data_8RW0
# 
_entry.id   8RW0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   8RW0         pdb_00008rw0 10.2210/pdb8rw0/pdb 
WWPDB D_1292136152 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RW0 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-02 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              joerg.standfuss@psi.ch 
_pdbx_contact_author.name_first         Joerg 
_pdbx_contact_author.name_last          Standfuss 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8825-386X 
# 
_audit_author.name               'Glover, H.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0001-6558-8878 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                10837 
_citation.page_last                 10837 
_citation.title                     
'Photoswitch dissociation from a G protein-coupled receptor resolved by time-resolved serial crystallography.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-55109-w 
_citation.pdbx_database_id_PubMed   39738009 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Glover, H.'          1  0000-0001-6558-8878 
primary 'Sassmannshausen, T.' 2  ?                   
primary 'Bertrand, Q.'        3  0000-0003-3476-1775 
primary 'Trabuco, M.'         4  0000-0001-9234-8685 
primary 'Slavov, C.'          5  0000-0001-9441-0243 
primary 'Bacchin, A.'         6  ?                   
primary 'Andres, F.'          7  ?                   
primary 'Kondo, Y.'           8  0000-0003-2131-575X 
primary 'Stipp, R.'           9  ?                   
primary 'Wranik, M.'          10 ?                   
primary 'Khusainov, G.'       11 ?                   
primary 'Carrillo, M.'        12 0000-0002-0744-4486 
primary 'Kekilli, D.'         13 ?                   
primary 'Nan, J.'             14 ?                   
primary 'Gonzalez, A.'        15 0000-0001-8858-399X 
primary 'Cheng, R.'           16 0000-0001-7564-1230 
primary 'Neidhart, W.'        17 ?                   
primary 'Weinert, T.'         18 0000-0002-0339-3722 
primary 'Leonarski, F.'       19 ?                   
primary 'Dworkowski, F.'      20 0000-0001-5004-8684 
primary 'Kepa, M.'            21 0000-0002-4045-3990 
primary 'Wachtveitl, J.'      22 0000-0002-8496-8240 
primary 'Hennig, M.'          23 0000-0002-1839-2351 
primary 'Standfuss, J.'       24 0000-0001-8825-386X 
# 
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 'Adenosine receptor A2a,Soluble cytochrome b562'                                  49829.039 1   ? ? ? 
'A2A-StaR2-bRIL562 construct (A2A with bRIL insertion), with A277S revert mutation.' 
2 non-polymer syn '8-[(~{E})-2-(3,4-dimethoxyphenyl)ethenyl]-1,3-diethyl-7-methyl-purine-2,6-dione' 384.429   1   ? ? ? ? 
3 non-polymer syn CHOLESTEROL                                                                       386.654   3   ? ? ? ? 
4 non-polymer syn 'OLEIC ACID'                                                                      282.461   23  ? ? ? ? 
5 non-polymer syn 'SODIUM ION'                                                                      22.990    1   ? ? ? ? 
6 water       nat water                                                                             18.015    119 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytochrome b-562' 
# 
_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       
;MKTIIALSYIFCLVFADYKDDDDGAPPIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADILV
GVLAIPFAITISTGFCAACHGCLFIACFVLVLAQSSIFSLLAIAIDRYIAIAIPLRYNGLVTGTRAAGIIAICWVLSFAI
GLTPMLGWNNCGQPKEGKAHSQGCGEGQVACLFEDVVPMNYMVYFNFFACVLVPLLLMLGVYLRIFAAARRQLADLEDNW
ETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEA
QAAAEQLKTTRNAYIQKYLERARSTLQKEVHAAKSAAIIAGLFALCWLPLHIINCFTFFCPDCSHAPLWLMYLAIVLSHT
NSVVNPFIYAYRIREFRQTFRKIIRSHVLRQQEPFKAAAHHHHHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKTIIALSYIFCLVFADYKDDDDGAPPIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADILV
GVLAIPFAITISTGFCAACHGCLFIACFVLVLAQSSIFSLLAIAIDRYIAIAIPLRYNGLVTGTRAAGIIAICWVLSFAI
GLTPMLGWNNCGQPKEGKAHSQGCGEGQVACLFEDVVPMNYMVYFNFFACVLVPLLLMLGVYLRIFAAARRQLADLEDNW
ETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEA
QAAAEQLKTTRNAYIQKYLERARSTLQKEVHAAKSAAIIAGLFALCWLPLHIINCFTFFCPDCSHAPLWLMYLAIVLSHT
NSVVNPFIYAYRIREFRQTFRKIIRSHVLRQQEPFKAAAHHHHHHHHHH
;
_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 '8-[(~{E})-2-(3,4-dimethoxyphenyl)ethenyl]-1,3-diethyl-7-methyl-purine-2,6-dione' JQ9 
3 CHOLESTEROL                                                                       CLR 
4 'OLEIC ACID'                                                                      OLA 
5 'SODIUM ION'                                                                      NA  
6 water                                                                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   THR n 
1 4   ILE n 
1 5   ILE n 
1 6   ALA n 
1 7   LEU n 
1 8   SER n 
1 9   TYR n 
1 10  ILE n 
1 11  PHE n 
1 12  CYS n 
1 13  LEU n 
1 14  VAL n 
1 15  PHE n 
1 16  ALA n 
1 17  ASP n 
1 18  TYR n 
1 19  LYS n 
1 20  ASP n 
1 21  ASP n 
1 22  ASP n 
1 23  ASP n 
1 24  GLY n 
1 25  ALA n 
1 26  PRO n 
1 27  PRO n 
1 28  ILE n 
1 29  MET n 
1 30  GLY n 
1 31  SER n 
1 32  SER n 
1 33  VAL n 
1 34  TYR n 
1 35  ILE n 
1 36  THR n 
1 37  VAL n 
1 38  GLU n 
1 39  LEU n 
1 40  ALA n 
1 41  ILE n 
1 42  ALA n 
1 43  VAL n 
1 44  LEU n 
1 45  ALA n 
1 46  ILE n 
1 47  LEU n 
1 48  GLY n 
1 49  ASN n 
1 50  VAL n 
1 51  LEU n 
1 52  VAL n 
1 53  CYS n 
1 54  TRP n 
1 55  ALA n 
1 56  VAL n 
1 57  TRP n 
1 58  LEU n 
1 59  ASN n 
1 60  SER n 
1 61  ASN n 
1 62  LEU n 
1 63  GLN n 
1 64  ASN n 
1 65  VAL n 
1 66  THR n 
1 67  ASN n 
1 68  TYR n 
1 69  PHE n 
1 70  VAL n 
1 71  VAL n 
1 72  SER n 
1 73  LEU n 
1 74  ALA n 
1 75  ALA n 
1 76  ALA n 
1 77  ASP n 
1 78  ILE n 
1 79  LEU n 
1 80  VAL n 
1 81  GLY n 
1 82  VAL n 
1 83  LEU n 
1 84  ALA n 
1 85  ILE n 
1 86  PRO n 
1 87  PHE n 
1 88  ALA n 
1 89  ILE n 
1 90  THR n 
1 91  ILE n 
1 92  SER n 
1 93  THR n 
1 94  GLY n 
1 95  PHE n 
1 96  CYS n 
1 97  ALA n 
1 98  ALA n 
1 99  CYS n 
1 100 HIS n 
1 101 GLY n 
1 102 CYS n 
1 103 LEU n 
1 104 PHE n 
1 105 ILE n 
1 106 ALA n 
1 107 CYS n 
1 108 PHE n 
1 109 VAL n 
1 110 LEU n 
1 111 VAL n 
1 112 LEU n 
1 113 ALA n 
1 114 GLN n 
1 115 SER n 
1 116 SER n 
1 117 ILE n 
1 118 PHE n 
1 119 SER n 
1 120 LEU n 
1 121 LEU n 
1 122 ALA n 
1 123 ILE n 
1 124 ALA n 
1 125 ILE n 
1 126 ASP n 
1 127 ARG n 
1 128 TYR n 
1 129 ILE n 
1 130 ALA n 
1 131 ILE n 
1 132 ALA n 
1 133 ILE n 
1 134 PRO n 
1 135 LEU n 
1 136 ARG n 
1 137 TYR n 
1 138 ASN n 
1 139 GLY n 
1 140 LEU n 
1 141 VAL n 
1 142 THR n 
1 143 GLY n 
1 144 THR n 
1 145 ARG n 
1 146 ALA n 
1 147 ALA n 
1 148 GLY n 
1 149 ILE n 
1 150 ILE n 
1 151 ALA n 
1 152 ILE n 
1 153 CYS n 
1 154 TRP n 
1 155 VAL n 
1 156 LEU n 
1 157 SER n 
1 158 PHE n 
1 159 ALA n 
1 160 ILE n 
1 161 GLY n 
1 162 LEU n 
1 163 THR n 
1 164 PRO n 
1 165 MET n 
1 166 LEU n 
1 167 GLY n 
1 168 TRP n 
1 169 ASN n 
1 170 ASN n 
1 171 CYS n 
1 172 GLY n 
1 173 GLN n 
1 174 PRO n 
1 175 LYS n 
1 176 GLU n 
1 177 GLY n 
1 178 LYS n 
1 179 ALA n 
1 180 HIS n 
1 181 SER n 
1 182 GLN n 
1 183 GLY n 
1 184 CYS n 
1 185 GLY n 
1 186 GLU n 
1 187 GLY n 
1 188 GLN n 
1 189 VAL n 
1 190 ALA n 
1 191 CYS n 
1 192 LEU n 
1 193 PHE n 
1 194 GLU n 
1 195 ASP n 
1 196 VAL n 
1 197 VAL n 
1 198 PRO n 
1 199 MET n 
1 200 ASN n 
1 201 TYR n 
1 202 MET n 
1 203 VAL n 
1 204 TYR n 
1 205 PHE n 
1 206 ASN n 
1 207 PHE n 
1 208 PHE n 
1 209 ALA n 
1 210 CYS n 
1 211 VAL n 
1 212 LEU n 
1 213 VAL n 
1 214 PRO n 
1 215 LEU n 
1 216 LEU n 
1 217 LEU n 
1 218 MET n 
1 219 LEU n 
1 220 GLY n 
1 221 VAL n 
1 222 TYR n 
1 223 LEU n 
1 224 ARG n 
1 225 ILE n 
1 226 PHE n 
1 227 ALA n 
1 228 ALA n 
1 229 ALA n 
1 230 ARG n 
1 231 ARG n 
1 232 GLN n 
1 233 LEU n 
1 234 ALA n 
1 235 ASP n 
1 236 LEU n 
1 237 GLU n 
1 238 ASP n 
1 239 ASN n 
1 240 TRP n 
1 241 GLU n 
1 242 THR n 
1 243 LEU n 
1 244 ASN n 
1 245 ASP n 
1 246 ASN n 
1 247 LEU n 
1 248 LYS n 
1 249 VAL n 
1 250 ILE n 
1 251 GLU n 
1 252 LYS n 
1 253 ALA n 
1 254 ASP n 
1 255 ASN n 
1 256 ALA n 
1 257 ALA n 
1 258 GLN n 
1 259 VAL n 
1 260 LYS n 
1 261 ASP n 
1 262 ALA n 
1 263 LEU n 
1 264 THR n 
1 265 LYS n 
1 266 MET n 
1 267 ARG n 
1 268 ALA n 
1 269 ALA n 
1 270 ALA n 
1 271 LEU n 
1 272 ASP n 
1 273 ALA n 
1 274 GLN n 
1 275 LYS n 
1 276 ALA n 
1 277 THR n 
1 278 PRO n 
1 279 PRO n 
1 280 LYS n 
1 281 LEU n 
1 282 GLU n 
1 283 ASP n 
1 284 LYS n 
1 285 SER n 
1 286 PRO n 
1 287 ASP n 
1 288 SER n 
1 289 PRO n 
1 290 GLU n 
1 291 MET n 
1 292 LYS n 
1 293 ASP n 
1 294 PHE n 
1 295 ARG n 
1 296 HIS n 
1 297 GLY n 
1 298 PHE n 
1 299 ASP n 
1 300 ILE n 
1 301 LEU n 
1 302 VAL n 
1 303 GLY n 
1 304 GLN n 
1 305 ILE n 
1 306 ASP n 
1 307 ASP n 
1 308 ALA n 
1 309 LEU n 
1 310 LYS n 
1 311 LEU n 
1 312 ALA n 
1 313 ASN n 
1 314 GLU n 
1 315 GLY n 
1 316 LYS n 
1 317 VAL n 
1 318 LYS n 
1 319 GLU n 
1 320 ALA n 
1 321 GLN n 
1 322 ALA n 
1 323 ALA n 
1 324 ALA n 
1 325 GLU n 
1 326 GLN n 
1 327 LEU n 
1 328 LYS n 
1 329 THR n 
1 330 THR n 
1 331 ARG n 
1 332 ASN n 
1 333 ALA n 
1 334 TYR n 
1 335 ILE n 
1 336 GLN n 
1 337 LYS n 
1 338 TYR n 
1 339 LEU n 
1 340 GLU n 
1 341 ARG n 
1 342 ALA n 
1 343 ARG n 
1 344 SER n 
1 345 THR n 
1 346 LEU n 
1 347 GLN n 
1 348 LYS n 
1 349 GLU n 
1 350 VAL n 
1 351 HIS n 
1 352 ALA n 
1 353 ALA n 
1 354 LYS n 
1 355 SER n 
1 356 ALA n 
1 357 ALA n 
1 358 ILE n 
1 359 ILE n 
1 360 ALA n 
1 361 GLY n 
1 362 LEU n 
1 363 PHE n 
1 364 ALA n 
1 365 LEU n 
1 366 CYS n 
1 367 TRP n 
1 368 LEU n 
1 369 PRO n 
1 370 LEU n 
1 371 HIS n 
1 372 ILE n 
1 373 ILE n 
1 374 ASN n 
1 375 CYS n 
1 376 PHE n 
1 377 THR n 
1 378 PHE n 
1 379 PHE n 
1 380 CYS n 
1 381 PRO n 
1 382 ASP n 
1 383 CYS n 
1 384 SER n 
1 385 HIS n 
1 386 ALA n 
1 387 PRO n 
1 388 LEU n 
1 389 TRP n 
1 390 LEU n 
1 391 MET n 
1 392 TYR n 
1 393 LEU n 
1 394 ALA n 
1 395 ILE n 
1 396 VAL n 
1 397 LEU n 
1 398 SER n 
1 399 HIS n 
1 400 THR n 
1 401 ASN n 
1 402 SER n 
1 403 VAL n 
1 404 VAL n 
1 405 ASN n 
1 406 PRO n 
1 407 PHE n 
1 408 ILE n 
1 409 TYR n 
1 410 ALA n 
1 411 TYR n 
1 412 ARG n 
1 413 ILE n 
1 414 ARG n 
1 415 GLU n 
1 416 PHE n 
1 417 ARG n 
1 418 GLN n 
1 419 THR n 
1 420 PHE n 
1 421 ARG n 
1 422 LYS n 
1 423 ILE n 
1 424 ILE n 
1 425 ARG n 
1 426 SER n 
1 427 HIS n 
1 428 VAL n 
1 429 LEU n 
1 430 ARG n 
1 431 GLN n 
1 432 GLN n 
1 433 GLU n 
1 434 PRO n 
1 435 PHE n 
1 436 LYS n 
1 437 ALA n 
1 438 ALA n 
1 439 ALA n 
1 440 HIS n 
1 441 HIS n 
1 442 HIS n 
1 443 HIS n 
1 444 HIS n 
1 445 HIS n 
1 446 HIS n 
1 447 HIS n 
1 448 HIS n 
1 449 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1   233 human ? 'ADORA2A, ADORA2' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 234 339 human ? cybC              ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 3 sample 'Biological sequence' 340 449 human ? 'ADORA2A, ADORA2' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                           ?              
'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                                          ?              
'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                        ?              
'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                   ?              
'C4 H7 N O4'     133.103 
CLR non-polymer         . CHOLESTEROL                                                                       ?              
'C27 H46 O'      386.654 
CYS 'L-peptide linking' y CYSTEINE                                                                          ?              
'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                         ?              
'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                   ?              
'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                                           ?              
'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                         ?              
'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                                             ?              'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                        ?              
'C6 H13 N O2'    131.173 
JQ9 non-polymer         . '8-[(~{E})-2-(3,4-dimethoxyphenyl)ethenyl]-1,3-diethyl-7-methyl-purine-2,6-dione' istradefylline 
'C20 H24 N4 O4'  384.429 
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 
NA  non-polymer         . 'SODIUM ION'                                                                      ?              'Na 1' 
22.990  
OLA non-polymer         . 'OLEIC ACID'                                                                      ?              
'C18 H34 O2'     282.461 
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   -24  ?    ?   ?   A . n 
A 1 2   LYS 2   -23  ?    ?   ?   A . n 
A 1 3   THR 3   -22  ?    ?   ?   A . n 
A 1 4   ILE 4   -21  ?    ?   ?   A . n 
A 1 5   ILE 5   -20  ?    ?   ?   A . n 
A 1 6   ALA 6   -19  ?    ?   ?   A . n 
A 1 7   LEU 7   -18  ?    ?   ?   A . n 
A 1 8   SER 8   -17  ?    ?   ?   A . n 
A 1 9   TYR 9   -16  ?    ?   ?   A . n 
A 1 10  ILE 10  -15  ?    ?   ?   A . n 
A 1 11  PHE 11  -14  ?    ?   ?   A . n 
A 1 12  CYS 12  -13  ?    ?   ?   A . n 
A 1 13  LEU 13  -12  ?    ?   ?   A . n 
A 1 14  VAL 14  -11  ?    ?   ?   A . n 
A 1 15  PHE 15  -10  ?    ?   ?   A . n 
A 1 16  ALA 16  -9   ?    ?   ?   A . n 
A 1 17  ASP 17  -8   ?    ?   ?   A . n 
A 1 18  TYR 18  -7   ?    ?   ?   A . n 
A 1 19  LYS 19  -6   ?    ?   ?   A . n 
A 1 20  ASP 20  -5   ?    ?   ?   A . n 
A 1 21  ASP 21  -4   ?    ?   ?   A . n 
A 1 22  ASP 22  -3   ?    ?   ?   A . n 
A 1 23  ASP 23  -2   ?    ?   ?   A . n 
A 1 24  GLY 24  -1   ?    ?   ?   A . n 
A 1 25  ALA 25  0    0    ALA ALA A . n 
A 1 26  PRO 26  1    1    PRO PRO A . n 
A 1 27  PRO 27  2    2    PRO PRO A . n 
A 1 28  ILE 28  3    3    ILE ILE A . n 
A 1 29  MET 29  4    4    MET MET A . n 
A 1 30  GLY 30  5    5    GLY GLY A . n 
A 1 31  SER 31  6    6    SER SER A . n 
A 1 32  SER 32  7    7    SER SER A . n 
A 1 33  VAL 33  8    8    VAL VAL A . n 
A 1 34  TYR 34  9    9    TYR TYR A . n 
A 1 35  ILE 35  10   10   ILE ILE A . n 
A 1 36  THR 36  11   11   THR THR A . n 
A 1 37  VAL 37  12   12   VAL VAL A . n 
A 1 38  GLU 38  13   13   GLU GLU A . n 
A 1 39  LEU 39  14   14   LEU LEU A . n 
A 1 40  ALA 40  15   15   ALA ALA A . n 
A 1 41  ILE 41  16   16   ILE ILE A . n 
A 1 42  ALA 42  17   17   ALA ALA A . n 
A 1 43  VAL 43  18   18   VAL VAL A . n 
A 1 44  LEU 44  19   19   LEU LEU A . n 
A 1 45  ALA 45  20   20   ALA ALA A . n 
A 1 46  ILE 46  21   21   ILE ILE A . n 
A 1 47  LEU 47  22   22   LEU LEU A . n 
A 1 48  GLY 48  23   23   GLY GLY A . n 
A 1 49  ASN 49  24   24   ASN ASN A . n 
A 1 50  VAL 50  25   25   VAL VAL A . n 
A 1 51  LEU 51  26   26   LEU LEU A . n 
A 1 52  VAL 52  27   27   VAL VAL A . n 
A 1 53  CYS 53  28   28   CYS CYS A . n 
A 1 54  TRP 54  29   29   TRP TRP A . n 
A 1 55  ALA 55  30   30   ALA ALA A . n 
A 1 56  VAL 56  31   31   VAL VAL A . n 
A 1 57  TRP 57  32   32   TRP TRP A . n 
A 1 58  LEU 58  33   33   LEU LEU A . n 
A 1 59  ASN 59  34   34   ASN ASN A . n 
A 1 60  SER 60  35   35   SER SER A . n 
A 1 61  ASN 61  36   36   ASN ASN A . n 
A 1 62  LEU 62  37   37   LEU LEU A . n 
A 1 63  GLN 63  38   38   GLN GLN A . n 
A 1 64  ASN 64  39   39   ASN ASN A . n 
A 1 65  VAL 65  40   40   VAL VAL A . n 
A 1 66  THR 66  41   41   THR THR A . n 
A 1 67  ASN 67  42   42   ASN ASN A . n 
A 1 68  TYR 68  43   43   TYR TYR A . n 
A 1 69  PHE 69  44   44   PHE PHE A . n 
A 1 70  VAL 70  45   45   VAL VAL A . n 
A 1 71  VAL 71  46   46   VAL VAL A . n 
A 1 72  SER 72  47   47   SER SER A . n 
A 1 73  LEU 73  48   48   LEU LEU A . n 
A 1 74  ALA 74  49   49   ALA ALA A . n 
A 1 75  ALA 75  50   50   ALA ALA A . n 
A 1 76  ALA 76  51   51   ALA ALA A . n 
A 1 77  ASP 77  52   52   ASP ASP A . n 
A 1 78  ILE 78  53   53   ILE ILE A . n 
A 1 79  LEU 79  54   54   LEU LEU A . n 
A 1 80  VAL 80  55   55   VAL VAL A . n 
A 1 81  GLY 81  56   56   GLY GLY A . n 
A 1 82  VAL 82  57   57   VAL VAL A . n 
A 1 83  LEU 83  58   58   LEU LEU A . n 
A 1 84  ALA 84  59   59   ALA ALA A . n 
A 1 85  ILE 85  60   60   ILE ILE A . n 
A 1 86  PRO 86  61   61   PRO PRO A . n 
A 1 87  PHE 87  62   62   PHE PHE A . n 
A 1 88  ALA 88  63   63   ALA ALA A . n 
A 1 89  ILE 89  64   64   ILE ILE A . n 
A 1 90  THR 90  65   65   THR THR A . n 
A 1 91  ILE 91  66   66   ILE ILE A . n 
A 1 92  SER 92  67   67   SER SER A . n 
A 1 93  THR 93  68   68   THR THR A . n 
A 1 94  GLY 94  69   69   GLY GLY A . n 
A 1 95  PHE 95  70   70   PHE PHE A . n 
A 1 96  CYS 96  71   71   CYS CYS A . n 
A 1 97  ALA 97  72   72   ALA ALA A . n 
A 1 98  ALA 98  73   73   ALA ALA A . n 
A 1 99  CYS 99  74   74   CYS CYS A . n 
A 1 100 HIS 100 75   75   HIS HIS A . n 
A 1 101 GLY 101 76   76   GLY GLY A . n 
A 1 102 CYS 102 77   77   CYS CYS A . n 
A 1 103 LEU 103 78   78   LEU LEU A . n 
A 1 104 PHE 104 79   79   PHE PHE A . n 
A 1 105 ILE 105 80   80   ILE ILE A . n 
A 1 106 ALA 106 81   81   ALA ALA A . n 
A 1 107 CYS 107 82   82   CYS CYS A . n 
A 1 108 PHE 108 83   83   PHE PHE A . n 
A 1 109 VAL 109 84   84   VAL VAL A . n 
A 1 110 LEU 110 85   85   LEU LEU A . n 
A 1 111 VAL 111 86   86   VAL VAL A . n 
A 1 112 LEU 112 87   87   LEU LEU A . n 
A 1 113 ALA 113 88   88   ALA ALA A . n 
A 1 114 GLN 114 89   89   GLN GLN A . n 
A 1 115 SER 115 90   90   SER SER A . n 
A 1 116 SER 116 91   91   SER SER A . n 
A 1 117 ILE 117 92   92   ILE ILE A . n 
A 1 118 PHE 118 93   93   PHE PHE A . n 
A 1 119 SER 119 94   94   SER SER A . n 
A 1 120 LEU 120 95   95   LEU LEU A . n 
A 1 121 LEU 121 96   96   LEU LEU A . n 
A 1 122 ALA 122 97   97   ALA ALA A . n 
A 1 123 ILE 123 98   98   ILE ILE A . n 
A 1 124 ALA 124 99   99   ALA ALA A . n 
A 1 125 ILE 125 100  100  ILE ILE A . n 
A 1 126 ASP 126 101  101  ASP ASP A . n 
A 1 127 ARG 127 102  102  ARG ARG A . n 
A 1 128 TYR 128 103  103  TYR TYR A . n 
A 1 129 ILE 129 104  104  ILE ILE A . n 
A 1 130 ALA 130 105  105  ALA ALA A . n 
A 1 131 ILE 131 106  106  ILE ILE A . n 
A 1 132 ALA 132 107  107  ALA ALA A . n 
A 1 133 ILE 133 108  108  ILE ILE A . n 
A 1 134 PRO 134 109  109  PRO PRO A . n 
A 1 135 LEU 135 110  110  LEU LEU A . n 
A 1 136 ARG 136 111  111  ARG ARG A . n 
A 1 137 TYR 137 112  112  TYR TYR A . n 
A 1 138 ASN 138 113  113  ASN ASN A . n 
A 1 139 GLY 139 114  114  GLY GLY A . n 
A 1 140 LEU 140 115  115  LEU LEU A . n 
A 1 141 VAL 141 116  116  VAL VAL A . n 
A 1 142 THR 142 117  117  THR THR A . n 
A 1 143 GLY 143 118  118  GLY GLY A . n 
A 1 144 THR 144 119  119  THR THR A . n 
A 1 145 ARG 145 120  120  ARG ARG A . n 
A 1 146 ALA 146 121  121  ALA ALA A . n 
A 1 147 ALA 147 122  122  ALA ALA A . n 
A 1 148 GLY 148 123  123  GLY GLY A . n 
A 1 149 ILE 149 124  124  ILE ILE A . n 
A 1 150 ILE 150 125  125  ILE ILE A . n 
A 1 151 ALA 151 126  126  ALA ALA A . n 
A 1 152 ILE 152 127  127  ILE ILE A . n 
A 1 153 CYS 153 128  128  CYS CYS A . n 
A 1 154 TRP 154 129  129  TRP TRP A . n 
A 1 155 VAL 155 130  130  VAL VAL A . n 
A 1 156 LEU 156 131  131  LEU LEU A . n 
A 1 157 SER 157 132  132  SER SER A . n 
A 1 158 PHE 158 133  133  PHE PHE A . n 
A 1 159 ALA 159 134  134  ALA ALA A . n 
A 1 160 ILE 160 135  135  ILE ILE A . n 
A 1 161 GLY 161 136  136  GLY GLY A . n 
A 1 162 LEU 162 137  137  LEU LEU A . n 
A 1 163 THR 163 138  138  THR THR A . n 
A 1 164 PRO 164 139  139  PRO PRO A . n 
A 1 165 MET 165 140  140  MET MET A . n 
A 1 166 LEU 166 141  141  LEU LEU A . n 
A 1 167 GLY 167 142  142  GLY GLY A . n 
A 1 168 TRP 168 143  143  TRP TRP A . n 
A 1 169 ASN 169 144  144  ASN ASN A . n 
A 1 170 ASN 170 145  145  ASN ASN A . n 
A 1 171 CYS 171 146  146  CYS CYS A . n 
A 1 172 GLY 172 147  147  GLY GLY A . n 
A 1 173 GLN 173 148  148  GLN GLN A . n 
A 1 174 PRO 174 149  149  PRO PRO A . n 
A 1 175 LYS 175 150  150  LYS LYS A . n 
A 1 176 GLU 176 151  151  GLU GLU A . n 
A 1 177 GLY 177 152  152  GLY GLY A . n 
A 1 178 LYS 178 153  153  LYS LYS A . n 
A 1 179 ALA 179 154  154  ALA ALA A . n 
A 1 180 HIS 180 155  155  HIS HIS A . n 
A 1 181 SER 181 156  156  SER SER A . n 
A 1 182 GLN 182 157  157  GLN GLN A . n 
A 1 183 GLY 183 158  158  GLY GLY A . n 
A 1 184 CYS 184 159  159  CYS CYS A . n 
A 1 185 GLY 185 160  160  GLY GLY A . n 
A 1 186 GLU 186 161  161  GLU GLU A . n 
A 1 187 GLY 187 162  162  GLY GLY A . n 
A 1 188 GLN 188 163  163  GLN GLN A . n 
A 1 189 VAL 189 164  164  VAL VAL A . n 
A 1 190 ALA 190 165  165  ALA ALA A . n 
A 1 191 CYS 191 166  166  CYS CYS A . n 
A 1 192 LEU 192 167  167  LEU LEU A . n 
A 1 193 PHE 193 168  168  PHE PHE A . n 
A 1 194 GLU 194 169  169  GLU GLU A . n 
A 1 195 ASP 195 170  170  ASP ASP A . n 
A 1 196 VAL 196 171  171  VAL VAL A . n 
A 1 197 VAL 197 172  172  VAL VAL A . n 
A 1 198 PRO 198 173  173  PRO PRO A . n 
A 1 199 MET 199 174  174  MET MET A . n 
A 1 200 ASN 200 175  175  ASN ASN A . n 
A 1 201 TYR 201 176  176  TYR TYR A . n 
A 1 202 MET 202 177  177  MET MET A . n 
A 1 203 VAL 203 178  178  VAL VAL A . n 
A 1 204 TYR 204 179  179  TYR TYR A . n 
A 1 205 PHE 205 180  180  PHE PHE A . n 
A 1 206 ASN 206 181  181  ASN ASN A . n 
A 1 207 PHE 207 182  182  PHE PHE A . n 
A 1 208 PHE 208 183  183  PHE PHE A . n 
A 1 209 ALA 209 184  184  ALA ALA A . n 
A 1 210 CYS 210 185  185  CYS CYS A . n 
A 1 211 VAL 211 186  186  VAL VAL A . n 
A 1 212 LEU 212 187  187  LEU LEU A . n 
A 1 213 VAL 213 188  188  VAL VAL A . n 
A 1 214 PRO 214 189  189  PRO PRO A . n 
A 1 215 LEU 215 190  190  LEU LEU A . n 
A 1 216 LEU 216 191  191  LEU LEU A . n 
A 1 217 LEU 217 192  192  LEU LEU A . n 
A 1 218 MET 218 193  193  MET MET A . n 
A 1 219 LEU 219 194  194  LEU LEU A . n 
A 1 220 GLY 220 195  195  GLY GLY A . n 
A 1 221 VAL 221 196  196  VAL VAL A . n 
A 1 222 TYR 222 197  197  TYR TYR A . n 
A 1 223 LEU 223 198  198  LEU LEU A . n 
A 1 224 ARG 224 199  199  ARG ARG A . n 
A 1 225 ILE 225 200  200  ILE ILE A . n 
A 1 226 PHE 226 201  201  PHE PHE A . n 
A 1 227 ALA 227 202  202  ALA ALA A . n 
A 1 228 ALA 228 203  203  ALA ALA A . n 
A 1 229 ALA 229 204  204  ALA ALA A . n 
A 1 230 ARG 230 205  205  ARG ARG A . n 
A 1 231 ARG 231 206  206  ARG ARG A . n 
A 1 232 GLN 232 207  207  GLN GLN A . n 
A 1 233 LEU 233 208  208  LEU LEU A . n 
A 1 234 ALA 234 1001 1001 ALA ALA A . n 
A 1 235 ASP 235 1002 1002 ASP ASP A . n 
A 1 236 LEU 236 1003 1003 LEU LEU A . n 
A 1 237 GLU 237 1004 1004 GLU GLU A . n 
A 1 238 ASP 238 1005 1005 ASP ASP A . n 
A 1 239 ASN 239 1006 1006 ASN ASN A . n 
A 1 240 TRP 240 1007 1007 TRP TRP A . n 
A 1 241 GLU 241 1008 1008 GLU GLU A . n 
A 1 242 THR 242 1009 1009 THR THR A . n 
A 1 243 LEU 243 1010 1010 LEU LEU A . n 
A 1 244 ASN 244 1011 1011 ASN ASN A . n 
A 1 245 ASP 245 1012 1012 ASP ASP A . n 
A 1 246 ASN 246 1013 1013 ASN ASN A . n 
A 1 247 LEU 247 1014 1014 LEU LEU A . n 
A 1 248 LYS 248 1015 1015 LYS LYS A . n 
A 1 249 VAL 249 1016 1016 VAL VAL A . n 
A 1 250 ILE 250 1017 1017 ILE ILE A . n 
A 1 251 GLU 251 1018 1018 GLU GLU A . n 
A 1 252 LYS 252 1019 1019 LYS LYS A . n 
A 1 253 ALA 253 1020 1020 ALA ALA A . n 
A 1 254 ASP 254 1021 1021 ASP ASP A . n 
A 1 255 ASN 255 1022 1022 ASN ASN A . n 
A 1 256 ALA 256 1023 1023 ALA ALA A . n 
A 1 257 ALA 257 1024 1024 ALA ALA A . n 
A 1 258 GLN 258 1025 1025 GLN GLN A . n 
A 1 259 VAL 259 1026 1026 VAL VAL A . n 
A 1 260 LYS 260 1027 1027 LYS LYS A . n 
A 1 261 ASP 261 1028 1028 ASP ASP A . n 
A 1 262 ALA 262 1029 1029 ALA ALA A . n 
A 1 263 LEU 263 1030 1030 LEU LEU A . n 
A 1 264 THR 264 1031 1031 THR THR A . n 
A 1 265 LYS 265 1032 1032 LYS LYS A . n 
A 1 266 MET 266 1033 1033 MET MET A . n 
A 1 267 ARG 267 1034 1034 ARG ARG A . n 
A 1 268 ALA 268 1035 1035 ALA ALA A . n 
A 1 269 ALA 269 1036 1036 ALA ALA A . n 
A 1 270 ALA 270 1037 1037 ALA ALA A . n 
A 1 271 LEU 271 1038 1038 LEU LEU A . n 
A 1 272 ASP 272 1039 1039 ASP ASP A . n 
A 1 273 ALA 273 1040 1040 ALA ALA A . n 
A 1 274 GLN 274 1041 1041 GLN GLN A . n 
A 1 275 LYS 275 1042 1042 LYS LYS A . n 
A 1 276 ALA 276 1043 ?    ?   ?   A . n 
A 1 277 THR 277 1044 ?    ?   ?   A . n 
A 1 278 PRO 278 1045 ?    ?   ?   A . n 
A 1 279 PRO 279 1046 ?    ?   ?   A . n 
A 1 280 LYS 280 1047 ?    ?   ?   A . n 
A 1 281 LEU 281 1048 ?    ?   ?   A . n 
A 1 282 GLU 282 1049 ?    ?   ?   A . n 
A 1 283 ASP 283 1050 ?    ?   ?   A . n 
A 1 284 LYS 284 1051 ?    ?   ?   A . n 
A 1 285 SER 285 1052 ?    ?   ?   A . n 
A 1 286 PRO 286 1053 ?    ?   ?   A . n 
A 1 287 ASP 287 1054 ?    ?   ?   A . n 
A 1 288 SER 288 1055 ?    ?   ?   A . n 
A 1 289 PRO 289 1056 ?    ?   ?   A . n 
A 1 290 GLU 290 1057 ?    ?   ?   A . n 
A 1 291 MET 291 1058 ?    ?   ?   A . n 
A 1 292 LYS 292 1059 1059 LYS LYS A . n 
A 1 293 ASP 293 1060 1060 ASP ASP A . n 
A 1 294 PHE 294 1061 1061 PHE PHE A . n 
A 1 295 ARG 295 1062 1062 ARG ARG A . n 
A 1 296 HIS 296 1063 1063 HIS HIS A . n 
A 1 297 GLY 297 1064 1064 GLY GLY A . n 
A 1 298 PHE 298 1065 1065 PHE PHE A . n 
A 1 299 ASP 299 1066 1066 ASP ASP A . n 
A 1 300 ILE 300 1067 1067 ILE ILE A . n 
A 1 301 LEU 301 1068 1068 LEU LEU A . n 
A 1 302 VAL 302 1069 1069 VAL VAL A . n 
A 1 303 GLY 303 1070 1070 GLY GLY A . n 
A 1 304 GLN 304 1071 1071 GLN GLN A . n 
A 1 305 ILE 305 1072 1072 ILE ILE A . n 
A 1 306 ASP 306 1073 1073 ASP ASP A . n 
A 1 307 ASP 307 1074 1074 ASP ASP A . n 
A 1 308 ALA 308 1075 1075 ALA ALA A . n 
A 1 309 LEU 309 1076 1076 LEU LEU A . n 
A 1 310 LYS 310 1077 1077 LYS LYS A . n 
A 1 311 LEU 311 1078 1078 LEU LEU A . n 
A 1 312 ALA 312 1079 1079 ALA ALA A . n 
A 1 313 ASN 313 1080 1080 ASN ASN A . n 
A 1 314 GLU 314 1081 1081 GLU GLU A . n 
A 1 315 GLY 315 1082 1082 GLY GLY A . n 
A 1 316 LYS 316 1083 1083 LYS LYS A . n 
A 1 317 VAL 317 1084 1084 VAL VAL A . n 
A 1 318 LYS 318 1085 1085 LYS LYS A . n 
A 1 319 GLU 319 1086 1086 GLU GLU A . n 
A 1 320 ALA 320 1087 1087 ALA ALA A . n 
A 1 321 GLN 321 1088 1088 GLN GLN A . n 
A 1 322 ALA 322 1089 1089 ALA ALA A . n 
A 1 323 ALA 323 1090 1090 ALA ALA A . n 
A 1 324 ALA 324 1091 1091 ALA ALA A . n 
A 1 325 GLU 325 1092 1092 GLU GLU A . n 
A 1 326 GLN 326 1093 1093 GLN GLN A . n 
A 1 327 LEU 327 1094 1094 LEU LEU A . n 
A 1 328 LYS 328 1095 1095 LYS LYS A . n 
A 1 329 THR 329 1096 1096 THR THR A . n 
A 1 330 THR 330 1097 1097 THR THR A . n 
A 1 331 ARG 331 1098 1098 ARG ARG A . n 
A 1 332 ASN 332 1099 1099 ASN ASN A . n 
A 1 333 ALA 333 1100 1100 ALA ALA A . n 
A 1 334 TYR 334 1101 1101 TYR TYR A . n 
A 1 335 ILE 335 1102 1102 ILE ILE A . n 
A 1 336 GLN 336 1103 1103 GLN GLN A . n 
A 1 337 LYS 337 1104 1104 LYS LYS A . n 
A 1 338 TYR 338 1105 1105 TYR TYR A . n 
A 1 339 LEU 339 1106 1106 LEU LEU A . n 
A 1 340 GLU 340 219  219  GLU GLU A . n 
A 1 341 ARG 341 220  220  ARG ARG A . n 
A 1 342 ALA 342 221  221  ALA ALA A . n 
A 1 343 ARG 343 222  222  ARG ARG A . n 
A 1 344 SER 344 223  223  SER SER A . n 
A 1 345 THR 345 224  224  THR THR A . n 
A 1 346 LEU 346 225  225  LEU LEU A . n 
A 1 347 GLN 347 226  226  GLN GLN A . n 
A 1 348 LYS 348 227  227  LYS LYS A . n 
A 1 349 GLU 349 228  228  GLU GLU A . n 
A 1 350 VAL 350 229  229  VAL VAL A . n 
A 1 351 HIS 351 230  230  HIS HIS A . n 
A 1 352 ALA 352 231  231  ALA ALA A . n 
A 1 353 ALA 353 232  232  ALA ALA A . n 
A 1 354 LYS 354 233  233  LYS LYS A . n 
A 1 355 SER 355 234  234  SER SER A . n 
A 1 356 ALA 356 235  235  ALA ALA A . n 
A 1 357 ALA 357 236  236  ALA ALA A . n 
A 1 358 ILE 358 237  237  ILE ILE A . n 
A 1 359 ILE 359 238  238  ILE ILE A . n 
A 1 360 ALA 360 239  239  ALA ALA A . n 
A 1 361 GLY 361 240  240  GLY GLY A . n 
A 1 362 LEU 362 241  241  LEU LEU A . n 
A 1 363 PHE 363 242  242  PHE PHE A . n 
A 1 364 ALA 364 243  243  ALA ALA A . n 
A 1 365 LEU 365 244  244  LEU LEU A . n 
A 1 366 CYS 366 245  245  CYS CYS A . n 
A 1 367 TRP 367 246  246  TRP TRP A . n 
A 1 368 LEU 368 247  247  LEU LEU A . n 
A 1 369 PRO 369 248  248  PRO PRO A . n 
A 1 370 LEU 370 249  249  LEU LEU A . n 
A 1 371 HIS 371 250  250  HIS HIS A . n 
A 1 372 ILE 372 251  251  ILE ILE A . n 
A 1 373 ILE 373 252  252  ILE ILE A . n 
A 1 374 ASN 374 253  253  ASN ASN A . n 
A 1 375 CYS 375 254  254  CYS CYS A . n 
A 1 376 PHE 376 255  255  PHE PHE A . n 
A 1 377 THR 377 256  256  THR THR A . n 
A 1 378 PHE 378 257  257  PHE PHE A . n 
A 1 379 PHE 379 258  258  PHE PHE A . n 
A 1 380 CYS 380 259  259  CYS CYS A . n 
A 1 381 PRO 381 260  260  PRO PRO A . n 
A 1 382 ASP 382 261  261  ASP ASP A . n 
A 1 383 CYS 383 262  262  CYS CYS A . n 
A 1 384 SER 384 263  263  SER SER A . n 
A 1 385 HIS 385 264  264  HIS HIS A . n 
A 1 386 ALA 386 265  265  ALA ALA A . n 
A 1 387 PRO 387 266  266  PRO PRO A . n 
A 1 388 LEU 388 267  267  LEU LEU A . n 
A 1 389 TRP 389 268  268  TRP TRP A . n 
A 1 390 LEU 390 269  269  LEU LEU A . n 
A 1 391 MET 391 270  270  MET MET A . n 
A 1 392 TYR 392 271  271  TYR TYR A . n 
A 1 393 LEU 393 272  272  LEU LEU A . n 
A 1 394 ALA 394 273  273  ALA ALA A . n 
A 1 395 ILE 395 274  274  ILE ILE A . n 
A 1 396 VAL 396 275  275  VAL VAL A . n 
A 1 397 LEU 397 276  276  LEU LEU A . n 
A 1 398 SER 398 277  277  SER SER A . n 
A 1 399 HIS 399 278  278  HIS HIS A . n 
A 1 400 THR 400 279  279  THR THR A . n 
A 1 401 ASN 401 280  280  ASN ASN A . n 
A 1 402 SER 402 281  281  SER SER A . n 
A 1 403 VAL 403 282  282  VAL VAL A . n 
A 1 404 VAL 404 283  283  VAL VAL A . n 
A 1 405 ASN 405 284  284  ASN ASN A . n 
A 1 406 PRO 406 285  285  PRO PRO A . n 
A 1 407 PHE 407 286  286  PHE PHE A . n 
A 1 408 ILE 408 287  287  ILE ILE A . n 
A 1 409 TYR 409 288  288  TYR TYR A . n 
A 1 410 ALA 410 289  289  ALA ALA A . n 
A 1 411 TYR 411 290  290  TYR TYR A . n 
A 1 412 ARG 412 291  291  ARG ARG A . n 
A 1 413 ILE 413 292  292  ILE ILE A . n 
A 1 414 ARG 414 293  293  ARG ARG A . n 
A 1 415 GLU 415 294  294  GLU GLU A . n 
A 1 416 PHE 416 295  295  PHE PHE A . n 
A 1 417 ARG 417 296  296  ARG ARG A . n 
A 1 418 GLN 418 297  297  GLN GLN A . n 
A 1 419 THR 419 298  298  THR THR A . n 
A 1 420 PHE 420 299  299  PHE PHE A . n 
A 1 421 ARG 421 300  300  ARG ARG A . n 
A 1 422 LYS 422 301  301  LYS LYS A . n 
A 1 423 ILE 423 302  302  ILE ILE A . n 
A 1 424 ILE 424 303  303  ILE ILE A . n 
A 1 425 ARG 425 304  304  ARG ARG A . n 
A 1 426 SER 426 305  305  SER SER A . n 
A 1 427 HIS 427 306  ?    ?   ?   A . n 
A 1 428 VAL 428 307  ?    ?   ?   A . n 
A 1 429 LEU 429 308  ?    ?   ?   A . n 
A 1 430 ARG 430 309  ?    ?   ?   A . n 
A 1 431 GLN 431 310  ?    ?   ?   A . n 
A 1 432 GLN 432 311  ?    ?   ?   A . n 
A 1 433 GLU 433 312  ?    ?   ?   A . n 
A 1 434 PRO 434 313  ?    ?   ?   A . n 
A 1 435 PHE 435 314  ?    ?   ?   A . n 
A 1 436 LYS 436 315  ?    ?   ?   A . n 
A 1 437 ALA 437 316  ?    ?   ?   A . n 
A 1 438 ALA 438 317  ?    ?   ?   A . n 
A 1 439 ALA 439 318  ?    ?   ?   A . n 
A 1 440 HIS 440 319  ?    ?   ?   A . n 
A 1 441 HIS 441 320  ?    ?   ?   A . n 
A 1 442 HIS 442 321  ?    ?   ?   A . n 
A 1 443 HIS 443 322  ?    ?   ?   A . n 
A 1 444 HIS 444 323  ?    ?   ?   A . n 
A 1 445 HIS 445 324  ?    ?   ?   A . n 
A 1 446 HIS 446 325  ?    ?   ?   A . n 
A 1 447 HIS 447 326  ?    ?   ?   A . n 
A 1 448 HIS 448 327  ?    ?   ?   A . n 
A 1 449 HIS 449 328  ?    ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        JQ9 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   JQ9 
_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 JQ9 1   1201 1201 JQ9 IST A . 
C  3 CLR 1   1202 1202 CLR CLR A . 
D  3 CLR 1   1203 1203 CLR CLR A . 
E  4 OLA 1   1204 1204 OLA OLA A . 
F  4 OLA 1   1205 1205 OLA OLA A . 
G  3 CLR 1   1206 1206 CLR CLR A . 
H  4 OLA 1   1207 1207 OLA OLA A . 
I  4 OLA 1   1208 1208 OLA OLA A . 
J  4 OLA 1   1209 1209 OLA OLA A . 
K  4 OLA 1   1210 1210 OLA OLA A . 
L  4 OLA 1   1211 1211 OLA OLA A . 
M  4 OLA 1   1212 1212 OLA OLA A . 
N  4 OLA 1   1213 1213 OLA OLA A . 
O  4 OLA 1   1214 1215 OLA OLA A . 
P  4 OLA 1   1215 1216 OLA OLA A . 
Q  4 OLA 1   1216 1217 OLA OLA A . 
R  4 OLA 1   1217 1218 OLA OLA A . 
S  4 OLA 1   1218 1219 OLA OLA A . 
T  4 OLA 1   1219 1220 OLA OLA A . 
U  4 OLA 1   1220 1221 OLA OLA A . 
V  4 OLA 1   1221 1222 OLA OLA A . 
W  4 OLA 1   1222 1223 OLA OLA A . 
X  4 OLA 1   1223 1224 OLA OLA A . 
Y  4 OLA 1   1224 1225 OLA OLA A . 
Z  4 OLA 1   1225 1226 OLA OLA A . 
AA 4 OLA 1   1226 1227 OLA OLA A . 
BA 4 OLA 1   1227 1228 OLA OLA A . 
CA 5 NA  1   1228 1    NA  NA  A . 
DA 6 HOH 1   1301 75   HOH HOH A . 
DA 6 HOH 2   1302 114  HOH HOH A . 
DA 6 HOH 3   1303 76   HOH HOH A . 
DA 6 HOH 4   1304 82   HOH HOH A . 
DA 6 HOH 5   1305 40   HOH HOH A . 
DA 6 HOH 6   1306 63   HOH HOH A . 
DA 6 HOH 7   1307 65   HOH HOH A . 
DA 6 HOH 8   1308 38   HOH HOH A . 
DA 6 HOH 9   1309 108  HOH HOH A . 
DA 6 HOH 10  1310 35   HOH HOH A . 
DA 6 HOH 11  1311 12   HOH HOH A . 
DA 6 HOH 12  1312 47   HOH HOH A . 
DA 6 HOH 13  1313 52   HOH HOH A . 
DA 6 HOH 14  1314 67   HOH HOH A . 
DA 6 HOH 15  1315 78   HOH HOH A . 
DA 6 HOH 16  1316 7    HOH HOH A . 
DA 6 HOH 17  1317 4    HOH HOH A . 
DA 6 HOH 18  1318 1    HOH HOH A . 
DA 6 HOH 19  1319 54   HOH HOH A . 
DA 6 HOH 20  1320 37   HOH HOH A . 
DA 6 HOH 21  1321 8    HOH HOH A . 
DA 6 HOH 22  1322 18   HOH HOH A . 
DA 6 HOH 23  1323 29   HOH HOH A . 
DA 6 HOH 24  1324 2    HOH HOH A . 
DA 6 HOH 25  1325 58   HOH HOH A . 
DA 6 HOH 26  1326 115  HOH HOH A . 
DA 6 HOH 27  1327 60   HOH HOH A . 
DA 6 HOH 28  1328 62   HOH HOH A . 
DA 6 HOH 29  1329 26   HOH HOH A . 
DA 6 HOH 30  1330 9    HOH HOH A . 
DA 6 HOH 31  1331 48   HOH HOH A . 
DA 6 HOH 32  1332 30   HOH HOH A . 
DA 6 HOH 33  1333 43   HOH HOH A . 
DA 6 HOH 34  1334 15   HOH HOH A . 
DA 6 HOH 35  1335 34   HOH HOH A . 
DA 6 HOH 36  1336 19   HOH HOH A . 
DA 6 HOH 37  1337 25   HOH HOH A . 
DA 6 HOH 38  1338 57   HOH HOH A . 
DA 6 HOH 39  1339 22   HOH HOH A . 
DA 6 HOH 40  1340 103  HOH HOH A . 
DA 6 HOH 41  1341 66   HOH HOH A . 
DA 6 HOH 42  1342 98   HOH HOH A . 
DA 6 HOH 43  1343 11   HOH HOH A . 
DA 6 HOH 44  1344 61   HOH HOH A . 
DA 6 HOH 45  1345 6    HOH HOH A . 
DA 6 HOH 46  1346 72   HOH HOH A . 
DA 6 HOH 47  1347 32   HOH HOH A . 
DA 6 HOH 48  1348 28   HOH HOH A . 
DA 6 HOH 49  1349 39   HOH HOH A . 
DA 6 HOH 50  1350 112  HOH HOH A . 
DA 6 HOH 51  1351 87   HOH HOH A . 
DA 6 HOH 52  1352 16   HOH HOH A . 
DA 6 HOH 53  1353 17   HOH HOH A . 
DA 6 HOH 54  1354 51   HOH HOH A . 
DA 6 HOH 55  1355 69   HOH HOH A . 
DA 6 HOH 56  1356 80   HOH HOH A . 
DA 6 HOH 57  1357 74   HOH HOH A . 
DA 6 HOH 58  1358 46   HOH HOH A . 
DA 6 HOH 59  1359 89   HOH HOH A . 
DA 6 HOH 60  1360 24   HOH HOH A . 
DA 6 HOH 61  1361 42   HOH HOH A . 
DA 6 HOH 62  1362 5    HOH HOH A . 
DA 6 HOH 63  1363 23   HOH HOH A . 
DA 6 HOH 64  1364 20   HOH HOH A . 
DA 6 HOH 65  1365 107  HOH HOH A . 
DA 6 HOH 66  1366 59   HOH HOH A . 
DA 6 HOH 67  1367 118  HOH HOH A . 
DA 6 HOH 68  1368 73   HOH HOH A . 
DA 6 HOH 69  1369 3    HOH HOH A . 
DA 6 HOH 70  1370 49   HOH HOH A . 
DA 6 HOH 71  1371 81   HOH HOH A . 
DA 6 HOH 72  1372 97   HOH HOH A . 
DA 6 HOH 73  1373 31   HOH HOH A . 
DA 6 HOH 74  1374 99   HOH HOH A . 
DA 6 HOH 75  1375 27   HOH HOH A . 
DA 6 HOH 76  1376 33   HOH HOH A . 
DA 6 HOH 77  1377 41   HOH HOH A . 
DA 6 HOH 78  1378 79   HOH HOH A . 
DA 6 HOH 79  1379 90   HOH HOH A . 
DA 6 HOH 80  1380 109  HOH HOH A . 
DA 6 HOH 81  1381 10   HOH HOH A . 
DA 6 HOH 82  1382 88   HOH HOH A . 
DA 6 HOH 83  1383 21   HOH HOH A . 
DA 6 HOH 84  1384 53   HOH HOH A . 
DA 6 HOH 85  1385 64   HOH HOH A . 
DA 6 HOH 86  1386 36   HOH HOH A . 
DA 6 HOH 87  1387 77   HOH HOH A . 
DA 6 HOH 88  1388 13   HOH HOH A . 
DA 6 HOH 89  1389 92   HOH HOH A . 
DA 6 HOH 90  1390 93   HOH HOH A . 
DA 6 HOH 91  1391 14   HOH HOH A . 
DA 6 HOH 92  1392 96   HOH HOH A . 
DA 6 HOH 93  1393 101  HOH HOH A . 
DA 6 HOH 94  1394 56   HOH HOH A . 
DA 6 HOH 95  1395 84   HOH HOH A . 
DA 6 HOH 96  1396 113  HOH HOH A . 
DA 6 HOH 97  1397 102  HOH HOH A . 
DA 6 HOH 98  1398 105  HOH HOH A . 
DA 6 HOH 99  1399 50   HOH HOH A . 
DA 6 HOH 100 1400 85   HOH HOH A . 
DA 6 HOH 101 1401 44   HOH HOH A . 
DA 6 HOH 102 1402 83   HOH HOH A . 
DA 6 HOH 103 1403 86   HOH HOH A . 
DA 6 HOH 104 1404 104  HOH HOH A . 
DA 6 HOH 105 1405 117  HOH HOH A . 
DA 6 HOH 106 1406 110  HOH HOH A . 
DA 6 HOH 107 1407 120  HOH HOH A . 
DA 6 HOH 108 1408 111  HOH HOH A . 
DA 6 HOH 109 1409 106  HOH HOH A . 
DA 6 HOH 110 1410 119  HOH HOH A . 
DA 6 HOH 111 1411 68   HOH HOH A . 
DA 6 HOH 112 1412 116  HOH HOH A . 
DA 6 HOH 113 1413 91   HOH HOH A . 
DA 6 HOH 114 1414 95   HOH HOH A . 
DA 6 HOH 115 1415 70   HOH HOH A . 
DA 6 HOH 116 1416 71   HOH HOH A . 
DA 6 HOH 117 1417 45   HOH HOH A . 
DA 6 HOH 118 1418 55   HOH HOH A . 
DA 6 HOH 119 1419 100  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 ARG 111  ? CG  ? A  ARG 136 CG  
2   1 Y 1 A ARG 111  ? CD  ? A  ARG 136 CD  
3   1 Y 1 A ARG 111  ? NE  ? A  ARG 136 NE  
4   1 Y 1 A ARG 111  ? CZ  ? A  ARG 136 CZ  
5   1 Y 1 A ARG 111  ? NH1 ? A  ARG 136 NH1 
6   1 Y 1 A ARG 111  ? NH2 ? A  ARG 136 NH2 
7   1 Y 1 A GLN 148  ? CG  ? A  GLN 173 CG  
8   1 Y 1 A GLN 148  ? CD  ? A  GLN 173 CD  
9   1 Y 1 A GLN 148  ? OE1 ? A  GLN 173 OE1 
10  1 Y 1 A GLN 148  ? NE2 ? A  GLN 173 NE2 
11  1 Y 1 A ARG 206  ? NE  ? A  ARG 231 NE  
12  1 Y 1 A ARG 206  ? CZ  ? A  ARG 231 CZ  
13  1 Y 1 A ARG 206  ? NH1 ? A  ARG 231 NH1 
14  1 Y 1 A ARG 206  ? NH2 ? A  ARG 231 NH2 
15  1 Y 1 A ASP 1021 ? CG  ? A  ASP 254 CG  
16  1 Y 1 A ASP 1021 ? OD1 ? A  ASP 254 OD1 
17  1 Y 1 A ASP 1021 ? OD2 ? A  ASP 254 OD2 
18  1 Y 1 A LYS 1059 ? CG  ? A  LYS 292 CG  
19  1 Y 1 A LYS 1059 ? CD  ? A  LYS 292 CD  
20  1 Y 1 A LYS 1059 ? CE  ? A  LYS 292 CE  
21  1 Y 1 A LYS 1059 ? NZ  ? A  LYS 292 NZ  
22  1 Y 1 A ASP 1060 ? CG  ? A  ASP 293 CG  
23  1 Y 1 A ASP 1060 ? OD1 ? A  ASP 293 OD1 
24  1 Y 1 A ASP 1060 ? OD2 ? A  ASP 293 OD2 
25  1 Y 1 A PHE 1061 ? CG  ? A  PHE 294 CG  
26  1 Y 1 A PHE 1061 ? CD1 ? A  PHE 294 CD1 
27  1 Y 1 A PHE 1061 ? CD2 ? A  PHE 294 CD2 
28  1 Y 1 A PHE 1061 ? CE1 ? A  PHE 294 CE1 
29  1 Y 1 A PHE 1061 ? CE2 ? A  PHE 294 CE2 
30  1 Y 1 A PHE 1061 ? CZ  ? A  PHE 294 CZ  
31  1 Y 1 A ARG 1062 ? CG  ? A  ARG 295 CG  
32  1 Y 1 A ARG 1062 ? CD  ? A  ARG 295 CD  
33  1 Y 1 A ARG 1062 ? NE  ? A  ARG 295 NE  
34  1 Y 1 A ARG 1062 ? CZ  ? A  ARG 295 CZ  
35  1 Y 1 A ARG 1062 ? NH1 ? A  ARG 295 NH1 
36  1 Y 1 A ARG 1062 ? NH2 ? A  ARG 295 NH2 
37  1 Y 1 A LYS 1077 ? CE  ? A  LYS 310 CE  
38  1 Y 1 A LYS 1077 ? NZ  ? A  LYS 310 NZ  
39  1 Y 1 A LYS 1104 ? CG  ? A  LYS 337 CG  
40  1 Y 1 A LYS 1104 ? CD  ? A  LYS 337 CD  
41  1 Y 1 A LYS 1104 ? CE  ? A  LYS 337 CE  
42  1 Y 1 A LYS 1104 ? NZ  ? A  LYS 337 NZ  
43  1 Y 1 A TYR 1105 ? CG  ? A  TYR 338 CG  
44  1 Y 1 A TYR 1105 ? CD1 ? A  TYR 338 CD1 
45  1 Y 1 A TYR 1105 ? CD2 ? A  TYR 338 CD2 
46  1 Y 1 A TYR 1105 ? CE1 ? A  TYR 338 CE1 
47  1 Y 1 A TYR 1105 ? CE2 ? A  TYR 338 CE2 
48  1 Y 1 A TYR 1105 ? CZ  ? A  TYR 338 CZ  
49  1 Y 1 A TYR 1105 ? OH  ? A  TYR 338 OH  
50  1 Y 1 A ARG 220  ? CG  ? A  ARG 341 CG  
51  1 Y 1 A ARG 220  ? CD  ? A  ARG 341 CD  
52  1 Y 1 A ARG 220  ? NE  ? A  ARG 341 NE  
53  1 Y 1 A ARG 220  ? CZ  ? A  ARG 341 CZ  
54  1 Y 1 A ARG 220  ? NH1 ? A  ARG 341 NH1 
55  1 Y 1 A ARG 220  ? NH2 ? A  ARG 341 NH2 
56  1 Y 1 A ARG 222  ? NE  ? A  ARG 343 NE  
57  1 Y 1 A ARG 222  ? CZ  ? A  ARG 343 CZ  
58  1 Y 1 A ARG 222  ? NH1 ? A  ARG 343 NH1 
59  1 Y 1 A ARG 222  ? NH2 ? A  ARG 343 NH2 
60  1 N 1 A OLA 1204 ? C13 ? E  OLA 1   C13 
61  1 N 1 A OLA 1204 ? C14 ? E  OLA 1   C14 
62  1 N 1 A OLA 1204 ? C15 ? E  OLA 1   C15 
63  1 N 1 A OLA 1204 ? C16 ? E  OLA 1   C16 
64  1 N 1 A OLA 1204 ? C17 ? E  OLA 1   C17 
65  1 N 1 A OLA 1204 ? C18 ? E  OLA 1   C18 
66  1 N 1 A OLA 1205 ? C16 ? F  OLA 1   C16 
67  1 N 1 A OLA 1205 ? C17 ? F  OLA 1   C17 
68  1 N 1 A OLA 1205 ? C18 ? F  OLA 1   C18 
69  1 N 1 A OLA 1207 ? C1  ? H  OLA 1   C1  
70  1 N 1 A OLA 1207 ? O1  ? H  OLA 1   O1  
71  1 N 1 A OLA 1207 ? O2  ? H  OLA 1   O2  
72  1 N 1 A OLA 1207 ? C2  ? H  OLA 1   C2  
73  1 N 1 A OLA 1207 ? C3  ? H  OLA 1   C3  
74  1 N 1 A OLA 1207 ? C4  ? H  OLA 1   C4  
75  1 N 1 A OLA 1207 ? C5  ? H  OLA 1   C5  
76  1 N 1 A OLA 1207 ? C6  ? H  OLA 1   C6  
77  1 N 1 A OLA 1207 ? C7  ? H  OLA 1   C7  
78  1 N 1 A OLA 1207 ? C8  ? H  OLA 1   C8  
79  1 N 1 A OLA 1207 ? C9  ? H  OLA 1   C9  
80  1 N 1 A OLA 1209 ? C8  ? J  OLA 1   C8  
81  1 N 1 A OLA 1209 ? C9  ? J  OLA 1   C9  
82  1 N 1 A OLA 1209 ? C10 ? J  OLA 1   C10 
83  1 N 1 A OLA 1209 ? C11 ? J  OLA 1   C11 
84  1 N 1 A OLA 1209 ? C12 ? J  OLA 1   C12 
85  1 N 1 A OLA 1209 ? C13 ? J  OLA 1   C13 
86  1 N 1 A OLA 1209 ? C14 ? J  OLA 1   C14 
87  1 N 1 A OLA 1209 ? C15 ? J  OLA 1   C15 
88  1 N 1 A OLA 1209 ? C16 ? J  OLA 1   C16 
89  1 N 1 A OLA 1209 ? C17 ? J  OLA 1   C17 
90  1 N 1 A OLA 1209 ? C18 ? J  OLA 1   C18 
91  1 N 1 A OLA 1210 ? C13 ? K  OLA 1   C13 
92  1 N 1 A OLA 1210 ? C14 ? K  OLA 1   C14 
93  1 N 1 A OLA 1210 ? C15 ? K  OLA 1   C15 
94  1 N 1 A OLA 1210 ? C16 ? K  OLA 1   C16 
95  1 N 1 A OLA 1210 ? C17 ? K  OLA 1   C17 
96  1 N 1 A OLA 1210 ? C18 ? K  OLA 1   C18 
97  1 N 1 A OLA 1211 ? C15 ? L  OLA 1   C15 
98  1 N 1 A OLA 1211 ? C16 ? L  OLA 1   C16 
99  1 N 1 A OLA 1211 ? C17 ? L  OLA 1   C17 
100 1 N 1 A OLA 1211 ? C18 ? L  OLA 1   C18 
101 1 N 1 A OLA 1212 ? C14 ? M  OLA 1   C14 
102 1 N 1 A OLA 1212 ? C15 ? M  OLA 1   C15 
103 1 N 1 A OLA 1212 ? C16 ? M  OLA 1   C16 
104 1 N 1 A OLA 1212 ? C17 ? M  OLA 1   C17 
105 1 N 1 A OLA 1212 ? C18 ? M  OLA 1   C18 
106 1 N 1 A OLA 1213 ? C11 ? N  OLA 1   C11 
107 1 N 1 A OLA 1213 ? C12 ? N  OLA 1   C12 
108 1 N 1 A OLA 1213 ? C13 ? N  OLA 1   C13 
109 1 N 1 A OLA 1213 ? C14 ? N  OLA 1   C14 
110 1 N 1 A OLA 1213 ? C15 ? N  OLA 1   C15 
111 1 N 1 A OLA 1213 ? C16 ? N  OLA 1   C16 
112 1 N 1 A OLA 1213 ? C17 ? N  OLA 1   C17 
113 1 N 1 A OLA 1213 ? C18 ? N  OLA 1   C18 
114 1 N 1 A OLA 1214 ? C1  ? O  OLA 1   C1  
115 1 N 1 A OLA 1214 ? O1  ? O  OLA 1   O1  
116 1 N 1 A OLA 1214 ? O2  ? O  OLA 1   O2  
117 1 N 1 A OLA 1214 ? C2  ? O  OLA 1   C2  
118 1 N 1 A OLA 1214 ? C3  ? O  OLA 1   C3  
119 1 N 1 A OLA 1214 ? C4  ? O  OLA 1   C4  
120 1 N 1 A OLA 1214 ? C5  ? O  OLA 1   C5  
121 1 N 1 A OLA 1214 ? C6  ? O  OLA 1   C6  
122 1 N 1 A OLA 1214 ? C7  ? O  OLA 1   C7  
123 1 N 1 A OLA 1214 ? C8  ? O  OLA 1   C8  
124 1 N 1 A OLA 1214 ? C9  ? O  OLA 1   C9  
125 1 N 1 A OLA 1214 ? C18 ? O  OLA 1   C18 
126 1 N 1 A OLA 1215 ? C12 ? P  OLA 1   C12 
127 1 N 1 A OLA 1215 ? C13 ? P  OLA 1   C13 
128 1 N 1 A OLA 1215 ? C14 ? P  OLA 1   C14 
129 1 N 1 A OLA 1215 ? C15 ? P  OLA 1   C15 
130 1 N 1 A OLA 1215 ? C16 ? P  OLA 1   C16 
131 1 N 1 A OLA 1215 ? C17 ? P  OLA 1   C17 
132 1 N 1 A OLA 1215 ? C18 ? P  OLA 1   C18 
133 1 N 1 A OLA 1216 ? C1  ? Q  OLA 1   C1  
134 1 N 1 A OLA 1216 ? O1  ? Q  OLA 1   O1  
135 1 N 1 A OLA 1216 ? O2  ? Q  OLA 1   O2  
136 1 N 1 A OLA 1216 ? C2  ? Q  OLA 1   C2  
137 1 N 1 A OLA 1216 ? C3  ? Q  OLA 1   C3  
138 1 N 1 A OLA 1217 ? C15 ? R  OLA 1   C15 
139 1 N 1 A OLA 1217 ? C16 ? R  OLA 1   C16 
140 1 N 1 A OLA 1217 ? C17 ? R  OLA 1   C17 
141 1 N 1 A OLA 1217 ? C18 ? R  OLA 1   C18 
142 1 N 1 A OLA 1218 ? C17 ? S  OLA 1   C17 
143 1 N 1 A OLA 1218 ? C18 ? S  OLA 1   C18 
144 1 N 1 A OLA 1219 ? C1  ? T  OLA 1   C1  
145 1 N 1 A OLA 1219 ? O1  ? T  OLA 1   O1  
146 1 N 1 A OLA 1219 ? O2  ? T  OLA 1   O2  
147 1 N 1 A OLA 1219 ? C16 ? T  OLA 1   C16 
148 1 N 1 A OLA 1219 ? C17 ? T  OLA 1   C17 
149 1 N 1 A OLA 1219 ? C18 ? T  OLA 1   C18 
150 1 N 1 A OLA 1220 ? C9  ? U  OLA 1   C9  
151 1 N 1 A OLA 1220 ? C10 ? U  OLA 1   C10 
152 1 N 1 A OLA 1220 ? C11 ? U  OLA 1   C11 
153 1 N 1 A OLA 1220 ? C12 ? U  OLA 1   C12 
154 1 N 1 A OLA 1220 ? C13 ? U  OLA 1   C13 
155 1 N 1 A OLA 1220 ? C14 ? U  OLA 1   C14 
156 1 N 1 A OLA 1220 ? C15 ? U  OLA 1   C15 
157 1 N 1 A OLA 1220 ? C16 ? U  OLA 1   C16 
158 1 N 1 A OLA 1220 ? C17 ? U  OLA 1   C17 
159 1 N 1 A OLA 1220 ? C18 ? U  OLA 1   C18 
160 1 N 1 A OLA 1221 ? C16 ? V  OLA 1   C16 
161 1 N 1 A OLA 1221 ? C17 ? V  OLA 1   C17 
162 1 N 1 A OLA 1221 ? C18 ? V  OLA 1   C18 
163 1 N 1 A OLA 1222 ? C7  ? W  OLA 1   C7  
164 1 N 1 A OLA 1222 ? C8  ? W  OLA 1   C8  
165 1 N 1 A OLA 1222 ? C9  ? W  OLA 1   C9  
166 1 N 1 A OLA 1222 ? C10 ? W  OLA 1   C10 
167 1 N 1 A OLA 1222 ? C11 ? W  OLA 1   C11 
168 1 N 1 A OLA 1222 ? C12 ? W  OLA 1   C12 
169 1 N 1 A OLA 1222 ? C13 ? W  OLA 1   C13 
170 1 N 1 A OLA 1222 ? C14 ? W  OLA 1   C14 
171 1 N 1 A OLA 1222 ? C15 ? W  OLA 1   C15 
172 1 N 1 A OLA 1222 ? C16 ? W  OLA 1   C16 
173 1 N 1 A OLA 1222 ? C17 ? W  OLA 1   C17 
174 1 N 1 A OLA 1222 ? C18 ? W  OLA 1   C18 
175 1 N 1 A OLA 1223 ? C10 ? X  OLA 1   C10 
176 1 N 1 A OLA 1223 ? C11 ? X  OLA 1   C11 
177 1 N 1 A OLA 1223 ? C12 ? X  OLA 1   C12 
178 1 N 1 A OLA 1223 ? C13 ? X  OLA 1   C13 
179 1 N 1 A OLA 1223 ? C14 ? X  OLA 1   C14 
180 1 N 1 A OLA 1223 ? C15 ? X  OLA 1   C15 
181 1 N 1 A OLA 1223 ? C16 ? X  OLA 1   C16 
182 1 N 1 A OLA 1223 ? C17 ? X  OLA 1   C17 
183 1 N 1 A OLA 1223 ? C18 ? X  OLA 1   C18 
184 1 N 1 A OLA 1224 ? C1  ? Y  OLA 1   C1  
185 1 N 1 A OLA 1224 ? O1  ? Y  OLA 1   O1  
186 1 N 1 A OLA 1224 ? O2  ? Y  OLA 1   O2  
187 1 N 1 A OLA 1224 ? C2  ? Y  OLA 1   C2  
188 1 N 1 A OLA 1224 ? C3  ? Y  OLA 1   C3  
189 1 N 1 A OLA 1224 ? C4  ? Y  OLA 1   C4  
190 1 N 1 A OLA 1224 ? C5  ? Y  OLA 1   C5  
191 1 N 1 A OLA 1224 ? C6  ? Y  OLA 1   C6  
192 1 N 1 A OLA 1224 ? C7  ? Y  OLA 1   C7  
193 1 N 1 A OLA 1224 ? C8  ? Y  OLA 1   C8  
194 1 N 1 A OLA 1224 ? C9  ? Y  OLA 1   C9  
195 1 N 1 A OLA 1225 ? C15 ? Z  OLA 1   C15 
196 1 N 1 A OLA 1225 ? C16 ? Z  OLA 1   C16 
197 1 N 1 A OLA 1225 ? C17 ? Z  OLA 1   C17 
198 1 N 1 A OLA 1225 ? C18 ? Z  OLA 1   C18 
199 1 N 1 A OLA 1227 ? C13 ? BA OLA 1   C13 
200 1 N 1 A OLA 1227 ? C14 ? BA OLA 1   C14 
201 1 N 1 A OLA 1227 ? C15 ? BA OLA 1   C15 
202 1 N 1 A OLA 1227 ? C16 ? BA OLA 1   C16 
203 1 N 1 A OLA 1227 ? C17 ? BA OLA 1   C17 
204 1 N 1 A OLA 1227 ? C18 ? BA OLA 1   C18 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20_4459: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                  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                     8RW0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     39.333 
_cell.length_a_esd                 ? 
_cell.length_b                     179.345 
_cell.length_b_esd                 ? 
_cell.length_c                     139.860 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8RW0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 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                   8RW0 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.47 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.30 
_exptl_crystal.description                  'square plates' 
_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          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.1 M Sodium citrate pH 5, 0.05 M Sodium thiocyanate, 3% (v/v) 
2-methyl-2,4-pentanediol, 32% (v/v) PEG 400, 1 mM Theophylline
;
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-04-27 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RW0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.94 
_reflns.d_resolution_low                               38.42 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     70192 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.64 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.30 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.04461 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.94 
_reflns_shell.d_res_low                                     2.01 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.19 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3585 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.6 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.5988 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.479 
_reflns_shell.pdbx_CC_star                                  0.805 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.95 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8RW0 
_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                            1.94 
_refine.ls_d_res_low                             38.42 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     70192 
_refine.ls_number_reflns_R_free                  3412 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.22 
_refine.ls_percent_reflns_R_free                 4.86 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1935 
_refine.ls_R_factor_R_free                       0.2166 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1923 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.31 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.25 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.94 
_refine_hist.d_res_low                        38.42 
_refine_hist.number_atoms_solvent             119 
_refine_hist.number_atoms_total               3475 
_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        2928 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         428 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  ? 3460 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.047  ? 4637 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 24.793 ? 700  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.065  ? 525  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 561  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.94 1.97  . . 154 2685 95.00  . . . . 0.3214 . . . . . . . . . . . 0.3438 
'X-RAY DIFFRACTION' 1.97 2.00  . . 130 2736 99.00  . . . . 0.3032 . . . . . . . . . . . 0.3190 
'X-RAY DIFFRACTION' 2.00 2.03  . . 153 2774 99.00  . . . . 0.2889 . . . . . . . . . . . 0.3190 
'X-RAY DIFFRACTION' 2.03 2.06  . . 120 2850 99.00  . . . . 0.2759 . . . . . . . . . . . 0.3278 
'X-RAY DIFFRACTION' 2.06 2.10  . . 105 2799 99.00  . . . . 0.2573 . . . . . . . . . . . 0.2576 
'X-RAY DIFFRACTION' 2.10 2.14  . . 139 2807 100.00 . . . . 0.2410 . . . . . . . . . . . 0.3092 
'X-RAY DIFFRACTION' 2.14 2.18  . . 147 2801 100.00 . . . . 0.2389 . . . . . . . . . . . 0.2610 
'X-RAY DIFFRACTION' 2.18 2.22  . . 137 2769 100.00 . . . . 0.2175 . . . . . . . . . . . 0.2875 
'X-RAY DIFFRACTION' 2.22 2.27  . . 168 2759 100.00 . . . . 0.2312 . . . . . . . . . . . 0.2537 
'X-RAY DIFFRACTION' 2.27 2.32  . . 150 2833 99.00  . . . . 0.2129 . . . . . . . . . . . 0.2180 
'X-RAY DIFFRACTION' 2.32 2.38  . . 147 2756 100.00 . . . . 0.1995 . . . . . . . . . . . 0.2296 
'X-RAY DIFFRACTION' 2.38 2.44  . . 144 2791 99.00  . . . . 0.1973 . . . . . . . . . . . 0.2654 
'X-RAY DIFFRACTION' 2.44 2.52  . . 156 2739 99.00  . . . . 0.1967 . . . . . . . . . . . 0.2302 
'X-RAY DIFFRACTION' 2.52 2.60  . . 133 2827 100.00 . . . . 0.1877 . . . . . . . . . . . 0.2337 
'X-RAY DIFFRACTION' 2.60 2.69  . . 138 2776 100.00 . . . . 0.1674 . . . . . . . . . . . 0.2111 
'X-RAY DIFFRACTION' 2.69 2.80  . . 151 2838 100.00 . . . . 0.1693 . . . . . . . . . . . 0.2200 
'X-RAY DIFFRACTION' 2.80 2.93  . . 150 2744 100.00 . . . . 0.1708 . . . . . . . . . . . 0.2201 
'X-RAY DIFFRACTION' 2.93 3.08  . . 136 2816 100.00 . . . . 0.1857 . . . . . . . . . . . 0.1945 
'X-RAY DIFFRACTION' 3.08 3.27  . . 140 2805 99.00  . . . . 0.1874 . . . . . . . . . . . 0.1971 
'X-RAY DIFFRACTION' 3.27 3.53  . . 165 2749 100.00 . . . . 0.1706 . . . . . . . . . . . 0.2003 
'X-RAY DIFFRACTION' 3.53 3.88  . . 120 2815 100.00 . . . . 0.1670 . . . . . . . . . . . 0.2796 
'X-RAY DIFFRACTION' 3.88 4.44  . . 152 2768 99.00  . . . . 0.1640 . . . . . . . . . . . 0.1548 
'X-RAY DIFFRACTION' 4.44 5.59  . . 128 2773 98.00  . . . . 0.1781 . . . . . . . . . . . 0.1620 
'X-RAY DIFFRACTION' 5.59 38.42 . . 149 2770 99.00  . . . . 0.1854 . . . . . . . . . . . 0.1868 
# 
_struct.entry_id                     8RW0 
_struct.title                        'Crystal structure of the adenosine A2A receptor in complex with Istradefylline' 
_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        8RW0 
_struct_keywords.text            
;GPCR, adenosine receptor, Parkinson's disease, MEMBRANE PROTEIN
;
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
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 3 ? 
E  N N 4 ? 
F  N N 4 ? 
G  N N 3 ? 
H  N N 4 ? 
I  N N 4 ? 
J  N N 4 ? 
K  N N 4 ? 
L  N N 4 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 4 ? 
P  N N 4 ? 
Q  N N 4 ? 
R  N N 4 ? 
S  N N 4 ? 
T  N N 4 ? 
U  N N 4 ? 
V  N N 4 ? 
W  N N 4 ? 
X  N N 4 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 4 ? 
BA N N 4 ? 
CA N N 5 ? 
DA N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP AA2AR_HUMAN P29274 ? 1 
;PIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADIAVGVLAIPFAITISTGFCAACHGCLFIA
CFVLVLTQSSIFSLLAIAIDRYIAIRIPLRYNGLVTGTRAKGIIAICWVLSFAIGLTPMLGWNNCGQPKEGKNHSQGCGE
GQVACLFEDVVPMNYMVYFNFFACVLVPLLLMLGVYLRIFLAARRQL
;
2   
2 UNP C562_ECOLX  P0ABE7 ? 1 
;ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLAN
EGKVKEAQAAAEQLKTTRNAYHQKY
;
23  
3 UNP AA2AR_HUMAN P29274 ? 1 
;ERARSTLQKEVHAAKSLAIIVGLFALCWLPLHIINCFTFFCPDCSHAPLWLMYLAIVLSHTNSVVNPFIYAYRIREFRQT
FRKIIRSHVLRQQEPFKAA
;
219 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8RW0 A 27  ? 233 ? P29274 2   ? 208 ? 2    208  
2 2 8RW0 A 234 ? 338 ? P0ABE7 23  ? 127 ? 1001 1105 
3 3 8RW0 A 340 ? 438 ? P29274 219 ? 317 ? 219  317  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8RW0 MET A 1   ? UNP P29274 ?   ?   'initiating methionine' -24  1  
1 8RW0 LYS A 2   ? UNP P29274 ?   ?   'expression tag'        -23  2  
1 8RW0 THR A 3   ? UNP P29274 ?   ?   'expression tag'        -22  3  
1 8RW0 ILE A 4   ? UNP P29274 ?   ?   'expression tag'        -21  4  
1 8RW0 ILE A 5   ? UNP P29274 ?   ?   'expression tag'        -20  5  
1 8RW0 ALA A 6   ? UNP P29274 ?   ?   'expression tag'        -19  6  
1 8RW0 LEU A 7   ? UNP P29274 ?   ?   'expression tag'        -18  7  
1 8RW0 SER A 8   ? UNP P29274 ?   ?   'expression tag'        -17  8  
1 8RW0 TYR A 9   ? UNP P29274 ?   ?   'expression tag'        -16  9  
1 8RW0 ILE A 10  ? UNP P29274 ?   ?   'expression tag'        -15  10 
1 8RW0 PHE A 11  ? UNP P29274 ?   ?   'expression tag'        -14  11 
1 8RW0 CYS A 12  ? UNP P29274 ?   ?   'expression tag'        -13  12 
1 8RW0 LEU A 13  ? UNP P29274 ?   ?   'expression tag'        -12  13 
1 8RW0 VAL A 14  ? UNP P29274 ?   ?   'expression tag'        -11  14 
1 8RW0 PHE A 15  ? UNP P29274 ?   ?   'expression tag'        -10  15 
1 8RW0 ALA A 16  ? UNP P29274 ?   ?   'expression tag'        -9   16 
1 8RW0 ASP A 17  ? UNP P29274 ?   ?   'expression tag'        -8   17 
1 8RW0 TYR A 18  ? UNP P29274 ?   ?   'expression tag'        -7   18 
1 8RW0 LYS A 19  ? UNP P29274 ?   ?   'expression tag'        -6   19 
1 8RW0 ASP A 20  ? UNP P29274 ?   ?   'expression tag'        -5   20 
1 8RW0 ASP A 21  ? UNP P29274 ?   ?   'expression tag'        -4   21 
1 8RW0 ASP A 22  ? UNP P29274 ?   ?   'expression tag'        -3   22 
1 8RW0 ASP A 23  ? UNP P29274 ?   ?   'expression tag'        -2   23 
1 8RW0 GLY A 24  ? UNP P29274 ?   ?   'expression tag'        -1   24 
1 8RW0 ALA A 25  ? UNP P29274 ?   ?   'expression tag'        0    25 
1 8RW0 PRO A 26  ? UNP P29274 ?   ?   'expression tag'        1    26 
1 8RW0 LEU A 79  ? UNP P29274 ALA 54  conflict                54   27 
1 8RW0 ALA A 113 ? UNP P29274 THR 88  conflict                88   28 
1 8RW0 ALA A 132 ? UNP P29274 ARG 107 conflict                107  29 
1 8RW0 ALA A 147 ? UNP P29274 LYS 122 conflict                122  30 
1 8RW0 ALA A 179 ? UNP P29274 ASN 154 conflict                154  31 
1 8RW0 ALA A 227 ? UNP P29274 LEU 202 conflict                202  32 
2 8RW0 TRP A 240 ? UNP P0ABE7 MET 29  conflict                1007 33 
2 8RW0 ILE A 335 ? UNP P0ABE7 HIS 124 conflict                1102 34 
2 8RW0 LEU A 339 ? UNP P0ABE7 ?   ?   linker                  1106 35 
3 8RW0 ALA A 356 ? UNP P29274 LEU 235 conflict                235  36 
3 8RW0 ALA A 360 ? UNP P29274 VAL 239 conflict                239  37 
3 8RW0 ALA A 439 ? UNP P29274 ?   ?   'expression tag'        318  38 
3 8RW0 HIS A 440 ? UNP P29274 ?   ?   'expression tag'        319  39 
3 8RW0 HIS A 441 ? UNP P29274 ?   ?   'expression tag'        320  40 
3 8RW0 HIS A 442 ? UNP P29274 ?   ?   'expression tag'        321  41 
3 8RW0 HIS A 443 ? UNP P29274 ?   ?   'expression tag'        322  42 
3 8RW0 HIS A 444 ? UNP P29274 ?   ?   'expression tag'        323  43 
3 8RW0 HIS A 445 ? UNP P29274 ?   ?   'expression tag'        324  44 
3 8RW0 HIS A 446 ? UNP P29274 ?   ?   'expression tag'        325  45 
3 8RW0 HIS A 447 ? UNP P29274 ?   ?   'expression tag'        326  46 
3 8RW0 HIS A 448 ? UNP P29274 ?   ?   'expression tag'        327  47 
3 8RW0 HIS A 449 ? UNP P29274 ?   ?   'expression tag'        328  48 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   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)' 12020 ? 
