data_9H8Z
# 
_entry.id   9H8Z 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9H8Z         pdb_00009h8z 10.2210/pdb9h8z/pdb 
WWPDB D_1292142859 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-19 ? 
2 'Structure model' 1 1 2025-04-02 ? 
# 
_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               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H8Z 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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                 2 
_pdbx_contact_author.email              gwen.tjallinks@iusspavia.it 
_pdbx_contact_author.name_first         Gwen 
_pdbx_contact_author.name_last          Tjallinks 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5174-913X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tjallinks, G.' 1 0000-0002-5174-913X 
'Mattevi, A.'   2 0000-0002-9523-7128 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Chem.Biol.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1554-8937 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            20 
_citation.language                  ? 
_citation.page_first                646 
_citation.page_last                 655 
_citation.title                     
;Structural and Mechanistic Characterization of the Flavin-Dependent Monooxygenase and Oxidase Involved in Sorbicillinoid Biosynthesis.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acschembio.4c00783 
_citation.pdbx_database_id_PubMed   40052414 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Tjallinks, G.'   1 ? 
primary 'Angeleri, N.'    2 ? 
primary 'Nguyen, Q.T.'    3 ? 
primary 'Mannucci, B.'    4 ? 
primary 'Arentshorst, M.' 5 ? 
primary 'Visser, J.'      6 ? 
primary 'Ram, A.F.J.'     7 ? 
primary 'Fraaije, M.W.'   8 ? 
primary 'Mattevi, A.'     9 ? 
# 
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 'FAD-dependent monooxygenase sorC'                                    48213.410 1   1.-.-.- ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'                                         785.550   1   ?       ? ? ? 
3 non-polymer syn '(2~{Z})-1-[3,5-dimethyl-2,4-bis(oxidanyl)phenyl]hexa-2,4-dien-1-one' 232.275   1   ?       ? ? ? 
4 water       nat water                                                                 18.015    259 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Sorbicillinoid biosynthetic cluster protein C' 
# 
_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       
;MTRSANSPFEVAIVGGGITGLALAVGLLKRNVSFTIYERAENFGELGVGITFTPNAQRAMEALDPCVLQSFTNVASAPSG
GTINFVDGVREQGSEDPRTSTAALLFQLHVKGGYKACRRCDFVDQIVQHIPKDCVQYRKWLDSIETDHESGRAVLKFRDG
EIAHADVVIGCDGIRSQVRASMFGTDELCPRAQYSHQLGYRGMVPLAQATAVLGPEKTSSAVLHTGPGAFVLTIPLAEVH
AMHIEAFIMDKEEWPEVQTSSDSKRYVLPATRNEATKAFAEFGPTVRSAVSMFPEKLEKWAVFDMLEAPVPTFAKGRVCL
AGDAAHASTPNQGGGAGFGIEDALVLAEVLAVLAEAPNVSGIVASEALAVYSEVRYERSQWLVRSSRRTGELCTWKDRDW
GLAAEELSRDIISRSHQLWDHDTAGMVSDALAILGERVRGADTAF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTRSANSPFEVAIVGGGITGLALAVGLLKRNVSFTIYERAENFGELGVGITFTPNAQRAMEALDPCVLQSFTNVASAPSG
GTINFVDGVREQGSEDPRTSTAALLFQLHVKGGYKACRRCDFVDQIVQHIPKDCVQYRKWLDSIETDHESGRAVLKFRDG
EIAHADVVIGCDGIRSQVRASMFGTDELCPRAQYSHQLGYRGMVPLAQATAVLGPEKTSSAVLHTGPGAFVLTIPLAEVH
AMHIEAFIMDKEEWPEVQTSSDSKRYVLPATRNEATKAFAEFGPTVRSAVSMFPEKLEKWAVFDMLEAPVPTFAKGRVCL
AGDAAHASTPNQGGGAGFGIEDALVLAEVLAVLAEAPNVSGIVASEALAVYSEVRYERSQWLVRSSRRTGELCTWKDRDW
GLAAEELSRDIISRSHQLWDHDTAGMVSDALAILGERVRGADTAF
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE'                                         FAD   
3 '(2~{Z})-1-[3,5-dimethyl-2,4-bis(oxidanyl)phenyl]hexa-2,4-dien-1-one' A1ITD 
4 water                                                                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   ARG n 
1 4   SER n 
1 5   ALA n 
1 6   ASN n 
1 7   SER n 
1 8   PRO n 
1 9   PHE n 
1 10  GLU n 
1 11  VAL n 
1 12  ALA n 
1 13  ILE n 
1 14  VAL n 
1 15  GLY n 
1 16  GLY n 
1 17  GLY n 
1 18  ILE n 
1 19  THR n 
1 20  GLY n 
1 21  LEU n 
1 22  ALA n 
1 23  LEU n 
1 24  ALA n 
1 25  VAL n 
1 26  GLY n 
1 27  LEU n 
1 28  LEU n 
1 29  LYS n 
1 30  ARG n 
1 31  ASN n 
1 32  VAL n 
1 33  SER n 
1 34  PHE n 
1 35  THR n 
1 36  ILE n 
1 37  TYR n 
1 38  GLU n 
1 39  ARG n 
1 40  ALA n 
1 41  GLU n 
1 42  ASN n 
1 43  PHE n 
1 44  GLY n 
1 45  GLU n 
1 46  LEU n 
1 47  GLY n 
1 48  VAL n 
1 49  GLY n 
1 50  ILE n 
1 51  THR n 
1 52  PHE n 
1 53  THR n 
1 54  PRO n 
1 55  ASN n 
1 56  ALA n 
1 57  GLN n 
1 58  ARG n 
1 59  ALA n 
1 60  MET n 
1 61  GLU n 
1 62  ALA n 
1 63  LEU n 
1 64  ASP n 
1 65  PRO n 
1 66  CYS n 
1 67  VAL n 
1 68  LEU n 
1 69  GLN n 
1 70  SER n 
1 71  PHE n 
1 72  THR n 
1 73  ASN n 
1 74  VAL n 
1 75  ALA n 
1 76  SER n 
1 77  ALA n 
1 78  PRO n 
1 79  SER n 
1 80  GLY n 
1 81  GLY n 
1 82  THR n 
1 83  ILE n 
1 84  ASN n 
1 85  PHE n 
1 86  VAL n 
1 87  ASP n 
1 88  GLY n 
1 89  VAL n 
1 90  ARG n 
1 91  GLU n 
1 92  GLN n 
1 93  GLY n 
1 94  SER n 
1 95  GLU n 
1 96  ASP n 
1 97  PRO n 
1 98  ARG n 
1 99  THR n 
1 100 SER n 
1 101 THR n 
1 102 ALA n 
1 103 ALA n 
1 104 LEU n 
1 105 LEU n 
1 106 PHE n 
1 107 GLN n 
1 108 LEU n 
1 109 HIS n 
1 110 VAL n 
1 111 LYS n 
1 112 GLY n 
1 113 GLY n 
1 114 TYR n 
1 115 LYS n 
1 116 ALA n 
1 117 CYS n 
1 118 ARG n 
1 119 ARG n 
1 120 CYS n 
1 121 ASP n 
1 122 PHE n 
1 123 VAL n 
1 124 ASP n 
1 125 GLN n 
1 126 ILE n 
1 127 VAL n 
1 128 GLN n 
1 129 HIS n 
1 130 ILE n 
1 131 PRO n 
1 132 LYS n 
1 133 ASP n 
1 134 CYS n 
1 135 VAL n 
1 136 GLN n 
1 137 TYR n 
1 138 ARG n 
1 139 LYS n 
1 140 TRP n 
1 141 LEU n 
1 142 ASP n 
1 143 SER n 
1 144 ILE n 
1 145 GLU n 
1 146 THR n 
1 147 ASP n 
1 148 HIS n 
1 149 GLU n 
1 150 SER n 
1 151 GLY n 
1 152 ARG n 
1 153 ALA n 
1 154 VAL n 
1 155 LEU n 
1 156 LYS n 
1 157 PHE n 
1 158 ARG n 
1 159 ASP n 
1 160 GLY n 
1 161 GLU n 
1 162 ILE n 
1 163 ALA n 
1 164 HIS n 
1 165 ALA n 
1 166 ASP n 
1 167 VAL n 
1 168 VAL n 
1 169 ILE n 
1 170 GLY n 
1 171 CYS n 
1 172 ASP n 
1 173 GLY n 
1 174 ILE n 
1 175 ARG n 
1 176 SER n 
1 177 GLN n 
1 178 VAL n 
1 179 ARG n 
1 180 ALA n 
1 181 SER n 
1 182 MET n 
1 183 PHE n 
1 184 GLY n 
1 185 THR n 
1 186 ASP n 
1 187 GLU n 
1 188 LEU n 
1 189 CYS n 
1 190 PRO n 
1 191 ARG n 
1 192 ALA n 
1 193 GLN n 
1 194 TYR n 
1 195 SER n 
1 196 HIS n 
1 197 GLN n 
1 198 LEU n 
1 199 GLY n 
1 200 TYR n 
1 201 ARG n 
1 202 GLY n 
1 203 MET n 
1 204 VAL n 
1 205 PRO n 
1 206 LEU n 
1 207 ALA n 
1 208 GLN n 
1 209 ALA n 
1 210 THR n 
1 211 ALA n 
1 212 VAL n 
1 213 LEU n 
1 214 GLY n 
1 215 PRO n 
1 216 GLU n 
1 217 LYS n 
1 218 THR n 
1 219 SER n 
1 220 SER n 
1 221 ALA n 
1 222 VAL n 
1 223 LEU n 
1 224 HIS n 
1 225 THR n 
1 226 GLY n 
1 227 PRO n 
1 228 GLY n 
1 229 ALA n 
1 230 PHE n 
1 231 VAL n 
1 232 LEU n 
1 233 THR n 
1 234 ILE n 
1 235 PRO n 
1 236 LEU n 
1 237 ALA n 
1 238 GLU n 
1 239 VAL n 
1 240 HIS n 
1 241 ALA n 
1 242 MET n 
1 243 HIS n 
1 244 ILE n 
1 245 GLU n 
1 246 ALA n 
1 247 PHE n 
1 248 ILE n 
1 249 MET n 
1 250 ASP n 
1 251 LYS n 
1 252 GLU n 
1 253 GLU n 
1 254 TRP n 
1 255 PRO n 
1 256 GLU n 
1 257 VAL n 
1 258 GLN n 
1 259 THR n 
1 260 SER n 
1 261 SER n 
1 262 ASP n 
1 263 SER n 
1 264 LYS n 
1 265 ARG n 
1 266 TYR n 
1 267 VAL n 
1 268 LEU n 
1 269 PRO n 
1 270 ALA n 
1 271 THR n 
1 272 ARG n 
1 273 ASN n 
1 274 GLU n 
1 275 ALA n 
1 276 THR n 
1 277 LYS n 
1 278 ALA n 
1 279 PHE n 
1 280 ALA n 
1 281 GLU n 
1 282 PHE n 
1 283 GLY n 
1 284 PRO n 
1 285 THR n 
1 286 VAL n 
1 287 ARG n 
1 288 SER n 
1 289 ALA n 
1 290 VAL n 
1 291 SER n 
1 292 MET n 
1 293 PHE n 
1 294 PRO n 
1 295 GLU n 
1 296 LYS n 
1 297 LEU n 
1 298 GLU n 
1 299 LYS n 
1 300 TRP n 
1 301 ALA n 
1 302 VAL n 
1 303 PHE n 
1 304 ASP n 
1 305 MET n 
1 306 LEU n 
1 307 GLU n 
1 308 ALA n 
1 309 PRO n 
1 310 VAL n 
1 311 PRO n 
1 312 THR n 
1 313 PHE n 
1 314 ALA n 
1 315 LYS n 
1 316 GLY n 
1 317 ARG n 
1 318 VAL n 
1 319 CYS n 
1 320 LEU n 
1 321 ALA n 
1 322 GLY n 
1 323 ASP n 
1 324 ALA n 
1 325 ALA n 
1 326 HIS n 
1 327 ALA n 
1 328 SER n 
1 329 THR n 
1 330 PRO n 
1 331 ASN n 
1 332 GLN n 
1 333 GLY n 
1 334 GLY n 
1 335 GLY n 
1 336 ALA n 
1 337 GLY n 
1 338 PHE n 
1 339 GLY n 
1 340 ILE n 
1 341 GLU n 
1 342 ASP n 
1 343 ALA n 
1 344 LEU n 
1 345 VAL n 
1 346 LEU n 
1 347 ALA n 
1 348 GLU n 
1 349 VAL n 
1 350 LEU n 
1 351 ALA n 
1 352 VAL n 
1 353 LEU n 
1 354 ALA n 
1 355 GLU n 
1 356 ALA n 
1 357 PRO n 
1 358 ASN n 
1 359 VAL n 
1 360 SER n 
1 361 GLY n 
1 362 ILE n 
1 363 VAL n 
1 364 ALA n 
1 365 SER n 
1 366 GLU n 
1 367 ALA n 
1 368 LEU n 
1 369 ALA n 
1 370 VAL n 
1 371 TYR n 
1 372 SER n 
1 373 GLU n 
1 374 VAL n 
1 375 ARG n 
1 376 TYR n 
1 377 GLU n 
1 378 ARG n 
1 379 SER n 
1 380 GLN n 
1 381 TRP n 
1 382 LEU n 
1 383 VAL n 
1 384 ARG n 
1 385 SER n 
1 386 SER n 
1 387 ARG n 
1 388 ARG n 
1 389 THR n 
1 390 GLY n 
1 391 GLU n 
1 392 LEU n 
1 393 CYS n 
1 394 THR n 
1 395 TRP n 
1 396 LYS n 
1 397 ASP n 
1 398 ARG n 
1 399 ASP n 
1 400 TRP n 
1 401 GLY n 
1 402 LEU n 
1 403 ALA n 
1 404 ALA n 
1 405 GLU n 
1 406 GLU n 
1 407 LEU n 
1 408 SER n 
1 409 ARG n 
1 410 ASP n 
1 411 ILE n 
1 412 ILE n 
1 413 SER n 
1 414 ARG n 
1 415 SER n 
1 416 HIS n 
1 417 GLN n 
1 418 LEU n 
1 419 TRP n 
1 420 ASP n 
1 421 HIS n 
1 422 ASP n 
1 423 THR n 
1 424 ALA n 
1 425 GLY n 
1 426 MET n 
1 427 VAL n 
1 428 SER n 
1 429 ASP n 
1 430 ALA n 
1 431 LEU n 
1 432 ALA n 
1 433 ILE n 
1 434 LEU n 
1 435 GLY n 
1 436 GLU n 
1 437 ARG n 
1 438 VAL n 
1 439 ARG n 
1 440 GLY n 
1 441 ALA n 
1 442 ASP n 
1 443 THR n 
1 444 ALA n 
1 445 PHE 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                   445 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'sorC, Pc21g05060' 
_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      'Penicillium rubens Wisconsin 54-1255' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     500485 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ITD non-polymer         . '(2~{Z})-1-[3,5-dimethyl-2,4-bis(oxidanyl)phenyl]hexa-2,4-dien-1-one' ? 'C14 H16 O3'        232.275 
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 
FAD   non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE'                                         ? 'C27 H33 N9 O15 P2' 785.550 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   ARG 3   3   ?   ?   ?   A . n 
A 1 4   SER 4   4   ?   ?   ?   A . n 
A 1 5   ALA 5   5   ?   ?   ?   A . n 
A 1 6   ASN 6   6   ?   ?   ?   A . n 
A 1 7   SER 7   7   ?   ?   ?   A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  GLU 10  10  10  GLU GLU A . n 
A 1 11  VAL 11  11  11  VAL VAL A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  PHE 34  34  34  PHE PHE A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  GLU 38  38  38  GLU GLU A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  GLU 41  41  41  GLU GLU A . n 
A 1 42  ASN 42  42  42  ASN ASN A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  THR 51  51  51  THR THR A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  THR 53  53  53  THR THR A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  MET 60  60  60  MET MET A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  ASP 64  64  64  ASP ASP A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  CYS 66  66  66  CYS CYS A . n 
A 1 67  VAL 67  67  67  VAL VAL A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  PHE 71  71  71  PHE PHE A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  ASN 73  73  73  ASN ASN A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  THR 82  82  82  THR THR A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  PHE 85  85  85  PHE PHE A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  ARG 98  98  98  ARG ARG A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 THR 101 101 101 THR THR A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 PHE 106 106 106 PHE PHE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 HIS 109 109 109 HIS HIS A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 CYS 120 120 120 CYS CYS A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 GLN 125 125 125 GLN GLN A . n 
A 1 126 ILE 126 126 126 ILE ILE A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 HIS 129 129 129 HIS HIS A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 CYS 134 134 134 CYS CYS A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 ARG 138 138 138 ARG ARG A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 TRP 140 140 140 TRP TRP A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASP 142 142 142 ASP ASP A . n 
A 1 143 SER 143 143 143 SER SER A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 HIS 148 148 148 HIS HIS A . n 
A 1 149 GLU 149 149 149 GLU GLU A . n 
A 1 150 SER 150 150 150 SER SER 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 ALA 153 153 153 ALA ALA A . n 
A 1 154 VAL 154 154 154 VAL VAL A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 ARG 158 158 158 ARG ARG A . n 
A 1 159 ASP 159 159 159 ASP ASP A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 ILE 162 162 162 ILE ILE A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 ASP 166 166 166 ASP ASP A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 CYS 171 171 171 CYS CYS A . n 
A 1 172 ASP 172 172 172 ASP ASP A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 ILE 174 174 174 ILE ILE A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 GLN 177 177 177 GLN GLN A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 MET 182 182 182 MET MET A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 THR 185 185 185 THR THR A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 CYS 189 189 189 CYS CYS A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 GLN 193 193 193 GLN GLN A . n 
A 1 194 TYR 194 194 194 TYR TYR A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 HIS 196 196 196 HIS HIS A . n 
A 1 197 GLN 197 197 197 GLN GLN A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 TYR 200 200 200 TYR TYR A . n 
A 1 201 ARG 201 201 201 ARG ARG A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 MET 203 203 203 MET MET A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 GLN 208 208 208 GLN GLN A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 GLU 216 216 216 GLU GLU A . n 
A 1 217 LYS 217 217 217 LYS LYS A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 HIS 224 224 224 HIS HIS A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 PRO 227 227 227 PRO PRO A . n 
A 1 228 GLY 228 228 228 GLY GLY A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 THR 233 233 233 THR THR A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 VAL 239 239 239 VAL VAL A . n 
A 1 240 HIS 240 240 240 HIS HIS A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 HIS 243 243 243 HIS HIS A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 GLU 245 245 245 GLU GLU A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 PHE 247 247 247 PHE PHE A . n 
A 1 248 ILE 248 248 248 ILE ILE A . n 
A 1 249 MET 249 249 249 MET MET A . n 
A 1 250 ASP 250 250 250 ASP ASP A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 GLU 252 252 252 GLU GLU A . n 
A 1 253 GLU 253 253 253 GLU GLU A . n 
A 1 254 TRP 254 254 254 TRP TRP A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 GLN 258 258 258 GLN GLN A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 ASP 262 262 262 ASP ASP A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 LYS 264 264 264 LYS LYS A . n 
A 1 265 ARG 265 265 265 ARG ARG A . n 
A 1 266 TYR 266 266 266 TYR TYR A . n 
A 1 267 VAL 267 267 267 VAL VAL A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 PRO 269 269 269 PRO PRO A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 ARG 272 272 272 ARG ARG A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 GLU 274 274 274 GLU GLU A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 THR 276 276 276 THR THR A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 GLU 281 281 281 GLU GLU A . n 
A 1 282 PHE 282 282 282 PHE PHE A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 THR 285 285 285 THR THR A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 ARG 287 287 287 ARG ARG A . n 
A 1 288 SER 288 288 288 SER SER A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 VAL 290 290 290 VAL VAL A . n 
A 1 291 SER 291 291 291 SER SER A . n 
A 1 292 MET 292 292 292 MET MET A . n 
A 1 293 PHE 293 293 293 PHE PHE A . n 
A 1 294 PRO 294 294 294 PRO PRO A . n 
A 1 295 GLU 295 295 295 GLU GLU A . n 
A 1 296 LYS 296 296 296 LYS LYS A . n 
A 1 297 LEU 297 297 297 LEU LEU A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 LYS 299 299 299 LYS LYS A . n 
A 1 300 TRP 300 300 300 TRP TRP A . n 
A 1 301 ALA 301 301 301 ALA ALA A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 PHE 303 303 303 PHE PHE A . n 
A 1 304 ASP 304 304 304 ASP ASP A . n 
A 1 305 MET 305 305 305 MET MET A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 PRO 309 309 309 PRO PRO A . n 
A 1 310 VAL 310 310 310 VAL VAL A . n 
A 1 311 PRO 311 311 311 PRO PRO A . n 
A 1 312 THR 312 312 312 THR THR A . n 
A 1 313 PHE 313 313 313 PHE PHE A . n 
A 1 314 ALA 314 314 314 ALA ALA A . n 
A 1 315 LYS 315 315 315 LYS LYS A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 ARG 317 317 317 ARG ARG A . n 
A 1 318 VAL 318 318 318 VAL VAL A . n 
A 1 319 CYS 319 319 319 CYS CYS A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 GLY 322 322 322 GLY GLY A . n 
A 1 323 ASP 323 323 323 ASP ASP A . n 
A 1 324 ALA 324 324 324 ALA ALA A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 HIS 326 326 326 HIS HIS A . n 
A 1 327 ALA 327 327 327 ALA ALA A . n 
A 1 328 SER 328 328 328 SER SER A . n 
A 1 329 THR 329 329 329 THR THR A . n 
A 1 330 PRO 330 330 330 PRO PRO A . n 
A 1 331 ASN 331 331 331 ASN ASN A . n 
A 1 332 GLN 332 332 332 GLN GLN A . n 
A 1 333 GLY 333 333 333 GLY GLY A . n 
A 1 334 GLY 334 334 334 GLY GLY A . n 
A 1 335 GLY 335 335 335 GLY GLY A . n 
A 1 336 ALA 336 336 336 ALA ALA A . n 
A 1 337 GLY 337 337 337 GLY GLY A . n 
A 1 338 PHE 338 338 338 PHE PHE A . n 
A 1 339 GLY 339 339 339 GLY GLY A . n 
A 1 340 ILE 340 340 340 ILE ILE A . n 
A 1 341 GLU 341 341 341 GLU GLU A . n 
A 1 342 ASP 342 342 342 ASP ASP A . n 
A 1 343 ALA 343 343 343 ALA ALA A . n 
A 1 344 LEU 344 344 344 LEU LEU A . n 
A 1 345 VAL 345 345 345 VAL VAL A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 GLU 348 348 348 GLU GLU A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 ALA 351 351 351 ALA ALA A . n 
A 1 352 VAL 352 352 352 VAL VAL A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 ALA 354 354 354 ALA ALA A . n 
A 1 355 GLU 355 355 355 GLU GLU A . n 
A 1 356 ALA 356 356 356 ALA ALA A . n 
A 1 357 PRO 357 357 357 PRO PRO A . n 
A 1 358 ASN 358 358 358 ASN ASN A . n 
A 1 359 VAL 359 359 359 VAL VAL A . n 
A 1 360 SER 360 360 360 SER SER A . n 
A 1 361 GLY 361 361 361 GLY GLY A . n 
A 1 362 ILE 362 362 362 ILE ILE A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 ALA 364 364 364 ALA ALA A . n 
A 1 365 SER 365 365 365 SER SER A . n 
A 1 366 GLU 366 366 366 GLU GLU A . n 
A 1 367 ALA 367 367 367 ALA ALA A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 TYR 371 371 371 TYR TYR A . n 
A 1 372 SER 372 372 372 SER SER A . n 
A 1 373 GLU 373 373 373 GLU GLU A . n 
A 1 374 VAL 374 374 374 VAL VAL A . n 
A 1 375 ARG 375 375 375 ARG ARG A . n 
A 1 376 TYR 376 376 376 TYR TYR A . n 
A 1 377 GLU 377 377 377 GLU GLU A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 SER 379 379 379 SER SER A . n 
A 1 380 GLN 380 380 380 GLN GLN A . n 
A 1 381 TRP 381 381 381 TRP TRP A . n 
A 1 382 LEU 382 382 382 LEU LEU A . n 
A 1 383 VAL 383 383 383 VAL VAL A . n 
A 1 384 ARG 384 384 384 ARG ARG A . n 
A 1 385 SER 385 385 385 SER SER A . n 
A 1 386 SER 386 386 386 SER SER A . n 
A 1 387 ARG 387 387 387 ARG ARG A . n 
A 1 388 ARG 388 388 388 ARG ARG A . n 
A 1 389 THR 389 389 389 THR THR A . n 
A 1 390 GLY 390 390 390 GLY GLY A . n 
A 1 391 GLU 391 391 391 GLU GLU A . n 
A 1 392 LEU 392 392 392 LEU LEU A . n 
A 1 393 CYS 393 393 393 CYS CYS A . n 
A 1 394 THR 394 394 394 THR THR A . n 
A 1 395 TRP 395 395 395 TRP TRP A . n 
A 1 396 LYS 396 396 396 LYS LYS A . n 
A 1 397 ASP 397 397 397 ASP ASP A . n 
A 1 398 ARG 398 398 398 ARG ARG A . n 
A 1 399 ASP 399 399 399 ASP ASP A . n 
A 1 400 TRP 400 400 400 TRP TRP A . n 
A 1 401 GLY 401 401 401 GLY GLY A . n 
A 1 402 LEU 402 402 402 LEU LEU A . n 
A 1 403 ALA 403 403 403 ALA ALA A . n 
A 1 404 ALA 404 404 404 ALA ALA A . n 
A 1 405 GLU 405 405 405 GLU GLU A . n 
A 1 406 GLU 406 406 406 GLU GLU A . n 
A 1 407 LEU 407 407 407 LEU LEU A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 ARG 409 409 409 ARG ARG A . n 
A 1 410 ASP 410 410 410 ASP ASP A . n 
A 1 411 ILE 411 411 411 ILE ILE A . n 
A 1 412 ILE 412 412 412 ILE ILE A . n 
A 1 413 SER 413 413 413 SER SER A . n 
A 1 414 ARG 414 414 414 ARG ARG A . n 
A 1 415 SER 415 415 415 SER SER A . n 
A 1 416 HIS 416 416 416 HIS HIS A . n 
A 1 417 GLN 417 417 417 GLN GLN A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 TRP 419 419 419 TRP TRP A . n 
A 1 420 ASP 420 420 420 ASP ASP A . n 
A 1 421 HIS 421 421 421 HIS HIS A . n 
A 1 422 ASP 422 422 422 ASP ASP A . n 
A 1 423 THR 423 423 423 THR THR A . n 
A 1 424 ALA 424 424 424 ALA ALA A . n 
A 1 425 GLY 425 425 425 GLY GLY A . n 
A 1 426 MET 426 426 426 MET MET A . n 
A 1 427 VAL 427 427 427 VAL VAL A . n 
A 1 428 SER 428 428 428 SER SER A . n 
A 1 429 ASP 429 429 429 ASP ASP A . n 
A 1 430 ALA 430 430 430 ALA ALA A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 ILE 433 433 433 ILE ILE A . n 
A 1 434 LEU 434 434 434 LEU LEU A . n 
A 1 435 GLY 435 435 435 GLY GLY A . n 
A 1 436 GLU 436 436 436 GLU GLU A . n 
A 1 437 ARG 437 437 437 ARG ARG A . n 
A 1 438 VAL 438 438 438 VAL VAL A . n 
A 1 439 ARG 439 439 ?   ?   ?   A . n 
A 1 440 GLY 440 440 ?   ?   ?   A . n 
A 1 441 ALA 441 441 ?   ?   ?   A . n 
A 1 442 ASP 442 442 ?   ?   ?   A . n 
A 1 443 THR 443 443 ?   ?   ?   A . n 
A 1 444 ALA 444 444 ?   ?   ?   A . n 
A 1 445 PHE 445 445 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ITD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ITD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FAD   1   501 501 FAD   FAD A . 
C 3 A1ITD 1   502 502 A1ITD DRG A . 
D 4 HOH   1   601 443 HOH   HOH A . 
D 4 HOH   2   602 464 HOH   HOH A . 
D 4 HOH   3   603 199 HOH   HOH A . 
D 4 HOH   4   604 441 HOH   HOH A . 
D 4 HOH   5   605 200 HOH   HOH A . 
D 4 HOH   6   606 212 HOH   HOH A . 
D 4 HOH   7   607 37  HOH   HOH A . 
D 4 HOH   8   608 174 HOH   HOH A . 
D 4 HOH   9   609 92  HOH   HOH A . 
D 4 HOH   10  610 442 HOH   HOH A . 
D 4 HOH   11  611 3   HOH   HOH A . 
D 4 HOH   12  612 245 HOH   HOH A . 
D 4 HOH   13  613 55  HOH   HOH A . 
D 4 HOH   14  614 328 HOH   HOH A . 
D 4 HOH   15  615 190 HOH   HOH A . 
D 4 HOH   16  616 70  HOH   HOH A . 
D 4 HOH   17  617 6   HOH   HOH A . 
D 4 HOH   18  618 149 HOH   HOH A . 
D 4 HOH   19  619 436 HOH   HOH A . 
D 4 HOH   20  620 185 HOH   HOH A . 
D 4 HOH   21  621 180 HOH   HOH A . 
D 4 HOH   22  622 113 HOH   HOH A . 
D 4 HOH   23  623 151 HOH   HOH A . 
D 4 HOH   24  624 103 HOH   HOH A . 
D 4 HOH   25  625 47  HOH   HOH A . 
D 4 HOH   26  626 463 HOH   HOH A . 
D 4 HOH   27  627 48  HOH   HOH A . 
D 4 HOH   28  628 21  HOH   HOH A . 
D 4 HOH   29  629 140 HOH   HOH A . 
D 4 HOH   30  630 285 HOH   HOH A . 
D 4 HOH   31  631 184 HOH   HOH A . 
D 4 HOH   32  632 50  HOH   HOH A . 
D 4 HOH   33  633 34  HOH   HOH A . 
D 4 HOH   34  634 65  HOH   HOH A . 
D 4 HOH   35  635 254 HOH   HOH A . 
D 4 HOH   36  636 154 HOH   HOH A . 
D 4 HOH   37  637 71  HOH   HOH A . 
D 4 HOH   38  638 202 HOH   HOH A . 
D 4 HOH   39  639 133 HOH   HOH A . 
D 4 HOH   40  640 5   HOH   HOH A . 
D 4 HOH   41  641 51  HOH   HOH A . 
D 4 HOH   42  642 7   HOH   HOH A . 
D 4 HOH   43  643 23  HOH   HOH A . 
D 4 HOH   44  644 339 HOH   HOH A . 
D 4 HOH   45  645 108 HOH   HOH A . 
D 4 HOH   46  646 439 HOH   HOH A . 
D 4 HOH   47  647 30  HOH   HOH A . 
D 4 HOH   48  648 16  HOH   HOH A . 
D 4 HOH   49  649 118 HOH   HOH A . 
D 4 HOH   50  650 129 HOH   HOH A . 
D 4 HOH   51  651 148 HOH   HOH A . 
D 4 HOH   52  652 142 HOH   HOH A . 
D 4 HOH   53  653 76  HOH   HOH A . 
D 4 HOH   54  654 4   HOH   HOH A . 
D 4 HOH   55  655 52  HOH   HOH A . 
D 4 HOH   56  656 12  HOH   HOH A . 
D 4 HOH   57  657 458 HOH   HOH A . 
D 4 HOH   58  658 111 HOH   HOH A . 
D 4 HOH   59  659 265 HOH   HOH A . 
D 4 HOH   60  660 42  HOH   HOH A . 
D 4 HOH   61  661 168 HOH   HOH A . 
D 4 HOH   62  662 9   HOH   HOH A . 
D 4 HOH   63  663 87  HOH   HOH A . 
D 4 HOH   64  664 8   HOH   HOH A . 
D 4 HOH   65  665 218 HOH   HOH A . 
D 4 HOH   66  666 165 HOH   HOH A . 
D 4 HOH   67  667 136 HOH   HOH A . 
D 4 HOH   68  668 26  HOH   HOH A . 
D 4 HOH   69  669 264 HOH   HOH A . 
D 4 HOH   70  670 125 HOH   HOH A . 
D 4 HOH   71  671 88  HOH   HOH A . 
D 4 HOH   72  672 14  HOH   HOH A . 
D 4 HOH   73  673 368 HOH   HOH A . 
D 4 HOH   74  674 19  HOH   HOH A . 
D 4 HOH   75  675 22  HOH   HOH A . 
D 4 HOH   76  676 249 HOH   HOH A . 
D 4 HOH   77  677 90  HOH   HOH A . 
D 4 HOH   78  678 20  HOH   HOH A . 
D 4 HOH   79  679 225 HOH   HOH A . 
D 4 HOH   80  680 63  HOH   HOH A . 
D 4 HOH   81  681 296 HOH   HOH A . 
D 4 HOH   82  682 43  HOH   HOH A . 
D 4 HOH   83  683 266 HOH   HOH A . 
D 4 HOH   84  684 40  HOH   HOH A . 
D 4 HOH   85  685 102 HOH   HOH A . 
D 4 HOH   86  686 95  HOH   HOH A . 
D 4 HOH   87  687 49  HOH   HOH A . 
D 4 HOH   88  688 124 HOH   HOH A . 
D 4 HOH   89  689 162 HOH   HOH A . 
D 4 HOH   90  690 1   HOH   HOH A . 
D 4 HOH   91  691 342 HOH   HOH A . 
D 4 HOH   92  692 106 HOH   HOH A . 
D 4 HOH   93  693 456 HOH   HOH A . 
D 4 HOH   94  694 105 HOH   HOH A . 
D 4 HOH   95  695 25  HOH   HOH A . 
D 4 HOH   96  696 139 HOH   HOH A . 
D 4 HOH   97  697 135 HOH   HOH A . 
D 4 HOH   98  698 15  HOH   HOH A . 
D 4 HOH   99  699 158 HOH   HOH A . 
D 4 HOH   100 700 29  HOH   HOH A . 
D 4 HOH   101 701 286 HOH   HOH A . 
D 4 HOH   102 702 17  HOH   HOH A . 
D 4 HOH   103 703 11  HOH   HOH A . 
D 4 HOH   104 704 44  HOH   HOH A . 
D 4 HOH   105 705 82  HOH   HOH A . 
D 4 HOH   106 706 197 HOH   HOH A . 
D 4 HOH   107 707 343 HOH   HOH A . 
D 4 HOH   108 708 13  HOH   HOH A . 
D 4 HOH   109 709 66  HOH   HOH A . 
D 4 HOH   110 710 258 HOH   HOH A . 
D 4 HOH   111 711 96  HOH   HOH A . 
D 4 HOH   112 712 210 HOH   HOH A . 
D 4 HOH   113 713 176 HOH   HOH A . 
D 4 HOH   114 714 36  HOH   HOH A . 
D 4 HOH   115 715 74  HOH   HOH A . 
D 4 HOH   116 716 32  HOH   HOH A . 
D 4 HOH   117 717 170 HOH   HOH A . 
D 4 HOH   118 718 64  HOH   HOH A . 
D 4 HOH   119 719 83  HOH   HOH A . 
D 4 HOH   120 720 31  HOH   HOH A . 
D 4 HOH   121 721 126 HOH   HOH A . 
D 4 HOH   122 722 10  HOH   HOH A . 
D 4 HOH   123 723 81  HOH   HOH A . 
D 4 HOH   124 724 27  HOH   HOH A . 
D 4 HOH   125 725 62  HOH   HOH A . 
D 4 HOH   126 726 86  HOH   HOH A . 
D 4 HOH   127 727 144 HOH   HOH A . 
D 4 HOH   128 728 18  HOH   HOH A . 
D 4 HOH   129 729 85  HOH   HOH A . 
D 4 HOH   130 730 216 HOH   HOH A . 
D 4 HOH   131 731 110 HOH   HOH A . 
D 4 HOH   132 732 69  HOH   HOH A . 
D 4 HOH   133 733 127 HOH   HOH A . 
D 4 HOH   134 734 56  HOH   HOH A . 
D 4 HOH   135 735 179 HOH   HOH A . 
D 4 HOH   136 736 45  HOH   HOH A . 
D 4 HOH   137 737 211 HOH   HOH A . 
D 4 HOH   138 738 68  HOH   HOH A . 
D 4 HOH   139 739 449 HOH   HOH A . 
D 4 HOH   140 740 38  HOH   HOH A . 
D 4 HOH   141 741 209 HOH   HOH A . 
D 4 HOH   142 742 117 HOH   HOH A . 
D 4 HOH   143 743 213 HOH   HOH A . 
D 4 HOH   144 744 295 HOH   HOH A . 
D 4 HOH   145 745 59  HOH   HOH A . 
D 4 HOH   146 746 138 HOH   HOH A . 
D 4 HOH   147 747 208 HOH   HOH A . 
D 4 HOH   148 748 187 HOH   HOH A . 
D 4 HOH   149 749 459 HOH   HOH A . 
D 4 HOH   150 750 94  HOH   HOH A . 
D 4 HOH   151 751 178 HOH   HOH A . 
D 4 HOH   152 752 77  HOH   HOH A . 
D 4 HOH   153 753 256 HOH   HOH A . 
D 4 HOH   154 754 112 HOH   HOH A . 
D 4 HOH   155 755 269 HOH   HOH A . 
D 4 HOH   156 756 53  HOH   HOH A . 
D 4 HOH   157 757 234 HOH   HOH A . 
D 4 HOH   158 758 385 HOH   HOH A . 
D 4 HOH   159 759 24  HOH   HOH A . 
D 4 HOH   160 760 107 HOH   HOH A . 
D 4 HOH   161 761 93  HOH   HOH A . 
D 4 HOH   162 762 143 HOH   HOH A . 
D 4 HOH   163 763 455 HOH   HOH A . 
D 4 HOH   164 764 159 HOH   HOH A . 
D 4 HOH   165 765 263 HOH   HOH A . 
D 4 HOH   166 766 67  HOH   HOH A . 
D 4 HOH   167 767 130 HOH   HOH A . 
D 4 HOH   168 768 189 HOH   HOH A . 
D 4 HOH   169 769 104 HOH   HOH A . 
D 4 HOH   170 770 97  HOH   HOH A . 
D 4 HOH   171 771 41  HOH   HOH A . 
D 4 HOH   172 772 157 HOH   HOH A . 
D 4 HOH   173 773 444 HOH   HOH A . 
D 4 HOH   174 774 243 HOH   HOH A . 
D 4 HOH   175 775 160 HOH   HOH A . 
D 4 HOH   176 776 46  HOH   HOH A . 
D 4 HOH   177 777 2   HOH   HOH A . 
D 4 HOH   178 778 115 HOH   HOH A . 
D 4 HOH   179 779 330 HOH   HOH A . 
D 4 HOH   180 780 172 HOH   HOH A . 
D 4 HOH   181 781 61  HOH   HOH A . 
D 4 HOH   182 782 156 HOH   HOH A . 
D 4 HOH   183 783 204 HOH   HOH A . 
D 4 HOH   184 784 350 HOH   HOH A . 
D 4 HOH   185 785 99  HOH   HOH A . 
D 4 HOH   186 786 220 HOH   HOH A . 
D 4 HOH   187 787 39  HOH   HOH A . 
D 4 HOH   188 788 35  HOH   HOH A . 
D 4 HOH   189 789 57  HOH   HOH A . 
D 4 HOH   190 790 75  HOH   HOH A . 
D 4 HOH   191 791 167 HOH   HOH A . 
D 4 HOH   192 792 294 HOH   HOH A . 
D 4 HOH   193 793 303 HOH   HOH A . 
D 4 HOH   194 794 147 HOH   HOH A . 
D 4 HOH   195 795 183 HOH   HOH A . 
D 4 HOH   196 796 275 HOH   HOH A . 
D 4 HOH   197 797 424 HOH   HOH A . 
D 4 HOH   198 798 114 HOH   HOH A . 
D 4 HOH   199 799 72  HOH   HOH A . 
D 4 HOH   200 800 28  HOH   HOH A . 
D 4 HOH   201 801 201 HOH   HOH A . 
D 4 HOH   202 802 242 HOH   HOH A . 
D 4 HOH   203 803 465 HOH   HOH A . 
D 4 HOH   204 804 451 HOH   HOH A . 
D 4 HOH   205 805 119 HOH   HOH A . 
D 4 HOH   206 806 78  HOH   HOH A . 
D 4 HOH   207 807 241 HOH   HOH A . 
D 4 HOH   208 808 181 HOH   HOH A . 
D 4 HOH   209 809 150 HOH   HOH A . 
D 4 HOH   210 810 325 HOH   HOH A . 
D 4 HOH   211 811 153 HOH   HOH A . 
D 4 HOH   212 812 317 HOH   HOH A . 
D 4 HOH   213 813 188 HOH   HOH A . 
D 4 HOH   214 814 422 HOH   HOH A . 
D 4 HOH   215 815 246 HOH   HOH A . 
D 4 HOH   216 816 89  HOH   HOH A . 
D 4 HOH   217 817 414 HOH   HOH A . 
D 4 HOH   218 818 310 HOH   HOH A . 
D 4 HOH   219 819 233 HOH   HOH A . 
D 4 HOH   220 820 146 HOH   HOH A . 
D 4 HOH   221 821 131 HOH   HOH A . 
D 4 HOH   222 822 344 HOH   HOH A . 
D 4 HOH   223 823 445 HOH   HOH A . 
D 4 HOH   224 824 428 HOH   HOH A . 
D 4 HOH   225 825 418 HOH   HOH A . 
D 4 HOH   226 826 454 HOH   HOH A . 
D 4 HOH   227 827 33  HOH   HOH A . 
D 4 HOH   228 828 205 HOH   HOH A . 
D 4 HOH   229 829 340 HOH   HOH A . 
D 4 HOH   230 830 311 HOH   HOH A . 
D 4 HOH   231 831 461 HOH   HOH A . 
D 4 HOH   232 832 214 HOH   HOH A . 
D 4 HOH   233 833 426 HOH   HOH A . 
D 4 HOH   234 834 239 HOH   HOH A . 
D 4 HOH   235 835 134 HOH   HOH A . 
D 4 HOH   236 836 417 HOH   HOH A . 
D 4 HOH   237 837 132 HOH   HOH A . 
D 4 HOH   238 838 452 HOH   HOH A . 
D 4 HOH   239 839 281 HOH   HOH A . 
D 4 HOH   240 840 423 HOH   HOH A . 
D 4 HOH   241 841 173 HOH   HOH A . 
D 4 HOH   242 842 420 HOH   HOH A . 
D 4 HOH   243 843 450 HOH   HOH A . 
D 4 HOH   244 844 73  HOH   HOH A . 
D 4 HOH   245 845 460 HOH   HOH A . 
D 4 HOH   246 846 60  HOH   HOH A . 
D 4 HOH   247 847 253 HOH   HOH A . 
D 4 HOH   248 848 101 HOH   HOH A . 
D 4 HOH   249 849 267 HOH   HOH A . 
D 4 HOH   250 850 415 HOH   HOH A . 
D 4 HOH   251 851 145 HOH   HOH A . 
D 4 HOH   252 852 438 HOH   HOH A . 
D 4 HOH   253 853 425 HOH   HOH A . 
D 4 HOH   254 854 453 HOH   HOH A . 
D 4 HOH   255 855 447 HOH   HOH A . 
D 4 HOH   256 856 171 HOH   HOH A . 
D 4 HOH   257 857 457 HOH   HOH A . 
D 4 HOH   258 858 466 HOH   HOH A . 
D 4 HOH   259 859 421 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU   41  ? CG  ? A GLU   41  CG  
2  1 Y 1 A GLU   41  ? CD  ? A GLU   41  CD  
3  1 Y 1 A GLU   41  ? OE1 ? A GLU   41  OE1 
4  1 Y 1 A GLU   41  ? OE2 ? A GLU   41  OE2 
5  1 Y 1 A GLU   45  ? CG  ? A GLU   45  CG  
6  1 Y 1 A GLU   45  ? CD  ? A GLU   45  CD  
7  1 Y 1 A GLU   45  ? OE1 ? A GLU   45  OE1 
8  1 Y 1 A GLU   45  ? OE2 ? A GLU   45  OE2 
9  1 Y 1 A SER   79  ? OG  ? A SER   79  OG  
10 1 Y 1 A GLN   92  ? CG  ? A GLN   92  CG  
11 1 Y 1 A GLN   92  ? CD  ? A GLN   92  CD  
12 1 Y 1 A GLN   92  ? OE1 ? A GLN   92  OE1 
13 1 Y 1 A GLN   92  ? NE2 ? A GLN   92  NE2 
14 1 Y 1 A LYS   132 ? CG  ? A LYS   132 CG  
15 1 Y 1 A LYS   132 ? CD  ? A LYS   132 CD  
16 1 Y 1 A LYS   132 ? CE  ? A LYS   132 CE  
17 1 Y 1 A LYS   132 ? NZ  ? A LYS   132 NZ  
18 1 Y 1 A HIS   148 ? CG  ? A HIS   148 CG  
19 1 Y 1 A HIS   148 ? ND1 ? A HIS   148 ND1 
20 1 Y 1 A HIS   148 ? CD2 ? A HIS   148 CD2 
21 1 Y 1 A HIS   148 ? CE1 ? A HIS   148 CE1 
22 1 Y 1 A HIS   148 ? NE2 ? A HIS   148 NE2 
23 1 Y 1 A GLU   149 ? CG  ? A GLU   149 CG  
24 1 Y 1 A GLU   149 ? CD  ? A GLU   149 CD  
25 1 Y 1 A GLU   149 ? OE1 ? A GLU   149 OE1 
26 1 Y 1 A GLU   149 ? OE2 ? A GLU   149 OE2 
27 1 Y 1 A LYS   156 ? CG  ? A LYS   156 CG  
28 1 Y 1 A LYS   156 ? CD  ? A LYS   156 CD  
29 1 Y 1 A LYS   156 ? CE  ? A LYS   156 CE  
30 1 Y 1 A LYS   156 ? NZ  ? A LYS   156 NZ  
31 1 Y 1 A ASP   186 ? CG  ? A ASP   186 CG  
32 1 Y 1 A ASP   186 ? OD1 ? A ASP   186 OD1 
33 1 Y 1 A ASP   186 ? OD2 ? A ASP   186 OD2 
34 1 Y 1 A GLU   187 ? CG  ? A GLU   187 CG  
35 1 Y 1 A GLU   187 ? CD  ? A GLU   187 CD  
36 1 Y 1 A GLU   187 ? OE1 ? A GLU   187 OE1 
37 1 Y 1 A GLU   187 ? OE2 ? A GLU   187 OE2 
38 1 Y 1 A LEU   188 ? CG  ? A LEU   188 CG  
39 1 Y 1 A LEU   188 ? CD1 ? A LEU   188 CD1 
40 1 Y 1 A LEU   188 ? CD2 ? A LEU   188 CD2 
41 1 Y 1 A GLU   238 ? CG  ? A GLU   238 CG  
42 1 Y 1 A GLU   238 ? CD  ? A GLU   238 CD  
43 1 Y 1 A GLU   238 ? OE1 ? A GLU   238 OE1 
44 1 Y 1 A GLU   238 ? OE2 ? A GLU   238 OE2 
45 1 Y 1 A LYS   251 ? CG  ? A LYS   251 CG  
46 1 Y 1 A LYS   251 ? CD  ? A LYS   251 CD  
47 1 Y 1 A LYS   251 ? CE  ? A LYS   251 CE  
48 1 Y 1 A LYS   251 ? NZ  ? A LYS   251 NZ  
49 1 Y 1 A GLU   256 ? CG  ? A GLU   256 CG  
50 1 Y 1 A GLU   256 ? CD  ? A GLU   256 CD  
51 1 Y 1 A GLU   256 ? OE1 ? A GLU   256 OE1 
52 1 Y 1 A GLU   256 ? OE2 ? A GLU   256 OE2 
53 1 Y 1 A LYS   264 ? CE  ? A LYS   264 CE  
54 1 Y 1 A LYS   264 ? NZ  ? A LYS   264 NZ  
55 1 Y 1 A GLU   281 ? CG  ? A GLU   281 CG  
56 1 Y 1 A GLU   281 ? CD  ? A GLU   281 CD  
57 1 Y 1 A GLU   281 ? OE1 ? A GLU   281 OE1 
58 1 Y 1 A GLU   281 ? OE2 ? A GLU   281 OE2 
59 1 Y 1 A GLU   355 ? CG  ? A GLU   355 CG  
60 1 Y 1 A GLU   355 ? CD  ? A GLU   355 CD  
61 1 Y 1 A GLU   355 ? OE1 ? A GLU   355 OE1 
62 1 Y 1 A GLU   355 ? OE2 ? A GLU   355 OE2 
63 1 Y 1 A ASN   358 ? CG  ? A ASN   358 CG  
64 1 Y 1 A ASN   358 ? OD1 ? A ASN   358 OD1 
65 1 Y 1 A ASN   358 ? ND2 ? A ASN   358 ND2 
66 1 Y 1 A GLU   405 ? CG  ? A GLU   405 CG  
67 1 Y 1 A GLU   405 ? CD  ? A GLU   405 CD  
68 1 Y 1 A GLU   405 ? OE1 ? A GLU   405 OE1 
69 1 Y 1 A GLU   405 ? OE2 ? A GLU   405 OE2 
70 1 N 1 A A1ITD 502 ? C1  ? C A1ITD 1   C1  
71 1 N 1 A A1ITD 502 ? C2  ? C A1ITD 1   C2  
72 1 N 1 A A1ITD 502 ? C3  ? C A1ITD 1   C3  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        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                     9H8Z 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.321 
_cell.length_a_esd                 ? 
_cell.length_b                     90.965 
_cell.length_b_esd                 ? 
_cell.length_c                     94.552 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9H8Z 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9H8Z 
_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             1.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          34.83 
_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' 
_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    '0.2 M ammonium citrate dibasic, 20% PEG3350, 1 mM sorbicillin, 1 mM NAD+' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 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         2024-03-03 
_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   0.96546 
_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                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.96546 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H8Z 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.71 
_reflns.d_resolution_low                               42.32 
_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                                     38849 
_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                           96.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.060 
_reflns.pdbx_Rpim_I_all                                0.028 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       165546 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.053 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.71 
_reflns_shell.d_res_low                                     1.74 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           7416 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1814 
_reflns_shell.percent_possible_obs                          86.8 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.1 
_reflns_shell.pdbx_chi_squared                              0.92 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.2 
_reflns_shell.pdbx_Rrim_I_all                               1.163 
_reflns_shell.pdbx_Rpim_I_all                               0.547 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.528 
_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                                  1.019 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.03 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.11 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.15 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               26.736 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.970 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9H8Z 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.71 
_refine.ls_d_res_low                             38.66 
_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                     36899 
_refine.ls_number_reflns_R_free                  1916 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.69 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17494 
_refine.ls_R_factor_R_free                       0.22737 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17237 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.120 
_refine.pdbx_overall_ESU_R_Free                  0.124 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.892 
_refine.overall_SU_ML                            0.090 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.71 
_refine_hist.d_res_low                        38.66 
_refine_hist.number_atoms_solvent             259 
_refine_hist.number_atoms_total               3541 
_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        3215 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         67 
_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' ? 0.007  0.012  3362 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3106 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.618  1.812  4586 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.561  1.738  7107 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.344  5.000  432  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.126 5.517  29   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.242 10.000 497  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.078  0.200  519  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  4072 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  783  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.421  2.770  1725 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.400  2.769  1725 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.371  4.965  2155 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.371  4.966  2156 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.213  3.061  1637 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.199  3.061  1637 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.765  5.491  2431 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.297  29.15  3830 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.308  28.54  3788 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.71 
_refine_ls_shell.d_res_low                        1.751 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             137 
_refine_ls_shell.number_reflns_R_work             2438 
_refine_ls_shell.percent_reflns_obs               87.50 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.363 
_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                  0.394 
# 
_struct.entry_id                     9H8Z 
_struct.title                        'FAD-dependent monooxygenase sorC with sorbicillin bound' 
_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        9H8Z 
_struct_keywords.text            'Flavin, FAD, natural product, monooxygenase, sorbicillinoids, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SORC_PENRW 
_struct_ref.pdbx_db_accession          B6HN76 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTRSANSPFEVAIVGGGITGLALAVGLLKRNVSFTIYERAENFGELGVGITFTPNAQRAMEALDPCVLQSFTNVASAPSG
GTINFVDGVREQGSEDPRTSTAALLFQLHVKGGYKACRRCDFVDQIVQHIPKDCVQYRKWLDSIETDHESGRAVLKFRDG
EIAHADVVIGCDGIRSQVRASMFGTDELCPRAQYSHQLGYRGMVPLAQATAVLGPEKTSSAVLHTGPGAFVLTIPLAEVH
AMHIEAFIMDKEEWPEVQTSSDSKRYVLPATRNEATKAFAEFGPTVRSAVSMFPEKLEKWAVFDMLEAPVPTFAKGRVCL
AGDAAHASTPNQGGGAGFGIEDALVLAEVLAVLAEAPNVSGIVASEALAVYSEVRYERSQWLVRSSRRTGELCTWKDRDW
GLAAEELSRDIISRSHQLWDHDTAGMVSDALAILGERVRGADTAF
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9H8Z 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 445 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             B6HN76 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  445 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       445 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1460  ? 
1 MORE         -6    ? 
1 'SSA (A^2)'  16630 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 17  ? ARG A 30  ? GLY A 17  ARG A 30  1 ? 14 
HELX_P HELX_P2  AA2 THR A 53  ? ASP A 64  ? THR A 53  ASP A 64  1 ? 12 
HELX_P HELX_P3  AA3 ASP A 64  ? ASN A 73  ? ASP A 64  ASN A 73  1 ? 10 
HELX_P HELX_P4  AA4 ARG A 119 ? GLN A 128 ? ARG A 119 GLN A 128 1 ? 10 
HELX_P HELX_P5  AA5 HIS A 129 ? ILE A 130 ? HIS A 129 ILE A 130 5 ? 2  
HELX_P HELX_P6  AA6 PRO A 131 ? ASP A 133 ? PRO A 131 ASP A 133 5 ? 3  
HELX_P HELX_P7  AA7 SER A 176 ? GLY A 184 ? SER A 176 GLY A 184 1 ? 9  
HELX_P HELX_P8  AA8 LEU A 206 ? GLY A 214 ? LEU A 206 GLY A 214 1 ? 9  
HELX_P HELX_P9  AA9 PRO A 215 ? SER A 219 ? PRO A 215 SER A 219 5 ? 5  
HELX_P HELX_P10 AB1 SER A 261 ? TYR A 266 ? SER A 261 TYR A 266 1 ? 6  
HELX_P HELX_P11 AB2 ARG A 272 ? PHE A 279 ? ARG A 272 PHE A 279 1 ? 8  
HELX_P HELX_P12 AB3 GLY A 283 ? MET A 292 ? GLY A 283 MET A 292 1 ? 10 
HELX_P HELX_P13 AB4 GLY A 322 ? ALA A 327 ? GLY A 322 ALA A 327 1 ? 6  
HELX_P HELX_P14 AB5 GLY A 335 ? ALA A 356 ? GLY A 335 ALA A 356 1 ? 22 
HELX_P HELX_P15 AB6 SER A 360 ? THR A 394 ? SER A 360 THR A 394 1 ? 35 
HELX_P HELX_P16 AB7 ASP A 399 ? LEU A 402 ? ASP A 399 LEU A 402 5 ? 4  
HELX_P HELX_P17 AB8 ALA A 403 ? ASP A 420 ? ALA A 403 ASP A 420 1 ? 18 
HELX_P HELX_P18 AB9 ASP A 422 ? VAL A 438 ? ASP A 422 VAL A 438 1 ? 17 
# 
_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 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 8 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? 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 135 ? GLN A 136 ? VAL A 135 GLN A 136 
AA1 2 SER A 33  ? TYR A 37  ? SER A 33  TYR A 37  
AA1 3 GLU A 10  ? VAL A 14  ? GLU A 10  VAL A 14  
AA1 4 VAL A 167 ? GLY A 170 ? VAL A 167 GLY A 170 
AA1 5 VAL A 318 ? LEU A 320 ? VAL A 318 LEU A 320 
AA1 6 ALA A 314 ? LYS A 315 ? ALA A 314 LYS A 315 
AA2 1 GLY A 49  ? PHE A 52  ? GLY A 49  PHE A 52  
AA2 2 LYS A 115 ? ARG A 118 ? LYS A 115 ARG A 118 
AA3 1 THR A 101 ? HIS A 109 ? THR A 101 HIS A 109 
AA3 2 THR A 82  ? GLN A 92  ? THR A 82  GLN A 92  
AA3 3 ALA A 221 ? THR A 225 ? ALA A 221 THR A 225 
AA3 4 ALA A 229 ? LEU A 236 ? ALA A 229 LEU A 236 
AA3 5 ALA A 241 ? MET A 249 ? ALA A 241 MET A 249 
AA3 6 ARG A 191 ? PRO A 205 ? ARG A 191 PRO A 205 
AA3 7 LYS A 296 ? ALA A 308 ? LYS A 296 ALA A 308 
AA3 8 VAL A 267 ? THR A 271 ? VAL A 267 THR A 271 
AA4 1 LEU A 141 ? THR A 146 ? LEU A 141 THR A 146 
AA4 2 ALA A 153 ? PHE A 157 ? ALA A 153 PHE A 157 
AA4 3 ILE A 162 ? ALA A 165 ? ILE A 162 ALA A 165 
# 
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 O GLN A 136 ? O GLN A 136 N ILE A 36  ? N ILE A 36  
AA1 2 3 O TYR A 37  ? O TYR A 37  N ILE A 13  ? N ILE A 13  
AA1 3 4 N ALA A 12  ? N ALA A 12  O ILE A 169 ? O ILE A 169 
AA1 4 5 N GLY A 170 ? N GLY A 170 O CYS A 319 ? O CYS A 319 
AA1 5 6 O VAL A 318 ? O VAL A 318 N LYS A 315 ? N LYS A 315 
AA2 1 2 N PHE A 52  ? N PHE A 52  O LYS A 115 ? O LYS A 115 
AA3 1 2 O LEU A 105 ? O LEU A 105 N PHE A 85  ? N PHE A 85  
AA3 2 3 N ASN A 84  ? N ASN A 84  O LEU A 223 ? O LEU A 223 
AA3 3 4 N HIS A 224 ? N HIS A 224 O VAL A 231 ? O VAL A 231 
AA3 4 5 N LEU A 232 ? N LEU A 232 O GLU A 245 ? O GLU A 245 
AA3 5 6 O ALA A 246 ? O ALA A 246 N TYR A 200 ? N TYR A 200 
AA3 6 7 N GLN A 193 ? N GLN A 193 O ASP A 304 ? O ASP A 304 
AA3 7 8 O LEU A 297 ? O LEU A 297 N ALA A 270 ? N ALA A 270 
AA4 1 2 N SER A 143 ? N SER A 143 O LYS A 156 ? O LYS A 156 
AA4 2 3 N LEU A 155 ? N LEU A 155 O ALA A 163 ? O ALA A 163 
# 
_pdbx_entry_details.entry_id                   9H8Z 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 45  ? ? -149.88 26.14  
2 1 ASP A 64  ? ? -175.41 142.20 
3 1 HIS A 326 ? ? -158.55 49.00  
4 1 ALA A 403 ? ? -144.60 51.82  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 179 ? ? 0.139 'SIDE CHAIN' 
2 1 ARG A 201 ? ? 0.154 'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A ARG 3   ? A ARG 3   
4  1 Y 1 A SER 4   ? A SER 4   
5  1 Y 1 A ALA 5   ? A ALA 5   
6  1 Y 1 A ASN 6   ? A ASN 6   
7  1 Y 1 A SER 7   ? A SER 7   
8  1 Y 1 A ARG 439 ? A ARG 439 
9  1 Y 1 A GLY 440 ? A GLY 440 
10 1 Y 1 A ALA 441 ? A ALA 441 
11 1 Y 1 A ASP 442 ? A ASP 442 
12 1 Y 1 A THR 443 ? A THR 443 
13 1 Y 1 A ALA 444 ? A ALA 444 
14 1 Y 1 A PHE 445 ? A PHE 445 
# 
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 
A1ITD C4     C N N 1   
A1ITD C14    C Y N 2   
A1ITD C5     C N N 3   
A1ITD C6     C N N 4   
A1ITD C11    C Y N 5   
A1ITD C7     C Y N 6   
A1ITD C8     C Y N 7   
A1ITD C9     C Y N 8   
A1ITD C10    C N N 9   
A1ITD C12    C Y N 10  
A1ITD C13    C N N 11  
A1ITD O1     O N N 12  
A1ITD O2     O N N 13  
A1ITD O3     O N N 14  
A1ITD H1     H N N 15  
A1ITD H3     H N N 16  
A1ITD H4     H N N 17  
A1ITD H5     H N N 18  
A1ITD H6     H N N 19  
A1ITD H7     H N N 20  
A1ITD H8     H N N 21  
A1ITD H9     H N N 22  
A1ITD H10    H N N 23  
A1ITD H11    H N N 24  
A1ITD H12    H N N 25  
A1ITD C1     C N N 26  
A1ITD C2     C N N 27  
A1ITD C3     C N N 28  
A1ITD H2     H N N 29  
A1ITD H13    H N N 30  
A1ITD H14    H N N 31  
A1ITD H15    H N N 32  
A1ITD H16    H N N 33  
ALA   N      N N N 34  
ALA   CA     C N S 35  
ALA   C      C N N 36  
ALA   O      O N N 37  
ALA   CB     C N N 38  
ALA   OXT    O N N 39  
ALA   H      H N N 40  
ALA   H2     H N N 41  
ALA   HA     H N N 42  
ALA   HB1    H N N 43  
ALA   HB2    H N N 44  
ALA   HB3    H N N 45  
ALA   HXT    H N N 46  
ARG   N      N N N 47  
ARG   CA     C N S 48  
ARG   C      C N N 49  
ARG   O      O N N 50  
ARG   CB     C N N 51  
ARG   CG     C N N 52  
ARG   CD     C N N 53  
ARG   NE     N N N 54  
ARG   CZ     C N N 55  
ARG   NH1    N N N 56  
ARG   NH2    N N N 57  
ARG   OXT    O N N 58  
ARG   H      H N N 59  
ARG   H2     H N N 60  
ARG   HA     H N N 61  
ARG   HB2    H N N 62  
ARG   HB3    H N N 63  
ARG   HG2    H N N 64  
ARG   HG3    H N N 65  
ARG   HD2    H N N 66  
ARG   HD3    H N N 67  
ARG   HE     H N N 68  
ARG   HH11   H N N 69  
ARG   HH12   H N N 70  
ARG   HH21   H N N 71  
ARG   HH22   H N N 72  
ARG   HXT    H N N 73  
ASN   N      N N N 74  
ASN   CA     C N S 75  
ASN   C      C N N 76  
ASN   O      O N N 77  
ASN   CB     C N N 78  
ASN   CG     C N N 79  
ASN   OD1    O N N 80  
ASN   ND2    N N N 81  
ASN   OXT    O N N 82  
ASN   H      H N N 83  
ASN   H2     H N N 84  
ASN   HA     H N N 85  
ASN   HB2    H N N 86  
ASN   HB3    H N N 87  
ASN   HD21   H N N 88  
ASN   HD22   H N N 89  
ASN   HXT    H N N 90  
ASP   N      N N N 91  
ASP   CA     C N S 92  
ASP   C      C N N 93  
ASP   O      O N N 94  
ASP   CB     C N N 95  
ASP   CG     C N N 96  
ASP   OD1    O N N 97  
ASP   OD2    O N N 98  
ASP   OXT    O N N 99  
ASP   H      H N N 100 
ASP   H2     H N N 101 
ASP   HA     H N N 102 
ASP   HB2    H N N 103 
ASP   HB3    H N N 104 
ASP   HD2    H N N 105 
ASP   HXT    H N N 106 
CYS   N      N N N 107 
CYS   CA     C N R 108 
CYS   C      C N N 109 
CYS   O      O N N 110 
CYS   CB     C N N 111 
CYS   SG     S N N 112 
CYS   OXT    O N N 113 
CYS   H      H N N 114 
CYS   H2     H N N 115 
CYS   HA     H N N 116 
CYS   HB2    H N N 117 
CYS   HB3    H N N 118 
CYS   HG     H N N 119 
CYS   HXT    H N N 120 
FAD   PA     P N R 121 
FAD   O1A    O N N 122 
FAD   O2A    O N N 123 
FAD   O5B    O N N 124 
FAD   C5B    C N N 125 
FAD   C4B    C N R 126 
FAD   O4B    O N N 127 
FAD   C3B    C N S 128 
FAD   O3B    O N N 129 
FAD   C2B    C N R 130 
FAD   O2B    O N N 131 
FAD   C1B    C N R 132 
FAD   N9A    N Y N 133 
FAD   C8A    C Y N 134 
FAD   N7A    N Y N 135 
FAD   C5A    C Y N 136 
FAD   C6A    C Y N 137 
FAD   N6A    N N N 138 
FAD   N1A    N Y N 139 
FAD   C2A    C Y N 140 
FAD   N3A    N Y N 141 
FAD   C4A    C Y N 142 
FAD   N1     N N N 143 
FAD   C2     C N N 144 
FAD   O2     O N N 145 
FAD   N3     N N N 146 
FAD   C4     C N N 147 
FAD   O4     O N N 148 
FAD   C4X    C N N 149 
FAD   N5     N N N 150 
FAD   C5X    C Y N 151 
FAD   C6     C Y N 152 
FAD   C7     C Y N 153 
FAD   C7M    C N N 154 
FAD   C8     C Y N 155 
FAD   C8M    C N N 156 
FAD   C9     C Y N 157 
FAD   C9A    C Y N 158 
FAD   N10    N N N 159 
FAD   C10    C N N 160 
FAD   "C1'"  C N N 161 
FAD   "C2'"  C N S 162 
FAD   "O2'"  O N N 163 
FAD   "C3'"  C N S 164 
FAD   "O3'"  O N N 165 
FAD   "C4'"  C N R 166 
FAD   "O4'"  O N N 167 
FAD   "C5'"  C N N 168 
FAD   "O5'"  O N N 169 
FAD   P      P N R 170 
FAD   O1P    O N N 171 
FAD   O2P    O N N 172 
FAD   O3P    O N N 173 
FAD   HOA2   H N N 174 
FAD   H51A   H N N 175 
FAD   H52A   H N N 176 
FAD   H4B    H N N 177 
FAD   H3B    H N N 178 
FAD   HO3A   H N N 179 
FAD   H2B    H N N 180 
FAD   HO2A   H N N 181 
FAD   H1B    H N N 182 
FAD   H8A    H N N 183 
FAD   H61A   H N N 184 
FAD   H62A   H N N 185 
FAD   H2A    H N N 186 
FAD   HN3    H N N 187 
FAD   H6     H N N 188 
FAD   HM71   H N N 189 
FAD   HM72   H N N 190 
FAD   HM73   H N N 191 
FAD   HM81   H N N 192 
FAD   HM82   H N N 193 
FAD   HM83   H N N 194 
FAD   H9     H N N 195 
FAD   "H1'1" H N N 196 
FAD   "H1'2" H N N 197 
FAD   "H2'"  H N N 198 
FAD   "HO2'" H N N 199 
FAD   "H3'"  H N N 200 
FAD   "HO3'" H N N 201 
FAD   "H4'"  H N N 202 
FAD   "HO4'" H N N 203 
FAD   "H5'1" H N N 204 
FAD   "H5'2" H N N 205 
FAD   HOP2   H N N 206 
GLN   N      N N N 207 
GLN   CA     C N S 208 
GLN   C      C N N 209 
GLN   O      O N N 210 
GLN   CB     C N N 211 
GLN   CG     C N N 212 
GLN   CD     C N N 213 
GLN   OE1    O N N 214 
GLN   NE2    N N N 215 
GLN   OXT    O N N 216 
GLN   H      H N N 217 
GLN   H2     H N N 218 
GLN   HA     H N N 219 
GLN   HB2    H N N 220 
GLN   HB3    H N N 221 
GLN   HG2    H N N 222 
GLN   HG3    H N N 223 
GLN   HE21   H N N 224 
GLN   HE22   H N N 225 
GLN   HXT    H N N 226 
GLU   N      N N N 227 
GLU   CA     C N S 228 
GLU   C      C N N 229 
GLU   O      O N N 230 
GLU   CB     C N N 231 
GLU   CG     C N N 232 
GLU   CD     C N N 233 
GLU   OE1    O N N 234 
GLU   OE2    O N N 235 
GLU   OXT    O N N 236 
