data_8XTB
# 
_entry.id   8XTB 
# 
_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   8XTB         pdb_00008xtb 10.2210/pdb8xtb/pdb 
WWPDB D_1300044149 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-01-15 
2 'Structure model' 1 1 2025-02-19 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Data collection' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            reflns 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_reflns.number_obs' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8XTB 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              liu_wd@tib.cas.cn 
_pdbx_contact_author.name_first         Weidong 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7954-7700 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Cong, L.'    1 ? 
'Li, Z.S.'    2 ? 
'Zheng, Z.R.' 3 ? 
'Han, X.'     4 ? 
'Wei, R.'     5 ? 
'Liu, W.D.'   6 ? 
'Uwe, B.'     7 ? 
# 
_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                     
'Crystal structure of a novel PU plastic degradation urethanase UMG-SP2 mutant from uncultured bacterium' 
_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 'Cong, L.'    1 ? 
primary 'Li, Z.S.'    2 ? 
primary 'Zheng, Z.R.' 3 ? 
primary 'Han, X.'     4 ? 
primary 'Wei, R.'     5 ? 
primary 'Liu, W.D.'   6 ? 
primary 'Uwe, B.'     7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man umgsp2                                          47044.090 2   ? ? ? ? 
2 non-polymer syn '4-oxidanylbutyl ~{N}-(4-aminophenyl)carbamate' 224.256   2   ? ? ? ? 
3 water       nat water                                           18.015    201 ? ? ? ? 
# 
_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       
;NLYFQGAGAGAGAGAMSELSAIETAAAIAGGSMTALEACDAAIARIEQRDGPINAVVVRDFDRARDAAKAADAEIAAAVR
KPLLGVPMTIKESFDIAGLPTSWGFAEHADHIATADSLVVSRLKAAGAVFLGKSNIPVGLADWQSVNPNYGRTNNPHDHS
RSAGGSSGGAAAALAAGMVPLEYGSDIGGSIRVPAHFCGVWGLKTTFDAVSLEGHYFPRTDSAKADLSVVGPMARTPADL
ALALDITSKVPLPQSRIANLSGLRILLLTAHPETVADSATISAVERAAAACEASGATVATSSPDLPDLSALVADYTRMLL
VVLARGLAPEGTEPVSLNAWYAMLDDQARMMRAFDRLFESFDAIFCPVLGTTAFAHSDEPDWAKRSLSIDGGIAPFAAQL
GWISMATYGGMPALSMPLGADGNGLPINLQIITRNWSDHDAIRIGALVAEALDR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;NLYFQGAGAGAGAGAMSELSAIETAAAIAGGSMTALEACDAAIARIEQRDGPINAVVVRDFDRARDAAKAADAEIAAAVR
KPLLGVPMTIKESFDIAGLPTSWGFAEHADHIATADSLVVSRLKAAGAVFLGKSNIPVGLADWQSVNPNYGRTNNPHDHS
RSAGGSSGGAAAALAAGMVPLEYGSDIGGSIRVPAHFCGVWGLKTTFDAVSLEGHYFPRTDSAKADLSVVGPMARTPADL
ALALDITSKVPLPQSRIANLSGLRILLLTAHPETVADSATISAVERAAAACEASGATVATSSPDLPDLSALVADYTRMLL
VVLARGLAPEGTEPVSLNAWYAMLDDQARMMRAFDRLFESFDAIFCPVLGTTAFAHSDEPDWAKRSLSIDGGIAPFAAQL
GWISMATYGGMPALSMPLGADGNGLPINLQIITRNWSDHDAIRIGALVAEALDR
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '4-oxidanylbutyl ~{N}-(4-aminophenyl)carbamate' A1D5H 
3 water                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASN n 
1 2   LEU n 
1 3   TYR n 
1 4   PHE n 
1 5   GLN n 
1 6   GLY n 
1 7   ALA n 
1 8   GLY n 
1 9   ALA n 
1 10  GLY n 
1 11  ALA n 
1 12  GLY n 
1 13  ALA n 
1 14  GLY n 
1 15  ALA n 
1 16  MET n 
1 17  SER n 
1 18  GLU n 
1 19  LEU n 
1 20  SER n 
1 21  ALA n 
1 22  ILE n 
1 23  GLU n 
1 24  THR n 
1 25  ALA n 
1 26  ALA n 
1 27  ALA n 
1 28  ILE n 
1 29  ALA n 
1 30  GLY n 
1 31  GLY n 
1 32  SER n 
1 33  MET n 
1 34  THR n 
1 35  ALA n 
1 36  LEU n 
1 37  GLU n 
1 38  ALA n 
1 39  CYS n 
1 40  ASP n 
1 41  ALA n 
1 42  ALA n 
1 43  ILE n 
1 44  ALA n 
1 45  ARG n 
1 46  ILE n 
1 47  GLU n 
1 48  GLN n 
1 49  ARG n 
1 50  ASP n 
1 51  GLY n 
1 52  PRO n 
1 53  ILE n 
1 54  ASN n 
1 55  ALA n 
1 56  VAL n 
1 57  VAL n 
1 58  VAL n 
1 59  ARG n 
1 60  ASP n 
1 61  PHE n 
1 62  ASP n 
1 63  ARG n 
1 64  ALA n 
1 65  ARG n 
1 66  ASP n 
1 67  ALA n 
1 68  ALA n 
1 69  LYS n 
1 70  ALA n 
1 71  ALA n 
1 72  ASP n 
1 73  ALA n 
1 74  GLU n 
1 75  ILE n 
1 76  ALA n 
1 77  ALA n 
1 78  ALA n 
1 79  VAL n 
1 80  ARG n 
1 81  LYS n 
1 82  PRO n 
1 83  LEU n 
1 84  LEU n 
1 85  GLY n 
1 86  VAL n 
1 87  PRO n 
1 88  MET n 
1 89  THR n 
1 90  ILE n 
1 91  LYS n 
1 92  GLU n 
1 93  SER n 
1 94  PHE n 
1 95  ASP n 
1 96  ILE n 
1 97  ALA n 
1 98  GLY n 
1 99  LEU n 
1 100 PRO n 
1 101 THR n 
1 102 SER n 
1 103 TRP n 
1 104 GLY n 
1 105 PHE n 
1 106 ALA n 
1 107 GLU n 
1 108 HIS n 
1 109 ALA n 
1 110 ASP n 
1 111 HIS n 
1 112 ILE n 
1 113 ALA n 
1 114 THR n 
1 115 ALA n 
1 116 ASP n 
1 117 SER n 
1 118 LEU n 
1 119 VAL n 
1 120 VAL n 
1 121 SER n 
1 122 ARG n 
1 123 LEU n 
1 124 LYS n 
1 125 ALA n 
1 126 ALA n 
1 127 GLY n 
1 128 ALA n 
1 129 VAL n 
1 130 PHE n 
1 131 LEU n 
1 132 GLY n 
1 133 LYS n 
1 134 SER n 
1 135 ASN n 
1 136 ILE n 
1 137 PRO n 
1 138 VAL n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 ASP n 
1 143 TRP n 
1 144 GLN n 
1 145 SER n 
1 146 VAL n 
1 147 ASN n 
1 148 PRO n 
1 149 ASN n 
1 150 TYR n 
1 151 GLY n 
1 152 ARG n 
1 153 THR n 
1 154 ASN n 
1 155 ASN n 
1 156 PRO n 
1 157 HIS n 
1 158 ASP n 
1 159 HIS n 
1 160 SER n 
1 161 ARG n 
1 162 SER n 
1 163 ALA n 
1 164 GLY n 
1 165 GLY n 
1 166 SER n 
1 167 SER n 
1 168 GLY n 
1 169 GLY n 
1 170 ALA n 
1 171 ALA n 
1 172 ALA n 
1 173 ALA n 
1 174 LEU n 
1 175 ALA n 
1 176 ALA n 
1 177 GLY n 
1 178 MET n 
1 179 VAL n 
1 180 PRO n 
1 181 LEU n 
1 182 GLU n 
1 183 TYR n 
1 184 GLY n 
1 185 SER n 
1 186 ASP n 
1 187 ILE n 
1 188 GLY n 
1 189 GLY n 
1 190 SER n 
1 191 ILE n 
1 192 ARG n 
1 193 VAL n 
1 194 PRO n 
1 195 ALA n 
1 196 HIS n 
1 197 PHE n 
1 198 CYS n 
1 199 GLY n 
1 200 VAL n 
1 201 TRP n 
1 202 GLY n 
1 203 LEU n 
1 204 LYS n 
1 205 THR n 
1 206 THR n 
1 207 PHE n 
1 208 ASP n 
1 209 ALA n 
1 210 VAL n 
1 211 SER n 
1 212 LEU n 
1 213 GLU n 
1 214 GLY n 
1 215 HIS n 
1 216 TYR n 
1 217 PHE n 
1 218 PRO n 
1 219 ARG n 
1 220 THR n 
1 221 ASP n 
1 222 SER n 
1 223 ALA n 
1 224 LYS n 
1 225 ALA n 
1 226 ASP n 
1 227 LEU n 
1 228 SER n 
1 229 VAL n 
1 230 VAL n 
1 231 GLY n 
1 232 PRO n 
1 233 MET n 
1 234 ALA n 
1 235 ARG n 
1 236 THR n 
1 237 PRO n 
1 238 ALA n 
1 239 ASP n 
1 240 LEU n 
1 241 ALA n 
1 242 LEU n 
1 243 ALA n 
1 244 LEU n 
1 245 ASP n 
1 246 ILE n 
1 247 THR n 
1 248 SER n 
1 249 LYS n 
1 250 VAL n 
1 251 PRO n 
1 252 LEU n 
1 253 PRO n 
1 254 GLN n 
1 255 SER n 
1 256 ARG n 
1 257 ILE n 
1 258 ALA n 
1 259 ASN n 
1 260 LEU n 
1 261 SER n 
1 262 GLY n 
1 263 LEU n 
1 264 ARG n 
1 265 ILE n 
1 266 LEU n 
1 267 LEU n 
1 268 LEU n 
1 269 THR n 
1 270 ALA n 
1 271 HIS n 
1 272 PRO n 
1 273 GLU n 
1 274 THR n 
1 275 VAL n 
1 276 ALA n 
1 277 ASP n 
1 278 SER n 
1 279 ALA n 
1 280 THR n 
1 281 ILE n 
1 282 SER n 
1 283 ALA n 
1 284 VAL n 
1 285 GLU n 
1 286 ARG n 
1 287 ALA n 
1 288 ALA n 
1 289 ALA n 
1 290 ALA n 
1 291 CYS n 
1 292 GLU n 
1 293 ALA n 
1 294 SER n 
1 295 GLY n 
1 296 ALA n 
1 297 THR n 
1 298 VAL n 
1 299 ALA n 
1 300 THR n 
1 301 SER n 
1 302 SER n 
1 303 PRO n 
1 304 ASP n 
1 305 LEU n 
1 306 PRO n 
1 307 ASP n 
1 308 LEU n 
1 309 SER n 
1 310 ALA n 
1 311 LEU n 
1 312 VAL n 
1 313 ALA n 
1 314 ASP n 
1 315 TYR n 
1 316 THR n 
1 317 ARG n 
1 318 MET n 
1 319 LEU n 
1 320 LEU n 
1 321 VAL n 
1 322 VAL n 
1 323 LEU n 
1 324 ALA n 
1 325 ARG n 
1 326 GLY n 
1 327 LEU n 
1 328 ALA n 
1 329 PRO n 
1 330 GLU n 
1 331 GLY n 
1 332 THR n 
1 333 GLU n 
1 334 PRO n 
1 335 VAL n 
1 336 SER n 
1 337 LEU n 
1 338 ASN n 
1 339 ALA n 
1 340 TRP n 
1 341 TYR n 
1 342 ALA n 
1 343 MET n 
1 344 LEU n 
1 345 ASP n 
1 346 ASP n 
1 347 GLN n 
1 348 ALA n 
1 349 ARG n 
1 350 MET n 
1 351 MET n 
1 352 ARG n 
1 353 ALA n 
1 354 PHE n 
1 355 ASP n 
1 356 ARG n 
1 357 LEU n 
1 358 PHE n 
1 359 GLU n 
1 360 SER n 
1 361 PHE n 
1 362 ASP n 
1 363 ALA n 
1 364 ILE n 
1 365 PHE n 
1 366 CYS n 
1 367 PRO n 
1 368 VAL n 
1 369 LEU n 
1 370 GLY n 
1 371 THR n 
1 372 THR n 
1 373 ALA n 
1 374 PHE n 
1 375 ALA n 
1 376 HIS n 
1 377 SER n 
1 378 ASP n 
1 379 GLU n 
1 380 PRO n 
1 381 ASP n 
1 382 TRP n 
1 383 ALA n 
1 384 LYS n 
1 385 ARG n 
1 386 SER n 
1 387 LEU n 
1 388 SER n 
1 389 ILE n 
1 390 ASP n 
1 391 GLY n 
1 392 GLY n 
1 393 ILE n 
1 394 ALA n 
1 395 PRO n 
1 396 PHE n 
1 397 ALA n 
1 398 ALA n 
1 399 GLN n 
1 400 LEU n 
1 401 GLY n 
1 402 TRP n 
1 403 ILE n 
1 404 SER n 
1 405 MET n 
1 406 ALA n 
1 407 THR n 
1 408 TYR n 
1 409 GLY n 
1 410 GLY n 
1 411 MET n 
1 412 PRO n 
1 413 ALA n 
1 414 LEU n 
1 415 SER n 
1 416 MET n 
1 417 PRO n 
1 418 LEU n 
1 419 GLY n 
1 420 ALA n 
1 421 ASP n 
1 422 GLY n 
1 423 ASN n 
1 424 GLY n 
1 425 LEU n 
1 426 PRO n 
1 427 ILE n 
1 428 ASN n 
1 429 LEU n 
1 430 GLN n 
1 431 ILE n 
1 432 ILE n 
1 433 THR n 
1 434 ARG n 
1 435 ASN n 
1 436 TRP n 
1 437 SER n 
1 438 ASP n 
1 439 HIS n 
1 440 ASP n 
1 441 ALA n 
1 442 ILE n 
1 443 ARG n 
1 444 ILE n 
1 445 GLY n 
1 446 ALA n 
1 447 LEU n 
1 448 VAL n 
1 449 ALA n 
1 450 GLU n 
1 451 ALA n 
1 452 LEU n 
1 453 ASP n 
1 454 ARG 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                   454 
_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      'uncultured bacterium' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     77133 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_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 
A1D5H non-polymer         . '4-oxidanylbutyl ~{N}-(4-aminophenyl)carbamate' ? 'C11 H16 N2 O3'  224.256 
ALA   'L-peptide linking' y ALANINE                                         ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                        ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                      ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                 ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                        ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                       ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                 ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                         ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                       ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                           ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                      ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                         ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                          ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                      ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                   ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                         ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                          ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                       ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                      ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                        ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ASN 1   1   ?   ?   ?   A . n 
A 1 2   LEU 2   2   ?   ?   ?   A . n 
A 1 3   TYR 3   3   ?   ?   ?   A . n 
A 1 4   PHE 4   4   ?   ?   ?   A . n 
A 1 5   GLN 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   ?   ?   ?   A . n 
A 1 7   ALA 7   7   ?   ?   ?   A . n 
A 1 8   GLY 8   8   ?   ?   ?   A . n 
A 1 9   ALA 9   9   ?   ?   ?   A . n 
A 1 10  GLY 10  10  ?   ?   ?   A . n 
A 1 11  ALA 11  11  ?   ?   ?   A . n 
A 1 12  GLY 12  12  ?   ?   ?   A . n 
A 1 13  ALA 13  13  ?   ?   ?   A . n 
A 1 14  GLY 14  14  ?   ?   ?   A . n 
A 1 15  ALA 15  15  ?   ?   ?   A . n 
A 1 16  MET 16  16  ?   ?   ?   A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  SER 20  20  20  SER SER A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  ILE 28  28  28  ILE ILE A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  MET 33  33  33  MET MET A . n 
A 1 34  THR 34  34  34  THR THR A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  CYS 39  39  39  CYS CYS A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  ARG 63  63  63  ARG ARG A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  ARG 65  65  65  ARG ARG A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  LYS 81  81  81  LYS LYS A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  MET 88  88  88  MET MET A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  ILE 90  90  90  ILE ILE A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 THR 101 101 101 THR THR A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 TRP 103 103 103 TRP TRP A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 PHE 105 105 105 PHE PHE A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 HIS 108 108 108 HIS HIS A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 THR 114 114 114 THR THR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ASP 116 116 116 ASP ASP A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 ASN 135 135 135 ASN ASN A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 ASP 142 142 142 ASP ASP A . n 
A 1 143 TRP 143 143 143 TRP TRP A . n 
A 1 144 GLN 144 144 144 GLN GLN A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 VAL 146 146 146 VAL VAL A . n 
A 1 147 ASN 147 147 147 ASN ASN A . n 
A 1 148 PRO 148 148 148 PRO PRO A . n 
A 1 149 ASN 149 149 149 ASN ASN A . n 
A 1 150 TYR 150 150 150 TYR TYR A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 ASN 154 154 154 ASN ASN A . n 
A 1 155 ASN 155 155 155 ASN ASN A . n 
A 1 156 PRO 156 156 156 PRO PRO A . n 
A 1 157 HIS 157 157 157 HIS HIS A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 HIS 159 159 159 HIS HIS A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 MET 178 178 178 MET MET A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 TYR 183 183 183 TYR TYR A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 ILE 191 191 191 ILE ILE A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 HIS 196 196 196 HIS HIS A . n 
A 1 197 PHE 197 197 197 PHE PHE A . n 
A 1 198 CYS 198 198 198 CYS CYS A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 TRP 201 201 201 TRP TRP A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 THR 206 206 206 THR THR A . n 
A 1 207 PHE 207 207 207 PHE PHE A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 SER 211 211 211 SER SER A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 HIS 215 215 215 HIS HIS A . n 
A 1 216 TYR 216 216 216 TYR TYR A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 PRO 218 218 218 PRO PRO A . n 
A 1 219 ARG 219 219 219 ARG ARG A . n 
A 1 220 THR 220 220 220 THR THR A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 SER 228 228 228 SER SER A . n 
A 1 229 VAL 229 229 229 VAL VAL A . n 
A 1 230 VAL 230 230 230 VAL VAL A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 PRO 232 232 232 PRO PRO A . n 
A 1 233 MET 233 233 233 MET MET A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 THR 236 236 236 THR THR A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 THR 247 247 247 THR THR A . n 
A 1 248 SER 248 248 248 SER SER A . n 
A 1 249 LYS 249 249 249 LYS LYS A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 PRO 251 251 251 PRO PRO A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 PRO 253 253 253 PRO PRO A . n 
A 1 254 GLN 254 254 254 GLN GLN A . n 
A 1 255 SER 255 255 255 SER SER A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 ILE 257 257 257 ILE ILE A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 ASN 259 259 259 ASN ASN A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 GLY 262 262 262 GLY GLY A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 ARG 264 264 264 ARG ARG A . n 
A 1 265 ILE 265 265 265 ILE ILE A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 THR 269 269 269 THR THR A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 HIS 271 271 271 HIS HIS A . n 
A 1 272 PRO 272 272 272 PRO PRO A . n 
A 1 273 GLU 273 273 273 GLU GLU A . n 
A 1 274 THR 274 274 274 THR THR A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 ASP 277 277 277 ASP ASP A . n 
A 1 278 SER 278 278 278 SER SER A . n 
A 1 279 ALA 279 279 279 ALA ALA A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 GLU 285 285 285 GLU GLU A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 CYS 291 291 291 CYS CYS A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 ALA 293 293 293 ALA ALA A . n 
A 1 294 SER 294 294 294 SER SER A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 ALA 296 296 296 ALA ALA A . n 
A 1 297 THR 297 297 297 THR THR A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 THR 300 300 300 THR THR A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 SER 302 302 302 SER SER A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 ASP 304 304 304 ASP ASP A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 PRO 306 306 306 PRO PRO A . n 
A 1 307 ASP 307 307 307 ASP ASP A . n 
A 1 308 LEU 308 308 308 LEU LEU A . n 
A 1 309 SER 309 309 309 SER SER A . n 
A 1 310 ALA 310 310 310 ALA ALA A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 ASP 314 314 314 ASP ASP A . n 
A 1 315 TYR 315 315 315 TYR TYR A . n 
A 1 316 THR 316 316 316 THR THR A . n 
A 1 317 ARG 317 317 317 ARG ARG A . n 
A 1 318 MET 318 318 318 MET MET A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 VAL 321 321 321 VAL VAL A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 LEU 323 323 323 LEU LEU A . n 
A 1 324 ALA 324 324 324 ALA ALA A . n 
A 1 325 ARG 325 325 325 ARG ARG A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 LEU 327 327 327 LEU LEU A . n 
A 1 328 ALA 328 328 328 ALA ALA A . n 
A 1 329 PRO 329 329 329 PRO PRO A . n 
A 1 330 GLU 330 330 330 GLU GLU A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 THR 332 332 332 THR THR A . n 
A 1 333 GLU 333 333 333 GLU GLU A . n 
A 1 334 PRO 334 334 334 PRO PRO A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 SER 336 336 336 SER SER A . n 
A 1 337 LEU 337 337 337 LEU LEU A . n 
A 1 338 ASN 338 338 338 ASN ASN A . n 
A 1 339 ALA 339 339 339 ALA ALA A . n 
A 1 340 TRP 340 340 340 TRP TRP A . n 
A 1 341 TYR 341 341 341 TYR TYR A . n 
A 1 342 ALA 342 342 342 ALA ALA A . n 
A 1 343 MET 343 343 343 MET MET A . n 
A 1 344 LEU 344 344 344 LEU LEU A . n 
A 1 345 ASP 345 345 345 ASP ASP A . n 
A 1 346 ASP 346 346 346 ASP ASP A . n 
A 1 347 GLN 347 347 347 GLN GLN A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 ARG 349 349 349 ARG ARG A . n 
A 1 350 MET 350 350 350 MET MET A . n 
A 1 351 MET 351 351 351 MET MET A . n 
A 1 352 ARG 352 352 352 ARG ARG A . n 
A 1 353 ALA 353 353 353 ALA ALA A . n 
A 1 354 PHE 354 354 354 PHE PHE A . n 
A 1 355 ASP 355 355 355 ASP ASP A . n 
A 1 356 ARG 356 356 356 ARG ARG A . n 
A 1 357 LEU 357 357 357 LEU LEU A . n 
A 1 358 PHE 358 358 358 PHE PHE A . n 
A 1 359 GLU 359 359 359 GLU GLU A . n 
A 1 360 SER 360 360 360 SER SER A . n 
A 1 361 PHE 361 361 361 PHE PHE A . n 
A 1 362 ASP 362 362 362 ASP ASP A . n 
A 1 363 ALA 363 363 363 ALA ALA A . n 
A 1 364 ILE 364 364 364 ILE ILE A . n 
A 1 365 PHE 365 365 365 PHE PHE A . n 
A 1 366 CYS 366 366 366 CYS CYS A . n 
A 1 367 PRO 367 367 367 PRO PRO A . n 
A 1 368 VAL 368 368 368 VAL VAL A . n 
A 1 369 LEU 369 369 369 LEU LEU A . n 
A 1 370 GLY 370 370 370 GLY GLY A . n 
A 1 371 THR 371 371 371 THR THR A . n 
A 1 372 THR 372 372 372 THR THR A . n 
A 1 373 ALA 373 373 373 ALA ALA A . n 
A 1 374 PHE 374 374 374 PHE PHE A . n 
A 1 375 ALA 375 375 375 ALA ALA A . n 
A 1 376 HIS 376 376 376 HIS HIS A . n 
A 1 377 SER 377 377 377 SER SER A . n 
A 1 378 ASP 378 378 378 ASP ASP A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 PRO 380 380 380 PRO PRO A . n 
A 1 381 ASP 381 381 381 ASP ASP A . n 
A 1 382 TRP 382 382 382 TRP TRP A . n 
A 1 383 ALA 383 383 383 ALA ALA A . n 
A 1 384 LYS 384 384 384 LYS LYS A . n 
A 1 385 ARG 385 385 385 ARG ARG A . n 
A 1 386 SER 386 386 386 SER SER A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 SER 388 388 388 SER SER A . n 
A 1 389 ILE 389 389 389 ILE ILE A . n 
A 1 390 ASP 390 390 390 ASP ASP A . n 
A 1 391 GLY 391 391 391 GLY GLY A . n 
A 1 392 GLY 392 392 392 GLY GLY A . n 
A 1 393 ILE 393 393 393 ILE ILE A . n 
A 1 394 ALA 394 394 394 ALA ALA A . n 
A 1 395 PRO 395 395 395 PRO PRO A . n 
A 1 396 PHE 396 396 396 PHE PHE A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 ALA 398 398 398 ALA ALA A . n 
A 1 399 GLN 399 399 399 GLN GLN A . n 
A 1 400 LEU 400 400 400 LEU LEU A . n 
A 1 401 GLY 401 401 401 GLY GLY A . n 
A 1 402 TRP 402 402 402 TRP TRP A . n 
A 1 403 ILE 403 403 403 ILE ILE A . n 
A 1 404 SER 404 404 404 SER SER A . n 
A 1 405 MET 405 405 405 MET MET A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 THR 407 407 407 THR THR A . n 
A 1 408 TYR 408 408 408 TYR TYR A . n 
A 1 409 GLY 409 409 409 GLY GLY A . n 
A 1 410 GLY 410 410 410 GLY GLY A . n 
A 1 411 MET 411 411 411 MET MET A . n 
A 1 412 PRO 412 412 412 PRO PRO A . n 
A 1 413 ALA 413 413 413 ALA ALA A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 SER 415 415 415 SER SER A . n 
A 1 416 MET 416 416 416 MET MET A . n 
A 1 417 PRO 417 417 417 PRO PRO A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 GLY 419 419 419 GLY GLY A . n 
A 1 420 ALA 420 420 420 ALA ALA A . n 
A 1 421 ASP 421 421 421 ASP ASP A . n 
A 1 422 GLY 422 422 422 GLY GLY A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 GLY 424 424 424 GLY GLY A . n 
A 1 425 LEU 425 425 425 LEU LEU A . n 
A 1 426 PRO 426 426 426 PRO PRO A . n 
A 1 427 ILE 427 427 427 ILE ILE A . n 
A 1 428 ASN 428 428 428 ASN ASN A . n 
A 1 429 LEU 429 429 429 LEU LEU A . n 
A 1 430 GLN 430 430 430 GLN GLN A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 ILE 432 432 432 ILE ILE A . n 
A 1 433 THR 433 433 433 THR THR A . n 
A 1 434 ARG 434 434 434 ARG ARG A . n 
A 1 435 ASN 435 435 435 ASN ASN A . n 
A 1 436 TRP 436 436 436 TRP TRP A . n 
A 1 437 SER 437 437 437 SER SER A . n 
A 1 438 ASP 438 438 438 ASP ASP A . n 
A 1 439 HIS 439 439 439 HIS HIS A . n 
A 1 440 ASP 440 440 440 ASP ASP A . n 
A 1 441 ALA 441 441 441 ALA ALA A . n 
A 1 442 ILE 442 442 442 ILE ILE A . n 
A 1 443 ARG 443 443 443 ARG ARG A . n 
A 1 444 ILE 444 444 444 ILE ILE A . n 
A 1 445 GLY 445 445 445 GLY GLY A . n 
A 1 446 ALA 446 446 446 ALA ALA A . n 
A 1 447 LEU 447 447 447 LEU LEU A . n 
A 1 448 VAL 448 448 448 VAL VAL A . n 
A 1 449 ALA 449 449 449 ALA ALA A . n 
A 1 450 GLU 450 450 450 GLU GLU A . n 
A 1 451 ALA 451 451 451 ALA ALA A . n 
A 1 452 LEU 452 452 452 LEU LEU A . n 
A 1 453 ASP 453 453 453 ASP ASP A . n 
A 1 454 ARG 454 454 454 ARG ARG A . n 
B 1 1   ASN 1   1   ?   ?   ?   B . n 
B 1 2   LEU 2   2   ?   ?   ?   B . n 
B 1 3   TYR 3   3   ?   ?   ?   B . n 
B 1 4   PHE 4   4   ?   ?   ?   B . n 
B 1 5   GLN 5   5   ?   ?   ?   B . n 
B 1 6   GLY 6   6   ?   ?   ?   B . n 
B 1 7   ALA 7   7   ?   ?   ?   B . n 
B 1 8   GLY 8   8   ?   ?   ?   B . n 
B 1 9   ALA 9   9   ?   ?   ?   B . n 
B 1 10  GLY 10  10  ?   ?   ?   B . n 
B 1 11  ALA 11  11  ?   ?   ?   B . n 
B 1 12  GLY 12  12  ?   ?   ?   B . n 
B 1 13  ALA 13  13  ?   ?   ?   B . n 
B 1 14  GLY 14  14  ?   ?   ?   B . n 
B 1 15  ALA 15  15  ?   ?   ?   B . n 
B 1 16  MET 16  16  ?   ?   ?   B . n 
B 1 17  SER 17  17  17  SER SER B . n 
B 1 18  GLU 18  18  18  GLU GLU B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  SER 20  20  20  SER SER B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  GLU 23  23  23  GLU GLU B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  ALA 26  26  26  ALA ALA B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  ILE 28  28  28  ILE ILE B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  GLY 30  30  30  GLY GLY B . n 
B 1 31  GLY 31  31  31  GLY GLY B . n 
B 1 32  SER 32  32  32  SER SER B . n 
B 1 33  MET 33  33  33  MET MET B . n 
B 1 34  THR 34  34  34  THR THR B . n 
B 1 35  ALA 35  35  35  ALA ALA B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  GLU 37  37  37  GLU GLU B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  CYS 39  39  39  CYS CYS B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  ARG 45  45  45  ARG ARG B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  GLN 48  48  48  GLN GLN B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  ASP 50  50  50  ASP ASP B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  ILE 53  53  53  ILE ILE B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  VAL 57  57  57  VAL VAL B . n 
B 1 58  VAL 58  58  58  VAL VAL B . n 
B 1 59  ARG 59  59  59  ARG ARG B . n 
B 1 60  ASP 60  60  60  ASP ASP B . n 
B 1 61  PHE 61  61  61  PHE PHE B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  ARG 63  63  63  ARG ARG B . n 
B 1 64  ALA 64  64  64  ALA ALA B . n 
B 1 65  ARG 65  65  65  ARG ARG B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ALA 67  67  67  ALA ALA B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  ALA 71  71  71  ALA ALA B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  GLU 74  74  74  GLU GLU B . n 
B 1 75  ILE 75  75  75  ILE ILE B . n 
B 1 76  ALA 76  76  76  ALA ALA B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  ALA 78  78  78  ALA ALA B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  ARG 80  80  80  ARG ARG B . n 
B 1 81  LYS 81  81  81  LYS LYS B . n 
B 1 82  PRO 82  82  82  PRO PRO B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  PRO 87  87  87  PRO PRO B . n 
B 1 88  MET 88  88  88  MET MET B . n 
B 1 89  THR 89  89  89  THR THR B . n 
B 1 90  ILE 90  90  90  ILE ILE B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  GLU 92  92  92  GLU GLU B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  PHE 94  94  94  PHE PHE B . n 
B 1 95  ASP 95  95  95  ASP ASP B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 THR 101 101 101 THR THR B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 TRP 103 103 103 TRP TRP B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 PHE 105 105 105 PHE PHE B . n 
B 1 106 ALA 106 106 106 ALA ALA B . n 
B 1 107 GLU 107 107 107 GLU GLU B . n 
B 1 108 HIS 108 108 108 HIS HIS B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 THR 114 114 114 THR THR B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 ASP 116 116 116 ASP ASP B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 ARG 122 122 122 ARG ARG B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 LYS 124 124 124 LYS LYS B . n 
B 1 125 ALA 125 125 125 ALA ALA B . n 
B 1 126 ALA 126 126 126 ALA ALA B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 ALA 128 128 128 ALA ALA B . n 
B 1 129 VAL 129 129 129 VAL VAL B . n 
B 1 130 PHE 130 130 130 PHE PHE B . n 
B 1 131 LEU 131 131 131 LEU LEU B . n 
B 1 132 GLY 132 132 132 GLY GLY B . n 
B 1 133 LYS 133 133 133 LYS LYS B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 ASN 135 135 135 ASN ASN B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 PRO 137 137 137 PRO PRO B . n 
B 1 138 VAL 138 138 138 VAL VAL B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ALA 141 141 141 ALA ALA B . n 
B 1 142 ASP 142 142 142 ASP ASP B . n 
B 1 143 TRP 143 143 143 TRP TRP B . n 
B 1 144 GLN 144 144 144 GLN GLN B . n 
B 1 145 SER 145 145 145 SER SER B . n 
B 1 146 VAL 146 146 146 VAL VAL B . n 
B 1 147 ASN 147 147 147 ASN ASN B . n 
B 1 148 PRO 148 148 148 PRO PRO B . n 
B 1 149 ASN 149 149 149 ASN ASN B . n 
B 1 150 TYR 150 150 150 TYR TYR B . n 
B 1 151 GLY 151 151 151 GLY GLY B . n 
B 1 152 ARG 152 152 152 ARG ARG B . n 
B 1 153 THR 153 153 153 THR THR B . n 
B 1 154 ASN 154 154 154 ASN ASN B . n 
B 1 155 ASN 155 155 155 ASN ASN B . n 
B 1 156 PRO 156 156 156 PRO PRO B . n 
B 1 157 HIS 157 157 157 HIS HIS B . n 
B 1 158 ASP 158 158 158 ASP ASP B . n 
B 1 159 HIS 159 159 159 HIS HIS B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 SER 162 162 162 SER SER B . n 
B 1 163 ALA 163 163 163 ALA ALA B . n 
B 1 164 GLY 164 164 164 GLY GLY B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 GLY 168 168 168 GLY GLY B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 ALA 170 170 170 ALA ALA B . n 
B 1 171 ALA 171 171 171 ALA ALA B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 ALA 176 176 176 ALA ALA B . n 
B 1 177 GLY 177 177 177 GLY GLY B . n 
B 1 178 MET 178 178 178 MET MET B . n 
B 1 179 VAL 179 179 179 VAL VAL B . n 
B 1 180 PRO 180 180 180 PRO PRO B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 GLU 182 182 182 GLU GLU B . n 
B 1 183 TYR 183 183 183 TYR TYR B . n 
B 1 184 GLY 184 184 184 GLY GLY B . n 
B 1 185 SER 185 185 185 SER SER B . n 
B 1 186 ASP 186 186 186 ASP ASP B . n 
B 1 187 ILE 187 187 187 ILE ILE B . n 
B 1 188 GLY 188 188 188 GLY GLY B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 ILE 191 191 191 ILE ILE B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 VAL 193 193 193 VAL VAL B . n 
B 1 194 PRO 194 194 194 PRO PRO B . n 
B 1 195 ALA 195 195 195 ALA ALA B . n 
B 1 196 HIS 196 196 196 HIS HIS B . n 
B 1 197 PHE 197 197 197 PHE PHE B . n 
B 1 198 CYS 198 198 198 CYS CYS B . n 
B 1 199 GLY 199 199 199 GLY GLY B . n 
B 1 200 VAL 200 200 200 VAL VAL B . n 
B 1 201 TRP 201 201 201 TRP TRP B . n 
B 1 202 GLY 202 202 202 GLY GLY B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 LYS 204 204 204 LYS LYS B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 THR 206 206 206 THR THR B . n 
B 1 207 PHE 207 207 207 PHE PHE B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 ALA 209 209 209 ALA ALA B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 SER 211 211 211 SER SER B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 GLU 213 213 213 GLU GLU B . n 
B 1 214 GLY 214 214 214 GLY GLY B . n 
B 1 215 HIS 215 215 215 HIS HIS B . n 
B 1 216 TYR 216 216 216 TYR TYR B . n 
B 1 217 PHE 217 217 217 PHE PHE B . n 
B 1 218 PRO 218 218 218 PRO PRO B . n 
B 1 219 ARG 219 219 219 ARG ARG B . n 
B 1 220 THR 220 220 220 THR THR B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 SER 222 222 222 SER SER B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 LYS 224 224 224 LYS LYS B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 ASP 226 226 226 ASP ASP B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 SER 228 228 228 SER SER B . n 
B 1 229 VAL 229 229 229 VAL VAL B . n 
B 1 230 VAL 230 230 230 VAL VAL B . n 
B 1 231 GLY 231 231 231 GLY GLY B . n 
B 1 232 PRO 232 232 232 PRO PRO B . n 
B 1 233 MET 233 233 233 MET MET B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 ARG 235 235 235 ARG ARG B . n 
B 1 236 THR 236 236 236 THR THR B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 ALA 238 238 238 ALA ALA B . n 
B 1 239 ASP 239 239 239 ASP ASP B . n 
B 1 240 LEU 240 240 240 LEU LEU B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 ALA 243 243 243 ALA ALA B . n 
B 1 244 LEU 244 244 244 LEU LEU B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 ILE 246 246 246 ILE ILE B . n 
B 1 247 THR 247 247 247 THR THR B . n 
B 1 248 SER 248 248 248 SER SER B . n 
B 1 249 LYS 249 249 249 LYS LYS B . n 
B 1 250 VAL 250 250 250 VAL VAL B . n 
B 1 251 PRO 251 251 251 PRO PRO B . n 
B 1 252 LEU 252 252 252 LEU LEU B . n 
B 1 253 PRO 253 253 253 PRO PRO B . n 
B 1 254 GLN 254 254 254 GLN GLN B . n 
B 1 255 SER 255 255 255 SER SER B . n 
B 1 256 ARG 256 256 256 ARG ARG B . n 
B 1 257 ILE 257 257 257 ILE ILE B . n 
B 1 258 ALA 258 258 258 ALA ALA B . n 
B 1 259 ASN 259 259 259 ASN ASN B . n 
B 1 260 LEU 260 260 260 LEU LEU B . n 
B 1 261 SER 261 261 261 SER SER B . n 
B 1 262 GLY 262 262 262 GLY GLY B . n 
B 1 263 LEU 263 263 263 LEU LEU B . n 
B 1 264 ARG 264 264 264 ARG ARG B . n 
B 1 265 ILE 265 265 265 ILE ILE B . n 
B 1 266 LEU 266 266 266 LEU LEU B . n 
B 1 267 LEU 267 267 267 LEU LEU B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 THR 269 269 269 THR THR B . n 
B 1 270 ALA 270 270 270 ALA ALA B . n 
B 1 271 HIS 271 271 271 HIS HIS B . n 
B 1 272 PRO 272 272 272 PRO PRO B . n 
B 1 273 GLU 273 273 273 GLU GLU B . n 
B 1 274 THR 274 274 274 THR THR B . n 
B 1 275 VAL 275 275 275 VAL VAL B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 ASP 277 277 277 ASP ASP B . n 
B 1 278 SER 278 278 278 SER SER B . n 
B 1 279 ALA 279 279 279 ALA ALA B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 SER 282 282 282 SER SER B . n 
B 1 283 ALA 283 283 283 ALA ALA B . n 
B 1 284 VAL 284 284 284 VAL VAL B . n 
B 1 285 GLU 285 285 285 GLU GLU B . n 
B 1 286 ARG 286 286 286 ARG ARG B . n 
B 1 287 ALA 287 287 287 ALA ALA B . n 
B 1 288 ALA 288 288 288 ALA ALA B . n 
B 1 289 ALA 289 289 289 ALA ALA B . n 
B 1 290 ALA 290 290 290 ALA ALA B . n 
B 1 291 CYS 291 291 291 CYS CYS B . n 
B 1 292 GLU 292 292 292 GLU GLU B . n 
B 1 293 ALA 293 293 293 ALA ALA B . n 
B 1 294 SER 294 294 294 SER SER B . n 
B 1 295 GLY 295 295 295 GLY GLY B . n 
B 1 296 ALA 296 296 296 ALA ALA B . n 
B 1 297 THR 297 297 297 THR THR B . n 
B 1 298 VAL 298 298 298 VAL VAL B . n 
B 1 299 ALA 299 299 299 ALA ALA B . n 
B 1 300 THR 300 300 300 THR THR B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 SER 302 302 302 SER SER B . n 
B 1 303 PRO 303 303 303 PRO PRO B . n 
B 1 304 ASP 304 304 304 ASP ASP B . n 
B 1 305 LEU 305 305 305 LEU LEU B . n 
B 1 306 PRO 306 306 306 PRO PRO B . n 
B 1 307 ASP 307 307 307 ASP ASP B . n 
B 1 308 LEU 308 308 308 LEU LEU B . n 
B 1 309 SER 309 309 309 SER SER B . n 
B 1 310 ALA 310 310 310 ALA ALA B . n 
B 1 311 LEU 311 311 311 LEU LEU B . n 
B 1 312 VAL 312 312 312 VAL VAL B . n 
B 1 313 ALA 313 313 313 ALA ALA B . n 
B 1 314 ASP 314 314 314 ASP ASP B . n 
B 1 315 TYR 315 315 315 TYR TYR B . n 
B 1 316 THR 316 316 316 THR THR B . n 
B 1 317 ARG 317 317 317 ARG ARG B . n 
B 1 318 MET 318 318 318 MET MET B . n 
B 1 319 LEU 319 319 319 LEU LEU B . n 
B 1 320 LEU 320 320 320 LEU LEU B . n 
B 1 321 VAL 321 321 321 VAL VAL B . n 
B 1 322 VAL 322 322 322 VAL VAL B . n 
B 1 323 LEU 323 323 323 LEU LEU B . n 
B 1 324 ALA 324 324 324 ALA ALA B . n 
B 1 325 ARG 325 325 325 ARG ARG B . n 
B 1 326 GLY 326 326 326 GLY GLY B . n 
B 1 327 LEU 327 327 327 LEU LEU B . n 
B 1 328 ALA 328 328 328 ALA ALA B . n 
B 1 329 PRO 329 329 329 PRO PRO B . n 
B 1 330 GLU 330 330 330 GLU GLU B . n 
B 1 331 GLY 331 331 331 GLY GLY B . n 
B 1 332 THR 332 332 332 THR THR B . n 
B 1 333 GLU 333 333 333 GLU GLU B . n 
B 1 334 PRO 334 334 334 PRO PRO B . n 
B 1 335 VAL 335 335 335 VAL VAL B . n 
B 1 336 SER 336 336 336 SER SER B . n 
B 1 337 LEU 337 337 337 LEU LEU B . n 
B 1 338 ASN 338 338 338 ASN ASN B . n 
B 1 339 ALA 339 339 339 ALA ALA B . n 
B 1 340 TRP 340 340 340 TRP TRP B . n 
B 1 341 TYR 341 341 341 TYR TYR B . n 
B 1 342 ALA 342 342 342 ALA ALA B . n 
B 1 343 MET 343 343 343 MET MET B . n 
B 1 344 LEU 344 344 344 LEU LEU B . n 
B 1 345 ASP 345 345 345 ASP ASP B . n 
B 1 346 ASP 346 346 346 ASP ASP B . n 
B 1 347 GLN 347 347 347 GLN GLN B . n 
B 1 348 ALA 348 348 348 ALA ALA B . n 
B 1 349 ARG 349 349 349 ARG ARG B . n 
B 1 350 MET 350 350 350 MET MET B . n 
B 1 351 MET 351 351 351 MET MET B . n 
B 1 352 ARG 352 352 352 ARG ARG B . n 
B 1 353 ALA 353 353 353 ALA ALA B . n 
B 1 354 PHE 354 354 354 PHE PHE B . n 
B 1 355 ASP 355 355 355 ASP ASP B . n 
B 1 356 ARG 356 356 356 ARG ARG B . n 
B 1 357 LEU 357 357 357 LEU LEU B . n 
B 1 358 PHE 358 358 358 PHE PHE B . n 
B 1 359 GLU 359 359 359 GLU GLU B . n 
B 1 360 SER 360 360 360 SER SER B . n 
B 1 361 PHE 361 361 361 PHE PHE B . n 
B 1 362 ASP 362 362 362 ASP ASP B . n 
B 1 363 ALA 363 363 363 ALA ALA B . n 
B 1 364 ILE 364 364 364 ILE ILE B . n 
B 1 365 PHE 365 365 365 PHE PHE B . n 
B 1 366 CYS 366 366 366 CYS CYS B . n 
B 1 367 PRO 367 367 367 PRO PRO B . n 
B 1 368 VAL 368 368 368 VAL VAL B . n 
B 1 369 LEU 369 369 369 LEU LEU B . n 
B 1 370 GLY 370 370 370 GLY GLY B . n 
B 1 371 THR 371 371 371 THR THR B . n 
B 1 372 THR 372 372 372 THR THR B . n 
B 1 373 ALA 373 373 373 ALA ALA B . n 
B 1 374 PHE 374 374 374 PHE PHE B . n 
B 1 375 ALA 375 375 375 ALA ALA B . n 
B 1 376 HIS 376 376 376 HIS HIS B . n 
B 1 377 SER 377 377 377 SER SER B . n 
B 1 378 ASP 378 378 378 ASP ASP B . n 
B 1 379 GLU 379 379 379 GLU GLU B . n 
B 1 380 PRO 380 380 380 PRO PRO B . n 
B 1 381 ASP 381 381 381 ASP ASP B . n 
B 1 382 TRP 382 382 382 TRP TRP B . n 
B 1 383 ALA 383 383 383 ALA ALA B . n 
B 1 384 LYS 384 384 384 LYS LYS B . n 
B 1 385 ARG 385 385 385 ARG ARG B . n 
B 1 386 SER 386 386 386 SER SER B . n 
B 1 387 LEU 387 387 387 LEU LEU B . n 
B 1 388 SER 388 388 388 SER SER B . n 
B 1 389 ILE 389 389 389 ILE ILE B . n 
B 1 390 ASP 390 390 390 ASP ASP B . n 
B 1 391 GLY 391 391 391 GLY GLY B . n 
B 1 392 GLY 392 392 392 GLY GLY B . n 
B 1 393 ILE 393 393 393 ILE ILE B . n 
B 1 394 ALA 394 394 394 ALA ALA B . n 
B 1 395 PRO 395 395 395 PRO PRO B . n 
B 1 396 PHE 396 396 396 PHE PHE B . n 
B 1 397 ALA 397 397 397 ALA ALA B . n 
B 1 398 ALA 398 398 398 ALA ALA B . n 
B 1 399 GLN 399 399 399 GLN GLN B . n 
B 1 400 LEU 400 400 400 LEU LEU B . n 
B 1 401 GLY 401 401 401 GLY GLY B . n 
B 1 402 TRP 402 402 402 TRP TRP B . n 
B 1 403 ILE 403 403 403 ILE ILE B . n 
B 1 404 SER 404 404 404 SER SER B . n 
B 1 405 MET 405 405 405 MET MET B . n 
B 1 406 ALA 406 406 406 ALA ALA B . n 
B 1 407 THR 407 407 407 THR THR B . n 
B 1 408 TYR 408 408 408 TYR TYR B . n 
B 1 409 GLY 409 409 409 GLY GLY B . n 
B 1 410 GLY 410 410 410 GLY GLY B . n 
B 1 411 MET 411 411 411 MET MET B . n 
B 1 412 PRO 412 412 412 PRO PRO B . n 
B 1 413 ALA 413 413 413 ALA ALA B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 SER 415 415 415 SER SER B . n 
B 1 416 MET 416 416 416 MET MET B . n 
B 1 417 PRO 417 417 417 PRO PRO B . n 
B 1 418 LEU 418 418 418 LEU LEU B . n 
B 1 419 GLY 419 419 419 GLY GLY B . n 
B 1 420 ALA 420 420 420 ALA ALA B . n 
B 1 421 ASP 421 421 421 ASP ASP B . n 
B 1 422 GLY 422 422 422 GLY GLY B . n 
B 1 423 ASN 423 423 423 ASN ASN B . n 
B 1 424 GLY 424 424 424 GLY GLY B . n 
B 1 425 LEU 425 425 425 LEU LEU B . n 
B 1 426 PRO 426 426 426 PRO PRO B . n 
B 1 427 ILE 427 427 427 ILE ILE B . n 
B 1 428 ASN 428 428 428 ASN ASN B . n 
B 1 429 LEU 429 429 429 LEU LEU B . n 
B 1 430 GLN 430 430 430 GLN GLN B . n 
B 1 431 ILE 431 431 431 ILE ILE B . n 
B 1 432 ILE 432 432 432 ILE ILE B . n 
B 1 433 THR 433 433 433 THR THR B . n 
B 1 434 ARG 434 434 434 ARG ARG B . n 
B 1 435 ASN 435 435 435 ASN ASN B . n 
B 1 436 TRP 436 436 436 TRP TRP B . n 
B 1 437 SER 437 437 437 SER SER B . n 
B 1 438 ASP 438 438 438 ASP ASP B . n 
B 1 439 HIS 439 439 439 HIS HIS B . n 
B 1 440 ASP 440 440 440 ASP ASP B . n 
B 1 441 ALA 441 441 441 ALA ALA B . n 
B 1 442 ILE 442 442 442 ILE ILE B . n 
B 1 443 ARG 443 443 443 ARG ARG B . n 
B 1 444 ILE 444 444 444 ILE ILE B . n 
B 1 445 GLY 445 445 445 GLY GLY B . n 
B 1 446 ALA 446 446 446 ALA ALA B . n 
B 1 447 LEU 447 447 447 LEU LEU B . n 
B 1 448 VAL 448 448 448 VAL VAL B . n 
B 1 449 ALA 449 449 449 ALA ALA B . n 
B 1 450 GLU 450 450 450 GLU GLU B . n 
B 1 451 ALA 451 451 451 ALA ALA B . n 
B 1 452 LEU 452 452 452 LEU LEU B . n 
B 1 453 ASP 453 453 453 ASP ASP B . n 
B 1 454 ARG 454 454 454 ARG ARG B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1D5H 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1D5H 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1D5H 1   501 501 A1D5H BBC A . 
D 2 A1D5H 1   501 501 A1D5H BBC B . 
E 3 HOH   1   601 216 HOH   HOH A . 
E 3 HOH   2   602 180 HOH   HOH A . 
E 3 HOH   3   603 237 HOH   HOH A . 
E 3 HOH   4   604 91  HOH   HOH A . 
E 3 HOH   5   605 231 HOH   HOH A . 
E 3 HOH   6   606 58  HOH   HOH A . 
E 3 HOH   7   607 56  HOH   HOH A . 
E 3 HOH   8   608 158 HOH   HOH A . 
E 3 HOH   9   609 105 HOH   HOH A . 
E 3 HOH   10  610 77  HOH   HOH A . 
E 3 HOH   11  611 67  HOH   HOH A . 
E 3 HOH   12  612 13  HOH   HOH A . 
E 3 HOH   13  613 144 HOH   HOH A . 
E 3 HOH   14  614 90  HOH   HOH A . 
E 3 HOH   15  615 55  HOH   HOH A . 
E 3 HOH   16  616 159 HOH   HOH A . 
E 3 HOH   17  617 37  HOH   HOH A . 
E 3 HOH   18  618 75  HOH   HOH A . 
E 3 HOH   19  619 92  HOH   HOH A . 
E 3 HOH   20  620 186 HOH   HOH A . 
E 3 HOH   21  621 175 HOH   HOH A . 
E 3 HOH   22  622 200 HOH   HOH A . 
E 3 HOH   23  623 74  HOH   HOH A . 
E 3 HOH   24  624 11  HOH   HOH A . 
E 3 HOH   25  625 177 HOH   HOH A . 
E 3 HOH   26  626 18  HOH   HOH A . 
E 3 HOH   27  627 14  HOH   HOH A . 
E 3 HOH   28  628 163 HOH   HOH A . 
E 3 HOH   29  629 19  HOH   HOH A . 
E 3 HOH   30  630 169 HOH   HOH A . 
E 3 HOH   31  631 201 HOH   HOH A . 
E 3 HOH   32  632 49  HOH   HOH A . 
E 3 HOH   33  633 243 HOH   HOH A . 
E 3 HOH   34  634 81  HOH   HOH A . 
E 3 HOH   35  635 46  HOH   HOH A . 
E 3 HOH   36  636 137 HOH   HOH A . 
E 3 HOH   37  637 45  HOH   HOH A . 
E 3 HOH   38  638 143 HOH   HOH A . 
E 3 HOH   39  639 26  HOH   HOH A . 
E 3 HOH   40  640 219 HOH   HOH A . 
E 3 HOH   41  641 172 HOH   HOH A . 
E 3 HOH   42  642 127 HOH   HOH A . 
E 3 HOH   43  643 68  HOH   HOH A . 
E 3 HOH   44  644 204 HOH   HOH A . 
E 3 HOH   45  645 109 HOH   HOH A . 
E 3 HOH   46  646 136 HOH   HOH A . 
E 3 HOH   47  647 96  HOH   HOH A . 
E 3 HOH   48  648 185 HOH   HOH A . 
E 3 HOH   49  649 190 HOH   HOH A . 
E 3 HOH   50  650 43  HOH   HOH A . 
E 3 HOH   51  651 44  HOH   HOH A . 
E 3 HOH   52  652 156 HOH   HOH A . 
E 3 HOH   53  653 52  HOH   HOH A . 
E 3 HOH   54  654 84  HOH   HOH A . 
E 3 HOH   55  655 138 HOH   HOH A . 
E 3 HOH   56  656 47  HOH   HOH A . 
E 3 HOH   57  657 140 HOH   HOH A . 
E 3 HOH   58  658 173 HOH   HOH A . 
E 3 HOH   59  659 25  HOH   HOH A . 
E 3 HOH   60  660 82  HOH   HOH A . 
E 3 HOH   61  661 64  HOH   HOH A . 
E 3 HOH   62  662 39  HOH   HOH A . 
E 3 HOH   63  663 33  HOH   HOH A . 
E 3 HOH   64  664 73  HOH   HOH A . 
E 3 HOH   65  665 50  HOH   HOH A . 
E 3 HOH   66  666 193 HOH   HOH A . 
E 3 HOH   67  667 106 HOH   HOH A . 
E 3 HOH   68  668 63  HOH   HOH A . 
E 3 HOH   69  669 8   HOH   HOH A . 
E 3 HOH   70  670 86  HOH   HOH A . 
E 3 HOH   71  671 27  HOH   HOH A . 
E 3 HOH   72  672 112 HOH   HOH A . 
E 3 HOH   73  673 23  HOH   HOH A . 
E 3 HOH   74  674 155 HOH   HOH A . 
E 3 HOH   75  675 99  HOH   HOH A . 
E 3 HOH   76  676 220 HOH   HOH A . 
E 3 HOH   77  677 117 HOH   HOH A . 
E 3 HOH   78  678 246 HOH   HOH A . 
E 3 HOH   79  679 176 HOH   HOH A . 
E 3 HOH   80  680 147 HOH   HOH A . 
E 3 HOH   81  681 69  HOH   HOH A . 
E 3 HOH   82  682 87  HOH   HOH A . 
E 3 HOH   83  683 132 HOH   HOH A . 
E 3 HOH   84  684 85  HOH   HOH A . 
E 3 HOH   85  685 167 HOH   HOH A . 
E 3 HOH   86  686 149 HOH   HOH A . 
E 3 HOH   87  687 187 HOH   HOH A . 
E 3 HOH   88  688 188 HOH   HOH A . 
E 3 HOH   89  689 228 HOH   HOH A . 
E 3 HOH   90  690 183 HOH   HOH A . 
E 3 HOH   91  691 129 HOH   HOH A . 
E 3 HOH   92  692 240 HOH   HOH A . 
E 3 HOH   93  693 114 HOH   HOH A . 
E 3 HOH   94  694 242 HOH   HOH A . 
E 3 HOH   95  695 162 HOH   HOH A . 
E 3 HOH   96  696 62  HOH   HOH A . 
E 3 HOH   97  697 248 HOH   HOH A . 
E 3 HOH   98  698 229 HOH   HOH A . 
E 3 HOH   99  699 241 HOH   HOH A . 
E 3 HOH   100 700 195 HOH   HOH A . 
E 3 HOH   101 701 3   HOH   HOH A . 
E 3 HOH   102 702 211 HOH   HOH A . 
E 3 HOH   103 703 60  HOH   HOH A . 
E 3 HOH   104 704 35  HOH   HOH A . 
E 3 HOH   105 705 151 HOH   HOH A . 
E 3 HOH   106 706 214 HOH   HOH A . 
E 3 HOH   107 707 230 HOH   HOH A . 
E 3 HOH   108 708 191 HOH   HOH A . 
E 3 HOH   109 709 157 HOH   HOH A . 
E 3 HOH   110 710 148 HOH   HOH A . 
E 3 HOH   111 711 181 HOH   HOH A . 
E 3 HOH   112 712 247 HOH   HOH A . 
E 3 HOH   113 713 161 HOH   HOH A . 
E 3 HOH   114 714 223 HOH   HOH A . 
E 3 HOH   115 715 166 HOH   HOH A . 
E 3 HOH   116 716 17  HOH   HOH A . 
F 3 HOH   1   601 70  HOH   HOH B . 
F 3 HOH   2   602 20  HOH   HOH B . 
F 3 HOH   3   603 53  HOH   HOH B . 
F 3 HOH   4   604 115 HOH   HOH B . 
F 3 HOH   5   605 83  HOH   HOH B . 
F 3 HOH   6   606 21  HOH   HOH B . 
F 3 HOH   7   607 141 HOH   HOH B . 
F 3 HOH   8   608 29  HOH   HOH B . 
F 3 HOH   9   609 71  HOH   HOH B . 
F 3 HOH   10  610 93  HOH   HOH B . 
F 3 HOH   11  611 16  HOH   HOH B . 
F 3 HOH   12  612 103 HOH   HOH B . 
F 3 HOH   13  613 97  HOH   HOH B . 
F 3 HOH   14  614 95  HOH   HOH B . 
F 3 HOH   15  615 152 HOH   HOH B . 
F 3 HOH   16  616 164 HOH   HOH B . 
F 3 HOH   17  617 178 HOH   HOH B . 
F 3 HOH   18  618 42  HOH   HOH B . 
F 3 HOH   19  619 108 HOH   HOH B . 
F 3 HOH   20  620 34  HOH   HOH B . 
F 3 HOH   21  621 222 HOH   HOH B . 
F 3 HOH   22  622 139 HOH   HOH B . 
F 3 HOH   23  623 89  HOH   HOH B . 
F 3 HOH   24  624 94  HOH   HOH B . 
F 3 HOH   25  625 6   HOH   HOH B . 
F 3 HOH   26  626 165 HOH   HOH B . 
F 3 HOH   27  627 2   HOH   HOH B . 
F 3 HOH   28  628 66  HOH   HOH B . 
F 3 HOH   29  629 194 HOH   HOH B . 
F 3 HOH   30  630 128 HOH   HOH B . 
F 3 HOH   31  631 41  HOH   HOH B . 
F 3 HOH   32  632 107 HOH   HOH B . 
F 3 HOH   33  633 78  HOH   HOH B . 
F 3 HOH   34  634 134 HOH   HOH B . 
F 3 HOH   35  635 170 HOH   HOH B . 
F 3 HOH   36  636 118 HOH   HOH B . 
F 3 HOH   37  637 215 HOH   HOH B . 
F 3 HOH   38  638 126 HOH   HOH B . 
F 3 HOH   39  639 101 HOH   HOH B . 
F 3 HOH   40  640 225 HOH   HOH B . 
F 3 HOH   41  641 54  HOH   HOH B . 
F 3 HOH   42  642 79  HOH   HOH B . 
F 3 HOH   43  643 10  HOH   HOH B . 
F 3 HOH   44  644 1   HOH   HOH B . 
F 3 HOH   45  645 12  HOH   HOH B . 
F 3 HOH   46  646 182 HOH   HOH B . 
F 3 HOH   47  647 244 HOH   HOH B . 
F 3 HOH   48  648 111 HOH   HOH B . 
F 3 HOH   49  649 153 HOH   HOH B . 
F 3 HOH   50  650 120 HOH   HOH B . 
F 3 HOH   51  651 24  HOH   HOH B . 
F 3 HOH   52  652 113 HOH   HOH B . 
F 3 HOH   53  653 7   HOH   HOH B . 
F 3 HOH   54  654 15  HOH   HOH B . 
F 3 HOH   55  655 28  HOH   HOH B . 
F 3 HOH   56  656 121 HOH   HOH B . 
F 3 HOH   57  657 4   HOH   HOH B . 
F 3 HOH   58  658 236 HOH   HOH B . 
F 3 HOH   59  659 104 HOH   HOH B . 
F 3 HOH   60  660 59  HOH   HOH B . 
F 3 HOH   61  661 203 HOH   HOH B . 
F 3 HOH   62  662 31  HOH   HOH B . 
F 3 HOH   63  663 124 HOH   HOH B . 
F 3 HOH   64  664 100 HOH   HOH B . 
F 3 HOH   65  665 125 HOH   HOH B . 
F 3 HOH   66  666 38  HOH   HOH B . 
F 3 HOH   67  667 202 HOH   HOH B . 
F 3 HOH   68  668 122 HOH   HOH B . 
F 3 HOH   69  669 189 HOH   HOH B . 
F 3 HOH   70  670 80  HOH   HOH B . 
F 3 HOH   71  671 123 HOH   HOH B . 
F 3 HOH   72  672 198 HOH   HOH B . 
F 3 HOH   73  673 227 HOH   HOH B . 
F 3 HOH   74  674 235 HOH   HOH B . 
F 3 HOH   75  675 245 HOH   HOH B . 
F 3 HOH   76  676 184 HOH   HOH B . 
F 3 HOH   77  677 205 HOH   HOH B . 
F 3 HOH   78  678 210 HOH   HOH B . 
F 3 HOH   79  679 174 HOH   HOH B . 
F 3 HOH   80  680 208 HOH   HOH B . 
F 3 HOH   81  681 252 HOH   HOH B . 
F 3 HOH   82  682 22  HOH   HOH B . 
F 3 HOH   83  683 250 HOH   HOH B . 
F 3 HOH   84  684 249 HOH   HOH B . 
F 3 HOH   85  685 116 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    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                     8XTB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.936 
_cell.length_a_esd                 ? 
_cell.length_b                     84.936 
_cell.length_b_esd                 ? 
_cell.length_c                     275.819 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         8XTB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_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                   8XTB 
_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             2.64 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.47 
_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    '1.26M (NH4)2SO4, 0.1M HEPES pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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         2023-09-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979183 
_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                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979183 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XTB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.35 
_reflns.d_resolution_low                               50 
_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                                     43036 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                17.0 
_reflns.pdbx_netI_over_av_sigmaI                       10.2 
_reflns.pdbx_netI_over_sigmaI                          7.68 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.35 2.5  ? 2.2 ? ? ? ? 12905 ? ? ? ? ? ? ? ? ? ? ? 16.2 ? ? ? ? ? ? 1 1 0.696 ? ? 99.6 ? ?     ? ? ? ? ? ? ? ? ? 
2.50 2.67 ? ?   ? ? ? ? 12094 ? ? ? ? ? ? ? ? ? ? ? ?    ? ? ? ? ? ? 2 1 0.84  ? ? ?    ? 0.917 ? ? ? ? ? ? ? ? ? 
2.67 2.88 ? ?   ? ? ? ? 11264 ? ? ? ? ? ? ? ? ? ? ? ?    ? ? ? ? ? ? 3 1 0.909 ? ? ?    ? ?     ? ? ? ? ? ? ? ? ? 
2.88 3.15 ? ?   ? ? ? ? 10445 ? ? ? ? ? ? ? ? ? ? ? ?    ? ? ? ? ? ? 4 1 0.96  ? ? ?    ? ?     ? ? ? ? ? ? ? ? ? 
3.15 3.52 ? ?   ? ? ? ? 9372  ? ? ? ? ? ? ? ? ? ? ? ?    ? ? ? ? ? ? 5 1 0.976 ? ? ?    ? ?     ? ? ? ? ? ? ? ? ? 
3.52 4.07 ? ?   ? ? ? ? 8275  ? ? ? ? ? ? ? ? ? ? ? ?    ? ? ? ? ? ? 6 1 0.99  ? ? ?    ? ?     ? ? ? ? ? ? ? ? ? 
4.07 4.97 ? ?   ? ? ? ? 7021  ? ? ? ? ? ? ? ? ? ? ? ?    ? ? ? ? ? ? 7 1 0.992 ? ? ?    ? ?     ? ? ? ? ? ? ? ? ? 
4.97 6.99 ? ?   ? ? ? ? 5429  ? ? ? ? ? ? ? ? ? ? ? ?    ? ? ? ? ? ? 8 1 0.992 ? ? ?    ? ?     ? ? ? ? ? ? ? ? ? 
6.99 50   ? ?   ? ? ? ? 3022  ? ? ? ? ? ? ? ? ? ? ? ?    ? ? ? ? ? ? 9 1 0.996 ? ? ?    ? ?     ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 8XTB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.35 
_refine.ls_d_res_low                             19.23 
_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                     42847 
_refine.ls_number_reflns_R_free                  2143 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2083 
_refine.ls_R_factor_R_free                       0.2425 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2066 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.34 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 25.29 
_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                             ? 
_refine.overall_SU_ML                            0.35 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.35 
_refine_hist.d_res_low                        19.23 
_refine_hist.number_atoms_solvent             201 
_refine_hist.number_atoms_total               6637 
_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        6404 
_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' ? 0.003 ? 6568 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.617 ? 8954 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.210 ? 942  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.043 ? 1034 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 1178 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_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 
_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 
'X-RAY DIFFRACTION' 2.35 2.44  . . 209 3977 100.00 . . . . 0.2904 . . . . . . . . . . . 0.3303 
'X-RAY DIFFRACTION' 2.44 2.54  . . 210 3981 100.00 . . . . 0.2644 . . . . . . . . . . . 0.3230 
'X-RAY DIFFRACTION' 2.54 2.65  . . 210 4005 100.00 . . . . 0.2617 . . . . . . . . . . . 0.2742 
'X-RAY DIFFRACTION' 2.65 2.79  . . 212 4013 100.00 . . . . 0.2503 . . . . . . . . . . . 0.3174 
'X-RAY DIFFRACTION' 2.79 2.96  . . 211 4019 100.00 . . . . 0.2509 . . . . . . . . . . . 0.3147 
'X-RAY DIFFRACTION' 2.96 3.19  . . 212 4033 100.00 . . . . 0.2440 . . . . . . . . . . . 0.2696 
'X-RAY DIFFRACTION' 3.19 3.51  . . 215 4072 100.00 . . . . 0.2184 . . . . . . . . . . . 0.2439 
'X-RAY DIFFRACTION' 3.51 4.01  . . 216 4097 100.00 . . . . 0.1892 . . . . . . . . . . . 0.2297 
'X-RAY DIFFRACTION' 4.02 5.04  . . 218 4147 100.00 . . . . 0.1654 . . . . . . . . . . . 0.1976 
'X-RAY DIFFRACTION' 5.04 19.23 . . 230 4360 100.00 . . . . 0.1773 . . . . . . . . . . . 0.2064 
# 
_struct.entry_id                     8XTB 
_struct.title                        
'Crystal structure of a novel PU plastic degradation urethanase UMG-SP2 from uncultured bacterium in complex with ligand' 
_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        8XTB 
_struct_keywords.text            'PU, degradation, mutant, 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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8XTB 
_struct_ref.pdbx_db_accession          8XTB 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8XTB A 1 ? 454 ? 8XTB 1 ? 454 ? 1 454 
2 1 8XTB B 1 ? 454 ? 8XTB 1 ? 454 ? 1 454 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2420  ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  30330 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 20  ? GLY A 30  ? SER A 20  GLY A 30  1 ? 11 
HELX_P HELX_P2  AA2 THR A 34  ? ASP A 50  ? THR A 34  ASP A 50  1 ? 17 
HELX_P HELX_P3  AA3 ASP A 60  ? ALA A 77  ? ASP A 60  ALA A 77  1 ? 18 
HELX_P HELX_P4  AA4 PHE A 105 ? ALA A 109 ? PHE A 105 ALA A 109 5 ? 5  
HELX_P HELX_P5  AA5 SER A 117 ? ALA A 126 ? SER A 117 ALA A 126 1 ? 10 
HELX_P HELX_P6  AA6 PRO A 137 ? ALA A 141 ? PRO A 137 ALA A 141 5 ? 5  
HELX_P HELX_P7  AA7 SER A 167 ? ALA A 176 ? SER A 167 ALA A 176 1 ? 10 
HELX_P HELX_P8  AA8 ILE A 191 ? GLY A 199 ? ILE A 191 GLY A 199 1 ? 9  
HELX_P HELX_P9  AA9 THR A 236 ? SER A 248 ? THR A 236 SER A 248 1 ? 13 
HELX_P HELX_P10 AB1 ASP A 277 ? ALA A 293 ? ASP A 277 ALA A 293 1 ? 17 
HELX_P HELX_P11 AB2 ASP A 307 ? ALA A 324 ? ASP A 307 ALA A 324 1 ? 18 
HELX_P HELX_P12 AB3 ALA A 328 ? THR A 332 ? ALA A 328 THR A 332 5 ? 5  
HELX_P HELX_P13 AB4 SER A 336 ? PHE A 361 ? SER A 336 PHE A 361 1 ? 26 
HELX_P HELX_P14 AB5 ASP A 381 ? LYS A 384 ? ASP A 381 LYS A 384 5 ? 4  
HELX_P HELX_P15 AB6 GLN A 399 ? GLY A 410 ? GLN A 399 GLY A 410 1 ? 12 
HELX_P HELX_P16 AB7 SER A 437 ? ARG A 454 ? SER A 437 ARG A 454 1 ? 18 
HELX_P HELX_P17 AB8 SER B 20  ? GLY B 30  ? SER B 20  GLY B 30  1 ? 11 
HELX_P HELX_P18 AB9 THR B 34  ? ASN B 54  ? THR B 34  ASN B 54  1 ? 21 
HELX_P HELX_P19 AC1 ASP B 60  ? ALA B 76  ? ASP B 60  ALA B 76  1 ? 17 
HELX_P HELX_P20 AC2 PHE B 105 ? ALA B 109 ? PHE B 105 ALA B 109 5 ? 5  
HELX_P HELX_P21 AC3 SER B 117 ? ALA B 126 ? SER B 117 ALA B 126 1 ? 10 
HELX_P HELX_P22 AC4 PRO B 137 ? ALA B 141 ? PRO B 137 ALA B 141 5 ? 5  
HELX_P HELX_P23 AC5 SER B 167 ? ALA B 176 ? SER B 167 ALA B 176 1 ? 10 
HELX_P HELX_P24 AC6 ILE B 191 ? GLY B 199 ? ILE B 191 GLY B 199 1 ? 9  
HELX_P HELX_P25 AC7 THR B 236 ? SER B 248 ? THR B 236 SER B 248 1 ? 13 
HELX_P HELX_P26 AC8 ASP B 277 ? ALA B 293 ? ASP B 277 ALA B 293 1 ? 17 
HELX_P HELX_P27 AC9 ASP B 307 ? ALA B 324 ? ASP B 307 ALA B 324 1 ? 18 
HELX_P HELX_P28 AD1 SER B 336 ? PHE B 358 ? SER B 336 PHE B 358 1 ? 23 
HELX_P HELX_P29 AD2 ASP B 381 ? LYS B 384 ? ASP B 381 LYS B 384 5 ? 4  
HELX_P HELX_P30 AD3 GLN B 399 ? GLY B 410 ? GLN B 399 GLY B 410 1 ? 12 
HELX_P HELX_P31 AD4 SER B 437 ? LEU B 452 ? SER B 437 LEU B 452 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 8 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
AA8 ? 8 ? 
AA9 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? parallel      
AA4 7 8 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 6 7 ? parallel      
AA8 7 8 ? parallel      
AA9 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 56  ? ARG A 59  ? VAL A 56  ARG A 59  
AA1 2 VAL A 129 ? SER A 134 ? VAL A 129 SER A 134 
AA1 3 PRO A 87  ? LYS A 91  ? PRO A 87  LYS A 91  
AA2 1 VAL A 146 ? ASN A 147 ? VAL A 146 ASN A 147 
AA2 2 GLY A 151 ? ARG A 152 ? GLY A 151 ARG A 152 
AA3 1 ASN A 154 ? ASN A 155 ? ASN A 154 ASN A 155 
AA3 2 ASP A 158 ? SER A 162 ? ASP A 158 SER A 162 
AA4 1 LEU A 181 ? ASP A 186 ? LEU A 181 ASP A 186 
AA4 2 VAL A 229 ? ALA A 234 ? VAL A 229 ALA A 234 
AA4 3 TRP A 201 ? LYS A 204 ? TRP A 201 LYS A 204 
AA4 4 ALA A 413 ? ALA A 420 ? ALA A 413 ALA A 420 
AA4 5 PRO A 426 ? ILE A 432 ? PRO A 426 ILE A 432 
AA4 6 ALA A 363 ? PRO A 367 ? ALA A 363 PRO A 367 
AA4 7 ARG A 264 ? LEU A 267 ? ARG A 264 LEU A 267 
AA4 8 THR A 297 ? ALA A 299 ? THR A 297 ALA A 299 
AA5 1 SER A 386 ? ILE A 389 ? SER A 386 ILE A 389 
AA5 2 GLY A 392 ? PRO A 395 ? GLY A 392 PRO A 395 
AA6 1 VAL B 56  ? ARG B 59  ? VAL B 56  ARG B 59  
AA6 2 VAL B 129 ? SER B 134 ? VAL B 129 SER B 134 
AA6 3 PRO B 87  ? LYS B 91  ? PRO B 87  LYS B 91  
AA7 1 VAL B 146 ? ASN B 147 ? VAL B 146 ASN B 147 
AA7 2 GLY B 151 ? ARG B 152 ? GLY B 151 ARG B 152 
AA8 1 LEU B 181 ? ASP B 186 ? LEU B 181 ASP B 186 
AA8 2 VAL B 229 ? ALA B 234 ? VAL B 229 ALA B 234 
AA8 3 TRP B 201 ? LYS B 204 ? TRP B 201 LYS B 204 
AA8 4 ALA B 413 ? ALA B 420 ? ALA B 413 ALA B 420 
AA8 5 PRO B 426 ? ILE B 432 ? PRO B 426 ILE B 432 
AA8 6 ALA B 363 ? PRO B 367 ? ALA B 363 PRO B 367 
AA8 7 ARG B 264 ? LEU B 267 ? ARG B 264 LEU B 267 
AA8 8 THR B 297 ? ALA B 299 ? THR B 297 ALA B 299 
AA9 1 SER B 386 ? ILE B 389 ? SER B 386 ILE B 389 
AA9 2 GLY B 392 ? PRO B 395 ? GLY B 392 PRO B 395 
# 
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 VAL A 58  ? N VAL A 58  O LYS A 133 ? O LYS A 133 
AA1 2 3 O LEU A 131 ? O LEU A 131 N MET A 88  ? N MET A 88  
AA2 1 2 N ASN A 147 ? N ASN A 147 O GLY A 151 ? O GLY A 151 
AA3 1 2 N ASN A 155 ? N ASN A 155 O ARG A 161 ? O ARG A 161 
AA4 1 2 N ASP A 186 ? N ASP A 186 O VAL A 229 ? O VAL A 229 
AA4 2 3 O ALA A 234 ? O ALA A 234 N TRP A 201 ? N TRP A 201 
AA4 3 4 N GLY A 202 ? N GLY A 202 O SER A 415 ? O SER A 415 
AA4 4 5 N GLY A 419 ? N GLY A 419 O ILE A 427 ? O ILE A 427 
AA4 5 6 O ILE A 432 ? O ILE A 432 N ILE A 364 ? N ILE A 364 
AA4 6 7 O PHE A 365 ? O PHE A 365 N LEU A 266 ? N LEU A 266 
AA4 7 8 N LEU A 267 ? N LEU A 267 O ALA A 299 ? O ALA A 299 
AA5 1 2 N ILE A 389 ? N ILE A 389 O GLY A 392 ? O GLY A 392 
AA6 1 2 N VAL B 58  ? N VAL B 58  O LYS B 133 ? O LYS B 133 
AA6 2 3 O LEU B 131 ? O LEU B 131 N MET B 88  ? N MET B 88  
AA7 1 2 N ASN B 147 ? N ASN B 147 O GLY B 151 ? O GLY B 151 
AA8 1 2 N GLU B 182 ? N GLU B 182 O MET B 233 ? O MET B 233 
AA8 2 3 O ALA B 234 ? O ALA B 234 N TRP B 201 ? N TRP B 201 
AA8 3 4 N LYS B 204 ? N LYS B 204 O ALA B 413 ? O ALA B 413 
AA8 4 5 N LEU B 418 ? N LEU B 418 O ILE B 427 ? O ILE B 427 
AA8 5 6 O ILE B 432 ? O ILE B 432 N ILE B 364 ? N ILE B 364 
AA8 6 7 O PHE B 365 ? O PHE B 365 N LEU B 266 ? N LEU B 266 
AA8 7 8 N LEU B 267 ? N LEU B 267 O ALA B 299 ? O ALA B 299 
AA9 1 2 N ILE B 389 ? N ILE B 389 O GLY B 392 ? O GLY B 392 
# 
_pdbx_entry_details.entry_id                   8XTB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 54  ? ? 62.50   62.07  
2 1 ASP A 158 ? ? -164.07 108.18 
3 1 SER A 166 ? ? 73.29   -57.71 
4 1 LEU A 227 ? ? 70.33   -22.54 
5 1 SER A 437 ? ? -103.26 47.95  
6 1 TRP B 143 ? ? -98.51  32.31  
7 1 SER B 166 ? ? 88.68   -20.07 
8 1 ASP B 453 ? ? -132.26 -32.48 
# 
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 ASN 1  ? A ASN 1  
2  1 Y 1 A LEU 2  ? A LEU 2  
3  1 Y 1 A TYR 3  ? A TYR 3  
4  1 Y 1 A PHE 4  ? A PHE 4  
5  1 Y 1 A GLN 5  ? A GLN 5  
6  1 Y 1 A GLY 6  ? A GLY 6  
7  1 Y 1 A ALA 7  ? A ALA 7  
8  1 Y 1 A GLY 8  ? A GLY 8  
9  1 Y 1 A ALA 9  ? A ALA 9  
10 1 Y 1 A GLY 10 ? A GLY 10 
11 1 Y 1 A ALA 11 ? A ALA 11 
12 1 Y 1 A GLY 12 ? A GLY 12 
13 1 Y 1 A ALA 13 ? A ALA 13 
14 1 Y 1 A GLY 14 ? A GLY 14 
15 1 Y 1 A ALA 15 ? A ALA 15 
16 1 Y 1 A MET 16 ? A MET 16 
17 1 Y 1 B ASN 1  ? B ASN 1  
18 1 Y 1 B LEU 2  ? B LEU 2  
19 1 Y 1 B TYR 3  ? B TYR 3  
20 1 Y 1 B PHE 4  ? B PHE 4  
21 1 Y 1 B GLN 5  ? B GLN 5  
22 1 Y 1 B GLY 6  ? B GLY 6  
23 1 Y 1 B ALA 7  ? B ALA 7  
24 1 Y 1 B GLY 8  ? B GLY 8  
25 1 Y 1 B ALA 9  ? B ALA 9  
26 1 Y 1 B GLY 10 ? B GLY 10 
27 1 Y 1 B ALA 11 ? B ALA 11 
28 1 Y 1 B GLY 12 ? B GLY 12 
29 1 Y 1 B ALA 13 ? B ALA 13 
30 1 Y 1 B GLY 14 ? B GLY 14 
31 1 Y 1 B ALA 15 ? B ALA 15 
32 1 Y 1 B MET 16 ? B MET 16 
# 
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 
A1D5H C05  C Y N 1   
A1D5H C09  C N N 2   
A1D5H C10  C N N 3   
A1D5H C02  C Y N 4   
A1D5H C03  C Y N 5   
A1D5H C04  C Y N 6   
A1D5H C07  C N N 7   
A1D5H C11  C N N 8   
A1D5H C12  C N N 9   
A1D5H C15  C Y N 10  
A1D5H C16  C Y N 11  
A1D5H N01  N N N 12  
A1D5H N06  N N N 13  
A1D5H O08  O N N 14  
A1D5H O13  O N N 15  
A1D5H O14  O N N 16  
A1D5H H1   H N N 17  
A1D5H H2   H N N 18  
A1D5H H3   H N N 19  
A1D5H H4   H N N 20  
A1D5H H5   H N N 21  
A1D5H H6   H N N 22  
A1D5H H7   H N N 23  
A1D5H H8   H N N 24  
A1D5H H9   H N N 25  
A1D5H H10  H N N 26  
A1D5H H11  H N N 27  
A1D5H H12  H N N 28  
A1D5H H13  H N N 29  
A1D5H H14  H N N 30  
A1D5H H15  H N N 31  
A1D5H H16  H N N 32  
ALA   N    N N N 33  
ALA   CA   C N S 34  
ALA   C    C N N 35  
ALA   O    O N N 36  
ALA   CB   C N N 37  
ALA   OXT  O N N 38  
ALA   H    H N N 39  
ALA   H2   H N N 40  
ALA   HA   H N N 41  
ALA   HB1  H N N 42  
ALA   HB2  H N N 43  
ALA   HB3  H N N 44  
ALA   HXT  H N N 45  
ARG   N    N N N 46  
ARG   CA   C N S 47  
ARG   C    C N N 48  
ARG   O    O N N 49  
ARG   CB   C N N 50  
ARG   CG   C N N 51  
ARG   CD   C N N 52  
ARG   NE   N N N 53  
ARG   CZ   C N N 54  
ARG   NH1  N N N 55  
ARG   NH2  N N N 56  
ARG   OXT  O N N 57  
ARG   H    H N N 58  
ARG   H2   H N N 59  
ARG   HA   H N N 60  
ARG   HB2  H N N 61  
ARG   HB3  H N N 62  
ARG   HG2  H N N 63  
ARG   HG3  H N N 64  
ARG   HD2  H N N 65  
ARG   HD3  H N N 66  
ARG   HE   H N N 67  
ARG   HH11 H N N 68  
ARG   HH12 H N N 69  
ARG   HH21 H N N 70  
ARG   HH22 H N N 71  
ARG   HXT  H N N 72  
ASN   N    N N N 73  
ASN   CA   C N S 74  
ASN   C    C N N 75  
ASN   O    O N N 76  
ASN   CB   C N N 77  
ASN   CG   C N N 78  
ASN   OD1  O N N 79  
ASN   ND2  N N N 80  
ASN   OXT  O N N 81  
ASN   H    H N N 82  
ASN   H2   H N N 83  
ASN   HA   H N N 84  
ASN   HB2  H N N 85  
ASN   HB3  H N N 86  
ASN   HD21 H N N 87  
ASN   HD22 H N N 88  
ASN   HXT  H N N 89  
ASP   N    N N N 90  
ASP   CA   C N S 91  
ASP   C    C N N 92  
ASP   O    O N N 93  
ASP   CB   C N N 94  
ASP   CG   C N N 95  
ASP   OD1  O N N 96  
ASP   OD2  O N N 97  
ASP   OXT  O N N 98  
ASP   H    H N N 99  
ASP   H2   H N N 100 
ASP   HA   H N N 101 
ASP   HB2  H N N 102 
ASP   HB3  H N N 103 
ASP   HD2  H N N 104 
ASP   HXT  H N N 105 
CYS   N    N N N 106 
CYS   CA   C N R 107 
CYS   C    C N N 108 
CYS   O    O N N 109 
CYS   CB   C N N 110 
CYS   SG   S N N 111 
CYS   OXT  O N N 112 
CYS   H    H N N 113 
CYS   H2   H N N 114 
CYS   HA   H N N 115 
CYS   HB2  H N N 116 
CYS   HB3  H N N 117 
CYS   HG   H N N 118 
CYS   HXT  H N N 119 
GLN   N    N N N 120 
GLN   CA   C N S 121 
GLN   C    C N N 122 
GLN   O    O N N 123 
GLN   CB   C N N 124 
GLN   CG   C N N 125 
GLN   CD   C N N 126 
GLN   OE1  O N N 127 
GLN   NE2  N N N 128 
GLN   OXT  O N N 129 
GLN   H    H N N 130 
GLN   H2   H N N 131 
GLN   HA   H N N 132 
GLN   HB2  H N N 133 
GLN   HB3  H N N 134 
GLN   HG2  H N N 135 
GLN   HG3  H N N 136 
GLN   HE21 H N N 137 
GLN   HE22 H N N 138 
GLN   HXT  H N N 139 
GLU   N    N N N 140 
GLU   CA   C N S 141 
GLU   C    C N N 142 
GLU   O    O N N 143 
GLU   CB   C N N 144 
GLU   CG   C N N 145 
GLU   CD   C N N 146 
GLU   OE1  O N N 147 
GLU   OE2  O N N 148 
GLU   OXT  O N N 149 
GLU   H    H N N 150 
GLU   H2   H N N 151 
GLU   HA   H N N 152 
GLU   HB2  H N N 153 
GLU   HB3  H N N 154 
GLU   HG2  H N N 155 
GLU   HG3  H N N 156 
GLU   HE2  H N N 157 
GLU   HXT  H N N 158 
GLY   N    N N N 159 
GLY   CA   C N N 160 
GLY   C    C N N 161 
GLY   O    O N N 162 
GLY   OXT  O N N 163 
GLY   H    H N N 164 
GLY   H2   H N N 165 
GLY   HA2  H N N 166 
GLY   HA3  H N N 167 
GLY   HXT  H N N 168 
HIS   N    N N N 169 
HIS   CA   C N S 170 
HIS   C    C N N 171 
HIS   O    O N N 172 
HIS   CB   C N N 173 
HIS   CG   C Y N 174 
HIS   ND1  N Y N 175 
HIS   CD2  C Y N 176 
HIS   CE1  C Y N 177 
HIS   NE2  N Y N 178 
HIS   OXT  O N N 179 
HIS   H    H N N 180 
HIS   H2   H N N 181 
HIS   HA   H N N 182 
HIS   HB2  H N N 183 
HIS   HB3  H N N 184 
HIS   HD1  H N N 185 
HIS   HD2  H N N 186 
HIS   HE1  H N N 187 
HIS   HE2  H N N 188 
HIS   HXT  H N N 189 
HOH   O    O N N 190 
HOH   H1   H N N 191 
HOH   H2   H N N 192 
ILE   N    N N N 193 
ILE   CA   C N S 194 
ILE   C    C N N 195 
ILE   O    O N N 196 
ILE   CB   C N S 197 
ILE   CG1  C N N 198 
ILE   CG2  C N N 199 
ILE   CD1  C N N 200 
ILE   OXT  O N N 201 
ILE   H    H N N 202 
ILE   H2   H N N 203 
ILE   HA   H N N 204 
ILE   HB   H N N 205 
ILE   HG12 H N N 206 
ILE   HG13 H N N 207 
ILE   HG21 H N N 208 
ILE   HG22 H N N 209 
ILE   HG23 H N N 210 
ILE   HD11 H N N 211 
ILE   HD12 H N N 212 
ILE   HD13 H N N 213 
ILE   HXT  H N N 214 
LEU   N    N N N 215 
LEU   CA   C N S 216 
LEU   C    C N N 217 
LEU   O    O N N 218 
LEU   CB   C N N 219 
LEU   CG   C N N 220 
LEU   CD1  C N N 221 
LEU   CD2  C N N 222 
LEU   OXT  O N N 223 
LEU   H    H N N 224 
LEU   H2   H N N 225 
LEU   HA   H N N 226 
LEU   HB2  H N N 227 
LEU   HB3  H N N 228 
LEU   HG   H N N 229 
LEU   HD11 H N N 230 
LEU   HD12 H N N 231 
LEU   HD13 H N N 232 
LEU   HD21 H N N 233 
LEU   HD22 H N N 234 
LEU   HD23 H N N 235 
LEU   HXT  H N N 236 
LYS   N    N N N 237 
LYS   CA   C N S 238 
LYS   C    C N N 239 
LYS   O    O N N 240 
LYS   CB   C N N 241 
LYS   CG   C N N 242 
LYS   CD   C N N 243 
LYS   CE   C N N 244 
LYS   NZ   N N N 245 
LYS   OXT  O N N 246 
LYS   H    H N N 247 
LYS   H2   H N N 248 
LYS   HA   H N N 249 
LYS   HB2  H N N 250 
LYS   HB3  H N N 251 
LYS   HG2  H N N 252 
LYS   HG3  H N N 253 
LYS   HD2  H N N 254 
LYS   HD3  H N N 255 
LYS   HE2  H N N 256 
LYS   HE3  H N N 257 
LYS   HZ1  H N N 258 
LYS   HZ2  H N N 259 
LYS   HZ3  H N N 260 
LYS   HXT  H N N 261 
MET   N    N N N 262 
MET   CA   C N S 263 
MET   C    C N N 264 
MET   O    O N N 265 
MET   CB   C N N 266 
MET   CG   C N N 267 
MET   SD   S N N 268 
MET   CE   C N N 269 
MET   OXT  O N N 270 
MET   H    H N N 271 
MET   H2   H N N 272 
MET   HA   H N N 273 
MET   HB2  H N N 274 
MET   HB3  H N N 275 
MET   HG2  H N N 276 
MET   HG3  H N N 277 
MET   HE1  H N N 278 
MET   HE2  H N N 279 
MET   HE3  H N N 280 
MET   HXT  H N N 281 
PHE   N    N N N 282 
PHE   CA   C N S 283 
PHE   C    C N N 284 
PHE   O    O N N 285 
PHE   CB   C N N 286 
PHE   CG   C Y N 287 
PHE   CD1  C Y N 288 
PHE   CD2  C Y N 289 
PHE   CE1  C Y N 290 
PHE   CE2  C Y N 291 
PHE   CZ   C Y N 292 
PHE   OXT  O N N 293 
PHE   H    H N N 294 
PHE   H2   H N N 295 
PHE   HA   H N N 296 
PHE   HB2  H N N 297 
PHE   HB3  H N N 298 
PHE   HD1  H N N 299 
PHE   HD2  H N N 300 
PHE   HE1  H N N 301 
PHE   HE2  H N N 302 
PHE   HZ   H N N 303 
PHE   HXT  H N N 304 
PRO   N    N N N 305 
PRO   CA   C N S 306 
PRO   C    C N N 307 
PRO   O    O N N 308 
PRO   CB   C N N 309 
PRO   CG   C N N 310 
PRO   CD   C N N 311 
PRO   OXT  O N N 312 
PRO   H    H N N 313 
PRO   HA   H N N 314 
PRO   HB2  H N N 315 
PRO   HB3  H N N 316 
PRO   HG2  H N N 317 
PRO   HG3  H N N 318 
PRO   HD2  H N N 319 
PRO   HD3  H N N 320 
PRO   HXT  H N N 321 
SER   N    N N N 322 
SER   CA   C N S 323 
SER   C    C N N 324 
SER   O    O N N 325 
SER   CB   C N N 326 
SER   OG   O N N 327 
SER   OXT  O N N 328 
SER   H    H N N 329 
SER   H2   H N N 330 
SER   HA   H N N 331 
SER   HB2  H N N 332 
SER   HB3  H N N 333 
SER   HG   H N N 334 
SER   HXT  H N N 335 
THR   N    N N N 336 
THR   CA   C N S 337 
THR   C    C N N 338 
THR   O    O N N 339 
THR   CB   C N R 340 
THR   OG1  O N N 341 
THR   CG2  C N N 342 
THR   OXT  O N N 343 
THR   H    H N N 344 
THR   H2   H N N 345 
THR   HA   H N N 346 
THR   HB   H N N 347 
THR   HG1  H N N 348 
THR   HG21 H N N 349 
THR   HG22 H N N 350 
THR   HG23 H N N 351 
THR   HXT  H N N 352 
TRP   N    N N N 353 
TRP   CA   C N S 354 
TRP   C    C N N 355 
TRP   O    O N N 356 
TRP   CB   C N N 357 
TRP   CG   C Y N 358 
TRP   CD1  C Y N 359 
TRP   CD2  C Y N 360 
TRP   NE1  N Y N 361 
TRP   CE2  C Y N 362 
TRP   CE3  C Y N 363 
TRP   CZ2  C Y N 364 
TRP   CZ3  C Y N 365 
TRP   CH2  C Y N 366 
TRP   OXT  O N N 367 
TRP   H    H N N 368 
TRP   H2   H N N 369 
TRP   HA   H N N 370 
TRP   HB2  H N N 371 
TRP   HB3  H N N 372 
TRP   HD1  H N N 373 
TRP   HE1  H N N 374 
TRP   HE3  H N N 375 
TRP   HZ2  H N N 376 
TRP   HZ3  H N N 377 
TRP   HH2  H N N 378 
TRP   HXT  H N N 379 
TYR   N    N N N 380 
TYR   CA   C N S 381 
TYR   C    C N N 382 
TYR   O    O N N 383 
TYR   CB   C N N 384 
TYR   CG   C Y N 385 
TYR   CD1  C Y N 386 
TYR   CD2  C Y N 387 
TYR   CE1  C Y N 388 
TYR   CE2  C Y N 389 
TYR   CZ   C Y N 390 
TYR   OH   O N N 391 
TYR   OXT  O N N 392 
TYR   H    H N N 393 
TYR   H2   H N N 394 
TYR   HA   H N N 395 
TYR   HB2  H N N 396 
TYR   HB3  H N N 397 
TYR   HD1  H N N 398 
TYR   HD2  H N N 399 
TYR   HE1  H N N 400 
TYR   HE2  H N N 401 
TYR   HH   H N N 402 
TYR   HXT  H N N 403 
VAL   N    N N N 404 
VAL   CA   C N S 405 
VAL   C    C N N 406 
VAL   O    O N N 407 
VAL   CB   C N N 408 
VAL   CG1  C N N 409 
VAL   CG2  C N N 410 
VAL   OXT  O N N 411 
VAL   H    H N N 412 
VAL   H2   H N N 413 
VAL   HA   H N N 414 
VAL   HB   H N N 415 
VAL   HG11 H N N 416 
VAL   HG12 H N N 417 
VAL   HG13 H N N 418 
VAL   HG21 H N N 419 
VAL   HG22 H N N 420 
VAL   HG23 H N N 421 
VAL   HXT  H N N 422 
# 
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 
A1D5H O13 C12  sing N N 1   
A1D5H C12 C11  sing N N 2   
A1D5H C11 C10  sing N N 3   
A1D5H C10 C09  sing N N 4   
A1D5H N01 C02  sing N N 5   
A1D5H C03 C02  doub Y N 6   
A1D5H C03 C04  sing Y N 7   
A1D5H C09 O08  sing N N 8   
A1D5H O08 C07  sing N N 9   
A1D5H C02 C16  sing Y N 10  
A1D5H C04 C05  doub Y N 11  
A1D5H C07 O14  doub N N 12  
A1D5H C07 N06  sing N N 13  
A1D5H C16 C15  doub Y N 14  
A1D5H C05 C15  sing Y N 15  
A1D5H C05 N06  sing N N 16  
A1D5H C09 H1   sing N N 17  
A1D5H C09 H2   sing N N 18  
A1D5H C10 H3   sing N N 19  
A1D5H C10 H4   sing N N 20  
A1D5H C03 H5   sing N N 21  
A1D5H C04 H6   sing N N 22  
A1D5H C11 H7   sing N N 23  
A1D5H C11 H8   sing N N 24  
A1D5H C12 H9   sing N N 25  
A1D5H C12 H10  sing N N 26  
A1D5H C15 H11  sing N N 27  
A1D5H C16 H12  sing N N 28  
A1D5H N01 H13  sing N N 29  
A1D5H N01 H14  sing N N 30  
A1D5H N06 H15  sing N N 31  
A1D5H O13 H16  sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
GLN   N   CA   sing N N 115 
GLN   N   H    sing N N 116 
GLN   N   H2   sing N N 117 
GLN   CA  C    sing N N 118 
GLN   CA  CB   sing N N 119 
GLN   CA  HA   sing N N 120 
GLN   C   O    doub N N 121 
GLN   C   OXT  sing N N 122 
GLN   CB  CG   sing N N 123 
GLN   CB  HB2  sing N N 124 
GLN   CB  HB3  sing N N 125 
GLN   CG  CD   sing N N 126 
GLN   CG  HG2  sing N N 127 
GLN   CG  HG3  sing N N 128 
GLN   CD  OE1  doub N N 129 
GLN   CD  NE2  sing N N 130 
GLN   NE2 HE21 sing N N 131 
GLN   NE2 HE22 sing N N 132 
GLN   OXT HXT  sing N N 133 
GLU   N   CA   sing N N 134 
GLU   N   H    sing N N 135 
GLU   N   H2   sing N N 136 
GLU   CA  C    sing N N 137 
GLU   CA  CB   sing N N 138 
GLU   CA  HA   sing N N 139 
GLU   C   O    doub N N 140 
GLU   C   OXT  sing N N 141 
GLU   CB  CG   sing N N 142 
GLU   CB  HB2  sing N N 143 
GLU   CB  HB3  sing N N 144 
GLU   CG  CD   sing N N 145 
GLU   CG  HG2  sing N N 146 
GLU   CG  HG3  sing N N 147 
GLU   CD  OE1  doub N N 148 
GLU   CD  OE2  sing N N 149 
GLU   OE2 HE2  sing N N 150 
GLU   OXT HXT  sing N N 151 
GLY   N   CA   sing N N 152 
GLY   N   H    sing N N 153 
GLY   N   H2   sing N N 154 
GLY   CA  C    sing N N 155 
GLY   CA  HA2  sing N N 156 
GLY   CA  HA3  sing N N 157 
GLY   C   O    doub N N 158 
GLY   C   OXT  sing N N 159 
GLY   OXT HXT  sing N N 160 
HIS   N   CA   sing N N 161 
HIS   N   H    sing N N 162 
HIS   N   H2   sing N N 163 
HIS   CA  C    sing N N 164 
HIS   CA  CB   sing N N 165 
HIS   CA  HA   sing N N 166 
HIS   C   O    doub N N 167 
HIS   C   OXT  sing N N 168 
HIS   CB  CG   sing N N 169 
HIS   CB  HB2  sing N N 170 
HIS   CB  HB3  sing N N 171 
HIS   CG  ND1  sing Y N 172 
HIS   CG  CD2  doub Y N 173 
HIS   ND1 CE1  doub Y N 174 
HIS   ND1 HD1  sing N N 175 
HIS   CD2 NE2  sing Y N 176 
HIS   CD2 HD2  sing N N 177 
HIS   CE1 NE2  sing Y N 178 
HIS   CE1 HE1  sing N N 179 
HIS   NE2 HE2  sing N N 180 
HIS   OXT HXT  sing N N 181 
HOH   O   H1   sing N N 182 
HOH   O   H2   sing N N 183 
ILE   N   CA   sing N N 184 
ILE   N   H    sing N N 185 
ILE   N   H2   sing N N 186 
ILE   CA  C    sing N N 187 
ILE   CA  CB   sing N N 188 
ILE   CA  HA   sing N N 189 
ILE   C   O    doub N N 190 
ILE   C   OXT  sing N N 191 
ILE   CB  CG1  sing N N 192 
ILE   CB  CG2  sing N N 193 
ILE   CB  HB   sing N N 194 
ILE   CG1 CD1  sing N N 195 
ILE   CG1 HG12 sing N N 196 
ILE   CG1 HG13 sing N N 197 
ILE   CG2 HG21 sing N N 198 
ILE   CG2 HG22 sing N N 199 
ILE   CG2 HG23 sing N N 200 
ILE   CD1 HD11 sing N N 201 
ILE   CD1 HD12 sing N N 202 
ILE   CD1 HD13 sing N N 203 
ILE   OXT HXT  sing N N 204 
LEU   N   CA   sing N N 205 
LEU   N   H    sing N N 206 
LEU   N   H2   sing N N 207 
LEU   CA  C    sing N N 208 
LEU   CA  CB   sing N N 209 
LEU   CA  HA   sing N N 210 
LEU   C   O    doub N N 211 
LEU   C   OXT  sing N N 212 
LEU   CB  CG   sing N N 213 
LEU   CB  HB2  sing N N 214 
LEU   CB  HB3  sing N N 215 
LEU   CG  CD1  sing N N 216 
LEU   CG  CD2  sing N N 217 
LEU   CG  HG   sing N N 218 
LEU   CD1 HD11 sing N N 219 
LEU   CD1 HD12 sing N N 220 
LEU   CD1 HD13 sing N N 221 
LEU   CD2 HD21 sing N N 222 
LEU   CD2 HD22 sing N N 223 
LEU   CD2 HD23 sing N N 224 
LEU   OXT HXT  sing N N 225 
LYS   N   CA   sing N N 226 
LYS   N   H    sing N N 227 
LYS   N   H2   sing N N 228 
LYS   CA  C    sing N N 229 
LYS   CA  CB   sing N N 230 
LYS   CA  HA   sing N N 231 
LYS   C   O    doub N N 232 
LYS   C   OXT  sing N N 233 
LYS   CB  CG   sing N N 234 
LYS   CB  HB2  sing N N 235 
LYS   CB  HB3  sing N N 236 
LYS   CG  CD   sing N N 237 
LYS   CG  HG2  sing N N 238 
LYS   CG  HG3  sing N N 239 
LYS   CD  CE   sing N N 240 
LYS   CD  HD2  sing N N 241 
LYS   CD  HD3  sing N N 242 
LYS   CE  NZ   sing N N 243 
LYS   CE  HE2  sing N N 244 
LYS   CE  HE3  sing N N 245 
LYS   NZ  HZ1  sing N N 246 
LYS   NZ  HZ2  sing N N 247 
LYS   NZ  HZ3  sing N N 248 
LYS   OXT HXT  sing N N 249 
MET   N   CA   sing N N 250 
MET   N   H    sing N N 251 
MET   N   H2   sing N N 252 
MET   CA  C    sing N N 253 
MET   CA  CB   sing N N 254 
MET   CA  HA   sing N N 255 
MET   C   O    doub N N 256 
MET   C   OXT  sing N N 257 
MET   CB  CG   sing N N 258 
MET   CB  HB2  sing N N 259 
MET   CB  HB3  sing N N 260 
MET   CG  SD   sing N N 261 
MET   CG  HG2  sing N N 262 
MET   CG  HG3  sing N N 263 
MET   SD  CE   sing N N 264 
MET   CE  HE1  sing N N 265 
MET   CE  HE2  sing N N 266 
MET   CE  HE3  sing N N 267 
MET   OXT HXT  sing N N 268 
PHE   N   CA   sing N N 269 
PHE   N   H    sing N N 270 
PHE   N   H2   sing N N 271 
PHE   CA  C    sing N N 272 
PHE   CA  CB   sing N N 273 
PHE   CA  HA   sing N N 274 
PHE   C   O    doub N N 275 
PHE   C   OXT  sing N N 276 
PHE   CB  CG   sing N N 277 
PHE   CB  HB2  sing N N 278 
PHE   CB  HB3  sing N N 279 
PHE   CG  CD1  doub Y N 280 
PHE   CG  CD2  sing Y N 281 
PHE   CD1 CE1  sing Y N 282 
PHE   CD1 HD1  sing N N 283 
PHE   CD2 CE2  doub Y N 284 
PHE   CD2 HD2  sing N N 285 
PHE   CE1 CZ   doub Y N 286 
PHE   CE1 HE1  sing N N 287 
PHE   CE2 CZ   sing Y N 288 
PHE   CE2 HE2  sing N N 289 
PHE   CZ  HZ   sing N N 290 
PHE   OXT HXT  sing N N 291 
PRO   N   CA   sing N N 292 
PRO   N   CD   sing N N 293 
PRO   N   H    sing N N 294 
PRO   CA  C    sing N N 295 
PRO   CA  CB   sing N N 296 
PRO   CA  HA   sing N N 297 
PRO   C   O    doub N N 298 
PRO   C   OXT  sing N N 299 
PRO   CB  CG   sing N N 300 
PRO   CB  HB2  sing N N 301 
PRO   CB  HB3  sing N N 302 
PRO   CG  CD   sing N N 303 
PRO   CG  HG2  sing N N 304 
PRO   CG  HG3  sing N N 305 
PRO   CD  HD2  sing N N 306 
PRO   CD  HD3  sing N N 307 
PRO   OXT HXT  sing N N 308 
SER   N   CA   sing N N 309 
SER   N   H    sing N N 310 
SER   N   H2   sing N N 311 
SER   CA  C    sing N N 312 
SER   CA  CB   sing N N 313 
SER   CA  HA   sing N N 314 
SER   C   O    doub N N 315 
SER   C   OXT  sing N N 316 
SER   CB  OG   sing N N 317 
SER   CB  HB2  sing N N 318 
SER   CB  HB3  sing N N 319 
SER   OG  HG   sing N N 320 
SER   OXT HXT  sing N N 321 
THR   N   CA   sing N N 322 
THR   N   H    sing N N 323 
THR   N   H2   sing N N 324 
THR   CA  C    sing N N 325 
THR   CA  CB   sing N N 326 
THR   CA  HA   sing N N 327 
THR   C   O    doub N N 328 
THR   C   OXT  sing N N 329 
THR   CB  OG1  sing N N 330 
THR   CB  CG2  sing N N 331 
THR   CB  HB   sing N N 332 
THR   OG1 HG1  sing N N 333 
THR   CG2 HG21 sing N N 334 
THR   CG2 HG22 sing N N 335 
THR   CG2 HG23 sing N N 336 
THR   OXT HXT  sing N N 337 
TRP   N   CA   sing N N 338 
TRP   N   H    sing N N 339 
TRP   N   H2   sing N N 340 
TRP   CA  C    sing N N 341 
TRP   CA  CB   sing N N 342 
TRP   CA  HA   sing N N 343 
TRP   C   O    doub N N 344 
TRP   C   OXT  sing N N 345 
TRP   CB  CG   sing N N 346 
TRP   CB  HB2  sing N N 347 
TRP   CB  HB3  sing N N 348 
TRP   CG  CD1  doub Y N 349 
TRP   CG  CD2  sing Y N 350 
TRP   CD1 NE1  sing Y N 351 
TRP   CD1 HD1  sing N N 352 
TRP   CD2 CE2  doub Y N 353 
TRP   CD2 CE3  sing Y N 354 
TRP   NE1 CE2  sing Y N 355 
TRP   NE1 HE1  sing N N 356 
TRP   CE2 CZ2  sing Y N 357 
TRP   CE3 CZ3  doub Y N 358 
TRP   CE3 HE3  sing N N 359 
TRP   CZ2 CH2  doub Y N 360 
TRP   CZ2 HZ2  sing N N 361 
TRP   CZ3 CH2  sing Y N 362 
TRP   CZ3 HZ3  sing N N 363 
TRP   CH2 HH2  sing N N 364 
TRP   OXT HXT  sing N N 365 
TYR   N   CA   sing N N 366 
TYR   N   H    sing N N 367 
TYR   N   H2   sing N N 368 
TYR   CA  C    sing N N 369 
TYR   CA  CB   sing N N 370 
TYR   CA  HA   sing N N 371 
TYR   C   O    doub N N 372 
TYR   C   OXT  sing N N 373 
TYR   CB  CG   sing N N 374 
TYR   CB  HB2  sing N N 375 
TYR   CB  HB3  sing N N 376 
TYR   CG  CD1  doub Y N 377 
TYR   CG  CD2  sing Y N 378 
TYR   CD1 CE1  sing Y N 379 
TYR   CD1 HD1  sing N N 380 
TYR   CD2 CE2  doub Y N 381 
TYR   CD2 HD2  sing N N 382 
TYR   CE1 CZ   doub Y N 383 
TYR   CE1 HE1  sing N N 384 
TYR   CE2 CZ   sing Y N 385 
TYR   CE2 HE2  sing N N 386 
TYR   CZ  OH   sing N N 387 
TYR   OH  HH   sing N N 388 
TYR   OXT HXT  sing N N 389 
VAL   N   CA   sing N N 390 
VAL   N   H    sing N N 391 
VAL   N   H2   sing N N 392 
VAL   CA  C    sing N N 393 
VAL   CA  CB   sing N N 394 
VAL   CA  HA   sing N N 395 
VAL   C   O    doub N N 396 
VAL   C   OXT  sing N N 397 
VAL   CB  CG1  sing N N 398 
VAL   CB  CG2  sing N N 399 
VAL   CB  HB   sing N N 400 
VAL   CG1 HG11 sing N N 401 
VAL   CG1 HG12 sing N N 402 
VAL   CG1 HG13 sing N N 403 
VAL   CG2 HG21 sing N N 404 
VAL   CG2 HG22 sing N N 405 
VAL   CG2 HG23 sing N N 406 
VAL   OXT HXT  sing N N 407 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XTB 
_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]   0.011774 
_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]   0.011774 
_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]   0.003626 
_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   . SER   A 1 17  ? -18.104 -8.852  -7.380  1.00 56.87  ? 17  SER   A N   1 
ATOM   2    C CA  . SER   A 1 17  ? -17.365 -8.037  -6.421  1.00 56.81  ? 17  SER   A CA  1 
ATOM   3    C C   . SER   A 1 17  ? -15.964 -7.694  -6.927  1.00 58.65  ? 17  SER   A C   1 
ATOM   4    O O   . SER   A 1 17  ? -15.226 -6.955  -6.276  1.00 61.25  ? 17  SER   A O   1 
ATOM   5    C CB  . SER   A 1 17  ? -17.275 -8.753  -5.073  1.00 61.56  ? 17  SER   A CB  1 
ATOM   6    O OG  . SER   A 1 17  ? -16.629 -10.006 -5.208  1.00 66.11  ? 17  SER   A OG  1 
ATOM   7    N N   . GLU   A 1 18  ? -15.602 -8.241  -8.087  1.00 54.35  ? 18  GLU   A N   1 
ATOM   8    C CA  . GLU   A 1 18  ? -14.325 -7.965  -8.729  1.00 51.24  ? 18  GLU   A CA  1 
ATOM   9    C C   . GLU   A 1 18  ? -14.567 -7.451  -10.144 1.00 51.44  ? 18  GLU   A C   1 
ATOM   10   O O   . GLU   A 1 18  ? -15.558 -7.807  -10.791 1.00 49.30  ? 18  GLU   A O   1 
ATOM   11   C CB  . GLU   A 1 18  ? -13.429 -9.217  -8.776  1.00 47.75  ? 18  GLU   A CB  1 
ATOM   12   C CG  . GLU   A 1 18  ? -13.094 -9.841  -7.421  1.00 48.93  ? 18  GLU   A CG  1 
ATOM   13   C CD  . GLU   A 1 18  ? -12.372 -8.889  -6.476  1.00 50.69  ? 18  GLU   A CD  1 
ATOM   14   O OE1 . GLU   A 1 18  ? -11.721 -7.931  -6.953  1.00 53.17  ? 18  GLU   A OE1 1 
ATOM   15   O OE2 . GLU   A 1 18  ? -12.442 -9.113  -5.248  1.00 51.27  ? 18  GLU   A OE2 1 
ATOM   16   N N   . LEU   A 1 19  ? -13.647 -6.615  -10.621 1.00 47.70  ? 19  LEU   A N   1 
ATOM   17   C CA  . LEU   A 1 19  ? -13.812 -5.977  -11.921 1.00 46.24  ? 19  LEU   A CA  1 
ATOM   18   C C   . LEU   A 1 19  ? -13.619 -6.987  -13.047 1.00 46.18  ? 19  LEU   A C   1 
ATOM   19   O O   . LEU   A 1 19  ? -12.634 -7.732  -13.068 1.00 47.11  ? 19  LEU   A O   1 
ATOM   20   C CB  . LEU   A 1 19  ? -12.818 -4.824  -12.070 1.00 47.79  ? 19  LEU   A CB  1 
ATOM   21   C CG  . LEU   A 1 19  ? -13.236 -3.436  -11.573 1.00 46.23  ? 19  LEU   A CG  1 
ATOM   22   C CD1 . LEU   A 1 19  ? -12.254 -2.376  -12.050 1.00 43.61  ? 19  LEU   A CD1 1 
ATOM   23   C CD2 . LEU   A 1 19  ? -14.644 -3.100  -12.032 1.00 48.20  ? 19  LEU   A CD2 1 
ATOM   24   N N   . SER   A 1 20  ? -14.564 -7.008  -13.985 1.00 43.09  ? 20  SER   A N   1 
ATOM   25   C CA  . SER   A 1 20  ? -14.408 -7.791  -15.200 1.00 44.15  ? 20  SER   A CA  1 
ATOM   26   C C   . SER   A 1 20  ? -13.255 -7.237  -16.042 1.00 41.24  ? 20  SER   A C   1 
ATOM   27   O O   . SER   A 1 20  ? -12.719 -6.156  -15.783 1.00 42.05  ? 20  SER   A O   1 
ATOM   28   C CB  . SER   A 1 20  ? -15.711 -7.791  -16.001 1.00 42.62  ? 20  SER   A CB  1 
ATOM   29   O OG  . SER   A 1 20  ? -15.692 -6.813  -17.026 1.00 42.28  ? 20  SER   A OG  1 
ATOM   30   N N   . ALA   A 1 21  ? -12.870 -8.000  -17.067 1.00 42.27  ? 21  ALA   A N   1 
ATOM   31   C CA  . ALA   A 1 21  ? -11.780 -7.562  -17.934 1.00 42.10  ? 21  ALA   A CA  1 
ATOM   32   C C   . ALA   A 1 21  ? -12.161 -6.311  -18.713 1.00 41.78  ? 21  ALA   A C   1 
ATOM   33   O O   . ALA   A 1 21  ? -11.354 -5.381  -18.838 1.00 41.33  ? 21  ALA   A O   1 
ATOM   34   C CB  . ALA   A 1 21  ? -11.377 -8.685  -18.889 1.00 37.46  ? 21  ALA   A CB  1 
ATOM   35   N N   . ILE   A 1 22  ? -13.388 -6.269  -19.238 1.00 42.01  ? 22  ILE   A N   1 
ATOM   36   C CA  . ILE   A 1 22  ? -13.854 -5.087  -19.958 1.00 39.87  ? 22  ILE   A CA  1 
ATOM   37   C C   . ILE   A 1 22  ? -13.974 -3.901  -19.010 1.00 42.57  ? 22  ILE   A C   1 
ATOM   38   O O   . ILE   A 1 22  ? -13.558 -2.782  -19.337 1.00 42.61  ? 22  ILE   A O   1 
ATOM   39   C CB  . ILE   A 1 22  ? -15.187 -5.388  -20.670 1.00 37.97  ? 22  ILE   A CB  1 
ATOM   40   C CG1 . ILE   A 1 22  ? -14.946 -6.233  -21.925 1.00 40.85  ? 22  ILE   A CG1 1 
ATOM   41   C CG2 . ILE   A 1 22  ? -15.913 -4.100  -21.027 1.00 37.64  ? 22  ILE   A CG2 1 
ATOM   42   C CD1 . ILE   A 1 22  ? -16.167 -7.013  -22.397 1.00 36.11  ? 22  ILE   A CD1 1 
ATOM   43   N N   . GLU   A 1 23  ? -14.540 -4.124  -17.818 1.00 42.67  ? 23  GLU   A N   1 
ATOM   44   C CA  . GLU   A 1 23  ? -14.628 -3.052  -16.829 1.00 42.55  ? 23  GLU   A CA  1 
ATOM   45   C C   . GLU   A 1 23  ? -13.245 -2.536  -16.455 1.00 42.14  ? 23  GLU   A C   1 
ATOM   46   O O   . GLU   A 1 23  ? -13.058 -1.330  -16.258 1.00 43.93  ? 23  GLU   A O   1 
ATOM   47   C CB  . GLU   A 1 23  ? -15.361 -3.537  -15.579 1.00 45.07  ? 23  GLU   A CB  1 
ATOM   48   C CG  . GLU   A 1 23  ? -16.799 -3.964  -15.797 1.00 45.79  ? 23  GLU   A CG  1 
ATOM   49   C CD  . GLU   A 1 23  ? -17.424 -4.532  -14.535 1.00 52.69  ? 23  GLU   A CD  1 
ATOM   50   O OE1 . GLU   A 1 23  ? -18.656 -4.411  -14.368 1.00 61.95  ? 23  GLU   A OE1 1 
ATOM   51   O OE2 . GLU   A 1 23  ? -16.680 -5.096  -13.706 1.00 46.30  ? 23  GLU   A OE2 1 
ATOM   52   N N   . THR   A 1 24  ? -12.265 -3.436  -16.350 1.00 39.76  ? 24  THR   A N   1 
ATOM   53   C CA  . THR   A 1 24  ? -10.906 -3.020  -16.015 1.00 42.22  ? 24  THR   A CA  1 
ATOM   54   C C   . THR   A 1 24  ? -10.313 -2.145  -17.113 1.00 43.75  ? 24  THR   A C   1 
ATOM   55   O O   . THR   A 1 24  ? -9.707  -1.105  -16.833 1.00 43.56  ? 24  THR   A O   1 
ATOM   56   C CB  . THR   A 1 24  ? -10.024 -4.244  -15.770 1.00 41.21  ? 24  THR   A CB  1 
ATOM   57   O OG1 . THR   A 1 24  ? -10.634 -5.090  -14.787 1.00 44.40  ? 24  THR   A OG1 1 
ATOM   58   C CG2 . THR   A 1 24  ? -8.649  -3.817  -15.280 1.00 42.34  ? 24  THR   A CG2 1 
ATOM   59   N N   . ALA   A 1 25  ? -10.480 -2.555  -18.376 1.00 43.91  ? 25  ALA   A N   1 
ATOM   60   C CA  . ALA   A 1 25  ? -9.970  -1.762  -19.490 1.00 44.37  ? 25  ALA   A CA  1 
ATOM   61   C C   . ALA   A 1 25  ? -10.620 -0.386  -19.531 1.00 42.62  ? 25  ALA   A C   1 
ATOM   62   O O   . ALA   A 1 25  ? -9.966  0.609   -19.867 1.00 40.94  ? 25  ALA   A O   1 
ATOM   63   C CB  . ALA   A 1 25  ? -10.194 -2.501  -20.809 1.00 38.73  ? 25  ALA   A CB  1 
ATOM   64   N N   . ALA   A 1 26  ? -11.909 -0.309  -19.189 1.00 42.56  ? 26  ALA   A N   1 
ATOM   65   C CA  . ALA   A 1 26  ? -12.584 0.983   -19.143 1.00 44.63  ? 26  ALA   A CA  1 
ATOM   66   C C   . ALA   A 1 26  ? -12.107 1.810   -17.956 1.00 47.37  ? 26  ALA   A C   1 
ATOM   67   O O   . ALA   A 1 26  ? -11.941 3.030   -18.070 1.00 48.74  ? 26  ALA   A O   1 
ATOM   68   C CB  . ALA   A 1 26  ? -14.098 0.786   -19.090 1.00 40.89  ? 26  ALA   A CB  1 
ATOM   69   N N   . ALA   A 1 27  ? -11.873 1.164   -16.810 1.00 43.81  ? 27  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 27  ? -11.394 1.887   -15.636 1.00 46.17  ? 27  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 27  ? -10.004 2.469   -15.856 1.00 48.71  ? 27  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 27  ? -9.651  3.474   -15.228 1.00 55.67  ? 27  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 27  ? -11.399 0.971   -14.413 1.00 46.49  ? 27  ALA   A CB  1 
ATOM   74   N N   . ILE   A 1 28  ? -9.202  1.863   -16.734 1.00 46.55  ? 28  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 28  ? -7.876  2.404   -17.015 1.00 49.06  ? 28  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 28  ? -7.960  3.506   -18.064 1.00 50.87  ? 28  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 28  ? -7.242  4.510   -17.987 1.00 51.68  ? 28  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 28  ? -6.911  1.279   -17.440 1.00 46.56  ? 28  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 28  ? -6.757  0.251   -16.316 1.00 47.31  ? 28  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 28  ? -5.547  1.840   -17.819 1.00 46.00  ? 28  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 28  ? -6.556  -1.166  -16.803 1.00 42.39  ? 28  ILE   A CD1 1 
ATOM   82   N N   . ALA   A 1 29  ? -8.840  3.340   -19.053 1.00 50.80  ? 29  ALA   A N   1 
ATOM   83   C CA  . ALA   A 1 29  ? -9.068  4.401   -20.029 1.00 51.72  ? 29  ALA   A CA  1 
ATOM   84   C C   . ALA   A 1 29  ? -9.803  5.577   -19.398 1.00 52.81  ? 29  ALA   A C   1 
ATOM   85   O O   . ALA   A 1 29  ? -9.490  6.739   -19.683 1.00 56.00  ? 29  ALA   A O   1 
ATOM   86   C CB  . ALA   A 1 29  ? -9.847  3.850   -21.223 1.00 50.65  ? 29  ALA   A CB  1 
ATOM   87   N N   . GLY   A 1 30  ? -10.772 5.292   -18.525 1.00 54.91  ? 30  GLY   A N   1 
ATOM   88   C CA  . GLY   A 1 30  ? -11.563 6.304   -17.845 1.00 51.42  ? 30  GLY   A CA  1 
ATOM   89   C C   . GLY   A 1 30  ? -10.843 7.100   -16.776 1.00 55.10  ? 30  GLY   A C   1 
ATOM   90   O O   . GLY   A 1 30  ? -11.355 8.145   -16.364 1.00 58.18  ? 30  GLY   A O   1 
ATOM   91   N N   . GLY   A 1 31  ? -9.690  6.628   -16.296 1.00 58.22  ? 31  GLY   A N   1 
ATOM   92   C CA  . GLY   A 1 31  ? -8.822  7.429   -15.459 1.00 56.81  ? 31  GLY   A CA  1 
ATOM   93   C C   . GLY   A 1 31  ? -8.895  7.175   -13.966 1.00 57.88  ? 31  GLY   A C   1 