1 MORE         57    ? 
1 'SSA (A^2)'  19160 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 26  ? ASN A 59  ? PRO A 1    ASN A 34   1 ? 34 
HELX_P HELX_P2  AA2 SER A 60  ? GLN A 63  ? SER A 35   GLN A 38   5 ? 4  
HELX_P HELX_P3  AA3 ASN A 64  ? LEU A 83  ? ASN A 39   LEU A 58   1 ? 20 
HELX_P HELX_P4  AA4 LEU A 83  ? THR A 93  ? LEU A 58   THR A 68   1 ? 11 
HELX_P HELX_P5  AA5 CYS A 99  ? ILE A 133 ? CYS A 74   ILE A 108  1 ? 35 
HELX_P HELX_P6  AA6 ILE A 133 ? VAL A 141 ? ILE A 108  VAL A 116  1 ? 9  
HELX_P HELX_P7  AA7 THR A 142 ? LEU A 162 ? THR A 117  LEU A 137  1 ? 21 
HELX_P HELX_P8  AA8 THR A 163 ? GLY A 167 ? THR A 138  GLY A 142  5 ? 5  
HELX_P HELX_P9  AA9 LYS A 175 ? GLN A 182 ? LYS A 150  GLN A 157  1 ? 8  
HELX_P HELX_P10 AB1 LEU A 192 ? VAL A 197 ? LEU A 167  VAL A 172  1 ? 6  
HELX_P HELX_P11 AB2 PRO A 198 ? PHE A 205 ? PRO A 173  PHE A 180  1 ? 8  
HELX_P HELX_P12 AB3 VAL A 211 ? LYS A 252 ? VAL A 186  LYS A 1019 1 ? 42 
HELX_P HELX_P13 AB4 ASN A 255 ? LYS A 275 ? ASN A 1022 LYS A 1042 1 ? 21 
HELX_P HELX_P14 AB5 ASP A 293 ? GLU A 314 ? ASP A 1060 GLU A 1081 1 ? 22 
HELX_P HELX_P15 AB6 LYS A 316 ? GLN A 326 ? LYS A 1083 GLN A 1093 1 ? 11 
HELX_P HELX_P16 AB7 GLN A 326 ? TYR A 334 ? GLN A 1093 TYR A 1101 1 ? 9  
HELX_P HELX_P17 AB8 TYR A 334 ? CYS A 380 ? TYR A 1101 CYS A 259  1 ? 47 
HELX_P HELX_P18 AB9 PRO A 387 ? ILE A 413 ? PRO A 266  ILE A 292  1 ? 27 
HELX_P HELX_P19 AC1 ILE A 413 ? SER A 426 ? ILE A 292  SER A 305  1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A  CYS 96  SG  ? ? ? 1_555 A  CYS 184 SG ? ? A CYS 71   A CYS 159  1_555 ? ? ? ? ? ? ? 2.068 ? ? 
disulf2 disulf ? ? A  CYS 99  SG  ? ? ? 1_555 A  CYS 171 SG ? ? A CYS 74   A CYS 146  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf3 disulf ? ? A  CYS 102 SG  ? ? ? 1_555 A  CYS 191 SG ? ? A CYS 77   A CYS 166  1_555 ? ? ? ? ? ? ? 2.055 ? ? 
disulf4 disulf ? ? A  CYS 380 SG  ? ? ? 1_555 A  CYS 383 SG ? ? A CYS 259  A CYS 262  1_555 ? ? ? ? ? ? ? 2.040 ? ? 
metalc1 metalc ? ? A  ASP 77  OD1 ? ? ? 1_555 CA NA  .   NA ? ? A ASP 52   A NA  1228 1_555 ? ? ? ? ? ? ? 2.439 ? ? 
metalc2 metalc ? ? A  SER 116 OG  ? ? ? 1_555 CA NA  .   NA ? ? A SER 91   A NA  1228 1_555 ? ? ? ? ? ? ? 2.559 ? ? 
metalc3 metalc ? ? CA NA  .   NA  ? ? ? 1_555 DA HOH .   O  ? ? A NA  1228 A HOH 1339 1_555 ? ? ? ? ? ? ? 2.252 ? ? 
metalc4 metalc ? ? CA NA  .   NA  ? ? ? 1_555 DA HOH .   O  ? ? A NA  1228 A HOH 1364 1_555 ? ? ? ? ? ? ? 2.594 ? ? 
metalc5 metalc ? ? CA NA  .   NA  ? ? ? 1_555 DA HOH .   O  ? ? A NA  1228 A HOH 1383 1_555 ? ? ? ? ? ? ? 2.585 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A  ASP 77  ? A ASP 52   ? 1_555 NA ? CA NA . ? A NA 1228 ? 1_555 OG ? A  SER 116 ? A SER 91   ? 1_555 127.6 ? 
2  OD1 ? A  ASP 77  ? A ASP 52   ? 1_555 NA ? CA NA . ? A NA 1228 ? 1_555 O  ? DA HOH .   ? A HOH 1339 ? 1_555 87.2  ? 
3  OG  ? A  SER 116 ? A SER 91   ? 1_555 NA ? CA NA . ? A NA 1228 ? 1_555 O  ? DA HOH .   ? A HOH 1339 ? 1_555 115.0 ? 
4  OD1 ? A  ASP 77  ? A ASP 52   ? 1_555 NA ? CA NA . ? A NA 1228 ? 1_555 O  ? DA HOH .   ? A HOH 1364 ? 1_555 102.9 ? 
5  OG  ? A  SER 116 ? A SER 91   ? 1_555 NA ? CA NA . ? A NA 1228 ? 1_555 O  ? DA HOH .   ? A HOH 1364 ? 1_555 122.7 ? 
6  O   ? DA HOH .   ? A HOH 1339 ? 1_555 NA ? CA NA . ? A NA 1228 ? 1_555 O  ? DA HOH .   ? A HOH 1364 ? 1_555 89.9  ? 
7  OD1 ? A  ASP 77  ? A ASP 52   ? 1_555 NA ? CA NA . ? A NA 1228 ? 1_555 O  ? DA HOH .   ? A HOH 1383 ? 1_555 89.2  ? 
8  OG  ? A  SER 116 ? A SER 91   ? 1_555 NA ? CA NA . ? A NA 1228 ? 1_555 O  ? DA HOH .   ? A HOH 1383 ? 1_555 70.5  ? 
9  O   ? DA HOH .   ? A HOH 1339 ? 1_555 NA ? CA NA . ? A NA 1228 ? 1_555 O  ? DA HOH .   ? A HOH 1383 ? 1_555 174.5 ? 
10 O   ? DA HOH .   ? A HOH 1364 ? 1_555 NA ? CA NA . ? A NA 1228 ? 1_555 O  ? DA HOH .   ? A HOH 1383 ? 1_555 86.9  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 96  ? CYS A 184 ? CYS A 71  ? 1_555 CYS A 159 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 99  ? CYS A 171 ? CYS A 74  ? 1_555 CYS A 146 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 102 ? CYS A 191 ? CYS A 77  ? 1_555 CYS A 166 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS A 380 ? CYS A 383 ? CYS A 259 ? 1_555 CYS A 262 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        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 CYS A 96  ? ALA A 98  ? CYS A 71  ALA A 73  
AA1 2 GLN A 188 ? ALA A 190 ? GLN A 163 ALA A 165 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   ALA 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    97 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    ALA 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     72 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   VAL 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    189 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    VAL 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     164 
# 
_pdbx_entry_details.entry_id                   8RW0 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 LEU A 58   ? ? -120.82 -50.96 
2 1 TYR A 1101 ? ? -124.98 -61.50 
# 
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 -24  ? A MET 1   
2  1 Y 1 A LYS -23  ? A LYS 2   
3  1 Y 1 A THR -22  ? A THR 3   
4  1 Y 1 A ILE -21  ? A ILE 4   
5  1 Y 1 A ILE -20  ? A ILE 5   
6  1 Y 1 A ALA -19  ? A ALA 6   
7  1 Y 1 A LEU -18  ? A LEU 7   
8  1 Y 1 A SER -17  ? A SER 8   
9  1 Y 1 A TYR -16  ? A TYR 9   
10 1 Y 1 A ILE -15  ? A ILE 10  
11 1 Y 1 A PHE -14  ? A PHE 11  
12 1 Y 1 A CYS -13  ? A CYS 12  
13 1 Y 1 A LEU -12  ? A LEU 13  
14 1 Y 1 A VAL -11  ? A VAL 14  
15 1 Y 1 A PHE -10  ? A PHE 15  
16 1 Y 1 A ALA -9   ? A ALA 16  
17 1 Y 1 A ASP -8   ? A ASP 17  
18 1 Y 1 A TYR -7   ? A TYR 18  
19 1 Y 1 A LYS -6   ? A LYS 19  
20 1 Y 1 A ASP -5   ? A ASP 20  
21 1 Y 1 A ASP -4   ? A ASP 21  
22 1 Y 1 A ASP -3   ? A ASP 22  
23 1 Y 1 A ASP -2   ? A ASP 23  
24 1 Y 1 A GLY -1   ? A GLY 24  
25 1 Y 1 A ALA 1043 ? A ALA 276 
26 1 Y 1 A THR 1044 ? A THR 277 
27 1 Y 1 A PRO 1045 ? A PRO 278 
28 1 Y 1 A PRO 1046 ? A PRO 279 
29 1 Y 1 A LYS 1047 ? A LYS 280 
30 1 Y 1 A LEU 1048 ? A LEU 281 
31 1 Y 1 A GLU 1049 ? A GLU 282 
32 1 Y 1 A ASP 1050 ? A ASP 283 
33 1 Y 1 A LYS 1051 ? A LYS 284 
34 1 Y 1 A SER 1052 ? A SER 285 
35 1 Y 1 A PRO 1053 ? A PRO 286 
36 1 Y 1 A ASP 1054 ? A ASP 287 
37 1 Y 1 A SER 1055 ? A SER 288 
38 1 Y 1 A PRO 1056 ? A PRO 289 
39 1 Y 1 A GLU 1057 ? A GLU 290 
40 1 Y 1 A MET 1058 ? A MET 291 
41 1 Y 1 A HIS 306  ? A HIS 427 
42 1 Y 1 A VAL 307  ? A VAL 428 
43 1 Y 1 A LEU 308  ? A LEU 429 
44 1 Y 1 A ARG 309  ? A ARG 430 
45 1 Y 1 A GLN 310  ? A GLN 431 
46 1 Y 1 A GLN 311  ? A GLN 432 
47 1 Y 1 A GLU 312  ? A GLU 433 
48 1 Y 1 A PRO 313  ? A PRO 434 
49 1 Y 1 A PHE 314  ? A PHE 435 
50 1 Y 1 A LYS 315  ? A LYS 436 
51 1 Y 1 A ALA 316  ? A ALA 437 
52 1 Y 1 A ALA 317  ? A ALA 438 
53 1 Y 1 A ALA 318  ? A ALA 439 
54 1 Y 1 A HIS 319  ? A HIS 440 
55 1 Y 1 A HIS 320  ? A HIS 441 
56 1 Y 1 A HIS 321  ? A HIS 442 
57 1 Y 1 A HIS 322  ? A HIS 443 
58 1 Y 1 A HIS 323  ? A HIS 444 
59 1 Y 1 A HIS 324  ? A HIS 445 
60 1 Y 1 A HIS 325  ? A HIS 446 
61 1 Y 1 A HIS 326  ? A HIS 447 
62 1 Y 1 A HIS 327  ? A HIS 448 
63 1 Y 1 A HIS 328  ? A HIS 449 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N     N  N N 1   
ALA CA    C  N S 2   
ALA C     C  N N 3   
ALA O     O  N N 4   
ALA CB    C  N N 5   
ALA OXT   O  N N 6   
ALA H     H  N N 7   
ALA H2    H  N N 8   
ALA HA    H  N N 9   
ALA HB1   H  N N 10  
ALA HB2   H  N N 11  
ALA HB3   H  N N 12  
ALA HXT   H  N N 13  
ARG N     N  N N 14  
ARG CA    C  N S 15  
ARG C     C  N N 16  
ARG O     O  N N 17  
ARG CB    C  N N 18  
ARG CG    C  N N 19  
ARG CD    C  N N 20  
ARG NE    N  N N 21  
ARG CZ    C  N N 22  
ARG NH1   N  N N 23  
ARG NH2   N  N N 24  
ARG OXT   O  N N 25  
ARG H     H  N N 26  
ARG H2    H  N N 27  
ARG HA    H  N N 28  
ARG HB2   H  N N 29  
ARG HB3   H  N N 30  
ARG HG2   H  N N 31  
ARG HG3   H  N N 32  
ARG HD2   H  N N 33  
ARG HD3   H  N N 34  
ARG HE    H  N N 35  
ARG HH11  H  N N 36  
ARG HH12  H  N N 37  
ARG HH21  H  N N 38  
ARG HH22  H  N N 39  
ARG HXT   H  N N 40  
ASN N     N  N N 41  
ASN CA    C  N S 42  
ASN C     C  N N 43  
ASN O     O  N N 44  
ASN CB    C  N N 45  
ASN CG    C  N N 46  
ASN OD1   O  N N 47  
ASN ND2   N  N N 48  
ASN OXT   O  N N 49  
ASN H     H  N N 50  
ASN H2    H  N N 51  
ASN HA    H  N N 52  
ASN HB2   H  N N 53  
ASN HB3   H  N N 54  
ASN HD21  H  N N 55  
ASN HD22  H  N N 56  
ASN HXT   H  N N 57  
ASP N     N  N N 58  
ASP CA    C  N S 59  
ASP C     C  N N 60  
ASP O     O  N N 61  
ASP CB    C  N N 62  
ASP CG    C  N N 63  
ASP OD1   O  N N 64  
ASP OD2   O  N N 65  
ASP OXT   O  N N 66  
ASP H     H  N N 67  
ASP H2    H  N N 68  
ASP HA    H  N N 69  
ASP HB2   H  N N 70  
ASP HB3   H  N N 71  
ASP HD2   H  N N 72  
ASP HXT   H  N N 73  
CLR C1    C  N N 74  
CLR C2    C  N N 75  
CLR C3    C  N S 76  
CLR C4    C  N N 77  
CLR C5    C  N N 78  
CLR C6    C  N N 79  
CLR C7    C  N N 80  
CLR C8    C  N S 81  
CLR C9    C  N S 82  
CLR C10   C  N R 83  
CLR C11   C  N N 84  
CLR C12   C  N N 85  
CLR C13   C  N R 86  
CLR C14   C  N S 87  
CLR C15   C  N N 88  
CLR C16   C  N N 89  
CLR C17   C  N R 90  
CLR C18   C  N N 91  
CLR C19   C  N N 92  
CLR C20   C  N R 93  
CLR C21   C  N N 94  
CLR C22   C  N N 95  
CLR C23   C  N N 96  
CLR C24   C  N N 97  
CLR C25   C  N N 98  
CLR C26   C  N N 99  
CLR C27   C  N N 100 
CLR O1    O  N N 101 
CLR H11   H  N N 102 
CLR H12   H  N N 103 
CLR H21   H  N N 104 
CLR H22   H  N N 105 
CLR H3    H  N N 106 
CLR H41   H  N N 107 
CLR H42   H  N N 108 
CLR H6    H  N N 109 
CLR H71   H  N N 110 
CLR H72   H  N N 111 
CLR H8    H  N N 112 
CLR H9    H  N N 113 
CLR H111  H  N N 114 
CLR H112  H  N N 115 
CLR H121  H  N N 116 
CLR H122  H  N N 117 
CLR H14   H  N N 118 
CLR H151  H  N N 119 
CLR H152  H  N N 120 
CLR H161  H  N N 121 
CLR H162  H  N N 122 
CLR H17   H  N N 123 
CLR H181  H  N N 124 
CLR H182  H  N N 125 
CLR H183  H  N N 126 
CLR H191  H  N N 127 
CLR H192  H  N N 128 
CLR H193  H  N N 129 
CLR H20   H  N N 130 
CLR H211  H  N N 131 
CLR H212  H  N N 132 
CLR H213  H  N N 133 
CLR H221  H  N N 134 
CLR H222  H  N N 135 
CLR H231  H  N N 136 
CLR H232  H  N N 137 
CLR H241  H  N N 138 
CLR H242  H  N N 139 
CLR H25   H  N N 140 
CLR H261  H  N N 141 
CLR H262  H  N N 142 
CLR H263  H  N N 143 
CLR H271  H  N N 144 
CLR H272  H  N N 145 
CLR H273  H  N N 146 
CLR H1    H  N N 147 
CYS N     N  N N 148 
CYS CA    C  N R 149 
CYS C     C  N N 150 
CYS O     O  N N 151 
CYS CB    C  N N 152 
CYS SG    S  N N 153 
CYS OXT   O  N N 154 
CYS H     H  N N 155 
CYS H2    H  N N 156 
CYS HA    H  N N 157 
CYS HB2   H  N N 158 
CYS HB3   H  N N 159 
CYS HG    H  N N 160 
CYS HXT   H  N N 161 
GLN N     N  N N 162 
GLN CA    C  N S 163 
GLN C     C  N N 164 
GLN O     O  N N 165 
GLN CB    C  N N 166 
GLN CG    C  N N 167 
GLN CD    C  N N 168 
GLN OE1   O  N N 169 
GLN NE2   N  N N 170 
GLN OXT   O  N N 171 
GLN H     H  N N 172 
GLN H2    H  N N 173 
GLN HA    H  N N 174 
GLN HB2   H  N N 175 
GLN HB3   H  N N 176 
GLN HG2   H  N N 177 
GLN HG3   H  N N 178 
GLN HE21  H  N N 179 
GLN HE22  H  N N 180 
GLN HXT   H  N N 181 
GLU N     N  N N 182 
GLU CA    C  N S 183 
GLU C     C  N N 184 
GLU O     O  N N 185 
GLU CB    C  N N 186 
GLU CG    C  N N 187 
GLU CD    C  N N 188 
GLU OE1   O  N N 189 
GLU OE2   O  N N 190 
GLU OXT   O  N N 191 
GLU H     H  N N 192 
GLU H2    H  N N 193 
GLU HA    H  N N 194 
GLU HB2   H  N N 195 
GLU HB3   H  N N 196 
GLU HG2   H  N N 197 
GLU HG3   H  N N 198 
GLU HE2   H  N N 199 
GLU HXT   H  N N 200 
GLY N     N  N N 201 
GLY CA    C  N N 202 
GLY C     C  N N 203 
GLY O     O  N N 204 
GLY OXT   O  N N 205 
GLY H     H  N N 206 
GLY H2    H  N N 207 
GLY HA2   H  N N 208 
GLY HA3   H  N N 209 
GLY HXT   H  N N 210 
HIS N     N  N N 211 
HIS CA    C  N S 212 
HIS C     C  N N 213 
HIS O     O  N N 214 
HIS CB    C  N N 215 
HIS CG    C  Y N 216 
HIS ND1   N  Y N 217 
HIS CD2   C  Y N 218 
HIS CE1   C  Y N 219 
HIS NE2   N  Y N 220 
HIS OXT   O  N N 221 
HIS H     H  N N 222 
HIS H2    H  N N 223 
HIS HA    H  N N 224 
HIS HB2   H  N N 225 
HIS HB3   H  N N 226 
HIS HD1   H  N N 227 
HIS HD2   H  N N 228 
HIS HE1   H  N N 229 
HIS HE2   H  N N 230 
HIS HXT   H  N N 231 
HOH O     O  N N 232 
HOH H1    H  N N 233 
HOH H2    H  N N 234 
ILE N     N  N N 235 
ILE CA    C  N S 236 
ILE C     C  N N 237 
ILE O     O  N N 238 
ILE CB    C  N S 239 
ILE CG1   C  N N 240 
ILE CG2   C  N N 241 
ILE CD1   C  N N 242 
ILE OXT   O  N N 243 
ILE H     H  N N 244 
ILE H2    H  N N 245 
ILE HA    H  N N 246 
ILE HB    H  N N 247 
ILE HG12  H  N N 248 
ILE HG13  H  N N 249 
ILE HG21  H  N N 250 
ILE HG22  H  N N 251 
ILE HG23  H  N N 252 
ILE HD11  H  N N 253 
ILE HD12  H  N N 254 
ILE HD13  H  N N 255 
ILE HXT   H  N N 256 
JQ9 N1    N  N N 257 
JQ9 C12   C  N N 258 
JQ9 O2    O  N N 259 
JQ9 C2    C  N N 260 
JQ9 N3    N  N N 261 
JQ9 C21   C  N N 262 
JQ9 C22   C  N N 263 
JQ9 C4    C  Y N 264 
JQ9 N9    N  Y N 265 
JQ9 C8    C  Y N 266 
JQ9 N7    N  Y N 267 
JQ9 C7    C  N N 268 
JQ9 C5    C  Y N 269 
JQ9 C6    C  N N 270 
JQ9 O6    O  N N 271 
JQ9 C11   C  N N 272 
JQ9 CA    C  N N 273 
JQ9 CB    C  N N 274 
JQ9 "C1'" C  Y N 275 
JQ9 "C6'" C  Y N 276 
JQ9 "C5'" C  Y N 277 
JQ9 "C4'" C  Y N 278 
JQ9 "O4'" O  N N 279 
JQ9 "C8'" C  N N 280 
JQ9 "C3'" C  Y N 281 
JQ9 "C2'" C  Y N 282 
JQ9 "O3'" O  N N 283 
JQ9 "C9'" C  N N 284 
JQ9 H1    H  N N 285 
JQ9 H2    H  N N 286 
JQ9 H3    H  N N 287 
JQ9 H4    H  N N 288 
JQ9 H5    H  N N 289 
JQ9 H6    H  N N 290 
JQ9 H7    H  N N 291 
JQ9 H8    H  N N 292 
JQ9 H9    H  N N 293 
JQ9 H10   H  N N 294 
JQ9 H11   H  N N 295 
JQ9 H12   H  N N 296 
JQ9 H13   H  N N 297 
JQ9 H14   H  N N 298 
JQ9 H15   H  N N 299 
JQ9 H16   H  N N 300 
JQ9 H17   H  N N 301 
JQ9 H18   H  N N 302 
JQ9 H19   H  N N 303 
JQ9 H20   H  N N 304 
JQ9 H21   H  N N 305 
JQ9 H22   H  N N 306 
JQ9 H23   H  N N 307 
JQ9 H24   H  N N 308 
LEU N     N  N N 309 
LEU CA    C  N S 310 
LEU C     C  N N 311 
LEU O     O  N N 312 
LEU CB    C  N N 313 
LEU CG    C  N N 314 
LEU CD1   C  N N 315 
LEU CD2   C  N N 316 
LEU OXT   O  N N 317 
LEU H     H  N N 318 
LEU H2    H  N N 319 
LEU HA    H  N N 320 
LEU HB2   H  N N 321 
LEU HB3   H  N N 322 
LEU HG    H  N N 323 
LEU HD11  H  N N 324 
LEU HD12  H  N N 325 
LEU HD13  H  N N 326 
LEU HD21  H  N N 327 
LEU HD22  H  N N 328 
LEU HD23  H  N N 329 
LEU HXT   H  N N 330 
LYS N     N  N N 331 
LYS CA    C  N S 332 
LYS C     C  N N 333 
LYS O     O  N N 334 
LYS CB    C  N N 335 
LYS CG    C  N N 336 
LYS CD    C  N N 337 
LYS CE    C  N N 338 
LYS NZ    N  N N 339 
LYS OXT   O  N N 340 
LYS H     H  N N 341 
LYS H2    H  N N 342 
LYS HA    H  N N 343 
LYS HB2   H  N N 344 
LYS HB3   H  N N 345 
LYS HG2   H  N N 346 
LYS HG3   H  N N 347 
LYS HD2   H  N N 348 
LYS HD3   H  N N 349 
LYS HE2   H  N N 350 
LYS HE3   H  N N 351 
LYS HZ1   H  N N 352 
LYS HZ2   H  N N 353 
LYS HZ3   H  N N 354 
LYS HXT   H  N N 355 
MET N     N  N N 356 
MET CA    C  N S 357 
MET C     C  N N 358 
MET O     O  N N 359 
MET CB    C  N N 360 
MET CG    C  N N 361 
MET SD    S  N N 362 
MET CE    C  N N 363 
MET OXT   O  N N 364 
MET H     H  N N 365 
MET H2    H  N N 366 
MET HA    H  N N 367 
MET HB2   H  N N 368 
MET HB3   H  N N 369 
MET HG2   H  N N 370 
MET HG3   H  N N 371 
MET HE1   H  N N 372 
MET HE2   H  N N 373 
MET HE3   H  N N 374 
MET HXT   H  N N 375 
NA  NA    NA N N 376 
OLA C1    C  N N 377 
OLA O1    O  N N 378 
OLA O2    O  N N 379 
OLA C2    C  N N 380 
OLA C3    C  N N 381 
OLA C4    C  N N 382 
OLA C5    C  N N 383 
OLA C6    C  N N 384 
OLA C7    C  N N 385 
OLA C8    C  N N 386 
OLA C9    C  N N 387 
OLA C10   C  N N 388 
OLA C11   C  N N 389 
OLA C12   C  N N 390 
OLA C13   C  N N 391 
OLA C14   C  N N 392 
OLA C15   C  N N 393 
OLA C16   C  N N 394 
OLA C17   C  N N 395 
OLA C18   C  N N 396 
OLA HO2   H  N N 397 
OLA H21   H  N N 398 
OLA H22   H  N N 399 
OLA H31   H  N N 400 
OLA H32   H  N N 401 
OLA H41   H  N N 402 
OLA H42   H  N N 403 
OLA H51   H  N N 404 
OLA H52   H  N N 405 
OLA H61   H  N N 406 
OLA H62   H  N N 407 
OLA H71   H  N N 408 
OLA H72   H  N N 409 
OLA H81   H  N N 410 
OLA H82   H  N N 411 
OLA H9    H  N N 412 
OLA H10   H  N N 413 
OLA H111  H  N N 414 
OLA H112  H  N N 415 
OLA H121  H  N N 416 
OLA H122  H  N N 417 
OLA H131  H  N N 418 
OLA H132  H  N N 419 
OLA H141  H  N N 420 
OLA H142  H  N N 421 
OLA H151  H  N N 422 
OLA H152  H  N N 423 
OLA H161  H  N N 424 
OLA H162  H  N N 425 
OLA H171  H  N N 426 
OLA H172  H  N N 427 
OLA H181  H  N N 428 
OLA H182  H  N N 429 
OLA H183  H  N N 430 
PHE N     N  N N 431 
PHE CA    C  N S 432 
PHE C     C  N N 433 
PHE O     O  N N 434 
PHE CB    C  N N 435 
PHE CG    C  Y N 436 
PHE CD1   C  Y N 437 
PHE CD2   C  Y N 438 
PHE CE1   C  Y N 439 
PHE CE2   C  Y N 440 
PHE CZ    C  Y N 441 
PHE OXT   O  N N 442 
PHE H     H  N N 443 
PHE H2    H  N N 444 
PHE HA    H  N N 445 
PHE HB2   H  N N 446 
PHE HB3   H  N N 447 
PHE HD1   H  N N 448 
PHE HD2   H  N N 449 
PHE HE1   H  N N 450 
PHE HE2   H  N N 451 
PHE HZ    H  N N 452 
PHE HXT   H  N N 453 
PRO N     N  N N 454 
PRO CA    C  N S 455 
PRO C     C  N N 456 
PRO O     O  N N 457 
PRO CB    C  N N 458 
PRO CG    C  N N 459 
PRO CD    C  N N 460 
PRO OXT   O  N N 461 
PRO H     H  N N 462 
PRO HA    H  N N 463 
PRO HB2   H  N N 464 
PRO HB3   H  N N 465 
PRO HG2   H  N N 466 
PRO HG3   H  N N 467 
PRO HD2   H  N N 468 
PRO HD3   H  N N 469 
PRO HXT   H  N N 470 
SER N     N  N N 471 
SER CA    C  N S 472 
SER C     C  N N 473 
SER O     O  N N 474 
SER CB    C  N N 475 
SER OG    O  N N 476 
SER OXT   O  N N 477 
SER H     H  N N 478 
SER H2    H  N N 479 
SER HA    H  N N 480 
SER HB2   H  N N 481 
SER HB3   H  N N 482 
SER HG    H  N N 483 
SER HXT   H  N N 484 
THR N     N  N N 485 
THR CA    C  N S 486 
THR C     C  N N 487 
THR O     O  N N 488 
THR CB    C  N R 489 
THR OG1   O  N N 490 
THR CG2   C  N N 491 
THR OXT   O  N N 492 
THR H     H  N N 493 
THR H2    H  N N 494 
THR HA    H  N N 495 
THR HB    H  N N 496 
THR HG1   H  N N 497 
THR HG21  H  N N 498 
THR HG22  H  N N 499 
THR HG23  H  N N 500 
THR HXT   H  N N 501 
TRP N     N  N N 502 
TRP CA    C  N S 503 
TRP C     C  N N 504 
TRP O     O  N N 505 
TRP CB    C  N N 506 
TRP CG    C  Y N 507 
TRP CD1   C  Y N 508 
TRP CD2   C  Y N 509 
TRP NE1   N  Y N 510 
TRP CE2   C  Y N 511 
TRP CE3   C  Y N 512 
TRP CZ2   C  Y N 513 
TRP CZ3   C  Y N 514 
TRP CH2   C  Y N 515 
TRP OXT   O  N N 516 
TRP H     H  N N 517 
TRP H2    H  N N 518 
TRP HA    H  N N 519 
TRP HB2   H  N N 520 
TRP HB3   H  N N 521 
TRP HD1   H  N N 522 
TRP HE1   H  N N 523 
TRP HE3   H  N N 524 
TRP HZ2   H  N N 525 
TRP HZ3   H  N N 526 
TRP HH2   H  N N 527 
TRP HXT   H  N N 528 
TYR N     N  N N 529 
TYR CA    C  N S 530 
TYR C     C  N N 531 
TYR O     O  N N 532 
TYR CB    C  N N 533 
TYR CG    C  Y N 534 
TYR CD1   C  Y N 535 
TYR CD2   C  Y N 536 
TYR CE1   C  Y N 537 
TYR CE2   C  Y N 538 
TYR CZ    C  Y N 539 
TYR OH    O  N N 540 
TYR OXT   O  N N 541 
TYR H     H  N N 542 
TYR H2    H  N N 543 
TYR HA    H  N N 544 
TYR HB2   H  N N 545 
TYR HB3   H  N N 546 
TYR HD1   H  N N 547 
TYR HD2   H  N N 548 
TYR HE1   H  N N 549 
TYR HE2   H  N N 550 
TYR HH    H  N N 551 
TYR HXT   H  N N 552 
VAL N     N  N N 553 
VAL CA    C  N S 554 
VAL C     C  N N 555 
VAL O     O  N N 556 
VAL CB    C  N N 557 
VAL CG1   C  N N 558 
VAL CG2   C  N N 559 
VAL OXT   O  N N 560 
VAL H     H  N N 561 
VAL H2    H  N N 562 
VAL HA    H  N N 563 
VAL HB    H  N N 564 
VAL HG11  H  N N 565 
VAL HG12  H  N N 566 
VAL HG13  H  N N 567 
VAL HG21  H  N N 568 
VAL HG22  H  N N 569 
VAL HG23  H  N N 570 
VAL HXT   H  N N 571 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA    sing N N 1   
ALA N     H     sing N N 2   
ALA N     H2    sing N N 3   
ALA CA    C     sing N N 4   
ALA CA    CB    sing N N 5   
ALA CA    HA    sing N N 6   
ALA C     O     doub N N 7   
ALA C     OXT   sing N N 8   
ALA CB    HB1   sing N N 9   
ALA CB    HB2   sing N N 10  
ALA CB    HB3   sing N N 11  
ALA OXT   HXT   sing N N 12  
ARG N     CA    sing N N 13  
ARG N     H     sing N N 14  
ARG N     H2    sing N N 15  
ARG CA    C     sing N N 16  
ARG CA    CB    sing N N 17  
ARG CA    HA    sing N N 18  
ARG C     O     doub N N 19  
ARG C     OXT   sing N N 20  
ARG CB    CG    sing N N 21  
ARG CB    HB2   sing N N 22  
ARG CB    HB3   sing N N 23  
ARG CG    CD    sing N N 24  
ARG CG    HG2   sing N N 25  
ARG CG    HG3   sing N N 26  
ARG CD    NE    sing N N 27  
ARG CD    HD2   sing N N 28  
ARG CD    HD3   sing N N 29  
ARG NE    CZ    sing N N 30  
ARG NE    HE    sing N N 31  
ARG CZ    NH1   sing N N 32  
ARG CZ    NH2   doub N N 33  
ARG NH1   HH11  sing N N 34  
ARG NH1   HH12  sing N N 35  
ARG NH2   HH21  sing N N 36  
ARG NH2   HH22  sing N N 37  
ARG OXT   HXT   sing N N 38  
ASN N     CA    sing N N 39  
ASN N     H     sing N N 40  
ASN N     H2    sing N N 41  
ASN CA    C     sing N N 42  
ASN CA    CB    sing N N 43  
ASN CA    HA    sing N N 44  
ASN C     O     doub N N 45  
ASN C     OXT   sing N N 46  
ASN CB    CG    sing N N 47  
ASN CB    HB2   sing N N 48  
ASN CB    HB3   sing N N 49  
ASN CG    OD1   doub N N 50  
ASN CG    ND2   sing N N 51  
ASN ND2   HD21  sing N N 52  
ASN ND2   HD22  sing N N 53  
ASN OXT   HXT   sing N N 54  
ASP N     CA    sing N N 55  
ASP N     H     sing N N 56  
ASP N     H2    sing N N 57  
ASP CA    C     sing N N 58  
ASP CA    CB    sing N N 59  
ASP CA    HA    sing N N 60  
ASP C     O     doub N N 61  
ASP C     OXT   sing N N 62  
ASP CB    CG    sing N N 63  
ASP CB    HB2   sing N N 64  
ASP CB    HB3   sing N N 65  
ASP CG    OD1   doub N N 66  
ASP CG    OD2   sing N N 67  
ASP OD2   HD2   sing N N 68  
ASP OXT   HXT   sing N N 69  
CLR C1    C2    sing N N 70  
CLR C1    C10   sing N N 71  
CLR C1    H11   sing N N 72  
CLR C1    H12   sing N N 73  
CLR C2    C3    sing N N 74  
CLR C2    H21   sing N N 75  
CLR C2    H22   sing N N 76  
CLR C3    C4    sing N N 77  
CLR C3    O1    sing N N 78  
CLR C3    H3    sing N N 79  
CLR C4    C5    sing N N 80  
CLR C4    H41   sing N N 81  
CLR C4    H42   sing N N 82  
CLR C5    C6    doub N N 83  
CLR C5    C10   sing N N 84  
CLR C6    C7    sing N N 85  
CLR C6    H6    sing N N 86  
CLR C7    C8    sing N N 87  
CLR C7    H71   sing N N 88  
CLR C7    H72   sing N N 89  
CLR C8    C9    sing N N 90  
CLR C8    C14   sing N N 91  
CLR C8    H8    sing N N 92  
CLR C9    C10   sing N N 93  
CLR C9    C11   sing N N 94  
CLR C9    H9    sing N N 95  
CLR C10   C19   sing N N 96  
CLR C11   C12   sing N N 97  
CLR C11   H111  sing N N 98  
CLR C11   H112  sing N N 99  
CLR C12   C13   sing N N 100 
CLR C12   H121  sing N N 101 
CLR C12   H122  sing N N 102 
CLR C13   C14   sing N N 103 
CLR C13   C17   sing N N 104 
CLR C13   C18   sing N N 105 
CLR C14   C15   sing N N 106 
CLR C14   H14   sing N N 107 
CLR C15   C16   sing N N 108 
CLR C15   H151  sing N N 109 
CLR C15   H152  sing N N 110 
CLR C16   C17   sing N N 111 
CLR C16   H161  sing N N 112 
CLR C16   H162  sing N N 113 
CLR C17   C20   sing N N 114 
CLR C17   H17   sing N N 115 
CLR C18   H181  sing N N 116 
CLR C18   H182  sing N N 117 
CLR C18   H183  sing N N 118 
CLR C19   H191  sing N N 119 
CLR C19   H192  sing N N 120 
CLR C19   H193  sing N N 121 
CLR C20   C21   sing N N 122 
CLR C20   C22   sing N N 123 
CLR C20   H20   sing N N 124 
CLR C21   H211  sing N N 125 
CLR C21   H212  sing N N 126 
CLR C21   H213  sing N N 127 
CLR C22   C23   sing N N 128 
CLR C22   H221  sing N N 129 
CLR C22   H222  sing N N 130 
CLR C23   C24   sing N N 131 
CLR C23   H231  sing N N 132 
CLR C23   H232  sing N N 133 
CLR C24   C25   sing N N 134 
CLR C24   H241  sing N N 135 
CLR C24   H242  sing N N 136 
CLR C25   C26   sing N N 137 
CLR C25   C27   sing N N 138 
CLR C25   H25   sing N N 139 
CLR C26   H261  sing N N 140 
CLR C26   H262  sing N N 141 
CLR C26   H263  sing N N 142 
CLR C27   H271  sing N N 143 
CLR C27   H272  sing N N 144 
CLR C27   H273  sing N N 145 
CLR O1    H1    sing N N 146 
CYS N     CA    sing N N 147 
CYS N     H     sing N N 148 
CYS N     H2    sing N N 149 
CYS CA    C     sing N N 150 
CYS CA    CB    sing N N 151 
CYS CA    HA    sing N N 152 
CYS C     O     doub N N 153 
CYS C     OXT   sing N N 154 
CYS CB    SG    sing N N 155 
CYS CB    HB2   sing N N 156 
CYS CB    HB3   sing N N 157 
CYS SG    HG    sing N N 158 
CYS OXT   HXT   sing N N 159 
GLN N     CA    sing N N 160 
GLN N     H     sing N N 161 
GLN N     H2    sing N N 162 
GLN CA    C     sing N N 163 
GLN CA    CB    sing N N 164 
GLN CA    HA    sing N N 165 
GLN C     O     doub N N 166 
GLN C     OXT   sing N N 167 
GLN CB    CG    sing N N 168 
GLN CB    HB2   sing N N 169 
GLN CB    HB3   sing N N 170 
GLN CG    CD    sing N N 171 
GLN CG    HG2   sing N N 172 
GLN CG    HG3   sing N N 173 
GLN CD    OE1   doub N N 174 
GLN CD    NE2   sing N N 175 
GLN NE2   HE21  sing N N 176 
GLN NE2   HE22  sing N N 177 
GLN OXT   HXT   sing N N 178 
GLU N     CA    sing N N 179 
GLU N     H     sing N N 180 
GLU N     H2    sing N N 181 
GLU CA    C     sing N N 182 
GLU CA    CB    sing N N 183 
GLU CA    HA    sing N N 184 
GLU C     O     doub N N 185 
GLU C     OXT   sing N N 186 
GLU CB    CG    sing N N 187 
GLU CB    HB2   sing N N 188 
GLU CB    HB3   sing N N 189 
GLU CG    CD    sing N N 190 
GLU CG    HG2   sing N N 191 
GLU CG    HG3   sing N N 192 
GLU CD    OE1   doub N N 193 
GLU CD    OE2   sing N N 194 
GLU OE2   HE2   sing N N 195 
GLU OXT   HXT   sing N N 196 
GLY N     CA    sing N N 197 
GLY N     H     sing N N 198 
GLY N     H2    sing N N 199 
GLY CA    C     sing N N 200 
GLY CA    HA2   sing N N 201 
GLY CA    HA3   sing N N 202 
GLY C     O     doub N N 203 
GLY C     OXT   sing N N 204 
GLY OXT   HXT   sing N N 205 
HIS N     CA    sing N N 206 
HIS N     H     sing N N 207 
HIS N     H2    sing N N 208 
HIS CA    C     sing N N 209 
HIS CA    CB    sing N N 210 
HIS CA    HA    sing N N 211 
HIS C     O     doub N N 212 
HIS C     OXT   sing N N 213 
HIS CB    CG    sing N N 214 
HIS CB    HB2   sing N N 215 
HIS CB    HB3   sing N N 216 
HIS CG    ND1   sing Y N 217 
HIS CG    CD2   doub Y N 218 
HIS ND1   CE1   doub Y N 219 
HIS ND1   HD1   sing N N 220 
HIS CD2   NE2   sing Y N 221 
HIS CD2   HD2   sing N N 222 
HIS CE1   NE2   sing Y N 223 
HIS CE1   HE1   sing N N 224 
HIS NE2   HE2   sing N N 225 
HIS OXT   HXT   sing N N 226 
HOH O     H1    sing N N 227 
HOH O     H2    sing N N 228 
ILE N     CA    sing N N 229 
ILE N     H     sing N N 230 
ILE N     H2    sing N N 231 
ILE CA    C     sing N N 232 
ILE CA    CB    sing N N 233 
ILE CA    HA    sing N N 234 
ILE C     O     doub N N 235 
ILE C     OXT   sing N N 236 
ILE CB    CG1   sing N N 237 
ILE CB    CG2   sing N N 238 
ILE CB    HB    sing N N 239 
ILE CG1   CD1   sing N N 240 
ILE CG1   HG12  sing N N 241 
ILE CG1   HG13  sing N N 242 
ILE CG2   HG21  sing N N 243 
ILE CG2   HG22  sing N N 244 
ILE CG2   HG23  sing N N 245 
ILE CD1   HD11  sing N N 246 
ILE CD1   HD12  sing N N 247 
ILE CD1   HD13  sing N N 248 
ILE OXT   HXT   sing N N 249 
JQ9 C22   C21   sing N N 250 
JQ9 C12   C11   sing N N 251 
JQ9 O2    C2    doub N N 252 
JQ9 C21   N3    sing N N 253 
JQ9 C2    N3    sing N N 254 
JQ9 C2    N1    sing N N 255 
JQ9 C11   N1    sing N N 256 
JQ9 N3    C4    sing N N 257 
JQ9 N1    C6    sing N N 258 
JQ9 C4    N9    sing Y N 259 
JQ9 C4    C5    doub Y N 260 
JQ9 C6    C5    sing N N 261 
JQ9 C6    O6    doub N N 262 
JQ9 N9    C8    doub Y N 263 
JQ9 C5    N7    sing Y N 264 
JQ9 C8    N7    sing Y N 265 
JQ9 C8    CA    sing N N 266 
JQ9 N7    C7    sing N N 267 
JQ9 CB    CA    doub N E 268 
JQ9 CB    "C1'" sing N N 269 
JQ9 "C2'" "C1'" doub Y N 270 
JQ9 "C2'" "C3'" sing Y N 271 
JQ9 "C9'" "O3'" sing N N 272 
JQ9 "C1'" "C6'" sing Y N 273 
JQ9 "O3'" "C3'" sing N N 274 
JQ9 "C3'" "C4'" doub Y N 275 
JQ9 "C6'" "C5'" doub Y N 276 
JQ9 "C4'" "C5'" sing Y N 277 
JQ9 "C4'" "O4'" sing N N 278 
JQ9 "O4'" "C8'" sing N N 279 
JQ9 C12   H1    sing N N 280 
JQ9 C12   H2    sing N N 281 
JQ9 C12   H3    sing N N 282 
JQ9 C21   H4    sing N N 283 
JQ9 C21   H5    sing N N 284 
JQ9 C22   H6    sing N N 285 
JQ9 C22   H7    sing N N 286 
JQ9 C22   H8    sing N N 287 
JQ9 C7    H9    sing N N 288 
JQ9 C7    H10   sing N N 289 
JQ9 C7    H11   sing N N 290 
JQ9 C11   H12   sing N N 291 
JQ9 C11   H13   sing N N 292 
JQ9 CA    H14   sing N N 293 
JQ9 CB    H15   sing N N 294 
JQ9 "C6'" H16   sing N N 295 
JQ9 "C5'" H17   sing N N 296 
JQ9 "C8'" H18   sing N N 297 
JQ9 "C8'" H19   sing N N 298 
JQ9 "C8'" H20   sing N N 299 
JQ9 "C2'" H21   sing N N 300 
JQ9 "C9'" H22   sing N N 301 
JQ9 "C9'" H23   sing N N 302 
JQ9 "C9'" H24   sing N N 303 
LEU N     CA    sing N N 304 
LEU N     H     sing N N 305 
LEU N     H2    sing N N 306 
LEU CA    C     sing N N 307 
LEU CA    CB    sing N N 308 
LEU CA    HA    sing N N 309 
LEU C     O     doub N N 310 
LEU C     OXT   sing N N 311 
LEU CB    CG    sing N N 312 
LEU CB    HB2   sing N N 313 
LEU CB    HB3   sing N N 314 
LEU CG    CD1   sing N N 315 
LEU CG    CD2   sing N N 316 
LEU CG    HG    sing N N 317 
LEU CD1   HD11  sing N N 318 
LEU CD1   HD12  sing N N 319 
LEU CD1   HD13  sing N N 320 
LEU CD2   HD21  sing N N 321 
LEU CD2   HD22  sing N N 322 
LEU CD2   HD23  sing N N 323 
LEU OXT   HXT   sing N N 324 
LYS N     CA    sing N N 325 
LYS N     H     sing N N 326 
LYS N     H2    sing N N 327 
LYS CA    C     sing N N 328 
LYS CA    CB    sing N N 329 
LYS CA    HA    sing N N 330 
LYS C     O     doub N N 331 
LYS C     OXT   sing N N 332 
LYS CB    CG    sing N N 333 
LYS CB    HB2   sing N N 334 
LYS CB    HB3   sing N N 335 
LYS CG    CD    sing N N 336 
LYS CG    HG2   sing N N 337 
LYS CG    HG3   sing N N 338 
LYS CD    CE    sing N N 339 
LYS CD    HD2   sing N N 340 
LYS CD    HD3   sing N N 341 
LYS CE    NZ    sing N N 342 
LYS CE    HE2   sing N N 343 
LYS CE    HE3   sing N N 344 
LYS NZ    HZ1   sing N N 345 
LYS NZ    HZ2   sing N N 346 
LYS NZ    HZ3   sing N N 347 
LYS OXT   HXT   sing N N 348 
MET N     CA    sing N N 349 
MET N     H     sing N N 350 
MET N     H2    sing N N 351 
MET CA    C     sing N N 352 
MET CA    CB    sing N N 353 
MET CA    HA    sing N N 354 
MET C     O     doub N N 355 
MET C     OXT   sing N N 356 
MET CB    CG    sing N N 357 
MET CB    HB2   sing N N 358 
MET CB    HB3   sing N N 359 
MET CG    SD    sing N N 360 
MET CG    HG2   sing N N 361 
MET CG    HG3   sing N N 362 
MET SD    CE    sing N N 363 
MET CE    HE1   sing N N 364 
MET CE    HE2   sing N N 365 
MET CE    HE3   sing N N 366 
MET OXT   HXT   sing N N 367 
OLA C1    O1    doub N N 368 
OLA C1    O2    sing N N 369 
OLA C1    C2    sing N N 370 
OLA O2    HO2   sing N N 371 
OLA C2    C3    sing N N 372 
OLA C2    H21   sing N N 373 
OLA C2    H22   sing N N 374 
OLA C3    C4    sing N N 375 
OLA C3    H31   sing N N 376 
OLA C3    H32   sing N N 377 
OLA C4    C5    sing N N 378 
OLA C4    H41   sing N N 379 
OLA C4    H42   sing N N 380 
OLA C5    C6    sing N N 381 
OLA C5    H51   sing N N 382 
OLA C5    H52   sing N N 383 
OLA C6    C7    sing N N 384 
OLA C6    H61   sing N N 385 
OLA C6    H62   sing N N 386 
OLA C7    C8    sing N N 387 
OLA C7    H71   sing N N 388 
OLA C7    H72   sing N N 389 
OLA C8    C9    sing N N 390 
OLA C8    H81   sing N N 391 
OLA C8    H82   sing N N 392 
OLA C9    C10   doub N Z 393 
OLA C9    H9    sing N N 394 
OLA C10   C11   sing N N 395 
OLA C10   H10   sing N N 396 
OLA C11   C12   sing N N 397 
OLA C11   H111  sing N N 398 
OLA C11   H112  sing N N 399 
OLA C12   C13   sing N N 400 
OLA C12   H121  sing N N 401 
OLA C12   H122  sing N N 402 
OLA C13   C14   sing N N 403 
OLA C13   H131  sing N N 404 
OLA C13   H132  sing N N 405 
OLA C14   C15   sing N N 406 
OLA C14   H141  sing N N 407 
OLA C14   H142  sing N N 408 
OLA C15   C16   sing N N 409 
OLA C15   H151  sing N N 410 
OLA C15   H152  sing N N 411 
OLA C16   C17   sing N N 412 
OLA C16   H161  sing N N 413 
OLA C16   H162  sing N N 414 
OLA C17   C18   sing N N 415 
OLA C17   H171  sing N N 416 
OLA C17   H172  sing N N 417 
OLA C18   H181  sing N N 418 
OLA C18   H182  sing N N 419 
OLA C18   H183  sing N N 420 
PHE N     CA    sing N N 421 
PHE N     H     sing N N 422 
PHE N     H2    sing N N 423 
PHE CA    C     sing N N 424 
PHE CA    CB    sing N N 425 
PHE CA    HA    sing N N 426 
PHE C     O     doub N N 427 
PHE C     OXT   sing N N 428 
PHE CB    CG    sing N N 429 
PHE CB    HB2   sing N N 430 
PHE CB    HB3   sing N N 431 
PHE CG    CD1   doub Y N 432 
PHE CG    CD2   sing Y N 433 
PHE CD1   CE1   sing Y N 434 
PHE CD1   HD1   sing N N 435 
PHE CD2   CE2   doub Y N 436 
PHE CD2   HD2   sing N N 437 
PHE CE1   CZ    doub Y N 438 
PHE CE1   HE1   sing N N 439 
PHE CE2   CZ    sing Y N 440 
PHE CE2   HE2   sing N N 441 
PHE CZ    HZ    sing N N 442 
PHE OXT   HXT   sing N N 443 
PRO N     CA    sing N N 444 
PRO N     CD    sing N N 445 
PRO N     H     sing N N 446 
PRO CA    C     sing N N 447 
PRO CA    CB    sing N N 448 
PRO CA    HA    sing N N 449 
PRO C     O     doub N N 450 
PRO C     OXT   sing N N 451 
PRO CB    CG    sing N N 452 
PRO CB    HB2   sing N N 453 
PRO CB    HB3   sing N N 454 
PRO CG    CD    sing N N 455 
PRO CG    HG2   sing N N 456 
PRO CG    HG3   sing N N 457 
PRO CD    HD2   sing N N 458 
PRO CD    HD3   sing N N 459 
PRO OXT   HXT   sing N N 460 
SER N     CA    sing N N 461 
SER N     H     sing N N 462 
SER N     H2    sing N N 463 
SER CA    C     sing N N 464 
SER CA    CB    sing N N 465 
SER CA    HA    sing N N 466 
SER C     O     doub N N 467 
SER C     OXT   sing N N 468 
SER CB    OG    sing N N 469 
SER CB    HB2   sing N N 470 
SER CB    HB3   sing N N 471 
SER OG    HG    sing N N 472 
SER OXT   HXT   sing N N 473 
THR N     CA    sing N N 474 
THR N     H     sing N N 475 
THR N     H2    sing N N 476 
THR CA    C     sing N N 477 
THR CA    CB    sing N N 478 
THR CA    HA    sing N N 479 
THR C     O     doub N N 480 
THR C     OXT   sing N N 481 
THR CB    OG1   sing N N 482 
THR CB    CG2   sing N N 483 
THR CB    HB    sing N N 484 
THR OG1   HG1   sing N N 485 
THR CG2   HG21  sing N N 486 
THR CG2   HG22  sing N N 487 
THR CG2   HG23  sing N N 488 
THR OXT   HXT   sing N N 489 
TRP N     CA    sing N N 490 
TRP N     H     sing N N 491 
TRP N     H2    sing N N 492 
TRP CA    C     sing N N 493 
TRP CA    CB    sing N N 494 
TRP CA    HA    sing N N 495 
TRP C     O     doub N N 496 
TRP C     OXT   sing N N 497 
TRP CB    CG    sing N N 498 
TRP CB    HB2   sing N N 499 
TRP CB    HB3   sing N N 500 
TRP CG    CD1   doub Y N 501 
TRP CG    CD2   sing Y N 502 
TRP CD1   NE1   sing Y N 503 
TRP CD1   HD1   sing N N 504 
TRP CD2   CE2   doub Y N 505 
TRP CD2   CE3   sing Y N 506 
TRP NE1   CE2   sing Y N 507 
TRP NE1   HE1   sing N N 508 
TRP CE2   CZ2   sing Y N 509 
TRP CE3   CZ3   doub Y N 510 
TRP CE3   HE3   sing N N 511 
TRP CZ2   CH2   doub Y N 512 
TRP CZ2   HZ2   sing N N 513 
TRP CZ3   CH2   sing Y N 514 
TRP CZ3   HZ3   sing N N 515 
TRP CH2   HH2   sing N N 516 
TRP OXT   HXT   sing N N 517 
TYR N     CA    sing N N 518 
TYR N     H     sing N N 519 
TYR N     H2    sing N N 520 
TYR CA    C     sing N N 521 
TYR CA    CB    sing N N 522 
TYR CA    HA    sing N N 523 
TYR C     O     doub N N 524 
TYR C     OXT   sing N N 525 
TYR CB    CG    sing N N 526 
TYR CB    HB2   sing N N 527 
TYR CB    HB3   sing N N 528 
TYR CG    CD1   doub Y N 529 
TYR CG    CD2   sing Y N 530 
TYR CD1   CE1   sing Y N 531 
TYR CD1   HD1   sing N N 532 
TYR CD2   CE2   doub Y N 533 
TYR CD2   HD2   sing N N 534 
TYR CE1   CZ    doub Y N 535 
TYR CE1   HE1   sing N N 536 
TYR CE2   CZ    sing Y N 537 
TYR CE2   HE2   sing N N 538 
TYR CZ    OH    sing N N 539 
TYR OH    HH    sing N N 540 
TYR OXT   HXT   sing N N 541 
VAL N     CA    sing N N 542 
VAL N     H     sing N N 543 
VAL N     H2    sing N N 544 
VAL CA    C     sing N N 545 
VAL CA    CB    sing N N 546 
VAL CA    HA    sing N N 547 
VAL C     O     doub N N 548 
VAL C     OXT   sing N N 549 
VAL CB    CG1   sing N N 550 
VAL CB    CG2   sing N N 551 
VAL CB    HB    sing N N 552 
VAL CG1   HG11  sing N N 553 
VAL CG1   HG12  sing N N 554 
VAL CG1   HG13  sing N N 555 
VAL CG2   HG21  sing N N 556 
VAL CG2   HG22  sing N N 557 
VAL CG2   HG23  sing N N 558 
VAL OXT   HXT   sing N N 559 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Swiss National Science Foundation' Switzerland 310030_207462   1 
'Swiss National Science Foundation' Switzerland 310030_197674   2 
'Swiss National Science Foundation' Switzerland CRSII4_213507   3 
'Other government'                  Switzerland '42711.1 IP-LS' 4 
'Swiss Nanoscience Institute'       Switzerland '#1904'         5 
'German Research Foundation (DFG)'  Germany     1850/4-3        6 
'German Research Foundation (DFG)'  Germany     ?               7 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5MZJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RW0 
_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]   0.025424 
_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]   0.005576 
_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]   0.007150 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . ALA A  1 25  ? 2.695   21.659  138.872 1.00 55.49 ? 0    ALA A N     1 
ATOM   2    C  CA    . ALA A  1 25  ? 3.857   21.026  139.484 1.00 56.67 ? 0    ALA A CA    1 
ATOM   3    C  C     . ALA A  1 25  ? 4.966   20.754  138.468 1.00 58.05 ? 0    ALA A C     1 
ATOM   4    O  O     . ALA A  1 25  ? 4.674   20.423  137.315 1.00 56.45 ? 0    ALA A O     1 
ATOM   5    C  CB    . ALA A  1 25  ? 3.437   19.739  140.131 1.00 53.31 ? 0    ALA A CB    1 
ATOM   6    N  N     . PRO A  1 26  ? 6.226   20.822  138.905 1.00 52.21 ? 1    PRO A N     1 
ATOM   7    C  CA    . PRO A  1 26  ? 7.356   20.591  137.978 1.00 49.70 ? 1    PRO A CA    1 
ATOM   8    C  C     . PRO A  1 26  ? 7.191   19.284  137.224 1.00 42.66 ? 1    PRO A C     1 
ATOM   9    O  O     . PRO A  1 26  ? 6.870   18.250  137.825 1.00 43.16 ? 1    PRO A O     1 
ATOM   10   C  CB    . PRO A  1 26  ? 8.580   20.556  138.902 1.00 45.08 ? 1    PRO A CB    1 
ATOM   11   C  CG    . PRO A  1 26  ? 8.182   21.403  140.092 1.00 45.41 ? 1    PRO A CG    1 
ATOM   12   C  CD    . PRO A  1 26  ? 6.684   21.200  140.262 1.00 48.23 ? 1    PRO A CD    1 
ATOM   13   N  N     . PRO A  1 27  ? 7.325   19.311  135.895 1.00 51.10 ? 2    PRO A N     1 
ATOM   14   C  CA    . PRO A  1 27  ? 7.057   18.096  135.111 1.00 46.88 ? 2    PRO A CA    1 
ATOM   15   C  C     . PRO A  1 27  ? 7.964   16.946  135.500 1.00 39.01 ? 2    PRO A C     1 
ATOM   16   O  O     . PRO A  1 27  ? 7.570   15.780  135.356 1.00 42.72 ? 2    PRO A O     1 
ATOM   17   C  CB    . PRO A  1 27  ? 7.305   18.542  133.656 1.00 52.77 ? 2    PRO A CB    1 
ATOM   18   C  CG    . PRO A  1 27  ? 7.210   20.026  133.685 1.00 56.81 ? 2    PRO A CG    1 
ATOM   19   C  CD    . PRO A  1 27  ? 7.732   20.437  135.033 1.00 58.03 ? 2    PRO A CD    1 
ATOM   20   N  N     . ILE A  1 28  ? 9.172   17.242  135.997 1.00 41.44 ? 3    ILE A N     1 
ATOM   21   C  CA    . ILE A  1 28  ? 10.101  16.173  136.325 1.00 38.04 ? 3    ILE A CA    1 
ATOM   22   C  C     . ILE A  1 28  ? 9.561   15.296  137.447 1.00 36.01 ? 3    ILE A C     1 
ATOM   23   O  O     . ILE A  1 28  ? 10.016  14.165  137.597 1.00 33.94 ? 3    ILE A O     1 
ATOM   24   C  CB    . ILE A  1 28  ? 11.467  16.772  136.727 1.00 37.27 ? 3    ILE A CB    1 
ATOM   25   C  CG1   . ILE A  1 28  ? 12.535  15.691  136.804 1.00 38.35 ? 3    ILE A CG1   1 
ATOM   26   C  CG2   . ILE A  1 28  ? 11.342  17.472  138.071 1.00 42.55 ? 3    ILE A CG2   1 
ATOM   27   C  CD1   . ILE A  1 28  ? 13.946  16.207  136.846 1.00 57.02 ? 3    ILE A CD1   1 
ATOM   28   N  N     . MET A  1 29  ? 8.578   15.769  138.226 1.00 32.31 ? 4    MET A N     1 
ATOM   29   C  CA    . MET A  1 29  ? 8.088   14.931  139.319 1.00 35.68 ? 4    MET A CA    1 
ATOM   30   C  C     . MET A  1 29  ? 7.165   13.823  138.797 1.00 30.28 ? 4    MET A C     1 
ATOM   31   O  O     . MET A  1 29  ? 7.406   12.638  139.047 1.00 30.99 ? 4    MET A O     1 
ATOM   32   C  CB    . MET A  1 29  ? 7.421   15.762  140.425 1.00 29.74 ? 4    MET A CB    1 
ATOM   33   C  CG    . MET A  1 29  ? 8.325   16.811  141.023 1.00 35.80 ? 4    MET A CG    1 
ATOM   34   S  SD    . MET A  1 29  ? 7.506   17.788  142.320 1.00 40.51 ? 4    MET A SD    1 
ATOM   35   C  CE    . MET A  1 29  ? 7.271   16.559  143.637 1.00 35.36 ? 4    MET A CE    1 
ATOM   36   N  N     . GLY A  1 30  ? 6.089   14.184  138.088 1.00 31.05 ? 5    GLY A N     1 
ATOM   37   C  CA    . GLY A  1 30  ? 5.257   13.155  137.469 1.00 30.18 ? 5    GLY A CA    1 
ATOM   38   C  C     . GLY A  1 30  ? 6.027   12.344  136.438 1.00 34.03 ? 5    GLY A C     1 
ATOM   39   O  O     . GLY A  1 30  ? 5.809   11.131  136.299 1.00 33.48 ? 5    GLY A O     1 
ATOM   40   N  N     . SER A  1 31  ? 6.980   12.981  135.743 1.00 30.83 ? 6    SER A N     1 
ATOM   41   C  CA    . SER A  1 31  ? 7.864   12.220  134.868 1.00 30.79 ? 6    SER A CA    1 
ATOM   42   C  C     . SER A  1 31  ? 8.628   11.156  135.648 1.00 33.92 ? 6    SER A C     1 
ATOM   43   O  O     . SER A  1 31  ? 8.790   10.031  135.165 1.00 27.08 ? 6    SER A O     1 
ATOM   44   C  CB    . SER A  1 31  ? 8.858   13.143  134.148 1.00 37.84 ? 6    SER A CB    1 
ATOM   45   O  OG    . SER A  1 31  ? 8.210   13.935  133.166 1.00 47.42 ? 6    SER A OG    1 
ATOM   46   N  N     . SER A  1 32  ? 9.141   11.508  136.836 1.00 26.93 ? 7    SER A N     1 
ATOM   47   C  CA    . SER A  1 32  ? 9.935   10.568  137.629 1.00 25.12 ? 7    SER A CA    1 
ATOM   48   C  C     . SER A  1 32  ? 9.140   9.321   137.969 1.00 20.89 ? 7    SER A C     1 
ATOM   49   O  O     . SER A  1 32  ? 9.691   8.214   137.979 1.00 23.50 ? 7    SER A O     1 
ATOM   50   C  CB    . SER A  1 32  ? 10.433  11.236  138.905 1.00 32.80 ? 7    SER A CB    1 
ATOM   51   O  OG    . SER A  1 32  ? 11.352  12.246  138.556 1.00 39.68 ? 7    SER A OG    1 
ATOM   52   N  N     . VAL A  1 33  ? 7.863   9.502   138.338 1.00 22.02 ? 8    VAL A N     1 
ATOM   53   C  CA    . VAL A  1 33  ? 6.989   8.376   138.665 1.00 20.90 ? 8    VAL A CA    1 
ATOM   54   C  C     . VAL A  1 33  ? 6.772   7.511   137.426 1.00 28.98 ? 8    VAL A C     1 
ATOM   55   O  O     . VAL A  1 33  ? 6.940   6.286   137.465 1.00 21.21 ? 8    VAL A O     1 
ATOM   56   C  CB    . VAL A  1 33  ? 5.650   8.891   139.224 1.00 27.41 ? 8    VAL A CB    1 
ATOM   57   C  CG1   . VAL A  1 33  ? 4.634   7.752   139.378 1.00 24.54 ? 8    VAL A CG1   1 
ATOM   58   C  CG2   . VAL A  1 33  ? 5.852   9.638   140.552 1.00 26.94 ? 8    VAL A CG2   1 
ATOM   59   N  N     . TYR A  1 34  ? 6.414   8.144   136.298 1.00 22.68 ? 9    TYR A N     1 
ATOM   60   C  CA    . TYR A  1 34  ? 6.201   7.395   135.061 1.00 23.34 ? 9    TYR A CA    1 
ATOM   61   C  C     . TYR A  1 34  ? 7.450   6.601   134.680 1.00 19.59 ? 9    TYR A C     1 
ATOM   62   O  O     . TYR A  1 34  ? 7.381   5.400   134.401 1.00 20.27 ? 9    TYR A O     1 
ATOM   63   C  CB    . TYR A  1 34  ? 5.814   8.371   133.933 1.00 33.12 ? 9    TYR A CB    1 
ATOM   64   C  CG    . TYR A  1 34  ? 5.863   7.762   132.527 1.00 20.79 ? 9    TYR A CG    1 
ATOM   65   C  CD1   . TYR A  1 34  ? 5.014   6.725   132.171 1.00 24.24 ? 9    TYR A CD1   1 
ATOM   66   C  CD2   . TYR A  1 34  ? 6.766   8.221   131.585 1.00 21.58 ? 9    TYR A CD2   1 
ATOM   67   C  CE1   . TYR A  1 34  ? 5.066   6.165   130.906 1.00 19.77 ? 9    TYR A CE1   1 
ATOM   68   C  CE2   . TYR A  1 34  ? 6.835   7.665   130.327 1.00 20.86 ? 9    TYR A CE2   1 
ATOM   69   C  CZ    . TYR A  1 34  ? 5.986   6.633   130.000 1.00 25.37 ? 9    TYR A CZ    1 
ATOM   70   O  OH    . TYR A  1 34  ? 6.031   6.072   128.741 1.00 25.08 ? 9    TYR A OH    1 
ATOM   71   N  N     . ILE A  1 35  ? 8.608   7.254   134.708 1.00 21.16 ? 10   ILE A N     1 
ATOM   72   C  CA    . ILE A  1 35  ? 9.847   6.620   134.283 1.00 18.71 ? 10   ILE A CA    1 
ATOM   73   C  C     . ILE A  1 35  ? 10.224  5.472   135.218 1.00 21.07 ? 10   ILE A C     1 
ATOM   74   O  O     . ILE A  1 35  ? 10.631  4.396   134.765 1.00 21.66 ? 10   ILE A O     1 
ATOM   75   C  CB    . ILE A  1 35  ? 10.958  7.684   134.187 1.00 24.42 ? 10   ILE A CB    1 
ATOM   76   C  CG1   . ILE A  1 35  ? 10.659  8.664   133.053 1.00 24.32 ? 10   ILE A CG1   1 
ATOM   77   C  CG2   . ILE A  1 35  ? 12.326  7.040   133.995 1.00 20.71 ? 10   ILE A CG2   1 
ATOM   78   C  CD1   . ILE A  1 35  ? 11.611  9.846   133.000 1.00 25.57 ? 10   ILE A CD1   1 
ATOM   79   N  N     . THR A  1 36  ? 10.074  5.667   136.532 1.00 19.59 ? 11   THR A N     1 
ATOM   80   C  CA    . THR A  1 36  ? 10.408  4.610   137.476 1.00 22.12 ? 11   THR A CA    1 
ATOM   81   C  C     . THR A  1 36  ? 9.525   3.397   137.256 1.00 17.82 ? 11   THR A C     1 
ATOM   82   O  O     . THR A  1 36  ? 10.006  2.259   137.295 1.00 21.46 ? 11   THR A O     1 
ATOM   83   C  CB    . THR A  1 36  ? 10.251  5.130   138.920 1.00 24.62 ? 11   THR A CB    1 
ATOM   84   O  OG1   . THR A  1 36  ? 11.084  6.282   139.101 1.00 20.08 ? 11   THR A OG1   1 
ATOM   85   C  CG2   . THR A  1 36  ? 10.644  4.072   139.941 1.00 20.06 ? 11   THR A CG2   1 
ATOM   86   N  N     . VAL A  1 37  ? 8.225   3.621   137.037 1.00 17.39 ? 12   VAL A N     1 
ATOM   87   C  CA    . VAL A  1 37  ? 7.313   2.518   136.774 1.00 19.67 ? 12   VAL A CA    1 
ATOM   88   C  C     . VAL A  1 37  ? 7.704   1.816   135.474 1.00 21.90 ? 12   VAL A C     1 
ATOM   89   O  O     . VAL A  1 37  ? 7.744   0.581   135.403 1.00 19.96 ? 12   VAL A O     1 
ATOM   90   C  CB    . VAL A  1 37  ? 5.863   3.034   136.754 1.00 21.16 ? 12   VAL A CB    1 
ATOM   91   C  CG1   . VAL A  1 37  ? 4.896   1.987   136.166 1.00 22.79 ? 12   VAL A CG1   1 
ATOM   92   C  CG2   . VAL A  1 37  ? 5.434   3.477   138.156 1.00 24.63 ? 12   VAL A CG2   1 
ATOM   93   N  N     . GLU A  1 38  ? 8.025   2.592   134.433 1.00 19.42 ? 13   GLU A N     1 
ATOM   94   C  CA    . GLU A  1 38  ? 8.430   1.983   133.163 1.00 18.02 ? 13   GLU A CA    1 
ATOM   95   C  C     . GLU A  1 38  ? 9.670   1.120   133.362 1.00 18.46 ? 13   GLU A C     1 
ATOM   96   O  O     . GLU A  1 38  ? 9.762   0.001   132.836 1.00 19.87 ? 13   GLU A O     1 
ATOM   97   C  CB    . GLU A  1 38  ? 8.724   3.066   132.111 1.00 21.11 ? 13   GLU A CB    1 
ATOM   98   C  CG    . GLU A  1 38  ? 7.486   3.797   131.594 1.00 19.59 ? 13   GLU A CG    1 
ATOM   99   C  CD    . GLU A  1 38  ? 6.775   3.073   130.464 1.00 31.79 ? 13   GLU A CD    1 
ATOM   100  O  OE1   . GLU A  1 38  ? 6.369   1.915   130.695 1.00 28.98 ? 13   GLU A OE1   1 
ATOM   101  O  OE2   . GLU A  1 38  ? 6.553   3.676   129.378 1.00 22.93 ? 13   GLU A OE2   1 
ATOM   102  N  N     . LEU A  1 39  ? 10.649  1.628   134.109 1.00 17.26 ? 14   LEU A N     1 
ATOM   103  C  CA    . LEU A  1 39  ? 11.860  0.842   134.339 1.00 16.38 ? 14   LEU A CA    1 
ATOM   104  C  C     . LEU A  1 39  ? 11.581  -0.441  135.110 1.00 18.16 ? 14   LEU A C     1 
ATOM   105  O  O     . LEU A  1 39  ? 12.127  -1.499  134.767 1.00 20.54 ? 14   LEU A O     1 
ATOM   106  C  CB    . LEU A  1 39  ? 12.912  1.689   135.060 1.00 23.46 ? 14   LEU A CB    1 
ATOM   107  C  CG    . LEU A  1 39  ? 13.460  2.817   134.174 1.00 25.58 ? 14   LEU A CG    1 
ATOM   108  C  CD1   . LEU A  1 39  ? 14.437  3.674   134.964 1.00 28.66 ? 14   LEU A CD1   1 
ATOM   109  C  CD2   . LEU A  1 39  ? 14.069  2.235   132.924 1.00 25.26 ? 14   LEU A CD2   1 
ATOM   110  N  N     . ALA A  1 40  ? 10.707  -0.378  136.126 1.00 19.82 ? 15   ALA A N     1 
ATOM   111  C  CA    . ALA A  1 40  ? 10.320  -1.587  136.860 1.00 21.10 ? 15   ALA A CA    1 
ATOM   112  C  C     . ALA A  1 40  ? 9.672   -2.618  135.938 1.00 22.50 ? 15   ALA A C     1 
ATOM   113  O  O     . ALA A  1 40  ? 9.998   -3.818  135.992 1.00 18.43 ? 15   ALA A O     1 
ATOM   114  C  CB    . ALA A  1 40  ? 9.332   -1.199  137.974 1.00 16.45 ? 15   ALA A CB    1 
ATOM   115  N  N     . ILE A  1 41  ? 8.800   -2.157  135.038 1.00 19.78 ? 16   ILE A N     1 
ATOM   116  C  CA    . ILE A  1 41  ? 8.139   -3.069  134.102 1.00 17.73 ? 16   ILE A CA    1 
ATOM   117  C  C     . ILE A  1 41  ? 9.169   -3.678  133.155 1.00 16.25 ? 16   ILE A C     1 
ATOM   118  O  O     . ILE A  1 41  ? 9.128   -4.880  132.847 1.00 21.20 ? 16   ILE A O     1 
ATOM   119  C  CB    . ILE A  1 41  ? 7.021   -2.320  133.351 1.00 20.30 ? 16   ILE A CB    1 
ATOM   120  C  CG1   . ILE A  1 41  ? 5.909   -1.943  134.323 1.00 19.55 ? 16   ILE A CG1   1 
ATOM   121  C  CG2   . ILE A  1 41  ? 6.446   -3.142  132.187 1.00 20.82 ? 16   ILE A CG2   1 
ATOM   122  C  CD1   . ILE A  1 41  ? 4.954   -0.954  133.763 1.00 18.27 ? 16   ILE A CD1   1 
ATOM   123  N  N     . ALA A  1 42  ? 10.123  -2.863  132.698 1.00 20.30 ? 17   ALA A N     1 
ATOM   124  C  CA    . ALA A  1 42  ? 11.145  -3.343  131.776 1.00 20.98 ? 17   ALA A CA    1 
ATOM   125  C  C     . ALA A  1 42  ? 11.969  -4.465  132.420 1.00 22.29 ? 17   ALA A C     1 
ATOM   126  O  O     . ALA A  1 42  ? 12.226  -5.504  131.798 1.00 21.81 ? 17   ALA A O     1 
ATOM   127  C  CB    . ALA A  1 42  ? 12.044  -2.167  131.359 1.00 17.34 ? 17   ALA A CB    1 
ATOM   128  N  N     . VAL A  1 43  ? 12.371  -4.281  133.680 1.00 24.24 ? 18   VAL A N     1 
ATOM   129  C  CA    . VAL A  1 43  ? 13.119  -5.326  134.387 1.00 19.70 ? 18   VAL A CA    1 
ATOM   130  C  C     . VAL A  1 43  ? 12.330  -6.624  134.410 1.00 20.75 ? 18   VAL A C     1 
ATOM   131  O  O     . VAL A  1 43  ? 12.866  -7.701  134.123 1.00 22.02 ? 18   VAL A O     1 
ATOM   132  C  CB    . VAL A  1 43  ? 13.466  -4.872  135.822 1.00 24.09 ? 18   VAL A CB    1 
ATOM   133  C  CG1   . VAL A  1 43  ? 13.956  -6.076  136.631 1.00 25.95 ? 18   VAL A CG1   1 
ATOM   134  C  CG2   . VAL A  1 43  ? 14.544  -3.789  135.779 1.00 21.30 ? 18   VAL A CG2   1 
ATOM   135  N  N     . LEU A  1 44  ? 11.058  -6.545  134.792 1.00 18.36 ? 19   LEU A N     1 
ATOM   136  C  CA    . LEU A  1 44  ? 10.244  -7.745  134.934 1.00 20.04 ? 19   LEU A CA    1 
ATOM   137  C  C     . LEU A  1 44  ? 9.959   -8.391  133.579 1.00 22.36 ? 19   LEU A C     1 
ATOM   138  O  O     . LEU A  1 44  ? 9.856   -9.623  133.484 1.00 21.54 ? 19   LEU A O     1 
ATOM   139  C  CB    . LEU A  1 44  ? 8.944   -7.398  135.652 1.00 22.20 ? 19   LEU A CB    1 
ATOM   140  C  CG    . LEU A  1 44  ? 9.087   -6.927  137.117 1.00 23.81 ? 19   LEU A CG    1 
ATOM   141  C  CD1   . LEU A  1 44  ? 7.763   -6.293  137.616 1.00 17.69 ? 19   LEU A CD1   1 
ATOM   142  C  CD2   . LEU A  1 44  ? 9.525   -8.088  138.040 1.00 25.22 ? 19   LEU A CD2   1 
ATOM   143  N  N     . ALA A  1 45  ? 9.774   -7.580  132.531 1.00 21.12 ? 20   ALA A N     1 
ATOM   144  C  CA    . ALA A  1 45  ? 9.529   -8.152  131.204 1.00 24.08 ? 20   ALA A CA    1 
ATOM   145  C  C     . ALA A  1 45  ? 10.736  -8.934  130.712 1.00 22.74 ? 20   ALA A C     1 
ATOM   146  O  O     . ALA A  1 45  ? 10.593  -10.031 130.152 1.00 21.53 ? 20   ALA A O     1 
ATOM   147  C  CB    . ALA A  1 45  ? 9.164   -7.058  130.192 1.00 14.17 ? 20   ALA A CB    1 
ATOM   148  N  N     . ILE A  1 46  ? 11.935  -8.387  130.926 1.00 18.57 ? 21   ILE A N     1 
ATOM   149  C  CA    . ILE A  1 46  ? 13.152  -9.076  130.519 1.00 19.72 ? 21   ILE A CA    1 
ATOM   150  C  C     . ILE A  1 46  ? 13.317  -10.371 131.307 1.00 25.00 ? 21   ILE A C     1 
ATOM   151  O  O     . ILE A  1 46  ? 13.501  -11.447 130.726 1.00 23.25 ? 21   ILE A O     1 
ATOM   152  C  CB    . ILE A  1 46  ? 14.370  -8.146  130.658 1.00 21.21 ? 21   ILE A CB    1 
ATOM   153  C  CG1   . ILE A  1 46  ? 14.224  -6.963  129.684 1.00 21.68 ? 21   ILE A CG1   1 
ATOM   154  C  CG2   . ILE A  1 46  ? 15.660  -8.934  130.425 1.00 28.01 ? 21   ILE A CG2   1 
ATOM   155  C  CD1   . ILE A  1 46  ? 15.131  -5.810  129.990 1.00 20.94 ? 21   ILE A CD1   1 
ATOM   156  N  N     . LEU A  1 47  ? 13.218  -10.295 132.637 1.00 23.68 ? 22   LEU A N     1 
ATOM   157  C  CA    . LEU A  1 47  ? 13.484  -11.473 133.460 1.00 18.82 ? 22   LEU A CA    1 
ATOM   158  C  C     . LEU A  1 47  ? 12.501  -12.609 133.164 1.00 26.46 ? 22   LEU A C     1 
ATOM   159  O  O     . LEU A  1 47  ? 12.902  -13.761 132.974 1.00 25.34 ? 22   LEU A O     1 
ATOM   160  C  CB    . LEU A  1 47  ? 13.377  -11.089 134.940 1.00 22.66 ? 22   LEU A CB    1 
ATOM   161  C  CG    . LEU A  1 47  ? 14.448  -10.148 135.483 1.00 23.85 ? 22   LEU A CG    1 
ATOM   162  C  CD1   . LEU A  1 47  ? 14.134  -9.794  136.954 1.00 28.22 ? 22   LEU A CD1   1 
ATOM   163  C  CD2   . LEU A  1 47  ? 15.795  -10.840 135.336 1.00 34.07 ? 22   LEU A CD2   1 
ATOM   164  N  N     . GLY A  1 48  ? 11.204  -12.307 133.102 1.00 20.08 ? 23   GLY A N     1 
