data_8RWD
# 
_entry.id   8RWD 
# 
_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   8RWD         pdb_00008rwd 10.2210/pdb8rwd/pdb 
WWPDB D_1292136156 ?            ?                   
# 
_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                        8RWD 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              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   ? ? ? ? 
2 non-polymer syn '1,3-diethyl-8-[(~{E})-2-(4-methoxy-3-oxidanyl-phenyl)ethenyl]-7-methyl-purine-2,6-dione' 370.402   1   ? ? ? ? 
3 non-polymer syn CHOLESTEROL                                                                               386.654   3   ? ? ? ? 
4 non-polymer syn 'OLEIC ACID'                                                                              282.461   26  ? ? ? ? 
5 non-polymer syn 'SODIUM ION'                                                                              22.990    1   ? ? ? ? 
6 water       nat water                                                                                     18.015    102 ? ? ? ? 
# 
_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 '1,3-diethyl-8-[(~{E})-2-(4-methoxy-3-oxidanyl-phenyl)ethenyl]-7-methyl-purine-2,6-dione' A1H3H 
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 
A1H3H non-polymer         . '1,3-diethyl-8-[(~{E})-2-(4-methoxy-3-oxidanyl-phenyl)ethenyl]-7-methyl-purine-2,6-dione' ? 
'C19 H22 N4 O4'  370.402 
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 
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 ?    ?   ?   A . n 
A 1 293 ASP 293 1060 ?    ?   ?   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        A1H3H 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H3H 
_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 A1H3H 1   1201 1201 A1H3H 3DM A . 
C  3 CLR   1   1202 1202 CLR   CLR A . 
D  3 CLR   1   1203 1203 CLR   CLR A . 
E  3 CLR   1   1204 1204 CLR   CLR A . 
F  4 OLA   1   1205 1205 OLA   OLA A . 
G  4 OLA   1   1206 1206 OLA   OLA 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 1214 OLA   OLA A . 
P  4 OLA   1   1215 1215 OLA   OLA A . 
Q  4 OLA   1   1216 1216 OLA   OLA A . 
R  4 OLA   1   1217 1217 OLA   OLA A . 
S  4 OLA   1   1218 1218 OLA   OLA A . 
T  4 OLA   1   1219 1219 OLA   OLA A . 
U  4 OLA   1   1220 1220 OLA   OLA A . 
V  4 OLA   1   1221 1221 OLA   OLA A . 
W  4 OLA   1   1222 1222 OLA   OLA A . 
X  4 OLA   1   1223 1223 OLA   OLA A . 
Y  4 OLA   1   1224 1224 OLA   OLA A . 
Z  4 OLA   1   1225 1225 OLA   OLA A . 
AA 4 OLA   1   1226 1226 OLA   OLA A . 
BA 4 OLA   1   1227 1227 OLA   OLA A . 
CA 4 OLA   1   1228 1228 OLA   OLA A . 
DA 4 OLA   1   1229 1229 OLA   OLA A . 
EA 4 OLA   1   1230 1230 OLA   OLA A . 
FA 5 NA    1   1231 1    NA    NA  A . 
GA 6 HOH   1   1301 89   HOH   HOH A . 
GA 6 HOH   2   1302 59   HOH   HOH A . 
GA 6 HOH   3   1303 96   HOH   HOH A . 
GA 6 HOH   4   1304 80   HOH   HOH A . 
GA 6 HOH   5   1305 31   HOH   HOH A . 
GA 6 HOH   6   1306 63   HOH   HOH A . 
GA 6 HOH   7   1307 54   HOH   HOH A . 
GA 6 HOH   8   1308 85   HOH   HOH A . 
GA 6 HOH   9   1309 23   HOH   HOH A . 
GA 6 HOH   10  1310 78   HOH   HOH A . 
GA 6 HOH   11  1311 93   HOH   HOH A . 
GA 6 HOH   12  1312 58   HOH   HOH A . 
GA 6 HOH   13  1313 17   HOH   HOH A . 
GA 6 HOH   14  1314 30   HOH   HOH A . 
GA 6 HOH   15  1315 69   HOH   HOH A . 
GA 6 HOH   16  1316 48   HOH   HOH A . 
GA 6 HOH   17  1317 40   HOH   HOH A . 
GA 6 HOH   18  1318 3    HOH   HOH A . 
GA 6 HOH   19  1319 100  HOH   HOH A . 
GA 6 HOH   20  1320 28   HOH   HOH A . 
GA 6 HOH   21  1321 83   HOH   HOH A . 
GA 6 HOH   22  1322 75   HOH   HOH A . 
GA 6 HOH   23  1323 19   HOH   HOH A . 
GA 6 HOH   24  1324 55   HOH   HOH A . 
GA 6 HOH   25  1325 16   HOH   HOH A . 
GA 6 HOH   26  1326 25   HOH   HOH A . 
GA 6 HOH   27  1327 14   HOH   HOH A . 
GA 6 HOH   28  1328 26   HOH   HOH A . 
GA 6 HOH   29  1329 73   HOH   HOH A . 
GA 6 HOH   30  1330 35   HOH   HOH A . 
GA 6 HOH   31  1331 22   HOH   HOH A . 
GA 6 HOH   32  1332 8    HOH   HOH A . 
GA 6 HOH   33  1333 86   HOH   HOH A . 
GA 6 HOH   34  1334 10   HOH   HOH A . 
GA 6 HOH   35  1335 2    HOH   HOH A . 
GA 6 HOH   36  1336 33   HOH   HOH A . 
GA 6 HOH   37  1337 61   HOH   HOH A . 
GA 6 HOH   38  1338 37   HOH   HOH A . 
GA 6 HOH   39  1339 12   HOH   HOH A . 
GA 6 HOH   40  1340 11   HOH   HOH A . 
GA 6 HOH   41  1341 4    HOH   HOH A . 
GA 6 HOH   42  1342 43   HOH   HOH A . 
GA 6 HOH   43  1343 1    HOH   HOH A . 
GA 6 HOH   44  1344 13   HOH   HOH A . 
GA 6 HOH   45  1345 72   HOH   HOH A . 
GA 6 HOH   46  1346 32   HOH   HOH A . 
GA 6 HOH   47  1347 39   HOH   HOH A . 
GA 6 HOH   48  1348 27   HOH   HOH A . 
GA 6 HOH   49  1349 49   HOH   HOH A . 
GA 6 HOH   50  1350 21   HOH   HOH A . 
GA 6 HOH   51  1351 41   HOH   HOH A . 
GA 6 HOH   52  1352 84   HOH   HOH A . 
GA 6 HOH   53  1353 5    HOH   HOH A . 
GA 6 HOH   54  1354 44   HOH   HOH A . 
GA 6 HOH   55  1355 68   HOH   HOH A . 
GA 6 HOH   56  1356 34   HOH   HOH A . 
GA 6 HOH   57  1357 18   HOH   HOH A . 
GA 6 HOH   58  1358 99   HOH   HOH A . 
GA 6 HOH   59  1359 15   HOH   HOH A . 
GA 6 HOH   60  1360 52   HOH   HOH A . 
GA 6 HOH   61  1361 65   HOH   HOH A . 
GA 6 HOH   62  1362 67   HOH   HOH A . 
GA 6 HOH   63  1363 6    HOH   HOH A . 
GA 6 HOH   64  1364 56   HOH   HOH A . 
GA 6 HOH   65  1365 20   HOH   HOH A . 
GA 6 HOH   66  1366 64   HOH   HOH A . 
GA 6 HOH   67  1367 46   HOH   HOH A . 
GA 6 HOH   68  1368 24   HOH   HOH A . 
GA 6 HOH   69  1369 102  HOH   HOH A . 
GA 6 HOH   70  1370 38   HOH   HOH A . 
GA 6 HOH   71  1371 42   HOH   HOH A . 
GA 6 HOH   72  1372 74   HOH   HOH A . 
GA 6 HOH   73  1373 7    HOH   HOH A . 
GA 6 HOH   74  1374 70   HOH   HOH A . 
GA 6 HOH   75  1375 92   HOH   HOH A . 
GA 6 HOH   76  1376 101  HOH   HOH A . 
GA 6 HOH   77  1377 60   HOH   HOH A . 
GA 6 HOH   78  1378 29   HOH   HOH A . 
GA 6 HOH   79  1379 62   HOH   HOH A . 
GA 6 HOH   80  1380 95   HOH   HOH A . 
GA 6 HOH   81  1381 90   HOH   HOH A . 
GA 6 HOH   82  1382 87   HOH   HOH A . 
GA 6 HOH   83  1383 71   HOH   HOH A . 
GA 6 HOH   84  1384 36   HOH   HOH A . 
GA 6 HOH   85  1385 51   HOH   HOH A . 
GA 6 HOH   86  1386 9    HOH   HOH A . 
GA 6 HOH   87  1387 47   HOH   HOH A . 
GA 6 HOH   88  1388 66   HOH   HOH A . 
GA 6 HOH   89  1389 45   HOH   HOH A . 
GA 6 HOH   90  1390 79   HOH   HOH A . 
GA 6 HOH   91  1391 91   HOH   HOH A . 
GA 6 HOH   92  1392 97   HOH   HOH A . 
GA 6 HOH   93  1393 98   HOH   HOH A . 
GA 6 HOH   94  1394 57   HOH   HOH A . 
GA 6 HOH   95  1395 53   HOH   HOH A . 
GA 6 HOH   96  1396 77   HOH   HOH A . 
GA 6 HOH   97  1397 81   HOH   HOH A . 
GA 6 HOH   98  1398 88   HOH   HOH A . 
GA 6 HOH   99  1399 76   HOH   HOH A . 
GA 6 HOH   100 1400 82   HOH   HOH A . 
GA 6 HOH   101 1401 50   HOH   HOH A . 
GA 6 HOH   102 1402 94   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 LYS 1015 ? CD  ? A  LYS 248 CD  
2   1 Y 1 A LYS 1015 ? CE  ? A  LYS 248 CE  
3   1 Y 1 A LYS 1015 ? NZ  ? A  LYS 248 NZ  
4   1 Y 1 A LYS 1042 ? CG  ? A  LYS 275 CG  
5   1 Y 1 A LYS 1042 ? CD  ? A  LYS 275 CD  
6   1 Y 1 A LYS 1042 ? CE  ? A  LYS 275 CE  
7   1 Y 1 A LYS 1042 ? NZ  ? A  LYS 275 NZ  
8   1 Y 1 A PHE 1061 ? CG  ? A  PHE 294 CG  
9   1 Y 1 A PHE 1061 ? CD1 ? A  PHE 294 CD1 
10  1 Y 1 A PHE 1061 ? CD2 ? A  PHE 294 CD2 
11  1 Y 1 A PHE 1061 ? CE1 ? A  PHE 294 CE1 
12  1 Y 1 A PHE 1061 ? CE2 ? A  PHE 294 CE2 
13  1 Y 1 A PHE 1061 ? CZ  ? A  PHE 294 CZ  
14  1 Y 1 A ARG 1062 ? CG  ? A  ARG 295 CG  
15  1 Y 1 A ARG 1062 ? CD  ? A  ARG 295 CD  
16  1 Y 1 A ARG 1062 ? NE  ? A  ARG 295 NE  
17  1 Y 1 A ARG 1062 ? CZ  ? A  ARG 295 CZ  
18  1 Y 1 A ARG 1062 ? NH1 ? A  ARG 295 NH1 
19  1 Y 1 A ARG 1062 ? NH2 ? A  ARG 295 NH2 
20  1 Y 1 A LYS 1077 ? CE  ? A  LYS 310 CE  
21  1 Y 1 A LYS 1077 ? NZ  ? A  LYS 310 NZ  
22  1 Y 1 A TYR 1101 ? CD1 ? A  TYR 334 CD1 
23  1 Y 1 A TYR 1101 ? CD2 ? A  TYR 334 CD2 
24  1 Y 1 A TYR 1101 ? CE1 ? A  TYR 334 CE1 
25  1 Y 1 A TYR 1101 ? CE2 ? A  TYR 334 CE2 
26  1 Y 1 A TYR 1101 ? CZ  ? A  TYR 334 CZ  
27  1 Y 1 A TYR 1101 ? OH  ? A  TYR 334 OH  
28  1 Y 1 A LYS 1104 ? CG  ? A  LYS 337 CG  
29  1 Y 1 A LYS 1104 ? CD  ? A  LYS 337 CD  
30  1 Y 1 A LYS 1104 ? CE  ? A  LYS 337 CE  
31  1 Y 1 A LYS 1104 ? NZ  ? A  LYS 337 NZ  
32  1 Y 1 A TYR 1105 ? CD1 ? A  TYR 338 CD1 
33  1 Y 1 A TYR 1105 ? CD2 ? A  TYR 338 CD2 
34  1 Y 1 A TYR 1105 ? CE1 ? A  TYR 338 CE1 
35  1 Y 1 A TYR 1105 ? CE2 ? A  TYR 338 CE2 
36  1 Y 1 A TYR 1105 ? CZ  ? A  TYR 338 CZ  
37  1 Y 1 A TYR 1105 ? OH  ? A  TYR 338 OH  
38  1 Y 1 A ARG 220  ? CG  ? A  ARG 341 CG  
39  1 Y 1 A ARG 220  ? CD  ? A  ARG 341 CD  
40  1 Y 1 A ARG 220  ? NE  ? A  ARG 341 NE  
41  1 Y 1 A ARG 220  ? CZ  ? A  ARG 341 CZ  
42  1 Y 1 A ARG 220  ? NH1 ? A  ARG 341 NH1 
43  1 Y 1 A ARG 220  ? NH2 ? A  ARG 341 NH2 
44  1 Y 1 A LYS 233  ? CG  ? A  LYS 354 CG  
45  1 Y 1 A LYS 233  ? CD  ? A  LYS 354 CD  
46  1 Y 1 A LYS 233  ? CE  ? A  LYS 354 CE  
47  1 Y 1 A LYS 233  ? NZ  ? A  LYS 354 NZ  
48  1 Y 1 A ARG 293  ? NE  ? A  ARG 414 NE  
49  1 Y 1 A ARG 293  ? CZ  ? A  ARG 414 CZ  
50  1 Y 1 A ARG 293  ? NH1 ? A  ARG 414 NH1 
51  1 Y 1 A ARG 293  ? NH2 ? A  ARG 414 NH2 
52  1 N 1 A OLA 1205 ? C16 ? F  OLA 1   C16 
53  1 N 1 A OLA 1205 ? C17 ? F  OLA 1   C17 
54  1 N 1 A OLA 1205 ? C18 ? F  OLA 1   C18 
55  1 N 1 A OLA 1207 ? C14 ? H  OLA 1   C14 
56  1 N 1 A OLA 1207 ? C15 ? H  OLA 1   C15 
57  1 N 1 A OLA 1207 ? C16 ? H  OLA 1   C16 
58  1 N 1 A OLA 1207 ? C17 ? H  OLA 1   C17 
59  1 N 1 A OLA 1207 ? C18 ? H  OLA 1   C18 
60  1 N 1 A OLA 1208 ? C16 ? I  OLA 1   C16 
61  1 N 1 A OLA 1208 ? C17 ? I  OLA 1   C17 
62  1 N 1 A OLA 1208 ? C18 ? I  OLA 1   C18 
63  1 N 1 A OLA 1209 ? C1  ? J  OLA 1   C1  
64  1 N 1 A OLA 1209 ? O1  ? J  OLA 1   O1  
65  1 N 1 A OLA 1209 ? O2  ? J  OLA 1   O2  
66  1 N 1 A OLA 1209 ? C2  ? J  OLA 1   C2  
67  1 N 1 A OLA 1209 ? C3  ? J  OLA 1   C3  
68  1 N 1 A OLA 1209 ? C4  ? J  OLA 1   C4  
69  1 N 1 A OLA 1209 ? C5  ? J  OLA 1   C5  
70  1 N 1 A OLA 1209 ? C6  ? J  OLA 1   C6  
71  1 N 1 A OLA 1209 ? C7  ? J  OLA 1   C7  
72  1 N 1 A OLA 1209 ? C8  ? J  OLA 1   C8  
73  1 N 1 A OLA 1211 ? C12 ? L  OLA 1   C12 
74  1 N 1 A OLA 1211 ? C13 ? L  OLA 1   C13 
75  1 N 1 A OLA 1211 ? C14 ? L  OLA 1   C14 
76  1 N 1 A OLA 1211 ? C15 ? L  OLA 1   C15 
77  1 N 1 A OLA 1211 ? C16 ? L  OLA 1   C16 
78  1 N 1 A OLA 1211 ? C17 ? L  OLA 1   C17 
79  1 N 1 A OLA 1211 ? C18 ? L  OLA 1   C18 
80  1 N 1 A OLA 1212 ? C15 ? M  OLA 1   C15 
81  1 N 1 A OLA 1212 ? C16 ? M  OLA 1   C16 
82  1 N 1 A OLA 1212 ? C17 ? M  OLA 1   C17 
83  1 N 1 A OLA 1212 ? C18 ? M  OLA 1   C18 
84  1 N 1 A OLA 1213 ? C12 ? N  OLA 1   C12 
85  1 N 1 A OLA 1213 ? C13 ? N  OLA 1   C13 
86  1 N 1 A OLA 1213 ? C14 ? N  OLA 1   C14 
87  1 N 1 A OLA 1213 ? C15 ? N  OLA 1   C15 
88  1 N 1 A OLA 1213 ? C16 ? N  OLA 1   C16 
89  1 N 1 A OLA 1213 ? C17 ? N  OLA 1   C17 
90  1 N 1 A OLA 1213 ? C18 ? N  OLA 1   C18 
91  1 N 1 A OLA 1214 ? C12 ? O  OLA 1   C12 
92  1 N 1 A OLA 1214 ? C13 ? O  OLA 1   C13 
93  1 N 1 A OLA 1214 ? C14 ? O  OLA 1   C14 
94  1 N 1 A OLA 1214 ? C15 ? O  OLA 1   C15 
95  1 N 1 A OLA 1214 ? C16 ? O  OLA 1   C16 
96  1 N 1 A OLA 1214 ? C17 ? O  OLA 1   C17 
97  1 N 1 A OLA 1214 ? C18 ? O  OLA 1   C18 
98  1 N 1 A OLA 1215 ? C12 ? P  OLA 1   C12 
99  1 N 1 A OLA 1215 ? C13 ? P  OLA 1   C13 
100 1 N 1 A OLA 1215 ? C14 ? P  OLA 1   C14 
101 1 N 1 A OLA 1215 ? C15 ? P  OLA 1   C15 
102 1 N 1 A OLA 1215 ? C16 ? P  OLA 1   C16 
103 1 N 1 A OLA 1215 ? C17 ? P  OLA 1   C17 
104 1 N 1 A OLA 1215 ? C18 ? P  OLA 1   C18 
105 1 N 1 A OLA 1216 ? C9  ? Q  OLA 1   C9  
106 1 N 1 A OLA 1216 ? C10 ? Q  OLA 1   C10 
107 1 N 1 A OLA 1216 ? C11 ? Q  OLA 1   C11 
108 1 N 1 A OLA 1216 ? C12 ? Q  OLA 1   C12 
109 1 N 1 A OLA 1216 ? C13 ? Q  OLA 1   C13 
110 1 N 1 A OLA 1216 ? C14 ? Q  OLA 1   C14 
111 1 N 1 A OLA 1216 ? C15 ? Q  OLA 1   C15 
112 1 N 1 A OLA 1216 ? C16 ? Q  OLA 1   C16 
113 1 N 1 A OLA 1216 ? C17 ? Q  OLA 1   C17 
114 1 N 1 A OLA 1216 ? C18 ? Q  OLA 1   C18 
115 1 N 1 A OLA 1217 ? C18 ? R  OLA 1   C18 
116 1 N 1 A OLA 1218 ? C11 ? S  OLA 1   C11 
117 1 N 1 A OLA 1218 ? C12 ? S  OLA 1   C12 
118 1 N 1 A OLA 1218 ? C13 ? S  OLA 1   C13 
119 1 N 1 A OLA 1218 ? C14 ? S  OLA 1   C14 
120 1 N 1 A OLA 1218 ? C15 ? S  OLA 1   C15 
121 1 N 1 A OLA 1218 ? C16 ? S  OLA 1   C16 
122 1 N 1 A OLA 1218 ? C17 ? S  OLA 1   C17 
123 1 N 1 A OLA 1218 ? C18 ? S  OLA 1   C18 
124 1 N 1 A OLA 1220 ? C1  ? U  OLA 1   C1  
125 1 N 1 A OLA 1220 ? O1  ? U  OLA 1   O1  
126 1 N 1 A OLA 1220 ? O2  ? U  OLA 1   O2  
127 1 N 1 A OLA 1220 ? C2  ? U  OLA 1   C2  
128 1 N 1 A OLA 1220 ? C3  ? U  OLA 1   C3  
129 1 N 1 A OLA 1220 ? C4  ? U  OLA 1   C4  
130 1 N 1 A OLA 1220 ? C5  ? U  OLA 1   C5  
131 1 N 1 A OLA 1220 ? C18 ? U  OLA 1   C18 
132 1 N 1 A OLA 1221 ? C17 ? V  OLA 1   C17 
133 1 N 1 A OLA 1221 ? C18 ? V  OLA 1   C18 
134 1 N 1 A OLA 1222 ? C1  ? W  OLA 1   C1  
135 1 N 1 A OLA 1222 ? O1  ? W  OLA 1   O1  
136 1 N 1 A OLA 1222 ? O2  ? W  OLA 1   O2  
137 1 N 1 A OLA 1222 ? C2  ? W  OLA 1   C2  
138 1 N 1 A OLA 1222 ? C3  ? W  OLA 1   C3  
139 1 N 1 A OLA 1222 ? C4  ? W  OLA 1   C4  
140 1 N 1 A OLA 1222 ? C5  ? W  OLA 1   C5  
141 1 N 1 A OLA 1222 ? C6  ? W  OLA 1   C6  
142 1 N 1 A OLA 1222 ? C7  ? W  OLA 1   C7  
143 1 N 1 A OLA 1222 ? C8  ? W  OLA 1   C8  
144 1 N 1 A OLA 1222 ? C9  ? W  OLA 1   C9  
145 1 N 1 A OLA 1222 ? C18 ? W  OLA 1   C18 
146 1 N 1 A OLA 1223 ? C1  ? X  OLA 1   C1  
147 1 N 1 A OLA 1223 ? O1  ? X  OLA 1   O1  
148 1 N 1 A OLA 1223 ? O2  ? X  OLA 1   O2  
149 1 N 1 A OLA 1223 ? C2  ? X  OLA 1   C2  
150 1 N 1 A OLA 1223 ? C3  ? X  OLA 1   C3  
151 1 N 1 A OLA 1224 ? C12 ? Y  OLA 1   C12 
152 1 N 1 A OLA 1224 ? C13 ? Y  OLA 1   C13 
153 1 N 1 A OLA 1224 ? C14 ? Y  OLA 1   C14 
154 1 N 1 A OLA 1224 ? C15 ? Y  OLA 1   C15 
155 1 N 1 A OLA 1224 ? C16 ? Y  OLA 1   C16 
156 1 N 1 A OLA 1224 ? C17 ? Y  OLA 1   C17 
157 1 N 1 A OLA 1224 ? C18 ? Y  OLA 1   C18 
158 1 N 1 A OLA 1225 ? C14 ? Z  OLA 1   C14 
159 1 N 1 A OLA 1225 ? C15 ? Z  OLA 1   C15 
160 1 N 1 A OLA 1225 ? C16 ? Z  OLA 1   C16 
161 1 N 1 A OLA 1225 ? C17 ? Z  OLA 1   C17 
162 1 N 1 A OLA 1225 ? C18 ? Z  OLA 1   C18 
163 1 N 1 A OLA 1228 ? C11 ? CA OLA 1   C11 
164 1 N 1 A OLA 1228 ? C12 ? CA OLA 1   C12 
165 1 N 1 A OLA 1228 ? C13 ? CA OLA 1   C13 
166 1 N 1 A OLA 1228 ? C14 ? CA OLA 1   C14 
167 1 N 1 A OLA 1228 ? C15 ? CA OLA 1   C15 
168 1 N 1 A OLA 1228 ? C16 ? CA OLA 1   C16 
169 1 N 1 A OLA 1228 ? C17 ? CA OLA 1   C17 
170 1 N 1 A OLA 1228 ? C18 ? CA OLA 1   C18 
171 1 N 1 A OLA 1229 ? C1  ? DA OLA 1   C1  
172 1 N 1 A OLA 1229 ? O1  ? DA OLA 1   O1  
173 1 N 1 A OLA 1229 ? O2  ? DA OLA 1   O2  
174 1 N 1 A OLA 1229 ? C2  ? DA OLA 1   C2  
175 1 N 1 A OLA 1229 ? C13 ? DA OLA 1   C13 
176 1 N 1 A OLA 1229 ? C14 ? DA OLA 1   C14 
177 1 N 1 A OLA 1229 ? C15 ? DA OLA 1   C15 
178 1 N 1 A OLA 1229 ? C16 ? DA OLA 1   C16 
179 1 N 1 A OLA 1229 ? C17 ? DA OLA 1   C17 
180 1 N 1 A OLA 1229 ? C18 ? DA OLA 1   C18 
181 1 N 1 A OLA 1230 ? O1  ? EA OLA 1   O1  
182 1 N 1 A OLA 1230 ? O2  ? EA OLA 1   O2  
183 1 N 1 A OLA 1230 ? C10 ? EA OLA 1   C10 
184 1 N 1 A OLA 1230 ? C11 ? EA OLA 1   C11 
185 1 N 1 A OLA 1230 ? C12 ? EA OLA 1   C12 
186 1 N 1 A OLA 1230 ? C13 ? EA OLA 1   C13 
187 1 N 1 A OLA 1230 ? C14 ? EA OLA 1   C14 
188 1 N 1 A OLA 1230 ? C15 ? EA OLA 1   C15 
189 1 N 1 A OLA 1230 ? C16 ? EA OLA 1   C16 
190 1 N 1 A OLA 1230 ? C17 ? EA OLA 1   C17 
191 1 N 1 A OLA 1230 ? C18 ? EA 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                     8RWD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     39.327 
_cell.length_a_esd                 ? 
_cell.length_b                     179.010 
_cell.length_b_esd                 ? 
_cell.length_c                     139.328 
_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                         8RWD 
_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                   8RWD 
_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             2.46 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.01 
_exptl_crystal.description                  'Square plate' 
_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         2021-09-06 
_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 X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RWD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.05 
_reflns.d_resolution_low                               46.44 
_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                                     31499 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                33.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.1 
_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                                0.027 
_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                                   ? 
_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                                    2.05 
_reflns_shell.d_res_low                                     2.11 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2346 
_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                               8.4 
_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                               0.468 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.617 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.6 
_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                                 8RWD 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.05 
_refine.ls_d_res_low                             41.22 
_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                     31452 
_refine.ls_number_reflns_R_free                  1564 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.82 
_refine.ls_percent_reflns_R_free                 4.97 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1943 
_refine.ls_R_factor_R_free                       0.2095 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1935 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.44 
_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                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.05 
_refine_hist.d_res_low                        41.22 
_refine_hist.number_atoms_solvent             102 
_refine_hist.number_atoms_total               3513 
_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        2919 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         492 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003  ? 3537 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.725  ? 4721 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.085 ? 802  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.044  ? 526  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 577  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.05 2.12  . . 134 2607 98.00  . . . . 0.2582 . . . . . . . . . . . 0.2790 
'X-RAY DIFFRACTION' 2.12 2.19  . . 151 2712 100.00 . . . . 0.2296 . . . . . . . . . . . 0.2628 
'X-RAY DIFFRACTION' 2.19 2.28  . . 147 2655 100.00 . . . . 0.2096 . . . . . . . . . . . 0.2400 
'X-RAY DIFFRACTION' 2.28 2.38  . . 139 2682 100.00 . . . . 0.1971 . . . . . . . . . . . 0.2359 
'X-RAY DIFFRACTION' 2.38 2.51  . . 137 2694 100.00 . . . . 0.1933 . . . . . . . . . . . 0.2408 
'X-RAY DIFFRACTION' 2.51 2.67  . . 116 2713 100.00 . . . . 0.1897 . . . . . . . . . . . 0.1938 
'X-RAY DIFFRACTION' 2.67 2.87  . . 171 2694 100.00 . . . . 0.1969 . . . . . . . . . . . 0.2294 
'X-RAY DIFFRACTION' 2.87 3.16  . . 139 2716 100.00 . . . . 0.2019 . . . . . . . . . . . 0.2194 
'X-RAY DIFFRACTION' 3.16 3.62  . . 158 2723 100.00 . . . . 0.1902 . . . . . . . . . . . 0.2306 
'X-RAY DIFFRACTION' 3.62 4.56  . . 137 2771 100.00 . . . . 0.1701 . . . . . . . . . . . 0.1787 
'X-RAY DIFFRACTION' 4.56 41.22 . . 135 2921 100.00 . . . . 0.1944 . . . . . . . . . . . 0.1761 
# 
_struct.entry_id                     8RWD 
_struct.title                        
;Crystal structure of the adenosine A2A receptor in complex with the synthetic photoswitch 'StilSwitch3
;
_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        8RWD 
_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 3 ? 
F  N N 4 ? 
G  N N 4 ? 
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 4 ? 
DA N N 4 ? 
EA N N 4 ? 
FA N N 5 ? 
GA 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 8RWD A 27  ? 233 ? P29274 2   ? 208 ? 2    208  
2 2 8RWD A 234 ? 338 ? P0ABE7 23  ? 127 ? 1001 1105 
3 3 8RWD 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 8RWD MET A 1   ? UNP P29274 ?   ?   'initiating methionine' -24  1  
1 8RWD LYS A 2   ? UNP P29274 ?   ?   'expression tag'        -23  2  
1 8RWD THR A 3   ? UNP P29274 ?   ?   'expression tag'        -22  3  
1 8RWD ILE A 4   ? UNP P29274 ?   ?   'expression tag'        -21  4  
1 8RWD ILE A 5   ? UNP P29274 ?   ?   'expression tag'        -20  5  
1 8RWD ALA A 6   ? UNP P29274 ?   ?   'expression tag'        -19  6  
1 8RWD LEU A 7   ? UNP P29274 ?   ?   'expression tag'        -18  7  
1 8RWD SER A 8   ? UNP P29274 ?   ?   'expression tag'        -17  8  
1 8RWD TYR A 9   ? UNP P29274 ?   ?   'expression tag'        -16  9  
1 8RWD ILE A 10  ? UNP P29274 ?   ?   'expression tag'        -15  10 
1 8RWD PHE A 11  ? UNP P29274 ?   ?   'expression tag'        -14  11 
1 8RWD CYS A 12  ? UNP P29274 ?   ?   'expression tag'        -13  12 
1 8RWD LEU A 13  ? UNP P29274 ?   ?   'expression tag'        -12  13 
1 8RWD VAL A 14  ? UNP P29274 ?   ?   'expression tag'        -11  14 
1 8RWD PHE A 15  ? UNP P29274 ?   ?   'expression tag'        -10  15 
1 8RWD ALA A 16  ? UNP P29274 ?   ?   'expression tag'        -9   16 
1 8RWD ASP A 17  ? UNP P29274 ?   ?   'expression tag'        -8   17 
1 8RWD TYR A 18  ? UNP P29274 ?   ?   'expression tag'        -7   18 
1 8RWD LYS A 19  ? UNP P29274 ?   ?   'expression tag'        -6   19 
1 8RWD ASP A 20  ? UNP P29274 ?   ?   'expression tag'        -5   20 
1 8RWD ASP A 21  ? UNP P29274 ?   ?   'expression tag'        -4   21 
1 8RWD ASP A 22  ? UNP P29274 ?   ?   'expression tag'        -3   22 
1 8RWD ASP A 23  ? UNP P29274 ?   ?   'expression tag'        -2   23 
1 8RWD GLY A 24  ? UNP P29274 ?   ?   'expression tag'        -1   24 
1 8RWD ALA A 25  ? UNP P29274 ?   ?   'expression tag'        0    25 
1 8RWD PRO A 26  ? UNP P29274 ?   ?   'expression tag'        1    26 
1 8RWD LEU A 79  ? UNP P29274 ALA 54  conflict                54   27 
1 8RWD ALA A 113 ? UNP P29274 THR 88  conflict                88   28 
1 8RWD ALA A 132 ? UNP P29274 ARG 107 conflict                107  29 
1 8RWD ALA A 147 ? UNP P29274 LYS 122 conflict                122  30 
1 8RWD ALA A 179 ? UNP P29274 ASN 154 conflict                154  31 
1 8RWD ALA A 227 ? UNP P29274 LEU 202 conflict                202  32 
2 8RWD TRP A 240 ? UNP P0ABE7 MET 29  conflict                1007 33 
2 8RWD ILE A 335 ? UNP P0ABE7 HIS 124 conflict                1102 34 
2 8RWD LEU A 339 ? UNP P0ABE7 ?   ?   linker                  1106 35 
3 8RWD ALA A 356 ? UNP P29274 LEU 235 conflict                235  36 
3 8RWD ALA A 360 ? UNP P29274 VAL 239 conflict                239  37 
3 8RWD ALA A 439 ? UNP P29274 ?   ?   'expression tag'        318  38 
3 8RWD HIS A 440 ? UNP P29274 ?   ?   'expression tag'        319  39 
3 8RWD HIS A 441 ? UNP P29274 ?   ?   'expression tag'        320  40 
3 8RWD HIS A 442 ? UNP P29274 ?   ?   'expression tag'        321  41 
3 8RWD HIS A 443 ? UNP P29274 ?   ?   'expression tag'        322  42 
3 8RWD HIS A 444 ? UNP P29274 ?   ?   'expression tag'        323  43 
3 8RWD HIS A 445 ? UNP P29274 ?   ?   'expression tag'        324  44 
3 8RWD HIS A 446 ? UNP P29274 ?   ?   'expression tag'        325  45 
3 8RWD HIS A 447 ? UNP P29274 ?   ?   'expression tag'        326  46 
3 8RWD HIS A 448 ? UNP P29274 ?   ?   'expression tag'        327  47 
3 8RWD 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)' 14040 ? 
1 MORE         59    ? 
1 'SSA (A^2)'  18870 ? 
# 
_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,EA,FA,GA 
# 
_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 ARG A 136 ? VAL A 141 ? ARG A 111  VAL A 116  1 ? 6  
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 ARG A 295 ? GLU A 314 ? ARG A 1062 GLU A 1081 1 ? 20 
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 ? ? ? ? ? ? ? 2.034 ? ? 
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 ? ? ? ? ? ? ? 2.035 ? ? 
disulf4 disulf ? ? A  CYS 380 SG  ? ? ? 1_555 A  CYS 383 SG ? ? A CYS 259  A CYS 262  1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc1 metalc ? ? A  ASP 77  OD1 ? ? ? 1_555 FA NA  .   NA ? ? A ASP 52   A NA  1231 1_555 ? ? ? ? ? ? ? 2.564 ? ? 
metalc2 metalc ? ? A  SER 116 OG  ? ? ? 1_555 FA NA  .   NA ? ? A SER 91   A NA  1231 1_555 ? ? ? ? ? ? ? 2.689 ? ? 
metalc3 metalc ? ? FA NA  .   NA  ? ? ? 1_555 GA HOH .   O  ? ? A NA  1231 A HOH 1309 1_555 ? ? ? ? ? ? ? 3.007 ? ? 
metalc4 metalc ? ? FA NA  .   NA  ? ? ? 1_555 GA HOH .   O  ? ? A NA  1231 A HOH 1317 1_555 ? ? ? ? ? ? ? 2.977 ? ? 
# 
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 ? FA NA . ? A NA 1231 ? 1_555 OG ? A  SER 116 ? A SER 91   ? 1_555 116.6 ? 