ATOM   94   O O   . GLY   A 1 31  ? -7.988  7.613   -13.249 1.00 58.34  ? 31  GLY   A O   1 
ATOM   95   N N   . SER   A 1 32  ? -9.935  6.499   -13.467 1.00 56.27  ? 32  SER   A N   1 
ATOM   96   C CA  . SER   A 1 32  ? -10.044 6.273   -12.027 1.00 56.99  ? 32  SER   A CA  1 
ATOM   97   C C   . SER   A 1 32  ? -8.930  5.394   -11.476 1.00 59.13  ? 32  SER   A C   1 
ATOM   98   O O   . SER   A 1 32  ? -8.798  5.282   -10.252 1.00 57.15  ? 32  SER   A O   1 
ATOM   99   C CB  . SER   A 1 32  ? -11.392 5.641   -11.690 1.00 55.16  ? 32  SER   A CB  1 
ATOM   100  O OG  . SER   A 1 32  ? -11.305 4.229   -11.632 1.00 55.77  ? 32  SER   A OG  1 
ATOM   101  N N   . MET   A 1 33  ? -8.134  4.776   -12.343 1.00 60.18  ? 33  MET   A N   1 
ATOM   102  C CA  . MET   A 1 33  ? -7.049  3.902   -11.933 1.00 55.39  ? 33  MET   A CA  1 
ATOM   103  C C   . MET   A 1 33  ? -6.092  3.743   -13.107 1.00 52.75  ? 33  MET   A C   1 
ATOM   104  O O   . MET   A 1 33  ? -6.482  3.897   -14.268 1.00 55.92  ? 33  MET   A O   1 
ATOM   105  C CB  . MET   A 1 33  ? -7.592  2.549   -11.457 1.00 54.08  ? 33  MET   A CB  1 
ATOM   106  C CG  . MET   A 1 33  ? -7.899  1.557   -12.564 1.00 55.87  ? 33  MET   A CG  1 
ATOM   107  S SD  . MET   A 1 33  ? -7.941  -0.145  -11.973 1.00 52.86  ? 33  MET   A SD  1 
ATOM   108  C CE  . MET   A 1 33  ? -9.359  -0.079  -10.888 1.00 45.69  ? 33  MET   A CE  1 
ATOM   109  N N   . THR   A 1 34  ? -4.832  3.460   -12.792 1.00 52.96  ? 34  THR   A N   1 
ATOM   110  C CA  . THR   A 1 34  ? -3.793  3.289   -13.797 1.00 52.72  ? 34  THR   A CA  1 
ATOM   111  C C   . THR   A 1 34  ? -3.517  1.804   -14.028 1.00 51.89  ? 34  THR   A C   1 
ATOM   112  O O   . THR   A 1 34  ? -3.935  0.939   -13.255 1.00 48.97  ? 34  THR   A O   1 
ATOM   113  C CB  . THR   A 1 34  ? -2.509  4.021   -13.377 1.00 53.99  ? 34  THR   A CB  1 
ATOM   114  O OG1 . THR   A 1 34  ? -1.966  3.415   -12.197 1.00 54.56  ? 34  THR   A OG1 1 
ATOM   115  C CG2 . THR   A 1 34  ? -2.795  5.491   -13.099 1.00 49.54  ? 34  THR   A CG2 1 
ATOM   116  N N   . ALA   A 1 35  ? -2.809  1.515   -15.125 1.00 49.34  ? 35  ALA   A N   1 
ATOM   117  C CA  . ALA   A 1 35  ? -2.455  0.130   -15.428 1.00 49.79  ? 35  ALA   A CA  1 
ATOM   118  C C   . ALA   A 1 35  ? -1.544  -0.454  -14.355 1.00 49.95  ? 35  ALA   A C   1 
ATOM   119  O O   . ALA   A 1 35  ? -1.628  -1.648  -14.039 1.00 52.03  ? 35  ALA   A O   1 
ATOM   120  C CB  . ALA   A 1 35  ? -1.792  0.041   -16.803 1.00 46.43  ? 35  ALA   A CB  1 
ATOM   121  N N   . LEU   A 1 36  ? -0.666  0.374   -13.782 1.00 47.07  ? 36  LEU   A N   1 
ATOM   122  C CA  . LEU   A 1 36  ? 0.159   -0.072  -12.664 1.00 49.15  ? 36  LEU   A CA  1 
ATOM   123  C C   . LEU   A 1 36  ? -0.694  -0.365  -11.436 1.00 47.29  ? 36  LEU   A C   1 
ATOM   124  O O   . LEU   A 1 36  ? -0.458  -1.353  -10.731 1.00 48.65  ? 36  LEU   A O   1 
ATOM   125  C CB  . LEU   A 1 36  ? 1.222   0.982   -12.345 1.00 46.62  ? 36  LEU   A CB  1 
ATOM   126  C CG  . LEU   A 1 36  ? 2.298   0.646   -11.308 1.00 42.64  ? 36  LEU   A CG  1 
ATOM   127  C CD1 . LEU   A 1 36  ? 3.019   -0.646  -11.656 1.00 46.70  ? 36  LEU   A CD1 1 
ATOM   128  C CD2 . LEU   A 1 36  ? 3.290   1.791   -11.191 1.00 44.25  ? 36  LEU   A CD2 1 
ATOM   129  N N   . GLU   A 1 37  ? -1.694  0.480   -11.170 1.00 47.20  ? 37  GLU   A N   1 
ATOM   130  C CA  . GLU   A 1 37  ? -2.596  0.242   -10.047 1.00 49.15  ? 37  GLU   A CA  1 
ATOM   131  C C   . GLU   A 1 37  ? -3.422  -1.021  -10.258 1.00 48.82  ? 37  GLU   A C   1 
ATOM   132  O O   . GLU   A 1 37  ? -3.604  -1.813  -9.325  1.00 48.84  ? 37  GLU   A O   1 
ATOM   133  C CB  . GLU   A 1 37  ? -3.509  1.452   -9.841  1.00 48.66  ? 37  GLU   A CB  1 
ATOM   134  C CG  . GLU   A 1 37  ? -2.902  2.535   -8.961  1.00 51.49  ? 37  GLU   A CG  1 
ATOM   135  C CD  . GLU   A 1 37  ? -3.621  3.871   -9.070  1.00 58.70  ? 37  GLU   A CD  1 
ATOM   136  O OE1 . GLU   A 1 37  ? -4.634  3.958   -9.797  1.00 55.11  ? 37  GLU   A OE1 1 
ATOM   137  O OE2 . GLU   A 1 37  ? -3.165  4.840   -8.425  1.00 59.68  ? 37  GLU   A OE2 1 
ATOM   138  N N   . ALA   A 1 38  ? -3.937  -1.222  -11.474 1.00 48.95  ? 38  ALA   A N   1 
ATOM   139  C CA  . ALA   A 1 38  ? -4.684  -2.441  -11.768 1.00 46.27  ? 38  ALA   A CA  1 
ATOM   140  C C   . ALA   A 1 38  ? -3.820  -3.678  -11.583 1.00 45.09  ? 38  ALA   A C   1 
ATOM   141  O O   . ALA   A 1 38  ? -4.310  -4.722  -11.135 1.00 46.51  ? 38  ALA   A O   1 
ATOM   142  C CB  . ALA   A 1 38  ? -5.240  -2.389  -13.190 1.00 47.54  ? 38  ALA   A CB  1 
ATOM   143  N N   . CYS   A 1 39  ? -2.531  -3.575  -11.901 1.00 45.77  ? 39  CYS   A N   1 
ATOM   144  C CA  . CYS   A 1 39  ? -1.636  -4.717  -11.791 1.00 47.01  ? 39  CYS   A CA  1 
ATOM   145  C C   . CYS   A 1 39  ? -1.213  -4.976  -10.349 1.00 47.99  ? 39  CYS   A C   1 
ATOM   146  O O   . CYS   A 1 39  ? -1.041  -6.137  -9.961  1.00 44.50  ? 39  CYS   A O   1 
ATOM   147  C CB  . CYS   A 1 39  ? -0.415  -4.496  -12.682 1.00 48.26  ? 39  CYS   A CB  1 
ATOM   148  S SG  . CYS   A 1 39  ? 0.933   -5.661  -12.431 1.00 55.36  ? 39  CYS   A SG  1 
ATOM   149  N N   . ASP   A 1 40  ? -1.055  -3.921  -9.541  1.00 46.16  ? 40  ASP   A N   1 
ATOM   150  C CA  . ASP   A 1 40  ? -0.674  -4.115  -8.144  1.00 48.06  ? 40  ASP   A CA  1 
ATOM   151  C C   . ASP   A 1 40  ? -1.841  -4.614  -7.305  1.00 42.22  ? 40  ASP   A C   1 
ATOM   152  O O   . ASP   A 1 40  ? -1.629  -5.315  -6.310  1.00 44.39  ? 40  ASP   A O   1 
ATOM   153  C CB  . ASP   A 1 40  ? -0.119  -2.818  -7.550  1.00 46.36  ? 40  ASP   A CB  1 
ATOM   154  C CG  . ASP   A 1 40  ? 1.290   -2.512  -8.026  1.00 50.42  ? 40  ASP   A CG  1 
ATOM   155  O OD1 . ASP   A 1 40  ? 2.047   -3.468  -8.304  1.00 51.03  ? 40  ASP   A OD1 1 
ATOM   156  O OD2 . ASP   A 1 40  ? 1.646   -1.318  -8.111  1.00 49.79  ? 40  ASP   A OD2 1 
ATOM   157  N N   . ALA   A 1 41  ? -3.071  -4.254  -7.678  1.00 44.99  ? 41  ALA   A N   1 
ATOM   158  C CA  . ALA   A 1 41  ? -4.239  -4.787  -6.982  1.00 45.11  ? 41  ALA   A CA  1 
ATOM   159  C C   . ALA   A 1 41  ? -4.434  -6.265  -7.291  1.00 43.69  ? 41  ALA   A C   1 
ATOM   160  O O   . ALA   A 1 41  ? -4.830  -7.042  -6.414  1.00 44.93  ? 41  ALA   A O   1 
ATOM   161  C CB  . ALA   A 1 41  ? -5.487  -3.992  -7.363  1.00 40.45  ? 41  ALA   A CB  1 
ATOM   162  N N   . ALA   A 1 42  ? -4.168  -6.670  -8.535  1.00 44.08  ? 42  ALA   A N   1 
ATOM   163  C CA  . ALA   A 1 42  ? -4.274  -8.081  -8.892  1.00 46.77  ? 42  ALA   A CA  1 
ATOM   164  C C   . ALA   A 1 42  ? -3.214  -8.903  -8.174  1.00 44.24  ? 42  ALA   A C   1 
ATOM   165  O O   . ALA   A 1 42  ? -3.506  -9.977  -7.634  1.00 43.23  ? 42  ALA   A O   1 
ATOM   166  C CB  . ALA   A 1 42  ? -4.160  -8.251  -10.408 1.00 42.46  ? 42  ALA   A CB  1 
ATOM   167  N N   . ILE   A 1 43  ? -1.972  -8.409  -8.162  1.00 43.84  ? 43  ILE   A N   1 
ATOM   168  C CA  . ILE   A 1 43  ? -0.911  -9.043  -7.385  1.00 46.73  ? 43  ILE   A CA  1 
ATOM   169  C C   . ILE   A 1 43  ? -1.317  -9.150  -5.919  1.00 46.22  ? 43  ILE   A C   1 
ATOM   170  O O   . ILE   A 1 43  ? -1.115  -10.189 -5.276  1.00 44.30  ? 43  ILE   A O   1 
ATOM   171  C CB  . ILE   A 1 43  ? 0.408   -8.263  -7.555  1.00 46.09  ? 43  ILE   A CB  1 
ATOM   172  C CG1 . ILE   A 1 43  ? 0.978   -8.479  -8.959  1.00 46.18  ? 43  ILE   A CG1 1 
ATOM   173  C CG2 . ILE   A 1 43  ? 1.425   -8.677  -6.497  1.00 42.01  ? 43  ILE   A CG2 1 
ATOM   174  C CD1 . ILE   A 1 43  ? 2.088   -7.519  -9.323  1.00 45.95  ? 43  ILE   A CD1 1 
ATOM   175  N N   . ALA   A 1 44  ? -1.917  -8.086  -5.376  1.00 45.74  ? 44  ALA   A N   1 
ATOM   176  C CA  . ALA   A 1 44  ? -2.345  -8.109  -3.980  1.00 45.97  ? 44  ALA   A CA  1 
ATOM   177  C C   . ALA   A 1 44  ? -3.422  -9.163  -3.744  1.00 43.22  ? 44  ALA   A C   1 
ATOM   178  O O   . ALA   A 1 44  ? -3.381  -9.883  -2.740  1.00 44.71  ? 44  ALA   A O   1 
ATOM   179  C CB  . ALA   A 1 44  ? -2.843  -6.728  -3.556  1.00 39.48  ? 44  ALA   A CB  1 
ATOM   180  N N   . ARG   A 1 45  ? -4.397  -9.268  -4.652  1.00 43.08  ? 45  ARG   A N   1 
ATOM   181  C CA  . ARG   A 1 45  ? -5.407  -10.317 -4.526  1.00 45.19  ? 45  ARG   A CA  1 
ATOM   182  C C   . ARG   A 1 45  ? -4.776  -11.700 -4.626  1.00 45.25  ? 45  ARG   A C   1 
ATOM   183  O O   . ARG   A 1 45  ? -5.126  -12.607 -3.861  1.00 44.62  ? 45  ARG   A O   1 
ATOM   184  C CB  . ARG   A 1 45  ? -6.490  -10.146 -5.593  1.00 45.09  ? 45  ARG   A CB  1 
ATOM   185  C CG  . ARG   A 1 45  ? -7.465  -9.015  -5.317  1.00 44.92  ? 45  ARG   A CG  1 
ATOM   186  C CD  . ARG   A 1 45  ? -8.562  -8.939  -6.371  1.00 43.97  ? 45  ARG   A CD  1 
ATOM   187  N NE  . ARG   A 1 45  ? -8.042  -8.953  -7.735  1.00 45.17  ? 45  ARG   A NE  1 
ATOM   188  C CZ  . ARG   A 1 45  ? -7.911  -7.875  -8.498  1.00 47.08  ? 45  ARG   A CZ  1 
ATOM   189  N NH1 . ARG   A 1 45  ? -8.211  -6.667  -8.046  1.00 42.43  ? 45  ARG   A NH1 1 
ATOM   190  N NH2 . ARG   A 1 45  ? -7.472  -8.011  -9.747  1.00 44.12  ? 45  ARG   A NH2 1 
ATOM   191  N N   . ILE   A 1 46  ? -3.839  -11.878 -5.560  1.00 45.29  ? 46  ILE   A N   1 
ATOM   192  C CA  . ILE   A 1 46  ? -3.154  -13.162 -5.698  1.00 42.75  ? 46  ILE   A CA  1 
ATOM   193  C C   . ILE   A 1 46  ? -2.464  -13.536 -4.391  1.00 46.62  ? 46  ILE   A C   1 
ATOM   194  O O   . ILE   A 1 46  ? -2.644  -14.641 -3.867  1.00 46.29  ? 46  ILE   A O   1 
ATOM   195  C CB  . ILE   A 1 46  ? -2.161  -13.115 -6.874  1.00 41.79  ? 46  ILE   A CB  1 
ATOM   196  C CG1 . ILE   A 1 46  ? -2.905  -13.192 -8.211  1.00 43.47  ? 46  ILE   A CG1 1 
ATOM   197  C CG2 . ILE   A 1 46  ? -1.135  -14.237 -6.763  1.00 39.53  ? 46  ILE   A CG2 1 
ATOM   198  C CD1 . ILE   A 1 46  ? -2.110  -12.645 -9.389  1.00 43.69  ? 46  ILE   A CD1 1 
ATOM   199  N N   . GLU   A 1 47  ? -1.685  -12.610 -3.828  1.00 46.77  ? 47  GLU   A N   1 
ATOM   200  C CA  . GLU   A 1 47  ? -0.948  -12.923 -2.607  1.00 47.93  ? 47  GLU   A CA  1 
ATOM   201  C C   . GLU   A 1 47  ? -1.867  -13.097 -1.404  1.00 45.80  ? 47  GLU   A C   1 
ATOM   202  O O   . GLU   A 1 47  ? -1.581  -13.921 -0.528  1.00 48.29  ? 47  GLU   A O   1 
ATOM   203  C CB  . GLU   A 1 47  ? 0.096   -11.845 -2.333  1.00 48.29  ? 47  GLU   A CB  1 
ATOM   204  C CG  . GLU   A 1 47  ? 1.380   -12.047 -3.119  1.00 50.55  ? 47  GLU   A CG  1 
ATOM   205  C CD  . GLU   A 1 47  ? 2.095   -10.750 -3.406  1.00 50.47  ? 47  GLU   A CD  1 
ATOM   206  O OE1 . GLU   A 1 47  ? 1.548   -9.681  -3.060  1.00 52.50  ? 47  GLU   A OE1 1 
ATOM   207  O OE2 . GLU   A 1 47  ? 3.199   -10.800 -3.986  1.00 51.41  ? 47  GLU   A OE2 1 
ATOM   208  N N   . GLN   A 1 48  ? -2.971  -12.353 -1.343  1.00 46.09  ? 48  GLN   A N   1 
ATOM   209  C CA  . GLN   A 1 48  ? -3.874  -12.457 -0.202  1.00 44.00  ? 48  GLN   A CA  1 
ATOM   210  C C   . GLN   A 1 48  ? -4.786  -13.674 -0.266  1.00 45.44  ? 48  GLN   A C   1 
ATOM   211  O O   . GLN   A 1 48  ? -5.339  -14.063 0.768   1.00 49.00  ? 48  GLN   A O   1 
ATOM   212  C CB  . GLN   A 1 48  ? -4.731  -11.195 -0.081  1.00 47.63  ? 48  GLN   A CB  1 
ATOM   213  C CG  . GLN   A 1 48  ? -4.063  -10.059 0.683   1.00 47.77  ? 48  GLN   A CG  1 
ATOM   214  C CD  . GLN   A 1 48  ? -4.426  -8.690  0.139   1.00 53.08  ? 48  GLN   A CD  1 
ATOM   215  O OE1 . GLN   A 1 48  ? -5.541  -8.470  -0.339  1.00 56.66  ? 48  GLN   A OE1 1 
ATOM   216  N NE2 . GLN   A 1 48  ? -3.479  -7.763  0.202   1.00 57.14  ? 48  GLN   A NE2 1 
ATOM   217  N N   . ARG   A 1 49  ? -4.953  -14.289 -1.441  1.00 45.48  ? 49  ARG   A N   1 
ATOM   218  C CA  . ARG   A 1 49  ? -5.908  -15.377 -1.600  1.00 42.07  ? 49  ARG   A CA  1 
ATOM   219  C C   . ARG   A 1 49  ? -5.316  -16.698 -2.072  1.00 40.17  ? 49  ARG   A C   1 
ATOM   220  O O   . ARG   A 1 49  ? -5.935  -17.740 -1.833  1.00 39.82  ? 49  ARG   A O   1 
ATOM   221  C CB  . ARG   A 1 49  ? -7.029  -14.977 -2.575  1.00 40.17  ? 49  ARG   A CB  1 
ATOM   222  C CG  . ARG   A 1 49  ? -7.733  -13.679 -2.212  1.00 41.88  ? 49  ARG   A CG  1 
ATOM   223  C CD  . ARG   A 1 49  ? -8.408  -13.031 -3.413  1.00 41.62  ? 49  ARG   A CD  1 
ATOM   224  N NE  . ARG   A 1 49  ? -8.986  -11.742 -3.054  1.00 45.76  ? 49  ARG   A NE  1 
ATOM   225  C CZ  . ARG   A 1 49  ? -10.015 -11.177 -3.670  1.00 45.89  ? 49  ARG   A CZ  1 
ATOM   226  N NH1 . ARG   A 1 49  ? -10.627 -11.770 -4.682  1.00 43.77  ? 49  ARG   A NH1 1 
ATOM   227  N NH2 . ARG   A 1 49  ? -10.435 -9.981  -3.267  1.00 43.66  ? 49  ARG   A NH2 1 
ATOM   228  N N   . ASP   A 1 50  ? -4.150  -16.700 -2.720  1.00 41.64  ? 50  ASP   A N   1 
ATOM   229  C CA  . ASP   A 1 50  ? -3.681  -17.925 -3.363  1.00 42.38  ? 50  ASP   A CA  1 
ATOM   230  C C   . ASP   A 1 50  ? -3.188  -18.975 -2.374  1.00 39.57  ? 50  ASP   A C   1 
ATOM   231  O O   . ASP   A 1 50  ? -3.148  -20.158 -2.727  1.00 41.81  ? 50  ASP   A O   1 
ATOM   232  C CB  . ASP   A 1 50  ? -2.571  -17.611 -4.363  1.00 40.76  ? 50  ASP   A CB  1 
ATOM   233  C CG  . ASP   A 1 50  ? -2.585  -18.540 -5.552  1.00 46.03  ? 50  ASP   A CG  1 
ATOM   234  O OD1 . ASP   A 1 50  ? -1.698  -18.413 -6.424  1.00 49.94  ? 50  ASP   A OD1 1 
ATOM   235  O OD2 . ASP   A 1 50  ? -3.494  -19.395 -5.619  1.00 48.83  ? 50  ASP   A OD2 1 
ATOM   236  N N   . GLY   A 1 51  ? -2.820  -18.578 -1.156  1.00 39.94  ? 51  GLY   A N   1 
ATOM   237  C CA  . GLY   A 1 51  ? -2.295  -19.486 -0.157  1.00 41.71  ? 51  GLY   A CA  1 
ATOM   238  C C   . GLY   A 1 51  ? -3.029  -20.810 -0.030  1.00 40.78  ? 51  GLY   A C   1 
ATOM   239  O O   . GLY   A 1 51  ? -2.445  -21.887 -0.187  1.00 39.16  ? 51  GLY   A O   1 
ATOM   240  N N   . PRO   A 1 52  ? -4.328  -20.756 0.281   1.00 38.48  ? 52  PRO   A N   1 
ATOM   241  C CA  . PRO   A 1 52  ? -5.113  -21.995 0.388   1.00 38.98  ? 52  PRO   A CA  1 
ATOM   242  C C   . PRO   A 1 52  ? -5.570  -22.582 -0.943  1.00 40.84  ? 52  PRO   A C   1 
ATOM   243  O O   . PRO   A 1 52  ? -6.081  -23.711 -0.947  1.00 41.48  ? 52  PRO   A O   1 
ATOM   244  C CB  . PRO   A 1 52  ? -6.320  -21.567 1.235   1.00 42.43  ? 52  PRO   A CB  1 
ATOM   245  C CG  . PRO   A 1 52  ? -6.443  -20.094 0.997   1.00 39.54  ? 52  PRO   A CG  1 
ATOM   246  C CD  . PRO   A 1 52  ? -5.045  -19.593 0.838   1.00 41.61  ? 52  PRO   A CD  1 
ATOM   247  N N   . ILE   A 1 53  ? -5.404  -21.876 -2.059  1.00 39.23  ? 53  ILE   A N   1 
ATOM   248  C CA  . ILE   A 1 53  ? -5.921  -22.319 -3.358  1.00 37.87  ? 53  ILE   A CA  1 
ATOM   249  C C   . ILE   A 1 53  ? -4.815  -22.874 -4.251  1.00 41.53  ? 53  ILE   A C   1 
ATOM   250  O O   . ILE   A 1 53  ? -4.975  -23.937 -4.850  1.00 40.44  ? 53  ILE   A O   1 
ATOM   251  C CB  . ILE   A 1 53  ? -6.681  -21.169 -4.060  1.00 40.88  ? 53  ILE   A CB  1 
ATOM   252  C CG1 . ILE   A 1 53  ? -7.993  -20.865 -3.335  1.00 37.27  ? 53  ILE   A CG1 1 
ATOM   253  C CG2 . ILE   A 1 53  ? -6.971  -21.517 -5.518  1.00 39.00  ? 53  ILE   A CG2 1 
ATOM   254  C CD1 . ILE   A 1 53  ? -8.347  -19.400 -3.323  1.00 39.05  ? 53  ILE   A CD1 1 
ATOM   255  N N   . ASN   A 1 54  ? -3.694  -22.155 -4.369  1.00 41.12  ? 54  ASN   A N   1 
ATOM   256  C CA  . ASN   A 1 54  ? -2.549  -22.576 -5.184  1.00 38.92  ? 54  ASN   A CA  1 
ATOM   257  C C   . ASN   A 1 54  ? -2.932  -22.682 -6.664  1.00 39.93  ? 54  ASN   A C   1 
ATOM   258  O O   . ASN   A 1 54  ? -2.868  -23.749 -7.282  1.00 38.04  ? 54  ASN   A O   1 
ATOM   259  C CB  . ASN   A 1 54  ? -1.965  -23.894 -4.663  1.00 41.50  ? 54  ASN   A CB  1 
ATOM   260  C CG  . ASN   A 1 54  ? -0.579  -24.186 -5.209  1.00 39.05  ? 54  ASN   A CG  1 
ATOM   261  O OD1 . ASN   A 1 54  ? 0.217   -23.278 -5.444  1.00 40.95  ? 54  ASN   A OD1 1 
ATOM   262  N ND2 . ASN   A 1 54  ? -0.288  -25.462 -5.420  1.00 37.39  ? 54  ASN   A ND2 1 
ATOM   263  N N   . ALA   A 1 55  ? -3.328  -21.539 -7.226  1.00 39.55  ? 55  ALA   A N   1 
ATOM   264  C CA  . ALA   A 1 55  ? -3.748  -21.437 -8.618  1.00 39.83  ? 55  ALA   A CA  1 
ATOM   265  C C   . ALA   A 1 55  ? -2.692  -20.786 -9.503  1.00 37.29  ? 55  ALA   A C   1 
ATOM   266  O O   . ALA   A 1 55  ? -2.380  -21.307 -10.578 1.00 36.38  ? 55  ALA   A O   1 
ATOM   267  C CB  . ALA   A 1 55  ? -5.063  -20.655 -8.713  1.00 41.11  ? 55  ALA   A CB  1 
ATOM   268  N N   . VAL   A 1 56  ? -2.135  -19.654 -9.074  1.00 42.10  ? 56  VAL   A N   1 
ATOM   269  C CA  . VAL   A 1 56  ? -1.118  -18.937 -9.849  1.00 38.50  ? 56  VAL   A CA  1 
ATOM   270  C C   . VAL   A 1 56  ? 0.234   -19.499 -9.416  1.00 42.36  ? 56  VAL   A C   1 
ATOM   271  O O   . VAL   A 1 56  ? 0.855   -19.029 -8.460  1.00 42.27  ? 56  VAL   A O   1 
ATOM   272  C CB  . VAL   A 1 56  ? -1.210  -17.425 -9.654  1.00 38.53  ? 56  VAL   A CB  1 
ATOM   273  C CG1 . VAL   A 1 56  ? -0.435  -16.704 -10.743 1.00 42.69  ? 56  VAL   A CG1 1 
ATOM   274  C CG2 . VAL   A 1 56  ? -2.661  -16.976 -9.653  1.00 36.98  ? 56  VAL   A CG2 1 
ATOM   275  N N   . VAL   A 1 57  ? 0.703   -20.512 -10.145 1.00 39.60  ? 57  VAL   A N   1 
ATOM   276  C CA  . VAL   A 1 57  ? 1.891   -21.255 -9.737  1.00 41.62  ? 57  VAL   A CA  1 
ATOM   277  C C   . VAL   A 1 57  ? 3.177   -20.743 -10.379 1.00 41.65  ? 57  VAL   A C   1 
ATOM   278  O O   . VAL   A 1 57  ? 4.264   -20.970 -9.828  1.00 43.67  ? 57  VAL   A O   1 
ATOM   279  C CB  . VAL   A 1 57  ? 1.711   -22.752 -10.045 1.00 42.62  ? 57  VAL   A CB  1 
ATOM   280  C CG1 . VAL   A 1 57  ? 0.663   -23.354 -9.122  1.00 39.35  ? 57  VAL   A CG1 1 
ATOM   281  C CG2 . VAL   A 1 57  ? 1.321   -22.947 -11.499 1.00 39.94  ? 57  VAL   A CG2 1 
ATOM   282  N N   . VAL   A 1 58  ? 3.089   -20.071 -11.522 1.00 43.25  ? 58  VAL   A N   1 
ATOM   283  C CA  . VAL   A 1 58  ? 4.204   -19.347 -12.120 1.00 41.95  ? 58  VAL   A CA  1 
ATOM   284  C C   . VAL   A 1 58  ? 3.895   -17.863 -11.988 1.00 43.13  ? 58  VAL   A C   1 
ATOM   285  O O   . VAL   A 1 58  ? 2.790   -17.425 -12.325 1.00 43.05  ? 58  VAL   A O   1 
ATOM   286  C CB  . VAL   A 1 58  ? 4.412   -19.739 -13.594 1.00 40.85  ? 58  VAL   A CB  1 
ATOM   287  C CG1 . VAL   A 1 58  ? 5.528   -18.905 -14.218 1.00 43.09  ? 58  VAL   A CG1 1 
ATOM   288  C CG2 . VAL   A 1 58  ? 4.707   -21.222 -13.720 1.00 42.39  ? 58  VAL   A CG2 1 
ATOM   289  N N   . ARG   A 1 59  ? 4.854   -17.093 -11.480 1.00 42.07  ? 59  ARG   A N   1 
ATOM   290  C CA  . ARG   A 1 59  ? 4.630   -15.679 -11.211 1.00 42.92  ? 59  ARG   A CA  1 
ATOM   291  C C   . ARG   A 1 59  ? 5.710   -14.836 -11.867 1.00 42.50  ? 59  ARG   A C   1 
ATOM   292  O O   . ARG   A 1 59  ? 6.902   -15.137 -11.750 1.00 47.13  ? 59  ARG   A O   1 
ATOM   293  C CB  . ARG   A 1 59  ? 4.570   -15.400 -9.707  1.00 41.21  ? 59  ARG   A CB  1 
ATOM   294  C CG  . ARG   A 1 59  ? 3.304   -15.937 -9.069  1.00 44.47  ? 59  ARG   A CG  1 
ATOM   295  C CD  . ARG   A 1 59  ? 3.391   -15.989 -7.561  1.00 43.66  ? 59  ARG   A CD  1 
ATOM   296  N NE  . ARG   A 1 59  ? 2.187   -16.575 -6.988  1.00 42.99  ? 59  ARG   A NE  1 
ATOM   297  C CZ  . ARG   A 1 59  ? 1.778   -16.382 -5.743  1.00 43.04  ? 59  ARG   A CZ  1 
ATOM   298  N NH1 . ARG   A 1 59  ? 2.442   -15.594 -4.912  1.00 40.67  ? 59  ARG   A NH1 1 
ATOM   299  N NH2 . ARG   A 1 59  ? 0.682   -17.003 -5.316  1.00 41.91  ? 59  ARG   A NH2 1 
ATOM   300  N N   . ASP   A 1 60  ? 5.278   -13.779 -12.551 1.00 43.83  ? 60  ASP   A N   1 
ATOM   301  C CA  . ASP   A 1 60  ? 6.149   -12.874 -13.290 1.00 46.02  ? 60  ASP   A CA  1 
ATOM   302  C C   . ASP   A 1 60  ? 5.811   -11.437 -12.899 1.00 46.66  ? 60  ASP   A C   1 
ATOM   303  O O   . ASP   A 1 60  ? 5.511   -10.589 -13.737 1.00 46.86  ? 60  ASP   A O   1 
ATOM   304  C CB  . ASP   A 1 60  ? 5.990   -13.095 -14.793 1.00 45.22  ? 60  ASP   A CB  1 
ATOM   305  C CG  . ASP   A 1 60  ? 7.300   -12.969 -15.550 1.00 51.46  ? 60  ASP   A CG  1 
ATOM   306  O OD1 . ASP   A 1 60  ? 8.357   -13.350 -15.001 1.00 54.16  ? 60  ASP   A OD1 1 
ATOM   307  O OD2 . ASP   A 1 60  ? 7.268   -12.491 -16.703 1.00 55.14  ? 60  ASP   A OD2 1 
ATOM   308  N N   . PHE   A 1 61  ? 5.872   -11.165 -11.592 1.00 42.97  ? 61  PHE   A N   1 
ATOM   309  C CA  . PHE   A 1 61  ? 5.315   -9.922  -11.068 1.00 45.14  ? 61  PHE   A CA  1 
ATOM   310  C C   . PHE   A 1 61  ? 6.158   -8.704  -11.433 1.00 46.90  ? 61  PHE   A C   1 
ATOM   311  O O   . PHE   A 1 61  ? 5.605   -7.622  -11.660 1.00 46.37  ? 61  PHE   A O   1 
ATOM   312  C CB  . PHE   A 1 61  ? 5.153   -10.027 -9.553  1.00 44.56  ? 61  PHE   A CB  1 
ATOM   313  C CG  . PHE   A 1 61  ? 4.036   -10.940 -9.125  1.00 40.49  ? 61  PHE   A CG  1 
ATOM   314  C CD1 . PHE   A 1 61  ? 3.114   -11.409 -10.047 1.00 44.14  ? 61  PHE   A CD1 1 
ATOM   315  C CD2 . PHE   A 1 61  ? 3.907   -11.326 -7.802  1.00 42.05  ? 61  PHE   A CD2 1 
ATOM   316  C CE1 . PHE   A 1 61  ? 2.089   -12.250 -9.661  1.00 43.76  ? 61  PHE   A CE1 1 
ATOM   317  C CE2 . PHE   A 1 61  ? 2.878   -12.167 -7.406  1.00 45.28  ? 61  PHE   A CE2 1 
ATOM   318  C CZ  . PHE   A 1 61  ? 1.970   -12.629 -8.337  1.00 43.98  ? 61  PHE   A CZ  1 
ATOM   319  N N   . ASP   A 1 62  ? 7.483   -8.849  -11.503 1.00 46.55  ? 62  ASP   A N   1 
ATOM   320  C CA  . ASP   A 1 62  ? 8.322   -7.692  -11.812 1.00 50.13  ? 62  ASP   A CA  1 
ATOM   321  C C   . ASP   A 1 62  ? 8.218   -7.305  -13.283 1.00 51.14  ? 62  ASP   A C   1 
ATOM   322  O O   . ASP   A 1 62  ? 8.116   -6.117  -13.610 1.00 50.81  ? 62  ASP   A O   1 
ATOM   323  C CB  . ASP   A 1 62  ? 9.774   -7.970  -11.426 1.00 50.10  ? 62  ASP   A CB  1 
ATOM   324  C CG  . ASP   A 1 62  ? 9.976   -8.022  -9.920  1.00 57.55  ? 62  ASP   A CG  1 
ATOM   325  O OD1 . ASP   A 1 62  ? 9.262   -7.293  -9.195  1.00 57.24  ? 62  ASP   A OD1 1 
ATOM   326  O OD2 . ASP   A 1 62  ? 10.850  -8.787  -9.460  1.00 65.41  ? 62  ASP   A OD2 1 
ATOM   327  N N   . ARG   A 1 63  ? 8.245   -8.290  -14.184 1.00 48.28  ? 63  ARG   A N   1 
ATOM   328  C CA  . ARG   A 1 63  ? 8.065   -7.989  -15.600 1.00 47.43  ? 63  ARG   A CA  1 
ATOM   329  C C   . ARG   A 1 63  ? 6.667   -7.451  -15.880 1.00 49.68  ? 63  ARG   A C   1 
ATOM   330  O O   . ARG   A 1 63  ? 6.490   -6.622  -16.780 1.00 50.12  ? 63  ARG   A O   1 
ATOM   331  C CB  . ARG   A 1 63  ? 8.322   -9.237  -16.445 1.00 46.51  ? 63  ARG   A CB  1 
ATOM   332  C CG  . ARG   A 1 63  ? 9.704   -9.852  -16.298 1.00 48.35  ? 63  ARG   A CG  1 
ATOM   333  C CD  . ARG   A 1 63  ? 10.168  -10.418 -17.621 1.00 44.28  ? 63  ARG   A CD  1 
ATOM   334  N NE  . ARG   A 1 63  ? 9.664   -11.771 -17.814 1.00 44.09  ? 63  ARG   A NE  1 
ATOM   335  C CZ  . ARG   A 1 63  ? 9.508   -12.354 -18.995 1.00 44.24  ? 63  ARG   A CZ  1 
ATOM   336  N NH1 . ARG   A 1 63  ? 9.865   -11.750 -20.117 1.00 45.46  ? 63  ARG   A NH1 1 
ATOM   337  N NH2 . ARG   A 1 63  ? 8.966   -13.566 -19.052 1.00 45.50  ? 63  ARG   A NH2 1 
ATOM   338  N N   . ALA   A 1 64  ? 5.665   -7.912  -15.125 1.00 50.38  ? 64  ALA   A N   1 
ATOM   339  C CA  . ALA   A 1 64  ? 4.307   -7.414  -15.315 1.00 49.22  ? 64  ALA   A CA  1 
ATOM   340  C C   . ALA   A 1 64  ? 4.188   -5.963  -14.870 1.00 49.12  ? 64  ALA   A C   1 
ATOM   341  O O   . ALA   A 1 64  ? 3.492   -5.167  -15.512 1.00 46.88  ? 64  ALA   A O   1 
ATOM   342  C CB  . ALA   A 1 64  ? 3.309   -8.291  -14.558 1.00 45.19  ? 64  ALA   A CB  1 
ATOM   343  N N   . ARG   A 1 65  ? 4.858   -5.600  -13.773 1.00 49.00  ? 65  ARG   A N   1 
ATOM   344  C CA  . ARG   A 1 65  ? 4.821   -4.214  -13.318 1.00 49.78  ? 65  ARG   A CA  1 
ATOM   345  C C   . ARG   A 1 65  ? 5.446   -3.282  -14.348 1.00 46.81  ? 65  ARG   A C   1 
ATOM   346  O O   . ARG   A 1 65  ? 4.967   -2.163  -14.550 1.00 48.04  ? 65  ARG   A O   1 
ATOM   347  C CB  . ARG   A 1 65  ? 5.524   -4.082  -11.966 1.00 49.15  ? 65  ARG   A CB  1 
ATOM   348  C CG  . ARG   A 1 65  ? 4.677   -4.554  -10.792 1.00 50.48  ? 65  ARG   A CG  1 
ATOM   349  C CD  . ARG   A 1 65  ? 5.303   -4.178  -9.461  1.00 49.37  ? 65  ARG   A CD  1 
ATOM   350  N NE  . ARG   A 1 65  ? 4.713   -2.965  -8.907  1.00 54.09  ? 65  ARG   A NE  1 
ATOM   351  C CZ  . ARG   A 1 65  ? 5.301   -1.777  -8.913  1.00 51.25  ? 65  ARG   A CZ  1 
ATOM   352  N NH1 . ARG   A 1 65  ? 6.510   -1.607  -9.422  1.00 51.65  ? 65  ARG   A NH1 1 
ATOM   353  N NH2 . ARG   A 1 65  ? 4.659   -0.732  -8.397  1.00 47.61  ? 65  ARG   A NH2 1 
ATOM   354  N N   . ASP   A 1 66  ? 6.506   -3.733  -15.025 1.00 48.22  ? 66  ASP   A N   1 
ATOM   355  C CA  . ASP   A 1 66  ? 7.094   -2.930  -16.094 1.00 51.02  ? 66  ASP   A CA  1 
ATOM   356  C C   . ASP   A 1 66  ? 6.158   -2.830  -17.291 1.00 49.63  ? 66  ASP   A C   1 
ATOM   357  O O   . ASP   A 1 66  ? 6.072   -1.775  -17.932 1.00 52.07  ? 66  ASP   A O   1 
ATOM   358  C CB  . ASP   A 1 66  ? 8.440   -3.515  -16.520 1.00 51.95  ? 66  ASP   A CB  1 
ATOM   359  C CG  . ASP   A 1 66  ? 9.512   -3.328  -15.470 1.00 54.98  ? 66  ASP   A CG  1 
ATOM   360  O OD1 . ASP   A 1 66  ? 9.342   -2.445  -14.601 1.00 56.08  ? 66  ASP   A OD1 1 
ATOM   361  O OD2 . ASP   A 1 66  ? 10.526  -4.054  -15.518 1.00 57.99  ? 66  ASP   A OD2 1 
ATOM   362  N N   . ALA   A 1 67  ? 5.457   -3.919  -17.615 1.00 48.88  ? 67  ALA   A N   1 
ATOM   363  C CA  . ALA   A 1 67  ? 4.493   -3.877  -18.708 1.00 48.35  ? 67  ALA   A CA  1 
ATOM   364  C C   . ALA   A 1 67  ? 3.357   -2.908  -18.400 1.00 49.82  ? 67  ALA   A C   1 
ATOM   365  O O   . ALA   A 1 67  ? 2.867   -2.208  -19.294 1.00 49.77  ? 67  ALA   A O   1 
ATOM   366  C CB  . ALA   A 1 67  ? 3.949   -5.280  -18.981 1.00 46.98  ? 67  ALA   A CB  1 
ATOM   367  N N   . ALA   A 1 68  ? 2.932   -2.846  -17.136 1.00 48.10  ? 68  ALA   A N   1 
ATOM   368  C CA  . ALA   A 1 68  ? 1.865   -1.925  -16.761 1.00 47.89  ? 68  ALA   A CA  1 
ATOM   369  C C   . ALA   A 1 68  ? 2.304   -0.473  -16.910 1.00 49.79  ? 68  ALA   A C   1 
ATOM   370  O O   . ALA   A 1 68  ? 1.511   0.377   -17.331 1.00 50.33  ? 68  ALA   A O   1 
ATOM   371  C CB  . ALA   A 1 68  ? 1.408   -2.206  -15.331 1.00 47.66  ? 68  ALA   A CB  1 
ATOM   372  N N   . LYS   A 1 69  ? 3.560   -0.164  -16.563 1.00 50.71  ? 69  LYS   A N   1 
ATOM   373  C CA  . LYS   A 1 69  ? 4.067   1.190   -16.774 1.00 50.38  ? 69  LYS   A CA  1 
ATOM   374  C C   . LYS   A 1 69  ? 4.077   1.539   -18.254 1.00 49.97  ? 69  LYS   A C   1 
ATOM   375  O O   . LYS   A 1 69  ? 3.696   2.650   -18.643 1.00 51.35  ? 69  LYS   A O   1 
ATOM   376  C CB  . LYS   A 1 69  ? 5.469   1.335   -16.179 1.00 48.01  ? 69  LYS   A CB  1 
ATOM   377  C CG  . LYS   A 1 69  ? 5.612   0.731   -14.796 1.00 49.03  ? 69  LYS   A CG  1 
ATOM   378  C CD  . LYS   A 1 69  ? 6.778   1.299   -14.010 1.00 50.08  ? 69  LYS   A CD  1 
ATOM   379  C CE  . LYS   A 1 69  ? 7.046   0.448   -12.775 1.00 52.53  ? 69  LYS   A CE  1 
ATOM   380  N NZ  . LYS   A 1 69  ? 7.954   1.115   -11.803 1.00 51.01  ? 69  LYS   A NZ  1 
ATOM   381  N N   . ALA   A 1 70  ? 4.505   0.595   -19.096 1.00 50.39  ? 70  ALA   A N   1 
ATOM   382  C CA  . ALA   A 1 70  ? 4.450   0.802   -20.539 1.00 50.26  ? 70  ALA   A CA  1 
ATOM   383  C C   . ALA   A 1 70  ? 3.017   1.011   -21.008 1.00 53.06  ? 70  ALA   A C   1 
ATOM   384  O O   . ALA   A 1 70  ? 2.765   1.800   -21.927 1.00 56.00  ? 70  ALA   A O   1 
ATOM   385  C CB  . ALA   A 1 70  ? 5.085   -0.386  -21.261 1.00 49.69  ? 70  ALA   A CB  1 
ATOM   386  N N   . ALA   A 1 71  ? 2.062   0.316   -20.383 1.00 51.55  ? 71  ALA   A N   1 
ATOM   387  C CA  . ALA   A 1 71  ? 0.659   0.484   -20.748 1.00 51.19  ? 71  ALA   A CA  1 
ATOM   388  C C   . ALA   A 1 71  ? 0.149   1.866   -20.362 1.00 52.23  ? 71  ALA   A C   1 
ATOM   389  O O   . ALA   A 1 71  ? -0.574  2.505   -21.137 1.00 52.58  ? 71  ALA   A O   1 
ATOM   390  C CB  . ALA   A 1 71  ? -0.189  -0.605  -20.092 1.00 48.98  ? 71  ALA   A CB  1 
ATOM   391  N N   . ASP   A 1 72  ? 0.513   2.345   -19.169 1.00 51.40  ? 72  ASP   A N   1 
ATOM   392  C CA  . ASP   A 1 72  ? 0.109   3.685   -18.757 1.00 52.05  ? 72  ASP   A CA  1 
ATOM   393  C C   . ASP   A 1 72  ? 0.717   4.751   -19.657 1.00 52.63  ? 72  ASP   A C   1 
ATOM   394  O O   . ASP   A 1 72  ? 0.097   5.795   -19.885 1.00 56.15  ? 72  ASP   A O   1 
ATOM   395  C CB  . ASP   A 1 72  ? 0.506   3.927   -17.302 1.00 51.16  ? 72  ASP   A CB  1 
ATOM   396  C CG  . ASP   A 1 72  ? -0.496  3.347   -16.320 1.00 53.16  ? 72  ASP   A CG  1 
ATOM   397  O OD1 . ASP   A 1 72  ? -1.717  3.515   -16.536 1.00 52.48  ? 72  ASP   A OD1 1 
ATOM   398  O OD2 . ASP   A 1 72  ? -0.061  2.722   -15.329 1.00 53.71  ? 72  ASP   A OD2 1 
ATOM   399  N N   . ALA   A 1 73  ? 1.922   4.509   -20.177 1.00 52.52  ? 73  ALA   A N   1 
ATOM   400  C CA  . ALA   A 1 73  ? 2.490   5.427   -21.157 1.00 55.41  ? 73  ALA   A CA  1 
ATOM   401  C C   . ALA   A 1 73  ? 1.644   5.459   -22.423 1.00 56.87  ? 73  ALA   A C   1 
ATOM   402  O O   . ALA   A 1 73  ? 1.413   6.530   -22.998 1.00 59.69  ? 73  ALA   A O   1 
ATOM   403  C CB  . ALA   A 1 73  ? 3.931   5.031   -21.479 1.00 52.38  ? 73  ALA   A CB  1 
ATOM   404  N N   . GLU   A 1 74  ? 1.166   4.293   -22.867 1.00 54.15  ? 74  GLU   A N   1 
ATOM   405  C CA  . GLU   A 1 74  ? 0.246   4.254   -24.000 1.00 56.02  ? 74  GLU   A CA  1 
ATOM   406  C C   . GLU   A 1 74  ? -1.069  4.944   -23.662 1.00 57.98  ? 74  GLU   A C   1 
ATOM   407  O O   . GLU   A 1 74  ? -1.616  5.691   -24.483 1.00 60.08  ? 74  GLU   A O   1 
ATOM   408  C CB  . GLU   A 1 74  ? -0.002  2.807   -24.430 1.00 57.07  ? 74  GLU   A CB  1 
ATOM   409  C CG  . GLU   A 1 74  ? 1.268   2.030   -24.741 1.00 53.47  ? 74  GLU   A CG  1 
ATOM   410  C CD  . GLU   A 1 74  ? 1.030   0.851   -25.665 1.00 55.81  ? 74  GLU   A CD  1 
ATOM   411  O OE1 . GLU   A 1 74  ? 0.480   1.056   -26.769 1.00 56.93  ? 74  GLU   A OE1 1 
ATOM   412  O OE2 . GLU   A 1 74  ? 1.399   -0.281  -25.288 1.00 59.32  ? 74  GLU   A OE2 1 
ATOM   413  N N   . ILE   A 1 75  ? -1.595  4.704   -22.457 1.00 55.35  ? 75  ILE   A N   1 
ATOM   414  C CA  . ILE   A 1 75  ? -2.813  5.386   -22.024 1.00 57.53  ? 75  ILE   A CA  1 
ATOM   415  C C   . ILE   A 1 75  ? -2.605  6.895   -22.020 1.00 58.75  ? 75  ILE   A C   1 
ATOM   416  O O   . ILE   A 1 75  ? -3.494  7.663   -22.411 1.00 58.12  ? 75  ILE   A O   1 
ATOM   417  C CB  . ILE   A 1 75  ? -3.254  4.869   -20.642 1.00 56.64  ? 75  ILE   A CB  1 
ATOM   418  C CG1 . ILE   A 1 75  ? -3.695  3.405   -20.725 1.00 52.85  ? 75  ILE   A CG1 1 
ATOM   419  C CG2 . ILE   A 1 75  ? -4.382  5.724   -20.089 1.00 55.59  ? 75  ILE   A CG2 1 
ATOM   420  C CD1 . ILE   A 1 75  ? -5.123  3.233   -21.209 1.00 52.36  ? 75  ILE   A CD1 1 
ATOM   421  N N   . ALA   A 1 76  ? -1.424  7.345   -21.589 1.00 57.57  ? 76  ALA   A N   1 
ATOM   422  C CA  . ALA   A 1 76  ? -1.128  8.773   -21.608 1.00 57.03  ? 76  ALA   A CA  1 
ATOM   423  C C   . ALA   A 1 76  ? -1.012  9.295   -23.036 1.00 57.17  ? 76  ALA   A C   1 
ATOM   424  O O   . ALA   A 1 76  ? -1.441  10.418  -23.326 1.00 58.93  ? 76  ALA   A O   1 
ATOM   425  C CB  . ALA   A 1 76  ? 0.152   9.051   -20.820 1.00 56.19  ? 76  ALA   A CB  1 
ATOM   426  N N   . ALA   A 1 77  ? -0.451  8.489   -23.944 1.00 59.00  ? 77  ALA   A N   1 
ATOM   427  C CA  . ALA   A 1 77  ? -0.281  8.853   -25.347 1.00 59.61  ? 77  ALA   A CA  1 
ATOM   428  C C   . ALA   A 1 77  ? -1.547  8.665   -26.178 1.00 56.62  ? 77  ALA   A C   1 
ATOM   429  O O   . ALA   A 1 77  ? -1.450  8.511   -27.404 1.00 55.51  ? 77  ALA   A O   1 
ATOM   430  C CB  . ALA   A 1 77  ? 0.867   8.048   -25.965 1.00 56.51  ? 77  ALA   A CB  1 
ATOM   431  N N   . ALA   A 1 78  ? -2.718  8.662   -25.540 1.00 57.07  ? 78  ALA   A N   1 
ATOM   432  C CA  . ALA   A 1 78  ? -4.016  8.587   -26.207 1.00 60.56  ? 78  ALA   A CA  1 
ATOM   433  C C   . ALA   A 1 78  ? -4.235  7.262   -26.934 1.00 57.21  ? 78  ALA   A C   1 
ATOM   434  O O   . ALA   A 1 78  ? -5.116  7.169   -27.794 1.00 58.64  ? 78  ALA   A O   1 
ATOM   435  C CB  . ALA   A 1 78  ? -4.211  9.760   -27.180 1.00 58.79  ? 78  ALA   A CB  1 
ATOM   436  N N   . VAL   A 1 79  ? -3.461  6.231   -26.601 1.00 56.50  ? 79  VAL   A N   1 
ATOM   437  C CA  . VAL   A 1 79  ? -3.624  4.916   -27.212 1.00 56.15  ? 79  VAL   A CA  1 
ATOM   438  C C   . VAL   A 1 79  ? -4.728  4.157   -26.489 1.00 56.07  ? 79  VAL   A C   1 
ATOM   439  O O   . VAL   A 1 79  ? -4.780  4.129   -25.253 1.00 57.35  ? 79  VAL   A O   1 
ATOM   440  C CB  . VAL   A 1 79  ? -2.297  4.135   -27.182 1.00 56.70  ? 79  VAL   A CB  1 
ATOM   441  C CG1 . VAL   A 1 79  ? -2.523  2.671   -27.549 1.00 54.93  ? 79  VAL   A CG1 1 
ATOM   442  C CG2 . VAL   A 1 79  ? -1.281  4.770   -28.120 1.00 58.59  ? 79  VAL   A CG2 1 
ATOM   443  N N   . ARG   A 1 80  ? -5.622  3.540   -27.261 1.00 54.82  ? 80  ARG   A N   1 
ATOM   444  C CA  . ARG   A 1 80  ? -6.728  2.761   -26.718 1.00 54.38  ? 80  ARG   A CA  1 
ATOM   445  C C   . ARG   A 1 80  ? -6.735  1.392   -27.382 1.00 54.03  ? 80  ARG   A C   1 
ATOM   446  O O   . ARG   A 1 80  ? -6.919  1.292   -28.599 1.00 54.46  ? 80  ARG   A O   1 
ATOM   447  C CB  . ARG   A 1 80  ? -8.068  3.474   -26.939 1.00 55.98  ? 80  ARG   A CB  1 
ATOM   448  C CG  . ARG   A 1 80  ? -8.409  4.549   -25.908 1.00 56.79  ? 80  ARG   A CG  1 
ATOM   449  C CD  . ARG   A 1 80  ? -7.845  4.231   -24.532 1.00 60.25  ? 80  ARG   A CD  1 
ATOM   450  N NE  . ARG   A 1 80  ? -8.023  5.334   -23.594 1.00 61.71  ? 80  ARG   A NE  1 
ATOM   451  C CZ  . ARG   A 1 80  ? -7.080  6.210   -23.272 1.00 58.98  ? 80  ARG   A CZ  1 
ATOM   452  N NH1 . ARG   A 1 80  ? -5.867  6.146   -23.797 1.00 60.99  ? 80  ARG   A NH1 1 
ATOM   453  N NH2 . ARG   A 1 80  ? -7.360  7.173   -22.398 1.00 59.20  ? 80  ARG   A NH2 1 
ATOM   454  N N   . LYS   A 1 81  ? -6.529  0.346   -26.584 1.00 54.92  ? 81  LYS   A N   1 
ATOM   455  C CA  . LYS   A 1 81  ? -6.607  -1.045  -27.001 1.00 46.70  ? 81  LYS   A CA  1 
ATOM   456  C C   . LYS   A 1 81  ? -7.631  -1.770  -26.136 1.00 45.65  ? 81  LYS   A C   1 
ATOM   457  O O   . LYS   A 1 81  ? -7.771  -1.452  -24.952 1.00 46.40  ? 81  LYS   A O   1 
ATOM   458  C CB  . LYS   A 1 81  ? -5.242  -1.737  -26.881 1.00 45.66  ? 81  LYS   A CB  1 
ATOM   459  C CG  . LYS   A 1 81  ? -4.266  -1.375  -27.988 1.00 49.27  ? 81  LYS   A CG  1 
ATOM   460  C CD  . LYS   A 1 81  ? -2.835  -1.335  -27.471 1.00 52.20  ? 81  LYS   A CD  1 
ATOM   461  C CE  . LYS   A 1 81  ? -1.824  -1.347  -28.606 1.00 53.15  ? 81  LYS   A CE  1 
ATOM   462  N NZ  . LYS   A 1 81  ? -0.661  -2.228  -28.300 1.00 52.53  ? 81  LYS   A NZ  1 
ATOM   463  N N   . PRO   A 1 82  ? -8.360  -2.747  -26.690 1.00 44.23  ? 82  PRO   A N   1 
ATOM   464  C CA  . PRO   A 1 82  ? -9.506  -3.311  -25.948 1.00 41.25  ? 82  PRO   A CA  1 
ATOM   465  C C   . PRO   A 1 82  ? -9.149  -3.933  -24.606 1.00 39.81  ? 82  PRO   A C   1 
ATOM   466  O O   . PRO   A 1 82  ? -10.016 -4.012  -23.727 1.00 41.41  ? 82  PRO   A O   1 
ATOM   467  C CB  . PRO   A 1 82  ? -10.071 -4.357  -26.923 1.00 38.42  ? 82  PRO   A CB  1 
ATOM   468  C CG  . PRO   A 1 82  ? -8.932  -4.691  -27.828 1.00 46.48  ? 82  PRO   A CG  1 
ATOM   469  C CD  . PRO   A 1 82  ? -8.171  -3.407  -27.994 1.00 42.17  ? 82  PRO   A CD  1 
ATOM   470  N N   . LEU   A 1 83  ? -7.906  -4.373  -24.411 1.00 42.67  ? 83  LEU   A N   1 
ATOM   471  C CA  . LEU   A 1 83  ? -7.498  -5.022  -23.169 1.00 42.36  ? 83  LEU   A CA  1 
ATOM   472  C C   . LEU   A 1 83  ? -6.299  -4.317  -22.546 1.00 42.79  ? 83  LEU   A C   1 
ATOM   473  O O   . LEU   A 1 83  ? -5.508  -4.935  -21.828 1.00 42.29  ? 83  LEU   A O   1 
ATOM   474  C CB  . LEU   A 1 83  ? -7.182  -6.498  -23.413 1.00 41.22  ? 83  LEU   A CB  1 
ATOM   475  C CG  . LEU   A 1 83  ? -8.361  -7.473  -23.498 1.00 39.70  ? 83  LEU   A CG  1 
ATOM   476  C CD1 . LEU   A 1 83  ? -7.893  -8.905  -23.287 1.00 39.95  ? 83  LEU   A CD1 1 
ATOM   477  C CD2 . LEU   A 1 83  ? -9.443  -7.109  -22.494 1.00 40.23  ? 83  LEU   A CD2 1 
ATOM   478  N N   . LEU   A 1 84  ? -6.163  -3.020  -22.810 1.00 42.71  ? 84  LEU   A N   1 
ATOM   479  C CA  . LEU   A 1 84  ? -4.963  -2.282  -22.436 1.00 43.98  ? 84  LEU   A CA  1 
ATOM   480  C C   . LEU   A 1 84  ? -4.849  -2.184  -20.917 1.00 44.68  ? 84  LEU   A C   1 
ATOM   481  O O   . LEU   A 1 84  ? -5.742  -1.652  -20.249 1.00 43.73  ? 84  LEU   A O   1 
ATOM   482  C CB  . LEU   A 1 84  ? -4.991  -0.896  -23.082 1.00 45.31  ? 84  LEU   A CB  1 
ATOM   483  C CG  . LEU   A 1 84  ? -3.778  0.031   -22.974 1.00 49.51  ? 84  LEU   A CG  1 
ATOM   484  C CD1 . LEU   A 1 84  ? -2.491  -0.694  -23.322 1.00 43.66  ? 84  LEU   A CD1 1 
ATOM   485  C CD2 . LEU   A 1 84  ? -3.971  1.217   -23.901 1.00 47.43  ? 84  LEU   A CD2 1 
ATOM   486  N N   . GLY   A 1 85  ? -3.755  -2.717  -20.376 1.00 43.65  ? 85  GLY   A N   1 
ATOM   487  C CA  . GLY   A 1 85  ? -3.480  -2.634  -18.958 1.00 43.39  ? 85  GLY   A CA  1 
ATOM   488  C C   . GLY   A 1 85  ? -4.235  -3.611  -18.086 1.00 42.22  ? 85  GLY   A C   1 
ATOM   489  O O   . GLY   A 1 85  ? -4.134  -3.521  -16.859 1.00 40.72  ? 85  GLY   A O   1 
ATOM   490  N N   . VAL   A 1 86  ? -4.980  -4.542  -18.672 1.00 43.38  ? 86  VAL   A N   1 
ATOM   491  C CA  . VAL   A 1 86  ? -5.786  -5.482  -17.897 1.00 40.04  ? 86  VAL   A CA  1 
ATOM   492  C C   . VAL   A 1 86  ? -4.892  -6.616  -17.412 1.00 41.30  ? 86  VAL   A C   1 
ATOM   493  O O   . VAL   A 1 86  ? -4.307  -7.335  -18.235 1.00 41.16  ? 86  VAL   A O   1 
ATOM   494  C CB  . VAL   A 1 86  ? -6.966  -6.008  -18.730 1.00 40.84  ? 86  VAL   A CB  1 
ATOM   495  C CG1 . VAL   A 1 86  ? -7.745  -7.061  -17.955 1.00 40.23  ? 86  VAL   A CG1 1 
ATOM   496  C CG2 . VAL   A 1 86  ? -7.865  -4.858  -19.149 1.00 40.02  ? 86  VAL   A CG2 1 
ATOM   497  N N   . PRO   A 1 87  ? -4.736  -6.802  -16.099 1.00 41.84  ? 87  PRO   A N   1 
ATOM   498  C CA  . PRO   A 1 87  ? -3.916  -7.912  -15.598 1.00 42.81  ? 87  PRO   A CA  1 
ATOM   499  C C   . PRO   A 1 87  ? -4.649  -9.238  -15.728 1.00 42.75  ? 87  PRO   A C   1 
ATOM   500  O O   . PRO   A 1 87  ? -5.858  -9.325  -15.500 1.00 42.60  ? 87  PRO   A O   1 
ATOM   501  C CB  . PRO   A 1 87  ? -3.688  -7.545  -14.127 1.00 45.88  ? 87  PRO   A CB  1 
ATOM   502  C CG  . PRO   A 1 87  ? -4.891  -6.732  -13.765 1.00 45.96  ? 87  PRO   A CG  1 
ATOM   503  C CD  . PRO   A 1 87  ? -5.259  -5.961  -15.007 1.00 43.03  ? 87  PRO   A CD  1 
ATOM   504  N N   . MET   A 1 88  ? -3.901  -10.279 -16.089 1.00 40.45  ? 88  MET   A N   1 
ATOM   505  C CA  . MET   A 1 88  ? -4.486  -11.586 -16.358 1.00 41.45  ? 88  MET   A CA  1 
ATOM   506  C C   . MET   A 1 88  ? -3.412  -12.663 -16.271 1.00 42.63  ? 88  MET   A C   1 
ATOM   507  O O   . MET   A 1 88  ? -2.215  -12.377 -16.190 1.00 43.16  ? 88  MET   A O   1 
ATOM   508  C CB  . MET   A 1 88  ? -5.166  -11.609 -17.728 1.00 40.92  ? 88  MET   A CB  1 
ATOM   509  C CG  . MET   A 1 88  ? -4.197  -11.776 -18.881 1.00 41.56  ? 88  MET   A CG  1 
ATOM   510  S SD  . MET   A 1 88  ? -5.059  -11.926 -20.453 1.00 46.54  ? 88  MET   A SD  1 
ATOM   511  C CE  . MET   A 1 88  ? -6.051  -13.379 -20.138 1.00 40.07  ? 88  MET   A CE  1 
ATOM   512  N N   . THR   A 1 89  ? -3.867  -13.915 -16.286 1.00 41.61  ? 89  THR   A N   1 
ATOM   513  C CA  . THR   A 1 89  ? -2.996  -15.079 -16.322 1.00 43.33  ? 89  THR   A CA  1 
ATOM   514  C C   . THR   A 1 89  ? -3.438  -15.991 -17.456 1.00 42.94  ? 89  THR   A C   1 
ATOM   515  O O   . THR   A 1 89  ? -4.518  -15.832 -18.031 1.00 44.64  ? 89  THR   A O   1 
ATOM   516  C CB  . THR   A 1 89  ? -3.012  -15.855 -14.994 1.00 45.76  ? 89  THR   A CB  1 
ATOM   517  O OG1 . THR   A 1 89  ? -4.363  -16.169 -14.634 1.00 40.41  ? 89  THR   A OG1 1 
ATOM   518  C CG2 . THR   A 1 89  ? -2.370  -15.033 -13.885 1.00 42.56  ? 89  THR   A CG2 1 
ATOM   519  N N   . ILE   A 1 90  ? -2.581  -16.955 -17.779 1.00 41.16  ? 90  ILE   A N   1 
ATOM   520  C CA  . ILE   A 1 90  ? -2.876  -17.955 -18.795 1.00 40.72  ? 90  ILE   A CA  1 
ATOM   521  C C   . ILE   A 1 90  ? -2.431  -19.313 -18.273 1.00 41.36  ? 90  ILE   A C   1 
ATOM   522  O O   . ILE   A 1 90  ? -1.567  -19.414 -17.398 1.00 41.28  ? 90  ILE   A O   1 
ATOM   523  C CB  . ILE   A 1 90  ? -2.204  -17.628 -20.149 1.00 41.83  ? 90  ILE   A CB  1 
ATOM   524  C CG1 . ILE   A 1 90  ? -2.934  -18.340 -21.294 1.00 40.46  ? 90  ILE   A CG1 1 
ATOM   525  C CG2 . ILE   A 1 90  ? -0.731  -17.993 -20.123 1.00 39.19  ? 90  ILE   A CG2 1 
ATOM   526  C CD1 . ILE   A 1 90  ? -2.979  -17.554 -22.585 1.00 40.39  ? 90  ILE   A CD1 1 
ATOM   527  N N   . LYS   A 1 91  ? -3.052  -20.363 -18.801 1.00 43.39  ? 91  LYS   A N   1 
ATOM   528  C CA  . LYS   A 1 91  ? -2.717  -21.727 -18.417 1.00 41.62  ? 91  LYS   A CA  1 
ATOM   529  C C   . LYS   A 1 91  ? -1.234  -22.007 -18.635 1.00 40.77  ? 91  LYS   A C   1 
ATOM   530  O O   . LYS   A 1 91  ? -0.629  -21.519 -19.593 1.00 41.27  ? 91  LYS   A O   1 
ATOM   531  C CB  . LYS   A 1 91  ? -3.574  -22.688 -19.233 1.00 39.10  ? 91  LYS   A CB  1 
ATOM   532  C CG  . LYS   A 1 91  ? -3.666  -24.097 -18.727 1.00 37.78  ? 91  LYS   A CG  1 
ATOM   533  C CD  . LYS   A 1 91  ? -4.723  -24.802 -19.542 1.00 37.92  ? 91  LYS   A CD  1 
ATOM   534  C CE  . LYS   A 1 91  ? -4.461  -26.272 -19.679 1.00 39.43  ? 91  LYS   A CE  1 
ATOM   535  N NZ  . LYS   A 1 91  ? -5.604  -26.888 -20.397 1.00 44.43  ? 91  LYS   A NZ  1 
ATOM   536  N N   . GLU   A 1 92  ? -0.651  -22.808 -17.734 1.00 36.97  ? 92  GLU   A N   1 
ATOM   537  C CA  . GLU   A 1 92  ? 0.789   -23.059 -17.749 1.00 40.63  ? 92  GLU   A CA  1 
ATOM   538  C C   . GLU   A 1 92  ? 1.286   -23.683 -19.049 1.00 41.87  ? 92  GLU   A C   1 
ATOM   539  O O   . GLU   A 1 92  ? 2.477   -23.567 -19.358 1.00 38.96  ? 92  GLU   A O   1 
ATOM   540  C CB  . GLU   A 1 92  ? 1.185   -23.969 -16.585 1.00 40.69  ? 92  GLU   A CB  1 
ATOM   541  C CG  . GLU   A 1 92  ? 2.647   -23.841 -16.160 1.00 42.09  ? 92  GLU   A CG  1 
ATOM   542  C CD  . GLU   A 1 92  ? 3.516   -24.977 -16.684 1.00 43.55  ? 92  GLU   A CD  1 
ATOM   543  O OE1 . GLU   A 1 92  ? 2.985   -25.877 -17.371 1.00 42.06  ? 92  GLU   A OE1 1 
ATOM   544  O OE2 . GLU   A 1 92  ? 4.734   -24.973 -16.403 1.00 43.44  ? 92  GLU   A OE2 1 
ATOM   545  N N   . SER   A 1 93  ? 0.419   -24.353 -19.810 1.00 41.66  ? 93  SER   A N   1 
ATOM   546  C CA  . SER   A 1 93  ? 0.859   -24.987 -21.048 1.00 40.69  ? 93  SER   A CA  1 
ATOM   547  C C   . SER   A 1 93  ? 1.124   -23.990 -22.171 1.00 40.86  ? 93  SER   A C   1 
ATOM   548  O O   . SER   A 1 93  ? 1.855   -24.324 -23.109 1.00 43.76  ? 93  SER   A O   1 
ATOM   549  C CB  . SER   A 1 93  ? -0.172  -26.018 -21.507 1.00 41.79  ? 93  SER   A CB  1 
ATOM   550  O OG  . SER   A 1 93  ? -1.495  -25.550 -21.318 1.00 41.43  ? 93  SER   A OG  1 
ATOM   551  N N   . PHE   A 1 94  ? 0.561   -22.785 -22.101 1.00 38.75  ? 94  PHE   A N   1 
ATOM   552  C CA  . PHE   A 1 94  ? 0.791   -21.777 -23.129 1.00 41.14  ? 94  PHE   A CA  1 
ATOM   553  C C   . PHE   A 1 94  ? 2.162   -21.139 -22.953 1.00 42.44  ? 94  PHE   A C   1 
ATOM   554  O O   . PHE   A 1 94  ? 2.524   -20.725 -21.848 1.00 40.14  ? 94  PHE   A O   1 
ATOM   555  C CB  . PHE   A 1 94  ? -0.286  -20.695 -23.078 1.00 41.09  ? 94  PHE   A CB  1 
ATOM   556  C CG  . PHE   A 1 94  ? -1.623  -21.149 -23.564 1.00 36.31  ? 94  PHE   A CG  1 
ATOM   557  C CD1 . PHE   A 1 94  ? -1.983  -20.989 -24.891 1.00 39.03  ? 94  PHE   A CD1 1 
ATOM   558  C CD2 . PHE   A 1 94  ? -2.521  -21.743 -22.694 1.00 41.16  ? 94  PHE   A CD2 1 
ATOM   559  C CE1 . PHE   A 1 94  ? -3.217  -21.409 -25.342 1.00 42.77  ? 94  PHE   A CE1 1 
ATOM   560  C CE2 . PHE   A 1 94  ? -3.759  -22.166 -23.136 1.00 40.57  ? 94  PHE   A CE2 1 
ATOM   561  C CZ  . PHE   A 1 94  ? -4.108  -21.996 -24.460 1.00 41.79  ? 94  PHE   A CZ  1 
ATOM   562  N N   . ASP   A 1 95  ? 2.910   -21.029 -24.046 1.00 40.21  ? 95  ASP   A N   1 
ATOM   563  C CA  . ASP   A 1 95  ? 4.248   -20.459 -23.969 1.00 40.26  ? 95  ASP   A CA  1 
ATOM   564  C C   . ASP   A 1 95  ? 4.180   -18.958 -23.718 1.00 43.26  ? 95  ASP   A C   1 
ATOM   565  O O   . ASP   A 1 95  ? 3.410   -18.241 -24.366 1.00 39.64  ? 95  ASP   A O   1 
ATOM   566  C CB  . ASP   A 1 95  ? 5.024   -20.745 -25.253 1.00 41.33  ? 95  ASP   A CB  1 
ATOM   567  C CG  . ASP   A 1 95  ? 5.780   -22.067 -25.201 1.00 43.19  ? 95  ASP   A CG  1 
ATOM   568  O OD1 . ASP   A 1 95  ? 5.625   -22.815 -24.210 1.00 42.23  ? 95  ASP   A OD1 1 
ATOM   569  O OD2 . ASP   A 1 95  ? 6.520   -22.361 -26.164 1.00 41.37  ? 95  ASP   A OD2 1 
ATOM   570  N N   . ILE   A 1 96  ? 4.979   -18.489 -22.761 1.00 43.75  ? 96  ILE   A N   1 
ATOM   571  C CA  . ILE   A 1 96  ? 5.249   -17.069 -22.565 1.00 42.83  ? 96  ILE   A CA  1 
ATOM   572  C C   . ILE   A 1 96  ? 6.760   -16.893 -22.550 1.00 45.38  ? 96  ILE   A C   1 
ATOM   573  O O   . ILE   A 1 96  ? 7.463   -17.612 -21.830 1.00 42.58  ? 96  ILE   A O   1 
ATOM   574  C CB  . ILE   A 1 96  ? 4.629   -16.527 -21.263 1.00 42.71  ? 96  ILE   A CB  1 
ATOM   575  C CG1 . ILE   A 1 96  ? 3.114   -16.750 -21.252 1.00 39.77  ? 96  ILE   A CG1 1 
ATOM   576  C CG2 . ILE   A 1 96  ? 4.966   -15.044 -21.099 1.00 43.66  ? 96  ILE   A CG2 1 
ATOM   577  C CD1 . ILE   A 1 96  ? 2.382   -15.970 -20.178 1.00 37.86  ? 96  ILE   A CD1 1 
ATOM   578  N N   . ALA   A 1 97  ? 7.255   -15.948 -23.350 1.00 46.01  ? 97  ALA   A N   1 
ATOM   579  C CA  . ALA   A 1 97  ? 8.693   -15.761 -23.501 1.00 44.95  ? 97  ALA   A CA  1 
ATOM   580  C C   . ALA   A 1 97  ? 9.348   -15.445 -22.163 1.00 46.43  ? 97  ALA   A C   1 
ATOM   581  O O   . ALA   A 1 97  ? 8.917   -14.540 -21.442 1.00 45.55  ? 97  ALA   A O   1 
ATOM   582  C CB  . ALA   A 1 97  ? 8.975   -14.641 -24.504 1.00 43.74  ? 97  ALA   A CB  1 
ATOM   583  N N   . GLY   A 1 98  ? 10.394  -16.201 -21.833 1.00 45.10  ? 98  GLY   A N   1 
ATOM   584  C CA  . GLY   A 1 98  ? 11.092  -16.035 -20.576 1.00 45.40  ? 98  GLY   A CA  1 
ATOM   585  C C   . GLY   A 1 98  ? 10.463  -16.730 -19.390 1.00 46.84  ? 98  GLY   A C   1 
ATOM   586  O O   . GLY   A 1 98  ? 10.891  -16.494 -18.255 1.00 43.15  ? 98  GLY   A O   1 
ATOM   587  N N   . LEU   A 1 99  ? 9.467   -17.578 -19.610 1.00 48.27  ? 99  LEU   A N   1 
ATOM   588  C CA  . LEU   A 1 99  ? 8.754   -18.271 -18.552 1.00 45.28  ? 99  LEU   A CA  1 
ATOM   589  C C   . LEU   A 1 99  ? 8.843   -19.773 -18.779 1.00 45.05  ? 99  LEU   A C   1 
ATOM   590  O O   . LEU   A 1 99  ? 9.053   -20.226 -19.910 1.00 45.79  ? 99  LEU   A O   1 
ATOM   591  C CB  . LEU   A 1 99  ? 7.282   -17.836 -18.513 1.00 47.08  ? 99  LEU   A CB  1 
ATOM   592  C CG  . LEU   A 1 99  ? 6.982   -16.493 -17.839 1.00 47.76  ? 99  LEU   A CG  1 
ATOM   593  C CD1 . LEU   A 1 99  ? 5.502   -16.373 -17.512 1.00 41.75  ? 99  LEU   A CD1 1 
ATOM   594  C CD2 . LEU   A 1 99  ? 7.828   -16.302 -16.586 1.00 47.36  ? 99  LEU   A CD2 1 
ATOM   595  N N   . PRO   A 1 100 ? 8.698   -20.577 -17.726 1.00 47.04  ? 100 PRO   A N   1 
ATOM   596  C CA  . PRO   A 1 100 ? 8.728   -22.033 -17.901 1.00 44.80  ? 100 PRO   A CA  1 
ATOM   597  C C   . PRO   A 1 100 ? 7.414   -22.584 -18.436 1.00 42.64  ? 100 PRO   A C   1 
ATOM   598  O O   . PRO   A 1 100 ? 6.327   -22.134 -18.063 1.00 42.25  ? 100 PRO   A O   1 
ATOM   599  C CB  . PRO   A 1 100 ? 8.995   -22.542 -16.479 1.00 46.20  ? 100 PRO   A CB  1 
ATOM   600  C CG  . PRO   A 1 100 ? 8.360   -21.508 -15.619 1.00 43.15  ? 100 PRO   A CG  1 
ATOM   601  C CD  . PRO   A 1 100 ? 8.705   -20.208 -16.299 1.00 41.91  ? 100 PRO   A CD  1 
ATOM   602  N N   . THR   A 1 101 ? 7.528   -23.573 -19.324 1.00 42.74  ? 101 THR   A N   1 
ATOM   603  C CA  . THR   A 1 101 ? 6.399   -24.386 -19.772 1.00 41.21  ? 101 THR   A CA  1 
ATOM   604  C C   . THR   A 1 101 ? 6.748   -25.840 -19.486 1.00 45.45  ? 101 THR   A C   1 
ATOM   605  O O   . THR   A 1 101 ? 7.598   -26.424 -20.168 1.00 44.31  ? 101 THR   A O   1 
ATOM   606  C CB  . THR   A 1 101 ? 6.100   -24.190 -21.258 1.00 40.14  ? 101 THR   A CB  1 
ATOM   607  O OG1 . THR   A 1 101 ? 5.583   -22.872 -21.479 1.00 43.26  ? 101 THR   A OG1 1 
ATOM   608  C CG2 . THR   A 1 101 ? 5.065   -25.215 -21.718 1.00 39.29  ? 101 THR   A CG2 1 
ATOM   609  N N   . SER   A 1 102 ? 6.097   -26.421 -18.480 1.00 43.12  ? 102 SER   A N   1 
ATOM   610  C CA  . SER   A 1 102 ? 6.427   -27.763 -18.021 1.00 43.12  ? 102 SER   A CA  1 
ATOM   611  C C   . SER   A 1 102 ? 5.355   -28.796 -18.313 1.00 41.44  ? 102 SER   A C   1 
ATOM   612  O O   . SER   A 1 102 ? 5.681   -29.979 -18.442 1.00 43.11  ? 102 SER   A O   1 
ATOM   613  C CB  . SER   A 1 102 ? 6.692   -27.757 -16.509 1.00 44.94  ? 102 SER   A CB  1 
ATOM   614  O OG  . SER   A 1 102 ? 5.476   -27.679 -15.779 1.00 41.08  ? 102 SER   A OG  1 
ATOM   615  N N   . TRP   A 1 103 ? 4.091   -28.375 -18.418 1.00 42.30  ? 103 TRP   A N   1 
ATOM   616  C CA  . TRP   A 1 103 ? 2.935   -29.271 -18.476 1.00 42.81  ? 103 TRP   A CA  1 
ATOM   617  C C   . TRP   A 1 103 ? 2.850   -30.164 -17.240 1.00 40.60  ? 103 TRP   A C   1 
ATOM   618  O O   . TRP   A 1 103 ? 2.263   -31.249 -17.291 1.00 41.60  ? 103 TRP   A O   1 
ATOM   619  C CB  . TRP   A 1 103 ? 2.944   -30.128 -19.749 1.00 40.86  ? 103 TRP   A CB  1 
ATOM   620  C CG  . TRP   A 1 103 ? 2.569   -29.383 -20.997 1.00 43.07  ? 103 TRP   A CG  1 
ATOM   621  C CD1 . TRP   A 1 103 ? 2.881   -28.090 -21.306 1.00 41.45  ? 103 TRP   A CD1 1 
ATOM   622  C CD2 . TRP   A 1 103 ? 1.843   -29.900 -22.120 1.00 41.12  ? 103 TRP   A CD2 1 
ATOM   623  N NE1 . TRP   A 1 103 ? 2.380   -27.765 -22.543 1.00 41.63  ? 103 TRP   A NE1 1 
ATOM   624  C CE2 . TRP   A 1 103 ? 1.739   -28.858 -23.064 1.00 44.52  ? 103 TRP   A CE2 1 
ATOM   625  C CE3 . TRP   A 1 103 ? 1.266   -31.138 -22.416 1.00 39.37  ? 103 TRP   A CE3 1 
ATOM   626  C CZ2 . TRP   A 1 103 ? 1.077   -29.017 -24.282 1.00 44.28  ? 103 TRP   A CZ2 1 
ATOM   627  C CZ3 . TRP   A 1 103 ? 0.611   -31.293 -23.628 1.00 42.94  ? 103 TRP   A CZ3 1 
ATOM   628  C CH2 . TRP   A 1 103 ? 0.523   -30.239 -24.545 1.00 39.62  ? 103 TRP   A CH2 1 
ATOM   629  N N   . GLY   A 1 104 ? 3.438   -29.725 -16.127 1.00 40.01  ? 104 GLY   A N   1 
ATOM   630  C CA  . GLY   A 1 104 ? 3.464   -30.501 -14.908 1.00 40.31  ? 104 GLY   A CA  1 
ATOM   631  C C   . GLY   A 1 104 ? 4.573   -31.527 -14.813 1.00 40.62  ? 104 GLY   A C   1 
ATOM   632  O O   . GLY   A 1 104 ? 4.689   -32.188 -13.773 1.00 43.06  ? 104 GLY   A O   1 
ATOM   633  N N   . PHE   A 1 105 ? 5.389   -31.687 -15.854 1.00 39.49  ? 105 PHE   A N   1 
ATOM   634  C CA  . PHE   A 1 105 ? 6.456   -32.679 -15.843 1.00 43.73  ? 105 PHE   A CA  1 
ATOM   635  C C   . PHE   A 1 105 ? 7.681   -32.129 -15.122 1.00 44.48  ? 105 PHE   A C   1 
ATOM   636  O O   . PHE   A 1 105 ? 8.157   -31.033 -15.437 1.00 45.01  ? 105 PHE   A O   1 
ATOM   637  C CB  . PHE   A 1 105 ? 6.826   -33.080 -17.270 1.00 42.91  ? 105 PHE   A CB  1 
ATOM   638  C CG  . PHE   A 1 105 ? 5.766   -33.877 -17.976 1.00 40.00  ? 105 PHE   A CG  1 
ATOM   639  C CD1 . PHE   A 1 105 ? 5.567   -35.212 -17.668 1.00 42.03  ? 105 PHE   A CD1 1 
ATOM   640  C CD2 . PHE   A 1 105 ? 4.981   -33.295 -18.957 1.00 39.00  ? 105 PHE   A CD2 1 
ATOM   641  C CE1 . PHE   A 1 105 ? 4.596   -35.951 -18.315 1.00 38.80  ? 105 PHE   A CE1 1 
ATOM   642  C CE2 . PHE   A 1 105 ? 4.008   -34.029 -19.610 1.00 40.89  ? 105 PHE   A CE2 1 
ATOM   643  C CZ  . PHE   A 1 105 ? 3.815   -35.360 -19.287 1.00 40.01  ? 105 PHE   A CZ  1 
ATOM   644  N N   . ALA   A 1 106 ? 8.192   -32.891 -14.150 1.00 45.39  ? 106 ALA   A N   1 
ATOM   645  C CA  . ALA   A 1 106 ? 9.427   -32.492 -13.480 1.00 41.17  ? 106 ALA   A CA  1 
ATOM   646  C C   . ALA   A 1 106 ? 10.595  -32.481 -14.456 1.00 42.28  ? 106 ALA   A C   1 
ATOM   647  O O   . ALA   A 1 106 ? 11.482  -31.624 -14.370 1.00 45.93  ? 106 ALA   A O   1 
ATOM   648  C CB  . ALA   A 1 106 ? 9.716   -33.422 -12.302 1.00 42.42  ? 106 ALA   A CB  1 
ATOM   649  N N   . GLU   A 1 107 ? 10.600  -33.424 -15.398 1.00 43.29  ? 107 GLU   A N   1 
ATOM   650  C CA  . GLU   A 1 107 ? 11.608  -33.448 -16.451 1.00 42.91  ? 107 GLU   A CA  1 
ATOM   651  C C   . GLU   A 1 107 ? 11.610  -32.156 -17.257 1.00 44.05  ? 107 GLU   A C   1 
ATOM   652  O O   . GLU   A 1 107 ? 12.653  -31.753 -17.783 1.00 48.93  ? 107 GLU   A O   1 
ATOM   653  C CB  . GLU   A 1 107 ? 11.369  -34.646 -17.377 1.00 42.90  ? 107 GLU   A CB  1 
ATOM   654  C CG  . GLU   A 1 107 ? 11.046  -35.986 -16.690 1.00 48.98  ? 107 GLU   A CG  1 
ATOM   655  C CD  . GLU   A 1 107 ? 9.638   -36.087 -16.091 1.00 56.60  ? 107 GLU   A CD  1 
ATOM   656  O OE1 . GLU   A 1 107 ? 9.073   -37.202 -16.118 1.00 56.43  ? 107 GLU   A OE1 1 
ATOM   657  O OE2 . GLU   A 1 107 ? 9.100   -35.073 -15.589 1.00 50.83  ? 107 GLU   A OE2 1 
ATOM   658  N N   . HIS   A 1 108 ? 10.460  -31.494 -17.365 1.00 43.98  ? 108 HIS   A N   1 
ATOM   659  C CA  . HIS   A 1 108 ? 10.324  -30.281 -18.159 1.00 47.21  ? 108 HIS   A CA  1 
ATOM   660  C C   . HIS   A 1 108 ? 10.176  -29.035 -17.297 1.00 45.61  ? 108 HIS   A C   1 
ATOM   661  O O   . HIS   A 1 108 ? 9.833   -27.970 -17.821 1.00 46.38  ? 108 HIS   A O   1 
ATOM   662  C CB  . HIS   A 1 108 ? 9.129   -30.410 -19.104 1.00 44.66  ? 108 HIS   A CB  1 
ATOM   663  C CG  . HIS   A 1 108 ? 9.260   -31.535 -20.082 1.00 46.20  ? 108 HIS   A CG  1 
ATOM   664  N ND1 . HIS   A 1 108 ? 10.477  -31.941 -20.586 1.00 44.37  ? 108 HIS   A ND1 1 
ATOM   665  C CD2 . HIS   A 1 108 ? 8.333   -32.355 -20.629 1.00 46.50  ? 108 HIS   A CD2 1 
ATOM   666  C CE1 . HIS   A 1 108 ? 10.292  -32.955 -21.412 1.00 44.86  ? 108 HIS   A CE1 1 
ATOM   667  N NE2 . HIS   A 1 108 ? 9.000   -33.226 -21.456 1.00 47.67  ? 108 HIS   A NE2 1 
ATOM   668  N N   . ALA   A 1 109 ? 10.439  -29.140 -15.991 1.00 45.53  ? 109 ALA   A N   1 
ATOM   669  C CA  . ALA   A 1 109 ? 10.220  -28.011 -15.093 1.00 45.44  ? 109 ALA   A CA  1 
ATOM   670  C C   . ALA   A 1 109 ? 11.092  -26.814 -15.457 1.00 47.14  ? 109 ALA   A C   1 
ATOM   671  O O   . ALA   A 1 109 ? 10.690  -25.666 -15.228 1.00 50.72  ? 109 ALA   A O   1 
ATOM   672  C CB  . ALA   A 1 109 ? 10.471  -28.437 -13.645 1.00 42.39  ? 109 ALA   A CB  1 
ATOM   673  N N   . ASP   A 1 110 ? 12.264  -27.055 -16.047 1.00 47.23  ? 110 ASP   A N   1 
ATOM   674  C CA  . ASP   A 1 110 ? 13.211  -25.997 -16.373 1.00 50.00  ? 110 ASP   A CA  1 
ATOM   675  C C   . ASP   A 1 110 ? 13.184  -25.592 -17.845 1.00 49.10  ? 110 ASP   A C   1 
ATOM   676  O O   . ASP   A 1 110 ? 14.049  -24.822 -18.274 1.00 52.11  ? 110 ASP   A O   1 
ATOM   677  C CB  . ASP   A 1 110 ? 14.637  -26.420 -15.994 1.00 52.49  ? 110 ASP   A CB  1 
ATOM   678  C CG  . ASP   A 1 110 ? 15.067  -27.728 -16.653 1.00 60.07  ? 110 ASP   A CG  1 
ATOM   679  O OD1 . ASP   A 1 110 ? 14.286  -28.707 -16.633 1.00 55.56  ? 110 ASP   A OD1 1 
ATOM   680  O OD2 . ASP   A 1 110 ? 16.190  -27.777 -17.195 1.00 76.86  ? 110 ASP   A OD2 1 
ATOM   681  N N   . HIS   A 1 111 ? 12.229  -26.091 -18.629 1.00 48.88  ? 111 HIS   A N   1 
ATOM   682  C CA  . HIS   A 1 111 ? 12.123  -25.696 -20.033 1.00 47.20  ? 111 HIS   A CA  1 
ATOM   683  C C   . HIS   A 1 111 ? 11.518  -24.299 -20.108 1.00 47.77  ? 111 HIS   A C   1 
ATOM   684  O O   . HIS   A 1 111 ? 10.329  -24.114 -19.830 1.00 46.95  ? 111 HIS   A O   1 
ATOM   685  C CB  . HIS   A 1 111 ? 11.287  -26.690 -20.834 1.00 47.88  ? 111 HIS   A CB  1 
ATOM   686  C CG  . HIS   A 1 111 ? 10.794  -26.140 -22.139 1.00 51.62  ? 111 HIS   A CG  1 
ATOM   687  N ND1 . HIS   A 1 111 ? 11.555  -26.162 -23.289 1.00 51.09  ? 111 HIS   A ND1 1 
ATOM   688  C CD2 . HIS   A 1 111 ? 9.620   -25.557 -22.476 1.00 48.81  ? 111 HIS   A CD2 1 
ATOM   689  C CE1 . HIS   A 1 111 ? 10.872  -25.612 -24.276 1.00 48.92  ? 111 HIS   A CE1 1 
ATOM   690  N NE2 . HIS   A 1 111 ? 9.694   -25.238 -23.810 1.00 48.69  ? 111 HIS   A NE2 1 
ATOM   691  N N   . ILE   A 1 112 ? 12.327  -23.321 -20.512 1.00 47.77  ? 112 ILE   A N   1 
ATOM   692  C CA  . ILE   A 1 112 ? 11.911  -21.926 -20.589 1.00 45.39  ? 112 ILE   A CA  1 
ATOM   693  C C   . ILE   A 1 112 ? 11.571  -21.591 -22.034 1.00 47.16  ? 112 ILE   A C   1 
ATOM   694  O O   . ILE   A 1 112 ? 12.340  -21.907 -22.951 1.00 48.71  ? 112 ILE   A O   1 
ATOM   695  C CB  . ILE   A 1 112 ? 13.006  -20.992 -20.046 1.00 44.78  ? 112 ILE   A CB  1 
ATOM   696  C CG1 . ILE   A 1 112 ? 13.505  -21.499 -18.694 1.00 47.83  ? 112 ILE   A CG1 1 
ATOM   697  C CG2 . ILE   A 1 112 ? 12.494  -19.566 -19.929 1.00 46.48  ? 112 ILE   A CG2 1 
ATOM   698  C CD1 . ILE   A 1 112 ? 12.440  -21.483 -17.624 1.00 47.83  ? 112 ILE   A CD1 1 
ATOM   699  N N   . ALA   A 1 113 ? 10.420  -20.955 -22.241 1.00 44.90  ? 113 ALA   A N   1 
ATOM   700  C CA  . ALA   A 1 113 ? 9.996   -20.588 -23.584 1.00 45.88  ? 113 ALA   A CA  1 
ATOM   701  C C   . ALA   A 1 113 ? 10.725  -19.336 -24.053 1.00 48.19  ? 113 ALA   A C   1 
ATOM   702  O O   . ALA   A 1 113 ? 10.912  -18.381 -23.293 1.00 45.69  ? 113 ALA   A O   1 
ATOM   703  C CB  . ALA   A 1 113 ? 8.485   -20.364 -23.632 1.00 43.14  ? 113 ALA   A CB  1 
ATOM   704  N N   . THR   A 1 114 ? 11.139  -19.348 -25.317 1.00 48.93  ? 114 THR   A N   1 
ATOM   705  C CA  . THR   A 1 114 ? 11.870  -18.237 -25.903 1.00 45.17  ? 114 THR   A CA  1 
ATOM   706  C C   . THR   A 1 114 ? 10.981  -17.280 -26.683 1.00 44.92  ? 114 THR   A C   1 
ATOM   707  O O   . THR   A 1 114 ? 11.449  -16.202 -27.066 1.00 49.59  ? 114 THR   A O   1 
ATOM   708  C CB  . THR   A 1 114 ? 12.979  -18.760 -26.824 1.00 46.43  ? 114 THR   A CB  1 
ATOM   709  O OG1 . THR   A 1 114 ? 12.427  -19.050 -28.112 1.00 51.58  ? 114 THR   A OG1 1 
ATOM   710  C CG2 . THR   A 1 114 ? 13.602  -20.029 -26.250 1.00 47.20  ? 114 THR   A CG2 1 
ATOM   711  N N   . ALA   A 1 115 ? 9.722   -17.640 -26.928 1.00 47.52  ? 115 ALA   A N   1 
ATOM   712  C CA  . ALA   A 1 115 ? 8.798   -16.775 -27.646 1.00 45.52  ? 115 ALA   A CA  1 
ATOM   713  C C   . ALA   A 1 115 ? 7.395   -16.965 -27.089 1.00 42.20  ? 115 ALA   A C   1 
ATOM   714  O O   . ALA   A 1 115 ? 7.051   -18.037 -26.582 1.00 43.64  ? 115 ALA   A O   1 
ATOM   715  C CB  . ALA   A 1 115 ? 8.812   -17.056 -29.154 1.00 41.61  ? 115 ALA   A CB  1 
ATOM   716  N N   . ASP   A 1 116 ? 6.586   -15.915 -27.191 1.00 41.57  ? 116 ASP   A N   1 
ATOM   717  C CA  . ASP   A 1 116 ? 5.204   -16.000 -26.744 1.00 41.22  ? 116 ASP   A CA  1 
ATOM   718  C C   . ASP   A 1 116 ? 4.399   -16.906 -27.666 1.00 42.83  ? 116 ASP   A C   1 
ATOM   719  O O   . ASP   A 1 116 ? 4.719   -17.073 -28.846 1.00 47.22  ? 116 ASP   A O   1 
ATOM   720  C CB  . ASP   A 1 116 ? 4.563   -14.613 -26.705 1.00 46.39  ? 116 ASP   A CB  1 
ATOM   721  C CG  . ASP   A 1 116 ? 5.023   -13.790 -25.520 1.00 47.82  ? 116 ASP   A CG  1 
ATOM   722  O OD1 . ASP   A 1 116 ? 5.461   -14.382 -24.509 1.00 47.03  ? 116 ASP   A OD1 1 
ATOM   723  O OD2 . ASP   A 1 116 ? 4.926   -12.547 -25.596 1.00 46.84  ? 116 ASP   A OD2 1 
ATOM   724  N N   . SER   A 1 117 ? 3.340   -17.495 -27.115 1.00 40.96  ? 117 SER   A N   1 
ATOM   725  C CA  . SER   A 1 117 ? 2.398   -18.246 -27.927 1.00 42.17  ? 117 SER   A CA  1 
ATOM   726  C C   . SER   A 1 117 ? 1.506   -17.290 -28.719 1.00 43.06  ? 117 SER   A C   1 
ATOM   727  O O   . SER   A 1 117 ? 1.440   -16.089 -28.442 1.00 43.61  ? 117 SER   A O   1 
ATOM   728  C CB  . SER   A 1 117 ? 1.552   -19.175 -27.051 1.00 39.18  ? 117 SER   A CB  1 
ATOM   729  O OG  . SER   A 1 117 ? 0.727   -18.449 -26.160 1.00 43.34  ? 117 SER   A OG  1 
ATOM   730  N N   . LEU   A 1 118 ? 0.821   -17.840 -29.725 1.00 40.66  ? 118 LEU   A N   1 
ATOM   731  C CA  . LEU   A 1 118 ? -0.044  -17.011 -30.560 1.00 42.62  ? 118 LEU   A CA  1 
ATOM   732  C C   . LEU   A 1 118 ? -1.137  -16.346 -29.732 1.00 43.69  ? 118 LEU   A C   1 
ATOM   733  O O   . LEU   A 1 118 ? -1.418  -15.154 -29.905 1.00 44.88  ? 118 LEU   A O   1 
ATOM   734  C CB  . LEU   A 1 118 ? -0.654  -17.853 -31.684 1.00 43.04  ? 118 LEU   A CB  1 
ATOM   735  C CG  . LEU   A 1 118 ? -1.327  -17.116 -32.852 1.00 42.62  ? 118 LEU   A CG  1 
ATOM   736  C CD1 . LEU   A 1 118 ? -2.826  -16.959 -32.632 1.00 39.46  ? 118 LEU   A CD1 1 
ATOM   737  C CD2 . LEU   A 1 118 ? -0.675  -15.762 -33.116 1.00 42.69  ? 118 LEU   A CD2 1 
ATOM   738  N N   . VAL   A 1 119 ? -1.756  -17.095 -28.818 1.00 42.02  ? 119 VAL   A N   1 
ATOM   739  C CA  . VAL   A 1 119 ? -2.852  -16.545 -28.024 1.00 41.20  ? 119 VAL   A CA  1 
ATOM   740  C C   . VAL   A 1 119 ? -2.340  -15.454 -27.090 1.00 39.80  ? 119 VAL   A C   1 
ATOM   741  O O   . VAL   A 1 119 ? -3.011  -14.437 -26.873 1.00 41.20  ? 119 VAL   A O   1 
ATOM   742  C CB  . VAL   A 1 119 ? -3.571  -17.677 -27.263 1.00 41.25  ? 119 VAL   A CB  1 
ATOM   743  C CG1 . VAL   A 1 119 ? -4.371  -17.132 -26.090 1.00 39.15  ? 119 VAL   A CG1 1 
ATOM   744  C CG2 . VAL   A 1 119 ? -4.480  -18.449 -28.211 1.00 38.20  ? 119 VAL   A CG2 1 
ATOM   745  N N   . VAL   A 1 120 ? -1.135  -15.632 -26.545 1.00 40.42  ? 120 VAL   A N   1 
ATOM   746  C CA  . VAL   A 1 120 ? -0.538  -14.599 -25.705 1.00 39.96  ? 120 VAL   A CA  1 
ATOM   747  C C   . VAL   A 1 120 ? -0.142  -13.389 -26.545 1.00 40.50  ? 120 VAL   A C   1 
ATOM   748  O O   . VAL   A 1 120 ? -0.332  -12.240 -26.129 1.00 41.95  ? 120 VAL   A O   1 
ATOM   749  C CB  . VAL   A 1 120 ? 0.660   -15.176 -24.926 1.00 40.96  ? 120 VAL   A CB  1 
ATOM   750  C CG1 . VAL   A 1 120 ? 1.517   -14.062 -24.346 1.00 39.16  ? 120 VAL   A CG1 1 
ATOM   751  C CG2 . VAL   A 1 120 ? 0.175   -16.106 -23.822 1.00 38.32  ? 120 VAL   A CG2 1 
ATOM   752  N N   . SER   A 1 121 ? 0.398   -13.624 -27.746 1.00 41.06  ? 121 SER   A N   1 
ATOM   753  C CA  . SER   A 1 121 ? 0.762   -12.515 -28.624 1.00 40.33  ? 121 SER   A CA  1 
ATOM   754  C C   . SER   A 1 121 ? -0.454  -11.673 -28.983 1.00 41.07  ? 121 SER   A C   1 
ATOM   755  O O   . SER   A 1 121 ? -0.381  -10.439 -29.008 1.00 43.33  ? 121 SER   A O   1 
ATOM   756  C CB  . SER   A 1 121 ? 1.432   -13.040 -29.895 1.00 43.21  ? 121 SER   A CB  1 
ATOM   757  O OG  . SER   A 1 121 ? 2.297   -14.122 -29.609 1.00 49.02  ? 121 SER   A OG  1 
ATOM   758  N N   . ARG   A 1 122 ? -1.582  -12.326 -29.267 1.00 40.78  ? 122 ARG   A N   1 
ATOM   759  C CA  . ARG   A 1 122 ? -2.800  -11.589 -29.581 1.00 40.97  ? 122 ARG   A CA  1 
ATOM   760  C C   . ARG   A 1 122 ? -3.291  -10.790 -28.380 1.00 41.95  ? 122 ARG   A C   1 
ATOM   761  O O   . ARG   A 1 122 ? -3.685  -9.627  -28.524 1.00 38.65  ? 122 ARG   A O   1 
ATOM   762  C CB  . ARG   A 1 122 ? -3.880  -12.552 -30.069 1.00 40.46  ? 122 ARG   A CB  1 
ATOM   763  C CG  . ARG   A 1 122 ? -3.540  -13.228 -31.387 1.00 43.11  ? 122 ARG   A CG  1 
ATOM   764  C CD  . ARG   A 1 122 ? -3.875  -12.322 -32.562 1.00 37.75  ? 122 ARG   A CD  1 
ATOM   765  N NE  . ARG   A 1 122 ? -4.071  -13.070 -33.798 1.00 44.28  ? 122 ARG   A NE  1 
ATOM   766  C CZ  . ARG   A 1 122 ? -5.255  -13.336 -34.335 1.00 39.46  ? 122 ARG   A CZ  1 
ATOM   767  N NH1 . ARG   A 1 122 ? -6.380  -12.952 -33.755 1.00 39.81  ? 122 ARG   A NH1 1 
ATOM   768  N NH2 . ARG   A 1 122 ? -5.310  -14.002 -35.484 1.00 38.27  ? 122 ARG   A NH2 1 
ATOM   769  N N   . LEU   A 1 123 ? -3.269  -11.387 -27.185 1.00 40.45  ? 123 LEU   A N   1 
ATOM   770  C CA  . LEU   A 1 123 ? -3.746  -10.669 -26.007 1.00 41.46  ? 123 LEU   A CA  1 
ATOM   771  C C   . LEU   A 1 123 ? -2.807  -9.535  -25.620 1.00 41.65  ? 123 LEU   A C   1 
ATOM   772  O O   . LEU   A 1 123 ? -3.268  -8.484  -25.164 1.00 42.82  ? 123 LEU   A O   1 
ATOM   773  C CB  . LEU   A 1 123 ? -3.942  -11.636 -24.841 1.00 40.16  ? 123 LEU   A CB  1 
ATOM   774  C CG  . LEU   A 1 123 ? -5.098  -12.610 -25.068 1.00 38.43  ? 123 LEU   A CG  1 
ATOM   775  C CD1 . LEU   A 1 123 ? -5.046  -13.761 -24.082 1.00 40.55  ? 123 LEU   A CD1 1 
ATOM   776  C CD2 . LEU   A 1 123 ? -6.424  -11.872 -24.977 1.00 35.18  ? 123 LEU   A CD2 1 
ATOM   777  N N   . LYS   A 1 124 ? -1.496  -9.716  -25.806 1.00 44.76  ? 124 LYS   A N   1 
ATOM   778  C CA  . LYS   A 1 124 ? -0.561  -8.627  -25.539 1.00 42.32  ? 124 LYS   A CA  1 
ATOM   779  C C   . LYS   A 1 124 ? -0.714  -7.492  -26.545 1.00 42.41  ? 124 LYS   A C   1 
ATOM   780  O O   . LYS   A 1 124 ? -0.522  -6.323  -26.189 1.00 44.44  ? 124 LYS   A O   1 
ATOM   781  C CB  . LYS   A 1 124 ? 0.874   -9.155  -25.533 1.00 41.57  ? 124 LYS   A CB  1 
ATOM   782  C CG  . LYS   A 1 124 ? 1.225   -9.953  -24.285 1.00 43.38  ? 124 LYS   A CG  1 
ATOM   783  C CD  . LYS   A 1 124 ? 2.654   -10.463 -24.324 1.00 42.89  ? 124 LYS   A CD  1 
ATOM   784  C CE  . LYS   A 1 124 ? 3.103   -10.926 -22.947 1.00 44.21  ? 124 LYS   A CE  1 
ATOM   785  N NZ  . LYS   A 1 124 ? 4.359   -11.716 -23.010 1.00 43.63  ? 124 LYS   A NZ  1 
ATOM   786  N N   . ALA   A 1 125 ? -1.056  -7.810  -27.798 1.00 39.29  ? 125 ALA   A N   1 
ATOM   787  C CA  . ALA   A 1 125 ? -1.318  -6.763  -28.781 1.00 41.28  ? 125 ALA   A CA  1 
ATOM   788  C C   . ALA   A 1 125 ? -2.602  -6.011  -28.463 1.00 40.19  ? 125 ALA   A C   1 
ATOM   789  O O   . ALA   A 1 125 ? -2.718  -4.822  -28.781 1.00 42.53  ? 125 ALA   A O   1 
ATOM   790  C CB  . ALA   A 1 125 ? -1.384  -7.357  -30.187 1.00 35.96  ? 125 ALA   A CB  1 
ATOM   791  N N   . ALA   A 1 126 ? -3.571  -6.683  -27.842 1.00 39.71  ? 126 ALA   A N   1 
ATOM   792  C CA  . ALA   A 1 126 ? -4.732  -6.005  -27.284 1.00 42.01  ? 126 ALA   A CA  1 
ATOM   793  C C   . ALA   A 1 126 ? -4.397  -5.227  -26.019 1.00 42.33  ? 126 ALA   A C   1 
ATOM   794  O O   . ALA   A 1 126 ? -5.286  -4.575  -25.462 1.00 42.47  ? 126 ALA   A O   1 
ATOM   795  C CB  . ALA   A 1 126 ? -5.844  -7.019  -27.000 1.00 42.15  ? 126 ALA   A CB  1 
ATOM   796  N N   . GLY   A 1 127 ? -3.150  -5.286  -25.553 1.00 40.66  ? 127 GLY   A N   1 
ATOM   797  C CA  . GLY   A 1 127 ? -2.703  -4.504  -24.421 1.00 43.49  ? 127 GLY   A CA  1 
ATOM   798  C C   . GLY   A 1 127 ? -2.694  -5.223  -23.090 1.00 42.68  ? 127 GLY   A C   1 
ATOM   799  O O   . GLY   A 1 127 ? -2.373  -4.595  -22.074 1.00 45.17  ? 127 GLY   A O   1 
ATOM   800  N N   . ALA   A 1 128 ? -3.024  -6.512  -23.060 1.00 41.03  ? 128 ALA   A N   1 
ATOM   801  C CA  . ALA   A 1 128 ? -3.127  -7.232  -21.799 1.00 43.62  ? 128 ALA   A CA  1 
ATOM   802  C C   . ALA   A 1 128 ? -1.761  -7.395  -21.138 1.00 45.27  ? 128 ALA   A C   1 
ATOM   803  O O   . ALA   A 1 128 ? -0.718  -7.433  -21.798 1.00 44.96  ? 128 ALA   A O   1 
ATOM   804  C CB  . ALA   A 1 128 ? -3.767  -8.603  -22.017 1.00 42.53  ? 128 ALA   A CB  1 
ATOM   805  N N   . VAL   A 1 129 ? -1.782  -7.493  -19.812 1.00 44.94  ? 129 VAL   A N   1 
ATOM   806  C CA  . VAL   A 1 129 ? -0.583  -7.652  -18.997 1.00 42.19  ? 129 VAL   A CA  1 
ATOM   807  C C   . VAL   A 1 129 ? -0.669  -9.005  -18.305 1.00 44.60  ? 129 VAL   A C   1 
ATOM   808  O O   . VAL   A 1 129 ? -1.635  -9.277  -17.582 1.00 42.56  ? 129 VAL   A O   1 
ATOM   809  C CB  . VAL   A 1 129 ? -0.440  -6.520  -17.970 1.00 39.03  ? 129 VAL   A CB  1 
ATOM   810  C CG1 . VAL   A 1 129 ? 0.667   -6.839  -16.984 1.00 44.16  ? 129 VAL   A CG1 1 
ATOM   811  C CG2 . VAL   A 1 129 ? -0.176  -5.201  -18.670 1.00 43.69  ? 129 VAL   A CG2 1 
ATOM   812  N N   . PHE   A 1 130 ? 0.339   -9.846  -18.519 1.00 45.17  ? 130 PHE   A N   1 
ATOM   813  C CA  . PHE   A 1 130 ? 0.349   -11.209 -18.000 1.00 45.59  ? 130 PHE   A CA  1 
ATOM   814  C C   . PHE   A 1 130 ? 1.163   -11.259 -16.710 1.00 46.31  ? 130 PHE   A C   1 
ATOM   815  O O   . PHE   A 1 130 ? 2.368   -10.984 -16.721 1.00 45.33  ? 130 PHE   A O   1 
ATOM   816  C CB  . PHE   A 1 130 ? 0.912   -12.175 -19.044 1.00 41.73  ? 130 PHE   A CB  1 
ATOM   817  C CG  . PHE   A 1 130 ? -0.057  -12.508 -20.144 1.00 42.64  ? 130 PHE   A CG  1 
ATOM   818  C CD1 . PHE   A 1 130 ? -0.197  -11.675 -21.241 1.00 39.67  ? 130 PHE   A CD1 1 
ATOM   819  C CD2 . PHE   A 1 130 ? -0.840  -13.647 -20.074 1.00 43.13  ? 130 PHE   A CD2 1 
ATOM   820  C CE1 . PHE   A 1 130 ? -1.091  -11.978 -22.246 1.00 40.92  ? 130 PHE   A CE1 1 
ATOM   821  C CE2 . PHE   A 1 130 ? -1.739  -13.952 -21.080 1.00 39.24  ? 130 PHE   A CE2 1 
ATOM   822  C CZ  . PHE   A 1 130 ? -1.863  -13.118 -22.165 1.00 38.38  ? 130 PHE   A CZ  1 
ATOM   823  N N   . LEU   A 1 131 ? 0.499   -11.608 -15.603 1.00 45.60  ? 131 LEU   A N   1 
ATOM   824  C CA  . LEU   A 1 131 ? 1.147   -11.694 -14.297 1.00 45.33  ? 131 LEU   A CA  1 
ATOM   825  C C   . LEU   A 1 131 ? 1.826   -13.033 -14.057 1.00 44.31  ? 131 LEU   A C   1 
ATOM   826  O O   . LEU   A 1 131 ? 2.775   -13.106 -13.267 1.00 45.03  ? 131 LEU   A O   1 
ATOM   827  C CB  . LEU   A 1 131 ? 0.129   -11.466 -13.179 1.00 42.51  ? 131 LEU   A CB  1 
ATOM   828  C CG  . LEU   A 1 131 ? -0.800  -10.264 -13.290 1.00 45.04  ? 131 LEU   A CG  1 
ATOM   829  C CD1 . LEU   A 1 131 ? -2.151  -10.598 -12.682 1.00 43.85  ? 131 LEU   A CD1 1 
ATOM   830  C CD2 . LEU   A 1 131 ? -0.183  -9.062  -12.606 1.00 44.85  ? 131 LEU   A CD2 1 
ATOM   831  N N   . GLY   A 1 132 ? 1.355   -14.092 -14.707 1.00 42.32  ? 132 GLY   A N   1 
ATOM   832  C CA  . GLY   A 1 132 ? 1.891   -15.415 -14.457 1.00 42.97  ? 132 GLY   A CA  1 
ATOM   833  C C   . GLY   A 1 132 ? 1.046   -16.468 -15.144 1.00 41.82  ? 132 GLY   A C   1 
ATOM   834  O O   . GLY   A 1 132 ? 0.266   -16.163 -16.047 1.00 41.20  ? 132 GLY   A O   1 
ATOM   835  N N   . LYS   A 1 133 ? 1.209   -17.712 -14.697 1.00 39.81  ? 133 LYS   A N   1 
ATOM   836  C CA  . LYS   A 1 133 ? 0.542   -18.836 -15.336 1.00 39.44  ? 133 LYS   A CA  1 
ATOM   837  C C   . LYS   A 1 133 ? -0.130  -19.718 -14.291 1.00 41.84  ? 133 LYS   A C   1 
ATOM   838  O O   . LYS   A 1 133 ? 0.333   -19.819 -13.151 1.00 40.08  ? 133 LYS   A O   1 
ATOM   839  C CB  . LYS   A 1 133 ? 1.534   -19.640 -16.178 1.00 40.31  ? 133 LYS   A CB  1 
ATOM   840  C CG  . LYS   A 1 133 ? 1.657   -19.108 -17.601 1.00 38.97  ? 133 LYS   A CG  1 
ATOM   841  C CD  . LYS   A 1 133 ? 3.052   -19.297 -18.138 1.00 39.15  ? 133 LYS   A CD  1 
ATOM   842  C CE  . LYS   A 1 133 ? 3.158   -20.613 -18.857 1.00 36.91  ? 133 LYS   A CE  1 
ATOM   843  N NZ  . LYS   A 1 133 ? 4.498   -20.884 -19.429 1.00 42.05  ? 133 LYS   A NZ  1 
ATOM   844  N N   . SER   A 1 134 ? -1.232  -20.352 -14.692 1.00 37.49  ? 134 SER   A N   1 
ATOM   845  C CA  . SER   A 1 134 ? -2.090  -21.102 -13.783 1.00 39.31  ? 134 SER   A CA  1 
ATOM   846  C C   . SER   A 1 134 ? -1.822  -22.603 -13.862 1.00 37.14  ? 134 SER   A C   1 
ATOM   847  O O   . SER   A 1 134 ? -1.319  -23.124 -14.859 1.00 35.58  ? 134 SER   A O   1 
ATOM   848  C CB  . SER   A 1 134 ? -3.566  -20.822 -14.073 1.00 38.29  ? 134 SER   A CB  1 
ATOM   849  O OG  . SER   A 1 134 ? -3.859  -20.980 -15.449 1.00 40.98  ? 134 SER   A OG  1 
ATOM   850  N N   . ASN   A 1 135 ? -2.212  -23.297 -12.796 1.00 38.38  ? 135 ASN   A N   1 
ATOM   851  C CA  . ASN   A 1 135 ? -1.771  -24.656 -12.521 1.00 38.03  ? 135 ASN   A CA  1 
ATOM   852  C C   . ASN   A 1 135 ? -2.473  -25.683 -13.406 1.00 37.38  ? 135 ASN   A C   1 
ATOM   853  O O   . ASN   A 1 135 ? -3.578  -25.467 -13.911 1.00 36.32  ? 135 ASN   A O   1 
ATOM   854  C CB  . ASN   A 1 135 ? -2.009  -24.998 -11.054 1.00 39.73  ? 135 ASN   A CB  1 
ATOM   855  C CG  . ASN   A 1 135 ? -1.189  -26.176 -10.596 1.00 35.03  ? 135 ASN   A CG  1 
ATOM   856  O OD1 . ASN   A 1 135 ? -0.114  -26.441 -11.134 1.00 36.59  ? 135 ASN   A OD1 1 
ATOM   857  N ND2 . ASN   A 1 135 ? -1.690  -26.897 -9.595  1.00 35.62  ? 135 ASN   A ND2 1 
ATOM   858  N N   . ILE   A 1 136 ? -1.814  -26.829 -13.558 1.00 39.91  ? 136 ILE   A N   1 
ATOM   859  C CA  . ILE   A 1 136 ? -2.216  -27.896 -14.473 1.00 37.86  ? 136 ILE   A CA  1 
ATOM   860  C C   . ILE   A 1 136 ? -1.864  -29.250 -13.859 1.00 39.62  ? 136 ILE   A C   1 
ATOM   861  O O   . ILE   A 1 136 ? -1.026  -29.310 -12.948 1.00 42.46  ? 136 ILE   A O   1 
ATOM   862  C CB  . ILE   A 1 136 ? -1.566  -27.700 -15.860 1.00 35.59  ? 136 ILE   A CB  1 
ATOM   863  C CG1 . ILE   A 1 136 ? -0.133  -27.141 -15.784 1.00 41.29  ? 136 ILE   A CG1 1 
ATOM   864  C CG2 . ILE   A 1 136 ? -2.355  -26.724 -16.682 1.00 36.67  ? 136 ILE   A CG2 1 
ATOM   865  C CD1 . ILE   A 1 136 ? 0.897   -28.007 -15.128 1.00 41.24  ? 136 ILE   A CD1 1 
ATOM   866  N N   . PRO   A 1 137 ? -2.504  -30.343 -14.277 1.00 40.26  ? 137 PRO   A N   1 
ATOM   867  C CA  . PRO   A 1 137 ? -2.018  -31.680 -13.928 1.00 39.44  ? 137 PRO   A CA  1 
ATOM   868  C C   . PRO   A 1 137 ? -0.920  -32.117 -14.886 1.00 39.59  ? 137 PRO   A C   1 
ATOM   869  O O   . PRO   A 1 137 ? -0.672  -31.496 -15.920 1.00 41.28  ? 137 PRO   A O   1 
ATOM   870  C CB  . PRO   A 1 137 ? -3.261  -32.562 -14.085 1.00 39.41  ? 137 PRO   A CB  1 
ATOM   871  C CG  . PRO   A 1 137 ? -4.033  -31.896 -15.157 1.00 42.68  ? 137 PRO   A CG  1 
ATOM   872  C CD  . PRO   A 1 137 ? -3.821  -30.408 -14.919 1.00 39.10  ? 137 PRO   A CD  1 
ATOM   873  N N   . VAL   A 1 138 ? -0.269  -33.224 -14.523 1.00 41.16  ? 138 VAL   A N   1 
ATOM   874  C CA  . VAL   A 1 138 ? 0.823   -33.758 -15.330 1.00 40.73  ? 138 VAL   A CA  1 
ATOM   875  C C   . VAL   A 1 138 ? 0.298   -34.140 -16.706 1.00 39.49  ? 138 VAL   A C   1 
ATOM   876  O O   . VAL   A 1 138 ? -0.626  -34.953 -16.834 1.00 39.53  ? 138 VAL   A O   1 
ATOM   877  C CB  . VAL   A 1 138 ? 1.477   -34.955 -14.628 1.00 38.24  ? 138 VAL   A CB  1 
ATOM   878  C CG1 . VAL   A 1 138 ? 2.802   -35.300 -15.289 1.00 36.95  ? 138 VAL   A CG1 1 
ATOM   879  C CG2 . VAL   A 1 138 ? 1.679   -34.661 -13.150 1.00 34.68  ? 138 VAL   A CG2 1 
ATOM   880  N N   . GLY   A 1 139 ? 0.887   -33.555 -17.747 1.00 42.12  ? 139 GLY   A N   1 
ATOM   881  C CA  . GLY   A 1 139 ? 0.506   -33.894 -19.104 1.00 40.56  ? 139 GLY   A CA  1 
ATOM   882  C C   . GLY   A 1 139 ? -0.875  -33.442 -19.509 1.00 40.68  ? 139 GLY   A C   1 
ATOM   883  O O   . GLY   A 1 139 ? -1.378  -33.883 -20.546 1.00 39.87  ? 139 GLY   A O   1 
ATOM   884  N N   . LEU   A 1 140 ? -1.501  -32.567 -18.716 1.00 45.79  ? 140 LEU   A N   1 
ATOM   885  C CA  . LEU   A 1 140 ? -2.852  -32.070 -18.981 1.00 41.21  ? 140 LEU   A CA  1 
ATOM   886  C C   . LEU   A 1 140 ? -3.836  -33.222 -19.152 1.00 40.31  ? 140 LEU   A C   1 
ATOM   887  O O   . LEU   A 1 140 ? -4.730  -33.184 -20.000 1.00 43.61  ? 140 LEU   A O   1 
ATOM   888  C CB  . LEU   A 1 140 ? -2.876  -31.150 -20.204 1.00 42.69  ? 140 LEU   A CB  1 
ATOM   889  C CG  . LEU   A 1 140 ? -1.731  -30.154 -20.403 1.00 43.33  ? 140 LEU   A CG  1 
ATOM   890  C CD1 . LEU   A 1 140 ? -2.026  -29.250 -21.586 1.00 42.20  ? 140 LEU   A CD1 1 
ATOM   891  C CD2 . LEU   A 1 140 ? -1.503  -29.326 -19.153 1.00 38.97  ? 140 LEU   A CD2 1 
ATOM   892  N N   . ALA   A 1 141 ? -3.676  -34.259 -18.329 1.00 41.55  ? 141 ALA   A N   1 
ATOM   893  C CA  . ALA   A 1 141 ? -4.392  -35.515 -18.523 1.00 45.91  ? 141 ALA   A CA  1 
ATOM   894  C C   . ALA   A 1 141 ? -5.246  -35.894 -17.318 1.00 42.75  ? 141 ALA   A C   1 
ATOM   895  O O   . ALA   A 1 141 ? -5.400  -37.078 -17.013 1.00 46.76  ? 141 ALA   A O   1 
ATOM   896  C CB  . ALA   A 1 141 ? -3.415  -36.645 -18.844 1.00 40.87  ? 141 ALA   A CB  1 
ATOM   897  N N   . ASP   A 1 142 ? -5.814  -34.910 -16.626 1.00 41.82  ? 142 ASP   A N   1 
ATOM   898  C CA  . ASP   A 1 142 ? -6.700  -35.191 -15.507 1.00 41.70  ? 142 ASP   A CA  1 
ATOM   899  C C   . ASP   A 1 142 ? -7.787  -34.131 -15.432 1.00 41.02  ? 142 ASP   A C   1 
ATOM   900  O O   . ASP   A 1 142 ? -7.684  -33.061 -16.034 1.00 40.63  ? 142 ASP   A O   1 
ATOM   901  C CB  . ASP   A 1 142 ? -5.940  -35.258 -14.173 1.00 39.94  ? 142 ASP   A CB  1 
ATOM   902  C CG  . ASP   A 1 142 ? -6.662  -36.102 -13.131 1.00 44.25  ? 142 ASP   A CG  1 
ATOM   903  O OD1 . ASP   A 1 142 ? -7.851  -36.418 -13.342 1.00 40.96  ? 142 ASP   A OD1 1 
ATOM   904  O OD2 . ASP   A 1 142 ? -6.049  -36.438 -12.096 1.00 42.20  ? 142 ASP   A OD2 1 
ATOM   905  N N   . TRP   A 1 143 ? -8.851  -34.468 -14.698 1.00 41.54  ? 143 TRP   A N   1 
ATOM   906  C CA  . TRP   A 1 143 ? -9.898  -33.528 -14.322 1.00 41.24  ? 143 TRP   A CA  1 
ATOM   907  C C   . TRP   A 1 143 ? -9.628  -32.884 -12.966 1.00 40.07  ? 143 TRP   A C   1 
ATOM   908  O O   . TRP   A 1 143 ? -10.564 -32.461 -12.276 1.00 40.27  ? 143 TRP   A O   1 
ATOM   909  C CB  . TRP   A 1 143 ? -11.260 -34.225 -14.341 1.00 40.95  ? 143 TRP   A CB  1 
ATOM   910  C CG  . TRP   A 1 143 ? -11.852 -34.307 -15.726 1.00 40.94  ? 143 TRP   A CG  1 
ATOM   911  C CD1 . TRP   A 1 143 ? -11.472 -33.590 -16.826 1.00 38.53  ? 143 TRP   A CD1 1 
ATOM   912  C CD2 . TRP   A 1 143 ? -12.902 -35.181 -16.163 1.00 39.72  ? 143 TRP   A CD2 1 
ATOM   913  N NE1 . TRP   A 1 143 ? -12.230 -33.953 -17.914 1.00 38.08  ? 143 TRP   A NE1 1 
ATOM   914  C CE2 . TRP   A 1 143 ? -13.113 -34.929 -17.535 1.00 37.16  ? 143 TRP   A CE2 1 
ATOM   915  C CE3 . TRP   A 1 143 ? -13.687 -36.147 -15.527 1.00 38.13  ? 143 TRP   A CE3 1 
ATOM   916  C CZ2 . TRP   A 1 143 ? -14.078 -35.605 -18.279 1.00 38.16  ? 143 TRP   A CZ2 1 
ATOM   917  C CZ3 . TRP   A 1 143 ? -14.644 -36.819 -16.269 1.00 41.37  ? 143 TRP   A CZ3 1 
ATOM   918  C CH2 . TRP   A 1 143 ? -14.831 -36.545 -17.630 1.00 41.79  ? 143 TRP   A CH2 1 
ATOM   919  N N   . GLN   A 1 144 ? -8.359  -32.817 -12.570 1.00 37.52  ? 144 GLN   A N   1 
ATOM   920  C CA  . GLN   A 1 144 ? -7.911  -32.016 -11.444 1.00 41.10  ? 144 GLN   A CA  1 
ATOM   921  C C   . GLN   A 1 144 ? -6.550  -31.442 -11.816 1.00 38.97  ? 144 GLN   A C   1 
ATOM   922  O O   . GLN   A 1 144 ? -5.960  -31.821 -12.827 1.00 41.25  ? 144 GLN   A O   1 
ATOM   923  C CB  . GLN   A 1 144 ? -7.883  -32.837 -10.150 1.00 39.20  ? 144 GLN   A CB  1 
ATOM   924  C CG  . GLN   A 1 144 ? -7.009  -34.065 -10.205 1.00 42.58  ? 144 GLN   A CG  1 
ATOM   925  C CD  . GLN   A 1 144 ? -7.410  -35.113 -9.181  1.00 43.71  ? 144 GLN   A CD  1 
ATOM   926  O OE1 . GLN   A 1 144 ? -8.067  -34.809 -8.185  1.00 41.97  ? 144 GLN   A OE1 1 
ATOM   927  N NE2 . GLN   A 1 144 ? -7.010  -36.356 -9.422  1.00 39.74  ? 144 GLN   A NE2 1 
ATOM   928  N N   . SER   A 1 145 ? -6.063  -30.496 -11.013 1.00 37.84  ? 145 SER   A N   1 
ATOM   929  C CA  . SER   A 1 145 ? -4.825  -29.773 -11.321 1.00 38.97  ? 145 SER   A CA  1 
ATOM   930  C C   . SER   A 1 145 ? -3.821  -29.970 -10.191 1.00 40.13  ? 145 SER   A C   1 
ATOM   931  O O   . SER   A 1 145 ? -3.882  -29.286 -9.163  1.00 36.59  ? 145 SER   A O   1 
ATOM   932  C CB  . SER   A 1 145 ? -5.096  -28.291 -11.564 1.00 37.96  ? 145 SER   A CB  1 
ATOM   933  O OG  . SER   A 1 145 ? -5.904  -28.109 -12.710 1.00 41.11  ? 145 SER   A OG  1 
ATOM   934  N N   . VAL   A 1 146 ? -2.883  -30.889 -10.403 1.00 40.92  ? 146 VAL   A N   1 
ATOM   935  C CA  . VAL   A 1 146 ? -1.874  -31.229 -9.408  1.00 37.17  ? 146 VAL   A CA  1 
ATOM   936  C C   . VAL   A 1 146 ? -0.703  -31.873 -10.137 1.00 41.27  ? 146 VAL   A C   1 
ATOM   937  O O   . VAL   A 1 146 ? -0.893  -32.646 -11.079 1.00 43.64  ? 146 VAL   A O   1 
ATOM   938  C CB  . VAL   A 1 146 ? -2.465  -32.155 -8.318  1.00 39.55  ? 146 VAL   A CB  1 
ATOM   939  C CG1 . VAL   A 1 146 ? -3.226  -33.305 -8.963  1.00 38.09  ? 146 VAL   A CG1 1 
ATOM   940  C CG2 . VAL   A 1 146 ? -1.378  -32.666 -7.386  1.00 37.76  ? 146 VAL   A CG2 1 
ATOM   941  N N   . ASN   A 1 147 ? 0.507   -31.542 -9.704  1.00 41.93  ? 147 ASN   A N   1 
ATOM   942  C CA  . ASN   A 1 147 ? 1.717   -31.979 -10.387 1.00 39.39  ? 147 ASN   A CA  1 
ATOM   943  C C   . ASN   A 1 147 ? 2.904   -31.773 -9.445  1.00 41.10  ? 147 ASN   A C   1 
ATOM   944  O O   . ASN   A 1 147 ? 2.797   -31.024 -8.469  1.00 39.49  ? 147 ASN   A O   1 
ATOM   945  C CB  . ASN   A 1 147 ? 1.925   -31.207 -11.697 1.00 33.52  ? 147 ASN   A CB  1 
ATOM   946  C CG  . ASN   A 1 147 ? 2.296   -29.763 -11.462 1.00 42.35  ? 147 ASN   A CG  1 
ATOM   947  O OD1 . ASN   A 1 147 ? 3.478   -29.422 -11.354 1.00 41.18  ? 147 ASN   A OD1 1 
ATOM   948  N ND2 . ASN   A 1 147 ? 1.286   -28.899 -11.381 1.00 39.52  ? 147 ASN   A ND2 1 
ATOM   949  N N   . PRO   A 1 148 ? 4.037   -32.428 -9.722  1.00 40.40  ? 148 PRO   A N   1 
ATOM   950  C CA  . PRO   A 1 148 ? 5.186   -32.314 -8.805  1.00 37.90  ? 148 PRO   A CA  1 
ATOM   951  C C   . PRO   A 1 148 ? 5.867   -30.953 -8.802  1.00 37.32  ? 148 PRO   A C   1 
ATOM   952  O O   . PRO   A 1 148 ? 6.492   -30.600 -7.794  1.00 40.06  ? 148 PRO   A O   1 
ATOM   953  C CB  . PRO   A 1 148 ? 6.135   -33.414 -9.306  1.00 40.49  ? 148 PRO   A CB  1 
ATOM   954  C CG  . PRO   A 1 148 ? 5.744   -33.617 -10.742 1.00 39.73  ? 148 PRO   A CG  1 
ATOM   955  C CD  . PRO   A 1 148 ? 4.256   -33.472 -10.739 1.00 34.80  ? 148 PRO   A CD  1 
ATOM   956  N N   . ASN   A 1 149 ? 5.790   -30.178 -9.887  1.00 40.14  ? 149 ASN   A N   1 
ATOM   957  C CA  . ASN   A 1 149 ? 6.497   -28.900 -9.919  1.00 39.26  ? 149 ASN   A CA  1 
ATOM   958  C C   . ASN   A 1 149 ? 5.818   -27.827 -9.080  1.00 40.55  ? 149 ASN   A C   1 
ATOM   959  O O   . ASN   A 1 149 ? 6.500   -26.952 -8.536  1.00 40.93  ? 149 ASN   A O   1 
ATOM   960  C CB  . ASN   A 1 149 ? 6.638   -28.387 -11.353 1.00 39.19  ? 149 ASN   A CB  1 
ATOM   961  C CG  . ASN   A 1 149 ? 7.180   -29.433 -12.295 1.00 42.06  ? 149 ASN   A CG  1 
ATOM   962  O OD1 . ASN   A 1 149 ? 7.984   -30.276 -11.899 1.00 38.08  ? 149 ASN   A OD1 1 
ATOM   963  N ND2 . ASN   A 1 149 ? 6.767   -29.366 -13.558 1.00 42.34  ? 149 ASN   A ND2 1 
ATOM   964  N N   . TYR   A 1 150 ? 4.493   -27.869 -8.965  1.00 41.73  ? 150 TYR   A N   1 
ATOM   965  C CA  . TYR   A 1 150 ? 3.736   -26.748 -8.432  1.00 42.94  ? 150 TYR   A CA  1 
ATOM   966  C C   . TYR   A 1 150 ? 2.841   -27.096 -7.255  1.00 39.94  ? 150 TYR   A C   1 
ATOM   967  O O   . TYR   A 1 150 ? 2.476   -26.192 -6.496  1.00 40.17  ? 150 TYR   A O   1 
ATOM   968  C CB  . TYR   A 1 150 ? 2.873   -26.128 -9.541  1.00 39.87  ? 150 TYR   A CB  1 
ATOM   969  C CG  . TYR   A 1 150 ? 3.662   -25.681 -10.753 1.00 38.86  ? 150 TYR   A CG  1 
ATOM   970  C CD1 . TYR   A 1 150 ? 4.716   -24.785 -10.629 1.00 40.84  ? 150 TYR   A CD1 1 
ATOM   971  C CD2 . TYR   A 1 150 ? 3.364   -26.170 -12.021 1.00 41.05  ? 150 TYR   A CD2 1 
ATOM   972  C CE1 . TYR   A 1 150 ? 5.444   -24.379 -11.734 1.00 41.41  ? 150 TYR   A CE1 1 
ATOM   973  C CE2 . TYR   A 1 150 ? 4.089   -25.772 -13.132 1.00 37.26  ? 150 TYR   A CE2 1 
ATOM   974  C CZ  . TYR   A 1 150 ? 5.127   -24.876 -12.981 1.00 41.42  ? 150 TYR   A CZ  1 
ATOM   975  O OH  . TYR   A 1 150 ? 5.855   -24.472 -14.076 1.00 40.98  ? 150 TYR   A OH  1 
ATOM   976  N N   . GLY   A 1 151 ? 2.486   -28.361 -7.071  1.00 40.07  ? 151 GLY   A N   1 
ATOM   977  C CA  . GLY   A 1 151 ? 1.556   -28.722 -6.025  1.00 39.16  ? 151 GLY   A CA  1 
ATOM   978  C C   . GLY   A 1 151 ? 0.155   -28.909 -6.560  1.00 37.37  ? 151 GLY   A C   1 
ATOM   979  O O   . GLY   A 1 151 ? -0.028  -29.190 -7.751  1.00 35.96  ? 151 GLY   A O   1 
ATOM   980  N N   . ARG   A 1 152 ? -0.842  -28.741 -5.695  1.00 38.73  ? 152 ARG   A N   1 
ATOM   981  C CA  . ARG   A 1 152 ? -2.235  -28.980 -6.041  1.00 39.48  ? 152 ARG   A CA  1 
ATOM   982  C C   . ARG   A 1 152 ? -3.041  -27.695 -5.920  1.00 37.19  ? 152 ARG   A C   1 
ATOM   983  O O   . ARG   A 1 152 ? -2.817  -26.889 -5.011  1.00 35.34  ? 152 ARG   A O   1 
ATOM   984  C CB  . ARG   A 1 152 ? -2.843  -30.064 -5.138  1.00 38.81  ? 152 ARG   A CB  1 
ATOM   985  C CG  . ARG   A 1 152 ? -4.317  -30.327 -5.408  1.00 37.12  ? 152 ARG   A CG  1 
ATOM   986  C CD  . ARG   A 1 152 ? -4.938  -31.223 -4.348  1.00 40.36  ? 152 ARG   A CD  1 
ATOM   987  N NE  . ARG   A 1 152 ? -5.088  -30.570 -3.052  1.00 37.37  ? 152 ARG   A NE  1 
ATOM   988  C CZ  . ARG   A 1 152 ? -5.168  -31.220 -1.899  1.00 36.82  ? 152 ARG   A CZ  1 
ATOM   989  N NH1 . ARG   A 1 152 ? -5.064  -32.536 -1.840  1.00 40.81  ? 152 ARG   A NH1 1 
ATOM   990  N NH2 . ARG   A 1 152 ? -5.370  -30.533 -0.778  1.00 35.27  ? 152 ARG   A NH2 1 
ATOM   991  N N   . THR   A 1 153 ? -3.980  -27.511 -6.843  1.00 38.80  ? 153 THR   A N   1 
ATOM   992  C CA  . THR   A 1 153 ? -4.948  -26.425 -6.773  1.00 36.62  ? 153 THR   A CA  1 
ATOM   993  C C   . THR   A 1 153 ? -6.220  -26.931 -6.105  1.00 37.08  ? 153 THR   A C   1 
ATOM   994  O O   . THR   A 1 153 ? -6.734  -27.996 -6.464  1.00 36.96  ? 153 THR   A O   1 
ATOM   995  C CB  . THR   A 1 153 ? -5.265  -25.875 -8.166  1.00 33.80  ? 153 THR   A CB  1 
ATOM   996  O OG1 . THR   A 1 153 ? -4.067  -25.351 -8.744  1.00 38.96  ? 153 THR   A OG1 1 
ATOM   997  C CG2 . THR   A 1 153 ? -6.296  -24.754 -8.077  1.00 33.93  ? 153 THR   A CG2 1 
ATOM   998  N N   . ASN   A 1 154 ? -6.723  -26.170 -5.140  1.00 36.06  ? 154 ASN   A N   1 
ATOM   999  C CA  . ASN   A 1 154 ? -7.923  -26.540 -4.406  1.00 36.91  ? 154 ASN   A CA  1 
ATOM   1000 C C   . ASN   A 1 154 ? -9.094  -25.660 -4.821  1.00 35.83  ? 154 ASN   A C   1 
ATOM   1001 O O   . ASN   A 1 154 ? -8.933  -24.455 -5.040  1.00 38.80  ? 154 ASN   A O   1 
ATOM   1002 C CB  . ASN   A 1 154 ? -7.688  -26.436 -2.901  1.00 35.78  ? 154 ASN   A CB  1 
ATOM   1003 C CG  . ASN   A 1 154 ? -6.457  -27.199 -2.457  1.00 39.03  ? 154 ASN   A CG  1 
ATOM   1004 O OD1 . ASN   A 1 154 ? -6.455  -28.430 -2.434  1.00 37.03  ? 154 ASN   A OD1 1 
ATOM   1005 N ND2 . ASN   A 1 154 ? -5.402  -26.472 -2.096  1.00 37.24  ? 154 ASN   A ND2 1 
ATOM   1006 N N   . ASN   A 1 155 ? -10.265 -26.274 -4.937  1.00 36.68  ? 155 ASN   A N   1 
ATOM   1007 C CA  . ASN   A 1 155 ? -11.474 -25.540 -5.283  1.00 36.07  ? 155 ASN   A CA  1 
ATOM   1008 C C   . ASN   A 1 155 ? -11.713 -24.420 -4.273  1.00 37.45  ? 155 ASN   A C   1 
ATOM   1009 O O   . ASN   A 1 155 ? -11.648 -24.662 -3.062  1.00 38.38  ? 155 ASN   A O   1 
ATOM   1010 C CB  . ASN   A 1 155 ? -12.669 -26.491 -5.302  1.00 36.49  ? 155 ASN   A CB  1 
ATOM   1011 C CG  . ASN   A 1 155 ? -13.831 -25.954 -6.102  1.00 37.72  ? 155 ASN   A CG  1 
ATOM   1012 O OD1 . ASN   A 1 155 ? -14.497 -25.001 -5.695  1.00 36.22  ? 155 ASN   A OD1 1 
ATOM   1013 N ND2 . ASN   A 1 155 ? -14.099 -26.579 -7.239  1.00 37.76  ? 155 ASN   A ND2 1 
ATOM   1014 N N   . PRO   A 1 156 ? -11.975 -23.189 -4.721  1.00 36.64  ? 156 PRO   A N   1 
ATOM   1015 C CA  . PRO   A 1 156 ? -12.246 -22.103 -3.763  1.00 34.77  ? 156 PRO   A CA  1 
ATOM   1016 C C   . PRO   A 1 156 ? -13.578 -22.231 -3.039  1.00 35.30  ? 156 PRO   A C   1 
ATOM   1017 O O   . PRO   A 1 156 ? -13.706 -21.700 -1.929  1.00 37.11  ? 156 PRO   A O   1 
ATOM   1018 C CB  . PRO   A 1 156 ? -12.209 -20.844 -4.643  1.00 35.52  ? 156 PRO   A CB  1 
ATOM   1019 C CG  . PRO   A 1 156 ? -11.389 -21.249 -5.836  1.00 34.18  ? 156 PRO   A CG  1 
ATOM   1020 C CD  . PRO   A 1 156 ? -11.797 -22.672 -6.087  1.00 33.82  ? 156 PRO   A CD  1 
ATOM   1021 N N   . HIS   A 1 157 ? -14.576 -22.898 -3.626  1.00 38.18  ? 157 HIS   A N   1 
ATOM   1022 C CA  . HIS   A 1 157 ? -15.834 -23.139 -2.925  1.00 36.47  ? 157 HIS   A CA  1 
ATOM   1023 C C   . HIS   A 1 157 ? -15.727 -24.252 -1.896  1.00 36.08  ? 157 HIS   A C   1 
ATOM   1024 O O   . HIS   A 1 157 ? -16.594 -24.352 -1.022  1.00 35.59  ? 157 HIS   A O   1 
ATOM   1025 C CB  . HIS   A 1 157 ? -16.950 -23.482 -3.912  1.00 36.71  ? 157 HIS   A CB  1 
ATOM   1026 C CG  . HIS   A 1 157 ? -17.067 -22.520 -5.050  1.00 35.88  ? 157 HIS   A CG  1 
ATOM   1027 N ND1 . HIS   A 1 157 ? -17.913 -21.433 -5.020  1.00 37.52  ? 157 HIS   A ND1 1 
ATOM   1028 C CD2 . HIS   A 1 157 ? -16.460 -22.494 -6.260  1.00 37.68  ? 157 HIS   A CD2 1 