ATOM   165  C  CA    . GLY A  1 48  ? 10.239  -13.373 132.926 1.00 20.80 ? 23   GLY A CA    1 
ATOM   166  C  C     . GLY A  1 48  ? 10.344  -14.027 131.563 1.00 23.31 ? 23   GLY A C     1 
ATOM   167  O  O     . GLY A  1 48  ? 10.239  -15.251 131.433 1.00 24.40 ? 23   GLY A O     1 
ATOM   168  N  N     . ASN A  1 49  ? 10.552  -13.223 130.526 1.00 19.97 ? 24   ASN A N     1 
ATOM   169  C  CA    . ASN A  1 49  ? 10.550  -13.788 129.185 1.00 19.30 ? 24   ASN A CA    1 
ATOM   170  C  C     . ASN A  1 49  ? 11.883  -14.422 128.815 1.00 24.13 ? 24   ASN A C     1 
ATOM   171  O  O     . ASN A  1 49  ? 11.898  -15.353 128.012 1.00 24.38 ? 24   ASN A O     1 
ATOM   172  C  CB    . ASN A  1 49  ? 10.123  -12.704 128.197 1.00 19.75 ? 24   ASN A CB    1 
ATOM   173  C  CG    . ASN A  1 49  ? 8.638   -12.414 128.308 1.00 23.29 ? 24   ASN A CG    1 
ATOM   174  O  OD1   . ASN A  1 49  ? 7.818   -13.244 127.911 1.00 20.66 ? 24   ASN A OD1   1 
ATOM   175  N  ND2   . ASN A  1 49  ? 8.280   -11.307 128.958 1.00 17.48 ? 24   ASN A ND2   1 
ATOM   176  N  N     . VAL A  1 50  ? 12.997  -13.948 129.376 1.00 21.26 ? 25   VAL A N     1 
ATOM   177  C  CA    . VAL A  1 50  ? 14.234  -14.728 129.316 1.00 26.25 ? 25   VAL A CA    1 
ATOM   178  C  C     . VAL A  1 50  ? 14.021  -16.103 129.941 1.00 26.43 ? 25   VAL A C     1 
ATOM   179  O  O     . VAL A  1 50  ? 14.505  -17.120 129.431 1.00 26.85 ? 25   VAL A O     1 
ATOM   180  C  CB    . VAL A  1 50  ? 15.382  -13.957 129.987 1.00 28.31 ? 25   VAL A CB    1 
ATOM   181  C  CG1   . VAL A  1 50  ? 16.529  -14.910 130.381 1.00 25.84 ? 25   VAL A CG1   1 
ATOM   182  C  CG2   . VAL A  1 50  ? 15.870  -12.834 129.067 1.00 25.70 ? 25   VAL A CG2   1 
ATOM   183  N  N     . LEU A  1 51  ? 13.298  -16.158 131.059 1.00 27.33 ? 26   LEU A N     1 
ATOM   184  C  CA    . LEU A  1 51  ? 13.020  -17.440 131.693 1.00 22.52 ? 26   LEU A CA    1 
ATOM   185  C  C     . LEU A  1 51  ? 12.200  -18.357 130.790 1.00 29.99 ? 26   LEU A C     1 
ATOM   186  O  O     . LEU A  1 51  ? 12.506  -19.553 130.658 1.00 26.08 ? 26   LEU A O     1 
ATOM   187  C  CB    . LEU A  1 51  ? 12.274  -17.183 133.004 1.00 27.86 ? 26   LEU A CB    1 
ATOM   188  C  CG    . LEU A  1 51  ? 12.078  -18.342 133.973 1.00 38.59 ? 26   LEU A CG    1 
ATOM   189  C  CD1   . LEU A  1 51  ? 13.409  -18.860 134.509 1.00 41.72 ? 26   LEU A CD1   1 
ATOM   190  C  CD2   . LEU A  1 51  ? 11.095  -17.938 135.102 1.00 36.05 ? 26   LEU A CD2   1 
ATOM   191  N  N     . VAL A  1 52  ? 11.220  -17.796 130.079 1.00 20.63 ? 27   VAL A N     1 
ATOM   192  C  CA    . VAL A  1 52  ? 10.443  -18.582 129.117 1.00 24.15 ? 27   VAL A CA    1 
ATOM   193  C  C     . VAL A  1 52  ? 11.360  -19.178 128.050 1.00 27.14 ? 27   VAL A C     1 
ATOM   194  O  O     . VAL A  1 52  ? 11.242  -20.359 127.689 1.00 27.20 ? 27   VAL A O     1 
ATOM   195  C  CB    . VAL A  1 52  ? 9.339   -17.707 128.485 1.00 25.30 ? 27   VAL A CB    1 
ATOM   196  C  CG1   . VAL A  1 52  ? 8.777   -18.382 127.227 1.00 21.62 ? 27   VAL A CG1   1 
ATOM   197  C  CG2   . VAL A  1 52  ? 8.252   -17.407 129.493 1.00 25.93 ? 27   VAL A CG2   1 
ATOM   198  N  N     . CYS A  1 53  ? 12.215  -18.332 127.454 1.00 23.21 ? 28   CYS A N     1 
ATOM   199  C  CA    . CYS A  1 53  ? 13.102  -18.776 126.381 1.00 26.59 ? 28   CYS A CA    1 
ATOM   200  C  C     . CYS A  1 53  ? 14.103  -19.811 126.888 1.00 33.95 ? 28   CYS A C     1 
ATOM   201  O  O     . CYS A  1 53  ? 14.386  -20.798 126.199 1.00 27.47 ? 28   CYS A O     1 
ATOM   202  C  CB    . CYS A  1 53  ? 13.848  -17.591 125.776 1.00 30.72 ? 28   CYS A CB    1 
ATOM   203  S  SG    . CYS A  1 53  ? 12.830  -16.393 124.893 1.00 27.80 ? 28   CYS A SG    1 
ATOM   204  N  N     . TRP A  1 54  ? 14.659  -19.601 128.086 1.00 30.44 ? 29   TRP A N     1 
ATOM   205  C  CA    A TRP A  1 54  ? 15.570  -20.597 128.638 0.48 31.20 ? 29   TRP A CA    1 
ATOM   206  C  CA    B TRP A  1 54  ? 15.565  -20.591 128.665 0.52 31.19 ? 29   TRP A CA    1 
ATOM   207  C  C     . TRP A  1 54  ? 14.862  -21.927 128.877 1.00 32.52 ? 29   TRP A C     1 
ATOM   208  O  O     . TRP A  1 54  ? 15.443  -22.988 128.634 1.00 30.44 ? 29   TRP A O     1 
ATOM   209  C  CB    A TRP A  1 54  ? 16.227  -20.085 129.922 0.48 33.52 ? 29   TRP A CB    1 
ATOM   210  C  CB    B TRP A  1 54  ? 16.156  -20.068 129.980 0.52 33.47 ? 29   TRP A CB    1 
ATOM   211  C  CG    A TRP A  1 54  ? 17.726  -20.171 129.824 0.48 42.81 ? 29   TRP A CG    1 
ATOM   212  C  CG    B TRP A  1 54  ? 17.532  -20.627 130.342 0.52 42.77 ? 29   TRP A CG    1 
ATOM   213  C  CD1   A TRP A  1 54  ? 18.476  -21.316 129.753 0.48 47.12 ? 29   TRP A CD1   1 
ATOM   214  C  CD1   B TRP A  1 54  ? 18.005  -20.862 131.604 0.52 43.19 ? 29   TRP A CD1   1 
ATOM   215  C  CD2   A TRP A  1 54  ? 18.657  -19.083 129.758 0.48 41.38 ? 29   TRP A CD2   1 
ATOM   216  C  CD2   B TRP A  1 54  ? 18.603  -21.003 129.443 0.52 47.17 ? 29   TRP A CD2   1 
ATOM   217  N  NE1   A TRP A  1 54  ? 19.811  -21.005 129.645 0.48 49.55 ? 29   TRP A NE1   1 
ATOM   218  N  NE1   B TRP A  1 54  ? 19.278  -21.373 131.551 0.52 43.37 ? 29   TRP A NE1   1 
ATOM   219  C  CE2   A TRP A  1 54  ? 19.949  -19.643 129.652 0.48 45.01 ? 29   TRP A CE2   1 
ATOM   220  C  CE2   B TRP A  1 54  ? 19.670  -21.470 130.240 0.52 49.39 ? 29   TRP A CE2   1 
ATOM   221  C  CE3   A TRP A  1 54  ? 18.527  -17.695 129.786 0.48 32.79 ? 29   TRP A CE3   1 
ATOM   222  C  CE3   B TRP A  1 54  ? 18.761  -20.992 128.049 0.52 42.96 ? 29   TRP A CE3   1 
ATOM   223  C  CZ2   A TRP A  1 54  ? 21.097  -18.859 129.576 0.48 46.21 ? 29   TRP A CZ2   1 
ATOM   224  C  CZ2   B TRP A  1 54  ? 20.873  -21.920 129.688 0.52 45.28 ? 29   TRP A CZ2   1 
ATOM   225  C  CZ3   A TRP A  1 54  ? 19.671  -16.919 129.715 0.48 41.96 ? 29   TRP A CZ3   1 
ATOM   226  C  CZ3   B TRP A  1 54  ? 19.951  -21.448 127.509 0.52 42.08 ? 29   TRP A CZ3   1 
ATOM   227  C  CH2   A TRP A  1 54  ? 20.937  -17.502 129.609 0.48 48.95 ? 29   TRP A CH2   1 
ATOM   228  C  CH2   B TRP A  1 54  ? 20.989  -21.900 128.326 0.52 44.36 ? 29   TRP A CH2   1 
ATOM   229  N  N     . ALA A  1 55  ? 13.599  -21.899 129.324 1.00 31.64 ? 30   ALA A N     1 
ATOM   230  C  CA    . ALA A  1 55  ? 12.882  -23.149 129.571 1.00 28.02 ? 30   ALA A CA    1 
ATOM   231  C  C     . ALA A  1 55  ? 12.701  -23.953 128.288 1.00 33.92 ? 30   ALA A C     1 
ATOM   232  O  O     . ALA A  1 55  ? 12.836  -25.181 128.290 1.00 32.19 ? 30   ALA A O     1 
ATOM   233  C  CB    . ALA A  1 55  ? 11.527  -22.878 130.221 1.00 25.76 ? 30   ALA A CB    1 
ATOM   234  N  N     . VAL A  1 56  ? 12.290  -23.292 127.206 1.00 30.00 ? 31   VAL A N     1 
ATOM   235  C  CA    . VAL A  1 56  ? 12.090  -23.989 125.945 1.00 27.76 ? 31   VAL A CA    1 
ATOM   236  C  C     . VAL A  1 56  ? 13.415  -24.530 125.419 1.00 33.84 ? 31   VAL A C     1 
ATOM   237  O  O     . VAL A  1 56  ? 13.482  -25.654 124.920 1.00 30.86 ? 31   VAL A O     1 
ATOM   238  C  CB    . VAL A  1 56  ? 11.410  -23.074 124.910 1.00 31.40 ? 31   VAL A CB    1 
ATOM   239  C  CG1   . VAL A  1 56  ? 11.297  -23.812 123.584 1.00 28.22 ? 31   VAL A CG1   1 
ATOM   240  C  CG2   . VAL A  1 56  ? 10.039  -22.669 125.393 1.00 30.62 ? 31   VAL A CG2   1 
ATOM   241  N  N     . TRP A  1 57  ? 14.479  -23.725 125.494 1.00 30.69 ? 32   TRP A N     1 
ATOM   242  C  CA    . TRP A  1 57  ? 15.786  -24.187 125.044 1.00 39.13 ? 32   TRP A CA    1 
ATOM   243  C  C     . TRP A  1 57  ? 16.239  -25.431 125.816 1.00 45.76 ? 32   TRP A C     1 
ATOM   244  O  O     . TRP A  1 57  ? 16.821  -26.354 125.234 1.00 43.54 ? 32   TRP A O     1 
ATOM   245  C  CB    . TRP A  1 57  ? 16.808  -23.068 125.185 1.00 37.33 ? 32   TRP A CB    1 
ATOM   246  C  CG    . TRP A  1 57  ? 18.229  -23.458 124.831 1.00 52.44 ? 32   TRP A CG    1 
ATOM   247  C  CD1   . TRP A  1 57  ? 19.090  -24.236 125.559 1.00 51.45 ? 32   TRP A CD1   1 
ATOM   248  C  CD2   . TRP A  1 57  ? 18.959  -23.037 123.670 1.00 58.79 ? 32   TRP A CD2   1 
ATOM   249  N  NE1   . TRP A  1 57  ? 20.296  -24.342 124.908 1.00 53.52 ? 32   TRP A NE1   1 
ATOM   250  C  CE2   . TRP A  1 57  ? 20.243  -23.613 123.749 1.00 58.03 ? 32   TRP A CE2   1 
ATOM   251  C  CE3   . TRP A  1 57  ? 18.648  -22.226 122.570 1.00 60.08 ? 32   TRP A CE3   1 
ATOM   252  C  CZ2   . TRP A  1 57  ? 21.216  -23.405 122.771 1.00 60.05 ? 32   TRP A CZ2   1 
ATOM   253  C  CZ3   . TRP A  1 57  ? 19.617  -22.019 121.594 1.00 58.62 ? 32   TRP A CZ3   1 
ATOM   254  C  CH2   . TRP A  1 57  ? 20.887  -22.604 121.704 1.00 61.62 ? 32   TRP A CH2   1 
ATOM   255  N  N     . LEU A  1 58  ? 15.984  -25.470 127.126 1.00 39.05 ? 33   LEU A N     1 
ATOM   256  C  CA    . LEU A  1 58  ? 16.519  -26.516 127.988 1.00 39.65 ? 33   LEU A CA    1 
ATOM   257  C  C     . LEU A  1 58  ? 15.676  -27.792 127.981 1.00 42.17 ? 33   LEU A C     1 
ATOM   258  O  O     . LEU A  1 58  ? 16.235  -28.881 128.151 1.00 50.74 ? 33   LEU A O     1 
ATOM   259  C  CB    . LEU A  1 58  ? 16.664  -26.003 129.427 1.00 37.10 ? 33   LEU A CB    1 
ATOM   260  C  CG    . LEU A  1 58  ? 17.792  -24.982 129.646 1.00 42.80 ? 33   LEU A CG    1 
ATOM   261  C  CD1   . LEU A  1 58  ? 17.852  -24.468 131.077 1.00 42.64 ? 33   LEU A CD1   1 
ATOM   262  C  CD2   . LEU A  1 58  ? 19.116  -25.589 129.248 1.00 41.95 ? 33   LEU A CD2   1 
ATOM   263  N  N     . ASN A  1 59  ? 14.353  -27.695 127.852 1.00 33.44 ? 34   ASN A N     1 
ATOM   264  C  CA    . ASN A  1 59  ? 13.448  -28.821 128.054 1.00 31.72 ? 34   ASN A CA    1 
ATOM   265  C  C     . ASN A  1 59  ? 12.866  -29.318 126.727 1.00 44.68 ? 34   ASN A C     1 
ATOM   266  O  O     . ASN A  1 59  ? 12.071  -28.619 126.089 1.00 35.47 ? 34   ASN A O     1 
ATOM   267  C  CB    . ASN A  1 59  ? 12.330  -28.444 129.017 1.00 33.02 ? 34   ASN A CB    1 
ATOM   268  C  CG    . ASN A  1 59  ? 11.453  -29.631 129.372 1.00 37.07 ? 34   ASN A CG    1 
ATOM   269  O  OD1   . ASN A  1 59  ? 11.570  -30.700 128.770 1.00 45.23 ? 34   ASN A OD1   1 
ATOM   270  N  ND2   . ASN A  1 59  ? 10.560  -29.449 130.333 1.00 35.32 ? 34   ASN A ND2   1 
ATOM   271  N  N     . SER A  1 60  ? 13.187  -30.570 126.363 1.00 34.41 ? 35   SER A N     1 
ATOM   272  C  CA    . SER A  1 60  ? 12.750  -31.108 125.073 1.00 34.79 ? 35   SER A CA    1 
ATOM   273  C  C     . SER A  1 60  ? 11.246  -31.340 125.030 1.00 28.90 ? 35   SER A C     1 
ATOM   274  O  O     . SER A  1 60  ? 10.647  -31.315 123.951 1.00 38.58 ? 35   SER A O     1 
ATOM   275  C  CB    . SER A  1 60  ? 13.478  -32.417 124.762 1.00 42.42 ? 35   SER A CB    1 
ATOM   276  O  OG    . SER A  1 60  ? 14.635  -32.117 124.014 1.00 55.75 ? 35   SER A OG    1 
ATOM   277  N  N     . ASN A  1 61  ? 10.631  -31.578 126.178 1.00 27.48 ? 36   ASN A N     1 
ATOM   278  C  CA    . ASN A  1 61  ? 9.177   -31.673 126.246 1.00 32.83 ? 36   ASN A CA    1 
ATOM   279  C  C     . ASN A  1 61  ? 8.506   -30.346 125.887 1.00 38.52 ? 36   ASN A C     1 
ATOM   280  O  O     . ASN A  1 61  ? 7.309   -30.327 125.590 1.00 35.07 ? 36   ASN A O     1 
ATOM   281  C  CB    . ASN A  1 61  ? 8.759   -32.092 127.653 1.00 40.38 ? 36   ASN A CB    1 
ATOM   282  C  CG    . ASN A  1 61  ? 9.235   -33.497 128.002 1.00 56.21 ? 36   ASN A CG    1 
ATOM   283  O  OD1   . ASN A  1 61  ? 9.235   -34.384 127.152 1.00 56.79 ? 36   ASN A OD1   1 
ATOM   284  N  ND2   . ASN A  1 61  ? 9.658   -33.696 129.251 1.00 51.10 ? 36   ASN A ND2   1 
ATOM   285  N  N     . LEU A  1 62  ? 9.252   -29.241 125.899 1.00 31.36 ? 37   LEU A N     1 
ATOM   286  C  CA    . LEU A  1 62  ? 8.716   -27.937 125.534 1.00 38.10 ? 37   LEU A CA    1 
ATOM   287  C  C     . LEU A  1 62  ? 9.071   -27.532 124.114 1.00 38.26 ? 37   LEU A C     1 
ATOM   288  O  O     . LEU A  1 62  ? 8.652   -26.461 123.668 1.00 34.13 ? 37   LEU A O     1 
ATOM   289  C  CB    . LEU A  1 62  ? 9.219   -26.856 126.510 1.00 28.82 ? 37   LEU A CB    1 
ATOM   290  C  CG    . LEU A  1 62  ? 8.611   -26.949 127.916 1.00 36.56 ? 37   LEU A CG    1 
ATOM   291  C  CD1   . LEU A  1 62  ? 9.312   -26.017 128.923 1.00 33.56 ? 37   LEU A CD1   1 
ATOM   292  C  CD2   . LEU A  1 62  ? 7.116   -26.658 127.836 1.00 28.96 ? 37   LEU A CD2   1 
ATOM   293  N  N     . GLN A  1 63  ? 9.815   -28.364 123.387 1.00 33.09 ? 38   GLN A N     1 
ATOM   294  C  CA    . GLN A  1 63  ? 10.260  -28.005 122.042 1.00 33.39 ? 38   GLN A CA    1 
ATOM   295  C  C     . GLN A  1 63  ? 9.265   -28.588 121.051 1.00 38.45 ? 38   GLN A C     1 
ATOM   296  O  O     . GLN A  1 63  ? 9.414   -29.710 120.572 1.00 39.45 ? 38   GLN A O     1 
ATOM   297  C  CB    . GLN A  1 63  ? 11.683  -28.482 121.801 1.00 35.77 ? 38   GLN A CB    1 
ATOM   298  C  CG    . GLN A  1 63  ? 12.677  -27.768 122.692 1.00 41.29 ? 38   GLN A CG    1 
ATOM   299  C  CD    . GLN A  1 63  ? 14.003  -28.479 122.724 1.00 43.89 ? 38   GLN A CD    1 
ATOM   300  O  OE1   . GLN A  1 63  ? 14.298  -29.298 121.849 1.00 46.15 ? 38   GLN A OE1   1 
ATOM   301  N  NE2   . GLN A  1 63  ? 14.814  -28.169 123.719 1.00 36.16 ? 38   GLN A NE2   1 
ATOM   302  N  N     . ASN A  1 64  ? 8.238   -27.803 120.739 1.00 40.73 ? 39   ASN A N     1 
ATOM   303  C  CA    . ASN A  1 64  ? 7.225   -28.140 119.750 1.00 35.69 ? 39   ASN A CA    1 
ATOM   304  C  C     . ASN A  1 64  ? 6.880   -26.861 119.001 1.00 39.65 ? 39   ASN A C     1 
ATOM   305  O  O     . ASN A  1 64  ? 7.318   -25.768 119.381 1.00 36.79 ? 39   ASN A O     1 
ATOM   306  C  CB    . ASN A  1 64  ? 5.979   -28.760 120.408 1.00 31.99 ? 39   ASN A CB    1 
ATOM   307  C  CG    . ASN A  1 64  ? 5.494   -27.941 121.599 1.00 43.58 ? 39   ASN A CG    1 
ATOM   308  O  OD1   . ASN A  1 64  ? 5.077   -26.801 121.432 1.00 40.19 ? 39   ASN A OD1   1 
ATOM   309  N  ND2   . ASN A  1 64  ? 5.530   -28.522 122.801 1.00 36.97 ? 39   ASN A ND2   1 
ATOM   310  N  N     . VAL A  1 65  ? 6.115   -26.999 117.908 1.00 32.76 ? 40   VAL A N     1 
ATOM   311  C  CA    . VAL A  1 65  ? 5.837   -25.846 117.051 1.00 33.77 ? 40   VAL A CA    1 
ATOM   312  C  C     . VAL A  1 65  ? 5.092   -24.761 117.815 1.00 34.03 ? 40   VAL A C     1 
ATOM   313  O  O     . VAL A  1 65  ? 5.381   -23.565 117.662 1.00 31.04 ? 40   VAL A O     1 
ATOM   314  C  CB    . VAL A  1 65  ? 5.055   -26.277 115.797 1.00 40.49 ? 40   VAL A CB    1 
ATOM   315  C  CG1   . VAL A  1 65  ? 4.455   -25.049 115.142 1.00 35.14 ? 40   VAL A CG1   1 
ATOM   316  C  CG2   . VAL A  1 65  ? 5.983   -26.949 114.827 1.00 33.70 ? 40   VAL A CG2   1 
ATOM   317  N  N     . THR A  1 66  ? 4.099   -25.155 118.620 1.00 28.38 ? 41   THR A N     1 
ATOM   318  C  CA    . THR A  1 66  ? 3.362   -24.166 119.388 1.00 33.85 ? 41   THR A CA    1 
ATOM   319  C  C     . THR A  1 66  ? 4.319   -23.289 120.177 1.00 34.05 ? 41   THR A C     1 
ATOM   320  O  O     . THR A  1 66  ? 4.208   -22.063 120.155 1.00 31.05 ? 41   THR A O     1 
ATOM   321  C  CB    . THR A  1 66  ? 2.345   -24.833 120.319 1.00 39.40 ? 41   THR A CB    1 
ATOM   322  O  OG1   . THR A  1 66  ? 1.854   -26.052 119.734 1.00 36.94 ? 41   THR A OG1   1 
ATOM   323  C  CG2   . THR A  1 66  ? 1.212   -23.892 120.608 1.00 29.19 ? 41   THR A CG2   1 
ATOM   324  N  N     . ASN A  1 67  ? 5.324   -23.896 120.800 1.00 28.47 ? 42   ASN A N     1 
ATOM   325  C  CA    . ASN A  1 67  ? 6.223   -23.134 121.641 1.00 26.13 ? 42   ASN A CA    1 
ATOM   326  C  C     . ASN A  1 67  ? 7.263   -22.354 120.849 1.00 26.44 ? 42   ASN A C     1 
ATOM   327  O  O     . ASN A  1 67  ? 7.895   -21.456 121.414 1.00 26.75 ? 42   ASN A O     1 
ATOM   328  C  CB    . ASN A  1 67  ? 6.884   -24.041 122.670 1.00 26.80 ? 42   ASN A CB    1 
ATOM   329  C  CG    . ASN A  1 67  ? 5.938   -24.401 123.790 1.00 34.31 ? 42   ASN A CG    1 
ATOM   330  O  OD1   . ASN A  1 67  ? 4.867   -23.793 123.935 1.00 30.10 ? 42   ASN A OD1   1 
ATOM   331  N  ND2   . ASN A  1 67  ? 6.335   -25.361 124.617 1.00 29.31 ? 42   ASN A ND2   1 
ATOM   332  N  N     . TYR A  1 68  ? 7.473   -22.652 119.564 1.00 20.75 ? 43   TYR A N     1 
ATOM   333  C  CA    . TYR A  1 68  ? 8.315   -21.731 118.808 1.00 25.25 ? 43   TYR A CA    1 
ATOM   334  C  C     . TYR A  1 68  ? 7.639   -20.368 118.675 1.00 23.04 ? 43   TYR A C     1 
ATOM   335  O  O     . TYR A  1 68  ? 8.312   -19.332 118.747 1.00 23.49 ? 43   TYR A O     1 
ATOM   336  C  CB    . TYR A  1 68  ? 8.667   -22.312 117.445 1.00 27.41 ? 43   TYR A CB    1 
ATOM   337  C  CG    . TYR A  1 68  ? 9.367   -23.644 117.608 1.00 40.61 ? 43   TYR A CG    1 
ATOM   338  C  CD1   . TYR A  1 68  ? 10.146  -23.897 118.745 1.00 39.15 ? 43   TYR A CD1   1 
ATOM   339  C  CD2   . TYR A  1 68  ? 9.259   -24.634 116.651 1.00 38.25 ? 43   TYR A CD2   1 
ATOM   340  C  CE1   . TYR A  1 68  ? 10.780  -25.089 118.925 1.00 45.17 ? 43   TYR A CE1   1 
ATOM   341  C  CE2   . TYR A  1 68  ? 9.901   -25.848 116.822 1.00 46.18 ? 43   TYR A CE2   1 
ATOM   342  C  CZ    . TYR A  1 68  ? 10.662  -26.067 117.961 1.00 48.46 ? 43   TYR A CZ    1 
ATOM   343  O  OH    . TYR A  1 68  ? 11.309  -27.268 118.148 1.00 60.87 ? 43   TYR A OH    1 
ATOM   344  N  N     . PHE A  1 69  ? 6.310   -20.349 118.520 1.00 19.17 ? 44   PHE A N     1 
ATOM   345  C  CA    . PHE A  1 69  ? 5.568   -19.081 118.532 1.00 25.59 ? 44   PHE A CA    1 
ATOM   346  C  C     . PHE A  1 69  ? 5.552   -18.446 119.918 1.00 21.79 ? 44   PHE A C     1 
ATOM   347  O  O     . PHE A  1 69  ? 5.605   -17.222 120.030 1.00 21.16 ? 44   PHE A O     1 
ATOM   348  C  CB    . PHE A  1 69  ? 4.136   -19.288 118.029 1.00 20.97 ? 44   PHE A CB    1 
ATOM   349  C  CG    . PHE A  1 69  ? 4.079   -19.688 116.576 1.00 26.53 ? 44   PHE A CG    1 
ATOM   350  C  CD1   . PHE A  1 69  ? 4.416   -18.784 115.582 1.00 29.03 ? 44   PHE A CD1   1 
ATOM   351  C  CD2   . PHE A  1 69  ? 3.730   -20.982 116.215 1.00 25.34 ? 44   PHE A CD2   1 
ATOM   352  C  CE1   . PHE A  1 69  ? 4.400   -19.162 114.235 1.00 30.23 ? 44   PHE A CE1   1 
ATOM   353  C  CE2   . PHE A  1 69  ? 3.707   -21.357 114.873 1.00 31.62 ? 44   PHE A CE2   1 
ATOM   354  C  CZ    . PHE A  1 69  ? 4.046   -20.446 113.890 1.00 23.41 ? 44   PHE A CZ    1 
ATOM   355  N  N     . VAL A  1 70  ? 5.487   -19.262 120.982 1.00 20.15 ? 45   VAL A N     1 
ATOM   356  C  CA    . VAL A  1 70  ? 5.617   -18.746 122.347 1.00 22.54 ? 45   VAL A CA    1 
ATOM   357  C  C     . VAL A  1 70  ? 6.950   -18.042 122.536 1.00 22.53 ? 45   VAL A C     1 
ATOM   358  O  O     . VAL A  1 70  ? 7.016   -16.963 123.146 1.00 23.01 ? 45   VAL A O     1 
ATOM   359  C  CB    . VAL A  1 70  ? 5.478   -19.891 123.369 1.00 26.15 ? 45   VAL A CB    1 
ATOM   360  C  CG1   . VAL A  1 70  ? 5.952   -19.444 124.771 1.00 21.42 ? 45   VAL A CG1   1 
ATOM   361  C  CG2   . VAL A  1 70  ? 4.048   -20.438 123.403 1.00 20.93 ? 45   VAL A CG2   1 
ATOM   362  N  N     . VAL A  1 71  ? 8.025   -18.609 121.966 1.00 19.07 ? 46   VAL A N     1 
ATOM   363  C  CA    . VAL A  1 71  ? 9.355   -18.004 122.056 1.00 20.29 ? 46   VAL A CA    1 
ATOM   364  C  C     . VAL A  1 71  ? 9.433   -16.721 121.243 1.00 19.90 ? 46   VAL A C     1 
ATOM   365  O  O     . VAL A  1 71  ? 10.032  -15.731 121.684 1.00 19.34 ? 46   VAL A O     1 
ATOM   366  C  CB    . VAL A  1 71  ? 10.422  -19.021 121.610 1.00 28.09 ? 46   VAL A CB    1 
ATOM   367  C  CG1   . VAL A  1 71  ? 11.757  -18.319 121.376 1.00 25.65 ? 46   VAL A CG1   1 
ATOM   368  C  CG2   . VAL A  1 71  ? 10.559  -20.167 122.671 1.00 24.47 ? 46   VAL A CG2   1 
ATOM   369  N  N     . SER A  1 72  ? 8.852   -16.717 120.040 1.00 18.99 ? 47   SER A N     1 
ATOM   370  C  CA    . SER A  1 72  ? 8.783   -15.484 119.246 1.00 21.28 ? 47   SER A CA    1 
ATOM   371  C  C     . SER A  1 72  ? 8.088   -14.373 120.030 1.00 21.88 ? 47   SER A C     1 
ATOM   372  O  O     . SER A  1 72  ? 8.538   -13.217 120.025 1.00 18.25 ? 47   SER A O     1 
ATOM   373  C  CB    . SER A  1 72  ? 8.040   -15.733 117.930 1.00 19.72 ? 47   SER A CB    1 
ATOM   374  O  OG    . SER A  1 72  ? 8.138   -14.595 117.074 1.00 24.50 ? 47   SER A OG    1 
ATOM   375  N  N     . LEU A  1 73  ? 7.001   -14.726 120.726 1.00 19.44 ? 48   LEU A N     1 
ATOM   376  C  CA    . LEU A  1 73  ? 6.257   -13.777 121.554 1.00 23.23 ? 48   LEU A CA    1 
ATOM   377  C  C     . LEU A  1 73  ? 7.078   -13.312 122.741 1.00 20.03 ? 48   LEU A C     1 
ATOM   378  O  O     . LEU A  1 73  ? 7.109   -12.116 123.051 1.00 18.01 ? 48   LEU A O     1 
ATOM   379  C  CB    . LEU A  1 73  ? 4.956   -14.442 122.024 1.00 25.81 ? 48   LEU A CB    1 
ATOM   380  C  CG    . LEU A  1 73  ? 3.876   -13.694 122.778 1.00 28.21 ? 48   LEU A CG    1 
ATOM   381  C  CD1   . LEU A  1 73  ? 3.415   -12.488 121.950 1.00 22.42 ? 48   LEU A CD1   1 
ATOM   382  C  CD2   . LEU A  1 73  ? 2.683   -14.649 123.060 1.00 25.90 ? 48   LEU A CD2   1 
ATOM   383  N  N     . ALA A  1 74  ? 7.818   -14.224 123.372 1.00 22.08 ? 49   ALA A N     1 
ATOM   384  C  CA    . ALA A  1 74  ? 8.699   -13.814 124.469 1.00 21.46 ? 49   ALA A CA    1 
ATOM   385  C  C     . ALA A  1 74  ? 9.837   -12.918 123.985 1.00 20.19 ? 49   ALA A C     1 
ATOM   386  O  O     . ALA A  1 74  ? 10.263  -12.001 124.698 1.00 19.90 ? 49   ALA A O     1 
ATOM   387  C  CB    . ALA A  1 74  ? 9.247   -15.066 125.184 1.00 20.41 ? 49   ALA A CB    1 
ATOM   388  N  N     . ALA A  1 75  ? 10.352  -13.165 122.779 1.00 19.80 ? 50   ALA A N     1 
ATOM   389  C  CA    . ALA A  1 75  ? 11.381  -12.289 122.226 1.00 22.48 ? 50   ALA A CA    1 
ATOM   390  C  C     . ALA A  1 75  ? 10.847  -10.882 122.000 1.00 19.80 ? 50   ALA A C     1 
ATOM   391  O  O     . ALA A  1 75  ? 11.538  -9.889  122.281 1.00 21.13 ? 50   ALA A O     1 
ATOM   392  C  CB    . ALA A  1 75  ? 11.938  -12.858 120.915 1.00 21.27 ? 50   ALA A CB    1 
ATOM   393  N  N     . ALA A  1 76  ? 9.619   -10.773 121.480 1.00 19.41 ? 51   ALA A N     1 
ATOM   394  C  CA    . ALA A  1 76  ? 9.017   -9.455  121.324 1.00 22.49 ? 51   ALA A CA    1 
ATOM   395  C  C     . ALA A  1 76  ? 8.914   -8.752  122.671 1.00 21.39 ? 51   ALA A C     1 
ATOM   396  O  O     . ALA A  1 76  ? 9.123   -7.538  122.758 1.00 19.48 ? 51   ALA A O     1 
ATOM   397  C  CB    . ALA A  1 76  ? 7.628   -9.583  120.678 1.00 18.34 ? 51   ALA A CB    1 
ATOM   398  N  N     . ASP A  1 77  ? 8.552   -9.499  123.727 1.00 18.08 ? 52   ASP A N     1 
ATOM   399  C  CA    . ASP A  1 77  ? 8.398   -8.890  125.051 1.00 19.73 ? 52   ASP A CA    1 
ATOM   400  C  C     . ASP A  1 77  ? 9.756   -8.543  125.673 1.00 21.24 ? 52   ASP A C     1 
ATOM   401  O  O     . ASP A  1 77  ? 9.868   -7.513  126.357 1.00 21.15 ? 52   ASP A O     1 
ATOM   402  C  CB    . ASP A  1 77  ? 7.536   -9.804  125.949 1.00 22.06 ? 52   ASP A CB    1 
ATOM   403  C  CG    . ASP A  1 77  ? 6.039   -9.794  125.534 1.00 29.22 ? 52   ASP A CG    1 
ATOM   404  O  OD1   . ASP A  1 77  ? 5.591   -8.739  125.003 1.00 30.41 ? 52   ASP A OD1   1 
ATOM   405  O  OD2   . ASP A  1 77  ? 5.292   -10.807 125.726 1.00 29.05 ? 52   ASP A OD2   1 
ATOM   406  N  N     . ILE A  1 78  ? 10.805  -9.346  125.412 1.00 23.72 ? 53   ILE A N     1 
ATOM   407  C  CA    . ILE A  1 78  ? 12.158  -8.964  125.828 1.00 19.12 ? 53   ILE A CA    1 
ATOM   408  C  C     . ILE A  1 78  ? 12.553  -7.639  125.180 1.00 17.63 ? 53   ILE A C     1 
ATOM   409  O  O     . ILE A  1 78  ? 13.129  -6.758  125.834 1.00 19.95 ? 53   ILE A O     1 
ATOM   410  C  CB    . ILE A  1 78  ? 13.177  -10.071 125.489 1.00 18.31 ? 53   ILE A CB    1 
ATOM   411  C  CG1   . ILE A  1 78  ? 12.955  -11.294 126.366 1.00 20.53 ? 53   ILE A CG1   1 
ATOM   412  C  CG2   . ILE A  1 78  ? 14.593  -9.551  125.691 1.00 21.95 ? 53   ILE A CG2   1 
ATOM   413  C  CD1   . ILE A  1 78  ? 13.672  -12.573 125.875 1.00 25.90 ? 53   ILE A CD1   1 
ATOM   414  N  N     . LEU A  1 79  ? 12.231  -7.463  123.891 1.00 17.29 ? 54   LEU A N     1 
ATOM   415  C  CA    . LEU A  1 79  ? 12.565  -6.216  123.209 1.00 18.21 ? 54   LEU A CA    1 
ATOM   416  C  C     . LEU A  1 79  ? 11.688  -5.042  123.655 1.00 16.21 ? 54   LEU A C     1 
ATOM   417  O  O     . LEU A  1 79  ? 12.099  -3.891  123.485 1.00 18.54 ? 54   LEU A O     1 
ATOM   418  C  CB    . LEU A  1 79  ? 12.459  -6.389  121.683 1.00 21.86 ? 54   LEU A CB    1 
ATOM   419  C  CG    . LEU A  1 79  ? 13.484  -7.416  121.171 1.00 21.31 ? 54   LEU A CG    1 
ATOM   420  C  CD1   . LEU A  1 79  ? 13.255  -7.761  119.708 1.00 28.04 ? 54   LEU A CD1   1 
ATOM   421  C  CD2   . LEU A  1 79  ? 14.890  -6.847  121.405 1.00 26.14 ? 54   LEU A CD2   1 
ATOM   422  N  N     . VAL A  1 80  ? 10.486  -5.288  124.192 1.00 15.89 ? 55   VAL A N     1 
ATOM   423  C  CA    . VAL A  1 80  ? 9.747   -4.201  124.847 1.00 16.90 ? 55   VAL A CA    1 
ATOM   424  C  C     . VAL A  1 80  ? 10.551  -3.676  126.024 1.00 19.00 ? 55   VAL A C     1 
ATOM   425  O  O     . VAL A  1 80  ? 10.693  -2.468  126.217 1.00 19.37 ? 55   VAL A O     1 
ATOM   426  C  CB    . VAL A  1 80  ? 8.331   -4.660  125.280 1.00 20.64 ? 55   VAL A CB    1 
ATOM   427  C  CG1   . VAL A  1 80  ? 7.666   -3.649  126.251 1.00 16.67 ? 55   VAL A CG1   1 
ATOM   428  C  CG2   . VAL A  1 80  ? 7.414   -4.809  124.049 1.00 19.96 ? 55   VAL A CG2   1 
ATOM   429  N  N     . GLY A  1 81  ? 11.148  -4.577  126.792 1.00 16.91 ? 56   GLY A N     1 
ATOM   430  C  CA    . GLY A  1 81  ? 11.927  -4.135  127.934 1.00 18.06 ? 56   GLY A CA    1 
ATOM   431  C  C     . GLY A  1 81  ? 13.233  -3.463  127.546 1.00 19.62 ? 56   GLY A C     1 
ATOM   432  O  O     . GLY A  1 81  ? 13.625  -2.464  128.145 1.00 22.02 ? 56   GLY A O     1 
ATOM   433  N  N     . VAL A  1 82  ? 13.940  -4.023  126.570 1.00 18.51 ? 57   VAL A N     1 
ATOM   434  C  CA    . VAL A  1 82  ? 15.263  -3.531  126.205 1.00 18.37 ? 57   VAL A CA    1 
ATOM   435  C  C     . VAL A  1 82  ? 15.184  -2.270  125.342 1.00 20.80 ? 57   VAL A C     1 
ATOM   436  O  O     . VAL A  1 82  ? 16.042  -1.382  125.455 1.00 22.11 ? 57   VAL A O     1 
ATOM   437  C  CB    . VAL A  1 82  ? 16.030  -4.676  125.513 1.00 23.34 ? 57   VAL A CB    1 
ATOM   438  C  CG1   . VAL A  1 82  ? 17.295  -4.191  124.859 1.00 27.56 ? 57   VAL A CG1   1 
ATOM   439  C  CG2   . VAL A  1 82  ? 16.276  -5.806  126.526 1.00 22.13 ? 57   VAL A CG2   1 
ATOM   440  N  N     . LEU A  1 83  ? 14.195  -2.182  124.441 1.00 20.28 ? 58   LEU A N     1 
ATOM   441  C  CA    . LEU A  1 83  ? 14.131  -1.087  123.471 1.00 20.94 ? 58   LEU A CA    1 
ATOM   442  C  C     . LEU A  1 83  ? 12.863  -0.241  123.547 1.00 16.70 ? 58   LEU A C     1 
ATOM   443  O  O     . LEU A  1 83  ? 12.969  0.998   123.609 1.00 19.23 ? 58   LEU A O     1 
ATOM   444  C  CB    . LEU A  1 83  ? 14.291  -1.657  122.046 1.00 22.18 ? 58   LEU A CB    1 
ATOM   445  C  CG    . LEU A  1 83  ? 15.669  -2.211  121.655 1.00 26.29 ? 58   LEU A CG    1 
ATOM   446  C  CD1   . LEU A  1 83  ? 15.634  -2.796  120.236 1.00 26.18 ? 58   LEU A CD1   1 
ATOM   447  C  CD2   . LEU A  1 83  ? 16.767  -1.139  121.786 1.00 24.37 ? 58   LEU A CD2   1 
ATOM   448  N  N     . ALA A  1 84  ? 11.658  -0.848  123.537 1.00 15.45 ? 59   ALA A N     1 
ATOM   449  C  CA    . ALA A  1 84  ? 10.447  -0.021  123.441 1.00 17.48 ? 59   ALA A CA    1 
ATOM   450  C  C     . ALA A  1 84  ? 10.274  0.825   124.696 1.00 17.29 ? 59   ALA A C     1 
ATOM   451  O  O     . ALA A  1 84  ? 9.786   1.956   124.629 1.00 17.68 ? 59   ALA A O     1 
ATOM   452  C  CB    . ALA A  1 84  ? 9.186   -0.865  123.214 1.00 16.61 ? 59   ALA A CB    1 
ATOM   453  N  N     . ILE A  1 85  ? 10.614  0.289   125.858 1.00 17.84 ? 60   ILE A N     1 
ATOM   454  C  CA    . ILE A  1 85  ? 10.404  1.097   127.064 1.00 14.15 ? 60   ILE A CA    1 
ATOM   455  C  C     . ILE A  1 85  ? 11.459  2.208   127.149 1.00 17.31 ? 60   ILE A C     1 
ATOM   456  O  O     . ILE A  1 85  ? 11.103  3.358   127.424 1.00 18.93 ? 60   ILE A O     1 
ATOM   457  C  CB    . ILE A  1 85  ? 10.339  0.208   128.315 1.00 19.60 ? 60   ILE A CB    1 
ATOM   458  C  CG1   . ILE A  1 85  ? 8.976   -0.484  128.351 1.00 17.35 ? 60   ILE A CG1   1 
ATOM   459  C  CG2   . ILE A  1 85  ? 10.484  1.050   129.571 1.00 19.75 ? 60   ILE A CG2   1 
ATOM   460  C  CD1   . ILE A  1 85  ? 8.823   -1.559  129.493 1.00 18.63 ? 60   ILE A CD1   1 
ATOM   461  N  N     . PRO A  1 86  ? 12.752  1.960   126.933 1.00 18.20 ? 61   PRO A N     1 
ATOM   462  C  CA    . PRO A  1 86  ? 13.672  3.114   126.813 1.00 19.95 ? 61   PRO A CA    1 
ATOM   463  C  C     . PRO A  1 86  ? 13.219  4.105   125.746 1.00 21.80 ? 61   PRO A C     1 
ATOM   464  O  O     . PRO A  1 86  ? 13.369  5.321   125.924 1.00 18.95 ? 61   PRO A O     1 
ATOM   465  C  CB    . PRO A  1 86  ? 15.018  2.458   126.471 1.00 18.75 ? 61   PRO A CB    1 
ATOM   466  C  CG    . PRO A  1 86  ? 14.941  1.128   127.190 1.00 19.71 ? 61   PRO A CG    1 
ATOM   467  C  CD    . PRO A  1 86  ? 13.495  0.679   126.988 1.00 21.83 ? 61   PRO A CD    1 
ATOM   468  N  N     . PHE A  1 87  ? 12.683  3.619   124.622 1.00 16.65 ? 62   PHE A N     1 
ATOM   469  C  CA    . PHE A  1 87  ? 12.188  4.550   123.608 1.00 18.25 ? 62   PHE A CA    1 
ATOM   470  C  C     . PHE A  1 87  ? 10.997  5.345   124.127 1.00 18.16 ? 62   PHE A C     1 
ATOM   471  O  O     . PHE A  1 87  ? 10.875  6.544   123.842 1.00 18.97 ? 62   PHE A O     1 
ATOM   472  C  CB    . PHE A  1 87  ? 11.787  3.804   122.315 1.00 17.66 ? 62   PHE A CB    1 
ATOM   473  C  CG    . PHE A  1 87  ? 12.957  3.251   121.498 1.00 18.90 ? 62   PHE A CG    1 
ATOM   474  C  CD1   . PHE A  1 87  ? 14.291  3.429   121.894 1.00 25.21 ? 62   PHE A CD1   1 
ATOM   475  C  CD2   . PHE A  1 87  ? 12.708  2.549   120.315 1.00 15.62 ? 62   PHE A CD2   1 
ATOM   476  C  CE1   . PHE A  1 87  ? 15.358  2.888   121.133 1.00 20.84 ? 62   PHE A CE1   1 
ATOM   477  C  CE2   . PHE A  1 87  ? 13.752  2.014   119.542 1.00 19.76 ? 62   PHE A CE2   1 
ATOM   478  C  CZ    . PHE A  1 87  ? 15.090  2.197   119.954 1.00 18.80 ? 62   PHE A CZ    1 
ATOM   479  N  N     . ALA A  1 88  ? 10.084  4.694   124.863 1.00 19.74 ? 63   ALA A N     1 
ATOM   480  C  CA    . ALA A  1 88  ? 8.923   5.411   125.400 1.00 16.87 ? 63   ALA A CA    1 
ATOM   481  C  C     . ALA A  1 88  ? 9.344   6.468   126.423 1.00 16.93 ? 63   ALA A C     1 
ATOM   482  O  O     . ALA A  1 88  ? 8.828   7.588   126.422 1.00 16.59 ? 63   ALA A O     1 
ATOM   483  C  CB    . ALA A  1 88  ? 7.919   4.424   126.023 1.00 17.07 ? 63   ALA A CB    1 
ATOM   484  N  N     . ILE A  1 89  ? 10.292  6.137   127.289 1.00 19.52 ? 64   ILE A N     1 
ATOM   485  C  CA    . ILE A  1 89  ? 10.832  7.132   128.221 1.00 18.62 ? 64   ILE A CA    1 
ATOM   486  C  C     . ILE A  1 89  ? 11.404  8.319   127.445 1.00 20.88 ? 64   ILE A C     1 
ATOM   487  O  O     . ILE A  1 89  ? 11.126  9.487   127.752 1.00 23.34 ? 64   ILE A O     1 
ATOM   488  C  CB    . ILE A  1 89  ? 11.900  6.470   129.116 1.00 20.96 ? 64   ILE A CB    1 
ATOM   489  C  CG1   . ILE A  1 89  ? 11.253  5.450   130.060 1.00 14.00 ? 64   ILE A CG1   1 
ATOM   490  C  CG2   . ILE A  1 89  ? 12.775  7.526   129.844 1.00 21.05 ? 64   ILE A CG2   1 
ATOM   491  C  CD1   . ILE A  1 89  ? 12.262  4.523   130.767 1.00 16.91 ? 64   ILE A CD1   1 
ATOM   492  N  N     . THR A  1 90  ? 12.188  8.039   126.406 1.00 16.67 ? 65   THR A N     1 
ATOM   493  C  CA    . THR A  1 90  ? 12.797  9.116   125.627 1.00 18.00 ? 65   THR A CA    1 
ATOM   494  C  C     . THR A  1 90  ? 11.744  10.035  125.008 1.00 23.33 ? 65   THR A C     1 
ATOM   495  O  O     . THR A  1 90  ? 11.859  11.263  125.089 1.00 20.35 ? 65   THR A O     1 
ATOM   496  C  CB    . THR A  1 90  ? 13.696  8.520   124.540 1.00 20.77 ? 65   THR A CB    1 
ATOM   497  O  OG1   . THR A  1 90  ? 14.677  7.683   125.150 1.00 25.69 ? 65   THR A OG1   1 
ATOM   498  C  CG2   . THR A  1 90  ? 14.405  9.590   123.754 1.00 25.10 ? 65   THR A CG2   1 
ATOM   499  N  N     . ILE A  1 91  ? 10.696  9.459   124.405 1.00 20.88 ? 66   ILE A N     1 
ATOM   500  C  CA    . ILE A  1 91  ? 9.719   10.263  123.675 1.00 17.94 ? 66   ILE A CA    1 
ATOM   501  C  C     . ILE A  1 91  ? 8.767   11.003  124.610 1.00 23.34 ? 66   ILE A C     1 
ATOM   502  O  O     . ILE A  1 91  ? 8.089   11.953  124.191 1.00 28.12 ? 66   ILE A O     1 
ATOM   503  C  CB    . ILE A  1 91  ? 8.925   9.390   122.669 1.00 20.58 ? 66   ILE A CB    1 
ATOM   504  C  CG1   . ILE A  1 91  ? 8.308   10.279  121.559 1.00 26.28 ? 66   ILE A CG1   1 
ATOM   505  C  CG2   . ILE A  1 91  ? 7.834   8.579   123.383 1.00 22.04 ? 66   ILE A CG2   1 
ATOM   506  C  CD1   . ILE A  1 91  ? 8.283   9.670   120.115 1.00 23.74 ? 66   ILE A CD1   1 
ATOM   507  N  N     . SER A  1 92  ? 8.691   10.607  125.879 1.00 21.05 ? 67   SER A N     1 
ATOM   508  C  CA    . SER A  1 92  ? 7.922   11.397  126.832 1.00 21.09 ? 67   SER A CA    1 
ATOM   509  C  C     . SER A  1 92  ? 8.600   12.728  127.164 1.00 26.31 ? 67   SER A C     1 
ATOM   510  O  O     . SER A  1 92  ? 7.938   13.621  127.693 1.00 26.71 ? 67   SER A O     1 
ATOM   511  C  CB    . SER A  1 92  ? 7.688   10.606  128.136 1.00 19.16 ? 67   SER A CB    1 
ATOM   512  O  OG    . SER A  1 92  ? 8.875   10.577  128.933 1.00 24.93 ? 67   SER A OG    1 
ATOM   513  N  N     . THR A  1 93  ? 9.898   12.882  126.886 1.00 22.66 ? 68   THR A N     1 
ATOM   514  C  CA    . THR A  1 93  ? 10.568  14.127  127.246 1.00 24.77 ? 68   THR A CA    1 
ATOM   515  C  C     . THR A  1 93  ? 10.382  15.225  126.210 1.00 32.47 ? 68   THR A C     1 
ATOM   516  O  O     . THR A  1 93  ? 10.621  16.390  126.522 1.00 31.86 ? 68   THR A O     1 
ATOM   517  C  CB    . THR A  1 93  ? 12.076  13.900  127.441 1.00 25.49 ? 68   THR A CB    1 
ATOM   518  O  OG1   . THR A  1 93  ? 12.710  13.679  126.164 1.00 22.28 ? 68   THR A OG1   1 
ATOM   519  C  CG2   . THR A  1 93  ? 12.338  12.693  128.340 1.00 24.54 ? 68   THR A CG2   1 
ATOM   520  N  N     . GLY A  1 94  ? 9.930   14.904  125.003 1.00 27.07 ? 69   GLY A N     1 
ATOM   521  C  CA    . GLY A  1 94  ? 9.827   15.928  123.983 1.00 26.25 ? 69   GLY A CA    1 
ATOM   522  C  C     . GLY A  1 94  ? 11.146  16.489  123.488 1.00 32.27 ? 69   GLY A C     1 
ATOM   523  O  O     . GLY A  1 94  ? 11.165  17.597  122.941 1.00 28.08 ? 69   GLY A O     1 
ATOM   524  N  N     . PHE A  1 95  ? 12.242  15.738  123.619 1.00 25.41 ? 70   PHE A N     1 
ATOM   525  C  CA    . PHE A  1 95  ? 13.573  16.234  123.267 1.00 30.63 ? 70   PHE A CA    1 
ATOM   526  C  C     . PHE A  1 95  ? 13.672  16.567  121.772 1.00 30.98 ? 70   PHE A C     1 
ATOM   527  O  O     . PHE A  1 95  ? 12.962  16.004  120.932 1.00 24.94 ? 70   PHE A O     1 
ATOM   528  C  CB    . PHE A  1 95  ? 14.635  15.192  123.642 1.00 28.59 ? 70   PHE A CB    1 
ATOM   529  C  CG    . PHE A  1 95  ? 14.708  14.044  122.683 1.00 28.14 ? 70   PHE A CG    1 
ATOM   530  C  CD1   . PHE A  1 95  ? 13.653  13.139  122.582 1.00 27.16 ? 70   PHE A CD1   1 
ATOM   531  C  CD2   . PHE A  1 95  ? 15.799  13.884  121.845 1.00 30.50 ? 70   PHE A CD2   1 
ATOM   532  C  CE1   . PHE A  1 95  ? 13.698  12.085  121.670 1.00 27.31 ? 70   PHE A CE1   1 
ATOM   533  C  CE2   . PHE A  1 95  ? 15.850  12.837  120.937 1.00 28.25 ? 70   PHE A CE2   1 
ATOM   534  C  CZ    . PHE A  1 95  ? 14.806  11.934  120.847 1.00 26.28 ? 70   PHE A CZ    1 
ATOM   535  N  N     . CYS A  1 96  ? 14.595  17.475  121.441 1.00 28.57 ? 71   CYS A N     1 
ATOM   536  C  CA    . CYS A  1 96  ? 14.791  17.895  120.057 1.00 28.85 ? 71   CYS A CA    1 
ATOM   537  C  C     . CYS A  1 96  ? 15.409  16.756  119.240 1.00 27.73 ? 71   CYS A C     1 
ATOM   538  O  O     . CYS A  1 96  ? 16.403  16.158  119.653 1.00 28.13 ? 71   CYS A O     1 
ATOM   539  C  CB    . CYS A  1 96  ? 15.708  19.135  120.019 1.00 27.83 ? 71   CYS A CB    1 
ATOM   540  S  SG    . CYS A  1 96  ? 14.965  20.619  120.750 1.00 35.07 ? 71   CYS A SG    1 
ATOM   541  N  N     . ALA A  1 97  ? 14.827  16.454  118.079 1.00 21.55 ? 72   ALA A N     1 
ATOM   542  C  CA    . ALA A  1 97  ? 15.283  15.342  117.260 1.00 20.47 ? 72   ALA A CA    1 
ATOM   543  C  C     . ALA A  1 97  ? 14.910  15.592  115.812 1.00 24.66 ? 72   ALA A C     1 
ATOM   544  O  O     . ALA A  1 97  ? 13.923  16.270  115.529 1.00 27.04 ? 72   ALA A O     1 
ATOM   545  C  CB    . ALA A  1 97  ? 14.679  14.012  117.722 1.00 24.84 ? 72   ALA A CB    1 
ATOM   546  N  N     . ALA A  1 98  ? 15.734  15.087  114.894 1.00 24.26 ? 73   ALA A N     1 
ATOM   547  C  CA    . ALA A  1 98  ? 15.312  14.963  113.501 1.00 28.96 ? 73   ALA A CA    1 
ATOM   548  C  C     . ALA A  1 98  ? 14.008  14.170  113.400 1.00 30.10 ? 73   ALA A C     1 
ATOM   549  O  O     . ALA A  1 98  ? 13.840  13.148  114.070 1.00 23.73 ? 73   ALA A O     1 
ATOM   550  C  CB    . ALA A  1 98  ? 16.407  14.291  112.677 1.00 27.67 ? 73   ALA A CB    1 
ATOM   551  N  N     . CYS A  1 99  ? 13.059  14.660  112.591 1.00 29.25 ? 74   CYS A N     1 
ATOM   552  C  CA    . CYS A  1 99  ? 11.702  14.113  112.669 1.00 27.86 ? 74   CYS A CA    1 
ATOM   553  C  C     . CYS A  1 99  ? 11.656  12.617  112.349 1.00 26.52 ? 74   CYS A C     1 
ATOM   554  O  O     . CYS A  1 99  ? 10.917  11.865  112.997 1.00 24.24 ? 74   CYS A O     1 
ATOM   555  C  CB    . CYS A  1 99  ? 10.768  14.877  111.738 1.00 33.19 ? 74   CYS A CB    1 
ATOM   556  S  SG    . CYS A  1 99  ? 9.038   14.408  112.002 1.00 38.81 ? 74   CYS A SG    1 
ATOM   557  N  N     . HIS A  1 100 ? 12.446  12.151  111.376 1.00 23.07 ? 75   HIS A N     1 
ATOM   558  C  CA    . HIS A  1 100 ? 12.393  10.726  111.031 1.00 27.89 ? 75   HIS A CA    1 
ATOM   559  C  C     . HIS A  1 100 ? 13.082  9.816   112.054 1.00 25.89 ? 75   HIS A C     1 
ATOM   560  O  O     . HIS A  1 100 ? 12.704  8.639   112.187 1.00 21.82 ? 75   HIS A O     1 
ATOM   561  C  CB    . HIS A  1 100 ? 12.976  10.535  109.632 1.00 30.45 ? 75   HIS A CB    1 
ATOM   562  C  CG    . HIS A  1 100 ? 12.091  11.107  108.579 1.00 36.52 ? 75   HIS A CG    1 
ATOM   563  N  ND1   . HIS A  1 100 ? 12.142  12.435  108.209 1.00 37.73 ? 75   HIS A ND1   1 
ATOM   564  C  CD2   . HIS A  1 100 ? 11.100  10.545  107.850 1.00 34.70 ? 75   HIS A CD2   1 
ATOM   565  C  CE1   . HIS A  1 100 ? 11.217  12.668  107.294 1.00 34.32 ? 75   HIS A CE1   1 
ATOM   566  N  NE2   . HIS A  1 100 ? 10.572  11.538  107.058 1.00 42.38 ? 75   HIS A NE2   1 
ATOM   567  N  N     . GLY A  1 101 ? 14.106  10.302  112.751 1.00 28.77 ? 76   GLY A N     1 
ATOM   568  C  CA    . GLY A  1 101 ? 14.621  9.552   113.892 1.00 28.03 ? 76   GLY A CA    1 
ATOM   569  C  C     . GLY A  1 101 ? 13.604  9.469   115.012 1.00 22.50 ? 76   GLY A C     1 
ATOM   570  O  O     . GLY A  1 101 ? 13.444  8.423   115.650 1.00 22.21 ? 76   GLY A O     1 
ATOM   571  N  N     . CYS A  1 102 ? 12.923  10.580  115.281 1.00 22.63 ? 77   CYS A N     1 
ATOM   572  C  CA    . CYS A  1 102 ? 11.834  10.581  116.247 1.00 25.71 ? 77   CYS A CA    1 
ATOM   573  C  C     . CYS A  1 102 ? 10.754  9.571   115.844 1.00 26.88 ? 77   CYS A C     1 
ATOM   574  O  O     . CYS A  1 102 ? 10.233  8.822   116.685 1.00 20.65 ? 77   CYS A O     1 
ATOM   575  C  CB    . CYS A  1 102 ? 11.261  11.999  116.359 1.00 25.24 ? 77   CYS A CB    1 
ATOM   576  S  SG    . CYS A  1 102 ? 9.868   12.090  117.518 1.00 30.60 ? 77   CYS A SG    1 
ATOM   577  N  N     A LEU A  1 103 ? 10.433  9.522   114.549 0.41 23.19 ? 78   LEU A N     1 
ATOM   578  N  N     B LEU A  1 103 ? 10.389  9.552   114.560 0.59 23.19 ? 78   LEU A N     1 
ATOM   579  C  CA    A LEU A  1 103 ? 9.449   8.570   114.048 0.41 23.62 ? 78   LEU A CA    1 
ATOM   580  C  CA    B LEU A  1 103 ? 9.444   8.561   114.055 0.59 23.65 ? 78   LEU A CA    1 
ATOM   581  C  C     A LEU A  1 103 ? 9.855   7.137   114.365 0.41 20.51 ? 78   LEU A C     1 
ATOM   582  C  C     B LEU A  1 103 ? 9.864   7.139   114.394 0.59 20.45 ? 78   LEU A C     1 
ATOM   583  O  O     A LEU A  1 103 ? 9.013   6.317   114.759 0.41 23.49 ? 78   LEU A O     1 
ATOM   584  O  O     B LEU A  1 103 ? 9.029   6.317   114.803 0.59 23.55 ? 78   LEU A O     1 
ATOM   585  C  CB    A LEU A  1 103 ? 9.292   8.742   112.536 0.41 22.77 ? 78   LEU A CB    1 
ATOM   586  C  CB    B LEU A  1 103 ? 9.309   8.706   112.541 0.59 22.78 ? 78   LEU A CB    1 
ATOM   587  C  CG    A LEU A  1 103 ? 8.163   9.587   111.959 0.41 20.91 ? 78   LEU A CG    1 
ATOM   588  C  CG    B LEU A  1 103 ? 8.023   8.271   111.873 0.59 20.77 ? 78   LEU A CG    1 
ATOM   589  C  CD1   A LEU A  1 103 ? 8.256   9.478   110.455 0.41 20.97 ? 78   LEU A CD1   1 
ATOM   590  C  CD1   B LEU A  1 103 ? 6.750   8.768   112.584 0.59 20.58 ? 78   LEU A CD1   1 
ATOM   591  C  CD2   A LEU A  1 103 ? 6.786   9.162   112.463 0.41 20.16 ? 78   LEU A CD2   1 
ATOM   592  C  CD2   B LEU A  1 103 ? 8.113   8.823   110.460 0.59 20.09 ? 78   LEU A CD2   1 
ATOM   593  N  N     . PHE A  1 104 ? 11.136  6.801   114.172 1.00 21.98 ? 79   PHE A N     1 
ATOM   594  C  CA    . PHE A  1 104 ? 11.574  5.436   114.442 1.00 20.93 ? 79   PHE A CA    1 
ATOM   595  C  C     . PHE A  1 104 ? 11.393  5.096   115.917 1.00 19.21 ? 79   PHE A C     1 
ATOM   596  O  O     . PHE A  1 104 ? 10.851  4.044   116.258 1.00 19.22 ? 79   PHE A O     1 
ATOM   597  C  CB    . PHE A  1 104 ? 13.025  5.190   114.012 1.00 22.03 ? 79   PHE A CB    1 
ATOM   598  C  CG    . PHE A  1 104 ? 13.490  3.778   114.300 1.00 22.11 ? 79   PHE A CG    1 
ATOM   599  C  CD1   . PHE A  1 104 ? 13.129  2.721   113.466 1.00 27.97 ? 79   PHE A CD1   1 
ATOM   600  C  CD2   . PHE A  1 104 ? 14.209  3.487   115.447 1.00 17.17 ? 79   PHE A CD2   1 
ATOM   601  C  CE1   . PHE A  1 104 ? 13.534  1.410   113.738 1.00 26.29 ? 79   PHE A CE1   1 
ATOM   602  C  CE2   . PHE A  1 104 ? 14.604  2.174   115.733 1.00 25.62 ? 79   PHE A CE2   1 
ATOM   603  C  CZ    . PHE A  1 104 ? 14.267  1.133   114.879 1.00 25.85 ? 79   PHE A CZ    1 
ATOM   604  N  N     . ILE A  1 105 ? 11.815  5.981   116.818 1.00 18.44 ? 80   ILE A N     1 
ATOM   605  C  CA    . ILE A  1 105 ? 11.633  5.600   118.216 1.00 21.01 ? 80   ILE A CA    1 
ATOM   606  C  C     . ILE A  1 105 ? 10.159  5.609   118.600 1.00 21.54 ? 80   ILE A C     1 
ATOM   607  O  O     . ILE A  1 105 ? 9.760   4.878   119.507 1.00 17.92 ? 80   ILE A O     1 
ATOM   608  C  CB    . ILE A  1 105 ? 12.499  6.449   119.175 1.00 26.43 ? 80   ILE A CB    1 
ATOM   609  C  CG1   . ILE A  1 105 ? 11.908  7.808   119.408 1.00 23.96 ? 80   ILE A CG1   1 
ATOM   610  C  CG2   . ILE A  1 105 ? 13.978  6.489   118.762 1.00 29.76 ? 80   ILE A CG2   1 
ATOM   611  C  CD1   . ILE A  1 105 ? 12.684  8.619   120.437 1.00 31.74 ? 80   ILE A CD1   1 
ATOM   612  N  N     . ALA A  1 106 ? 9.317   6.386   117.913 1.00 15.92 ? 81   ALA A N     1 
ATOM   613  C  CA    . ALA A  1 106 ? 7.887   6.306   118.189 1.00 20.79 ? 81   ALA A CA    1 
ATOM   614  C  C     . ALA A  1 106 ? 7.294   4.987   117.702 1.00 20.11 ? 81   ALA A C     1 
ATOM   615  O  O     . ALA A  1 106 ? 6.424   4.411   118.369 1.00 18.76 ? 81   ALA A O     1 
ATOM   616  C  CB    . ALA A  1 106 ? 7.149   7.471   117.522 1.00 17.71 ? 81   ALA A CB    1 
ATOM   617  N  N     . CYS A  1 107 ? 7.748   4.486   116.546 1.00 16.76 ? 82   CYS A N     1 
ATOM   618  C  CA    . CYS A  1 107 ? 7.036   3.389   115.886 1.00 18.48 ? 82   CYS A CA    1 
ATOM   619  C  C     . CYS A  1 107 ? 7.573   2.001   116.190 1.00 21.36 ? 82   CYS A C     1 
ATOM   620  O  O     . CYS A  1 107 ? 6.900   1.009   115.871 1.00 16.20 ? 82   CYS A O     1 
ATOM   621  C  CB    . CYS A  1 107 ? 7.060   3.586   114.360 1.00 19.98 ? 82   CYS A CB    1 
ATOM   622  S  SG    . CYS A  1 107 ? 6.107   5.032   113.782 1.00 23.65 ? 82   CYS A SG    1 
ATOM   623  N  N     . PHE A  1 108 ? 8.777   1.892   116.738 1.00 16.91 ? 83   PHE A N     1 
ATOM   624  C  CA    . PHE A  1 108 ? 9.347   0.564   116.906 1.00 15.03 ? 83   PHE A CA    1 
ATOM   625  C  C     . PHE A  1 108 ? 8.444   -0.336  117.752 1.00 14.06 ? 83   PHE A C     1 
ATOM   626  O  O     . PHE A  1 108 ? 8.339   -1.539  117.487 1.00 17.75 ? 83   PHE A O     1 
ATOM   627  C  CB    . PHE A  1 108 ? 10.752  0.655   117.524 1.00 17.47 ? 83   PHE A CB    1 
ATOM   628  C  CG    . PHE A  1 108 ? 11.412  -0.682  117.631 1.00 21.23 ? 83   PHE A CG    1 
ATOM   629  C  CD1   . PHE A  1 108 ? 11.785  -1.366  116.483 1.00 24.43 ? 83   PHE A CD1   1 
ATOM   630  C  CD2   . PHE A  1 108 ? 11.600  -1.293  118.871 1.00 19.96 ? 83   PHE A CD2   1 
ATOM   631  C  CE1   . PHE A  1 108 ? 12.367  -2.624  116.558 1.00 27.11 ? 83   PHE A CE1   1 
ATOM   632  C  CE2   . PHE A  1 108 ? 12.191  -2.540  118.960 1.00 23.08 ? 83   PHE A CE2   1 
ATOM   633  C  CZ    . PHE A  1 108 ? 12.573  -3.215  117.803 1.00 28.58 ? 83   PHE A CZ    1 
ATOM   634  N  N     . VAL A  1 109 ? 7.769   0.230   118.765 1.00 18.50 ? 84   VAL A N     1 
ATOM   635  C  CA    . VAL A  1 109 ? 6.898   -0.589  119.613 1.00 14.79 ? 84   VAL A CA    1 
ATOM   636  C  C     . VAL A  1 109 ? 5.742   -1.194  118.800 1.00 17.45 ? 84   VAL A C     1 
ATOM   637  O  O     . VAL A  1 109 ? 5.215   -2.260  119.146 1.00 14.62 ? 84   VAL A O     1 
ATOM   638  C  CB    . VAL A  1 109 ? 6.364   0.262   120.785 1.00 16.62 ? 84   VAL A CB    1 
ATOM   639  C  CG1   . VAL A  1 109 ? 5.464   1.410   120.293 1.00 16.41 ? 84   VAL A CG1   1 
ATOM   640  C  CG2   . VAL A  1 109 ? 5.632   -0.600  121.813 1.00 16.43 ? 84   VAL A CG2   1 
ATOM   641  N  N     . LEU A  1 110 ? 5.318   -0.511  117.726 1.00 17.08 ? 85   LEU A N     1 
ATOM   642  C  CA    . LEU A  1 110 ? 4.267   -1.029  116.854 1.00 14.46 ? 85   LEU A CA    1 
ATOM   643  C  C     . LEU A  1 110 ? 4.723   -2.266  116.120 1.00 16.38 ? 85   LEU A C     1 
ATOM   644  O  O     . LEU A  1 110 ? 3.910   -3.144  115.821 1.00 17.60 ? 85   LEU A O     1 
ATOM   645  C  CB    . LEU A  1 110 ? 3.868   0.056   115.850 1.00 18.41 ? 85   LEU A CB    1 
ATOM   646  C  CG    . LEU A  1 110 ? 3.455   1.360   116.520 1.00 23.89 ? 85   LEU A CG    1 
ATOM   647  C  CD1   . LEU A  1 110 ? 3.102   2.386   115.461 1.00 18.15 ? 85   LEU A CD1   1 
ATOM   648  C  CD2   . LEU A  1 110 ? 2.260   1.085   117.472 1.00 19.29 ? 85   LEU A CD2   1 
ATOM   649  N  N     . VAL A  1 111 ? 6.019   -2.346  115.813 1.00 16.34 ? 86   VAL A N     1 
ATOM   650  C  CA    . VAL A  1 111 ? 6.572   -3.572  115.227 1.00 14.04 ? 86   VAL A CA    1 
ATOM   651  C  C     . VAL A  1 111 ? 6.432   -4.729  116.207 1.00 16.17 ? 86   VAL A C     1 
ATOM   652  O  O     . VAL A  1 111 ? 6.020   -5.839  115.851 1.00 15.68 ? 86   VAL A O     1 
ATOM   653  C  CB    . VAL A  1 111 ? 8.046   -3.362  114.838 1.00 15.64 ? 86   VAL A CB    1 
ATOM   654  C  CG1   . VAL A  1 111 ? 8.645   -4.682  114.261 1.00 15.00 ? 86   VAL A CG1   1 
ATOM   655  C  CG2   . VAL A  1 111 ? 8.172   -2.228  113.858 1.00 17.17 ? 86   VAL A CG2   1 
ATOM   656  N  N     . LEU A  1 112 ? 6.781   -4.485  117.468 1.00 12.88 ? 87   LEU A N     1 
ATOM   657  C  CA    . LEU A  1 112 ? 6.742   -5.555  118.450 1.00 14.84 ? 87   LEU A CA    1 
ATOM   658  C  C     . LEU A  1 112 ? 5.303   -6.000  118.724 1.00 16.53 ? 87   LEU A C     1 
ATOM   659  O  O     . LEU A  1 112 ? 5.051   -7.192  118.916 1.00 17.85 ? 87   LEU A O     1 
ATOM   660  C  CB    . LEU A  1 112 ? 7.432   -5.073  119.746 1.00 16.17 ? 87   LEU A CB    1 
ATOM   661  C  CG    . LEU A  1 112 ? 8.915   -4.607  119.599 1.00 19.50 ? 87   LEU A CG    1 
ATOM   662  C  CD1   . LEU A  1 112 ? 9.523   -4.221  120.958 1.00 14.85 ? 87   LEU A CD1   1 
ATOM   663  C  CD2   . LEU A  1 112 ? 9.783   -5.654  118.893 1.00 17.16 ? 87   LEU A CD2   1 
ATOM   664  N  N     . ALA A  1 113 ? 4.362   -5.046  118.821 1.00 15.70 ? 88   ALA A N     1 
ATOM   665  C  CA    . ALA A  1 113 ? 2.957   -5.398  119.014 1.00 15.71 ? 88   ALA A CA    1 
ATOM   666  C  C     . ALA A  1 113 ? 2.445   -6.189  117.830 1.00 17.19 ? 88   ALA A C     1 
ATOM   667  O  O     . ALA A  1 113 ? 1.679   -7.141  117.997 1.00 17.68 ? 88   ALA A O     1 
ATOM   668  C  CB    . ALA A  1 113 ? 2.104   -4.140  119.191 1.00 12.35 ? 88   ALA A CB    1 
ATOM   669  N  N     . GLN A  1 114 ? 2.847   -5.797  116.621 1.00 15.45 ? 89   GLN A N     1 
ATOM   670  C  CA    . GLN A  1 114 ? 2.360   -6.505  115.440 1.00 16.13 ? 89   GLN A CA    1 
ATOM   671  C  C     . GLN A  1 114 ? 2.913   -7.918  115.433 1.00 21.39 ? 89   GLN A C     1 
ATOM   672  O  O     . GLN A  1 114 ? 2.187   -8.878  115.151 1.00 18.31 ? 89   GLN A O     1 
ATOM   673  C  CB    . GLN A  1 114 ? 2.789   -5.778  114.151 1.00 15.20 ? 89   GLN A CB    1 
ATOM   674  C  CG    . GLN A  1 114 ? 1.904   -6.166  112.958 1.00 22.22 ? 89   GLN A CG    1 
ATOM   675  C  CD    . GLN A  1 114 ? 0.444   -5.870  113.255 1.00 23.56 ? 89   GLN A CD    1 
ATOM   676  O  OE1   . GLN A  1 114 ? 0.130   -4.779  113.721 1.00 23.28 ? 89   GLN A OE1   1 
ATOM   677  N  NE2   . GLN A  1 114 ? -0.448  -6.836  113.009 1.00 20.97 ? 89   GLN A NE2   1 
ATOM   678  N  N     . SER A  1 115 ? 4.201   -8.072  115.774 1.00 16.58 ? 90   SER A N     1 
ATOM   679  C  CA    . SER A  1 115 ? 4.757   -9.419  115.866 1.00 15.30 ? 90   SER A CA    1 
ATOM   680  C  C     . SER A  1 115 ? 4.012   -10.257 116.898 1.00 19.35 ? 90   SER A C     1 
ATOM   681  O  O     . SER A  1 115 ? 3.756   -11.452 116.681 1.00 18.61 ? 90   SER A O     1 
ATOM   682  C  CB    . SER A  1 115 ? 6.247   -9.342  116.231 1.00 17.74 ? 90   SER A CB    1 
ATOM   683  O  OG    . SER A  1 115 ? 6.811   -10.652 116.327 1.00 17.47 ? 90   SER A OG    1 
ATOM   684  N  N     . SER A  1 116 ? 3.674   -9.648  118.041 1.00 16.15 ? 91   SER A N     1 
ATOM   685  C  CA    . SER A  1 116 ? 2.909   -10.356 119.067 1.00 17.19 ? 91   SER A CA    1 
ATOM   686  C  C     . SER A  1 116 ? 1.568   -10.817 118.513 1.00 18.48 ? 91   SER A C     1 
ATOM   687  O  O     . SER A  1 116 ? 1.134   -11.943 118.771 1.00 19.18 ? 91   SER A O     1 
ATOM   688  C  CB    . SER A  1 116 ? 2.698   -9.422  120.261 1.00 17.19 ? 91   SER A CB    1 
ATOM   689  O  OG    . SER A  1 116 ? 3.961   -9.084  120.840 1.00 21.79 ? 91   SER A OG    1 
ATOM   690  N  N     . ILE A  1 117 ? 0.888   -9.934  117.766 1.00 16.42 ? 92   ILE A N     1 
ATOM   691  C  CA    A ILE A  1 117 ? -0.389  -10.278 117.146 0.51 18.47 ? 92   ILE A CA    1 
ATOM   692  C  CA    B ILE A  1 117 ? -0.391  -10.292 117.168 0.49 18.45 ? 92   ILE A CA    1 
ATOM   693  C  C     . ILE A  1 117 ? -0.233  -11.484 116.228 1.00 17.33 ? 92   ILE A C     1 
ATOM   694  O  O     . ILE A  1 117 ? -1.046  -12.415 116.247 1.00 21.16 ? 92   ILE A O     1 
ATOM   695  C  CB    A ILE A  1 117 ? -0.954  -9.069  116.376 0.51 20.10 ? 92   ILE A CB    1 
ATOM   696  C  CB    B ILE A  1 117 ? -0.997  -9.076  116.444 0.49 20.21 ? 92   ILE A CB    1 
ATOM   697  C  CG1   A ILE A  1 117 ? -1.592  -8.066  117.342 0.51 21.10 ? 92   ILE A CG1   1 
ATOM   698  C  CG1   B ILE A  1 117 ? -1.571  -8.085  117.467 0.49 21.08 ? 92   ILE A CG1   1 
ATOM   699  C  CG2   A ILE A  1 117 ? -1.997  -9.527  115.361 0.51 19.59 ? 92   ILE A CG2   1 
ATOM   700  C  CG2   B ILE A  1 117 ? -2.098  -9.522  115.489 0.49 19.55 ? 92   ILE A CG2   1 
ATOM   701  C  CD1   A ILE A  1 117 ? -2.921  -8.538  117.869 0.51 19.36 ? 92   ILE A CD1   1 
ATOM   702  C  CD1   B ILE A  1 117 ? -1.627  -6.665  116.975 0.49 18.82 ? 92   ILE A CD1   1 
ATOM   703  N  N     . PHE A  1 118 ? 0.804   -11.474 115.389 1.00 17.69 ? 93   PHE A N     1 
ATOM   704  C  CA    . PHE A  1 118 ? 1.007   -12.600 114.473 1.00 20.46 ? 93   PHE A CA    1 
ATOM   705  C  C     . PHE A  1 118 ? 1.309   -13.884 115.242 1.00 22.79 ? 93   PHE A C     1 
ATOM   706  O  O     . PHE A  1 118 ? 0.771   -14.952 114.918 1.00 22.31 ? 93   PHE A O     1 
ATOM   707  C  CB    . PHE A  1 118 ? 2.141   -12.282 113.499 1.00 23.86 ? 93   PHE A CB    1 
ATOM   708  C  CG    . PHE A  1 118 ? 1.758   -11.312 112.409 1.00 27.09 ? 93   PHE A CG    1 
ATOM   709  C  CD1   . PHE A  1 118 ? 0.521   -11.397 111.775 1.00 42.06 ? 93   PHE A CD1   1 
ATOM   710  C  CD2   . PHE A  1 118 ? 2.623   -10.305 112.036 1.00 19.90 ? 93   PHE A CD2   1 
ATOM   711  C  CE1   . PHE A  1 118 ? 0.165   -10.490 110.774 1.00 45.15 ? 93   PHE A CE1   1 
ATOM   712  C  CE2   . PHE A  1 118 ? 2.269   -9.386  111.027 1.00 25.53 ? 93   PHE A CE2   1 
ATOM   713  C  CZ    . PHE A  1 118 ? 1.056   -9.484  110.401 1.00 31.54 ? 93   PHE A CZ    1 
ATOM   714  N  N     . SER A  1 119 ? 2.127   -13.794 116.298 1.00 18.52 ? 94   SER A N     1 
ATOM   715  C  CA    . SER A  1 119 ? 2.408   -14.993 117.095 1.00 20.07 ? 94   SER A CA    1 
ATOM   716  C  C     . SER A  1 119 ? 1.143   -15.516 117.758 1.00 22.20 ? 94   SER A C     1 
ATOM   717  O  O     . SER A  1 119 ? 0.940   -16.737 117.851 1.00 18.70 ? 94   SER A O     1 
ATOM   718  C  CB    . SER A  1 119 ? 3.468   -14.709 118.157 1.00 20.97 ? 94   SER A CB    1 
ATOM   719  O  OG    . SER A  1 119 ? 4.708   -14.412 117.550 1.00 25.94 ? 94   SER A OG    1 
ATOM   720  N  N     . LEU A  1 120 ? 0.322   -14.611 118.308 1.00 18.80 ? 95   LEU A N     1 
ATOM   721  C  CA    . LEU A  1 120 ? -0.906  -15.046 118.972 1.00 17.85 ? 95   LEU A CA    1 
ATOM   722  C  C     . LEU A  1 120 ? -1.855  -15.698 117.986 1.00 21.17 ? 95   LEU A C     1 
ATOM   723  O  O     . LEU A  1 120 ? -2.496  -16.709 118.302 1.00 25.23 ? 95   LEU A O     1 