2 OD1 ? A  ASP 77  ? A ASP 52   ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1309 ? 1_555 94.4  ? 
3 OG  ? A  SER 116 ? A SER 91   ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1309 ? 1_555 112.3 ? 
4 OD1 ? A  ASP 77  ? A ASP 52   ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1317 ? 1_555 75.0  ? 
5 OG  ? A  SER 116 ? A SER 91   ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1317 ? 1_555 53.1  ? 
6 O   ? GA HOH .   ? A HOH 1309 ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1317 ? 1_555 85.2  ? 
# 
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                   8RWD 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   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   ? ? -120.77 -50.41 
2 1 VAL A 186  ? ? -120.26 -57.54 
3 1 VAL A 186  ? ? -120.26 -57.70 
4 1 TYR A 1101 ? ? -124.76 -60.82 
# 
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 LYS 1059 ? A LYS 292 
42 1 Y 1 A ASP 1060 ? A ASP 293 
43 1 Y 1 A HIS 306  ? A HIS 427 
44 1 Y 1 A VAL 307  ? A VAL 428 
45 1 Y 1 A LEU 308  ? A LEU 429 
46 1 Y 1 A ARG 309  ? A ARG 430 
47 1 Y 1 A GLN 310  ? A GLN 431 
48 1 Y 1 A GLN 311  ? A GLN 432 
49 1 Y 1 A GLU 312  ? A GLU 433 
50 1 Y 1 A PRO 313  ? A PRO 434 
51 1 Y 1 A PHE 314  ? A PHE 435 
52 1 Y 1 A LYS 315  ? A LYS 436 
53 1 Y 1 A ALA 316  ? A ALA 437 
54 1 Y 1 A ALA 317  ? A ALA 438 
55 1 Y 1 A ALA 318  ? A ALA 439 
56 1 Y 1 A HIS 319  ? A HIS 440 
57 1 Y 1 A HIS 320  ? A HIS 441 
58 1 Y 1 A HIS 321  ? A HIS 442 
59 1 Y 1 A HIS 322  ? A HIS 443 
60 1 Y 1 A HIS 323  ? A HIS 444 
61 1 Y 1 A HIS 324  ? A HIS 445 
62 1 Y 1 A HIS 325  ? A HIS 446 
63 1 Y 1 A HIS 326  ? A HIS 447 
64 1 Y 1 A HIS 327  ? A HIS 448 
65 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 
A1H3H N1   N  N N 1   
A1H3H N3   N  Y N 2   
A1H3H C4   C  N N 3   
A1H3H C5   C  Y N 4   
A1H3H C6   C  Y N 5   
A1H3H C8   C  Y N 6   
A1H3H C13  C  Y N 7   
A1H3H C15  C  N N 8   
A1H3H C9   C  N N 9   
A1H3H C17  C  Y N 10  
A1H3H C1   C  N N 11  
A1H3H C2   C  N N 12  
A1H3H C3   C  N N 13  
A1H3H C14  C  Y N 14  
A1H3H C16  C  Y N 15  
A1H3H C19  C  N N 16  
A1H3H O1   O  N N 17  
A1H3H N    N  N N 18  
A1H3H C    C  N N 19  
A1H3H O    O  N N 20  
A1H3H C10  C  N N 21  
A1H3H C11  C  Y N 22  
A1H3H C12  C  Y N 23  
A1H3H C7   C  N N 24  
A1H3H N2   N  Y N 25  
A1H3H O2   O  N N 26  
A1H3H O3   O  N N 27  
A1H3H H1   H  N N 28  
A1H3H H2   H  N N 29  
A1H3H H3   H  N N 30  
A1H3H H4   H  N N 31  
A1H3H H5   H  N N 32  
A1H3H H6   H  N N 33  
A1H3H H7   H  N N 34  
A1H3H H8   H  N N 35  
A1H3H H9   H  N N 36  
A1H3H H10  H  N N 37  
A1H3H H11  H  N N 38  
A1H3H H12  H  N N 39  
A1H3H H13  H  N N 40  
A1H3H H14  H  N N 41  
A1H3H H15  H  N N 42  
A1H3H H16  H  N N 43  
A1H3H H17  H  N N 44  
A1H3H H18  H  N N 45  
A1H3H H19  H  N N 46  
A1H3H H20  H  N N 47  
A1H3H H21  H  N N 48  
A1H3H H22  H  N N 49  
ALA   N    N  N N 50  
ALA   CA   C  N S 51  
ALA   C    C  N N 52  
ALA   O    O  N N 53  
ALA   CB   C  N N 54  
ALA   OXT  O  N N 55  
ALA   H    H  N N 56  
ALA   H2   H  N N 57  
ALA   HA   H  N N 58  
ALA   HB1  H  N N 59  
ALA   HB2  H  N N 60  
ALA   HB3  H  N N 61  
ALA   HXT  H  N N 62  
ARG   N    N  N N 63  
ARG   CA   C  N S 64  
ARG   C    C  N N 65  
ARG   O    O  N N 66  
ARG   CB   C  N N 67  
ARG   CG   C  N N 68  
ARG   CD   C  N N 69  
ARG   NE   N  N N 70  
ARG   CZ   C  N N 71  
ARG   NH1  N  N N 72  
ARG   NH2  N  N N 73  
ARG   OXT  O  N N 74  
ARG   H    H  N N 75  
ARG   H2   H  N N 76  
ARG   HA   H  N N 77  
ARG   HB2  H  N N 78  
ARG   HB3  H  N N 79  
ARG   HG2  H  N N 80  
ARG   HG3  H  N N 81  
ARG   HD2  H  N N 82  
ARG   HD3  H  N N 83  
ARG   HE   H  N N 84  
ARG   HH11 H  N N 85  
ARG   HH12 H  N N 86  
ARG   HH21 H  N N 87  
ARG   HH22 H  N N 88  
ARG   HXT  H  N N 89  
ASN   N    N  N N 90  
ASN   CA   C  N S 91  
ASN   C    C  N N 92  
ASN   O    O  N N 93  
ASN   CB   C  N N 94  
ASN   CG   C  N N 95  
ASN   OD1  O  N N 96  
ASN   ND2  N  N N 97  
ASN   OXT  O  N N 98  
ASN   H    H  N N 99  
ASN   H2   H  N N 100 
ASN   HA   H  N N 101 
ASN   HB2  H  N N 102 
ASN   HB3  H  N N 103 
ASN   HD21 H  N N 104 
ASN   HD22 H  N N 105 
ASN   HXT  H  N N 106 
ASP   N    N  N N 107 
ASP   CA   C  N S 108 
ASP   C    C  N N 109 
ASP   O    O  N N 110 
ASP   CB   C  N N 111 
ASP   CG   C  N N 112 
ASP   OD1  O  N N 113 
ASP   OD2  O  N N 114 
ASP   OXT  O  N N 115 
ASP   H    H  N N 116 
ASP   H2   H  N N 117 
ASP   HA   H  N N 118 
ASP   HB2  H  N N 119 
ASP   HB3  H  N N 120 
ASP   HD2  H  N N 121 
ASP   HXT  H  N N 122 
CLR   C1   C  N N 123 
CLR   C2   C  N N 124 
CLR   C3   C  N S 125 
CLR   C4   C  N N 126 
CLR   C5   C  N N 127 
CLR   C6   C  N N 128 
CLR   C7   C  N N 129 
CLR   C8   C  N S 130 
CLR   C9   C  N S 131 
CLR   C10  C  N R 132 
CLR   C11  C  N N 133 
CLR   C12  C  N N 134 
CLR   C13  C  N R 135 
CLR   C14  C  N S 136 
CLR   C15  C  N N 137 
CLR   C16  C  N N 138 
CLR   C17  C  N R 139 
CLR   C18  C  N N 140 
CLR   C19  C  N N 141 
CLR   C20  C  N R 142 
CLR   C21  C  N N 143 
CLR   C22  C  N N 144 
CLR   C23  C  N N 145 
CLR   C24  C  N N 146 
CLR   C25  C  N N 147 
CLR   C26  C  N N 148 
CLR   C27  C  N N 149 
CLR   O1   O  N N 150 
CLR   H11  H  N N 151 
CLR   H12  H  N N 152 
CLR   H21  H  N N 153 
CLR   H22  H  N N 154 
CLR   H3   H  N N 155 
CLR   H41  H  N N 156 
CLR   H42  H  N N 157 
CLR   H6   H  N N 158 
CLR   H71  H  N N 159 
CLR   H72  H  N N 160 
CLR   H8   H  N N 161 
CLR   H9   H  N N 162 
CLR   H111 H  N N 163 
CLR   H112 H  N N 164 
CLR   H121 H  N N 165 
CLR   H122 H  N N 166 
CLR   H14  H  N N 167 
CLR   H151 H  N N 168 
CLR   H152 H  N N 169 
CLR   H161 H  N N 170 
CLR   H162 H  N N 171 
CLR   H17  H  N N 172 
CLR   H181 H  N N 173 
CLR   H182 H  N N 174 
CLR   H183 H  N N 175 
CLR   H191 H  N N 176 
CLR   H192 H  N N 177 
CLR   H193 H  N N 178 
CLR   H20  H  N N 179 
CLR   H211 H  N N 180 
CLR   H212 H  N N 181 
CLR   H213 H  N N 182 
CLR   H221 H  N N 183 
CLR   H222 H  N N 184 
CLR   H231 H  N N 185 
CLR   H232 H  N N 186 
CLR   H241 H  N N 187 
CLR   H242 H  N N 188 
CLR   H25  H  N N 189 
CLR   H261 H  N N 190 
CLR   H262 H  N N 191 
CLR   H263 H  N N 192 
CLR   H271 H  N N 193 
CLR   H272 H  N N 194 
CLR   H273 H  N N 195 
CLR   H1   H  N N 196 
CYS   N    N  N N 197 
CYS   CA   C  N R 198 
CYS   C    C  N N 199 
CYS   O    O  N N 200 
CYS   CB   C  N N 201 
CYS   SG   S  N N 202 
CYS   OXT  O  N N 203 
CYS   H    H  N N 204 
CYS   H2   H  N N 205 
CYS   HA   H  N N 206 
CYS   HB2  H  N N 207 
CYS   HB3  H  N N 208 
CYS   HG   H  N N 209 
CYS   HXT  H  N N 210 
GLN   N    N  N N 211 
GLN   CA   C  N S 212 
GLN   C    C  N N 213 
GLN   O    O  N N 214 
GLN   CB   C  N N 215 
GLN   CG   C  N N 216 
GLN   CD   C  N N 217 
GLN   OE1  O  N N 218 
GLN   NE2  N  N N 219 
GLN   OXT  O  N N 220 
GLN   H    H  N N 221 
GLN   H2   H  N N 222 
GLN   HA   H  N N 223 
GLN   HB2  H  N N 224 
GLN   HB3  H  N N 225 
GLN   HG2  H  N N 226 
GLN   HG3  H  N N 227 
GLN   HE21 H  N N 228 
GLN   HE22 H  N N 229 
GLN   HXT  H  N N 230 
GLU   N    N  N N 231 
GLU   CA   C  N S 232 
GLU   C    C  N N 233 
GLU   O    O  N N 234 
GLU   CB   C  N N 235 
GLU   CG   C  N N 236 
GLU   CD   C  N N 237 
GLU   OE1  O  N N 238 
GLU   OE2  O  N N 239 
GLU   OXT  O  N N 240 
GLU   H    H  N N 241 
GLU   H2   H  N N 242 
GLU   HA   H  N N 243 
GLU   HB2  H  N N 244 
GLU   HB3  H  N N 245 
GLU   HG2  H  N N 246 
GLU   HG3  H  N N 247 
GLU   HE2  H  N N 248 
GLU   HXT  H  N N 249 
GLY   N    N  N N 250 
GLY   CA   C  N N 251 
GLY   C    C  N N 252 
GLY   O    O  N N 253 
GLY   OXT  O  N N 254 
GLY   H    H  N N 255 
GLY   H2   H  N N 256 
GLY   HA2  H  N N 257 
GLY   HA3  H  N N 258 
GLY   HXT  H  N N 259 
HIS   N    N  N N 260 
HIS   CA   C  N S 261 
HIS   C    C  N N 262 
HIS   O    O  N N 263 
HIS   CB   C  N N 264 
HIS   CG   C  Y N 265 
HIS   ND1  N  Y N 266 
HIS   CD2  C  Y N 267 
HIS   CE1  C  Y N 268 
HIS   NE2  N  Y N 269 
HIS   OXT  O  N N 270 
HIS   H    H  N N 271 
HIS   H2   H  N N 272 
HIS   HA   H  N N 273 
HIS   HB2  H  N N 274 
HIS   HB3  H  N N 275 
HIS   HD1  H  N N 276 
HIS   HD2  H  N N 277 
HIS   HE1  H  N N 278 
HIS   HE2  H  N N 279 
HIS   HXT  H  N N 280 
HOH   O    O  N N 281 
HOH   H1   H  N N 282 
HOH   H2   H  N N 283 
ILE   N    N  N N 284 
ILE   CA   C  N S 285 
ILE   C    C  N N 286 
ILE   O    O  N N 287 
ILE   CB   C  N S 288 
ILE   CG1  C  N N 289 
ILE   CG2  C  N N 290 
ILE   CD1  C  N N 291 
ILE   OXT  O  N N 292 
ILE   H    H  N N 293 
ILE   H2   H  N N 294 
ILE   HA   H  N N 295 
ILE   HB   H  N N 296 
ILE   HG12 H  N N 297 
ILE   HG13 H  N N 298 
ILE   HG21 H  N N 299 
ILE   HG22 H  N N 300 
ILE   HG23 H  N N 301 
ILE   HD11 H  N N 302 
ILE   HD12 H  N N 303 
ILE   HD13 H  N N 304 
ILE   HXT  H  N N 305 
LEU   N    N  N N 306 
LEU   CA   C  N S 307 
LEU   C    C  N N 308 
LEU   O    O  N N 309 
LEU   CB   C  N N 310 
LEU   CG   C  N N 311 
LEU   CD1  C  N N 312 
LEU   CD2  C  N N 313 
LEU   OXT  O  N N 314 
LEU   H    H  N N 315 
LEU   H2   H  N N 316 
LEU   HA   H  N N 317 
LEU   HB2  H  N N 318 
LEU   HB3  H  N N 319 
LEU   HG   H  N N 320 
LEU   HD11 H  N N 321 
LEU   HD12 H  N N 322 
LEU   HD13 H  N N 323 
LEU   HD21 H  N N 324 
LEU   HD22 H  N N 325 
LEU   HD23 H  N N 326 
LEU   HXT  H  N N 327 
LYS   N    N  N N 328 
LYS   CA   C  N S 329 
LYS   C    C  N N 330 
LYS   O    O  N N 331 
LYS   CB   C  N N 332 
LYS   CG   C  N N 333 
LYS   CD   C  N N 334 
LYS   CE   C  N N 335 
LYS   NZ   N  N N 336 
LYS   OXT  O  N N 337 
LYS   H    H  N N 338 
LYS   H2   H  N N 339 
LYS   HA   H  N N 340 
LYS   HB2  H  N N 341 
LYS   HB3  H  N N 342 
LYS   HG2  H  N N 343 
LYS   HG3  H  N N 344 
LYS   HD2  H  N N 345 
LYS   HD3  H  N N 346 
LYS   HE2  H  N N 347 
LYS   HE3  H  N N 348 
LYS   HZ1  H  N N 349 
LYS   HZ2  H  N N 350 
LYS   HZ3  H  N N 351 
LYS   HXT  H  N N 352 
MET   N    N  N N 353 
MET   CA   C  N S 354 
MET   C    C  N N 355 
MET   O    O  N N 356 
MET   CB   C  N N 357 
MET   CG   C  N N 358 
MET   SD   S  N N 359 
MET   CE   C  N N 360 
MET   OXT  O  N N 361 
MET   H    H  N N 362 
MET   H2   H  N N 363 
MET   HA   H  N N 364 
MET   HB2  H  N N 365 
MET   HB3  H  N N 366 
MET   HG2  H  N N 367 
MET   HG3  H  N N 368 
MET   HE1  H  N N 369 
MET   HE2  H  N N 370 
MET   HE3  H  N N 371 
MET   HXT  H  N N 372 
NA    NA   NA N N 373 
OLA   C1   C  N N 374 
OLA   O1   O  N N 375 
OLA   O2   O  N N 376 
OLA   C2   C  N N 377 
OLA   C3   C  N N 378 
OLA   C4   C  N N 379 
OLA   C5   C  N N 380 
OLA   C6   C  N N 381 
OLA   C7   C  N N 382 
OLA   C8   C  N N 383 
OLA   C9   C  N N 384 
OLA   C10  C  N N 385 
OLA   C11  C  N N 386 
OLA   C12  C  N N 387 
OLA   C13  C  N N 388 
OLA   C14  C  N N 389 
OLA   C15  C  N N 390 
OLA   C16  C  N N 391 
OLA   C17  C  N N 392 
OLA   C18  C  N N 393 
OLA   HO2  H  N N 394 
OLA   H21  H  N N 395 
OLA   H22  H  N N 396 
OLA   H31  H  N N 397 
OLA   H32  H  N N 398 
OLA   H41  H  N N 399 
OLA   H42  H  N N 400 
OLA   H51  H  N N 401 
OLA   H52  H  N N 402 
OLA   H61  H  N N 403 
OLA   H62  H  N N 404 
OLA   H71  H  N N 405 
OLA   H72  H  N N 406 
OLA   H81  H  N N 407 
OLA   H82  H  N N 408 
OLA   H9   H  N N 409 
OLA   H10  H  N N 410 
OLA   H111 H  N N 411 
OLA   H112 H  N N 412 
OLA   H121 H  N N 413 
OLA   H122 H  N N 414 
OLA   H131 H  N N 415 
OLA   H132 H  N N 416 
OLA   H141 H  N N 417 
OLA   H142 H  N N 418 
OLA   H151 H  N N 419 
OLA   H152 H  N N 420 
OLA   H161 H  N N 421 
OLA   H162 H  N N 422 
OLA   H171 H  N N 423 
OLA   H172 H  N N 424 
OLA   H181 H  N N 425 
OLA   H182 H  N N 426 
OLA   H183 H  N N 427 
PHE   N    N  N N 428 
PHE   CA   C  N S 429 
PHE   C    C  N N 430 
PHE   O    O  N N 431 
PHE   CB   C  N N 432 
PHE   CG   C  Y N 433 
PHE   CD1  C  Y N 434 
PHE   CD2  C  Y N 435 
PHE   CE1  C  Y N 436 
PHE   CE2  C  Y N 437 
PHE   CZ   C  Y N 438 
PHE   OXT  O  N N 439 
PHE   H    H  N N 440 
PHE   H2   H  N N 441 
PHE   HA   H  N N 442 
PHE   HB2  H  N N 443 
PHE   HB3  H  N N 444 
PHE   HD1  H  N N 445 
PHE   HD2  H  N N 446 
PHE   HE1  H  N N 447 
PHE   HE2  H  N N 448 
PHE   HZ   H  N N 449 
PHE   HXT  H  N N 450 
PRO   N    N  N N 451 
PRO   CA   C  N S 452 
PRO   C    C  N N 453 
PRO   O    O  N N 454 
PRO   CB   C  N N 455 
PRO   CG   C  N N 456 
PRO   CD   C  N N 457 
PRO   OXT  O  N N 458 
PRO   H    H  N N 459 
PRO   HA   H  N N 460 
PRO   HB2  H  N N 461 
PRO   HB3  H  N N 462 
PRO   HG2  H  N N 463 
PRO   HG3  H  N N 464 
PRO   HD2  H  N N 465 
PRO   HD3  H  N N 466 
PRO   HXT  H  N N 467 
SER   N    N  N N 468 
SER   CA   C  N S 469 
SER   C    C  N N 470 
SER   O    O  N N 471 
SER   CB   C  N N 472 
SER   OG   O  N N 473 
SER   OXT  O  N N 474 
SER   H    H  N N 475 
SER   H2   H  N N 476 
SER   HA   H  N N 477 
SER   HB2  H  N N 478 
SER   HB3  H  N N 479 
SER   HG   H  N N 480 
SER   HXT  H  N N 481 
THR   N    N  N N 482 
THR   CA   C  N S 483 
THR   C    C  N N 484 
THR   O    O  N N 485 
THR   CB   C  N R 486 
THR   OG1  O  N N 487 
THR   CG2  C  N N 488 
THR   OXT  O  N N 489 
THR   H    H  N N 490 
THR   H2   H  N N 491 
THR   HA   H  N N 492 
THR   HB   H  N N 493 
THR   HG1  H  N N 494 
THR   HG21 H  N N 495 
THR   HG22 H  N N 496 
THR   HG23 H  N N 497 
THR   HXT  H  N N 498 
TRP   N    N  N N 499 
TRP   CA   C  N S 500 
TRP   C    C  N N 501 
TRP   O    O  N N 502 
TRP   CB   C  N N 503 
TRP   CG   C  Y N 504 
TRP   CD1  C  Y N 505 
TRP   CD2  C  Y N 506 
TRP   NE1  N  Y N 507 
TRP   CE2  C  Y N 508 
TRP   CE3  C  Y N 509 
TRP   CZ2  C  Y N 510 
TRP   CZ3  C  Y N 511 
TRP   CH2  C  Y N 512 
TRP   OXT  O  N N 513 
TRP   H    H  N N 514 
TRP   H2   H  N N 515 
TRP   HA   H  N N 516 
TRP   HB2  H  N N 517 
TRP   HB3  H  N N 518 
TRP   HD1  H  N N 519 
TRP   HE1  H  N N 520 
TRP   HE3  H  N N 521 
TRP   HZ2  H  N N 522 
TRP   HZ3  H  N N 523 
TRP   HH2  H  N N 524 
TRP   HXT  H  N N 525 
TYR   N    N  N N 526 
TYR   CA   C  N S 527 
TYR   C    C  N N 528 
TYR   O    O  N N 529 
TYR   CB   C  N N 530 
TYR   CG   C  Y N 531 
TYR   CD1  C  Y N 532 
TYR   CD2  C  Y N 533 
TYR   CE1  C  Y N 534 
TYR   CE2  C  Y N 535 
TYR   CZ   C  Y N 536 
TYR   OH   O  N N 537 
TYR   OXT  O  N N 538 
TYR   H    H  N N 539 
TYR   H2   H  N N 540 
TYR   HA   H  N N 541 
TYR   HB2  H  N N 542 
TYR   HB3  H  N N 543 
TYR   HD1  H  N N 544 
TYR   HD2  H  N N 545 
TYR   HE1  H  N N 546 
TYR   HE2  H  N N 547 
TYR   HH   H  N N 548 
TYR   HXT  H  N N 549 
VAL   N    N  N N 550 
VAL   CA   C  N S 551 
VAL   C    C  N N 552 
VAL   O    O  N N 553 
VAL   CB   C  N N 554 
VAL   CG1  C  N N 555 
VAL   CG2  C  N N 556 
VAL   OXT  O  N N 557 
VAL   H    H  N N 558 
VAL   H2   H  N N 559 
VAL   HA   H  N N 560 
VAL   HB   H  N N 561 
VAL   HG11 H  N N 562 
VAL   HG12 H  N N 563 
VAL   HG13 H  N N 564 
VAL   HG21 H  N N 565 
VAL   HG22 H  N N 566 
VAL   HG23 H  N N 567 
VAL   HXT  H  N N 568 
# 
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 
A1H3H O2  C13  sing N N 1   
A1H3H C13 C12  doub Y N 2   
A1H3H C13 C14  sing Y N 3   
A1H3H O1  C14  sing N N 4   
A1H3H O1  C15  sing N N 5   
A1H3H C12 C11  sing Y N 6   
A1H3H C14 C16  doub Y N 7   
A1H3H C11 C17  doub Y N 8   
A1H3H C11 C10  sing N N 9   
A1H3H C16 C17  sing Y N 10  
A1H3H C10 C9   doub N E 11  
A1H3H C3  C4   sing N N 12  
A1H3H C3  N1   sing N N 13  
A1H3H C9  C8   sing N N 14  
A1H3H N3  C8   doub Y N 15  
A1H3H N3  C5   sing Y N 16  
A1H3H C8  N2   sing Y N 17  
A1H3H N1  C5   sing N N 18  
A1H3H N1  C2   sing N N 19  
A1H3H C5  C6   doub Y N 20  
A1H3H O   C2   doub N N 21  
A1H3H N2  C6   sing Y N 22  
A1H3H N2  C7   sing N N 23  
A1H3H C2  N    sing N N 24  
A1H3H C6  C19  sing N N 25  
A1H3H N   C19  sing N N 26  
A1H3H N   C1   sing N N 27  
A1H3H C   C1   sing N N 28  
A1H3H C19 O3   doub N N 29  
A1H3H C4  H1   sing N N 30  
A1H3H C4  H2   sing N N 31  
A1H3H C4  H3   sing N N 32  
A1H3H C15 H4   sing N N 33  
A1H3H C15 H5   sing N N 34  
A1H3H C15 H6   sing N N 35  
A1H3H C9  H7   sing N N 36  
A1H3H C17 H8   sing N N 37  
A1H3H C1  H9   sing N N 38  
A1H3H C1  H10  sing N N 39  
A1H3H C3  H11  sing N N 40  
A1H3H C3  H12  sing N N 41  
A1H3H C16 H13  sing N N 42  
A1H3H C   H14  sing N N 43  
A1H3H C   H15  sing N N 44  
A1H3H C   H16  sing N N 45  
A1H3H C10 H17  sing N N 46  
A1H3H C12 H18  sing N N 47  
A1H3H C7  H19  sing N N 48  
A1H3H C7  H20  sing N N 49  
A1H3H C7  H21  sing N N 50  
A1H3H O2  H22  sing N N 51  
ALA   N   CA   sing N N 52  
ALA   N   H    sing N N 53  
ALA   N   H2   sing N N 54  
ALA   CA  C    sing N N 55  
ALA   CA  CB   sing N N 56  
ALA   CA  HA   sing N N 57  
ALA   C   O    doub N N 58  
ALA   C   OXT  sing N N 59  
ALA   CB  HB1  sing N N 60  
ALA   CB  HB2  sing N N 61  
ALA   CB  HB3  sing N N 62  
ALA   OXT HXT  sing N N 63  
ARG   N   CA   sing N N 64  
ARG   N   H    sing N N 65  
ARG   N   H2   sing N N 66  
ARG   CA  C    sing N N 67  
ARG   CA  CB   sing N N 68  
ARG   CA  HA   sing N N 69  
ARG   C   O    doub N N 70  
ARG   C   OXT  sing N N 71  
ARG   CB  CG   sing N N 72  
ARG   CB  HB2  sing N N 73  
ARG   CB  HB3  sing N N 74  
ARG   CG  CD   sing N N 75  
ARG   CG  HG2  sing N N 76  
ARG   CG  HG3  sing N N 77  
ARG   CD  NE   sing N N 78  
ARG   CD  HD2  sing N N 79  
ARG   CD  HD3  sing N N 80  
ARG   NE  CZ   sing N N 81  
ARG   NE  HE   sing N N 82  
ARG   CZ  NH1  sing N N 83  
ARG   CZ  NH2  doub N N 84  
ARG   NH1 HH11 sing N N 85  
ARG   NH1 HH12 sing N N 86  
ARG   NH2 HH21 sing N N 87  
ARG   NH2 HH22 sing N N 88  
ARG   OXT HXT  sing N N 89  
ASN   N   CA   sing N N 90  
ASN   N   H    sing N N 91  
ASN   N   H2   sing N N 92  
ASN   CA  C    sing N N 93  
ASN   CA  CB   sing N N 94  
ASN   CA  HA   sing N N 95  
ASN   C   O    doub N N 96  
ASN   C   OXT  sing N N 97  
ASN   CB  CG   sing N N 98  
ASN   CB  HB2  sing N N 99  
ASN   CB  HB3  sing N N 100 
ASN   CG  OD1  doub N N 101 
ASN   CG  ND2  sing N N 102 
ASN   ND2 HD21 sing N N 103 
ASN   ND2 HD22 sing N N 104 
ASN   OXT HXT  sing N N 105 
ASP   N   CA   sing N N 106 
ASP   N   H    sing N N 107 
ASP   N   H2   sing N N 108 
ASP   CA  C    sing N N 109 
ASP   CA  CB   sing N N 110 
ASP   CA  HA   sing N N 111 
ASP   C   O    doub N N 112 
ASP   C   OXT  sing N N 113 
ASP   CB  CG   sing N N 114 
ASP   CB  HB2  sing N N 115 
ASP   CB  HB3  sing N N 116 
ASP   CG  OD1  doub N N 117 
ASP   CG  OD2  sing N N 118 
ASP   OD2 HD2  sing N N 119 
ASP   OXT HXT  sing N N 120 
CLR   C1  C2   sing N N 121 
CLR   C1  C10  sing N N 122 
CLR   C1  H11  sing N N 123 
CLR   C1  H12  sing N N 124 
CLR   C2  C3   sing N N 125 
CLR   C2  H21  sing N N 126 
CLR   C2  H22  sing N N 127 
CLR   C3  C4   sing N N 128 
CLR   C3  O1   sing N N 129 
CLR   C3  H3   sing N N 130 
CLR   C4  C5   sing N N 131 
CLR   C4  H41  sing N N 132 
CLR   C4  H42  sing N N 133 
CLR   C5  C6   doub N N 134 
CLR   C5  C10  sing N N 135 
CLR   C6  C7   sing N N 136 
CLR   C6  H6   sing N N 137 
CLR   C7  C8   sing N N 138 
CLR   C7  H71  sing N N 139 
CLR   C7  H72  sing N N 140 
CLR   C8  C9   sing N N 141 
CLR   C8  C14  sing N N 142 
CLR   C8  H8   sing N N 143 
CLR   C9  C10  sing N N 144 
CLR   C9  C11  sing N N 145 
CLR   C9  H9   sing N N 146 
CLR   C10 C19  sing N N 147 
CLR   C11 C12  sing N N 148 
CLR   C11 H111 sing N N 149 
CLR   C11 H112 sing N N 150 
CLR   C12 C13  sing N N 151 
CLR   C12 H121 sing N N 152 
CLR   C12 H122 sing N N 153 
CLR   C13 C14  sing N N 154 
CLR   C13 C17  sing N N 155 
CLR   C13 C18  sing N N 156 
CLR   C14 C15  sing N N 157 
CLR   C14 H14  sing N N 158 
CLR   C15 C16  sing N N 159 
CLR   C15 H151 sing N N 160 
CLR   C15 H152 sing N N 161 
CLR   C16 C17  sing N N 162 
CLR   C16 H161 sing N N 163 
CLR   C16 H162 sing N N 164 
CLR   C17 C20  sing N N 165 
CLR   C17 H17  sing N N 166 
CLR   C18 H181 sing N N 167 
CLR   C18 H182 sing N N 168 
CLR   C18 H183 sing N N 169 
CLR   C19 H191 sing N N 170 
CLR   C19 H192 sing N N 171 
CLR   C19 H193 sing N N 172 
CLR   C20 C21  sing N N 173 
CLR   C20 C22  sing N N 174 
CLR   C20 H20  sing N N 175 
CLR   C21 H211 sing N N 176 
CLR   C21 H212 sing N N 177 
CLR   C21 H213 sing N N 178 
CLR   C22 C23  sing N N 179 
CLR   C22 H221 sing N N 180 
CLR   C22 H222 sing N N 181 
CLR   C23 C24  sing N N 182 
CLR   C23 H231 sing N N 183 
CLR   C23 H232 sing N N 184 
CLR   C24 C25  sing N N 185 
CLR   C24 H241 sing N N 186 
CLR   C24 H242 sing N N 187 
CLR   C25 C26  sing N N 188 
CLR   C25 C27  sing N N 189 
CLR   C25 H25  sing N N 190 
CLR   C26 H261 sing N N 191 
CLR   C26 H262 sing N N 192 
CLR   C26 H263 sing N N 193 
CLR   C27 H271 sing N N 194 
CLR   C27 H272 sing N N 195 
CLR   C27 H273 sing N N 196 
CLR   O1  H1   sing N N 197 
CYS   N   CA   sing N N 198 
CYS   N   H    sing N N 199 
CYS   N   H2   sing N N 200 
CYS   CA  C    sing N N 201 
CYS   CA  CB   sing N N 202 
CYS   CA  HA   sing N N 203 
CYS   C   O    doub N N 204 
CYS   C   OXT  sing N N 205 
CYS   CB  SG   sing N N 206 
CYS   CB  HB2  sing N N 207 
CYS   CB  HB3  sing N N 208 
CYS   SG  HG   sing N N 209 
CYS   OXT HXT  sing N N 210 
GLN   N   CA   sing N N 211 
GLN   N   H    sing N N 212 
GLN   N   H2   sing N N 213 
GLN   CA  C    sing N N 214 
GLN   CA  CB   sing N N 215 
GLN   CA  HA   sing N N 216 
GLN   C   O    doub N N 217 
GLN   C   OXT  sing N N 218 
GLN   CB  CG   sing N N 219 
GLN   CB  HB2  sing N N 220 
GLN   CB  HB3  sing N N 221 
GLN   CG  CD   sing N N 222 
GLN   CG  HG2  sing N N 223 
GLN   CG  HG3  sing N N 224 
GLN   CD  OE1  doub N N 225 
GLN   CD  NE2  sing N N 226 
GLN   NE2 HE21 sing N N 227 
GLN   NE2 HE22 sing N N 228 
GLN   OXT HXT  sing N N 229 
GLU   N   CA   sing N N 230 
GLU   N   H    sing N N 231 
GLU   N   H2   sing N N 232 
GLU   CA  C    sing N N 233 
GLU   CA  CB   sing N N 234 
GLU   CA  HA   sing N N 235 
GLU   C   O    doub N N 236 
GLU   C   OXT  sing N N 237 
GLU   CB  CG   sing N N 238 
GLU   CB  HB2  sing N N 239 
GLU   CB  HB3  sing N N 240 
GLU   CG  CD   sing N N 241 
GLU   CG  HG2  sing N N 242 
GLU   CG  HG3  sing N N 243 
GLU   CD  OE1  doub N N 244 
GLU   CD  OE2  sing N N 245 
GLU   OE2 HE2  sing N N 246 
GLU   OXT HXT  sing N N 247 
GLY   N   CA   sing N N 248 
GLY   N   H    sing N N 249 
GLY   N   H2   sing N N 250 
GLY   CA  C    sing N N 251 
GLY   CA  HA2  sing N N 252 
GLY   CA  HA3  sing N N 253 
GLY   C   O    doub N N 254 
GLY   C   OXT  sing N N 255 
GLY   OXT HXT  sing N N 256 
HIS   N   CA   sing N N 257 
HIS   N   H    sing N N 258 
HIS   N   H2   sing N N 259 
HIS   CA  C    sing N N 260 
HIS   CA  CB   sing N N 261 
HIS   CA  HA   sing N N 262 
HIS   C   O    doub N N 263 
HIS   C   OXT  sing N N 264 
HIS   CB  CG   sing N N 265 
HIS   CB  HB2  sing N N 266 
HIS   CB  HB3  sing N N 267 
HIS   CG  ND1  sing Y N 268 
HIS   CG  CD2  doub Y N 269 
HIS   ND1 CE1  doub Y N 270 
HIS   ND1 HD1  sing N N 271 
HIS   CD2 NE2  sing Y N 272 
HIS   CD2 HD2  sing N N 273 
HIS   CE1 NE2  sing Y N 274 
HIS   CE1 HE1  sing N N 275 
HIS   NE2 HE2  sing N N 276 
HIS   OXT HXT  sing N N 277 
HOH   O   H1   sing N N 278 
HOH   O   H2   sing N N 279 
ILE   N   CA   sing N N 280 
ILE   N   H    sing N N 281 
ILE   N   H2   sing N N 282 
ILE   CA  C    sing N N 283 
ILE   CA  CB   sing N N 284 
ILE   CA  HA   sing N N 285 
ILE   C   O    doub N N 286 
ILE   C   OXT  sing N N 287 
ILE   CB  CG1  sing N N 288 
ILE   CB  CG2  sing N N 289 
ILE   CB  HB   sing N N 290 
ILE   CG1 CD1  sing N N 291 
ILE   CG1 HG12 sing N N 292 
ILE   CG1 HG13 sing N N 293 
ILE   CG2 HG21 sing N N 294 
ILE   CG2 HG22 sing N N 295 
ILE   CG2 HG23 sing N N 296 
ILE   CD1 HD11 sing N N 297 
ILE   CD1 HD12 sing N N 298 
ILE   CD1 HD13 sing N N 299 
ILE   OXT HXT  sing N N 300 
LEU   N   CA   sing N N 301 
LEU   N   H    sing N N 302 
LEU   N   H2   sing N N 303 
LEU   CA  C    sing N N 304 
LEU   CA  CB   sing N N 305 
LEU   CA  HA   sing N N 306 
LEU   C   O    doub N N 307 
LEU   C   OXT  sing N N 308 
LEU   CB  CG   sing N N 309 
LEU   CB  HB2  sing N N 310 
LEU   CB  HB3  sing N N 311 
LEU   CG  CD1  sing N N 312 
LEU   CG  CD2  sing N N 313 
LEU   CG  HG   sing N N 314 
LEU   CD1 HD11 sing N N 315 
LEU   CD1 HD12 sing N N 316 
LEU   CD1 HD13 sing N N 317 
LEU   CD2 HD21 sing N N 318 
LEU   CD2 HD22 sing N N 319 
LEU   CD2 HD23 sing N N 320 
LEU   OXT HXT  sing N N 321 
LYS   N   CA   sing N N 322 
LYS   N   H    sing N N 323 
LYS   N   H2   sing N N 324 
LYS   CA  C    sing N N 325 
LYS   CA  CB   sing N N 326 
LYS   CA  HA   sing N N 327 
LYS   C   O    doub N N 328 
LYS   C   OXT  sing N N 329 
LYS   CB  CG   sing N N 330 
LYS   CB  HB2  sing N N 331 
LYS   CB  HB3  sing N N 332 
LYS   CG  CD   sing N N 333 
LYS   CG  HG2  sing N N 334 
LYS   CG  HG3  sing N N 335 
LYS   CD  CE   sing N N 336 
LYS   CD  HD2  sing N N 337 
LYS   CD  HD3  sing N N 338 
LYS   CE  NZ   sing N N 339 
LYS   CE  HE2  sing N N 340 
LYS   CE  HE3  sing N N 341 
LYS   NZ  HZ1  sing N N 342 
LYS   NZ  HZ2  sing N N 343 
LYS   NZ  HZ3  sing N N 344 
LYS   OXT HXT  sing N N 345 
MET   N   CA   sing N N 346 
MET   N   H    sing N N 347 
MET   N   H2   sing N N 348 
MET   CA  C    sing N N 349 
MET   CA  CB   sing N N 350 
MET   CA  HA   sing N N 351 
MET   C   O    doub N N 352 
MET   C   OXT  sing N N 353 
MET   CB  CG   sing N N 354 
MET   CB  HB2  sing N N 355 
MET   CB  HB3  sing N N 356 
MET   CG  SD   sing N N 357 
MET   CG  HG2  sing N N 358 
MET   CG  HG3  sing N N 359 
MET   SD  CE   sing N N 360 
MET   CE  HE1  sing N N 361 
MET   CE  HE2  sing N N 362 
MET   CE  HE3  sing N N 363 
MET   OXT HXT  sing N N 364 
OLA   C1  O1   doub N N 365 
OLA   C1  O2   sing N N 366 
OLA   C1  C2   sing N N 367 
OLA   O2  HO2  sing N N 368 
OLA   C2  C3   sing N N 369 
OLA   C2  H21  sing N N 370 
OLA   C2  H22  sing N N 371 
OLA   C3  C4   sing N N 372 
OLA   C3  H31  sing N N 373 
OLA   C3  H32  sing N N 374 
OLA   C4  C5   sing N N 375 
OLA   C4  H41  sing N N 376 
OLA   C4  H42  sing N N 377 
OLA   C5  C6   sing N N 378 
OLA   C5  H51  sing N N 379 
OLA   C5  H52  sing N N 380 
OLA   C6  C7   sing N N 381 
OLA   C6  H61  sing N N 382 
OLA   C6  H62  sing N N 383 
OLA   C7  C8   sing N N 384 
OLA   C7  H71  sing N N 385 
OLA   C7  H72  sing N N 386 
OLA   C8  C9   sing N N 387 
OLA   C8  H81  sing N N 388 
OLA   C8  H82  sing N N 389 
OLA   C9  C10  doub N Z 390 
OLA   C9  H9   sing N N 391 
OLA   C10 C11  sing N N 392 
OLA   C10 H10  sing N N 393 
OLA   C11 C12  sing N N 394 
OLA   C11 H111 sing N N 395 
OLA   C11 H112 sing N N 396 
OLA   C12 C13  sing N N 397 
OLA   C12 H121 sing N N 398 
OLA   C12 H122 sing N N 399 
OLA   C13 C14  sing N N 400 
OLA   C13 H131 sing N N 401 
OLA   C13 H132 sing N N 402 
OLA   C14 C15  sing N N 403 
OLA   C14 H141 sing N N 404 
OLA   C14 H142 sing N N 405 
OLA   C15 C16  sing N N 406 
OLA   C15 H151 sing N N 407 
OLA   C15 H152 sing N N 408 
OLA   C16 C17  sing N N 409 
OLA   C16 H161 sing N N 410 
OLA   C16 H162 sing N N 411 
OLA   C17 C18  sing N N 412 
OLA   C17 H171 sing N N 413 
OLA   C17 H172 sing N N 414 
OLA   C18 H181 sing N N 415 
OLA   C18 H182 sing N N 416 
OLA   C18 H183 sing N N 417 
PHE   N   CA   sing N N 418 
PHE   N   H    sing N N 419 
PHE   N   H2   sing N N 420 
PHE   CA  C    sing N N 421 
PHE   CA  CB   sing N N 422 
PHE   CA  HA   sing N N 423 
PHE   C   O    doub N N 424 
PHE   C   OXT  sing N N 425 
PHE   CB  CG   sing N N 426 
PHE   CB  HB2  sing N N 427 
PHE   CB  HB3  sing N N 428 
PHE   CG  CD1  doub Y N 429 
PHE   CG  CD2  sing Y N 430 
PHE   CD1 CE1  sing Y N 431 
PHE   CD1 HD1  sing N N 432 
PHE   CD2 CE2  doub Y N 433 
PHE   CD2 HD2  sing N N 434 
PHE   CE1 CZ   doub Y N 435 
PHE   CE1 HE1  sing N N 436 
PHE   CE2 CZ   sing Y N 437 
PHE   CE2 HE2  sing N N 438 
PHE   CZ  HZ   sing N N 439 
PHE   OXT HXT  sing N N 440 
PRO   N   CA   sing N N 441 
PRO   N   CD   sing N N 442 
PRO   N   H    sing N N 443 
PRO   CA  C    sing N N 444 
PRO   CA  CB   sing N N 445 
PRO   CA  HA   sing N N 446 
PRO   C   O    doub N N 447 
PRO   C   OXT  sing N N 448 
PRO   CB  CG   sing N N 449 
PRO   CB  HB2  sing N N 450 
PRO   CB  HB3  sing N N 451 
PRO   CG  CD   sing N N 452 
PRO   CG  HG2  sing N N 453 
PRO   CG  HG3  sing N N 454 
PRO   CD  HD2  sing N N 455 
PRO   CD  HD3  sing N N 456 
PRO   OXT HXT  sing N N 457 
SER   N   CA   sing N N 458 
SER   N   H    sing N N 459 
SER   N   H2   sing N N 460 
SER   CA  C    sing N N 461 
SER   CA  CB   sing N N 462 
SER   CA  HA   sing N N 463 
SER   C   O    doub N N 464 
SER   C   OXT  sing N N 465 
SER   CB  OG   sing N N 466 
SER   CB  HB2  sing N N 467 
SER   CB  HB3  sing N N 468 
SER   OG  HG   sing N N 469 
SER   OXT HXT  sing N N 470 
THR   N   CA   sing N N 471 
THR   N   H    sing N N 472 
THR   N   H2   sing N N 473 
THR   CA  C    sing N N 474 
THR   CA  CB   sing N N 475 
THR   CA  HA   sing N N 476 
THR   C   O    doub N N 477 
THR   C   OXT  sing N N 478 
THR   CB  OG1  sing N N 479 
THR   CB  CG2  sing N N 480 
THR   CB  HB   sing N N 481 
THR   OG1 HG1  sing N N 482 
THR   CG2 HG21 sing N N 483 
THR   CG2 HG22 sing N N 484 
THR   CG2 HG23 sing N N 485 
THR   OXT HXT  sing N N 486 
TRP   N   CA   sing N N 487 
TRP   N   H    sing N N 488 
TRP   N   H2   sing N N 489 
TRP   CA  C    sing N N 490 
TRP   CA  CB   sing N N 491 
TRP   CA  HA   sing N N 492 
TRP   C   O    doub N N 493 
TRP   C   OXT  sing N N 494 
TRP   CB  CG   sing N N 495 
TRP   CB  HB2  sing N N 496 
TRP   CB  HB3  sing N N 497 
TRP   CG  CD1  doub Y N 498 
TRP   CG  CD2  sing Y N 499 
TRP   CD1 NE1  sing Y N 500 
TRP   CD1 HD1  sing N N 501 
TRP   CD2 CE2  doub Y N 502 
TRP   CD2 CE3  sing Y N 503 
TRP   NE1 CE2  sing Y N 504 
TRP   NE1 HE1  sing N N 505 
TRP   CE2 CZ2  sing Y N 506 
TRP   CE3 CZ3  doub Y N 507 
TRP   CE3 HE3  sing N N 508 
TRP   CZ2 CH2  doub Y N 509 
TRP   CZ2 HZ2  sing N N 510 
TRP   CZ3 CH2  sing Y N 511 
TRP   CZ3 HZ3  sing N N 512 
TRP   CH2 HH2  sing N N 513 
TRP   OXT HXT  sing N N 514 
TYR   N   CA   sing N N 515 
TYR   N   H    sing N N 516 
TYR   N   H2   sing N N 517 
TYR   CA  C    sing N N 518 
TYR   CA  CB   sing N N 519 
TYR   CA  HA   sing N N 520 
TYR   C   O    doub N N 521 
TYR   C   OXT  sing N N 522 
TYR   CB  CG   sing N N 523 
TYR   CB  HB2  sing N N 524 
TYR   CB  HB3  sing N N 525 
TYR   CG  CD1  doub Y N 526 
TYR   CG  CD2  sing Y N 527 
TYR   CD1 CE1  sing Y N 528 
TYR   CD1 HD1  sing N N 529 
TYR   CD2 CE2  doub Y N 530 
TYR   CD2 HD2  sing N N 531 
TYR   CE1 CZ   doub Y N 532 
TYR   CE1 HE1  sing N N 533 
TYR   CE2 CZ   sing Y N 534 
TYR   CE2 HE2  sing N N 535 
TYR   CZ  OH   sing N N 536 
TYR   OH  HH   sing N N 537 
TYR   OXT HXT  sing N N 538 
VAL   N   CA   sing N N 539 
VAL   N   H    sing N N 540 
VAL   N   H2   sing N N 541 
VAL   CA  C    sing N N 542 
VAL   CA  CB   sing N N 543 
VAL   CA  HA   sing N N 544 
VAL   C   O    doub N N 545 
VAL   C   OXT  sing N N 546 
VAL   CB  CG1  sing N N 547 
VAL   CB  CG2  sing N N 548 
VAL   CB  HB   sing N N 549 
VAL   CG1 HG11 sing N N 550 
VAL   CG1 HG12 sing N N 551 
VAL   CG1 HG13 sing N N 552 
VAL   CG2 HG21 sing N N 553 
VAL   CG2 HG22 sing N N 554 
VAL   CG2 HG23 sing N N 555 
VAL   OXT HXT  sing N N 556 
# 
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                    8RWD 
_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]   0.025428 
_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]   0.005586 
_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]   0.007177 
_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  ? -22.624 21.716  0.708  1.00 66.95  ? 0    ALA   A N   1 
ATOM   2    C  CA  . ALA   A  1 25  ? -23.782 21.032  0.136  1.00 72.47  ? 0    ALA   A CA  1 
ATOM   3    C  C   . ALA   A  1 25  ? -24.847 20.764  1.199  1.00 74.99  ? 0    ALA   A C   1 
ATOM   4    O  O   . ALA   A  1 25  ? -24.516 20.569  2.366  1.00 71.52  ? 0    ALA   A O   1 
ATOM   5    C  CB  . ALA   A  1 25  ? -23.351 19.727  -0.522 1.00 67.20  ? 0    ALA   A CB  1 
ATOM   6    N  N   . PRO   A  1 26  ? -26.116 20.777  0.790  1.00 76.14  ? 1    PRO   A N   1 
ATOM   7    C  CA  . PRO   A  1 26  ? -27.213 20.540  1.737  1.00 64.47  ? 1    PRO   A CA  1 
ATOM   8    C  C   . PRO   A  1 26  ? -26.997 19.260  2.523  1.00 63.76  ? 1    PRO   A C   1 
ATOM   9    O  O   . PRO   A  1 26  ? -26.700 18.206  1.939  1.00 55.86  ? 1    PRO   A O   1 
ATOM   10   C  CB  . PRO   A  1 26  ? -28.447 20.434  0.831  1.00 66.04  ? 1    PRO   A CB  1 
ATOM   11   C  CG  . PRO   A  1 26  ? -28.117 21.249  -0.344 1.00 67.10  ? 1    PRO   A CG  1 
ATOM   12   C  CD  . PRO   A  1 26  ? -26.627 21.091  -0.562 1.00 67.40  ? 1    PRO   A CD  1 
ATOM   13   N  N   . PRO   A  1 27  ? -27.109 19.311  3.853  1.00 74.49  ? 2    PRO   A N   1 
ATOM   14   C  CA  . PRO   A  1 27  ? -26.792 18.114  4.649  1.00 63.30  ? 2    PRO   A CA  1 
ATOM   15   C  C   . PRO   A  1 27  ? -27.671 16.935  4.286  1.00 56.71  ? 2    PRO   A C   1 
ATOM   16   O  O   . PRO   A  1 27  ? -27.249 15.781  4.443  1.00 49.27  ? 2    PRO   A O   1 
ATOM   17   C  CB  . PRO   A  1 27  ? -27.002 18.575  6.099  1.00 65.90  ? 2    PRO   A CB  1 
ATOM   18   C  CG  . PRO   A  1 27  ? -27.043 20.080  6.040  1.00 80.99  ? 2    PRO   A CG  1 
ATOM   19   C  CD  . PRO   A  1 27  ? -27.591 20.421  4.691  1.00 73.42  ? 2    PRO   A CD  1 
ATOM   20   N  N   . ILE   A  1 28  ? -28.891 17.194  3.805  1.00 46.04  ? 3    ILE   A N   1 