ATOM   1029 C CE1 . HIS   A 1 157 ? -17.809 -20.767 -6.156  1.00 39.21  ? 157 HIS   A CE1 1 
ATOM   1030 N NE2 . HIS   A 1 157 ? -16.934 -21.391 -6.926  1.00 40.02  ? 157 HIS   A NE2 1 
ATOM   1031 N N   . ASP   A 1 158 ? -14.696 -25.089 -1.993  1.00 37.76  ? 158 ASP   A N   1 
ATOM   1032 C CA  . ASP   A 1 158 ? -14.446 -26.170 -1.048  1.00 36.39  ? 158 ASP   A CA  1 
ATOM   1033 C C   . ASP   A 1 158 ? -13.015 -26.658 -1.220  1.00 38.55  ? 158 ASP   A C   1 
ATOM   1034 O O   . ASP   A 1 158 ? -12.697 -27.307 -2.221  1.00 37.32  ? 158 ASP   A O   1 
ATOM   1035 C CB  . ASP   A 1 158 ? -15.441 -27.315 -1.258  1.00 38.45  ? 158 ASP   A CB  1 
ATOM   1036 C CG  . ASP   A 1 158 ? -15.457 -28.302 -0.103  1.00 40.81  ? 158 ASP   A CG  1 
ATOM   1037 O OD1 . ASP   A 1 158 ? -14.411 -28.471 0.562   1.00 38.55  ? 158 ASP   A OD1 1 
ATOM   1038 O OD2 . ASP   A 1 158 ? -16.519 -28.918 0.135   1.00 40.99  ? 158 ASP   A OD2 1 
ATOM   1039 N N   . HIS   A 1 159 ? -12.145 -26.353 -0.254  1.00 37.06  ? 159 HIS   A N   1 
ATOM   1040 C CA  . HIS   A 1 159 ? -10.726 -26.658 -0.406  1.00 38.38  ? 159 HIS   A CA  1 
ATOM   1041 C C   . HIS   A 1 159 ? -10.452 -28.156 -0.487  1.00 38.24  ? 159 HIS   A C   1 
ATOM   1042 O O   . HIS   A 1 159 ? -9.388  -28.552 -0.973  1.00 39.47  ? 159 HIS   A O   1 
ATOM   1043 C CB  . HIS   A 1 159 ? -9.938  -26.034 0.748   1.00 36.66  ? 159 HIS   A CB  1 
ATOM   1044 C CG  . HIS   A 1 159 ? -9.966  -24.537 0.750   1.00 40.98  ? 159 HIS   A CG  1 
ATOM   1045 N ND1 . HIS   A 1 159 ? -10.208 -23.797 -0.387  1.00 40.71  ? 159 HIS   A ND1 1 
ATOM   1046 C CD2 . HIS   A 1 159 ? -9.812  -23.641 1.755   1.00 38.86  ? 159 HIS   A CD2 1 
ATOM   1047 C CE1 . HIS   A 1 159 ? -10.189 -22.510 -0.087  1.00 36.72  ? 159 HIS   A CE1 1 
ATOM   1048 N NE2 . HIS   A 1 159 ? -9.950  -22.389 1.207   1.00 38.92  ? 159 HIS   A NE2 1 
ATOM   1049 N N   . SER   A 1 160 ? -11.389 -28.992 -0.039  1.00 33.50  ? 160 SER   A N   1 
ATOM   1050 C CA  . SER   A 1 160 ? -11.234 -30.440 -0.104  1.00 38.96  ? 160 SER   A CA  1 
ATOM   1051 C C   . SER   A 1 160 ? -11.624 -31.024 -1.455  1.00 40.34  ? 160 SER   A C   1 
ATOM   1052 O O   . SER   A 1 160 ? -11.315 -32.191 -1.717  1.00 40.02  ? 160 SER   A O   1 
ATOM   1053 C CB  . SER   A 1 160 ? -12.069 -31.102 0.993   1.00 36.92  ? 160 SER   A CB  1 
ATOM   1054 O OG  . SER   A 1 160 ? -13.444 -31.097 0.650   1.00 36.96  ? 160 SER   A OG  1 
ATOM   1055 N N   . ARG   A 1 161 ? -12.290 -30.253 -2.307  1.00 36.29  ? 161 ARG   A N   1 
ATOM   1056 C CA  . ARG   A 1 161 ? -12.708 -30.707 -3.625  1.00 39.57  ? 161 ARG   A CA  1 
ATOM   1057 C C   . ARG   A 1 161 ? -11.720 -30.242 -4.691  1.00 41.97  ? 161 ARG   A C   1 
ATOM   1058 O O   . ARG   A 1 161 ? -11.106 -29.178 -4.573  1.00 38.50  ? 161 ARG   A O   1 
ATOM   1059 C CB  . ARG   A 1 161 ? -14.108 -30.189 -3.959  1.00 39.98  ? 161 ARG   A CB  1 
ATOM   1060 C CG  . ARG   A 1 161 ? -15.166 -30.527 -2.920  1.00 40.51  ? 161 ARG   A CG  1 
ATOM   1061 C CD  . ARG   A 1 161 ? -15.128 -31.989 -2.540  1.00 38.80  ? 161 ARG   A CD  1 
ATOM   1062 N NE  . ARG   A 1 161 ? -16.183 -32.738 -3.209  1.00 43.01  ? 161 ARG   A NE  1 
ATOM   1063 C CZ  . ARG   A 1 161 ? -16.631 -33.918 -2.804  1.00 41.94  ? 161 ARG   A CZ  1 
ATOM   1064 N NH1 . ARG   A 1 161 ? -16.131 -34.515 -1.735  1.00 46.69  ? 161 ARG   A NH1 1 
ATOM   1065 N NH2 . ARG   A 1 161 ? -17.603 -34.512 -3.490  1.00 44.42  ? 161 ARG   A NH2 1 
ATOM   1066 N N   . SER   A 1 162 ? -11.580 -31.049 -5.741  1.00 39.70  ? 162 SER   A N   1 
ATOM   1067 C CA  . SER   A 1 162 ? -10.699 -30.692 -6.844  1.00 37.22  ? 162 SER   A CA  1 
ATOM   1068 C C   . SER   A 1 162 ? -11.237 -29.472 -7.590  1.00 40.09  ? 162 SER   A C   1 
ATOM   1069 O O   . SER   A 1 162 ? -12.445 -29.231 -7.647  1.00 37.42  ? 162 SER   A O   1 
ATOM   1070 C CB  . SER   A 1 162 ? -10.542 -31.867 -7.810  1.00 40.30  ? 162 SER   A CB  1 
ATOM   1071 O OG  . SER   A 1 162 ? -10.884 -31.502 -9.137  1.00 40.30  ? 162 SER   A OG  1 
ATOM   1072 N N   . ALA   A 1 163 ? -10.328 -28.706 -8.205  1.00 34.86  ? 163 ALA   A N   1 
ATOM   1073 C CA  . ALA   A 1 163 ? -10.724 -27.445 -8.882  1.00 34.78  ? 163 ALA   A CA  1 
ATOM   1074 C C   . ALA   A 1 163 ? -10.870 -27.612 -10.397 1.00 36.83  ? 163 ALA   A C   1 
ATOM   1075 O O   . ALA   A 1 163 ? -10.856 -26.586 -11.100 1.00 37.98  ? 163 ALA   A O   1 
ATOM   1076 C CB  . ALA   A 1 163 ? -9.697  -26.383 -8.576  1.00 34.40  ? 163 ALA   A CB  1 
ATOM   1077 N N   . GLY   A 1 164 ? -11.089 -28.831 -10.881 1.00 35.85  ? 164 GLY   A N   1 
ATOM   1078 C CA  . GLY   A 1 164 ? -11.171 -29.084 -12.333 1.00 37.01  ? 164 GLY   A CA  1 
ATOM   1079 C C   . GLY   A 1 164 ? -9.838  -29.440 -12.949 1.00 41.43  ? 164 GLY   A C   1 
ATOM   1080 O O   . GLY   A 1 164 ? -8.816  -29.248 -12.266 1.00 37.26  ? 164 GLY   A O   1 
ATOM   1081 N N   . GLY   A 1 165 ? -9.826  -29.804 -14.235 1.00 39.71  ? 165 GLY   A N   1 
ATOM   1082 C CA  . GLY   A 1 165 ? -8.600  -30.359 -14.836 1.00 43.14  ? 165 GLY   A CA  1 
ATOM   1083 C C   . GLY   A 1 165 ? -7.951  -29.571 -15.946 1.00 45.81  ? 165 GLY   A C   1 
ATOM   1084 O O   . GLY   A 1 165 ? -8.678  -29.163 -16.869 1.00 44.34  ? 165 GLY   A O   1 
ATOM   1085 N N   . SER   A 1 166 ? -6.631  -29.385 -15.856 1.00 48.11  ? 166 SER   A N   1 
ATOM   1086 C CA  . SER   A 1 166 ? -5.824  -28.649 -16.867 1.00 42.27  ? 166 SER   A CA  1 
ATOM   1087 C C   . SER   A 1 166 ? -6.090  -27.140 -16.765 1.00 39.60  ? 166 SER   A C   1 
ATOM   1088 O O   . SER   A 1 166 ? -5.173  -26.397 -16.431 1.00 42.83  ? 166 SER   A O   1 
ATOM   1089 C CB  . SER   A 1 166 ? -5.998  -29.202 -18.264 1.00 45.22  ? 166 SER   A CB  1 
ATOM   1090 O OG  . SER   A 1 166 ? -5.966  -30.622 -18.271 1.00 46.46  ? 166 SER   A OG  1 
ATOM   1091 N N   . SER   A 1 167 ? -7.335  -26.722 -16.908 1.00 39.66  ? 167 SER   A N   1 
ATOM   1092 C CA  . SER   A 1 167 ? -7.658  -25.280 -16.794 1.00 38.14  ? 167 SER   A CA  1 
ATOM   1093 C C   . SER   A 1 167 ? -8.143  -24.999 -15.365 1.00 37.98  ? 167 SER   A C   1 
ATOM   1094 O O   . SER   A 1 167 ? -8.723  -23.928 -15.139 1.00 37.67  ? 167 SER   A O   1 
ATOM   1095 C CB  . SER   A 1 167 ? -8.597  -24.828 -17.861 1.00 36.84  ? 167 SER   A CB  1 
ATOM   1096 O OG  . SER   A 1 167 ? -8.226  -25.366 -19.122 1.00 36.65  ? 167 SER   A OG  1 
ATOM   1097 N N   . GLY   A 1 168 ? -7.981  -25.970 -14.465 1.00 38.45  ? 168 GLY   A N   1 
ATOM   1098 C CA  . GLY   A 1 168 ? -8.452  -25.825 -13.074 1.00 39.16  ? 168 GLY   A CA  1 
ATOM   1099 C C   . GLY   A 1 168 ? -7.767  -24.685 -12.349 1.00 37.12  ? 168 GLY   A C   1 
ATOM   1100 O O   . GLY   A 1 168 ? -8.461  -23.972 -11.601 1.00 36.93  ? 168 GLY   A O   1 
ATOM   1101 N N   . GLY   A 1 169 ? -6.465  -24.496 -12.563 1.00 37.87  ? 169 GLY   A N   1 
ATOM   1102 C CA  . GLY   A 1 169 ? -5.795  -23.336 -11.952 1.00 32.93  ? 169 GLY   A CA  1 
ATOM   1103 C C   . GLY   A 1 169 ? -6.422  -22.066 -12.486 1.00 35.18  ? 169 GLY   A C   1 
ATOM   1104 O O   . GLY   A 1 169 ? -6.632  -21.133 -11.691 1.00 32.72  ? 169 GLY   A O   1 
ATOM   1105 N N   . ALA   A 1 170 ? -6.732  -22.041 -13.782 1.00 35.43  ? 170 ALA   A N   1 
ATOM   1106 C CA  . ALA   A 1 170 ? -7.387  -20.871 -14.407 1.00 35.03  ? 170 ALA   A CA  1 
ATOM   1107 C C   . ALA   A 1 170 ? -8.745  -20.609 -13.758 1.00 33.43  ? 170 ALA   A C   1 
ATOM   1108 O O   . ALA   A 1 170 ? -9.018  -19.456 -13.379 1.00 32.86  ? 170 ALA   A O   1 
ATOM   1109 C CB  . ALA   A 1 170 ? -7.547  -21.136 -15.881 1.00 33.51  ? 170 ALA   A CB  1 
ATOM   1110 N N   . ALA   A 1 171 ? -9.571  -21.648 -13.639 1.00 33.81  ? 171 ALA   A N   1 
ATOM   1111 C CA  . ALA   A 1 171 ? -10.917 -21.456 -13.114 1.00 32.16  ? 171 ALA   A CA  1 
ATOM   1112 C C   . ALA   A 1 171 ? -10.892 -21.064 -11.641 1.00 30.18  ? 171 ALA   A C   1 
ATOM   1113 O O   . ALA   A 1 171 ? -11.696 -20.235 -11.202 1.00 33.70  ? 171 ALA   A O   1 
ATOM   1114 C CB  . ALA   A 1 171 ? -11.742 -22.724 -13.327 1.00 33.05  ? 171 ALA   A CB  1 
ATOM   1115 N N   . ALA   A 1 172 ? -9.975  -21.642 -10.863 1.00 28.11  ? 172 ALA   A N   1 
ATOM   1116 C CA  . ALA   A 1 172 ? -9.864  -21.264 -9.457  1.00 31.35  ? 172 ALA   A CA  1 
ATOM   1117 C C   . ALA   A 1 172 ? -9.351  -19.837 -9.295  1.00 32.29  ? 172 ALA   A C   1 
ATOM   1118 O O   . ALA   A 1 172 ? -9.718  -19.157 -8.333  1.00 35.31  ? 172 ALA   A O   1 
ATOM   1119 C CB  . ALA   A 1 172 ? -8.960  -22.245 -8.713  1.00 30.88  ? 172 ALA   A CB  1 
ATOM   1120 N N   . ALA   A 1 173 ? -8.514  -19.362 -10.223 1.00 31.68  ? 173 ALA   A N   1 
ATOM   1121 C CA  . ALA   A 1 173 ? -8.080  -17.969 -10.176 1.00 34.76  ? 173 ALA   A CA  1 
ATOM   1122 C C   . ALA   A 1 173 ? -9.241  -17.025 -10.462 1.00 37.11  ? 173 ALA   A C   1 
ATOM   1123 O O   . ALA   A 1 173 ? -9.382  -15.985 -9.807  1.00 37.91  ? 173 ALA   A O   1 
ATOM   1124 C CB  . ALA   A 1 173 ? -6.944  -17.733 -11.171 1.00 29.26  ? 173 ALA   A CB  1 
ATOM   1125 N N   . LEU   A 1 174 ? -10.080 -17.370 -11.444 1.00 34.26  ? 174 LEU   A N   1 
ATOM   1126 C CA  . LEU   A 1 174 ? -11.256 -16.557 -11.734 1.00 35.93  ? 174 LEU   A CA  1 
ATOM   1127 C C   . LEU   A 1 174 ? -12.276 -16.643 -10.607 1.00 36.52  ? 174 LEU   A C   1 
ATOM   1128 O O   . LEU   A 1 174 ? -12.859 -15.626 -10.215 1.00 40.18  ? 174 LEU   A O   1 
ATOM   1129 C CB  . LEU   A 1 174 ? -11.888 -16.992 -13.057 1.00 34.77  ? 174 LEU   A CB  1 
ATOM   1130 C CG  . LEU   A 1 174 ? -11.065 -16.830 -14.335 1.00 36.39  ? 174 LEU   A CG  1 
ATOM   1131 C CD1 . LEU   A 1 174 ? -11.491 -17.867 -15.352 1.00 36.90  ? 174 LEU   A CD1 1 
ATOM   1132 C CD2 . LEU   A 1 174 ? -11.224 -15.426 -14.898 1.00 38.18  ? 174 LEU   A CD2 1 
ATOM   1133 N N   . ALA   A 1 175 ? -12.514 -17.851 -10.082 1.00 35.74  ? 175 ALA   A N   1 
ATOM   1134 C CA  . ALA   A 1 175 ? -13.503 -18.012 -9.020  1.00 32.83  ? 175 ALA   A CA  1 
ATOM   1135 C C   . ALA   A 1 175 ? -13.073 -17.289 -7.751  1.00 36.85  ? 175 ALA   A C   1 
ATOM   1136 O O   . ALA   A 1 175 ? -13.895 -16.649 -7.085  1.00 40.70  ? 175 ALA   A O   1 
ATOM   1137 C CB  . ALA   A 1 175 ? -13.742 -19.495 -8.738  1.00 35.15  ? 175 ALA   A CB  1 
ATOM   1138 N N   . ALA   A 1 176 ? -11.788 -17.377 -7.400  1.00 37.35  ? 176 ALA   A N   1 
ATOM   1139 C CA  . ALA   A 1 176 ? -11.271 -16.644 -6.250  1.00 35.34  ? 176 ALA   A CA  1 
ATOM   1140 C C   . ALA   A 1 176 ? -11.179 -15.145 -6.503  1.00 37.38  ? 176 ALA   A C   1 
ATOM   1141 O O   . ALA   A 1 176 ? -10.850 -14.401 -5.575  1.00 35.24  ? 176 ALA   A O   1 
ATOM   1142 C CB  . ALA   A 1 176 ? -9.897  -17.184 -5.854  1.00 36.55  ? 176 ALA   A CB  1 
ATOM   1143 N N   . GLY   A 1 177 ? -11.446 -14.691 -7.727  1.00 36.49  ? 177 GLY   A N   1 
ATOM   1144 C CA  . GLY   A 1 177 ? -11.468 -13.278 -8.041  1.00 36.66  ? 177 GLY   A CA  1 
ATOM   1145 C C   . GLY   A 1 177 ? -10.118 -12.625 -8.234  1.00 40.82  ? 177 GLY   A C   1 
ATOM   1146 O O   . GLY   A 1 177 ? -10.048 -11.390 -8.236  1.00 41.28  ? 177 GLY   A O   1 
ATOM   1147 N N   . MET   A 1 178 ? -9.044  -13.402 -8.413  1.00 39.24  ? 178 MET   A N   1 
ATOM   1148 C CA  . MET   A 1 178 ? -7.719  -12.796 -8.517  1.00 41.12  ? 178 MET   A CA  1 
ATOM   1149 C C   . MET   A 1 178 ? -7.522  -12.097 -9.857  1.00 41.74  ? 178 MET   A C   1 
ATOM   1150 O O   . MET   A 1 178 ? -7.010  -10.973 -9.903  1.00 42.03  ? 178 MET   A O   1 
ATOM   1151 C CB  . MET   A 1 178 ? -6.623  -13.839 -8.289  1.00 39.74  ? 178 MET   A CB  1 
ATOM   1152 C CG  . MET   A 1 178 ? -7.032  -15.035 -7.433  1.00 43.53  ? 178 MET   A CG  1 
ATOM   1153 S SD  . MET   A 1 178 ? -5.680  -16.220 -7.240  1.00 41.65  ? 178 MET   A SD  1 
ATOM   1154 C CE  . MET   A 1 178 ? -6.243  -17.195 -5.858  1.00 38.03  ? 178 MET   A CE  1 
ATOM   1155 N N   . VAL   A 1 179 ? -7.906  -12.736 -10.957 1.00 40.92  ? 179 VAL   A N   1 
ATOM   1156 C CA  . VAL   A 1 179 ? -7.745  -12.117 -12.271 1.00 40.12  ? 179 VAL   A CA  1 
ATOM   1157 C C   . VAL   A 1 179 ? -9.058  -12.194 -13.041 1.00 42.77  ? 179 VAL   A C   1 
ATOM   1158 O O   . VAL   A 1 179 ? -9.846  -13.130 -12.837 1.00 38.67  ? 179 VAL   A O   1 
ATOM   1159 C CB  . VAL   A 1 179 ? -6.598  -12.765 -13.063 1.00 39.59  ? 179 VAL   A CB  1 
ATOM   1160 C CG1 . VAL   A 1 179 ? -5.279  -12.592 -12.327 1.00 42.75  ? 179 VAL   A CG1 1 
ATOM   1161 C CG2 . VAL   A 1 179 ? -6.890  -14.233 -13.307 1.00 36.59  ? 179 VAL   A CG2 1 
ATOM   1162 N N   . PRO   A 1 180 ? -9.334  -11.230 -13.925 1.00 43.20  ? 180 PRO   A N   1 
ATOM   1163 C CA  . PRO   A 1 180 ? -10.630 -11.199 -14.618 1.00 42.50  ? 180 PRO   A CA  1 
ATOM   1164 C C   . PRO   A 1 180 ? -10.715 -12.081 -15.852 1.00 38.59  ? 180 PRO   A C   1 
ATOM   1165 O O   . PRO   A 1 180 ? -11.819 -12.237 -16.390 1.00 41.76  ? 180 PRO   A O   1 
ATOM   1166 C CB  . PRO   A 1 180 ? -10.772 -9.723  -15.016 1.00 44.49  ? 180 PRO   A CB  1 
ATOM   1167 C CG  . PRO   A 1 180 ? -9.365  -9.250  -15.148 1.00 40.23  ? 180 PRO   A CG  1 
ATOM   1168 C CD  . PRO   A 1 180 ? -8.602  -9.962  -14.069 1.00 41.39  ? 180 PRO   A CD  1 
ATOM   1169 N N   . LEU   A 1 181 ? -9.611  -12.647 -16.333 1.00 39.54  ? 181 LEU   A N   1 
ATOM   1170 C CA  . LEU   A 1 181 ? -9.650  -13.343 -17.612 1.00 39.77  ? 181 LEU   A CA  1 
ATOM   1171 C C   . LEU   A 1 181 ? -8.573  -14.418 -17.649 1.00 38.50  ? 181 LEU   A C   1 
ATOM   1172 O O   . LEU   A 1 181 ? -7.496  -14.259 -17.069 1.00 41.01  ? 181 LEU   A O   1 
ATOM   1173 C CB  . LEU   A 1 181 ? -9.478  -12.362 -18.782 1.00 39.41  ? 181 LEU   A CB  1 
ATOM   1174 C CG  . LEU   A 1 181 ? -9.624  -12.891 -20.215 1.00 38.26  ? 181 LEU   A CG  1 
ATOM   1175 C CD1 . LEU   A 1 181 ? -11.035 -13.385 -20.482 1.00 41.36  ? 181 LEU   A CD1 1 
ATOM   1176 C CD2 . LEU   A 1 181 ? -9.231  -11.825 -21.234 1.00 37.36  ? 181 LEU   A CD2 1 
ATOM   1177 N N   . GLU   A 1 182 ? -8.875  -15.508 -18.353 1.00 38.46  ? 182 GLU   A N   1 
ATOM   1178 C CA  . GLU   A 1 182 ? -7.973  -16.646 -18.443 1.00 38.93  ? 182 GLU   A CA  1 
ATOM   1179 C C   . GLU   A 1 182 ? -8.187  -17.347 -19.779 1.00 39.84  ? 182 GLU   A C   1 
ATOM   1180 O O   . GLU   A 1 182 ? -9.157  -17.084 -20.494 1.00 41.45  ? 182 GLU   A O   1 
ATOM   1181 C CB  . GLU   A 1 182 ? -8.187  -17.612 -17.272 1.00 38.84  ? 182 GLU   A CB  1 
ATOM   1182 C CG  . GLU   A 1 182 ? -7.084  -17.573 -16.228 1.00 39.16  ? 182 GLU   A CG  1 
ATOM   1183 C CD  . GLU   A 1 182 ? -5.869  -18.393 -16.620 1.00 42.66  ? 182 GLU   A CD  1 
ATOM   1184 O OE1 . GLU   A 1 182 ? -5.746  -18.766 -17.808 1.00 44.36  ? 182 GLU   A OE1 1 
ATOM   1185 O OE2 . GLU   A 1 182 ? -5.033  -18.663 -15.734 1.00 43.42  ? 182 GLU   A OE2 1 
ATOM   1186 N N   . TYR   A 1 183 ? -7.271  -18.254 -20.109 1.00 39.95  ? 183 TYR   A N   1 
ATOM   1187 C CA  . TYR   A 1 183 ? -7.332  -18.978 -21.373 1.00 39.95  ? 183 TYR   A CA  1 
ATOM   1188 C C   . TYR   A 1 183 ? -6.848  -20.404 -21.156 1.00 38.24  ? 183 TYR   A C   1 
ATOM   1189 O O   . TYR   A 1 183 ? -5.783  -20.616 -20.571 1.00 37.83  ? 183 TYR   A O   1 
ATOM   1190 C CB  . TYR   A 1 183 ? -6.489  -18.282 -22.452 1.00 36.29  ? 183 TYR   A CB  1 
ATOM   1191 C CG  . TYR   A 1 183 ? -7.166  -18.189 -23.805 1.00 38.40  ? 183 TYR   A CG  1 
ATOM   1192 C CD1 . TYR   A 1 183 ? -7.063  -19.226 -24.726 1.00 39.23  ? 183 TYR   A CD1 1 
ATOM   1193 C CD2 . TYR   A 1 183 ? -7.902  -17.063 -24.165 1.00 36.75  ? 183 TYR   A CD2 1 
ATOM   1194 C CE1 . TYR   A 1 183 ? -7.675  -19.151 -25.963 1.00 36.04  ? 183 TYR   A CE1 1 
ATOM   1195 C CE2 . TYR   A 1 183 ? -8.520  -16.978 -25.404 1.00 38.51  ? 183 TYR   A CE2 1 
ATOM   1196 C CZ  . TYR   A 1 183 ? -8.403  -18.028 -26.298 1.00 41.02  ? 183 TYR   A CZ  1 
ATOM   1197 O OH  . TYR   A 1 183 ? -9.012  -17.958 -27.532 1.00 41.23  ? 183 TYR   A OH  1 
ATOM   1198 N N   . GLY   A 1 184 ? -7.632  -21.379 -21.623 1.00 38.31  ? 184 GLY   A N   1 
ATOM   1199 C CA  . GLY   A 1 184 ? -7.312  -22.779 -21.440 1.00 37.90  ? 184 GLY   A CA  1 
ATOM   1200 C C   . GLY   A 1 184 ? -7.337  -23.542 -22.753 1.00 39.75  ? 184 GLY   A C   1 
ATOM   1201 O O   . GLY   A 1 184 ? -7.539  -22.971 -23.827 1.00 38.55  ? 184 GLY   A O   1 
ATOM   1202 N N   . SER   A 1 185 ? -7.117  -24.851 -22.634 1.00 40.12  ? 185 SER   A N   1 
ATOM   1203 C CA  . SER   A 1 185 ? -7.176  -25.791 -23.746 1.00 38.84  ? 185 SER   A CA  1 
ATOM   1204 C C   . SER   A 1 185 ? -8.062  -26.965 -23.347 1.00 38.33  ? 185 SER   A C   1 
ATOM   1205 O O   . SER   A 1 185 ? -8.219  -27.255 -22.160 1.00 37.80  ? 185 SER   A O   1 
ATOM   1206 C CB  . SER   A 1 185 ? -5.777  -26.274 -24.129 1.00 39.80  ? 185 SER   A CB  1 
ATOM   1207 O OG  . SER   A 1 185 ? -5.206  -27.033 -23.078 1.00 42.52  ? 185 SER   A OG  1 
ATOM   1208 N N   . ASP   A 1 186 ? -8.642  -27.644 -24.342 1.00 35.83  ? 186 ASP   A N   1 
ATOM   1209 C CA  . ASP   A 1 186 ? -9.692  -28.634 -24.077 1.00 39.26  ? 186 ASP   A CA  1 
ATOM   1210 C C   . ASP   A 1 186 ? -9.591  -29.745 -25.121 1.00 42.13  ? 186 ASP   A C   1 
ATOM   1211 O O   . ASP   A 1 186 ? -10.035 -29.568 -26.260 1.00 41.70  ? 186 ASP   A O   1 
ATOM   1212 C CB  . ASP   A 1 186 ? -11.070 -27.973 -24.096 1.00 40.52  ? 186 ASP   A CB  1 
ATOM   1213 C CG  . ASP   A 1 186 ? -12.207 -28.922 -23.701 1.00 42.95  ? 186 ASP   A CG  1 
ATOM   1214 O OD1 . ASP   A 1 186 ? -12.276 -30.061 -24.214 1.00 42.15  ? 186 ASP   A OD1 1 
ATOM   1215 O OD2 . ASP   A 1 186 ? -13.058 -28.506 -22.882 1.00 36.88  ? 186 ASP   A OD2 1 
ATOM   1216 N N   . ILE   A 1 187 ? -9.021  -30.883 -24.724 1.00 41.27  ? 187 ILE   A N   1 
ATOM   1217 C CA  . ILE   A 1 187 ? -9.109  -32.096 -25.529 1.00 40.91  ? 187 ILE   A CA  1 
ATOM   1218 C C   . ILE   A 1 187 ? -10.092 -33.100 -24.933 1.00 41.50  ? 187 ILE   A C   1 
ATOM   1219 O O   . ILE   A 1 187 ? -10.604 -33.960 -25.666 1.00 41.46  ? 187 ILE   A O   1 
ATOM   1220 C CB  . ILE   A 1 187 ? -7.725  -32.756 -25.716 1.00 43.08  ? 187 ILE   A CB  1 
ATOM   1221 C CG1 . ILE   A 1 187 ? -7.654  -33.459 -27.071 1.00 43.18  ? 187 ILE   A CG1 1 
ATOM   1222 C CG2 . ILE   A 1 187 ? -7.439  -33.769 -24.617 1.00 40.82  ? 187 ILE   A CG2 1 
ATOM   1223 C CD1 . ILE   A 1 187 ? -6.348  -34.170 -27.308 1.00 40.37  ? 187 ILE   A CD1 1 
ATOM   1224 N N   . GLY   A 1 188 ? -10.380 -33.010 -23.637 1.00 42.12  ? 188 GLY   A N   1 
ATOM   1225 C CA  . GLY   A 1 188 ? -11.306 -33.920 -22.996 1.00 39.67  ? 188 GLY   A CA  1 
ATOM   1226 C C   . GLY   A 1 188 ? -12.133 -33.234 -21.931 1.00 41.38  ? 188 GLY   A C   1 
ATOM   1227 O O   . GLY   A 1 188 ? -12.435 -33.829 -20.893 1.00 43.89  ? 188 GLY   A O   1 
ATOM   1228 N N   . GLY   A 1 189 ? -12.501 -31.979 -22.180 1.00 41.01  ? 189 GLY   A N   1 
ATOM   1229 C CA  . GLY   A 1 189 ? -13.323 -31.217 -21.266 1.00 40.36  ? 189 GLY   A CA  1 
ATOM   1230 C C   . GLY   A 1 189 ? -12.592 -30.216 -20.398 1.00 40.95  ? 189 GLY   A C   1 
ATOM   1231 O O   . GLY   A 1 189 ? -13.173 -29.737 -19.419 1.00 39.69  ? 189 GLY   A O   1 
ATOM   1232 N N   . SER   A 1 190 ? -11.354 -29.862 -20.735 1.00 42.35  ? 190 SER   A N   1 
ATOM   1233 C CA  . SER   A 1 190 ? -10.516 -29.118 -19.805 1.00 39.27  ? 190 SER   A CA  1 
ATOM   1234 C C   . SER   A 1 190 ? -10.821 -27.637 -19.708 1.00 38.27  ? 190 SER   A C   1 
ATOM   1235 O O   . SER   A 1 190 ? -10.274 -26.989 -18.815 1.00 38.45  ? 190 SER   A O   1 
ATOM   1236 C CB  . SER   A 1 190 ? -9.051  -29.279 -20.148 1.00 40.87  ? 190 SER   A CB  1 
ATOM   1237 O OG  . SER   A 1 190 ? -8.556  -30.386 -19.450 1.00 48.04  ? 190 SER   A OG  1 
ATOM   1238 N N   . ILE   A 1 191 ? -11.644 -27.077 -20.585 1.00 38.74  ? 191 ILE   A N   1 
ATOM   1239 C CA  . ILE   A 1 191 ? -12.150 -25.734 -20.330 1.00 38.64  ? 191 ILE   A CA  1 
ATOM   1240 C C   . ILE   A 1 191 ? -13.483 -25.794 -19.594 1.00 37.42  ? 191 ILE   A C   1 
ATOM   1241 O O   . ILE   A 1 191 ? -13.697 -25.072 -18.617 1.00 37.26  ? 191 ILE   A O   1 
ATOM   1242 C CB  . ILE   A 1 191 ? -12.260 -24.941 -21.649 1.00 38.88  ? 191 ILE   A CB  1 
ATOM   1243 C CG1 . ILE   A 1 191 ? -10.879 -24.730 -22.273 1.00 36.79  ? 191 ILE   A CG1 1 
ATOM   1244 C CG2 . ILE   A 1 191 ? -12.938 -23.606 -21.411 1.00 35.77  ? 191 ILE   A CG2 1 
ATOM   1245 C CD1 . ILE   A 1 191 ? -10.915 -24.396 -23.749 1.00 35.45  ? 191 ILE   A CD1 1 
ATOM   1246 N N   . ARG   A 1 192 ? -14.367 -26.696 -20.024 1.00 37.25  ? 192 ARG   A N   1 
ATOM   1247 C CA  . ARG   A 1 192 ? -15.718 -26.759 -19.480 1.00 38.65  ? 192 ARG   A CA  1 
ATOM   1248 C C   . ARG   A 1 192 ? -15.749 -27.386 -18.088 1.00 36.26  ? 192 ARG   A C   1 
ATOM   1249 O O   . ARG   A 1 192 ? -16.467 -26.897 -17.210 1.00 34.68  ? 192 ARG   A O   1 
ATOM   1250 C CB  . ARG   A 1 192 ? -16.622 -27.534 -20.439 1.00 36.69  ? 192 ARG   A CB  1 
ATOM   1251 C CG  . ARG   A 1 192 ? -16.614 -26.981 -21.858 1.00 38.27  ? 192 ARG   A CG  1 
ATOM   1252 C CD  . ARG   A 1 192 ? -17.177 -27.997 -22.842 1.00 41.88  ? 192 ARG   A CD  1 
ATOM   1253 N NE  . ARG   A 1 192 ? -16.170 -28.956 -23.284 1.00 43.08  ? 192 ARG   A NE  1 
ATOM   1254 C CZ  . ARG   A 1 192 ? -16.421 -30.002 -24.059 1.00 41.22  ? 192 ARG   A CZ  1 
ATOM   1255 N NH1 . ARG   A 1 192 ? -17.639 -30.249 -24.515 1.00 40.47  ? 192 ARG   A NH1 1 
ATOM   1256 N NH2 . ARG   A 1 192 ? -15.425 -30.818 -24.390 1.00 39.60  ? 192 ARG   A NH2 1 
ATOM   1257 N N   . VAL   A 1 193 ? -14.982 -28.461 -17.865 1.00 36.59  ? 193 VAL   A N   1 
ATOM   1258 C CA  . VAL   A 1 193 ? -15.015 -29.137 -16.563 1.00 36.76  ? 193 VAL   A CA  1 
ATOM   1259 C C   . VAL   A 1 193 ? -14.510 -28.242 -15.439 1.00 34.46  ? 193 VAL   A C   1 
ATOM   1260 O O   . VAL   A 1 193 ? -15.194 -28.144 -14.405 1.00 36.53  ? 193 VAL   A O   1 
ATOM   1261 C CB  . VAL   A 1 193 ? -14.261 -30.479 -16.642 1.00 39.02  ? 193 VAL   A CB  1 
ATOM   1262 C CG1 . VAL   A 1 193 ? -13.974 -31.021 -15.246 1.00 36.65  ? 193 VAL   A CG1 1 
ATOM   1263 C CG2 . VAL   A 1 193 ? -15.055 -31.490 -17.462 1.00 36.24  ? 193 VAL   A CG2 1 
ATOM   1264 N N   . PRO   A 1 194 ? -13.358 -27.567 -15.551 1.00 34.50  ? 194 PRO   A N   1 
ATOM   1265 C CA  . PRO   A 1 194 ? -12.959 -26.642 -14.476 1.00 36.86  ? 194 PRO   A CA  1 
ATOM   1266 C C   . PRO   A 1 194 ? -13.931 -25.493 -14.272 1.00 38.70  ? 194 PRO   A C   1 
ATOM   1267 O O   . PRO   A 1 194 ? -14.229 -25.144 -13.122 1.00 38.73  ? 194 PRO   A O   1 
ATOM   1268 C CB  . PRO   A 1 194 ? -11.582 -26.147 -14.940 1.00 35.34  ? 194 PRO   A CB  1 
ATOM   1269 C CG  . PRO   A 1 194 ? -11.073 -27.250 -15.785 1.00 39.21  ? 194 PRO   A CG  1 
ATOM   1270 C CD  . PRO   A 1 194 ? -12.283 -27.700 -16.550 1.00 38.24  ? 194 PRO   A CD  1 
ATOM   1271 N N   . ALA   A 1 195 ? -14.421 -24.884 -15.356 1.00 34.05  ? 195 ALA   A N   1 
ATOM   1272 C CA  . ALA   A 1 195 ? -15.438 -23.846 -15.228 1.00 36.60  ? 195 ALA   A CA  1 
ATOM   1273 C C   . ALA   A 1 195 ? -16.658 -24.371 -14.487 1.00 34.11  ? 195 ALA   A C   1 
ATOM   1274 O O   . ALA   A 1 195 ? -17.257 -23.664 -13.669 1.00 33.77  ? 195 ALA   A O   1 
ATOM   1275 C CB  . ALA   A 1 195 ? -15.833 -23.319 -16.610 1.00 33.94  ? 195 ALA   A CB  1 
ATOM   1276 N N   . HIS   A 1 196 ? -17.026 -25.625 -14.750 1.00 35.51  ? 196 HIS   A N   1 
ATOM   1277 C CA  . HIS   A 1 196 ? -18.144 -26.245 -14.050 1.00 35.18  ? 196 HIS   A CA  1 
ATOM   1278 C C   . HIS   A 1 196 ? -17.822 -26.444 -12.572 1.00 35.70  ? 196 HIS   A C   1 
ATOM   1279 O O   . HIS   A 1 196 ? -18.605 -26.055 -11.696 1.00 35.88  ? 196 HIS   A O   1 
ATOM   1280 C CB  . HIS   A 1 196 ? -18.488 -27.567 -14.740 1.00 35.47  ? 196 HIS   A CB  1 
ATOM   1281 C CG  . HIS   A 1 196 ? -19.258 -28.527 -13.889 1.00 36.24  ? 196 HIS   A CG  1 
ATOM   1282 N ND1 . HIS   A 1 196 ? -20.439 -28.191 -13.261 1.00 35.68  ? 196 HIS   A ND1 1 
ATOM   1283 C CD2 . HIS   A 1 196 ? -19.022 -29.823 -13.579 1.00 34.83  ? 196 HIS   A CD2 1 
ATOM   1284 C CE1 . HIS   A 1 196 ? -20.890 -29.237 -12.592 1.00 39.56  ? 196 HIS   A CE1 1 
ATOM   1285 N NE2 . HIS   A 1 196 ? -20.049 -30.240 -12.770 1.00 38.07  ? 196 HIS   A NE2 1 
ATOM   1286 N N   . PHE   A 1 197 ? -16.651 -27.017 -12.277 1.00 33.64  ? 197 PHE   A N   1 
ATOM   1287 C CA  . PHE   A 1 197 ? -16.278 -27.294 -10.893 1.00 35.14  ? 197 PHE   A CA  1 
ATOM   1288 C C   . PHE   A 1 197 ? -16.170 -26.018 -10.065 1.00 35.89  ? 197 PHE   A C   1 
ATOM   1289 O O   . PHE   A 1 197 ? -16.513 -26.013 -8.878  1.00 35.28  ? 197 PHE   A O   1 
ATOM   1290 C CB  . PHE   A 1 197 ? -14.955 -28.058 -10.850 1.00 36.30  ? 197 PHE   A CB  1 
ATOM   1291 C CG  . PHE   A 1 197 ? -15.097 -29.532 -11.065 1.00 32.81  ? 197 PHE   A CG  1 
ATOM   1292 C CD1 . PHE   A 1 197 ? -16.322 -30.083 -11.396 1.00 35.12  ? 197 PHE   A CD1 1 
ATOM   1293 C CD2 . PHE   A 1 197 ? -14.007 -30.371 -10.926 1.00 36.76  ? 197 PHE   A CD2 1 
ATOM   1294 C CE1 . PHE   A 1 197 ? -16.457 -31.442 -11.594 1.00 36.36  ? 197 PHE   A CE1 1 
ATOM   1295 C CE2 . PHE   A 1 197 ? -14.134 -31.730 -11.121 1.00 37.26  ? 197 PHE   A CE2 1 
ATOM   1296 C CZ  . PHE   A 1 197 ? -15.361 -32.268 -11.454 1.00 34.47  ? 197 PHE   A CZ  1 
ATOM   1297 N N   . CYS   A 1 198 ? -15.684 -24.930 -10.664 1.00 33.15  ? 198 CYS   A N   1 
ATOM   1298 C CA  . CYS   A 1 198 ? -15.448 -23.683 -9.945  1.00 34.74  ? 198 CYS   A CA  1 
ATOM   1299 C C   . CYS   A 1 198 ? -16.510 -22.620 -10.209 1.00 35.24  ? 198 CYS   A C   1 
ATOM   1300 O O   . CYS   A 1 198 ? -16.360 -21.487 -9.740  1.00 36.73  ? 198 CYS   A O   1 
ATOM   1301 C CB  . CYS   A 1 198 ? -14.062 -23.118 -10.287 1.00 32.79  ? 198 CYS   A CB  1 
ATOM   1302 S SG  . CYS   A 1 198 ? -12.643 -24.086 -9.710  1.00 39.97  ? 198 CYS   A SG  1 
ATOM   1303 N N   . GLY   A 1 199 ? -17.563 -22.949 -10.953 1.00 33.10  ? 199 GLY   A N   1 
ATOM   1304 C CA  . GLY   A 1 199 ? -18.633 -22.003 -11.216 1.00 33.40  ? 199 GLY   A CA  1 
ATOM   1305 C C   . GLY   A 1 199 ? -18.218 -20.724 -11.919 1.00 35.90  ? 199 GLY   A C   1 
ATOM   1306 O O   . GLY   A 1 199 ? -18.551 -19.624 -11.465 1.00 34.01  ? 199 GLY   A O   1 
ATOM   1307 N N   . VAL   A 1 200 ? -17.492 -20.852 -13.030 1.00 34.24  ? 200 VAL   A N   1 
ATOM   1308 C CA  . VAL   A 1 200 ? -17.104 -19.727 -13.865 1.00 32.35  ? 200 VAL   A CA  1 
ATOM   1309 C C   . VAL   A 1 200 ? -17.473 -20.048 -15.312 1.00 34.30  ? 200 VAL   A C   1 
ATOM   1310 O O   . VAL   A 1 200 ? -18.012 -21.111 -15.616 1.00 33.00  ? 200 VAL   A O   1 
ATOM   1311 C CB  . VAL   A 1 200 ? -15.603 -19.383 -13.730 1.00 34.11  ? 200 VAL   A CB  1 
ATOM   1312 C CG1 . VAL   A 1 200 ? -15.245 -19.104 -12.272 1.00 34.45  ? 200 VAL   A CG1 1 
ATOM   1313 C CG2 . VAL   A 1 200 ? -14.739 -20.496 -14.286 1.00 30.57  ? 200 VAL   A CG2 1 
ATOM   1314 N N   . TRP   A 1 201 ? -17.183 -19.109 -16.206 1.00 35.22  ? 201 TRP   A N   1 
ATOM   1315 C CA  . TRP   A 1 201 ? -17.532 -19.242 -17.613 1.00 36.99  ? 201 TRP   A CA  1 
ATOM   1316 C C   . TRP   A 1 201 ? -16.331 -19.750 -18.397 1.00 36.82  ? 201 TRP   A C   1 
ATOM   1317 O O   . TRP   A 1 201 ? -15.228 -19.207 -18.272 1.00 35.46  ? 201 TRP   A O   1 
ATOM   1318 C CB  . TRP   A 1 201 ? -18.003 -17.907 -18.192 1.00 36.67  ? 201 TRP   A CB  1 
ATOM   1319 C CG  . TRP   A 1 201 ? -19.261 -17.372 -17.583 1.00 36.92  ? 201 TRP   A CG  1 
ATOM   1320 C CD1 . TRP   A 1 201 ? -19.451 -16.982 -16.288 1.00 35.53  ? 201 TRP   A CD1 1 
ATOM   1321 C CD2 . TRP   A 1 201 ? -20.509 -17.160 -18.252 1.00 36.02  ? 201 TRP   A CD2 1 
ATOM   1322 N NE1 . TRP   A 1 201 ? -20.740 -16.541 -16.112 1.00 33.03  ? 201 TRP   A NE1 1 
ATOM   1323 C CE2 . TRP   A 1 201 ? -21.411 -16.641 -17.303 1.00 34.84  ? 201 TRP   A CE2 1 
ATOM   1324 C CE3 . TRP   A 1 201 ? -20.951 -17.361 -19.564 1.00 38.85  ? 201 TRP   A CE3 1 
ATOM   1325 C CZ2 . TRP   A 1 201 ? -22.730 -16.320 -17.624 1.00 34.86  ? 201 TRP   A CZ2 1 
ATOM   1326 C CZ3 . TRP   A 1 201 ? -22.261 -17.042 -19.881 1.00 35.87  ? 201 TRP   A CZ3 1 
ATOM   1327 C CH2 . TRP   A 1 201 ? -23.134 -16.528 -18.916 1.00 36.20  ? 201 TRP   A CH2 1 
ATOM   1328 N N   . GLY   A 1 202 ? -16.553 -20.782 -19.207 1.00 36.65  ? 202 GLY   A N   1 
ATOM   1329 C CA  . GLY   A 1 202 ? -15.520 -21.327 -20.065 1.00 34.95  ? 202 GLY   A CA  1 
ATOM   1330 C C   . GLY   A 1 202 ? -16.073 -21.714 -21.419 1.00 35.38  ? 202 GLY   A C   1 
ATOM   1331 O O   . GLY   A 1 202 ? -17.121 -22.360 -21.502 1.00 35.47  ? 202 GLY   A O   1 
ATOM   1332 N N   . LEU   A 1 203 ? -15.390 -21.319 -22.491 1.00 35.80  ? 203 LEU   A N   1 
ATOM   1333 C CA  . LEU   A 1 203 ? -15.871 -21.542 -23.850 1.00 36.71  ? 203 LEU   A CA  1 
ATOM   1334 C C   . LEU   A 1 203 ? -14.931 -22.500 -24.572 1.00 35.85  ? 203 LEU   A C   1 
ATOM   1335 O O   . LEU   A 1 203 ? -13.813 -22.123 -24.942 1.00 33.13  ? 203 LEU   A O   1 
ATOM   1336 C CB  . LEU   A 1 203 ? -15.987 -20.228 -24.619 1.00 34.14  ? 203 LEU   A CB  1 
ATOM   1337 C CG  . LEU   A 1 203 ? -16.247 -20.420 -26.118 1.00 34.52  ? 203 LEU   A CG  1 
ATOM   1338 C CD1 . LEU   A 1 203 ? -17.637 -20.993 -26.362 1.00 32.87  ? 203 LEU   A CD1 1 
ATOM   1339 C CD2 . LEU   A 1 203 ? -16.046 -19.122 -26.885 1.00 31.46  ? 203 LEU   A CD2 1 
ATOM   1340 N N   . LYS   A 1 204 ? -15.388 -23.733 -24.773 1.00 32.97  ? 204 LYS   A N   1 
ATOM   1341 C CA  . LYS   A 1 204 ? -14.720 -24.649 -25.685 1.00 33.91  ? 204 LYS   A CA  1 
ATOM   1342 C C   . LYS   A 1 204 ? -15.040 -24.194 -27.104 1.00 37.94  ? 204 LYS   A C   1 
ATOM   1343 O O   . LYS   A 1 204 ? -16.208 -24.189 -27.506 1.00 38.02  ? 204 LYS   A O   1 
ATOM   1344 C CB  . LYS   A 1 204 ? -15.177 -26.088 -25.429 1.00 35.47  ? 204 LYS   A CB  1 
ATOM   1345 C CG  . LYS   A 1 204 ? -14.566 -27.147 -26.357 1.00 40.71  ? 204 LYS   A CG  1 
ATOM   1346 C CD  . LYS   A 1 204 ? -15.371 -27.349 -27.641 1.00 36.17  ? 204 LYS   A CD  1 
ATOM   1347 C CE  . LYS   A 1 204 ? -14.705 -28.358 -28.558 1.00 36.26  ? 204 LYS   A CE  1 
ATOM   1348 N NZ  . LYS   A 1 204 ? -15.280 -28.331 -29.930 1.00 36.03  ? 204 LYS   A NZ  1 
ATOM   1349 N N   . THR   A 1 205 ? -14.021 -23.781 -27.851 1.00 38.03  ? 205 THR   A N   1 
ATOM   1350 C CA  . THR   A 1 205 ? -14.243 -23.172 -29.155 1.00 37.42  ? 205 THR   A CA  1 
ATOM   1351 C C   . THR   A 1 205 ? -14.370 -24.226 -30.251 1.00 38.30  ? 205 THR   A C   1 
ATOM   1352 O O   . THR   A 1 205 ? -14.012 -25.393 -30.074 1.00 39.63  ? 205 THR   A O   1 
ATOM   1353 C CB  . THR   A 1 205 ? -13.107 -22.207 -29.502 1.00 36.65  ? 205 THR   A CB  1 
ATOM   1354 O OG1 . THR   A 1 205 ? -11.850 -22.796 -29.152 1.00 40.33  ? 205 THR   A OG1 1 
ATOM   1355 C CG2 . THR   A 1 205 ? -13.275 -20.900 -28.742 1.00 35.98  ? 205 THR   A CG2 1 
ATOM   1356 N N   . THR   A 1 206 ? -14.893 -23.789 -31.398 1.00 37.47  ? 206 THR   A N   1 
ATOM   1357 C CA  . THR   A 1 206 ? -14.960 -24.646 -32.576 1.00 36.21  ? 206 THR   A CA  1 
ATOM   1358 C C   . THR   A 1 206 ? -13.564 -25.125 -32.946 1.00 39.06  ? 206 THR   A C   1 
ATOM   1359 O O   . THR   A 1 206 ? -12.602 -24.355 -32.917 1.00 39.46  ? 206 THR   A O   1 
ATOM   1360 C CB  . THR   A 1 206 ? -15.584 -23.890 -33.757 1.00 41.96  ? 206 THR   A CB  1 
ATOM   1361 O OG1 . THR   A 1 206 ? -16.953 -23.581 -33.468 1.00 40.77  ? 206 THR   A OG1 1 
ATOM   1362 C CG2 . THR   A 1 206 ? -15.523 -24.723 -35.041 1.00 39.68  ? 206 THR   A CG2 1 
ATOM   1363 N N   . PHE   A 1 207 ? -13.451 -26.412 -33.273 1.00 36.22  ? 207 PHE   A N   1 
ATOM   1364 C CA  . PHE   A 1 207 ? -12.168 -26.959 -33.691 1.00 41.11  ? 207 PHE   A CA  1 
ATOM   1365 C C   . PHE   A 1 207 ? -11.606 -26.154 -34.855 1.00 42.05  ? 207 PHE   A C   1 
ATOM   1366 O O   . PHE   A 1 207 ? -12.345 -25.733 -35.748 1.00 40.56  ? 207 PHE   A O   1 
ATOM   1367 C CB  . PHE   A 1 207 ? -12.314 -28.428 -34.088 1.00 40.74  ? 207 PHE   A CB  1 
ATOM   1368 C CG  . PHE   A 1 207 ? -11.016 -29.082 -34.459 1.00 45.38  ? 207 PHE   A CG  1 
ATOM   1369 C CD1 . PHE   A 1 207 ? -10.040 -29.310 -33.501 1.00 44.97  ? 207 PHE   A CD1 1 
ATOM   1370 C CD2 . PHE   A 1 207 ? -10.767 -29.465 -35.767 1.00 46.81  ? 207 PHE   A CD2 1 
ATOM   1371 C CE1 . PHE   A 1 207 ? -8.843  -29.907 -33.843 1.00 43.10  ? 207 PHE   A CE1 1 
ATOM   1372 C CE2 . PHE   A 1 207 ? -9.571  -30.066 -36.114 1.00 45.75  ? 207 PHE   A CE2 1 
ATOM   1373 C CZ  . PHE   A 1 207 ? -8.610  -30.287 -35.152 1.00 46.72  ? 207 PHE   A CZ  1 
ATOM   1374 N N   . ASP   A 1 208 ? -10.293 -25.917 -34.819 1.00 40.87  ? 208 ASP   A N   1 
ATOM   1375 C CA  . ASP   A 1 208 ? -9.534  -25.168 -35.820 1.00 46.21  ? 208 ASP   A CA  1 
ATOM   1376 C C   . ASP   A 1 208 ? -9.858  -23.676 -35.856 1.00 42.87  ? 208 ASP   A C   1 
ATOM   1377 O O   . ASP   A 1 208 ? -9.330  -22.964 -36.718 1.00 41.68  ? 208 ASP   A O   1 
ATOM   1378 C CB  . ASP   A 1 208 ? -9.715  -25.751 -37.229 1.00 46.88  ? 208 ASP   A CB  1 
ATOM   1379 C CG  . ASP   A 1 208 ? -8.598  -26.703 -37.620 1.00 54.37  ? 208 ASP   A CG  1 
ATOM   1380 O OD1 . ASP   A 1 208 ? -7.705  -26.966 -36.783 1.00 57.36  ? 208 ASP   A OD1 1 
ATOM   1381 O OD2 . ASP   A 1 208 ? -8.610  -27.183 -38.773 1.00 61.75  ? 208 ASP   A OD2 1 
ATOM   1382 N N   . ALA   A 1 209 ? -10.695 -23.171 -34.947 1.00 40.27  ? 209 ALA   A N   1 
ATOM   1383 C CA  . ALA   A 1 209 ? -11.038 -21.752 -34.964 1.00 39.52  ? 209 ALA   A CA  1 
ATOM   1384 C C   . ALA   A 1 209 ? -9.985  -20.874 -34.300 1.00 40.97  ? 209 ALA   A C   1 
ATOM   1385 O O   . ALA   A 1 209 ? -9.938  -19.672 -34.581 1.00 36.42  ? 209 ALA   A O   1 
ATOM   1386 C CB  . ALA   A 1 209 ? -12.387 -21.521 -34.285 1.00 36.72  ? 209 ALA   A CB  1 
ATOM   1387 N N   . VAL   A 1 210 ? -9.149  -21.438 -33.430 1.00 37.58  ? 210 VAL   A N   1 
ATOM   1388 C CA  . VAL   A 1 210 ? -8.097  -20.693 -32.747 1.00 38.66  ? 210 VAL   A CA  1 
ATOM   1389 C C   . VAL   A 1 210 ? -6.799  -21.481 -32.859 1.00 41.83  ? 210 VAL   A C   1 
ATOM   1390 O O   . VAL   A 1 210 ? -6.778  -22.691 -32.604 1.00 41.82  ? 210 VAL   A O   1 
ATOM   1391 C CB  . VAL   A 1 210 ? -8.437  -20.420 -31.267 1.00 37.39  ? 210 VAL   A CB  1 
ATOM   1392 C CG1 . VAL   A 1 210 ? -7.378  -19.524 -30.639 1.00 39.72  ? 210 VAL   A CG1 1 
ATOM   1393 C CG2 . VAL   A 1 210 ? -9.807  -19.769 -31.137 1.00 33.39  ? 210 VAL   A CG2 1 
ATOM   1394 N N   . SER   A 1 211 ? -5.719  -20.793 -33.226 1.00 40.09  ? 211 SER   A N   1 
ATOM   1395 C CA  . SER   A 1 211 ? -4.436  -21.454 -33.419 1.00 42.39  ? 211 SER   A CA  1 
ATOM   1396 C C   . SER   A 1 211 ? -3.875  -21.957 -32.095 1.00 41.62  ? 211 SER   A C   1 
ATOM   1397 O O   . SER   A 1 211 ? -4.000  -21.303 -31.056 1.00 38.41  ? 211 SER   A O   1 
ATOM   1398 C CB  . SER   A 1 211 ? -3.438  -20.501 -34.076 1.00 38.70  ? 211 SER   A CB  1 
ATOM   1399 O OG  . SER   A 1 211 ? -2.104  -20.906 -33.813 1.00 44.66  ? 211 SER   A OG  1 
ATOM   1400 N N   . LEU   A 1 212 ? -3.243  -23.128 -32.140 1.00 44.49  ? 212 LEU   A N   1 
ATOM   1401 C CA  . LEU   A 1 212 ? -2.594  -23.708 -30.974 1.00 43.75  ? 212 LEU   A CA  1 
ATOM   1402 C C   . LEU   A 1 212 ? -1.100  -23.424 -30.929 1.00 43.25  ? 212 LEU   A C   1 
ATOM   1403 O O   . LEU   A 1 212 ? -0.426  -23.896 -30.010 1.00 46.12  ? 212 LEU   A O   1 
ATOM   1404 C CB  . LEU   A 1 212 ? -2.832  -25.222 -30.930 1.00 43.38  ? 212 LEU   A CB  1 
ATOM   1405 C CG  . LEU   A 1 212 ? -4.252  -25.702 -31.240 1.00 44.23  ? 212 LEU   A CG  1 
ATOM   1406 C CD1 . LEU   A 1 212 ? -4.257  -27.166 -31.651 1.00 50.10  ? 212 LEU   A CD1 1 
ATOM   1407 C CD2 . LEU   A 1 212 ? -5.151  -25.485 -30.040 1.00 45.98  ? 212 LEU   A CD2 1 
ATOM   1408 N N   . GLU   A 1 213 ? -0.569  -22.664 -31.887 1.00 45.43  ? 213 GLU   A N   1 
ATOM   1409 C CA  . GLU   A 1 213 ? 0.863   -22.392 -31.918 1.00 45.13  ? 213 GLU   A CA  1 
ATOM   1410 C C   . GLU   A 1 213 ? 1.315   -21.751 -30.611 1.00 44.75  ? 213 GLU   A C   1 
ATOM   1411 O O   . GLU   A 1 213 ? 0.709   -20.790 -30.127 1.00 44.08  ? 213 GLU   A O   1 
ATOM   1412 C CB  . GLU   A 1 213 ? 1.212   -21.489 -33.099 1.00 41.37  ? 213 GLU   A CB  1 
ATOM   1413 C CG  . GLU   A 1 213 ? 2.496   -20.703 -32.892 1.00 45.09  ? 213 GLU   A CG  1 
ATOM   1414 C CD  . GLU   A 1 213 ? 2.777   -19.719 -34.006 1.00 45.50  ? 213 GLU   A CD  1 
ATOM   1415 O OE1 . GLU   A 1 213 ? 1.954   -19.617 -34.938 1.00 50.18  ? 213 GLU   A OE1 1 
ATOM   1416 O OE2 . GLU   A 1 213 ? 3.831   -19.052 -33.954 1.00 48.46  ? 213 GLU   A OE2 1 
ATOM   1417 N N   . GLY   A 1 214 ? 2.386   -22.294 -30.039 1.00 45.09  ? 214 GLY   A N   1 
ATOM   1418 C CA  . GLY   A 1 214 ? 2.837   -21.905 -28.729 1.00 42.44  ? 214 GLY   A CA  1 
ATOM   1419 C C   . GLY   A 1 214 ? 2.279   -22.739 -27.597 1.00 42.68  ? 214 GLY   A C   1 
ATOM   1420 O O   . GLY   A 1 214 ? 2.838   -22.713 -26.496 1.00 44.25  ? 214 GLY   A O   1 
ATOM   1421 N N   . HIS   A 1 215 ? 1.191   -23.475 -27.832 1.00 42.33  ? 215 HIS   A N   1 
ATOM   1422 C CA  . HIS   A 1 215 ? 0.731   -24.490 -26.889 1.00 43.44  ? 215 HIS   A CA  1 
ATOM   1423 C C   . HIS   A 1 215 ? 1.516   -25.771 -27.142 1.00 42.43  ? 215 HIS   A C   1 
ATOM   1424 O O   . HIS   A 1 215 ? 0.938   -26.845 -27.337 1.00 46.25  ? 215 HIS   A O   1 
ATOM   1425 C CB  . HIS   A 1 215 ? -0.776  -24.718 -27.023 1.00 40.47  ? 215 HIS   A CB  1 
ATOM   1426 C CG  . HIS   A 1 215 ? -1.400  -25.392 -25.840 1.00 38.89  ? 215 HIS   A CG  1 
ATOM   1427 N ND1 . HIS   A 1 215 ? -1.516  -26.761 -25.741 1.00 38.97  ? 215 HIS   A ND1 1 
ATOM   1428 C CD2 . HIS   A 1 215 ? -1.936  -24.886 -24.704 1.00 39.83  ? 215 HIS   A CD2 1 
ATOM   1429 C CE1 . HIS   A 1 215 ? -2.103  -27.071 -24.599 1.00 39.01  ? 215 HIS   A CE1 1 
ATOM   1430 N NE2 . HIS   A 1 215 ? -2.368  -25.951 -23.950 1.00 39.23  ? 215 HIS   A NE2 1 
ATOM   1431 N N   . TYR   A 1 216 ? 2.841   -25.654 -27.138 1.00 44.34  ? 216 TYR   A N   1 
ATOM   1432 C CA  . TYR   A 1 216 ? 3.717   -26.747 -27.526 1.00 45.00  ? 216 TYR   A CA  1 
ATOM   1433 C C   . TYR   A 1 216 ? 3.932   -27.698 -26.360 1.00 44.33  ? 216 TYR   A C   1 
ATOM   1434 O O   . TYR   A 1 216 ? 4.011   -27.277 -25.202 1.00 46.60  ? 216 TYR   A O   1 
ATOM   1435 C CB  . TYR   A 1 216 ? 5.073   -26.208 -27.984 1.00 48.68  ? 216 TYR   A CB  1 
ATOM   1436 C CG  . TYR   A 1 216 ? 5.046   -25.335 -29.220 1.00 47.84  ? 216 TYR   A CG  1 
ATOM   1437 C CD1 . TYR   A 1 216 ? 4.377   -25.735 -30.368 1.00 46.74  ? 216 TYR   A CD1 1 
ATOM   1438 C CD2 . TYR   A 1 216 ? 5.697   -24.109 -29.237 1.00 42.51  ? 216 TYR   A CD2 1 
ATOM   1439 C CE1 . TYR   A 1 216 ? 4.356   -24.938 -31.499 1.00 45.13  ? 216 TYR   A CE1 1 
ATOM   1440 C CE2 . TYR   A 1 216 ? 5.683   -23.307 -30.361 1.00 40.32  ? 216 TYR   A CE2 1 
ATOM   1441 C CZ  . TYR   A 1 216 ? 5.011   -23.725 -31.489 1.00 45.22  ? 216 TYR   A CZ  1 
ATOM   1442 O OH  . TYR   A 1 216 ? 4.994   -22.925 -32.608 1.00 47.55  ? 216 TYR   A OH  1 
ATOM   1443 N N   . PHE   A 1 217 ? 4.030   -28.984 -26.672 1.00 46.13  ? 217 PHE   A N   1 
ATOM   1444 C CA  . PHE   A 1 217 ? 4.591   -29.911 -25.706 1.00 45.61  ? 217 PHE   A CA  1 
ATOM   1445 C C   . PHE   A 1 217 ? 6.012   -29.459 -25.377 1.00 46.97  ? 217 PHE   A C   1 
ATOM   1446 O O   . PHE   A 1 217 ? 6.758   -29.064 -26.281 1.00 47.37  ? 217 PHE   A O   1 
ATOM   1447 C CB  . PHE   A 1 217 ? 4.595   -31.338 -26.256 1.00 43.34  ? 217 PHE   A CB  1 
ATOM   1448 C CG  . PHE   A 1 217 ? 4.917   -32.383 -25.225 1.00 44.17  ? 217 PHE   A CG  1 
ATOM   1449 C CD1 . PHE   A 1 217 ? 3.914   -32.936 -24.447 1.00 45.58  ? 217 PHE   A CD1 1 
ATOM   1450 C CD2 . PHE   A 1 217 ? 6.221   -32.805 -25.027 1.00 44.01  ? 217 PHE   A CD2 1 
ATOM   1451 C CE1 . PHE   A 1 217 ? 4.207   -33.892 -23.491 1.00 45.65  ? 217 PHE   A CE1 1 
ATOM   1452 C CE2 . PHE   A 1 217 ? 6.518   -33.759 -24.071 1.00 42.69  ? 217 PHE   A CE2 1 
ATOM   1453 C CZ  . PHE   A 1 217 ? 5.510   -34.303 -23.304 1.00 41.45  ? 217 PHE   A CZ  1 
ATOM   1454 N N   . PRO   A 1 218 ? 6.408   -29.473 -24.103 1.00 45.13  ? 218 PRO   A N   1 
ATOM   1455 C CA  . PRO   A 1 218 ? 7.701   -28.889 -23.721 1.00 44.98  ? 218 PRO   A CA  1 
ATOM   1456 C C   . PRO   A 1 218 ? 8.869   -29.486 -24.497 1.00 46.37  ? 218 PRO   A C   1 
ATOM   1457 O O   . PRO   A 1 218 ? 8.907   -30.685 -24.780 1.00 47.08  ? 218 PRO   A O   1 
ATOM   1458 C CB  . PRO   A 1 218 ? 7.797   -29.206 -22.225 1.00 46.28  ? 218 PRO   A CB  1 
ATOM   1459 C CG  . PRO   A 1 218 ? 6.362   -29.312 -21.787 1.00 45.06  ? 218 PRO   A CG  1 
ATOM   1460 C CD  . PRO   A 1 218 ? 5.678   -29.995 -22.933 1.00 46.35  ? 218 PRO   A CD  1 
ATOM   1461 N N   . ARG   A 1 219 ? 9.820   -28.618 -24.850 1.00 47.53  ? 219 ARG   A N   1 
ATOM   1462 C CA  . ARG   A 1 219 ? 11.022  -28.966 -25.607 1.00 47.98  ? 219 ARG   A CA  1 
ATOM   1463 C C   . ARG   A 1 219 ? 10.703  -29.459 -27.013 1.00 50.03  ? 219 ARG   A C   1 
ATOM   1464 O O   . ARG   A 1 219 ? 11.532  -30.122 -27.646 1.00 55.01  ? 219 ARG   A O   1 
ATOM   1465 C CB  . ARG   A 1 219 ? 11.871  -30.003 -24.861 1.00 48.07  ? 219 ARG   A CB  1 
ATOM   1466 C CG  . ARG   A 1 219 ? 12.141  -29.629 -23.417 1.00 47.64  ? 219 ARG   A CG  1 
ATOM   1467 C CD  . ARG   A 1 219 ? 13.611  -29.308 -23.180 1.00 55.65  ? 219 ARG   A CD  1 
ATOM   1468 N NE  . ARG   A 1 219 ? 13.867  -28.864 -21.813 1.00 53.93  ? 219 ARG   A NE  1 
ATOM   1469 C CZ  . ARG   A 1 219 ? 13.693  -29.608 -20.729 1.00 49.69  ? 219 ARG   A CZ  1 
ATOM   1470 N NH1 . ARG   A 1 219 ? 13.305  -30.870 -20.808 1.00 49.78  ? 219 ARG   A NH1 1 
ATOM   1471 N NH2 . ARG   A 1 219 ? 13.918  -29.072 -19.532 1.00 51.77  ? 219 ARG   A NH2 1 
ATOM   1472 N N   . THR   A 1 220 ? 9.508   -29.159 -27.514 1.00 47.60  ? 220 THR   A N   1 
ATOM   1473 C CA  . THR   A 1 220 ? 9.110   -29.492 -28.873 1.00 49.79  ? 220 THR   A CA  1 
ATOM   1474 C C   . THR   A 1 220 ? 8.446   -28.279 -29.511 1.00 49.17  ? 220 THR   A C   1 
ATOM   1475 O O   . THR   A 1 220 ? 8.217   -27.251 -28.867 1.00 45.17  ? 220 THR   A O   1 
ATOM   1476 C CB  . THR   A 1 220 ? 8.147   -30.693 -28.922 1.00 46.52  ? 220 THR   A CB  1 
ATOM   1477 O OG1 . THR   A 1 220 ? 6.804   -30.240 -28.707 1.00 47.07  ? 220 THR   A OG1 1 
ATOM   1478 C CG2 . THR   A 1 220 ? 8.504   -31.739 -27.875 1.00 41.89  ? 220 THR   A CG2 1 
ATOM   1479 N N   . ASP   A 1 221 ? 8.136   -28.412 -30.798 1.00 46.41  ? 221 ASP   A N   1 
ATOM   1480 C CA  . ASP   A 1 221 ? 7.353   -27.418 -31.519 1.00 47.89  ? 221 ASP   A CA  1 
ATOM   1481 C C   . ASP   A 1 221 ? 6.061   -28.036 -32.046 1.00 48.00  ? 221 ASP   A C   1 
ATOM   1482 O O   . ASP   A 1 221 ? 5.486   -27.564 -33.030 1.00 49.27  ? 221 ASP   A O   1 
ATOM   1483 C CB  . ASP   A 1 221 ? 8.180   -26.786 -32.641 1.00 45.85  ? 221 ASP   A CB  1 
ATOM   1484 C CG  . ASP   A 1 221 ? 8.259   -27.658 -33.876 1.00 48.26  ? 221 ASP   A CG  1 
ATOM   1485 O OD1 . ASP   A 1 221 ? 8.462   -28.880 -33.739 1.00 48.84  ? 221 ASP   A OD1 1 
ATOM   1486 O OD2 . ASP   A 1 221 ? 8.115   -27.112 -34.992 1.00 54.43  ? 221 ASP   A OD2 1 
ATOM   1487 N N   . SER   A 1 222 ? 5.584   -29.084 -31.374 1.00 47.25  ? 222 SER   A N   1 
ATOM   1488 C CA  . SER   A 1 222 ? 4.351   -29.769 -31.744 1.00 50.53  ? 222 SER   A CA  1 
ATOM   1489 C C   . SER   A 1 222 ? 3.234   -29.296 -30.821 1.00 50.46  ? 222 SER   A C   1 
ATOM   1490 O O   . SER   A 1 222 ? 3.202   -29.651 -29.638 1.00 48.61  ? 222 SER   A O   1 
ATOM   1491 C CB  . SER   A 1 222 ? 4.520   -31.286 -31.668 1.00 48.45  ? 222 SER   A CB  1 
ATOM   1492 O OG  . SER   A 1 222 ? 4.940   -31.694 -30.381 1.00 54.89  ? 222 SER   A OG  1 
ATOM   1493 N N   . ALA   A 1 223 ? 2.329   -28.486 -31.362 1.00 51.59  ? 223 ALA   A N   1 
ATOM   1494 C CA  . ALA   A 1 223 ? 1.138   -28.043 -30.655 1.00 50.05  ? 223 ALA   A CA  1 
ATOM   1495 C C   . ALA   A 1 223 ? -0.156  -28.502 -31.300 1.00 53.07  ? 223 ALA   A C   1 
ATOM   1496 O O   . ALA   A 1 223 ? -1.155  -28.661 -30.597 1.00 55.69  ? 223 ALA   A O   1 
ATOM   1497 C CB  . ALA   A 1 223 ? 1.107   -26.513 -30.553 1.00 51.83  ? 223 ALA   A CB  1 
ATOM   1498 N N   . LYS   A 1 224 ? -0.167  -28.714 -32.612 1.00 58.61  ? 224 LYS   A N   1 
ATOM   1499 C CA  . LYS   A 1 224 ? -1.387  -29.113 -33.298 1.00 57.24  ? 224 LYS   A CA  1 
ATOM   1500 C C   . LYS   A 1 224 ? -1.729  -30.555 -32.955 1.00 56.11  ? 224 LYS   A C   1 
ATOM   1501 O O   . LYS   A 1 224 ? -0.864  -31.437 -32.982 1.00 57.99  ? 224 LYS   A O   1 
ATOM   1502 C CB  . LYS   A 1 224 ? -1.235  -28.935 -34.808 1.00 58.93  ? 224 LYS   A CB  1 
ATOM   1503 C CG  . LYS   A 1 224 ? -1.864  -27.646 -35.315 1.00 63.58  ? 224 LYS   A CG  1 
ATOM   1504 C CD  . LYS   A 1 224 ? -0.860  -26.497 -35.314 1.00 60.00  ? 224 LYS   A CD  1 
ATOM   1505 C CE  . LYS   A 1 224 ? -1.525  -25.181 -35.695 1.00 64.06  ? 224 LYS   A CE  1 
ATOM   1506 N NZ  . LYS   A 1 224 ? -2.583  -24.784 -34.718 1.00 55.64  ? 224 LYS   A NZ  1 
ATOM   1507 N N   . ALA   A 1 225 ? -2.990  -30.782 -32.598 1.00 51.85  ? 225 ALA   A N   1 
ATOM   1508 C CA  . ALA   A 1 225 ? -3.479  -32.107 -32.241 1.00 51.04  ? 225 ALA   A CA  1 
ATOM   1509 C C   . ALA   A 1 225 ? -4.982  -32.121 -32.463 1.00 54.61  ? 225 ALA   A C   1 
ATOM   1510 O O   . ALA   A 1 225 ? -5.670  -31.159 -32.104 1.00 54.00  ? 225 ALA   A O   1 
ATOM   1511 C CB  . ALA   A 1 225 ? -3.141  -32.457 -30.785 1.00 51.91  ? 225 ALA   A CB  1 
ATOM   1512 N N   . ASP   A 1 226 ? -5.484  -33.197 -33.060 1.00 49.55  ? 226 ASP   A N   1 
ATOM   1513 C CA  . ASP   A 1 226 ? -6.901  -33.260 -33.382 1.00 48.40  ? 226 ASP   A CA  1 
ATOM   1514 C C   . ASP   A 1 226 ? -7.741  -33.321 -32.106 1.00 49.97  ? 226 ASP   A C   1 
ATOM   1515 O O   . ASP   A 1 226 ? -7.261  -33.699 -31.033 1.00 51.27  ? 226 ASP   A O   1 
ATOM   1516 C CB  . ASP   A 1 226 ? -7.181  -34.455 -34.291 1.00 48.62  ? 226 ASP   A CB  1 
ATOM   1517 C CG  . ASP   A 1 226 ? -6.416  -34.375 -35.600 1.00 52.92  ? 226 ASP   A CG  1 
ATOM   1518 O OD1 . ASP   A 1 226 ? -5.267  -34.865 -35.653 1.00 55.11  ? 226 ASP   A OD1 1 
ATOM   1519 O OD2 . ASP   A 1 226 ? -6.957  -33.804 -36.571 1.00 53.18  ? 226 ASP   A OD2 1 
ATOM   1520 N N   . LEU   A 1 227 ? -9.008  -32.912 -32.240 1.00 46.66  ? 227 LEU   A N   1 
ATOM   1521 C CA  . LEU   A 1 227 ? -9.985  -32.803 -31.157 1.00 44.70  ? 227 LEU   A CA  1 
ATOM   1522 C C   . LEU   A 1 227 ? -9.674  -31.662 -30.194 1.00 42.59  ? 227 LEU   A C   1 
ATOM   1523 O O   . LEU   A 1 227 ? -10.574 -31.166 -29.512 1.00 43.41  ? 227 LEU   A O   1 
ATOM   1524 C CB  . LEU   A 1 227 ? -10.111 -34.111 -30.366 1.00 43.99  ? 227 LEU   A CB  1 
ATOM   1525 C CG  . LEU   A 1 227 ? -10.379 -35.415 -31.113 1.00 47.01  ? 227 LEU   A CG  1 
ATOM   1526 C CD1 . LEU   A 1 227 ? -9.864  -36.598 -30.307 1.00 41.10  ? 227 LEU   A CD1 1 
ATOM   1527 C CD2 . LEU   A 1 227 ? -11.864 -35.552 -31.401 1.00 42.28  ? 227 LEU   A CD2 1 
ATOM   1528 N N   . SER   A 1 228 ? -8.420  -31.226 -30.136 1.00 40.90  ? 228 SER   A N   1 
ATOM   1529 C CA  . SER   A 1 228 ? -8.008  -30.245 -29.143 1.00 41.07  ? 228 SER   A CA  1 
ATOM   1530 C C   . SER   A 1 228 ? -8.304  -28.830 -29.617 1.00 41.33  ? 228 SER   A C   1 
ATOM   1531 O O   . SER   A 1 228 ? -8.129  -28.505 -30.795 1.00 40.89  ? 228 SER   A O   1 
ATOM   1532 C CB  . SER   A 1 228 ? -6.521  -30.383 -28.837 1.00 43.16  ? 228 SER   A CB  1 
ATOM   1533 O OG  . SER   A 1 228 ? -6.154  -29.487 -27.803 1.00 45.20  ? 228 SER   A OG  1 
ATOM   1534 N N   . VAL   A 1 229 ? -8.773  -27.989 -28.688 1.00 40.74  ? 229 VAL   A N   1 
ATOM   1535 C CA  . VAL   A 1 229 ? -9.041  -26.579 -28.946 1.00 39.69  ? 229 VAL   A CA  1 
ATOM   1536 C C   . VAL   A 1 229 ? -8.573  -25.763 -27.749 1.00 40.99  ? 229 VAL   A C   1 
ATOM   1537 O O   . VAL   A 1 229 ? -8.407  -26.280 -26.643 1.00 38.11  ? 229 VAL   A O   1 
ATOM   1538 C CB  . VAL   A 1 229 ? -10.537 -26.283 -29.211 1.00 38.59  ? 229 VAL   A CB  1 
ATOM   1539 C CG1 . VAL   A 1 229 ? -11.096 -27.213 -30.270 1.00 39.15  ? 229 VAL   A CG1 1 
ATOM   1540 C CG2 . VAL   A 1 229 ? -11.339 -26.384 -27.918 1.00 38.32  ? 229 VAL   A CG2 1 
ATOM   1541 N N   . VAL   A 1 230 ? -8.368  -24.467 -27.984 1.00 39.60  ? 230 VAL   A N   1 
ATOM   1542 C CA  . VAL   A 1 230 ? -8.062  -23.509 -26.931 1.00 37.09  ? 230 VAL   A CA  1 
ATOM   1543 C C   . VAL   A 1 230 ? -9.168  -22.463 -26.907 1.00 39.13  ? 230 VAL   A C   1 
ATOM   1544 O O   . VAL   A 1 230 ? -9.730  -22.105 -27.947 1.00 41.13  ? 230 VAL   A O   1 
ATOM   1545 C CB  . VAL   A 1 230 ? -6.682  -22.847 -27.130 1.00 39.40  ? 230 VAL   A CB  1 
ATOM   1546 C CG1 . VAL   A 1 230 ? -5.577  -23.856 -26.875 1.00 38.83  ? 230 VAL   A CG1 1 
ATOM   1547 C CG2 . VAL   A 1 230 ? -6.567  -22.271 -28.531 1.00 39.87  ? 230 VAL   A CG2 1 
ATOM   1548 N N   . GLY   A 1 231 ? -9.487  -21.977 -25.710 1.00 35.35  ? 231 GLY   A N   1 
ATOM   1549 C CA  . GLY   A 1 231 ? -10.609 -21.085 -25.551 1.00 36.92  ? 231 GLY   A CA  1 
ATOM   1550 C C   . GLY   A 1 231 ? -10.547 -20.203 -24.320 1.00 38.16  ? 231 GLY   A C   1 
ATOM   1551 O O   . GLY   A 1 231 ? -9.778  -20.444 -23.383 1.00 38.51  ? 231 GLY   A O   1 
ATOM   1552 N N   . PRO   A 1 232 ? -11.366 -19.157 -24.306 1.00 39.42  ? 232 PRO   A N   1 
ATOM   1553 C CA  . PRO   A 1 232 ? -11.333 -18.192 -23.204 1.00 37.43  ? 232 PRO   A CA  1 
ATOM   1554 C C   . PRO   A 1 232 ? -12.103 -18.680 -21.985 1.00 37.27  ? 232 PRO   A C   1 
ATOM   1555 O O   . PRO   A 1 232 ? -13.011 -19.509 -22.071 1.00 39.05  ? 232 PRO   A O   1 
ATOM   1556 C CB  . PRO   A 1 232 ? -12.002 -16.955 -23.812 1.00 38.09  ? 232 PRO   A CB  1 
ATOM   1557 C CG  . PRO   A 1 232 ? -12.976 -17.536 -24.791 1.00 36.34  ? 232 PRO   A CG  1 
ATOM   1558 C CD  . PRO   A 1 232 ? -12.245 -18.708 -25.401 1.00 37.48  ? 232 PRO   A CD  1 
ATOM   1559 N N   . MET   A 1 233 ? -11.716 -18.133 -20.833 1.00 37.27  ? 233 MET   A N   1 
ATOM   1560 C CA  . MET   A 1 233 ? -12.351 -18.415 -19.553 1.00 38.08  ? 233 MET   A CA  1 
ATOM   1561 C C   . MET   A 1 233 ? -12.474 -17.112 -18.777 1.00 37.23  ? 233 MET   A C   1 
ATOM   1562 O O   . MET   A 1 233 ? -11.527 -16.324 -18.733 1.00 39.10  ? 233 MET   A O   1 
ATOM   1563 C CB  . MET   A 1 233 ? -11.548 -19.444 -18.746 1.00 33.26  ? 233 MET   A CB  1 
ATOM   1564 C CG  . MET   A 1 233 ? -11.653 -20.867 -19.281 1.00 34.78  ? 233 MET   A CG  1 
ATOM   1565 S SD  . MET   A 1 233 ? -10.390 -21.993 -18.646 1.00 38.03  ? 233 MET   A SD  1 
ATOM   1566 C CE  . MET   A 1 233 ? -11.215 -22.627 -17.192 1.00 32.42  ? 233 MET   A CE  1 
ATOM   1567 N N   . ALA   A 1 234 ? -13.641 -16.877 -18.183 1.00 34.47  ? 234 ALA   A N   1 
ATOM   1568 C CA  . ALA   A 1 234 ? -13.908 -15.599 -17.534 1.00 37.70  ? 234 ALA   A CA  1 
ATOM   1569 C C   . ALA   A 1 234 ? -15.092 -15.753 -16.591 1.00 35.90  ? 234 ALA   A C   1 
ATOM   1570 O O   . ALA   A 1 234 ? -15.608 -16.853 -16.376 1.00 35.42  ? 234 ALA   A O   1 
ATOM   1571 C CB  . ALA   A 1 234 ? -14.170 -14.500 -18.568 1.00 35.73  ? 234 ALA   A CB  1 
ATOM   1572 N N   . ARG   A 1 235 ? -15.523 -14.622 -16.031 1.00 36.86  ? 235 ARG   A N   1 
ATOM   1573 C CA  . ARG   A 1 235 ? -16.712 -14.568 -15.192 1.00 36.94  ? 235 ARG   A CA  1 
ATOM   1574 C C   . ARG   A 1 235 ? -17.905 -13.930 -15.894 1.00 38.30  ? 235 ARG   A C   1 
ATOM   1575 O O   . ARG   A 1 235 ? -19.016 -13.983 -15.358 1.00 39.85  ? 235 ARG   A O   1 
ATOM   1576 C CB  . ARG   A 1 235 ? -16.423 -13.796 -13.899 1.00 37.96  ? 235 ARG   A CB  1 
ATOM   1577 C CG  . ARG   A 1 235 ? -15.224 -14.288 -13.102 1.00 40.33  ? 235 ARG   A CG  1 
ATOM   1578 C CD  . ARG   A 1 235 ? -15.328 -13.790 -11.679 1.00 40.14  ? 235 ARG   A CD  1 
ATOM   1579 N NE  . ARG   A 1 235 ? -14.749 -12.461 -11.523 1.00 47.38  ? 235 ARG   A NE  1 
ATOM   1580 C CZ  . ARG   A 1 235 ? -13.455 -12.178 -11.575 1.00 43.23  ? 235 ARG   A CZ  1 
ATOM   1581 N NH1 . ARG   A 1 235 ? -12.536 -13.129 -11.600 1.00 42.16  ? 235 ARG   A NH1 1 
ATOM   1582 N NH2 . ARG   A 1 235 ? -13.070 -10.904 -11.594 1.00 44.37  ? 235 ARG   A NH2 1 
ATOM   1583 N N   . THR   A 1 236 ? -17.704 -13.312 -17.055 1.00 36.57  ? 236 THR   A N   1 
ATOM   1584 C CA  . THR   A 1 236 ? -18.796 -12.731 -17.821 1.00 36.80  ? 236 THR   A CA  1 
ATOM   1585 C C   . THR   A 1 236 ? -18.733 -13.202 -19.265 1.00 37.60  ? 236 THR   A C   1 
ATOM   1586 O O   . THR   A 1 236 ? -17.645 -13.429 -19.806 1.00 36.14  ? 236 THR   A O   1 
ATOM   1587 C CB  . THR   A 1 236 ? -18.774 -11.193 -17.797 1.00 36.20  ? 236 THR   A CB  1 
ATOM   1588 O OG1 . THR   A 1 236 ? -17.859 -10.702 -18.786 1.00 36.30  ? 236 THR   A OG1 1 
ATOM   1589 C CG2 . THR   A 1 236 ? -18.381 -10.666 -16.423 1.00 35.68  ? 236 THR   A CG2 1 
ATOM   1590 N N   . PRO   A 1 237 ? -19.889 -13.362 -19.914 1.00 38.87  ? 237 PRO   A N   1 
ATOM   1591 C CA  . PRO   A 1 237 ? -19.873 -13.740 -21.336 1.00 36.57  ? 237 PRO   A CA  1 
ATOM   1592 C C   . PRO   A 1 237 ? -19.324 -12.648 -22.237 1.00 37.18  ? 237 PRO   A C   1 
ATOM   1593 O O   . PRO   A 1 237 ? -18.781 -12.959 -23.304 1.00 35.84  ? 237 PRO   A O   1 
ATOM   1594 C CB  . PRO   A 1 237 ? -21.349 -14.043 -21.636 1.00 37.16  ? 237 PRO   A CB  1 
ATOM   1595 C CG  . PRO   A 1 237 ? -22.115 -13.304 -20.584 1.00 35.23  ? 237 PRO   A CG  1 
ATOM   1596 C CD  . PRO   A 1 237 ? -21.253 -13.328 -19.360 1.00 34.89  ? 237 PRO   A CD  1 
ATOM   1597 N N   . ALA   A 1 238 ? -19.443 -11.377 -21.841 1.00 35.76  ? 238 ALA   A N   1 
ATOM   1598 C CA  . ALA   A 1 238 ? -18.846 -10.303 -22.628 1.00 39.16  ? 238 ALA   A CA  1 
ATOM   1599 C C   . ALA   A 1 238 ? -17.330 -10.449 -22.695 1.00 40.51  ? 238 ALA   A C   1 
ATOM   1600 O O   . ALA   A 1 238 ? -16.715 -10.169 -23.732 1.00 39.45  ? 238 ALA   A O   1 
ATOM   1601 C CB  . ALA   A 1 238 ? -19.234 -8.945  -22.043 1.00 37.59  ? 238 ALA   A CB  1 
ATOM   1602 N N   . ASP   A 1 239 ? -16.712 -10.893 -21.597 1.00 37.26  ? 239 ASP   A N   1 
ATOM   1603 C CA  . ASP   A 1 239 ? -15.272 -11.130 -21.592 1.00 39.42  ? 239 ASP   A CA  1 
ATOM   1604 C C   . ASP   A 1 239 ? -14.894 -12.283 -22.522 1.00 36.62  ? 239 ASP   A C   1 
ATOM   1605 O O   . ASP   A 1 239 ? -13.872 -12.220 -23.217 1.00 34.22  ? 239 ASP   A O   1 
ATOM   1606 C CB  . ASP   A 1 239 ? -14.797 -11.410 -20.163 1.00 39.50  ? 239 ASP   A CB  1 
ATOM   1607 C CG  . ASP   A 1 239 ? -14.551 -10.140 -19.360 1.00 41.62  ? 239 ASP   A CG  1 
ATOM   1608 O OD1 . ASP   A 1 239 ? -14.747 -9.032  -19.905 1.00 44.32  ? 239 ASP   A OD1 1 
ATOM   1609 O OD2 . ASP   A 1 239 ? -14.160 -10.252 -18.176 1.00 40.50  ? 239 ASP   A OD2 1 
ATOM   1610 N N   . LEU   A 1 240 ? -15.705 -13.347 -22.548 1.00 33.50  ? 240 LEU   A N   1 
ATOM   1611 C CA  . LEU   A 1 240 ? -15.432 -14.459 -23.457 1.00 34.05  ? 240 LEU   A CA  1 
ATOM   1612 C C   . LEU   A 1 240 ? -15.536 -14.021 -24.912 1.00 36.03  ? 240 LEU   A C   1 
ATOM   1613 O O   . LEU   A 1 240 ? -14.676 -14.358 -25.733 1.00 37.89  ? 240 LEU   A O   1 
ATOM   1614 C CB  . LEU   A 1 240 ? -16.387 -15.621 -23.193 1.00 36.25  ? 240 LEU   A CB  1 
ATOM   1615 C CG  . LEU   A 1 240 ? -16.501 -16.207 -21.790 1.00 37.49  ? 240 LEU   A CG  1 
ATOM   1616 C CD1 . LEU   A 1 240 ? -17.812 -16.966 -21.674 1.00 36.00  ? 240 LEU   A CD1 1 
ATOM   1617 C CD2 . LEU   A 1 240 ? -15.320 -17.112 -21.490 1.00 34.67  ? 240 LEU   A CD2 1 
ATOM   1618 N N   . ALA   A 1 241 ? -16.588 -13.269 -25.251 1.00 34.96  ? 241 ALA   A N   1 
ATOM   1619 C CA  . ALA   A 1 241 ? -16.774 -12.832 -26.632 1.00 39.09  ? 241 ALA   A CA  1 
ATOM   1620 C C   . ALA   A 1 241 ? -15.617 -11.957 -27.100 1.00 39.35  ? 241 ALA   A C   1 
ATOM   1621 O O   . ALA   A 1 241 ? -15.144 -12.099 -28.234 1.00 38.42  ? 241 ALA   A O   1 
ATOM   1622 C CB  . ALA   A 1 241 ? -18.102 -12.089 -26.775 1.00 41.00  ? 241 ALA   A CB  1 
ATOM   1623 N N   . LEU   A 1 242 ? -15.143 -11.052 -26.239 1.00 33.66  ? 242 LEU   A N   1 
ATOM   1624 C CA  . LEU   A 1 242 ? -14.050 -10.167 -26.631 1.00 36.90  ? 242 LEU   A CA  1 
ATOM   1625 C C   . LEU   A 1 242 ? -12.734 -10.926 -26.753 1.00 36.92  ? 242 LEU   A C   1 
ATOM   1626 O O   . LEU   A 1 242 ? -11.983 -10.721 -27.713 1.00 37.87  ? 242 LEU   A O   1 
ATOM   1627 C CB  . LEU   A 1 242 ? -13.915 -9.013  -25.637 1.00 36.10  ? 242 LEU   A CB  1 
ATOM   1628 C CG  . LEU   A 1 242 ? -12.672 -8.135  -25.817 1.00 35.55  ? 242 LEU   A CG  1 
ATOM   1629 C CD1 . LEU   A 1 242 ? -12.701 -7.407  -27.156 1.00 38.13  ? 242 LEU   A CD1 1 
ATOM   1630 C CD2 . LEU   A 1 242 ? -12.513 -7.150  -24.672 1.00 34.01  ? 242 LEU   A CD2 1 
ATOM   1631 N N   . ALA   A 1 243 ? -12.432 -11.802 -25.791 1.00 36.74  ? 243 ALA   A N   1 
ATOM   1632 C CA  . ALA   A 1 243 ? -11.211 -12.596 -25.877 1.00 37.66  ? 243 ALA   A CA  1 
ATOM   1633 C C   . ALA   A 1 243 ? -11.219 -13.505 -27.099 1.00 39.39  ? 243 ALA   A C   1 
ATOM   1634 O O   . ALA   A 1 243 ? -10.167 -13.741 -27.704 1.00 37.38  ? 243 ALA   A O   1 
ATOM   1635 C CB  . ALA   A 1 243 ? -11.026 -13.421 -24.606 1.00 39.57  ? 243 ALA   A CB  1 
ATOM   1636 N N   . LEU   A 1 244 ? -12.392 -14.019 -27.480 1.00 36.91  ? 244 LEU   A N   1 
ATOM   1637 C CA  . LEU   A 1 244 ? -12.477 -14.848 -28.677 1.00 36.49  ? 244 LEU   A CA  1 
ATOM   1638 C C   . LEU   A 1 244 ? -12.218 -14.028 -29.937 1.00 40.82  ? 244 LEU   A C   1 
ATOM   1639 O O   . LEU   A 1 244 ? -11.556 -14.502 -30.866 1.00 40.26  ? 244 LEU   A O   1 
ATOM   1640 C CB  . LEU   A 1 244 ? -13.844 -15.530 -28.744 1.00 37.25  ? 244 LEU   A CB  1 
ATOM   1641 C CG  . LEU   A 1 244 ? -14.216 -16.246 -30.045 1.00 38.52  ? 244 LEU   A CG  1 
ATOM   1642 C CD1 . LEU   A 1 244 ? -13.453 -17.552 -30.185 1.00 41.20  ? 244 LEU   A CD1 1 
ATOM   1643 C CD2 . LEU   A 1 244 ? -15.710 -16.491 -30.108 1.00 38.03  ? 244 LEU   A CD2 1 
ATOM   1644 N N   . ASP   A 1 245 ? -12.725 -12.791 -29.986 1.00 44.17  ? 245 ASP   A N   1 
ATOM   1645 C CA  . ASP   A 1 245 ? -12.465 -11.932 -31.139 1.00 43.35  ? 245 ASP   A CA  1 
ATOM   1646 C C   . ASP   A 1 245 ? -10.998 -11.541 -31.228 1.00 42.23  ? 245 ASP   A C   1 
ATOM   1647 O O   . ASP   A 1 245 ? -10.470 -11.355 -32.330 1.00 43.02  ? 245 ASP   A O   1 
ATOM   1648 C CB  . ASP   A 1 245 ? -13.334 -10.678 -31.078 1.00 41.34  ? 245 ASP   A CB  1 
ATOM   1649 C CG  . ASP   A 1 245 ? -14.771 -10.948 -31.465 1.00 45.95  ? 245 ASP   A CG  1 
ATOM   1650 O OD1 . ASP   A 1 245 ? -15.001 -11.821 -32.331 1.00 46.44  ? 245 ASP   A OD1 1 
ATOM   1651 O OD2 . ASP   A 1 245 ? -15.669 -10.280 -30.911 1.00 48.11  ? 245 ASP   A OD2 1 
ATOM   1652 N N   . ILE   A 1 246 ? -10.328 -11.412 -30.080 1.00 42.21  ? 246 ILE   A N   1 
ATOM   1653 C CA  . ILE   A 1 246 ? -8.910  -11.075 -30.063 1.00 39.16  ? 246 ILE   A CA  1 
ATOM   1654 C C   . ILE   A 1 246 ? -8.063  -12.248 -30.550 1.00 40.09  ? 246 ILE   A C   1 
ATOM   1655 O O   . ILE   A 1 246 ? -7.032  -12.048 -31.205 1.00 37.02  ? 246 ILE   A O   1 
ATOM   1656 C CB  . ILE   A 1 246 ? -8.510  -10.620 -28.644 1.00 36.38  ? 246 ILE   A CB  1 
ATOM   1657 C CG1 . ILE   A 1 246 ? -9.118  -9.249  -28.330 1.00 40.51  ? 246 ILE   A CG1 1 
ATOM   1658 C CG2 . ILE   A 1 246 ? -7.000  -10.571 -28.479 1.00 39.84  ? 246 ILE   A CG2 1 
ATOM   1659 C CD1 . ILE   A 1 246 ? -9.129  -8.894  -26.857 1.00 40.53  ? 246 ILE   A CD1 1 
ATOM   1660 N N   . THR   A 1 247 ? -8.495  -13.483 -30.281 1.00 38.23  ? 247 THR   A N   1 
ATOM   1661 C CA  . THR   A 1 247 ? -7.643  -14.654 -30.453 1.00 37.52  ? 247 THR   A CA  1 
ATOM   1662 C C   . THR   A 1 247 ? -7.965  -15.497 -31.683 1.00 39.17  ? 247 THR   A C   1 
ATOM   1663 O O   . THR   A 1 247 ? -7.117  -16.299 -32.092 1.00 36.85  ? 247 THR   A O   1 
ATOM   1664 C CB  . THR   A 1 247 ? -7.726  -15.548 -29.210 1.00 39.03  ? 247 THR   A CB  1 
ATOM   1665 O OG1 . THR   A 1 247 ? -9.101  -15.832 -28.918 1.00 39.96  ? 247 THR   A OG1 1 
ATOM   1666 C CG2 . THR   A 1 247 ? -7.087  -14.861 -28.009 1.00 37.21  ? 247 THR   A CG2 1 
ATOM   1667 N N   . SER   A 1 248 ? -9.149  -15.352 -32.276 1.00 38.93  ? 248 SER   A N   1 
ATOM   1668 C CA  . SER   A 1 248 ? -9.534  -16.214 -33.389 1.00 41.23  ? 248 SER   A CA  1 
ATOM   1669 C C   . SER   A 1 248 ? -8.669  -15.946 -34.618 1.00 38.01  ? 248 SER   A C   1 
ATOM   1670 O O   . SER   A 1 248 ? -8.179  -14.833 -34.829 1.00 41.03  ? 248 SER   A O   1 
ATOM   1671 C CB  . SER   A 1 248 ? -11.009 -16.017 -33.745 1.00 41.00  ? 248 SER   A CB  1 
ATOM   1672 O OG  . SER   A 1 248 ? -11.353 -14.642 -33.804 1.00 42.40  ? 248 SER   A OG  1 
ATOM   1673 N N   . LYS   A 1 249 ? -8.480  -16.992 -35.430 1.00 37.01  ? 249 LYS   A N   1 
ATOM   1674 C CA  . LYS   A 1 249 ? -7.698  -16.851 -36.657 1.00 39.39  ? 249 LYS   A CA  1 
ATOM   1675 C C   . LYS   A 1 249 ? -8.275  -15.764 -37.553 1.00 41.59  ? 249 LYS   A C   1 
ATOM   1676 O O   . LYS   A 1 249 ? -7.535  -14.941 -38.106 1.00 43.60  ? 249 LYS   A O   1 
ATOM   1677 C CB  . LYS   A 1 249 ? -7.641  -18.184 -37.404 1.00 37.52  ? 249 LYS   A CB  1 
ATOM   1678 C CG  . LYS   A 1 249 ? -6.977  -19.312 -36.632 1.00 41.02  ? 249 LYS   A CG  1 
ATOM   1679 C CD  . LYS   A 1 249 ? -7.040  -20.624 -37.409 1.00 42.76  ? 249 LYS   A CD  1 
ATOM   1680 C CE  . LYS   A 1 249 ? -6.249  -21.722 -36.720 1.00 41.67  ? 249 LYS   A CE  1 
ATOM   1681 N NZ  . LYS   A 1 249 ? -6.687  -23.080 -37.147 1.00 44.46  ? 249 LYS   A NZ  1 
ATOM   1682 N N   . VAL   A 1 250 ? -9.594  -15.749 -37.709 1.00 40.41  ? 250 VAL   A N   1 
ATOM   1683 C CA  . VAL   A 1 250 ? -10.304 -14.671 -38.392 1.00 40.08  ? 250 VAL   A CA  1 
ATOM   1684 C C   . VAL   A 1 250 ? -11.465 -14.247 -37.505 1.00 43.24  ? 250 VAL   A C   1 
ATOM   1685 O O   . VAL   A 1 250 ? -11.863 -14.986 -36.589 1.00 44.39  ? 250 VAL   A O   1 
ATOM   1686 C CB  . VAL   A 1 250 ? -10.808 -15.108 -39.790 1.00 38.70  ? 250 VAL   A CB  1 
ATOM   1687 C CG1 . VAL   A 1 250 ? -9.647  -15.499 -40.683 1.00 40.49  ? 250 VAL   A CG1 1 
ATOM   1688 C CG2 . VAL   A 1 250 ? -11.805 -16.252 -39.668 1.00 35.58  ? 250 VAL   A CG2 1 
ATOM   1689 N N   . PRO   A 1 251 ? -12.022 -13.059 -37.734 1.00 38.96  ? 251 PRO   A N   1 
ATOM   1690 C CA  . PRO   A 1 251 ? -13.253 -12.686 -37.029 1.00 41.90  ? 251 PRO   A CA  1 
ATOM   1691 C C   . PRO   A 1 251 ? -14.371 -13.679 -37.317 1.00 42.60  ? 251 PRO   A C   1 
ATOM   1692 O O   . PRO   A 1 251 ? -14.713 -13.940 -38.472 1.00 44.20  ? 251 PRO   A O   1 
ATOM   1693 C CB  . PRO   A 1 251 ? -13.569 -11.295 -37.589 1.00 44.22  ? 251 PRO   A CB  1 
ATOM   1694 C CG  . PRO   A 1 251 ? -12.235 -10.753 -37.984 1.00 42.68  ? 251 PRO   A CG  1 
ATOM   1695 C CD  . PRO   A 1 251 ? -11.489 -11.938 -38.530 1.00 40.25  ? 251 PRO   A CD  1 
ATOM   1696 N N   . LEU   A 1 252 ? -14.938 -14.238 -36.247 1.00 41.98  ? 252 LEU   A N   1 
ATOM   1697 C CA  . LEU   A 1 252 ? -16.031 -15.196 -36.300 1.00 42.55  ? 252 LEU   A CA  1 
ATOM   1698 C C   . LEU   A 1 252 ? -17.374 -14.469 -36.359 1.00 44.16  ? 252 LEU   A C   1 
ATOM   1699 O O   . LEU   A 1 252 ? -17.504 -13.349 -35.850 1.00 48.95  ? 252 LEU   A O   1 
ATOM   1700 C CB  . LEU   A 1 252 ? -15.990 -16.110 -35.079 1.00 43.46  ? 252 LEU   A CB  1 
ATOM   1701 C CG  . LEU   A 1 252 ? -14.832 -17.112 -35.092 1.00 44.51  ? 252 LEU   A CG  1 
ATOM   1702 C CD1 . LEU   A 1 252 ? -14.988 -18.135 -33.984 1.00 42.00  ? 252 LEU   A CD1 1 
ATOM   1703 C CD2 . LEU   A 1 252 ? -14.733 -17.798 -36.445 1.00 42.60  ? 252 LEU   A CD2 1 
ATOM   1704 N N   . PRO   A 1 253 ? -18.386 -15.077 -36.978 1.00 43.13  ? 253 PRO   A N   1 
ATOM   1705 C CA  . PRO   A 1 253 ? -19.679 -14.391 -37.141 1.00 45.98  ? 253 PRO   A CA  1 
ATOM   1706 C C   . PRO   A 1 253 ? -20.309 -14.044 -35.801 1.00 44.76  ? 253 PRO   A C   1 
ATOM   1707 O O   . PRO   A 1 253 ? -20.530 -14.911 -34.951 1.00 48.01  ? 253 PRO   A O   1 
ATOM   1708 C CB  . PRO   A 1 253 ? -20.523 -15.414 -37.913 1.00 42.16  ? 253 PRO   A CB  1 
ATOM   1709 C CG  . PRO   A 1 253 ? -19.523 -16.316 -38.573 1.00 43.11  ? 253 PRO   A CG  1 
ATOM   1710 C CD  . PRO   A 1 253 ? -18.403 -16.418 -37.584 1.00 44.35  ? 253 PRO   A CD  1 
ATOM   1711 N N   . GLN   A 1 254 ? -20.601 -12.759 -35.618 1.00 46.74  ? 254 GLN   A N   1 
ATOM   1712 C CA  . GLN   A 1 254 ? -21.266 -12.305 -34.409 1.00 43.85  ? 254 GLN   A CA  1 
ATOM   1713 C C   . GLN   A 1 254 ? -22.689 -12.853 -34.352 1.00 44.21  ? 254 GLN   A C   1 
ATOM   1714 O O   . GLN   A 1 254 ? -23.268 -13.270 -35.359 1.00 47.59  ? 254 GLN   A O   1 
ATOM   1715 C CB  . GLN   A 1 254 ? -21.282 -10.777 -34.344 1.00 46.12  ? 254 GLN   A CB  1 
ATOM   1716 C CG  . GLN   A 1 254 ? -19.901 -10.146 -34.397 1.00 38.54  ? 254 GLN   A CG  1 
ATOM   1717 C CD  . GLN   A 1 254 ? -19.120 -10.327 -33.108 1.00 42.82  ? 254 GLN   A CD  1 
ATOM   1718 O OE1 . GLN   A 1 254 ? -19.693 -10.396 -32.020 1.00 41.91  ? 254 GLN   A OE1 1 
ATOM   1719 N NE2 . GLN   A 1 254 ? -17.801 -10.420 -33.229 1.00 49.01  ? 254 GLN   A NE2 1 
ATOM   1720 N N   . SER   A 1 255 ? -23.254 -12.850 -33.151 1.00 45.40  ? 255 SER   A N   1 
ATOM   1721 C CA  . SER   A 1 255 ? -24.559 -13.450 -32.923 1.00 44.97  ? 255 SER   A CA  1 
ATOM   1722 C C   . SER   A 1 255 ? -25.671 -12.446 -33.191 1.00 48.22  ? 255 SER   A C   1 
ATOM   1723 O O   . SER   A 1 255 ? -25.603 -11.291 -32.764 1.00 48.56  ? 255 SER   A O   1 
ATOM   1724 C CB  . SER   A 1 255 ? -24.668 -13.975 -31.492 1.00 41.83  ? 255 SER   A CB  1 
ATOM   1725 O OG  . SER   A 1 255 ? -25.952 -14.525 -31.255 1.00 43.55  ? 255 SER   A OG  1 
ATOM   1726 N N   . ARG   A 1 256 ? -26.703 -12.903 -33.892 1.00 48.98  ? 256 ARG   A N   1 
ATOM   1727 C CA  . ARG   A 1 256 ? -27.877 -12.094 -34.171 1.00 51.33  ? 256 ARG   A CA  1 
ATOM   1728 C C   . ARG   A 1 256 ? -29.057 -12.467 -33.283 1.00 50.29  ? 256 ARG   A C   1 
ATOM   1729 O O   . ARG   A 1 256 ? -30.179 -12.018 -33.535 1.00 52.36  ? 256 ARG   A O   1 
ATOM   1730 C CB  . ARG   A 1 256 ? -28.259 -12.222 -35.645 1.00 54.89  ? 256 ARG   A CB  1 
ATOM   1731 C CG  . ARG   A 1 256 ? -27.174 -11.744 -36.595 1.00 57.57  ? 256 ARG   A CG  1 
ATOM   1732 C CD  . ARG   A 1 256 ? -27.750 -10.887 -37.702 1.00 70.76  ? 256 ARG   A CD  1 
ATOM   1733 N NE  . ARG   A 1 256 ? -27.084 -11.123 -38.976 1.00 77.67  ? 256 ARG   A NE  1 
ATOM   1734 C CZ  . ARG   A 1 256 ? -27.389 -10.500 -40.106 1.00 82.91  ? 256 ARG   A CZ  1 
ATOM   1735 N NH1 . ARG   A 1 256 ? -28.361 -9.603  -40.160 1.00 77.57  ? 256 ARG   A NH1 1 
ATOM   1736 N NH2 . ARG   A 1 256 ? -26.701 -10.782 -41.209 1.00 81.21  ? 256 ARG   A NH2 1 
ATOM   1737 N N   . ILE   A 1 257 ? -28.827 -13.281 -32.257 1.00 49.32  ? 257 ILE   A N   1 
ATOM   1738 C CA  . ILE   A 1 257 ? -29.879 -13.676 -31.326 1.00 47.49  ? 257 ILE   A CA  1 
ATOM   1739 C C   . ILE   A 1 257 ? -30.069 -12.540 -30.327 1.00 47.95  ? 257 ILE   A C   1 
ATOM   1740 O O   . ILE   A 1 257 ? -29.187 -12.266 -29.510 1.00 46.79  ? 257 ILE   A O   1 
ATOM   1741 C CB  . ILE   A 1 257 ? -29.536 -14.991 -30.617 1.00 47.14  ? 257 ILE   A CB  1 
ATOM   1742 C CG1 . ILE   A 1 257 ? -28.922 -15.983 -31.609 1.00 46.35  ? 257 ILE   A CG1 1 
ATOM   1743 C CG2 . ILE   A 1 257 ? -30.774 -15.578 -29.951 1.00 45.27  ? 257 ILE   A CG2 1 
ATOM   1744 C CD1 . ILE   A 1 257 ? -28.316 -17.205 -30.960 1.00 43.67  ? 257 ILE   A CD1 1 
ATOM   1745 N N   . ALA   A 1 258 ? -31.222 -11.872 -30.395 1.00 49.14  ? 258 ALA   A N   1 
ATOM   1746 C CA  . ALA   A 1 258 ? -31.512 -10.757 -29.500 1.00 44.40  ? 258 ALA   A CA  1 
ATOM   1747 C C   . ALA   A 1 258 ? -32.158 -11.214 -28.199 1.00 47.90  ? 258 ALA   A C   1 
ATOM   1748 O O   . ALA   A 1 258 ? -31.862 -10.660 -27.135 1.00 44.95  ? 258 ALA   A O   1 
ATOM   1749 C CB  . ALA   A 1 258 ? -32.417 -9.739  -30.197 1.00 49.09  ? 258 ALA   A CB  1 
ATOM   1750 N N   . ASN   A 1 259 ? -33.036 -12.210 -28.261 1.00 48.27  ? 259 ASN   A N   1 
ATOM   1751 C CA  . ASN   A 1 259 ? -33.683 -12.735 -27.071 1.00 49.11  ? 259 ASN   A CA  1 
ATOM   1752 C C   . ASN   A 1 259 ? -33.933 -14.226 -27.272 1.00 50.15  ? 259 ASN   A C   1 
ATOM   1753 O O   . ASN   A 1 259 ? -33.589 -14.802 -28.308 1.00 51.31  ? 259 ASN   A O   1 
ATOM   1754 C CB  . ASN   A 1 259 ? -34.975 -11.969 -26.766 1.00 49.79  ? 259 ASN   A CB  1 
ATOM   1755 C CG  . ASN   A 1 259 ? -36.075 -12.267 -27.762 1.00 53.99  ? 259 ASN   A CG  1 
ATOM   1756 O OD1 . ASN   A 1 259 ? -36.790 -13.257 -27.629 1.00 57.76  ? 259 ASN   A OD1 1 
ATOM   1757 N ND2 . ASN   A 1 259 ? -36.225 -11.404 -28.760 1.00 51.95  ? 259 ASN   A ND2 1 
ATOM   1758 N N   . LEU   A 1 260 ? -34.552 -14.847 -26.268 1.00 49.28  ? 260 LEU   A N   1 
ATOM   1759 C CA  . LEU   A 1 260 ? -34.690 -16.296 -26.207 1.00 52.11  ? 260 LEU   A CA  1 
ATOM   1760 C C   . LEU   A 1 260 ? -35.922 -16.826 -26.930 1.00 51.48  ? 260 LEU   A C   1 
ATOM   1761 O O   . LEU   A 1 260 ? -36.041 -18.044 -27.093 1.00 49.85  ? 260 LEU   A O   1 
ATOM   1762 C CB  . LEU   A 1 260 ? -34.735 -16.747 -24.744 1.00 51.84  ? 260 LEU   A CB  1 
ATOM   1763 C CG  . LEU   A 1 260 ? -33.404 -16.705 -23.996 1.00 47.72  ? 260 LEU   A CG  1 
ATOM   1764 C CD1 . LEU   A 1 260 ? -33.636 -16.744 -22.492 1.00 47.67  ? 260 LEU   A CD1 1 
ATOM   1765 C CD2 . LEU   A 1 260 ? -32.495 -17.845 -24.437 1.00 46.68  ? 260 LEU   A CD2 1 
ATOM   1766 N N   . SER   A 1 261 ? -36.832 -15.958 -27.366 1.00 51.69  ? 261 SER   A N   1 
ATOM   1767 C CA  . SER   A 1 261 ? -38.078 -16.412 -27.972 1.00 54.44  ? 261 SER   A CA  1 
ATOM   1768 C C   . SER   A 1 261 ? -37.834 -16.929 -29.383 1.00 50.74  ? 261 SER   A C   1 
ATOM   1769 O O   . SER   A 1 261 ? -37.079 -16.336 -30.157 1.00 49.88  ? 261 SER   A O   1 
ATOM   1770 C CB  . SER   A 1 261 ? -39.110 -15.282 -27.996 1.00 55.41  ? 261 SER   A CB  1 
ATOM   1771 O OG  . SER   A 1 261 ? -39.959 -15.384 -29.123 1.00 59.16  ? 261 SER   A OG  1 
ATOM   1772 N N   . GLY   A 1 262 ? -38.495 -18.037 -29.717 1.00 51.04  ? 262 GLY   A N   1 
ATOM   1773 C CA  . GLY   A 1 262 ? -38.252 -18.730 -30.961 1.00 53.70  ? 262 GLY   A CA  1 
ATOM   1774 C C   . GLY   A 1 262 ? -37.077 -19.681 -30.942 1.00 51.02  ? 262 GLY   A C   1 
ATOM   1775 O O   . GLY   A 1 262 ? -36.970 -20.527 -31.839 1.00 51.90  ? 262 GLY   A O   1 
ATOM   1776 N N   . LEU   A 1 263 ? -36.195 -19.574 -29.949 1.00 48.86  ? 263 LEU   A N   1 
ATOM   1777 C CA  . LEU   A 1 263 ? -35.053 -20.472 -29.851 1.00 50.83  ? 263 LEU   A CA  1 
ATOM   1778 C C   . LEU   A 1 263 ? -35.512 -21.917 -29.710 1.00 53.29  ? 263 LEU   A C   1 
ATOM   1779 O O   . LEU   A 1 263 ? -36.436 -22.225 -28.951 1.00 54.75  ? 263 LEU   A O   1 
ATOM   1780 C CB  . LEU   A 1 263 ? -34.178 -20.087 -28.658 1.00 51.13  ? 263 LEU   A CB  1 
ATOM   1781 C CG  . LEU   A 1 263 ? -32.668 -20.199 -28.850 1.00 48.12  ? 263 LEU   A CG  1 
ATOM   1782 C CD1 . LEU   A 1 263 ? -32.205 -19.247 -29.938 1.00 49.75  ? 263 LEU   A CD1 1 
ATOM   1783 C CD2 . LEU   A 1 263 ? -31.951 -19.922 -27.538 1.00 47.83  ? 263 LEU   A CD2 1 
ATOM   1784 N N   . ARG   A 1 264 ? -34.856 -22.805 -30.449 1.00 50.49  ? 264 ARG   A N   1 
ATOM   1785 C CA  . ARG   A 1 264 ? -35.158 -24.230 -30.435 1.00 48.88  ? 264 ARG   A CA  1 
ATOM   1786 C C   . ARG   A 1 264 ? -34.057 -24.948 -29.667 1.00 49.04  ? 264 ARG   A C   1 
ATOM   1787 O O   . ARG   A 1 264 ? -32.892 -24.922 -30.076 1.00 50.09  ? 264 ARG   A O   1 
ATOM   1788 C CB  . ARG   A 1 264 ? -35.280 -24.771 -31.859 1.00 48.76  ? 264 ARG   A CB  1 
ATOM   1789 C CG  . ARG   A 1 264 ? -36.416 -24.145 -32.661 1.00 52.16  ? 264 ARG   A CG  1 
ATOM   1790 C CD  . ARG   A 1 264 ? -36.148 -24.219 -34.163 1.00 51.22  ? 264 ARG   A CD  1 
ATOM   1791 N NE  . ARG   A 1 264 ? -34.742 -23.993 -34.479 1.00 54.41  ? 264 ARG   A NE  1 
ATOM   1792 C CZ  . ARG   A 1 264 ? -34.182 -24.253 -35.653 1.00 54.77  ? 264 ARG   A CZ  1 
ATOM   1793 N NH1 . ARG   A 1 264 ? -34.879 -24.770 -36.653 1.00 51.27  ? 264 ARG   A NH1 1 
ATOM   1794 N NH2 . ARG   A 1 264 ? -32.889 -23.992 -35.828 1.00 52.72  ? 264 ARG   A NH2 1 
ATOM   1795 N N   . ILE   A 1 265 ? -34.426 -25.579 -28.555 1.00 50.12  ? 265 ILE   A N   1 
ATOM   1796 C CA  . ILE   A 1 265 ? -33.474 -26.184 -27.632 1.00 46.69  ? 265 ILE   A CA  1 
ATOM   1797 C C   . ILE   A 1 265 ? -33.763 -27.674 -27.545 1.00 47.22  ? 265 ILE   A C   1 
ATOM   1798 O O   . ILE   A 1 265 ? -34.919 -28.078 -27.374 1.00 48.11  ? 265 ILE   A O   1 
ATOM   1799 C CB  . ILE   A 1 265 ? -33.552 -25.541 -26.235 1.00 47.70  ? 265 ILE   A CB  1 
ATOM   1800 C CG1 . ILE   A 1 265 ? -33.268 -24.039 -26.312 1.00 46.59  ? 265 ILE   A CG1 1 
ATOM   1801 C CG2 . ILE   A 1 265 ? -32.585 -26.222 -25.275 1.00 41.64  ? 265 ILE   A CG2 1 
ATOM   1802 C CD1 . ILE   A 1 265 ? -33.511 -23.306 -25.008 1.00 42.15  ? 265 ILE   A CD1 1 
ATOM   1803 N N   . LEU   A 1 266 ? -32.717 -28.487 -27.660 1.00 48.77  ? 266 LEU   A N   1 
ATOM   1804 C CA  . LEU   A 1 266 ? -32.797 -29.906 -27.348 1.00 47.08  ? 266 LEU   A CA  1 
ATOM   1805 C C   . LEU   A 1 266 ? -32.166 -30.124 -25.977 1.00 46.51  ? 266 LEU   A C   1 
ATOM   1806 O O   . LEU   A 1 266 ? -30.973 -29.865 -25.789 1.00 46.75  ? 266 LEU   A O   1 
ATOM   1807 C CB  . LEU   A 1 266 ? -32.104 -30.755 -28.413 1.00 43.90  ? 266 LEU   A CB  1 
ATOM   1808 C CG  . LEU   A 1 266 ? -32.000 -32.245 -28.074 1.00 45.83  ? 266 LEU   A CG  1 
ATOM   1809 C CD1 . LEU   A 1 266 ? -33.360 -32.911 -28.171 1.00 48.14  ? 266 LEU   A CD1 1 
ATOM   1810 C CD2 . LEU   A 1 266 ? -31.000 -32.941 -28.981 1.00 45.10  ? 266 LEU   A CD2 1 
ATOM   1811 N N   . LEU   A 1 267 ? -32.968 -30.581 -25.023 1.00 43.83  ? 267 LEU   A N   1 
ATOM   1812 C CA  . LEU   A 1 267 ? -32.528 -30.742 -23.644 1.00 44.06  ? 267 LEU   A CA  1 
ATOM   1813 C C   . LEU   A 1 267 ? -32.168 -32.202 -23.405 1.00 45.90  ? 267 LEU   A C   1 
ATOM   1814 O O   . LEU   A 1 267 ? -33.035 -33.079 -23.480 1.00 46.17  ? 267 LEU   A O   1 
ATOM   1815 C CB  . LEU   A 1 267 ? -33.618 -30.279 -22.678 1.00 43.23  ? 267 LEU   A CB  1 
ATOM   1816 C CG  . LEU   A 1 267 ? -33.563 -30.761 -21.229 1.00 46.49  ? 267 LEU   A CG  1 
ATOM   1817 C CD1 . LEU   A 1 267 ? -32.568 -29.936 -20.447 1.00 42.92  ? 267 LEU   A CD1 1 
ATOM   1818 C CD2 . LEU   A 1 267 ? -34.940 -30.674 -20.594 1.00 42.83  ? 267 LEU   A CD2 1 
ATOM   1819 N N   . LEU   A 1 268 ? -30.890 -32.463 -23.136 1.00 46.11  ? 268 LEU   A N   1 
ATOM   1820 C CA  . LEU   A 1 268 ? -30.403 -33.806 -22.833 1.00 46.93  ? 268 LEU   A CA  1 
ATOM   1821 C C   . LEU   A 1 268 ? -30.018 -33.868 -21.360 1.00 47.94  ? 268 LEU   A C   1 
ATOM   1822 O O   . LEU   A 1 268 ? -29.051 -33.226 -20.938 1.00 45.78  ? 268 LEU   A O   1 
ATOM   1823 C CB  . LEU   A 1 268 ? -29.217 -34.186 -23.719 1.00 43.26  ? 268 LEU   A CB  1 
ATOM   1824 C CG  . LEU   A 1 268 ? -29.330 -34.006 -25.234 1.00 48.11  ? 268 LEU   A CG  1 
ATOM   1825 C CD1 . LEU   A 1 268 ? -28.022 -34.412 -25.902 1.00 43.11  ? 268 LEU   A CD1 1 
ATOM   1826 C CD2 . LEU   A 1 268 ? -30.495 -34.810 -25.797 1.00 50.22  ? 268 LEU   A CD2 1 
ATOM   1827 N N   . THR   A 1 269 ? -30.772 -34.644 -20.581 1.00 47.71  ? 269 THR   A N   1 
ATOM   1828 C CA  . THR   A 1 269 ? -30.431 -34.919 -19.193 1.00 45.74  ? 269 THR   A CA  1 
ATOM   1829 C C   . THR   A 1 269 ? -29.997 -36.362 -18.979 1.00 48.12  ? 269 THR   A C   1 
ATOM   1830 O O   . THR   A 1 269 ? -29.724 -36.755 -17.839 1.00 48.47  ? 269 THR   A O   1 
ATOM   1831 C CB  . THR   A 1 269 ? -31.615 -34.594 -18.270 1.00 47.18  ? 269 THR   A CB  1 
ATOM   1832 O OG1 . THR   A 1 269 ? -32.832 -35.082 -18.846 1.00 51.36  ? 269 THR   A OG1 1 
ATOM   1833 C CG2 . THR   A 1 269 ? -31.731 -33.093 -18.071 1.00 43.06  ? 269 THR   A CG2 1 
ATOM   1834 N N   . ALA   A 1 270 ? -29.919 -37.156 -20.046 1.00 44.94  ? 270 ALA   A N   1 
ATOM   1835 C CA  . ALA   A 1 270 ? -29.525 -38.553 -19.962 1.00 45.84  ? 270 ALA   A CA  1 
ATOM   1836 C C   . ALA   A 1 270 ? -28.532 -38.857 -21.073 1.00 44.86  ? 270 ALA   A C   1 
ATOM   1837 O O   . ALA   A 1 270 ? -28.564 -38.242 -22.141 1.00 44.55  ? 270 ALA   A O   1 
ATOM   1838 C CB  . ALA   A 1 270 ? -30.737 -39.491 -20.063 1.00 40.40  ? 270 ALA   A CB  1 
ATOM   1839 N N   . HIS   A 1 271 ? -27.644 -39.813 -20.807 1.00 43.19  ? 271 HIS   A N   1 
ATOM   1840 C CA  . HIS   A 1 271 ? -26.646 -40.241 -21.770 1.00 45.38  ? 271 HIS   A CA  1 
ATOM   1841 C C   . HIS   A 1 271 ? -26.579 -41.761 -21.730 1.00 48.11  ? 271 HIS   A C   1 
ATOM   1842 O O   . HIS   A 1 271 ? -26.652 -42.354 -20.643 1.00 47.11  ? 271 HIS   A O   1 
ATOM   1843 C CB  . HIS   A 1 271 ? -25.266 -39.638 -21.469 1.00 45.63  ? 271 HIS   A CB  1 
ATOM   1844 C CG  . HIS   A 1 271 ? -24.291 -39.761 -22.599 1.00 45.55  ? 271 HIS   A CG  1 
ATOM   1845 N ND1 . HIS   A 1 271 ? -23.615 -40.930 -22.876 1.00 46.51  ? 271 HIS   A ND1 1 
ATOM   1846 C CD2 . HIS   A 1 271 ? -23.880 -38.861 -23.524 1.00 42.63  ? 271 HIS   A CD2 1 
ATOM   1847 C CE1 . HIS   A 1 271 ? -22.829 -40.745 -23.921 1.00 43.88  ? 271 HIS   A CE1 1 
ATOM   1848 N NE2 . HIS   A 1 271 ? -22.971 -39.498 -24.333 1.00 46.02  ? 271 HIS   A NE2 1 
ATOM   1849 N N   . PRO   A 1 272 ? -26.461 -42.419 -22.889 1.00 47.07  ? 272 PRO   A N   1 
ATOM   1850 C CA  . PRO   A 1 272 ? -26.459 -43.890 -22.894 1.00 47.18  ? 272 PRO   A CA  1 
ATOM   1851 C C   . PRO   A 1 272 ? -25.260 -44.516 -22.199 1.00 45.83  ? 272 PRO   A C   1 
ATOM   1852 O O   . PRO   A 1 272 ? -25.323 -45.703 -21.861 1.00 49.28  ? 272 PRO   A O   1 
ATOM   1853 C CB  . PRO   A 1 272 ? -26.471 -44.236 -24.391 1.00 49.22  ? 272 PRO   A CB  1 
ATOM   1854 C CG  . PRO   A 1 272 ? -25.918 -43.016 -25.063 1.00 48.62  ? 272 PRO   A CG  1 
ATOM   1855 C CD  . PRO   A 1 272 ? -26.454 -41.870 -24.255 1.00 44.70  ? 272 PRO   A CD  1 
ATOM   1856 N N   . GLU   A 1 273 ? -24.177 -43.772 -21.972 1.00 48.08  ? 273 GLU   A N   1 
ATOM   1857 C CA  . GLU   A 1 273 ? -22.964 -44.341 -21.399 1.00 46.53  ? 273 GLU   A CA  1 
ATOM   1858 C C   . GLU   A 1 273 ? -22.595 -43.777 -20.034 1.00 47.95  ? 273 GLU   A C   1 
ATOM   1859 O O   . GLU   A 1 273 ? -21.584 -44.205 -19.464 1.00 45.52  ? 273 GLU   A O   1 
ATOM   1860 C CB  . GLU   A 1 273 ? -21.779 -44.148 -22.354 1.00 43.28  ? 273 GLU   A CB  1 
ATOM   1861 C CG  . GLU   A 1 273 ? -21.989 -44.738 -23.737 1.00 48.71  ? 273 GLU   A CG  1 
ATOM   1862 C CD  . GLU   A 1 273 ? -22.402 -46.196 -23.689 1.00 52.01  ? 273 GLU   A CD  1 
ATOM   1863 O OE1 . GLU   A 1 273 ? -21.606 -47.030 -23.210 1.00 52.70  ? 273 GLU   A OE1 1 
ATOM   1864 O OE2 . GLU   A 1 273 ? -23.524 -46.508 -24.137 1.00 55.27  ? 273 GLU   A OE2 1 
ATOM   1865 N N   . THR   A 1 274 ? -23.366 -42.840 -19.491 1.00 44.56  ? 274 THR   A N   1 
ATOM   1866 C CA  . THR   A 1 274 ? -23.038 -42.248 -18.199 1.00 42.53  ? 274 THR   A CA  1 
ATOM   1867 C C   . THR   A 1 274 ? -24.324 -41.721 -17.568 1.00 44.43  ? 274 THR   A C   1 
ATOM   1868 O O   . THR   A 1 274 ? -25.424 -41.919 -18.095 1.00 46.61  ? 274 THR   A O   1 
ATOM   1869 C CB  . THR   A 1 274 ? -21.964 -41.163 -18.355 1.00 44.94  ? 274 THR   A CB  1 
ATOM   1870 O OG1 . THR   A 1 274 ? -21.712 -40.539 -17.090 1.00 47.14  ? 274 THR   A OG1 1 
ATOM   1871 C CG2 . THR   A 1 274 ? -22.398 -40.112 -19.364 1.00 43.79  ? 274 THR   A CG2 1 
ATOM   1872 N N   . VAL   A 1 275 ? -24.183 -41.043 -16.429 1.00 43.31  ? 275 VAL   A N   1 
ATOM   1873 C CA  . VAL   A 1 275 ? -25.318 -40.640 -15.610 1.00 41.90  ? 275 VAL   A CA  1 
ATOM   1874 C C   . VAL   A 1 275 ? -25.032 -39.263 -15.024 1.00 43.76  ? 275 VAL   A C   1 
ATOM   1875 O O   . VAL   A 1 275 ? -23.893 -38.790 -15.010 1.00 44.11  ? 275 VAL   A O   1 
ATOM   1876 C CB  . VAL   A 1 275 ? -25.595 -41.668 -14.486 1.00 42.33  ? 275 VAL   A CB  1 
ATOM   1877 C CG1 . VAL   A 1 275 ? -24.556 -41.539 -13.379 1.00 41.77  ? 275 VAL   A CG1 1 
ATOM   1878 C CG2 . VAL   A 1 275 ? -27.020 -41.540 -13.943 1.00 42.84  ? 275 VAL   A CG2 1 
ATOM   1879 N N   . ALA   A 1 276 ? -26.091 -38.616 -14.540 1.00 41.79  ? 276 ALA   A N   1 
ATOM   1880 C CA  . ALA   A 1 276 ? -25.996 -37.300 -13.932 1.00 43.81  ? 276 ALA   A CA  1 
ATOM   1881 C C   . ALA   A 1 276 ? -26.714 -37.290 -12.589 1.00 43.28  ? 276 ALA   A C   1 
ATOM   1882 O O   . ALA   A 1 276 ? -27.665 -38.044 -12.369 1.00 46.70  ? 276 ALA   A O   1 
ATOM   1883 C CB  . ALA   A 1 276 ? -26.587 -36.218 -14.851 1.00 42.07  ? 276 ALA   A CB  1 
ATOM   1884 N N   . ASP   A 1 277 ? -26.234 -36.429 -11.688 1.00 46.58  ? 277 ASP   A N   1 
ATOM   1885 C CA  . ASP   A 1 277 ? -26.885 -36.152 -10.411 1.00 49.54  ? 277 ASP   A CA  1 
ATOM   1886 C C   . ASP   A 1 277 ? -28.340 -35.745 -10.601 1.00 45.38  ? 277 ASP   A C   1 
ATOM   1887 O O   . ASP   A 1 277 ? -28.704 -35.215 -11.654 1.00 43.18  ? 277 ASP   A O   1 
ATOM   1888 C CB  . ASP   A 1 277 ? -26.147 -35.028 -9.674  1.00 45.89  ? 277 ASP   A CB  1 
ATOM   1889 C CG  . ASP   A 1 277 ? -25.289 -35.533 -8.541  1.00 55.24  ? 277 ASP   A CG  1 
ATOM   1890 O OD1 . ASP   A 1 277 ? -25.469 -36.699 -8.137  1.00 59.60  ? 277 ASP   A OD1 1 
ATOM   1891 O OD2 . ASP   A 1 277 ? -24.432 -34.760 -8.053  1.00 55.69  ? 277 ASP   A OD2 1 
ATOM   1892 N N   . SER   A 1 278 ? -29.178 -35.954 -9.586  1.00 45.31  ? 278 SER   A N   1 
ATOM   1893 C CA  . SER   A 1 278 ? -30.522 -35.388 -9.642  1.00 46.66  ? 278 SER   A CA  1 
ATOM   1894 C C   . SER   A 1 278 ? -30.506 -33.882 -9.416  1.00 45.37  ? 278 SER   A C   1 
ATOM   1895 O O   . SER   A 1 278 ? -31.362 -33.170 -9.952  1.00 43.84  ? 278 SER   A O   1 
ATOM   1896 C CB  . SER   A 1 278 ? -31.431 -36.071 -8.623  1.00 45.45  ? 278 SER   A CB  1 
ATOM   1897 O OG  . SER   A 1 278 ? -30.822 -36.110 -7.347  1.00 51.62  ? 278 SER   A OG  1 
ATOM   1898 N N   . ALA   A 1 279 ? -29.547 -33.383 -8.632  1.00 45.63  ? 279 ALA   A N   1 
ATOM   1899 C CA  . ALA   A 1 279 ? -29.345 -31.941 -8.542  1.00 43.02  ? 279 ALA   A CA  1 
ATOM   1900 C C   . ALA   A 1 279 ? -28.869 -31.378 -9.872  1.00 43.11  ? 279 ALA   A C   1 
ATOM   1901 O O   . ALA   A 1 279 ? -29.307 -30.301 -10.294 1.00 43.38  ? 279 ALA   A O   1 
ATOM   1902 C CB  . ALA   A 1 279 ? -28.341 -31.613 -7.437  1.00 41.98  ? 279 ALA   A CB  1 
ATOM   1903 N N   . THR   A 1 280 ? -27.963 -32.095 -10.542 1.00 42.98  ? 280 THR   A N   1 
ATOM   1904 C CA  . THR   A 1 280 ? -27.520 -31.685 -11.870 1.00 39.57  ? 280 THR   A CA  1 
ATOM   1905 C C   . THR   A 1 280 ? -28.672 -31.722 -12.865 1.00 42.01  ? 280 THR   A C   1 
ATOM   1906 O O   . THR   A 1 280 ? -28.825 -30.806 -13.682 1.00 39.50  ? 280 THR   A O   1 
ATOM   1907 C CB  . THR   A 1 280 ? -26.378 -32.587 -12.341 1.00 40.85  ? 280 THR   A CB  1 
ATOM   1908 O OG1 . THR   A 1 280 ? -25.270 -32.461 -11.443 1.00 41.56  ? 280 THR   A OG1 1 
ATOM   1909 C CG2 . THR   A 1 280 ? -25.929 -32.202 -13.748 1.00 39.46  ? 280 THR   A CG2 1 
ATOM   1910 N N   . ILE   A 1 281 ? -29.500 -32.766 -12.805 1.00 44.35  ? 281 ILE   A N   1 
ATOM   1911 C CA  . ILE   A 1 281 ? -30.623 -32.855 -13.729 1.00 43.67  ? 281 ILE   A CA  1 
ATOM   1912 C C   . ILE   A 1 281 ? -31.605 -31.717 -13.479 1.00 45.15  ? 281 ILE   A C   1 
ATOM   1913 O O   . ILE   A 1 281 ? -31.986 -31.004 -14.412 1.00 47.20  ? 281 ILE   A O   1 
ATOM   1914 C CB  . ILE   A 1 281 ? -31.289 -34.241 -13.636 1.00 43.32  ? 281 ILE   A CB  1 
ATOM   1915 C CG1 . ILE   A 1 281 ? -30.427 -35.276 -14.362 1.00 45.70  ? 281 ILE   A CG1 1 
ATOM   1916 C CG2 . ILE   A 1 281 ? -32.664 -34.228 -14.256 1.00 44.94  ? 281 ILE   A CG2 1 
ATOM   1917 C CD1 . ILE   A 1 281 ? -30.641 -36.705 -13.905 1.00 45.00  ? 281 ILE   A CD1 1 
ATOM   1918 N N   . SER   A 1 282 ? -31.987 -31.491 -12.218 1.00 44.69  ? 282 SER   A N   1 
ATOM   1919 C CA  . SER   A 1 282 ? -32.920 -30.407 -11.907 1.00 44.25  ? 282 SER   A CA  1 
ATOM   1920 C C   . SER   A 1 282 ? -32.381 -29.051 -12.351 1.00 42.04  ? 282 SER   A C   1 
ATOM   1921 O O   . SER   A 1 282 ? -33.130 -28.221 -12.880 1.00 43.67  ? 282 SER   A O   1 
ATOM   1922 C CB  . SER   A 1 282 ? -33.232 -30.386 -10.410 1.00 42.14  ? 282 SER   A CB  1 
ATOM   1923 O OG  . SER   A 1 282 ? -33.695 -31.647 -9.969  1.00 47.08  ? 282 SER   A OG  1 
ATOM   1924 N N   . ALA   A 1 283 ? -31.085 -28.807 -12.143 1.00 40.09  ? 283 ALA   A N   1 
ATOM   1925 C CA  . ALA   A 1 283 ? -30.490 -27.542 -12.564 1.00 42.09  ? 283 ALA   A CA  1 
ATOM   1926 C C   . ALA   A 1 283 ? -30.626 -27.342 -14.071 1.00 44.66  ? 283 ALA   A C   1 
ATOM   1927 O O   . ALA   A 1 283 ? -31.017 -26.263 -14.533 1.00 42.67  ? 283 ALA   A O   1 
ATOM   1928 C CB  . ALA   A 1 283 ? -29.020 -27.490 -12.143 1.00 40.64  ? 283 ALA   A CB  1 
ATOM   1929 N N   . VAL   A 1 284 ? -30.320 -28.380 -14.855 1.00 42.06  ? 284 VAL   A N   1 
ATOM   1930 C CA  . VAL   A 1 284 ? -30.386 -28.253 -16.308 1.00 44.61  ? 284 VAL   A CA  1 
ATOM   1931 C C   . VAL   A 1 284 ? -31.831 -28.083 -16.778 1.00 43.97  ? 284 VAL   A C   1 
ATOM   1932 O O   . VAL   A 1 284 ? -32.104 -27.293 -17.689 1.00 44.14  ? 284 VAL   A O   1 
ATOM   1933 C CB  . VAL   A 1 284 ? -29.692 -29.451 -16.985 1.00 42.09  ? 284 VAL   A CB  1 
ATOM   1934 C CG1 . VAL   A 1 284 ? -29.708 -29.289 -18.491 1.00 43.99  ? 284 VAL   A CG1 1 
ATOM   1935 C CG2 . VAL   A 1 284 ? -28.252 -29.559 -16.509 1.00 39.13  ? 284 VAL   A CG2 1 
ATOM   1936 N N   . GLU   A 1 285 ? -32.781 -28.801 -16.165 1.00 44.34  ? 285 GLU   A N   1 
ATOM   1937 C CA  . GLU   A 1 285 ? -34.189 -28.600 -16.518 1.00 46.13  ? 285 GLU   A CA  1 
ATOM   1938 C C   . GLU   A 1 285 ? -34.656 -27.191 -16.161 1.00 48.29  ? 285 GLU   A C   1 
ATOM   1939 O O   . GLU   A 1 285 ? -35.438 -26.582 -16.904 1.00 45.56  ? 285 GLU   A O   1 
ATOM   1940 C CB  . GLU   A 1 285 ? -35.077 -29.642 -15.831 1.00 43.96  ? 285 GLU   A CB  1 
ATOM   1941 C CG  . GLU   A 1 285 ? -34.534 -31.063 -15.842 1.00 49.85  ? 285 GLU   A CG  1 
ATOM   1942 C CD  . GLU   A 1 285 ? -35.376 -32.028 -15.020 1.00 51.92  ? 285 GLU   A CD  1 
ATOM   1943 O OE1 . GLU   A 1 285 ? -35.753 -33.106 -15.534 1.00 51.73  ? 285 GLU   A OE1 1 
ATOM   1944 O OE2 . GLU   A 1 285 ? -35.659 -31.701 -13.850 1.00 53.95  ? 285 GLU   A OE2 1 
ATOM   1945 N N   . ARG   A 1 286 ? -34.195 -26.657 -15.025 1.00 47.23  ? 286 ARG   A N   1 
ATOM   1946 C CA  . ARG   A 1 286 ? -34.570 -25.297 -14.649 1.00 44.06  ? 286 ARG   A CA  1 
ATOM   1947 C C   . ARG   A 1 286 ? -34.083 -24.286 -15.678 1.00 45.74  ? 286 ARG   A C   1 
ATOM   1948 O O   . ARG   A 1 286 ? -34.773 -23.297 -15.953 1.00 47.63  ? 286 ARG   A O   1 
ATOM   1949 C CB  . ARG   A 1 286 ? -34.025 -24.959 -13.261 1.00 43.14  ? 286 ARG   A CB  1 
ATOM   1950 C CG  . ARG   A 1 286 ? -33.959 -23.467 -12.967 1.00 47.33  ? 286 ARG   A CG  1 
ATOM   1951 C CD  . ARG   A 1 286 ? -33.771 -23.196 -11.485 1.00 47.39  ? 286 ARG   A CD  1 
ATOM   1952 N NE  . ARG   A 1 286 ? -32.781 -24.084 -10.889 1.00 48.95  ? 286 ARG   A NE  1 
ATOM   1953 C CZ  . ARG   A 1 286 ? -31.534 -23.732 -10.608 1.00 52.14  ? 286 ARG   A CZ  1 
ATOM   1954 N NH1 . ARG   A 1 286 ? -31.088 -22.509 -10.850 1.00 45.36  ? 286 ARG   A NH1 1 
ATOM   1955 N NH2 . ARG   A 1 286 ? -30.712 -24.631 -10.073 1.00 52.23  ? 286 ARG   A NH2 1 
ATOM   1956 N N   . ALA   A 1 287 ? -32.912 -24.525 -16.273 1.00 43.25  ? 287 ALA   A N   1 
ATOM   1957 C CA  . ALA   A 1 287 ? -32.440 -23.651 -17.341 1.00 43.89  ? 287 ALA   A CA  1 
ATOM   1958 C C   . ALA   A 1 287 ? -33.330 -23.758 -18.575 1.00 42.91  ? 287 ALA   A C   1 
ATOM   1959 O O   . ALA   A 1 287 ? -33.652 -22.744 -19.202 1.00 47.54  ? 287 ALA   A O   1 
ATOM   1960 C CB  . ALA   A 1 287 ? -30.988 -23.978 -17.687 1.00 42.82  ? 287 ALA   A CB  1 
ATOM   1961 N N   . ALA   A 1 288 ? -33.743 -24.976 -18.935 1.00 41.90  ? 288 ALA   A N   1 
ATOM   1962 C CA  . ALA   A 1 288 ? -34.646 -25.141 -20.071 1.00 44.16  ? 288 ALA   A CA  1 