ATOM   724  C  CB    . LEU A  1 120 ? -1.620  -13.858 119.612 1.00 16.87 ? 95   LEU A CB    1 
ATOM   725  C  CG    . LEU A  1 120 ? -0.945  -13.258 120.841 1.00 23.28 ? 95   LEU A CG    1 
ATOM   726  C  CD1   . LEU A  1 120 ? -1.581  -11.876 121.146 1.00 20.59 ? 95   LEU A CD1   1 
ATOM   727  C  CD2   . LEU A  1 120 ? -1.081  -14.217 122.014 1.00 22.43 ? 95   LEU A CD2   1 
ATOM   728  N  N     . LEU A  1 121 ? -1.960  -15.127 116.783 1.00 19.01 ? 96   LEU A N     1 
ATOM   729  C  CA    . LEU A  1 121 ? -2.808  -15.712 115.753 1.00 19.59 ? 96   LEU A CA    1 
ATOM   730  C  C     . LEU A  1 121 ? -2.270  -17.083 115.331 1.00 21.53 ? 96   LEU A C     1 
ATOM   731  O  O     . LEU A  1 121 ? -3.040  -18.035 115.133 1.00 22.54 ? 96   LEU A O     1 
ATOM   732  C  CB    . LEU A  1 121 ? -2.920  -14.747 114.563 1.00 21.74 ? 96   LEU A CB    1 
ATOM   733  C  CG    . LEU A  1 121 ? -3.833  -15.122 113.386 1.00 28.57 ? 96   LEU A CG    1 
ATOM   734  C  CD1   . LEU A  1 121 ? -5.229  -15.476 113.881 1.00 29.00 ? 96   LEU A CD1   1 
ATOM   735  C  CD2   . LEU A  1 121 ? -3.891  -13.985 112.331 1.00 30.14 ? 96   LEU A CD2   1 
ATOM   736  N  N     . ALA A  1 122 ? -0.952  -17.209 115.195 1.00 20.72 ? 97   ALA A N     1 
ATOM   737  C  CA    . ALA A  1 122 ? -0.382  -18.502 114.820 1.00 24.39 ? 97   ALA A CA    1 
ATOM   738  C  C     . ALA A  1 122 ? -0.685  -19.568 115.866 1.00 25.17 ? 97   ALA A C     1 
ATOM   739  O  O     . ALA A  1 122 ? -0.955  -20.724 115.524 1.00 24.00 ? 97   ALA A O     1 
ATOM   740  C  CB    . ALA A  1 122 ? 1.129   -18.386 114.653 1.00 21.87 ? 97   ALA A CB    1 
ATOM   741  N  N     . ILE A  1 123 ? -0.563  -19.215 117.150 1.00 24.62 ? 98   ILE A N     1 
ATOM   742  C  CA    . ILE A  1 123 ? -0.850  -20.166 118.225 1.00 23.91 ? 98   ILE A CA    1 
ATOM   743  C  C     . ILE A  1 123 ? -2.300  -20.633 118.157 1.00 24.92 ? 98   ILE A C     1 
ATOM   744  O  O     . ILE A  1 123 ? -2.584  -21.831 118.267 1.00 25.15 ? 98   ILE A O     1 
ATOM   745  C  CB    . ILE A  1 123 ? -0.499  -19.547 119.595 1.00 19.68 ? 98   ILE A CB    1 
ATOM   746  C  CG1   . ILE A  1 123 ? 1.030   -19.427 119.721 1.00 22.08 ? 98   ILE A CG1   1 
ATOM   747  C  CG2   . ILE A  1 123 ? -1.127  -20.375 120.721 1.00 23.66 ? 98   ILE A CG2   1 
ATOM   748  C  CD1   . ILE A  1 123 ? 1.518   -18.534 120.882 1.00 24.85 ? 98   ILE A CD1   1 
ATOM   749  N  N     . ALA A  1 124 ? -3.229  -19.711 117.914 1.00 22.88 ? 99   ALA A N     1 
ATOM   750  C  CA    . ALA A  1 124 ? -4.635  -20.088 117.823 1.00 22.36 ? 99   ALA A CA    1 
ATOM   751  C  C     . ALA A  1 124 ? -4.837  -21.053 116.662 1.00 26.72 ? 99   ALA A C     1 
ATOM   752  O  O     . ALA A  1 124 ? -5.480  -22.094 116.810 1.00 24.78 ? 99   ALA A O     1 
ATOM   753  C  CB    . ALA A  1 124 ? -5.506  -18.834 117.657 1.00 18.47 ? 99   ALA A CB    1 
ATOM   754  N  N     . ILE A  1 125 ? -4.249  -20.736 115.507 1.00 24.05 ? 100  ILE A N     1 
ATOM   755  C  CA    . ILE A  1 125 ? -4.430  -21.575 114.330 1.00 30.50 ? 100  ILE A CA    1 
ATOM   756  C  C     . ILE A  1 125 ? -3.783  -22.941 114.547 1.00 28.34 ? 100  ILE A C     1 
ATOM   757  O  O     . ILE A  1 125 ? -4.322  -23.975 114.130 1.00 25.29 ? 100  ILE A O     1 
ATOM   758  C  CB    . ILE A  1 125 ? -3.878  -20.868 113.077 1.00 26.09 ? 100  ILE A CB    1 
ATOM   759  C  CG1   . ILE A  1 125 ? -4.782  -19.695 112.712 1.00 22.92 ? 100  ILE A CG1   1 
ATOM   760  C  CG2   . ILE A  1 125 ? -3.761  -21.833 111.893 1.00 24.55 ? 100  ILE A CG2   1 
ATOM   761  C  CD1   . ILE A  1 125 ? -4.182  -18.778 111.716 1.00 30.98 ? 100  ILE A CD1   1 
ATOM   762  N  N     . ASP A  1 126 ? -2.610  -22.958 115.181 1.00 21.65 ? 101  ASP A N     1 
ATOM   763  C  CA    . ASP A  1 126 ? -1.940  -24.215 115.485 1.00 28.07 ? 101  ASP A CA    1 
ATOM   764  C  C     . ASP A  1 126 ? -2.821  -25.131 116.336 1.00 31.13 ? 101  ASP A C     1 
ATOM   765  O  O     . ASP A  1 126 ? -2.936  -26.334 116.065 1.00 25.26 ? 101  ASP A O     1 
ATOM   766  C  CB    . ASP A  1 126 ? -0.608  -23.913 116.182 1.00 24.15 ? 101  ASP A CB    1 
ATOM   767  C  CG    . ASP A  1 126 ? 0.122   -25.166 116.619 1.00 30.47 ? 101  ASP A CG    1 
ATOM   768  O  OD1   . ASP A  1 126 ? 0.742   -25.791 115.752 1.00 30.63 ? 101  ASP A OD1   1 
ATOM   769  O  OD2   . ASP A  1 126 ? 0.116   -25.509 117.813 1.00 29.65 ? 101  ASP A OD2   1 
ATOM   770  N  N     . ARG A  1 127 ? -3.436  -24.584 117.389 1.00 24.79 ? 102  ARG A N     1 
ATOM   771  C  CA    . ARG A  1 127 ? -4.306  -25.398 118.239 1.00 25.83 ? 102  ARG A CA    1 
ATOM   772  C  C     . ARG A  1 127 ? -5.562  -25.833 117.506 1.00 30.08 ? 102  ARG A C     1 
ATOM   773  O  O     . ARG A  1 127 ? -6.097  -26.909 117.783 1.00 29.58 ? 102  ARG A O     1 
ATOM   774  C  CB    . ARG A  1 127 ? -4.640  -24.646 119.521 1.00 29.03 ? 102  ARG A CB    1 
ATOM   775  C  CG    . ARG A  1 127 ? -3.435  -24.372 120.419 1.00 30.77 ? 102  ARG A CG    1 
ATOM   776  C  CD    . ARG A  1 127 ? -2.801  -25.676 120.986 1.00 33.02 ? 102  ARG A CD    1 
ATOM   777  N  NE    . ARG A  1 127 ? -1.882  -26.330 120.052 1.00 37.38 ? 102  ARG A NE    1 
ATOM   778  C  CZ    . ARG A  1 127 ? -1.740  -27.644 119.923 1.00 38.18 ? 102  ARG A CZ    1 
ATOM   779  N  NH1   . ARG A  1 127 ? -2.449  -28.486 120.657 1.00 37.42 ? 102  ARG A NH1   1 
ATOM   780  N  NH2   . ARG A  1 127 ? -0.877  -28.126 119.022 1.00 32.38 ? 102  ARG A NH2   1 
ATOM   781  N  N     . TYR A  1 128 ? -6.054  -25.014 116.577 1.00 25.32 ? 103  TYR A N     1 
ATOM   782  C  CA    . TYR A  1 128 ? -7.195  -25.448 115.791 1.00 31.59 ? 103  TYR A CA    1 
ATOM   783  C  C     . TYR A  1 128 ? -6.829  -26.618 114.878 1.00 32.12 ? 103  TYR A C     1 
ATOM   784  O  O     . TYR A  1 128 ? -7.573  -27.599 114.802 1.00 30.74 ? 103  TYR A O     1 
ATOM   785  C  CB    . TYR A  1 128 ? -7.768  -24.295 114.981 1.00 28.64 ? 103  TYR A CB    1 
ATOM   786  C  CG    . TYR A  1 128 ? -8.894  -24.763 114.097 1.00 31.55 ? 103  TYR A CG    1 
ATOM   787  C  CD1   . TYR A  1 128 ? -10.136 -25.082 114.636 1.00 30.18 ? 103  TYR A CD1   1 
ATOM   788  C  CD2   . TYR A  1 128 ? -8.716  -24.904 112.738 1.00 39.05 ? 103  TYR A CD2   1 
ATOM   789  C  CE1   . TYR A  1 128 ? -11.184 -25.527 113.827 1.00 34.16 ? 103  TYR A CE1   1 
ATOM   790  C  CE2   . TYR A  1 128 ? -9.755  -25.350 111.920 1.00 46.99 ? 103  TYR A CE2   1 
ATOM   791  C  CZ    . TYR A  1 128 ? -10.986 -25.654 112.471 1.00 39.81 ? 103  TYR A CZ    1 
ATOM   792  O  OH    . TYR A  1 128 ? -12.014 -26.106 111.660 1.00 46.56 ? 103  TYR A OH    1 
ATOM   793  N  N     . ILE A  1 129 ? -5.685  -26.555 114.203 1.00 29.83 ? 104  ILE A N     1 
ATOM   794  C  CA    . ILE A  1 129 ? -5.270  -27.692 113.375 1.00 35.40 ? 104  ILE A CA    1 
ATOM   795  C  C     . ILE A  1 129 ? -5.114  -28.941 114.227 1.00 33.18 ? 104  ILE A C     1 
ATOM   796  O  O     . ILE A  1 129 ? -5.521  -30.038 113.829 1.00 35.58 ? 104  ILE A O     1 
ATOM   797  C  CB    . ILE A  1 129 ? -3.987  -27.374 112.587 1.00 33.37 ? 104  ILE A CB    1 
ATOM   798  C  CG1   . ILE A  1 129 ? -4.221  -26.200 111.630 1.00 30.22 ? 104  ILE A CG1   1 
ATOM   799  C  CG2   . ILE A  1 129 ? -3.489  -28.606 111.825 1.00 36.82 ? 104  ILE A CG2   1 
ATOM   800  C  CD1   . ILE A  1 129 ? -2.930  -25.654 111.044 1.00 31.20 ? 104  ILE A CD1   1 
ATOM   801  N  N     . ALA A  1 130 ? -4.547  -28.795 115.420 1.00 27.96 ? 105  ALA A N     1 
ATOM   802  C  CA    . ALA A  1 130 ? -4.329  -29.954 116.275 1.00 28.79 ? 105  ALA A CA    1 
ATOM   803  C  C     . ALA A  1 130 ? -5.655  -30.580 116.711 1.00 36.49 ? 105  ALA A C     1 
ATOM   804  O  O     . ALA A  1 130 ? -5.744  -31.805 116.821 1.00 45.17 ? 105  ALA A O     1 
ATOM   805  C  CB    . ALA A  1 130 ? -3.478  -29.567 117.490 1.00 30.42 ? 105  ALA A CB    1 
ATOM   806  N  N     . ILE A  1 131 ? -6.699  -29.770 116.945 1.00 32.99 ? 106  ILE A N     1 
ATOM   807  C  CA    . ILE A  1 131 ? -7.977  -30.335 117.392 1.00 34.05 ? 106  ILE A CA    1 
ATOM   808  C  C     . ILE A  1 131 ? -8.826  -30.820 116.213 1.00 40.44 ? 106  ILE A C     1 
ATOM   809  O  O     . ILE A  1 131 ? -9.636  -31.742 116.361 1.00 40.34 ? 106  ILE A O     1 
ATOM   810  C  CB    . ILE A  1 131 ? -8.779  -29.323 118.237 1.00 35.64 ? 106  ILE A CB    1 
ATOM   811  C  CG1   . ILE A  1 131 ? -9.945  -30.015 118.944 1.00 42.65 ? 106  ILE A CG1   1 
ATOM   812  C  CG2   . ILE A  1 131 ? -9.407  -28.225 117.356 1.00 31.46 ? 106  ILE A CG2   1 
ATOM   813  C  CD1   . ILE A  1 131 ? -9.606  -30.597 120.304 1.00 47.86 ? 106  ILE A CD1   1 
ATOM   814  N  N     . ALA A  1 132 ? -8.665  -30.229 115.034 1.00 33.00 ? 107  ALA A N     1 
ATOM   815  C  CA    . ALA A  1 132 ? -9.577  -30.511 113.941 1.00 37.85 ? 107  ALA A CA    1 
ATOM   816  C  C     . ALA A  1 132 ? -9.040  -31.608 113.026 1.00 41.11 ? 107  ALA A C     1 
ATOM   817  O  O     . ALA A  1 132 ? -9.814  -32.430 112.524 1.00 46.84 ? 107  ALA A O     1 
ATOM   818  C  CB    . ALA A  1 132 ? -9.827  -29.233 113.129 1.00 36.13 ? 107  ALA A CB    1 
ATOM   819  N  N     . ILE A  1 133 ? -7.731  -31.670 112.824 1.00 35.57 ? 108  ILE A N     1 
ATOM   820  C  CA    . ILE A  1 133 ? -7.154  -32.748 112.030 1.00 40.97 ? 108  ILE A CA    1 
ATOM   821  C  C     . ILE A  1 133 ? -5.916  -33.305 112.723 1.00 39.89 ? 108  ILE A C     1 
ATOM   822  O  O     . ILE A  1 133 ? -4.809  -33.208 112.171 1.00 37.78 ? 108  ILE A O     1 
ATOM   823  C  CB    . ILE A  1 133 ? -6.822  -32.271 110.608 1.00 46.44 ? 108  ILE A CB    1 
ATOM   824  C  CG1   . ILE A  1 133 ? -6.251  -30.856 110.631 1.00 46.52 ? 108  ILE A CG1   1 
ATOM   825  C  CG2   . ILE A  1 133 ? -8.085  -32.261 109.768 1.00 48.34 ? 108  ILE A CG2   1 
ATOM   826  C  CD1   . ILE A  1 133 ? -5.715  -30.417 109.288 1.00 48.25 ? 108  ILE A CD1   1 
ATOM   827  N  N     . PRO A  1 134 ? -6.039  -33.935 113.896 1.00 37.57 ? 109  PRO A N     1 
ATOM   828  C  CA    . PRO A  1 134 ? -4.824  -34.417 114.582 1.00 46.54 ? 109  PRO A CA    1 
ATOM   829  C  C     . PRO A  1 134 ? -4.041  -35.446 113.777 1.00 48.89 ? 109  PRO A C     1 
ATOM   830  O  O     . PRO A  1 134 ? -2.822  -35.563 113.961 1.00 44.42 ? 109  PRO A O     1 
ATOM   831  C  CB    . PRO A  1 134 ? -5.379  -35.036 115.874 1.00 38.55 ? 109  PRO A CB    1 
ATOM   832  C  CG    . PRO A  1 134 ? -6.829  -35.326 115.564 1.00 38.62 ? 109  PRO A CG    1 
ATOM   833  C  CD    . PRO A  1 134 ? -7.264  -34.232 114.656 1.00 38.70 ? 109  PRO A CD    1 
ATOM   834  N  N     . LEU A  1 135 ? -4.690  -36.146 112.842 1.00 52.59 ? 110  LEU A N     1 
ATOM   835  C  CA    . LEU A  1 135 ? -4.008  -37.181 112.077 1.00 53.92 ? 110  LEU A CA    1 
ATOM   836  C  C     . LEU A  1 135 ? -3.026  -36.575 111.085 1.00 51.47 ? 110  LEU A C     1 
ATOM   837  O  O     . LEU A  1 135 ? -2.030  -37.214 110.729 1.00 52.47 ? 110  LEU A O     1 
ATOM   838  C  CB    . LEU A  1 135 ? -5.026  -38.065 111.363 1.00 56.02 ? 110  LEU A CB    1 
ATOM   839  C  CG    . LEU A  1 135 ? -5.895  -38.846 112.349 1.00 59.20 ? 110  LEU A CG    1 
ATOM   840  C  CD1   . LEU A  1 135 ? -6.916  -39.692 111.613 1.00 64.02 ? 110  LEU A CD1   1 
ATOM   841  C  CD2   . LEU A  1 135 ? -5.038  -39.704 113.285 1.00 50.71 ? 110  LEU A CD2   1 
ATOM   842  N  N     . ARG A  1 136 ? -3.257  -35.342 110.656 1.00 44.45 ? 111  ARG A N     1 
ATOM   843  C  CA    . ARG A  1 136 ? -2.379  -34.722 109.683 1.00 46.74 ? 111  ARG A CA    1 
ATOM   844  C  C     . ARG A  1 136 ? -1.627  -33.530 110.259 1.00 53.41 ? 111  ARG A C     1 
ATOM   845  O  O     . ARG A  1 136 ? -0.859  -32.889 109.529 1.00 42.98 ? 111  ARG A O     1 
ATOM   846  C  CB    . ARG A  1 136 ? -3.208  -34.273 108.470 1.00 47.09 ? 111  ARG A CB    1 
ATOM   847  N  N     . TYR A  1 137 ? -1.775  -33.263 111.562 1.00 44.39 ? 112  TYR A N     1 
ATOM   848  C  CA    . TYR A  1 137 ? -1.065  -32.153 112.189 1.00 40.60 ? 112  TYR A CA    1 
ATOM   849  C  C     . TYR A  1 137 ? 0.448   -32.296 111.998 1.00 44.30 ? 112  TYR A C     1 
ATOM   850  O  O     . TYR A  1 137 ? 1.120   -31.373 111.523 1.00 39.48 ? 112  TYR A O     1 
ATOM   851  C  CB    . TYR A  1 137 ? -1.459  -32.037 113.667 1.00 37.38 ? 112  TYR A CB    1 
ATOM   852  C  CG    . TYR A  1 137 ? -0.660  -30.987 114.433 1.00 36.41 ? 112  TYR A CG    1 
ATOM   853  C  CD1   . TYR A  1 137 ? -1.088  -29.659 114.470 1.00 33.09 ? 112  TYR A CD1   1 
ATOM   854  C  CD2   . TYR A  1 137 ? 0.515   -31.313 115.101 1.00 39.64 ? 112  TYR A CD2   1 
ATOM   855  C  CE1   . TYR A  1 137 ? -0.371  -28.690 115.153 1.00 30.18 ? 112  TYR A CE1   1 
ATOM   856  C  CE2   . TYR A  1 137 ? 1.252   -30.343 115.783 1.00 44.85 ? 112  TYR A CE2   1 
ATOM   857  C  CZ    . TYR A  1 137 ? 0.799   -29.029 115.808 1.00 40.91 ? 112  TYR A CZ    1 
ATOM   858  O  OH    . TYR A  1 137 ? 1.521   -28.062 116.494 1.00 34.15 ? 112  TYR A OH    1 
ATOM   859  N  N     . ASN A  1 138 ? 1.016   -33.426 112.430 1.00 42.80 ? 113  ASN A N     1 
ATOM   860  C  CA    . ASN A  1 138 ? 2.471   -33.548 112.426 1.00 50.51 ? 113  ASN A CA    1 
ATOM   861  C  C     . ASN A  1 138 ? 3.066   -33.446 111.023 1.00 46.26 ? 113  ASN A C     1 
ATOM   862  O  O     . ASN A  1 138 ? 4.213   -33.010 110.860 1.00 45.72 ? 113  ASN A O     1 
ATOM   863  C  CB    . ASN A  1 138 ? 2.900   -34.823 113.124 1.00 51.81 ? 113  ASN A CB    1 
ATOM   864  C  CG    . ASN A  1 138 ? 2.877   -34.660 114.616 1.00 57.34 ? 113  ASN A CG    1 
ATOM   865  O  OD1   . ASN A  1 138 ? 3.266   -33.607 115.139 1.00 57.16 ? 113  ASN A OD1   1 
ATOM   866  N  ND2   . ASN A  1 138 ? 2.491   -35.708 115.318 1.00 68.31 ? 113  ASN A ND2   1 
ATOM   867  N  N     . GLY A  1 139 ? 2.336   -33.891 110.006 1.00 42.02 ? 114  GLY A N     1 
ATOM   868  C  CA    . GLY A  1 139 ? 2.833   -33.709 108.664 1.00 47.33 ? 114  GLY A CA    1 
ATOM   869  C  C     . GLY A  1 139 ? 2.611   -32.317 108.106 1.00 48.41 ? 114  GLY A C     1 
ATOM   870  O  O     . GLY A  1 139 ? 3.338   -31.911 107.194 1.00 50.42 ? 114  GLY A O     1 
ATOM   871  N  N     . LEU A  1 140 ? 1.612   -31.583 108.610 1.00 46.66 ? 115  LEU A N     1 
ATOM   872  C  CA    . LEU A  1 140 ? 1.343   -30.250 108.077 1.00 42.20 ? 115  LEU A CA    1 
ATOM   873  C  C     . LEU A  1 140 ? 2.160   -29.173 108.793 1.00 44.03 ? 115  LEU A C     1 
ATOM   874  O  O     . LEU A  1 140 ? 2.736   -28.297 108.141 1.00 41.55 ? 115  LEU A O     1 
ATOM   875  C  CB    . LEU A  1 140 ? -0.156  -29.963 108.182 1.00 42.59 ? 115  LEU A CB    1 
ATOM   876  C  CG    . LEU A  1 140 ? -0.708  -28.543 108.080 1.00 52.52 ? 115  LEU A CG    1 
ATOM   877  C  CD1   . LEU A  1 140 ? -0.238  -27.850 106.809 1.00 58.29 ? 115  LEU A CD1   1 
ATOM   878  C  CD2   . LEU A  1 140 ? -2.217  -28.559 108.165 1.00 50.60 ? 115  LEU A CD2   1 
ATOM   879  N  N     . VAL A  1 141 ? 2.265   -29.256 110.117 1.00 41.47 ? 116  VAL A N     1 
ATOM   880  C  CA    . VAL A  1 141 ? 2.835   -28.207 110.961 1.00 36.10 ? 116  VAL A CA    1 
ATOM   881  C  C     . VAL A  1 141 ? 4.171   -28.740 111.476 1.00 41.08 ? 116  VAL A C     1 
ATOM   882  O  O     . VAL A  1 141 ? 4.213   -29.550 112.411 1.00 47.66 ? 116  VAL A O     1 
ATOM   883  C  CB    . VAL A  1 141 ? 1.909   -27.815 112.119 1.00 38.86 ? 116  VAL A CB    1 
ATOM   884  C  CG1   . VAL A  1 141 ? 2.451   -26.594 112.845 1.00 38.21 ? 116  VAL A CG1   1 
ATOM   885  C  CG2   . VAL A  1 141 ? 0.502   -27.542 111.627 1.00 42.51 ? 116  VAL A CG2   1 
ATOM   886  N  N     . THR A  1 142 ? 5.262   -28.302 110.851 1.00 33.36 ? 117  THR A N     1 
ATOM   887  C  CA    . THR A  1 142 ? 6.613   -28.761 111.131 1.00 36.51 ? 117  THR A CA    1 
ATOM   888  C  C     . THR A  1 142 ? 7.437   -27.604 111.667 1.00 37.76 ? 117  THR A C     1 
ATOM   889  O  O     . THR A  1 142 ? 7.082   -26.434 111.499 1.00 35.69 ? 117  THR A O     1 
ATOM   890  C  CB    . THR A  1 142 ? 7.304   -29.302 109.875 1.00 39.37 ? 117  THR A CB    1 
ATOM   891  O  OG1   . THR A  1 142 ? 7.536   -28.215 108.976 1.00 41.13 ? 117  THR A OG1   1 
ATOM   892  C  CG2   . THR A  1 142 ? 6.430   -30.362 109.168 1.00 38.30 ? 117  THR A CG2   1 
ATOM   893  N  N     . GLY A  1 143 ? 8.537   -27.940 112.338 1.00 34.39 ? 118  GLY A N     1 
ATOM   894  C  CA    . GLY A  1 143 ? 9.394   -26.898 112.878 1.00 37.16 ? 118  GLY A CA    1 
ATOM   895  C  C     . GLY A  1 143 ? 9.986   -25.989 111.812 1.00 39.34 ? 118  GLY A C     1 
ATOM   896  O  O     . GLY A  1 143 ? 10.047  -24.770 111.994 1.00 40.98 ? 118  GLY A O     1 
ATOM   897  N  N     . THR A  1 144 ? 10.418  -26.555 110.679 1.00 36.17 ? 119  THR A N     1 
ATOM   898  C  CA    . THR A  1 144 ? 11.000  -25.704 109.634 1.00 36.66 ? 119  THR A CA    1 
ATOM   899  C  C     . THR A  1 144 ? 9.949   -24.778 109.031 1.00 33.71 ? 119  THR A C     1 
ATOM   900  O  O     . THR A  1 144 ? 10.246  -23.624 108.712 1.00 41.49 ? 119  THR A O     1 
ATOM   901  C  CB    . THR A  1 144 ? 11.729  -26.517 108.553 1.00 46.57 ? 119  THR A CB    1 
ATOM   902  O  OG1   . THR A  1 144 ? 10.817  -27.370 107.856 1.00 48.67 ? 119  THR A OG1   1 
ATOM   903  C  CG2   . THR A  1 144 ? 12.847  -27.334 109.170 1.00 42.30 ? 119  THR A CG2   1 
ATOM   904  N  N     . ARG A  1 145 ? 8.720   -25.261 108.851 1.00 38.53 ? 120  ARG A N     1 
ATOM   905  C  CA    . ARG A  1 145 ? 7.686   -24.365 108.343 1.00 44.34 ? 120  ARG A CA    1 
ATOM   906  C  C     . ARG A  1 145 ? 7.331   -23.301 109.382 1.00 35.03 ? 120  ARG A C     1 
ATOM   907  O  O     . ARG A  1 145 ? 7.168   -22.125 109.035 1.00 35.43 ? 120  ARG A O     1 
ATOM   908  C  CB    . ARG A  1 145 ? 6.445   -25.165 107.940 1.00 39.41 ? 120  ARG A CB    1 
ATOM   909  C  CG    . ARG A  1 145 ? 6.624   -26.015 106.675 1.00 38.15 ? 120  ARG A CG    1 
ATOM   910  C  CD    . ARG A  1 145 ? 5.402   -26.879 106.430 1.00 38.64 ? 120  ARG A CD    1 
ATOM   911  N  NE    . ARG A  1 145 ? 5.638   -27.903 105.423 1.00 47.17 ? 120  ARG A NE    1 
ATOM   912  C  CZ    . ARG A  1 145 ? 4.802   -28.899 105.164 1.00 40.84 ? 120  ARG A CZ    1 
ATOM   913  N  NH1   . ARG A  1 145 ? 3.720   -29.101 105.897 1.00 42.82 ? 120  ARG A NH1   1 
ATOM   914  N  NH2   . ARG A  1 145 ? 5.065   -29.724 104.153 1.00 53.66 ? 120  ARG A NH2   1 
ATOM   915  N  N     . ALA A  1 146 ? 7.278   -23.678 110.662 1.00 29.37 ? 121  ALA A N     1 
ATOM   916  C  CA    . ALA A  1 146 ? 7.040   -22.687 111.710 1.00 32.98 ? 121  ALA A CA    1 
ATOM   917  C  C     . ALA A  1 146 ? 8.128   -21.614 111.721 1.00 32.67 ? 121  ALA A C     1 
ATOM   918  O  O     . ALA A  1 146 ? 7.826   -20.415 111.813 1.00 32.40 ? 121  ALA A O     1 
ATOM   919  C  CB    . ALA A  1 146 ? 6.949   -23.378 113.070 1.00 32.94 ? 121  ALA A CB    1 
ATOM   920  N  N     . ALA A  1 147 ? 9.399   -22.013 111.586 1.00 30.25 ? 122  ALA A N     1 
ATOM   921  C  CA    . ALA A  1 147 ? 10.479  -21.025 111.639 1.00 33.51 ? 122  ALA A CA    1 
ATOM   922  C  C     . ALA A  1 147 ? 10.396  -20.070 110.452 1.00 36.16 ? 122  ALA A C     1 
ATOM   923  O  O     . ALA A  1 147 ? 10.704  -18.875 110.582 1.00 28.66 ? 122  ALA A O     1 
ATOM   924  C  CB    . ALA A  1 147 ? 11.842  -21.713 111.669 1.00 32.29 ? 122  ALA A CB    1 
ATOM   925  N  N     . GLY A  1 148 ? 9.998   -20.588 109.282 1.00 31.88 ? 123  GLY A N     1 
ATOM   926  C  CA    . GLY A  1 148 ? 9.782   -19.727 108.126 1.00 31.94 ? 123  GLY A CA    1 
ATOM   927  C  C     . GLY A  1 148 ? 8.618   -18.764 108.317 1.00 31.98 ? 123  GLY A C     1 
ATOM   928  O  O     . GLY A  1 148 ? 8.683   -17.601 107.903 1.00 30.04 ? 123  GLY A O     1 
ATOM   929  N  N     . ILE A  1 149 ? 7.511   -19.253 108.880 1.00 26.25 ? 124  ILE A N     1 
ATOM   930  C  CA    . ILE A  1 149 ? 6.368   -18.389 109.174 1.00 27.67 ? 124  ILE A CA    1 
ATOM   931  C  C     . ILE A  1 149 ? 6.781   -17.285 110.141 1.00 27.20 ? 124  ILE A C     1 
ATOM   932  O  O     . ILE A  1 149 ? 6.417   -16.112 109.968 1.00 25.36 ? 124  ILE A O     1 
ATOM   933  C  CB    . ILE A  1 149 ? 5.206   -19.227 109.743 1.00 29.19 ? 124  ILE A CB    1 
ATOM   934  C  CG1   . ILE A  1 149 ? 4.710   -20.258 108.726 1.00 36.48 ? 124  ILE A CG1   1 
ATOM   935  C  CG2   . ILE A  1 149 ? 4.017   -18.335 110.186 1.00 21.33 ? 124  ILE A CG2   1 
ATOM   936  C  CD1   . ILE A  1 149 ? 3.755   -19.697 107.718 1.00 46.95 ? 124  ILE A CD1   1 
ATOM   937  N  N     . ILE A  1 150 ? 7.540   -17.646 111.181 1.00 21.76 ? 125  ILE A N     1 
ATOM   938  C  CA    . ILE A  1 150 ? 7.995   -16.647 112.153 1.00 27.18 ? 125  ILE A CA    1 
ATOM   939  C  C     . ILE A  1 150 ? 8.850   -15.572 111.488 1.00 29.60 ? 125  ILE A C     1 
ATOM   940  O  O     . ILE A  1 150 ? 8.690   -14.377 111.771 1.00 25.15 ? 125  ILE A O     1 
ATOM   941  C  CB    . ILE A  1 150 ? 8.729   -17.331 113.326 1.00 26.76 ? 125  ILE A CB    1 
ATOM   942  C  CG1   . ILE A  1 150 ? 7.735   -18.170 114.124 1.00 28.02 ? 125  ILE A CG1   1 
ATOM   943  C  CG2   . ILE A  1 150 ? 9.446   -16.280 114.241 1.00 21.37 ? 125  ILE A CG2   1 
ATOM   944  C  CD1   . ILE A  1 150 ? 8.383   -19.116 115.113 1.00 25.58 ? 125  ILE A CD1   1 
ATOM   945  N  N     . ALA A  1 151 ? 9.771   -15.971 110.603 1.00 23.05 ? 126  ALA A N     1 
ATOM   946  C  CA    . ALA A  1 151 ? 10.603  -15.003 109.889 1.00 24.95 ? 126  ALA A CA    1 
ATOM   947  C  C     . ALA A  1 151 ? 9.748   -14.056 109.048 1.00 22.33 ? 126  ALA A C     1 
ATOM   948  O  O     . ALA A  1 151 ? 9.973   -12.837 109.034 1.00 23.54 ? 126  ALA A O     1 
ATOM   949  C  CB    . ALA A  1 151 ? 11.640  -15.742 109.023 1.00 26.17 ? 126  ALA A CB    1 
ATOM   950  N  N     . ILE A  1 152 ? 8.788   -14.613 108.306 1.00 25.06 ? 127  ILE A N     1 
ATOM   951  C  CA    . ILE A  1 152 ? 7.897   -13.816 107.471 1.00 29.48 ? 127  ILE A CA    1 
ATOM   952  C  C     . ILE A  1 152 ? 7.100   -12.841 108.327 1.00 23.44 ? 127  ILE A C     1 
ATOM   953  O  O     . ILE A  1 152 ? 6.930   -11.672 107.971 1.00 22.48 ? 127  ILE A O     1 
ATOM   954  C  CB    . ILE A  1 152 ? 6.971   -14.739 106.663 1.00 28.09 ? 127  ILE A CB    1 
ATOM   955  C  CG1   . ILE A  1 152 ? 7.770   -15.471 105.582 1.00 29.99 ? 127  ILE A CG1   1 
ATOM   956  C  CG2   . ILE A  1 152 ? 5.822   -13.936 106.047 1.00 25.32 ? 127  ILE A CG2   1 
ATOM   957  C  CD1   . ILE A  1 152 ? 6.957   -16.584 104.933 1.00 36.26 ? 127  ILE A CD1   1 
ATOM   958  N  N     . CYS A  1 153 ? 6.595   -13.308 109.471 1.00 22.40 ? 128  CYS A N     1 
ATOM   959  C  CA    . CYS A  1 153 ? 5.775   -12.447 110.315 1.00 24.18 ? 128  CYS A CA    1 
ATOM   960  C  C     . CYS A  1 153 ? 6.595   -11.300 110.897 1.00 22.37 ? 128  CYS A C     1 
ATOM   961  O  O     . CYS A  1 153 ? 6.100   -10.169 111.011 1.00 20.60 ? 128  CYS A O     1 
ATOM   962  C  CB    . CYS A  1 153 ? 5.104   -13.284 111.403 1.00 25.00 ? 128  CYS A CB    1 
ATOM   963  S  SG    . CYS A  1 153 ? 3.783   -14.303 110.699 1.00 29.14 ? 128  CYS A SG    1 
ATOM   964  N  N     . TRP A  1 154 ? 7.863   -11.555 111.231 1.00 16.80 ? 129  TRP A N     1 
ATOM   965  C  CA    . TRP A  1 154 ? 8.712   -10.463 111.711 1.00 26.57 ? 129  TRP A CA    1 
ATOM   966  C  C     . TRP A  1 154 ? 8.966   -9.433  110.610 1.00 25.79 ? 129  TRP A C     1 
ATOM   967  O  O     . TRP A  1 154 ? 8.984   -8.226  110.877 1.00 19.35 ? 129  TRP A O     1 
ATOM   968  C  CB    . TRP A  1 154 ? 10.037  -10.993 112.234 1.00 24.41 ? 129  TRP A CB    1 
ATOM   969  C  CG    . TRP A  1 154 ? 9.968   -11.404 113.674 1.00 22.81 ? 129  TRP A CG    1 
ATOM   970  C  CD1   . TRP A  1 154 ? 9.851   -12.676 114.166 1.00 23.10 ? 129  TRP A CD1   1 
ATOM   971  C  CD2   . TRP A  1 154 ? 9.977   -10.529 114.807 1.00 20.65 ? 129  TRP A CD2   1 
ATOM   972  N  NE1   . TRP A  1 154 ? 9.830   -12.642 115.542 1.00 24.74 ? 129  TRP A NE1   1 
ATOM   973  C  CE2   . TRP A  1 154 ? 9.898   -11.336 115.959 1.00 21.80 ? 129  TRP A CE2   1 
ATOM   974  C  CE3   . TRP A  1 154 ? 10.059  -9.135  114.957 1.00 22.56 ? 129  TRP A CE3   1 
ATOM   975  C  CZ2   . TRP A  1 154 ? 9.883   -10.797 117.260 1.00 24.57 ? 129  TRP A CZ2   1 
ATOM   976  C  CZ3   . TRP A  1 154 ? 10.076  -8.600  116.239 1.00 23.28 ? 129  TRP A CZ3   1 
ATOM   977  C  CH2   . TRP A  1 154 ? 9.973   -9.433  117.380 1.00 21.52 ? 129  TRP A CH2   1 
ATOM   978  N  N     . VAL A  1 155 ? 9.177   -9.885  109.370 1.00 23.56 ? 130  VAL A N     1 
ATOM   979  C  CA    . VAL A  1 155 ? 9.352   -8.943  108.268 1.00 21.88 ? 130  VAL A CA    1 
ATOM   980  C  C     . VAL A  1 155 ? 8.093   -8.103  108.089 1.00 17.10 ? 130  VAL A C     1 
ATOM   981  O  O     . VAL A  1 155 ? 8.162   -6.875  107.970 1.00 18.81 ? 130  VAL A O     1 
ATOM   982  C  CB    . VAL A  1 155 ? 9.713   -9.688  106.969 1.00 26.81 ? 130  VAL A CB    1 
ATOM   983  C  CG1   . VAL A  1 155 ? 9.677   -8.728  105.792 1.00 28.98 ? 130  VAL A CG1   1 
ATOM   984  C  CG2   . VAL A  1 155 ? 11.105  -10.288 107.092 1.00 22.97 ? 130  VAL A CG2   1 
ATOM   985  N  N     . LEU A  1 156 ? 6.928   -8.757  108.042 1.00 19.62 ? 131  LEU A N     1 
ATOM   986  C  CA    . LEU A  1 156 ? 5.661   -8.039  107.893 1.00 21.40 ? 131  LEU A CA    1 
ATOM   987  C  C     . LEU A  1 156 ? 5.410   -7.099  109.071 1.00 21.25 ? 131  LEU A C     1 
ATOM   988  O  O     . LEU A  1 156 ? 4.789   -6.037  108.912 1.00 21.54 ? 131  LEU A O     1 
ATOM   989  C  CB    . LEU A  1 156 ? 4.511   -9.041  107.776 1.00 20.65 ? 131  LEU A CB    1 
ATOM   990  C  CG    . LEU A  1 156 ? 4.554   -9.936  106.531 1.00 27.14 ? 131  LEU A CG    1 
ATOM   991  C  CD1   . LEU A  1 156 ? 3.472   -11.004 106.632 1.00 29.44 ? 131  LEU A CD1   1 
ATOM   992  C  CD2   . LEU A  1 156 ? 4.398   -9.101  105.271 1.00 25.92 ? 131  LEU A CD2   1 
ATOM   993  N  N     . SER A  1 157 ? 5.862   -7.485  110.261 1.00 17.97 ? 132  SER A N     1 
ATOM   994  C  CA    . SER A  1 157 ? 5.689   -6.629  111.433 1.00 16.21 ? 132  SER A CA    1 
ATOM   995  C  C     . SER A  1 157 ? 6.499   -5.341  111.302 1.00 18.20 ? 132  SER A C     1 
ATOM   996  O  O     . SER A  1 157 ? 6.019   -4.262  111.687 1.00 16.89 ? 132  SER A O     1 
ATOM   997  C  CB    . SER A  1 157 ? 6.109   -7.375  112.691 1.00 15.41 ? 132  SER A CB    1 
ATOM   998  O  OG    . SER A  1 157 ? 5.224   -8.456  112.963 1.00 18.20 ? 132  SER A OG    1 
ATOM   999  N  N     . PHE A  1 158 ? 7.742   -5.433  110.786 1.00 18.14 ? 133  PHE A N     1 
ATOM   1000 C  CA    . PHE A  1 158 ? 8.520   -4.217  110.517 1.00 21.78 ? 133  PHE A CA    1 
ATOM   1001 C  C     . PHE A  1 158 ? 7.824   -3.355  109.469 1.00 19.70 ? 133  PHE A C     1 
ATOM   1002 O  O     . PHE A  1 158 ? 7.759   -2.130  109.609 1.00 20.61 ? 133  PHE A O     1 
ATOM   1003 C  CB    . PHE A  1 158 ? 9.963   -4.568  110.083 1.00 19.28 ? 133  PHE A CB    1 
ATOM   1004 C  CG    . PHE A  1 158 ? 10.930  -4.724  111.250 1.00 23.51 ? 133  PHE A CG    1 
ATOM   1005 C  CD1   . PHE A  1 158 ? 11.560  -3.616  111.805 1.00 24.92 ? 133  PHE A CD1   1 
ATOM   1006 C  CD2   . PHE A  1 158 ? 11.150  -5.966  111.829 1.00 21.38 ? 133  PHE A CD2   1 
ATOM   1007 C  CE1   . PHE A  1 158 ? 12.429  -3.751  112.892 1.00 24.88 ? 133  PHE A CE1   1 
ATOM   1008 C  CE2   . PHE A  1 158 ? 11.999  -6.115  112.913 1.00 20.56 ? 133  PHE A CE2   1 
ATOM   1009 C  CZ    . PHE A  1 158 ? 12.652  -5.011  113.449 1.00 23.48 ? 133  PHE A CZ    1 
ATOM   1010 N  N     . ALA A  1 159 ? 7.280   -3.977  108.413 1.00 19.90 ? 134  ALA A N     1 
ATOM   1011 C  CA    . ALA A  1 159 ? 6.629   -3.196  107.359 1.00 19.41 ? 134  ALA A CA    1 
ATOM   1012 C  C     . ALA A  1 159 ? 5.386   -2.481  107.871 1.00 19.50 ? 134  ALA A C     1 
ATOM   1013 O  O     . ALA A  1 159 ? 5.179   -1.297  107.567 1.00 21.34 ? 134  ALA A O     1 
ATOM   1014 C  CB    . ALA A  1 159 ? 6.260   -4.092  106.166 1.00 22.24 ? 134  ALA A CB    1 
ATOM   1015 N  N     . ILE A  1 160 ? 4.565   -3.176  108.663 1.00 15.10 ? 135  ILE A N     1 
ATOM   1016 C  CA    . ILE A  1 160 ? 3.351   -2.582  109.218 1.00 19.24 ? 135  ILE A CA    1 
ATOM   1017 C  C     . ILE A  1 160 ? 3.700   -1.512  110.253 1.00 20.21 ? 135  ILE A C     1 
ATOM   1018 O  O     . ILE A  1 160 ? 3.131   -0.406  110.263 1.00 17.91 ? 135  ILE A O     1 
ATOM   1019 C  CB    . ILE A  1 160 ? 2.448   -3.683  109.819 1.00 20.22 ? 135  ILE A CB    1 
ATOM   1020 C  CG1   . ILE A  1 160 ? 1.810   -4.512  108.711 1.00 26.63 ? 135  ILE A CG1   1 
ATOM   1021 C  CG2   . ILE A  1 160 ? 1.320   -3.089  110.698 1.00 19.75 ? 135  ILE A CG2   1 
ATOM   1022 C  CD1   . ILE A  1 160 ? 1.179   -5.818  109.205 1.00 31.15 ? 135  ILE A CD1   1 
ATOM   1023 N  N     . GLY A  1 161 ? 4.580   -1.853  111.194 1.00 18.73 ? 136  GLY A N     1 
ATOM   1024 C  CA    . GLY A  1 161 ? 4.857   -0.926  112.280 1.00 15.69 ? 136  GLY A CA    1 
ATOM   1025 C  C     . GLY A  1 161 ? 5.646   0.290   111.861 1.00 19.44 ? 136  GLY A C     1 
ATOM   1026 O  O     . GLY A  1 161 ? 5.501   1.352   112.464 1.00 17.09 ? 136  GLY A O     1 
ATOM   1027 N  N     . LEU A  1 162 ? 6.487   0.168   110.824 1.00 15.76 ? 137  LEU A N     1 
ATOM   1028 C  CA    . LEU A  1 162 ? 7.255   1.317   110.358 1.00 18.49 ? 137  LEU A CA    1 
ATOM   1029 C  C     . LEU A  1 162 ? 6.654   1.962   109.119 1.00 18.00 ? 137  LEU A C     1 
ATOM   1030 O  O     . LEU A  1 162 ? 7.318   2.781   108.487 1.00 17.71 ? 137  LEU A O     1 
ATOM   1031 C  CB    . LEU A  1 162 ? 8.713   0.918   110.086 1.00 15.51 ? 137  LEU A CB    1 
ATOM   1032 C  CG    . LEU A  1 162 ? 9.442   0.328   111.305 1.00 19.17 ? 137  LEU A CG    1 
ATOM   1033 C  CD1   . LEU A  1 162 ? 10.899  -0.008  110.988 1.00 22.52 ? 137  LEU A CD1   1 
ATOM   1034 C  CD2   . LEU A  1 162 ? 9.299   1.252   112.538 1.00 18.91 ? 137  LEU A CD2   1 
ATOM   1035 N  N     . THR A  1 163 ? 5.428   1.598   108.750 1.00 17.18 ? 138  THR A N     1 
ATOM   1036 C  CA    . THR A  1 163 ? 4.749   2.277   107.644 1.00 20.21 ? 138  THR A CA    1 
ATOM   1037 C  C     . THR A  1 163 ? 4.782   3.804   107.741 1.00 16.79 ? 138  THR A C     1 
ATOM   1038 O  O     . THR A  1 163 ? 5.014   4.444   106.704 1.00 18.70 ? 138  THR A O     1 
ATOM   1039 C  CB    . THR A  1 163 ? 3.289   1.755   107.554 1.00 21.84 ? 138  THR A CB    1 
ATOM   1040 O  OG1   . THR A  1 163 ? 3.268   0.530   106.814 1.00 24.34 ? 138  THR A OG1   1 
ATOM   1041 C  CG2   . THR A  1 163 ? 2.317   2.758   106.929 1.00 17.59 ? 138  THR A CG2   1 
ATOM   1042 N  N     . PRO A  1 164 ? 4.657   4.439   108.915 1.00 16.15 ? 139  PRO A N     1 
ATOM   1043 C  CA    . PRO A  1 164 ? 4.824   5.907   108.961 1.00 17.97 ? 139  PRO A CA    1 
ATOM   1044 C  C     . PRO A  1 164 ? 6.159   6.390   108.421 1.00 19.41 ? 139  PRO A C     1 
ATOM   1045 O  O     . PRO A  1 164 ? 6.217   7.504   107.878 1.00 18.02 ? 139  PRO A O     1 
ATOM   1046 C  CB    . PRO A  1 164 ? 4.680   6.230   110.462 1.00 15.38 ? 139  PRO A CB    1 
ATOM   1047 C  CG    . PRO A  1 164 ? 3.733   5.135   110.951 1.00 17.39 ? 139  PRO A CG    1 
ATOM   1048 C  CD    . PRO A  1 164 ? 4.246   3.909   110.233 1.00 18.11 ? 139  PRO A CD    1 
ATOM   1049 N  N     . MET A  1 165 ? 7.231   5.586   108.523 1.00 18.63 ? 140  MET A N     1 
ATOM   1050 C  CA    A MET A  1 165 ? 8.534   5.992   107.981 0.63 20.80 ? 140  MET A CA    1 
ATOM   1051 C  CA    B MET A  1 165 ? 8.508   6.031   107.981 0.37 20.80 ? 140  MET A CA    1 
ATOM   1052 C  C     . MET A  1 165 ? 8.536   6.015   106.466 1.00 24.26 ? 140  MET A C     1 
ATOM   1053 O  O     . MET A  1 165 ? 9.432   6.620   105.879 1.00 21.74 ? 140  MET A O     1 
ATOM   1054 C  CB    A MET A  1 165 ? 9.650   5.051   108.470 0.63 20.02 ? 140  MET A CB    1 
ATOM   1055 C  CB    B MET A  1 165 ? 9.610   5.155   108.528 0.37 20.17 ? 140  MET A CB    1 
ATOM   1056 C  CG    A MET A  1 165 ? 9.705   4.898   109.996 0.63 26.50 ? 140  MET A CG    1 
ATOM   1057 C  CG    B MET A  1 165 ? 9.370   4.949   109.985 0.37 25.65 ? 140  MET A CG    1 
ATOM   1058 S  SD    A MET A  1 165 ? 11.314  4.349   110.622 0.63 33.85 ? 140  MET A SD    1 
ATOM   1059 S  SD    B MET A  1 165 ? 10.825  5.370   110.867 0.37 31.90 ? 140  MET A SD    1 
ATOM   1060 C  CE    A MET A  1 165 ? 12.376  5.796   110.298 0.63 23.80 ? 140  MET A CE    1 
ATOM   1061 C  CE    B MET A  1 165 ? 11.558  3.733   110.764 0.37 27.00 ? 140  MET A CE    1 
ATOM   1062 N  N     . LEU A  1 166 ? 7.579   5.333   105.827 1.00 21.72 ? 141  LEU A N     1 
ATOM   1063 C  CA    . LEU A  1 166 ? 7.484   5.381   104.374 1.00 20.71 ? 141  LEU A CA    1 
ATOM   1064 C  C     . LEU A  1 166 ? 6.755   6.624   103.895 1.00 25.17 ? 141  LEU A C     1 
ATOM   1065 O  O     . LEU A  1 166 ? 6.639   6.820   102.679 1.00 26.90 ? 141  LEU A O     1 
ATOM   1066 C  CB    . LEU A  1 166 ? 6.793   4.123   103.825 1.00 21.80 ? 141  LEU A CB    1 
ATOM   1067 C  CG    . LEU A  1 166 ? 7.363   2.756   104.215 1.00 30.43 ? 141  LEU A CG    1 
ATOM   1068 C  CD1   . LEU A  1 166 ? 6.821   1.673   103.288 1.00 29.97 ? 141  LEU A CD1   1 
ATOM   1069 C  CD2   . LEU A  1 166 ? 8.846   2.742   104.203 1.00 28.39 ? 141  LEU A CD2   1 
ATOM   1070 N  N     . GLY A  1 167 ? 6.291   7.485   104.808 1.00 19.51 ? 142  GLY A N     1 
ATOM   1071 C  CA    . GLY A  1 167 ? 5.757   8.764   104.394 1.00 21.13 ? 142  GLY A CA    1 
ATOM   1072 C  C     . GLY A  1 167 ? 4.415   9.122   105.006 1.00 22.05 ? 142  GLY A C     1 
ATOM   1073 O  O     . GLY A  1 167 ? 3.955   10.262  104.893 1.00 23.44 ? 142  GLY A O     1 
ATOM   1074 N  N     . TRP A  1 168 ? 3.769   8.169   105.667 1.00 20.97 ? 143  TRP A N     1 
ATOM   1075 C  CA    . TRP A  1 168 ? 2.497   8.436   106.338 1.00 15.21 ? 143  TRP A CA    1 
ATOM   1076 C  C     . TRP A  1 168 ? 2.836   8.965   107.723 1.00 16.50 ? 143  TRP A C     1 
ATOM   1077 O  O     . TRP A  1 168 ? 2.741   8.277   108.734 1.00 14.80 ? 143  TRP A O     1 
ATOM   1078 C  CB    . TRP A  1 168 ? 1.631   7.183   106.378 1.00 15.51 ? 143  TRP A CB    1 
ATOM   1079 C  CG    . TRP A  1 168 ? 0.192   7.430   106.761 1.00 19.99 ? 143  TRP A CG    1 
ATOM   1080 C  CD1   . TRP A  1 168 ? -0.383  8.625   107.159 1.00 21.83 ? 143  TRP A CD1   1 
ATOM   1081 C  CD2   . TRP A  1 168 ? -0.841  6.449   106.822 1.00 20.09 ? 143  TRP A CD2   1 
ATOM   1082 N  NE1   . TRP A  1 168 ? -1.700  8.429   107.456 1.00 19.37 ? 143  TRP A NE1   1 
ATOM   1083 C  CE2   . TRP A  1 168 ? -2.013  7.103   107.262 1.00 19.79 ? 143  TRP A CE2   1 
ATOM   1084 C  CE3   . TRP A  1 168 ? -0.888  5.076   106.547 1.00 17.87 ? 143  TRP A CE3   1 
ATOM   1085 C  CZ2   . TRP A  1 168 ? -3.223  6.429   107.424 1.00 19.75 ? 143  TRP A CZ2   1 
ATOM   1086 C  CZ3   . TRP A  1 168 ? -2.100  4.412   106.690 1.00 17.65 ? 143  TRP A CZ3   1 
ATOM   1087 C  CH2   . TRP A  1 168 ? -3.242  5.079   107.136 1.00 16.25 ? 143  TRP A CH2   1 
ATOM   1088 N  N     . ASN A  1 169 ? 3.227   10.227  107.765 1.00 16.07 ? 144  ASN A N     1 
ATOM   1089 C  CA    . ASN A  1 169 ? 3.724   10.813  108.999 1.00 21.68 ? 144  ASN A CA    1 
ATOM   1090 C  C     . ASN A  1 169 ? 3.459   12.308  108.965 1.00 19.77 ? 144  ASN A C     1 
ATOM   1091 O  O     . ASN A  1 169 ? 3.071   12.868  107.934 1.00 20.39 ? 144  ASN A O     1 
ATOM   1092 C  CB    . ASN A  1 169 ? 5.218   10.492  109.201 1.00 16.34 ? 144  ASN A CB    1 
ATOM   1093 C  CG    . ASN A  1 169 ? 6.101   11.075  108.095 1.00 18.95 ? 144  ASN A CG    1 
ATOM   1094 O  OD1   . ASN A  1 169 ? 6.157   12.282  107.889 1.00 22.01 ? 144  ASN A OD1   1 
ATOM   1095 N  ND2   . ASN A  1 169 ? 6.805   10.210  107.397 1.00 18.92 ? 144  ASN A ND2   1 
ATOM   1096 N  N     . ASN A  1 170 ? 3.695   12.969  110.102 1.00 22.52 ? 145  ASN A N     1 
ATOM   1097 C  CA    . ASN A  1 170 ? 3.489   14.406  110.172 1.00 21.00 ? 145  ASN A CA    1 
ATOM   1098 C  C     . ASN A  1 170 ? 4.790   15.193  110.057 1.00 24.58 ? 145  ASN A C     1 
ATOM   1099 O  O     . ASN A  1 170 ? 4.808   16.363  110.431 1.00 27.98 ? 145  ASN A O     1 
ATOM   1100 C  CB    . ASN A  1 170 ? 2.831   14.807  111.497 1.00 21.98 ? 145  ASN A CB    1 
ATOM   1101 C  CG    . ASN A  1 170 ? 1.455   14.182  111.713 1.00 26.58 ? 145  ASN A CG    1 
ATOM   1102 O  OD1   . ASN A  1 170 ? 0.703   13.956  110.780 1.00 32.08 ? 145  ASN A OD1   1 
ATOM   1103 N  ND2   . ASN A  1 170 ? 1.119   13.942  112.969 1.00 26.33 ? 145  ASN A ND2   1 
ATOM   1104 N  N     . CYS A  1 171 ? 5.851   14.608  109.498 1.00 24.68 ? 146  CYS A N     1 
ATOM   1105 C  CA    . CYS A  1 171 ? 7.122   15.320  109.422 1.00 28.48 ? 146  CYS A CA    1 
ATOM   1106 C  C     . CYS A  1 171 ? 7.054   16.466  108.421 1.00 33.40 ? 146  CYS A C     1 
ATOM   1107 O  O     . CYS A  1 171 ? 7.791   17.443  108.562 1.00 33.61 ? 146  CYS A O     1 
ATOM   1108 C  CB    . CYS A  1 171 ? 8.253   14.354  109.076 1.00 29.12 ? 146  CYS A CB    1 
ATOM   1109 S  SG    . CYS A  1 171 ? 8.590   13.165  110.459 1.00 33.68 ? 146  CYS A SG    1 
ATOM   1110 N  N     . GLY A  1 172 ? 6.158   16.374  107.438 1.00 31.93 ? 147  GLY A N     1 
ATOM   1111 C  CA    . GLY A  1 172 ? 5.939   17.456  106.496 1.00 25.18 ? 147  GLY A CA    1 
ATOM   1112 C  C     . GLY A  1 172 ? 5.307   18.680  107.126 1.00 30.63 ? 147  GLY A C     1 
ATOM   1113 O  O     . GLY A  1 172 ? 5.333   19.753  106.525 1.00 38.68 ? 147  GLY A O     1 
ATOM   1114 N  N     . GLN A  1 173 ? 4.675   18.536  108.288 1.00 30.76 ? 148  GLN A N     1 
ATOM   1115 C  CA    . GLN A  1 173 ? 4.006   19.656  108.951 1.00 30.50 ? 148  GLN A CA    1 
ATOM   1116 C  C     . GLN A  1 173 ? 4.505   19.803  110.387 1.00 34.48 ? 148  GLN A C     1 
ATOM   1117 O  O     . GLN A  1 173 ? 3.746   19.616  111.343 1.00 32.69 ? 148  GLN A O     1 
ATOM   1118 C  CB    . GLN A  1 173 ? 2.493   19.460  108.912 1.00 37.50 ? 148  GLN A CB    1 
ATOM   1119 N  N     . PRO A  1 174 ? 5.792   20.117  110.580 1.00 35.64 ? 149  PRO A N     1 
ATOM   1120 C  CA    . PRO A  1 174 ? 6.318   20.187  111.950 1.00 30.90 ? 149  PRO A CA    1 
ATOM   1121 C  C     . PRO A  1 174 ? 5.657   21.307  112.741 1.00 30.73 ? 149  PRO A C     1 
ATOM   1122 O  O     . PRO A  1 174 ? 5.283   22.345  112.193 1.00 31.67 ? 149  PRO A O     1 
ATOM   1123 C  CB    . PRO A  1 174 ? 7.812   20.470  111.735 1.00 32.48 ? 149  PRO A CB    1 
ATOM   1124 C  CG    . PRO A  1 174 ? 7.883   21.158  110.438 1.00 35.73 ? 149  PRO A CG    1 
ATOM   1125 C  CD    . PRO A  1 174 ? 6.826   20.471  109.587 1.00 34.15 ? 149  PRO A CD    1 
ATOM   1126 N  N     . LYS A  1 175 ? 5.522   21.101  114.047 1.00 26.13 ? 150  LYS A N     1 
ATOM   1127 C  CA    . LYS A  1 175 ? 5.109   22.188  114.934 1.00 36.62 ? 150  LYS A CA    1 
ATOM   1128 C  C     . LYS A  1 175 ? 6.304   23.089  115.228 1.00 34.10 ? 150  LYS A C     1 
ATOM   1129 O  O     . LYS A  1 175 ? 6.998   22.923  116.231 1.00 27.12 ? 150  LYS A O     1 
ATOM   1130 C  CB    . LYS A  1 175 ? 4.498   21.637  116.213 1.00 34.16 ? 150  LYS A CB    1 
ATOM   1131 C  CG    . LYS A  1 175 ? 3.133   20.980  116.058 1.00 39.28 ? 150  LYS A CG    1 
ATOM   1132 C  CD    . LYS A  1 175 ? 2.692   20.413  117.384 1.00 37.61 ? 150  LYS A CD    1 
ATOM   1133 C  CE    . LYS A  1 175 ? 1.472   19.557  117.241 1.00 49.84 ? 150  LYS A CE    1 
ATOM   1134 N  NZ    . LYS A  1 175 ? 0.408   20.359  116.611 1.00 58.74 ? 150  LYS A NZ    1 
ATOM   1135 N  N     . GLU A  1 176 ? 6.479   24.121  114.405 1.00 41.06 ? 151  GLU A N     1 
ATOM   1136 C  CA    . GLU A  1 176 ? 7.658   24.985  114.515 1.00 45.32 ? 151  GLU A CA    1 
ATOM   1137 C  C     . GLU A  1 176 ? 7.636   25.835  115.777 1.00 36.73 ? 151  GLU A C     1 
ATOM   1138 O  O     . GLU A  1 176 ? 8.699   26.132  116.332 1.00 42.64 ? 151  GLU A O     1 
ATOM   1139 C  CB    . GLU A  1 176 ? 7.838   25.827  113.253 1.00 45.59 ? 151  GLU A CB    1 
ATOM   1140 C  CG    . GLU A  1 176 ? 7.819   24.946  112.020 1.00 49.70 ? 151  GLU A CG    1 
ATOM   1141 C  CD    . GLU A  1 176 ? 9.214   24.532  111.592 1.00 54.51 ? 151  GLU A CD    1 
ATOM   1142 O  OE1   . GLU A  1 176 ? 9.979   24.043  112.455 1.00 54.42 ? 151  GLU A OE1   1 
ATOM   1143 O  OE2   . GLU A  1 176 ? 9.542   24.672  110.390 1.00 71.25 ? 151  GLU A OE2   1 
ATOM   1144 N  N     . GLY A  1 177 ? 6.463   26.255  116.243 1.00 37.95 ? 152  GLY A N     1 
ATOM   1145 C  CA    . GLY A  1 177 ? 6.443   27.053  117.459 1.00 40.99 ? 152  GLY A CA    1 
ATOM   1146 C  C     . GLY A  1 177 ? 6.912   26.252  118.661 1.00 42.23 ? 152  GLY A C     1 
ATOM   1147 O  O     . GLY A  1 177 ? 7.638   26.766  119.523 1.00 39.23 ? 152  GLY A O     1 
ATOM   1148 N  N     . LYS A  1 178 ? 6.529   24.976  118.727 1.00 36.77 ? 153  LYS A N     1 
ATOM   1149 C  CA    . LYS A  1 178 ? 7.015   24.127  119.806 1.00 34.94 ? 153  LYS A CA    1 
ATOM   1150 C  C     . LYS A  1 178 ? 8.511   23.850  119.673 1.00 33.45 ? 153  LYS A C     1 
ATOM   1151 O  O     . LYS A  1 178 ? 9.232   23.808  120.680 1.00 35.38 ? 153  LYS A O     1 
ATOM   1152 C  CB    . LYS A  1 178 ? 6.236   22.807  119.845 1.00 37.30 ? 153  LYS A CB    1 
ATOM   1153 C  CG    . LYS A  1 178 ? 6.546   22.013  121.070 1.00 34.29 ? 153  LYS A CG    1 
ATOM   1154 C  CD    . LYS A  1 178 ? 5.675   20.777  121.266 1.00 44.33 ? 153  LYS A CD    1 
ATOM   1155 C  CE    . LYS A  1 178 ? 4.402   20.815  120.470 1.00 41.92 ? 153  LYS A CE    1 
ATOM   1156 N  NZ    . LYS A  1 178 ? 3.468   19.729  120.919 1.00 44.53 ? 153  LYS A NZ    1 
ATOM   1157 N  N     . ALA A  1 179 ? 8.983   23.619  118.448 1.00 28.19 ? 154  ALA A N     1 
ATOM   1158 C  CA    . ALA A  1 179 ? 10.410  23.410  118.238 1.00 31.35 ? 154  ALA A CA    1 
ATOM   1159 C  C     . ALA A  1 179 ? 11.218  24.652  118.625 1.00 39.40 ? 154  ALA A C     1 
ATOM   1160 O  O     . ALA A  1 179 ? 12.243  24.549  119.311 1.00 37.33 ? 154  ALA A O     1 
ATOM   1161 C  CB    . ALA A  1 179 ? 10.690  23.033  116.780 1.00 26.94 ? 154  ALA A CB    1 
ATOM   1162 N  N     . HIS A  1 180 ? 10.755  25.839  118.223 1.00 35.48 ? 155  HIS A N     1 
ATOM   1163 C  CA    . HIS A  1 180 ? 11.494  27.053  118.560 1.00 41.38 ? 155  HIS A CA    1 
ATOM   1164 C  C     . HIS A  1 180 ? 11.481  27.309  120.057 1.00 41.74 ? 155  HIS A C     1 
ATOM   1165 O  O     . HIS A  1 180 ? 12.504  27.697  120.632 1.00 44.11 ? 155  HIS A O     1 
ATOM   1166 C  CB    . HIS A  1 180 ? 10.883  28.246  117.821 1.00 46.77 ? 155  HIS A CB    1 
ATOM   1167 C  CG    . HIS A  1 180 ? 11.052  28.187  116.338 1.00 47.01 ? 155  HIS A CG    1 
ATOM   1168 N  ND1   . HIS A  1 180 ? 12.248  27.863  115.735 1.00 54.94 ? 155  HIS A ND1   1 
ATOM   1169 C  CD2   . HIS A  1 180 ? 10.170  28.406  115.334 1.00 47.25 ? 155  HIS A CD2   1 
ATOM   1170 C  CE1   . HIS A  1 180 ? 12.093  27.878  114.422 1.00 55.25 ? 155  HIS A CE1   1 
ATOM   1171 N  NE2   . HIS A  1 180 ? 10.840  28.200  114.153 1.00 57.02 ? 155  HIS A NE2   1 
ATOM   1172 N  N     . SER A  1 181 ? 10.366  27.013  120.724 1.00 32.80 ? 156  SER A N     1 
ATOM   1173 C  CA    . SER A  1 181 ? 10.309  27.295  122.153 1.00 37.52 ? 156  SER A CA    1 
ATOM   1174 C  C     . SER A  1 181 ? 11.277  26.407  122.925 1.00 46.06 ? 156  SER A C     1 
ATOM   1175 O  O     . SER A  1 181 ? 11.797  26.813  123.971 1.00 48.77 ? 156  SER A O     1 
ATOM   1176 C  CB    . SER A  1 181 ? 8.879   27.138  122.675 1.00 42.75 ? 156  SER A CB    1 
ATOM   1177 O  OG    . SER A  1 181 ? 8.447   25.785  122.574 1.00 53.74 ? 156  SER A OG    1 
ATOM   1178 N  N     . GLN A  1 182 ? 11.548  25.211  122.412 1.00 41.17 ? 157  GLN A N     1 
ATOM   1179 C  CA    . GLN A  1 182 ? 12.464  24.274  123.032 1.00 36.02 ? 157  GLN A CA    1 
ATOM   1180 C  C     . GLN A  1 182 ? 13.879  24.422  122.513 1.00 38.09 ? 157  GLN A C     1 
ATOM   1181 O  O     . GLN A  1 182 ? 14.735  23.596  122.831 1.00 43.91 ? 157  GLN A O     1 
ATOM   1182 C  CB    . GLN A  1 182 ? 11.984  22.846  122.793 1.00 36.83 ? 157  GLN A CB    1 
ATOM   1183 C  CG    . GLN A  1 182 ? 10.688  22.521  123.461 1.00 46.47 ? 157  GLN A CG    1 
ATOM   1184 C  CD    . GLN A  1 182 ? 10.498  21.038  123.474 1.00 57.60 ? 157  GLN A CD    1 
ATOM   1185 O  OE1   . GLN A  1 182 ? 11.408  20.308  123.075 1.00 58.90 ? 157  GLN A OE1   1 
ATOM   1186 N  NE2   . GLN A  1 182 ? 9.331   20.568  123.927 1.00 61.00 ? 157  GLN A NE2   1 
ATOM   1187 N  N     . GLY A  1 183 ? 14.137  25.437  121.703 1.00 41.51 ? 158  GLY A N     1 
ATOM   1188 C  CA    . GLY A  1 183 ? 15.479  25.647  121.228 1.00 38.71 ? 158  GLY A CA    1 
ATOM   1189 C  C     . GLY A  1 183 ? 15.948  24.615  120.251 1.00 39.65 ? 158  GLY A C     1 
ATOM   1190 O  O     . GLY A  1 183 ? 17.151  24.464  120.062 1.00 46.55 ? 158  GLY A O     1 
ATOM   1191 N  N     . CYS A  1 184 ? 15.032  23.919  119.587 1.00 38.24 ? 159  CYS A N     1 
ATOM   1192 C  CA    . CYS A  1 184 ? 15.446  22.900  118.636 1.00 35.17 ? 159  CYS A CA    1 
ATOM   1193 C  C     . CYS A  1 184 ? 16.168  23.545  117.464 1.00 42.48 ? 159  CYS A C     1 
ATOM   1194 O  O     . CYS A  1 184 ? 15.929  24.702  117.119 1.00 45.27 ? 159  CYS A O     1 
ATOM   1195 C  CB    . CYS A  1 184 ? 14.249  22.095  118.121 1.00 36.04 ? 159  CYS A CB    1 
ATOM   1196 S  SG    . CYS A  1 184 ? 13.471  21.104  119.405 1.00 36.32 ? 159  CYS A SG    1 
ATOM   1197 N  N     . GLY A  1 185 ? 17.055  22.778  116.852 1.00 38.75 ? 160  GLY A N     1 
ATOM   1198 C  CA    . GLY A  1 185 ? 17.815  23.249  115.726 1.00 44.34 ? 160  GLY A CA    1 
ATOM   1199 C  C     . GLY A  1 185 ? 17.005  23.169  114.459 1.00 49.47 ? 160  GLY A C     1 
ATOM   1200 O  O     . GLY A  1 185 ? 15.855  22.727  114.433 1.00 49.59 ? 160  GLY A O     1 
ATOM   1201 N  N     . GLU A  1 186 ? 17.637  23.580  113.368 1.00 52.87 ? 161  GLU A N     1 
ATOM   1202 C  CA    . GLU A  1 186 ? 16.938  23.592  112.096 1.00 52.01 ? 161  GLU A CA    1 
ATOM   1203 C  C     . GLU A  1 186 ? 16.701  22.165  111.630 1.00 46.10 ? 161  GLU A C     1 
ATOM   1204 O  O     . GLU A  1 186 ? 17.575  21.303  111.746 1.00 51.77 ? 161  GLU A O     1 
ATOM   1205 C  CB    . GLU A  1 186 ? 17.763  24.363  111.064 1.00 62.92 ? 161  GLU A CB    1 
ATOM   1206 C  CG    . GLU A  1 186 ? 17.538  25.884  111.117 1.00 70.22 ? 161  GLU A CG    1 
ATOM   1207 C  CD    . GLU A  1 186 ? 16.200  26.325  110.558 1.00 87.65 ? 161  GLU A CD    1 
ATOM   1208 O  OE1   . GLU A  1 186 ? 16.017  26.243  109.325 1.00 95.99 ? 161  GLU A OE1   1 
ATOM   1209 O  OE2   . GLU A  1 186 ? 15.328  26.746  111.352 1.00 80.02 ? 161  GLU A OE2   1 
ATOM   1210 N  N     . GLY A  1 187 ? 15.490  21.906  111.123 1.00 52.42 ? 162  GLY A N     1 
ATOM   1211 C  CA    . GLY A  1 187 ? 15.123  20.554  110.763 1.00 47.70 ? 162  GLY A CA    1 
ATOM   1212 C  C     . GLY A  1 187 ? 14.753  19.640  111.911 1.00 45.78 ? 162  GLY A C     1 
ATOM   1213 O  O     . GLY A  1 187 ? 14.531  18.451  111.679 1.00 44.94 ? 162  GLY A O     1 
ATOM   1214 N  N     . GLN A  1 188 ? 14.682  20.136  113.135 1.00 41.84 ? 163  GLN A N     1 
ATOM   1215 C  CA    . GLN A  1 188 ? 14.334  19.316  114.289 1.00 38.86 ? 163  GLN A CA    1 
ATOM   1216 C  C     . GLN A  1 188 ? 12.934  19.645  114.796 1.00 37.01 ? 163  GLN A C     1 
ATOM   1217 O  O     . GLN A  1 188 ? 12.377  20.709  114.510 1.00 35.18 ? 163  GLN A O     1 
ATOM   1218 C  CB    . GLN A  1 188 ? 15.362  19.497  115.412 1.00 31.08 ? 163  GLN A CB    1 
ATOM   1219 C  CG    . GLN A  1 188 ? 16.730  18.937  115.085 1.00 35.94 ? 163  GLN A CG    1 
ATOM   1220 C  CD    . GLN A  1 188 ? 17.638  18.965  116.290 1.00 35.63 ? 163  GLN A CD    1 
ATOM   1221 O  OE1   . GLN A  1 188 ? 17.511  19.840  117.146 1.00 37.00 ? 163  GLN A OE1   1 
ATOM   1222 N  NE2   . GLN A  1 188 ? 18.561  18.015  116.363 1.00 37.58 ? 163  GLN A NE2   1 
ATOM   1223 N  N     . VAL A  1 189 ? 12.328  18.669  115.473 1.00 26.47 ? 164  VAL A N     1 
ATOM   1224 C  CA    . VAL A  1 189 ? 11.037  18.856  116.120 1.00 26.07 ? 164  VAL A CA    1 
ATOM   1225 C  C     . VAL A  1 189 ? 11.185  18.448  117.580 1.00 25.32 ? 164  VAL A C     1 
ATOM   1226 O  O     . VAL A  1 189 ? 12.117  17.734  117.957 1.00 23.78 ? 164  VAL A O     1 
ATOM   1227 C  CB    . VAL A  1 189 ? 9.928   17.995  115.441 1.00 28.81 ? 164  VAL A CB    1 
ATOM   1228 C  CG1   . VAL A  1 189 ? 9.753   18.387  113.990 1.00 30.70 ? 164  VAL A CG1   1 
ATOM   1229 C  CG2   . VAL A  1 189 ? 10.257  16.504  115.547 1.00 25.71 ? 164  VAL A CG2   1 
ATOM   1230 N  N     . ALA A  1 190 ? 10.268  18.933  118.410 1.00 20.84 ? 165  ALA A N     1 
ATOM   1231 C  CA    . ALA A  1 190 ? 10.090  18.332  119.726 1.00 28.65 ? 165  ALA A CA    1 
ATOM   1232 C  C     . ALA A  1 190 ? 9.550   16.923  119.506 1.00 28.28 ? 165  ALA A C     1 
ATOM   1233 O  O     . ALA A  1 190 ? 8.506   16.748  118.860 1.00 23.01 ? 165  ALA A O     1 
ATOM   1234 C  CB    . ALA A  1 190 ? 9.124   19.147  120.578 1.00 28.45 ? 165  ALA A CB    1 
ATOM   1235 N  N     . CYS A  1 191 ? 10.288  15.922  119.971 1.00 25.69 ? 166  CYS A N     1 
ATOM   1236 C  CA    . CYS A  1 191 ? 9.982   14.524  119.665 1.00 23.74 ? 166  CYS A CA    1 
ATOM   1237 C  C     . CYS A  1 191 ? 8.891   14.049  120.605 1.00 25.28 ? 166  CYS A C     1 
ATOM   1238 O  O     . CYS A  1 191 ? 9.156   13.700  121.765 1.00 29.73 ? 166  CYS A O     1 
ATOM   1239 C  CB    . CYS A  1 191 ? 11.232  13.659  119.775 1.00 26.71 ? 166  CYS A CB    1 
ATOM   1240 S  SG    . CYS A  1 191 ? 10.878  11.957  119.303 1.00 34.40 ? 166  CYS A SG    1 
ATOM   1241 N  N     . LEU A  1 192 ? 7.655   14.074  120.101 1.00 24.09 ? 167  LEU A N     1 
ATOM   1242 C  CA    . LEU A  1 192 ? 6.456   13.665  120.817 1.00 25.60 ? 167  LEU A CA    1 
ATOM   1243 C  C     . LEU A  1 192 ? 5.625   12.727  119.958 1.00 22.59 ? 167  LEU A C     1 
ATOM   1244 O  O     . LEU A  1 192 ? 5.408   13.019  118.780 1.00 20.57 ? 167  LEU A O     1 
ATOM   1245 C  CB    . LEU A  1 192 ? 5.617   14.889  121.184 1.00 21.34 ? 167  LEU A CB    1 
ATOM   1246 C  CG    . LEU A  1 192 ? 6.286   15.811  122.210 1.00 29.86 ? 167  LEU A CG    1 
ATOM   1247 C  CD1   . LEU A  1 192 ? 5.488   17.092  122.342 1.00 29.66 ? 167  LEU A CD1   1 
ATOM   1248 C  CD2   . LEU A  1 192 ? 6.409   15.086  123.520 1.00 25.55 ? 167  LEU A CD2   1 
ATOM   1249 N  N     . PHE A  1 193 ? 5.142   11.625  120.553 1.00 18.72 ? 168  PHE A N     1 
ATOM   1250 C  CA    . PHE A  1 193 ? 4.450   10.585  119.773 1.00 18.53 ? 168  PHE A CA    1 
ATOM   1251 C  C     . PHE A  1 193 ? 3.343   11.186  118.906 1.00 19.46 ? 168  PHE A C     1 
ATOM   1252 O  O     . PHE A  1 193 ? 3.264   10.926  117.692 1.00 19.82 ? 168  PHE A O     1 
ATOM   1253 C  CB    . PHE A  1 193 ? 3.875   9.501   120.689 1.00 20.86 ? 168  PHE A CB    1 
ATOM   1254 C  CG    . PHE A  1 193 ? 3.288   8.306   119.927 1.00 15.32 ? 168  PHE A CG    1 
ATOM   1255 C  CD1   . PHE A  1 193 ? 2.006   8.372   119.387 1.00 19.20 ? 168  PHE A CD1   1 
ATOM   1256 C  CD2   . PHE A  1 193 ? 4.042   7.162   119.723 1.00 16.18 ? 168  PHE A CD2   1 
ATOM   1257 C  CE1   . PHE A  1 193 ? 1.450   7.285   118.701 1.00 19.47 ? 168  PHE A CE1   1 
ATOM   1258 C  CE2   . PHE A  1 193 ? 3.523   6.082   119.007 1.00 22.68 ? 168  PHE A CE2   1 
ATOM   1259 C  CZ    . PHE A  1 193 ? 2.218   6.145   118.497 1.00 17.93 ? 168  PHE A CZ    1 
ATOM   1260 N  N     . GLU A  1 194 ? 2.441   11.941  119.517 1.00 18.93 ? 169  GLU A N     1 
ATOM   1261 C  CA    . GLU A  1 194 ? 1.293   12.411  118.747 1.00 21.73 ? 169  GLU A CA    1 
ATOM   1262 C  C     . GLU A  1 194 ? 1.643   13.560  117.825 1.00 23.23 ? 169  GLU A C     1 
ATOM   1263 O  O     . GLU A  1 194 ? 0.816   13.926  116.988 1.00 25.04 ? 169  GLU A O     1 
ATOM   1264 C  CB    . GLU A  1 194 ? 0.141   12.849  119.659 1.00 23.99 ? 169  GLU A CB    1 
ATOM   1265 C  CG    . GLU A  1 194 ? -0.471  11.682  120.453 1.00 21.32 ? 169  GLU A CG    1 
ATOM   1266 C  CD    . GLU A  1 194 ? -1.752  12.038  121.196 1.00 25.45 ? 169  GLU A CD    1 
ATOM   1267 O  OE1   . GLU A  1 194 ? -2.407  13.039  120.851 1.00 27.45 ? 169  GLU A OE1   1 
ATOM   1268 O  OE2   . GLU A  1 194 ? -2.104  11.316  122.154 1.00 27.73 ? 169  GLU A OE2   1 
ATOM   1269 N  N     . ASP A  1 195 ? 2.837   14.133  117.942 1.00 20.33 ? 170  ASP A N     1 
ATOM   1270 C  CA    . ASP A  1 195 ? 3.238   15.148  116.977 1.00 21.68 ? 170  ASP A CA    1 
ATOM   1271 C  C     . ASP A  1 195 ? 3.772   14.526  115.689 1.00 23.65 ? 170  ASP A C     1 
ATOM   1272 O  O     . ASP A  1 195 ? 3.649   15.145  114.632 1.00 23.98 ? 170  ASP A O     1 
ATOM   1273 C  CB    . ASP A  1 195 ? 4.282   16.115  117.570 1.00 22.00 ? 170  ASP A CB    1 
ATOM   1274 C  CG    . ASP A  1 195 ? 3.693   17.050  118.662 1.00 32.97 ? 170  ASP A CG    1 
ATOM   1275 O  OD1   . ASP A  1 195 ? 2.472   17.001  118.884 1.00 33.88 ? 170  ASP A OD1   1 
ATOM   1276 O  OD2   . ASP A  1 195 ? 4.441   17.867  119.261 1.00 31.32 ? 170  ASP A OD2   1 
ATOM   1277 N  N     . VAL A  1 196 ? 4.316   13.301  115.722 1.00 15.55 ? 171  VAL A N     1 
ATOM   1278 C  CA    . VAL A  1 196 ? 4.923   12.722  114.531 1.00 18.19 ? 171  VAL A CA    1 
ATOM   1279 C  C     . VAL A  1 196 ? 4.105   11.566  113.921 1.00 19.31 ? 171  VAL A C     1 
ATOM   1280 O  O     . VAL A  1 196 ? 4.131   11.394  112.695 1.00 20.00 ? 171  VAL A O     1 
ATOM   1281 C  CB    . VAL A  1 196 ? 6.381   12.276  114.820 1.00 21.48 ? 171  VAL A CB    1 
ATOM   1282 C  CG1   . VAL A  1 196 ? 7.221   13.464  115.237 1.00 24.81 ? 171  VAL A CG1   1 