GLU   H      H N N 237 
GLU   H2     H N N 238 
GLU   HA     H N N 239 
GLU   HB2    H N N 240 
GLU   HB3    H N N 241 
GLU   HG2    H N N 242 
GLU   HG3    H N N 243 
GLU   HE2    H N N 244 
GLU   HXT    H N N 245 
GLY   N      N N N 246 
GLY   CA     C N N 247 
GLY   C      C N N 248 
GLY   O      O N N 249 
GLY   OXT    O N N 250 
GLY   H      H N N 251 
GLY   H2     H N N 252 
GLY   HA2    H N N 253 
GLY   HA3    H N N 254 
GLY   HXT    H N N 255 
HIS   N      N N N 256 
HIS   CA     C N S 257 
HIS   C      C N N 258 
HIS   O      O N N 259 
HIS   CB     C N N 260 
HIS   CG     C Y N 261 
HIS   ND1    N Y N 262 
HIS   CD2    C Y N 263 
HIS   CE1    C Y N 264 
HIS   NE2    N Y N 265 
HIS   OXT    O N N 266 
HIS   H      H N N 267 
HIS   H2     H N N 268 
HIS   HA     H N N 269 
HIS   HB2    H N N 270 
HIS   HB3    H N N 271 
HIS   HD1    H N N 272 
HIS   HD2    H N N 273 
HIS   HE1    H N N 274 
HIS   HE2    H N N 275 
HIS   HXT    H N N 276 
HOH   O      O N N 277 
HOH   H1     H N N 278 
HOH   H2     H N N 279 
ILE   N      N N N 280 
ILE   CA     C N S 281 
ILE   C      C N N 282 
ILE   O      O N N 283 
ILE   CB     C N S 284 
ILE   CG1    C N N 285 
ILE   CG2    C N N 286 
ILE   CD1    C N N 287 
ILE   OXT    O N N 288 
ILE   H      H N N 289 
ILE   H2     H N N 290 
ILE   HA     H N N 291 
ILE   HB     H N N 292 
ILE   HG12   H N N 293 
ILE   HG13   H N N 294 
ILE   HG21   H N N 295 
ILE   HG22   H N N 296 
ILE   HG23   H N N 297 
ILE   HD11   H N N 298 
ILE   HD12   H N N 299 
ILE   HD13   H N N 300 
ILE   HXT    H N N 301 
LEU   N      N N N 302 
LEU   CA     C N S 303 
LEU   C      C N N 304 
LEU   O      O N N 305 
LEU   CB     C N N 306 
LEU   CG     C N N 307 
LEU   CD1    C N N 308 
LEU   CD2    C N N 309 
LEU   OXT    O N N 310 
LEU   H      H N N 311 
LEU   H2     H N N 312 
LEU   HA     H N N 313 
LEU   HB2    H N N 314 
LEU   HB3    H N N 315 
LEU   HG     H N N 316 
LEU   HD11   H N N 317 
LEU   HD12   H N N 318 
LEU   HD13   H N N 319 
LEU   HD21   H N N 320 
LEU   HD22   H N N 321 
LEU   HD23   H N N 322 
LEU   HXT    H N N 323 
LYS   N      N N N 324 
LYS   CA     C N S 325 
LYS   C      C N N 326 
LYS   O      O N N 327 
LYS   CB     C N N 328 
LYS   CG     C N N 329 
LYS   CD     C N N 330 
LYS   CE     C N N 331 
LYS   NZ     N N N 332 
LYS   OXT    O N N 333 
LYS   H      H N N 334 
LYS   H2     H N N 335 
LYS   HA     H N N 336 
LYS   HB2    H N N 337 
LYS   HB3    H N N 338 
LYS   HG2    H N N 339 
LYS   HG3    H N N 340 
LYS   HD2    H N N 341 
LYS   HD3    H N N 342 
LYS   HE2    H N N 343 
LYS   HE3    H N N 344 
LYS   HZ1    H N N 345 
LYS   HZ2    H N N 346 
LYS   HZ3    H N N 347 
LYS   HXT    H N N 348 
MET   N      N N N 349 
MET   CA     C N S 350 
MET   C      C N N 351 
MET   O      O N N 352 
MET   CB     C N N 353 
MET   CG     C N N 354 
MET   SD     S N N 355 
MET   CE     C N N 356 
MET   OXT    O N N 357 
MET   H      H N N 358 
MET   H2     H N N 359 
MET   HA     H N N 360 
MET   HB2    H N N 361 
MET   HB3    H N N 362 
MET   HG2    H N N 363 
MET   HG3    H N N 364 
MET   HE1    H N N 365 
MET   HE2    H N N 366 
MET   HE3    H N N 367 
MET   HXT    H N N 368 
PHE   N      N N N 369 
PHE   CA     C N S 370 
PHE   C      C N N 371 
PHE   O      O N N 372 
PHE   CB     C N N 373 
PHE   CG     C Y N 374 
PHE   CD1    C Y N 375 
PHE   CD2    C Y N 376 
PHE   CE1    C Y N 377 
PHE   CE2    C Y N 378 
PHE   CZ     C Y N 379 
PHE   OXT    O N N 380 
PHE   H      H N N 381 
PHE   H2     H N N 382 
PHE   HA     H N N 383 
PHE   HB2    H N N 384 
PHE   HB3    H N N 385 
PHE   HD1    H N N 386 
PHE   HD2    H N N 387 
PHE   HE1    H N N 388 
PHE   HE2    H N N 389 
PHE   HZ     H N N 390 
PHE   HXT    H N N 391 
PRO   N      N N N 392 
PRO   CA     C N S 393 
PRO   C      C N N 394 
PRO   O      O N N 395 
PRO   CB     C N N 396 
PRO   CG     C N N 397 
PRO   CD     C N N 398 
PRO   OXT    O N N 399 
PRO   H      H N N 400 
PRO   HA     H N N 401 
PRO   HB2    H N N 402 
PRO   HB3    H N N 403 
PRO   HG2    H N N 404 
PRO   HG3    H N N 405 
PRO   HD2    H N N 406 
PRO   HD3    H N N 407 
PRO   HXT    H N N 408 
SER   N      N N N 409 
SER   CA     C N S 410 
SER   C      C N N 411 
SER   O      O N N 412 
SER   CB     C N N 413 
SER   OG     O N N 414 
SER   OXT    O N N 415 
SER   H      H N N 416 
SER   H2     H N N 417 
SER   HA     H N N 418 
SER   HB2    H N N 419 
SER   HB3    H N N 420 
SER   HG     H N N 421 
SER   HXT    H N N 422 
THR   N      N N N 423 
THR   CA     C N S 424 
THR   C      C N N 425 
THR   O      O N N 426 
THR   CB     C N R 427 
THR   OG1    O N N 428 
THR   CG2    C N N 429 
THR   OXT    O N N 430 
THR   H      H N N 431 
THR   H2     H N N 432 
THR   HA     H N N 433 
THR   HB     H N N 434 
THR   HG1    H N N 435 
THR   HG21   H N N 436 
THR   HG22   H N N 437 
THR   HG23   H N N 438 
THR   HXT    H N N 439 
TRP   N      N N N 440 
TRP   CA     C N S 441 
TRP   C      C N N 442 
TRP   O      O N N 443 
TRP   CB     C N N 444 
TRP   CG     C Y N 445 
TRP   CD1    C Y N 446 
TRP   CD2    C Y N 447 
TRP   NE1    N Y N 448 
TRP   CE2    C Y N 449 
TRP   CE3    C Y N 450 
TRP   CZ2    C Y N 451 
TRP   CZ3    C Y N 452 
TRP   CH2    C Y N 453 
TRP   OXT    O N N 454 
TRP   H      H N N 455 
TRP   H2     H N N 456 
TRP   HA     H N N 457 
TRP   HB2    H N N 458 
TRP   HB3    H N N 459 
TRP   HD1    H N N 460 
TRP   HE1    H N N 461 
TRP   HE3    H N N 462 
TRP   HZ2    H N N 463 
TRP   HZ3    H N N 464 
TRP   HH2    H N N 465 
TRP   HXT    H N N 466 
TYR   N      N N N 467 
TYR   CA     C N S 468 
TYR   C      C N N 469 
TYR   O      O N N 470 
TYR   CB     C N N 471 
TYR   CG     C Y N 472 
TYR   CD1    C Y N 473 
TYR   CD2    C Y N 474 
TYR   CE1    C Y N 475 
TYR   CE2    C Y N 476 
TYR   CZ     C Y N 477 
TYR   OH     O N N 478 
TYR   OXT    O N N 479 
TYR   H      H N N 480 
TYR   H2     H N N 481 
TYR   HA     H N N 482 
TYR   HB2    H N N 483 
TYR   HB3    H N N 484 
TYR   HD1    H N N 485 
TYR   HD2    H N N 486 
TYR   HE1    H N N 487 
TYR   HE2    H N N 488 
TYR   HH     H N N 489 
TYR   HXT    H N N 490 
VAL   N      N N N 491 
VAL   CA     C N S 492 
VAL   C      C N N 493 
VAL   O      O N N 494 
VAL   CB     C N N 495 
VAL   CG1    C N N 496 
VAL   CG2    C N N 497 
VAL   OXT    O N N 498 
VAL   H      H N N 499 
VAL   H2     H N N 500 
VAL   HA     H N N 501 
VAL   HB     H N N 502 
VAL   HG11   H N N 503 
VAL   HG12   H N N 504 
VAL   HG13   H N N 505 
VAL   HG21   H N N 506 
VAL   HG22   H N N 507 
VAL   HG23   H N N 508 
VAL   HXT    H N N 509 
# 
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 
A1ITD O1    C6     doub N N 1   
A1ITD C10   C9     sing N N 2   
A1ITD C8    C9     doub Y N 3   
A1ITD C8    C7     sing Y N 4   
A1ITD C6    C7     sing N N 5   
A1ITD C6    C5     sing N N 6   
A1ITD C9    C11    sing Y N 7   
A1ITD C4    C5     doub N E 8   
A1ITD C7    C14    doub Y N 9   
A1ITD C11   O2     sing N N 10  
A1ITD C11   C12    doub Y N 11  
A1ITD C14   C12    sing Y N 12  
A1ITD C14   O3     sing N N 13  
A1ITD C12   C13    sing N N 14  
A1ITD C4    H1     sing N N 15  
A1ITD C5    H3     sing N N 16  
A1ITD C8    H4     sing N N 17  
A1ITD C10   H5     sing N N 18  
A1ITD C10   H6     sing N N 19  
A1ITD C10   H7     sing N N 20  
A1ITD C13   H8     sing N N 21  
A1ITD C13   H9     sing N N 22  
A1ITD C13   H10    sing N N 23  
A1ITD O2    H11    sing N N 24  
A1ITD O3    H12    sing N N 25  
A1ITD C4    C1     sing N N 26  
A1ITD C1    C2     doub N N 27  
A1ITD C2    C3     sing N N 28  
A1ITD C1    H2     sing N N 29  
A1ITD C2    H13    sing N N 30  
A1ITD C3    H14    sing N N 31  
A1ITD C3    H15    sing N N 32  
A1ITD C3    H16    sing N N 33  
ALA   N     CA     sing N N 34  
ALA   N     H      sing N N 35  
ALA   N     H2     sing N N 36  
ALA   CA    C      sing N N 37  
ALA   CA    CB     sing N N 38  
ALA   CA    HA     sing N N 39  
ALA   C     O      doub N N 40  
ALA   C     OXT    sing N N 41  
ALA   CB    HB1    sing N N 42  
ALA   CB    HB2    sing N N 43  
ALA   CB    HB3    sing N N 44  
ALA   OXT   HXT    sing N N 45  
ARG   N     CA     sing N N 46  
ARG   N     H      sing N N 47  
ARG   N     H2     sing N N 48  
ARG   CA    C      sing N N 49  
ARG   CA    CB     sing N N 50  
ARG   CA    HA     sing N N 51  
ARG   C     O      doub N N 52  
ARG   C     OXT    sing N N 53  
ARG   CB    CG     sing N N 54  
ARG   CB    HB2    sing N N 55  
ARG   CB    HB3    sing N N 56  
ARG   CG    CD     sing N N 57  
ARG   CG    HG2    sing N N 58  
ARG   CG    HG3    sing N N 59  
ARG   CD    NE     sing N N 60  
ARG   CD    HD2    sing N N 61  
ARG   CD    HD3    sing N N 62  
ARG   NE    CZ     sing N N 63  
ARG   NE    HE     sing N N 64  
ARG   CZ    NH1    sing N N 65  
ARG   CZ    NH2    doub N N 66  
ARG   NH1   HH11   sing N N 67  
ARG   NH1   HH12   sing N N 68  
ARG   NH2   HH21   sing N N 69  
ARG   NH2   HH22   sing N N 70  
ARG   OXT   HXT    sing N N 71  
ASN   N     CA     sing N N 72  
ASN   N     H      sing N N 73  
ASN   N     H2     sing N N 74  
ASN   CA    C      sing N N 75  
ASN   CA    CB     sing N N 76  
ASN   CA    HA     sing N N 77  
ASN   C     O      doub N N 78  
ASN   C     OXT    sing N N 79  
ASN   CB    CG     sing N N 80  
ASN   CB    HB2    sing N N 81  
ASN   CB    HB3    sing N N 82  
ASN   CG    OD1    doub N N 83  
ASN   CG    ND2    sing N N 84  
ASN   ND2   HD21   sing N N 85  
ASN   ND2   HD22   sing N N 86  
ASN   OXT   HXT    sing N N 87  
ASP   N     CA     sing N N 88  
ASP   N     H      sing N N 89  
ASP   N     H2     sing N N 90  
ASP   CA    C      sing N N 91  
ASP   CA    CB     sing N N 92  
ASP   CA    HA     sing N N 93  
ASP   C     O      doub N N 94  
ASP   C     OXT    sing N N 95  
ASP   CB    CG     sing N N 96  
ASP   CB    HB2    sing N N 97  
ASP   CB    HB3    sing N N 98  
ASP   CG    OD1    doub N N 99  
ASP   CG    OD2    sing N N 100 
ASP   OD2   HD2    sing N N 101 
ASP   OXT   HXT    sing N N 102 
CYS   N     CA     sing N N 103 
CYS   N     H      sing N N 104 
CYS   N     H2     sing N N 105 
CYS   CA    C      sing N N 106 
CYS   CA    CB     sing N N 107 
CYS   CA    HA     sing N N 108 
CYS   C     O      doub N N 109 
CYS   C     OXT    sing N N 110 
CYS   CB    SG     sing N N 111 
CYS   CB    HB2    sing N N 112 
CYS   CB    HB3    sing N N 113 
CYS   SG    HG     sing N N 114 
CYS   OXT   HXT    sing N N 115 
FAD   PA    O1A    doub N N 116 
FAD   PA    O2A    sing N N 117 
FAD   PA    O5B    sing N N 118 
FAD   PA    O3P    sing N N 119 
FAD   O2A   HOA2   sing N N 120 
FAD   O5B   C5B    sing N N 121 
FAD   C5B   C4B    sing N N 122 
FAD   C5B   H51A   sing N N 123 
FAD   C5B   H52A   sing N N 124 
FAD   C4B   O4B    sing N N 125 
FAD   C4B   C3B    sing N N 126 
FAD   C4B   H4B    sing N N 127 
FAD   O4B   C1B    sing N N 128 
FAD   C3B   O3B    sing N N 129 
FAD   C3B   C2B    sing N N 130 
FAD   C3B   H3B    sing N N 131 
FAD   O3B   HO3A   sing N N 132 
FAD   C2B   O2B    sing N N 133 
FAD   C2B   C1B    sing N N 134 
FAD   C2B   H2B    sing N N 135 
FAD   O2B   HO2A   sing N N 136 
FAD   C1B   N9A    sing N N 137 
FAD   C1B   H1B    sing N N 138 
FAD   N9A   C8A    sing Y N 139 
FAD   N9A   C4A    sing Y N 140 
FAD   C8A   N7A    doub Y N 141 
FAD   C8A   H8A    sing N N 142 
FAD   N7A   C5A    sing Y N 143 
FAD   C5A   C6A    sing Y N 144 
FAD   C5A   C4A    doub Y N 145 
FAD   C6A   N6A    sing N N 146 
FAD   C6A   N1A    doub Y N 147 
FAD   N6A   H61A   sing N N 148 
FAD   N6A   H62A   sing N N 149 
FAD   N1A   C2A    sing Y N 150 
FAD   C2A   N3A    doub Y N 151 
FAD   C2A   H2A    sing N N 152 
FAD   N3A   C4A    sing Y N 153 
FAD   N1    C2     sing N N 154 
FAD   N1    C10    doub N N 155 
FAD   C2    O2     doub N N 156 
FAD   C2    N3     sing N N 157 
FAD   N3    C4     sing N N 158 
FAD   N3    HN3    sing N N 159 
FAD   C4    O4     doub N N 160 
FAD   C4    C4X    sing N N 161 
FAD   C4X   N5     doub N N 162 
FAD   C4X   C10    sing N N 163 
FAD   N5    C5X    sing N N 164 
FAD   C5X   C6     doub Y N 165 
FAD   C5X   C9A    sing Y N 166 
FAD   C6    C7     sing Y N 167 
FAD   C6    H6     sing N N 168 
FAD   C7    C7M    sing N N 169 
FAD   C7    C8     doub Y N 170 
FAD   C7M   HM71   sing N N 171 
FAD   C7M   HM72   sing N N 172 
FAD   C7M   HM73   sing N N 173 
FAD   C8    C8M    sing N N 174 
FAD   C8    C9     sing Y N 175 
FAD   C8M   HM81   sing N N 176 
FAD   C8M   HM82   sing N N 177 
FAD   C8M   HM83   sing N N 178 
FAD   C9    C9A    doub Y N 179 
FAD   C9    H9     sing N N 180 
FAD   C9A   N10    sing N N 181 
FAD   N10   C10    sing N N 182 
FAD   N10   "C1'"  sing N N 183 
FAD   "C1'" "C2'"  sing N N 184 
FAD   "C1'" "H1'1" sing N N 185 
FAD   "C1'" "H1'2" sing N N 186 
FAD   "C2'" "O2'"  sing N N 187 
FAD   "C2'" "C3'"  sing N N 188 
FAD   "C2'" "H2'"  sing N N 189 
FAD   "O2'" "HO2'" sing N N 190 
FAD   "C3'" "O3'"  sing N N 191 
FAD   "C3'" "C4'"  sing N N 192 
FAD   "C3'" "H3'"  sing N N 193 
FAD   "O3'" "HO3'" sing N N 194 
FAD   "C4'" "O4'"  sing N N 195 
FAD   "C4'" "C5'"  sing N N 196 
FAD   "C4'" "H4'"  sing N N 197 
FAD   "O4'" "HO4'" sing N N 198 
FAD   "C5'" "O5'"  sing N N 199 
FAD   "C5'" "H5'1" sing N N 200 
FAD   "C5'" "H5'2" sing N N 201 
FAD   "O5'" P      sing N N 202 
FAD   P     O1P    doub N N 203 
FAD   P     O2P    sing N N 204 
FAD   P     O3P    sing N N 205 
FAD   O2P   HOP2   sing N N 206 
GLN   N     CA     sing N N 207 
GLN   N     H      sing N N 208 
GLN   N     H2     sing N N 209 
GLN   CA    C      sing N N 210 
GLN   CA    CB     sing N N 211 
GLN   CA    HA     sing N N 212 
GLN   C     O      doub N N 213 
GLN   C     OXT    sing N N 214 
GLN   CB    CG     sing N N 215 
GLN   CB    HB2    sing N N 216 
GLN   CB    HB3    sing N N 217 
GLN   CG    CD     sing N N 218 
GLN   CG    HG2    sing N N 219 
GLN   CG    HG3    sing N N 220 
GLN   CD    OE1    doub N N 221 
GLN   CD    NE2    sing N N 222 
GLN   NE2   HE21   sing N N 223 
GLN   NE2   HE22   sing N N 224 
GLN   OXT   HXT    sing N N 225 
GLU   N     CA     sing N N 226 
GLU   N     H      sing N N 227 
GLU   N     H2     sing N N 228 
GLU   CA    C      sing N N 229 
GLU   CA    CB     sing N N 230 
GLU   CA    HA     sing N N 231 
GLU   C     O      doub N N 232 
GLU   C     OXT    sing N N 233 
GLU   CB    CG     sing N N 234 
GLU   CB    HB2    sing N N 235 
GLU   CB    HB3    sing N N 236 
GLU   CG    CD     sing N N 237 
GLU   CG    HG2    sing N N 238 
GLU   CG    HG3    sing N N 239 
GLU   CD    OE1    doub N N 240 
GLU   CD    OE2    sing N N 241 
GLU   OE2   HE2    sing N N 242 
GLU   OXT   HXT    sing N N 243 
GLY   N     CA     sing N N 244 
GLY   N     H      sing N N 245 
GLY   N     H2     sing N N 246 
GLY   CA    C      sing N N 247 
GLY   CA    HA2    sing N N 248 
GLY   CA    HA3    sing N N 249 
GLY   C     O      doub N N 250 
GLY   C     OXT    sing N N 251 
GLY   OXT   HXT    sing N N 252 
HIS   N     CA     sing N N 253 
HIS   N     H      sing N N 254 
HIS   N     H2     sing N N 255 
HIS   CA    C      sing N N 256 
HIS   CA    CB     sing N N 257 
HIS   CA    HA     sing N N 258 
HIS   C     O      doub N N 259 
HIS   C     OXT    sing N N 260 
HIS   CB    CG     sing N N 261 
HIS   CB    HB2    sing N N 262 
HIS   CB    HB3    sing N N 263 
HIS   CG    ND1    sing Y N 264 
HIS   CG    CD2    doub Y N 265 
HIS   ND1   CE1    doub Y N 266 
HIS   ND1   HD1    sing N N 267 
HIS   CD2   NE2    sing Y N 268 
HIS   CD2   HD2    sing N N 269 
HIS   CE1   NE2    sing Y N 270 
HIS   CE1   HE1    sing N N 271 
HIS   NE2   HE2    sing N N 272 
HIS   OXT   HXT    sing N N 273 
HOH   O     H1     sing N N 274 
HOH   O     H2     sing N N 275 
ILE   N     CA     sing N N 276 
ILE   N     H      sing N N 277 
ILE   N     H2     sing N N 278 
ILE   CA    C      sing N N 279 
ILE   CA    CB     sing N N 280 
ILE   CA    HA     sing N N 281 
ILE   C     O      doub N N 282 
ILE   C     OXT    sing N N 283 
ILE   CB    CG1    sing N N 284 
ILE   CB    CG2    sing N N 285 
ILE   CB    HB     sing N N 286 
ILE   CG1   CD1    sing N N 287 
ILE   CG1   HG12   sing N N 288 
ILE   CG1   HG13   sing N N 289 
ILE   CG2   HG21   sing N N 290 
ILE   CG2   HG22   sing N N 291 
ILE   CG2   HG23   sing N N 292 
ILE   CD1   HD11   sing N N 293 
ILE   CD1   HD12   sing N N 294 
ILE   CD1   HD13   sing N N 295 
ILE   OXT   HXT    sing N N 296 
LEU   N     CA     sing N N 297 
LEU   N     H      sing N N 298 
LEU   N     H2     sing N N 299 
LEU   CA    C      sing N N 300 
LEU   CA    CB     sing N N 301 
LEU   CA    HA     sing N N 302 
LEU   C     O      doub N N 303 
LEU   C     OXT    sing N N 304 
LEU   CB    CG     sing N N 305 
LEU   CB    HB2    sing N N 306 
LEU   CB    HB3    sing N N 307 
LEU   CG    CD1    sing N N 308 
LEU   CG    CD2    sing N N 309 
LEU   CG    HG     sing N N 310 
LEU   CD1   HD11   sing N N 311 
LEU   CD1   HD12   sing N N 312 
LEU   CD1   HD13   sing N N 313 
LEU   CD2   HD21   sing N N 314 
LEU   CD2   HD22   sing N N 315 
LEU   CD2   HD23   sing N N 316 
LEU   OXT   HXT    sing N N 317 
LYS   N     CA     sing N N 318 
LYS   N     H      sing N N 319 
LYS   N     H2     sing N N 320 
LYS   CA    C      sing N N 321 
LYS   CA    CB     sing N N 322 
LYS   CA    HA     sing N N 323 
LYS   C     O      doub N N 324 
LYS   C     OXT    sing N N 325 
LYS   CB    CG     sing N N 326 
LYS   CB    HB2    sing N N 327 
LYS   CB    HB3    sing N N 328 
LYS   CG    CD     sing N N 329 
LYS   CG    HG2    sing N N 330 
LYS   CG    HG3    sing N N 331 
LYS   CD    CE     sing N N 332 
LYS   CD    HD2    sing N N 333 
LYS   CD    HD3    sing N N 334 
LYS   CE    NZ     sing N N 335 
LYS   CE    HE2    sing N N 336 
LYS   CE    HE3    sing N N 337 
LYS   NZ    HZ1    sing N N 338 
LYS   NZ    HZ2    sing N N 339 
LYS   NZ    HZ3    sing N N 340 
LYS   OXT   HXT    sing N N 341 
MET   N     CA     sing N N 342 
MET   N     H      sing N N 343 
MET   N     H2     sing N N 344 
MET   CA    C      sing N N 345 
MET   CA    CB     sing N N 346 
MET   CA    HA     sing N N 347 
MET   C     O      doub N N 348 
MET   C     OXT    sing N N 349 
MET   CB    CG     sing N N 350 
MET   CB    HB2    sing N N 351 
MET   CB    HB3    sing N N 352 
MET   CG    SD     sing N N 353 
MET   CG    HG2    sing N N 354 
MET   CG    HG3    sing N N 355 
MET   SD    CE     sing N N 356 
MET   CE    HE1    sing N N 357 
MET   CE    HE2    sing N N 358 
MET   CE    HE3    sing N N 359 
MET   OXT   HXT    sing N N 360 
PHE   N     CA     sing N N 361 
PHE   N     H      sing N N 362 
PHE   N     H2     sing N N 363 
PHE   CA    C      sing N N 364 
PHE   CA    CB     sing N N 365 
PHE   CA    HA     sing N N 366 
PHE   C     O      doub N N 367 
PHE   C     OXT    sing N N 368 
PHE   CB    CG     sing N N 369 
PHE   CB    HB2    sing N N 370 
PHE   CB    HB3    sing N N 371 
PHE   CG    CD1    doub Y N 372 
PHE   CG    CD2    sing Y N 373 
PHE   CD1   CE1    sing Y N 374 
PHE   CD1   HD1    sing N N 375 
PHE   CD2   CE2    doub Y N 376 
PHE   CD2   HD2    sing N N 377 
PHE   CE1   CZ     doub Y N 378 
PHE   CE1   HE1    sing N N 379 
PHE   CE2   CZ     sing Y N 380 
PHE   CE2   HE2    sing N N 381 
PHE   CZ    HZ     sing N N 382 
PHE   OXT   HXT    sing N N 383 
PRO   N     CA     sing N N 384 
PRO   N     CD     sing N N 385 
PRO   N     H      sing N N 386 
PRO   CA    C      sing N N 387 
PRO   CA    CB     sing N N 388 
PRO   CA    HA     sing N N 389 
PRO   C     O      doub N N 390 
PRO   C     OXT    sing N N 391 
PRO   CB    CG     sing N N 392 
PRO   CB    HB2    sing N N 393 
PRO   CB    HB3    sing N N 394 
PRO   CG    CD     sing N N 395 
PRO   CG    HG2    sing N N 396 
PRO   CG    HG3    sing N N 397 
PRO   CD    HD2    sing N N 398 
PRO   CD    HD3    sing N N 399 
PRO   OXT   HXT    sing N N 400 
SER   N     CA     sing N N 401 
SER   N     H      sing N N 402 
SER   N     H2     sing N N 403 
SER   CA    C      sing N N 404 
SER   CA    CB     sing N N 405 
SER   CA    HA     sing N N 406 
SER   C     O      doub N N 407 
SER   C     OXT    sing N N 408 
SER   CB    OG     sing N N 409 
SER   CB    HB2    sing N N 410 
SER   CB    HB3    sing N N 411 
SER   OG    HG     sing N N 412 
SER   OXT   HXT    sing N N 413 
THR   N     CA     sing N N 414 
THR   N     H      sing N N 415 
THR   N     H2     sing N N 416 
THR   CA    C      sing N N 417 
THR   CA    CB     sing N N 418 
THR   CA    HA     sing N N 419 
THR   C     O      doub N N 420 
THR   C     OXT    sing N N 421 
THR   CB    OG1    sing N N 422 
THR   CB    CG2    sing N N 423 
THR   CB    HB     sing N N 424 
THR   OG1   HG1    sing N N 425 
THR   CG2   HG21   sing N N 426 
THR   CG2   HG22   sing N N 427 
THR   CG2   HG23   sing N N 428 
THR   OXT   HXT    sing N N 429 
TRP   N     CA     sing N N 430 
TRP   N     H      sing N N 431 
TRP   N     H2     sing N N 432 
TRP   CA    C      sing N N 433 
TRP   CA    CB     sing N N 434 
TRP   CA    HA     sing N N 435 
TRP   C     O      doub N N 436 
TRP   C     OXT    sing N N 437 
TRP   CB    CG     sing N N 438 
TRP   CB    HB2    sing N N 439 
TRP   CB    HB3    sing N N 440 
TRP   CG    CD1    doub Y N 441 
TRP   CG    CD2    sing Y N 442 
TRP   CD1   NE1    sing Y N 443 
TRP   CD1   HD1    sing N N 444 
TRP   CD2   CE2    doub Y N 445 
TRP   CD2   CE3    sing Y N 446 
TRP   NE1   CE2    sing Y N 447 
TRP   NE1   HE1    sing N N 448 
TRP   CE2   CZ2    sing Y N 449 
TRP   CE3   CZ3    doub Y N 450 
TRP   CE3   HE3    sing N N 451 
TRP   CZ2   CH2    doub Y N 452 
TRP   CZ2   HZ2    sing N N 453 
TRP   CZ3   CH2    sing Y N 454 
TRP   CZ3   HZ3    sing N N 455 
TRP   CH2   HH2    sing N N 456 
TRP   OXT   HXT    sing N N 457 
TYR   N     CA     sing N N 458 
TYR   N     H      sing N N 459 
TYR   N     H2     sing N N 460 
TYR   CA    C      sing N N 461 
TYR   CA    CB     sing N N 462 
TYR   CA    HA     sing N N 463 
TYR   C     O      doub N N 464 
TYR   C     OXT    sing N N 465 
TYR   CB    CG     sing N N 466 
TYR   CB    HB2    sing N N 467 
TYR   CB    HB3    sing N N 468 
TYR   CG    CD1    doub Y N 469 
TYR   CG    CD2    sing Y N 470 
TYR   CD1   CE1    sing Y N 471 
TYR   CD1   HD1    sing N N 472 
TYR   CD2   CE2    doub Y N 473 
TYR   CD2   HD2    sing N N 474 
TYR   CE1   CZ     doub Y N 475 
TYR   CE1   HE1    sing N N 476 
TYR   CE2   CZ     sing Y N 477 
TYR   CE2   HE2    sing N N 478 
TYR   CZ    OH     sing N N 479 
TYR   OH    HH     sing N N 480 
TYR   OXT   HXT    sing N N 481 
VAL   N     CA     sing N N 482 
VAL   N     H      sing N N 483 
VAL   N     H2     sing N N 484 
VAL   CA    C      sing N N 485 
VAL   CA    CB     sing N N 486 
VAL   CA    HA     sing N N 487 
VAL   C     O      doub N N 488 
VAL   C     OXT    sing N N 489 
VAL   CB    CG1    sing N N 490 
VAL   CB    CG2    sing N N 491 
VAL   CB    HB     sing N N 492 
VAL   CG1   HG11   sing N N 493 
VAL   CG1   HG12   sing N N 494 
VAL   CG1   HG13   sing N N 495 
VAL   CG2   HG21   sing N N 496 
VAL   CG2   HG22   sing N N 497 
VAL   CG2   HG23   sing N N 498 
VAL   OXT   HXT    sing N N 499 
# 
_pdbx_audit_support.funding_organization   'European Cooperation in Science and Technology (COST) action' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           'COZYME (CA21162)' 
_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                    9H8Z 
_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]   0.023629 
_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]   0.010993 
_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]   0.010576 
_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 
P 
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     . PRO   A 1 8   ? -29.889 -9.605  12.691  1.00 58.74 ? 8   PRO   A N     1 
ATOM   2    C CA    . PRO   A 1 8   ? -29.401 -8.239  12.555  1.00 59.15 ? 8   PRO   A CA    1 
ATOM   3    C C     . PRO   A 1 8   ? -28.870 -7.918  11.157  1.00 48.24 ? 8   PRO   A C     1 
ATOM   4    O O     . PRO   A 1 8   ? -28.439 -8.797  10.420  1.00 47.25 ? 8   PRO   A O     1 
ATOM   5    C CB    . PRO   A 1 8   ? -28.300 -8.084  13.622  1.00 60.04 ? 8   PRO   A CB    1 
ATOM   6    C CG    . PRO   A 1 8   ? -28.101 -9.485  14.177  1.00 63.89 ? 8   PRO   A CG    1 
ATOM   7    C CD    . PRO   A 1 8   ? -28.831 -10.430 13.217  1.00 64.25 ? 8   PRO   A CD    1 
ATOM   8    N N     . PHE   A 1 9   ? -28.829 -6.617  10.865  1.00 45.97 ? 9   PHE   A N     1 
ATOM   9    C CA    . PHE   A 1 9   ? -28.852 -6.098  9.510   1.00 37.76 ? 9   PHE   A CA    1 
ATOM   10   C C     . PHE   A 1 9   ? -27.479 -6.236  8.862   1.00 35.61 ? 9   PHE   A C     1 
ATOM   11   O O     . PHE   A 1 9   ? -26.496 -5.701  9.365   1.00 36.86 ? 9   PHE   A O     1 
ATOM   12   C CB    . PHE   A 1 9   ? -29.310 -4.649  9.650   1.00 36.69 ? 9   PHE   A CB    1 
ATOM   13   C CG    . PHE   A 1 9   ? -29.487 -3.921  8.334   1.00 32.54 ? 9   PHE   A CG    1 
ATOM   14   C CD1   . PHE   A 1 9   ? -30.596 -4.161  7.544   1.00 31.26 ? 9   PHE   A CD1   1 
ATOM   15   C CD2   . PHE   A 1 9   ? -28.561 -2.977  7.912   1.00 33.54 ? 9   PHE   A CD2   1 
ATOM   16   C CE1   . PHE   A 1 9   ? -30.766 -3.487  6.346   1.00 33.35 ? 9   PHE   A CE1   1 
ATOM   17   C CE2   . PHE   A 1 9   ? -28.741 -2.305  6.722   1.00 31.01 ? 9   PHE   A CE2   1 
ATOM   18   C CZ    . PHE   A 1 9   ? -29.844 -2.552  5.946   1.00 31.26 ? 9   PHE   A CZ    1 
ATOM   19   N N     . GLU   A 1 10  ? -27.438 -6.915  7.711   1.00 29.64 ? 10  GLU   A N     1 
ATOM   20   C CA    . GLU   A 1 10  ? -26.191 -7.194  7.021   1.00 24.85 ? 10  GLU   A CA    1 
ATOM   21   C C     . GLU   A 1 10  ? -26.245 -6.579  5.630   1.00 25.19 ? 10  GLU   A C     1 
ATOM   22   O O     . GLU   A 1 10  ? -27.167 -6.875  4.859   1.00 23.65 ? 10  GLU   A O     1 
ATOM   23   C CB    . GLU   A 1 10  ? -25.992 -8.703  6.886   1.00 26.35 ? 10  GLU   A CB    1 
ATOM   24   C CG    . GLU   A 1 10  ? -24.937 -9.163  5.881   1.00 26.66 ? 10  GLU   A CG    1 
ATOM   25   C CD    . GLU   A 1 10  ? -23.443 -8.942  6.166   1.00 28.88 ? 10  GLU   A CD    1 
ATOM   26   O OE1   . GLU   A 1 10  ? -22.632 -9.383  5.333   1.00 30.14 ? 10  GLU   A OE1   1 
ATOM   27   O OE2   . GLU   A 1 10  ? -23.069 -8.368  7.204   1.00 31.27 ? 10  GLU   A OE2   1 
ATOM   28   N N     . VAL   A 1 11  ? -25.226 -5.772  5.319   1.00 22.73 ? 11  VAL   A N     1 
ATOM   29   C CA    . VAL   A 1 11  ? -25.096 -5.190  3.995   1.00 21.93 ? 11  VAL   A CA    1 
ATOM   30   C C     . VAL   A 1 11  ? -24.057 -5.970  3.200   1.00 20.82 ? 11  VAL   A C     1 
ATOM   31   O O     . VAL   A 1 11  ? -22.904 -6.104  3.628   1.00 21.05 ? 11  VAL   A O     1 
ATOM   32   C CB    . VAL   A 1 11  ? -24.651 -3.725  4.178   1.00 21.91 ? 11  VAL   A CB    1 
ATOM   33   C CG1   . VAL   A 1 11  ? -24.345 -3.078  2.837   1.00 22.27 ? 11  VAL   A CG1   1 
ATOM   34   C CG2   . VAL   A 1 11  ? -25.642 -2.913  5.011   1.00 22.31 ? 11  VAL   A CG2   1 
ATOM   35   N N     . ALA   A 1 12  ? -24.413 -6.413  1.992   1.00 20.98 ? 12  ALA   A N     1 
ATOM   36   C CA    . ALA   A 1 12  ? -23.439 -6.979  1.080   1.00 20.14 ? 12  ALA   A CA    1 
ATOM   37   C C     . ALA   A 1 12  ? -23.012 -5.904  0.088   1.00 22.12 ? 12  ALA   A C     1 
ATOM   38   O O     . ALA   A 1 12  ? -23.861 -5.404  -0.653  1.00 20.57 ? 12  ALA   A O     1 
ATOM   39   C CB    . ALA   A 1 12  ? -24.010 -8.180  0.362   1.00 19.57 ? 12  ALA   A CB    1 
ATOM   40   N N     . ILE   A 1 13  ? -21.716 -5.583  0.103   1.00 21.09 ? 13  ILE   A N     1 
ATOM   41   C CA    . ILE   A 1 13  ? -21.104 -4.696  -0.878  1.00 20.25 ? 13  ILE   A CA    1 
ATOM   42   C C     . ILE   A 1 13  ? -20.474 -5.571  -1.957  1.00 19.44 ? 13  ILE   A C     1 
ATOM   43   O O     . ILE   A 1 13  ? -19.548 -6.354  -1.714  1.00 19.64 ? 13  ILE   A O     1 
ATOM   44   C CB    . ILE   A 1 13  ? -20.091 -3.740  -0.215  1.00 21.70 ? 13  ILE   A CB    1 
ATOM   45   C CG1   . ILE   A 1 13  ? -20.710 -2.927  0.921   1.00 23.39 ? 13  ILE   A CG1   1 
ATOM   46   C CG2   . ILE   A 1 13  ? -19.444 -2.839  -1.279  1.00 21.93 ? 13  ILE   A CG2   1 
ATOM   47   C CD1   . ILE   A 1 13  ? -19.713 -2.074  1.694   1.00 22.85 ? 13  ILE   A CD1   1 
ATOM   48   N N     . VAL   A 1 14  ? -20.924 -5.407  -3.205  1.00 18.17 ? 14  VAL   A N     1 
ATOM   49   C CA    . VAL   A 1 14  ? -20.363 -6.181  -4.285  1.00 19.10 ? 14  VAL   A CA    1 
ATOM   50   C C     . VAL   A 1 14  ? -19.389 -5.276  -5.028  1.00 21.67 ? 14  VAL   A C     1 
ATOM   51   O O     . VAL   A 1 14  ? -19.829 -4.319  -5.650  1.00 21.45 ? 14  VAL   A O     1 
ATOM   52   C CB    . VAL   A 1 14  ? -21.483 -6.704  -5.219  1.00 19.79 ? 14  VAL   A CB    1 
ATOM   53   C CG1   . VAL   A 1 14  ? -20.881 -7.414  -6.417  1.00 21.73 ? 14  VAL   A CG1   1 
ATOM   54   C CG2   . VAL   A 1 14  ? -22.442 -7.627  -4.476  1.00 21.38 ? 14  VAL   A CG2   1 
ATOM   55   N N     . GLY   A 1 15  ? -18.090 -5.580  -4.929  1.00 20.81 ? 15  GLY   A N     1 
ATOM   56   C CA    . GLY   A 1 15  ? -17.053 -4.779  -5.562  1.00 20.44 ? 15  GLY   A CA    1 
ATOM   57   C C     . GLY   A 1 15  ? -16.304 -3.869  -4.596  1.00 20.26 ? 15  GLY   A C     1 
ATOM   58   O O     . GLY   A 1 15  ? -16.877 -2.954  -3.993  1.00 20.66 ? 15  GLY   A O     1 
ATOM   59   N N     . GLY   A 1 16  ? -14.980 -4.056  -4.555  1.00 20.69 ? 16  GLY   A N     1 
ATOM   60   C CA    . GLY   A 1 16  ? -14.105 -3.248  -3.722  1.00 23.43 ? 16  GLY   A CA    1 
ATOM   61   C C     . GLY   A 1 16  ? -13.349 -2.237  -4.569  1.00 23.83 ? 16  GLY   A C     1 
ATOM   62   O O     . GLY   A 1 16  ? -12.120 -2.199  -4.543  1.00 23.73 ? 16  GLY   A O     1 
ATOM   63   N N     . GLY   A 1 17  ? -14.107 -1.441  -5.332  1.00 21.27 ? 17  GLY   A N     1 
ATOM   64   C CA    . GLY   A 1 17  ? -13.550 -0.262  -5.978  1.00 21.43 ? 17  GLY   A CA    1 
ATOM   65   C C     . GLY   A 1 17  ? -13.571 0.927   -5.031  1.00 22.28 ? 17  GLY   A C     1 
ATOM   66   O O     . GLY   A 1 17  ? -13.794 0.777   -3.841  1.00 22.35 ? 17  GLY   A O     1 
ATOM   67   N N     . ILE   A 1 18  ? -13.409 2.133   -5.589  1.00 21.83 ? 18  ILE   A N     1 
ATOM   68   C CA    . ILE   A 1 18  ? -13.420 3.332   -4.771  1.00 21.29 ? 18  ILE   A CA    1 
ATOM   69   C C     . ILE   A 1 18  ? -14.787 3.501   -4.103  1.00 19.69 ? 18  ILE   A C     1 
ATOM   70   O O     . ILE   A 1 18  ? -14.844 3.748   -2.896  1.00 20.10 ? 18  ILE   A O     1 
ATOM   71   C CB    . ILE   A 1 18  ? -13.020 4.580   -5.590  1.00 21.19 ? 18  ILE   A CB    1 
ATOM   72   C CG1   . ILE   A 1 18  ? -11.519 4.512   -5.952  1.00 26.04 ? 18  ILE   A CG1   1 
ATOM   73   C CG2   . ILE   A 1 18  ? -13.325 5.845   -4.785  1.00 21.47 ? 18  ILE   A CG2   1 
ATOM   74   C CD1   . ILE   A 1 18  ? -11.099 5.520   -6.985  1.00 29.36 ? 18  ILE   A CD1   1 
ATOM   75   N N     . THR   A 1 19  ? -15.879 3.326   -4.867  1.00 17.58 ? 19  THR   A N     1 
ATOM   76   C CA    . THR   A 1 19  ? -17.231 3.443   -4.318  1.00 18.46 ? 19  THR   A CA    1 
ATOM   77   C C     . THR   A 1 19  ? -17.405 2.457   -3.157  1.00 18.74 ? 19  THR   A C     1 
ATOM   78   O O     . THR   A 1 19  ? -17.827 2.851   -2.055  1.00 19.45 ? 19  THR   A O     1 
ATOM   79   C CB    . THR   A 1 19  ? -18.268 3.199   -5.415  1.00 20.04 ? 19  THR   A CB    1 
ATOM   80   O OG1   . THR   A 1 19  ? -18.067 4.146   -6.477  1.00 18.85 ? 19  THR   A OG1   1 
ATOM   81   C CG2   . THR   A 1 19  ? -19.694 3.356   -4.934  1.00 20.36 ? 19  THR   A CG2   1 
ATOM   82   N N     . GLY   A 1 20  ? -17.125 1.178   -3.420  1.00 18.48 ? 20  GLY   A N     1 
ATOM   83   C CA    . GLY   A 1 20  ? -17.396 0.117   -2.439  1.00 18.50 ? 20  GLY   A CA    1 
ATOM   84   C C     . GLY   A 1 20  ? -16.545 0.270   -1.167  1.00 21.01 ? 20  GLY   A C     1 
ATOM   85   O O     . GLY   A 1 20  ? -17.012 0.055   -0.049  1.00 20.34 ? 20  GLY   A O     1 
ATOM   86   N N     . LEU   A 1 21  ? -15.281 0.606   -1.339  1.00 20.98 ? 21  LEU   A N     1 
ATOM   87   C CA    . LEU   A 1 21  ? -14.375 0.778   -0.202  1.00 21.49 ? 21  LEU   A CA    1 
ATOM   88   C C     . LEU   A 1 21  ? -14.765 1.995   0.622   1.00 20.70 ? 21  LEU   A C     1 
ATOM   89   O O     . LEU   A 1 21  ? -14.718 1.953   1.862   1.00 20.32 ? 21  LEU   A O     1 
ATOM   90   C CB    . LEU   A 1 21  ? -12.944 0.901   -0.709  1.00 22.23 ? 21  LEU   A CB    1 
ATOM   91   C CG    . LEU   A 1 21  ? -12.375 -0.322  -1.426  1.00 24.55 ? 21  LEU   A CG    1 
ATOM   92   C CD1   . LEU   A 1 21  ? -11.017 0.034   -2.035  1.00 27.96 ? 21  LEU   A CD1   1 
ATOM   93   C CD2   . LEU   A 1 21  ? -12.271 -1.506  -0.493  1.00 25.93 ? 21  LEU   A CD2   1 
ATOM   94   N N     . ALA   A 1 22  ? -15.126 3.092   -0.053  1.00 21.16 ? 22  ALA   A N     1 
ATOM   95   C CA    . ALA   A 1 22  ? -15.575 4.285   0.650   1.00 20.49 ? 22  ALA   A CA    1 
ATOM   96   C C     . ALA   A 1 22  ? -16.808 3.988   1.521   1.00 22.79 ? 22  ALA   A C     1 
ATOM   97   O O     . ALA   A 1 22  ? -16.875 4.350   2.710   1.00 20.34 ? 22  ALA   A O     1 
ATOM   98   C CB    . ALA   A 1 22  ? -15.830 5.382   -0.381  1.00 20.91 ? 22  ALA   A CB    1 
ATOM   99   N N     . LEU   A 1 23  ? -17.799 3.294   0.932   1.00 22.11 ? 23  LEU   A N     1 
ATOM   100  C CA    . LEU   A 1 23  ? -19.001 2.881   1.632   1.00 21.75 ? 23  LEU   A CA    1 
ATOM   101  C C     . LEU   A 1 23  ? -18.616 2.019   2.826   1.00 19.49 ? 23  LEU   A C     1 
ATOM   102  O O     . LEU   A 1 23  ? -19.117 2.267   3.946   1.00 20.63 ? 23  LEU   A O     1 
ATOM   103  C CB    . LEU   A 1 23  ? -19.932 2.093   0.706   1.00 21.53 ? 23  LEU   A CB    1 
ATOM   104  C CG    . LEU   A 1 23  ? -21.198 1.497   1.335   1.00 20.55 ? 23  LEU   A CG    1 
ATOM   105  C CD1   . LEU   A 1 23  ? -22.035 2.530   2.036   1.00 19.43 ? 23  LEU   A CD1   1 
ATOM   106  C CD2   . LEU   A 1 23  ? -21.985 0.782   0.229   1.00 20.92 ? 23  LEU   A CD2   1 
ATOM   107  N N     . ALA   A 1 24  ? -17.717 1.056   2.582   1.00 18.74 ? 24  ALA   A N     1 
ATOM   108  C CA    . ALA   A 1 24  ? -17.313 0.137   3.641   1.00 20.56 ? 24  ALA   A CA    1 
ATOM   109  C C     . ALA   A 1 24  ? -16.779 0.893   4.859   1.00 21.24 ? 24  ALA   A C     1 
ATOM   110  O O     . ALA   A 1 24  ? -17.199 0.607   5.990   1.00 21.54 ? 24  ALA   A O     1 
ATOM   111  C CB    . ALA   A 1 24  ? -16.339 -0.871  3.143   1.00 22.55 ? 24  ALA   A CB    1 
ATOM   112  N N     . VAL   A 1 25  ? -15.922 1.895   4.640   1.00 21.54 ? 25  VAL   A N     1 
ATOM   113  C CA    . VAL   A 1 25  ? -15.410 2.646   5.784   1.00 23.35 ? 25  VAL   A CA    1 
ATOM   114  C C     . VAL   A 1 25  ? -16.557 3.386   6.461   1.00 21.89 ? 25  VAL   A C     1 
ATOM   115  O O     . VAL   A 1 25  ? -16.640 3.443   7.707   1.00 21.76 ? 25  VAL   A O     1 
ATOM   116  C CB    . VAL   A 1 25  ? -14.258 3.609   5.435   1.00 22.84 ? 25  VAL   A CB    1 
ATOM   117  C CG1   . VAL   A 1 25  ? -13.857 4.457   6.634   1.00 22.91 ? 25  VAL   A CG1   1 
ATOM   118  C CG2   . VAL   A 1 25  ? -13.066 2.864   4.896   1.00 24.94 ? 25  VAL   A CG2   1 
ATOM   119  N N     . GLY   A 1 26  ? -17.425 4.015   5.654   1.00 20.73 ? 26  GLY   A N     1 
ATOM   120  C CA    . GLY   A 1 26  ? -18.622 4.656   6.174   1.00 21.64 ? 26  GLY   A CA    1 
ATOM   121  C C     . GLY   A 1 26  ? -19.436 3.751   7.099   1.00 22.05 ? 26  GLY   A C     1 
ATOM   122  O O     . GLY   A 1 26  ? -19.872 4.187   8.169   1.00 21.84 ? 26  GLY   A O     1 
ATOM   123  N N     . LEU   A 1 27  ? -19.671 2.503   6.672   1.00 19.07 ? 27  LEU   A N     1 
ATOM   124  C CA    . LEU   A 1 27  ? -20.473 1.577   7.475   1.00 20.73 ? 27  LEU   A CA    1 
ATOM   125  C C     . LEU   A 1 27  ? -19.729 1.173   8.745   1.00 23.33 ? 27  LEU   A C     1 
ATOM   126  O O     . LEU   A 1 27  ? -20.328 1.153   9.834   1.00 22.70 ? 27  LEU   A O     1 
ATOM   127  C CB    . LEU   A 1 27  ? -20.792 0.376   6.599   1.00 21.94 ? 27  LEU   A CB    1 
ATOM   128  C CG    . LEU   A 1 27  ? -21.748 0.679   5.438   1.00 20.71 ? 27  LEU   A CG    1 
ATOM   129  C CD1   . LEU   A 1 27  ? -22.058 -0.590  4.676   1.00 22.68 ? 27  LEU   A CD1   1 
ATOM   130  C CD2   . LEU   A 1 27  ? -23.018 1.376   5.854   1.00 22.71 ? 27  LEU   A CD2   1 
ATOM   131  N N     . LEU   A 1 28  ? -18.429 0.898   8.588   1.00 23.80 ? 28  LEU   A N     1 
ATOM   132  C CA    . LEU   A 1 28  ? -17.579 0.509   9.718   1.00 23.49 ? 28  LEU   A CA    1 
ATOM   133  C C     . LEU   A 1 28  ? -17.670 1.558   10.820  1.00 23.40 ? 28  LEU   A C     1 
ATOM   134  O O     . LEU   A 1 28  ? -17.879 1.235   12.005  1.00 24.07 ? 28  LEU   A O     1 
ATOM   135  C CB    . LEU   A 1 28  ? -16.148 0.291   9.244   1.00 25.01 ? 28  LEU   A CB    1 
ATOM   136  C CG    . LEU   A 1 28  ? -15.176 -0.273  10.283  1.00 35.84 ? 28  LEU   A CG    1 
ATOM   137  C CD1   . LEU   A 1 28  ? -15.549 -1.732  10.556  1.00 37.24 ? 28  LEU   A CD1   1 
ATOM   138  C CD2   . LEU   A 1 28  ? -13.738 -0.147  9.789   1.00 38.06 ? 28  LEU   A CD2   1 
ATOM   139  N N     . LYS   A 1 29  ? -17.589 2.830   10.440  1.00 22.62 ? 29  LYS   A N     1 
ATOM   140  C CA    . LYS   A 1 29  ? -17.571 3.909   11.419  1.00 24.41 ? 29  LYS   A CA    1 
ATOM   141  C C     . LYS   A 1 29  ? -18.941 4.185   12.048  1.00 27.47 ? 29  LYS   A C     1 
ATOM   142  O O     . LYS   A 1 29  ? -19.036 4.848   13.091  1.00 27.30 ? 29  LYS   A O     1 
ATOM   143  C CB    . LYS   A 1 29  ? -16.916 5.108   10.738  1.00 24.34 ? 29  LYS   A CB    1 
ATOM   144  C CG    . LYS   A 1 29  ? -15.478 4.839   10.351  1.00 26.74 ? 29  LYS   A CG    1 
ATOM   145  C CD    . LYS   A 1 29  ? -14.496 4.736   11.523  1.00 29.95 ? 29  LYS   A CD    1 
ATOM   146  C CE    . LYS   A 1 29  ? -13.068 4.653   11.074  1.00 33.54 ? 29  LYS   A CE    1 
ATOM   147  N NZ    . LYS   A 1 29  ? -12.164 4.747   12.222  1.00 36.24 ? 29  LYS   A NZ    1 
ATOM   148  N N     . ARG   A 1 30  ? -19.995 3.636   11.444  1.00 23.24 ? 30  ARG   A N     1 
ATOM   149  C CA    . ARG   A 1 30  ? -21.350 3.723   11.952  1.00 24.15 ? 30  ARG   A CA    1 
ATOM   150  C C     . ARG   A 1 30  ? -21.823 2.397   12.553  1.00 23.03 ? 30  ARG   A C     1 
ATOM   151  O O     . ARG   A 1 30  ? -22.998 2.274   12.902  1.00 22.88 ? 30  ARG   A O     1 
ATOM   152  C CB    . ARG   A 1 30  ? -22.237 4.133   10.768  1.00 21.15 ? 30  ARG   A CB    1 
ATOM   153  C CG    . ARG   A 1 30  ? -22.021 5.587   10.362  1.00 21.46 ? 30  ARG   A CG    1 
ATOM   154  C CD    . ARG   A 1 30  ? -22.732 5.901   9.063   1.00 22.52 ? 30  ARG   A CD    1 
ATOM   155  N NE    . ARG   A 1 30  ? -22.540 7.284   8.625   1.00 24.28 ? 30  ARG   A NE    1 
ATOM   156  C CZ    . ARG   A 1 30  ? -21.410 7.802   8.115   1.00 23.06 ? 30  ARG   A CZ    1 
ATOM   157  N NH1   . ARG   A 1 30  ? -20.340 7.055   7.875   1.00 22.34 ? 30  ARG   A NH1   1 
ATOM   158  N NH2   . ARG   A 1 30  ? -21.346 9.093   7.868   1.00 22.07 ? 30  ARG   A NH2   1 
ATOM   159  N N     . ASN   A 1 31  ? -20.914 1.428   12.677  1.00 22.29 ? 31  ASN   A N     1 
ATOM   160  C CA    . ASN   A 1 31  ? -21.203 0.157   13.316  1.00 22.63 ? 31  ASN   A CA    1 
ATOM   161  C C     . ASN   A 1 31  ? -22.348 -0.534  12.575  1.00 23.75 ? 31  ASN   A C     1 
ATOM   162  O O     . ASN   A 1 31  ? -23.241 -1.080  13.196  1.00 23.29 ? 31  ASN   A O     1 
ATOM   163  C CB    . ASN   A 1 31  ? -21.452 0.355   14.812  1.00 23.36 ? 31  ASN   A CB    1 
ATOM   164  C CG    . ASN   A 1 31  ? -21.534 -0.960  15.554  1.00 24.86 ? 31  ASN   A CG    1 
ATOM   165  O OD1   . ASN   A 1 31  ? -20.789 -1.889  15.227  1.00 25.48 ? 31  ASN   A OD1   1 
ATOM   166  N ND2   . ASN   A 1 31  ? -22.449 -1.069  16.513  1.00 25.86 ? 31  ASN   A ND2   1 
ATOM   167  N N     . VAL   A 1 32  ? -22.268 -0.551  11.232  1.00 20.95 ? 32  VAL   A N     1 
ATOM   168  C CA    . VAL   A 1 32  ? -23.191 -1.300  10.408  1.00 21.81 ? 32  VAL   A CA    1 
ATOM   169  C C     . VAL   A 1 32  ? -22.455 -2.515  9.862   1.00 20.88 ? 32  VAL   A C     1 
ATOM   170  O O     . VAL   A 1 32  ? -21.397 -2.391  9.274   1.00 22.06 ? 32  VAL   A O     1 
ATOM   171  C CB    . VAL   A 1 32  ? -23.738 -0.439  9.255   1.00 22.56 ? 32  VAL   A CB    1 
ATOM   172  C CG1   . VAL   A 1 32  ? -24.687 -1.232  8.358   1.00 22.79 ? 32  VAL   A CG1   1 
ATOM   173  C CG2   . VAL   A 1 32  ? -24.416 0.832   9.751   1.00 24.13 ? 32  VAL   A CG2   1 
ATOM   174  N N     . SER   A 1 33  ? -23.050 -3.683  10.057  1.00 21.89 ? 33  SER   A N     1 
ATOM   175  C CA    . SER   A 1 33  ? -22.474 -4.946  9.644   1.00 22.78 ? 33  SER   A CA    1 
ATOM   176  C C     . SER   A 1 33  ? -22.467 -5.037  8.123   1.00 21.84 ? 33  SER   A C     1 
ATOM   177  O O     . SER   A 1 33  ? -23.490 -4.733  7.516   1.00 22.08 ? 33  SER   A O     1 
ATOM   178  C CB    . SER   A 1 33  ? -23.242 -6.093  10.236  1.00 25.32 ? 33  SER   A CB    1 
ATOM   179  O OG    . SER   A 1 33  ? -22.734 -7.330  9.755   1.00 29.31 ? 33  SER   A OG    1 
ATOM   180  N N     . PHE   A 1 34  ? -21.305 -5.376  7.553   1.00 22.67 ? 34  PHE   A N     1 
ATOM   181  C CA    . PHE   A 1 34  ? -21.185 -5.536  6.109   1.00 23.82 ? 34  PHE   A CA    1 
ATOM   182  C C     . PHE   A 1 34  ? -20.117 -6.566  5.766   1.00 24.35 ? 34  PHE   A C     1 
ATOM   183  O O     . PHE   A 1 34  ? -19.270 -6.932  6.590   1.00 26.97 ? 34  PHE   A O     1 
ATOM   184  C CB    . PHE   A 1 34  ? -20.803 -4.219  5.413   1.00 23.41 ? 34  PHE   A CB    1 
ATOM   185  C CG    . PHE   A 1 34  ? -19.373 -3.800  5.699   1.00 22.68 ? 34  PHE   A CG    1 
ATOM   186  C CD1   . PHE   A 1 34  ? -19.058 -3.090  6.855   1.00 21.19 ? 34  PHE   A CD1   1 
ATOM   187  C CD2   . PHE   A 1 34  ? -18.341 -4.110  4.840   1.00 21.49 ? 34  PHE   A CD2   1 
ATOM   188  C CE1   . PHE   A 1 34  ? -17.742 -2.745  7.154   1.00 22.76 ? 34  PHE   A CE1   1 
ATOM   189  C CE2   . PHE   A 1 34  ? -17.033 -3.754  5.136   1.00 21.32 ? 34  PHE   A CE2   1 
ATOM   190  C CZ    . PHE   A 1 34  ? -16.745 -3.056  6.291   1.00 22.97 ? 34  PHE   A CZ    1 
ATOM   191  N N     . THR   A 1 35  ? -20.146 -6.994  4.497   1.00 22.33 ? 35  THR   A N     1 
ATOM   192  C CA    . THR   A 1 35  ? -19.105 -7.766  3.879   1.00 22.65 ? 35  THR   A CA    1 
ATOM   193  C C     . THR   A 1 35  ? -18.869 -7.209  2.477   1.00 23.22 ? 35  THR   A C     1 
ATOM   194  O O     . THR   A 1 35  ? -19.840 -6.973  1.791   1.00 19.86 ? 35  THR   A O     1 
ATOM   195  C CB    . THR   A 1 35  ? -19.541 -9.227  3.761   1.00 25.35 ? 35  THR   A CB    1 
ATOM   196  O OG1   . THR   A 1 35  ? -19.880 -9.730  5.055   1.00 25.02 ? 35  THR   A OG1   1 
ATOM   197  C CG2   . THR   A 1 35  ? -18.435 -10.086 3.195   1.00 24.16 ? 35  THR   A CG2   1 
ATOM   198  N N     . ILE   A 1 36  ? -17.602 -7.104  2.057   1.00 23.52 ? 36  ILE   A N     1 
ATOM   199  C CA    . ILE   A 1 36  ? -17.262 -6.798  0.671   1.00 22.18 ? 36  ILE   A CA    1 
ATOM   200  C C     . ILE   A 1 36  ? -16.988 -8.126  -0.006  1.00 22.46 ? 36  ILE   A C     1 
ATOM   201  O O     . ILE   A 1 36  ? -16.163 -8.904  0.468   1.00 24.18 ? 36  ILE   A O     1 
ATOM   202  C CB    . ILE   A 1 36  ? -16.046 -5.872  0.511   1.00 22.77 ? 36  ILE   A CB    1 
ATOM   203  C CG1   . ILE   A 1 36  ? -16.217 -4.569  1.277   1.00 27.92 ? 36  ILE   A CG1   1 
ATOM   204  C CG2   . ILE   A 1 36  ? -15.722 -5.654  -0.976  1.00 23.44 ? 36  ILE   A CG2   1 
ATOM   205  C CD1   . ILE   A 1 36  ? -14.957 -3.731  1.364   1.00 31.79 ? 36  ILE   A CD1   1 
ATOM   206  N N     . TYR   A 1 37  ? -17.642 -8.311  -1.153  1.00 20.65 ? 37  TYR   A N     1 
ATOM   207  C CA    . TYR   A 1 37  ? -17.389 -9.432  -2.052  1.00 21.67 ? 37  TYR   A CA    1 
ATOM   208  C C     . TYR   A 1 37  ? -16.687 -8.899  -3.297  1.00 22.73 ? 37  TYR   A C     1 
ATOM   209  O O     . TYR   A 1 37  ? -17.275 -8.122  -4.045  1.00 22.94 ? 37  TYR   A O     1 
ATOM   210  C CB    . TYR   A 1 37  ? -18.719 -10.088 -2.416  1.00 21.62 ? 37  TYR   A CB    1 
ATOM   211  C CG    . TYR   A 1 37  ? -19.464 -10.615 -1.195  1.00 21.41 ? 37  TYR   A CG    1 
ATOM   212  C CD1   . TYR   A 1 37  ? -19.053 -11.810 -0.608  1.00 23.77 ? 37  TYR   A CD1   1 
ATOM   213  C CD2   . TYR   A 1 37  ? -20.541 -9.949  -0.641  1.00 23.31 ? 37  TYR   A CD2   1 
ATOM   214  C CE1   . TYR   A 1 37  ? -19.660 -12.291 0.536   1.00 25.35 ? 37  TYR   A CE1   1 
ATOM   215  C CE2   . TYR   A 1 37  ? -21.170 -10.437 0.500   1.00 24.03 ? 37  TYR   A CE2   1 
ATOM   216  C CZ    . TYR   A 1 37  ? -20.733 -11.620 1.078   1.00 23.29 ? 37  TYR   A CZ    1 
ATOM   217  O OH    . TYR   A 1 37  ? -21.338 -12.106 2.207   1.00 24.02 ? 37  TYR   A OH    1 
ATOM   218  N N     . GLU   A 1 38  ? -15.451 -9.342  -3.512  1.00 22.14 ? 38  GLU   A N     1 
ATOM   219  C CA    . GLU   A 1 38  ? -14.617 -8.859  -4.597  1.00 21.67 ? 38  GLU   A CA    1 
ATOM   220  C C     . GLU   A 1 38  ? -14.243 -10.030 -5.480  1.00 21.69 ? 38  GLU   A C     1 
ATOM   221  O O     . GLU   A 1 38  ? -13.726 -11.048 -5.002  1.00 23.18 ? 38  GLU   A O     1 
ATOM   222  C CB    . GLU   A 1 38  ? -13.411 -8.125  -4.018  1.00 23.05 ? 38  GLU   A CB    1 
ATOM   223  C CG    . GLU   A 1 38  ? -12.323 -7.781  -5.027  1.00 23.70 ? 38  GLU   A CG    1 
ATOM   224  C CD    . GLU   A 1 38  ? -12.750 -6.993  -6.251  1.00 25.18 ? 38  GLU   A CD    1 
ATOM   225  O OE1   . GLU   A 1 38  ? -12.434 -7.422  -7.390  1.00 25.43 ? 38  GLU   A OE1   1 
ATOM   226  O OE2   . GLU   A 1 38  ? -13.349 -5.933  -6.059  1.00 21.47 ? 38  GLU   A OE2   1 
ATOM   227  N N     . ARG   A 1 39  ? -14.402 -9.876  -6.788  1.00 22.32 ? 39  ARG   A N     1 
ATOM   228  C CA    . ARG   A 1 39  ? -14.111 -11.002 -7.653  1.00 23.64 ? 39  ARG   A CA    1 
ATOM   229  C C     . ARG   A 1 39  ? -12.605 -11.296 -7.766  1.00 25.91 ? 39  ARG   A C     1 
ATOM   230  O O     . ARG   A 1 39  ? -12.222 -12.441 -7.999  1.00 25.05 ? 39  ARG   A O     1 
ATOM   231  C CB    . ARG   A 1 39  ? -14.721 -10.747 -9.028  1.00 24.83 ? 39  ARG   A CB    1 
ATOM   232  C CG    . ARG   A 1 39  ? -14.082 -9.593  -9.784  1.00 25.79 ? 39  ARG   A CG    1 
ATOM   233  C CD    . ARG   A 1 39  ? -14.642 -9.539  -11.190 1.00 26.96 ? 39  ARG   A CD    1 
ATOM   234  N NE    . ARG   A 1 39  ? -14.224 -8.308  -11.855 1.00 28.78 ? 39  ARG   A NE    1 
ATOM   235  C CZ    . ARG   A 1 39  ? -14.683 -7.867  -13.005 1.00 32.97 ? 39  ARG   A CZ    1 
ATOM   236  N NH1   . ARG   A 1 39  ? -15.556 -8.591  -13.698 1.00 34.66 ? 39  ARG   A NH1   1 
ATOM   237  N NH2   . ARG   A 1 39  ? -14.254 -6.697  -13.443 1.00 32.56 ? 39  ARG   A NH2   1 
ATOM   238  N N     . ALA   A 1 40  ? -11.751 -10.268 -7.690  1.00 24.91 ? 40  ALA   A N     1 
ATOM   239  C CA    . ALA   A 1 40  ? -10.323 -10.441 -7.917  1.00 28.09 ? 40  ALA   A CA    1 
ATOM   240  C C     . ALA   A 1 40  ? -9.643  -11.025 -6.669  1.00 30.59 ? 40  ALA   A C     1 
ATOM   241  O O     . ALA   A 1 40  ? -10.265 -11.100 -5.617  1.00 25.82 ? 40  ALA   A O     1 
ATOM   242  C CB    . ALA   A 1 40  ? -9.719  -9.111  -8.313  1.00 28.62 ? 40  ALA   A CB    1 
ATOM   243  N N     . GLU   A 1 41  ? -8.379  -11.462 -6.799  1.00 31.42 ? 41  GLU   A N     1 
ATOM   244  C CA    . GLU   A 1 41  ? -7.617  -12.020 -5.673  1.00 31.28 ? 41  GLU   A CA    1 
ATOM   245  C C     . GLU   A 1 41  ? -7.139  -10.900 -4.753  1.00 33.27 ? 41  GLU   A C     1 
ATOM   246  O O     . GLU   A 1 41  ? -6.860  -11.108 -3.575  1.00 34.90 ? 41  GLU   A O     1 
ATOM   247  C CB    . GLU   A 1 41  ? -6.434  -12.872 -6.161  1.00 34.85 ? 41  GLU   A CB    1 
ATOM   248  N N     . ASN   A 1 42  ? -7.106  -9.678  -5.285  1.00 33.17 ? 42  ASN   A N     1 
ATOM   249  C CA    . ASN   A 1 42  ? -6.650  -8.506  -4.571  1.00 39.11 ? 42  ASN   A CA    1 
ATOM   250  C C     . ASN   A 1 42  ? -7.146  -7.297  -5.365  1.00 41.75 ? 42  ASN   A C     1 
ATOM   251  O O     . ASN   A 1 42  ? -7.808  -7.465  -6.385  1.00 36.96 ? 42  ASN   A O     1 
ATOM   252  C CB    . ASN   A 1 42  ? -5.133  -8.546  -4.422  1.00 41.66 ? 42  ASN   A CB    1 
ATOM   253  C CG    . ASN   A 1 42  ? -4.479  -8.628  -5.778  1.00 42.30 ? 42  ASN   A CG    1 
ATOM   254  O OD1   . ASN   A 1 42  ? -4.717  -7.761  -6.624  1.00 44.81 ? 42  ASN   A OD1   1 
ATOM   255  N ND2   . ASN   A 1 42  ? -3.729  -9.688  -6.036  1.00 46.50 ? 42  ASN   A ND2   1 
ATOM   256  N N     . PHE   A 1 43  ? -6.814  -6.077  -4.937  1.00 43.86 ? 43  PHE   A N     1 
ATOM   257  C CA    . PHE   A 1 43  ? -7.364  -4.910  -5.607  1.00 44.30 ? 43  PHE   A CA    1 
ATOM   258  C C     . PHE   A 1 43  ? -6.483  -4.427  -6.761  1.00 46.94 ? 43  PHE   A C     1 
ATOM   259  O O     . PHE   A 1 43  ? -6.743  -3.359  -7.322  1.00 52.39 ? 43  PHE   A O     1 
ATOM   260  C CB    . PHE   A 1 43  ? -7.616  -3.864  -4.526  1.00 41.71 ? 43  PHE   A CB    1 
ATOM   261  C CG    . PHE   A 1 43  ? -8.762  -4.226  -3.596  1.00 38.23 ? 43  PHE   A CG    1 
ATOM   262  C CD1   . PHE   A 1 43  ? -9.986  -4.674  -4.095  1.00 39.44 ? 43  PHE   A CD1   1 
ATOM   263  C CD2   . PHE   A 1 43  ? -8.627  -4.093  -2.217  1.00 34.39 ? 43  PHE   A CD2   1 
ATOM   264  C CE1   . PHE   A 1 43  ? -11.028 -4.988  -3.230  1.00 36.86 ? 43  PHE   A CE1   1 
ATOM   265  C CE2   . PHE   A 1 43  ? -9.673  -4.394  -1.360  1.00 35.24 ? 43  PHE   A CE2   1 
ATOM   266  C CZ    . PHE   A 1 43  ? -10.873 -4.858  -1.866  1.00 37.39 ? 43  PHE   A CZ    1 
ATOM   267  N N     . GLY   A 1 44  ? -5.464  -5.207  -7.142  1.00 46.84 ? 44  GLY   A N     1 
ATOM   268  C CA    . GLY   A 1 44  ? -4.686  -4.898  -8.333  1.00 50.61 ? 44  GLY   A CA    1 
ATOM   269  C C     . GLY   A 1 44  ? -3.833  -3.641  -8.148  1.00 49.83 ? 44  GLY   A C     1 
ATOM   270  O O     . GLY   A 1 44  ? -3.487  -3.278  -7.024  1.00 44.89 ? 44  GLY   A O     1 
ATOM   271  N N     . GLU   A 1 45  ? -3.490  -2.985  -9.263  1.00 46.28 ? 45  GLU   A N     1 
ATOM   272  C CA    . GLU   A 1 45  ? -2.468  -1.948  -9.251  1.00 50.86 ? 45  GLU   A CA    1 
ATOM   273  C C     . GLU   A 1 45  ? -2.737  -0.887  -10.322 1.00 50.72 ? 45  GLU   A C     1 
ATOM   274  O O     . GLU   A 1 45  ? -1.813  -0.193  -10.750 1.00 49.29 ? 45  GLU   A O     1 
ATOM   275  C CB    . GLU   A 1 45  ? -1.090  -2.596  -9.431  1.00 54.24 ? 45  GLU   A CB    1 
ATOM   276  N N     . LEU   A 1 46  ? -4.006  -0.707  -10.715 1.00 46.58 ? 46  LEU   A N     1 
ATOM   277  C CA    . LEU   A 1 46  ? -4.329  0.272   -11.739 1.00 44.37 ? 46  LEU   A CA    1 
ATOM   278  C C     . LEU   A 1 46  ? -3.953  1.666   -11.233 1.00 44.37 ? 46  LEU   A C     1 
ATOM   279  O O     . LEU   A 1 46  ? -4.439  2.106   -10.197 1.00 39.45 ? 46  LEU   A O     1 
ATOM   280  C CB    . LEU   A 1 46  ? -5.807  0.176   -12.110 1.00 52.86 ? 46  LEU   A CB    1 
ATOM   281  C CG    . LEU   A 1 46  ? -6.258  1.053   -13.285 1.00 54.23 ? 46  LEU   A CG    1 
ATOM   282  C CD1   . LEU   A 1 46  ? -5.453  0.735   -14.547 1.00 53.88 ? 46  LEU   A CD1   1 
ATOM   283  C CD2   . LEU   A 1 46  ? -7.753  0.899   -13.527 1.00 54.30 ? 46  LEU   A CD2   1 
ATOM   284  N N     . GLY   A 1 47  ? -3.067  2.356   -11.964 1.00 44.83 ? 47  GLY   A N     1 
ATOM   285  C CA    . GLY   A 1 47  ? -2.442  3.570   -11.458 1.00 42.95 ? 47  GLY   A CA    1 
ATOM   286  C C     . GLY   A 1 47  ? -3.009  4.843   -12.087 1.00 41.48 ? 47  GLY   A C     1 
ATOM   287  O O     . GLY   A 1 47  ? -2.427  5.924   -11.913 1.00 37.70 ? 47  GLY   A O     1 
ATOM   288  N N     . VAL   A 1 48  ? -4.166  4.715   -12.764 1.00 37.18 ? 48  VAL   A N     1 
ATOM   289  C CA    . VAL   A 1 48  ? -4.784  5.827   -13.464 1.00 34.22 ? 48  VAL   A CA    1 
ATOM   290  C C     . VAL   A 1 48  ? -4.953  6.991   -12.505 1.00 33.11 ? 48  VAL   A C     1 
ATOM   291  O O     . VAL   A 1 48  ? -5.266  6.808   -11.327 1.00 37.90 ? 48  VAL   A O     1 
ATOM   292  C CB    . VAL   A 1 48  ? -6.131  5.457   -14.112 1.00 40.45 ? 48  VAL   A CB    1 
ATOM   293  C CG1   . VAL   A 1 48  ? -5.952  4.442   -15.235 1.00 40.70 ? 48  VAL   A CG1   1 
ATOM   294  C CG2   . VAL   A 1 48  ? -7.167  4.975   -13.094 1.00 36.31 ? 48  VAL   A CG2   1 
ATOM   295  N N     . GLY   A 1 49  ? -4.715  8.195   -13.023 1.00 32.76 ? 49  GLY   A N     1 
ATOM   296  C CA    . GLY   A 1 49  ? -4.955  9.409   -12.279 1.00 33.33 ? 49  GLY   A CA    1 