ATOM   1963 C C   . ALA   A 1 288 ? -36.019 -24.555 -19.773 1.00 49.19  ? 288 ALA   A C   1 
ATOM   1964 O O   . ALA   A 1 288 ? -36.651 -23.957 -20.653 1.00 49.53  ? 288 ALA   A O   1 
ATOM   1965 C CB  . ALA   A 1 288 ? -34.765 -26.619 -20.441 1.00 43.75  ? 288 ALA   A CB  1 
ATOM   1966 N N   . ALA   A 1 289 ? -36.496 -24.716 -18.536 1.00 47.30  ? 289 ALA   A N   1 
ATOM   1967 C CA  . ALA   A 1 289 ? -37.785 -24.147 -18.159 1.00 47.42  ? 289 ALA   A CA  1 
ATOM   1968 C C   . ALA   A 1 289 ? -37.755 -22.624 -18.215 1.00 49.70  ? 289 ALA   A C   1 
ATOM   1969 O O   . ALA   A 1 289 ? -38.708 -21.995 -18.689 1.00 52.20  ? 289 ALA   A O   1 
ATOM   1970 C CB  . ALA   A 1 289 ? -38.182 -24.630 -16.764 1.00 47.15  ? 289 ALA   A CB  1 
ATOM   1971 N N   . ALA   A 1 290 ? -36.665 -22.013 -17.743 1.00 46.62  ? 290 ALA   A N   1 
ATOM   1972 C CA  . ALA   A 1 290 ? -36.577 -20.556 -17.754 1.00 47.00  ? 290 ALA   A CA  1 
ATOM   1973 C C   . ALA   A 1 290 ? -36.559 -20.004 -19.172 1.00 50.61  ? 290 ALA   A C   1 
ATOM   1974 O O   . ALA   A 1 290 ? -37.090 -18.915 -19.420 1.00 53.64  ? 290 ALA   A O   1 
ATOM   1975 C CB  . ALA   A 1 290 ? -35.338 -20.098 -16.986 1.00 48.47  ? 290 ALA   A CB  1 
ATOM   1976 N N   . CYS   A 1 291 ? -35.959 -20.734 -20.114 1.00 51.33  ? 291 CYS   A N   1 
ATOM   1977 C CA  . CYS   A 1 291 ? -35.980 -20.308 -21.509 1.00 51.09  ? 291 CYS   A CA  1 
ATOM   1978 C C   . CYS   A 1 291 ? -37.340 -20.562 -22.146 1.00 52.26  ? 291 CYS   A C   1 
ATOM   1979 O O   . CYS   A 1 291 ? -37.807 -19.753 -22.955 1.00 53.47  ? 291 CYS   A O   1 
ATOM   1980 C CB  . CYS   A 1 291 ? -34.880 -21.017 -22.296 1.00 48.65  ? 291 CYS   A CB  1 
ATOM   1981 S SG  . CYS   A 1 291 ? -33.212 -20.683 -21.687 1.00 48.57  ? 291 CYS   A SG  1 
ATOM   1982 N N   . GLU   A 1 292 ? -37.979 -21.683 -21.797 1.00 52.18  ? 292 GLU   A N   1 
ATOM   1983 C CA  . GLU   A 1 292 ? -39.346 -21.937 -22.244 1.00 53.10  ? 292 GLU   A CA  1 
ATOM   1984 C C   . GLU   A 1 292 ? -40.275 -20.800 -21.842 1.00 54.63  ? 292 GLU   A C   1 
ATOM   1985 O O   . GLU   A 1 292 ? -41.105 -20.350 -22.640 1.00 53.48  ? 292 GLU   A O   1 
ATOM   1986 C CB  . GLU   A 1 292 ? -39.851 -23.260 -21.669 1.00 53.09  ? 292 GLU   A CB  1 
ATOM   1987 C CG  . GLU   A 1 292 ? -40.076 -24.346 -22.702 1.00 56.19  ? 292 GLU   A CG  1 
ATOM   1988 C CD  . GLU   A 1 292 ? -40.997 -25.441 -22.196 1.00 62.85  ? 292 GLU   A CD  1 
ATOM   1989 O OE1 . GLU   A 1 292 ? -41.118 -25.594 -20.959 1.00 63.50  ? 292 GLU   A OE1 1 
ATOM   1990 O OE2 . GLU   A 1 292 ? -41.596 -26.149 -23.034 1.00 64.86  ? 292 GLU   A OE2 1 
ATOM   1991 N N   . ALA   A 1 293 ? -40.146 -20.322 -20.602 1.00 52.57  ? 293 ALA   A N   1 
ATOM   1992 C CA  . ALA   A 1 293 ? -40.912 -19.168 -20.151 1.00 53.84  ? 293 ALA   A CA  1 
ATOM   1993 C C   . ALA   A 1 293 ? -40.524 -17.891 -20.883 1.00 54.61  ? 293 ALA   A C   1 
ATOM   1994 O O   . ALA   A 1 293 ? -41.294 -16.924 -20.862 1.00 55.83  ? 293 ALA   A O   1 
ATOM   1995 C CB  . ALA   A 1 293 ? -40.729 -18.977 -18.646 1.00 54.70  ? 293 ALA   A CB  1 
ATOM   1996 N N   . SER   A 1 294 ? -39.353 -17.860 -21.521 1.00 54.31  ? 294 SER   A N   1 
ATOM   1997 C CA  . SER   A 1 294 ? -38.902 -16.699 -22.278 1.00 54.42  ? 294 SER   A CA  1 
ATOM   1998 C C   . SER   A 1 294 ? -39.167 -16.844 -23.770 1.00 56.20  ? 294 SER   A C   1 
ATOM   1999 O O   . SER   A 1 294 ? -38.582 -16.106 -24.571 1.00 56.79  ? 294 SER   A O   1 
ATOM   2000 C CB  . SER   A 1 294 ? -37.414 -16.443 -22.032 1.00 54.02  ? 294 SER   A CB  1 
ATOM   2001 O OG  . SER   A 1 294 ? -37.121 -16.427 -20.646 1.00 58.80  ? 294 SER   A OG  1 
ATOM   2002 N N   . GLY   A 1 295 ? -40.032 -17.779 -24.156 1.00 53.80  ? 295 GLY   A N   1 
ATOM   2003 C CA  . GLY   A 1 295 ? -40.441 -17.932 -25.536 1.00 54.29  ? 295 GLY   A CA  1 
ATOM   2004 C C   . GLY   A 1 295 ? -39.702 -18.990 -26.327 1.00 55.78  ? 295 GLY   A C   1 
ATOM   2005 O O   . GLY   A 1 295 ? -40.020 -19.187 -27.508 1.00 56.20  ? 295 GLY   A O   1 
ATOM   2006 N N   . ALA   A 1 296 ? -38.724 -19.664 -25.731 1.00 52.75  ? 296 ALA   A N   1 
ATOM   2007 C CA  . ALA   A 1 296 ? -38.040 -20.734 -26.436 1.00 53.83  ? 296 ALA   A CA  1 
ATOM   2008 C C   . ALA   A 1 296 ? -38.907 -21.988 -26.462 1.00 51.63  ? 296 ALA   A C   1 
ATOM   2009 O O   . ALA   A 1 296 ? -39.830 -22.154 -25.661 1.00 55.84  ? 296 ALA   A O   1 
ATOM   2010 C CB  . ALA   A 1 296 ? -36.691 -21.045 -25.785 1.00 52.62  ? 296 ALA   A CB  1 
ATOM   2011 N N   . THR   A 1 297 ? -38.607 -22.871 -27.408 1.00 51.80  ? 297 THR   A N   1 
ATOM   2012 C CA  . THR   A 1 297 ? -39.209 -24.195 -27.457 1.00 55.80  ? 297 THR   A CA  1 
ATOM   2013 C C   . THR   A 1 297 ? -38.174 -25.221 -27.022 1.00 52.96  ? 297 THR   A C   1 
ATOM   2014 O O   . THR   A 1 297 ? -37.017 -25.169 -27.451 1.00 53.77  ? 297 THR   A O   1 
ATOM   2015 C CB  . THR   A 1 297 ? -39.729 -24.535 -28.858 1.00 53.32  ? 297 THR   A CB  1 
ATOM   2016 O OG1 . THR   A 1 297 ? -38.623 -24.769 -29.741 1.00 57.88  ? 297 THR   A OG1 1 
ATOM   2017 C CG2 . THR   A 1 297 ? -40.581 -23.404 -29.401 1.00 51.48  ? 297 THR   A CG2 1 
ATOM   2018 N N   . VAL   A 1 298 ? -38.583 -26.137 -26.152 1.00 48.73  ? 298 VAL   A N   1 
ATOM   2019 C CA  . VAL   A 1 298 ? -37.688 -27.144 -25.599 1.00 50.26  ? 298 VAL   A CA  1 
ATOM   2020 C C   . VAL   A 1 298 ? -38.215 -28.518 -25.983 1.00 52.45  ? 298 VAL   A C   1 
ATOM   2021 O O   . VAL   A 1 298 ? -39.331 -28.893 -25.599 1.00 51.85  ? 298 VAL   A O   1 
ATOM   2022 C CB  . VAL   A 1 298 ? -37.552 -27.016 -24.074 1.00 47.17  ? 298 VAL   A CB  1 
ATOM   2023 C CG1 . VAL   A 1 298 ? -36.746 -28.177 -23.523 1.00 47.40  ? 298 VAL   A CG1 1 
ATOM   2024 C CG2 . VAL   A 1 298 ? -36.893 -25.694 -23.711 1.00 47.58  ? 298 VAL   A CG2 1 
ATOM   2025 N N   . ALA   A 1 299 ? -37.423 -29.259 -26.748 1.00 49.41  ? 299 ALA   A N   1 
ATOM   2026 C CA  . ALA   A 1 299 ? -37.680 -30.666 -27.005 1.00 50.16  ? 299 ALA   A CA  1 
ATOM   2027 C C   . ALA   A 1 299 ? -36.750 -31.514 -26.147 1.00 50.28  ? 299 ALA   A C   1 
ATOM   2028 O O   . ALA   A 1 299 ? -35.671 -31.075 -25.740 1.00 50.77  ? 299 ALA   A O   1 
ATOM   2029 C CB  . ALA   A 1 299 ? -37.491 -31.000 -28.486 1.00 47.97  ? 299 ALA   A CB  1 
ATOM   2030 N N   . THR   A 1 300 ? -37.187 -32.743 -25.872 1.00 50.42  ? 300 THR   A N   1 
ATOM   2031 C CA  . THR   A 1 300 ? -36.445 -33.662 -25.018 1.00 52.38  ? 300 THR   A CA  1 
ATOM   2032 C C   . THR   A 1 300 ? -35.996 -34.915 -25.757 1.00 53.52  ? 300 THR   A C   1 
ATOM   2033 O O   . THR   A 1 300 ? -35.425 -35.818 -25.136 1.00 55.92  ? 300 THR   A O   1 
ATOM   2034 C CB  . THR   A 1 300 ? -37.284 -34.041 -23.793 1.00 49.27  ? 300 THR   A CB  1 
ATOM   2035 O OG1 . THR   A 1 300 ? -38.537 -34.588 -24.216 1.00 50.41  ? 300 THR   A OG1 1 
ATOM   2036 C CG2 . THR   A 1 300 ? -37.546 -32.809 -22.934 1.00 48.58  ? 300 THR   A CG2 1 
ATOM   2037 N N   . SER   A 1 301 ? -36.243 -34.995 -27.060 1.00 51.16  ? 301 SER   A N   1 
ATOM   2038 C CA  . SER   A 1 301 ? -35.738 -36.083 -27.883 1.00 53.21  ? 301 SER   A CA  1 
ATOM   2039 C C   . SER   A 1 301 ? -35.770 -35.621 -29.331 1.00 50.69  ? 301 SER   A C   1 
ATOM   2040 O O   . SER   A 1 301 ? -36.369 -34.596 -29.662 1.00 51.51  ? 301 SER   A O   1 
ATOM   2041 C CB  . SER   A 1 301 ? -36.551 -37.366 -27.692 1.00 56.84  ? 301 SER   A CB  1 
ATOM   2042 O OG  . SER   A 1 301 ? -37.778 -37.301 -28.397 1.00 59.87  ? 301 SER   A OG  1 
ATOM   2043 N N   . SER   A 1 302 ? -35.122 -36.393 -30.193 1.00 52.67  ? 302 SER   A N   1 
ATOM   2044 C CA  . SER   A 1 302 ? -35.062 -36.051 -31.607 1.00 52.28  ? 302 SER   A CA  1 
ATOM   2045 C C   . SER   A 1 302 ? -34.590 -37.244 -32.424 1.00 50.20  ? 302 SER   A C   1 
ATOM   2046 O O   . SER   A 1 302 ? -33.615 -37.907 -32.047 1.00 50.52  ? 302 SER   A O   1 
ATOM   2047 C CB  . SER   A 1 302 ? -34.133 -34.859 -31.842 1.00 50.26  ? 302 SER   A CB  1 
ATOM   2048 O OG  . SER   A 1 302 ? -33.921 -34.645 -33.228 1.00 52.45  ? 302 SER   A OG  1 
ATOM   2049 N N   . PRO   A 1 303 ? -35.248 -37.552 -33.543 1.00 49.86  ? 303 PRO   A N   1 
ATOM   2050 C CA  . PRO   A 1 303 ? -34.737 -38.617 -34.417 1.00 47.27  ? 303 PRO   A CA  1 
ATOM   2051 C C   . PRO   A 1 303 ? -33.398 -38.277 -35.039 1.00 49.28  ? 303 PRO   A C   1 
ATOM   2052 O O   . PRO   A 1 303 ? -32.679 -39.189 -35.470 1.00 48.08  ? 303 PRO   A O   1 
ATOM   2053 C CB  . PRO   A 1 303 ? -35.836 -38.760 -35.478 1.00 49.50  ? 303 PRO   A CB  1 
ATOM   2054 C CG  . PRO   A 1 303 ? -36.507 -37.422 -35.503 1.00 49.08  ? 303 PRO   A CG  1 
ATOM   2055 C CD  . PRO   A 1 303 ? -36.465 -36.922 -34.086 1.00 48.61  ? 303 PRO   A CD  1 
ATOM   2056 N N   . ASP   A 1 304 ? -33.034 -36.994 -35.078 1.00 48.63  ? 304 ASP   A N   1 
ATOM   2057 C CA  . ASP   A 1 304 ? -31.810 -36.526 -35.711 1.00 51.39  ? 304 ASP   A CA  1 
ATOM   2058 C C   . ASP   A 1 304 ? -30.593 -36.593 -34.799 1.00 50.99  ? 304 ASP   A C   1 
ATOM   2059 O O   . ASP   A 1 304 ? -29.464 -36.492 -35.294 1.00 51.81  ? 304 ASP   A O   1 
ATOM   2060 C CB  . ASP   A 1 304 ? -31.994 -35.083 -36.190 1.00 52.32  ? 304 ASP   A CB  1 
ATOM   2061 C CG  . ASP   A 1 304 ? -32.657 -35.003 -37.545 1.00 57.42  ? 304 ASP   A CG  1 
ATOM   2062 O OD1 . ASP   A 1 304 ? -32.654 -36.026 -38.262 1.00 56.30  ? 304 ASP   A OD1 1 
ATOM   2063 O OD2 . ASP   A 1 304 ? -33.184 -33.920 -37.892 1.00 61.93  ? 304 ASP   A OD2 1 
ATOM   2064 N N   . LEU   A 1 305 ? -30.785 -36.755 -33.497 1.00 49.26  ? 305 LEU   A N   1 
ATOM   2065 C CA  . LEU   A 1 305 ? -29.656 -36.797 -32.580 1.00 50.02  ? 305 LEU   A CA  1 
ATOM   2066 C C   . LEU   A 1 305 ? -28.775 -37.998 -32.904 1.00 47.24  ? 305 LEU   A C   1 
ATOM   2067 O O   . LEU   A 1 305 ? -29.276 -39.133 -32.934 1.00 45.98  ? 305 LEU   A O   1 
ATOM   2068 C CB  . LEU   A 1 305 ? -30.138 -36.865 -31.131 1.00 47.95  ? 305 LEU   A CB  1 
ATOM   2069 C CG  . LEU   A 1 305 ? -29.075 -37.196 -30.086 1.00 48.13  ? 305 LEU   A CG  1 
ATOM   2070 C CD1 . LEU   A 1 305 ? -28.348 -35.933 -29.668 1.00 44.55  ? 305 LEU   A CD1 1 
ATOM   2071 C CD2 . LEU   A 1 305 ? -29.703 -37.876 -28.878 1.00 50.00  ? 305 LEU   A CD2 1 
ATOM   2072 N N   . PRO   A 1 306 ? -27.480 -37.804 -33.155 1.00 44.40  ? 306 PRO   A N   1 
ATOM   2073 C CA  . PRO   A 1 306 ? -26.605 -38.935 -33.491 1.00 42.11  ? 306 PRO   A CA  1 
ATOM   2074 C C   . PRO   A 1 306 ? -26.544 -39.946 -32.356 1.00 45.39  ? 306 PRO   A C   1 
ATOM   2075 O O   . PRO   A 1 306 ? -26.994 -39.702 -31.234 1.00 46.78  ? 306 PRO   A O   1 
ATOM   2076 C CB  . PRO   A 1 306 ? -25.242 -38.269 -33.730 1.00 41.80  ? 306 PRO   A CB  1 
ATOM   2077 C CG  . PRO   A 1 306 ? -25.560 -36.824 -33.988 1.00 45.56  ? 306 PRO   A CG  1 
ATOM   2078 C CD  . PRO   A 1 306 ? -26.734 -36.536 -33.107 1.00 44.67  ? 306 PRO   A CD  1 
ATOM   2079 N N   . ASP   A 1 307 ? -25.978 -41.109 -32.661 1.00 47.13  ? 307 ASP   A N   1 
ATOM   2080 C CA  . ASP   A 1 307 ? -25.884 -42.176 -31.668 1.00 49.28  ? 307 ASP   A CA  1 
ATOM   2081 C C   . ASP   A 1 307 ? -24.783 -41.797 -30.686 1.00 46.90  ? 307 ASP   A C   1 
ATOM   2082 O O   . ASP   A 1 307 ? -23.598 -42.013 -30.948 1.00 49.08  ? 307 ASP   A O   1 
ATOM   2083 C CB  . ASP   A 1 307 ? -25.624 -43.523 -32.337 1.00 50.45  ? 307 ASP   A CB  1 
ATOM   2084 C CG  . ASP   A 1 307 ? -25.442 -44.650 -31.333 1.00 54.17  ? 307 ASP   A CG  1 
ATOM   2085 O OD1 . ASP   A 1 307 ? -25.956 -44.537 -30.199 1.00 51.90  ? 307 ASP   A OD1 1 
ATOM   2086 O OD2 . ASP   A 1 307 ? -24.816 -45.671 -31.690 1.00 56.56  ? 307 ASP   A OD2 1 
ATOM   2087 N N   . LEU   A 1 308 ? -25.183 -41.219 -29.546 1.00 47.91  ? 308 LEU   A N   1 
ATOM   2088 C CA  . LEU   A 1 308 ? -24.217 -40.744 -28.559 1.00 46.97  ? 308 LEU   A CA  1 
ATOM   2089 C C   . LEU   A 1 308 ? -23.352 -41.878 -28.026 1.00 45.79  ? 308 LEU   A C   1 
ATOM   2090 O O   . LEU   A 1 308 ? -22.220 -41.643 -27.587 1.00 46.79  ? 308 LEU   A O   1 
ATOM   2091 C CB  . LEU   A 1 308 ? -24.950 -40.044 -27.412 1.00 45.22  ? 308 LEU   A CB  1 
ATOM   2092 C CG  . LEU   A 1 308 ? -25.915 -38.921 -27.808 1.00 46.58  ? 308 LEU   A CG  1 
ATOM   2093 C CD1 . LEU   A 1 308 ? -26.484 -38.215 -26.583 1.00 41.55  ? 308 LEU   A CD1 1 
ATOM   2094 C CD2 . LEU   A 1 308 ? -25.214 -37.924 -28.718 1.00 44.12  ? 308 LEU   A CD2 1 
ATOM   2095 N N   . SER   A 1 309 ? -23.861 -43.109 -28.061 1.00 46.01  ? 309 SER   A N   1 
ATOM   2096 C CA  . SER   A 1 309 ? -23.071 -44.245 -27.602 1.00 46.69  ? 309 SER   A CA  1 
ATOM   2097 C C   . SER   A 1 309 ? -21.957 -44.578 -28.589 1.00 45.91  ? 309 SER   A C   1 
ATOM   2098 O O   . SER   A 1 309 ? -20.814 -44.819 -28.184 1.00 46.95  ? 309 SER   A O   1 
ATOM   2099 C CB  . SER   A 1 309 ? -23.978 -45.450 -27.371 1.00 48.29  ? 309 SER   A CB  1 
ATOM   2100 O OG  . SER   A 1 309 ? -23.217 -46.620 -27.151 1.00 51.40  ? 309 SER   A OG  1 
ATOM   2101 N N   . ALA   A 1 310 ? -22.265 -44.595 -29.890 1.00 46.51  ? 310 ALA   A N   1 
ATOM   2102 C CA  . ALA   A 1 310 ? -21.220 -44.811 -30.887 1.00 49.44  ? 310 ALA   A CA  1 
ATOM   2103 C C   . ALA   A 1 310 ? -20.248 -43.643 -30.932 1.00 48.36  ? 310 ALA   A C   1 
ATOM   2104 O O   . ALA   A 1 310 ? -19.070 -43.828 -31.263 1.00 45.20  ? 310 ALA   A O   1 
ATOM   2105 C CB  . ALA   A 1 310 ? -21.834 -45.030 -32.267 1.00 46.94  ? 310 ALA   A CB  1 
ATOM   2106 N N   . LEU   A 1 311 ? -20.722 -42.442 -30.597 1.00 46.81  ? 311 LEU   A N   1 
ATOM   2107 C CA  . LEU   A 1 311 ? -19.868 -41.261 -30.620 1.00 44.72  ? 311 LEU   A CA  1 
ATOM   2108 C C   . LEU   A 1 311 ? -18.706 -41.405 -29.644 1.00 44.26  ? 311 LEU   A C   1 
ATOM   2109 O O   . LEU   A 1 311 ? -17.540 -41.237 -30.021 1.00 44.50  ? 311 LEU   A O   1 
ATOM   2110 C CB  . LEU   A 1 311 ? -20.702 -40.021 -30.295 1.00 44.37  ? 311 LEU   A CB  1 
ATOM   2111 C CG  . LEU   A 1 311 ? -20.077 -38.640 -30.500 1.00 41.59  ? 311 LEU   A CG  1 
ATOM   2112 C CD1 . LEU   A 1 311 ? -21.165 -37.644 -30.807 1.00 43.25  ? 311 LEU   A CD1 1 
ATOM   2113 C CD2 . LEU   A 1 311 ? -19.295 -38.187 -29.285 1.00 43.91  ? 311 LEU   A CD2 1 
ATOM   2114 N N   . VAL   A 1 312 ? -19.005 -41.719 -28.380 1.00 43.05  ? 312 VAL   A N   1 
ATOM   2115 C CA  . VAL   A 1 312 ? -17.959 -41.735 -27.361 1.00 45.60  ? 312 VAL   A CA  1 
ATOM   2116 C C   . VAL   A 1 312 ? -17.003 -42.905 -27.576 1.00 45.82  ? 312 VAL   A C   1 
ATOM   2117 O O   . VAL   A 1 312 ? -15.835 -42.844 -27.170 1.00 44.86  ? 312 VAL   A O   1 
ATOM   2118 C CB  . VAL   A 1 312 ? -18.588 -41.746 -25.952 1.00 46.21  ? 312 VAL   A CB  1 
ATOM   2119 C CG1 . VAL   A 1 312 ? -19.294 -43.066 -25.675 1.00 41.65  ? 312 VAL   A CG1 1 
ATOM   2120 C CG2 . VAL   A 1 312 ? -17.542 -41.442 -24.886 1.00 42.45  ? 312 VAL   A CG2 1 
ATOM   2121 N N   . ALA   A 1 313 ? -17.461 -43.975 -28.226 1.00 45.24  ? 313 ALA   A N   1 
ATOM   2122 C CA  . ALA   A 1 313 ? -16.553 -45.060 -28.584 1.00 43.38  ? 313 ALA   A CA  1 
ATOM   2123 C C   . ALA   A 1 313 ? -15.540 -44.594 -29.625 1.00 44.61  ? 313 ALA   A C   1 
ATOM   2124 O O   . ALA   A 1 313 ? -14.326 -44.730 -29.433 1.00 45.51  ? 313 ALA   A O   1 
ATOM   2125 C CB  . ALA   A 1 313 ? -17.344 -46.266 -29.093 1.00 42.30  ? 313 ALA   A CB  1 
ATOM   2126 N N   . ASP   A 1 314 ? -16.028 -44.041 -30.740 1.00 44.25  ? 314 ASP   A N   1 
ATOM   2127 C CA  . ASP   A 1 314 ? -15.137 -43.453 -31.737 1.00 47.11  ? 314 ASP   A CA  1 
ATOM   2128 C C   . ASP   A 1 314 ? -14.252 -42.380 -31.118 1.00 46.84  ? 314 ASP   A C   1 
ATOM   2129 O O   . ASP   A 1 314 ? -13.054 -42.299 -31.418 1.00 43.65  ? 314 ASP   A O   1 
ATOM   2130 C CB  . ASP   A 1 314 ? -15.951 -42.855 -32.888 1.00 46.91  ? 314 ASP   A CB  1 
ATOM   2131 C CG  . ASP   A 1 314 ? -16.747 -43.895 -33.648 1.00 49.89  ? 314 ASP   A CG  1 
ATOM   2132 O OD1 . ASP   A 1 314 ? -16.450 -45.099 -33.507 1.00 48.40  ? 314 ASP   A OD1 1 
ATOM   2133 O OD2 . ASP   A 1 314 ? -17.677 -43.504 -34.385 1.00 55.46  ? 314 ASP   A OD2 1 
ATOM   2134 N N   . TYR   A 1 315 ? -14.827 -41.552 -30.242 1.00 45.30  ? 315 TYR   A N   1 
ATOM   2135 C CA  . TYR   A 1 315 ? -14.088 -40.435 -29.665 1.00 44.13  ? 315 TYR   A CA  1 
ATOM   2136 C C   . TYR   A 1 315 ? -12.932 -40.924 -28.799 1.00 45.24  ? 315 TYR   A C   1 
ATOM   2137 O O   . TYR   A 1 315 ? -11.793 -40.468 -28.953 1.00 44.22  ? 315 TYR   A O   1 
ATOM   2138 C CB  . TYR   A 1 315 ? -15.038 -39.546 -28.862 1.00 44.29  ? 315 TYR   A CB  1 
ATOM   2139 C CG  . TYR   A 1 315 ? -14.353 -38.652 -27.855 1.00 45.46  ? 315 TYR   A CG  1 
ATOM   2140 C CD1 . TYR   A 1 315 ? -13.512 -37.631 -28.268 1.00 43.15  ? 315 TYR   A CD1 1 
ATOM   2141 C CD2 . TYR   A 1 315 ? -14.562 -38.819 -26.492 1.00 45.81  ? 315 TYR   A CD2 1 
ATOM   2142 C CE1 . TYR   A 1 315 ? -12.886 -36.809 -27.353 1.00 45.72  ? 315 TYR   A CE1 1 
ATOM   2143 C CE2 . TYR   A 1 315 ? -13.943 -37.999 -25.569 1.00 45.53  ? 315 TYR   A CE2 1 
ATOM   2144 C CZ  . TYR   A 1 315 ? -13.107 -36.994 -26.005 1.00 45.98  ? 315 TYR   A CZ  1 
ATOM   2145 O OH  . TYR   A 1 315 ? -12.485 -36.172 -25.091 1.00 47.83  ? 315 TYR   A OH  1 
ATOM   2146 N N   . THR   A 1 316 ? -13.208 -41.855 -27.882 1.00 43.55  ? 316 THR   A N   1 
ATOM   2147 C CA  . THR   A 1 316 ? -12.154 -42.372 -27.015 1.00 43.21  ? 316 THR   A CA  1 
ATOM   2148 C C   . THR   A 1 316 ? -11.072 -43.073 -27.826 1.00 46.22  ? 316 THR   A C   1 
ATOM   2149 O O   . THR   A 1 316 ? -9.878  -42.943 -27.530 1.00 43.18  ? 316 THR   A O   1 
ATOM   2150 C CB  . THR   A 1 316 ? -12.749 -43.323 -25.980 1.00 43.16  ? 316 THR   A CB  1 
ATOM   2151 O OG1 . THR   A 1 316 ? -13.934 -42.741 -25.425 1.00 44.40  ? 316 THR   A OG1 1 
ATOM   2152 C CG2 . THR   A 1 316 ? -11.753 -43.582 -24.864 1.00 42.27  ? 316 THR   A CG2 1 
ATOM   2153 N N   . ARG   A 1 317 ? -11.473 -43.816 -28.860 1.00 46.09  ? 317 ARG   A N   1 
ATOM   2154 C CA  . ARG   A 1 317 ? -10.501 -44.463 -29.735 1.00 45.77  ? 317 ARG   A CA  1 
ATOM   2155 C C   . ARG   A 1 317 ? -9.574  -43.436 -30.372 1.00 48.89  ? 317 ARG   A C   1 
ATOM   2156 O O   . ARG   A 1 317 ? -8.345  -43.561 -30.303 1.00 49.00  ? 317 ARG   A O   1 
ATOM   2157 C CB  . ARG   A 1 317 ? -11.230 -45.272 -30.807 1.00 49.57  ? 317 ARG   A CB  1 
ATOM   2158 C CG  . ARG   A 1 317 ? -10.355 -46.246 -31.575 1.00 56.22  ? 317 ARG   A CG  1 
ATOM   2159 C CD  . ARG   A 1 317 ? -11.215 -47.283 -32.280 1.00 57.85  ? 317 ARG   A CD  1 
ATOM   2160 N NE  . ARG   A 1 317 ? -10.480 -47.982 -33.328 1.00 65.05  ? 317 ARG   A NE  1 
ATOM   2161 C CZ  . ARG   A 1 317 ? -10.900 -48.107 -34.581 1.00 67.81  ? 317 ARG   A CZ  1 
ATOM   2162 N NH1 . ARG   A 1 317 ? -12.039 -47.567 -34.987 1.00 68.73  ? 317 ARG   A NH1 1 
ATOM   2163 N NH2 . ARG   A 1 317 ? -10.157 -48.790 -35.449 1.00 62.19  ? 317 ARG   A NH2 1 
ATOM   2164 N N   . MET   A 1 318 ? -10.149 -42.400 -30.987 1.00 48.00  ? 318 MET   A N   1 
ATOM   2165 C CA  . MET   A 1 318 ? -9.323  -41.366 -31.597 1.00 44.40  ? 318 MET   A CA  1 
ATOM   2166 C C   . MET   A 1 318 ? -8.557  -40.578 -30.542 1.00 44.11  ? 318 MET   A C   1 
ATOM   2167 O O   . MET   A 1 318 ? -7.426  -40.145 -30.792 1.00 41.27  ? 318 MET   A O   1 
ATOM   2168 C CB  . MET   A 1 318 ? -10.187 -40.438 -32.456 1.00 41.69  ? 318 MET   A CB  1 
ATOM   2169 C CG  . MET   A 1 318 ? -9.513  -39.123 -32.822 1.00 45.37  ? 318 MET   A CG  1 
ATOM   2170 S SD  . MET   A 1 318 ? -10.435 -38.095 -33.980 1.00 42.69  ? 318 MET   A SD  1 
ATOM   2171 C CE  . MET   A 1 318 ? -10.740 -39.239 -35.313 1.00 45.09  ? 318 MET   A CE  1 
ATOM   2172 N N   . LEU   A 1 319 ? -9.138  -40.412 -29.353 1.00 45.60  ? 319 LEU   A N   1 
ATOM   2173 C CA  . LEU   A 1 319 ? -8.457  -39.692 -28.282 1.00 44.25  ? 319 LEU   A CA  1 
ATOM   2174 C C   . LEU   A 1 319 ? -7.213  -40.440 -27.815 1.00 44.65  ? 319 LEU   A C   1 
ATOM   2175 O O   . LEU   A 1 319 ? -6.151  -39.838 -27.616 1.00 44.87  ? 319 LEU   A O   1 
ATOM   2176 C CB  . LEU   A 1 319 ? -9.423  -39.465 -27.118 1.00 43.50  ? 319 LEU   A CB  1 
ATOM   2177 C CG  . LEU   A 1 319 ? -8.887  -38.883 -25.814 1.00 46.94  ? 319 LEU   A CG  1 
ATOM   2178 C CD1 . LEU   A 1 319 ? -8.505  -37.427 -26.005 1.00 46.37  ? 319 LEU   A CD1 1 
ATOM   2179 C CD2 . LEU   A 1 319 ? -9.947  -39.021 -24.738 1.00 44.74  ? 319 LEU   A CD2 1 
ATOM   2180 N N   . LEU   A 1 320 ? -7.328  -41.758 -27.628 1.00 44.85  ? 320 LEU   A N   1 
ATOM   2181 C CA  . LEU   A 1 320 ? -6.178  -42.546 -27.190 1.00 42.03  ? 320 LEU   A CA  1 
ATOM   2182 C C   . LEU   A 1 320 ? -5.042  -42.477 -28.202 1.00 44.10  ? 320 LEU   A C   1 
ATOM   2183 O O   . LEU   A 1 320 ? -3.871  -42.334 -27.826 1.00 43.98  ? 320 LEU   A O   1 
ATOM   2184 C CB  . LEU   A 1 320 ? -6.594  -43.998 -26.960 1.00 43.13  ? 320 LEU   A CB  1 
ATOM   2185 C CG  . LEU   A 1 320 ? -7.554  -44.300 -25.811 1.00 44.42  ? 320 LEU   A CG  1 
ATOM   2186 C CD1 . LEU   A 1 320 ? -8.086  -45.723 -25.936 1.00 43.42  ? 320 LEU   A CD1 1 
ATOM   2187 C CD2 . LEU   A 1 320 ? -6.872  -44.088 -24.470 1.00 40.86  ? 320 LEU   A CD2 1 
ATOM   2188 N N   . VAL   A 1 321 ? -5.370  -42.572 -29.492 1.00 43.97  ? 321 VAL   A N   1 
ATOM   2189 C CA  . VAL   A 1 321 ? -4.344  -42.564 -30.530 1.00 41.76  ? 321 VAL   A CA  1 
ATOM   2190 C C   . VAL   A 1 321 ? -3.638  -41.215 -30.576 1.00 46.38  ? 321 VAL   A C   1 
ATOM   2191 O O   . VAL   A 1 321 ? -2.408  -41.145 -30.689 1.00 47.87  ? 321 VAL   A O   1 
ATOM   2192 C CB  . VAL   A 1 321 ? -4.972  -42.921 -31.889 1.00 44.81  ? 321 VAL   A CB  1 
ATOM   2193 C CG1 . VAL   A 1 321 ? -4.028  -42.572 -33.024 1.00 39.18  ? 321 VAL   A CG1 1 
ATOM   2194 C CG2 . VAL   A 1 321 ? -5.364  -44.391 -31.930 1.00 44.43  ? 321 VAL   A CG2 1 
ATOM   2195 N N   . VAL   A 1 322 ? -4.403  -40.124 -30.486 1.00 43.95  ? 322 VAL   A N   1 
ATOM   2196 C CA  . VAL   A 1 322 ? -3.818  -38.789 -30.577 1.00 44.06  ? 322 VAL   A CA  1 
ATOM   2197 C C   . VAL   A 1 322 ? -2.862  -38.541 -29.417 1.00 47.06  ? 322 VAL   A C   1 
ATOM   2198 O O   . VAL   A 1 322 ? -1.757  -38.015 -29.604 1.00 45.54  ? 322 VAL   A O   1 
ATOM   2199 C CB  . VAL   A 1 322 ? -4.928  -37.722 -30.638 1.00 42.25  ? 322 VAL   A CB  1 
ATOM   2200 C CG1 . VAL   A 1 322 ? -4.350  -36.329 -30.401 1.00 44.16  ? 322 VAL   A CG1 1 
ATOM   2201 C CG2 . VAL   A 1 322 ? -5.653  -37.781 -31.975 1.00 43.28  ? 322 VAL   A CG2 1 
ATOM   2202 N N   . LEU   A 1 323 ? -3.266  -38.920 -28.200 1.00 45.81  ? 323 LEU   A N   1 
ATOM   2203 C CA  . LEU   A 1 323 ? -2.409  -38.711 -27.036 1.00 47.41  ? 323 LEU   A CA  1 
ATOM   2204 C C   . LEU   A 1 323 ? -1.155  -39.577 -27.090 1.00 48.04  ? 323 LEU   A C   1 
ATOM   2205 O O   . LEU   A 1 323 ? -0.087  -39.142 -26.644 1.00 46.39  ? 323 LEU   A O   1 
ATOM   2206 C CB  . LEU   A 1 323 ? -3.191  -38.979 -25.750 1.00 45.30  ? 323 LEU   A CB  1 
ATOM   2207 C CG  . LEU   A 1 323 ? -4.445  -38.127 -25.541 1.00 46.14  ? 323 LEU   A CG  1 
ATOM   2208 C CD1 . LEU   A 1 323 ? -5.201  -38.584 -24.307 1.00 48.34  ? 323 LEU   A CD1 1 
ATOM   2209 C CD2 . LEU   A 1 323 ? -4.095  -36.644 -25.450 1.00 44.78  ? 323 LEU   A CD2 1 
ATOM   2210 N N   . ALA   A 1 324 ? -1.259  -40.789 -27.636 1.00 47.92  ? 324 ALA   A N   1 
ATOM   2211 C CA  . ALA   A 1 324 ? -0.108  -41.667 -27.810 1.00 49.10  ? 324 ALA   A CA  1 
ATOM   2212 C C   . ALA   A 1 324 ? 0.716   -41.335 -29.050 1.00 53.20  ? 324 ALA   A C   1 
ATOM   2213 O O   . ALA   A 1 324 ? 1.703   -42.032 -29.312 1.00 54.64  ? 324 ALA   A O   1 
ATOM   2214 C CB  . ALA   A 1 324 ? -0.564  -43.128 -27.876 1.00 49.32  ? 324 ALA   A CB  1 
ATOM   2215 N N   . ARG   A 1 325 ? 0.344   -40.290 -29.800 1.00 50.82  ? 325 ARG   A N   1 
ATOM   2216 C CA  . ARG   A 1 325 ? 0.989   -39.937 -31.069 1.00 46.60  ? 325 ARG   A CA  1 
ATOM   2217 C C   . ARG   A 1 325 ? 1.161   -41.162 -31.966 1.00 51.11  ? 325 ARG   A C   1 
ATOM   2218 O O   . ARG   A 1 325 ? 2.159   -41.312 -32.675 1.00 49.35  ? 325 ARG   A O   1 
ATOM   2219 C CB  . ARG   A 1 325 ? 2.329   -39.235 -30.843 1.00 48.10  ? 325 ARG   A CB  1 
ATOM   2220 C CG  . ARG   A 1 325 ? 2.219   -37.804 -30.337 1.00 47.29  ? 325 ARG   A CG  1 
ATOM   2221 C CD  . ARG   A 1 325 ? 3.495   -37.007 -30.631 1.00 49.30  ? 325 ARG   A CD  1 
ATOM   2222 N NE  . ARG   A 1 325 ? 3.359   -36.043 -31.720 1.00 47.88  ? 325 ARG   A NE  1 
ATOM   2223 C CZ  . ARG   A 1 325 ? 4.029   -36.093 -32.866 1.00 50.81  ? 325 ARG   A CZ  1 
ATOM   2224 N NH1 . ARG   A 1 325 ? 4.832   -37.104 -33.157 1.00 54.87  ? 325 ARG   A NH1 1 
ATOM   2225 N NH2 . ARG   A 1 325 ? 3.887   -35.104 -33.744 1.00 48.12  ? 325 ARG   A NH2 1 
ATOM   2226 N N   . GLY   A 1 326 ? 0.193   -42.080 -31.904 1.00 49.43  ? 326 GLY   A N   1 
ATOM   2227 C CA  . GLY   A 1 326 ? 0.223   -43.250 -32.804 1.00 49.51  ? 326 GLY   A CA  1 
ATOM   2228 C C   . GLY   A 1 326 ? 0.961   -44.444 -32.231 1.00 57.35  ? 326 GLY   A C   1 
ATOM   2229 O O   . GLY   A 1 326 ? 0.706   -45.566 -32.708 1.00 65.06  ? 326 GLY   A O   1 
ATOM   2230 N N   . LEU   A 1 327 ? 1.838   -44.231 -31.249 1.00 57.06  ? 327 LEU   A N   1 
ATOM   2231 C CA  . LEU   A 1 327 ? 2.663   -45.338 -30.693 1.00 60.04  ? 327 LEU   A CA  1 
ATOM   2232 C C   . LEU   A 1 327 ? 1.758   -46.359 -29.987 1.00 67.27  ? 327 LEU   A C   1 
ATOM   2233 O O   . LEU   A 1 327 ? 0.762   -45.932 -29.367 1.00 65.56  ? 327 LEU   A O   1 
ATOM   2234 C CB  . LEU   A 1 327 ? 3.723   -44.750 -29.768 1.00 55.64  ? 327 LEU   A CB  1 
ATOM   2235 C CG  . LEU   A 1 327 ? 4.596   -43.660 -30.396 1.00 55.33  ? 327 LEU   A CG  1 
ATOM   2236 C CD1 . LEU   A 1 327 ? 5.223   -42.765 -29.345 1.00 53.26  ? 327 LEU   A CD1 1 
ATOM   2237 C CD2 . LEU   A 1 327 ? 5.657   -44.280 -31.285 1.00 51.68  ? 327 LEU   A CD2 1 
ATOM   2238 N N   . ALA   A 1 328 ? 2.092   -47.652 -30.070 1.00 71.76  ? 328 ALA   A N   1 
ATOM   2239 C CA  . ALA   A 1 328 ? 1.185   -48.687 -29.514 1.00 79.01  ? 328 ALA   A CA  1 
ATOM   2240 C C   . ALA   A 1 328 ? 1.800   -49.404 -28.310 1.00 86.54  ? 328 ALA   A C   1 
ATOM   2241 O O   . ALA   A 1 328 ? 2.949   -49.887 -28.386 1.00 84.28  ? 328 ALA   A O   1 
ATOM   2242 C CB  . ALA   A 1 328 ? 0.818   -49.668 -30.600 1.00 79.85  ? 328 ALA   A CB  1 
ATOM   2243 N N   . PRO   A 1 329 ? 1.066   -49.479 -27.180 1.00 91.19  ? 329 PRO   A N   1 
ATOM   2244 C CA  . PRO   A 1 329 ? 1.554   -50.132 -25.967 1.00 94.18  ? 329 PRO   A CA  1 
ATOM   2245 C C   . PRO   A 1 329 ? 1.673   -51.652 -25.912 1.00 94.21  ? 329 PRO   A C   1 
ATOM   2246 O O   . PRO   A 1 329 ? 0.874   -52.327 -26.579 1.00 93.90  ? 329 PRO   A O   1 
ATOM   2247 C CB  . PRO   A 1 329 ? 0.535   -49.628 -24.913 1.00 94.55  ? 329 PRO   A CB  1 
ATOM   2248 C CG  . PRO   A 1 329 ? -0.189  -48.487 -25.586 1.00 92.77  ? 329 PRO   A CG  1 
ATOM   2249 C CD  . PRO   A 1 329 ? -0.263  -48.927 -27.030 1.00 89.43  ? 329 PRO   A CD  1 
ATOM   2250 N N   . GLU   A 1 330 ? 2.649   -52.174 -25.163 1.00 98.47  ? 330 GLU   A N   1 
ATOM   2251 C CA  . GLU   A 1 330 ? 2.770   -53.640 -24.912 1.00 99.76  ? 330 GLU   A CA  1 
ATOM   2252 C C   . GLU   A 1 330 ? 2.913   -54.461 -26.201 1.00 98.71  ? 330 GLU   A C   1 
ATOM   2253 O O   . GLU   A 1 330 ? 2.342   -55.571 -26.247 1.00 95.72  ? 330 GLU   A O   1 
ATOM   2254 C CB  . GLU   A 1 330 ? 1.569   -54.134 -24.103 1.00 98.65  ? 330 GLU   A CB  1 
ATOM   2255 C CG  . GLU   A 1 330 ? 1.493   -53.525 -22.706 1.00 100.06 ? 330 GLU   A CG  1 
ATOM   2256 C CD  . GLU   A 1 330 ? 0.467   -52.414 -22.581 1.00 105.97 ? 330 GLU   A CD  1 
ATOM   2257 O OE1 . GLU   A 1 330 ? -0.587  -52.509 -23.244 1.00 105.02 ? 330 GLU   A OE1 1 
ATOM   2258 O OE2 . GLU   A 1 330 ? 0.724   -51.453 -21.827 1.00 106.63 ? 330 GLU   A OE2 1 
ATOM   2259 N N   . GLY   A 1 331 ? 3.613   -53.945 -27.211 1.00 95.75  ? 331 GLY   A N   1 
ATOM   2260 C CA  . GLY   A 1 331 ? 3.884   -54.762 -28.410 1.00 94.61  ? 331 GLY   A CA  1 
ATOM   2261 C C   . GLY   A 1 331 ? 2.660   -54.913 -29.291 1.00 96.02  ? 331 GLY   A C   1 
ATOM   2262 O O   . GLY   A 1 331 ? 2.705   -55.753 -30.212 1.00 92.57  ? 331 GLY   A O   1 
ATOM   2263 N N   . THR   A 1 332 ? 1.603   -54.138 -29.032 1.00 94.65  ? 332 THR   A N   1 
ATOM   2264 C CA  . THR   A 1 332 ? 0.411   -54.176 -29.904 1.00 92.33  ? 332 THR   A CA  1 
ATOM   2265 C C   . THR   A 1 332 ? 0.781   -53.571 -31.237 1.00 88.01  ? 332 THR   A C   1 
ATOM   2266 O O   . THR   A 1 332 ? 1.646   -52.672 -31.254 1.00 83.14  ? 332 THR   A O   1 
ATOM   2267 C CB  . THR   A 1 332 ? -0.761  -53.446 -29.253 1.00 91.39  ? 332 THR   A CB  1 
ATOM   2268 O OG1 . THR   A 1 332 ? -0.226  -52.207 -28.800 1.00 90.70  ? 332 THR   A OG1 1 
ATOM   2269 C CG2 . THR   A 1 332 ? -1.348  -54.224 -28.089 1.00 89.74  ? 332 THR   A CG2 1 
ATOM   2270 N N   . GLU   A 1 333 ? 0.189   -54.061 -32.327 1.00 87.35  ? 333 GLU   A N   1 
ATOM   2271 C CA  . GLU   A 1 333 ? 0.458   -53.405 -33.630 1.00 84.47  ? 333 GLU   A CA  1 
ATOM   2272 C C   . GLU   A 1 333 ? -0.097  -51.975 -33.572 1.00 80.17  ? 333 GLU   A C   1 
ATOM   2273 O O   . GLU   A 1 333 ? -1.218  -51.786 -33.052 1.00 77.54  ? 333 GLU   A O   1 
ATOM   2274 C CB  . GLU   A 1 333 ? -0.167  -54.211 -34.768 1.00 84.74  ? 333 GLU   A CB  1 
ATOM   2275 C CG  . GLU   A 1 333 ? -1.571  -54.717 -34.451 1.00 90.36  ? 333 GLU   A CG  1 
ATOM   2276 C CD  . GLU   A 1 333 ? -2.670  -54.014 -35.227 1.00 93.33  ? 333 GLU   A CD  1 
ATOM   2277 O OE1 . GLU   A 1 333 ? -2.407  -52.927 -35.785 1.00 91.21  ? 333 GLU   A OE1 1 
ATOM   2278 O OE2 . GLU   A 1 333 ? -3.793  -54.556 -35.273 1.00 94.02  ? 333 GLU   A OE2 1 
ATOM   2279 N N   . PRO   A 1 334 ? 0.635   -50.963 -34.078 1.00 72.71  ? 334 PRO   A N   1 
ATOM   2280 C CA  . PRO   A 1 334 ? 0.125   -49.600 -34.122 1.00 69.30  ? 334 PRO   A CA  1 
ATOM   2281 C C   . PRO   A 1 334 ? -0.995  -49.424 -35.133 1.00 63.61  ? 334 PRO   A C   1 
ATOM   2282 O O   . PRO   A 1 334 ? -0.984  -50.118 -36.167 1.00 67.09  ? 334 PRO   A O   1 
ATOM   2283 C CB  . PRO   A 1 334 ? 1.370   -48.779 -34.485 1.00 68.08  ? 334 PRO   A CB  1 
ATOM   2284 C CG  . PRO   A 1 334 ? 2.526   -49.714 -34.219 1.00 67.45  ? 334 PRO   A CG  1 
ATOM   2285 C CD  . PRO   A 1 334 ? 1.987   -51.083 -34.579 1.00 70.18  ? 334 PRO   A CD  1 
ATOM   2286 N N   . VAL   A 1 335 ? -1.947  -48.534 -34.847 1.00 59.88  ? 335 VAL   A N   1 
ATOM   2287 C CA  . VAL   A 1 335 ? -3.008  -48.225 -35.850 1.00 52.98  ? 335 VAL   A CA  1 
ATOM   2288 C C   . VAL   A 1 335 ? -2.309  -47.739 -37.129 1.00 51.60  ? 335 VAL   A C   1 
ATOM   2289 O O   . VAL   A 1 335 ? -1.431  -46.860 -37.023 1.00 51.48  ? 335 VAL   A O   1 
ATOM   2290 C CB  . VAL   A 1 335 ? -4.003  -47.180 -35.313 1.00 51.36  ? 335 VAL   A CB  1 
ATOM   2291 C CG1 . VAL   A 1 335 ? -4.880  -46.593 -36.411 1.00 50.08  ? 335 VAL   A CG1 1 
ATOM   2292 C CG2 . VAL   A 1 335 ? -4.858  -47.744 -34.186 1.00 52.72  ? 335 VAL   A CG2 1 
ATOM   2293 N N   . SER   A 1 336 ? -2.674  -48.301 -38.283 1.00 49.91  ? 336 SER   A N   1 
ATOM   2294 C CA  . SER   A 1 336 ? -2.047  -47.917 -39.536 1.00 48.61  ? 336 SER   A CA  1 
ATOM   2295 C C   . SER   A 1 336 ? -2.448  -46.499 -39.927 1.00 47.31  ? 336 SER   A C   1 
ATOM   2296 O O   . SER   A 1 336 ? -3.489  -45.985 -39.509 1.00 46.15  ? 336 SER   A O   1 
ATOM   2297 C CB  . SER   A 1 336 ? -2.432  -48.901 -40.637 1.00 48.81  ? 336 SER   A CB  1 
ATOM   2298 O OG  . SER   A 1 336 ? -3.563  -48.438 -41.349 1.00 49.95  ? 336 SER   A OG  1 
ATOM   2299 N N   . LEU   A 1 337 ? -1.589  -45.858 -40.726 1.00 46.31  ? 337 LEU   A N   1 
ATOM   2300 C CA  . LEU   A 1 337 ? -1.928  -44.548 -41.275 1.00 47.86  ? 337 LEU   A CA  1 
ATOM   2301 C C   . LEU   A 1 337 ? -3.197  -44.616 -42.115 1.00 49.23  ? 337 LEU   A C   1 
ATOM   2302 O O   . LEU   A 1 337 ? -4.025  -43.697 -42.078 1.00 47.45  ? 337 LEU   A O   1 
ATOM   2303 C CB  . LEU   A 1 337 ? -0.766  -44.008 -42.108 1.00 48.97  ? 337 LEU   A CB  1 
ATOM   2304 C CG  . LEU   A 1 337 ? -0.948  -42.611 -42.713 1.00 45.86  ? 337 LEU   A CG  1 
ATOM   2305 C CD1 . LEU   A 1 337 ? -1.554  -41.637 -41.708 1.00 45.86  ? 337 LEU   A CD1 1 
ATOM   2306 C CD2 . LEU   A 1 337 ? 0.370   -42.079 -43.248 1.00 44.40  ? 337 LEU   A CD2 1 
ATOM   2307 N N   . ASN   A 1 338 ? -3.368  -45.699 -42.879 1.00 48.74  ? 338 ASN   A N   1 
ATOM   2308 C CA  . ASN   A 1 338 ? -4.592  -45.873 -43.656 1.00 48.69  ? 338 ASN   A CA  1 
ATOM   2309 C C   . ASN   A 1 338 ? -5.817  -45.943 -42.753 1.00 48.32  ? 338 ASN   A C   1 
ATOM   2310 O O   . ASN   A 1 338 ? -6.884  -45.420 -43.098 1.00 48.37  ? 338 ASN   A O   1 
ATOM   2311 C CB  . ASN   A 1 338 ? -4.494  -47.135 -44.513 1.00 50.26  ? 338 ASN   A CB  1 
ATOM   2312 C CG  . ASN   A 1 338 ? -5.711  -47.335 -45.393 1.00 46.46  ? 338 ASN   A CG  1 
ATOM   2313 O OD1 . ASN   A 1 338 ? -6.389  -48.356 -45.309 1.00 54.35  ? 338 ASN   A OD1 1 
ATOM   2314 N ND2 . ASN   A 1 338 ? -5.989  -46.362 -46.249 1.00 47.18  ? 338 ASN   A ND2 1 
ATOM   2315 N N   . ALA   A 1 339 ? -5.689  -46.602 -41.598 1.00 46.46  ? 339 ALA   A N   1 
ATOM   2316 C CA  . ALA   A 1 339 ? -6.808  -46.694 -40.669 1.00 45.24  ? 339 ALA   A CA  1 
ATOM   2317 C C   . ALA   A 1 339 ? -7.063  -45.370 -39.965 1.00 48.06  ? 339 ALA   A C   1 
ATOM   2318 O O   . ALA   A 1 339 ? -8.204  -45.080 -39.587 1.00 48.60  ? 339 ALA   A O   1 
ATOM   2319 C CB  . ALA   A 1 339 ? -6.556  -47.798 -39.643 1.00 43.01  ? 339 ALA   A CB  1 
ATOM   2320 N N   . TRP   A 1 340 ? -6.017  -44.563 -39.771 1.00 47.15  ? 340 TRP   A N   1 
ATOM   2321 C CA  . TRP   A 1 340 ? -6.202  -43.233 -39.200 1.00 47.56  ? 340 TRP   A CA  1 
ATOM   2322 C C   . TRP   A 1 340 ? -7.004  -42.344 -40.140 1.00 47.79  ? 340 TRP   A C   1 
ATOM   2323 O O   . TRP   A 1 340 ? -7.837  -41.547 -39.692 1.00 46.51  ? 340 TRP   A O   1 
ATOM   2324 C CB  . TRP   A 1 340 ? -4.845  -42.602 -38.887 1.00 46.55  ? 340 TRP   A CB  1 
ATOM   2325 C CG  . TRP   A 1 340 ? -4.916  -41.149 -38.504 1.00 47.13  ? 340 TRP   A CG  1 
ATOM   2326 C CD1 . TRP   A 1 340 ? -4.453  -40.086 -39.226 1.00 45.61  ? 340 TRP   A CD1 1 
ATOM   2327 C CD2 . TRP   A 1 340 ? -5.470  -40.603 -37.299 1.00 45.35  ? 340 TRP   A CD2 1 
ATOM   2328 N NE1 . TRP   A 1 340 ? -4.693  -38.913 -38.550 1.00 42.27  ? 340 TRP   A NE1 1 
ATOM   2329 C CE2 . TRP   A 1 340 ? -5.313  -39.203 -37.363 1.00 46.86  ? 340 TRP   A CE2 1 
ATOM   2330 C CE3 . TRP   A 1 340 ? -6.084  -41.162 -36.174 1.00 41.58  ? 340 TRP   A CE3 1 
ATOM   2331 C CZ2 . TRP   A 1 340 ? -5.750  -38.354 -36.345 1.00 45.04  ? 340 TRP   A CZ2 1 
ATOM   2332 C CZ3 . TRP   A 1 340 ? -6.518  -40.318 -35.166 1.00 44.66  ? 340 TRP   A CZ3 1 
ATOM   2333 C CH2 . TRP   A 1 340 ? -6.349  -38.930 -35.259 1.00 44.48  ? 340 TRP   A CH2 1 
ATOM   2334 N N   . TYR   A 1 341 ? -6.767  -42.469 -41.448 1.00 48.22  ? 341 TYR   A N   1 
ATOM   2335 C CA  . TYR   A 1 341 ? -7.560  -41.725 -42.420 1.00 45.88  ? 341 TYR   A CA  1 
ATOM   2336 C C   . TYR   A 1 341 ? -9.024  -42.144 -42.369 1.00 45.83  ? 341 TYR   A C   1 
ATOM   2337 O O   . TYR   A 1 341 ? -9.924  -41.305 -42.491 1.00 47.23  ? 341 TYR   A O   1 
ATOM   2338 C CB  . TYR   A 1 341 ? -6.992  -41.926 -43.825 1.00 45.40  ? 341 TYR   A CB  1 
ATOM   2339 C CG  . TYR   A 1 341 ? -5.670  -41.227 -44.065 1.00 46.61  ? 341 TYR   A CG  1 
ATOM   2340 C CD1 . TYR   A 1 341 ? -5.372  -40.020 -43.443 1.00 45.72  ? 341 TYR   A CD1 1 
ATOM   2341 C CD2 . TYR   A 1 341 ? -4.720  -41.777 -44.915 1.00 47.35  ? 341 TYR   A CD2 1 
ATOM   2342 C CE1 . TYR   A 1 341 ? -4.163  -39.381 -43.661 1.00 45.18  ? 341 TYR   A CE1 1 
ATOM   2343 C CE2 . TYR   A 1 341 ? -3.510  -41.146 -45.142 1.00 47.31  ? 341 TYR   A CE2 1 
ATOM   2344 C CZ  . TYR   A 1 341 ? -3.235  -39.950 -44.512 1.00 48.89  ? 341 TYR   A CZ  1 
ATOM   2345 O OH  . TYR   A 1 341 ? -2.030  -39.323 -44.738 1.00 45.75  ? 341 TYR   A OH  1 
ATOM   2346 N N   . ALA   A 1 342 ? -9.284  -43.440 -42.183 1.00 43.37  ? 342 ALA   A N   1 
ATOM   2347 C CA  . ALA   A 1 342 ? -10.664 -43.900 -42.072 1.00 45.74  ? 342 ALA   A CA  1 
ATOM   2348 C C   . ALA   A 1 342 ? -11.317 -43.406 -40.787 1.00 45.40  ? 342 ALA   A C   1 
ATOM   2349 O O   . ALA   A 1 342 ? -12.525 -43.144 -40.768 1.00 42.78  ? 342 ALA   A O   1 
ATOM   2350 C CB  . ALA   A 1 342 ? -10.721 -45.424 -42.153 1.00 42.12  ? 342 ALA   A CB  1 
ATOM   2351 N N   . MET   A 1 343 ? -10.539 -43.268 -39.710 1.00 44.69  ? 343 MET   A N   1 
ATOM   2352 C CA  . MET   A 1 343 ? -11.081 -42.713 -38.474 1.00 46.18  ? 343 MET   A CA  1 
ATOM   2353 C C   . MET   A 1 343 ? -11.479 -41.254 -38.657 1.00 45.38  ? 343 MET   A C   1 
ATOM   2354 O O   . MET   A 1 343 ? -12.490 -40.807 -38.103 1.00 48.40  ? 343 MET   A O   1 
ATOM   2355 C CB  . MET   A 1 343 ? -10.065 -42.847 -37.340 1.00 47.68  ? 343 MET   A CB  1 
ATOM   2356 C CG  . MET   A 1 343 ? -9.942  -44.246 -36.755 1.00 48.95  ? 343 MET   A CG  1 
ATOM   2357 S SD  . MET   A 1 343 ? -8.406  -44.455 -35.832 1.00 54.45  ? 343 MET   A SD  1 
ATOM   2358 C CE  . MET   A 1 343 ? -8.576  -43.151 -34.623 1.00 44.33  ? 343 MET   A CE  1 
ATOM   2359 N N   . LEU   A 1 344 ? -10.693 -40.495 -39.426 1.00 44.04  ? 344 LEU   A N   1 
ATOM   2360 C CA  . LEU   A 1 344 ? -11.057 -39.111 -39.713 1.00 43.85  ? 344 LEU   A CA  1 
ATOM   2361 C C   . LEU   A 1 344 ? -12.316 -39.040 -40.567 1.00 45.18  ? 344 LEU   A C   1 
ATOM   2362 O O   . LEU   A 1 344 ? -13.130 -38.122 -40.407 1.00 47.32  ? 344 LEU   A O   1 
ATOM   2363 C CB  . LEU   A 1 344 ? -9.897  -38.393 -40.400 1.00 44.07  ? 344 LEU   A CB  1 
ATOM   2364 C CG  . LEU   A 1 344 ? -8.647  -38.211 -39.539 1.00 44.27  ? 344 LEU   A CG  1 
ATOM   2365 C CD1 . LEU   A 1 344 ? -7.515  -37.594 -40.346 1.00 41.38  ? 344 LEU   A CD1 1 
ATOM   2366 C CD2 . LEU   A 1 344 ? -8.965  -37.368 -38.313 1.00 43.69  ? 344 LEU   A CD2 1 
ATOM   2367 N N   . ASP   A 1 345 ? -12.488 -39.996 -41.487 1.00 43.98  ? 345 ASP   A N   1 
ATOM   2368 C CA  . ASP   A 1 345 ? -13.750 -40.112 -42.211 1.00 44.79  ? 345 ASP   A CA  1 
ATOM   2369 C C   . ASP   A 1 345 ? -14.904 -40.390 -41.255 1.00 43.83  ? 345 ASP   A C   1 
ATOM   2370 O O   . ASP   A 1 345 ? -15.980 -39.790 -41.377 1.00 43.86  ? 345 ASP   A O   1 
ATOM   2371 C CB  . ASP   A 1 345 ? -13.659 -41.217 -43.268 1.00 44.90  ? 345 ASP   A CB  1 
ATOM   2372 C CG  . ASP   A 1 345 ? -12.746 -40.854 -44.430 1.00 47.66  ? 345 ASP   A CG  1 
ATOM   2373 O OD1 . ASP   A 1 345 ? -12.665 -39.659 -44.780 1.00 48.53  ? 345 ASP   A OD1 1 
ATOM   2374 O OD2 . ASP   A 1 345 ? -12.114 -41.768 -45.001 1.00 50.53  ? 345 ASP   A OD2 1 
ATOM   2375 N N   . ASP   A 1 346 ? -14.698 -41.303 -40.298 1.00 44.87  ? 346 ASP   A N   1 
ATOM   2376 C CA  . ASP   A 1 346 ? -15.724 -41.590 -39.299 1.00 45.11  ? 346 ASP   A CA  1 
ATOM   2377 C C   . ASP   A 1 346 ? -16.111 -40.334 -38.532 1.00 45.94  ? 346 ASP   A C   1 
ATOM   2378 O O   . ASP   A 1 346 ? -17.297 -40.089 -38.280 1.00 42.35  ? 346 ASP   A O   1 
ATOM   2379 C CB  . ASP   A 1 346 ? -15.236 -42.667 -38.329 1.00 46.48  ? 346 ASP   A CB  1 
ATOM   2380 C CG  . ASP   A 1 346 ? -14.841 -43.958 -39.027 1.00 50.25  ? 346 ASP   A CG  1 
ATOM   2381 O OD1 . ASP   A 1 346 ? -15.449 -44.293 -40.067 1.00 49.05  ? 346 ASP   A OD1 1 
ATOM   2382 O OD2 . ASP   A 1 346 ? -13.918 -44.639 -38.530 1.00 53.23  ? 346 ASP   A OD2 1 
ATOM   2383 N N   . GLN   A 1 347 ? -15.120 -39.526 -38.151 1.00 43.55  ? 347 GLN   A N   1 
ATOM   2384 C CA  . GLN   A 1 347 ? -15.413 -38.265 -37.481 1.00 44.25  ? 347 GLN   A CA  1 
ATOM   2385 C C   . GLN   A 1 347 ? -16.187 -37.329 -38.400 1.00 44.55  ? 347 GLN   A C   1 
ATOM   2386 O O   . GLN   A 1 347 ? -17.220 -36.775 -38.009 1.00 40.61  ? 347 GLN   A O   1 
ATOM   2387 C CB  . GLN   A 1 347 ? -14.115 -37.614 -37.006 1.00 41.95  ? 347 GLN   A CB  1 
ATOM   2388 C CG  . GLN   A 1 347 ? -14.309 -36.298 -36.283 1.00 44.62  ? 347 GLN   A CG  1 
ATOM   2389 C CD  . GLN   A 1 347 ? -12.993 -35.659 -35.888 1.00 47.42  ? 347 GLN   A CD  1 
ATOM   2390 O OE1 . GLN   A 1 347 ? -12.006 -35.733 -36.625 1.00 42.33  ? 347 GLN   A OE1 1 
ATOM   2391 N NE2 . GLN   A 1 347 ? -12.972 -35.019 -34.722 1.00 46.66  ? 347 GLN   A NE2 1 
ATOM   2392 N N   . ALA   A 1 348 ? -15.706 -37.155 -39.636 1.00 47.18  ? 348 ALA   A N   1 
ATOM   2393 C CA  . ALA   A 1 348 ? -16.363 -36.259 -40.587 1.00 44.70  ? 348 ALA   A CA  1 
ATOM   2394 C C   . ALA   A 1 348 ? -17.820 -36.652 -40.806 1.00 41.31  ? 348 ALA   A C   1 
ATOM   2395 O O   . ALA   A 1 348 ? -18.708 -35.793 -40.841 1.00 42.56  ? 348 ALA   A O   1 
ATOM   2396 C CB  . ALA   A 1 348 ? -15.601 -36.256 -41.912 1.00 41.50  ? 348 ALA   A CB  1 
ATOM   2397 N N   . ARG   A 1 349 ? -18.077 -37.953 -40.976 1.00 44.84  ? 349 ARG   A N   1 
ATOM   2398 C CA  . ARG   A 1 349 ? -19.445 -38.464 -41.010 1.00 41.81  ? 349 ARG   A CA  1 
ATOM   2399 C C   . ARG   A 1 349 ? -20.239 -37.995 -39.798 1.00 44.47  ? 349 ARG   A C   1 
ATOM   2400 O O   . ARG   A 1 349 ? -21.355 -37.478 -39.930 1.00 44.77  ? 349 ARG   A O   1 
ATOM   2401 C CB  . ARG   A 1 349 ? -19.426 -39.993 -41.061 1.00 44.10  ? 349 ARG   A CB  1 
ATOM   2402 C CG  . ARG   A 1 349 ? -20.665 -40.628 -41.681 1.00 45.72  ? 349 ARG   A CG  1 
ATOM   2403 C CD  . ARG   A 1 349 ? -20.402 -42.085 -42.042 1.00 47.39  ? 349 ARG   A CD  1 
ATOM   2404 N NE  . ARG   A 1 349 ? -19.194 -42.235 -42.843 1.00 47.17  ? 349 ARG   A NE  1 
ATOM   2405 C CZ  . ARG   A 1 349 ? -18.145 -42.964 -42.487 1.00 49.57  ? 349 ARG   A CZ  1 
ATOM   2406 N NH1 . ARG   A 1 349 ? -18.120 -43.625 -41.341 1.00 50.20  ? 349 ARG   A NH1 1 
ATOM   2407 N NH2 . ARG   A 1 349 ? -17.091 -43.022 -43.296 1.00 44.50  ? 349 ARG   A NH2 1 
ATOM   2408 N N   . MET   A 1 350 ? -19.670 -38.176 -38.602 1.00 41.90  ? 350 MET   A N   1 
ATOM   2409 C CA  . MET   A 1 350 ? -20.358 -37.792 -37.372 1.00 44.41  ? 350 MET   A CA  1 
ATOM   2410 C C   . MET   A 1 350 ? -20.661 -36.297 -37.340 1.00 43.40  ? 350 MET   A C   1 
ATOM   2411 O O   . MET   A 1 350 ? -21.708 -35.882 -36.830 1.00 46.81  ? 350 MET   A O   1 
ATOM   2412 C CB  . MET   A 1 350 ? -19.517 -38.202 -36.162 1.00 43.88  ? 350 MET   A CB  1 
ATOM   2413 C CG  . MET   A 1 350 ? -20.140 -37.864 -34.816 1.00 46.28  ? 350 MET   A CG  1 
ATOM   2414 S SD  . MET   A 1 350 ? -21.710 -38.698 -34.519 1.00 47.64  ? 350 MET   A SD  1 
ATOM   2415 C CE  . MET   A 1 350 ? -21.173 -40.407 -34.471 1.00 44.41  ? 350 MET   A CE  1 
ATOM   2416 N N   . MET   A 1 351 ? -19.758 -35.470 -37.876 1.00 44.27  ? 351 MET   A N   1 
ATOM   2417 C CA  . MET   A 1 351 ? -20.015 -34.032 -37.923 1.00 45.14  ? 351 MET   A CA  1 
ATOM   2418 C C   . MET   A 1 351 ? -21.187 -33.698 -38.834 1.00 45.13  ? 351 MET   A C   1 
ATOM   2419 O O   . MET   A 1 351 ? -21.942 -32.761 -38.549 1.00 45.13  ? 351 MET   A O   1 
ATOM   2420 C CB  . MET   A 1 351 ? -18.767 -33.275 -38.378 1.00 43.65  ? 351 MET   A CB  1 
ATOM   2421 C CG  . MET   A 1 351 ? -17.473 -33.820 -37.812 1.00 46.15  ? 351 MET   A CG  1 
ATOM   2422 S SD  . MET   A 1 351 ? -16.020 -32.825 -38.185 1.00 53.04  ? 351 MET   A SD  1 
ATOM   2423 C CE  . MET   A 1 351 ? -16.767 -31.224 -38.493 1.00 48.90  ? 351 MET   A CE  1 
ATOM   2424 N N   . ARG   A 1 352 ? -21.356 -34.444 -39.928 1.00 46.81  ? 352 ARG   A N   1 
ATOM   2425 C CA  . ARG   A 1 352 ? -22.487 -34.195 -40.815 1.00 45.12  ? 352 ARG   A CA  1 
ATOM   2426 C C   . ARG   A 1 352 ? -23.803 -34.537 -40.130 1.00 46.75  ? 352 ARG   A C   1 
ATOM   2427 O O   . ARG   A 1 352 ? -24.803 -33.837 -40.320 1.00 50.45  ? 352 ARG   A O   1 
ATOM   2428 C CB  . ARG   A 1 352 ? -22.318 -34.976 -42.122 1.00 42.48  ? 352 ARG   A CB  1 
ATOM   2429 C CG  . ARG   A 1 352 ? -21.230 -34.385 -43.015 1.00 47.74  ? 352 ARG   A CG  1 
ATOM   2430 C CD  . ARG   A 1 352 ? -21.055 -35.082 -44.369 1.00 45.35  ? 352 ARG   A CD  1 
ATOM   2431 N NE  . ARG   A 1 352 ? -20.984 -36.536 -44.284 1.00 45.94  ? 352 ARG   A NE  1 
ATOM   2432 C CZ  . ARG   A 1 352 ? -19.871 -37.241 -44.451 1.00 43.90  ? 352 ARG   A CZ  1 
ATOM   2433 N NH1 . ARG   A 1 352 ? -18.697 -36.653 -44.609 1.00 42.19  ? 352 ARG   A NH1 1 
ATOM   2434 N NH2 . ARG   A 1 352 ? -19.938 -38.570 -44.450 1.00 40.64  ? 352 ARG   A NH2 1 
ATOM   2435 N N   . ALA   A 1 353 ? -23.818 -35.596 -39.313 1.00 44.12  ? 353 ALA   A N   1 
ATOM   2436 C CA  . ALA   A 1 353 ? -25.014 -35.917 -38.539 1.00 42.68  ? 353 ALA   A CA  1 
ATOM   2437 C C   . ALA   A 1 353 ? -25.392 -34.772 -37.610 1.00 45.46  ? 353 ALA   A C   1 
ATOM   2438 O O   . ALA   A 1 353 ? -26.579 -34.511 -37.384 1.00 44.27  ? 353 ALA   A O   1 
ATOM   2439 C CB  . ALA   A 1 353 ? -24.797 -37.201 -37.739 1.00 40.17  ? 353 ALA   A CB  1 
ATOM   2440 N N   . PHE   A 1 354 ? -24.397 -34.071 -37.069 1.00 45.28  ? 354 PHE   A N   1 
ATOM   2441 C CA  . PHE   A 1 354 ? -24.678 -32.949 -36.184 1.00 43.88  ? 354 PHE   A CA  1 
ATOM   2442 C C   . PHE   A 1 354 ? -25.124 -31.714 -36.953 1.00 45.70  ? 354 PHE   A C   1 
ATOM   2443 O O   . PHE   A 1 354 ? -25.858 -30.884 -36.406 1.00 45.84  ? 354 PHE   A O   1 
ATOM   2444 C CB  . PHE   A 1 354 ? -23.450 -32.642 -35.333 1.00 42.70  ? 354 PHE   A CB  1 
ATOM   2445 C CG  . PHE   A 1 354 ? -23.426 -33.389 -34.035 1.00 39.95  ? 354 PHE   A CG  1 
ATOM   2446 C CD1 . PHE   A 1 354 ? -24.378 -33.145 -33.060 1.00 42.97  ? 354 PHE   A CD1 1 
ATOM   2447 C CD2 . PHE   A 1 354 ? -22.473 -34.362 -33.805 1.00 41.15  ? 354 PHE   A CD2 1 
ATOM   2448 C CE1 . PHE   A 1 354 ? -24.364 -33.844 -31.866 1.00 43.29  ? 354 PHE   A CE1 1 
ATOM   2449 C CE2 . PHE   A 1 354 ? -22.454 -35.063 -32.617 1.00 43.61  ? 354 PHE   A CE2 1 
ATOM   2450 C CZ  . PHE   A 1 354 ? -23.402 -34.805 -31.644 1.00 43.33  ? 354 PHE   A CZ  1 
ATOM   2451 N N   . ASP   A 1 355 ? -24.707 -31.575 -38.215 1.00 46.95  ? 355 ASP   A N   1 
ATOM   2452 C CA  . ASP   A 1 355 ? -25.253 -30.504 -39.043 1.00 48.82  ? 355 ASP   A CA  1 
ATOM   2453 C C   . ASP   A 1 355 ? -26.744 -30.702 -39.277 1.00 47.17  ? 355 ASP   A C   1 
ATOM   2454 O O   . ASP   A 1 355 ? -27.513 -29.734 -39.265 1.00 49.18  ? 355 ASP   A O   1 
ATOM   2455 C CB  . ASP   A 1 355 ? -24.510 -30.420 -40.376 1.00 48.94  ? 355 ASP   A CB  1 
ATOM   2456 C CG  . ASP   A 1 355 ? -23.034 -30.136 -40.204 1.00 52.09  ? 355 ASP   A CG  1 
ATOM   2457 O OD1 . ASP   A 1 355 ? -22.657 -29.562 -39.159 1.00 60.33  ? 355 ASP   A OD1 1 
ATOM   2458 O OD2 . ASP   A 1 355 ? -22.252 -30.476 -41.117 1.00 52.68  ? 355 ASP   A OD2 1 
ATOM   2459 N N   . ARG   A 1 356 ? -27.174 -31.951 -39.486 1.00 45.69  ? 356 ARG   A N   1 
ATOM   2460 C CA  . ARG   A 1 356 ? -28.596 -32.209 -39.682 1.00 49.57  ? 356 ARG   A CA  1 
ATOM   2461 C C   . ARG   A 1 356 ? -29.379 -31.957 -38.401 1.00 46.79  ? 356 ARG   A C   1 
ATOM   2462 O O   . ARG   A 1 356 ? -30.487 -31.409 -38.443 1.00 48.85  ? 356 ARG   A O   1 
ATOM   2463 C CB  . ARG   A 1 356 ? -28.823 -33.640 -40.176 1.00 50.95  ? 356 ARG   A CB  1 
ATOM   2464 C CG  . ARG   A 1 356 ? -27.729 -34.187 -41.083 1.00 54.88  ? 356 ARG   A CG  1 
ATOM   2465 C CD  . ARG   A 1 356 ? -27.597 -33.397 -42.379 1.00 60.55  ? 356 ARG   A CD  1 
ATOM   2466 N NE  . ARG   A 1 356 ? -26.200 -33.136 -42.712 1.00 58.32  ? 356 ARG   A NE  1 
ATOM   2467 C CZ  . ARG   A 1 356 ? -25.788 -32.179 -43.534 1.00 60.40  ? 356 ARG   A CZ  1 
ATOM   2468 N NH1 . ARG   A 1 356 ? -26.644 -31.376 -44.146 1.00 60.64  ? 356 ARG   A NH1 1 
ATOM   2469 N NH2 . ARG   A 1 356 ? -24.483 -32.021 -43.743 1.00 58.56  ? 356 ARG   A NH2 1 
ATOM   2470 N N   . LEU   A 1 357 ? -28.822 -32.347 -37.253 1.00 44.45  ? 357 LEU   A N   1 
ATOM   2471 C CA  . LEU   A 1 357 ? -29.487 -32.058 -35.987 1.00 44.66  ? 357 LEU   A CA  1 
ATOM   2472 C C   . LEU   A 1 357 ? -29.611 -30.557 -35.766 1.00 44.19  ? 357 LEU   A C   1 
ATOM   2473 O O   . LEU   A 1 357 ? -30.654 -30.072 -35.310 1.00 41.43  ? 357 LEU   A O   1 
ATOM   2474 C CB  . LEU   A 1 357 ? -28.732 -32.713 -34.832 1.00 43.69  ? 357 LEU   A CB  1 
ATOM   2475 C CG  . LEU   A 1 357 ? -29.177 -32.279 -33.433 1.00 41.01  ? 357 LEU   A CG  1 
ATOM   2476 C CD1 . LEU   A 1 357 ? -30.520 -32.900 -33.073 1.00 45.09  ? 357 LEU   A CD1 1 
ATOM   2477 C CD2 . LEU   A 1 357 ? -28.122 -32.632 -32.397 1.00 41.04  ? 357 LEU   A CD2 1 
ATOM   2478 N N   . PHE   A 1 358 ? -28.568 -29.804 -36.107 1.00 45.60  ? 358 PHE   A N   1 
ATOM   2479 C CA  . PHE   A 1 358 ? -28.564 -28.364 -35.896 1.00 43.18  ? 358 PHE   A CA  1 
ATOM   2480 C C   . PHE   A 1 358 ? -29.384 -27.611 -36.934 1.00 47.32  ? 358 PHE   A C   1 
ATOM   2481 O O   . PHE   A 1 358 ? -29.461 -26.380 -36.864 1.00 47.28  ? 358 PHE   A O   1 
ATOM   2482 C CB  . PHE   A 1 358 ? -27.118 -27.850 -35.867 1.00 43.43  ? 358 PHE   A CB  1 
ATOM   2483 C CG  . PHE   A 1 358 ? -26.461 -27.996 -34.518 1.00 41.28  ? 358 PHE   A CG  1 
ATOM   2484 C CD1 . PHE   A 1 358 ? -27.052 -27.458 -33.387 1.00 41.32  ? 358 PHE   A CD1 1 
ATOM   2485 C CD2 . PHE   A 1 358 ? -25.278 -28.706 -34.378 1.00 39.45  ? 358 PHE   A CD2 1 
ATOM   2486 C CE1 . PHE   A 1 358 ? -26.466 -27.606 -32.142 1.00 41.51  ? 358 PHE   A CE1 1 
ATOM   2487 C CE2 . PHE   A 1 358 ? -24.684 -28.858 -33.138 1.00 41.54  ? 358 PHE   A CE2 1 
ATOM   2488 C CZ  . PHE   A 1 358 ? -25.281 -28.309 -32.016 1.00 39.98  ? 358 PHE   A CZ  1 
ATOM   2489 N N   . GLU   A 1 359 ? -30.001 -28.316 -37.888 1.00 48.44  ? 359 GLU   A N   1 
ATOM   2490 C CA  . GLU   A 1 359 ? -31.011 -27.696 -38.739 1.00 48.85  ? 359 GLU   A CA  1 
ATOM   2491 C C   . GLU   A 1 359 ? -32.330 -27.505 -38.006 1.00 49.98  ? 359 GLU   A C   1 
ATOM   2492 O O   . GLU   A 1 359 ? -33.096 -26.595 -38.341 1.00 50.86  ? 359 GLU   A O   1 
ATOM   2493 C CB  . GLU   A 1 359 ? -31.251 -28.531 -39.997 1.00 48.72  ? 359 GLU   A CB  1 
ATOM   2494 C CG  . GLU   A 1 359 ? -30.059 -28.672 -40.924 1.00 51.34  ? 359 GLU   A CG  1 
ATOM   2495 C CD  . GLU   A 1 359 ? -30.323 -29.665 -42.039 1.00 59.68  ? 359 GLU   A CD  1 
ATOM   2496 O OE1 . GLU   A 1 359 ? -31.510 -29.966 -42.295 1.00 63.06  ? 359 GLU   A OE1 1 
ATOM   2497 O OE2 . GLU   A 1 359 ? -29.350 -30.142 -42.660 1.00 58.69  ? 359 GLU   A OE2 1 
ATOM   2498 N N   . SER   A 1 360 ? -32.607 -28.345 -37.010 1.00 48.69  ? 360 SER   A N   1 
ATOM   2499 C CA  . SER   A 1 360 ? -33.846 -28.284 -36.249 1.00 49.67  ? 360 SER   A CA  1 
ATOM   2500 C C   . SER   A 1 360 ? -33.686 -27.597 -34.900 1.00 49.31  ? 360 SER   A C   1 
ATOM   2501 O O   . SER   A 1 360 ? -34.694 -27.232 -34.287 1.00 49.65  ? 360 SER   A O   1 
ATOM   2502 C CB  . SER   A 1 360 ? -34.398 -29.698 -36.032 1.00 45.76  ? 360 SER   A CB  1 
ATOM   2503 O OG  . SER   A 1 360 ? -34.835 -30.267 -37.250 1.00 48.50  ? 360 SER   A OG  1 
ATOM   2504 N N   . PHE   A 1 361 ? -32.457 -27.411 -34.429 1.00 49.87  ? 361 PHE   A N   1 
ATOM   2505 C CA  . PHE   A 1 361 ? -32.209 -26.880 -33.099 1.00 47.44  ? 361 PHE   A CA  1 
ATOM   2506 C C   . PHE   A 1 361 ? -31.147 -25.795 -33.161 1.00 45.62  ? 361 PHE   A C   1 
ATOM   2507 O O   . PHE   A 1 361 ? -30.236 -25.840 -33.992 1.00 49.68  ? 361 PHE   A O   1 
ATOM   2508 C CB  . PHE   A 1 361 ? -31.757 -27.985 -32.140 1.00 45.85  ? 361 PHE   A CB  1 
ATOM   2509 C CG  . PHE   A 1 361 ? -32.804 -29.023 -31.889 1.00 47.23  ? 361 PHE   A CG  1 
ATOM   2510 C CD1 . PHE   A 1 361 ? -33.810 -28.808 -30.960 1.00 47.34  ? 361 PHE   A CD1 1 
ATOM   2511 C CD2 . PHE   A 1 361 ? -32.794 -30.213 -32.598 1.00 47.29  ? 361 PHE   A CD2 1 
ATOM   2512 C CE1 . PHE   A 1 361 ? -34.784 -29.773 -30.735 1.00 46.06  ? 361 PHE   A CE1 1 
ATOM   2513 C CE2 . PHE   A 1 361 ? -33.760 -31.177 -32.380 1.00 44.22  ? 361 PHE   A CE2 1 
ATOM   2514 C CZ  . PHE   A 1 361 ? -34.757 -30.958 -31.448 1.00 43.58  ? 361 PHE   A CZ  1 
ATOM   2515 N N   . ASP   A 1 362 ? -31.271 -24.818 -32.265 1.00 44.79  ? 362 ASP   A N   1 
ATOM   2516 C CA  . ASP   A 1 362 ? -30.251 -23.787 -32.132 1.00 46.57  ? 362 ASP   A CA  1 
ATOM   2517 C C   . ASP   A 1 362 ? -29.205 -24.134 -31.082 1.00 48.14  ? 362 ASP   A C   1 
ATOM   2518 O O   . ASP   A 1 362 ? -28.071 -23.649 -31.168 1.00 48.71  ? 362 ASP   A O   1 
ATOM   2519 C CB  . ASP   A 1 362 ? -30.896 -22.442 -31.783 1.00 50.97  ? 362 ASP   A CB  1 
ATOM   2520 C CG  . ASP   A 1 362 ? -31.940 -22.007 -32.802 1.00 53.94  ? 362 ASP   A CG  1 
ATOM   2521 O OD1 . ASP   A 1 362 ? -31.573 -21.763 -33.973 1.00 52.74  ? 362 ASP   A OD1 1 
ATOM   2522 O OD2 . ASP   A 1 362 ? -33.133 -21.916 -32.431 1.00 52.27  ? 362 ASP   A OD2 1 
ATOM   2523 N N   . ALA   A 1 363 ? -29.547 -24.973 -30.104 1.00 43.65  ? 363 ALA   A N   1 
ATOM   2524 C CA  . ALA   A 1 363 ? -28.609 -25.306 -29.042 1.00 46.00  ? 363 ALA   A CA  1 
ATOM   2525 C C   . ALA   A 1 363 ? -29.032 -26.594 -28.351 1.00 45.44  ? 363 ALA   A C   1 
ATOM   2526 O O   . ALA   A 1 363 ? -30.218 -26.930 -28.300 1.00 46.67  ? 363 ALA   A O   1 
ATOM   2527 C CB  . ALA   A 1 363 ? -28.511 -24.178 -28.010 1.00 43.33  ? 363 ALA   A CB  1 
ATOM   2528 N N   . ILE   A 1 364 ? -28.043 -27.304 -27.817 1.00 46.59  ? 364 ILE   A N   1 
ATOM   2529 C CA  . ILE   A 1 364 ? -28.274 -28.435 -26.927 1.00 43.23  ? 364 ILE   A CA  1 
ATOM   2530 C C   . ILE   A 1 364 ? -28.021 -27.970 -25.502 1.00 41.97  ? 364 ILE   A C   1 
ATOM   2531 O O   . ILE   A 1 364 ? -26.993 -27.341 -25.220 1.00 41.76  ? 364 ILE   A O   1 
ATOM   2532 C CB  . ILE   A 1 364 ? -27.368 -29.628 -27.277 1.00 40.46  ? 364 ILE   A CB  1 
ATOM   2533 C CG1 . ILE   A 1 364 ? -27.637 -30.114 -28.700 1.00 43.18  ? 364 ILE   A CG1 1 
ATOM   2534 C CG2 . ILE   A 1 364 ? -27.575 -30.761 -26.273 1.00 41.62  ? 364 ILE   A CG2 1 
ATOM   2535 C CD1 . ILE   A 1 364 ? -26.637 -31.137 -29.190 1.00 43.43  ? 364 ILE   A CD1 1 
ATOM   2536 N N   . PHE   A 1 365 ? -28.955 -28.267 -24.606 1.00 42.47  ? 365 PHE   A N   1 
ATOM   2537 C CA  . PHE   A 1 365 ? -28.766 -28.044 -23.179 1.00 42.69  ? 365 PHE   A CA  1 
ATOM   2538 C C   . PHE   A 1 365 ? -28.509 -29.393 -22.520 1.00 41.38  ? 365 PHE   A C   1 
ATOM   2539 O O   . PHE   A 1 365 ? -29.327 -30.310 -22.641 1.00 45.22  ? 365 PHE   A O   1 
ATOM   2540 C CB  . PHE   A 1 365 ? -29.984 -27.360 -22.557 1.00 40.94  ? 365 PHE   A CB  1 
ATOM   2541 C CG  . PHE   A 1 365 ? -30.021 -25.870 -22.763 1.00 42.42  ? 365 PHE   A CG  1 
ATOM   2542 C CD1 . PHE   A 1 365 ? -29.272 -25.271 -23.764 1.00 40.37  ? 365 PHE   A CD1 1 
ATOM   2543 C CD2 . PHE   A 1 365 ? -30.809 -25.069 -21.952 1.00 41.29  ? 365 PHE   A CD2 1 
ATOM   2544 C CE1 . PHE   A 1 365 ? -29.310 -23.902 -23.956 1.00 38.11  ? 365 PHE   A CE1 1 
ATOM   2545 C CE2 . PHE   A 1 365 ? -30.850 -23.700 -22.138 1.00 42.15  ? 365 PHE   A CE2 1 
ATOM   2546 C CZ  . PHE   A 1 365 ? -30.099 -23.117 -23.143 1.00 40.27  ? 365 PHE   A CZ  1 
ATOM   2547 N N   . CYS   A 1 366 ? -27.377 -29.517 -21.837 1.00 41.73  ? 366 CYS   A N   1 
ATOM   2548 C CA  . CYS   A 1 366 ? -26.987 -30.788 -21.243 1.00 42.10  ? 366 CYS   A CA  1 
ATOM   2549 C C   . CYS   A 1 366 ? -26.000 -30.510 -20.117 1.00 41.62  ? 366 CYS   A C   1 
ATOM   2550 O O   . CYS   A 1 366 ? -25.441 -29.409 -20.037 1.00 39.65  ? 366 CYS   A O   1 
ATOM   2551 C CB  . CYS   A 1 366 ? -26.369 -31.726 -22.295 1.00 40.14  ? 366 CYS   A CB  1 
ATOM   2552 S SG  . CYS   A 1 366 ? -24.717 -31.261 -22.850 1.00 45.02  ? 366 CYS   A SG  1 
ATOM   2553 N N   . PRO   A 1 367 ? -25.772 -31.478 -19.226 1.00 39.88  ? 367 PRO   A N   1 
ATOM   2554 C CA  . PRO   A 1 367 ? -24.785 -31.270 -18.161 1.00 37.60  ? 367 PRO   A CA  1 
ATOM   2555 C C   . PRO   A 1 367 ? -23.384 -31.107 -18.729 1.00 38.19  ? 367 PRO   A C   1 
ATOM   2556 O O   . PRO   A 1 367 ? -23.079 -31.562 -19.834 1.00 38.11  ? 367 PRO   A O   1 
ATOM   2557 C CB  . PRO   A 1 367 ? -24.897 -32.547 -17.317 1.00 37.98  ? 367 PRO   A CB  1 
ATOM   2558 C CG  . PRO   A 1 367 ? -26.252 -33.095 -17.630 1.00 40.73  ? 367 PRO   A CG  1 
ATOM   2559 C CD  . PRO   A 1 367 ? -26.468 -32.769 -19.075 1.00 40.46  ? 367 PRO   A CD  1 
ATOM   2560 N N   . VAL   A 1 368 ? -22.532 -30.426 -17.963 1.00 35.41  ? 368 VAL   A N   1 
ATOM   2561 C CA  . VAL   A 1 368 ? -21.103 -30.444 -18.252 1.00 38.56  ? 368 VAL   A CA  1 
ATOM   2562 C C   . VAL   A 1 368 ? -20.502 -31.771 -17.810 1.00 36.83  ? 368 VAL   A C   1 
ATOM   2563 O O   . VAL   A 1 368 ? -19.783 -32.435 -18.568 1.00 36.48  ? 368 VAL   A O   1 
ATOM   2564 C CB  . VAL   A 1 368 ? -20.398 -29.251 -17.577 1.00 37.04  ? 368 VAL   A CB  1 
ATOM   2565 C CG1 . VAL   A 1 368 ? -18.889 -29.355 -17.771 1.00 34.30  ? 368 VAL   A CG1 1 
ATOM   2566 C CG2 . VAL   A 1 368 ? -20.923 -27.932 -18.123 1.00 33.70  ? 368 VAL   A CG2 1 
ATOM   2567 N N   . LEU   A 1 369 ? -20.804 -32.173 -16.578 1.00 36.72  ? 369 LEU   A N   1 
ATOM   2568 C CA  . LEU   A 1 369 ? -20.462 -33.482 -16.048 1.00 37.07  ? 369 LEU   A CA  1 
ATOM   2569 C C   . LEU   A 1 369 ? -21.626 -33.951 -15.186 1.00 40.49  ? 369 LEU   A C   1 
ATOM   2570 O O   . LEU   A 1 369 ? -22.485 -33.158 -14.793 1.00 40.39  ? 369 LEU   A O   1 
ATOM   2571 C CB  . LEU   A 1 369 ? -19.168 -33.434 -15.229 1.00 37.86  ? 369 LEU   A CB  1 
ATOM   2572 C CG  . LEU   A 1 369 ? -17.862 -33.693 -15.983 1.00 40.40  ? 369 LEU   A CG  1 
ATOM   2573 C CD1 . LEU   A 1 369 ? -16.753 -34.076 -15.015 1.00 40.16  ? 369 LEU   A CD1 1 
ATOM   2574 C CD2 . LEU   A 1 369 ? -18.039 -34.767 -17.048 1.00 40.57  ? 369 LEU   A CD2 1 
ATOM   2575 N N   . GLY   A 1 370 ? -21.649 -35.250 -14.885 1.00 39.84  ? 370 GLY   A N   1 
ATOM   2576 C CA  . GLY   A 1 370 ? -22.764 -35.811 -14.143 1.00 39.33  ? 370 GLY   A CA  1 
ATOM   2577 C C   . GLY   A 1 370 ? -22.880 -35.338 -12.706 1.00 40.07  ? 370 GLY   A C   1 
ATOM   2578 O O   . GLY   A 1 370 ? -23.960 -35.453 -12.118 1.00 39.78  ? 370 GLY   A O   1 
ATOM   2579 N N   . THR   A 1 371 ? -21.805 -34.807 -12.125 1.00 42.99  ? 371 THR   A N   1 
ATOM   2580 C CA  . THR   A 1 371 ? -21.820 -34.415 -10.722 1.00 45.07  ? 371 THR   A CA  1 
ATOM   2581 C C   . THR   A 1 371 ? -20.894 -33.221 -10.515 1.00 41.71  ? 371 THR   A C   1 
ATOM   2582 O O   . THR   A 1 371 ? -20.209 -32.766 -11.436 1.00 39.45  ? 371 THR   A O   1 
ATOM   2583 C CB  . THR   A 1 371 ? -21.421 -35.588 -9.816  1.00 45.17  ? 371 THR   A CB  1 
ATOM   2584 O OG1 . THR   A 1 371 ? -21.706 -35.263 -8.449  1.00 47.40  ? 371 THR   A OG1 1 
ATOM   2585 C CG2 . THR   A 1 371 ? -19.940 -35.901 -9.963  1.00 41.58  ? 371 THR   A CG2 1 
ATOM   2586 N N   . THR   A 1 372 ? -20.880 -32.719 -9.281  1.00 43.88  ? 372 THR   A N   1 
ATOM   2587 C CA  . THR   A 1 372 ? -20.061 -31.577 -8.906  1.00 42.49  ? 372 THR   A CA  1 
ATOM   2588 C C   . THR   A 1 372 ? -18.617 -32.020 -8.648  1.00 39.11  ? 372 THR   A C   1 
ATOM   2589 O O   . THR   A 1 372 ? -18.256 -33.187 -8.819  1.00 41.82  ? 372 THR   A O   1 
ATOM   2590 C CB  . THR   A 1 372 ? -20.662 -30.882 -7.684  1.00 43.73  ? 372 THR   A CB  1 
ATOM   2591 O OG1 . THR   A 1 372 ? -20.912 -31.843 -6.649  1.00 43.92  ? 372 THR   A OG1 1 
ATOM   2592 C CG2 . THR   A 1 372 ? -21.971 -30.209 -8.051  1.00 38.81  ? 372 THR   A CG2 1 
ATOM   2593 N N   . ALA   A 1 373 ? -17.778 -31.069 -8.235  1.00 38.66  ? 373 ALA   A N   1 
ATOM   2594 C CA  . ALA   A 1 373 ? -16.358 -31.341 -8.027  1.00 39.24  ? 373 ALA   A CA  1 
ATOM   2595 C C   . ALA   A 1 373 ? -16.147 -32.436 -6.986  1.00 38.82  ? 373 ALA   A C   1 
ATOM   2596 O O   . ALA   A 1 373 ? -16.707 -32.385 -5.887  1.00 37.80  ? 373 ALA   A O   1 
ATOM   2597 C CB  . ALA   A 1 373 ? -15.640 -30.062 -7.595  1.00 36.52  ? 373 ALA   A CB  1 
ATOM   2598 N N   . PHE   A 1 374 ? -15.326 -33.422 -7.334  1.00 38.29  ? 374 PHE   A N   1 
ATOM   2599 C CA  . PHE   A 1 374 ? -15.058 -34.555 -6.459  1.00 40.14  ? 374 PHE   A CA  1 
ATOM   2600 C C   . PHE   A 1 374 ? -13.886 -34.259 -5.529  1.00 40.97  ? 374 PHE   A C   1 
ATOM   2601 O O   . PHE   A 1 374 ? -13.056 -33.384 -5.788  1.00 40.62  ? 374 PHE   A O   1 
ATOM   2602 C CB  . PHE   A 1 374 ? -14.761 -35.814 -7.276  1.00 40.15  ? 374 PHE   A CB  1 
ATOM   2603 C CG  . PHE   A 1 374 ? -13.748 -35.608 -8.371  1.00 39.84  ? 374 PHE   A CG  1 
ATOM   2604 C CD1 . PHE   A 1 374 ? -12.391 -35.730 -8.112  1.00 39.51  ? 374 PHE   A CD1 1 
ATOM   2605 C CD2 . PHE   A 1 374 ? -14.153 -35.300 -9.660  1.00 36.53  ? 374 PHE   A CD2 1 
ATOM   2606 C CE1 . PHE   A 1 374 ? -11.457 -35.543 -9.117  1.00 38.66  ? 374 PHE   A CE1 1 
ATOM   2607 C CE2 . PHE   A 1 374 ? -13.226 -35.114 -10.668 1.00 37.31  ? 374 PHE   A CE2 1 
ATOM   2608 C CZ  . PHE   A 1 374 ? -11.876 -35.237 -10.396 1.00 39.55  ? 374 PHE   A CZ  1 
ATOM   2609 N N   . ALA   A 1 375 ? -13.826 -35.012 -4.433  1.00 40.44  ? 375 ALA   A N   1 
ATOM   2610 C CA  . ALA   A 1 375 ? -12.720 -34.869 -3.498  1.00 42.06  ? 375 ALA   A CA  1 
ATOM   2611 C C   . ALA   A 1 375 ? -11.406 -35.261 -4.169  1.00 38.78  ? 375 ALA   A C   1 
ATOM   2612 O O   . ALA   A 1 375 ? -11.372 -36.092 -5.080  1.00 40.26  ? 375 ALA   A O   1 
ATOM   2613 C CB  . ALA   A 1 375 ? -12.958 -35.722 -2.250  1.00 41.74  ? 375 ALA   A CB  1 
ATOM   2614 N N   . HIS   A 1 376 ? -10.320 -34.637 -3.714  1.00 39.32  ? 376 HIS   A N   1 
ATOM   2615 C CA  . HIS   A 1 376 ? -9.000  -34.863 -4.293  1.00 39.56  ? 376 HIS   A CA  1 
ATOM   2616 C C   . HIS   A 1 376 ? -8.675  -36.348 -4.353  1.00 41.74  ? 376 HIS   A C   1 
ATOM   2617 O O   . HIS   A 1 376 ? -8.884  -37.084 -3.384  1.00 40.88  ? 376 HIS   A O   1 
ATOM   2618 C CB  . HIS   A 1 376 ? -7.935  -34.136 -3.472  1.00 40.61  ? 376 HIS   A CB  1 
ATOM   2619 C CG  . HIS   A 1 376 ? -8.137  -32.657 -3.390  1.00 41.40  ? 376 HIS   A CG  1 
ATOM   2620 N ND1 . HIS   A 1 376 ? -8.160  -31.846 -4.504  1.00 41.02  ? 376 HIS   A ND1 1 
ATOM   2621 C CD2 . HIS   A 1 376 ? -8.335  -31.843 -2.327  1.00 40.76  ? 376 HIS   A CD2 1 
ATOM   2622 C CE1 . HIS   A 1 376 ? -8.357  -30.594 -4.129  1.00 40.45  ? 376 HIS   A CE1 1 
ATOM   2623 N NE2 . HIS   A 1 376 ? -8.466  -30.565 -2.813  1.00 37.62  ? 376 HIS   A NE2 1 
ATOM   2624 N N   . SER   A 1 377 ? -8.165  -36.783 -5.499  1.00 43.27  ? 377 SER   A N   1 
ATOM   2625 C CA  . SER   A 1 377 ? -7.787  -38.171 -5.713  1.00 43.74  ? 377 SER   A CA  1 
ATOM   2626 C C   . SER   A 1 377 ? -6.310  -38.242 -6.063  1.00 44.52  ? 377 SER   A C   1 
ATOM   2627 O O   . SER   A 1 377 ? -5.833  -37.494 -6.922  1.00 41.04  ? 377 SER   A O   1 
ATOM   2628 C CB  . SER   A 1 377 ? -8.623  -38.808 -6.824  1.00 43.46  ? 377 SER   A CB  1 
ATOM   2629 O OG  . SER   A 1 377 ? -7.917  -39.877 -7.428  1.00 43.36  ? 377 SER   A OG  1 
ATOM   2630 N N   . ASP   A 1 378 ? -5.589  -39.134 -5.392  1.00 48.15  ? 378 ASP   A N   1 
ATOM   2631 C CA  . ASP   A 1 378 ? -4.193  -39.390 -5.705  1.00 48.69  ? 378 ASP   A CA  1 
ATOM   2632 C C   . ASP   A 1 378 ? -4.024  -40.551 -6.674  1.00 46.56  ? 378 ASP   A C   1 
ATOM   2633 O O   . ASP   A 1 378 ? -2.893  -40.977 -6.922  1.00 49.06  ? 378 ASP   A O   1 
ATOM   2634 C CB  . ASP   A 1 378 ? -3.406  -39.660 -4.420  1.00 46.49  ? 378 ASP   A CB  1 
ATOM   2635 C CG  . ASP   A 1 378 ? -3.892  -40.893 -3.689  1.00 53.63  ? 378 ASP   A CG  1 
ATOM   2636 O OD1 . ASP   A 1 378 ? -5.053  -41.300 -3.908  1.00 51.01  ? 378 ASP   A OD1 1 
ATOM   2637 O OD2 . ASP   A 1 378 ? -3.110  -41.457 -2.893  1.00 62.20  ? 378 ASP   A OD2 1 
ATOM   2638 N N   . GLU   A 1 379 ? -5.122  -41.065 -7.226  1.00 47.43  ? 379 GLU   A N   1 
ATOM   2639 C CA  . GLU   A 1 379 ? -5.073  -42.225 -8.104  1.00 48.09  ? 379 GLU   A CA  1 
ATOM   2640 C C   . GLU   A 1 379 ? -4.975  -41.761 -9.552  1.00 49.52  ? 379 GLU   A C   1 
ATOM   2641 O O   . GLU   A 1 379 ? -5.941  -41.183 -10.072 1.00 49.53  ? 379 GLU   A O   1 
ATOM   2642 C CB  . GLU   A 1 379 ? -6.306  -43.093 -7.907  1.00 47.63  ? 379 GLU   A CB  1 
ATOM   2643 C CG  . GLU   A 1 379 ? -6.449  -44.176 -8.948  1.00 49.11  ? 379 GLU   A CG  1 
ATOM   2644 C CD  . GLU   A 1 379 ? -5.355  -45.219 -8.827  1.00 50.63  ? 379 GLU   A CD  1 
ATOM   2645 O OE1 . GLU   A 1 379 ? -5.214  -45.816 -7.737  1.00 51.80  ? 379 GLU   A OE1 1 
ATOM   2646 O OE2 . GLU   A 1 379 ? -4.617  -45.423 -9.813  1.00 48.83  ? 379 GLU   A OE2 1 
ATOM   2647 N N   . PRO   A 1 380 ? -3.854  -41.994 -10.241 1.00 52.18  ? 380 PRO   A N   1 
ATOM   2648 C CA  . PRO   A 1 380 ? -3.746  -41.553 -11.643 1.00 48.14  ? 380 PRO   A CA  1 
ATOM   2649 C C   . PRO   A 1 380 ? -4.570  -42.377 -12.625 1.00 52.38  ? 380 PRO   A C   1 
ATOM   2650 O O   . PRO   A 1 380 ? -4.889  -41.869 -13.709 1.00 52.85  ? 380 PRO   A O   1 
ATOM   2651 C CB  . PRO   A 1 380 ? -2.247  -41.694 -11.936 1.00 50.32  ? 380 PRO   A CB  1 
ATOM   2652 C CG  . PRO   A 1 380 ? -1.790  -42.759 -10.983 1.00 47.77  ? 380 PRO   A CG  1 
ATOM   2653 C CD  . PRO   A 1 380 ? -2.581  -42.529 -9.732  1.00 49.05  ? 380 PRO   A CD  1 
ATOM   2654 N N   . ASP   A 1 381 ? -4.914  -43.622 -12.296 1.00 51.00  ? 381 ASP   A N   1 
ATOM   2655 C CA  . ASP   A 1 381 ? -5.629  -44.503 -13.214 1.00 52.58  ? 381 ASP   A CA  1 
ATOM   2656 C C   . ASP   A 1 381 ? -7.131  -44.273 -13.073 1.00 50.46  ? 381 ASP   A C   1 
ATOM   2657 O O   . ASP   A 1 381 ? -7.708  -44.542 -12.013 1.00 48.54  ? 381 ASP   A O   1 
ATOM   2658 C CB  . ASP   A 1 381 ? -5.271  -45.966 -12.944 1.00 51.34  ? 381 ASP   A CB  1 
ATOM   2659 C CG  . ASP   A 1 381 ? -5.897  -46.927 -13.952 1.00 56.01  ? 381 ASP   A CG  1 
ATOM   2660 O OD1 . ASP   A 1 381 ? -6.425  -46.463 -14.983 1.00 56.45  ? 381 ASP   A OD1 1 
ATOM   2661 O OD2 . ASP   A 1 381 ? -5.855  -48.155 -13.716 1.00 60.40  ? 381 ASP   A OD2 1 
ATOM   2662 N N   . TRP   A 1 382 ? -7.764  -43.796 -14.150 1.00 49.60  ? 382 TRP   A N   1 
ATOM   2663 C CA  . TRP   A 1 382 ? -9.186  -43.467 -14.092 1.00 49.19  ? 382 TRP   A CA  1 
ATOM   2664 C C   . TRP   A 1 382 ? -10.048 -44.695 -13.829 1.00 49.56  ? 382 TRP   A C   1 
ATOM   2665 O O   . TRP   A 1 382 ? -11.118 -44.580 -13.221 1.00 48.18  ? 382 TRP   A O   1 
ATOM   2666 C CB  . TRP   A 1 382 ? -9.629  -42.782 -15.387 1.00 47.67  ? 382 TRP   A CB  1 
ATOM   2667 C CG  . TRP   A 1 382 ? -9.313  -41.319 -15.429 1.00 49.54  ? 382 TRP   A CG  1 
ATOM   2668 C CD1 . TRP   A 1 382 ? -8.276  -40.689 -14.807 1.00 46.14  ? 382 TRP   A CD1 1 
ATOM   2669 C CD2 . TRP   A 1 382 ? -10.041 -40.298 -16.127 1.00 47.10  ? 382 TRP   A CD2 1 
ATOM   2670 N NE1 . TRP   A 1 382 ? -8.311  -39.343 -15.074 1.00 45.26  ? 382 TRP   A NE1 1 
ATOM   2671 C CE2 . TRP   A 1 382 ? -9.385  -39.077 -15.881 1.00 45.06  ? 382 TRP   A CE2 1 
ATOM   2672 C CE3 . TRP   A 1 382 ? -11.184 -40.300 -16.933 1.00 48.92  ? 382 TRP   A CE3 1 
ATOM   2673 C CZ2 . TRP   A 1 382 ? -9.832  -37.867 -16.414 1.00 43.45  ? 382 TRP   A CZ2 1 
ATOM   2674 C CZ3 . TRP   A 1 382 ? -11.626 -39.095 -17.463 1.00 46.62  ? 382 TRP   A CZ3 1 
ATOM   2675 C CH2 . TRP   A 1 382 ? -10.950 -37.897 -17.201 1.00 42.16  ? 382 TRP   A CH2 1 
ATOM   2676 N N   . ALA   A 1 383 ? -9.608  -45.874 -14.277 1.00 50.47  ? 383 ALA   A N   1 
ATOM   2677 C CA  . ALA   A 1 383 ? -10.359 -47.096 -14.008 1.00 52.51  ? 383 ALA   A CA  1 
ATOM   2678 C C   . ALA   A 1 383 ? -10.399 -47.440 -12.527 1.00 49.83  ? 383 ALA   A C   1 
ATOM   2679 O O   . ALA   A 1 383 ? -11.321 -48.138 -12.092 1.00 48.11  ? 383 ALA   A O   1 
ATOM   2680 C CB  . ALA   A 1 383 ? -9.767  -48.264 -14.790 1.00 55.80  ? 383 ALA   A CB  1 
ATOM   2681 N N   . LYS   A 1 384 ? -9.429  -46.967 -11.751 1.00 49.40  ? 384 LYS   A N   1 
ATOM   2682 C CA  . LYS   A 1 384 ? -9.405  -47.186 -10.312 1.00 50.67  ? 384 LYS   A CA  1 
ATOM   2683 C C   . LYS   A 1 384 ? -10.126 -46.090 -9.541  1.00 50.95  ? 384 LYS   A C   1 
ATOM   2684 O O   . LYS   A 1 384 ? -10.253 -46.197 -8.318  1.00 48.63  ? 384 LYS   A O   1 
ATOM   2685 C CB  . LYS   A 1 384 ? -7.956  -47.303 -9.821  1.00 51.60  ? 384 LYS   A CB  1 
ATOM   2686 C CG  . LYS   A 1 384 ? -7.048  -48.146 -10.710 1.00 50.95  ? 384 LYS   A CG  1 
ATOM   2687 C CD  . LYS   A 1 384 ? -6.769  -49.502 -10.087 1.00 56.42  ? 384 LYS   A CD  1 
ATOM   2688 C CE  . LYS   A 1 384 ? -5.671  -50.252 -10.826 1.00 57.44  ? 384 LYS   A CE  1 
ATOM   2689 N NZ  . LYS   A 1 384 ? -4.456  -50.407 -9.979  1.00 57.60  ? 384 LYS   A NZ  1 
ATOM   2690 N N   . ARG   A 1 385 ? -10.596 -45.049 -10.220 1.00 51.87  ? 385 ARG   A N   1 
ATOM   2691 C CA  . ARG   A 1 385 ? -11.387 -44.013 -9.576  1.00 49.85  ? 385 ARG   A CA  1 
ATOM   2692 C C   . ARG   A 1 385 ? -12.874 -44.340 -9.642  1.00 50.22  ? 385 ARG   A C   1 
ATOM   2693 O O   . ARG   A 1 385 ? -13.327 -45.158 -10.446 1.00 49.82  ? 385 ARG   A O   1 
ATOM   2694 C CB  . ARG   A 1 385 ? -11.164 -42.647 -10.222 1.00 45.90  ? 385 ARG   A CB  1 
ATOM   2695 C CG  . ARG   A 1 385 ? -9.778  -42.076 -10.104 1.00 46.09  ? 385 ARG   A CG  1 
ATOM   2696 C CD  . ARG   A 1 385 ? -9.618  -40.989 -11.145 1.00 43.95  ? 385 ARG   A CD  1 
ATOM   2697 N NE  . ARG   A 1 385 ? -8.270  -40.444 -11.202 1.00 45.22  ? 385 ARG   A NE  1 
ATOM   2698 C CZ  . ARG   A 1 385 ? -7.995  -39.152 -11.307 1.00 45.98  ? 385 ARG   A CZ  1 
ATOM   2699 N NH1 . ARG   A 1 385 ? -8.956  -38.242 -11.334 1.00 44.70  ? 385 ARG   A NH1 1 
ATOM   2700 N NH2 . ARG   A 1 385 ? -6.726  -38.763 -11.393 1.00 47.48  ? 385 ARG   A NH2 1 
ATOM   2701 N N   . SER   A 1 386 ? -13.636 -43.654 -8.796  1.00 50.19  ? 386 SER   A N   1 
ATOM   2702 C CA  . SER   A 1 386 ? -15.080 -43.797 -8.762  1.00 48.78  ? 386 SER   A CA  1 
ATOM   2703 C C   . SER   A 1 386 ? -15.692 -42.473 -8.332  1.00 47.46  ? 386 SER   A C   1 
ATOM   2704 O O   . SER   A 1 386 ? -15.033 -41.635 -7.713  1.00 49.81  ? 386 SER   A O   1 
ATOM   2705 C CB  . SER   A 1 386 ? -15.509 -44.920 -7.816  1.00 54.23  ? 386 SER   A CB  1 
ATOM   2706 O OG  . SER   A 1 386 ? -16.867 -45.257 -8.024  1.00 59.24  ? 386 SER   A OG  1 
ATOM   2707 N N   . LEU   A 1 387 ? -16.967 -42.294 -8.668  1.00 49.08  ? 387 LEU   A N   1 
ATOM   2708 C CA  . LEU   A 1 387 ? -17.706 -41.096 -8.300  1.00 45.66  ? 387 LEU   A CA  1 
ATOM   2709 C C   . LEU   A 1 387 ? -18.968 -41.474 -7.538  1.00 47.90  ? 387 LEU   A C   1 
ATOM   2710 O O   . LEU   A 1 387 ? -19.517 -42.566 -7.711  1.00 48.16  ? 387 LEU   A O   1 
ATOM   2711 C CB  . LEU   A 1 387 ? -18.076 -40.265 -9.532  1.00 39.00  ? 387 LEU   A CB  1 
ATOM   2712 C CG  . LEU   A 1 387 ? -16.908 -39.500 -10.150 1.00 42.34  ? 387 LEU   A CG  1 
ATOM   2713 C CD1 . LEU   A 1 387 ? -17.217 -39.108 -11.583 1.00 42.95  ? 387 LEU   A CD1 1 
ATOM   2714 C CD2 . LEU   A 1 387 ? -16.574 -38.279 -9.314  1.00 41.14  ? 387 LEU   A CD2 1 
ATOM   2715 N N   . SER   A 1 388 ? -19.423 -40.557 -6.690  1.00 45.51  ? 388 SER   A N   1 
ATOM   2716 C CA  . SER   A 1 388 ? -20.655 -40.734 -5.933  1.00 44.77  ? 388 SER   A CA  1 
ATOM   2717 C C   . SER   A 1 388 ? -21.777 -39.977 -6.632  1.00 46.34  ? 388 SER   A C   1 
ATOM   2718 O O   . SER   A 1 388 ? -21.721 -38.749 -6.756  1.00 48.06  ? 388 SER   A O   1 
ATOM   2719 C CB  . SER   A 1 388 ? -20.487 -40.246 -4.494  1.00 46.42  ? 388 SER   A CB  1 
ATOM   2720 O OG  . SER   A 1 388 ? -21.696 -39.695 -4.003  1.00 49.86  ? 388 SER   A OG  1 
ATOM   2721 N N   . ILE   A 1 389 ? -22.789 -40.709 -7.089  1.00 51.54  ? 389 ILE   A N   1 
ATOM   2722 C CA  . ILE   A 1 389 ? -23.935 -40.139 -7.791  1.00 51.41  ? 389 ILE   A CA  1 
ATOM   2723 C C   . ILE   A 1 389 ? -25.158 -40.425 -6.930  1.00 48.27  ? 389 ILE   A C   1 
ATOM   2724 O O   . ILE   A 1 389 ? -25.649 -41.559 -6.893  1.00 50.07  ? 389 ILE   A O   1 
ATOM   2725 C CB  . ILE   A 1 389 ? -24.092 -40.711 -9.206  1.00 46.89  ? 389 ILE   A CB  1 
ATOM   2726 C CG1 . ILE   A 1 389 ? -22.967 -40.201 -10.104 1.00 47.24  ? 389 ILE   A CG1 1 
ATOM   2727 C CG2 . ILE   A 1 389 ? -25.436 -40.329 -9.802  1.00 44.83  ? 389 ILE   A CG2 1 
ATOM   2728 C CD1 . ILE   A 1 389 ? -23.062 -38.729 -10.418 1.00 45.85  ? 389 ILE   A CD1 1 
ATOM   2729 N N   . ASP   A 1 390 ? -25.649 -39.397 -6.233  1.00 49.31  ? 390 ASP   A N   1 
ATOM   2730 C CA  . ASP   A 1 390 ? -26.763 -39.528 -5.292  1.00 51.28  ? 390 ASP   A CA  1 
ATOM   2731 C C   . ASP   A 1 390 ? -26.495 -40.639 -4.278  1.00 54.13  ? 390 ASP   A C   1 
ATOM   2732 O O   . ASP   A 1 390 ? -27.346 -41.486 -3.997  1.00 54.71  ? 390 ASP   A O   1 
ATOM   2733 C CB  . ASP   A 1 390 ? -28.087 -39.762 -6.021  1.00 49.51  ? 390 ASP   A CB  1 
ATOM   2734 C CG  . ASP   A 1 390 ? -28.455 -38.619 -6.951  1.00 51.18  ? 390 ASP   A CG  1 
ATOM   2735 O OD1 . ASP   A 1 390 ? -28.186 -37.451 -6.600  1.00 50.92  ? 390 ASP   A OD1 1 
ATOM   2736 O OD2 . ASP   A 1 390 ? -29.021 -38.888 -8.032  1.00 52.03  ? 390 ASP   A OD2 1 
ATOM   2737 N N   . GLY   A 1 391 ? -25.284 -40.634 -3.726  1.00 53.96  ? 391 GLY   A N   1 
ATOM   2738 C CA  . GLY   A 1 391 ? -24.914 -41.658 -2.773  1.00 56.53  ? 391 GLY   A CA  1 
ATOM   2739 C C   . GLY   A 1 391 ? -24.744 -43.039 -3.361  1.00 59.36  ? 391 GLY   A C   1 
ATOM   2740 O O   . GLY   A 1 391 ? -24.767 -44.026 -2.622  1.00 63.15  ? 391 GLY   A O   1 
ATOM   2741 N N   . GLY   A 1 392 ? -24.590 -43.140 -4.678  1.00 55.65  ? 392 GLY   A N   1 
ATOM   2742 C CA  . GLY   A 1 392 ? -24.304 -44.405 -5.322  1.00 54.25  ? 392 GLY   A CA  1 
ATOM   2743 C C   . GLY   A 1 392 ? -23.016 -44.335 -6.111  1.00 55.06  ? 392 GLY   A C   1 
ATOM   2744 O O   . GLY   A 1 392 ? -22.587 -43.252 -6.516  1.00 54.08  ? 392 GLY   A O   1 
ATOM   2745 N N   . ILE   A 1 393 ? -22.386 -45.477 -6.333  1.00 53.85  ? 393 ILE   A N   1 
ATOM   2746 C CA  . ILE   A 1 393 ? -21.122 -45.522 -7.058  1.00 53.36  ? 393 ILE   A CA  1 
ATOM   2747 C C   . ILE   A 1 393 ? -21.391 -45.435 -8.556  1.00 55.45  ? 393 ILE   A C   1 
ATOM   2748 O O   . ILE   A 1 393 ? -22.356 -46.019 -9.066  1.00 50.60  ? 393 ILE   A O   1 
ATOM   2749 C CB  . ILE   A 1 393 ? -20.347 -46.797 -6.672  1.00 52.63  ? 393 ILE   A CB  1 
ATOM   2750 C CG1 . ILE   A 1 393 ? -19.769 -46.656 -5.258  1.00 53.62  ? 393 ILE   A CG1 1 
ATOM   2751 C CG2 . ILE   A 1 393 ? -19.268 -47.136 -7.690  1.00 51.18  ? 393 ILE   A CG2 1 
ATOM   2752 C CD1 . ILE   A 1 393 ? -18.675 -45.601 -5.138  1.00 53.10  ? 393 ILE   A CD1 1 
ATOM   2753 N N   . ALA   A 1 394 ? -20.560 -44.670 -9.262  1.00 51.66  ? 394 ALA   A N   1 
ATOM   2754 C CA  . ALA   A 1 394 ? -20.609 -44.549 -10.712 1.00 47.27  ? 394 ALA   A CA  1 
ATOM   2755 C C   . ALA   A 1 394 ? -19.195 -44.580 -11.275 1.00 50.29  ? 394 ALA   A C   1 
ATOM   2756 O O   . ALA   A 1 394 ? -18.245 -44.174 -10.593 1.00 47.60  ? 394 ALA   A O   1 
ATOM   2757 C CB  . ALA   A 1 394 ? -21.312 -43.257 -11.154 1.00 48.46  ? 394 ALA   A CB  1 
ATOM   2758 N N   . PRO   A 1 395 ? -19.022 -45.063 -12.509 1.00 45.78  ? 395 PRO   A N   1 
ATOM   2759 C CA  . PRO   A 1 395 ? -17.680 -45.106 -13.105 1.00 45.49  ? 395 PRO   A CA  1 
ATOM   2760 C C   . PRO   A 1 395 ? -17.157 -43.714 -13.429 1.00 45.53  ? 395 PRO   A C   1 
ATOM   2761 O O   . PRO   A 1 395 ? -17.884 -42.859 -13.942 1.00 46.30  ? 395 PRO   A O   1 
ATOM   2762 C CB  . PRO   A 1 395 ? -17.888 -45.930 -14.384 1.00 44.16  ? 395 PRO   A CB  1 
ATOM   2763 C CG  . PRO   A 1 395 ? -19.149 -46.689 -14.141 1.00 45.08  ? 395 PRO   A CG  1 
ATOM   2764 C CD  . PRO   A 1 395 ? -20.006 -45.735 -13.374 1.00 46.62  ? 395 PRO   A CD  1 
ATOM   2765 N N   . PHE   A 1 396 ? -15.871 -43.502 -13.145 1.00 45.55  ? 396 PHE   A N   1 
ATOM   2766 C CA  . PHE   A 1 396 ? -15.263 -42.192 -13.361 1.00 44.89  ? 396 PHE   A CA  1 
ATOM   2767 C C   . PHE   A 1 396 ? -15.123 -41.880 -14.847 1.00 44.59  ? 396 PHE   A C   1 
ATOM   2768 O O   . PHE   A 1 396 ? -15.590 -40.836 -15.320 1.00 45.85  ? 396 PHE   A O   1 
ATOM   2769 C CB  . PHE   A 1 396 ? -13.900 -42.132 -12.667 1.00 43.84  ? 396 PHE   A CB  1 
ATOM   2770 C CG  . PHE   A 1 396 ? -13.331 -40.744 -12.548 1.00 43.20  ? 396 PHE   A CG  1 
ATOM   2771 C CD1 . PHE   A 1 396 ? -12.720 -40.132 -13.633 1.00 43.64  ? 396 PHE   A CD1 1 
ATOM   2772 C CD2 . PHE   A 1 396 ? -13.391 -40.057 -11.347 1.00 44.26  ? 396 PHE   A CD2 1 
ATOM   2773 C CE1 . PHE   A 1 396 ? -12.190 -38.860 -13.526 1.00 43.14  ? 396 PHE   A CE1 1 
ATOM   2774 C CE2 . PHE   A 1 396 ? -12.861 -38.782 -11.231 1.00 42.04  ? 396 PHE   A CE2 1 
ATOM   2775 C CZ  . PHE   A 1 396 ? -12.260 -38.184 -12.323 1.00 42.23  ? 396 PHE   A CZ  1 
ATOM   2776 N N   . ALA   A 1 397 ? -14.470 -42.768 -15.600 1.00 45.72  ? 397 ALA   A N   1 
ATOM   2777 C CA  . ALA   A 1 397 ? -14.145 -42.478 -16.992 1.00 46.30  ? 397 ALA   A CA  1 
ATOM   2778 C C   . ALA   A 1 397 ? -15.377 -42.393 -17.886 1.00 44.61  ? 397 ALA   A C   1 
ATOM   2779 O O   . ALA   A 1 397 ? -15.328 -41.715 -18.918 1.00 43.39  ? 397 ALA   A O   1 
ATOM   2780 C CB  . ALA   A 1 397 ? -13.178 -43.532 -17.531 1.00 47.21  ? 397 ALA   A CB  1 
ATOM   2781 N N   . ALA   A 1 398 ? -16.478 -43.052 -17.514 1.00 44.13  ? 398 ALA   A N   1 
ATOM   2782 C CA  . ALA   A 1 398 ? -17.686 -42.993 -18.331 1.00 41.26  ? 398 ALA   A CA  1 
ATOM   2783 C C   . ALA   A 1 398 ? -18.234 -41.579 -18.445 1.00 45.00  ? 398 ALA   A C   1 
ATOM   2784 O O   . ALA   A 1 398 ? -18.947 -41.280 -19.408 1.00 40.54  ? 398 ALA   A O   1 
ATOM   2785 C CB  . ALA   A 1 398 ? -18.753 -43.925 -17.761 1.00 41.63  ? 398 ALA   A CB  1 
ATOM   2786 N N   . GLN   A 1 399 ? -17.900 -40.699 -17.497 1.00 43.92  ? 399 GLN   A N   1 
ATOM   2787 C CA  . GLN   A 1 399 ? -18.358 -39.315 -17.523 1.00 43.74  ? 399 GLN   A CA  1 
ATOM   2788 C C   . GLN   A 1 399 ? -17.825 -38.534 -18.721 1.00 44.28  ? 399 GLN   A C   1 
ATOM   2789 O O   . GLN   A 1 399 ? -18.353 -37.457 -19.018 1.00 44.78  ? 399 GLN   A O   1 
ATOM   2790 C CB  . GLN   A 1 399 ? -17.955 -38.618 -16.221 1.00 43.55  ? 399 GLN   A CB  1 
ATOM   2791 C CG  . GLN   A 1 399 ? -18.697 -39.120 -14.979 1.00 42.95  ? 399 GLN   A CG  1 
ATOM   2792 C CD  . GLN   A 1 399 ? -20.161 -38.706 -14.958 1.00 43.92  ? 399 GLN   A CD  1 
ATOM   2793 O OE1 . GLN   A 1 399 ? -20.514 -37.612 -15.396 1.00 44.69  ? 399 GLN   A OE1 1 
ATOM   2794 N NE2 . GLN   A 1 399 ? -21.020 -39.582 -14.445 1.00 42.87  ? 399 GLN   A NE2 1 
ATOM   2795 N N   . LEU   A 1 400 ? -16.807 -39.050 -19.415 1.00 44.37  ? 400 LEU   A N   1 
ATOM   2796 C CA  . LEU   A 1 400 ? -16.312 -38.407 -20.629 1.00 44.31  ? 400 LEU   A CA  1 
ATOM   2797 C C   . LEU   A 1 400 ? -17.403 -38.239 -21.681 1.00 43.99  ? 400 LEU   A C   1 
ATOM   2798 O O   . LEU   A 1 400 ? -17.235 -37.444 -22.612 1.00 40.13  ? 400 LEU   A O   1 
ATOM   2799 C CB  . LEU   A 1 400 ? -15.161 -39.228 -21.216 1.00 46.30  ? 400 LEU   A CB  1 
ATOM   2800 C CG  . LEU   A 1 400 ? -13.725 -38.717 -21.086 1.00 49.47  ? 400 LEU   A CG  1 
ATOM   2801 C CD1 . LEU   A 1 400 ? -12.754 -39.765 -21.611 1.00 51.32  ? 400 LEU   A CD1 1 
ATOM   2802 C CD2 . LEU   A 1 400 ? -13.530 -37.392 -21.812 1.00 47.80  ? 400 LEU   A CD2 1 
ATOM   2803 N N   . GLY   A 1 401 ? -18.514 -38.969 -21.544 1.00 44.24  ? 401 GLY   A N   1 
ATOM   2804 C CA  . GLY   A 1 401 ? -19.566 -38.915 -22.546 1.00 43.59  ? 401 GLY   A CA  1 
ATOM   2805 C C   . GLY   A 1 401 ? -20.202 -37.544 -22.682 1.00 42.71  ? 401 GLY   A C   1 
ATOM   2806 O O   . GLY   A 1 401 ? -20.525 -37.112 -23.789 1.00 42.23  ? 401 GLY   A O   1 
ATOM   2807 N N   . TRP   A 1 402 ? -20.410 -36.847 -21.558 1.00 43.41  ? 402 TRP   A N   1 
ATOM   2808 C CA  . TRP   A 1 402 ? -20.956 -35.493 -21.631 1.00 42.09  ? 402 TRP   A CA  1 
ATOM   2809 C C   . TRP   A 1 402 ? -20.035 -34.567 -22.406 1.00 41.03  ? 402 TRP   A C   1 
ATOM   2810 O O   . TRP   A 1 402 ? -20.500 -33.631 -23.068 1.00 39.32  ? 402 TRP   A O   1 
ATOM   2811 C CB  . TRP   A 1 402 ? -21.190 -34.923 -20.233 1.00 40.65  ? 402 TRP   A CB  1 
ATOM   2812 C CG  . TRP   A 1 402 ? -22.019 -35.776 -19.333 1.00 41.25  ? 402 TRP   A CG  1 
ATOM   2813 C CD1 . TRP   A 1 402 ? -21.595 -36.453 -18.229 1.00 43.34  ? 402 TRP   A CD1 1 
ATOM   2814 C CD2 . TRP   A 1 402 ? -23.424 -36.028 -19.445 1.00 38.42  ? 402 TRP   A CD2 1 
ATOM   2815 N NE1 . TRP   A 1 402 ? -22.647 -37.118 -17.648 1.00 41.08  ? 402 TRP   A NE1 1 
ATOM   2816 C CE2 . TRP   A 1 402 ? -23.782 -36.874 -18.375 1.00 39.70  ? 402 TRP   A CE2 1 
ATOM   2817 C CE3 . TRP   A 1 402 ? -24.415 -35.623 -20.346 1.00 39.23  ? 402 TRP   A CE3 1 
ATOM   2818 C CZ2 . TRP   A 1 402 ? -25.088 -37.325 -18.182 1.00 42.29  ? 402 TRP   A CZ2 1 
ATOM   2819 C CZ3 . TRP   A 1 402 ? -25.712 -36.073 -20.155 1.00 42.25  ? 402 TRP   A CZ3 1 
ATOM   2820 C CH2 . TRP   A 1 402 ? -26.036 -36.914 -19.081 1.00 44.62  ? 402 TRP   A CH2 1 
ATOM   2821 N N   . ILE   A 1 403 ? -18.728 -34.822 -22.340 1.00 43.58  ? 403 ILE   A N   1 
ATOM   2822 C CA  . ILE   A 1 403 ? -17.732 -33.987 -22.996 1.00 41.00  ? 403 ILE   A CA  1 
ATOM   2823 C C   . ILE   A 1 403 ? -17.596 -34.319 -24.476 1.00 42.40  ? 403 ILE   A C   1 
ATOM   2824 O O   . ILE   A 1 403 ? -17.191 -33.457 -25.269 1.00 40.48  ? 403 ILE   A O   1 
ATOM   2825 C CB  . ILE   A 1 403 ? -16.402 -34.166 -22.238 1.00 40.94  ? 403 ILE   A CB  1 
ATOM   2826 C CG1 . ILE   A 1 403 ? -16.281 -33.146 -21.105 1.00 41.23  ? 403 ILE   A CG1 1 
ATOM   2827 C CG2 . ILE   A 1 403 ? -15.195 -34.130 -23.172 1.00 41.36  ? 403 ILE   A CG2 1 
ATOM   2828 C CD1 . ILE   A 1 403 ? -17.284 -32.016 -21.182 1.00 38.47  ? 403 ILE   A CD1 1 
ATOM   2829 N N   . SER   A 1 404 ? -17.990 -35.528 -24.876 1.00 40.38  ? 404 SER   A N   1 
ATOM   2830 C CA  . SER   A 1 404 ? -17.535 -36.092 -26.141 1.00 42.17  ? 404 SER   A CA  1 
ATOM   2831 C C   . SER   A 1 404 ? -18.172 -35.422 -27.352 1.00 38.99  ? 404 SER   A C   1 
ATOM   2832 O O   . SER   A 1 404 ? -17.509 -35.275 -28.384 1.00 41.22  ? 404 SER   A O   1 
ATOM   2833 C CB  . SER   A 1 404 ? -17.811 -37.596 -26.160 1.00 43.67  ? 404 SER   A CB  1 
ATOM   2834 O OG  . SER   A 1 404 ? -19.182 -37.868 -25.920 1.00 44.25  ? 404 SER   A OG  1 
ATOM   2835 N N   . MET   A 1 405 ? -19.445 -35.024 -27.263 1.00 39.10  ? 405 MET   A N   1 
ATOM   2836 C CA  . MET   A 1 405 ? -20.147 -34.527 -28.447 1.00 39.89  ? 405 MET   A CA  1 
ATOM   2837 C C   . MET   A 1 405 ? -19.461 -33.296 -29.029 1.00 40.05  ? 405 MET   A C   1 
ATOM   2838 O O   . MET   A 1 405 ? -19.123 -33.265 -30.218 1.00 39.70  ? 405 MET   A O   1 
ATOM   2839 C CB  . MET   A 1 405 ? -21.605 -34.219 -28.108 1.00 39.17  ? 405 MET   A CB  1 
ATOM   2840 C CG  . MET   A 1 405 ? -22.414 -35.437 -27.709 1.00 41.91  ? 405 MET   A CG  1 
ATOM   2841 S SD  . MET   A 1 405 ? -22.496 -35.638 -25.918 1.00 48.86  ? 405 MET   A SD  1 
ATOM   2842 C CE  . MET   A 1 405 ? -23.736 -34.413 -25.490 1.00 41.15  ? 405 MET   A CE  1 
ATOM   2843 N N   . ALA   A 1 406 ? -19.245 -32.269 -28.206 1.00 38.48  ? 406 ALA   A N   1 
ATOM   2844 C CA  . ALA   A 1 406 ? -18.651 -31.039 -28.720 1.00 39.71  ? 406 ALA   A CA  1 
ATOM   2845 C C   . ALA   A 1 406 ? -17.196 -31.238 -29.115 1.00 37.37  ? 406 ALA   A C   1 
ATOM   2846 O O   . ALA   A 1 406 ? -16.704 -30.567 -30.028 1.00 36.15  ? 406 ALA   A O   1 
ATOM   2847 C CB  . ALA   A 1 406 ? -18.768 -29.922 -27.689 1.00 36.61  ? 406 ALA   A CB  1 
ATOM   2848 N N   . THR   A 1 407 ? -16.496 -32.154 -28.449 1.00 38.61  ? 407 THR   A N   1 
ATOM   2849 C CA  . THR   A 1 407 ? -15.110 -32.417 -28.810 1.00 35.96  ? 407 THR   A CA  1 
ATOM   2850 C C   . THR   A 1 407 ? -15.021 -33.196 -30.117 1.00 37.46  ? 407 THR   A C   1 
ATOM   2851 O O   . THR   A 1 407 ? -14.325 -32.779 -31.047 1.00 38.92  ? 407 THR   A O   1 
ATOM   2852 C CB  . THR   A 1 407 ? -14.408 -33.178 -27.689 1.00 38.69  ? 407 THR   A CB  1 
ATOM   2853 O OG1 . THR   A 1 407 ? -14.459 -32.406 -26.484 1.00 37.44  ? 407 THR   A OG1 1 
ATOM   2854 C CG2 . THR   A 1 407 ? -12.958 -33.429 -28.058 1.00 41.79  ? 407 THR   A CG2 1 
ATOM   2855 N N   . TYR   A 1 408 ? -15.722 -34.330 -30.203 1.00 37.48  ? 408 TYR   A N   1 
ATOM   2856 C CA  . TYR   A 1 408 ? -15.659 -35.156 -31.407 1.00 39.97  ? 408 TYR   A CA  1 
ATOM   2857 C C   . TYR   A 1 408 ? -16.240 -34.424 -32.611 1.00 40.98  ? 408 TYR   A C   1 
ATOM   2858 O O   . TYR   A 1 408 ? -15.648 -34.422 -33.698 1.00 43.48  ? 408 TYR   A O   1 
ATOM   2859 C CB  . TYR   A 1 408 ? -16.395 -36.477 -31.177 1.00 42.78  ? 408 TYR   A CB  1 
ATOM   2860 C CG  . TYR   A 1 408 ? -16.093 -37.539 -32.214 1.00 44.45  ? 408 TYR   A CG  1 
ATOM   2861 C CD1 . TYR   A 1 408 ? -14.789 -37.953 -32.459 1.00 42.33  ? 408 TYR   A CD1 1 
ATOM   2862 C CD2 . TYR   A 1 408 ? -17.115 -38.117 -32.958 1.00 41.62  ? 408 TYR   A CD2 1 
ATOM   2863 C CE1 . TYR   A 1 408 ? -14.515 -38.922 -33.408 1.00 44.38  ? 408 TYR   A CE1 1 
ATOM   2864 C CE2 . TYR   A 1 408 ? -16.851 -39.082 -33.907 1.00 43.82  ? 408 TYR   A CE2 1 
ATOM   2865 C CZ  . TYR   A 1 408 ? -15.549 -39.482 -34.129 1.00 45.15  ? 408 TYR   A CZ  1 
ATOM   2866 O OH  . TYR   A 1 408 ? -15.283 -40.446 -35.075 1.00 44.99  ? 408 TYR   A OH  1 
ATOM   2867 N N   . GLY   A 1 409 ? -17.407 -33.796 -32.436 1.00 39.72  ? 409 GLY   A N   1 
ATOM   2868 C CA  . GLY   A 1 409 ? -18.042 -33.084 -33.530 1.00 36.86  ? 409 GLY   A CA  1 
ATOM   2869 C C   . GLY   A 1 409 ? -17.374 -31.781 -33.911 1.00 41.92  ? 409 GLY   A C   1 
ATOM   2870 O O   . GLY   A 1 409 ? -17.639 -31.264 -35.000 1.00 45.52  ? 409 GLY   A O   1 
ATOM   2871 N N   . GLY   A 1 410 ? -16.508 -31.243 -33.049 1.00 37.62  ? 410 GLY   A N   1 
ATOM   2872 C CA  . GLY   A 1 410 ? -15.891 -29.953 -33.274 1.00 39.06  ? 410 GLY   A CA  1 
ATOM   2873 C C   . GLY   A 1 410 ? -16.721 -28.769 -32.833 1.00 39.54  ? 410 GLY   A C   1 
ATOM   2874 O O   . GLY   A 1 410 ? -16.207 -27.644 -32.825 1.00 39.27  ? 410 GLY   A O   1 
ATOM   2875 N N   . MET   A 1 411 ? -17.977 -28.992 -32.453 1.00 40.66  ? 411 MET   A N   1 
ATOM   2876 C CA  . MET   A 1 411 ? -18.887 -27.909 -32.117 1.00 39.92  ? 411 MET   A CA  1 
ATOM   2877 C C   . MET   A 1 411 ? -18.358 -27.092 -30.939 1.00 38.20  ? 411 MET   A C   1 
ATOM   2878 O O   . MET   A 1 411 ? -17.634 -27.611 -30.084 1.00 38.58  ? 411 MET   A O   1 
ATOM   2879 C CB  . MET   A 1 411 ? -20.261 -28.473 -31.768 1.00 40.94  ? 411 MET   A CB  1 
ATOM   2880 C CG  . MET   A 1 411 ? -21.040 -28.940 -32.964 1.00 38.43  ? 411 MET   A CG  1 
ATOM   2881 S SD  . MET   A 1 411 ? -20.895 -30.722 -33.159 1.00 40.30  ? 411 MET   A SD  1 
ATOM   2882 C CE  . MET   A 1 411 ? -21.514 -31.311 -31.590 1.00 38.84  ? 411 MET   A CE  1 
ATOM   2883 N N   . PRO   A 1 412 ? -18.700 -25.810 -30.871 1.00 38.24  ? 412 PRO   A N   1 
ATOM   2884 C CA  . PRO   A 1 412 ? -18.412 -25.049 -29.653 1.00 37.77  ? 412 PRO   A CA  1 
ATOM   2885 C C   . PRO   A 1 412 ? -19.381 -25.438 -28.549 1.00 38.33  ? 412 PRO   A C   1 
ATOM   2886 O O   . PRO   A 1 412 ? -20.560 -25.700 -28.796 1.00 38.35  ? 412 PRO   A O   1 
ATOM   2887 C CB  . PRO   A 1 412 ? -18.608 -23.592 -30.088 1.00 35.96  ? 412 PRO   A CB  1 
ATOM   2888 C CG  . PRO   A 1 412 ? -19.584 -23.673 -31.209 1.00 39.41  ? 412 PRO   A CG  1 
ATOM   2889 C CD  . PRO   A 1 412 ? -19.324 -24.977 -31.913 1.00 39.93  ? 412 PRO   A CD  1 
ATOM   2890 N N   . ALA   A 1 413 ? -18.868 -25.493 -27.323 1.00 36.71  ? 413 ALA   A N   1 
ATOM   2891 C CA  . ALA   A 1 413 ? -19.681 -25.772 -26.149 1.00 34.40  ? 413 ALA   A CA  1 
ATOM   2892 C C   . ALA   A 1 413 ? -19.321 -24.774 -25.064 1.00 37.88  ? 413 ALA   A C   1 
ATOM   2893 O O   . ALA   A 1 413 ? -18.140 -24.602 -24.745 1.00 35.56  ? 413 ALA   A O   1 
ATOM   2894 C CB  . ALA   A 1 413 ? -19.470 -27.198 -25.637 1.00 37.15  ? 413 ALA   A CB  1 
ATOM   2895 N N   . LEU   A 1 414 ? -20.331 -24.123 -24.499 1.00 37.71  ? 414 LEU   A N   1 
ATOM   2896 C CA  . LEU   A 1 414 ? -20.129 -23.170 -23.421 1.00 38.89  ? 414 LEU   A CA  1 
ATOM   2897 C C   . LEU   A 1 414 ? -20.500 -23.804 -22.086 1.00 36.93  ? 414 LEU   A C   1 