ATOM   1283 C  CG2   . VAL A  1 196 ? 6.444   11.221  115.938 1.00 16.47 ? 171  VAL A CG2   1 
ATOM   1284 N  N     . VAL A  1 197 ? 3.379   10.778  114.712 1.00 17.34 ? 172  VAL A N     1 
ATOM   1285 C  CA    . VAL A  1 197 ? 2.599   9.655   114.189 1.00 17.57 ? 172  VAL A CA    1 
ATOM   1286 C  C     . VAL A  1 197 ? 1.177   10.149  113.935 1.00 17.30 ? 172  VAL A C     1 
ATOM   1287 O  O     . VAL A  1 197 ? 0.536   10.632  114.874 1.00 19.75 ? 172  VAL A O     1 
ATOM   1288 C  CB    . VAL A  1 197 ? 2.593   8.460   115.148 1.00 20.75 ? 172  VAL A CB    1 
ATOM   1289 C  CG1   . VAL A  1 197 ? 1.856   7.279   114.499 1.00 15.23 ? 172  VAL A CG1   1 
ATOM   1290 C  CG2   . VAL A  1 197 ? 4.055   8.030   115.491 1.00 16.53 ? 172  VAL A CG2   1 
ATOM   1291 N  N     . PRO A  1 198 ? 0.658   10.052  112.703 1.00 20.78 ? 173  PRO A N     1 
ATOM   1292 C  CA    . PRO A  1 198 ? -0.705  10.557  112.419 1.00 20.87 ? 173  PRO A CA    1 
ATOM   1293 C  C     . PRO A  1 198 ? -1.745  9.710   113.136 1.00 14.90 ? 173  PRO A C     1 
ATOM   1294 O  O     . PRO A  1 198 ? -1.595  8.488   113.226 1.00 15.87 ? 173  PRO A O     1 
ATOM   1295 C  CB    . PRO A  1 198 ? -0.840  10.403  110.896 1.00 22.63 ? 173  PRO A CB    1 
ATOM   1296 C  CG    . PRO A  1 198 ? 0.585   10.268  110.373 1.00 18.92 ? 173  PRO A CG    1 
ATOM   1297 C  CD    . PRO A  1 198 ? 1.318   9.528   111.490 1.00 17.07 ? 173  PRO A CD    1 
ATOM   1298 N  N     . MET A  1 199 ? -2.803  10.348  113.648 1.00 16.16 ? 174  MET A N     1 
ATOM   1299 C  CA    A MET A  1 199 ? -3.833  9.572   114.347 0.62 18.38 ? 174  MET A CA    1 
ATOM   1300 C  CA    B MET A  1 199 ? -3.842  9.590   114.348 0.38 18.46 ? 174  MET A CA    1 
ATOM   1301 C  C     . MET A  1 199 ? -4.664  8.740   113.385 1.00 16.82 ? 174  MET A C     1 
ATOM   1302 O  O     . MET A  1 199 ? -5.181  7.690   113.777 1.00 17.66 ? 174  MET A O     1 
ATOM   1303 C  CB    A MET A  1 199 ? -4.749  10.477  115.166 0.62 19.81 ? 174  MET A CB    1 
ATOM   1304 C  CB    B MET A  1 199 ? -4.756  10.532  115.138 0.38 19.85 ? 174  MET A CB    1 
ATOM   1305 C  CG    A MET A  1 199 ? -5.247  9.852   116.459 0.62 21.58 ? 174  MET A CG    1 
ATOM   1306 C  CG    B MET A  1 199 ? -4.366  10.714  116.606 0.38 20.30 ? 174  MET A CG    1 
ATOM   1307 S  SD    A MET A  1 199 ? -4.004  9.014   117.488 0.62 29.68 ? 174  MET A SD    1 
ATOM   1308 S  SD    B MET A  1 199 ? -4.024  9.137   117.453 0.38 29.54 ? 174  MET A SD    1 
ATOM   1309 C  CE    A MET A  1 199 ? -3.523  10.378  118.566 0.62 25.47 ? 174  MET A CE    1 
ATOM   1310 C  CE    B MET A  1 199 ? -3.233  9.722   118.955 0.38 26.29 ? 174  MET A CE    1 
ATOM   1311 N  N     . ASN A  1 200 ? -4.787  9.158   112.121 1.00 17.11 ? 175  ASN A N     1 
ATOM   1312 C  CA    . ASN A  1 200 ? -5.562  8.325   111.197 1.00 17.21 ? 175  ASN A CA    1 
ATOM   1313 C  C     . ASN A  1 200 ? -4.822  7.019   110.915 1.00 16.23 ? 175  ASN A C     1 
ATOM   1314 O  O     . ASN A  1 200 ? -5.450  5.951   110.829 1.00 18.35 ? 175  ASN A O     1 
ATOM   1315 C  CB    . ASN A  1 200 ? -5.924  9.072   109.889 1.00 17.84 ? 175  ASN A CB    1 
ATOM   1316 C  CG    . ASN A  1 200 ? -4.721  9.752   109.183 1.00 20.09 ? 175  ASN A CG    1 
ATOM   1317 O  OD1   . ASN A  1 200 ? -3.557  9.440   109.423 1.00 23.29 ? 175  ASN A OD1   1 
ATOM   1318 N  ND2   . ASN A  1 200 ? -5.032  10.676  108.274 1.00 25.90 ? 175  ASN A ND2   1 
ATOM   1319 N  N     . TYR A  1 201 ? -3.486  7.065   110.841 1.00 14.97 ? 176  TYR A N     1 
ATOM   1320 C  CA    . TYR A  1 201 ? -2.718  5.817   110.829 1.00 14.86 ? 176  TYR A CA    1 
ATOM   1321 C  C     . TYR A  1 201 ? -2.993  4.986   112.081 1.00 16.81 ? 176  TYR A C     1 
ATOM   1322 O  O     . TYR A  1 201 ? -3.230  3.775   111.998 1.00 16.36 ? 176  TYR A O     1 
ATOM   1323 C  CB    . TYR A  1 201 ? -1.215  6.082   110.678 1.00 20.16 ? 176  TYR A CB    1 
ATOM   1324 C  CG    . TYR A  1 201 ? -0.393  4.833   110.986 1.00 15.88 ? 176  TYR A CG    1 
ATOM   1325 C  CD1   . TYR A  1 201 ? -0.087  3.907   109.988 1.00 14.70 ? 176  TYR A CD1   1 
ATOM   1326 C  CD2   . TYR A  1 201 ? 0.064   4.591   112.267 1.00 15.79 ? 176  TYR A CD2   1 
ATOM   1327 C  CE1   . TYR A  1 201 ? 0.636   2.766   110.272 1.00 19.44 ? 176  TYR A CE1   1 
ATOM   1328 C  CE2   . TYR A  1 201 ? 0.786   3.456   112.563 1.00 15.66 ? 176  TYR A CE2   1 
ATOM   1329 C  CZ    . TYR A  1 201 ? 1.068   2.547   111.574 1.00 21.33 ? 176  TYR A CZ    1 
ATOM   1330 O  OH    . TYR A  1 201 ? 1.803   1.421   111.912 1.00 21.43 ? 176  TYR A OH    1 
ATOM   1331 N  N     . MET A  1 202 ? -2.904  5.609   113.262 1.00 14.62 ? 177  MET A N     1 
ATOM   1332 C  CA    . MET A  1 202 ? -3.028  4.835   114.503 1.00 15.92 ? 177  MET A CA    1 
ATOM   1333 C  C     . MET A  1 202 ? -4.400  4.193   114.655 1.00 15.64 ? 177  MET A C     1 
ATOM   1334 O  O     . MET A  1 202 ? -4.512  3.100   115.230 1.00 16.47 ? 177  MET A O     1 
ATOM   1335 C  CB    . MET A  1 202 ? -2.754  5.697   115.727 1.00 15.78 ? 177  MET A CB    1 
ATOM   1336 C  CG    . MET A  1 202 ? -1.278  5.953   116.080 1.00 19.91 ? 177  MET A CG    1 
ATOM   1337 S  SD    . MET A  1 202 ? -0.302  4.433   116.089 1.00 17.99 ? 177  MET A SD    1 
ATOM   1338 C  CE    . MET A  1 202 ? -1.071  3.537   117.439 1.00 18.79 ? 177  MET A CE    1 
ATOM   1339 N  N     . VAL A  1 203 ? -5.455  4.879   114.199 1.00 15.19 ? 178  VAL A N     1 
ATOM   1340 C  CA    . VAL A  1 203 ? -6.828  4.406   114.384 1.00 16.16 ? 178  VAL A CA    1 
ATOM   1341 C  C     . VAL A  1 203 ? -7.257  3.469   113.260 1.00 13.04 ? 178  VAL A C     1 
ATOM   1342 O  O     . VAL A  1 203 ? -7.656  2.323   113.509 1.00 16.58 ? 178  VAL A O     1 
ATOM   1343 C  CB    . VAL A  1 203 ? -7.801  5.603   114.504 1.00 14.28 ? 178  VAL A CB    1 
ATOM   1344 C  CG1   . VAL A  1 203 ? -9.251  5.115   114.463 1.00 19.26 ? 178  VAL A CG1   1 
ATOM   1345 C  CG2   . VAL A  1 203 ? -7.535  6.373   115.803 1.00 17.93 ? 178  VAL A CG2   1 
ATOM   1346 N  N     . TYR A  1 204 ? -7.153  3.925   112.010 1.00 17.44 ? 179  TYR A N     1 
ATOM   1347 C  CA    . TYR A  1 204 ? -7.698  3.102   110.931 1.00 17.25 ? 179  TYR A CA    1 
ATOM   1348 C  C     . TYR A  1 204 ? -6.759  1.976   110.552 1.00 21.97 ? 179  TYR A C     1 
ATOM   1349 O  O     . TYR A  1 204 ? -7.194  0.839   110.324 1.00 21.30 ? 179  TYR A O     1 
ATOM   1350 C  CB    . TYR A  1 204 ? -7.981  3.933   109.687 1.00 17.39 ? 179  TYR A CB    1 
ATOM   1351 C  CG    . TYR A  1 204 ? -9.104  4.918   109.814 1.00 21.61 ? 179  TYR A CG    1 
ATOM   1352 C  CD1   . TYR A  1 204 ? -10.302 4.567   110.415 1.00 20.85 ? 179  TYR A CD1   1 
ATOM   1353 C  CD2   . TYR A  1 204 ? -8.982  6.199   109.292 1.00 22.99 ? 179  TYR A CD2   1 
ATOM   1354 C  CE1   . TYR A  1 204 ? -11.356 5.485   110.501 1.00 21.51 ? 179  TYR A CE1   1 
ATOM   1355 C  CE2   . TYR A  1 204 ? -10.025 7.111   109.376 1.00 26.73 ? 179  TYR A CE2   1 
ATOM   1356 C  CZ    . TYR A  1 204 ? -11.203 6.740   109.989 1.00 25.48 ? 179  TYR A CZ    1 
ATOM   1357 O  OH    . TYR A  1 204 ? -12.231 7.645   110.065 1.00 30.60 ? 179  TYR A OH    1 
ATOM   1358 N  N     . PHE A  1 205 ? -5.473  2.285   110.433 1.00 18.27 ? 180  PHE A N     1 
ATOM   1359 C  CA    . PHE A  1 205 ? -4.539  1.302   109.911 1.00 22.41 ? 180  PHE A CA    1 
ATOM   1360 C  C     . PHE A  1 205 ? -4.035  0.427   111.038 1.00 20.96 ? 180  PHE A C     1 
ATOM   1361 O  O     . PHE A  1 205 ? -4.168  -0.801  110.992 1.00 21.86 ? 180  PHE A O     1 
ATOM   1362 C  CB    . PHE A  1 205 ? -3.387  2.014   109.185 1.00 19.85 ? 180  PHE A CB    1 
ATOM   1363 C  CG    . PHE A  1 205 ? -2.494  1.090   108.383 1.00 21.14 ? 180  PHE A CG    1 
ATOM   1364 C  CD1   . PHE A  1 205 ? -1.419  0.434   108.980 1.00 18.62 ? 180  PHE A CD1   1 
ATOM   1365 C  CD2   . PHE A  1 205 ? -2.720  0.909   107.016 1.00 21.51 ? 180  PHE A CD2   1 
ATOM   1366 C  CE1   . PHE A  1 205 ? -0.565  -0.421  108.232 1.00 27.45 ? 180  PHE A CE1   1 
ATOM   1367 C  CE2   . PHE A  1 205 ? -1.868  0.089   106.250 1.00 26.15 ? 180  PHE A CE2   1 
ATOM   1368 C  CZ    . PHE A  1 205 ? -0.786  -0.586  106.855 1.00 21.58 ? 180  PHE A CZ    1 
ATOM   1369 N  N     . ASN A  1 206 ? -3.458  1.041   112.060 1.00 17.47 ? 181  ASN A N     1 
ATOM   1370 C  CA    . ASN A  1 206 ? -2.882  0.215   113.099 1.00 19.01 ? 181  ASN A CA    1 
ATOM   1371 C  C     . ASN A  1 206 ? -3.962  -0.486  113.932 1.00 23.35 ? 181  ASN A C     1 
ATOM   1372 O  O     . ASN A  1 206 ? -3.978  -1.723  114.019 1.00 27.64 ? 181  ASN A O     1 
ATOM   1373 C  CB    . ASN A  1 206 ? -1.931  1.023   113.969 1.00 21.37 ? 181  ASN A CB    1 
ATOM   1374 C  CG    . ASN A  1 206 ? -1.098  0.118   114.826 1.00 28.48 ? 181  ASN A CG    1 
ATOM   1375 O  OD1   . ASN A  1 206 ? -0.016  -0.312  114.399 1.00 23.35 ? 181  ASN A OD1   1 
ATOM   1376 N  ND2   . ASN A  1 206 ? -1.593  -0.206  116.019 1.00 19.31 ? 181  ASN A ND2   1 
ATOM   1377 N  N     . PHE A  1 207 ? -4.909  0.265   114.493 1.00 18.65 ? 182  PHE A N     1 
ATOM   1378 C  CA    . PHE A  1 207 ? -5.881  -0.336  115.414 1.00 16.51 ? 182  PHE A CA    1 
ATOM   1379 C  C     . PHE A  1 207 ? -6.907  -1.185  114.669 1.00 19.63 ? 182  PHE A C     1 
ATOM   1380 O  O     . PHE A  1 207 ? -7.004  -2.398  114.899 1.00 21.15 ? 182  PHE A O     1 
ATOM   1381 C  CB    . PHE A  1 207 ? -6.573  0.757   116.242 1.00 19.37 ? 182  PHE A CB    1 
ATOM   1382 C  CG    . PHE A  1 207 ? -7.547  0.223   117.292 1.00 16.97 ? 182  PHE A CG    1 
ATOM   1383 C  CD1   . PHE A  1 207 ? -7.312  -0.969  117.954 1.00 18.45 ? 182  PHE A CD1   1 
ATOM   1384 C  CD2   . PHE A  1 207 ? -8.692  0.945   117.619 1.00 20.78 ? 182  PHE A CD2   1 
ATOM   1385 C  CE1   . PHE A  1 207 ? -8.182  -1.446  118.929 1.00 17.28 ? 182  PHE A CE1   1 
ATOM   1386 C  CE2   . PHE A  1 207 ? -9.583  0.471   118.595 1.00 22.16 ? 182  PHE A CE2   1 
ATOM   1387 C  CZ    . PHE A  1 207 ? -9.335  -0.717  119.242 1.00 22.74 ? 182  PHE A CZ    1 
ATOM   1388 N  N     . PHE A  1 208 ? -7.717  -0.566  113.811 1.00 16.45 ? 183  PHE A N     1 
ATOM   1389 C  CA    . PHE A  1 208 ? -8.829  -1.304  113.203 1.00 20.36 ? 183  PHE A CA    1 
ATOM   1390 C  C     . PHE A  1 208 ? -8.301  -2.451  112.339 1.00 18.13 ? 183  PHE A C     1 
ATOM   1391 O  O     . PHE A  1 208 ? -8.650  -3.623  112.550 1.00 20.46 ? 183  PHE A O     1 
ATOM   1392 C  CB    . PHE A  1 208 ? -9.708  -0.375  112.356 1.00 15.80 ? 183  PHE A CB    1 
ATOM   1393 C  CG    . PHE A  1 208 ? -10.586 0.616   113.147 1.00 20.00 ? 183  PHE A CG    1 
ATOM   1394 C  CD1   . PHE A  1 208 ? -10.606 0.650   114.531 1.00 22.21 ? 183  PHE A CD1   1 
ATOM   1395 C  CD2   . PHE A  1 208 ? -11.396 1.509   112.460 1.00 21.21 ? 183  PHE A CD2   1 
ATOM   1396 C  CE1   . PHE A  1 208 ? -11.428 1.544   115.231 1.00 23.32 ? 183  PHE A CE1   1 
ATOM   1397 C  CE2   . PHE A  1 208 ? -12.213 2.416   113.150 1.00 24.91 ? 183  PHE A CE2   1 
ATOM   1398 C  CZ    . PHE A  1 208 ? -12.218 2.430   114.544 1.00 21.17 ? 183  PHE A CZ    1 
ATOM   1399 N  N     . ALA A  1 209 ? -7.409  -2.139  111.397 1.00 15.79 ? 184  ALA A N     1 
ATOM   1400 C  CA    . ALA A  1 209 ? -6.985  -3.148  110.425 1.00 20.23 ? 184  ALA A CA    1 
ATOM   1401 C  C     . ALA A  1 209 ? -5.996  -4.146  111.013 1.00 24.26 ? 184  ALA A C     1 
ATOM   1402 O  O     . ALA A  1 209 ? -6.139  -5.356  110.807 1.00 22.07 ? 184  ALA A O     1 
ATOM   1403 C  CB    . ALA A  1 209 ? -6.366  -2.474  109.196 1.00 20.40 ? 184  ALA A CB    1 
ATOM   1404 N  N     . CYS A  1 210 ? -4.968  -3.668  111.734 1.00 19.35 ? 185  CYS A N     1 
ATOM   1405 C  CA    . CYS A  1 210 ? -3.847  -4.543  112.102 1.00 21.41 ? 185  CYS A CA    1 
ATOM   1406 C  C     . CYS A  1 210 ? -3.980  -5.147  113.495 1.00 18.39 ? 185  CYS A C     1 
ATOM   1407 O  O     . CYS A  1 210 ? -3.280  -6.114  113.802 1.00 19.70 ? 185  CYS A O     1 
ATOM   1408 C  CB    . CYS A  1 210 ? -2.513  -3.809  111.961 1.00 20.69 ? 185  CYS A CB    1 
ATOM   1409 S  SG    . CYS A  1 210 ? -2.205  -3.397  110.200 1.00 29.00 ? 185  CYS A SG    1 
ATOM   1410 N  N     . VAL A  1 211 ? -4.901  -4.657  114.311 1.00 17.72 ? 186  VAL A N     1 
ATOM   1411 C  CA    . VAL A  1 211 ? -5.051  -5.152  115.673 1.00 20.70 ? 186  VAL A CA    1 
ATOM   1412 C  C     . VAL A  1 211 ? -6.443  -5.739  115.860 1.00 22.60 ? 186  VAL A C     1 
ATOM   1413 O  O     . VAL A  1 211 ? -6.574  -6.923  116.188 1.00 21.01 ? 186  VAL A O     1 
ATOM   1414 C  CB    . VAL A  1 211 ? -4.816  -4.034  116.704 1.00 21.14 ? 186  VAL A CB    1 
ATOM   1415 C  CG1   . VAL A  1 211 ? -5.181  -4.541  118.109 1.00 18.49 ? 186  VAL A CG1   1 
ATOM   1416 C  CG2   . VAL A  1 211 ? -3.369  -3.576  116.657 1.00 19.58 ? 186  VAL A CG2   1 
ATOM   1417 N  N     . LEU A  1 212 ? -7.482  -4.929  115.641 1.00 18.64 ? 187  LEU A N     1 
ATOM   1418 C  CA    . LEU A  1 212 ? -8.840  -5.388  115.920 1.00 20.30 ? 187  LEU A CA    1 
ATOM   1419 C  C     . LEU A  1 212 ? -9.212  -6.567  115.039 1.00 17.56 ? 187  LEU A C     1 
ATOM   1420 O  O     . LEU A  1 212 ? -9.700  -7.591  115.533 1.00 23.93 ? 187  LEU A O     1 
ATOM   1421 C  CB    . LEU A  1 212 ? -9.838  -4.252  115.723 1.00 22.61 ? 187  LEU A CB    1 
ATOM   1422 C  CG    . LEU A  1 212 ? -10.328 -3.494  116.933 1.00 34.54 ? 187  LEU A CG    1 
ATOM   1423 C  CD1   . LEU A  1 212 ? -11.520 -2.616  116.504 1.00 28.69 ? 187  LEU A CD1   1 
ATOM   1424 C  CD2   . LEU A  1 212 ? -10.714 -4.471  118.032 1.00 27.91 ? 187  LEU A CD2   1 
ATOM   1425 N  N     . VAL A  1 213 ? -8.999  -6.451  113.728 1.00 19.22 ? 188  VAL A N     1 
ATOM   1426 C  CA    . VAL A  1 213 ? -9.359  -7.560  112.832 1.00 23.64 ? 188  VAL A CA    1 
ATOM   1427 C  C     . VAL A  1 213 ? -8.634  -8.846  113.207 1.00 25.02 ? 188  VAL A C     1 
ATOM   1428 O  O     . VAL A  1 213 ? -9.304  -9.879  113.366 1.00 25.57 ? 188  VAL A O     1 
ATOM   1429 C  CB    . VAL A  1 213 ? -9.132  -7.170  111.359 1.00 22.53 ? 188  VAL A CB    1 
ATOM   1430 C  CG1   . VAL A  1 213 ? -9.166  -8.439  110.462 1.00 25.24 ? 188  VAL A CG1   1 
ATOM   1431 C  CG2   . VAL A  1 213 ? -10.170 -6.179  110.895 1.00 20.28 ? 188  VAL A CG2   1 
ATOM   1432 N  N     . PRO A  1 214 ? -7.306  -8.858  113.416 1.00 25.66 ? 189  PRO A N     1 
ATOM   1433 C  CA    . PRO A  1 214 ? -6.678  -10.110 113.873 1.00 22.60 ? 189  PRO A CA    1 
ATOM   1434 C  C     . PRO A  1 214 ? -7.205  -10.601 115.210 1.00 25.11 ? 189  PRO A C     1 
ATOM   1435 O  O     . PRO A  1 214 ? -7.320  -11.813 115.392 1.00 24.00 ? 189  PRO A O     1 
ATOM   1436 C  CB    . PRO A  1 214 ? -5.185  -9.750  113.939 1.00 22.26 ? 189  PRO A CB    1 
ATOM   1437 C  CG    . PRO A  1 214 ? -5.017  -8.654  112.951 1.00 25.41 ? 189  PRO A CG    1 
ATOM   1438 C  CD    . PRO A  1 214 ? -6.286  -7.838  113.073 1.00 22.63 ? 189  PRO A CD    1 
ATOM   1439 N  N     . LEU A  1 215 ? -7.484  -9.717  116.169 1.00 18.76 ? 190  LEU A N     1 
ATOM   1440 C  CA    . LEU A  1 215 ? -8.042  -10.192 117.437 1.00 21.15 ? 190  LEU A CA    1 
ATOM   1441 C  C     . LEU A  1 215 ? -9.409  -10.835 117.232 1.00 21.69 ? 190  LEU A C     1 
ATOM   1442 O  O     . LEU A  1 215 ? -9.709  -11.878 117.829 1.00 20.83 ? 190  LEU A O     1 
ATOM   1443 C  CB    . LEU A  1 215 ? -8.111  -9.052  118.468 1.00 19.96 ? 190  LEU A CB    1 
ATOM   1444 C  CG    . LEU A  1 215 ? -6.744  -8.597  119.049 1.00 24.01 ? 190  LEU A CG    1 
ATOM   1445 C  CD1   . LEU A  1 215 ? -6.912  -7.334  119.927 1.00 27.72 ? 190  LEU A CD1   1 
ATOM   1446 C  CD2   . LEU A  1 215 ? -6.015  -9.699  119.823 1.00 25.64 ? 190  LEU A CD2   1 
ATOM   1447 N  N     . LEU A  1 216 ? -10.238 -10.242 116.370 1.00 20.98 ? 191  LEU A N     1 
ATOM   1448 C  CA    . LEU A  1 216 ? -11.552 -10.813 116.050 1.00 23.02 ? 191  LEU A CA    1 
ATOM   1449 C  C     . LEU A  1 216 ? -11.422 -12.150 115.324 1.00 26.55 ? 191  LEU A C     1 
ATOM   1450 O  O     . LEU A  1 216 ? -12.186 -13.082 115.590 1.00 25.37 ? 191  LEU A O     1 
ATOM   1451 C  CB    . LEU A  1 216 ? -12.355 -9.802  115.210 1.00 22.53 ? 191  LEU A CB    1 
ATOM   1452 C  CG    . LEU A  1 216 ? -12.774 -8.538  115.990 1.00 26.74 ? 191  LEU A CG    1 
ATOM   1453 C  CD1   . LEU A  1 216 ? -13.473 -7.508  115.107 1.00 26.37 ? 191  LEU A CD1   1 
ATOM   1454 C  CD2   . LEU A  1 216 ? -13.637 -8.877  117.188 1.00 32.04 ? 191  LEU A CD2   1 
ATOM   1455 N  N     . LEU A  1 217 ? -10.446 -12.274 114.425 1.00 21.31 ? 192  LEU A N     1 
ATOM   1456 C  CA    . LEU A  1 217 ? -10.177 -13.571 113.813 1.00 21.72 ? 192  LEU A CA    1 
ATOM   1457 C  C     . LEU A  1 217 ? -9.770  -14.602 114.860 1.00 29.09 ? 192  LEU A C     1 
ATOM   1458 O  O     . LEU A  1 217 ? -10.266 -15.733 114.852 1.00 26.81 ? 192  LEU A O     1 
ATOM   1459 C  CB    . LEU A  1 217 ? -9.062  -13.429 112.780 1.00 23.37 ? 192  LEU A CB    1 
ATOM   1460 C  CG    . LEU A  1 217 ? -9.355  -12.572 111.530 1.00 29.88 ? 192  LEU A CG    1 
ATOM   1461 C  CD1   . LEU A  1 217 ? -8.121  -12.507 110.684 1.00 35.90 ? 192  LEU A CD1   1 
ATOM   1462 C  CD2   . LEU A  1 217 ? -10.523 -13.101 110.715 1.00 36.61 ? 192  LEU A CD2   1 
ATOM   1463 N  N     . MET A  1 218 ? -8.915  -14.202 115.807 1.00 23.80 ? 193  MET A N     1 
ATOM   1464 C  CA    . MET A  1 218 ? -8.506  -15.077 116.903 1.00 25.23 ? 193  MET A CA    1 
ATOM   1465 C  C     . MET A  1 218 ? -9.715  -15.538 117.687 1.00 25.25 ? 193  MET A C     1 
ATOM   1466 O  O     . MET A  1 218 ? -9.810  -16.706 118.079 1.00 26.99 ? 193  MET A O     1 
ATOM   1467 C  CB    . MET A  1 218 ? -7.576  -14.326 117.840 1.00 24.23 ? 193  MET A CB    1 
ATOM   1468 C  CG    . MET A  1 218 ? -6.133  -14.303 117.424 1.00 32.23 ? 193  MET A CG    1 
ATOM   1469 S  SD    . MET A  1 218 ? -5.256  -13.358 118.689 1.00 32.56 ? 193  MET A SD    1 
ATOM   1470 C  CE    . MET A  1 218 ? -4.406  -12.168 117.610 1.00 28.41 ? 193  MET A CE    1 
ATOM   1471 N  N     . LEU A  1 219 ? -10.611 -14.599 118.004 1.00 24.09 ? 194  LEU A N     1 
ATOM   1472 C  CA    . LEU A  1 219 ? -11.842 -14.959 118.700 1.00 28.72 ? 194  LEU A CA    1 
ATOM   1473 C  C     . LEU A  1 219 ? -12.613 -16.012 117.912 1.00 24.40 ? 194  LEU A C     1 
ATOM   1474 O  O     . LEU A  1 219 ? -13.074 -17.011 118.469 1.00 26.98 ? 194  LEU A O     1 
ATOM   1475 C  CB    . LEU A  1 219 ? -12.703 -13.711 118.900 1.00 25.06 ? 194  LEU A CB    1 
ATOM   1476 C  CG    . LEU A  1 219 ? -14.079 -13.950 119.526 1.00 29.39 ? 194  LEU A CG    1 
ATOM   1477 C  CD1   . LEU A  1 219 ? -13.963 -14.608 120.904 1.00 31.20 ? 194  LEU A CD1   1 
ATOM   1478 C  CD2   . LEU A  1 219 ? -14.852 -12.668 119.585 1.00 29.84 ? 194  LEU A CD2   1 
ATOM   1479 N  N     . GLY A  1 220 ? -12.733 -15.816 116.601 1.00 26.39 ? 195  GLY A N     1 
ATOM   1480 C  CA    . GLY A  1 220 ? -13.420 -16.804 115.791 1.00 26.83 ? 195  GLY A CA    1 
ATOM   1481 C  C     . GLY A  1 220 ? -12.749 -18.164 115.804 1.00 25.78 ? 195  GLY A C     1 
ATOM   1482 O  O     . GLY A  1 220 ? -13.424 -19.189 115.892 1.00 29.73 ? 195  GLY A O     1 
ATOM   1483 N  N     . VAL A  1 221 ? -11.414 -18.193 115.733 1.00 22.64 ? 196  VAL A N     1 
ATOM   1484 C  CA    . VAL A  1 221 ? -10.671 -19.461 115.806 1.00 23.85 ? 196  VAL A CA    1 
ATOM   1485 C  C     . VAL A  1 221 ? -10.889 -20.168 117.140 1.00 28.60 ? 196  VAL A C     1 
ATOM   1486 O  O     . VAL A  1 221 ? -11.111 -21.383 117.179 1.00 25.72 ? 196  VAL A O     1 
ATOM   1487 C  CB    . VAL A  1 221 ? -9.173  -19.241 115.517 1.00 23.68 ? 196  VAL A CB    1 
ATOM   1488 C  CG1   . VAL A  1 221 ? -8.374  -20.527 115.723 1.00 21.53 ? 196  VAL A CG1   1 
ATOM   1489 C  CG2   . VAL A  1 221 ? -8.991  -18.770 114.093 1.00 23.17 ? 196  VAL A CG2   1 
ATOM   1490 N  N     . TYR A  1 222 ? -10.815 -19.430 118.252 1.00 25.87 ? 197  TYR A N     1 
ATOM   1491 C  CA    . TYR A  1 222 ? -11.019 -20.060 119.559 1.00 26.15 ? 197  TYR A CA    1 
ATOM   1492 C  C     . TYR A  1 222 ? -12.442 -20.614 119.687 1.00 33.00 ? 197  TYR A C     1 
ATOM   1493 O  O     . TYR A  1 222 ? -12.645 -21.679 120.279 1.00 28.20 ? 197  TYR A O     1 
ATOM   1494 C  CB    . TYR A  1 222 ? -10.675 -19.077 120.703 1.00 19.39 ? 197  TYR A CB    1 
ATOM   1495 C  CG    . TYR A  1 222 ? -9.155  -19.045 120.928 1.00 28.23 ? 197  TYR A CG    1 
ATOM   1496 C  CD1   . TYR A  1 222 ? -8.473  -20.197 121.329 1.00 27.47 ? 197  TYR A CD1   1 
ATOM   1497 C  CD2   . TYR A  1 222 ? -8.407  -17.894 120.666 1.00 27.68 ? 197  TYR A CD2   1 
ATOM   1498 C  CE1   . TYR A  1 222 ? -7.096  -20.206 121.498 1.00 27.75 ? 197  TYR A CE1   1 
ATOM   1499 C  CE2   . TYR A  1 222 ? -7.011  -17.882 120.825 1.00 26.44 ? 197  TYR A CE2   1 
ATOM   1500 C  CZ    . TYR A  1 222 ? -6.361  -19.046 121.238 1.00 28.09 ? 197  TYR A CZ    1 
ATOM   1501 O  OH    . TYR A  1 222 ? -4.986  -19.059 121.389 1.00 33.63 ? 197  TYR A OH    1 
ATOM   1502 N  N     . LEU A  1 223 ? -13.440 -19.892 119.161 1.00 27.53 ? 198  LEU A N     1 
ATOM   1503 C  CA    . LEU A  1 223 ? -14.803 -20.409 119.142 1.00 28.19 ? 198  LEU A CA    1 
ATOM   1504 C  C     . LEU A  1 223 ? -14.880 -21.728 118.391 1.00 28.34 ? 198  LEU A C     1 
ATOM   1505 O  O     . LEU A  1 223 ? -15.499 -22.679 118.875 1.00 27.10 ? 198  LEU A O     1 
ATOM   1506 C  CB    . LEU A  1 223 ? -15.739 -19.373 118.508 1.00 27.98 ? 198  LEU A CB    1 
ATOM   1507 C  CG    . LEU A  1 223 ? -15.990 -18.180 119.422 1.00 35.56 ? 198  LEU A CG    1 
ATOM   1508 C  CD1   . LEU A  1 223 ? -16.811 -17.120 118.722 1.00 29.46 ? 198  LEU A CD1   1 
ATOM   1509 C  CD2   . LEU A  1 223 ? -16.714 -18.678 120.659 1.00 41.19 ? 198  LEU A CD2   1 
ATOM   1510 N  N     . ARG A  1 224 ? -14.211 -21.820 117.238 1.00 27.96 ? 199  ARG A N     1 
ATOM   1511 C  CA    . ARG A  1 224 ? -14.194 -23.065 116.484 1.00 29.27 ? 199  ARG A CA    1 
ATOM   1512 C  C     . ARG A  1 224 ? -13.463 -24.160 117.254 1.00 34.95 ? 199  ARG A C     1 
ATOM   1513 O  O     . ARG A  1 224 ? -13.860 -25.331 117.195 1.00 31.02 ? 199  ARG A O     1 
ATOM   1514 C  CB    . ARG A  1 224 ? -13.564 -22.858 115.101 1.00 29.69 ? 199  ARG A CB    1 
ATOM   1515 C  CG    . ARG A  1 224 ? -14.408 -21.986 114.148 1.00 33.21 ? 199  ARG A CG    1 
ATOM   1516 C  CD    . ARG A  1 224 ? -13.797 -21.864 112.734 1.00 39.59 ? 199  ARG A CD    1 
ATOM   1517 N  NE    . ARG A  1 224 ? -13.983 -20.531 112.155 1.00 67.06 ? 199  ARG A NE    1 
ATOM   1518 C  CZ    . ARG A  1 224 ? -13.081 -19.871 111.431 1.00 76.62 ? 199  ARG A CZ    1 
ATOM   1519 N  NH1   . ARG A  1 224 ? -11.889 -20.386 111.166 1.00 73.23 ? 199  ARG A NH1   1 
ATOM   1520 N  NH2   . ARG A  1 224 ? -13.382 -18.657 110.966 1.00 63.78 ? 199  ARG A NH2   1 
ATOM   1521 N  N     . ILE A  1 225 ? -12.376 -23.809 117.951 1.00 23.75 ? 200  ILE A N     1 
ATOM   1522 C  CA    . ILE A  1 225 ? -11.651 -24.802 118.748 1.00 24.98 ? 200  ILE A CA    1 
ATOM   1523 C  C     . ILE A  1 225 ? -12.556 -25.392 119.831 1.00 30.51 ? 200  ILE A C     1 
ATOM   1524 O  O     . ILE A  1 225 ? -12.654 -26.616 119.992 1.00 27.42 ? 200  ILE A O     1 
ATOM   1525 C  CB    . ILE A  1 225 ? -10.371 -24.193 119.350 1.00 25.91 ? 200  ILE A CB    1 
ATOM   1526 C  CG1   . ILE A  1 225 ? -9.324  -23.938 118.262 1.00 28.63 ? 200  ILE A CG1   1 
ATOM   1527 C  CG2   . ILE A  1 225 ? -9.738  -25.150 120.351 1.00 20.44 ? 200  ILE A CG2   1 
ATOM   1528 C  CD1   . ILE A  1 225 ? -8.145  -23.116 118.775 1.00 25.14 ? 200  ILE A CD1   1 
ATOM   1529 N  N     . PHE A  1 226 ? -13.203 -24.533 120.617 1.00 29.39 ? 201  PHE A N     1 
ATOM   1530 C  CA    . PHE A  1 226 ? -14.014 -25.037 121.718 1.00 26.88 ? 201  PHE A CA    1 
ATOM   1531 C  C     . PHE A  1 226 ? -15.251 -25.778 121.208 1.00 33.30 ? 201  PHE A C     1 
ATOM   1532 O  O     . PHE A  1 226 ? -15.654 -26.793 121.788 1.00 31.11 ? 201  PHE A O     1 
ATOM   1533 C  CB    . PHE A  1 226 ? -14.383 -23.879 122.642 1.00 31.29 ? 201  PHE A CB    1 
ATOM   1534 C  CG    . PHE A  1 226 ? -13.193 -23.301 123.380 1.00 27.01 ? 201  PHE A CG    1 
ATOM   1535 C  CD1   . PHE A  1 226 ? -12.366 -24.122 124.122 1.00 31.02 ? 201  PHE A CD1   1 
ATOM   1536 C  CD2   . PHE A  1 226 ? -12.867 -21.962 123.275 1.00 31.79 ? 201  PHE A CD2   1 
ATOM   1537 C  CE1   . PHE A  1 226 ? -11.264 -23.614 124.796 1.00 34.48 ? 201  PHE A CE1   1 
ATOM   1538 C  CE2   . PHE A  1 226 ? -11.751 -21.448 123.938 1.00 29.99 ? 201  PHE A CE2   1 
ATOM   1539 C  CZ    . PHE A  1 226 ? -10.948 -22.279 124.690 1.00 30.58 ? 201  PHE A CZ    1 
ATOM   1540 N  N     . ALA A  1 227 ? -15.837 -25.322 120.100 1.00 28.87 ? 202  ALA A N     1 
ATOM   1541 C  CA    . ALA A  1 227 ? -16.957 -26.057 119.520 1.00 38.45 ? 202  ALA A CA    1 
ATOM   1542 C  C     . ALA A  1 227 ? -16.518 -27.409 118.976 1.00 37.20 ? 202  ALA A C     1 
ATOM   1543 O  O     . ALA A  1 227 ? -17.242 -28.397 119.125 1.00 40.65 ? 202  ALA A O     1 
ATOM   1544 C  CB    . ALA A  1 227 ? -17.637 -25.238 118.425 1.00 27.44 ? 202  ALA A CB    1 
ATOM   1545 N  N     . ALA A  1 228 ? -15.338 -27.491 118.358 1.00 33.19 ? 203  ALA A N     1 
ATOM   1546 C  CA    . ALA A  1 228 ? -14.890 -28.796 117.875 1.00 34.60 ? 203  ALA A CA    1 
ATOM   1547 C  C     . ALA A  1 228 ? -14.624 -29.753 119.030 1.00 40.97 ? 203  ALA A C     1 
ATOM   1548 O  O     . ALA A  1 228 ? -14.985 -30.934 118.957 1.00 39.63 ? 203  ALA A O     1 
ATOM   1549 C  CB    . ALA A  1 228 ? -13.637 -28.662 117.020 1.00 29.55 ? 203  ALA A CB    1 
ATOM   1550 N  N     . ALA A  1 229 ? -13.991 -29.263 120.099 1.00 29.06 ? 204  ALA A N     1 
ATOM   1551 C  CA    . ALA A  1 229 ? -13.771 -30.091 121.279 1.00 37.27 ? 204  ALA A CA    1 
ATOM   1552 C  C     . ALA A  1 229 ? -15.087 -30.554 121.900 1.00 44.81 ? 204  ALA A C     1 
ATOM   1553 O  O     . ALA A  1 229 ? -15.238 -31.730 122.259 1.00 38.87 ? 204  ALA A O     1 
ATOM   1554 C  CB    . ALA A  1 229 ? -12.939 -29.325 122.295 1.00 32.94 ? 204  ALA A CB    1 
ATOM   1555 N  N     . ARG A  1 230 ? -16.051 -29.642 122.041 1.00 37.86 ? 205  ARG A N     1 
ATOM   1556 C  CA    . ARG A  1 230 ? -17.328 -30.019 122.637 1.00 39.58 ? 205  ARG A CA    1 
ATOM   1557 C  C     . ARG A  1 230 ? -18.021 -31.082 121.788 1.00 40.89 ? 205  ARG A C     1 
ATOM   1558 O  O     . ARG A  1 230 ? -18.611 -32.030 122.324 1.00 47.79 ? 205  ARG A O     1 
ATOM   1559 C  CB    . ARG A  1 230 ? -18.210 -28.781 122.858 1.00 36.95 ? 205  ARG A CB    1 
ATOM   1560 C  CG    . ARG A  1 230 ? -19.592 -29.122 123.428 1.00 51.62 ? 205  ARG A CG    1 
ATOM   1561 C  CD    . ARG A  1 230 ? -20.752 -28.714 122.527 1.00 55.99 ? 205  ARG A CD    1 
ATOM   1562 N  NE    . ARG A  1 230 ? -20.799 -27.270 122.330 1.00 52.97 ? 205  ARG A NE    1 
ATOM   1563 C  CZ    . ARG A  1 230 ? -20.616 -26.663 121.165 1.00 63.67 ? 205  ARG A CZ    1 
ATOM   1564 N  NH1   . ARG A  1 230 ? -20.370 -27.349 120.051 1.00 53.79 ? 205  ARG A NH1   1 
ATOM   1565 N  NH2   . ARG A  1 230 ? -20.667 -25.335 121.115 1.00 61.29 ? 205  ARG A NH2   1 
ATOM   1566 N  N     . ARG A  1 231 ? -17.964 -30.935 120.460 1.00 34.76 ? 206  ARG A N     1 
ATOM   1567 C  CA    . ARG A  1 231 ? -18.592 -31.904 119.570 1.00 41.16 ? 206  ARG A CA    1 
ATOM   1568 C  C     . ARG A  1 231 ? -17.895 -33.259 119.644 1.00 46.72 ? 206  ARG A C     1 
ATOM   1569 O  O     . ARG A  1 231 ? -18.555 -34.302 119.664 1.00 47.53 ? 206  ARG A O     1 
ATOM   1570 C  CB    . ARG A  1 231 ? -18.534 -31.388 118.134 1.00 38.88 ? 206  ARG A CB    1 
ATOM   1571 C  CG    . ARG A  1 231 ? -18.835 -32.433 117.075 1.00 50.12 ? 206  ARG A CG    1 
ATOM   1572 C  CD    . ARG A  1 231 ? -18.529 -31.909 115.675 1.00 72.22 ? 206  ARG A CD    1 
ATOM   1573 N  N     . GLN A  1 232 ? -16.563 -33.272 119.702 1.00 41.78 ? 207  GLN A N     1 
ATOM   1574 C  CA    . GLN A  1 232 ? -15.853 -34.543 119.713 1.00 43.34 ? 207  GLN A CA    1 
ATOM   1575 C  C     . GLN A  1 232 ? -16.076 -35.279 121.027 1.00 40.80 ? 207  GLN A C     1 
ATOM   1576 O  O     . GLN A  1 232 ? -16.162 -36.514 121.048 1.00 42.77 ? 207  GLN A O     1 
ATOM   1577 C  CB    . GLN A  1 232 ? -14.374 -34.321 119.433 1.00 39.98 ? 207  GLN A CB    1 
ATOM   1578 C  CG    . GLN A  1 232 ? -14.165 -33.721 118.068 1.00 38.16 ? 207  GLN A CG    1 
ATOM   1579 C  CD    . GLN A  1 232 ? -12.709 -33.539 117.732 1.00 49.54 ? 207  GLN A CD    1 
ATOM   1580 O  OE1   . GLN A  1 232 ? -11.835 -34.155 118.349 1.00 45.83 ? 207  GLN A OE1   1 
ATOM   1581 N  NE2   . GLN A  1 232 ? -12.433 -32.685 116.745 1.00 42.33 ? 207  GLN A NE2   1 
ATOM   1582 N  N     . LEU A  1 233 ? -16.134 -34.541 122.135 1.00 37.76 ? 208  LEU A N     1 
ATOM   1583 C  CA    . LEU A  1 233 ? -16.431 -35.144 123.430 1.00 36.92 ? 208  LEU A CA    1 
ATOM   1584 C  C     . LEU A  1 233 ? -17.839 -35.723 123.445 1.00 49.62 ? 208  LEU A C     1 
ATOM   1585 O  O     . LEU A  1 233 ? -18.067 -36.805 123.998 1.00 49.54 ? 208  LEU A O     1 
ATOM   1586 C  CB    . LEU A  1 233 ? -16.276 -34.088 124.524 1.00 37.45 ? 208  LEU A CB    1 
ATOM   1587 C  CG    . LEU A  1 233 ? -14.863 -33.621 124.885 1.00 57.07 ? 208  LEU A CG    1 
ATOM   1588 C  CD1   . LEU A  1 233 ? -14.881 -32.467 125.882 1.00 54.66 ? 208  LEU A CD1   1 
ATOM   1589 C  CD2   . LEU A  1 233 ? -14.125 -34.788 125.513 1.00 48.28 ? 208  LEU A CD2   1 
ATOM   1590 N  N     . ALA A  1 234 ? -18.801 -34.987 122.881 1.00 48.28 ? 1001 ALA A N     1 
ATOM   1591 C  CA    . ALA A  1 234 ? -20.163 -35.493 122.757 1.00 48.67 ? 1001 ALA A CA    1 
ATOM   1592 C  C     . ALA A  1 234 ? -20.211 -36.756 121.907 1.00 48.57 ? 1001 ALA A C     1 
ATOM   1593 O  O     . ALA A  1 234 ? -20.894 -37.720 122.259 1.00 52.80 ? 1001 ALA A O     1 
ATOM   1594 C  CB    . ALA A  1 234 ? -21.070 -34.409 122.175 1.00 36.00 ? 1001 ALA A CB    1 
ATOM   1595 N  N     . ASP A  1 235 ? -19.455 -36.785 120.809 1.00 46.75 ? 1002 ASP A N     1 
ATOM   1596 C  CA    . ASP A  1 235 ? -19.418 -37.972 119.957 1.00 52.78 ? 1002 ASP A CA    1 
ATOM   1597 C  C     . ASP A  1 235 ? -18.843 -39.182 120.680 1.00 56.41 ? 1002 ASP A C     1 
ATOM   1598 O  O     . ASP A  1 235 ? -19.320 -40.307 120.492 1.00 55.05 ? 1002 ASP A O     1 
ATOM   1599 C  CB    . ASP A  1 235 ? -18.622 -37.693 118.685 1.00 52.87 ? 1002 ASP A CB    1 
ATOM   1600 C  CG    . ASP A  1 235 ? -19.335 -36.737 117.748 1.00 69.10 ? 1002 ASP A CG    1 
ATOM   1601 O  OD1   . ASP A  1 235 ? -20.445 -36.268 118.093 1.00 68.33 ? 1002 ASP A OD1   1 
ATOM   1602 O  OD2   . ASP A  1 235 ? -18.777 -36.452 116.662 1.00 77.14 ? 1002 ASP A OD2   1 
ATOM   1603 N  N     . LEU A  1 236 ? -17.831 -38.977 121.523 1.00 49.36 ? 1003 LEU A N     1 
ATOM   1604 C  CA    . LEU A  1 236 ? -17.290 -40.092 122.294 1.00 56.65 ? 1003 LEU A CA    1 
ATOM   1605 C  C     . LEU A  1 236 ? -18.356 -40.680 123.209 1.00 58.84 ? 1003 LEU A C     1 
ATOM   1606 O  O     . LEU A  1 236 ? -18.533 -41.902 123.266 1.00 53.79 ? 1003 LEU A O     1 
ATOM   1607 C  CB    . LEU A  1 236 ? -16.084 -39.625 123.105 1.00 53.68 ? 1003 LEU A CB    1 
ATOM   1608 C  CG    . LEU A  1 236 ? -14.795 -39.318 122.342 1.00 56.14 ? 1003 LEU A CG    1 
ATOM   1609 C  CD1   . LEU A  1 236 ? -13.822 -38.666 123.304 1.00 52.87 ? 1003 LEU A CD1   1 
ATOM   1610 C  CD2   . LEU A  1 236 ? -14.188 -40.550 121.666 1.00 62.80 ? 1003 LEU A CD2   1 
ATOM   1611 N  N     . GLU A  1 237 ? -19.082 -39.824 123.931 1.00 51.14 ? 1004 GLU A N     1 
ATOM   1612 C  CA    . GLU A  1 237 ? -20.103 -40.339 124.838 1.00 61.94 ? 1004 GLU A CA    1 
ATOM   1613 C  C     . GLU A  1 237 ? -21.266 -40.966 124.071 1.00 64.53 ? 1004 GLU A C     1 
ATOM   1614 O  O     . GLU A  1 237 ? -21.896 -41.905 124.567 1.00 58.36 ? 1004 GLU A O     1 
ATOM   1615 C  CB    . GLU A  1 237 ? -20.579 -39.234 125.778 1.00 62.36 ? 1004 GLU A CB    1 
ATOM   1616 C  CG    . GLU A  1 237 ? -19.595 -38.925 126.919 1.00 70.31 ? 1004 GLU A CG    1 
ATOM   1617 C  CD    . GLU A  1 237 ? -19.131 -40.180 127.653 1.00 78.20 ? 1004 GLU A CD    1 
ATOM   1618 O  OE1   . GLU A  1 237 ? -19.917 -40.719 128.462 1.00 79.38 ? 1004 GLU A OE1   1 
ATOM   1619 O  OE2   . GLU A  1 237 ? -17.980 -40.624 127.429 1.00 80.33 ? 1004 GLU A OE2   1 
ATOM   1620 N  N     . ASP A  1 238 ? -21.595 -40.425 122.896 1.00 56.83 ? 1005 ASP A N     1 
ATOM   1621 C  CA    . ASP A  1 238 ? -22.655 -41.003 122.081 1.00 60.98 ? 1005 ASP A CA    1 
ATOM   1622 C  C     . ASP A  1 238 ? -22.284 -42.391 121.562 1.00 65.68 ? 1005 ASP A C     1 
ATOM   1623 O  O     . ASP A  1 238 ? -23.117 -43.305 121.578 1.00 62.59 ? 1005 ASP A O     1 
ATOM   1624 C  CB    . ASP A  1 238 ? -22.962 -40.088 120.896 1.00 59.53 ? 1005 ASP A CB    1 
ATOM   1625 C  CG    . ASP A  1 238 ? -24.119 -39.146 121.169 1.00 76.20 ? 1005 ASP A CG    1 
ATOM   1626 O  OD1   . ASP A  1 238 ? -24.204 -38.609 122.291 1.00 83.64 ? 1005 ASP A OD1   1 
ATOM   1627 O  OD2   . ASP A  1 238 ? -24.956 -38.954 120.261 1.00 90.41 ? 1005 ASP A OD2   1 
ATOM   1628 N  N     . ASN A  1 239 ? -21.029 -42.585 121.133 1.00 55.64 ? 1006 ASN A N     1 
ATOM   1629 C  CA    . ASN A  1 239 ? -20.641 -43.902 120.644 1.00 56.75 ? 1006 ASN A CA    1 
ATOM   1630 C  C     . ASN A  1 239 ? -20.589 -44.933 121.756 1.00 54.15 ? 1006 ASN A C     1 
ATOM   1631 O  O     . ASN A  1 239 ? -20.971 -46.088 121.539 1.00 49.58 ? 1006 ASN A O     1 
ATOM   1632 C  CB    . ASN A  1 239 ? -19.289 -43.825 119.945 1.00 55.76 ? 1006 ASN A CB    1 
ATOM   1633 C  CG    . ASN A  1 239 ? -19.421 -43.512 118.477 1.00 67.85 ? 1006 ASN A CG    1 
ATOM   1634 O  OD1   . ASN A  1 239 ? -20.312 -42.770 118.076 1.00 69.06 ? 1006 ASN A OD1   1 
ATOM   1635 N  ND2   . ASN A  1 239 ? -18.527 -44.062 117.664 1.00 69.14 ? 1006 ASN A ND2   1 
ATOM   1636 N  N     . TRP A  1 240 ? -20.195 -44.518 122.955 1.00 48.85 ? 1007 TRP A N     1 
ATOM   1637 C  CA    . TRP A  1 240 ? -20.215 -45.400 124.113 1.00 52.74 ? 1007 TRP A CA    1 
ATOM   1638 C  C     . TRP A  1 240 ? -21.643 -45.791 124.467 1.00 54.01 ? 1007 TRP A C     1 
ATOM   1639 O  O     . TRP A  1 240 ? -21.945 -46.970 124.684 1.00 47.29 ? 1007 TRP A O     1 
ATOM   1640 C  CB    . TRP A  1 240 ? -19.547 -44.685 125.286 1.00 46.74 ? 1007 TRP A CB    1 
ATOM   1641 C  CG    . TRP A  1 240 ? -19.483 -45.431 126.568 1.00 52.89 ? 1007 TRP A CG    1 
ATOM   1642 C  CD1   . TRP A  1 240 ? -20.193 -45.159 127.702 1.00 48.06 ? 1007 TRP A CD1   1 
ATOM   1643 C  CD2   . TRP A  1 240 ? -18.626 -46.532 126.886 1.00 49.32 ? 1007 TRP A CD2   1 
ATOM   1644 N  NE1   . TRP A  1 240 ? -19.857 -46.043 128.692 1.00 55.62 ? 1007 TRP A NE1   1 
ATOM   1645 C  CE2   . TRP A  1 240 ? -18.893 -46.895 128.220 1.00 58.19 ? 1007 TRP A CE2   1 
ATOM   1646 C  CE3   . TRP A  1 240 ? -17.667 -47.254 126.169 1.00 57.40 ? 1007 TRP A CE3   1 
ATOM   1647 C  CZ2   . TRP A  1 240 ? -18.231 -47.949 128.857 1.00 54.29 ? 1007 TRP A CZ2   1 
ATOM   1648 C  CZ3   . TRP A  1 240 ? -17.010 -48.304 126.802 1.00 57.73 ? 1007 TRP A CZ3   1 
ATOM   1649 C  CH2   . TRP A  1 240 ? -17.298 -48.640 128.131 1.00 54.60 ? 1007 TRP A CH2   1 
ATOM   1650 N  N     . GLU A  1 241 ? -22.545 -44.809 124.494 1.00 50.75 ? 1008 GLU A N     1 
ATOM   1651 C  CA    . GLU A  1 241 ? -23.940 -45.101 124.803 1.00 56.39 ? 1008 GLU A CA    1 
ATOM   1652 C  C     . GLU A  1 241 ? -24.578 -45.976 123.727 1.00 54.70 ? 1008 GLU A C     1 
ATOM   1653 O  O     . GLU A  1 241 ? -25.310 -46.921 124.046 1.00 51.49 ? 1008 GLU A O     1 
ATOM   1654 C  CB    . GLU A  1 241 ? -24.708 -43.785 125.003 1.00 60.15 ? 1008 GLU A CB    1 
ATOM   1655 C  CG    . GLU A  1 241 ? -25.596 -43.372 123.823 1.00 71.30 ? 1008 GLU A CG    1 
ATOM   1656 C  CD    . GLU A  1 241 ? -26.243 -42.008 123.996 1.00 80.75 ? 1008 GLU A CD    1 
ATOM   1657 O  OE1   . GLU A  1 241 ? -26.681 -41.698 125.124 1.00 87.35 ? 1008 GLU A OE1   1 
ATOM   1658 O  OE2   . GLU A  1 241 ? -26.311 -41.247 122.998 1.00 78.23 ? 1008 GLU A OE2   1 
ATOM   1659 N  N     . THR A  1 242 ? -24.316 -45.680 122.451 1.00 48.52 ? 1009 THR A N     1 
ATOM   1660 C  CA    . THR A  1 242 ? -24.857 -46.492 121.367 1.00 46.20 ? 1009 THR A CA    1 
ATOM   1661 C  C     . THR A  1 242 ? -24.405 -47.949 121.480 1.00 58.30 ? 1009 THR A C     1 
ATOM   1662 O  O     . THR A  1 242 ? -25.183 -48.880 121.222 1.00 56.30 ? 1009 THR A O     1 
ATOM   1663 C  CB    . THR A  1 242 ? -24.450 -45.884 120.028 1.00 45.05 ? 1009 THR A CB    1 
ATOM   1664 O  OG1   . THR A  1 242 ? -25.154 -44.652 119.845 1.00 64.60 ? 1009 THR A OG1   1 
ATOM   1665 C  CG2   . THR A  1 242 ? -24.777 -46.818 118.882 1.00 49.90 ? 1009 THR A CG2   1 
ATOM   1666 N  N     . LEU A  1 243 ? -23.145 -48.164 121.848 1.00 50.65 ? 1010 LEU A N     1 
ATOM   1667 C  CA    . LEU A  1 243 ? -22.644 -49.519 122.050 1.00 48.40 ? 1010 LEU A CA    1 
ATOM   1668 C  C     . LEU A  1 243 ? -23.412 -50.226 123.168 1.00 52.58 ? 1010 LEU A C     1 
ATOM   1669 O  O     . LEU A  1 243 ? -23.843 -51.377 123.013 1.00 44.49 ? 1010 LEU A O     1 
ATOM   1670 C  CB    . LEU A  1 243 ? -21.138 -49.503 122.292 1.00 45.59 ? 1010 LEU A CB    1 
ATOM   1671 C  CG    . LEU A  1 243 ? -20.572 -50.853 122.717 1.00 50.50 ? 1010 LEU A CG    1 
ATOM   1672 C  CD1   . LEU A  1 243 ? -20.037 -51.538 121.480 1.00 65.81 ? 1010 LEU A CD1   1 
ATOM   1673 C  CD2   . LEU A  1 243 ? -19.461 -50.671 123.720 1.00 57.80 ? 1010 LEU A CD2   1 
ATOM   1674 N  N     . ASN A  1 244 ? -23.578 -49.555 124.312 1.00 38.95 ? 1011 ASN A N     1 
ATOM   1675 C  CA    . ASN A  1 244 ? -24.205 -50.195 125.467 1.00 46.55 ? 1011 ASN A CA    1 
ATOM   1676 C  C     . ASN A  1 244 ? -25.708 -50.365 125.257 1.00 49.22 ? 1011 ASN A C     1 
ATOM   1677 O  O     . ASN A  1 244 ? -26.301 -51.322 125.766 1.00 47.88 ? 1011 ASN A O     1 
ATOM   1678 C  CB    . ASN A  1 244 ? -23.935 -49.374 126.724 1.00 47.63 ? 1011 ASN A CB    1 
ATOM   1679 C  CG    . ASN A  1 244 ? -22.515 -49.523 127.233 1.00 58.29 ? 1011 ASN A CG    1 
ATOM   1680 O  OD1   . ASN A  1 244 ? -21.779 -50.417 126.811 1.00 59.38 ? 1011 ASN A OD1   1 
ATOM   1681 N  ND2   . ASN A  1 244 ? -22.114 -48.625 128.130 1.00 60.02 ? 1011 ASN A ND2   1 
ATOM   1682 N  N     . ASP A  1 245 ? -26.353 -49.399 124.598 1.00 44.79 ? 1012 ASP A N     1 
ATOM   1683 C  CA    . ASP A  1 245 ? -27.763 -49.544 124.250 1.00 45.31 ? 1012 ASP A CA    1 
ATOM   1684 C  C     . ASP A  1 245 ? -27.963 -50.752 123.358 1.00 48.52 ? 1012 ASP A C     1 
ATOM   1685 O  O     . ASP A  1 245 ? -28.878 -51.552 123.575 1.00 46.66 ? 1012 ASP A O     1 
ATOM   1686 C  CB    . ASP A  1 245 ? -28.308 -48.289 123.584 1.00 44.04 ? 1012 ASP A CB    1 
ATOM   1687 C  CG    . ASP A  1 245 ? -28.329 -47.121 124.526 1.00 57.29 ? 1012 ASP A CG    1 
ATOM   1688 O  OD1   . ASP A  1 245 ? -28.302 -47.371 125.753 1.00 61.00 ? 1012 ASP A OD1   1 
ATOM   1689 O  OD2   . ASP A  1 245 ? -28.353 -45.967 124.051 1.00 58.94 ? 1012 ASP A OD2   1 
ATOM   1690 N  N     . ASN A  1 246 ? -27.152 -50.865 122.309 1.00 44.32 ? 1013 ASN A N     1 
ATOM   1691 C  CA    . ASN A  1 246 ? -27.340 -51.943 121.351 1.00 47.67 ? 1013 ASN A CA    1 
ATOM   1692 C  C     . ASN A  1 246 ? -27.041 -53.302 121.990 1.00 46.93 ? 1013 ASN A C     1 
ATOM   1693 O  O     . ASN A  1 246 ? -27.608 -54.315 121.566 1.00 47.75 ? 1013 ASN A O     1 
ATOM   1694 C  CB    . ASN A  1 246 ? -26.446 -51.706 120.133 1.00 50.58 ? 1013 ASN A CB    1 
ATOM   1695 C  CG    . ASN A  1 246 ? -27.102 -50.817 119.084 1.00 59.19 ? 1013 ASN A CG    1 
ATOM   1696 O  OD1   . ASN A  1 246 ? -28.319 -50.840 118.910 1.00 61.06 ? 1013 ASN A OD1   1 
ATOM   1697 N  ND2   . ASN A  1 246 ? -26.294 -50.004 118.402 1.00 54.46 ? 1013 ASN A ND2   1 
ATOM   1698 N  N     . LEU A  1 247 ? -26.150 -53.355 122.989 1.00 42.80 ? 1014 LEU A N     1 
ATOM   1699 C  CA    . LEU A  1 247 ? -26.001 -54.596 123.742 1.00 44.93 ? 1014 LEU A CA    1 
ATOM   1700 C  C     . LEU A  1 247 ? -27.304 -54.978 124.442 1.00 57.31 ? 1014 LEU A C     1 
ATOM   1701 O  O     . LEU A  1 247 ? -27.694 -56.152 124.433 1.00 48.76 ? 1014 LEU A O     1 
ATOM   1702 C  CB    . LEU A  1 247 ? -24.869 -54.490 124.772 1.00 45.57 ? 1014 LEU A CB    1 
ATOM   1703 C  CG    . LEU A  1 247 ? -23.436 -54.555 124.258 1.00 53.28 ? 1014 LEU A CG    1 
ATOM   1704 C  CD1   . LEU A  1 247 ? -22.469 -53.895 125.240 1.00 55.03 ? 1014 LEU A CD1   1 
ATOM   1705 C  CD2   . LEU A  1 247 ? -23.037 -55.998 123.997 1.00 49.56 ? 1014 LEU A CD2   1 
ATOM   1706 N  N     . LYS A  1 248 ? -27.990 -54.001 125.052 1.00 47.28 ? 1015 LYS A N     1 
ATOM   1707 C  CA    . LYS A  1 248 ? -29.276 -54.280 125.690 1.00 50.97 ? 1015 LYS A CA    1 
ATOM   1708 C  C     . LYS A  1 248 ? -30.318 -54.743 124.681 1.00 44.63 ? 1015 LYS A C     1 
ATOM   1709 O  O     . LYS A  1 248 ? -31.079 -55.676 124.953 1.00 53.33 ? 1015 LYS A O     1 
ATOM   1710 C  CB    . LYS A  1 248 ? -29.791 -53.055 126.446 1.00 51.83 ? 1015 LYS A CB    1 
ATOM   1711 C  CG    . LYS A  1 248 ? -28.937 -52.597 127.620 1.00 56.39 ? 1015 LYS A CG    1 
ATOM   1712 C  CD    . LYS A  1 248 ? -28.116 -53.749 128.199 1.00 66.35 ? 1015 LYS A CD    1 
ATOM   1713 C  CE    . LYS A  1 248 ? -27.487 -53.367 129.539 1.00 71.60 ? 1015 LYS A CE    1 
ATOM   1714 N  NZ    . LYS A  1 248 ? -27.020 -54.561 130.307 1.00 72.77 ? 1015 LYS A NZ    1 
ATOM   1715 N  N     . VAL A  1 249 ? -30.352 -54.123 123.503 1.00 46.87 ? 1016 VAL A N     1 
ATOM   1716 C  CA    . VAL A  1 249 ? -31.290 -54.536 122.464 1.00 51.94 ? 1016 VAL A CA    1 
ATOM   1717 C  C     . VAL A  1 249 ? -31.086 -56.012 122.131 1.00 55.59 ? 1016 VAL A C     1 
ATOM   1718 O  O     . VAL A  1 249 ? -32.050 -56.779 122.030 1.00 51.01 ? 1016 VAL A O     1 
ATOM   1719 C  CB    . VAL A  1 249 ? -31.110 -53.640 121.222 1.00 46.40 ? 1016 VAL A CB    1 
ATOM   1720 C  CG1   . VAL A  1 249 ? -31.852 -54.191 120.020 1.00 37.40 ? 1016 VAL A CG1   1 
ATOM   1721 C  CG2   . VAL A  1 249 ? -31.575 -52.237 121.523 1.00 49.64 ? 1016 VAL A CG2   1 
ATOM   1722 N  N     . ILE A  1 250 ? -29.826 -56.438 122.003 1.00 52.45 ? 1017 ILE A N     1 
ATOM   1723 C  CA    . ILE A  1 250 ? -29.524 -57.833 121.692 1.00 52.99 ? 1017 ILE A CA    1 
ATOM   1724 C  C     . ILE A  1 250 ? -29.981 -58.736 122.830 1.00 50.59 ? 1017 ILE A C     1 
ATOM   1725 O  O     . ILE A  1 250 ? -30.536 -59.818 122.603 1.00 55.19 ? 1017 ILE A O     1 
ATOM   1726 C  CB    . ILE A  1 250 ? -28.023 -58.002 121.392 1.00 41.92 ? 1017 ILE A CB    1 
ATOM   1727 C  CG1   . ILE A  1 250 ? -27.674 -57.294 120.084 1.00 39.20 ? 1017 ILE A CG1   1 
ATOM   1728 C  CG2   . ILE A  1 250 ? -27.598 -59.472 121.360 1.00 44.90 ? 1017 ILE A CG2   1 
ATOM   1729 C  CD1   . ILE A  1 250 ? -26.205 -57.085 119.885 1.00 45.27 ? 1017 ILE A CD1   1 
ATOM   1730 N  N     . GLU A  1 251 ? -29.758 -58.307 124.071 1.00 47.49 ? 1018 GLU A N     1 
ATOM   1731 C  CA    . GLU A  1 251 ? -30.115 -59.127 125.222 1.00 50.08 ? 1018 GLU A CA    1 
ATOM   1732 C  C     . GLU A  1 251 ? -31.600 -59.426 125.271 1.00 62.18 ? 1018 GLU A C     1 
ATOM   1733 O  O     . GLU A  1 251 ? -31.992 -60.552 125.583 1.00 65.17 ? 1018 GLU A O     1 
ATOM   1734 C  CB    . GLU A  1 251 ? -29.673 -58.442 126.503 1.00 50.03 ? 1018 GLU A CB    1 
ATOM   1735 C  CG    . GLU A  1 251 ? -28.205 -58.625 126.803 1.00 53.55 ? 1018 GLU A CG    1 
ATOM   1736 C  CD    . GLU A  1 251 ? -27.717 -57.674 127.869 1.00 62.14 ? 1018 GLU A CD    1 
ATOM   1737 O  OE1   . GLU A  1 251 ? -28.570 -56.968 128.438 1.00 65.77 ? 1018 GLU A OE1   1 
ATOM   1738 O  OE2   . GLU A  1 251 ? -26.486 -57.570 128.087 1.00 61.44 ? 1018 GLU A OE2   1 
ATOM   1739 N  N     . LYS A  1 252 ? -32.433 -58.434 124.969 1.00 57.65 ? 1019 LYS A N     1 
ATOM   1740 C  CA    . LYS A  1 252 ? -33.881 -58.538 125.024 1.00 59.47 ? 1019 LYS A CA    1 
ATOM   1741 C  C     . LYS A  1 252 ? -34.500 -58.702 123.643 1.00 60.31 ? 1019 LYS A C     1 
ATOM   1742 O  O     . LYS A  1 252 ? -35.716 -58.537 123.496 1.00 61.36 ? 1019 LYS A O     1 
ATOM   1743 C  CB    . LYS A  1 252 ? -34.461 -57.262 125.652 1.00 62.61 ? 1019 LYS A CB    1 
ATOM   1744 C  CG    . LYS A  1 252 ? -33.631 -56.609 126.762 1.00 60.95 ? 1019 LYS A CG    1 
ATOM   1745 C  CD    . LYS A  1 252 ? -34.173 -56.780 128.166 1.00 66.80 ? 1019 LYS A CD    1 
ATOM   1746 C  CE    . LYS A  1 252 ? -33.931 -55.496 128.957 1.00 76.80 ? 1019 LYS A CE    1 
ATOM   1747 N  NZ    . LYS A  1 252 ? -34.049 -55.643 130.436 1.00 71.10 ? 1019 LYS A NZ    1 
ATOM   1748 N  N     . ALA A  1 253 ? -33.713 -59.091 122.648 1.00 49.79 ? 1020 ALA A N     1 
ATOM   1749 C  CA    . ALA A  1 253 ? -34.271 -59.439 121.352 1.00 55.99 ? 1020 ALA A CA    1 
ATOM   1750 C  C     . ALA A  1 253 ? -35.070 -60.730 121.424 1.00 63.35 ? 1020 ALA A C     1 
ATOM   1751 O  O     . ALA A  1 253 ? -34.859 -61.575 122.297 1.00 56.11 ? 1020 ALA A O     1 
ATOM   1752 C  CB    . ALA A  1 253 ? -33.158 -59.587 120.316 1.00 52.01 ? 1020 ALA A CB    1 
ATOM   1753 N  N     . ASP A  1 254 ? -36.026 -60.868 120.509 1.00 60.93 ? 1021 ASP A N     1 
ATOM   1754 C  CA    . ASP A  1 254 ? -36.825 -62.077 120.485 1.00 74.79 ? 1021 ASP A CA    1 
ATOM   1755 C  C     . ASP A  1 254 ? -36.737 -62.835 119.170 1.00 70.96 ? 1021 ASP A C     1 
ATOM   1756 O  O     . ASP A  1 254 ? -37.353 -63.901 119.054 1.00 70.80 ? 1021 ASP A O     1 
ATOM   1757 C  CB    . ASP A  1 254 ? -38.292 -61.741 120.793 1.00 73.89 ? 1021 ASP A CB    1 
ATOM   1758 N  N     . ASN A  1 255 ? -35.985 -62.336 118.188 1.00 66.89 ? 1022 ASN A N     1 
ATOM   1759 C  CA    . ASN A  1 255 ? -35.724 -63.082 116.964 1.00 63.68 ? 1022 ASN A CA    1 
ATOM   1760 C  C     . ASN A  1 255 ? -34.325 -62.765 116.459 1.00 68.18 ? 1022 ASN A C     1 
ATOM   1761 O  O     . ASN A  1 255 ? -33.670 -61.818 116.906 1.00 57.33 ? 1022 ASN A O     1 
ATOM   1762 C  CB    . ASN A  1 255 ? -36.757 -62.813 115.861 1.00 65.55 ? 1022 ASN A CB    1 
ATOM   1763 C  CG    . ASN A  1 255 ? -36.861 -61.356 115.485 1.00 62.48 ? 1022 ASN A CG    1 
ATOM   1764 O  OD1   . ASN A  1 255 ? -35.923 -60.585 115.647 1.00 61.84 ? 1022 ASN A OD1   1 
ATOM   1765 N  ND2   . ASN A  1 255 ? -38.011 -60.977 114.941 1.00 71.20 ? 1022 ASN A ND2   1 
ATOM   1766 N  N     . ALA A  1 256 ? -33.876 -63.583 115.511 1.00 63.34 ? 1023 ALA A N     1 
ATOM   1767 C  CA    . ALA A  1 256 ? -32.532 -63.419 114.991 1.00 53.22 ? 1023 ALA A CA    1 
ATOM   1768 C  C     . ALA A  1 256 ? -32.416 -62.118 114.214 1.00 60.01 ? 1023 ALA A C     1 
ATOM   1769 O  O     . ALA A  1 256 ? -31.345 -61.505 114.187 1.00 66.10 ? 1023 ALA A O     1 
ATOM   1770 C  CB    . ALA A  1 256 ? -32.162 -64.611 114.102 1.00 46.78 ? 1023 ALA A CB    1 
ATOM   1771 N  N     . ALA A  1 257 ? -33.516 -61.658 113.617 1.00 60.39 ? 1024 ALA A N     1 
ATOM   1772 C  CA    . ALA A  1 257 ? -33.471 -60.436 112.820 1.00 59.96 ? 1024 ALA A CA    1 
ATOM   1773 C  C     . ALA A  1 257 ? -33.201 -59.203 113.677 1.00 60.68 ? 1024 ALA A C     1 
ATOM   1774 O  O     . ALA A  1 257 ? -32.547 -58.260 113.216 1.00 61.57 ? 1024 ALA A O     1 
ATOM   1775 C  CB    . ALA A  1 257 ? -34.775 -60.278 112.039 1.00 61.29 ? 1024 ALA A CB    1 
ATOM   1776 N  N     . GLN A  1 258 ? -33.731 -59.166 114.902 1.00 52.48 ? 1025 GLN A N     1 
ATOM   1777 C  CA    . GLN A  1 258 ? -33.457 -58.041 115.792 1.00 56.82 ? 1025 GLN A CA    1 
ATOM   1778 C  C     . GLN A  1 258 ? -32.000 -58.005 116.219 1.00 56.47 ? 1025 GLN A C     1 
ATOM   1779 O  O     . GLN A  1 258 ? -31.395 -56.929 116.290 1.00 53.18 ? 1025 GLN A O     1 
ATOM   1780 C  CB    . GLN A  1 258 ? -34.345 -58.115 117.029 1.00 50.75 ? 1025 GLN A CB    1 
ATOM   1781 C  CG    . GLN A  1 258 ? -35.588 -57.289 116.922 1.00 62.57 ? 1025 GLN A CG    1 
ATOM   1782 C  CD    . GLN A  1 258 ? -36.754 -57.942 117.608 1.00 67.50 ? 1025 GLN A CD    1 
ATOM   1783 O  OE1   . GLN A  1 258 ? -36.649 -58.379 118.757 1.00 66.22 ? 1025 GLN A OE1   1 
ATOM   1784 N  NE2   . GLN A  1 258 ? -37.886 -58.003 116.913 1.00 61.65 ? 1025 GLN A NE2   1 
ATOM   1785 N  N     . VAL A  1 259 ? -31.436 -59.172 116.536 1.00 53.50 ? 1026 VAL A N     1 
ATOM   1786 C  CA    . VAL A  1 259 ? -30.016 -59.264 116.856 1.00 49.25 ? 1026 VAL A CA    1 
ATOM   1787 C  C     . VAL A  1 259 ? -29.171 -58.792 115.685 1.00 53.71 ? 1026 VAL A C     1 
ATOM   1788 O  O     . VAL A  1 259 ? -28.216 -58.028 115.865 1.00 48.75 ? 1026 VAL A O     1 
ATOM   1789 C  CB    . VAL A  1 259 ? -29.654 -60.702 117.268 1.00 45.18 ? 1026 VAL A CB    1 
ATOM   1790 C  CG1   . VAL A  1 259 ? -28.192 -60.788 117.584 1.00 40.51 ? 1026 VAL A CG1   1 
ATOM   1791 C  CG2   . VAL A  1 259 ? -30.453 -61.091 118.497 1.00 39.84 ? 1026 VAL A CG2   1 
ATOM   1792 N  N     . LYS A  1 260 ? -29.528 -59.208 114.466 1.00 50.55 ? 1027 LYS A N     1 
ATOM   1793 C  CA    . LYS A  1 260 ? -28.762 -58.815 113.286 1.00 53.01 ? 1027 LYS A CA    1 
ATOM   1794 C  C     . LYS A  1 260 ? -28.765 -57.305 113.119 1.00 57.01 ? 1027 LYS A C     1 
ATOM   1795 O  O     . LYS A  1 260 ? -27.718 -56.693 112.866 1.00 54.02 ? 1027 LYS A O     1 
ATOM   1796 C  CB    . LYS A  1 260 ? -29.356 -59.473 112.041 1.00 56.29 ? 1027 LYS A CB    1 
ATOM   1797 C  CG    . LYS A  1 260 ? -28.566 -59.268 110.753 1.00 65.00 ? 1027 LYS A CG    1 
ATOM   1798 C  CD    . LYS A  1 260 ? -29.508 -59.327 109.557 1.00 63.91 ? 1027 LYS A CD    1 
ATOM   1799 C  CE    . LYS A  1 260 ? -28.977 -58.542 108.384 1.00 63.89 ? 1027 LYS A CE    1 
ATOM   1800 N  NZ    . LYS A  1 260 ? -28.029 -59.371 107.619 1.00 74.49 ? 1027 LYS A NZ    1 
ATOM   1801 N  N     . ASP A  1 261 ? -29.942 -56.693 113.243 1.00 60.51 ? 1028 ASP A N     1 
ATOM   1802 C  CA    . ASP A  1 261 ? -30.063 -55.246 113.101 1.00 53.54 ? 1028 ASP A CA    1 
ATOM   1803 C  C     . ASP A  1 261 ? -29.131 -54.513 114.060 1.00 49.78 ? 1028 ASP A C     1 
ATOM   1804 O  O     . ASP A  1 261 ? -28.370 -53.627 113.651 1.00 55.29 ? 1028 ASP A O     1 
ATOM   1805 C  CB    . ASP A  1 261 ? -31.517 -54.823 113.327 1.00 64.98 ? 1028 ASP A CB    1 
ATOM   1806 C  CG    . ASP A  1 261 ? -32.372 -54.963 112.075 1.00 81.43 ? 1028 ASP A CG    1 
ATOM   1807 O  OD1   . ASP A  1 261 ? -33.456 -54.337 112.006 1.00 81.99 ? 1028 ASP A OD1   1 
ATOM   1808 O  OD2   . ASP A  1 261 ? -31.958 -55.709 111.154 1.00 83.87 ? 1028 ASP A OD2   1 
ATOM   1809 N  N     . ALA A  1 262 ? -29.151 -54.894 115.341 1.00 49.83 ? 1029 ALA A N     1 
ATOM   1810 C  CA    . ALA A  1 262 ? -28.334 -54.172 116.311 1.00 43.82 ? 1029 ALA A CA    1 
ATOM   1811 C  C     . ALA A  1 262 ? -26.844 -54.405 116.088 1.00 46.61 ? 1029 ALA A C     1 
ATOM   1812 O  O     . ALA A  1 262 ? -26.042 -53.481 116.246 1.00 48.03 ? 1029 ALA A O     1 
ATOM   1813 C  CB    . ALA A  1 262 ? -28.730 -54.565 117.730 1.00 37.80 ? 1029 ALA A CB    1 
ATOM   1814 N  N     . LEU A  1 263 ? -26.456 -55.613 115.690 1.00 44.47 ? 1030 LEU A N     1 
ATOM   1815 C  CA    . LEU A  1 263 ? -25.037 -55.888 115.484 1.00 50.94 ? 1030 LEU A CA    1 
ATOM   1816 C  C     . LEU A  1 263 ? -24.492 -55.137 114.274 1.00 47.74 ? 1030 LEU A C     1 
ATOM   1817 O  O     . LEU A  1 263 ? -23.348 -54.660 114.288 1.00 40.44 ? 1030 LEU A O     1 
ATOM   1818 C  CB    . LEU A  1 263 ? -24.801 -57.387 115.327 1.00 46.42 ? 1030 LEU A CB    1 
ATOM   1819 C  CG    . LEU A  1 263 ? -24.958 -58.237 116.586 1.00 47.24 ? 1030 LEU A CG    1 
ATOM   1820 C  CD1   . LEU A  1 263 ? -25.168 -59.689 116.170 1.00 44.11 ? 1030 LEU A CD1   1 
ATOM   1821 C  CD2   . LEU A  1 263 ? -23.763 -58.076 117.543 1.00 36.41 ? 1030 LEU A CD2   1 
ATOM   1822 N  N     . THR A  1 264 ? -25.283 -55.062 113.203 1.00 47.99 ? 1031 THR A N     1 
ATOM   1823 C  CA    . THR A  1 264 ? -24.872 -54.319 112.017 1.00 52.42 ? 1031 THR A CA    1 
ATOM   1824 C  C     . THR A  1 264 ? -24.601 -52.860 112.360 1.00 51.83 ? 1031 THR A C     1 
ATOM   1825 O  O     . THR A  1 264 ? -23.646 -52.254 111.855 1.00 48.57 ? 1031 THR A O     1 
ATOM   1826 C  CB    . THR A  1 264 ? -25.954 -54.441 110.953 1.00 54.89 ? 1031 THR A CB    1 
ATOM   1827 O  OG1   . THR A  1 264 ? -27.227 -54.446 111.606 1.00 63.66 ? 1031 THR A OG1   1 
ATOM   1828 C  CG2   . THR A  1 264 ? -25.803 -55.741 110.184 1.00 49.33 ? 1031 THR A CG2   1 
ATOM   1829 N  N     . LYS A  1 265 ? -25.419 -52.290 113.246 1.00 51.46 ? 1032 LYS A N     1 
ATOM   1830 C  CA    . LYS A  1 265 ? -25.183 -50.930 113.709 1.00 50.48 ? 1032 LYS A CA    1 
ATOM   1831 C  C     . LYS A  1 265 ? -23.976 -50.865 114.626 1.00 56.78 ? 1032 LYS A C     1 
ATOM   1832 O  O     . LYS A  1 265 ? -23.250 -49.862 114.635 1.00 56.33 ? 1032 LYS A O     1 
ATOM   1833 C  CB    . LYS A  1 265 ? -26.409 -50.398 114.439 1.00 50.13 ? 1032 LYS A CB    1 
ATOM   1834 C  CG    . LYS A  1 265 ? -27.478 -49.787 113.546 1.00 52.53 ? 1032 LYS A CG    1 
ATOM   1835 C  CD    . LYS A  1 265 ? -28.865 -50.018 114.136 1.00 58.03 ? 1032 LYS A CD    1 
ATOM   1836 C  CE    . LYS A  1 265 ? -29.167 -49.039 115.250 1.00 63.12 ? 1032 LYS A CE    1 
ATOM   1837 N  NZ    . LYS A  1 265 ? -30.576 -48.581 115.183 1.00 59.37 ? 1032 LYS A NZ    1 
ATOM   1838 N  N     . MET A  1 266 ? -23.736 -51.929 115.392 1.00 46.61 ? 1033 MET A N     1 
ATOM   1839 C  CA    . MET A  1 266 ? -22.551 -51.957 116.231 1.00 49.04 ? 1033 MET A CA    1 
ATOM   1840 C  C     . MET A  1 266 ? -21.297 -52.041 115.377 1.00 49.04 ? 1033 MET A C     1 
ATOM   1841 O  O     . MET A  1 266 ? -20.272 -51.434 115.704 1.00 48.62 ? 1033 MET A O     1 