ATOM   21   C  CA  . ILE   A  1 28  ? -29.813 16.121  3.473  1.00 55.49  ? 3    ILE   A CA  1 
ATOM   22   C  C   . ILE   A  1 28  ? -29.283 15.269  2.326  1.00 46.17  ? 3    ILE   A C   1 
ATOM   23   O  O   . ILE   A  1 28  ? -29.740 14.138  2.137  1.00 47.76  ? 3    ILE   A O   1 
ATOM   24   C  CB  . ILE   A  1 28  ? -31.191 16.724  3.121  1.00 48.39  ? 3    ILE   A CB  1 
ATOM   25   C  CG1 . ILE   A  1 28  ? -32.278 15.645  3.149  1.00 49.57  ? 3    ILE   A CG1 1 
ATOM   26   C  CG2 . ILE   A  1 28  ? -31.129 17.432  1.783  1.00 62.09  ? 3    ILE   A CG2 1 
ATOM   27   C  CD1 . ILE   A  1 28  ? -33.598 16.072  2.523  1.00 57.14  ? 3    ILE   A CD1 1 
ATOM   28   N  N   . MET   A  1 29  ? -28.314 15.776  1.561  1.00 46.66  ? 4    MET   A N   1 
ATOM   29   C  CA  . MET   A  1 29  ? -27.802 15.011  0.429  1.00 48.92  ? 4    MET   A CA  1 
ATOM   30   C  C   . MET   A  1 29  ? -26.874 13.906  0.918  1.00 46.29  ? 4    MET   A C   1 
ATOM   31   O  O   . MET   A  1 29  ? -27.096 12.722  0.636  1.00 47.00  ? 4    MET   A O   1 
ATOM   32   C  CB  . MET   A  1 29  ? -27.076 15.927  -0.562 1.00 43.80  ? 4    MET   A CB  1 
ATOM   33   C  CG  . MET   A  1 29  ? -27.968 16.930  -1.265 1.00 48.23  ? 4    MET   A CG  1 
ATOM   34   S  SD  . MET   A  1 29  ? -27.075 17.921  -2.474 1.00 55.68  ? 4    MET   A SD  1 
ATOM   35   C  CE  . MET   A  1 29  ? -26.646 16.666  -3.676 1.00 43.20  ? 4    MET   A CE  1 
ATOM   36   N  N   . GLY   A  1 30  ? -25.826 14.284  1.655  1.00 42.45  ? 5    GLY   A N   1 
ATOM   37   C  CA  . GLY   A  1 30  ? -24.958 13.289  2.262  1.00 39.51  ? 5    GLY   A CA  1 
ATOM   38   C  C   . GLY   A  1 30  ? -25.684 12.418  3.266  1.00 44.16  ? 5    GLY   A C   1 
ATOM   39   O  O   . GLY   A  1 30  ? -25.355 11.239  3.425  1.00 38.54  ? 5    GLY   A O   1 
ATOM   40   N  N   A SER   A  1 31  ? -26.681 12.980  3.953  0.70 37.32  ? 6    SER   A N   1 
ATOM   41   N  N   B SER   A  1 31  ? -26.676 12.981  3.961  0.30 37.54  ? 6    SER   A N   1 
ATOM   42   C  CA  A SER   A  1 31  ? -27.489 12.180  4.866  0.70 41.51  ? 6    SER   A CA  1 
ATOM   43   C  CA  B SER   A  1 31  ? -27.475 12.177  4.877  0.30 41.41  ? 6    SER   A CA  1 
ATOM   44   C  C   A SER   A  1 31  ? -28.313 11.148  4.108  0.70 38.67  ? 6    SER   A C   1 
ATOM   45   C  C   B SER   A  1 31  ? -28.312 11.150  4.129  0.30 38.59  ? 6    SER   A C   1 
ATOM   46   O  O   A SER   A  1 31  ? -28.508 10.028  4.593  0.70 37.21  ? 6    SER   A O   1 
ATOM   47   O  O   B SER   A  1 31  ? -28.511 10.037  4.626  0.30 37.11  ? 6    SER   A O   1 
ATOM   48   C  CB  A SER   A  1 31  ? -28.398 13.083  5.699  0.70 41.74  ? 6    SER   A CB  1 
ATOM   49   C  CB  B SER   A  1 31  ? -28.371 13.076  5.728  0.30 41.81  ? 6    SER   A CB  1 
ATOM   50   O  OG  A SER   A  1 31  ? -27.646 13.873  6.603  0.70 52.32  ? 6    SER   A OG  1 
ATOM   51   O  OG  B SER   A  1 31  ? -29.194 12.311  6.591  0.30 42.79  ? 6    SER   A OG  1 
ATOM   52   N  N   A SER   A  1 32  ? -28.801 11.506  2.917  0.70 36.68  ? 7    SER   A N   1 
ATOM   53   N  N   B SER   A  1 32  ? -28.802 11.498  2.935  0.30 36.76  ? 7    SER   A N   1 
ATOM   54   C  CA  A SER   A  1 32  ? -29.608 10.573  2.135  0.70 35.09  ? 7    SER   A CA  1 
ATOM   55   C  CA  B SER   A  1 32  ? -29.610 10.558  2.163  0.30 35.17  ? 7    SER   A CA  1 
ATOM   56   C  C   A SER   A  1 32  ? -28.806 9.338   1.751  0.70 28.86  ? 7    SER   A C   1 
ATOM   57   C  C   B SER   A  1 32  ? -28.801 9.330   1.766  0.30 29.11  ? 7    SER   A C   1 
ATOM   58   O  O   A SER   A  1 32  ? -29.325 8.217   1.782  0.70 31.57  ? 7    SER   A O   1 
ATOM   59   O  O   B SER   A  1 32  ? -29.314 8.206   1.797  0.30 31.55  ? 7    SER   A O   1 
ATOM   60   C  CB  A SER   A  1 32  ? -30.154 11.267  0.887  0.70 40.47  ? 7    SER   A CB  1 
ATOM   61   C  CB  B SER   A  1 32  ? -30.181 11.247  0.924  0.30 40.42  ? 7    SER   A CB  1 
ATOM   62   O  OG  A SER   A  1 32  ? -31.197 12.166  1.221  0.70 39.97  ? 7    SER   A OG  1 
ATOM   63   O  OG  B SER   A  1 32  ? -29.179 11.433  -0.060 0.30 37.53  ? 7    SER   A OG  1 
ATOM   64   N  N   . VAL   A  1 33  ? -27.537 9.524   1.385  1.00 24.71  ? 8    VAL   A N   1 
ATOM   65   C  CA  . VAL   A  1 33  ? -26.675 8.388   1.070  1.00 29.25  ? 8    VAL   A CA  1 
ATOM   66   C  C   . VAL   A  1 33  ? -26.450 7.541   2.317  1.00 34.66  ? 8    VAL   A C   1 
ATOM   67   O  O   . VAL   A  1 33  ? -26.593 6.313   2.287  1.00 24.27  ? 8    VAL   A O   1 
ATOM   68   C  CB  . VAL   A  1 33  ? -25.347 8.870   0.461  1.00 32.17  ? 8    VAL   A CB  1 
ATOM   69   C  CG1 . VAL   A  1 33  ? -24.359 7.716   0.351  1.00 25.01  ? 8    VAL   A CG1 1 
ATOM   70   C  CG2 . VAL   A  1 33  ? -25.594 9.487   -0.903 1.00 38.20  ? 8    VAL   A CG2 1 
ATOM   71   N  N   . TYR   A  1 34  ? -26.081 8.188   3.427  1.00 34.06  ? 9    TYR   A N   1 
ATOM   72   C  CA  . TYR   A  1 34  ? -25.862 7.472   4.680  1.00 28.59  ? 9    TYR   A CA  1 
ATOM   73   C  C   . TYR   A  1 34  ? -27.106 6.695   5.094  1.00 26.50  ? 9    TYR   A C   1 
ATOM   74   O  O   . TYR   A  1 34  ? -27.028 5.508   5.429  1.00 24.79  ? 9    TYR   A O   1 
ATOM   75   C  CB  . TYR   A  1 34  ? -25.458 8.455   5.780  1.00 34.61  ? 9    TYR   A CB  1 
ATOM   76   C  CG  . TYR   A  1 34  ? -25.519 7.861   7.171  1.00 30.43  ? 9    TYR   A CG  1 
ATOM   77   C  CD1 . TYR   A  1 34  ? -24.698 6.801   7.535  1.00 25.41  ? 9    TYR   A CD1 1 
ATOM   78   C  CD2 . TYR   A  1 34  ? -26.426 8.338   8.107  1.00 30.64  ? 9    TYR   A CD2 1 
ATOM   79   C  CE1 . TYR   A  1 34  ? -24.766 6.248   8.801  1.00 25.47  ? 9    TYR   A CE1 1 
ATOM   80   C  CE2 . TYR   A  1 34  ? -26.502 7.794   9.375  1.00 27.72  ? 9    TYR   A CE2 1 
ATOM   81   C  CZ  . TYR   A  1 34  ? -25.673 6.748   9.715  1.00 27.23  ? 9    TYR   A CZ  1 
ATOM   82   O  OH  . TYR   A  1 34  ? -25.745 6.210   10.977 1.00 30.81  ? 9    TYR   A OH  1 
ATOM   83   N  N   . ILE   A  1 35  ? -28.270 7.350   5.058  1.00 23.32  ? 10   ILE   A N   1 
ATOM   84   C  CA  . ILE   A  1 35  ? -29.510 6.714   5.502  1.00 28.41  ? 10   ILE   A CA  1 
ATOM   85   C  C   . ILE   A  1 35  ? -29.883 5.557   4.583  1.00 25.54  ? 10   ILE   A C   1 
ATOM   86   O  O   . ILE   A  1 35  ? -30.318 4.496   5.046  1.00 27.43  ? 10   ILE   A O   1 
ATOM   87   C  CB  . ILE   A  1 35  ? -30.645 7.751   5.609  1.00 27.62  ? 10   ILE   A CB  1 
ATOM   88   C  CG1 . ILE   A  1 35  ? -30.367 8.732   6.751  1.00 34.03  ? 10   ILE   A CG1 1 
ATOM   89   C  CG2 . ILE   A  1 35  ? -31.992 7.070   5.802  1.00 25.73  ? 10   ILE   A CG2 1 
ATOM   90   C  CD1 . ILE   A  1 35  ? -31.367 9.864   6.846  1.00 36.40  ? 10   ILE   A CD1 1 
ATOM   91   N  N   . THR   A  1 36  ? -29.729 5.741   3.270  1.00 27.49  ? 11   THR   A N   1 
ATOM   92   C  CA  . THR   A  1 36  ? -30.067 4.673   2.335  1.00 30.82  ? 11   THR   A CA  1 
ATOM   93   C  C   . THR   A  1 36  ? -29.190 3.449   2.566  1.00 19.48  ? 11   THR   A C   1 
ATOM   94   O  O   . THR   A  1 36  ? -29.676 2.312   2.541  1.00 21.94  ? 11   THR   A O   1 
ATOM   95   C  CB  . THR   A  1 36  ? -29.919 5.166   0.895  1.00 31.09  ? 11   THR   A CB  1 
ATOM   96   O  OG1 . THR   A  1 36  ? -30.741 6.324   0.695  1.00 28.18  ? 11   THR   A OG1 1 
ATOM   97   C  CG2 . THR   A  1 36  ? -30.329 4.079   -0.089 1.00 26.80  ? 11   THR   A CG2 1 
ATOM   98   N  N   . VAL   A  1 37  ? -27.892 3.664   2.788  1.00 22.78  ? 12   VAL   A N   1 
ATOM   99   C  CA  . VAL   A  1 37  ? -26.989 2.549   3.060  1.00 21.58  ? 12   VAL   A CA  1 
ATOM   100  C  C   . VAL   A  1 37  ? -27.392 1.847   4.352  1.00 24.84  ? 12   VAL   A C   1 
ATOM   101  O  O   . VAL   A  1 37  ? -27.414 0.612   4.424  1.00 24.32  ? 12   VAL   A O   1 
ATOM   102  C  CB  . VAL   A  1 37  ? -25.532 3.044   3.104  1.00 23.94  ? 12   VAL   A CB  1 
ATOM   103  C  CG1 . VAL   A  1 37  ? -24.623 1.985   3.713  1.00 24.91  ? 12   VAL   A CG1 1 
ATOM   104  C  CG2 . VAL   A  1 37  ? -25.063 3.443   1.711  1.00 30.04  ? 12   VAL   A CG2 1 
ATOM   105  N  N   . GLU   A  1 38  ? -27.722 2.621   5.392  1.00 22.36  ? 13   GLU   A N   1 
ATOM   106  C  CA  . GLU   A  1 38  ? -28.134 2.030   6.664  1.00 20.50  ? 13   GLU   A CA  1 
ATOM   107  C  C   . GLU   A  1 38  ? -29.375 1.163   6.491  1.00 19.95  ? 13   GLU   A C   1 
ATOM   108  O  O   . GLU   A  1 38  ? -29.446 0.044   7.013  1.00 21.95  ? 13   GLU   A O   1 
ATOM   109  C  CB  . GLU   A  1 38  ? -28.410 3.137   7.685  1.00 23.19  ? 13   GLU   A CB  1 
ATOM   110  C  CG  . GLU   A  1 38  ? -27.181 3.851   8.222  1.00 23.14  ? 13   GLU   A CG  1 
ATOM   111  C  CD  . GLU   A  1 38  ? -26.529 3.116   9.379  1.00 27.89  ? 13   GLU   A CD  1 
ATOM   112  O  OE1 . GLU   A  1 38  ? -26.183 1.926   9.223  1.00 29.34  ? 13   GLU   A OE1 1 
ATOM   113  O  OE2 . GLU   A  1 38  ? -26.361 3.737   10.449 1.00 24.51  ? 13   GLU   A OE2 1 
ATOM   114  N  N   . LEU   A  1 39  ? -30.366 1.667   5.753  1.00 24.23  ? 14   LEU   A N   1 
ATOM   115  C  CA  . LEU   A  1 39  ? -31.585 0.899   5.523  1.00 25.00  ? 14   LEU   A CA  1 
ATOM   116  C  C   . LEU   A  1 39  ? -31.300 -0.381  4.745  1.00 22.62  ? 14   LEU   A C   1 
ATOM   117  O  O   . LEU   A  1 39  ? -31.874 -1.435  5.042  1.00 23.81  ? 14   LEU   A O   1 
ATOM   118  C  CB  . LEU   A  1 39  ? -32.615 1.764   4.803  1.00 28.03  ? 14   LEU   A CB  1 
ATOM   119  C  CG  . LEU   A  1 39  ? -33.152 2.915   5.658  1.00 33.88  ? 14   LEU   A CG  1 
ATOM   120  C  CD1 . LEU   A  1 39  ? -34.041 3.834   4.837  1.00 36.95  ? 14   LEU   A CD1 1 
ATOM   121  C  CD2 . LEU   A  1 39  ? -33.892 2.378   6.872  1.00 31.57  ? 14   LEU   A CD2 1 
ATOM   122  N  N   . ALA   A  1 40  ? -30.417 -0.307  3.745  1.00 23.74  ? 15   ALA   A N   1 
ATOM   123  C  CA  . ALA   A  1 40  ? -30.020 -1.506  3.015  1.00 25.70  ? 15   ALA   A CA  1 
ATOM   124  C  C   . ALA   A  1 40  ? -29.371 -2.524  3.944  1.00 25.91  ? 15   ALA   A C   1 
ATOM   125  O  O   . ALA   A  1 40  ? -29.635 -3.729  3.843  1.00 24.13  ? 15   ALA   A O   1 
ATOM   126  C  CB  . ALA   A  1 40  ? -29.067 -1.134  1.878  1.00 24.61  ? 15   ALA   A CB  1 
ATOM   127  N  N   . ILE   A  1 41  ? -28.519 -2.058  4.858  1.00 23.22  ? 16   ILE   A N   1 
ATOM   128  C  CA  . ILE   A  1 41  ? -27.868 -2.968  5.794  1.00 24.34  ? 16   ILE   A CA  1 
ATOM   129  C  C   . ILE   A  1 41  ? -28.900 -3.591  6.726  1.00 22.57  ? 16   ILE   A C   1 
ATOM   130  O  O   . ILE   A  1 41  ? -28.835 -4.788  7.035  1.00 26.37  ? 16   ILE   A O   1 
ATOM   131  C  CB  . ILE   A  1 41  ? -26.767 -2.226  6.572  1.00 26.58  ? 16   ILE   A CB  1 
ATOM   132  C  CG1 . ILE   A  1 41  ? -25.630 -1.832  5.629  1.00 24.82  ? 16   ILE   A CG1 1 
ATOM   133  C  CG2 . ILE   A  1 41  ? -26.240 -3.081  7.720  1.00 21.98  ? 16   ILE   A CG2 1 
ATOM   134  C  CD1 . ILE   A  1 41  ? -24.670 -0.848  6.231  1.00 19.95  ? 16   ILE   A CD1 1 
ATOM   135  N  N   . ALA   A  1 42  ? -29.869 -2.792  7.185  1.00 24.76  ? 17   ALA   A N   1 
ATOM   136  C  CA  . ALA   A  1 42  ? -30.885 -3.302  8.100  1.00 22.55  ? 17   ALA   A CA  1 
ATOM   137  C  C   . ALA   A  1 42  ? -31.694 -4.420  7.457  1.00 25.26  ? 17   ALA   A C   1 
ATOM   138  O  O   . ALA   A  1 42  ? -31.946 -5.455  8.086  1.00 29.02  ? 17   ALA   A O   1 
ATOM   139  C  CB  . ALA   A  1 42  ? -31.804 -2.166  8.551  1.00 18.84  ? 17   ALA   A CB  1 
ATOM   140  N  N   . VAL   A  1 43  ? -32.102 -4.232  6.200  1.00 29.06  ? 18   VAL   A N   1 
ATOM   141  C  CA  . VAL   A  1 43  ? -32.865 -5.261  5.495  1.00 27.40  ? 18   VAL   A CA  1 
ATOM   142  C  C   . VAL   A  1 43  ? -32.074 -6.561  5.439  1.00 23.98  ? 18   VAL   A C   1 
ATOM   143  O  O   . VAL   A  1 43  ? -32.599 -7.644  5.723  1.00 22.10  ? 18   VAL   A O   1 
ATOM   144  C  CB  . VAL   A  1 43  ? -33.245 -4.774  4.085  1.00 28.19  ? 18   VAL   A CB  1 
ATOM   145  C  CG1 . VAL   A  1 43  ? -33.795 -5.926  3.256  1.00 29.68  ? 18   VAL   A CG1 1 
ATOM   146  C  CG2 . VAL   A  1 43  ? -34.252 -3.636  4.166  1.00 27.62  ? 18   VAL   A CG2 1 
ATOM   147  N  N   . LEU   A  1 44  ? -30.792 -6.468  5.082  1.00 24.21  ? 19   LEU   A N   1 
ATOM   148  C  CA  . LEU   A  1 44  ? -29.982 -7.670  4.921  1.00 23.13  ? 19   LEU   A CA  1 
ATOM   149  C  C   . LEU   A  1 44  ? -29.692 -8.326  6.265  1.00 27.91  ? 19   LEU   A C   1 
ATOM   150  O  O   . LEU   A  1 44  ? -29.636 -9.559  6.361  1.00 27.34  ? 19   LEU   A O   1 
ATOM   151  C  CB  . LEU   A  1 44  ? -28.681 -7.323  4.199  1.00 23.88  ? 19   LEU   A CB  1 
ATOM   152  C  CG  . LEU   A  1 44  ? -28.826 -6.874  2.743  1.00 31.26  ? 19   LEU   A CG  1 
ATOM   153  C  CD1 . LEU   A  1 44  ? -27.534 -6.236  2.247  1.00 23.69  ? 19   LEU   A CD1 1 
ATOM   154  C  CD2 . LEU   A  1 44  ? -29.235 -8.036  1.850  1.00 32.22  ? 19   LEU   A CD2 1 
ATOM   155  N  N   . ALA   A  1 45  ? -29.492 -7.520  7.312  1.00 23.77  ? 20   ALA   A N   1 
ATOM   156  C  CA  . ALA   A  1 45  ? -29.244 -8.079  8.639  1.00 25.01  ? 20   ALA   A CA  1 
ATOM   157  C  C   . ALA   A  1 45  ? -30.454 -8.855  9.144  1.00 26.20  ? 20   ALA   A C   1 
ATOM   158  O  O   . ALA   A  1 45  ? -30.313 -9.935  9.729  1.00 26.27  ? 20   ALA   A O   1 
ATOM   159  C  CB  . ALA   A  1 45  ? -28.874 -6.967  9.620  1.00 20.06  ? 20   ALA   A CB  1 
ATOM   160  N  N   . ILE   A  1 46  ? -31.653 -8.312  8.928  1.00 25.34  ? 21   ILE   A N   1 
ATOM   161  C  CA  . ILE   A  1 46  ? -32.876 -8.992  9.342  1.00 30.25  ? 21   ILE   A CA  1 
ATOM   162  C  C   . ILE   A  1 46  ? -33.069 -10.286 8.556  1.00 30.41  ? 21   ILE   A C   1 
ATOM   163  O  O   . ILE   A  1 46  ? -33.283 -11.355 9.139  1.00 29.38  ? 21   ILE   A O   1 
ATOM   164  C  CB  . ILE   A  1 46  ? -34.083 -8.048  9.197  1.00 27.09  ? 21   ILE   A CB  1 
ATOM   165  C  CG1 . ILE   A  1 46  ? -33.936 -6.861  10.152 1.00 27.94  ? 21   ILE   A CG1 1 
ATOM   166  C  CG2 . ILE   A  1 46  ? -35.381 -8.795  9.465  1.00 33.55  ? 21   ILE   A CG2 1 
ATOM   167  C  CD1 . ILE   A  1 46  ? -34.871 -5.708  9.855  1.00 25.08  ? 21   ILE   A CD1 1 
ATOM   168  N  N   . LEU   A  1 47  ? -32.986 -10.211 7.224  1.00 28.37  ? 22   LEU   A N   1 
ATOM   169  C  CA  . LEU   A  1 47  ? -33.289 -11.373 6.392  1.00 24.64  ? 22   LEU   A CA  1 
ATOM   170  C  C   . LEU   A  1 47  ? -32.331 -12.524 6.667  1.00 30.26  ? 22   LEU   A C   1 
ATOM   171  O  O   . LEU   A  1 47  ? -32.755 -13.673 6.838  1.00 29.06  ? 22   LEU   A O   1 
ATOM   172  C  CB  . LEU   A  1 47  ? -33.226 -10.988 4.913  1.00 31.15  ? 22   LEU   A CB  1 
ATOM   173  C  CG  . LEU   A  1 47  ? -34.317 -10.077 4.359  1.00 28.20  ? 22   LEU   A CG  1 
ATOM   174  C  CD1 . LEU   A  1 47  ? -34.019 -9.744  2.907  1.00 37.49  ? 22   LEU   A CD1 1 
ATOM   175  C  CD2 . LEU   A  1 47  ? -35.672 -10.746 4.494  1.00 42.39  ? 22   LEU   A CD2 1 
ATOM   176  N  N   . GLY   A  1 48  ? -31.033 -12.233 6.727  1.00 23.77  ? 23   GLY   A N   1 
ATOM   177  C  CA  . GLY   A  1 48  ? -30.062 -13.300 6.889  1.00 23.44  ? 23   GLY   A CA  1 
ATOM   178  C  C   . GLY   A  1 48  ? -30.166 -13.971 8.243  1.00 30.16  ? 23   GLY   A C   1 
ATOM   179  O  O   . GLY   A  1 48  ? -30.057 -15.196 8.352  1.00 28.03  ? 23   GLY   A O   1 
ATOM   180  N  N   . ASN   A  1 49  ? -30.376 -13.181 9.292  1.00 26.35  ? 24   ASN   A N   1 
ATOM   181  C  CA  . ASN   A  1 49  ? -30.384 -13.735 10.636 1.00 28.17  ? 24   ASN   A CA  1 
ATOM   182  C  C   . ASN   A  1 49  ? -31.728 -14.353 11.008 1.00 28.16  ? 24   ASN   A C   1 
ATOM   183  O  O   . ASN   A  1 49  ? -31.766 -15.269 11.836 1.00 32.10  ? 24   ASN   A O   1 
ATOM   184  C  CB  . ASN   A  1 49  ? -29.970 -12.649 11.625 1.00 22.79  ? 24   ASN   A CB  1 
ATOM   185  C  CG  . ASN   A  1 49  ? -28.491 -12.335 11.531 1.00 28.31  ? 24   ASN   A CG  1 
ATOM   186  O  OD1 . ASN   A  1 49  ? -27.651 -13.150 11.914 1.00 24.55  ? 24   ASN   A OD1 1 
ATOM   187  N  ND2 . ASN   A  1 49  ? -28.163 -11.172 10.979 1.00 24.24  ? 24   ASN   A ND2 1 
ATOM   188  N  N   . VAL   A  1 50  ? -32.835 -13.868 10.438 1.00 29.22  ? 25   VAL   A N   1 
ATOM   189  C  CA  . VAL   A  1 50  ? -34.079 -14.634 10.512 1.00 33.50  ? 25   VAL   A CA  1 
ATOM   190  C  C   . VAL   A  1 50  ? -33.880 -16.019 9.905  1.00 37.86  ? 25   VAL   A C   1 
ATOM   191  O  O   . VAL   A  1 50  ? -34.352 -17.027 10.447 1.00 35.23  ? 25   VAL   A O   1 
ATOM   192  C  CB  . VAL   A  1 50  ? -35.228 -13.868 9.829  1.00 34.53  ? 25   VAL   A CB  1 
ATOM   193  C  CG1 . VAL   A  1 50  ? -36.375 -14.812 9.490  1.00 31.00  ? 25   VAL   A CG1 1 
ATOM   194  C  CG2 . VAL   A  1 50  ? -35.714 -12.736 10.723 1.00 31.00  ? 25   VAL   A CG2 1 
ATOM   195  N  N   . LEU   A  1 51  ? -33.168 -16.089 8.776  1.00 34.03  ? 26   LEU   A N   1 
ATOM   196  C  CA  . LEU   A  1 51  ? -32.899 -17.375 8.138  1.00 34.27  ? 26   LEU   A CA  1 
ATOM   197  C  C   . LEU   A  1 51  ? -32.067 -18.273 9.043  1.00 37.48  ? 26   LEU   A C   1 
ATOM   198  O  O   . LEU   A  1 51  ? -32.285 -19.489 9.096  1.00 32.58  ? 26   LEU   A O   1 
ATOM   199  C  CB  . LEU   A  1 51  ? -32.191 -17.156 6.801  1.00 38.22  ? 26   LEU   A CB  1 
ATOM   200  C  CG  . LEU   A  1 51  ? -32.009 -18.367 5.883  1.00 51.79  ? 26   LEU   A CG  1 
ATOM   201  C  CD1 . LEU   A  1 51  ? -33.349 -18.929 5.437  1.00 50.92  ? 26   LEU   A CD1 1 
ATOM   202  C  CD2 . LEU   A  1 51  ? -31.150 -17.998 4.683  1.00 41.32  ? 26   LEU   A CD2 1 
ATOM   203  N  N   . VAL   A  1 52  ? -31.097 -17.692 9.750  1.00 23.50  ? 27   VAL   A N   1 
ATOM   204  C  CA  . VAL   A  1 52  ? -30.316 -18.456 10.720 1.00 28.52  ? 27   VAL   A CA  1 
ATOM   205  C  C   . VAL   A  1 52  ? -31.231 -19.040 11.791 1.00 31.64  ? 27   VAL   A C   1 
ATOM   206  O  O   . VAL   A  1 52  ? -31.171 -20.235 12.103 1.00 32.47  ? 27   VAL   A O   1 
ATOM   207  C  CB  . VAL   A  1 52  ? -29.212 -17.575 11.334 1.00 29.77  ? 27   VAL   A CB  1 
ATOM   208  C  CG1 . VAL   A  1 52  ? -28.644 -18.231 12.583 1.00 25.25  ? 27   VAL   A CG1 1 
ATOM   209  C  CG2 . VAL   A  1 52  ? -28.115 -17.319 10.314 1.00 34.05  ? 27   VAL   A CG2 1 
ATOM   210  N  N   . CYS   A  1 53  ? -32.085 -18.196 12.379 1.00 27.88  ? 28   CYS   A N   1 
ATOM   211  C  CA  . CYS   A  1 53  ? -32.957 -18.652 13.457 1.00 32.08  ? 28   CYS   A CA  1 
ATOM   212  C  C   . CYS   A  1 53  ? -33.947 -19.701 12.969 1.00 39.38  ? 28   CYS   A C   1 
ATOM   213  O  O   . CYS   A  1 53  ? -34.229 -20.674 13.678 1.00 33.25  ? 28   CYS   A O   1 
ATOM   214  C  CB  . CYS   A  1 53  ? -33.695 -17.465 14.076 1.00 36.98  ? 28   CYS   A CB  1 
ATOM   215  S  SG  . CYS   A  1 53  ? -32.628 -16.280 14.923 1.00 35.73  ? 28   CYS   A SG  1 
ATOM   216  N  N   A TRP   A  1 54  ? -34.493 -19.521 11.763 0.47 38.90  ? 29   TRP   A N   1 
ATOM   217  N  N   B TRP   A  1 54  ? -34.489 -19.518 11.762 0.53 38.90  ? 29   TRP   A N   1 
ATOM   218  C  CA  A TRP   A  1 54  ? -35.436 -20.503 11.238 0.47 40.67  ? 29   TRP   A CA  1 
ATOM   219  C  CA  B TRP   A  1 54  ? -35.430 -20.493 11.219 0.53 40.66  ? 29   TRP   A CA  1 
ATOM   220  C  C   A TRP   A  1 54  ? -34.758 -21.837 10.954 0.47 39.29  ? 29   TRP   A C   1 
ATOM   221  C  C   B TRP   A  1 54  ? -34.753 -21.835 10.973 0.53 39.29  ? 29   TRP   A C   1 
ATOM   222  O  O   A TRP   A  1 54  ? -35.389 -22.890 11.091 0.47 40.27  ? 29   TRP   A O   1 
ATOM   223  O  O   B TRP   A  1 54  ? -35.371 -22.891 11.149 0.53 40.22  ? 29   TRP   A O   1 
ATOM   224  C  CB  A TRP   A  1 54  ? -36.114 -19.973 9.974  0.47 42.49  ? 29   TRP   A CB  1 
ATOM   225  C  CB  B TRP   A  1 54  ? -36.053 -19.962 9.927  0.53 42.42  ? 29   TRP   A CB  1 
ATOM   226  C  CG  A TRP   A  1 54  ? -37.507 -20.505 9.786  0.47 50.33  ? 29   TRP   A CG  1 
ATOM   227  C  CG  B TRP   A  1 54  ? -37.466 -19.474 10.082 0.53 50.20  ? 29   TRP   A CG  1 
ATOM   228  C  CD1 A TRP   A  1 54  ? -38.245 -21.204 10.697 0.47 55.56  ? 29   TRP   A CD1 1 
ATOM   229  C  CD1 B TRP   A  1 54  ? -37.913 -18.195 9.916  0.53 48.65  ? 29   TRP   A CD1 1 
ATOM   230  C  CD2 A TRP   A  1 54  ? -38.327 -20.381 8.617  0.47 51.22  ? 29   TRP   A CD2 1 
ATOM   231  C  CD2 B TRP   A  1 54  ? -38.616 -20.259 10.425 0.53 52.95  ? 29   TRP   A CD2 1 
ATOM   232  N  NE1 A TRP   A  1 54  ? -39.472 -21.523 10.169 0.47 59.26  ? 29   TRP   A NE1 1 
ATOM   233  N  NE1 B TRP   A  1 54  ? -39.268 -18.135 10.138 0.53 57.09  ? 29   TRP   A NE1 1 
ATOM   234  C  CE2 A TRP   A  1 54  ? -39.548 -21.029 8.893  0.47 54.84  ? 29   TRP   A CE2 1 
ATOM   235  C  CE2 B TRP   A  1 54  ? -39.724 -19.388 10.452 0.53 57.36  ? 29   TRP   A CE2 1 
ATOM   236  C  CE3 A TRP   A  1 54  ? -38.149 -19.785 7.365  0.47 56.53  ? 29   TRP   A CE3 1 
ATOM   237  C  CE3 B TRP   A  1 54  ? -38.816 -21.613 10.714 0.53 57.09  ? 29   TRP   A CE3 1 
ATOM   238  C  CZ2 A TRP   A  1 54  ? -40.583 -21.098 7.964  0.47 59.42  ? 29   TRP   A CZ2 1 
ATOM   239  C  CZ2 B TRP   A  1 54  ? -41.012 -19.827 10.755 0.53 55.56  ? 29   TRP   A CZ2 1 
ATOM   240  C  CZ3 A TRP   A  1 54  ? -39.178 -19.855 6.444  0.47 52.64  ? 29   TRP   A CZ3 1 
ATOM   241  C  CZ3 B TRP   A  1 54  ? -40.096 -22.046 11.015 0.53 54.39  ? 29   TRP   A CZ3 1 
ATOM   242  C  CH2 A TRP   A  1 54  ? -40.380 -20.506 6.748  0.47 56.01  ? 29   TRP   A CH2 1 
ATOM   243  C  CH2 B TRP   A  1 54  ? -41.177 -21.156 11.032 0.53 56.90  ? 29   TRP   A CH2 1 
ATOM   244  N  N   . ALA   A  1 55  ? -33.482 -21.815 10.565 1.00 33.45  ? 30   ALA   A N   1 
ATOM   245  C  CA  . ALA   A  1 55  ? -32.766 -23.063 10.324 1.00 34.71  ? 30   ALA   A CA  1 
ATOM   246  C  C   . ALA   A  1 55  ? -32.600 -23.857 11.615 1.00 42.19  ? 30   ALA   A C   1 
ATOM   247  O  O   . ALA   A  1 55  ? -32.826 -25.072 11.643 1.00 39.38  ? 30   ALA   A O   1 
ATOM   248  C  CB  . ALA   A  1 55  ? -31.405 -22.772 9.690  1.00 32.39  ? 30   ALA   A CB  1 
ATOM   249  N  N   . VAL   A  1 56  ? -32.194 -23.184 12.695 1.00 36.44  ? 31   VAL   A N   1 
ATOM   250  C  CA  . VAL   A  1 56  ? -32.001 -23.868 13.971 1.00 35.30  ? 31   VAL   A CA  1 
ATOM   251  C  C   . VAL   A  1 56  ? -33.322 -24.410 14.500 1.00 42.56  ? 31   VAL   A C   1 
ATOM   252  O  O   . VAL   A  1 56  ? -33.392 -25.541 14.996 1.00 37.77  ? 31   VAL   A O   1 
ATOM   253  C  CB  . VAL   A  1 56  ? -31.331 -22.924 14.987 1.00 33.07  ? 31   VAL   A CB  1 
ATOM   254  C  CG1 . VAL   A  1 56  ? -31.172 -23.617 16.330 1.00 29.79  ? 31   VAL   A CG1 1 
ATOM   255  C  CG2 . VAL   A  1 56  ? -29.979 -22.464 14.464 1.00 35.71  ? 31   VAL   A CG2 1 
ATOM   256  N  N   . TRP   A  1 57  ? -34.387 -23.609 14.413 1.00 36.95  ? 32   TRP   A N   1 
ATOM   257  C  CA  . TRP   A  1 57  ? -35.700 -24.056 14.869 1.00 48.36  ? 32   TRP   A CA  1 
ATOM   258  C  C   . TRP   A  1 57  ? -36.157 -25.304 14.118 1.00 50.57  ? 32   TRP   A C   1 
ATOM   259  O  O   . TRP   A  1 57  ? -36.732 -26.221 14.714 1.00 53.02  ? 32   TRP   A O   1 
ATOM   260  C  CB  . TRP   A  1 57  ? -36.717 -22.925 14.702 1.00 44.09  ? 32   TRP   A CB  1 
ATOM   261  C  CG  . TRP   A  1 57  ? -38.138 -23.291 15.053 1.00 58.90  ? 32   TRP   A CG  1 
ATOM   262  C  CD1 . TRP   A  1 57  ? -39.015 -24.031 14.308 1.00 57.44  ? 32   TRP   A CD1 1 
ATOM   263  C  CD2 . TRP   A  1 57  ? -38.854 -22.885 16.226 1.00 64.98  ? 32   TRP   A CD2 1 
ATOM   264  N  NE1 . TRP   A  1 57  ? -40.221 -24.132 14.961 1.00 61.59  ? 32   TRP   A NE1 1 
ATOM   265  C  CE2 . TRP   A  1 57  ? -40.149 -23.434 16.139 1.00 69.97  ? 32   TRP   A CE2 1 
ATOM   266  C  CE3 . TRP   A  1 57  ? -38.521 -22.117 17.347 1.00 65.95  ? 32   TRP   A CE3 1 
ATOM   267  C  CZ2 . TRP   A  1 57  ? -41.111 -23.240 17.131 1.00 66.76  ? 32   TRP   A CZ2 1 
ATOM   268  C  CZ3 . TRP   A  1 57  ? -39.476 -21.925 18.330 1.00 64.68  ? 32   TRP   A CZ3 1 
ATOM   269  C  CH2 . TRP   A  1 57  ? -40.756 -22.483 18.215 1.00 66.72  ? 32   TRP   A CH2 1 
ATOM   270  N  N   . LEU   A  1 58  ? -35.903 -25.358 12.807 1.00 44.69  ? 33   LEU   A N   1 
ATOM   271  C  CA  . LEU   A  1 58  ? -36.465 -26.419 11.977 1.00 48.25  ? 33   LEU   A CA  1 
ATOM   272  C  C   . LEU   A  1 58  ? -35.641 -27.701 12.004 1.00 57.63  ? 33   LEU   A C   1 
ATOM   273  O  O   . LEU   A  1 58  ? -36.211 -28.795 11.930 1.00 53.06  ? 33   LEU   A O   1 
ATOM   274  C  CB  . LEU   A  1 58  ? -36.601 -25.935 10.532 1.00 44.90  ? 33   LEU   A CB  1 
ATOM   275  C  CG  . LEU   A  1 58  ? -37.728 -24.949 10.220 1.00 51.05  ? 33   LEU   A CG  1 
ATOM   276  C  CD1 . LEU   A  1 58  ? -37.725 -24.591 8.742  1.00 52.79  ? 33   LEU   A CD1 1 
ATOM   277  C  CD2 . LEU   A  1 58  ? -39.075 -25.523 10.631 1.00 53.86  ? 33   LEU   A CD2 1 
ATOM   278  N  N   . ASN   A  1 59  ? -34.318 -27.599 12.103 1.00 42.53  ? 34   ASN   A N   1 
ATOM   279  C  CA  . ASN   A  1 59  ? -33.428 -28.739 11.909 1.00 42.26  ? 34   ASN   A CA  1 
ATOM   280  C  C   . ASN   A  1 59  ? -32.869 -29.152 13.265 1.00 55.15  ? 34   ASN   A C   1 
ATOM   281  O  O   . ASN   A  1 59  ? -32.037 -28.444 13.843 1.00 41.44  ? 34   ASN   A O   1 
ATOM   282  C  CB  . ASN   A  1 59  ? -32.312 -28.391 10.925 1.00 40.19  ? 34   ASN   A CB  1 
ATOM   283  C  CG  . ASN   A  1 59  ? -31.451 -29.590 10.562 1.00 52.14  ? 34   ASN   A CG  1 
ATOM   284  O  OD1 . ASN   A  1 59  ? -31.568 -30.662 11.155 1.00 54.59  ? 34   ASN   A OD1 1 
ATOM   285  N  ND2 . ASN   A  1 59  ? -30.578 -29.410 9.577  1.00 48.54  ? 34   ASN   A ND2 1 
ATOM   286  N  N   . SER   A  1 60  ? -33.319 -30.308 13.764 1.00 47.20  ? 35   SER   A N   1 
ATOM   287  C  CA  . SER   A  1 60  ? -32.849 -30.800 15.054 1.00 44.34  ? 35   SER   A CA  1 
ATOM   288  C  C   . SER   A  1 60  ? -31.365 -31.140 15.036 1.00 42.25  ? 35   SER   A C   1 
ATOM   289  O  O   . SER   A  1 60  ? -30.738 -31.192 16.100 1.00 52.33  ? 35   SER   A O   1 
ATOM   290  C  CB  . SER   A  1 60  ? -33.665 -32.023 15.478 1.00 46.52  ? 35   SER   A CB  1 
ATOM   291  O  OG  . SER   A  1 60  ? -33.102 -33.214 14.955 1.00 57.71  ? 35   SER   A OG  1 
ATOM   292  N  N   . ASN   A  1 61  ? -30.789 -31.372 13.853 1.00 38.31  ? 36   ASN   A N   1 
ATOM   293  C  CA  . ASN   A  1 61  ? -29.349 -31.576 13.748 1.00 41.99  ? 36   ASN   A CA  1 
ATOM   294  C  C   . ASN   A  1 61  ? -28.570 -30.305 14.059 1.00 52.45  ? 36   ASN   A C   1 
ATOM   295  O  O   . ASN   A  1 61  ? -27.363 -30.376 14.315 1.00 43.83  ? 36   ASN   A O   1 
ATOM   296  C  CB  . ASN   A  1 61  ? -28.998 -32.085 12.352 1.00 48.80  ? 36   ASN   A CB  1 
ATOM   297  C  CG  . ASN   A  1 61  ? -29.527 -33.482 12.098 1.00 58.62  ? 36   ASN   A CG  1 
ATOM   298  O  OD1 . ASN   A  1 61  ? -29.793 -34.235 13.034 1.00 59.20  ? 36   ASN   A OD1 1 
ATOM   299  N  ND2 . ASN   A  1 61  ? -29.694 -33.832 10.828 1.00 56.85  ? 36   ASN   A ND2 1 
ATOM   300  N  N   . LEU   A  1 62  ? -29.232 -29.151 14.040 1.00 40.92  ? 37   LEU   A N   1 
ATOM   301  C  CA  . LEU   A  1 62  ? -28.621 -27.872 14.366 1.00 43.31  ? 37   LEU   A CA  1 
ATOM   302  C  C   . LEU   A  1 62  ? -28.942 -27.428 15.784 1.00 45.93  ? 37   LEU   A C   1 
ATOM   303  O  O   . LEU   A  1 62  ? -28.484 -26.364 16.207 1.00 35.65  ? 37   LEU   A O   1 
ATOM   304  C  CB  . LEU   A  1 62  ? -29.055 -26.791 13.370 1.00 37.61  ? 37   LEU   A CB  1 
ATOM   305  C  CG  . LEU   A  1 62  ? -28.511 -26.925 11.946 1.00 43.46  ? 37   LEU   A CG  1 
ATOM   306  C  CD1 . LEU   A  1 62  ? -29.211 -25.957 11.008 1.00 35.86  ? 37   LEU   A CD1 1 
ATOM   307  C  CD2 . LEU   A  1 62  ? -27.007 -26.691 11.933 1.00 38.84  ? 37   LEU   A CD2 1 
ATOM   308  N  N   . GLN   A  1 63  ? -29.708 -28.223 16.530 1.00 44.75  ? 38   GLN   A N   1 
ATOM   309  C  CA  . GLN   A  1 63  ? -30.147 -27.853 17.874 1.00 46.71  ? 38   GLN   A CA  1 
ATOM   310  C  C   . GLN   A  1 63  ? -29.148 -28.447 18.857 1.00 42.79  ? 38   GLN   A C   1 
ATOM   311  O  O   . GLN   A  1 63  ? -29.289 -29.576 19.328 1.00 50.38  ? 38   GLN   A O   1 
ATOM   312  C  CB  . GLN   A  1 63  ? -31.570 -28.324 18.143 1.00 44.24  ? 38   GLN   A CB  1 
ATOM   313  C  CG  . GLN   A  1 63  ? -32.618 -27.660 17.264 1.00 48.34  ? 38   GLN   A CG  1 
ATOM   314  C  CD  . GLN   A  1 63  ? -33.962 -28.358 17.322 1.00 52.13  ? 38   GLN   A CD  1 
ATOM   315  O  OE1 . GLN   A  1 63  ? -34.152 -29.303 18.087 1.00 55.82  ? 38   GLN   A OE1 1 
ATOM   316  N  NE2 . GLN   A  1 63  ? -34.906 -27.888 16.517 1.00 50.37  ? 38   GLN   A NE2 1 
ATOM   317  N  N   . ASN   A  1 64  ? -28.116 -27.660 19.154 1.00 45.21  ? 39   ASN   A N   1 
ATOM   318  C  CA  . ASN   A  1 64  ? -27.092 -27.989 20.132 1.00 47.14  ? 39   ASN   A CA  1 
ATOM   319  C  C   . ASN   A  1 64  ? -26.738 -26.711 20.878 1.00 41.90  ? 39   ASN   A C   1 
ATOM   320  O  O   . ASN   A  1 64  ? -27.162 -25.616 20.500 1.00 37.18  ? 39   ASN   A O   1 
ATOM   321  C  CB  . ASN   A  1 64  ? -25.858 -28.597 19.455 1.00 40.25  ? 39   ASN   A CB  1 
ATOM   322  C  CG  . ASN   A  1 64  ? -25.394 -27.784 18.258 1.00 52.70  ? 39   ASN   A CG  1 
ATOM   323  O  OD1 . ASN   A  1 64  ? -24.966 -26.638 18.399 1.00 48.62  ? 39   ASN   A OD1 1 
ATOM   324  N  ND2 . ASN   A  1 64  ? -25.487 -28.371 17.070 1.00 43.41  ? 39   ASN   A ND2 1 
ATOM   325  N  N   . VAL   A  1 65  ? -25.968 -26.852 21.960 1.00 42.13  ? 40   VAL   A N   1 
ATOM   326  C  CA  . VAL   A  1 65  ? -25.687 -25.696 22.810 1.00 45.16  ? 40   VAL   A CA  1 
ATOM   327  C  C   . VAL   A  1 65  ? -24.951 -24.614 22.030 1.00 39.40  ? 40   VAL   A C   1 
ATOM   328  O  O   . VAL   A  1 65  ? -25.253 -23.421 22.167 1.00 40.18  ? 40   VAL   A O   1 
ATOM   329  C  CB  . VAL   A  1 65  ? -24.901 -26.125 24.063 1.00 47.34  ? 40   VAL   A CB  1 
ATOM   330  C  CG1 . VAL   A  1 65  ? -24.310 -24.902 24.742 1.00 42.02  ? 40   VAL   A CG1 1 
ATOM   331  C  CG2 . VAL   A  1 65  ? -25.804 -26.885 25.014 1.00 38.56  ? 40   VAL   A CG2 1 
ATOM   332  N  N   . THR   A  1 66  ? -23.965 -25.008 21.215 1.00 34.01  ? 41   THR   A N   1 
ATOM   333  C  CA  . THR   A  1 66  ? -23.211 -24.038 20.421 1.00 42.07  ? 41   THR   A CA  1 
ATOM   334  C  C   . THR   A  1 66  ? -24.133 -23.146 19.606 1.00 41.37  ? 41   THR   A C   1 
ATOM   335  O  O   . THR   A  1 66  ? -23.942 -21.927 19.549 1.00 41.31  ? 41   THR   A O   1 
ATOM   336  C  CB  . THR   A  1 66  ? -22.211 -24.737 19.499 1.00 37.28  ? 41   THR   A CB  1 
ATOM   337  O  OG1 . THR   A  1 66  ? -21.740 -25.931 20.127 1.00 47.98  ? 41   THR   A OG1 1 
ATOM   338  C  CG2 . THR   A  1 66  ? -21.027 -23.833 19.209 1.00 39.95  ? 41   THR   A CG2 1 
ATOM   339  N  N   . ASN   A  1 67  ? -25.150 -23.736 18.982 1.00 35.49  ? 42   ASN   A N   1 
ATOM   340  C  CA  . ASN   A  1 67  ? -26.036 -22.978 18.113 1.00 32.65  ? 42   ASN   A CA  1 
ATOM   341  C  C   . ASN   A  1 67  ? -27.073 -22.167 18.876 1.00 27.23  ? 42   ASN   A C   1 
ATOM   342  O  O   . ASN   A  1 67  ? -27.669 -21.259 18.290 1.00 34.62  ? 42   ASN   A O   1 
ATOM   343  C  CB  . ASN   A  1 67  ? -26.738 -23.913 17.130 1.00 27.66  ? 42   ASN   A CB  1 
ATOM   344  C  CG  . ASN   A  1 67  ? -25.826 -24.360 16.006 1.00 38.13  ? 42   ASN   A CG  1 
ATOM   345  O  OD1 . ASN   A  1 67  ? -24.750 -23.795 15.805 1.00 35.08  ? 42   ASN   A OD1 1 
ATOM   346  N  ND2 . ASN   A  1 67  ? -26.259 -25.365 15.253 1.00 35.39  ? 42   ASN   A ND2 1 
ATOM   347  N  N   . TYR   A  1 68  ? -27.306 -22.456 20.158 1.00 27.65  ? 43   TYR   A N   1 
ATOM   348  C  CA  . TYR   A  1 68  ? -28.136 -21.548 20.942 1.00 34.65  ? 43   TYR   A CA  1 
ATOM   349  C  C   . TYR   A  1 68  ? -27.451 -20.200 21.123 1.00 30.21  ? 43   TYR   A C   1 
ATOM   350  O  O   . TYR   A  1 68  ? -28.113 -19.155 21.103 1.00 26.42  ? 43   TYR   A O   1 
ATOM   351  C  CB  . TYR   A  1 68  ? -28.477 -22.170 22.297 1.00 30.75  ? 43   TYR   A CB  1 
ATOM   352  C  CG  . TYR   A  1 68  ? -29.159 -23.516 22.192 1.00 49.80  ? 43   TYR   A CG  1 
ATOM   353  C  CD1 . TYR   A  1 68  ? -29.945 -23.831 21.089 1.00 47.85  ? 43   TYR   A CD1 1 
ATOM   354  C  CD2 . TYR   A  1 68  ? -29.027 -24.467 23.195 1.00 45.41  ? 43   TYR   A CD2 1 
ATOM   355  C  CE1 . TYR   A  1 68  ? -30.574 -25.055 20.985 1.00 56.11  ? 43   TYR   A CE1 1 
ATOM   356  C  CE2 . TYR   A  1 68  ? -29.653 -25.696 23.099 1.00 49.79  ? 43   TYR   A CE2 1 
ATOM   357  C  CZ  . TYR   A  1 68  ? -30.426 -25.983 21.991 1.00 57.61  ? 43   TYR   A CZ  1 
ATOM   358  O  OH  . TYR   A  1 68  ? -31.054 -27.203 21.887 1.00 64.87  ? 43   TYR   A OH  1 
ATOM   359  N  N   . PHE   A  1 69  ? -26.128 -20.197 21.295 1.00 25.64  ? 44   PHE   A N   1 
ATOM   360  C  CA  . PHE   A  1 69  ? -25.402 -18.931 21.314 1.00 27.72  ? 44   PHE   A CA  1 
ATOM   361  C  C   . PHE   A  1 69  ? -25.387 -18.289 19.932 1.00 26.46  ? 44   PHE   A C   1 
ATOM   362  O  O   . PHE   A  1 69  ? -25.447 -17.060 19.812 1.00 27.55  ? 44   PHE   A O   1 
ATOM   363  C  CB  . PHE   A  1 69  ? -23.981 -19.140 21.836 1.00 27.82  ? 44   PHE   A CB  1 
ATOM   364  C  CG  . PHE   A  1 69  ? -23.922 -19.545 23.284 1.00 30.71  ? 44   PHE   A CG  1 
ATOM   365  C  CD1 . PHE   A  1 69  ? -24.225 -18.635 24.284 1.00 34.31  ? 44   PHE   A CD1 1 
ATOM   366  C  CD2 . PHE   A  1 69  ? -23.569 -20.835 23.643 1.00 33.84  ? 44   PHE   A CD2 1 
ATOM   367  C  CE1 . PHE   A  1 69  ? -24.175 -19.005 25.618 1.00 36.03  ? 44   PHE   A CE1 1 
ATOM   368  C  CE2 . PHE   A  1 69  ? -23.517 -21.210 24.974 1.00 34.10  ? 44   PHE   A CE2 1 
ATOM   369  C  CZ  . PHE   A  1 69  ? -23.820 -20.294 25.962 1.00 35.90  ? 44   PHE   A CZ  1 
ATOM   370  N  N   . VAL   A  1 70  ? -25.306 -19.107 18.878 1.00 27.02  ? 45   VAL   A N   1 