ATOM   2898 O O   . LEU   A 1 414 ? -21.517 -24.493 -21.977 1.00 37.83  ? 414 LEU   A O   1 
ATOM   2899 C CB  . LEU   A 1 414 ? -20.955 -21.904 -23.646 1.00 38.52  ? 414 LEU   A CB  1 
ATOM   2900 C CG  . LEU   A 1 414 ? -21.016 -20.941 -22.459 1.00 39.60  ? 414 LEU   A CG  1 
ATOM   2901 C CD1 . LEU   A 1 414 ? -19.868 -19.947 -22.518 1.00 36.98  ? 414 LEU   A CD1 1 
ATOM   2902 C CD2 . LEU   A 1 414 ? -22.354 -20.226 -22.420 1.00 41.39  ? 414 LEU   A CD2 1 
ATOM   2903 N N   . SER   A 1 415 ? -19.658 -23.583 -21.081 1.00 35.05  ? 415 SER   A N   1 
ATOM   2904 C CA  . SER   A 1 415 ? -19.925 -23.997 -19.709 1.00 35.00  ? 415 SER   A CA  1 
ATOM   2905 C C   . SER   A 1 415 ? -20.158 -22.745 -18.869 1.00 35.05  ? 415 SER   A C   1 
ATOM   2906 O O   . SER   A 1 415 ? -19.247 -21.928 -18.702 1.00 33.08  ? 415 SER   A O   1 
ATOM   2907 C CB  . SER   A 1 415 ? -18.769 -24.830 -19.154 1.00 32.90  ? 415 SER   A CB  1 
ATOM   2908 O OG  . SER   A 1 415 ? -18.787 -24.865 -17.738 1.00 34.95  ? 415 SER   A OG  1 
ATOM   2909 N N   . MET   A 1 416 ? -21.375 -22.593 -18.355 1.00 36.13  ? 416 MET   A N   1 
ATOM   2910 C CA  . MET   A 1 416 ? -21.791 -21.380 -17.669 1.00 35.90  ? 416 MET   A CA  1 
ATOM   2911 C C   . MET   A 1 416 ? -22.472 -21.711 -16.348 1.00 35.95  ? 416 MET   A C   1 
ATOM   2912 O O   . MET   A 1 416 ? -23.144 -22.741 -16.229 1.00 32.61  ? 416 MET   A O   1 
ATOM   2913 C CB  . MET   A 1 416 ? -22.739 -20.555 -18.553 1.00 32.99  ? 416 MET   A CB  1 
ATOM   2914 C CG  . MET   A 1 416 ? -23.986 -21.308 -18.987 1.00 38.58  ? 416 MET   A CG  1 
ATOM   2915 S SD  . MET   A 1 416 ? -25.442 -20.252 -19.137 1.00 45.99  ? 416 MET   A SD  1 
ATOM   2916 C CE  . MET   A 1 416 ? -25.435 -19.411 -17.559 1.00 36.33  ? 416 MET   A CE  1 
ATOM   2917 N N   . PRO   A 1 417 ? -22.318 -20.847 -15.341 1.00 38.20  ? 417 PRO   A N   1 
ATOM   2918 C CA  . PRO   A 1 417 ? -22.848 -21.153 -14.004 1.00 37.37  ? 417 PRO   A CA  1 
ATOM   2919 C C   . PRO   A 1 417 ? -24.366 -21.243 -13.974 1.00 36.12  ? 417 PRO   A C   1 
ATOM   2920 O O   . PRO   A 1 417 ? -25.070 -20.468 -14.624 1.00 38.74  ? 417 PRO   A O   1 
ATOM   2921 C CB  . PRO   A 1 417 ? -22.352 -19.974 -13.156 1.00 34.83  ? 417 PRO   A CB  1 
ATOM   2922 C CG  . PRO   A 1 417 ? -21.140 -19.486 -13.885 1.00 37.15  ? 417 PRO   A CG  1 
ATOM   2923 C CD  . PRO   A 1 417 ? -21.524 -19.609 -15.332 1.00 37.06  ? 417 PRO   A CD  1 
ATOM   2924 N N   . LEU   A 1 418 ? -24.866 -22.196 -13.183 1.00 38.42  ? 418 LEU   A N   1 
ATOM   2925 C CA  . LEU   A 1 418 ? -26.295 -22.396 -12.982 1.00 39.44  ? 418 LEU   A CA  1 
ATOM   2926 C C   . LEU   A 1 418 ? -26.726 -22.320 -11.526 1.00 42.17  ? 418 LEU   A C   1 
ATOM   2927 O O   . LEU   A 1 418 ? -27.927 -22.194 -11.265 1.00 47.69  ? 418 LEU   A O   1 
ATOM   2928 C CB  . LEU   A 1 418 ? -26.732 -23.764 -13.527 1.00 41.84  ? 418 LEU   A CB  1 
ATOM   2929 C CG  . LEU   A 1 418 ? -27.115 -23.933 -14.995 1.00 43.13  ? 418 LEU   A CG  1 
ATOM   2930 C CD1 . LEU   A 1 418 ? -28.068 -25.109 -15.135 1.00 42.33  ? 418 LEU   A CD1 1 
ATOM   2931 C CD2 . LEU   A 1 418 ? -27.729 -22.673 -15.579 1.00 40.66  ? 418 LEU   A CD2 1 
ATOM   2932 N N   . GLY   A 1 419 ? -25.799 -22.396 -10.585 1.00 41.75  ? 419 GLY   A N   1 
ATOM   2933 C CA  . GLY   A 1 419 ? -26.093 -22.490 -9.176  1.00 42.86  ? 419 GLY   A CA  1 
ATOM   2934 C C   . GLY   A 1 419 ? -25.171 -23.497 -8.526  1.00 44.41  ? 419 GLY   A C   1 
ATOM   2935 O O   . GLY   A 1 419 ? -24.095 -23.796 -9.041  1.00 42.24  ? 419 GLY   A O   1 
ATOM   2936 N N   . ALA   A 1 420 ? -25.606 -24.027 -7.386  1.00 44.54  ? 420 ALA   A N   1 
ATOM   2937 C CA  . ALA   A 1 420 ? -24.800 -24.969 -6.624  1.00 44.67  ? 420 ALA   A CA  1 
ATOM   2938 C C   . ALA   A 1 420 ? -25.671 -26.131 -6.172  1.00 42.79  ? 420 ALA   A C   1 
ATOM   2939 O O   . ALA   A 1 420 ? -26.902 -26.050 -6.175  1.00 43.91  ? 420 ALA   A O   1 
ATOM   2940 C CB  . ALA   A 1 420 ? -24.138 -24.296 -5.412  1.00 41.97  ? 420 ALA   A CB  1 
ATOM   2941 N N   . ASP   A 1 421 ? -25.016 -27.224 -5.787  1.00 41.26  ? 421 ASP   A N   1 
ATOM   2942 C CA  . ASP   A 1 421 ? -25.729 -28.360 -5.231  1.00 40.99  ? 421 ASP   A CA  1 
ATOM   2943 C C   . ASP   A 1 421 ? -25.961 -28.134 -3.737  1.00 39.40  ? 421 ASP   A C   1 
ATOM   2944 O O   . ASP   A 1 421 ? -25.641 -27.077 -3.188  1.00 42.56  ? 421 ASP   A O   1 
ATOM   2945 C CB  . ASP   A 1 421 ? -24.981 -29.664 -5.532  1.00 42.25  ? 421 ASP   A CB  1 
ATOM   2946 C CG  . ASP   A 1 421 ? -23.700 -29.845 -4.710  1.00 44.78  ? 421 ASP   A CG  1 
ATOM   2947 O OD1 . ASP   A 1 421 ? -23.269 -28.927 -3.979  1.00 43.86  ? 421 ASP   A OD1 1 
ATOM   2948 O OD2 . ASP   A 1 421 ? -23.105 -30.939 -4.811  1.00 49.03  ? 421 ASP   A OD2 1 
ATOM   2949 N N   . GLY   A 1 422 ? -26.527 -29.140 -3.069  1.00 41.47  ? 422 GLY   A N   1 
ATOM   2950 C CA  . GLY   A 1 422 ? -26.813 -29.020 -1.648  1.00 41.16  ? 422 GLY   A CA  1 
ATOM   2951 C C   . GLY   A 1 422 ? -25.592 -28.760 -0.789  1.00 42.01  ? 422 GLY   A C   1 
ATOM   2952 O O   . GLY   A 1 422 ? -25.723 -28.187 0.297   1.00 43.73  ? 422 GLY   A O   1 
ATOM   2953 N N   . ASN   A 1 423 ? -24.409 -29.150 -1.256  1.00 40.97  ? 423 ASN   A N   1 
ATOM   2954 C CA  . ASN   A 1 423 ? -23.168 -28.971 -0.515  1.00 43.97  ? 423 ASN   A CA  1 
ATOM   2955 C C   . ASN   A 1 423 ? -22.425 -27.700 -0.899  1.00 43.56  ? 423 ASN   A C   1 
ATOM   2956 O O   . ASN   A 1 423 ? -21.259 -27.547 -0.528  1.00 43.99  ? 423 ASN   A O   1 
ATOM   2957 C CB  . ASN   A 1 423 ? -22.254 -30.175 -0.728  1.00 43.41  ? 423 ASN   A CB  1 
ATOM   2958 C CG  . ASN   A 1 423 ? -22.712 -31.385 0.044   1.00 49.06  ? 423 ASN   A CG  1 
ATOM   2959 O OD1 . ASN   A 1 423 ? -23.465 -31.269 1.011   1.00 52.70  ? 423 ASN   A OD1 1 
ATOM   2960 N ND2 . ASN   A 1 423 ? -22.273 -32.560 -0.385  1.00 52.59  ? 423 ASN   A ND2 1 
ATOM   2961 N N   . GLY   A 1 424 ? -23.060 -26.796 -1.638  1.00 39.17  ? 424 GLY   A N   1 
ATOM   2962 C CA  . GLY   A 1 424 ? -22.394 -25.566 -2.009  1.00 38.94  ? 424 GLY   A CA  1 
ATOM   2963 C C   . GLY   A 1 424 ? -21.385 -25.696 -3.125  1.00 41.92  ? 424 GLY   A C   1 
ATOM   2964 O O   . GLY   A 1 424 ? -20.574 -24.787 -3.317  1.00 41.64  ? 424 GLY   A O   1 
ATOM   2965 N N   . LEU   A 1 425 ? -21.405 -26.803 -3.869  1.00 38.91  ? 425 LEU   A N   1 
ATOM   2966 C CA  . LEU   A 1 425 ? -20.507 -26.954 -5.009  1.00 40.58  ? 425 LEU   A CA  1 
ATOM   2967 C C   . LEU   A 1 425 ? -21.209 -26.562 -6.306  1.00 39.85  ? 425 LEU   A C   1 
ATOM   2968 O O   . LEU   A 1 425 ? -22.355 -26.966 -6.540  1.00 42.47  ? 425 LEU   A O   1 
ATOM   2969 C CB  . LEU   A 1 425 ? -19.999 -28.393 -5.118  1.00 40.14  ? 425 LEU   A CB  1 
ATOM   2970 C CG  . LEU   A 1 425 ? -19.293 -28.942 -3.876  1.00 42.28  ? 425 LEU   A CG  1 
ATOM   2971 C CD1 . LEU   A 1 425 ? -18.881 -30.392 -4.068  1.00 42.27  ? 425 LEU   A CD1 1 
ATOM   2972 C CD2 . LEU   A 1 425 ? -18.090 -28.076 -3.546  1.00 40.06  ? 425 LEU   A CD2 1 
ATOM   2973 N N   . PRO   A 1 426 ? -20.533 -25.792 -7.158  1.00 38.87  ? 426 PRO   A N   1 
ATOM   2974 C CA  . PRO   A 1 426 ? -21.192 -25.241 -8.350  1.00 38.60  ? 426 PRO   A CA  1 
ATOM   2975 C C   . PRO   A 1 426 ? -21.654 -26.311 -9.330  1.00 39.55  ? 426 PRO   A C   1 
ATOM   2976 O O   . PRO   A 1 426 ? -21.044 -27.374 -9.468  1.00 37.41  ? 426 PRO   A O   1 
ATOM   2977 C CB  . PRO   A 1 426 ? -20.099 -24.364 -8.972  1.00 33.87  ? 426 PRO   A CB  1 
ATOM   2978 C CG  . PRO   A 1 426 ? -19.242 -23.989 -7.803  1.00 36.05  ? 426 PRO   A CG  1 
ATOM   2979 C CD  . PRO   A 1 426 ? -19.171 -25.254 -7.007  1.00 36.60  ? 426 PRO   A CD  1 
ATOM   2980 N N   . ILE   A 1 427 ? -22.747 -25.998 -10.025 1.00 40.08  ? 427 ILE   A N   1 
ATOM   2981 C CA  . ILE   A 1 427 ? -23.265 -26.797 -11.132 1.00 37.18  ? 427 ILE   A CA  1 
ATOM   2982 C C   . ILE   A 1 427 ? -23.369 -25.881 -12.343 1.00 38.69  ? 427 ILE   A C   1 
ATOM   2983 O O   . ILE   A 1 427 ? -24.013 -24.828 -12.272 1.00 37.44  ? 427 ILE   A O   1 
ATOM   2984 C CB  . ILE   A 1 427 ? -24.634 -27.421 -10.811 1.00 39.94  ? 427 ILE   A CB  1 
ATOM   2985 C CG1 . ILE   A 1 427 ? -24.558 -28.288 -9.555  1.00 38.70  ? 427 ILE   A CG1 1 
ATOM   2986 C CG2 . ILE   A 1 427 ? -25.149 -28.233 -11.995 1.00 38.52  ? 427 ILE   A CG2 1 
ATOM   2987 C CD1 . ILE   A 1 427 ? -25.880 -28.920 -9.178  1.00 39.59  ? 427 ILE   A CD1 1 
ATOM   2988 N N   . ASN   A 1 428 ? -22.742 -26.275 -13.447 1.00 34.74  ? 428 ASN   A N   1 
ATOM   2989 C CA  . ASN   A 1 428 ? -22.742 -25.475 -14.660 1.00 33.79  ? 428 ASN   A CA  1 
ATOM   2990 C C   . ASN   A 1 428 ? -23.555 -26.151 -15.756 1.00 38.07  ? 428 ASN   A C   1 
ATOM   2991 O O   . ASN   A 1 428 ? -23.693 -27.378 -15.791 1.00 37.83  ? 428 ASN   A O   1 
ATOM   2992 C CB  . ASN   A 1 428 ? -21.321 -25.220 -15.162 1.00 33.14  ? 428 ASN   A CB  1 
ATOM   2993 C CG  . ASN   A 1 428 ? -20.682 -24.014 -14.511 1.00 34.23  ? 428 ASN   A CG  1 
ATOM   2994 O OD1 . ASN   A 1 428 ? -20.935 -23.726 -13.339 1.00 35.37  ? 428 ASN   A OD1 1 
ATOM   2995 N ND2 . ASN   A 1 428 ? -19.835 -23.309 -15.263 1.00 35.19  ? 428 ASN   A ND2 1 
ATOM   2996 N N   . LEU   A 1 429 ? -24.106 -25.322 -16.638 1.00 36.57  ? 429 LEU   A N   1 
ATOM   2997 C CA  . LEU   A 1 429 ? -24.777 -25.767 -17.848 1.00 36.61  ? 429 LEU   A CA  1 
ATOM   2998 C C   . LEU   A 1 429 ? -23.776 -25.875 -18.992 1.00 37.81  ? 429 LEU   A C   1 
ATOM   2999 O O   . LEU   A 1 429 ? -22.835 -25.083 -19.092 1.00 38.36  ? 429 LEU   A O   1 
ATOM   3000 C CB  . LEU   A 1 429 ? -25.891 -24.787 -18.229 1.00 35.19  ? 429 LEU   A CB  1 
ATOM   3001 C CG  . LEU   A 1 429 ? -26.661 -25.012 -19.534 1.00 37.55  ? 429 LEU   A CG  1 
ATOM   3002 C CD1 . LEU   A 1 429 ? -27.434 -26.320 -19.474 1.00 34.98  ? 429 LEU   A CD1 1 
ATOM   3003 C CD2 . LEU   A 1 429 ? -27.603 -23.841 -19.833 1.00 39.26  ? 429 LEU   A CD2 1 
ATOM   3004 N N   . GLN   A 1 430 ? -23.982 -26.864 -19.856 1.00 37.56  ? 430 GLN   A N   1 
ATOM   3005 C CA  . GLN   A 1 430 ? -23.271 -26.942 -21.124 1.00 36.95  ? 430 GLN   A CA  1 
ATOM   3006 C C   . GLN   A 1 430 ? -24.228 -26.576 -22.247 1.00 39.63  ? 430 GLN   A C   1 
ATOM   3007 O O   . GLN   A 1 430 ? -25.345 -27.100 -22.313 1.00 41.04  ? 430 GLN   A O   1 
ATOM   3008 C CB  . GLN   A 1 430 ? -22.676 -28.331 -21.367 1.00 37.55  ? 430 GLN   A CB  1 
ATOM   3009 C CG  . GLN   A 1 430 ? -21.801 -28.382 -22.611 1.00 38.00  ? 430 GLN   A CG  1 
ATOM   3010 C CD  . GLN   A 1 430 ? -21.118 -29.718 -22.812 1.00 40.68  ? 430 GLN   A CD  1 
ATOM   3011 O OE1 . GLN   A 1 430 ? -20.394 -29.915 -23.788 1.00 43.34  ? 430 GLN   A OE1 1 
ATOM   3012 N NE2 . GLN   A 1 430 ? -21.344 -30.646 -21.890 1.00 42.17  ? 430 GLN   A NE2 1 
ATOM   3013 N N   . ILE   A 1 431 ? -23.796 -25.667 -23.115 1.00 43.03  ? 431 ILE   A N   1 
ATOM   3014 C CA  . ILE   A 1 431 ? -24.589 -25.212 -24.250 1.00 39.81  ? 431 ILE   A CA  1 
ATOM   3015 C C   . ILE   A 1 431 ? -23.803 -25.525 -25.512 1.00 41.18  ? 431 ILE   A C   1 
ATOM   3016 O O   . ILE   A 1 431 ? -22.765 -24.905 -25.774 1.00 41.92  ? 431 ILE   A O   1 
ATOM   3017 C CB  . ILE   A 1 431 ? -24.922 -23.718 -24.163 1.00 38.35  ? 431 ILE   A CB  1 
ATOM   3018 C CG1 . ILE   A 1 431 ? -25.701 -23.419 -22.882 1.00 38.67  ? 431 ILE   A CG1 1 
ATOM   3019 C CG2 . ILE   A 1 431 ? -25.700 -23.277 -25.394 1.00 39.10  ? 431 ILE   A CG2 1 
ATOM   3020 C CD1 . ILE   A 1 431 ? -26.200 -21.991 -22.793 1.00 38.67  ? 431 ILE   A CD1 1 
ATOM   3021 N N   . ILE   A 1 432 ? -24.298 -26.477 -26.298 1.00 42.43  ? 432 ILE   A N   1 
ATOM   3022 C CA  . ILE   A 1 432 ? -23.649 -26.910 -27.529 1.00 40.61  ? 432 ILE   A CA  1 
ATOM   3023 C C   . ILE   A 1 432 ? -24.391 -26.298 -28.708 1.00 40.12  ? 432 ILE   A C   1 
ATOM   3024 O O   . ILE   A 1 432 ? -25.611 -26.463 -28.836 1.00 39.10  ? 432 ILE   A O   1 
ATOM   3025 C CB  . ILE   A 1 432 ? -23.629 -28.444 -27.636 1.00 41.62  ? 432 ILE   A CB  1 
ATOM   3026 C CG1 . ILE   A 1 432 ? -23.083 -29.066 -26.346 1.00 42.21  ? 432 ILE   A CG1 1 
ATOM   3027 C CG2 . ILE   A 1 432 ? -22.808 -28.874 -28.837 1.00 38.52  ? 432 ILE   A CG2 1 
ATOM   3028 C CD1 . ILE   A 1 432 ? -23.142 -30.577 -26.317 1.00 36.67  ? 432 ILE   A CD1 1 
ATOM   3029 N N   . THR   A 1 433 ? -23.662 -25.590 -29.564 1.00 36.88  ? 433 THR   A N   1 
ATOM   3030 C CA  . THR   A 1 433 ? -24.211 -25.019 -30.786 1.00 40.78  ? 433 THR   A CA  1 
ATOM   3031 C C   . THR   A 1 433 ? -23.429 -25.550 -31.984 1.00 41.38  ? 433 THR   A C   1 
ATOM   3032 O O   . THR   A 1 433 ? -22.377 -26.172 -31.836 1.00 44.92  ? 433 THR   A O   1 
ATOM   3033 C CB  . THR   A 1 433 ? -24.173 -23.482 -30.750 1.00 40.93  ? 433 THR   A CB  1 
ATOM   3034 O OG1 . THR   A 1 433 ? -22.880 -23.039 -30.330 1.00 44.38  ? 433 THR   A OG1 1 
ATOM   3035 C CG2 . THR   A 1 433 ? -25.200 -22.950 -29.778 1.00 40.91  ? 433 THR   A CG2 1 
ATOM   3036 N N   . ARG   A 1 434 ? -23.957 -25.303 -33.183 1.00 42.12  ? 434 ARG   A N   1 
ATOM   3037 C CA  . ARG   A 1 434 ? -23.331 -25.794 -34.406 1.00 42.04  ? 434 ARG   A CA  1 
ATOM   3038 C C   . ARG   A 1 434 ? -21.929 -25.209 -34.573 1.00 40.83  ? 434 ARG   A C   1 
ATOM   3039 O O   . ARG   A 1 434 ? -21.593 -24.163 -34.012 1.00 38.32  ? 434 ARG   A O   1 
ATOM   3040 C CB  . ARG   A 1 434 ? -24.188 -25.444 -35.625 1.00 40.10  ? 434 ARG   A CB  1 
ATOM   3041 C CG  . ARG   A 1 434 ? -24.016 -24.017 -36.123 1.00 42.88  ? 434 ARG   A CG  1 
ATOM   3042 C CD  . ARG   A 1 434 ? -25.283 -23.512 -36.797 1.00 47.78  ? 434 ARG   A CD  1 
ATOM   3043 N NE  . ARG   A 1 434 ? -24.992 -22.680 -37.959 1.00 51.17  ? 434 ARG   A NE  1 
ATOM   3044 C CZ  . ARG   A 1 434 ? -25.360 -21.412 -38.087 1.00 52.31  ? 434 ARG   A CZ  1 
ATOM   3045 N NH1 . ARG   A 1 434 ? -26.039 -20.788 -37.137 1.00 54.19  ? 434 ARG   A NH1 1 
ATOM   3046 N NH2 . ARG   A 1 434 ? -25.034 -20.751 -39.194 1.00 56.68  ? 434 ARG   A NH2 1 
ATOM   3047 N N   . ASN   A 1 435 ? -21.106 -25.907 -35.362 1.00 40.67  ? 435 ASN   A N   1 
ATOM   3048 C CA  . ASN   A 1 435 ? -19.754 -25.441 -35.644 1.00 40.48  ? 435 ASN   A CA  1 
ATOM   3049 C C   . ASN   A 1 435 ? -19.767 -24.015 -36.178 1.00 43.48  ? 435 ASN   A C   1 
ATOM   3050 O O   . ASN   A 1 435 ? -20.668 -23.622 -36.924 1.00 45.66  ? 435 ASN   A O   1 
ATOM   3051 C CB  . ASN   A 1 435 ? -19.060 -26.361 -36.654 1.00 41.89  ? 435 ASN   A CB  1 
ATOM   3052 C CG  . ASN   A 1 435 ? -18.789 -27.748 -36.103 1.00 43.21  ? 435 ASN   A CG  1 
ATOM   3053 O OD1 . ASN   A 1 435 ? -19.708 -28.478 -35.740 1.00 47.86  ? 435 ASN   A OD1 1 
ATOM   3054 N ND2 . ASN   A 1 435 ? -17.515 -28.107 -36.014 1.00 42.61  ? 435 ASN   A ND2 1 
ATOM   3055 N N   . TRP   A 1 436 ? -18.766 -23.237 -35.763 1.00 42.32  ? 436 TRP   A N   1 
ATOM   3056 C CA  . TRP   A 1 436 ? -18.514 -21.860 -36.180 1.00 41.78  ? 436 TRP   A CA  1 
ATOM   3057 C C   . TRP   A 1 436 ? -19.501 -20.862 -35.587 1.00 41.49  ? 436 TRP   A C   1 
ATOM   3058 O O   . TRP   A 1 436 ? -19.391 -19.664 -35.874 1.00 44.28  ? 436 TRP   A O   1 
ATOM   3059 C CB  . TRP   A 1 436 ? -18.494 -21.724 -37.709 1.00 41.92  ? 436 TRP   A CB  1 
ATOM   3060 C CG  . TRP   A 1 436 ? -17.533 -22.689 -38.305 1.00 41.56  ? 436 TRP   A CG  1 
ATOM   3061 C CD1 . TRP   A 1 436 ? -17.825 -23.797 -39.046 1.00 43.96  ? 436 TRP   A CD1 1 
ATOM   3062 C CD2 . TRP   A 1 436 ? -16.112 -22.657 -38.171 1.00 40.04  ? 436 TRP   A CD2 1 
ATOM   3063 N NE1 . TRP   A 1 436 ? -16.666 -24.447 -39.397 1.00 45.49  ? 436 TRP   A NE1 1 
ATOM   3064 C CE2 . TRP   A 1 436 ? -15.600 -23.767 -38.870 1.00 41.30  ? 436 TRP   A CE2 1 
ATOM   3065 C CE3 . TRP   A 1 436 ? -15.220 -21.788 -37.537 1.00 40.08  ? 436 TRP   A CE3 1 
ATOM   3066 C CZ2 . TRP   A 1 436 ? -14.235 -24.032 -38.952 1.00 47.10  ? 436 TRP   A CZ2 1 
ATOM   3067 C CZ3 . TRP   A 1 436 ? -13.866 -22.053 -37.618 1.00 42.73  ? 436 TRP   A CZ3 1 
ATOM   3068 C CH2 . TRP   A 1 436 ? -13.385 -23.164 -38.320 1.00 40.84  ? 436 TRP   A CH2 1 
ATOM   3069 N N   . SER   A 1 437 ? -20.442 -21.302 -34.760 1.00 43.50  ? 437 SER   A N   1 
ATOM   3070 C CA  . SER   A 1 437 ? -21.369 -20.399 -34.072 1.00 41.27  ? 437 SER   A CA  1 
ATOM   3071 C C   . SER   A 1 437 ? -20.976 -20.215 -32.611 1.00 41.43  ? 437 SER   A C   1 
ATOM   3072 O O   . SER   A 1 437 ? -21.806 -20.318 -31.705 1.00 40.62  ? 437 SER   A O   1 
ATOM   3073 C CB  . SER   A 1 437 ? -22.797 -20.917 -34.196 1.00 41.26  ? 437 SER   A CB  1 
ATOM   3074 O OG  . SER   A 1 437 ? -23.014 -22.038 -33.356 1.00 44.18  ? 437 SER   A OG  1 
ATOM   3075 N N   . ASP   A 1 438 ? -19.688 -19.942 -32.373 1.00 41.71  ? 438 ASP   A N   1 
ATOM   3076 C CA  . ASP   A 1 438 ? -19.211 -19.722 -31.011 1.00 39.03  ? 438 ASP   A CA  1 
ATOM   3077 C C   . ASP   A 1 438 ? -19.899 -18.526 -30.367 1.00 39.72  ? 438 ASP   A C   1 
ATOM   3078 O O   . ASP   A 1 438 ? -20.259 -18.568 -29.184 1.00 38.24  ? 438 ASP   A O   1 
ATOM   3079 C CB  . ASP   A 1 438 ? -17.692 -19.528 -31.000 1.00 36.91  ? 438 ASP   A CB  1 
ATOM   3080 C CG  . ASP   A 1 438 ? -16.949 -20.630 -31.740 1.00 43.54  ? 438 ASP   A CG  1 
ATOM   3081 O OD1 . ASP   A 1 438 ? -17.278 -20.900 -32.915 1.00 43.53  ? 438 ASP   A OD1 1 
ATOM   3082 O OD2 . ASP   A 1 438 ? -16.035 -21.232 -31.136 1.00 40.02  ? 438 ASP   A OD2 1 
ATOM   3083 N N   . HIS   A 1 439 ? -20.095 -17.448 -31.130 1.00 39.32  ? 439 HIS   A N   1 
ATOM   3084 C CA  . HIS   A 1 439 ? -20.728 -16.258 -30.574 1.00 40.81  ? 439 HIS   A CA  1 
ATOM   3085 C C   . HIS   A 1 439 ? -22.189 -16.511 -30.221 1.00 40.65  ? 439 HIS   A C   1 
ATOM   3086 O O   . HIS   A 1 439 ? -22.715 -15.891 -29.289 1.00 41.10  ? 439 HIS   A O   1 
ATOM   3087 C CB  . HIS   A 1 439 ? -20.594 -15.096 -31.557 1.00 40.25  ? 439 HIS   A CB  1 
ATOM   3088 C CG  . HIS   A 1 439 ? -19.296 -14.362 -31.442 1.00 40.88  ? 439 HIS   A CG  1 
ATOM   3089 N ND1 . HIS   A 1 439 ? -18.959 -13.620 -30.331 1.00 41.25  ? 439 HIS   A ND1 1 
ATOM   3090 C CD2 . HIS   A 1 439 ? -18.244 -14.270 -32.289 1.00 44.78  ? 439 HIS   A CD2 1 
ATOM   3091 C CE1 . HIS   A 1 439 ? -17.759 -13.094 -30.503 1.00 42.51  ? 439 HIS   A CE1 1 
ATOM   3092 N NE2 . HIS   A 1 439 ? -17.303 -13.475 -31.682 1.00 44.61  ? 439 HIS   A NE2 1 
ATOM   3093 N N   . ASP   A 1 440 ? -22.856 -17.416 -30.944 1.00 41.10  ? 440 ASP   A N   1 
ATOM   3094 C CA  . ASP   A 1 440 ? -24.199 -17.832 -30.551 1.00 39.27  ? 440 ASP   A CA  1 
ATOM   3095 C C   . ASP   A 1 440 ? -24.179 -18.530 -29.197 1.00 39.63  ? 440 ASP   A C   1 
ATOM   3096 O O   . ASP   A 1 440 ? -25.081 -18.333 -28.373 1.00 40.40  ? 440 ASP   A O   1 
ATOM   3097 C CB  . ASP   A 1 440 ? -24.801 -18.758 -31.610 1.00 38.52  ? 440 ASP   A CB  1 
ATOM   3098 C CG  . ASP   A 1 440 ? -25.259 -18.016 -32.851 1.00 43.77  ? 440 ASP   A CG  1 
ATOM   3099 O OD1 . ASP   A 1 440 ? -25.349 -18.650 -33.924 1.00 45.36  ? 440 ASP   A OD1 1 
ATOM   3100 O OD2 . ASP   A 1 440 ? -25.531 -16.801 -32.757 1.00 49.26  ? 440 ASP   A OD2 1 
ATOM   3101 N N   . ALA   A 1 441 ? -23.157 -19.353 -28.951 1.00 39.75  ? 441 ALA   A N   1 
ATOM   3102 C CA  . ALA   A 1 441 ? -23.051 -20.048 -27.673 1.00 38.76  ? 441 ALA   A CA  1 
ATOM   3103 C C   . ALA   A 1 441 ? -22.919 -19.059 -26.520 1.00 38.55  ? 441 ALA   A C   1 
ATOM   3104 O O   . ALA   A 1 441 ? -23.599 -19.188 -25.496 1.00 36.94  ? 441 ALA   A O   1 
ATOM   3105 C CB  . ALA   A 1 441 ? -21.866 -21.014 -27.703 1.00 38.83  ? 441 ALA   A CB  1 
ATOM   3106 N N   . ILE   A 1 442 ? -22.047 -18.060 -26.673 1.00 37.14  ? 442 ILE   A N   1 
ATOM   3107 C CA  . ILE   A 1 442 ? -21.892 -17.037 -25.641 1.00 39.24  ? 442 ILE   A CA  1 
ATOM   3108 C C   . ILE   A 1 442 ? -23.192 -16.262 -25.467 1.00 40.66  ? 442 ILE   A C   1 
ATOM   3109 O O   . ILE   A 1 442 ? -23.676 -16.066 -24.346 1.00 38.46  ? 442 ILE   A O   1 
ATOM   3110 C CB  . ILE   A 1 442 ? -20.723 -16.097 -25.988 1.00 39.46  ? 442 ILE   A CB  1 
ATOM   3111 C CG1 . ILE   A 1 442 ? -19.402 -16.864 -26.038 1.00 38.82  ? 442 ILE   A CG1 1 
ATOM   3112 C CG2 . ILE   A 1 442 ? -20.647 -14.946 -24.999 1.00 38.45  ? 442 ILE   A CG2 1 
ATOM   3113 C CD1 . ILE   A 1 442 ? -18.360 -16.192 -26.894 1.00 34.28  ? 442 ILE   A CD1 1 
ATOM   3114 N N   . ARG   A 1 443 ? -23.776 -15.817 -26.583 1.00 39.96  ? 443 ARG   A N   1 
ATOM   3115 C CA  . ARG   A 1 443 ? -24.987 -15.004 -26.533 1.00 40.35  ? 443 ARG   A CA  1 
ATOM   3116 C C   . ARG   A 1 443 ? -26.133 -15.746 -25.852 1.00 41.08  ? 443 ARG   A C   1 
ATOM   3117 O O   . ARG   A 1 443 ? -26.857 -15.166 -25.034 1.00 44.27  ? 443 ARG   A O   1 
ATOM   3118 C CB  . ARG   A 1 443 ? -25.381 -14.580 -27.948 1.00 40.77  ? 443 ARG   A CB  1 
ATOM   3119 C CG  . ARG   A 1 443 ? -26.691 -13.816 -28.034 1.00 43.86  ? 443 ARG   A CG  1 
ATOM   3120 C CD  . ARG   A 1 443 ? -26.664 -12.571 -27.163 1.00 43.82  ? 443 ARG   A CD  1 
ATOM   3121 N NE  . ARG   A 1 443 ? -25.543 -11.701 -27.495 1.00 47.20  ? 443 ARG   A NE  1 
ATOM   3122 C CZ  . ARG   A 1 443 ? -25.539 -10.837 -28.502 1.00 46.09  ? 443 ARG   A CZ  1 
ATOM   3123 N NH1 . ARG   A 1 443 ? -26.588 -10.699 -29.298 1.00 51.55  ? 443 ARG   A NH1 1 
ATOM   3124 N NH2 . ARG   A 1 443 ? -24.458 -10.092 -28.713 1.00 45.00  ? 443 ARG   A NH2 1 
ATOM   3125 N N   . ILE   A 1 444 ? -26.315 -17.029 -26.174 1.00 38.40  ? 444 ILE   A N   1 
ATOM   3126 C CA  . ILE   A 1 444 ? -27.374 -17.800 -25.531 1.00 39.34  ? 444 ILE   A CA  1 
ATOM   3127 C C   . ILE   A 1 444 ? -27.092 -17.956 -24.042 1.00 40.43  ? 444 ILE   A C   1 
ATOM   3128 O O   . ILE   A 1 444 ? -28.006 -17.878 -23.212 1.00 42.14  ? 444 ILE   A O   1 
ATOM   3129 C CB  . ILE   A 1 444 ? -27.545 -19.162 -26.228 1.00 37.73  ? 444 ILE   A CB  1 
ATOM   3130 C CG1 . ILE   A 1 444 ? -28.155 -18.970 -27.614 1.00 39.87  ? 444 ILE   A CG1 1 
ATOM   3131 C CG2 . ILE   A 1 444 ? -28.425 -20.087 -25.405 1.00 39.02  ? 444 ILE   A CG2 1 
ATOM   3132 C CD1 . ILE   A 1 444 ? -27.856 -20.099 -28.565 1.00 40.65  ? 444 ILE   A CD1 1 
ATOM   3133 N N   . GLY   A 1 445 ? -25.826 -18.162 -23.679 1.00 42.13  ? 445 GLY   A N   1 
ATOM   3134 C CA  . GLY   A 1 445 ? -25.483 -18.280 -22.270 1.00 43.97  ? 445 GLY   A CA  1 
ATOM   3135 C C   . GLY   A 1 445 ? -25.797 -17.021 -21.485 1.00 41.61  ? 445 GLY   A C   1 
ATOM   3136 O O   . GLY   A 1 445 ? -26.275 -17.089 -20.350 1.00 41.46  ? 445 GLY   A O   1 
ATOM   3137 N N   . ALA   A 1 446 ? -25.531 -15.854 -22.079 1.00 39.42  ? 446 ALA   A N   1 
ATOM   3138 C CA  . ALA   A 1 446 ? -25.876 -14.599 -21.419 1.00 42.30  ? 446 ALA   A CA  1 
ATOM   3139 C C   . ALA   A 1 446 ? -27.381 -14.487 -21.211 1.00 43.15  ? 446 ALA   A C   1 
ATOM   3140 O O   . ALA   A 1 446 ? -27.841 -14.055 -20.147 1.00 41.58  ? 446 ALA   A O   1 
ATOM   3141 C CB  . ALA   A 1 446 ? -25.353 -13.416 -22.234 1.00 38.34  ? 446 ALA   A CB  1 
ATOM   3142 N N   . LEU   A 1 447 ? -28.163 -14.899 -22.210 1.00 42.96  ? 447 LEU   A N   1 
ATOM   3143 C CA  . LEU   A 1 447 ? -29.615 -14.818 -22.101 1.00 47.19  ? 447 LEU   A CA  1 
ATOM   3144 C C   . LEU   A 1 447 ? -30.154 -15.816 -21.082 1.00 46.51  ? 447 LEU   A C   1 
ATOM   3145 O O   . LEU   A 1 447 ? -31.084 -15.500 -20.328 1.00 46.96  ? 447 LEU   A O   1 
ATOM   3146 C CB  . LEU   A 1 447 ? -30.244 -15.046 -23.474 1.00 47.32  ? 447 LEU   A CB  1 
ATOM   3147 C CG  . LEU   A 1 447 ? -29.945 -13.930 -24.477 1.00 48.08  ? 447 LEU   A CG  1 
ATOM   3148 C CD1 . LEU   A 1 447 ? -30.203 -14.392 -25.903 1.00 46.74  ? 447 LEU   A CD1 1 
ATOM   3149 C CD2 . LEU   A 1 447 ? -30.757 -12.684 -24.151 1.00 45.00  ? 447 LEU   A CD2 1 
ATOM   3150 N N   . VAL   A 1 448 ? -29.590 -17.026 -21.051 1.00 44.36  ? 448 VAL   A N   1 
ATOM   3151 C CA  . VAL   A 1 448 ? -29.958 -17.998 -20.023 1.00 42.38  ? 448 VAL   A CA  1 
ATOM   3152 C C   . VAL   A 1 448 ? -29.672 -17.432 -18.639 1.00 45.49  ? 448 VAL   A C   1 
ATOM   3153 O O   . VAL   A 1 448 ? -30.499 -17.529 -17.724 1.00 47.77  ? 448 VAL   A O   1 
ATOM   3154 C CB  . VAL   A 1 448 ? -29.214 -19.327 -20.248 1.00 41.89  ? 448 VAL   A CB  1 
ATOM   3155 C CG1 . VAL   A 1 448 ? -29.372 -20.242 -19.039 1.00 44.12  ? 448 VAL   A CG1 1 
ATOM   3156 C CG2 . VAL   A 1 448 ? -29.709 -20.011 -21.506 1.00 40.75  ? 448 VAL   A CG2 1 
ATOM   3157 N N   . ALA   A 1 449 ? -28.493 -16.828 -18.469 1.00 46.82  ? 449 ALA   A N   1 
ATOM   3158 C CA  . ALA   A 1 449 ? -28.127 -16.256 -17.177 1.00 49.20  ? 449 ALA   A CA  1 
ATOM   3159 C C   . ALA   A 1 449 ? -29.117 -15.182 -16.747 1.00 50.39  ? 449 ALA   A C   1 
ATOM   3160 O O   . ALA   A 1 449 ? -29.462 -15.084 -15.564 1.00 50.24  ? 449 ALA   A O   1 
ATOM   3161 C CB  . ALA   A 1 449 ? -26.710 -15.688 -17.238 1.00 40.96  ? 449 ALA   A CB  1 
ATOM   3162 N N   . GLU   A 1 450 ? -29.589 -14.369 -17.695 1.00 53.63  ? 450 GLU   A N   1 
ATOM   3163 C CA  . GLU   A 1 450 ? -30.603 -13.370 -17.369 1.00 53.49  ? 450 GLU   A CA  1 
ATOM   3164 C C   . GLU   A 1 450 ? -31.952 -14.019 -17.085 1.00 52.16  ? 450 GLU   A C   1 
ATOM   3165 O O   . GLU   A 1 450 ? -32.650 -13.624 -16.144 1.00 53.83  ? 450 GLU   A O   1 
ATOM   3166 C CB  . GLU   A 1 450 ? -30.725 -12.352 -18.502 1.00 52.40  ? 450 GLU   A CB  1 
ATOM   3167 C CG  . GLU   A 1 450 ? -29.618 -11.320 -18.508 1.00 58.64  ? 450 GLU   A CG  1 
ATOM   3168 C CD  . GLU   A 1 450 ? -29.498 -10.602 -17.176 1.00 66.34  ? 450 GLU   A CD  1 
ATOM   3169 O OE1 . GLU   A 1 450 ? -30.540 -10.179 -16.628 1.00 68.88  ? 450 GLU   A OE1 1 
ATOM   3170 O OE2 . GLU   A 1 450 ? -28.362 -10.470 -16.672 1.00 65.83  ? 450 GLU   A OE2 1 
ATOM   3171 N N   . ALA   A 1 451 ? -32.333 -15.019 -17.886 1.00 52.25  ? 451 ALA   A N   1 
ATOM   3172 C CA  . ALA   A 1 451 ? -33.605 -15.710 -17.694 1.00 51.20  ? 451 ALA   A CA  1 
ATOM   3173 C C   . ALA   A 1 451 ? -33.707 -16.393 -16.336 1.00 52.87  ? 451 ALA   A C   1 
ATOM   3174 O O   . ALA   A 1 451 ? -34.822 -16.600 -15.843 1.00 57.96  ? 451 ALA   A O   1 
ATOM   3175 C CB  . ALA   A 1 451 ? -33.813 -16.738 -18.807 1.00 47.21  ? 451 ALA   A CB  1 
ATOM   3176 N N   . LEU   A 1 452 ? -32.578 -16.751 -15.723 1.00 52.54  ? 452 LEU   A N   1 
ATOM   3177 C CA  . LEU   A 1 452 ? -32.606 -17.359 -14.399 1.00 55.43  ? 452 LEU   A CA  1 
ATOM   3178 C C   . LEU   A 1 452 ? -32.739 -16.332 -13.286 1.00 55.88  ? 452 LEU   A C   1 
ATOM   3179 O O   . LEU   A 1 452 ? -33.161 -16.692 -12.182 1.00 57.05  ? 452 LEU   A O   1 
ATOM   3180 C CB  . LEU   A 1 452 ? -31.354 -18.206 -14.186 1.00 50.91  ? 452 LEU   A CB  1 
ATOM   3181 C CG  . LEU   A 1 452 ? -31.281 -19.384 -15.153 1.00 48.92  ? 452 LEU   A CG  1 
ATOM   3182 C CD1 . LEU   A 1 452 ? -29.846 -19.816 -15.358 1.00 43.04  ? 452 LEU   A CD1 1 
ATOM   3183 C CD2 . LEU   A 1 452 ? -32.147 -20.538 -14.665 1.00 45.15  ? 452 LEU   A CD2 1 
ATOM   3184 N N   . ASP   A 1 453 ? -32.389 -15.069 -13.547 1.00 56.32  ? 453 ASP   A N   1 
ATOM   3185 C CA  . ASP   A 1 453 ? -32.653 -14.008 -12.585 1.00 62.80  ? 453 ASP   A CA  1 
ATOM   3186 C C   . ASP   A 1 453 ? -34.136 -13.689 -12.494 1.00 67.92  ? 453 ASP   A C   1 
ATOM   3187 O O   . ASP   A 1 453 ? -34.570 -13.088 -11.506 1.00 67.99  ? 453 ASP   A O   1 
ATOM   3188 C CB  . ASP   A 1 453 ? -31.869 -12.747 -12.954 1.00 64.00  ? 453 ASP   A CB  1 
ATOM   3189 C CG  . ASP   A 1 453 ? -30.381 -12.893 -12.701 1.00 67.19  ? 453 ASP   A CG  1 
ATOM   3190 O OD1 . ASP   A 1 453 ? -29.998 -13.844 -11.984 1.00 70.78  ? 453 ASP   A OD1 1 
ATOM   3191 O OD2 . ASP   A 1 453 ? -29.600 -12.056 -13.207 1.00 67.50  ? 453 ASP   A OD2 1 
ATOM   3192 N N   . ARG   A 1 454 ? -34.918 -14.081 -13.495 1.00 65.18  ? 454 ARG   A N   1 
ATOM   3193 C CA  . ARG   A 1 454 ? -36.360 -13.895 -13.451 1.00 65.86  ? 454 ARG   A CA  1 
ATOM   3194 C C   . ARG   A 1 454 ? -37.002 -14.920 -12.517 1.00 67.73  ? 454 ARG   A C   1 
ATOM   3195 O O   . ARG   A 1 454 ? -37.005 -16.121 -12.801 1.00 64.59  ? 454 ARG   A O   1 
ATOM   3196 C CB  . ARG   A 1 454 ? -36.970 -14.004 -14.850 1.00 63.83  ? 454 ARG   A CB  1 
ATOM   3197 C CG  . ARG   A 1 454 ? -37.345 -12.661 -15.458 1.00 66.82  ? 454 ARG   A CG  1 
ATOM   3198 C CD  . ARG   A 1 454 ? -37.807 -12.794 -16.891 1.00 68.92  ? 454 ARG   A CD  1 
ATOM   3199 N NE  . ARG   A 1 454 ? -36.748 -13.155 -17.824 1.00 68.82  ? 454 ARG   A NE  1 
ATOM   3200 C CZ  . ARG   A 1 454 ? -36.912 -13.227 -19.138 1.00 69.85  ? 454 ARG   A CZ  1 
ATOM   3201 N NH1 . ARG   A 1 454 ? -38.084 -12.981 -19.703 1.00 72.67  ? 454 ARG   A NH1 1 
ATOM   3202 N NH2 . ARG   A 1 454 ? -35.877 -13.558 -19.905 1.00 64.46  ? 454 ARG   A NH2 1 
ATOM   3203 N N   . SER   B 1 17  ? -16.197 -9.331  -73.068 1.00 58.59  ? 17  SER   B N   1 
ATOM   3204 C CA  . SER   B 1 17  ? -17.178 -9.532  -74.129 1.00 60.16  ? 17  SER   B CA  1 
ATOM   3205 C C   . SER   B 1 17  ? -18.444 -10.192 -73.585 1.00 59.82  ? 17  SER   B C   1 
ATOM   3206 O O   . SER   B 1 17  ? -19.544 -9.655  -73.729 1.00 60.16  ? 17  SER   B O   1 
ATOM   3207 C CB  . SER   B 1 17  ? -16.585 -10.374 -75.259 1.00 61.09  ? 17  SER   B CB  1 
ATOM   3208 O OG  . SER   B 1 17  ? -17.577 -11.186 -75.864 1.00 61.00  ? 17  SER   B OG  1 
ATOM   3209 N N   . GLU   B 1 18  ? -18.287 -11.359 -72.966 1.00 54.94  ? 18  GLU   B N   1 
ATOM   3210 C CA  . GLU   B 1 18  ? -19.411 -12.010 -72.313 1.00 52.37  ? 18  GLU   B CA  1 
ATOM   3211 C C   . GLU   B 1 18  ? -19.721 -11.322 -70.984 1.00 50.44  ? 18  GLU   B C   1 
ATOM   3212 O O   . GLU   B 1 18  ? -18.879 -10.636 -70.395 1.00 54.40  ? 18  GLU   B O   1 
ATOM   3213 C CB  . GLU   B 1 18  ? -19.116 -13.492 -72.072 1.00 47.53  ? 18  GLU   B CB  1 
ATOM   3214 C CG  . GLU   B 1 18  ? -19.008 -14.359 -73.326 1.00 49.35  ? 18  GLU   B CG  1 
ATOM   3215 C CD  . GLU   B 1 18  ? -20.151 -14.155 -74.302 1.00 49.28  ? 18  GLU   B CD  1 
ATOM   3216 O OE1 . GLU   B 1 18  ? -21.315 -14.077 -73.857 1.00 50.72  ? 18  GLU   B OE1 1 
ATOM   3217 O OE2 . GLU   B 1 18  ? -19.887 -14.105 -75.523 1.00 52.42  ? 18  GLU   B OE2 1 
ATOM   3218 N N   . LEU   B 1 19  ? -20.948 -11.512 -70.512 1.00 46.42  ? 19  LEU   B N   1 
ATOM   3219 C CA  . LEU   B 1 19  ? -21.329 -10.982 -69.212 1.00 47.15  ? 19  LEU   B CA  1 
ATOM   3220 C C   . LEU   B 1 19  ? -20.710 -11.811 -68.091 1.00 45.09  ? 19  LEU   B C   1 
ATOM   3221 O O   . LEU   B 1 19  ? -20.465 -13.012 -68.237 1.00 43.88  ? 19  LEU   B O   1 
ATOM   3222 C CB  . LEU   B 1 19  ? -22.851 -10.962 -69.066 1.00 45.25  ? 19  LEU   B CB  1 
ATOM   3223 C CG  . LEU   B 1 19  ? -23.556 -9.806  -69.767 1.00 45.75  ? 19  LEU   B CG  1 
ATOM   3224 C CD1 . LEU   B 1 19  ? -25.032 -9.784  -69.405 1.00 45.17  ? 19  LEU   B CD1 1 
ATOM   3225 C CD2 . LEU   B 1 19  ? -22.885 -8.498  -69.395 1.00 48.87  ? 19  LEU   B CD2 1 
ATOM   3226 N N   . SER   B 1 20  ? -20.452 -11.155 -66.964 1.00 43.38  ? 20  SER   B N   1 
ATOM   3227 C CA  . SER   B 1 20  ? -19.948 -11.818 -65.771 1.00 42.05  ? 20  SER   B CA  1 
ATOM   3228 C C   . SER   B 1 20  ? -21.108 -12.312 -64.906 1.00 42.27  ? 20  SER   B C   1 
ATOM   3229 O O   . SER   B 1 20  ? -22.272 -11.979 -65.134 1.00 43.69  ? 20  SER   B O   1 
ATOM   3230 C CB  . SER   B 1 20  ? -19.050 -10.872 -64.977 1.00 40.69  ? 20  SER   B CB  1 
ATOM   3231 O OG  . SER   B 1 20  ? -19.788 -10.216 -63.963 1.00 43.59  ? 20  SER   B OG  1 
ATOM   3232 N N   . ALA   B 1 21  ? -20.776 -13.119 -63.893 1.00 42.30  ? 21  ALA   B N   1 
ATOM   3233 C CA  . ALA   B 1 21  ? -21.817 -13.679 -63.033 1.00 44.79  ? 21  ALA   B CA  1 
ATOM   3234 C C   . ALA   B 1 21  ? -22.569 -12.581 -62.292 1.00 42.06  ? 21  ALA   B C   1 
ATOM   3235 O O   . ALA   B 1 21  ? -23.802 -12.612 -62.201 1.00 43.24  ? 21  ALA   B O   1 
ATOM   3236 C CB  . ALA   B 1 21  ? -21.212 -14.679 -62.047 1.00 42.79  ? 21  ALA   B CB  1 
ATOM   3237 N N   . ILE   B 1 22  ? -21.841 -11.600 -61.759 1.00 40.80  ? 22  ILE   B N   1 
ATOM   3238 C CA  . ILE   B 1 22  ? -22.485 -10.458 -61.123 1.00 40.88  ? 22  ILE   B CA  1 
ATOM   3239 C C   . ILE   B 1 22  ? -23.285 -9.661  -62.149 1.00 42.03  ? 22  ILE   B C   1 
ATOM   3240 O O   . ILE   B 1 22  ? -24.435 -9.277  -61.899 1.00 38.21  ? 22  ILE   B O   1 
ATOM   3241 C CB  . ILE   B 1 22  ? -21.425 -9.593  -60.414 1.00 42.21  ? 22  ILE   B CB  1 
ATOM   3242 C CG1 . ILE   B 1 22  ? -21.026 -10.235 -59.082 1.00 44.53  ? 22  ILE   B CG1 1 
ATOM   3243 C CG2 . ILE   B 1 22  ? -21.933 -8.181  -60.194 1.00 37.29  ? 22  ILE   B CG2 1 
ATOM   3244 C CD1 . ILE   B 1 22  ? -19.608 -9.920  -58.639 1.00 37.27  ? 22  ILE   B CD1 1 
ATOM   3245 N N   . GLU   B 1 23  ? -22.699 -9.412  -63.323 1.00 44.39  ? 23  GLU   B N   1 
ATOM   3246 C CA  . GLU   B 1 23  ? -23.424 -8.711  -64.381 1.00 44.88  ? 23  GLU   B CA  1 
ATOM   3247 C C   . GLU   B 1 23  ? -24.662 -9.490  -64.806 1.00 42.66  ? 23  GLU   B C   1 
ATOM   3248 O O   . GLU   B 1 23  ? -25.742 -8.915  -64.986 1.00 41.48  ? 23  GLU   B O   1 
ATOM   3249 C CB  . GLU   B 1 23  ? -22.505 -8.471  -65.579 1.00 43.70  ? 23  GLU   B CB  1 
ATOM   3250 C CG  . GLU   B 1 23  ? -21.352 -7.537  -65.290 1.00 46.23  ? 23  GLU   B CG  1 
ATOM   3251 C CD  . GLU   B 1 23  ? -20.401 -7.404  -66.461 1.00 46.80  ? 23  GLU   B CD  1 
ATOM   3252 O OE1 . GLU   B 1 23  ? -20.404 -8.292  -67.339 1.00 48.27  ? 23  GLU   B OE1 1 
ATOM   3253 O OE2 . GLU   B 1 23  ? -19.647 -6.411  -66.501 1.00 53.08  ? 23  GLU   B OE2 1 
ATOM   3254 N N   . THR   B 1 24  ? -24.518 -10.806 -64.978 1.00 41.07  ? 24  THR   B N   1 
ATOM   3255 C CA  . THR   B 1 24  ? -25.664 -11.649 -65.304 1.00 40.35  ? 24  THR   B CA  1 
ATOM   3256 C C   . THR   B 1 24  ? -26.751 -11.529 -64.245 1.00 43.54  ? 24  THR   B C   1 
ATOM   3257 O O   . THR   B 1 24  ? -27.935 -11.376 -64.567 1.00 45.43  ? 24  THR   B O   1 
ATOM   3258 C CB  . THR   B 1 24  ? -25.220 -13.106 -65.450 1.00 44.84  ? 24  THR   B CB  1 
ATOM   3259 O OG1 . THR   B 1 24  ? -24.152 -13.199 -66.404 1.00 44.82  ? 24  THR   B OG1 1 
ATOM   3260 C CG2 . THR   B 1 24  ? -26.381 -13.975 -65.897 1.00 41.47  ? 24  THR   B CG2 1 
ATOM   3261 N N   . ALA   B 1 25  ? -26.364 -11.591 -62.967 1.00 39.77  ? 25  ALA   B N   1 
ATOM   3262 C CA  . ALA   B 1 25  ? -27.344 -11.479 -61.892 1.00 41.12  ? 25  ALA   B CA  1 
ATOM   3263 C C   . ALA   B 1 25  ? -28.051 -10.129 -61.925 1.00 40.83  ? 25  ALA   B C   1 
ATOM   3264 O O   . ALA   B 1 25  ? -29.251 -10.041 -61.640 1.00 39.39  ? 25  ALA   B O   1 
ATOM   3265 C CB  . ALA   B 1 25  ? -26.666 -11.697 -60.539 1.00 38.43  ? 25  ALA   B CB  1 
ATOM   3266 N N   . ALA   B 1 26  ? -27.323 -9.067  -62.278 1.00 39.38  ? 26  ALA   B N   1 
ATOM   3267 C CA  . ALA   B 1 26  ? -27.928 -7.739  -62.337 1.00 42.06  ? 26  ALA   B CA  1 
ATOM   3268 C C   . ALA   B 1 26  ? -28.913 -7.630  -63.494 1.00 44.84  ? 26  ALA   B C   1 
ATOM   3269 O O   . ALA   B 1 26  ? -29.994 -7.050  -63.342 1.00 44.86  ? 26  ALA   B O   1 
ATOM   3270 C CB  . ALA   B 1 26  ? -26.839 -6.674  -62.456 1.00 41.00  ? 26  ALA   B CB  1 
ATOM   3271 N N   . ALA   B 1 27  ? -28.555 -8.186  -64.655 1.00 42.75  ? 27  ALA   B N   1 
ATOM   3272 C CA  . ALA   B 1 27  ? -29.450 -8.145  -65.808 1.00 45.01  ? 27  ALA   B CA  1 
ATOM   3273 C C   . ALA   B 1 27  ? -30.749 -8.894  -65.532 1.00 47.87  ? 27  ALA   B C   1 
ATOM   3274 O O   . ALA   B 1 27  ? -31.824 -8.468  -65.971 1.00 48.91  ? 27  ALA   B O   1 
ATOM   3275 C CB  . ALA   B 1 27  ? -28.745 -8.722  -67.035 1.00 43.80  ? 27  ALA   B CB  1 
ATOM   3276 N N   . ILE   B 1 28  ? -30.673 -10.017 -64.813 1.00 45.02  ? 28  ILE   B N   1 
ATOM   3277 C CA  . ILE   B 1 28  ? -31.885 -10.755 -64.470 1.00 46.33  ? 28  ILE   B CA  1 
ATOM   3278 C C   . ILE   B 1 28  ? -32.695 -9.986  -63.437 1.00 48.34  ? 28  ILE   B C   1 
ATOM   3279 O O   . ILE   B 1 28  ? -33.917 -9.838  -63.565 1.00 51.41  ? 28  ILE   B O   1 
ATOM   3280 C CB  . ILE   B 1 28  ? -31.542 -12.172 -63.973 1.00 45.69  ? 28  ILE   B CB  1 
ATOM   3281 C CG1 . ILE   B 1 28  ? -30.807 -12.962 -65.055 1.00 48.12  ? 28  ILE   B CG1 1 
ATOM   3282 C CG2 . ILE   B 1 28  ? -32.797 -12.913 -63.545 1.00 49.05  ? 28  ILE   B CG2 1 
ATOM   3283 C CD1 . ILE   B 1 28  ? -29.811 -13.949 -64.505 1.00 46.80  ? 28  ILE   B CD1 1 
ATOM   3284 N N   . ALA   B 1 29  ? -32.023 -9.484  -62.399 1.00 47.21  ? 29  ALA   B N   1 
ATOM   3285 C CA  . ALA   B 1 29  ? -32.703 -8.692  -61.380 1.00 48.14  ? 29  ALA   B CA  1 
ATOM   3286 C C   . ALA   B 1 29  ? -33.363 -7.463  -61.994 1.00 45.58  ? 29  ALA   B C   1 
ATOM   3287 O O   . ALA   B 1 29  ? -34.530 -7.168  -61.719 1.00 47.56  ? 29  ALA   B O   1 
ATOM   3288 C CB  . ALA   B 1 29  ? -31.713 -8.289  -60.285 1.00 43.94  ? 29  ALA   B CB  1 
ATOM   3289 N N   . GLY   B 1 30  ? -32.632 -6.737  -62.841 1.00 46.72  ? 30  GLY   B N   1 
ATOM   3290 C CA  . GLY   B 1 30  ? -33.207 -5.580  -63.504 1.00 51.82  ? 30  GLY   B CA  1 
ATOM   3291 C C   . GLY   B 1 30  ? -34.302 -5.917  -64.495 1.00 54.36  ? 30  GLY   B C   1 
ATOM   3292 O O   . GLY   B 1 30  ? -35.128 -5.053  -64.811 1.00 53.95  ? 30  GLY   B O   1 
ATOM   3293 N N   . GLY   B 1 31  ? -34.337 -7.151  -64.983 1.00 51.71  ? 31  GLY   B N   1 
ATOM   3294 C CA  . GLY   B 1 31  ? -35.302 -7.529  -65.989 1.00 55.48  ? 31  GLY   B CA  1 
ATOM   3295 C C   . GLY   B 1 31  ? -34.856 -7.319  -67.416 1.00 54.98  ? 31  GLY   B C   1 
ATOM   3296 O O   . GLY   B 1 31  ? -35.696 -7.371  -68.322 1.00 56.07  ? 31  GLY   B O   1 
ATOM   3297 N N   . SER   B 1 32  ? -33.565 -7.060  -67.647 1.00 50.84  ? 32  SER   B N   1 
ATOM   3298 C CA  . SER   B 1 32  ? -33.050 -7.066  -69.012 1.00 53.11  ? 32  SER   B CA  1 
ATOM   3299 C C   . SER   B 1 32  ? -33.259 -8.423  -69.666 1.00 54.45  ? 32  SER   B C   1 
ATOM   3300 O O   . SER   B 1 32  ? -33.429 -8.510  -70.887 1.00 57.82  ? 32  SER   B O   1 
ATOM   3301 C CB  . SER   B 1 32  ? -31.566 -6.697  -69.016 1.00 53.44  ? 32  SER   B CB  1 
ATOM   3302 O OG  . SER   B 1 32  ? -31.272 -5.744  -68.008 1.00 60.23  ? 32  SER   B OG  1 
ATOM   3303 N N   . MET   B 1 33  ? -33.250 -9.487  -68.868 1.00 55.86  ? 33  MET   B N   1 
ATOM   3304 C CA  . MET   B 1 33  ? -33.529 -10.836 -69.335 1.00 53.91  ? 33  MET   B CA  1 
ATOM   3305 C C   . MET   B 1 33  ? -34.043 -11.637 -68.149 1.00 52.91  ? 33  MET   B C   1 
ATOM   3306 O O   . MET   B 1 33  ? -33.793 -11.291 -66.992 1.00 54.60  ? 33  MET   B O   1 
ATOM   3307 C CB  . MET   B 1 33  ? -32.283 -11.493 -69.938 1.00 53.59  ? 33  MET   B CB  1 
ATOM   3308 C CG  . MET   B 1 33  ? -31.242 -11.897 -68.901 1.00 54.44  ? 33  MET   B CG  1 
ATOM   3309 S SD  . MET   B 1 33  ? -29.556 -11.936 -69.537 1.00 66.09  ? 33  MET   B SD  1 
ATOM   3310 C CE  . MET   B 1 33  ? -29.841 -12.490 -71.217 1.00 58.20  ? 33  MET   B CE  1 
ATOM   3311 N N   . THR   B 1 34  ? -34.778 -12.703 -68.447 1.00 51.83  ? 34  THR   B N   1 
ATOM   3312 C CA  . THR   B 1 34  ? -35.204 -13.624 -67.405 1.00 52.23  ? 34  THR   B CA  1 
ATOM   3313 C C   . THR   B 1 34  ? -34.116 -14.667 -67.154 1.00 51.66  ? 34  THR   B C   1 
ATOM   3314 O O   . THR   B 1 34  ? -33.157 -14.803 -67.918 1.00 50.02  ? 34  THR   B O   1 
ATOM   3315 C CB  . THR   B 1 34  ? -36.525 -14.304 -67.779 1.00 53.20  ? 34  THR   B CB  1 
ATOM   3316 O OG1 . THR   B 1 34  ? -36.284 -15.333 -68.747 1.00 54.96  ? 34  THR   B OG1 1 
ATOM   3317 C CG2 . THR   B 1 34  ? -37.520 -13.295 -68.339 1.00 50.84  ? 34  THR   B CG2 1 
ATOM   3318 N N   . ALA   B 1 35  ? -34.268 -15.404 -66.051 1.00 51.05  ? 35  ALA   B N   1 
ATOM   3319 C CA  . ALA   B 1 35  ? -33.326 -16.480 -65.755 1.00 48.84  ? 35  ALA   B CA  1 
ATOM   3320 C C   . ALA   B 1 35  ? -33.412 -17.597 -66.786 1.00 49.71  ? 35  ALA   B C   1 
ATOM   3321 O O   . ALA   B 1 35  ? -32.396 -18.231 -67.099 1.00 48.80  ? 35  ALA   B O   1 
ATOM   3322 C CB  . ALA   B 1 35  ? -33.578 -17.032 -64.354 1.00 48.72  ? 35  ALA   B CB  1 
ATOM   3323 N N   . LEU   B 1 36  ? -34.607 -17.846 -67.328 1.00 49.88  ? 36  LEU   B N   1 
ATOM   3324 C CA  . LEU   B 1 36  ? -34.747 -18.851 -68.376 1.00 49.37  ? 36  LEU   B CA  1 
ATOM   3325 C C   . LEU   B 1 36  ? -33.999 -18.434 -69.636 1.00 49.55  ? 36  LEU   B C   1 
ATOM   3326 O O   . LEU   B 1 36  ? -33.390 -19.272 -70.312 1.00 47.17  ? 36  LEU   B O   1 
ATOM   3327 C CB  . LEU   B 1 36  ? -36.227 -19.087 -68.677 1.00 47.91  ? 36  LEU   B CB  1 
ATOM   3328 C CG  . LEU   B 1 36  ? -36.582 -20.188 -69.677 1.00 47.22  ? 36  LEU   B CG  1 
ATOM   3329 C CD1 . LEU   B 1 36  ? -35.990 -21.523 -69.256 1.00 47.08  ? 36  LEU   B CD1 1 
ATOM   3330 C CD2 . LEU   B 1 36  ? -38.090 -20.290 -69.828 1.00 44.48  ? 36  LEU   B CD2 1 
ATOM   3331 N N   . GLU   B 1 37  ? -34.020 -17.138 -69.959 1.00 50.07  ? 37  GLU   B N   1 
ATOM   3332 C CA  . GLU   B 1 37  ? -33.319 -16.658 -71.146 1.00 48.78  ? 37  GLU   B CA  1 
ATOM   3333 C C   . GLU   B 1 37  ? -31.807 -16.721 -70.963 1.00 48.62  ? 37  GLU   B C   1 
ATOM   3334 O O   . GLU   B 1 37  ? -31.084 -17.135 -71.876 1.00 49.04  ? 37  GLU   B O   1 
ATOM   3335 C CB  . GLU   B 1 37  ? -33.764 -15.235 -71.472 1.00 50.79  ? 37  GLU   B CB  1 
ATOM   3336 C CG  . GLU   B 1 37  ? -35.074 -15.166 -72.238 1.00 53.78  ? 37  GLU   B CG  1 
ATOM   3337 C CD  . GLU   B 1 37  ? -35.798 -13.851 -72.029 1.00 59.03  ? 37  GLU   B CD  1 
ATOM   3338 O OE1 . GLU   B 1 37  ? -35.137 -12.863 -71.643 1.00 59.19  ? 37  GLU   B OE1 1 
ATOM   3339 O OE2 . GLU   B 1 37  ? -37.029 -13.808 -72.241 1.00 63.06  ? 37  GLU   B OE2 1 
ATOM   3340 N N   . ALA   B 1 38  ? -31.309 -16.309 -69.794 1.00 49.58  ? 38  ALA   B N   1 
ATOM   3341 C CA  . ALA   B 1 38  ? -29.881 -16.435 -69.519 1.00 45.94  ? 38  ALA   B CA  1 
ATOM   3342 C C   . ALA   B 1 38  ? -29.451 -17.895 -69.532 1.00 48.03  ? 38  ALA   B C   1 
ATOM   3343 O O   . ALA   B 1 38  ? -28.347 -18.224 -69.985 1.00 45.40  ? 38  ALA   B O   1 
ATOM   3344 C CB  . ALA   B 1 38  ? -29.538 -15.790 -68.177 1.00 46.82  ? 38  ALA   B CB  1 
ATOM   3345 N N   . CYS   B 1 39  ? -30.313 -18.786 -69.040 1.00 47.67  ? 39  CYS   B N   1 
ATOM   3346 C CA  . CYS   B 1 39  ? -30.008 -20.210 -69.091 1.00 45.08  ? 39  CYS   B CA  1 
ATOM   3347 C C   . CYS   B 1 39  ? -29.964 -20.704 -70.532 1.00 44.75  ? 39  CYS   B C   1 
ATOM   3348 O O   . CYS   B 1 39  ? -29.023 -21.400 -70.931 1.00 45.19  ? 39  CYS   B O   1 
ATOM   3349 C CB  . CYS   B 1 39  ? -31.037 -20.994 -68.280 1.00 48.05  ? 39  CYS   B CB  1 
ATOM   3350 S SG  . CYS   B 1 39  ? -30.941 -22.775 -68.512 1.00 50.46  ? 39  CYS   B SG  1 
ATOM   3351 N N   . ASP   B 1 40  ? -30.974 -20.345 -71.332 1.00 45.76  ? 40  ASP   B N   1 
ATOM   3352 C CA  . ASP   B 1 40  ? -30.987 -20.743 -72.737 1.00 43.55  ? 40  ASP   B CA  1 
ATOM   3353 C C   . ASP   B 1 40  ? -29.818 -20.128 -73.495 1.00 44.42  ? 40  ASP   B C   1 
ATOM   3354 O O   . ASP   B 1 40  ? -29.247 -20.761 -74.390 1.00 45.72  ? 40  ASP   B O   1 
ATOM   3355 C CB  . ASP   B 1 40  ? -32.312 -20.345 -73.389 1.00 44.31  ? 40  ASP   B CB  1 
ATOM   3356 C CG  . ASP   B 1 40  ? -33.460 -21.261 -72.996 1.00 49.49  ? 40  ASP   B CG  1 
ATOM   3357 O OD1 . ASP   B 1 40  ? -33.214 -22.464 -72.762 1.00 50.57  ? 40  ASP   B OD1 1 
ATOM   3358 O OD2 . ASP   B 1 40  ? -34.610 -20.778 -72.924 1.00 50.24  ? 40  ASP   B OD2 1 
ATOM   3359 N N   . ALA   B 1 41  ? -29.450 -18.891 -73.153 1.00 45.15  ? 41  ALA   B N   1 
ATOM   3360 C CA  . ALA   B 1 41  ? -28.313 -18.253 -73.809 1.00 44.69  ? 41  ALA   B CA  1 
ATOM   3361 C C   . ALA   B 1 41  ? -27.019 -18.990 -73.499 1.00 43.85  ? 41  ALA   B C   1 
ATOM   3362 O O   . ALA   B 1 41  ? -26.152 -19.132 -74.369 1.00 46.61  ? 41  ALA   B O   1 
ATOM   3363 C CB  . ALA   B 1 41  ? -28.214 -16.788 -73.384 1.00 42.55  ? 41  ALA   B CB  1 
ATOM   3364 N N   . ALA   B 1 42  ? -26.869 -19.467 -72.262 1.00 44.16  ? 42  ALA   B N   1 
ATOM   3365 C CA  . ALA   B 1 42  ? -25.673 -20.220 -71.904 1.00 44.47  ? 42  ALA   B CA  1 
ATOM   3366 C C   . ALA   B 1 42  ? -25.657 -21.581 -72.588 1.00 42.96  ? 42  ALA   B C   1 
ATOM   3367 O O   . ALA   B 1 42  ? -24.614 -22.012 -73.096 1.00 43.38  ? 42  ALA   B O   1 
ATOM   3368 C CB  . ALA   B 1 42  ? -25.583 -20.372 -70.385 1.00 37.72  ? 42  ALA   B CB  1 
ATOM   3369 N N   . ILE   B 1 43  ? -26.803 -22.268 -72.612 1.00 43.60  ? 43  ILE   B N   1 
ATOM   3370 C CA  . ILE   B 1 43  ? -26.901 -23.547 -73.312 1.00 44.25  ? 43  ILE   B CA  1 
ATOM   3371 C C   . ILE   B 1 43  ? -26.515 -23.381 -74.776 1.00 45.28  ? 43  ILE   B C   1 
ATOM   3372 O O   . ILE   B 1 43  ? -25.769 -24.195 -75.336 1.00 44.87  ? 43  ILE   B O   1 
ATOM   3373 C CB  . ILE   B 1 43  ? -28.321 -24.129 -73.164 1.00 45.25  ? 43  ILE   B CB  1 
ATOM   3374 C CG1 . ILE   B 1 43  ? -28.556 -24.628 -71.738 1.00 42.48  ? 43  ILE   B CG1 1 
ATOM   3375 C CG2 . ILE   B 1 43  ? -28.554 -25.253 -74.163 1.00 46.80  ? 43  ILE   B CG2 1 
ATOM   3376 C CD1 . ILE   B 1 43  ? -30.001 -24.948 -71.444 1.00 39.24  ? 43  ILE   B CD1 1 
ATOM   3377 N N   . ALA   B 1 44  ? -27.006 -22.315 -75.414 1.00 44.83  ? 44  ALA   B N   1 
ATOM   3378 C CA  . ALA   B 1 44  ? -26.672 -22.066 -76.812 1.00 44.50  ? 44  ALA   B CA  1 
ATOM   3379 C C   . ALA   B 1 44  ? -25.181 -21.816 -76.989 1.00 46.56  ? 44  ALA   B C   1 
ATOM   3380 O O   . ALA   B 1 44  ? -24.575 -22.293 -77.956 1.00 47.97  ? 44  ALA   B O   1 
ATOM   3381 C CB  . ALA   B 1 44  ? -27.479 -20.880 -77.338 1.00 44.30  ? 44  ALA   B CB  1 
ATOM   3382 N N   . ARG   B 1 45  ? -24.571 -21.064 -76.069 1.00 46.91  ? 45  ARG   B N   1 
ATOM   3383 C CA  . ARG   B 1 45  ? -23.138 -20.802 -76.167 1.00 46.00  ? 45  ARG   B CA  1 
ATOM   3384 C C   . ARG   B 1 45  ? -22.336 -22.088 -76.022 1.00 46.62  ? 45  ARG   B C   1 
ATOM   3385 O O   . ARG   B 1 45  ? -21.297 -22.258 -76.673 1.00 46.39  ? 45  ARG   B O   1 
ATOM   3386 C CB  . ARG   B 1 45  ? -22.716 -19.778 -75.113 1.00 46.01  ? 45  ARG   B CB  1 
ATOM   3387 C CG  . ARG   B 1 45  ? -22.981 -18.335 -75.516 1.00 47.59  ? 45  ARG   B CG  1 
ATOM   3388 C CD  . ARG   B 1 45  ? -22.386 -17.348 -74.521 1.00 46.25  ? 45  ARG   B CD  1 
ATOM   3389 N NE  . ARG   B 1 45  ? -22.574 -17.766 -73.136 1.00 44.56  ? 45  ARG   B NE  1 
ATOM   3390 C CZ  . ARG   B 1 45  ? -23.526 -17.302 -72.338 1.00 44.51  ? 45  ARG   B CZ  1 
ATOM   3391 N NH1 . ARG   B 1 45  ? -24.415 -16.420 -72.762 1.00 43.51  ? 45  ARG   B NH1 1 
ATOM   3392 N NH2 . ARG   B 1 45  ? -23.587 -17.734 -71.081 1.00 42.59  ? 45  ARG   B NH2 1 
ATOM   3393 N N   . ILE   B 1 46  ? -22.807 -23.009 -75.179 1.00 45.69  ? 46  ILE   B N   1 
ATOM   3394 C CA  . ILE   B 1 46  ? -22.136 -24.297 -75.033 1.00 48.84  ? 46  ILE   B CA  1 
ATOM   3395 C C   . ILE   B 1 46  ? -22.287 -25.124 -76.304 1.00 45.38  ? 46  ILE   B C   1 
ATOM   3396 O O   . ILE   B 1 46  ? -21.319 -25.713 -76.797 1.00 46.06  ? 46  ILE   B O   1 
ATOM   3397 C CB  . ILE   B 1 46  ? -22.673 -25.048 -73.800 1.00 48.47  ? 46  ILE   B CB  1 
ATOM   3398 C CG1 . ILE   B 1 46  ? -22.141 -24.416 -72.511 1.00 45.13  ? 46  ILE   B CG1 1 
ATOM   3399 C CG2 . ILE   B 1 46  ? -22.307 -26.528 -73.870 1.00 44.64  ? 46  ILE   B CG2 1 
ATOM   3400 C CD1 . ILE   B 1 46  ? -22.935 -24.788 -71.279 1.00 44.77  ? 46  ILE   B CD1 1 
ATOM   3401 N N   . GLU   B 1 47  ? -23.498 -25.173 -76.863 1.00 46.84  ? 47  GLU   B N   1 
ATOM   3402 C CA  . GLU   B 1 47  ? -23.706 -25.952 -78.079 1.00 50.07  ? 47  GLU   B CA  1 
ATOM   3403 C C   . GLU   B 1 47  ? -22.966 -25.355 -79.269 1.00 50.22  ? 47  GLU   B C   1 
ATOM   3404 O O   . GLU   B 1 47  ? -22.558 -26.093 -80.173 1.00 55.03  ? 47  GLU   B O   1 
ATOM   3405 C CB  . GLU   B 1 47  ? -25.196 -26.070 -78.380 1.00 49.63  ? 47  GLU   B CB  1 
ATOM   3406 C CG  . GLU   B 1 47  ? -25.788 -27.404 -77.962 1.00 53.51  ? 47  GLU   B CG  1 
ATOM   3407 C CD  . GLU   B 1 47  ? -27.209 -27.277 -77.463 1.00 58.28  ? 47  GLU   B CD  1 
ATOM   3408 O OE1 . GLU   B 1 47  ? -27.785 -26.174 -77.589 1.00 57.62  ? 47  GLU   B OE1 1 
ATOM   3409 O OE2 . GLU   B 1 47  ? -27.746 -28.276 -76.937 1.00 58.71  ? 47  GLU   B OE2 1 
ATOM   3410 N N   . GLN   B 1 48  ? -22.760 -24.038 -79.280 1.00 47.99  ? 48  GLN   B N   1 
ATOM   3411 C CA  . GLN   B 1 48  ? -22.082 -23.403 -80.405 1.00 49.17  ? 48  GLN   B CA  1 
ATOM   3412 C C   . GLN   B 1 48  ? -20.562 -23.499 -80.312 1.00 51.21  ? 48  GLN   B C   1 
ATOM   3413 O O   . GLN   B 1 48  ? -19.889 -23.511 -81.348 1.00 50.13  ? 48  GLN   B O   1 
ATOM   3414 C CB  . GLN   B 1 48  ? -22.495 -21.935 -80.510 1.00 52.54  ? 48  GLN   B CB  1 
ATOM   3415 C CG  . GLN   B 1 48  ? -23.558 -21.650 -81.559 1.00 58.56  ? 48  GLN   B CG  1 
ATOM   3416 C CD  . GLN   B 1 48  ? -24.926 -22.171 -81.167 1.00 60.75  ? 48  GLN   B CD  1 
ATOM   3417 O OE1 . GLN   B 1 48  ? -25.688 -21.492 -80.476 1.00 59.80  ? 48  GLN   B OE1 1 
ATOM   3418 N NE2 . GLN   B 1 48  ? -25.249 -23.380 -81.612 1.00 60.56  ? 48  GLN   B NE2 1 
ATOM   3419 N N   . ARG   B 1 49  ? -20.001 -23.578 -79.100 1.00 49.75  ? 49  ARG   B N   1 
ATOM   3420 C CA  . ARG   B 1 49  ? -18.560 -23.439 -78.920 1.00 46.29  ? 49  ARG   B CA  1 
ATOM   3421 C C   . ARG   B 1 49  ? -17.855 -24.672 -78.373 1.00 45.31  ? 49  ARG   B C   1 
ATOM   3422 O O   . ARG   B 1 49  ? -16.638 -24.784 -78.551 1.00 46.14  ? 49  ARG   B O   1 
ATOM   3423 C CB  . ARG   B 1 49  ? -18.250 -22.259 -77.985 1.00 47.66  ? 49  ARG   B CB  1 
ATOM   3424 C CG  . ARG   B 1 49  ? -18.801 -20.929 -78.462 1.00 51.42  ? 49  ARG   B CG  1 
ATOM   3425 C CD  . ARG   B 1 49  ? -19.102 -19.999 -77.305 1.00 48.02  ? 49  ARG   B CD  1 
ATOM   3426 N NE  . ARG   B 1 49  ? -19.848 -18.829 -77.748 1.00 51.19  ? 49  ARG   B NE  1 
ATOM   3427 C CZ  . ARG   B 1 49  ? -19.758 -17.628 -77.194 1.00 48.56  ? 49  ARG   B CZ  1 
ATOM   3428 N NH1 . ARG   B 1 49  ? -18.963 -17.401 -76.161 1.00 46.91  ? 49  ARG   B NH1 1 
ATOM   3429 N NH2 . ARG   B 1 49  ? -20.483 -16.630 -77.690 1.00 45.86  ? 49  ARG   B NH2 1 
ATOM   3430 N N   . ASP   B 1 50  ? -18.564 -25.587 -77.708 1.00 44.74  ? 50  ASP   B N   1 
ATOM   3431 C CA  . ASP   B 1 50  ? -17.888 -26.686 -77.022 1.00 46.97  ? 50  ASP   B CA  1 
ATOM   3432 C C   . ASP   B 1 50  ? -17.297 -27.713 -77.984 1.00 47.33  ? 50  ASP   B C   1 
ATOM   3433 O O   . ASP   B 1 50  ? -16.390 -28.453 -77.588 1.00 44.89  ? 50  ASP   B O   1 
ATOM   3434 C CB  . ASP   B 1 50  ? -18.851 -27.383 -76.057 1.00 46.69  ? 50  ASP   B CB  1 
ATOM   3435 C CG  . ASP   B 1 50  ? -18.135 -28.074 -74.907 1.00 47.13  ? 50  ASP   B CG  1 
ATOM   3436 O OD1 . ASP   B 1 50  ? -17.049 -27.596 -74.511 1.00 45.55  ? 50  ASP   B OD1 1 
ATOM   3437 O OD2 . ASP   B 1 50  ? -18.654 -29.093 -74.400 1.00 48.24  ? 50  ASP   B OD2 1 
ATOM   3438 N N   . GLY   B 1 51  ? -17.782 -27.766 -79.226 1.00 47.76  ? 51  GLY   B N   1 
ATOM   3439 C CA  . GLY   B 1 51  ? -17.380 -28.757 -80.202 1.00 43.61  ? 51  GLY   B CA  1 
ATOM   3440 C C   . GLY   B 1 51  ? -15.894 -29.059 -80.261 1.00 47.06  ? 51  GLY   B C   1 
ATOM   3441 O O   . GLY   B 1 51  ? -15.466 -30.201 -80.066 1.00 45.63  ? 51  GLY   B O   1 
ATOM   3442 N N   . PRO   B 1 52  ? -15.075 -28.047 -80.565 1.00 45.94  ? 52  PRO   B N   1 
ATOM   3443 C CA  . PRO   B 1 52  ? -13.618 -28.254 -80.565 1.00 42.04  ? 52  PRO   B CA  1 
ATOM   3444 C C   . PRO   B 1 52  ? -12.979 -28.224 -79.185 1.00 42.79  ? 52  PRO   B C   1 
ATOM   3445 O O   . PRO   B 1 52  ? -11.815 -28.628 -79.060 1.00 43.33  ? 52  PRO   B O   1 
ATOM   3446 C CB  . PRO   B 1 52  ? -13.100 -27.092 -81.420 1.00 42.61  ? 52  PRO   B CB  1 
ATOM   3447 C CG  . PRO   B 1 52  ? -14.144 -26.032 -81.277 1.00 43.80  ? 52  PRO   B CG  1 
ATOM   3448 C CD  . PRO   B 1 52  ? -15.453 -26.748 -81.151 1.00 43.51  ? 52  PRO   B CD  1 
ATOM   3449 N N   . ILE   B 1 53  ? -13.685 -27.761 -78.156 1.00 44.27  ? 53  ILE   B N   1 
ATOM   3450 C CA  . ILE   B 1 53  ? -13.107 -27.633 -76.819 1.00 41.83  ? 53  ILE   B CA  1 
ATOM   3451 C C   . ILE   B 1 53  ? -13.331 -28.892 -75.993 1.00 42.94  ? 53  ILE   B C   1 
ATOM   3452 O O   . ILE   B 1 53  ? -12.395 -29.414 -75.380 1.00 41.32  ? 53  ILE   B O   1 
ATOM   3453 C CB  . ILE   B 1 53  ? -13.685 -26.392 -76.100 1.00 46.09  ? 53  ILE   B CB  1 
ATOM   3454 C CG1 . ILE   B 1 53  ? -13.730 -25.179 -77.037 1.00 46.60  ? 53  ILE   B CG1 1 
ATOM   3455 C CG2 . ILE   B 1 53  ? -12.882 -26.079 -74.840 1.00 45.12  ? 53  ILE   B CG2 1 
ATOM   3456 C CD1 . ILE   B 1 53  ? -12.380 -24.791 -77.606 1.00 44.39  ? 53  ILE   B CD1 1 
ATOM   3457 N N   . ASN   B 1 54  ? -14.574 -29.378 -75.959 1.00 42.07  ? 54  ASN   B N   1 
ATOM   3458 C CA  . ASN   B 1 54  ? -14.982 -30.511 -75.127 1.00 42.93  ? 54  ASN   B CA  1 
ATOM   3459 C C   . ASN   B 1 54  ? -14.733 -30.227 -73.644 1.00 42.49  ? 54  ASN   B C   1 
ATOM   3460 O O   . ASN   B 1 54  ? -14.013 -30.954 -72.954 1.00 43.00  ? 54  ASN   B O   1 
ATOM   3461 C CB  . ASN   B 1 54  ? -14.280 -31.803 -75.558 1.00 43.07  ? 54  ASN   B CB  1 
ATOM   3462 C CG  . ASN   B 1 54  ? -15.000 -33.040 -75.076 1.00 41.47  ? 54  ASN   B CG  1 
ATOM   3463 O OD1 . ASN   B 1 54  ? -16.213 -33.020 -74.876 1.00 44.58  ? 54  ASN   B OD1 1 
ATOM   3464 N ND2 . ASN   B 1 54  ? -14.258 -34.123 -74.878 1.00 36.34  ? 54  ASN   B ND2 1 
ATOM   3465 N N   . ALA   B 1 55  ? -15.355 -29.149 -73.163 1.00 41.33  ? 55  ALA   B N   1 
ATOM   3466 C CA  . ALA   B 1 55  ? -15.252 -28.733 -71.768 1.00 40.72  ? 55  ALA   B CA  1 
ATOM   3467 C C   . ALA   B 1 55  ? -16.460 -29.134 -70.931 1.00 42.16  ? 55  ALA   B C   1 
ATOM   3468 O O   . ALA   B 1 55  ? -16.292 -29.670 -69.834 1.00 40.63  ? 55  ALA   B O   1 
ATOM   3469 C CB  . ALA   B 1 55  ? -15.054 -27.218 -71.680 1.00 39.31  ? 55  ALA   B CB  1 
ATOM   3470 N N   . VAL   B 1 56  ? -17.676 -28.903 -71.423 1.00 43.27  ? 56  VAL   B N   1 
ATOM   3471 C CA  . VAL   B 1 56  ? -18.892 -29.202 -70.661 1.00 44.29  ? 56  VAL   B CA  1 
ATOM   3472 C C   . VAL   B 1 56  ? -19.305 -30.623 -71.036 1.00 44.55  ? 56  VAL   B C   1 
ATOM   3473 O O   . VAL   B 1 56  ? -20.103 -30.848 -71.950 1.00 42.66  ? 56  VAL   B O   1 
ATOM   3474 C CB  . VAL   B 1 56  ? -19.996 -28.180 -70.920 1.00 45.65  ? 56  VAL   B CB  1 
ATOM   3475 C CG1 . VAL   B 1 56  ? -21.135 -28.344 -69.913 1.00 44.39  ? 56  VAL   B CG1 1 
ATOM   3476 C CG2 . VAL   B 1 56  ? -19.430 -26.768 -70.859 1.00 41.73  ? 56  VAL   B CG2 1 
ATOM   3477 N N   . VAL   B 1 57  ? -18.776 -31.598 -70.293 1.00 41.35  ? 57  VAL   B N   1 
ATOM   3478 C CA  . VAL   B 1 57  ? -18.924 -33.006 -70.649 1.00 41.61  ? 57  VAL   B CA  1 
ATOM   3479 C C   . VAL   B 1 57  ? -20.134 -33.678 -70.001 1.00 45.49  ? 57  VAL   B C   1 
ATOM   3480 O O   . VAL   B 1 57  ? -20.623 -34.686 -70.536 1.00 44.68  ? 57  VAL   B O   1 
ATOM   3481 C CB  . VAL   B 1 57  ? -17.639 -33.789 -70.306 1.00 41.52  ? 57  VAL   B CB  1 
ATOM   3482 C CG1 . VAL   B 1 57  ? -16.474 -33.299 -71.164 1.00 41.47  ? 57  VAL   B CG1 1 
ATOM   3483 C CG2 . VAL   B 1 57  ? -17.310 -33.666 -68.823 1.00 38.40  ? 57  VAL   B CG2 1 
ATOM   3484 N N   . VAL   B 1 58  ? -20.621 -33.166 -68.873 1.00 44.32  ? 58  VAL   B N   1 
ATOM   3485 C CA  . VAL   B 1 58  ? -21.857 -33.632 -68.249 1.00 42.83  ? 58  VAL   B CA  1 
ATOM   3486 C C   . VAL   B 1 58  ? -22.879 -32.514 -68.383 1.00 43.30  ? 58  VAL   B C   1 
ATOM   3487 O O   . VAL   B 1 58  ? -22.675 -31.416 -67.854 1.00 43.65  ? 58  VAL   B O   1 
ATOM   3488 C CB  . VAL   B 1 58  ? -21.645 -34.022 -66.775 1.00 41.77  ? 58  VAL   B CB  1 
ATOM   3489 C CG1 . VAL   B 1 58  ? -22.975 -34.363 -66.107 1.00 39.68  ? 58  VAL   B CG1 1 
ATOM   3490 C CG2 . VAL   B 1 58  ? -20.688 -35.199 -66.663 1.00 38.09  ? 58  VAL   B CG2 1 
ATOM   3491 N N   . ARG   B 1 59  ? -23.970 -32.778 -69.097 1.00 42.69  ? 59  ARG   B N   1 
ATOM   3492 C CA  . ARG   B 1 59  ? -24.960 -31.753 -69.397 1.00 43.81  ? 59  ARG   B CA  1 
ATOM   3493 C C   . ARG   B 1 59  ? -26.287 -32.104 -68.744 1.00 47.50  ? 59  ARG   B C   1 
ATOM   3494 O O   . ARG   B 1 59  ? -26.782 -33.227 -68.888 1.00 51.45  ? 59  ARG   B O   1 
ATOM   3495 C CB  . ARG   B 1 59  ? -25.126 -31.571 -70.908 1.00 43.50  ? 59  ARG   B CB  1 
ATOM   3496 C CG  . ARG   B 1 59  ? -23.910 -30.926 -71.558 1.00 42.47  ? 59  ARG   B CG  1 
ATOM   3497 C CD  . ARG   B 1 59  ? -23.860 -31.145 -73.053 1.00 41.61  ? 59  ARG   B CD  1 
ATOM   3498 N NE  . ARG   B 1 59  ? -22.604 -30.662 -73.614 1.00 45.32  ? 59  ARG   B NE  1 
ATOM   3499 C CZ  . ARG   B 1 59  ? -22.466 -30.172 -74.838 1.00 47.16  ? 59  ARG   B CZ  1 
ATOM   3500 N NH1 . ARG   B 1 59  ? -23.495 -30.084 -75.667 1.00 44.92  ? 59  ARG   B NH1 1 
ATOM   3501 N NH2 . ARG   B 1 59  ? -21.266 -29.762 -75.242 1.00 42.01  ? 59  ARG   B NH2 1 
ATOM   3502 N N   . ASP   B 1 60  ? -26.851 -31.135 -68.030 1.00 42.06  ? 60  ASP   B N   1 
ATOM   3503 C CA  . ASP   B 1 60  ? -28.072 -31.282 -67.251 1.00 43.76  ? 60  ASP   B CA  1 
ATOM   3504 C C   . ASP   B 1 60  ? -29.100 -30.241 -67.677 1.00 47.94  ? 60  ASP   B C   1 
ATOM   3505 O O   . ASP   B 1 60  ? -29.793 -29.643 -66.848 1.00 47.14  ? 60  ASP   B O   1 
ATOM   3506 C CB  . ASP   B 1 60  ? -27.761 -31.164 -65.762 1.00 43.03  ? 60  ASP   B CB  1 
ATOM   3507 C CG  . ASP   B 1 60  ? -28.773 -31.875 -64.897 1.00 45.75  ? 60  ASP   B CG  1 
ATOM   3508 O OD1 . ASP   B 1 60  ? -29.507 -32.735 -65.427 1.00 46.00  ? 60  ASP   B OD1 1 
ATOM   3509 O OD2 . ASP   B 1 60  ? -28.824 -31.580 -63.684 1.00 47.94  ? 60  ASP   B OD2 1 
ATOM   3510 N N   . PHE   B 1 61  ? -29.220 -30.035 -68.993 1.00 43.90  ? 61  PHE   B N   1 
ATOM   3511 C CA  . PHE   B 1 61  ? -29.853 -28.824 -69.508 1.00 45.59  ? 61  PHE   B CA  1 
ATOM   3512 C C   . PHE   B 1 61  ? -31.338 -28.765 -69.170 1.00 48.93  ? 61  PHE   B C   1 
ATOM   3513 O O   . PHE   B 1 61  ? -31.872 -27.685 -68.893 1.00 46.96  ? 61  PHE   B O   1 
ATOM   3514 C CB  . PHE   B 1 61  ? -29.646 -28.725 -71.020 1.00 43.61  ? 61  PHE   B CB  1 
ATOM   3515 C CG  . PHE   B 1 61  ? -28.227 -28.422 -71.424 1.00 44.14  ? 61  PHE   B CG  1 
ATOM   3516 C CD1 . PHE   B 1 61  ? -27.301 -27.977 -70.491 1.00 44.74  ? 61  PHE   B CD1 1 
ATOM   3517 C CD2 . PHE   B 1 61  ? -27.824 -28.570 -72.741 1.00 42.78  ? 61  PHE   B CD2 1 
ATOM   3518 C CE1 . PHE   B 1 61  ? -25.997 -27.695 -70.867 1.00 44.67  ? 61  PHE   B CE1 1 
ATOM   3519 C CE2 . PHE   B 1 61  ? -26.523 -28.288 -73.123 1.00 43.22  ? 61  PHE   B CE2 1 
ATOM   3520 C CZ  . PHE   B 1 61  ? -25.610 -27.851 -72.187 1.00 43.67  ? 61  PHE   B CZ  1 
ATOM   3521 N N   . ASP   B 1 62  ? -32.024 -29.910 -69.190 1.00 48.00  ? 62  ASP   B N   1 
ATOM   3522 C CA  . ASP   B 1 62  ? -33.469 -29.897 -68.976 1.00 49.78  ? 62  ASP   B CA  1 
ATOM   3523 C C   . ASP   B 1 62  ? -33.815 -29.599 -67.523 1.00 51.47  ? 62  ASP   B C   1 
ATOM   3524 O O   . ASP   B 1 62  ? -34.741 -28.828 -67.246 1.00 51.38  ? 62  ASP   B O   1 
ATOM   3525 C CB  . ASP   B 1 62  ? -34.075 -31.226 -69.416 1.00 53.14  ? 62  ASP   B CB  1 
ATOM   3526 C CG  . ASP   B 1 62  ? -34.429 -31.236 -70.887 1.00 63.30  ? 62  ASP   B CG  1 
ATOM   3527 O OD1 . ASP   B 1 62  ? -34.592 -32.337 -71.454 1.00 64.28  ? 62  ASP   B OD1 1 
ATOM   3528 O OD2 . ASP   B 1 62  ? -34.539 -30.138 -71.476 1.00 71.55  ? 62  ASP   B OD2 1 
ATOM   3529 N N   . ARG   B 1 63  ? -33.091 -30.205 -66.582 1.00 48.09  ? 63  ARG   B N   1 
ATOM   3530 C CA  . ARG   B 1 63  ? -33.291 -29.865 -65.180 1.00 48.47  ? 63  ARG   B CA  1 
ATOM   3531 C C   . ARG   B 1 63  ? -32.845 -28.438 -64.890 1.00 48.97  ? 63  ARG   B C   1 
ATOM   3532 O O   . ARG   B 1 63  ? -33.414 -27.775 -64.016 1.00 50.01  ? 63  ARG   B O   1 
ATOM   3533 C CB  . ARG   B 1 63  ? -32.544 -30.857 -64.291 1.00 49.64  ? 63  ARG   B CB  1 
ATOM   3534 C CG  . ARG   B 1 63  ? -33.226 -32.216 -64.162 1.00 45.72  ? 63  ARG   B CG  1 
ATOM   3535 C CD  . ARG   B 1 63  ? -32.908 -32.854 -62.821 1.00 45.27  ? 63  ARG   B CD  1 
ATOM   3536 N NE  . ARG   B 1 63  ? -31.469 -32.913 -62.589 1.00 50.48  ? 63  ARG   B NE  1 
ATOM   3537 C CZ  . ARG   B 1 63  ? -30.891 -33.556 -61.583 1.00 44.79  ? 63  ARG   B CZ  1 
ATOM   3538 N NH1 . ARG   B 1 63  ? -31.602 -34.208 -60.677 1.00 45.85  ? 63  ARG   B NH1 1 
ATOM   3539 N NH2 . ARG   B 1 63  ? -29.565 -33.537 -61.480 1.00 41.96  ? 63  ARG   B NH2 1 
ATOM   3540 N N   . ALA   B 1 64  ? -31.843 -27.947 -65.621 1.00 45.41  ? 64  ALA   B N   1 
ATOM   3541 C CA  . ALA   B 1 64  ? -31.407 -26.568 -65.438 1.00 47.21  ? 64  ALA   B CA  1 
ATOM   3542 C C   . ALA   B 1 64  ? -32.482 -25.587 -65.887 1.00 46.58  ? 64  ALA   B C   1 
ATOM   3543 O O   . ALA   B 1 64  ? -32.681 -24.542 -65.255 1.00 46.66  ? 64  ALA   B O   1 
ATOM   3544 C CB  . ALA   B 1 64  ? -30.103 -26.325 -66.196 1.00 41.74  ? 64  ALA   B CB  1 
ATOM   3545 N N   . ARG   B 1 65  ? -33.194 -25.911 -66.970 1.00 46.90  ? 65  ARG   B N   1 
ATOM   3546 C CA  . ARG   B 1 65  ? -34.235 -25.015 -67.467 1.00 49.05  ? 65  ARG   B CA  1 
ATOM   3547 C C   . ARG   B 1 65  ? -35.414 -24.950 -66.504 1.00 48.45  ? 65  ARG   B C   1 
ATOM   3548 O O   . ARG   B 1 65  ? -36.015 -23.885 -66.325 1.00 51.37  ? 65  ARG   B O   1 
ATOM   3549 C CB  . ARG   B 1 65  ? -34.695 -25.458 -68.855 1.00 47.58  ? 65  ARG   B CB  1 
ATOM   3550 C CG  . ARG   B 1 65  ? -33.717 -25.098 -69.961 1.00 48.10  ? 65  ARG   B CG  1 
ATOM   3551 C CD  . ARG   B 1 65  ? -34.212 -25.560 -71.324 1.00 50.61  ? 65  ARG   B CD  1 
ATOM   3552 N NE  . ARG   B 1 65  ? -34.855 -24.486 -72.072 1.00 52.47  ? 65  ARG   B NE  1 
ATOM   3553 C CZ  . ARG   B 1 65  ? -36.166 -24.288 -72.129 1.00 52.01  ? 65  ARG   B CZ  1 
ATOM   3554 N NH1 . ARG   B 1 65  ? -37.013 -25.082 -71.495 1.00 54.47  ? 65  ARG   B NH1 1 
ATOM   3555 N NH2 . ARG   B 1 65  ? -36.638 -23.270 -72.843 1.00 47.95  ? 65  ARG   B NH2 1 
ATOM   3556 N N   . ASP   B 1 66  ? -35.767 -26.077 -65.879 1.00 46.60  ? 66  ASP   B N   1 
ATOM   3557 C CA  . ASP   B 1 66  ? -36.787 -26.040 -64.835 1.00 51.37  ? 66  ASP   B CA  1 
ATOM   3558 C C   . ASP   B 1 66  ? -36.306 -25.240 -63.631 1.00 48.77  ? 66  ASP   B C   1 
ATOM   3559 O O   . ASP   B 1 66  ? -37.076 -24.480 -63.033 1.00 51.42  ? 66  ASP   B O   1 
ATOM   3560 C CB  . ASP   B 1 66  ? -37.178 -27.458 -64.416 1.00 51.51  ? 66  ASP   B CB  1 
ATOM   3561 C CG  . ASP   B 1 66  ? -37.730 -28.276 -65.567 1.00 55.31  ? 66  ASP   B CG  1 
ATOM   3562 O OD1 . ASP   B 1 66  ? -38.370 -27.687 -66.465 1.00 59.89  ? 66  ASP   B OD1 1 
ATOM   3563 O OD2 . ASP   B 1 66  ? -37.529 -29.509 -65.571 1.00 55.51  ? 66  ASP   B OD2 1 
ATOM   3564 N N   . ALA   B 1 67  ? -35.034 -25.400 -63.258 1.00 50.20  ? 67  ALA   B N   1 
ATOM   3565 C CA  . ALA   B 1 67  ? -34.468 -24.579 -62.194 1.00 51.35  ? 67  ALA   B CA  1 
ATOM   3566 C C   . ALA   B 1 67  ? -34.430 -23.107 -62.584 1.00 49.12  ? 67  ALA   B C   1 
ATOM   3567 O O   . ALA   B 1 67  ? -34.601 -22.236 -61.723 1.00 50.75  ? 67  ALA   B O   1 
ATOM   3568 C CB  . ALA   B 1 67  ? -33.066 -25.071 -61.837 1.00 49.62  ? 67  ALA   B CB  1 
ATOM   3569 N N   . ALA   B 1 68  ? -34.206 -22.809 -63.866 1.00 46.77  ? 68  ALA   B N   1 
ATOM   3570 C CA  . ALA   B 1 68  ? -34.249 -21.422 -64.316 1.00 46.76  ? 68  ALA   B CA  1 
ATOM   3571 C C   . ALA   B 1 68  ? -35.658 -20.855 -64.208 1.00 50.37  ? 68  ALA   B C   1 
ATOM   3572 O O   . ALA   B 1 68  ? -35.837 -19.689 -63.838 1.00 50.45  ? 68  ALA   B O   1 
ATOM   3573 C CB  . ALA   B 1 68  ? -33.735 -21.317 -65.751 1.00 48.56  ? 68  ALA   B CB  1 
ATOM   3574 N N   . LYS   B 1 69  ? -36.669 -21.669 -64.521 1.00 50.43  ? 69  LYS   B N   1 
ATOM   3575 C CA  . LYS   B 1 69  ? -38.052 -21.221 -64.386 1.00 51.30  ? 69  LYS   B CA  1 
ATOM   3576 C C   . LYS   B 1 69  ? -38.404 -20.960 -62.927 1.00 53.13  ? 69  LYS   B C   1 
ATOM   3577 O O   . LYS   B 1 69  ? -39.121 -20.001 -62.614 1.00 52.37  ? 69  LYS   B O   1 
ATOM   3578 C CB  . LYS   B 1 69  ? -38.998 -22.258 -64.994 1.00 49.12  ? 69  LYS   B CB  1 
ATOM   3579 C CG  . LYS   B 1 69  ? -39.077 -22.212 -66.513 1.00 51.47  ? 69  LYS   B CG  1 
ATOM   3580 C CD  . LYS   B 1 69  ? -39.527 -23.546 -67.086 1.00 52.35  ? 69  LYS   B CD  1 
ATOM   3581 C CE  . LYS   B 1 69  ? -38.812 -23.853 -68.394 1.00 53.52  ? 69  LYS   B CE  1 
ATOM   3582 N NZ  . LYS   B 1 69  ? -39.734 -24.418 -69.421 1.00 53.80  ? 69  LYS   B NZ  1 
ATOM   3583 N N   . ALA   B 1 70  ? -37.907 -21.804 -62.019 1.00 53.33  ? 70  ALA   B N   1 
ATOM   3584 C CA  . ALA   B 1 70  ? -38.139 -21.579 -60.596 1.00 53.25  ? 70  ALA   B CA  1 
ATOM   3585 C C   . ALA   B 1 70  ? -37.507 -20.271 -60.136 1.00 56.23  ? 70  ALA   B C   1 
ATOM   3586 O O   . ALA   B 1 70  ? -38.121 -19.509 -59.381 1.00 57.10  ? 70  ALA   B O   1 
ATOM   3587 C CB  . ALA   B 1 70  ? -37.596 -22.755 -59.784 1.00 47.33  ? 70  ALA   B CB  1 
ATOM   3588 N N   . ALA   B 1 71  ? -36.281 -19.993 -60.588 1.00 55.35  ? 71  ALA   B N   1 
ATOM   3589 C CA  . ALA   B 1 71  ? -35.631 -18.734 -60.243 1.00 54.95  ? 71  ALA   B CA  1 
ATOM   3590 C C   . ALA   B 1 71  ? -36.456 -17.536 -60.692 1.00 54.95  ? 71  ALA   B C   1 
ATOM   3591 O O   . ALA   B 1 71  ? -36.478 -16.509 -60.006 1.00 54.24  ? 71  ALA   B O   1 
ATOM   3592 C CB  . ALA   B 1 71  ? -34.233 -18.677 -60.857 1.00 50.74  ? 71  ALA   B CB  1 
ATOM   3593 N N   . ASP   B 1 72  ? -37.148 -17.652 -61.830 1.00 53.21  ? 72  ASP   B N   1 
ATOM   3594 C CA  . ASP   B 1 72  ? -37.987 -16.554 -62.299 1.00 53.17  ? 72  ASP   B CA  1 
ATOM   3595 C C   . ASP   B 1 72  ? -39.229 -16.385 -61.435 1.00 56.44  ? 72  ASP   B C   1 
ATOM   3596 O O   . ASP   B 1 72  ? -39.728 -15.264 -61.287 1.00 59.21  ? 72  ASP   B O   1 
ATOM   3597 C CB  . ASP   B 1 72  ? -38.375 -16.773 -63.763 1.00 48.89  ? 72  ASP   B CB  1 
ATOM   3598 C CG  . ASP   B 1 72  ? -37.286 -16.329 -64.730 1.00 54.44  ? 72  ASP   B CG  1 
ATOM   3599 O OD1 . ASP   B 1 72  ? -36.766 -15.202 -64.576 1.00 51.98  ? 72  ASP   B OD1 1 
ATOM   3600 O OD2 . ASP   B 1 72  ? -36.948 -17.110 -65.647 1.00 56.18  ? 72  ASP   B OD2 1 
ATOM   3601 N N   . ALA   B 1 73  ? -39.742 -17.476 -60.860 1.00 56.44  ? 73  ALA   B N   1 
ATOM   3602 C CA  . ALA   B 1 73  ? -40.827 -17.364 -59.891 1.00 57.15  ? 73  ALA   B CA  1 
ATOM   3603 C C   . ALA   B 1 73  ? -40.390 -16.635 -58.628 1.00 60.36  ? 73  ALA   B C   1 
ATOM   3604 O O   . ALA   B 1 73  ? -41.239 -16.100 -57.906 1.00 62.19  ? 73  ALA   B O   1 
ATOM   3605 C CB  . ALA   B 1 73  ? -41.364 -18.750 -59.538 1.00 53.83  ? 73  ALA   B CB  1 
ATOM   3606 N N   . GLU   B 1 74  ? -39.087 -16.594 -58.357 1.00 60.16  ? 74  GLU   B N   1 
ATOM   3607 C CA  . GLU   B 1 74  ? -38.536 -15.893 -57.205 1.00 61.93  ? 74  GLU   B CA  1 
ATOM   3608 C C   . GLU   B 1 74  ? -38.220 -14.433 -57.511 1.00 62.62  ? 74  GLU   B C   1 
ATOM   3609 O O   . GLU   B 1 74  ? -38.391 -13.574 -56.641 1.00 60.80  ? 74  GLU   B O   1 
ATOM   3610 C CB  . GLU   B 1 74  ? -37.281 -16.614 -56.718 1.00 59.56  ? 74  GLU   B CB  1 
ATOM   3611 C CG  . GLU   B 1 74  ? -37.527 -18.063 -56.347 1.00 58.17  ? 74  GLU   B CG  1 
ATOM   3612 C CD  . GLU   B 1 74  ? -36.309 -18.730 -55.752 1.00 58.15  ? 74  GLU   B CD  1 
ATOM   3613 O OE1 . GLU   B 1 74  ? -36.115 -18.625 -54.522 1.00 56.31  ? 74  GLU   B OE1 1 
ATOM   3614 O OE2 . GLU   B 1 74  ? -35.548 -19.361 -56.514 1.00 60.05  ? 74  GLU   B OE2 1 
ATOM   3615 N N   . ILE   B 1 75  ? -37.749 -14.134 -58.728 1.00 58.91  ? 75  ILE   B N   1 
ATOM   3616 C CA  . ILE   B 1 75  ? -37.635 -12.738 -59.153 1.00 63.93  ? 75  ILE   B CA  1 
ATOM   3617 C C   . ILE   B 1 75  ? -38.998 -12.061 -59.098 1.00 64.76  ? 75  ILE   B C   1 
ATOM   3618 O O   . ILE   B 1 75  ? -39.114 -10.885 -58.726 1.00 62.74  ? 75  ILE   B O   1 
ATOM   3619 C CB  . ILE   B 1 75  ? -37.017 -12.635 -60.563 1.00 63.49  ? 75  ILE   B CB  1 
ATOM   3620 C CG1 . ILE   B 1 75  ? -35.802 -13.556 -60.722 1.00 61.79  ? 75  ILE   B CG1 1 
ATOM   3621 C CG2 . ILE   B 1 75  ? -36.624 -11.193 -60.869 1.00 55.84  ? 75  ILE   B CG2 1 
ATOM   3622 C CD1 . ILE   B 1 75  ? -34.488 -12.918 -60.319 1.00 53.41  ? 75  ILE   B CD1 1 
ATOM   3623 N N   . ALA   B 1 76  ? -40.051 -12.790 -59.476 1.00 65.79  ? 76  ALA   B N   1 
ATOM   3624 C CA  . ALA   B 1 76  ? -41.413 -12.282 -59.354 1.00 67.66  ? 76  ALA   B CA  1 
ATOM   3625 C C   . ALA   B 1 76  ? -41.874 -12.203 -57.903 1.00 69.95  ? 76  ALA   B C   1 
ATOM   3626 O O   . ALA   B 1 76  ? -42.835 -11.483 -57.612 1.00 73.26  ? 76  ALA   B O   1 
ATOM   3627 C CB  . ALA   B 1 76  ? -42.372 -13.156 -60.166 1.00 66.52  ? 76  ALA   B CB  1 
ATOM   3628 N N   . ALA   B 1 77  ? -41.216 -12.924 -56.995 1.00 67.98  ? 77  ALA   B N   1 
ATOM   3629 C CA  . ALA   B 1 77  ? -41.462 -12.816 -55.563 1.00 68.25  ? 77  ALA   B CA  1 
ATOM   3630 C C   . ALA   B 1 77  ? -40.532 -11.820 -54.884 1.00 66.33  ? 77  ALA   B C   1 
ATOM   3631 O O   . ALA   B 1 77  ? -40.614 -11.655 -53.663 1.00 60.51  ? 77  ALA   B O   1 
ATOM   3632 C CB  . ALA   B 1 77  ? -41.321 -14.186 -54.892 1.00 65.56  ? 77  ALA   B CB  1 
ATOM   3633 N N   . ALA   B 1 78  ? -39.650 -11.167 -55.646 1.00 67.32  ? 78  ALA   B N   1 
ATOM   3634 C CA  . ALA   B 1 78  ? -38.735 -10.147 -55.132 1.00 65.46  ? 78  ALA   B CA  1 
ATOM   3635 C C   . ALA   B 1 78  ? -37.784 -10.703 -54.076 1.00 65.36  ? 78  ALA   B C   1 
ATOM   3636 O O   . ALA   B 1 78  ? -37.340 -9.974  -53.184 1.00 65.17  ? 78  ALA   B O   1 
ATOM   3637 C CB  . ALA   B 1 78  ? -39.493 -8.936  -54.578 1.00 61.51  ? 78  ALA   B CB  1 
ATOM   3638 N N   . VAL   B 1 79  ? -37.459 -11.994 -54.160 1.00 66.01  ? 79  VAL   B N   1 
ATOM   3639 C CA  . VAL   B 1 79  ? -36.459 -12.565 -53.266 1.00 67.79  ? 79  VAL   B CA  1 
ATOM   3640 C C   . VAL   B 1 79  ? -35.077 -12.132 -53.740 1.00 65.63  ? 79  VAL   B C   1 
ATOM   3641 O O   . VAL   B 1 79  ? -34.828 -11.961 -54.941 1.00 62.61  ? 79  VAL   B O   1 
ATOM   3642 C CB  . VAL   B 1 79  ? -36.589 -14.102 -53.181 1.00 65.03  ? 79  VAL   B CB  1 
ATOM   3643 C CG1 . VAL   B 1 79  ? -38.048 -14.537 -53.329 1.00 60.73  ? 79  VAL   B CG1 1 
ATOM   3644 C CG2 . VAL   B 1 79  ? -35.686 -14.801 -54.194 1.00 61.85  ? 79  VAL   B CG2 1 
ATOM   3645 N N   . ARG   B 1 80  ? -34.178 -11.916 -52.782 1.00 68.40  ? 80  ARG   B N   1 
ATOM   3646 C CA  . ARG   B 1 80  ? -32.856 -11.353 -53.039 1.00 66.56  ? 80  ARG   B CA  1 
ATOM   3647 C C   . ARG   B 1 80  ? -31.803 -12.431 -52.811 1.00 61.82  ? 80  ARG   B C   1 
ATOM   3648 O O   . ARG   B 1 80  ? -31.558 -12.844 -51.672 1.00 62.12  ? 80  ARG   B O   1 
ATOM   3649 C CB  . ARG   B 1 80  ? -32.610 -10.132 -52.154 1.00 62.60  ? 80  ARG   B CB  1 
ATOM   3650 C CG  . ARG   B 1 80  ? -33.381 -10.164 -50.847 1.00 68.44  ? 80  ARG   B CG  1 
ATOM   3651 C CD  . ARG   B 1 80  ? -33.554 -8.769  -50.254 1.00 73.81  ? 80  ARG   B CD  1 
ATOM   3652 N NE  . ARG   B 1 80  ? -34.537 -7.976  -50.986 1.00 70.16  ? 80  ARG   B NE  1 
ATOM   3653 C CZ  . ARG   B 1 80  ? -34.359 -6.715  -51.357 1.00 68.11  ? 80  ARG   B CZ  1 
ATOM   3654 N NH1 . ARG   B 1 80  ? -33.255 -6.053  -51.049 1.00 68.98  ? 80  ARG   B NH1 1 
ATOM   3655 N NH2 . ARG   B 1 80  ? -35.317 -6.099  -52.045 1.00 68.95  ? 80  ARG   B NH2 1 
ATOM   3656 N N   . LYS   B 1 81  ? -31.186 -12.883 -53.904 1.00 55.89  ? 81  LYS   B N   1 
ATOM   3657 C CA  . LYS   B 1 81  ? -30.133 -13.875 -53.873 1.00 49.78  ? 81  LYS   B CA  1 
ATOM   3658 C C   . LYS   B 1 81  ? -29.052 -13.349 -54.813 1.00 47.43  ? 81  LYS   B C   1 
ATOM   3659 O O   . LYS   B 1 81  ? -29.365 -12.947 -55.950 1.00 47.94  ? 81  LYS   B O   1 
ATOM   3660 C CB  . LYS   B 1 81  ? -30.627 -15.252 -54.321 1.00 49.16  ? 81  LYS   B CB  1 
ATOM   3661 C CG  . LYS   B 1 81  ? -31.140 -16.147 -53.200 1.00 48.01  ? 81  LYS   B CG  1 
ATOM   3662 C CD  . LYS   B 1 81  ? -32.351 -16.949 -53.664 1.00 50.24  ? 81  LYS   B CD  1 
ATOM   3663 C CE  . LYS   B 1 81  ? -33.019 -17.677 -52.513 1.00 50.03  ? 81  LYS   B CE  1 
ATOM   3664 N NZ  . LYS   B 1 81  ? -33.410 -19.062 -52.901 1.00 53.78  ? 81  LYS   B NZ  1 
ATOM   3665 N N   . PRO   B 1 82  ? -27.785 -13.336 -54.391 1.00 44.63  ? 82  PRO   B N   1 
ATOM   3666 C CA  . PRO   B 1 82  ? -26.749 -12.658 -55.189 1.00 41.30  ? 82  PRO   B CA  1 
ATOM   3667 C C   . PRO   B 1 82  ? -26.421 -13.339 -56.508 1.00 43.18  ? 82  PRO   B C   1 
ATOM   3668 O O   . PRO   B 1 82  ? -25.742 -12.723 -57.338 1.00 40.39  ? 82  PRO   B O   1 
ATOM   3669 C CB  . PRO   B 1 82  ? -25.534 -12.662 -54.255 1.00 40.36  ? 82  PRO   B CB  1 
ATOM   3670 C CG  . PRO   B 1 82  ? -25.761 -13.830 -53.356 1.00 40.17  ? 82  PRO   B CG  1 
ATOM   3671 C CD  . PRO   B 1 82  ? -27.243 -13.902 -53.144 1.00 45.23  ? 82  PRO   B CD  1 
ATOM   3672 N N   . LEU   B 1 83  ? -26.867 -14.580 -56.731 1.00 43.66  ? 83  LEU   B N   1 
ATOM   3673 C CA  . LEU   B 1 83  ? -26.553 -15.310 -57.956 1.00 43.21  ? 83  LEU   B CA  1 
ATOM   3674 C C   . LEU   B 1 83  ? -27.809 -15.829 -58.648 1.00 46.96  ? 83  LEU   B C   1 
ATOM   3675 O O   . LEU   B 1 83  ? -27.719 -16.748 -59.471 1.00 44.41  ? 83  LEU   B O   1 
ATOM   3676 C CB  . LEU   B 1 83  ? -25.604 -16.477 -57.667 1.00 40.12  ? 83  LEU   B CB  1 
ATOM   3677 C CG  . LEU   B 1 83  ? -24.104 -16.205 -57.516 1.00 43.13  ? 83  LEU   B CG  1 
ATOM   3678 C CD1 . LEU   B 1 83  ? -23.328 -17.517 -57.533 1.00 40.82  ? 83  LEU   B CD1 1 
ATOM   3679 C CD2 . LEU   B 1 83  ? -23.596 -15.269 -58.600 1.00 40.02  ? 83  LEU   B CD2 1 
ATOM   3680 N N   . LEU   B 1 84  ? -28.972 -15.255 -58.339 1.00 42.79  ? 84  LEU   B N   1 
ATOM   3681 C CA  . LEU   B 1 84  ? -30.243 -15.812 -58.787 1.00 47.31  ? 84  LEU   B CA  1 
ATOM   3682 C C   . LEU   B 1 84  ? -30.312 -15.861 -60.309 1.00 47.77  ? 84  LEU   B C   1 
ATOM   3683 O O   . LEU   B 1 84  ? -30.119 -14.845 -60.985 1.00 45.23  ? 84  LEU   B O   1 
ATOM   3684 C CB  . LEU   B 1 84  ? -31.397 -14.988 -58.212 1.00 46.06  ? 84  LEU   B CB  1 
ATOM   3685 C CG  . LEU   B 1 84  ? -32.798 -15.596 -58.289 1.00 49.61  ? 84  LEU   B CG  1 
ATOM   3686 C CD1 . LEU   B 1 84  ? -32.765 -17.048 -57.863 1.00 48.91  ? 84  LEU   B CD1 1 
ATOM   3687 C CD2 . LEU   B 1 84  ? -33.753 -14.812 -57.404 1.00 52.32  ? 84  LEU   B CD2 1 
ATOM   3688 N N   . GLY   B 1 85  ? -30.566 -17.055 -60.842 1.00 43.44  ? 85  GLY   B N   1 
ATOM   3689 C CA  . GLY   B 1 85  ? -30.669 -17.256 -62.273 1.00 44.65  ? 85  GLY   B CA  1 
ATOM   3690 C C   . GLY   B 1 85  ? -29.367 -17.230 -63.043 1.00 40.92  ? 85  GLY   B C   1 
ATOM   3691 O O   . GLY   B 1 85  ? -29.404 -17.244 -64.278 1.00 45.27  ? 85  GLY   B O   1 
ATOM   3692 N N   . VAL   B 1 86  ? -28.222 -17.197 -62.369 1.00 41.15  ? 86  VAL   B N   1 
ATOM   3693 C CA  . VAL   B 1 86  ? -26.927 -17.168 -63.045 1.00 40.41  ? 86  VAL   B CA  1 
ATOM   3694 C C   . VAL   B 1 86  ? -26.522 -18.587 -63.426 1.00 40.32  ? 86  VAL   B C   1 
ATOM   3695 O O   . VAL   B 1 86  ? -26.256 -19.411 -62.539 1.00 39.76  ? 86  VAL   B O   1 
ATOM   3696 C CB  . VAL   B 1 86  ? -25.850 -16.518 -62.164 1.00 41.93  ? 86  VAL   B CB  1 
ATOM   3697 C CG1 . VAL   B 1 86  ? -24.468 -16.709 -62.784 1.00 35.31  ? 86  VAL   B CG1 1 
ATOM   3698 C CG2 . VAL   B 1 86  ? -26.159 -15.051 -61.947 1.00 40.29  ? 86  VAL   B CG2 1 
ATOM   3699 N N   . PRO   B 1 87  ? -26.463 -18.919 -64.716 1.00 41.71  ? 87  PRO   B N   1 
ATOM   3700 C CA  . PRO   B 1 87  ? -26.037 -20.266 -65.110 1.00 41.50  ? 87  PRO   B CA  1 
ATOM   3701 C C   . PRO   B 1 87  ? -24.543 -20.450 -64.905 1.00 40.24  ? 87  PRO   B C   1 
ATOM   3702 O O   . PRO   B 1 87  ? -23.751 -19.527 -65.107 1.00 43.27  ? 87  PRO   B O   1 
ATOM   3703 C CB  . PRO   B 1 87  ? -26.407 -20.336 -66.596 1.00 44.00  ? 87  PRO   B CB  1 
ATOM   3704 C CG  . PRO   B 1 87  ? -26.353 -18.913 -67.046 1.00 46.28  ? 87  PRO   B CG  1 
ATOM   3705 C CD  . PRO   B 1 87  ? -26.842 -18.099 -65.880 1.00 44.14  ? 87  PRO   B CD  1 
ATOM   3706 N N   . MET   B 1 88  ? -24.162 -21.658 -64.503 1.00 39.34  ? 88  MET   B N   1 
ATOM   3707 C CA  . MET   B 1 88  ? -22.760 -21.988 -64.294 1.00 40.69  ? 88  MET   B CA  1 
ATOM   3708 C C   . MET   B 1 88  ? -22.587 -23.492 -64.413 1.00 41.31  ? 88  MET   B C   1 
ATOM   3709 O O   . MET   B 1 88  ? -23.556 -24.253 -64.443 1.00 43.92  ? 88  MET   B O   1 
ATOM   3710 C CB  . MET   B 1 88  ? -22.260 -21.498 -62.931 1.00 40.23  ? 88  MET   B CB  1 
ATOM   3711 C CG  . MET   B 1 88  ? -23.044 -22.051 -61.750 1.00 40.90  ? 88  MET   B CG  1 
ATOM   3712 S SD  . MET   B 1 88  ? -22.367 -21.552 -60.147 1.00 46.91  ? 88  MET   B SD  1 
ATOM   3713 C CE  . MET   B 1 88  ? -20.634 -21.933 -60.369 1.00 38.86  ? 88  MET   B CE  1 
ATOM   3714 N N   . THR   B 1 89  ? -21.331 -23.909 -64.478 1.00 43.06  ? 89  THR   B N   1 
ATOM   3715 C CA  . THR   B 1 89  ? -20.961 -25.308 -64.360 1.00 44.29  ? 89  THR   B CA  1 
ATOM   3716 C C   . THR   B 1 89  ? -20.071 -25.481 -63.137 1.00 42.26  ? 89  THR   B C   1 
ATOM   3717 O O   . THR   B 1 89  ? -19.651 -24.512 -62.501 1.00 43.90  ? 89  THR   B O   1 
ATOM   3718 C CB  . THR   B 1 89  ? -20.247 -25.813 -65.623 1.00 41.91  ? 89  THR   B CB  1 
ATOM   3719 O OG1 . THR   B 1 89  ? -19.219 -24.892 -66.000 1.00 44.41  ? 89  THR   B OG1 1 
ATOM   3720 C CG2 . THR   B 1 89  ? -21.233 -25.962 -66.771 1.00 44.04  ? 89  THR   B CG2 1 
ATOM   3721 N N   . ILE   B 1 90  ? -19.800 -26.738 -62.804 1.00 41.45  ? 90  ILE   B N   1 
ATOM   3722 C CA  . ILE   B 1 90  ? -18.945 -27.098 -61.681 1.00 42.21  ? 90  ILE   B CA  1 
ATOM   3723 C C   . ILE   B 1 90  ? -18.015 -28.203 -62.162 1.00 41.29  ? 90  ILE   B C   1 
ATOM   3724 O O   . ILE   B 1 90  ? -18.339 -28.949 -63.089 1.00 36.72  ? 90  ILE   B O   1 
ATOM   3725 C CB  . ILE   B 1 90  ? -19.774 -27.556 -60.450 1.00 38.50  ? 90  ILE   B CB  1 
ATOM   3726 C CG1 . ILE   B 1 90  ? -18.906 -27.783 -59.209 1.00 41.71  ? 90  ILE   B CG1 1 
ATOM   3727 C CG2 . ILE   B 1 90  ? -20.547 -28.808 -60.753 1.00 38.04  ? 90  ILE   B CG2 1 
ATOM   3728 C CD1 . ILE   B 1 90  ? -18.877 -26.631 -58.255 1.00 36.33  ? 90  ILE   B CD1 1 
ATOM   3729 N N   . LYS   B 1 91  ? -16.844 -28.297 -61.540 1.00 41.50  ? 91  LYS   B N   1 
ATOM   3730 C CA  . LYS   B 1 91  ? -15.944 -29.402 -61.834 1.00 39.46  ? 91  LYS   B CA  1 
ATOM   3731 C C   . LYS   B 1 91  ? -16.644 -30.734 -61.582 1.00 39.59  ? 91  LYS   B C   1 
ATOM   3732 O O   . LYS   B 1 91  ? -17.416 -30.878 -60.630 1.00 39.08  ? 91  LYS   B O   1 
ATOM   3733 C CB  . LYS   B 1 91  ? -14.686 -29.297 -60.978 1.00 38.54  ? 91  LYS   B CB  1 
ATOM   3734 C CG  . LYS   B 1 91  ? -13.537 -30.156 -61.449 1.00 37.96  ? 91  LYS   B CG  1 
ATOM   3735 C CD  . LYS   B 1 91  ? -12.261 -29.742 -60.751 1.00 37.77  ? 91  LYS   B CD  1 
ATOM   3736 C CE  . LYS   B 1 91  ? -11.458 -30.941 -60.315 1.00 42.15  ? 91  LYS   B CE  1 
ATOM   3737 N NZ  . LYS   B 1 91  ? -10.230 -30.517 -59.605 1.00 41.27  ? 91  LYS   B NZ  1 
ATOM   3738 N N   . GLU   B 1 92  ? -16.363 -31.715 -62.445 1.00 37.71  ? 92  GLU   B N   1 
ATOM   3739 C CA  . GLU   B 1 92  ? -17.041 -33.007 -62.369 1.00 40.47  ? 92  GLU   B CA  1 
ATOM   3740 C C   . GLU   B 1 92  ? -16.797 -33.731 -61.051 1.00 42.79  ? 92  GLU   B C   1 
ATOM   3741 O O   . GLU   B 1 92  ? -17.601 -34.593 -60.674 1.00 40.95  ? 92  GLU   B O   1 
ATOM   3742 C CB  . GLU   B 1 92  ? -16.599 -33.906 -63.524 1.00 38.20  ? 92  GLU   B CB  1 
ATOM   3743 C CG  . GLU   B 1 92  ? -17.568 -35.039 -63.816 1.00 37.31  ? 92  GLU   B CG  1 
ATOM   3744 C CD  . GLU   B 1 92  ? -17.060 -36.385 -63.339 1.00 41.37  ? 92  GLU   B CD  1 
ATOM   3745 O OE1 . GLU   B 1 92  ? -16.027 -36.423 -62.633 1.00 39.30  ? 92  GLU   B OE1 1 
ATOM   3746 O OE2 . GLU   B 1 92  ? -17.708 -37.406 -63.660 1.00 44.49  ? 92  GLU   B OE2 1 
ATOM   3747 N N   . SER   B 1 93  ? -15.714 -33.411 -60.342 1.00 35.33  ? 93  SER   B N   1 
ATOM   3748 C CA  . SER   B 1 93  ? -15.435 -34.086 -59.080 1.00 36.90  ? 93  SER   B CA  1 
ATOM   3749 C C   . SER   B 1 93  ? -16.411 -33.696 -57.974 1.00 36.68  ? 93  SER   B C   1 
ATOM   3750 O O   . SER   B 1 93  ? -16.517 -34.426 -56.983 1.00 36.47  ? 93  SER   B O   1 
ATOM   3751 C CB  . SER   B 1 93  ? -14.000 -33.798 -58.642 1.00 37.26  ? 93  SER   B CB  1 
ATOM   3752 O OG  . SER   B 1 93  ? -13.715 -32.413 -58.716 1.00 40.36  ? 93  SER   B OG  1 
ATOM   3753 N N   . PHE   B 1 94  ? -17.121 -32.575 -58.114 1.00 37.64  ? 94  PHE   B N   1 
ATOM   3754 C CA  . PHE   B 1 94  ? -18.097 -32.165 -57.109 1.00 37.16  ? 94  PHE   B CA  1 
ATOM   3755 C C   . PHE   B 1 94  ? -19.413 -32.902 -57.313 1.00 38.89  ? 94  PHE   B C   1 
ATOM   3756 O O   . PHE   B 1 94  ? -19.875 -33.070 -58.443 1.00 39.12  ? 94  PHE   B O   1 
ATOM   3757 C CB  . PHE   B 1 94  ? -18.348 -30.656 -57.162 1.00 35.79  ? 94  PHE   B CB  1 
ATOM   3758 C CG  . PHE   B 1 94  ? -17.154 -29.815 -56.791 1.00 36.26  ? 94  PHE   B CG  1 
ATOM   3759 C CD1 . PHE   B 1 94  ? -16.207 -29.465 -57.741 1.00 37.08  ? 94  PHE   B CD1 1 
ATOM   3760 C CD2 . PHE   B 1 94  ? -16.988 -29.367 -55.491 1.00 37.59  ? 94  PHE   B CD2 1 
ATOM   3761 C CE1 . PHE   B 1 94  ? -15.117 -28.686 -57.401 1.00 38.96  ? 94  PHE   B CE1 1 
ATOM   3762 C CE2 . PHE   B 1 94  ? -15.899 -28.593 -55.144 1.00 38.63  ? 94  PHE   B CE2 1 
ATOM   3763 C CZ  . PHE   B 1 94  ? -14.962 -28.250 -56.104 1.00 40.08  ? 94  PHE   B CZ  1 
ATOM   3764 N N   . ASP   B 1 95  ? -20.027 -33.330 -56.215 1.00 35.98  ? 95  ASP   B N   1 
ATOM   3765 C CA  . ASP   B 1 95  ? -21.277 -34.069 -56.315 1.00 38.13  ? 95  ASP   B CA  1 
ATOM   3766 C C   . ASP   B 1 95  ? -22.428 -33.129 -56.656 1.00 37.48  ? 95  ASP   B C   1 
ATOM   3767 O O   . ASP   B 1 95  ? -22.530 -32.022 -56.120 1.00 37.48  ? 95  ASP   B O   1 
ATOM   3768 C CB  . ASP   B 1 95  ? -21.570 -34.806 -55.007 1.00 39.40  ? 95  ASP   B CB  1 
ATOM   3769 C CG  . ASP   B 1 95  ? -20.906 -36.173 -54.935 1.00 43.07  ? 95  ASP   B CG  1 
ATOM   3770 O OD1 . ASP   B 1 95  ? -20.173 -36.545 -55.879 1.00 44.53  ? 95  ASP   B OD1 1 
ATOM   3771 O OD2 . ASP   B 1 95  ? -21.106 -36.870 -53.919 1.00 42.29  ? 95  ASP   B OD2 1 
ATOM   3772 N N   . ILE   B 1 96  ? -23.276 -33.566 -57.585 1.00 36.35  ? 96  ILE   B N   1 
ATOM   3773 C CA  . ILE   B 1 96  ? -24.566 -32.943 -57.851 1.00 39.02  ? 96  ILE   B CA  1 
ATOM   3774 C C   . ILE   B 1 96  ? -25.601 -34.056 -57.878 1.00 40.51  ? 96  ILE   B C   1 
ATOM   3775 O O   . ILE   B 1 96  ? -25.426 -35.048 -58.595 1.00 41.17  ? 96  ILE   B O   1 
ATOM   3776 C CB  . ILE   B 1 96  ? -24.583 -32.154 -59.175 1.00 40.46  ? 96  ILE   B CB  1 
ATOM   3777 C CG1 . ILE   B 1 96  ? -23.755 -30.874 -59.054 1.00 40.59  ? 96  ILE   B CG1 1 
ATOM   3778 C CG2 . ILE   B 1 96  ? -26.008 -31.803 -59.570 1.00 41.81  ? 96  ILE   B CG2 1 
ATOM   3779 C CD1 . ILE   B 1 96  ? -23.794 -30.018 -60.299 1.00 36.65  ? 96  ILE   B CD1 1 
ATOM   3780 N N   . ALA   B 1 97  ? -26.657 -33.906 -57.081 1.00 37.78  ? 97  ALA   B N   1 
ATOM   3781 C CA  . ALA   B 1 97  ? -27.684 -34.936 -56.977 1.00 42.61  ? 97  ALA   B CA  1 
ATOM   3782 C C   . ALA   B 1 97  ? -28.250 -35.271 -58.351 1.00 43.74  ? 97  ALA   B C   1 
ATOM   3783 O O   . ALA   B 1 97  ? -28.721 -34.385 -59.071 1.00 44.97  ? 97  ALA   B O   1 
ATOM   3784 C CB  . ALA   B 1 97  ? -28.796 -34.469 -56.039 1.00 44.86  ? 97  ALA   B CB  1 
ATOM   3785 N N   . GLY   B 1 98  ? -28.188 -36.550 -58.720 1.00 43.56  ? 98  GLY   B N   1 
ATOM   3786 C CA  . GLY   B 1 98  ? -28.700 -37.009 -59.993 1.00 43.04  ? 98  GLY   B CA  1 
ATOM   3787 C C   . GLY   B 1 98  ? -27.701 -37.014 -61.132 1.00 41.11  ? 98  GLY   B C   1 
ATOM   3788 O O   . GLY   B 1 98  ? -28.009 -37.552 -62.202 1.00 40.86  ? 98  GLY   B O   1 
ATOM   3789 N N   . LEU   B 1 99  ? -26.519 -36.442 -60.941 1.00 38.74  ? 99  LEU   B N   1 
ATOM   3790 C CA  . LEU   B 1 99  ? -25.496 -36.388 -61.969 1.00 40.27  ? 99  LEU   B CA  1 
ATOM   3791 C C   . LEU   B 1 99  ? -24.355 -37.343 -61.628 1.00 38.33  ? 99  LEU   B C   1 
ATOM   3792 O O   . LEU   B 1 99  ? -24.119 -37.636 -60.452 1.00 38.81  ? 99  LEU   B O   1 
ATOM   3793 C CB  . LEU   B 1 99  ? -24.943 -34.963 -62.112 1.00 41.66  ? 99  LEU   B CB  1 
ATOM   3794 C CG  . LEU   B 1 99  ? -25.820 -33.972 -62.885 1.00 40.26  ? 99  LEU   B CG  1 
ATOM   3795 C CD1 . LEU   B 1 99  ? -25.027 -32.738 -63.278 1.00 41.12  ? 99  LEU   B CD1 1 
ATOM   3796 C CD2 . LEU   B 1 99  ? -26.444 -34.622 -64.110 1.00 40.20  ? 99  LEU   B CD2 1 
ATOM   3797 N N   . PRO   B 1 100 ? -23.634 -37.851 -62.627 1.00 41.01  ? 100 PRO   B N   1 
ATOM   3798 C CA  . PRO   B 1 100 ? -22.519 -38.760 -62.339 1.00 39.44  ? 100 PRO   B CA  1 
ATOM   3799 C C   . PRO   B 1 100 ? -21.328 -38.017 -61.753 1.00 39.27  ? 100 PRO   B C   1 
ATOM   3800 O O   . PRO   B 1 100 ? -21.097 -36.841 -62.042 1.00 40.55  ? 100 PRO   B O   1 
ATOM   3801 C CB  . PRO   B 1 100 ? -22.173 -39.360 -63.709 1.00 40.85  ? 100 PRO   B CB  1 
ATOM   3802 C CG  . PRO   B 1 100 ? -23.238 -38.888 -64.658 1.00 36.37  ? 100 PRO   B CG  1 
ATOM   3803 C CD  . PRO   B 1 100 ? -23.830 -37.654 -64.072 1.00 41.03  ? 100 PRO   B CD  1 
ATOM   3804 N N   . THR   B 1 101 ? -20.570 -38.723 -60.912 1.00 36.90  ? 101 THR   B N   1 
ATOM   3805 C CA  . THR   B 1 101 ? -19.317 -38.228 -60.342 1.00 35.65  ? 101 THR   B CA  1 
ATOM   3806 C C   . THR   B 1 101 ? -18.314 -39.369 -60.467 1.00 38.31  ? 101 THR   B C   1 
ATOM   3807 O O   . THR   B 1 101 ? -18.227 -40.234 -59.591 1.00 38.01  ? 101 THR   B O   1 
ATOM   3808 C CB  . THR   B 1 101 ? -19.479 -37.784 -58.895 1.00 32.54  ? 101 THR   B CB  1 
ATOM   3809 O OG1 . THR   B 1 101 ? -20.464 -36.748 -58.823 1.00 42.64  ? 101 THR   B OG1 1 
ATOM   3810 C CG2 . THR   B 1 101 ? -18.163 -37.240 -58.363 1.00 36.50  ? 101 THR   B CG2 1 
ATOM   3811 N N   . SER   B 1 102 ? -17.552 -39.369 -61.558 1.00 33.86  ? 102 SER   B N   1 
ATOM   3812 C CA  . SER   B 1 102 ? -16.661 -40.479 -61.854 1.00 38.19  ? 102 SER   B CA  1 
ATOM   3813 C C   . SER   B 1 102 ? -15.202 -40.185 -61.561 1.00 38.09  ? 102 SER   B C   1 
ATOM   3814 O O   . SER   B 1 102 ? -14.421 -41.130 -61.404 1.00 41.12  ? 102 SER   B O   1 
ATOM   3815 C CB  . SER   B 1 102 ? -16.788 -40.881 -63.328 1.00 37.98  ? 102 SER   B CB  1 
ATOM   3816 O OG  . SER   B 1 102 ? -16.111 -39.955 -64.159 1.00 39.98  ? 102 SER   B OG  1 
ATOM   3817 N N   . TRP   B 1 103 ? -14.822 -38.909 -61.494 1.00 39.33  ? 103 TRP   B N   1 
ATOM   3818 C CA  . TRP   B 1 103 ? -13.425 -38.489 -61.453 1.00 38.33  ? 103 TRP   B CA  1 
ATOM   3819 C C   . TRP   B 1 103 ? -12.645 -39.028 -62.647 1.00 41.04  ? 103 TRP   B C   1 
ATOM   3820 O O   . TRP   B 1 103 ? -11.419 -39.152 -62.591 1.00 40.27  ? 103 TRP   B O   1 
ATOM   3821 C CB  . TRP   B 1 103 ? -12.756 -38.907 -60.139 1.00 36.80  ? 103 TRP   B CB  1 
ATOM   3822 C CG  . TRP   B 1 103 ? -13.220 -38.115 -58.958 1.00 37.25  ? 103 TRP   B CG  1 
ATOM   3823 C CD1 . TRP   B 1 103 ? -14.456 -37.564 -58.776 1.00 36.06  ? 103 TRP   B CD1 1 
ATOM   3824 C CD2 . TRP   B 1 103 ? -12.470 -37.816 -57.777 1.00 36.17  ? 103 TRP   B CD2 1 
ATOM   3825 N NE1 . TRP   B 1 103 ? -14.514 -36.923 -57.566 1.00 35.59  ? 103 TRP   B NE1 1 
ATOM   3826 C CE2 . TRP   B 1 103 ? -13.309 -37.064 -56.930 1.00 37.64  ? 103 TRP   B CE2 1 
ATOM   3827 C CE3 . TRP   B 1 103 ? -11.168 -38.103 -57.355 1.00 39.74  ? 103 TRP   B CE3 1 
ATOM   3828 C CZ2 . TRP   B 1 103 ? -12.888 -36.595 -55.686 1.00 38.73  ? 103 TRP   B CZ2 1 
ATOM   3829 C CZ3 . TRP   B 1 103 ? -10.753 -37.637 -56.120 1.00 40.16  ? 103 TRP   B CZ3 1 
ATOM   3830 C CH2 . TRP   B 1 103 ? -11.611 -36.892 -55.300 1.00 37.12  ? 103 TRP   B CH2 1 
ATOM   3831 N N   . GLY   B 1 104 ? -13.348 -39.342 -63.737 1.00 40.43  ? 104 GLY   B N   1 
ATOM   3832 C CA  . GLY   B 1 104 ? -12.711 -39.802 -64.954 1.00 41.83  ? 104 GLY   B CA  1 