ATOM   1842 C  CB    . MET A  1 266 ? -22.622 -53.126 117.205 1.00 50.71 ? 1033 MET A CB    1 
ATOM   1843 C  CG    . MET A  1 266 ? -23.403 -52.802 118.449 1.00 48.24 ? 1033 MET A CG    1 
ATOM   1844 S  SD    . MET A  1 266 ? -23.773 -54.290 119.393 1.00 55.53 ? 1033 MET A SD    1 
ATOM   1845 C  CE    . MET A  1 266 ? -22.222 -54.438 120.255 1.00 50.87 ? 1033 MET A CE    1 
ATOM   1846 N  N     . ARG A  1 267 ? -21.353 -52.805 114.284 1.00 47.51 ? 1034 ARG A N     1 
ATOM   1847 C  CA    . ARG A  1 267 ? -20.162 -53.006 113.474 1.00 47.11 ? 1034 ARG A CA    1 
ATOM   1848 C  C     . ARG A  1 267 ? -19.742 -51.716 112.779 1.00 57.06 ? 1034 ARG A C     1 
ATOM   1849 O  O     . ARG A  1 267 ? -18.563 -51.342 112.817 1.00 57.07 ? 1034 ARG A O     1 
ATOM   1850 C  CB    . ARG A  1 267 ? -20.413 -54.095 112.433 1.00 42.26 ? 1034 ARG A CB    1 
ATOM   1851 C  CG    . ARG A  1 267 ? -19.132 -54.604 111.802 1.00 37.13 ? 1034 ARG A CG    1 
ATOM   1852 C  CD    . ARG A  1 267 ? -19.436 -55.513 110.650 1.00 42.18 ? 1034 ARG A CD    1 
ATOM   1853 N  NE    . ARG A  1 267 ? -18.212 -56.100 110.120 1.00 59.02 ? 1034 ARG A NE    1 
ATOM   1854 C  CZ    . ARG A  1 267 ? -17.465 -55.526 109.185 1.00 63.31 ? 1034 ARG A CZ    1 
ATOM   1855 N  NH1   . ARG A  1 267 ? -17.789 -54.351 108.665 1.00 68.84 ? 1034 ARG A NH1   1 
ATOM   1856 N  NH2   . ARG A  1 267 ? -16.375 -56.149 108.752 1.00 70.44 ? 1034 ARG A NH2   1 
ATOM   1857 N  N     . ALA A  1 268 ? -20.698 -50.993 112.189 1.00 54.23 ? 1035 ALA A N     1 
ATOM   1858 C  CA    . ALA A  1 268 ? -20.367 -49.716 111.568 1.00 57.38 ? 1035 ALA A CA    1 
ATOM   1859 C  C     . ALA A  1 268 ? -19.829 -48.701 112.565 1.00 51.49 ? 1035 ALA A C     1 
ATOM   1860 O  O     . ALA A  1 268 ? -18.893 -47.971 112.236 1.00 56.93 ? 1035 ALA A O     1 
ATOM   1861 C  CB    . ALA A  1 268 ? -21.600 -49.147 110.858 1.00 49.12 ? 1035 ALA A CB    1 
ATOM   1862 N  N     . ALA A  1 269 ? -20.313 -48.708 113.810 1.00 50.60 ? 1036 ALA A N     1 
ATOM   1863 C  CA    . ALA A  1 269 ? -19.787 -47.758 114.790 1.00 49.17 ? 1036 ALA A CA    1 
ATOM   1864 C  C     . ALA A  1 269 ? -18.377 -48.130 115.228 1.00 66.58 ? 1036 ALA A C     1 
ATOM   1865 O  O     . ALA A  1 269 ? -17.534 -47.249 115.452 1.00 64.02 ? 1036 ALA A O     1 
ATOM   1866 C  CB    . ALA A  1 269 ? -20.703 -47.694 116.011 1.00 44.93 ? 1036 ALA A CB    1 
ATOM   1867 N  N     . ALA A  1 270 ? -18.111 -49.428 115.369 1.00 54.45 ? 1037 ALA A N     1 
ATOM   1868 C  CA    . ALA A  1 270 ? -16.789 -49.878 115.777 1.00 55.98 ? 1037 ALA A CA    1 
ATOM   1869 C  C     . ALA A  1 270 ? -15.738 -49.482 114.751 1.00 54.29 ? 1037 ALA A C     1 
ATOM   1870 O  O     . ALA A  1 270 ? -14.666 -48.982 115.102 1.00 59.07 ? 1037 ALA A O     1 
ATOM   1871 C  CB    . ALA A  1 270 ? -16.793 -51.393 115.996 1.00 54.37 ? 1037 ALA A CB    1 
ATOM   1872 N  N     . LEU A  1 271 ? -16.031 -49.690 113.467 1.00 60.05 ? 1038 LEU A N     1 
ATOM   1873 C  CA    . LEU A  1 271 ? -15.098 -49.261 112.428 1.00 67.18 ? 1038 LEU A CA    1 
ATOM   1874 C  C     . LEU A  1 271 ? -14.933 -47.748 112.389 1.00 72.61 ? 1038 LEU A C     1 
ATOM   1875 O  O     . LEU A  1 271 ? -13.848 -47.250 112.067 1.00 74.75 ? 1038 LEU A O     1 
ATOM   1876 C  CB    . LEU A  1 271 ? -15.589 -49.759 111.073 1.00 64.73 ? 1038 LEU A CB    1 
ATOM   1877 C  CG    . LEU A  1 271 ? -15.867 -51.253 111.020 1.00 61.59 ? 1038 LEU A CG    1 
ATOM   1878 C  CD1   . LEU A  1 271 ? -16.153 -51.688 109.598 1.00 70.55 ? 1038 LEU A CD1   1 
ATOM   1879 C  CD2   . LEU A  1 271 ? -14.692 -52.009 111.594 1.00 71.94 ? 1038 LEU A CD2   1 
ATOM   1880 N  N     . ASP A  1 272 ? -15.986 -47.002 112.715 1.00 71.04 ? 1039 ASP A N     1 
ATOM   1881 C  CA    . ASP A  1 272 ? -15.874 -45.548 112.724 1.00 70.48 ? 1039 ASP A CA    1 
ATOM   1882 C  C     . ASP A  1 272 ? -14.976 -45.075 113.859 1.00 69.62 ? 1039 ASP A C     1 
ATOM   1883 O  O     . ASP A  1 272 ? -14.218 -44.112 113.705 1.00 79.47 ? 1039 ASP A O     1 
ATOM   1884 C  CB    . ASP A  1 272 ? -17.255 -44.917 112.826 1.00 66.23 ? 1039 ASP A CB    1 
ATOM   1885 C  CG    . ASP A  1 272 ? -17.407 -43.730 111.914 1.00 80.05 ? 1039 ASP A CG    1 
ATOM   1886 O  OD1   . ASP A  1 272 ? -18.410 -42.998 112.050 1.00 92.93 ? 1039 ASP A OD1   1 
ATOM   1887 O  OD2   . ASP A  1 272 ? -16.541 -43.550 111.032 1.00 86.77 ? 1039 ASP A OD2   1 
ATOM   1888 N  N     . ALA A  1 273 ? -15.032 -45.763 114.997 1.00 68.71 ? 1040 ALA A N     1 
ATOM   1889 C  CA    . ALA A  1 273 ? -14.159 -45.484 116.132 1.00 78.70 ? 1040 ALA A CA    1 
ATOM   1890 C  C     . ALA A  1 273 ? -12.747 -46.039 115.949 1.00 78.19 ? 1040 ALA A C     1 
ATOM   1891 O  O     . ALA A  1 273 ? -11.834 -45.611 116.664 1.00 77.63 ? 1040 ALA A O     1 
ATOM   1892 C  CB    . ALA A  1 273 ? -14.777 -46.029 117.423 1.00 64.16 ? 1040 ALA A CB    1 
ATOM   1893 N  N     . GLN A  1 274 ? -12.540 -46.959 114.995 1.00 75.38 ? 1041 GLN A N     1 
ATOM   1894 C  CA    . GLN A  1 274 ? -11.204 -47.491 114.740 1.00 76.27 ? 1041 GLN A CA    1 
ATOM   1895 C  C     . GLN A  1 274 ? -10.358 -46.507 113.944 1.00 90.82 ? 1041 GLN A C     1 
ATOM   1896 O  O     . GLN A  1 274 ? -9.128  -46.504 114.062 1.00 96.53 ? 1041 GLN A O     1 
ATOM   1897 C  CB    . GLN A  1 274 ? -11.313 -48.824 113.995 1.00 69.07 ? 1041 GLN A CB    1 
ATOM   1898 C  CG    . GLN A  1 274 ? -10.180 -49.816 114.230 1.00 68.71 ? 1041 GLN A CG    1 
ATOM   1899 C  CD    . GLN A  1 274 ? -10.442 -51.164 113.556 1.00 78.36 ? 1041 GLN A CD    1 
ATOM   1900 O  OE1   . GLN A  1 274 ? -11.261 -51.265 112.643 1.00 85.70 ? 1041 GLN A OE1   1 
ATOM   1901 N  NE2   . GLN A  1 274 ? -9.750  -52.207 114.013 1.00 73.07 ? 1041 GLN A NE2   1 
ATOM   1902 N  N     . LYS A  1 275 ? -10.994 -45.670 113.132 1.00 88.78 ? 1042 LYS A N     1 
ATOM   1903 C  CA    . LYS A  1 275 ? -10.296 -44.654 112.357 1.00 79.66 ? 1042 LYS A CA    1 
ATOM   1904 C  C     . LYS A  1 275 ? -10.694 -43.275 112.849 1.00 82.68 ? 1042 LYS A C     1 
ATOM   1905 O  O     . LYS A  1 275 ? -10.160 -42.794 113.851 1.00 83.09 ? 1042 LYS A O     1 
ATOM   1906 C  CB    . LYS A  1 275 ? -10.567 -44.808 110.857 1.00 77.20 ? 1042 LYS A CB    1 
ATOM   1907 C  CG    . LYS A  1 275 ? -9.923  -46.038 110.179 1.00 82.09 ? 1042 LYS A CG    1 
ATOM   1908 C  CD    . LYS A  1 275 ? -10.411 -47.407 110.643 1.00 85.84 ? 1042 LYS A CD    1 
ATOM   1909 C  CE    . LYS A  1 275 ? -11.639 -47.864 109.880 1.00 86.57 ? 1042 LYS A CE    1 
ATOM   1910 N  NZ    . LYS A  1 275 ? -12.322 -48.969 110.611 1.00 81.04 ? 1042 LYS A NZ    1 
ATOM   1911 N  N     . LYS A  1 292 ? -2.319  -50.093 119.525 1.00 88.14 ? 1059 LYS A N     1 
ATOM   1912 C  CA    . LYS A  1 292 ? -1.678  -51.416 119.743 1.00 91.09 ? 1059 LYS A CA    1 
ATOM   1913 C  C     . LYS A  1 292 ? -2.609  -52.251 120.625 1.00 89.04 ? 1059 LYS A C     1 
ATOM   1914 O  O     . LYS A  1 292 ? -3.363  -53.064 120.076 1.00 86.22 ? 1059 LYS A O     1 
ATOM   1915 C  CB    . LYS A  1 292 ? -0.296  -51.234 120.375 1.00 94.73 ? 1059 LYS A CB    1 
ATOM   1916 N  N     . ASP A  1 293 ? -2.555  -52.057 121.939 1.00 87.72 ? 1060 ASP A N     1 
ATOM   1917 C  CA    . ASP A  1 293 ? -3.538  -52.748 122.806 1.00 87.64 ? 1060 ASP A CA    1 
ATOM   1918 C  C     . ASP A  1 293 ? -4.916  -52.254 122.366 1.00 84.55 ? 1060 ASP A C     1 
ATOM   1919 O  O     . ASP A  1 293 ? -5.879  -53.029 122.455 1.00 84.00 ? 1060 ASP A O     1 
ATOM   1920 C  CB    . ASP A  1 293 ? -3.265  -52.494 124.288 1.00 90.06 ? 1060 ASP A CB    1 
ATOM   1921 N  N     . PHE A  1 294 ? -4.978  -51.023 121.862 1.00 85.28 ? 1061 PHE A N     1 
ATOM   1922 C  CA    . PHE A  1 294 ? -6.256  -50.435 121.400 1.00 80.03 ? 1061 PHE A CA    1 
ATOM   1923 C  C     . PHE A  1 294 ? -6.660  -51.073 120.076 1.00 71.90 ? 1061 PHE A C     1 
ATOM   1924 O  O     . PHE A  1 294 ? -7.844  -51.380 119.886 1.00 70.89 ? 1061 PHE A O     1 
ATOM   1925 C  CB    . PHE A  1 294 ? -6.081  -48.933 121.190 1.00 77.92 ? 1061 PHE A CB    1 
ATOM   1926 N  N     . ARG A  1 295 ? -5.696  -51.221 119.177 1.00 77.24 ? 1062 ARG A N     1 
ATOM   1927 C  CA    . ARG A  1 295 ? -5.987  -51.834 117.858 1.00 76.43 ? 1062 ARG A CA    1 
ATOM   1928 C  C     . ARG A  1 295 ? -6.303  -53.309 118.109 1.00 63.92 ? 1062 ARG A C     1 
ATOM   1929 O  O     . ARG A  1 295 ? -7.182  -53.849 117.425 1.00 52.90 ? 1062 ARG A O     1 
ATOM   1930 C  CB    . ARG A  1 295 ? -4.812  -51.588 116.910 1.00 76.43 ? 1062 ARG A CB    1 
ATOM   1931 N  N     . HIS A  1 296 ? -5.637  -53.910 119.093 1.00 58.19 ? 1063 HIS A N     1 
ATOM   1932 C  CA    . HIS A  1 296 ? -5.984  -55.304 119.453 1.00 64.46 ? 1063 HIS A CA    1 
ATOM   1933 C  C     . HIS A  1 296 ? -7.441  -55.318 119.916 1.00 61.58 ? 1063 HIS A C     1 
ATOM   1934 O  O     . HIS A  1 296 ? -8.194  -56.200 119.489 1.00 49.51 ? 1063 HIS A O     1 
ATOM   1935 C  CB    . HIS A  1 296 ? -5.039  -55.852 120.525 1.00 56.95 ? 1063 HIS A CB    1 
ATOM   1936 C  CG    . HIS A  1 296 ? -5.251  -57.301 120.804 1.00 66.93 ? 1063 HIS A CG    1 
ATOM   1937 N  ND1   . HIS A  1 296 ? -5.471  -58.218 119.800 1.00 65.51 ? 1063 HIS A ND1   1 
ATOM   1938 C  CD2   . HIS A  1 296 ? -5.282  -57.993 121.948 1.00 66.87 ? 1063 HIS A CD2   1 
ATOM   1939 C  CE1   . HIS A  1 296 ? -5.628  -59.419 120.332 1.00 57.05 ? 1063 HIS A CE1   1 
ATOM   1940 N  NE2   . HIS A  1 296 ? -5.516  -59.306 121.635 1.00 56.83 ? 1063 HIS A NE2   1 
ATOM   1941 N  N     . GLY A  1 297 ? -7.811  -54.366 120.775 1.00 55.56 ? 1064 GLY A N     1 
ATOM   1942 C  CA    . GLY A  1 297 ? -9.181  -54.301 121.312 1.00 48.82 ? 1064 GLY A CA    1 
ATOM   1943 C  C     . GLY A  1 297 ? -10.205 -54.156 120.207 1.00 45.00 ? 1064 GLY A C     1 
ATOM   1944 O  O     . GLY A  1 297 ? -11.219 -54.858 120.239 1.00 42.04 ? 1064 GLY A O     1 
ATOM   1945 N  N     . PHE A  1 298 ? -9.919  -53.282 119.255 1.00 42.90 ? 1065 PHE A N     1 
ATOM   1946 C  CA    . PHE A  1 298 ? -10.872 -53.047 118.151 1.00 51.85 ? 1065 PHE A CA    1 
ATOM   1947 C  C     . PHE A  1 298 ? -10.890 -54.281 117.243 1.00 56.57 ? 1065 PHE A C     1 
ATOM   1948 O  O     . PHE A  1 298 ? -11.960 -54.620 116.727 1.00 53.48 ? 1065 PHE A O     1 
ATOM   1949 C  CB    . PHE A  1 298 ? -10.524 -51.748 117.428 1.00 56.74 ? 1065 PHE A CB    1 
ATOM   1950 C  CG    . PHE A  1 298 ? -11.258 -50.556 117.982 1.00 64.49 ? 1065 PHE A CG    1 
ATOM   1951 C  CD1   . PHE A  1 298 ? -12.609 -50.382 117.736 1.00 57.30 ? 1065 PHE A CD1   1 
ATOM   1952 C  CD2   . PHE A  1 298 ? -10.610 -49.629 118.779 1.00 61.30 ? 1065 PHE A CD2   1 
ATOM   1953 C  CE1   . PHE A  1 298 ? -13.291 -49.297 118.258 1.00 61.90 ? 1065 PHE A CE1   1 
ATOM   1954 C  CE2   . PHE A  1 298 ? -11.292 -48.541 119.298 1.00 55.63 ? 1065 PHE A CE2   1 
ATOM   1955 C  CZ    . PHE A  1 298 ? -12.630 -48.378 119.038 1.00 60.85 ? 1065 PHE A CZ    1 
ATOM   1956 N  N     . ASP A  1 299 ? -9.743  -54.942 117.094 1.00 53.13 ? 1066 ASP A N     1 
ATOM   1957 C  CA    . ASP A  1 299 ? -9.730  -56.151 116.284 1.00 48.28 ? 1066 ASP A CA    1 
ATOM   1958 C  C     . ASP A  1 299 ? -10.591 -57.232 116.918 1.00 43.89 ? 1066 ASP A C     1 
ATOM   1959 O  O     . ASP A  1 299 ? -11.390 -57.882 116.235 1.00 50.30 ? 1066 ASP A O     1 
ATOM   1960 C  CB    . ASP A  1 299 ? -8.298  -56.659 116.100 1.00 55.13 ? 1066 ASP A CB    1 
ATOM   1961 C  CG    . ASP A  1 299 ? -7.547  -55.911 115.019 1.00 69.61 ? 1066 ASP A CG    1 
ATOM   1962 O  OD1   . ASP A  1 299 ? -8.210  -55.364 114.109 1.00 76.29 ? 1066 ASP A OD1   1 
ATOM   1963 O  OD2   . ASP A  1 299 ? -6.296  -55.899 115.057 1.00 68.97 ? 1066 ASP A OD2   1 
ATOM   1964 N  N     . ILE A  1 300 ? -10.456 -57.417 118.233 1.00 35.52 ? 1067 ILE A N     1 
ATOM   1965 C  CA    . ILE A  1 300 ? -11.328 -58.332 118.957 1.00 40.37 ? 1067 ILE A CA    1 
ATOM   1966 C  C     . ILE A  1 300 ? -12.786 -57.903 118.826 1.00 45.54 ? 1067 ILE A C     1 
ATOM   1967 O  O     . ILE A  1 300 ? -13.664 -58.718 118.521 1.00 40.45 ? 1067 ILE A O     1 
ATOM   1968 C  CB    . ILE A  1 300 ? -10.895 -58.452 120.429 1.00 36.04 ? 1067 ILE A CB    1 
ATOM   1969 C  CG1   . ILE A  1 300 ? -9.410  -58.831 120.537 1.00 46.73 ? 1067 ILE A CG1   1 
ATOM   1970 C  CG2   . ILE A  1 300 ? -11.775 -59.439 121.173 1.00 37.91 ? 1067 ILE A CG2   1 
ATOM   1971 C  CD1   . ILE A  1 300 ? -8.807  -58.597 121.919 1.00 43.40 ? 1067 ILE A CD1   1 
ATOM   1972 N  N     . LEU A  1 301 ? -13.056 -56.607 119.005 1.00 38.94 ? 1068 LEU A N     1 
ATOM   1973 C  CA    . LEU A  1 301 ? -14.430 -56.128 119.034 1.00 36.46 ? 1068 LEU A CA    1 
ATOM   1974 C  C     . LEU A  1 301 ? -15.127 -56.391 117.714 1.00 33.02 ? 1068 LEU A C     1 
ATOM   1975 O  O     . LEU A  1 301 ? -16.232 -56.947 117.681 1.00 37.55 ? 1068 LEU A O     1 
ATOM   1976 C  CB    . LEU A  1 301 ? -14.462 -54.634 119.342 1.00 37.70 ? 1068 LEU A CB    1 
ATOM   1977 C  CG    . LEU A  1 301 ? -15.866 -54.159 119.704 1.00 41.23 ? 1068 LEU A CG    1 
ATOM   1978 C  CD1   . LEU A  1 301 ? -16.200 -54.690 121.084 1.00 35.65 ? 1068 LEU A CD1   1 
ATOM   1979 C  CD2   . LEU A  1 301 ? -15.992 -52.647 119.628 1.00 40.91 ? 1068 LEU A CD2   1 
ATOM   1980 N  N     . VAL A  1 302 ? -14.501 -55.984 116.613 1.00 32.52 ? 1069 VAL A N     1 
ATOM   1981 C  CA    . VAL A  1 302 ? -15.095 -56.203 115.298 1.00 33.31 ? 1069 VAL A CA    1 
ATOM   1982 C  C     . VAL A  1 302 ? -15.216 -57.692 115.012 1.00 38.95 ? 1069 VAL A C     1 
ATOM   1983 O  O     . VAL A  1 302 ? -16.243 -58.156 114.500 1.00 37.53 ? 1069 VAL A O     1 
ATOM   1984 C  CB    . VAL A  1 302 ? -14.278 -55.479 114.210 1.00 41.18 ? 1069 VAL A CB    1 
ATOM   1985 C  CG1   . VAL A  1 302 ? -14.864 -55.738 112.821 1.00 38.45 ? 1069 VAL A CG1   1 
ATOM   1986 C  CG2   . VAL A  1 302 ? -14.252 -53.985 114.494 1.00 46.02 ? 1069 VAL A CG2   1 
ATOM   1987 N  N     . GLY A  1 303 ? -14.189 -58.468 115.374 1.00 34.60 ? 1070 GLY A N     1 
ATOM   1988 C  CA    . GLY A  1 303 ? -14.260 -59.902 115.163 1.00 31.75 ? 1070 GLY A CA    1 
ATOM   1989 C  C     . GLY A  1 303 ? -15.387 -60.551 115.942 1.00 34.53 ? 1070 GLY A C     1 
ATOM   1990 O  O     . GLY A  1 303 ? -16.070 -61.442 115.435 1.00 35.63 ? 1070 GLY A O     1 
ATOM   1991 N  N     . GLN A  1 304 ? -15.588 -60.124 117.183 1.00 29.42 ? 1071 GLN A N     1 
ATOM   1992 C  CA    . GLN A  1 304 ? -16.663 -60.690 117.986 1.00 35.16 ? 1071 GLN A CA    1 
ATOM   1993 C  C     . GLN A  1 304 ? -18.038 -60.264 117.486 1.00 41.60 ? 1071 GLN A C     1 
ATOM   1994 O  O     . GLN A  1 304 ? -19.001 -61.032 117.584 1.00 38.92 ? 1071 GLN A O     1 
ATOM   1995 C  CB    . GLN A  1 304 ? -16.479 -60.276 119.431 1.00 33.33 ? 1071 GLN A CB    1 
ATOM   1996 C  CG    . GLN A  1 304 ? -15.301 -60.926 120.112 1.00 43.10 ? 1071 GLN A CG    1 
ATOM   1997 C  CD    . GLN A  1 304 ? -15.089 -60.364 121.486 1.00 43.33 ? 1071 GLN A CD    1 
ATOM   1998 O  OE1   . GLN A  1 304 ? -15.161 -59.144 121.672 1.00 39.38 ? 1071 GLN A OE1   1 
ATOM   1999 N  NE2   . GLN A  1 304 ? -14.885 -61.235 122.471 1.00 39.04 ? 1071 GLN A NE2   1 
ATOM   2000 N  N     . ILE A  1 305 ? -18.136 -59.076 116.892 1.00 35.69 ? 1072 ILE A N     1 
ATOM   2001 C  CA    . ILE A  1 305 ? -19.380 -58.669 116.259 1.00 38.34 ? 1072 ILE A CA    1 
ATOM   2002 C  C     . ILE A  1 305 ? -19.653 -59.527 115.030 1.00 34.91 ? 1072 ILE A C     1 
ATOM   2003 O  O     . ILE A  1 305 ? -20.771 -60.015 114.835 1.00 36.54 ? 1072 ILE A O     1 
ATOM   2004 C  CB    . ILE A  1 305 ? -19.319 -57.164 115.919 1.00 33.24 ? 1072 ILE A CB    1 
ATOM   2005 C  CG1   . ILE A  1 305 ? -19.337 -56.334 117.204 1.00 35.70 ? 1072 ILE A CG1   1 
ATOM   2006 C  CG2   . ILE A  1 305 ? -20.449 -56.780 114.967 1.00 43.92 ? 1072 ILE A CG2   1 
ATOM   2007 C  CD1   . ILE A  1 305 ? -19.006 -54.844 117.004 1.00 40.48 ? 1072 ILE A CD1   1 
ATOM   2008 N  N     . ASP A  1 306 ? -18.618 -59.779 114.219 1.00 34.68 ? 1073 ASP A N     1 
ATOM   2009 C  CA    . ASP A  1 306 ? -18.768 -60.645 113.051 1.00 41.04 ? 1073 ASP A CA    1 
ATOM   2010 C  C     . ASP A  1 306 ? -19.176 -62.062 113.440 1.00 45.86 ? 1073 ASP A C     1 
ATOM   2011 O  O     . ASP A  1 306 ? -19.973 -62.697 112.733 1.00 39.27 ? 1073 ASP A O     1 
ATOM   2012 C  CB    . ASP A  1 306 ? -17.471 -60.691 112.247 1.00 42.34 ? 1073 ASP A CB    1 
ATOM   2013 C  CG    . ASP A  1 306 ? -17.180 -59.390 111.528 1.00 50.41 ? 1073 ASP A CG    1 
ATOM   2014 O  OD1   . ASP A  1 306 ? -18.118 -58.571 111.348 1.00 48.36 ? 1073 ASP A OD1   1 
ATOM   2015 O  OD2   . ASP A  1 306 ? -16.015 -59.216 111.105 1.00 50.81 ? 1073 ASP A OD2   1 
ATOM   2016 N  N     . ASP A  1 307 ? -18.590 -62.596 114.521 1.00 36.93 ? 1074 ASP A N     1 
ATOM   2017 C  CA    . ASP A  1 307 ? -18.972 -63.922 115.002 1.00 35.13 ? 1074 ASP A CA    1 
ATOM   2018 C  C     . ASP A  1 307 ? -20.471 -63.950 115.278 1.00 37.71 ? 1074 ASP A C     1 
ATOM   2019 O  O     . ASP A  1 307 ? -21.202 -64.819 114.785 1.00 36.40 ? 1074 ASP A O     1 
ATOM   2020 C  CB    . ASP A  1 307 ? -18.219 -64.284 116.302 1.00 38.65 ? 1074 ASP A CB    1 
ATOM   2021 C  CG    . ASP A  1 307 ? -16.701 -64.496 116.107 1.00 45.37 ? 1074 ASP A CG    1 
ATOM   2022 O  OD1   . ASP A  1 307 ? -15.966 -64.601 117.132 1.00 35.63 ? 1074 ASP A OD1   1 
ATOM   2023 O  OD2   . ASP A  1 307 ? -16.216 -64.460 114.950 1.00 42.61 ? 1074 ASP A OD2   1 
ATOM   2024 N  N     . ALA A  1 308 ? -20.958 -62.936 115.999 1.00 38.50 ? 1075 ALA A N     1 
ATOM   2025 C  CA    . ALA A  1 308 ? -22.362 -62.892 116.384 1.00 38.70 ? 1075 ALA A CA    1 
ATOM   2026 C  C     . ALA A  1 308 ? -23.277 -62.669 115.182 1.00 42.21 ? 1075 ALA A C     1 
ATOM   2027 O  O     . ALA A  1 308 ? -24.332 -63.305 115.083 1.00 37.38 ? 1075 ALA A O     1 
ATOM   2028 C  CB    . ALA A  1 308 ? -22.570 -61.813 117.449 1.00 35.97 ? 1075 ALA A CB    1 
ATOM   2029 N  N     . LEU A  1 309 ? -22.888 -61.794 114.249 1.00 38.18 ? 1076 LEU A N     1 
ATOM   2030 C  CA    . LEU A  1 309 ? -23.674 -61.612 113.027 1.00 42.32 ? 1076 LEU A CA    1 
ATOM   2031 C  C     . LEU A  1 309 ? -23.780 -62.892 112.211 1.00 42.52 ? 1076 LEU A C     1 
ATOM   2032 O  O     . LEU A  1 309 ? -24.786 -63.118 111.527 1.00 45.75 ? 1076 LEU A O     1 
ATOM   2033 C  CB    . LEU A  1 309 ? -23.071 -60.514 112.151 1.00 49.64 ? 1076 LEU A CB    1 
ATOM   2034 C  CG    . LEU A  1 309 ? -23.331 -59.081 112.532 1.00 52.03 ? 1076 LEU A CG    1 
ATOM   2035 C  CD1   . LEU A  1 309 ? -22.380 -58.178 111.770 1.00 56.05 ? 1076 LEU A CD1   1 
ATOM   2036 C  CD2   . LEU A  1 309 ? -24.762 -58.825 112.110 1.00 54.40 ? 1076 LEU A CD2   1 
ATOM   2037 N  N     . LYS A  1 310 ? -22.727 -63.701 112.199 1.00 38.06 ? 1077 LYS A N     1 
ATOM   2038 C  CA    . LYS A  1 310 ? -22.790 -64.924 111.421 1.00 45.71 ? 1077 LYS A CA    1 
ATOM   2039 C  C     . LYS A  1 310 ? -23.824 -65.862 112.025 1.00 51.36 ? 1077 LYS A C     1 
ATOM   2040 O  O     . LYS A  1 310 ? -24.606 -66.485 111.298 1.00 52.09 ? 1077 LYS A O     1 
ATOM   2041 C  CB    . LYS A  1 310 ? -21.404 -65.576 111.361 1.00 40.97 ? 1077 LYS A CB    1 
ATOM   2042 C  CG    . LYS A  1 310 ? -21.167 -66.469 110.152 1.00 46.15 ? 1077 LYS A CG    1 
ATOM   2043 C  CD    . LYS A  1 310 ? -20.575 -67.820 110.517 1.00 48.78 ? 1077 LYS A CD    1 
ATOM   2044 N  N     . LEU A  1 311 ? -23.846 -65.960 113.358 1.00 41.93 ? 1078 LEU A N     1 
ATOM   2045 C  CA    . LEU A  1 311 ? -24.851 -66.777 114.023 1.00 43.62 ? 1078 LEU A CA    1 
ATOM   2046 C  C     . LEU A  1 311 ? -26.252 -66.215 113.819 1.00 47.93 ? 1078 LEU A C     1 
ATOM   2047 O  O     . LEU A  1 311 ? -27.180 -66.958 113.479 1.00 44.67 ? 1078 LEU A O     1 
ATOM   2048 C  CB    . LEU A  1 311 ? -24.521 -66.870 115.517 1.00 34.87 ? 1078 LEU A CB    1 
ATOM   2049 C  CG    . LEU A  1 311 ? -23.229 -67.631 115.800 1.00 39.14 ? 1078 LEU A CG    1 
ATOM   2050 C  CD1   . LEU A  1 311 ? -22.825 -67.463 117.264 1.00 44.02 ? 1078 LEU A CD1   1 
ATOM   2051 C  CD2   . LEU A  1 311 ? -23.375 -69.116 115.437 1.00 43.64 ? 1078 LEU A CD2   1 
ATOM   2052 N  N     . ALA A  1 312 ? -26.403 -64.896 113.949 1.00 38.08 ? 1079 ALA A N     1 
ATOM   2053 C  CA    . ALA A  1 312 ? -27.693 -64.248 113.729 1.00 43.92 ? 1079 ALA A CA    1 
ATOM   2054 C  C     . ALA A  1 312 ? -28.253 -64.538 112.338 1.00 56.30 ? 1079 ALA A C     1 
ATOM   2055 O  O     . ALA A  1 312 ? -29.434 -64.874 112.186 1.00 62.96 ? 1079 ALA A O     1 
ATOM   2056 C  CB    . ALA A  1 312 ? -27.564 -62.748 113.969 1.00 44.66 ? 1079 ALA A CB    1 
ATOM   2057 N  N     . ASN A  1 313 ? -27.424 -64.388 111.308 1.00 46.52 ? 1080 ASN A N     1 
ATOM   2058 C  CA    . ASN A  1 313 ? -27.860 -64.609 109.936 1.00 51.35 ? 1080 ASN A CA    1 
ATOM   2059 C  C     . ASN A  1 313 ? -28.221 -66.069 109.669 1.00 53.72 ? 1080 ASN A C     1 
ATOM   2060 O  O     . ASN A  1 313 ? -28.891 -66.366 108.674 1.00 55.67 ? 1080 ASN A O     1 
ATOM   2061 C  CB    . ASN A  1 313 ? -26.789 -64.140 108.967 1.00 45.92 ? 1080 ASN A CB    1 
ATOM   2062 C  CG    . ASN A  1 313 ? -26.666 -62.628 108.934 1.00 56.37 ? 1080 ASN A CG    1 
ATOM   2063 O  OD1   . ASN A  1 313 ? -27.657 -61.918 108.757 1.00 70.65 ? 1080 ASN A OD1   1 
ATOM   2064 N  ND2   . ASN A  1 313 ? -25.447 -62.134 109.030 1.00 59.83 ? 1080 ASN A ND2   1 
ATOM   2065 N  N     . GLU A  1 314 ? -27.729 -66.979 110.492 1.00 50.02 ? 1081 GLU A N     1 
ATOM   2066 C  CA    . GLU A  1 314 ? -28.112 -68.375 110.481 1.00 53.55 ? 1081 GLU A CA    1 
ATOM   2067 C  C     . GLU A  1 314 ? -29.378 -68.647 111.284 1.00 54.61 ? 1081 GLU A C     1 
ATOM   2068 O  O     . GLU A  1 314 ? -29.761 -69.812 111.408 1.00 58.60 ? 1081 GLU A O     1 
ATOM   2069 C  CB    . GLU A  1 314 ? -26.962 -69.216 111.041 1.00 58.70 ? 1081 GLU A CB    1 
ATOM   2070 C  CG    . GLU A  1 314 ? -26.081 -69.829 109.979 1.00 61.33 ? 1081 GLU A CG    1 
ATOM   2071 C  CD    . GLU A  1 314 ? -24.620 -69.883 110.400 1.00 65.58 ? 1081 GLU A CD    1 
ATOM   2072 O  OE1   . GLU A  1 314 ? -24.333 -70.360 111.519 1.00 70.44 ? 1081 GLU A OE1   1 
ATOM   2073 O  OE2   . GLU A  1 314 ? -23.754 -69.434 109.621 1.00 76.84 ? 1081 GLU A OE2   1 
ATOM   2074 N  N     . GLY A  1 315 ? -30.017 -67.615 111.832 1.00 55.98 ? 1082 GLY A N     1 
ATOM   2075 C  CA    . GLY A  1 315 ? -31.213 -67.797 112.636 1.00 54.39 ? 1082 GLY A CA    1 
ATOM   2076 C  C     . GLY A  1 315 ? -30.982 -68.388 114.009 1.00 52.57 ? 1082 GLY A C     1 
ATOM   2077 O  O     . GLY A  1 315 ? -31.924 -68.888 114.621 1.00 61.43 ? 1082 GLY A O     1 
ATOM   2078 N  N     . LYS A  1 316 ? -29.758 -68.325 114.526 1.00 44.47 ? 1083 LYS A N     1 
ATOM   2079 C  CA    . LYS A  1 316 ? -29.430 -68.864 115.843 1.00 37.39 ? 1083 LYS A CA    1 
ATOM   2080 C  C     . LYS A  1 316 ? -29.412 -67.745 116.878 1.00 42.73 ? 1083 LYS A C     1 
ATOM   2081 O  O     . LYS A  1 316 ? -28.369 -67.196 117.220 1.00 48.32 ? 1083 LYS A O     1 
ATOM   2082 C  CB    . LYS A  1 316 ? -28.108 -69.620 115.797 1.00 39.03 ? 1083 LYS A CB    1 
ATOM   2083 C  CG    . LYS A  1 316 ? -28.040 -70.657 114.693 1.00 50.94 ? 1083 LYS A CG    1 
ATOM   2084 C  CD    . LYS A  1 316 ? -26.692 -71.355 114.627 1.00 53.49 ? 1083 LYS A CD    1 
ATOM   2085 C  CE    . LYS A  1 316 ? -26.652 -72.318 113.439 1.00 62.03 ? 1083 LYS A CE    1 
ATOM   2086 N  NZ    . LYS A  1 316 ? -25.381 -73.107 113.361 1.00 47.93 ? 1083 LYS A NZ    1 
ATOM   2087 N  N     . VAL A  1 317 ? -30.593 -67.426 117.411 1.00 45.23 ? 1084 VAL A N     1 
ATOM   2088 C  CA    . VAL A  1 317 ? -30.718 -66.243 118.266 1.00 42.39 ? 1084 VAL A CA    1 
ATOM   2089 C  C     . VAL A  1 317 ? -29.946 -66.445 119.569 1.00 44.12 ? 1084 VAL A C     1 
ATOM   2090 O  O     . VAL A  1 317 ? -29.065 -65.649 119.906 1.00 45.18 ? 1084 VAL A O     1 
ATOM   2091 C  CB    . VAL A  1 317 ? -32.197 -65.890 118.508 1.00 48.86 ? 1084 VAL A CB    1 
ATOM   2092 C  CG1   . VAL A  1 317 ? -32.967 -67.047 119.185 1.00 59.42 ? 1084 VAL A CG1   1 
ATOM   2093 C  CG2   . VAL A  1 317 ? -32.281 -64.652 119.362 1.00 45.86 ? 1084 VAL A CG2   1 
ATOM   2094 N  N     . LYS A  1 318 ? -30.262 -67.509 120.317 1.00 43.54 ? 1085 LYS A N     1 
ATOM   2095 C  CA    . LYS A  1 318 ? -29.575 -67.778 121.579 1.00 44.10 ? 1085 LYS A CA    1 
ATOM   2096 C  C     . LYS A  1 318 ? -28.052 -67.823 121.417 1.00 40.07 ? 1085 LYS A C     1 
ATOM   2097 O  O     . LYS A  1 318 ? -27.312 -67.288 122.254 1.00 41.57 ? 1085 LYS A O     1 
ATOM   2098 C  CB    . LYS A  1 318 ? -30.098 -69.083 122.193 1.00 43.66 ? 1085 LYS A CB    1 
ATOM   2099 C  CG    . LYS A  1 318 ? -30.877 -68.854 123.489 1.00 44.35 ? 1085 LYS A CG    1 
ATOM   2100 C  CD    . LYS A  1 318 ? -32.148 -68.082 123.215 1.00 48.07 ? 1085 LYS A CD    1 
ATOM   2101 C  CE    . LYS A  1 318 ? -33.273 -68.431 124.179 1.00 37.46 ? 1085 LYS A CE    1 
ATOM   2102 N  NZ    . LYS A  1 318 ? -32.919 -68.044 125.566 1.00 47.43 ? 1085 LYS A NZ    1 
ATOM   2103 N  N     . GLU A  1 319 ? -27.559 -68.495 120.374 1.00 32.24 ? 1086 GLU A N     1 
ATOM   2104 C  CA    . GLU A  1 319 ? -26.116 -68.551 120.175 1.00 38.74 ? 1086 GLU A CA    1 
ATOM   2105 C  C     . GLU A  1 319 ? -25.545 -67.172 119.839 1.00 42.31 ? 1086 GLU A C     1 
ATOM   2106 O  O     . GLU A  1 319 ? -24.472 -66.802 120.331 1.00 38.13 ? 1086 GLU A O     1 
ATOM   2107 C  CB    . GLU A  1 319 ? -25.771 -69.528 119.055 1.00 40.28 ? 1086 GLU A CB    1 
ATOM   2108 C  CG    . GLU A  1 319 ? -24.553 -70.360 119.315 1.00 54.82 ? 1086 GLU A CG    1 
ATOM   2109 C  CD    . GLU A  1 319 ? -24.685 -71.745 118.714 1.00 67.30 ? 1086 GLU A CD    1 
ATOM   2110 O  OE1   . GLU A  1 319 ? -24.756 -71.826 117.466 1.00 57.20 ? 1086 GLU A OE1   1 
ATOM   2111 O  OE2   . GLU A  1 319 ? -24.753 -72.740 119.484 1.00 65.01 ? 1086 GLU A OE2   1 
ATOM   2112 N  N     . ALA A  1 320 ? -26.292 -66.371 119.077 1.00 33.40 ? 1087 ALA A N     1 
ATOM   2113 C  CA    . ALA A  1 320 ? -25.828 -65.028 118.747 1.00 43.38 ? 1087 ALA A CA    1 
ATOM   2114 C  C     . ALA A  1 320 ? -25.828 -64.132 119.980 1.00 42.88 ? 1087 ALA A C     1 
ATOM   2115 O  O     . ALA A  1 320 ? -24.877 -63.373 120.198 1.00 39.18 ? 1087 ALA A O     1 
ATOM   2116 C  CB    . ALA A  1 320 ? -26.682 -64.429 117.628 1.00 31.77 ? 1087 ALA A CB    1 
ATOM   2117 N  N     . GLN A  1 321 ? -26.860 -64.239 120.827 1.00 39.93 ? 1088 GLN A N     1 
ATOM   2118 C  CA    . GLN A  1 321 ? -26.896 -63.429 122.044 1.00 37.61 ? 1088 GLN A CA    1 
ATOM   2119 C  C     . GLN A  1 321 ? -25.778 -63.806 123.014 1.00 48.30 ? 1088 GLN A C     1 
ATOM   2120 O  O     . GLN A  1 321 ? -25.200 -62.932 123.667 1.00 53.09 ? 1088 GLN A O     1 
ATOM   2121 C  CB    . GLN A  1 321 ? -28.251 -63.577 122.726 1.00 32.99 ? 1088 GLN A CB    1 
ATOM   2122 C  CG    . GLN A  1 321 ? -29.423 -62.993 121.954 1.00 37.15 ? 1088 GLN A CG    1 
ATOM   2123 C  CD    . GLN A  1 321 ? -30.754 -63.337 122.601 1.00 48.88 ? 1088 GLN A CD    1 
ATOM   2124 O  OE1   . GLN A  1 321 ? -31.069 -64.509 122.792 1.00 45.24 ? 1088 GLN A OE1   1 
ATOM   2125 N  NE2   . GLN A  1 321 ? -31.544 -62.318 122.928 1.00 40.96 ? 1088 GLN A NE2   1 
ATOM   2126 N  N     . ALA A  1 322 ? -25.448 -65.094 123.122 1.00 39.16 ? 1089 ALA A N     1 
ATOM   2127 C  CA    . ALA A  1 322 ? -24.319 -65.473 123.966 1.00 47.41 ? 1089 ALA A CA    1 
ATOM   2128 C  C     . ALA A  1 322 ? -23.005 -64.945 123.398 1.00 43.67 ? 1089 ALA A C     1 
ATOM   2129 O  O     . ALA A  1 322 ? -22.133 -64.507 124.153 1.00 50.33 ? 1089 ALA A O     1 
ATOM   2130 C  CB    . ALA A  1 322 ? -24.262 -66.995 124.142 1.00 37.78 ? 1089 ALA A CB    1 
ATOM   2131 N  N     . ALA A  1 323 ? -22.813 -65.057 122.077 1.00 36.99 ? 1090 ALA A N     1 
ATOM   2132 C  CA    . ALA A  1 323 ? -21.635 -64.475 121.434 1.00 41.43 ? 1090 ALA A CA    1 
ATOM   2133 C  C     . ALA A  1 323 ? -21.541 -62.972 121.686 1.00 46.55 ? 1090 ALA A C     1 
ATOM   2134 O  O     . ALA A  1 323 ? -20.445 -62.437 121.892 1.00 40.86 ? 1090 ALA A O     1 
ATOM   2135 C  CB    . ALA A  1 323 ? -21.652 -64.766 119.932 1.00 36.00 ? 1090 ALA A CB    1 
ATOM   2136 N  N     . ALA A  1 324 ? -22.683 -62.277 121.688 1.00 39.45 ? 1091 ALA A N     1 
ATOM   2137 C  CA    . ALA A  1 324 ? -22.666 -60.829 121.848 1.00 46.40 ? 1091 ALA A CA    1 
ATOM   2138 C  C     . ALA A  1 324 ? -22.328 -60.442 123.280 1.00 53.22 ? 1091 ALA A C     1 
ATOM   2139 O  O     . ALA A  1 324 ? -21.830 -59.337 123.516 1.00 47.84 ? 1091 ALA A O     1 
ATOM   2140 C  CB    . ALA A  1 324 ? -24.017 -60.235 121.446 1.00 37.59 ? 1091 ALA A CB    1 
ATOM   2141 N  N     . GLU A  1 325 ? -22.624 -61.321 124.246 1.00 44.67 ? 1092 GLU A N     1 
ATOM   2142 C  CA    . GLU A  1 325 ? -22.238 -61.075 125.634 1.00 46.26 ? 1092 GLU A CA    1 
ATOM   2143 C  C     . GLU A  1 325 ? -20.721 -61.049 125.806 1.00 51.09 ? 1092 GLU A C     1 
ATOM   2144 O  O     . GLU A  1 325 ? -20.199 -60.338 126.674 1.00 53.06 ? 1092 GLU A O     1 
ATOM   2145 C  CB    . GLU A  1 325 ? -22.829 -62.156 126.538 1.00 51.86 ? 1092 GLU A CB    1 
ATOM   2146 C  CG    . GLU A  1 325 ? -24.203 -61.846 127.060 1.00 57.02 ? 1092 GLU A CG    1 
ATOM   2147 C  CD    . GLU A  1 325 ? -24.210 -60.597 127.906 1.00 63.11 ? 1092 GLU A CD    1 
ATOM   2148 O  OE1   . GLU A  1 325 ? -23.318 -60.464 128.771 1.00 71.60 ? 1092 GLU A OE1   1 
ATOM   2149 O  OE2   . GLU A  1 325 ? -25.104 -59.751 127.706 1.00 64.34 ? 1092 GLU A OE2   1 
ATOM   2150 N  N     . GLN A  1 326 ? -20.000 -61.768 124.947 1.00 41.57 ? 1093 GLN A N     1 
ATOM   2151 C  CA    . GLN A  1 326 ? -18.545 -61.764 124.995 1.00 48.71 ? 1093 GLN A CA    1 
ATOM   2152 C  C     . GLN A  1 326 ? -18.005 -60.357 124.789 1.00 53.44 ? 1093 GLN A C     1 
ATOM   2153 O  O     . GLN A  1 326 ? -16.889 -60.042 125.226 1.00 50.18 ? 1093 GLN A O     1 
ATOM   2154 C  CB    . GLN A  1 326 ? -18.008 -62.740 123.946 1.00 50.19 ? 1093 GLN A CB    1 
ATOM   2155 C  CG    . GLN A  1 326 ? -18.716 -64.096 124.066 1.00 55.75 ? 1093 GLN A CG    1 
ATOM   2156 C  CD    . GLN A  1 326 ? -18.615 -64.721 125.458 1.00 55.32 ? 1093 GLN A CD    1 
ATOM   2157 O  OE1   . GLN A  1 326 ? -17.578 -64.652 126.121 1.00 62.02 ? 1093 GLN A OE1   1 
ATOM   2158 N  NE2   . GLN A  1 326 ? -19.720 -65.307 125.920 1.00 57.92 ? 1093 GLN A NE2   1 
ATOM   2159 N  N     . LEU A  1 327 ? -18.752 -59.540 124.040 1.00 45.05 ? 1094 LEU A N     1 
ATOM   2160 C  CA    . LEU A  1 327 ? -18.393 -58.148 123.794 1.00 46.40 ? 1094 LEU A CA    1 
ATOM   2161 C  C     . LEU A  1 327 ? -18.149 -57.386 125.091 1.00 45.07 ? 1094 LEU A C     1 
ATOM   2162 O  O     . LEU A  1 327 ? -17.344 -56.451 125.107 1.00 49.51 ? 1094 LEU A O     1 
ATOM   2163 C  CB    . LEU A  1 327 ? -19.472 -57.457 122.954 1.00 36.83 ? 1094 LEU A CB    1 
ATOM   2164 C  CG    . LEU A  1 327 ? -19.493 -58.007 121.521 1.00 39.48 ? 1094 LEU A CG    1 
ATOM   2165 C  CD1   . LEU A  1 327 ? -20.766 -57.584 120.825 1.00 34.43 ? 1094 LEU A CD1   1 
ATOM   2166 C  CD2   . LEU A  1 327 ? -18.260 -57.578 120.733 1.00 41.42 ? 1094 LEU A CD2   1 
ATOM   2167 N  N     . LYS A  1 328 ? -18.811 -57.776 126.192 1.00 45.81 ? 1095 LYS A N     1 
ATOM   2168 C  CA    . LYS A  1 328 ? -18.679 -57.009 127.425 1.00 47.93 ? 1095 LYS A CA    1 
ATOM   2169 C  C     . LYS A  1 328 ? -17.262 -57.108 127.992 1.00 55.14 ? 1095 LYS A C     1 
ATOM   2170 O  O     . LYS A  1 328 ? -16.751 -56.119 128.528 1.00 53.12 ? 1095 LYS A O     1 
ATOM   2171 C  CB    . LYS A  1 328 ? -19.717 -57.490 128.441 1.00 48.52 ? 1095 LYS A CB    1 
ATOM   2172 C  CG    . LYS A  1 328 ? -21.167 -57.106 128.096 1.00 56.28 ? 1095 LYS A CG    1 
ATOM   2173 C  CD    . LYS A  1 328 ? -22.103 -57.395 129.253 1.00 55.47 ? 1095 LYS A CD    1 
ATOM   2174 C  CE    . LYS A  1 328 ? -23.507 -56.914 128.963 1.00 58.28 ? 1095 LYS A CE    1 
ATOM   2175 N  NZ    . LYS A  1 328 ? -23.893 -57.113 127.542 1.00 58.43 ? 1095 LYS A NZ    1 
ATOM   2176 N  N     . THR A  1 329 ? -16.611 -58.286 127.926 1.00 53.65 ? 1096 THR A N     1 
ATOM   2177 C  CA    . THR A  1 329 ? -15.202 -58.348 128.341 1.00 52.27 ? 1096 THR A CA    1 
ATOM   2178 C  C     . THR A  1 329 ? -14.337 -57.455 127.468 1.00 49.49 ? 1096 THR A C     1 
ATOM   2179 O  O     . THR A  1 329 ? -13.440 -56.777 127.972 1.00 54.41 ? 1096 THR A O     1 
ATOM   2180 C  CB    . THR A  1 329 ? -14.609 -59.785 128.453 1.00 59.52 ? 1096 THR A CB    1 
ATOM   2181 O  OG1   . THR A  1 329 ? -14.100 -60.306 127.195 1.00 59.01 ? 1096 THR A OG1   1 
ATOM   2182 C  CG2   . THR A  1 329 ? -15.425 -60.790 129.432 1.00 61.96 ? 1096 THR A CG2   1 
ATOM   2183 N  N     . THR A  1 330 ? -14.579 -57.439 126.163 1.00 45.59 ? 1097 THR A N     1 
ATOM   2184 C  CA    . THR A  1 330 ? -13.764 -56.571 125.329 1.00 46.47 ? 1097 THR A CA    1 
ATOM   2185 C  C     . THR A  1 330 ? -14.021 -55.108 125.648 1.00 52.49 ? 1097 THR A C     1 
ATOM   2186 O  O     . THR A  1 330 ? -13.080 -54.308 125.702 1.00 47.22 ? 1097 THR A O     1 
ATOM   2187 C  CB    . THR A  1 330 ? -14.058 -56.851 123.864 1.00 44.16 ? 1097 THR A CB    1 
ATOM   2188 O  OG1   . THR A  1 330 ? -13.962 -58.263 123.635 1.00 49.52 ? 1097 THR A OG1   1 
ATOM   2189 C  CG2   . THR A  1 330 ? -13.042 -56.125 122.994 1.00 38.10 ? 1097 THR A CG2   1 
ATOM   2190 N  N     . ARG A  1 331 ? -15.283 -54.747 125.872 1.00 49.19 ? 1098 ARG A N     1 
ATOM   2191 C  CA    . ARG A  1 331 ? -15.605 -53.372 126.235 1.00 53.88 ? 1098 ARG A CA    1 
ATOM   2192 C  C     . ARG A  1 331 ? -14.916 -52.968 127.533 1.00 54.93 ? 1098 ARG A C     1 
ATOM   2193 O  O     . ARG A  1 331 ? -14.336 -51.881 127.624 1.00 51.15 ? 1098 ARG A O     1 
ATOM   2194 C  CB    . ARG A  1 331 ? -17.121 -53.203 126.330 1.00 44.69 ? 1098 ARG A CB    1 
ATOM   2195 C  CG    . ARG A  1 331 ? -17.576 -51.799 126.544 1.00 47.54 ? 1098 ARG A CG    1 
ATOM   2196 C  CD    . ARG A  1 331 ? -18.920 -51.778 127.222 1.00 53.40 ? 1098 ARG A CD    1 
ATOM   2197 N  NE    . ARG A  1 331 ? -18.967 -52.622 128.410 1.00 54.44 ? 1098 ARG A NE    1 
ATOM   2198 C  CZ    . ARG A  1 331 ? -20.088 -53.076 128.953 1.00 52.37 ? 1098 ARG A CZ    1 
ATOM   2199 N  NH1   . ARG A  1 331 ? -21.275 -52.791 128.432 1.00 48.91 ? 1098 ARG A NH1   1 
ATOM   2200 N  NH2   . ARG A  1 331 ? -20.015 -53.850 130.032 1.00 56.55 ? 1098 ARG A NH2   1 
ATOM   2201 N  N     . ASN A  1 332 ? -14.941 -53.843 128.538 1.00 55.12 ? 1099 ASN A N     1 
ATOM   2202 C  CA    . ASN A  1 332 ? -14.362 -53.506 129.833 1.00 54.17 ? 1099 ASN A CA    1 
ATOM   2203 C  C     . ASN A  1 332 ? -12.843 -53.460 129.759 1.00 56.77 ? 1099 ASN A C     1 
ATOM   2204 O  O     . ASN A  1 332 ? -12.217 -52.531 130.278 1.00 64.99 ? 1099 ASN A O     1 
ATOM   2205 C  CB    . ASN A  1 332 ? -14.807 -54.513 130.898 1.00 58.10 ? 1099 ASN A CB    1 
ATOM   2206 C  CG    . ASN A  1 332 ? -16.319 -54.583 131.052 1.00 56.57 ? 1099 ASN A CG    1 
ATOM   2207 O  OD1   . ASN A  1 332 ? -17.047 -53.714 130.578 1.00 56.32 ? 1099 ASN A OD1   1 
ATOM   2208 N  ND2   . ASN A  1 332 ? -16.794 -55.618 131.732 1.00 54.29 ? 1099 ASN A ND2   1 
ATOM   2209 N  N     . ALA A  1 333 ? -12.233 -54.455 129.117 1.00 54.13 ? 1100 ALA A N     1 
ATOM   2210 C  CA    . ALA A  1 333 ? -10.779 -54.581 129.127 1.00 45.46 ? 1100 ALA A CA    1 
ATOM   2211 C  C     . ALA A  1 333 ? -10.079 -53.614 128.183 1.00 51.09 ? 1100 ALA A C     1 
ATOM   2212 O  O     . ALA A  1 333 ? -8.919  -53.273 128.422 1.00 57.43 ? 1100 ALA A O     1 
ATOM   2213 C  CB    . ALA A  1 333 ? -10.375 -56.013 128.774 1.00 51.08 ? 1100 ALA A CB    1 
ATOM   2214 N  N     . TYR A  1 334 ? -10.732 -53.197 127.095 1.00 53.91 ? 1101 TYR A N     1 
ATOM   2215 C  CA    . TYR A  1 334 ? -10.080 -52.385 126.067 1.00 45.45 ? 1101 TYR A CA    1 
ATOM   2216 C  C     . TYR A  1 334 ? -10.835 -51.088 125.804 1.00 52.50 ? 1101 TYR A C     1 
ATOM   2217 O  O     . TYR A  1 334 ? -10.276 -50.007 126.002 1.00 50.05 ? 1101 TYR A O     1 
ATOM   2218 C  CB    . TYR A  1 334 ? -9.937  -53.183 124.765 1.00 47.96 ? 1101 TYR A CB    1 
ATOM   2219 C  CG    . TYR A  1 334 ? -9.075  -54.414 124.892 1.00 59.21 ? 1101 TYR A CG    1 
ATOM   2220 C  CD1   . TYR A  1 334 ? -9.626  -55.621 125.321 1.00 55.04 ? 1101 TYR A CD1   1 
ATOM   2221 C  CD2   . TYR A  1 334 ? -7.721  -54.381 124.582 1.00 55.95 ? 1101 TYR A CD2   1 
ATOM   2222 C  CE1   . TYR A  1 334 ? -8.856  -56.752 125.440 1.00 52.94 ? 1101 TYR A CE1   1 
ATOM   2223 C  CE2   . TYR A  1 334 ? -6.938  -55.515 124.699 1.00 65.01 ? 1101 TYR A CE2   1 
ATOM   2224 C  CZ    . TYR A  1 334 ? -7.513  -56.698 125.130 1.00 60.83 ? 1101 TYR A CZ    1 
ATOM   2225 O  OH    . TYR A  1 334 ? -6.741  -57.831 125.249 1.00 65.40 ? 1101 TYR A OH    1 
ATOM   2226 N  N     . ILE A  1 335 ? -12.089 -51.173 125.352 1.00 46.64 ? 1102 ILE A N     1 
ATOM   2227 C  CA    . ILE A  1 335 ? -12.780 -50.026 124.764 1.00 45.81 ? 1102 ILE A CA    1 
ATOM   2228 C  C     . ILE A  1 335 ? -12.939 -48.909 125.786 1.00 52.78 ? 1102 ILE A C     1 
ATOM   2229 O  O     . ILE A  1 335 ? -12.825 -47.726 125.453 1.00 46.57 ? 1102 ILE A O     1 
ATOM   2230 C  CB    . ILE A  1 335 ? -14.140 -50.450 124.186 1.00 45.10 ? 1102 ILE A CB    1 
ATOM   2231 C  CG1   . ILE A  1 335 ? -13.999 -51.650 123.232 1.00 45.62 ? 1102 ILE A CG1   1 
ATOM   2232 C  CG2   . ILE A  1 335 ? -14.796 -49.279 123.477 1.00 46.96 ? 1102 ILE A CG2   1 
ATOM   2233 C  CD1   . ILE A  1 335 ? -12.703 -51.705 122.387 1.00 50.58 ? 1102 ILE A CD1   1 
ATOM   2234 N  N     . GLN A  1 336 ? -13.259 -49.256 127.030 1.00 45.20 ? 1103 GLN A N     1 
ATOM   2235 C  CA    . GLN A  1 336 ? -13.426 -48.201 128.022 1.00 49.80 ? 1103 GLN A CA    1 
ATOM   2236 C  C     . GLN A  1 336 ? -12.113 -47.474 128.276 1.00 49.54 ? 1103 GLN A C     1 
ATOM   2237 O  O     . GLN A  1 336 ? -12.104 -46.256 128.505 1.00 44.19 ? 1103 GLN A O     1 
ATOM   2238 C  CB    . GLN A  1 336 ? -13.961 -48.787 129.320 1.00 49.10 ? 1103 GLN A CB    1 
ATOM   2239 C  CG    . GLN A  1 336 ? -14.497 -47.717 130.259 1.00 56.50 ? 1103 GLN A CG    1 
ATOM   2240 C  CD    . GLN A  1 336 ? -14.773 -48.254 131.639 1.00 67.23 ? 1103 GLN A CD    1 
ATOM   2241 O  OE1   . GLN A  1 336 ? -15.770 -48.957 131.839 1.00 80.28 ? 1103 GLN A OE1   1 
ATOM   2242 N  NE2   . GLN A  1 336 ? -13.892 -47.954 132.600 1.00 70.71 ? 1103 GLN A NE2   1 
ATOM   2243 N  N     . LYS A  1 337 ? -10.995 -48.196 128.211 1.00 40.46 ? 1104 LYS A N     1 
ATOM   2244 C  CA    . LYS A  1 337 ? -9.687  -47.570 128.349 1.00 46.28 ? 1104 LYS A CA    1 
ATOM   2245 C  C     . LYS A  1 337 ? -9.407  -46.622 127.192 1.00 49.67 ? 1104 LYS A C     1 
ATOM   2246 O  O     . LYS A  1 337 ? -8.875  -45.528 127.401 1.00 49.57 ? 1104 LYS A O     1 
ATOM   2247 C  CB    . LYS A  1 337 ? -8.602  -48.639 128.467 1.00 39.43 ? 1104 LYS A CB    1 
ATOM   2248 N  N     . TYR A  1 338 ? -9.781  -47.004 125.965 1.00 45.40 ? 1105 TYR A N     1 
ATOM   2249 C  CA    . TYR A  1 338 ? -9.591  -46.087 124.843 1.00 42.22 ? 1105 TYR A CA    1 
ATOM   2250 C  C     . TYR A  1 338 ? -10.433 -44.833 125.022 1.00 47.52 ? 1105 TYR A C     1 
ATOM   2251 O  O     . TYR A  1 338 ? -9.927  -43.713 124.882 1.00 45.31 ? 1105 TYR A O     1 
ATOM   2252 C  CB    . TYR A  1 338 ? -9.934  -46.778 123.519 1.00 42.14 ? 1105 TYR A CB    1 
ATOM   2253 N  N     . LEU A  1 339 ? -11.707 -45.003 125.384 1.00 43.14 ? 1106 LEU A N     1 
ATOM   2254 C  CA    . LEU A  1 339 ? -12.586 -43.865 125.636 1.00 47.79 ? 1106 LEU A CA    1 
ATOM   2255 C  C     . LEU A  1 339 ? -12.004 -42.899 126.671 1.00 40.19 ? 1106 LEU A C     1 
ATOM   2256 O  O     . LEU A  1 339 ? -12.008 -41.678 126.456 1.00 39.94 ? 1106 LEU A O     1 
ATOM   2257 C  CB    . LEU A  1 339 ? -13.971 -44.361 126.074 1.00 47.88 ? 1106 LEU A CB    1 
ATOM   2258 C  CG    . LEU A  1 339 ? -14.887 -43.362 126.803 1.00 70.73 ? 1106 LEU A CG    1 
ATOM   2259 C  CD1   . LEU A  1 339 ? -15.560 -42.385 125.835 1.00 64.09 ? 1106 LEU A CD1   1 
ATOM   2260 C  CD2   . LEU A  1 339 ? -15.939 -44.067 127.689 1.00 64.39 ? 1106 LEU A CD2   1 
ATOM   2261 N  N     . GLU A  1 340 ? -11.533 -43.415 127.820 1.00 41.45 ? 219  GLU A N     1 
ATOM   2262 C  CA    . GLU A  1 340 ? -11.027 -42.504 128.850 1.00 40.72 ? 219  GLU A CA    1 
ATOM   2263 C  C     . GLU A  1 340 ? -9.785  -41.751 128.393 1.00 46.44 ? 219  GLU A C     1 
ATOM   2264 O  O     . GLU A  1 340 ? -9.615  -40.571 128.743 1.00 40.89 ? 219  GLU A O     1 
ATOM   2265 C  CB    . GLU A  1 340 ? -10.722 -43.184 130.188 1.00 43.94 ? 219  GLU A CB    1 
ATOM   2266 C  CG    . GLU A  1 340 ? -11.867 -43.840 130.925 1.00 49.38 ? 219  GLU A CG    1 
ATOM   2267 C  CD    . GLU A  1 340 ? -11.424 -45.047 131.749 1.00 69.53 ? 219  GLU A CD    1 
ATOM   2268 O  OE1   . GLU A  1 340 ? -10.265 -45.517 131.609 1.00 67.79 ? 219  GLU A OE1   1 
ATOM   2269 O  OE2   . GLU A  1 340 ? -12.251 -45.510 132.567 1.00 64.25 ? 219  GLU A OE2   1 
ATOM   2270 N  N     . ARG A  1 341 ? -8.902  -42.409 127.633 1.00 38.14 ? 220  ARG A N     1 
ATOM   2271 C  CA    . ARG A  1 341 ? -7.708  -41.723 127.156 1.00 36.45 ? 220  ARG A CA    1 
ATOM   2272 C  C     . ARG A  1 341 ? -8.066  -40.673 126.112 1.00 43.48 ? 220  ARG A C     1 
ATOM   2273 O  O     . ARG A  1 341 ? -7.473  -39.591 126.096 1.00 41.59 ? 220  ARG A O     1 
ATOM   2274 C  CB    . ARG A  1 341 ? -6.706  -42.726 126.596 1.00 41.02 ? 220  ARG A CB    1 
ATOM   2275 N  N     . ALA A  1 342 ? -9.007  -40.985 125.214 1.00 36.13 ? 221  ALA A N     1 
ATOM   2276 C  CA    . ALA A  1 342 ? -9.454  -39.992 124.244 1.00 39.38 ? 221  ALA A CA    1 
ATOM   2277 C  C     . ALA A  1 342 ? -10.091 -38.802 124.941 1.00 39.97 ? 221  ALA A C     1 
ATOM   2278 O  O     . ALA A  1 342 ? -9.838  -37.650 124.572 1.00 38.63 ? 221  ALA A O     1 
ATOM   2279 C  CB    . ALA A  1 342 ? -10.436 -40.601 123.257 1.00 34.19 ? 221  ALA A CB    1 
ATOM   2280 N  N     . ARG A  1 343 ? -10.939 -39.060 125.939 1.00 39.03 ? 222  ARG A N     1 
ATOM   2281 C  CA    . ARG A  1 343 ? -11.507 -37.967 126.717 1.00 38.20 ? 222  ARG A CA    1 
ATOM   2282 C  C     . ARG A  1 343 ? -10.413 -37.154 127.395 1.00 48.07 ? 222  ARG A C     1 
ATOM   2283 O  O     . ARG A  1 343 ? -10.452 -35.918 127.382 1.00 43.72 ? 222  ARG A O     1 
ATOM   2284 C  CB    . ARG A  1 343 ? -12.484 -38.513 127.751 1.00 43.15 ? 222  ARG A CB    1 
ATOM   2285 C  CG    . ARG A  1 343 ? -13.271 -37.442 128.492 1.00 44.72 ? 222  ARG A CG    1 
ATOM   2286 C  CD    . ARG A  1 343 ? -14.114 -38.050 129.594 1.00 59.68 ? 222  ARG A CD    1 
ATOM   2287 N  N     . SER A  1 344 ? -9.408  -37.832 127.955 1.00 41.81 ? 223  SER A N     1 
ATOM   2288 C  CA    . SER A  1 344 ? -8.344  -37.122 128.657 1.00 41.72 ? 223  SER A CA    1 
ATOM   2289 C  C     . SER A  1 344 ? -7.507  -36.279 127.706 1.00 42.51 ? 223  SER A C     1 
ATOM   2290 O  O     . SER A  1 344 ? -7.127  -35.152 128.043 1.00 41.61 ? 223  SER A O     1 
ATOM   2291 C  CB    . SER A  1 344 ? -7.463  -38.122 129.388 1.00 45.55 ? 223  SER A CB    1 
ATOM   2292 O  OG    . SER A  1 344 ? -6.314  -37.481 129.922 1.00 54.17 ? 223  SER A OG    1 
ATOM   2293 N  N     . THR A  1 345 ? -7.275  -36.775 126.490 1.00 34.27 ? 224  THR A N     1 
ATOM   2294 C  CA    . THR A  1 345 ? -6.544  -35.981 125.513 1.00 42.01 ? 224  THR A CA    1 
ATOM   2295 C  C     . THR A  1 345 ? -7.341  -34.756 125.087 1.00 41.97 ? 224  THR A C     1 
ATOM   2296 O  O     . THR A  1 345 ? -6.798  -33.649 125.012 1.00 36.41 ? 224  THR A O     1 
ATOM   2297 C  CB    . THR A  1 345 ? -6.195  -36.850 124.313 1.00 42.15 ? 224  THR A CB    1 
ATOM   2298 O  OG1   . THR A  1 345 ? -5.308  -37.893 124.728 1.00 43.31 ? 224  THR A OG1   1 
ATOM   2299 C  CG2   . THR A  1 345 ? -5.541  -36.012 123.215 1.00 38.60 ? 224  THR A CG2   1 
ATOM   2300 N  N     . LEU A  1 346 ? -8.635  -34.934 124.825 1.00 35.26 ? 225  LEU A N     1 
ATOM   2301 C  CA    . LEU A  1 346 ? -9.477  -33.803 124.444 1.00 37.19 ? 225  LEU A CA    1 
ATOM   2302 C  C     . LEU A  1 346 ? -9.536  -32.769 125.560 1.00 41.86 ? 225  LEU A C     1 
ATOM   2303 O  O     . LEU A  1 346 ? -9.537  -31.561 125.299 1.00 38.62 ? 225  LEU A O     1 
ATOM   2304 C  CB    . LEU A  1 346 ? -10.873 -34.301 124.087 1.00 40.13 ? 225  LEU A CB    1 
ATOM   2305 C  CG    . LEU A  1 346 ? -11.022 -34.850 122.659 1.00 48.11 ? 225  LEU A CG    1 
ATOM   2306 C  CD1   . LEU A  1 346 ? -12.375 -35.528 122.492 1.00 41.50 ? 225  LEU A CD1   1 
ATOM   2307 C  CD2   . LEU A  1 346 ? -10.787 -33.820 121.550 1.00 44.43 ? 225  LEU A CD2   1 
ATOM   2308 N  N     . GLN A  1 347 ? -9.630  -33.228 126.808 1.00 36.44 ? 226  GLN A N     1 
ATOM   2309 C  CA    . GLN A  1 347 ? -9.715  -32.307 127.933 1.00 36.64 ? 226  GLN A CA    1 
ATOM   2310 C  C     . GLN A  1 347 ? -8.428  -31.513 128.107 1.00 40.62 ? 226  GLN A C     1 
ATOM   2311 O  O     . GLN A  1 347 ? -8.469  -30.325 128.472 1.00 31.87 ? 226  GLN A O     1 
ATOM   2312 C  CB    . GLN A  1 347 ? -10.087 -33.103 129.178 1.00 41.03 ? 226  GLN A CB    1 
ATOM   2313 C  CG    . GLN A  1 347 ? -11.580 -33.029 129.411 1.00 44.87 ? 226  GLN A CG    1 
ATOM   2314 C  CD    . GLN A  1 347 ? -12.116 -34.250 130.148 1.00 71.98 ? 226  GLN A CD    1 
ATOM   2315 O  OE1   . GLN A  1 347 ? -13.297 -34.589 130.032 1.00 62.12 ? 226  GLN A OE1   1 
ATOM   2316 N  NE2   . GLN A  1 347 ? -11.248 -34.919 130.904 1.00 67.81 ? 226  GLN A NE2   1 
ATOM   2317 N  N     . LYS A  1 348 ? -7.285  -32.152 127.809 1.00 33.36 ? 227  LYS A N     1 
ATOM   2318 C  CA    . LYS A  1 348 ? -5.991  -31.476 127.845 1.00 40.06 ? 227  LYS A CA    1 
ATOM   2319 C  C     . LYS A  1 348 ? -5.879  -30.447 126.727 1.00 33.90 ? 227  LYS A C     1 
ATOM   2320 O  O     . LYS A  1 348 ? -5.307  -29.364 126.910 1.00 35.22 ? 227  LYS A O     1 
ATOM   2321 C  CB    . LYS A  1 348 ? -4.888  -32.519 127.722 1.00 32.32 ? 227  LYS A CB    1 
ATOM   2322 C  CG    . LYS A  1 348 ? -4.426  -33.025 129.042 1.00 39.87 ? 227  LYS A CG    1 
ATOM   2323 C  CD    . LYS A  1 348 ? -3.391  -34.116 128.885 1.00 48.92 ? 227  LYS A CD    1 
ATOM   2324 C  CE    . LYS A  1 348 ? -2.967  -34.606 130.267 1.00 70.17 ? 227  LYS A CE    1 
ATOM   2325 N  NZ    . LYS A  1 348 ? -3.411  -36.019 130.503 1.00 63.16 ? 227  LYS A NZ    1 
ATOM   2326 N  N     . GLU A  1 349 ? -6.434  -30.760 125.566 1.00 34.13 ? 228  GLU A N     1 
ATOM   2327 C  CA    . GLU A  1 349 ? -6.476  -29.784 124.484 1.00 34.64 ? 228  GLU A CA    1 
ATOM   2328 C  C     . GLU A  1 349 ? -7.377  -28.597 124.839 1.00 37.37 ? 228  GLU A C     1 
ATOM   2329 O  O     . GLU A  1 349 ? -7.043  -27.447 124.515 1.00 33.49 ? 228  GLU A O     1 
ATOM   2330 C  CB    . GLU A  1 349 ? -6.932  -30.451 123.189 1.00 38.92 ? 228  GLU A CB    1 
ATOM   2331 C  CG    . GLU A  1 349 ? -5.784  -31.065 122.404 1.00 40.76 ? 228  GLU A CG    1 
ATOM   2332 C  CD    . GLU A  1 349 ? -6.244  -31.710 121.104 1.00 48.82 ? 228  GLU A CD    1 
ATOM   2333 O  OE1   . GLU A  1 349 ? -6.766  -32.849 121.153 1.00 43.59 ? 228  GLU A OE1   1 
ATOM   2334 O  OE2   . GLU A  1 349 ? -6.102  -31.070 120.037 1.00 41.89 ? 228  GLU A OE2   1 
ATOM   2335 N  N     . VAL A  1 350 ? -8.540  -28.848 125.464 1.00 31.48 ? 229  VAL A N     1 
ATOM   2336 C  CA    . VAL A  1 350 ? -9.372  -27.734 125.930 1.00 32.68 ? 229  VAL A CA    1 
ATOM   2337 C  C     . VAL A  1 350 ? -8.601  -26.876 126.928 1.00 33.23 ? 229  VAL A C     1 
ATOM   2338 O  O     . VAL A  1 350 ? -8.626  -25.644 126.850 1.00 32.43 ? 229  VAL A O     1 
ATOM   2339 C  CB    . VAL A  1 350 ? -10.685 -28.244 126.534 1.00 32.91 ? 229  VAL A CB    1 
ATOM   2340 C  CG1   . VAL A  1 350 ? -11.469 -27.079 127.144 1.00 31.48 ? 229  VAL A CG1   1 
ATOM   2341 C  CG2   . VAL A  1 350 ? -11.497 -28.962 125.487 1.00 41.22 ? 229  VAL A CG2   1 
ATOM   2342 N  N     . HIS A  1 351 ? -7.895  -27.512 127.874 1.00 29.27 ? 230  HIS A N     1 
ATOM   2343 C  CA    . HIS A  1 351 ? -7.149  -26.759 128.878 1.00 34.04 ? 230  HIS A CA    1 
ATOM   2344 C  C     . HIS A  1 351 ? -6.042  -25.931 128.250 1.00 37.77 ? 230  HIS A C     1 
ATOM   2345 O  O     . HIS A  1 351 ? -5.880  -24.745 128.574 1.00 31.61 ? 230  HIS A O     1 
ATOM   2346 C  CB    . HIS A  1 351 ? -6.526  -27.716 129.898 1.00 38.07 ? 230  HIS A CB    1 
ATOM   2347 C  CG    . HIS A  1 351 ? -5.824  -27.021 131.031 1.00 47.89 ? 230  HIS A CG    1 
ATOM   2348 N  ND1   . HIS A  1 351 ? -6.451  -26.604 132.187 1.00 53.16 ? 230  HIS A ND1   1 
ATOM   2349 C  CD2   . HIS A  1 351 ? -4.518  -26.679 131.168 1.00 47.57 ? 230  HIS A CD2   1 
ATOM   2350 C  CE1   . HIS A  1 351 ? -5.563  -26.031 132.984 1.00 53.19 ? 230  HIS A CE1   1 
ATOM   2351 N  NE2   . HIS A  1 351 ? -4.383  -26.067 132.390 1.00 52.60 ? 230  HIS A NE2   1 
ATOM   2352 N  N     . ALA A  1 352 ? -5.336  -26.508 127.275 1.00 29.57 ? 231  ALA A N     1 
ATOM   2353 C  CA    . ALA A  1 352 ? -4.265  -25.768 126.626 1.00 39.85 ? 231  ALA A CA    1 
ATOM   2354 C  C     . ALA A  1 352 ? -4.823  -24.639 125.763 1.00 34.09 ? 231  ALA A C     1 
ATOM   2355 O  O     . ALA A  1 352 ? -4.241  -23.543 125.730 1.00 34.70 ? 231  ALA A O     1 
ATOM   2356 C  CB    . ALA A  1 352 ? -3.392  -26.723 125.807 1.00 29.77 ? 231  ALA A CB    1 
ATOM   2357 N  N     . ALA A  1 353 ? -5.965  -24.868 125.091 1.00 28.57 ? 232  ALA A N     1 
ATOM   2358 C  CA    . ALA A  1 353 ? -6.570  -23.799 124.303 1.00 30.66 ? 232  ALA A CA    1 
ATOM   2359 C  C     . ALA A  1 353 ? -7.078  -22.683 125.200 1.00 29.14 ? 232  ALA A C     1 
ATOM   2360 O  O     . ALA A  1 353 ? -6.975  -21.505 124.837 1.00 29.91 ? 232  ALA A O     1 
ATOM   2361 C  CB    . ALA A  1 353 ? -7.698  -24.331 123.420 1.00 27.38 ? 232  ALA A CB    1 
ATOM   2362 N  N     . LYS A  1 354 ? -7.602  -23.025 126.388 1.00 26.96 ? 233  LYS A N     1 
ATOM   2363 C  CA    . LYS A  1 354 ? -8.008  -21.981 127.326 1.00 28.34 ? 233  LYS A CA    1 
ATOM   2364 C  C     . LYS A  1 354 ? -6.815  -21.147 127.777 1.00 29.18 ? 233  LYS A C     1 
ATOM   2365 O  O     . LYS A  1 354 ? -6.931  -19.922 127.920 1.00 27.77 ? 233  LYS A O     1 
ATOM   2366 C  CB    . LYS A  1 354 ? -8.738  -22.569 128.535 1.00 34.09 ? 233  LYS A CB    1 
ATOM   2367 C  CG    . LYS A  1 354 ? -10.257 -22.437 128.449 1.00 44.52 ? 233  LYS A CG    1 
ATOM   2368 C  CD    . LYS A  1 354 ? -11.032 -23.701 128.827 1.00 52.15 ? 233  LYS A CD    1 
ATOM   2369 C  CE    . LYS A  1 354 ? -12.564 -23.457 128.932 1.00 63.04 ? 233  LYS A CE    1 
ATOM   2370 N  NZ    . LYS A  1 354 ? -13.283 -23.033 127.668 1.00 60.59 ? 233  LYS A NZ    1 
ATOM   2371 N  N     . SER A  1 355 ? -5.675  -21.792 128.036 1.00 28.38 ? 234  SER A N     1 
ATOM   2372 C  CA    . SER A  1 355 ? -4.484  -21.054 128.440 1.00 26.82 ? 234  SER A CA    1 
ATOM   2373 C  C     . SER A  1 355 ? -4.037  -20.076 127.354 1.00 30.23 ? 234  SER A C     1 
ATOM   2374 O  O     . SER A  1 355 ? -3.741  -18.910 127.638 1.00 30.90 ? 234  SER A O     1 
ATOM   2375 C  CB    . SER A  1 355 ? -3.368  -22.033 128.796 1.00 25.95 ? 234  SER A CB    1 
ATOM   2376 O  OG    . SER A  1 355 ? -3.785  -22.858 129.868 1.00 32.51 ? 234  SER A OG    1 
ATOM   2377 N  N     . ALA A  1 356 ? -4.005  -20.534 126.101 1.00 28.60 ? 235  ALA A N     1 
ATOM   2378 C  CA    . ALA A  1 356 ? -3.642  -19.667 124.989 1.00 29.80 ? 235  ALA A CA    1 
ATOM   2379 C  C     . ALA A  1 356 ? -4.652  -18.536 124.814 1.00 31.74 ? 235  ALA A C     1 
ATOM   2380 O  O     . ALA A  1 356 ? -4.276  -17.398 124.496 1.00 25.26 ? 235  ALA A O     1 
ATOM   2381 C  CB    . ALA A  1 356 ? -3.517  -20.488 123.707 1.00 25.05 ? 235  ALA A CB    1 
ATOM   2382 N  N     . ALA A  1 357 ? -5.944  -18.838 124.978 1.00 25.01 ? 236  ALA A N     1 
ATOM   2383 C  CA    . ALA A  1 357 ? -6.959  -17.802 124.831 1.00 26.07 ? 236  ALA A CA    1 
ATOM   2384 C  C     . ALA A  1 357 ? -6.832  -16.744 125.922 1.00 24.77 ? 236  ALA A C     1 
ATOM   2385 O  O     . ALA A  1 357 ? -7.081  -15.560 125.668 1.00 22.08 ? 236  ALA A O     1 
ATOM   2386 C  CB    . ALA A  1 357 ? -8.368  -18.419 124.855 1.00 27.71 ? 236  ALA A CB    1 
ATOM   2387 N  N     . ILE A  1 358 ? -6.458  -17.151 127.140 1.00 21.54 ? 237  ILE A N     1 
ATOM   2388 C  CA    . ILE A  1 358 ? -6.237  -16.182 128.214 1.00 22.72 ? 237  ILE A CA    1 
ATOM   2389 C  C     . ILE A  1 358 ? -5.131  -15.203 127.843 1.00 27.11 ? 237  ILE A C     1 
ATOM   2390 O  O     . ILE A  1 358 ? -5.257  -13.994 128.075 1.00 23.57 ? 237  ILE A O     1 
ATOM   2391 C  CB    . ILE A  1 358 ? -5.945  -16.898 129.540 1.00 22.47 ? 237  ILE A CB    1 
ATOM   2392 C  CG1   . ILE A  1 358 ? -7.220  -17.586 130.041 1.00 22.98 ? 237  ILE A CG1   1 
ATOM   2393 C  CG2   . ILE A  1 358 ? -5.387  -15.918 130.582 1.00 24.60 ? 237  ILE A CG2   1 
ATOM   2394 C  CD1   . ILE A  1 358 ? -6.958  -18.563 131.171 1.00 32.16 ? 237  ILE A CD1   1 
ATOM   2395 N  N     . ILE A  1 359 ? -4.035  -15.715 127.262 1.00 20.46 ? 238  ILE A N     1 
ATOM   2396 C  CA    . ILE A  1 359 ? -2.926  -14.883 126.806 1.00 24.28 ? 238  ILE A CA    1 
ATOM   2397 C  C     . ILE A  1 359 ? -3.392  -13.877 125.759 1.00 25.53 ? 238  ILE A C     1 
ATOM   2398 O  O     . ILE A  1 359 ? -3.032  -12.690 125.800 1.00 22.65 ? 238  ILE A O     1 
ATOM   2399 C  CB    . ILE A  1 359 ? -1.807  -15.776 126.245 1.00 29.40 ? 238  ILE A CB    1 
ATOM   2400 C  CG1   . ILE A  1 359 ? -1.289  -16.729 127.331 1.00 28.80 ? 238  ILE A CG1   1 