ATOM   371  C  CA  . VAL   A  1 70  ? -25.432 -18.597 17.514 1.00 27.59  ? 45   VAL   A CA  1 
ATOM   372  C  C   . VAL   A  1 70  ? -26.778 -17.912 17.317 1.00 28.54  ? 45   VAL   A C   1 
ATOM   373  O  O   . VAL   A  1 70  ? -26.866 -16.857 16.675 1.00 26.32  ? 45   VAL   A O   1 
ATOM   374  C  CB  . VAL   A  1 70  ? -25.221 -19.737 16.498 1.00 28.18  ? 45   VAL   A CB  1 
ATOM   375  C  CG1 . VAL   A  1 70  ? -25.694 -19.319 15.110 1.00 24.81  ? 45   VAL   A CG1 1 
ATOM   376  C  CG2 . VAL   A  1 70  ? -23.757 -20.149 16.460 1.00 27.38  ? 45   VAL   A CG2 1 
ATOM   377  N  N   . VAL   A  1 71  ? -27.843 -18.485 17.883 1.00 23.95  ? 46   VAL   A N   1 
ATOM   378  C  CA  . VAL   A  1 71  ? -29.163 -17.870 17.775 1.00 22.66  ? 46   VAL   A CA  1 
ATOM   379  C  C   . VAL   A  1 71  ? -29.229 -16.581 18.587 1.00 26.23  ? 46   VAL   A C   1 
ATOM   380  O  O   . VAL   A  1 71  ? -29.775 -15.571 18.126 1.00 25.51  ? 46   VAL   A O   1 
ATOM   381  C  CB  . VAL   A  1 71  ? -30.251 -18.870 18.205 1.00 33.42  ? 46   VAL   A CB  1 
ATOM   382  C  CG1 . VAL   A  1 71  ? -31.574 -18.157 18.418 1.00 27.81  ? 46   VAL   A CG1 1 
ATOM   383  C  CG2 . VAL   A  1 71  ? -30.400 -19.967 17.158 1.00 29.91  ? 46   VAL   A CG2 1 
ATOM   384  N  N   . SER   A  1 72  ? -28.685 -16.593 19.807 1.00 24.17  ? 47   SER   A N   1 
ATOM   385  C  CA  . SER   A  1 72  ? -28.609 -15.359 20.585 1.00 28.67  ? 47   SER   A CA  1 
ATOM   386  C  C   . SER   A  1 72  ? -27.849 -14.284 19.820 1.00 25.76  ? 47   SER   A C   1 
ATOM   387  O  O   . SER   A  1 72  ? -28.219 -13.104 19.850 1.00 24.37  ? 47   SER   A O   1 
ATOM   388  C  CB  . SER   A  1 72  ? -27.946 -15.628 21.937 1.00 26.18  ? 47   SER   A CB  1 
ATOM   389  O  OG  . SER   A  1 72  ? -27.918 -14.455 22.735 1.00 28.08  ? 47   SER   A OG  1 
ATOM   390  N  N   . LEU   A  1 73  ? -26.795 -14.683 19.110 1.00 22.23  ? 48   LEU   A N   1 
ATOM   391  C  CA  . LEU   A  1 73  ? -26.031 -13.739 18.306 1.00 27.35  ? 48   LEU   A CA  1 
ATOM   392  C  C   . LEU   A  1 73  ? -26.848 -13.235 17.119 1.00 23.89  ? 48   LEU   A C   1 
ATOM   393  O  O   . LEU   A  1 73  ? -26.816 -12.041 16.797 1.00 22.96  ? 48   LEU   A O   1 
ATOM   394  C  CB  . LEU   A  1 73  ? -24.739 -14.414 17.841 1.00 27.03  ? 48   LEU   A CB  1 
ATOM   395  C  CG  . LEU   A  1 73  ? -23.700 -13.643 17.034 1.00 36.16  ? 48   LEU   A CG  1 
ATOM   396  C  CD1 . LEU   A  1 73  ? -23.220 -12.435 17.817 1.00 25.77  ? 48   LEU   A CD1 1 
ATOM   397  C  CD2 . LEU   A  1 73  ? -22.531 -14.560 16.703 1.00 29.32  ? 48   LEU   A CD2 1 
ATOM   398  N  N   . ALA   A  1 74  ? -27.608 -14.124 16.473 1.00 24.13  ? 49   ALA   A N   1 
ATOM   399  C  CA  . ALA   A  1 74  ? -28.489 -13.699 15.387 1.00 23.81  ? 49   ALA   A CA  1 
ATOM   400  C  C   . ALA   A  1 74  ? -29.623 -12.804 15.873 1.00 24.52  ? 49   ALA   A C   1 
ATOM   401  O  O   . ALA   A  1 74  ? -30.039 -11.891 15.149 1.00 23.83  ? 49   ALA   A O   1 
ATOM   402  C  CB  . ALA   A  1 74  ? -29.054 -14.924 14.666 1.00 26.27  ? 49   ALA   A CB  1 
ATOM   403  N  N   . ALA   A  1 75  ? -30.139 -13.046 17.081 1.00 22.91  ? 50   ALA   A N   1 
ATOM   404  C  CA  . ALA   A  1 75  ? -31.172 -12.174 17.634 1.00 24.55  ? 50   ALA   A CA  1 
ATOM   405  C  C   . ALA   A  1 75  ? -30.650 -10.758 17.841 1.00 26.09  ? 50   ALA   A C   1 
ATOM   406  O  O   . ALA   A  1 75  ? -31.353 -9.781  17.558 1.00 22.58  ? 50   ALA   A O   1 
ATOM   407  C  CB  . ALA   A  1 75  ? -31.697 -12.749 18.950 1.00 29.37  ? 50   ALA   A CB  1 
ATOM   408  N  N   . ALA   A  1 76  ? -29.420 -10.630 18.345 1.00 24.56  ? 51   ALA   A N   1 
ATOM   409  C  CA  . ALA   A  1 76  ? -28.807 -9.313  18.480 1.00 27.17  ? 51   ALA   A CA  1 
ATOM   410  C  C   . ALA   A  1 76  ? -28.701 -8.616  17.131 1.00 20.44  ? 51   ALA   A C   1 
ATOM   411  O  O   . ALA   A  1 76  ? -28.940 -7.406  17.028 1.00 26.43  ? 51   ALA   A O   1 
ATOM   412  C  CB  . ALA   A  1 76  ? -27.430 -9.437  19.130 1.00 22.14  ? 51   ALA   A CB  1 
ATOM   413  N  N   . ASP   A  1 77  ? -28.353 -9.364  16.081 1.00 21.44  ? 52   ASP   A N   1 
ATOM   414  C  CA  . ASP   A  1 77  ? -28.188 -8.753  14.768 1.00 22.58  ? 52   ASP   A CA  1 
ATOM   415  C  C   . ASP   A  1 77  ? -29.531 -8.379  14.157 1.00 20.01  ? 52   ASP   A C   1 
ATOM   416  O  O   . ASP   A  1 77  ? -29.630 -7.365  13.456 1.00 22.92  ? 52   ASP   A O   1 
ATOM   417  C  CB  . ASP   A  1 77  ? -27.432 -9.706  13.842 1.00 21.98  ? 52   ASP   A CB  1 
ATOM   418  C  CG  . ASP   A  1 77  ? -25.967 -9.830  14.208 1.00 29.56  ? 52   ASP   A CG  1 
ATOM   419  O  OD1 . ASP   A  1 77  ? -25.402 -8.849  14.735 1.00 31.54  ? 52   ASP   A OD1 1 
ATOM   420  O  OD2 . ASP   A  1 77  ? -25.382 -10.909 13.969 1.00 37.31  ? 52   ASP   A OD2 1 
ATOM   421  N  N   . ILE   A  1 78  ? -30.575 -9.169  14.423 1.00 28.17  ? 53   ILE   A N   1 
ATOM   422  C  CA  . ILE   A  1 78  ? -31.923 -8.786  14.012 1.00 25.80  ? 53   ILE   A CA  1 
ATOM   423  C  C   . ILE   A  1 78  ? -32.315 -7.461  14.654 1.00 24.27  ? 53   ILE   A C   1 
ATOM   424  O  O   . ILE   A  1 78  ? -32.904 -6.587  14.004 1.00 24.25  ? 53   ILE   A O   1 
ATOM   425  C  CB  . ILE   A  1 78  ? -32.925 -9.909  14.345 1.00 26.12  ? 53   ILE   A CB  1 
ATOM   426  C  CG1 . ILE   A  1 78  ? -32.674 -11.126 13.449 1.00 28.32  ? 53   ILE   A CG1 1 
ATOM   427  C  CG2 . ILE   A  1 78  ? -34.360 -9.420  14.203 1.00 28.56  ? 53   ILE   A CG2 1 
ATOM   428  C  CD1 . ILE   A  1 78  ? -33.432 -12.374 13.865 1.00 30.62  ? 53   ILE   A CD1 1 
ATOM   429  N  N   . LEU   A  1 79  ? -31.989 -7.284  15.938 1.00 23.16  ? 54   LEU   A N   1 
ATOM   430  C  CA  . LEU   A  1 79  ? -32.326 -6.043  16.625 1.00 22.92  ? 54   LEU   A CA  1 
ATOM   431  C  C   . LEU   A  1 79  ? -31.461 -4.868  16.183 1.00 21.03  ? 54   LEU   A C   1 
ATOM   432  O  O   . LEU   A  1 79  ? -31.889 -3.717  16.324 1.00 25.01  ? 54   LEU   A O   1 
ATOM   433  C  CB  . LEU   A  1 79  ? -32.202 -6.229  18.139 1.00 24.76  ? 54   LEU   A CB  1 
ATOM   434  C  CG  . LEU   A  1 79  ? -33.175 -7.220  18.776 1.00 31.67  ? 54   LEU   A CG  1 
ATOM   435  C  CD1 . LEU   A  1 79  ? -32.829 -7.455  20.238 1.00 32.87  ? 54   LEU   A CD1 1 
ATOM   436  C  CD2 . LEU   A  1 79  ? -34.602 -6.707  18.634 1.00 29.65  ? 54   LEU   A CD2 1 
ATOM   437  N  N   . VAL   A  1 80  ? -30.261 -5.120  15.653 1.00 22.35  ? 55   VAL   A N   1 
ATOM   438  C  CA  . VAL   A  1 80  ? -29.513 -4.047  15.000 1.00 21.18  ? 55   VAL   A CA  1 
ATOM   439  C  C   . VAL   A  1 80  ? -30.297 -3.504  13.813 1.00 21.94  ? 55   VAL   A C   1 
ATOM   440  O  O   . VAL   A  1 80  ? -30.390 -2.288  13.611 1.00 23.60  ? 55   VAL   A O   1 
ATOM   441  C  CB  . VAL   A  1 80  ? -28.116 -4.544  14.580 1.00 26.46  ? 55   VAL   A CB  1 
ATOM   442  C  CG1 . VAL   A  1 80  ? -27.459 -3.557  13.625 1.00 19.44  ? 55   VAL   A CG1 1 
ATOM   443  C  CG2 . VAL   A  1 80  ? -27.233 -4.751  15.805 1.00 19.27  ? 55   VAL   A CG2 1 
ATOM   444  N  N   . GLY   A  1 81  ? -30.898 -4.397  13.027 1.00 23.20  ? 56   GLY   A N   1 
ATOM   445  C  CA  . GLY   A  1 81  ? -31.669 -3.954  11.879 1.00 25.56  ? 56   GLY   A CA  1 
ATOM   446  C  C   . GLY   A  1 81  ? -32.974 -3.288  12.267 1.00 22.32  ? 56   GLY   A C   1 
ATOM   447  O  O   . GLY   A  1 81  ? -33.350 -2.257  11.702 1.00 25.31  ? 56   GLY   A O   1 
ATOM   448  N  N   . VAL   A  1 82  ? -33.680 -3.862  13.241 1.00 24.70  ? 57   VAL   A N   1 
ATOM   449  C  CA  . VAL   A  1 82  ? -35.005 -3.369  13.604 1.00 24.61  ? 57   VAL   A CA  1 
ATOM   450  C  C   . VAL   A  1 82  ? -34.923 -2.111  14.467 1.00 27.29  ? 57   VAL   A C   1 
ATOM   451  O  O   . VAL   A  1 82  ? -35.746 -1.198  14.327 1.00 23.70  ? 57   VAL   A O   1 
ATOM   452  C  CB  . VAL   A  1 82  ? -35.794 -4.496  14.299 1.00 30.86  ? 57   VAL   A CB  1 
ATOM   453  C  CG1 . VAL   A  1 82  ? -37.043 -3.958  14.972 1.00 35.69  ? 57   VAL   A CG1 1 
ATOM   454  C  CG2 . VAL   A  1 82  ? -36.147 -5.585  13.295 1.00 30.86  ? 57   VAL   A CG2 1 
ATOM   455  N  N   . LEU   A  1 83  ? -33.944 -2.028  15.370 1.00 23.62  ? 58   LEU   A N   1 
ATOM   456  C  CA  . LEU   A  1 83  ? -33.899 -0.926  16.327 1.00 26.00  ? 58   LEU   A CA  1 
ATOM   457  C  C   . LEU   A  1 83  ? -32.633 -0.088  16.248 1.00 21.37  ? 58   LEU   A C   1 
ATOM   458  O  O   . LEU   A  1 83  ? -32.721 1.145   16.179 1.00 21.73  ? 58   LEU   A O   1 
ATOM   459  C  CB  . LEU   A  1 83  ? -34.071 -1.461  17.759 1.00 28.14  ? 58   LEU   A CB  1 
ATOM   460  C  CG  . LEU   A  1 83  ? -35.448 -2.023  18.110 1.00 28.26  ? 58   LEU   A CG  1 
ATOM   461  C  CD1 . LEU   A  1 83  ? -35.449 -2.586  19.523 1.00 28.58  ? 58   LEU   A CD1 1 
ATOM   462  C  CD2 . LEU   A  1 83  ? -36.492 -0.934  17.964 1.00 23.66  ? 58   LEU   A CD2 1 
ATOM   463  N  N   . ALA   A  1 84  ? -31.450 -0.708  16.266 1.00 21.18  ? 59   ALA   A N   1 
ATOM   464  C  CA  . ALA   A  1 84  ? -30.229 0.086   16.376 1.00 24.13  ? 59   ALA   A CA  1 
ATOM   465  C  C   . ALA   A  1 84  ? -30.003 0.946   15.138 1.00 20.48  ? 59   ALA   A C   1 
ATOM   466  O  O   . ALA   A  1 84  ? -29.530 2.084   15.246 1.00 21.67  ? 59   ALA   A O   1 
ATOM   467  C  CB  . ALA   A  1 84  ? -29.026 -0.824  16.621 1.00 21.90  ? 59   ALA   A CB  1 
ATOM   468  N  N   . ILE   A  1 85  ? -30.332 0.431   13.958 1.00 18.73  ? 60   ILE   A N   1 
ATOM   469  C  CA  . ILE   A  1 85  ? -30.089 1.191   12.733 1.00 21.32  ? 60   ILE   A CA  1 
ATOM   470  C  C   . ILE   A  1 85  ? -31.114 2.320   12.638 1.00 19.23  ? 60   ILE   A C   1 
ATOM   471  O  O   . ILE   A  1 85  ? -30.729 3.463   12.347 1.00 21.51  ? 60   ILE   A O   1 
ATOM   472  C  CB  . ILE   A  1 85  ? -30.076 0.277   11.495 1.00 23.03  ? 60   ILE   A CB  1 
ATOM   473  C  CG1 . ILE   A  1 85  ? -28.756 -0.503  11.454 1.00 22.74  ? 60   ILE   A CG1 1 
ATOM   474  C  CG2 . ILE   A  1 85  ? -30.276 1.090   10.221 1.00 21.24  ? 60   ILE   A CG2 1 
ATOM   475  C  CD1 . ILE   A  1 85  ? -28.643 -1.496  10.317 1.00 25.13  ? 60   ILE   A CD1 1 
ATOM   476  N  N   . PRO   A  1 86  ? -32.413 2.076   12.873 1.00 21.51  ? 61   PRO   A N   1 
ATOM   477  C  CA  . PRO   A  1 86  ? -33.339 3.214   12.997 1.00 22.98  ? 61   PRO   A CA  1 
ATOM   478  C  C   . PRO   A  1 86  ? -32.903 4.224   14.048 1.00 28.71  ? 61   PRO   A C   1 
ATOM   479  O  O   . PRO   A  1 86  ? -33.070 5.431   13.842 1.00 23.80  ? 61   PRO   A O   1 
ATOM   480  C  CB  . PRO   A  1 86  ? -34.665 2.537   13.358 1.00 21.41  ? 61   PRO   A CB  1 
ATOM   481  C  CG  . PRO   A  1 86  ? -34.593 1.238   12.653 1.00 24.22  ? 61   PRO   A CG  1 
ATOM   482  C  CD  . PRO   A  1 86  ? -33.156 0.799   12.812 1.00 25.11  ? 61   PRO   A CD  1 
ATOM   483  N  N   . PHE   A  1 87  ? -32.359 3.762   15.180 1.00 22.28  ? 62   PHE   A N   1 
ATOM   484  C  CA  . PHE   A  1 87  ? -31.874 4.699   16.188 1.00 21.66  ? 62   PHE   A CA  1 
ATOM   485  C  C   . PHE   A  1 87  ? -30.688 5.502   15.665 1.00 22.74  ? 62   PHE   A C   1 
ATOM   486  O  O   . PHE   A  1 87  ? -30.583 6.706   15.927 1.00 24.90  ? 62   PHE   A O   1 
ATOM   487  C  CB  . PHE   A  1 87  ? -31.469 3.959   17.469 1.00 18.77  ? 62   PHE   A CB  1 
ATOM   488  C  CG  . PHE   A  1 87  ? -32.624 3.392   18.261 1.00 23.82  ? 62   PHE   A CG  1 
ATOM   489  C  CD1 . PHE   A  1 87  ? -33.939 3.590   17.867 1.00 24.70  ? 62   PHE   A CD1 1 
ATOM   490  C  CD2 . PHE   A  1 87  ? -32.380 2.681   19.427 1.00 19.66  ? 62   PHE   A CD2 1 
ATOM   491  C  CE1 . PHE   A  1 87  ? -34.989 3.068   18.612 1.00 26.82  ? 62   PHE   A CE1 1 
ATOM   492  C  CE2 . PHE   A  1 87  ? -33.422 2.161   20.178 1.00 30.41  ? 62   PHE   A CE2 1 
ATOM   493  C  CZ  . PHE   A  1 87  ? -34.729 2.354   19.770 1.00 24.01  ? 62   PHE   A CZ  1 
ATOM   494  N  N   . ALA   A  1 88  ? -29.778 4.846   14.936 1.00 23.77  ? 63   ALA   A N   1 
ATOM   495  C  CA  . ALA   A  1 88  ? -28.614 5.538   14.386 1.00 22.51  ? 63   ALA   A CA  1 
ATOM   496  C  C   . ALA   A  1 88  ? -29.015 6.582   13.350 1.00 23.66  ? 63   ALA   A C   1 
ATOM   497  O  O   . ALA   A  1 88  ? -28.463 7.688   13.329 1.00 22.01  ? 63   ALA   A O   1 
ATOM   498  C  CB  . ALA   A  1 88  ? -27.644 4.527   13.775 1.00 20.33  ? 63   ALA   A CB  1 
ATOM   499  N  N   . ILE   A  1 89  ? -29.971 6.247   12.481 1.00 24.90  ? 64   ILE   A N   1 
ATOM   500  C  CA  . ILE   A  1 89  ? -30.496 7.222   11.528 1.00 21.77  ? 64   ILE   A CA  1 
ATOM   501  C  C   . ILE   A  1 89  ? -31.072 8.421   12.269 1.00 29.74  ? 64   ILE   A C   1 
ATOM   502  O  O   . ILE   A  1 89  ? -30.814 9.579   11.918 1.00 26.09  ? 64   ILE   A O   1 
ATOM   503  C  CB  . ILE   A  1 89  ? -31.541 6.559   10.610 1.00 22.79  ? 64   ILE   A CB  1 
ATOM   504  C  CG1 . ILE   A  1 89  ? -30.865 5.533   9.696  1.00 23.44  ? 64   ILE   A CG1 1 
ATOM   505  C  CG2 . ILE   A  1 89  ? -32.290 7.605   9.795  1.00 24.61  ? 64   ILE   A CG2 1 
ATOM   506  C  CD1 . ILE   A  1 89  ? -31.836 4.637   8.952  1.00 25.08  ? 64   ILE   A CD1 1 
ATOM   507  N  N   . THR   A  1 90  ? -31.868 8.155   13.305 1.00 23.67  ? 65   THR   A N   1 
ATOM   508  C  CA  . THR   A  1 90  ? -32.495 9.227   14.069 1.00 24.00  ? 65   THR   A CA  1 
ATOM   509  C  C   . THR   A  1 90  ? -31.453 10.148  14.696 1.00 24.82  ? 65   THR   A C   1 
ATOM   510  O  O   . THR   A  1 90  ? -31.552 11.377  14.597 1.00 25.51  ? 65   THR   A O   1 
ATOM   511  C  CB  . THR   A  1 90  ? -33.403 8.626   15.143 1.00 24.32  ? 65   THR   A CB  1 
ATOM   512  O  OG1 . THR   A  1 90  ? -34.359 7.758   14.523 1.00 31.99  ? 65   THR   A OG1 1 
ATOM   513  C  CG2 . THR   A  1 90  ? -34.138 9.715   15.892 1.00 26.72  ? 65   THR   A CG2 1 
ATOM   514  N  N   . ILE   A  1 91  ? -30.436 9.571   15.343 1.00 26.44  ? 66   ILE   A N   1 
ATOM   515  C  CA  . ILE   A  1 91  ? -29.471 10.397  16.058 1.00 21.27  ? 66   ILE   A CA  1 
ATOM   516  C  C   . ILE   A  1 91  ? -28.565 11.168  15.106 1.00 28.43  ? 66   ILE   A C   1 
ATOM   517  O  O   . ILE   A  1 91  ? -27.961 12.169  15.509 1.00 30.24  ? 66   ILE   A O   1 
ATOM   518  C  CB  . ILE   A  1 91  ? -28.641 9.546   17.041 1.00 29.75  ? 66   ILE   A CB  1 
ATOM   519  C  CG1 . ILE   A  1 91  ? -28.018 10.444  18.112 1.00 32.35  ? 66   ILE   A CG1 1 
ATOM   520  C  CG2 . ILE   A  1 91  ? -27.569 8.754   16.306 1.00 27.87  ? 66   ILE   A CG2 1 
ATOM   521  C  CD1 . ILE   A  1 91  ? -27.607 9.715   19.365 1.00 37.81  ? 66   ILE   A CD1 1 
ATOM   522  N  N   . SER   A  1 92  ? -28.469 10.746  13.843 1.00 26.55  ? 67   SER   A N   1 
ATOM   523  C  CA  . SER   A  1 92  ? -27.663 11.487  12.879 1.00 26.26  ? 67   SER   A CA  1 
ATOM   524  C  C   . SER   A  1 92  ? -28.280 12.832  12.512 1.00 27.95  ? 67   SER   A C   1 
ATOM   525  O  O   . SER   A  1 92  ? -27.572 13.699  11.989 1.00 29.16  ? 67   SER   A O   1 
ATOM   526  C  CB  . SER   A  1 92  ? -27.449 10.647  11.617 1.00 26.69  ? 67   SER   A CB  1 
ATOM   527  O  OG  . SER   A  1 92  ? -28.602 10.649  10.793 1.00 26.37  ? 67   SER   A OG  1 
ATOM   528  N  N   . THR   A  1 93  ? -29.573 13.031  12.774 1.00 26.34  ? 68   THR   A N   1 
ATOM   529  C  CA  . THR   A  1 93  ? -30.231 14.282  12.414 1.00 29.02  ? 68   THR   A CA  1 
ATOM   530  C  C   . THR   A  1 93  ? -30.040 15.382  13.452 1.00 30.63  ? 68   THR   A C   1 
ATOM   531  O  O   . THR   A  1 93  ? -30.291 16.552  13.141 1.00 32.09  ? 68   THR   A O   1 
ATOM   532  C  CB  . THR   A  1 93  ? -31.729 14.055  12.196 1.00 33.34  ? 68   THR   A CB  1 
ATOM   533  O  OG1 . THR   A  1 93  ? -32.366 13.803  13.456 1.00 27.35  ? 68   THR   A OG1 1 
ATOM   534  C  CG2 . THR   A  1 93  ? -31.963 12.876  11.266 1.00 27.24  ? 68   THR   A CG2 1 
ATOM   535  N  N   . GLY   A  1 94  ? -29.594 15.049  14.661 1.00 28.57  ? 69   GLY   A N   1 
ATOM   536  C  CA  . GLY   A  1 94  ? -29.469 16.052  15.700 1.00 27.91  ? 69   GLY   A CA  1 
ATOM   537  C  C   . GLY   A  1 94  ? -30.777 16.623  16.197 1.00 32.50  ? 69   GLY   A C   1 
ATOM   538  O  O   . GLY   A  1 94  ? -30.797 17.747  16.704 1.00 36.39  ? 69   GLY   A O   1 
ATOM   539  N  N   . PHE   A  1 95  ? -31.875 15.884  16.055 1.00 26.38  ? 70   PHE   A N   1 
ATOM   540  C  CA  . PHE   A  1 95  ? -33.193 16.401  16.396 1.00 34.66  ? 70   PHE   A CA  1 
ATOM   541  C  C   . PHE   A  1 95  ? -33.281 16.727  17.886 1.00 36.83  ? 70   PHE   A C   1 
ATOM   542  O  O   . PHE   A  1 95  ? -32.557 16.173  18.719 1.00 29.47  ? 70   PHE   A O   1 
ATOM   543  C  CB  . PHE   A  1 95  ? -34.275 15.382  16.033 1.00 29.82  ? 70   PHE   A CB  1 
ATOM   544  C  CG  . PHE   A  1 95  ? -34.376 14.237  17.005 1.00 30.34  ? 70   PHE   A CG  1 
ATOM   545  C  CD1 . PHE   A  1 95  ? -33.340 13.324  17.137 1.00 28.92  ? 70   PHE   A CD1 1 
ATOM   546  C  CD2 . PHE   A  1 95  ? -35.507 14.075  17.789 1.00 32.26  ? 70   PHE   A CD2 1 
ATOM   547  C  CE1 . PHE   A  1 95  ? -33.428 12.278  18.037 1.00 30.55  ? 70   PHE   A CE1 1 
ATOM   548  C  CE2 . PHE   A  1 95  ? -35.604 13.027  18.688 1.00 32.54  ? 70   PHE   A CE2 1 
ATOM   549  C  CZ  . PHE   A  1 95  ? -34.564 12.126  18.811 1.00 27.10  ? 70   PHE   A CZ  1 
ATOM   550  N  N   . CYS   A  1 96  ? -34.188 17.644  18.217 1.00 31.32  ? 71   CYS   A N   1 
ATOM   551  C  CA  . CYS   A  1 96  ? -34.379 18.048  19.605 1.00 31.36  ? 71   CYS   A CA  1 
ATOM   552  C  C   . CYS   A  1 96  ? -35.010 16.910  20.399 1.00 35.95  ? 71   CYS   A C   1 
ATOM   553  O  O   . CYS   A  1 96  ? -36.000 16.312  19.967 1.00 32.86  ? 71   CYS   A O   1 
ATOM   554  C  CB  . CYS   A  1 96  ? -35.260 19.295  19.683 1.00 34.04  ? 71   CYS   A CB  1 
ATOM   555  S  SG  . CYS   A  1 96  ? -34.519 20.792  18.999 1.00 38.51  ? 71   CYS   A SG  1 
ATOM   556  N  N   . ALA   A  1 97  ? -34.430 16.599  21.555 1.00 26.24  ? 72   ALA   A N   1 
ATOM   557  C  CA  . ALA   A  1 97  ? -34.901 15.478  22.353 1.00 28.75  ? 72   ALA   A CA  1 
ATOM   558  C  C   . ALA   A  1 97  ? -34.550 15.715  23.812 1.00 28.58  ? 72   ALA   A C   1 
ATOM   559  O  O   . ALA   A  1 97  ? -33.534 16.342  24.125 1.00 30.72  ? 72   ALA   A O   1 
ATOM   560  C  CB  . ALA   A  1 97  ? -34.295 14.153  21.874 1.00 29.58  ? 72   ALA   A CB  1 
ATOM   561  N  N   . ALA   A  1 98  ? -35.404 15.216  24.705 1.00 28.85  ? 73   ALA   A N   1 
ATOM   562  C  CA  . ALA   A  1 98  ? -35.012 15.086  26.101 1.00 35.00  ? 73   ALA   A CA  1 
ATOM   563  C  C   . ALA   A  1 98  ? -33.725 14.277  26.188 1.00 35.10  ? 73   ALA   A C   1 
ATOM   564  O  O   . ALA   A  1 98  ? -33.595 13.229  25.549 1.00 28.59  ? 73   ALA   A O   1 
ATOM   565  C  CB  . ALA   A  1 98  ? -36.126 14.415  26.906 1.00 30.81  ? 73   ALA   A CB  1 
ATOM   566  N  N   . CYS   A  1 99  ? -32.771 14.773  26.981 1.00 34.27  ? 74   CYS   A N   1 
ATOM   567  C  CA  . CYS   A  1 99  ? -31.412 14.243  26.914 1.00 31.19  ? 74   CYS   A CA  1 
ATOM   568  C  C   . CYS   A  1 99  ? -31.357 12.764  27.270 1.00 30.26  ? 74   CYS   A C   1 
ATOM   569  O  O   . CYS   A  1 99  ? -30.611 11.999  26.649 1.00 28.48  ? 74   CYS   A O   1 
ATOM   570  C  CB  . CYS   A  1 99  ? -30.487 15.039  27.833 1.00 38.93  ? 74   CYS   A CB  1 
ATOM   571  S  SG  . CYS   A  1 99  ? -28.738 14.598  27.662 1.00 35.69  ? 74   CYS   A SG  1 
ATOM   572  N  N   . HIS   A  1 100 ? -32.147 12.333  28.256 1.00 23.63  ? 75   HIS   A N   1 
ATOM   573  C  CA  . HIS   A  1 100 ? -32.081 10.933  28.654 1.00 31.95  ? 75   HIS   A CA  1 
ATOM   574  C  C   . HIS   A  1 100 ? -32.766 10.022  27.643 1.00 30.66  ? 75   HIS   A C   1 
ATOM   575  O  O   . HIS   A  1 100 ? -32.372 8.858   27.498 1.00 25.70  ? 75   HIS   A O   1 
ATOM   576  C  CB  . HIS   A  1 100 ? -32.692 10.770  30.044 1.00 36.26  ? 75   HIS   A CB  1 
ATOM   577  C  CG  . HIS   A  1 100 ? -31.871 11.396  31.129 1.00 42.97  ? 75   HIS   A CG  1 
ATOM   578  N  ND1 . HIS   A  1 100 ? -31.008 10.674  31.925 1.00 39.12  ? 75   HIS   A ND1 1 
ATOM   579  C  CD2 . HIS   A  1 100 ? -31.768 12.684  31.534 1.00 40.30  ? 75   HIS   A CD2 1 
ATOM   580  C  CE1 . HIS   A  1 100 ? -30.417 11.489  32.780 1.00 39.53  ? 75   HIS   A CE1 1 
ATOM   581  N  NE2 . HIS   A  1 100 ? -30.861 12.714  32.565 1.00 41.24  ? 75   HIS   A NE2 1 
ATOM   582  N  N   . GLY   A  1 101 ? -33.787 10.517  26.939 1.00 30.82  ? 76   GLY   A N   1 
ATOM   583  C  CA  . GLY   A  1 101 ? -34.307 9.771   25.805 1.00 33.64  ? 76   GLY   A CA  1 
ATOM   584  C  C   . GLY   A  1 101 ? -33.292 9.668   24.683 1.00 26.93  ? 76   GLY   A C   1 
ATOM   585  O  O   . GLY   A  1 101 ? -33.145 8.615   24.057 1.00 28.24  ? 76   GLY   A O   1 
ATOM   586  N  N   . CYS   A  1 102 ? -32.599 10.773  24.399 1.00 26.95  ? 77   CYS   A N   1 
ATOM   587  C  CA  . CYS   A  1 102 ? -31.510 10.748  23.432 1.00 28.17  ? 77   CYS   A CA  1 
ATOM   588  C  C   . CYS   A  1 102 ? -30.444 9.744   23.851 1.00 34.16  ? 77   CYS   A C   1 
ATOM   589  O  O   . CYS   A  1 102 ? -29.890 9.020   23.015 1.00 26.61  ? 77   CYS   A O   1 
ATOM   590  C  CB  . CYS   A  1 102 ? -30.913 12.146  23.285 1.00 27.93  ? 77   CYS   A CB  1 
ATOM   591  S  SG  . CYS   A  1 102 ? -29.506 12.213  22.172 1.00 32.45  ? 77   CYS   A SG  1 
ATOM   592  N  N   . LEU   A  1 103 ? -30.145 9.697   25.152 1.00 28.30  ? 78   LEU   A N   1 
ATOM   593  C  CA  . LEU   A  1 103 ? -29.146 8.774   25.677 1.00 26.23  ? 78   LEU   A CA  1 
ATOM   594  C  C   . LEU   A  1 103 ? -29.517 7.328   25.384 1.00 25.84  ? 78   LEU   A C   1 
ATOM   595  O  O   . LEU   A  1 103 ? -28.648 6.511   25.053 1.00 24.33  ? 78   LEU   A O   1 
ATOM   596  C  CB  . LEU   A  1 103 ? -29.003 8.977   27.183 1.00 28.28  ? 78   LEU   A CB  1 
ATOM   597  C  CG  . LEU   A  1 103 ? -27.706 9.480   27.807 1.00 41.00  ? 78   LEU   A CG  1 
ATOM   598  C  CD1 . LEU   A  1 103 ? -27.793 9.228   29.300 1.00 23.64  ? 78   LEU   A CD1 1 
ATOM   599  C  CD2 . LEU   A  1 103 ? -26.478 8.814   27.201 1.00 20.98  ? 78   LEU   A CD2 1 
ATOM   600  N  N   . PHE   A  1 104 ? -30.800 6.985   25.523 1.00 22.35  ? 79   PHE   A N   1 
ATOM   601  C  CA  . PHE   A  1 104 ? -31.217 5.607   25.289 1.00 22.28  ? 79   PHE   A CA  1 
ATOM   602  C  C   . PHE   A  1 104 ? -31.024 5.219   23.829 1.00 21.70  ? 79   PHE   A C   1 
ATOM   603  O  O   . PHE   A  1 104 ? -30.491 4.145   23.528 1.00 24.89  ? 79   PHE   A O   1 
ATOM   604  C  CB  . PHE   A  1 104 ? -32.674 5.407   25.701 1.00 26.33  ? 79   PHE   A CB  1 
ATOM   605  C  CG  . PHE   A  1 104 ? -33.162 4.004   25.490 1.00 28.72  ? 79   PHE   A CG  1 
ATOM   606  C  CD1 . PHE   A  1 104 ? -32.820 2.999   26.378 1.00 28.79  ? 79   PHE   A CD1 1 
ATOM   607  C  CD2 . PHE   A  1 104 ? -33.929 3.681   24.383 1.00 27.77  ? 79   PHE   A CD2 1 
ATOM   608  C  CE1 . PHE   A  1 104 ? -33.255 1.706   26.181 1.00 30.42  ? 79   PHE   A CE1 1 
ATOM   609  C  CE2 . PHE   A  1 104 ? -34.365 2.387   24.180 1.00 26.97  ? 79   PHE   A CE2 1 
ATOM   610  C  CZ  . PHE   A  1 104 ? -34.027 1.399   25.082 1.00 31.44  ? 79   PHE   A CZ  1 
ATOM   611  N  N   . ILE   A  1 105 ? -31.459 6.081   22.906 1.00 22.47  ? 80   ILE   A N   1 
ATOM   612  C  CA  A ILE   A  1 105 ? -31.303 5.831   21.474 0.27 25.36  ? 80   ILE   A CA  1 
ATOM   613  C  CA  B ILE   A  1 105 ? -31.302 5.732   21.501 0.73 25.50  ? 80   ILE   A CA  1 
ATOM   614  C  C   . ILE   A  1 105 ? -29.830 5.714   21.107 1.00 20.04  ? 80   ILE   A C   1 
ATOM   615  O  O   . ILE   A  1 105 ? -29.449 4.964   20.200 1.00 22.04  ? 80   ILE   A O   1 
ATOM   616  C  CB  A ILE   A  1 105 ? -32.002 6.964   20.692 0.27 23.94  ? 80   ILE   A CB  1 
ATOM   617  C  CB  B ILE   A  1 105 ? -32.132 6.662   20.595 0.73 23.78  ? 80   ILE   A CB  1 
ATOM   618  C  CG1 A ILE   A  1 105 ? -33.525 6.867   20.852 0.27 28.64  ? 80   ILE   A CG1 1 
ATOM   619  C  CG1 B ILE   A  1 105 ? -31.536 8.066   20.530 0.73 22.20  ? 80   ILE   A CG1 1 
ATOM   620  C  CG2 A ILE   A  1 105 ? -31.566 6.992   19.230 0.27 22.18  ? 80   ILE   A CG2 1 
ATOM   621  C  CG2 B ILE   A  1 105 ? -33.576 6.712   21.066 0.73 29.15  ? 80   ILE   A CG2 1 
ATOM   622  C  CD1 A ILE   A  1 105 ? -34.276 6.577   19.573 0.27 24.70  ? 80   ILE   A CD1 1 
ATOM   623  C  CD1 B ILE   A  1 105 ? -32.151 8.925   19.441 0.73 33.64  ? 80   ILE   A CD1 1 
ATOM   624  N  N   . ALA   A  1 106 ? -28.977 6.476   21.795 1.00 20.73  ? 81   ALA   A N   1 
ATOM   625  C  CA  . ALA   A  1 106 ? -27.547 6.422   21.514 1.00 23.74  ? 81   ALA   A CA  1 
ATOM   626  C  C   . ALA   A  1 106 ? -26.932 5.121   22.018 1.00 22.18  ? 81   ALA   A C   1 
ATOM   627  O  O   . ALA   A  1 106 ? -26.050 4.552   21.363 1.00 23.12  ? 81   ALA   A O   1 
ATOM   628  C  CB  . ALA   A  1 106 ? -26.841 7.621   22.148 1.00 18.45  ? 81   ALA   A CB  1 
ATOM   629  N  N   . CYS   A  1 107 ? -27.379 4.637   23.179 1.00 22.56  ? 82   CYS   A N   1 
ATOM   630  C  CA  . CYS   A  1 107 ? -26.688 3.557   23.871 1.00 24.38  ? 82   CYS   A CA  1 
ATOM   631  C  C   . CYS   A  1 107 ? -27.241 2.168   23.583 1.00 24.44  ? 82   CYS   A C   1 
ATOM   632  O  O   . CYS   A  1 107 ? -26.561 1.183   23.890 1.00 18.42  ? 82   CYS   A O   1 
ATOM   633  C  CB  . CYS   A  1 107 ? -26.719 3.792   25.388 1.00 24.61  ? 82   CYS   A CB  1 
ATOM   634  S  SG  . CYS   A  1 107 ? -25.727 5.200   25.938 1.00 25.61  ? 82   CYS   A SG  1 
ATOM   635  N  N   . PHE   A  1 108 ? -28.448 2.051   23.018 1.00 20.56  ? 83   PHE   A N   1 
ATOM   636  C  CA  . PHE   A  1 108 ? -29.031 0.721   22.848 1.00 21.95  ? 83   PHE   A CA  1 
ATOM   637  C  C   . PHE   A  1 108 ? -28.135 -0.185  22.010 1.00 18.42  ? 83   PHE   A C   1 
ATOM   638  O  O   . PHE   A  1 108 ? -28.062 -1.394  22.258 1.00 21.00  ? 83   PHE   A O   1 
ATOM   639  C  CB  . PHE   A  1 108 ? -30.424 0.804   22.225 1.00 23.13  ? 83   PHE   A CB  1 
ATOM   640  C  CG  . PHE   A  1 108 ? -31.105 -0.533  22.124 1.00 28.18  ? 83   PHE   A CG  1 
ATOM   641  C  CD1 . PHE   A  1 108 ? -31.491 -1.213  23.271 1.00 29.63  ? 83   PHE   A CD1 1 
ATOM   642  C  CD2 . PHE   A  1 108 ? -31.327 -1.128  20.892 1.00 23.82  ? 83   PHE   A CD2 1 
ATOM   643  C  CE1 . PHE   A  1 108 ? -32.105 -2.452  23.190 1.00 26.65  ? 83   PHE   A CE1 1 
ATOM   644  C  CE2 . PHE   A  1 108 ? -31.941 -2.368  20.804 1.00 23.77  ? 83   PHE   A CE2 1 
ATOM   645  C  CZ  . PHE   A  1 108 ? -32.329 -3.031  21.955 1.00 30.79  ? 83   PHE   A CZ  1 
ATOM   646  N  N   . VAL   A  1 109 ? -27.455 0.375   21.003 1.00 24.90  ? 84   VAL   A N   1 
ATOM   647  C  CA  . VAL   A  1 109 ? -26.588 -0.450  20.162 1.00 21.89  ? 84   VAL   A CA  1 
ATOM   648  C  C   . VAL   A  1 109 ? -25.456 -1.050  20.987 1.00 19.34  ? 84   VAL   A C   1 
ATOM   649  O  O   . VAL   A  1 109 ? -24.943 -2.129  20.662 1.00 20.67  ? 84   VAL   A O   1 
ATOM   650  C  CB  . VAL   A  1 109 ? -26.049 0.376   18.974 1.00 17.12  ? 84   VAL   A CB  1 
ATOM   651  C  CG1 . VAL   A  1 109 ? -25.152 1.497   19.463 1.00 14.93  ? 84   VAL   A CG1 1 
ATOM   652  C  CG2 . VAL   A  1 109 ? -25.313 -0.515  17.977 1.00 18.64  ? 84   VAL   A CG2 1 
ATOM   653  N  N   . LEU   A  1 110 ? -25.050 -0.370  22.064 1.00 20.36  ? 85   LEU   A N   1 
ATOM   654  C  CA  . LEU   A  1 110 ? -24.014 -0.910  22.938 1.00 21.81  ? 85   LEU   A CA  1 
ATOM   655  C  C   . LEU   A  1 110 ? -24.495 -2.161  23.657 1.00 20.32  ? 85   LEU   A C   1 
ATOM   656  O  O   . LEU   A  1 110 ? -23.690 -3.050  23.957 1.00 19.54  ? 85   LEU   A O   1 
ATOM   657  C  CB  . LEU   A  1 110 ? -23.572 0.151   23.947 1.00 20.21  ? 85   LEU   A CB  1 
ATOM   658  C  CG  . LEU   A  1 110 ? -23.117 1.483   23.348 1.00 29.08  ? 85   LEU   A CG  1 
ATOM   659  C  CD1 . LEU   A  1 110 ? -22.749 2.479   24.440 1.00 21.82  ? 85   LEU   A CD1 1 
ATOM   660  C  CD2 . LEU   A  1 110 ? -21.948 1.266   22.393 1.00 21.22  ? 85   LEU   A CD2 1 
ATOM   661  N  N   . VAL   A  1 111 ? -25.796 -2.243  23.947 1.00 20.27  ? 86   VAL   A N   1 
ATOM   662  C  CA  . VAL   A  1 111 ? -26.360 -3.463  24.519 1.00 19.44  ? 86   VAL   A CA  1 
ATOM   663  C  C   . VAL   A  1 111 ? -26.215 -4.615  23.536 1.00 23.14  ? 86   VAL   A C   1 
ATOM   664  O  O   . VAL   A  1 111 ? -25.793 -5.720  23.896 1.00 18.38  ? 86   VAL   A O   1 
ATOM   665  C  CB  . VAL   A  1 111 ? -27.835 -3.244  24.905 1.00 23.03  ? 86   VAL   A CB  1 
ATOM   666  C  CG1 . VAL   A  1 111 ? -28.430 -4.522  25.488 1.00 20.56  ? 86   VAL   A CG1 1 
ATOM   667  C  CG2 . VAL   A  1 111 ? -27.970 -2.084  25.878 1.00 16.50  ? 86   VAL   A CG2 1 
ATOM   668  N  N   . LEU   A  1 112 ? -26.561 -4.364  22.271 1.00 17.84  ? 87   LEU   A N   1 
ATOM   669  C  CA  . LEU   A  1 112 ? -26.508 -5.413  21.261 1.00 19.27  ? 87   LEU   A CA  1 
ATOM   670  C  C   . LEU   A  1 112 ? -25.070 -5.830  20.986 1.00 18.88  ? 87   LEU   A C   1 
ATOM   671  O  O   . LEU   A  1 112 ? -24.782 -7.022  20.827 1.00 21.71  ? 87   LEU   A O   1 
ATOM   672  C  CB  . LEU   A  1 112 ? -27.189 -4.934  19.979 1.00 17.45  ? 87   LEU   A CB  1 
ATOM   673  C  CG  . LEU   A  1 112 ? -28.656 -4.512  20.132 1.00 22.14  ? 87   LEU   A CG  1 
ATOM   674  C  CD1 . LEU   A  1 112 ? -29.257 -4.137  18.784 1.00 19.97  ? 87   LEU   A CD1 1 
ATOM   675  C  CD2 . LEU   A  1 112 ? -29.482 -5.596  20.814 1.00 19.86  ? 87   LEU   A CD2 1 
ATOM   676  N  N   . ALA   A  1 113 ? -24.153 -4.861  20.919 1.00 20.06  ? 88   ALA   A N   1 
ATOM   677  C  CA  . ALA   A  1 113 ? -22.748 -5.202  20.734 1.00 21.78  ? 88   ALA   A CA  1 
ATOM   678  C  C   . ALA   A  1 113 ? -22.228 -6.019  21.909 1.00 19.99  ? 88   ALA   A C   1 
ATOM   679  O  O   . ALA   A  1 113 ? -21.461 -6.970  21.721 1.00 20.89  ? 88   ALA   A O   1 
ATOM   680  C  CB  . ALA   A  1 113 ? -21.919 -3.931  20.552 1.00 17.08  ? 88   ALA   A CB  1 
ATOM   681  N  N   . GLN   A  1 114 ? -22.629 -5.659  23.133 1.00 23.50  ? 89   GLN   A N   1 
ATOM   682  C  CA  . GLN   A  1 114 ? -22.134 -6.377  24.303 1.00 20.37  ? 89   GLN   A CA  1 
ATOM   683  C  C   . GLN   A  1 114 ? -22.670 -7.803  24.329 1.00 25.72  ? 89   GLN   A C   1 
ATOM   684  O  O   . GLN   A  1 114 ? -21.935 -8.746  24.644 1.00 21.51  ? 89   GLN   A O   1 
ATOM   685  C  CB  . GLN   A  1 114 ? -22.513 -5.642  25.586 1.00 25.89  ? 89   GLN   A CB  1 
ATOM   686  C  CG  . GLN   A  1 114 ? -21.656 -6.049  26.772 1.00 23.94  ? 89   GLN   A CG  1 
ATOM   687  C  CD  . GLN   A  1 114 ? -20.179 -5.822  26.503 1.00 25.73  ? 89   GLN   A CD  1 
ATOM   688  O  OE1 . GLN   A  1 114 ? -19.785 -4.758  26.025 1.00 26.59  ? 89   GLN   A OE1 1 
ATOM   689  N  NE2 . GLN   A  1 114 ? -19.357 -6.826  26.793 1.00 26.05  ? 89   GLN   A NE2 1 
ATOM   690  N  N   . SER   A  1 115 ? -23.958 -7.975  24.011 1.00 17.81  ? 90   SER   A N   1 
ATOM   691  C  CA  . SER   A  1 115 ? -24.529 -9.314  23.925 1.00 20.15  ? 90   SER   A CA  1 
ATOM   692  C  C   . SER   A  1 115 ? -23.802 -10.151 22.883 1.00 25.89  ? 90   SER   A C   1 
ATOM   693  O  O   . SER   A  1 115 ? -23.550 -11.342 23.097 1.00 21.96  ? 90   SER   A O   1 
ATOM   694  C  CB  . SER   A  1 115 ? -26.019 -9.228  23.595 1.00 21.20  ? 90   SER   A CB  1 
ATOM   695  O  OG  . SER   A  1 115 ? -26.596 -10.521 23.505 1.00 21.84  ? 90   SER   A OG  1 
ATOM   696  N  N   . SER   A  1 116 ? -23.462 -9.542  21.744 1.00 20.81  ? 91   SER   A N   1 
ATOM   697  C  CA  . SER   A  1 116 ? -22.711 -10.256 20.717 1.00 22.96  ? 91   SER   A CA  1 
ATOM   698  C  C   . SER   A  1 116 ? -21.371 -10.735 21.259 1.00 21.71  ? 91   SER   A C   1 
ATOM   699  O  O   . SER   A  1 116 ? -20.950 -11.868 20.997 1.00 25.86  ? 91   SER   A O   1 
ATOM   700  C  CB  . SER   A  1 116 ? -22.508 -9.353  19.500 1.00 23.02  ? 91   SER   A CB  1 
ATOM   701  O  OG  . SER   A  1 116 ? -23.747 -9.054  18.881 1.00 23.50  ? 91   SER   A OG  1 
ATOM   702  N  N   . ILE   A  1 117 ? -20.693 -9.882  22.028 1.00 21.91  ? 92   ILE   A N   1 
ATOM   703  C  CA  . ILE   A  1 117 ? -19.393 -10.237 22.586 1.00 19.33  ? 92   ILE   A CA  1 
ATOM   704  C  C   . ILE   A  1 117 ? -19.524 -11.420 23.534 1.00 22.14  ? 92   ILE   A C   1 
ATOM   705  O  O   . ILE   A  1 117 ? -18.723 -12.362 23.489 1.00 23.71  ? 92   ILE   A O   1 
ATOM   706  C  CB  . ILE   A  1 117 ? -18.772 -9.013  23.282 1.00 21.31  ? 92   ILE   A CB  1 
ATOM   707  C  CG1 . ILE   A  1 117 ? -18.160 -8.074  22.242 1.00 25.55  ? 92   ILE   A CG1 1 
ATOM   708  C  CG2 . ILE   A  1 117 ? -17.738 -9.444  24.312 1.00 21.99  ? 92   ILE   A CG2 1 
ATOM   709  C  CD1 . ILE   A  1 117 ? -17.938 -6.676  22.756 1.00 33.00  ? 92   ILE   A CD1 1 
ATOM   710  N  N   . PHE   A  1 118 ? -20.542 -11.396 24.400 1.00 18.62  ? 93   PHE   A N   1 
ATOM   711  C  CA  . PHE   A  1 118 ? -20.756 -12.505 25.325 1.00 24.84  ? 93   PHE   A CA  1 
ATOM   712  C  C   . PHE   A  1 118 ? -21.063 -13.795 24.574 1.00 28.53  ? 93   PHE   A C   1 
ATOM   713  O  O   . PHE   A  1 118 ? -20.576 -14.870 24.946 1.00 25.67  ? 93   PHE   A O   1 
ATOM   714  C  CB  . PHE   A  1 118 ? -21.896 -12.167 26.288 1.00 24.25  ? 93   PHE   A CB  1 
ATOM   715  C  CG  . PHE   A  1 118 ? -21.512 -11.200 27.375 1.00 28.93  ? 93   PHE   A CG  1 
ATOM   716  C  CD1 . PHE   A  1 118 ? -20.267 -11.268 27.982 1.00 36.53  ? 93   PHE   A CD1 1 
ATOM   717  C  CD2 . PHE   A  1 118 ? -22.401 -10.219 27.789 1.00 24.61  ? 93   PHE   A CD2 1 
ATOM   718  C  CE1 . PHE   A  1 118 ? -19.916 -10.376 28.983 1.00 40.19  ? 93   PHE   A CE1 1 
ATOM   719  C  CE2 . PHE   A  1 118 ? -22.057 -9.323  28.791 1.00 24.53  ? 93   PHE   A CE2 1 
ATOM   720  C  CZ  . PHE   A  1 118 ? -20.812 -9.403  29.389 1.00 28.68  ? 93   PHE   A CZ  1 