ATOM   297  C C     . GLY   A 1 49  ? -6.447  9.751   -12.276 1.00 37.77 ? 49  GLY   A C     1 
ATOM   298  O O     . GLY   A 1 49  ? -7.074  9.782   -13.334 1.00 35.55 ? 49  GLY   A O     1 
ATOM   299  N N     . ILE   A 1 50  ? -6.993  9.969   -11.074 1.00 31.95 ? 50  ILE   A N     1 
ATOM   300  C CA    . ILE   A 1 50  ? -8.347  10.457  -10.907 1.00 29.66 ? 50  ILE   A CA    1 
ATOM   301  C C     . ILE   A 1 50  ? -8.300  11.772  -10.146 1.00 29.54 ? 50  ILE   A C     1 
ATOM   302  O O     . ILE   A 1 50  ? -7.609  11.889  -9.131  1.00 32.43 ? 50  ILE   A O     1 
ATOM   303  C CB    . ILE   A 1 50  ? -9.204  9.412   -10.189 1.00 30.06 ? 50  ILE   A CB    1 
ATOM   304  C CG1   . ILE   A 1 50  ? -9.130  8.073   -10.904 1.00 30.12 ? 50  ILE   A CG1   1 
ATOM   305  C CG2   . ILE   A 1 50  ? -10.648 9.895   -10.028 1.00 29.63 ? 50  ILE   A CG2   1 
ATOM   306  C CD1   . ILE   A 1 50  ? -9.801  6.965   -10.134 1.00 30.18 ? 50  ILE   A CD1   1 
ATOM   307  N N     . THR   A 1 51  ? -9.028  12.760  -10.671 1.00 24.57 ? 51  THR   A N     1 
ATOM   308  C CA    . THR   A 1 51  ? -9.149  14.068  -10.071 1.00 29.00 ? 51  THR   A CA    1 
ATOM   309  C C     . THR   A 1 51  ? -10.448 14.117  -9.284  1.00 27.09 ? 51  THR   A C     1 
ATOM   310  O O     . THR   A 1 51  ? -11.517 13.843  -9.828  1.00 30.45 ? 51  THR   A O     1 
ATOM   311  C CB    . THR   A 1 51  ? -9.105  15.136  -11.166 1.00 34.11 ? 51  THR   A CB    1 
ATOM   312  O OG1   . THR   A 1 51  ? -7.880  14.892  -11.843 1.00 37.06 ? 51  THR   A OG1   1 
ATOM   313  C CG2   . THR   A 1 51  ? -9.154  16.537  -10.602 1.00 38.23 ? 51  THR   A CG2   1 
ATOM   314  N N     . PHE   A 1 52  ? -10.345 14.430  -7.991  1.00 26.63 ? 52  PHE   A N     1 
ATOM   315  C CA    . PHE   A 1 52  ? -11.523 14.563  -7.154  1.00 25.08 ? 52  PHE   A CA    1 
ATOM   316  C C     . PHE   A 1 52  ? -11.828 16.033  -6.906  1.00 28.53 ? 52  PHE   A C     1 
ATOM   317  O O     . PHE   A 1 52  ? -10.964 16.825  -6.510  1.00 31.27 ? 52  PHE   A O     1 
ATOM   318  C CB    . PHE   A 1 52  ? -11.384 13.850  -5.812  1.00 26.27 ? 52  PHE   A CB    1 
ATOM   319  C CG    . PHE   A 1 52  ? -11.329 12.345  -6.052  1.00 26.69 ? 52  PHE   A CG    1 
ATOM   320  C CD1   . PHE   A 1 52  ? -10.145 11.740  -6.447  1.00 24.95 ? 52  PHE   A CD1   1 
ATOM   321  C CD2   . PHE   A 1 52  ? -12.471 11.562  -5.925  1.00 25.13 ? 52  PHE   A CD2   1 
ATOM   322  C CE1   . PHE   A 1 52  ? -10.082 10.371  -6.629  1.00 26.73 ? 52  PHE   A CE1   1 
ATOM   323  C CE2   . PHE   A 1 52  ? -12.419 10.197  -6.171  1.00 27.44 ? 52  PHE   A CE2   1 
ATOM   324  C CZ    . PHE   A 1 52  ? -11.219 9.597   -6.492  1.00 27.38 ? 52  PHE   A CZ    1 
ATOM   325  N N     . THR   A 1 53  ? -13.109 16.337  -7.095  1.00 24.10 ? 53  THR   A N     1 
ATOM   326  C CA    . THR   A 1 53  ? -13.623 17.689  -7.001  1.00 24.48 ? 53  THR   A CA    1 
ATOM   327  C C     . THR   A 1 53  ? -14.117 17.998  -5.593  1.00 23.40 ? 53  THR   A C     1 
ATOM   328  O O     . THR   A 1 53  ? -14.204 17.126  -4.717  1.00 24.64 ? 53  THR   A O     1 
ATOM   329  C CB    . THR   A 1 53  ? -14.682 17.832  -8.093  1.00 26.09 ? 53  THR   A CB    1 
ATOM   330  O OG1   . THR   A 1 53  ? -15.693 16.844  -7.961  1.00 26.67 ? 53  THR   A OG1   1 
ATOM   331  C CG2   . THR   A 1 53  ? -14.059 17.639  -9.468  1.00 27.39 ? 53  THR   A CG2   1 
ATOM   332  N N     . PRO   A 1 54  ? -14.392 19.280  -5.273  1.00 22.39 ? 54  PRO   A N     1 
ATOM   333  C CA    . PRO   A 1 54  ? -14.716 19.677  -3.902  1.00 24.05 ? 54  PRO   A CA    1 
ATOM   334  C C     . PRO   A 1 54  ? -15.875 18.905  -3.293  1.00 24.11 ? 54  PRO   A C     1 
ATOM   335  O O     . PRO   A 1 54  ? -15.832 18.577  -2.115  1.00 24.43 ? 54  PRO   A O     1 
ATOM   336  C CB    . PRO   A 1 54  ? -15.093 21.147  -4.033  1.00 26.97 ? 54  PRO   A CB    1 
ATOM   337  C CG    . PRO   A 1 54  ? -14.398 21.592  -5.288  1.00 25.59 ? 54  PRO   A CG    1 
ATOM   338  C CD    . PRO   A 1 54  ? -14.320 20.411  -6.193  1.00 24.89 ? 54  PRO   A CD    1 
ATOM   339  N N     . ASN   A 1 55  ? -16.913 18.653  -4.103  1.00 23.06 ? 55  ASN   A N     1 
ATOM   340  C CA    . ASN   A 1 55  ? -18.067 17.869  -3.665  1.00 22.56 ? 55  ASN   A CA    1 
ATOM   341  C C     . ASN   A 1 55  ? -17.626 16.488  -3.208  1.00 22.36 ? 55  ASN   A C     1 
ATOM   342  O O     . ASN   A 1 55  ? -18.132 15.994  -2.213  1.00 25.36 ? 55  ASN   A O     1 
ATOM   343  C CB    . ASN   A 1 55  ? -19.142 17.756  -4.735  1.00 24.10 ? 55  ASN   A CB    1 
ATOM   344  C CG    . ASN   A 1 55  ? -18.607 17.203  -6.028  1.00 24.63 ? 55  ASN   A CG    1 
ATOM   345  O OD1   . ASN   A 1 55  ? -17.684 17.787  -6.616  1.00 24.51 ? 55  ASN   A OD1   1 
ATOM   346  N ND2   . ASN   A 1 55  ? -19.109 16.057  -6.451  1.00 24.64 ? 55  ASN   A ND2   1 
ATOM   347  N N     . ALA   A 1 56  ? -16.707 15.864  -3.943  1.00 23.13 ? 56  ALA   A N     1 
ATOM   348  C CA    . ALA   A 1 56  ? -16.264 14.520  -3.597  1.00 22.31 ? 56  ALA   A CA    1 
ATOM   349  C C     . ALA   A 1 56  ? -15.461 14.533  -2.302  1.00 21.70 ? 56  ALA   A C     1 
ATOM   350  O O     . ALA   A 1 56  ? -15.635 13.668  -1.458  1.00 23.78 ? 56  ALA   A O     1 
ATOM   351  C CB    . ALA   A 1 56  ? -15.457 13.938  -4.732  1.00 24.56 ? 56  ALA   A CB    1 
ATOM   352  N N     . GLN   A 1 57  ? -14.623 15.560  -2.116  1.00 20.35 ? 57  GLN   A N     1 
ATOM   353  C CA    . GLN   A 1 57  ? -13.863 15.693  -0.886  1.00 21.32 ? 57  GLN   A CA    1 
ATOM   354  C C     . GLN   A 1 57  ? -14.745 15.893  0.345   1.00 23.01 ? 57  GLN   A C     1 
ATOM   355  O O     . GLN   A 1 57  ? -14.486 15.200  1.346   1.00 24.20 ? 57  GLN   A O     1 
ATOM   356  C CB    . GLN   A 1 57  ? -12.755 16.729  -1.039  1.00 21.40 ? 57  GLN   A CB    1 
ATOM   357  C CG    . GLN   A 1 57  ? -11.734 16.285  -2.067  1.00 23.95 ? 57  GLN   A CG    1 
ATOM   358  C CD    . GLN   A 1 57  ? -10.561 17.224  -2.171  1.00 28.26 ? 57  GLN   A CD    1 
ATOM   359  O OE1   . GLN   A 1 57  ? -9.841  17.440  -1.204  1.00 31.83 ? 57  GLN   A OE1   1 
ATOM   360  N NE2   . GLN   A 1 57  ? -10.376 17.775  -3.351  1.00 35.24 ? 57  GLN   A NE2   1 
ATOM   361  N N     . ARG   A 1 58  ? -15.799 16.732  0.255   1.00 20.53 ? 58  ARG   A N     1 
ATOM   362  C CA    . ARG   A 1 58  ? -16.767 16.899  1.334   1.00 22.40 ? 58  ARG   A CA    1 
ATOM   363  C C     . ARG   A 1 58  ? -17.430 15.564  1.670   1.00 21.52 ? 58  ARG   A C     1 
ATOM   364  O O     . ARG   A 1 58  ? -17.645 15.239  2.837   1.00 21.20 ? 58  ARG   A O     1 
ATOM   365  C CB    . ARG   A 1 58  ? -17.863 17.926  1.003   1.00 23.42 ? 58  ARG   A CB    1 
ATOM   366  C CG    . ARG   A 1 58  ? -17.361 19.373  0.951   1.00 23.82 ? 58  ARG   A CG    1 
ATOM   367  C CD    . ARG   A 1 58  ? -18.487 20.412  0.934   1.00 24.92 ? 58  ARG   A CD    1 
ATOM   368  N NE    . ARG   A 1 58  ? -19.248 20.320  -0.315  1.00 25.64 ? 58  ARG   A NE    1 
ATOM   369  C CZ    . ARG   A 1 58  ? -18.863 20.877  -1.465  1.00 25.44 ? 58  ARG   A CZ    1 
ATOM   370  N NH1   . ARG   A 1 58  ? -19.629 20.773  -2.543  1.00 24.24 ? 58  ARG   A NH1   1 
ATOM   371  N NH2   . ARG   A 1 58  ? -17.732 21.559  -1.547  1.00 24.87 ? 58  ARG   A NH2   1 
ATOM   372  N N     . ALA   A 1 59  ? -17.773 14.795  0.642   1.00 22.42 ? 59  ALA   A N     1 
ATOM   373  C CA    . ALA   A 1 59  ? -18.445 13.519  0.843   1.00 21.72 ? 59  ALA   A CA    1 
ATOM   374  C C     . ALA   A 1 59  ? -17.510 12.540  1.543   1.00 22.78 ? 59  ALA   A C     1 
ATOM   375  O O     . ALA   A 1 59  ? -17.965 11.768  2.395   1.00 22.89 ? 59  ALA   A O     1 
ATOM   376  C CB    . ALA   A 1 59  ? -18.918 12.944  -0.466  1.00 23.30 ? 59  ALA   A CB    1 
ATOM   377  N N     . MET   A 1 60  ? -16.223 12.576  1.165   1.00 20.68 ? 60  MET   A N     1 
ATOM   378  C CA    . MET   A 1 60  ? -15.211 11.743  1.806   1.00 24.30 ? 60  MET   A CA    1 
ATOM   379  C C     . MET   A 1 60  ? -15.164 12.052  3.303   1.00 20.94 ? 60  MET   A C     1 
ATOM   380  O O     . MET   A 1 60  ? -15.237 11.147  4.141   1.00 22.38 ? 60  MET   A O     1 
ATOM   381  C CB    . MET   A 1 60  ? -13.818 11.993  1.234   1.00 24.42 ? 60  MET   A CB    1 
ATOM   382  C CG    . MET   A 1 60  ? -13.592 11.612  -0.181  1.00 24.49 ? 60  MET   A CG    1 
ATOM   383  S SD    . MET   A 1 60  ? -11.919 12.071  -0.699  1.00 27.07 ? 60  MET   A SD    1 
ATOM   384  C CE    . MET   A 1 60  ? -11.908 11.834  -2.480  1.00 27.02 ? 60  MET   A CE    1 
ATOM   385  N N     . GLU   A 1 61  ? -15.182 13.331  3.649   1.00 21.48 ? 61  GLU   A N     1 
ATOM   386  C CA    . GLU   A 1 61  ? -15.063 13.711  5.056   1.00 25.56 ? 61  GLU   A CA    1 
ATOM   387  C C     . GLU   A 1 61  ? -16.310 13.292  5.847   1.00 26.35 ? 61  GLU   A C     1 
ATOM   388  O O     . GLU   A 1 61  ? -16.220 12.869  7.012   1.00 26.80 ? 61  GLU   A O     1 
ATOM   389  C CB    . GLU   A 1 61  ? -14.802 15.218  5.108   1.00 30.26 ? 61  GLU   A CB    1 
ATOM   390  C CG    . GLU   A 1 61  ? -14.886 15.843  6.501   1.00 35.96 ? 61  GLU   A CG    1 
ATOM   391  C CD    . GLU   A 1 61  ? -13.648 15.639  7.342   1.00 44.85 ? 61  GLU   A CD    1 
ATOM   392  O OE1   . GLU   A 1 61  ? -12.758 14.925  6.876   1.00 50.57 ? 61  GLU   A OE1   1 
ATOM   393  O OE2   . GLU   A 1 61  ? -13.572 16.186  8.456   1.00 58.66 ? 61  GLU   A OE2   1 
ATOM   394  N N     . ALA   A 1 62  ? -17.484 13.427  5.216   1.00 21.75 ? 62  ALA   A N     1 
ATOM   395  C CA    . ALA   A 1 62  ? -18.754 13.132  5.869   1.00 24.03 ? 62  ALA   A CA    1 
ATOM   396  C C     . ALA   A 1 62  ? -18.849 11.625  6.084   1.00 22.51 ? 62  ALA   A C     1 
ATOM   397  O O     . ALA   A 1 62  ? -19.435 11.214  7.068   1.00 24.76 ? 62  ALA   A O     1 
ATOM   398  C CB    . ALA   A 1 62  ? -19.923 13.690  5.101   1.00 23.60 ? 62  ALA   A CB    1 
ATOM   399  N N     . LEU   A 1 63  ? -18.261 10.819  5.188   1.00 23.70 ? 63  LEU   A N     1 
ATOM   400  C CA    . LEU   A 1 63  ? -18.199 9.377   5.388   1.00 22.00 ? 63  LEU   A CA    1 
ATOM   401  C C     . LEU   A 1 63  ? -17.430 9.103   6.673   1.00 25.59 ? 63  LEU   A C     1 
ATOM   402  O O     . LEU   A 1 63  ? -17.928 8.450   7.578   1.00 24.85 ? 63  LEU   A O     1 
ATOM   403  C CB    . LEU   A 1 63  ? -17.579 8.629   4.207   1.00 23.14 ? 63  LEU   A CB    1 
ATOM   404  C CG    . LEU   A 1 63  ? -18.533 8.341   3.041   1.00 23.86 ? 63  LEU   A CG    1 
ATOM   405  C CD1   . LEU   A 1 63  ? -17.798 8.010   1.771   1.00 23.83 ? 63  LEU   A CD1   1 
ATOM   406  C CD2   . LEU   A 1 63  ? -19.442 7.165   3.411   1.00 22.64 ? 63  LEU   A CD2   1 
ATOM   407  N N     . ASP   A 1 64  ? -16.219 9.643   6.725   1.00 26.12 ? 64  ASP   A N     1 
ATOM   408  C CA    . ASP   A 1 64  ? -15.399 9.626   7.920   1.00 27.70 ? 64  ASP   A CA    1 
ATOM   409  C C     . ASP   A 1 64  ? -14.138 10.432  7.639   1.00 25.39 ? 64  ASP   A C     1 
ATOM   410  O O     . ASP   A 1 64  ? -13.625 10.401  6.523   1.00 23.79 ? 64  ASP   A O     1 
ATOM   411  C CB    . ASP   A 1 64  ? -14.952 8.230   8.316   1.00 26.44 ? 64  ASP   A CB    1 
ATOM   412  C CG    . ASP   A 1 64  ? -14.397 8.170   9.737   1.00 33.09 ? 64  ASP   A CG    1 
ATOM   413  O OD1   . ASP   A 1 64  ? -15.216 8.114   10.685  1.00 34.29 ? 64  ASP   A OD1   1 
ATOM   414  O OD2   . ASP   A 1 64  ? -13.163 8.261   9.888   1.00 30.83 ? 64  ASP   A OD2   1 
ATOM   415  N N     . PRO   A 1 65  ? -13.621 11.204  8.612   1.00 29.45 ? 65  PRO   A N     1 
ATOM   416  C CA    . PRO   A 1 65  ? -12.345 11.903  8.430   1.00 30.47 ? 65  PRO   A CA    1 
ATOM   417  C C     . PRO   A 1 65  ? -11.251 11.007  7.850   1.00 27.62 ? 65  PRO   A C     1 
ATOM   418  O O     . PRO   A 1 65  ? -10.438 11.489  7.081   1.00 27.69 ? 65  PRO   A O     1 
ATOM   419  C CB    . PRO   A 1 65  ? -12.031 12.391  9.840   1.00 30.95 ? 65  PRO   A CB    1 
ATOM   420  C CG    . PRO   A 1 65  ? -13.389 12.630  10.431  1.00 32.33 ? 65  PRO   A CG    1 
ATOM   421  C CD    . PRO   A 1 65  ? -14.245 11.508  9.909   1.00 27.46 ? 65  PRO   A CD    1 
ATOM   422  N N     . CYS   A 1 66  ? -11.255 9.692   8.140   1.00 26.99 ? 66  CYS   A N     1 
ATOM   423  C CA    . CYS   A 1 66  ? -10.169 8.860   7.641   1.00 27.54 ? 66  CYS   A CA    1 
ATOM   424  C C     . CYS   A 1 66  ? -10.274 8.586   6.143   1.00 28.82 ? 66  CYS   A C     1 
ATOM   425  O O     . CYS   A 1 66  ? -9.280  8.245   5.495   1.00 29.84 ? 66  CYS   A O     1 
ATOM   426  C CB    . CYS   A 1 66  ? -9.993  7.587   8.456   1.00 31.44 ? 66  CYS   A CB    1 
ATOM   427  S SG    . CYS   A 1 66  ? -11.248 6.334   8.138   1.00 40.10 ? 66  CYS   A SG    1 
ATOM   428  N N     . VAL   A 1 67  ? -11.479 8.734   5.576   1.00 27.22 ? 67  VAL   A N     1 
ATOM   429  C CA    . VAL   A 1 67  ? -11.615 8.584   4.135   1.00 26.21 ? 67  VAL   A CA    1 
ATOM   430  C C     . VAL   A 1 67  ? -10.946 9.789   3.475   1.00 23.11 ? 67  VAL   A C     1 
ATOM   431  O O     . VAL   A 1 67  ? -10.197 9.639   2.512   1.00 25.45 ? 67  VAL   A O     1 
ATOM   432  C CB    . VAL   A 1 67  ? -13.083 8.428   3.678   1.00 23.26 ? 67  VAL   A CB    1 
ATOM   433  C CG1   . VAL   A 1 67  ? -13.226 8.383   2.162   1.00 24.89 ? 67  VAL   A CG1   1 
ATOM   434  C CG2   . VAL   A 1 67  ? -13.747 7.199   4.289   1.00 24.78 ? 67  VAL   A CG2   1 
ATOM   435  N N     . LEU   A 1 68  ? -11.267 10.997  3.935   1.00 24.91 ? 68  LEU   A N     1 
ATOM   436  C CA    . LEU   A 1 68  ? -10.618 12.178  3.351   1.00 25.11 ? 68  LEU   A CA    1 
ATOM   437  C C     . LEU   A 1 68  ? -9.102  12.108  3.579   1.00 29.38 ? 68  LEU   A C     1 
ATOM   438  O O     . LEU   A 1 68  ? -8.302  12.512  2.726   1.00 29.20 ? 68  LEU   A O     1 
ATOM   439  C CB    . LEU   A 1 68  ? -11.200 13.439  3.987   1.00 24.84 ? 68  LEU   A CB    1 
ATOM   440  C CG    . LEU   A 1 68  ? -10.628 14.759  3.441   1.00 25.99 ? 68  LEU   A CG    1 
ATOM   441  C CD1   . LEU   A 1 68  ? -10.712 14.789  1.920   1.00 26.05 ? 68  LEU   A CD1   1 
ATOM   442  C CD2   . LEU   A 1 68  ? -11.306 15.987  3.999   1.00 30.30 ? 68  LEU   A CD2   1 
ATOM   443  N N     . GLN   A 1 69  ? -8.709  11.668  4.783   1.00 28.79 ? 69  GLN   A N     1 
ATOM   444  C CA    . GLN   A 1 69  ? -7.291  11.551  5.145   1.00 30.03 ? 69  GLN   A CA    1 
ATOM   445  C C     . GLN   A 1 69  ? -6.552  10.603  4.199   1.00 30.00 ? 69  GLN   A C     1 
ATOM   446  O O     . GLN   A 1 69  ? -5.435  10.916  3.747   1.00 33.09 ? 69  GLN   A O     1 
ATOM   447  C CB    . GLN   A 1 69  ? -7.226  11.088  6.597   1.00 33.71 ? 69  GLN   A CB    1 
ATOM   448  C CG    . GLN   A 1 69  ? -5.850  11.157  7.246   1.00 42.42 ? 69  GLN   A CG    1 
ATOM   449  C CD    . GLN   A 1 69  ? -5.905  10.718  8.698   1.00 54.30 ? 69  GLN   A CD    1 
ATOM   450  O OE1   . GLN   A 1 69  ? -6.976  10.405  9.240   1.00 65.50 ? 69  GLN   A OE1   1 
ATOM   451  N NE2   . GLN   A 1 69  ? -4.757  10.710  9.357   1.00 58.01 ? 69  GLN   A NE2   1 
ATOM   452  N N     . SER   A 1 70  ? -7.181  9.448   3.909   1.00 27.73 ? 70  SER   A N     1 
ATOM   453  C CA    . SER   A 1 70  ? -6.669  8.414   3.024   1.00 27.81 ? 70  SER   A CA    1 
ATOM   454  C C     . SER   A 1 70  ? -6.365  9.018   1.659   1.00 30.01 ? 70  SER   A C     1 
ATOM   455  O O     . SER   A 1 70  ? -5.388  8.651   1.005   1.00 29.52 ? 70  SER   A O     1 
ATOM   456  C CB    . SER   A 1 70  ? -7.667  7.263   2.873   1.00 30.77 ? 70  SER   A CB    1 
ATOM   457  O OG    . SER   A 1 70  ? -7.797  6.470   4.049   1.00 29.70 ? 70  SER   A OG    1 
ATOM   458  N N     . PHE   A 1 71  ? -7.244  9.931   1.235   1.00 28.55 ? 71  PHE   A N     1 
ATOM   459  C CA    . PHE   A 1 71  ? -7.094  10.633  -0.023  1.00 27.43 ? 71  PHE   A CA    1 
ATOM   460  C C     . PHE   A 1 71  ? -5.983  11.686  0.065   1.00 25.19 ? 71  PHE   A C     1 
ATOM   461  O O     . PHE   A 1 71  ? -5.110  11.711  -0.811  1.00 27.58 ? 71  PHE   A O     1 
ATOM   462  C CB    . PHE   A 1 71  ? -8.432  11.273  -0.428  1.00 25.87 ? 71  PHE   A CB    1 
ATOM   463  C CG    . PHE   A 1 71  ? -8.328  12.120  -1.684  1.00 26.48 ? 71  PHE   A CG    1 
ATOM   464  C CD1   . PHE   A 1 71  ? -8.050  11.527  -2.902  1.00 26.95 ? 71  PHE   A CD1   1 
ATOM   465  C CD2   . PHE   A 1 71  ? -8.462  13.497  -1.632  1.00 29.17 ? 71  PHE   A CD2   1 
ATOM   466  C CE1   . PHE   A 1 71  ? -7.894  12.295  -4.035  1.00 26.42 ? 71  PHE   A CE1   1 
ATOM   467  C CE2   . PHE   A 1 71  ? -8.345  14.257  -2.780  1.00 25.97 ? 71  PHE   A CE2   1 
ATOM   468  C CZ    . PHE   A 1 71  ? -8.045  13.658  -3.963  1.00 26.29 ? 71  PHE   A CZ    1 
ATOM   469  N N     . THR   A 1 72  ? -6.033  12.566  1.056   1.00 29.36 ? 72  THR   A N     1 
ATOM   470  C CA    . THR   A 1 72  ? -5.096  13.680  1.132   1.00 33.37 ? 72  THR   A CA    1 
ATOM   471  C C     . THR   A 1 72  ? -3.668  13.150  1.319   1.00 35.22 ? 72  THR   A C     1 
ATOM   472  O O     . THR   A 1 72  ? -2.736  13.728  0.750   1.00 37.57 ? 72  THR   A O     1 
ATOM   473  C CB    . THR   A 1 72  ? -5.501  14.672  2.220   1.00 36.44 ? 72  THR   A CB    1 
ATOM   474  O OG1   . THR   A 1 72  ? -5.642  13.974  3.444   1.00 37.97 ? 72  THR   A OG1   1 
ATOM   475  C CG2   . THR   A 1 72  ? -6.825  15.348  1.918   1.00 39.27 ? 72  THR   A CG2   1 
ATOM   476  N N     . ASN   A 1 73  ? -3.523  12.018  2.034   1.00 30.16 ? 73  ASN   A N     1 
ATOM   477  C CA    . ASN   A 1 73  ? -2.237  11.347  2.248   1.00 31.98 ? 73  ASN   A CA    1 
ATOM   478  C C     . ASN   A 1 73  ? -1.508  11.099  0.933   1.00 31.22 ? 73  ASN   A C     1 
ATOM   479  O O     . ASN   A 1 73  ? -0.268  11.070  0.902   1.00 32.24 ? 73  ASN   A O     1 
ATOM   480  C CB    . ASN   A 1 73  ? -2.350  9.981   2.941   1.00 31.43 ? 73  ASN   A CB    1 
ATOM   481  C CG    . ASN   A 1 73  ? -2.757  10.015  4.395   1.00 30.88 ? 73  ASN   A CG    1 
ATOM   482  O OD1   . ASN   A 1 73  ? -3.185  8.980   4.943   1.00 31.14 ? 73  ASN   A OD1   1 
ATOM   483  N ND2   . ASN   A 1 73  ? -2.679  11.173  5.038   1.00 29.57 ? 73  ASN   A ND2   1 
ATOM   484  N N     . VAL   A 1 74  ? -2.262  10.909  -0.161  1.00 26.29 ? 74  VAL   A N     1 
ATOM   485  C CA    . VAL   A 1 74  ? -1.676  10.481  -1.420  1.00 25.44 ? 74  VAL   A CA    1 
ATOM   486  C C     . VAL   A 1 74  ? -1.948  11.450  -2.566  1.00 28.01 ? 74  VAL   A C     1 
ATOM   487  O O     . VAL   A 1 74  ? -1.428  11.246  -3.662  1.00 30.37 ? 74  VAL   A O     1 
ATOM   488  C CB    . VAL   A 1 74  ? -2.111  9.073   -1.858  1.00 26.57 ? 74  VAL   A CB    1 
ATOM   489  C CG1   . VAL   A 1 74  ? -1.559  8.026   -0.904  1.00 27.94 ? 74  VAL   A CG1   1 
ATOM   490  C CG2   . VAL   A 1 74  ? -3.621  8.942   -2.053  1.00 26.32 ? 74  VAL   A CG2   1 
ATOM   491  N N     . ALA   A 1 75  ? -2.746  12.486  -2.340  1.00 28.49 ? 75  ALA   A N     1 
ATOM   492  C CA    . ALA   A 1 75  ? -3.166  13.337  -3.451  1.00 31.31 ? 75  ALA   A CA    1 
ATOM   493  C C     . ALA   A 1 75  ? -2.171  14.484  -3.662  1.00 34.10 ? 75  ALA   A C     1 
ATOM   494  O O     . ALA   A 1 75  ? -1.540  14.930  -2.711  1.00 34.11 ? 75  ALA   A O     1 
ATOM   495  C CB    . ALA   A 1 75  ? -4.571  13.847  -3.184  1.00 34.06 ? 75  ALA   A CB    1 
ATOM   496  N N     . SER   A 1 76  ? -2.061  14.970  -4.909  1.00 38.28 ? 76  SER   A N     1 
ATOM   497  C CA    . SER   A 1 76  ? -1.257  16.152  -5.217  1.00 42.72 ? 76  SER   A CA    1 
ATOM   498  C C     . SER   A 1 76  ? -2.163  17.305  -5.642  1.00 49.08 ? 76  SER   A C     1 
ATOM   499  O O     . SER   A 1 76  ? -3.053  17.127  -6.496  1.00 41.81 ? 76  SER   A O     1 
ATOM   500  C CB    . SER   A 1 76  ? -0.213  15.907  -6.297  1.00 43.28 ? 76  SER   A CB    1 
ATOM   501  O OG    . SER   A 1 76  ? 0.399   14.631  -6.213  1.00 45.32 ? 76  SER   A OG    1 
ATOM   502  N N     . ALA   A 1 77  ? -1.888  18.467  -5.023  1.00 48.96 ? 77  ALA   A N     1 
ATOM   503  C CA    . ALA   A 1 77  ? -2.471  19.753  -5.371  1.00 51.33 ? 77  ALA   A CA    1 
ATOM   504  C C     . ALA   A 1 77  ? -1.740  20.352  -6.576  1.00 52.61 ? 77  ALA   A C     1 
ATOM   505  O O     . ALA   A 1 77  ? -0.509  20.296  -6.696  1.00 46.64 ? 77  ALA   A O     1 
ATOM   506  C CB    . ALA   A 1 77  ? -2.407  20.680  -4.160  1.00 55.87 ? 77  ALA   A CB    1 
ATOM   507  N N     . PRO   A 1 78  ? -2.454  20.943  -7.550  1.00 46.36 ? 78  PRO   A N     1 
ATOM   508  C CA    . PRO   A 1 78  ? -1.769  21.647  -8.632  1.00 43.38 ? 78  PRO   A CA    1 
ATOM   509  C C     . PRO   A 1 78  ? -1.214  22.961  -8.067  1.00 37.29 ? 78  PRO   A C     1 
ATOM   510  O O     . PRO   A 1 78  ? -1.582  23.393  -6.978  1.00 35.90 ? 78  PRO   A O     1 
ATOM   511  C CB    . PRO   A 1 78  ? -2.871  21.808  -9.691  1.00 46.95 ? 78  PRO   A CB    1 
ATOM   512  C CG    . PRO   A 1 78  ? -3.913  20.816  -9.240  1.00 48.70 ? 78  PRO   A CG    1 
ATOM   513  C CD    . PRO   A 1 78  ? -3.912  20.919  -7.723  1.00 49.96 ? 78  PRO   A CD    1 
ATOM   514  N N     . SER   A 1 79  ? -0.278  23.561  -8.783  1.00 40.11 ? 79  SER   A N     1 
ATOM   515  C CA    . SER   A 1 79  ? 0.566   24.594  -8.205  1.00 42.92 ? 79  SER   A CA    1 
ATOM   516  C C     . SER   A 1 79  ? -0.288  25.814  -7.877  1.00 44.11 ? 79  SER   A C     1 
ATOM   517  O O     . SER   A 1 79  ? -0.220  26.353  -6.768  1.00 51.44 ? 79  SER   A O     1 
ATOM   518  C CB    . SER   A 1 79  ? 1.722   24.918  -9.128  1.00 47.81 ? 79  SER   A CB    1 
ATOM   519  N N     . GLY   A 1 80  ? -1.049  26.258  -8.881  1.00 43.29 ? 80  GLY   A N     1 
ATOM   520  C CA    . GLY   A 1 80  ? -2.131  27.209  -8.710  1.00 41.00 ? 80  GLY   A CA    1 
ATOM   521  C C     . GLY   A 1 80  ? -3.442  26.451  -8.900  1.00 43.00 ? 80  GLY   A C     1 
ATOM   522  O O     . GLY   A 1 80  ? -3.455  25.405  -9.568  1.00 43.58 ? 80  GLY   A O     1 
ATOM   523  N N     . GLY   A 1 81  ? -4.520  26.978  -8.308  1.00 32.95 ? 81  GLY   A N     1 
ATOM   524  C CA    . GLY   A 1 81  ? -5.724  26.197  -8.030  1.00 30.41 ? 81  GLY   A CA    1 
ATOM   525  C C     . GLY   A 1 81  ? -6.882  26.530  -8.976  1.00 26.64 ? 81  GLY   A C     1 
ATOM   526  O O     . GLY   A 1 81  ? -7.972  25.997  -8.852  1.00 30.20 ? 81  GLY   A O     1 
ATOM   527  N N     . THR   A 1 82  ? -6.650  27.463  -9.898  1.00 25.76 ? 82  THR   A N     1 
ATOM   528  C CA    . THR   A 1 82  ? -7.631  27.866  -10.893 1.00 27.82 ? 82  THR   A CA    1 
ATOM   529  C C     . THR   A 1 82  ? -7.306  27.136  -12.190 1.00 26.59 ? 82  THR   A C     1 
ATOM   530  O O     . THR   A 1 82  ? -6.132  26.921  -12.449 1.00 25.62 ? 82  THR   A O     1 
ATOM   531  C CB    . THR   A 1 82  ? -7.499  29.375  -11.078 1.00 27.87 ? 82  THR   A CB    1 
ATOM   532  O OG1   . THR   A 1 82  ? -8.058  29.874  -9.863  1.00 28.49 ? 82  THR   A OG1   1 
ATOM   533  C CG2   . THR   A 1 82  ? -8.212  29.907  -12.307 1.00 31.29 ? 82  THR   A CG2   1 
ATOM   534  N N     . ILE   A 1 83  ? -8.332  26.823  -12.985 1.00 25.56 ? 83  ILE   A N     1 
ATOM   535  C CA    . ILE   A 1 83  ? -8.125  26.204  -14.283 1.00 25.15 ? 83  ILE   A CA    1 
ATOM   536  C C     . ILE   A 1 83  ? -8.340  27.285  -15.339 1.00 24.08 ? 83  ILE   A C     1 
ATOM   537  O O     . ILE   A 1 83  ? -9.444  27.832  -15.439 1.00 24.21 ? 83  ILE   A O     1 
ATOM   538  C CB    . ILE   A 1 83  ? -9.044  24.993  -14.473 1.00 25.97 ? 83  ILE   A CB    1 
ATOM   539  C CG1   . ILE   A 1 83  ? -8.777  23.925  -13.404 1.00 27.02 ? 83  ILE   A CG1   1 
ATOM   540  C CG2   . ILE   A 1 83  ? -8.893  24.410  -15.880 1.00 24.65 ? 83  ILE   A CG2   1 
ATOM   541  C CD1   . ILE   A 1 83  ? -10.010 23.242  -12.883 1.00 29.98 ? 83  ILE   A CD1   1 
ATOM   542  N N     . ASN   A 1 84  ? -7.283  27.578  -16.103 1.00 22.66 ? 84  ASN   A N     1 
ATOM   543  C CA    . ASN   A 1 84  ? -7.342  28.537  -17.195 1.00 24.45 ? 84  ASN   A CA    1 
ATOM   544  C C     . ASN   A 1 84  ? -7.826  27.788  -18.441 1.00 23.37 ? 84  ASN   A C     1 
ATOM   545  O O     . ASN   A 1 84  ? -7.181  26.807  -18.826 1.00 22.81 ? 84  ASN   A O     1 
ATOM   546  C CB    . ASN   A 1 84  ? -5.991  29.188  -17.452 1.00 26.84 ? 84  ASN   A CB    1 
ATOM   547  C CG    . ASN   A 1 84  ? -5.530  30.134  -16.361 1.00 31.18 ? 84  ASN   A CG    1 
ATOM   548  O OD1   . ASN   A 1 84  ? -6.225  30.356  -15.366 1.00 35.32 ? 84  ASN   A OD1   1 
ATOM   549  N ND2   . ASN   A 1 84  ? -4.374  30.741  -16.559 1.00 42.18 ? 84  ASN   A ND2   1 
ATOM   550  N N     . PHE   A 1 85  ? -8.961  28.234  -19.001 1.00 23.26 ? 85  PHE   A N     1 
ATOM   551  C CA    . PHE   A 1 85  ? -9.441  27.771  -20.293 1.00 22.23 ? 85  PHE   A CA    1 
ATOM   552  C C     . PHE   A 1 85  ? -8.821  28.650  -21.360 1.00 22.94 ? 85  PHE   A C     1 
ATOM   553  O O     . PHE   A 1 85  ? -8.994  29.877  -21.317 1.00 21.29 ? 85  PHE   A O     1 
ATOM   554  C CB    . PHE   A 1 85  ? -10.973 27.780  -20.347 1.00 22.83 ? 85  PHE   A CB    1 
ATOM   555  C CG    . PHE   A 1 85  ? -11.596 26.598  -19.626 1.00 22.70 ? 85  PHE   A CG    1 
ATOM   556  C CD1   . PHE   A 1 85  ? -11.454 26.458  -18.250 1.00 25.25 ? 85  PHE   A CD1   1 
ATOM   557  C CD2   . PHE   A 1 85  ? -12.314 25.633  -20.310 1.00 24.03 ? 85  PHE   A CD2   1 
ATOM   558  C CE1   . PHE   A 1 85  ? -12.033 25.379  -17.596 1.00 24.19 ? 85  PHE   A CE1   1 
ATOM   559  C CE2   . PHE   A 1 85  ? -12.842 24.542  -19.656 1.00 23.37 ? 85  PHE   A CE2   1 
ATOM   560  C CZ    . PHE   A 1 85  ? -12.724 24.436  -18.297 1.00 25.04 ? 85  PHE   A CZ    1 
ATOM   561  N N     . VAL   A 1 86  ? -8.096  28.012  -22.304 1.00 19.92 ? 86  VAL   A N     1 
ATOM   562  C CA    . VAL   A 1 86  ? -7.478  28.770  -23.370 1.00 21.39 ? 86  VAL   A CA    1 
ATOM   563  C C     . VAL   A 1 86  ? -7.954  28.229  -24.710 1.00 20.71 ? 86  VAL   A C     1 
ATOM   564  O O     . VAL   A 1 86  ? -8.490  27.118  -24.816 1.00 19.93 ? 86  VAL   A O     1 
ATOM   565  C CB    . VAL   A 1 86  ? -5.946  28.786  -23.284 1.00 21.88 ? 86  VAL   A CB    1 
ATOM   566  C CG1   . VAL   A 1 86  ? -5.484  29.317  -21.932 1.00 22.49 ? 86  VAL   A CG1   1 
ATOM   567  C CG2   . VAL   A 1 86  ? -5.341  27.428  -23.620 1.00 20.12 ? 86  VAL   A CG2   1 
ATOM   568  N N     . ASP   A 1 87  ? -7.786  29.081  -25.709 1.00 22.35 ? 87  ASP   A N     1 
ATOM   569  C CA    . ASP   A 1 87  ? -7.931  28.712  -27.110 1.00 24.49 ? 87  ASP   A CA    1 
ATOM   570  C C     . ASP   A 1 87  ? -6.603  28.169  -27.605 1.00 22.12 ? 87  ASP   A C     1 
ATOM   571  O O     . ASP   A 1 87  ? -5.643  28.906  -27.773 1.00 24.74 ? 87  ASP   A O     1 
ATOM   572  C CB    . ASP   A 1 87  ? -8.403  29.902  -27.927 1.00 23.42 ? 87  ASP   A CB    1 
ATOM   573  C CG    . ASP   A 1 87  ? -8.480  29.674  -29.425 1.00 26.05 ? 87  ASP   A CG    1 
ATOM   574  O OD1   . ASP   A 1 87  ? -7.845  28.686  -29.903 1.00 24.35 ? 87  ASP   A OD1   1 
ATOM   575  O OD2   . ASP   A 1 87  ? -9.181  30.488  -30.080 1.00 24.93 ? 87  ASP   A OD2   1 
ATOM   576  N N     . GLY   A 1 88  ? -6.543  26.842  -27.796 1.00 21.07 ? 88  GLY   A N     1 
ATOM   577  C CA    . GLY   A 1 88  ? -5.281  26.166  -28.010 1.00 21.22 ? 88  GLY   A CA    1 
ATOM   578  C C     . GLY   A 1 88  ? -4.795  26.345  -29.450 1.00 20.70 ? 88  GLY   A C     1 
ATOM   579  O O     . GLY   A 1 88  ? -3.672  25.956  -29.749 1.00 23.91 ? 88  GLY   A O     1 
ATOM   580  N N     . VAL   A 1 89  ? -5.650  26.888  -30.324 1.00 21.67 ? 89  VAL   A N     1 
ATOM   581  C CA    . VAL   A 1 89  ? -5.267  27.204  -31.708 1.00 23.54 ? 89  VAL   A CA    1 
ATOM   582  C C     . VAL   A 1 89  ? -4.682  28.621  -31.847 1.00 25.15 ? 89  VAL   A C     1 
ATOM   583  O O     . VAL   A 1 89  ? -3.693  28.806  -32.554 1.00 23.97 ? 89  VAL   A O     1 
ATOM   584  C CB    . VAL   A 1 89  ? -6.533  27.065  -32.572 1.00 23.72 ? 89  VAL   A CB    1 
ATOM   585  C CG1   . VAL   A 1 89  ? -6.360  27.626  -33.989 1.00 28.18 ? 89  VAL   A CG1   1 
ATOM   586  C CG2   . VAL   A 1 89  ? -7.056  25.637  -32.617 1.00 26.76 ? 89  VAL   A CG2   1 
ATOM   587  N N     . ARG   A 1 90  ? -5.286  29.620  -31.193 1.00 26.28 ? 90  ARG   A N     1 
ATOM   588  C CA    . ARG   A 1 90  ? -5.000  31.026  -31.482 1.00 26.26 ? 90  ARG   A CA    1 
ATOM   589  C C     . ARG   A 1 90  ? -4.007  31.647  -30.500 1.00 27.91 ? 90  ARG   A C     1 
ATOM   590  O O     . ARG   A 1 90  ? -3.977  32.864  -30.324 1.00 32.03 ? 90  ARG   A O     1 
ATOM   591  C CB    . ARG   A 1 90  ? -6.299  31.823  -31.506 1.00 26.29 ? 90  ARG   A CB    1 
ATOM   592  C CG    . ARG   A 1 90  ? -7.309  31.388  -32.561 1.00 24.72 ? 90  ARG   A CG    1 
ATOM   593  C CD    . ARG   A 1 90  ? -8.442  32.406  -32.646 1.00 26.41 ? 90  ARG   A CD    1 
ATOM   594  N NE    . ARG   A 1 90  ? -9.431  32.097  -33.677 1.00 24.18 ? 90  ARG   A NE    1 
ATOM   595  C CZ    . ARG   A 1 90  ? -10.431 31.209  -33.596 1.00 25.58 ? 90  ARG   A CZ    1 
ATOM   596  N NH1   . ARG   A 1 90  ? -10.635 30.459  -32.515 1.00 23.06 ? 90  ARG   A NH1   1 
ATOM   597  N NH2   . ARG   A 1 90  ? -11.253 31.079  -34.607 1.00 25.54 ? 90  ARG   A NH2   1 
ATOM   598  N N     . GLU   A 1 91  ? -3.150  30.820  -29.908 1.00 27.62 ? 91  GLU   A N     1 
ATOM   599  C CA    . GLU   A 1 91  ? -1.950  31.259  -29.222 1.00 29.13 ? 91  GLU   A CA    1 
ATOM   600  C C     . GLU   A 1 91  ? -1.194  32.244  -30.116 1.00 33.56 ? 91  GLU   A C     1 
ATOM   601  O O     . GLU   A 1 91  ? -1.044  32.015  -31.311 1.00 30.82 ? 91  GLU   A O     1 
ATOM   602  C CB    . GLU   A 1 91  ? -1.150  29.993  -28.911 1.00 30.40 ? 91  GLU   A CB    1 
ATOM   603  C CG    . GLU   A 1 91  ? 0.078   30.211  -28.035 1.00 31.28 ? 91  GLU   A CG    1 
ATOM   604  C CD    . GLU   A 1 91  ? 0.864   28.930  -27.802 1.00 32.43 ? 91  GLU   A CD    1 
ATOM   605  O OE1   . GLU   A 1 91  ? 0.361   27.878  -28.259 1.00 30.16 ? 91  GLU   A OE1   1 
ATOM   606  O OE2   . GLU   A 1 91  ? 1.961   28.953  -27.177 1.00 33.28 ? 91  GLU   A OE2   1 
ATOM   607  N N     . GLN   A 1 92  ? -0.797  33.375  -29.542 1.00 38.93 ? 92  GLN   A N     1 
ATOM   608  C CA    . GLN   A 1 92  ? -0.239  34.468  -30.323 1.00 46.65 ? 92  GLN   A CA    1 
ATOM   609  C C     . GLN   A 1 92  ? 1.213   34.673  -29.905 1.00 46.86 ? 92  GLN   A C     1 
ATOM   610  O O     . GLN   A 1 92  ? 1.618   34.217  -28.842 1.00 49.85 ? 92  GLN   A O     1 
ATOM   611  C CB    . GLN   A 1 92  ? -1.128  35.696  -30.105 1.00 45.98 ? 92  GLN   A CB    1 
ATOM   612  N N     . GLY   A 1 93  ? 2.007   35.319  -30.770 1.00 56.42 ? 93  GLY   A N     1 
ATOM   613  C CA    . GLY   A 1 93  ? 3.175   36.072  -30.328 1.00 57.02 ? 93  GLY   A CA    1 
ATOM   614  C C     . GLY   A 1 93  ? 4.503   35.442  -30.739 1.00 61.76 ? 93  GLY   A C     1 
ATOM   615  O O     . GLY   A 1 93  ? 5.495   36.151  -30.897 1.00 68.09 ? 93  GLY   A O     1 
ATOM   616  N N     . SER   A 1 94  ? 4.522   34.115  -30.888 1.00 63.16 ? 94  SER   A N     1 
ATOM   617  C CA    . SER   A 1 94  ? 5.745   33.402  -31.216 1.00 62.36 ? 94  SER   A CA    1 
ATOM   618  C C     . SER   A 1 94  ? 5.435   31.926  -31.460 1.00 59.84 ? 94  SER   A C     1 
ATOM   619  O O     . SER   A 1 94  ? 4.356   31.454  -31.106 1.00 65.07 ? 94  SER   A O     1 
ATOM   620  C CB    . SER   A 1 94  ? 6.772   33.591  -30.125 1.00 58.60 ? 94  SER   A CB    1 
ATOM   621  O OG    . SER   A 1 94  ? 7.863   32.695  -30.272 1.00 59.41 ? 94  SER   A OG    1 
ATOM   622  N N     . GLU   A 1 95  ? 6.382   31.229  -32.101 1.00 56.53 ? 95  GLU   A N     1 
ATOM   623  C CA    . GLU   A 1 95  ? 6.295   29.800  -32.372 1.00 54.93 ? 95  GLU   A CA    1 
ATOM   624  C C     . GLU   A 1 95  ? 7.033   29.009  -31.285 1.00 50.75 ? 95  GLU   A C     1 
ATOM   625  O O     . GLU   A 1 95  ? 6.998   27.775  -31.272 1.00 51.76 ? 95  GLU   A O     1 
ATOM   626  C CB    . GLU   A 1 95  ? 6.838   29.568  -33.783 1.00 57.96 ? 95  GLU   A CB    1 
ATOM   627  C CG    . GLU   A 1 95  ? 6.997   28.103  -34.179 1.00 63.35 ? 95  GLU   A CG    1 
ATOM   628  C CD    . GLU   A 1 95  ? 5.742   27.243  -34.245 1.00 66.64 ? 95  GLU   A CD    1 
ATOM   629  O OE1   . GLU   A 1 95  ? 4.589   27.750  -34.297 1.00 55.88 ? 95  GLU   A OE1   1 
ATOM   630  O OE2   . GLU   A 1 95  ? 5.959   26.007  -34.257 1.00 69.99 ? 95  GLU   A OE2   1 
ATOM   631  N N     . ASP   A 1 96  ? 7.709   29.736  -30.386 1.00 46.78 ? 96  ASP   A N     1 
ATOM   632  C CA    . ASP   A 1 96  ? 8.341   29.183  -29.201 1.00 44.06 ? 96  ASP   A CA    1 
ATOM   633  C C     . ASP   A 1 96  ? 7.386   29.410  -28.033 1.00 39.80 ? 96  ASP   A C     1 
ATOM   634  O O     . ASP   A 1 96  ? 7.090   30.561  -27.710 1.00 38.42 ? 96  ASP   A O     1 
ATOM   635  C CB    . ASP   A 1 96  ? 9.666   29.887  -28.949 1.00 44.01 ? 96  ASP   A CB    1 
ATOM   636  C CG    . ASP   A 1 96  ? 10.505  29.392  -27.779 1.00 49.74 ? 96  ASP   A CG    1 
ATOM   637  O OD1   . ASP   A 1 96  ? 9.981   28.588  -26.970 1.00 41.13 ? 96  ASP   A OD1   1 
ATOM   638  O OD2   . ASP   A 1 96  ? 11.686  29.826  -27.685 1.00 43.08 ? 96  ASP   A OD2   1 
ATOM   639  N N     . PRO   A 1 97  ? 6.843   28.360  -27.370 1.00 38.33 ? 97  PRO   A N     1 
ATOM   640  C CA    . PRO   A 1 97  ? 5.805   28.587  -26.366 1.00 35.39 ? 97  PRO   A CA    1 
ATOM   641  C C     . PRO   A 1 97  ? 6.344   29.507  -25.278 1.00 38.85 ? 97  PRO   A C     1 
ATOM   642  O O     . PRO   A 1 97  ? 5.562   30.189  -24.629 1.00 38.65 ? 97  PRO   A O     1 
ATOM   643  C CB    . PRO   A 1 97  ? 5.409   27.205  -25.806 1.00 35.59 ? 97  PRO   A CB    1 
ATOM   644  C CG    . PRO   A 1 97  ? 6.114   26.200  -26.679 1.00 33.94 ? 97  PRO   A CG    1 
ATOM   645  C CD    . PRO   A 1 97  ? 7.192   26.933  -27.500 1.00 37.28 ? 97  PRO   A CD    1 
ATOM   646  N N     . ARG   A 1 98  ? 7.672   29.509  -25.058 1.00 39.42 ? 98  ARG   A N     1 
ATOM   647  C CA    . ARG   A 1 98  ? 8.248   30.313  -23.988 1.00 41.29 ? 98  ARG   A CA    1 
ATOM   648  C C     . ARG   A 1 98  ? 8.006   31.809  -24.220 1.00 44.12 ? 98  ARG   A C     1 
ATOM   649  O O     . ARG   A 1 98  ? 7.988   32.582  -23.267 1.00 51.34 ? 98  ARG   A O     1 
ATOM   650  C CB    . ARG   A 1 98  ? 9.744   30.031  -23.831 1.00 41.18 ? 98  ARG   A CB    1 
ATOM   651  C CG    . ARG   A 1 98  ? 10.043  28.618  -23.346 1.00 44.27 ? 98  ARG   A CG    1 
ATOM   652  C CD    . ARG   A 1 98  ? 11.535  28.366  -23.208 1.00 48.81 ? 98  ARG   A CD    1 
ATOM   653  N NE    . ARG   A 1 98  ? 12.287  28.655  -24.437 1.00 55.05 ? 98  ARG   A NE    1 
ATOM   654  C CZ    . ARG   A 1 98  ? 13.318  27.964  -24.925 1.00 60.02 ? 98  ARG   A CZ    1 
ATOM   655  N NH1   . ARG   A 1 98  ? 13.794  26.907  -24.291 1.00 62.31 ? 98  ARG   A NH1   1 
ATOM   656  N NH2   . ARG   A 1 98  ? 13.883  28.343  -26.056 1.00 57.01 ? 98  ARG   A NH2   1 
ATOM   657  N N     . THR   A 1 99  ? 7.816   32.210  -25.477 1.00 41.00 ? 99  THR   A N     1 
ATOM   658  C CA    . THR   A 1 99  ? 7.714   33.620  -25.826 1.00 52.77 ? 99  THR   A CA    1 
ATOM   659  C C     . THR   A 1 99  ? 6.300   33.954  -26.308 1.00 52.83 ? 99  THR   A C     1 
ATOM   660  O O     . THR   A 1 99  ? 6.004   35.115  -26.583 1.00 59.55 ? 99  THR   A O     1 
ATOM   661  C CB    . THR   A 1 99  ? 8.767   33.938  -26.891 1.00 58.25 ? 99  THR   A CB    1 
ATOM   662  O OG1   . THR   A 1 99  ? 8.402   33.172  -28.032 1.00 66.01 ? 99  THR   A OG1   1 
ATOM   663  C CG2   . THR   A 1 99  ? 10.174  33.518  -26.500 1.00 59.00 ? 99  THR   A CG2   1 
ATOM   664  N N     . SER   A 1 100 ? 5.427   32.940  -26.402 1.00 45.31 ? 100 SER   A N     1 
ATOM   665  C CA    . SER   A 1 100 ? 4.067   33.134  -26.867 1.00 40.41 ? 100 SER   A CA    1 
ATOM   666  C C     . SER   A 1 100 ? 3.167   33.610  -25.726 1.00 37.40 ? 100 SER   A C     1 
ATOM   667  O O     . SER   A 1 100 ? 3.506   33.490  -24.551 1.00 43.39 ? 100 SER   A O     1 
ATOM   668  C CB    . SER   A 1 100 ? 3.527   31.863  -27.487 1.00 40.56 ? 100 SER   A CB    1 
ATOM   669  O OG    . SER   A 1 100 ? 3.221   30.923  -26.472 1.00 37.57 ? 100 SER   A OG    1 
ATOM   670  N N     . THR   A 1 101 ? 2.003   34.157  -26.099 1.00 40.29 ? 101 THR   A N     1 
ATOM   671  C CA    . THR   A 1 101 ? 0.946   34.517  -25.171 1.00 41.06 ? 101 THR   A CA    1 
ATOM   672  C C     . THR   A 1 101 ? -0.211  33.531  -25.339 1.00 35.15 ? 101 THR   A C     1 
ATOM   673  O O     . THR   A 1 101 ? -0.777  33.440  -26.418 1.00 33.53 ? 101 THR   A O     1 
ATOM   674  C CB    . THR   A 1 101 ? 0.494   35.942  -25.484 1.00 45.09 ? 101 THR   A CB    1 
ATOM   675  O OG1   . THR   A 1 101 ? 1.683   36.732  -25.450 1.00 50.28 ? 101 THR   A OG1   1 
ATOM   676  C CG2   . THR   A 1 101 ? -0.535  36.452  -24.492 1.00 46.66 ? 101 THR   A CG2   1 
ATOM   677  N N     . ALA   A 1 102 ? -0.577  32.826  -24.268 1.00 36.87 ? 102 ALA   A N     1 
ATOM   678  C CA    . ALA   A 1 102 ? -1.754  31.964  -24.277 1.00 35.15 ? 102 ALA   A CA    1 
ATOM   679  C C     . ALA   A 1 102 ? -2.994  32.793  -24.610 1.00 34.73 ? 102 ALA   A C     1 
ATOM   680  O O     . ALA   A 1 102 ? -3.075  33.948  -24.207 1.00 33.92 ? 102 ALA   A O     1 
ATOM   681  C CB    . ALA   A 1 102 ? -1.869  31.287  -22.928 1.00 32.86 ? 102 ALA   A CB    1 
ATOM   682  N N     . ALA   A 1 103 ? -3.923  32.229  -25.394 1.00 27.94 ? 103 ALA   A N     1 
ATOM   683  C CA    . ALA   A 1 103 ? -5.166  32.913  -25.738 1.00 27.97 ? 103 ALA   A CA    1 
ATOM   684  C C     . ALA   A 1 103 ? -6.216  32.544  -24.691 1.00 28.32 ? 103 ALA   A C     1 
ATOM   685  O O     . ALA   A 1 103 ? -7.002  31.604  -24.820 1.00 23.46 ? 103 ALA   A O     1 
ATOM   686  C CB    . ALA   A 1 103 ? -5.603  32.561  -27.142 1.00 32.35 ? 103 ALA   A CB    1 
ATOM   687  N N     . LEU   A 1 104 ? -6.212  33.304  -23.608 1.00 27.80 ? 104 LEU   A N     1 
ATOM   688  C CA    . LEU   A 1 104 ? -7.028  32.977  -22.468 1.00 28.23 ? 104 LEU   A CA    1 
ATOM   689  C C     . LEU   A 1 104 ? -8.475  33.283  -22.797 1.00 28.59 ? 104 LEU   A C     1 
ATOM   690  O O     . LEU   A 1 104 ? -8.806  34.344  -23.317 1.00 30.19 ? 104 LEU   A O     1 
ATOM   691  C CB    . LEU   A 1 104 ? -6.534  33.773  -21.263 1.00 30.28 ? 104 LEU   A CB    1 
ATOM   692  C CG    . LEU   A 1 104 ? -7.316  33.557  -19.968 1.00 31.70 ? 104 LEU   A CG    1 
ATOM   693  C CD1   . LEU   A 1 104 ? -7.140  32.152  -19.388 1.00 30.70 ? 104 LEU   A CD1   1 
ATOM   694  C CD2   . LEU   A 1 104 ? -6.955  34.632  -18.956 1.00 33.21 ? 104 LEU   A CD2   1 
ATOM   695  N N     . LEU   A 1 105 ? -9.344  32.338  -22.460 1.00 23.03 ? 105 LEU   A N     1 
ATOM   696  C CA    . LEU   A 1 105 ? -10.776 32.503  -22.613 1.00 22.51 ? 105 LEU   A CA    1 
ATOM   697  C C     . LEU   A 1 105 ? -11.381 32.920  -21.283 1.00 22.59 ? 105 LEU   A C     1 
ATOM   698  O O     . LEU   A 1 105 ? -12.137 33.891  -21.204 1.00 25.25 ? 105 LEU   A O     1 
ATOM   699  C CB    . LEU   A 1 105 ? -11.383 31.212  -23.155 1.00 24.18 ? 105 LEU   A CB    1 
ATOM   700  C CG    . LEU   A 1 105 ? -10.803 30.769  -24.503 1.00 24.20 ? 105 LEU   A CG    1 
ATOM   701  C CD1   . LEU   A 1 105 ? -11.326 29.394  -24.915 1.00 22.84 ? 105 LEU   A CD1   1 
ATOM   702  C CD2   . LEU   A 1 105 ? -11.165 31.756  -25.575 1.00 25.51 ? 105 LEU   A CD2   1 
ATOM   703  N N     . PHE   A 1 106 ? -11.095 32.153  -20.227 1.00 21.00 ? 106 PHE   A N     1 
ATOM   704  C CA    . PHE   A 1 106 ? -11.683 32.487  -18.929 1.00 21.13 ? 106 PHE   A CA    1 
ATOM   705  C C     . PHE   A 1 106 ? -11.005 31.621  -17.884 1.00 24.00 ? 106 PHE   A C     1 
ATOM   706  O O     . PHE   A 1 106 ? -10.332 30.649  -18.213 1.00 21.93 ? 106 PHE   A O     1 
ATOM   707  C CB    . PHE   A 1 106 ? -13.192 32.304  -18.748 1.00 21.29 ? 106 PHE   A CB    1 
ATOM   708  C CG    . PHE   A 1 106 ? -13.686 30.859  -18.807 1.00 22.15 ? 106 PHE   A CG    1 
ATOM   709  C CD1   . PHE   A 1 106 ? -13.822 30.210  -20.023 1.00 22.75 ? 106 PHE   A CD1   1 
ATOM   710  C CD2   . PHE   A 1 106 ? -13.985 30.157  -17.645 1.00 20.61 ? 106 PHE   A CD2   1 
ATOM   711  C CE1   . PHE   A 1 106 ? -14.253 28.891  -20.078 1.00 24.99 ? 106 PHE   A CE1   1 
ATOM   712  C CE2   . PHE   A 1 106 ? -14.369 28.816  -17.718 1.00 24.36 ? 106 PHE   A CE2   1 
ATOM   713  C CZ    . PHE   A 1 106 ? -14.495 28.198  -18.926 1.00 25.43 ? 106 PHE   A CZ    1 
ATOM   714  N N     . GLN   A 1 107 ? -11.197 32.001  -16.614 1.00 23.33 ? 107 GLN   A N     1 
ATOM   715  C CA    . GLN   A 1 107 ? -10.576 31.281  -15.520 1.00 23.71 ? 107 GLN   A CA    1 
ATOM   716  C C     . GLN   A 1 107 ? -11.673 30.628  -14.704 1.00 23.78 ? 107 GLN   A C     1 
ATOM   717  O O     . GLN   A 1 107 ? -12.690 31.258  -14.429 1.00 22.26 ? 107 GLN   A O     1 
ATOM   718  C CB    . GLN   A 1 107 ? -9.832  32.312  -14.675 1.00 27.22 ? 107 GLN   A CB    1 
ATOM   719  C CG    . GLN   A 1 107 ? -8.645  32.936  -15.400 1.00 30.57 ? 107 GLN   A CG    1 
ATOM   720  C CD    . GLN   A 1 107 ? -7.748  33.684  -14.451 1.00 40.54 ? 107 GLN   A CD    1 
ATOM   721  O OE1   . GLN   A 1 107 ? -8.156  34.698  -13.884 1.00 47.46 ? 107 GLN   A OE1   1 
ATOM   722  N NE2   . GLN   A 1 107 ? -6.547  33.157  -14.228 1.00 43.63 ? 107 GLN   A NE2   1 
ATOM   723  N N     . LEU   A 1 108 ? -11.496 29.340  -14.393 1.00 21.90 ? 108 LEU   A N     1 
ATOM   724  C CA    . LEU   A 1 108 ? -12.462 28.620  -13.587 1.00 20.14 ? 108 LEU   A CA    1 
ATOM   725  C C     . LEU   A 1 108 ? -11.872 28.485  -12.198 1.00 21.46 ? 108 LEU   A C     1 
ATOM   726  O O     . LEU   A 1 108 ? -10.908 27.760  -12.012 1.00 23.28 ? 108 LEU   A O     1 
ATOM   727  C CB    . LEU   A 1 108 ? -12.722 27.241  -14.189 1.00 21.78 ? 108 LEU   A CB    1 
ATOM   728  C CG    . LEU   A 1 108 ? -13.735 26.376  -13.448 1.00 21.83 ? 108 LEU   A CG    1 
ATOM   729  C CD1   . LEU   A 1 108 ? -15.087 27.075  -13.366 1.00 25.24 ? 108 LEU   A CD1   1 
ATOM   730  C CD2   . LEU   A 1 108 ? -13.875 25.004  -14.131 1.00 25.40 ? 108 LEU   A CD2   1 
ATOM   731  N N     . HIS   A 1 109 ? -12.464 29.172  -11.217 1.00 22.59 ? 109 HIS   A N     1 
ATOM   732  C CA    . HIS   A 1 109 ? -11.977 29.053  -9.851  1.00 23.29 ? 109 HIS   A CA    1 
ATOM   733  C C     . HIS   A 1 109 ? -12.777 27.974  -9.128  1.00 26.02 ? 109 HIS   A C     1 
ATOM   734  O O     . HIS   A 1 109 ? -14.003 27.887  -9.234  1.00 33.69 ? 109 HIS   A O     1 
ATOM   735  C CB    . HIS   A 1 109 ? -12.142 30.392  -9.142  1.00 21.08 ? 109 HIS   A CB    1 
ATOM   736  C CG    . HIS   A 1 109 ? -11.533 31.505  -9.927  1.00 21.13 ? 109 HIS   A CG    1 
ATOM   737  N ND1   . HIS   A 1 109 ? -12.225 32.588  -10.418 1.00 25.22 ? 109 HIS   A ND1   1 
ATOM   738  C CD2   . HIS   A 1 109 ? -10.259 31.702  -10.226 1.00 20.25 ? 109 HIS   A CD2   1 
ATOM   739  C CE1   . HIS   A 1 109 ? -11.356 33.411  -11.005 1.00 22.53 ? 109 HIS   A CE1   1 
ATOM   740  N NE2   . HIS   A 1 109 ? -10.165 32.869  -10.916 1.00 24.31 ? 109 HIS   A NE2   1 
ATOM   741  N N     . VAL   A 1 110 ? -12.047 27.067  -8.503  1.00 27.94 ? 110 VAL   A N     1 
ATOM   742  C CA    . VAL   A 1 110 ? -12.641 25.946  -7.805  1.00 30.54 ? 110 VAL   A CA    1 
ATOM   743  C C     . VAL   A 1 110 ? -12.770 26.365  -6.346  1.00 30.52 ? 110 VAL   A C     1 
ATOM   744  O O     . VAL   A 1 110 ? -11.870 27.006  -5.793  1.00 33.08 ? 110 VAL   A O     1 
ATOM   745  C CB    . VAL   A 1 110 ? -11.738 24.718  -8.015  1.00 29.23 ? 110 VAL   A CB    1 
ATOM   746  C CG1   . VAL   A 1 110 ? -12.296 23.489  -7.314  1.00 32.82 ? 110 VAL   A CG1   1 
ATOM   747  C CG2   . VAL   A 1 110 ? -11.495 24.424  -9.483  1.00 32.79 ? 110 VAL   A CG2   1 
ATOM   748  N N     . LYS   A 1 111 ? -13.940 26.142  -5.756  1.00 28.01 ? 111 LYS   A N     1 
ATOM   749  C CA    . LYS   A 1 111 ? -14.132 26.457  -4.354  1.00 31.20 ? 111 LYS   A CA    1 
ATOM   750  C C     . LYS   A 1 111 ? -14.024 25.151  -3.569  1.00 32.97 ? 111 LYS   A C     1 
ATOM   751  O O     . LYS   A 1 111 ? -14.785 24.214  -3.822  1.00 35.19 ? 111 LYS   A O     1 
ATOM   752  C CB    . LYS   A 1 111 ? -15.454 27.210  -4.228  1.00 35.44 ? 111 LYS   A CB    1 
ATOM   753  C CG    . LYS   A 1 111 ? -15.709 27.766  -2.843  1.00 39.90 ? 111 LYS   A CG    1 
ATOM   754  C CD    . LYS   A 1 111 ? -16.836 28.789  -2.806  1.00 48.40 ? 111 LYS   A CD    1 
ATOM   755  C CE    . LYS   A 1 111 ? -18.121 28.305  -3.411  1.00 55.31 ? 111 LYS   A CE    1 
ATOM   756  N NZ    . LYS   A 1 111 ? -19.160 29.337  -3.315  1.00 58.23 ? 111 LYS   A NZ    1 
ATOM   757  N N     . GLY   A 1 112 ? -13.026 25.062  -2.683  1.00 32.78 ? 112 GLY   A N     1 
ATOM   758  C CA    . GLY   A 1 112 ? -12.853 23.885  -1.832  1.00 33.87 ? 112 GLY   A CA    1 
ATOM   759  C C     . GLY   A 1 112 ? -11.895 22.855  -2.443  1.00 38.35 ? 112 GLY   A C     1 
ATOM   760  O O     . GLY   A 1 112 ? -11.879 21.697  -2.011  1.00 43.33 ? 112 GLY   A O     1 
ATOM   761  N N     . GLY   A 1 113 ? -11.153 23.262  -3.484  1.00 34.45 ? 113 GLY   A N     1 
ATOM   762  C CA    . GLY   A 1 113 ? -9.985  22.534  -3.971  1.00 40.18 ? 113 GLY   A CA    1 
ATOM   763  C C     . GLY   A 1 113 ? -10.291 21.294  -4.829  1.00 42.16 ? 113 GLY   A C     1 
ATOM   764  O O     . GLY   A 1 113 ? -11.250 20.542  -4.591  1.00 39.69 ? 113 GLY   A O     1 
ATOM   765  N N     . TYR   A 1 114 ? -9.428  21.069  -5.834  1.00 38.04 ? 114 TYR   A N     1 
ATOM   766  C CA    . TYR   A 1 114 ? -9.367  19.780  -6.504  1.00 36.26 ? 114 TYR   A CA    1 
ATOM   767  C C     . TYR   A 1 114 ? -7.961  19.217  -6.296  1.00 36.51 ? 114 TYR   A C     1 
ATOM   768  O O     . TYR   A 1 114 ? -6.984  19.946  -6.138  1.00 32.46 ? 114 TYR   A O     1 
ATOM   769  C CB    . TYR   A 1 114 ? -9.779  19.810  -7.984  1.00 35.80 ? 114 TYR   A CB    1 
ATOM   770  C CG    . TYR   A 1 114 ? -8.745  20.453  -8.894  1.00 38.12 ? 114 TYR   A CG    1 
ATOM   771  C CD1   . TYR   A 1 114 ? -8.642  21.832  -8.986  1.00 39.85 ? 114 TYR   A CD1   1 
ATOM   772  C CD2   . TYR   A 1 114 ? -7.850  19.681  -9.629  1.00 38.23 ? 114 TYR   A CD2   1 
ATOM   773  C CE1   . TYR   A 1 114 ? -7.692  22.431  -9.793  1.00 39.68 ? 114 TYR   A CE1   1 
ATOM   774  C CE2   . TYR   A 1 114 ? -6.895  20.268  -10.439 1.00 38.32 ? 114 TYR   A CE2   1 
ATOM   775  C CZ    . TYR   A 1 114 ? -6.815  21.646  -10.515 1.00 38.61 ? 114 TYR   A CZ    1 
ATOM   776  O OH    . TYR   A 1 114 ? -5.867  22.245  -11.284 1.00 40.56 ? 114 TYR   A OH    1 
ATOM   777  N N     . LYS   A 1 115 ? -7.899  17.889  -6.211  1.00 33.37 ? 115 LYS   A N     1 
ATOM   778  C CA    . LYS   A 1 115 ? -6.626  17.202  -6.156  1.00 35.15 ? 115 LYS   A CA    1 
ATOM   779  C C     . LYS   A 1 115 ? -6.767  15.962  -7.007  1.00 33.53 ? 115 LYS   A C     1 
ATOM   780  O O     . LYS   A 1 115 ? -7.882  15.525  -7.280  1.00 34.66 ? 115 LYS   A O     1 
ATOM   781  C CB    . LYS   A 1 115 ? -6.237  16.834  -4.726  1.00 36.32 ? 115 LYS   A CB    1 
ATOM   782  C CG    . LYS   A 1 115 ? -6.065  18.001  -3.759  1.00 39.66 ? 115 LYS   A CG    1 
ATOM   783  C CD    . LYS   A 1 115 ? -5.586  17.488  -2.408  1.00 44.17 ? 115 LYS   A CD    1 
ATOM   784  C CE    . LYS   A 1 115 ? -5.841  18.389  -1.265  1.00 48.75 ? 115 LYS   A CE    1 
ATOM   785  N NZ    . LYS   A 1 115 ? -4.873  19.481  -1.188  1.00 53.28 ? 115 LYS   A NZ    1 
ATOM   786  N N     . ALA   A 1 116 ? -5.618  15.429  -7.413  1.00 31.59 ? 116 ALA   A N     1 
ATOM   787  C CA    . ALA   A 1 116 ? -5.532  14.224  -8.201  1.00 31.14 ? 116 ALA   A CA    1 
ATOM   788  C C     . ALA   A 1 116 ? -4.745  13.189  -7.417  1.00 31.54 ? 116 ALA   A C     1 
ATOM   789  O O     . ALA   A 1 116 ? -3.854  13.538  -6.637  1.00 32.35 ? 116 ALA   A O     1 
ATOM   790  C CB    . ALA   A 1 116 ? -4.871  14.498  -9.535  1.00 33.32 ? 116 ALA   A CB    1 
ATOM   791  N N     . CYS   A 1 117 ? -5.059  11.916  -7.654  1.00 29.26 ? 117 CYS   A N     1 
ATOM   792  C CA    . CYS   A 1 117 ? -4.242  10.867  -7.076  1.00 30.43 ? 117 CYS   A CA    1 
ATOM   793  C C     . CYS   A 1 117 ? -4.223  9.703   -8.039  1.00 29.13 ? 117 CYS   A C     1 
ATOM   794  O O     . CYS   A 1 117 ? -5.024  9.652   -8.974  1.00 34.88 ? 117 CYS   A O     1 
ATOM   795  C CB    . CYS   A 1 117 ? -4.724  10.452  -5.693  1.00 32.04 ? 117 CYS   A CB    1 
ATOM   796  S SG    . CYS   A 1 117 ? -6.294  9.551   -5.768  1.00 36.44 ? 117 CYS   A SG    1 
ATOM   797  N N     . ARG   A 1 118 ? -3.305  8.769   -7.784  1.00 30.58 ? 118 ARG   A N     1 
ATOM   798  C CA    . ARG   A 1 118 ? -3.313  7.496   -8.476  1.00 31.07 ? 118 ARG   A CA    1 
ATOM   799  C C     . ARG   A 1 118 ? -4.333  6.620   -7.750  1.00 28.84 ? 118 ARG   A C     1 
ATOM   800  O O     . ARG   A 1 118 ? -4.384  6.604   -6.520  1.00 28.07 ? 118 ARG   A O     1 
ATOM   801  C CB    . ARG   A 1 118 ? -1.955  6.776   -8.466  1.00 37.29 ? 118 ARG   A CB    1 
ATOM   802  C CG    . ARG   A 1 118 ? -0.758  7.626   -8.878  1.00 42.81 ? 118 ARG   A CG    1 
ATOM   803  C CD    . ARG   A 1 118 ? 0.453   6.744   -9.212  1.00 47.53 ? 118 ARG   A CD    1 
ATOM   804  N NE    . ARG   A 1 118 ? 0.951   6.074   -8.002  1.00 51.41 ? 118 ARG   A NE    1 
ATOM   805  C CZ    . ARG   A 1 118 ? 1.812   5.052   -7.951  1.00 56.17 ? 118 ARG   A CZ    1 
ATOM   806  N NH1   . ARG   A 1 118 ? 2.312   4.530   -9.059  1.00 56.03 ? 118 ARG   A NH1   1 
ATOM   807  N NH2   . ARG   A 1 118 ? 2.175   4.556   -6.778  1.00 52.57 ? 118 ARG   A NH2   1 
ATOM   808  N N     . ARG   A 1 119 ? -5.141  5.917   -8.542  1.00 27.89 ? 119 ARG   A N     1 
ATOM   809  C CA    . ARG   A 1 119 ? -6.246  5.113   -8.039  1.00 25.24 ? 119 ARG   A CA    1 
ATOM   810  C C     . ARG   A 1 119 ? -5.709  4.089   -7.036  1.00 26.31 ? 119 ARG   A C     1 
ATOM   811  O O     . ARG   A 1 119 ? -6.241  3.959   -5.923  1.00 24.40 ? 119 ARG   A O     1 
ATOM   812  C CB    . ARG   A 1 119 ? -6.949  4.444   -9.224  1.00 23.25 ? 119 ARG   A CB    1 
ATOM   813  C CG    . ARG   A 1 119 ? -8.230  3.711   -8.822  1.00 23.91 ? 119 ARG   A CG    1 
ATOM   814  C CD    . ARG   A 1 119 ? -8.818  2.838   -9.866  1.00 24.51 ? 119 ARG   A CD    1 
ATOM   815  N NE    . ARG   A 1 119 ? -10.028 2.089   -9.500  1.00 23.00 ? 119 ARG   A NE    1 
ATOM   816  C CZ    . ARG   A 1 119 ? -10.059 0.922   -8.860  1.00 26.98 ? 119 ARG   A CZ    1 
ATOM   817  N NH1   . ARG   A 1 119 ? -8.915  0.357   -8.502  1.00 25.55 ? 119 ARG   A NH1   1 
ATOM   818  N NH2   . ARG   A 1 119 ? -11.205 0.296   -8.583  1.00 24.30 ? 119 ARG   A NH2   1 
ATOM   819  N N     . CYS   A 1 120 ? -4.599  3.424   -7.400  1.00 26.66 ? 120 CYS   A N     1 
ATOM   820  C CA    . CYS   A 1 120 ? -4.021  2.359   -6.580  1.00 29.50 ? 120 CYS   A CA    1 
ATOM   821  C C     . CYS   A 1 120 ? -3.555  2.887   -5.226  1.00 29.96 ? 120 CYS   A C     1 
ATOM   822  O O     . CYS   A 1 120 ? -3.645  2.174   -4.224  1.00 27.85 ? 120 CYS   A O     1 
ATOM   823  C CB    . CYS   A 1 120 ? -2.905  1.614   -7.318  1.00 32.55 ? 120 CYS   A CB    1 
ATOM   824  S SG    . CYS   A 1 120 ? -1.486  2.665   -7.768  1.00 35.50 ? 120 CYS   A SG    1 
ATOM   825  N N     . ASP   A 1 121 ? -3.099  4.149   -5.193  1.00 29.61 ? 121 ASP   A N     1 
ATOM   826  C CA    . ASP   A 1 121 ? -2.599  4.786   -3.983  1.00 30.51 ? 121 ASP   A CA    1 
ATOM   827  C C     . ASP   A 1 121 ? -3.744  5.048   -3.009  1.00 31.05 ? 121 ASP   A C     1 
ATOM   828  O O     . ASP   A 1 121 ? -3.646  4.787   -1.811  1.00 28.53 ? 121 ASP   A O     1 
ATOM   829  C CB    . ASP   A 1 121 ? -1.872  6.091   -4.291  1.00 33.32 ? 121 ASP   A CB    1 
ATOM   830  C CG    . ASP   A 1 121 ? -0.453  5.948   -4.839  1.00 38.16 ? 121 ASP   A CG    1 
ATOM   831  O OD1   . ASP   A 1 121 ? 0.095   4.842   -4.749  1.00 34.20 ? 121 ASP   A OD1   1 
ATOM   832  O OD2   . ASP   A 1 121 ? 0.093   6.948   -5.359  1.00 35.96 ? 121 ASP   A OD2   1 
ATOM   833  N N     . PHE   A 1 122 ? -4.859  5.558   -3.534  1.00 28.75 ? 122 PHE   A N     1 
ATOM   834  C CA    . PHE   A 1 122 ? -6.017  5.820   -2.697  1.00 28.41 ? 122 PHE   A CA    1 
ATOM   835  C C     . PHE   A 1 122 ? -6.636  4.517   -2.178  1.00 26.25 ? 122 PHE   A C     1 
ATOM   836  O O     . PHE   A 1 122 ? -6.959  4.406   -1.001  1.00 24.36 ? 122 PHE   A O     1 
ATOM   837  C CB    . PHE   A 1 122 ? -6.968  6.662   -3.548  1.00 29.66 ? 122 PHE   A CB    1 
ATOM   838  C CG    . PHE   A 1 122 ? -8.169  7.220   -2.803  1.00 27.14 ? 122 PHE   A CG    1 