ATOM   2401 C  CG2   . ILE A  1 359 ? -0.718  -14.914 125.630 1.00 24.32 ? 238  ILE A CG2   1 
ATOM   2402 C  CD1   . ILE A  1 359 ? -0.309  -16.097 128.254 1.00 34.65 ? 238  ILE A CD1   1 
ATOM   2403 N  N     . ALA A  1 360 ? -4.135  -14.353 124.758 1.00 20.98 ? 239  ALA A N     1 
ATOM   2404 C  CA    . ALA A  1 360 ? -4.672  -13.452 123.744 1.00 24.83 ? 239  ALA A CA    1 
ATOM   2405 C  C     . ALA A  1 360 ? -5.638  -12.441 124.358 1.00 23.73 ? 239  ALA A C     1 
ATOM   2406 O  O     . ALA A  1 360 ? -5.650  -11.276 123.967 1.00 19.40 ? 239  ALA A O     1 
ATOM   2407 C  CB    . ALA A  1 360 ? -5.337  -14.251 122.621 1.00 23.77 ? 239  ALA A CB    1 
ATOM   2408 N  N     . GLY A  1 361 ? -6.463  -12.866 125.314 1.00 22.99 ? 240  GLY A N     1 
ATOM   2409 C  CA    . GLY A  1 361 ? -7.377  -11.926 125.933 1.00 23.65 ? 240  GLY A CA    1 
ATOM   2410 C  C     . GLY A  1 361 ? -6.670  -10.875 126.770 1.00 24.30 ? 240  GLY A C     1 
ATOM   2411 O  O     . GLY A  1 361 ? -7.087  -9.718  126.794 1.00 21.55 ? 240  GLY A O     1 
ATOM   2412 N  N     . LEU A  1 362 ? -5.582  -11.255 127.452 1.00 20.87 ? 241  LEU A N     1 
ATOM   2413 C  CA    . LEU A  1 362 ? -4.827  -10.277 128.233 1.00 19.79 ? 241  LEU A CA    1 
ATOM   2414 C  C     . LEU A  1 362 ? -4.105  -9.287  127.333 1.00 20.36 ? 241  LEU A C     1 
ATOM   2415 O  O     . LEU A  1 362 ? -3.951  -8.116  127.696 1.00 21.25 ? 241  LEU A O     1 
ATOM   2416 C  CB    . LEU A  1 362 ? -3.836  -10.971 129.167 1.00 23.64 ? 241  LEU A CB    1 
ATOM   2417 C  CG    . LEU A  1 362 ? -4.515  -11.626 130.385 1.00 25.27 ? 241  LEU A CG    1 
ATOM   2418 C  CD1   . LEU A  1 362 ? -3.531  -12.468 131.158 1.00 26.13 ? 241  LEU A CD1   1 
ATOM   2419 C  CD2   . LEU A  1 362 ? -5.131  -10.572 131.313 1.00 28.96 ? 241  LEU A CD2   1 
ATOM   2420 N  N     . PHE A  1 363 ? -3.638  -9.733  126.170 1.00 18.85 ? 242  PHE A N     1 
ATOM   2421 C  CA    . PHE A  1 363 ? -3.105  -8.771  125.212 1.00 19.90 ? 242  PHE A CA    1 
ATOM   2422 C  C     . PHE A  1 363 ? -4.175  -7.740  124.866 1.00 18.68 ? 242  PHE A C     1 
ATOM   2423 O  O     . PHE A  1 363 ? -3.927  -6.527  124.896 1.00 17.85 ? 242  PHE A O     1 
ATOM   2424 C  CB    . PHE A  1 363 ? -2.598  -9.504  123.955 1.00 20.18 ? 242  PHE A CB    1 
ATOM   2425 C  CG    . PHE A  1 363 ? -2.026  -8.575  122.903 1.00 20.67 ? 242  PHE A CG    1 
ATOM   2426 C  CD1   . PHE A  1 363 ? -2.868  -7.875  122.049 1.00 20.31 ? 242  PHE A CD1   1 
ATOM   2427 C  CD2   . PHE A  1 363 ? -0.653  -8.389  122.787 1.00 20.35 ? 242  PHE A CD2   1 
ATOM   2428 C  CE1   . PHE A  1 363 ? -2.353  -6.996  121.083 1.00 20.09 ? 242  PHE A CE1   1 
ATOM   2429 C  CE2   . PHE A  1 363 ? -0.133  -7.537  121.815 1.00 20.09 ? 242  PHE A CE2   1 
ATOM   2430 C  CZ    . PHE A  1 363 ? -0.990  -6.825  120.980 1.00 18.82 ? 242  PHE A CZ    1 
ATOM   2431 N  N     . ALA A  1 364 ? -5.397  -8.202  124.567 1.00 18.02 ? 243  ALA A N     1 
ATOM   2432 C  CA    . ALA A  1 364 ? -6.463  -7.254  124.244 1.00 18.79 ? 243  ALA A CA    1 
ATOM   2433 C  C     . ALA A  1 364 ? -6.767  -6.330  125.433 1.00 19.38 ? 243  ALA A C     1 
ATOM   2434 O  O     . ALA A  1 364 ? -6.922  -5.117  125.267 1.00 22.15 ? 243  ALA A O     1 
ATOM   2435 C  CB    . ALA A  1 364 ? -7.717  -8.011  123.797 1.00 23.87 ? 243  ALA A CB    1 
ATOM   2436 N  N     . LEU A  1 365 ? -6.820  -6.864  126.648 1.00 20.09 ? 244  LEU A N     1 
ATOM   2437 C  CA    A LEU A  1 365 ? -7.160  -6.028  127.798 0.62 20.42 ? 244  LEU A CA    1 
ATOM   2438 C  CA    B LEU A  1 365 ? -7.172  -6.009  127.777 0.38 20.45 ? 244  LEU A CA    1 
ATOM   2439 C  C     . LEU A  1 365 ? -6.087  -4.974  128.064 1.00 23.69 ? 244  LEU A C     1 
ATOM   2440 O  O     . LEU A  1 365 ? -6.393  -3.845  128.464 1.00 19.62 ? 244  LEU A O     1 
ATOM   2441 C  CB    A LEU A  1 365 ? -7.377  -6.915  129.033 0.62 24.44 ? 244  LEU A CB    1 
ATOM   2442 C  CB    B LEU A  1 365 ? -7.446  -6.853  129.019 0.38 24.41 ? 244  LEU A CB    1 
ATOM   2443 C  CG    A LEU A  1 365 ? -7.942  -6.310  130.322 0.62 25.70 ? 244  LEU A CG    1 
ATOM   2444 C  CG    B LEU A  1 365 ? -8.772  -7.603  128.980 0.38 21.67 ? 244  LEU A CG    1 
ATOM   2445 C  CD1   A LEU A  1 365 ? -9.419  -6.010  130.172 0.62 25.68 ? 244  LEU A CD1   1 
ATOM   2446 C  CD1   B LEU A  1 365 ? -8.889  -8.456  130.223 0.38 18.83 ? 244  LEU A CD1   1 
ATOM   2447 C  CD2   A LEU A  1 365 ? -7.713  -7.309  131.476 0.62 22.43 ? 244  LEU A CD2   1 
ATOM   2448 C  CD2   B LEU A  1 365 ? -9.927  -6.612  128.844 0.38 23.05 ? 244  LEU A CD2   1 
ATOM   2449 N  N     . CYS A  1 366 ? -4.822  -5.323  127.852 1.00 18.60 ? 245  CYS A N     1 
ATOM   2450 C  CA    . CYS A  1 366 ? -3.742  -4.380  128.133 1.00 21.27 ? 245  CYS A CA    1 
ATOM   2451 C  C     . CYS A  1 366 ? -3.591  -3.313  127.044 1.00 18.92 ? 245  CYS A C     1 
ATOM   2452 O  O     . CYS A  1 366 ? -3.122  -2.208  127.336 1.00 19.18 ? 245  CYS A O     1 
ATOM   2453 C  CB    . CYS A  1 366 ? -2.419  -5.132  128.292 1.00 21.58 ? 245  CYS A CB    1 
ATOM   2454 S  SG    . CYS A  1 366 ? -2.334  -6.182  129.804 1.00 25.20 ? 245  CYS A SG    1 
ATOM   2455 N  N     . TRP A  1 367 ? -3.906  -3.631  125.790 1.00 17.13 ? 246  TRP A N     1 
ATOM   2456 C  CA    . TRP A  1 367 ? -3.692  -2.662  124.709 1.00 16.71 ? 246  TRP A CA    1 
ATOM   2457 C  C     . TRP A  1 367 ? -4.913  -1.839  124.354 1.00 18.68 ? 246  TRP A C     1 
ATOM   2458 O  O     . TRP A  1 367 ? -4.765  -0.736  123.811 1.00 15.99 ? 246  TRP A O     1 
ATOM   2459 C  CB    . TRP A  1 367 ? -3.222  -3.388  123.448 1.00 18.79 ? 246  TRP A CB    1 
ATOM   2460 C  CG    . TRP A  1 367 ? -1.803  -3.744  123.509 1.00 19.92 ? 246  TRP A CG    1 
ATOM   2461 C  CD1   . TRP A  1 367 ? -1.252  -4.923  123.904 1.00 22.09 ? 246  TRP A CD1   1 
ATOM   2462 C  CD2   . TRP A  1 367 ? -0.733  -2.896  123.112 1.00 20.20 ? 246  TRP A CD2   1 
ATOM   2463 N  NE1   . TRP A  1 367 ? 0.127   -4.851  123.801 1.00 22.12 ? 246  TRP A NE1   1 
ATOM   2464 C  CE2   . TRP A  1 367 ? 0.462   -3.610  123.307 1.00 24.03 ? 246  TRP A CE2   1 
ATOM   2465 C  CE3   . TRP A  1 367 ? -0.676  -1.589  122.619 1.00 20.65 ? 246  TRP A CE3   1 
ATOM   2466 C  CZ2   . TRP A  1 367 ? 1.715   -3.054  123.045 1.00 21.93 ? 246  TRP A CZ2   1 
ATOM   2467 C  CZ3   . TRP A  1 367 ? 0.581   -1.036  122.338 1.00 26.80 ? 246  TRP A CZ3   1 
ATOM   2468 C  CH2   . TRP A  1 367 ? 1.751   -1.776  122.549 1.00 24.06 ? 246  TRP A CH2   1 
ATOM   2469 N  N     . LEU A  1 368 ? -6.115  -2.363  124.598 1.00 16.61 ? 247  LEU A N     1 
ATOM   2470 C  CA    . LEU A  1 368 ? -7.324  -1.651  124.185 1.00 17.98 ? 247  LEU A CA    1 
ATOM   2471 C  C     . LEU A  1 368 ? -7.457  -0.267  124.816 1.00 19.68 ? 247  LEU A C     1 
ATOM   2472 O  O     . LEU A  1 368 ? -7.956  0.648   124.129 1.00 19.59 ? 247  LEU A O     1 
ATOM   2473 C  CB    . LEU A  1 368 ? -8.569  -2.505  124.490 1.00 22.62 ? 247  LEU A CB    1 
ATOM   2474 C  CG    . LEU A  1 368 ? -8.938  -3.528  123.404 1.00 25.71 ? 247  LEU A CG    1 
ATOM   2475 C  CD1   . LEU A  1 368 ? -10.026 -4.503  123.938 1.00 27.61 ? 247  LEU A CD1   1 
ATOM   2476 C  CD2   . LEU A  1 368 ? -9.375  -2.845  122.120 1.00 24.21 ? 247  LEU A CD2   1 
ATOM   2477 N  N     . PRO A  1 369 ? -7.112  -0.044  126.095 1.00 18.91 ? 248  PRO A N     1 
ATOM   2478 C  CA    . PRO A  1 369 ? -7.324  1.306   126.641 1.00 16.58 ? 248  PRO A CA    1 
ATOM   2479 C  C     . PRO A  1 369 ? -6.584  2.368   125.849 1.00 16.38 ? 248  PRO A C     1 
ATOM   2480 O  O     . PRO A  1 369 ? -7.175  3.402   125.509 1.00 17.24 ? 248  PRO A O     1 
ATOM   2481 C  CB    . PRO A  1 369 ? -6.785  1.176   128.068 1.00 19.06 ? 248  PRO A CB    1 
ATOM   2482 C  CG    . PRO A  1 369 ? -7.059  -0.273  128.416 1.00 19.98 ? 248  PRO A CG    1 
ATOM   2483 C  CD    . PRO A  1 369 ? -6.677  -0.984  127.153 1.00 17.51 ? 248  PRO A CD    1 
ATOM   2484 N  N     . LEU A  1 370 ? -5.306  2.128   125.517 1.00 15.68 ? 249  LEU A N     1 
ATOM   2485 C  CA    . LEU A  1 370 ? -4.557  3.104   124.734 1.00 15.01 ? 249  LEU A CA    1 
ATOM   2486 C  C     . LEU A  1 370 ? -5.167  3.283   123.350 1.00 18.02 ? 249  LEU A C     1 
ATOM   2487 O  O     . LEU A  1 370 ? -5.334  4.409   122.887 1.00 17.52 ? 249  LEU A O     1 
ATOM   2488 C  CB    . LEU A  1 370 ? -3.082  2.690   124.607 1.00 21.14 ? 249  LEU A CB    1 
ATOM   2489 C  CG    . LEU A  1 370 ? -2.051  3.718   124.090 1.00 21.44 ? 249  LEU A CG    1 
ATOM   2490 C  CD1   . LEU A  1 370 ? -2.107  5.136   124.740 1.00 20.26 ? 249  LEU A CD1   1 
ATOM   2491 C  CD2   . LEU A  1 370 ? -0.640  3.152   124.213 1.00 18.60 ? 249  LEU A CD2   1 
ATOM   2492 N  N     . HIS A  1 371 ? -5.554  2.185   122.692 1.00 14.61 ? 250  HIS A N     1 
ATOM   2493 C  CA    . HIS A  1 371 ? -6.192  2.330   121.381 1.00 18.06 ? 250  HIS A CA    1 
ATOM   2494 C  C     . HIS A  1 371 ? -7.507  3.097   121.489 1.00 20.37 ? 250  HIS A C     1 
ATOM   2495 O  O     . HIS A  1 371 ? -7.833  3.918   120.622 1.00 15.40 ? 250  HIS A O     1 
ATOM   2496 C  CB    . HIS A  1 371 ? -6.413  0.960   120.730 1.00 15.55 ? 250  HIS A CB    1 
ATOM   2497 C  CG    . HIS A  1 371 ? -5.154  0.332   120.220 1.00 19.03 ? 250  HIS A CG    1 
ATOM   2498 N  ND1   . HIS A  1 371 ? -4.410  0.883   119.194 1.00 18.20 ? 250  HIS A ND1   1 
ATOM   2499 C  CD2   . HIS A  1 371 ? -4.551  -0.840  120.535 1.00 20.96 ? 250  HIS A CD2   1 
ATOM   2500 C  CE1   . HIS A  1 371 ? -3.370  0.108   118.943 1.00 19.58 ? 250  HIS A CE1   1 
ATOM   2501 N  NE2   . HIS A  1 371 ? -3.427  -0.940  119.750 1.00 21.92 ? 250  HIS A NE2   1 
ATOM   2502 N  N     . ILE A  1 372 ? -8.303  2.795   122.510 1.00 14.78 ? 251  ILE A N     1 
ATOM   2503 C  CA    . ILE A  1 372 ? -9.571  3.490   122.699 1.00 15.01 ? 251  ILE A CA    1 
ATOM   2504 C  C     . ILE A  1 372 ? -9.344  4.972   122.940 1.00 14.74 ? 251  ILE A C     1 
ATOM   2505 O  O     . ILE A  1 372 ? -10.086 5.819   122.437 1.00 15.76 ? 251  ILE A O     1 
ATOM   2506 C  CB    . ILE A  1 372 ? -10.370 2.842   123.841 1.00 18.30 ? 251  ILE A CB    1 
ATOM   2507 C  CG1   . ILE A  1 372 ? -10.801 1.420   123.429 1.00 16.02 ? 251  ILE A CG1   1 
ATOM   2508 C  CG2   . ILE A  1 372 ? -11.600 3.717   124.159 1.00 18.01 ? 251  ILE A CG2   1 
ATOM   2509 C  CD1   . ILE A  1 372 ? -11.374 0.596   124.588 1.00 19.39 ? 251  ILE A CD1   1 
ATOM   2510 N  N     . ILE A  1 373 ? -8.353  5.317   123.751 1.00 14.12 ? 252  ILE A N     1 
ATOM   2511 C  CA    . ILE A  1 373 ? -8.052  6.731   123.919 1.00 15.24 ? 252  ILE A CA    1 
ATOM   2512 C  C     . ILE A  1 373 ? -7.717  7.385   122.580 1.00 15.46 ? 252  ILE A C     1 
ATOM   2513 O  O     . ILE A  1 373 ? -8.169  8.500   122.290 1.00 17.75 ? 252  ILE A O     1 
ATOM   2514 C  CB    . ILE A  1 373 ? -6.917  6.918   124.944 1.00 19.16 ? 252  ILE A CB    1 
ATOM   2515 C  CG1   . ILE A  1 373 ? -7.404  6.537   126.346 1.00 16.95 ? 252  ILE A CG1   1 
ATOM   2516 C  CG2   . ILE A  1 373 ? -6.363  8.340   124.892 1.00 13.84 ? 252  ILE A CG2   1 
ATOM   2517 C  CD1   . ILE A  1 373 ? -6.244  6.419   127.365 1.00 20.34 ? 252  ILE A CD1   1 
ATOM   2518 N  N     . ASN A  1 374 ? -6.901  6.722   121.756 1.00 18.09 ? 253  ASN A N     1 
ATOM   2519 C  CA    . ASN A  1 374 ? -6.594  7.260   120.434 1.00 16.78 ? 253  ASN A CA    1 
ATOM   2520 C  C     . ASN A  1 374 ? -7.859  7.478   119.624 1.00 15.86 ? 253  ASN A C     1 
ATOM   2521 O  O     . ASN A  1 374 ? -7.965  8.470   118.885 1.00 16.57 ? 253  ASN A O     1 
ATOM   2522 C  CB    . ASN A  1 374 ? -5.628  6.324   119.685 1.00 17.50 ? 253  ASN A CB    1 
ATOM   2523 C  CG    . ASN A  1 374 ? -4.213  6.386   120.262 1.00 21.34 ? 253  ASN A CG    1 
ATOM   2524 O  OD1   . ASN A  1 374 ? -3.879  7.312   120.992 1.00 19.47 ? 253  ASN A OD1   1 
ATOM   2525 N  ND2   . ASN A  1 374 ? -3.366  5.442   119.883 1.00 15.88 ? 253  ASN A ND2   1 
ATOM   2526 N  N     . CYS A  1 375 ? -8.849  6.575   119.763 1.00 15.86 ? 254  CYS A N     1 
ATOM   2527 C  CA    . CYS A  1 375 ? -10.110 6.773   119.039 1.00 15.97 ? 254  CYS A CA    1 
ATOM   2528 C  C     . CYS A  1 375 ? -10.816 8.041   119.516 1.00 14.91 ? 254  CYS A C     1 
ATOM   2529 O  O     . CYS A  1 375 ? -11.331 8.815   118.696 1.00 15.52 ? 254  CYS A O     1 
ATOM   2530 C  CB    . CYS A  1 375 ? -11.039 5.556   119.228 1.00 16.39 ? 254  CYS A CB    1 
ATOM   2531 S  SG    . CYS A  1 375 ? -10.491 4.099   118.331 1.00 19.85 ? 254  CYS A SG    1 
ATOM   2532 N  N     . PHE A  1 376 ? -10.819 8.293   120.837 1.00 14.49 ? 255  PHE A N     1 
ATOM   2533 C  CA    . PHE A  1 376 ? -11.414 9.544   121.330 1.00 16.80 ? 255  PHE A CA    1 
ATOM   2534 C  C     . PHE A  1 376 ? -10.645 10.753  120.800 1.00 20.15 ? 255  PHE A C     1 
ATOM   2535 O  O     . PHE A  1 376 ? -11.257 11.732  120.352 1.00 22.03 ? 255  PHE A O     1 
ATOM   2536 C  CB    . PHE A  1 376 ? -11.453 9.579   122.864 1.00 16.43 ? 255  PHE A CB    1 
ATOM   2537 C  CG    . PHE A  1 376 ? -12.652 8.901   123.446 1.00 19.92 ? 255  PHE A CG    1 
ATOM   2538 C  CD1   . PHE A  1 376 ? -13.846 9.607   123.612 1.00 17.01 ? 255  PHE A CD1   1 
ATOM   2539 C  CD2   . PHE A  1 376 ? -12.610 7.538   123.780 1.00 17.44 ? 255  PHE A CD2   1 
ATOM   2540 C  CE1   . PHE A  1 376 ? -14.984 8.968   124.121 1.00 19.22 ? 255  PHE A CE1   1 
ATOM   2541 C  CE2   . PHE A  1 376 ? -13.736 6.899   124.301 1.00 24.57 ? 255  PHE A CE2   1 
ATOM   2542 C  CZ    . PHE A  1 376 ? -14.931 7.624   124.473 1.00 22.25 ? 255  PHE A CZ    1 
ATOM   2543 N  N     . THR A  1 377 ? -9.303  10.694  120.814 1.00 18.76 ? 256  THR A N     1 
ATOM   2544 C  CA    . THR A  1 377 ? -8.508  11.824  120.320 1.00 19.08 ? 256  THR A CA    1 
ATOM   2545 C  C     . THR A  1 377 ? -8.849  12.102  118.867 1.00 22.00 ? 256  THR A C     1 
ATOM   2546 O  O     . THR A  1 377 ? -9.062  13.257  118.483 1.00 20.96 ? 256  THR A O     1 
ATOM   2547 C  CB    . THR A  1 377 ? -7.012  11.519  120.449 1.00 19.37 ? 256  THR A CB    1 
ATOM   2548 O  OG1   . THR A  1 377 ? -6.689  11.340  121.827 1.00 23.89 ? 256  THR A OG1   1 
ATOM   2549 C  CG2   . THR A  1 377 ? -6.115  12.656  119.840 1.00 18.26 ? 256  THR A CG2   1 
ATOM   2550 N  N     . PHE A  1 378 ? -9.008  11.039  118.071 1.00 13.99 ? 257  PHE A N     1 
ATOM   2551 C  CA    . PHE A  1 378 ? -9.199  11.175  116.630 1.00 20.75 ? 257  PHE A CA    1 
ATOM   2552 C  C     . PHE A  1 378 ? -10.638 11.535  116.263 1.00 21.19 ? 257  PHE A C     1 
ATOM   2553 O  O     . PHE A  1 378 ? -10.881 12.500  115.529 1.00 20.54 ? 257  PHE A O     1 
ATOM   2554 C  CB    . PHE A  1 378 ? -8.796  9.857   115.945 1.00 16.69 ? 257  PHE A CB    1 
ATOM   2555 C  CG    . PHE A  1 378 ? -8.915  9.873   114.446 1.00 21.65 ? 257  PHE A CG    1 
ATOM   2556 C  CD1   . PHE A  1 378 ? -8.137  10.726  113.671 1.00 20.30 ? 257  PHE A CD1   1 
ATOM   2557 C  CD2   . PHE A  1 378 ? -9.753  8.961   113.800 1.00 21.99 ? 257  PHE A CD2   1 
ATOM   2558 C  CE1   . PHE A  1 378 ? -8.239  10.712  112.271 1.00 20.08 ? 257  PHE A CE1   1 
ATOM   2559 C  CE2   . PHE A  1 378 ? -9.859  8.936   112.406 1.00 21.95 ? 257  PHE A CE2   1 
ATOM   2560 C  CZ    . PHE A  1 378 ? -9.094  9.816   111.639 1.00 27.66 ? 257  PHE A CZ    1 
ATOM   2561 N  N     . PHE A  1 379 ? -11.607 10.778  116.790 1.00 18.38 ? 258  PHE A N     1 
ATOM   2562 C  CA    . PHE A  1 379 ? -13.003 10.897  116.377 1.00 21.76 ? 258  PHE A CA    1 
ATOM   2563 C  C     . PHE A  1 379 ? -13.754 12.004  117.093 1.00 24.57 ? 258  PHE A C     1 
ATOM   2564 O  O     . PHE A  1 379 ? -14.815 12.396  116.613 1.00 26.07 ? 258  PHE A O     1 
ATOM   2565 C  CB    . PHE A  1 379 ? -13.757 9.575   116.626 1.00 14.39 ? 258  PHE A CB    1 
ATOM   2566 C  CG    . PHE A  1 379 ? -13.393 8.489   115.678 1.00 16.86 ? 258  PHE A CG    1 
ATOM   2567 C  CD1   . PHE A  1 379 ? -13.494 8.691   114.312 1.00 18.75 ? 258  PHE A CD1   1 
ATOM   2568 C  CD2   . PHE A  1 379 ? -12.953 7.257   116.151 1.00 15.93 ? 258  PHE A CD2   1 
ATOM   2569 C  CE1   . PHE A  1 379 ? -13.161 7.657   113.422 1.00 20.88 ? 258  PHE A CE1   1 
ATOM   2570 C  CE2   . PHE A  1 379 ? -12.631 6.234   115.283 1.00 19.69 ? 258  PHE A CE2   1 
ATOM   2571 C  CZ    . PHE A  1 379 ? -12.725 6.439   113.907 1.00 18.29 ? 258  PHE A CZ    1 
ATOM   2572 N  N     . CYS A  1 380 ? -13.252 12.501  118.225 1.00 26.78 ? 259  CYS A N     1 
ATOM   2573 C  CA    . CYS A  1 380 ? -13.947 13.522  119.010 1.00 25.32 ? 259  CYS A CA    1 
ATOM   2574 C  C     . CYS A  1 380 ? -13.046 14.737  119.194 1.00 30.43 ? 259  CYS A C     1 
ATOM   2575 O  O     . CYS A  1 380 ? -12.551 14.997  120.298 1.00 29.24 ? 259  CYS A O     1 
ATOM   2576 C  CB    . CYS A  1 380 ? -14.398 13.000  120.372 1.00 28.77 ? 259  CYS A CB    1 
ATOM   2577 S  SG    . CYS A  1 380 ? -15.586 14.183  121.120 1.00 38.68 ? 259  CYS A SG    1 
ATOM   2578 N  N     . PRO A  1 381 ? -12.831 15.521  118.135 1.00 31.37 ? 260  PRO A N     1 
ATOM   2579 C  CA    . PRO A  1 381 ? -12.019 16.738  118.281 1.00 35.01 ? 260  PRO A CA    1 
ATOM   2580 C  C     . PRO A  1 381 ? -12.675 17.814  119.132 1.00 36.67 ? 260  PRO A C     1 
ATOM   2581 O  O     . PRO A  1 381 ? -11.981 18.765  119.511 1.00 36.08 ? 260  PRO A O     1 
ATOM   2582 C  CB    . PRO A  1 381 ? -11.839 17.215  116.835 1.00 42.19 ? 260  PRO A CB    1 
ATOM   2583 C  CG    . PRO A  1 381 ? -13.044 16.703  116.125 1.00 33.40 ? 260  PRO A CG    1 
ATOM   2584 C  CD    . PRO A  1 381 ? -13.334 15.356  116.756 1.00 28.55 ? 260  PRO A CD    1 
ATOM   2585 N  N     . ASP A  1 382 ? -13.976 17.706  119.425 1.00 28.15 ? 261  ASP A N     1 
ATOM   2586 C  CA    . ASP A  1 382 ? -14.638 18.571  120.394 1.00 35.80 ? 261  ASP A CA    1 
ATOM   2587 C  C     . ASP A  1 382 ? -14.446 18.126  121.837 1.00 36.60 ? 261  ASP A C     1 
ATOM   2588 O  O     . ASP A  1 382 ? -14.815 18.876  122.742 1.00 35.79 ? 261  ASP A O     1 
ATOM   2589 C  CB    . ASP A  1 382 ? -16.151 18.661  120.126 1.00 40.74 ? 261  ASP A CB    1 
ATOM   2590 C  CG    . ASP A  1 382 ? -16.464 19.172  118.738 1.00 56.71 ? 261  ASP A CG    1 
ATOM   2591 O  OD1   . ASP A  1 382 ? -15.647 19.990  118.261 1.00 57.53 ? 261  ASP A OD1   1 
ATOM   2592 O  OD2   . ASP A  1 382 ? -17.508 18.786  118.140 1.00 63.26 ? 261  ASP A OD2   1 
ATOM   2593 N  N     . CYS A  1 383 ? -13.935 16.925  122.078 1.00 30.19 ? 262  CYS A N     1 
ATOM   2594 C  CA    . CYS A  1 383 ? -13.661 16.435  123.427 1.00 30.36 ? 262  CYS A CA    1 
ATOM   2595 C  C     . CYS A  1 383 ? -12.270 16.889  123.851 1.00 29.81 ? 262  CYS A C     1 
ATOM   2596 O  O     . CYS A  1 383 ? -11.327 16.809  123.065 1.00 32.47 ? 262  CYS A O     1 
ATOM   2597 C  CB    . CYS A  1 383 ? -13.724 14.896  123.470 1.00 35.92 ? 262  CYS A CB    1 
ATOM   2598 S  SG    . CYS A  1 383 ? -15.349 14.106  123.145 1.00 43.64 ? 262  CYS A SG    1 
ATOM   2599 N  N     . SER A  1 384 ? -12.133 17.335  125.096 1.00 25.69 ? 263  SER A N     1 
ATOM   2600 C  CA    . SER A  1 384 ? -10.796 17.538  125.637 1.00 31.26 ? 263  SER A CA    1 
ATOM   2601 C  C     . SER A  1 384 ? -9.970  16.260  125.523 1.00 27.88 ? 263  SER A C     1 
ATOM   2602 O  O     . SER A  1 384 ? -10.476 15.145  125.699 1.00 27.99 ? 263  SER A O     1 
ATOM   2603 C  CB    . SER A  1 384 ? -10.848 17.982  127.104 1.00 34.92 ? 263  SER A CB    1 
ATOM   2604 O  OG    . SER A  1 384 ? -11.593 19.179  127.224 1.00 50.88 ? 263  SER A OG    1 
ATOM   2605 N  N     . HIS A  1 385 ? -8.696  16.441  125.211 1.00 23.31 ? 264  HIS A N     1 
ATOM   2606 C  CA    . HIS A  1 385 ? -7.771  15.321  125.158 1.00 26.99 ? 264  HIS A CA    1 
ATOM   2607 C  C     . HIS A  1 385 ? -7.714  14.634  126.519 1.00 30.00 ? 264  HIS A C     1 
ATOM   2608 O  O     . HIS A  1 385 ? -7.723  15.298  127.558 1.00 24.68 ? 264  HIS A O     1 
ATOM   2609 C  CB    . HIS A  1 385 ? -6.407  15.852  124.742 1.00 23.60 ? 264  HIS A CB    1 
ATOM   2610 C  CG    . HIS A  1 385 ? -5.467  14.806  124.241 1.00 22.48 ? 264  HIS A CG    1 
ATOM   2611 N  ND1   . HIS A  1 385 ? -4.932  13.830  125.059 1.00 25.65 ? 264  HIS A ND1   1 
ATOM   2612 C  CD2   . HIS A  1 385 ? -4.984  14.567  123.000 1.00 22.25 ? 264  HIS A CD2   1 
ATOM   2613 C  CE1   . HIS A  1 385 ? -4.134  13.053  124.346 1.00 26.91 ? 264  HIS A CE1   1 
ATOM   2614 N  NE2   . HIS A  1 385 ? -4.151  13.477  123.093 1.00 24.12 ? 264  HIS A NE2   1 
ATOM   2615 N  N     . ALA A  1 386 ? -7.654  13.299  126.506 1.00 22.41 ? 265  ALA A N     1 
ATOM   2616 C  CA    . ALA A  1 386 ? -7.394  12.548  127.730 1.00 23.59 ? 265  ALA A CA    1 
ATOM   2617 C  C     . ALA A  1 386 ? -6.218  13.171  128.473 1.00 21.11 ? 265  ALA A C     1 
ATOM   2618 O  O     . ALA A  1 386 ? -5.243  13.585  127.838 1.00 19.39 ? 265  ALA A O     1 
ATOM   2619 C  CB    . ALA A  1 386 ? -7.073  11.077  127.431 1.00 20.94 ? 265  ALA A CB    1 
ATOM   2620 N  N     . PRO A  1 387 ? -6.292  13.312  129.796 1.00 19.29 ? 266  PRO A N     1 
ATOM   2621 C  CA    . PRO A  1 387 ? -5.204  13.983  130.515 1.00 24.02 ? 266  PRO A CA    1 
ATOM   2622 C  C     . PRO A  1 387 ? -3.921  13.161  130.471 1.00 29.82 ? 266  PRO A C     1 
ATOM   2623 O  O     . PRO A  1 387 ? -3.925  11.940  130.289 1.00 22.04 ? 266  PRO A O     1 
ATOM   2624 C  CB    . PRO A  1 387 ? -5.748  14.129  131.944 1.00 26.16 ? 266  PRO A CB    1 
ATOM   2625 C  CG    . PRO A  1 387 ? -6.791  13.046  132.071 1.00 28.92 ? 266  PRO A CG    1 
ATOM   2626 C  CD    . PRO A  1 387 ? -7.387  12.893  130.689 1.00 23.85 ? 266  PRO A CD    1 
ATOM   2627 N  N     . LEU A  1 388 ? -2.807  13.869  130.655 1.00 23.82 ? 267  LEU A N     1 
ATOM   2628 C  CA    . LEU A  1 388 ? -1.490  13.247  130.600 1.00 27.22 ? 267  LEU A CA    1 
ATOM   2629 C  C     . LEU A  1 388 ? -1.359  12.070  131.567 1.00 25.06 ? 267  LEU A C     1 
ATOM   2630 O  O     . LEU A  1 388 ? -0.732  11.057  131.225 1.00 20.77 ? 267  LEU A O     1 
ATOM   2631 C  CB    . LEU A  1 388 ? -0.408  14.291  130.895 1.00 33.98 ? 267  LEU A CB    1 
ATOM   2632 C  CG    . LEU A  1 388 ? 1.042   13.801  130.757 1.00 37.14 ? 267  LEU A CG    1 
ATOM   2633 C  CD1   . LEU A  1 388 ? 1.246   13.089  129.413 1.00 36.16 ? 267  LEU A CD1   1 
ATOM   2634 C  CD2   . LEU A  1 388 ? 2.034   14.961  130.947 1.00 31.70 ? 267  LEU A CD2   1 
ATOM   2635 N  N     . TRP A  1 389 ? -1.902  12.186  132.787 1.00 19.56 ? 268  TRP A N     1 
ATOM   2636 C  CA    . TRP A  1 389 ? -1.756  11.075  133.737 1.00 25.36 ? 268  TRP A CA    1 
ATOM   2637 C  C     . TRP A  1 389 ? -2.416  9.812   133.210 1.00 23.32 ? 268  TRP A C     1 
ATOM   2638 O  O     . TRP A  1 389 ? -1.935  8.699   133.472 1.00 18.47 ? 268  TRP A O     1 
ATOM   2639 C  CB    . TRP A  1 389 ? -2.317  11.436  135.115 1.00 24.95 ? 268  TRP A CB    1 
ATOM   2640 C  CG    . TRP A  1 389 ? -3.811  11.620  135.183 1.00 24.36 ? 268  TRP A CG    1 
ATOM   2641 C  CD1   . TRP A  1 389 ? -4.485  12.804  135.107 1.00 28.87 ? 268  TRP A CD1   1 
ATOM   2642 C  CD2   . TRP A  1 389 ? -4.805  10.611  135.373 1.00 28.80 ? 268  TRP A CD2   1 
ATOM   2643 N  NE1   . TRP A  1 389 ? -5.827  12.595  135.217 1.00 27.48 ? 268  TRP A NE1   1 
ATOM   2644 C  CE2   . TRP A  1 389 ? -6.057  11.256  135.380 1.00 27.76 ? 268  TRP A CE2   1 
ATOM   2645 C  CE3   . TRP A  1 389 ? -4.763  9.224   135.535 1.00 24.94 ? 268  TRP A CE3   1 
ATOM   2646 C  CZ2   . TRP A  1 389 ? -7.245  10.570  135.545 1.00 31.18 ? 268  TRP A CZ2   1 
ATOM   2647 C  CZ3   . TRP A  1 389 ? -5.952  8.540   135.683 1.00 30.57 ? 268  TRP A CZ3   1 
ATOM   2648 C  CH2   . TRP A  1 389 ? -7.173  9.210   135.692 1.00 30.16 ? 268  TRP A CH2   1 
ATOM   2649 N  N     . LEU A  1 390 ? -3.516  9.970   132.466 1.00 18.95 ? 269  LEU A N     1 
ATOM   2650 C  CA    . LEU A  1 390 ? -4.228  8.824   131.899 1.00 21.48 ? 269  LEU A CA    1 
ATOM   2651 C  C     . LEU A  1 390 ? -3.475  8.269   130.687 1.00 19.91 ? 269  LEU A C     1 
ATOM   2652 O  O     . LEU A  1 390 ? -3.470  7.050   130.456 1.00 21.84 ? 269  LEU A O     1 
ATOM   2653 C  CB    . LEU A  1 390 ? -5.655  9.229   131.511 1.00 16.54 ? 269  LEU A CB    1 
ATOM   2654 C  CG    . LEU A  1 390 ? -6.545  8.100   131.001 1.00 20.73 ? 269  LEU A CG    1 
ATOM   2655 C  CD1   . LEU A  1 390 ? -6.635  6.978   132.052 1.00 23.16 ? 269  LEU A CD1   1 
ATOM   2656 C  CD2   . LEU A  1 390 ? -7.921  8.605   130.622 1.00 20.50 ? 269  LEU A CD2   1 
ATOM   2657 N  N     . MET A  1 391 ? -2.876  9.152   129.880 1.00 19.45 ? 270  MET A N     1 
ATOM   2658 C  CA    . MET A  1 391 ? -1.991  8.704   128.804 1.00 21.44 ? 270  MET A CA    1 
ATOM   2659 C  C     . MET A  1 391 ? -0.911  7.824   129.389 1.00 18.72 ? 270  MET A C     1 
ATOM   2660 O  O     . MET A  1 391 ? -0.633  6.737   128.878 1.00 20.55 ? 270  MET A O     1 
ATOM   2661 C  CB    . MET A  1 391 ? -1.366  9.878   128.060 1.00 18.34 ? 270  MET A CB    1 
ATOM   2662 C  CG    . MET A  1 391 ? -2.414  10.792  127.446 1.00 23.24 ? 270  MET A CG    1 
ATOM   2663 S  SD    . MET A  1 391 ? -3.560  9.974   126.313 1.00 22.46 ? 270  MET A SD    1 
ATOM   2664 C  CE    . MET A  1 391 ? -2.458  9.176   125.147 1.00 19.64 ? 270  MET A CE    1 
ATOM   2665 N  N     . TYR A  1 392 ? -0.317  8.258   130.500 1.00 16.86 ? 271  TYR A N     1 
ATOM   2666 C  CA    . TYR A  1 392 ? 0.813   7.502   130.991 1.00 18.33 ? 271  TYR A CA    1 
ATOM   2667 C  C     . TYR A  1 392 ? 0.359   6.206   131.640 1.00 19.10 ? 271  TYR A C     1 
ATOM   2668 O  O     . TYR A  1 392 ? 1.047   5.189   131.514 1.00 20.20 ? 271  TYR A O     1 
ATOM   2669 C  CB    . TYR A  1 392 ? 1.559   8.292   132.086 1.00 24.11 ? 271  TYR A CB    1 
ATOM   2670 C  CG    . TYR A  1 392 ? 2.480   9.389   131.651 1.00 26.45 ? 271  TYR A CG    1 
ATOM   2671 C  CD1   . TYR A  1 392 ? 3.165   9.306   130.439 1.00 28.83 ? 271  TYR A CD1   1 
ATOM   2672 C  CD2   . TYR A  1 392 ? 2.755   10.466  132.496 1.00 31.04 ? 271  TYR A CD2   1 
ATOM   2673 C  CE1   . TYR A  1 392 ? 4.050   10.305  130.036 1.00 31.30 ? 271  TYR A CE1   1 
ATOM   2674 C  CE2   . TYR A  1 392 ? 3.657   11.478  132.107 1.00 32.70 ? 271  TYR A CE2   1 
ATOM   2675 C  CZ    . TYR A  1 392 ? 4.302   11.383  130.870 1.00 39.02 ? 271  TYR A CZ    1 
ATOM   2676 O  OH    . TYR A  1 392 ? 5.191   12.358  130.426 1.00 43.61 ? 271  TYR A OH    1 
ATOM   2677 N  N     . LEU A  1 393 ? -0.829  6.201   132.258 1.00 15.62 ? 272  LEU A N     1 
ATOM   2678 C  CA    . LEU A  1 393 ? -1.400  4.950   132.756 1.00 17.98 ? 272  LEU A CA    1 
ATOM   2679 C  C     . LEU A  1 393 ? -1.684  3.960   131.635 1.00 17.22 ? 272  LEU A C     1 
ATOM   2680 O  O     . LEU A  1 393 ? -1.408  2.763   131.765 1.00 19.68 ? 272  LEU A O     1 
ATOM   2681 C  CB    . LEU A  1 393 ? -2.688  5.255   133.527 1.00 19.34 ? 272  LEU A CB    1 
ATOM   2682 C  CG    . LEU A  1 393 ? -3.382  4.054   134.157 1.00 27.65 ? 272  LEU A CG    1 
ATOM   2683 C  CD1   . LEU A  1 393 ? -2.446  3.375   135.136 1.00 32.91 ? 272  LEU A CD1   1 
ATOM   2684 C  CD2   . LEU A  1 393 ? -4.716  4.509   134.848 1.00 26.69 ? 272  LEU A CD2   1 
ATOM   2685 N  N     . ALA A  1 394 ? -2.236  4.449   130.513 1.00 18.28 ? 273  ALA A N     1 
ATOM   2686 C  CA    . ALA A  1 394 ? -2.554  3.563   129.396 1.00 16.15 ? 273  ALA A CA    1 
ATOM   2687 C  C     . ALA A  1 394 ? -1.299  3.031   128.727 1.00 14.10 ? 273  ALA A C     1 
ATOM   2688 O  O     . ALA A  1 394 ? -1.288  1.881   128.257 1.00 15.74 ? 273  ALA A O     1 
ATOM   2689 C  CB    . ALA A  1 394 ? -3.402  4.311   128.363 1.00 17.14 ? 273  ALA A CB    1 
ATOM   2690 N  N     . ILE A  1 395 ? -0.235  3.845   128.676 1.00 15.14 ? 274  ILE A N     1 
ATOM   2691 C  CA    . ILE A  1 395 ? 1.042   3.393   128.105 1.00 16.15 ? 274  ILE A CA    1 
ATOM   2692 C  C     . ILE A  1 395 ? 1.654   2.321   128.983 1.00 16.65 ? 274  ILE A C     1 
ATOM   2693 O  O     . ILE A  1 395 ? 2.046   1.251   128.511 1.00 19.11 ? 274  ILE A O     1 
ATOM   2694 C  CB    . ILE A  1 395 ? 1.991   4.598   127.929 1.00 15.49 ? 274  ILE A CB    1 
ATOM   2695 C  CG1   . ILE A  1 395 ? 1.471   5.514   126.816 1.00 16.42 ? 274  ILE A CG1   1 
ATOM   2696 C  CG2   . ILE A  1 395 ? 3.458   4.160   127.665 1.00 17.91 ? 274  ILE A CG2   1 
ATOM   2697 C  CD1   . ILE A  1 395 ? 2.060   6.916   126.883 1.00 16.44 ? 274  ILE A CD1   1 
ATOM   2698 N  N     . VAL A  1 396 ? 1.704   2.588   130.285 1.00 14.30 ? 275  VAL A N     1 
ATOM   2699 C  CA    . VAL A  1 396 ? 2.251   1.638   131.253 1.00 18.16 ? 275  VAL A CA    1 
ATOM   2700 C  C     . VAL A  1 396 ? 1.476   0.324   131.219 1.00 15.78 ? 275  VAL A C     1 
ATOM   2701 O  O     . VAL A  1 396 ? 2.066   -0.760  131.302 1.00 18.80 ? 275  VAL A O     1 
ATOM   2702 C  CB    . VAL A  1 396 ? 2.234   2.302   132.651 1.00 27.25 ? 275  VAL A CB    1 
ATOM   2703 C  CG1   . VAL A  1 396 ? 2.235   1.290   133.746 1.00 33.01 ? 275  VAL A CG1   1 
ATOM   2704 C  CG2   . VAL A  1 396 ? 3.436   3.283   132.764 1.00 21.06 ? 275  VAL A CG2   1 
ATOM   2705 N  N     . LEU A  1 397 ? 0.141   0.399   131.131 1.00 15.01 ? 276  LEU A N     1 
ATOM   2706 C  CA    . LEU A  1 397 ? -0.676  -0.815  131.040 1.00 17.75 ? 276  LEU A CA    1 
ATOM   2707 C  C     . LEU A  1 397 ? -0.336  -1.625  129.795 1.00 16.96 ? 276  LEU A C     1 
ATOM   2708 O  O     . LEU A  1 397 ? -0.222  -2.848  129.857 1.00 16.83 ? 276  LEU A O     1 
ATOM   2709 C  CB    . LEU A  1 397 ? -2.150  -0.452  131.023 1.00 16.71 ? 276  LEU A CB    1 
ATOM   2710 C  CG    . LEU A  1 397 ? -3.122  -1.625  130.869 1.00 25.76 ? 276  LEU A CG    1 
ATOM   2711 C  CD1   . LEU A  1 397 ? -2.975  -2.609  132.053 1.00 24.19 ? 276  LEU A CD1   1 
ATOM   2712 C  CD2   . LEU A  1 397 ? -4.548  -1.153  130.713 1.00 30.40 ? 276  LEU A CD2   1 
ATOM   2713 N  N     . SER A  1 398 ? -0.165  -0.957  128.648 1.00 16.19 ? 277  SER A N     1 
ATOM   2714 C  CA    . SER A  1 398 ? 0.228   -1.677  127.441 1.00 15.87 ? 277  SER A CA    1 
ATOM   2715 C  C     . SER A  1 398 ? 1.572   -2.387  127.644 1.00 19.60 ? 277  SER A C     1 
ATOM   2716 O  O     . SER A  1 398 ? 1.737   -3.542  127.244 1.00 20.13 ? 277  SER A O     1 
ATOM   2717 C  CB    . SER A  1 398 ? 0.247   -0.704  126.239 1.00 16.35 ? 277  SER A CB    1 
ATOM   2718 O  OG    . SER A  1 398 ? 1.431   0.071   126.216 1.00 17.61 ? 277  SER A OG    1 
ATOM   2719 N  N     . HIS A  1 399 ? 2.514   -1.750  128.347 1.00 16.02 ? 278  HIS A N     1 
ATOM   2720 C  CA    . HIS A  1 399 ? 3.819   -2.374  128.575 1.00 14.87 ? 278  HIS A CA    1 
ATOM   2721 C  C     . HIS A  1 399 ? 3.716   -3.544  129.557 1.00 17.41 ? 278  HIS A C     1 
ATOM   2722 O  O     . HIS A  1 399 ? 4.486   -4.502  129.461 1.00 19.16 ? 278  HIS A O     1 
ATOM   2723 C  CB    . HIS A  1 399 ? 4.794   -1.309  129.102 1.00 15.00 ? 278  HIS A CB    1 
ATOM   2724 C  CG    . HIS A  1 399 ? 5.109   -0.251  128.093 1.00 16.72 ? 278  HIS A CG    1 
ATOM   2725 N  ND1   . HIS A  1 399 ? 5.640   0.977   128.436 1.00 20.01 ? 278  HIS A ND1   1 
ATOM   2726 C  CD2   . HIS A  1 399 ? 4.982   -0.244  126.743 1.00 21.45 ? 278  HIS A CD2   1 
ATOM   2727 C  CE1   . HIS A  1 399 ? 5.823   1.698   127.339 1.00 25.65 ? 278  HIS A CE1   1 
ATOM   2728 N  NE2   . HIS A  1 399 ? 5.425   0.984   126.297 1.00 20.33 ? 278  HIS A NE2   1 
ATOM   2729 N  N     . THR A  1 400 ? 2.813   -3.438  130.541 1.00 17.42 ? 279  THR A N     1 
ATOM   2730 C  CA    A THR A  1 400 ? 2.556   -4.519  131.498 0.60 19.48 ? 279  THR A CA    1 
ATOM   2731 C  CA    B THR A  1 400 ? 2.607   -4.529  131.488 0.40 19.48 ? 279  THR A CA    1 
ATOM   2732 C  C     . THR A  1 400 ? 2.195   -5.827  130.804 1.00 21.71 ? 279  THR A C     1 
ATOM   2733 O  O     . THR A  1 400 ? 2.416   -6.916  131.364 1.00 20.77 ? 279  THR A O     1 
ATOM   2734 C  CB    A THR A  1 400 ? 1.441   -4.076  132.473 0.60 19.83 ? 279  THR A CB    1 
ATOM   2735 C  CB    B THR A  1 400 ? 1.582   -4.093  132.548 0.40 19.94 ? 279  THR A CB    1 
ATOM   2736 O  OG1   A THR A  1 400 ? 1.845   -2.876  133.154 0.60 13.94 ? 279  THR A OG1   1 
ATOM   2737 O  OG1   B THR A  1 400 ? 1.966   -4.620  133.826 0.40 26.99 ? 279  THR A OG1   1 
ATOM   2738 C  CG2   A THR A  1 400 ? 1.090   -5.164  133.496 0.60 22.07 ? 279  THR A CG2   1 
ATOM   2739 C  CG2   B THR A  1 400 ? 0.169   -4.500  132.195 0.40 12.85 ? 279  THR A CG2   1 
ATOM   2740 N  N     . ASN A  1 401 ? 1.623   -5.757  129.601 1.00 19.17 ? 280  ASN A N     1 
ATOM   2741 C  CA    . ASN A  1 401 ? 1.345   -7.005  128.904 1.00 21.20 ? 280  ASN A CA    1 
ATOM   2742 C  C     . ASN A  1 401 ? 2.612   -7.817  128.672 1.00 21.74 ? 280  ASN A C     1 
ATOM   2743 O  O     . ASN A  1 401 ? 2.553   -9.046  128.567 1.00 21.42 ? 280  ASN A O     1 
ATOM   2744 C  CB    . ASN A  1 401 ? 0.674   -6.758  127.551 1.00 21.75 ? 280  ASN A CB    1 
ATOM   2745 C  CG    . ASN A  1 401 ? 0.310   -8.077  126.875 1.00 26.59 ? 280  ASN A CG    1 
ATOM   2746 O  OD1   . ASN A  1 401 ? 0.859   -8.444  125.846 1.00 23.38 ? 280  ASN A OD1   1 
ATOM   2747 N  ND2   . ASN A  1 401 ? -0.554  -8.827  127.518 1.00 19.60 ? 280  ASN A ND2   1 
ATOM   2748 N  N     . SER A  1 402 ? 3.766   -7.156  128.549 1.00 19.06 ? 281  SER A N     1 
ATOM   2749 C  CA    . SER A  1 402 ? 5.007   -7.905  128.351 1.00 24.61 ? 281  SER A CA    1 
ATOM   2750 C  C     . SER A  1 402 ? 5.500   -8.609  129.621 1.00 22.80 ? 281  SER A C     1 
ATOM   2751 O  O     . SER A  1 402 ? 6.524   -9.287  129.561 1.00 22.62 ? 281  SER A O     1 
ATOM   2752 C  CB    . SER A  1 402 ? 6.101   -6.974  127.805 1.00 21.12 ? 281  SER A CB    1 
ATOM   2753 O  OG    . SER A  1 402 ? 5.755   -6.542  126.469 1.00 25.23 ? 281  SER A OG    1 
ATOM   2754 N  N     . VAL A  1 403 ? 4.842   -8.428  130.762 1.00 22.70 ? 282  VAL A N     1 
ATOM   2755 C  CA    . VAL A  1 403 ? 5.211   -9.100  132.015 1.00 21.01 ? 282  VAL A CA    1 
ATOM   2756 C  C     . VAL A  1 403 ? 4.370   -10.360 132.224 1.00 25.36 ? 282  VAL A C     1 
ATOM   2757 O  O     . VAL A  1 403 ? 4.797   -11.297 132.909 1.00 23.75 ? 282  VAL A O     1 
ATOM   2758 C  CB    . VAL A  1 403 ? 5.061   -8.142  133.216 1.00 23.96 ? 282  VAL A CB    1 
ATOM   2759 C  CG1   . VAL A  1 403 ? 5.395   -8.864  134.533 1.00 22.42 ? 282  VAL A CG1   1 
ATOM   2760 C  CG2   . VAL A  1 403 ? 5.944   -6.933  133.026 1.00 19.77 ? 282  VAL A CG2   1 
ATOM   2761 N  N     . VAL A  1 404 ? 3.148   -10.384 131.684 1.00 19.87 ? 283  VAL A N     1 
ATOM   2762 C  CA    . VAL A  1 404 ? 2.147   -11.291 132.243 1.00 20.20 ? 283  VAL A CA    1 
ATOM   2763 C  C     . VAL A  1 404 ? 2.273   -12.713 131.686 1.00 24.26 ? 283  VAL A C     1 
ATOM   2764 O  O     . VAL A  1 404 ? 1.964   -13.673 132.402 1.00 23.61 ? 283  VAL A O     1 
ATOM   2765 C  CB    . VAL A  1 404 ? 0.708   -10.768 132.040 1.00 25.24 ? 283  VAL A CB    1 
ATOM   2766 C  CG1   . VAL A  1 404 ? 0.525   -9.398  132.672 1.00 26.47 ? 283  VAL A CG1   1 
ATOM   2767 C  CG2   . VAL A  1 404 ? 0.338   -10.702 130.576 1.00 26.01 ? 283  VAL A CG2   1 
ATOM   2768 N  N     . ASN A  1 405 ? 2.695   -12.897 130.433 1.00 20.51 ? 284  ASN A N     1 
ATOM   2769 C  CA    . ASN A  1 405 ? 2.702   -14.257 129.874 1.00 28.44 ? 284  ASN A CA    1 
ATOM   2770 C  C     . ASN A  1 405 ? 3.509   -15.265 130.690 1.00 26.17 ? 284  ASN A C     1 
ATOM   2771 O  O     . ASN A  1 405 ? 2.988   -16.366 130.935 1.00 26.64 ? 284  ASN A O     1 
ATOM   2772 C  CB    . ASN A  1 405 ? 3.148   -14.245 128.403 1.00 27.11 ? 284  ASN A CB    1 
ATOM   2773 C  CG    . ASN A  1 405 ? 2.171   -13.484 127.510 1.00 32.47 ? 284  ASN A CG    1 
ATOM   2774 O  OD1   . ASN A  1 405 ? 1.074   -13.104 127.951 1.00 31.98 ? 284  ASN A OD1   1 
ATOM   2775 N  ND2   . ASN A  1 405 ? 2.558   -13.253 126.258 1.00 28.13 ? 284  ASN A ND2   1 
ATOM   2776 N  N     . PRO A  1 406 ? 4.737   -14.980 131.145 1.00 24.12 ? 285  PRO A N     1 
ATOM   2777 C  CA    . PRO A  1 406 ? 5.444   -15.975 131.976 1.00 26.49 ? 285  PRO A CA    1 
ATOM   2778 C  C     . PRO A  1 406 ? 4.637   -16.460 133.175 1.00 28.86 ? 285  PRO A C     1 
ATOM   2779 O  O     . PRO A  1 406 ? 4.724   -17.648 133.522 1.00 29.94 ? 285  PRO A O     1 
ATOM   2780 C  CB    . PRO A  1 406 ? 6.715   -15.231 132.408 1.00 21.90 ? 285  PRO A CB    1 
ATOM   2781 C  CG    . PRO A  1 406 ? 6.959   -14.254 131.287 1.00 24.19 ? 285  PRO A CG    1 
ATOM   2782 C  CD    . PRO A  1 406 ? 5.583   -13.797 130.878 1.00 24.60 ? 285  PRO A CD    1 
ATOM   2783 N  N     . PHE A  1 407 ? 3.811   -15.596 133.776 1.00 25.36 ? 286  PHE A N     1 
ATOM   2784 C  CA    . PHE A  1 407 ? 2.953   -16.005 134.894 1.00 27.70 ? 286  PHE A CA    1 
ATOM   2785 C  C     . PHE A  1 407 ? 1.830   -16.924 134.453 1.00 34.23 ? 286  PHE A C     1 
ATOM   2786 O  O     . PHE A  1 407 ? 1.512   -17.898 135.151 1.00 29.93 ? 286  PHE A O     1 
ATOM   2787 C  CB    . PHE A  1 407 ? 2.373   -14.769 135.573 1.00 29.77 ? 286  PHE A CB    1 
ATOM   2788 C  CG    . PHE A  1 407 ? 3.363   -14.052 136.392 1.00 32.41 ? 286  PHE A CG    1 
ATOM   2789 C  CD1   . PHE A  1 407 ? 4.155   -13.053 135.846 1.00 34.46 ? 286  PHE A CD1   1 
ATOM   2790 C  CD2   . PHE A  1 407 ? 3.494   -14.366 137.745 1.00 32.72 ? 286  PHE A CD2   1 
ATOM   2791 C  CE1   . PHE A  1 407 ? 5.107   -12.403 136.631 1.00 38.39 ? 286  PHE A CE1   1 
ATOM   2792 C  CE2   . PHE A  1 407 ? 4.431   -13.710 138.539 1.00 38.12 ? 286  PHE A CE2   1 
ATOM   2793 C  CZ    . PHE A  1 407 ? 5.236   -12.737 137.981 1.00 31.96 ? 286  PHE A CZ    1 
ATOM   2794 N  N     . ILE A  1 408 ? 1.226   -16.648 133.294 1.00 26.09 ? 287  ILE A N     1 
ATOM   2795 C  CA    . ILE A  1 408 ? 0.177   -17.532 132.804 1.00 28.61 ? 287  ILE A CA    1 
ATOM   2796 C  C     . ILE A  1 408 ? 0.750   -18.914 132.542 1.00 29.50 ? 287  ILE A C     1 
ATOM   2797 O  O     . ILE A  1 408 ? 0.120   -19.932 132.863 1.00 30.85 ? 287  ILE A O     1 
ATOM   2798 C  CB    . ILE A  1 408 ? -0.500  -16.955 131.551 1.00 29.34 ? 287  ILE A CB    1 
ATOM   2799 C  CG1   . ILE A  1 408 ? -1.009  -15.544 131.809 1.00 28.64 ? 287  ILE A CG1   1 
ATOM   2800 C  CG2   . ILE A  1 408 ? -1.629  -17.855 131.107 1.00 27.94 ? 287  ILE A CG2   1 
ATOM   2801 C  CD1   . ILE A  1 408 ? -2.049  -15.458 132.885 1.00 32.64 ? 287  ILE A CD1   1 
ATOM   2802 N  N     . TYR A  1 409 ? 1.951   -18.977 131.951 1.00 25.43 ? 288  TYR A N     1 
ATOM   2803 C  CA    . TYR A  1 409 ? 2.568   -20.282 131.707 1.00 34.25 ? 288  TYR A CA    1 
ATOM   2804 C  C     . TYR A  1 409 ? 2.869   -21.006 133.009 1.00 28.60 ? 288  TYR A C     1 
ATOM   2805 O  O     . TYR A  1 409 ? 2.586   -22.203 133.138 1.00 35.52 ? 288  TYR A O     1 
ATOM   2806 C  CB    . TYR A  1 409 ? 3.866   -20.136 130.909 1.00 27.68 ? 288  TYR A CB    1 
ATOM   2807 C  CG    . TYR A  1 409 ? 3.688   -19.443 129.599 1.00 24.00 ? 288  TYR A CG    1 
ATOM   2808 C  CD1   . TYR A  1 409 ? 2.599   -19.726 128.784 1.00 27.50 ? 288  TYR A CD1   1 
ATOM   2809 C  CD2   . TYR A  1 409 ? 4.638   -18.538 129.143 1.00 25.89 ? 288  TYR A CD2   1 
ATOM   2810 C  CE1   . TYR A  1 409 ? 2.443   -19.095 127.549 1.00 35.44 ? 288  TYR A CE1   1 
ATOM   2811 C  CE2   . TYR A  1 409 ? 4.482   -17.884 127.929 1.00 22.96 ? 288  TYR A CE2   1 
ATOM   2812 C  CZ    . TYR A  1 409 ? 3.388   -18.173 127.134 1.00 31.49 ? 288  TYR A CZ    1 
ATOM   2813 O  OH    . TYR A  1 409 ? 3.262   -17.511 125.928 1.00 30.60 ? 288  TYR A OH    1 
ATOM   2814 N  N     . ALA A  1 410 ? 3.367   -20.278 134.006 1.00 28.07 ? 289  ALA A N     1 
ATOM   2815 C  CA    . ALA A  1 410 ? 3.728   -20.902 135.273 1.00 30.56 ? 289  ALA A CA    1 
ATOM   2816 C  C     . ALA A  1 410 ? 2.493   -21.455 135.967 1.00 38.78 ? 289  ALA A C     1 
ATOM   2817 O  O     . ALA A  1 410 ? 2.514   -22.579 136.482 1.00 42.28 ? 289  ALA A O     1 
ATOM   2818 C  CB    . ALA A  1 410 ? 4.467   -19.897 136.165 1.00 28.58 ? 289  ALA A CB    1 
ATOM   2819 N  N     . TYR A  1 411 ? 1.389   -20.699 135.948 1.00 36.16 ? 290  TYR A N     1 
ATOM   2820 C  CA    . TYR A  1 411 ? 0.192   -21.124 136.657 1.00 39.18 ? 290  TYR A CA    1 
ATOM   2821 C  C     . TYR A  1 411 ? -0.627  -22.162 135.906 1.00 44.82 ? 290  TYR A C     1 
ATOM   2822 O  O     . TYR A  1 411 ? -1.328  -22.954 136.546 1.00 40.67 ? 290  TYR A O     1 
ATOM   2823 C  CB    . TYR A  1 411 ? -0.705  -19.910 136.924 1.00 40.22 ? 290  TYR A CB    1 
ATOM   2824 C  CG    . TYR A  1 411 ? -0.405  -19.186 138.211 1.00 48.95 ? 290  TYR A CG    1 
ATOM   2825 C  CD1   . TYR A  1 411 ? -0.012  -17.856 138.219 1.00 56.28 ? 290  TYR A CD1   1 
ATOM   2826 C  CD2   . TYR A  1 411 ? -0.561  -19.833 139.435 1.00 62.26 ? 290  TYR A CD2   1 
ATOM   2827 C  CE1   . TYR A  1 411 ? 0.250   -17.198 139.418 1.00 65.75 ? 290  TYR A CE1   1 
ATOM   2828 C  CE2   . TYR A  1 411 ? -0.305  -19.190 140.630 1.00 54.41 ? 290  TYR A CE2   1 
ATOM   2829 C  CZ    . TYR A  1 411 ? 0.097   -17.880 140.623 1.00 64.73 ? 290  TYR A CZ    1 
ATOM   2830 O  OH    . TYR A  1 411 ? 0.344   -17.258 141.827 1.00 70.17 ? 290  TYR A OH    1 
ATOM   2831 N  N     . ARG A  1 412 ? -0.497  -22.248 134.583 1.00 36.54 ? 291  ARG A N     1 
ATOM   2832 C  CA    . ARG A  1 412 ? -1.410  -23.069 133.806 1.00 40.73 ? 291  ARG A CA    1 
ATOM   2833 C  C     . ARG A  1 412 ? -0.768  -24.244 133.085 1.00 33.63 ? 291  ARG A C     1 
ATOM   2834 O  O     . ARG A  1 412 ? -1.499  -25.143 132.649 1.00 38.81 ? 291  ARG A O     1 
ATOM   2835 C  CB    . ARG A  1 412 ? -2.180  -22.197 132.794 1.00 32.77 ? 291  ARG A CB    1 
ATOM   2836 C  CG    . ARG A  1 412 ? -3.127  -21.186 133.473 1.00 29.67 ? 291  ARG A CG    1 
ATOM   2837 C  CD    . ARG A  1 412 ? -4.262  -20.753 132.539 1.00 35.15 ? 291  ARG A CD    1 
ATOM   2838 N  NE    . ARG A  1 412 ? -4.845  -21.898 131.845 1.00 46.16 ? 291  ARG A NE    1 
ATOM   2839 C  CZ    . ARG A  1 412 ? -6.016  -22.447 132.150 1.00 47.41 ? 291  ARG A CZ    1 
ATOM   2840 N  NH1   . ARG A  1 412 ? -6.764  -21.972 133.136 1.00 44.44 ? 291  ARG A NH1   1 
ATOM   2841 N  NH2   . ARG A  1 412 ? -6.437  -23.516 131.465 1.00 44.22 ? 291  ARG A NH2   1 
ATOM   2842 N  N     . ILE A  1 413 ? 0.555   -24.289 132.950 1.00 32.44 ? 292  ILE A N     1 
ATOM   2843 C  CA    . ILE A  1 413 ? 1.219   -25.317 132.154 1.00 34.39 ? 292  ILE A CA    1 
ATOM   2844 C  C     . ILE A  1 413 ? 2.271   -25.986 133.033 1.00 36.12 ? 292  ILE A C     1 
ATOM   2845 O  O     . ILE A  1 413 ? 3.332   -25.411 133.293 1.00 34.10 ? 292  ILE A O     1 
ATOM   2846 C  CB    . ILE A  1 413 ? 1.848   -24.730 130.885 1.00 35.29 ? 292  ILE A CB    1 
ATOM   2847 C  CG1   . ILE A  1 413 ? 0.857   -23.783 130.200 1.00 39.86 ? 292  ILE A CG1   1 
ATOM   2848 C  CG2   . ILE A  1 413 ? 2.251   -25.847 129.897 1.00 34.29 ? 292  ILE A CG2   1 
ATOM   2849 C  CD1   . ILE A  1 413 ? 1.358   -23.211 128.890 1.00 33.23 ? 292  ILE A CD1   1 
ATOM   2850 N  N     . ARG A  1 414 ? 1.969   -27.209 133.493 1.00 38.73 ? 293  ARG A N     1 
ATOM   2851 C  CA    . ARG A  1 414 ? 2.853   -27.936 134.407 1.00 42.91 ? 293  ARG A CA    1 
ATOM   2852 C  C     . ARG A  1 414 ? 4.278   -28.051 133.875 1.00 34.59 ? 293  ARG A C     1 
ATOM   2853 O  O     . ARG A  1 414 ? 5.245   -27.884 134.624 1.00 37.37 ? 293  ARG A O     1 
ATOM   2854 C  CB    . ARG A  1 414 ? 2.235   -29.305 134.737 1.00 43.23 ? 293  ARG A CB    1 
ATOM   2855 C  CG    . ARG A  1 414 ? 2.794   -29.942 136.013 1.00 54.70 ? 293  ARG A CG    1 
ATOM   2856 C  CD    . ARG A  1 414 ? 2.136   -31.286 136.322 1.00 54.41 ? 293  ARG A CD    1 
ATOM   2857 N  NE    . ARG A  1 414 ? 0.836   -31.051 136.953 1.00 71.01 ? 293  ARG A NE    1 
ATOM   2858 C  CZ    . ARG A  1 414 ? -0.341  -31.115 136.344 1.00 70.61 ? 293  ARG A CZ    1 
ATOM   2859 N  NH1   . ARG A  1 414 ? -0.445  -31.416 135.060 1.00 66.79 ? 293  ARG A NH1   1 
ATOM   2860 N  NH2   . ARG A  1 414 ? -1.445  -30.861 137.042 1.00 76.02 ? 293  ARG A NH2   1 
ATOM   2861 N  N     . GLU A  1 415 ? 4.434   -28.347 132.589 1.00 37.58 ? 294  GLU A N     1 
ATOM   2862 C  CA    . GLU A  1 415 ? 5.778   -28.525 132.054 1.00 37.10 ? 294  GLU A CA    1 
ATOM   2863 C  C     . GLU A  1 415 ? 6.600   -27.240 132.144 1.00 36.99 ? 294  GLU A C     1 
ATOM   2864 O  O     . GLU A  1 415 ? 7.815   -27.291 132.367 1.00 34.36 ? 294  GLU A O     1 
ATOM   2865 C  CB    . GLU A  1 415 ? 5.695   -29.003 130.612 1.00 36.57 ? 294  GLU A CB    1 
ATOM   2866 C  CG    . GLU A  1 415 ? 6.971   -29.599 130.101 1.00 47.83 ? 294  GLU A CG    1 
ATOM   2867 C  CD    . GLU A  1 415 ? 7.323   -30.889 130.777 1.00 54.48 ? 294  GLU A CD    1 
ATOM   2868 O  OE1   . GLU A  1 415 ? 6.402   -31.674 131.110 1.00 59.05 ? 294  GLU A OE1   1 
ATOM   2869 O  OE2   . GLU A  1 415 ? 8.538   -31.103 130.970 1.00 46.84 ? 294  GLU A OE2   1 
ATOM   2870 N  N     . PHE A  1 416 ? 5.962   -26.075 131.955 1.00 33.35 ? 295  PHE A N     1 
ATOM   2871 C  CA    . PHE A  1 416 ? 6.661   -24.808 132.156 1.00 29.63 ? 295  PHE A CA    1 
ATOM   2872 C  C     . PHE A  1 416 ? 6.967   -24.598 133.628 1.00 29.09 ? 295  PHE A C     1 
ATOM   2873 O  O     . PHE A  1 416 ? 8.100   -24.271 134.004 1.00 30.79 ? 295  PHE A O     1 
ATOM   2874 C  CB    . PHE A  1 416 ? 5.815   -23.636 131.636 1.00 28.89 ? 295  PHE A CB    1 
ATOM   2875 C  CG    . PHE A  1 416 ? 6.112   -23.273 130.213 1.00 30.88 ? 295  PHE A CG    1 
ATOM   2876 C  CD1   . PHE A  1 416 ? 7.328   -22.720 129.863 1.00 29.27 ? 295  PHE A CD1   1 
ATOM   2877 C  CD2   . PHE A  1 416 ? 5.178   -23.534 129.215 1.00 32.56 ? 295  PHE A CD2   1 
ATOM   2878 C  CE1   . PHE A  1 416 ? 7.608   -22.400 128.540 1.00 30.23 ? 295  PHE A CE1   1 
ATOM   2879 C  CE2   . PHE A  1 416 ? 5.451   -23.218 127.893 1.00 30.79 ? 295  PHE A CE2   1 
ATOM   2880 C  CZ    . PHE A  1 416 ? 6.661   -22.653 127.558 1.00 26.00 ? 295  PHE A CZ    1 
ATOM   2881 N  N     . ARG A  1 417 ? 5.943   -24.739 134.469 1.00 31.60 ? 296  ARG A N     1 
ATOM   2882 C  CA    . ARG A  1 417 ? 6.102   -24.499 135.895 1.00 33.25 ? 296  ARG A CA    1 
ATOM   2883 C  C     . ARG A  1 417 ? 7.234   -25.348 136.472 1.00 36.97 ? 296  ARG A C     1 
ATOM   2884 O  O     . ARG A  1 417 ? 8.079   -24.846 137.216 1.00 35.80 ? 296  ARG A O     1 
ATOM   2885 C  CB    . ARG A  1 417 ? 4.803   -24.852 136.612 1.00 34.79 ? 296  ARG A CB    1 
ATOM   2886 C  CG    . ARG A  1 417 ? 4.857   -24.599 138.102 1.00 41.99 ? 296  ARG A CG    1 
ATOM   2887 C  CD    . ARG A  1 417 ? 3.684   -25.233 138.819 1.00 42.26 ? 296  ARG A CD    1 
ATOM   2888 N  NE    . ARG A  1 417 ? 2.411   -24.947 138.184 1.00 52.40 ? 296  ARG A NE    1 
ATOM   2889 C  CZ    . ARG A  1 417 ? 1.654   -25.863 137.602 1.00 44.54 ? 296  ARG A CZ    1 
ATOM   2890 N  NH1   . ARG A  1 417 ? 1.934   -27.147 137.693 1.00 49.46 ? 296  ARG A NH1   1 
ATOM   2891 N  NH2   . ARG A  1 417 ? 0.582   -25.479 136.921 1.00 50.91 ? 296  ARG A NH2   1 
ATOM   2892 N  N     . GLN A  1 418 ? 7.314   -26.620 136.067 1.00 35.50 ? 297  GLN A N     1 
ATOM   2893 C  CA    . GLN A  1 418 ? 8.358   -27.488 136.600 1.00 37.44 ? 297  GLN A CA    1 
ATOM   2894 C  C     . GLN A  1 418 ? 9.731   -27.088 136.080 1.00 37.38 ? 297  GLN A C     1 
ATOM   2895 O  O     . GLN A  1 418 ? 10.715  -27.105 136.826 1.00 34.94 ? 297  GLN A O     1 
ATOM   2896 C  CB    . GLN A  1 418 ? 8.052   -28.946 136.258 1.00 36.59 ? 297  GLN A CB    1 
ATOM   2897 C  CG    . GLN A  1 418 ? 6.843   -29.523 136.997 1.00 41.62 ? 297  GLN A CG    1 
ATOM   2898 C  CD    . GLN A  1 418 ? 6.440   -30.923 136.512 1.00 63.55 ? 297  GLN A CD    1 
ATOM   2899 O  OE1   . GLN A  1 418 ? 6.730   -31.308 135.375 1.00 59.92 ? 297  GLN A OE1   1 
ATOM   2900 N  NE2   . GLN A  1 418 ? 5.768   -31.685 137.375 1.00 52.94 ? 297  GLN A NE2   1 
ATOM   2901 N  N     . THR A  1 419 ? 9.813   -26.679 134.822 1.00 34.83 ? 298  THR A N     1 
ATOM   2902 C  CA    . THR A  1 419 ? 11.099  -26.254 134.287 1.00 29.66 ? 298  THR A CA    1 
ATOM   2903 C  C     . THR A  1 419 ? 11.544  -24.937 134.913 1.00 33.61 ? 298  THR A C     1 
ATOM   2904 O  O     . THR A  1 419 ? 12.734  -24.736 135.170 1.00 33.02 ? 298  THR A O     1 
ATOM   2905 C  CB    . THR A  1 419 ? 11.008  -26.128 132.776 1.00 31.20 ? 298  THR A CB    1 
ATOM   2906 O  OG1   . THR A  1 419 ? 10.418  -27.323 132.265 1.00 34.48 ? 298  THR A OG1   1 
ATOM   2907 C  CG2   . THR A  1 419 ? 12.394  -25.965 132.196 1.00 32.28 ? 298  THR A CG2   1 
ATOM   2908 N  N     . PHE A  1 420 ? 10.610  -24.004 135.107 1.00 33.38 ? 299  PHE A N     1 
ATOM   2909 C  CA    . PHE A  1 420 ? 10.933  -22.783 135.837 1.00 35.08 ? 299  PHE A CA    1 
ATOM   2910 C  C     . PHE A  1 420 ? 11.537  -23.105 137.199 1.00 38.41 ? 299  PHE A C     1 
ATOM   2911 O  O     . PHE A  1 420 ? 12.585  -22.561 137.568 1.00 38.56 ? 299  PHE A O     1 
ATOM   2912 C  CB    . PHE A  1 420 ? 9.686   -21.917 136.014 1.00 33.42 ? 299  PHE A CB    1 
ATOM   2913 C  CG    . PHE A  1 420 ? 9.170   -21.287 134.739 1.00 32.98 ? 299  PHE A CG    1 
ATOM   2914 C  CD1   . PHE A  1 420 ? 9.934   -21.274 133.581 1.00 30.85 ? 299  PHE A CD1   1 
ATOM   2915 C  CD2   . PHE A  1 420 ? 7.916   -20.678 134.724 1.00 30.06 ? 299  PHE A CD2   1 
ATOM   2916 C  CE1   . PHE A  1 420 ? 9.448   -20.673 132.419 1.00 32.96 ? 299  PHE A CE1   1 
ATOM   2917 C  CE2   . PHE A  1 420 ? 7.431   -20.071 133.583 1.00 30.68 ? 299  PHE A CE2   1 
ATOM   2918 C  CZ    . PHE A  1 420 ? 8.190   -20.082 132.427 1.00 32.73 ? 299  PHE A CZ    1 
ATOM   2919 N  N     . ARG A  1 421 ? 10.881  -23.988 137.962 1.00 35.33 ? 300  ARG A N     1 
ATOM   2920 C  CA    . ARG A  1 421 ? 11.369  -24.324 139.300 1.00 44.76 ? 300  ARG A CA    1 
ATOM   2921 C  C     . ARG A  1 421 ? 12.799  -24.845 139.242 1.00 36.08 ? 300  ARG A C     1 
ATOM   2922 O  O     . ARG A  1 421 ? 13.674  -24.399 139.994 1.00 40.31 ? 300  ARG A O     1 
ATOM   2923 C  CB    . ARG A  1 421 ? 10.447  -25.361 139.936 1.00 46.07 ? 300  ARG A CB    1 
ATOM   2924 C  CG    . ARG A  1 421 ? 9.285   -24.749 140.674 1.00 59.86 ? 300  ARG A CG    1 
ATOM   2925 C  CD    . ARG A  1 421 ? 8.710   -25.729 141.664 1.00 63.87 ? 300  ARG A CD    1 
ATOM   2926 N  NE    . ARG A  1 421 ? 7.613   -26.503 141.096 1.00 67.37 ? 300  ARG A NE    1 
ATOM   2927 C  CZ    . ARG A  1 421 ? 6.332   -26.194 141.232 1.00 66.92 ? 300  ARG A CZ    1 
ATOM   2928 N  NH1   . ARG A  1 421 ? 5.952   -25.080 141.840 1.00 63.31 ? 300  ARG A NH1   1 
ATOM   2929 N  NH2   . ARG A  1 421 ? 5.412   -27.028 140.750 1.00 59.36 ? 300  ARG A NH2   1 
ATOM   2930 N  N     . LYS A  1 422 ? 13.057  -25.752 138.300 1.00 39.74 ? 301  LYS A N     1 
ATOM   2931 C  CA    . LYS A  1 422 ? 14.382  -26.337 138.144 1.00 39.66 ? 301  LYS A CA    1 
ATOM   2932 C  C     . LYS A  1 422 ? 15.417  -25.290 137.771 1.00 43.20 ? 301  LYS A C     1 
ATOM   2933 O  O     . LYS A  1 422 ? 16.551  -25.321 138.260 1.00 42.35 ? 301  LYS A O     1 
ATOM   2934 C  CB    . LYS A  1 422 ? 14.305  -27.407 137.057 1.00 38.40 ? 301  LYS A CB    1 
ATOM   2935 C  CG    . LYS A  1 422 ? 13.567  -28.672 137.437 1.00 51.59 ? 301  LYS A CG    1 
ATOM   2936 C  CD    . LYS A  1 422 ? 13.605  -29.696 136.291 1.00 66.43 ? 301  LYS A CD    1 
ATOM   2937 C  CE    . LYS A  1 422 ? 14.571  -29.284 135.180 1.00 70.19 ? 301  LYS A CE    1 
ATOM   2938 N  NZ    . LYS A  1 422 ? 14.234  -29.931 133.859 1.00 83.63 ? 301  LYS A NZ    1 
ATOM   2939 N  N     . ILE A  1 423 ? 15.050  -24.356 136.894 1.00 39.07 ? 302  ILE A N     1 
ATOM   2940 C  CA    . ILE A  1 423 ? 15.982  -23.302 136.510 1.00 39.60 ? 302  ILE A CA    1 
ATOM   2941 C  C     . ILE A  1 423 ? 16.295  -22.419 137.707 1.00 46.84 ? 302  ILE A C     1 
ATOM   2942 O  O     . ILE A  1 423 ? 17.447  -22.035 137.938 1.00 42.78 ? 302  ILE A O     1 
ATOM   2943 C  CB    . ILE A  1 423 ? 15.416  -22.477 135.342 1.00 44.60 ? 302  ILE A CB    1 
ATOM   2944 C  CG1   . ILE A  1 423 ? 15.326  -23.335 134.082 1.00 42.18 ? 302  ILE A CG1   1 
ATOM   2945 C  CG2   . ILE A  1 423 ? 16.337  -21.305 135.069 1.00 35.34 ? 302  ILE A CG2   1 
ATOM   2946 C  CD1   . ILE A  1 423 ? 14.419  -22.739 133.030 1.00 36.66 ? 302  ILE A CD1   1 
ATOM   2947 N  N     . ILE A  1 424 ? 15.254  -22.037 138.445 1.00 41.93 ? 303  ILE A N     1 
ATOM   2948 C  CA    . ILE A  1 424 ? 15.407  -21.140 139.588 1.00 48.84 ? 303  ILE A CA    1 
ATOM   2949 C  C     . ILE A  1 424 ? 16.202  -21.829 140.688 1.00 46.11 ? 303  ILE A C     1 
ATOM   2950 O  O     . ILE A  1 424 ? 17.158  -21.262 141.236 1.00 49.05 ? 303  ILE A O     1 
ATOM   2951 C  CB    . ILE A  1 424 ? 14.030  -20.646 140.076 1.00 40.40 ? 303  ILE A CB    1 
ATOM   2952 C  CG1   . ILE A  1 424 ? 13.380  -19.765 138.999 1.00 43.23 ? 303  ILE A CG1   1 
ATOM   2953 C  CG2   . ILE A  1 424 ? 14.130  -19.880 141.391 1.00 40.83 ? 303  ILE A CG2   1 
ATOM   2954 C  CD1   . ILE A  1 424 ? 11.878  -19.801 138.981 1.00 37.63 ? 303  ILE A CD1   1 
ATOM   2955 N  N     . ARG A  1 425 ? 15.827  -23.065 141.026 1.00 50.11 ? 304  ARG A N     1 
ATOM   2956 C  CA    . ARG A  1 425 ? 16.542  -23.781 142.085 1.00 56.06 ? 304  ARG A CA    1 
ATOM   2957 C  C     . ARG A  1 425 ? 18.027  -23.896 141.762 1.00 57.59 ? 304  ARG A C     1 
ATOM   2958 O  O     . ARG A  1 425 ? 18.880  -23.506 142.564 1.00 55.95 ? 304  ARG A O     1 
ATOM   2959 C  CB    . ARG A  1 425 ? 15.921  -25.155 142.313 1.00 48.46 ? 304  ARG A CB    1 
