.009  -1.408  1.00 17.08 ? 822 HOH A O     1 
HETATM 3775 O O     . HOH E 5 .   ? -9.629  -12.221 -19.792 1.00 11.18 ? 823 HOH A O     1 
HETATM 3776 O O     . HOH E 5 .   ? -6.751  -18.619 -28.463 1.00 20.34 ? 824 HOH A O     1 
HETATM 3777 O O     . HOH E 5 .   ? 27.312  -4.415  -8.694  1.00 25.11 ? 825 HOH A O     1 
HETATM 3778 O O     . HOH E 5 .   ? 29.196  -3.066  -31.238 1.00 15.05 ? 826 HOH A O     1 
HETATM 3779 O O     . HOH E 5 .   ? 11.664  -27.277 -4.913  1.00 27.75 ? 827 HOH A O     1 
HETATM 3780 O O     . HOH E 5 .   ? 6.727   0.921   -32.957 1.00 10.84 ? 828 HOH A O     1 
HETATM 3781 O O     . HOH E 5 .   ? 2.902   5.378   -1.689  1.00 19.41 ? 829 HOH A O     1 
HETATM 3782 O O     . HOH E 5 .   ? -8.890  -0.231  -17.291 1.00 15.62 ? 830 HOH A O     1 
HETATM 3783 O O     . HOH E 5 .   ? -0.706  -26.237 -2.828  1.00 17.33 ? 831 HOH A O     1 
HETATM 3784 O O     . HOH E 5 .   ? 6.997   12.918  -29.491 1.00 18.94 ? 832 HOH A O     1 
HETATM 3785 O O     . HOH E 5 .   ? 6.251   -28.276 -30.516 1.00 15.72 ? 833 HOH A O     1 
HETATM 3786 O O     . HOH E 5 .   ? 29.729  -16.694 -34.020 1.00 18.90 ? 834 HOH A O     1 
HETATM 3787 O O     . HOH E 5 .   ? 13.281  -6.439  10.530  1.00 26.91 ? 835 HOH A O     1 
HETATM 3788 O O     . HOH E 5 .   ? 21.937  -34.561 -21.694 1.00 30.30 ? 836 HOH A O     1 
HETATM 3789 O O     . HOH E 5 .   ? 4.999   -8.410  -18.443 1.00 6.68  ? 837 HOH A O     1 
HETATM 3790 O O     . HOH E 5 .   ? 6.322   -7.855  5.177   1.00 29.49 ? 838 HOH A O     1 
HETATM 3791 O O     . HOH E 5 .   ? 31.470  -9.859  -1.065  1.00 20.61 ? 839 HOH A O     1 
HETATM 3792 O O     . HOH E 5 .   ? -17.407 -14.679 -5.627  1.00 18.17 ? 840 HOH A O     1 
HETATM 3793 O O     . HOH E 5 .   ? 19.720  -32.346 2.562   1.00 25.69 ? 841 HOH A O     1 
HETATM 3794 O O     . HOH E 5 .   ? 18.176  12.222  -15.350 1.00 24.01 ? 842 HOH A O     1 
HETATM 3795 O O     . HOH E 5 .   ? 13.448  1.368   -39.699 1.00 12.49 ? 843 HOH A O     1 
HETATM 3796 O O     . HOH E 5 .   ? 27.519  7.288   -19.278 1.00 26.72 ? 844 HOH A O     1 
HETATM 3797 O O     . HOH E 5 .   ? 28.377  -7.645  -2.382  1.00 18.30 ? 845 HOH A O     1 
HETATM 3798 O O     . HOH E 5 .   ? -1.549  -24.870 -17.150 1.00 22.63 ? 846 HOH A O     1 
HETATM 3799 O O     . HOH E 5 .   ? 16.521  6.550   3.153   1.00 25.75 ? 847 HOH A O     1 
HETATM 3800 O O     . HOH E 5 .   ? 17.691  -18.542 7.932   1.00 26.63 ? 848 HOH A O     1 
HETATM 3801 O O     . HOH E 5 .   ? -5.470  -20.046 -7.288  1.00 12.34 ? 849 HOH A O     1 
HETATM 3802 O O     . HOH E 5 .   ? 13.490  -19.056 -36.367 1.00 15.07 ? 850 HOH A O     1 
HETATM 3803 O O     . HOH E 5 .   ? -9.449  -15.267 -7.344  1.00 15.65 ? 851 HOH A O     1 
HETATM 3804 O O     . HOH E 5 .   ? 25.931  -13.169 7.084   1.00 15.36 ? 852 HOH A O     1 
HETATM 3805 O O     . HOH E 5 .   ? -4.314  -14.183 -28.845 1.00 14.86 ? 853 HOH A O     1 
HETATM 3806 O O     . HOH E 5 .   ? 16.715  -0.830  -15.303 1.00 14.66 ? 854 HOH A O     1 
HETATM 3807 O O     . HOH E 5 .   ? 29.371  -18.026 -31.522 1.00 21.68 ? 855 HOH A O     1 
HETATM 3808 O O     . HOH E 5 .   ? 29.868  -4.916  -9.679  1.00 31.00 ? 856 HOH A O     1 
HETATM 3809 O O     . HOH E 5 .   ? 35.839  -31.908 -20.230 1.00 20.28 ? 857 HOH A O     1 
HETATM 3810 O O     . HOH E 5 .   ? 19.739  -37.087 4.359   1.00 26.16 ? 858 HOH A O     1 