ATOM   839  C CD1   . PHE   A 1 122 ? -8.162  7.397   -1.425  1.00 25.73 ? 122 PHE   A CD1   1 
ATOM   840  C CD2   . PHE   A 1 122 ? -9.296  7.609   -3.509  1.00 26.97 ? 122 PHE   A CD2   1 
ATOM   841  C CE1   . PHE   A 1 122 ? -9.268  7.935   -0.779  1.00 26.05 ? 122 PHE   A CE1   1 
ATOM   842  C CE2   . PHE   A 1 122 ? -10.400 8.123   -2.857  1.00 25.72 ? 122 PHE   A CE2   1 
ATOM   843  C CZ    . PHE   A 1 122 ? -10.393 8.264   -1.493  1.00 27.27 ? 122 PHE   A CZ    1 
ATOM   844  N N     . VAL   A 1 123 ? -6.770  3.517   -3.055  1.00 24.21 ? 123 VAL   A N     1 
ATOM   845  C CA    . VAL   A 1 123 ? -7.269  2.219   -2.641  1.00 26.69 ? 123 VAL   A CA    1 
ATOM   846  C C     . VAL   A 1 123 ? -6.414  1.646   -1.511  1.00 26.20 ? 123 VAL   A C     1 
ATOM   847  O O     . VAL   A 1 123 ? -6.944  1.156   -0.518  1.00 26.95 ? 123 VAL   A O     1 
ATOM   848  C CB    . VAL   A 1 123 ? -7.316  1.286   -3.866  1.00 26.33 ? 123 VAL   A CB    1 
ATOM   849  C CG1   . VAL   A 1 123 ? -7.440  -0.187  -3.495  1.00 29.88 ? 123 VAL   A CG1   1 
ATOM   850  C CG2   . VAL   A 1 123 ? -8.438  1.704   -4.813  1.00 24.21 ? 123 VAL   A CG2   1 
ATOM   851  N N     . ASP   A 1 124 ? -5.092  1.684   -1.673  1.00 27.82 ? 124 ASP   A N     1 
ATOM   852  C CA    . ASP   A 1 124 ? -4.194  1.143   -0.667  1.00 28.95 ? 124 ASP   A CA    1 
ATOM   853  C C     . ASP   A 1 124 ? -4.421  1.834   0.672   1.00 28.00 ? 124 ASP   A C     1 
ATOM   854  O O     . ASP   A 1 124 ? -4.425  1.169   1.710   1.00 27.65 ? 124 ASP   A O     1 
ATOM   855  C CB    . ASP   A 1 124 ? -2.743  1.239   -1.119  1.00 35.16 ? 124 ASP   A CB    1 
ATOM   856  C CG    . ASP   A 1 124 ? -1.703  0.920   -0.048  1.00 41.99 ? 124 ASP   A CG    1 
ATOM   857  O OD1   . ASP   A 1 124 ? -1.413  -0.281  0.146   1.00 45.08 ? 124 ASP   A OD1   1 
ATOM   858  O OD2   . ASP   A 1 124 ? -1.207  1.866   0.597   1.00 39.88 ? 124 ASP   A OD2   1 
ATOM   859  N N     . GLN   A 1 125 ? -4.637  3.156   0.658   1.00 24.83 ? 125 GLN   A N     1 
ATOM   860  C CA    . GLN   A 1 125 ? -4.873  3.913   1.868   1.00 25.91 ? 125 GLN   A CA    1 
ATOM   861  C C     . GLN   A 1 125 ? -6.188  3.476   2.524   1.00 27.42 ? 125 GLN   A C     1 
ATOM   862  O O     . GLN   A 1 125 ? -6.228  3.208   3.728   1.00 25.81 ? 125 GLN   A O     1 
ATOM   863  C CB    . GLN   A 1 125 ? -4.907  5.430   1.657   1.00 27.26 ? 125 GLN   A CB    1 
ATOM   864  C CG    . GLN   A 1 125 ? -3.547  6.090   1.429   1.00 28.17 ? 125 GLN   A CG    1 
ATOM   865  C CD    . GLN   A 1 125 ? -2.623  5.919   2.608   1.00 27.26 ? 125 GLN   A CD    1 
ATOM   866  O OE1   . GLN   A 1 125 ? -2.893  6.393   3.721   1.00 32.94 ? 125 GLN   A OE1   1 
ATOM   867  N NE2   . GLN   A 1 125 ? -1.561  5.171   2.380   1.00 30.71 ? 125 GLN   A NE2   1 
ATOM   868  N N     . ILE   A 1 126 ? -7.295  3.476   1.764   1.00 25.82 ? 126 ILE   A N     1 
ATOM   869  C CA    . ILE   A 1 126 ? -8.604  3.198   2.342   1.00 25.86 ? 126 ILE   A CA    1 
ATOM   870  C C     . ILE   A 1 126 ? -8.619  1.780   2.897   1.00 25.96 ? 126 ILE   A C     1 
ATOM   871  O O     . ILE   A 1 126 ? -9.205  1.536   3.951   1.00 26.24 ? 126 ILE   A O     1 
ATOM   872  C CB    . ILE   A 1 126 ? -9.758  3.377   1.334   1.00 28.16 ? 126 ILE   A CB    1 
ATOM   873  C CG1   . ILE   A 1 126 ? -9.769  4.714   0.643   1.00 31.04 ? 126 ILE   A CG1   1 
ATOM   874  C CG2   . ILE   A 1 126 ? -11.103 3.180   2.041   1.00 30.85 ? 126 ILE   A CG2   1 
ATOM   875  C CD1   . ILE   A 1 126 ? -10.570 4.708   -0.661  1.00 33.52 ? 126 ILE   A CD1   1 
ATOM   876  N N     . VAL   A 1 127 ? -8.017  0.849   2.163   1.00 25.57 ? 127 VAL   A N     1 
ATOM   877  C CA    . VAL   A 1 127 ? -8.046  -0.552  2.560   1.00 27.49 ? 127 VAL   A CA    1 
ATOM   878  C C     . VAL   A 1 127 ? -7.424  -0.738  3.951   1.00 32.72 ? 127 VAL   A C     1 
ATOM   879  O O     . VAL   A 1 127 ? -7.826  -1.664  4.657   1.00 31.34 ? 127 VAL   A O     1 
ATOM   880  C CB    . VAL   A 1 127 ? -7.370  -1.414  1.485   1.00 30.68 ? 127 VAL   A CB    1 
ATOM   881  C CG1   . VAL   A 1 127 ? -6.897  -2.778  1.977   1.00 36.26 ? 127 VAL   A CG1   1 
ATOM   882  C CG2   . VAL   A 1 127 ? -8.276  -1.574  0.278   1.00 35.47 ? 127 VAL   A CG2   1 
ATOM   883  N N     . GLN   A 1 128 ? -6.480  0.139   4.353   1.00 30.07 ? 128 GLN   A N     1 
ATOM   884  C CA    . GLN   A 1 128 ? -5.833  0.021   5.660   1.00 31.74 ? 128 GLN   A CA    1 
ATOM   885  C C     . GLN   A 1 128 ? -6.850  0.239   6.779   1.00 31.42 ? 128 GLN   A C     1 
ATOM   886  O O     . GLN   A 1 128 ? -6.602  -0.119  7.932   1.00 30.96 ? 128 GLN   A O     1 
ATOM   887  C CB    . GLN   A 1 128 ? -4.735  1.062   5.915   1.00 40.23 ? 128 GLN   A CB    1 
ATOM   888  C CG    . GLN   A 1 128 ? -3.509  1.007   4.999   1.00 45.67 ? 128 GLN   A CG    1 
ATOM   889  C CD    . GLN   A 1 128 ? -2.582  2.209   5.120   1.00 52.83 ? 128 GLN   A CD    1 
ATOM   890  O OE1   . GLN   A 1 128 ? -2.594  2.986   6.088   1.00 50.99 ? 128 GLN   A OE1   1 
ATOM   891  N NE2   . GLN   A 1 128 ? -1.722  2.368   4.127   1.00 55.14 ? 128 GLN   A NE2   1 
ATOM   892  N N     . HIS   A 1 129 ? -7.996  0.871   6.478   1.00 28.56 ? 129 HIS   A N     1 
ATOM   893  C CA    . HIS   A 1 129 ? -9.004  1.156   7.487   1.00 27.24 ? 129 HIS   A CA    1 
ATOM   894  C C     . HIS   A 1 129 ? -10.114 0.099   7.510   1.00 29.39 ? 129 HIS   A C     1 
ATOM   895  O O     . HIS   A 1 129 ? -11.109 0.272   8.227   1.00 33.03 ? 129 HIS   A O     1 
ATOM   896  C CB    . HIS   A 1 129 ? -9.660  2.523   7.229   1.00 27.92 ? 129 HIS   A CB    1 
ATOM   897  C CG    . HIS   A 1 129 ? -8.660  3.610   7.350   1.00 32.58 ? 129 HIS   A CG    1 
ATOM   898  N ND1   . HIS   A 1 129 ? -8.282  4.106   8.588   1.00 37.56 ? 129 HIS   A ND1   1 
ATOM   899  C CD2   . HIS   A 1 129 ? -7.892  4.218   6.450   1.00 35.04 ? 129 HIS   A CD2   1 
ATOM   900  C CE1   . HIS   A 1 129 ? -7.359  5.037   8.411   1.00 36.78 ? 129 HIS   A CE1   1 
ATOM   901  N NE2   . HIS   A 1 129 ? -7.091  5.113   7.130   1.00 37.73 ? 129 HIS   A NE2   1 
ATOM   902  N N     . ILE   A 1 130 ? -9.989  -0.951  6.690   1.00 28.13 ? 130 ILE   A N     1 
ATOM   903  C CA    . ILE   A 1 130 ? -11.023 -1.975  6.621   1.00 27.83 ? 130 ILE   A CA    1 
ATOM   904  C C     . ILE   A 1 130 ? -10.426 -3.269  7.155   1.00 25.51 ? 130 ILE   A C     1 
ATOM   905  O O     . ILE   A 1 130 ? -9.419  -3.731  6.632   1.00 26.14 ? 130 ILE   A O     1 
ATOM   906  C CB    . ILE   A 1 130 ? -11.530 -2.175  5.178   1.00 28.58 ? 130 ILE   A CB    1 
ATOM   907  C CG1   . ILE   A 1 130 ? -12.091 -0.861  4.601   1.00 28.92 ? 130 ILE   A CG1   1 
ATOM   908  C CG2   . ILE   A 1 130 ? -12.538 -3.328  5.130   1.00 29.00 ? 130 ILE   A CG2   1 
ATOM   909  C CD1   . ILE   A 1 130 ? -12.408 -0.900  3.111   1.00 26.88 ? 130 ILE   A CD1   1 
ATOM   910  N N     . PRO   A 1 131 ? -11.063 -3.942  8.122   1.00 27.78 ? 131 PRO   A N     1 
ATOM   911  C CA    . PRO   A 1 131 ? -10.534 -5.222  8.593   1.00 30.36 ? 131 PRO   A CA    1 
ATOM   912  C C     . PRO   A 1 131 ? -10.484 -6.237  7.466   1.00 32.25 ? 131 PRO   A C     1 
ATOM   913  O O     . PRO   A 1 131 ? -11.417 -6.312  6.679   1.00 35.75 ? 131 PRO   A O     1 
ATOM   914  C CB    . PRO   A 1 131 ? -11.485 -5.595  9.725   1.00 28.93 ? 131 PRO   A CB    1 
ATOM   915  C CG    . PRO   A 1 131 ? -12.029 -4.264  10.198  1.00 30.10 ? 131 PRO   A CG    1 
ATOM   916  C CD    . PRO   A 1 131 ? -12.233 -3.503  8.891   1.00 27.67 ? 131 PRO   A CD    1 
ATOM   917  N N     . LYS   A 1 132 ? -9.400  -7.025  7.420   1.00 29.95 ? 132 LYS   A N     1 
ATOM   918  C CA    . LYS   A 1 132 ? -9.169  -7.993  6.356   1.00 31.44 ? 132 LYS   A CA    1 
ATOM   919  C C     . LYS   A 1 132 ? -10.318 -8.994  6.289   1.00 32.40 ? 132 LYS   A C     1 
ATOM   920  O O     . LYS   A 1 132 ? -10.642 -9.467  5.210   1.00 36.28 ? 132 LYS   A O     1 
ATOM   921  C CB    . LYS   A 1 132 ? -7.856  -8.783  6.492   1.00 34.95 ? 132 LYS   A CB    1 
ATOM   922  N N     . ASP   A 1 133 ? -10.937 -9.313  7.433   1.00 30.47 ? 133 ASP   A N     1 
ATOM   923  C CA    . ASP   A 1 133 ? -11.956 -10.352 7.450   1.00 35.28 ? 133 ASP   A CA    1 
ATOM   924  C C     . ASP   A 1 133 ? -13.275 -9.831  6.876   1.00 35.38 ? 133 ASP   A C     1 
ATOM   925  O O     . ASP   A 1 133 ? -14.168 -10.636 6.624   1.00 33.18 ? 133 ASP   A O     1 
ATOM   926  C CB    . ASP   A 1 133 ? -12.125 -10.940 8.841   1.00 39.16 ? 133 ASP   A CB    1 
ATOM   927  C CG    . ASP   A 1 133 ? -10.964 -11.805 9.314   1.00 48.86 ? 133 ASP   A CG    1 
ATOM   928  O OD1   . ASP   A 1 133 ? -10.094 -12.174 8.472   1.00 47.25 ? 133 ASP   A OD1   1 
ATOM   929  O OD2   . ASP   A 1 133 ? -10.916 -12.072 10.531  1.00 50.87 ? 133 ASP   A OD2   1 
ATOM   930  N N     . CYS   A 1 134 ? -13.385 -8.506  6.659   1.00 28.12 ? 134 CYS   A N     1 
ATOM   931  C CA    . CYS   A 1 134 ? -14.601 -7.929  6.097   1.00 29.98 ? 134 CYS   A CA    1 
ATOM   932  C C     . CYS   A 1 134 ? -14.560 -8.024  4.574   1.00 28.84 ? 134 CYS   A C     1 
ATOM   933  O O     . CYS   A 1 134 ? -15.529 -7.644  3.944   1.00 26.99 ? 134 CYS   A O     1 
ATOM   934  C CB    . CYS   A 1 134 ? -14.783 -6.468  6.491   1.00 28.73 ? 134 CYS   A CB    1 
ATOM   935  S SG    . CYS   A 1 134 ? -15.256 -6.218  8.230   1.00 36.51 ? 134 CYS   A SG    1 
ATOM   936  N N     . VAL   A 1 135 ? -13.427 -8.442  3.994   1.00 26.51 ? 135 VAL   A N     1 
ATOM   937  C CA    . VAL   A 1 135 ? -13.294 -8.554  2.547   1.00 29.15 ? 135 VAL   A CA    1 
ATOM   938  C C     . VAL   A 1 135 ? -13.195 -10.028 2.176   1.00 32.57 ? 135 VAL   A C     1 
ATOM   939  O O     . VAL   A 1 135 ? -12.359 -10.737 2.734   1.00 33.74 ? 135 VAL   A O     1 
ATOM   940  C CB    . VAL   A 1 135 ? -12.086 -7.759  2.026   1.00 31.68 ? 135 VAL   A CB    1 
ATOM   941  C CG1   . VAL   A 1 135 ? -11.957 -7.855  0.510   1.00 33.17 ? 135 VAL   A CG1   1 
ATOM   942  C CG2   . VAL   A 1 135 ? -12.158 -6.298  2.450   1.00 32.88 ? 135 VAL   A CG2   1 
ATOM   943  N N     . GLN   A 1 136 ? -14.038 -10.477 1.232   1.00 26.78 ? 136 GLN   A N     1 
ATOM   944  C CA    . GLN   A 1 136 ? -13.937 -11.829 0.715   1.00 29.87 ? 136 GLN   A CA    1 
ATOM   945  C C     . GLN   A 1 136 ? -13.529 -11.752 -0.747  1.00 26.06 ? 136 GLN   A C     1 
ATOM   946  O O     . GLN   A 1 136 ? -14.323 -11.294 -1.573  1.00 25.33 ? 136 GLN   A O     1 
ATOM   947  C CB    . GLN   A 1 136 ? -15.249 -12.593 0.880   1.00 31.35 ? 136 GLN   A CB    1 
ATOM   948  C CG    . GLN   A 1 136 ? -15.615 -12.828 2.338   1.00 35.36 ? 136 GLN   A CG    1 
ATOM   949  C CD    . GLN   A 1 136 ? -16.699 -13.865 2.528   1.00 35.76 ? 136 GLN   A CD    1 
ATOM   950  O OE1   . GLN   A 1 136 ? -16.968 -14.714 1.663   1.00 40.65 ? 136 GLN   A OE1   1 
ATOM   951  N NE2   . GLN   A 1 136 ? -17.327 -13.796 3.687   1.00 38.00 ? 136 GLN   A NE2   1 
ATOM   952  N N     . TYR   A 1 137 ? -12.283 -12.171 -1.032  1.00 26.01 ? 137 TYR   A N     1 
ATOM   953  C CA    . TYR   A 1 137 ? -11.737 -12.155 -2.385  1.00 24.80 ? 137 TYR   A CA    1 
ATOM   954  C C     . TYR   A 1 137 ? -12.141 -13.441 -3.101  1.00 25.77 ? 137 TYR   A C     1 
ATOM   955  O O     . TYR   A 1 137 ? -12.706 -14.345 -2.506  1.00 26.12 ? 137 TYR   A O     1 
ATOM   956  C CB    . TYR   A 1 137 ? -10.227 -11.938 -2.409  1.00 28.55 ? 137 TYR   A CB    1 
ATOM   957  C CG    . TYR   A 1 137 ? -9.721  -10.645 -1.800  1.00 27.29 ? 137 TYR   A CG    1 
ATOM   958  C CD1   . TYR   A 1 137 ? -9.752  -9.455  -2.513  1.00 26.19 ? 137 TYR   A CD1   1 
ATOM   959  C CD2   . TYR   A 1 137 ? -9.255  -10.610 -0.494  1.00 29.83 ? 137 TYR   A CD2   1 
ATOM   960  C CE1   . TYR   A 1 137 ? -9.269  -8.278  -1.967  1.00 31.65 ? 137 TYR   A CE1   1 
ATOM   961  C CE2   . TYR   A 1 137 ? -8.772  -9.437  0.066   1.00 32.26 ? 137 TYR   A CE2   1 
ATOM   962  C CZ    . TYR   A 1 137 ? -8.788  -8.266  -0.671  1.00 32.64 ? 137 TYR   A CZ    1 
ATOM   963  O OH    . TYR   A 1 137 ? -8.341  -7.101  -0.136  1.00 35.63 ? 137 TYR   A OH    1 
ATOM   964  N N     . ARG   A 1 138 ? -11.969 -13.473 -4.421  1.00 24.77 ? 138 ARG   A N     1 
ATOM   965  C CA    . ARG   A 1 138 ? -12.414 -14.591 -5.257  1.00 29.74 ? 138 ARG   A CA    1 
ATOM   966  C C     . ARG   A 1 138 ? -13.921 -14.852 -5.121  1.00 27.68 ? 138 ARG   A C     1 
ATOM   967  O O     . ARG   A 1 138 ? -14.392 -15.997 -5.209  1.00 26.89 ? 138 ARG   A O     1 
ATOM   968  C CB    . ARG   A 1 138 ? -11.571 -15.842 -4.949  1.00 33.76 ? 138 ARG   A CB    1 
ATOM   969  C CG    . ARG   A 1 138 ? -10.086 -15.595 -5.170  1.00 40.86 ? 138 ARG   A CG    1 
ATOM   970  C CD    . ARG   A 1 138 ? -9.219  -16.855 -5.022  1.00 45.94 ? 138 ARG   A CD    1 
ATOM   971  N NE    . ARG   A 1 138 ? -7.872  -16.542 -5.510  1.00 56.68 ? 138 ARG   A NE    1 
ATOM   972  C CZ    . ARG   A 1 138 ? -7.506  -16.438 -6.795  1.00 67.11 ? 138 ARG   A CZ    1 
ATOM   973  N NH1   . ARG   A 1 138 ? -8.321  -16.824 -7.767  1.00 65.49 ? 138 ARG   A NH1   1 
ATOM   974  N NH2   . ARG   A 1 138 ? -6.303  -15.978 -7.111  1.00 68.78 ? 138 ARG   A NH2   1 
ATOM   975  N N     . LYS   A 1 139 ? -14.695 -13.781 -4.913  1.00 25.59 ? 139 LYS   A N     1 
ATOM   976  C CA    . LYS   A 1 139 ? -16.132 -13.892 -4.794  1.00 24.88 ? 139 LYS   A CA    1 
ATOM   977  C C     . LYS   A 1 139 ? -16.742 -13.079 -5.930  1.00 23.24 ? 139 LYS   A C     1 
ATOM   978  O O     . LYS   A 1 139 ? -16.963 -11.869 -5.816  1.00 22.70 ? 139 LYS   A O     1 
ATOM   979  C CB    . LYS   A 1 139 ? -16.601 -13.427 -3.417  1.00 24.68 ? 139 LYS   A CB    1 
ATOM   980  C CG    . LYS   A 1 139 ? -16.186 -14.350 -2.289  1.00 25.81 ? 139 LYS   A CG    1 
ATOM   981  C CD    . LYS   A 1 139 ? -16.982 -15.643 -2.335  1.00 29.25 ? 139 LYS   A CD    1 
ATOM   982  C CE    . LYS   A 1 139 ? -16.555 -16.589 -1.267  1.00 32.45 ? 139 LYS   A CE    1 
ATOM   983  N NZ    . LYS   A 1 139 ? -17.216 -17.855 -1.534  1.00 32.94 ? 139 LYS   A NZ    1 
ATOM   984  N N     . TRP   A 1 140 ? -16.899 -13.773 -7.052  1.00 22.42 ? 140 TRP   A N     1 
ATOM   985  C CA    . TRP   A 1 140 ? -17.379 -13.190 -8.289  1.00 23.66 ? 140 TRP   A CA    1 
ATOM   986  C C     . TRP   A 1 140 ? -18.892 -13.382 -8.354  1.00 23.57 ? 140 TRP   A C     1 
ATOM   987  O O     . TRP   A 1 140 ? -19.396 -14.495 -8.652  1.00 21.25 ? 140 TRP   A O     1 
ATOM   988  C CB    . TRP   A 1 140 ? -16.673 -13.881 -9.464  1.00 22.80 ? 140 TRP   A CB    1 
ATOM   989  C CG    . TRP   A 1 140 ? -16.792 -13.144 -10.766 1.00 24.61 ? 140 TRP   A CG    1 
ATOM   990  C CD1   . TRP   A 1 140 ? -17.795 -12.305 -11.162 1.00 25.93 ? 140 TRP   A CD1   1 
ATOM   991  C CD2   . TRP   A 1 140 ? -15.852 -13.193 -11.851 1.00 25.06 ? 140 TRP   A CD2   1 
ATOM   992  N NE1   . TRP   A 1 140 ? -17.537 -11.819 -12.410 1.00 23.78 ? 140 TRP   A NE1   1 
ATOM   993  C CE2   . TRP   A 1 140 ? -16.359 -12.348 -12.861 1.00 22.88 ? 140 TRP   A CE2   1 
ATOM   994  C CE3   . TRP   A 1 140 ? -14.644 -13.880 -12.067 1.00 26.97 ? 140 TRP   A CE3   1 
ATOM   995  C CZ2   . TRP   A 1 140 ? -15.688 -12.164 -14.066 1.00 24.24 ? 140 TRP   A CZ2   1 
ATOM   996  C CZ3   . TRP   A 1 140 ? -13.982 -13.698 -13.263 1.00 30.95 ? 140 TRP   A CZ3   1 
ATOM   997  C CH2   . TRP   A 1 140 ? -14.491 -12.832 -14.229 1.00 26.32 ? 140 TRP   A CH2   1 
ATOM   998  N N     . LEU   A 1 141 ? -19.623 -12.302 -8.032  1.00 20.60 ? 141 LEU   A N     1 
ATOM   999  C CA    . LEU   A 1 141 ? -21.073 -12.316 -8.011  1.00 21.45 ? 141 LEU   A CA    1 
ATOM   1000 C C     . LEU   A 1 141 ? -21.587 -12.686 -9.400  1.00 22.41 ? 141 LEU   A C     1 
ATOM   1001 O O     . LEU   A 1 141 ? -21.152 -12.110 -10.381 1.00 22.34 ? 141 LEU   A O     1 
ATOM   1002 C CB    . LEU   A 1 141 ? -21.701 -10.985 -7.593  1.00 24.71 ? 141 LEU   A CB    1 
ATOM   1003 C CG    . LEU   A 1 141 ? -23.226 -11.029 -7.624  1.00 28.70 ? 141 LEU   A CG    1 
ATOM   1004 C CD1   . LEU   A 1 141 ? -23.689 -11.888 -6.455  1.00 26.15 ? 141 LEU   A CD1   1 
ATOM   1005 C CD2   . LEU   A 1 141 ? -24.004 -9.726  -7.747  1.00 34.70 ? 141 LEU   A CD2   1 
ATOM   1006 N N     . ASP   A 1 142 ? -22.509 -13.638 -9.473  1.00 22.48 ? 142 ASP   A N     1 
ATOM   1007 C CA    . ASP   A 1 142 ? -23.086 -14.063 -10.738 1.00 23.09 ? 142 ASP   A CA    1 
ATOM   1008 C C     . ASP   A 1 142 ? -24.598 -13.870 -10.767 1.00 23.49 ? 142 ASP   A C     1 
ATOM   1009 O O     . ASP   A 1 142 ? -25.170 -13.535 -11.807 1.00 24.08 ? 142 ASP   A O     1 
ATOM   1010 C CB    . ASP   A 1 142 ? -22.733 -15.507 -11.034 1.00 23.87 ? 142 ASP   A CB    1 
ATOM   1011 C CG    . ASP   A 1 142 ? -23.030 -15.918 -12.468 1.00 26.70 ? 142 ASP   A CG    1 
ATOM   1012 O OD1   . ASP   A 1 142 ? -22.597 -15.205 -13.384 1.00 24.36 ? 142 ASP   A OD1   1 
ATOM   1013 O OD2   . ASP   A 1 142 ? -23.729 -16.911 -12.652 1.00 28.27 ? 142 ASP   A OD2   1 
ATOM   1014 N N     . SER   A 1 143 ? -25.285 -14.107 -9.649  1.00 21.82 ? 143 SER   A N     1 
ATOM   1015 C CA    . SER   A 1 143 ? -26.708 -13.816 -9.605  1.00 22.97 ? 143 SER   A CA    1 
ATOM   1016 C C     . SER   A 1 143 ? -27.151 -13.553 -8.165  1.00 24.10 ? 143 SER   A C     1 
ATOM   1017 O O     . SER   A 1 143 ? -26.380 -13.818 -7.237  1.00 22.42 ? 143 SER   A O     1 
ATOM   1018 C CB    . SER   A 1 143 ? -27.499 -14.942 -10.222 1.00 25.69 ? 143 SER   A CB    1 
ATOM   1019 O OG    . SER   A 1 143 ? -27.382 -16.131 -9.478  1.00 26.43 ? 143 SER   A OG    1 
ATOM   1020 N N     . ILE   A 1 144 ? -28.385 -13.053 -8.048  1.00 22.69 ? 144 ILE   A N     1 
ATOM   1021 C CA    . ILE   A 1 144 ? -29.072 -12.765 -6.799  1.00 22.48 ? 144 ILE   A CA    1 
ATOM   1022 C C     . ILE   A 1 144 ? -30.473 -13.378 -6.827  1.00 26.10 ? 144 ILE   A C     1 
ATOM   1023 O O     . ILE   A 1 144 ? -31.262 -13.145 -7.758  1.00 25.75 ? 144 ILE   A O     1 
ATOM   1024 C CB    . ILE   A 1 144 ? -29.138 -11.247 -6.600  1.00 20.46 ? 144 ILE   A CB    1 
ATOM   1025 C CG1   . ILE   A 1 144 ? -27.741 -10.615 -6.728  1.00 23.42 ? 144 ILE   A CG1   1 
ATOM   1026 C CG2   . ILE   A 1 144 ? -29.859 -10.885 -5.287  1.00 22.38 ? 144 ILE   A CG2   1 
ATOM   1027 C CD1   . ILE   A 1 144 ? -27.701 -9.100  -6.620  1.00 23.21 ? 144 ILE   A CD1   1 
ATOM   1028 N N     . GLU   A 1 145 ? -30.822 -14.088 -5.745  1.00 26.52 ? 145 GLU   A N     1 
ATOM   1029 C CA    . GLU   A 1 145 ? -32.163 -14.633 -5.608  1.00 33.57 ? 145 GLU   A CA    1 
ATOM   1030 C C     . GLU   A 1 145 ? -32.720 -14.212 -4.257  1.00 34.18 ? 145 GLU   A C     1 
ATOM   1031 O O     . GLU   A 1 145 ? -32.007 -13.600 -3.474  1.00 29.12 ? 145 GLU   A O     1 
ATOM   1032 C CB    . GLU   A 1 145 ? -32.180 -16.158 -5.664  1.00 36.89 ? 145 GLU   A CB    1 
ATOM   1033 C CG    . GLU   A 1 145 ? -31.480 -16.777 -6.867  1.00 43.72 ? 145 GLU   A CG    1 
ATOM   1034 C CD    . GLU   A 1 145 ? -31.439 -18.288 -6.668  1.00 56.89 ? 145 GLU   A CD    1 
ATOM   1035 O OE1   . GLU   A 1 145 ? -32.346 -18.829 -5.970  1.00 61.91 ? 145 GLU   A OE1   1 
ATOM   1036 O OE2   . GLU   A 1 145 ? -30.471 -18.921 -7.143  1.00 54.68 ? 145 GLU   A OE2   1 
ATOM   1037 N N     . THR   A 1 146 ? -34.002 -14.525 -4.029  1.00 40.66 ? 146 THR   A N     1 
ATOM   1038 C CA    . THR   A 1 146 ? -34.660 -14.282 -2.754  1.00 38.33 ? 146 THR   A CA    1 
ATOM   1039 C C     . THR   A 1 146 ? -34.737 -15.597 -1.981  1.00 38.36 ? 146 THR   A C     1 
ATOM   1040 O O     . THR   A 1 146 ? -35.058 -16.634 -2.534  1.00 40.30 ? 146 THR   A O     1 
ATOM   1041 C CB    . THR   A 1 146 ? -36.038 -13.668 -3.002  1.00 42.87 ? 146 THR   A CB    1 
ATOM   1042 O OG1   . THR   A 1 146 ? -35.867 -12.403 -3.639  1.00 42.98 ? 146 THR   A OG1   1 
ATOM   1043 C CG2   . THR   A 1 146 ? -36.793 -13.359 -1.722  1.00 40.41 ? 146 THR   A CG2   1 
ATOM   1044 N N     . ASP   A 1 147 ? -34.421 -15.564 -0.686  1.00 34.76 ? 147 ASP   A N     1 
ATOM   1045 C CA    . ASP   A 1 147 ? -34.521 -16.759 0.128   1.00 40.33 ? 147 ASP   A CA    1 
ATOM   1046 C C     . ASP   A 1 147 ? -36.007 -17.034 0.347   1.00 40.88 ? 147 ASP   A C     1 
ATOM   1047 O O     . ASP   A 1 147 ? -36.731 -16.139 0.758   1.00 38.26 ? 147 ASP   A O     1 
ATOM   1048 C CB    . ASP   A 1 147 ? -33.761 -16.605 1.435   1.00 40.39 ? 147 ASP   A CB    1 
ATOM   1049 C CG    . ASP   A 1 147 ? -33.689 -17.869 2.285   1.00 49.89 ? 147 ASP   A CG    1 
ATOM   1050 O OD1   . ASP   A 1 147 ? -32.800 -18.698 2.020   1.00 54.11 ? 147 ASP   A OD1   1 
ATOM   1051 O OD2   . ASP   A 1 147 ? -34.542 -18.024 3.183   1.00 53.88 ? 147 ASP   A OD2   1 
ATOM   1052 N N     . HIS   A 1 148 ? -36.464 -18.252 0.038   1.00 45.86 ? 148 HIS   A N     1 
ATOM   1053 C CA    . HIS   A 1 148 ? -37.871 -18.591 0.179   1.00 50.95 ? 148 HIS   A CA    1 
ATOM   1054 C C     . HIS   A 1 148 ? -38.269 -18.488 1.650   1.00 54.05 ? 148 HIS   A C     1 
ATOM   1055 O O     . HIS   A 1 148 ? -39.273 -17.861 1.975   1.00 58.08 ? 148 HIS   A O     1 
ATOM   1056 C CB    . HIS   A 1 148 ? -38.159 -19.977 -0.410  1.00 55.80 ? 148 HIS   A CB    1 
ATOM   1057 N N     . GLU   A 1 149 ? -37.433 -19.061 2.527   1.00 56.46 ? 149 GLU   A N     1 
ATOM   1058 C CA    . GLU   A 1 149 ? -37.713 -19.157 3.954   1.00 55.11 ? 149 GLU   A CA    1 
ATOM   1059 C C     . GLU   A 1 149 ? -37.687 -17.775 4.613   1.00 55.03 ? 149 GLU   A C     1 
ATOM   1060 O O     . GLU   A 1 149 ? -38.607 -17.445 5.356   1.00 55.73 ? 149 GLU   A O     1 
ATOM   1061 C CB    . GLU   A 1 149 ? -36.729 -20.139 4.593   1.00 50.71 ? 149 GLU   A CB    1 
ATOM   1062 N N     . SER   A 1 150 ? -36.656 -16.955 4.335   1.00 50.77 ? 150 SER   A N     1 
ATOM   1063 C CA    . SER   A 1 150 ? -36.469 -15.702 5.059   1.00 44.91 ? 150 SER   A CA    1 
ATOM   1064 C C     . SER   A 1 150 ? -36.855 -14.470 4.238   1.00 42.68 ? 150 SER   A C     1 
ATOM   1065 O O     . SER   A 1 150 ? -37.082 -13.412 4.815   1.00 44.49 ? 150 SER   A O     1 
ATOM   1066 C CB    . SER   A 1 150 ? -35.052 -15.569 5.542   1.00 44.82 ? 150 SER   A CB    1 
ATOM   1067 O OG    . SER   A 1 150 ? -34.174 -15.346 4.447   1.00 38.96 ? 150 SER   A OG    1 
ATOM   1068 N N     . GLY   A 1 151 ? -36.863 -14.562 2.903   1.00 40.64 ? 151 GLY   A N     1 
ATOM   1069 C CA    . GLY   A 1 151 ? -37.104 -13.383 2.078   1.00 38.58 ? 151 GLY   A CA    1 
ATOM   1070 C C     . GLY   A 1 151 ? -35.860 -12.487 1.926   1.00 35.64 ? 151 GLY   A C     1 
ATOM   1071 O O     . GLY   A 1 151 ? -35.927 -11.458 1.253   1.00 36.28 ? 151 GLY   A O     1 
ATOM   1072 N N     . ARG   A 1 152 ? -34.729 -12.886 2.528   1.00 34.35 ? 152 ARG   A N     1 
ATOM   1073 C CA    . ARG   A 1 152 ? -33.490 -12.120 2.442   1.00 31.50 ? 152 ARG   A CA    1 
ATOM   1074 C C     . ARG   A 1 152 ? -32.828 -12.363 1.091   1.00 27.13 ? 152 ARG   A C     1 
ATOM   1075 O O     . ARG   A 1 152 ? -33.201 -13.271 0.346   1.00 27.15 ? 152 ARG   A O     1 
ATOM   1076 C CB    . ARG   A 1 152 ? -32.576 -12.466 3.625   1.00 29.52 ? 152 ARG   A CB    1 
ATOM   1077 C CG    . ARG   A 1 152 ? -33.277 -12.027 4.894   1.00 33.53 ? 152 ARG   A CG    1 
ATOM   1078 C CD    . ARG   A 1 152 ? -32.487 -12.400 6.107   1.00 35.49 ? 152 ARG   A CD    1 
ATOM   1079 N NE    . ARG   A 1 152 ? -31.234 -11.645 6.158   1.00 33.99 ? 152 ARG   A NE    1 
ATOM   1080 C CZ    . ARG   A 1 152 ? -30.024 -12.159 6.355   1.00 37.94 ? 152 ARG   A CZ    1 
ATOM   1081 N NH1   . ARG   A 1 152 ? -29.818 -13.462 6.247   1.00 37.35 ? 152 ARG   A NH1   1 
ATOM   1082 N NH2   . ARG   A 1 152 ? -29.014 -11.348 6.651   1.00 35.06 ? 152 ARG   A NH2   1 
ATOM   1083 N N     . ALA   A 1 153 ? -31.884 -11.500 0.742   1.00 25.72 ? 153 ALA   A N     1 
ATOM   1084 C CA    . ALA   A 1 153 ? -31.197 -11.648 -0.525  1.00 25.41 ? 153 ALA   A CA    1 
ATOM   1085 C C     . ALA   A 1 153 ? -30.187 -12.784 -0.405  1.00 25.01 ? 153 ALA   A C     1 
ATOM   1086 O O     . ALA   A 1 153 ? -29.569 -12.958 0.646   1.00 25.21 ? 153 ALA   A O     1 
ATOM   1087 C CB    . ALA   A 1 153 ? -30.548 -10.341 -0.955  1.00 27.50 ? 153 ALA   A CB    1 
ATOM   1088 N N     . VAL   A 1 154 ? -30.039 -13.525 -1.517  1.00 22.85 ? 154 VAL   A N     1 
ATOM   1089 C CA    . VAL   A 1 154 ? -29.113 -14.614 -1.661  1.00 26.48 ? 154 VAL   A CA    1 
ATOM   1090 C C     . VAL   A 1 154 ? -28.171 -14.280 -2.809  1.00 26.97 ? 154 VAL   A C     1 
ATOM   1091 O O     . VAL   A 1 154 ? -28.610 -14.223 -3.953  1.00 29.05 ? 154 VAL   A O     1 
ATOM   1092 C CB    . VAL   A 1 154 ? -29.834 -15.945 -1.943  1.00 28.36 ? 154 VAL   A CB    1 
ATOM   1093 C CG1   . VAL   A 1 154 ? -28.819 -17.070 -2.037  1.00 28.24 ? 154 VAL   A CG1   1 
ATOM   1094 C CG2   . VAL   A 1 154 ? -30.923 -16.226 -0.898  1.00 30.56 ? 154 VAL   A CG2   1 
ATOM   1095 N N     . LEU   A 1 155 ? -26.903 -14.016 -2.482  1.00 23.53 ? 155 LEU   A N     1 
ATOM   1096 C CA    . LEU   A 1 155 ? -25.875 -13.801 -3.499  1.00 24.44 ? 155 LEU   A CA    1 
ATOM   1097 C C     . LEU   A 1 155 ? -25.313 -15.153 -3.935  1.00 23.76 ? 155 LEU   A C     1 
ATOM   1098 O O     . LEU   A 1 155 ? -24.989 -15.979 -3.076  1.00 25.64 ? 155 LEU   A O     1 
ATOM   1099 C CB    . LEU   A 1 155 ? -24.788 -12.932 -2.890  1.00 21.90 ? 155 LEU   A CB    1 
ATOM   1100 C CG    . LEU   A 1 155 ? -25.181 -11.497 -2.510  1.00 23.77 ? 155 LEU   A CG    1 
ATOM   1101 C CD1   . LEU   A 1 155 ? -25.766 -11.469 -1.073  1.00 24.44 ? 155 LEU   A CD1   1 
ATOM   1102 C CD2   . LEU   A 1 155 ? -24.006 -10.540 -2.596  1.00 24.95 ? 155 LEU   A CD2   1 
ATOM   1103 N N     . LYS   A 1 156 ? -25.216 -15.390 -5.254  1.00 22.51 ? 156 LYS   A N     1 
ATOM   1104 C CA    . LYS   A 1 156 ? -24.630 -16.600 -5.789  1.00 22.76 ? 156 LYS   A CA    1 
ATOM   1105 C C     . LYS   A 1 156 ? -23.372 -16.255 -6.578  1.00 22.63 ? 156 LYS   A C     1 
ATOM   1106 O O     . LYS   A 1 156 ? -23.417 -15.418 -7.482  1.00 22.53 ? 156 LYS   A O     1 
ATOM   1107 C CB    . LYS   A 1 156 ? -25.635 -17.405 -6.623  1.00 24.34 ? 156 LYS   A CB    1 
ATOM   1108 N N     . PHE   A 1 157 ? -22.239 -16.890 -6.224  1.00 23.25 ? 157 PHE   A N     1 
ATOM   1109 C CA    . PHE   A 1 157 ? -20.964 -16.582 -6.852  1.00 20.65 ? 157 PHE   A CA    1 
ATOM   1110 C C     . PHE   A 1 157 ? -20.552 -17.636 -7.872  1.00 23.08 ? 157 PHE   A C     1 
ATOM   1111 O O     . PHE   A 1 157 ? -21.039 -18.775 -7.846  1.00 24.08 ? 157 PHE   A O     1 
ATOM   1112 C CB    . PHE   A 1 157 ? -19.831 -16.403 -5.846  1.00 23.28 ? 157 PHE   A CB    1 
ATOM   1113 C CG    . PHE   A 1 157 ? -20.219 -15.400 -4.763  1.00 22.83 ? 157 PHE   A CG    1 
ATOM   1114 C CD1   . PHE   A 1 157 ? -20.066 -14.038 -4.957  1.00 23.02 ? 157 PHE   A CD1   1 
ATOM   1115 C CD2   . PHE   A 1 157 ? -20.790 -15.836 -3.579  1.00 22.21 ? 157 PHE   A CD2   1 
ATOM   1116 C CE1   . PHE   A 1 157 ? -20.446 -13.126 -3.979  1.00 23.06 ? 157 PHE   A CE1   1 
ATOM   1117 C CE2   . PHE   A 1 157 ? -21.187 -14.933 -2.615  1.00 22.40 ? 157 PHE   A CE2   1 
ATOM   1118 C CZ    . PHE   A 1 157 ? -20.987 -13.575 -2.797  1.00 24.54 ? 157 PHE   A CZ    1 
ATOM   1119 N N     . ARG   A 1 158 ? -19.550 -17.275 -8.690  1.00 22.85 ? 158 ARG   A N     1 
ATOM   1120 C CA    . ARG   A 1 158 ? -19.049 -18.175 -9.727  1.00 24.11 ? 158 ARG   A CA    1 
ATOM   1121 C C     . ARG   A 1 158 ? -18.399 -19.447 -9.165  1.00 28.44 ? 158 ARG   A C     1 
ATOM   1122 O O     . ARG   A 1 158 ? -18.344 -20.470 -9.849  1.00 27.88 ? 158 ARG   A O     1 
ATOM   1123 C CB    . ARG   A 1 158 ? -18.032 -17.464 -10.620 1.00 25.50 ? 158 ARG   A CB    1 
ATOM   1124 C CG    . ARG   A 1 158 ? -18.727 -16.527 -11.588 1.00 25.41 ? 158 ARG   A CG    1 
ATOM   1125 C CD    . ARG   A 1 158 ? -17.802 -16.099 -12.684 1.00 25.97 ? 158 ARG   A CD    1 
ATOM   1126 N NE    . ARG   A 1 158 ? -18.422 -15.018 -13.446 1.00 27.78 ? 158 ARG   A NE    1 
ATOM   1127 C CZ    . ARG   A 1 158 ? -17.968 -14.604 -14.605 1.00 28.35 ? 158 ARG   A CZ    1 
ATOM   1128 N NH1   . ARG   A 1 158 ? -16.915 -15.205 -15.119 1.00 29.03 ? 158 ARG   A NH1   1 
ATOM   1129 N NH2   . ARG   A 1 158 ? -18.571 -13.598 -15.218 1.00 26.26 ? 158 ARG   A NH2   1 
ATOM   1130 N N     . ASP   A 1 159 ? -17.941 -19.409 -7.915  1.00 29.64 ? 159 ASP   A N     1 
ATOM   1131 C CA    . ASP   A 1 159 ? -17.349 -20.570 -7.271  1.00 33.75 ? 159 ASP   A CA    1 
ATOM   1132 C C     . ASP   A 1 159 ? -18.404 -21.557 -6.753  1.00 33.94 ? 159 ASP   A C     1 
ATOM   1133 O O     . ASP   A 1 159 ? -18.031 -22.561 -6.136  1.00 36.64 ? 159 ASP   A O     1 
ATOM   1134 C CB    . ASP   A 1 159 ? -16.456 -20.132 -6.120  1.00 34.69 ? 159 ASP   A CB    1 
ATOM   1135 C CG    . ASP   A 1 159 ? -17.167 -19.481 -4.938  1.00 34.64 ? 159 ASP   A CG    1 
ATOM   1136 O OD1   . ASP   A 1 159 ? -18.422 -19.364 -4.989  1.00 32.44 ? 159 ASP   A OD1   1 
ATOM   1137 O OD2   . ASP   A 1 159 ? -16.463 -19.097 -3.967  1.00 33.57 ? 159 ASP   A OD2   1 
ATOM   1138 N N     . GLY   A 1 160 ? -19.691 -21.229 -6.891  1.00 29.95 ? 160 GLY   A N     1 
ATOM   1139 C CA    . GLY   A 1 160 ? -20.785 -22.118 -6.525  1.00 33.49 ? 160 GLY   A CA    1 
ATOM   1140 C C     . GLY   A 1 160 ? -21.325 -21.866 -5.115  1.00 34.87 ? 160 GLY   A C     1 
ATOM   1141 O O     . GLY   A 1 160 ? -22.323 -22.469 -4.738  1.00 33.20 ? 160 GLY   A O     1 
ATOM   1142 N N     . GLU   A 1 161 ? -20.669 -20.980 -4.347  1.00 32.33 ? 161 GLU   A N     1 
ATOM   1143 C CA    A GLU   A 1 161 ? -21.055 -20.686 -2.976  0.50 33.96 ? 161 GLU   A CA    1 
ATOM   1144 C CA    B GLU   A 1 161 ? -21.068 -20.695 -2.979  0.50 34.28 ? 161 GLU   A CA    1 
ATOM   1145 C C     . GLU   A 1 161 ? -22.108 -19.577 -2.973  1.00 32.62 ? 161 GLU   A C     1 
ATOM   1146 O O     . GLU   A 1 161 ? -22.280 -18.865 -3.975  1.00 29.07 ? 161 GLU   A O     1 
ATOM   1147 C CB    A GLU   A 1 161 ? -19.827 -20.260 -2.169  0.50 35.10 ? 161 GLU   A CB    1 
ATOM   1148 C CB    B GLU   A 1 161 ? -19.828 -20.350 -2.156  0.50 35.97 ? 161 GLU   A CB    1 
ATOM   1149 C CG    A GLU   A 1 161 ? -18.708 -21.301 -2.129  0.50 38.03 ? 161 GLU   A CG    1 
ATOM   1150 C CG    B GLU   A 1 161 ? -18.781 -21.461 -2.203  0.50 39.24 ? 161 GLU   A CG    1 
ATOM   1151 C CD    A GLU   A 1 161 ? -18.997 -22.541 -1.294  0.50 36.82 ? 161 GLU   A CD    1 
ATOM   1152 C CD    B GLU   A 1 161 ? -17.717 -21.408 -1.124  0.50 39.36 ? 161 GLU   A CD    1 
ATOM   1153 O OE1   A GLU   A 1 161 ? -19.497 -22.371 -0.172  0.50 39.98 ? 161 GLU   A OE1   1 
ATOM   1154 O OE1   B GLU   A 1 161 ? -17.641 -20.405 -0.400  0.50 36.77 ? 161 GLU   A OE1   1 
ATOM   1155 O OE2   A GLU   A 1 161 ? -18.696 -23.664 -1.744  0.50 39.94 ? 161 GLU   A OE2   1 
ATOM   1156 O OE2   B GLU   A 1 161 ? -16.972 -22.397 -1.008  0.50 44.76 ? 161 GLU   A OE2   1 
ATOM   1157 N N     . ILE   A 1 162 ? -22.797 -19.435 -1.836  1.00 29.35 ? 162 ILE   A N     1 
ATOM   1158 C CA    . ILE   A 1 162 ? -23.800 -18.402 -1.671  1.00 28.77 ? 162 ILE   A CA    1 
ATOM   1159 C C     . ILE   A 1 162 ? -23.471 -17.608 -0.410  1.00 31.18 ? 162 ILE   A C     1 
ATOM   1160 O O     . ILE   A 1 162 ? -22.627 -17.988 0.389   1.00 30.94 ? 162 ILE   A O     1 
ATOM   1161 C CB    . ILE   A 1 162 ? -25.239 -18.946 -1.608  1.00 31.11 ? 162 ILE   A CB    1 
ATOM   1162 C CG1   . ILE   A 1 162 ? -25.493 -19.769 -0.334  1.00 33.51 ? 162 ILE   A CG1   1 
ATOM   1163 C CG2   . ILE   A 1 162 ? -25.597 -19.756 -2.851  1.00 29.91 ? 162 ILE   A CG2   1 
ATOM   1164 C CD1   . ILE   A 1 162 ? -26.910 -20.300 -0.238  1.00 34.84 ? 162 ILE   A CD1   1 
ATOM   1165 N N     . ALA   A 1 163 ? -24.140 -16.473 -0.286  1.00 27.57 ? 163 ALA   A N     1 
ATOM   1166 C CA    . ALA   A 1 163 ? -24.128 -15.679 0.925   1.00 29.59 ? 163 ALA   A CA    1 
ATOM   1167 C C     . ALA   A 1 163 ? -25.482 -14.975 1.038   1.00 28.28 ? 163 ALA   A C     1 
ATOM   1168 O O     . ALA   A 1 163 ? -26.203 -14.840 0.044   1.00 28.35 ? 163 ALA   A O     1 
ATOM   1169 C CB    . ALA   A 1 163 ? -22.970 -14.700 0.876   1.00 29.95 ? 163 ALA   A CB    1 
ATOM   1170 N N     . HIS   A 1 164 ? -25.808 -14.507 2.248   1.00 23.18 ? 164 HIS   A N     1 
ATOM   1171 C CA    . HIS   A 1 164 ? -27.086 -13.876 2.513   1.00 26.58 ? 164 HIS   A CA    1 
ATOM   1172 C C     . HIS   A 1 164 ? -26.863 -12.447 2.966   1.00 24.21 ? 164 HIS   A C     1 
ATOM   1173 O O     . HIS   A 1 164 ? -25.845 -12.171 3.589   1.00 25.56 ? 164 HIS   A O     1 
ATOM   1174 C CB    . HIS   A 1 164 ? -27.831 -14.642 3.609   1.00 29.01 ? 164 HIS   A CB    1 
ATOM   1175 C CG    . HIS   A 1 164 ? -28.078 -16.041 3.181   1.00 32.45 ? 164 HIS   A CG    1 
ATOM   1176 N ND1   . HIS   A 1 164 ? -29.296 -16.419 2.669   1.00 37.96 ? 164 HIS   A ND1   1 
ATOM   1177 C CD2   . HIS   A 1 164 ? -27.292 -17.128 3.153   1.00 37.02 ? 164 HIS   A CD2   1 
ATOM   1178 C CE1   . HIS   A 1 164 ? -29.247 -17.708 2.359   1.00 37.37 ? 164 HIS   A CE1   1 
ATOM   1179 N NE2   . HIS   A 1 164 ? -28.043 -18.158 2.649   1.00 37.99 ? 164 HIS   A NE2   1 
ATOM   1180 N N     . ALA   A 1 165 ? -27.834 -11.569 2.679   1.00 23.48 ? 165 ALA   A N     1 
ATOM   1181 C CA    . ALA   A 1 165 ? -27.754 -10.187 3.125   1.00 23.57 ? 165 ALA   A CA    1 
ATOM   1182 C C     . ALA   A 1 165 ? -29.150 -9.589  3.147   1.00 23.69 ? 165 ALA   A C     1 
ATOM   1183 O O     . ALA   A 1 165 ? -30.059 -10.086 2.483   1.00 24.05 ? 165 ALA   A O     1 
ATOM   1184 C CB    . ALA   A 1 165 ? -26.820 -9.389  2.217   1.00 26.28 ? 165 ALA   A CB    1 
ATOM   1185 N N     . ASP   A 1 166 ? -29.305 -8.494  3.890   1.00 20.70 ? 166 ASP   A N     1 
ATOM   1186 C CA    . ASP   A 1 166 ? -30.549 -7.756  3.936   1.00 24.10 ? 166 ASP   A CA    1 
ATOM   1187 C C     . ASP   A 1 166 ? -30.643 -6.817  2.740   1.00 23.90 ? 166 ASP   A C     1 
ATOM   1188 O O     . ASP   A 1 166 ? -31.744 -6.595  2.267   1.00 25.35 ? 166 ASP   A O     1 
ATOM   1189 C CB    . ASP   A 1 166 ? -30.716 -7.042  5.260   1.00 23.57 ? 166 ASP   A CB    1 
ATOM   1190 C CG    . ASP   A 1 166 ? -30.830 -8.019  6.421   1.00 26.34 ? 166 ASP   A CG    1 
ATOM   1191 O OD1   . ASP   A 1 166 ? -31.898 -8.642  6.535   1.00 28.52 ? 166 ASP   A OD1   1 
ATOM   1192 O OD2   . ASP   A 1 166 ? -29.802 -8.267  7.085   1.00 30.16 ? 166 ASP   A OD2   1 
ATOM   1193 N N     . VAL   A 1 167 ? -29.490 -6.296  2.290   1.00 21.48 ? 167 VAL   A N     1 
ATOM   1194 C CA    . VAL   A 1 167 ? -29.420 -5.400  1.144   1.00 20.96 ? 167 VAL   A CA    1 
ATOM   1195 C C     . VAL   A 1 167 ? -28.151 -5.736  0.370   1.00 20.49 ? 167 VAL   A C     1 
ATOM   1196 O O     . VAL   A 1 167 ? -27.154 -6.195  0.934   1.00 20.26 ? 167 VAL   A O     1 
ATOM   1197 C CB    . VAL   A 1 167 ? -29.467 -3.895  1.471   1.00 24.42 ? 167 VAL   A CB    1 
ATOM   1198 C CG1   . VAL   A 1 167 ? -30.843 -3.426  1.921   1.00 22.65 ? 167 VAL   A CG1   1 
ATOM   1199 C CG2   . VAL   A 1 167 ? -28.384 -3.507  2.463   1.00 24.68 ? 167 VAL   A CG2   1 
ATOM   1200 N N     . VAL   A 1 168 ? -28.195 -5.497  -0.955  1.00 19.81 ? 168 VAL   A N     1 
ATOM   1201 C CA    . VAL   A 1 168 ? -27.086 -5.770  -1.826  1.00 19.07 ? 168 VAL   A CA    1 
ATOM   1202 C C     . VAL   A 1 168 ? -26.764 -4.467  -2.539  1.00 19.86 ? 168 VAL   A C     1 
ATOM   1203 O O     . VAL   A 1 168 ? -27.683 -3.908  -3.146  1.00 18.41 ? 168 VAL   A O     1 
ATOM   1204 C CB    . VAL   A 1 168 ? -27.370 -6.873  -2.852  1.00 21.08 ? 168 VAL   A CB    1 
ATOM   1205 C CG1   . VAL   A 1 168 ? -26.179 -7.083  -3.745  1.00 21.13 ? 168 VAL   A CG1   1 
ATOM   1206 C CG2   . VAL   A 1 168 ? -27.738 -8.188  -2.150  1.00 22.66 ? 168 VAL   A CG2   1 
ATOM   1207 N N     . ILE   A 1 169 ? -25.511 -4.036  -2.396  1.00 19.86 ? 169 ILE   A N     1 
ATOM   1208 C CA    . ILE   A 1 169 ? -25.052 -2.772  -2.975  1.00 20.28 ? 169 ILE   A CA    1 
ATOM   1209 C C     . ILE   A 1 169 ? -24.090 -3.110  -4.100  1.00 18.89 ? 169 ILE   A C     1 
ATOM   1210 O O     . ILE   A 1 169 ? -22.980 -3.598  -3.862  1.00 20.33 ? 169 ILE   A O     1 
ATOM   1211 C CB    . ILE   A 1 169 ? -24.401 -1.806  -1.969  1.00 19.94 ? 169 ILE   A CB    1 
ATOM   1212 C CG1   . ILE   A 1 169 ? -25.035 -1.786  -0.564  1.00 19.53 ? 169 ILE   A CG1   1 
ATOM   1213 C CG2   . ILE   A 1 169 ? -24.339 -0.401  -2.579  1.00 20.96 ? 169 ILE   A CG2   1 
ATOM   1214 C CD1   . ILE   A 1 169 ? -26.471 -1.367  -0.463  1.00 19.88 ? 169 ILE   A CD1   1 
ATOM   1215 N N     . GLY   A 1 170 ? -24.550 -2.841  -5.346  1.00 17.99 ? 170 GLY   A N     1 
ATOM   1216 C CA    . GLY   A 1 170 ? -23.732 -3.063  -6.523  1.00 19.06 ? 170 GLY   A CA    1 
ATOM   1217 C C     . GLY   A 1 170 ? -22.737 -1.930  -6.706  1.00 19.73 ? 170 GLY   A C     1 
ATOM   1218 O O     . GLY   A 1 170 ? -23.119 -0.837  -7.158  1.00 21.27 ? 170 GLY   A O     1 
ATOM   1219 N N     . CYS   A 1 171 ? -21.488 -2.170  -6.247  1.00 17.97 ? 171 CYS   A N     1 
ATOM   1220 C CA    . CYS   A 1 171 ? -20.402 -1.220  -6.383  1.00 18.82 ? 171 CYS   A CA    1 
ATOM   1221 C C     . CYS   A 1 171 ? -19.373 -1.828  -7.341  1.00 19.07 ? 171 CYS   A C     1 
ATOM   1222 O O     . CYS   A 1 171 ? -18.174 -1.591  -7.232  1.00 19.50 ? 171 CYS   A O     1 
ATOM   1223 C CB    . CYS   A 1 171 ? -19.746 -0.893  -5.046  1.00 19.94 ? 171 CYS   A CB    1 
ATOM   1224 S SG    . CYS   A 1 171 ? -20.880 -0.190  -3.825  1.00 21.60 ? 171 CYS   A SG    1 
ATOM   1225 N N     . ASP   A 1 172 ? -19.884 -2.559  -8.342  1.00 19.79 ? 172 ASP   A N     1 
ATOM   1226 C CA    . ASP   A 1 172 ? -19.105 -3.494  -9.136  1.00 19.42 ? 172 ASP   A CA    1 
ATOM   1227 C C     . ASP   A 1 172 ? -18.767 -2.901  -10.503 1.00 18.88 ? 172 ASP   A C     1 
ATOM   1228 O O     . ASP   A 1 172 ? -18.371 -3.621  -11.424 1.00 22.26 ? 172 ASP   A O     1 
ATOM   1229 C CB    . ASP   A 1 172 ? -19.797 -4.857  -9.175  1.00 20.05 ? 172 ASP   A CB    1 
ATOM   1230 C CG    . ASP   A 1 172 ? -21.263 -4.933  -9.565  1.00 21.01 ? 172 ASP   A CG    1 
ATOM   1231 O OD1   . ASP   A 1 172 ? -21.999 -3.935  -9.419  1.00 21.52 ? 172 ASP   A OD1   1 
ATOM   1232 O OD2   . ASP   A 1 172 ? -21.691 -6.009  -10.037 1.00 21.21 ? 172 ASP   A OD2   1 
ATOM   1233 N N     . GLY   A 1 173 ? -18.880 -1.577  -10.638 1.00 20.24 ? 173 GLY   A N     1 
ATOM   1234 C CA    . GLY   A 1 173 ? -18.229 -0.873  -11.746 1.00 19.46 ? 173 GLY   A CA    1 
ATOM   1235 C C     . GLY   A 1 173 ? -19.068 -0.787  -13.019 1.00 19.54 ? 173 GLY   A C     1 
ATOM   1236 O O     . GLY   A 1 173 ? -20.228 -1.204  -13.085 1.00 20.11 ? 173 GLY   A O     1 
ATOM   1237 N N     . ILE   A 1 174 ? -18.386 -0.320  -14.085 1.00 18.39 ? 174 ILE   A N     1 
ATOM   1238 C CA    . ILE   A 1 174 ? -19.017 -0.010  -15.352 1.00 19.36 ? 174 ILE   A CA    1 
ATOM   1239 C C     . ILE   A 1 174 ? -19.716 -1.198  -16.017 1.00 18.55 ? 174 ILE   A C     1 
ATOM   1240 O O     . ILE   A 1 174 ? -20.665 -0.980  -16.761 1.00 20.99 ? 174 ILE   A O     1 
ATOM   1241 C CB    . ILE   A 1 174 ? -17.955 0.652   -16.241 1.00 21.18 ? 174 ILE   A CB    1 
ATOM   1242 C CG1   . ILE   A 1 174 ? -18.567 1.294   -17.455 1.00 21.74 ? 174 ILE   A CG1   1 
ATOM   1243 C CG2   . ILE   A 1 174 ? -16.807 -0.306  -16.574 1.00 20.61 ? 174 ILE   A CG2   1 
ATOM   1244 C CD1   . ILE   A 1 174 ? -17.668 2.311   -18.120 1.00 24.95 ? 174 ILE   A CD1   1 
ATOM   1245 N N     . ARG   A 1 175 ? -19.281 -2.435  -15.743 1.00 20.02 ? 175 ARG   A N     1 
ATOM   1246 C CA    . ARG   A 1 175 ? -19.908 -3.620  -16.292 1.00 21.33 ? 175 ARG   A CA    1 
ATOM   1247 C C     . ARG   A 1 175 ? -20.490 -4.451  -15.150 1.00 20.73 ? 175 ARG   A C     1 
ATOM   1248 O O     . ARG   A 1 175 ? -20.319 -5.665  -15.112 1.00 21.67 ? 175 ARG   A O     1 
ATOM   1249 C CB    . ARG   A 1 175 ? -18.907 -4.361  -17.181 1.00 24.20 ? 175 ARG   A CB    1 
ATOM   1250 C CG    . ARG   A 1 175 ? -18.782 -3.603  -18.502 1.00 27.48 ? 175 ARG   A CG    1 
ATOM   1251 C CD    . ARG   A 1 175 ? -17.901 -4.392  -19.476 1.00 29.99 ? 175 ARG   A CD    1 
ATOM   1252 N NE    . ARG   A 1 175 ? -16.569 -4.706  -18.944 1.00 30.78 ? 175 ARG   A NE    1 
ATOM   1253 C CZ    . ARG   A 1 175 ? -15.775 -5.664  -19.455 1.00 34.89 ? 175 ARG   A CZ    1 
ATOM   1254 N NH1   . ARG   A 1 175 ? -16.203 -6.388  -20.485 1.00 35.10 ? 175 ARG   A NH1   1 
ATOM   1255 N NH2   . ARG   A 1 175 ? -14.579 -5.925  -18.928 1.00 31.87 ? 175 ARG   A NH2   1 
ATOM   1256 N N     . SER   A 1 176 ? -21.191 -3.755  -14.260 1.00 22.32 ? 176 SER   A N     1 
ATOM   1257 C CA    . SER   A 1 176 ? -21.852 -4.308  -13.083 1.00 22.02 ? 176 SER   A CA    1 
ATOM   1258 C C     . SER   A 1 176 ? -22.711 -5.533  -13.382 1.00 19.64 ? 176 SER   A C     1 
ATOM   1259 O O     . SER   A 1 176 ? -23.637 -5.485  -14.200 1.00 21.57 ? 176 SER   A O     1 
ATOM   1260 C CB    . SER   A 1 176 ? -22.721 -3.225  -12.453 1.00 23.43 ? 176 SER   A CB    1 
ATOM   1261 O OG    . SER   A 1 176 ? -23.594 -3.742  -11.453 1.00 20.79 ? 176 SER   A OG    1 
ATOM   1262 N N     . GLN   A 1 177 ? -22.441 -6.619  -12.643 1.00 20.41 ? 177 GLN   A N     1 
ATOM   1263 C CA    . GLN   A 1 177 ? -23.286 -7.804  -12.633 1.00 20.69 ? 177 GLN   A CA    1 
ATOM   1264 C C     . GLN   A 1 177 ? -24.535 -7.538  -11.796 1.00 22.06 ? 177 GLN   A C     1 
ATOM   1265 O O     . GLN   A 1 177 ? -25.593 -8.045  -12.119 1.00 20.16 ? 177 GLN   A O     1 
ATOM   1266 C CB    . GLN   A 1 177 ? -22.536 -9.031  -12.106 1.00 21.72 ? 177 GLN   A CB    1 
ATOM   1267 C CG    . GLN   A 1 177 ? -23.268 -10.358 -12.282 1.00 22.38 ? 177 GLN   A CG    1 
ATOM   1268 C CD    . GLN   A 1 177 ? -23.330 -10.850 -13.708 1.00 25.14 ? 177 GLN   A CD    1 
ATOM   1269 O OE1   . GLN   A 1 177 ? -22.775 -10.249 -14.632 1.00 23.09 ? 177 GLN   A OE1   1 
ATOM   1270 N NE2   . GLN   A 1 177 ? -24.049 -11.945 -13.906 1.00 27.90 ? 177 GLN   A NE2   1 
ATOM   1271 N N     . VAL   A 1 178 ? -24.429 -6.731  -10.747 1.00 19.90 ? 178 VAL   A N     1 
ATOM   1272 C CA    . VAL   A 1 178 ? -25.654 -6.386  -9.973  1.00 22.04 ? 178 VAL   A CA    1 
ATOM   1273 C C     . VAL   A 1 178 ? -26.666 -5.678  -10.902 1.00 21.00 ? 178 VAL   A C     1 
ATOM   1274 O O     . VAL   A 1 178 ? -27.843 -6.014  -10.842 1.00 21.19 ? 178 VAL   A O     1 
ATOM   1275 C CB    . VAL   A 1 178 ? -25.341 -5.561  -8.709  1.00 22.36 ? 178 VAL   A CB    1 
ATOM   1276 C CG1   . VAL   A 1 178 ? -26.598 -5.157  -7.965  1.00 23.27 ? 178 VAL   A CG1   1 
ATOM   1277 C CG2   . VAL   A 1 178 ? -24.381 -6.298  -7.788  1.00 22.04 ? 178 VAL   A CG2   1 
ATOM   1278 N N     . ARG   A 1 179 ? -26.195 -4.762  -11.746 1.00 19.95 ? 179 ARG   A N     1 
ATOM   1279 C CA    . ARG   A 1 179 ? -27.086 -4.056  -12.704 1.00 20.83 ? 179 ARG   A CA    1 
ATOM   1280 C C     . ARG   A 1 179 ? -27.784 -5.079  -13.618 1.00 21.26 ? 179 ARG   A C     1 
ATOM   1281 O O     . ARG   A 1 179 ? -28.981 -4.934  -13.854 1.00 20.72 ? 179 ARG   A O     1 
ATOM   1282 C CB    . ARG   A 1 179 ? -26.277 -3.061  -13.539 1.00 22.97 ? 179 ARG   A CB    1 
ATOM   1283 C CG    . ARG   A 1 179 ? -27.088 -2.156  -14.454 1.00 26.10 ? 179 ARG   A CG    1 
ATOM   1284 C CD    . ARG   A 1 179 ? -26.230 -1.531  -15.544 1.00 31.72 ? 179 ARG   A CD    1 
ATOM   1285 N NE    . ARG   A 1 179 ? -24.950 -1.029  -15.040 1.00 31.68 ? 179 ARG   A NE    1 
ATOM   1286 C CZ    . ARG   A 1 179 ? -23.843 -0.923  -15.753 1.00 25.68 ? 179 ARG   A CZ    1 
ATOM   1287 N NH1   . ARG   A 1 179 ? -22.967 0.010   -15.453 1.00 25.25 ? 179 ARG   A NH1   1 
ATOM   1288 N NH2   . ARG   A 1 179 ? -23.613 -1.748  -16.757 1.00 22.84 ? 179 ARG   A NH2   1 
ATOM   1289 N N     . ALA   A 1 180 ? -27.027 -6.062  -14.095 1.00 21.68 ? 180 ALA   A N     1 
ATOM   1290 C CA    . ALA   A 1 180 ? -27.592 -7.123  -14.951 1.00 23.25 ? 180 ALA   A CA    1 
ATOM   1291 C C     . ALA   A 1 180 ? -28.694 -7.852  -14.180 1.00 25.10 ? 180 ALA   A C     1 
ATOM   1292 O O     . ALA   A 1 180 ? -29.742 -8.157  -14.745 1.00 23.78 ? 180 ALA   A O     1 
ATOM   1293 C CB    . ALA   A 1 180 ? -26.496 -8.075  -15.345 1.00 24.74 ? 180 ALA   A CB    1 
ATOM   1294 N N     . SER   A 1 181 ? -28.432 -8.118  -12.900 1.00 22.85 ? 181 SER   A N     1 
ATOM   1295 C CA    . SER   A 1 181 ? -29.453 -8.792  -12.099 1.00 25.54 ? 181 SER   A CA    1 
ATOM   1296 C C     . SER   A 1 181 ? -30.741 -7.979  -12.035 1.00 23.91 ? 181 SER   A C     1 
ATOM   1297 O O     . SER   A 1 181 ? -31.833 -8.536  -11.986 1.00 24.22 ? 181 SER   A O     1 
ATOM   1298 C CB    . SER   A 1 181 ? -28.948 -9.077  -10.693 1.00 27.94 ? 181 SER   A CB    1 
ATOM   1299 O OG    . SER   A 1 181 ? -29.902 -9.904  -10.043 1.00 33.82 ? 181 SER   A OG    1 
ATOM   1300 N N     . MET   A 1 182 ? -30.619 -6.647  -11.989 1.00 22.79 ? 182 MET   A N     1 
ATOM   1301 C CA    . MET   A 1 182 ? -31.771 -5.793  -11.820 1.00 21.60 ? 182 MET   A CA    1 
ATOM   1302 C C     . MET   A 1 182 ? -32.522 -5.592  -13.139 1.00 22.25 ? 182 MET   A C     1 
ATOM   1303 O O     . MET   A 1 182 ? -33.754 -5.576  -13.121 1.00 24.66 ? 182 MET   A O     1 
ATOM   1304 C CB    . MET   A 1 182 ? -31.379 -4.419  -11.260 1.00 22.84 ? 182 MET   A CB    1 
ATOM   1305 C CG    . MET   A 1 182 ? -30.768 -4.451  -9.885  1.00 21.33 ? 182 MET   A CG    1 
ATOM   1306 S SD    . MET   A 1 182 ? -29.893 -2.951  -9.382  1.00 21.93 ? 182 MET   A SD    1 
ATOM   1307 C CE    . MET   A 1 182 ? -31.251 -1.814  -9.122  1.00 23.06 ? 182 MET   A CE    1 
ATOM   1308 N N     . PHE   A 1 183 ? -31.785 -5.404  -14.242 1.00 23.94 ? 183 PHE   A N     1 
ATOM   1309 C CA    . PHE   A 1 183 ? -32.370 -4.951  -15.495 1.00 27.93 ? 183 PHE   A CA    1 
ATOM   1310 C C     . PHE   A 1 183 ? -32.051 -5.816  -16.724 1.00 33.62 ? 183 PHE   A C     1 
ATOM   1311 O O     . PHE   A 1 183 ? -32.640 -5.554  -17.765 1.00 36.79 ? 183 PHE   A O     1 
ATOM   1312 C CB    . PHE   A 1 183 ? -31.890 -3.529  -15.784 1.00 27.47 ? 183 PHE   A CB    1 
ATOM   1313 C CG    . PHE   A 1 183 ? -32.167 -2.549  -14.657 1.00 24.00 ? 183 PHE   A CG    1 
ATOM   1314 C CD1   . PHE   A 1 183 ? -33.466 -2.208  -14.308 1.00 23.91 ? 183 PHE   A CD1   1 
ATOM   1315 C CD2   . PHE   A 1 183 ? -31.120 -1.963  -13.955 1.00 22.49 ? 183 PHE   A CD2   1 
ATOM   1316 C CE1   . PHE   A 1 183 ? -33.732 -1.341  -13.264 1.00 23.39 ? 183 PHE   A CE1   1 
ATOM   1317 C CE2   . PHE   A 1 183 ? -31.382 -1.093  -12.926 1.00 20.53 ? 183 PHE   A CE2   1 
ATOM   1318 C CZ    . PHE   A 1 183 ? -32.684 -0.782  -12.571 1.00 22.15 ? 183 PHE   A CZ    1 
ATOM   1319 N N     . GLY   A 1 184 ? -31.143 -6.804  -16.641 1.00 36.61 ? 184 GLY   A N     1 
ATOM   1320 C CA    . GLY   A 1 184 ? -30.760 -7.662  -17.766 1.00 37.33 ? 184 GLY   A CA    1 
ATOM   1321 C C     . GLY   A 1 184 ? -29.589 -7.070  -18.565 1.00 41.13 ? 184 GLY   A C     1 
ATOM   1322 O O     . GLY   A 1 184 ? -29.220 -5.928  -18.306 1.00 34.29 ? 184 GLY   A O     1 
ATOM   1323 N N     . THR   A 1 185 ? -29.033 -7.844  -19.511 1.00 43.17 ? 185 THR   A N     1 
ATOM   1324 C CA    . THR   A 1 185 ? -27.861 -7.397  -20.305 1.00 45.56 ? 185 THR   A CA    1 
ATOM   1325 C C     . THR   A 1 185 ? -28.067 -7.686  -21.786 1.00 46.48 ? 185 THR   A C     1 
ATOM   1326 O O     . THR   A 1 185 ? -27.068 -7.983  -22.474 1.00 43.28 ? 185 THR   A O     1 
ATOM   1327 C CB    . THR   A 1 185 ? -26.561 -8.025  -19.787 1.00 47.56 ? 185 THR   A CB    1 
ATOM   1328 O OG1   . THR   A 1 185 ? -26.895 -9.292  -19.232 1.00 54.00 ? 185 THR   A OG1   1 
ATOM   1329 C CG2   . THR   A 1 185 ? -25.878 -7.146  -18.758 1.00 48.63 ? 185 THR   A CG2   1 
ATOM   1330 N N     . ASP   A 1 186 ? -29.299 -7.596  -22.273 1.00 44.57 ? 186 ASP   A N     1 
ATOM   1331 C CA    . ASP   A 1 186 ? -29.549 -7.758  -23.731 1.00 49.83 ? 186 ASP   A CA    1 
ATOM   1332 C C     . ASP   A 1 186 ? -29.050 -6.510  -24.469 1.00 51.56 ? 186 ASP   A C     1 
ATOM   1333 O O     . ASP   A 1 186 ? -28.455 -5.638  -23.830 1.00 45.12 ? 186 ASP   A O     1 
ATOM   1334 C CB    . ASP   A 1 186 ? -31.016 -8.039  -24.019 1.00 49.63 ? 186 ASP   A CB    1 
ATOM   1335 N N     . GLU   A 1 187 ? -29.313 -6.423  -25.773 1.00 56.52 ? 187 GLU   A N     1 
ATOM   1336 C CA    . GLU   A 1 187 ? -28.789 -5.290  -26.578 1.00 55.94 ? 187 GLU   A CA    1 
ATOM   1337 C C     . GLU   A 1 187 ? -29.525 -3.991  -26.230 1.00 47.53 ? 187 GLU   A C     1 
ATOM   1338 O O     . GLU   A 1 187 ? -28.990 -2.932  -26.551 1.00 52.18 ? 187 GLU   A O     1 
ATOM   1339 C CB    . GLU   A 1 187 ? -28.911 -5.541  -28.082 1.00 60.01 ? 187 GLU   A CB    1 
ATOM   1340 N N     . LEU   A 1 188 ? -30.725 -4.076  -25.673 1.00 42.43 ? 188 LEU   A N     1 
ATOM   1341 C CA    . LEU   A 1 188 ? -31.460 -2.848  -25.389 1.00 46.09 ? 188 LEU   A CA    1 
ATOM   1342 C C     . LEU   A 1 188 ? -31.362 -2.458  -23.905 1.00 44.04 ? 188 LEU   A C     1 
ATOM   1343 O O     . LEU   A 1 188 ? -31.976 -1.477  -23.465 1.00 41.90 ? 188 LEU   A O     1 
ATOM   1344 C CB    . LEU   A 1 188 ? -32.912 -3.071  -25.823 1.00 43.76 ? 188 LEU   A CB    1 
ATOM   1345 N N     . CYS   A 1 189 ? -30.605 -3.227  -23.112 1.00 38.75 ? 189 CYS   A N     1 
ATOM   1346 C CA    . CYS   A 1 189 ? -30.655 -3.090  -21.662 1.00 34.60 ? 189 CYS   A CA    1 
ATOM   1347 C C     . CYS   A 1 189 ? -29.760 -1.927  -21.227 1.00 28.95 ? 189 CYS   A C     1 
ATOM   1348 O O     . CYS   A 1 189 ? -28.932 -1.456  -21.998 1.00 25.94 ? 189 CYS   A O     1 
ATOM   1349 C CB    . CYS   A 1 189 ? -30.288 -4.416  -21.008 1.00 41.92 ? 189 CYS   A CB    1 
ATOM   1350 S SG    . CYS   A 1 189 ? -31.582 -5.684  -21.171 1.00 49.92 ? 189 CYS   A SG    1 
ATOM   1351 N N     . PRO   A 1 190 ? -29.899 -1.386  -19.995 1.00 24.74 ? 190 PRO   A N     1 
ATOM   1352 C CA    . PRO   A 1 190 ? -28.993 -0.334  -19.531 1.00 24.83 ? 190 PRO   A CA    1 
ATOM   1353 C C     . PRO   A 1 190 ? -27.563 -0.845  -19.580 1.00 25.55 ? 190 PRO   A C     1 
ATOM   1354 O O     . PRO   A 1 190 ? -27.284 -1.996  -19.211 1.00 23.40 ? 190 PRO   A O     1 
ATOM   1355 C CB    . PRO   A 1 190 ? -29.461 -0.070  -18.079 1.00 26.80 ? 190 PRO   A CB    1 
ATOM   1356 C CG    . PRO   A 1 190 ? -30.897 -0.525  -18.068 1.00 25.79 ? 190 PRO   A CG    1 
ATOM   1357 C CD    . PRO   A 1 190 ? -30.901 -1.745  -18.974 1.00 24.52 ? 190 PRO   A CD    1 
ATOM   1358 N N     . ARG   A 1 191 ? -26.660 0.018   -20.052 1.00 25.87 ? 191 ARG   A N     1 
ATOM   1359 C CA    . ARG   A 1 191 ? -25.257 -0.317  -20.157 1.00 26.17 ? 191 ARG   A CA    1 
ATOM   1360 C C     . ARG   A 1 191 ? -24.456 0.928   -20.531 1.00 26.57 ? 191 ARG   A C     1 
ATOM   1361 O O     . ARG   A 1 191 ? -25.039 1.906   -20.996 1.00 25.25 ? 191 ARG   A O     1 
ATOM   1362 C CB    . ARG   A 1 191 ? -25.101 -1.369  -21.258 1.00 28.54 ? 191 ARG   A CB    1 
ATOM   1363 C CG    . ARG   A 1 191 ? -25.646 -0.860  -22.582 1.00 30.17 ? 191 ARG   A CG    1 
ATOM   1364 C CD    . ARG   A 1 191 ? -25.660 -2.013  -23.588 1.00 36.91 ? 191 ARG   A CD    1 
ATOM   1365 N NE    . ARG   A 1 191 ? -26.022 -1.519  -24.922 1.00 44.52 ? 191 ARG   A NE    1 
ATOM   1366 C CZ    . ARG   A 1 191 ? -27.206 -1.043  -25.324 1.00 47.16 ? 191 ARG   A CZ    1 
ATOM   1367 N NH1   . ARG   A 1 191 ? -28.248 -0.941  -24.506 1.00 42.20 ? 191 ARG   A NH1   1 
ATOM   1368 N NH2   . ARG   A 1 191 ? -27.347 -0.691  -26.590 1.00 53.83 ? 191 ARG   A NH2   1 
ATOM   1369 N N     . ALA   A 1 192 ? -23.135 0.861   -20.316 1.00 26.41 ? 192 ALA   A N     1 
ATOM   1370 C CA    . ALA   A 1 192 ? -22.207 1.884   -20.778 1.00 22.54 ? 192 ALA   A CA    1 
ATOM   1371 C C     . ALA   A 1 192 ? -21.853 1.653   -22.240 1.00 23.86 ? 192 ALA   A C     1 
ATOM   1372 O O     . ALA   A 1 192 ? -21.639 0.521   -22.682 1.00 24.82 ? 192 ALA   A O     1 
ATOM   1373 C CB    . ALA   A 1 192 ? -20.953 1.902   -19.928 1.00 22.92 ? 192 ALA   A CB    1 
ATOM   1374 N N     . GLN   A 1 193 ? -21.801 2.750   -22.990 1.00 20.84 ? 193 GLN   A N     1 
ATOM   1375 C CA    . GLN   A 1 193 ? -21.416 2.692   -24.388 1.00 23.25 ? 193 GLN   A CA    1 
ATOM   1376 C C     . GLN   A 1 193 ? -20.353 3.759   -24.650 1.00 22.80 ? 193 GLN   A C     1 
ATOM   1377 O O     . GLN   A 1 193 ? -20.113 4.621   -23.824 1.00 21.18 ? 193 GLN   A O     1 
ATOM   1378 C CB    . GLN   A 1 193 ? -22.661 2.866   -25.252 1.00 24.13 ? 193 GLN   A CB    1 
ATOM   1379 C CG    . GLN   A 1 193 ? -23.715 1.781   -25.045 1.00 23.32 ? 193 GLN   A CG    1 