ATOM   3833 C C   . GLY   B 1 104 ? -12.428 -41.282 -65.016 1.00 38.71  ? 104 GLY   B C   1 
ATOM   3834 O O   . GLY   B 1 104 ? -11.837 -41.740 -66.001 1.00 40.15  ? 104 GLY   B O   1 
ATOM   3835 N N   . PHE   B 1 105 ? -12.822 -42.041 -63.996 1.00 40.01  ? 105 PHE   B N   1 
ATOM   3836 C CA  . PHE   B 1 105 ? -12.662 -43.486 -63.994 1.00 42.47  ? 105 PHE   B CA  1 
ATOM   3837 C C   . PHE   B 1 105 ? -13.823 -44.117 -64.745 1.00 40.72  ? 105 PHE   B C   1 
ATOM   3838 O O   . PHE   B 1 105 ? -14.983 -43.751 -64.526 1.00 41.61  ? 105 PHE   B O   1 
ATOM   3839 C CB  . PHE   B 1 105 ? -12.606 -44.025 -62.565 1.00 40.60  ? 105 PHE   B CB  1 
ATOM   3840 C CG  . PHE   B 1 105 ? -11.382 -43.604 -61.808 1.00 40.02  ? 105 PHE   B CG  1 
ATOM   3841 C CD1 . PHE   B 1 105 ? -10.150 -44.151 -62.108 1.00 42.56  ? 105 PHE   B CD1 1 
ATOM   3842 C CD2 . PHE   B 1 105 ? -11.469 -42.679 -60.780 1.00 41.96  ? 105 PHE   B CD2 1 
ATOM   3843 C CE1 . PHE   B 1 105 ? -9.021  -43.776 -61.408 1.00 45.42  ? 105 PHE   B CE1 1 
ATOM   3844 C CE2 . PHE   B 1 105 ? -10.342 -42.298 -60.075 1.00 42.33  ? 105 PHE   B CE2 1 
ATOM   3845 C CZ  . PHE   B 1 105 ? -9.116  -42.847 -60.390 1.00 41.88  ? 105 PHE   B CZ  1 
ATOM   3846 N N   . ALA   B 1 106 ? -13.505 -45.057 -65.635 1.00 42.02  ? 106 ALA   B N   1 
ATOM   3847 C CA  . ALA   B 1 106 ? -14.545 -45.765 -66.371 1.00 39.99  ? 106 ALA   B CA  1 
ATOM   3848 C C   . ALA   B 1 106 ? -15.429 -46.576 -65.433 1.00 40.70  ? 106 ALA   B C   1 
ATOM   3849 O O   . ALA   B 1 106 ? -16.648 -46.656 -65.628 1.00 39.99  ? 106 ALA   B O   1 
ATOM   3850 C CB  . ALA   B 1 106 ? -13.909 -46.669 -67.425 1.00 36.91  ? 106 ALA   B CB  1 
ATOM   3851 N N   . GLU   B 1 107 ? -14.830 -47.186 -64.409 1.00 40.21  ? 107 GLU   B N   1 
ATOM   3852 C CA  . GLU   B 1 107 ? -15.604 -47.963 -63.450 1.00 42.26  ? 107 GLU   B CA  1 
ATOM   3853 C C   . GLU   B 1 107 ? -16.594 -47.101 -62.681 1.00 44.20  ? 107 GLU   B C   1 
ATOM   3854 O O   . GLU   B 1 107 ? -17.581 -47.626 -62.158 1.00 44.65  ? 107 GLU   B O   1 
ATOM   3855 C CB  . GLU   B 1 107 ? -14.668 -48.675 -62.473 1.00 43.48  ? 107 GLU   B CB  1 
ATOM   3856 C CG  . GLU   B 1 107 ? -13.717 -47.740 -61.741 1.00 48.93  ? 107 GLU   B CG  1 
ATOM   3857 C CD  . GLU   B 1 107 ? -12.932 -48.432 -60.639 1.00 53.96  ? 107 GLU   B CD  1 
ATOM   3858 O OE1 . GLU   B 1 107 ? -13.500 -49.317 -59.963 1.00 56.63  ? 107 GLU   B OE1 1 
ATOM   3859 O OE2 . GLU   B 1 107 ? -11.750 -48.076 -60.438 1.00 53.63  ? 107 GLU   B OE2 1 
ATOM   3860 N N   . HIS   B 1 108 ? -16.361 -45.793 -62.611 1.00 42.55  ? 108 HIS   B N   1 
ATOM   3861 C CA  . HIS   B 1 108 ? -17.222 -44.884 -61.869 1.00 41.65  ? 108 HIS   B CA  1 
ATOM   3862 C C   . HIS   B 1 108 ? -18.086 -44.021 -62.779 1.00 42.11  ? 108 HIS   B C   1 
ATOM   3863 O O   . HIS   B 1 108 ? -18.754 -43.103 -62.291 1.00 43.78  ? 108 HIS   B O   1 
ATOM   3864 C CB  . HIS   B 1 108 ? -16.374 -44.007 -60.947 1.00 41.39  ? 108 HIS   B CB  1 
ATOM   3865 C CG  . HIS   B 1 108 ? -15.592 -44.785 -59.935 1.00 42.88  ? 108 HIS   B CG  1 
ATOM   3866 N ND1 . HIS   B 1 108 ? -16.119 -45.864 -59.256 1.00 45.57  ? 108 HIS   B ND1 1 
ATOM   3867 C CD2 . HIS   B 1 108 ? -14.314 -44.660 -59.506 1.00 41.97  ? 108 HIS   B CD2 1 
ATOM   3868 C CE1 . HIS   B 1 108 ? -15.205 -46.358 -58.441 1.00 42.73  ? 108 HIS   B CE1 1 
ATOM   3869 N NE2 . HIS   B 1 108 ? -14.100 -45.647 -58.574 1.00 41.20  ? 108 HIS   B NE2 1 
ATOM   3870 N N   . ALA   B 1 109 ? -18.103 -44.303 -64.087 1.00 41.35  ? 109 ALA   B N   1 
ATOM   3871 C CA  . ALA   B 1 109 ? -18.901 -43.518 -65.024 1.00 41.90  ? 109 ALA   B CA  1 
ATOM   3872 C C   . ALA   B 1 109 ? -20.385 -43.553 -64.692 1.00 41.85  ? 109 ALA   B C   1 
ATOM   3873 O O   . ALA   B 1 109 ? -21.125 -42.653 -65.108 1.00 40.06  ? 109 ALA   B O   1 
ATOM   3874 C CB  . ALA   B 1 109 ? -18.677 -44.020 -66.452 1.00 38.09  ? 109 ALA   B CB  1 
ATOM   3875 N N   . ASP   B 1 110 ? -20.832 -44.564 -63.950 1.00 44.80  ? 110 ASP   B N   1 
ATOM   3876 C CA  . ASP   B 1 110 ? -22.236 -44.720 -63.599 1.00 45.32  ? 110 ASP   B CA  1 
ATOM   3877 C C   . ASP   B 1 110 ? -22.507 -44.456 -62.123 1.00 43.36  ? 110 ASP   B C   1 
ATOM   3878 O O   . ASP   B 1 110 ? -23.605 -44.763 -61.646 1.00 44.71  ? 110 ASP   B O   1 
ATOM   3879 C CB  . ASP   B 1 110 ? -22.721 -46.125 -63.964 1.00 46.05  ? 110 ASP   B CB  1 
ATOM   3880 C CG  . ASP   B 1 110 ? -21.705 -47.199 -63.630 1.00 49.99  ? 110 ASP   B CG  1 
ATOM   3881 O OD1 . ASP   B 1 110 ? -22.123 -48.298 -63.216 1.00 55.53  ? 110 ASP   B OD1 1 
ATOM   3882 O OD2 . ASP   B 1 110 ? -20.490 -46.950 -63.788 1.00 58.66  ? 110 ASP   B OD2 1 
ATOM   3883 N N   . HIS   B 1 111 ? -21.541 -43.911 -61.384 1.00 39.98  ? 111 HIS   B N   1 
ATOM   3884 C CA  . HIS   B 1 111 ? -21.772 -43.558 -59.987 1.00 41.54  ? 111 HIS   B CA  1 
ATOM   3885 C C   . HIS   B 1 111 ? -22.518 -42.230 -59.941 1.00 39.62  ? 111 HIS   B C   1 
ATOM   3886 O O   . HIS   B 1 111 ? -21.958 -41.182 -60.275 1.00 41.47  ? 111 HIS   B O   1 
ATOM   3887 C CB  . HIS   B 1 111 ? -20.465 -43.470 -59.207 1.00 37.59  ? 111 HIS   B CB  1 
ATOM   3888 C CG  . HIS   B 1 111 ? -20.585 -42.676 -57.944 1.00 42.83  ? 111 HIS   B CG  1 
ATOM   3889 N ND1 . HIS   B 1 111 ? -20.032 -41.422 -57.794 1.00 39.79  ? 111 HIS   B ND1 1 
ATOM   3890 C CD2 . HIS   B 1 111 ? -21.240 -42.938 -56.788 1.00 41.52  ? 111 HIS   B CD2 1 
ATOM   3891 C CE1 . HIS   B 1 111 ? -20.316 -40.959 -56.591 1.00 39.89  ? 111 HIS   B CE1 1 
ATOM   3892 N NE2 . HIS   B 1 111 ? -21.049 -41.858 -55.960 1.00 43.39  ? 111 HIS   B NE2 1 
ATOM   3893 N N   . ILE   B 1 112 ? -23.776 -42.271 -59.517 1.00 39.22  ? 112 ILE   B N   1 
ATOM   3894 C CA  . ILE   B 1 112 ? -24.635 -41.094 -59.485 1.00 40.32  ? 112 ILE   B CA  1 
ATOM   3895 C C   . ILE   B 1 112 ? -24.679 -40.579 -58.054 1.00 40.29  ? 112 ILE   B C   1 
ATOM   3896 O O   . ILE   B 1 112 ? -25.030 -41.321 -57.129 1.00 42.83  ? 112 ILE   B O   1 
ATOM   3897 C CB  . ILE   B 1 112 ? -26.043 -41.417 -60.009 1.00 39.92  ? 112 ILE   B CB  1 
ATOM   3898 C CG1 . ILE   B 1 112 ? -25.954 -42.224 -61.304 1.00 41.47  ? 112 ILE   B CG1 1 
ATOM   3899 C CG2 . ILE   B 1 112 ? -26.832 -40.146 -60.243 1.00 40.44  ? 112 ILE   B CG2 1 
ATOM   3900 C CD1 . ILE   B 1 112 ? -25.101 -41.562 -62.375 1.00 40.92  ? 112 ILE   B CD1 1 
ATOM   3901 N N   . ALA   B 1 113 ? -24.308 -39.316 -57.866 1.00 40.03  ? 113 ALA   B N   1 
ATOM   3902 C CA  . ALA   B 1 113 ? -24.351 -38.724 -56.539 1.00 38.76  ? 113 ALA   B CA  1 
ATOM   3903 C C   . ALA   B 1 113 ? -25.791 -38.593 -56.070 1.00 40.43  ? 113 ALA   B C   1 
ATOM   3904 O O   . ALA   B 1 113 ? -26.690 -38.266 -56.850 1.00 42.24  ? 113 ALA   B O   1 
ATOM   3905 C CB  . ALA   B 1 113 ? -23.672 -37.358 -56.540 1.00 39.85  ? 113 ALA   B CB  1 
ATOM   3906 N N   . THR   B 1 114 ? -26.006 -38.842 -54.780 1.00 39.71  ? 114 THR   B N   1 
ATOM   3907 C CA  . THR   B 1 114 ? -27.341 -38.836 -54.202 1.00 41.48  ? 114 THR   B CA  1 
ATOM   3908 C C   . THR   B 1 114 ? -27.709 -37.515 -53.539 1.00 41.36  ? 114 THR   B C   1 
ATOM   3909 O O   . THR   B 1 114 ? -28.887 -37.308 -53.230 1.00 42.65  ? 114 THR   B O   1 
ATOM   3910 C CB  . THR   B 1 114 ? -27.472 -39.974 -53.185 1.00 43.45  ? 114 THR   B CB  1 
ATOM   3911 O OG1 . THR   B 1 114 ? -26.382 -39.912 -52.259 1.00 42.77  ? 114 THR   B OG1 1 
ATOM   3912 C CG2 . THR   B 1 114 ? -27.440 -41.321 -53.895 1.00 42.00  ? 114 THR   B CG2 1 
ATOM   3913 N N   . ALA   B 1 115 ? -26.745 -36.625 -53.315 1.00 42.24  ? 115 ALA   B N   1 
ATOM   3914 C CA  . ALA   B 1 115 ? -27.029 -35.322 -52.735 1.00 42.08  ? 115 ALA   B CA  1 
ATOM   3915 C C   . ALA   B 1 115 ? -26.018 -34.313 -53.257 1.00 37.67  ? 115 ALA   B C   1 
ATOM   3916 O O   . ALA   B 1 115 ? -24.908 -34.668 -53.663 1.00 38.29  ? 115 ALA   B O   1 
ATOM   3917 C CB  . ALA   B 1 115 ? -26.995 -35.363 -51.203 1.00 37.07  ? 115 ALA   B CB  1 
ATOM   3918 N N   . ASP   B 1 116 ? -26.417 -33.043 -53.238 1.00 40.34  ? 116 ASP   B N   1 
ATOM   3919 C CA  . ASP   B 1 116 ? -25.532 -31.972 -53.680 1.00 42.06  ? 116 ASP   B CA  1 
ATOM   3920 C C   . ASP   B 1 116 ? -24.343 -31.842 -52.735 1.00 37.77  ? 116 ASP   B C   1 
ATOM   3921 O O   . ASP   B 1 116 ? -24.486 -31.951 -51.513 1.00 35.25  ? 116 ASP   B O   1 
ATOM   3922 C CB  . ASP   B 1 116 ? -26.284 -30.639 -53.745 1.00 39.63  ? 116 ASP   B CB  1 
ATOM   3923 C CG  . ASP   B 1 116 ? -27.254 -30.559 -54.919 1.00 45.06  ? 116 ASP   B CG  1 
ATOM   3924 O OD1 . ASP   B 1 116 ? -27.033 -31.246 -55.940 1.00 44.69  ? 116 ASP   B OD1 1 
ATOM   3925 O OD2 . ASP   B 1 116 ? -28.239 -29.792 -54.821 1.00 48.40  ? 116 ASP   B OD2 1 
ATOM   3926 N N   . SER   B 1 117 ? -23.162 -31.617 -53.308 1.00 38.87  ? 117 SER   B N   1 
ATOM   3927 C CA  . SER   B 1 117 ? -22.012 -31.233 -52.504 1.00 38.48  ? 117 SER   B CA  1 
ATOM   3928 C C   . SER   B 1 117 ? -22.297 -29.912 -51.796 1.00 39.97  ? 117 SER   B C   1 
ATOM   3929 O O   . SER   B 1 117 ? -23.199 -29.158 -52.172 1.00 41.98  ? 117 SER   B O   1 
ATOM   3930 C CB  . SER   B 1 117 ? -20.755 -31.115 -53.372 1.00 37.65  ? 117 SER   B CB  1 
ATOM   3931 O OG  . SER   B 1 117 ? -20.892 -30.110 -54.362 1.00 41.28  ? 117 SER   B OG  1 
ATOM   3932 N N   . LEU   B 1 118 ? -21.520 -29.638 -50.746 1.00 38.92  ? 118 LEU   B N   1 
ATOM   3933 C CA  . LEU   B 1 118 ? -21.748 -28.423 -49.969 1.00 40.50  ? 118 LEU   B CA  1 
ATOM   3934 C C   . LEU   B 1 118 ? -21.586 -27.180 -50.835 1.00 40.19  ? 118 LEU   B C   1 
ATOM   3935 O O   . LEU   B 1 118 ? -22.415 -26.264 -50.789 1.00 40.47  ? 118 LEU   B O   1 
ATOM   3936 C CB  . LEU   B 1 118 ? -20.801 -28.374 -48.767 1.00 40.78  ? 118 LEU   B CB  1 
ATOM   3937 C CG  . LEU   B 1 118 ? -20.803 -27.069 -47.961 1.00 39.85  ? 118 LEU   B CG  1 
ATOM   3938 C CD1 . LEU   B 1 118 ? -20.665 -27.384 -46.491 1.00 38.43  ? 118 LEU   B CD1 1 
ATOM   3939 C CD2 . LEU   B 1 118 ? -19.692 -26.108 -48.400 1.00 42.02  ? 118 LEU   B CD2 1 
ATOM   3940 N N   . VAL   B 1 119 ? -20.516 -27.131 -51.634 1.00 41.84  ? 119 VAL   B N   1 
ATOM   3941 C CA  . VAL   B 1 119 ? -20.254 -25.955 -52.462 1.00 41.71  ? 119 VAL   B CA  1 
ATOM   3942 C C   . VAL   B 1 119 ? -21.378 -25.751 -53.470 1.00 40.38  ? 119 VAL   B C   1 
ATOM   3943 O O   . VAL   B 1 119 ? -21.807 -24.619 -53.725 1.00 41.39  ? 119 VAL   B O   1 
ATOM   3944 C CB  . VAL   B 1 119 ? -18.883 -26.085 -53.150 1.00 39.52  ? 119 VAL   B CB  1 
ATOM   3945 C CG1 . VAL   B 1 119 ? -18.837 -25.259 -54.425 1.00 35.65  ? 119 VAL   B CG1 1 
ATOM   3946 C CG2 . VAL   B 1 119 ? -17.771 -25.667 -52.197 1.00 37.21  ? 119 VAL   B CG2 1 
ATOM   3947 N N   . VAL   B 1 120 ? -21.878 -26.840 -54.054 1.00 38.25  ? 120 VAL   B N   1 
ATOM   3948 C CA  . VAL   B 1 120 ? -23.040 -26.741 -54.933 1.00 40.23  ? 120 VAL   B CA  1 
ATOM   3949 C C   . VAL   B 1 120 ? -24.247 -26.241 -54.149 1.00 42.52  ? 120 VAL   B C   1 
ATOM   3950 O O   . VAL   B 1 120 ? -24.983 -25.353 -54.600 1.00 39.12  ? 120 VAL   B O   1 
ATOM   3951 C CB  . VAL   B 1 120 ? -23.317 -28.097 -55.607 1.00 37.96  ? 120 VAL   B CB  1 
ATOM   3952 C CG1 . VAL   B 1 120 ? -24.727 -28.141 -56.169 1.00 40.35  ? 120 VAL   B CG1 1 
ATOM   3953 C CG2 . VAL   B 1 120 ? -22.301 -28.343 -56.712 1.00 39.04  ? 120 VAL   B CG2 1 
ATOM   3954 N N   . SER   B 1 121 ? -24.449 -26.791 -52.949 1.00 42.10  ? 121 SER   B N   1 
ATOM   3955 C CA  . SER   B 1 121 ? -25.584 -26.398 -52.121 1.00 40.19  ? 121 SER   B CA  1 
ATOM   3956 C C   . SER   B 1 121 ? -25.549 -24.909 -51.795 1.00 39.10  ? 121 SER   B C   1 
ATOM   3957 O O   . SER   B 1 121 ? -26.585 -24.234 -51.828 1.00 39.23  ? 121 SER   B O   1 
ATOM   3958 C CB  . SER   B 1 121 ? -25.594 -27.229 -50.839 1.00 39.12  ? 121 SER   B CB  1 
ATOM   3959 O OG  . SER   B 1 121 ? -26.878 -27.237 -50.250 1.00 51.64  ? 121 SER   B OG  1 
ATOM   3960 N N   . ARG   B 1 122 ? -24.365 -24.378 -51.486 1.00 36.37  ? 122 ARG   B N   1 
ATOM   3961 C CA  . ARG   B 1 122 ? -24.255 -22.961 -51.153 1.00 39.38  ? 122 ARG   B CA  1 
ATOM   3962 C C   . ARG   B 1 122 ? -24.575 -22.082 -52.356 1.00 38.52  ? 122 ARG   B C   1 
ATOM   3963 O O   . ARG   B 1 122 ? -25.312 -21.096 -52.239 1.00 36.87  ? 122 ARG   B O   1 
ATOM   3964 C CB  . ARG   B 1 122 ? -22.858 -22.654 -50.617 1.00 35.41  ? 122 ARG   B CB  1 
ATOM   3965 C CG  . ARG   B 1 122 ? -22.584 -23.263 -49.259 1.00 36.25  ? 122 ARG   B CG  1 
ATOM   3966 C CD  . ARG   B 1 122 ? -23.231 -22.427 -48.165 1.00 34.83  ? 122 ARG   B CD  1 
ATOM   3967 N NE  . ARG   B 1 122 ? -22.620 -22.655 -46.861 1.00 35.63  ? 122 ARG   B NE  1 
ATOM   3968 C CZ  . ARG   B 1 122 ? -21.620 -21.933 -46.374 1.00 41.22  ? 122 ARG   B CZ  1 
ATOM   3969 N NH1 . ARG   B 1 122 ? -21.091 -20.935 -47.063 1.00 38.05  ? 122 ARG   B NH1 1 
ATOM   3970 N NH2 . ARG   B 1 122 ? -21.135 -22.225 -45.169 1.00 38.22  ? 122 ARG   B NH2 1 
ATOM   3971 N N   . LEU   B 1 123 ? -24.023 -22.418 -53.524 1.00 38.79  ? 123 LEU   B N   1 
ATOM   3972 C CA  . LEU   B 1 123 ? -24.276 -21.610 -54.712 1.00 37.35  ? 123 LEU   B CA  1 
ATOM   3973 C C   . LEU   B 1 123 ? -25.741 -21.681 -55.126 1.00 39.34  ? 123 LEU   B C   1 
ATOM   3974 O O   . LEU   B 1 123 ? -26.316 -20.679 -55.564 1.00 39.36  ? 123 LEU   B O   1 
ATOM   3975 C CB  . LEU   B 1 123 ? -23.360 -22.057 -55.854 1.00 39.79  ? 123 LEU   B CB  1 
ATOM   3976 C CG  . LEU   B 1 123 ? -21.871 -21.808 -55.593 1.00 39.12  ? 123 LEU   B CG  1 
ATOM   3977 C CD1 . LEU   B 1 123 ? -21.006 -22.621 -56.540 1.00 42.23  ? 123 LEU   B CD1 1 
ATOM   3978 C CD2 . LEU   B 1 123 ? -21.550 -20.329 -55.708 1.00 35.59  ? 123 LEU   B CD2 1 
ATOM   3979 N N   . LYS   B 1 124 ? -26.366 -22.855 -54.986 1.00 39.62  ? 124 LYS   B N   1 
ATOM   3980 C CA  . LYS   B 1 124 ? -27.783 -22.976 -55.316 1.00 41.60  ? 124 LYS   B CA  1 
ATOM   3981 C C   . LYS   B 1 124 ? -28.641 -22.150 -54.367 1.00 39.80  ? 124 LYS   B C   1 
ATOM   3982 O O   . LYS   B 1 124 ? -29.623 -21.531 -54.791 1.00 38.87  ? 124 LYS   B O   1 
ATOM   3983 C CB  . LYS   B 1 124 ? -28.209 -24.445 -55.291 1.00 40.83  ? 124 LYS   B CB  1 
ATOM   3984 C CG  . LYS   B 1 124 ? -27.834 -25.218 -56.545 1.00 40.68  ? 124 LYS   B CG  1 
ATOM   3985 C CD  . LYS   B 1 124 ? -28.113 -26.700 -56.383 1.00 44.20  ? 124 LYS   B CD  1 
ATOM   3986 C CE  . LYS   B 1 124 ? -28.205 -27.397 -57.733 1.00 45.21  ? 124 LYS   B CE  1 
ATOM   3987 N NZ  . LYS   B 1 124 ? -28.604 -28.827 -57.595 1.00 43.55  ? 124 LYS   B NZ  1 
ATOM   3988 N N   . ALA   B 1 125 ? -28.286 -22.126 -53.081 1.00 40.02  ? 125 ALA   B N   1 
ATOM   3989 C CA  . ALA   B 1 125 ? -29.032 -21.316 -52.125 1.00 39.13  ? 125 ALA   B CA  1 
ATOM   3990 C C   . ALA   B 1 125 ? -28.891 -19.831 -52.425 1.00 42.03  ? 125 ALA   B C   1 
ATOM   3991 O O   . ALA   B 1 125 ? -29.778 -19.042 -52.077 1.00 45.57  ? 125 ALA   B O   1 
ATOM   3992 C CB  . ALA   B 1 125 ? -28.571 -21.627 -50.704 1.00 38.82  ? 125 ALA   B CB  1 
ATOM   3993 N N   . ALA   B 1 126 ? -27.793 -19.435 -53.068 1.00 39.54  ? 126 ALA   B N   1 
ATOM   3994 C CA  . ALA   B 1 126 ? -27.631 -18.080 -53.579 1.00 43.38  ? 126 ALA   B CA  1 
ATOM   3995 C C   . ALA   B 1 126 ? -28.316 -17.874 -54.925 1.00 43.65  ? 126 ALA   B C   1 
ATOM   3996 O O   . ALA   B 1 126 ? -28.215 -16.781 -55.490 1.00 45.60  ? 126 ALA   B O   1 
ATOM   3997 C CB  . ALA   B 1 126 ? -26.143 -17.733 -53.698 1.00 41.43  ? 126 ALA   B CB  1 
ATOM   3998 N N   . GLY   B 1 127 ? -28.987 -18.895 -55.457 1.00 43.86  ? 127 GLY   B N   1 
ATOM   3999 C CA  . GLY   B 1 127 ? -29.767 -18.766 -56.670 1.00 43.29  ? 127 GLY   B CA  1 
ATOM   4000 C C   . GLY   B 1 127 ? -29.095 -19.239 -57.941 1.00 43.69  ? 127 GLY   B C   1 
ATOM   4001 O O   . GLY   B 1 127 ? -29.679 -19.083 -59.022 1.00 43.25  ? 127 GLY   B O   1 
ATOM   4002 N N   . ALA   B 1 128 ? -27.898 -19.811 -57.856 1.00 39.85  ? 128 ALA   B N   1 
ATOM   4003 C CA  . ALA   B 1 128 ? -27.197 -20.228 -59.062 1.00 40.94  ? 128 ALA   B CA  1 
ATOM   4004 C C   . ALA   B 1 128 ? -27.882 -21.436 -59.688 1.00 43.20  ? 128 ALA   B C   1 
ATOM   4005 O O   . ALA   B 1 128 ? -28.445 -22.286 -58.991 1.00 42.48  ? 128 ALA   B O   1 
ATOM   4006 C CB  . ALA   B 1 128 ? -25.736 -20.546 -58.750 1.00 41.97  ? 128 ALA   B CB  1 
ATOM   4007 N N   . VAL   B 1 129 ? -27.849 -21.494 -61.016 1.00 42.45  ? 129 VAL   B N   1 
ATOM   4008 C CA  . VAL   B 1 129 ? -28.434 -22.586 -61.785 1.00 42.51  ? 129 VAL   B CA  1 
ATOM   4009 C C   . VAL   B 1 129 ? -27.293 -23.345 -62.445 1.00 42.33  ? 129 VAL   B C   1 
ATOM   4010 O O   . VAL   B 1 129 ? -26.480 -22.754 -63.166 1.00 40.21  ? 129 VAL   B O   1 
ATOM   4011 C CB  . VAL   B 1 129 ? -29.437 -22.073 -62.830 1.00 40.20  ? 129 VAL   B CB  1 
ATOM   4012 C CG1 . VAL   B 1 129 ? -29.805 -23.183 -63.798 1.00 45.02  ? 129 VAL   B CG1 1 
ATOM   4013 C CG2 . VAL   B 1 129 ? -30.682 -21.520 -62.148 1.00 39.20  ? 129 VAL   B CG2 1 
ATOM   4014 N N   . PHE   B 1 130 ? -27.227 -24.650 -62.199 1.00 42.24  ? 130 PHE   B N   1 
ATOM   4015 C CA  . PHE   B 1 130 ? -26.121 -25.477 -62.664 1.00 43.58  ? 130 PHE   B CA  1 
ATOM   4016 C C   . PHE   B 1 130 ? -26.513 -26.168 -63.966 1.00 44.97  ? 130 PHE   B C   1 
ATOM   4017 O O   . PHE   B 1 130 ? -27.402 -27.027 -63.982 1.00 46.80  ? 130 PHE   B O   1 
ATOM   4018 C CB  . PHE   B 1 130 ? -25.715 -26.485 -61.592 1.00 38.55  ? 130 PHE   B CB  1 
ATOM   4019 C CG  . PHE   B 1 130 ? -24.903 -25.883 -60.482 1.00 42.93  ? 130 PHE   B CG  1 
ATOM   4020 C CD1 . PHE   B 1 130 ? -25.517 -25.250 -59.415 1.00 40.73  ? 130 PHE   B CD1 1 
ATOM   4021 C CD2 . PHE   B 1 130 ? -23.519 -25.922 -60.521 1.00 43.98  ? 130 PHE   B CD2 1 
ATOM   4022 C CE1 . PHE   B 1 130 ? -24.765 -24.686 -58.398 1.00 41.53  ? 130 PHE   B CE1 1 
ATOM   4023 C CE2 . PHE   B 1 130 ? -22.764 -25.358 -59.509 1.00 41.78  ? 130 PHE   B CE2 1 
ATOM   4024 C CZ  . PHE   B 1 130 ? -23.389 -24.739 -58.447 1.00 42.71  ? 130 PHE   B CZ  1 
ATOM   4025 N N   . LEU   B 1 131 ? -25.840 -25.789 -65.056 1.00 44.47  ? 131 LEU   B N   1 
ATOM   4026 C CA  . LEU   B 1 131 ? -26.084 -26.388 -66.364 1.00 44.38  ? 131 LEU   B CA  1 
ATOM   4027 C C   . LEU   B 1 131 ? -25.469 -27.775 -66.483 1.00 44.53  ? 131 LEU   B C   1 
ATOM   4028 O O   . LEU   B 1 131 ? -25.967 -28.604 -67.252 1.00 45.25  ? 131 LEU   B O   1 
ATOM   4029 C CB  . LEU   B 1 131 ? -25.513 -25.495 -67.467 1.00 44.40  ? 131 LEU   B CB  1 
ATOM   4030 C CG  . LEU   B 1 131 ? -26.125 -24.119 -67.731 1.00 43.63  ? 131 LEU   B CG  1 
ATOM   4031 C CD1 . LEU   B 1 131 ? -26.026 -23.785 -69.207 1.00 45.73  ? 131 LEU   B CD1 1 
ATOM   4032 C CD2 . LEU   B 1 131 ? -27.569 -24.043 -67.263 1.00 45.01  ? 131 LEU   B CD2 1 
ATOM   4033 N N   . GLY   B 1 132 ? -24.388 -28.036 -65.752 1.00 44.61  ? 132 GLY   B N   1 
ATOM   4034 C CA  . GLY   B 1 132 ? -23.679 -29.297 -65.907 1.00 40.88  ? 132 GLY   B CA  1 
ATOM   4035 C C   . GLY   B 1 132 ? -22.321 -29.258 -65.240 1.00 40.59  ? 132 GLY   B C   1 
ATOM   4036 O O   . GLY   B 1 132 ? -22.093 -28.484 -64.303 1.00 40.70  ? 132 GLY   B O   1 
ATOM   4037 N N   . LYS   B 1 133 ? -21.421 -30.112 -65.730 1.00 39.39  ? 133 LYS   B N   1 
ATOM   4038 C CA  . LYS   B 1 133 ? -20.116 -30.286 -65.108 1.00 38.66  ? 133 LYS   B CA  1 
ATOM   4039 C C   . LYS   B 1 133 ? -19.022 -30.363 -66.164 1.00 39.13  ? 133 LYS   B C   1 
ATOM   4040 O O   . LYS   B 1 133 ? -19.247 -30.833 -67.283 1.00 41.38  ? 133 LYS   B O   1 
ATOM   4041 C CB  . LYS   B 1 133 ? -20.079 -31.538 -64.227 1.00 40.26  ? 133 LYS   B CB  1 
ATOM   4042 C CG  . LYS   B 1 133 ? -21.193 -31.598 -63.203 1.00 36.65  ? 133 LYS   B CG  1 
ATOM   4043 C CD  . LYS   B 1 133 ? -21.351 -33.000 -62.667 1.00 37.23  ? 133 LYS   B CD  1 
ATOM   4044 C CE  . LYS   B 1 133 ? -20.810 -33.084 -61.274 1.00 37.95  ? 133 LYS   B CE  1 
ATOM   4045 N NZ  . LYS   B 1 133 ? -20.269 -34.432 -60.947 1.00 37.18  ? 133 LYS   B NZ  1 
ATOM   4046 N N   . SER   B 1 134 ? -17.828 -29.915 -65.784 1.00 40.27  ? 134 SER   B N   1 
ATOM   4047 C CA  . SER   B 1 134 ? -16.714 -29.752 -66.708 1.00 38.14  ? 134 SER   B CA  1 
ATOM   4048 C C   . SER   B 1 134 ? -15.692 -30.878 -66.558 1.00 38.51  ? 134 SER   B C   1 
ATOM   4049 O O   . SER   B 1 134 ? -15.601 -31.539 -65.521 1.00 38.30  ? 134 SER   B O   1 
ATOM   4050 C CB  . SER   B 1 134 ? -16.040 -28.392 -66.506 1.00 38.70  ? 134 SER   B CB  1 
ATOM   4051 O OG  . SER   B 1 134 ? -15.901 -28.082 -65.131 1.00 42.07  ? 134 SER   B OG  1 
ATOM   4052 N N   . ASN   B 1 135 ? -14.905 -31.068 -67.617 1.00 37.17  ? 135 ASN   B N   1 
ATOM   4053 C CA  . ASN   B 1 135 ? -14.084 -32.260 -67.787 1.00 39.08  ? 135 ASN   B CA  1 
ATOM   4054 C C   . ASN   B 1 135 ? -12.895 -32.276 -66.829 1.00 39.60  ? 135 ASN   B C   1 
ATOM   4055 O O   . ASN   B 1 135 ? -12.445 -31.245 -66.324 1.00 40.06  ? 135 ASN   B O   1 
ATOM   4056 C CB  . ASN   B 1 135 ? -13.581 -32.351 -69.226 1.00 38.09  ? 135 ASN   B CB  1 
ATOM   4057 C CG  . ASN   B 1 135 ? -13.126 -33.744 -69.600 1.00 38.16  ? 135 ASN   B CG  1 
ATOM   4058 O OD1 . ASN   B 1 135 ? -13.505 -34.727 -68.958 1.00 38.17  ? 135 ASN   B OD1 1 
ATOM   4059 N ND2 . ASN   B 1 135 ? -12.310 -33.839 -70.646 1.00 38.41  ? 135 ASN   B ND2 1 
ATOM   4060 N N   . ILE   B 1 136 ? -12.369 -33.478 -66.609 1.00 38.26  ? 136 ILE   B N   1 
ATOM   4061 C CA  . ILE   B 1 136 ? -11.290 -33.723 -65.654 1.00 42.14  ? 136 ILE   B CA  1 
ATOM   4062 C C   . ILE   B 1 136 ? -10.415 -34.876 -66.146 1.00 43.02  ? 136 ILE   B C   1 
ATOM   4063 O O   . ILE   B 1 136 ? -10.872 -35.690 -66.962 1.00 42.27  ? 136 ILE   B O   1 
ATOM   4064 C CB  . ILE   B 1 136 ? -11.873 -34.019 -64.261 1.00 39.58  ? 136 ILE   B CB  1 
ATOM   4065 C CG1 . ILE   B 1 136 ? -13.079 -34.939 -64.404 1.00 41.96  ? 136 ILE   B CG1 1 
ATOM   4066 C CG2 . ILE   B 1 136 ? -12.306 -32.755 -63.537 1.00 37.61  ? 136 ILE   B CG2 1 
ATOM   4067 C CD1 . ILE   B 1 136 ? -12.722 -36.367 -64.452 1.00 40.41  ? 136 ILE   B CD1 1 
ATOM   4068 N N   . PRO   B 1 137 ? -9.167  -34.982 -65.695 1.00 42.54  ? 137 PRO   B N   1 
ATOM   4069 C CA  . PRO   B 1 137 ? -8.378  -36.191 -65.944 1.00 41.58  ? 137 PRO   B CA  1 
ATOM   4070 C C   . PRO   B 1 137 ? -8.744  -37.316 -64.989 1.00 40.67  ? 137 PRO   B C   1 
ATOM   4071 O O   . PRO   B 1 137 ? -9.367  -37.111 -63.945 1.00 40.14  ? 137 PRO   B O   1 
ATOM   4072 C CB  . PRO   B 1 137 ? -6.937  -35.730 -65.692 1.00 41.44  ? 137 PRO   B CB  1 
ATOM   4073 C CG  . PRO   B 1 137 ? -7.070  -34.615 -64.730 1.00 43.63  ? 137 PRO   B CG  1 
ATOM   4074 C CD  . PRO   B 1 137 ? -8.345  -33.912 -65.120 1.00 42.20  ? 137 PRO   B CD  1 
ATOM   4075 N N   . VAL   B 1 138 ? -8.305  -38.521 -65.359 1.00 39.79  ? 138 VAL   B N   1 
ATOM   4076 C CA  . VAL   B 1 138 ? -8.557  -39.708 -64.548 1.00 40.47  ? 138 VAL   B CA  1 
ATOM   4077 C C   . VAL   B 1 138 ? -7.974  -39.503 -63.157 1.00 41.59  ? 138 VAL   B C   1 
ATOM   4078 O O   . VAL   B 1 138 ? -6.765  -39.294 -62.996 1.00 41.98  ? 138 VAL   B O   1 
ATOM   4079 C CB  . VAL   B 1 138 ? -7.969  -40.954 -65.220 1.00 40.16  ? 138 VAL   B CB  1 
ATOM   4080 C CG1 . VAL   B 1 138 ? -8.467  -42.214 -64.532 1.00 42.44  ? 138 VAL   B CG1 1 
ATOM   4081 C CG2 . VAL   B 1 138 ? -8.320  -40.975 -66.695 1.00 39.62  ? 138 VAL   B CG2 1 
ATOM   4082 N N   . GLY   B 1 139 ? -8.834  -39.557 -62.143 1.00 40.40  ? 139 GLY   B N   1 
ATOM   4083 C CA  . GLY   B 1 139 ? -8.377  -39.393 -60.775 1.00 41.49  ? 139 GLY   B CA  1 
ATOM   4084 C C   . GLY   B 1 139 ? -7.836  -38.021 -60.442 1.00 42.67  ? 139 GLY   B C   1 
ATOM   4085 O O   . GLY   B 1 139 ? -7.191  -37.859 -59.402 1.00 43.71  ? 139 GLY   B O   1 
ATOM   4086 N N   . LEU   B 1 140 ? -8.084  -37.022 -61.297 1.00 41.23  ? 140 LEU   B N   1 
ATOM   4087 C CA  . LEU   B 1 140 ? -7.609  -35.651 -61.086 1.00 43.42  ? 140 LEU   B CA  1 
ATOM   4088 C C   . LEU   B 1 140 ? -6.097  -35.605 -60.886 1.00 44.10  ? 140 LEU   B C   1 
ATOM   4089 O O   . LEU   B 1 140 ? -5.580  -34.779 -60.130 1.00 45.51  ? 140 LEU   B O   1 
ATOM   4090 C CB  . LEU   B 1 140 ? -8.318  -34.982 -59.903 1.00 42.82  ? 140 LEU   B CB  1 
ATOM   4091 C CG  . LEU   B 1 140 ? -9.811  -35.227 -59.683 1.00 40.86  ? 140 LEU   B CG  1 
ATOM   4092 C CD1 . LEU   B 1 140 ? -10.314 -34.396 -58.511 1.00 40.34  ? 140 LEU   B CD1 1 
ATOM   4093 C CD2 . LEU   B 1 140 ? -10.595 -34.902 -60.939 1.00 39.46  ? 140 LEU   B CD2 1 
ATOM   4094 N N   . ALA   B 1 141 ? -5.371  -36.489 -61.567 1.00 43.24  ? 141 ALA   B N   1 
ATOM   4095 C CA  . ALA   B 1 141 ? -3.950  -36.677 -61.313 1.00 44.05  ? 141 ALA   B CA  1 
ATOM   4096 C C   . ALA   B 1 141 ? -3.071  -36.173 -62.455 1.00 44.90  ? 141 ALA   B C   1 
ATOM   4097 O O   . ALA   B 1 141 ? -2.025  -36.763 -62.737 1.00 50.06  ? 141 ALA   B O   1 
ATOM   4098 C CB  . ALA   B 1 141 ? -3.655  -38.151 -61.039 1.00 40.23  ? 141 ALA   B CB  1 
ATOM   4099 N N   . ASP   B 1 142 ? -3.458  -35.079 -63.109 1.00 45.01  ? 142 ASP   B N   1 
ATOM   4100 C CA  . ASP   B 1 142 ? -2.651  -34.549 -64.199 1.00 46.47  ? 142 ASP   B CA  1 
ATOM   4101 C C   . ASP   B 1 142 ? -2.910  -33.061 -64.385 1.00 47.91  ? 142 ASP   B C   1 
ATOM   4102 O O   . ASP   B 1 142 ? -3.832  -32.485 -63.805 1.00 46.08  ? 142 ASP   B O   1 
ATOM   4103 C CB  . ASP   B 1 142 ? -2.913  -35.293 -65.513 1.00 46.02  ? 142 ASP   B CB  1 
ATOM   4104 C CG  . ASP   B 1 142 ? -1.712  -35.274 -66.434 1.00 45.24  ? 142 ASP   B CG  1 
ATOM   4105 O OD1 . ASP   B 1 142 ? -0.715  -34.610 -66.088 1.00 49.36  ? 142 ASP   B OD1 1 
ATOM   4106 O OD2 . ASP   B 1 142 ? -1.769  -35.904 -67.509 1.00 50.85  ? 142 ASP   B OD2 1 
ATOM   4107 N N   . TRP   B 1 143 ? -2.048  -32.446 -65.200 1.00 50.03  ? 143 TRP   B N   1 
ATOM   4108 C CA  . TRP   B 1 143 ? -2.193  -31.073 -65.664 1.00 43.52  ? 143 TRP   B CA  1 
ATOM   4109 C C   . TRP   B 1 143 ? -2.799  -31.012 -67.065 1.00 45.45  ? 143 TRP   B C   1 
ATOM   4110 O O   . TRP   B 1 143 ? -2.465  -30.123 -67.856 1.00 43.64  ? 143 TRP   B O   1 
ATOM   4111 C CB  . TRP   B 1 143 ? -0.845  -30.355 -65.618 1.00 45.38  ? 143 TRP   B CB  1 
ATOM   4112 C CG  . TRP   B 1 143 ? -0.419  -30.021 -64.216 1.00 49.10  ? 143 TRP   B CG  1 
ATOM   4113 C CD1 . TRP   B 1 143 ? -1.224  -29.922 -63.125 1.00 48.02  ? 143 TRP   B CD1 1 
ATOM   4114 C CD2 . TRP   B 1 143 ? 0.915   -29.780 -63.751 1.00 50.01  ? 143 TRP   B CD2 1 
ATOM   4115 N NE1 . TRP   B 1 143 ? -0.487  -29.610 -62.011 1.00 46.15  ? 143 TRP   B NE1 1 
ATOM   4116 C CE2 . TRP   B 1 143 ? 0.833   -29.523 -62.365 1.00 49.06  ? 143 TRP   B CE2 1 
ATOM   4117 C CE3 . TRP   B 1 143 ? 2.169   -29.750 -64.369 1.00 50.08  ? 143 TRP   B CE3 1 
ATOM   4118 C CZ2 . TRP   B 1 143 ? 1.954   -29.238 -61.589 1.00 49.18  ? 143 TRP   B CZ2 1 
ATOM   4119 C CZ3 . TRP   B 1 143 ? 3.282   -29.468 -63.597 1.00 51.06  ? 143 TRP   B CZ3 1 
ATOM   4120 C CH2 . TRP   B 1 143 ? 3.167   -29.216 -62.221 1.00 50.48  ? 143 TRP   B CH2 1 
ATOM   4121 N N   . GLN   B 1 144 ? -3.671  -31.966 -67.388 1.00 43.72  ? 144 GLN   B N   1 
ATOM   4122 C CA  . GLN   B 1 144 ? -4.503  -31.929 -68.581 1.00 42.00  ? 144 GLN   B CA  1 
ATOM   4123 C C   . GLN   B 1 144 ? -5.801  -32.651 -68.261 1.00 45.15  ? 144 GLN   B C   1 
ATOM   4124 O O   . GLN   B 1 144 ? -5.842  -33.510 -67.379 1.00 45.87  ? 144 GLN   B O   1 
ATOM   4125 C CB  . GLN   B 1 144 ? -3.811  -32.564 -69.791 1.00 40.24  ? 144 GLN   B CB  1 
ATOM   4126 C CG  . GLN   B 1 144 ? -2.790  -33.620 -69.436 1.00 44.95  ? 144 GLN   B CG  1 
ATOM   4127 C CD  . GLN   B 1 144 ? -2.162  -34.264 -70.656 1.00 43.40  ? 144 GLN   B CD  1 
ATOM   4128 O OE1 . GLN   B 1 144 ? -1.990  -33.625 -71.694 1.00 45.52  ? 144 GLN   B OE1 1 
ATOM   4129 N NE2 . GLN   B 1 144 ? -1.810  -35.536 -70.534 1.00 43.08  ? 144 GLN   B NE2 1 
ATOM   4130 N N   . SER   B 1 145 ? -6.867  -32.292 -68.972 1.00 45.20  ? 145 SER   B N   1 
ATOM   4131 C CA  . SER   B 1 145 ? -8.189  -32.868 -68.745 1.00 42.90  ? 145 SER   B CA  1 
ATOM   4132 C C   . SER   B 1 145 ? -8.508  -33.845 -69.871 1.00 42.33  ? 145 SER   B C   1 
ATOM   4133 O O   . SER   B 1 145 ? -8.805  -33.433 -70.998 1.00 41.63  ? 145 SER   B O   1 
ATOM   4134 C CB  . SER   B 1 145 ? -9.249  -31.777 -68.634 1.00 40.48  ? 145 SER   B CB  1 
ATOM   4135 O OG  . SER   B 1 145 ? -9.056  -31.038 -67.444 1.00 41.88  ? 145 SER   B OG  1 
ATOM   4136 N N   . VAL   B 1 146 ? -8.456  -35.137 -69.550 1.00 41.79  ? 146 VAL   B N   1 
ATOM   4137 C CA  . VAL   B 1 146 ? -8.651  -36.213 -70.514 1.00 39.20  ? 146 VAL   B CA  1 
ATOM   4138 C C   . VAL   B 1 146 ? -8.940  -37.499 -69.748 1.00 42.07  ? 146 VAL   B C   1 
ATOM   4139 O O   . VAL   B 1 146 ? -8.283  -37.792 -68.741 1.00 40.34  ? 146 VAL   B O   1 
ATOM   4140 C CB  . VAL   B 1 146 ? -7.420  -36.361 -71.431 1.00 43.09  ? 146 VAL   B CB  1 
ATOM   4141 C CG1 . VAL   B 1 146 ? -6.133  -36.428 -70.611 1.00 44.47  ? 146 VAL   B CG1 1 
ATOM   4142 C CG2 . VAL   B 1 146 ? -7.558  -37.579 -72.328 1.00 40.28  ? 146 VAL   B CG2 1 
ATOM   4143 N N   . ASN   B 1 147 ? -9.917  -38.273 -70.207 1.00 38.32  ? 147 ASN   B N   1 
ATOM   4144 C CA  . ASN   B 1 147 ? -10.355 -39.464 -69.490 1.00 41.45  ? 147 ASN   B CA  1 
ATOM   4145 C C   . ASN   B 1 147 ? -11.219 -40.312 -70.427 1.00 38.25  ? 147 ASN   B C   1 
ATOM   4146 O O   . ASN   B 1 147 ? -11.754 -39.797 -71.414 1.00 35.71  ? 147 ASN   B O   1 
ATOM   4147 C CB  . ASN   B 1 147 ? -11.136 -39.094 -68.219 1.00 37.87  ? 147 ASN   B CB  1 
ATOM   4148 C CG  . ASN   B 1 147 ? -12.454 -38.430 -68.525 1.00 38.66  ? 147 ASN   B CG  1 
ATOM   4149 O OD1 . ASN   B 1 147 ? -13.480 -39.095 -68.665 1.00 40.98  ? 147 ASN   B OD1 1 
ATOM   4150 N ND2 . ASN   B 1 147 ? -12.436 -37.110 -68.635 1.00 38.77  ? 147 ASN   B ND2 1 
ATOM   4151 N N   . PRO   B 1 148 ? -11.368 -41.611 -70.131 1.00 40.83  ? 148 PRO   B N   1 
ATOM   4152 C CA  . PRO   B 1 148 ? -12.146 -42.478 -71.035 1.00 38.21  ? 148 PRO   B CA  1 
ATOM   4153 C C   . PRO   B 1 148 ? -13.627 -42.141 -71.115 1.00 38.26  ? 148 PRO   B C   1 
ATOM   4154 O O   . PRO   B 1 148 ? -14.234 -42.366 -72.169 1.00 41.02  ? 148 PRO   B O   1 
ATOM   4155 C CB  . PRO   B 1 148 ? -11.923 -43.883 -70.451 1.00 33.85  ? 148 PRO   B CB  1 
ATOM   4156 C CG  . PRO   B 1 148 ? -11.528 -43.649 -69.024 1.00 38.46  ? 148 PRO   B CG  1 
ATOM   4157 C CD  . PRO   B 1 148 ? -10.697 -42.395 -69.078 1.00 39.14  ? 148 PRO   B CD  1 
ATOM   4158 N N   . ASN   B 1 149 ? -14.239 -41.622 -70.045 1.00 38.34  ? 149 ASN   B N   1 
ATOM   4159 C CA  . ASN   B 1 149 ? -15.686 -41.412 -70.067 1.00 37.57  ? 149 ASN   B CA  1 
ATOM   4160 C C   . ASN   B 1 149 ? -16.093 -40.269 -70.987 1.00 39.67  ? 149 ASN   B C   1 
ATOM   4161 O O   . ASN   B 1 149 ? -17.158 -40.333 -71.614 1.00 41.00  ? 149 ASN   B O   1 
ATOM   4162 C CB  . ASN   B 1 149 ? -16.219 -41.144 -68.660 1.00 39.42  ? 149 ASN   B CB  1 
ATOM   4163 C CG  . ASN   B 1 149 ? -15.773 -42.182 -67.658 1.00 40.64  ? 149 ASN   B CG  1 
ATOM   4164 O OD1 . ASN   B 1 149 ? -15.469 -43.310 -68.020 1.00 40.24  ? 149 ASN   B OD1 1 
ATOM   4165 N ND2 . ASN   B 1 149 ? -15.750 -41.810 -66.389 1.00 36.93  ? 149 ASN   B ND2 1 
ATOM   4166 N N   . TYR   B 1 150 ? -15.277 -39.220 -71.075 1.00 39.52  ? 150 TYR   B N   1 
ATOM   4167 C CA  . TYR   B 1 150 ? -15.682 -37.983 -71.729 1.00 39.32  ? 150 TYR   B CA  1 
ATOM   4168 C C   . TYR   B 1 150 ? -14.763 -37.529 -72.851 1.00 37.93  ? 150 TYR   B C   1 
ATOM   4169 O O   . TYR   B 1 150 ? -15.176 -36.675 -73.644 1.00 38.32  ? 150 TYR   B O   1 
ATOM   4170 C CB  . TYR   B 1 150 ? -15.781 -36.848 -70.700 1.00 38.55  ? 150 TYR   B CB  1 
ATOM   4171 C CG  . TYR   B 1 150 ? -16.597 -37.188 -69.468 1.00 39.85  ? 150 TYR   B CG  1 
ATOM   4172 C CD1 . TYR   B 1 150 ? -17.907 -37.644 -69.576 1.00 38.36  ? 150 TYR   B CD1 1 
ATOM   4173 C CD2 . TYR   B 1 150 ? -16.054 -37.049 -68.195 1.00 38.59  ? 150 TYR   B CD2 1 
ATOM   4174 C CE1 . TYR   B 1 150 ? -18.650 -37.954 -68.449 1.00 37.21  ? 150 TYR   B CE1 1 
ATOM   4175 C CE2 . TYR   B 1 150 ? -16.787 -37.356 -67.067 1.00 37.03  ? 150 TYR   B CE2 1 
ATOM   4176 C CZ  . TYR   B 1 150 ? -18.083 -37.807 -67.198 1.00 39.63  ? 150 TYR   B CZ  1 
ATOM   4177 O OH  . TYR   B 1 150 ? -18.807 -38.105 -66.068 1.00 35.18  ? 150 TYR   B OH  1 
ATOM   4178 N N   . GLY   B 1 151 ? -13.548 -38.059 -72.954 1.00 33.15  ? 151 GLY   B N   1 
ATOM   4179 C CA  . GLY   B 1 151 ? -12.608 -37.572 -73.941 1.00 37.09  ? 151 GLY   B CA  1 
ATOM   4180 C C   . GLY   B 1 151 ? -11.647 -36.557 -73.361 1.00 39.39  ? 151 GLY   B C   1 
ATOM   4181 O O   . GLY   B 1 151 ? -11.372 -36.577 -72.155 1.00 41.59  ? 151 GLY   B O   1 
ATOM   4182 N N   . ARG   B 1 152 ? -11.143 -35.653 -74.200 1.00 39.28  ? 152 ARG   B N   1 
ATOM   4183 C CA  . ARG   B 1 152 ? -10.110 -34.702 -73.811 1.00 39.74  ? 152 ARG   B CA  1 
ATOM   4184 C C   . ARG   B 1 152 ? -10.584 -33.276 -74.058 1.00 40.95  ? 152 ARG   B C   1 
ATOM   4185 O O   . ARG   B 1 152 ? -11.304 -33.006 -75.026 1.00 41.87  ? 152 ARG   B O   1 
ATOM   4186 C CB  . ARG   B 1 152 ? -8.808  -34.975 -74.584 1.00 40.00  ? 152 ARG   B CB  1 
ATOM   4187 C CG  . ARG   B 1 152 ? -7.629  -34.090 -74.189 1.00 40.99  ? 152 ARG   B CG  1 
ATOM   4188 C CD  . ARG   B 1 152 ? -6.505  -34.155 -75.217 1.00 40.42  ? 152 ARG   B CD  1 
ATOM   4189 N NE  . ARG   B 1 152 ? -6.915  -33.660 -76.525 1.00 38.16  ? 152 ARG   B NE  1 
ATOM   4190 C CZ  . ARG   B 1 152 ? -6.398  -34.068 -77.677 1.00 37.33  ? 152 ARG   B CZ  1 
ATOM   4191 N NH1 . ARG   B 1 152 ? -5.460  -35.000 -77.722 1.00 35.69  ? 152 ARG   B NH1 1 
ATOM   4192 N NH2 . ARG   B 1 152 ? -6.829  -33.523 -78.811 1.00 34.53  ? 152 ARG   B NH2 1 
ATOM   4193 N N   . THR   B 1 153 ? -10.177 -32.366 -73.177 1.00 42.88  ? 153 THR   B N   1 
ATOM   4194 C CA  . THR   B 1 153 ? -10.484 -30.950 -73.319 1.00 41.84  ? 153 THR   B CA  1 
ATOM   4195 C C   . THR   B 1 153 ? -9.300  -30.247 -73.965 1.00 42.07  ? 153 THR   B C   1 
ATOM   4196 O O   . THR   B 1 153 ? -8.166  -30.354 -73.484 1.00 42.08  ? 153 THR   B O   1 
ATOM   4197 C CB  . THR   B 1 153 ? -10.808 -30.311 -71.965 1.00 40.00  ? 153 THR   B CB  1 
ATOM   4198 O OG1 . THR   B 1 153 ? -11.950 -30.964 -71.403 1.00 43.13  ? 153 THR   B OG1 1 
ATOM   4199 C CG2 . THR   B 1 153 ? -11.140 -28.829 -72.136 1.00 38.25  ? 153 THR   B CG2 1 
ATOM   4200 N N   . ASN   B 1 154 ? -9.565  -29.538 -75.052 1.00 40.19  ? 154 ASN   B N   1 
ATOM   4201 C CA  . ASN   B 1 154 ? -8.535  -28.837 -75.798 1.00 41.58  ? 154 ASN   B CA  1 
ATOM   4202 C C   . ASN   B 1 154 ? -8.530  -27.370 -75.395 1.00 43.03  ? 154 ASN   B C   1 
ATOM   4203 O O   . ASN   B 1 154 ? -9.589  -26.780 -75.158 1.00 40.69  ? 154 ASN   B O   1 
ATOM   4204 C CB  . ASN   B 1 154 ? -8.781  -28.978 -77.299 1.00 41.88  ? 154 ASN   B CB  1 
ATOM   4205 C CG  . ASN   B 1 154 ? -9.129  -30.401 -77.694 1.00 42.61  ? 154 ASN   B CG  1 
ATOM   4206 O OD1 . ASN   B 1 154 ? -8.295  -31.306 -77.608 1.00 42.72  ? 154 ASN   B OD1 1 
ATOM   4207 N ND2 . ASN   B 1 154 ? -10.374 -30.611 -78.111 1.00 38.45  ? 154 ASN   B ND2 1 
ATOM   4208 N N   . ASN   B 1 155 ? -7.337  -26.797 -75.294 1.00 41.85  ? 155 ASN   B N   1 
ATOM   4209 C CA  . ASN   B 1 155 ? -7.216  -25.394 -74.930 1.00 41.69  ? 155 ASN   B CA  1 
ATOM   4210 C C   . ASN   B 1 155 ? -7.942  -24.524 -75.951 1.00 43.50  ? 155 ASN   B C   1 
ATOM   4211 O O   . ASN   B 1 155 ? -7.727  -24.688 -77.159 1.00 45.15  ? 155 ASN   B O   1 
ATOM   4212 C CB  . ASN   B 1 155 ? -5.750  -24.983 -74.856 1.00 44.75  ? 155 ASN   B CB  1 
ATOM   4213 C CG  . ASN   B 1 155 ? -5.553  -23.683 -74.113 1.00 40.77  ? 155 ASN   B CG  1 
ATOM   4214 O OD1 . ASN   B 1 155 ? -5.961  -22.622 -74.580 1.00 44.48  ? 155 ASN   B OD1 1 
ATOM   4215 N ND2 . ASN   B 1 155 ? -4.910  -23.756 -72.958 1.00 39.25  ? 155 ASN   B ND2 1 
ATOM   4216 N N   . PRO   B 1 156 ? -8.795  -23.594 -75.514 1.00 42.45  ? 156 PRO   B N   1 
ATOM   4217 C CA  . PRO   B 1 156 ? -9.501  -22.737 -76.482 1.00 41.47  ? 156 PRO   B CA  1 
ATOM   4218 C C   . PRO   B 1 156 ? -8.587  -21.811 -77.269 1.00 43.94  ? 156 PRO   B C   1 
ATOM   4219 O O   . PRO   B 1 156 ? -8.932  -21.440 -78.398 1.00 44.02  ? 156 PRO   B O   1 
ATOM   4220 C CB  . PRO   B 1 156 ? -10.471 -21.945 -75.594 1.00 40.11  ? 156 PRO   B CB  1 
ATOM   4221 C CG  . PRO   B 1 156 ? -10.666 -22.818 -74.394 1.00 41.88  ? 156 PRO   B CG  1 
ATOM   4222 C CD  . PRO   B 1 156 ? -9.312  -23.414 -74.149 1.00 39.54  ? 156 PRO   B CD  1 
ATOM   4223 N N   . HIS   B 1 157 ? -7.440  -21.412 -76.712 1.00 43.44  ? 157 HIS   B N   1 
ATOM   4224 C CA  . HIS   B 1 157 ? -6.529  -20.529 -77.434 1.00 47.89  ? 157 HIS   B CA  1 
ATOM   4225 C C   . HIS   B 1 157 ? -5.685  -21.273 -78.457 1.00 46.89  ? 157 HIS   B C   1 
ATOM   4226 O O   . HIS   B 1 157 ? -5.239  -20.665 -79.435 1.00 47.18  ? 157 HIS   B O   1 
ATOM   4227 C CB  . HIS   B 1 157 ? -5.617  -19.786 -76.457 1.00 44.53  ? 157 HIS   B CB  1 
ATOM   4228 C CG  . HIS   B 1 157 ? -6.356  -19.104 -75.349 1.00 45.13  ? 157 HIS   B CG  1 
ATOM   4229 N ND1 . HIS   B 1 157 ? -6.774  -17.793 -75.429 1.00 45.44  ? 157 HIS   B ND1 1 
ATOM   4230 C CD2 . HIS   B 1 157 ? -6.757  -19.553 -74.136 1.00 47.88  ? 157 HIS   B CD2 1 
ATOM   4231 C CE1 . HIS   B 1 157 ? -7.404  -17.465 -74.315 1.00 47.43  ? 157 HIS   B CE1 1 
ATOM   4232 N NE2 . HIS   B 1 157 ? -7.406  -18.515 -73.513 1.00 47.80  ? 157 HIS   B NE2 1 
ATOM   4233 N N   . ASP   B 1 158 ? -5.459  -22.568 -78.249 1.00 48.11  ? 158 ASP   B N   1 
ATOM   4234 C CA  . ASP   B 1 158 ? -4.729  -23.394 -79.205 1.00 44.16  ? 158 ASP   B CA  1 
ATOM   4235 C C   . ASP   B 1 158 ? -5.175  -24.829 -78.962 1.00 45.92  ? 158 ASP   B C   1 
ATOM   4236 O O   . ASP   B 1 158 ? -4.801  -25.426 -77.948 1.00 46.78  ? 158 ASP   B O   1 
ATOM   4237 C CB  . ASP   B 1 158 ? -3.223  -23.232 -79.027 1.00 43.70  ? 158 ASP   B CB  1 
ATOM   4238 C CG  . ASP   B 1 158 ? -2.414  -23.946 -80.107 1.00 46.85  ? 158 ASP   B CG  1 
ATOM   4239 O OD1 . ASP   B 1 158 ? -2.965  -24.809 -80.820 1.00 46.26  ? 158 ASP   B OD1 1 
ATOM   4240 O OD2 . ASP   B 1 158 ? -1.207  -23.644 -80.235 1.00 52.75  ? 158 ASP   B OD2 1 
ATOM   4241 N N   . HIS   B 1 159 ? -5.967  -25.374 -79.888 1.00 44.38  ? 159 HIS   B N   1 
ATOM   4242 C CA  . HIS   B 1 159 ? -6.578  -26.682 -79.673 1.00 43.04  ? 159 HIS   B CA  1 
ATOM   4243 C C   . HIS   B 1 159 ? -5.550  -27.804 -79.590 1.00 44.17  ? 159 HIS   B C   1 
ATOM   4244 O O   . HIS   B 1 159 ? -5.879  -28.889 -79.101 1.00 44.75  ? 159 HIS   B O   1 
ATOM   4245 C CB  . HIS   B 1 159 ? -7.586  -26.970 -80.786 1.00 45.29  ? 159 HIS   B CB  1 
ATOM   4246 C CG  . HIS   B 1 159 ? -8.696  -25.969 -80.864 1.00 45.95  ? 159 HIS   B CG  1 
ATOM   4247 N ND1 . HIS   B 1 159 ? -9.313  -25.629 -82.049 1.00 48.90  ? 159 HIS   B ND1 1 
ATOM   4248 C CD2 . HIS   B 1 159 ? -9.291  -25.226 -79.902 1.00 45.43  ? 159 HIS   B CD2 1 
ATOM   4249 C CE1 . HIS   B 1 159 ? -10.243 -24.720 -81.812 1.00 48.28  ? 159 HIS   B CE1 1 
ATOM   4250 N NE2 . HIS   B 1 159 ? -10.250 -24.459 -80.517 1.00 48.76  ? 159 HIS   B NE2 1 
ATOM   4251 N N   . SER   B 1 160 ? -4.317  -27.570 -80.043 1.00 43.95  ? 160 SER   B N   1 
ATOM   4252 C CA  . SER   B 1 160 ? -3.267  -28.575 -79.943 1.00 42.96  ? 160 SER   B CA  1 
ATOM   4253 C C   . SER   B 1 160 ? -2.632  -28.634 -78.562 1.00 42.74  ? 160 SER   B C   1 
ATOM   4254 O O   . SER   B 1 160 ? -1.812  -29.525 -78.315 1.00 43.30  ? 160 SER   B O   1 
ATOM   4255 C CB  . SER   B 1 160 ? -2.185  -28.308 -80.994 1.00 41.91  ? 160 SER   B CB  1 
ATOM   4256 O OG  . SER   B 1 160 ? -1.389  -27.185 -80.647 1.00 46.31  ? 160 SER   B OG  1 
ATOM   4257 N N   . ARG   B 1 161 ? -2.990  -27.722 -77.664 1.00 42.99  ? 161 ARG   B N   1 
ATOM   4258 C CA  . ARG   B 1 161 ? -2.370  -27.618 -76.352 1.00 45.47  ? 161 ARG   B CA  1 
ATOM   4259 C C   . ARG   B 1 161 ? -3.346  -28.034 -75.259 1.00 42.60  ? 161 ARG   B C   1 
ATOM   4260 O O   . ARG   B 1 161 ? -4.563  -27.876 -75.393 1.00 42.03  ? 161 ARG   B O   1 
ATOM   4261 C CB  . ARG   B 1 161 ? -1.888  -26.190 -76.084 1.00 45.89  ? 161 ARG   B CB  1 
ATOM   4262 C CG  . ARG   B 1 161 ? -1.243  -25.517 -77.279 1.00 47.32  ? 161 ARG   B CG  1 
ATOM   4263 C CD  . ARG   B 1 161 ? -0.014  -26.257 -77.761 1.00 44.79  ? 161 ARG   B CD  1 
ATOM   4264 N NE  . ARG   B 1 161 ? 1.158   -25.916 -76.963 1.00 50.86  ? 161 ARG   B NE  1 
ATOM   4265 C CZ  . ARG   B 1 161 ? 2.361   -26.445 -77.135 1.00 52.86  ? 161 ARG   B CZ  1 
ATOM   4266 N NH1 . ARG   B 1 161 ? 2.600   -27.322 -78.097 1.00 54.11  ? 161 ARG   B NH1 1 
ATOM   4267 N NH2 . ARG   B 1 161 ? 3.352   -26.085 -76.323 1.00 53.83  ? 161 ARG   B NH2 1 
ATOM   4268 N N   . SER   B 1 162 ? -2.796  -28.547 -74.162 1.00 45.42  ? 162 SER   B N   1 
ATOM   4269 C CA  . SER   B 1 162 ? -3.623  -28.991 -73.049 1.00 42.41  ? 162 SER   B CA  1 
ATOM   4270 C C   . SER   B 1 162 ? -4.387  -27.820 -72.438 1.00 42.46  ? 162 SER   B C   1 
ATOM   4271 O O   . SER   B 1 162 ? -3.969  -26.661 -72.517 1.00 40.25  ? 162 SER   B O   1 
ATOM   4272 C CB  . SER   B 1 162 ? -2.762  -29.663 -71.980 1.00 45.51  ? 162 SER   B CB  1 
ATOM   4273 O OG  . SER   B 1 162 ? -3.305  -29.457 -70.685 1.00 43.94  ? 162 SER   B OG  1 
ATOM   4274 N N   . ALA   B 1 163 ? -5.506  -28.121 -71.776 1.00 41.64  ? 163 ALA   B N   1 
ATOM   4275 C CA  . ALA   B 1 163 ? -6.366  -27.041 -71.230 1.00 42.54  ? 163 ALA   B CA  1 
ATOM   4276 C C   . ALA   B 1 163 ? -6.168  -26.849 -69.724 1.00 39.22  ? 163 ALA   B C   1 
ATOM   4277 O O   . ALA   B 1 163 ? -7.026  -26.197 -69.101 1.00 39.96  ? 163 ALA   B O   1 
ATOM   4278 C CB  . ALA   B 1 163 ? -7.808  -27.360 -71.541 1.00 41.02  ? 163 ALA   B CB  1 
ATOM   4279 N N   . GLY   B 1 164 ? -5.053  -27.316 -69.164 1.00 40.20  ? 164 GLY   B N   1 
ATOM   4280 C CA  . GLY   B 1 164 ? -4.857  -27.249 -67.702 1.00 42.68  ? 164 GLY   B CA  1 
ATOM   4281 C C   . GLY   B 1 164 ? -5.279  -28.540 -67.041 1.00 42.60  ? 164 GLY   B C   1 
ATOM   4282 O O   . GLY   B 1 164 ? -6.051  -29.296 -67.662 1.00 36.88  ? 164 GLY   B O   1 
ATOM   4283 N N   . GLY   B 1 165 ? -4.829  -28.777 -65.806 1.00 41.54  ? 165 GLY   B N   1 
ATOM   4284 C CA  . GLY   B 1 165 ? -5.108  -30.103 -65.242 1.00 46.89  ? 165 GLY   B CA  1 
ATOM   4285 C C   . GLY   B 1 165 ? -6.073  -30.203 -64.098 1.00 51.11  ? 165 GLY   B C   1 
ATOM   4286 O O   . GLY   B 1 165 ? -5.814  -29.550 -63.074 1.00 51.71  ? 165 GLY   B O   1 
ATOM   4287 N N   . SER   B 1 166 ? -7.171  -30.922 -64.308 1.00 51.47  ? 166 SER   B N   1 
ATOM   4288 C CA  . SER   B 1 166 ? -8.185  -31.295 -63.290 1.00 48.08  ? 166 SER   B CA  1 
ATOM   4289 C C   . SER   B 1 166 ? -9.245  -30.199 -63.212 1.00 42.90  ? 166 SER   B C   1 
ATOM   4290 O O   . SER   B 1 166 ? -10.382 -30.544 -62.962 1.00 45.92  ? 166 SER   B O   1 
ATOM   4291 C CB  . SER   B 1 166 ? -7.578  -31.659 -61.955 1.00 47.22  ? 166 SER   B CB  1 
ATOM   4292 O OG  . SER   B 1 166 ? -8.572  -31.955 -60.988 1.00 50.42  ? 166 SER   B OG  1 
ATOM   4293 N N   . SER   B 1 167 ? -8.940  -28.996 -63.674 1.00 36.98  ? 167 SER   B N   1 
ATOM   4294 C CA  . SER   B 1 167 ? -9.983  -27.946 -63.775 1.00 40.41  ? 167 SER   B CA  1 
ATOM   4295 C C   . SER   B 1 167 ? -9.981  -27.467 -65.225 1.00 41.63  ? 167 SER   B C   1 
ATOM   4296 O O   . SER   B 1 167 ? -10.467 -26.350 -65.474 1.00 41.09  ? 167 SER   B O   1 
ATOM   4297 C CB  . SER   B 1 167 ? -9.805  -26.840 -62.784 1.00 40.69  ? 167 SER   B CB  1 
ATOM   4298 O OG  . SER   B 1 167 ? -9.893  -27.333 -61.454 1.00 37.28  ? 167 SER   B OG  1 
ATOM   4299 N N   . GLY   B 1 168 ? -9.391  -28.258 -66.123 1.00 40.78  ? 168 GLY   B N   1 
ATOM   4300 C CA  . GLY   B 1 168 ? -9.238  -27.786 -67.510 1.00 38.59  ? 168 GLY   B CA  1 
ATOM   4301 C C   . GLY   B 1 168 ? -10.589 -27.544 -68.125 1.00 40.58  ? 168 GLY   B C   1 
ATOM   4302 O O   . GLY   B 1 168 ? -10.742 -26.517 -68.805 1.00 39.96  ? 168 GLY   B O   1 
ATOM   4303 N N   . GLY   B 1 169 ? -11.545 -28.429 -67.864 1.00 37.63  ? 169 GLY   B N   1 
ATOM   4304 C CA  . GLY   B 1 169 ? -12.905 -28.158 -68.345 1.00 39.33  ? 169 GLY   B CA  1 
ATOM   4305 C C   . GLY   B 1 169 ? -13.372 -26.826 -67.800 1.00 40.99  ? 169 GLY   B C   1 
ATOM   4306 O O   . GLY   B 1 169 ? -13.905 -26.026 -68.587 1.00 38.23  ? 169 GLY   B O   1 
ATOM   4307 N N   . ALA   B 1 170 ? -13.166 -26.587 -66.500 1.00 39.98  ? 170 ALA   B N   1 
ATOM   4308 C CA  . ALA   B 1 170 ? -13.670 -25.353 -65.907 1.00 40.00  ? 170 ALA   B CA  1 
ATOM   4309 C C   . ALA   B 1 170 ? -13.006 -24.133 -66.532 1.00 38.56  ? 170 ALA   B C   1 
ATOM   4310 O O   . ALA   B 1 170 ? -13.679 -23.170 -66.916 1.00 40.80  ? 170 ALA   B O   1 
ATOM   4311 C CB  . ALA   B 1 170 ? -13.436 -25.371 -64.397 1.00 38.85  ? 170 ALA   B CB  1 
ATOM   4312 N N   . ALA   B 1 171 ? -11.677 -24.156 -66.631 1.00 37.76  ? 171 ALA   B N   1 
ATOM   4313 C CA  . ALA   B 1 171 ? -10.953 -23.022 -67.191 1.00 37.75  ? 171 ALA   B CA  1 
ATOM   4314 C C   . ALA   B 1 171 ? -11.314 -22.802 -68.655 1.00 40.39  ? 171 ALA   B C   1 
ATOM   4315 O O   . ALA   B 1 171 ? -11.519 -21.662 -69.088 1.00 41.71  ? 171 ALA   B O   1 
ATOM   4316 C CB  . ALA   B 1 171 ? -9.448  -23.239 -67.032 1.00 37.90  ? 171 ALA   B CB  1 
ATOM   4317 N N   . ALA   B 1 172 ? -11.400 -23.886 -69.433 1.00 38.75  ? 172 ALA   B N   1 
ATOM   4318 C CA  . ALA   B 1 172 ? -11.701 -23.760 -70.856 1.00 39.98  ? 172 ALA   B CA  1 
ATOM   4319 C C   . ALA   B 1 172 ? -13.114 -23.241 -71.080 1.00 41.93  ? 172 ALA   B C   1 
ATOM   4320 O O   . ALA   B 1 172 ? -13.354 -22.455 -72.005 1.00 39.55  ? 172 ALA   B O   1 
ATOM   4321 C CB  . ALA   B 1 172 ? -11.505 -25.106 -71.554 1.00 39.70  ? 172 ALA   B CB  1 
ATOM   4322 N N   . ALA   B 1 173 ? -14.062 -23.667 -70.242 1.00 41.48  ? 173 ALA   B N   1 
ATOM   4323 C CA  . ALA   B 1 173 ? -15.435 -23.199 -70.378 1.00 40.61  ? 173 ALA   B CA  1 
ATOM   4324 C C   . ALA   B 1 173 ? -15.550 -21.708 -70.089 1.00 43.47  ? 173 ALA   B C   1 
ATOM   4325 O O   . ALA   B 1 173 ? -16.369 -21.020 -70.708 1.00 41.74  ? 173 ALA   B O   1 
ATOM   4326 C CB  . ALA   B 1 173 ? -16.354 -23.999 -69.457 1.00 38.48  ? 173 ALA   B CB  1 
ATOM   4327 N N   . LEU   B 1 174 ? -14.741 -21.193 -69.161 1.00 40.04  ? 174 LEU   B N   1 
ATOM   4328 C CA  . LEU   B 1 174 ? -14.710 -19.753 -68.929 1.00 41.64  ? 174 LEU   B CA  1 
ATOM   4329 C C   . LEU   B 1 174 ? -13.949 -19.035 -70.034 1.00 39.49  ? 174 LEU   B C   1 
ATOM   4330 O O   . LEU   B 1 174 ? -14.367 -17.963 -70.483 1.00 40.97  ? 174 LEU   B O   1 
ATOM   4331 C CB  . LEU   B 1 174 ? -14.079 -19.438 -67.571 1.00 37.16  ? 174 LEU   B CB  1 
ATOM   4332 C CG  . LEU   B 1 174 ? -14.713 -20.017 -66.307 1.00 39.81  ? 174 LEU   B CG  1 
ATOM   4333 C CD1 . LEU   B 1 174 ? -13.694 -20.070 -65.178 1.00 34.66  ? 174 LEU   B CD1 1 
ATOM   4334 C CD2 . LEU   B 1 174 ? -15.922 -19.201 -65.889 1.00 40.91  ? 174 LEU   B CD2 1 
ATOM   4335 N N   . ALA   B 1 175 ? -12.832 -19.616 -70.481 1.00 40.88  ? 175 ALA   B N   1 
ATOM   4336 C CA  . ALA   B 1 175 ? -12.044 -19.003 -71.545 1.00 40.43  ? 175 ALA   B CA  1 
ATOM   4337 C C   . ALA   B 1 175 ? -12.830 -18.900 -72.845 1.00 43.03  ? 175 ALA   B C   1 
ATOM   4338 O O   . ALA   B 1 175 ? -12.638 -17.948 -73.611 1.00 43.34  ? 175 ALA   B O   1 
ATOM   4339 C CB  . ALA   B 1 175 ? -10.754 -19.793 -71.759 1.00 38.28  ? 175 ALA   B CB  1 
ATOM   4340 N N   . ALA   B 1 176 ? -13.717 -19.858 -73.109 1.00 43.16  ? 176 ALA   B N   1 
ATOM   4341 C CA  . ALA   B 1 176 ? -14.572 -19.827 -74.287 1.00 41.97  ? 176 ALA   B CA  1 
ATOM   4342 C C   . ALA   B 1 176 ? -15.833 -18.997 -74.081 1.00 44.21  ? 176 ALA   B C   1 
ATOM   4343 O O   . ALA   B 1 176 ? -16.605 -18.829 -75.029 1.00 44.69  ? 176 ALA   B O   1 
ATOM   4344 C CB  . ALA   B 1 176 ? -14.954 -21.251 -74.702 1.00 39.00  ? 176 ALA   B CB  1 
ATOM   4345 N N   . GLY   B 1 177 ? -16.065 -18.482 -72.875 1.00 40.40  ? 177 GLY   B N   1 
ATOM   4346 C CA  . GLY   B 1 177 ? -17.212 -17.626 -72.652 1.00 40.03  ? 177 GLY   B CA  1 
ATOM   4347 C C   . GLY   B 1 177 ? -18.527 -18.353 -72.512 1.00 44.00  ? 177 GLY   B C   1 
ATOM   4348 O O   . GLY   B 1 177 ? -19.587 -17.730 -72.636 1.00 43.37  ? 177 GLY   B O   1 
ATOM   4349 N N   . MET   B 1 178 ? -18.489 -19.663 -72.255 1.00 43.71  ? 178 MET   B N   1 
ATOM   4350 C CA  . MET   B 1 178 ? -19.722 -20.433 -72.121 1.00 42.08  ? 178 MET   B CA  1 
ATOM   4351 C C   . MET   B 1 178 ? -20.448 -20.098 -70.827 1.00 41.26  ? 178 MET   B C   1 
ATOM   4352 O O   . MET   B 1 178 ? -21.644 -19.784 -70.839 1.00 44.02  ? 178 MET   B O   1 
ATOM   4353 C CB  . MET   B 1 178 ? -19.420 -21.929 -72.195 1.00 45.48  ? 178 MET   B CB  1 
ATOM   4354 C CG  . MET   B 1 178 ? -18.705 -22.353 -73.458 1.00 45.33  ? 178 MET   B CG  1 
ATOM   4355 S SD  . MET   B 1 178 ? -18.502 -24.140 -73.516 1.00 42.94  ? 178 MET   B SD  1 
ATOM   4356 C CE  . MET   B 1 178 ? -16.721 -24.302 -73.593 1.00 47.25  ? 178 MET   B CE  1 
ATOM   4357 N N   . VAL   B 1 179 ? -19.745 -20.157 -69.701 1.00 41.03  ? 179 VAL   B N   1 
ATOM   4358 C CA  . VAL   B 1 179 ? -20.348 -19.857 -68.404 1.00 42.51  ? 179 VAL   B CA  1 
ATOM   4359 C C   . VAL   B 1 179 ? -19.551 -18.751 -67.722 1.00 41.49  ? 179 VAL   B C   1 
ATOM   4360 O O   . VAL   B 1 179 ? -18.339 -18.636 -67.947 1.00 40.48  ? 179 VAL   B O   1 
ATOM   4361 C CB  . VAL   B 1 179 ? -20.417 -21.109 -67.516 1.00 41.30  ? 179 VAL   B CB  1 
ATOM   4362 C CG1 . VAL   B 1 179 ? -21.619 -21.953 -67.891 1.00 43.42  ? 179 VAL   B CG1 1 
ATOM   4363 C CG2 . VAL   B 1 179 ? -19.128 -21.915 -67.622 1.00 41.70  ? 179 VAL   B CG2 1 
ATOM   4364 N N   . PRO   B 1 180 ? -20.185 -17.916 -66.890 1.00 42.46  ? 180 PRO   B N   1 
ATOM   4365 C CA  . PRO   B 1 180 ? -19.434 -16.858 -66.198 1.00 42.10  ? 180 PRO   B CA  1 
ATOM   4366 C C   . PRO   B 1 180 ? -18.685 -17.331 -64.966 1.00 43.40  ? 180 PRO   B C   1 
ATOM   4367 O O   . PRO   B 1 180 ? -17.735 -16.654 -64.548 1.00 42.83  ? 180 PRO   B O   1 
ATOM   4368 C CB  . PRO   B 1 180 ? -20.526 -15.859 -65.799 1.00 38.68  ? 180 PRO   B CB  1 
ATOM   4369 C CG  . PRO   B 1 180 ? -21.733 -16.706 -65.637 1.00 41.69  ? 180 PRO   B CG  1 
ATOM   4370 C CD  . PRO   B 1 180 ? -21.636 -17.786 -66.678 1.00 42.99  ? 180 PRO   B CD  1 
ATOM   4371 N N   . LEU   B 1 181 ? -19.075 -18.452 -64.365 1.00 40.24  ? 181 LEU   B N   1 
ATOM   4372 C CA  . LEU   B 1 181 ? -18.529 -18.850 -63.075 1.00 41.16  ? 181 LEU   B CA  1 
ATOM   4373 C C   . LEU   B 1 181 ? -18.304 -20.355 -63.037 1.00 43.18  ? 181 LEU   B C   1 
ATOM   4374 O O   . LEU   B 1 181 ? -19.060 -21.122 -63.639 1.00 45.67  ? 181 LEU   B O   1 
ATOM   4375 C CB  . LEU   B 1 181 ? -19.464 -18.416 -61.933 1.00 37.62  ? 181 LEU   B CB  1 
ATOM   4376 C CG  . LEU   B 1 181 ? -19.016 -18.628 -60.486 1.00 39.16  ? 181 LEU   B CG  1 
ATOM   4377 C CD1 . LEU   B 1 181 ? -17.856 -17.709 -60.142 1.00 38.82  ? 181 LEU   B CD1 1 
ATOM   4378 C CD2 . LEU   B 1 181 ? -20.188 -18.375 -59.550 1.00 37.98  ? 181 LEU   B CD2 1 
ATOM   4379 N N   . GLU   B 1 182 ? -17.254 -20.769 -62.331 1.00 39.97  ? 182 GLU   B N   1 
ATOM   4380 C CA  . GLU   B 1 182 ? -16.960 -22.182 -62.147 1.00 40.58  ? 182 GLU   B CA  1 
ATOM   4381 C C   . GLU   B 1 182 ? -16.372 -22.383 -60.754 1.00 41.80  ? 182 GLU   B C   1 
ATOM   4382 O O   . GLU   B 1 182 ? -16.282 -21.450 -59.951 1.00 40.14  ? 182 GLU   B O   1 
ATOM   4383 C CB  . GLU   B 1 182 ? -16.017 -22.702 -63.239 1.00 41.53  ? 182 GLU   B CB  1 
ATOM   4384 C CG  . GLU   B 1 182 ? -16.699 -23.599 -64.263 1.00 44.77  ? 182 GLU   B CG  1 
ATOM   4385 C CD  . GLU   B 1 182 ? -16.693 -25.065 -63.855 1.00 46.96  ? 182 GLU   B CD  1 
ATOM   4386 O OE1 . GLU   B 1 182 ? -16.382 -25.358 -62.679 1.00 47.48  ? 182 GLU   B OE1 1 
ATOM   4387 O OE2 . GLU   B 1 182 ? -17.002 -25.924 -64.710 1.00 45.09  ? 182 GLU   B OE2 1 
ATOM   4388 N N   . TYR   B 1 183 ? -15.973 -23.618 -60.469 1.00 39.69  ? 183 TYR   B N   1 
ATOM   4389 C CA  . TYR   B 1 183 ? -15.411 -23.950 -59.167 1.00 39.37  ? 183 TYR   B CA  1 
ATOM   4390 C C   . TYR   B 1 183 ? -14.546 -25.189 -59.321 1.00 41.24  ? 183 TYR   B C   1 
ATOM   4391 O O   . TYR   B 1 183 ? -14.988 -26.180 -59.909 1.00 39.00  ? 183 TYR   B O   1 
ATOM   4392 C CB  . TYR   B 1 183 ? -16.520 -24.195 -58.140 1.00 38.17  ? 183 TYR   B CB  1 
ATOM   4393 C CG  . TYR   B 1 183 ? -16.256 -23.620 -56.771 1.00 39.60  ? 183 TYR   B CG  1 
ATOM   4394 C CD1 . TYR   B 1 183 ? -15.488 -24.315 -55.848 1.00 36.85  ? 183 TYR   B CD1 1 
ATOM   4395 C CD2 . TYR   B 1 183 ? -16.795 -22.396 -56.390 1.00 35.40  ? 183 TYR   B CD2 1 
ATOM   4396 C CE1 . TYR   B 1 183 ? -15.246 -23.803 -54.593 1.00 37.46  ? 183 TYR   B CE1 1 
ATOM   4397 C CE2 . TYR   B 1 183 ? -16.561 -21.876 -55.130 1.00 35.73  ? 183 TYR   B CE2 1 
ATOM   4398 C CZ  . TYR   B 1 183 ? -15.785 -22.584 -54.238 1.00 37.02  ? 183 TYR   B CZ  1 
ATOM   4399 O OH  . TYR   B 1 183 ? -15.546 -22.076 -52.982 1.00 40.58  ? 183 TYR   B OH  1 
ATOM   4400 N N   . GLY   B 1 184 ? -13.327 -25.135 -58.796 1.00 38.59  ? 184 GLY   B N   1 
ATOM   4401 C CA  . GLY   B 1 184 ? -12.429 -26.263 -58.932 1.00 37.66  ? 184 GLY   B CA  1 
ATOM   4402 C C   . GLY   B 1 184 ? -11.861 -26.757 -57.621 1.00 41.39  ? 184 GLY   B C   1 
ATOM   4403 O O   . GLY   B 1 184 ? -12.270 -26.311 -56.543 1.00 40.77  ? 184 GLY   B O   1 
ATOM   4404 N N   . SER   B 1 185 ? -10.919 -27.693 -57.707 1.00 39.31  ? 185 SER   B N   1 
ATOM   4405 C CA  . SER   B 1 185 ? -10.193 -28.188 -56.549 1.00 40.90  ? 185 SER   B CA  1 
ATOM   4406 C C   . SER   B 1 185 ? -8.714  -28.237 -56.905 1.00 42.53  ? 185 SER   B C   1 
ATOM   4407 O O   . SER   B 1 185 ? -8.341  -28.208 -58.079 1.00 40.50  ? 185 SER   B O   1 
ATOM   4408 C CB  . SER   B 1 185 ? -10.710 -29.562 -56.101 1.00 42.57  ? 185 SER   B CB  1 
ATOM   4409 O OG  . SER   B 1 185 ? -10.259 -30.588 -56.968 1.00 42.61  ? 185 SER   B OG  1 
ATOM   4410 N N   . ASP   B 1 186 ? -7.871  -28.315 -55.879 1.00 43.11  ? 186 ASP   B N   1 
ATOM   4411 C CA  . ASP   B 1 186 ? -6.441  -28.075 -56.063 1.00 42.82  ? 186 ASP   B CA  1 
ATOM   4412 C C   . ASP   B 1 186 ? -5.677  -28.790 -54.960 1.00 44.22  ? 186 ASP   B C   1 
ATOM   4413 O O   . ASP   B 1 186 ? -5.868  -28.485 -53.779 1.00 46.77  ? 186 ASP   B O   1 
ATOM   4414 C CB  . ASP   B 1 186 ? -6.162  -26.561 -56.043 1.00 42.02  ? 186 ASP   B CB  1 
ATOM   4415 C CG  . ASP   B 1 186 ? -4.725  -26.206 -56.398 1.00 42.61  ? 186 ASP   B CG  1 
ATOM   4416 O OD1 . ASP   B 1 186 ? -3.783  -26.867 -55.905 1.00 44.36  ? 186 ASP   B OD1 1 
ATOM   4417 O OD2 . ASP   B 1 186 ? -4.538  -25.236 -57.165 1.00 37.78  ? 186 ASP   B OD2 1 
ATOM   4418 N N   . ILE   B 1 187 ? -4.820  -29.736 -55.337 1.00 43.94  ? 187 ILE   B N   1 
ATOM   4419 C CA  . ILE   B 1 187 ? -3.898  -30.353 -54.389 1.00 46.50  ? 187 ILE   B CA  1 
ATOM   4420 C C   . ILE   B 1 187 ? -2.482  -30.190 -54.922 1.00 47.90  ? 187 ILE   B C   1 
ATOM   4421 O O   . ILE   B 1 187 ? -1.510  -30.214 -54.159 1.00 46.54  ? 187 ILE   B O   1 
ATOM   4422 C CB  . ILE   B 1 187 ? -4.237  -31.834 -54.132 1.00 44.94  ? 187 ILE   B CB  1 
ATOM   4423 C CG1 . ILE   B 1 187 ? -3.863  -32.220 -52.701 1.00 46.48  ? 187 ILE   B CG1 1 
ATOM   4424 C CG2 . ILE   B 1 187 ? -3.516  -32.742 -55.111 1.00 45.83  ? 187 ILE   B CG2 1 
ATOM   4425 C CD1 . ILE   B 1 187 ? -4.241  -33.636 -52.332 1.00 46.88  ? 187 ILE   B CD1 1 
ATOM   4426 N N   . GLY   B 1 188 ? -2.360  -30.014 -56.236 1.00 47.87  ? 188 GLY   B N   1 
ATOM   4427 C CA  . GLY   B 1 188 ? -1.074  -29.823 -56.873 1.00 45.05  ? 188 GLY   B CA  1 
ATOM   4428 C C   . GLY   B 1 188 ? -1.165  -28.830 -58.010 1.00 46.42  ? 188 GLY   B C   1 
ATOM   4429 O O   . GLY   B 1 188 ? -0.573  -29.035 -59.076 1.00 50.12  ? 188 GLY   B O   1 
ATOM   4430 N N   . GLY   B 1 189 ? -1.927  -27.764 -57.798 1.00 43.79  ? 189 GLY   B N   1 
ATOM   4431 C CA  . GLY   B 1 189 ? -2.047  -26.695 -58.761 1.00 44.10  ? 189 GLY   B CA  1 
ATOM   4432 C C   . GLY   B 1 189 ? -3.273  -26.727 -59.646 1.00 43.62  ? 189 GLY   B C   1 
ATOM   4433 O O   . GLY   B 1 189 ? -3.281  -26.044 -60.674 1.00 43.83  ? 189 GLY   B O   1 
ATOM   4434 N N   . SER   B 1 190 ? -4.317  -27.464 -59.273 1.00 44.29  ? 190 SER   B N   1 
ATOM   4435 C CA  . SER   B 1 190 ? -5.389  -27.740 -60.221 1.00 43.04  ? 190 SER   B CA  1 
ATOM   4436 C C   . SER   B 1 190 ? -6.441  -26.649 -60.333 1.00 41.59  ? 190 SER   B C   1 
ATOM   4437 O O   . SER   B 1 190 ? -7.299  -26.751 -61.211 1.00 43.28  ? 190 SER   B O   1 
ATOM   4438 C CB  . SER   B 1 190 ? -6.072  -29.050 -59.884 1.00 45.54  ? 190 SER   B CB  1 
ATOM   4439 O OG  . SER   B 1 190 ? -5.514  -30.063 -60.687 1.00 51.68  ? 190 SER   B OG  1 
ATOM   4440 N N   . ILE   B 1 191 ? -6.418  -25.627 -59.489 1.00 41.02  ? 191 ILE   B N   1 
ATOM   4441 C CA  . ILE   B 1 191 ? -7.113  -24.394 -59.838 1.00 43.54  ? 191 ILE   B CA  1 
ATOM   4442 C C   . ILE   B 1 191 ? -6.196  -23.465 -60.618 1.00 41.84  ? 191 ILE   B C   1 
ATOM   4443 O O   . ILE   B 1 191 ? -6.577  -22.919 -61.657 1.00 42.25  ? 191 ILE   B O   1 
ATOM   4444 C CB  . ILE   B 1 191 ? -7.667  -23.700 -58.577 1.00 40.65  ? 191 ILE   B CB  1 
ATOM   4445 C CG1 . ILE   B 1 191 ? -8.694  -24.586 -57.883 1.00 38.53  ? 191 ILE   B CG1 1 
ATOM   4446 C CG2 . ILE   B 1 191 ? -8.301  -22.370 -58.942 1.00 37.60  ? 191 ILE   B CG2 1 
ATOM   4447 C CD1 . ILE   B 1 191 ? -8.925  -24.207 -56.445 1.00 41.04  ? 191 ILE   B CD1 1 
ATOM   4448 N N   . ARG   B 1 192 ? -4.962  -23.310 -60.137 1.00 43.05  ? 192 ARG   B N   1 
ATOM   4449 C CA  . ARG   B 1 192 ? -4.053  -22.312 -60.690 1.00 42.69  ? 192 ARG   B CA  1 
ATOM   4450 C C   . ARG   B 1 192 ? -3.580  -22.700 -62.087 1.00 37.95  ? 192 ARG   B C   1 
ATOM   4451 O O   . ARG   B 1 192 ? -3.651  -21.891 -63.020 1.00 39.34  ? 192 ARG   B O   1 
ATOM   4452 C CB  . ARG   B 1 192 ? -2.867  -22.123 -59.741 1.00 41.51  ? 192 ARG   B CB  1 
ATOM   4453 C CG  . ARG   B 1 192 ? -3.260  -21.602 -58.362 1.00 40.40  ? 192 ARG   B CG  1 
ATOM   4454 C CD  . ARG   B 1 192 ? -2.174  -21.893 -57.333 1.00 41.05  ? 192 ARG   B CD  1 
ATOM   4455 N NE  . ARG   B 1 192 ? -2.263  -23.259 -56.830 1.00 42.21  ? 192 ARG   B NE  1 
ATOM   4456 C CZ  . ARG   B 1 192 ? -1.356  -23.837 -56.053 1.00 43.80  ? 192 ARG   B CZ  1 
ATOM   4457 N NH1 . ARG   B 1 192 ? -0.268  -23.194 -55.663 1.00 44.23  ? 192 ARG   B NH1 1 
ATOM   4458 N NH2 . ARG   B 1 192 ? -1.548  -25.092 -55.655 1.00 41.79  ? 192 ARG   B NH2 1 
ATOM   4459 N N   . VAL   B 1 193 ? -3.101  -23.938 -62.253 1.00 39.80  ? 193 VAL   B N   1 
ATOM   4460 C CA  . VAL   B 1 193 ? -2.522  -24.349 -63.537 1.00 40.51  ? 193 VAL   B CA  1 
ATOM   4461 C C   . VAL   B 1 193 ? -3.535  -24.278 -64.678 1.00 41.99  ? 193 VAL   B C   1 
ATOM   4462 O O   . VAL   B 1 193 ? -3.194  -23.739 -65.742 1.00 42.30  ? 193 VAL   B O   1 
ATOM   4463 C CB  . VAL   B 1 193 ? -1.868  -25.732 -63.405 1.00 43.01  ? 193 VAL   B CB  1 
ATOM   4464 C CG1 . VAL   B 1 193 ? -1.538  -26.306 -64.775 1.00 43.40  ? 193 VAL   B CG1 1 
ATOM   4465 C CG2 . VAL   B 1 193 ? -0.622  -25.656 -62.531 1.00 41.27  ? 193 VAL   B CG2 1 
ATOM   4466 N N   . PRO   B 1 194 ? -4.777  -24.826 -64.588 1.00 41.88  ? 194 PRO   B N   1 
ATOM   4467 C CA  . PRO   B 1 194 ? -5.736  -24.663 -65.673 1.00 40.84  ? 194 PRO   B CA  1 
ATOM   4468 C C   . PRO   B 1 194 ? -6.006  -23.197 -65.984 1.00 41.19  ? 194 PRO   B C   1 
ATOM   4469 O O   . PRO   B 1 194 ? -6.084  -22.834 -67.170 1.00 43.74  ? 194 PRO   B O   1 
ATOM   4470 C CB  . PRO   B 1 194 ? -6.987  -25.378 -65.162 1.00 40.11  ? 194 PRO   B CB  1 
ATOM   4471 C CG  . PRO   B 1 194 ? -6.442  -26.428 -64.245 1.00 41.99  ? 194 PRO   B CG  1 
ATOM   4472 C CD  . PRO   B 1 194 ? -5.338  -25.686 -63.531 1.00 42.20  ? 194 PRO   B CD  1 
ATOM   4473 N N   . ALA   B 1 195 ? -6.133  -22.369 -64.945 1.00 40.56  ? 195 ALA   B N   1 
ATOM   4474 C CA  . ALA   B 1 195 ? -6.397  -20.925 -65.147 1.00 42.03  ? 195 ALA   B CA  1 
ATOM   4475 C C   . ALA   B 1 195 ? -5.221  -20.303 -65.899 1.00 41.17  ? 195 ALA   B C   1 
ATOM   4476 O O   . ALA   B 1 195 ? -5.465  -19.450 -66.768 1.00 39.61  ? 195 ALA   B O   1 
ATOM   4477 C CB  . ALA   B 1 195 ? -6.624  -20.250 -63.817 1.00 38.35  ? 195 ALA   B CB  1 
ATOM   4478 N N   . HIS   B 1 196 ? -3.994  -20.691 -65.551 1.00 37.68  ? 196 HIS   B N   1 
ATOM   4479 C CA  . HIS   B 1 196 ? -2.796  -20.216 -66.292 1.00 41.41  ? 196 HIS   B CA  1 
ATOM   4480 C C   . HIS   B 1 196 ? -2.834  -20.716 -67.739 1.00 44.05  ? 196 HIS   B C   1 
ATOM   4481 O O   . HIS   B 1 196 ? -2.519  -19.930 -68.654 1.00 44.90  ? 196 HIS   B O   1 
ATOM   4482 C CB  . HIS   B 1 196 ? -1.528  -20.668 -65.562 1.00 40.42  ? 196 HIS   B CB  1 
ATOM   4483 C CG  . HIS   B 1 196 ? -0.276  -20.694 -66.373 1.00 42.80  ? 196 HIS   B CG  1 
ATOM   4484 N ND1 . HIS   B 1 196 ? 0.133   -19.664 -67.191 1.00 44.57  ? 196 HIS   B ND1 1 
ATOM   4485 C CD2 . HIS   B 1 196 ? 0.670   -21.635 -66.462 1.00 44.45  ? 196 HIS   B CD2 1 
ATOM   4486 C CE1 . HIS   B 1 196 ? 1.283   -19.991 -67.761 1.00 42.73  ? 196 HIS   B CE1 1 
ATOM   4487 N NE2 . HIS   B 1 196 ? 1.628   -21.184 -67.331 1.00 47.32  ? 196 HIS   B NE2 1 
ATOM   4488 N N   . PHE   B 1 197 ? -3.238  -21.969 -67.947 1.00 40.14  ? 197 PHE   B N   1 
ATOM   4489 C CA  . PHE   B 1 197 ? -3.176  -22.563 -69.310 1.00 42.25  ? 197 PHE   B CA  1 
ATOM   4490 C C   . PHE   B 1 197 ? -4.240  -21.946 -70.206 1.00 42.56  ? 197 PHE   B C   1 
ATOM   4491 O O   . PHE   B 1 197 ? -4.047  -21.913 -71.433 1.00 41.54  ? 197 PHE   B O   1 
ATOM   4492 C CB  . PHE   B 1 197 ? -3.304  -24.085 -69.203 1.00 43.07  ? 197 PHE   B CB  1 
ATOM   4493 C CG  . PHE   B 1 197 ? -2.001  -24.805 -68.884 1.00 42.22  ? 197 PHE   B CG  1 
ATOM   4494 C CD1 . PHE   B 1 197 ? -0.897  -24.107 -68.410 1.00 40.72  ? 197 PHE   B CD1 1 
ATOM   4495 C CD2 . PHE   B 1 197 ? -1.880  -26.176 -69.069 1.00 41.79  ? 197 PHE   B CD2 1 
ATOM   4496 C CE1 . PHE   B 1 197 ? 0.288   -24.764 -68.125 1.00 45.52  ? 197 PHE   B CE1 1 
ATOM   4497 C CE2 . PHE   B 1 197 ? -0.694  -26.828 -68.781 1.00 44.77  ? 197 PHE   B CE2 1 
ATOM   4498 C CZ  . PHE   B 1 197 ? 0.387   -26.122 -68.311 1.00 43.58  ? 197 PHE   B CZ  1 
ATOM   4499 N N   . CYS   B 1 198 ? -5.322  -21.449 -69.618 1.00 40.61  ? 198 CYS   B N   1 
ATOM   4500 C CA  . CYS   B 1 198 ? -6.424  -20.903 -70.399 1.00 40.32  ? 198 CYS   B CA  1 
ATOM   4501 C C   . CYS   B 1 198 ? -6.612  -19.403 -70.218 1.00 42.11  ? 198 CYS   B C   1 
ATOM   4502 O O   . CYS   B 1 198 ? -7.478  -18.820 -70.880 1.00 38.94  ? 198 CYS   B O   1 
ATOM   4503 C CB  . CYS   B 1 198 ? -7.731  -21.622 -70.041 1.00 44.06  ? 198 CYS   B CB  1 
ATOM   4504 S SG  . CYS   B 1 198 ? -7.797  -23.368 -70.511 1.00 43.04  ? 198 CYS   B SG  1 
ATOM   4505 N N   . GLY   B 1 199 ? -5.846  -18.764 -69.336 1.00 41.13  ? 199 GLY   B N   1 
ATOM   4506 C CA  . GLY   B 1 199 ? -5.954  -17.331 -69.153 1.00 37.14  ? 199 GLY   B CA  1 
ATOM   4507 C C   . GLY   B 1 199 ? -7.261  -16.869 -68.542 1.00 40.23  ? 199 GLY   B C   1 
ATOM   4508 O O   . GLY   B 1 199 ? -7.933  -15.989 -69.089 1.00 40.69  ? 199 GLY   B O   1 
ATOM   4509 N N   . VAL   B 1 200 ? -7.636  -17.458 -67.410 1.00 40.91  ? 200 VAL   B N   1 
ATOM   4510 C CA  . VAL   B 1 200 ? -8.779  -17.015 -66.630 1.00 40.40  ? 200 VAL   B CA  1 
ATOM   4511 C C   . VAL   B 1 200 ? -8.334  -16.843 -65.179 1.00 39.42  ? 200 VAL   B C   1 
ATOM   4512 O O   . VAL   B 1 200 ? -7.169  -17.042 -64.837 1.00 39.79  ? 200 VAL   B O   1 
ATOM   4513 C CB  . VAL   B 1 200 ? -9.982  -17.978 -66.739 1.00 42.27  ? 200 VAL   B CB  1 
ATOM   4514 C CG1 . VAL   B 1 200 ? -10.500 -18.025 -68.174 1.00 40.29  ? 200 VAL   B CG1 1 
ATOM   4515 C CG2 . VAL   B 1 200 ? -9.613  -19.372 -66.246 1.00 39.75  ? 200 VAL   B CG2 1 
ATOM   4516 N N   . TRP   B 1 201 ? -9.281  -16.465 -64.328 1.00 40.76  ? 201 TRP   B N   1 
ATOM   4517 C CA  . TRP   B 1 201 ? -9.025  -16.231 -62.915 1.00 42.49  ? 201 TRP   B CA  1 
ATOM   4518 C C   . TRP   B 1 201 ? -9.370  -17.473 -62.105 1.00 40.51  ? 201 TRP   B C   1 
ATOM   4519 O O   . TRP   B 1 201 ? -10.395 -18.117 -62.345 1.00 39.28  ? 201 TRP   B O   1 
ATOM   4520 C CB  . TRP   B 1 201 ? -9.838  -15.032 -62.411 1.00 44.02  ? 201 TRP   B CB  1 
ATOM   4521 C CG  . TRP   B 1 201 ? -9.452  -13.739 -63.063 1.00 42.02  ? 201 TRP   B CG  1 
ATOM   4522 C CD1 . TRP   B 1 201 ? -9.577  -13.415 -64.384 1.00 41.44  ? 201 TRP   B CD1 1 
ATOM   4523 C CD2 . TRP   B 1 201 ? -8.860  -12.600 -62.425 1.00 41.82  ? 201 TRP   B CD2 1 
ATOM   4524 N NE1 . TRP   B 1 201 ? -9.105  -12.143 -64.606 1.00 45.03  ? 201 TRP   B NE1 1 
ATOM   4525 C CE2 . TRP   B 1 201 ? -8.657  -11.622 -63.420 1.00 46.05  ? 201 TRP   B CE2 1 
ATOM   4526 C CE3 . TRP   B 1 201 ? -8.483  -12.312 -61.109 1.00 42.64  ? 201 TRP   B CE3 1 
ATOM   4527 C CZ2 . TRP   B 1 201 ? -8.096  -10.377 -63.140 1.00 41.65  ? 201 TRP   B CZ2 1 
ATOM   4528 C CZ3 . TRP   B 1 201 ? -7.925  -11.075 -60.833 1.00 43.98  ? 201 TRP   B CZ3 1 
ATOM   4529 C CH2 . TRP   B 1 201 ? -7.737  -10.124 -61.844 1.00 43.83  ? 201 TRP   B CH2 1 
ATOM   4530 N N   . GLY   B 1 202 ? -8.507  -17.803 -61.147 1.00 42.47  ? 202 GLY   B N   1 
ATOM   4531 C CA  . GLY   B 1 202 ? -8.735  -18.929 -60.260 1.00 44.31  ? 202 GLY   B CA  1 
ATOM   4532 C C   . GLY   B 1 202 ? -8.115  -18.725 -58.893 1.00 43.65  ? 202 GLY   B C   1 
ATOM   4533 O O   . GLY   B 1 202 ? -6.925  -18.412 -58.790 1.00 44.15  ? 202 GLY   B O   1 
ATOM   4534 N N   . LEU   B 1 203 ? -8.900  -18.889 -57.831 1.00 42.13  ? 203 LEU   B N   1 
ATOM   4535 C CA  . LEU   B 1 203 ? -8.419  -18.662 -56.473 1.00 42.99  ? 203 LEU   B CA  1 
ATOM   4536 C C   . LEU   B 1 203 ? -8.208  -20.003 -55.780 1.00 40.72  ? 203 LEU   B C   1 
ATOM   4537 O O   . LEU   B 1 203 ? -9.170  -20.729 -55.506 1.00 40.88  ? 203 LEU   B O   1 
ATOM   4538 C CB  . LEU   B 1 203 ? -9.386  -17.789 -55.676 1.00 38.14  ? 203 LEU   B CB  1 
ATOM   4539 C CG  . LEU   B 1 203 ? -8.977  -17.605 -54.211 1.00 37.05  ? 203 LEU   B CG  1 
ATOM   4540 C CD1 . LEU   B 1 203 ? -7.668  -16.833 -54.116 1.00 39.51  ? 203 LEU   B CD1 1 
ATOM   4541 C CD2 . LEU   B 1 203 ? -10.066 -16.903 -53.408 1.00 36.25  ? 203 LEU   B CD2 1 
ATOM   4542 N N   . LYS   B 1 204 ? -6.950  -20.323 -55.494 1.00 39.04  ? 204 LYS   B N   1 
ATOM   4543 C CA  . LYS   B 1 204 ? -6.631  -21.399 -54.568 1.00 38.34  ? 204 LYS   B CA  1 
ATOM   4544 C C   . LYS   B 1 204 ? -6.792  -20.858 -53.155 1.00 39.59  ? 204 LYS   B C   1 
ATOM   4545 O O   . LYS   B 1 204 ? -6.069  -19.940 -52.754 1.00 36.27  ? 204 LYS   B O   1 
ATOM   4546 C CB  . LYS   B 1 204 ? -5.212  -21.910 -54.805 1.00 37.45  ? 204 LYS   B CB  1 
ATOM   4547 C CG  . LYS   B 1 204 ? -4.796  -23.067 -53.902 1.00 40.78  ? 204 LYS   B CG  1 
ATOM   4548 C CD  . LYS   B 1 204 ? -3.918  -22.601 -52.753 1.00 37.75  ? 204 LYS   B CD  1 
ATOM   4549 C CE  . LYS   B 1 204 ? -3.758  -23.686 -51.704 1.00 37.16  ? 204 LYS   B CE  1 
ATOM   4550 N NZ  . LYS   B 1 204 ? -3.831  -23.152 -50.316 1.00 38.43  ? 204 LYS   B NZ  1 
ATOM   4551 N N   . THR   B 1 205 ? -7.747  -21.401 -52.410 1.00 39.20  ? 205 THR   B N   1 
ATOM   4552 C CA  . THR   B 1 205 ? -8.120  -20.812 -51.134 1.00 38.17  ? 205 THR   B CA  1 
ATOM   4553 C C   . THR   B 1 205 ? -7.222  -21.308 -50.005 1.00 36.08  ? 205 THR   B C   1 
ATOM   4554 O O   . THR   B 1 205 ? -6.502  -22.301 -50.136 1.00 38.79  ? 205 THR   B O   1 
ATOM   4555 C CB  . THR   B 1 205 ? -9.582  -21.116 -50.805 1.00 36.26  ? 205 THR   B CB  1 
ATOM   4556 O OG1 . THR   B 1 205 ? -9.858  -22.499 -51.054 1.00 37.21  ? 205 THR   B OG1 1 
ATOM   4557 C CG2 . THR   B 1 205 ? -10.499 -20.260 -51.662 1.00 33.42  ? 205 THR   B CG2 1 
ATOM   4558 N N   . THR   B 1 206 ? -7.271  -20.584 -48.886 1.00 37.01  ? 206 THR   B N   1 
ATOM   4559 C CA  . THR   B 1 206 ? -6.571  -21.004 -47.680 1.00 36.03  ? 206 THR   B CA  1 
ATOM   4560 C C   . THR   B 1 206 ? -7.049  -22.387 -47.269 1.00 38.95  ? 206 THR   B C   1 
ATOM   4561 O O   . THR   B 1 206 ? -8.249  -22.675 -47.301 1.00 37.90  ? 206 THR   B O   1 
ATOM   4562 C CB  . THR   B 1 206 ? -6.823  -20.016 -46.536 1.00 36.54  ? 206 THR   B CB  1 
ATOM   4563 O OG1 . THR   B 1 206 ? -6.404  -18.703 -46.926 1.00 39.63  ? 206 THR   B OG1 1 
ATOM   4564 C CG2 . THR   B 1 206 ? -6.057  -20.432 -45.283 1.00 36.79  ? 206 THR   B CG2 1 
ATOM   4565 N N   . PHE   B 1 207 ? -6.105  -23.252 -46.899 1.00 39.02  ? 207 PHE   B N   1 
ATOM   4566 C CA  . PHE   B 1 207 ? -6.472  -24.594 -46.473 1.00 39.36  ? 207 PHE   B CA  1 
ATOM   4567 C C   . PHE   B 1 207 ? -7.464  -24.519 -45.321 1.00 42.19  ? 207 PHE   B C   1 
ATOM   4568 O O   . PHE   B 1 207 ? -7.310  -23.708 -44.404 1.00 42.86  ? 207 PHE   B O   1 
ATOM   4569 C CB  . PHE   B 1 207 ? -5.234  -25.392 -46.056 1.00 41.28  ? 207 PHE   B CB  1 
ATOM   4570 C CG  . PHE   B 1 207 ? -5.540  -26.806 -45.640 1.00 41.62  ? 207 PHE   B CG  1 
ATOM   4571 C CD1 . PHE   B 1 207 ? -5.963  -27.743 -46.572 1.00 40.86  ? 207 PHE   B CD1 1 
ATOM   4572 C CD2 . PHE   B 1 207 ? -5.418  -27.192 -44.315 1.00 39.07  ? 207 PHE   B CD2 1 
ATOM   4573 C CE1 . PHE   B 1 207 ? -6.255  -29.040 -46.189 1.00 42.87  ? 207 PHE   B CE1 1 
ATOM   4574 C CE2 . PHE   B 1 207 ? -5.706  -28.486 -43.924 1.00 45.56  ? 207 PHE   B CE2 1 
ATOM   4575 C CZ  . PHE   B 1 207 ? -6.126  -29.413 -44.863 1.00 47.69  ? 207 PHE   B CZ  1 
ATOM   4576 N N   . ASP   B 1 208 ? -8.510  -25.343 -45.404 1.00 42.91  ? 208 ASP   B N   1 
ATOM   4577 C CA  . ASP   B 1 208 ? -9.564  -25.481 -44.400 1.00 43.97  ? 208 ASP   B CA  1 
ATOM   4578 C C   . ASP   B 1 208 ? -10.549 -24.318 -44.383 1.00 40.97  ? 208 ASP   B C   1 
ATOM   4579 O O   . ASP   B 1 208 ? -11.359 -24.226 -43.453 1.00 42.92  ? 208 ASP   B O   1 
ATOM   4580 C CB  . ASP   B 1 208 ? -8.995  -25.664 -42.986 1.00 46.41  ? 208 ASP   B CB  1 
ATOM   4581 C CG  . ASP   B 1 208 ? -8.930  -27.116 -42.563 1.00 51.51  ? 208 ASP   B CG  1 
ATOM   4582 O OD1 . ASP   B 1 208 ? -9.593  -27.954 -43.210 1.00 49.90  ? 208 ASP   B OD1 1 
ATOM   4583 O OD2 . ASP   B 1 208 ? -8.234  -27.418 -41.568 1.00 54.67  ? 208 ASP   B OD2 1 
ATOM   4584 N N   . ALA   B 1 209 ? -10.514 -23.430 -45.377 1.00 38.93  ? 209 ALA   B N   1 
ATOM   4585 C CA  . ALA   B 1 209 ? -11.427 -22.291 -45.406 1.00 37.73  ? 209 ALA   B CA  1 
ATOM   4586 C C   . ALA   B 1 209 ? -12.774 -22.621 -46.031 1.00 37.83  ? 209 ALA   B C   1 
ATOM   4587 O O   . ALA   B 1 209 ? -13.797 -22.070 -45.606 1.00 37.98  ? 209 ALA   B O   1 
ATOM   4588 C CB  . ALA   B 1 209 ? -10.796 -21.121 -46.163 1.00 40.52  ? 209 ALA   B CB  1 
ATOM   4589 N N   . VAL   B 1 210 ? -12.799 -23.497 -47.033 1.00 39.08  ? 210 VAL   B N   1 
ATOM   4590 C CA  . VAL   B 1 210 ? -14.033 -23.945 -47.668 1.00 38.77  ? 210 VAL   B CA  1 
ATOM   4591 C C   . VAL   B 1 210 ? -14.148 -25.450 -47.473 1.00 39.01  ? 210 VAL   B C   1 
ATOM   4592 O O   . VAL   B 1 210 ? -13.147 -26.172 -47.545 1.00 40.88  ? 210 VAL   B O   1 
ATOM   4593 C CB  . VAL   B 1 210 ? -14.077 -23.584 -49.169 1.00 39.51  ? 210 VAL   B CB  1 
ATOM   4594 C CG1 . VAL   B 1 210 ? -15.457 -23.890 -49.753 1.00 36.01  ? 210 VAL   B CG1 1 
ATOM   4595 C CG2 . VAL   B 1 210 ? -13.699 -22.123 -49.388 1.00 37.83  ? 210 VAL   B CG2 1 
ATOM   4596 N N   . SER   B 1 211 ? -15.369 -25.922 -47.233 1.00 37.94  ? 211 SER   B N   1 
ATOM   4597 C CA  . SER   B 1 211 ? -15.592 -27.331 -46.942 1.00 40.68  ? 211 SER   B CA  1 
ATOM   4598 C C   . SER   B 1 211 ? -15.501 -28.171 -48.210 1.00 41.66  ? 211 SER   B C   1 
ATOM   4599 O O   . SER   B 1 211 ? -16.000 -27.784 -49.272 1.00 42.21  ? 211 SER   B O   1 
ATOM   4600 C CB  . SER   B 1 211 ? -16.955 -27.528 -46.277 1.00 39.74  ? 211 SER   B CB  1 
ATOM   4601 O OG  . SER   B 1 211 ? -17.521 -28.782 -46.618 1.00 45.78  ? 211 SER   B OG  1 
ATOM   4602 N N   . LEU   B 1 212 ? -14.855 -29.329 -48.089 1.00 43.49  ? 212 LEU   B N   1 
ATOM   4603 C CA  . LEU   B 1 212 ? -14.704 -30.281 -49.181 1.00 40.56  ? 212 LEU   B CA  1 
ATOM   4604 C C   . LEU   B 1 212 ? -15.824 -31.315 -49.219 1.00 41.24  ? 212 LEU   B C   1 
ATOM   4605 O O   . LEU   B 1 212 ? -15.745 -32.261 -50.010 1.00 41.20  ? 212 LEU   B O   1 
ATOM   4606 C CB  . LEU   B 1 212 ? -13.353 -30.996 -49.072 1.00 38.50  ? 212 LEU   B CB  1 
ATOM   4607 C CG  . LEU   B 1 212 ? -12.124 -30.335 -49.698 1.00 43.75  ? 212 LEU   B CG  1 
ATOM   4608 C CD1 . LEU   B 1 212 ? -10.897 -30.600 -48.847 1.00 46.47  ? 212 LEU   B CD1 1 
ATOM   4609 C CD2 . LEU   B 1 212 ? -11.907 -30.840 -51.113 1.00 44.57  ? 212 LEU   B CD2 1 
ATOM   4610 N N   . GLU   B 1 213 ? -16.854 -31.160 -48.386 1.00 41.95  ? 213 GLU   B N   1 
ATOM   4611 C CA  . GLU   B 1 213 ? -17.922 -32.150 -48.323 1.00 41.53  ? 213 GLU   B CA  1 
ATOM   4612 C C   . GLU   B 1 213 ? -18.637 -32.238 -49.665 1.00 42.45  ? 213 GLU   B C   1 
ATOM   4613 O O   . GLU   B 1 213 ? -19.038 -31.221 -50.240 1.00 40.30  ? 213 GLU   B O   1 
ATOM   4614 C CB  . GLU   B 1 213 ? -18.914 -31.799 -47.213 1.00 42.11  ? 213 GLU   B CB  1 
ATOM   4615 C CG  . GLU   B 1 213 ? -20.344 -32.256 -47.498 1.00 44.09  ? 213 GLU   B CG  1 
ATOM   4616 C CD  . GLU   B 1 213 ? -21.342 -31.783 -46.456 1.00 49.44  ? 213 GLU   B CD  1 
ATOM   4617 O OE1 . GLU   B 1 213 ? -21.124 -30.706 -45.865 1.00 51.92  ? 213 GLU   B OE1 1 
ATOM   4618 O OE2 . GLU   B 1 213 ? -22.348 -32.489 -46.229 1.00 53.84  ? 213 GLU   B OE2 1 
ATOM   4619 N N   . GLY   B 1 214 ? -18.791 -33.461 -50.166 1.00 40.33  ? 214 GLY   B N   1 
ATOM   4620 C CA  . GLY   B 1 214 ? -19.354 -33.680 -51.476 1.00 39.69  ? 214 GLY   B CA  1 
ATOM   4621 C C   . GLY   B 1 214 ? -18.339 -33.744 -52.594 1.00 40.30  ? 214 GLY   B C   1 
ATOM   4622 O O   . GLY   B 1 214 ? -18.679 -34.207 -53.690 1.00 40.32  ? 214 GLY   B O   1 
ATOM   4623 N N   . HIS   B 1 215 ? -17.108 -33.281 -52.358 1.00 39.31  ? 215 HIS   B N   1 
ATOM   4624 C CA  . HIS   B 1 215 ? -15.979 -33.553 -53.249 1.00 38.57  ? 215 HIS   B CA  1 
ATOM   4625 C C   . HIS   B 1 215 ? -15.417 -34.941 -52.930 1.00 38.73  ? 215 HIS   B C   1 
ATOM   4626 O O   . HIS   B 1 215 ? -14.248 -35.125 -52.597 1.00 40.87  ? 215 HIS   B O   1 
ATOM   4627 C CB  . HIS   B 1 215 ? -14.920 -32.465 -53.112 1.00 38.35  ? 215 HIS   B CB  1 
ATOM   4628 C CG  . HIS   B 1 215 ? -13.953 -32.405 -54.256 1.00 38.01  ? 215 HIS   B CG  1 
ATOM   4629 N ND1 . HIS   B 1 215 ? -12.723 -33.028 -54.230 1.00 41.09  ? 215 HIS   B ND1 1 
ATOM   4630 C CD2 . HIS   B 1 215 ? -14.041 -31.798 -55.463 1.00 36.94  ? 215 HIS   B CD2 1 
ATOM   4631 C CE1 . HIS   B 1 215 ? -12.094 -32.804 -55.371 1.00 39.77  ? 215 HIS   B CE1 1 
ATOM   4632 N NE2 . HIS   B 1 215 ? -12.873 -32.060 -56.136 1.00 38.40  ? 215 HIS   B NE2 1 
ATOM   4633 N N   . TYR   B 1 216 ? -16.299 -35.930 -53.033 1.00 40.00  ? 216 TYR   B N   1 
ATOM   4634 C CA  . TYR   B 1 216 ? -16.028 -37.282 -52.574 1.00 39.81  ? 216 TYR   B CA  1 
ATOM   4635 C C   . TYR   B 1 216 ? -15.385 -38.112 -53.674 1.00 38.29  ? 216 TYR   B C   1 
ATOM   4636 O O   . TYR   B 1 216 ? -15.736 -37.983 -54.851 1.00 36.95  ? 216 TYR   B O   1 
ATOM   4637 C CB  . TYR   B 1 216 ? -17.329 -37.952 -52.135 1.00 39.11  ? 216 TYR   B CB  1 
ATOM   4638 C CG  . TYR   B 1 216 ? -17.910 -37.397 -50.865 1.00 38.06  ? 216 TYR   B CG  1 
ATOM   4639 C CD1 . TYR   B 1 216 ? -17.092 -36.917 -49.854 1.00 41.81  ? 216 TYR   B CD1 1 
ATOM   4640 C CD2 . TYR   B 1 216 ? -19.282 -37.322 -50.692 1.00 39.75  ? 216 TYR   B CD2 1 
ATOM   4641 C CE1 . TYR   B 1 216 ? -17.628 -36.400 -48.692 1.00 40.88  ? 216 TYR   B CE1 1 
ATOM   4642 C CE2 . TYR   B 1 216 ? -19.826 -36.808 -49.538 1.00 42.01  ? 216 TYR   B CE2 1 
ATOM   4643 C CZ  . TYR   B 1 216 ? -18.995 -36.348 -48.541 1.00 41.27  ? 216 TYR   B CZ  1 
ATOM   4644 O OH  . TYR   B 1 216 ? -19.541 -35.832 -47.389 1.00 46.11  ? 216 TYR   B OH  1 
ATOM   4645 N N   . PHE   B 1 217 ? -14.450 -38.971 -53.286 1.00 39.32  ? 217 PHE   B N   1 
ATOM   4646 C CA  . PHE   B 1 217 ? -14.031 -40.015 -54.202 1.00 37.73  ? 217 PHE   B CA  1 
ATOM   4647 C C   . PHE   B 1 217 ? -15.244 -40.883 -54.532 1.00 40.69  ? 217 PHE   B C   1 
ATOM   4648 O O   . PHE   B 1 217 ? -16.032 -41.208 -53.634 1.00 37.75  ? 217 PHE   B O   1 
ATOM   4649 C CB  . PHE   B 1 217 ? -12.909 -40.864 -53.601 1.00 36.31  ? 217 PHE   B CB  1 
ATOM   4650 C CG  . PHE   B 1 217 ? -12.250 -41.777 -54.598 1.00 40.48  ? 217 PHE   B CG  1 
ATOM   4651 C CD1 . PHE   B 1 217 ? -11.167 -41.342 -55.347 1.00 41.99  ? 217 PHE   B CD1 1 
ATOM   4652 C CD2 . PHE   B 1 217 ? -12.730 -43.061 -54.804 1.00 39.78  ? 217 PHE   B CD2 1 
ATOM   4653 C CE1 . PHE   B 1 217 ? -10.569 -42.175 -56.274 1.00 41.23  ? 217 PHE   B CE1 1 
ATOM   4654 C CE2 . PHE   B 1 217 ? -12.137 -43.899 -55.730 1.00 39.71  ? 217 PHE   B CE2 1 
ATOM   4655 C CZ  . PHE   B 1 217 ? -11.055 -43.456 -56.467 1.00 40.40  ? 217 PHE   B CZ  1 
ATOM   4656 N N   . PRO   B 1 218 ? -15.441 -41.247 -55.801 1.00 36.09  ? 218 PRO   B N   1 
ATOM   4657 C CA  . PRO   B 1 218 ? -16.679 -41.930 -56.199 1.00 36.59  ? 218 PRO   B CA  1 
ATOM   4658 C C   . PRO   B 1 218 ? -16.981 -43.161 -55.350 1.00 38.66  ? 218 PRO   B C   1 
ATOM   4659 O O   . PRO   B 1 218 ? -16.095 -43.958 -55.034 1.00 38.44  ? 218 PRO   B O   1 
ATOM   4660 C CB  . PRO   B 1 218 ? -16.409 -42.301 -57.660 1.00 38.28  ? 218 PRO   B CB  1 
ATOM   4661 C CG  . PRO   B 1 218 ? -15.500 -41.201 -58.127 1.00 37.23  ? 218 PRO   B CG  1 
ATOM   4662 C CD  . PRO   B 1 218 ? -14.568 -40.997 -56.962 1.00 37.73  ? 218 PRO   B CD  1 
ATOM   4663 N N   . ARG   B 1 219 ? -18.255 -43.291 -54.971 1.00 38.02  ? 219 ARG   B N   1 
ATOM   4664 C CA  . ARG   B 1 219 ? -18.788 -44.393 -54.172 1.00 40.41  ? 219 ARG   B CA  1 
ATOM   4665 C C   . ARG   B 1 219 ? -18.279 -44.384 -52.732 1.00 44.07  ? 219 ARG   B C   1 
ATOM   4666 O O   . ARG   B 1 219 ? -18.403 -45.390 -52.024 1.00 40.99  ? 219 ARG   B O   1 
ATOM   4667 C CB  . ARG   B 1 219 ? -18.503 -45.751 -54.828 1.00 36.64  ? 219 ARG   B CB  1 
ATOM   4668 C CG  . ARG   B 1 219 ? -19.036 -45.863 -56.255 1.00 41.22  ? 219 ARG   B CG  1 
ATOM   4669 C CD  . ARG   B 1 219 ? -18.749 -47.222 -56.876 1.00 39.96  ? 219 ARG   B CD  1 
ATOM   4670 N NE  . ARG   B 1 219 ? -18.696 -47.163 -58.333 1.00 45.57  ? 219 ARG   B NE  1 
ATOM   4671 C CZ  . ARG   B 1 219 ? -19.761 -47.184 -59.125 1.00 45.58  ? 219 ARG   B CZ  1 
ATOM   4672 N NH1 . ARG   B 1 219 ? -20.988 -47.243 -58.633 1.00 43.36  ? 219 ARG   B NH1 1 
ATOM   4673 N NH2 . ARG   B 1 219 ? -19.591 -47.144 -60.444 1.00 43.61  ? 219 ARG   B NH2 1 
ATOM   4674 N N   . THR   B 1 220 ? -17.710 -43.266 -52.276 1.00 39.19  ? 220 THR   B N   1 
ATOM   4675 C CA  . THR   B 1 220 ? -17.261 -43.099 -50.898 1.00 39.38  ? 220 THR   B CA  1 
ATOM   4676 C C   . THR   B 1 220 ? -17.806 -41.783 -50.350 1.00 40.02  ? 220 THR   B C   1 
ATOM   4677 O O   . THR   B 1 220 ? -18.479 -41.021 -51.052 1.00 39.33  ? 220 THR   B O   1 
ATOM   4678 C CB  . THR   B 1 220 ? -15.727 -43.121 -50.786 1.00 41.00  ? 220 THR   B CB  1 
ATOM   4679 O OG1 . THR   B 1 220 ? -15.207 -41.797 -50.973 1.00 41.06  ? 220 THR   B OG1 1 
ATOM   4680 C CG2 . THR   B 1 220 ? -15.111 -44.051 -51.821 1.00 38.80  ? 220 THR   B CG2 1 
ATOM   4681 N N   . ASP   B 1 221 ? -17.521 -41.527 -49.073 1.00 43.17  ? 221 ASP   B N   1 
ATOM   4682 C CA  . ASP   B 1 221 ? -17.752 -40.233 -48.443 1.00 41.84  ? 221 ASP   B CA  1 
ATOM   4683 C C   . ASP   B 1 221 ? -16.439 -39.669 -47.912 1.00 42.75  ? 221 ASP   B C   1 
ATOM   4684 O O   . ASP   B 1 221 ? -16.393 -39.026 -46.858 1.00 43.29  ? 221 ASP   B O   1 
ATOM   4685 C CB  . ASP   B 1 221 ? -18.795 -40.322 -47.324 1.00 42.26  ? 221 ASP   B CB  1 
ATOM   4686 C CG  . ASP   B 1 221 ? -18.474 -41.400 -46.296 1.00 46.38  ? 221 ASP   B CG  1 
ATOM   4687 O OD1 . ASP   B 1 221 ? -17.289 -41.758 -46.136 1.00 45.52  ? 221 ASP   B OD1 1 
ATOM   4688 O OD2 . ASP   B 1 221 ? -19.418 -41.879 -45.626 1.00 50.75  ? 221 ASP   B OD2 1 
ATOM   4689 N N   . SER   B 1 222 ? -15.374 -39.871 -48.679 1.00 45.10  ? 222 SER   B N   1 
ATOM   4690 C CA  . SER   B 1 222 ? -14.047 -39.437 -48.188 1.00 48.63  ? 222 SER   B CA  1 
ATOM   4691 C C   . SER   B 1 222 ? -13.572 -38.168 -48.902 1.00 49.89  ? 222 SER   B C   1 
ATOM   4692 O O   . SER   B 1 222 ? -13.071 -38.289 -50.038 1.00 51.03  ? 222 SER   B O   1 
ATOM   4693 C CB  . SER   B 1 222 ? -13.045 -40.551 -48.331 1.00 47.46  ? 222 SER   B CB  1 
ATOM   4694 O OG  . SER   B 1 222 ? -13.541 -41.750 -47.752 1.00 53.81  ? 222 SER   B OG  1 
ATOM   4695 N N   . ALA   B 1 223 ? -13.771 -36.995 -48.291 1.00 50.72  ? 223 ALA   B N   1 
ATOM   4696 C CA  . ALA   B 1 223 ? -13.168 -35.772 -48.866 1.00 51.87  ? 223 ALA   B CA  1 
ATOM   4697 C C   . ALA   B 1 223 ? -11.670 -36.029 -48.779 1.00 60.00  ? 223 ALA   B C   1 
ATOM   4698 O O   . ALA   B 1 223 ? -10.961 -35.589 -49.705 1.00 60.70  ? 223 ALA   B O   1 
ATOM   4699 C CB  . ALA   B 1 223 ? -13.588 -34.564 -48.081 1.00 48.73  ? 223 ALA   B CB  1 
ATOM   4700 N N   . LYS   B 1 224 ? -11.197 -36.598 -47.660 1.00 65.90  ? 224 LYS   B N   1 
ATOM   4701 C CA  . LYS   B 1 224 ? -9.801  -37.112 -47.556 1.00 66.59  ? 224 LYS   B CA  1 
ATOM   4702 C C   . LYS   B 1 224 ? -8.743  -36.077 -47.930 1.00 65.64  ? 224 LYS   B C   1 
ATOM   4703 O O   . LYS   B 1 224 ? -7.757  -36.449 -48.603 1.00 69.22  ? 224 LYS   B O   1 
ATOM   4704 C CB  . LYS   B 1 224 ? -9.622  -38.363 -48.429 1.00 67.75  ? 224 LYS   B CB  1 
ATOM   4705 C CG  . LYS   B 1 224 ? -9.646  -38.299 -49.961 1.00 64.77  ? 224 LYS   B CG  1 
ATOM   4706 C CD  . LYS   B 1 224 ? -9.994  -39.602 -50.668 1.00 61.75  ? 224 LYS   B CD  1 
ATOM   4707 C CE  . LYS   B 1 224 ? -9.678  -39.560 -52.128 1.00 64.93  ? 224 LYS   B CE  1 
ATOM   4708 N NZ  . LYS   B 1 224 ? -8.594  -38.619 -52.418 1.00 54.90  ? 224 LYS   B NZ  1 
ATOM   4709 N N   . ALA   B 1 225 ? -8.886  -34.838 -47.485 1.00 60.27  ? 225 ALA   B N   1 
ATOM   4710 C CA  . ALA   B 1 225 ? -7.884  -33.904 -48.040 1.00 65.80  ? 225 ALA   B CA  1 
ATOM   4711 C C   . ALA   B 1 225 ? -6.915  -33.267 -47.053 1.00 62.19  ? 225 ALA   B C   1 
ATOM   4712 O O   . ALA   B 1 225 ? -7.352  -32.638 -46.069 1.00 60.63  ? 225 ALA   B O   1 
ATOM   4713 C CB  . ALA   B 1 225 ? -8.614  -32.845 -48.813 1.00 68.92  ? 225 ALA   B CB  1 
ATOM   4714 N N   . ASP   B 1 226 ? -5.624  -33.437 -47.328 1.00 54.08  ? 226 ASP   B N   1 
ATOM   4715 C CA  . ASP   B 1 226 ? -4.586  -32.681 -46.594 1.00 51.56  ? 226 ASP   B CA  1 
ATOM   4716 C C   . ASP   B 1 226 ? -3.869  -32.006 -47.761 1.00 47.98  ? 226 ASP   B C   1 
ATOM   4717 O O   . ASP   B 1 226 ? -3.599  -32.738 -48.735 1.00 48.51  ? 226 ASP   B O   1 
ATOM   4718 C CB  . ASP   B 1 226 ? -3.712  -33.580 -45.739 1.00 49.95  ? 226 ASP   B CB  1 
ATOM   4719 C CG  . ASP   B 1 226 ? -4.039  -33.611 -44.254 1.00 54.69  ? 226 ASP   B CG  1 
ATOM   4720 O OD1 . ASP   B 1 226 ? -4.517  -34.663 -43.784 1.00 57.51  ? 226 ASP   B OD1 1 
ATOM   4721 O OD2 . ASP   B 1 226 ? -3.808  -32.587 -43.581 1.00 48.43  ? 226 ASP   B OD2 1 
ATOM   4722 N N   . LEU   B 1 227 ? -3.690  -30.686 -47.730 1.00 45.15  ? 227 LEU   B N   1 
ATOM   4723 C CA  . LEU   B 1 227 ? -3.035  -29.925 -48.833 1.00 44.11  ? 227 LEU   B CA  1 
ATOM   4724 C C   . LEU   B 1 227 ? -4.063  -29.726 -49.958 1.00 41.45  ? 227 LEU   B C   1 
ATOM   4725 O O   . LEU   B 1 227 ? -3.699  -29.150 -50.989 1.00 45.15  ? 227 LEU   B O   1 
ATOM   4726 C CB  . LEU   B 1 227 ? -1.759  -30.548 -49.410 1.00 45.50  ? 227 LEU   B CB  1 
ATOM   4727 C CG  . LEU   B 1 227 ? -0.714  -31.096 -48.435 1.00 44.06  ? 227 LEU   B CG  1 
ATOM   4728 C CD1 . LEU   B 1 227 ? -0.225  -32.410 -49.016 1.00 44.45  ? 227 LEU   B CD1 1 
ATOM   4729 C CD2 . LEU   B 1 227 ? 0.439   -30.122 -48.320 1.00 41.82  ? 227 LEU   B CD2 1 
ATOM   4730 N N   . SER   B 1 228 ? -5.314  -30.131 -49.758 1.00 41.96  ? 228 SER   B N   1 
ATOM   4731 C CA  . SER   B 1 228 ? -6.278  -30.049 -50.884 1.00 42.28  ? 228 SER   B CA  1 
ATOM   4732 C C   . SER   B 1 228 ? -7.331  -28.987 -50.577 1.00 41.53  ? 228 SER   B C   1 
ATOM   4733 O O   . SER   B 1 228 ? -7.889  -29.001 -49.464 1.00 43.22  ? 228 SER   B O   1 
ATOM   4734 C CB  . SER   B 1 228 ? -6.918  -31.367 -51.191 1.00 43.83  ? 228 SER   B CB  1 
ATOM   4735 O OG  . SER   B 1 228 ? -8.063  -31.187 -52.012 1.00 51.70  ? 228 SER   B OG  1 
ATOM   4736 N N   . VAL   B 1 229 ? -7.552  -28.088 -51.533 1.00 39.63  ? 229 VAL   B N   1 
ATOM   4737 C CA  . VAL   B 1 229 ? -8.505  -26.973 -51.286 1.00 41.82  ? 229 VAL   B CA  1 
ATOM   4738 C C   . VAL   B 1 229 ? -9.429  -26.791 -52.493 1.00 39.26  ? 229 VAL   B C   1 
ATOM   4739 O O   . VAL   B 1 229 ? -9.024  -27.137 -53.620 1.00 39.18  ? 229 VAL   B O   1 
ATOM   4740 C CB  . VAL   B 1 229 ? -7.790  -25.644 -50.965 1.00 42.70  ? 229 VAL   B CB  1 
ATOM   4741 C CG1 . VAL   B 1 229 ? -6.669  -25.805 -49.947 1.00 41.72  ? 229 VAL   B CG1 1 
ATOM   4742 C CG2 . VAL   B 1 229 ? -7.283  -24.947 -52.220 1.00 38.15  ? 229 VAL   B CG2 1 
ATOM   4743 N N   . VAL   B 1 230 ? -10.644 -26.329 -52.238 1.00 36.05  ? 230 VAL   B N   1 
ATOM   4744 C CA  . VAL   B 1 230 ? -11.572 -25.967 -53.301 1.00 40.60  ? 230 VAL   B CA  1 
ATOM   4745 C C   . VAL   B 1 230 ? -11.665 -24.450 -53.341 1.00 38.42  ? 230 VAL   B C   1 
ATOM   4746 O O   . VAL   B 1 230 ? -11.570 -23.773 -52.311 1.00 37.23  ? 230 VAL   B O   1 
ATOM   4747 C CB  . VAL   B 1 230 ? -12.970 -26.596 -53.110 1.00 40.16  ? 230 VAL   B CB  1 
ATOM   4748 C CG1 . VAL   B 1 230 ? -12.902 -28.095 -53.312 1.00 39.14  ? 230 VAL   B CG1 1 
ATOM   4749 C CG2 . VAL   B 1 230 ? -13.540 -26.254 -51.737 1.00 38.12  ? 230 VAL   B CG2 1 
ATOM   4750 N N   . GLY   B 1 231 ? -11.834 -23.914 -54.543 1.00 37.11  ? 231 GLY   B N   1 
ATOM   4751 C CA  . GLY   B 1 231 ? -11.936 -22.488 -54.724 1.00 38.10  ? 231 GLY   B CA  1 
ATOM   4752 C C   . GLY   B 1 231 ? -12.538 -22.129 -56.064 1.00 37.15  ? 231 GLY   B C   1 
ATOM   4753 O O   . GLY   B 1 231 ? -12.543 -22.928 -57.004 1.00 39.51  ? 231 GLY   B O   1 
ATOM   4754 N N   . PRO   B 1 232 ? -13.053 -20.912 -56.181 1.00 42.07  ? 232 PRO   B N   1 
ATOM   4755 C CA  . PRO   B 1 232 ? -13.789 -20.532 -57.387 1.00 38.85  ? 232 PRO   B CA  1 
ATOM   4756 C C   . PRO   B 1 232 ? -12.863 -20.226 -58.555 1.00 39.58  ? 232 PRO   B C   1 
ATOM   4757 O O   . PRO   B 1 232 ? -11.664 -19.986 -58.401 1.00 39.97  ? 232 PRO   B O   1 
ATOM   4758 C CB  . PRO   B 1 232 ? -14.543 -19.277 -56.943 1.00 38.52  ? 232 PRO   B CB  1 
ATOM   4759 C CG  . PRO   B 1 232 ? -13.605 -18.653 -55.958 1.00 39.78  ? 232 PRO   B CG  1 
ATOM   4760 C CD  . PRO   B 1 232 ? -13.034 -19.822 -55.189 1.00 43.40  ? 232 PRO   B CD  1 
ATOM   4761 N N   . MET   B 1 233 ? -13.455 -20.262 -59.746 1.00 37.72  ? 233 MET   B N   1 
ATOM   4762 C CA  . MET   B 1 233 ? -12.797 -19.868 -60.982 1.00 37.64  ? 233 MET   B CA  1 
ATOM   4763 C C   . MET   B 1 233 ? -13.765 -19.014 -61.780 1.00 39.51  ? 233 MET   B C   1 
ATOM   4764 O O   . MET   B 1 233 ? -14.952 -19.339 -61.882 1.00 38.59  ? 233 MET   B O   1 
ATOM   4765 C CB  . MET   B 1 233 ? -12.345 -21.084 -61.802 1.00 34.39  ? 233 MET   B CB  1 
ATOM   4766 C CG  . MET   B 1 233 ? -11.639 -22.124 -60.956 1.00 38.45  ? 233 MET   B CG  1 
ATOM   4767 S SD  . MET   B 1 233 ? -11.271 -23.690 -61.754 1.00 40.32  ? 233 MET   B SD  1 