ATOM   721  N  N   . SER   A  1 119 ? -21.880 -13.712 23.520 1.00 22.99  ? 94   SER   A N   1 
ATOM   722  C  CA  . SER   A  1 119 ? -22.176 -14.902 22.726 1.00 23.97  ? 94   SER   A CA  1 
ATOM   723  C  C   . SER   A  1 119 ? -20.920 -15.433 22.049 1.00 27.74  ? 94   SER   A C   1 
ATOM   724  O  O   . SER   A  1 119 ? -20.688 -16.647 22.018 1.00 24.04  ? 94   SER   A O   1 
ATOM   725  C  CB  . SER   A  1 119 ? -23.256 -14.593 21.690 1.00 26.72  ? 94   SER   A CB  1 
ATOM   726  O  OG  . SER   A  1 119 ? -24.496 -14.315 22.313 1.00 26.83  ? 94   SER   A OG  1 
ATOM   727  N  N   . LEU   A  1 120 ? -20.106 -14.536 21.484 1.00 25.38  ? 95   LEU   A N   1 
ATOM   728  C  CA  . LEU   A  1 120 ? -18.890 -14.970 20.805 1.00 21.80  ? 95   LEU   A CA  1 
ATOM   729  C  C   . LEU   A  1 120 ? -17.917 -15.613 21.782 1.00 27.05  ? 95   LEU   A C   1 
ATOM   730  O  O   . LEU   A  1 120 ? -17.278 -16.623 21.462 1.00 27.63  ? 95   LEU   A O   1 
ATOM   731  C  CB  . LEU   A  1 120 ? -18.232 -13.785 20.096 1.00 27.14  ? 95   LEU   A CB  1 
ATOM   732  C  CG  . LEU   A  1 120 ? -18.964 -13.235 18.873 1.00 27.09  ? 95   LEU   A CG  1 
ATOM   733  C  CD1 . LEU   A  1 120 ? -18.423 -11.862 18.484 1.00 24.79  ? 95   LEU   A CD1 1 
ATOM   734  C  CD2 . LEU   A  1 120 ? -18.838 -14.213 17.716 1.00 24.72  ? 95   LEU   A CD2 1 
ATOM   735  N  N   . LEU   A  1 121 ? -17.790 -15.040 22.982 1.00 21.82  ? 96   LEU   A N   1 
ATOM   736  C  CA  . LEU   A  1 121 ? -16.917 -15.621 23.997 1.00 24.66  ? 96   LEU   A CA  1 
ATOM   737  C  C   . LEU   A  1 121 ? -17.426 -16.987 24.438 1.00 25.20  ? 96   LEU   A C   1 
ATOM   738  O  O   . LEU   A  1 121 ? -16.636 -17.919 24.634 1.00 26.52  ? 96   LEU   A O   1 
ATOM   739  C  CB  . LEU   A  1 121 ? -16.787 -14.669 25.186 1.00 30.84  ? 96   LEU   A CB  1 
ATOM   740  C  CG  . LEU   A  1 121 ? -15.889 -15.128 26.336 1.00 37.15  ? 96   LEU   A CG  1 
ATOM   741  C  CD1 . LEU   A  1 121 ? -14.504 -15.480 25.814 1.00 34.23  ? 96   LEU   A CD1 1 
ATOM   742  C  CD2 . LEU   A  1 121 ? -15.796 -14.047 27.405 1.00 34.31  ? 96   LEU   A CD2 1 
ATOM   743  N  N   . ALA   A  1 122 ? -18.743 -17.118 24.612 1.00 23.36  ? 97   ALA   A N   1 
ATOM   744  C  CA  . ALA   A  1 122 ? -19.319 -18.400 25.008 1.00 33.10  ? 97   ALA   A CA  1 
ATOM   745  C  C   . ALA   A  1 122 ? -19.063 -19.468 23.954 1.00 35.02  ? 97   ALA   A C   1 
ATOM   746  O  O   . ALA   A  1 122 ? -18.754 -20.618 24.287 1.00 27.66  ? 97   ALA   A O   1 
ATOM   747  C  CB  . ALA   A  1 122 ? -20.818 -18.246 25.258 1.00 29.55  ? 97   ALA   A CB  1 
ATOM   748  N  N   . ILE   A  1 123 ? -19.216 -19.114 22.675 1.00 31.19  ? 98   ILE   A N   1 
ATOM   749  C  CA  . ILE   A  1 123 ? -18.973 -20.073 21.599 1.00 26.25  ? 98   ILE   A CA  1 
ATOM   750  C  C   . ILE   A  1 123 ? -17.532 -20.561 21.641 1.00 33.45  ? 98   ILE   A C   1 
ATOM   751  O  O   . ILE   A  1 123 ? -17.262 -21.759 21.490 1.00 32.01  ? 98   ILE   A O   1 
ATOM   752  C  CB  . ILE   A  1 123 ? -19.324 -19.448 20.237 1.00 24.85  ? 98   ILE   A CB  1 
ATOM   753  C  CG1 . ILE   A  1 123 ? -20.837 -19.261 20.116 1.00 28.56  ? 98   ILE   A CG1 1 
ATOM   754  C  CG2 . ILE   A  1 123 ? -18.798 -20.313 19.098 1.00 26.35  ? 98   ILE   A CG2 1 
ATOM   755  C  CD1 . ILE   A  1 123 ? -21.258 -18.399 18.943 1.00 23.86  ? 98   ILE   A CD1 1 
ATOM   756  N  N   . ALA   A  1 124 ? -16.585 -19.646 21.866 1.00 26.93  ? 99   ALA   A N   1 
ATOM   757  C  CA  . ALA   A  1 124 ? -15.183 -20.041 21.938 1.00 30.31  ? 99   ALA   A CA  1 
ATOM   758  C  C   . ALA   A  1 124 ? -14.965 -20.998 23.100 1.00 32.87  ? 99   ALA   A C   1 
ATOM   759  O  O   . ALA   A  1 124 ? -14.289 -22.023 22.962 1.00 31.56  ? 99   ALA   A O   1 
ATOM   760  C  CB  . ALA   A  1 124 ? -14.294 -18.804 22.080 1.00 23.16  ? 99   ALA   A CB  1 
ATOM   761  N  N   . ILE   A  1 125 ? -15.531 -20.669 24.262 1.00 30.19  ? 100  ILE   A N   1 
ATOM   762  C  CA  . ILE   A  1 125 ? -15.332 -21.497 25.444 1.00 35.73  ? 100  ILE   A CA  1 
ATOM   763  C  C   . ILE   A  1 125 ? -15.993 -22.854 25.239 1.00 34.83  ? 100  ILE   A C   1 
ATOM   764  O  O   . ILE   A  1 125 ? -15.438 -23.895 25.609 1.00 35.81  ? 100  ILE   A O   1 
ATOM   765  C  CB  . ILE   A  1 125 ? -15.876 -20.770 26.687 1.00 32.94  ? 100  ILE   A CB  1 
ATOM   766  C  CG1 . ILE   A  1 125 ? -14.979 -19.582 27.040 1.00 29.03  ? 100  ILE   A CG1 1 
ATOM   767  C  CG2 . ILE   A  1 125 ? -15.974 -21.722 27.871 1.00 27.28  ? 100  ILE   A CG2 1 
ATOM   768  C  CD1 . ILE   A  1 125 ? -15.566 -18.664 28.086 1.00 36.71  ? 100  ILE   A CD1 1 
ATOM   769  N  N   . ASP   A  1 126 ? -17.183 -22.859 24.630 1.00 30.38  ? 101  ASP   A N   1 
ATOM   770  C  CA  . ASP   A  1 126 ? -17.876 -24.106 24.324 1.00 30.89  ? 101  ASP   A CA  1 
ATOM   771  C  C   . ASP   A  1 126 ? -17.019 -25.013 23.446 1.00 37.48  ? 101  ASP   A C   1 
ATOM   772  O  O   . ASP   A  1 126 ? -16.901 -26.216 23.704 1.00 32.55  ? 101  ASP   A O   1 
ATOM   773  C  CB  . ASP   A  1 126 ? -19.217 -23.792 23.656 1.00 28.89  ? 101  ASP   A CB  1 
ATOM   774  C  CG  . ASP   A  1 126 ? -19.952 -25.035 23.201 1.00 40.78  ? 101  ASP   A CG  1 
ATOM   775  O  OD1 . ASP   A  1 126 ? -19.736 -25.470 22.052 1.00 39.62  ? 101  ASP   A OD1 1 
ATOM   776  O  OD2 . ASP   A  1 126 ? -20.753 -25.572 23.993 1.00 42.19  ? 101  ASP   A OD2 1 
ATOM   777  N  N   . ARG   A  1 127 ? -16.417 -24.453 22.393 1.00 29.90  ? 102  ARG   A N   1 
ATOM   778  C  CA  . ARG   A  1 127 ? -15.560 -25.260 21.528 1.00 33.62  ? 102  ARG   A CA  1 
ATOM   779  C  C   . ARG   A  1 127 ? -14.297 -25.714 22.246 1.00 39.43  ? 102  ARG   A C   1 
ATOM   780  O  O   . ARG   A  1 127 ? -13.768 -26.789 21.940 1.00 38.28  ? 102  ARG   A O   1 
ATOM   781  C  CB  . ARG   A  1 127 ? -15.211 -24.497 20.249 1.00 35.27  ? 102  ARG   A CB  1 
ATOM   782  C  CG  . ARG   A  1 127 ? -16.399 -24.162 19.347 1.00 38.07  ? 102  ARG   A CG  1 
ATOM   783  C  CD  . ARG   A  1 127 ? -17.061 -25.424 18.775 1.00 45.32  ? 102  ARG   A CD  1 
ATOM   784  N  NE  . ARG   A  1 127 ? -17.966 -26.086 19.708 1.00 53.82  ? 102  ARG   A NE  1 
ATOM   785  C  CZ  . ARG   A  1 127 ? -18.094 -27.401 19.825 1.00 50.95  ? 102  ARG   A CZ  1 
ATOM   786  N  NH1 . ARG   A  1 127 ? -17.381 -28.235 19.085 1.00 49.82  ? 102  ARG   A NH1 1 
ATOM   787  N  NH2 . ARG   A  1 127 ? -18.960 -27.893 20.707 1.00 41.79  ? 102  ARG   A NH2 1 
ATOM   788  N  N   . TYR   A  1 128 ? -13.786 -24.912 23.184 1.00 30.22  ? 103  TYR   A N   1 
ATOM   789  C  CA  . TYR   A  1 128 ? -12.633 -25.358 23.959 1.00 38.93  ? 103  TYR   A CA  1 
ATOM   790  C  C   . TYR   A  1 128 ? -13.010 -26.533 24.852 1.00 37.85  ? 103  TYR   A C   1 
ATOM   791  O  O   . TYR   A  1 128 ? -12.259 -27.509 24.958 1.00 41.50  ? 103  TYR   A O   1 
ATOM   792  C  CB  . TYR   A  1 128 ? -12.055 -24.217 24.793 1.00 36.69  ? 103  TYR   A CB  1 
ATOM   793  C  CG  . TYR   A  1 128 ? -10.914 -24.680 25.668 1.00 40.91  ? 103  TYR   A CG  1 
ATOM   794  C  CD1 . TYR   A  1 128 ? -9.659  -24.913 25.121 1.00 38.09  ? 103  TYR   A CD1 1 
ATOM   795  C  CD2 . TYR   A  1 128 ? -11.090 -24.912 27.025 1.00 50.02  ? 103  TYR   A CD2 1 
ATOM   796  C  CE1 . TYR   A  1 128 ? -8.606  -25.342 25.900 1.00 46.74  ? 103  TYR   A CE1 1 
ATOM   797  C  CE2 . TYR   A  1 128 ? -10.039 -25.349 27.815 1.00 50.53  ? 103  TYR   A CE2 1 
ATOM   798  C  CZ  . TYR   A  1 128 ? -8.800  -25.560 27.245 1.00 52.44  ? 103  TYR   A CZ  1 
ATOM   799  O  OH  . TYR   A  1 128 ? -7.748  -25.998 28.017 1.00 55.18  ? 103  TYR   A OH  1 
ATOM   800  N  N   . ILE   A  1 129 ? -14.168 -26.446 25.511 1.00 38.46  ? 104  ILE   A N   1 
ATOM   801  C  CA  . ILE   A  1 129 ? -14.656 -27.548 26.337 1.00 38.62  ? 104  ILE   A CA  1 
ATOM   802  C  C   . ILE   A  1 129 ? -14.839 -28.808 25.502 1.00 42.88  ? 104  ILE   A C   1 
ATOM   803  O  O   . ILE   A  1 129 ? -14.488 -29.913 25.934 1.00 42.89  ? 104  ILE   A O   1 
ATOM   804  C  CB  . ILE   A  1 129 ? -15.959 -27.133 27.051 1.00 41.71  ? 104  ILE   A CB  1 
ATOM   805  C  CG1 . ILE   A  1 129 ? -15.722 -25.929 27.968 1.00 35.01  ? 104  ILE   A CG1 1 
ATOM   806  C  CG2 . ILE   A  1 129 ? -16.632 -28.293 27.753 1.00 41.35  ? 104  ILE   A CG2 1 
ATOM   807  C  CD1 . ILE   A  1 129 ? -16.995 -25.294 28.479 1.00 39.73  ? 104  ILE   A CD1 1 
ATOM   808  N  N   . ALA   A  1 130 ? -15.372 -28.665 24.288 1.00 32.70  ? 105  ALA   A N   1 
ATOM   809  C  CA  . ALA   A  1 130 ? -15.615 -29.838 23.454 1.00 36.35  ? 105  ALA   A CA  1 
ATOM   810  C  C   . ALA   A  1 130 ? -14.313 -30.520 23.050 1.00 42.29  ? 105  ALA   A C   1 
ATOM   811  O  O   . ALA   A  1 130 ? -14.255 -31.752 22.964 1.00 53.48  ? 105  ALA   A O   1 
ATOM   812  C  CB  . ALA   A  1 130 ? -16.417 -29.442 22.216 1.00 36.98  ? 105  ALA   A CB  1 
ATOM   813  N  N   . ILE   A  1 131 ? -13.260 -29.744 22.801 1.00 37.78  ? 106  ILE   A N   1 
ATOM   814  C  CA  . ILE   A  1 131 ? -11.985 -30.325 22.390 1.00 40.59  ? 106  ILE   A CA  1 
ATOM   815  C  C   . ILE   A  1 131 ? -11.114 -30.765 23.568 1.00 51.27  ? 106  ILE   A C   1 
ATOM   816  O  O   . ILE   A  1 131 ? -10.303 -31.685 23.419 1.00 46.76  ? 106  ILE   A O   1 
ATOM   817  C  CB  . ILE   A  1 131 ? -11.217 -29.371 21.458 1.00 44.45  ? 106  ILE   A CB  1 
ATOM   818  C  CG1 . ILE   A  1 131 ? -10.148 -30.154 20.694 1.00 46.06  ? 106  ILE   A CG1 1 
ATOM   819  C  CG2 . ILE   A  1 131 ? -10.585 -28.230 22.236 1.00 46.09  ? 106  ILE   A CG2 1 
ATOM   820  C  CD1 . ILE   A  1 131 ? -9.873  -29.618 19.320 1.00 56.49  ? 106  ILE   A CD1 1 
ATOM   821  N  N   . ALA   A  1 132 ? -11.254 -30.149 24.743 1.00 44.62  ? 107  ALA   A N   1 
ATOM   822  C  CA  . ALA   A  1 132 ? -10.282 -30.425 25.796 1.00 50.95  ? 107  ALA   A CA  1 
ATOM   823  C  C   . ALA   A  1 132 ? -10.748 -31.523 26.742 1.00 50.17  ? 107  ALA   A C   1 
ATOM   824  O  O   . ALA   A  1 132 ? -9.925  -32.309 27.224 1.00 58.85  ? 107  ALA   A O   1 
ATOM   825  C  CB  . ALA   A  1 132 ? -9.984  -29.151 26.588 1.00 43.97  ? 107  ALA   A CB  1 
ATOM   826  N  N   . ILE   A  1 133 ? -12.045 -31.607 27.019 1.00 45.74  ? 108  ILE   A N   1 
ATOM   827  C  CA  . ILE   A  1 133 ? -12.567 -32.703 27.834 1.00 49.18  ? 108  ILE   A CA  1 
ATOM   828  C  C   . ILE   A  1 133 ? -13.829 -33.235 27.157 1.00 45.75  ? 108  ILE   A C   1 
ATOM   829  O  O   . ILE   A  1 133 ? -14.919 -33.214 27.746 1.00 50.07  ? 108  ILE   A O   1 
ATOM   830  C  CB  . ILE   A  1 133 ? -12.733 -32.299 29.320 1.00 53.43  ? 108  ILE   A CB  1 
ATOM   831  C  CG1 . ILE   A  1 133 ? -13.381 -30.923 29.573 1.00 57.19  ? 108  ILE   A CG1 1 
ATOM   832  C  CG2 . ILE   A  1 133 ? -11.387 -32.350 30.041 1.00 58.53  ? 108  ILE   A CG2 1 
ATOM   833  C  CD1 . ILE   A  1 133 ? -14.714 -30.679 29.021 1.00 61.07  ? 108  ILE   A CD1 1 
ATOM   834  N  N   . PRO   A  1 134 ? -13.702 -33.822 25.959 1.00 44.15  ? 109  PRO   A N   1 
ATOM   835  C  CA  . PRO   A  1 134 ? -14.896 -34.298 25.239 1.00 48.30  ? 109  PRO   A CA  1 
ATOM   836  C  C   . PRO   A  1 134 ? -15.662 -35.355 25.998 1.00 56.69  ? 109  PRO   A C   1 
ATOM   837  O  O   . PRO   A  1 134 ? -16.860 -35.532 25.748 1.00 53.68  ? 109  PRO   A O   1 
ATOM   838  C  CB  . PRO   A  1 134 ? -14.323 -34.863 23.930 1.00 43.47  ? 109  PRO   A CB  1 
ATOM   839  C  CG  . PRO   A  1 134 ? -12.895 -35.146 24.229 1.00 45.61  ? 109  PRO   A CG  1 
ATOM   840  C  CD  . PRO   A  1 134 ? -12.469 -34.089 25.198 1.00 46.01  ? 109  PRO   A CD  1 
ATOM   841  N  N   . LEU   A  1 135 ? -15.018 -36.041 26.942 1.00 65.19  ? 110  LEU   A N   1 
ATOM   842  C  CA  . LEU   A  1 135 ? -15.692 -37.112 27.658 1.00 67.96  ? 110  LEU   A CA  1 
ATOM   843  C  C   . LEU   A  1 135 ? -16.760 -36.566 28.593 1.00 63.83  ? 110  LEU   A C   1 
ATOM   844  O  O   . LEU   A  1 135 ? -17.723 -37.271 28.911 1.00 71.07  ? 110  LEU   A O   1 
ATOM   845  C  CB  . LEU   A  1 135 ? -14.668 -37.913 28.459 1.00 73.47  ? 110  LEU   A CB  1 
ATOM   846  C  CG  . LEU   A  1 135 ? -13.649 -38.718 27.656 1.00 74.63  ? 110  LEU   A CG  1 
ATOM   847  C  CD1 . LEU   A  1 135 ? -12.733 -39.506 28.581 1.00 77.99  ? 110  LEU   A CD1 1 
ATOM   848  C  CD2 . LEU   A  1 135 ? -14.352 -39.634 26.676 1.00 60.33  ? 110  LEU   A CD2 1 
ATOM   849  N  N   . ARG   A  1 136 ? -16.608 -35.325 29.052 1.00 59.90  ? 111  ARG   A N   1 
ATOM   850  C  CA  . ARG   A  1 136 ? -17.572 -34.730 29.971 1.00 69.76  ? 111  ARG   A CA  1 
ATOM   851  C  C   . ARG   A  1 136 ? -18.301 -33.530 29.378 1.00 62.02  ? 111  ARG   A C   1 
ATOM   852  O  O   . ARG   A  1 136 ? -19.008 -32.836 30.118 1.00 47.19  ? 111  ARG   A O   1 
ATOM   853  C  CB  . ARG   A  1 136 ? -16.960 -34.339 31.317 1.00 69.13  ? 111  ARG   A CB  1 
ATOM   854  C  CG  . ARG   A  1 136 ? -15.975 -35.298 31.928 1.00 77.15  ? 111  ARG   A CG  1 
ATOM   855  C  CD  . ARG   A  1 136 ? -15.682 -34.955 33.402 1.00 78.56  ? 111  ARG   A CD  1 
ATOM   856  N  NE  . ARG   A  1 136 ? -15.683 -33.530 33.745 1.00 89.77  ? 111  ARG   A NE  1 
ATOM   857  C  CZ  . ARG   A  1 136 ? -16.771 -32.799 33.977 1.00 84.73  ? 111  ARG   A CZ  1 
ATOM   858  N  NH1 . ARG   A  1 136 ? -17.987 -33.321 33.915 1.00 92.79  ? 111  ARG   A NH1 1 
ATOM   859  N  NH2 . ARG   A  1 136 ? -16.635 -31.509 34.268 1.00 62.41  ? 111  ARG   A NH2 1 
ATOM   860  N  N   . TYR   A  1 137 ? -18.120 -33.238 28.085 1.00 56.14  ? 112  TYR   A N   1 
ATOM   861  C  CA  . TYR   A  1 137 ? -18.809 -32.098 27.482 1.00 47.99  ? 112  TYR   A CA  1 
ATOM   862  C  C   . TYR   A  1 137 ? -20.320 -32.198 27.683 1.00 56.67  ? 112  TYR   A C   1 
ATOM   863  O  O   . TYR   A  1 137 ? -20.937 -31.275 28.226 1.00 50.36  ? 112  TYR   A O   1 
ATOM   864  C  CB  . TYR   A  1 137 ? -18.443 -31.994 25.997 1.00 44.99  ? 112  TYR   A CB  1 
ATOM   865  C  CG  . TYR   A  1 137 ? -19.208 -30.935 25.234 1.00 43.67  ? 112  TYR   A CG  1 
ATOM   866  C  CD1 . TYR   A  1 137 ? -20.414 -31.226 24.612 1.00 50.52  ? 112  TYR   A CD1 1 
ATOM   867  C  CD2 . TYR   A  1 137 ? -18.720 -29.638 25.145 1.00 41.49  ? 112  TYR   A CD2 1 
ATOM   868  C  CE1 . TYR   A  1 137 ? -21.109 -30.258 23.918 1.00 54.52  ? 112  TYR   A CE1 1 
ATOM   869  C  CE2 . TYR   A  1 137 ? -19.408 -28.663 24.455 1.00 39.92  ? 112  TYR   A CE2 1 
ATOM   870  C  CZ  . TYR   A  1 137 ? -20.600 -28.977 23.844 1.00 49.04  ? 112  TYR   A CZ  1 
ATOM   871  O  OH  . TYR   A  1 137 ? -21.285 -28.003 23.156 1.00 44.64  ? 112  TYR   A OH  1 
ATOM   872  N  N   . ASN   A  1 138 ? -20.945 -33.295 27.236 1.00 53.48  ? 113  ASN   A N   1 
ATOM   873  C  CA  . ASN   A  1 138 ? -22.406 -33.350 27.290 1.00 63.46  ? 113  ASN   A CA  1 
ATOM   874  C  C   . ASN   A  1 138 ? -22.926 -33.251 28.718 1.00 56.20  ? 113  ASN   A C   1 
ATOM   875  O  O   . ASN   A  1 138 ? -24.027 -32.732 28.936 1.00 60.03  ? 113  ASN   A O   1 
ATOM   876  C  CB  . ASN   A  1 138 ? -22.981 -34.609 26.633 1.00 61.82  ? 113  ASN   A CB  1 
ATOM   877  C  CG  . ASN   A  1 138 ? -23.029 -34.521 25.123 1.00 70.13  ? 113  ASN   A CG  1 
ATOM   878  O  OD1 . ASN   A  1 138 ? -23.150 -33.432 24.560 1.00 71.38  ? 113  ASN   A OD1 1 
ATOM   879  N  ND2 . ASN   A  1 138 ? -23.007 -35.671 24.459 1.00 77.54  ? 113  ASN   A ND2 1 
ATOM   880  N  N   . GLY   A  1 139 ? -22.172 -33.745 29.704 1.00 57.06  ? 114  GLY   A N   1 
ATOM   881  C  CA  . GLY   A  1 139 ? -22.631 -33.579 31.072 1.00 59.65  ? 114  GLY   A CA  1 
ATOM   882  C  C   . GLY   A  1 139 ? -22.369 -32.205 31.643 1.00 60.02  ? 114  GLY   A C   1 
ATOM   883  O  O   . GLY   A  1 139 ? -23.074 -31.785 32.566 1.00 62.69  ? 114  GLY   A O   1 
ATOM   884  N  N   . LEU   A  1 140 ? -21.370 -31.499 31.122 1.00 53.65  ? 115  LEU   A N   1 
ATOM   885  C  CA  . LEU   A  1 140 ? -21.067 -30.173 31.631 1.00 52.90  ? 115  LEU   A CA  1 
ATOM   886  C  C   . LEU   A  1 140 ? -21.880 -29.114 30.894 1.00 55.15  ? 115  LEU   A C   1 
ATOM   887  O  O   . LEU   A  1 140 ? -22.380 -28.169 31.512 1.00 47.94  ? 115  LEU   A O   1 
ATOM   888  C  CB  . LEU   A  1 140 ? -19.565 -29.892 31.540 1.00 56.28  ? 115  LEU   A CB  1 
ATOM   889  C  CG  . LEU   A  1 140 ? -19.041 -28.470 31.747 1.00 68.20  ? 115  LEU   A CG  1 
ATOM   890  C  CD1 . LEU   A  1 140 ? -19.538 -27.900 33.073 1.00 68.14  ? 115  LEU   A CD1 1 
ATOM   891  C  CD2 . LEU   A  1 140 ? -17.520 -28.503 31.730 1.00 66.02  ? 115  LEU   A CD2 1 
ATOM   892  N  N   . VAL   A  1 141 ? -22.012 -29.239 29.577 1.00 51.03  ? 116  VAL   A N   1 
ATOM   893  C  CA  . VAL   A  1 141 ? -22.583 -28.194 28.737 1.00 46.64  ? 116  VAL   A CA  1 
ATOM   894  C  C   . VAL   A  1 141 ? -23.938 -28.697 28.263 1.00 46.06  ? 116  VAL   A C   1 
ATOM   895  O  O   . VAL   A  1 141 ? -24.016 -29.498 27.327 1.00 56.91  ? 116  VAL   A O   1 
ATOM   896  C  CB  . VAL   A  1 141 ? -21.672 -27.835 27.559 1.00 49.34  ? 116  VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A  1 141 ? -22.271 -26.683 26.768 1.00 43.61  ? 116  VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A  1 141 ? -20.276 -27.457 28.075 1.00 50.73  ? 116  VAL   A CG2 1 
ATOM   899  N  N   . THR   A  1 142 ? -25.002 -28.230 28.913 1.00 40.06  ? 117  THR   A N   1 
ATOM   900  C  CA  . THR   A  1 142 ? -26.366 -28.669 28.658 1.00 46.15  ? 117  THR   A CA  1 
ATOM   901  C  C   . THR   A  1 142 ? -27.201 -27.508 28.130 1.00 48.03  ? 117  THR   A C   1 
ATOM   902  O  O   . THR   A  1 142 ? -26.848 -26.336 28.291 1.00 42.96  ? 117  THR   A O   1 
ATOM   903  C  CB  . THR   A  1 142 ? -27.009 -29.244 29.927 1.00 50.15  ? 117  THR   A CB  1 
ATOM   904  O  OG1 . THR   A  1 142 ? -27.136 -28.206 30.906 1.00 46.35  ? 117  THR   A OG1 1 
ATOM   905  C  CG2 . THR   A  1 142 ? -26.162 -30.374 30.493 1.00 46.94  ? 117  THR   A CG2 1 
ATOM   906  N  N   . GLY   A  1 143 ? -28.315 -27.852 27.481 1.00 48.66  ? 118  GLY   A N   1 
ATOM   907  C  CA  . GLY   A  1 143 ? -29.195 -26.828 26.938 1.00 42.98  ? 118  GLY   A CA  1 
ATOM   908  C  C   . GLY   A  1 143 ? -29.773 -25.909 27.999 1.00 45.29  ? 118  GLY   A C   1 
ATOM   909  O  O   . GLY   A  1 143 ? -29.872 -24.697 27.794 1.00 44.86  ? 118  GLY   A O   1 
ATOM   910  N  N   . THR   A  1 144 ? -30.152 -26.469 29.151 1.00 43.08  ? 119  THR   A N   1 
ATOM   911  C  CA  . THR   A  1 144 ? -30.724 -25.647 30.216 1.00 49.59  ? 119  THR   A CA  1 
ATOM   912  C  C   . THR   A  1 144 ? -29.696 -24.673 30.783 1.00 37.76  ? 119  THR   A C   1 
ATOM   913  O  O   . THR   A  1 144 ? -30.030 -23.524 31.097 1.00 48.87  ? 119  THR   A O   1 
ATOM   914  C  CB  . THR   A  1 144 ? -31.305 -26.535 31.319 1.00 45.48  ? 119  THR   A CB  1 
ATOM   915  O  OG1 . THR   A  1 144 ? -30.265 -26.946 32.214 1.00 55.34  ? 119  THR   A OG1 1 
ATOM   916  C  CG2 . THR   A  1 144 ? -31.977 -27.763 30.717 1.00 54.90  ? 119  THR   A CG2 1 
ATOM   917  N  N   . ARG   A  1 145 ? -28.443 -25.110 30.927 1.00 42.16  ? 120  ARG   A N   1 
ATOM   918  C  CA  . ARG   A  1 145 ? -27.398 -24.202 31.395 1.00 46.59  ? 120  ARG   A CA  1 
ATOM   919  C  C   . ARG   A  1 145 ? -27.078 -23.140 30.354 1.00 44.68  ? 120  ARG   A C   1 
ATOM   920  O  O   . ARG   A  1 145 ? -26.824 -21.981 30.702 1.00 45.62  ? 120  ARG   A O   1 
ATOM   921  C  CB  . ARG   A  1 145 ? -26.136 -24.975 31.771 1.00 42.28  ? 120  ARG   A CB  1 
ATOM   922  C  CG  . ARG   A  1 145 ? -26.273 -25.789 33.036 1.00 56.02  ? 120  ARG   A CG  1 
ATOM   923  C  CD  . ARG   A  1 145 ? -25.051 -26.646 33.285 1.00 44.09  ? 120  ARG   A CD  1 
ATOM   924  N  NE  . ARG   A  1 145 ? -25.300 -27.615 34.343 1.00 55.06  ? 120  ARG   A NE  1 
ATOM   925  C  CZ  . ARG   A  1 145 ? -24.532 -28.665 34.600 1.00 51.82  ? 120  ARG   A CZ  1 
ATOM   926  N  NH1 . ARG   A  1 145 ? -23.469 -28.941 33.863 1.00 52.27  ? 120  ARG   A NH1 1 
ATOM   927  N  NH2 . ARG   A  1 145 ? -24.840 -29.457 35.623 1.00 58.95  ? 120  ARG   A NH2 1 
ATOM   928  N  N   . ALA   A  1 146 ? -27.075 -23.515 29.073 1.00 41.58  ? 121  ALA   A N   1 
ATOM   929  C  CA  . ALA   A  1 146 ? -26.859 -22.524 28.026 1.00 45.25  ? 121  ALA   A CA  1 
ATOM   930  C  C   . ALA   A  1 146 ? -27.924 -21.437 28.069 1.00 34.87  ? 121  ALA   A C   1 
ATOM   931  O  O   . ALA   A  1 146 ? -27.609 -20.248 27.943 1.00 39.89  ? 121  ALA   A O   1 
ATOM   932  C  CB  . ALA   A  1 146 ? -26.845 -23.205 26.658 1.00 33.70  ? 121  ALA   A CB  1 
ATOM   933  N  N   . ALA   A  1 147 ? -29.189 -21.820 28.254 1.00 39.01  ? 122  ALA   A N   1 
ATOM   934  C  CA  . ALA   A  1 147 ? -30.255 -20.824 28.251 1.00 36.06  ? 122  ALA   A CA  1 
ATOM   935  C  C   . ALA   A  1 147 ? -30.130 -19.873 29.435 1.00 41.77  ? 122  ALA   A C   1 
ATOM   936  O  O   . ALA   A  1 147 ? -30.407 -18.675 29.306 1.00 33.14  ? 122  ALA   A O   1 
ATOM   937  C  CB  . ALA   A  1 147 ? -31.619 -21.513 28.258 1.00 40.07  ? 122  ALA   A CB  1 
ATOM   938  N  N   . GLY   A  1 148 ? -29.707 -20.385 30.595 1.00 40.28  ? 123  GLY   A N   1 
ATOM   939  C  CA  . GLY   A  1 148 ? -29.472 -19.511 31.733 1.00 34.46  ? 123  GLY   A CA  1 
ATOM   940  C  C   . GLY   A  1 148 ? -28.320 -18.548 31.518 1.00 35.36  ? 123  GLY   A C   1 
ATOM   941  O  O   . GLY   A  1 148 ? -28.412 -17.370 31.874 1.00 32.11  ? 123  GLY   A O   1 
ATOM   942  N  N   . ILE   A  1 149 ? -27.213 -19.038 30.955 1.00 32.81  ? 124  ILE   A N   1 
ATOM   943  C  CA  . ILE   A  1 149 ? -26.083 -18.163 30.652 1.00 31.24  ? 124  ILE   A CA  1 
ATOM   944  C  C   . ILE   A  1 149 ? -26.496 -17.076 29.668 1.00 30.71  ? 124  ILE   A C   1 
ATOM   945  O  O   . ILE   A  1 149 ? -26.151 -15.900 29.839 1.00 29.63  ? 124  ILE   A O   1 
ATOM   946  C  CB  . ILE   A  1 149 ? -24.887 -18.985 30.137 1.00 35.09  ? 124  ILE   A CB  1 
ATOM   947  C  CG1 . ILE   A  1 149 ? -24.337 -19.871 31.256 1.00 42.53  ? 124  ILE   A CG1 1 
ATOM   948  C  CG2 . ILE   A  1 149 ? -23.795 -18.075 29.591 1.00 32.36  ? 124  ILE   A CG2 1 
ATOM   949  C  CD1 . ILE   A  1 149 ? -23.465 -21.008 30.771 1.00 41.12  ? 124  ILE   A CD1 1 
ATOM   950  N  N   . ILE   A  1 150 ? -27.239 -17.451 28.620 1.00 27.83  ? 125  ILE   A N   1 
ATOM   951  C  CA  . ILE   A  1 150 ? -27.697 -16.466 27.641 1.00 32.99  ? 125  ILE   A CA  1 
ATOM   952  C  C   . ILE   A  1 150 ? -28.570 -15.407 28.303 1.00 32.02  ? 125  ILE   A C   1 
ATOM   953  O  O   . ILE   A  1 150 ? -28.415 -14.206 28.046 1.00 25.96  ? 125  ILE   A O   1 
ATOM   954  C  CB  . ILE   A  1 150 ? -28.440 -17.165 26.485 1.00 32.21  ? 125  ILE   A CB  1 
ATOM   955  C  CG1 . ILE   A  1 150 ? -27.473 -18.022 25.666 1.00 28.19  ? 125  ILE   A CG1 1 
ATOM   956  C  CG2 . ILE   A  1 150 ? -29.160 -16.148 25.605 1.00 23.93  ? 125  ILE   A CG2 1 
ATOM   957  C  CD1 . ILE   A  1 150 ? -28.158 -18.985 24.720 1.00 29.05  ? 125  ILE   A CD1 1 
ATOM   958  N  N   . ALA   A  1 151 ? -29.488 -15.830 29.176 1.00 28.19  ? 126  ALA   A N   1 
ATOM   959  C  CA  . ALA   A  1 151 ? -30.331 -14.875 29.892 1.00 26.60  ? 126  ALA   A CA  1 
ATOM   960  C  C   . ALA   A  1 151 ? -29.488 -13.934 30.744 1.00 28.65  ? 126  ALA   A C   1 
ATOM   961  O  O   . ALA   A  1 151 ? -29.700 -12.715 30.745 1.00 29.37  ? 126  ALA   A O   1 
ATOM   962  C  CB  . ALA   A  1 151 ? -31.352 -15.621 30.752 1.00 27.37  ? 126  ALA   A CB  1 
ATOM   963  N  N   . ILE   A  1 152 ? -28.532 -14.492 31.489 1.00 32.51  ? 127  ILE   A N   1 
ATOM   964  C  CA  . ILE   A  1 152 ? -27.658 -13.685 32.338 1.00 34.32  ? 127  ILE   A CA  1 
ATOM   965  C  C   . ILE   A  1 152 ? -26.867 -12.690 31.498 1.00 24.42  ? 127  ILE   A C   1 
ATOM   966  O  O   . ILE   A  1 152 ? -26.719 -11.517 31.865 1.00 27.13  ? 127  ILE   A O   1 
ATOM   967  C  CB  . ILE   A  1 152 ? -26.731 -14.604 33.153 1.00 29.62  ? 127  ILE   A CB  1 
ATOM   968  C  CG1 . ILE   A  1 152 ? -27.528 -15.332 34.236 1.00 32.22  ? 127  ILE   A CG1 1 
ATOM   969  C  CG2 . ILE   A  1 152 ? -25.593 -13.805 33.776 1.00 27.93  ? 127  ILE   A CG2 1 
ATOM   970  C  CD1 . ILE   A  1 152 ? -26.736 -16.391 34.955 1.00 37.67  ? 127  ILE   A CD1 1 
ATOM   971  N  N   . CYS   A  1 153 ? -26.353 -13.142 30.353 1.00 23.02  ? 128  CYS   A N   1 
ATOM   972  C  CA  . CYS   A  1 153 ? -25.526 -12.280 29.514 1.00 28.82  ? 128  CYS   A CA  1 
ATOM   973  C  C   . CYS   A  1 153 ? -26.330 -11.123 28.932 1.00 26.03  ? 128  CYS   A C   1 
ATOM   974  O  O   . CYS   A  1 153 ? -25.804 -10.014 28.779 1.00 25.43  ? 128  CYS   A O   1 
ATOM   975  C  CB  . CYS   A  1 153 ? -24.871 -13.107 28.411 1.00 29.40  ? 128  CYS   A CB  1 
ATOM   976  S  SG  . CYS   A  1 153 ? -23.552 -14.181 29.027 1.00 34.85  ? 128  CYS   A SG  1 
ATOM   977  N  N   . TRP   A  1 154 ? -27.602 -11.355 28.593 1.00 26.74  ? 129  TRP   A N   1 
ATOM   978  C  CA  . TRP   A  1 154 ? -28.428 -10.257 28.098 1.00 28.00  ? 129  TRP   A CA  1 
ATOM   979  C  C   . TRP   A  1 154 ? -28.673 -9.216  29.183 1.00 27.31  ? 129  TRP   A C   1 
ATOM   980  O  O   . TRP   A  1 154 ? -28.658 -8.011  28.906 1.00 19.54  ? 129  TRP   A O   1 
ATOM   981  C  CB  . TRP   A  1 154 ? -29.753 -10.785 27.549 1.00 26.97  ? 129  TRP   A CB  1 
ATOM   982  C  CG  . TRP   A  1 154 ? -29.678 -11.192 26.109 1.00 29.15  ? 129  TRP   A CG  1 
ATOM   983  C  CD1 . TRP   A  1 154 ? -29.558 -12.457 25.614 1.00 29.05  ? 129  TRP   A CD1 1 
ATOM   984  C  CD2 . TRP   A  1 154 ? -29.711 -10.316 24.974 1.00 31.38  ? 129  TRP   A CD2 1 
ATOM   985  N  NE1 . TRP   A  1 154 ? -29.520 -12.424 24.237 1.00 30.83  ? 129  TRP   A NE1 1 
ATOM   986  C  CE2 . TRP   A  1 154 ? -29.610 -11.121 23.822 1.00 32.05  ? 129  TRP   A CE2 1 
ATOM   987  C  CE3 . TRP   A  1 154 ? -29.817 -8.930  24.822 1.00 23.67  ? 129  TRP   A CE3 1 
ATOM   988  C  CZ2 . TRP   A  1 154 ? -29.612 -10.585 22.533 1.00 30.97  ? 129  TRP   A CZ2 1 
ATOM   989  C  CZ3 . TRP   A  1 154 ? -29.821 -8.399  23.542 1.00 25.90  ? 129  TRP   A CZ3 1 
ATOM   990  C  CH2 . TRP   A  1 154 ? -29.719 -9.226  22.415 1.00 26.05  ? 129  TRP   A CH2 1 
ATOM   991  N  N   . VAL   A  1 155 ? -28.904 -9.658  30.422 1.00 23.77  ? 130  VAL   A N   1 
ATOM   992  C  CA  . VAL   A  1 155 ? -29.073 -8.714  31.523 1.00 25.61  ? 130  VAL   A CA  1 
ATOM   993  C  C   . VAL   A  1 155 ? -27.797 -7.905  31.724 1.00 18.75  ? 130  VAL   A C   1 
ATOM   994  O  O   . VAL   A  1 155 ? -27.835 -6.678  31.872 1.00 22.59  ? 130  VAL   A O   1 
ATOM   995  C  CB  . VAL   A  1 155 ? -29.483 -9.453  32.810 1.00 31.26  ? 130  VAL   A CB  1 
ATOM   996  C  CG1 . VAL   A  1 155 ? -29.453 -8.500  33.998 1.00 32.22  ? 130  VAL   A CG1 1 
ATOM   997  C  CG2 . VAL   A  1 155 ? -30.866 -10.069 32.652 1.00 28.21  ? 130  VAL   A CG2 1 
ATOM   998  N  N   . LEU   A  1 156 ? -26.644 -8.582  31.721 1.00 23.41  ? 131  LEU   A N   1 
ATOM   999  C  CA  . LEU   A  1 156 ? -25.372 -7.879  31.856 1.00 24.43  ? 131  LEU   A CA  1 
ATOM   1000 C  C   . LEU   A  1 156 ? -25.123 -6.937  30.685 1.00 25.06  ? 131  LEU   A C   1 
ATOM   1001 O  O   . LEU   A  1 156 ? -24.518 -5.874  30.864 1.00 23.10  ? 131  LEU   A O   1 
ATOM   1002 C  CB  . LEU   A  1 156 ? -24.225 -8.882  31.974 1.00 21.47  ? 131  LEU   A CB  1 
ATOM   1003 C  CG  . LEU   A  1 156 ? -24.207 -9.748  33.232 1.00 34.79  ? 131  LEU   A CG  1 
ATOM   1004 C  CD1 . LEU   A  1 156 ? -23.176 -10.857 33.098 1.00 33.25  ? 131  LEU   A CD1 1 
ATOM   1005 C  CD2 . LEU   A  1 156 ? -23.927 -8.891  34.456 1.00 34.70  ? 131  LEU   A CD2 1 
ATOM   1006 N  N   . SER   A  1 157 ? -25.573 -7.308  29.484 1.00 20.25  ? 132  SER   A N   1 
ATOM   1007 C  CA  . SER   A  1 157 ? -25.381 -6.438  28.328 1.00 19.64  ? 132  SER   A CA  1 
ATOM   1008 C  C   . SER   A  1 157 ? -26.204 -5.162  28.449 1.00 22.42  ? 132  SER   A C   1 
ATOM   1009 O  O   . SER   A  1 157 ? -25.745 -4.084  28.054 1.00 20.90  ? 132  SER   A O   1 
ATOM   1010 C  CB  . SER   A  1 157 ? -25.730 -7.188  27.044 1.00 20.27  ? 132  SER   A CB  1 
ATOM   1011 O  OG  . SER   A  1 157 ? -24.925 -8.345  26.911 1.00 22.32  ? 132  SER   A OG  1 
ATOM   1012 N  N   . PHE   A  1 158 ? -27.424 -5.260  28.986 1.00 22.42  ? 133  PHE   A N   1 
ATOM   1013 C  CA  . PHE   A  1 158 ? -28.199 -4.051  29.252 1.00 24.68  ? 133  PHE   A CA  1 
ATOM   1014 C  C   . PHE   A  1 158 ? -27.516 -3.181  30.301 1.00 20.84  ? 133  PHE   A C   1 
ATOM   1015 O  O   . PHE   A  1 158 ? -27.471 -1.953  30.166 1.00 25.17  ? 133  PHE   A O   1 
ATOM   1016 C  CB  . PHE   A  1 158 ? -29.619 -4.420  29.682 1.00 24.66  ? 133  PHE   A CB  1 
ATOM   1017 C  CG  . PHE   A  1 158 ? -30.569 -4.598  28.530 1.00 25.34  ? 133  PHE   A CG  1 
ATOM   1018 C  CD1 . PHE   A  1 158 ? -31.205 -3.501  27.970 1.00 26.28  ? 133  PHE   A CD1 1 
ATOM   1019 C  CD2 . PHE   A  1 158 ? -30.814 -5.852  27.997 1.00 28.64  ? 133  PHE   A CD2 1 
ATOM   1020 C  CE1 . PHE   A  1 158 ? -32.079 -3.654  26.904 1.00 27.80  ? 133  PHE   A CE1 1 
ATOM   1021 C  CE2 . PHE   A  1 158 ? -31.685 -6.012  26.930 1.00 27.40  ? 133  PHE   A CE2 1 
ATOM   1022 C  CZ  . PHE   A  1 158 ? -32.317 -4.910  26.383 1.00 26.84  ? 133  PHE   A CZ  1 
ATOM   1023 N  N   . ALA   A  1 159 ? -26.982 -3.798  31.357 1.00 20.82  ? 134  ALA   A N   1 
ATOM   1024 C  CA  . ALA   A  1 159 ? -26.338 -3.025  32.413 1.00 23.98  ? 134  ALA   A CA  1 
ATOM   1025 C  C   . ALA   A  1 159 ? -25.090 -2.321  31.893 1.00 23.55  ? 134  ALA   A C   1 
ATOM   1026 O  O   . ALA   A  1 159 ? -24.859 -1.144  32.193 1.00 23.41  ? 134  ALA   A O   1 
ATOM   1027 C  CB  . ALA   A  1 159 ? -25.991 -3.932  33.593 1.00 24.07  ? 134  ALA   A CB  1 
ATOM   1028 N  N   . ILE   A  1 160 ? -24.280 -3.027  31.103 1.00 22.02  ? 135  ILE   A N   1 
ATOM   1029 C  CA  . ILE   A  1 160 ? -23.066 -2.439  30.545 1.00 19.24  ? 135  ILE   A CA  1 
ATOM   1030 C  C   . ILE   A  1 160 ? -23.411 -1.366  29.518 1.00 23.14  ? 135  ILE   A C   1 
ATOM   1031 O  O   . ILE   A  1 160 ? -22.879 -0.251  29.557 1.00 19.93  ? 135  ILE   A O   1 
ATOM   1032 C  CB  . ILE   A  1 160 ? -22.177 -3.537  29.933 1.00 20.06  ? 135  ILE   A CB  1 
ATOM   1033 C  CG1 . ILE   A  1 160 ? -21.522 -4.373  31.032 1.00 26.56  ? 135  ILE   A CG1 1 
ATOM   1034 C  CG2 . ILE   A  1 160 ? -21.119 -2.926  29.022 1.00 24.52  ? 135  ILE   A CG2 1 
ATOM   1035 C  CD1 . ILE   A  1 160 ? -20.870 -5.648  30.517 1.00 25.37  ? 135  ILE   A CD1 1 
ATOM   1036 N  N   . GLY   A  1 161 ? -24.294 -1.693  28.572 1.00 21.31  ? 136  GLY   A N   1 
ATOM   1037 C  CA  . GLY   A  1 161 ? -24.574 -0.771  27.484 1.00 20.62  ? 136  GLY   A CA  1 
ATOM   1038 C  C   . GLY   A  1 161 ? -25.355 0.460   27.900 1.00 21.05  ? 136  GLY   A C   1 
ATOM   1039 O  O   . GLY   A  1 161 ? -25.208 1.523   27.290 1.00 18.85  ? 136  GLY   A O   1 
ATOM   1040 N  N   . LEU   A  1 162 ? -26.179 0.348   28.939 1.00 20.07  ? 137  LEU   A N   1 
ATOM   1041 C  CA  . LEU   A  1 162 ? -26.948 1.482   29.432 1.00 24.62  ? 137  LEU   A CA  1 
ATOM   1042 C  C   . LEU   A  1 162 ? -26.334 2.129   30.669 1.00 20.79  ? 137  LEU   A C   1 
ATOM   1043 O  O   . LEU   A  1 162 ? -27.003 2.930   31.328 1.00 18.95  ? 137  LEU   A O   1 
ATOM   1044 C  CB  . LEU   A  1 162 ? -28.394 1.067   29.718 1.00 23.47  ? 137  LEU   A CB  1 
ATOM   1045 C  CG  . LEU   A  1 162 ? -29.163 0.495   28.522 1.00 21.85  ? 137  LEU   A CG  1 
ATOM   1046 C  CD1 . LEU   A  1 162 ? -30.597 0.155   28.912 1.00 22.92  ? 137  LEU   A CD1 1 
ATOM   1047 C  CD2 . LEU   A  1 162 ? -29.124 1.441   27.327 1.00 21.03  ? 137  LEU   A CD2 1 
ATOM   1048 N  N   . THR   A  1 163 ? -25.096 1.781   31.015 1.00 23.11  ? 138  THR   A N   1 
ATOM   1049 C  CA  . THR   A  1 163 ? -24.412 2.463   32.113 1.00 24.39  ? 138  THR   A CA  1 
ATOM   1050 C  C   . THR   A  1 163 ? -24.458 3.988   32.018 1.00 26.41  ? 138  THR   A C   1 
ATOM   1051 O  O   . THR   A  1 163 ? -24.622 4.634   33.069 1.00 23.03  ? 138  THR   A O   1 
ATOM   1052 C  CB  . THR   A  1 163 ? -22.959 1.963   32.191 1.00 25.11  ? 138  THR   A CB  1 
ATOM   1053 O  OG1 . THR   A  1 163 ? -22.916 0.735   32.926 1.00 26.70  ? 138  THR   A OG1 1 
ATOM   1054 C  CG2 . THR   A  1 163 ? -22.051 2.987   32.869 1.00 20.92  ? 138  THR   A CG2 1 
ATOM   1055 N  N   . PRO   A  1 164 ? -24.355 4.622   30.841 1.00 20.79  ? 139  PRO   A N   1 
ATOM   1056 C  CA  . PRO   A  1 164 ? -24.540 6.081   30.798 1.00 21.28  ? 139  PRO   A CA  1 
ATOM   1057 C  C   . PRO   A  1 164 ? -25.876 6.539   31.351 1.00 25.53  ? 139  PRO   A C   1 
ATOM   1058 O  O   . PRO   A  1 164 ? -25.956 7.637   31.917 1.00 21.49  ? 139  PRO   A O   1 
ATOM   1059 C  CB  . PRO   A  1 164 ? -24.400 6.397   29.304 1.00 17.59  ? 139  PRO   A CB  1 
ATOM   1060 C  CG  . PRO   A  1 164 ? -23.422 5.370   28.849 1.00 17.57  ? 139  PRO   A CG  1 
ATOM   1061 C  CD  . PRO   A  1 164 ? -23.941 4.124   29.516 1.00 19.35  ? 139  PRO   A CD  1 
ATOM   1062 N  N   . MET   A  1 165 ? -26.927 5.726   31.212 1.00 24.58  ? 140  MET   A N   1 
ATOM   1063 C  CA  A MET   A  1 165 ? -28.225 6.103   31.758 0.54 25.12  ? 140  MET   A CA  1 
ATOM   1064 C  CA  B MET   A  1 165 ? -28.232 6.080   31.762 0.46 25.13  ? 140  MET   A CA  1 
ATOM   1065 C  C   . MET   A  1 165 ? -28.229 6.113   33.282 1.00 28.71  ? 140  MET   A C   1 
ATOM   1066 O  O   . MET   A  1 165 ? -29.142 6.690   33.880 1.00 24.51  ? 140  MET   A O   1 
ATOM   1067 C  CB  A MET   A  1 165 ? -29.310 5.160   31.231 0.54 22.56  ? 140  MET   A CB  1 
ATOM   1068 C  CB  B MET   A  1 165 ? -29.298 5.096   31.276 0.46 22.55  ? 140  MET   A CB  1 
ATOM   1069 C  CG  A MET   A  1 165 ? -29.352 5.070   29.709 0.54 25.73  ? 140  MET   A CG  1 
ATOM   1070 C  CG  B MET   A  1 165 ? -29.293 4.864   29.779 0.46 26.40  ? 140  MET   A CG  1 