ATOM   1380 C CD    . GLN   A 1 193 ? -24.940 2.056   -25.879 1.00 27.09 ? 193 GLN   A CD    1 
ATOM   1381 O OE1   . GLN   A 1 193 ? -25.972 2.548   -25.401 1.00 29.15 ? 193 GLN   A OE1   1 
ATOM   1382 N NE2   . GLN   A 1 193 ? -24.796 1.826   -27.171 1.00 30.34 ? 193 GLN   A NE2   1 
ATOM   1383 N N     . TYR   A 1 194 ? -19.690 3.682   -25.804 1.00 22.06 ? 194 TYR   A N     1 
ATOM   1384 C CA    . TYR   A 1 194 ? -18.562 4.553   -26.062 1.00 23.05 ? 194 TYR   A CA    1 
ATOM   1385 C C     . TYR   A 1 194 ? -19.051 5.991   -26.186 1.00 22.98 ? 194 TYR   A C     1 
ATOM   1386 O O     . TYR   A 1 194 ? -20.026 6.273   -26.855 1.00 23.44 ? 194 TYR   A O     1 
ATOM   1387 C CB    . TYR   A 1 194 ? -17.929 4.036   -27.358 1.00 24.77 ? 194 TYR   A CB    1 
ATOM   1388 C CG    . TYR   A 1 194 ? -16.688 4.766   -27.847 1.00 24.25 ? 194 TYR   A CG    1 
ATOM   1389 C CD1   . TYR   A 1 194 ? -15.669 5.112   -26.977 1.00 24.59 ? 194 TYR   A CD1   1 
ATOM   1390 C CD2   . TYR   A 1 194 ? -16.511 5.051   -29.200 1.00 26.07 ? 194 TYR   A CD2   1 
ATOM   1391 C CE1   . TYR   A 1 194 ? -14.526 5.743   -27.418 1.00 25.20 ? 194 TYR   A CE1   1 
ATOM   1392 C CE2   . TYR   A 1 194 ? -15.347 5.642   -29.661 1.00 24.98 ? 194 TYR   A CE2   1 
ATOM   1393 C CZ    . TYR   A 1 194 ? -14.359 6.006   -28.761 1.00 26.57 ? 194 TYR   A CZ    1 
ATOM   1394 O OH    . TYR   A 1 194 ? -13.194 6.600   -29.130 1.00 28.33 ? 194 TYR   A OH    1 
ATOM   1395 N N     . SER   A 1 195 ? -18.348 6.895   -25.523 1.00 20.53 ? 195 SER   A N     1 
ATOM   1396 C CA    . SER   A 1 195 ? -18.657 8.314   -25.500 1.00 23.09 ? 195 SER   A CA    1 
ATOM   1397 C C     . SER   A 1 195 ? -17.972 9.072   -26.635 1.00 22.15 ? 195 SER   A C     1 
ATOM   1398 O O     . SER   A 1 195 ? -18.108 10.286  -26.693 1.00 22.96 ? 195 SER   A O     1 
ATOM   1399 C CB    . SER   A 1 195 ? -18.229 8.914   -24.182 1.00 23.08 ? 195 SER   A CB    1 
ATOM   1400 O OG    . SER   A 1 195 ? -16.814 8.940   -24.044 1.00 23.71 ? 195 SER   A OG    1 
ATOM   1401 N N     . HIS   A 1 196 ? -17.213 8.387   -27.489 1.00 25.60 ? 196 HIS   A N     1 
ATOM   1402 C CA    . HIS   A 1 196 ? -16.528 9.023   -28.613 1.00 24.75 ? 196 HIS   A CA    1 
ATOM   1403 C C     . HIS   A 1 196 ? -15.383 9.943   -28.173 1.00 25.58 ? 196 HIS   A C     1 
ATOM   1404 O O     . HIS   A 1 196 ? -15.076 10.947  -28.811 1.00 26.79 ? 196 HIS   A O     1 
ATOM   1405 C CB    . HIS   A 1 196 ? -17.535 9.722   -29.539 1.00 27.26 ? 196 HIS   A CB    1 
ATOM   1406 C CG    . HIS   A 1 196 ? -18.549 8.795   -30.075 1.00 29.00 ? 196 HIS   A CG    1 
ATOM   1407 N ND1   . HIS   A 1 196 ? -18.201 7.749   -30.904 1.00 34.93 ? 196 HIS   A ND1   1 
ATOM   1408 C CD2   . HIS   A 1 196 ? -19.857 8.684   -29.851 1.00 32.87 ? 196 HIS   A CD2   1 
ATOM   1409 C CE1   . HIS   A 1 196 ? -19.294 7.047   -31.194 1.00 36.66 ? 196 HIS   A CE1   1 
ATOM   1410 N NE2   . HIS   A 1 196 ? -20.311 7.604   -30.576 1.00 36.56 ? 196 HIS   A NE2   1 
ATOM   1411 N N     . GLN   A 1 197 ? -14.758 9.609   -27.057 1.00 21.50 ? 197 GLN   A N     1 
ATOM   1412 C CA    . GLN   A 1 197 ? -13.675 10.361  -26.473 1.00 26.16 ? 197 GLN   A CA    1 
ATOM   1413 C C     . GLN   A 1 197 ? -12.585 9.378   -26.072 1.00 26.60 ? 197 GLN   A C     1 
ATOM   1414 O O     . GLN   A 1 197 ? -12.888 8.384   -25.410 1.00 24.28 ? 197 GLN   A O     1 
ATOM   1415 C CB    . GLN   A 1 197 ? -14.309 11.094  -25.313 1.00 29.05 ? 197 GLN   A CB    1 
ATOM   1416 C CG    . GLN   A 1 197 ? -13.334 11.574  -24.274 1.00 30.10 ? 197 GLN   A CG    1 
ATOM   1417 C CD    . GLN   A 1 197 ? -13.977 12.508  -23.274 1.00 29.20 ? 197 GLN   A CD    1 
ATOM   1418 O OE1   . GLN   A 1 197 ? -15.152 12.894  -23.383 1.00 26.77 ? 197 GLN   A OE1   1 
ATOM   1419 N NE2   . GLN   A 1 197 ? -13.147 12.919  -22.342 1.00 25.98 ? 197 GLN   A NE2   1 
ATOM   1420 N N     . LEU   A 1 198 ? -11.370 9.637   -26.573 1.00 23.70 ? 198 LEU   A N     1 
ATOM   1421 C CA    . LEU   A 1 198 ? -10.187 8.805   -26.393 1.00 24.23 ? 198 LEU   A CA    1 
ATOM   1422 C C     . LEU   A 1 198 ? -9.123  9.590   -25.640 1.00 24.65 ? 198 LEU   A C     1 
ATOM   1423 O O     . LEU   A 1 198 ? -8.756  10.688  -26.060 1.00 24.27 ? 198 LEU   A O     1 
ATOM   1424 C CB    . LEU   A 1 198 ? -9.618  8.430   -27.758 1.00 26.38 ? 198 LEU   A CB    1 
ATOM   1425 C CG    . LEU   A 1 198 ? -10.219 7.228   -28.472 1.00 30.12 ? 198 LEU   A CG    1 
ATOM   1426 C CD1   . LEU   A 1 198 ? -9.629  7.151   -29.873 1.00 29.09 ? 198 LEU   A CD1   1 
ATOM   1427 C CD2   . LEU   A 1 198 ? -9.928  5.964   -27.676 1.00 27.91 ? 198 LEU   A CD2   1 
ATOM   1428 N N     . GLY   A 1 199 ? -8.644  9.031   -24.538 1.00 23.09 ? 199 GLY   A N     1 
ATOM   1429 C CA    . GLY   A 1 199 ? -7.705  9.690   -23.646 1.00 25.79 ? 199 GLY   A CA    1 
ATOM   1430 C C     . GLY   A 1 199 ? -6.275  9.166   -23.843 1.00 28.69 ? 199 GLY   A C     1 
ATOM   1431 O O     . GLY   A 1 199 ? -6.041  7.950   -23.911 1.00 25.08 ? 199 GLY   A O     1 
ATOM   1432 N N     . TYR   A 1 200 ? -5.348  10.114  -23.936 1.00 26.29 ? 200 TYR   A N     1 
ATOM   1433 C CA    . TYR   A 1 200 ? -3.913  9.858   -24.005 1.00 27.28 ? 200 TYR   A CA    1 
ATOM   1434 C C     . TYR   A 1 200 ? -3.295  10.599  -22.827 1.00 27.39 ? 200 TYR   A C     1 
ATOM   1435 O O     . TYR   A 1 200 ? -3.558  11.790  -22.643 1.00 28.20 ? 200 TYR   A O     1 
ATOM   1436 C CB    . TYR   A 1 200 ? -3.319  10.340  -25.338 1.00 27.19 ? 200 TYR   A CB    1 
ATOM   1437 C CG    . TYR   A 1 200 ? -3.937  9.753   -26.598 1.00 29.08 ? 200 TYR   A CG    1 
ATOM   1438 C CD1   . TYR   A 1 200 ? -5.212  10.111  -27.015 1.00 27.27 ? 200 TYR   A CD1   1 
ATOM   1439 C CD2   . TYR   A 1 200 ? -3.235  8.853   -27.396 1.00 26.13 ? 200 TYR   A CD2   1 
ATOM   1440 C CE1   . TYR   A 1 200 ? -5.772  9.583   -28.169 1.00 31.81 ? 200 TYR   A CE1   1 
ATOM   1441 C CE2   . TYR   A 1 200 ? -3.777  8.347   -28.561 1.00 26.02 ? 200 TYR   A CE2   1 
ATOM   1442 C CZ    . TYR   A 1 200 ? -5.051  8.699   -28.951 1.00 28.70 ? 200 TYR   A CZ    1 
ATOM   1443 O OH    . TYR   A 1 200 ? -5.593  8.181   -30.101 1.00 28.53 ? 200 TYR   A OH    1 
ATOM   1444 N N     . ARG   A 1 201 ? -2.548  9.864   -22.017 1.00 25.43 ? 201 ARG   A N     1 
ATOM   1445 C CA    . ARG   A 1 201 ? -2.054  10.459  -20.762 1.00 29.07 ? 201 ARG   A CA    1 
ATOM   1446 C C     . ARG   A 1 201 ? -0.557  10.217  -20.560 1.00 32.87 ? 201 ARG   A C     1 
ATOM   1447 O O     . ARG   A 1 201 ? -0.047  9.178   -20.989 1.00 31.01 ? 201 ARG   A O     1 
ATOM   1448 C CB    . ARG   A 1 201 ? -2.844  9.901   -19.578 1.00 35.15 ? 201 ARG   A CB    1 
ATOM   1449 C CG    . ARG   A 1 201 ? -4.330  10.189  -19.722 1.00 44.79 ? 201 ARG   A CG    1 
ATOM   1450 C CD    . ARG   A 1 201 ? -5.240  9.154   -19.092 1.00 47.27 ? 201 ARG   A CD    1 
ATOM   1451 N NE    . ARG   A 1 201 ? -5.430  7.923   -19.862 1.00 54.06 ? 201 ARG   A NE    1 
ATOM   1452 C CZ    . ARG   A 1 201 ? -5.717  6.766   -19.283 1.00 58.95 ? 201 ARG   A CZ    1 
ATOM   1453 N NH1   . ARG   A 1 201 ? -6.411  6.752   -18.157 1.00 48.21 ? 201 ARG   A NH1   1 
ATOM   1454 N NH2   . ARG   A 1 201 ? -5.299  5.635   -19.821 1.00 57.97 ? 201 ARG   A NH2   1 
ATOM   1455 N N     . GLY   A 1 202 ? 0.080   11.177  -19.915 1.00 34.36 ? 202 GLY   A N     1 
ATOM   1456 C CA    . GLY   A 1 202 ? 1.510   11.117  -19.641 1.00 33.62 ? 202 GLY   A CA    1 
ATOM   1457 C C     . GLY   A 1 202 ? 1.914   12.027  -18.488 1.00 32.58 ? 202 GLY   A C     1 
ATOM   1458 O O     . GLY   A 1 202 ? 1.219   12.981  -18.147 1.00 28.38 ? 202 GLY   A O     1 
ATOM   1459 N N     . MET   A 1 203 ? 3.062   11.697  -17.876 1.00 31.94 ? 203 MET   A N     1 
ATOM   1460 C CA    . MET   A 1 203 ? 3.639   12.436  -16.769 1.00 34.89 ? 203 MET   A CA    1 
ATOM   1461 C C     . MET   A 1 203 ? 5.092   12.715  -17.158 1.00 33.10 ? 203 MET   A C     1 
ATOM   1462 O O     . MET   A 1 203 ? 5.791   11.810  -17.598 1.00 34.82 ? 203 MET   A O     1 
ATOM   1463 C CB    . MET   A 1 203 ? 3.685   11.623  -15.465 1.00 41.60 ? 203 MET   A CB    1 
ATOM   1464 C CG    . MET   A 1 203 ? 2.391   11.528  -14.665 1.00 47.72 ? 203 MET   A CG    1 
ATOM   1465 S SD    . MET   A 1 203 ? 2.070   12.965  -13.624 1.00 50.25 ? 203 MET   A SD    1 
ATOM   1466 C CE    . MET   A 1 203 ? 1.176   12.277  -12.223 1.00 63.19 ? 203 MET   A CE    1 
ATOM   1467 N N     . VAL   A 1 204 ? 5.528   13.962  -17.026 1.00 30.35 ? 204 VAL   A N     1 
ATOM   1468 C CA    . VAL   A 1 204 ? 6.917   14.310  -17.268 1.00 29.74 ? 204 VAL   A CA    1 
ATOM   1469 C C     . VAL   A 1 204 ? 7.402   15.125  -16.079 1.00 26.59 ? 204 VAL   A C     1 
ATOM   1470 O O     . VAL   A 1 204 ? 6.597   15.652  -15.313 1.00 29.26 ? 204 VAL   A O     1 
ATOM   1471 C CB    . VAL   A 1 204 ? 7.123   15.091  -18.577 1.00 27.58 ? 204 VAL   A CB    1 
ATOM   1472 C CG1   . VAL   A 1 204 ? 6.638   14.295  -19.780 1.00 30.07 ? 204 VAL   A CG1   1 
ATOM   1473 C CG2   . VAL   A 1 204 ? 6.501   16.483  -18.505 1.00 27.14 ? 204 VAL   A CG2   1 
ATOM   1474 N N     . PRO   A 1 205 ? 8.729   15.302  -15.885 1.00 27.80 ? 205 PRO   A N     1 
ATOM   1475 C CA    . PRO   A 1 205 ? 9.213   16.174  -14.824 1.00 26.38 ? 205 PRO   A CA    1 
ATOM   1476 C C     . PRO   A 1 205 ? 8.709   17.589  -15.054 1.00 28.23 ? 205 PRO   A C     1 
ATOM   1477 O O     . PRO   A 1 205 ? 8.712   18.081  -16.187 1.00 27.22 ? 205 PRO   A O     1 
ATOM   1478 C CB    . PRO   A 1 205 ? 10.733  16.087  -14.914 1.00 29.38 ? 205 PRO   A CB    1 
ATOM   1479 C CG    . PRO   A 1 205 ? 10.990  14.809  -15.674 1.00 29.94 ? 205 PRO   A CG    1 
ATOM   1480 C CD    . PRO   A 1 205 ? 9.822   14.650  -16.628 1.00 28.12 ? 205 PRO   A CD    1 
ATOM   1481 N N     . LEU   A 1 206 ? 8.274   18.234  -13.976 1.00 29.40 ? 206 LEU   A N     1 
ATOM   1482 C CA    . LEU   A 1 206 ? 7.799   19.603  -14.085 1.00 31.05 ? 206 LEU   A CA    1 
ATOM   1483 C C     . LEU   A 1 206 ? 8.906   20.492  -14.665 1.00 29.63 ? 206 LEU   A C     1 
ATOM   1484 O O     . LEU   A 1 206 ? 8.638   21.447  -15.388 1.00 28.50 ? 206 LEU   A O     1 
ATOM   1485 C CB    . LEU   A 1 206 ? 7.316   20.113  -12.731 1.00 32.12 ? 206 LEU   A CB    1 
ATOM   1486 C CG    . LEU   A 1 206 ? 6.593   21.469  -12.742 1.00 32.60 ? 206 LEU   A CG    1 
ATOM   1487 C CD1   . LEU   A 1 206 ? 5.513   21.499  -13.812 1.00 31.42 ? 206 LEU   A CD1   1 
ATOM   1488 C CD2   . LEU   A 1 206 ? 5.984   21.743  -11.368 1.00 35.82 ? 206 LEU   A CD2   1 
ATOM   1489 N N     . ALA   A 1 207 ? 10.169  20.184  -14.340 1.00 28.96 ? 207 ALA   A N     1 
ATOM   1490 C CA    . ALA   A 1 207 ? 11.302  20.967  -14.831 1.00 29.06 ? 207 ALA   A CA    1 
ATOM   1491 C C     . ALA   A 1 207 ? 11.407  20.878  -16.351 1.00 24.87 ? 207 ALA   A C     1 
ATOM   1492 O O     . ALA   A 1 207 ? 11.752  21.868  -16.998 1.00 31.92 ? 207 ALA   A O     1 
ATOM   1493 C CB    . ALA   A 1 207 ? 12.600  20.526  -14.150 1.00 28.76 ? 207 ALA   A CB    1 
ATOM   1494 N N     . GLN   A 1 208 ? 11.099  19.702  -16.919 1.00 29.34 ? 208 GLN   A N     1 
ATOM   1495 C CA    . GLN   A 1 208 ? 11.080  19.522  -18.365 1.00 26.91 ? 208 GLN   A CA    1 
ATOM   1496 C C     . GLN   A 1 208 ? 9.997   20.401  -18.988 1.00 24.53 ? 208 GLN   A C     1 
ATOM   1497 O O     . GLN   A 1 208 ? 10.267  21.174  -19.916 1.00 24.72 ? 208 GLN   A O     1 
ATOM   1498 C CB    . GLN   A 1 208 ? 10.902  18.052  -18.747 1.00 26.26 ? 208 GLN   A CB    1 
ATOM   1499 C CG    . GLN   A 1 208 ? 10.777  17.826  -20.249 1.00 28.90 ? 208 GLN   A CG    1 
ATOM   1500 C CD    . GLN   A 1 208 ? 10.433  16.408  -20.649 1.00 29.05 ? 208 GLN   A CD    1 
ATOM   1501 O OE1   . GLN   A 1 208 ? 10.395  15.492  -19.823 1.00 30.22 ? 208 GLN   A OE1   1 
ATOM   1502 N NE2   . GLN   A 1 208 ? 10.209  16.202  -21.940 1.00 31.08 ? 208 GLN   A NE2   1 
ATOM   1503 N N     . ALA   A 1 209 ? 8.757   20.296  -18.477 1.00 25.97 ? 209 ALA   A N     1 
ATOM   1504 C CA    . ALA   A 1 209 ? 7.672   21.129  -18.982 1.00 24.14 ? 209 ALA   A CA    1 
ATOM   1505 C C     . ALA   A 1 209 ? 8.038   22.608  -18.910 1.00 25.38 ? 209 ALA   A C     1 
ATOM   1506 O O     . ALA   A 1 209 ? 7.737   23.353  -19.850 1.00 25.68 ? 209 ALA   A O     1 
ATOM   1507 C CB    . ALA   A 1 209 ? 6.391   20.876  -18.224 1.00 27.34 ? 209 ALA   A CB    1 
ATOM   1508 N N     . THR   A 1 210 ? 8.621   23.041  -17.777 1.00 25.36 ? 210 THR   A N     1 
ATOM   1509 C CA    . THR   A 1 210 ? 8.975   24.444  -17.615 1.00 27.97 ? 210 THR   A CA    1 
ATOM   1510 C C     . THR   A 1 210 ? 10.042  24.850  -18.633 1.00 29.37 ? 210 THR   A C     1 
ATOM   1511 O O     . THR   A 1 210 ? 9.946   25.943  -19.212 1.00 33.52 ? 210 THR   A O     1 
ATOM   1512 C CB    . THR   A 1 210 ? 9.397   24.754  -16.181 1.00 29.07 ? 210 THR   A CB    1 
ATOM   1513 O OG1   . THR   A 1 210 ? 8.178   24.561  -15.470 1.00 29.95 ? 210 THR   A OG1   1 
ATOM   1514 C CG2   . THR   A 1 210 ? 9.906   26.173  -16.017 1.00 31.56 ? 210 THR   A CG2   1 
ATOM   1515 N N     . ALA   A 1 211 ? 11.025  23.967  -18.864 1.00 31.14 ? 211 ALA   A N     1 
ATOM   1516 C CA    . ALA   A 1 211 ? 12.113  24.225  -19.805 1.00 33.58 ? 211 ALA   A CA    1 
ATOM   1517 C C     . ALA   A 1 211 ? 11.563  24.447  -21.203 1.00 32.44 ? 211 ALA   A C     1 
ATOM   1518 O O     . ALA   A 1 211 ? 12.063  25.308  -21.923 1.00 35.98 ? 211 ALA   A O     1 
ATOM   1519 C CB    . ALA   A 1 211 ? 13.113  23.084  -19.826 1.00 33.53 ? 211 ALA   A CB    1 
ATOM   1520 N N     . VAL   A 1 212 ? 10.529  23.668  -21.560 1.00 30.08 ? 212 VAL   A N     1 
ATOM   1521 C CA    . VAL   A 1 212 ? 9.978   23.592  -22.904 1.00 27.91 ? 212 VAL   A CA    1 
ATOM   1522 C C     . VAL   A 1 212 ? 8.920   24.681  -23.104 1.00 29.82 ? 212 VAL   A C     1 
ATOM   1523 O O     . VAL   A 1 212 ? 8.848   25.265  -24.176 1.00 29.84 ? 212 VAL   A O     1 
ATOM   1524 C CB    . VAL   A 1 212 ? 9.396   22.184  -23.156 1.00 29.92 ? 212 VAL   A CB    1 
ATOM   1525 C CG1   . VAL   A 1 212 ? 8.486   22.124  -24.386 1.00 31.37 ? 212 VAL   A CG1   1 
ATOM   1526 C CG2   . VAL   A 1 212 ? 10.495  21.125  -23.247 1.00 32.40 ? 212 VAL   A CG2   1 
ATOM   1527 N N     . LEU   A 1 213 ? 8.072   24.925  -22.096 1.00 27.94 ? 213 LEU   A N     1 
ATOM   1528 C CA    . LEU   A 1 213 ? 6.910   25.796  -22.241 1.00 27.68 ? 213 LEU   A CA    1 
ATOM   1529 C C     . LEU   A 1 213 ? 7.119   27.166  -21.603 1.00 27.94 ? 213 LEU   A C     1 
ATOM   1530 O O     . LEU   A 1 213 ? 6.402   28.092  -21.958 1.00 32.36 ? 213 LEU   A O     1 
ATOM   1531 C CB    . LEU   A 1 213 ? 5.675   25.130  -21.621 1.00 27.33 ? 213 LEU   A CB    1 
ATOM   1532 C CG    . LEU   A 1 213 ? 5.270   23.765  -22.178 1.00 26.61 ? 213 LEU   A CG    1 
ATOM   1533 C CD1   . LEU   A 1 213 ? 4.032   23.222  -21.464 1.00 29.44 ? 213 LEU   A CD1   1 
ATOM   1534 C CD2   . LEU   A 1 213 ? 4.990   23.858  -23.683 1.00 30.47 ? 213 LEU   A CD2   1 
ATOM   1535 N N     . GLY   A 1 214 ? 8.015   27.273  -20.618 1.00 32.14 ? 214 GLY   A N     1 
ATOM   1536 C CA    . GLY   A 1 214 ? 8.187   28.480  -19.826 1.00 32.81 ? 214 GLY   A CA    1 
ATOM   1537 C C     . GLY   A 1 214 ? 7.336   28.404  -18.560 1.00 37.27 ? 214 GLY   A C     1 
ATOM   1538 O O     . GLY   A 1 214 ? 6.313   27.721  -18.521 1.00 31.71 ? 214 GLY   A O     1 
ATOM   1539 N N     . PRO   A 1 215 ? 7.746   29.068  -17.462 1.00 37.95 ? 215 PRO   A N     1 
ATOM   1540 C CA    . PRO   A 1 215 ? 7.045   28.920  -16.191 1.00 37.60 ? 215 PRO   A CA    1 
ATOM   1541 C C     . PRO   A 1 215 ? 5.669   29.585  -16.137 1.00 37.38 ? 215 PRO   A C     1 
ATOM   1542 O O     . PRO   A 1 215 ? 4.854   29.216  -15.294 1.00 34.15 ? 215 PRO   A O     1 
ATOM   1543 C CB    . PRO   A 1 215 ? 8.047   29.515  -15.202 1.00 39.71 ? 215 PRO   A CB    1 
ATOM   1544 C CG    . PRO   A 1 215 ? 8.742   30.585  -16.008 1.00 40.74 ? 215 PRO   A CG    1 
ATOM   1545 C CD    . PRO   A 1 215 ? 8.905   29.974  -17.392 1.00 39.00 ? 215 PRO   A CD    1 
ATOM   1546 N N     . GLU   A 1 216 ? 5.404   30.522  -17.064 1.00 38.65 ? 216 GLU   A N     1 
ATOM   1547 C CA    . GLU   A 1 216 ? 4.109   31.175  -17.177 1.00 40.76 ? 216 GLU   A CA    1 
ATOM   1548 C C     . GLU   A 1 216 ? 3.054   30.117  -17.520 1.00 38.95 ? 216 GLU   A C     1 
ATOM   1549 O O     . GLU   A 1 216 ? 1.937   30.173  -17.024 1.00 37.74 ? 216 GLU   A O     1 
ATOM   1550 C CB    . GLU   A 1 216 ? 4.065   32.258  -18.258 1.00 41.98 ? 216 GLU   A CB    1 
ATOM   1551 C CG    . GLU   A 1 216 ? 5.065   33.397  -18.054 1.00 50.40 ? 216 GLU   A CG    1 
ATOM   1552 C CD    . GLU   A 1 216 ? 6.537   33.076  -18.310 1.00 56.47 ? 216 GLU   A CD    1 
ATOM   1553 O OE1   . GLU   A 1 216 ? 6.859   32.081  -19.010 1.00 52.68 ? 216 GLU   A OE1   1 
ATOM   1554 O OE2   . GLU   A 1 216 ? 7.380   33.833  -17.776 1.00 61.02 ? 216 GLU   A OE2   1 
ATOM   1555 N N     . LYS   A 1 217 ? 3.446   29.120  -18.318 1.00 34.17 ? 217 LYS   A N     1 
ATOM   1556 C CA    . LYS   A 1 217 ? 2.501   28.130  -18.804 1.00 34.08 ? 217 LYS   A CA    1 
ATOM   1557 C C     . LYS   A 1 217 ? 2.480   26.872  -17.947 1.00 32.83 ? 217 LYS   A C     1 
ATOM   1558 O O     . LYS   A 1 217 ? 1.721   25.940  -18.230 1.00 29.87 ? 217 LYS   A O     1 
ATOM   1559 C CB    . LYS   A 1 217 ? 2.845   27.813  -20.261 1.00 33.33 ? 217 LYS   A CB    1 
ATOM   1560 C CG    . LYS   A 1 217 ? 2.623   28.984  -21.177 1.00 33.19 ? 217 LYS   A CG    1 
ATOM   1561 C CD    . LYS   A 1 217 ? 3.020   28.707  -22.614 1.00 34.97 ? 217 LYS   A CD    1 
ATOM   1562 C CE    . LYS   A 1 217 ? 2.547   29.729  -23.562 1.00 34.96 ? 217 LYS   A CE    1 
ATOM   1563 N NZ    . LYS   A 1 217 ? 3.160   31.055  -23.423 1.00 37.11 ? 217 LYS   A NZ    1 
ATOM   1564 N N     . THR   A 1 218 ? 3.295   26.838  -16.891 1.00 30.70 ? 218 THR   A N     1 
ATOM   1565 C CA    . THR   A 1 218 ? 3.341   25.673  -16.028 1.00 30.08 ? 218 THR   A CA    1 
ATOM   1566 C C     . THR   A 1 218 ? 2.997   26.079  -14.598 1.00 33.24 ? 218 THR   A C     1 
ATOM   1567 O O     . THR   A 1 218 ? 3.218   25.303  -13.684 1.00 31.71 ? 218 THR   A O     1 
ATOM   1568 C CB    . THR   A 1 218 ? 4.723   25.030  -16.125 1.00 33.33 ? 218 THR   A CB    1 
ATOM   1569 O OG1   . THR   A 1 218 ? 5.730   25.886  -15.589 1.00 30.76 ? 218 THR   A OG1   1 
ATOM   1570 C CG2   . THR   A 1 218 ? 5.076   24.725  -17.563 1.00 29.41 ? 218 THR   A CG2   1 
ATOM   1571 N N     . SER   A 1 219 ? 2.461   27.291  -14.442 1.00 37.22 ? 219 SER   A N     1 
ATOM   1572 C CA    . SER   A 1 219 ? 2.215   27.873  -13.134 1.00 42.05 ? 219 SER   A CA    1 
ATOM   1573 C C     . SER   A 1 219 ? 0.818   27.518  -12.633 1.00 41.36 ? 219 SER   A C     1 
ATOM   1574 O O     . SER   A 1 219 ? 0.548   27.702  -11.456 1.00 43.93 ? 219 SER   A O     1 
ATOM   1575 C CB    . SER   A 1 219 ? 2.418   29.365  -13.160 1.00 47.32 ? 219 SER   A CB    1 
ATOM   1576 O OG    . SER   A 1 219 ? 1.332   30.036  -13.792 1.00 47.29 ? 219 SER   A OG    1 
ATOM   1577 N N     . SER   A 1 220 ? -0.059  27.010  -13.517 1.00 36.05 ? 220 SER   A N     1 
ATOM   1578 C CA    . SER   A 1 220 ? -1.385  26.543  -13.134 1.00 38.45 ? 220 SER   A CA    1 
ATOM   1579 C C     . SER   A 1 220 ? -1.901  25.507  -14.126 1.00 33.57 ? 220 SER   A C     1 
ATOM   1580 O O     . SER   A 1 220 ? -1.340  25.347  -15.205 1.00 30.20 ? 220 SER   A O     1 
ATOM   1581 C CB    . SER   A 1 220 ? -2.369  27.688  -13.046 1.00 44.31 ? 220 SER   A CB    1 
ATOM   1582 O OG    . SER   A 1 220 ? -2.823  28.048  -14.343 1.00 47.06 ? 220 SER   A OG    1 
ATOM   1583 N N     . ALA   A 1 221 ? -2.994  24.834  -13.762 1.00 30.11 ? 221 ALA   A N     1 
ATOM   1584 C CA    . ALA   A 1 221 ? -3.687  23.963  -14.693 1.00 28.82 ? 221 ALA   A CA    1 
ATOM   1585 C C     . ALA   A 1 221 ? -4.197  24.801  -15.867 1.00 27.01 ? 221 ALA   A C     1 
ATOM   1586 O O     . ALA   A 1 221 ? -4.681  25.928  -15.689 1.00 25.92 ? 221 ALA   A O     1 
ATOM   1587 C CB    . ALA   A 1 221 ? -4.812  23.203  -14.019 1.00 30.26 ? 221 ALA   A CB    1 
ATOM   1588 N N     . VAL   A 1 222 ? -4.057  24.241  -17.076 1.00 25.02 ? 222 VAL   A N     1 
ATOM   1589 C CA    . VAL   A 1 222 ? -4.568  24.881  -18.276 1.00 21.12 ? 222 VAL   A CA    1 
ATOM   1590 C C     . VAL   A 1 222 ? -5.307  23.825  -19.089 1.00 19.93 ? 222 VAL   A C     1 
ATOM   1591 O O     . VAL   A 1 222 ? -4.770  22.735  -19.342 1.00 20.93 ? 222 VAL   A O     1 
ATOM   1592 C CB    . VAL   A 1 222 ? -3.469  25.538  -19.132 1.00 23.15 ? 222 VAL   A CB    1 
ATOM   1593 C CG1   . VAL   A 1 222 ? -4.080  26.244  -20.338 1.00 21.53 ? 222 VAL   A CG1   1 
ATOM   1594 C CG2   . VAL   A 1 222 ? -2.586  26.491  -18.342 1.00 24.13 ? 222 VAL   A CG2   1 
ATOM   1595 N N     . LEU   A 1 223 ? -6.508  24.179  -19.519 1.00 20.64 ? 223 LEU   A N     1 
ATOM   1596 C CA    . LEU   A 1 223 ? -7.282  23.348  -20.419 1.00 21.12 ? 223 LEU   A CA    1 
ATOM   1597 C C     . LEU   A 1 223 ? -7.292  24.020  -21.788 1.00 20.95 ? 223 LEU   A C     1 
ATOM   1598 O O     . LEU   A 1 223 ? -7.851  25.096  -21.939 1.00 20.75 ? 223 LEU   A O     1 
ATOM   1599 C CB    . LEU   A 1 223 ? -8.686  23.113  -19.888 1.00 22.32 ? 223 LEU   A CB    1 
ATOM   1600 C CG    . LEU   A 1 223 ? -9.450  22.015  -20.624 1.00 22.77 ? 223 LEU   A CG    1 
ATOM   1601 C CD1   . LEU   A 1 223 ? -10.476 21.382  -19.711 1.00 23.58 ? 223 LEU   A CD1   1 
ATOM   1602 C CD2   . LEU   A 1 223 ? -10.073 22.455  -21.943 1.00 22.42 ? 223 LEU   A CD2   1 
ATOM   1603 N N     . HIS   A 1 224 ? -6.657  23.359  -22.766 1.00 22.13 ? 224 HIS   A N     1 
ATOM   1604 C CA    . HIS   A 1 224 ? -6.448  23.919  -24.091 1.00 21.62 ? 224 HIS   A CA    1 
ATOM   1605 C C     . HIS   A 1 224 ? -7.540  23.386  -25.023 1.00 21.71 ? 224 HIS   A C     1 
ATOM   1606 O O     . HIS   A 1 224 ? -7.513  22.216  -25.440 1.00 22.01 ? 224 HIS   A O     1 
ATOM   1607 C CB    . HIS   A 1 224 ? -5.037  23.628  -24.622 1.00 19.13 ? 224 HIS   A CB    1 
ATOM   1608 C CG    . HIS   A 1 224 ? -3.904  23.848  -23.666 1.00 20.48 ? 224 HIS   A CG    1 
ATOM   1609 N ND1   . HIS   A 1 224 ? -2.988  24.870  -23.790 1.00 21.17 ? 224 HIS   A ND1   1 
ATOM   1610 C CD2   . HIS   A 1 224 ? -3.557  23.174  -22.580 1.00 19.33 ? 224 HIS   A CD2   1 
ATOM   1611 C CE1   . HIS   A 1 224 ? -2.111  24.785  -22.824 1.00 19.97 ? 224 HIS   A CE1   1 
ATOM   1612 N NE2   . HIS   A 1 224 ? -2.458  23.773  -22.049 1.00 21.21 ? 224 HIS   A NE2   1 
ATOM   1613 N N     . THR   A 1 225 ? -8.464  24.276  -25.428 1.00 18.92 ? 225 THR   A N     1 
ATOM   1614 C CA    . THR   A 1 225 ? -9.637  23.873  -26.198 1.00 19.78 ? 225 THR   A CA    1 
ATOM   1615 C C     . THR   A 1 225 ? -9.250  24.009  -27.667 1.00 19.48 ? 225 THR   A C     1 
ATOM   1616 O O     . THR   A 1 225 ? -8.319  24.735  -28.017 1.00 21.07 ? 225 THR   A O     1 
ATOM   1617 C CB    . THR   A 1 225 ? -10.940 24.645  -25.907 1.00 18.80 ? 225 THR   A CB    1 
ATOM   1618 O OG1   . THR   A 1 225 ? -10.718 25.995  -26.316 1.00 20.37 ? 225 THR   A OG1   1 
ATOM   1619 C CG2   . THR   A 1 225 ? -11.319 24.691  -24.429 1.00 19.37 ? 225 THR   A CG2   1 
ATOM   1620 N N     . GLY   A 1 226 ? -10.001 23.313  -28.511 1.00 19.64 ? 226 GLY   A N     1 
ATOM   1621 C CA    . GLY   A 1 226 ? -9.774  23.423  -29.942 1.00 20.42 ? 226 GLY   A CA    1 
ATOM   1622 C C     . GLY   A 1 226 ? -10.624 22.429  -30.708 1.00 21.20 ? 226 GLY   A C     1 
ATOM   1623 O O     . GLY   A 1 226 ? -11.482 21.752  -30.150 1.00 20.80 ? 226 GLY   A O     1 
ATOM   1624 N N     . PRO   A 1 227 ? -10.427 22.360  -32.036 1.00 22.00 ? 227 PRO   A N     1 
ATOM   1625 C CA    . PRO   A 1 227 ? -11.309 21.582  -32.899 1.00 22.84 ? 227 PRO   A CA    1 
ATOM   1626 C C     . PRO   A 1 227 ? -11.048 20.076  -32.807 1.00 23.40 ? 227 PRO   A C     1 
ATOM   1627 O O     . PRO   A 1 227 ? -9.986  19.582  -33.203 1.00 24.91 ? 227 PRO   A O     1 
ATOM   1628 C CB    . PRO   A 1 227 ? -11.014 22.170  -34.316 1.00 23.01 ? 227 PRO   A CB    1 
ATOM   1629 C CG    . PRO   A 1 227 ? -9.649  22.740  -34.207 1.00 24.23 ? 227 PRO   A CG    1 
ATOM   1630 C CD    . PRO   A 1 227 ? -9.406  23.140  -32.749 1.00 22.26 ? 227 PRO   A CD    1 
ATOM   1631 N N     . GLY   A 1 228 ? -12.014 19.374  -32.228 1.00 23.75 ? 228 GLY   A N     1 
ATOM   1632 C CA    . GLY   A 1 228 ? -12.074 17.923  -32.232 1.00 22.88 ? 228 GLY   A CA    1 
ATOM   1633 C C     . GLY   A 1 228 ? -11.258 17.258  -31.131 1.00 22.66 ? 228 GLY   A C     1 
ATOM   1634 O O     . GLY   A 1 228 ? -11.161 16.024  -31.126 1.00 21.53 ? 228 GLY   A O     1 
ATOM   1635 N N     . ALA   A 1 229 ? -10.610 18.057  -30.265 1.00 22.16 ? 229 ALA   A N     1 
ATOM   1636 C CA    . ALA   A 1 229 ? -9.660  17.540  -29.305 1.00 21.89 ? 229 ALA   A CA    1 
ATOM   1637 C C     . ALA   A 1 229 ? -9.320  18.605  -28.286 1.00 23.33 ? 229 ALA   A C     1 
ATOM   1638 O O     . ALA   A 1 229 ? -9.399  19.777  -28.619 1.00 24.40 ? 229 ALA   A O     1 
ATOM   1639 C CB    . ALA   A 1 229 ? -8.377  17.086  -29.984 1.00 21.67 ? 229 ALA   A CB    1 
ATOM   1640 N N     . PHE   A 1 230 ? -8.904  18.201  -27.077 1.00 22.86 ? 230 PHE   A N     1 
ATOM   1641 C CA    . PHE   A 1 230 ? -8.419  19.177  -26.112 1.00 21.07 ? 230 PHE   A CA    1 
ATOM   1642 C C     . PHE   A 1 230 ? -7.291  18.565  -25.296 1.00 21.09 ? 230 PHE   A C     1 
ATOM   1643 O O     . PHE   A 1 230 ? -7.153  17.343  -25.270 1.00 22.09 ? 230 PHE   A O     1 
ATOM   1644 C CB    . PHE   A 1 230 ? -9.512  19.726  -25.186 1.00 22.11 ? 230 PHE   A CB    1 
ATOM   1645 C CG    . PHE   A 1 230 ? -10.081 18.790  -24.131 1.00 21.87 ? 230 PHE   A CG    1 
ATOM   1646 C CD1   . PHE   A 1 230 ? -11.161 17.967  -24.431 1.00 23.67 ? 230 PHE   A CD1   1 
ATOM   1647 C CD2   . PHE   A 1 230 ? -9.596  18.809  -22.827 1.00 24.16 ? 230 PHE   A CD2   1 
ATOM   1648 C CE1   . PHE   A 1 230 ? -11.750 17.188  -23.448 1.00 24.31 ? 230 PHE   A CE1   1 
ATOM   1649 C CE2   . PHE   A 1 230 ? -10.174 18.002  -21.855 1.00 23.94 ? 230 PHE   A CE2   1 
ATOM   1650 C CZ    . PHE   A 1 230 ? -11.238 17.189  -22.179 1.00 23.80 ? 230 PHE   A CZ    1 
ATOM   1651 N N     . VAL   A 1 231 ? -6.485  19.432  -24.663 1.00 19.93 ? 231 VAL   A N     1 
ATOM   1652 C CA    . VAL   A 1 231 ? -5.400  19.000  -23.799 1.00 23.74 ? 231 VAL   A CA    1 
ATOM   1653 C C     . VAL   A 1 231 ? -5.518  19.652  -22.426 1.00 24.01 ? 231 VAL   A C     1 
ATOM   1654 O O     . VAL   A 1 231 ? -5.792  20.835  -22.333 1.00 22.85 ? 231 VAL   A O     1 
ATOM   1655 C CB    . VAL   A 1 231 ? -4.033  19.360  -24.415 1.00 25.28 ? 231 VAL   A CB    1 
ATOM   1656 C CG1   . VAL   A 1 231 ? -2.901  18.865  -23.516 1.00 29.19 ? 231 VAL   A CG1   1 
ATOM   1657 C CG2   . VAL   A 1 231 ? -3.878  18.778  -25.803 1.00 27.61 ? 231 VAL   A CG2   1 
ATOM   1658 N N     . LEU   A 1 232 ? -5.230  18.896  -21.366 1.00 22.66 ? 232 LEU   A N     1 
ATOM   1659 C CA    . LEU   A 1 232 ? -5.080  19.452  -20.036 1.00 24.03 ? 232 LEU   A CA    1 
ATOM   1660 C C     . LEU   A 1 232 ? -3.618  19.347  -19.634 1.00 28.67 ? 232 LEU   A C     1 
ATOM   1661 O O     . LEU   A 1 232 ? -3.049  18.252  -19.701 1.00 29.62 ? 232 LEU   A O     1 
ATOM   1662 C CB    . LEU   A 1 232 ? -5.894  18.645  -19.040 1.00 34.30 ? 232 LEU   A CB    1 
ATOM   1663 C CG    . LEU   A 1 232 ? -7.332  19.074  -18.777 1.00 41.16 ? 232 LEU   A CG    1 
ATOM   1664 C CD1   . LEU   A 1 232 ? -8.075  17.835  -18.265 1.00 43.61 ? 232 LEU   A CD1   1 
ATOM   1665 C CD2   . LEU   A 1 232 ? -7.356  20.223  -17.771 1.00 39.96 ? 232 LEU   A CD2   1 
ATOM   1666 N N     . THR   A 1 233 ? -3.031  20.471  -19.214 1.00 23.48 ? 233 THR   A N     1 
ATOM   1667 C CA    . THR   A 1 233 ? -1.716  20.437  -18.614 1.00 25.34 ? 233 THR   A CA    1 
ATOM   1668 C C     . THR   A 1 233 ? -1.892  20.845  -17.161 1.00 27.52 ? 233 THR   A C     1 
ATOM   1669 O O     . THR   A 1 233 ? -2.351  21.953  -16.877 1.00 29.40 ? 233 THR   A O     1 
ATOM   1670 C CB    . THR   A 1 233 ? -0.703  21.325  -19.340 1.00 24.86 ? 233 THR   A CB    1 
ATOM   1671 O OG1   . THR   A 1 233 ? -1.182  22.676  -19.362 1.00 22.96 ? 233 THR   A OG1   1 
ATOM   1672 C CG2   . THR   A 1 233 ? -0.394  20.806  -20.736 1.00 25.98 ? 233 THR   A CG2   1 
ATOM   1673 N N     . ILE   A 1 234 ? -1.458  19.954  -16.259 1.00 28.78 ? 234 ILE   A N     1 
ATOM   1674 C CA    . ILE   A 1 234 ? -1.765  20.077  -14.845 1.00 29.32 ? 234 ILE   A CA    1 
ATOM   1675 C C     . ILE   A 1 234 ? -0.445  19.991  -14.081 1.00 28.96 ? 234 ILE   A C     1 
ATOM   1676 O O     . ILE   A 1 234 ? 0.117   18.910  -14.004 1.00 27.78 ? 234 ILE   A O     1 
ATOM   1677 C CB    . ILE   A 1 234 ? -2.748  18.965  -14.441 1.00 35.95 ? 234 ILE   A CB    1 
ATOM   1678 C CG1   . ILE   A 1 234 ? -4.089  19.073  -15.191 1.00 40.78 ? 234 ILE   A CG1   1 
ATOM   1679 C CG2   . ILE   A 1 234 ? -2.957  18.940  -12.924 1.00 36.97 ? 234 ILE   A CG2   1 
ATOM   1680 C CD1   . ILE   A 1 234 ? -5.006  17.877  -14.988 1.00 44.52 ? 234 ILE   A CD1   1 
ATOM   1681 N N     . PRO   A 1 235 ? 0.127   21.108  -13.592 1.00 31.40 ? 235 PRO   A N     1 
ATOM   1682 C CA    . PRO   A 1 235 ? 1.359   21.052  -12.800 1.00 36.10 ? 235 PRO   A CA    1 
ATOM   1683 C C     . PRO   A 1 235 ? 1.150   20.589  -11.358 1.00 40.85 ? 235 PRO   A C     1 
ATOM   1684 O O     . PRO   A 1 235 ? 0.350   21.169  -10.624 1.00 41.79 ? 235 PRO   A O     1 
ATOM   1685 C CB    . PRO   A 1 235 ? 1.912   22.482  -12.898 1.00 37.39 ? 235 PRO   A CB    1 
ATOM   1686 C CG    . PRO   A 1 235 ? 0.679   23.360  -13.120 1.00 40.59 ? 235 PRO   A CG    1 
ATOM   1687 C CD    . PRO   A 1 235 ? -0.329  22.484  -13.841 1.00 35.04 ? 235 PRO   A CD    1 
ATOM   1688 N N     . LEU   A 1 236 ? 1.867   19.519  -10.977 1.00 38.88 ? 236 LEU   A N     1 
ATOM   1689 C CA    . LEU   A 1 236 ? 1.753   18.895  -9.664  1.00 38.02 ? 236 LEU   A CA    1 
ATOM   1690 C C     . LEU   A 1 236 ? 3.065   19.074  -8.900  1.00 38.58 ? 236 LEU   A C     1 
ATOM   1691 O O     . LEU   A 1 236 ? 3.892   18.159  -8.884  1.00 36.51 ? 236 LEU   A O     1 
ATOM   1692 C CB    . LEU   A 1 236 ? 1.411   17.423  -9.881  1.00 34.38 ? 236 LEU   A CB    1 
ATOM   1693 C CG    . LEU   A 1 236 ? 0.088   17.133  -10.593 1.00 39.00 ? 236 LEU   A CG    1 
ATOM   1694 C CD1   . LEU   A 1 236 ? -0.067  15.678  -10.979 1.00 35.75 ? 236 LEU   A CD1   1 
ATOM   1695 C CD2   . LEU   A 1 236 ? -1.075  17.593  -9.724  1.00 41.36 ? 236 LEU   A CD2   1 
ATOM   1696 N N     . ALA   A 1 237 ? 3.237   20.253  -8.280  1.00 40.09 ? 237 ALA   A N     1 
ATOM   1697 C CA    . ALA   A 1 237 ? 4.534   20.719  -7.813  1.00 46.08 ? 237 ALA   A CA    1 
ATOM   1698 C C     . ALA   A 1 237 ? 5.099   19.806  -6.728  1.00 44.15 ? 237 ALA   A C     1 
ATOM   1699 O O     . ALA   A 1 237 ? 6.310   19.775  -6.558  1.00 39.52 ? 237 ALA   A O     1 
ATOM   1700 C CB    . ALA   A 1 237 ? 4.465   22.160  -7.340  1.00 48.04 ? 237 ALA   A CB    1 
ATOM   1701 N N     . GLU   A 1 238 ? 4.239   19.036  -6.044  1.00 50.27 ? 238 GLU   A N     1 
ATOM   1702 C CA    . GLU   A 1 238 ? 4.652   18.294  -4.861  1.00 51.06 ? 238 GLU   A CA    1 
ATOM   1703 C C     . GLU   A 1 238 ? 5.227   16.927  -5.245  1.00 47.70 ? 238 GLU   A C     1 
ATOM   1704 O O     . GLU   A 1 238 ? 5.866   16.279  -4.430  1.00 53.09 ? 238 GLU   A O     1 
ATOM   1705 C CB    . GLU   A 1 238 ? 3.504   18.224  -3.849  1.00 51.20 ? 238 GLU   A CB    1 
ATOM   1706 N N     . VAL   A 1 239 ? 5.019   16.472  -6.482  1.00 41.17 ? 239 VAL   A N     1 
ATOM   1707 C CA    . VAL   A 1 239 ? 5.763   15.324  -6.963  1.00 36.44 ? 239 VAL   A CA    1 
ATOM   1708 C C     . VAL   A 1 239 ? 6.676   15.750  -8.120  1.00 29.67 ? 239 VAL   A C     1 
ATOM   1709 O O     . VAL   A 1 239 ? 7.292   14.902  -8.751  1.00 30.14 ? 239 VAL   A O     1 
ATOM   1710 C CB    . VAL   A 1 239 ? 4.845   14.133  -7.299  1.00 35.86 ? 239 VAL   A CB    1 
ATOM   1711 C CG1   . VAL   A 1 239 ? 4.049   13.712  -6.063  1.00 40.46 ? 239 VAL   A CG1   1 
ATOM   1712 C CG2   . VAL   A 1 239 ? 3.889   14.390  -8.452  1.00 33.73 ? 239 VAL   A CG2   1 
ATOM   1713 N N     . HIS   A 1 240 ? 6.795   17.068  -8.342  1.00 27.72 ? 240 HIS   A N     1 
ATOM   1714 C CA    . HIS   A 1 240 ? 7.702   17.649  -9.321  1.00 28.12 ? 240 HIS   A CA    1 
ATOM   1715 C C     . HIS   A 1 240 ? 7.376   17.094  -10.700 1.00 29.48 ? 240 HIS   A C     1 
ATOM   1716 O O     . HIS   A 1 240 ? 8.276   16.853  -11.496 1.00 29.30 ? 240 HIS   A O     1 
ATOM   1717 C CB    . HIS   A 1 240 ? 9.169   17.397  -8.949  1.00 32.53 ? 240 HIS   A CB    1 
ATOM   1718 C CG    . HIS   A 1 240 ? 9.457   17.687  -7.514  1.00 32.43 ? 240 HIS   A CG    1 
ATOM   1719 N ND1   . HIS   A 1 240 ? 9.445   18.976  -7.020  1.00 36.77 ? 240 HIS   A ND1   1 
ATOM   1720 C CD2   . HIS   A 1 240 ? 9.629   16.887  -6.469  1.00 34.34 ? 240 HIS   A CD2   1 
ATOM   1721 C CE1   . HIS   A 1 240 ? 9.665   18.941  -5.717  1.00 34.15 ? 240 HIS   A CE1   1 
ATOM   1722 N NE2   . HIS   A 1 240 ? 9.782   17.681  -5.357  1.00 36.83 ? 240 HIS   A NE2   1 
ATOM   1723 N N     . ALA   A 1 241 ? 6.075   16.934  -10.983 1.00 28.96 ? 241 ALA   A N     1 
ATOM   1724 C CA    . ALA   A 1 241 ? 5.606   16.402  -12.250 1.00 27.28 ? 241 ALA   A CA    1 
ATOM   1725 C C     . ALA   A 1 241 ? 4.676   17.390  -12.958 1.00 27.83 ? 241 ALA   A C     1 
ATOM   1726 O O     . ALA   A 1 241 ? 4.035   18.235  -12.333 1.00 26.45 ? 241 ALA   A O     1 
ATOM   1727 C CB    . ALA   A 1 241 ? 4.921   15.075  -12.040 1.00 28.40 ? 241 ALA   A CB    1 
ATOM   1728 N N     . MET   A 1 242 ? 4.626   17.234  -14.285 1.00 28.29 ? 242 MET   A N     1 
ATOM   1729 C CA    . MET   A 1 242 ? 3.570   17.774  -15.113 1.00 28.10 ? 242 MET   A CA    1 
ATOM   1730 C C     . MET   A 1 242 ? 2.778   16.606  -15.680 1.00 25.76 ? 242 MET   A C     1 
ATOM   1731 O O     . MET   A 1 242 ? 3.322   15.726  -16.374 1.00 25.48 ? 242 MET   A O     1 
ATOM   1732 C CB    . MET   A 1 242 ? 4.149   18.609  -16.257 1.00 30.42 ? 242 MET   A CB    1 
ATOM   1733 C CG    . MET   A 1 242 ? 3.152   18.879  -17.348 1.00 34.36 ? 242 MET   A CG    1 
ATOM   1734 S SD    . MET   A 1 242 ? 2.019   20.168  -16.823 1.00 38.41 ? 242 MET   A SD    1 
ATOM   1735 C CE    . MET   A 1 242 ? 2.998   21.652  -17.043 1.00 35.72 ? 242 MET   A CE    1 
ATOM   1736 N N     . HIS   A 1 243 ? 1.473   16.620  -15.392 1.00 26.21 ? 243 HIS   A N     1 
ATOM   1737 C CA    . HIS   A 1 243 ? 0.550   15.656  -15.965 1.00 26.59 ? 243 HIS   A CA    1 
ATOM   1738 C C     . HIS   A 1 243 ? -0.048  16.243  -17.243 1.00 25.61 ? 243 HIS   A C     1 
ATOM   1739 O O     . HIS   A 1 243 ? -0.553  17.361  -17.229 1.00 29.94 ? 243 HIS   A O     1 
ATOM   1740 C CB    . HIS   A 1 243 ? -0.546  15.289  -14.953 1.00 31.23 ? 243 HIS   A CB    1 
ATOM   1741 C CG    . HIS   A 1 243 ? -1.446  14.213  -15.427 1.00 36.19 ? 243 HIS   A CG    1 
ATOM   1742 N ND1   . HIS   A 1 243 ? -2.774  14.414  -15.732 1.00 44.80 ? 243 HIS   A ND1   1 
ATOM   1743 C CD2   . HIS   A 1 243 ? -1.216  12.903  -15.593 1.00 43.99 ? 243 HIS   A CD2   1 
ATOM   1744 C CE1   . HIS   A 1 243 ? -3.304  13.258  -16.108 1.00 46.35 ? 243 HIS   A CE1   1 
ATOM   1745 N NE2   . HIS   A 1 243 ? -2.375  12.332  -16.034 1.00 43.47 ? 243 HIS   A NE2   1 
ATOM   1746 N N     . ILE   A 1 244 ? 0.096   15.506  -18.343 1.00 28.61 ? 244 ILE   A N     1 
ATOM   1747 C CA    . ILE   A 1 244 ? -0.466  15.884  -19.624 1.00 28.79 ? 244 ILE   A CA    1 
ATOM   1748 C C     . ILE   A 1 244 ? -1.552  14.884  -20.016 1.00 30.38 ? 244 ILE   A C     1 
ATOM   1749 O O     . ILE   A 1 244 ? -1.315  13.677  -20.069 1.00 25.34 ? 244 ILE   A O     1 
ATOM   1750 C CB    . ILE   A 1 244 ? 0.616   15.943  -20.705 1.00 26.82 ? 244 ILE   A CB    1 
ATOM   1751 C CG1   . ILE   A 1 244 ? 1.807   16.748  -20.238 1.00 27.06 ? 244 ILE   A CG1   1 
ATOM   1752 C CG2   . ILE   A 1 244 ? 0.029   16.453  -22.020 1.00 25.73 ? 244 ILE   A CG2   1 
ATOM   1753 C CD1   . ILE   A 1 244 ? 2.990   16.690  -21.184 1.00 27.55 ? 244 ILE   A CD1   1 
ATOM   1754 N N     . GLU   A 1 245 ? -2.749  15.415  -20.310 1.00 29.28 ? 245 GLU   A N     1 
ATOM   1755 C CA    . GLU   A 1 245 ? -3.883  14.585  -20.650 1.00 31.61 ? 245 GLU   A CA    1 
ATOM   1756 C C     . GLU   A 1 245 ? -4.490  15.131  -21.941 1.00 34.19 ? 245 GLU   A C     1 
ATOM   1757 O O     . GLU   A 1 245 ? -4.859  16.302  -22.019 1.00 34.69 ? 245 GLU   A O     1 
ATOM   1758 C CB    . GLU   A 1 245 ? -4.812  14.543  -19.432 1.00 38.90 ? 245 GLU   A CB    1 
ATOM   1759 C CG    . GLU   A 1 245 ? -5.918  13.505  -19.595 1.00 51.20 ? 245 GLU   A CG    1 
ATOM   1760 C CD    . GLU   A 1 245 ? -6.436  12.853  -18.319 1.00 54.83 ? 245 GLU   A CD    1 
ATOM   1761 O OE1   . GLU   A 1 245 ? -6.378  13.497  -17.246 1.00 64.64 ? 245 GLU   A OE1   1 
ATOM   1762 O OE2   . GLU   A 1 245 ? -6.860  11.673  -18.397 1.00 59.52 ? 245 GLU   A OE2   1 
ATOM   1763 N N     . ALA   A 1 246 ? -4.569  14.292  -22.967 1.00 25.40 ? 246 ALA   A N     1 
ATOM   1764 C CA    . ALA   A 1 246 ? -5.164  14.704  -24.220 1.00 27.81 ? 246 ALA   A CA    1 
ATOM   1765 C C     . ALA   A 1 246 ? -6.385  13.827  -24.478 1.00 30.41 ? 246 ALA   A C     1 
ATOM   1766 O O     . ALA   A 1 246 ? -6.336  12.627  -24.224 1.00 30.93 ? 246 ALA   A O     1 
ATOM   1767 C CB    . ALA   A 1 246 ? -4.181  14.625  -25.349 1.00 28.05 ? 246 ALA   A CB    1 
ATOM   1768 N N     . PHE   A 1 247 ? -7.475  14.465  -24.914 1.00 24.70 ? 247 PHE   A N     1 
ATOM   1769 C CA    . PHE   A 1 247 ? -8.693  13.766  -25.288 1.00 23.50 ? 247 PHE   A CA    1 
ATOM   1770 C C     . PHE   A 1 247 ? -8.991  14.092  -26.732 1.00 25.73 ? 247 PHE   A C     1 
ATOM   1771 O O     . PHE   A 1 247 ? -9.092  15.266  -27.096 1.00 24.14 ? 247 PHE   A O     1 
ATOM   1772 C CB    . PHE   A 1 247 ? -9.896  14.084  -24.403 1.00 25.48 ? 247 PHE   A CB    1 
ATOM   1773 C CG    . PHE   A 1 247 ? -9.791  13.424  -23.045 1.00 23.16 ? 247 PHE   A CG    1 
ATOM   1774 C CD1   . PHE   A 1 247 ? -10.001 12.055  -22.895 1.00 26.28 ? 247 PHE   A CD1   1 
ATOM   1775 C CD2   . PHE   A 1 247 ? -9.449  14.159  -21.927 1.00 24.33 ? 247 PHE   A CD2   1 
ATOM   1776 C CE1   . PHE   A 1 247 ? -9.909  11.468  -21.639 1.00 25.58 ? 247 PHE   A CE1   1 
ATOM   1777 C CE2   . PHE   A 1 247 ? -9.308  13.552  -20.694 1.00 28.79 ? 247 PHE   A CE2   1 
ATOM   1778 C CZ    . PHE   A 1 247 ? -9.518  12.205  -20.559 1.00 26.75 ? 247 PHE   A CZ    1 
ATOM   1779 N N     . ILE   A 1 248 ? -9.128  13.035  -27.541 1.00 22.42 ? 248 ILE   A N     1 
ATOM   1780 C CA    . ILE   A 1 248 ? -9.448  13.203  -28.943 1.00 24.97 ? 248 ILE   A CA    1 
ATOM   1781 C C     . ILE   A 1 248 ? -10.828 12.619  -29.197 1.00 25.46 ? 248 ILE   A C     1 
ATOM   1782 O O     . ILE   A 1 248 ? -11.086 11.485  -28.783 1.00 25.70 ? 248 ILE   A O     1 
ATOM   1783 C CB    . ILE   A 1 248 ? -8.387  12.540  -29.835 1.00 27.29 ? 248 ILE   A CB    1 
ATOM   1784 C CG1   . ILE   A 1 248 ? -6.973  13.075  -29.507 1.00 29.93 ? 248 ILE   A CG1   1 
ATOM   1785 C CG2   . ILE   A 1 248 ? -8.770  12.719  -31.307 1.00 30.30 ? 248 ILE   A CG2   1 
ATOM   1786 C CD1   . ILE   A 1 248 ? -5.870  12.512  -30.395 1.00 33.36 ? 248 ILE   A CD1   1 
ATOM   1787 N N     . MET   A 1 249 ? -11.693 13.405  -29.847 1.00 26.61 ? 249 MET   A N     1 
ATOM   1788 C CA    . MET   A 1 249 ? -13.033 12.965  -30.197 1.00 29.80 ? 249 MET   A CA    1 
ATOM   1789 C C     . MET   A 1 249 ? -12.994 12.077  -31.432 1.00 31.27 ? 249 MET   A C     1 
ATOM   1790 O O     . MET   A 1 249 ? -12.326 12.386  -32.407 1.00 32.60 ? 249 MET   A O     1 
ATOM   1791 C CB    . MET   A 1 249 ? -13.972 14.143  -30.477 1.00 34.83 ? 249 MET   A CB    1 
ATOM   1792 C CG    . MET   A 1 249 ? -14.255 14.984  -29.276 1.00 34.91 ? 249 MET   A CG    1 
ATOM   1793 S SD    . MET   A 1 249 ? -14.602 13.992  -27.807 1.00 39.81 ? 249 MET   A SD    1 
ATOM   1794 C CE    . MET   A 1 249 ? -13.002 14.342  -27.066 1.00 27.80 ? 249 MET   A CE    1 
ATOM   1795 N N     . ASP   A 1 250 ? -13.726 10.970  -31.359 1.00 34.35 ? 250 ASP   A N     1 
ATOM   1796 C CA    . ASP   A 1 250 ? -13.603 9.842   -32.278 1.00 37.31 ? 250 ASP   A CA    1 
ATOM   1797 C C     . ASP   A 1 250 ? -15.002 9.470   -32.729 1.00 42.65 ? 250 ASP   A C     1 
ATOM   1798 O O     . ASP   A 1 250 ? -15.701 8.795   -31.984 1.00 32.98 ? 250 ASP   A O     1 
ATOM   1799 C CB    . ASP   A 1 250 ? -12.983 8.659   -31.541 1.00 36.82 ? 250 ASP   A CB    1 
ATOM   1800 C CG    . ASP   A 1 250 ? -12.832 7.343   -32.289 1.00 42.03 ? 250 ASP   A CG    1 
ATOM   1801 O OD1   . ASP   A 1 250 ? -12.647 7.396   -33.512 1.00 45.85 ? 250 ASP   A OD1   1 
ATOM   1802 O OD2   . ASP   A 1 250 ? -12.818 6.276   -31.620 1.00 40.58 ? 250 ASP   A OD2   1 
ATOM   1803 N N     . LYS   A 1 251 ? -15.422 9.909   -33.925 1.00 44.65 ? 251 LYS   A N     1 
ATOM   1804 C CA    . LYS   A 1 251 ? -16.779 9.619   -34.380 1.00 47.59 ? 251 LYS   A CA    1 
ATOM   1805 C C     . LYS   A 1 251 ? -16.942 8.119   -34.688 1.00 46.54 ? 251 LYS   A C     1 
ATOM   1806 O O     . LYS   A 1 251 ? -18.063 7.650   -34.852 1.00 53.72 ? 251 LYS   A O     1 
ATOM   1807 C CB    . LYS   A 1 251 ? -17.212 10.544  -35.526 1.00 52.26 ? 251 LYS   A CB    1 
ATOM   1808 N N     . GLU   A 1 252 ? -15.838 7.357   -34.706 1.00 48.66 ? 252 GLU   A N     1 
ATOM   1809 C CA    . GLU   A 1 252 ? -15.875 5.911   -34.900 1.00 46.15 ? 252 GLU   A CA    1 
ATOM   1810 C C     . GLU   A 1 252 ? -16.562 5.222   -33.707 1.00 40.14 ? 252 GLU   A C     1 
ATOM   1811 O O     . GLU   A 1 252 ? -16.725 5.816   -32.649 1.00 37.59 ? 252 GLU   A O     1 
ATOM   1812 C CB    . GLU   A 1 252 ? -14.456 5.340   -35.010 1.00 46.98 ? 252 GLU   A CB    1 
ATOM   1813 C CG    . GLU   A 1 252 ? -13.531 6.026   -36.017 1.00 48.98 ? 252 GLU   A CG    1 
ATOM   1814 C CD    . GLU   A 1 252 ? -14.051 6.012   -37.438 1.00 48.55 ? 252 GLU   A CD    1 
ATOM   1815 O OE1   . GLU   A 1 252 ? -14.416 4.927   -37.919 1.00 53.19 ? 252 GLU   A OE1   1 
ATOM   1816 O OE2   . GLU   A 1 252 ? -14.094 7.085   -38.062 1.00 52.37 ? 252 GLU   A OE2   1 
ATOM   1817 N N     . GLU   A 1 253 ? -16.952 3.956   -33.876 1.00 34.67 ? 253 GLU   A N     1 
ATOM   1818 C CA    . GLU   A 1 253 ? -17.304 3.101   -32.740 1.00 34.40 ? 253 GLU   A CA    1 
ATOM   1819 C C     . GLU   A 1 253 ? -16.041 2.435   -32.191 1.00 33.10 ? 253 GLU   A C     1 
ATOM   1820 O O     . GLU   A 1 253 ? -15.021 2.361   -32.854 1.00 29.66 ? 253 GLU   A O     1 
ATOM   1821 C CB    . GLU   A 1 253 ? -18.339 2.052   -33.160 1.00 40.35 ? 253 GLU   A CB    1 
ATOM   1822 C CG    . GLU   A 1 253 ? -19.714 2.621   -33.514 1.00 44.33 ? 253 GLU   A CG    1 
ATOM   1823 C CD    . GLU   A 1 253 ? -20.287 3.554   -32.455 1.00 51.40 ? 253 GLU   A CD    1 
ATOM   1824 O OE1   . GLU   A 1 253 ? -20.029 3.290   -31.258 1.00 51.78 ? 253 GLU   A OE1   1 
ATOM   1825 O OE2   . GLU   A 1 253 ? -20.956 4.549   -32.810 1.00 50.22 ? 253 GLU   A OE2   1 
ATOM   1826 N N     . TRP   A 1 254 ? -16.090 1.945   -30.949 1.00 27.58 ? 254 TRP   A N     1 
ATOM   1827 C CA    . TRP   A 1 254 ? -14.923 1.331   -30.354 1.00 31.16 ? 254 TRP   A CA    1 
ATOM   1828 C C     . TRP   A 1 254 ? -14.970 -0.158  -30.680 1.00 34.99 ? 254 TRP   A C     1 
ATOM   1829 O O     . TRP   A 1 254 ? -16.042 -0.761  -30.551 1.00 32.82 ? 254 TRP   A O     1 
ATOM   1830 C CB    . TRP   A 1 254 ? -14.927 1.573   -28.840 1.00 29.94 ? 254 TRP   A CB    1 
ATOM   1831 C CG    . TRP   A 1 254 ? -13.744 1.038   -28.090 1.00 31.18 ? 254 TRP   A CG    1 
ATOM   1832 C CD1   . TRP   A 1 254 ? -13.746 -0.001  -27.202 1.00 27.89 ? 254 TRP   A CD1   1 
ATOM   1833 C CD2   . TRP   A 1 254 ? -12.391 1.537   -28.136 1.00 30.59 ? 254 TRP   A CD2   1 
ATOM   1834 N NE1   . TRP   A 1 254 ? -12.501 -0.164  -26.669 1.00 27.15 ? 254 TRP   A NE1   1 
ATOM   1835 C CE2   . TRP   A 1 254 ? -11.648 0.761   -27.217 1.00 27.63 ? 254 TRP   A CE2   1 
ATOM   1836 C CE3   . TRP   A 1 254 ? -11.741 2.567   -28.841 1.00 34.07 ? 254 TRP   A CE3   1 
ATOM   1837 C CZ2   . TRP   A 1 254 ? -10.284 0.956   -27.014 1.00 33.42 ? 254 TRP   A CZ2   1 
ATOM   1838 C CZ3   . TRP   A 1 254 ? -10.387 2.755   -28.641 1.00 32.44 ? 254 TRP   A CZ3   1 
ATOM   1839 C CH2   . TRP   A 1 254 ? -9.671  1.965   -27.736 1.00 32.06 ? 254 TRP   A CH2   1 
ATOM   1840 N N     . PRO   A 1 255 ? -13.853 -0.767  -31.152 1.00 34.63 ? 255 PRO   A N     1 
ATOM   1841 C CA    . PRO   A 1 255 ? -13.841 -2.201  -31.467 1.00 39.34 ? 255 PRO   A CA    1 
ATOM   1842 C C     . PRO   A 1 255 ? -14.262 -3.001  -30.232 1.00 38.00 ? 255 PRO   A C     1 
ATOM   1843 O O     . PRO   A 1 255 ? -13.739 -2.770  -29.142 1.00 37.32 ? 255 PRO   A O     1 
ATOM   1844 C CB    . PRO   A 1 255 ? -12.373 -2.474  -31.898 1.00 39.00 ? 255 PRO   A CB    1 
ATOM   1845 C CG    . PRO   A 1 255 ? -11.883 -1.129  -32.380 1.00 37.19 ? 255 PRO   A CG    1 
ATOM   1846 C CD    . PRO   A 1 255 ? -12.554 -0.127  -31.433 1.00 36.42 ? 255 PRO   A CD    1 
ATOM   1847 N N     . GLU   A 1 256 ? -15.248 -3.892  -30.417 1.00 41.94 ? 256 GLU   A N     1 
ATOM   1848 C CA    . GLU   A 1 256 ? -15.785 -4.725  -29.351 1.00 41.99 ? 256 GLU   A CA    1 
ATOM   1849 C C     . GLU   A 1 256 ? -14.802 -5.858  -29.069 1.00 40.70 ? 256 GLU   A C     1 
ATOM   1850 O O     . GLU   A 1 256 ? -14.359 -6.521  -30.003 1.00 43.14 ? 256 GLU   A O     1 
ATOM   1851 C CB    . GLU   A 1 256 ? -17.151 -5.275  -29.775 1.00 42.77 ? 256 GLU   A CB    1 
ATOM   1852 N N     . VAL   A 1 257 ? -14.440 -6.061  -27.794 1.00 38.92 ? 257 VAL   A N     1 
ATOM   1853 C CA    . VAL   A 1 257 ? -13.660 -7.227  -27.395 1.00 42.08 ? 257 VAL   A CA    1 
ATOM   1854 C C     . VAL   A 1 257 ? -14.406 -7.893  -26.239 1.00 43.26 ? 257 VAL   A C     1 
ATOM   1855 O O     . VAL   A 1 257 ? -14.916 -7.192  -25.361 1.00 38.57 ? 257 VAL   A O     1 
ATOM   1856 C CB    . VAL   A 1 257 ? -12.178 -6.988  -27.019 1.00 43.26 ? 257 VAL   A CB    1 
ATOM   1857 C CG1   . VAL   A 1 257 ? -11.433 -6.150  -28.052 1.00 41.57 ? 257 VAL   A CG1   1 
ATOM   1858 C CG2   . VAL   A 1 257 ? -11.995 -6.375  -25.639 1.00 45.67 ? 257 VAL   A CG2   1 
ATOM   1859 N N     . GLN   A 1 258 ? -14.457 -9.237  -26.267 1.00 45.44 ? 258 GLN   A N     1 
ATOM   1860 C CA    . GLN   A 1 258 ? -15.104 -10.027 -25.223 1.00 47.48 ? 258 GLN   A CA    1 
ATOM   1861 C C     . GLN   A 1 258 ? -14.064 -10.396 -24.167 1.00 45.41 ? 258 GLN   A C     1 
ATOM   1862 O O     . GLN   A 1 258 ? -13.181 -11.221 -24.408 1.00 41.55 ? 258 GLN   A O     1 
ATOM   1863 C CB    . GLN   A 1 258 ? -15.783 -11.287 -25.784 1.00 49.40 ? 258 GLN   A CB    1 
ATOM   1864 C CG    . GLN   A 1 258 ? -16.622 -12.070 -24.773 1.00 49.82 ? 258 GLN   A CG    1 
ATOM   1865 C CD    . GLN   A 1 258 ? -17.700 -11.242 -24.095 1.00 46.00 ? 258 GLN   A CD    1 
ATOM   1866 O OE1   . GLN   A 1 258 ? -18.628 -10.747 -24.744 1.00 48.07 ? 258 GLN   A OE1   1 
ATOM   1867 N NE2   . GLN   A 1 258 ? -17.599 -11.087 -22.778 1.00 46.03 ? 258 GLN   A NE2   1 
ATOM   1868 N N     . THR   A 1 259 ? -14.176 -9.789  -22.978 1.00 39.07 ? 259 THR   A N     1 
ATOM   1869 C CA    . THR   A 1 259 ? -13.138 -9.932  -21.967 1.00 38.07 ? 259 THR   A CA    1 
ATOM   1870 C C     . THR   A 1 259 ? -13.659 -9.471  -20.609 1.00 36.67 ? 259 THR   A C     1 
ATOM   1871 O O     . THR   A 1 259 ? -14.399 -8.491  -20.538 1.00 36.64 ? 259 THR   A O     1 
ATOM   1872 C CB    . THR   A 1 259 ? -11.923 -9.105  -22.392 1.00 38.72 ? 259 THR   A CB    1 
ATOM   1873 O OG1   . THR   A 1 259 ? -10.956 -9.207  -21.356 1.00 34.51 ? 259 THR   A OG1   1 
ATOM   1874 C CG2   . THR   A 1 259 ? -12.243 -7.631  -22.567 1.00 40.71 ? 259 THR   A CG2   1 
ATOM   1875 N N     . SER   A 1 260 ? -13.200 -10.145 -19.549 1.00 35.30 ? 260 SER   A N     1 
ATOM   1876 C CA    . SER   A 1 260 ? -13.518 -9.775  -18.177 1.00 40.98 ? 260 SER   A CA    1 
ATOM   1877 C C     . SER   A 1 260 ? -12.734 -8.542  -17.743 1.00 40.49 ? 260 SER   A C     1 
ATOM   1878 O O     . SER   A 1 260 ? -13.013 -7.989  -16.687 1.00 38.55 ? 260 SER   A O     1 
ATOM   1879 C CB    . SER   A 1 260 ? -13.208 -10.909 -17.220 1.00 47.93 ? 260 SER   A CB    1 
ATOM   1880 O OG    . SER   A 1 260 ? -13.746 -12.145 -17.670 1.00 60.04 ? 260 SER   A OG    1 
ATOM   1881 N N     . SER   A 1 261 ? -11.665 -8.205  -18.475 1.00 37.82 ? 261 SER   A N     1 
ATOM   1882 C CA    . SER   A 1 261 ? -10.758 -7.154  -18.038 1.00 39.91 ? 261 SER   A CA    1 
ATOM   1883 C C     . SER   A 1 261 ? -11.204 -5.820  -18.638 1.00 33.40 ? 261 SER   A C     1 
ATOM   1884 O O     . SER   A 1 261 ? -11.314 -5.711  -19.854 1.00 31.15 ? 261 SER   A O     1 
ATOM   1885 C CB    . SER   A 1 261 ? -9.326  -7.486  -18.433 1.00 38.70 ? 261 SER   A CB    1 
ATOM   1886 O OG    . SER   A 1 261 ? -8.493  -6.334  -18.339 1.00 40.23 ? 261 SER   A OG    1 
ATOM   1887 N N     . ASP   A 1 262 ? -11.461 -4.814  -17.792 1.00 33.65 ? 262 ASP   A N     1 
ATOM   1888 C CA    . ASP   A 1 262 ? -11.765 -3.463  -18.263 1.00 31.65 ? 262 ASP   A CA    1 
ATOM   1889 C C     . ASP   A 1 262 ? -10.585 -2.838  -19.027 1.00 34.49 ? 262 ASP   A C     1 
ATOM   1890 O O     . ASP   A 1 262 ? -10.767 -2.059  -19.976 1.00 33.55 ? 262 ASP   A O     1 
ATOM   1891 C CB    . ASP   A 1 262 ? -12.137 -2.555  -17.096 1.00 32.53 ? 262 ASP   A CB    1 
ATOM   1892 C CG    . ASP   A 1 262 ? -13.482 -2.815  -16.422 1.00 33.25 ? 262 ASP   A CG    1 
ATOM   1893 O OD1   . ASP   A 1 262 ? -14.180 -3.783  -16.809 1.00 30.43 ? 262 ASP   A OD1   1 
ATOM   1894 O OD2   . ASP   A 1 262 ? -13.832 -2.037  -15.507 1.00 34.82 ? 262 ASP   A OD2   1 
ATOM   1895 N N     . SER   A 1 263 ? -9.354  -3.126  -18.589 1.00 38.17 ? 263 SER   A N     1 
ATOM   1896 C CA    . SER   A 1 263 ? -8.171  -2.652  -19.299 1.00 38.37 ? 263 SER   A CA    1 
ATOM   1897 C C     . SER   A 1 263 ? -8.175  -3.169  -20.741 1.00 38.51 ? 263 SER   A C     1 
ATOM   1898 O O     . SER   A 1 263 ? -7.921  -2.420  -21.685 1.00 35.77 ? 263 SER   A O     1 
ATOM   1899 C CB    . SER   A 1 263 ? -6.906  -3.040  -18.571 1.00 43.66 ? 263 SER   A CB    1 
ATOM   1900 O OG    . SER   A 1 263 ? -6.899  -2.493  -17.259 1.00 43.39 ? 263 SER   A OG    1 
ATOM   1901 N N     . LYS   A 1 264 ? -8.511  -4.448  -20.913 1.00 34.17 ? 264 LYS   A N     1 
ATOM   1902 C CA    . LYS   A 1 264 ? -8.574  -5.047  -22.240 1.00 36.53 ? 264 LYS   A CA    1 
ATOM   1903 C C     . LYS   A 1 264 ? -9.811  -4.557  -23.002 1.00 33.54 ? 264 LYS   A C     1 
ATOM   1904 O O     . LYS   A 1 264 ? -9.811  -4.452  -24.238 1.00 31.61 ? 264 LYS   A O     1 
ATOM   1905 C CB    . LYS   A 1 264 ? -8.559  -6.579  -22.164 1.00 42.61 ? 264 LYS   A CB    1 
ATOM   1906 C CG    . LYS   A 1 264 ? -7.232  -7.227  -22.547 1.00 49.14 ? 264 LYS   A CG    1 
ATOM   1907 C CD    . LYS   A 1 264 ? -6.127  -7.041  -21.512 1.00 57.62 ? 264 LYS   A CD    1 
ATOM   1908 N N     . ARG   A 1 265 ? -10.889 -4.268  -22.274 1.00 28.73 ? 265 ARG   A N     1 
ATOM   1909 C CA    . ARG   A 1 265 ? -12.119 -3.831  -22.914 1.00 30.80 ? 265 ARG   A CA    1 
ATOM   1910 C C     . ARG   A 1 265 ? -11.948 -2.405  -23.437 1.00 27.42 ? 265 ARG   A C     1 
ATOM   1911 O O     . ARG   A 1 265 ? -12.449 -2.114  -24.523 1.00 30.46 ? 265 ARG   A O     1 
ATOM   1912 C CB    . ARG   A 1 265 ? -13.296 -3.947  -21.930 1.00 31.67 ? 265 ARG   A CB    1 
ATOM   1913 C CG    . ARG   A 1 265 ? -14.669 -3.581  -22.468 1.00 31.43 ? 265 ARG   A CG    1 
ATOM   1914 C CD    . ARG   A 1 265 ? -15.313 -4.562  -23.443 1.00 37.55 ? 265 ARG   A CD    1 
ATOM   1915 N NE    . ARG   A 1 265 ? -16.722 -4.215  -23.696 1.00 37.58 ? 265 ARG   A NE    1 
ATOM   1916 C CZ    . ARG   A 1 265 ? -17.224 -3.361  -24.600 1.00 43.81 ? 265 ARG   A CZ    1 
ATOM   1917 N NH1   . ARG   A 1 265 ? -18.470 -2.930  -24.468 1.00 42.68 ? 265 ARG   A NH1   1 
ATOM   1918 N NH2   . ARG   A 1 265 ? -16.484 -2.875  -25.585 1.00 48.36 ? 265 ARG   A NH2   1 
ATOM   1919 N N     . TYR   A 1 266 ? -11.243 -1.542  -22.679 1.00 27.43 ? 266 TYR   A N     1 
ATOM   1920 C CA    . TYR   A 1 266 ? -11.338 -0.101  -22.911 1.00 27.40 ? 266 TYR   A CA    1 
ATOM   1921 C C     . TYR   A 1 266 ? -10.009 0.555   -23.294 1.00 28.19 ? 266 TYR   A C     1 