ATOM   2960 C  CG    . ARG A  1 425 ? 14.676  -25.094 143.175 1.00 53.80 ? 304  ARG A CG    1 
ATOM   2961 C  CD    . ARG A  1 425 ? 13.938  -26.428 143.180 1.00 59.73 ? 304  ARG A CD    1 
ATOM   2962 N  NE    . ARG A  1 425 ? 12.570  -26.279 143.674 1.00 70.75 ? 304  ARG A NE    1 
ATOM   2963 C  CZ    . ARG A  1 425 ? 11.638  -27.221 143.616 1.00 79.42 ? 304  ARG A CZ    1 
ATOM   2964 N  NH1   . ARG A  1 425 ? 11.894  -28.423 143.116 1.00 73.05 ? 304  ARG A NH1   1 
ATOM   2965 N  NH2   . ARG A  1 425 ? 10.423  -26.956 144.085 1.00 72.01 ? 304  ARG A NH2   1 
ATOM   2966 N  N     . SER A  1 426 ? 18.358  -24.382 140.576 1.00 50.80 ? 305  SER A N     1 
ATOM   2967 C  CA    . SER A  1 426 ? 19.760  -24.477 140.204 1.00 51.68 ? 305  SER A CA    1 
ATOM   2968 C  C     . SER A  1 426 ? 20.391  -23.100 139.970 1.00 50.27 ? 305  SER A C     1 
ATOM   2969 O  O     . SER A  1 426 ? 20.188  -22.463 138.938 1.00 64.91 ? 305  SER A O     1 
ATOM   2970 C  CB    . SER A  1 426 ? 19.897  -25.339 138.950 1.00 62.70 ? 305  SER A CB    1 
ATOM   2971 O  OG    . SER A  1 426 ? 19.211  -26.575 139.125 1.00 61.34 ? 305  SER A OG    1 
HETATM 2972 N  N1    . JQ9 B  2 .   ? 1.532   4.264   121.368 1.00 23.05 ? 1201 JQ9 A N1    1 
HETATM 2973 C  C12   . JQ9 B  2 .   ? 0.395   2.104   121.065 1.00 32.85 ? 1201 JQ9 A C12   1 
HETATM 2974 O  O2    . JQ9 B  2 .   ? 3.333   3.262   122.392 1.00 29.14 ? 1201 JQ9 A O2    1 
HETATM 2975 C  C2    . JQ9 B  2 .   ? 2.628   4.247   122.235 1.00 26.48 ? 1201 JQ9 A C2    1 
HETATM 2976 N  N3    . JQ9 B  2 .   ? 2.875   5.418   122.908 1.00 21.46 ? 1201 JQ9 A N3    1 
HETATM 2977 C  C21   . JQ9 B  2 .   ? 3.949   5.430   123.921 1.00 21.97 ? 1201 JQ9 A C21   1 
HETATM 2978 C  C22   . JQ9 B  2 .   ? 5.273   5.796   123.299 1.00 28.97 ? 1201 JQ9 A C22   1 
HETATM 2979 C  C4    . JQ9 B  2 .   ? 2.004   6.478   122.842 1.00 19.46 ? 1201 JQ9 A C4    1 
HETATM 2980 N  N9    . JQ9 B  2 .   ? 2.152   7.671   123.478 1.00 21.73 ? 1201 JQ9 A N9    1 
HETATM 2981 C  C8    . JQ9 B  2 .   ? 1.063   8.346   123.128 1.00 19.76 ? 1201 JQ9 A C8    1 
HETATM 2982 N  N7    . JQ9 B  2 .   ? 0.254   7.634   122.283 1.00 17.21 ? 1201 JQ9 A N7    1 
HETATM 2983 C  C7    . JQ9 B  2 .   ? -1.003  8.089   121.689 1.00 15.39 ? 1201 JQ9 A C7    1 
HETATM 2984 C  C5    . JQ9 B  2 .   ? 0.882   6.419   122.098 1.00 21.05 ? 1201 JQ9 A C5    1 
HETATM 2985 C  C6    . JQ9 B  2 .   ? 0.564   5.288   121.284 1.00 20.69 ? 1201 JQ9 A C6    1 
HETATM 2986 O  O6    . JQ9 B  2 .   ? -0.435  5.152   120.603 1.00 18.57 ? 1201 JQ9 A O6    1 
HETATM 2987 C  C11   . JQ9 B  2 .   ? 1.331   3.085   120.492 1.00 20.83 ? 1201 JQ9 A C11   1 
HETATM 2988 C  CA    . JQ9 B  2 .   ? 0.713   9.649   123.643 1.00 21.87 ? 1201 JQ9 A CA    1 
HETATM 2989 C  CB    . JQ9 B  2 .   ? 1.517   10.310  124.437 1.00 25.67 ? 1201 JQ9 A CB    1 
HETATM 2990 C  "C1'" . JQ9 B  2 .   ? 1.335   11.638  125.000 1.00 30.35 ? 1201 JQ9 A "C1'" 1 
HETATM 2991 C  "C6'" . JQ9 B  2 .   ? 0.243   12.449  124.703 1.00 30.38 ? 1201 JQ9 A "C6'" 1 
HETATM 2992 C  "C5'" . JQ9 B  2 .   ? 0.210   13.776  125.100 1.00 40.52 ? 1201 JQ9 A "C5'" 1 
HETATM 2993 C  "C4'" . JQ9 B  2 .   ? 1.290   14.309  125.794 1.00 44.22 ? 1201 JQ9 A "C4'" 1 
HETATM 2994 O  "O4'" . JQ9 B  2 .   ? 1.384   15.612  126.197 1.00 49.63 ? 1201 JQ9 A "O4'" 1 
HETATM 2995 C  "C8'" . JQ9 B  2 .   ? 0.224   16.434  126.041 1.00 47.51 ? 1201 JQ9 A "C8'" 1 
HETATM 2996 C  "C3'" . JQ9 B  2 .   ? 2.386   13.488  126.125 1.00 34.14 ? 1201 JQ9 A "C3'" 1 
HETATM 2997 C  "C2'" . JQ9 B  2 .   ? 2.384   12.162  125.758 1.00 31.48 ? 1201 JQ9 A "C2'" 1 
HETATM 2998 O  "O3'" . JQ9 B  2 .   ? 3.421   14.102  126.768 1.00 37.99 ? 1201 JQ9 A "O3'" 1 
HETATM 2999 C  "C9'" . JQ9 B  2 .   ? 4.494   13.276  127.227 1.00 38.18 ? 1201 JQ9 A "C9'" 1 
HETATM 3000 C  C1    . CLR C  3 .   ? -16.641 8.022   118.708 1.00 21.02 ? 1202 CLR A C1    1 
HETATM 3001 C  C2    . CLR C  3 .   ? -16.791 9.538   118.730 1.00 21.91 ? 1202 CLR A C2    1 
HETATM 3002 C  C3    . CLR C  3 .   ? -17.724 9.958   119.839 1.00 26.39 ? 1202 CLR A C3    1 
HETATM 3003 C  C4    . CLR C  3 .   ? -17.174 9.445   121.172 1.00 22.12 ? 1202 CLR A C4    1 
HETATM 3004 C  C5    . CLR C  3 .   ? -16.995 7.944   121.140 1.00 21.21 ? 1202 CLR A C5    1 
HETATM 3005 C  C6    . CLR C  3 .   ? -17.556 7.148   122.055 1.00 22.76 ? 1202 CLR A C6    1 
HETATM 3006 C  C7    . CLR C  3 .   ? -17.280 5.687   122.182 1.00 20.66 ? 1202 CLR A C7    1 
HETATM 3007 C  C8    . CLR C  3 .   ? -16.117 5.213   121.304 1.00 20.63 ? 1202 CLR A C8    1 
HETATM 3008 C  C9    . CLR C  3 .   ? -16.177 5.880   119.920 1.00 20.29 ? 1202 CLR A C9    1 
HETATM 3009 C  C10   . CLR C  3 .   ? -16.093 7.425   120.032 1.00 22.57 ? 1202 CLR A C10   1 
HETATM 3010 C  C11   . CLR C  3 .   ? -15.175 5.300   118.924 1.00 19.59 ? 1202 CLR A C11   1 
HETATM 3011 C  C12   . CLR C  3 .   ? -15.127 3.773   118.831 1.00 24.80 ? 1202 CLR A C12   1 
HETATM 3012 C  C13   . CLR C  3 .   ? -15.002 3.155   120.230 1.00 26.08 ? 1202 CLR A C13   1 
HETATM 3013 C  C14   . CLR C  3 .   ? -16.183 3.714   121.057 1.00 20.23 ? 1202 CLR A C14   1 
HETATM 3014 C  C15   . CLR C  3 .   ? -16.326 2.814   122.272 1.00 26.06 ? 1202 CLR A C15   1 
HETATM 3015 C  C16   . CLR C  3 .   ? -15.634 1.490   121.859 1.00 30.54 ? 1202 CLR A C16   1 
HETATM 3016 C  C17   . CLR C  3 .   ? -15.265 1.634   120.354 1.00 29.94 ? 1202 CLR A C17   1 
HETATM 3017 C  C18   . CLR C  3 .   ? -13.627 3.499   120.864 1.00 21.98 ? 1202 CLR A C18   1 
HETATM 3018 C  C19   . CLR C  3 .   ? -14.649 7.913   120.320 1.00 17.33 ? 1202 CLR A C19   1 
HETATM 3019 C  C20   . CLR C  3 .   ? -14.133 0.672   119.983 1.00 35.75 ? 1202 CLR A C20   1 
HETATM 3020 C  C21   . CLR C  3 .   ? -13.676 0.707   118.519 1.00 25.32 ? 1202 CLR A C21   1 
HETATM 3021 C  C22   . CLR C  3 .   ? -14.571 -0.741  120.364 1.00 36.35 ? 1202 CLR A C22   1 
HETATM 3022 C  C23   . CLR C  3 .   ? -13.372 -1.624  120.657 1.00 36.87 ? 1202 CLR A C23   1 
HETATM 3023 C  C24   . CLR C  3 .   ? -13.376 -2.824  119.745 1.00 41.97 ? 1202 CLR A C24   1 
HETATM 3024 C  C25   . CLR C  3 .   ? -13.958 -4.072  120.381 1.00 37.26 ? 1202 CLR A C25   1 
HETATM 3025 C  C26   . CLR C  3 .   ? -15.370 -4.284  119.858 1.00 50.88 ? 1202 CLR A C26   1 
HETATM 3026 C  C27   . CLR C  3 .   ? -13.926 -3.982  121.896 1.00 39.79 ? 1202 CLR A C27   1 
HETATM 3027 O  O1    . CLR C  3 .   ? -17.841 11.363  119.773 1.00 25.19 ? 1202 CLR A O1    1 
HETATM 3028 C  C1    . CLR D  3 .   ? 18.531  10.692  117.997 1.00 22.40 ? 1203 CLR A C1    1 
HETATM 3029 C  C2    . CLR D  3 .   ? 18.290  12.184  117.710 1.00 25.32 ? 1203 CLR A C2    1 
HETATM 3030 C  C3    . CLR D  3 .   ? 18.493  12.497  116.238 1.00 26.80 ? 1203 CLR A C3    1 
HETATM 3031 C  C4    . CLR D  3 .   ? 17.620  11.616  115.362 1.00 22.54 ? 1203 CLR A C4    1 
HETATM 3032 C  C5    . CLR D  3 .   ? 17.872  10.158  115.614 1.00 26.62 ? 1203 CLR A C5    1 
HETATM 3033 C  C6    . CLR D  3 .   ? 18.144  9.345   114.595 1.00 25.91 ? 1203 CLR A C6    1 
HETATM 3034 C  C7    . CLR D  3 .   ? 18.321  7.864   114.707 1.00 24.47 ? 1203 CLR A C7    1 
HETATM 3035 C  C8    . CLR D  3 .   ? 17.984  7.313   116.108 1.00 24.75 ? 1203 CLR A C8    1 
HETATM 3036 C  C9    . CLR D  3 .   ? 18.397  8.287   117.217 1.00 24.33 ? 1203 CLR A C9    1 
HETATM 3037 C  C10   . CLR D  3 .   ? 17.768  9.695   117.065 1.00 27.73 ? 1203 CLR A C10   1 
HETATM 3038 C  C11   . CLR D  3 .   ? 18.131  7.654   118.594 1.00 24.94 ? 1203 CLR A C11   1 
HETATM 3039 C  C12   . CLR D  3 .   ? 18.945  6.369   118.783 1.00 20.27 ? 1203 CLR A C12   1 
HETATM 3040 C  C13   . CLR D  3 .   ? 18.457  5.338   117.732 1.00 25.40 ? 1203 CLR A C13   1 
HETATM 3041 C  C14   . CLR D  3 .   ? 18.677  5.978   116.346 1.00 21.71 ? 1203 CLR A C14   1 
HETATM 3042 C  C15   . CLR D  3 .   ? 18.392  4.851   115.355 1.00 22.17 ? 1203 CLR A C15   1 
HETATM 3043 C  C16   . CLR D  3 .   ? 18.974  3.621   116.078 1.00 25.71 ? 1203 CLR A C16   1 
HETATM 3044 C  C17   . CLR D  3 .   ? 19.236  4.000   117.568 1.00 20.07 ? 1203 CLR A C17   1 
HETATM 3045 C  C18   . CLR D  3 .   ? 16.985  4.979   117.912 1.00 24.65 ? 1203 CLR A C18   1 
HETATM 3046 C  C19   . CLR D  3 .   ? 16.277  9.651   117.479 1.00 24.08 ? 1203 CLR A C19   1 
HETATM 3047 C  C20   . CLR D  3 .   ? 18.966  2.790   118.476 1.00 19.14 ? 1203 CLR A C20   1 
HETATM 3048 C  C21   . CLR D  3 .   ? 19.096  3.093   119.972 1.00 25.56 ? 1203 CLR A C21   1 
HETATM 3049 C  C22   . CLR D  3 .   ? 19.902  1.628   118.086 1.00 28.05 ? 1203 CLR A C22   1 
HETATM 3050 C  C23   . CLR D  3 .   ? 19.735  0.352   118.913 1.00 23.34 ? 1203 CLR A C23   1 
HETATM 3051 C  C24   . CLR D  3 .   ? 20.414  -0.840  118.241 1.00 43.73 ? 1203 CLR A C24   1 
HETATM 3052 C  C25   . CLR D  3 .   ? 20.075  -2.212  118.837 1.00 48.31 ? 1203 CLR A C25   1 
HETATM 3053 C  C26   . CLR D  3 .   ? 20.345  -2.243  120.350 1.00 45.70 ? 1203 CLR A C26   1 
HETATM 3054 C  C27   . CLR D  3 .   ? 20.882  -3.311  118.162 1.00 57.79 ? 1203 CLR A C27   1 
HETATM 3055 O  O1    . CLR D  3 .   ? 18.228  13.868  115.973 1.00 27.74 ? 1203 CLR A O1    1 
HETATM 3056 C  C1    . OLA E  4 .   ? -17.515 11.881  113.857 1.00 49.38 ? 1204 OLA A C1    1 
HETATM 3057 O  O1    . OLA E  4 .   ? -17.011 11.758  112.724 1.00 66.38 ? 1204 OLA A O1    1 
HETATM 3058 O  O2    . OLA E  4 .   ? -18.000 12.991  114.216 1.00 48.45 ? 1204 OLA A O2    1 
HETATM 3059 C  C2    . OLA E  4 .   ? -17.510 10.675  114.754 1.00 33.35 ? 1204 OLA A C2    1 
HETATM 3060 C  C3    . OLA E  4 .   ? -17.299 9.455   113.877 1.00 29.55 ? 1204 OLA A C3    1 
HETATM 3061 C  C4    . OLA E  4 .   ? -17.079 8.286   114.807 1.00 22.81 ? 1204 OLA A C4    1 
HETATM 3062 C  C5    . OLA E  4 .   ? -16.845 7.021   114.027 1.00 24.93 ? 1204 OLA A C5    1 
HETATM 3063 C  C6    . OLA E  4 .   ? -16.704 5.864   114.994 1.00 29.39 ? 1204 OLA A C6    1 
HETATM 3064 C  C7    . OLA E  4 .   ? -16.082 4.707   114.247 1.00 33.63 ? 1204 OLA A C7    1 
HETATM 3065 C  C8    . OLA E  4 .   ? -16.824 3.394   114.372 1.00 38.71 ? 1204 OLA A C8    1 
HETATM 3066 C  C9    . OLA E  4 .   ? -16.275 2.666   115.555 1.00 36.14 ? 1204 OLA A C9    1 
HETATM 3067 C  C10   . OLA E  4 .   ? -15.721 1.307   115.457 1.00 45.12 ? 1204 OLA A C10   1 
HETATM 3068 C  C11   . OLA E  4 .   ? -16.163 0.279   114.453 1.00 41.47 ? 1204 OLA A C11   1 
HETATM 3069 C  C12   . OLA E  4 .   ? -15.536 -1.036  114.901 1.00 49.88 ? 1204 OLA A C12   1 
HETATM 3070 C  C1    . OLA F  4 .   ? 19.481  13.498  122.237 1.00 44.59 ? 1205 OLA A C1    1 
HETATM 3071 O  O1    . OLA F  4 .   ? 19.746  12.838  121.213 1.00 45.37 ? 1205 OLA A O1    1 
HETATM 3072 O  O2    . OLA F  4 .   ? 19.820  14.698  122.335 1.00 48.50 ? 1205 OLA A O2    1 
HETATM 3073 C  C2    . OLA F  4 .   ? 18.747  12.793  123.330 1.00 47.15 ? 1205 OLA A C2    1 
HETATM 3074 C  C3    . OLA F  4 .   ? 19.107  11.324  123.176 1.00 45.18 ? 1205 OLA A C3    1 
HETATM 3075 C  C4    . OLA F  4 .   ? 17.986  10.530  122.545 1.00 36.20 ? 1205 OLA A C4    1 
HETATM 3076 C  C5    . OLA F  4 .   ? 18.444  9.100   122.421 1.00 34.64 ? 1205 OLA A C5    1 
HETATM 3077 C  C6    . OLA F  4 .   ? 17.734  8.185   123.384 1.00 32.46 ? 1205 OLA A C6    1 
HETATM 3078 C  C7    . OLA F  4 .   ? 17.795  6.761   122.844 1.00 36.66 ? 1205 OLA A C7    1 
HETATM 3079 C  C8    . OLA F  4 .   ? 16.836  5.886   123.625 1.00 41.78 ? 1205 OLA A C8    1 
HETATM 3080 C  C9    . OLA F  4 .   ? 17.418  4.521   123.816 1.00 32.98 ? 1205 OLA A C9    1 
HETATM 3081 C  C10   . OLA F  4 .   ? 18.300  4.341   124.957 1.00 36.57 ? 1205 OLA A C10   1 
HETATM 3082 C  C11   . OLA F  4 .   ? 18.813  2.958   125.245 1.00 47.03 ? 1205 OLA A C11   1 
HETATM 3083 C  C12   . OLA F  4 .   ? 19.009  2.285   123.903 1.00 43.32 ? 1205 OLA A C12   1 
HETATM 3084 C  C13   . OLA F  4 .   ? 18.747  0.805   124.064 1.00 43.00 ? 1205 OLA A C13   1 
HETATM 3085 C  C14   . OLA F  4 .   ? 19.940  0.121   124.692 1.00 47.89 ? 1205 OLA A C14   1 
HETATM 3086 C  C15   . OLA F  4 .   ? 20.551  -0.840  123.676 1.00 51.46 ? 1205 OLA A C15   1 
HETATM 3087 C  C1    . CLR G  3 .   ? -11.515 10.750  126.510 1.00 21.66 ? 1206 CLR A C1    1 
HETATM 3088 C  C2    . CLR G  3 .   ? -11.417 12.269  126.532 1.00 26.66 ? 1206 CLR A C2    1 
HETATM 3089 C  C3    . CLR G  3 .   ? -12.752 12.931  126.849 1.00 28.80 ? 1206 CLR A C3    1 
HETATM 3090 C  C4    . CLR G  3 .   ? -13.251 12.428  128.196 1.00 23.95 ? 1206 CLR A C4    1 
HETATM 3091 C  C5    . CLR G  3 .   ? -13.306 10.920  128.215 1.00 26.22 ? 1206 CLR A C5    1 
HETATM 3092 C  C6    . CLR G  3 .   ? -14.318 10.294  128.806 1.00 26.46 ? 1206 CLR A C6    1 
HETATM 3093 C  C7    . CLR G  3 .   ? -14.417 8.811   128.942 1.00 25.95 ? 1206 CLR A C7    1 
HETATM 3094 C  C8    . CLR G  3 .   ? -13.049 8.103   128.896 1.00 28.72 ? 1206 CLR A C8    1 
HETATM 3095 C  C9    . CLR G  3 .   ? -12.205 8.664   127.736 1.00 22.83 ? 1206 CLR A C9    1 
HETATM 3096 C  C10   . CLR G  3 .   ? -12.009 10.200  127.860 1.00 27.09 ? 1206 CLR A C10   1 
HETATM 3097 C  C11   . CLR G  3 .   ? -10.900 7.880   127.577 1.00 23.02 ? 1206 CLR A C11   1 
HETATM 3098 C  C12   . CLR G  3 .   ? -11.139 6.373   127.409 1.00 24.55 ? 1206 CLR A C12   1 
HETATM 3099 C  C13   . CLR G  3 .   ? -11.859 5.802   128.635 1.00 23.31 ? 1206 CLR A C13   1 
HETATM 3100 C  C14   . CLR G  3 .   ? -13.196 6.588   128.719 1.00 30.86 ? 1206 CLR A C14   1 
HETATM 3101 C  C15   . CLR G  3 .   ? -14.035 5.807   129.721 1.00 30.66 ? 1206 CLR A C15   1 
HETATM 3102 C  C16   . CLR G  3 .   ? -13.644 4.329   129.469 1.00 28.84 ? 1206 CLR A C16   1 
HETATM 3103 C  C17   . CLR G  3 .   ? -12.363 4.327   128.569 1.00 25.14 ? 1206 CLR A C17   1 
HETATM 3104 C  C18   . CLR G  3 .   ? -11.025 6.057   129.893 1.00 25.79 ? 1206 CLR A C18   1 
HETATM 3105 C  C19   . CLR G  3 .   ? -10.987 10.547  128.951 1.00 25.55 ? 1206 CLR A C19   1 
HETATM 3106 C  C20   . CLR G  3 .   ? -11.392 3.164   128.886 1.00 27.38 ? 1206 CLR A C20   1 
HETATM 3107 C  C21   . CLR G  3 .   ? -10.108 3.194   128.050 1.00 29.56 ? 1206 CLR A C21   1 
HETATM 3108 C  C22   . CLR G  3 .   ? -12.086 1.820   128.669 1.00 23.91 ? 1206 CLR A C22   1 
HETATM 3109 C  C23   . CLR G  3 .   ? -11.296 0.573   129.047 1.00 30.29 ? 1206 CLR A C23   1 
HETATM 3110 C  C24   . CLR G  3 .   ? -12.087 -0.703  128.778 1.00 35.95 ? 1206 CLR A C24   1 
HETATM 3111 C  C25   . CLR G  3 .   ? -11.333 -2.038  128.972 1.00 38.03 ? 1206 CLR A C25   1 
HETATM 3112 C  C26   . CLR G  3 .   ? -10.644 -2.438  127.669 1.00 30.45 ? 1206 CLR A C26   1 
HETATM 3113 C  C27   . CLR G  3 .   ? -12.273 -3.188  129.343 1.00 46.65 ? 1206 CLR A C27   1 
HETATM 3114 O  O1    . CLR G  3 .   ? -12.596 14.344  126.820 1.00 33.22 ? 1206 CLR A O1    1 
HETATM 3115 C  C10   . OLA H  4 .   ? -11.135 -15.665 123.972 1.00 44.55 ? 1207 OLA A C10   1 
HETATM 3116 C  C11   . OLA H  4 .   ? -10.141 -15.389 122.864 1.00 34.99 ? 1207 OLA A C11   1 
HETATM 3117 C  C12   . OLA H  4 .   ? -9.609  -13.964 122.955 1.00 43.62 ? 1207 OLA A C12   1 
HETATM 3118 C  C13   . OLA H  4 .   ? -9.200  -13.449 121.579 1.00 36.16 ? 1207 OLA A C13   1 
HETATM 3119 C  C14   . OLA H  4 .   ? -9.093  -11.925 121.560 1.00 37.23 ? 1207 OLA A C14   1 
HETATM 3120 C  C15   . OLA H  4 .   ? -10.278 -11.231 122.217 1.00 34.50 ? 1207 OLA A C15   1 
HETATM 3121 C  C16   . OLA H  4 .   ? -10.967 -10.304 121.217 1.00 44.79 ? 1207 OLA A C16   1 
HETATM 3122 C  C17   . OLA H  4 .   ? -11.207 -8.887  121.726 1.00 40.07 ? 1207 OLA A C17   1 
HETATM 3123 C  C18   . OLA H  4 .   ? -11.438 -7.961  120.536 1.00 40.71 ? 1207 OLA A C18   1 
HETATM 3124 C  C1    . OLA I  4 .   ? 16.453  15.228  126.826 1.00 59.03 ? 1208 OLA A C1    1 
HETATM 3125 O  O1    . OLA I  4 .   ? 15.638  16.136  127.118 1.00 64.59 ? 1208 OLA A O1    1 
HETATM 3126 O  O2    . OLA I  4 .   ? 17.362  15.457  125.995 1.00 61.31 ? 1208 OLA A O2    1 
HETATM 3127 C  C2    . OLA I  4 .   ? 16.355  13.865  127.465 1.00 43.99 ? 1208 OLA A C2    1 
HETATM 3128 C  C3    . OLA I  4 .   ? 17.064  12.901  126.542 1.00 35.25 ? 1208 OLA A C3    1 
HETATM 3129 C  C4    . OLA I  4 .   ? 16.280  11.609  126.403 1.00 45.28 ? 1208 OLA A C4    1 
HETATM 3130 C  C5    . OLA I  4 .   ? 16.200  10.871  127.728 1.00 41.58 ? 1208 OLA A C5    1 
HETATM 3131 C  C6    . OLA I  4 .   ? 17.094  9.643   127.720 1.00 43.40 ? 1208 OLA A C6    1 
HETATM 3132 C  C7    . OLA I  4 .   ? 16.269  8.372   127.756 1.00 42.30 ? 1208 OLA A C7    1 
HETATM 3133 C  C8    . OLA I  4 .   ? 16.978  7.319   128.586 1.00 41.54 ? 1208 OLA A C8    1 
HETATM 3134 C  C9    . OLA I  4 .   ? 16.374  5.973   128.285 1.00 35.90 ? 1208 OLA A C9    1 
HETATM 3135 C  C10   . OLA I  4 .   ? 16.343  4.952   129.337 1.00 40.10 ? 1208 OLA A C10   1 
HETATM 3136 C  C11   . OLA I  4 .   ? 17.411  5.009   130.393 1.00 53.10 ? 1208 OLA A C11   1 
HETATM 3137 C  C12   . OLA I  4 .   ? 17.814  3.587   130.731 1.00 53.41 ? 1208 OLA A C12   1 
HETATM 3138 C  C13   . OLA I  4 .   ? 18.396  2.902   129.506 1.00 56.34 ? 1208 OLA A C13   1 
HETATM 3139 C  C14   . OLA I  4 .   ? 18.450  1.410   129.788 1.00 61.41 ? 1208 OLA A C14   1 
HETATM 3140 C  C15   . OLA I  4 .   ? 17.082  0.927   130.273 1.00 60.86 ? 1208 OLA A C15   1 
HETATM 3141 C  C16   . OLA I  4 .   ? 17.167  -0.453  130.923 1.00 67.89 ? 1208 OLA A C16   1 
HETATM 3142 C  C17   . OLA I  4 .   ? 15.809  -1.093  131.198 1.00 40.32 ? 1208 OLA A C17   1 
HETATM 3143 C  C18   . OLA I  4 .   ? 16.072  -2.451  131.829 1.00 41.46 ? 1208 OLA A C18   1 
HETATM 3144 C  C1    . OLA J  4 .   ? 0.479   -22.529 112.014 1.00 43.11 ? 1209 OLA A C1    1 
HETATM 3145 O  O1    . OLA J  4 .   ? 0.949   -23.669 111.802 1.00 61.45 ? 1209 OLA A O1    1 
HETATM 3146 O  O2    . OLA J  4 .   ? 0.331   -22.186 113.197 1.00 57.30 ? 1209 OLA A O2    1 
HETATM 3147 C  C2    . OLA J  4 .   ? 0.096   -21.593 110.892 1.00 41.06 ? 1209 OLA A C2    1 
HETATM 3148 C  C3    . OLA J  4 .   ? 0.558   -20.177 111.214 1.00 41.80 ? 1209 OLA A C3    1 
HETATM 3149 C  C4    . OLA J  4 .   ? -0.377  -19.099 110.668 1.00 39.82 ? 1209 OLA A C4    1 
HETATM 3150 C  C5    . OLA J  4 .   ? 0.339   -17.755 110.768 1.00 39.29 ? 1209 OLA A C5    1 
HETATM 3151 C  C6    . OLA J  4 .   ? -0.587  -16.554 110.890 1.00 35.15 ? 1209 OLA A C6    1 
HETATM 3152 C  C7    . OLA J  4 .   ? 0.089   -15.312 110.324 1.00 37.62 ? 1209 OLA A C7    1 
HETATM 3153 C  C1    . OLA K  4 .   ? 14.477  -21.699 122.036 1.00 53.32 ? 1210 OLA A C1    1 
HETATM 3154 O  O1    . OLA K  4 .   ? 14.497  -22.068 120.838 1.00 57.46 ? 1210 OLA A O1    1 
HETATM 3155 O  O2    . OLA K  4 .   ? 14.077  -22.509 122.900 1.00 61.88 ? 1210 OLA A O2    1 
HETATM 3156 C  C2    . OLA K  4 .   ? 14.921  -20.319 122.476 1.00 41.79 ? 1210 OLA A C2    1 
HETATM 3157 C  C3    . OLA K  4 .   ? 15.932  -19.723 121.506 1.00 47.54 ? 1210 OLA A C3    1 
HETATM 3158 C  C4    . OLA K  4 .   ? 15.630  -18.250 121.243 1.00 47.12 ? 1210 OLA A C4    1 
HETATM 3159 C  C5    . OLA K  4 .   ? 15.586  -17.511 122.570 1.00 50.44 ? 1210 OLA A C5    1 
HETATM 3160 C  C6    . OLA K  4 .   ? 15.916  -16.029 122.437 1.00 45.09 ? 1210 OLA A C6    1 
HETATM 3161 C  C7    . OLA K  4 .   ? 15.541  -15.489 121.075 1.00 42.01 ? 1210 OLA A C7    1 
HETATM 3162 C  C8    . OLA K  4 .   ? 15.252  -13.990 121.165 1.00 55.88 ? 1210 OLA A C8    1 
HETATM 3163 C  C9    . OLA K  4 .   ? 15.868  -13.353 122.391 1.00 40.76 ? 1210 OLA A C9    1 
HETATM 3164 C  C10   . OLA K  4 .   ? 15.806  -11.896 122.589 1.00 44.93 ? 1210 OLA A C10   1 
HETATM 3165 C  C11   . OLA K  4 .   ? 15.669  -10.994 121.390 1.00 41.72 ? 1210 OLA A C11   1 
HETATM 3166 C  C12   . OLA K  4 .   ? 17.041  -10.427 121.038 1.00 53.77 ? 1210 OLA A C12   1 
HETATM 3167 C  C1    . OLA L  4 .   ? 12.731  -21.220 116.776 1.00 66.16 ? 1211 OLA A C1    1 
HETATM 3168 O  O1    . OLA L  4 .   ? 12.629  -22.311 116.154 1.00 62.00 ? 1211 OLA A O1    1 
HETATM 3169 O  O2    . OLA L  4 .   ? 13.869  -20.754 117.019 1.00 78.33 ? 1211 OLA A O2    1 
HETATM 3170 C  C2    . OLA L  4 .   ? 11.512  -20.460 117.242 1.00 43.72 ? 1211 OLA A C2    1 
HETATM 3171 C  C3    . OLA L  4 .   ? 11.931  -19.126 117.843 1.00 41.97 ? 1211 OLA A C3    1 
HETATM 3172 C  C4    . OLA L  4 .   ? 11.746  -18.037 116.796 1.00 47.58 ? 1211 OLA A C4    1 
HETATM 3173 C  C5    . OLA L  4 .   ? 11.826  -16.664 117.430 1.00 36.77 ? 1211 OLA A C5    1 
HETATM 3174 C  C6    . OLA L  4 .   ? 13.252  -16.351 117.817 1.00 45.17 ? 1211 OLA A C6    1 
HETATM 3175 C  C7    . OLA L  4 .   ? 13.398  -14.858 118.032 1.00 43.44 ? 1211 OLA A C7    1 
HETATM 3176 C  C8    . OLA L  4 .   ? 13.249  -14.096 116.731 1.00 39.99 ? 1211 OLA A C8    1 
HETATM 3177 C  C9    . OLA L  4 .   ? 13.244  -12.648 117.119 1.00 37.21 ? 1211 OLA A C9    1 
HETATM 3178 C  C10   . OLA L  4 .   ? 13.352  -11.616 116.087 1.00 42.34 ? 1211 OLA A C10   1 
HETATM 3179 C  C11   . OLA L  4 .   ? 13.985  -10.292 116.445 1.00 39.48 ? 1211 OLA A C11   1 
HETATM 3180 C  C12   . OLA L  4 .   ? 13.855  -9.293  115.304 1.00 42.29 ? 1211 OLA A C12   1 
HETATM 3181 C  C13   . OLA L  4 .   ? 13.891  -7.865  115.838 1.00 39.90 ? 1211 OLA A C13   1 
HETATM 3182 C  C14   . OLA L  4 .   ? 15.325  -7.357  115.951 1.00 51.40 ? 1211 OLA A C14   1 
HETATM 3183 C  C1    . OLA M  4 .   ? -11.147 14.629  130.291 1.00 54.92 ? 1212 OLA A C1    1 
HETATM 3184 O  O1    . OLA M  4 .   ? -10.252 15.027  129.489 1.00 44.18 ? 1212 OLA A O1    1 
HETATM 3185 O  O2    . OLA M  4 .   ? -12.260 15.218  130.336 1.00 59.79 ? 1212 OLA A O2    1 
HETATM 3186 C  C2    . OLA M  4 .   ? -10.893 13.425  131.169 1.00 45.63 ? 1212 OLA A C2    1 
HETATM 3187 C  C3    . OLA M  4 .   ? -11.308 13.658  132.608 1.00 46.38 ? 1212 OLA A C3    1 
HETATM 3188 C  C4    . OLA M  4 .   ? -10.820 12.460  133.418 1.00 47.50 ? 1212 OLA A C4    1 
HETATM 3189 C  C5    . OLA M  4 .   ? -11.379 11.170  132.839 1.00 42.47 ? 1212 OLA A C5    1 
HETATM 3190 C  C6    . OLA M  4 .   ? -10.853 9.958   133.609 1.00 46.31 ? 1212 OLA A C6    1 
HETATM 3191 C  C7    . OLA M  4 .   ? -11.611 8.699   133.215 1.00 44.43 ? 1212 OLA A C7    1 
HETATM 3192 C  C8    . OLA M  4 .   ? -11.553 7.642   134.314 1.00 46.16 ? 1212 OLA A C8    1 
HETATM 3193 C  C9    . OLA M  4 .   ? -10.594 6.540   133.930 1.00 46.41 ? 1212 OLA A C9    1 
HETATM 3194 C  C10   . OLA M  4 .   ? -9.461  6.233   134.825 1.00 58.43 ? 1212 OLA A C10   1 
HETATM 3195 C  C11   . OLA M  4 .   ? -9.173  4.839   135.347 1.00 52.18 ? 1212 OLA A C11   1 
HETATM 3196 C  C12   . OLA M  4 .   ? -8.425  4.955   136.674 1.00 44.55 ? 1212 OLA A C12   1 
HETATM 3197 C  C13   . OLA M  4 .   ? -7.976  3.604   137.223 1.00 52.29 ? 1212 OLA A C13   1 
HETATM 3198 C  C1    . OLA N  4 .   ? 16.908  10.213  110.281 1.00 58.76 ? 1213 OLA A C1    1 
HETATM 3199 O  O1    . OLA N  4 .   ? 17.425  10.126  109.140 1.00 71.18 ? 1213 OLA A O1    1 
HETATM 3200 O  O2    . OLA N  4 .   ? 16.463  11.325  110.668 1.00 49.95 ? 1213 OLA A O2    1 
HETATM 3201 C  C2    . OLA N  4 .   ? 16.820  8.999   111.182 1.00 52.62 ? 1213 OLA A C2    1 
HETATM 3202 C  C3    . OLA N  4 .   ? 17.103  7.700   110.429 1.00 58.38 ? 1213 OLA A C3    1 
HETATM 3203 C  C4    . OLA N  4 .   ? 16.563  6.508   111.213 1.00 44.85 ? 1213 OLA A C4    1 
HETATM 3204 C  C5    . OLA N  4 .   ? 17.261  5.243   110.738 1.00 49.94 ? 1213 OLA A C5    1 
HETATM 3205 C  C6    . OLA N  4 .   ? 16.625  4.037   111.415 1.00 49.64 ? 1213 OLA A C6    1 
HETATM 3206 C  C7    . OLA N  4 .   ? 17.717  3.083   111.881 1.00 54.34 ? 1213 OLA A C7    1 
HETATM 3207 C  C8    . OLA N  4 .   ? 17.240  1.640   111.986 1.00 49.48 ? 1213 OLA A C8    1 
HETATM 3208 C  C9    . OLA N  4 .   ? 18.164  0.910   112.941 1.00 60.60 ? 1213 OLA A C9    1 
HETATM 3209 C  C10   . OLA N  4 .   ? 18.334  -0.554  112.902 1.00 51.38 ? 1213 OLA A C10   1 
HETATM 3210 C  C10   . OLA O  4 .   ? 4.820   -2.902  137.942 1.00 45.18 ? 1214 OLA A C10   1 
HETATM 3211 C  C11   . OLA O  4 .   ? 4.558   -4.074  136.990 1.00 38.98 ? 1214 OLA A C11   1 
HETATM 3212 C  C12   . OLA O  4 .   ? 3.400   -4.953  137.466 1.00 32.14 ? 1214 OLA A C12   1 
HETATM 3213 C  C13   . OLA O  4 .   ? 3.090   -6.029  136.436 1.00 31.77 ? 1214 OLA A C13   1 
HETATM 3214 C  C14   . OLA O  4 .   ? 1.925   -6.920  136.862 1.00 40.46 ? 1214 OLA A C14   1 
HETATM 3215 C  C15   . OLA O  4 .   ? 1.976   -8.239  136.097 1.00 45.87 ? 1214 OLA A C15   1 
HETATM 3216 C  C16   . OLA O  4 .   ? 1.663   -9.377  137.038 1.00 45.71 ? 1214 OLA A C16   1 
HETATM 3217 C  C17   . OLA O  4 .   ? 1.073   -10.613 136.514 1.00 45.10 ? 1214 OLA A C17   1 
HETATM 3218 C  C1    . OLA P  4 .   ? -12.540 8.473   106.270 1.00 57.10 ? 1215 OLA A C1    1 
HETATM 3219 O  O1    . OLA P  4 .   ? -13.318 9.459   106.312 1.00 63.68 ? 1215 OLA A O1    1 
HETATM 3220 O  O2    . OLA P  4 .   ? -11.300 8.660   106.335 1.00 54.98 ? 1215 OLA A O2    1 
HETATM 3221 C  C2    . OLA P  4 .   ? -13.090 7.079   106.136 1.00 40.96 ? 1215 OLA A C2    1 
HETATM 3222 C  C3    . OLA P  4 .   ? -12.026 6.087   106.564 1.00 36.35 ? 1215 OLA A C3    1 
HETATM 3223 C  C4    . OLA P  4 .   ? -12.519 4.692   106.240 1.00 37.34 ? 1215 OLA A C4    1 
HETATM 3224 C  C5    . OLA P  4 .   ? -12.675 3.797   107.458 1.00 37.78 ? 1215 OLA A C5    1 
HETATM 3225 C  C6    . OLA P  4 .   ? -11.763 2.591   107.272 1.00 44.03 ? 1215 OLA A C6    1 
HETATM 3226 C  C7    . OLA P  4 .   ? -11.920 1.507   108.325 1.00 45.52 ? 1215 OLA A C7    1 
HETATM 3227 C  C8    . OLA P  4 .   ? -11.480 0.160   107.771 1.00 45.94 ? 1215 OLA A C8    1 
HETATM 3228 C  C9    . OLA P  4 .   ? -10.440 -0.382  108.707 1.00 38.24 ? 1215 OLA A C9    1 
HETATM 3229 C  C10   . OLA P  4 .   ? -10.159 -1.822  108.848 1.00 36.46 ? 1215 OLA A C10   1 
HETATM 3230 C  C11   . OLA P  4 .   ? -10.732 -2.868  107.926 1.00 58.48 ? 1215 OLA A C11   1 
HETATM 3231 C  C4    . OLA Q  4 .   ? 13.656  -17.949 112.500 1.00 47.00 ? 1216 OLA A C4    1 
HETATM 3232 C  C5    . OLA Q  4 .   ? 13.355  -16.752 113.395 1.00 44.40 ? 1216 OLA A C5    1 
HETATM 3233 C  C6    . OLA Q  4 .   ? 13.108  -15.476 112.600 1.00 44.08 ? 1216 OLA A C6    1 
HETATM 3234 C  C7    . OLA Q  4 .   ? 14.081  -14.402 113.051 1.00 52.62 ? 1216 OLA A C7    1 
HETATM 3235 C  C8    . OLA Q  4 .   ? 13.583  -13.001 112.739 1.00 46.57 ? 1216 OLA A C8    1 
HETATM 3236 C  C9    . OLA Q  4 .   ? 13.648  -12.746 111.251 1.00 57.02 ? 1216 OLA A C9    1 
HETATM 3237 C  C10   . OLA Q  4 .   ? 13.894  -11.374 110.778 1.00 55.92 ? 1216 OLA A C10   1 
HETATM 3238 C  C11   . OLA Q  4 .   ? 14.255  -10.320 111.800 1.00 54.20 ? 1216 OLA A C11   1 
HETATM 3239 C  C12   . OLA Q  4 .   ? 13.853  -8.934  111.323 1.00 56.06 ? 1216 OLA A C12   1 
HETATM 3240 C  C13   . OLA Q  4 .   ? 13.835  -8.855  109.806 1.00 47.83 ? 1216 OLA A C13   1 
HETATM 3241 C  C14   . OLA Q  4 .   ? 14.571  -7.604  109.345 1.00 60.68 ? 1216 OLA A C14   1 
HETATM 3242 C  C15   . OLA Q  4 .   ? 13.625  -6.429  109.143 1.00 50.07 ? 1216 OLA A C15   1 
HETATM 3243 C  C16   . OLA Q  4 .   ? 13.519  -6.077  107.668 1.00 48.33 ? 1216 OLA A C16   1 
HETATM 3244 C  C17   . OLA Q  4 .   ? 12.612  -4.874  107.469 1.00 46.93 ? 1216 OLA A C17   1 
HETATM 3245 C  C18   . OLA Q  4 .   ? 13.180  -3.673  108.219 1.00 55.77 ? 1216 OLA A C18   1 
HETATM 3246 C  C1    . OLA R  4 .   ? 1.168   12.865  135.844 1.00 59.17 ? 1217 OLA A C1    1 
HETATM 3247 O  O1    . OLA R  4 .   ? 1.231   13.126  134.616 1.00 51.73 ? 1217 OLA A O1    1 
HETATM 3248 O  O2    . OLA R  4 .   ? 1.167   13.798  136.680 1.00 64.88 ? 1217 OLA A O2    1 
HETATM 3249 C  C2    . OLA R  4 .   ? 1.099   11.441  136.335 1.00 50.78 ? 1217 OLA A C2    1 
HETATM 3250 C  C3    . OLA R  4 .   ? 2.432   10.773  136.049 1.00 46.52 ? 1217 OLA A C3    1 
HETATM 3251 C  C4    . OLA R  4 .   ? 2.472   9.401   136.710 1.00 46.38 ? 1217 OLA A C4    1 
HETATM 3252 C  C5    . OLA R  4 .   ? 1.089   8.792   136.889 1.00 38.43 ? 1217 OLA A C5    1 
HETATM 3253 C  C6    . OLA R  4 .   ? 0.969   7.429   136.199 1.00 38.46 ? 1217 OLA A C6    1 
HETATM 3254 C  C7    . OLA R  4 .   ? 2.319   6.902   135.729 1.00 43.09 ? 1217 OLA A C7    1 
HETATM 3255 C  C8    . OLA R  4 .   ? 2.488   5.433   136.080 1.00 38.03 ? 1217 OLA A C8    1 
HETATM 3256 C  C9    . OLA R  4 .   ? 1.275   4.928   136.815 1.00 41.25 ? 1217 OLA A C9    1 
HETATM 3257 C  C10   . OLA R  4 .   ? 1.079   3.485   136.903 1.00 41.85 ? 1217 OLA A C10   1 
HETATM 3258 C  C11   . OLA R  4 .   ? 0.507   2.834   138.136 1.00 42.68 ? 1217 OLA A C11   1 
HETATM 3259 C  C12   . OLA R  4 .   ? 1.284   1.547   138.432 1.00 50.41 ? 1217 OLA A C12   1 
HETATM 3260 C  C13   . OLA R  4 .   ? 0.881   0.370   137.538 1.00 51.78 ? 1217 OLA A C13   1 
HETATM 3261 C  C14   . OLA R  4 .   ? 1.881   -0.784  137.629 1.00 48.84 ? 1217 OLA A C14   1 
HETATM 3262 C  C1    . OLA S  4 .   ? -17.312 13.792  126.268 1.00 48.63 ? 1218 OLA A C1    1 
HETATM 3263 O  O1    . OLA S  4 .   ? -16.544 14.749  126.553 1.00 52.10 ? 1218 OLA A O1    1 
HETATM 3264 O  O2    . OLA S  4 .   ? -18.324 14.026  125.572 1.00 62.84 ? 1218 OLA A O2    1 
HETATM 3265 C  C2    . OLA S  4 .   ? -17.033 12.388  126.757 1.00 37.76 ? 1218 OLA A C2    1 
HETATM 3266 C  C3    . OLA S  4 .   ? -17.834 11.335  126.001 1.00 34.55 ? 1218 OLA A C3    1 
HETATM 3267 C  C4    . OLA S  4 .   ? -18.051 10.127  126.893 1.00 38.96 ? 1218 OLA A C4    1 
HETATM 3268 C  C5    . OLA S  4 .   ? -17.893 8.799   126.161 1.00 41.76 ? 1218 OLA A C5    1 
HETATM 3269 C  C6    . OLA S  4 .   ? -18.527 7.703   127.008 1.00 42.51 ? 1218 OLA A C6    1 
HETATM 3270 C  C7    . OLA S  4 .   ? -18.239 6.297   126.497 1.00 40.88 ? 1218 OLA A C7    1 
HETATM 3271 C  C8    . OLA S  4 .   ? -17.202 5.592   127.360 1.00 43.62 ? 1218 OLA A C8    1 
HETATM 3272 C  C9    . OLA S  4 .   ? -16.945 4.218   126.793 1.00 40.99 ? 1218 OLA A C9    1 
HETATM 3273 C  C10   . OLA S  4 .   ? -15.645 3.890   126.210 1.00 33.86 ? 1218 OLA A C10   1 
HETATM 3274 C  C11   . OLA S  4 .   ? -15.444 2.507   125.654 1.00 42.31 ? 1218 OLA A C11   1 
HETATM 3275 C  C12   . OLA S  4 .   ? -16.004 1.567   126.705 1.00 46.93 ? 1218 OLA A C12   1 
HETATM 3276 C  C13   . OLA S  4 .   ? -15.473 0.157   126.530 1.00 47.08 ? 1218 OLA A C13   1 
HETATM 3277 C  C14   . OLA S  4 .   ? -15.495 -0.281  125.078 1.00 49.76 ? 1218 OLA A C14   1 
HETATM 3278 C  C15   . OLA S  4 .   ? -15.277 -1.790  124.989 1.00 52.12 ? 1218 OLA A C15   1 
HETATM 3279 C  C16   . OLA S  4 .   ? -14.059 -2.238  125.788 1.00 55.29 ? 1218 OLA A C16   1 
HETATM 3280 C  C2    . OLA T  4 .   ? 20.008  12.721  130.377 1.00 55.37 ? 1219 OLA A C2    1 
HETATM 3281 C  C3    . OLA T  4 .   ? 19.106  11.494  130.471 1.00 47.94 ? 1219 OLA A C3    1 
HETATM 3282 C  C4    . OLA T  4 .   ? 19.902  10.217  130.252 1.00 53.13 ? 1219 OLA A C4    1 
HETATM 3283 C  C5    . OLA T  4 .   ? 20.945  10.093  131.348 1.00 53.69 ? 1219 OLA A C5    1 
HETATM 3284 C  C6    . OLA T  4 .   ? 21.818  8.878   131.107 1.00 50.56 ? 1219 OLA A C6    1 
HETATM 3285 C  C7    . OLA T  4 .   ? 21.121  7.615   131.585 1.00 49.84 ? 1219 OLA A C7    1 
HETATM 3286 C  C8    . OLA T  4 .   ? 22.178  6.667   132.139 1.00 52.35 ? 1219 OLA A C8    1 
HETATM 3287 C  C9    . OLA T  4 .   ? 21.683  5.243   132.082 1.00 53.35 ? 1219 OLA A C9    1 
HETATM 3288 C  C10   . OLA T  4 .   ? 22.634  4.130   132.250 1.00 56.18 ? 1219 OLA A C10   1 
HETATM 3289 C  C11   . OLA T  4 .   ? 22.165  2.737   131.898 1.00 57.49 ? 1219 OLA A C11   1 
HETATM 3290 C  C12   . OLA T  4 .   ? 23.169  2.032   130.993 1.00 58.50 ? 1219 OLA A C12   1 
HETATM 3291 C  C13   . OLA T  4 .   ? 22.644  0.653   130.605 1.00 56.42 ? 1219 OLA A C13   1 
HETATM 3292 C  C14   . OLA T  4 .   ? 23.788  -0.322  130.352 1.00 55.24 ? 1219 OLA A C14   1 
HETATM 3293 C  C15   . OLA T  4 .   ? 23.286  -1.751  130.173 1.00 52.07 ? 1219 OLA A C15   1 
HETATM 3294 C  C1    . OLA U  4 .   ? -15.989 8.194   109.276 1.00 57.19 ? 1220 OLA A C1    1 
HETATM 3295 O  O1    . OLA U  4 .   ? -15.738 8.402   108.068 1.00 63.97 ? 1220 OLA A O1    1 
HETATM 3296 O  O2    . OLA U  4 .   ? -15.834 9.127   110.101 1.00 52.77 ? 1220 OLA A O2    1 
HETATM 3297 C  C2    . OLA U  4 .   ? -16.480 6.832   109.706 1.00 47.15 ? 1220 OLA A C2    1 
HETATM 3298 C  C3    . OLA U  4 .   ? -15.497 6.253   110.705 1.00 47.89 ? 1220 OLA A C3    1 
HETATM 3299 C  C4    . OLA U  4 .   ? -14.789 5.022   110.149 1.00 51.58 ? 1220 OLA A C4    1 
HETATM 3300 C  C5    . OLA U  4 .   ? -15.730 3.875   109.823 1.00 45.81 ? 1220 OLA A C5    1 
HETATM 3301 C  C6    . OLA U  4 .   ? -15.437 2.677   110.725 1.00 46.75 ? 1220 OLA A C6    1 
HETATM 3302 C  C7    . OLA U  4 .   ? -15.057 1.442   109.925 1.00 41.08 ? 1220 OLA A C7    1 
HETATM 3303 C  C8    . OLA U  4 .   ? -15.638 0.169   110.544 1.00 45.63 ? 1220 OLA A C8    1 
HETATM 3304 C  C1    . OLA V  4 .   ? 15.041  9.236   106.506 1.00 60.19 ? 1221 OLA A C1    1 
HETATM 3305 O  O1    . OLA V  4 .   ? 14.585  10.390  106.267 1.00 63.31 ? 1221 OLA A O1    1 
HETATM 3306 O  O2    . OLA V  4 .   ? 16.278  9.048   106.427 1.00 63.84 ? 1221 OLA A O2    1 
HETATM 3307 C  C2    . OLA V  4 .   ? 14.115  8.085   106.863 1.00 49.92 ? 1221 OLA A C2    1 
HETATM 3308 C  C3    . OLA V  4 .   ? 14.873  6.920   107.494 1.00 52.68 ? 1221 OLA A C3    1 
HETATM 3309 C  C4    . OLA V  4 .   ? 14.789  5.619   106.701 1.00 46.78 ? 1221 OLA A C4    1 
HETATM 3310 C  C5    . OLA V  4 .   ? 13.700  4.698   107.249 1.00 50.90 ? 1221 OLA A C5    1 
HETATM 3311 C  C6    . OLA V  4 .   ? 14.033  3.226   107.033 1.00 54.88 ? 1221 OLA A C6    1 
HETATM 3312 C  C7    . OLA V  4 .   ? 13.948  2.449   108.346 1.00 52.92 ? 1221 OLA A C7    1 
HETATM 3313 C  C8    . OLA V  4 .   ? 14.949  1.292   108.408 1.00 49.54 ? 1221 OLA A C8    1 
HETATM 3314 C  C9    . OLA V  4 .   ? 14.744  0.448   109.650 1.00 48.91 ? 1221 OLA A C9    1 
HETATM 3315 C  C10   . OLA V  4 .   ? 15.252  -0.938  109.692 1.00 45.23 ? 1221 OLA A C10   1 
HETATM 3316 C  C11   . OLA V  4 .   ? 14.975  -1.825  110.879 1.00 47.48 ? 1221 OLA A C11   1 
HETATM 3317 C  C12   . OLA V  4 .   ? 15.614  -3.199  110.672 1.00 55.95 ? 1221 OLA A C12   1 
HETATM 3318 C  C13   . OLA V  4 .   ? 16.660  -3.517  111.738 1.00 57.69 ? 1221 OLA A C13   1 
HETATM 3319 C  C14   . OLA V  4 .   ? 16.227  -4.682  112.623 1.00 48.13 ? 1221 OLA A C14   1 
HETATM 3320 C  C15   . OLA V  4 .   ? 16.822  -6.012  112.174 1.00 52.33 ? 1221 OLA A C15   1 
HETATM 3321 C  C1    . OLA W  4 .   ? -4.216  13.240  138.937 1.00 51.10 ? 1222 OLA A C1    1 
HETATM 3322 O  O1    . OLA W  4 .   ? -3.746  14.348  138.567 1.00 54.19 ? 1222 OLA A O1    1 
HETATM 3323 O  O2    . OLA W  4 .   ? -5.381  13.176  139.392 1.00 59.55 ? 1222 OLA A O2    1 
HETATM 3324 C  C2    . OLA W  4 .   ? -3.401  11.975  138.846 1.00 50.83 ? 1222 OLA A C2    1 
HETATM 3325 C  C3    . OLA W  4 .   ? -4.301  10.773  139.116 1.00 43.23 ? 1222 OLA A C3    1 
HETATM 3326 C  C4    . OLA W  4 .   ? -3.414  9.531   139.173 1.00 51.38 ? 1222 OLA A C4    1 
HETATM 3327 C  C5    . OLA W  4 .   ? -4.204  8.247   138.920 1.00 56.32 ? 1222 OLA A C5    1 
HETATM 3328 C  C6    . OLA W  4 .   ? -3.279  7.066   138.610 1.00 48.22 ? 1222 OLA A C6    1 
HETATM 3329 C  C1    . OLA X  4 .   ? 14.414  10.123  137.072 1.00 66.78 ? 1223 OLA A C1    1 
HETATM 3330 O  O1    . OLA X  4 .   ? 14.319  10.855  136.053 1.00 61.72 ? 1223 OLA A O1    1 
HETATM 3331 O  O2    . OLA X  4 .   ? 14.668  10.676  138.161 1.00 84.80 ? 1223 OLA A O2    1 
HETATM 3332 C  C2    . OLA X  4 .   ? 14.251  8.616   137.005 1.00 49.59 ? 1223 OLA A C2    1 
HETATM 3333 C  C3    . OLA X  4 .   ? 14.249  7.963   138.386 1.00 47.43 ? 1223 OLA A C3    1 
HETATM 3334 C  C4    . OLA X  4 .   ? 15.441  7.020   138.442 1.00 49.41 ? 1223 OLA A C4    1 
HETATM 3335 C  C5    . OLA X  4 .   ? 15.227  5.862   139.398 1.00 42.58 ? 1223 OLA A C5    1 
HETATM 3336 C  C6    . OLA X  4 .   ? 15.016  4.558   138.635 1.00 49.27 ? 1223 OLA A C6    1 
HETATM 3337 C  C7    . OLA X  4 .   ? 14.862  3.371   139.585 1.00 49.26 ? 1223 OLA A C7    1 
HETATM 3338 C  C8    . OLA X  4 .   ? 13.940  2.286   139.014 1.00 47.68 ? 1223 OLA A C8    1 
HETATM 3339 C  C9    . OLA X  4 .   ? 13.299  1.505   140.145 1.00 39.28 ? 1223 OLA A C9    1 
HETATM 3340 C  C10   . OLA Y  4 .   ? -7.085  -3.523  132.279 1.00 59.89 ? 1224 OLA A C10   1 
HETATM 3341 C  C11   . OLA Y  4 .   ? -8.332  -2.868  131.716 1.00 50.74 ? 1224 OLA A C11   1 
HETATM 3342 C  C12   . OLA Y  4 .   ? -8.876  -1.802  132.664 1.00 57.24 ? 1224 OLA A C12   1 
HETATM 3343 C  C13   . OLA Y  4 .   ? -8.894  -0.414  132.014 1.00 61.68 ? 1224 OLA A C13   1 
HETATM 3344 C  C14   . OLA Y  4 .   ? -8.546  0.695   133.011 1.00 57.09 ? 1224 OLA A C14   1 
HETATM 3345 C  C15   . OLA Y  4 .   ? -9.205  2.043   132.686 1.00 54.73 ? 1224 OLA A C15   1 
HETATM 3346 C  C16   . OLA Y  4 .   ? -8.334  2.898   131.770 1.00 40.26 ? 1224 OLA A C16   1 
HETATM 3347 C  C17   . OLA Y  4 .   ? -6.852  2.661   132.047 1.00 40.06 ? 1224 OLA A C17   1 
HETATM 3348 C  C18   . OLA Y  4 .   ? -6.036  3.404   130.997 1.00 37.17 ? 1224 OLA A C18   1 
HETATM 3349 C  C1    . OLA Z  4 .   ? 12.537  14.504  131.996 1.00 67.89 ? 1225 OLA A C1    1 
HETATM 3350 O  O1    . OLA Z  4 .   ? 11.644  13.672  131.711 1.00 61.72 ? 1225 OLA A O1    1 
HETATM 3351 O  O2    . OLA Z  4 .   ? 12.175  15.678  132.240 1.00 75.79 ? 1225 OLA A O2    1 
HETATM 3352 C  C2    . OLA Z  4 .   ? 14.004  14.104  132.042 1.00 55.90 ? 1225 OLA A C2    1 
HETATM 3353 C  C3    . OLA Z  4 .   ? 14.150  12.595  131.855 1.00 60.23 ? 1225 OLA A C3    1 
HETATM 3354 C  C4    . OLA Z  4 .   ? 15.600  12.151  131.646 1.00 58.19 ? 1225 OLA A C4    1 
HETATM 3355 C  C5    . OLA Z  4 .   ? 15.660  10.709  131.125 1.00 52.94 ? 1225 OLA A C5    1 
HETATM 3356 C  C6    . OLA Z  4 .   ? 15.431  9.637   132.188 1.00 47.25 ? 1225 OLA A C6    1 
HETATM 3357 C  C7    . OLA Z  4 .   ? 16.735  8.903   132.465 1.00 53.27 ? 1225 OLA A C7    1 
HETATM 3358 C  C8    . OLA Z  4 .   ? 16.559  7.452   132.907 1.00 49.60 ? 1225 OLA A C8    1 
HETATM 3359 C  C9    . OLA Z  4 .   ? 16.852  7.362   134.387 1.00 51.59 ? 1225 OLA A C9    1 
HETATM 3360 C  C10   . OLA Z  4 .   ? 17.637  6.246   134.940 1.00 57.12 ? 1225 OLA A C10   1 
HETATM 3361 C  C11   . OLA Z  4 .   ? 17.716  4.910   134.233 1.00 52.03 ? 1225 OLA A C11   1 
HETATM 3362 C  C12   . OLA Z  4 .   ? 18.529  3.917   135.067 1.00 58.03 ? 1225 OLA A C12   1 
HETATM 3363 C  C13   . OLA Z  4 .   ? 18.181  2.464   134.742 1.00 64.51 ? 1225 OLA A C13   1 
HETATM 3364 C  C14   . OLA Z  4 .   ? 19.224  1.789   133.854 1.00 62.36 ? 1225 OLA A C14   1 
HETATM 3365 C  C1    . OLA AA 4 .   ? 8.112   -20.616 100.009 1.00 62.52 ? 1226 OLA A C1    1 
HETATM 3366 O  O1    . OLA AA 4 .   ? 7.555   -21.742 99.970  1.00 58.80 ? 1226 OLA A O1    1 
HETATM 3367 O  O2    . OLA AA 4 .   ? 9.212   -20.485 99.424  1.00 63.01 ? 1226 OLA A O2    1 
HETATM 3368 C  C2    . OLA AA 4 .   ? 7.474   -19.444 100.747 1.00 64.25 ? 1226 OLA A C2    1 
HETATM 3369 C  C3    . OLA AA 4 .   ? 7.519   -18.142 99.934  1.00 60.98 ? 1226 OLA A C3    1 
HETATM 3370 C  C4    . OLA AA 4 .   ? 7.697   -16.889 100.795 1.00 52.81 ? 1226 OLA A C4    1 
HETATM 3371 C  C5    . OLA AA 4 .   ? 6.550   -15.896 100.570 1.00 49.85 ? 1226 OLA A C5    1 
HETATM 3372 C  C6    . OLA AA 4 .   ? 5.292   -16.283 101.351 1.00 49.41 ? 1226 OLA A C6    1 
HETATM 3373 C  C7    . OLA AA 4 .   ? 4.366   -15.103 101.655 1.00 48.41 ? 1226 OLA A C7    1 
HETATM 3374 C  C8    . OLA AA 4 .   ? 5.075   -13.754 101.592 1.00 51.01 ? 1226 OLA A C8    1 
HETATM 3375 C  C9    . OLA AA 4 .   ? 4.038   -12.657 101.508 1.00 57.83 ? 1226 OLA A C9    1 
HETATM 3376 C  C10   . OLA AA 4 .   ? 4.174   -11.541 100.554 1.00 54.86 ? 1226 OLA A C10   1 
HETATM 3377 C  C11   . OLA AA 4 .   ? 4.549   -10.145 100.986 1.00 56.70 ? 1226 OLA A C11   1 
HETATM 3378 C  C12   . OLA AA 4 .   ? 3.683   -9.175  100.179 1.00 52.00 ? 1226 OLA A C12   1 
HETATM 3379 C  C13   . OLA AA 4 .   ? 4.008   -7.723  100.493 1.00 39.21 ? 1226 OLA A C13   1 
HETATM 3380 C  C14   . OLA AA 4 .   ? 2.790   -7.005  101.067 1.00 38.53 ? 1226 OLA A C14   1 
HETATM 3381 C  C15   . OLA AA 4 .   ? 3.086   -6.473  102.474 1.00 45.63 ? 1226 OLA A C15   1 
HETATM 3382 C  C16   . OLA AA 4 .   ? 2.112   -5.358  102.860 1.00 46.89 ? 1226 OLA A C16   1 
HETATM 3383 C  C17   . OLA AA 4 .   ? 2.383   -4.811  104.252 1.00 44.49 ? 1226 OLA A C17   1 
HETATM 3384 C  C18   . OLA AA 4 .   ? 2.869   -3.374  104.182 1.00 38.79 ? 1226 OLA A C18   1 
HETATM 3385 C  C1    . OLA BA 4 .   ? 8.364   -20.940 104.906 1.00 62.11 ? 1227 OLA A C1    1 
HETATM 3386 O  O1    . OLA BA 4 .   ? 7.113   -20.806 104.805 1.00 60.06 ? 1227 OLA A O1    1 
HETATM 3387 O  O2    . OLA BA 4 .   ? 8.848   -22.086 105.116 1.00 60.88 ? 1227 OLA A O2    1 
HETATM 3388 C  C2    . OLA BA 4 .   ? 9.267   -19.719 104.797 1.00 61.08 ? 1227 OLA A C2    1 
HETATM 3389 C  C3    . OLA BA 4 .   ? 9.882   -19.486 103.416 1.00 63.52 ? 1227 OLA A C3    1 
HETATM 3390 C  C4    . OLA BA 4 .   ? 11.077  -18.528 103.477 1.00 64.54 ? 1227 OLA A C4    1 
HETATM 3391 C  C5    . OLA BA 4 .   ? 10.669  -17.110 103.876 1.00 54.29 ? 1227 OLA A C5    1 
HETATM 3392 C  C6    . OLA BA 4 .   ? 11.702  -16.451 104.797 1.00 63.37 ? 1227 OLA A C6    1 
HETATM 3393 C  C7    . OLA BA 4 .   ? 11.736  -14.912 104.725 1.00 47.97 ? 1227 OLA A C7    1 
HETATM 3394 C  C8    . OLA BA 4 .   ? 10.821  -14.345 103.632 1.00 62.03 ? 1227 OLA A C8    1 
HETATM 3395 C  C9    . OLA BA 4 .   ? 10.976  -12.842 103.501 1.00 53.56 ? 1227 OLA A C9    1 
HETATM 3396 C  C10   . OLA BA 4 .   ? 9.880   -11.922 103.118 1.00 52.08 ? 1227 OLA A C10   1 
HETATM 3397 C  C11   . OLA BA 4 .   ? 8.414   -12.293 103.142 1.00 56.18 ? 1227 OLA A C11   1 
HETATM 3398 C  C12   . OLA BA 4 .   ? 7.542   -11.038 103.092 1.00 39.61 ? 1227 OLA A C12   1 
HETATM 3399 NA NA    . NA  CA 5 .   ? 3.821   -8.542  123.337 1.00 41.76 ? 1228 NA  A NA    1 
HETATM 3400 O  O     . HOH DA 6 .   ? -34.030 -62.038 124.308 1.00 58.19 ? 1301 HOH A O     1 
HETATM 3401 O  O     . HOH DA 6 .   ? -20.004 -50.926 117.859 1.00 50.93 ? 1302 HOH A O     1 
HETATM 3402 O  O     . HOH DA 6 .   ? 18.147  16.215  121.809 1.00 50.41 ? 1303 HOH A O     1 
HETATM 3403 O  O     . HOH DA 6 .   ? -9.296  9.281   105.260 1.00 45.52 ? 1304 HOH A O     1 
HETATM 3404 O  O     . HOH DA 6 .   ? -0.563  -35.757 113.150 1.00 45.05 ? 1305 HOH A O     1 
HETATM 3405 O  O     . HOH DA 6 .   ? -15.263 -37.712 119.137 1.00 45.86 ? 1306 HOH A O     1 
HETATM 3406 O  O     . HOH DA 6 .   ? -21.337 -46.750 119.162 1.00 50.83 ? 1307 HOH A O     1 
HETATM 3407 O  O     . HOH DA 6 .   ? 6.297   -12.147 114.363 1.00 25.51 ? 1308 HOH A O     1 
HETATM 3408 O  O     . HOH DA 6 .   ? -3.431  14.854  119.365 1.00 40.68 ? 1309 HOH A O     1 
HETATM 3409 O  O     . HOH DA 6 .   ? 3.670   15.027  106.681 1.00 34.31 ? 1310 HOH A O     1 
HETATM 3410 O  O     . HOH DA 6 .   ? -3.528  -17.015 120.839 1.00 25.32 ? 1311 HOH A O     1 
HETATM 3411 O  O     . HOH DA 6 .   ? -16.774 -64.650 119.577 1.00 43.00 ? 1312 HOH A O     1 
HETATM 3412 O  O     . HOH DA 6 .   ? 3.203   -28.249 118.442 1.00 39.81 ? 1313 HOH A O     1 
HETATM 3413 O  O     . HOH DA 6 .   ? 19.341  16.672  114.299 1.00 49.59 ? 1314 HOH A O     1 
HETATM 3414 O  O     . HOH DA 6 .   ? 5.058   23.442  109.852 1.00 42.88 ? 1315 HOH A O     1 
HETATM 3415 O  O     . HOH DA 6 .   ? 6.681   18.237  117.762 1.00 22.49 ? 1316 HOH A O     1 
HETATM 3416 O  O     . HOH DA 6 .   ? -3.491  0.376   127.272 1.00 18.09 ? 1317 HOH A O     1 
HETATM 3417 O  O     . HOH DA 6 .   ? -4.463  9.962   121.978 1.00 20.07 ? 1318 HOH A O     1 
HETATM 3418 O  O     . HOH DA 6 .   ? 3.155   0.277   124.238 1.00 35.89 ? 1319 HOH A O     1 
HETATM 3419 O  O     . HOH DA 6 .   ? 4.766   16.693  137.526 1.00 37.95 ? 1320 HOH A O     1 
HETATM 3420 O  O     . HOH DA 6 .   ? -0.866  -11.540 126.763 1.00 24.48 ? 1321 HOH A O     1 
HETATM 3421 O  O     . HOH DA 6 .   ? -0.327  -1.900  117.592 1.00 24.09 ? 1322 HOH A O     1 
HETATM 3422 O  O     . HOH DA 6 .   ? -0.732  9.841   117.052 1.00 31.40 ? 1323 HOH A O     1 
HETATM 3423 O  O     . HOH DA 6 .   ? 6.222   -12.289 118.329 1.00 23.63 ? 1324 HOH A O     1 
HETATM 3424 O  O     . HOH DA 6 .   ? -14.429 -31.577 115.393 1.00 46.83 ? 1325 HOH A O     1 
HETATM 3425 O  O     . HOH DA 6 .   ? 8.886   12.246  131.002 1.00 47.57 ? 1326 HOH A O     1 
HETATM 3426 O  O     . HOH DA 6 .   ? -6.829  -33.547 118.513 1.00 48.54 ? 1327 HOH A O     1 
HETATM 3427 O  O     . HOH DA 6 .   ? -6.541  17.513  128.449 1.00 44.48 ? 1328 HOH A O     1 
HETATM 3428 O  O     . HOH DA 6 .   ? -18.834 -62.834 119.805 1.00 38.85 ? 1329 HOH A O     1 
HETATM 3429 O  O     . HOH DA 6 .   ? 5.954   7.625   126.572 1.00 19.60 ? 1330 HOH A O     1 
HETATM 3430 O  O     . HOH DA 6 .   ? -15.167 -63.824 121.884 1.00 39.04 ? 1331 HOH A O     1 
HETATM 3431 O  O     . HOH DA 6 .   ? 8.882   2.448   120.198 1.00 24.32 ? 1332 HOH A O     1 
HETATM 3432 O  O     . HOH DA 6 .   ? -17.478 13.031  117.708 1.00 33.43 ? 1333 HOH A O     1 
HETATM 3433 O  O     . HOH DA 6 .   ? -1.374  12.604  116.188 1.00 29.49 ? 1334 HOH A O     1 
HETATM 3434 O  O     . HOH DA 6 .   ? -11.674 10.015  108.942 1.00 46.91 ? 1335 HOH A O     1 
HETATM 3435 O  O     . HOH DA 6 .   ? 5.632   -13.581 126.394 1.00 25.78 ? 1336 HOH A O     1 
HETATM 3436 O  O     . HOH DA 6 .   ? 7.976   2.831   122.833 1.00 19.79 ? 1337 HOH A O     1 
HETATM 3437 O  O     . HOH DA 6 .   ? -9.386  19.292  118.980 1.00 40.15 ? 1338 HOH A O     1 
HETATM 3438 O  O     . HOH DA 6 .   ? 2.648   -10.019 124.568 1.00 33.75 ? 1339 HOH A O     1 
HETATM 3439 O  O     . HOH DA 6 .   ? 5.436   14.331  132.265 1.00 49.37 ? 1340 HOH A O     1 
HETATM 3440 O  O     . HOH DA 6 .   ? -6.025  -28.194 120.169 1.00 42.40 ? 1341 HOH A O     1 
HETATM 3441 O  O     . HOH DA 6 .   ? 13.463  25.434  115.769 1.00 56.97 ? 1342 HOH A O     1 
HETATM 3442 O  O     . HOH DA 6 .   ? 5.499   2.378   123.951 1.00 21.01 ? 1343 HOH A O     1 
HETATM 3443 O  O     . HOH DA 6 .   ? -3.018  16.552  131.135 1.00 32.92 ? 1344 HOH A O     1 
HETATM 3444 O  O     . HOH DA 6 .   ? 3.751   -4.875  125.645 1.00 19.52 ? 1345 HOH A O     1 
HETATM 3445 O  O     . HOH DA 6 .   ? 1.256   -27.738 121.802 1.00 41.98 ? 1346 HOH A O     1 
HETATM 3446 O  O     . HOH DA 6 .   ? -5.405  -27.036 122.362 1.00 31.36 ? 1347 HOH A O     1 
HETATM 3447 O  O     . HOH DA 6 .   ? 6.115   18.598  114.987 1.00 24.92 ? 1348 HOH A O     1 
HETATM 3448 O  O     . HOH DA 6 .   ? 5.501   -16.063 125.266 1.00 26.07 ? 1349 HOH A O     1 
HETATM 3449 O  O     . HOH DA 6 .   ? -23.722 -47.426 113.454 1.00 47.80 ? 1350 HOH A O     1 
HETATM 3450 O  O     . HOH DA 6 .   ? 4.882   12.767  104.192 1.00 49.73 ? 1351 HOH A O     1 
HETATM 3451 O  O     . HOH DA 6 .   ? 4.167   -11.299 128.508 1.00 31.06 ? 1352 HOH A O     1 
HETATM 3452 O  O     . HOH DA 6 .   ? -8.320  11.905  124.200 1.00 21.79 ? 1353 HOH A O     1 
HETATM 3453 O  O     . HOH DA 6 .   ? -9.846  14.985  120.950 1.00 37.13 ? 1354 HOH A O     1 
HETATM 3454 O  O     . HOH DA 6 .   ? -9.405  14.696  114.653 1.00 37.02 ? 1355 HOH A O     1 
HETATM 3455 O  O     . HOH DA 6 .   ? 20.638  14.912  116.916 1.00 51.81 ? 1356 HOH A O     1 
HETATM 3456 O  O     . HOH DA 6 .   ? -6.973  -35.844 111.249 1.00 51.42 ? 1357 HOH A O     1 
HETATM 3457 O  O     . HOH DA 6 .   ? 8.372   5.336   121.899 1.00 30.01 ? 1358 HOH A O     1 
HETATM 3458 O  O     . HOH DA 6 .   ? -8.188  15.015  116.457 1.00 40.13 ? 1359 HOH A O     1 
HETATM 3459 O  O     . HOH DA 6 .   ? 1.123   -2.796  115.485 1.00 21.99 ? 1360 HOH A O     1 
HETATM 3460 O  O     . HOH DA 6 .   ? 8.141   20.616  117.403 1.00 25.80 ? 1361 HOH A O     1 
HETATM 3461 O  O     . HOH DA 6 .   ? 2.505   12.903  122.181 1.00 22.62 ? 1362 HOH A O     1 
HETATM 3462 O  O     . HOH DA 6 .   ? 1.055   -11.535 124.561 1.00 34.29 ? 1363 HOH A O     1 
HETATM 3463 O  O     . HOH DA 6 .   ? 2.361   -6.612  124.271 1.00 26.56 ? 1364 HOH A O     1 
HETATM 3464 O  O     . HOH DA 6 .   ? -23.015 -73.099 115.610 1.00 48.04 ? 1365 HOH A O     1 
HETATM 3465 O  O     . HOH DA 6 .   ? -9.003  -34.307 117.977 1.00 48.64 ? 1366 HOH A O     1 
HETATM 3466 O  O     . HOH DA 6 .   ? 7.319   16.391  128.057 1.00 51.22 ? 1367 HOH A O     1 
HETATM 3467 O  O     . HOH DA 6 .   ? 5.553   -29.693 117.114 1.00 46.16 ? 1368 HOH A O     1 
HETATM 3468 O  O     . HOH DA 6 .   ? -4.674  3.503   118.065 1.00 18.72 ? 1369 HOH A O     1 
HETATM 3469 O  O     . HOH DA 6 .   ? 6.076   -14.663 115.045 1.00 29.31 ? 1370 HOH A O     1 
HETATM 3470 O  O     . HOH DA 6 .   ? -14.421 17.312  126.824 1.00 53.90 ? 1371 HOH A O     1 
HETATM 3471 O  O     . HOH DA 6 .   ? 12.790  23.484  113.905 1.00 54.60 ? 1372 HOH A O     1 
HETATM 3472 O  O     . HOH DA 6 .   ? -1.430  -3.002  119.658 1.00 23.28 ? 1373 HOH A O     1 
HETATM 3473 O  O     . HOH DA 6 .   ? -15.492 -26.020 114.930 1.00 42.10 ? 1374 HOH A O     1 
HETATM 3474 O  O     . HOH DA 6 .   ? 5.116   11.439  123.433 1.00 22.71 ? 1375 HOH A O     1 
HETATM 3475 O  O     . HOH DA 6 .   ? -16.150 16.189  118.214 1.00 36.12 ? 1376 HOH A O     1 
HETATM 3476 O  O     . HOH DA 6 .   ? -1.743  -17.574 123.065 1.00 29.88 ? 1377 HOH A O     1 
HETATM 3477 O  O     . HOH DA 6 .   ? 7.668   -11.758 133.238 1.00 33.14 ? 1378 HOH A O     1 
HETATM 3478 O  O     . HOH DA 6 .   ? -1.246  15.451  122.049 1.00 42.50 ? 1379 HOH A O     1 
HETATM 3479 O  O     . HOH DA 6 .   ? -7.578  19.114  124.706 1.00 39.21 ? 1380 HOH A O     1 
HETATM 3480 O  O     . HOH DA 6 .   ? 4.515   9.059   124.610 1.00 21.83 ? 1381 HOH A O     1 
HETATM 3481 O  O     . HOH DA 6 .   ? -2.229  13.578  110.546 1.00 48.17 ? 1382 HOH A O     1 
HETATM 3482 O  O     . HOH DA 6 .   ? 5.208   -6.722  122.134 1.00 29.72 ? 1383 HOH A O     1 
HETATM 3483 O  O     . HOH DA 6 .   ? -2.184  14.992  133.726 1.00 33.78 ? 1384 HOH A O     1 
HETATM 3484 O  O     . HOH DA 6 .   ? -25.329 -76.093 113.244 1.00 35.68 ? 1385 HOH A O     1 
HETATM 3485 O  O     . HOH DA 6 .   ? 14.608  13.504  109.516 1.00 39.45 ? 1386 HOH A O     1 
HETATM 3486 O  O     . HOH DA 6 .   ? 16.326  18.533  123.656 1.00 45.99 ? 1387 HOH A O     1 
HETATM 3487 O  O     . HOH DA 6 .   ? -4.520  12.103  111.527 1.00 23.35 ? 1388 HOH A O     1 
HETATM 3488 O  O     . HOH DA 6 .   ? -2.520  14.892  127.533 1.00 47.97 ? 1389 HOH A O     1 
HETATM 3489 O  O     . HOH DA 6 .   ? 10.192  17.772  110.394 1.00 42.90 ? 1390 HOH A O     1 
HETATM 3490 O  O     . HOH DA 6 .   ? -2.354  13.346  113.968 1.00 33.99 ? 1391 HOH A O     1 
HETATM 3491 O  O     . HOH DA 6 .   ? 11.565  21.534  111.684 1.00 51.21 ? 1392 HOH A O     1 
HETATM 3492 O  O     . HOH DA 6 .   ? -1.166  -23.495 125.802 1.00 46.90 ? 1393 HOH A O     1 
HETATM 3493 O  O     . HOH DA 6 .   ? 4.863   -3.873  121.760 1.00 31.68 ? 1394 HOH A O     1 
HETATM 3494 O  O     . HOH DA 6 .   ? -2.401  11.927  107.165 1.00 43.50 ? 1395 HOH A O     1 
HETATM 3495 O  O     . HOH DA 6 .   ? -24.379 -47.096 115.568 1.00 47.91 ? 1396 HOH A O     1 
HETATM 3496 O  O     . HOH DA 6 .   ? -8.338  14.500  135.301 1.00 45.55 ? 1397 HOH A O     1 
HETATM 3497 O  O     . HOH DA 6 .   ? -13.842 -61.463 111.531 1.00 46.66 ? 1398 HOH A O     1 
HETATM 3498 O  O     . HOH DA 6 .   ? -10.543 13.370  123.030 1.00 25.60 ? 1399 HOH A O     1 
HETATM 3499 O  O     . HOH DA 6 .   ? -0.030  12.354  107.092 1.00 43.20 ? 1400 HOH A O     1 
HETATM 3500 O  O     . HOH DA 6 .   ? 10.731  20.152  136.073 1.00 44.16 ? 1401 HOH A O     1 
HETATM 3501 O  O     . HOH DA 6 .   ? -8.301  10.203  107.621 1.00 38.47 ? 1402 HOH A O     1 
HETATM 3502 O  O     . HOH DA 6 .   ? 1.093   12.056  105.061 1.00 45.27 ? 1403 HOH A O     1 
HETATM 3503 O  O     . HOH DA 6 .   ? 3.659   -15.809 113.334 1.00 37.62 ? 1404 HOH A O     1 
HETATM 3504 O  O     . HOH DA 6 .   ? -3.962  16.741  127.455 1.00 50.79 ? 1405 HOH A O     1 
HETATM 3505 O  O     . HOH DA 6 .   ? -25.831 -71.080 122.364 1.00 44.96 ? 1406 HOH A O     1 
HETATM 3506 O  O     . HOH DA 6 .   ? 4.082   15.195  134.554 1.00 52.24 ? 1407 HOH A O     1 
HETATM 3507 O  O     . HOH DA 6 .   ? -8.214  16.529  121.390 1.00 46.38 ? 1408 HOH A O     1 
HETATM 3508 O  O     . HOH DA 6 .   ? 7.914   29.336  112.462 1.00 53.24 ? 1409 HOH A O     1 
HETATM 3509 O  O     . HOH DA 6 .   ? 7.625   18.339  126.224 1.00 51.32 ? 1410 HOH A O     1 
HETATM 3510 O  O     . HOH DA 6 .   ? -17.088 16.350  115.440 1.00 52.36 ? 1411 HOH A O     1 
HETATM 3511 O  O     . HOH DA 6 .   ? 11.263  19.693  110.494 1.00 49.46 ? 1412 HOH A O     1 
HETATM 3512 O  O     . HOH DA 6 .   ? 1.987   15.271  122.409 1.00 39.93 ? 1413 HOH A O     1 
HETATM 3513 O  O     . HOH DA 6 .   ? 11.471  16.238  108.803 1.00 53.12 ? 1414 HOH A O     1 
HETATM 3514 O  O     . HOH DA 6 .   ? -6.056  13.476  116.022 1.00 33.35 ? 1415 HOH A O     1 
HETATM 3515 O  O     . HOH DA 6 .   ? -23.590 -75.779 117.149 1.00 42.40 ? 1416 HOH A O     1 
HETATM 3516 O  O     . HOH DA 6 .   ? 11.460  -22.261 142.696 1.00 35.51 ? 1417 HOH A O     1 
HETATM 3517 O  O     . HOH DA 6 .   ? 4.677   -2.650  124.286 1.00 32.71 ? 1418 HOH A O     1 
HETATM 3518 O  O     . HOH DA 6 .   ? 0.543   -21.508 124.697 1.00 47.08 ? 1419 HOH A O     1 
# 