ATOM   1071 S  SD  A MET   A  1 165 ? -30.906 4.420   29.065 0.54 25.60  ? 140  MET   A SD  1 
ATOM   1072 S  SD  B MET   A  1 165 ? -30.192 6.152   28.904 0.46 27.21  ? 140  MET   A SD  1 
ATOM   1073 C  CE  A MET   A  1 165 ? -32.010 5.792   29.394 0.54 31.02  ? 140  MET   A CE  1 
ATOM   1074 C  CE  B MET   A  1 165 ? -31.863 5.849   29.475 0.46 31.07  ? 140  MET   A CE  1 
ATOM   1075 N  N   A LEU   A  1 166 ? -27.237 5.494   33.919 0.67 23.58  ? 141  LEU   A N   1 
ATOM   1076 N  N   B LEU   A  1 166 ? -27.231 5.505   33.920 0.33 23.68  ? 141  LEU   A N   1 
ATOM   1077 C  CA  A LEU   A  1 166 ? -27.120 5.505   35.370 0.67 24.48  ? 141  LEU   A CA  1 
ATOM   1078 C  CA  B LEU   A  1 166 ? -27.114 5.507   35.371 0.33 24.58  ? 141  LEU   A CA  1 
ATOM   1079 C  C   A LEU   A  1 166 ? -26.393 6.737   35.893 0.67 29.58  ? 141  LEU   A C   1 
ATOM   1080 C  C   B LEU   A  1 166 ? -26.406 6.747   35.899 0.33 29.44  ? 141  LEU   A C   1 
ATOM   1081 O  O   A LEU   A  1 166 ? -26.140 6.823   37.099 0.67 29.30  ? 141  LEU   A O   1 
ATOM   1082 O  O   B LEU   A  1 166 ? -26.181 6.850   37.109 0.33 29.21  ? 141  LEU   A O   1 
ATOM   1083 C  CB  A LEU   A  1 166 ? -26.411 4.235   35.854 0.67 27.11  ? 141  LEU   A CB  1 
ATOM   1084 C  CB  B LEU   A  1 166 ? -26.381 4.245   35.842 0.33 27.07  ? 141  LEU   A CB  1 
ATOM   1085 C  CG  A LEU   A  1 166 ? -26.918 2.918   35.259 0.67 29.20  ? 141  LEU   A CG  1 
ATOM   1086 C  CG  B LEU   A  1 166 ? -27.248 3.006   36.096 0.33 26.82  ? 141  LEU   A CG  1 
ATOM   1087 C  CD1 A LEU   A  1 166 ? -26.208 1.730   35.886 0.67 26.32  ? 141  LEU   A CD1 1 
ATOM   1088 C  CD1 B LEU   A  1 166 ? -27.842 2.466   34.802 0.33 29.85  ? 141  LEU   A CD1 1 
ATOM   1089 C  CD2 A LEU   A  1 166 ? -28.422 2.793   35.433 0.67 30.20  ? 141  LEU   A CD2 1 
ATOM   1090 C  CD2 B LEU   A  1 166 ? -26.448 1.926   36.806 0.33 26.50  ? 141  LEU   A CD2 1 
ATOM   1091 N  N   . GLY   A  1 167 ? -26.050 7.682   35.023 1.00 21.80  ? 142  GLY   A N   1 
ATOM   1092 C  CA  . GLY   A  1 167 ? -25.465 8.948   35.425 1.00 24.45  ? 142  GLY   A CA  1 
ATOM   1093 C  C   . GLY   A  1 167 ? -24.132 9.280   34.787 1.00 24.44  ? 142  GLY   A C   1 
ATOM   1094 O  O   . GLY   A  1 167 ? -23.667 10.420  34.917 1.00 23.90  ? 142  GLY   A O   1 
ATOM   1095 N  N   . TRP   A  1 168 ? -23.501 8.325   34.102 1.00 24.78  ? 143  TRP   A N   1 
ATOM   1096 C  CA  . TRP   A  1 168 ? -22.233 8.582   33.417 1.00 21.42  ? 143  TRP   A CA  1 
ATOM   1097 C  C   . TRP   A  1 168 ? -22.561 9.121   32.028 1.00 23.38  ? 143  TRP   A C   1 
ATOM   1098 O  O   . TRP   A  1 168 ? -22.467 8.427   31.014 1.00 21.44  ? 143  TRP   A O   1 
ATOM   1099 C  CB  . TRP   A  1 168 ? -21.372 7.325   33.362 1.00 20.94  ? 143  TRP   A CB  1 
ATOM   1100 C  CG  . TRP   A  1 168 ? -19.941 7.604   32.980 1.00 26.39  ? 143  TRP   A CG  1 
ATOM   1101 C  CD1 . TRP   A  1 168 ? -19.410 8.808   32.611 1.00 23.57  ? 143  TRP   A CD1 1 
ATOM   1102 C  CD2 . TRP   A  1 168 ? -18.860 6.662   32.944 1.00 20.51  ? 143  TRP   A CD2 1 
ATOM   1103 N  NE1 . TRP   A  1 168 ? -18.070 8.671   32.340 1.00 21.02  ? 143  TRP   A NE1 1 
ATOM   1104 C  CE2 . TRP   A  1 168 ? -17.707 7.365   32.537 1.00 24.10  ? 143  TRP   A CE2 1 
ATOM   1105 C  CE3 . TRP   A  1 168 ? -18.756 5.294   33.212 1.00 19.18  ? 143  TRP   A CE3 1 
ATOM   1106 C  CZ2 . TRP   A  1 168 ? -16.466 6.745   32.394 1.00 22.78  ? 143  TRP   A CZ2 1 
ATOM   1107 C  CZ3 . TRP   A  1 168 ? -17.522 4.680   33.067 1.00 21.04  ? 143  TRP   A CZ3 1 
ATOM   1108 C  CH2 . TRP   A  1 168 ? -16.394 5.405   32.664 1.00 21.24  ? 143  TRP   A CH2 1 
ATOM   1109 N  N   . ASN   A  1 169 ? -22.939 10.394  31.987 1.00 25.42  ? 144  ASN   A N   1 
ATOM   1110 C  CA  . ASN   A  1 169 ? -23.421 11.001  30.756 1.00 27.61  ? 144  ASN   A CA  1 
ATOM   1111 C  C   . ASN   A  1 169 ? -23.144 12.497  30.804 1.00 23.23  ? 144  ASN   A C   1 
ATOM   1112 O  O   . ASN   A  1 169 ? -22.752 13.043  31.838 1.00 28.82  ? 144  ASN   A O   1 
ATOM   1113 C  CB  . ASN   A  1 169 ? -24.907 10.681  30.538 1.00 22.43  ? 144  ASN   A CB  1 
ATOM   1114 C  CG  . ASN   A  1 169 ? -25.810 11.273  31.616 1.00 27.87  ? 144  ASN   A CG  1 
ATOM   1115 O  OD1 . ASN   A  1 169 ? -25.843 12.484  31.828 1.00 28.45  ? 144  ASN   A OD1 1 
ATOM   1116 N  ND2 . ASN   A  1 169 ? -26.545 10.406  32.307 1.00 21.34  ? 144  ASN   A ND2 1 
ATOM   1117 N  N   . ASN   A  1 170 ? -23.357 13.162  29.667 1.00 24.37  ? 145  ASN   A N   1 
ATOM   1118 C  CA  . ASN   A  1 170 ? -23.146 14.600  29.572 1.00 24.26  ? 145  ASN   A CA  1 
ATOM   1119 C  C   . ASN   A  1 170 ? -24.439 15.401  29.642 1.00 26.66  ? 145  ASN   A C   1 
ATOM   1120 O  O   . ASN   A  1 170 ? -24.464 16.557  29.206 1.00 29.33  ? 145  ASN   A O   1 
ATOM   1121 C  CB  . ASN   A  1 170 ? -22.400 14.942  28.283 1.00 22.54  ? 145  ASN   A CB  1 
ATOM   1122 C  CG  . ASN   A  1 170 ? -21.023 14.318  28.224 1.00 33.66  ? 145  ASN   A CG  1 
ATOM   1123 O  OD1 . ASN   A  1 170 ? -20.360 14.152  29.246 1.00 34.37  ? 145  ASN   A OD1 1 
ATOM   1124 N  ND2 . ASN   A  1 170 ? -20.585 13.967  27.020 1.00 36.60  ? 145  ASN   A ND2 1 
ATOM   1125 N  N   . CYS   A  1 171 ? -25.505 14.829  30.199 1.00 25.59  ? 146  CYS   A N   1 
ATOM   1126 C  CA  . CYS   A  1 171 ? -26.766 15.556  30.247 1.00 27.08  ? 146  CYS   A CA  1 
ATOM   1127 C  C   . CYS   A  1 171 ? -26.691 16.719  31.227 1.00 35.89  ? 146  CYS   A C   1 
ATOM   1128 O  O   . CYS   A  1 171 ? -27.437 17.692  31.076 1.00 35.81  ? 146  CYS   A O   1 
ATOM   1129 C  CB  . CYS   A  1 171 ? -27.925 14.617  30.593 1.00 30.92  ? 146  CYS   A CB  1 
ATOM   1130 S  SG  . CYS   A  1 171 ? -28.331 13.427  29.271 1.00 35.02  ? 146  CYS   A SG  1 
ATOM   1131 N  N   . GLY   A  1 172 ? -25.797 16.640  32.218 1.00 32.68  ? 147  GLY   A N   1 
ATOM   1132 C  CA  . GLY   A  1 172 ? -25.594 17.744  33.140 1.00 34.29  ? 147  GLY   A CA  1 
ATOM   1133 C  C   . GLY   A  1 172 ? -24.962 18.976  32.523 1.00 38.61  ? 147  GLY   A C   1 
ATOM   1134 O  O   . GLY   A  1 172 ? -25.085 20.066  33.093 1.00 46.59  ? 147  GLY   A O   1 
ATOM   1135 N  N   . GLN   A  1 173 ? -24.288 18.839  31.379 1.00 33.69  ? 148  GLN   A N   1 
ATOM   1136 C  CA  . GLN   A  1 173 ? -23.620 19.966  30.719 1.00 38.89  ? 148  GLN   A CA  1 
ATOM   1137 C  C   . GLN   A  1 173 ? -24.097 20.062  29.272 1.00 33.87  ? 148  GLN   A C   1 
ATOM   1138 O  O   . GLN   A  1 173 ? -23.320 19.867  28.333 1.00 38.12  ? 148  GLN   A O   1 
ATOM   1139 C  CB  . GLN   A  1 173 ? -22.092 19.882  30.773 1.00 53.36  ? 148  GLN   A CB  1 
ATOM   1140 C  CG  . GLN   A  1 173 ? -21.423 19.423  32.068 1.00 59.56  ? 148  GLN   A CG  1 
ATOM   1141 C  CD  . GLN   A  1 173 ? -21.150 17.939  32.132 1.00 75.04  ? 148  GLN   A CD  1 
ATOM   1142 O  OE1 . GLN   A  1 173 ? -20.737 17.328  31.146 1.00 72.82  ? 148  GLN   A OE1 1 
ATOM   1143 N  NE2 . GLN   A  1 173 ? -21.311 17.362  33.315 1.00 79.67  ? 148  GLN   A NE2 1 
ATOM   1144 N  N   . PRO   A  1 174 ? -25.386 20.345  29.055 1.00 39.32  ? 149  PRO   A N   1 
ATOM   1145 C  CA  . PRO   A  1 174 ? -25.909 20.375  27.685 1.00 33.97  ? 149  PRO   A CA  1 
ATOM   1146 C  C   . PRO   A  1 174 ? -25.263 21.483  26.865 1.00 42.04  ? 149  PRO   A C   1 
ATOM   1147 O  O   . PRO   A  1 174 ? -24.884 22.535  27.384 1.00 39.77  ? 149  PRO   A O   1 
ATOM   1148 C  CB  . PRO   A  1 174 ? -27.408 20.626  27.892 1.00 42.34  ? 149  PRO   A CB  1 
ATOM   1149 C  CG  . PRO   A  1 174 ? -27.482 21.362  29.166 1.00 41.44  ? 149  PRO   A CG  1 
ATOM   1150 C  CD  . PRO   A  1 174 ? -26.418 20.741  30.032 1.00 37.08  ? 149  PRO   A CD  1 
ATOM   1151 N  N   . LYS   A  1 175 ? -25.137 21.247  25.564 1.00 35.29  ? 150  LYS   A N   1 
ATOM   1152 C  CA  . LYS   A  1 175 ? -24.728 22.306  24.639 1.00 39.44  ? 150  LYS   A CA  1 
ATOM   1153 C  C   . LYS   A  1 175 ? -25.927 23.202  24.353 1.00 45.97  ? 150  LYS   A C   1 
ATOM   1154 O  O   . LYS   A  1 175 ? -26.710 22.948  23.433 1.00 37.32  ? 150  LYS   A O   1 
ATOM   1155 C  CB  . LYS   A  1 175 ? -24.154 21.710  23.358 1.00 40.11  ? 150  LYS   A CB  1 
ATOM   1156 C  CG  . LYS   A  1 175 ? -22.878 20.890  23.532 1.00 46.97  ? 150  LYS   A CG  1 
ATOM   1157 C  CD  . LYS   A  1 175 ? -22.129 20.759  22.238 1.00 41.65  ? 150  LYS   A CD  1 
ATOM   1158 C  CE  . LYS   A  1 175 ? -20.982 19.797  22.365 1.00 57.60  ? 150  LYS   A CE  1 
ATOM   1159 N  NZ  . LYS   A  1 175 ? -19.996 20.190  23.357 1.00 57.62  ? 150  LYS   A NZ  1 
ATOM   1160 N  N   . GLU   A  1 176 ? -26.070 24.267  25.144 1.00 50.20  ? 151  GLU   A N   1 
ATOM   1161 C  CA  . GLU   A  1 176 ? -27.241 25.134  25.036 1.00 53.98  ? 151  GLU   A CA  1 
ATOM   1162 C  C   . GLU   A  1 176 ? -27.252 25.944  23.744 1.00 47.09  ? 151  GLU   A C   1 
ATOM   1163 O  O   . GLU   A  1 176 ? -28.327 26.221  23.200 1.00 53.73  ? 151  GLU   A O   1 
ATOM   1164 C  CB  . GLU   A  1 176 ? -27.336 26.046  26.258 1.00 56.32  ? 151  GLU   A CB  1 
ATOM   1165 C  CG  . GLU   A  1 176 ? -27.850 25.323  27.498 1.00 49.63  ? 151  GLU   A CG  1 
ATOM   1166 C  CD  . GLU   A  1 176 ? -29.226 24.685  27.297 1.00 59.16  ? 151  GLU   A CD  1 
ATOM   1167 O  OE1 . GLU   A  1 176 ? -29.970 25.098  26.380 1.00 71.30  ? 151  GLU   A OE1 1 
ATOM   1168 O  OE2 . GLU   A  1 176 ? -29.559 23.752  28.058 1.00 60.90  ? 151  GLU   A OE2 1 
ATOM   1169 N  N   . GLY   A  1 177 ? -26.084 26.349  23.249 1.00 45.85  ? 152  GLY   A N   1 
ATOM   1170 C  CA  . GLY   A  1 177 ? -26.057 27.112  22.013 1.00 54.36  ? 152  GLY   A CA  1 
ATOM   1171 C  C   . GLY   A  1 177 ? -26.520 26.279  20.833 1.00 56.32  ? 152  GLY   A C   1 
ATOM   1172 O  O   . GLY   A  1 177 ? -27.224 26.775  19.947 1.00 50.28  ? 152  GLY   A O   1 
ATOM   1173 N  N   . LYS   A  1 178 ? -26.135 25.001  20.801 1.00 43.87  ? 153  LYS   A N   1 
ATOM   1174 C  CA  . LYS   A  1 178 ? -26.625 24.128  19.740 1.00 40.72  ? 153  LYS   A CA  1 
ATOM   1175 C  C   . LYS   A  1 178 ? -28.116 23.869  19.912 1.00 44.45  ? 153  LYS   A C   1 
ATOM   1176 O  O   . LYS   A  1 178 ? -28.867 23.834  18.930 1.00 40.16  ? 153  LYS   A O   1 
ATOM   1177 C  CB  . LYS   A  1 178 ? -25.858 22.805  19.727 1.00 50.57  ? 153  LYS   A CB  1 
ATOM   1178 C  CG  . LYS   A  1 178 ? -26.084 21.985  18.465 1.00 53.03  ? 153  LYS   A CG  1 
ATOM   1179 C  CD  . LYS   A  1 178 ? -24.798 21.408  17.879 1.00 65.24  ? 153  LYS   A CD  1 
ATOM   1180 C  CE  . LYS   A  1 178 ? -24.158 20.416  18.840 1.00 42.13  ? 153  LYS   A CE  1 
ATOM   1181 N  NZ  . LYS   A  1 178 ? -22.753 20.066  18.488 1.00 48.99  ? 153  LYS   A NZ  1 
ATOM   1182 N  N   . ALA   A  1 179 ? -28.558 23.666  21.158 1.00 34.96  ? 154  ALA   A N   1 
ATOM   1183 C  CA  . ALA   A  1 179 ? -29.980 23.476  21.426 1.00 45.16  ? 154  ALA   A CA  1 
ATOM   1184 C  C   . ALA   A  1 179 ? -30.790 24.713  21.056 1.00 52.61  ? 154  ALA   A C   1 
ATOM   1185 O  O   . ALA   A  1 179 ? -31.857 24.601  20.441 1.00 44.06  ? 154  ALA   A O   1 
ATOM   1186 C  CB  . ALA   A  1 179 ? -30.191 23.122  22.897 1.00 34.93  ? 154  ALA   A CB  1 
ATOM   1187 N  N   . HIS   A  1 180 ? -30.305 25.904  21.425 1.00 43.09  ? 155  HIS   A N   1 
ATOM   1188 C  CA  . HIS   A  1 180 ? -31.037 27.125  21.100 1.00 54.81  ? 155  HIS   A CA  1 
ATOM   1189 C  C   . HIS   A  1 180 ? -31.062 27.364  19.597 1.00 48.76  ? 155  HIS   A C   1 
ATOM   1190 O  O   . HIS   A  1 180 ? -32.059 27.856  19.058 1.00 59.18  ? 155  HIS   A O   1 
ATOM   1191 C  CB  . HIS   A  1 180 ? -30.425 28.327  21.819 1.00 50.65  ? 155  HIS   A CB  1 
ATOM   1192 C  CG  . HIS   A  1 180 ? -30.723 28.372  23.285 1.00 52.08  ? 155  HIS   A CG  1 
ATOM   1193 N  ND1 . HIS   A  1 180 ? -31.941 27.997  23.810 1.00 58.74  ? 155  HIS   A ND1 1 
ATOM   1194 C  CD2 . HIS   A  1 180 ? -29.975 28.788  24.334 1.00 52.93  ? 155  HIS   A CD2 1 
ATOM   1195 C  CE1 . HIS   A  1 180 ? -31.921 28.154  25.122 1.00 67.67  ? 155  HIS   A CE1 1 
ATOM   1196 N  NE2 . HIS   A  1 180 ? -30.740 28.636  25.465 1.00 65.90  ? 155  HIS   A NE2 1 
ATOM   1197 N  N   A SER   A  1 181 ? -29.973 27.021  18.904 0.61 46.56  ? 156  SER   A N   1 
ATOM   1198 N  N   B SER   A  1 181 ? -29.972 27.020  18.905 0.39 46.67  ? 156  SER   A N   1 
ATOM   1199 C  CA  A SER   A  1 181 ? -29.923 27.221  17.460 0.61 49.03  ? 156  SER   A CA  1 
ATOM   1200 C  CA  B SER   A  1 181 ? -29.917 27.216  17.461 0.39 49.07  ? 156  SER   A CA  1 
ATOM   1201 C  C   A SER   A  1 181 ? -30.956 26.368  16.738 0.61 50.87  ? 156  SER   A C   1 
ATOM   1202 C  C   B SER   A  1 181 ? -30.951 26.366  16.737 0.39 50.84  ? 156  SER   A C   1 
ATOM   1203 O  O   A SER   A  1 181 ? -31.477 26.777  15.695 0.61 51.25  ? 156  SER   A O   1 
ATOM   1204 O  O   B SER   A  1 181 ? -31.468 26.774  15.691 0.39 51.24  ? 156  SER   A O   1 
ATOM   1205 C  CB  A SER   A  1 181 ? -28.521 26.914  16.935 0.61 50.05  ? 156  SER   A CB  1 
ATOM   1206 C  CB  B SER   A  1 181 ? -28.514 26.898  16.941 0.39 50.08  ? 156  SER   A CB  1 
ATOM   1207 O  OG  A SER   A  1 181 ? -28.154 25.575  17.219 0.61 53.06  ? 156  SER   A OG  1 
ATOM   1208 O  OG  B SER   A  1 181 ? -28.428 27.109  15.543 0.39 54.08  ? 156  SER   A OG  1 
ATOM   1209 N  N   . GLN   A  1 182 ? -31.265 25.188  17.271 1.00 53.54  ? 157  GLN   A N   1 
ATOM   1210 C  CA  . GLN   A  1 182 ? -32.247 24.298  16.672 1.00 47.59  ? 157  GLN   A CA  1 
ATOM   1211 C  C   . GLN   A  1 182 ? -33.637 24.462  17.270 1.00 46.93  ? 157  GLN   A C   1 
ATOM   1212 O  O   . GLN   A  1 182 ? -34.507 23.620  17.020 1.00 49.51  ? 157  GLN   A O   1 
ATOM   1213 C  CB  . GLN   A  1 182 ? -31.789 22.844  16.803 1.00 46.97  ? 157  GLN   A CB  1 
ATOM   1214 C  CG  . GLN   A  1 182 ? -30.439 22.577  16.169 1.00 52.01  ? 157  GLN   A CG  1 
ATOM   1215 C  CD  . GLN   A  1 182 ? -30.265 21.132  15.762 1.00 73.15  ? 157  GLN   A CD  1 
ATOM   1216 O  OE1 . GLN   A  1 182 ? -29.495 20.392  16.369 1.00 73.06  ? 157  GLN   A OE1 1 
ATOM   1217 N  NE2 . GLN   A  1 182 ? -30.988 20.718  14.728 1.00 79.45  ? 157  GLN   A NE2 1 
ATOM   1218 N  N   . GLY   A  1 183 ? -33.870 25.521  18.043 1.00 50.89  ? 158  GLY   A N   1 
ATOM   1219 C  CA  . GLY   A  1 183 ? -35.196 25.741  18.580 1.00 46.08  ? 158  GLY   A CA  1 
ATOM   1220 C  C   . GLY   A  1 183 ? -35.645 24.708  19.583 1.00 47.28  ? 158  GLY   A C   1 
ATOM   1221 O  O   . GLY   A  1 183 ? -36.850 24.538  19.783 1.00 52.23  ? 158  GLY   A O   1 
ATOM   1222 N  N   . CYS   A  1 184 ? -34.711 24.011  20.223 1.00 39.81  ? 159  CYS   A N   1 
ATOM   1223 C  CA  . CYS   A  1 184 ? -35.079 22.977  21.176 1.00 36.22  ? 159  CYS   A CA  1 
ATOM   1224 C  C   . CYS   A  1 184 ? -35.782 23.575  22.391 1.00 44.61  ? 159  CYS   A C   1 
ATOM   1225 O  O   . CYS   A  1 184 ? -35.545 24.722  22.779 1.00 49.51  ? 159  CYS   A O   1 
ATOM   1226 C  CB  . CYS   A  1 184 ? -33.836 22.207  21.622 1.00 39.86  ? 159  CYS   A CB  1 
ATOM   1227 S  SG  . CYS   A  1 184 ? -33.034 21.247  20.312 1.00 40.06  ? 159  CYS   A SG  1 
ATOM   1228 N  N   . GLY   A  1 185 ? -36.646 22.767  22.998 1.00 49.95  ? 160  GLY   A N   1 
ATOM   1229 C  CA  . GLY   A  1 185 ? -37.402 23.166  24.164 1.00 45.94  ? 160  GLY   A CA  1 
ATOM   1230 C  C   . GLY   A  1 185 ? -36.600 23.043  25.441 1.00 60.54  ? 160  GLY   A C   1 
ATOM   1231 O  O   . GLY   A  1 185 ? -35.429 22.664  25.450 1.00 52.05  ? 160  GLY   A O   1 
ATOM   1232 N  N   . GLU   A  1 186 ? -37.250 23.388  26.550 1.00 58.17  ? 161  GLU   A N   1 
ATOM   1233 C  CA  . GLU   A  1 186 ? -36.573 23.327  27.835 1.00 61.22  ? 161  GLU   A CA  1 
ATOM   1234 C  C   . GLU   A  1 186 ? -36.344 21.874  28.224 1.00 55.58  ? 161  GLU   A C   1 
ATOM   1235 O  O   . GLU   A  1 186 ? -37.223 21.023  28.062 1.00 58.11  ? 161  GLU   A O   1 
ATOM   1236 C  CB  . GLU   A  1 186 ? -37.412 24.015  28.913 1.00 72.95  ? 161  GLU   A CB  1 
ATOM   1237 C  CG  . GLU   A  1 186 ? -37.977 25.369  28.522 1.00 89.53  ? 161  GLU   A CG  1 
ATOM   1238 C  CD  . GLU   A  1 186 ? -37.036 26.511  28.847 1.00 106.45 ? 161  GLU   A CD  1 
ATOM   1239 O  OE1 . GLU   A  1 186 ? -37.142 27.069  29.960 1.00 103.94 ? 161  GLU   A OE1 1 
ATOM   1240 O  OE2 . GLU   A  1 186 ? -36.196 26.853  27.989 1.00 107.07 ? 161  GLU   A OE2 1 
ATOM   1241 N  N   . GLY   A  1 187 ? -35.148 21.589  28.731 1.00 53.37  ? 162  GLY   A N   1 
ATOM   1242 C  CA  . GLY   A  1 187 ? -34.780 20.223  29.022 1.00 48.86  ? 162  GLY   A CA  1 
ATOM   1243 C  C   . GLY   A  1 187 ? -34.403 19.390  27.819 1.00 47.24  ? 162  GLY   A C   1 
ATOM   1244 O  O   . GLY   A  1 187 ? -34.143 18.190  27.978 1.00 48.76  ? 162  GLY   A O   1 
ATOM   1245 N  N   . GLN   A  1 188 ? -34.349 19.977  26.626 1.00 44.25  ? 163  GLN   A N   1 
ATOM   1246 C  CA  . GLN   A  1 188 ? -33.988 19.246  25.422 1.00 40.38  ? 163  GLN   A CA  1 
ATOM   1247 C  C   . GLN   A  1 188 ? -32.603 19.645  24.934 1.00 45.64  ? 163  GLN   A C   1 
ATOM   1248 O  O   . GLN   A  1 188 ? -32.129 20.758  25.179 1.00 42.89  ? 163  GLN   A O   1 
ATOM   1249 C  CB  . GLN   A  1 188 ? -34.999 19.504  24.300 1.00 38.48  ? 163  GLN   A CB  1 
ATOM   1250 C  CG  . GLN   A  1 188 ? -36.399 18.995  24.564 1.00 35.70  ? 163  GLN   A CG  1 
ATOM   1251 C  CD  . GLN   A  1 188 ? -37.280 19.095  23.336 1.00 40.05  ? 163  GLN   A CD  1 
ATOM   1252 O  OE1 . GLN   A  1 188 ? -37.147 20.023  22.536 1.00 43.35  ? 163  GLN   A OE1 1 
ATOM   1253 N  NE2 . GLN   A  1 188 ? -38.192 18.144  23.182 1.00 42.72  ? 163  GLN   A NE2 1 
ATOM   1254 N  N   . VAL   A  1 189 ? -31.965 18.713  24.228 1.00 31.50  ? 164  VAL   A N   1 
ATOM   1255 C  CA  . VAL   A  1 189 ? -30.682 18.932  23.579 1.00 34.54  ? 164  VAL   A CA  1 
ATOM   1256 C  C   . VAL   A  1 189 ? -30.814 18.531  22.119 1.00 30.47  ? 164  VAL   A C   1 
ATOM   1257 O  O   . VAL   A  1 189 ? -31.717 17.785  21.734 1.00 28.48  ? 164  VAL   A O   1 
ATOM   1258 C  CB  . VAL   A  1 189 ? -29.539 18.135  24.245 1.00 33.85  ? 164  VAL   A CB  1 
ATOM   1259 C  CG1 . VAL   A  1 189 ? -29.364 18.558  25.692 1.00 33.30  ? 164  VAL   A CG1 1 
ATOM   1260 C  CG2 . VAL   A  1 189 ? -29.807 16.641  24.148 1.00 30.65  ? 164  VAL   A CG2 1 
ATOM   1261 N  N   . ALA   A  1 190 ? -29.900 19.039  21.300 1.00 23.57  ? 165  ALA   A N   1 
ATOM   1262 C  CA  . ALA   A  1 190 ? -29.706 18.453  19.982 1.00 31.19  ? 165  ALA   A CA  1 
ATOM   1263 C  C   . ALA   A  1 190 ? -29.148 17.049  20.182 1.00 28.11  ? 165  ALA   A C   1 
ATOM   1264 O  O   . ALA   A  1 190 ? -28.072 16.882  20.766 1.00 30.31  ? 165  ALA   A O   1 
ATOM   1265 C  CB  . ALA   A  1 190 ? -28.757 19.309  19.148 1.00 31.49  ? 165  ALA   A CB  1 
ATOM   1266 N  N   . CYS   A  1 191 ? -29.870 16.042  19.700 1.00 30.38  ? 166  CYS   A N   1 
ATOM   1267 C  CA  . CYS   A  1 191 ? -29.537 14.650  20.004 1.00 33.40  ? 166  CYS   A CA  1 
ATOM   1268 C  C   . CYS   A  1 191 ? -28.421 14.181  19.082 1.00 30.83  ? 166  CYS   A C   1 
ATOM   1269 O  O   . CYS   A  1 191 ? -28.662 13.783  17.940 1.00 32.42  ? 166  CYS   A O   1 
ATOM   1270 C  CB  . CYS   A  1 191 ? -30.760 13.754  19.882 1.00 31.19  ? 166  CYS   A CB  1 
ATOM   1271 S  SG  . CYS   A  1 191 ? -30.402 12.055  20.352 1.00 33.76  ? 166  CYS   A SG  1 
ATOM   1272 N  N   . LEU   A  1 192 ? -27.195 14.223  19.596 1.00 26.74  ? 167  LEU   A N   1 
ATOM   1273 C  CA  . LEU   A  1 192 ? -25.995 13.807  18.884 1.00 29.07  ? 167  LEU   A CA  1 
ATOM   1274 C  C   . LEU   A  1 192 ? -25.191 12.885  19.787 1.00 25.22  ? 167  LEU   A C   1 
ATOM   1275 O  O   . LEU   A  1 192 ? -25.038 13.169  20.979 1.00 22.91  ? 167  LEU   A O   1 
ATOM   1276 C  CB  . LEU   A  1 192 ? -25.155 15.017  18.469 1.00 31.11  ? 167  LEU   A CB  1 
ATOM   1277 C  CG  . LEU   A  1 192 ? -25.806 15.935  17.434 1.00 33.62  ? 167  LEU   A CG  1 
ATOM   1278 C  CD1 . LEU   A  1 192 ? -25.023 17.226  17.301 1.00 33.61  ? 167  LEU   A CD1 1 
ATOM   1279 C  CD2 . LEU   A  1 192 ? -25.903 15.223  16.095 1.00 38.35  ? 167  LEU   A CD2 1 
ATOM   1280 N  N   . PHE   A  1 193 ? -24.713 11.771  19.222 1.00 23.36  ? 168  PHE   A N   1 
ATOM   1281 C  CA  . PHE   A  1 193 ? -24.062 10.732  20.019 1.00 24.75  ? 168  PHE   A CA  1 
ATOM   1282 C  C   . PHE   A  1 193 ? -22.969 11.318  20.906 1.00 22.94  ? 168  PHE   A C   1 
ATOM   1283 O  O   . PHE   A  1 193 ? -22.963 11.106  22.124 1.00 25.09  ? 168  PHE   A O   1 
ATOM   1284 C  CB  . PHE   A  1 193 ? -23.484 9.641   19.109 1.00 22.81  ? 168  PHE   A CB  1 
ATOM   1285 C  CG  . PHE   A  1 193 ? -22.963 8.442   19.861 1.00 23.75  ? 168  PHE   A CG  1 
ATOM   1286 C  CD1 . PHE   A  1 193 ? -21.701 8.459   20.443 1.00 25.10  ? 168  PHE   A CD1 1 
ATOM   1287 C  CD2 . PHE   A  1 193 ? -23.742 7.302   19.996 1.00 21.95  ? 168  PHE   A CD2 1 
ATOM   1288 C  CE1 . PHE   A  1 193 ? -21.224 7.361   21.146 1.00 21.89  ? 168  PHE   A CE1 1 
ATOM   1289 C  CE2 . PHE   A  1 193 ? -23.272 6.200   20.692 1.00 24.77  ? 168  PHE   A CE2 1 
ATOM   1290 C  CZ  . PHE   A  1 193 ? -22.011 6.230   21.270 1.00 20.91  ? 168  PHE   A CZ  1 
ATOM   1291 N  N   . GLU   A  1 194 ? -22.032 12.058  20.316 1.00 23.54  ? 169  GLU   A N   1 
ATOM   1292 C  CA  . GLU   A  1 194 ? -20.881 12.512  21.085 1.00 24.14  ? 169  GLU   A CA  1 
ATOM   1293 C  C   . GLU   A  1 194 ? -21.217 13.670  22.015 1.00 28.52  ? 169  GLU   A C   1 
ATOM   1294 O  O   . GLU   A  1 194 ? -20.380 14.038  22.846 1.00 27.45  ? 169  GLU   A O   1 
ATOM   1295 C  CB  . GLU   A  1 194 ? -19.741 12.922  20.146 1.00 28.32  ? 169  GLU   A CB  1 
ATOM   1296 C  CG  . GLU   A  1 194 ? -19.172 11.772  19.325 1.00 21.65  ? 169  GLU   A CG  1 
ATOM   1297 C  CD  . GLU   A  1 194 ? -17.908 12.149  18.564 1.00 26.11  ? 169  GLU   A CD  1 
ATOM   1298 O  OE1 . GLU   A  1 194 ? -17.376 13.257  18.780 1.00 32.14  ? 169  GLU   A OE1 1 
ATOM   1299 O  OE2 . GLU   A  1 194 ? -17.451 11.332  17.739 1.00 26.23  ? 169  GLU   A OE2 1 
ATOM   1300 N  N   . ASP   A  1 195 ? -22.412 14.254  21.900 1.00 22.63  ? 170  ASP   A N   1 
ATOM   1301 C  CA  . ASP   A  1 195 ? -22.823 15.274  22.857 1.00 27.38  ? 170  ASP   A CA  1 
ATOM   1302 C  C   . ASP   A  1 195 ? -23.379 14.681  24.147 1.00 25.17  ? 170  ASP   A C   1 
ATOM   1303 O  O   . ASP   A  1 195 ? -23.337 15.345  25.188 1.00 27.26  ? 170  ASP   A O   1 
ATOM   1304 C  CB  . ASP   A  1 195 ? -23.855 16.215  22.233 1.00 28.06  ? 170  ASP   A CB  1 
ATOM   1305 C  CG  . ASP   A  1 195 ? -23.259 17.106  21.156 1.00 34.05  ? 170  ASP   A CG  1 
ATOM   1306 O  OD1 . ASP   A  1 195 ? -22.025 17.080  20.967 1.00 36.49  ? 170  ASP   A OD1 1 
ATOM   1307 O  OD2 . ASP   A  1 195 ? -24.025 17.845  20.507 1.00 33.24  ? 170  ASP   A OD2 1 
ATOM   1308 N  N   . VAL   A  1 196 ? -23.930 13.467  24.113 1.00 21.27  ? 171  VAL   A N   1 
ATOM   1309 C  CA  . VAL   A  1 196 ? -24.557 12.900  25.296 1.00 21.78  ? 171  VAL   A CA  1 
ATOM   1310 C  C   . VAL   A  1 196 ? -23.768 11.739  25.898 1.00 27.23  ? 171  VAL   A C   1 
ATOM   1311 O  O   . VAL   A  1 196 ? -23.798 11.563  27.122 1.00 23.33  ? 171  VAL   A O   1 
ATOM   1312 C  CB  . VAL   A  1 196 ? -26.014 12.477  25.005 1.00 22.80  ? 171  VAL   A CB  1 
ATOM   1313 C  CG1 . VAL   A  1 196 ? -26.825 13.675  24.534 1.00 29.04  ? 171  VAL   A CG1 1 
ATOM   1314 C  CG2 . VAL   A  1 196 ? -26.067 11.354  23.975 1.00 18.35  ? 171  VAL   A CG2 1 
ATOM   1315 N  N   . VAL   A  1 197 ? -23.057 10.950  25.098 1.00 20.73  ? 172  VAL   A N   1 
ATOM   1316 C  CA  . VAL   A  1 197 ? -22.303 9.806   25.599 1.00 19.53  ? 172  VAL   A CA  1 
ATOM   1317 C  C   . VAL   A  1 197 ? -20.871 10.265  25.867 1.00 21.22  ? 172  VAL   A C   1 
ATOM   1318 O  O   . VAL   A  1 197 ? -20.213 10.757  24.937 1.00 24.51  ? 172  VAL   A O   1 
ATOM   1319 C  CB  . VAL   A  1 197 ? -22.325 8.630   24.615 1.00 24.68  ? 172  VAL   A CB  1 
ATOM   1320 C  CG1 . VAL   A  1 197 ? -21.652 7.412   25.235 1.00 20.60  ? 172  VAL   A CG1 1 
ATOM   1321 C  CG2 . VAL   A  1 197 ? -23.754 8.293   24.212 1.00 23.66  ? 172  VAL   A CG2 1 
ATOM   1322 N  N   . PRO   A  1 198 ? -20.361 10.131  27.090 1.00 26.05  ? 173  PRO   A N   1 
ATOM   1323 C  CA  . PRO   A  1 198 ? -18.998 10.599  27.370 1.00 24.00  ? 173  PRO   A CA  1 
ATOM   1324 C  C   . PRO   A  1 198 ? -17.981 9.747   26.632 1.00 19.79  ? 173  PRO   A C   1 
ATOM   1325 O  O   . PRO   A  1 198 ? -18.142 8.531   26.500 1.00 18.96  ? 173  PRO   A O   1 
ATOM   1326 C  CB  . PRO   A  1 198 ? -18.865 10.436  28.890 1.00 22.01  ? 173  PRO   A CB  1 
ATOM   1327 C  CG  . PRO   A  1 198 ? -20.264 10.344  29.395 1.00 26.88  ? 173  PRO   A CG  1 
ATOM   1328 C  CD  . PRO   A  1 198 ? -21.031 9.649   28.308 1.00 22.71  ? 173  PRO   A CD  1 
ATOM   1329 N  N   A MET   A  1 199 ? -16.923 10.393  26.143 0.61 22.36  ? 174  MET   A N   1 
ATOM   1330 N  N   B MET   A  1 199 ? -16.917 10.398  26.158 0.39 22.38  ? 174  MET   A N   1 
ATOM   1331 C  CA  A MET   A  1 199 ? -15.899 9.655   25.417 0.61 21.24  ? 174  MET   A CA  1 
ATOM   1332 C  CA  B MET   A  1 199 ? -15.887 9.671   25.424 0.39 21.30  ? 174  MET   A CA  1 
ATOM   1333 C  C   A MET   A  1 199 ? -15.003 8.835   26.337 0.61 23.18  ? 174  MET   A C   1 
ATOM   1334 C  C   B MET   A  1 199 ? -15.032 8.814   26.348 0.39 23.17  ? 174  MET   A C   1 
ATOM   1335 O  O   A MET   A  1 199 ? -14.426 7.840   25.887 0.61 21.78  ? 174  MET   A O   1 
ATOM   1336 O  O   B MET   A  1 199 ? -14.509 7.779   25.918 0.39 21.73  ? 174  MET   A O   1 
ATOM   1337 C  CB  A MET   A  1 199 ? -15.050 10.608  24.575 0.61 22.55  ? 174  MET   A CB  1 
ATOM   1338 C  CB  B MET   A  1 199 ? -15.011 10.644  24.638 0.39 22.62  ? 174  MET   A CB  1 
ATOM   1339 C  CG  A MET   A  1 199 ? -14.470 9.972   23.318 0.61 25.81  ? 174  MET   A CG  1 
ATOM   1340 C  CG  B MET   A  1 199 ? -15.464 10.854  23.204 0.39 23.34  ? 174  MET   A CG  1 
ATOM   1341 S  SD  A MET   A  1 199 ? -15.687 9.143   22.269 0.61 30.91  ? 174  MET   A SD  1 
ATOM   1342 S  SD  B MET   A  1 199 ? -15.724 9.308   22.310 0.39 31.78  ? 174  MET   A SD  1 
ATOM   1343 C  CE  A MET   A  1 199 ? -16.103 10.464  21.132 0.61 31.84  ? 174  MET   A CE  1 
ATOM   1344 C  CE  B MET   A  1 199 ? -16.267 9.939   20.727 0.39 32.09  ? 174  MET   A CE  1 
ATOM   1345 N  N   . ASN   A  1 200 ? -14.875 9.217   27.612 1.00 22.85  ? 175  ASN   A N   1 
ATOM   1346 C  CA  . ASN   A  1 200 ? -14.113 8.384   28.539 1.00 21.37  ? 175  ASN   A CA  1 
ATOM   1347 C  C   . ASN   A  1 200 ? -14.852 7.080   28.814 1.00 22.65  ? 175  ASN   A C   1 
ATOM   1348 O  O   . ASN   A  1 200 ? -14.223 6.025   28.963 1.00 24.14  ? 175  ASN   A O   1 
ATOM   1349 C  CB  . ASN   A  1 200 ? -13.793 9.124   29.846 1.00 25.76  ? 175  ASN   A CB  1 
ATOM   1350 C  CG  . ASN   A  1 200 ? -15.003 9.793   30.482 1.00 27.48  ? 175  ASN   A CG  1 
ATOM   1351 O  OD1 . ASN   A  1 200 ? -16.148 9.442   30.209 1.00 28.52  ? 175  ASN   A OD1 1 
ATOM   1352 N  ND2 . ASN   A  1 200 ? -14.742 10.749  31.370 1.00 26.26  ? 175  ASN   A ND2 1 
ATOM   1353 N  N   . TYR   A  1 201 ? -16.187 7.125   28.878 1.00 19.10  ? 176  TYR   A N   1 
ATOM   1354 C  CA  . TYR   A  1 201 ? -16.956 5.883   28.894 1.00 20.99  ? 176  TYR   A CA  1 
ATOM   1355 C  C   . TYR   A  1 201 ? -16.670 5.048   27.651 1.00 15.02  ? 176  TYR   A C   1 
ATOM   1356 O  O   . TYR   A  1 201 ? -16.394 3.846   27.746 1.00 20.56  ? 176  TYR   A O   1 
ATOM   1357 C  CB  . TYR   A  1 201 ? -18.455 6.174   29.006 1.00 22.11  ? 176  TYR   A CB  1 
ATOM   1358 C  CG  . TYR   A  1 201 ? -19.291 4.944   28.734 1.00 21.06  ? 176  TYR   A CG  1 
ATOM   1359 C  CD1 . TYR   A  1 201 ? -19.564 4.024   29.738 1.00 18.69  ? 176  TYR   A CD1 1 
ATOM   1360 C  CD2 . TYR   A  1 201 ? -19.788 4.691   27.460 1.00 20.70  ? 176  TYR   A CD2 1 
ATOM   1361 C  CE1 . TYR   A  1 201 ? -20.311 2.884   29.478 1.00 18.92  ? 176  TYR   A CE1 1 
ATOM   1362 C  CE2 . TYR   A  1 201 ? -20.533 3.560   27.191 1.00 20.43  ? 176  TYR   A CE2 1 
ATOM   1363 C  CZ  . TYR   A  1 201 ? -20.791 2.659   28.200 1.00 23.94  ? 176  TYR   A CZ  1 
ATOM   1364 O  OH  . TYR   A  1 201 ? -21.540 1.536   27.927 1.00 26.41  ? 176  TYR   A OH  1 
ATOM   1365 N  N   . MET   A  1 202 ? -16.763 5.664   26.469 1.00 19.09  ? 177  MET   A N   1 
ATOM   1366 C  CA  . MET   A  1 202 ? -16.623 4.894   25.236 1.00 22.95  ? 177  MET   A CA  1 
ATOM   1367 C  C   . MET   A  1 202 ? -15.240 4.276   25.100 1.00 17.68  ? 177  MET   A C   1 
ATOM   1368 O  O   . MET   A  1 202 ? -15.109 3.151   24.606 1.00 19.89  ? 177  MET   A O   1 
ATOM   1369 C  CB  . MET   A  1 202 ? -16.936 5.755   24.014 1.00 18.00  ? 177  MET   A CB  1 
ATOM   1370 C  CG  . MET   A  1 202 ? -18.412 6.072   23.799 1.00 20.59  ? 177  MET   A CG  1 
ATOM   1371 S  SD  . MET   A  1 202 ? -19.387 4.551   23.707 1.00 21.04  ? 177  MET   A SD  1 
ATOM   1372 C  CE  . MET   A  1 202 ? -18.714 3.795   22.225 1.00 25.22  ? 177  MET   A CE  1 
ATOM   1373 N  N   . VAL   A  1 203 ? -14.201 4.975   25.550 1.00 19.64  ? 178  VAL   A N   1 
ATOM   1374 C  CA  . VAL   A  1 203 ? -12.838 4.482   25.366 1.00 22.23  ? 178  VAL   A CA  1 
ATOM   1375 C  C   . VAL   A  1 203 ? -12.417 3.556   26.498 1.00 19.79  ? 178  VAL   A C   1 
ATOM   1376 O  O   . VAL   A  1 203 ? -12.009 2.418   26.255 1.00 21.23  ? 178  VAL   A O   1 
ATOM   1377 C  CB  . VAL   A  1 203 ? -11.862 5.667   25.216 1.00 22.39  ? 178  VAL   A CB  1 
ATOM   1378 C  CG1 . VAL   A  1 203 ? -10.425 5.162   25.225 1.00 23.56  ? 178  VAL   A CG1 1 
ATOM   1379 C  CG2 . VAL   A  1 203 ? -12.153 6.427   23.927 1.00 23.26  ? 178  VAL   A CG2 1 
ATOM   1380 N  N   . TYR   A  1 204 ? -12.512 4.010   27.751 1.00 18.15  ? 179  TYR   A N   1 
ATOM   1381 C  CA  . TYR   A  1 204 ? -11.979 3.209   28.851 1.00 18.85  ? 179  TYR   A CA  1 
ATOM   1382 C  C   . TYR   A  1 204 ? -12.925 2.088   29.247 1.00 23.55  ? 179  TYR   A C   1 
ATOM   1383 O  O   . TYR   A  1 204 ? -12.493 0.945   29.438 1.00 23.80  ? 179  TYR   A O   1 
ATOM   1384 C  CB  . TYR   A  1 204 ? -11.689 4.075   30.078 1.00 21.95  ? 179  TYR   A CB  1 
ATOM   1385 C  CG  . TYR   A  1 204 ? -10.542 5.044   29.933 1.00 25.41  ? 179  TYR   A CG  1 
ATOM   1386 C  CD1 . TYR   A  1 204 ? -9.324  4.634   29.404 1.00 28.19  ? 179  TYR   A CD1 1 
ATOM   1387 C  CD2 . TYR   A  1 204 ? -10.661 6.358   30.365 1.00 27.73  ? 179  TYR   A CD2 1 
ATOM   1388 C  CE1 . TYR   A  1 204 ? -8.268  5.514   29.281 1.00 27.36  ? 179  TYR   A CE1 1 
ATOM   1389 C  CE2 . TYR   A  1 204 ? -9.608  7.246   30.249 1.00 31.20  ? 179  TYR   A CE2 1 
ATOM   1390 C  CZ  . TYR   A  1 204 ? -8.413  6.817   29.708 1.00 28.77  ? 179  TYR   A CZ  1 
ATOM   1391 O  OH  . TYR   A  1 204 ? -7.359  7.692   29.594 1.00 33.97  ? 179  TYR   A OH  1 
ATOM   1392 N  N   . PHE   A  1 205 ? -14.217 2.387   29.361 1.00 23.09  ? 180  PHE   A N   1 
ATOM   1393 C  CA  . PHE   A  1 205 ? -15.162 1.409   29.882 1.00 23.37  ? 180  PHE   A CA  1 
ATOM   1394 C  C   . PHE   A  1 205 ? -15.678 0.509   28.764 1.00 17.75  ? 180  PHE   A C   1 
ATOM   1395 O  O   . PHE   A  1 205 ? -15.544 -0.716  28.834 1.00 24.90  ? 180  PHE   A O   1 
ATOM   1396 C  CB  . PHE   A  1 205 ? -16.313 2.140   30.587 1.00 22.16  ? 180  PHE   A CB  1 
ATOM   1397 C  CG  . PHE   A  1 205 ? -17.226 1.242   31.382 1.00 25.71  ? 180  PHE   A CG  1 
ATOM   1398 C  CD1 . PHE   A  1 205 ? -18.277 0.573   30.769 1.00 20.15  ? 180  PHE   A CD1 1 
ATOM   1399 C  CD2 . PHE   A  1 205 ? -17.054 1.096   32.751 1.00 23.73  ? 180  PHE   A CD2 1 
ATOM   1400 C  CE1 . PHE   A  1 205 ? -19.127 -0.241  31.502 1.00 25.54  ? 180  PHE   A CE1 1 
ATOM   1401 C  CE2 . PHE   A  1 205 ? -17.902 0.284   33.492 1.00 25.91  ? 180  PHE   A CE2 1 
ATOM   1402 C  CZ  . PHE   A  1 205 ? -18.939 -0.386  32.867 1.00 23.62  ? 180  PHE   A CZ  1 
ATOM   1403 N  N   . ASN   A  1 206 ? -16.268 1.102   27.726 1.00 20.84  ? 181  ASN   A N   1 
ATOM   1404 C  CA  . ASN   A  1 206 ? -16.861 0.286   26.673 1.00 22.83  ? 181  ASN   A CA  1 
ATOM   1405 C  C   . ASN   A  1 206 ? -15.790 -0.409  25.835 1.00 22.00  ? 181  ASN   A C   1 
ATOM   1406 O  O   . ASN   A  1 206 ? -15.804 -1.636  25.692 1.00 26.72  ? 181  ASN   A O   1 
ATOM   1407 C  CB  . ASN   A  1 206 ? -17.788 1.122   25.796 1.00 22.84  ? 181  ASN   A CB  1 
ATOM   1408 C  CG  . ASN   A  1 206 ? -18.647 0.259   24.896 1.00 31.91  ? 181  ASN   A CG  1 
ATOM   1409 O  OD1 . ASN   A  1 206 ? -19.733 -0.173  25.288 1.00 26.81  ? 181  ASN   A OD1 1 
ATOM   1410 N  ND2 . ASN   A  1 206 ? -18.155 -0.020  23.696 1.00 24.22  ? 181  ASN   A ND2 1 
ATOM   1411 N  N   . PHE   A  1 207 ? -14.837 0.354   25.291 1.00 20.66  ? 182  PHE   A N   1 
ATOM   1412 C  CA  . PHE   A  1 207 ? -13.867 -0.233  24.368 1.00 22.78  ? 182  PHE   A CA  1 
ATOM   1413 C  C   . PHE   A  1 207 ? -12.847 -1.092  25.108 1.00 21.74  ? 182  PHE   A C   1 
ATOM   1414 O  O   . PHE   A  1 207 ? -12.768 -2.305  24.883 1.00 25.12  ? 182  PHE   A O   1 
ATOM   1415 C  CB  . PHE   A  1 207 ? -13.173 0.866   23.556 1.00 17.83  ? 182  PHE   A CB  1 
ATOM   1416 C  CG  . PHE   A  1 207 ? -12.221 0.343   22.509 1.00 22.85  ? 182  PHE   A CG  1 
ATOM   1417 C  CD1 . PHE   A  1 207 ? -12.475 -0.848  21.846 1.00 22.49  ? 182  PHE   A CD1 1 
ATOM   1418 C  CD2 . PHE   A  1 207 ? -11.072 1.052   22.185 1.00 24.13  ? 182  PHE   A CD2 1 
ATOM   1419 C  CE1 . PHE   A  1 207 ? -11.598 -1.329  20.885 1.00 20.46  ? 182  PHE   A CE1 1 
ATOM   1420 C  CE2 . PHE   A  1 207 ? -10.194 0.581   21.225 1.00 23.99  ? 182  PHE   A CE2 1 