ATOM   1922 O O     . TYR   A 1 266 ? -9.949  1.788   -23.369 1.00 28.94 ? 266 TYR   A O     1 
ATOM   1923 C CB    . TYR   A 1 266 ? -11.862 0.609   -21.657 1.00 25.47 ? 266 TYR   A CB    1 
ATOM   1924 C CG    . TYR   A 1 266 ? -13.258 0.156   -21.242 1.00 25.02 ? 266 TYR   A CG    1 
ATOM   1925 C CD1   . TYR   A 1 266 ? -14.347 0.214   -22.108 1.00 26.49 ? 266 TYR   A CD1   1 
ATOM   1926 C CD2   . TYR   A 1 266 ? -13.470 -0.375  -19.977 1.00 28.16 ? 266 TYR   A CD2   1 
ATOM   1927 C CE1   . TYR   A 1 266 ? -15.612 -0.221  -21.724 1.00 25.36 ? 266 TYR   A CE1   1 
ATOM   1928 C CE2   . TYR   A 1 266 ? -14.716 -0.824  -19.586 1.00 26.94 ? 266 TYR   A CE2   1 
ATOM   1929 C CZ    . TYR   A 1 266 ? -15.791 -0.761  -20.460 1.00 27.30 ? 266 TYR   A CZ    1 
ATOM   1930 O OH    . TYR   A 1 266 ? -17.019 -1.189  -20.049 1.00 29.34 ? 266 TYR   A OH    1 
ATOM   1931 N N     . VAL   A 1 267 ? -8.953  -0.236  -23.529 1.00 27.68 ? 267 VAL   A N     1 
ATOM   1932 C CA    . VAL   A 1 267 ? -7.631  0.321   -23.783 1.00 28.77 ? 267 VAL   A CA    1 
ATOM   1933 C C     . VAL   A 1 267 ? -7.062  -0.356  -25.020 1.00 31.03 ? 267 VAL   A C     1 
ATOM   1934 O O     . VAL   A 1 267 ? -7.305  -1.538  -25.273 1.00 27.48 ? 267 VAL   A O     1 
ATOM   1935 C CB    . VAL   A 1 267 ? -6.676  0.176   -22.587 1.00 32.87 ? 267 VAL   A CB    1 
ATOM   1936 C CG1   . VAL   A 1 267 ? -5.258  0.628   -22.907 1.00 34.79 ? 267 VAL   A CG1   1 
ATOM   1937 C CG2   . VAL   A 1 267 ? -7.193  0.933   -21.378 1.00 32.68 ? 267 VAL   A CG2   1 
ATOM   1938 N N     . LEU   A 1 268 ? -6.347  0.435   -25.810 1.00 28.04 ? 268 LEU   A N     1 
ATOM   1939 C CA    . LEU   A 1 268 ? -5.662  -0.092  -26.976 1.00 29.68 ? 268 LEU   A CA    1 
ATOM   1940 C C     . LEU   A 1 268 ? -4.282  0.546   -27.018 1.00 31.47 ? 268 LEU   A C     1 
ATOM   1941 O O     . LEU   A 1 268 ? -4.077  1.651   -26.510 1.00 28.81 ? 268 LEU   A O     1 
ATOM   1942 C CB    . LEU   A 1 268 ? -6.519  0.242   -28.193 1.00 35.35 ? 268 LEU   A CB    1 
ATOM   1943 C CG    . LEU   A 1 268 ? -6.910  -0.884  -29.157 1.00 39.04 ? 268 LEU   A CG    1 
ATOM   1944 C CD1   . LEU   A 1 268 ? -7.136  -2.267  -28.583 1.00 38.21 ? 268 LEU   A CD1   1 
ATOM   1945 C CD2   . LEU   A 1 268 ? -8.159  -0.437  -29.912 1.00 36.54 ? 268 LEU   A CD2   1 
ATOM   1946 N N     . PRO   A 1 269 ? -3.263  -0.173  -27.544 1.00 30.95 ? 269 PRO   A N     1 
ATOM   1947 C CA    . PRO   A 1 269 ? -1.982  0.449   -27.886 1.00 30.85 ? 269 PRO   A CA    1 
ATOM   1948 C C     . PRO   A 1 269 ? -2.187  1.637   -28.826 1.00 26.84 ? 269 PRO   A C     1 
ATOM   1949 O O     . PRO   A 1 269 ? -3.085  1.619   -29.666 1.00 28.17 ? 269 PRO   A O     1 
ATOM   1950 C CB    . PRO   A 1 269 ? -1.189  -0.689  -28.583 1.00 31.05 ? 269 PRO   A CB    1 
ATOM   1951 C CG    . PRO   A 1 269 ? -1.815  -1.971  -28.071 1.00 32.36 ? 269 PRO   A CG    1 
ATOM   1952 C CD    . PRO   A 1 269 ? -3.283  -1.630  -27.778 1.00 32.53 ? 269 PRO   A CD    1 
ATOM   1953 N N     . ALA   A 1 270 ? -1.339  2.658   -28.671 1.00 25.28 ? 270 ALA   A N     1 
ATOM   1954 C CA    . ALA   A 1 270 ? -1.317  3.779   -29.594 1.00 27.93 ? 270 ALA   A CA    1 
ATOM   1955 C C     . ALA   A 1 270 ? 0.115   4.251   -29.829 1.00 26.07 ? 270 ALA   A C     1 
ATOM   1956 O O     . ALA   A 1 270 ? 1.059   3.790   -29.178 1.00 25.26 ? 270 ALA   A O     1 
ATOM   1957 C CB    . ALA   A 1 270 ? -2.173  4.905   -29.039 1.00 29.91 ? 270 ALA   A CB    1 
ATOM   1958 N N     . THR   A 1 271 ? 0.256   5.232   -30.741 1.00 26.31 ? 271 THR   A N     1 
ATOM   1959 C CA    . THR   A 1 271 ? 1.507   5.953   -30.881 1.00 26.74 ? 271 THR   A CA    1 
ATOM   1960 C C     . THR   A 1 271 ? 1.232   7.441   -30.709 1.00 27.11 ? 271 THR   A C     1 
ATOM   1961 O O     . THR   A 1 271 ? 0.116   7.914   -30.961 1.00 28.23 ? 271 THR   A O     1 
ATOM   1962 C CB    . THR   A 1 271 ? 2.207   5.690   -32.216 1.00 32.85 ? 271 THR   A CB    1 
ATOM   1963 O OG1   . THR   A 1 271 ? 1.582   6.491   -33.214 1.00 34.87 ? 271 THR   A OG1   1 
ATOM   1964 C CG2   . THR   A 1 271 ? 2.177   4.232   -32.620 1.00 32.08 ? 271 THR   A CG2   1 
ATOM   1965 N N     . ARG   A 1 272 ? 2.304   8.145   -30.339 1.00 28.82 ? 272 ARG   A N     1 
ATOM   1966 C CA    . ARG   A 1 272 ? 2.296   9.590   -30.176 1.00 26.64 ? 272 ARG   A CA    1 
ATOM   1967 C C     . ARG   A 1 272 ? 1.855   10.247  -31.472 1.00 26.96 ? 272 ARG   A C     1 
ATOM   1968 O O     . ARG   A 1 272 ? 1.261   11.318  -31.421 1.00 26.73 ? 272 ARG   A O     1 
ATOM   1969 C CB    . ARG   A 1 272 ? 3.670   10.120  -29.745 1.00 28.34 ? 272 ARG   A CB    1 
ATOM   1970 C CG    . ARG   A 1 272 ? 3.660   11.628  -29.517 1.00 30.17 ? 272 ARG   A CG    1 
ATOM   1971 C CD    . ARG   A 1 272 ? 5.003   12.165  -29.048 1.00 35.39 ? 272 ARG   A CD    1 
ATOM   1972 N NE    . ARG   A 1 272 ? 6.085   11.942  -30.008 1.00 36.55 ? 272 ARG   A NE    1 
ATOM   1973 C CZ    . ARG   A 1 272 ? 7.364   11.681  -29.736 1.00 37.45 ? 272 ARG   A CZ    1 
ATOM   1974 N NH1   . ARG   A 1 272 ? 7.803   11.447  -28.509 1.00 39.56 ? 272 ARG   A NH1   1 
ATOM   1975 N NH2   . ARG   A 1 272 ? 8.214   11.644  -30.737 1.00 39.88 ? 272 ARG   A NH2   1 
ATOM   1976 N N     . ASN   A 1 273 ? 2.118   9.614   -32.627 1.00 23.79 ? 273 ASN   A N     1 
ATOM   1977 C CA    . ASN   A 1 273 ? 1.720   10.222  -33.891 1.00 31.22 ? 273 ASN   A CA    1 
ATOM   1978 C C     . ASN   A 1 273 ? 0.214   10.499  -33.973 1.00 31.75 ? 273 ASN   A C     1 
ATOM   1979 O O     . ASN   A 1 273 ? -0.199  11.439  -34.654 1.00 27.79 ? 273 ASN   A O     1 
ATOM   1980 C CB    . ASN   A 1 273 ? 2.170   9.382   -35.084 1.00 36.71 ? 273 ASN   A CB    1 
ATOM   1981 C CG    . ASN   A 1 273 ? 3.590   9.672   -35.521 1.00 46.60 ? 273 ASN   A CG    1 
ATOM   1982 O OD1   . ASN   A 1 273 ? 4.222   10.632  -35.060 1.00 51.20 ? 273 ASN   A OD1   1 
ATOM   1983 N ND2   . ASN   A 1 273 ? 4.098   8.872   -36.447 1.00 45.25 ? 273 ASN   A ND2   1 
ATOM   1984 N N     . GLU   A 1 274 ? -0.620  9.641   -33.359 1.00 30.08 ? 274 GLU   A N     1 
ATOM   1985 C CA    . GLU   A 1 274 ? -2.062  9.849   -33.388 1.00 32.97 ? 274 GLU   A CA    1 
ATOM   1986 C C     . GLU   A 1 274 ? -2.405  11.188  -32.751 1.00 33.68 ? 274 GLU   A C     1 
ATOM   1987 O O     . GLU   A 1 274 ? -3.287  11.893  -33.225 1.00 35.94 ? 274 GLU   A O     1 
ATOM   1988 C CB    . GLU   A 1 274 ? -2.847  8.832   -32.559 1.00 36.20 ? 274 GLU   A CB    1 
ATOM   1989 C CG    . GLU   A 1 274 ? -2.509  7.411   -32.971 1.00 36.24 ? 274 GLU   A CG    1 
ATOM   1990 C CD    . GLU   A 1 274 ? -3.203  6.311   -32.210 1.00 41.84 ? 274 GLU   A CD    1 
ATOM   1991 O OE1   . GLU   A 1 274 ? -4.286  6.503   -31.606 1.00 37.58 ? 274 GLU   A OE1   1 
ATOM   1992 O OE2   . GLU   A 1 274 ? -2.578  5.233   -32.251 1.00 39.95 ? 274 GLU   A OE2   1 
ATOM   1993 N N     . ALA   A 1 275 ? -1.702  11.525  -31.671 1.00 29.34 ? 275 ALA   A N     1 
ATOM   1994 C CA    . ALA   A 1 275 ? -1.924  12.803  -31.018 1.00 31.06 ? 275 ALA   A CA    1 
ATOM   1995 C C     . ALA   A 1 275 ? -1.306  13.926  -31.840 1.00 33.35 ? 275 ALA   A C     1 
ATOM   1996 O O     . ALA   A 1 275 ? -1.888  15.009  -31.978 1.00 32.15 ? 275 ALA   A O     1 
ATOM   1997 C CB    . ALA   A 1 275 ? -1.371  12.772  -29.618 1.00 30.80 ? 275 ALA   A CB    1 
ATOM   1998 N N     . THR   A 1 276 ? -0.118  13.667  -32.386 1.00 28.74 ? 276 THR   A N     1 
ATOM   1999 C CA    . THR   A 1 276 ? 0.578   14.687  -33.140 1.00 28.70 ? 276 THR   A CA    1 
ATOM   2000 C C     . THR   A 1 276 ? -0.362  15.148  -34.240 1.00 28.57 ? 276 THR   A C     1 
ATOM   2001 O O     . THR   A 1 276 ? -0.512  16.351  -34.455 1.00 29.90 ? 276 THR   A O     1 
ATOM   2002 C CB    . THR   A 1 276 ? 1.906   14.156  -33.697 1.00 28.67 ? 276 THR   A CB    1 
ATOM   2003 O OG1   . THR   A 1 276 ? 2.666   13.761  -32.563 1.00 27.25 ? 276 THR   A OG1   1 
ATOM   2004 C CG2   . THR   A 1 276 ? 2.656   15.173  -34.537 1.00 31.62 ? 276 THR   A CG2   1 
ATOM   2005 N N     . LYS   A 1 277 ? -0.975  14.170  -34.940 1.00 28.31 ? 277 LYS   A N     1 
ATOM   2006 C CA    . LYS   A 1 277 ? -1.825  14.450  -36.086 1.00 27.52 ? 277 LYS   A CA    1 
ATOM   2007 C C     . LYS   A 1 277 ? -3.094  15.182  -35.661 1.00 28.26 ? 277 LYS   A C     1 
ATOM   2008 O O     . LYS   A 1 277 ? -3.579  16.082  -36.356 1.00 28.78 ? 277 LYS   A O     1 
ATOM   2009 C CB    . LYS   A 1 277 ? -2.169  13.142  -36.816 1.00 27.55 ? 277 LYS   A CB    1 
ATOM   2010 C CG    . LYS   A 1 277 ? -1.007  12.482  -37.505 1.00 27.25 ? 277 LYS   A CG    1 
ATOM   2011 C CD    . LYS   A 1 277 ? -1.406  11.155  -38.162 1.00 30.50 ? 277 LYS   A CD    1 
ATOM   2012 C CE    . LYS   A 1 277 ? -0.226  10.419  -38.745 1.00 31.85 ? 277 LYS   A CE    1 
ATOM   2013 N NZ    . LYS   A 1 277 ? -0.616  9.036   -39.085 1.00 30.24 ? 277 LYS   A NZ    1 
ATOM   2014 N N     . ALA   A 1 278 ? -3.652  14.769  -34.521 1.00 27.54 ? 278 ALA   A N     1 
ATOM   2015 C CA    . ALA   A 1 278 ? -4.891  15.338  -34.025 1.00 28.79 ? 278 ALA   A CA    1 
ATOM   2016 C C     . ALA   A 1 278 ? -4.730  16.818  -33.693 1.00 27.11 ? 278 ALA   A C     1 
ATOM   2017 O O     . ALA   A 1 278 ? -5.694  17.557  -33.834 1.00 28.01 ? 278 ALA   A O     1 
ATOM   2018 C CB    . ALA   A 1 278 ? -5.344  14.586  -32.803 1.00 30.47 ? 278 ALA   A CB    1 
ATOM   2019 N N     . PHE   A 1 279 ? -3.532  17.226  -33.249 1.00 24.06 ? 279 PHE   A N     1 
ATOM   2020 C CA    . PHE   A 1 279 ? -3.310  18.572  -32.774 1.00 23.89 ? 279 PHE   A CA    1 
ATOM   2021 C C     . PHE   A 1 279 ? -2.441  19.369  -33.740 1.00 26.20 ? 279 PHE   A C     1 
ATOM   2022 O O     . PHE   A 1 279 ? -1.948  20.416  -33.358 1.00 26.40 ? 279 PHE   A O     1 
ATOM   2023 C CB    . PHE   A 1 279 ? -2.649  18.550  -31.394 1.00 24.55 ? 279 PHE   A CB    1 
ATOM   2024 C CG    . PHE   A 1 279 ? -3.589  18.038  -30.322 1.00 24.43 ? 279 PHE   A CG    1 
ATOM   2025 C CD1   . PHE   A 1 279 ? -4.567  18.863  -29.785 1.00 24.45 ? 279 PHE   A CD1   1 
ATOM   2026 C CD2   . PHE   A 1 279 ? -3.498  16.733  -29.865 1.00 25.81 ? 279 PHE   A CD2   1 
ATOM   2027 C CE1   . PHE   A 1 279 ? -5.409  18.390  -28.790 1.00 26.46 ? 279 PHE   A CE1   1 
ATOM   2028 C CE2   . PHE   A 1 279 ? -4.360  16.251  -28.897 1.00 28.65 ? 279 PHE   A CE2   1 
ATOM   2029 C CZ    . PHE   A 1 279 ? -5.315  17.082  -28.363 1.00 29.23 ? 279 PHE   A CZ    1 
ATOM   2030 N N     . ALA   A 1 280 ? -2.293  18.914  -34.992 1.00 26.12 ? 280 ALA   A N     1 
ATOM   2031 C CA    . ALA   A 1 280 ? -1.419  19.587  -35.945 1.00 26.43 ? 280 ALA   A CA    1 
ATOM   2032 C C     . ALA   A 1 280 ? -1.846  21.033  -36.220 1.00 27.86 ? 280 ALA   A C     1 
ATOM   2033 O O     . ALA   A 1 280 ? -0.990  21.856  -36.537 1.00 33.22 ? 280 ALA   A O     1 
ATOM   2034 C CB    . ALA   A 1 280 ? -1.378  18.800  -37.256 1.00 27.59 ? 280 ALA   A CB    1 
ATOM   2035 N N     . GLU   A 1 281 ? -3.140  21.343  -36.136 1.00 28.37 ? 281 GLU   A N     1 
ATOM   2036 C CA    . GLU   A 1 281 ? -3.618  22.681  -36.447 1.00 28.83 ? 281 GLU   A CA    1 
ATOM   2037 C C     . GLU   A 1 281 ? -3.655  23.555  -35.189 1.00 28.29 ? 281 GLU   A C     1 
ATOM   2038 O O     . GLU   A 1 281 ? -4.067  24.717  -35.255 1.00 26.74 ? 281 GLU   A O     1 
ATOM   2039 C CB    . GLU   A 1 281 ? -5.003  22.622  -37.098 1.00 33.08 ? 281 GLU   A CB    1 
ATOM   2040 N N     . PHE   A 1 282 ? -3.229  23.002  -34.048 1.00 24.17 ? 282 PHE   A N     1 
ATOM   2041 C CA    . PHE   A 1 282 ? -3.176  23.781  -32.809 1.00 23.75 ? 282 PHE   A CA    1 
ATOM   2042 C C     . PHE   A 1 282 ? -1.888  24.595  -32.722 1.00 24.82 ? 282 PHE   A C     1 
ATOM   2043 O O     . PHE   A 1 282 ? -0.953  24.504  -33.535 1.00 25.63 ? 282 PHE   A O     1 
ATOM   2044 C CB    . PHE   A 1 282 ? -3.287  22.862  -31.585 1.00 21.24 ? 282 PHE   A CB    1 
ATOM   2045 C CG    . PHE   A 1 282 ? -4.672  22.294  -31.318 1.00 21.75 ? 282 PHE   A CG    1 
ATOM   2046 C CD1   . PHE   A 1 282 ? -5.345  21.527  -32.264 1.00 21.44 ? 282 PHE   A CD1   1 
ATOM   2047 C CD2   . PHE   A 1 282 ? -5.274  22.461  -30.081 1.00 22.83 ? 282 PHE   A CD2   1 
ATOM   2048 C CE1   . PHE   A 1 282 ? -6.600  20.977  -31.984 1.00 20.94 ? 282 PHE   A CE1   1 
ATOM   2049 C CE2   . PHE   A 1 282 ? -6.511  21.898  -29.805 1.00 22.41 ? 282 PHE   A CE2   1 
ATOM   2050 C CZ    . PHE   A 1 282 ? -7.169  21.163  -30.745 1.00 22.31 ? 282 PHE   A CZ    1 
ATOM   2051 N N     . GLY   A 1 283 ? -1.826  25.442  -31.696 1.00 25.42 ? 283 GLY   A N     1 
ATOM   2052 C CA    . GLY   A 1 283 ? -0.671  26.285  -31.493 1.00 24.64 ? 283 GLY   A CA    1 
ATOM   2053 C C     . GLY   A 1 283 ? 0.527   25.566  -30.873 1.00 23.39 ? 283 GLY   A C     1 
ATOM   2054 O O     . GLY   A 1 283 ? 0.488   24.379  -30.550 1.00 24.40 ? 283 GLY   A O     1 
ATOM   2055 N N     . PRO   A 1 284 ? 1.653   26.296  -30.715 1.00 25.67 ? 284 PRO   A N     1 
ATOM   2056 C CA    . PRO   A 1 284 ? 2.923   25.742  -30.235 1.00 27.76 ? 284 PRO   A CA    1 
ATOM   2057 C C     . PRO   A 1 284 ? 2.891   25.085  -28.862 1.00 26.26 ? 284 PRO   A C     1 
ATOM   2058 O O     . PRO   A 1 284 ? 3.599   24.099  -28.641 1.00 24.66 ? 284 PRO   A O     1 
ATOM   2059 C CB    . PRO   A 1 284 ? 3.931   26.935  -30.226 1.00 29.49 ? 284 PRO   A CB    1 
ATOM   2060 C CG    . PRO   A 1 284 ? 3.162   28.149  -30.734 1.00 31.03 ? 284 PRO   A CG    1 
ATOM   2061 C CD    . PRO   A 1 284 ? 1.768   27.710  -31.136 1.00 29.63 ? 284 PRO   A CD    1 
ATOM   2062 N N     . THR   A 1 285 ? 2.094   25.655  -27.943 1.00 24.55 ? 285 THR   A N     1 
ATOM   2063 C CA    . THR   A 1 285 ? 2.047   25.106  -26.606 1.00 24.67 ? 285 THR   A CA    1 
ATOM   2064 C C     . THR   A 1 285 ? 1.487   23.686  -26.624 1.00 23.22 ? 285 THR   A C     1 
ATOM   2065 O O     . THR   A 1 285 ? 2.085   22.795  -26.043 1.00 25.01 ? 285 THR   A O     1 
ATOM   2066 C CB    . THR   A 1 285 ? 1.257   25.985  -25.644 1.00 27.54 ? 285 THR   A CB    1 
ATOM   2067 O OG1   . THR   A 1 285 ? 2.023   27.155  -25.411 1.00 27.80 ? 285 THR   A OG1   1 
ATOM   2068 C CG2   . THR   A 1 285 ? 1.104   25.279  -24.312 1.00 29.82 ? 285 THR   A CG2   1 
ATOM   2069 N N     . VAL   A 1 286 ? 0.333   23.488  -27.271 1.00 22.43 ? 286 VAL   A N     1 
ATOM   2070 C CA    . VAL   A 1 286 ? -0.302  22.183  -27.366 1.00 24.33 ? 286 VAL   A CA    1 
ATOM   2071 C C     . VAL   A 1 286 ? 0.605   21.243  -28.155 1.00 24.20 ? 286 VAL   A C     1 
ATOM   2072 O O     . VAL   A 1 286 ? 0.825   20.124  -27.761 1.00 23.09 ? 286 VAL   A O     1 
ATOM   2073 C CB    . VAL   A 1 286 ? -1.701  22.321  -27.996 1.00 23.02 ? 286 VAL   A CB    1 
ATOM   2074 C CG1   . VAL   A 1 286 ? -2.262  21.006  -28.507 1.00 22.77 ? 286 VAL   A CG1   1 
ATOM   2075 C CG2   . VAL   A 1 286 ? -2.675  22.995  -27.031 1.00 24.23 ? 286 VAL   A CG2   1 
ATOM   2076 N N     . ARG   A 1 287 ? 1.147   21.699  -29.284 1.00 25.57 ? 287 ARG   A N     1 
ATOM   2077 C CA    . ARG   A 1 287 ? 2.018   20.829  -30.063 1.00 25.12 ? 287 ARG   A CA    1 
ATOM   2078 C C     . ARG   A 1 287 ? 3.238   20.373  -29.259 1.00 23.13 ? 287 ARG   A C     1 
ATOM   2079 O O     . ARG   A 1 287 ? 3.619   19.205  -29.319 1.00 24.06 ? 287 ARG   A O     1 
ATOM   2080 C CB    . ARG   A 1 287 ? 2.334   21.508  -31.396 1.00 25.65 ? 287 ARG   A CB    1 
ATOM   2081 C CG    . ARG   A 1 287 ? 1.119   21.506  -32.299 1.00 27.22 ? 287 ARG   A CG    1 
ATOM   2082 C CD    . ARG   A 1 287 ? 1.511   21.832  -33.737 1.00 29.67 ? 287 ARG   A CD    1 
ATOM   2083 N NE    . ARG   A 1 287 ? 1.612   23.284  -33.856 1.00 34.27 ? 287 ARG   A NE    1 
ATOM   2084 C CZ    . ARG   A 1 287 ? 2.703   24.035  -33.935 1.00 35.00 ? 287 ARG   A CZ    1 
ATOM   2085 N NH1   . ARG   A 1 287 ? 3.891   23.496  -33.836 1.00 35.51 ? 287 ARG   A NH1   1 
ATOM   2086 N NH2   . ARG   A 1 287 ? 2.577   25.335  -34.093 1.00 38.48 ? 287 ARG   A NH2   1 
ATOM   2087 N N     . SER   A 1 288 ? 3.821   21.283  -28.469 1.00 24.00 ? 288 SER   A N     1 
ATOM   2088 C CA    . SER   A 1 288 ? 4.943   20.983  -27.598 1.00 25.25 ? 288 SER   A CA    1 
ATOM   2089 C C     . SER   A 1 288 ? 4.530   20.021  -26.481 1.00 24.97 ? 288 SER   A C     1 
ATOM   2090 O O     . SER   A 1 288 ? 5.263   19.088  -26.163 1.00 24.21 ? 288 SER   A O     1 
ATOM   2091 C CB    . SER   A 1 288 ? 5.531   22.253  -27.026 1.00 27.54 ? 288 SER   A CB    1 
ATOM   2092 O OG    . SER   A 1 288 ? 6.072   23.055  -28.073 1.00 30.41 ? 288 SER   A OG    1 
ATOM   2093 N N     . ALA   A 1 289 ? 3.339   20.228  -25.896 1.00 23.79 ? 289 ALA   A N     1 
ATOM   2094 C CA    . ALA   A 1 289 ? 2.897   19.367  -24.804 1.00 23.43 ? 289 ALA   A CA    1 
ATOM   2095 C C     . ALA   A 1 289 ? 2.721   17.935  -25.305 1.00 25.18 ? 289 ALA   A C     1 
ATOM   2096 O O     . ALA   A 1 289 ? 3.165   16.969  -24.685 1.00 24.55 ? 289 ALA   A O     1 
ATOM   2097 C CB    . ALA   A 1 289 ? 1.625   19.901  -24.191 1.00 26.18 ? 289 ALA   A CB    1 
ATOM   2098 N N     . VAL   A 1 290 ? 2.081   17.800  -26.463 1.00 24.15 ? 290 VAL   A N     1 
ATOM   2099 C CA    . VAL   A 1 290 ? 1.855   16.487  -27.030 1.00 26.38 ? 290 VAL   A CA    1 
ATOM   2100 C C     . VAL   A 1 290 ? 3.171   15.811  -27.409 1.00 26.06 ? 290 VAL   A C     1 
ATOM   2101 O O     . VAL   A 1 290 ? 3.282   14.594  -27.331 1.00 27.78 ? 290 VAL   A O     1 
ATOM   2102 C CB    . VAL   A 1 290 ? 0.898   16.674  -28.217 1.00 31.08 ? 290 VAL   A CB    1 
ATOM   2103 C CG1   . VAL   A 1 290 ? 0.887   15.479  -29.153 1.00 31.98 ? 290 VAL   A CG1   1 
ATOM   2104 C CG2   . VAL   A 1 290 ? -0.505  16.961  -27.693 1.00 33.99 ? 290 VAL   A CG2   1 
ATOM   2105 N N     . SER   A 1 291 ? 4.160   16.613  -27.818 1.00 27.88 ? 291 SER   A N     1 
ATOM   2106 C CA    . SER   A 1 291 ? 5.464   16.112  -28.199 1.00 28.66 ? 291 SER   A CA    1 
ATOM   2107 C C     . SER   A 1 291 ? 6.159   15.471  -26.996 1.00 27.47 ? 291 SER   A C     1 
ATOM   2108 O O     . SER   A 1 291 ? 7.088   14.693  -27.193 1.00 29.55 ? 291 SER   A O     1 
ATOM   2109 C CB    . SER   A 1 291 ? 6.322   17.200  -28.801 1.00 26.74 ? 291 SER   A CB    1 
ATOM   2110 O OG    . SER   A 1 291 ? 6.976   17.986  -27.804 1.00 28.63 ? 291 SER   A OG    1 
ATOM   2111 N N     . MET   A 1 292 ? 5.731   15.810  -25.766 1.00 27.31 ? 292 MET   A N     1 
ATOM   2112 C CA    . MET   A 1 292 ? 6.364   15.315  -24.548 1.00 29.37 ? 292 MET   A CA    1 
ATOM   2113 C C     . MET   A 1 292 ? 5.862   13.935  -24.126 1.00 33.26 ? 292 MET   A C     1 
ATOM   2114 O O     . MET   A 1 292 ? 6.448   13.303  -23.241 1.00 33.60 ? 292 MET   A O     1 
ATOM   2115 C CB    . MET   A 1 292 ? 6.194   16.312  -23.400 1.00 30.70 ? 292 MET   A CB    1 
ATOM   2116 C CG    . MET   A 1 292 ? 7.015   17.551  -23.613 1.00 30.91 ? 292 MET   A CG    1 
ATOM   2117 S SD    . MET   A 1 292 ? 7.103   18.655  -22.193 1.00 35.21 ? 292 MET   A SD    1 
ATOM   2118 C CE    . MET   A 1 292 ? 5.541   19.512  -22.369 1.00 36.29 ? 292 MET   A CE    1 
ATOM   2119 N N     . PHE   A 1 293 ? 4.836   13.428  -24.809 1.00 29.46 ? 293 PHE   A N     1 
ATOM   2120 C CA    . PHE   A 1 293 ? 4.419   12.048  -24.635 1.00 29.72 ? 293 PHE   A CA    1 
ATOM   2121 C C     . PHE   A 1 293 ? 5.531   11.077  -25.043 1.00 31.57 ? 293 PHE   A C     1 
ATOM   2122 O O     . PHE   A 1 293 ? 6.316   11.368  -25.947 1.00 28.42 ? 293 PHE   A O     1 
ATOM   2123 C CB    . PHE   A 1 293 ? 3.195   11.757  -25.506 1.00 26.74 ? 293 PHE   A CB    1 
ATOM   2124 C CG    . PHE   A 1 293 ? 1.852   12.298  -25.007 1.00 26.19 ? 293 PHE   A CG    1 
ATOM   2125 C CD1   . PHE   A 1 293 ? 1.539   12.326  -23.659 1.00 28.34 ? 293 PHE   A CD1   1 
ATOM   2126 C CD2   . PHE   A 1 293 ? 0.885   12.721  -25.910 1.00 28.82 ? 293 PHE   A CD2   1 
ATOM   2127 C CE1   . PHE   A 1 293 ? 0.302   12.794  -23.222 1.00 29.39 ? 293 PHE   A CE1   1 
ATOM   2128 C CE2   . PHE   A 1 293 ? -0.360  13.157  -25.475 1.00 30.27 ? 293 PHE   A CE2   1 
ATOM   2129 C CZ    . PHE   A 1 293 ? -0.646  13.185  -24.128 1.00 28.91 ? 293 PHE   A CZ    1 
ATOM   2130 N N     . PRO   A 1 294 ? 5.557   9.847   -24.476 1.00 30.41 ? 294 PRO   A N     1 
ATOM   2131 C CA    . PRO   A 1 294 ? 6.363   8.751   -25.026 1.00 33.21 ? 294 PRO   A CA    1 
ATOM   2132 C C     . PRO   A 1 294 ? 5.930   8.421   -26.454 1.00 36.00 ? 294 PRO   A C     1 
ATOM   2133 O O     . PRO   A 1 294 ? 4.783   8.652   -26.823 1.00 29.69 ? 294 PRO   A O     1 
ATOM   2134 C CB    . PRO   A 1 294 ? 6.102   7.543   -24.078 1.00 32.34 ? 294 PRO   A CB    1 
ATOM   2135 C CG    . PRO   A 1 294 ? 5.441   8.141   -22.863 1.00 34.57 ? 294 PRO   A CG    1 
ATOM   2136 C CD    . PRO   A 1 294 ? 4.742   9.417   -23.330 1.00 30.56 ? 294 PRO   A CD    1 
ATOM   2137 N N     . GLU   A 1 295 ? 6.830   7.817   -27.246 1.00 32.93 ? 295 GLU   A N     1 
ATOM   2138 C CA    . GLU   A 1 295 ? 6.504   7.460   -28.620 1.00 34.73 ? 295 GLU   A CA    1 
ATOM   2139 C C     . GLU   A 1 295 ? 5.396   6.401   -28.664 1.00 32.35 ? 295 GLU   A C     1 
ATOM   2140 O O     . GLU   A 1 295 ? 4.542   6.428   -29.555 1.00 31.83 ? 295 GLU   A O     1 
ATOM   2141 C CB    . GLU   A 1 295 ? 7.779   7.055   -29.373 1.00 41.95 ? 295 GLU   A CB    1 
ATOM   2142 C CG    . GLU   A 1 295 ? 8.721   8.241   -29.575 1.00 46.32 ? 295 GLU   A CG    1 
ATOM   2143 C CD    . GLU   A 1 295 ? 9.938   8.059   -30.470 1.00 58.78 ? 295 GLU   A CD    1 
ATOM   2144 O OE1   . GLU   A 1 295 ? 10.263  6.916   -30.859 1.00 77.08 ? 295 GLU   A OE1   1 
ATOM   2145 O OE2   . GLU   A 1 295 ? 10.568  9.093   -30.783 1.00 57.17 ? 295 GLU   A OE2   1 
ATOM   2146 N N     . LYS   A 1 296 ? 5.402   5.489   -27.686 1.00 32.73 ? 296 LYS   A N     1 
ATOM   2147 C CA    . LYS   A 1 296 ? 4.420   4.422   -27.599 1.00 32.77 ? 296 LYS   A CA    1 
ATOM   2148 C C     . LYS   A 1 296 ? 3.628   4.638   -26.319 1.00 31.28 ? 296 LYS   A C     1 
ATOM   2149 O O     . LYS   A 1 296 ? 4.217   4.839   -25.268 1.00 30.73 ? 296 LYS   A O     1 
ATOM   2150 C CB    . LYS   A 1 296 ? 5.070   3.038   -27.478 1.00 38.55 ? 296 LYS   A CB    1 
ATOM   2151 C CG    . LYS   A 1 296 ? 5.890   2.616   -28.698 1.00 43.68 ? 296 LYS   A CG    1 
ATOM   2152 C CD    . LYS   A 1 296 ? 5.036   2.370   -29.938 1.00 51.57 ? 296 LYS   A CD    1 
ATOM   2153 C CE    . LYS   A 1 296 ? 5.766   1.736   -31.101 1.00 53.12 ? 296 LYS   A CE    1 
ATOM   2154 N NZ    . LYS   A 1 296 ? 4.823   1.187   -32.093 1.00 55.87 ? 296 LYS   A NZ    1 
ATOM   2155 N N     . LEU   A 1 297 ? 2.314   4.580   -26.452 1.00 31.46 ? 297 LEU   A N     1 
ATOM   2156 C CA    . LEU   A 1 297 ? 1.450   4.759   -25.265 1.00 34.77 ? 297 LEU   A CA    1 
ATOM   2157 C C     . LEU   A 1 297 ? 0.120   4.022   -25.463 1.00 34.58 ? 297 LEU   A C     1 
ATOM   2158 O O     . LEU   A 1 297 ? -0.028  3.305   -26.457 1.00 33.42 ? 297 LEU   A O     1 
ATOM   2159 C CB    . LEU   A 1 297 ? 1.281   6.251   -24.974 1.00 37.98 ? 297 LEU   A CB    1 
ATOM   2160 C CG    . LEU   A 1 297 ? 0.396   7.082   -25.907 1.00 41.04 ? 297 LEU   A CG    1 
ATOM   2161 C CD1   . LEU   A 1 297 ? 0.217   8.429   -25.236 1.00 42.77 ? 297 LEU   A CD1   1 
ATOM   2162 C CD2   . LEU   A 1 297 ? 1.002   7.292   -27.269 1.00 47.05 ? 297 LEU   A CD2   1 
ATOM   2163 N N     . GLU   A 1 298 ? -0.764  4.134   -24.482 1.00 32.95 ? 298 GLU   A N     1 
ATOM   2164 C CA    . GLU   A 1 298 ? -2.077  3.522   -24.576 1.00 32.35 ? 298 GLU   A CA    1 
ATOM   2165 C C     . GLU   A 1 298 ? -3.129  4.609   -24.794 1.00 32.42 ? 298 GLU   A C     1 
ATOM   2166 O O     . GLU   A 1 298 ? -2.910  5.790   -24.526 1.00 33.02 ? 298 GLU   A O     1 
ATOM   2167 C CB    . GLU   A 1 298 ? -2.319  2.677   -23.327 1.00 36.22 ? 298 GLU   A CB    1 
ATOM   2168 C CG    . GLU   A 1 298 ? -1.443  1.427   -23.264 1.00 42.65 ? 298 GLU   A CG    1 
ATOM   2169 C CD    . GLU   A 1 298 ? -1.790  0.452   -22.144 1.00 49.03 ? 298 GLU   A CD    1 
ATOM   2170 O OE1   . GLU   A 1 298 ? -1.996  -0.757  -22.423 1.00 52.99 ? 298 GLU   A OE1   1 
ATOM   2171 O OE2   . GLU   A 1 298 ? -1.889  0.916   -20.989 1.00 49.89 ? 298 GLU   A OE2   1 
ATOM   2172 N N     . LYS   A 1 299 ? -4.252  4.215   -25.378 1.00 29.84 ? 299 LYS   A N     1 
ATOM   2173 C CA    . LYS   A 1 299 ? -5.393  5.106   -25.482 1.00 28.29 ? 299 LYS   A CA    1 
ATOM   2174 C C     . LYS   A 1 299 ? -6.543  4.450   -24.733 1.00 29.95 ? 299 LYS   A C     1 
ATOM   2175 O O     . LYS   A 1 299 ? -6.755  3.236   -24.866 1.00 31.54 ? 299 LYS   A O     1 
ATOM   2176 C CB    . LYS   A 1 299 ? -5.642  5.475   -26.939 1.00 29.37 ? 299 LYS   A CB    1 
ATOM   2177 C CG    . LYS   A 1 299 ? -5.935  4.336   -27.867 1.00 30.85 ? 299 LYS   A CG    1 
ATOM   2178 C CD    . LYS   A 1 299 ? -6.043  4.782   -29.311 1.00 35.10 ? 299 LYS   A CD    1 
ATOM   2179 C CE    . LYS   A 1 299 ? -6.322  3.648   -30.219 1.00 36.43 ? 299 LYS   A CE    1 
ATOM   2180 N NZ    . LYS   A 1 299 ? -6.024  4.051   -31.598 1.00 39.70 ? 299 LYS   A NZ    1 
ATOM   2181 N N     . TRP   A 1 300 ? -7.210  5.270   -23.905 1.00 27.04 ? 300 TRP   A N     1 
ATOM   2182 C CA    . TRP   A 1 300 ? -8.345  4.855   -23.087 1.00 25.58 ? 300 TRP   A CA    1 
ATOM   2183 C C     . TRP   A 1 300 ? -9.644  5.305   -23.741 1.00 24.08 ? 300 TRP   A C     1 
ATOM   2184 O O     . TRP   A 1 300 ? -9.888  6.501   -23.917 1.00 23.13 ? 300 TRP   A O     1 
ATOM   2185 C CB    . TRP   A 1 300 ? -8.209  5.426   -21.672 1.00 25.36 ? 300 TRP   A CB    1 
ATOM   2186 C CG    . TRP   A 1 300 ? -9.434  5.253   -20.807 1.00 26.62 ? 300 TRP   A CG    1 
ATOM   2187 C CD1   . TRP   A 1 300 ? -10.194 4.128   -20.653 1.00 27.88 ? 300 TRP   A CD1   1 
ATOM   2188 C CD2   . TRP   A 1 300 ? -10.033 6.252   -19.959 1.00 24.27 ? 300 TRP   A CD2   1 
ATOM   2189 N NE1   . TRP   A 1 300 ? -11.219 4.353   -19.773 1.00 28.13 ? 300 TRP   A NE1   1 
ATOM   2190 C CE2   . TRP   A 1 300 ? -11.143 5.647   -19.321 1.00 25.64 ? 300 TRP   A CE2   1 
ATOM   2191 C CE3   . TRP   A 1 300 ? -9.733  7.589   -19.672 1.00 22.91 ? 300 TRP   A CE3   1 
ATOM   2192 C CZ2   . TRP   A 1 300 ? -11.978 6.348   -18.452 1.00 24.84 ? 300 TRP   A CZ2   1 
ATOM   2193 C CZ3   . TRP   A 1 300 ? -10.527 8.257   -18.774 1.00 21.09 ? 300 TRP   A CZ3   1 
ATOM   2194 C CH2   . TRP   A 1 300 ? -11.618 7.644   -18.158 1.00 22.76 ? 300 TRP   A CH2   1 
ATOM   2195 N N     . ALA   A 1 301 ? -10.468 4.338   -24.131 1.00 22.87 ? 301 ALA   A N     1 
ATOM   2196 C CA    . ALA   A 1 301 ? -11.792 4.624   -24.666 1.00 22.93 ? 301 ALA   A CA    1 
ATOM   2197 C C     . ALA   A 1 301 ? -12.749 4.921   -23.506 1.00 22.79 ? 301 ALA   A C     1 
ATOM   2198 O O     . ALA   A 1 301 ? -13.025 4.046   -22.714 1.00 23.45 ? 301 ALA   A O     1 
ATOM   2199 C CB    . ALA   A 1 301 ? -12.287 3.479   -25.507 1.00 25.40 ? 301 ALA   A CB    1 
ATOM   2200 N N     . VAL   A 1 302 ? -13.268 6.146   -23.431 1.00 22.80 ? 302 VAL   A N     1 
ATOM   2201 C CA    . VAL   A 1 302 ? -14.148 6.526   -22.332 1.00 21.78 ? 302 VAL   A CA    1 
ATOM   2202 C C     . VAL   A 1 302 ? -15.577 6.091   -22.678 1.00 21.08 ? 302 VAL   A C     1 
ATOM   2203 O O     . VAL   A 1 302 ? -16.144 6.474   -23.706 1.00 22.83 ? 302 VAL   A O     1 
ATOM   2204 C CB    . VAL   A 1 302 ? -14.064 8.044   -22.030 1.00 23.93 ? 302 VAL   A CB    1 
ATOM   2205 C CG1   . VAL   A 1 302 ? -14.965 8.414   -20.854 1.00 26.26 ? 302 VAL   A CG1   1 
ATOM   2206 C CG2   . VAL   A 1 302 ? -12.630 8.534   -21.767 1.00 24.55 ? 302 VAL   A CG2   1 
ATOM   2207 N N     . PHE   A 1 303 ? -16.179 5.280   -21.797 1.00 21.35 ? 303 PHE   A N     1 
ATOM   2208 C CA    . PHE   A 1 303 ? -17.554 4.838   -21.916 1.00 19.79 ? 303 PHE   A CA    1 
ATOM   2209 C C     . PHE   A 1 303 ? -18.396 5.548   -20.849 1.00 21.60 ? 303 PHE   A C     1 
ATOM   2210 O O     . PHE   A 1 303 ? -17.864 5.943   -19.790 1.00 21.73 ? 303 PHE   A O     1 
ATOM   2211 C CB    . PHE   A 1 303 ? -17.623 3.312   -21.779 1.00 20.87 ? 303 PHE   A CB    1 
ATOM   2212 C CG    . PHE   A 1 303 ? -17.353 2.497   -23.038 1.00 21.31 ? 303 PHE   A CG    1 
ATOM   2213 C CD1   . PHE   A 1 303 ? -16.210 2.711   -23.803 1.00 22.64 ? 303 PHE   A CD1   1 
ATOM   2214 C CD2   . PHE   A 1 303 ? -18.271 1.535   -23.463 1.00 22.92 ? 303 PHE   A CD2   1 
ATOM   2215 C CE1   . PHE   A 1 303 ? -15.987 1.970   -24.962 1.00 23.26 ? 303 PHE   A CE1   1 
ATOM   2216 C CE2   . PHE   A 1 303 ? -18.043 0.817   -24.627 1.00 24.85 ? 303 PHE   A CE2   1 
ATOM   2217 C CZ    . PHE   A 1 303 ? -16.892 1.005   -25.353 1.00 24.04 ? 303 PHE   A CZ    1 
ATOM   2218 N N     . ASP   A 1 304 ? -19.673 5.767   -21.161 1.00 20.97 ? 304 ASP   A N     1 
ATOM   2219 C CA    . ASP   A 1 304 ? -20.612 6.301   -20.185 1.00 21.59 ? 304 ASP   A CA    1 
ATOM   2220 C C     . ASP   A 1 304 ? -22.004 5.700   -20.389 1.00 21.44 ? 304 ASP   A C     1 
ATOM   2221 O O     . ASP   A 1 304 ? -22.269 4.961   -21.340 1.00 20.30 ? 304 ASP   A O     1 
ATOM   2222 C CB    . ASP   A 1 304 ? -20.576 7.822   -20.229 1.00 22.21 ? 304 ASP   A CB    1 
ATOM   2223 C CG    . ASP   A 1 304 ? -21.211 8.456   -21.448 1.00 23.13 ? 304 ASP   A CG    1 
ATOM   2224 O OD1   . ASP   A 1 304 ? -21.904 7.744   -22.169 1.00 20.51 ? 304 ASP   A OD1   1 
ATOM   2225 O OD2   . ASP   A 1 304 ? -21.029 9.671   -21.617 1.00 19.43 ? 304 ASP   A OD2   1 
ATOM   2226 N N     . MET   A 1 305 ? -22.937 6.081   -19.502 1.00 19.51 ? 305 MET   A N     1 
ATOM   2227 C CA    . MET   A 1 305 ? -24.269 5.538   -19.511 1.00 19.87 ? 305 MET   A CA    1 
ATOM   2228 C C     . MET   A 1 305 ? -25.259 6.602   -19.975 1.00 19.26 ? 305 MET   A C     1 
ATOM   2229 O O     . MET   A 1 305 ? -26.413 6.600   -19.565 1.00 22.08 ? 305 MET   A O     1 
ATOM   2230 C CB    . MET   A 1 305 ? -24.593 4.942   -18.133 1.00 21.31 ? 305 MET   A CB    1 
ATOM   2231 C CG    . MET   A 1 305 ? -23.723 3.753   -17.792 1.00 22.09 ? 305 MET   A CG    1 
ATOM   2232 S SD    . MET   A 1 305 ? -24.055 3.165   -16.110 1.00 24.71 ? 305 MET   A SD    1 
ATOM   2233 C CE    . MET   A 1 305 ? -25.719 2.517   -16.305 1.00 25.07 ? 305 MET   A CE    1 
ATOM   2234 N N     . LEU   A 1 306 ? -24.843 7.450   -20.929 1.00 20.35 ? 306 LEU   A N     1 
ATOM   2235 C CA    . LEU   A 1 306 ? -25.698 8.497   -21.452 1.00 22.34 ? 306 LEU   A CA    1 
ATOM   2236 C C     . LEU   A 1 306 ? -26.832 7.907   -22.283 1.00 21.76 ? 306 LEU   A C     1 
ATOM   2237 O O     . LEU   A 1 306 ? -27.979 8.310   -22.124 1.00 21.70 ? 306 LEU   A O     1 
ATOM   2238 C CB    . LEU   A 1 306 ? -24.921 9.500   -22.291 1.00 21.55 ? 306 LEU   A CB    1 
ATOM   2239 C CG    . LEU   A 1 306 ? -25.751 10.691  -22.794 1.00 25.02 ? 306 LEU   A CG    1 
ATOM   2240 C CD1   . LEU   A 1 306 ? -26.361 11.464  -21.647 1.00 28.80 ? 306 LEU   A CD1   1 
ATOM   2241 C CD2   . LEU   A 1 306 ? -24.883 11.622  -23.631 1.00 31.40 ? 306 LEU   A CD2   1 
ATOM   2242 N N     . GLU   A 1 307 ? -26.519 6.974   -23.194 1.00 20.72 ? 307 GLU   A N     1 
ATOM   2243 C CA    . GLU   A 1 307 ? -27.494 6.549   -24.187 1.00 24.83 ? 307 GLU   A CA    1 
ATOM   2244 C C     . GLU   A 1 307 ? -28.455 5.498   -23.634 1.00 23.71 ? 307 GLU   A C     1 
ATOM   2245 O O     . GLU   A 1 307 ? -29.613 5.479   -24.038 1.00 22.66 ? 307 GLU   A O     1 
ATOM   2246 C CB    . GLU   A 1 307 ? -26.821 6.071   -25.475 1.00 32.29 ? 307 GLU   A CB    1 
ATOM   2247 C CG    . GLU   A 1 307 ? -26.066 7.172   -26.224 1.00 39.74 ? 307 GLU   A CG    1 
ATOM   2248 C CD    . GLU   A 1 307 ? -26.834 8.345   -26.838 1.00 50.89 ? 307 GLU   A CD    1 
ATOM   2249 O OE1   . GLU   A 1 307 ? -26.211 8.990   -27.717 1.00 54.78 ? 307 GLU   A OE1   1 
ATOM   2250 O OE2   . GLU   A 1 307 ? -27.991 8.666   -26.464 1.00 51.67 ? 307 GLU   A OE2   1 
ATOM   2251 N N     . ALA   A 1 308 ? -27.992 4.685   -22.677 1.00 23.22 ? 308 ALA   A N     1 
ATOM   2252 C CA    . ALA   A 1 308 ? -28.739 3.574   -22.116 1.00 21.84 ? 308 ALA   A CA    1 
ATOM   2253 C C     . ALA   A 1 308 ? -28.670 3.619   -20.588 1.00 21.34 ? 308 ALA   A C     1 
ATOM   2254 O O     . ALA   A 1 308 ? -28.095 2.728   -19.994 1.00 20.33 ? 308 ALA   A O     1 
ATOM   2255 C CB    . ALA   A 1 308 ? -28.162 2.251   -22.637 1.00 22.09 ? 308 ALA   A CB    1 
ATOM   2256 N N     . PRO   A 1 309 ? -29.242 4.636   -19.912 1.00 21.41 ? 309 PRO   A N     1 
ATOM   2257 C CA    . PRO   A 1 309 ? -29.171 4.730   -18.457 1.00 19.97 ? 309 PRO   A CA    1 
ATOM   2258 C C     . PRO   A 1 309 ? -30.018 3.668   -17.793 1.00 22.09 ? 309 PRO   A C     1 
ATOM   2259 O O     . PRO   A 1 309 ? -30.975 3.137   -18.376 1.00 20.75 ? 309 PRO   A O     1 
ATOM   2260 C CB    . PRO   A 1 309 ? -29.683 6.147   -18.174 1.00 21.39 ? 309 PRO   A CB    1 
ATOM   2261 C CG    . PRO   A 1 309 ? -30.615 6.410   -19.334 1.00 24.23 ? 309 PRO   A CG    1 
ATOM   2262 C CD    . PRO   A 1 309 ? -29.937 5.780   -20.501 1.00 23.56 ? 309 PRO   A CD    1 
ATOM   2263 N N     . VAL   A 1 310 ? -29.715 3.413   -16.517 1.00 18.99 ? 310 VAL   A N     1 
ATOM   2264 C CA    . VAL   A 1 310 ? -30.669 2.671   -15.717 1.00 21.15 ? 310 VAL   A CA    1 
ATOM   2265 C C     . VAL   A 1 310 ? -31.843 3.583   -15.384 1.00 22.32 ? 310 VAL   A C     1 
ATOM   2266 O O     . VAL   A 1 310 ? -31.649 4.784   -15.268 1.00 22.83 ? 310 VAL   A O     1 
ATOM   2267 C CB    . VAL   A 1 310 ? -29.997 2.114   -14.459 1.00 21.34 ? 310 VAL   A CB    1 
ATOM   2268 C CG1   . VAL   A 1 310 ? -28.944 1.095   -14.801 1.00 21.38 ? 310 VAL   A CG1   1 
ATOM   2269 C CG2   . VAL   A 1 310 ? -29.400 3.230   -13.614 1.00 22.50 ? 310 VAL   A CG2   1 
ATOM   2270 N N     . PRO   A 1 311 ? -33.065 3.018   -15.258 1.00 21.38 ? 311 PRO   A N     1 
ATOM   2271 C CA    . PRO   A 1 311 ? -34.274 3.765   -14.921 1.00 22.76 ? 311 PRO   A CA    1 
ATOM   2272 C C     . PRO   A 1 311 ? -34.370 4.198   -13.469 1.00 22.23 ? 311 PRO   A C     1 
ATOM   2273 O O     . PRO   A 1 311 ? -35.100 5.119   -13.174 1.00 21.56 ? 311 PRO   A O     1 
ATOM   2274 C CB    . PRO   A 1 311 ? -35.410 2.792   -15.323 1.00 24.34 ? 311 PRO   A CB    1 
ATOM   2275 C CG    . PRO   A 1 311 ? -34.806 1.466   -15.131 1.00 23.66 ? 311 PRO   A CG    1 
ATOM   2276 C CD    . PRO   A 1 311 ? -33.362 1.616   -15.581 1.00 23.42 ? 311 PRO   A CD    1 
ATOM   2277 N N     . THR   A 1 312 ? -33.610 3.518   -12.605 1.00 20.67 ? 312 THR   A N     1 
ATOM   2278 C CA    . THR   A 1 312 ? -33.590 3.793   -11.178 1.00 22.47 ? 312 THR   A CA    1 
ATOM   2279 C C     . THR   A 1 312 ? -32.315 3.153   -10.639 1.00 18.76 ? 312 THR   A C     1 
ATOM   2280 O O     . THR   A 1 312 ? -31.716 2.315   -11.287 1.00 18.60 ? 312 THR   A O     1 
ATOM   2281 C CB    . THR   A 1 312 ? -34.838 3.222   -10.498 1.00 23.28 ? 312 THR   A CB    1 
ATOM   2282 O OG1   . THR   A 1 312 ? -34.868 3.491   -9.086  1.00 23.23 ? 312 THR   A OG1   1 
ATOM   2283 C CG2   . THR   A 1 312 ? -34.959 1.724   -10.669 1.00 20.93 ? 312 THR   A CG2   1 
ATOM   2284 N N     . PHE   A 1 313 ? -31.961 3.488   -9.407  1.00 17.59 ? 313 PHE   A N     1 
ATOM   2285 C CA    . PHE   A 1 313 ? -30.787 2.922   -8.775  1.00 18.04 ? 313 PHE   A CA    1 
ATOM   2286 C C     . PHE   A 1 313 ? -31.152 1.862   -7.737  1.00 17.98 ? 313 PHE   A C     1 
ATOM   2287 O O     . PHE   A 1 313 ? -30.238 1.299   -7.156  1.00 21.21 ? 313 PHE   A O     1 
ATOM   2288 C CB    . PHE   A 1 313 ? -29.944 3.991   -8.086  1.00 18.79 ? 313 PHE   A CB    1 
ATOM   2289 C CG    . PHE   A 1 313 ? -29.304 5.001   -9.021  1.00 19.05 ? 313 PHE   A CG    1 
ATOM   2290 C CD1   . PHE   A 1 313 ? -29.227 4.792   -10.396 1.00 19.85 ? 313 PHE   A CD1   1 
ATOM   2291 C CD2   . PHE   A 1 313 ? -28.690 6.123   -8.502  1.00 19.05 ? 313 PHE   A CD2   1 
ATOM   2292 C CE1   . PHE   A 1 313 ? -28.648 5.749   -11.206 1.00 20.58 ? 313 PHE   A CE1   1 
ATOM   2293 C CE2   . PHE   A 1 313 ? -28.139 7.075   -9.316  1.00 19.40 ? 313 PHE   A CE2   1 
ATOM   2294 C CZ    . PHE   A 1 313 ? -28.109 6.885   -10.665 1.00 20.06 ? 313 PHE   A CZ    1 
ATOM   2295 N N     . ALA   A 1 314 ? -32.444 1.577   -7.575  1.00 19.14 ? 314 ALA   A N     1 
ATOM   2296 C CA    . ALA   A 1 314 ? -32.900 0.616   -6.576  1.00 19.78 ? 314 ALA   A CA    1 
ATOM   2297 C C     . ALA   A 1 314 ? -34.077 -0.201  -7.078  1.00 20.20 ? 314 ALA   A C     1 
ATOM   2298 O O     . ALA   A 1 314 ? -35.018 0.362   -7.634  1.00 21.61 ? 314 ALA   A O     1 
ATOM   2299 C CB    . ALA   A 1 314 ? -33.331 1.369   -5.350  1.00 19.46 ? 314 ALA   A CB    1 
ATOM   2300 N N     . LYS   A 1 315 ? -34.102 -1.463  -6.640  1.00 20.53 ? 315 LYS   A N     1 
ATOM   2301 C CA    . LYS   A 1 315 ? -35.156 -2.399  -6.961  1.00 22.61 ? 315 LYS   A CA    1 
ATOM   2302 C C     . LYS   A 1 315 ? -35.133 -3.461  -5.871  1.00 19.55 ? 315 LYS   A C     1 
ATOM   2303 O O     . LYS   A 1 315 ? -34.182 -4.246  -5.790  1.00 22.18 ? 315 LYS   A O     1 
ATOM   2304 C CB    . LYS   A 1 315 ? -34.972 -3.054  -8.340  1.00 24.99 ? 315 LYS   A CB    1 
ATOM   2305 C CG    . LYS   A 1 315 ? -36.147 -3.884  -8.815  1.00 32.30 ? 315 LYS   A CG    1 
ATOM   2306 C CD    . LYS   A 1 315 ? -36.030 -4.222  -10.305 1.00 36.83 ? 315 LYS   A CD    1 
ATOM   2307 C CE    . LYS   A 1 315 ? -36.731 -5.486  -10.655 1.00 40.23 ? 315 LYS   A CE    1 
ATOM   2308 N NZ    . LYS   A 1 315 ? -36.649 -5.747  -12.093 1.00 44.05 ? 315 LYS   A NZ    1 
ATOM   2309 N N     . GLY   A 1 316 ? -36.197 -3.445  -5.058  1.00 22.01 ? 316 GLY   A N     1 
ATOM   2310 C CA    . GLY   A 1 316 ? -36.301 -4.314  -3.908  1.00 21.13 ? 316 GLY   A CA    1 
ATOM   2311 C C     . GLY   A 1 316 ? -35.119 -4.071  -2.974  1.00 20.24 ? 316 GLY   A C     1 
ATOM   2312 O O     . GLY   A 1 316 ? -34.783 -2.935  -2.689  1.00 19.75 ? 316 GLY   A O     1 
ATOM   2313 N N     . ARG   A 1 317 ? -34.451 -5.158  -2.582  1.00 19.90 ? 317 ARG   A N     1 
ATOM   2314 C CA    . ARG   A 1 317 ? -33.331 -5.089  -1.657  1.00 20.74 ? 317 ARG   A CA    1 
ATOM   2315 C C     . ARG   A 1 317 ? -31.990 -4.778  -2.329  1.00 20.39 ? 317 ARG   A C     1 
ATOM   2316 O O     . ARG   A 1 317 ? -30.930 -4.866  -1.694  1.00 21.43 ? 317 ARG   A O     1 
ATOM   2317 C CB    . ARG   A 1 317 ? -33.248 -6.468  -0.997  1.00 21.85 ? 317 ARG   A CB    1 
ATOM   2318 C CG    . ARG   A 1 317 ? -34.314 -6.788  0.034   1.00 26.09 ? 317 ARG   A CG    1 
ATOM   2319 C CD    . ARG   A 1 317 ? -34.120 -8.215  0.491   1.00 27.40 ? 317 ARG   A CD    1 
ATOM   2320 N NE    . ARG   A 1 317 ? -35.079 -8.663  1.519   1.00 28.97 ? 317 ARG   A NE    1 
ATOM   2321 C CZ    . ARG   A 1 317 ? -35.012 -8.441  2.835   1.00 30.12 ? 317 ARG   A CZ    1 
ATOM   2322 N NH1   . ARG   A 1 317 ? -34.140 -7.595  3.363   1.00 27.03 ? 317 ARG   A NH1   1 
ATOM   2323 N NH2   . ARG   A 1 317 ? -35.864 -9.067  3.641   1.00 28.95 ? 317 ARG   A NH2   1 
ATOM   2324 N N     . VAL   A 1 318 ? -31.994 -4.466  -3.634  1.00 19.50 ? 318 VAL   A N     1 
ATOM   2325 C CA    . VAL   A 1 318 ? -30.777 -4.350  -4.413  1.00 19.88 ? 318 VAL   A CA    1 
ATOM   2326 C C     . VAL   A 1 318 ? -30.704 -2.928  -4.973  1.00 19.39 ? 318 VAL   A C     1 
ATOM   2327 O O     . VAL   A 1 318 ? -31.730 -2.357  -5.363  1.00 19.62 ? 318 VAL   A O     1 
ATOM   2328 C CB    . VAL   A 1 318 ? -30.725 -5.399  -5.529  1.00 19.43 ? 318 VAL   A CB    1 
ATOM   2329 C CG1   . VAL   A 1 318 ? -29.467 -5.322  -6.366  1.00 20.97 ? 318 VAL   A CG1   1 
ATOM   2330 C CG2   . VAL   A 1 318 ? -30.923 -6.798  -4.963  1.00 21.28 ? 318 VAL   A CG2   1 
ATOM   2331 N N     . CYS   A 1 319 ? -29.489 -2.376  -4.947  1.00 20.21 ? 319 CYS   A N     1 
ATOM   2332 C CA    . CYS   A 1 319 ? -29.226 -1.079  -5.554  1.00 18.69 ? 319 CYS   A CA    1 
ATOM   2333 C C     . CYS   A 1 319 ? -27.836 -1.009  -6.156  1.00 20.04 ? 319 CYS   A C     1 
ATOM   2334 O O     . CYS   A 1 319 ? -27.021 -1.939  -6.063  1.00 21.12 ? 319 CYS   A O     1 
ATOM   2335 C CB    . CYS   A 1 319 ? -29.434 0.076   -4.578  1.00 20.06 ? 319 CYS   A CB    1 
ATOM   2336 S SG    . CYS   A 1 319 ? -28.221 0.085   -3.232  1.00 22.65 ? 319 CYS   A SG    1 
ATOM   2337 N N     . LEU   A 1 320 ? -27.618 0.122   -6.846  1.00 18.01 ? 320 LEU   A N     1 
ATOM   2338 C CA    . LEU   A 1 320 ? -26.392 0.422   -7.552  1.00 17.40 ? 320 LEU   A CA    1 
ATOM   2339 C C     . LEU   A 1 320 ? -25.813 1.751   -7.043  1.00 16.42 ? 320 LEU   A C     1 
ATOM   2340 O O     . LEU   A 1 320 ? -26.561 2.693   -6.789  1.00 17.93 ? 320 LEU   A O     1 
ATOM   2341 C CB    . LEU   A 1 320 ? -26.690 0.545   -9.043  1.00 17.62 ? 320 LEU   A CB    1 
ATOM   2342 C CG    . LEU   A 1 320 ? -27.428 -0.628  -9.711  1.00 17.99 ? 320 LEU   A CG    1 
ATOM   2343 C CD1   . LEU   A 1 320 ? -27.831 -0.296  -11.135 1.00 19.79 ? 320 LEU   A CD1   1 
ATOM   2344 C CD2   . LEU   A 1 320 ? -26.500 -1.832  -9.718  1.00 18.92 ? 320 LEU   A CD2   1 
ATOM   2345 N N     . ALA   A 1 321 ? -24.478 1.817   -7.015  1.00 16.66 ? 321 ALA   A N     1 
ATOM   2346 C CA    . ALA   A 1 321 ? -23.692 3.001   -6.693  1.00 18.30 ? 321 ALA   A CA    1 
ATOM   2347 C C     . ALA   A 1 321 ? -22.462 3.091   -7.604  1.00 19.30 ? 321 ALA   A C     1 
ATOM   2348 O O     . ALA   A 1 321 ? -21.954 2.087   -8.099  1.00 18.62 ? 321 ALA   A O     1 
ATOM   2349 C CB    . ALA   A 1 321 ? -23.291 2.945   -5.219  1.00 17.73 ? 321 ALA   A CB    1 
ATOM   2350 N N     . GLY   A 1 322 ? -21.962 4.310   -7.816  1.00 19.47 ? 322 GLY   A N     1 
ATOM   2351 C CA    . GLY   A 1 322 ? -20.722 4.505   -8.544  1.00 18.15 ? 322 GLY   A CA    1 
ATOM   2352 C C     . GLY   A 1 322 ? -20.946 4.238   -10.028 1.00 17.46 ? 322 GLY   A C     1 
ATOM   2353 O O     . GLY   A 1 322 ? -22.042 4.505   -10.571 1.00 16.99 ? 322 GLY   A O     1 
ATOM   2354 N N     . ASP   A 1 323 ? -19.922 3.715   -10.679 1.00 17.72 ? 323 ASP   A N     1 
ATOM   2355 C CA    . ASP   A 1 323 ? -19.952 3.492   -12.131 1.00 16.77 ? 323 ASP   A CA    1 
ATOM   2356 C C     . ASP   A 1 323 ? -21.020 2.473   -12.520 1.00 19.59 ? 323 ASP   A C     1 
ATOM   2357 O O     . ASP   A 1 323 ? -21.540 2.465   -13.644 1.00 18.80 ? 323 ASP   A O     1 
ATOM   2358 C CB    . ASP   A 1 323 ? -18.588 3.074   -12.648 1.00 17.81 ? 323 ASP   A CB    1 
ATOM   2359 C CG    . ASP   A 1 323 ? -17.528 4.174   -12.695 1.00 20.15 ? 323 ASP   A CG    1 
ATOM   2360 O OD1   . ASP   A 1 323 ? -17.841 5.333   -12.296 1.00 22.24 ? 323 ASP   A OD1   1 
ATOM   2361 O OD2   . ASP   A 1 323 ? -16.387 3.845   -13.087 1.00 20.90 ? 323 ASP   A OD2   1 
ATOM   2362 N N     . ALA   A 1 324 ? -21.333 1.557   -11.595 1.00 18.32 ? 324 ALA   A N     1 
ATOM   2363 C CA    . ALA   A 1 324 ? -22.458 0.657   -11.835 1.00 19.24 ? 324 ALA   A CA    1 
ATOM   2364 C C     . ALA   A 1 324 ? -23.749 1.432   -12.118 1.00 18.95 ? 324 ALA   A C     1 
ATOM   2365 O O     . ALA   A 1 324 ? -24.582 0.978   -12.881 1.00 20.02 ? 324 ALA   A O     1 
ATOM   2366 C CB    . ALA   A 1 324 ? -22.643 -0.240  -10.646 1.00 20.16 ? 324 ALA   A CB    1 
ATOM   2367 N N     . ALA   A 1 325 ? -23.969 2.570   -11.443 1.00 18.96 ? 325 ALA   A N     1 
ATOM   2368 C CA    . ALA   A 1 325 ? -25.194 3.347   -11.544 1.00 18.29 ? 325 ALA   A CA    1 
ATOM   2369 C C     . ALA   A 1 325 ? -25.120 4.410   -12.636 1.00 18.15 ? 325 ALA   A C     1 
ATOM   2370 O O     . ALA   A 1 325 ? -26.135 4.671   -13.298 1.00 18.37 ? 325 ALA   A O     1 
ATOM   2371 C CB    . ALA   A 1 325 ? -25.491 4.011   -10.228 1.00 19.14 ? 325 ALA   A CB    1 
ATOM   2372 N N     . HIS   A 1 326 ? -23.944 5.016   -12.822 1.00 19.84 ? 326 HIS   A N     1 
ATOM   2373 C CA    . HIS   A 1 326 ? -23.877 6.220   -13.651 1.00 17.84 ? 326 HIS   A CA    1 
ATOM   2374 C C     . HIS   A 1 326 ? -22.465 6.482   -14.190 1.00 20.69 ? 326 HIS   A C     1 
ATOM   2375 O O     . HIS   A 1 326 ? -21.997 7.613   -14.103 1.00 21.48 ? 326 HIS   A O     1 
ATOM   2376 C CB    . HIS   A 1 326 ? -24.363 7.425   -12.843 1.00 18.04 ? 326 HIS   A CB    1 
ATOM   2377 C CG    . HIS   A 1 326 ? -23.737 7.557   -11.515 1.00 19.47 ? 326 HIS   A CG    1 
ATOM   2378 N ND1   . HIS   A 1 326 ? -22.380 7.778   -11.381 1.00 22.30 ? 326 HIS   A ND1   1 
ATOM   2379 C CD2   . HIS   A 1 326 ? -24.243 7.456   -10.268 1.00 20.81 ? 326 HIS   A CD2   1 
ATOM   2380 C CE1   . HIS   A 1 326 ? -22.077 7.808   -10.084 1.00 20.73 ? 326 HIS   A CE1   1 
ATOM   2381 N NE2   . HIS   A 1 326 ? -23.197 7.613   -9.394  1.00 19.38 ? 326 HIS   A NE2   1 
ATOM   2382 N N     . ALA   A 1 327 ? -21.798 5.470   -14.778 1.00 18.79 ? 327 ALA   A N     1 
ATOM   2383 C CA    . ALA   A 1 327 ? -20.488 5.690   -15.380 1.00 19.27 ? 327 ALA   A CA    1 
ATOM   2384 C C     . ALA   A 1 327 ? -20.551 6.929   -16.278 1.00 18.53 ? 327 ALA   A C     1 
ATOM   2385 O O     . ALA   A 1 327 ? -21.454 7.046   -17.112 1.00 21.34 ? 327 ALA   A O     1 
ATOM   2386 C CB    . ALA   A 1 327 ? -20.062 4.489   -16.192 1.00 20.45 ? 327 ALA   A CB    1 
ATOM   2387 N N     . SER   A 1 328 ? -19.592 7.832   -16.048 1.00 18.74 ? 328 SER   A N     1 
ATOM   2388 C CA    . SER   A 1 328 ? -19.565 9.146   -16.660 1.00 20.11 ? 328 SER   A CA    1 
ATOM   2389 C C     . SER   A 1 328 ? -18.242 9.372   -17.393 1.00 19.85 ? 328 SER   A C     1 
ATOM   2390 O O     . SER   A 1 328 ? -17.194 8.837   -17.027 1.00 20.46 ? 328 SER   A O     1 
ATOM   2391 C CB    . SER   A 1 328 ? -19.737 10.223  -15.624 1.00 22.47 ? 328 SER   A CB    1 
ATOM   2392 O OG    . SER   A 1 328 ? -19.903 11.469  -16.285 1.00 28.87 ? 328 SER   A OG    1 
ATOM   2393 N N     . THR   A 1 329 ? -18.243 10.290  -18.366 1.00 18.77 ? 329 THR   A N     1 
ATOM   2394 C CA    . THR   A 1 329 ? -16.974 10.854  -18.809 1.00 18.54 ? 329 THR   A CA    1 
ATOM   2395 C C     . THR   A 1 329 ? -16.344 11.623  -17.646 1.00 20.83 ? 329 THR   A C     1 
ATOM   2396 O O     . THR   A 1 329 ? -17.057 12.020  -16.729 1.00 21.19 ? 329 THR   A O     1 
ATOM   2397 C CB    . THR   A 1 329 ? -17.141 11.766  -20.019 1.00 20.89 ? 329 THR   A CB    1 
ATOM   2398 O OG1   . THR   A 1 329 ? -17.940 12.879  -19.624 1.00 21.92 ? 329 THR   A OG1   1 
ATOM   2399 C CG2   . THR   A 1 329 ? -17.739 11.020  -21.184 1.00 23.36 ? 329 THR   A CG2   1 
ATOM   2400 N N     . PRO   A 1 330 ? -15.006 11.825  -17.643 1.00 20.59 ? 330 PRO   A N     1 
ATOM   2401 C CA    . PRO   A 1 330 ? -14.325 12.556  -16.574 1.00 22.18 ? 330 PRO   A CA    1 
ATOM   2402 C C     . PRO   A 1 330 ? -14.189 14.062  -16.788 1.00 20.64 ? 330 PRO   A C     1 
ATOM   2403 O O     . PRO   A 1 330 ? -13.387 14.678  -16.108 1.00 22.83 ? 330 PRO   A O     1 
ATOM   2404 C CB    . PRO   A 1 330 ? -12.943 11.883  -16.585 1.00 23.40 ? 330 PRO   A CB    1 
ATOM   2405 C CG    . PRO   A 1 330 ? -12.688 11.661  -18.046 1.00 22.63 ? 330 PRO   A CG    1 
ATOM   2406 C CD    . PRO   A 1 330 ? -14.044 11.188  -18.573 1.00 21.17 ? 330 PRO   A CD    1 
ATOM   2407 N N     . ASN   A 1 331 ? -14.993 14.648  -17.695 1.00 21.39 ? 331 ASN   A N     1 
ATOM   2408 C CA    . ASN   A 1 331 ? -14.763 16.011  -18.150 1.00 21.53 ? 331 ASN   A CA    1 
ATOM   2409 C C     . ASN   A 1 331 ? -15.107 17.032  -17.075 1.00 25.35 ? 331 ASN   A C     1 
ATOM   2410 O O     . ASN   A 1 331 ? -14.715 18.205  -17.193 1.00 24.93 ? 331 ASN   A O     1 
ATOM   2411 C CB    . ASN   A 1 331 ? -15.518 16.309  -19.428 1.00 22.94 ? 331 ASN   A CB    1 
ATOM   2412 C CG    . ASN   A 1 331 ? -15.110 15.354  -20.521 1.00 22.34 ? 331 ASN   A CG    1 
ATOM   2413 O OD1   . ASN   A 1 331 ? -13.915 15.049  -20.651 1.00 26.57 ? 331 ASN   A OD1   1 
ATOM   2414 N ND2   . ASN   A 1 331 ? -16.067 14.812  -21.249 1.00 24.68 ? 331 ASN   A ND2   1 
ATOM   2415 N N     . GLN   A 1 332 ? -15.821 16.608  -16.033 1.00 22.68 ? 332 GLN   A N     1 
ATOM   2416 C CA    . GLN   A 1 332 ? -16.152 17.516  -14.901 1.00 23.66 ? 332 GLN   A CA    1 
ATOM   2417 C C     . GLN   A 1 332 ? -15.603 16.891  -13.620 1.00 25.08 ? 332 GLN   A C     1 
ATOM   2418 O O     . GLN   A 1 332 ? -16.190 17.115  -12.560 1.00 25.51 ? 332 GLN   A O     1 
ATOM   2419 C CB    . GLN   A 1 332 ? -17.652 17.773  -14.780 1.00 23.44 ? 332 GLN   A CB    1 
ATOM   2420 C CG    . GLN   A 1 332 ? -18.209 18.720  -15.837 1.00 26.73 ? 332 GLN   A CG    1 
ATOM   2421 C CD    . GLN   A 1 332 ? -18.097 20.182  -15.462 1.00 36.49 ? 332 GLN   A CD    1 
ATOM   2422 O OE1   . GLN   A 1 332 ? -17.665 20.544  -14.362 1.00 39.83 ? 332 GLN   A OE1   1 
ATOM   2423 N NE2   . GLN   A 1 332 ? -18.474 21.046  -16.390 1.00 40.41 ? 332 GLN   A NE2   1 
ATOM   2424 N N     . GLY   A 1 333 ? -14.505 16.168  -13.747 1.00 24.73 ? 333 GLY   A N     1 
ATOM   2425 C CA    . GLY   A 1 333 ? -13.901 15.455  -12.643 1.00 26.91 ? 333 GLY   A CA    1 
ATOM   2426 C C     . GLY   A 1 333 ? -14.270 13.974  -12.673 1.00 23.73 ? 333 GLY   A C     1 
ATOM   2427 O O     . GLY   A 1 333 ? -15.181 13.533  -13.362 1.00 25.87 ? 333 GLY   A O     1 
ATOM   2428 N N     . GLY   A 1 334 ? -13.507 13.180  -11.939 1.00 24.81 ? 334 GLY   A N     1 
ATOM   2429 C CA    . GLY   A 1 334 ? -13.683 11.737  -11.992 1.00 24.00 ? 334 GLY   A CA    1 
ATOM   2430 C C     . GLY   A 1 334 ? -15.054 11.364  -11.433 1.00 24.71 ? 334 GLY   A C     1 
ATOM   2431 O O     . GLY   A 1 334 ? -15.444 11.836  -10.368 1.00 24.58 ? 334 GLY   A O     1 
ATOM   2432 N N     . GLY   A 1 335 ? -15.745 10.494  -12.164 1.00 24.62 ? 335 GLY   A N     1 
ATOM   2433 C CA    . GLY   A 1 335 ? -17.025 9.942   -11.745 1.00 25.98 ? 335 GLY   A CA    1 
ATOM   2434 C C     . GLY   A 1 335 ? -16.937 9.269   -10.380 1.00 23.98 ? 335 GLY   A C     1 
ATOM   2435 O O     . GLY   A 1 335 ? -17.928 9.235   -9.644  1.00 25.53 ? 335 GLY   A O     1 
ATOM   2436 N N     . ALA   A 1 336 ? -15.731 8.800   -10.037 1.00 23.67 ? 336 ALA   A N     1 
ATOM   2437 C CA    . ALA   A 1 336 ? -15.501 8.149   -8.753  1.00 23.95 ? 336 ALA   A CA    1 
ATOM   2438 C C     . ALA   A 1 336 ? -15.928 9.085   -7.639  1.00 22.46 ? 336 ALA   A C     1 
ATOM   2439 O O     . ALA   A 1 336 ? -16.440 8.651   -6.611  1.00 22.76 ? 336 ALA   A O     1 
ATOM   2440 C CB    . ALA   A 1 336 ? -14.037 7.768   -8.593  1.00 25.15 ? 336 ALA   A CB    1 
ATOM   2441 N N     . GLY   A 1 337 ? -15.723 10.389  -7.830  1.00 22.74 ? 337 GLY   A N     1 
ATOM   2442 C CA    . GLY   A 1 337 ? -16.150 11.337  -6.806  1.00 22.81 ? 337 GLY   A CA    1 
ATOM   2443 C C     . GLY   A 1 337 ? -17.655 11.299  -6.508  1.00 22.89 ? 337 GLY   A C     1 
ATOM   2444 O O     . GLY   A 1 337 ? -18.084 11.443  -5.357  1.00 24.38 ? 337 GLY   A O     1 
ATOM   2445 N N     . PHE   A 1 338 ? -18.491 11.106  -7.533  1.00 23.49 ? 338 PHE   A N     1 
ATOM   2446 C CA    . PHE   A 1 338 ? -19.931 11.064  -7.347  1.00 23.86 ? 338 PHE   A CA    1 
ATOM   2447 C C     . PHE   A 1 338 ? -20.312 9.684   -6.823  1.00 24.22 ? 338 PHE   A C     1 
ATOM   2448 O O     . PHE   A 1 338 ? -21.310 9.535   -6.118  1.00 24.06 ? 338 PHE   A O     1 
ATOM   2449 C CB    . PHE   A 1 338 ? -20.640 11.555  -8.619  1.00 28.31 ? 338 PHE   A CB    1 
ATOM   2450 C CG    . PHE   A 1 338 ? -20.096 12.914  -9.072  1.00 28.04 ? 338 PHE   A CG    1 
ATOM   2451 C CD1   . PHE   A 1 338 ? -18.862 12.999  -9.737  1.00 32.90 ? 338 PHE   A CD1   1 
ATOM   2452 C CD2   . PHE   A 1 338 ? -20.828 14.092  -8.892  1.00 29.01 ? 338 PHE   A CD2   1 
ATOM   2453 C CE1   . PHE   A 1 338 ? -18.362 14.227  -10.182 1.00 35.58 ? 338 PHE   A CE1   1 
ATOM   2454 C CE2   . PHE   A 1 338 ? -20.334 15.307  -9.349  1.00 31.68 ? 338 PHE   A CE2   1 
ATOM   2455 C CZ    . PHE   A 1 338 ? -19.103 15.380  -9.994  1.00 32.75 ? 338 PHE   A CZ    1 
ATOM   2456 N N     . GLY   A 1 339 ? -19.484 8.670   -7.097  1.00 19.83 ? 339 GLY   A N     1 
ATOM   2457 C CA    . GLY   A 1 339 ? -19.621 7.403   -6.394  1.00 19.05 ? 339 GLY   A CA    1 
ATOM   2458 C C     . GLY   A 1 339 ? -19.456 7.569   -4.888  1.00 18.65 ? 339 GLY   A C     1 
ATOM   2459 O O     . GLY   A 1 339 ? -20.152 6.893   -4.104  1.00 20.18 ? 339 GLY   A O     1 
ATOM   2460 N N     . ILE   A 1 340 ? -18.532 8.450   -4.477  1.00 20.08 ? 340 ILE   A N     1 
ATOM   2461 C CA    . ILE   A 1 340 ? -18.336 8.715   -3.053  1.00 19.79 ? 340 ILE   A CA    1 
ATOM   2462 C C     . ILE   A 1 340 ? -19.574 9.408   -2.474  1.00 19.85 ? 340 ILE   A C     1 
ATOM   2463 O O     . ILE   A 1 340 ? -19.974 9.127   -1.342  1.00 20.06 ? 340 ILE   A O     1 