ATOM   4768 C CE  . MET   B 1 233 ? -10.170 -23.180 -63.068 1.00 36.51  ? 233 MET   B CE  1 
ATOM   4769 N N   . ALA   B 1 234 ? -13.260 -17.916 -62.331 1.00 37.01  ? 234 ALA   B N   1 
ATOM   4770 C CA  . ALA   B 1 234 ? -14.122 -16.941 -62.976 1.00 39.59  ? 234 ALA   B CA  1 
ATOM   4771 C C   . ALA   B 1 234 ? -13.316 -16.193 -64.029 1.00 40.20  ? 234 ALA   B C   1 
ATOM   4772 O O   . ALA   B 1 234 ? -12.158 -16.523 -64.306 1.00 39.10  ? 234 ALA   B O   1 
ATOM   4773 C CB  . ALA   B 1 234 ? -14.728 -16.000 -61.928 1.00 38.36  ? 234 ALA   B CB  1 
ATOM   4774 N N   . ARG   B 1 235 ? -13.941 -15.177 -64.624 1.00 37.86  ? 235 ARG   B N   1 
ATOM   4775 C CA  . ARG   B 1 235 ? -13.253 -14.267 -65.526 1.00 40.62  ? 235 ARG   B CA  1 
ATOM   4776 C C   . ARG   B 1 235 ? -12.984 -12.904 -64.907 1.00 42.62  ? 235 ARG   B C   1 
ATOM   4777 O O   . ARG   B 1 235 ? -12.314 -12.081 -65.538 1.00 42.58  ? 235 ARG   B O   1 
ATOM   4778 C CB  . ARG   B 1 235 ? -14.056 -14.087 -66.823 1.00 38.14  ? 235 ARG   B CB  1 
ATOM   4779 C CG  . ARG   B 1 235 ? -13.595 -14.994 -67.953 1.00 38.65  ? 235 ARG   B CG  1 
ATOM   4780 C CD  . ARG   B 1 235 ? -14.392 -14.772 -69.228 1.00 40.11  ? 235 ARG   B CD  1 
ATOM   4781 N NE  . ARG   B 1 235 ? -15.809 -14.546 -68.973 1.00 40.87  ? 235 ARG   B NE  1 
ATOM   4782 C CZ  . ARG   B 1 235 ? -16.742 -15.487 -69.032 1.00 38.58  ? 235 ARG   B CZ  1 
ATOM   4783 N NH1 . ARG   B 1 235 ? -16.440 -16.742 -69.321 1.00 38.70  ? 235 ARG   B NH1 1 
ATOM   4784 N NH2 . ARG   B 1 235 ? -18.009 -15.159 -68.797 1.00 36.78  ? 235 ARG   B NH2 1 
ATOM   4785 N N   . THR   B 1 236 ? -13.493 -12.639 -63.707 1.00 40.12  ? 236 THR   B N   1 
ATOM   4786 C CA  . THR   B 1 236 ? -13.289 -11.371 -63.023 1.00 44.45  ? 236 THR   B CA  1 
ATOM   4787 C C   . THR   B 1 236 ? -12.960 -11.624 -61.559 1.00 44.02  ? 236 THR   B C   1 
ATOM   4788 O O   . THR   B 1 236 ? -13.406 -12.622 -60.980 1.00 41.31  ? 236 THR   B O   1 
ATOM   4789 C CB  . THR   B 1 236 ? -14.522 -10.452 -63.113 1.00 39.69  ? 236 THR   B CB  1 
ATOM   4790 O OG1 . THR   B 1 236 ? -15.487 -10.838 -62.125 1.00 38.31  ? 236 THR   B OG1 1 
ATOM   4791 C CG2 . THR   B 1 236 ? -15.155 -10.496 -64.502 1.00 39.11  ? 236 THR   B CG2 1 
ATOM   4792 N N   . PRO   B 1 237 ? -12.179 -10.736 -60.938 1.00 41.70  ? 237 PRO   B N   1 
ATOM   4793 C CA  . PRO   B 1 237 ? -11.893 -10.895 -59.504 1.00 39.76  ? 237 PRO   B CA  1 
ATOM   4794 C C   . PRO   B 1 237 ? -13.113 -10.721 -58.617 1.00 41.06  ? 237 PRO   B C   1 
ATOM   4795 O O   . PRO   B 1 237 ? -13.189 -11.365 -57.562 1.00 37.88  ? 237 PRO   B O   1 
ATOM   4796 C CB  . PRO   B 1 237 ? -10.843 -9.807  -59.235 1.00 40.20  ? 237 PRO   B CB  1 
ATOM   4797 C CG  . PRO   B 1 237 ? -11.054 -8.809  -60.328 1.00 41.08  ? 237 PRO   B CG  1 
ATOM   4798 C CD  . PRO   B 1 237 ? -11.406 -9.632  -61.528 1.00 43.66  ? 237 PRO   B CD  1 
ATOM   4799 N N   . ALA   B 1 238 ? -14.066 -9.867  -59.002 1.00 39.35  ? 238 ALA   B N   1 
ATOM   4800 C CA  . ALA   B 1 238 ? -15.243 -9.657  -58.165 1.00 39.43  ? 238 ALA   B CA  1 
ATOM   4801 C C   . ALA   B 1 238 ? -16.137 -10.889 -58.138 1.00 40.88  ? 238 ALA   B C   1 
ATOM   4802 O O   . ALA   B 1 238 ? -16.846 -11.119 -57.152 1.00 39.64  ? 238 ALA   B O   1 
ATOM   4803 C CB  . ALA   B 1 238 ? -16.030 -8.440  -58.650 1.00 38.51  ? 238 ALA   B CB  1 
ATOM   4804 N N   . ASP   B 1 239 ? -16.119 -11.687 -59.209 1.00 40.09  ? 239 ASP   B N   1 
ATOM   4805 C CA  . ASP   B 1 239 ? -16.862 -12.942 -59.209 1.00 38.75  ? 239 ASP   B CA  1 
ATOM   4806 C C   . ASP   B 1 239 ? -16.264 -13.932 -58.215 1.00 39.49  ? 239 ASP   B C   1 
ATOM   4807 O O   . ASP   B 1 239 ? -17.001 -14.639 -57.516 1.00 36.79  ? 239 ASP   B O   1 
ATOM   4808 C CB  . ASP   B 1 239 ? -16.882 -13.536 -60.617 1.00 40.08  ? 239 ASP   B CB  1 
ATOM   4809 C CG  . ASP   B 1 239 ? -17.981 -12.954 -61.488 1.00 44.13  ? 239 ASP   B CG  1 
ATOM   4810 O OD1 . ASP   B 1 239 ? -18.089 -13.369 -62.664 1.00 46.56  ? 239 ASP   B OD1 1 
ATOM   4811 O OD2 . ASP   B 1 239 ? -18.736 -12.084 -61.004 1.00 48.14  ? 239 ASP   B OD2 1 
ATOM   4812 N N   . LEU   B 1 240 ? -14.931 -13.993 -58.131 1.00 38.87  ? 240 LEU   B N   1 
ATOM   4813 C CA  . LEU   B 1 240 ? -14.292 -14.855 -57.141 1.00 36.55  ? 240 LEU   B CA  1 
ATOM   4814 C C   . LEU   B 1 240 ? -14.632 -14.414 -55.723 1.00 38.64  ? 240 LEU   B C   1 
ATOM   4815 O O   . LEU   B 1 240 ? -14.904 -15.251 -54.854 1.00 36.85  ? 240 LEU   B O   1 
ATOM   4816 C CB  . LEU   B 1 240 ? -12.777 -14.862 -57.337 1.00 34.96  ? 240 LEU   B CB  1 
ATOM   4817 C CG  . LEU   B 1 240 ? -12.246 -15.224 -58.722 1.00 38.59  ? 240 LEU   B CG  1 
ATOM   4818 C CD1 . LEU   B 1 240 ? -10.799 -14.778 -58.868 1.00 37.30  ? 240 LEU   B CD1 1 
ATOM   4819 C CD2 . LEU   B 1 240 ? -12.391 -16.716 -58.981 1.00 37.69  ? 240 LEU   B CD2 1 
ATOM   4820 N N   . ALA   B 1 241 ? -14.613 -13.101 -55.470 1.00 38.76  ? 241 ALA   B N   1 
ATOM   4821 C CA  . ALA   B 1 241 ? -14.932 -12.594 -54.140 1.00 37.97  ? 241 ALA   B CA  1 
ATOM   4822 C C   . ALA   B 1 241 ? -16.337 -12.999 -53.716 1.00 37.06  ? 241 ALA   B C   1 
ATOM   4823 O O   . ALA   B 1 241 ? -16.554 -13.418 -52.572 1.00 38.21  ? 241 ALA   B O   1 
ATOM   4824 C CB  . ALA   B 1 241 ? -14.781 -11.073 -54.109 1.00 34.15  ? 241 ALA   B CB  1 
ATOM   4825 N N   . LEU   B 1 242 ? -17.304 -12.887 -54.628 1.00 35.49  ? 242 LEU   B N   1 
ATOM   4826 C CA  . LEU   B 1 242 ? -18.674 -13.272 -54.308 1.00 37.89  ? 242 LEU   B CA  1 
ATOM   4827 C C   . LEU   B 1 242 ? -18.791 -14.780 -54.108 1.00 36.96  ? 242 LEU   B C   1 
ATOM   4828 O O   . LEU   B 1 242 ? -19.421 -15.242 -53.150 1.00 36.81  ? 242 LEU   B O   1 
ATOM   4829 C CB  . LEU   B 1 242 ? -19.619 -12.795 -55.411 1.00 38.21  ? 242 LEU   B CB  1 
ATOM   4830 C CG  . LEU   B 1 242 ? -21.086 -13.191 -55.245 1.00 39.02  ? 242 LEU   B CG  1 
ATOM   4831 C CD1 . LEU   B 1 242 ? -21.621 -12.703 -53.910 1.00 35.01  ? 242 LEU   B CD1 1 
ATOM   4832 C CD2 . LEU   B 1 242 ? -21.919 -12.644 -56.395 1.00 36.99  ? 242 LEU   B CD2 1 
ATOM   4833 N N   . ALA   B 1 243 ? -18.189 -15.564 -55.006 1.00 35.41  ? 243 ALA   B N   1 
ATOM   4834 C CA  . ALA   B 1 243 ? -18.237 -17.015 -54.864 1.00 36.13  ? 243 ALA   B CA  1 
ATOM   4835 C C   . ALA   B 1 243 ? -17.561 -17.463 -53.575 1.00 38.57  ? 243 ALA   B C   1 
ATOM   4836 O O   . ALA   B 1 243 ? -18.013 -18.412 -52.923 1.00 40.28  ? 243 ALA   B O   1 
ATOM   4837 C CB  . ALA   B 1 243 ? -17.587 -17.680 -56.076 1.00 36.17  ? 243 ALA   B CB  1 
ATOM   4838 N N   . LEU   B 1 244 ? -16.482 -16.782 -53.185 1.00 39.36  ? 244 LEU   B N   1 
ATOM   4839 C CA  . LEU   B 1 244 ? -15.784 -17.134 -51.953 1.00 42.08  ? 244 LEU   B CA  1 
ATOM   4840 C C   . LEU   B 1 244 ? -16.646 -16.849 -50.726 1.00 39.15  ? 244 LEU   B C   1 
ATOM   4841 O O   . LEU   B 1 244 ? -16.684 -17.653 -49.789 1.00 39.49  ? 244 LEU   B O   1 
ATOM   4842 C CB  . LEU   B 1 244 ? -14.453 -16.382 -51.883 1.00 39.11  ? 244 LEU   B CB  1 
ATOM   4843 C CG  . LEU   B 1 244 ? -13.602 -16.494 -50.618 1.00 37.99  ? 244 LEU   B CG  1 
ATOM   4844 C CD1 . LEU   B 1 244 ? -13.024 -17.887 -50.486 1.00 36.10  ? 244 LEU   B CD1 1 
ATOM   4845 C CD2 . LEU   B 1 244 ? -12.489 -15.455 -50.636 1.00 37.25  ? 244 LEU   B CD2 1 
ATOM   4846 N N   . ASP   B 1 245 ? -17.357 -15.717 -50.719 1.00 41.13  ? 245 ASP   B N   1 
ATOM   4847 C CA  . ASP   B 1 245 ? -18.205 -15.385 -49.577 1.00 41.12  ? 245 ASP   B CA  1 
ATOM   4848 C C   . ASP   B 1 245 ? -19.420 -16.301 -49.485 1.00 39.24  ? 245 ASP   B C   1 
ATOM   4849 O O   . ASP   B 1 245 ? -19.954 -16.511 -48.390 1.00 41.74  ? 245 ASP   B O   1 
ATOM   4850 C CB  . ASP   B 1 245 ? -18.651 -13.924 -49.657 1.00 39.22  ? 245 ASP   B CB  1 
ATOM   4851 C CG  . ASP   B 1 245 ? -17.525 -12.945 -49.336 1.00 43.74  ? 245 ASP   B CG  1 
ATOM   4852 O OD1 . ASP   B 1 245 ? -16.707 -13.238 -48.437 1.00 45.19  ? 245 ASP   B OD1 1 
ATOM   4853 O OD2 . ASP   B 1 245 ? -17.461 -11.876 -49.982 1.00 44.86  ? 245 ASP   B OD2 1 
ATOM   4854 N N   . ILE   B 1 246 ? -19.866 -16.856 -50.613 1.00 40.03  ? 246 ILE   B N   1 
ATOM   4855 C CA  . ILE   B 1 246 ? -21.018 -17.753 -50.597 1.00 38.34  ? 246 ILE   B CA  1 
ATOM   4856 C C   . ILE   B 1 246 ? -20.632 -19.146 -50.099 1.00 37.74  ? 246 ILE   B C   1 
ATOM   4857 O O   . ILE   B 1 246 ? -21.439 -19.822 -49.449 1.00 35.90  ? 246 ILE   B O   1 
ATOM   4858 C CB  . ILE   B 1 246 ? -21.657 -17.809 -51.999 1.00 34.57  ? 246 ILE   B CB  1 
ATOM   4859 C CG1 . ILE   B 1 246 ? -22.314 -16.471 -52.341 1.00 37.29  ? 246 ILE   B CG1 1 
ATOM   4860 C CG2 . ILE   B 1 246 ? -22.685 -18.929 -52.098 1.00 34.26  ? 246 ILE   B CG2 1 
ATOM   4861 C CD1 . ILE   B 1 246 ? -22.570 -16.275 -53.816 1.00 35.97  ? 246 ILE   B CD1 1 
ATOM   4862 N N   . THR   B 1 247 ? -19.399 -19.590 -50.362 1.00 37.33  ? 247 THR   B N   1 
ATOM   4863 C CA  . THR   B 1 247 ? -19.024 -20.981 -50.142 1.00 39.97  ? 247 THR   B CA  1 
ATOM   4864 C C   . THR   B 1 247 ? -18.134 -21.217 -48.930 1.00 38.32  ? 247 THR   B C   1 
ATOM   4865 O O   . THR   B 1 247 ? -18.051 -22.358 -48.470 1.00 39.87  ? 247 THR   B O   1 
ATOM   4866 C CB  . THR   B 1 247 ? -18.311 -21.545 -51.382 1.00 37.23  ? 247 THR   B CB  1 
ATOM   4867 O OG1 . THR   B 1 247 ? -17.161 -20.747 -51.683 1.00 34.00  ? 247 THR   B OG1 1 
ATOM   4868 C CG2 . THR   B 1 247 ? -19.246 -21.541 -52.582 1.00 38.74  ? 247 THR   B CG2 1 
ATOM   4869 N N   . SER   B 1 248 ? -17.466 -20.190 -48.408 1.00 37.66  ? 248 SER   B N   1 
ATOM   4870 C CA  . SER   B 1 248 ? -16.551 -20.392 -47.292 1.00 38.84  ? 248 SER   B CA  1 
ATOM   4871 C C   . SER   B 1 248 ? -17.308 -20.809 -46.033 1.00 37.42  ? 248 SER   B C   1 
ATOM   4872 O O   . SER   B 1 248 ? -18.465 -20.433 -45.824 1.00 38.57  ? 248 SER   B O   1 
ATOM   4873 C CB  . SER   B 1 248 ? -15.745 -19.120 -47.024 1.00 38.04  ? 248 SER   B CB  1 
ATOM   4874 O OG  . SER   B 1 248 ? -16.592 -18.041 -46.672 1.00 43.98  ? 248 SER   B OG  1 
ATOM   4875 N N   . LYS   B 1 249 ? -16.636 -21.609 -45.193 1.00 42.36  ? 249 LYS   B N   1 
ATOM   4876 C CA  . LYS   B 1 249 ? -17.238 -22.074 -43.943 1.00 37.90  ? 249 LYS   B CA  1 
ATOM   4877 C C   . LYS   B 1 249 ? -17.727 -20.906 -43.101 1.00 39.62  ? 249 LYS   B C   1 
ATOM   4878 O O   . LYS   B 1 249 ? -18.757 -20.997 -42.423 1.00 38.63  ? 249 LYS   B O   1 
ATOM   4879 C CB  . LYS   B 1 249 ? -16.231 -22.890 -43.130 1.00 36.39  ? 249 LYS   B CB  1 
ATOM   4880 C CG  . LYS   B 1 249 ? -15.673 -24.128 -43.798 1.00 38.89  ? 249 LYS   B CG  1 
ATOM   4881 C CD  . LYS   B 1 249 ? -14.681 -24.814 -42.867 1.00 40.56  ? 249 LYS   B CD  1 
ATOM   4882 C CE  . LYS   B 1 249 ? -14.128 -26.090 -43.480 1.00 41.72  ? 249 LYS   B CE  1 
ATOM   4883 N NZ  . LYS   B 1 249 ? -12.881 -26.534 -42.802 1.00 43.04  ? 249 LYS   B NZ  1 
ATOM   4884 N N   . VAL   B 1 250 ? -16.988 -19.803 -43.129 1.00 37.48  ? 250 VAL   B N   1 
ATOM   4885 C CA  . VAL   B 1 250 ? -17.269 -18.619 -42.329 1.00 39.81  ? 250 VAL   B CA  1 
ATOM   4886 C C   . VAL   B 1 250 ? -16.895 -17.420 -43.193 1.00 43.69  ? 250 VAL   B C   1 
ATOM   4887 O O   . VAL   B 1 250 ? -15.922 -17.500 -43.959 1.00 40.76  ? 250 VAL   B O   1 
ATOM   4888 C CB  . VAL   B 1 250 ? -16.495 -18.661 -41.000 1.00 39.54  ? 250 VAL   B CB  1 
ATOM   4889 C CG1 . VAL   B 1 250 ? -15.742 -17.360 -40.746 1.00 42.06  ? 250 VAL   B CG1 1 
ATOM   4890 C CG2 . VAL   B 1 250 ? -17.431 -18.995 -39.850 1.00 42.04  ? 250 VAL   B CG2 1 
ATOM   4891 N N   . PRO   B 1 251 ? -17.650 -16.320 -43.145 1.00 42.91  ? 251 PRO   B N   1 
ATOM   4892 C CA  . PRO   B 1 251 ? -17.283 -15.127 -43.927 1.00 42.32  ? 251 PRO   B CA  1 
ATOM   4893 C C   . PRO   B 1 251 ? -15.857 -14.682 -43.635 1.00 43.12  ? 251 PRO   B C   1 
ATOM   4894 O O   . PRO   B 1 251 ? -15.519 -14.300 -42.512 1.00 43.93  ? 251 PRO   B O   1 
ATOM   4895 C CB  . PRO   B 1 251 ? -18.311 -14.086 -43.471 1.00 39.70  ? 251 PRO   B CB  1 
ATOM   4896 C CG  . PRO   B 1 251 ? -19.495 -14.909 -43.079 1.00 40.92  ? 251 PRO   B CG  1 
ATOM   4897 C CD  . PRO   B 1 251 ? -18.925 -16.136 -42.430 1.00 39.23  ? 251 PRO   B CD  1 
ATOM   4898 N N   . LEU   B 1 252 ? -15.015 -14.743 -44.663 1.00 42.15  ? 252 LEU   B N   1 
ATOM   4899 C CA  . LEU   B 1 252 ? -13.616 -14.388 -44.507 1.00 40.79  ? 252 LEU   B CA  1 
ATOM   4900 C C   . LEU   B 1 252 ? -13.472 -12.871 -44.394 1.00 41.12  ? 252 LEU   B C   1 
ATOM   4901 O O   . LEU   B 1 252 ? -14.335 -12.123 -44.863 1.00 45.71  ? 252 LEU   B O   1 
ATOM   4902 C CB  . LEU   B 1 252 ? -12.808 -14.910 -45.691 1.00 40.34  ? 252 LEU   B CB  1 
ATOM   4903 C CG  . LEU   B 1 252 ? -12.723 -16.433 -45.808 1.00 42.80  ? 252 LEU   B CG  1 
ATOM   4904 C CD1 . LEU   B 1 252 ? -11.814 -16.827 -46.954 1.00 42.06  ? 252 LEU   B CD1 1 
ATOM   4905 C CD2 . LEU   B 1 252 ? -12.226 -17.045 -44.510 1.00 39.91  ? 252 LEU   B CD2 1 
ATOM   4906 N N   . PRO   B 1 253 ? -12.399 -12.389 -43.765 1.00 41.56  ? 253 PRO   B N   1 
ATOM   4907 C CA  . PRO   B 1 253 ? -12.226 -10.938 -43.620 1.00 40.62  ? 253 PRO   B CA  1 
ATOM   4908 C C   . PRO   B 1 253 ? -12.069 -10.250 -44.971 1.00 43.13  ? 253 PRO   B C   1 
ATOM   4909 O O   . PRO   B 1 253 ? -11.291 -10.682 -45.824 1.00 41.10  ? 253 PRO   B O   1 
ATOM   4910 C CB  . PRO   B 1 253 ? -10.956 -10.817 -42.768 1.00 42.12  ? 253 PRO   B CB  1 
ATOM   4911 C CG  . PRO   B 1 253 ? -10.243 -12.119 -42.952 1.00 41.62  ? 253 PRO   B CG  1 
ATOM   4912 C CD  . PRO   B 1 253 ? -11.330 -13.139 -43.081 1.00 43.50  ? 253 PRO   B CD  1 
ATOM   4913 N N   . GLN   B 1 254 ? -12.826 -9.170  -45.157 1.00 46.48  ? 254 GLN   B N   1 
ATOM   4914 C CA  . GLN   B 1 254 ? -12.747 -8.385  -46.381 1.00 45.53  ? 254 GLN   B CA  1 
ATOM   4915 C C   . GLN   B 1 254 ? -11.424 -7.630  -46.454 1.00 46.58  ? 254 GLN   B C   1 
ATOM   4916 O O   . GLN   B 1 254 ? -10.824 -7.275  -45.434 1.00 50.49  ? 254 GLN   B O   1 
ATOM   4917 C CB  . GLN   B 1 254 ? -13.913 -7.397  -46.458 1.00 44.49  ? 254 GLN   B CB  1 
ATOM   4918 C CG  . GLN   B 1 254 ? -15.216 -7.996  -46.962 1.00 44.07  ? 254 GLN   B CG  1 
ATOM   4919 C CD  . GLN   B 1 254 ? -15.029 -8.828  -48.215 1.00 50.33  ? 254 GLN   B CD  1 
ATOM   4920 O OE1 . GLN   B 1 254 ? -15.366 -10.011 -48.244 1.00 51.56  ? 254 GLN   B OE1 1 
ATOM   4921 N NE2 . GLN   B 1 254 ? -14.492 -8.211  -49.262 1.00 53.12  ? 254 GLN   B NE2 1 
ATOM   4922 N N   . SER   B 1 255 ? -10.977 -7.373  -47.679 1.00 45.60  ? 255 SER   B N   1 
ATOM   4923 C CA  . SER   B 1 255 ? -9.703  -6.701  -47.895 1.00 44.36  ? 255 SER   B CA  1 
ATOM   4924 C C   . SER   B 1 255 ? -9.817  -5.208  -47.619 1.00 47.64  ? 255 SER   B C   1 
ATOM   4925 O O   . SER   B 1 255 ? -10.834 -4.578  -47.922 1.00 48.12  ? 255 SER   B O   1 
ATOM   4926 C CB  . SER   B 1 255 ? -9.219  -6.927  -49.326 1.00 44.32  ? 255 SER   B CB  1 
ATOM   4927 O OG  . SER   B 1 255 ? -8.069  -6.148  -49.598 1.00 42.79  ? 255 SER   B OG  1 
ATOM   4928 N N   . ARG   B 1 256 ? -8.756  -4.644  -47.043 1.00 47.86  ? 256 ARG   B N   1 
ATOM   4929 C CA  . ARG   B 1 256 ? -8.663  -3.215  -46.778 1.00 48.82  ? 256 ARG   B CA  1 
ATOM   4930 C C   . ARG   B 1 256 ? -7.725  -2.508  -47.750 1.00 52.22  ? 256 ARG   B C   1 
ATOM   4931 O O   . ARG   B 1 256 ? -7.457  -1.314  -47.579 1.00 54.56  ? 256 ARG   B O   1 
ATOM   4932 C CB  . ARG   B 1 256 ? -8.195  -2.975  -45.341 1.00 50.15  ? 256 ARG   B CB  1 
ATOM   4933 C CG  . ARG   B 1 256 ? -9.194  -3.392  -44.277 1.00 52.77  ? 256 ARG   B CG  1 
ATOM   4934 C CD  . ARG   B 1 256 ? -10.291 -2.359  -44.091 1.00 59.04  ? 256 ARG   B CD  1 
ATOM   4935 N NE  . ARG   B 1 256 ? -11.512 -2.959  -43.566 1.00 61.79  ? 256 ARG   B NE  1 
ATOM   4936 C CZ  . ARG   B 1 256 ? -12.493 -3.446  -44.315 1.00 65.32  ? 256 ARG   B CZ  1 
ATOM   4937 N NH1 . ARG   B 1 256 ? -12.446 -3.394  -45.638 1.00 56.98  ? 256 ARG   B NH1 1 
ATOM   4938 N NH2 . ARG   B 1 256 ? -13.550 -3.995  -43.722 1.00 60.27  ? 256 ARG   B NH2 1 
ATOM   4939 N N   . ILE   B 1 257 ? -7.216  -3.214  -48.756 1.00 47.65  ? 257 ILE   B N   1 
ATOM   4940 C CA  . ILE   B 1 257 ? -6.271  -2.644  -49.712 1.00 52.81  ? 257 ILE   B CA  1 
ATOM   4941 C C   . ILE   B 1 257 ? -7.051  -1.833  -50.741 1.00 51.68  ? 257 ILE   B C   1 
ATOM   4942 O O   . ILE   B 1 257 ? -7.738  -2.396  -51.595 1.00 49.63  ? 257 ILE   B O   1 
ATOM   4943 C CB  . ILE   B 1 257 ? -5.431  -3.733  -50.390 1.00 52.38  ? 257 ILE   B CB  1 
ATOM   4944 C CG1 . ILE   B 1 257 ? -4.981  -4.784  -49.373 1.00 48.77  ? 257 ILE   B CG1 1 
ATOM   4945 C CG2 . ILE   B 1 257 ? -4.238  -3.127  -51.114 1.00 48.23  ? 257 ILE   B CG2 1 
ATOM   4946 C CD1 . ILE   B 1 257 ? -4.640  -6.117  -49.999 1.00 48.36  ? 257 ILE   B CD1 1 
ATOM   4947 N N   . ALA   B 1 258 ? -6.938  -0.505  -50.672 1.00 52.97  ? 258 ALA   B N   1 
ATOM   4948 C CA  . ALA   B 1 258 ? -7.615  0.353   -51.639 1.00 53.19  ? 258 ALA   B CA  1 
ATOM   4949 C C   . ALA   B 1 258 ? -6.802  0.572   -52.906 1.00 52.06  ? 258 ALA   B C   1 
ATOM   4950 O O   . ALA   B 1 258 ? -7.382  0.830   -53.966 1.00 54.00  ? 258 ALA   B O   1 
ATOM   4951 C CB  . ALA   B 1 258 ? -7.951  1.707   -51.010 1.00 52.10  ? 258 ALA   B CB  1 
ATOM   4952 N N   . ASN   B 1 259 ? -5.479  0.469   -52.826 1.00 52.47  ? 259 ASN   B N   1 
ATOM   4953 C CA  . ASN   B 1 259 ? -4.622  0.692   -53.982 1.00 52.55  ? 259 ASN   B CA  1 
ATOM   4954 C C   . ASN   B 1 259 ? -3.260  0.066   -53.706 1.00 54.81  ? 259 ASN   B C   1 
ATOM   4955 O O   . ASN   B 1 259 ? -3.019  -0.510  -52.642 1.00 53.33  ? 259 ASN   B O   1 
ATOM   4956 C CB  . ASN   B 1 259 ? -4.505  2.185   -54.299 1.00 52.64  ? 259 ASN   B CB  1 
ATOM   4957 C CG  . ASN   B 1 259 ? -4.083  2.994   -53.097 1.00 52.49  ? 259 ASN   B CG  1 
ATOM   4958 O OD1 . ASN   B 1 259 ? -2.895  3.113   -52.801 1.00 55.03  ? 259 ASN   B OD1 1 
ATOM   4959 N ND2 . ASN   B 1 259 ? -5.058  3.556   -52.392 1.00 50.01  ? 259 ASN   B ND2 1 
ATOM   4960 N N   . LEU   B 1 260 ? -2.362  0.200   -54.681 1.00 51.68  ? 260 LEU   B N   1 
ATOM   4961 C CA  . LEU   B 1 260 ? -1.082  -0.495  -54.658 1.00 55.24  ? 260 LEU   B CA  1 
ATOM   4962 C C   . LEU   B 1 260 ? 0.013   0.266   -53.923 1.00 57.00  ? 260 LEU   B C   1 
ATOM   4963 O O   . LEU   B 1 260 ? 1.036   -0.337  -53.582 1.00 55.67  ? 260 LEU   B O   1 
ATOM   4964 C CB  . LEU   B 1 260 ? -0.625  -0.780  -56.092 1.00 56.44  ? 260 LEU   B CB  1 
ATOM   4965 C CG  . LEU   B 1 260 ? -1.350  -1.937  -56.779 1.00 55.79  ? 260 LEU   B CG  1 
ATOM   4966 C CD1 . LEU   B 1 260 ? -1.036  -1.986  -58.269 1.00 53.16  ? 260 LEU   B CD1 1 
ATOM   4967 C CD2 . LEU   B 1 260 ? -1.005  -3.257  -56.108 1.00 51.45  ? 260 LEU   B CD2 1 
ATOM   4968 N N   . SER   B 1 261 ? -0.172  1.561   -53.671 1.00 55.44  ? 261 SER   B N   1 
ATOM   4969 C CA  . SER   B 1 261 ? 0.864   2.361   -53.026 1.00 57.62  ? 261 SER   B CA  1 
ATOM   4970 C C   . SER   B 1 261 ? 1.092   1.875   -51.599 1.00 55.13  ? 261 SER   B C   1 
ATOM   4971 O O   . SER   B 1 261 ? 0.167   1.872   -50.780 1.00 56.84  ? 261 SER   B O   1 
ATOM   4972 C CB  . SER   B 1 261 ? 0.475   3.837   -53.032 1.00 56.22  ? 261 SER   B CB  1 
ATOM   4973 O OG  . SER   B 1 261 ? -0.200  4.193   -51.839 1.00 53.77  ? 261 SER   B OG  1 
ATOM   4974 N N   . GLY   B 1 262 ? 2.328   1.482   -51.297 1.00 52.39  ? 262 GLY   B N   1 
ATOM   4975 C CA  . GLY   B 1 262 ? 2.681   0.949   -49.999 1.00 55.10  ? 262 GLY   B CA  1 
ATOM   4976 C C   . GLY   B 1 262 ? 2.695   -0.562  -49.916 1.00 54.36  ? 262 GLY   B C   1 
ATOM   4977 O O   . GLY   B 1 262 ? 3.146   -1.105  -48.900 1.00 54.21  ? 262 GLY   B O   1 
ATOM   4978 N N   . LEU   B 1 263 ? 2.214   -1.254  -50.946 1.00 54.14  ? 263 LEU   B N   1 
ATOM   4979 C CA  . LEU   B 1 263 ? 2.193   -2.710  -50.930 1.00 55.17  ? 263 LEU   B CA  1 
ATOM   4980 C C   . LEU   B 1 263 ? 3.611   -3.257  -51.023 1.00 54.29  ? 263 LEU   B C   1 
ATOM   4981 O O   . LEU   B 1 263 ? 4.375   -2.881  -51.917 1.00 56.21  ? 263 LEU   B O   1 
ATOM   4982 C CB  . LEU   B 1 263 ? 1.345   -3.240  -52.087 1.00 55.93  ? 263 LEU   B CB  1 
ATOM   4983 C CG  . LEU   B 1 263 ? 0.532   -4.513  -51.830 1.00 55.55  ? 263 LEU   B CG  1 
ATOM   4984 C CD1 . LEU   B 1 263 ? -0.663  -4.229  -50.934 1.00 47.92  ? 263 LEU   B CD1 1 
ATOM   4985 C CD2 . LEU   B 1 263 ? 0.084   -5.138  -53.144 1.00 51.22  ? 263 LEU   B CD2 1 
ATOM   4986 N N   . ARG   B 1 264 ? 3.967   -4.140  -50.095 1.00 51.18  ? 264 ARG   B N   1 
ATOM   4987 C CA  . ARG   B 1 264 ? 5.260   -4.811  -50.126 1.00 53.48  ? 264 ARG   B CA  1 
ATOM   4988 C C   . ARG   B 1 264 ? 5.126   -6.129  -50.879 1.00 52.06  ? 264 ARG   B C   1 
ATOM   4989 O O   . ARG   B 1 264 ? 4.406   -7.033  -50.443 1.00 50.97  ? 264 ARG   B O   1 
ATOM   4990 C CB  . ARG   B 1 264 ? 5.793   -5.039  -48.712 1.00 52.98  ? 264 ARG   B CB  1 
ATOM   4991 C CG  . ARG   B 1 264 ? 5.790   -3.791  -47.835 1.00 56.49  ? 264 ARG   B CG  1 
ATOM   4992 C CD  . ARG   B 1 264 ? 5.795   -4.165  -46.361 1.00 55.95  ? 264 ARG   B CD  1 
ATOM   4993 N NE  . ARG   B 1 264 ? 4.520   -4.743  -45.955 1.00 55.92  ? 264 ARG   B NE  1 
ATOM   4994 C CZ  . ARG   B 1 264 ? 4.302   -5.335  -44.790 1.00 57.77  ? 264 ARG   B CZ  1 
ATOM   4995 N NH1 . ARG   B 1 264 ? 5.264   -5.464  -43.890 1.00 58.16  ? 264 ARG   B NH1 1 
ATOM   4996 N NH2 . ARG   B 1 264 ? 3.092   -5.819  -44.524 1.00 54.25  ? 264 ARG   B NH2 1 
ATOM   4997 N N   . ILE   B 1 265 ? 5.820   -6.232  -52.009 1.00 52.80  ? 265 ILE   B N   1 
ATOM   4998 C CA  . ILE   B 1 265 ? 5.784   -7.412  -52.865 1.00 50.40  ? 265 ILE   B CA  1 
ATOM   4999 C C   . ILE   B 1 265 ? 7.154   -8.073  -52.829 1.00 54.06  ? 265 ILE   B C   1 
ATOM   5000 O O   . ILE   B 1 265 ? 8.184   -7.387  -52.846 1.00 54.30  ? 265 ILE   B O   1 
ATOM   5001 C CB  . ILE   B 1 265 ? 5.392   -7.041  -54.310 1.00 49.86  ? 265 ILE   B CB  1 
ATOM   5002 C CG1 . ILE   B 1 265 ? 3.929   -6.601  -54.371 1.00 49.90  ? 265 ILE   B CG1 1 
ATOM   5003 C CG2 . ILE   B 1 265 ? 5.635   -8.207  -55.260 1.00 49.10  ? 265 ILE   B CG2 1 
ATOM   5004 C CD1 . ILE   B 1 265 ? 3.616   -5.713  -55.551 1.00 44.73  ? 265 ILE   B CD1 1 
ATOM   5005 N N   . LEU   B 1 266 ? 7.170   -9.403  -52.762 1.00 51.72  ? 266 LEU   B N   1 
ATOM   5006 C CA  . LEU   B 1 266 ? 8.392   -10.179 -52.943 1.00 52.16  ? 266 LEU   B CA  1 
ATOM   5007 C C   . LEU   B 1 266 ? 8.260   -10.946 -54.255 1.00 53.25  ? 266 LEU   B C   1 
ATOM   5008 O O   . LEU   B 1 266 ? 7.465   -11.888 -54.350 1.00 53.60  ? 266 LEU   B O   1 
ATOM   5009 C CB  . LEU   B 1 266 ? 8.643   -11.123 -51.767 1.00 49.68  ? 266 LEU   B CB  1 
ATOM   5010 C CG  . LEU   B 1 266 ? 9.825   -12.071 -51.988 1.00 52.76  ? 266 LEU   B CG  1 
ATOM   5011 C CD1 . LEU   B 1 266 ? 11.142  -11.328 -51.848 1.00 55.17  ? 266 LEU   B CD1 1 
ATOM   5012 C CD2 . LEU   B 1 266 ? 9.779   -13.249 -51.027 1.00 54.18  ? 266 LEU   B CD2 1 
ATOM   5013 N N   . LEU   B 1 267 ? 9.028   -10.536 -55.264 1.00 52.30  ? 267 LEU   B N   1 
ATOM   5014 C CA  . LEU   B 1 267 ? 8.972   -11.158 -56.582 1.00 49.98  ? 267 LEU   B CA  1 
ATOM   5015 C C   . LEU   B 1 267 ? 9.992   -12.289 -56.644 1.00 57.37  ? 267 LEU   B C   1 
ATOM   5016 O O   . LEU   B 1 267 ? 11.186  -12.073 -56.404 1.00 58.70  ? 267 LEU   B O   1 
ATOM   5017 C CB  . LEU   B 1 267 ? 9.229   -10.133 -57.691 1.00 54.59  ? 267 LEU   B CB  1 
ATOM   5018 C CG  . LEU   B 1 267 ? 9.558   -10.629 -59.113 1.00 59.12  ? 267 LEU   B CG  1 
ATOM   5019 C CD1 . LEU   B 1 267 ? 8.964   -9.674  -60.120 1.00 57.00  ? 267 LEU   B CD1 1 
ATOM   5020 C CD2 . LEU   B 1 267 ? 11.055  -10.777 -59.387 1.00 58.24  ? 267 LEU   B CD2 1 
ATOM   5021 N N   . LEU   B 1 268 ? 9.521   -13.493 -56.952 1.00 54.98  ? 268 LEU   B N   1 
ATOM   5022 C CA  . LEU   B 1 268 ? 10.389  -14.620 -57.265 1.00 54.79  ? 268 LEU   B CA  1 
ATOM   5023 C C   . LEU   B 1 268 ? 10.195  -15.005 -58.722 1.00 56.99  ? 268 LEU   B C   1 
ATOM   5024 O O   . LEU   B 1 268 ? 9.059   -15.133 -59.191 1.00 56.69  ? 268 LEU   B O   1 
ATOM   5025 C CB  . LEU   B 1 268 ? 10.111  -15.824 -56.363 1.00 54.07  ? 268 LEU   B CB  1 
ATOM   5026 C CG  . LEU   B 1 268 ? 9.710   -15.588 -54.911 1.00 55.30  ? 268 LEU   B CG  1 
ATOM   5027 C CD1 . LEU   B 1 268 ? 9.575   -16.918 -54.184 1.00 52.72  ? 268 LEU   B CD1 1 
ATOM   5028 C CD2 . LEU   B 1 268 ? 10.748  -14.720 -54.233 1.00 56.77  ? 268 LEU   B CD2 1 
ATOM   5029 N N   . THR   B 1 269 ? 11.302  -15.166 -59.437 1.00 58.79  ? 269 THR   B N   1 
ATOM   5030 C CA  . THR   B 1 269 ? 11.279  -15.684 -60.794 1.00 57.41  ? 269 THR   B CA  1 
ATOM   5031 C C   . THR   B 1 269 ? 12.163  -16.910 -60.948 1.00 60.42  ? 269 THR   B C   1 
ATOM   5032 O O   . THR   B 1 269 ? 12.244  -17.466 -62.050 1.00 62.22  ? 269 THR   B O   1 
ATOM   5033 C CB  . THR   B 1 269 ? 11.708  -14.600 -61.792 1.00 57.24  ? 269 THR   B CB  1 
ATOM   5034 O OG1 . THR   B 1 269 ? 12.958  -14.035 -61.378 1.00 59.34  ? 269 THR   B OG1 1 
ATOM   5035 C CG2 . THR   B 1 269 ? 10.657  -13.496 -61.864 1.00 59.26  ? 269 THR   B CG2 1 
ATOM   5036 N N   . ALA   B 1 270 ? 12.820  -17.345 -59.877 1.00 57.65  ? 270 ALA   B N   1 
ATOM   5037 C CA  . ALA   B 1 270 ? 13.657  -18.532 -59.882 1.00 57.73  ? 270 ALA   B CA  1 
ATOM   5038 C C   . ALA   B 1 270 ? 13.304  -19.390 -58.676 1.00 56.30  ? 270 ALA   B C   1 
ATOM   5039 O O   . ALA   B 1 270 ? 12.768  -18.904 -57.677 1.00 59.58  ? 270 ALA   B O   1 
ATOM   5040 C CB  . ALA   B 1 270 ? 15.148  -18.173 -59.863 1.00 56.40  ? 270 ALA   B CB  1 
ATOM   5041 N N   . HIS   B 1 271 ? 13.615  -20.682 -58.784 1.00 52.04  ? 271 HIS   B N   1 
ATOM   5042 C CA  . HIS   B 1 271 ? 13.292  -21.652 -57.755 1.00 55.54  ? 271 HIS   B CA  1 
ATOM   5043 C C   . HIS   B 1 271 ? 14.431  -22.663 -57.740 1.00 55.81  ? 271 HIS   B C   1 
ATOM   5044 O O   . HIS   B 1 271 ? 14.826  -23.145 -58.813 1.00 55.66  ? 271 HIS   B O   1 
ATOM   5045 C CB  . HIS   B 1 271 ? 11.951  -22.341 -58.025 1.00 52.17  ? 271 HIS   B CB  1 
ATOM   5046 C CG  . HIS   B 1 271 ? 11.550  -23.337 -56.981 1.00 53.30  ? 271 HIS   B CG  1 
ATOM   5047 N ND1 . HIS   B 1 271 ? 12.251  -24.501 -56.750 1.00 53.85  ? 271 HIS   B ND1 1 
ATOM   5048 C CD2 . HIS   B 1 271 ? 10.513  -23.344 -56.109 1.00 51.93  ? 271 HIS   B CD2 1 
ATOM   5049 C CE1 . HIS   B 1 271 ? 11.666  -25.181 -55.780 1.00 53.45  ? 271 HIS   B CE1 1 
ATOM   5050 N NE2 . HIS   B 1 271 ? 10.610  -24.501 -55.373 1.00 54.54  ? 271 HIS   B NE2 1 
ATOM   5051 N N   . PRO   B 1 272 ? 14.973  -22.999 -56.567 1.00 54.64  ? 272 PRO   B N   1 
ATOM   5052 C CA  . PRO   B 1 272 ? 16.206  -23.807 -56.527 1.00 55.81  ? 272 PRO   B CA  1 
ATOM   5053 C C   . PRO   B 1 272 ? 16.082  -25.191 -57.146 1.00 57.17  ? 272 PRO   B C   1 
ATOM   5054 O O   . PRO   B 1 272 ? 17.114  -25.815 -57.420 1.00 59.91  ? 272 PRO   B O   1 
ATOM   5055 C CB  . PRO   B 1 272 ? 16.515  -23.898 -55.024 1.00 57.68  ? 272 PRO   B CB  1 
ATOM   5056 C CG  . PRO   B 1 272 ? 15.206  -23.600 -54.348 1.00 58.25  ? 272 PRO   B CG  1 
ATOM   5057 C CD  . PRO   B 1 272 ? 14.552  -22.578 -55.221 1.00 53.51  ? 272 PRO   B CD  1 
ATOM   5058 N N   . GLU   B 1 273 ? 14.871  -25.700 -57.377 1.00 58.45  ? 273 GLU   B N   1 
ATOM   5059 C CA  . GLU   B 1 273 ? 14.706  -27.047 -57.911 1.00 58.72  ? 273 GLU   B CA  1 
ATOM   5060 C C   . GLU   B 1 273 ? 13.936  -27.106 -59.225 1.00 58.10  ? 273 GLU   B C   1 
ATOM   5061 O O   . GLU   B 1 273 ? 13.682  -28.211 -59.719 1.00 60.35  ? 273 GLU   B O   1 
ATOM   5062 C CB  . GLU   B 1 273 ? 14.014  -27.953 -56.883 1.00 56.93  ? 273 GLU   B CB  1 
ATOM   5063 C CG  . GLU   B 1 273 ? 14.688  -28.013 -55.517 1.00 60.14  ? 273 GLU   B CG  1 
ATOM   5064 C CD  . GLU   B 1 273 ? 16.173  -28.321 -55.596 1.00 62.38  ? 273 GLU   B CD  1 
ATOM   5065 O OE1 . GLU   B 1 273 ? 16.536  -29.438 -56.021 1.00 64.18  ? 273 GLU   B OE1 1 
ATOM   5066 O OE2 . GLU   B 1 273 ? 16.981  -27.449 -55.211 1.00 67.64  ? 273 GLU   B OE2 1 
ATOM   5067 N N   . THR   B 1 274 ? 13.556  -25.970 -59.807 1.00 54.02  ? 274 THR   B N   1 
ATOM   5068 C CA  . THR   B 1 274 ? 12.851  -25.971 -61.086 1.00 55.77  ? 274 THR   B CA  1 
ATOM   5069 C C   . THR   B 1 274 ? 13.230  -24.707 -61.856 1.00 56.20  ? 274 THR   B C   1 
ATOM   5070 O O   . THR   B 1 274 ? 14.160  -23.986 -61.481 1.00 58.50  ? 274 THR   B O   1 
ATOM   5071 C CB  . THR   B 1 274 ? 11.334  -26.097 -60.880 1.00 57.40  ? 274 THR   B CB  1 
ATOM   5072 O OG1 . THR   B 1 274 ? 10.678  -26.215 -62.150 1.00 56.36  ? 274 THR   B OG1 1 
ATOM   5073 C CG2 . THR   B 1 274 ? 10.785  -24.888 -60.142 1.00 53.78  ? 274 THR   B CG2 1 
ATOM   5074 N N   . VAL   B 1 275 ? 12.502  -24.439 -62.944 1.00 53.35  ? 275 VAL   B N   1 
ATOM   5075 C CA  . VAL   B 1 275 ? 12.845  -23.369 -63.875 1.00 51.98  ? 275 VAL   B CA  1 
ATOM   5076 C C   . VAL   B 1 275 ? 11.573  -22.837 -64.522 1.00 53.41  ? 275 VAL   B C   1 
ATOM   5077 O O   . VAL   B 1 275 ? 10.547  -23.517 -64.586 1.00 58.68  ? 275 VAL   B O   1 
ATOM   5078 C CB  . VAL   B 1 275 ? 13.846  -23.859 -64.954 1.00 56.48  ? 275 VAL   B CB  1 
ATOM   5079 C CG1 . VAL   B 1 275 ? 13.132  -24.671 -66.025 1.00 54.59  ? 275 VAL   B CG1 1 
ATOM   5080 C CG2 . VAL   B 1 275 ? 14.599  -22.687 -65.578 1.00 59.47  ? 275 VAL   B CG2 1 
ATOM   5081 N N   . ALA   B 1 276 ? 11.643  -21.595 -64.991 1.00 53.52  ? 276 ALA   B N   1 
ATOM   5082 C CA  . ALA   B 1 276 ? 10.622  -20.999 -65.837 1.00 58.35  ? 276 ALA   B CA  1 
ATOM   5083 C C   . ALA   B 1 276 ? 11.279  -20.504 -67.120 1.00 61.89  ? 276 ALA   B C   1 
ATOM   5084 O O   . ALA   B 1 276 ? 12.494  -20.298 -67.174 1.00 61.06  ? 276 ALA   B O   1 
ATOM   5085 C CB  . ALA   B 1 276 ? 9.899   -19.847 -65.122 1.00 53.41  ? 276 ALA   B CB  1 
ATOM   5086 N N   . ASP   B 1 277 ? 10.473  -20.325 -68.164 1.00 62.46  ? 277 ASP   B N   1 
ATOM   5087 C CA  . ASP   B 1 277 ? 11.013  -19.811 -69.414 1.00 64.79  ? 277 ASP   B CA  1 
ATOM   5088 C C   . ASP   B 1 277 ? 10.897  -18.287 -69.466 1.00 62.91  ? 277 ASP   B C   1 
ATOM   5089 O O   . ASP   B 1 277 ? 10.227  -17.658 -68.643 1.00 60.17  ? 277 ASP   B O   1 
ATOM   5090 C CB  . ASP   B 1 277 ? 10.347  -20.496 -70.621 1.00 64.55  ? 277 ASP   B CB  1 
ATOM   5091 C CG  . ASP   B 1 277 ? 8.888   -20.090 -70.840 1.00 62.14  ? 277 ASP   B CG  1 
ATOM   5092 O OD1 . ASP   B 1 277 ? 8.402   -19.098 -70.267 1.00 63.92  ? 277 ASP   B OD1 1 
ATOM   5093 O OD2 . ASP   B 1 277 ? 8.211   -20.799 -71.616 1.00 67.47  ? 277 ASP   B OD2 1 
ATOM   5094 N N   . SER   B 1 278 ? 11.568  -17.695 -70.457 1.00 64.20  ? 278 SER   B N   1 
ATOM   5095 C CA  . SER   B 1 278 ? 11.756  -16.247 -70.469 1.00 62.60  ? 278 SER   B CA  1 
ATOM   5096 C C   . SER   B 1 278 ? 10.437  -15.503 -70.627 1.00 62.92  ? 278 SER   B C   1 
ATOM   5097 O O   . SER   B 1 278 ? 10.224  -14.470 -69.981 1.00 60.51  ? 278 SER   B O   1 
ATOM   5098 C CB  . SER   B 1 278 ? 12.720  -15.856 -71.585 1.00 65.64  ? 278 SER   B CB  1 
ATOM   5099 O OG  . SER   B 1 278 ? 12.050  -15.855 -72.831 1.00 70.69  ? 278 SER   B OG  1 
ATOM   5100 N N   . ALA   B 1 279 ? 9.546   -16.000 -71.489 1.00 60.89  ? 279 ALA   B N   1 
ATOM   5101 C CA  . ALA   B 1 279 ? 8.250   -15.350 -71.657 1.00 59.84  ? 279 ALA   B CA  1 
ATOM   5102 C C   . ALA   B 1 279 ? 7.473   -15.330 -70.348 1.00 58.63  ? 279 ALA   B C   1 
ATOM   5103 O O   . ALA   B 1 279 ? 6.742   -14.374 -70.064 1.00 57.25  ? 279 ALA   B O   1 
ATOM   5104 C CB  . ALA   B 1 279 ? 7.444   -16.053 -72.748 1.00 61.12  ? 279 ALA   B CB  1 
ATOM   5105 N N   . THR   B 1 280 ? 7.624   -16.377 -69.535 1.00 57.96  ? 280 THR   B N   1 
ATOM   5106 C CA  . THR   B 1 280 ? 6.953   -16.420 -68.240 1.00 59.65  ? 280 THR   B CA  1 
ATOM   5107 C C   . THR   B 1 280 ? 7.604   -15.457 -67.255 1.00 59.98  ? 280 THR   B C   1 
ATOM   5108 O O   . THR   B 1 280 ? 6.913   -14.715 -66.547 1.00 58.30  ? 280 THR   B O   1 
ATOM   5109 C CB  . THR   B 1 280 ? 6.969   -17.847 -67.689 1.00 58.39  ? 280 THR   B CB  1 
ATOM   5110 O OG1 . THR   B 1 280 ? 6.192   -18.699 -68.540 1.00 57.85  ? 280 THR   B OG1 1 
ATOM   5111 C CG2 . THR   B 1 280 ? 6.405   -17.886 -66.275 1.00 58.08  ? 280 THR   B CG2 1 
ATOM   5112 N N   . ILE   B 1 281 ? 8.939   -15.462 -67.195 1.00 62.04  ? 281 ILE   B N   1 
ATOM   5113 C CA  . ILE   B 1 281 ? 9.656   -14.514 -66.348 1.00 59.00  ? 281 ILE   B CA  1 
ATOM   5114 C C   . ILE   B 1 281 ? 9.271   -13.087 -66.711 1.00 59.97  ? 281 ILE   B C   1 
ATOM   5115 O O   . ILE   B 1 281 ? 9.041   -12.247 -65.833 1.00 60.76  ? 281 ILE   B O   1 
ATOM   5116 C CB  . ILE   B 1 281 ? 11.176  -14.740 -66.466 1.00 58.19  ? 281 ILE   B CB  1 
ATOM   5117 C CG1 . ILE   B 1 281 ? 11.627  -15.865 -65.536 1.00 56.97  ? 281 ILE   B CG1 1 
ATOM   5118 C CG2 . ILE   B 1 281 ? 11.944  -13.462 -66.149 1.00 63.30  ? 281 ILE   B CG2 1 
ATOM   5119 C CD1 . ILE   B 1 281 ? 13.122  -16.077 -65.522 1.00 59.51  ? 281 ILE   B CD1 1 
ATOM   5120 N N   . SER   B 1 282 ? 9.151   -12.803 -68.011 1.00 58.04  ? 282 SER   B N   1 
ATOM   5121 C CA  . SER   B 1 282 ? 8.890   -11.438 -68.457 1.00 59.56  ? 282 SER   B CA  1 
ATOM   5122 C C   . SER   B 1 282 ? 7.524   -10.935 -68.016 1.00 59.71  ? 282 SER   B C   1 
ATOM   5123 O O   . SER   B 1 282 ? 7.376   -9.748  -67.706 1.00 61.68  ? 282 SER   B O   1 
ATOM   5124 C CB  . SER   B 1 282 ? 9.001   -11.341 -69.975 1.00 59.80  ? 282 SER   B CB  1 
ATOM   5125 O OG  . SER   B 1 282 ? 8.168   -10.302 -70.456 1.00 58.61  ? 282 SER   B OG  1 
ATOM   5126 N N   . ALA   B 1 283 ? 6.515   -11.803 -67.991 1.00 60.35  ? 283 ALA   B N   1 
ATOM   5127 C CA  . ALA   B 1 283 ? 5.195   -11.352 -67.572 1.00 61.22  ? 283 ALA   B CA  1 
ATOM   5128 C C   . ALA   B 1 283 ? 5.154   -11.064 -66.077 1.00 58.68  ? 283 ALA   B C   1 
ATOM   5129 O O   . ALA   B 1 283 ? 4.635   -10.022 -65.661 1.00 60.25  ? 283 ALA   B O   1 
ATOM   5130 C CB  . ALA   B 1 283 ? 4.139   -12.385 -67.950 1.00 61.19  ? 283 ALA   B CB  1 
ATOM   5131 N N   . VAL   B 1 284 ? 5.706   -11.965 -65.259 1.00 56.03  ? 284 VAL   B N   1 
ATOM   5132 C CA  . VAL   B 1 284 ? 5.713   -11.760 -63.811 1.00 58.26  ? 284 VAL   B CA  1 
ATOM   5133 C C   . VAL   B 1 284 ? 6.417   -10.456 -63.457 1.00 60.06  ? 284 VAL   B C   1 
ATOM   5134 O O   . VAL   B 1 284 ? 5.937   -9.681  -62.619 1.00 58.94  ? 284 VAL   B O   1 
ATOM   5135 C CB  . VAL   B 1 284 ? 6.362   -12.965 -63.102 1.00 54.70  ? 284 VAL   B CB  1 
ATOM   5136 C CG1 . VAL   B 1 284 ? 6.320   -12.784 -61.588 1.00 53.41  ? 284 VAL   B CG1 1 
ATOM   5137 C CG2 . VAL   B 1 284 ? 5.671   -14.258 -63.511 1.00 53.06  ? 284 VAL   B CG2 1 
ATOM   5138 N N   . GLU   B 1 285 ? 7.562   -10.187 -64.090 1.00 59.70  ? 285 GLU   B N   1 
ATOM   5139 C CA  . GLU   B 1 285 ? 8.264   -8.932  -63.839 1.00 58.31  ? 285 GLU   B CA  1 
ATOM   5140 C C   . GLU   B 1 285 ? 7.462   -7.734  -64.332 1.00 59.35  ? 285 GLU   B C   1 
ATOM   5141 O O   . GLU   B 1 285 ? 7.578   -6.639  -63.771 1.00 60.98  ? 285 GLU   B O   1 
ATOM   5142 C CB  . GLU   B 1 285 ? 9.640   -8.953  -64.502 1.00 58.44  ? 285 GLU   B CB  1 
ATOM   5143 C CG  . GLU   B 1 285 ? 10.492  -10.157 -64.144 1.00 61.06  ? 285 GLU   B CG  1 
ATOM   5144 C CD  . GLU   B 1 285 ? 11.942  -9.800  -63.893 1.00 63.64  ? 285 GLU   B CD  1 
ATOM   5145 O OE1 . GLU   B 1 285 ? 12.772  -10.728 -63.797 1.00 64.87  ? 285 GLU   B OE1 1 
ATOM   5146 O OE2 . GLU   B 1 285 ? 12.254  -8.595  -63.799 1.00 69.33  ? 285 GLU   B OE2 1 
ATOM   5147 N N   . ARG   B 1 286 ? 6.643   -7.921  -65.370 1.00 58.48  ? 286 ARG   B N   1 
ATOM   5148 C CA  . ARG   B 1 286 ? 5.832   -6.816  -65.867 1.00 61.55  ? 286 ARG   B CA  1 
ATOM   5149 C C   . ARG   B 1 286 ? 4.733   -6.449  -64.878 1.00 59.42  ? 286 ARG   B C   1 
ATOM   5150 O O   . ARG   B 1 286 ? 4.383   -5.270  -64.751 1.00 56.62  ? 286 ARG   B O   1 
ATOM   5151 C CB  . ARG   B 1 286 ? 5.247   -7.164  -67.242 1.00 63.86  ? 286 ARG   B CB  1 
ATOM   5152 C CG  . ARG   B 1 286 ? 4.140   -6.219  -67.720 1.00 62.95  ? 286 ARG   B CG  1 
ATOM   5153 C CD  . ARG   B 1 286 ? 3.688   -6.521  -69.151 1.00 65.31  ? 286 ARG   B CD  1 
ATOM   5154 N NE  . ARG   B 1 286 ? 3.362   -7.926  -69.369 1.00 67.15  ? 286 ARG   B NE  1 
ATOM   5155 C CZ  . ARG   B 1 286 ? 3.982   -8.723  -70.230 1.00 64.38  ? 286 ARG   B CZ  1 
ATOM   5156 N NH1 . ARG   B 1 286 ? 5.022   -8.308  -70.934 1.00 61.53  ? 286 ARG   B NH1 1 
ATOM   5157 N NH2 . ARG   B 1 286 ? 3.550   -9.971  -70.385 1.00 66.66  ? 286 ARG   B NH2 1 
ATOM   5158 N N   . ALA   B 1 287 ? 4.203   -7.432  -64.149 1.00 58.68  ? 287 ALA   B N   1 
ATOM   5159 C CA  . ALA   B 1 287 ? 3.186   -7.139  -63.145 1.00 57.40  ? 287 ALA   B CA  1 
ATOM   5160 C C   . ALA   B 1 287 ? 3.787   -6.395  -61.960 1.00 54.25  ? 287 ALA   B C   1 
ATOM   5161 O O   . ALA   B 1 287 ? 3.211   -5.416  -61.472 1.00 54.01  ? 287 ALA   B O   1 
ATOM   5162 C CB  . ALA   B 1 287 ? 2.511   -8.432  -62.686 1.00 56.95  ? 287 ALA   B CB  1 
ATOM   5163 N N   . ALA   B 1 288 ? 4.949   -6.848  -61.484 1.00 54.48  ? 288 ALA   B N   1 
ATOM   5164 C CA  . ALA   B 1 288 ? 5.624   -6.158  -60.388 1.00 58.00  ? 288 ALA   B CA  1 
ATOM   5165 C C   . ALA   B 1 288 ? 6.052   -4.755  -60.801 1.00 58.10  ? 288 ALA   B C   1 
ATOM   5166 O O   . ALA   B 1 288 ? 5.801   -3.780  -60.083 1.00 57.35  ? 288 ALA   B O   1 
ATOM   5167 C CB  . ALA   B 1 288 ? 6.829   -6.973  -59.922 1.00 53.58  ? 288 ALA   B CB  1 
ATOM   5168 N N   . ALA   B 1 289 ? 6.704   -4.634  -61.962 1.00 57.18  ? 289 ALA   B N   1 
ATOM   5169 C CA  . ALA   B 1 289 ? 7.143   -3.327  -62.443 1.00 59.39  ? 289 ALA   B CA  1 
ATOM   5170 C C   . ALA   B 1 289 ? 5.977   -2.359  -62.609 1.00 57.77  ? 289 ALA   B C   1 
ATOM   5171 O O   . ALA   B 1 289 ? 6.153   -1.146  -62.448 1.00 62.34  ? 289 ALA   B O   1 
ATOM   5172 C CB  . ALA   B 1 289 ? 7.904   -3.479  -63.760 1.00 61.06  ? 289 ALA   B CB  1 
ATOM   5173 N N   . ALA   B 1 290 ? 4.784   -2.869  -62.923 1.00 57.21  ? 290 ALA   B N   1 
ATOM   5174 C CA  . ALA   B 1 290 ? 3.598   -2.021  -62.987 1.00 57.18  ? 290 ALA   B CA  1 
ATOM   5175 C C   . ALA   B 1 290 ? 3.025   -1.706  -61.614 1.00 58.70  ? 290 ALA   B C   1 
ATOM   5176 O O   . ALA   B 1 290 ? 2.342   -0.688  -61.464 1.00 56.89  ? 290 ALA   B O   1 
ATOM   5177 C CB  . ALA   B 1 290 ? 2.521   -2.675  -63.848 1.00 56.47  ? 290 ALA   B CB  1 
ATOM   5178 N N   . CYS   B 1 291 ? 3.272   -2.559  -60.618 1.00 58.10  ? 291 CYS   B N   1 
ATOM   5179 C CA  . CYS   B 1 291 ? 2.905   -2.217  -59.248 1.00 59.03  ? 291 CYS   B CA  1 
ATOM   5180 C C   . CYS   B 1 291 ? 3.872   -1.198  -58.668 1.00 58.60  ? 291 CYS   B C   1 
ATOM   5181 O O   . CYS   B 1 291 ? 3.459   -0.300  -57.926 1.00 59.94  ? 291 CYS   B O   1 
ATOM   5182 C CB  . CYS   B 1 291 ? 2.868   -3.469  -58.374 1.00 57.19  ? 291 CYS   B CB  1 
ATOM   5183 S SG  . CYS   B 1 291 ? 1.605   -4.672  -58.836 1.00 58.72  ? 291 CYS   B SG  1 
ATOM   5184 N N   . GLU   B 1 292 ? 5.159   -1.336  -58.992 1.00 60.74  ? 292 GLU   B N   1 
ATOM   5185 C CA  . GLU   B 1 292 ? 6.137   -0.306  -58.657 1.00 59.75  ? 292 GLU   B CA  1 
ATOM   5186 C C   . GLU   B 1 292 ? 5.696   1.055   -59.183 1.00 58.96  ? 292 GLU   B C   1 
ATOM   5187 O O   . GLU   B 1 292 ? 5.747   2.061   -58.466 1.00 60.88  ? 292 GLU   B O   1 
ATOM   5188 C CB  . GLU   B 1 292 ? 7.503   -0.687  -59.232 1.00 58.62  ? 292 GLU   B CB  1 
ATOM   5189 C CG  . GLU   B 1 292 ? 8.681   -0.296  -58.360 1.00 64.13  ? 292 GLU   B CG  1 
ATOM   5190 C CD  . GLU   B 1 292 ? 9.771   -1.351  -58.346 1.00 72.11  ? 292 GLU   B CD  1 
ATOM   5191 O OE1 . GLU   B 1 292 ? 10.177  -1.807  -59.437 1.00 77.65  ? 292 GLU   B OE1 1 
ATOM   5192 O OE2 . GLU   B 1 292 ? 10.228  -1.719  -57.243 1.00 72.45  ? 292 GLU   B OE2 1 
ATOM   5193 N N   . ALA   B 1 293 ? 5.245   1.097   -60.441 1.00 58.41  ? 293 ALA   B N   1 
ATOM   5194 C CA  . ALA   B 1 293 ? 4.789   2.345   -61.044 1.00 58.54  ? 293 ALA   B CA  1 
ATOM   5195 C C   . ALA   B 1 293 ? 3.569   2.926   -60.343 1.00 59.38  ? 293 ALA   B C   1 
ATOM   5196 O O   . ALA   B 1 293 ? 3.274   4.113   -60.521 1.00 64.76  ? 293 ALA   B O   1 
ATOM   5197 C CB  . ALA   B 1 293 ? 4.474   2.127   -62.524 1.00 60.21  ? 293 ALA   B CB  1 
ATOM   5198 N N   . SER   B 1 294 ? 2.854   2.125   -59.557 1.00 59.97  ? 294 SER   B N   1 
ATOM   5199 C CA  . SER   B 1 294 ? 1.686   2.591   -58.823 1.00 59.44  ? 294 SER   B CA  1 
ATOM   5200 C C   . SER   B 1 294 ? 1.984   2.886   -57.361 1.00 57.00  ? 294 SER   B C   1 
ATOM   5201 O O   . SER   B 1 294 ? 1.080   3.307   -56.634 1.00 55.81  ? 294 SER   B O   1 
ATOM   5202 C CB  . SER   B 1 294 ? 0.553   1.565   -58.922 1.00 58.45  ? 294 SER   B CB  1 
ATOM   5203 O OG  . SER   B 1 294 ? 0.477   1.014   -60.225 1.00 60.72  ? 294 SER   B OG  1 
ATOM   5204 N N   . GLY   B 1 295 ? 3.218   2.672   -56.914 1.00 54.93  ? 295 GLY   B N   1 
ATOM   5205 C CA  . GLY   B 1 295 ? 3.622   3.009   -55.566 1.00 57.04  ? 295 GLY   B CA  1 
ATOM   5206 C C   . GLY   B 1 295 ? 3.937   1.839   -54.659 1.00 56.90  ? 295 GLY   B C   1 
ATOM   5207 O O   . GLY   B 1 295 ? 4.083   2.042   -53.448 1.00 58.21  ? 295 GLY   B O   1 
ATOM   5208 N N   . ALA   B 1 296 ? 4.045   0.630   -55.196 1.00 57.73  ? 296 ALA   B N   1 
ATOM   5209 C CA  . ALA   B 1 296 ? 4.377   -0.539  -54.396 1.00 57.88  ? 296 ALA   B CA  1 
ATOM   5210 C C   . ALA   B 1 296 ? 5.885   -0.730  -54.332 1.00 56.73  ? 296 ALA   B C   1 
ATOM   5211 O O   . ALA   B 1 296 ? 6.597   -0.490  -55.310 1.00 56.16  ? 296 ALA   B O   1 
ATOM   5212 C CB  . ALA   B 1 296 ? 3.718   -1.793  -54.976 1.00 55.80  ? 296 ALA   B CB  1 
ATOM   5213 N N   . THR   B 1 297 ? 6.367   -1.162  -53.172 1.00 56.12  ? 297 THR   B N   1 
ATOM   5214 C CA  . THR   B 1 297 ? 7.767   -1.520  -53.006 1.00 57.94  ? 297 THR   B CA  1 
ATOM   5215 C C   . THR   B 1 297 ? 7.952   -2.974  -53.415 1.00 56.36  ? 297 THR   B C   1 
ATOM   5216 O O   . THR   B 1 297 ? 7.200   -3.848  -52.973 1.00 56.97  ? 297 THR   B O   1 
ATOM   5217 C CB  . THR   B 1 297 ? 8.218   -1.320  -51.559 1.00 62.73  ? 297 THR   B CB  1 
ATOM   5218 O OG1 . THR   B 1 297 ? 7.965   -2.518  -50.810 1.00 63.18  ? 297 THR   B OG1 1 
ATOM   5219 C CG2 . THR   B 1 297 ? 7.463   -0.165  -50.920 1.00 57.24  ? 297 THR   B CG2 1 
ATOM   5220 N N   . VAL   B 1 298 ? 8.941   -3.232  -54.265 1.00 56.03  ? 298 VAL   B N   1 
ATOM   5221 C CA  . VAL   B 1 298 ? 9.225   -4.578  -54.748 1.00 58.75  ? 298 VAL   B CA  1 
ATOM   5222 C C   . VAL   B 1 298 ? 10.624  -4.969  -54.297 1.00 51.64  ? 298 VAL   B C   1 
ATOM   5223 O O   . VAL   B 1 298 ? 11.567  -4.180  -54.425 1.00 56.21  ? 298 VAL   B O   1 
ATOM   5224 C CB  . VAL   B 1 298 ? 9.093   -4.680  -56.279 1.00 56.83  ? 298 VAL   B CB  1 
ATOM   5225 C CG1 . VAL   B 1 298 ? 9.405   -6.096  -56.747 1.00 54.01  ? 298 VAL   B CG1 1 
ATOM   5226 C CG2 . VAL   B 1 298 ? 7.696   -4.269  -56.718 1.00 55.63  ? 298 VAL   B CG2 1 
ATOM   5227 N N   . ALA   B 1 299 ? 10.747  -6.175  -53.754 1.00 51.99  ? 299 ALA   B N   1 
ATOM   5228 C CA  . ALA   B 1 299 ? 12.029  -6.782  -53.444 1.00 49.78  ? 299 ALA   B CA  1 
ATOM   5229 C C   . ALA   B 1 299 ? 12.154  -8.085  -54.216 1.00 54.37  ? 299 ALA   B C   1 
ATOM   5230 O O   . ALA   B 1 299 ? 11.149  -8.717  -54.561 1.00 52.99  ? 299 ALA   B O   1 
ATOM   5231 C CB  . ALA   B 1 299 ? 12.183  -7.042  -51.939 1.00 49.53  ? 299 ALA   B CB  1 
ATOM   5232 N N   . THR   B 1 300 ? 13.397  -8.478  -54.496 1.00 53.58  ? 300 THR   B N   1 
ATOM   5233 C CA  . THR   B 1 300 ? 13.680  -9.715  -55.211 1.00 56.90  ? 300 THR   B CA  1 
ATOM   5234 C C   . THR   B 1 300 ? 14.409  -10.722 -54.339 1.00 60.71  ? 300 THR   B C   1 
ATOM   5235 O O   . THR   B 1 300 ? 14.904  -11.733 -54.852 1.00 59.66  ? 300 THR   B O   1 
ATOM   5236 C CB  . THR   B 1 300 ? 14.492  -9.433  -56.477 1.00 59.69  ? 300 THR   B CB  1 
ATOM   5237 O OG1 . THR   B 1 300 ? 15.430  -8.380  -56.223 1.00 66.86  ? 300 THR   B OG1 1 
ATOM   5238 C CG2 . THR   B 1 300 ? 13.558  -9.010  -57.602 1.00 57.96  ? 300 THR   B CG2 1 
ATOM   5239 N N   . SER   B 1 301 ? 14.501  -10.463 -53.042 1.00 59.06  ? 301 SER   B N   1 
ATOM   5240 C CA  . SER   B 1 301 ? 15.021  -11.435 -52.094 1.00 56.10  ? 301 SER   B CA  1 
ATOM   5241 C C   . SER   B 1 301 ? 14.519  -11.047 -50.713 1.00 61.04  ? 301 SER   B C   1 
ATOM   5242 O O   . SER   B 1 301 ? 13.966  -9.963  -50.511 1.00 62.96  ? 301 SER   B O   1 
ATOM   5243 C CB  . SER   B 1 301 ? 16.551  -11.500 -52.125 1.00 58.69  ? 301 SER   B CB  1 
ATOM   5244 O OG  . SER   B 1 301 ? 17.113  -10.203 -52.034 1.00 60.65  ? 301 SER   B OG  1 
ATOM   5245 N N   . SER   B 1 302 ? 14.728  -11.946 -49.764 1.00 61.71  ? 302 SER   B N   1 
ATOM   5246 C CA  . SER   B 1 302 ? 14.365  -11.720 -48.375 1.00 61.58  ? 302 SER   B CA  1 
ATOM   5247 C C   . SER   B 1 302 ? 15.075  -12.744 -47.501 1.00 62.42  ? 302 SER   B C   1 
ATOM   5248 O O   . SER   B 1 302 ? 15.074  -13.939 -47.821 1.00 61.79  ? 302 SER   B O   1 
ATOM   5249 C CB  . SER   B 1 302 ? 12.848  -11.805 -48.184 1.00 61.37  ? 302 SER   B CB  1 
ATOM   5250 O OG  . SER   B 1 302 ? 12.490  -11.735 -46.813 1.00 62.76  ? 302 SER   B OG  1 
ATOM   5251 N N   . PRO   B 1 303 ? 15.715  -12.319 -46.407 1.00 61.24  ? 303 PRO   B N   1 
ATOM   5252 C CA  . PRO   B 1 303 ? 16.296  -13.298 -45.471 1.00 61.24  ? 303 PRO   B CA  1 
ATOM   5253 C C   . PRO   B 1 303 ? 15.265  -14.234 -44.865 1.00 62.48  ? 303 PRO   B C   1 
ATOM   5254 O O   . PRO   B 1 303 ? 15.650  -15.259 -44.285 1.00 61.72  ? 303 PRO   B O   1 
ATOM   5255 C CB  . PRO   B 1 303 ? 16.952  -12.430 -44.386 1.00 61.16  ? 303 PRO   B CB  1 
ATOM   5256 C CG  . PRO   B 1 303 ? 16.576  -11.024 -44.666 1.00 64.17  ? 303 PRO   B CG  1 
ATOM   5257 C CD  . PRO   B 1 303 ? 15.988  -10.922 -46.033 1.00 61.78  ? 303 PRO   B CD  1 
ATOM   5258 N N   . ASP   B 1 304 ? 13.977  -13.919 -44.985 1.00 60.84  ? 304 ASP   B N   1 
ATOM   5259 C CA  . ASP   B 1 304 ? 12.915  -14.675 -44.342 1.00 61.51  ? 304 ASP   B CA  1 
ATOM   5260 C C   . ASP   B 1 304 ? 12.262  -15.697 -45.262 1.00 60.54  ? 304 ASP   B C   1 
ATOM   5261 O O   . ASP   B 1 304 ? 11.495  -16.534 -44.777 1.00 59.88  ? 304 ASP   B O   1 
ATOM   5262 C CB  . ASP   B 1 304 ? 11.847  -13.714 -43.806 1.00 61.38  ? 304 ASP   B CB  1 
ATOM   5263 C CG  . ASP   B 1 304 ? 12.244  -13.081 -42.482 1.00 65.17  ? 304 ASP   B CG  1 
ATOM   5264 O OD1 . ASP   B 1 304 ? 13.221  -13.562 -41.867 1.00 63.46  ? 304 ASP   B OD1 1 
ATOM   5265 O OD2 . ASP   B 1 304 ? 11.592  -12.095 -42.063 1.00 63.55  ? 304 ASP   B OD2 1 
ATOM   5266 N N   . LEU   B 1 305 ? 12.540  -15.657 -46.560 1.00 58.85  ? 305 LEU   B N   1 
ATOM   5267 C CA  . LEU   B 1 305 ? 11.975  -16.652 -47.465 1.00 59.52  ? 305 LEU   B CA  1 
ATOM   5268 C C   . LEU   B 1 305 ? 12.538  -18.024 -47.121 1.00 59.47  ? 305 LEU   B C   1 
ATOM   5269 O O   . LEU   B 1 305 ? 13.756  -18.223 -47.222 1.00 59.93  ? 305 LEU   B O   1 
ATOM   5270 C CB  . LEU   B 1 305 ? 12.272  -16.306 -48.920 1.00 56.45  ? 305 LEU   B CB  1 
ATOM   5271 C CG  . LEU   B 1 305 ? 11.822  -17.374 -49.920 1.00 59.63  ? 305 LEU   B CG  1 
ATOM   5272 C CD1 . LEU   B 1 305 ? 10.500  -16.988 -50.564 1.00 55.77  ? 305 LEU   B CD1 1 
ATOM   5273 C CD2 . LEU   B 1 305 ? 12.888  -17.623 -50.979 1.00 55.99  ? 305 LEU   B CD2 1 
ATOM   5274 N N   . PRO   B 1 306 ? 11.707  -18.993 -46.715 1.00 59.11  ? 306 PRO   B N   1 
ATOM   5275 C CA  . PRO   B 1 306 ? 12.243  -20.297 -46.303 1.00 57.07  ? 306 PRO   B CA  1 
ATOM   5276 C C   . PRO   B 1 306 ? 12.831  -21.096 -47.457 1.00 56.15  ? 306 PRO   B C   1 
ATOM   5277 O O   . PRO   B 1 306 ? 12.784  -20.667 -48.615 1.00 56.83  ? 306 PRO   B O   1 
ATOM   5278 C CB  . PRO   B 1 306 ? 11.023  -20.995 -45.689 1.00 57.01  ? 306 PRO   B CB  1 
ATOM   5279 C CG  . PRO   B 1 306 ? 9.852   -20.380 -46.383 1.00 56.98  ? 306 PRO   B CG  1 
ATOM   5280 C CD  . PRO   B 1 306 ? 10.236  -18.939 -46.617 1.00 56.77  ? 306 PRO   B CD  1 
ATOM   5281 N N   . ASP   B 1 307 ? 13.392  -22.260 -47.143 1.00 57.67  ? 307 ASP   B N   1 
ATOM   5282 C CA  . ASP   B 1 307 ? 14.092  -23.086 -48.126 1.00 58.38  ? 307 ASP   B CA  1 
ATOM   5283 C C   . ASP   B 1 307 ? 13.070  -23.766 -49.031 1.00 57.33  ? 307 ASP   B C   1 
ATOM   5284 O O   . ASP   B 1 307 ? 12.439  -24.754 -48.647 1.00 53.53  ? 307 ASP   B O   1 
ATOM   5285 C CB  . ASP   B 1 307 ? 14.978  -24.108 -47.424 1.00 58.98  ? 307 ASP   B CB  1 
ATOM   5286 C CG  . ASP   B 1 307 ? 15.897  -24.842 -48.381 1.00 63.23  ? 307 ASP   B CG  1 
ATOM   5287 O OD1 . ASP   B 1 307 ? 16.452  -25.891 -47.987 1.00 67.12  ? 307 ASP   B OD1 1 
ATOM   5288 O OD2 . ASP   B 1 307 ? 16.065  -24.374 -49.527 1.00 65.56  ? 307 ASP   B OD2 1 
ATOM   5289 N N   . LEU   B 1 308 ? 12.926  -23.246 -50.254 1.00 59.87  ? 308 LEU   B N   1 
ATOM   5290 C CA  . LEU   B 1 308 ? 11.961  -23.795 -51.202 1.00 55.42  ? 308 LEU   B CA  1 
ATOM   5291 C C   . LEU   B 1 308 ? 12.320  -25.208 -51.647 1.00 54.68  ? 308 LEU   B C   1 
ATOM   5292 O O   . LEU   B 1 308 ? 11.432  -25.954 -52.076 1.00 55.39  ? 308 LEU   B O   1 
ATOM   5293 C CB  . LEU   B 1 308 ? 11.841  -22.866 -52.412 1.00 53.53  ? 308 LEU   B CB  1 
ATOM   5294 C CG  . LEU   B 1 308 ? 11.485  -21.403 -52.122 1.00 55.14  ? 308 LEU   B CG  1 
ATOM   5295 C CD1 . LEU   B 1 308 ? 10.974  -20.716 -53.376 1.00 54.65  ? 308 LEU   B CD1 1 
ATOM   5296 C CD2 . LEU   B 1 308 ? 10.460  -21.285 -51.001 1.00 50.44  ? 308 LEU   B CD2 1 
ATOM   5297 N N   . SER   B 1 309 ? 13.594  -25.594 -51.546 1.00 54.58  ? 309 SER   B N   1 
ATOM   5298 C CA  . SER   B 1 309 ? 13.985  -26.956 -51.898 1.00 56.68  ? 309 SER   B CA  1 
ATOM   5299 C C   . SER   B 1 309 ? 13.549  -27.950 -50.829 1.00 55.02  ? 309 SER   B C   1 
ATOM   5300 O O   . SER   B 1 309 ? 13.067  -29.042 -51.149 1.00 49.25  ? 309 SER   B O   1 
ATOM   5301 C CB  . SER   B 1 309 ? 15.495  -27.028 -52.115 1.00 55.76  ? 309 SER   B CB  1 
ATOM   5302 O OG  . SER   B 1 309 ? 16.072  -25.734 -52.081 1.00 57.86  ? 309 SER   B OG  1 
ATOM   5303 N N   . ALA   B 1 310 ? 13.727  -27.597 -49.554 1.00 54.92  ? 310 ALA   B N   1 
ATOM   5304 C CA  . ALA   B 1 310 ? 13.217  -28.444 -48.482 1.00 55.63  ? 310 ALA   B CA  1 
ATOM   5305 C C   . ALA   B 1 310 ? 11.697  -28.517 -48.527 1.00 54.06  ? 310 ALA   B C   1 
ATOM   5306 O O   . ALA   B 1 310 ? 11.109  -29.577 -48.281 1.00 52.59  ? 310 ALA   B O   1 
ATOM   5307 C CB  . ALA   B 1 310 ? 13.691  -27.920 -47.127 1.00 56.60  ? 310 ALA   B CB  1 
ATOM   5308 N N   . LEU   B 1 311 ? 11.049  -27.394 -48.850 1.00 53.14  ? 311 LEU   B N   1 
ATOM   5309 C CA  . LEU   B 1 311 ? 9.594   -27.347 -48.936 1.00 48.97  ? 311 LEU   B CA  1 
ATOM   5310 C C   . LEU   B 1 311 ? 9.072   -28.331 -49.978 1.00 49.84  ? 311 LEU   B C   1 
ATOM   5311 O O   . LEU   B 1 311 ? 8.242   -29.195 -49.676 1.00 48.16  ? 311 LEU   B O   1 
ATOM   5312 C CB  . LEU   B 1 311 ? 9.149   -25.917 -49.262 1.00 49.96  ? 311 LEU   B CB  1 
ATOM   5313 C CG  . LEU   B 1 311 ? 7.682   -25.508 -49.098 1.00 48.40  ? 311 LEU   B CG  1 
ATOM   5314 C CD1 . LEU   B 1 311 ? 7.597   -24.010 -48.916 1.00 45.89  ? 311 LEU   B CD1 1 
ATOM   5315 C CD2 . LEU   B 1 311 ? 6.830   -25.933 -50.287 1.00 46.57  ? 311 LEU   B CD2 1 
ATOM   5316 N N   . VAL   B 1 312 ? 9.554   -28.212 -51.219 1.00 48.55  ? 312 VAL   B N   1 
ATOM   5317 C CA  . VAL   B 1 312 ? 9.052   -29.058 -52.299 1.00 49.16  ? 312 VAL   B CA  1 
ATOM   5318 C C   . VAL   B 1 312 ? 9.325   -30.530 -52.014 1.00 50.52  ? 312 VAL   B C   1 
ATOM   5319 O O   . VAL   B 1 312 ? 8.519   -31.398 -52.370 1.00 48.35  ? 312 VAL   B O   1 
ATOM   5320 C CB  . VAL   B 1 312 ? 9.649   -28.611 -53.650 1.00 50.37  ? 312 VAL   B CB  1 
ATOM   5321 C CG1 . VAL   B 1 312 ? 11.166  -28.760 -53.658 1.00 52.00  ? 312 VAL   B CG1 1 
ATOM   5322 C CG2 . VAL   B 1 312 ? 9.023   -29.385 -54.798 1.00 48.95  ? 312 VAL   B CG2 1 
ATOM   5323 N N   . ALA   B 1 313 ? 10.442  -30.838 -51.350 1.00 50.42  ? 313 ALA   B N   1 
ATOM   5324 C CA  . ALA   B 1 313 ? 10.731  -32.225 -51.001 1.00 46.82  ? 313 ALA   B CA  1 
ATOM   5325 C C   . ALA   B 1 313 ? 9.742   -32.749 -49.968 1.00 51.75  ? 313 ALA   B C   1 
ATOM   5326 O O   . ALA   B 1 313 ? 9.204   -33.853 -50.113 1.00 53.85  ? 313 ALA   B O   1 
ATOM   5327 C CB  . ALA   B 1 313 ? 12.164  -32.352 -50.487 1.00 47.88  ? 313 ALA   B CB  1 
ATOM   5328 N N   . ASP   B 1 314 ? 9.491   -31.972 -48.911 1.00 52.30  ? 314 ASP   B N   1 
ATOM   5329 C CA  . ASP   B 1 314 ? 8.523   -32.394 -47.903 1.00 52.08  ? 314 ASP   B CA  1 
ATOM   5330 C C   . ASP   B 1 314 ? 7.109   -32.397 -48.467 1.00 47.90  ? 314 ASP   B C   1 
ATOM   5331 O O   . ASP   B 1 314 ? 6.297   -33.261 -48.119 1.00 49.37  ? 314 ASP   B O   1 
ATOM   5332 C CB  . ASP   B 1 314 ? 8.605   -31.488 -46.674 1.00 51.71  ? 314 ASP   B CB  1 
ATOM   5333 C CG  . ASP   B 1 314 ? 9.962   -31.538 -45.998 1.00 58.31  ? 314 ASP   B CG  1 
ATOM   5334 O OD1 . ASP   B 1 314 ? 10.752  -32.459 -46.301 1.00 59.69  ? 314 ASP   B OD1 1 
ATOM   5335 O OD2 . ASP   B 1 314 ? 10.238  -30.654 -45.158 1.00 56.10  ? 314 ASP   B OD2 1 
ATOM   5336 N N   . TYR   B 1 315 ? 6.798   -31.437 -49.338 1.00 49.10  ? 315 TYR   B N   1 
ATOM   5337 C CA  . TYR   B 1 315 ? 5.475   -31.391 -49.950 1.00 49.43  ? 315 TYR   B CA  1 
ATOM   5338 C C   . TYR   B 1 315 ? 5.236   -32.616 -50.823 1.00 48.26  ? 315 TYR   B C   1 
ATOM   5339 O O   . TYR   B 1 315 ? 4.181   -33.255 -50.738 1.00 49.14  ? 315 TYR   B O   1 
ATOM   5340 C CB  . TYR   B 1 315 ? 5.321   -30.105 -50.763 1.00 47.32  ? 315 TYR   B CB  1 
ATOM   5341 C CG  . TYR   B 1 315 ? 4.193   -30.145 -51.767 1.00 50.78  ? 315 TYR   B CG  1 
ATOM   5342 C CD1 . TYR   B 1 315 ? 2.876   -30.300 -51.354 1.00 49.08  ? 315 TYR   B CD1 1 
ATOM   5343 C CD2 . TYR   B 1 315 ? 4.445   -30.036 -53.128 1.00 48.42  ? 315 TYR   B CD2 1 
ATOM   5344 C CE1 . TYR   B 1 315 ? 1.842   -30.338 -52.268 1.00 48.97  ? 315 TYR   B CE1 1 
ATOM   5345 C CE2 . TYR   B 1 315 ? 3.418   -30.070 -54.048 1.00 50.81  ? 315 TYR   B CE2 1 
ATOM   5346 C CZ  . TYR   B 1 315 ? 2.119   -30.222 -53.613 1.00 49.36  ? 315 TYR   B CZ  1 
ATOM   5347 O OH  . TYR   B 1 315 ? 1.092   -30.259 -54.527 1.00 48.49  ? 315 TYR   B OH  1 
ATOM   5348 N N   . THR   B 1 316 ? 6.208   -32.955 -51.675 1.00 49.20  ? 316 THR   B N   1 
ATOM   5349 C CA  . THR   B 1 316 ? 6.103   -34.163 -52.490 1.00 49.26  ? 316 THR   B CA  1 
ATOM   5350 C C   . THR   B 1 316 ? 5.929   -35.397 -51.615 1.00 49.79  ? 316 THR   B C   1 
ATOM   5351 O O   . THR   B 1 316 ? 5.106   -36.273 -51.908 1.00 47.93  ? 316 THR   B O   1 
ATOM   5352 C CB  . THR   B 1 316 ? 7.344   -34.314 -53.371 1.00 46.27  ? 316 THR   B CB  1 
ATOM   5353 O OG1 . THR   B 1 316 ? 7.540   -33.120 -54.135 1.00 50.46  ? 316 THR   B OG1 1 
ATOM   5354 C CG2 . THR   B 1 316 ? 7.196   -35.505 -54.311 1.00 44.57  ? 316 THR   B CG2 1 
ATOM   5355 N N   . ARG   B 1 317 ? 6.704   -35.478 -50.532 1.00 48.37  ? 317 ARG   B N   1 
ATOM   5356 C CA  . ARG   B 1 317 ? 6.626   -36.632 -49.645 1.00 50.32  ? 317 ARG   B CA  1 
ATOM   5357 C C   . ARG   B 1 317 ? 5.255   -36.729 -48.984 1.00 49.46  ? 317 ARG   B C   1 
ATOM   5358 O O   . ARG   B 1 317 ? 4.714   -37.828 -48.819 1.00 47.71  ? 317 ARG   B O   1 
ATOM   5359 C CB  . ARG   B 1 317 ? 7.742   -36.553 -48.604 1.00 51.67  ? 317 ARG   B CB  1 
ATOM   5360 C CG  . ARG   B 1 317 ? 7.486   -37.345 -47.344 1.00 56.27  ? 317 ARG   B CG  1 
ATOM   5361 C CD  . ARG   B 1 317 ? 8.618   -37.144 -46.346 1.00 58.50  ? 317 ARG   B CD  1 
ATOM   5362 N NE  . ARG   B 1 317 ? 8.564   -38.046 -45.197 1.00 68.83  ? 317 ARG   B NE  1 
ATOM   5363 C CZ  . ARG   B 1 317 ? 8.463   -39.371 -45.245 1.00 67.25  ? 317 ARG   B CZ  1 
ATOM   5364 N NH1 . ARG   B 1 317 ? 8.456   -40.033 -46.394 1.00 66.65  ? 317 ARG   B NH1 1 
ATOM   5365 N NH2 . ARG   B 1 317 ? 8.380   -40.053 -44.106 1.00 64.14  ? 317 ARG   B NH2 1 
ATOM   5366 N N   . MET   B 1 318 ? 4.669   -35.588 -48.615 1.00 48.73  ? 318 MET   B N   1 
ATOM   5367 C CA  . MET   B 1 318 ? 3.326   -35.593 -48.043 1.00 48.83  ? 318 MET   B CA  1 
ATOM   5368 C C   . MET   B 1 318 ? 2.258   -35.830 -49.106 1.00 46.64  ? 318 MET   B C   1 
ATOM   5369 O O   . MET   B 1 318 ? 1.295   -36.568 -48.867 1.00 43.89  ? 318 MET   B O   1 
ATOM   5370 C CB  . MET   B 1 318 ? 3.061   -34.278 -47.315 1.00 47.33  ? 318 MET   B CB  1 
ATOM   5371 C CG  . MET   B 1 318 ? 1.700   -34.217 -46.657 1.00 46.25  ? 318 MET   B CG  1 
ATOM   5372 S SD  . MET   B 1 318 ? 1.483   -32.753 -45.638 1.00 49.52  ? 318 MET   B SD  1 
ATOM   5373 C CE  . MET   B 1 318 ? 2.686   -33.058 -44.347 1.00 47.65  ? 318 MET   B CE  1 
ATOM   5374 N N   . LEU   B 1 319 ? 2.408   -35.204 -50.275 1.00 46.05  ? 319 LEU   B N   1 
ATOM   5375 C CA  . LEU   B 1 319 ? 1.446   -35.387 -51.359 1.00 47.39  ? 319 LEU   B CA  1 
ATOM   5376 C C   . LEU   B 1 319 ? 1.286   -36.862 -51.710 1.00 47.03  ? 319 LEU   B C   1 
ATOM   5377 O O   . LEU   B 1 319 ? 0.165   -37.374 -51.797 1.00 48.58  ? 319 LEU   B O   1 
ATOM   5378 C CB  . LEU   B 1 319 ? 1.888   -34.581 -52.583 1.00 47.18  ? 319 LEU   B CB  1 
ATOM   5379 C CG  . LEU   B 1 319 ? 1.009   -34.605 -53.834 1.00 50.13  ? 319 LEU   B CG  1 
ATOM   5380 C CD1 . LEU   B 1 319 ? -0.337  -33.957 -53.559 1.00 52.47  ? 319 LEU   B CD1 1 
ATOM   5381 C CD2 . LEU   B 1 319 ? 1.712   -33.905 -54.987 1.00 46.74  ? 319 LEU   B CD2 1 
ATOM   5382 N N   . LEU   B 1 320 ? 2.407   -37.565 -51.895 1.00 46.18  ? 320 LEU   B N   1 
ATOM   5383 C CA  . LEU   B 1 320 ? 2.350   -38.980 -52.254 1.00 46.89  ? 320 LEU   B CA  1 
ATOM   5384 C C   . LEU   B 1 320 ? 1.681   -39.806 -51.162 1.00 46.46  ? 320 LEU   B C   1 
ATOM   5385 O O   . LEU   B 1 320 ? 0.853   -40.678 -51.453 1.00 45.90  ? 320 LEU   B O   1 
ATOM   5386 C CB  . LEU   B 1 320 ? 3.758   -39.504 -52.537 1.00 48.15  ? 320 LEU   B CB  1 
ATOM   5387 C CG  . LEU   B 1 320 ? 4.428   -38.977 -53.807 1.00 48.49  ? 320 LEU   B CG  1 
ATOM   5388 C CD1 . LEU   B 1 320 ? 5.758   -39.673 -54.046 1.00 46.37  ? 320 LEU   B CD1 1 
ATOM   5389 C CD2 . LEU   B 1 320 ? 3.505   -39.153 -55.000 1.00 44.17  ? 320 LEU   B CD2 1 
ATOM   5390 N N   . VAL   B 1 321 ? 2.031   -39.551 -49.900 1.00 47.51  ? 321 VAL   B N   1 
ATOM   5391 C CA  . VAL   B 1 321 ? 1.411   -40.277 -48.795 1.00 46.08  ? 321 VAL   B CA  1 
ATOM   5392 C C   . VAL   B 1 321 ? -0.094  -40.039 -48.781 1.00 47.54  ? 321 VAL   B C   1 
ATOM   5393 O O   . VAL   B 1 321 ? -0.883  -40.971 -48.582 1.00 47.68  ? 321 VAL   B O   1 
ATOM   5394 C CB  . VAL   B 1 321 ? 2.066   -39.870 -47.460 1.00 48.93  ? 321 VAL   B CB  1 
ATOM   5395 C CG1 . VAL   B 1 321 ? 1.200   -40.297 -46.284 1.00 44.40  ? 321 VAL   B CG1 1 
ATOM   5396 C CG2 . VAL   B 1 321 ? 3.461   -40.471 -47.346 1.00 45.25  ? 321 VAL   B CG2 1 
ATOM   5397 N N   . VAL   B 1 322 ? -0.515  -38.794 -49.015 1.00 45.79  ? 322 VAL   B N   1 
ATOM   5398 C CA  . VAL   B 1 322 ? -1.938  -38.465 -48.995 1.00 46.04  ? 322 VAL   B CA  1 
ATOM   5399 C C   . VAL   B 1 322 ? -2.665  -39.160 -50.141 1.00 48.64  ? 322 VAL   B C   1 
ATOM   5400 O O   . VAL   B 1 322 ? -3.730  -39.759 -49.948 1.00 48.79  ? 322 VAL   B O   1 
ATOM   5401 C CB  . VAL   B 1 322 ? -2.137  -36.940 -49.046 1.00 46.72  ? 322 VAL   B CB  1 
ATOM   5402 C CG1 . VAL   B 1 322 ? -3.578  -36.601 -49.416 1.00 43.27  ? 322 VAL   B CG1 1 
ATOM   5403 C CG2 . VAL   B 1 322 ? -1.757  -36.308 -47.717 1.00 45.70  ? 322 VAL   B CG2 1 
ATOM   5404 N N   . LEU   B 1 323 ? -2.105  -39.086 -51.353 1.00 49.43  ? 323 LEU   B N   1 
ATOM   5405 C CA  . LEU   B 1 323 ? -2.752  -39.710 -52.504 1.00 49.45  ? 323 LEU   B CA  1 
ATOM   5406 C C   . LEU   B 1 323 ? -2.859  -41.220 -52.340 1.00 46.76  ? 323 LEU   B C   1 
ATOM   5407 O O   . LEU   B 1 323 ? -3.851  -41.823 -52.767 1.00 45.23  ? 323 LEU   B O   1 
ATOM   5408 C CB  . LEU   B 1 323 ? -1.996  -39.367 -53.789 1.00 47.68  ? 323 LEU   B CB  1 
ATOM   5409 C CG  . LEU   B 1 323 ? -1.872  -37.888 -54.155 1.00 46.21  ? 323 LEU   B CG  1 
ATOM   5410 C CD1 . LEU   B 1 323 ? -1.037  -37.736 -55.411 1.00 49.53  ? 323 LEU   B CD1 1 
ATOM   5411 C CD2 . LEU   B 1 323 ? -3.241  -37.251 -54.332 1.00 46.32  ? 323 LEU   B CD2 1 
ATOM   5412 N N   . ALA   B 1 324 ? -1.861  -41.846 -51.722 1.00 48.37  ? 324 ALA   B N   1 
ATOM   5413 C CA  . ALA   B 1 324 ? -1.897  -43.279 -51.471 1.00 48.69  ? 324 ALA   B CA  1 
ATOM   5414 C C   . ALA   B 1 324 ? -2.734  -43.646 -50.254 1.00 51.83  ? 324 ALA   B C   1 
ATOM   5415 O O   . ALA   B 1 324 ? -2.829  -44.835 -49.933 1.00 54.34  ? 324 ALA   B O   1 
ATOM   5416 C CB  . ALA   B 1 324 ? -0.476  -43.818 -51.299 1.00 51.57  ? 324 ALA   B CB  1 
ATOM   5417 N N   . ARG   B 1 325 ? -3.340  -42.662 -49.582 1.00 49.90  ? 325 ARG   B N   1 
ATOM   5418 C CA  . ARG   B 1 325 ? -4.134  -42.889 -48.373 1.00 51.34  ? 325 ARG   B CA  1 
ATOM   5419 C C   . ARG   B 1 325 ? -3.367  -43.739 -47.363 1.00 51.26  ? 325 ARG   B C   1 
ATOM   5420 O O   . ARG   B 1 325 ? -3.927  -44.608 -46.689 1.00 51.68  ? 325 ARG   B O   1 
ATOM   5421 C CB  . ARG   B 1 325 ? -5.490  -43.516 -48.708 1.00 49.43  ? 325 ARG   B CB  1 
ATOM   5422 C CG  . ARG   B 1 325 ? -6.415  -42.581 -49.474 1.00 53.46  ? 325 ARG   B CG  1 
ATOM   5423 C CD  . ARG   B 1 325 ? -7.893  -42.938 -49.340 1.00 57.88  ? 325 ARG   B CD  1 
ATOM   5424 N NE  . ARG   B 1 325 ? -8.316  -43.158 -47.961 1.00 56.49  ? 325 ARG   B NE  1 
ATOM   5425 C CZ  . ARG   B 1 325 ? -9.158  -42.371 -47.305 1.00 55.22  ? 325 ARG   B CZ  1 
ATOM   5426 N NH1 . ARG   B 1 325 ? -9.629  -41.258 -47.846 1.00 55.08  ? 325 ARG   B NH1 1 
ATOM   5427 N NH2 . ARG   B 1 325 ? -9.536  -42.706 -46.073 1.00 49.42  ? 325 ARG   B NH2 1 
ATOM   5428 N N   . GLY   B 1 326 ? -2.062  -43.486 -47.267 1.00 47.83  ? 326 GLY   B N   1 
ATOM   5429 C CA  . GLY   B 1 326 ? -1.203  -44.183 -46.335 1.00 51.06  ? 326 GLY   B CA  1 
ATOM   5430 C C   . GLY   B 1 326 ? -0.711  -45.541 -46.785 1.00 55.85  ? 326 GLY   B C   1 
ATOM   5431 O O   . GLY   B 1 326 ? 0.157   -46.116 -46.114 1.00 55.34  ? 326 GLY   B O   1 
ATOM   5432 N N   . LEU   B 1 327 ? -1.232  -46.080 -47.886 1.00 57.74  ? 327 LEU   B N   1 
ATOM   5433 C CA  . LEU   B 1 327 ? -0.786  -47.376 -48.375 1.00 57.57  ? 327 LEU   B CA  1 
ATOM   5434 C C   . LEU   B 1 327 ? 0.575   -47.254 -49.050 1.00 62.72  ? 327 LEU   B C   1 
ATOM   5435 O O   . LEU   B 1 327 ? 0.947   -46.197 -49.568 1.00 58.67  ? 327 LEU   B O   1 
ATOM   5436 C CB  . LEU   B 1 327 ? -1.796  -47.971 -49.358 1.00 55.04  ? 327 LEU   B CB  1 
ATOM   5437 C CG  . LEU   B 1 327 ? -3.129  -48.533 -48.843 1.00 55.40  ? 327 LEU   B CG  1 
ATOM   5438 C CD1 . LEU   B 1 327 ? -2.982  -49.224 -47.488 1.00 51.61  ? 327 LEU   B CD1 1 
ATOM   5439 C CD2 . LEU   B 1 327 ? -4.207  -47.460 -48.800 1.00 55.03  ? 327 LEU   B CD2 1 
ATOM   5440 N N   . ALA   B 1 328 ? 1.315   -48.355 -49.047 1.00 65.93  ? 328 ALA   B N   1 
ATOM   5441 C CA  . ALA   B 1 328 ? 2.668   -48.427 -49.569 1.00 71.01  ? 328 ALA   B CA  1 
ATOM   5442 C C   . ALA   B 1 328 ? 2.788   -49.608 -50.519 1.00 78.75  ? 328 ALA   B C   1 
ATOM   5443 O O   . ALA   B 1 328 ? 1.966   -50.530 -50.479 1.00 78.33  ? 328 ALA   B O   1 
ATOM   5444 C CB  . ALA   B 1 328 ? 3.686   -48.573 -48.428 1.00 71.57  ? 328 ALA   B CB  1 
ATOM   5445 N N   . PRO   B 1 329 ? 3.796   -49.608 -51.394 1.00 84.94  ? 329 PRO   B N   1 
ATOM   5446 C CA  . PRO   B 1 329 ? 4.066   -50.802 -52.204 1.00 88.40  ? 329 PRO   B CA  1 
ATOM   5447 C C   . PRO   B 1 329 ? 4.410   -51.999 -51.330 1.00 91.71  ? 329 PRO   B C   1 
ATOM   5448 O O   . PRO   B 1 329 ? 4.824   -51.867 -50.176 1.00 91.11  ? 329 PRO   B O   1 
ATOM   5449 C CB  . PRO   B 1 329 ? 5.264   -50.388 -53.071 1.00 88.25  ? 329 PRO   B CB  1 
ATOM   5450 C CG  . PRO   B 1 329 ? 5.242   -48.897 -53.066 1.00 86.47  ? 329 PRO   B CG  1 
ATOM   5451 C CD  . PRO   B 1 329 ? 4.720   -48.506 -51.721 1.00 84.22  ? 329 PRO   B CD  1 
ATOM   5452 N N   . GLU   B 1 330 ? 4.243   -53.191 -51.903 1.00 94.08  ? 330 GLU   B N   1 
ATOM   5453 C CA  . GLU   B 1 330 ? 4.500   -54.411 -51.146 1.00 98.95  ? 330 GLU   B CA  1 
ATOM   5454 C C   . GLU   B 1 330 ? 5.973   -54.575 -50.780 1.00 98.81  ? 330 GLU   B C   1 
ATOM   5455 O O   . GLU   B 1 330 ? 6.278   -55.252 -49.792 1.00 96.47  ? 330 GLU   B O   1 
ATOM   5456 C CB  . GLU   B 1 330 ? 4.004   -55.621 -51.935 1.00 101.98 ? 330 GLU   B CB  1 
ATOM   5457 C CG  . GLU   B 1 330 ? 2.884   -56.387 -51.249 1.00 103.53 ? 330 GLU   B CG  1 
ATOM   5458 C CD  . GLU   B 1 330 ? 2.065   -57.202 -52.225 1.00 110.21 ? 330 GLU   B CD  1 
ATOM   5459 O OE1 . GLU   B 1 330 ? 2.662   -58.014 -52.964 1.00 111.35 ? 330 GLU   B OE1 1 
ATOM   5460 O OE2 . GLU   B 1 330 ? 0.830   -57.019 -52.267 1.00 110.96 ? 330 GLU   B OE2 1 
ATOM   5461 N N   . GLY   B 1 331 ? 6.890   -53.958 -51.531 1.00 97.99  ? 331 GLY   B N   1 
ATOM   5462 C CA  . GLY   B 1 331 ? 8.300   -53.998 -51.192 1.00 95.90  ? 331 GLY   B CA  1 
ATOM   5463 C C   . GLY   B 1 331 ? 8.783   -52.901 -50.269 1.00 93.21  ? 331 GLY   B C   1 
ATOM   5464 O O   . GLY   B 1 331 ? 9.919   -52.961 -49.788 1.00 90.60  ? 331 GLY   B O   1 
ATOM   5465 N N   . THR   B 1 332 ? 7.951   -51.896 -50.015 1.00 91.88  ? 332 THR   B N   1 
ATOM   5466 C CA  . THR   B 1 332 ? 8.303   -50.765 -49.172 1.00 89.35  ? 332 THR   B CA  1 
ATOM   5467 C C   . THR   B 1 332 ? 7.507   -50.824 -47.874 1.00 85.60  ? 332 THR   B C   1 
ATOM   5468 O O   . THR   B 1 332 ? 6.484   -51.509 -47.777 1.00 84.21  ? 332 THR   B O   1 
ATOM   5469 C CB  . THR   B 1 332 ? 8.033   -49.440 -49.896 1.00 87.38  ? 332 THR   B CB  1 
ATOM   5470 O OG1 . THR   B 1 332 ? 8.413   -49.562 -51.272 1.00 92.76  ? 332 THR   B OG1 1 
ATOM   5471 C CG2 . THR   B 1 332 ? 8.835   -48.308 -49.273 1.00 83.19  ? 332 THR   B CG2 1 
ATOM   5472 N N   . GLU   B 1 333 ? 8.001   -50.108 -46.870 1.00 82.13  ? 333 GLU   B N   1 
ATOM   5473 C CA  . GLU   B 1 333 ? 7.269   -50.012 -45.615 1.00 78.63  ? 333 GLU   B CA  1 
ATOM   5474 C C   . GLU   B 1 333 ? 6.320   -48.819 -45.645 1.00 72.95  ? 333 GLU   B C   1 
ATOM   5475 O O   . GLU   B 1 333 ? 6.671   -47.758 -46.170 1.00 70.84  ? 333 GLU   B O   1 
ATOM   5476 C CB  . GLU   B 1 333 ? 8.227   -49.863 -44.439 1.00 78.18  ? 333 GLU   B CB  1 
ATOM   5477 C CG  . GLU   B 1 333 ? 8.953   -51.139 -44.073 1.00 81.90  ? 333 GLU   B CG  1 
ATOM   5478 C CD  . GLU   B 1 333 ? 8.205   -51.945 -43.033 1.00 85.77  ? 333 GLU   B CD  1 
ATOM   5479 O OE1 . GLU   B 1 333 ? 8.501   -51.793 -41.829 1.00 86.87  ? 333 GLU   B OE1 1 
ATOM   5480 O OE2 . GLU   B 1 333 ? 7.313   -52.725 -43.422 1.00 88.13  ? 333 GLU   B OE2 1 
ATOM   5481 N N   . PRO   B 1 334 ? 5.118   -48.970 -45.097 1.00 66.84  ? 334 PRO   B N   1 
ATOM   5482 C CA  . PRO   B 1 334 ? 4.214   -47.822 -44.998 1.00 63.45  ? 334 PRO   B CA  1 
ATOM   5483 C C   . PRO   B 1 334 ? 4.725   -46.815 -43.983 1.00 58.86  ? 334 PRO   B C   1 
ATOM   5484 O O   . PRO   B 1 334 ? 5.340   -47.170 -42.974 1.00 60.65  ? 334 PRO   B O   1 
ATOM   5485 C CB  . PRO   B 1 334 ? 2.892   -48.449 -44.543 1.00 58.79  ? 334 PRO   B CB  1 
ATOM   5486 C CG  . PRO   B 1 334 ? 3.306   -49.685 -43.822 1.00 61.43  ? 334 PRO   B CG  1 
ATOM   5487 C CD  . PRO   B 1 334 ? 4.521   -50.197 -44.545 1.00 65.67  ? 334 PRO   B CD  1 
ATOM   5488 N N   . VAL   B 1 335 ? 4.485   -45.536 -44.278 1.00 54.31  ? 335 VAL   B N   1 
ATOM   5489 C CA  . VAL   B 1 335 ? 4.741   -44.497 -43.291 1.00 49.66  ? 335 VAL   B CA  1 
ATOM   5490 C C   . VAL   B 1 335 ? 3.878   -44.766 -42.070 1.00 47.90  ? 335 VAL   B C   1 
ATOM   5491 O O   . VAL   B 1 335 ? 2.680   -45.054 -42.184 1.00 48.27  ? 335 VAL   B O   1 
ATOM   5492 C CB  . VAL   B 1 335 ? 4.471   -43.108 -43.890 1.00 48.70  ? 335 VAL   B CB  1 
ATOM   5493 C CG1 . VAL   B 1 335 ? 4.398   -42.060 -42.796 1.00 48.60  ? 335 VAL   B CG1 1 
ATOM   5494 C CG2 . VAL   B 1 335 ? 5.552   -42.746 -44.897 1.00 50.43  ? 335 VAL   B CG2 1 
ATOM   5495 N N   . SER   B 1 336 ? 4.490   -44.712 -40.893 1.00 47.66  ? 336 SER   B N   1 
ATOM   5496 C CA  . SER   B 1 336 ? 3.753   -44.980 -39.671 1.00 48.35  ? 336 SER   B CA  1 
ATOM   5497 C C   . SER   B 1 336 ? 2.921   -43.766 -39.267 1.00 45.92  ? 336 SER   B C   1 
ATOM   5498 O O   . SER   B 1 336 ? 3.188   -42.630 -39.673 1.00 43.56  ? 336 SER   B O   1 
ATOM   5499 C CB  . SER   B 1 336 ? 4.709   -45.370 -38.543 1.00 45.87  ? 336 SER   B CB  1 
ATOM   5500 O OG  . SER   B 1 336 ? 5.267   -44.221 -37.930 1.00 47.36  ? 336 SER   B OG  1 
ATOM   5501 N N   . LEU   B 1 337 ? 1.889   -44.026 -38.459 1.00 48.20  ? 337 LEU   B N   1 
ATOM   5502 C CA  . LEU   B 1 337 ? 1.049   -42.944 -37.952 1.00 48.13  ? 337 LEU   B CA  1 
ATOM   5503 C C   . LEU   B 1 337 ? 1.870   -41.935 -37.156 1.00 46.60  ? 337 LEU   B C   1 
ATOM   5504 O O   . LEU   B 1 337 ? 1.641   -40.723 -37.249 1.00 45.74  ? 337 LEU   B O   1 
ATOM   5505 C CB  . LEU   B 1 337 ? -0.083  -43.518 -37.096 1.00 45.04  ? 337 LEU   B CB  1 
ATOM   5506 C CG  . LEU   B 1 337 ? -1.152  -42.555 -36.567 1.00 47.22  ? 337 LEU   B CG  1 
ATOM   5507 C CD1 . LEU   B 1 337 ? -1.506  -41.509 -37.610 1.00 46.92  ? 337 LEU   B CD1 1 
ATOM   5508 C CD2 . LEU   B 1 337 ? -2.399  -43.312 -36.125 1.00 48.25  ? 337 LEU   B CD2 1 
ATOM   5509 N N   . ASN   B 1 338 ? 2.835   -42.418 -36.372 1.00 42.55  ? 338 ASN   B N   1 
ATOM   5510 C CA  . ASN   B 1 338 ? 3.694   -41.512 -35.618 1.00 43.01  ? 338 ASN   B CA  1 
ATOM   5511 C C   . ASN   B 1 338 ? 4.566   -40.675 -36.546 1.00 44.92  ? 338 ASN   B C   1 
ATOM   5512 O O   . ASN   B 1 338 ? 4.785   -39.483 -36.300 1.00 42.64  ? 338 ASN   B O   1 
ATOM   5513 C CB  . ASN   B 1 338 ? 4.562   -42.302 -34.641 1.00 47.78  ? 338 ASN   B CB  1 
ATOM   5514 C CG  . ASN   B 1 338 ? 5.383   -41.403 -33.744 1.00 49.64  ? 338 ASN   B CG  1 
ATOM   5515 O OD1 . ASN   B 1 338 ? 6.533   -41.088 -34.050 1.00 48.85  ? 338 ASN   B OD1 1 
ATOM   5516 N ND2 . ASN   B 1 338 ? 4.795   -40.978 -32.631 1.00 48.95  ? 338 ASN   B ND2 1 
ATOM   5517 N N   . ALA   B 1 339 ? 5.088   -41.286 -37.612 1.00 48.00  ? 339 ALA   B N   1 
ATOM   5518 C CA  . ALA   B 1 339 ? 5.858   -40.526 -38.590 1.00 45.24  ? 339 ALA   B CA  1 
ATOM   5519 C C   . ALA   B 1 339 ? 4.979   -39.533 -39.335 1.00 43.78  ? 339 ALA   B C   1 
ATOM   5520 O O   . ALA   B 1 339 ? 5.442   -38.446 -39.700 1.00 45.93  ? 339 ALA   B O   1 
ATOM   5521 C CB  . ALA   B 1 339 ? 6.547   -41.473 -39.569 1.00 43.90  ? 339 ALA   B CB  1 
ATOM   5522 N N   . TRP   B 1 340 ? 3.711   -39.885 -39.559 1.00 44.40  ? 340 TRP   B N   1 
ATOM   5523 C CA  . TRP   B 1 340 ? 2.775   -38.958 -40.186 1.00 44.19  ? 340 TRP   B CA  1 
ATOM   5524 C C   . TRP   B 1 340 ? 2.563   -37.719 -39.324 1.00 42.99  ? 340 TRP   B C   1 
ATOM   5525 O O   . TRP   B 1 340 ? 2.534   -36.595 -39.839 1.00 45.77  ? 340 TRP   B O   1 
ATOM   5526 C CB  . TRP   B 1 340 ? 1.445   -39.665 -40.448 1.00 44.95  ? 340 TRP   B CB  1 
ATOM   5527 C CG  . TRP   B 1 340 ? 0.353   -38.753 -40.922 1.00 47.81  ? 340 TRP   B CG  1 
ATOM   5528 C CD1 . TRP   B 1 340 ? -0.779  -38.404 -40.242 1.00 44.05  ? 340 TRP   B CD1 1 
ATOM   5529 C CD2 . TRP   B 1 340 ? 0.287   -38.080 -42.185 1.00 47.72  ? 340 TRP   B CD2 1 
ATOM   5530 N NE1 . TRP   B 1 340 ? -1.543  -37.553 -41.003 1.00 43.76  ? 340 TRP   B NE1 1 
ATOM   5531 C CE2 . TRP   B 1 340 ? -0.911  -37.338 -42.200 1.00 45.73  ? 340 TRP   B CE2 1 
ATOM   5532 C CE3 . TRP   B 1 340 ? 1.125   -38.032 -43.304 1.00 48.41  ? 340 TRP   B CE3 1 
ATOM   5533 C CZ2 . TRP   B 1 340 ? -1.291  -36.557 -43.291 1.00 48.73  ? 340 TRP   B CZ2 1 
ATOM   5534 C CZ3 . TRP   B 1 340 ? 0.747   -37.256 -44.384 1.00 48.86  ? 340 TRP   B CZ3 1 
ATOM   5535 C CH2 . TRP   B 1 340 ? -0.450  -36.529 -44.369 1.00 48.30  ? 340 TRP   B CH2 1 
ATOM   5536 N N   . TYR   B 1 341 ? 2.413   -37.907 -38.009 1.00 42.23  ? 341 TYR   B N   1 
ATOM   5537 C CA  . TYR   B 1 341 ? 2.240   -36.770 -37.108 1.00 42.92  ? 341 TYR   B CA  1 
ATOM   5538 C C   . TYR   B 1 341 ? 3.451   -35.849 -37.146 1.00 43.78  ? 341 TYR   B C   1 
ATOM   5539 O O   . TYR   B 1 341 ? 3.308   -34.620 -37.152 1.00 44.34  ? 341 TYR   B O   1 
ATOM   5540 C CB  . TYR   B 1 341 ? 1.992   -37.262 -35.682 1.00 42.79  ? 341 TYR   B CB  1 
ATOM   5541 C CG  . TYR   B 1 341 ? 0.620   -37.858 -35.461 1.00 46.44  ? 341 TYR   B CG  1 
ATOM   5542 C CD1 . TYR   B 1 341 ? -0.488  -37.389 -36.159 1.00 44.92  ? 341 TYR   B CD1 1 
ATOM   5543 C CD2 . TYR   B 1 341 ? 0.432   -38.893 -34.555 1.00 44.79  ? 341 TYR   B CD2 1 
ATOM   5544 C CE1 . TYR   B 1 341 ? -1.745  -37.933 -35.955 1.00 43.76  ? 341 TYR   B CE1 1 
ATOM   5545 C CE2 . TYR   B 1 341 ? -0.816  -39.442 -34.346 1.00 45.65  ? 341 TYR   B CE2 1 
ATOM   5546 C CZ  . TYR   B 1 341 ? -1.902  -38.961 -35.047 1.00 47.17  ? 341 TYR   B CZ  1 
ATOM   5547 O OH  . TYR   B 1 341 ? -3.145  -39.517 -34.836 1.00 44.65  ? 341 TYR   B OH  1 
ATOM   5548 N N   . ALA   B 1 342 ? 4.653   -36.427 -37.168 1.00 43.53  ? 342 ALA   B N   1 
ATOM   5549 C CA  . ALA   B 1 342 ? 5.864   -35.622 -37.284 1.00 42.89  ? 342 ALA   B CA  1 
ATOM   5550 C C   . ALA   B 1 342 ? 5.880   -34.840 -38.592 1.00 44.29  ? 342 ALA   B C   1 
ATOM   5551 O O   . ALA   B 1 342 ? 6.342   -33.693 -38.632 1.00 45.06  ? 342 ALA   B O   1 
ATOM   5552 C CB  . ALA   B 1 342 ? 7.098   -36.517 -37.176 1.00 40.16  ? 342 ALA   B CB  1 
ATOM   5553 N N   . MET   B 1 343 ? 5.380   -35.446 -39.674 1.00 42.93  ? 343 MET   B N   1 
ATOM   5554 C CA  . MET   B 1 343 ? 5.289   -34.740 -40.949 1.00 44.37  ? 343 MET   B CA  1 
ATOM   5555 C C   . MET   B 1 343 ? 4.334   -33.559 -40.853 1.00 42.07  ? 343 MET   B C   1 
ATOM   5556 O O   . MET   B 1 343 ? 4.560   -32.513 -41.472 1.00 45.35  ? 343 MET   B O   1 
ATOM   5557 C CB  . MET   B 1 343 ? 4.838   -35.698 -42.054 1.00 45.73  ? 343 MET   B CB  1 
ATOM   5558 C CG  . MET   B 1 343 ? 5.892   -36.700 -42.506 1.00 44.66  ? 343 MET   B CG  1 
ATOM   5559 S SD  . MET   B 1 343 ? 5.212   -37.957 -43.608 1.00 48.70  ? 343 MET   B SD  1 
ATOM   5560 C CE  . MET   B 1 343 ? 4.433   -36.936 -44.855 1.00 49.06  ? 343 MET   B CE  1 
ATOM   5561 N N   . LEU   B 1 344 ? 3.254   -33.707 -40.084 1.00 43.00  ? 344 LEU   B N   1 
ATOM   5562 C CA  . LEU   B 1 344 ? 2.353   -32.583 -39.871 1.00 46.01  ? 344 LEU   B CA  1 
ATOM   5563 C C   . LEU   B 1 344 ? 3.015   -31.493 -39.039 1.00 44.96  ? 344 LEU   B C   1 
ATOM   5564 O O   . LEU   B 1 344 ? 2.726   -30.307 -39.235 1.00 43.39  ? 344 LEU   B O   1 
ATOM   5565 C CB  . LEU   B 1 344 ? 1.060   -33.061 -39.215 1.00 42.56  ? 344 LEU   B CB  1 
ATOM   5566 C CG  . LEU   B 1 344 ? 0.219   -33.965 -40.117 1.00 41.52  ? 344 LEU   B CG  1 
ATOM   5567 C CD1 . LEU   B 1 344 ? -0.953  -34.558 -39.359 1.00 40.21  ? 344 LEU   B CD1 1 
ATOM   5568 C CD2 . LEU   B 1 344 ? -0.253  -33.199 -41.346 1.00 40.80  ? 344 LEU   B CD2 1 
ATOM   5569 N N   . ASP   B 1 345 ? 3.906   -31.871 -38.117 1.00 42.09  ? 345 ASP   B N   1 
ATOM   5570 C CA  . ASP   B 1 345 ? 4.694   -30.870 -37.406 1.00 44.93  ? 345 ASP   B CA  1 
ATOM   5571 C C   . ASP   B 1 345 ? 5.669   -30.176 -38.348 1.00 45.42  ? 345 ASP   B C   1 
ATOM   5572 O O   . ASP   B 1 345 ? 5.878   -28.961 -38.247 1.00 45.98  ? 345 ASP   B O   1 
ATOM   5573 C CB  . ASP   B 1 345 ? 5.443   -31.510 -36.238 1.00 44.09  ? 345 ASP   B CB  1 
ATOM   5574 C CG  . ASP   B 1 345 ? 4.532   -31.845 -35.073 1.00 46.32  ? 345 ASP   B CG  1 
ATOM   5575 O OD1 . ASP   B 1 345 ? 3.563   -31.091 -34.833 1.00 46.33  ? 345 ASP   B OD1 1 
ATOM   5576 O OD2 . ASP   B 1 345 ? 4.787   -32.860 -34.393 1.00 46.71  ? 345 ASP   B OD2 1 
ATOM   5577 N N   . ASP   B 1 346 ? 6.280   -30.936 -39.264 1.00 44.68  ? 346 ASP   B N   1 
ATOM   5578 C CA  . ASP   B 1 346 ? 7.145   -30.331 -40.273 1.00 47.68  ? 346 ASP   B CA  1 
ATOM   5579 C C   . ASP   B 1 346 ? 6.385   -29.306 -41.100 1.00 43.56  ? 346 ASP   B C   1 
ATOM   5580 O O   . ASP   B 1 346 ? 6.915   -28.232 -41.409 1.00 42.43  ? 346 ASP   B O   1 
ATOM   5581 C CB  . ASP   B 1 346 ? 7.743   -31.403 -41.186 1.00 47.69  ? 346 ASP   B CB  1 
ATOM   5582 C CG  . ASP   B 1 346 ? 8.545   -32.441 -40.429 1.00 50.96  ? 346 ASP   B CG  1 
ATOM   5583 O OD1 . ASP   B 1 346 ? 9.180   -32.085 -39.411 1.00 51.17  ? 346 ASP   B OD1 1 
ATOM   5584 O OD2 . ASP   B 1 346 ? 8.544   -33.616 -40.857 1.00 50.44  ? 346 ASP   B OD2 1 
ATOM   5585 N N   . GLN   B 1 347 ? 5.142   -29.621 -41.472 1.00 40.76  ? 347 GLN   B N   1 
ATOM   5586 C CA  . GLN   B 1 347 ? 4.329   -28.657 -42.208 1.00 43.81  ? 347 GLN   B CA  1 
ATOM   5587 C C   . GLN   B 1 347 ? 4.058   -27.413 -41.369 1.00 45.11  ? 347 GLN   B C   1 
ATOM   5588 O O   . GLN   B 1 347 ? 4.194   -26.284 -41.854 1.00 43.81  ? 347 GLN   B O   1 
ATOM   5589 C CB  . GLN   B 1 347 ? 3.017   -29.302 -42.656 1.00 43.91  ? 347 GLN   B CB  1 
ATOM   5590 C CG  . GLN   B 1 347 ? 2.196   -28.428 -43.593 1.00 43.72  ? 347 GLN   B CG  1 
ATOM   5591 C CD  . GLN   B 1 347 ? 0.888   -29.078 -44.006 1.00 44.02  ? 347 GLN   B CD  1 
ATOM   5592 O OE1 . GLN   B 1 347 ? 0.314   -29.870 -43.263 1.00 39.15  ? 347 GLN   B OE1 1 
ATOM   5593 N NE2 . GLN   B 1 347 ? 0.413   -28.747 -45.201 1.00 42.03  ? 347 GLN   B NE2 1 
ATOM   5594 N N   . ALA   B 1 348 ? 3.670   -27.600 -40.102 1.00 44.02  ? 348 ALA   B N   1 
ATOM   5595 C CA  . ALA   B 1 348 ? 3.411   -26.452 -39.236 1.00 44.40  ? 348 ALA   B CA  1 
ATOM   5596 C C   . ALA   B 1 348 ? 4.659   -25.600 -39.058 1.00 42.90  ? 348 ALA   B C   1 
ATOM   5597 O O   . ALA   B 1 348 ? 4.562   -24.372 -38.954 1.00 43.82  ? 348 ALA   B O   1 
ATOM   5598 C CB  . ALA   B 1 348 ? 2.883   -26.916 -37.880 1.00 40.16  ? 348 ALA   B CB  1 
ATOM   5599 N N   . ARG   B 1 349 ? 5.836   -26.231 -39.035 1.00 42.54  ? 349 ARG   B N   1 
ATOM   5600 C CA  . ARG   B 1 349 ? 7.085   -25.478 -39.012 1.00 47.18  ? 349 ARG   B CA  1 
ATOM   5601 C C   . ARG   B 1 349 ? 7.236   -24.621 -40.262 1.00 43.94  ? 349 ARG   B C   1 
ATOM   5602 O O   . ARG   B 1 349 ? 7.642   -23.456 -40.181 1.00 46.41  ? 349 ARG   B O   1 
ATOM   5603 C CB  . ARG   B 1 349 ? 8.267   -26.436 -38.880 1.00 48.43  ? 349 ARG   B CB  1 
ATOM   5604 C CG  . ARG   B 1 349 ? 9.516   -25.824 -38.271 1.00 48.74  ? 349 ARG   B CG  1 
ATOM   5605 C CD  . ARG   B 1 349 ? 10.489  -26.917 -37.870 1.00 48.28  ? 349 ARG   B CD  1 
ATOM   5606 N NE  . ARG   B 1 349 ? 9.844   -27.897 -37.003 1.00 48.64  ? 349 ARG   B NE  1 
ATOM   5607 C CZ  . ARG   B 1 349 ? 9.624   -29.161 -37.335 1.00 51.22  ? 349 ARG   B CZ  1 
ATOM   5608 N NH1 . ARG   B 1 349 ? 9.989   -29.640 -38.513 1.00 49.70  ? 349 ARG   B NH1 1 
ATOM   5609 N NH2 . ARG   B 1 349 ? 9.020   -29.965 -36.464 1.00 50.68  ? 349 ARG   B NH2 1 
ATOM   5610 N N   . MET   B 1 350 ? 6.911   -25.180 -41.430 1.00 42.19  ? 350 MET   B N   1 
ATOM   5611 C CA  . MET   B 1 350 ? 7.018   -24.415 -42.668 1.00 45.49  ? 350 MET   B CA  1 
ATOM   5612 C C   . MET   B 1 350 ? 6.004   -23.277 -42.711 1.00 45.98  ? 350 MET   B C   1 
ATOM   5613 O O   . MET   B 1 350 ? 6.320   -22.180 -43.187 1.00 48.17  ? 350 MET   B O   1 
ATOM   5614 C CB  . MET   B 1 350 ? 6.848   -25.338 -43.875 1.00 46.04  ? 350 MET   B CB  1 
ATOM   5615 C CG  . MET   B 1 350 ? 7.260   -24.696 -45.193 1.00 49.56  ? 350 MET   B CG  1 
ATOM   5616 S SD  . MET   B 1 350 ? 9.015   -24.266 -45.312 1.00 55.33  ? 350 MET   B SD  1 
ATOM   5617 C CE  . MET   B 1 350 ? 9.762   -25.881 -45.519 1.00 53.88  ? 350 MET   B CE  1 
ATOM   5618 N N   . MET   B 1 351 ? 4.782   -23.511 -42.219 1.00 44.96  ? 351 MET   B N   1 
ATOM   5619 C CA  . MET   B 1 351 ? 3.774   -22.454 -42.232 1.00 45.31  ? 351 MET   B CA  1 
ATOM   5620 C C   . MET   B 1 351 ? 4.191   -21.284 -41.352 1.00 47.33  ? 351 MET   B C   1 
ATOM   5621 O O   . MET   B 1 351 ? 4.007   -20.120 -41.728 1.00 47.26  ? 351 MET   B O   1 
ATOM   5622 C CB  . MET   B 1 351 ? 2.416   -22.995 -41.782 1.00 41.82  ? 351 MET   B CB  1 
ATOM   5623 C CG  . MET   B 1 351 ? 1.943   -24.222 -42.538 1.00 45.73  ? 351 MET   B CG  1 
ATOM   5624 S SD  . MET   B 1 351 ? 0.422   -24.898 -41.844 1.00 48.94  ? 351 MET   B SD  1 
ATOM   5625 C CE  . MET   B 1 351 ? -0.416  -25.439 -43.329 1.00 47.37  ? 351 MET   B CE  1 
ATOM   5626 N N   . ARG   B 1 352 ? 4.757   -21.572 -40.175 1.00 48.02  ? 352 ARG   B N   1 
ATOM   5627 C CA  . ARG   B 1 352 ? 5.242   -20.502 -39.309 1.00 46.26  ? 352 ARG   B CA  1 
ATOM   5628 C C   . ARG   B 1 352 ? 6.376   -19.724 -39.963 1.00 49.32  ? 352 ARG   B C   1 
ATOM   5629 O O   . ARG   B 1 352 ? 6.522   -18.523 -39.713 1.00 52.54  ? 352 ARG   B O   1 
ATOM   5630 C CB  . ARG   B 1 352 ? 5.693   -21.067 -37.962 1.00 45.46  ? 352 ARG   B CB  1 
ATOM   5631 C CG  . ARG   B 1 352 ? 4.549   -21.424 -37.028 1.00 46.04  ? 352 ARG   B CG  1 
ATOM   5632 C CD  . ARG   B 1 352 ? 5.044   -21.861 -35.658 1.00 45.39  ? 352 ARG   B CD  1 
ATOM   5633 N NE  . ARG   B 1 352 ? 6.331   -22.541 -35.723 1.00 48.77  ? 352 ARG   B NE  1 
ATOM   5634 C CZ  . ARG   B 1 352 ? 6.494   -23.849 -35.580 1.00 47.05  ? 352 ARG   B CZ  1 
ATOM   5635 N NH1 . ARG   B 1 352 ? 5.462   -24.658 -35.400 1.00 45.78  ? 352 ARG   B NH1 1 
ATOM   5636 N NH2 . ARG   B 1 352 ? 7.721   -24.359 -35.625 1.00 46.96  ? 352 ARG   B NH2 1 
ATOM   5637 N N   . ALA   B 1 353 ? 7.179   -20.383 -40.802 1.00 48.00  ? 353 ALA   B N   1 
ATOM   5638 C CA  . ALA   B 1 353 ? 8.220   -19.670 -41.535 1.00 49.89  ? 353 ALA   B CA  1 
ATOM   5639 C C   . ALA   B 1 353 ? 7.616   -18.661 -42.501 1.00 48.86  ? 353 ALA   B C   1 
ATOM   5640 O O   . ALA   B 1 353 ? 8.174   -17.578 -42.711 1.00 49.77  ? 353 ALA   B O   1 
ATOM   5641 C CB  . ALA   B 1 353 ? 9.113   -20.659 -42.283 1.00 49.53  ? 353 ALA   B CB  1 
ATOM   5642 N N   . PHE   B 1 354 ? 6.469   -18.995 -43.092 1.00 50.91  ? 354 PHE   B N   1 
ATOM   5643 C CA  . PHE   B 1 354 ? 5.806   -18.068 -43.999 1.00 49.37  ? 354 PHE   B CA  1 
ATOM   5644 C C   . PHE   B 1 354 ? 5.110   -16.943 -43.248 1.00 50.06  ? 354 PHE   B C   1 
ATOM   5645 O O   . PHE   B 1 354 ? 5.008   -15.828 -43.770 1.00 50.66  ? 354 PHE   B O   1 
ATOM   5646 C CB  . PHE   B 1 354 ? 4.815   -18.827 -44.876 1.00 46.28  ? 354 PHE   B CB  1 
ATOM   5647 C CG  . PHE   B 1 354 ? 5.432   -19.391 -46.116 1.00 48.47  ? 354 PHE   B CG  1 
ATOM   5648 C CD1 . PHE   B 1 354 ? 5.877   -18.559 -47.131 1.00 52.00  ? 354 PHE   B CD1 1 
ATOM   5649 C CD2 . PHE   B 1 354 ? 5.606   -20.756 -46.249 1.00 46.74  ? 354 PHE   B CD2 1 
ATOM   5650 C CE1 . PHE   B 1 354 ? 6.461   -19.086 -48.271 1.00 51.13  ? 354 PHE   B CE1 1 
ATOM   5651 C CE2 . PHE   B 1 354 ? 6.186   -21.287 -47.381 1.00 49.09  ? 354 PHE   B CE2 1 
ATOM   5652 C CZ  . PHE   B 1 354 ? 6.616   -20.452 -48.395 1.00 48.62  ? 354 PHE   B CZ  1 
ATOM   5653 N N   . ASP   B 1 355 ? 4.635   -17.214 -42.030 1.00 50.69  ? 355 ASP   B N   1 
ATOM   5654 C CA  . ASP   B 1 355 ? 4.113   -16.150 -41.177 1.00 52.00  ? 355 ASP   B CA  1 
ATOM   5655 C C   . ASP   B 1 355 ? 5.133   -15.031 -41.022 1.00 51.99  ? 355 ASP   B C   1 
ATOM   5656 O O   . ASP   B 1 355 ? 4.809   -13.851 -41.193 1.00 55.17  ? 355 ASP   B O   1 
ATOM   5657 C CB  . ASP   B 1 355 ? 3.735   -16.713 -39.806 1.00 51.20  ? 355 ASP   B CB  1 
ATOM   5658 C CG  . ASP   B 1 355 ? 2.591   -17.707 -39.871 1.00 53.48  ? 355 ASP   B CG  1 
ATOM   5659 O OD1 . ASP   B 1 355 ? 2.183   -18.206 -38.801 1.00 56.76  ? 355 ASP   B OD1 1 
ATOM   5660 O OD2 . ASP   B 1 355 ? 2.092   -17.980 -40.984 1.00 55.63  ? 355 ASP   B OD2 1 
ATOM   5661 N N   . ARG   B 1 356 ? 6.378   -15.390 -40.696 1.00 54.60  ? 356 ARG   B N   1 
ATOM   5662 C CA  . ARG   B 1 356 ? 7.417   -14.383 -40.510 1.00 56.53  ? 356 ARG   B CA  1 
ATOM   5663 C C   . ARG   B 1 356 ? 7.725   -13.658 -41.812 1.00 55.38  ? 356 ARG   B C   1 
ATOM   5664 O O   . ARG   B 1 356 ? 7.904   -12.434 -41.820 1.00 58.23  ? 356 ARG   B O   1 
ATOM   5665 C CB  . ARG   B 1 356 ? 8.684   -15.025 -39.945 1.00 56.91  ? 356 ARG   B CB  1 
ATOM   5666 C CG  . ARG   B 1 356 ? 8.756   -15.021 -38.424 1.00 65.08  ? 356 ARG   B CG  1 
ATOM   5667 C CD  . ARG   B 1 356 ? 8.490   -16.399 -37.854 1.00 64.39  ? 356 ARG   B CD  1 
ATOM   5668 N NE  . ARG   B 1 356 ? 9.397   -17.387 -38.425 1.00 66.85  ? 356 ARG   B NE  1 
ATOM   5669 C CZ  . ARG   B 1 356 ? 9.664   -18.565 -37.881 1.00 64.32  ? 356 ARG   B CZ  1 
ATOM   5670 N NH1 . ARG   B 1 356 ? 9.116   -18.938 -36.736 1.00 65.71  ? 356 ARG   B NH1 1 
ATOM   5671 N NH2 . ARG   B 1 356 ? 10.503  -19.391 -38.503 1.00 62.89  ? 356 ARG   B NH2 1 
ATOM   5672 N N   . LEU   B 1 357 ? 7.808   -14.398 -42.921 1.00 53.72  ? 357 LEU   B N   1 
ATOM   5673 C CA  . LEU   B 1 357 ? 8.024   -13.761 -44.216 1.00 52.13  ? 357 LEU   B CA  1 
ATOM   5674 C C   . LEU   B 1 357 ? 6.929   -12.748 -44.516 1.00 51.35  ? 357 LEU   B C   1 
ATOM   5675 O O   . LEU   B 1 357 ? 7.199   -11.671 -45.061 1.00 53.30  ? 357 LEU   B O   1 
ATOM   5676 C CB  . LEU   B 1 357 ? 8.090   -14.820 -45.317 1.00 53.53  ? 357 LEU   B CB  1 
ATOM   5677 C CG  . LEU   B 1 357 ? 8.011   -14.274 -46.744 1.00 51.83  ? 357 LEU   B CG  1 
ATOM   5678 C CD1 . LEU   B 1 357 ? 9.267   -13.487 -47.087 1.00 53.40  ? 357 LEU   B CD1 1 
ATOM   5679 C CD2 . LEU   B 1 357 ? 7.781   -15.397 -47.743 1.00 52.85  ? 357 LEU   B CD2 1 
ATOM   5680 N N   . PHE   B 1 358 ? 5.692   -13.068 -44.153 1.00 49.77  ? 358 PHE   B N   1 
ATOM   5681 C CA  . PHE   B 1 358 ? 4.561   -12.195 -44.426 1.00 49.99  ? 358 PHE   B CA  1 
ATOM   5682 C C   . PHE   B 1 358 ? 4.430   -11.057 -43.422 1.00 51.98  ? 358 PHE   B C   1 
ATOM   5683 O O   . PHE   B 1 358 ? 3.562   -10.195 -43.599 1.00 52.08  ? 358 PHE   B O   1 
ATOM   5684 C CB  . PHE   B 1 358 ? 3.277   -13.026 -44.471 1.00 48.41  ? 358 PHE   B CB  1 
ATOM   5685 C CG  . PHE   B 1 358 ? 3.034   -13.670 -45.806 1.00 49.46  ? 358 PHE   B CG  1 
ATOM   5686 C CD1 . PHE   B 1 358 ? 2.915   -12.896 -46.951 1.00 46.89  ? 358 PHE   B CD1 1 
ATOM   5687 C CD2 . PHE   B 1 358 ? 2.959   -15.052 -45.923 1.00 47.35  ? 358 PHE   B CD2 1 
ATOM   5688 C CE1 . PHE   B 1 358 ? 2.703   -13.487 -48.186 1.00 47.50  ? 358 PHE   B CE1 1 
ATOM   5689 C CE2 . PHE   B 1 358 ? 2.749   -15.651 -47.155 1.00 46.53  ? 358 PHE   B CE2 1 
ATOM   5690 C CZ  . PHE   B 1 358 ? 2.622   -14.867 -48.289 1.00 44.61  ? 358 PHE   B CZ  1 
ATOM   5691 N N   . GLU   B 1 359 ? 5.266   -11.024 -42.379 1.00 51.65  ? 359 GLU   B N   1 
ATOM   5692 C CA  . GLU   B 1 359 ? 5.368   -9.811  -41.574 1.00 54.41  ? 359 GLU   B CA  1 
ATOM   5693 C C   . GLU   B 1 359 ? 6.059   -8.696  -42.346 1.00 52.97  ? 359 GLU   B C   1 
ATOM   5694 O O   . GLU   B 1 359 ? 5.800   -7.515  -42.091 1.00 51.09  ? 359 GLU   B O   1 
ATOM   5695 C CB  . GLU   B 1 359 ? 6.110   -10.090 -40.266 1.00 54.84  ? 359 GLU   B CB  1 
ATOM   5696 C CG  . GLU   B 1 359 ? 5.509   -11.207 -39.424 1.00 56.51  ? 359 GLU   B CG  1 
ATOM   5697 C CD  . GLU   B 1 359 ? 6.464   -11.714 -38.358 1.00 64.31  ? 359 GLU   B CD  1 
ATOM   5698 O OE1 . GLU   B 1 359 ? 7.637   -11.281 -38.353 1.00 68.14  ? 359 GLU   B OE1 1 
ATOM   5699 O OE2 . GLU   B 1 359 ? 6.042   -12.553 -37.533 1.00 66.55  ? 359 GLU   B OE2 1 
ATOM   5700 N N   . SER   B 1 360 ? 6.918   -9.050  -43.304 1.00 51.71  ? 360 SER   B N   1 
ATOM   5701 C CA  . SER   B 1 360 ? 7.646   -8.085  -44.118 1.00 53.28  ? 360 SER   B CA  1 
ATOM   5702 C C   . SER   B 1 360 ? 7.044   -7.884  -45.501 1.00 55.10  ? 360 SER   B C   1 