ATOM   1421 C  CZ  . PHE   A  1 207 ? -10.457 -0.612  20.573 1.00 28.30  ? 182  PHE   A CZ  1 
ATOM   1422 N  N   . PHE   A  1 208 ? -12.035 -0.482  25.975 1.00 20.75  ? 183  PHE   A N   1 
ATOM   1423 C  CA  . PHE   A  1 208 ? -10.924 -1.220  26.572 1.00 25.93  ? 183  PHE   A CA  1 
ATOM   1424 C  C   . PHE   A  1 208 ? -11.430 -2.374  27.431 1.00 20.40  ? 183  PHE   A C   1 
ATOM   1425 O  O   . PHE   A  1 208 ? -11.057 -3.534  27.217 1.00 21.64  ? 183  PHE   A O   1 
ATOM   1426 C  CB  . PHE   A  1 208 ? -10.043 -0.285  27.407 1.00 20.81  ? 183  PHE   A CB  1 
ATOM   1427 C  CG  . PHE   A  1 208 ? -9.189  0.655   26.595 1.00 24.86  ? 183  PHE   A CG  1 
ATOM   1428 C  CD1 . PHE   A  1 208 ? -9.222  0.641   25.211 1.00 26.86  ? 183  PHE   A CD1 1 
ATOM   1429 C  CD2 . PHE   A  1 208 ? -8.356  1.564   27.229 1.00 29.54  ? 183  PHE   A CD2 1 
ATOM   1430 C  CE1 . PHE   A  1 208 ? -8.429  1.509   24.474 1.00 29.27  ? 183  PHE   A CE1 1 
ATOM   1431 C  CE2 . PHE   A  1 208 ? -7.565  2.433   26.500 1.00 31.83  ? 183  PHE   A CE2 1 
ATOM   1432 C  CZ  . PHE   A  1 208 ? -7.604  2.407   25.120 1.00 24.22  ? 183  PHE   A CZ  1 
ATOM   1433 N  N   . ALA   A  1 209 ? -12.314 -2.079  28.386 1.00 20.02  ? 184  ALA   A N   1 
ATOM   1434 C  CA  . ALA   A  1 209 ? -12.717 -3.090  29.359 1.00 23.49  ? 184  ALA   A CA  1 
ATOM   1435 C  C   . ALA   A  1 209 ? -13.707 -4.090  28.773 1.00 25.68  ? 184  ALA   A C   1 
ATOM   1436 O  O   . ALA   A  1 209 ? -13.557 -5.301  28.962 1.00 23.96  ? 184  ALA   A O   1 
ATOM   1437 C  CB  . ALA   A  1 209 ? -13.313 -2.414  30.596 1.00 21.99  ? 184  ALA   A CB  1 
ATOM   1438 N  N   . CYS   A  1 210 ? -14.732 -3.605  28.070 1.00 22.34  ? 185  CYS   A N   1 
ATOM   1439 C  CA  . CYS   A  1 210 ? -15.860 -4.450  27.697 1.00 25.32  ? 185  CYS   A CA  1 
ATOM   1440 C  C   . CYS   A  1 210 ? -15.754 -5.038  26.295 1.00 22.50  ? 185  CYS   A C   1 
ATOM   1441 O  O   . CYS   A  1 210 ? -16.516 -5.956  25.970 1.00 26.60  ? 185  CYS   A O   1 
ATOM   1442 C  CB  . CYS   A  1 210 ? -17.168 -3.660  27.826 1.00 27.05  ? 185  CYS   A CB  1 
ATOM   1443 S  SG  . CYS   A  1 210 ? -17.579 -3.262  29.543 1.00 30.24  ? 185  CYS   A SG  1 
ATOM   1444 N  N   . VAL   A  1 211 ? -14.839 -4.545  25.462 1.00 21.58  ? 186  VAL   A N   1 
ATOM   1445 C  CA  . VAL   A  1 211 ? -14.723 -5.028  24.091 1.00 23.89  ? 186  VAL   A CA  1 
ATOM   1446 C  C   . VAL   A  1 211 ? -13.331 -5.604  23.864 1.00 26.76  ? 186  VAL   A C   1 
ATOM   1447 O  O   . VAL   A  1 211 ? -13.184 -6.774  23.494 1.00 23.83  ? 186  VAL   A O   1 
ATOM   1448 C  CB  . VAL   A  1 211 ? -15.015 -3.911  23.071 1.00 26.07  ? 186  VAL   A CB  1 
ATOM   1449 C  CG1 . VAL   A  1 211 ? -14.660 -4.374  21.661 1.00 21.19  ? 186  VAL   A CG1 1 
ATOM   1450 C  CG2 . VAL   A  1 211 ? -16.469 -3.467  23.154 1.00 25.79  ? 186  VAL   A CG2 1 
ATOM   1451 N  N   A LEU   A  1 212 ? -12.303 -4.782  24.090 0.54 25.77  ? 187  LEU   A N   1 
ATOM   1452 N  N   B LEU   A  1 212 ? -12.304 -4.780  24.087 0.46 25.76  ? 187  LEU   A N   1 
ATOM   1453 C  CA  A LEU   A  1 212 ? -10.936 -5.198  23.792 0.54 23.05  ? 187  LEU   A CA  1 
ATOM   1454 C  CA  B LEU   A  1 212 ? -10.934 -5.194  23.796 0.46 23.08  ? 187  LEU   A CA  1 
ATOM   1455 C  C   A LEU   A  1 212 ? -10.515 -6.379  24.659 0.54 24.71  ? 187  LEU   A C   1 
ATOM   1456 C  C   B LEU   A  1 212 ? -10.520 -6.380  24.658 0.46 24.72  ? 187  LEU   A C   1 
ATOM   1457 O  O   A LEU   A  1 212 ? -9.948  -7.358  24.161 0.54 26.63  ? 187  LEU   A O   1 
ATOM   1458 O  O   B LEU   A  1 212 ? -9.960  -7.362  24.158 0.46 26.62  ? 187  LEU   A O   1 
ATOM   1459 C  CB  A LEU   A  1 212 ? -9.982  -4.019  23.981 0.54 27.54  ? 187  LEU   A CB  1 
ATOM   1460 C  CB  B LEU   A  1 212 ? -9.981  -4.017  24.004 0.46 27.54  ? 187  LEU   A CB  1 
ATOM   1461 C  CG  A LEU   A  1 212 ? -8.667  -4.065  23.203 0.54 30.84  ? 187  LEU   A CG  1 
ATOM   1462 C  CG  B LEU   A  1 212 ? -9.393  -3.372  22.749 0.46 28.79  ? 187  LEU   A CG  1 
ATOM   1463 C  CD1 A LEU   A  1 212 ? -8.930  -4.284  21.719 0.54 33.77  ? 187  LEU   A CD1 1 
ATOM   1464 C  CD1 B LEU   A  1 212 ? -8.416  -2.266  23.123 0.46 25.50  ? 187  LEU   A CD1 1 
ATOM   1465 C  CD2 A LEU   A  1 212 ? -7.874  -2.787  23.428 0.54 29.13  ? 187  LEU   A CD2 1 
ATOM   1466 C  CD2 B LEU   A  1 212 ? -8.718  -4.415  21.870 0.46 34.28  ? 187  LEU   A CD2 1 
ATOM   1467 N  N   . VAL   A  1 213 ? -10.790 -6.305  25.963 1.00 22.43  ? 188  VAL   A N   1 
ATOM   1468 C  CA  . VAL   A  1 213 ? -10.413 -7.399  26.863 1.00 27.89  ? 188  VAL   A CA  1 
ATOM   1469 C  C   . VAL   A  1 213 ? -11.128 -8.700  26.519 1.00 31.47  ? 188  VAL   A C   1 
ATOM   1470 O  O   . VAL   A  1 213 ? -10.456 -9.742  26.429 1.00 28.70  ? 188  VAL   A O   1 
ATOM   1471 C  CB  . VAL   A  1 213 ? -10.609 -6.971  28.329 1.00 27.90  ? 188  VAL   A CB  1 
ATOM   1472 C  CG1 . VAL   A  1 213 ? -10.536 -8.183  29.247 1.00 27.67  ? 188  VAL   A CG1 1 
ATOM   1473 C  CG2 . VAL   A  1 213 ? -9.553  -5.947  28.723 1.00 24.41  ? 188  VAL   A CG2 1 
ATOM   1474 N  N   . PRO   A  1 214 ? -12.452 -8.731  26.314 1.00 27.34  ? 189  PRO   A N   1 
ATOM   1475 C  CA  . PRO   A  1 214 ? -13.077 -9.995  25.886 1.00 23.02  ? 189  PRO   A CA  1 
ATOM   1476 C  C   . PRO   A  1 214 ? -12.552 -10.521 24.559 1.00 24.74  ? 189  PRO   A C   1 
ATOM   1477 O  O   . PRO   A  1 214 ? -12.414 -11.739 24.399 1.00 24.55  ? 189  PRO   A O   1 
ATOM   1478 C  CB  . PRO   A  1 214 ? -14.565 -9.633  25.804 1.00 27.15  ? 189  PRO   A CB  1 
ATOM   1479 C  CG  . PRO   A  1 214 ? -14.730 -8.523  26.765 1.00 28.92  ? 189  PRO   A CG  1 
ATOM   1480 C  CD  . PRO   A  1 214 ? -13.470 -7.717  26.649 1.00 27.37  ? 189  PRO   A CD  1 
ATOM   1481 N  N   . LEU   A  1 215 ? -12.282 -9.645  23.588 1.00 22.59  ? 190  LEU   A N   1 
ATOM   1482 C  CA  . LEU   A  1 215 ? -11.724 -10.111 22.319 1.00 24.77  ? 190  LEU   A CA  1 
ATOM   1483 C  C   . LEU   A  1 215 ? -10.351 -10.745 22.511 1.00 26.44  ? 190  LEU   A C   1 
ATOM   1484 O  O   . LEU   A  1 215 ? -10.042 -11.773 21.896 1.00 26.94  ? 190  LEU   A O   1 
ATOM   1485 C  CB  . LEU   A  1 215 ? -11.650 -8.959  21.319 1.00 20.21  ? 190  LEU   A CB  1 
ATOM   1486 C  CG  . LEU   A  1 215 ? -12.987 -8.475  20.751 1.00 23.57  ? 190  LEU   A CG  1 
ATOM   1487 C  CD1 . LEU   A  1 215 ? -12.800 -7.203  19.934 1.00 32.95  ? 190  LEU   A CD1 1 
ATOM   1488 C  CD2 . LEU   A  1 215 ? -13.629 -9.566  19.904 1.00 24.85  ? 190  LEU   A CD2 1 
ATOM   1489 N  N   . LEU   A  1 216 ? -9.515  -10.153 23.365 1.00 25.37  ? 191  LEU   A N   1 
ATOM   1490 C  CA  . LEU   A  1 216 ? -8.212  -10.745 23.648 1.00 24.23  ? 191  LEU   A CA  1 
ATOM   1491 C  C   . LEU   A  1 216 ? -8.361  -12.085 24.358 1.00 30.21  ? 191  LEU   A C   1 
ATOM   1492 O  O   . LEU   A  1 216 ? -7.588  -13.017 24.105 1.00 30.24  ? 191  LEU   A O   1 
ATOM   1493 C  CB  . LEU   A  1 216 ? -7.365  -9.779  24.476 1.00 20.38  ? 191  LEU   A CB  1 
ATOM   1494 C  CG  . LEU   A  1 216 ? -6.953  -8.510  23.723 1.00 27.74  ? 191  LEU   A CG  1 
ATOM   1495 C  CD1 . LEU   A  1 216 ? -6.257  -7.522  24.648 1.00 34.97  ? 191  LEU   A CD1 1 
ATOM   1496 C  CD2 . LEU   A  1 216 ? -6.063  -8.862  22.539 1.00 34.20  ? 191  LEU   A CD2 1 
ATOM   1497 N  N   . LEU   A  1 217 ? -9.339  -12.197 25.264 1.00 30.91  ? 192  LEU   A N   1 
ATOM   1498 C  CA  . LEU   A  1 217 ? -9.634  -13.489 25.882 1.00 25.53  ? 192  LEU   A CA  1 
ATOM   1499 C  C   . LEU   A  1 217 ? -10.055 -14.520 24.841 1.00 32.99  ? 192  LEU   A C   1 
ATOM   1500 O  O   . LEU   A  1 217 ? -9.625  -15.678 24.897 1.00 31.08  ? 192  LEU   A O   1 
ATOM   1501 C  CB  . LEU   A  1 217 ? -10.724 -13.327 26.947 1.00 28.97  ? 192  LEU   A CB  1 
ATOM   1502 C  CG  . LEU   A  1 217 ? -10.377 -12.540 28.216 1.00 36.84  ? 192  LEU   A CG  1 
ATOM   1503 C  CD1 . LEU   A  1 217 ? -11.617 -12.397 29.082 1.00 41.12  ? 192  LEU   A CD1 1 
ATOM   1504 C  CD2 . LEU   A  1 217 ? -9.263  -13.238 28.979 1.00 45.07  ? 192  LEU   A CD2 1 
ATOM   1505 N  N   . MET   A  1 218 ? -10.889 -14.112 23.880 1.00 31.03  ? 193  MET   A N   1 
ATOM   1506 C  CA  . MET   A  1 218 ? -11.286 -15.001 22.795 1.00 30.15  ? 193  MET   A CA  1 
ATOM   1507 C  C   . MET   A  1 218 ? -10.072 -15.498 22.028 1.00 29.28  ? 193  MET   A C   1 
ATOM   1508 O  O   . MET   A  1 218 ? -9.966  -16.689 21.723 1.00 35.45  ? 193  MET   A O   1 
ATOM   1509 C  CB  . MET   A  1 218 ? -12.249 -14.284 21.848 1.00 30.69  ? 193  MET   A CB  1 
ATOM   1510 C  CG  . MET   A  1 218 ? -13.684 -14.126 22.350 1.00 37.67  ? 193  MET   A CG  1 
ATOM   1511 S  SD  . MET   A  1 218 ? -14.685 -13.325 21.088 1.00 33.92  ? 193  MET   A SD  1 
ATOM   1512 C  CE  . MET   A  1 218 ? -15.608 -12.195 22.094 1.00 30.48  ? 193  MET   A CE  1 
ATOM   1513 N  N   . LEU   A  1 219 ? -9.150  -14.587 21.700 1.00 31.13  ? 194  LEU   A N   1 
ATOM   1514 C  CA  . LEU   A  1 219 ? -7.925  -14.970 21.008 1.00 36.15  ? 194  LEU   A CA  1 
ATOM   1515 C  C   . LEU   A  1 219 ? -7.158  -16.025 21.792 1.00 28.33  ? 194  LEU   A C   1 
ATOM   1516 O  O   . LEU   A  1 219 ? -6.687  -17.015 21.222 1.00 32.57  ? 194  LEU   A O   1 
ATOM   1517 C  CB  . LEU   A  1 219 ? -7.052  -13.737 20.772 1.00 27.14  ? 194  LEU   A CB  1 
ATOM   1518 C  CG  . LEU   A  1 219 ? -5.675  -13.949 20.148 1.00 36.11  ? 194  LEU   A CG  1 
ATOM   1519 C  CD1 . LEU   A  1 219 ? -5.792  -14.638 18.794 1.00 31.53  ? 194  LEU   A CD1 1 
ATOM   1520 C  CD2 . LEU   A  1 219 ? -4.944  -12.619 20.023 1.00 27.35  ? 194  LEU   A CD2 1 
ATOM   1521 N  N   . GLY   A  1 220 ? -7.024  -15.828 23.104 1.00 34.49  ? 195  GLY   A N   1 
ATOM   1522 C  CA  . GLY   A  1 220 ? -6.346  -16.817 23.928 1.00 34.31  ? 195  GLY   A CA  1 
ATOM   1523 C  C   . GLY   A  1 220 ? -7.039  -18.167 23.938 1.00 37.39  ? 195  GLY   A C   1 
ATOM   1524 O  O   . GLY   A  1 220 ? -6.387  -19.210 23.861 1.00 34.38  ? 195  GLY   A O   1 
ATOM   1525 N  N   . VAL   A  1 221 ? -8.372  -18.165 24.015 1.00 28.30  ? 196  VAL   A N   1 
ATOM   1526 C  CA  . VAL   A  1 221 ? -9.128  -19.415 23.964 1.00 29.43  ? 196  VAL   A CA  1 
ATOM   1527 C  C   . VAL   A  1 221 ? -8.904  -20.130 22.637 1.00 35.66  ? 196  VAL   A C   1 
ATOM   1528 O  O   . VAL   A  1 221 ? -8.691  -21.347 22.600 1.00 32.27  ? 196  VAL   A O   1 
ATOM   1529 C  CB  . VAL   A  1 221 ? -10.623 -19.148 24.217 1.00 30.67  ? 196  VAL   A CB  1 
ATOM   1530 C  CG1 . VAL   A  1 221 ? -11.428 -20.433 24.076 1.00 34.63  ? 196  VAL   A CG1 1 
ATOM   1531 C  CG2 . VAL   A  1 221 ? -10.826 -18.556 25.605 1.00 33.14  ? 196  VAL   A CG2 1 
ATOM   1532 N  N   . TYR   A  1 222 ? -8.964  -19.390 21.528 1.00 30.39  ? 197  TYR   A N   1 
ATOM   1533 C  CA  . TYR   A  1 222 ? -8.759  -20.010 20.222 1.00 35.06  ? 197  TYR   A CA  1 
ATOM   1534 C  C   . TYR   A  1 222 ? -7.349  -20.573 20.075 1.00 39.89  ? 197  TYR   A C   1 
ATOM   1535 O  O   . TYR   A  1 222 ? -7.165  -21.648 19.493 1.00 33.43  ? 197  TYR   A O   1 
ATOM   1536 C  CB  . TYR   A  1 222 ? -9.097  -19.015 19.112 1.00 30.81  ? 197  TYR   A CB  1 
ATOM   1537 C  CG  . TYR   A  1 222 ? -10.590 -18.958 18.886 1.00 28.67  ? 197  TYR   A CG  1 
ATOM   1538 C  CD1 . TYR   A  1 222 ? -11.280 -20.077 18.434 1.00 32.54  ? 197  TYR   A CD1 1 
ATOM   1539 C  CD2 . TYR   A  1 222 ? -11.316 -17.808 19.164 1.00 31.94  ? 197  TYR   A CD2 1 
ATOM   1540 C  CE1 . TYR   A  1 222 ? -12.646 -20.045 18.236 1.00 31.06  ? 197  TYR   A CE1 1 
ATOM   1541 C  CE2 . TYR   A  1 222 ? -12.688 -17.766 18.975 1.00 30.47  ? 197  TYR   A CE2 1 
ATOM   1542 C  CZ  . TYR   A  1 222 ? -13.346 -18.888 18.511 1.00 32.71  ? 197  TYR   A CZ  1 
ATOM   1543 O  OH  . TYR   A  1 222 ? -14.709 -18.857 18.330 1.00 37.21  ? 197  TYR   A OH  1 
ATOM   1544 N  N   . LEU   A  1 223 ? -6.339  -19.861 20.587 1.00 34.05  ? 198  LEU   A N   1 
ATOM   1545 C  CA  . LEU   A  1 223 ? -4.980  -20.403 20.592 1.00 38.91  ? 198  LEU   A CA  1 
ATOM   1546 C  C   . LEU   A  1 223 ? -4.919  -21.723 21.349 1.00 34.54  ? 198  LEU   A C   1 
ATOM   1547 O  O   . LEU   A  1 223 ? -4.272  -22.679 20.904 1.00 34.06  ? 198  LEU   A O   1 
ATOM   1548 C  CB  . LEU   A  1 223 ? -4.007  -19.396 21.203 1.00 30.35  ? 198  LEU   A CB  1 
ATOM   1549 C  CG  . LEU   A  1 223 ? -3.747  -18.138 20.376 1.00 45.31  ? 198  LEU   A CG  1 
ATOM   1550 C  CD1 . LEU   A  1 223 ? -2.858  -17.167 21.136 1.00 43.33  ? 198  LEU   A CD1 1 
ATOM   1551 C  CD2 . LEU   A  1 223 ? -3.128  -18.506 19.037 1.00 43.19  ? 198  LEU   A CD2 1 
ATOM   1552 N  N   . ARG   A  1 224 ? -5.600  -21.788 22.493 1.00 35.99  ? 199  ARG   A N   1 
ATOM   1553 C  CA  . ARG   A  1 224 ? -5.646  -23.007 23.292 1.00 35.65  ? 199  ARG   A CA  1 
ATOM   1554 C  C   . ARG   A  1 224 ? -6.371  -24.126 22.549 1.00 41.99  ? 199  ARG   A C   1 
ATOM   1555 O  O   . ARG   A  1 224 ? -5.971  -25.295 22.629 1.00 41.58  ? 199  ARG   A O   1 
ATOM   1556 C  CB  . ARG   A  1 224 ? -6.353  -22.678 24.606 1.00 37.62  ? 199  ARG   A CB  1 
ATOM   1557 C  CG  . ARG   A  1 224 ? -5.543  -21.744 25.497 1.00 42.62  ? 199  ARG   A CG  1 
ATOM   1558 C  CD  . ARG   A  1 224 ? -6.293  -21.427 26.778 1.00 50.42  ? 199  ARG   A CD  1 
ATOM   1559 N  NE  . ARG   A  1 224 ? -5.459  -20.839 27.822 1.00 80.54  ? 199  ARG   A NE  1 
ATOM   1560 C  CZ  . ARG   A  1 224 ? -5.943  -20.222 28.893 1.00 96.64  ? 199  ARG   A CZ  1 
ATOM   1561 N  NH1 . ARG   A  1 224 ? -7.246  -20.089 29.082 1.00 93.59  ? 199  ARG   A NH1 1 
ATOM   1562 N  NH2 . ARG   A  1 224 ? -5.101  -19.734 29.801 1.00 102.85 ? 199  ARG   A NH2 1 
ATOM   1563 N  N   . ILE   A  1 225 ? -7.446  -23.788 21.832 1.00 34.78  ? 200  ILE   A N   1 
ATOM   1564 C  CA  . ILE   A  1 225 ? -8.173  -24.784 21.047 1.00 35.11  ? 200  ILE   A CA  1 
ATOM   1565 C  C   . ILE   A  1 225 ? -7.270  -25.391 19.979 1.00 40.99  ? 200  ILE   A C   1 
ATOM   1566 O  O   . ILE   A  1 225 ? -7.155  -26.616 19.853 1.00 35.44  ? 200  ILE   A O   1 
ATOM   1567 C  CB  . ILE   A  1 225 ? -9.430  -24.157 20.420 1.00 32.04  ? 200  ILE   A CB  1 
ATOM   1568 C  CG1 . ILE   A  1 225 ? -10.482 -23.868 21.489 1.00 35.57  ? 200  ILE   A CG1 1 
ATOM   1569 C  CG2 . ILE   A  1 225 ? -9.996  -25.062 19.333 1.00 32.40  ? 200  ILE   A CG2 1 
ATOM   1570 C  CD1 . ILE   A  1 225 ? -11.633 -23.019 20.993 1.00 29.98  ? 200  ILE   A CD1 1 
ATOM   1571 N  N   . PHE   A  1 226 ? -6.625  -24.535 19.184 1.00 33.96  ? 201  PHE   A N   1 
ATOM   1572 C  CA  . PHE   A  1 226 ? -5.810  -25.018 18.075 1.00 38.28  ? 201  PHE   A CA  1 
ATOM   1573 C  C   . PHE   A  1 226 ? -4.558  -25.736 18.565 1.00 43.12  ? 201  PHE   A C   1 
ATOM   1574 O  O   . PHE   A  1 226 ? -4.120  -26.714 17.950 1.00 41.09  ? 201  PHE   A O   1 
ATOM   1575 C  CB  . PHE   A  1 226 ? -5.451  -23.858 17.147 1.00 38.10  ? 201  PHE   A CB  1 
ATOM   1576 C  CG  . PHE   A  1 226 ? -6.633  -23.287 16.412 1.00 44.15  ? 201  PHE   A CG  1 
ATOM   1577 C  CD1 . PHE   A  1 226 ? -7.492  -24.117 15.707 1.00 42.80  ? 201  PHE   A CD1 1 
ATOM   1578 C  CD2 . PHE   A  1 226 ? -6.890  -21.926 16.431 1.00 40.61  ? 201  PHE   A CD2 1 
ATOM   1579 C  CE1 . PHE   A  1 226 ? -8.584  -23.599 15.030 1.00 42.01  ? 201  PHE   A CE1 1 
ATOM   1580 C  CE2 . PHE   A  1 226 ? -7.981  -21.402 15.756 1.00 36.91  ? 201  PHE   A CE2 1 
ATOM   1581 C  CZ  . PHE   A  1 226 ? -8.829  -22.240 15.055 1.00 42.81  ? 201  PHE   A CZ  1 
ATOM   1582 N  N   . ALA   A  1 227 ? -3.973  -25.274 19.673 1.00 36.51  ? 202  ALA   A N   1 
ATOM   1583 C  CA  . ALA   A  1 227 ? -2.836  -25.987 20.246 1.00 45.81  ? 202  ALA   A CA  1 
ATOM   1584 C  C   . ALA   A  1 227 ? -3.247  -27.349 20.787 1.00 45.16  ? 202  ALA   A C   1 
ATOM   1585 O  O   . ALA   A  1 227 ? -2.502  -28.327 20.651 1.00 49.30  ? 202  ALA   A O   1 
ATOM   1586 C  CB  . ALA   A  1 227 ? -2.186  -25.150 21.347 1.00 35.03  ? 202  ALA   A CB  1 
ATOM   1587 N  N   . ALA   A  1 228 ? -4.424  -27.434 21.407 1.00 39.63  ? 203  ALA   A N   1 
ATOM   1588 C  CA  . ALA   A  1 228 ? -4.890  -28.726 21.895 1.00 41.91  ? 203  ALA   A CA  1 
ATOM   1589 C  C   . ALA   A  1 228 ? -5.182  -29.682 20.746 1.00 52.60  ? 203  ALA   A C   1 
ATOM   1590 O  O   . ALA   A  1 228 ? -4.816  -30.859 20.809 1.00 47.39  ? 203  ALA   A O   1 
ATOM   1591 C  CB  . ALA   A  1 228 ? -6.132  -28.543 22.767 1.00 39.68  ? 203  ALA   A CB  1 
ATOM   1592 N  N   . ALA   A  1 229 ? -5.819  -29.192 19.680 1.00 42.29  ? 204  ALA   A N   1 
ATOM   1593 C  CA  . ALA   A  1 229 ? -6.060  -30.036 18.513 1.00 43.88  ? 204  ALA   A CA  1 
ATOM   1594 C  C   . ALA   A  1 229 ? -4.759  -30.522 17.887 1.00 55.52  ? 204  ALA   A C   1 
ATOM   1595 O  O   . ALA   A  1 229 ? -4.623  -31.705 17.552 1.00 45.89  ? 204  ALA   A O   1 
ATOM   1596 C  CB  . ALA   A  1 229 ? -6.888  -29.271 17.484 1.00 43.51  ? 204  ALA   A CB  1 
ATOM   1597 N  N   . ARG   A  1 230 ? -3.791  -29.619 17.715 1.00 42.09  ? 205  ARG   A N   1 
ATOM   1598 C  CA  . ARG   A  1 230 ? -2.519  -30.006 17.114 1.00 53.59  ? 205  ARG   A CA  1 
ATOM   1599 C  C   . ARG   A  1 230 ? -1.794  -31.045 17.955 1.00 54.99  ? 205  ARG   A C   1 
ATOM   1600 O  O   . ARG   A  1 230 ? -1.224  -32.004 17.419 1.00 64.24  ? 205  ARG   A O   1 
ATOM   1601 C  CB  . ARG   A  1 230 ? -1.619  -28.784 16.911 1.00 53.78  ? 205  ARG   A CB  1 
ATOM   1602 C  CG  . ARG   A  1 230 ? -0.223  -29.160 16.413 1.00 66.78  ? 205  ARG   A CG  1 
ATOM   1603 C  CD  . ARG   A  1 230 ? 0.893   -28.633 17.300 1.00 66.39  ? 205  ARG   A CD  1 
ATOM   1604 N  NE  . ARG   A  1 230 ? 0.910   -27.177 17.365 1.00 65.34  ? 205  ARG   A NE  1 
ATOM   1605 C  CZ  . ARG   A  1 230 ? 0.819   -26.474 18.485 1.00 69.61  ? 205  ARG   A CZ  1 
ATOM   1606 N  NH1 . ARG   A  1 230 ? 0.701   -27.063 19.664 1.00 73.95  ? 205  ARG   A NH1 1 
ATOM   1607 N  NH2 . ARG   A  1 230 ? 0.847   -25.146 18.420 1.00 66.95  ? 205  ARG   A NH2 1 
ATOM   1608 N  N   . ARG   A  1 231 ? -1.815  -30.876 19.279 1.00 49.47  ? 206  ARG   A N   1 
ATOM   1609 C  CA  . ARG   A  1 231 ? -1.116  -31.815 20.147 1.00 53.24  ? 206  ARG   A CA  1 
ATOM   1610 C  C   . ARG   A  1 231 ? -1.795  -33.181 20.092 1.00 63.39  ? 206  ARG   A C   1 
ATOM   1611 O  O   . ARG   A  1 231 ? -1.121  -34.218 20.082 1.00 55.75  ? 206  ARG   A O   1 
ATOM   1612 C  CB  . ARG   A  1 231 ? -1.063  -31.263 21.572 1.00 50.97  ? 206  ARG   A CB  1 
ATOM   1613 C  CG  . ARG   A  1 231 ? -0.361  -32.157 22.574 1.00 67.58  ? 206  ARG   A CG  1 
ATOM   1614 C  CD  . ARG   A  1 231 ? 0.995   -32.469 21.904 1.00 78.40  ? 206  ARG   A CD  1 
ATOM   1615 N  NE  . ARG   A  1 231 ? 1.854   -33.461 22.540 1.00 90.06  ? 206  ARG   A NE  1 
ATOM   1616 C  CZ  . ARG   A  1 231 ? 2.371   -33.342 23.757 1.00 91.33  ? 206  ARG   A CZ  1 
ATOM   1617 N  NH1 . ARG   A  1 231 ? 2.141   -32.276 24.510 1.00 82.30  ? 206  ARG   A NH1 1 
ATOM   1618 N  NH2 . ARG   A  1 231 ? 3.192   -34.287 24.206 1.00 85.98  ? 206  ARG   A NH2 1 
ATOM   1619 N  N   . GLN   A  1 232 ? -3.134  -33.198 20.055 1.00 49.48  ? 207  GLN   A N   1 
ATOM   1620 C  CA  . GLN   A  1 232 ? -3.871  -34.461 20.063 1.00 54.63  ? 207  GLN   A CA  1 
ATOM   1621 C  C   . GLN   A  1 232 ? -3.667  -35.209 18.752 1.00 55.93  ? 207  GLN   A C   1 
ATOM   1622 O  O   . GLN   A  1 232 ? -3.591  -36.442 18.739 1.00 58.58  ? 207  GLN   A O   1 
ATOM   1623 C  CB  . GLN   A  1 232 ? -5.362  -34.231 20.326 1.00 45.29  ? 207  GLN   A CB  1 
ATOM   1624 C  CG  . GLN   A  1 232 ? -5.687  -33.611 21.681 1.00 46.86  ? 207  GLN   A CG  1 
ATOM   1625 C  CD  . GLN   A  1 232 ? -7.185  -33.489 21.934 1.00 52.63  ? 207  GLN   A CD  1 
ATOM   1626 O  OE1 . GLN   A  1 232 ? -7.994  -34.163 21.293 1.00 55.13  ? 207  GLN   A OE1 1 
ATOM   1627 N  NE2 . GLN   A  1 232 ? -7.559  -32.624 22.873 1.00 42.11  ? 207  GLN   A NE2 1 
ATOM   1628 N  N   . LEU   A  1 233 ? -3.601  -34.480 17.635 1.00 53.02  ? 208  LEU   A N   1 
ATOM   1629 C  CA  . LEU   A  1 233 ? -3.307  -35.117 16.356 1.00 51.01  ? 208  LEU   A CA  1 
ATOM   1630 C  C   . LEU   A  1 233 ? -1.909  -35.713 16.373 1.00 62.93  ? 208  LEU   A C   1 
ATOM   1631 O  O   . LEU   A  1 233 ? -1.689  -36.817 15.862 1.00 63.29  ? 208  LEU   A O   1 
ATOM   1632 C  CB  . LEU   A  1 233 ? -3.444  -34.111 15.213 1.00 46.07  ? 208  LEU   A CB  1 
ATOM   1633 C  CG  . LEU   A  1 233 ? -4.847  -33.706 14.767 1.00 67.98  ? 208  LEU   A CG  1 
ATOM   1634 C  CD1 . LEU   A  1 233 ? -4.789  -32.557 13.770 1.00 62.43  ? 208  LEU   A CD1 1 
ATOM   1635 C  CD2 . LEU   A  1 233 ? -5.515  -34.914 14.127 1.00 59.74  ? 208  LEU   A CD2 1 
ATOM   1636 N  N   . ALA   A  1 234 ? -0.947  -34.978 16.939 1.00 55.86  ? 1001 ALA   A N   1 
ATOM   1637 C  CA  . ALA   A  1 234 ? 0.406   -35.498 17.091 1.00 56.21  ? 1001 ALA   A CA  1 
ATOM   1638 C  C   . ALA   A  1 234 ? 0.414   -36.761 17.944 1.00 60.03  ? 1001 ALA   A C   1 
ATOM   1639 O  O   . ALA   A  1 234 ? 1.140   -37.715 17.642 1.00 66.42  ? 1001 ALA   A O   1 
ATOM   1640 C  CB  . ALA   A  1 234 ? 1.316   -34.432 17.702 1.00 50.03  ? 1001 ALA   A CB  1 
ATOM   1641 N  N   . ASP   A  1 235 ? -0.388  -36.783 19.016 1.00 59.66  ? 1002 ASP   A N   1 
ATOM   1642 C  CA  . ASP   A  1 235 ? -0.466  -37.967 19.871 1.00 57.19  ? 1002 ASP   A CA  1 
ATOM   1643 C  C   . ASP   A  1 235 ? -1.012  -39.174 19.116 1.00 63.90  ? 1002 ASP   A C   1 
ATOM   1644 O  O   . ASP   A  1 235 ? -0.563  -40.305 19.339 1.00 64.99  ? 1002 ASP   A O   1 
ATOM   1645 C  CB  . ASP   A  1 235 ? -1.336  -37.691 21.100 1.00 61.24  ? 1002 ASP   A CB  1 
ATOM   1646 C  CG  . ASP   A  1 235 ? -0.712  -36.691 22.048 1.00 78.98  ? 1002 ASP   A CG  1 
ATOM   1647 O  OD1 . ASP   A  1 235 ? 0.524   -36.516 22.002 1.00 84.06  ? 1002 ASP   A OD1 1 
ATOM   1648 O  OD2 . ASP   A  1 235 ? -1.461  -36.090 22.850 1.00 85.31  ? 1002 ASP   A OD2 1 
ATOM   1649 N  N   . LEU   A  1 236 ? -1.984  -38.962 18.225 1.00 59.32  ? 1003 LEU   A N   1 
ATOM   1650 C  CA  . LEU   A  1 236 ? -2.488  -40.068 17.414 1.00 61.17  ? 1003 LEU   A CA  1 
ATOM   1651 C  C   . LEU   A  1 236 ? -1.383  -40.637 16.536 1.00 64.64  ? 1003 LEU   A C   1 
ATOM   1652 O  O   . LEU   A  1 236 ? -1.197  -41.858 16.457 1.00 62.11  ? 1003 LEU   A O   1 
ATOM   1653 C  CB  . LEU   A  1 236 ? -3.666  -39.600 16.561 1.00 62.46  ? 1003 LEU   A CB  1 
ATOM   1654 C  CG  . LEU   A  1 236 ? -4.983  -39.351 17.296 1.00 59.14  ? 1003 LEU   A CG  1 
ATOM   1655 C  CD1 . LEU   A  1 236 ? -5.953  -38.596 16.397 1.00 67.68  ? 1003 LEU   A CD1 1 
ATOM   1656 C  CD2 . LEU   A  1 236 ? -5.594  -40.652 17.791 1.00 60.59  ? 1003 LEU   A CD2 1 
ATOM   1657 N  N   . GLU   A  1 237 ? -0.639  -39.761 15.861 1.00 60.47  ? 1004 GLU   A N   1 
ATOM   1658 C  CA  . GLU   A  1 237 ? 0.428   -40.223 14.984 1.00 72.10  ? 1004 GLU   A CA  1 
ATOM   1659 C  C   . GLU   A  1 237 ? 1.567   -40.843 15.783 1.00 69.89  ? 1004 GLU   A C   1 
ATOM   1660 O  O   . GLU   A  1 237 ? 2.213   -41.783 15.308 1.00 71.59  ? 1004 GLU   A O   1 
ATOM   1661 C  CB  . GLU   A  1 237 ? 0.945   -39.072 14.122 1.00 74.90  ? 1004 GLU   A CB  1 
ATOM   1662 C  CG  . GLU   A  1 237 ? 0.406   -39.068 12.697 1.00 85.54  ? 1004 GLU   A CG  1 
ATOM   1663 C  CD  . GLU   A  1 237 ? 0.852   -40.278 11.896 1.00 92.77  ? 1004 GLU   A CD  1 
ATOM   1664 O  OE1 . GLU   A  1 237 ? 0.045   -40.791 11.091 1.00 92.33  ? 1004 GLU   A OE1 1 
ATOM   1665 O  OE2 . GLU   A  1 237 ? 2.008   -40.717 12.070 1.00 91.76  ? 1004 GLU   A OE2 1 
ATOM   1666 N  N   . ASP   A  1 238 ? 1.833   -40.330 16.989 1.00 64.03  ? 1005 ASP   A N   1 
ATOM   1667 C  CA  . ASP   A  1 238 ? 2.889   -40.913 17.809 1.00 64.79  ? 1005 ASP   A CA  1 
ATOM   1668 C  C   . ASP   A  1 238 ? 2.545   -42.333 18.245 1.00 75.15  ? 1005 ASP   A C   1 
ATOM   1669 O  O   . ASP   A  1 238 ? 3.405   -43.221 18.225 1.00 76.42  ? 1005 ASP   A O   1 
ATOM   1670 C  CB  . ASP   A  1 238 ? 3.103   -40.060 19.061 1.00 61.51  ? 1005 ASP   A CB  1 
ATOM   1671 C  CG  . ASP   A  1 238 ? 3.963   -38.839 18.813 1.00 78.95  ? 1005 ASP   A CG  1 
ATOM   1672 O  OD1 . ASP   A  1 238 ? 4.487   -38.682 17.691 1.00 79.97  ? 1005 ASP   A OD1 1 
ATOM   1673 O  OD2 . ASP   A  1 238 ? 4.128   -38.043 19.763 1.00 92.27  ? 1005 ASP   A OD2 1 
ATOM   1674 N  N   . ASN   A  1 239 ? 1.288   -42.566 18.634 1.00 68.15  ? 1006 ASN   A N   1 
ATOM   1675 C  CA  . ASN   A  1 239 ? 0.854   -43.899 19.036 1.00 70.87  ? 1006 ASN   A CA  1 
ATOM   1676 C  C   . ASN   A  1 239 ? 0.779   -44.855 17.851 1.00 70.19  ? 1006 ASN   A C   1 
ATOM   1677 O  O   . ASN   A  1 239 ? 1.045   -46.054 18.001 1.00 63.44  ? 1006 ASN   A O   1 
ATOM   1678 C  CB  . ASN   A  1 239 ? -0.497  -43.804 19.744 1.00 64.26  ? 1006 ASN   A CB  1 
ATOM   1679 C  CG  . ASN   A  1 239 ? -0.354  -43.729 21.253 1.00 76.16  ? 1006 ASN   A CG  1 
ATOM   1680 O  OD1 . ASN   A  1 239 ? 0.609   -43.156 21.763 1.00 83.59  ? 1006 ASN   A OD1 1 
ATOM   1681 N  ND2 . ASN   A  1 239 ? -1.316  -44.293 21.975 1.00 81.29  ? 1006 ASN   A ND2 1 
ATOM   1682 N  N   . TRP   A  1 240 ? 0.420   -44.346 16.672 1.00 62.45  ? 1007 TRP   A N   1 
ATOM   1683 C  CA  . TRP   A  1 240 ? 0.410   -45.185 15.481 1.00 57.78  ? 1007 TRP   A CA  1 
ATOM   1684 C  C   . TRP   A  1 240 ? 1.818   -45.646 15.121 1.00 71.52  ? 1007 TRP   A C   1 
ATOM   1685 O  O   . TRP   A  1 240 ? 2.043   -46.832 14.848 1.00 69.16  ? 1007 TRP   A O   1 
ATOM   1686 C  CB  . TRP   A  1 240 ? -0.258  -44.419 14.334 1.00 56.92  ? 1007 TRP   A CB  1 
ATOM   1687 C  CG  . TRP   A  1 240 ? -0.320  -45.161 13.041 1.00 65.27  ? 1007 TRP   A CG  1 
ATOM   1688 C  CD1 . TRP   A  1 240 ? 0.390   -44.893 11.909 1.00 60.25  ? 1007 TRP   A CD1 1 
ATOM   1689 C  CD2 . TRP   A  1 240 ? -1.147  -46.293 12.737 1.00 66.41  ? 1007 TRP   A CD2 1 
ATOM   1690 N  NE1 . TRP   A  1 240 ? 0.062   -45.788 10.921 1.00 65.31  ? 1007 TRP   A NE1 1 
ATOM   1691 C  CE2 . TRP   A  1 240 ? -0.879  -46.659 11.404 1.00 69.54  ? 1007 TRP   A CE2 1 
ATOM   1692 C  CE3 . TRP   A  1 240 ? -2.085  -47.034 13.464 1.00 70.89  ? 1007 TRP   A CE3 1 
ATOM   1693 C  CZ2 . TRP   A  1 240 ? -1.513  -47.731 10.781 1.00 70.14  ? 1007 TRP   A CZ2 1 
ATOM   1694 C  CZ3 . TRP   A  1 240 ? -2.714  -48.100 12.844 1.00 71.41  ? 1007 TRP   A CZ3 1 
ATOM   1695 C  CH2 . TRP   A  1 240 ? -2.423  -48.438 11.516 1.00 64.63  ? 1007 TRP   A CH2 1 
ATOM   1696 N  N   . GLU   A  1 241 ? 2.784   -44.725 15.124 1.00 63.81  ? 1008 GLU   A N   1 
ATOM   1697 C  CA  . GLU   A  1 241 ? 4.163   -45.111 14.835 1.00 73.97  ? 1008 GLU   A CA  1 
ATOM   1698 C  C   . GLU   A  1 241 ? 4.723   -46.029 15.919 1.00 63.04  ? 1008 GLU   A C   1 
ATOM   1699 O  O   . GLU   A  1 241 ? 5.443   -46.988 15.612 1.00 65.98  ? 1008 GLU   A O   1 
ATOM   1700 C  CB  . GLU   A  1 241 ? 5.039   -43.890 14.569 1.00 68.35  ? 1008 GLU   A CB  1 
ATOM   1701 C  CG  . GLU   A  1 241 ? 4.510   -43.076 13.376 1.00 81.33  ? 1008 GLU   A CG  1 
ATOM   1702 C  CD  . GLU   A  1 241 ? 5.204   -41.746 13.185 1.00 100.05 ? 1008 GLU   A CD  1 
ATOM   1703 O  OE1 . GLU   A  1 241 ? 5.191   -41.240 12.035 1.00 105.54 ? 1008 GLU   A OE1 1 
ATOM   1704 O  OE2 . GLU   A  1 241 ? 5.810   -41.243 14.149 1.00 104.95 ? 1008 GLU   A OE2 1 
ATOM   1705 N  N   . THR   A  1 242 ? 4.425   -45.739 17.192 1.00 60.74  ? 1009 THR   A N   1 
ATOM   1706 C  CA  . THR   A  1 242 ? 4.912   -46.592 18.276 1.00 62.34  ? 1009 THR   A CA  1 
ATOM   1707 C  C   . THR   A  1 242 ? 4.450   -48.028 18.087 1.00 70.82  ? 1009 THR   A C   1 
ATOM   1708 O  O   . THR   A  1 242 ? 5.228   -48.965 18.311 1.00 61.46  ? 1009 THR   A O   1 
ATOM   1709 C  CB  . THR   A  1 242 ? 4.415   -46.068 19.629 1.00 64.42  ? 1009 THR   A CB  1 
ATOM   1710 O  OG1 . THR   A  1 242 ? 5.111   -44.866 19.970 1.00 73.61  ? 1009 THR   A OG1 1 
ATOM   1711 C  CG2 . THR   A  1 242 ? 4.611   -47.096 20.734 1.00 62.80  ? 1009 THR   A CG2 1 
ATOM   1712 N  N   . LEU   A  1 243 ? 3.198   -48.222 17.657 1.00 60.51  ? 1010 LEU   A N   1 
ATOM   1713 C  CA  . LEU   A  1 243 ? 2.718   -49.570 17.373 1.00 70.29  ? 1010 LEU   A CA  1 
ATOM   1714 C  C   . LEU   A  1 243 ? 3.537   -50.208 16.257 1.00 65.63  ? 1010 LEU   A C   1 
ATOM   1715 O  O   . LEU   A  1 243 ? 4.019   -51.336 16.402 1.00 59.87  ? 1010 LEU   A O   1 
ATOM   1716 C  CB  . LEU   A  1 243 ? 1.228   -49.563 17.024 1.00 63.41  ? 1010 LEU   A CB  1 
ATOM   1717 C  CG  . LEU   A  1 243 ? 0.299   -49.272 18.199 1.00 82.99  ? 1010 LEU   A CG  1 
ATOM   1718 C  CD1 . LEU   A  1 243 ? -1.150  -49.303 17.748 1.00 82.26  ? 1010 LEU   A CD1 1 
ATOM   1719 C  CD2 . LEU   A  1 243 ? 0.548   -50.265 19.329 1.00 80.84  ? 1010 LEU   A CD2 1 
ATOM   1720 N  N   . ASN   A  1 244 ? 3.725   -49.487 15.137 1.00 51.28  ? 1011 ASN   A N   1 
ATOM   1721 C  CA  . ASN   A  1 244 ? 4.402   -50.088 13.988 1.00 63.67  ? 1011 ASN   A CA  1 
ATOM   1722 C  C   . ASN   A  1 244 ? 5.902   -50.220 14.228 1.00 66.06  ? 1011 ASN   A C   1 
ATOM   1723 O  O   . ASN   A  1 244 ? 6.511   -51.207 13.803 1.00 65.10  ? 1011 ASN   A O   1 
ATOM   1724 C  CB  . ASN   A  1 244 ? 4.163   -49.262 12.713 1.00 60.12  ? 1011 ASN   A CB  1 
ATOM   1725 C  CG  . ASN   A  1 244 ? 2.730   -49.340 12.225 1.00 73.96  ? 1011 ASN   A CG  1 
ATOM   1726 O  OD1 . ASN   A  1 244 ? 2.095   -50.384 12.334 1.00 71.86  ? 1011 ASN   A OD1 1 
ATOM   1727 N  ND2 . ASN   A  1 244 ? 2.192   -48.218 11.743 1.00 75.97  ? 1011 ASN   A ND2 1 
ATOM   1728 N  N   . ASP   A  1 245 ? 6.523   -49.246 14.901 1.00 62.83  ? 1012 ASP   A N   1 
ATOM   1729 C  CA  . ASP   A  1 245 ? 7.941   -49.373 15.237 1.00 61.35  ? 1012 ASP   A CA  1 
ATOM   1730 C  C   . ASP   A  1 245 ? 8.198   -50.596 16.110 1.00 64.40  ? 1012 ASP   A C   1 
ATOM   1731 O  O   . ASP   A  1 245 ? 9.104   -51.393 15.838 1.00 66.47  ? 1012 ASP   A O   1 
ATOM   1732 C  CB  . ASP   A  1 245 ? 8.468   -48.103 15.905 1.00 62.85  ? 1012 ASP   A CB  1 
ATOM   1733 C  CG  . ASP   A  1 245 ? 8.502   -46.923 14.954 1.00 76.40  ? 1012 ASP   A CG  1 
ATOM   1734 O  OD1 . ASP   A  1 245 ? 8.491   -47.154 13.725 1.00 76.13  ? 1012 ASP   A OD1 1 
ATOM   1735 O  OD2 . ASP   A  1 245 ? 8.559   -45.770 15.430 1.00 78.93  ? 1012 ASP   A OD2 1 
ATOM   1736 N  N   . ASN   A  1 246 ? 7.421   -50.750 17.182 1.00 59.16  ? 1013 ASN   A N   1 
ATOM   1737 C  CA  . ASN   A  1 246 ? 7.680   -51.839 18.113 1.00 61.04  ? 1013 ASN   A CA  1 
ATOM   1738 C  C   . ASN   A  1 246 ? 7.404   -53.201 17.479 1.00 66.10  ? 1013 ASN   A C   1 
ATOM   1739 O  O   . ASN   A  1 246 ? 8.032   -54.193 17.867 1.00 63.37  ? 1013 ASN   A O   1 
ATOM   1740 C  CB  . ASN   A  1 246 ? 6.850   -51.645 19.382 1.00 58.86  ? 1013 ASN   A CB  1 
ATOM   1741 C  CG  . ASN   A  1 246 ? 7.552   -50.771 20.414 1.00 75.89  ? 1013 ASN   A CG  1 
ATOM   1742 O  OD1 . ASN   A  1 246 ? 6.965   -49.832 20.955 1.00 74.43  ? 1013 ASN   A OD1 1 
ATOM   1743 N  ND2 . ASN   A  1 246 ? 8.817   -51.073 20.683 1.00 63.48  ? 1013 ASN   A ND2 1 
ATOM   1744 N  N   . LEU   A  1 247 ? 6.475   -53.280 16.516 1.00 64.95  ? 1014 LEU   A N   1 
ATOM   1745 C  CA  . LEU   A  1 247 ? 6.322   -54.521 15.754 1.00 67.14  ? 1014 LEU   A CA  1 
ATOM   1746 C  C   . LEU   A  1 247 ? 7.589   -54.878 14.992 1.00 73.80  ? 1014 LEU   A C   1 
ATOM   1747 O  O   . LEU   A  1 247 ? 8.007   -56.041 14.983 1.00 72.89  ? 1014 LEU   A O   1 
ATOM   1748 C  CB  . LEU   A  1 247 ? 5.166   -54.422 14.755 1.00 70.14  ? 1014 LEU   A CB  1 
ATOM   1749 C  CG  . LEU   A  1 247 ? 3.707   -54.594 15.149 1.00 67.97  ? 1014 LEU   A CG  1 
ATOM   1750 C  CD1 . LEU   A  1 247 ? 2.793   -54.207 13.999 1.00 64.47  ? 1014 LEU   A CD1 1 
ATOM   1751 C  CD2 . LEU   A  1 247 ? 3.489   -56.051 15.525 1.00 75.81  ? 1014 LEU   A CD2 1 
ATOM   1752 N  N   . LYS   A  1 248 ? 8.223   -53.887 14.362 1.00 70.53  ? 1015 LYS   A N   1 
ATOM   1753 C  CA  . LYS   A  1 248 ? 9.470   -54.131 13.645 1.00 71.65  ? 1015 LYS   A CA  1 
ATOM   1754 C  C   . LYS   A  1 248 ? 10.576  -54.585 14.588 1.00 71.23  ? 1015 LYS   A C   1 
ATOM   1755 O  O   . LYS   A  1 248 ? 11.362  -55.477 14.246 1.00 74.83  ? 1015 LYS   A O   1 
ATOM   1756 C  CB  . LYS   A  1 248 ? 9.884   -52.880 12.870 1.00 60.84  ? 1015 LYS   A CB  1 
ATOM   1757 C  CG  . LYS   A  1 248 ? 8.885   -52.478 11.794 1.00 73.36  ? 1015 LYS   A CG  1 
ATOM   1758 N  N   . VAL   A  1 249 ? 10.656  -53.976 15.774 1.00 61.02  ? 1016 VAL   A N   1 
ATOM   1759 C  CA  . VAL   A  1 249 ? 11.660  -54.372 16.759 1.00 69.63  ? 1016 VAL   A CA  1 
ATOM   1760 C  C   . VAL   A  1 249 ? 11.520  -55.851 17.098 1.00 76.59  ? 1016 VAL   A C   1 
ATOM   1761 O  O   . VAL   A  1 249 ? 12.514  -56.585 17.171 1.00 70.11  ? 1016 VAL   A O   1 
ATOM   1762 C  CB  . VAL   A  1 249 ? 11.538  -53.486 18.013 1.00 61.76  ? 1016 VAL   A CB  1 
ATOM   1763 C  CG1 . VAL   A  1 249 ? 12.410  -54.019 19.135 1.00 68.59  ? 1016 VAL   A CG1 1 
ATOM   1764 C  CG2 . VAL   A  1 249 ? 11.880  -52.046 17.681 1.00 71.18  ? 1016 VAL   A CG2 1 
ATOM   1765 N  N   . ILE   A  1 250 ? 10.283  -56.314 17.294 1.00 80.60  ? 1017 ILE   A N   1 
ATOM   1766 C  CA  . ILE   A  1 250 ? 10.044  -57.720 17.614 1.00 81.49  ? 1017 ILE   A CA  1 
ATOM   1767 C  C   . ILE   A  1 250 ? 10.469  -58.591 16.444 1.00 77.18  ? 1017 ILE   A C   1 
ATOM   1768 O  O   . ILE   A  1 250 ? 11.058  -59.665 16.620 1.00 83.75  ? 1017 ILE   A O   1 
ATOM   1769 C  CB  . ILE   A  1 250 ? 8.565   -57.942 17.982 1.00 73.54  ? 1017 ILE   A CB  1 
ATOM   1770 C  CG1 . ILE   A  1 250 ? 8.242   -57.250 19.305 1.00 64.52  ? 1017 ILE   A CG1 1 