ATOM   2464 C CB    . ILE   A 1 340 ? -17.003 9.456   -2.807  1.00 21.30 ? 340 ILE   A CB    1 
ATOM   2465 C CG1   . ILE   A 1 340 ? -15.781 8.580   -3.231  1.00 21.56 ? 340 ILE   A CG1   1 
ATOM   2466 C CG2   . ILE   A 1 340 ? -16.884 9.901   -1.352  1.00 20.73 ? 340 ILE   A CG2   1 
ATOM   2467 C CD1   . ILE   A 1 340 ? -14.431 9.211   -2.963  1.00 25.45 ? 340 ILE   A CD1   1 
ATOM   2468 N N     . GLU   A 1 341 ? -20.217 10.322  -3.222  1.00 17.61 ? 341 GLU   A N     1 
ATOM   2469 C CA    . GLU   A 1 341 ? -21.484 10.889  -2.784  1.00 19.34 ? 341 GLU   A CA    1 
ATOM   2470 C C     . GLU   A 1 341 ? -22.544 9.799   -2.588  1.00 20.07 ? 341 GLU   A C     1 
ATOM   2471 O O     . GLU   A 1 341 ? -23.346 9.832   -1.653  1.00 18.98 ? 341 GLU   A O     1 
ATOM   2472 C CB    . GLU   A 1 341 ? -22.063 11.908  -3.754  1.00 22.27 ? 341 GLU   A CB    1 
ATOM   2473 C CG    . GLU   A 1 341 ? -21.191 13.134  -3.886  1.00 24.17 ? 341 GLU   A CG    1 
ATOM   2474 C CD    . GLU   A 1 341 ? -21.815 14.120  -4.861  1.00 29.82 ? 341 GLU   A CD    1 
ATOM   2475 O OE1   . GLU   A 1 341 ? -21.295 15.231  -4.915  1.00 28.91 ? 341 GLU   A OE1   1 
ATOM   2476 O OE2   . GLU   A 1 341 ? -22.845 13.797  -5.517  1.00 30.58 ? 341 GLU   A OE2   1 
ATOM   2477 N N     . ASP   A 1 342 ? -22.603 8.862   -3.537  1.00 18.30 ? 342 ASP   A N     1 
ATOM   2478 C CA    . ASP   A 1 342 ? -23.556 7.781   -3.442  1.00 19.33 ? 342 ASP   A CA    1 
ATOM   2479 C C     . ASP   A 1 342 ? -23.331 7.009   -2.143  1.00 19.81 ? 342 ASP   A C     1 
ATOM   2480 O O     . ASP   A 1 342 ? -24.296 6.692   -1.418  1.00 19.47 ? 342 ASP   A O     1 
ATOM   2481 C CB    . ASP   A 1 342 ? -23.398 6.831   -4.605  1.00 19.56 ? 342 ASP   A CB    1 
ATOM   2482 C CG    . ASP   A 1 342 ? -23.726 7.399   -5.977  1.00 20.61 ? 342 ASP   A CG    1 
ATOM   2483 O OD1   . ASP   A 1 342 ? -24.417 8.457   -6.069  1.00 22.60 ? 342 ASP   A OD1   1 
ATOM   2484 O OD2   . ASP   A 1 342 ? -23.219 6.780   -6.944  1.00 20.41 ? 342 ASP   A OD2   1 
ATOM   2485 N N     . ALA   A 1 343 ? -22.058 6.676   -1.893  1.00 18.96 ? 343 ALA   A N     1 
ATOM   2486 C CA    . ALA   A 1 343 ? -21.672 5.913   -0.710  1.00 20.41 ? 343 ALA   A CA    1 
ATOM   2487 C C     . ALA   A 1 343 ? -22.082 6.633   0.571   1.00 19.34 ? 343 ALA   A C     1 
ATOM   2488 O O     . ALA   A 1 343 ? -22.482 5.980   1.541   1.00 19.51 ? 343 ALA   A O     1 
ATOM   2489 C CB    . ALA   A 1 343 ? -20.179 5.598   -0.711  1.00 20.96 ? 343 ALA   A CB    1 
ATOM   2490 N N     . LEU   A 1 344 ? -21.911 7.953   0.608   1.00 18.33 ? 344 LEU   A N     1 
ATOM   2491 C CA    . LEU   A 1 344 ? -22.306 8.714   1.792   1.00 18.97 ? 344 LEU   A CA    1 
ATOM   2492 C C     . LEU   A 1 344 ? -23.802 8.591   2.090   1.00 19.50 ? 344 LEU   A C     1 
ATOM   2493 O O     . LEU   A 1 344 ? -24.227 8.452   3.238   1.00 18.78 ? 344 LEU   A O     1 
ATOM   2494 C CB    . LEU   A 1 344 ? -21.945 10.182  1.556   1.00 20.15 ? 344 LEU   A CB    1 
ATOM   2495 C CG    . LEU   A 1 344 ? -22.428 11.144  2.647   1.00 20.62 ? 344 LEU   A CG    1 
ATOM   2496 C CD1   . LEU   A 1 344 ? -21.864 10.754  3.970   1.00 23.02 ? 344 LEU   A CD1   1 
ATOM   2497 C CD2   . LEU   A 1 344 ? -22.014 12.561  2.344   1.00 21.75 ? 344 LEU   A CD2   1 
ATOM   2498 N N     . VAL   A 1 345 ? -24.643 8.775   1.066   1.00 18.66 ? 345 VAL   A N     1 
ATOM   2499 C CA    . VAL   A 1 345 ? -26.078 8.670   1.269   1.00 18.83 ? 345 VAL   A CA    1 
ATOM   2500 C C     . VAL   A 1 345 ? -26.441 7.263   1.738   1.00 17.94 ? 345 VAL   A C     1 
ATOM   2501 O O     . VAL   A 1 345 ? -27.217 7.098   2.689   1.00 18.96 ? 345 VAL   A O     1 
ATOM   2502 C CB    . VAL   A 1 345 ? -26.888 9.103   0.028   1.00 19.78 ? 345 VAL   A CB    1 
ATOM   2503 C CG1   . VAL   A 1 345 ? -28.381 8.872   0.248   1.00 20.24 ? 345 VAL   A CG1   1 
ATOM   2504 C CG2   . VAL   A 1 345 ? -26.640 10.576  -0.260  1.00 22.28 ? 345 VAL   A CG2   1 
ATOM   2505 N N     . LEU   A 1 346 ? -25.837 6.243   1.119   1.00 18.73 ? 346 LEU   A N     1 
ATOM   2506 C CA    . LEU   A 1 346 ? -26.092 4.878   1.539   1.00 20.18 ? 346 LEU   A CA    1 
ATOM   2507 C C     . LEU   A 1 346 ? -25.644 4.648   2.984   1.00 20.83 ? 346 LEU   A C     1 
ATOM   2508 O O     . LEU   A 1 346 ? -26.350 3.974   3.747   1.00 20.81 ? 346 LEU   A O     1 
ATOM   2509 C CB    . LEU   A 1 346 ? -25.396 3.919   0.586   1.00 22.49 ? 346 LEU   A CB    1 
ATOM   2510 C CG    . LEU   A 1 346 ? -26.158 3.672   -0.706  1.00 23.76 ? 346 LEU   A CG    1 
ATOM   2511 C CD1   . LEU   A 1 346 ? -25.268 2.999   -1.718  1.00 23.80 ? 346 LEU   A CD1   1 
ATOM   2512 C CD2   . LEU   A 1 346 ? -27.417 2.824   -0.394  1.00 24.43 ? 346 LEU   A CD2   1 
ATOM   2513 N N     . ALA   A 1 347 ? -24.421 5.085   3.314   1.00 21.45 ? 347 ALA   A N     1 
ATOM   2514 C CA    . ALA   A 1 347 ? -23.905 4.878   4.665   1.00 20.77 ? 347 ALA   A CA    1 
ATOM   2515 C C     . ALA   A 1 347 ? -24.905 5.421   5.674   1.00 20.13 ? 347 ALA   A C     1 
ATOM   2516 O O     . ALA   A 1 347 ? -25.146 4.801   6.715   1.00 23.14 ? 347 ALA   A O     1 
ATOM   2517 C CB    . ALA   A 1 347 ? -22.550 5.536   4.848   1.00 22.06 ? 347 ALA   A CB    1 
ATOM   2518 N N     . GLU   A 1 348 ? -25.395 6.631   5.425   1.00 19.91 ? 348 GLU   A N     1 
ATOM   2519 C CA    . GLU   A 1 348 ? -26.298 7.324   6.348   1.00 20.29 ? 348 GLU   A CA    1 
ATOM   2520 C C     . GLU   A 1 348 ? -27.651 6.620   6.437   1.00 20.18 ? 348 GLU   A C     1 
ATOM   2521 O O     . GLU   A 1 348 ? -28.161 6.367   7.534   1.00 21.00 ? 348 GLU   A O     1 
ATOM   2522 C CB    . GLU   A 1 348 ? -26.380 8.790   5.927   1.00 23.02 ? 348 GLU   A CB    1 
ATOM   2523 C CG    . GLU   A 1 348 ? -25.089 9.541   6.219   1.00 25.48 ? 348 GLU   A CG    1 
ATOM   2524 C CD    . GLU   A 1 348 ? -24.971 10.027  7.646   1.00 29.35 ? 348 GLU   A CD    1 
ATOM   2525 O OE1   . GLU   A 1 348 ? -23.855 10.465  8.050   1.00 28.84 ? 348 GLU   A OE1   1 
ATOM   2526 O OE2   . GLU   A 1 348 ? -26.020 10.020  8.326   1.00 30.54 ? 348 GLU   A OE2   1 
ATOM   2527 N N     . VAL   A 1 349 ? -28.225 6.198   5.296   1.00 19.33 ? 349 VAL   A N     1 
ATOM   2528 C CA    . VAL   A 1 349 ? -29.537 5.565   5.320   1.00 20.73 ? 349 VAL   A CA    1 
ATOM   2529 C C     . VAL   A 1 349 ? -29.443 4.189   5.964   1.00 21.53 ? 349 VAL   A C     1 
ATOM   2530 O O     . VAL   A 1 349 ? -30.284 3.856   6.787   1.00 26.21 ? 349 VAL   A O     1 
ATOM   2531 C CB    . VAL   A 1 349 ? -30.100 5.468   3.890   1.00 22.47 ? 349 VAL   A CB    1 
ATOM   2532 C CG1   . VAL   A 1 349 ? -31.259 4.483   3.779   1.00 24.58 ? 349 VAL   A CG1   1 
ATOM   2533 C CG2   . VAL   A 1 349 ? -30.492 6.829   3.355   1.00 21.34 ? 349 VAL   A CG2   1 
ATOM   2534 N N     . LEU   A 1 350 ? -28.420 3.413   5.595   1.00 19.46 ? 350 LEU   A N     1 
ATOM   2535 C CA    . LEU   A 1 350 ? -28.246 2.073   6.121   1.00 21.07 ? 350 LEU   A CA    1 
ATOM   2536 C C     . LEU   A 1 350 ? -28.003 2.119   7.634   1.00 21.96 ? 350 LEU   A C     1 
ATOM   2537 O O     . LEU   A 1 350 ? -28.449 1.222   8.348   1.00 24.15 ? 350 LEU   A O     1 
ATOM   2538 C CB    . LEU   A 1 350 ? -27.141 1.354   5.357   1.00 22.40 ? 350 LEU   A CB    1 
ATOM   2539 C CG    . LEU   A 1 350 ? -27.460 1.121   3.873   1.00 24.99 ? 350 LEU   A CG    1 
ATOM   2540 C CD1   . LEU   A 1 350 ? -26.259 0.552   3.168   1.00 25.59 ? 350 LEU   A CD1   1 
ATOM   2541 C CD2   . LEU   A 1 350 ? -28.679 0.225   3.689   1.00 26.64 ? 350 LEU   A CD2   1 
ATOM   2542 N N     . ALA   A 1 351 ? -27.352 3.165   8.129   1.00 23.71 ? 351 ALA   A N     1 
ATOM   2543 C CA    . ALA   A 1 351 ? -27.130 3.276   9.573   1.00 22.13 ? 351 ALA   A CA    1 
ATOM   2544 C C     . ALA   A 1 351 ? -28.439 3.434   10.341  1.00 24.96 ? 351 ALA   A C     1 
ATOM   2545 O O     . ALA   A 1 351 ? -28.547 2.955   11.482  1.00 23.73 ? 351 ALA   A O     1 
ATOM   2546 C CB    . ALA   A 1 351 ? -26.217 4.427   9.870   1.00 22.39 ? 351 ALA   A CB    1 
ATOM   2547 N N     . VAL   A 1 352 ? -29.415 4.140   9.747   1.00 24.75 ? 352 VAL   A N     1 
ATOM   2548 C CA    . VAL   A 1 352 ? -30.729 4.286   10.363  1.00 28.12 ? 352 VAL   A CA    1 
ATOM   2549 C C     . VAL   A 1 352 ? -31.387 2.911   10.447  1.00 27.22 ? 352 VAL   A C     1 
ATOM   2550 O O     . VAL   A 1 352 ? -31.931 2.550   11.482  1.00 30.78 ? 352 VAL   A O     1 
ATOM   2551 C CB    . VAL   A 1 352 ? -31.606 5.329   9.633   1.00 28.87 ? 352 VAL   A CB    1 
ATOM   2552 C CG1   . VAL   A 1 352 ? -33.030 5.426   10.188  1.00 30.13 ? 352 VAL   A CG1   1 
ATOM   2553 C CG2   . VAL   A 1 352 ? -30.956 6.692   9.713   1.00 28.97 ? 352 VAL   A CG2   1 
ATOM   2554 N N     . LEU   A 1 353 ? -31.307 2.118   9.378   1.00 27.24 ? 353 LEU   A N     1 
ATOM   2555 C CA    . LEU   A 1 353 ? -31.908 0.795   9.359   1.00 28.13 ? 353 LEU   A CA    1 
ATOM   2556 C C     . LEU   A 1 353 ? -31.215 -0.133  10.344  1.00 30.95 ? 353 LEU   A C     1 
ATOM   2557 O O     . LEU   A 1 353 ? -31.867 -0.960  10.989  1.00 33.50 ? 353 LEU   A O     1 
ATOM   2558 C CB    . LEU   A 1 353 ? -31.858 0.183   7.971   1.00 28.82 ? 353 LEU   A CB    1 
ATOM   2559 C CG    . LEU   A 1 353 ? -33.074 0.430   7.079   1.00 33.09 ? 353 LEU   A CG    1 
ATOM   2560 C CD1   . LEU   A 1 353 ? -33.630 1.848   7.144   1.00 38.40 ? 353 LEU   A CD1   1 
ATOM   2561 C CD2   . LEU   A 1 353 ? -32.638 0.047   5.692   1.00 31.88 ? 353 LEU   A CD2   1 
ATOM   2562 N N     . ALA   A 1 354 ? -29.896 -0.019  10.431  1.00 27.63 ? 354 ALA   A N     1 
ATOM   2563 C CA    . ALA   A 1 354 ? -29.136 -0.902  11.296  1.00 30.65 ? 354 ALA   A CA    1 
ATOM   2564 C C     . ALA   A 1 354 ? -29.506 -0.690  12.766  1.00 33.45 ? 354 ALA   A C     1 
ATOM   2565 O O     . ALA   A 1 354 ? -29.218 -1.556  13.593  1.00 28.49 ? 354 ALA   A O     1 
ATOM   2566 C CB    . ALA   A 1 354 ? -27.682 -0.653  11.108  1.00 29.79 ? 354 ALA   A CB    1 
ATOM   2567 N N     . GLU   A 1 355 ? -30.019 0.503   13.088  1.00 32.93 ? 355 GLU   A N     1 
ATOM   2568 C CA    . GLU   A 1 355 ? -30.359 0.875   14.462  1.00 38.70 ? 355 GLU   A CA    1 
ATOM   2569 C C     . GLU   A 1 355 ? -31.653 0.195   14.903  1.00 45.81 ? 355 GLU   A C     1 
ATOM   2570 O O     . GLU   A 1 355 ? -31.884 0.045   16.103  1.00 48.05 ? 355 GLU   A O     1 
ATOM   2571 C CB    . GLU   A 1 355 ? -30.502 2.391   14.634  1.00 38.16 ? 355 GLU   A CB    1 
ATOM   2572 N N     . ALA   A 1 356 ? -32.500 -0.201  13.944  1.00 46.71 ? 356 ALA   A N     1 
ATOM   2573 C CA    . ALA   A 1 356 ? -33.729 -0.919  14.247  1.00 48.96 ? 356 ALA   A CA    1 
ATOM   2574 C C     . ALA   A 1 356 ? -33.404 -2.372  14.586  1.00 51.70 ? 356 ALA   A C     1 
ATOM   2575 O O     . ALA   A 1 356 ? -32.425 -2.910  14.085  1.00 59.20 ? 356 ALA   A O     1 
ATOM   2576 C CB    . ALA   A 1 356 ? -34.674 -0.817  13.067  1.00 48.56 ? 356 ALA   A CB    1 
ATOM   2577 N N     . PRO   A 1 357 ? -34.214 -3.072  15.421  1.00 65.52 ? 357 PRO   A N     1 
ATOM   2578 C CA    . PRO   A 1 357 ? -33.916 -4.460  15.803  1.00 59.65 ? 357 PRO   A CA    1 
ATOM   2579 C C     . PRO   A 1 357 ? -34.178 -5.473  14.692  1.00 55.69 ? 357 PRO   A C     1 
ATOM   2580 O O     . PRO   A 1 357 ? -33.439 -6.451  14.537  1.00 50.36 ? 357 PRO   A O     1 
ATOM   2581 C CB    . PRO   A 1 357 ? -34.791 -4.748  17.041  1.00 63.59 ? 357 PRO   A CB    1 
ATOM   2582 C CG    . PRO   A 1 357 ? -35.684 -3.520  17.214  1.00 65.93 ? 357 PRO   A CG    1 
ATOM   2583 C CD    . PRO   A 1 357 ? -35.440 -2.563  16.055  1.00 60.35 ? 357 PRO   A CD    1 
ATOM   2584 N N     . ASN   A 1 358 ? -35.261 -5.236  13.945  1.00 50.28 ? 358 ASN   A N     1 
ATOM   2585 C CA    . ASN   A 1 358 ? -35.603 -6.064  12.807  1.00 48.98 ? 358 ASN   A CA    1 
ATOM   2586 C C     . ASN   A 1 358 ? -35.933 -5.121  11.655  1.00 45.21 ? 358 ASN   A C     1 
ATOM   2587 O O     . ASN   A 1 358 ? -36.582 -4.095  11.839  1.00 49.37 ? 358 ASN   A O     1 
ATOM   2588 C CB    . ASN   A 1 358 ? -36.728 -7.045  13.131  1.00 52.18 ? 358 ASN   A CB    1 
ATOM   2589 N N     . VAL   A 1 359 ? -35.435 -5.461  10.470  1.00 37.53 ? 359 VAL   A N     1 
ATOM   2590 C CA    . VAL   A 1 359 ? -35.722 -4.672  9.292   1.00 34.35 ? 359 VAL   A CA    1 
ATOM   2591 C C     . VAL   A 1 359 ? -36.415 -5.576  8.283   1.00 30.68 ? 359 VAL   A C     1 
ATOM   2592 O O     . VAL   A 1 359 ? -35.830 -6.549  7.831   1.00 32.55 ? 359 VAL   A O     1 
ATOM   2593 C CB    . VAL   A 1 359 ? -34.423 -4.074  8.721   1.00 34.45 ? 359 VAL   A CB    1 
ATOM   2594 C CG1   . VAL   A 1 359 ? -34.669 -3.422  7.363   1.00 35.96 ? 359 VAL   A CG1   1 
ATOM   2595 C CG2   . VAL   A 1 359 ? -33.766 -3.090  9.685   1.00 35.27 ? 359 VAL   A CG2   1 
ATOM   2596 N N     . SER   A 1 360 ? -37.643 -5.222  7.902   1.00 32.57 ? 360 SER   A N     1 
ATOM   2597 C CA    . SER   A 1 360 ? -38.404 -5.984  6.921   1.00 30.12 ? 360 SER   A CA    1 
ATOM   2598 C C     . SER   A 1 360 ? -37.864 -5.738  5.508   1.00 32.04 ? 360 SER   A C     1 
ATOM   2599 O O     . SER   A 1 360 ? -37.196 -4.725  5.272   1.00 29.81 ? 360 SER   A O     1 
ATOM   2600 C CB    . SER   A 1 360 ? -39.854 -5.615  6.991   1.00 32.61 ? 360 SER   A CB    1 
ATOM   2601 O OG    . SER   A 1 360 ? -40.075 -4.311  6.466   1.00 31.33 ? 360 SER   A OG    1 
ATOM   2602 N N     . GLY   A 1 361 ? -38.197 -6.653  4.586   1.00 27.94 ? 361 GLY   A N     1 
ATOM   2603 C CA    . GLY   A 1 361 ? -37.979 -6.462  3.151   1.00 30.83 ? 361 GLY   A CA    1 
ATOM   2604 C C     . GLY   A 1 361 ? -38.578 -5.148  2.636   1.00 33.38 ? 361 GLY   A C     1 
ATOM   2605 O O     . GLY   A 1 361 ? -37.970 -4.428  1.844   1.00 27.47 ? 361 GLY   A O     1 
ATOM   2606 N N     . ILE   A 1 362 ? -39.802 -4.857  3.077   1.00 31.19 ? 362 ILE   A N     1 
ATOM   2607 C CA    . ILE   A 1 362 ? -40.512 -3.629  2.753   1.00 32.70 ? 362 ILE   A CA    1 
ATOM   2608 C C     . ILE   A 1 362 ? -39.684 -2.406  3.158   1.00 30.14 ? 362 ILE   A C     1 
ATOM   2609 O O     . ILE   A 1 362 ? -39.568 -1.422  2.410   1.00 26.56 ? 362 ILE   A O     1 
ATOM   2610 C CB    . ILE   A 1 362 ? -41.887 -3.665  3.454   1.00 36.91 ? 362 ILE   A CB    1 
ATOM   2611 C CG1   . ILE   A 1 362 ? -42.867 -4.536  2.676   1.00 41.60 ? 362 ILE   A CG1   1 
ATOM   2612 C CG2   . ILE   A 1 362 ? -42.467 -2.268  3.700   1.00 38.66 ? 362 ILE   A CG2   1 
ATOM   2613 C CD1   . ILE   A 1 362 ? -42.532 -6.019  2.669   1.00 47.22 ? 362 ILE   A CD1   1 
ATOM   2614 N N     . VAL   A 1 363 ? -39.181 -2.431  4.393   1.00 26.83 ? 363 VAL   A N     1 
ATOM   2615 C CA    . VAL   A 1 363 ? -38.494 -1.272  4.928   1.00 27.45 ? 363 VAL   A CA    1 
ATOM   2616 C C     . VAL   A 1 363 ? -37.125 -1.120  4.264   1.00 25.20 ? 363 VAL   A C     1 
ATOM   2617 O O     . VAL   A 1 363 ? -36.721 -0.001  3.952   1.00 25.46 ? 363 VAL   A O     1 
ATOM   2618 C CB    . VAL   A 1 363 ? -38.415 -1.322  6.464   1.00 27.28 ? 363 VAL   A CB    1 
ATOM   2619 C CG1   . VAL   A 1 363 ? -37.318 -0.425  7.002   1.00 27.55 ? 363 VAL   A CG1   1 
ATOM   2620 C CG2   . VAL   A 1 363 ? -39.785 -0.961  7.059   1.00 29.00 ? 363 VAL   A CG2   1 
ATOM   2621 N N     . ALA   A 1 364 ? -36.447 -2.243  4.024   1.00 25.86 ? 364 ALA   A N     1 
ATOM   2622 C CA    . ALA   A 1 364 ? -35.177 -2.255  3.307   1.00 26.59 ? 364 ALA   A CA    1 
ATOM   2623 C C     . ALA   A 1 364 ? -35.381 -1.656  1.910   1.00 25.21 ? 364 ALA   A C     1 
ATOM   2624 O O     . ALA   A 1 364 ? -34.596 -0.830  1.468   1.00 23.87 ? 364 ALA   A O     1 
ATOM   2625 C CB    . ALA   A 1 364 ? -34.609 -3.661  3.236   1.00 24.98 ? 364 ALA   A CB    1 
ATOM   2626 N N     . SER   A 1 365 ? -36.443 -2.076  1.228   1.00 24.57 ? 365 SER   A N     1 
ATOM   2627 C CA    . SER   A 1 365 ? -36.728 -1.593  -0.117  1.00 24.55 ? 365 SER   A CA    1 
ATOM   2628 C C     . SER   A 1 365 ? -37.052 -0.103  -0.144  1.00 27.56 ? 365 SER   A C     1 
ATOM   2629 O O     . SER   A 1 365 ? -36.589 0.617   -1.030  1.00 25.49 ? 365 SER   A O     1 
ATOM   2630 C CB    . SER   A 1 365 ? -37.824 -2.406  -0.747  1.00 26.38 ? 365 SER   A CB    1 
ATOM   2631 O OG    . SER   A 1 365 ? -37.437 -3.767  -0.673  1.00 32.18 ? 365 SER   A OG    1 
ATOM   2632 N N     . GLU   A 1 366 ? -37.807 0.364   0.851   1.00 26.31 ? 366 GLU   A N     1 
ATOM   2633 C CA    . GLU   A 1 366 ? -38.164 1.771   0.934   1.00 29.07 ? 366 GLU   A CA    1 
ATOM   2634 C C     . GLU   A 1 366 ? -36.896 2.606   1.138   1.00 24.55 ? 366 GLU   A C     1 
ATOM   2635 O O     . GLU   A 1 366 ? -36.768 3.683   0.570   1.00 24.04 ? 366 GLU   A O     1 
ATOM   2636 C CB    . GLU   A 1 366 ? -39.157 2.042   2.073   1.00 26.46 ? 366 GLU   A CB    1 
ATOM   2637 C CG    . GLU   A 1 366 ? -40.588 1.595   1.808   1.00 33.12 ? 366 GLU   A CG    1 
ATOM   2638 C CD    . GLU   A 1 366 ? -41.388 1.355   3.098   1.00 37.61 ? 366 GLU   A CD    1 
ATOM   2639 O OE1   . GLU   A 1 366 ? -40.788 1.440   4.201   1.00 39.32 ? 366 GLU   A OE1   1 
ATOM   2640 O OE2   . GLU   A 1 366 ? -42.601 1.037   3.010   1.00 41.61 ? 366 GLU   A OE2   1 
ATOM   2641 N N     . ALA   A 1 367 ? -35.969 2.127   1.967   1.00 23.45 ? 367 ALA   A N     1 
ATOM   2642 C CA    . ALA   A 1 367 ? -34.739 2.838   2.250   1.00 22.54 ? 367 ALA   A CA    1 
ATOM   2643 C C     . ALA   A 1 367 ? -33.907 3.021   0.978   1.00 23.74 ? 367 ALA   A C     1 
ATOM   2644 O O     . ALA   A 1 367 ? -33.396 4.093   0.710   1.00 20.92 ? 367 ALA   A O     1 
ATOM   2645 C CB    . ALA   A 1 367 ? -33.937 2.071   3.257   1.00 26.53 ? 367 ALA   A CB    1 
ATOM   2646 N N     . LEU   A 1 368 ? -33.738 1.939   0.234   1.00 19.85 ? 368 LEU   A N     1 
ATOM   2647 C CA    . LEU   A 1 368 ? -32.992 2.036   -1.008  1.00 21.11 ? 368 LEU   A CA    1 
ATOM   2648 C C     . LEU   A 1 368 ? -33.676 2.968   -2.003  1.00 22.35 ? 368 LEU   A C     1 
ATOM   2649 O O     . LEU   A 1 368 ? -32.971 3.696   -2.724  1.00 23.11 ? 368 LEU   A O     1 
ATOM   2650 C CB    . LEU   A 1 368 ? -32.778 0.633   -1.565  1.00 20.61 ? 368 LEU   A CB    1 
ATOM   2651 C CG    . LEU   A 1 368 ? -31.923 -0.278  -0.682  1.00 22.12 ? 368 LEU   A CG    1 
ATOM   2652 C CD1   . LEU   A 1 368 ? -31.574 -1.557  -1.432  1.00 20.23 ? 368 LEU   A CD1   1 
ATOM   2653 C CD2   . LEU   A 1 368 ? -30.657 0.382   -0.119  1.00 23.91 ? 368 LEU   A CD2   1 
ATOM   2654 N N     . ALA   A 1 369 ? -35.015 2.917   -2.069  1.00 21.55 ? 369 ALA   A N     1 
ATOM   2655 C CA    . ALA   A 1 369 ? -35.772 3.825   -2.920  1.00 21.05 ? 369 ALA   A CA    1 
ATOM   2656 C C     . ALA   A 1 369 ? -35.486 5.282   -2.563  1.00 21.12 ? 369 ALA   A C     1 
ATOM   2657 O O     . ALA   A 1 369 ? -35.422 6.125   -3.463  1.00 20.08 ? 369 ALA   A O     1 
ATOM   2658 C CB    . ALA   A 1 369 ? -37.259 3.505   -2.875  1.00 23.91 ? 369 ALA   A CB    1 
ATOM   2659 N N     . VAL   A 1 370 ? -35.364 5.594   -1.257  1.00 19.05 ? 370 VAL   A N     1 
ATOM   2660 C CA    . VAL   A 1 370 ? -35.026 6.957   -0.856  1.00 21.80 ? 370 VAL   A CA    1 
ATOM   2661 C C     . VAL   A 1 370 ? -33.636 7.373   -1.391  1.00 19.87 ? 370 VAL   A C     1 
ATOM   2662 O O     . VAL   A 1 370 ? -33.474 8.464   -1.933  1.00 20.59 ? 370 VAL   A O     1 
ATOM   2663 C CB    . VAL   A 1 370 ? -35.130 7.076   0.680   1.00 24.09 ? 370 VAL   A CB    1 
ATOM   2664 C CG1   . VAL   A 1 370 ? -34.507 8.366   1.170   1.00 25.08 ? 370 VAL   A CG1   1 
ATOM   2665 C CG2   . VAL   A 1 370 ? -36.576 6.950   1.166   1.00 23.00 ? 370 VAL   A CG2   1 
ATOM   2666 N N     . TYR   A 1 371 ? -32.641 6.492   -1.250  1.00 19.82 ? 371 TYR   A N     1 
ATOM   2667 C CA    . TYR   A 1 371 ? -31.294 6.698   -1.760  1.00 19.46 ? 371 TYR   A CA    1 
ATOM   2668 C C     . TYR   A 1 371 ? -31.399 7.033   -3.250  1.00 20.37 ? 371 TYR   A C     1 
ATOM   2669 O O     . TYR   A 1 371 ? -30.848 8.027   -3.705  1.00 21.71 ? 371 TYR   A O     1 
ATOM   2670 C CB    . TYR   A 1 371 ? -30.442 5.433   -1.537  1.00 22.49 ? 371 TYR   A CB    1 
ATOM   2671 C CG    . TYR   A 1 371 ? -29.334 5.268   -2.561  1.00 20.10 ? 371 TYR   A CG    1 
ATOM   2672 C CD1   . TYR   A 1 371 ? -28.209 6.086   -2.528  1.00 20.71 ? 371 TYR   A CD1   1 
ATOM   2673 C CD2   . TYR   A 1 371 ? -29.377 4.258   -3.525  1.00 19.57 ? 371 TYR   A CD2   1 
ATOM   2674 C CE1   . TYR   A 1 371 ? -27.156 5.923   -3.421  1.00 22.14 ? 371 TYR   A CE1   1 
ATOM   2675 C CE2   . TYR   A 1 371 ? -28.370 4.133   -4.466  1.00 19.89 ? 371 TYR   A CE2   1 
ATOM   2676 C CZ    . TYR   A 1 371 ? -27.250 4.959   -4.414  1.00 19.81 ? 371 TYR   A CZ    1 
ATOM   2677 O OH    . TYR   A 1 371 ? -26.218 4.860   -5.313  1.00 19.90 ? 371 TYR   A OH    1 
ATOM   2678 N N     . SER   A 1 372 ? -32.124 6.206   -3.996  1.00 19.74 ? 372 SER   A N     1 
ATOM   2679 C CA    . SER   A 1 372 ? -32.253 6.445   -5.442  1.00 19.19 ? 372 SER   A CA    1 
ATOM   2680 C C     . SER   A 1 372 ? -32.916 7.788   -5.737  1.00 19.76 ? 372 SER   A C     1 
ATOM   2681 O O     . SER   A 1 372 ? -32.434 8.525   -6.581  1.00 22.63 ? 372 SER   A O     1 
ATOM   2682 C CB    . SER   A 1 372 ? -32.963 5.345   -6.148  1.00 19.28 ? 372 SER   A CB    1 
ATOM   2683 O OG    . SER   A 1 372 ? -32.999 5.591   -7.561  1.00 21.37 ? 372 SER   A OG    1 
ATOM   2684 N N     . GLU   A 1 373 ? -33.991 8.140   -5.021  1.00 21.32 ? 373 GLU   A N     1 
ATOM   2685 C CA    . GLU   A 1 373 ? -34.673 9.409   -5.264  1.00 23.55 ? 373 GLU   A CA    1 
ATOM   2686 C C     . GLU   A 1 373 ? -33.737 10.600  -5.037  1.00 21.17 ? 373 GLU   A C     1 
ATOM   2687 O O     . GLU   A 1 373 ? -33.768 11.621  -5.755  1.00 21.24 ? 373 GLU   A O     1 
ATOM   2688 C CB    . GLU   A 1 373 ? -35.932 9.477   -4.395  1.00 28.11 ? 373 GLU   A CB    1 
ATOM   2689 C CG    . GLU   A 1 373 ? -36.815 10.683  -4.720  1.00 35.04 ? 373 GLU   A CG    1 
ATOM   2690 C CD    . GLU   A 1 373 ? -37.988 10.803  -3.762  1.00 39.93 ? 373 GLU   A CD    1 
ATOM   2691 O OE1   . GLU   A 1 373 ? -38.115 11.856  -3.087  1.00 47.05 ? 373 GLU   A OE1   1 
ATOM   2692 O OE2   . GLU   A 1 373 ? -38.726 9.800   -3.672  1.00 40.39 ? 373 GLU   A OE2   1 
ATOM   2693 N N     . VAL   A 1 374 ? -32.878 10.490  -4.017  1.00 20.87 ? 374 VAL   A N     1 
ATOM   2694 C CA    . VAL   A 1 374 ? -31.942 11.551  -3.704  1.00 22.29 ? 374 VAL   A CA    1 
ATOM   2695 C C     . VAL   A 1 374 ? -30.840 11.668  -4.757  1.00 20.67 ? 374 VAL   A C     1 
ATOM   2696 O O     . VAL   A 1 374 ? -30.426 12.774  -5.047  1.00 21.39 ? 374 VAL   A O     1 
ATOM   2697 C CB    . VAL   A 1 374 ? -31.344 11.308  -2.301  1.00 25.06 ? 374 VAL   A CB    1 
ATOM   2698 C CG1   . VAL   A 1 374 ? -30.161 12.222  -2.033  1.00 25.80 ? 374 VAL   A CG1   1 
ATOM   2699 C CG2   . VAL   A 1 374 ? -32.414 11.466  -1.225  1.00 27.61 ? 374 VAL   A CG2   1 
ATOM   2700 N N     . ARG   A 1 375 ? -30.382 10.553  -5.338  1.00 20.66 ? 375 ARG   A N     1 
ATOM   2701 C CA    . ARG   A 1 375 ? -29.177 10.573  -6.171  1.00 20.52 ? 375 ARG   A CA    1 
ATOM   2702 C C     . ARG   A 1 375 ? -29.466 10.504  -7.678  1.00 20.11 ? 375 ARG   A C     1 
ATOM   2703 O O     . ARG   A 1 375 ? -28.616 10.856  -8.489  1.00 21.10 ? 375 ARG   A O     1 
ATOM   2704 C CB    . ARG   A 1 375 ? -28.333 9.352   -5.795  1.00 22.13 ? 375 ARG   A CB    1 
ATOM   2705 C CG    . ARG   A 1 375 ? -27.750 9.397   -4.390  1.00 22.46 ? 375 ARG   A CG    1 
ATOM   2706 C CD    . ARG   A 1 375 ? -26.872 10.584  -4.212  1.00 24.56 ? 375 ARG   A CD    1 
ATOM   2707 N NE    . ARG   A 1 375 ? -25.757 10.527  -5.158  1.00 25.10 ? 375 ARG   A NE    1 
ATOM   2708 C CZ    . ARG   A 1 375 ? -25.105 11.566  -5.620  1.00 23.87 ? 375 ARG   A CZ    1 
ATOM   2709 N NH1   . ARG   A 1 375 ? -25.482 12.786  -5.306  1.00 27.36 ? 375 ARG   A NH1   1 
ATOM   2710 N NH2   . ARG   A 1 375 ? -24.082 11.372  -6.439  1.00 31.42 ? 375 ARG   A NH2   1 
ATOM   2711 N N     . TYR   A 1 376 ? -30.667 10.083  -8.072  1.00 20.92 ? 376 TYR   A N     1 
ATOM   2712 C CA    . TYR   A 1 376 ? -30.893 9.638   -9.447  1.00 20.28 ? 376 TYR   A CA    1 
ATOM   2713 C C     . TYR   A 1 376 ? -30.725 10.791  -10.427 1.00 19.89 ? 376 TYR   A C     1 
ATOM   2714 O O     . TYR   A 1 376 ? -29.903 10.702  -11.358 1.00 19.44 ? 376 TYR   A O     1 
ATOM   2715 C CB    . TYR   A 1 376 ? -32.270 8.983   -9.618  1.00 20.26 ? 376 TYR   A CB    1 
ATOM   2716 C CG    . TYR   A 1 376 ? -32.439 8.477   -11.039 1.00 19.27 ? 376 TYR   A CG    1 
ATOM   2717 C CD1   . TYR   A 1 376 ? -31.847 7.274   -11.434 1.00 17.68 ? 376 TYR   A CD1   1 
ATOM   2718 C CD2   . TYR   A 1 376 ? -33.164 9.200   -11.978 1.00 21.01 ? 376 TYR   A CD2   1 
ATOM   2719 C CE1   . TYR   A 1 376 ? -32.012 6.799   -12.729 1.00 22.11 ? 376 TYR   A CE1   1 
ATOM   2720 C CE2   . TYR   A 1 376 ? -33.315 8.725   -13.280 1.00 22.19 ? 376 TYR   A CE2   1 
ATOM   2721 C CZ    . TYR   A 1 376 ? -32.714 7.543   -13.658 1.00 19.93 ? 376 TYR   A CZ    1 
ATOM   2722 O OH    . TYR   A 1 376 ? -32.836 7.060   -14.924 1.00 21.08 ? 376 TYR   A OH    1 
ATOM   2723 N N     . GLU   A 1 377 ? -31.523 11.850  -10.289 1.00 19.58 ? 377 GLU   A N     1 
ATOM   2724 C CA    . GLU   A 1 377 ? -31.476 12.875  -11.346 1.00 21.44 ? 377 GLU   A CA    1 
ATOM   2725 C C     . GLU   A 1 377 ? -30.154 13.645  -11.332 1.00 19.87 ? 377 GLU   A C     1 
ATOM   2726 O O     . GLU   A 1 377 ? -29.652 14.056  -12.392 1.00 18.86 ? 377 GLU   A O     1 
ATOM   2727 C CB    . GLU   A 1 377 ? -32.635 13.869  -11.309 1.00 23.41 ? 377 GLU   A CB    1 
ATOM   2728 C CG    . GLU   A 1 377 ? -34.017 13.276  -11.584 1.00 25.61 ? 377 GLU   A CG    1 
ATOM   2729 C CD    . GLU   A 1 377 ? -34.248 12.678  -12.953 1.00 26.03 ? 377 GLU   A CD    1 
ATOM   2730 O OE1   . GLU   A 1 377 ? -33.419 12.902  -13.838 1.00 28.59 ? 377 GLU   A OE1   1 
ATOM   2731 O OE2   . GLU   A 1 377 ? -35.251 11.972  -13.122 1.00 29.59 ? 377 GLU   A OE2   1 
ATOM   2732 N N     . ARG   A 1 378 ? -29.577 13.906  -10.151 1.00 19.45 ? 378 ARG   A N     1 
ATOM   2733 C CA    . ARG   A 1 378 ? -28.284 14.581  -10.061 1.00 21.15 ? 378 ARG   A CA    1 
ATOM   2734 C C     . ARG   A 1 378 ? -27.190 13.758  -10.757 1.00 20.45 ? 378 ARG   A C     1 
ATOM   2735 O O     . ARG   A 1 378 ? -26.350 14.290  -11.474 1.00 20.16 ? 378 ARG   A O     1 
ATOM   2736 C CB    . ARG   A 1 378 ? -27.939 14.898  -8.594  1.00 23.41 ? 378 ARG   A CB    1 
ATOM   2737 C CG    . ARG   A 1 378 ? -26.454 15.159  -8.342  1.00 30.90 ? 378 ARG   A CG    1 
ATOM   2738 C CD    . ARG   A 1 378 ? -26.099 15.744  -6.954  1.00 34.39 ? 378 ARG   A CD    1 
ATOM   2739 N NE    . ARG   A 1 378 ? -24.657 15.883  -6.672  1.00 36.50 ? 378 ARG   A NE    1 
ATOM   2740 C CZ    . ARG   A 1 378 ? -23.878 16.885  -7.140  1.00 41.72 ? 378 ARG   A CZ    1 
ATOM   2741 N NH1   . ARG   A 1 378 ? -24.418 17.890  -7.831  1.00 37.66 ? 378 ARG   A NH1   1 
ATOM   2742 N NH2   . ARG   A 1 378 ? -22.579 16.902  -6.878  1.00 35.47 ? 378 ARG   A NH2   1 
ATOM   2743 N N     . SER   A 1 379 ? -27.276 12.425  -10.633 1.00 20.85 ? 379 SER   A N     1 
ATOM   2744 C CA    . SER   A 1 379 ? -26.376 11.501  -11.286 1.00 18.19 ? 379 SER   A CA    1 
ATOM   2745 C C     . SER   A 1 379 ? -26.552 11.519  -12.790 1.00 19.27 ? 379 SER   A C     1 
ATOM   2746 O O     . SER   A 1 379 ? -25.554 11.494  -13.515 1.00 19.82 ? 379 SER   A O     1 
ATOM   2747 C CB    . SER   A 1 379 ? -26.576 10.129  -10.774 1.00 21.46 ? 379 SER   A CB    1 
ATOM   2748 O OG    . SER   A 1 379 ? -26.160 10.069  -9.408  1.00 21.64 ? 379 SER   A OG    1 
ATOM   2749 N N     . GLN   A 1 380 ? -27.812 11.535  -13.236 1.00 18.00 ? 380 GLN   A N     1 
ATOM   2750 C CA    . GLN   A 1 380 ? -28.078 11.551  -14.672 1.00 19.16 ? 380 GLN   A CA    1 
ATOM   2751 C C     . GLN   A 1 380 ? -27.551 12.854  -15.272 1.00 18.97 ? 380 GLN   A C     1 
ATOM   2752 O O     . GLN   A 1 380 ? -27.042 12.848  -16.384 1.00 18.57 ? 380 GLN   A O     1 
ATOM   2753 C CB    . GLN   A 1 380 ? -29.560 11.370  -14.978 1.00 18.99 ? 380 GLN   A CB    1 
ATOM   2754 C CG    . GLN   A 1 380 ? -30.130 10.015  -14.551 1.00 19.77 ? 380 GLN   A CG    1 
ATOM   2755 C CD    . GLN   A 1 380 ? -29.347 8.855   -15.110 1.00 20.66 ? 380 GLN   A CD    1 
ATOM   2756 O OE1   . GLN   A 1 380 ? -28.827 8.898   -16.224 1.00 23.34 ? 380 GLN   A OE1   1 
ATOM   2757 N NE2   . GLN   A 1 380 ? -29.270 7.780   -14.359 1.00 20.32 ? 380 GLN   A NE2   1 
ATOM   2758 N N     . TRP   A 1 381 ? -27.729 13.946  -14.549 1.00 19.10 ? 381 TRP   A N     1 
ATOM   2759 C CA    . TRP   A 1 381 ? -27.224 15.243  -14.986 1.00 21.16 ? 381 TRP   A CA    1 
ATOM   2760 C C     . TRP   A 1 381 ? -25.698 15.261  -15.090 1.00 19.93 ? 381 TRP   A C     1 
ATOM   2761 O O     . TRP   A 1 381 ? -25.171 15.806  -16.058 1.00 21.14 ? 381 TRP   A O     1 
ATOM   2762 C CB    . TRP   A 1 381 ? -27.715 16.378  -14.082 1.00 21.54 ? 381 TRP   A CB    1 
ATOM   2763 C CG    . TRP   A 1 381 ? -27.257 17.735  -14.578 1.00 24.17 ? 381 TRP   A CG    1 
ATOM   2764 C CD1   . TRP   A 1 381 ? -26.633 18.694  -13.825 1.00 26.09 ? 381 TRP   A CD1   1 
ATOM   2765 C CD2   . TRP   A 1 381 ? -27.410 18.313  -15.904 1.00 23.97 ? 381 TRP   A CD2   1 
ATOM   2766 N NE1   . TRP   A 1 381 ? -26.370 19.810  -14.593 1.00 27.15 ? 381 TRP   A NE1   1 
ATOM   2767 C CE2   . TRP   A 1 381 ? -26.845 19.613  -15.862 1.00 25.74 ? 381 TRP   A CE2   1 
ATOM   2768 C CE3   . TRP   A 1 381 ? -27.935 17.871  -17.121 1.00 27.05 ? 381 TRP   A CE3   1 
ATOM   2769 C CZ2   . TRP   A 1 381 ? -26.805 20.460  -16.974 1.00 29.78 ? 381 TRP   A CZ2   1 
ATOM   2770 C CZ3   . TRP   A 1 381 ? -27.897 18.708  -18.227 1.00 28.38 ? 381 TRP   A CZ3   1 
ATOM   2771 C CH2   . TRP   A 1 381 ? -27.320 19.983  -18.155 1.00 28.72 ? 381 TRP   A CH2   1 
ATOM   2772 N N     . LEU   A 1 382 ? -24.976 14.621  -14.157 1.00 19.82 ? 382 LEU   A N     1 
ATOM   2773 C CA    . LEU   A 1 382 ? -23.524 14.483  -14.241 1.00 19.80 ? 382 LEU   A CA    1 
ATOM   2774 C C     . LEU   A 1 382 ? -23.122 13.850  -15.575 1.00 20.63 ? 382 LEU   A C     1 
ATOM   2775 O O     . LEU   A 1 382 ? -22.268 14.379  -16.293 1.00 17.82 ? 382 LEU   A O     1 
ATOM   2776 C CB    . LEU   A 1 382 ? -22.962 13.659  -13.080 1.00 21.47 ? 382 LEU   A CB    1 
ATOM   2777 C CG    . LEU   A 1 382 ? -21.514 13.183  -13.267 1.00 22.60 ? 382 LEU   A CG    1 
ATOM   2778 C CD1   . LEU   A 1 382 ? -20.509 14.333  -13.251 1.00 23.66 ? 382 LEU   A CD1   1 
ATOM   2779 C CD2   . LEU   A 1 382 ? -21.218 12.135  -12.233 1.00 27.05 ? 382 LEU   A CD2   1 
ATOM   2780 N N     . VAL   A 1 383 ? -23.775 12.735  -15.929 1.00 17.95 ? 383 VAL   A N     1 
ATOM   2781 C CA    . VAL   A 1 383 ? -23.412 12.017  -17.143 1.00 17.87 ? 383 VAL   A CA    1 
ATOM   2782 C C     . VAL   A 1 383 ? -23.624 12.925  -18.359 1.00 18.91 ? 383 VAL   A C     1 
ATOM   2783 O O     . VAL   A 1 383 ? -22.775 12.990  -19.255 1.00 19.12 ? 383 VAL   A O     1 
ATOM   2784 C CB    . VAL   A 1 383 ? -24.202 10.712  -17.259 1.00 19.46 ? 383 VAL   A CB    1 
ATOM   2785 C CG1   . VAL   A 1 383 ? -23.912 10.026  -18.597 1.00 19.88 ? 383 VAL   A CG1   1 
ATOM   2786 C CG2   . VAL   A 1 383 ? -23.901 9.781   -16.060 1.00 19.43 ? 383 VAL   A CG2   1 
ATOM   2787 N N     . ARG   A 1 384 ? -24.751 13.615  -18.400 1.00 19.15 ? 384 ARG   A N     1 
ATOM   2788 C CA    . ARG   A 1 384 ? -25.103 14.405  -19.585 1.00 20.72 ? 384 ARG   A CA    1 
ATOM   2789 C C     . ARG   A 1 384 ? -24.236 15.658  -19.624 1.00 20.06 ? 384 ARG   A C     1 
ATOM   2790 O O     . ARG   A 1 384 ? -23.757 16.046  -20.687 1.00 19.44 ? 384 ARG   A O     1 
ATOM   2791 C CB    . ARG   A 1 384 ? -26.600 14.748  -19.609 1.00 22.78 ? 384 ARG   A CB    1 
ATOM   2792 C CG    . ARG   A 1 384 ? -27.010 15.752  -20.691 1.00 30.77 ? 384 ARG   A CG    1 
ATOM   2793 C CD    . ARG   A 1 384 ? -28.526 15.797  -20.966 1.00 35.78 ? 384 ARG   A CD    1 
ATOM   2794 N NE    . ARG   A 1 384 ? -29.037 14.445  -21.214 1.00 32.92 ? 384 ARG   A NE    1 
ATOM   2795 C CZ    . ARG   A 1 384 ? -29.240 13.872  -22.398 1.00 34.87 ? 384 ARG   A CZ    1 
ATOM   2796 N NH1   . ARG   A 1 384 ? -29.202 14.586  -23.508 1.00 35.26 ? 384 ARG   A NH1   1 
ATOM   2797 N NH2   . ARG   A 1 384 ? -29.524 12.577  -22.462 1.00 33.05 ? 384 ARG   A NH2   1 
ATOM   2798 N N     . SER   A 1 385 ? -24.068 16.318  -18.481 1.00 19.69 ? 385 SER   A N     1 
ATOM   2799 C CA    . SER   A 1 385 ? -23.298 17.595  -18.422 1.00 21.37 ? 385 SER   A CA    1 
ATOM   2800 C C     . SER   A 1 385 ? -21.802 17.367  -18.721 1.00 22.55 ? 385 SER   A C     1 
ATOM   2801 O O     . SER   A 1 385 ? -21.200 18.178  -19.415 1.00 19.33 ? 385 SER   A O     1 
ATOM   2802 C CB    . SER   A 1 385 ? -23.491 18.322  -17.095 1.00 20.36 ? 385 SER   A CB    1 
ATOM   2803 O OG    . SER   A 1 385 ? -22.786 19.548  -17.043 1.00 21.75 ? 385 SER   A OG    1 
ATOM   2804 N N     . SER   A 1 386 ? -21.250 16.283  -18.192 1.00 20.08 ? 386 SER   A N     1 
ATOM   2805 C CA    . SER   A 1 386 ? -19.823 15.977  -18.429 1.00 20.73 ? 386 SER   A CA    1 
ATOM   2806 C C     . SER   A 1 386 ? -19.626 15.683  -19.920 1.00 18.32 ? 386 SER   A C     1 
ATOM   2807 O O     . SER   A 1 386 ? -18.646 16.154  -20.483 1.00 18.76 ? 386 SER   A O     1 
ATOM   2808 C CB    . SER   A 1 386 ? -19.359 14.833  -17.549 1.00 24.54 ? 386 SER   A CB    1 
ATOM   2809 O OG    . SER   A 1 386 ? -20.089 13.648  -17.823 1.00 30.96 ? 386 SER   A OG    1 
ATOM   2810 N N     . ARG   A 1 387 ? -20.570 14.959  -20.529 1.00 20.07 ? 387 ARG   A N     1 
ATOM   2811 C CA    . ARG   A 1 387 ? -20.485 14.716  -21.994 1.00 20.75 ? 387 ARG   A CA    1 
ATOM   2812 C C     . ARG   A 1 387 ? -20.478 16.070  -22.724 1.00 20.76 ? 387 ARG   A C     1 
ATOM   2813 O O     . ARG   A 1 387 ? -19.659 16.258  -23.613 1.00 20.57 ? 387 ARG   A O     1 
ATOM   2814 C CB    . ARG   A 1 387 ? -21.630 13.859  -22.545 1.00 22.78 ? 387 ARG   A CB    1 
ATOM   2815 C CG    . ARG   A 1 387 ? -21.506 13.455  -24.005 1.00 28.19 ? 387 ARG   A CG    1 
ATOM   2816 C CD    . ARG   A 1 387 ? -20.552 12.289  -24.209 1.00 35.82 ? 387 ARG   A CD    1 
ATOM   2817 N NE    . ARG   A 1 387 ? -21.179 10.973  -24.058 1.00 31.83 ? 387 ARG   A NE    1 
ATOM   2818 C CZ    . ARG   A 1 387 ? -21.765 10.281  -25.022 1.00 27.29 ? 387 ARG   A CZ    1 
ATOM   2819 N NH1   . ARG   A 1 387 ? -22.260 9.089   -24.760 1.00 25.57 ? 387 ARG   A NH1   1 
ATOM   2820 N NH2   . ARG   A 1 387 ? -21.853 10.777  -26.242 1.00 25.72 ? 387 ARG   A NH2   1 
ATOM   2821 N N     . ARG   A 1 388 ? -21.395 16.954  -22.346 1.00 20.75 ? 388 ARG   A N     1 
ATOM   2822 C CA    . ARG   A 1 388 ? -21.512 18.261  -23.044 1.00 20.78 ? 388 ARG   A CA    1 
ATOM   2823 C C     . ARG   A 1 388 ? -20.215 19.069  -22.853 1.00 19.04 ? 388 ARG   A C     1 
ATOM   2824 O O     . ARG   A 1 388 ? -19.787 19.708  -23.793 1.00 19.36 ? 388 ARG   A O     1 
ATOM   2825 C CB    . ARG   A 1 388 ? -22.757 19.027  -22.577 1.00 22.44 ? 388 ARG   A CB    1 
ATOM   2826 C CG    . ARG   A 1 388 ? -22.932 20.407  -23.188 1.00 24.63 ? 388 ARG   A CG    1 
ATOM   2827 C CD    . ARG   A 1 388 ? -23.214 20.319  -24.672 1.00 27.39 ? 388 ARG   A CD    1 
ATOM   2828 N NE    . ARG   A 1 388 ? -23.295 21.649  -25.281 1.00 30.32 ? 388 ARG   A NE    1 
ATOM   2829 C CZ    . ARG   A 1 388 ? -22.981 21.923  -26.535 1.00 34.85 ? 388 ARG   A CZ    1 
ATOM   2830 N NH1   . ARG   A 1 388 ? -22.451 20.992  -27.304 1.00 35.95 ? 388 ARG   A NH1   1 
ATOM   2831 N NH2   . ARG   A 1 388 ? -23.201 23.131  -27.015 1.00 37.25 ? 388 ARG   A NH2   1 
ATOM   2832 N N     . THR   A 1 389 ? -19.641 19.038  -21.654 1.00 17.49 ? 389 THR   A N     1 
ATOM   2833 C CA    . THR   A 1 389 ? -18.383 19.777  -21.377 1.00 20.27 ? 389 THR   A CA    1 
ATOM   2834 C C     . THR   A 1 389 ? -17.297 19.338  -22.355 1.00 20.07 ? 389 THR   A C     1 
ATOM   2835 O O     . THR   A 1 389 ? -16.555 20.191  -22.826 1.00 20.60 ? 389 THR   A O     1 
ATOM   2836 C CB    . THR   A 1 389 ? -17.967 19.591  -19.914 1.00 21.97 ? 389 THR   A CB    1 
ATOM   2837 O OG1   . THR   A 1 389 ? -19.038 20.071  -19.108 1.00 21.70 ? 389 THR   A OG1   1 
ATOM   2838 C CG2   . THR   A 1 389 ? -16.682 20.322  -19.567 1.00 22.07 ? 389 THR   A CG2   1 
ATOM   2839 N N     . GLY   A 1 390 ? -17.232 18.040  -22.656 1.00 19.76 ? 390 GLY   A N     1 
ATOM   2840 C CA    . GLY   A 1 390 ? -16.260 17.547  -23.651 1.00 20.67 ? 390 GLY   A CA    1 
ATOM   2841 C C     . GLY   A 1 390 ? -16.560 18.116  -25.028 1.00 21.37 ? 390 GLY   A C     1 
ATOM   2842 O O     . GLY   A 1 390 ? -15.623 18.479  -25.737 1.00 22.45 ? 390 GLY   A O     1 
ATOM   2843 N N     . GLU   A 1 391 ? -17.842 18.212  -25.369 1.00 19.40 ? 391 GLU   A N     1 
ATOM   2844 C CA    . GLU   A 1 391 ? -18.242 18.762  -26.661 1.00 21.60 ? 391 GLU   A CA    1 
ATOM   2845 C C     . GLU   A 1 391 ? -17.918 20.256  -26.734 1.00 22.18 ? 391 GLU   A C     1 
ATOM   2846 O O     . GLU   A 1 391 ? -17.543 20.763  -27.805 1.00 20.79 ? 391 GLU   A O     1 
ATOM   2847 C CB    . GLU   A 1 391 ? -19.733 18.583  -26.923 1.00 24.35 ? 391 GLU   A CB    1 
ATOM   2848 C CG    . GLU   A 1 391 ? -20.162 17.120  -26.922 1.00 26.94 ? 391 GLU   A CG    1 
ATOM   2849 C CD    . GLU   A 1 391 ? -21.654 16.951  -27.102 1.00 29.14 ? 391 GLU   A CD    1 
ATOM   2850 O OE1   . GLU   A 1 391 ? -22.058 15.794  -27.276 1.00 32.99 ? 391 GLU   A OE1   1 
ATOM   2851 O OE2   . GLU   A 1 391 ? -22.387 17.947  -27.045 1.00 29.27 ? 391 GLU   A OE2   1 
ATOM   2852 N N     . LEU   A 1 392 ? -18.070 20.954  -25.606 1.00 19.55 ? 392 LEU   A N     1 
ATOM   2853 C CA    . LEU   A 1 392 ? -17.695 22.365  -25.545 1.00 22.19 ? 392 LEU   A CA    1 
ATOM   2854 C C     . LEU   A 1 392 ? -16.183 22.513  -25.750 1.00 21.62 ? 392 LEU   A C     1 
ATOM   2855 O O     . LEU   A 1 392 ? -15.709 23.332  -26.545 1.00 19.68 ? 392 LEU   A O     1 
ATOM   2856 C CB    . LEU   A 1 392 ? -18.162 22.983  -24.231 1.00 20.26 ? 392 LEU   A CB    1 
ATOM   2857 C CG    . LEU   A 1 392 ? -19.669 23.100  -24.004 1.00 22.34 ? 392 LEU   A CG    1 
ATOM   2858 C CD1   . LEU   A 1 392 ? -19.920 23.650  -22.612 1.00 22.78 ? 392 LEU   A CD1   1 
ATOM   2859 C CD2   . LEU   A 1 392 ? -20.348 23.964  -25.016 1.00 22.01 ? 392 LEU   A CD2   1 
ATOM   2860 N N     . CYS   A 1 393 ? -15.392 21.693  -25.051 1.00 18.57 ? 393 CYS   A N     1 
ATOM   2861 C CA    . CYS   A 1 393 ? -13.956 21.832  -25.050 1.00 19.37 ? 393 CYS   A CA    1 
ATOM   2862 C C     . CYS   A 1 393 ? -13.318 21.408  -26.379 1.00 18.11 ? 393 CYS   A C     1 
ATOM   2863 O O     . CYS   A 1 393 ? -12.186 21.795  -26.593 1.00 18.37 ? 393 CYS   A O     1 
ATOM   2864 C CB    . CYS   A 1 393 ? -13.298 21.033  -23.934 1.00 20.01 ? 393 CYS   A CB    1 
ATOM   2865 S SG    . CYS   A 1 393 ? -13.685 21.664  -22.277 1.00 22.26 ? 393 CYS   A SG    1 
ATOM   2866 N N     . THR   A 1 394 ? -14.042 20.662  -27.214 1.00 18.27 ? 394 THR   A N     1 
ATOM   2867 C CA    . THR   A 1 394 ? -13.565 20.205  -28.518 1.00 21.55 ? 394 THR   A CA    1 
ATOM   2868 C C     . THR   A 1 394 ? -14.295 20.912  -29.656 1.00 22.33 ? 394 THR   A C     1 
ATOM   2869 O O     . THR   A 1 394 ? -14.155 20.495  -30.810 1.00 21.47 ? 394 THR   A O     1 
ATOM   2870 C CB    . THR   A 1 394 ? -13.751 18.690  -28.656 1.00 22.26 ? 394 THR   A CB    1 
ATOM   2871 O OG1   . THR   A 1 394 ? -15.140 18.350  -28.627 1.00 22.38 ? 394 THR   A OG1   1 
ATOM   2872 C CG2   . THR   A 1 394 ? -12.945 17.973  -27.603 1.00 24.07 ? 394 THR   A CG2   1 
ATOM   2873 N N     . TRP   A 1 395 ? -14.962 22.027  -29.338 1.00 21.79 ? 395 TRP   A N     1 
ATOM   2874 C CA    . TRP   A 1 395 ? -15.576 22.910  -30.321 1.00 23.14 ? 395 TRP   A CA    1 
ATOM   2875 C C     . TRP   A 1 395 ? -16.461 22.126  -31.288 1.00 23.72 ? 395 TRP   A C     1 
ATOM   2876 O O     . TRP   A 1 395 ? -16.418 22.334  -32.501 1.00 23.89 ? 395 TRP   A O     1 
ATOM   2877 C CB    . TRP   A 1 395 ? -14.513 23.704  -31.081 1.00 22.06 ? 395 TRP   A CB    1 
ATOM   2878 C CG    . TRP   A 1 395 ? -13.664 24.663  -30.279 1.00 21.63 ? 395 TRP   A CG    1 
ATOM   2879 C CD1   . TRP   A 1 395 ? -13.622 24.862  -28.928 1.00 20.87 ? 395 TRP   A CD1   1 
ATOM   2880 C CD2   . TRP   A 1 395 ? -12.627 25.506  -30.832 1.00 20.97 ? 395 TRP   A CD2   1 
ATOM   2881 N NE1   . TRP   A 1 395 ? -12.647 25.768  -28.615 1.00 20.82 ? 395 TRP   A NE1   1 
ATOM   2882 C CE2   . TRP   A 1 395 ? -12.002 26.170  -29.762 1.00 20.42 ? 395 TRP   A CE2   1 
ATOM   2883 C CE3   . TRP   A 1 395 ? -12.154 25.734  -32.131 1.00 21.83 ? 395 TRP   A CE3   1 
ATOM   2884 C CZ2   . TRP   A 1 395 ? -10.960 27.079  -29.949 1.00 22.24 ? 395 TRP   A CZ2   1 
ATOM   2885 C CZ3   . TRP   A 1 395 ? -11.126 26.627  -32.313 1.00 21.15 ? 395 TRP   A CZ3   1 
ATOM   2886 C CH2   . TRP   A 1 395 ? -10.524 27.284  -31.239 1.00 21.95 ? 395 TRP   A CH2   1 
ATOM   2887 N N     . LYS   A 1 396 ? -17.275 21.228  -30.746 1.00 23.52 ? 396 LYS   A N     1 
ATOM   2888 C CA    . LYS   A 1 396 ? -18.042 20.331  -31.585 1.00 26.12 ? 396 LYS   A CA    1 
ATOM   2889 C C     . LYS   A 1 396 ? -19.026 21.094  -32.475 1.00 27.07 ? 396 LYS   A C     1 
ATOM   2890 O O     . LYS   A 1 396 ? -19.179 20.769  -33.652 1.00 27.49 ? 396 LYS   A O     1 
ATOM   2891 C CB    . LYS   A 1 396 ? -18.776 19.298  -30.738 1.00 28.63 ? 396 LYS   A CB    1 
ATOM   2892 C CG    . LYS   A 1 396 ? -19.477 18.250  -31.577 1.00 33.38 ? 396 LYS   A CG    1 
ATOM   2893 C CD    . LYS   A 1 396 ? -20.176 17.197  -30.743 1.00 34.29 ? 396 LYS   A CD    1 
ATOM   2894 C CE    . LYS   A 1 396 ? -20.887 16.228  -31.647 1.00 42.02 ? 396 LYS   A CE    1 
ATOM   2895 N NZ    . LYS   A 1 396 ? -21.183 14.972  -30.955 1.00 47.70 ? 396 LYS   A NZ    1 
ATOM   2896 N N     . ASP   A 1 397 ? -19.737 22.065  -31.923 1.00 24.82 ? 397 ASP   A N     1 
ATOM   2897 C CA    . ASP   A 1 397 ? -20.784 22.733  -32.686 1.00 31.04 ? 397 ASP   A CA    1 
ATOM   2898 C C     . ASP   A 1 397 ? -20.523 24.231  -32.813 1.00 31.18 ? 397 ASP   A C     1 
ATOM   2899 O O     . ASP   A 1 397 ? -21.283 24.933  -33.474 1.00 29.59 ? 397 ASP   A O     1 
ATOM   2900 C CB    . ASP   A 1 397 ? -22.154 22.459  -32.102 1.00 36.99 ? 397 ASP   A CB    1 
ATOM   2901 C CG    . ASP   A 1 397 ? -22.179 22.417  -30.590 1.00 41.66 ? 397 ASP   A CG    1 
ATOM   2902 O OD1   . ASP   A 1 397 ? -21.847 23.448  -29.974 1.00 45.30 ? 397 ASP   A OD1   1 
ATOM   2903 O OD2   . ASP   A 1 397 ? -22.448 21.328  -30.059 1.00 49.45 ? 397 ASP   A OD2   1 
ATOM   2904 N N     . ARG   A 1 398 ? -19.466 24.722  -32.166 1.00 28.73 ? 398 ARG   A N     1 
ATOM   2905 C CA    . ARG   A 1 398 ? -19.139 26.135  -32.225 1.00 27.01 ? 398 ARG   A CA    1 
ATOM   2906 C C     . ARG   A 1 398 ? -17.653 26.283  -32.005 1.00 25.55 ? 398 ARG   A C     1 
ATOM   2907 O O     . ARG   A 1 398 ? -17.063 25.494  -31.272 1.00 24.33 ? 398 ARG   A O     1 
ATOM   2908 C CB    . ARG   A 1 398 ? -19.690 26.993  -31.081 1.00 30.31 ? 398 ARG   A CB    1 
ATOM   2909 C CG    . ARG   A 1 398 ? -21.198 27.084  -30.916 1.00 32.64 ? 398 ARG   A CG    1 
ATOM   2910 C CD    . ARG   A 1 398 ? -21.800 28.170  -31.777 1.00 31.77 ? 398 ARG   A CD    1 
ATOM   2911 N NE    . ARG   A 1 398 ? -21.311 29.482  -31.356 1.00 29.56 ? 398 ARG   A NE    1 
ATOM   2912 C CZ    . ARG   A 1 398 ? -21.698 30.175  -30.301 1.00 26.53 ? 398 ARG   A CZ    1 
ATOM   2913 N NH1   . ARG   A 1 398 ? -22.678 29.742  -29.520 1.00 29.95 ? 398 ARG   A NH1   1 
ATOM   2914 N NH2   . ARG   A 1 398 ? -21.084 31.306  -30.012 1.00 25.89 ? 398 ARG   A NH2   1 
ATOM   2915 N N     . ASP   A 1 399 ? -17.083 27.341  -32.590 1.00 23.43 ? 399 ASP   A N     1 
ATOM   2916 C CA    . ASP   A 1 399 ? -15.738 27.774  -32.284 1.00 22.59 ? 399 ASP   A CA    1 
ATOM   2917 C C     . ASP   A 1 399 ? -15.799 28.616  -31.013 1.00 25.49 ? 399 ASP   A C     1 
ATOM   2918 O O     . ASP   A 1 399 ? -15.982 29.811  -31.076 1.00 24.74 ? 399 ASP   A O     1 
ATOM   2919 C CB    . ASP   A 1 399 ? -15.134 28.509  -33.471 1.00 24.55 ? 399 ASP   A CB    1 
ATOM   2920 C CG    . ASP   A 1 399 ? -13.708 29.005  -33.310 1.00 29.16 ? 399 ASP   A CG    1 
ATOM   2921 O OD1   . ASP   A 1 399 ? -13.240 29.190  -32.167 1.00 23.54 ? 399 ASP   A OD1   1 
ATOM   2922 O OD2   . ASP   A 1 399 ? -13.038 29.138  -34.350 1.00 27.34 ? 399 ASP   A OD2   1 
ATOM   2923 N N     . TRP   A 1 400 ? -15.571 27.984  -29.856 1.00 24.40 ? 400 TRP   A N     1 
ATOM   2924 C CA    . TRP   A 1 400 ? -15.676 28.706  -28.596 1.00 21.60 ? 400 TRP   A CA    1 
ATOM   2925 C C     . TRP   A 1 400 ? -14.498 29.639  -28.360 1.00 22.57 ? 400 TRP   A C     1 
ATOM   2926 O O     . TRP   A 1 400 ? -14.539 30.456  -27.433 1.00 25.94 ? 400 TRP   A O     1 
ATOM   2927 C CB    . TRP   A 1 400 ? -15.846 27.695  -27.452 1.00 21.32 ? 400 TRP   A CB    1 
ATOM   2928 C CG    . TRP   A 1 400 ? -17.155 26.972  -27.534 1.00 23.30 ? 400 TRP   A CG    1 
ATOM   2929 C CD1   . TRP   A 1 400 ? -17.365 25.673  -27.884 1.00 22.88 ? 400 TRP   A CD1   1 
ATOM   2930 C CD2   . TRP   A 1 400 ? -18.450 27.531  -27.297 1.00 25.58 ? 400 TRP   A CD2   1 
ATOM   2931 N NE1   . TRP   A 1 400 ? -18.687 25.382  -27.882 1.00 25.62 ? 400 TRP   A NE1   1 
ATOM   2932 C CE2   . TRP   A 1 400 ? -19.388 26.509  -27.525 1.00 26.16 ? 400 TRP   A CE2   1 
ATOM   2933 C CE3   . TRP   A 1 400 ? -18.903 28.798  -26.914 1.00 27.23 ? 400 TRP   A CE3   1 
ATOM   2934 C CZ2   . TRP   A 1 400 ? -20.755 26.709  -27.382 1.00 28.24 ? 400 TRP   A CZ2   1 
ATOM   2935 C CZ3   . TRP   A 1 400 ? -20.257 28.993  -26.786 1.00 26.26 ? 400 TRP   A CZ3   1 
ATOM   2936 C CH2   . TRP   A 1 400 ? -21.168 27.972  -27.011 1.00 27.62 ? 400 TRP   A CH2   1 
ATOM   2937 N N     . GLY   A 1 401 ? -13.424 29.528  -29.142 1.00 20.56 ? 401 GLY   A N     1 
ATOM   2938 C CA    . GLY   A 1 401 ? -12.331 30.475  -29.064 1.00 22.33 ? 401 GLY   A CA    1 
ATOM   2939 C C     . GLY   A 1 401 ? -12.811 31.892  -29.362 1.00 23.06 ? 401 GLY   A C     1 
ATOM   2940 O O     . GLY   A 1 401 ? -12.213 32.852  -28.891 1.00 26.39 ? 401 GLY   A O     1 
ATOM   2941 N N     . LEU   A 1 402 ? -13.918 32.006  -30.116 1.00 23.42 ? 402 LEU   A N     1 
ATOM   2942 C CA    . LEU   A 1 402 ? -14.486 33.306  -30.468 1.00 24.87 ? 402 LEU   A CA    1 
ATOM   2943 C C     . LEU   A 1 402 ? -15.681 33.689  -29.587 1.00 28.22 ? 402 LEU   A C     1 
ATOM   2944 O O     . LEU   A 1 402 ? -16.365 34.679  -29.879 1.00 30.04 ? 402 LEU   A O     1 
ATOM   2945 C CB    . LEU   A 1 402 ? -14.886 33.288  -31.945 1.00 23.47 ? 402 LEU   A CB    1 
ATOM   2946 C CG    . LEU   A 1 402 ? -13.740 32.991  -32.915 1.00 22.13 ? 402 LEU   A CG    1 
ATOM   2947 C CD1   . LEU   A 1 402 ? -14.290 33.146  -34.343 1.00 23.86 ? 402 LEU   A CD1   1 
ATOM   2948 C CD2   . LEU   A 1 402 ? -12.532 33.848  -32.684 1.00 23.21 ? 402 LEU   A CD2   1 
ATOM   2949 N N     . ALA   A 1 403 ? -15.939 32.915  -28.514 1.00 25.52 ? 403 ALA   A N     1 
ATOM   2950 C CA    . ALA   A 1 403 ? -17.123 33.112  -27.700 1.00 26.91 ? 403 ALA   A CA    1 
ATOM   2951 C C     . ALA   A 1 403 ? -16.790 32.822  -26.234 1.00 23.46 ? 403 ALA   A C     1 
ATOM   2952 O O     . ALA   A 1 403 ? -17.512 32.074  -25.573 1.00 26.23 ? 403 ALA   A O     1 
ATOM   2953 C CB    . ALA   A 1 403 ? -18.251 32.257  -28.192 1.00 30.10 ? 403 ALA   A CB    1 
ATOM   2954 N N     . ALA   A 1 404 ? -15.724 33.473  -25.771 1.00 24.89 ? 404 ALA   A N     1 
ATOM   2955 C CA    . ALA   A 1 404 ? -15.149 33.234  -24.456 1.00 25.46 ? 404 ALA   A CA    1 
ATOM   2956 C C     . ALA   A 1 404 ? -16.152 33.514  -23.349 1.00 30.26 ? 404 ALA   A C     1 
ATOM   2957 O O     . ALA   A 1 404 ? -16.251 32.740  -22.401 1.00 26.65 ? 404 ALA   A O     1 
ATOM   2958 C CB    . ALA   A 1 404 ? -13.894 34.033  -24.266 1.00 24.89 ? 404 ALA   A CB    1 
ATOM   2959 N N     . GLU   A 1 405 ? -16.864 34.638  -23.430 1.00 29.87 ? 405 GLU   A N     1 
ATOM   2960 C CA    . GLU   A 1 405 ? -17.755 34.998  -22.330 1.00 29.36 ? 405 GLU   A CA    1 
ATOM   2961 C C     . GLU   A 1 405 ? -18.941 34.037  -22.276 1.00 30.97 ? 405 GLU   A C     1 
ATOM   2962 O O     . GLU   A 1 405 ? -19.306 33.588  -21.194 1.00 31.12 ? 405 GLU   A O     1 
ATOM   2963 C CB    . GLU   A 1 405 ? -18.101 36.492  -22.376 1.00 31.47 ? 405 GLU   A CB    1 
ATOM   2964 N N     . GLU   A 1 406 ? -19.488 33.636  -23.429 1.00 26.59 ? 406 GLU   A N     1 
ATOM   2965 C CA    . GLU   A 1 406 ? -20.589 32.690  -23.465 1.00 27.36 ? 406 GLU   A CA    1 
ATOM   2966 C C     . GLU   A 1 406 ? -20.130 31.320  -22.947 1.00 26.18 ? 406 GLU   A C     1 
ATOM   2967 O O     . GLU   A 1 406 ? -20.865 30.633  -22.229 1.00 25.11 ? 406 GLU   A O     1 
ATOM   2968 C CB    . GLU   A 1 406 ? -21.028 32.604  -24.921 1.00 30.39 ? 406 GLU   A CB    1 
ATOM   2969 C CG    . GLU   A 1 406 ? -22.261 31.769  -25.180 1.00 33.34 ? 406 GLU   A CG    1 
ATOM   2970 C CD    . GLU   A 1 406 ? -22.665 31.810  -26.649 1.00 36.78 ? 406 GLU   A CD    1 
ATOM   2971 O OE1   . GLU   A 1 406 ? -23.559 31.011  -26.956 1.00 37.01 ? 406 GLU   A OE1   1 
ATOM   2972 O OE2   . GLU   A 1 406 ? -22.090 32.581  -27.472 1.00 42.19 ? 406 GLU   A OE2   1 
ATOM   2973 N N     . LEU   A 1 407 ? -18.906 30.930  -23.331 1.00 24.15 ? 407 LEU   A N     1 
ATOM   2974 C CA    . LEU   A 1 407 ? -18.355 29.653  -22.881 1.00 24.83 ? 407 LEU   A CA    1 
ATOM   2975 C C     . LEU   A 1 407 ? -18.177 29.665  -21.369 1.00 23.60 ? 407 LEU   A C     1 
ATOM   2976 O O     . LEU   A 1 407 ? -18.527 28.689  -20.691 1.00 23.72 ? 407 LEU   A O     1 
ATOM   2977 C CB    . LEU   A 1 407 ? -17.030 29.364  -23.570 1.00 25.49 ? 407 LEU   A CB    1 
ATOM   2978 C CG    . LEU   A 1 407 ? -16.322 28.093  -23.092 1.00 24.56 ? 407 LEU   A CG    1 
ATOM   2979 C CD1   . LEU   A 1 407 ? -17.117 26.893  -23.521 1.00 25.98 ? 407 LEU   A CD1   1 
ATOM   2980 C CD2   . LEU   A 1 407 ? -14.922 28.046  -23.623 1.00 24.34 ? 407 LEU   A CD2   1 
ATOM   2981 N N     . SER   A 1 408 ? -17.651 30.774  -20.850 1.00 24.37 ? 408 SER   A N     1 
ATOM   2982 C CA    . SER   A 1 408 ? -17.363 30.877  -19.421 1.00 25.75 ? 408 SER   A CA    1 
ATOM   2983 C C     . SER   A 1 408 ? -18.664 30.742  -18.626 1.00 27.46 ? 408 SER   A C     1 
ATOM   2984 O O     . SER   A 1 408 ? -18.715 30.045  -17.618 1.00 25.81 ? 408 SER   A O     1 
ATOM   2985 C CB    . SER   A 1 408 ? -16.628 32.135  -19.074 1.00 25.64 ? 408 SER   A CB    1 
ATOM   2986 O OG    . SER   A 1 408 ? -17.514 33.245  -19.070 1.00 28.31 ? 408 SER   A OG    1 
ATOM   2987 N N     . ARG   A 1 409 ? -19.745 31.378  -19.084 1.00 26.39 ? 409 ARG   A N     1 
ATOM   2988 C CA    . ARG   A 1 409 ? -21.004 31.305  -18.352 1.00 29.03 ? 409 ARG   A CA    1 
ATOM   2989 C C     . ARG   A 1 409 ? -21.545 29.872  -18.305 1.00 27.28 ? 409 ARG   A C     1 
ATOM   2990 O O     . ARG   A 1 409 ? -22.029 29.405  -17.284 1.00 25.59 ? 409 ARG   A O     1 
ATOM   2991 C CB    . ARG   A 1 409 ? -21.981 32.275  -19.013 1.00 30.78 ? 409 ARG   A CB    1 
ATOM   2992 C CG    . ARG   A 1 409 ? -21.540 33.718  -18.828 1.00 33.57 ? 409 ARG   A CG    1 
ATOM   2993 C CD    . ARG   A 1 409 ? -22.626 34.668  -19.301 1.00 40.76 ? 409 ARG   A CD    1 
ATOM   2994 N NE    . ARG   A 1 409 ? -22.376 36.053  -18.889 1.00 44.70 ? 409 ARG   A NE    1 
ATOM   2995 C CZ    . ARG   A 1 409 ? -22.758 37.121  -19.597 1.00 53.21 ? 409 ARG   A CZ    1 
ATOM   2996 N NH1   . ARG   A 1 409 ? -22.654 38.328  -19.071 1.00 56.36 ? 409 ARG   A NH1   1 
ATOM   2997 N NH2   . ARG   A 1 409 ? -23.302 36.975  -20.796 1.00 54.63 ? 409 ARG   A NH2   1 
ATOM   2998 N N     . ASP   A 1 410 ? -21.396 29.156  -19.405 1.00 22.95 ? 410 ASP   A N     1 
ATOM   2999 C CA    . ASP   A 1 410 ? -21.848 27.789  -19.519 1.00 26.44 ? 410 ASP   A CA    1 
ATOM   3000 C C     . ASP   A 1 410 ? -21.028 26.878  -18.594 1.00 25.99 ? 410 ASP   A C     1 
ATOM   3001 O O     . ASP   A 1 410 ? -21.593 26.191  -17.738 1.00 29.09 ? 410 ASP   A O     1 
ATOM   3002 C CB    . ASP   A 1 410 ? -21.851 27.412  -20.993 1.00 26.33 ? 410 ASP   A CB    1 
ATOM   3003 C CG    . ASP   A 1 410 ? -22.397 26.031  -21.308 1.00 33.94 ? 410 ASP   A CG    1 
ATOM   3004 O OD1   . ASP   A 1 410 ? -22.404 25.199  -20.401 1.00 40.86 ? 410 ASP   A OD1   1 
ATOM   3005 O OD2   . ASP   A 1 410 ? -22.783 25.787  -22.462 1.00 36.74 ? 410 ASP   A OD2   1 