ATOM   5703 O O   . SER   B 1 360 ? 7.505   -7.004  -46.234 1.00 55.06  ? 360 SER   B O   1 
ATOM   5704 C CB  . SER   B 1 360 ? 9.106   -8.525  -44.280 1.00 53.76  ? 360 SER   B CB  1 
ATOM   5705 O OG  . SER   B 1 360 ? 9.897   -8.107  -43.186 1.00 60.35  ? 360 SER   B OG  1 
ATOM   5706 N N   . PHE   B 1 361 ? 6.039   -8.671  -45.878 1.00 53.70  ? 361 PHE   B N   1 
ATOM   5707 C CA  . PHE   B 1 361 ? 5.534   -8.651  -47.241 1.00 51.13  ? 361 PHE   B CA  1 
ATOM   5708 C C   . PHE   B 1 361 ? 4.031   -8.882  -47.243 1.00 52.55  ? 361 PHE   B C   1 
ATOM   5709 O O   . PHE   B 1 361 ? 3.516   -9.680  -46.455 1.00 53.27  ? 361 PHE   B O   1 
ATOM   5710 C CB  . PHE   B 1 361 ? 6.228   -9.717  -48.093 1.00 49.94  ? 361 PHE   B CB  1 
ATOM   5711 C CG  . PHE   B 1 361 ? 7.656   -9.395  -48.407 1.00 53.93  ? 361 PHE   B CG  1 
ATOM   5712 C CD1 . PHE   B 1 361 ? 7.973   -8.461  -49.380 1.00 54.76  ? 361 PHE   B CD1 1 
ATOM   5713 C CD2 . PHE   B 1 361 ? 8.683   -10.012 -47.715 1.00 53.85  ? 361 PHE   B CD2 1 
ATOM   5714 C CE1 . PHE   B 1 361 ? 9.293   -8.161  -49.664 1.00 53.31  ? 361 PHE   B CE1 1 
ATOM   5715 C CE2 . PHE   B 1 361 ? 10.002  -9.715  -47.993 1.00 53.94  ? 361 PHE   B CE2 1 
ATOM   5716 C CZ  . PHE   B 1 361 ? 10.308  -8.789  -48.968 1.00 52.03  ? 361 PHE   B CZ  1 
ATOM   5717 N N   . ASP   B 1 362 ? 3.338   -8.181  -48.143 1.00 51.82  ? 362 ASP   B N   1 
ATOM   5718 C CA  . ASP   B 1 362 ? 1.905   -8.371  -48.333 1.00 50.93  ? 362 ASP   B CA  1 
ATOM   5719 C C   . ASP   B 1 362 ? 1.581   -9.468  -49.338 1.00 48.31  ? 362 ASP   B C   1 
ATOM   5720 O O   . ASP   B 1 362 ? 0.559   -10.147 -49.192 1.00 46.82  ? 362 ASP   B O   1 
ATOM   5721 C CB  . ASP   B 1 362 ? 1.252   -7.066  -48.793 1.00 50.61  ? 362 ASP   B CB  1 
ATOM   5722 C CG  . ASP   B 1 362 ? 1.517   -5.916  -47.847 1.00 52.10  ? 362 ASP   B CG  1 
ATOM   5723 O OD1 . ASP   B 1 362 ? 2.289   -5.001  -48.212 1.00 54.74  ? 362 ASP   B OD1 1 
ATOM   5724 O OD2 . ASP   B 1 362 ? 0.950   -5.927  -46.735 1.00 57.72  ? 362 ASP   B OD2 1 
ATOM   5725 N N   . ALA   B 1 363 ? 2.422   -9.660  -50.351 1.00 45.86  ? 363 ALA   B N   1 
ATOM   5726 C CA  . ALA   B 1 363 ? 2.165   -10.671 -51.363 1.00 47.84  ? 363 ALA   B CA  1 
ATOM   5727 C C   . ALA   B 1 363 ? 3.484   -11.169 -51.935 1.00 47.17  ? 363 ALA   B C   1 
ATOM   5728 O O   . ALA   B 1 363 ? 4.516   -10.498 -51.854 1.00 49.57  ? 363 ALA   B O   1 
ATOM   5729 C CB  . ALA   B 1 363 ? 1.278   -10.129 -52.490 1.00 45.31  ? 363 ALA   B CB  1 
ATOM   5730 N N   . ILE   B 1 364 ? 3.433   -12.363 -52.517 1.00 42.37  ? 364 ILE   B N   1 
ATOM   5731 C CA  . ILE   B 1 364 ? 4.519   -12.901 -53.327 1.00 45.85  ? 364 ILE   B CA  1 
ATOM   5732 C C   . ILE   B 1 364 ? 4.049   -12.926 -54.773 1.00 49.14  ? 364 ILE   B C   1 
ATOM   5733 O O   . ILE   B 1 364 ? 2.924   -13.356 -55.059 1.00 47.87  ? 364 ILE   B O   1 
ATOM   5734 C CB  . ILE   B 1 364 ? 4.945   -14.305 -52.864 1.00 41.00  ? 364 ILE   B CB  1 
ATOM   5735 C CG1 . ILE   B 1 364 ? 5.458   -14.268 -51.427 1.00 44.82  ? 364 ILE   B CG1 1 
ATOM   5736 C CG2 . ILE   B 1 364 ? 6.013   -14.875 -53.786 1.00 45.85  ? 364 ILE   B CG2 1 
ATOM   5737 C CD1 . ILE   B 1 364 ? 5.667   -15.637 -50.834 1.00 45.16  ? 364 ILE   B CD1 1 
ATOM   5738 N N   . PHE   B 1 365 ? 4.893   -12.442 -55.678 1.00 51.06  ? 365 PHE   B N   1 
ATOM   5739 C CA  . PHE   B 1 365 ? 4.646   -12.537 -57.111 1.00 51.31  ? 365 PHE   B CA  1 
ATOM   5740 C C   . PHE   B 1 365 ? 5.595   -13.585 -57.674 1.00 48.80  ? 365 PHE   B C   1 
ATOM   5741 O O   . PHE   B 1 365 ? 6.813   -13.473 -57.503 1.00 48.79  ? 365 PHE   B O   1 
ATOM   5742 C CB  . PHE   B 1 365 ? 4.851   -11.192 -57.809 1.00 47.19  ? 365 PHE   B CB  1 
ATOM   5743 C CG  . PHE   B 1 365 ? 3.711   -10.227 -57.631 1.00 48.17  ? 365 PHE   B CG  1 
ATOM   5744 C CD1 . PHE   B 1 365 ? 2.815   -10.363 -56.582 1.00 48.15  ? 365 PHE   B CD1 1 
ATOM   5745 C CD2 . PHE   B 1 365 ? 3.539   -9.177  -58.518 1.00 49.51  ? 365 PHE   B CD2 1 
ATOM   5746 C CE1 . PHE   B 1 365 ? 1.772   -9.470  -56.421 1.00 44.73  ? 365 PHE   B CE1 1 
ATOM   5747 C CE2 . PHE   B 1 365 ? 2.499   -8.284  -58.363 1.00 47.38  ? 365 PHE   B CE2 1 
ATOM   5748 C CZ  . PHE   B 1 365 ? 1.614   -8.431  -57.313 1.00 48.95  ? 365 PHE   B CZ  1 
ATOM   5749 N N   . CYS   B 1 366 ? 5.040   -14.603 -58.324 1.00 48.47  ? 366 CYS   B N   1 
ATOM   5750 C CA  . CYS   B 1 366 ? 5.834   -15.700 -58.861 1.00 50.70  ? 366 CYS   B CA  1 
ATOM   5751 C C   . CYS   B 1 366 ? 5.061   -16.321 -60.018 1.00 47.32  ? 366 CYS   B C   1 
ATOM   5752 O O   . CYS   B 1 366 ? 3.891   -15.982 -60.245 1.00 46.93  ? 366 CYS   B O   1 
ATOM   5753 C CB  . CYS   B 1 366 ? 6.151   -16.746 -57.775 1.00 50.31  ? 366 CYS   B CB  1 
ATOM   5754 S SG  . CYS   B 1 366 ? 4.733   -17.662 -57.129 1.00 51.13  ? 366 CYS   B SG  1 
ATOM   5755 N N   . PRO   B 1 367 ? 5.688   -17.216 -60.782 1.00 47.04  ? 367 PRO   B N   1 
ATOM   5756 C CA  . PRO   B 1 367 ? 4.950   -17.925 -61.833 1.00 47.82  ? 367 PRO   B CA  1 
ATOM   5757 C C   . PRO   B 1 367 ? 3.977   -18.943 -61.261 1.00 48.06  ? 367 PRO   B C   1 
ATOM   5758 O O   . PRO   B 1 367 ? 4.169   -19.482 -60.168 1.00 43.37  ? 367 PRO   B O   1 
ATOM   5759 C CB  . PRO   B 1 367 ? 6.058   -18.629 -62.628 1.00 48.14  ? 367 PRO   B CB  1 
ATOM   5760 C CG  . PRO   B 1 367 ? 7.291   -17.865 -62.321 1.00 50.78  ? 367 PRO   B CG  1 
ATOM   5761 C CD  . PRO   B 1 367 ? 7.135   -17.473 -60.888 1.00 52.45  ? 367 PRO   B CD  1 
ATOM   5762 N N   . VAL   B 1 368 ? 2.920   -19.213 -62.029 1.00 43.73  ? 368 VAL   B N   1 
ATOM   5763 C CA  . VAL   B 1 368 ? 2.094   -20.383 -61.753 1.00 41.46  ? 368 VAL   B CA  1 
ATOM   5764 C C   . VAL   B 1 368 ? 2.843   -21.650 -62.145 1.00 46.37  ? 368 VAL   B C   1 
ATOM   5765 O O   . VAL   B 1 368 ? 2.965   -22.595 -61.357 1.00 46.21  ? 368 VAL   B O   1 
ATOM   5766 C CB  . VAL   B 1 368 ? 0.744   -20.279 -62.487 1.00 43.83  ? 368 VAL   B CB  1 
ATOM   5767 C CG1 . VAL   B 1 368 ? -0.031  -21.591 -62.360 1.00 41.20  ? 368 VAL   B CG1 1 
ATOM   5768 C CG2 . VAL   B 1 368 ? -0.070  -19.108 -61.955 1.00 42.66  ? 368 VAL   B CG2 1 
ATOM   5769 N N   . LEU   B 1 369 ? 3.365   -21.680 -63.368 1.00 45.70  ? 369 LEU   B N   1 
ATOM   5770 C CA  . LEU   B 1 369 ? 4.171   -22.789 -63.850 1.00 48.85  ? 369 LEU   B CA  1 
ATOM   5771 C C   . LEU   B 1 369 ? 5.313   -22.228 -64.684 1.00 49.49  ? 369 LEU   B C   1 
ATOM   5772 O O   . LEU   B 1 369 ? 5.302   -21.061 -65.081 1.00 47.48  ? 369 LEU   B O   1 
ATOM   5773 C CB  . LEU   B 1 369 ? 3.330   -23.777 -64.669 1.00 49.77  ? 369 LEU   B CB  1 
ATOM   5774 C CG  . LEU   B 1 369 ? 2.911   -25.067 -63.961 1.00 50.00  ? 369 LEU   B CG  1 
ATOM   5775 C CD1 . LEU   B 1 369 ? 2.645   -26.177 -64.967 1.00 51.74  ? 369 LEU   B CD1 1 
ATOM   5776 C CD2 . LEU   B 1 369 ? 3.962   -25.501 -62.951 1.00 48.58  ? 369 LEU   B CD2 1 
ATOM   5777 N N   . GLY   B 1 370 ? 6.306   -23.078 -64.950 1.00 48.03  ? 370 GLY   B N   1 
ATOM   5778 C CA  . GLY   B 1 370 ? 7.460   -22.632 -65.711 1.00 54.46  ? 370 GLY   B CA  1 
ATOM   5779 C C   . GLY   B 1 370 ? 7.147   -22.281 -67.152 1.00 57.08  ? 370 GLY   B C   1 
ATOM   5780 O O   . GLY   B 1 370 ? 7.776   -21.386 -67.726 1.00 56.60  ? 370 GLY   B O   1 
ATOM   5781 N N   . THR   B 1 371 ? 6.179   -22.964 -67.756 1.00 53.76  ? 371 THR   B N   1 
ATOM   5782 C CA  . THR   B 1 371 ? 5.869   -22.781 -69.164 1.00 55.76  ? 371 THR   B CA  1 
ATOM   5783 C C   . THR   B 1 371 ? 4.364   -22.657 -69.352 1.00 53.36  ? 371 THR   B C   1 
ATOM   5784 O O   . THR   B 1 371 ? 3.572   -22.923 -68.444 1.00 52.61  ? 371 THR   B O   1 
ATOM   5785 C CB  . THR   B 1 371 ? 6.413   -23.942 -70.012 1.00 59.20  ? 371 THR   B CB  1 
ATOM   5786 O OG1 . THR   B 1 371 ? 6.217   -23.657 -71.403 1.00 61.80  ? 371 THR   B OG1 1 
ATOM   5787 C CG2 . THR   B 1 371 ? 5.706   -25.243 -69.655 1.00 54.91  ? 371 THR   B CG2 1 
ATOM   5788 N N   . THR   B 1 372 ? 3.982   -22.240 -70.555 1.00 52.78  ? 372 THR   B N   1 
ATOM   5789 C CA  . THR   B 1 372 ? 2.581   -22.178 -70.931 1.00 50.62  ? 372 THR   B CA  1 
ATOM   5790 C C   . THR   B 1 372 ? 2.050   -23.581 -71.219 1.00 46.89  ? 372 THR   B C   1 
ATOM   5791 O O   . THR   B 1 372 ? 2.748   -24.589 -71.064 1.00 44.30  ? 372 THR   B O   1 
ATOM   5792 C CB  . THR   B 1 372 ? 2.399   -21.279 -72.149 1.00 50.21  ? 372 THR   B CB  1 
ATOM   5793 O OG1 . THR   B 1 372 ? 3.374   -21.621 -73.142 1.00 48.36  ? 372 THR   B OG1 1 
ATOM   5794 C CG2 . THR   B 1 372 ? 2.560   -19.832 -71.762 1.00 51.02  ? 372 THR   B CG2 1 
ATOM   5795 N N   . ALA   B 1 373 ? 0.795   -23.633 -71.658 1.00 46.59  ? 373 ALA   B N   1 
ATOM   5796 C CA  . ALA   B 1 373 ? 0.124   -24.901 -71.916 1.00 45.17  ? 373 ALA   B CA  1 
ATOM   5797 C C   . ALA   B 1 373 ? 0.899   -25.723 -72.938 1.00 47.51  ? 373 ALA   B C   1 
ATOM   5798 O O   . ALA   B 1 373 ? 1.060   -25.308 -74.091 1.00 47.55  ? 373 ALA   B O   1 
ATOM   5799 C CB  . ALA   B 1 373 ? -1.302  -24.644 -72.404 1.00 41.96  ? 373 ALA   B CB  1 
ATOM   5800 N N   . PHE   B 1 374 ? 1.385   -26.884 -72.507 1.00 46.28  ? 374 PHE   B N   1 
ATOM   5801 C CA  . PHE   B 1 374 ? 2.138   -27.781 -73.369 1.00 47.25  ? 374 PHE   B CA  1 
ATOM   5802 C C   . PHE   B 1 374 ? 1.198   -28.591 -74.259 1.00 48.61  ? 374 PHE   B C   1 
ATOM   5803 O O   . PHE   B 1 374 ? -0.010  -28.678 -74.020 1.00 48.01  ? 374 PHE   B O   1 
ATOM   5804 C CB  . PHE   B 1 374 ? 3.001   -28.726 -72.534 1.00 47.17  ? 374 PHE   B CB  1 
ATOM   5805 C CG  . PHE   B 1 374 ? 2.254   -29.389 -71.410 1.00 51.01  ? 374 PHE   B CG  1 
ATOM   5806 C CD1 . PHE   B 1 374 ? 1.513   -30.541 -71.633 1.00 47.54  ? 374 PHE   B CD1 1 
ATOM   5807 C CD2 . PHE   B 1 374 ? 2.288   -28.858 -70.131 1.00 48.10  ? 374 PHE   B CD2 1 
ATOM   5808 C CE1 . PHE   B 1 374 ? 0.822   -31.149 -70.603 1.00 48.56  ? 374 PHE   B CE1 1 
ATOM   5809 C CE2 . PHE   B 1 374 ? 1.598   -29.464 -69.096 1.00 47.28  ? 374 PHE   B CE2 1 
ATOM   5810 C CZ  . PHE   B 1 374 ? 0.865   -30.611 -69.333 1.00 45.09  ? 374 PHE   B CZ  1 
ATOM   5811 N N   . ALA   B 1 375 ? 1.774   -29.196 -75.294 1.00 47.57  ? 375 ALA   B N   1 
ATOM   5812 C CA  . ALA   B 1 375 ? 0.989   -30.020 -76.200 1.00 47.33  ? 375 ALA   B CA  1 
ATOM   5813 C C   . ALA   B 1 375 ? 0.457   -31.248 -75.472 1.00 45.81  ? 375 ALA   B C   1 
ATOM   5814 O O   . ALA   B 1 375 ? 1.060   -31.737 -74.513 1.00 46.95  ? 375 ALA   B O   1 
ATOM   5815 C CB  . ALA   B 1 375 ? 1.828   -30.447 -77.404 1.00 47.20  ? 375 ALA   B CB  1 
ATOM   5816 N N   . HIS   B 1 376 ? -0.696  -31.735 -75.935 1.00 46.36  ? 376 HIS   B N   1 
ATOM   5817 C CA  . HIS   B 1 376 ? -1.320  -32.916 -75.349 1.00 45.17  ? 376 HIS   B CA  1 
ATOM   5818 C C   . HIS   B 1 376 ? -0.329  -34.064 -75.258 1.00 43.46  ? 376 HIS   B C   1 
ATOM   5819 O O   . HIS   B 1 376 ? 0.300   -34.439 -76.251 1.00 46.19  ? 376 HIS   B O   1 
ATOM   5820 C CB  . HIS   B 1 376 ? -2.527  -33.353 -76.183 1.00 40.53  ? 376 HIS   B CB  1 
ATOM   5821 C CG  . HIS   B 1 376 ? -3.570  -32.294 -76.353 1.00 39.81  ? 376 HIS   B CG  1 
ATOM   5822 N ND1 . HIS   B 1 376 ? -4.232  -31.722 -75.290 1.00 41.76  ? 376 HIS   B ND1 1 
ATOM   5823 C CD2 . HIS   B 1 376 ? -4.067  -31.706 -77.467 1.00 41.41  ? 376 HIS   B CD2 1 
ATOM   5824 C CE1 . HIS   B 1 376 ? -5.093  -30.826 -75.740 1.00 40.87  ? 376 HIS   B CE1 1 
ATOM   5825 N NE2 . HIS   B 1 376 ? -5.012  -30.797 -77.058 1.00 42.06  ? 376 HIS   B NE2 1 
ATOM   5826 N N   . SER   B 1 377 ? -0.184  -34.617 -74.061 1.00 44.79  ? 377 SER   B N   1 
ATOM   5827 C CA  . SER   B 1 377 ? 0.642   -35.794 -73.852 1.00 45.62  ? 377 SER   B CA  1 
ATOM   5828 C C   . SER   B 1 377 ? -0.252  -36.975 -73.507 1.00 49.57  ? 377 SER   B C   1 
ATOM   5829 O O   . SER   B 1 377 ? -1.210  -36.838 -72.741 1.00 47.90  ? 377 SER   B O   1 
ATOM   5830 C CB  . SER   B 1 377 ? 1.670   -35.572 -72.741 1.00 46.43  ? 377 SER   B CB  1 
ATOM   5831 O OG  . SER   B 1 377 ? 2.112   -36.809 -72.209 1.00 48.29  ? 377 SER   B OG  1 
ATOM   5832 N N   . ASP   B 1 378 ? 0.053   -38.125 -74.100 1.00 53.73  ? 378 ASP   B N   1 
ATOM   5833 C CA  . ASP   B 1 378 ? -0.639  -39.369 -73.803 1.00 56.35  ? 378 ASP   B CA  1 
ATOM   5834 C C   . ASP   B 1 378 ? 0.179   -40.276 -72.894 1.00 58.40  ? 378 ASP   B C   1 
ATOM   5835 O O   . ASP   B 1 378 ? -0.206  -41.429 -72.673 1.00 59.27  ? 378 ASP   B O   1 
ATOM   5836 C CB  . ASP   B 1 378 ? -0.995  -40.100 -75.101 1.00 58.49  ? 378 ASP   B CB  1 
ATOM   5837 C CG  . ASP   B 1 378 ? 0.210   -40.751 -75.756 1.00 61.89  ? 378 ASP   B CG  1 
ATOM   5838 O OD1 . ASP   B 1 378 ? 1.281   -40.111 -75.814 1.00 70.21  ? 378 ASP   B OD1 1 
ATOM   5839 O OD2 . ASP   B 1 378 ? 0.083   -41.905 -76.217 1.00 62.95  ? 378 ASP   B OD2 1 
ATOM   5840 N N   . GLU   B 1 379 ? 1.297   -39.777 -72.361 1.00 53.38  ? 379 GLU   B N   1 
ATOM   5841 C CA  . GLU   B 1 379 ? 2.149   -40.563 -71.481 1.00 55.06  ? 379 GLU   B CA  1 
ATOM   5842 C C   . GLU   B 1 379 ? 1.730   -40.311 -70.038 1.00 57.04  ? 379 GLU   B C   1 
ATOM   5843 O O   . GLU   B 1 379 ? 1.903   -39.187 -69.542 1.00 54.25  ? 379 GLU   B O   1 
ATOM   5844 C CB  . GLU   B 1 379 ? 3.612   -40.199 -71.686 1.00 55.11  ? 379 GLU   B CB  1 
ATOM   5845 C CG  . GLU   B 1 379 ? 4.544   -40.765 -70.633 1.00 59.81  ? 379 GLU   B CG  1 
ATOM   5846 C CD  . GLU   B 1 379 ? 4.565   -42.284 -70.640 1.00 61.13  ? 379 GLU   B CD  1 
ATOM   5847 O OE1 . GLU   B 1 379 ? 4.809   -42.879 -71.713 1.00 63.99  ? 379 GLU   B OE1 1 
ATOM   5848 O OE2 . GLU   B 1 379 ? 4.330   -42.884 -69.572 1.00 59.06  ? 379 GLU   B OE2 1 
ATOM   5849 N N   . PRO   B 1 380 ? 1.178   -41.302 -69.333 1.00 57.75  ? 380 PRO   B N   1 
ATOM   5850 C CA  . PRO   B 1 380 ? 0.694   -41.043 -67.968 1.00 56.90  ? 380 PRO   B CA  1 
ATOM   5851 C C   . PRO   B 1 380 ? 1.801   -40.847 -66.943 1.00 58.43  ? 380 PRO   B C   1 
ATOM   5852 O O   . PRO   B 1 380 ? 1.589   -40.123 -65.963 1.00 57.37  ? 380 PRO   B O   1 
ATOM   5853 C CB  . PRO   B 1 380 ? -0.144  -42.291 -67.656 1.00 57.48  ? 380 PRO   B CB  1 
ATOM   5854 C CG  . PRO   B 1 380 ? 0.419   -43.347 -68.555 1.00 58.70  ? 380 PRO   B CG  1 
ATOM   5855 C CD  . PRO   B 1 380 ? 0.779   -42.634 -69.817 1.00 55.79  ? 380 PRO   B CD  1 
ATOM   5856 N N   . ASP   B 1 381 ? 2.966   -41.466 -67.124 1.00 58.30  ? 381 ASP   B N   1 
ATOM   5857 C CA  . ASP   B 1 381 ? 4.034   -41.370 -66.133 1.00 59.52  ? 381 ASP   B CA  1 
ATOM   5858 C C   . ASP   B 1 381 ? 4.752   -40.032 -66.279 1.00 59.35  ? 381 ASP   B C   1 
ATOM   5859 O O   . ASP   B 1 381 ? 5.358   -39.755 -67.321 1.00 56.76  ? 381 ASP   B O   1 
ATOM   5860 C CB  . ASP   B 1 381 ? 5.010   -42.535 -66.283 1.00 60.82  ? 381 ASP   B CB  1 
ATOM   5861 C CG  . ASP   B 1 381 ? 6.033   -42.596 -65.154 1.00 65.62  ? 381 ASP   B CG  1 
ATOM   5862 O OD1 . ASP   B 1 381 ? 5.933   -41.790 -64.204 1.00 70.55  ? 381 ASP   B OD1 1 
ATOM   5863 O OD2 . ASP   B 1 381 ? 6.933   -43.463 -65.207 1.00 64.76  ? 381 ASP   B OD2 1 
ATOM   5864 N N   . TRP   B 1 382 ? 4.692   -39.210 -65.225 1.00 57.00  ? 382 TRP   B N   1 
ATOM   5865 C CA  . TRP   B 1 382 ? 5.318   -37.890 -65.264 1.00 56.77  ? 382 TRP   B CA  1 
ATOM   5866 C C   . TRP   B 1 382 ? 6.832   -37.980 -65.397 1.00 57.56  ? 382 TRP   B C   1 
ATOM   5867 O O   . TRP   B 1 382 ? 7.463   -37.055 -65.923 1.00 56.84  ? 382 TRP   B O   1 
ATOM   5868 C CB  . TRP   B 1 382 ? 4.956   -37.089 -64.012 1.00 58.18  ? 382 TRP   B CB  1 
ATOM   5869 C CG  . TRP   B 1 382 ? 3.634   -36.393 -64.080 1.00 52.62  ? 382 TRP   B CG  1 
ATOM   5870 C CD1 . TRP   B 1 382 ? 2.537   -36.780 -64.790 1.00 51.89  ? 382 TRP   B CD1 1 
ATOM   5871 C CD2 . TRP   B 1 382 ? 3.274   -35.176 -63.417 1.00 54.29  ? 382 TRP   B CD2 1 
ATOM   5872 N NE1 . TRP   B 1 382 ? 1.513   -35.883 -64.605 1.00 51.82  ? 382 TRP   B NE1 1 
ATOM   5873 C CE2 . TRP   B 1 382 ? 1.940   -34.888 -63.767 1.00 53.82  ? 382 TRP   B CE2 1 
ATOM   5874 C CE3 . TRP   B 1 382 ? 3.950   -34.305 -62.557 1.00 53.66  ? 382 TRP   B CE3 1 
ATOM   5875 C CZ2 . TRP   B 1 382 ? 1.268   -33.763 -63.289 1.00 53.94  ? 382 TRP   B CZ2 1 
ATOM   5876 C CZ3 . TRP   B 1 382 ? 3.282   -33.189 -62.082 1.00 53.73  ? 382 TRP   B CZ3 1 
ATOM   5877 C CH2 . TRP   B 1 382 ? 1.955   -32.927 -62.450 1.00 52.38  ? 382 TRP   B CH2 1 
ATOM   5878 N N   . ALA   B 1 383 ? 7.436   -39.070 -64.916 1.00 60.41  ? 383 ALA   B N   1 
ATOM   5879 C CA  . ALA   B 1 383 ? 8.879   -39.244 -65.051 1.00 62.73  ? 383 ALA   B CA  1 
ATOM   5880 C C   . ALA   B 1 383 ? 9.305   -39.466 -66.495 1.00 62.99  ? 383 ALA   B C   1 
ATOM   5881 O O   . ALA   B 1 383 ? 10.460  -39.185 -66.836 1.00 65.04  ? 383 ALA   B O   1 
ATOM   5882 C CB  . ALA   B 1 383 ? 9.351   -40.406 -64.176 1.00 60.44  ? 383 ALA   B CB  1 
ATOM   5883 N N   . LYS   B 1 384 ? 8.407   -39.960 -67.345 1.00 60.99  ? 384 LYS   B N   1 
ATOM   5884 C CA  . LYS   B 1 384 ? 8.672   -40.136 -68.767 1.00 60.36  ? 384 LYS   B CA  1 
ATOM   5885 C C   . LYS   B 1 384 ? 8.310   -38.905 -69.579 1.00 56.66  ? 384 LYS   B C   1 
ATOM   5886 O O   . LYS   B 1 384 ? 8.294   -38.974 -70.811 1.00 55.77  ? 384 LYS   B O   1 
ATOM   5887 C CB  . LYS   B 1 384 ? 7.910   -41.355 -69.301 1.00 58.49  ? 384 LYS   B CB  1 
ATOM   5888 C CG  . LYS   B 1 384 ? 8.560   -42.698 -68.991 1.00 58.37  ? 384 LYS   B CG  1 
ATOM   5889 C CD  . LYS   B 1 384 ? 7.534   -43.703 -68.495 1.00 63.73  ? 384 LYS   B CD  1 
ATOM   5890 C CE  . LYS   B 1 384 ? 8.193   -44.848 -67.746 1.00 64.36  ? 384 LYS   B CE  1 
ATOM   5891 N NZ  . LYS   B 1 384 ? 7.264   -45.436 -66.740 1.00 66.94  ? 384 LYS   B NZ  1 
ATOM   5892 N N   . ARG   B 1 385 ? 8.018   -37.792 -68.919 1.00 58.42  ? 385 ARG   B N   1 
ATOM   5893 C CA  . ARG   B 1 385 ? 7.669   -36.539 -69.570 1.00 60.00  ? 385 ARG   B CA  1 
ATOM   5894 C C   . ARG   B 1 385 ? 8.800   -35.528 -69.419 1.00 60.78  ? 385 ARG   B C   1 
ATOM   5895 O O   . ARG   B 1 385 ? 9.741   -35.716 -68.642 1.00 61.53  ? 385 ARG   B O   1 
ATOM   5896 C CB  . ARG   B 1 385 ? 6.372   -35.963 -68.987 1.00 55.22  ? 385 ARG   B CB  1 
ATOM   5897 C CG  . ARG   B 1 385 ? 5.097   -36.589 -69.508 1.00 56.57  ? 385 ARG   B CG  1 
ATOM   5898 C CD  . ARG   B 1 385 ? 3.896   -35.828 -68.981 1.00 52.85  ? 385 ARG   B CD  1 
ATOM   5899 N NE  . ARG   B 1 385 ? 2.759   -36.689 -68.684 1.00 51.43  ? 385 ARG   B NE  1 
ATOM   5900 C CZ  . ARG   B 1 385 ? 1.528   -36.240 -68.478 1.00 50.79  ? 385 ARG   B CZ  1 
ATOM   5901 N NH1 . ARG   B 1 385 ? 1.247   -34.949 -68.532 1.00 47.15  ? 385 ARG   B NH1 1 
ATOM   5902 N NH2 . ARG   B 1 385 ? 0.556   -37.108 -68.209 1.00 45.73  ? 385 ARG   B NH2 1 
ATOM   5903 N N   . SER   B 1 386 ? 8.683   -34.435 -70.169 1.00 60.71  ? 386 SER   B N   1 
ATOM   5904 C CA  . SER   B 1 386 ? 9.638   -33.338 -70.114 1.00 58.74  ? 386 SER   B CA  1 
ATOM   5905 C C   . SER   B 1 386 ? 9.043   -32.144 -70.841 1.00 56.43  ? 386 SER   B C   1 
ATOM   5906 O O   . SER   B 1 386 ? 8.198   -32.301 -71.726 1.00 54.96  ? 386 SER   B O   1 
ATOM   5907 C CB  . SER   B 1 386 ? 10.986  -33.727 -70.735 1.00 58.07  ? 386 SER   B CB  1 
ATOM   5908 O OG  . SER   B 1 386 ? 10.865  -33.935 -72.130 1.00 56.87  ? 386 SER   B OG  1 
ATOM   5909 N N   . LEU   B 1 387 ? 9.492   -30.954 -70.454 1.00 59.73  ? 387 LEU   B N   1 
ATOM   5910 C CA  . LEU   B 1 387 ? 9.010   -29.695 -71.004 1.00 61.32  ? 387 LEU   B CA  1 
ATOM   5911 C C   . LEU   B 1 387 ? 10.100  -29.011 -71.812 1.00 62.48  ? 387 LEU   B C   1 
ATOM   5912 O O   . LEU   B 1 387 ? 11.293  -29.246 -71.609 1.00 62.43  ? 387 LEU   B O   1 
ATOM   5913 C CB  . LEU   B 1 387 ? 8.538   -28.754 -69.893 1.00 60.93  ? 387 LEU   B CB  1 
ATOM   5914 C CG  . LEU   B 1 387 ? 7.424   -29.321 -69.028 1.00 58.21  ? 387 LEU   B CG  1 
ATOM   5915 C CD1 . LEU   B 1 387 ? 7.037   -28.337 -67.952 1.00 54.89  ? 387 LEU   B CD1 1 
ATOM   5916 C CD2 . LEU   B 1 387 ? 6.242   -29.614 -69.928 1.00 55.16  ? 387 LEU   B CD2 1 
ATOM   5917 N N   . SER   B 1 388 ? 9.672   -28.141 -72.722 1.00 63.32  ? 388 SER   B N   1 
ATOM   5918 C CA  . SER   B 1 388 ? 10.579  -27.313 -73.505 1.00 66.03  ? 388 SER   B CA  1 
ATOM   5919 C C   . SER   B 1 388 ? 10.600  -25.915 -72.900 1.00 65.94  ? 388 SER   B C   1 
ATOM   5920 O O   . SER   B 1 388 ? 9.556   -25.260 -72.804 1.00 63.31  ? 388 SER   B O   1 
ATOM   5921 C CB  . SER   B 1 388 ? 10.154  -27.267 -74.973 1.00 68.93  ? 388 SER   B CB  1 
ATOM   5922 O OG  . SER   B 1 388 ? 9.262   -26.194 -75.216 1.00 71.79  ? 388 SER   B OG  1 
ATOM   5923 N N   . ILE   B 1 389 ? 11.782  -25.468 -72.489 1.00 70.23  ? 389 ILE   B N   1 
ATOM   5924 C CA  . ILE   B 1 389 ? 11.955  -24.200 -71.788 1.00 69.90  ? 389 ILE   B CA  1 
ATOM   5925 C C   . ILE   B 1 389 ? 12.961  -23.381 -72.586 1.00 69.41  ? 389 ILE   B C   1 
ATOM   5926 O O   . ILE   B 1 389 ? 14.177  -23.557 -72.438 1.00 71.64  ? 389 ILE   B O   1 
ATOM   5927 C CB  . ILE   B 1 389 ? 12.410  -24.401 -70.338 1.00 67.37  ? 389 ILE   B CB  1 
ATOM   5928 C CG1 . ILE   B 1 389 ? 11.359  -25.209 -69.565 1.00 63.89  ? 389 ILE   B CG1 1 
ATOM   5929 C CG2 . ILE   B 1 389 ? 12.699  -23.066 -69.659 1.00 67.10  ? 389 ILE   B CG2 1 
ATOM   5930 C CD1 . ILE   B 1 389 ? 10.249  -24.370 -68.949 1.00 62.25  ? 389 ILE   B CD1 1 
ATOM   5931 N N   . ASP   B 1 390 ? 12.454  -22.483 -73.436 1.00 73.69  ? 390 ASP   B N   1 
ATOM   5932 C CA  . ASP   B 1 390 ? 13.281  -21.627 -74.290 1.00 72.04  ? 390 ASP   B CA  1 
ATOM   5933 C C   . ASP   B 1 390 ? 14.235  -22.459 -75.151 1.00 77.42  ? 390 ASP   B C   1 
ATOM   5934 O O   . ASP   B 1 390 ? 15.434  -22.186 -75.242 1.00 80.50  ? 390 ASP   B O   1 
ATOM   5935 C CB  . ASP   B 1 390 ? 14.042  -20.588 -73.458 1.00 69.77  ? 390 ASP   B CB  1 
ATOM   5936 C CG  . ASP   B 1 390 ? 13.121  -19.565 -72.804 1.00 71.49  ? 390 ASP   B CG  1 
ATOM   5937 O OD1 . ASP   B 1 390 ? 12.047  -19.270 -73.371 1.00 67.95  ? 390 ASP   B OD1 1 
ATOM   5938 O OD2 . ASP   B 1 390 ? 13.474  -19.052 -71.719 1.00 72.20  ? 390 ASP   B OD2 1 
ATOM   5939 N N   . GLY   B 1 391 ? 13.683  -23.492 -75.791 1.00 80.09  ? 391 GLY   B N   1 
ATOM   5940 C CA  . GLY   B 1 391 ? 14.447  -24.370 -76.650 1.00 76.60  ? 391 GLY   B CA  1 
ATOM   5941 C C   . GLY   B 1 391 ? 15.143  -25.515 -75.949 1.00 77.80  ? 391 GLY   B C   1 
ATOM   5942 O O   . GLY   B 1 391 ? 15.642  -26.424 -76.627 1.00 77.29  ? 391 GLY   B O   1 
ATOM   5943 N N   . GLY   B 1 392 ? 15.194  -25.508 -74.620 1.00 76.60  ? 392 GLY   B N   1 
ATOM   5944 C CA  . GLY   B 1 392 ? 15.861  -26.547 -73.858 1.00 71.84  ? 392 GLY   B CA  1 
ATOM   5945 C C   . GLY   B 1 392 ? 14.860  -27.438 -73.148 1.00 69.48  ? 392 GLY   B C   1 
ATOM   5946 O O   . GLY   B 1 392 ? 13.801  -26.979 -72.709 1.00 70.19  ? 392 GLY   B O   1 
ATOM   5947 N N   . ILE   B 1 393 ? 15.204  -28.715 -73.029 1.00 64.42  ? 393 ILE   B N   1 
ATOM   5948 C CA  . ILE   B 1 393 ? 14.325  -29.678 -72.379 1.00 66.40  ? 393 ILE   B CA  1 
ATOM   5949 C C   . ILE   B 1 393 ? 14.539  -29.623 -70.871 1.00 67.51  ? 393 ILE   B C   1 
ATOM   5950 O O   . ILE   B 1 393 ? 15.655  -29.394 -70.385 1.00 66.74  ? 393 ILE   B O   1 
ATOM   5951 C CB  . ILE   B 1 393 ? 14.555  -31.092 -72.948 1.00 67.70  ? 393 ILE   B CB  1 
ATOM   5952 C CG1 . ILE   B 1 393 ? 13.219  -31.819 -73.118 1.00 62.95  ? 393 ILE   B CG1 1 
ATOM   5953 C CG2 . ILE   B 1 393 ? 15.504  -31.906 -72.071 1.00 70.25  ? 393 ILE   B CG2 1 
ATOM   5954 C CD1 . ILE   B 1 393 ? 12.394  -31.314 -74.283 1.00 61.27  ? 393 ILE   B CD1 1 
ATOM   5955 N N   . ALA   B 1 394 ? 13.455  -29.804 -70.125 1.00 66.08  ? 394 ALA   B N   1 
ATOM   5956 C CA  . ALA   B 1 394 ? 13.455  -29.744 -68.674 1.00 62.29  ? 394 ALA   B CA  1 
ATOM   5957 C C   . ALA   B 1 394 ? 12.496  -30.798 -68.146 1.00 61.73  ? 394 ALA   B C   1 
ATOM   5958 O O   . ALA   B 1 394 ? 11.475  -31.082 -68.783 1.00 59.32  ? 394 ALA   B O   1 
ATOM   5959 C CB  . ALA   B 1 394 ? 13.037  -28.356 -68.162 1.00 60.52  ? 394 ALA   B CB  1 
ATOM   5960 N N   . PRO   B 1 395 ? 12.796  -31.396 -66.994 1.00 62.32  ? 395 PRO   B N   1 
ATOM   5961 C CA  . PRO   B 1 395 ? 11.904  -32.427 -66.450 1.00 58.84  ? 395 PRO   B CA  1 
ATOM   5962 C C   . PRO   B 1 395 ? 10.520  -31.868 -66.140 1.00 57.06  ? 395 PRO   B C   1 
ATOM   5963 O O   . PRO   B 1 395 ? 10.368  -30.714 -65.734 1.00 51.72  ? 395 PRO   B O   1 
ATOM   5964 C CB  . PRO   B 1 395 ? 12.631  -32.894 -65.183 1.00 53.08  ? 395 PRO   B CB  1 
ATOM   5965 C CG  . PRO   B 1 395 ? 13.550  -31.768 -64.829 1.00 56.35  ? 395 PRO   B CG  1 
ATOM   5966 C CD  . PRO   B 1 395 ? 13.976  -31.179 -66.139 1.00 57.25  ? 395 PRO   B CD  1 
ATOM   5967 N N   . PHE   B 1 396 ? 9.504   -32.710 -66.346 1.00 56.13  ? 396 PHE   B N   1 
ATOM   5968 C CA  . PHE   B 1 396 ? 8.118   -32.283 -66.175 1.00 53.27  ? 396 PHE   B CA  1 
ATOM   5969 C C   . PHE   B 1 396 ? 7.767   -32.116 -64.702 1.00 50.07  ? 396 PHE   B C   1 
ATOM   5970 O O   . PHE   B 1 396 ? 7.206   -31.090 -64.299 1.00 49.42  ? 396 PHE   B O   1 
ATOM   5971 C CB  . PHE   B 1 396 ? 7.183   -33.299 -66.832 1.00 57.02  ? 396 PHE   B CB  1 
ATOM   5972 C CG  . PHE   B 1 396 ? 5.746   -32.852 -66.922 1.00 53.96  ? 396 PHE   B CG  1 
ATOM   5973 C CD1 . PHE   B 1 396 ? 4.891   -32.983 -65.836 1.00 50.94  ? 396 PHE   B CD1 1 
ATOM   5974 C CD2 . PHE   B 1 396 ? 5.245   -32.334 -68.102 1.00 53.59  ? 396 PHE   B CD2 1 
ATOM   5975 C CE1 . PHE   B 1 396 ? 3.573   -32.584 -65.918 1.00 50.92  ? 396 PHE   B CE1 1 
ATOM   5976 C CE2 . PHE   B 1 396 ? 3.925   -31.929 -68.194 1.00 50.81  ? 396 PHE   B CE2 1 
ATOM   5977 C CZ  . PHE   B 1 396 ? 3.085   -32.057 -67.097 1.00 51.82  ? 396 PHE   B CZ  1 
ATOM   5978 N N   . ALA   B 1 397 ? 8.072   -33.128 -63.886 1.00 48.50  ? 397 ALA   B N   1 
ATOM   5979 C CA  . ALA   B 1 397 ? 7.596   -33.160 -62.507 1.00 51.71  ? 397 ALA   B CA  1 
ATOM   5980 C C   . ALA   B 1 397 ? 8.234   -32.090 -61.633 1.00 53.80  ? 397 ALA   B C   1 
ATOM   5981 O O   . ALA   B 1 397 ? 7.628   -31.685 -60.635 1.00 53.25  ? 397 ALA   B O   1 
ATOM   5982 C CB  . ALA   B 1 397 ? 7.841   -34.541 -61.901 1.00 47.73  ? 397 ALA   B CB  1 
ATOM   5983 N N   . ALA   B 1 398 ? 9.434   -31.619 -61.983 1.00 54.07  ? 398 ALA   B N   1 
ATOM   5984 C CA  . ALA   B 1 398 ? 10.083  -30.574 -61.199 1.00 49.62  ? 398 ALA   B CA  1 
ATOM   5985 C C   . ALA   B 1 398 ? 9.244   -29.309 -61.122 1.00 53.05  ? 398 ALA   B C   1 
ATOM   5986 O O   . ALA   B 1 398 ? 9.418   -28.522 -60.186 1.00 54.69  ? 398 ALA   B O   1 
ATOM   5987 C CB  . ALA   B 1 398 ? 11.457  -30.255 -61.788 1.00 50.21  ? 398 ALA   B CB  1 
ATOM   5988 N N   . GLN   B 1 399 ? 8.327   -29.106 -62.070 1.00 51.81  ? 399 GLN   B N   1 
ATOM   5989 C CA  . GLN   B 1 399 ? 7.490   -27.913 -62.097 1.00 51.99  ? 399 GLN   B CA  1 
ATOM   5990 C C   . GLN   B 1 399 ? 6.514   -27.839 -60.930 1.00 51.24  ? 399 GLN   B C   1 
ATOM   5991 O O   . GLN   B 1 399 ? 5.889   -26.791 -60.737 1.00 49.14  ? 399 GLN   B O   1 
ATOM   5992 C CB  . GLN   B 1 399 ? 6.729   -27.854 -63.419 1.00 52.92  ? 399 GLN   B CB  1 
ATOM   5993 C CG  . GLN   B 1 399 ? 7.623   -27.588 -64.607 1.00 51.36  ? 399 GLN   B CG  1 
ATOM   5994 C CD  . GLN   B 1 399 ? 8.263   -26.218 -64.554 1.00 54.59  ? 399 GLN   B CD  1 
ATOM   5995 O OE1 . GLN   B 1 399 ? 7.675   -25.265 -64.044 1.00 54.32  ? 399 GLN   B OE1 1 
ATOM   5996 N NE2 . GLN   B 1 399 ? 9.483   -26.116 -65.066 1.00 55.28  ? 399 GLN   B NE2 1 
ATOM   5997 N N   . LEU   B 1 400 ? 6.369   -28.916 -60.154 1.00 50.88  ? 400 LEU   B N   1 
ATOM   5998 C CA  . LEU   B 1 400 ? 5.584   -28.866 -58.927 1.00 51.39  ? 400 LEU   B CA  1 
ATOM   5999 C C   . LEU   B 1 400 ? 6.165   -27.898 -57.904 1.00 46.88  ? 400 LEU   B C   1 
ATOM   6000 O O   . LEU   B 1 400 ? 5.512   -27.627 -56.890 1.00 47.98  ? 400 LEU   B O   1 
ATOM   6001 C CB  . LEU   B 1 400 ? 5.492   -30.265 -58.313 1.00 49.88  ? 400 LEU   B CB  1 
ATOM   6002 C CG  . LEU   B 1 400 ? 4.254   -31.116 -58.592 1.00 52.47  ? 400 LEU   B CG  1 
ATOM   6003 C CD1 . LEU   B 1 400 ? 4.568   -32.586 -58.350 1.00 51.71  ? 400 LEU   B CD1 1 
ATOM   6004 C CD2 . LEU   B 1 400 ? 3.073   -30.675 -57.741 1.00 53.25  ? 400 LEU   B CD2 1 
ATOM   6005 N N   . GLY   B 1 401 ? 7.371   -27.377 -58.141 1.00 49.19  ? 401 GLY   B N   1 
ATOM   6006 C CA  . GLY   B 1 401 ? 7.972   -26.460 -57.189 1.00 48.36  ? 401 GLY   B CA  1 
ATOM   6007 C C   . GLY   B 1 401 ? 7.243   -25.132 -57.103 1.00 49.27  ? 401 GLY   B C   1 
ATOM   6008 O O   . GLY   B 1 401 ? 7.047   -24.595 -56.010 1.00 51.02  ? 401 GLY   B O   1 
ATOM   6009 N N   . TRP   B 1 402 ? 6.838   -24.580 -58.253 1.00 46.89  ? 402 TRP   B N   1 
ATOM   6010 C CA  . TRP   B 1 402 ? 6.139   -23.296 -58.254 1.00 49.21  ? 402 TRP   B CA  1 
ATOM   6011 C C   . TRP   B 1 402 ? 4.811   -23.377 -57.516 1.00 50.32  ? 402 TRP   B C   1 
ATOM   6012 O O   . TRP   B 1 402 ? 4.360   -22.382 -56.936 1.00 49.83  ? 402 TRP   B O   1 
ATOM   6013 C CB  . TRP   B 1 402 ? 5.896   -22.818 -59.685 1.00 49.10  ? 402 TRP   B CB  1 
ATOM   6014 C CG  . TRP   B 1 402 ? 7.117   -22.766 -60.535 1.00 53.10  ? 402 TRP   B CG  1 
ATOM   6015 C CD1 . TRP   B 1 402 ? 7.470   -23.649 -61.508 1.00 53.55  ? 402 TRP   B CD1 1 
ATOM   6016 C CD2 . TRP   B 1 402 ? 8.147   -21.771 -60.500 1.00 54.94  ? 402 TRP   B CD2 1 
ATOM   6017 N NE1 . TRP   B 1 402 ? 8.659   -23.271 -62.082 1.00 52.89  ? 402 TRP   B NE1 1 
ATOM   6018 C CE2 . TRP   B 1 402 ? 9.096   -22.120 -61.481 1.00 54.68  ? 402 TRP   B CE2 1 
ATOM   6019 C CE3 . TRP   B 1 402 ? 8.360   -20.620 -59.734 1.00 51.49  ? 402 TRP   B CE3 1 
ATOM   6020 C CZ2 . TRP   B 1 402 ? 10.240  -21.363 -61.716 1.00 53.15  ? 402 TRP   B CZ2 1 
ATOM   6021 C CZ3 . TRP   B 1 402 ? 9.497   -19.870 -59.969 1.00 54.31  ? 402 TRP   B CZ3 1 
ATOM   6022 C CH2 . TRP   B 1 402 ? 10.422  -20.243 -60.952 1.00 55.45  ? 402 TRP   B CH2 1 
ATOM   6023 N N   . ILE   B 1 403 ? 4.174   -24.547 -57.536 1.00 50.45  ? 403 ILE   B N   1 
ATOM   6024 C CA  . ILE   B 1 403 ? 2.875   -24.743 -56.902 1.00 45.55  ? 403 ILE   B CA  1 
ATOM   6025 C C   . ILE   B 1 403 ? 2.997   -25.047 -55.410 1.00 46.72  ? 403 ILE   B C   1 
ATOM   6026 O O   . ILE   B 1 403 ? 2.057   -24.775 -54.647 1.00 43.21  ? 403 ILE   B O   1 
ATOM   6027 C CB  . ILE   B 1 403 ? 2.131   -25.870 -57.655 1.00 49.59  ? 403 ILE   B CB  1 
ATOM   6028 C CG1 . ILE   B 1 403 ? 1.291   -25.309 -58.810 1.00 46.02  ? 403 ILE   B CG1 1 
ATOM   6029 C CG2 . ILE   B 1 403 ? 1.296   -26.751 -56.722 1.00 45.72  ? 403 ILE   B CG2 1 
ATOM   6030 C CD1 . ILE   B 1 403 ? 1.011   -23.825 -58.723 1.00 48.21  ? 403 ILE   B CD1 1 
ATOM   6031 N N   . SER   B 1 404 ? 4.157   -25.532 -54.964 1.00 46.28  ? 404 SER   B N   1 
ATOM   6032 C CA  . SER   B 1 404 ? 4.279   -26.172 -53.658 1.00 44.88  ? 404 SER   B CA  1 
ATOM   6033 C C   . SER   B 1 404 ? 4.119   -25.201 -52.491 1.00 42.93  ? 404 SER   B C   1 
ATOM   6034 O O   . SER   B 1 404 ? 3.664   -25.609 -51.417 1.00 42.92  ? 404 SER   B O   1 
ATOM   6035 C CB  . SER   B 1 404 ? 5.626   -26.885 -53.572 1.00 44.52  ? 404 SER   B CB  1 
ATOM   6036 O OG  . SER   B 1 404 ? 6.696   -25.958 -53.628 1.00 46.57  ? 404 SER   B OG  1 
ATOM   6037 N N   . MET   B 1 405 ? 4.492   -23.932 -52.663 1.00 43.86  ? 405 MET   B N   1 
ATOM   6038 C CA  . MET   B 1 405 ? 4.524   -23.016 -51.524 1.00 43.94  ? 405 MET   B CA  1 
ATOM   6039 C C   . MET   B 1 405 ? 3.136   -22.813 -50.927 1.00 44.51  ? 405 MET   B C   1 
ATOM   6040 O O   . MET   B 1 405 ? 2.933   -22.996 -49.721 1.00 43.53  ? 405 MET   B O   1 
ATOM   6041 C CB  . MET   B 1 405 ? 5.128   -21.676 -51.941 1.00 41.89  ? 405 MET   B CB  1 
ATOM   6042 C CG  . MET   B 1 405 ? 6.594   -21.765 -52.296 1.00 47.18  ? 405 MET   B CG  1 
ATOM   6043 S SD  . MET   B 1 405 ? 6.835   -22.013 -54.060 1.00 54.15  ? 405 MET   B SD  1 
ATOM   6044 C CE  . MET   B 1 405 ? 6.753   -20.322 -54.643 1.00 50.04  ? 405 MET   B CE  1 
ATOM   6045 N N   . ALA   B 1 406 ? 2.165   -22.433 -51.757 1.00 42.13  ? 406 ALA   B N   1 
ATOM   6046 C CA  . ALA   B 1 406 ? 0.830   -22.155 -51.241 1.00 42.11  ? 406 ALA   B CA  1 
ATOM   6047 C C   . ALA   B 1 406 ? 0.112   -23.425 -50.797 1.00 43.49  ? 406 ALA   B C   1 
ATOM   6048 O O   . ALA   B 1 406 ? -0.712  -23.377 -49.878 1.00 41.67  ? 406 ALA   B O   1 
ATOM   6049 C CB  . ALA   B 1 406 ? 0.005   -21.418 -52.291 1.00 39.05  ? 406 ALA   B CB  1 
ATOM   6050 N N   . THR   B 1 407 ? 0.409   -24.565 -51.424 1.00 41.07  ? 407 THR   B N   1 
ATOM   6051 C CA  . THR   B 1 407 ? -0.262  -25.805 -51.047 1.00 42.23  ? 407 THR   B CA  1 
ATOM   6052 C C   . THR   B 1 407 ? 0.312   -26.384 -49.758 1.00 42.16  ? 407 THR   B C   1 
ATOM   6053 O O   . THR   B 1 407 ? -0.441  -26.812 -48.876 1.00 44.33  ? 407 THR   B O   1 
ATOM   6054 C CB  . THR   B 1 407 ? -0.170  -26.828 -52.179 1.00 44.47  ? 407 THR   B CB  1 
ATOM   6055 O OG1 . THR   B 1 407 ? -0.520  -26.203 -53.421 1.00 46.46  ? 407 THR   B OG1 1 
ATOM   6056 C CG2 . THR   B 1 407 ? -1.105  -27.995 -51.918 1.00 42.26  ? 407 THR   B CG2 1 
ATOM   6057 N N   . TYR   B 1 408 ? 1.640   -26.422 -49.637 1.00 39.74  ? 408 TYR   B N   1 
ATOM   6058 C CA  . TYR   B 1 408 ? 2.257   -26.915 -48.408 1.00 42.08  ? 408 TYR   B CA  1 
ATOM   6059 C C   . TYR   B 1 408 ? 2.029   -25.947 -47.254 1.00 43.06  ? 408 TYR   B C   1 
ATOM   6060 O O   . TYR   B 1 408 ? 1.587   -26.348 -46.171 1.00 42.32  ? 408 TYR   B O   1 
ATOM   6061 C CB  . TYR   B 1 408 ? 3.752   -27.152 -48.626 1.00 44.26  ? 408 TYR   B CB  1 
ATOM   6062 C CG  . TYR   B 1 408 ? 4.400   -28.017 -47.569 1.00 45.35  ? 408 TYR   B CG  1 
ATOM   6063 C CD1 . TYR   B 1 408 ? 3.917   -29.286 -47.288 1.00 46.60  ? 408 TYR   B CD1 1 
ATOM   6064 C CD2 . TYR   B 1 408 ? 5.491   -27.555 -46.842 1.00 48.32  ? 408 TYR   B CD2 1 
ATOM   6065 C CE1 . TYR   B 1 408 ? 4.506   -30.077 -46.319 1.00 45.29  ? 408 TYR   B CE1 1 
ATOM   6066 C CE2 . TYR   B 1 408 ? 6.086   -28.337 -45.872 1.00 47.96  ? 408 TYR   B CE2 1 
ATOM   6067 C CZ  . TYR   B 1 408 ? 5.588   -29.597 -45.614 1.00 47.20  ? 408 TYR   B CZ  1 
ATOM   6068 O OH  . TYR   B 1 408 ? 6.172   -30.381 -44.646 1.00 47.94  ? 408 TYR   B OH  1 
ATOM   6069 N N   . GLY   B 1 409 ? 2.323   -24.666 -47.468 1.00 41.22  ? 409 GLY   B N   1 
ATOM   6070 C CA  . GLY   B 1 409 ? 2.092   -23.654 -46.453 1.00 39.50  ? 409 GLY   B CA  1 
ATOM   6071 C C   . GLY   B 1 409 ? 0.632   -23.349 -46.176 1.00 43.11  ? 409 GLY   B C   1 
ATOM   6072 O O   . GLY   B 1 409 ? 0.339   -22.714 -45.157 1.00 41.83  ? 409 GLY   B O   1 
ATOM   6073 N N   . GLY   B 1 410 ? -0.284  -23.783 -47.045 1.00 40.00  ? 410 GLY   B N   1 
ATOM   6074 C CA  . GLY   B 1 410 ? -1.698  -23.533 -46.862 1.00 36.32  ? 410 GLY   B CA  1 
ATOM   6075 C C   . GLY   B 1 410 ? -2.183  -22.171 -47.310 1.00 39.98  ? 410 GLY   B C   1 
ATOM   6076 O O   . GLY   B 1 410 ? -3.399  -21.933 -47.297 1.00 38.89  ? 410 GLY   B O   1 
ATOM   6077 N N   . MET   B 1 411 ? -1.284  -21.281 -47.726 1.00 36.22  ? 411 MET   B N   1 
ATOM   6078 C CA  . MET   B 1 411 ? -1.654  -19.911 -48.049 1.00 38.31  ? 411 MET   B CA  1 
ATOM   6079 C C   . MET   B 1 411 ? -2.626  -19.866 -49.228 1.00 39.31  ? 411 MET   B C   1 
ATOM   6080 O O   . MET   B 1 411 ? -2.634  -20.764 -50.076 1.00 38.33  ? 411 MET   B O   1 
ATOM   6081 C CB  . MET   B 1 411 ? -0.410  -19.092 -48.394 1.00 38.86  ? 411 MET   B CB  1 
ATOM   6082 C CG  . MET   B 1 411 ? 0.566   -18.860 -47.251 1.00 37.45  ? 411 MET   B CG  1 
ATOM   6083 S SD  . MET   B 1 411 ? 1.773   -20.193 -47.114 1.00 39.36  ? 411 MET   B SD  1 
ATOM   6084 C CE  . MET   B 1 411 ? 2.848   -19.790 -48.489 1.00 41.46  ? 411 MET   B CE  1 
ATOM   6085 N N   . PRO   B 1 412 ? -3.451  -18.822 -49.313 1.00 38.28  ? 412 PRO   B N   1 
ATOM   6086 C CA  . PRO   B 1 412 ? -4.211  -18.593 -50.543 1.00 35.94  ? 412 PRO   B CA  1 
ATOM   6087 C C   . PRO   B 1 412 ? -3.281  -18.136 -51.653 1.00 40.86  ? 412 PRO   B C   1 
ATOM   6088 O O   . PRO   B 1 412 ? -2.306  -17.419 -51.416 1.00 37.50  ? 412 PRO   B O   1 
ATOM   6089 C CB  . PRO   B 1 412 ? -5.199  -17.489 -50.154 1.00 36.81  ? 412 PRO   B CB  1 
ATOM   6090 C CG  . PRO   B 1 412 ? -4.506  -16.751 -49.064 1.00 38.86  ? 412 PRO   B CG  1 
ATOM   6091 C CD  . PRO   B 1 412 ? -3.719  -17.786 -48.301 1.00 40.50  ? 412 PRO   B CD  1 
ATOM   6092 N N   . ALA   B 1 413 ? -3.582  -18.568 -52.872 1.00 37.90  ? 413 ALA   B N   1 
ATOM   6093 C CA  . ALA   B 1 413 ? -2.821  -18.153 -54.040 1.00 37.64  ? 413 ALA   B CA  1 
ATOM   6094 C C   . ALA   B 1 413 ? -3.784  -17.942 -55.191 1.00 39.92  ? 413 ALA   B C   1 
ATOM   6095 O O   . ALA   B 1 413 ? -4.589  -18.826 -55.499 1.00 45.47  ? 413 ALA   B O   1 
ATOM   6096 C CB  . ALA   B 1 413 ? -1.760  -19.190 -54.424 1.00 38.44  ? 413 ALA   B CB  1 
ATOM   6097 N N   . LEU   B 1 414 ? -3.710  -16.776 -55.813 1.00 41.22  ? 414 LEU   B N   1 
ATOM   6098 C CA  . LEU   B 1 414 ? -4.548  -16.464 -56.956 1.00 41.68  ? 414 LEU   B CA  1 
ATOM   6099 C C   . LEU   B 1 414 ? -3.752  -16.670 -58.235 1.00 41.87  ? 414 LEU   B C   1 
ATOM   6100 O O   . LEU   B 1 414 ? -2.542  -16.439 -58.276 1.00 44.66  ? 414 LEU   B O   1 
ATOM   6101 C CB  . LEU   B 1 414 ? -5.065  -15.029 -56.884 1.00 40.51  ? 414 LEU   B CB  1 
ATOM   6102 C CG  . LEU   B 1 414 ? -5.681  -14.456 -58.160 1.00 43.88  ? 414 LEU   B CG  1 
ATOM   6103 C CD1 . LEU   B 1 414 ? -7.139  -14.868 -58.275 1.00 44.02  ? 414 LEU   B CD1 1 
ATOM   6104 C CD2 . LEU   B 1 414 ? -5.531  -12.941 -58.201 1.00 44.21  ? 414 LEU   B CD2 1 
ATOM   6105 N N   . SER   B 1 415 ? -4.437  -17.139 -59.273 1.00 43.52  ? 415 SER   B N   1 
ATOM   6106 C CA  . SER   B 1 415 ? -3.873  -17.241 -60.613 1.00 41.22  ? 415 SER   B CA  1 
ATOM   6107 C C   . SER   B 1 415 ? -4.695  -16.334 -61.521 1.00 44.18  ? 415 SER   B C   1 
ATOM   6108 O O   . SER   B 1 415 ? -5.877  -16.599 -61.763 1.00 42.54  ? 415 SER   B O   1 
ATOM   6109 C CB  . SER   B 1 415 ? -3.879  -18.688 -61.103 1.00 39.08  ? 415 SER   B CB  1 
ATOM   6110 O OG  . SER   B 1 415 ? -3.759  -18.747 -62.511 1.00 42.28  ? 415 SER   B OG  1 
ATOM   6111 N N   . MET   B 1 416 ? -4.076  -15.260 -62.006 1.00 45.24  ? 416 MET   B N   1 
ATOM   6112 C CA  . MET   B 1 416 ? -4.774  -14.243 -62.775 1.00 45.27  ? 416 MET   B CA  1 
ATOM   6113 C C   . MET   B 1 416 ? -4.067  -13.986 -64.097 1.00 45.28  ? 416 MET   B C   1 
ATOM   6114 O O   . MET   B 1 416 ? -2.836  -14.045 -64.176 1.00 45.68  ? 416 MET   B O   1 
ATOM   6115 C CB  . MET   B 1 416 ? -4.881  -12.932 -61.984 1.00 42.02  ? 416 MET   B CB  1 
ATOM   6116 C CG  . MET   B 1 416 ? -3.553  -12.414 -61.469 1.00 45.37  ? 416 MET   B CG  1 
ATOM   6117 S SD  . MET   B 1 416 ? -3.483  -10.616 -61.462 1.00 56.42  ? 416 MET   B SD  1 
ATOM   6118 C CE  . MET   B 1 416 ? -4.009  -10.237 -63.128 1.00 44.96  ? 416 MET   B CE  1 
ATOM   6119 N N   . PRO   B 1 417 ? -4.828  -13.685 -65.149 1.00 45.54  ? 417 PRO   B N   1 
ATOM   6120 C CA  . PRO   B 1 417 ? -4.237  -13.540 -66.486 1.00 47.89  ? 417 PRO   B CA  1 
ATOM   6121 C C   . PRO   B 1 417 ? -3.343  -12.314 -66.580 1.00 47.95  ? 417 PRO   B C   1 
ATOM   6122 O O   . PRO   B 1 417 ? -3.707  -11.221 -66.143 1.00 48.57  ? 417 PRO   B O   1 
ATOM   6123 C CB  . PRO   B 1 417 ? -5.460  -13.406 -67.403 1.00 46.62  ? 417 PRO   B CB  1 
ATOM   6124 C CG  . PRO   B 1 417 ? -6.603  -13.940 -66.600 1.00 43.99  ? 417 PRO   B CG  1 
ATOM   6125 C CD  . PRO   B 1 417 ? -6.291  -13.572 -65.188 1.00 42.75  ? 417 PRO   B CD  1 
ATOM   6126 N N   . LEU   B 1 418 ? -2.177  -12.505 -67.185 1.00 49.73  ? 418 LEU   B N   1 
ATOM   6127 C CA  . LEU   B 1 418 ? -1.238  -11.426 -67.437 1.00 50.63  ? 418 LEU   B CA  1 
ATOM   6128 C C   . LEU   B 1 418 ? -1.104  -11.110 -68.917 1.00 52.27  ? 418 LEU   B C   1 
ATOM   6129 O O   . LEU   B 1 418 ? -1.202  -9.946  -69.315 1.00 56.56  ? 418 LEU   B O   1 
ATOM   6130 C CB  . LEU   B 1 418 ? 0.124   -11.799 -66.842 1.00 53.82  ? 418 LEU   B CB  1 
ATOM   6131 C CG  . LEU   B 1 418 ? 0.772   -10.751 -65.948 1.00 58.48  ? 418 LEU   B CG  1 
ATOM   6132 C CD1 . LEU   B 1 418 ? -0.267  -10.169 -65.004 1.00 52.12  ? 418 LEU   B CD1 1 
ATOM   6133 C CD2 . LEU   B 1 418 ? 1.852   -11.462 -65.165 1.00 56.77  ? 418 LEU   B CD2 1 
ATOM   6134 N N   . GLY   B 1 419 ? -0.891  -12.128 -69.745 1.00 53.74  ? 419 GLY   B N   1 
ATOM   6135 C CA  . GLY   B 1 419 ? -0.775  -11.938 -71.179 1.00 55.86  ? 419 GLY   B CA  1 
ATOM   6136 C C   . GLY   B 1 419 ? -0.711  -13.247 -71.934 1.00 53.12  ? 419 GLY   B C   1 
ATOM   6137 O O   . GLY   B 1 419 ? -1.524  -14.149 -71.710 1.00 57.54  ? 419 GLY   B O   1 
ATOM   6138 N N   . ALA   B 1 420 ? 0.261   -13.360 -72.831 1.00 55.12  ? 420 ALA   B N   1 
ATOM   6139 C CA  . ALA   B 1 420 ? 0.437   -14.572 -73.612 1.00 50.77  ? 420 ALA   B CA  1 
ATOM   6140 C C   . ALA   B 1 420 ? 1.878   -14.634 -74.088 1.00 53.73  ? 420 ALA   B C   1 
ATOM   6141 O O   . ALA   B 1 420 ? 2.562   -13.612 -74.187 1.00 55.42  ? 420 ALA   B O   1 
ATOM   6142 C CB  . ALA   B 1 420 ? -0.534  -14.623 -74.797 1.00 53.76  ? 420 ALA   B CB  1 
ATOM   6143 N N   . ASP   B 1 421 ? 2.335   -15.849 -74.373 1.00 51.96  ? 421 ASP   B N   1 
ATOM   6144 C CA  . ASP   B 1 421 ? 3.651   -16.024 -74.961 1.00 53.83  ? 421 ASP   B CA  1 
ATOM   6145 C C   . ASP   B 1 421 ? 3.573   -15.811 -76.476 1.00 56.00  ? 421 ASP   B C   1 
ATOM   6146 O O   . ASP   B 1 421 ? 2.524   -15.473 -77.031 1.00 56.61  ? 421 ASP   B O   1 
ATOM   6147 C CB  . ASP   B 1 421 ? 4.222   -17.390 -74.575 1.00 52.92  ? 421 ASP   B CB  1 
ATOM   6148 C CG  . ASP   B 1 421 ? 3.568   -18.544 -75.322 1.00 55.92  ? 421 ASP   B CG  1 
ATOM   6149 O OD1 . ASP   B 1 421 ? 2.433   -18.387 -75.816 1.00 56.05  ? 421 ASP   B OD1 1 
ATOM   6150 O OD2 . ASP   B 1 421 ? 4.189   -19.628 -75.395 1.00 56.61  ? 421 ASP   B OD2 1 
ATOM   6151 N N   . GLY   B 1 422 ? 4.703   -16.001 -77.158 1.00 56.39  ? 422 GLY   B N   1 
ATOM   6152 C CA  . GLY   B 1 422 ? 4.795   -15.739 -78.587 1.00 59.95  ? 422 GLY   B CA  1 
ATOM   6153 C C   . GLY   B 1 422 ? 3.901   -16.600 -79.462 1.00 63.62  ? 422 GLY   B C   1 
ATOM   6154 O O   . GLY   B 1 422 ? 3.734   -16.274 -80.643 1.00 65.93  ? 422 GLY   B O   1 
ATOM   6155 N N   . ASN   B 1 423 ? 3.333   -17.679 -78.924 1.00 61.50  ? 423 ASN   B N   1 
ATOM   6156 C CA  . ASN   B 1 423 ? 2.406   -18.532 -79.657 1.00 57.89  ? 423 ASN   B CA  1 
ATOM   6157 C C   . ASN   B 1 423 ? 0.957   -18.260 -79.282 1.00 59.33  ? 423 ASN   B C   1 
ATOM   6158 O O   . ASN   B 1 423 ? 0.070   -19.015 -79.689 1.00 61.60  ? 423 ASN   B O   1 
ATOM   6159 C CB  . ASN   B 1 423 ? 2.739   -20.007 -79.417 1.00 61.32  ? 423 ASN   B CB  1 
ATOM   6160 C CG  . ASN   B 1 423 ? 4.131   -20.382 -79.901 1.00 65.59  ? 423 ASN   B CG  1 
ATOM   6161 O OD1 . ASN   B 1 423 ? 4.564   -19.963 -80.977 1.00 66.96  ? 423 ASN   B OD1 1 
ATOM   6162 N ND2 . ASN   B 1 423 ? 4.843   -21.170 -79.102 1.00 61.89  ? 423 ASN   B ND2 1 
ATOM   6163 N N   . GLY   B 1 424 ? 0.698   -17.198 -78.521 1.00 54.88  ? 424 GLY   B N   1 
ATOM   6164 C CA  . GLY   B 1 424 ? -0.647  -16.877 -78.096 1.00 54.75  ? 424 GLY   B CA  1 
ATOM   6165 C C   . GLY   B 1 424 ? -1.153  -17.673 -76.917 1.00 54.10  ? 424 GLY   B C   1 
ATOM   6166 O O   . GLY   B 1 424 ? -2.342  -17.573 -76.591 1.00 51.96  ? 424 GLY   B O   1 
ATOM   6167 N N   . LEU   B 1 425 ? -0.299  -18.462 -76.269 1.00 49.80  ? 425 LEU   B N   1 
ATOM   6168 C CA  . LEU   B 1 425 ? -0.736  -19.237 -75.111 1.00 52.14  ? 425 LEU   B CA  1 
ATOM   6169 C C   . LEU   B 1 425 ? -0.687  -18.371 -73.856 1.00 50.96  ? 425 LEU   B C   1 
ATOM   6170 O O   . LEU   B 1 425 ? 0.359   -17.788 -73.554 1.00 50.19  ? 425 LEU   B O   1 
ATOM   6171 C CB  . LEU   B 1 425 ? 0.130   -20.481 -74.924 1.00 52.07  ? 425 LEU   B CB  1 
ATOM   6172 C CG  . LEU   B 1 425 ? -0.206  -21.678 -75.819 1.00 53.18  ? 425 LEU   B CG  1 
ATOM   6173 C CD1 . LEU   B 1 425 ? -1.714  -21.917 -75.845 1.00 49.81  ? 425 LEU   B CD1 1 
ATOM   6174 C CD2 . LEU   B 1 425 ? 0.344   -21.503 -77.227 1.00 53.72  ? 425 LEU   B CD2 1 
ATOM   6175 N N   . PRO   B 1 426 ? -1.783  -18.280 -73.100 1.00 51.16  ? 426 PRO   B N   1 
ATOM   6176 C CA  . PRO   B 1 426 ? -1.839  -17.338 -71.974 1.00 49.73  ? 426 PRO   B CA  1 
ATOM   6177 C C   . PRO   B 1 426 ? -0.780  -17.595 -70.912 1.00 47.24  ? 426 PRO   B C   1 
ATOM   6178 O O   . PRO   B 1 426 ? -0.292  -18.714 -70.735 1.00 46.42  ? 426 PRO   B O   1 
ATOM   6179 C CB  . PRO   B 1 426 ? -3.249  -17.561 -71.412 1.00 43.76  ? 426 PRO   B CB  1 
ATOM   6180 C CG  . PRO   B 1 426 ? -4.031  -18.013 -72.595 1.00 43.98  ? 426 PRO   B CG  1 
ATOM   6181 C CD  . PRO   B 1 426 ? -3.084  -18.938 -73.309 1.00 47.84  ? 426 PRO   B CD  1 
ATOM   6182 N N   . ILE   B 1 427 ? -0.431  -16.526 -70.199 1.00 49.81  ? 427 ILE   B N   1 
ATOM   6183 C CA  . ILE   B 1 427 ? 0.463   -16.579 -69.049 1.00 49.15  ? 427 ILE   B CA  1 
ATOM   6184 C C   . ILE   B 1 427 ? -0.247  -15.918 -67.877 1.00 48.62  ? 427 ILE   B C   1 
ATOM   6185 O O   . ILE   B 1 427 ? -0.781  -14.812 -68.014 1.00 50.00  ? 427 ILE   B O   1 
ATOM   6186 C CB  . ILE   B 1 427 ? 1.806   -15.875 -69.321 1.00 49.89  ? 427 ILE   B CB  1 
ATOM   6187 C CG1 . ILE   B 1 427 ? 2.719   -16.754 -70.169 1.00 50.75  ? 427 ILE   B CG1 1 
ATOM   6188 C CG2 . ILE   B 1 427 ? 2.504   -15.545 -68.015 1.00 47.05  ? 427 ILE   B CG2 1 
ATOM   6189 C CD1 . ILE   B 1 427 ? 3.891   -16.008 -70.768 1.00 53.09  ? 427 ILE   B CD1 1 
ATOM   6190 N N   . ASN   B 1 428 ? -0.249  -16.589 -66.731 1.00 45.29  ? 428 ASN   B N   1 
ATOM   6191 C CA  . ASN   B 1 428 ? -0.887  -16.085 -65.528 1.00 45.71  ? 428 ASN   B CA  1 
ATOM   6192 C C   . ASN   B 1 428 ? 0.147   -15.797 -64.447 1.00 47.96  ? 428 ASN   B C   1 
ATOM   6193 O O   . ASN   B 1 428 ? 1.189   -16.455 -64.357 1.00 45.40  ? 428 ASN   B O   1 
ATOM   6194 C CB  . ASN   B 1 428 ? -1.927  -17.073 -64.994 1.00 45.80  ? 428 ASN   B CB  1 
ATOM   6195 C CG  . ASN   B 1 428 ? -3.282  -16.904 -65.649 1.00 44.06  ? 428 ASN   B CG  1 
ATOM   6196 O OD1 . ASN   B 1 428 ? -3.379  -16.647 -66.850 1.00 42.29  ? 428 ASN   B OD1 1 
ATOM   6197 N ND2 . ASN   B 1 428 ? -4.339  -17.045 -64.859 1.00 42.41  ? 428 ASN   B ND2 1 
ATOM   6198 N N   . LEU   B 1 429 ? -0.157  -14.793 -63.633 1.00 45.36  ? 429 LEU   B N   1 
ATOM   6199 C CA  . LEU   B 1 429 ? 0.606   -14.498 -62.433 1.00 46.91  ? 429 LEU   B CA  1 
ATOM   6200 C C   . LEU   B 1 429 ? 0.017   -15.262 -61.254 1.00 46.81  ? 429 LEU   B C   1 
ATOM   6201 O O   . LEU   B 1 429 ? -1.205  -15.401 -61.140 1.00 43.13  ? 429 LEU   B O   1 
ATOM   6202 C CB  . LEU   B 1 429 ? 0.588   -12.992 -62.154 1.00 47.73  ? 429 LEU   B CB  1 
ATOM   6203 C CG  . LEU   B 1 429 ? 1.179   -12.461 -60.845 1.00 46.49  ? 429 LEU   B CG  1 
ATOM   6204 C CD1 . LEU   B 1 429 ? 2.693   -12.583 -60.821 1.00 43.88  ? 429 LEU   B CD1 1 
ATOM   6205 C CD2 . LEU   B 1 429 ? 0.744   -11.019 -60.609 1.00 44.98  ? 429 LEU   B CD2 1 
ATOM   6206 N N   . GLN   B 1 430 ? 0.889   -15.779 -60.389 1.00 46.11  ? 430 GLN   B N   1 
ATOM   6207 C CA  . GLN   B 1 430 ? 0.466   -16.337 -59.110 1.00 45.05  ? 430 GLN   B CA  1 
ATOM   6208 C C   . GLN   B 1 430 ? 0.755   -15.314 -58.019 1.00 46.63  ? 430 GLN   B C   1 
ATOM   6209 O O   . GLN   B 1 430 ? 1.897   -14.868 -57.867 1.00 47.93  ? 430 GLN   B O   1 
ATOM   6210 C CB  . GLN   B 1 430 ? 1.160   -17.663 -58.791 1.00 44.04  ? 430 GLN   B CB  1 
ATOM   6211 C CG  . GLN   B 1 430 ? 0.451   -18.434 -57.666 1.00 45.80  ? 430 GLN   B CG  1 
ATOM   6212 C CD  . GLN   B 1 430 ? 1.255   -19.597 -57.095 1.00 45.11  ? 430 GLN   B CD  1 
ATOM   6213 O OE1 . GLN   B 1 430 ? 0.863   -20.201 -56.093 1.00 45.73  ? 430 GLN   B OE1 1 
ATOM   6214 N NE2 . GLN   B 1 430 ? 2.377   -19.918 -57.729 1.00 44.99  ? 430 GLN   B NE2 1 
ATOM   6215 N N   . ILE   B 1 431 ? -0.279  -14.939 -57.276 1.00 48.71  ? 431 ILE   B N   1 
ATOM   6216 C CA  . ILE   B 1 431 ? -0.164  -14.008 -56.161 1.00 42.46  ? 431 ILE   B CA  1 
ATOM   6217 C C   . ILE   B 1 431 ? -0.409  -14.802 -54.886 1.00 46.25  ? 431 ILE   B C   1 
ATOM   6218 O O   . ILE   B 1 431 ? -1.535  -15.245 -54.630 1.00 44.32  ? 431 ILE   B O   1 
ATOM   6219 C CB  . ILE   B 1 431 ? -1.152  -12.842 -56.287 1.00 40.86  ? 431 ILE   B CB  1 
ATOM   6220 C CG1 . ILE   B 1 431 ? -1.055  -12.215 -57.680 1.00 42.44  ? 431 ILE   B CG1 1 
ATOM   6221 C CG2 . ILE   B 1 431 ? -0.903  -11.814 -55.191 1.00 44.19  ? 431 ILE   B CG2 1 
ATOM   6222 C CD1 . ILE   B 1 431 ? -1.698  -10.850 -57.790 1.00 44.55  ? 431 ILE   B CD1 1 
ATOM   6223 N N   . ILE   B 1 432 ? 0.640   -14.988 -54.089 1.00 45.35  ? 432 ILE   B N   1 
ATOM   6224 C CA  . ILE   B 1 432 ? 0.555   -15.702 -52.821 1.00 40.37  ? 432 ILE   B CA  1 
ATOM   6225 C C   . ILE   B 1 432 ? 0.497   -14.682 -51.696 1.00 40.84  ? 432 ILE   B C   1 
ATOM   6226 O O   . ILE   B 1 432 ? 1.332   -13.772 -51.630 1.00 41.72  ? 432 ILE   B O   1 
ATOM   6227 C CB  . ILE   B 1 432 ? 1.751   -16.650 -52.633 1.00 42.30  ? 432 ILE   B CB  1 
ATOM   6228 C CG1 . ILE   B 1 432 ? 1.968   -17.498 -53.886 1.00 41.45  ? 432 ILE   B CG1 1 
ATOM   6229 C CG2 . ILE   B 1 432 ? 1.547   -17.522 -51.401 1.00 36.42  ? 432 ILE   B CG2 1 
ATOM   6230 C CD1 . ILE   B 1 432 ? 2.980   -18.605 -53.703 1.00 37.17  ? 432 ILE   B CD1 1 
ATOM   6231 N N   . THR   B 1 433 ? -0.487  -14.828 -50.811 1.00 37.73  ? 433 THR   B N   1 
ATOM   6232 C CA  . THR   B 1 433 ? -0.614  -13.985 -49.631 1.00 41.69  ? 433 THR   B CA  1 
ATOM   6233 C C   . THR   B 1 433 ? -0.791  -14.874 -48.405 1.00 43.53  ? 433 THR   B C   1 
ATOM   6234 O O   . THR   B 1 433 ? -1.095  -16.064 -48.514 1.00 40.95  ? 433 THR   B O   1 
ATOM   6235 C CB  . THR   B 1 433 ? -1.782  -12.995 -49.762 1.00 40.47  ? 433 THR   B CB  1 
ATOM   6236 O OG1 . THR   B 1 433 ? -2.997  -13.709 -50.011 1.00 41.56  ? 433 THR   B OG1 1 
ATOM   6237 C CG2 . THR   B 1 433 ? -1.532  -12.022 -50.904 1.00 38.98  ? 433 THR   B CG2 1 
ATOM   6238 N N   . ARG   B 1 434 ? -0.594  -14.282 -47.227 1.00 43.84  ? 434 ARG   B N   1 
ATOM   6239 C CA  . ARG   B 1 434 ? -0.590  -15.044 -45.985 1.00 43.94  ? 434 ARG   B CA  1 
ATOM   6240 C C   . ARG   B 1 434 ? -1.935  -15.732 -45.761 1.00 41.02  ? 434 ARG   B C   1 
ATOM   6241 O O   . ARG   B 1 434 ? -2.964  -15.342 -46.321 1.00 41.32  ? 434 ARG   B O   1 
ATOM   6242 C CB  . ARG   B 1 434 ? -0.264  -14.134 -44.802 1.00 45.06  ? 434 ARG   B CB  1 
ATOM   6243 C CG  . ARG   B 1 434 ? -1.474  -13.458 -44.187 1.00 45.88  ? 434 ARG   B CG  1 
ATOM   6244 C CD  . ARG   B 1 434 ? -1.103  -12.125 -43.569 1.00 49.18  ? 434 ARG   B CD  1 
ATOM   6245 N NE  . ARG   B 1 434 ? -2.246  -11.223 -43.501 1.00 51.67  ? 434 ARG   B NE  1 
ATOM   6246 C CZ  . ARG   B 1 434 ? -2.741  -10.735 -42.373 1.00 54.65  ? 434 ARG   B CZ  1 
ATOM   6247 N NH1 . ARG   B 1 434 ? -2.198  -11.022 -41.201 1.00 56.01  ? 434 ARG   B NH1 1 
ATOM   6248 N NH2 . ARG   B 1 434 ? -3.806  -9.940  -42.422 1.00 50.64  ? 434 ARG   B NH2 1 
ATOM   6249 N N   . ASN   B 1 435 ? -1.909  -16.771 -44.922 1.00 37.94  ? 435 ASN   B N   1 
ATOM   6250 C CA  . ASN   B 1 435 ? -3.104  -17.562 -44.647 1.00 40.84  ? 435 ASN   B CA  1 
ATOM   6251 C C   . ASN   B 1 435 ? -4.255  -16.673 -44.195 1.00 41.03  ? 435 ASN   B C   1 
ATOM   6252 O O   . ASN   B 1 435 ? -4.058  -15.705 -43.454 1.00 42.27  ? 435 ASN   B O   1 
ATOM   6253 C CB  . ASN   B 1 435 ? -2.813  -18.621 -43.578 1.00 36.38  ? 435 ASN   B CB  1 
ATOM   6254 C CG  . ASN   B 1 435 ? -2.096  -19.846 -44.138 1.00 40.93  ? 435 ASN   B CG  1 
ATOM   6255 O OD1 . ASN   B 1 435 ? -2.718  -20.867 -44.416 1.00 43.87  ? 435 ASN   B OD1 1 
ATOM   6256 N ND2 . ASN   B 1 435 ? -0.781  -19.752 -44.281 1.00 45.36  ? 435 ASN   B ND2 1 
ATOM   6257 N N   . TRP   B 1 436 ? -5.456  -16.997 -44.680 1.00 37.94  ? 436 TRP   B N   1 
ATOM   6258 C CA  . TRP   B 1 436 ? -6.721  -16.343 -44.353 1.00 37.23  ? 436 TRP   B CA  1 
ATOM   6259 C C   . TRP   B 1 436 ? -6.877  -14.973 -45.002 1.00 41.64  ? 436 TRP   B C   1 
ATOM   6260 O O   . TRP   B 1 436 ? -7.862  -14.274 -44.726 1.00 43.68  ? 436 TRP   B O   1 
ATOM   6261 C CB  . TRP   B 1 436 ? -6.912  -16.239 -42.835 1.00 41.16  ? 436 TRP   B CB  1 
ATOM   6262 C CG  . TRP   B 1 436 ? -6.806  -17.580 -42.183 1.00 40.28  ? 436 TRP   B CG  1 
ATOM   6263 C CD1 . TRP   B 1 436 ? -5.807  -18.026 -41.367 1.00 39.57  ? 436 TRP   B CD1 1 
ATOM   6264 C CD2 . TRP   B 1 436 ? -7.724  -18.668 -42.328 1.00 37.86  ? 436 TRP   B CD2 1 
ATOM   6265 N NE1 . TRP   B 1 436 ? -6.056  -19.323 -40.982 1.00 39.78  ? 436 TRP   B NE1 1 
ATOM   6266 C CE2 . TRP   B 1 436 ? -7.228  -19.739 -41.559 1.00 40.24  ? 436 TRP   B CE2 1 
ATOM   6267 C CE3 . TRP   B 1 436 ? -8.924  -18.836 -43.026 1.00 40.76  ? 436 TRP   B CE3 1 
ATOM   6268 C CZ2 . TRP   B 1 436 ? -7.892  -20.963 -41.469 1.00 44.63  ? 436 TRP   B CZ2 1 
ATOM   6269 C CZ3 . TRP   B 1 436 ? -9.582  -20.051 -42.936 1.00 43.46  ? 436 TRP   B CZ3 1 
ATOM   6270 C CH2 . TRP   B 1 436 ? -9.064  -21.098 -42.165 1.00 43.66  ? 436 TRP   B CH2 1 
ATOM   6271 N N   . SER   B 1 437 ? -5.951  -14.574 -45.873 1.00 41.00  ? 437 SER   B N   1 
ATOM   6272 C CA  . SER   B 1 437 ? -6.050  -13.315 -46.611 1.00 40.65  ? 437 SER   B CA  1 
ATOM   6273 C C   . SER   B 1 437 ? -6.480  -13.543 -48.056 1.00 42.01  ? 437 SER   B C   1 
ATOM   6274 O O   . SER   B 1 437 ? -5.978  -12.889 -48.975 1.00 41.01  ? 437 SER   B O   1 
ATOM   6275 C CB  . SER   B 1 437 ? -4.721  -12.565 -46.552 1.00 41.53  ? 437 SER   B CB  1 
ATOM   6276 O OG  . SER   B 1 437 ? -3.704  -13.269 -47.241 1.00 42.02  ? 437 SER   B OG  1 
ATOM   6277 N N   . ASP   B 1 438 ? -7.416  -14.474 -48.274 1.00 42.10  ? 438 ASP   B N   1 
ATOM   6278 C CA  . ASP   B 1 438 ? -7.871  -14.779 -49.628 1.00 39.13  ? 438 ASP   B CA  1 
ATOM   6279 C C   . ASP   B 1 438 ? -8.413  -13.538 -50.324 1.00 42.98  ? 438 ASP   B C   1 
ATOM   6280 O O   . ASP   B 1 438 ? -8.135  -13.311 -51.508 1.00 43.53  ? 438 ASP   B O   1 
ATOM   6281 C CB  . ASP   B 1 438 ? -8.934  -15.876 -49.596 1.00 36.13  ? 438 ASP   B CB  1 
ATOM   6282 C CG  . ASP   B 1 438 ? -8.523  -17.068 -48.750 1.00 41.26  ? 438 ASP   B CG  1 
ATOM   6283 O OD1 . ASP   B 1 438 ? -8.085  -16.872 -47.595 1.00 39.13  ? 438 ASP   B OD1 1 
ATOM   6284 O OD2 . ASP   B 1 438 ? -8.631  -18.208 -49.251 1.00 41.03  ? 438 ASP   B OD2 1 
ATOM   6285 N N   . HIS   B 1 439 ? -9.180  -12.717 -49.603 1.00 38.85  ? 439 HIS   B N   1 
ATOM   6286 C CA  . HIS   B 1 439 ? -9.717  -11.501 -50.202 1.00 43.84  ? 439 HIS   B CA  1 
ATOM   6287 C C   . HIS   B 1 439 ? -8.613  -10.506 -50.533 1.00 44.10  ? 439 HIS   B C   1 
ATOM   6288 O O   . HIS   B 1 439 ? -8.753  -9.722  -51.478 1.00 44.69  ? 439 HIS   B O   1 
ATOM   6289 C CB  . HIS   B 1 439 ? -10.751 -10.869 -49.271 1.00 41.24  ? 439 HIS   B CB  1 
ATOM   6290 C CG  . HIS   B 1 439 ? -12.098 -11.514 -49.351 1.00 40.74  ? 439 HIS   B CG  1 
ATOM   6291 N ND1 . HIS   B 1 439 ? -12.824 -11.575 -50.521 1.00 41.20  ? 439 HIS   B ND1 1 
ATOM   6292 C CD2 . HIS   B 1 439 ? -12.846 -12.139 -48.411 1.00 41.44  ? 439 HIS   B CD2 1 
ATOM   6293 C CE1 . HIS   B 1 439 ? -13.964 -12.203 -50.297 1.00 44.40  ? 439 HIS   B CE1 1 
ATOM   6294 N NE2 . HIS   B 1 439 ? -14.002 -12.557 -49.025 1.00 44.74  ? 439 HIS   B NE2 1 
ATOM   6295 N N   . ASP   B 1 440 ? -7.516  -10.519 -49.771 1.00 39.29  ? 440 ASP   B N   1 
ATOM   6296 C CA  . ASP   B 1 440 ? -6.372  -9.688  -50.128 1.00 43.61  ? 440 ASP   B CA  1 
ATOM   6297 C C   . ASP   B 1 440 ? -5.737  -10.166 -51.428 1.00 44.78  ? 440 ASP   B C   1 
ATOM   6298 O O   . ASP   B 1 440 ? -5.314  -9.351  -52.256 1.00 43.85  ? 440 ASP   B O   1 
ATOM   6299 C CB  . ASP   B 1 440 ? -5.340  -9.682  -48.998 1.00 43.27  ? 440 ASP   B CB  1 
ATOM   6300 C CG  . ASP   B 1 440 ? -5.811  -8.912  -47.773 1.00 44.18  ? 440 ASP   B CG  1 
ATOM   6301 O OD1 . ASP   B 1 440 ? -6.424  -7.835  -47.937 1.00 40.91  ? 440 ASP   B OD1 1 
ATOM   6302 O OD2 . ASP   B 1 440 ? -5.550  -9.379  -46.643 1.00 44.00  ? 440 ASP   B OD2 1 
ATOM   6303 N N   . ALA   B 1 441 ? -5.660  -11.487 -51.626 1.00 42.95  ? 441 ALA   B N   1 
ATOM   6304 C CA  . ALA   B 1 441 ? -5.139  -12.012 -52.884 1.00 42.59  ? 441 ALA   B CA  1 
ATOM   6305 C C   . ALA   B 1 441 ? -6.014  -11.589 -54.058 1.00 44.02  ? 441 ALA   B C   1 
ATOM   6306 O O   . ALA   B 1 441 ? -5.501  -11.170 -55.103 1.00 44.22  ? 441 ALA   B O   1 
ATOM   6307 C CB  . ALA   B 1 441 ? -5.025  -13.535 -52.815 1.00 39.92  ? 441 ALA   B CB  1 
ATOM   6308 N N   . ILE   B 1 442 ? -7.338  -11.681 -53.900 1.00 40.60  ? 442 ILE   B N   1 
ATOM   6309 C CA  . ILE   B 1 442 ? -8.252  -11.211 -54.941 1.00 42.51  ? 442 ILE   B CA  1 
ATOM   6310 C C   . ILE   B 1 442 ? -8.061  -9.718  -55.178 1.00 44.89  ? 442 ILE   B C   1 
ATOM   6311 O O   . ILE   B 1 442 ? -7.981  -9.256  -56.323 1.00 43.87  ? 442 ILE   B O   1 
ATOM   6312 C CB  . ILE   B 1 442 ? -9.712  -11.533 -54.565 1.00 41.09  ? 442 ILE   B CB  1 
ATOM   6313 C CG1 . ILE   B 1 442 ? -9.949  -13.044 -54.506 1.00 37.71  ? 442 ILE   B CG1 1 
ATOM   6314 C CG2 . ILE   B 1 442 ? -10.679 -10.869 -55.539 1.00 40.83  ? 442 ILE   B CG2 1 
ATOM   6315 C CD1 . ILE   B 1 442 ? -11.225 -13.429 -53.779 1.00 37.36  ? 442 ILE   B CD1 1 
ATOM   6316 N N   . ARG   B 1 443 ? -7.975  -8.945  -54.092 1.00 43.54  ? 443 ARG   B N   1 
ATOM   6317 C CA  . ARG   B 1 443 ? -7.907  -7.492  -54.208 1.00 45.68  ? 443 ARG   B CA  1 
ATOM   6318 C C   . ARG   B 1 443 ? -6.629  -7.045  -54.908 1.00 46.36  ? 443 ARG   B C   1 
ATOM   6319 O O   . ARG   B 1 443 ? -6.665  -6.158  -55.769 1.00 48.24  ? 443 ARG   B O   1 
ATOM   6320 C CB  . ARG   B 1 443 ? -8.015  -6.855  -52.824 1.00 46.89  ? 443 ARG   B CB  1 
ATOM   6321 C CG  . ARG   B 1 443 ? -7.831  -5.348  -52.814 1.00 49.07  ? 443 ARG   B CG  1 
ATOM   6322 C CD  . ARG   B 1 443 ? -8.788  -4.657  -53.779 1.00 47.99  ? 443 ARG   B CD  1 
ATOM   6323 N NE  . ARG   B 1 443 ? -10.179 -5.048  -53.580 1.00 52.68  ? 443 ARG   B NE  1 
ATOM   6324 C CZ  . ARG   B 1 443 ? -10.933 -4.679  -52.552 1.00 53.29  ? 443 ARG   B CZ  1 
ATOM   6325 N NH1 . ARG   B 1 443 ? -10.460 -3.903  -51.589 1.00 49.94  ? 443 ARG   B NH1 1 
ATOM   6326 N NH2 . ARG   B 1 443 ? -12.195 -5.095  -52.491 1.00 49.52  ? 443 ARG   B NH2 1 
ATOM   6327 N N   . ILE   B 1 444 ? -5.491  -7.644  -54.553 1.00 44.07  ? 444 ILE   B N   1 
ATOM   6328 C CA  . ILE   B 1 444 ? -4.238  -7.292  -55.212 1.00 44.87  ? 444 ILE   B CA  1 
ATOM   6329 C C   . ILE   B 1 444 ? -4.300  -7.648  -56.692 1.00 50.18  ? 444 ILE   B C   1 
ATOM   6330 O O   . ILE   B 1 444 ? -3.882  -6.863  -57.552 1.00 49.55  ? 444 ILE   B O   1 
ATOM   6331 C CB  . ILE   B 1 444 ? -3.053  -7.976  -54.507 1.00 45.27  ? 444 ILE   B CB  1 
ATOM   6332 C CG1 . ILE   B 1 444 ? -2.871  -7.406  -53.099 1.00 45.15  ? 444 ILE   B CG1 1 
ATOM   6333 C CG2 . ILE   B 1 444 ? -1.774  -7.806  -55.309 1.00 49.04  ? 444 ILE   B CG2 1 
ATOM   6334 C CD1 . ILE   B 1 444 ? -2.145  -8.340  -52.154 1.00 44.12  ? 444 ILE   B CD1 1 
ATOM   6335 N N   . GLY   B 1 445 ? -4.836  -8.828  -57.014 1.00 51.33  ? 445 GLY   B N   1 
ATOM   6336 C CA  . GLY   B 1 445 ? -4.957  -9.221  -58.411 1.00 49.67  ? 445 GLY   B CA  1 
ATOM   6337 C C   . GLY   B 1 445 ? -5.812  -8.263  -59.220 1.00 50.31  ? 445 GLY   B C   1 
ATOM   6338 O O   . GLY   B 1 445 ? -5.463  -7.905  -60.348 1.00 49.95  ? 445 GLY   B O   1 
ATOM   6339 N N   . ALA   B 1 446 ? -6.944  -7.835  -58.656 1.00 48.92  ? 446 ALA   B N   1 
ATOM   6340 C CA  . ALA   B 1 446 ? -7.767  -6.834  -59.326 1.00 47.67  ? 446 ALA   B CA  1 
ATOM   6341 C C   . ALA   B 1 446 ? -6.993  -5.539  -59.538 1.00 51.32  ? 446 ALA   B C   1 
ATOM   6342 O O   . ALA   B 1 446 ? -7.088  -4.919  -60.602 1.00 54.44  ? 446 ALA   B O   1 
ATOM   6343 C CB  . ALA   B 1 446 ? -9.038  -6.574  -58.519 1.00 41.39  ? 446 ALA   B CB  1 
ATOM   6344 N N   . LEU   B 1 447 ? -6.211  -5.124  -58.539 1.00 52.23  ? 447 LEU   B N   1 
ATOM   6345 C CA  . LEU   B 1 447 ? -5.424  -3.899  -58.663 1.00 53.60  ? 447 LEU   B CA  1 
ATOM   6346 C C   . LEU   B 1 447 ? -4.347  -4.042  -59.734 1.00 53.49  ? 447 LEU   B C   1 
ATOM   6347 O O   . LEU   B 1 447 ? -4.147  -3.135  -60.551 1.00 57.02  ? 447 LEU   B O   1 
ATOM   6348 C CB  . LEU   B 1 447 ? -4.799  -3.543  -57.313 1.00 49.92  ? 447 LEU   B CB  1 
ATOM   6349 C CG  . LEU   B 1 447 ? -5.747  -3.068  -56.211 1.00 49.07  ? 447 LEU   B CG  1 
ATOM   6350 C CD1 . LEU   B 1 447 ? -5.003  -2.955  -54.894 1.00 47.50  ? 447 LEU   B CD1 1 
ATOM   6351 C CD2 . LEU   B 1 447 ? -6.399  -1.741  -56.580 1.00 51.86  ? 447 LEU   B CD2 1 
ATOM   6352 N N   . VAL   B 1 448 ? -3.634  -5.173  -59.736 1.00 51.03  ? 448 VAL   B N   1 
ATOM   6353 C CA  . VAL   B 1 448 ? -2.634  -5.431  -60.769 1.00 52.57  ? 448 VAL   B CA  1 
ATOM   6354 C C   . VAL   B 1 448 ? -3.273  -5.367  -62.149 1.00 57.03  ? 448 VAL   B C   1 
ATOM   6355 O O   . VAL   B 1 448 ? -2.691  -4.827  -63.099 1.00 57.15  ? 448 VAL   B O   1 
ATOM   6356 C CB  . VAL   B 1 448 ? -1.957  -6.795  -60.526 1.00 53.08  ? 448 VAL   B CB  1 
ATOM   6357 C CG1 . VAL   B 1 448 ? -1.091  -7.192  -61.717 1.00 50.69  ? 448 VAL   B CG1 1 
ATOM   6358 C CG2 . VAL   B 1 448 ? -1.142  -6.773  -59.242 1.00 50.17  ? 448 VAL   B CG2 1 
ATOM   6359 N N   . ALA   B 1 449 ? -4.489  -5.906  -62.276 1.00 55.86  ? 449 ALA   B N   1 
ATOM   6360 C CA  . ALA   B 1 449 ? -5.183  -5.903  -63.559 1.00 58.56  ? 449 ALA   B CA  1 
ATOM   6361 C C   . ALA   B 1 449 ? -5.471  -4.481  -64.029 1.00 61.58  ? 449 ALA   B C   1 
ATOM   6362 O O   . ALA   B 1 449 ? -5.196  -4.130  -65.182 1.00 64.27  ? 449 ALA   B O   1 
ATOM   6363 C CB  . ALA   B 1 449 ? -6.476  -6.712  -63.455 1.00 56.32  ? 449 ALA   B CB  1 
ATOM   6364 N N   . GLU   B 1 450 ? -6.031  -3.646  -63.150 1.00 59.96  ? 450 GLU   B N   1 
ATOM   6365 C CA  . GLU   B 1 450 ? -6.315  -2.264  -63.525 1.00 64.03  ? 450 GLU   B CA  1 
ATOM   6366 C C   . GLU   B 1 450 ? -5.051  -1.433  -63.703 1.00 63.81  ? 450 GLU   B C   1 
ATOM   6367 O O   . GLU   B 1 450 ? -5.109  -0.376  -64.339 1.00 67.71  ? 450 GLU   B O   1 
ATOM   6368 C CB  . GLU   B 1 450 ? -7.230  -1.617  -62.486 1.00 65.76  ? 450 GLU   B CB  1 
ATOM   6369 C CG  . GLU   B 1 450 ? -8.336  -2.533  -61.996 1.00 67.46  ? 450 GLU   B CG  1 
ATOM   6370 C CD  . GLU   B 1 450 ? -9.214  -1.891  -60.942 1.00 71.67  ? 450 GLU   B CD  1 
ATOM   6371 O OE1 . GLU   B 1 450 ? -10.438 -2.148  -60.950 1.00 75.51  ? 450 GLU   B OE1 1 
ATOM   6372 O OE2 . GLU   B 1 450 ? -8.682  -1.136  -60.103 1.00 72.66  ? 450 GLU   B OE2 1 
ATOM   6373 N N   . ALA   B 1 451 ? -3.915  -1.881  -63.163 1.00 58.49  ? 451 ALA   B N   1 
ATOM   6374 C CA  . ALA   B 1 451 ? -2.649  -1.203  -63.423 1.00 63.25  ? 451 ALA   B CA  1 
ATOM   6375 C C   . ALA   B 1 451 ? -2.079  -1.566  -64.785 1.00 67.68  ? 451 ALA   B C   1 
ATOM   6376 O O   . ALA   B 1 451 ? -1.409  -0.737  -65.412 1.00 66.78  ? 451 ALA   B O   1 
ATOM   6377 C CB  . ALA   B 1 451 ? -1.630  -1.534  -62.334 1.00 58.92  ? 451 ALA   B CB  1 
ATOM   6378 N N   . LEU   B 1 452 ? -2.334  -2.786  -65.257 1.00 64.65  ? 452 LEU   B N   1 
ATOM   6379 C CA  . LEU   B 1 452 ? -1.887  -3.221  -66.575 1.00 63.64  ? 452 LEU   B CA  1 
ATOM   6380 C C   . LEU   B 1 452 ? -2.865  -2.783  -67.658 1.00 68.12  ? 452 LEU   B C   1 
ATOM   6381 O O   . LEU   B 1 452 ? -2.973  -3.430  -68.704 1.00 69.48  ? 452 LEU   B O   1 
ATOM   6382 C CB  . LEU   B 1 452 ? -1.713  -4.740  -66.603 1.00 58.07  ? 452 LEU   B CB  1 
ATOM   6383 C CG  . LEU   B 1 452 ? -0.505  -5.301  -65.856 1.00 60.70  ? 452 LEU   B CG  1 
ATOM   6384 C CD1 . LEU   B 1 452 ? -0.364  -6.792  -66.103 1.00 56.85  ? 452 LEU   B CD1 1 
ATOM   6385 C CD2 . LEU   B 1 452 ? 0.751   -4.573  -66.285 1.00 59.05  ? 452 LEU   B CD2 1 
ATOM   6386 N N   . ASP   B 1 453 ? -3.573  -1.682  -67.416 1.00 69.95  ? 453 ASP   B N   1 
ATOM   6387 C CA  . ASP   B 1 453 ? -4.536  -1.166  -68.379 1.00 76.40  ? 453 ASP   B CA  1 
ATOM   6388 C C   . ASP   B 1 453 ? -4.353  0.329   -68.592 1.00 80.01  ? 453 ASP   B C   1 
ATOM   6389 O O   . ASP   B 1 453 ? -4.594  0.842   -69.690 1.00 80.61  ? 453 ASP   B O   1 
ATOM   6390 C CB  . ASP   B 1 453 ? -5.963  -1.442  -67.907 1.00 76.47  ? 453 ASP   B CB  1 
ATOM   6391 C CG  . ASP   B 1 453 ? -6.432  -2.828  -68.261 1.00 76.55  ? 453 ASP   B CG  1 
ATOM   6392 O OD1 . ASP   B 1 453 ? -6.070  -3.318  -69.352 1.00 77.73  ? 453 ASP   B OD1 1 
ATOM   6393 O OD2 . ASP   B 1 453 ? -7.170  -3.422  -67.448 1.00 77.81  ? 453 ASP   B OD2 1 
ATOM   6394 N N   . ARG   B 1 454 ? -3.935  1.034   -67.547 1.00 80.81  ? 454 ARG   B N   1 
ATOM   6395 C CA  . ARG   B 1 454 ? -3.944  2.491   -67.562 1.00 84.67  ? 454 ARG   B CA  1 
ATOM   6396 C C   . ARG   B 1 454 ? -3.052  3.087   -66.474 1.00 83.64  ? 454 ARG   B C   1 
ATOM   6397 O O   . ARG   B 1 454 ? -2.921  2.531   -65.384 1.00 79.52  ? 454 ARG   B O   1 
ATOM   6398 C CB  . ARG   B 1 454 ? -5.382  2.991   -67.411 1.00 85.55  ? 454 ARG   B CB  1 
ATOM   6399 C CG  . ARG   B 1 454 ? -6.094  2.381   -66.217 1.00 83.40  ? 454 ARG   B CG  1 
ATOM   6400 C CD  . ARG   B 1 454 ? -7.506  1.937   -66.562 1.00 85.02  ? 454 ARG   B CD  1 
ATOM   6401 N NE  . ARG   B 1 454 ? -8.277  1.628   -65.363 1.00 87.43  ? 454 ARG   B NE  1 
ATOM   6402 C CZ  . ARG   B 1 454 ? -9.191  0.670   -65.279 1.00 85.31  ? 454 ARG   B CZ  1 
ATOM   6403 N NH1 . ARG   B 1 454 ? -9.479  -0.105  -66.314 1.00 81.44  ? 454 ARG   B NH1 1 
ATOM   6404 N NH2 . ARG   B 1 454 ? -9.828  0.480   -64.127 1.00 81.57  ? 454 ARG   B NH2 1 
HETATM 6405 C C05 . A1D5H C 2 .   ? -8.067  -34.690 -20.421 1.00 46.11  ? 501 A1D5H A C05 1 
HETATM 6406 C C09 . A1D5H C 2 .   ? -6.660  -30.643 -22.318 1.00 48.30  ? 501 A1D5H A C09 1 
HETATM 6407 C C10 . A1D5H C 2 .   ? -5.308  -30.283 -22.902 1.00 43.43  ? 501 A1D5H A C10 1 
HETATM 6408 C C02 . A1D5H C 2 .   ? -8.788  -37.292 -20.937 1.00 51.52  ? 501 A1D5H A C02 1 
HETATM 6409 C C03 . A1D5H C 2 .   ? -7.573  -36.814 -21.398 1.00 50.28  ? 501 A1D5H A C03 1 
HETATM 6410 C C04 . A1D5H C 2 .   ? -7.214  -35.507 -21.141 1.00 45.39  ? 501 A1D5H A C04 1 
HETATM 6411 C C07 . A1D5H C 2 .   ? -7.766  -32.436 -21.301 1.00 46.54  ? 501 A1D5H A C07 1 
HETATM 6412 C C11 . A1D5H C 2 .   ? -5.338  -30.174 -24.421 1.00 45.44  ? 501 A1D5H A C11 1 
HETATM 6413 C C12 . A1D5H C 2 .   ? -4.175  -30.933 -25.051 1.00 45.36  ? 501 A1D5H A C12 1 
HETATM 6414 C C15 . A1D5H C 2 .   ? -9.281  -35.162 -19.965 1.00 44.44  ? 501 A1D5H A C15 1 
HETATM 6415 C C16 . A1D5H C 2 .   ? -9.642  -36.470 -20.224 1.00 46.56  ? 501 A1D5H A C16 1 
HETATM 6416 N N01 . A1D5H C 2 .   ? -9.168  -38.664 -21.202 1.00 60.06  ? 501 A1D5H A N01 1 
HETATM 6417 N N06 . A1D5H C 2 .   ? -7.692  -33.322 -20.166 1.00 47.41  ? 501 A1D5H A N06 1 
HETATM 6418 O O08 . A1D5H C 2 .   ? -6.600  -31.971 -21.903 1.00 53.11  ? 501 A1D5H A O08 1 
HETATM 6419 O O13 . A1D5H C 2 .   ? -4.077  -32.177 -24.411 1.00 46.75  ? 501 A1D5H A O13 1 
HETATM 6420 O O14 . A1D5H C 2 .   ? -8.824  -32.105 -21.708 1.00 41.58  ? 501 A1D5H A O14 1 
HETATM 6421 C C05 . A1D5H D 2 .   ? -2.010  -33.437 -59.390 1.00 52.20  ? 501 A1D5H B C05 1 
HETATM 6422 C C09 . A1D5H D 2 .   ? -5.306  -32.254 -58.075 1.00 52.51  ? 501 A1D5H B C09 1 
HETATM 6423 C C10 . A1D5H D 2 .   ? -6.579  -31.598 -57.557 1.00 47.21  ? 501 A1D5H B C10 1 
HETATM 6424 C C02 . A1D5H D 2 .   ? 0.303   -34.680 -58.561 1.00 56.87  ? 501 A1D5H B C02 1 
HETATM 6425 C C03 . A1D5H D 2 .   ? -0.918  -35.093 -58.058 1.00 54.76  ? 501 A1D5H B C03 1 
HETATM 6426 C C04 . A1D5H D 2 .   ? -2.079  -34.468 -58.472 1.00 49.59  ? 501 A1D5H B C04 1 
HETATM 6427 C C07 . A1D5H D 2 .   ? -3.483  -31.468 -59.283 1.00 47.17  ? 501 A1D5H B C07 1 
HETATM 6428 C C11 . A1D5H D 2 .   ? -7.465  -32.590 -56.817 1.00 43.74  ? 501 A1D5H B C11 1 
HETATM 6429 C C12 . A1D5H D 2 .   ? -7.740  -32.146 -55.386 1.00 48.54  ? 501 A1D5H B C12 1 
HETATM 6430 C C15 . A1D5H D 2 .   ? -0.794  -33.016 -59.890 1.00 49.97  ? 501 A1D5H B C15 1 
HETATM 6431 C C16 . A1D5H D 2 .   ? 0.365   -33.642 -59.472 1.00 52.20  ? 501 A1D5H B C16 1 
HETATM 6432 N N01 . A1D5H D 2 .   ? 1.523   -35.334 -58.130 1.00 62.82  ? 501 A1D5H B N01 1 
HETATM 6433 N N06 . A1D5H D 2 .   ? -3.220  -32.781 -59.816 1.00 50.55  ? 501 A1D5H B N06 1 
HETATM 6434 O O08 . A1D5H D 2 .   ? -4.279  -31.309 -58.149 1.00 50.78  ? 501 A1D5H B O08 1 
HETATM 6435 O O13 . A1D5H D 2 .   ? -8.449  -33.165 -54.738 1.00 51.68  ? 501 A1D5H B O13 1 
HETATM 6436 O O14 . A1D5H D 2 .   ? -3.046  -30.521 -59.833 1.00 45.72  ? 501 A1D5H B O14 1 
HETATM 6437 O O   . HOH   E 3 .   ? -12.776 -48.219 -10.292 1.00 49.17  ? 601 HOH   A O   1 
HETATM 6438 O O   . HOH   E 3 .   ? -28.243 -36.159 -37.445 1.00 44.66  ? 602 HOH   A O   1 
HETATM 6439 O O   . HOH   E 3 .   ? -29.643 -38.419 -24.219 1.00 53.12  ? 603 HOH   A O   1 
HETATM 6440 O O   . HOH   E 3 .   ? -12.166 -30.294 -26.962 1.00 40.27  ? 604 HOH   A O   1 
HETATM 6441 O O   . HOH   E 3 .   ? -39.551 -14.406 -18.481 1.00 63.17  ? 605 HOH   A O   1 
HETATM 6442 O O   . HOH   E 3 .   ? -24.021 -36.881 -6.132  1.00 48.01  ? 606 HOH   A O   1 
HETATM 6443 O O   . HOH   E 3 .   ? -27.826 -41.282 -18.116 1.00 43.98  ? 607 HOH   A O   1 
HETATM 6444 O O   . HOH   E 3 .   ? -15.118 -28.443 -36.672 1.00 43.90  ? 608 HOH   A O   1 
HETATM 6445 O O   . HOH   E 3 .   ? -13.715 -13.884 -33.386 1.00 42.30  ? 609 HOH   A O   1 
HETATM 6446 O O   . HOH   E 3 .   ? 0.176   -2.484  -25.481 1.00 50.14  ? 610 HOH   A O   1 
HETATM 6447 O O   . HOH   E 3 .   ? -18.135 -41.622 -36.021 1.00 48.14  ? 611 HOH   A O   1 
HETATM 6448 O O   . HOH   E 3 .   ? -17.108 -7.836  -18.864 1.00 38.08  ? 612 HOH   A O   1 
HETATM 6449 O O   . HOH   E 3 .   ? 0.167   -20.744 -5.538  1.00 43.05  ? 613 HOH   A O   1 
HETATM 6450 O O   . HOH   E 3 .   ? -26.517 -20.863 -34.642 1.00 46.29  ? 614 HOH   A O   1 
HETATM 6451 O O   . HOH   E 3 .   ? -23.241 -29.758 -15.012 1.00 31.82  ? 615 HOH   A O   1 
HETATM 6452 O O   . HOH   E 3 .   ? -3.536  -35.565 -33.869 1.00 46.64  ? 616 HOH   A O   1 
HETATM 6453 O O   . HOH   E 3 .   ? 6.450   -20.349 -21.038 1.00 40.56  ? 617 HOH   A O   1 
HETATM 6454 O O   . HOH   E 3 .   ? -10.886 -33.987 0.109   1.00 41.63  ? 618 HOH   A O   1 
HETATM 6455 O O   . HOH   E 3 .   ? -1.654  -20.228 -29.208 1.00 40.41  ? 619 HOH   A O   1 
HETATM 6456 O O   . HOH   E 3 .   ? 1.108   -5.925  -22.873 1.00 48.97  ? 620 HOH   A O   1 
HETATM 6457 O O   . HOH   E 3 .   ? -32.961 -37.551 -18.018 1.00 53.79  ? 621 HOH   A O   1 
HETATM 6458 O O   . HOH   E 3 .   ? -15.723 -11.012 -34.708 1.00 54.51  ? 622 HOH   A O   1 
HETATM 6459 O O   . HOH   E 3 .   ? -9.533  -36.696 -0.878  1.00 45.63  ? 623 HOH   A O   1 
HETATM 6460 O O   . HOH   E 3 .   ? -10.596 -23.230 -31.664 1.00 35.06  ? 624 HOH   A O   1 
HETATM 6461 O O   . HOH   E 3 .   ? -19.758 -33.860 -5.439  1.00 42.51  ? 625 HOH   A O   1 
HETATM 6462 O O   . HOH   E 3 .   ? 8.356   -26.296 -26.431 1.00 46.35  ? 626 HOH   A O   1 
HETATM 6463 O O   . HOH   E 3 .   ? -9.577  -33.894 -36.773 1.00 44.92  ? 627 HOH   A O   1 
HETATM 6464 O O   . HOH   E 3 .   ? 8.500   -24.066 -25.865 1.00 42.98  ? 628 HOH   A O   1 
HETATM 6465 O O   . HOH   E 3 .   ? -5.983  -18.219 -33.698 1.00 38.73  ? 629 HOH   A O   1 
HETATM 6466 O O   . HOH   E 3 .   ? -41.756 -26.099 -25.659 1.00 55.55  ? 630 HOH   A O   1 
HETATM 6467 O O   . HOH   E 3 .   ? -23.315 -37.695 -3.407  1.00 52.69  ? 631 HOH   A O   1 
HETATM 6468 O O   . HOH   E 3 .   ? -21.855 -11.632 -31.107 1.00 42.90  ? 632 HOH   A O   1 
HETATM 6469 O O   . HOH   E 3 .   ? -16.979 -11.375 -10.570 1.00 52.52  ? 633 HOH   A O   1 
HETATM 6470 O O   . HOH   E 3 .   ? -22.986 -31.595 -12.498 1.00 35.57  ? 634 HOH   A O   1 
HETATM 6471 O O   . HOH   E 3 .   ? 8.970   -10.630 -13.130 1.00 49.25  ? 635 HOH   A O   1 
HETATM 6472 O O   . HOH   E 3 .   ? -6.896  -5.306  -10.828 1.00 42.33  ? 636 HOH   A O   1 
HETATM 6473 O O   . HOH   E 3 .   ? -20.435 -32.579 -25.540 1.00 39.22  ? 637 HOH   A O   1 
HETATM 6474 O O   . HOH   E 3 .   ? 7.615   1.336   -9.131  1.00 46.74  ? 638 HOH   A O   1 
HETATM 6475 O O   . HOH   E 3 .   ? -28.162 -24.364 -35.573 1.00 43.55  ? 639 HOH   A O   1 
HETATM 6476 O O   . HOH   E 3 .   ? 7.947   -0.083  -18.993 1.00 52.38  ? 640 HOH   A O   1 
HETATM 6477 O O   . HOH   E 3 .   ? -28.167 -34.711 -6.498  1.00 51.87  ? 641 HOH   A O   1 
HETATM 6478 O O   . HOH   E 3 .   ? -27.811 -31.506 -3.597  1.00 45.56  ? 642 HOH   A O   1 
HETATM 6479 O O   . HOH   E 3 .   ? -6.028  -25.480 1.160   1.00 38.87  ? 643 HOH   A O   1 
HETATM 6480 O O   . HOH   E 3 .   ? -4.566  -15.274 -37.818 1.00 51.23  ? 644 HOH   A O   1 
HETATM 6481 O O   . HOH   E 3 .   ? -23.582 -38.749 -40.956 1.00 44.73  ? 645 HOH   A O   1 
HETATM 6482 O O   . HOH   E 3 .   ? -20.484 -42.285 -14.722 1.00 46.11  ? 646 HOH   A O   1 
HETATM 6483 O O   . HOH   E 3 .   ? 9.101   -31.065 -9.477  1.00 38.20  ? 647 HOH   A O   1 
HETATM 6484 O O   . HOH   E 3 .   ? 7.887   -13.559 -27.933 1.00 45.69  ? 648 HOH   A O   1 
HETATM 6485 O O   . HOH   E 3 .   ? -14.680 -45.137 -42.617 1.00 51.28  ? 649 HOH   A O   1 
HETATM 6486 O O   . HOH   E 3 .   ? -16.929 -14.459 -40.094 1.00 40.37  ? 650 HOH   A O   1 
HETATM 6487 O O   . HOH   E 3 .   ? -22.054 -22.586 -11.045 1.00 37.67  ? 651 HOH   A O   1 
HETATM 6488 O O   . HOH   E 3 .   ? -15.101 -33.567 0.685   1.00 41.61  ? 652 HOH   A O   1 
HETATM 6489 O O   . HOH   E 3 .   ? -18.524 -28.153 -8.522  1.00 32.60  ? 653 HOH   A O   1 
HETATM 6490 O O   . HOH   E 3 .   ? -14.662 -11.937 -15.972 1.00 40.64  ? 654 HOH   A O   1 
HETATM 6491 O O   . HOH   E 3 .   ? -8.020  -9.573  -1.123  1.00 46.79  ? 655 HOH   A O   1 
HETATM 6492 O O   . HOH   E 3 .   ? -4.938  -23.592 -15.586 1.00 34.27  ? 656 HOH   A O   1 
HETATM 6493 O O   . HOH   E 3 .   ? -5.395  5.682   -16.177 1.00 59.27  ? 657 HOH   A O   1 
HETATM 6494 O O   . HOH   E 3 .   ? 7.411   -12.269 -22.214 1.00 47.55  ? 658 HOH   A O   1 
HETATM 6495 O O   . HOH   E 3 .   ? -19.585 -17.468 -33.942 1.00 41.26  ? 659 HOH   A O   1 
HETATM 6496 O O   . HOH   E 3 .   ? -10.894 -32.902 -34.391 1.00 41.33  ? 660 HOH   A O   1 
HETATM 6497 O O   . HOH   E 3 .   ? -26.844 -15.536 -35.003 1.00 48.76  ? 661 HOH   A O   1 
HETATM 6498 O O   . HOH   E 3 .   ? -4.541  -50.457 -38.009 1.00 49.75  ? 662 HOH   A O   1 
HETATM 6499 O O   . HOH   E 3 .   ? -12.777 -3.236  -23.847 1.00 36.75  ? 663 HOH   A O   1 
HETATM 6500 O O   . HOH   E 3 .   ? -8.754  -6.464  -13.073 1.00 39.90  ? 664 HOH   A O   1 
HETATM 6501 O O   . HOH   E 3 .   ? 4.366   -13.438 -4.765  1.00 45.66  ? 665 HOH   A O   1 
HETATM 6502 O O   . HOH   E 3 .   ? -29.945 -41.007 -30.827 1.00 48.06  ? 666 HOH   A O   1 
HETATM 6503 O O   . HOH   E 3 .   ? -8.039  -46.266 -48.305 1.00 49.70  ? 667 HOH   A O   1 
HETATM 6504 O O   . HOH   E 3 .   ? -12.458 -35.421 -39.567 1.00 39.64  ? 668 HOH   A O   1 
HETATM 6505 O O   . HOH   E 3 .   ? -13.170 -30.050 -30.989 1.00 34.75  ? 669 HOH   A O   1 
HETATM 6506 O O   . HOH   E 3 .   ? -7.095  -32.147 -7.209  1.00 40.84  ? 670 HOH   A O   1 
HETATM 6507 O O   . HOH   E 3 .   ? -18.286 -8.507  -25.559 1.00 42.89  ? 671 HOH   A O   1 
HETATM 6508 O O   . HOH   E 3 .   ? -16.737 -27.218 -40.342 1.00 49.85  ? 672 HOH   A O   1 
HETATM 6509 O O   . HOH   E 3 .   ? -26.292 -23.570 -33.637 1.00 41.37  ? 673 HOH   A O   1 
HETATM 6510 O O   . HOH   E 3 .   ? -11.261 -18.363 -36.861 1.00 37.83  ? 674 HOH   A O   1 
HETATM 6511 O O   . HOH   E 3 .   ? -2.640  -27.248 -1.424  1.00 36.65  ? 675 HOH   A O   1 
HETATM 6512 O O   . HOH   E 3 .   ? -5.559  -26.307 -34.874 1.00 48.94  ? 676 HOH   A O   1 
HETATM 6513 O O   . HOH   E 3 .   ? -17.769 -38.229 -5.925  1.00 43.20  ? 677 HOH   A O   1 
HETATM 6514 O O   . HOH   E 3 .   ? -26.766 -12.938 -13.291 1.00 65.68  ? 678 HOH   A O   1 
HETATM 6515 O O   . HOH   E 3 .   ? 4.897   2.439   -23.910 1.00 54.26  ? 679 HOH   A O   1 
HETATM 6516 O O   . HOH   E 3 .   ? -22.614 -24.624 -38.957 1.00 43.59  ? 680 HOH   A O   1 
HETATM 6517 O O   . HOH   E 3 .   ? 1.554   -46.842 -37.276 1.00 51.11  ? 681 HOH   A O   1 
HETATM 6518 O O   . HOH   E 3 .   ? -21.398 -13.326 -28.441 1.00 37.95  ? 682 HOH   A O   1 
HETATM 6519 O O   . HOH   E 3 .   ? -38.839 -27.395 -20.141 1.00 50.18  ? 683 HOH   A O   1 
HETATM 6520 O O   . HOH   E 3 .   ? -32.542 -26.964 -9.417  1.00 44.89  ? 684 HOH   A O   1 
HETATM 6521 O O   . HOH   E 3 .   ? -32.709 -13.101 -21.281 1.00 50.71  ? 685 HOH   A O   1 
HETATM 6522 O O   . HOH   E 3 .   ? -34.691 -13.436 -23.549 1.00 48.46  ? 686 HOH   A O   1 
HETATM 6523 O O   . HOH   E 3 .   ? -36.754 -31.682 -10.272 1.00 48.83  ? 687 HOH   A O   1 
HETATM 6524 O O   . HOH   E 3 .   ? -27.979 -41.864 -28.419 1.00 47.15  ? 688 HOH   A O   1 
HETATM 6525 O O   . HOH   E 3 .   ? -11.093 -5.750  -9.125  1.00 51.52  ? 689 HOH   A O   1 
HETATM 6526 O O   . HOH   E 3 .   ? 6.367   -38.674 -15.821 1.00 47.19  ? 690 HOH   A O   1 
HETATM 6527 O O   . HOH   E 3 .   ? 6.529   -35.474 -13.687 1.00 40.98  ? 691 HOH   A O   1 
HETATM 6528 O O   . HOH   E 3 .   ? -17.060 -9.756  -12.697 1.00 50.48  ? 692 HOH   A O   1 
HETATM 6529 O O   . HOH   E 3 .   ? -5.165  -34.529 -6.232  1.00 41.30  ? 693 HOH   A O   1 
HETATM 6530 O O   . HOH   E 3 .   ? -37.390 -28.160 -33.022 1.00 51.12  ? 694 HOH   A O   1 
HETATM 6531 O O   . HOH   E 3 .   ? 4.457   -12.775 -18.201 1.00 46.09  ? 695 HOH   A O   1 
HETATM 6532 O O   . HOH   E 3 .   ? -21.433 -10.000 -19.863 1.00 34.32  ? 696 HOH   A O   1 
HETATM 6533 O O   . HOH   E 3 .   ? -18.421 -9.374  -29.348 1.00 52.61  ? 697 HOH   A O   1 
HETATM 6534 O O   . HOH   E 3 .   ? -33.052 -31.181 -6.927  1.00 52.98  ? 698 HOH   A O   1 
HETATM 6535 O O   . HOH   E 3 .   ? -9.371  -42.015 -5.636  1.00 51.11  ? 699 HOH   A O   1 
HETATM 6536 O O   . HOH   E 3 .   ? -8.528  -5.302  -5.216  1.00 42.67  ? 700 HOH   A O   1 
HETATM 6537 O O   . HOH   E 3 .   ? 7.251   -12.915 -9.346  1.00 41.03  ? 701 HOH   A O   1 
HETATM 6538 O O   . HOH   E 3 .   ? 5.179   -21.847 -6.912  1.00 53.71  ? 702 HOH   A O   1 
HETATM 6539 O O   . HOH   E 3 .   ? -15.662 -37.594 -4.120  1.00 44.30  ? 703 HOH   A O   1 
HETATM 6540 O O   . HOH   E 3 .   ? -5.905  -28.949 -38.508 1.00 55.15  ? 704 HOH   A O   1 
HETATM 6541 O O   . HOH   E 3 .   ? -37.910 -28.463 -17.718 1.00 47.67  ? 705 HOH   A O   1 
HETATM 6542 O O   . HOH   E 3 .   ? 3.231   -19.926 -6.318  1.00 44.28  ? 706 HOH   A O   1 
HETATM 6543 O O   . HOH   E 3 .   ? 5.508   -18.698 -7.405  1.00 55.89  ? 707 HOH   A O   1 
HETATM 6544 O O   . HOH   E 3 .   ? -15.988 -32.935 2.736   1.00 51.30  ? 708 HOH   A O   1 
HETATM 6545 O O   . HOH   E 3 .   ? -5.615  -36.233 -0.754  1.00 46.91  ? 709 HOH   A O   1 
HETATM 6546 O O   . HOH   E 3 .   ? -19.133 -12.567 -39.962 1.00 46.75  ? 710 HOH   A O   1 
HETATM 6547 O O   . HOH   E 3 .   ? -8.453  -10.736 -36.359 1.00 43.88  ? 711 HOH   A O   1 
HETATM 6548 O O   . HOH   E 3 .   ? -20.908 -9.009  -27.199 1.00 59.74  ? 712 HOH   A O   1 
HETATM 6549 O O   . HOH   E 3 .   ? -25.987 -33.818 -4.474  1.00 50.94  ? 713 HOH   A O   1 
HETATM 6550 O O   . HOH   E 3 .   ? -8.513  -32.063 1.600   1.00 46.81  ? 714 HOH   A O   1 
HETATM 6551 O O   . HOH   E 3 .   ? -18.936 -5.834  -20.352 1.00 37.34  ? 715 HOH   A O   1 
HETATM 6552 O O   . HOH   E 3 .   ? 6.487   -13.307 -7.015  1.00 39.52  ? 716 HOH   A O   1 
HETATM 6553 O O   . HOH   F 3 .   ? 11.089  -27.711 -64.486 1.00 54.45  ? 601 HOH   B O   1 
HETATM 6554 O O   . HOH   F 3 .   ? -17.639 -9.685  -62.135 1.00 43.89  ? 602 HOH   B O   1 
HETATM 6555 O O   . HOH   F 3 .   ? -1.691  -21.286 -71.711 1.00 44.68  ? 603 HOH   B O   1 
HETATM 6556 O O   . HOH   F 3 .   ? -0.588  -31.062 -79.846 1.00 44.80  ? 604 HOH   B O   1 
HETATM 6557 O O   . HOH   F 3 .   ? -16.776 -14.336 -64.814 1.00 44.11  ? 605 HOH   B O   1 
HETATM 6558 O O   . HOH   F 3 .   ? 9.139   -24.532 -53.309 1.00 47.26  ? 606 HOH   B O   1 
HETATM 6559 O O   . HOH   F 3 .   ? -3.444  -37.649 -68.338 1.00 45.67  ? 607 HOH   B O   1 
HETATM 6560 O O   . HOH   F 3 .   ? -15.461 -22.881 -79.809 1.00 46.08  ? 608 HOH   B O   1 
HETATM 6561 O O   . HOH   F 3 .   ? -23.035 -41.893 -66.677 1.00 40.85  ? 609 HOH   B O   1 
HETATM 6562 O O   . HOH   F 3 .   ? -6.545  -6.060  -46.042 1.00 47.27  ? 610 HOH   B O   1 
HETATM 6563 O O   . HOH   F 3 .   ? -4.455  -32.699 -72.881 1.00 40.36  ? 611 HOH   B O   1 
HETATM 6564 O O   . HOH   F 3 .   ? -16.668 -12.115 -46.032 1.00 44.21  ? 612 HOH   B O   1 
HETATM 6565 O O   . HOH   F 3 .   ? -15.700 -43.519 -47.236 1.00 47.13  ? 613 HOH   B O   1 
HETATM 6566 O O   . HOH   F 3 .   ? -13.900 -13.080 -40.853 1.00 43.34  ? 614 HOH   B O   1 
HETATM 6567 O O   . HOH   F 3 .   ? 1.173   -9.815  -44.613 1.00 50.10  ? 615 HOH   B O   1 
HETATM 6568 O O   . HOH   F 3 .   ? -15.616 -15.415 -47.422 1.00 40.61  ? 616 HOH   B O   1 
HETATM 6569 O O   . HOH   F 3 .   ? -6.883  0.776   -60.482 1.00 63.37  ? 617 HOH   B O   1 
HETATM 6570 O O   . HOH   F 3 .   ? -10.283 -23.829 -48.588 1.00 38.79  ? 618 HOH   B O   1 
HETATM 6571 O O   . HOH   F 3 .   ? -11.674 -6.861  -42.925 1.00 51.93  ? 619 HOH   B O   1 
HETATM 6572 O O   . HOH   F 3 .   ? -25.952 -16.769 -70.183 1.00 36.70  ? 620 HOH   B O   1 
HETATM 6573 O O   . HOH   F 3 .   ? 2.790   -24.282 -35.103 1.00 50.32  ? 621 HOH   B O   1 
HETATM 6574 O O   . HOH   F 3 .   ? -26.071 -31.477 -49.355 1.00 43.28  ? 622 HOH   B O   1 
HETATM 6575 O O   . HOH   F 3 .   ? -19.804 -40.508 -66.864 1.00 39.57  ? 623 HOH   B O   1 
HETATM 6576 O O   . HOH   F 3 .   ? -22.098 -14.804 -69.486 1.00 45.17  ? 624 HOH   B O   1 
HETATM 6577 O O   . HOH   F 3 .   ? -17.894 -28.813 -50.965 1.00 39.89  ? 625 HOH   B O   1 
HETATM 6578 O O   . HOH   F 3 .   ? 0.946   -47.169 -41.809 1.00 47.91  ? 626 HOH   B O   1 
HETATM 6579 O O   . HOH   F 3 .   ? -12.977 -29.073 -64.691 1.00 34.64  ? 627 HOH   B O   1 
HETATM 6580 O O   . HOH   F 3 .   ? -28.982 -32.330 -52.433 1.00 45.80  ? 628 HOH   B O   1 
HETATM 6581 O O   . HOH   F 3 .   ? 1.330   -27.764 -80.920 1.00 45.86  ? 629 HOH   B O   1 
HETATM 6582 O O   . HOH   F 3 .   ? 6.657   -45.547 -47.887 1.00 60.78  ? 630 HOH   B O   1 
HETATM 6583 O O   . HOH   F 3 .   ? -0.294  -11.538 -46.750 1.00 44.71  ? 631 HOH   B O   1 
HETATM 6584 O O   . HOH   F 3 .   ? -2.299  -15.503 -41.277 1.00 43.49  ? 632 HOH   B O   1 
HETATM 6585 O O   . HOH   F 3 .   ? -9.514  -13.055 -46.650 1.00 38.72  ? 633 HOH   B O   1 
HETATM 6586 O O   . HOH   F 3 .   ? -36.695 -28.337 -71.307 1.00 53.32  ? 634 HOH   B O   1 
HETATM 6587 O O   . HOH   F 3 .   ? -34.307 -34.919 -60.351 1.00 49.03  ? 635 HOH   B O   1 
HETATM 6588 O O   . HOH   F 3 .   ? -11.982 -47.090 -57.390 1.00 48.44  ? 636 HOH   B O   1 
HETATM 6589 O O   . HOH   F 3 .   ? -12.588 -26.999 -40.026 1.00 50.22  ? 637 HOH   B O   1 
HETATM 6590 O O   . HOH   F 3 .   ? -25.368 -8.362  -59.383 1.00 36.09  ? 638 HOH   B O   1 
HETATM 6591 O O   . HOH   F 3 .   ? -29.362 -25.982 -60.885 1.00 38.41  ? 639 HOH   B O   1 
HETATM 6592 O O   . HOH   F 3 .   ? -23.443 -13.551 -72.049 1.00 45.55  ? 640 HOH   B O   1 
HETATM 6593 O O   . HOH   F 3 .   ? -31.647 -32.608 -67.304 1.00 49.62  ? 641 HOH   B O   1 
HETATM 6594 O O   . HOH   F 3 .   ? 9.767   -5.473  -47.050 1.00 54.23  ? 642 HOH   B O   1 
HETATM 6595 O O   . HOH   F 3 .   ? -6.197  -31.091 -71.480 1.00 37.67  ? 643 HOH   B O   1 
HETATM 6596 O O   . HOH   F 3 .   ? 2.768   -21.848 -54.495 1.00 40.64  ? 644 HOH   B O   1 
HETATM 6597 O O   . HOH   F 3 .   ? -20.330 -16.602 -69.729 1.00 39.42  ? 645 HOH   B O   1 
HETATM 6598 O O   . HOH   F 3 .   ? -5.830  -38.615 -67.432 1.00 39.80  ? 646 HOH   B O   1 
HETATM 6599 O O   . HOH   F 3 .   ? 17.997  -20.962 -74.627 1.00 59.27  ? 647 HOH   B O   1 
HETATM 6600 O O   . HOH   F 3 .   ? -4.093  -36.949 -76.027 1.00 41.00  ? 648 HOH   B O   1 
HETATM 6601 O O   . HOH   F 3 .   ? -29.300 -25.288 -51.539 1.00 41.71  ? 649 HOH   B O   1 
HETATM 6602 O O   . HOH   F 3 .   ? -23.825 -24.549 -44.976 1.00 41.58  ? 650 HOH   B O   1 
HETATM 6603 O O   . HOH   F 3 .   ? -22.045 -18.419 -79.654 1.00 49.40  ? 651 HOH   B O   1 
HETATM 6604 O O   . HOH   F 3 .   ? -25.519 -19.297 -49.926 1.00 37.57  ? 652 HOH   B O   1 
HETATM 6605 O O   . HOH   F 3 .   ? -2.692  -29.052 -45.494 1.00 40.83  ? 653 HOH   B O   1 
HETATM 6606 O O   . HOH   F 3 .   ? -29.577 -31.584 -58.022 1.00 45.58  ? 654 HOH   B O   1 
HETATM 6607 O O   . HOH   F 3 .   ? -19.498 -17.710 -45.282 1.00 40.79  ? 655 HOH   B O   1 
HETATM 6608 O O   . HOH   F 3 .   ? -5.199  1.482   -49.319 1.00 53.12  ? 656 HOH   B O   1 
HETATM 6609 O O   . HOH   F 3 .   ? -3.256  -25.815 -49.133 1.00 35.27  ? 657 HOH   B O   1 
HETATM 6610 O O   . HOH   F 3 .   ? -31.463 -3.684  -50.695 1.00 59.06  ? 658 HOH   B O   1 
HETATM 6611 O O   . HOH   F 3 .   ? 4.794   -24.790 -73.796 1.00 49.73  ? 659 HOH   B O   1 
HETATM 6612 O O   . HOH   F 3 .   ? -0.782  -47.232 -43.483 1.00 48.48  ? 660 HOH   B O   1 
HETATM 6613 O O   . HOH   F 3 .   ? 6.741   -28.334 -73.468 1.00 57.49  ? 661 HOH   B O   1 
HETATM 6614 O O   . HOH   F 3 .   ? -25.917 -17.363 -76.855 1.00 44.62  ? 662 HOH   B O   1 
HETATM 6615 O O   . HOH   F 3 .   ? 4.186   -40.171 -62.267 1.00 53.75  ? 663 HOH   B O   1 
HETATM 6616 O O   . HOH   F 3 .   ? -11.861 -9.245  -52.299 1.00 45.77  ? 664 HOH   B O   1 
HETATM 6617 O O   . HOH   F 3 .   ? -2.458  -9.490  -46.472 1.00 44.66  ? 665 HOH   B O   1 
HETATM 6618 O O   . HOH   F 3 .   ? -3.328  1.004   -57.516 1.00 53.57  ? 666 HOH   B O   1 
HETATM 6619 O O   . HOH   F 3 .   ? 2.450   -44.236 -73.220 1.00 59.12  ? 667 HOH   B O   1 
HETATM 6620 O O   . HOH   F 3 .   ? 0.148   -33.527 -79.229 1.00 42.49  ? 668 HOH   B O   1 
HETATM 6621 O O   . HOH   F 3 .   ? 0.719   -50.335 -46.642 1.00 58.39  ? 669 HOH   B O   1 
HETATM 6622 O O   . HOH   F 3 .   ? -10.333 -45.349 -65.870 1.00 37.44  ? 670 HOH   B O   1 
HETATM 6623 O O   . HOH   F 3 .   ? 4.956   -29.414 -75.607 1.00 52.03  ? 671 HOH   B O   1 
HETATM 6624 O O   . HOH   F 3 .   ? -30.999 -32.915 -70.103 1.00 49.10  ? 672 HOH   B O   1 
HETATM 6625 O O   . HOH   F 3 .   ? -15.773 -13.532 -72.931 1.00 52.24  ? 673 HOH   B O   1 
HETATM 6626 O O   . HOH   F 3 .   ? -19.704 -36.242 -73.332 1.00 58.11  ? 674 HOH   B O   1 
HETATM 6627 O O   . HOH   F 3 .   ? 1.628   -11.612 -41.211 1.00 46.32  ? 675 HOH   B O   1 
HETATM 6628 O O   . HOH   F 3 .   ? -1.895  -39.305 -69.281 1.00 55.11  ? 676 HOH   B O   1 
HETATM 6629 O O   . HOH   F 3 .   ? -12.255 -7.302  -55.204 1.00 58.01  ? 677 HOH   B O   1 
HETATM 6630 O O   . HOH   F 3 .   ? -24.457 -30.123 -47.658 1.00 53.18  ? 678 HOH   B O   1 
HETATM 6631 O O   . HOH   F 3 .   ? -16.380 -14.904 -75.189 1.00 47.46  ? 679 HOH   B O   1 
HETATM 6632 O O   . HOH   F 3 .   ? 0.788   -14.550 -41.371 1.00 47.91  ? 680 HOH   B O   1 
HETATM 6633 O O   . HOH   F 3 .   ? -30.966 -24.981 -58.448 1.00 53.27  ? 681 HOH   B O   1 
HETATM 6634 O O   . HOH   F 3 .   ? -6.166  -31.398 -40.863 1.00 46.39  ? 682 HOH   B O   1 
HETATM 6635 O O   . HOH   F 3 .   ? -15.206 -6.951  -54.120 1.00 55.37  ? 683 HOH   B O   1 
HETATM 6636 O O   . HOH   F 3 .   ? 0.703   -39.622 -62.019 1.00 53.99  ? 684 HOH   B O   1 
HETATM 6637 O O   . HOH   F 3 .   ? -24.683 -18.013 -78.685 1.00 48.51  ? 685 HOH   B O   1 
# 