HETATM 3811 O O     . HOH E 5 .   ? -10.859 -6.125  -15.511 1.00 21.66 ? 859 HOH A O     1 
HETATM 3812 O O     . HOH E 5 .   ? 13.121  6.211   -4.766  1.00 24.78 ? 860 HOH A O     1 
HETATM 3813 O O     . HOH E 5 .   ? 32.666  -11.574 -3.197  1.00 25.02 ? 861 HOH A O     1 
HETATM 3814 O O     . HOH E 5 .   ? 1.568   -20.018 -0.153  1.00 25.00 ? 862 HOH A O     1 
HETATM 3815 O O     . HOH E 5 .   ? 8.266   7.341   -2.755  1.00 30.93 ? 863 HOH A O     1 
HETATM 3816 O O     . HOH E 5 .   ? 23.959  2.979   -5.719  1.00 26.82 ? 864 HOH A O     1 
HETATM 3817 O O     . HOH E 5 .   ? 25.143  -16.647 4.302   1.00 19.59 ? 865 HOH A O     1 
HETATM 3818 O O     . HOH E 5 .   ? 29.668  -9.369  3.457   1.00 23.45 ? 866 HOH A O     1 
HETATM 3819 O O     . HOH E 5 .   ? 3.567   -17.071 1.132   1.00 23.47 ? 867 HOH A O     1 
HETATM 3820 O O     . HOH E 5 .   ? -3.264  -21.857 -7.159  1.00 18.67 ? 868 HOH A O     1 
HETATM 3821 O O     . HOH E 5 .   ? 27.498  -16.697 5.418   1.00 16.55 ? 869 HOH A O     1 
HETATM 3822 O O     . HOH E 5 .   ? 15.351  -28.427 1.604   1.00 20.00 ? 870 HOH A O     1 
HETATM 3823 O O     . HOH E 5 .   ? -4.184  5.405   -22.049 1.00 17.97 ? 871 HOH A O     1 
HETATM 3824 O O     . HOH E 5 .   ? 1.154   13.289  -14.615 1.00 29.42 ? 872 HOH A O     1 
HETATM 3825 O O     . HOH E 5 .   ? 2.703   16.832  -13.968 1.00 23.04 ? 873 HOH A O     1 
HETATM 3826 O O     . HOH E 5 .   ? 7.427   -26.202 -27.534 1.00 18.09 ? 874 HOH A O     1 
HETATM 3827 O O     . HOH E 5 .   ? 10.976  10.007  -10.823 1.00 28.88 ? 875 HOH A O     1 
HETATM 3828 O O     . HOH E 5 .   ? 32.474  0.646   -26.582 1.00 17.99 ? 876 HOH A O     1 
HETATM 3829 O O     . HOH E 5 .   ? 19.543  1.749   0.803   1.00 24.38 ? 877 HOH A O     1 
HETATM 3830 O O     . HOH E 5 .   ? 8.284   15.887  -15.684 1.00 29.99 ? 878 HOH A O     1 
HETATM 3831 O O     . HOH E 5 .   ? 11.949  -19.640 -38.109 1.00 26.54 ? 879 HOH A O     1 
HETATM 3832 O O     . HOH E 5 .   ? 4.509   -0.386  -22.310 1.00 9.10  ? 880 HOH A O     1 
HETATM 3833 O O     . HOH E 5 .   ? 14.095  -1.000  -40.846 1.00 10.29 ? 881 HOH A O     1 
HETATM 3834 O O     . HOH E 5 .   ? 11.458  -11.629 -40.108 1.00 18.68 ? 882 HOH A O     1 
HETATM 3835 O O     . HOH E 5 .   ? -0.667  5.380   -2.020  1.00 20.48 ? 883 HOH A O     1 
HETATM 3836 O O     . HOH E 5 .   ? 10.763  -5.233  -40.612 1.00 22.38 ? 884 HOH A O     1 
HETATM 3837 O O     . HOH E 5 .   ? 31.333  -20.867 -6.498  1.00 25.82 ? 885 HOH A O     1 
HETATM 3838 O O     . HOH E 5 .   ? 6.307   -27.393 -35.033 1.00 28.61 ? 886 HOH A O     1 
HETATM 3839 O O     . HOH E 5 .   ? -11.982 -4.408  -5.369  1.00 23.46 ? 887 HOH A O     1 
HETATM 3840 O O     . HOH E 5 .   ? 29.996  -32.130 -11.808 1.00 26.93 ? 888 HOH A O     1 
HETATM 3841 O O     . HOH E 5 .   ? 21.822  7.014   -32.732 1.00 23.97 ? 889 HOH A O     1 
HETATM 3842 O O     . HOH E 5 .   ? -5.705  -11.320 -27.515 1.00 18.57 ? 890 HOH A O     1 
HETATM 3843 O O     . HOH E 5 .   ? 6.576   -22.708 -19.915 1.00 24.67 ? 891 HOH A O     1 
HETATM 3844 O O     . HOH E 5 .   ? 11.691  -9.203  -40.918 1.00 20.51 ? 892 HOH A O     1 
HETATM 3845 O O     . HOH E 5 .   ? 11.763  -2.266  -41.423 1.00 14.96 ? 893 HOH A O     1 
HETATM 3846 O O     . HOH E 5 .   ? 9.573   -13.306 -40.604 1.00 24.28 ? 894 HOH A O     1 
HETATM 3847 O O     . HOH E 5 .   ? 14.873  -0.703  -43.541 1.00 22.77 ? 895 HOH A O     1 
# 