ATOM   3006 N N     . ILE   A 1 411 ? -19.696 26.878  -18.723 1.00 25.82 ? 411 ILE   A N     1 
ATOM   3007 C CA    . ILE   A 1 411 ? -18.857 26.029  -17.872 1.00 23.97 ? 411 ILE   A CA    1 
ATOM   3008 C C     . ILE   A 1 411 ? -18.929 26.431  -16.391 1.00 23.75 ? 411 ILE   A C     1 
ATOM   3009 O O     . ILE   A 1 411 ? -18.947 25.563  -15.525 1.00 22.66 ? 411 ILE   A O     1 
ATOM   3010 C CB    . ILE   A 1 411 ? -17.428 25.966  -18.427 1.00 27.36 ? 411 ILE   A CB    1 
ATOM   3011 C CG1   . ILE   A 1 411 ? -17.473 25.190  -19.771 1.00 29.18 ? 411 ILE   A CG1   1 
ATOM   3012 C CG2   . ILE   A 1 411 ? -16.474 25.327  -17.411 1.00 24.98 ? 411 ILE   A CG2   1 
ATOM   3013 C CD1   . ILE   A 1 411 ? -16.158 25.020  -20.484 1.00 36.22 ? 411 ILE   A CD1   1 
ATOM   3014 N N     . ILE   A 1 412 ? -18.919 27.716  -16.057 1.00 22.98 ? 412 ILE   A N     1 
ATOM   3015 C CA    . ILE   A 1 412 ? -18.948 28.089  -14.642 1.00 26.32 ? 412 ILE   A CA    1 
ATOM   3016 C C     . ILE   A 1 412 ? -20.255 27.598  -14.004 1.00 26.60 ? 412 ILE   A C     1 
ATOM   3017 O O     . ILE   A 1 412 ? -20.273 27.103  -12.877 1.00 27.22 ? 412 ILE   A O     1 
ATOM   3018 C CB    . ILE   A 1 412 ? -18.711 29.603  -14.490 1.00 26.84 ? 412 ILE   A CB    1 
ATOM   3019 C CG1   . ILE   A 1 412 ? -17.246 29.929  -14.811 1.00 24.87 ? 412 ILE   A CG1   1 
ATOM   3020 C CG2   . ILE   A 1 412 ? -19.124 30.133  -13.113 1.00 29.21 ? 412 ILE   A CG2   1 
ATOM   3021 C CD1   . ILE   A 1 412 ? -16.952 31.406  -14.989 1.00 28.43 ? 412 ILE   A CD1   1 
ATOM   3022 N N     . SER   A 1 413 ? -21.365 27.703  -14.735 1.00 26.41 ? 413 SER   A N     1 
ATOM   3023 C CA    . SER   A 1 413 ? -22.661 27.275  -14.243 1.00 28.14 ? 413 SER   A CA    1 
ATOM   3024 C C     . SER   A 1 413 ? -22.681 25.760  -14.038 1.00 26.05 ? 413 SER   A C     1 
ATOM   3025 O O     . SER   A 1 413 ? -23.094 25.306  -12.976 1.00 28.19 ? 413 SER   A O     1 
ATOM   3026 C CB    . SER   A 1 413 ? -23.766 27.721  -15.180 1.00 30.86 ? 413 SER   A CB    1 
ATOM   3027 O OG    . SER   A 1 413 ? -24.971 27.050  -14.855 1.00 36.42 ? 413 SER   A OG    1 
ATOM   3028 N N     . ARG   A 1 414 ? -22.255 24.985  -15.036 1.00 22.20 ? 414 ARG   A N     1 
ATOM   3029 C CA    . ARG   A 1 414 ? -22.273 23.532  -14.907 1.00 25.69 ? 414 ARG   A CA    1 
ATOM   3030 C C     . ARG   A 1 414 ? -21.353 23.093  -13.768 1.00 24.15 ? 414 ARG   A C     1 
ATOM   3031 O O     . ARG   A 1 414 ? -21.681 22.145  -13.055 1.00 24.69 ? 414 ARG   A O     1 
ATOM   3032 C CB    . ARG   A 1 414 ? -21.789 22.784  -16.153 1.00 28.64 ? 414 ARG   A CB    1 
ATOM   3033 C CG    . ARG   A 1 414 ? -22.701 22.863  -17.358 1.00 31.22 ? 414 ARG   A CG    1 
ATOM   3034 C CD    . ARG   A 1 414 ? -21.914 22.556  -18.647 1.00 30.03 ? 414 ARG   A CD    1 
ATOM   3035 N NE    . ARG   A 1 414 ? -22.881 22.794  -19.707 1.00 30.09 ? 414 ARG   A NE    1 
ATOM   3036 C CZ    . ARG   A 1 414 ? -23.934 22.047  -19.972 1.00 35.56 ? 414 ARG   A CZ    1 
ATOM   3037 N NH1   . ARG   A 1 414 ? -24.109 20.887  -19.364 1.00 31.39 ? 414 ARG   A NH1   1 
ATOM   3038 N NH2   . ARG   A 1 414 ? -24.802 22.448  -20.885 1.00 40.51 ? 414 ARG   A NH2   1 
ATOM   3039 N N     . SER   A 1 415 ? -20.216 23.781  -13.575 1.00 22.98 ? 415 SER   A N     1 
ATOM   3040 C CA    . SER   A 1 415 ? -19.277 23.421  -12.508 1.00 23.54 ? 415 SER   A CA    1 
ATOM   3041 C C     . SER   A 1 415 ? -19.852 23.705  -11.125 1.00 23.47 ? 415 SER   A C     1 
ATOM   3042 O O     . SER   A 1 415 ? -19.734 22.881  -10.209 1.00 22.28 ? 415 SER   A O     1 
ATOM   3043 C CB    . SER   A 1 415 ? -17.943 24.116  -12.699 1.00 26.84 ? 415 SER   A CB    1 
ATOM   3044 O OG    . SER   A 1 415 ? -17.355 23.666  -13.902 1.00 29.25 ? 415 SER   A OG    1 
ATOM   3045 N N     . HIS   A 1 416 ? -20.479 24.879  -10.977 1.00 25.38 ? 416 HIS   A N     1 
ATOM   3046 C CA    . HIS   A 1 416 ? -21.223 25.223  -9.782  1.00 25.80 ? 416 HIS   A CA    1 
ATOM   3047 C C     . HIS   A 1 416 ? -22.240 24.140  -9.406  1.00 26.35 ? 416 HIS   A C     1 
ATOM   3048 O O     . HIS   A 1 416 ? -22.316 23.766  -8.235  1.00 27.32 ? 416 HIS   A O     1 
ATOM   3049 C CB    . HIS   A 1 416 ? -21.892 26.587  -9.964  1.00 29.54 ? 416 HIS   A CB    1 
ATOM   3050 C CG    . HIS   A 1 416 ? -22.576 27.084  -8.765  1.00 35.81 ? 416 HIS   A CG    1 
ATOM   3051 N ND1   . HIS   A 1 416 ? -21.948 27.209  -7.541  1.00 39.61 ? 416 HIS   A ND1   1 
ATOM   3052 C CD2   . HIS   A 1 416 ? -23.854 27.471  -8.586  1.00 39.87 ? 416 HIS   A CD2   1 
ATOM   3053 C CE1   . HIS   A 1 416 ? -22.824 27.676  -6.656  1.00 40.07 ? 416 HIS   A CE1   1 
ATOM   3054 N NE2   . HIS   A 1 416 ? -23.991 27.831  -7.267  1.00 40.55 ? 416 HIS   A NE2   1 
ATOM   3055 N N     . GLN   A 1 417 ? -23.037 23.685  -10.377 1.00 24.78 ? 417 GLN   A N     1 
ATOM   3056 C CA    . GLN   A 1 417 ? -24.101 22.728  -10.121 1.00 27.37 ? 417 GLN   A CA    1 
ATOM   3057 C C     . GLN   A 1 417 ? -23.490 21.414  -9.619  1.00 28.41 ? 417 GLN   A C     1 
ATOM   3058 O O     . GLN   A 1 417 ? -24.029 20.792  -8.703  1.00 28.86 ? 417 GLN   A O     1 
ATOM   3059 C CB    . GLN   A 1 417 ? -24.937 22.484  -11.374 1.00 29.72 ? 417 GLN   A CB    1 
ATOM   3060 C CG    . GLN   A 1 417 ? -25.703 23.689  -11.917 1.00 32.32 ? 417 GLN   A CG    1 
ATOM   3061 C CD    . GLN   A 1 417 ? -26.318 23.415  -13.279 1.00 38.26 ? 417 GLN   A CD    1 
ATOM   3062 O OE1   . GLN   A 1 417 ? -25.698 22.836  -14.188 1.00 40.85 ? 417 GLN   A OE1   1 
ATOM   3063 N NE2   . GLN   A 1 417 ? -27.562 23.828  -13.444 1.00 40.43 ? 417 GLN   A NE2   1 
ATOM   3064 N N     . LEU   A 1 418 ? -22.354 21.017  -10.197 1.00 25.70 ? 418 LEU   A N     1 
ATOM   3065 C CA    . LEU   A 1 418 ? -21.749 19.734  -9.858  1.00 25.50 ? 418 LEU   A CA    1 
ATOM   3066 C C     . LEU   A 1 418 ? -20.888 19.819  -8.600  1.00 29.06 ? 418 LEU   A C     1 
ATOM   3067 O O     . LEU   A 1 418 ? -20.930 18.902  -7.771  1.00 28.81 ? 418 LEU   A O     1 
ATOM   3068 C CB    . LEU   A 1 418 ? -20.970 19.126  -11.024 1.00 26.08 ? 418 LEU   A CB    1 
ATOM   3069 C CG    . LEU   A 1 418 ? -21.830 18.689  -12.216 1.00 28.56 ? 418 LEU   A CG    1 
ATOM   3070 C CD1   . LEU   A 1 418 ? -20.963 18.116  -13.349 1.00 29.35 ? 418 LEU   A CD1   1 
ATOM   3071 C CD2   . LEU   A 1 418 ? -22.881 17.663  -11.801 1.00 31.50 ? 418 LEU   A CD2   1 
ATOM   3072 N N     . TRP   A 1 419 ? -20.132 20.904  -8.423  1.00 22.95 ? 419 TRP   A N     1 
ATOM   3073 C CA    . TRP   A 1 419 ? -19.050 20.893  -7.447  1.00 24.62 ? 419 TRP   A CA    1 
ATOM   3074 C C     . TRP   A 1 419 ? -19.436 21.602  -6.152  1.00 26.13 ? 419 TRP   A C     1 
ATOM   3075 O O     . TRP   A 1 419 ? -18.852 21.339  -5.101  1.00 26.62 ? 419 TRP   A O     1 
ATOM   3076 C CB    . TRP   A 1 419 ? -17.771 21.527  -8.011  1.00 23.21 ? 419 TRP   A CB    1 
ATOM   3077 C CG    . TRP   A 1 419 ? -17.149 20.836  -9.189  1.00 22.57 ? 419 TRP   A CG    1 
ATOM   3078 C CD1   . TRP   A 1 419 ? -17.412 19.598  -9.696  1.00 25.69 ? 419 TRP   A CD1   1 
ATOM   3079 C CD2   . TRP   A 1 419 ? -16.158 21.425  -10.041 1.00 23.25 ? 419 TRP   A CD2   1 
ATOM   3080 N NE1   . TRP   A 1 419 ? -16.637 19.372  -10.798 1.00 25.16 ? 419 TRP   A NE1   1 
ATOM   3081 C CE2   . TRP   A 1 419 ? -15.864 20.475  -11.040 1.00 24.54 ? 419 TRP   A CE2   1 
ATOM   3082 C CE3   . TRP   A 1 419 ? -15.509 22.667  -10.053 1.00 26.05 ? 419 TRP   A CE3   1 
ATOM   3083 C CZ2   . TRP   A 1 419 ? -14.933 20.735  -12.041 1.00 26.58 ? 419 TRP   A CZ2   1 
ATOM   3084 C CZ3   . TRP   A 1 419 ? -14.620 22.936  -11.070 1.00 27.20 ? 419 TRP   A CZ3   1 
ATOM   3085 C CH2   . TRP   A 1 419 ? -14.338 21.977  -12.045 1.00 27.41 ? 419 TRP   A CH2   1 
ATOM   3086 N N     . ASP   A 1 420 ? -20.428 22.490  -6.210  1.00 28.03 ? 420 ASP   A N     1 
ATOM   3087 C CA    . ASP   A 1 420 ? -20.719 23.358  -5.081  1.00 27.84 ? 420 ASP   A CA    1 
ATOM   3088 C C     . ASP   A 1 420 ? -21.994 22.946  -4.363  1.00 25.87 ? 420 ASP   A C     1 
ATOM   3089 O O     . ASP   A 1 420 ? -22.456 23.676  -3.510  1.00 26.96 ? 420 ASP   A O     1 
ATOM   3090 C CB    . ASP   A 1 420 ? -20.796 24.794  -5.558  1.00 28.57 ? 420 ASP   A CB    1 
ATOM   3091 C CG    . ASP   A 1 420 ? -19.492 25.312  -6.135  1.00 33.47 ? 420 ASP   A CG    1 
ATOM   3092 O OD1   . ASP   A 1 420 ? -18.443 24.663  -5.902  1.00 30.16 ? 420 ASP   A OD1   1 
ATOM   3093 O OD2   . ASP   A 1 420 ? -19.546 26.372  -6.803  1.00 32.06 ? 420 ASP   A OD2   1 
ATOM   3094 N N     . HIS   A 1 421 ? -22.521 21.777  -4.738  1.00 27.90 ? 421 HIS   A N     1 
ATOM   3095 C CA    . HIS   A 1 421 ? -23.638 21.059  -4.143  1.00 35.57 ? 421 HIS   A CA    1 
ATOM   3096 C C     . HIS   A 1 421 ? -23.546 21.044  -2.616  1.00 33.36 ? 421 HIS   A C     1 
ATOM   3097 O O     . HIS   A 1 421 ? -22.456 20.906  -2.076  1.00 30.18 ? 421 HIS   A O     1 
ATOM   3098 C CB    . HIS   A 1 421 ? -23.555 19.652  -4.772  1.00 40.78 ? 421 HIS   A CB    1 
ATOM   3099 C CG    . HIS   A 1 421 ? -24.518 18.607  -4.297  1.00 42.16 ? 421 HIS   A CG    1 
ATOM   3100 N ND1   . HIS   A 1 421 ? -25.829 18.541  -4.718  1.00 45.48 ? 421 HIS   A ND1   1 
ATOM   3101 C CD2   . HIS   A 1 421 ? -24.339 17.561  -3.476  1.00 39.24 ? 421 HIS   A CD2   1 
ATOM   3102 C CE1   . HIS   A 1 421 ? -26.421 17.503  -4.146  1.00 43.07 ? 421 HIS   A CE1   1 
ATOM   3103 N NE2   . HIS   A 1 421 ? -25.532 16.889  -3.394  1.00 44.29 ? 421 HIS   A NE2   1 
ATOM   3104 N N     . ASP   A 1 422 ? -24.691 21.142  -1.923  1.00 35.80 ? 422 ASP   A N     1 
ATOM   3105 C CA    . ASP   A 1 422 ? -24.715 21.119  -0.463  1.00 34.11 ? 422 ASP   A CA    1 
ATOM   3106 C C     . ASP   A 1 422 ? -24.695 19.665  0.014   1.00 33.83 ? 422 ASP   A C     1 
ATOM   3107 O O     . ASP   A 1 422 ? -25.746 19.051  0.130   1.00 28.52 ? 422 ASP   A O     1 
ATOM   3108 C CB    . ASP   A 1 422 ? -25.930 21.837  0.123   1.00 43.32 ? 422 ASP   A CB    1 
ATOM   3109 C CG    . ASP   A 1 422 ? -26.013 21.947  1.646   1.00 38.10 ? 422 ASP   A CG    1 
ATOM   3110 O OD1   . ASP   A 1 422 ? -25.057 21.549  2.335   1.00 41.75 ? 422 ASP   A OD1   1 
ATOM   3111 O OD2   . ASP   A 1 422 ? -27.045 22.431  2.158   1.00 43.27 ? 422 ASP   A OD2   1 
ATOM   3112 N N     . THR   A 1 423 ? -23.487 19.131  0.255   1.00 31.40 ? 423 THR   A N     1 
ATOM   3113 C CA    . THR   A 1 423 ? -23.277 17.743  0.647   1.00 28.79 ? 423 THR   A CA    1 
ATOM   3114 C C     . THR   A 1 423 ? -24.016 17.446  1.959   1.00 31.23 ? 423 THR   A C     1 
ATOM   3115 O O     . THR   A 1 423 ? -24.689 16.425  2.091   1.00 27.42 ? 423 THR   A O     1 
ATOM   3116 C CB    . THR   A 1 423 ? -21.763 17.543  0.816   1.00 29.32 ? 423 THR   A CB    1 
ATOM   3117 O OG1   . THR   A 1 423 ? -21.092 18.001  -0.355  1.00 27.20 ? 423 THR   A OG1   1 
ATOM   3118 C CG2   . THR   A 1 423 ? -21.368 16.090  1.008   1.00 31.27 ? 423 THR   A CG2   1 
ATOM   3119 N N     . ALA   A 1 424 ? -23.901 18.360  2.933   1.00 31.13 ? 424 ALA   A N     1 
ATOM   3120 C CA    . ALA   A 1 424 ? -24.591 18.227  4.203   1.00 29.68 ? 424 ALA   A CA    1 
ATOM   3121 C C     . ALA   A 1 424 ? -26.102 18.163  3.996   1.00 29.10 ? 424 ALA   A C     1 
ATOM   3122 O O     . ALA   A 1 424 ? -26.794 17.369  4.631   1.00 28.69 ? 424 ALA   A O     1 
ATOM   3123 C CB    . ALA   A 1 424 ? -24.259 19.392  5.101   1.00 32.85 ? 424 ALA   A CB    1 
ATOM   3124 N N     . GLY   A 1 425 ? -26.604 19.019  3.115   1.00 28.04 ? 425 GLY   A N     1 
ATOM   3125 C CA    . GLY   A 1 425 ? -28.023 19.158  2.875   1.00 26.96 ? 425 GLY   A CA    1 
ATOM   3126 C C     . GLY   A 1 425 ? -28.556 17.917  2.181   1.00 25.91 ? 425 GLY   A C     1 
ATOM   3127 O O     . GLY   A 1 425 ? -29.685 17.499  2.425   1.00 24.63 ? 425 GLY   A O     1 
ATOM   3128 N N     . MET   A 1 426 ? -27.703 17.309  1.350   1.00 26.63 ? 426 MET   A N     1 
ATOM   3129 C CA    . MET   A 1 426 ? -28.055 16.088  0.658   1.00 24.48 ? 426 MET   A CA    1 
ATOM   3130 C C     . MET   A 1 426 ? -28.359 14.974  1.645   1.00 23.01 ? 426 MET   A C     1 
ATOM   3131 O O     . MET   A 1 426 ? -29.340 14.252  1.484   1.00 23.61 ? 426 MET   A O     1 
ATOM   3132 C CB    . MET   A 1 426 ? -26.947 15.637  -0.292  1.00 26.27 ? 426 MET   A CB    1 
ATOM   3133 C CG    . MET   A 1 426 ? -27.136 14.226  -0.827  1.00 26.56 ? 426 MET   A CG    1 
ATOM   3134 S SD    . MET   A 1 426 ? -25.775 13.877  -1.953  1.00 29.96 ? 426 MET   A SD    1 
ATOM   3135 C CE    . MET   A 1 426 ? -24.429 13.782  -0.760  1.00 29.53 ? 426 MET   A CE    1 
ATOM   3136 N N     . VAL   A 1 427 ? -27.495 14.829  2.644   1.00 22.08 ? 427 VAL   A N     1 
ATOM   3137 C CA    . VAL   A 1 427 ? -27.647 13.770  3.627   1.00 22.83 ? 427 VAL   A CA    1 
ATOM   3138 C C     . VAL   A 1 427 ? -28.857 14.051  4.523   1.00 21.98 ? 427 VAL   A C     1 
ATOM   3139 O O     . VAL   A 1 427 ? -29.672 13.172  4.837   1.00 21.18 ? 427 VAL   A O     1 
ATOM   3140 C CB    . VAL   A 1 427 ? -26.366 13.640  4.476   1.00 24.57 ? 427 VAL   A CB    1 
ATOM   3141 C CG1   . VAL   A 1 427 ? -26.628 12.712  5.646   1.00 22.18 ? 427 VAL   A CG1   1 
ATOM   3142 C CG2   . VAL   A 1 427 ? -25.149 13.171  3.681   1.00 26.62 ? 427 VAL   A CG2   1 
ATOM   3143 N N     . SER   A 1 428 ? -28.972 15.284  5.008   1.00 22.79 ? 428 SER   A N     1 
ATOM   3144 C CA    . SER   A 1 428 ? -30.093 15.620  5.875   1.00 21.99 ? 428 SER   A CA    1 
ATOM   3145 C C     . SER   A 1 428 ? -31.434 15.421  5.151   1.00 22.82 ? 428 SER   A C     1 
ATOM   3146 O O     . SER   A 1 428 ? -32.369 14.869  5.702   1.00 22.27 ? 428 SER   A O     1 
ATOM   3147 C CB    . SER   A 1 428 ? -29.933 17.021  6.417   1.00 24.78 ? 428 SER   A CB    1 
ATOM   3148 O OG    . SER   A 1 428 ? -30.778 17.197  7.534   1.00 28.38 ? 428 SER   A OG    1 
ATOM   3149 N N     . ASP   A 1 429 ? -31.529 15.848  3.885   1.00 23.02 ? 429 ASP   A N     1 
ATOM   3150 C CA    . ASP   A 1 429 ? -32.675 15.574  3.043   1.00 23.53 ? 429 ASP   A CA    1 
ATOM   3151 C C     . ASP   A 1 429 ? -33.002 14.076  2.966   1.00 23.41 ? 429 ASP   A C     1 
ATOM   3152 O O     . ASP   A 1 429 ? -34.161 13.699  3.148   1.00 23.65 ? 429 ASP   A O     1 
ATOM   3153 C CB    . ASP   A 1 429 ? -32.434 16.075  1.628   1.00 27.76 ? 429 ASP   A CB    1 
ATOM   3154 C CG    . ASP   A 1 429 ? -32.447 17.579  1.419   1.00 36.69 ? 429 ASP   A CG    1 
ATOM   3155 O OD1   . ASP   A 1 429 ? -32.567 18.323  2.425   1.00 36.50 ? 429 ASP   A OD1   1 
ATOM   3156 O OD2   . ASP   A 1 429 ? -32.317 17.990  0.236   1.00 40.74 ? 429 ASP   A OD2   1 
ATOM   3157 N N     . ALA   A 1 430 ? -31.997 13.232  2.693   1.00 22.22 ? 430 ALA   A N     1 
ATOM   3158 C CA    . ALA   A 1 430 ? -32.208 11.789  2.610   1.00 19.27 ? 430 ALA   A CA    1 
ATOM   3159 C C     . ALA   A 1 430 ? -32.814 11.256  3.904   1.00 19.33 ? 430 ALA   A C     1 
ATOM   3160 O O     . ALA   A 1 430 ? -33.722 10.439  3.912   1.00 20.43 ? 430 ALA   A O     1 
ATOM   3161 C CB    . ALA   A 1 430 ? -30.914 11.069  2.286   1.00 21.23 ? 430 ALA   A CB    1 
ATOM   3162 N N     . LEU   A 1 431 ? -32.247 11.676  5.027   1.00 18.03 ? 431 LEU   A N     1 
ATOM   3163 C CA    . LEU   A 1 431 ? -32.713 11.179  6.303   1.00 17.58 ? 431 LEU   A CA    1 
ATOM   3164 C C     . LEU   A 1 431 ? -34.086 11.730  6.691   1.00 18.53 ? 431 LEU   A C     1 
ATOM   3165 O O     . LEU   A 1 431 ? -34.806 11.071  7.431   1.00 18.74 ? 431 LEU   A O     1 
ATOM   3166 C CB    . LEU   A 1 431 ? -31.660 11.483  7.362   1.00 19.95 ? 431 LEU   A CB    1 
ATOM   3167 C CG    . LEU   A 1 431 ? -30.265 10.878  7.171   1.00 21.38 ? 431 LEU   A CG    1 
ATOM   3168 C CD1   . LEU   A 1 431 ? -29.314 11.295  8.250   1.00 23.55 ? 431 LEU   A CD1   1 
ATOM   3169 C CD2   . LEU   A 1 431 ? -30.325 9.342   7.096   1.00 25.23 ? 431 LEU   A CD2   1 
ATOM   3170 N N     . ALA   A 1 432 ? -34.413 12.962  6.307   1.00 19.75 ? 432 ALA   A N     1 
ATOM   3171 C CA    . ALA   A 1 432 ? -35.740 13.513  6.542   1.00 20.32 ? 432 ALA   A CA    1 
ATOM   3172 C C     . ALA   A 1 432 ? -36.774 12.684  5.787   1.00 22.17 ? 432 ALA   A C     1 
ATOM   3173 O O     . ALA   A 1 432 ? -37.773 12.256  6.345   1.00 22.17 ? 432 ALA   A O     1 
ATOM   3174 C CB    . ALA   A 1 432 ? -35.796 14.976  6.143   1.00 19.65 ? 432 ALA   A CB    1 
ATOM   3175 N N     . ILE   A 1 433 ? -36.501 12.442  4.503   1.00 21.23 ? 433 ILE   A N     1 
ATOM   3176 C CA    . ILE   A 1 433 ? -37.396 11.672  3.662   1.00 22.76 ? 433 ILE   A CA    1 
ATOM   3177 C C     . ILE   A 1 433 ? -37.548 10.250  4.207   1.00 23.08 ? 433 ILE   A C     1 
ATOM   3178 O O     . ILE   A 1 433 ? -38.670 9.739   4.328   1.00 24.28 ? 433 ILE   A O     1 
ATOM   3179 C CB    . ILE   A 1 433 ? -36.865 11.681  2.216   1.00 23.67 ? 433 ILE   A CB    1 
ATOM   3180 C CG1   . ILE   A 1 433 ? -36.917 13.064  1.599   1.00 25.53 ? 433 ILE   A CG1   1 
ATOM   3181 C CG2   . ILE   A 1 433 ? -37.640 10.682  1.365   1.00 24.83 ? 433 ILE   A CG2   1 
ATOM   3182 C CD1   . ILE   A 1 433 ? -36.152 13.170  0.291   1.00 28.83 ? 433 ILE   A CD1   1 
ATOM   3183 N N     . LEU   A 1 434 ? -36.415 9.617   4.535   1.00 22.58 ? 434 LEU   A N     1 
ATOM   3184 C CA    . LEU   A 1 434 ? -36.408 8.286   5.110   1.00 20.89 ? 434 LEU   A CA    1 
ATOM   3185 C C     . LEU   A 1 434 ? -37.294 8.277   6.359   1.00 22.80 ? 434 LEU   A C     1 
ATOM   3186 O O     . LEU   A 1 434 ? -38.093 7.367   6.527   1.00 24.45 ? 434 LEU   A O     1 
ATOM   3187 C CB    . LEU   A 1 434 ? -34.990 7.824   5.455   1.00 22.63 ? 434 LEU   A CB    1 
ATOM   3188 C CG    . LEU   A 1 434 ? -34.845 6.401   6.004   1.00 23.36 ? 434 LEU   A CG    1 
ATOM   3189 C CD1   . LEU   A 1 434 ? -35.242 5.372   4.934   1.00 25.27 ? 434 LEU   A CD1   1 
ATOM   3190 C CD2   . LEU   A 1 434 ? -33.430 6.110   6.507   1.00 24.87 ? 434 LEU   A CD2   1 
ATOM   3191 N N     . GLY   A 1 435 ? -37.125 9.264   7.244   1.00 21.79 ? 435 GLY   A N     1 
ATOM   3192 C CA    . GLY   A 1 435 ? -37.873 9.301   8.486   1.00 23.64 ? 435 GLY   A CA    1 
ATOM   3193 C C     . GLY   A 1 435 ? -39.383 9.395   8.238   1.00 26.57 ? 435 GLY   A C     1 
ATOM   3194 O O     . GLY   A 1 435 ? -40.173 8.765   8.932   1.00 28.32 ? 435 GLY   A O     1 
ATOM   3195 N N     . GLU   A 1 436 ? -39.775 10.146  7.202   1.00 25.40 ? 436 GLU   A N     1 
ATOM   3196 C CA    . GLU   A 1 436 ? -41.180 10.276  6.871   1.00 28.74 ? 436 GLU   A CA    1 
ATOM   3197 C C     . GLU   A 1 436 ? -41.697 8.965   6.294   1.00 29.98 ? 436 GLU   A C     1 
ATOM   3198 O O     . GLU   A 1 436 ? -42.844 8.625   6.554   1.00 33.61 ? 436 GLU   A O     1 
ATOM   3199 C CB    . GLU   A 1 436 ? -41.443 11.397  5.883   1.00 30.01 ? 436 GLU   A CB    1 
ATOM   3200 C CG    . GLU   A 1 436 ? -41.200 12.772  6.480   1.00 36.80 ? 436 GLU   A CG    1 
ATOM   3201 C CD    . GLU   A 1 436 ? -41.340 13.916  5.496   1.00 45.54 ? 436 GLU   A CD    1 
ATOM   3202 O OE1   . GLU   A 1 436 ? -41.440 15.084  5.950   1.00 57.31 ? 436 GLU   A OE1   1 
ATOM   3203 O OE2   . GLU   A 1 436 ? -41.343 13.640  4.281   1.00 53.20 ? 436 GLU   A OE2   1 
ATOM   3204 N N     . ARG   A 1 437 ? -40.868 8.241   5.524   1.00 30.61 ? 437 ARG   A N     1 
ATOM   3205 C CA    . ARG   A 1 437 ? -41.363 7.108   4.760   1.00 31.91 ? 437 ARG   A CA    1 
ATOM   3206 C C     . ARG   A 1 437 ? -41.351 5.757   5.466   1.00 34.94 ? 437 ARG   A C     1 
ATOM   3207 O O     . ARG   A 1 437 ? -42.011 4.854   4.959   1.00 35.16 ? 437 ARG   A O     1 
ATOM   3208 C CB    . ARG   A 1 437 ? -40.600 6.891   3.465   1.00 30.66 ? 437 ARG   A CB    1 
ATOM   3209 C CG    . ARG   A 1 437 ? -40.991 8.067   2.599   1.00 29.66 ? 437 ARG   A CG    1 
ATOM   3210 C CD    . ARG   A 1 437 ? -40.524 7.772   1.240   1.00 28.04 ? 437 ARG   A CD    1 
ATOM   3211 N NE    . ARG   A 1 437 ? -40.599 8.986   0.447   1.00 31.19 ? 437 ARG   A NE    1 
ATOM   3212 C CZ    . ARG   A 1 437 ? -40.107 9.042   -0.759  1.00 30.54 ? 437 ARG   A CZ    1 
ATOM   3213 N NH1   . ARG   A 1 437 ? -39.635 7.933   -1.296  1.00 32.38 ? 437 ARG   A NH1   1 
ATOM   3214 N NH2   . ARG   A 1 437 ? -40.162 10.178  -1.422  1.00 31.65 ? 437 ARG   A NH2   1 
ATOM   3215 N N     . VAL   A 1 438 ? -40.602 5.584   6.565   1.00 35.16 ? 438 VAL   A N     1 
ATOM   3216 C CA    . VAL   A 1 438 ? -40.507 4.272   7.202   1.00 40.42 ? 438 VAL   A CA    1 
ATOM   3217 C C     . VAL   A 1 438 ? -41.277 4.255   8.535   1.00 44.39 ? 438 VAL   A C     1 
ATOM   3218 O O     . VAL   A 1 438 ? -41.006 5.143   9.356   1.00 57.31 ? 438 VAL   A O     1 
ATOM   3219 C CB    . VAL   A 1 438 ? -39.058 3.781   7.387   1.00 42.83 ? 438 VAL   A CB    1 
ATOM   3220 C CG1   . VAL   A 1 438 ? -38.403 3.488   6.041   1.00 42.58 ? 438 VAL   A CG1   1 
ATOM   3221 C CG2   . VAL   A 1 438 ? -38.217 4.738   8.209   1.00 46.48 ? 438 VAL   A CG2   1 
HETATM 3222 P PA    . FAD   B 2 .   ? -14.666 0.115   -10.177 1.00 22.82 ? 501 FAD   A PA    1 
HETATM 3223 O O1A   . FAD   B 2 .   ? -14.921 -0.491  -11.504 1.00 24.52 ? 501 FAD   A O1A   1 
HETATM 3224 O O2A   . FAD   B 2 .   ? -13.482 0.972   -9.909  1.00 26.07 ? 501 FAD   A O2A   1 
HETATM 3225 O O5B   . FAD   B 2 .   ? -14.584 -1.068  -9.106  1.00 19.54 ? 501 FAD   A O5B   1 
HETATM 3226 C C5B   . FAD   B 2 .   ? -15.462 -2.188  -9.306  1.00 19.76 ? 501 FAD   A C5B   1 
HETATM 3227 C C4B   . FAD   B 2 .   ? -14.948 -3.328  -8.467  1.00 19.25 ? 501 FAD   A C4B   1 
HETATM 3228 O O4B   . FAD   B 2 .   ? -15.913 -4.406  -8.472  1.00 21.16 ? 501 FAD   A O4B   1 
HETATM 3229 C C3B   . FAD   B 2 .   ? -13.616 -3.900  -8.947  1.00 22.07 ? 501 FAD   A C3B   1 
HETATM 3230 O O3B   . FAD   B 2 .   ? -12.768 -4.184  -7.848  1.00 22.96 ? 501 FAD   A O3B   1 
HETATM 3231 C C2B   . FAD   B 2 .   ? -14.038 -5.167  -9.693  1.00 22.67 ? 501 FAD   A C2B   1 
HETATM 3232 O O2B   . FAD   B 2 .   ? -13.085 -6.205  -9.650  1.00 23.35 ? 501 FAD   A O2B   1 
HETATM 3233 C C1B   . FAD   B 2 .   ? -15.247 -5.592  -8.862  1.00 20.54 ? 501 FAD   A C1B   1 
HETATM 3234 N N9A   . FAD   B 2 .   ? -16.223 -6.424  -9.539  1.00 20.05 ? 501 FAD   A N9A   1 
HETATM 3235 C C8A   . FAD   B 2 .   ? -16.708 -6.284  -10.820 1.00 20.86 ? 501 FAD   A C8A   1 
HETATM 3236 N N7A   . FAD   B 2 .   ? -17.639 -7.155  -11.127 1.00 19.28 ? 501 FAD   A N7A   1 
HETATM 3237 C C5A   . FAD   B 2 .   ? -17.751 -7.944  -9.974  1.00 20.98 ? 501 FAD   A C5A   1 
HETATM 3238 C C6A   . FAD   B 2 .   ? -18.576 -9.041  -9.648  1.00 21.60 ? 501 FAD   A C6A   1 
HETATM 3239 N N6A   . FAD   B 2 .   ? -19.471 -9.589  -10.474 1.00 22.50 ? 501 FAD   A N6A   1 
HETATM 3240 N N1A   . FAD   B 2 .   ? -18.452 -9.573  -8.407  1.00 19.43 ? 501 FAD   A N1A   1 
HETATM 3241 C C2A   . FAD   B 2 .   ? -17.545 -9.026  -7.567  1.00 18.84 ? 501 FAD   A C2A   1 
HETATM 3242 N N3A   . FAD   B 2 .   ? -16.715 -8.005  -7.758  1.00 19.44 ? 501 FAD   A N3A   1 
HETATM 3243 C C4A   . FAD   B 2 .   ? -16.896 -7.479  -8.986  1.00 19.82 ? 501 FAD   A C4A   1 
HETATM 3244 N N1    . FAD   B 2 .   ? -11.533 7.330   -14.095 1.00 25.21 ? 501 FAD   A N1    1 
HETATM 3245 C C2    . FAD   B 2 .   ? -11.203 8.660   -14.123 1.00 28.47 ? 501 FAD   A C2    1 
HETATM 3246 O O2    . FAD   B 2 .   ? -11.803 9.510   -13.453 1.00 30.55 ? 501 FAD   A O2    1 
HETATM 3247 N N3    . FAD   B 2 .   ? -10.082 9.035   -14.846 1.00 27.65 ? 501 FAD   A N3    1 
HETATM 3248 C C4    . FAD   B 2 .   ? -9.287  8.219   -15.633 1.00 29.24 ? 501 FAD   A C4    1 
HETATM 3249 O O4    . FAD   B 2 .   ? -8.322  8.638   -16.253 1.00 29.49 ? 501 FAD   A O4    1 
HETATM 3250 C C4X   . FAD   B 2 .   ? -9.668  6.876   -15.624 1.00 25.94 ? 501 FAD   A C4X   1 
HETATM 3251 N N5    . FAD   B 2 .   ? -8.964  6.051   -16.369 1.00 25.56 ? 501 FAD   A N5    1 
HETATM 3252 C C5X   . FAD   B 2 .   ? -9.340  4.735   -16.367 1.00 27.10 ? 501 FAD   A C5X   1 
HETATM 3253 C C6    . FAD   B 2 .   ? -8.628  3.819   -17.170 1.00 28.40 ? 501 FAD   A C6    1 
HETATM 3254 C C7    . FAD   B 2 .   ? -8.983  2.489   -17.221 1.00 28.26 ? 501 FAD   A C7    1 
HETATM 3255 C C7M   . FAD   B 2 .   ? -8.200  1.527   -18.078 1.00 30.90 ? 501 FAD   A C7M   1 
HETATM 3256 C C8    . FAD   B 2 .   ? -10.035 2.011   -16.385 1.00 29.01 ? 501 FAD   A C8    1 
HETATM 3257 C C8M   . FAD   B 2 .   ? -10.439 0.566   -16.363 1.00 29.94 ? 501 FAD   A C8M   1 
HETATM 3258 C C9    . FAD   B 2 .   ? -10.736 2.904   -15.608 1.00 25.29 ? 501 FAD   A C9    1 
HETATM 3259 C C9A   . FAD   B 2 .   ? -10.412 4.264   -15.582 1.00 26.54 ? 501 FAD   A C9A   1 
HETATM 3260 N N10   . FAD   B 2 .   ? -11.129 5.178   -14.805 1.00 25.63 ? 501 FAD   A N10   1 
HETATM 3261 C C10   . FAD   B 2 .   ? -10.793 6.500   -14.803 1.00 23.94 ? 501 FAD   A C10   1 
HETATM 3262 C "C1'" . FAD   B 2 .   ? -12.289 4.747   -14.000 1.00 24.97 ? 501 FAD   A "C1'" 1 
HETATM 3263 C "C2'" . FAD   B 2 .   ? -12.047 4.688   -12.510 1.00 26.67 ? 501 FAD   A "C2'" 1 
HETATM 3264 O "O2'" . FAD   B 2 .   ? -11.154 3.621   -12.221 1.00 27.04 ? 501 FAD   A "O2'" 1 
HETATM 3265 C "C3'" . FAD   B 2 .   ? -13.384 4.452   -11.797 1.00 25.48 ? 501 FAD   A "C3'" 1 
HETATM 3266 O "O3'" . FAD   B 2 .   ? -14.297 5.455   -12.248 1.00 23.20 ? 501 FAD   A "O3'" 1 
HETATM 3267 C "C4'" . FAD   B 2 .   ? -13.325 4.440   -10.266 1.00 22.22 ? 501 FAD   A "C4'" 1 
HETATM 3268 O "O4'" . FAD   B 2 .   ? -12.542 3.325   -9.801  1.00 22.89 ? 501 FAD   A "O4'" 1 
HETATM 3269 C "C5'" . FAD   B 2 .   ? -14.736 4.398   -9.683  1.00 21.88 ? 501 FAD   A "C5'" 1 
HETATM 3270 O "O5'" . FAD   B 2 .   ? -15.382 3.176   -10.061 1.00 21.51 ? 501 FAD   A "O5'" 1 
HETATM 3271 P P     . FAD   B 2 .   ? -16.203 2.289   -9.027  1.00 21.69 ? 501 FAD   A P     1 
HETATM 3272 O O1P   . FAD   B 2 .   ? -15.581 2.332   -7.671  1.00 20.05 ? 501 FAD   A O1P   1 
HETATM 3273 O O2P   . FAD   B 2 .   ? -17.635 2.604   -9.104  1.00 21.86 ? 501 FAD   A O2P   1 
HETATM 3274 O O3P   . FAD   B 2 .   ? -16.021 0.872   -9.739  1.00 20.35 ? 501 FAD   A O3P   1 
HETATM 3275 C C4    . A1ITD C 3 .   ? -14.974 21.870  -16.034 1.00 52.10 ? 502 A1ITD A C4    1 
HETATM 3276 C C14   . A1ITD C 3 .   ? -11.284 19.733  -14.659 1.00 71.33 ? 502 A1ITD A C14   1 
HETATM 3277 C C5    . A1ITD C 3 .   ? -14.085 20.941  -15.608 1.00 55.62 ? 502 A1ITD A C5    1 
HETATM 3278 C C6    . A1ITD C 3 .   ? -12.875 20.645  -16.320 1.00 62.61 ? 502 A1ITD A C6    1 
HETATM 3279 C C11   . A1ITD C 3 .   ? -10.279 17.565  -14.966 1.00 73.68 ? 502 A1ITD A C11   1 
HETATM 3280 C C7    . A1ITD C 3 .   ? -11.985 19.565  -15.856 1.00 69.77 ? 502 A1ITD A C7    1 
HETATM 3281 C C8    . A1ITD C 3 .   ? -11.797 18.396  -16.601 1.00 67.31 ? 502 A1ITD A C8    1 
HETATM 3282 C C9    . A1ITD C 3 .   ? -10.965 17.382  -16.171 1.00 73.43 ? 502 A1ITD A C9    1 
HETATM 3283 C C10   . A1ITD C 3 .   ? -10.786 16.135  -16.996 1.00 79.69 ? 502 A1ITD A C10   1 
HETATM 3284 C C12   . A1ITD C 3 .   ? -10.425 18.735  -14.197 1.00 73.77 ? 502 A1ITD A C12   1 
HETATM 3285 C C13   . A1ITD C 3 .   ? -9.674  18.919  -12.907 1.00 74.16 ? 502 A1ITD A C13   1 
HETATM 3286 O O1    . A1ITD C 3 .   ? -12.577 21.268  -17.329 1.00 79.62 ? 502 A1ITD A O1    1 
HETATM 3287 O O2    . A1ITD C 3 .   ? -9.451  16.623  -14.508 1.00 75.59 ? 502 A1ITD A O2    1 
HETATM 3288 O O3    . A1ITD C 3 .   ? -11.439 20.861  -13.922 1.00 83.58 ? 502 A1ITD A O3    1 
HETATM 3289 O O     . HOH   D 4 .   ? -4.889  24.818  -11.233 1.00 35.43 ? 601 HOH   A O     1 
HETATM 3290 O O     . HOH   D 4 .   ? -1.045  4.073   -0.299  1.00 40.25 ? 602 HOH   A O     1 
HETATM 3291 O O     . HOH   D 4 .   ? -12.715 -14.312 -17.564 1.00 41.55 ? 603 HOH   A O     1 
HETATM 3292 O O     . HOH   D 4 .   ? -6.300  30.727  -8.427  1.00 32.34 ? 604 HOH   A O     1 
HETATM 3293 O O     . HOH   D 4 .   ? -21.726 -1.307  -24.295 1.00 38.78 ? 605 HOH   A O     1 
HETATM 3294 O O     . HOH   D 4 .   ? -34.123 -6.945  6.124   1.00 42.69 ? 606 HOH   A O     1 
HETATM 3295 O O     . HOH   D 4 .   ? -23.943 23.986  -23.718 1.00 36.81 ? 607 HOH   A O     1 
HETATM 3296 O O     . HOH   D 4 .   ? -1.949  7.231   -22.716 1.00 41.02 ? 608 HOH   A O     1 
HETATM 3297 O O     . HOH   D 4 .   ? 10.034  13.034  -20.186 1.00 37.72 ? 609 HOH   A O     1 
HETATM 3298 O O     . HOH   D 4 .   ? -28.945 -10.590 -19.887 1.00 31.97 ? 610 HOH   A O     1 
HETATM 3299 O O     . HOH   D 4 .   ? -21.661 16.578  -2.353  1.00 43.85 ? 611 HOH   A O     1 
HETATM 3300 O O     . HOH   D 4 .   ? -5.292  6.243   5.742   1.00 42.11 ? 612 HOH   A O     1 
HETATM 3301 O O     . HOH   D 4 .   ? -27.347 8.276   9.611   1.00 27.55 ? 613 HOH   A O     1 
HETATM 3302 O O     . HOH   D 4 .   ? -27.690 -3.803  -17.467 1.00 40.84 ? 614 HOH   A O     1 
HETATM 3303 O O     . HOH   D 4 .   ? -39.421 7.472   -4.429  1.00 43.09 ? 615 HOH   A O     1 
HETATM 3304 O O     . HOH   D 4 .   ? -20.989 13.482  -27.428 1.00 31.89 ? 616 HOH   A O     1 
HETATM 3305 O O     . HOH   D 4 .   ? -19.609 22.725  -28.957 1.00 31.16 ? 617 HOH   A O     1 
HETATM 3306 O O     . HOH   D 4 .   ? -14.706 -2.479  -13.119 1.00 30.53 ? 618 HOH   A O     1 
HETATM 3307 O O     . HOH   D 4 .   ? -12.641 3.487   14.411  1.00 39.66 ? 619 HOH   A O     1 
HETATM 3308 O O     . HOH   D 4 .   ? -22.730 1.828   -28.706 1.00 41.79 ? 620 HOH   A O     1 
HETATM 3309 O O     . HOH   D 4 .   ? -3.868  -0.228  -31.279 1.00 47.89 ? 621 HOH   A O     1 
HETATM 3310 O O     . HOH   D 4 .   ? -31.679 2.645   -20.804 1.00 39.31 ? 622 HOH   A O     1 
HETATM 3311 O O     . HOH   D 4 .   ? 10.493  25.432  -26.153 1.00 42.34 ? 623 HOH   A O     1 
HETATM 3312 O O     . HOH   D 4 .   ? -18.704 1.722   -29.694 1.00 28.60 ? 624 HOH   A O     1 
HETATM 3313 O O     . HOH   D 4 .   ? -13.803 -18.272 -4.130  1.00 36.90 ? 625 HOH   A O     1 
HETATM 3314 O O     . HOH   D 4 .   ? -31.273 19.719  4.183   1.00 32.29 ? 626 HOH   A O     1 
HETATM 3315 O O     . HOH   D 4 .   ? -35.234 6.791   -8.108  1.00 27.45 ? 627 HOH   A O     1 
HETATM 3316 O O     . HOH   D 4 .   ? -17.479 -3.592  -13.862 1.00 23.01 ? 628 HOH   A O     1 
HETATM 3317 O O     . HOH   D 4 .   ? -33.934 11.424  -15.918 1.00 38.70 ? 629 HOH   A O     1 
HETATM 3318 O O     . HOH   D 4 .   ? -23.576 24.756  -34.708 1.00 42.42 ? 630 HOH   A O     1 
HETATM 3319 O O     . HOH   D 4 .   ? -29.515 10.010  -20.858 1.00 37.32 ? 631 HOH   A O     1 
HETATM 3320 O O     . HOH   D 4 .   ? -23.391 -10.746 3.107   1.00 26.24 ? 632 HOH   A O     1 
HETATM 3321 O O     . HOH   D 4 .   ? -33.658 12.484  -8.234  1.00 24.78 ? 633 HOH   A O     1 
HETATM 3322 O O     . HOH   D 4 .   ? -23.488 -5.857  -16.800 1.00 45.43 ? 634 HOH   A O     1 
HETATM 3323 O O     . HOH   D 4 .   ? -24.813 -3.991  -17.429 1.00 48.31 ? 635 HOH   A O     1 
HETATM 3324 O O     . HOH   D 4 .   ? 5.713   30.300  -20.573 1.00 46.10 ? 636 HOH   A O     1 
HETATM 3325 O O     . HOH   D 4 .   ? -9.320  32.854  -28.930 1.00 32.83 ? 637 HOH   A O     1 
HETATM 3326 O O     . HOH   D 4 .   ? -4.471  29.422  -7.323  1.00 44.65 ? 638 HOH   A O     1 
HETATM 3327 O O     . HOH   D 4 .   ? -19.350 -7.559  -13.091 1.00 28.59 ? 639 HOH   A O     1 
HETATM 3328 O O     . HOH   D 4 .   ? -27.571 5.356   -15.404 1.00 21.09 ? 640 HOH   A O     1 
HETATM 3329 O O     . HOH   D 4 .   ? -16.798 6.174   -17.384 1.00 28.47 ? 641 HOH   A O     1 
HETATM 3330 O O     . HOH   D 4 .   ? -18.968 6.596   -10.264 1.00 35.33 ? 642 HOH   A O     1 
HETATM 3331 O O     . HOH   D 4 .   ? -17.571 7.376   -13.959 1.00 21.98 ? 643 HOH   A O     1 
HETATM 3332 O O     . HOH   D 4 .   ? -17.557 19.104  -34.927 1.00 45.59 ? 644 HOH   A O     1 
HETATM 3333 O O     . HOH   D 4 .   ? -34.112 -3.656  -18.889 1.00 42.49 ? 645 HOH   A O     1 
HETATM 3334 O O     . HOH   D 4 .   ? -20.626 11.338  -19.587 1.00 21.28 ? 646 HOH   A O     1 
HETATM 3335 O O     . HOH   D 4 .   ? -1.283  9.201   -5.692  1.00 31.08 ? 647 HOH   A O     1 
HETATM 3336 O O     . HOH   D 4 .   ? -15.885 1.273   -13.558 1.00 19.43 ? 648 HOH   A O     1 
HETATM 3337 O O     . HOH   D 4 .   ? -6.919  33.543  -11.620 1.00 46.80 ? 649 HOH   A O     1 
HETATM 3338 O O     . HOH   D 4 .   ? -8.013  -6.664  2.471   1.00 34.34 ? 650 HOH   A O     1 
HETATM 3339 O O     . HOH   D 4 .   ? -17.768 -8.979  7.404   1.00 36.05 ? 651 HOH   A O     1 
HETATM 3340 O O     . HOH   D 4 .   ? -5.374  -1.199  -6.540  1.00 41.35 ? 652 HOH   A O     1 
HETATM 3341 O O     . HOH   D 4 .   ? 13.216  23.881  -16.015 1.00 35.67 ? 653 HOH   A O     1 
HETATM 3342 O O     . HOH   D 4 .   ? -16.436 0.075   -6.049  1.00 18.50 ? 654 HOH   A O     1 
HETATM 3343 O O     . HOH   D 4 .   ? -10.770 -2.055  -6.857  1.00 29.72 ? 655 HOH   A O     1 
HETATM 3344 O O     . HOH   D 4 .   ? -17.074 14.322  -15.094 1.00 22.14 ? 656 HOH   A O     1 
HETATM 3345 O O     . HOH   D 4 .   ? -20.422 -3.658  13.241  1.00 41.07 ? 657 HOH   A O     1 
HETATM 3346 O O     . HOH   D 4 .   ? -17.330 12.331  -24.850 1.00 32.05 ? 658 HOH   A O     1 
HETATM 3347 O O     . HOH   D 4 .   ? -17.789 28.399  -6.670  1.00 40.09 ? 659 HOH   A O     1 
HETATM 3348 O O     . HOH   D 4 .   ? -28.121 14.053  -4.524  1.00 32.50 ? 660 HOH   A O     1 
HETATM 3349 O O     . HOH   D 4 .   ? -32.635 -11.085 -11.663 1.00 31.10 ? 661 HOH   A O     1 
HETATM 3350 O O     . HOH   D 4 .   ? 1.030   18.301  -33.423 1.00 29.68 ? 662 HOH   A O     1 
HETATM 3351 O O     . HOH   D 4 .   ? -8.588  17.307  -33.557 1.00 31.72 ? 663 HOH   A O     1 
HETATM 3352 O O     . HOH   D 4 .   ? -25.220 4.038   -22.633 1.00 20.27 ? 664 HOH   A O     1 
HETATM 3353 O O     . HOH   D 4 .   ? 4.985   12.045  -32.892 1.00 45.68 ? 665 HOH   A O     1 
HETATM 3354 O O     . HOH   D 4 .   ? -18.845 -10.000 -13.917 1.00 30.24 ? 666 HOH   A O     1 
HETATM 3355 O O     . HOH   D 4 .   ? 3.231   17.672  -31.508 1.00 34.11 ? 667 HOH   A O     1 
HETATM 3356 O O     . HOH   D 4 .   ? -1.540  25.974  -28.000 1.00 21.35 ? 668 HOH   A O     1 
HETATM 3357 O O     . HOH   D 4 .   ? -17.367 13.502  9.378   1.00 41.99 ? 669 HOH   A O     1 
HETATM 3358 O O     . HOH   D 4 .   ? -11.066 14.449  -14.479 1.00 34.25 ? 670 HOH   A O     1 
HETATM 3359 O O     . HOH   D 4 .   ? -23.907 -2.637  -26.194 1.00 56.03 ? 671 HOH   A O     1 
HETATM 3360 O O     . HOH   D 4 .   ? -13.607 8.045   -11.851 1.00 24.72 ? 672 HOH   A O     1 
HETATM 3361 O O     . HOH   D 4 .   ? 1.471   21.096  -37.382 1.00 45.94 ? 673 HOH   A O     1 
HETATM 3362 O O     . HOH   D 4 .   ? -6.188  0.987   -8.454  1.00 33.96 ? 674 HOH   A O     1 
HETATM 3363 O O     . HOH   D 4 .   ? -23.889 -14.354 -15.613 1.00 24.97 ? 675 HOH   A O     1 
HETATM 3364 O O     . HOH   D 4 .   ? -24.982 15.916  -23.105 1.00 40.37 ? 676 HOH   A O     1 
HETATM 3365 O O     . HOH   D 4 .   ? -23.604 10.379  10.751  1.00 34.21 ? 677 HOH   A O     1 
HETATM 3366 O O     . HOH   D 4 .   ? -23.394 20.672  -14.567 1.00 41.16 ? 678 HOH   A O     1 
HETATM 3367 O O     . HOH   D 4 .   ? -37.360 -0.184  -8.904  1.00 33.51 ? 679 HOH   A O     1 
HETATM 3368 O O     . HOH   D 4 .   ? -25.731 -3.781  11.133  1.00 27.92 ? 680 HOH   A O     1 
HETATM 3369 O O     . HOH   D 4 .   ? -32.761 -10.876 -7.833  1.00 46.64 ? 681 HOH   A O     1 
HETATM 3370 O O     . HOH   D 4 .   ? -30.515 -12.655 -10.330 1.00 27.60 ? 682 HOH   A O     1 
HETATM 3371 O O     . HOH   D 4 .   ? -12.744 -14.958 -8.907  1.00 33.88 ? 683 HOH   A O     1 
HETATM 3372 O O     . HOH   D 4 .   ? -0.063  23.955  -17.228 1.00 24.90 ? 684 HOH   A O     1 
HETATM 3373 O O     . HOH   D 4 .   ? -9.458  3.290   10.914  1.00 38.58 ? 685 HOH   A O     1 
HETATM 3374 O O     . HOH   D 4 .   ? -31.467 -8.416  -8.370  1.00 24.69 ? 686 HOH   A O     1 
HETATM 3375 O O     . HOH   D 4 .   ? -3.172  16.300  -0.063  1.00 44.22 ? 687 HOH   A O     1 
HETATM 3376 O O     . HOH   D 4 .   ? -30.610 -19.739 0.755   1.00 45.55 ? 688 HOH   A O     1 
HETATM 3377 O O     . HOH   D 4 .   ? -35.462 -14.576 -6.343  1.00 47.28 ? 689 HOH   A O     1 
HETATM 3378 O O     . HOH   D 4 .   ? -19.717 0.828   -9.128  1.00 18.71 ? 690 HOH   A O     1 
HETATM 3379 O O     . HOH   D 4 .   ? -17.820 8.866   10.303  1.00 41.81 ? 691 HOH   A O     1 
HETATM 3380 O O     . HOH   D 4 .   ? -24.264 14.987  -25.870 1.00 42.32 ? 692 HOH   A O     1 
HETATM 3381 O O     . HOH   D 4 .   ? -5.514  19.796  -35.406 1.00 29.89 ? 693 HOH   A O     1 
HETATM 3382 O O     . HOH   D 4 .   ? -15.858 -5.406  -15.369 1.00 33.46 ? 694 HOH   A O     1 
HETATM 3383 O O     . HOH   D 4 .   ? -38.440 13.155  8.855   1.00 30.40 ? 695 HOH   A O     1 
HETATM 3384 O O     . HOH   D 4 .   ? -16.083 25.040  -7.262  1.00 32.35 ? 696 HOH   A O     1 
HETATM 3385 O O     . HOH   D 4 .   ? -20.422 -14.415 3.391   1.00 38.22 ? 697 HOH   A O     1 
HETATM 3386 O O     . HOH   D 4 .   ? -22.782 12.965  7.618   1.00 45.14 ? 698 HOH   A O     1 
HETATM 3387 O O     . HOH   D 4 .   ? -16.726 -11.391 5.935   1.00 37.69 ? 699 HOH   A O     1 
HETATM 3388 O O     . HOH   D 4 .   ? -26.552 7.372   -16.924 1.00 21.06 ? 700 HOH   A O     1 
HETATM 3389 O O     . HOH   D 4 .   ? 8.785   23.517  -28.291 1.00 51.49 ? 701 HOH   A O     1 
HETATM 3390 O O     . HOH   D 4 .   ? -22.679 6.557   -26.143 1.00 26.88 ? 702 HOH   A O     1 
HETATM 3391 O O     . HOH   D 4 .   ? -16.451 -16.647 -6.935  1.00 29.51 ? 703 HOH   A O     1 
HETATM 3392 O O     . HOH   D 4 .   ? -17.876 14.598  -24.923 1.00 32.59 ? 704 HOH   A O     1 
HETATM 3393 O O     . HOH   D 4 .   ? -25.411 -17.725 -10.585 1.00 30.21 ? 705 HOH   A O     1 
HETATM 3394 O O     . HOH   D 4 .   ? -8.348  -4.583  -16.164 1.00 49.69 ? 706 HOH   A O     1 
HETATM 3395 O O     . HOH   D 4 .   ? 1.174   -1.271  0.086   1.00 42.82 ? 707 HOH   A O     1 
HETATM 3396 O O     . HOH   D 4 .   ? -35.826 -0.420  -3.486  1.00 22.59 ? 708 HOH   A O     1 
HETATM 3397 O O     . HOH   D 4 .   ? -10.562 11.978  -13.210 1.00 31.61 ? 709 HOH   A O     1 
HETATM 3398 O O     . HOH   D 4 .   ? -2.403  27.386  -34.559 1.00 37.34 ? 710 HOH   A O     1 
HETATM 3399 O O     . HOH   D 4 .   ? -13.872 -3.553  -26.482 1.00 41.71 ? 711 HOH   A O     1 
HETATM 3400 O O     . HOH   D 4 .   ? -18.769 -1.254  -30.736 1.00 50.60 ? 712 HOH   A O     1 
HETATM 3401 O O     . HOH   D 4 .   ? -20.370 -10.523 -15.997 1.00 39.27 ? 713 HOH   A O     1 
HETATM 3402 O O     . HOH   D 4 .   ? -2.451  26.913  -25.596 1.00 22.99 ? 714 HOH   A O     1 
HETATM 3403 O O     . HOH   D 4 .   ? -12.046 1.006   -12.602 1.00 22.38 ? 715 HOH   A O     1 
HETATM 3404 O O     . HOH   D 4 .   ? -17.506 23.743  -3.393  1.00 26.88 ? 716 HOH   A O     1 
HETATM 3405 O O     . HOH   D 4 .   ? -24.615 24.114  -6.683  1.00 46.79 ? 717 HOH   A O     1 
HETATM 3406 O O     . HOH   D 4 .   ? -24.113 1.075   17.190  1.00 41.09 ? 718 HOH   A O     1 
HETATM 3407 O O     . HOH   D 4 .   ? -13.529 0.690   -14.959 1.00 28.99 ? 719 HOH   A O     1 
HETATM 3408 O O     . HOH   D 4 .   ? -20.645 -13.231 -13.013 1.00 24.73 ? 720 HOH   A O     1 
HETATM 3409 O O     . HOH   D 4 .   ? -34.183 9.019   9.237   1.00 29.03 ? 721 HOH   A O     1 
HETATM 3410 O O     . HOH   D 4 .   ? -14.452 21.162  -34.123 1.00 34.50 ? 722 HOH   A O     1 
HETATM 3411 O O     . HOH   D 4 .   ? -3.440  29.554  -26.159 1.00 29.18 ? 723 HOH   A O     1 
HETATM 3412 O O     . HOH   D 4 .   ? -23.612 6.153   -23.734 1.00 22.06 ? 724 HOH   A O     1 
HETATM 3413 O O     . HOH   D 4 .   ? -27.758 19.003  -1.836  1.00 43.37 ? 725 HOH   A O     1 
HETATM 3414 O O     . HOH   D 4 .   ? -15.508 9.522   -14.880 1.00 32.93 ? 726 HOH   A O     1 
HETATM 3415 O O     . HOH   D 4 .   ? -17.176 -1.349  -28.040 1.00 35.65 ? 727 HOH   A O     1 
HETATM 3416 O O     . HOH   D 4 .   ? -31.035 13.766  -7.613  1.00 22.09 ? 728 HOH   A O     1 
HETATM 3417 O O     . HOH   D 4 .   ? -19.369 -1.209  -21.605 1.00 29.60 ? 729 HOH   A O     1 
HETATM 3418 O O     . HOH   D 4 .   ? -25.446 27.279  -12.085 1.00 56.80 ? 730 HOH   A O     1 
HETATM 3419 O O     . HOH   D 4 .   ? -19.067 -2.992  10.759  1.00 28.48 ? 731 HOH   A O     1 
HETATM 3420 O O     . HOH   D 4 .   ? -27.488 -4.323  -21.517 1.00 44.00 ? 732 HOH   A O     1 
HETATM 3421 O O     . HOH   D 4 .   ? -22.345 -21.550 -0.007  1.00 34.44 ? 733 HOH   A O     1 
HETATM 3422 O O     . HOH   D 4 .   ? -26.273 12.496  9.682   1.00 30.43 ? 734 HOH   A O     1 
HETATM 3423 O O     . HOH   D 4 .   ? -32.594 8.993   -16.984 1.00 38.66 ? 735 HOH   A O     1 
HETATM 3424 O O     . HOH   D 4 .   ? -38.827 -3.382  9.709   1.00 40.82 ? 736 HOH   A O     1 
HETATM 3425 O O     . HOH   D 4 .   ? -18.510 34.162  -16.576 1.00 39.43 ? 737 HOH   A O     1 
HETATM 3426 O O     . HOH   D 4 .   ? -19.897 8.766   -12.337 1.00 32.14 ? 738 HOH   A O     1 
HETATM 3427 O O     . HOH   D 4 .   ? -20.664 34.980  -28.010 1.00 39.41 ? 739 HOH   A O     1 
HETATM 3428 O O     . HOH   D 4 .   ? -24.714 7.727   10.406  1.00 32.39 ? 740 HOH   A O     1 
HETATM 3429 O O     . HOH   D 4 .   ? -2.236  2.755   8.902   1.00 42.09 ? 741 HOH   A O     1 
HETATM 3430 O O     . HOH   D 4 .   ? -12.101 34.676  -16.237 1.00 36.19 ? 742 HOH   A O     1 
HETATM 3431 O O     . HOH   D 4 .   ? -0.463  24.656  -36.478 1.00 40.92 ? 743 HOH   A O     1 
HETATM 3432 O O     . HOH   D 4 .   ? 1.119   26.441  -4.253  1.00 47.42 ? 744 HOH   A O     1 
HETATM 3433 O O     . HOH   D 4 .   ? -15.453 4.648   -15.662 1.00 26.66 ? 745 HOH   A O     1 
HETATM 3434 O O     . HOH   D 4 .   ? 7.742   4.861   -26.173 1.00 38.42 ? 746 HOH   A O     1 
HETATM 3435 O O     . HOH   D 4 .   ? 1.100   12.561  -3.895  1.00 42.34 ? 747 HOH   A O     1 
HETATM 3436 O O     . HOH   D 4 .   ? -24.776 27.799  -29.476 1.00 41.40 ? 748 HOH   A O     1 
HETATM 3437 O O     . HOH   D 4 .   ? -5.846  34.955  -29.743 1.00 46.53 ? 749 HOH   A O     1 
HETATM 3438 O O     . HOH   D 4 .   ? 11.770  28.066  -19.824 1.00 44.20 ? 750 HOH   A O     1 
HETATM 3439 O O     . HOH   D 4 .   ? -10.509 14.753  -33.611 1.00 41.78 ? 751 HOH   A O     1 
HETATM 3440 O O     . HOH   D 4 .   ? -15.536 -14.381 -17.559 1.00 33.27 ? 752 HOH   A O     1 
HETATM 3441 O O     . HOH   D 4 .   ? -13.276 -10.880 -28.299 1.00 44.05 ? 753 HOH   A O     1 
HETATM 3442 O O     . HOH   D 4 .   ? 0.285   25.090  -20.563 1.00 31.23 ? 754 HOH   A O     1 
HETATM 3443 O O     . HOH   D 4 .   ? -3.618  30.980  -19.316 1.00 49.04 ? 755 HOH   A O     1 
HETATM 3444 O O     . HOH   D 4 .   ? -18.123 17.263  4.815   1.00 32.94 ? 756 HOH   A O     1 
HETATM 3445 O O     . HOH   D 4 .   ? -38.510 -1.818  -5.551  1.00 42.36 ? 757 HOH   A O     1 
HETATM 3446 O O     . HOH   D 4 .   ? -8.890  -4.832  4.033   1.00 41.03 ? 758 HOH   A O     1 
HETATM 3447 O O     . HOH   D 4 .   ? -9.886  -2.327  -26.263 1.00 35.03 ? 759 HOH   A O     1 
HETATM 3448 O O     . HOH   D 4 .   ? 9.308   13.416  -22.961 1.00 32.31 ? 760 HOH   A O     1 
HETATM 3449 O O     . HOH   D 4 .   ? -39.441 -9.110  5.457   1.00 44.14 ? 761 HOH   A O     1 
HETATM 3450 O O     . HOH   D 4 .   ? -14.855 30.639  -11.909 1.00 29.96 ? 762 HOH   A O     1 
HETATM 3451 O O     . HOH   D 4 .   ? -0.175  1.472   6.561   1.00 43.85 ? 763 HOH   A O     1 
HETATM 3452 O O     . HOH   D 4 .   ? -35.419 -7.776  -3.352  1.00 32.12 ? 764 HOH   A O     1 
HETATM 3453 O O     . HOH   D 4 .   ? -20.148 -12.538 5.712   1.00 43.34 ? 765 HOH   A O     1 
HETATM 3454 O O     . HOH   D 4 .   ? -39.239 4.968   -0.226  1.00 30.81 ? 766 HOH   A O     1 
HETATM 3455 O O     . HOH   D 4 .   ? -6.625  22.800  -5.748  1.00 35.73 ? 767 HOH   A O     1 
HETATM 3456 O O     . HOH   D 4 .   ? -21.166 23.638  -0.905  1.00 48.39 ? 768 HOH   A O     1 
HETATM 3457 O O     . HOH   D 4 .   ? -10.859 -2.508  -28.836 1.00 32.23 ? 769 HOH   A O     1 
HETATM 3458 O O     . HOH   D 4 .   ? -21.617 -1.470  -19.468 1.00 30.07 ? 770 HOH   A O     1 
HETATM 3459 O O     . HOH   D 4 .   ? -26.301 21.220  -6.926  1.00 42.78 ? 771 HOH   A O     1 
HETATM 3460 O O     . HOH   D 4 .   ? -36.811 5.738   -5.999  1.00 33.14 ? 772 HOH   A O     1 
HETATM 3461 O O     . HOH   D 4 .   ? -1.668  7.590   -36.770 1.00 33.38 ? 773 HOH   A O     1 
HETATM 3462 O O     . HOH   D 4 .   ? -16.298 -7.733  -16.398 1.00 40.06 ? 774 HOH   A O     1 
HETATM 3463 O O     . HOH   D 4 .   ? -15.482 17.699  -31.462 1.00 40.61 ? 775 HOH   A O     1 
HETATM 3464 O O     . HOH   D 4 .   ? -20.305 1.344   -27.461 1.00 29.50 ? 776 HOH   A O     1 
HETATM 3465 O O     . HOH   D 4 .   ? -14.744 14.111  -8.452  1.00 25.17 ? 777 HOH   A O     1 
HETATM 3466 O O     . HOH   D 4 .   ? -16.510 -7.971  -22.939 1.00 36.63 ? 778 HOH   A O     1 
HETATM 3467 O O     . HOH   D 4 .   ? -19.801 -17.390 -0.182  1.00 38.12 ? 779 HOH   A O     1 
HETATM 3468 O O     . HOH   D 4 .   ? -8.234  36.290  -11.407 1.00 36.69 ? 780 HOH   A O     1 
HETATM 3469 O O     . HOH   D 4 .   ? -8.159  24.767  -6.181  1.00 33.59 ? 781 HOH   A O     1 
HETATM 3470 O O     . HOH   D 4 .   ? -0.025  5.475   -21.957 1.00 39.17 ? 782 HOH   A O     1 
HETATM 3471 O O     . HOH   D 4 .   ? -8.097  -6.157  -9.019  1.00 41.91 ? 783 HOH   A O     1 
HETATM 3472 O O     . HOH   D 4 .   ? -22.218 20.782  2.695   1.00 46.50 ? 784 HOH   A O     1 
HETATM 3473 O O     . HOH   D 4 .   ? -11.217 -5.271  -14.873 1.00 38.70 ? 785 HOH   A O     1 
HETATM 3474 O O     . HOH   D 4 .   ? -24.572 32.738  -29.145 1.00 52.60 ? 786 HOH   A O     1 
HETATM 3475 O O     . HOH   D 4 .   ? -10.794 -13.559 1.142   1.00 33.57 ? 787 HOH   A O     1 
HETATM 3476 O O     . HOH   D 4 .   ? -23.697 -14.737 4.338   1.00 33.02 ? 788 HOH   A O     1 
HETATM 3477 O O     . HOH   D 4 .   ? -25.515 -5.412  -23.396 1.00 52.33 ? 789 HOH   A O     1 
HETATM 3478 O O     . HOH   D 4 .   ? -6.053  -6.263  -1.854  1.00 39.87 ? 790 HOH   A O     1 
HETATM 3479 O O     . HOH   D 4 .   ? 10.868  18.178  -12.207 1.00 35.89 ? 791 HOH   A O     1 
HETATM 3480 O O     . HOH   D 4 .   ? -32.136 6.873   -23.206 1.00 38.57 ? 792 HOH   A O     1 
HETATM 3481 O O     . HOH   D 4 .   ? -22.272 31.433  -15.083 1.00 41.93 ? 793 HOH   A O     1 
HETATM 3482 O O     . HOH   D 4 .   ? -24.012 4.369   -28.577 1.00 41.80 ? 794 HOH   A O     1 
HETATM 3483 O O     . HOH   D 4 .   ? -37.183 0.516   -5.513  1.00 46.42 ? 795 HOH   A O     1 
HETATM 3484 O O     . HOH   D 4 .   ? 2.069   1.256   -27.244 1.00 46.59 ? 796 HOH   A O     1 
HETATM 3485 O O     . HOH   D 4 .   ? -4.180  29.060  -10.669 1.00 37.45 ? 797 HOH   A O     1 
HETATM 3486 O O     . HOH   D 4 .   ? -14.845 -17.218 -14.147 1.00 41.17 ? 798 HOH   A O     1 
HETATM 3487 O O     . HOH   D 4 .   ? -15.421 22.158  0.358   1.00 35.24 ? 799 HOH   A O     1 
HETATM 3488 O O     . HOH   D 4 .   ? -0.513  28.320  -24.160 1.00 26.57 ? 800 HOH   A O     1 
HETATM 3489 O O     . HOH   D 4 .   ? -12.568 -4.291  -12.569 1.00 43.89 ? 801 HOH   A O     1 
HETATM 3490 O O     . HOH   D 4 .   ? -2.373  20.865  -0.072  1.00 47.92 ? 802 HOH   A O     1 
HETATM 3491 O O     . HOH   D 4 .   ? -18.725 -6.079  -22.242 1.00 39.74 ? 803 HOH   A O     1 
HETATM 3492 O O     . HOH   D 4 .   ? -18.641 35.534  -25.802 1.00 35.64 ? 804 HOH   A O     1 
HETATM 3493 O O     . HOH   D 4 .   ? -23.968 25.979  -26.060 1.00 49.42 ? 805 HOH   A O     1 
HETATM 3494 O O     . HOH   D 4 .   ? -43.822 14.577  7.893   1.00 62.08 ? 806 HOH   A O     1 
HETATM 3495 O O     . HOH   D 4 .   ? -14.127 3.241   -19.900 1.00 37.55 ? 807 HOH   A O     1 
HETATM 3496 O O     . HOH   D 4 .   ? -14.415 7.347   -15.286 1.00 30.86 ? 808 HOH   A O     1 
HETATM 3497 O O     . HOH   D 4 .   ? -36.086 6.879   -10.794 1.00 36.46 ? 809 HOH   A O     1 
HETATM 3498 O O     . HOH   D 4 .   ? -34.646 -7.992  -10.738 1.00 46.74 ? 810 HOH   A O     1 
HETATM 3499 O O     . HOH   D 4 .   ? -18.841 -5.211  9.499   1.00 31.58 ? 811 HOH   A O     1 
HETATM 3500 O O     . HOH   D 4 .   ? -21.047 -25.295 -5.375  1.00 56.93 ? 812 HOH   A O     1 
HETATM 3501 O O     . HOH   D 4 .   ? -8.539  34.311  -26.489 1.00 44.39 ? 813 HOH   A O     1 
HETATM 3502 O O     . HOH   D 4 .   ? -15.250 33.449  -11.005 1.00 45.06 ? 814 HOH   A O     1 
HETATM 3503 O O     . HOH   D 4 .   ? -24.727 25.681  -18.155 1.00 44.17 ? 815 HOH   A O     1 
HETATM 3504 O O     . HOH   D 4 .   ? -8.630  20.326  -2.005  1.00 49.86 ? 816 HOH   A O     1 
HETATM 3505 O O     . HOH   D 4 .   ? -33.030 -9.352  -14.875 1.00 45.43 ? 817 HOH   A O     1 
HETATM 3506 O O     . HOH   D 4 .   ? -16.710 26.045  -9.537  1.00 45.69 ? 818 HOH   A O     1 
HETATM 3507 O O     . HOH   D 4 .   ? 4.207   9.164   -19.683 1.00 42.06 ? 819 HOH   A O     1 
HETATM 3508 O O     . HOH   D 4 .   ? -11.220 36.042  -11.257 1.00 42.86 ? 820 HOH   A O     1 
HETATM 3509 O O     . HOH   D 4 .   ? -28.855 16.365  -2.954  1.00 45.79 ? 821 HOH   A O     1 
HETATM 3510 O O     . HOH   D 4 .   ? -40.082 0.133   -1.660  1.00 44.39 ? 822 HOH   A O     1 
HETATM 3511 O O     . HOH   D 4 .   ? -15.052 18.913  -33.765 1.00 34.33 ? 823 HOH   A O     1 
HETATM 3512 O O     . HOH   D 4 .   ? -26.042 25.647  -20.355 1.00 51.46 ? 824 HOH   A O     1 
HETATM 3513 O O     . HOH   D 4 .   ? -33.341 -10.016 -3.346  1.00 42.97 ? 825 HOH   A O     1 
HETATM 3514 O O     . HOH   D 4 .   ? 13.096  18.067  -6.542  1.00 44.06 ? 826 HOH   A O     1 
HETATM 3515 O O     . HOH   D 4 .   ? -3.619  -1.938  4.603   1.00 45.45 ? 827 HOH   A O     1 
HETATM 3516 O O     . HOH   D 4 .   ? 0.113   31.775  -19.717 1.00 39.37 ? 828 HOH   A O     1 
HETATM 3517 O O     . HOH   D 4 .   ? -15.527 24.829  -0.053  1.00 41.71 ? 829 HOH   A O     1 
HETATM 3518 O O     . HOH   D 4 .   ? -20.655 29.993  -9.772  1.00 49.34 ? 830 HOH   A O     1 
HETATM 3519 O O     . HOH   D 4 .   ? -20.124 8.365   12.158  1.00 52.30 ? 831 HOH   A O     1 
HETATM 3520 O O     . HOH   D 4 .   ? -18.566 16.522  7.229   1.00 38.07 ? 832 HOH   A O     1 
HETATM 3521 O O     . HOH   D 4 .   ? -35.045 2.502   14.978  1.00 47.06 ? 833 HOH   A O     1 
HETATM 3522 O O     . HOH   D 4 .   ? -18.937 25.208  -1.849  1.00 44.32 ? 834 HOH   A O     1 
HETATM 3523 O O     . HOH   D 4 .   ? -14.684 -16.976 -8.956  1.00 30.60 ? 835 HOH   A O     1 
HETATM 3524 O O     . HOH   D 4 .   ? -10.216 -2.828  -10.773 1.00 51.08 ? 836 HOH   A O     1 
HETATM 3525 O O     . HOH   D 4 .   ? -13.240 -18.373 -1.703  1.00 46.82 ? 837 HOH   A O     1 
HETATM 3526 O O     . HOH   D 4 .   ? -1.820  11.310  -10.936 1.00 51.09 ? 838 HOH   A O     1 
HETATM 3527 O O     . HOH   D 4 .   ? -40.818 12.834  10.182  1.00 45.49 ? 839 HOH   A O     1 
HETATM 3528 O O     . HOH   D 4 .   ? -29.616 -13.347 10.401  1.00 51.97 ? 840 HOH   A O     1 
HETATM 3529 O O     . HOH   D 4 .   ? -1.279  29.619  -19.636 1.00 38.22 ? 841 HOH   A O     1 
HETATM 3530 O O     . HOH   D 4 .   ? -35.853 7.326   10.747  1.00 46.19 ? 842 HOH   A O     1 
HETATM 3531 O O     . HOH   D 4 .   ? -15.439 25.409  -35.965 1.00 38.92 ? 843 HOH   A O     1 
HETATM 3532 O O     . HOH   D 4 .   ? -12.452 -19.693 -5.937  1.00 51.73 ? 844 HOH   A O     1 
HETATM 3533 O O     . HOH   D 4 .   ? 9.611   22.246  -10.611 1.00 52.65 ? 845 HOH   A O     1 
HETATM 3534 O O     . HOH   D 4 .   ? -13.929 2.646   -16.887 1.00 34.25 ? 846 HOH   A O     1 
HETATM 3535 O O     . HOH   D 4 .   ? -10.716 -1.573  -12.524 1.00 43.20 ? 847 HOH   A O     1 
HETATM 3536 O O     . HOH   D 4 .   ? -0.751  27.712  -21.326 1.00 35.21 ? 848 HOH   A O     1 
HETATM 3537 O O     . HOH   D 4 .   ? -22.201 3.251   17.075  1.00 50.50 ? 849 HOH   A O     1 
HETATM 3538 O O     . HOH   D 4 .   ? -9.890  -4.271  -30.540 1.00 36.25 ? 850 HOH   A O     1 
HETATM 3539 O O     . HOH   D 4 .   ? -24.664 6.379   12.924  1.00 44.74 ? 851 HOH   A O     1 
HETATM 3540 O O     . HOH   D 4 .   ? -15.268 3.642   15.222  1.00 50.60 ? 852 HOH   A O     1 
HETATM 3541 O O     . HOH   D 4 .   ? -0.421  16.007  -39.525 1.00 44.84 ? 853 HOH   A O     1 
HETATM 3542 O O     . HOH   D 4 .   ? -26.556 18.308  -23.658 1.00 42.71 ? 854 HOH   A O     1 
HETATM 3543 O O     . HOH   D 4 .   ? -23.348 14.770  6.475   1.00 37.50 ? 855 HOH   A O     1 
HETATM 3544 O O     . HOH   D 4 .   ? -43.844 -1.656  6.967   1.00 44.14 ? 856 HOH   A O     1 
HETATM 3545 O O     . HOH   D 4 .   ? -20.754 33.366  -14.831 1.00 46.05 ? 857 HOH   A O     1 
HETATM 3546 O O     . HOH   D 4 .   ? -14.185 -17.616 -11.898 1.00 37.14 ? 858 HOH   A O     1 
HETATM 3547 O O     . HOH   D 4 .   ? -15.588 21.554  3.171   1.00 45.27 ? 859 HOH   A O     1 
# 