ATOM   1771 C  CG2 . ILE   A  1 250 ? 8.234   -59.426 18.029 1.00 64.78  ? 1017 ILE   A CG2 1 
ATOM   1772 C  CD1 . ILE   A  1 250 ? 6.767   -57.158 19.587 1.00 67.97  ? 1017 ILE   A CD1 1 
ATOM   1773 N  N   . GLU   A  1 251 ? 10.166  -58.134 15.232 1.00 67.54  ? 1018 GLU   A N   1 
ATOM   1774 C  CA  . GLU   A  1 251 ? 10.465  -58.898 14.030 1.00 69.45  ? 1018 GLU   A CA  1 
ATOM   1775 C  C   . GLU   A  1 251 ? 11.965  -59.150 13.908 1.00 83.92  ? 1018 GLU   A C   1 
ATOM   1776 O  O   . GLU   A  1 251 ? 12.381  -60.247 13.520 1.00 93.37  ? 1018 GLU   A O   1 
ATOM   1777 C  CB  . GLU   A  1 251 ? 9.878   -58.158 12.831 1.00 64.06  ? 1018 GLU   A CB  1 
ATOM   1778 C  CG  . GLU   A  1 251 ? 8.351   -58.260 12.869 1.00 67.98  ? 1018 GLU   A CG  1 
ATOM   1779 C  CD  . GLU   A  1 251 ? 7.640   -57.480 11.789 1.00 72.51  ? 1018 GLU   A CD  1 
ATOM   1780 O  OE1 . GLU   A  1 251 ? 8.086   -57.494 10.625 1.00 83.70  ? 1018 GLU   A OE1 1 
ATOM   1781 O  OE2 . GLU   A  1 251 ? 6.624   -56.835 12.125 1.00 86.84  ? 1018 GLU   A OE2 1 
ATOM   1782 N  N   . LYS   A  1 252 ? 12.798  -58.151 14.217 1.00 82.37  ? 1019 LYS   A N   1 
ATOM   1783 C  CA  . LYS   A  1 252 ? 14.236  -58.335 14.089 1.00 80.89  ? 1019 LYS   A CA  1 
ATOM   1784 C  C   . LYS   A  1 252 ? 14.914  -58.557 15.442 1.00 75.97  ? 1019 LYS   A C   1 
ATOM   1785 O  O   . LYS   A  1 252 ? 16.139  -58.425 15.537 1.00 80.81  ? 1019 LYS   A O   1 
ATOM   1786 C  CB  . LYS   A  1 252 ? 14.861  -57.090 13.454 1.00 80.78  ? 1019 LYS   A CB  1 
ATOM   1787 C  CG  . LYS   A  1 252 ? 14.107  -56.452 12.299 1.00 67.84  ? 1019 LYS   A CG  1 
ATOM   1788 C  CD  . LYS   A  1 252 ? 14.227  -57.211 11.000 1.00 77.54  ? 1019 LYS   A CD  1 
ATOM   1789 C  CE  . LYS   A  1 252 ? 14.753  -56.276 9.921  1.00 85.55  ? 1019 LYS   A CE  1 
ATOM   1790 N  NZ  . LYS   A  1 252 ? 13.776  -55.196 9.596  1.00 90.18  ? 1019 LYS   A NZ  1 
ATOM   1791 N  N   . ALA   A  1 253 ? 14.151  -58.879 16.486 1.00 65.99  ? 1020 ALA   A N   1 
ATOM   1792 C  CA  . ALA   A  1 253 ? 14.712  -59.315 17.762 1.00 79.20  ? 1020 ALA   A CA  1 
ATOM   1793 C  C   . ALA   A  1 253 ? 15.308  -60.721 17.704 1.00 89.98  ? 1020 ALA   A C   1 
ATOM   1794 O  O   . ALA   A  1 253 ? 14.911  -61.554 16.883 1.00 84.77  ? 1020 ALA   A O   1 
ATOM   1795 C  CB  . ALA   A  1 253 ? 13.645  -59.257 18.856 1.00 74.87  ? 1020 ALA   A CB  1 
ATOM   1796 N  N   . ASP   A  1 254 ? 16.281  -60.983 18.589 1.00 88.32  ? 1021 ASP   A N   1 
ATOM   1797 C  CA  . ASP   A  1 254 ? 16.894  -62.305 18.680 1.00 97.26  ? 1021 ASP   A CA  1 
ATOM   1798 C  C   . ASP   A  1 254 ? 16.733  -62.883 20.079 1.00 99.79  ? 1021 ASP   A C   1 
ATOM   1799 O  O   . ASP   A  1 254 ? 17.198  -64.002 20.320 1.00 97.10  ? 1021 ASP   A O   1 
ATOM   1800 C  CB  . ASP   A  1 254 ? 18.397  -62.337 18.359 1.00 103.93 ? 1021 ASP   A CB  1 
ATOM   1801 C  CG  . ASP   A  1 254 ? 19.253  -61.812 19.491 1.00 113.92 ? 1021 ASP   A CG  1 
ATOM   1802 O  OD1 . ASP   A  1 254 ? 18.921  -60.760 20.066 1.00 110.04 ? 1021 ASP   A OD1 1 
ATOM   1803 O  OD2 . ASP   A  1 254 ? 20.232  -62.510 19.848 1.00 107.83 ? 1021 ASP   A OD2 1 
ATOM   1804 N  N   . ASN   A  1 255 ? 16.083  -62.176 21.006 1.00 89.84  ? 1022 ASN   A N   1 
ATOM   1805 C  CA  . ASN   A  1 255 ? 15.827  -62.766 22.309 1.00 86.60  ? 1022 ASN   A CA  1 
ATOM   1806 C  C   . ASN   A  1 255 ? 14.483  -62.354 22.895 1.00 77.51  ? 1022 ASN   A C   1 
ATOM   1807 O  O   . ASN   A  1 255 ? 13.848  -61.389 22.462 1.00 72.54  ? 1022 ASN   A O   1 
ATOM   1808 C  CB  . ASN   A  1 255 ? 16.998  -62.336 23.221 1.00 83.53  ? 1022 ASN   A CB  1 
ATOM   1809 C  CG  . ASN   A  1 255 ? 16.554  -61.798 24.561 1.00 80.67  ? 1022 ASN   A CG  1 
ATOM   1810 O  OD1 . ASN   A  1 255 ? 16.126  -62.539 25.443 1.00 93.47  ? 1022 ASN   A OD1 1 
ATOM   1811 N  ND2 . ASN   A  1 255 ? 16.638  -60.481 24.710 1.00 71.38  ? 1022 ASN   A ND2 1 
ATOM   1812 N  N   . ALA   A  1 256 ? 14.071  -63.125 23.913 1.00 81.92  ? 1023 ALA   A N   1 
ATOM   1813 C  CA  . ALA   A  1 256 ? 12.768  -62.945 24.548 1.00 79.90  ? 1023 ALA   A CA  1 
ATOM   1814 C  C   . ALA   A  1 256 ? 12.660  -61.659 25.353 1.00 82.10  ? 1023 ALA   A C   1 
ATOM   1815 O  O   . ALA   A  1 256 ? 11.563  -61.101 25.470 1.00 85.07  ? 1023 ALA   A O   1 
ATOM   1816 C  CB  . ALA   A  1 256 ? 12.466  -64.146 25.443 1.00 70.18  ? 1023 ALA   A CB  1 
ATOM   1817 N  N   . ALA   A  1 257 ? 13.765  -61.180 25.925 1.00 81.89  ? 1024 ALA   A N   1 
ATOM   1818 C  CA  . ALA   A  1 257 ? 13.688  -59.962 26.723 1.00 76.47  ? 1024 ALA   A CA  1 
ATOM   1819 C  C   . ALA   A  1 257 ? 13.383  -58.765 25.841 1.00 78.17  ? 1024 ALA   A C   1 
ATOM   1820 O  O   . ALA   A  1 257 ? 12.659  -57.847 26.247 1.00 79.77  ? 1024 ALA   A O   1 
ATOM   1821 C  CB  . ALA   A  1 257 ? 14.986  -59.750 27.502 1.00 76.54  ? 1024 ALA   A CB  1 
ATOM   1822 N  N   . GLN   A  1 258 ? 13.930  -58.769 24.626 1.00 71.08  ? 1025 GLN   A N   1 
ATOM   1823 C  CA  . GLN   A  1 258 ? 13.663  -57.702 23.673 1.00 71.61  ? 1025 GLN   A CA  1 
ATOM   1824 C  C   . GLN   A  1 258 ? 12.214  -57.712 23.208 1.00 79.91  ? 1025 GLN   A C   1 
ATOM   1825 O  O   . GLN   A  1 258 ? 11.581  -56.654 23.109 1.00 77.33  ? 1025 GLN   A O   1 
ATOM   1826 C  CB  . GLN   A  1 258 ? 14.588  -57.901 22.478 1.00 66.13  ? 1025 GLN   A CB  1 
ATOM   1827 C  CG  . GLN   A  1 258 ? 16.051  -57.709 22.792 1.00 81.66  ? 1025 GLN   A CG  1 
ATOM   1828 C  CD  . GLN   A  1 258 ? 16.934  -58.076 21.623 1.00 84.50  ? 1025 GLN   A CD  1 
ATOM   1829 O  OE1 . GLN   A  1 258 ? 17.749  -58.991 21.721 1.00 95.40  ? 1025 GLN   A OE1 1 
ATOM   1830 N  NE2 . GLN   A  1 258 ? 16.759  -57.389 20.501 1.00 83.50  ? 1025 GLN   A NE2 1 
ATOM   1831 N  N   . VAL   A  1 259 ? 11.672  -58.899 22.912 1.00 75.67  ? 1026 VAL   A N   1 
ATOM   1832 C  CA  . VAL   A  1 259 ? 10.258  -59.006 22.566 1.00 68.53  ? 1026 VAL   A CA  1 
ATOM   1833 C  C   . VAL   A  1 259 ? 9.386   -58.540 23.723 1.00 66.41  ? 1026 VAL   A C   1 
ATOM   1834 O  O   . VAL   A  1 259 ? 8.417   -57.794 23.531 1.00 71.32  ? 1026 VAL   A O   1 
ATOM   1835 C  CB  . VAL   A  1 259 ? 9.922   -60.445 22.135 1.00 65.81  ? 1026 VAL   A CB  1 
ATOM   1836 C  CG1 . VAL   A  1 259 ? 8.441   -60.576 21.844 1.00 59.96  ? 1026 VAL   A CG1 1 
ATOM   1837 C  CG2 . VAL   A  1 259 ? 10.742  -60.826 20.913 1.00 57.78  ? 1026 VAL   A CG2 1 
ATOM   1838 N  N   . LYS   A  1 260 ? 9.721   -58.970 24.943 1.00 61.20  ? 1027 LYS   A N   1 
ATOM   1839 C  CA  . LYS   A  1 260 ? 8.937   -58.582 26.110 1.00 80.50  ? 1027 LYS   A CA  1 
ATOM   1840 C  C   . LYS   A  1 260 ? 8.985   -57.072 26.287 1.00 77.87  ? 1027 LYS   A C   1 
ATOM   1841 O  O   . LYS   A  1 260 ? 7.960   -56.425 26.533 1.00 73.91  ? 1027 LYS   A O   1 
ATOM   1842 C  CB  . LYS   A  1 260 ? 9.453   -59.312 27.354 1.00 67.41  ? 1027 LYS   A CB  1 
ATOM   1843 C  CG  . LYS   A  1 260 ? 8.863   -58.848 28.681 1.00 71.81  ? 1027 LYS   A CG  1 
ATOM   1844 C  CD  . LYS   A  1 260 ? 9.919   -58.251 29.595 1.00 76.42  ? 1027 LYS   A CD  1 
ATOM   1845 C  CE  . LYS   A  1 260 ? 9.355   -57.996 30.985 1.00 77.60  ? 1027 LYS   A CE  1 
ATOM   1846 N  NZ  . LYS   A  1 260 ? 9.364   -59.234 31.822 1.00 72.24  ? 1027 LYS   A NZ  1 
ATOM   1847 N  N   . ASP   A  1 261 ? 10.189  -56.504 26.189 1.00 80.27  ? 1028 ASP   A N   1 
ATOM   1848 C  CA  . ASP   A  1 261 ? 10.373  -55.066 26.337 1.00 76.43  ? 1028 ASP   A CA  1 
ATOM   1849 C  C   . ASP   A  1 261 ? 9.492   -54.298 25.356 1.00 72.90  ? 1028 ASP   A C   1 
ATOM   1850 O  O   . ASP   A  1 261 ? 8.785   -53.359 25.740 1.00 77.64  ? 1028 ASP   A O   1 
ATOM   1851 C  CB  . ASP   A  1 261 ? 11.847  -54.714 26.138 1.00 81.19  ? 1028 ASP   A CB  1 
ATOM   1852 C  CG  . ASP   A  1 261 ? 12.633  -54.750 27.435 1.00 90.13  ? 1028 ASP   A CG  1 
ATOM   1853 O  OD1 . ASP   A  1 261 ? 12.209  -55.467 28.367 1.00 88.77  ? 1028 ASP   A OD1 1 
ATOM   1854 O  OD2 . ASP   A  1 261 ? 13.681  -54.078 27.516 1.00 102.06 ? 1028 ASP   A OD2 1 
ATOM   1855 N  N   . ALA   A  1 262 ? 9.523   -54.688 24.077 1.00 68.34  ? 1029 ALA   A N   1 
ATOM   1856 C  CA  . ALA   A  1 262 ? 8.761   -53.963 23.065 1.00 69.67  ? 1029 ALA   A CA  1 
ATOM   1857 C  C   . ALA   A  1 262 ? 7.260   -54.152 23.249 1.00 74.96  ? 1029 ALA   A C   1 
ATOM   1858 O  O   . ALA   A  1 262 ? 6.480   -53.222 23.008 1.00 78.42  ? 1029 ALA   A O   1 
ATOM   1859 C  CB  . ALA   A  1 262 ? 9.190   -54.411 21.668 1.00 62.65  ? 1029 ALA   A CB  1 
ATOM   1860 N  N   . LEU   A  1 263 ? 6.831   -55.346 23.665 1.00 62.67  ? 1030 LEU   A N   1 
ATOM   1861 C  CA  . LEU   A  1 263 ? 5.402   -55.582 23.842 1.00 67.44  ? 1030 LEU   A CA  1 
ATOM   1862 C  C   . LEU   A  1 263 ? 4.865   -54.781 25.019 1.00 68.08  ? 1030 LEU   A C   1 
ATOM   1863 O  O   . LEU   A  1 263 ? 3.741   -54.268 24.972 1.00 62.74  ? 1030 LEU   A O   1 
ATOM   1864 C  CB  . LEU   A  1 263 ? 5.122   -57.071 24.033 1.00 73.30  ? 1030 LEU   A CB  1 
ATOM   1865 C  CG  . LEU   A  1 263 ? 5.232   -57.966 22.801 1.00 65.27  ? 1030 LEU   A CG  1 
ATOM   1866 C  CD1 . LEU   A  1 263 ? 5.365   -59.411 23.233 1.00 60.98  ? 1030 LEU   A CD1 1 
ATOM   1867 C  CD2 . LEU   A  1 263 ? 4.026   -57.782 21.893 1.00 52.25  ? 1030 LEU   A CD2 1 
ATOM   1868 N  N   . THR   A  1 264 ? 5.662   -54.668 26.085 1.00 63.16  ? 1031 THR   A N   1 
ATOM   1869 C  CA  . THR   A  1 264 ? 5.266   -53.872 27.240 1.00 72.34  ? 1031 THR   A CA  1 
ATOM   1870 C  C   . THR   A  1 264 ? 5.059   -52.408 26.870 1.00 71.84  ? 1031 THR   A C   1 
ATOM   1871 O  O   . THR   A  1 264 ? 4.225   -51.727 27.477 1.00 64.16  ? 1031 THR   A O   1 
ATOM   1872 C  CB  . THR   A  1 264 ? 6.317   -54.001 28.344 1.00 71.45  ? 1031 THR   A CB  1 
ATOM   1873 O  OG1 . THR   A  1 264 ? 7.619   -54.099 27.754 1.00 80.20  ? 1031 THR   A OG1 1 
ATOM   1874 C  CG2 . THR   A  1 264 ? 6.058   -55.244 29.183 1.00 57.10  ? 1031 THR   A CG2 1 
ATOM   1875 N  N   . LYS   A  1 265 ? 5.804   -51.907 25.880 1.00 62.26  ? 1032 LYS   A N   1 
ATOM   1876 C  CA  . LYS   A  1 265 ? 5.574   -50.555 25.385 1.00 69.86  ? 1032 LYS   A CA  1 
ATOM   1877 C  C   . LYS   A  1 265 ? 4.327   -50.486 24.517 1.00 76.70  ? 1032 LYS   A C   1 
ATOM   1878 O  O   . LYS   A  1 265 ? 3.623   -49.470 24.516 1.00 81.99  ? 1032 LYS   A O   1 
ATOM   1879 C  CB  . LYS   A  1 265 ? 6.765   -50.084 24.559 1.00 69.03  ? 1032 LYS   A CB  1 
ATOM   1880 C  CG  . LYS   A  1 265 ? 8.037   -49.820 25.334 1.00 69.38  ? 1032 LYS   A CG  1 
ATOM   1881 C  CD  . LYS   A  1 265 ? 9.155   -49.454 24.370 1.00 75.07  ? 1032 LYS   A CD  1 
ATOM   1882 C  CE  . LYS   A  1 265 ? 10.402  -48.978 25.095 1.00 78.48  ? 1032 LYS   A CE  1 
ATOM   1883 N  NZ  . LYS   A  1 265 ? 11.491  -48.639 24.133 1.00 77.65  ? 1032 LYS   A NZ  1 
ATOM   1884 N  N   . MET   A  1 266 ? 4.039   -51.564 23.789 1.00 62.01  ? 1033 MET   A N   1 
ATOM   1885 C  CA  . MET   A  1 266 ? 2.821   -51.635 22.993 1.00 69.09  ? 1033 MET   A CA  1 
ATOM   1886 C  C   . MET   A  1 266 ? 1.584   -51.713 23.874 1.00 71.47  ? 1033 MET   A C   1 
ATOM   1887 O  O   . MET   A  1 266 ? 0.543   -51.145 23.532 1.00 70.66  ? 1033 MET   A O   1 
ATOM   1888 C  CB  . MET   A  1 266 ? 2.879   -52.847 22.070 1.00 77.10  ? 1033 MET   A CB  1 
ATOM   1889 C  CG  . MET   A  1 266 ? 3.796   -52.689 20.907 1.00 69.64  ? 1033 MET   A CG  1 
ATOM   1890 S  SD  . MET   A  1 266 ? 3.828   -54.236 20.006 1.00 75.35  ? 1033 MET   A SD  1 
ATOM   1891 C  CE  . MET   A  1 266 ? 3.470   -53.620 18.390 1.00 60.80  ? 1033 MET   A CE  1 
ATOM   1892 N  N   . ARG   A  1 267 ? 1.663   -52.438 24.994 1.00 58.28  ? 1034 ARG   A N   1 
ATOM   1893 C  CA  . ARG   A  1 267 ? 0.468   -52.652 25.804 1.00 64.38  ? 1034 ARG   A CA  1 
ATOM   1894 C  C   . ARG   A  1 267 ? 0.015   -51.353 26.459 1.00 69.13  ? 1034 ARG   A C   1 
ATOM   1895 O  O   . ARG   A  1 267 ? -1.168  -51.000 26.414 1.00 75.73  ? 1034 ARG   A O   1 
ATOM   1896 C  CB  . ARG   A  1 267 ? 0.758   -53.662 26.910 1.00 50.72  ? 1034 ARG   A CB  1 
ATOM   1897 C  CG  . ARG   A  1 267 ? -0.468  -54.214 27.593 1.00 61.00  ? 1034 ARG   A CG  1 
ATOM   1898 C  CD  . ARG   A  1 267 ? -0.079  -54.984 28.831 1.00 57.89  ? 1034 ARG   A CD  1 
ATOM   1899 N  NE  . ARG   A  1 267 ? -1.056  -56.020 29.152 1.00 78.43  ? 1034 ARG   A NE  1 
ATOM   1900 C  CZ  . ARG   A  1 267 ? -2.207  -55.864 29.787 1.00 81.47  ? 1034 ARG   A CZ  1 
ATOM   1901 N  NH1 . ARG   A  1 267 ? -2.615  -54.678 30.209 1.00 74.45  ? 1034 ARG   A NH1 1 
ATOM   1902 N  NH2 . ARG   A  1 267 ? -2.966  -56.933 30.011 1.00 88.84  ? 1034 ARG   A NH2 1 
ATOM   1903 N  N   . ALA   A  1 268 ? 0.958   -50.611 27.046 1.00 76.23  ? 1035 ALA   A N   1 
ATOM   1904 C  CA  . ALA   A  1 268 ? 0.625   -49.313 27.624 1.00 72.72  ? 1035 ALA   A CA  1 
ATOM   1905 C  C   . ALA   A  1 268 ? 0.126   -48.320 26.576 1.00 69.38  ? 1035 ALA   A C   1 
ATOM   1906 O  O   . ALA   A  1 268 ? -0.765  -47.509 26.861 1.00 82.89  ? 1035 ALA   A O   1 
ATOM   1907 C  CB  . ALA   A  1 268 ? 1.849   -48.751 28.350 1.00 71.67  ? 1035 ALA   A CB  1 
ATOM   1908 N  N   . ALA   A  1 269 ? 0.657   -48.380 25.353 1.00 68.95  ? 1036 ALA   A N   1 
ATOM   1909 C  CA  . ALA   A  1 269 ? 0.164   -47.462 24.332 1.00 69.29  ? 1036 ALA   A CA  1 
ATOM   1910 C  C   . ALA   A  1 269 ? -1.226  -47.862 23.862 1.00 82.62  ? 1036 ALA   A C   1 
ATOM   1911 O  O   . ALA   A  1 269 ? -2.071  -46.998 23.600 1.00 85.63  ? 1036 ALA   A O   1 
ATOM   1912 C  CB  . ALA   A  1 269 ? 1.135   -47.410 23.150 1.00 55.16  ? 1036 ALA   A CB  1 
ATOM   1913 N  N   . ALA   A  1 270 ? -1.474  -49.166 23.736 1.00 76.45  ? 1037 ALA   A N   1 
ATOM   1914 C  CA  . ALA   A  1 270 ? -2.785  -49.635 23.306 1.00 73.00  ? 1037 ALA   A CA  1 
ATOM   1915 C  C   . ALA   A  1 270 ? -3.870  -49.252 24.307 1.00 74.01  ? 1037 ALA   A C   1 
ATOM   1916 O  O   . ALA   A  1 270 ? -4.941  -48.767 23.925 1.00 79.55  ? 1037 ALA   A O   1 
ATOM   1917 C  CB  . ALA   A  1 270 ? -2.752  -51.149 23.098 1.00 75.60  ? 1037 ALA   A CB  1 
ATOM   1918 N  N   . LEU   A  1 271 ? -3.610  -49.470 25.603 1.00 77.36  ? 1038 LEU   A N   1 
ATOM   1919 C  CA  . LEU   A  1 271 ? -4.565  -49.056 26.628 1.00 84.44  ? 1038 LEU   A CA  1 
ATOM   1920 C  C   . LEU   A  1 271 ? -4.726  -47.544 26.708 1.00 90.34  ? 1038 LEU   A C   1 
ATOM   1921 O  O   . LEU   A  1 271 ? -5.825  -47.054 26.990 1.00 93.63  ? 1038 LEU   A O   1 
ATOM   1922 C  CB  . LEU   A  1 271 ? -4.083  -49.570 27.987 1.00 77.55  ? 1038 LEU   A CB  1 
ATOM   1923 C  CG  . LEU   A  1 271 ? -3.785  -51.057 28.154 1.00 78.77  ? 1038 LEU   A CG  1 
ATOM   1924 C  CD1 . LEU   A  1 271 ? -3.409  -51.369 29.591 1.00 77.73  ? 1038 LEU   A CD1 1 
ATOM   1925 C  CD2 . LEU   A  1 271 ? -5.003  -51.851 27.762 1.00 87.79  ? 1038 LEU   A CD2 1 
ATOM   1926 N  N   . ASP   A  1 272 ? -3.649  -46.794 26.465 1.00 89.79  ? 1039 ASP   A N   1 
ATOM   1927 C  CA  . ASP   A  1 272 ? -3.726  -45.335 26.483 1.00 89.00  ? 1039 ASP   A CA  1 
ATOM   1928 C  C   . ASP   A  1 272 ? -4.513  -44.795 25.296 1.00 90.62  ? 1039 ASP   A C   1 
ATOM   1929 O  O   . ASP   A  1 272 ? -5.237  -43.800 25.421 1.00 97.96  ? 1039 ASP   A O   1 
ATOM   1930 C  CB  . ASP   A  1 272 ? -2.329  -44.727 26.566 1.00 85.53  ? 1039 ASP   A CB  1 
ATOM   1931 C  CG  . ASP   A  1 272 ? -1.819  -44.658 27.997 1.00 103.17 ? 1039 ASP   A CG  1 
ATOM   1932 O  OD1 . ASP   A  1 272 ? -2.502  -44.029 28.835 1.00 105.60 ? 1039 ASP   A OD1 1 
ATOM   1933 O  OD2 . ASP   A  1 272 ? -0.746  -45.224 28.290 1.00 103.80 ? 1039 ASP   A OD2 1 
ATOM   1934 N  N   . ALA   A  1 273 ? -4.392  -45.451 24.141 1.00 89.49  ? 1040 ALA   A N   1 
ATOM   1935 C  CA  . ALA   A  1 273 ? -5.163  -45.080 22.962 1.00 90.48  ? 1040 ALA   A CA  1 
ATOM   1936 C  C   . ALA   A  1 273 ? -6.598  -45.562 23.047 1.00 90.03  ? 1040 ALA   A C   1 
ATOM   1937 O  O   . ALA   A  1 273 ? -7.447  -45.087 22.284 1.00 87.24  ? 1040 ALA   A O   1 
ATOM   1938 C  CB  . ALA   A  1 273 ? -4.501  -45.638 21.700 1.00 75.25  ? 1040 ALA   A CB  1 
ATOM   1939 N  N   . GLN   A  1 274 ? -6.883  -46.497 23.949 1.00 87.73  ? 1041 GLN   A N   1 
ATOM   1940 C  CA  . GLN   A  1 274 ? -8.251  -46.949 24.138 1.00 91.08  ? 1041 GLN   A CA  1 
ATOM   1941 C  C   . GLN   A  1 274 ? -9.029  -45.936 24.967 1.00 99.73  ? 1041 GLN   A C   1 
ATOM   1942 O  O   . GLN   A  1 274 ? -10.248 -45.806 24.806 1.00 109.89 ? 1041 GLN   A O   1 
ATOM   1943 C  CB  . GLN   A  1 274 ? -8.227  -48.317 24.822 1.00 88.51  ? 1041 GLN   A CB  1 
ATOM   1944 C  CG  . GLN   A  1 274 ? -9.524  -49.089 24.857 1.00 91.18  ? 1041 GLN   A CG  1 
ATOM   1945 C  CD  . GLN   A  1 274 ? -9.314  -50.482 25.421 1.00 97.59  ? 1041 GLN   A CD  1 
ATOM   1946 O  OE1 . GLN   A  1 274 ? -8.332  -50.733 26.122 1.00 99.34  ? 1041 GLN   A OE1 1 
ATOM   1947 N  NE2 . GLN   A  1 274 ? -10.225 -51.396 25.112 1.00 98.40  ? 1041 GLN   A NE2 1 
ATOM   1948 N  N   . LYS   A  1 275 ? -8.332  -45.206 25.836 1.00 92.00  ? 1042 LYS   A N   1 
ATOM   1949 C  CA  . LYS   A  1 275 ? -8.913  -44.164 26.677 1.00 85.36  ? 1042 LYS   A CA  1 
ATOM   1950 C  C   . LYS   A  1 275 ? -9.425  -42.988 25.845 1.00 90.24  ? 1042 LYS   A C   1 
ATOM   1951 O  O   . LYS   A  1 275 ? -10.511 -43.034 25.272 1.00 99.16  ? 1042 LYS   A O   1 
ATOM   1952 C  CB  . LYS   A  1 275 ? -7.886  -43.677 27.701 1.00 87.45  ? 1042 LYS   A CB  1 
ATOM   1953 N  N   . PHE   A  1 294 ? -13.088 -50.768 17.049 1.00 77.83  ? 1061 PHE   A N   1 
ATOM   1954 C  CA  . PHE   A  1 294 ? -13.891 -50.322 18.183 1.00 83.36  ? 1061 PHE   A CA  1 
ATOM   1955 C  C   . PHE   A  1 294 ? -13.360 -50.931 19.471 1.00 80.00  ? 1061 PHE   A C   1 
ATOM   1956 O  O   . PHE   A  1 294 ? -12.164 -51.199 19.592 1.00 76.94  ? 1061 PHE   A O   1 
ATOM   1957 C  CB  . PHE   A  1 294 ? -15.358 -50.708 17.984 1.00 81.50  ? 1061 PHE   A CB  1 
ATOM   1958 N  N   . ARG   A  1 295 ? -14.258 -51.147 20.436 1.00 81.53  ? 1062 ARG   A N   1 
ATOM   1959 C  CA  . ARG   A  1 295 ? -13.840 -51.712 21.714 1.00 77.47  ? 1062 ARG   A CA  1 
ATOM   1960 C  C   . ARG   A  1 295 ? -13.314 -53.118 21.488 1.00 80.51  ? 1062 ARG   A C   1 
ATOM   1961 O  O   . ARG   A  1 295 ? -12.345 -53.549 22.126 1.00 77.95  ? 1062 ARG   A O   1 
ATOM   1962 C  CB  . ARG   A  1 295 ? -15.001 -51.712 22.706 1.00 74.48  ? 1062 ARG   A CB  1 
ATOM   1963 N  N   . HIS   A  1 296 ? -13.966 -53.845 20.580 1.00 66.51  ? 1063 HIS   A N   1 
ATOM   1964 C  CA  . HIS   A  1 296 ? -13.552 -55.192 20.221 1.00 80.71  ? 1063 HIS   A CA  1 
ATOM   1965 C  C   . HIS   A  1 296 ? -12.146 -55.177 19.635 1.00 76.65  ? 1063 HIS   A C   1 
ATOM   1966 O  O   . HIS   A  1 296 ? -11.313 -56.024 19.978 1.00 68.56  ? 1063 HIS   A O   1 
ATOM   1967 C  CB  . HIS   A  1 296 ? -14.559 -55.765 19.222 1.00 69.88  ? 1063 HIS   A CB  1 
ATOM   1968 C  CG  . HIS   A  1 296 ? -14.411 -57.230 18.960 1.00 76.95  ? 1063 HIS   A CG  1 
ATOM   1969 N  ND1 . HIS   A  1 296 ? -14.379 -58.174 19.964 1.00 70.77  ? 1063 HIS   A ND1 1 
ATOM   1970 C  CD2 . HIS   A  1 296 ? -14.302 -57.914 17.796 1.00 80.54  ? 1063 HIS   A CD2 1 
ATOM   1971 C  CE1 . HIS   A  1 296 ? -14.249 -59.376 19.429 1.00 59.90  ? 1063 HIS   A CE1 1 
ATOM   1972 N  NE2 . HIS   A  1 296 ? -14.198 -59.245 18.116 1.00 66.01  ? 1063 HIS   A NE2 1 
ATOM   1973 N  N   . GLY   A  1 297 ? -11.866 -54.218 18.746 1.00 68.88  ? 1064 GLY   A N   1 
ATOM   1974 C  CA  . GLY   A  1 297 ? -10.542 -54.131 18.151 1.00 61.50  ? 1064 GLY   A CA  1 
ATOM   1975 C  C   . GLY   A  1 297 ? -9.444  -53.973 19.186 1.00 60.28  ? 1064 GLY   A C   1 
ATOM   1976 O  O   . GLY   A  1 297 ? -8.409  -54.639 19.112 1.00 62.45  ? 1064 GLY   A O   1 
ATOM   1977 N  N   . PHE   A  1 298 ? -9.655  -53.095 20.171 1.00 60.51  ? 1065 PHE   A N   1 
ATOM   1978 C  CA  . PHE   A  1 298 ? -8.649  -52.920 21.213 1.00 72.84  ? 1065 PHE   A CA  1 
ATOM   1979 C  C   . PHE   A  1 298 ? -8.607  -54.104 22.170 1.00 70.68  ? 1065 PHE   A C   1 
ATOM   1980 O  O   . PHE   A  1 298 ? -7.548  -54.400 22.734 1.00 63.39  ? 1065 PHE   A O   1 
ATOM   1981 C  CB  . PHE   A  1 298 ? -8.910  -51.633 21.995 1.00 76.25  ? 1065 PHE   A CB  1 
ATOM   1982 C  CG  . PHE   A  1 298 ? -8.354  -50.400 21.344 1.00 78.25  ? 1065 PHE   A CG  1 
ATOM   1983 C  CD1 . PHE   A  1 298 ? -9.195  -49.431 20.825 1.00 80.02  ? 1065 PHE   A CD1 1 
ATOM   1984 C  CD2 . PHE   A  1 298 ? -6.985  -50.202 21.273 1.00 70.52  ? 1065 PHE   A CD2 1 
ATOM   1985 C  CE1 . PHE   A  1 298 ? -8.680  -48.295 20.232 1.00 78.28  ? 1065 PHE   A CE1 1 
ATOM   1986 C  CE2 . PHE   A  1 298 ? -6.464  -49.068 20.684 1.00 78.39  ? 1065 PHE   A CE2 1 
ATOM   1987 C  CZ  . PHE   A  1 298 ? -7.313  -48.113 20.162 1.00 75.38  ? 1065 PHE   A CZ  1 
ATOM   1988 N  N   . ASP   A  1 299 ? -9.738  -54.782 22.384 1.00 65.93  ? 1066 ASP   A N   1 
ATOM   1989 C  CA  . ASP   A  1 299 ? -9.714  -55.981 23.216 1.00 65.06  ? 1066 ASP   A CA  1 
ATOM   1990 C  C   . ASP   A  1 299 ? -8.874  -57.076 22.572 1.00 58.17  ? 1066 ASP   A C   1 
ATOM   1991 O  O   . ASP   A  1 299 ? -8.072  -57.736 23.246 1.00 70.30  ? 1066 ASP   A O   1 
ATOM   1992 C  CB  . ASP   A  1 299 ? -11.137 -56.465 23.487 1.00 70.28  ? 1066 ASP   A CB  1 
ATOM   1993 C  CG  . ASP   A  1 299 ? -11.820 -55.672 24.590 1.00 74.97  ? 1066 ASP   A CG  1 
ATOM   1994 O  OD1 . ASP   A  1 299 ? -11.110 -55.119 25.456 1.00 93.38  ? 1066 ASP   A OD1 1 
ATOM   1995 O  OD2 . ASP   A  1 299 ? -13.069 -55.605 24.597 1.00 85.79  ? 1066 ASP   A OD2 1 
ATOM   1996 N  N   . ILE   A  1 300 ? -9.052  -57.285 21.263 1.00 45.34  ? 1067 ILE   A N   1 
ATOM   1997 C  CA  . ILE   A  1 300 ? -8.197  -58.210 20.524 1.00 54.22  ? 1067 ILE   A CA  1 
ATOM   1998 C  C   . ILE   A  1 300 ? -6.743  -57.767 20.601 1.00 60.17  ? 1067 ILE   A C   1 
ATOM   1999 O  O   . ILE   A  1 300 ? -5.842  -58.585 20.817 1.00 57.02  ? 1067 ILE   A O   1 
ATOM   2000 C  CB  . ILE   A  1 300 ? -8.665  -58.353 19.064 1.00 55.61  ? 1067 ILE   A CB  1 
ATOM   2001 C  CG1 . ILE   A  1 300 ? -10.150 -58.707 19.013 1.00 64.20  ? 1067 ILE   A CG1 1 
ATOM   2002 C  CG2 . ILE   A  1 300 ? -7.831  -59.390 18.340 1.00 51.43  ? 1067 ILE   A CG2 1 
ATOM   2003 C  CD1 . ILE   A  1 300 ? -10.779 -58.556 17.646 1.00 54.59  ? 1067 ILE   A CD1 1 
ATOM   2004 N  N   . LEU   A  1 301 ? -6.491  -56.468 20.402 1.00 61.54  ? 1068 LEU   A N   1 
ATOM   2005 C  CA  . LEU   A  1 301 ? -5.113  -55.994 20.325 1.00 55.01  ? 1068 LEU   A CA  1 
ATOM   2006 C  C   . LEU   A  1 301 ? -4.383  -56.260 21.631 1.00 44.17  ? 1068 LEU   A C   1 
ATOM   2007 O  O   . LEU   A  1 301 ? -3.292  -56.837 21.639 1.00 52.69  ? 1068 LEU   A O   1 
ATOM   2008 C  CB  . LEU   A  1 301 ? -5.078  -54.496 20.002 1.00 54.59  ? 1068 LEU   A CB  1 
ATOM   2009 C  CG  . LEU   A  1 301 ? -3.701  -53.917 19.659 1.00 57.10  ? 1068 LEU   A CG  1 
ATOM   2010 C  CD1 . LEU   A  1 301 ? -3.279  -54.361 18.278 1.00 49.80  ? 1068 LEU   A CD1 1 
ATOM   2011 C  CD2 . LEU   A  1 301 ? -3.632  -52.397 19.797 1.00 60.13  ? 1068 LEU   A CD2 1 
ATOM   2012 N  N   . VAL   A  1 302 ? -4.975  -55.842 22.746 1.00 44.40  ? 1069 VAL   A N   1 
ATOM   2013 C  CA  . VAL   A  1 302 ? -4.367  -56.056 24.055 1.00 48.10  ? 1069 VAL   A CA  1 
ATOM   2014 C  C   . VAL   A  1 302 ? -4.256  -57.541 24.381 1.00 55.76  ? 1069 VAL   A C   1 
ATOM   2015 O  O   . VAL   A  1 302 ? -3.251  -57.994 24.944 1.00 51.55  ? 1069 VAL   A O   1 
ATOM   2016 C  CB  . VAL   A  1 302 ? -5.156  -55.295 25.131 1.00 65.58  ? 1069 VAL   A CB  1 
ATOM   2017 C  CG1 . VAL   A  1 302 ? -4.614  -55.610 26.520 1.00 62.67  ? 1069 VAL   A CG1 1 
ATOM   2018 C  CG2 . VAL   A  1 302 ? -5.090  -53.795 24.843 1.00 70.58  ? 1069 VAL   A CG2 1 
ATOM   2019 N  N   . GLY   A  1 303 ? -5.289  -58.320 24.055 1.00 51.45  ? 1070 GLY   A N   1 
ATOM   2020 C  CA  . GLY   A  1 303 ? -5.211  -59.749 24.306 1.00 50.83  ? 1070 GLY   A CA  1 
ATOM   2021 C  C   . GLY   A  1 303 ? -4.092  -60.405 23.527 1.00 50.07  ? 1070 GLY   A C   1 
ATOM   2022 O  O   . GLY   A  1 303 ? -3.380  -61.263 24.051 1.00 53.40  ? 1070 GLY   A O   1 
ATOM   2023 N  N   . GLN   A  1 304 ? -3.917  -60.006 22.266 1.00 48.33  ? 1071 GLN   A N   1 
ATOM   2024 C  CA  . GLN   A  1 304 ? -2.841  -60.568 21.458 1.00 53.95  ? 1071 GLN   A CA  1 
ATOM   2025 C  C   . GLN   A  1 304 ? -1.475  -60.088 21.933 1.00 56.46  ? 1071 GLN   A C   1 
ATOM   2026 O  O   . GLN   A  1 304 ? -0.486  -60.813 21.791 1.00 50.59  ? 1071 GLN   A O   1 
ATOM   2027 C  CB  . GLN   A  1 304 ? -3.050  -60.209 19.989 1.00 52.94  ? 1071 GLN   A CB  1 
ATOM   2028 C  CG  . GLN   A  1 304 ? -4.202  -60.941 19.342 1.00 64.73  ? 1071 GLN   A CG  1 
ATOM   2029 C  CD  . GLN   A  1 304 ? -4.506  -60.437 17.947 1.00 60.12  ? 1071 GLN   A CD  1 
ATOM   2030 O  OE1 . GLN   A  1 304 ? -5.005  -61.173 17.092 1.00 56.92  ? 1071 GLN   A OE1 1 
ATOM   2031 N  NE2 . GLN   A  1 304 ? -4.269  -59.149 17.732 1.00 58.51  ? 1071 GLN   A NE2 1 
ATOM   2032 N  N   . ILE   A  1 305 ? -1.397  -58.880 22.500 1.00 55.65  ? 1072 ILE   A N   1 
ATOM   2033 C  CA  . ILE   A  1 305 ? -0.151  -58.433 23.117 1.00 52.23  ? 1072 ILE   A CA  1 
ATOM   2034 C  C   . ILE   A  1 305 ? 0.136   -59.248 24.371 1.00 52.46  ? 1072 ILE   A C   1 
ATOM   2035 O  O   . ILE   A  1 305 ? 1.276   -59.666 24.612 1.00 47.37  ? 1072 ILE   A O   1 
ATOM   2036 C  CB  . ILE   A  1 305 ? -0.206  -56.920 23.404 1.00 45.61  ? 1072 ILE   A CB  1 
ATOM   2037 C  CG1 . ILE   A  1 305 ? -0.218  -56.135 22.089 1.00 49.88  ? 1072 ILE   A CG1 1 
ATOM   2038 C  CG2 . ILE   A  1 305 ? 0.961   -56.488 24.278 1.00 50.75  ? 1072 ILE   A CG2 1 
ATOM   2039 C  CD1 . ILE   A  1 305 ? -0.533  -54.665 22.247 1.00 57.33  ? 1072 ILE   A CD1 1 
ATOM   2040 N  N   . ASP   A  1 306 ? -0.891  -59.483 25.192 1.00 43.93  ? 1073 ASP   A N   1 
ATOM   2041 C  CA  . ASP   A  1 306 ? -0.717  -60.324 26.371 1.00 53.25  ? 1073 ASP   A CA  1 
ATOM   2042 C  C   . ASP   A  1 306 ? -0.324  -61.745 25.986 1.00 59.88  ? 1073 ASP   A C   1 
ATOM   2043 O  O   . ASP   A  1 306 ? 0.518   -62.361 26.650 1.00 50.55  ? 1073 ASP   A O   1 
ATOM   2044 C  CB  . ASP   A  1 306 ? -1.988  -60.334 27.221 1.00 52.81  ? 1073 ASP   A CB  1 
ATOM   2045 C  CG  . ASP   A  1 306 ? -2.277  -58.990 27.850 1.00 61.89  ? 1073 ASP   A CG  1 
ATOM   2046 O  OD1 . ASP   A  1 306 ? -1.328  -58.192 28.003 1.00 62.85  ? 1073 ASP   A OD1 1 
ATOM   2047 O  OD2 . ASP   A  1 306 ? -3.445  -58.741 28.216 1.00 64.99  ? 1073 ASP   A OD2 1 
ATOM   2048 N  N   . ASP   A  1 307 ? -0.937  -62.291 24.929 1.00 49.38  ? 1074 ASP   A N   1 
ATOM   2049 C  CA  . ASP   A  1 307 ? -0.568  -63.629 24.473 1.00 48.94  ? 1074 ASP   A CA  1 
ATOM   2050 C  C   . ASP   A  1 307 ? 0.920   -63.706 24.162 1.00 54.20  ? 1074 ASP   A C   1 
ATOM   2051 O  O   . ASP   A  1 307 ? 1.616   -64.623 24.614 1.00 50.44  ? 1074 ASP   A O   1 
ATOM   2052 C  CB  . ASP   A  1 307 ? -1.382  -64.009 23.234 1.00 46.84  ? 1074 ASP   A CB  1 
ATOM   2053 C  CG  . ASP   A  1 307 ? -2.854  -64.205 23.533 1.00 49.51  ? 1074 ASP   A CG  1 
ATOM   2054 O  OD1 . ASP   A  1 307 ? -3.222  -64.280 24.724 1.00 52.54  ? 1074 ASP   A OD1 1 
ATOM   2055 O  OD2 . ASP   A  1 307 ? -3.645  -64.284 22.569 1.00 43.63  ? 1074 ASP   A OD2 1 
ATOM   2056 N  N   . ALA   A  1 308 ? 1.428   -62.743 23.390 1.00 48.46  ? 1075 ALA   A N   1 
ATOM   2057 C  CA  . ALA   A  1 308 ? 2.836   -62.771 23.013 1.00 59.24  ? 1075 ALA   A CA  1 
ATOM   2058 C  C   . ALA   A  1 308 ? 3.736   -62.492 24.211 1.00 57.98  ? 1075 ALA   A C   1 
ATOM   2059 O  O   . ALA   A  1 308 ? 4.863   -62.995 24.271 1.00 54.68  ? 1075 ALA   A O   1 
ATOM   2060 C  CB  . ALA   A  1 308 ? 3.100   -61.772 21.888 1.00 50.17  ? 1075 ALA   A CB  1 
ATOM   2061 N  N   . LEU   A  1 309 ? 3.252   -61.696 25.168 1.00 48.03  ? 1076 LEU   A N   1 
ATOM   2062 C  CA  . LEU   A  1 309 ? 4.049   -61.364 26.344 1.00 62.46  ? 1076 LEU   A CA  1 
ATOM   2063 C  C   . LEU   A  1 309 ? 4.249   -62.580 27.238 1.00 58.12  ? 1076 LEU   A C   1 
ATOM   2064 O  O   . LEU   A  1 309 ? 5.356   -62.819 27.734 1.00 62.74  ? 1076 LEU   A O   1 
ATOM   2065 C  CB  . LEU   A  1 309 ? 3.377   -60.232 27.121 1.00 63.56  ? 1076 LEU   A CB  1 
ATOM   2066 C  CG  . LEU   A  1 309 ? 3.984   -58.839 26.965 1.00 62.23  ? 1076 LEU   A CG  1 
ATOM   2067 C  CD1 . LEU   A  1 309 ? 3.076   -57.787 27.581 1.00 63.22  ? 1076 LEU   A CD1 1 
ATOM   2068 C  CD2 . LEU   A  1 309 ? 5.368   -58.788 27.587 1.00 66.85  ? 1076 LEU   A CD2 1 
ATOM   2069 N  N   . LYS   A  1 310 ? 3.183   -63.352 27.465 1.00 56.28  ? 1077 LYS   A N   1 
ATOM   2070 C  CA  . LYS   A  1 310 ? 3.315   -64.597 28.215 1.00 61.25  ? 1077 LYS   A CA  1 
ATOM   2071 C  C   . LYS   A  1 310 ? 4.318   -65.534 27.557 1.00 66.36  ? 1077 LYS   A C   1 
ATOM   2072 O  O   . LYS   A  1 310 ? 5.125   -66.174 28.243 1.00 66.02  ? 1077 LYS   A O   1 
ATOM   2073 C  CB  . LYS   A  1 310 ? 1.954   -65.283 28.337 1.00 55.77  ? 1077 LYS   A CB  1 
ATOM   2074 C  CG  . LYS   A  1 310 ? 2.009   -66.639 29.026 1.00 65.43  ? 1077 LYS   A CG  1 
ATOM   2075 C  CD  . LYS   A  1 310 ? 0.620   -67.158 29.365 1.00 69.08  ? 1077 LYS   A CD  1 
ATOM   2076 N  N   . LEU   A  1 311 ? 4.283   -65.631 26.226 1.00 61.06  ? 1078 LEU   A N   1 
ATOM   2077 C  CA  . LEU   A  1 311 ? 5.259   -66.460 25.530 1.00 60.29  ? 1078 LEU   A CA  1 
ATOM   2078 C  C   . LEU   A  1 311 ? 6.671   -65.914 25.702 1.00 66.05  ? 1078 LEU   A C   1 
ATOM   2079 O  O   . LEU   A  1 311 ? 7.617   -66.680 25.921 1.00 61.85  ? 1078 LEU   A O   1 
ATOM   2080 C  CB  . LEU   A  1 311 ? 4.890   -66.558 24.049 1.00 53.83  ? 1078 LEU   A CB  1 
ATOM   2081 C  CG  . LEU   A  1 311 ? 3.576   -67.288 23.749 1.00 60.25  ? 1078 LEU   A CG  1 
ATOM   2082 C  CD1 . LEU   A  1 311 ? 3.176   -67.121 22.290 1.00 61.06  ? 1078 LEU   A CD1 1 
ATOM   2083 C  CD2 . LEU   A  1 311 ? 3.666   -68.763 24.118 1.00 57.66  ? 1078 LEU   A CD2 1 
ATOM   2084 N  N   . ALA   A  1 312 ? 6.837   -64.592 25.590 1.00 60.97  ? 1079 ALA   A N   1 
ATOM   2085 C  CA  . ALA   A  1 312 ? 8.146   -63.980 25.809 1.00 68.71  ? 1079 ALA   A CA  1 
ATOM   2086 C  C   . ALA   A  1 312 ? 8.693   -64.309 27.195 1.00 70.10  ? 1079 ALA   A C   1 
ATOM   2087 O  O   . ALA   A  1 312 ? 9.852   -64.716 27.339 1.00 76.63  ? 1079 ALA   A O   1 
ATOM   2088 C  CB  . ALA   A  1 312 ? 8.056   -62.467 25.607 1.00 65.65  ? 1079 ALA   A CB  1 
ATOM   2089 N  N   . ASN   A  1 313 ? 7.866   -64.134 28.230 1.00 60.80  ? 1080 ASN   A N   1 
ATOM   2090 C  CA  . ASN   A  1 313 ? 8.290   -64.386 29.605 1.00 68.65  ? 1080 ASN   A CA  1 
ATOM   2091 C  C   . ASN   A  1 313 ? 8.581   -65.856 29.883 1.00 73.53  ? 1080 ASN   A C   1 
ATOM   2092 O  O   . ASN   A  1 313 ? 9.297   -66.159 30.842 1.00 78.52  ? 1080 ASN   A O   1 
ATOM   2093 C  CB  . ASN   A  1 313 ? 7.250   -63.837 30.582 1.00 68.00  ? 1080 ASN   A CB  1 
ATOM   2094 C  CG  . ASN   A  1 313 ? 7.195   -62.320 30.568 1.00 77.87  ? 1080 ASN   A CG  1 
ATOM   2095 O  OD1 . ASN   A  1 313 ? 7.904   -61.673 29.798 1.00 83.64  ? 1080 ASN   A OD1 1 
ATOM   2096 N  ND2 . ASN   A  1 313 ? 6.364   -61.746 31.430 1.00 74.26  ? 1080 ASN   A ND2 1 
ATOM   2097 N  N   . GLU   A  1 314 ? 8.045   -66.772 29.081 1.00 69.97  ? 1081 GLU   A N   1 
ATOM   2098 C  CA  . GLU   A  1 314 ? 8.431   -68.173 29.177 1.00 75.38  ? 1081 GLU   A CA  1 
ATOM   2099 C  C   . GLU   A  1 314 ? 9.695   -68.471 28.383 1.00 71.11  ? 1081 GLU   A C   1 
ATOM   2100 O  O   . GLU   A  1 314 ? 10.093  -69.637 28.287 1.00 74.67  ? 1081 GLU   A O   1 
ATOM   2101 C  CB  . GLU   A  1 314 ? 7.278   -69.089 28.742 1.00 77.97  ? 1081 GLU   A CB  1 
ATOM   2102 C  CG  . GLU   A  1 314 ? 6.090   -69.060 29.709 1.00 72.65  ? 1081 GLU   A CG  1 
ATOM   2103 C  CD  . GLU   A  1 314 ? 4.809   -69.624 29.119 1.00 75.41  ? 1081 GLU   A CD  1 
ATOM   2104 O  OE1 . GLU   A  1 314 ? 4.802   -69.986 27.924 1.00 69.89  ? 1081 GLU   A OE1 1 
ATOM   2105 O  OE2 . GLU   A  1 314 ? 3.811   -69.720 29.865 1.00 93.93  ? 1081 GLU   A OE2 1 
ATOM   2106 N  N   . GLY   A  1 315 ? 10.302  -67.443 27.792 1.00 68.96  ? 1082 GLY   A N   1 
ATOM   2107 C  CA  . GLY   A  1 315 ? 11.503  -67.562 26.988 1.00 74.73  ? 1082 GLY   A CA  1 
ATOM   2108 C  C   . GLY   A  1 315 ? 11.307  -68.191 25.637 1.00 69.10  ? 1082 GLY   A C   1 
ATOM   2109 O  O   . GLY   A  1 315 ? 12.271  -68.701 25.056 1.00 77.97  ? 1082 GLY   A O   1 
ATOM   2110 N  N   . LYS   A  1 316 ? 10.079  -68.216 25.141 1.00 57.03  ? 1083 LYS   A N   1 
ATOM   2111 C  CA  . LYS   A  1 316 ? 9.788   -68.793 23.840 1.00 54.05  ? 1083 LYS   A CA  1 
ATOM   2112 C  C   . LYS   A  1 316 ? 9.678   -67.661 22.820 1.00 61.18  ? 1083 LYS   A C   1 
ATOM   2113 O  O   . LYS   A  1 316 ? 8.594   -67.141 22.547 1.00 67.05  ? 1083 LYS   A O   1 
ATOM   2114 C  CB  . LYS   A  1 316 ? 8.573   -69.695 23.919 1.00 57.67  ? 1083 LYS   A CB  1 
ATOM   2115 C  CG  . LYS   A  1 316 ? 8.601   -70.612 22.764 1.00 73.93  ? 1083 LYS   A CG  1 
ATOM   2116 C  CD  . LYS   A  1 316 ? 7.543   -71.634 22.814 1.00 69.39  ? 1083 LYS   A CD  1 
ATOM   2117 C  CE  . LYS   A  1 316 ? 8.169   -72.919 22.242 1.00 57.04  ? 1083 LYS   A CE  1 
ATOM   2118 N  NZ  . LYS   A  1 316 ? 8.143   -74.055 23.183 1.00 43.68  ? 1083 LYS   A NZ  1 
ATOM   2119 N  N   . VAL   A  1 317 ? 10.834  -67.264 22.281 1.00 50.92  ? 1084 VAL   A N   1 
ATOM   2120 C  CA  . VAL   A  1 317 ? 10.932  -66.069 21.444 1.00 59.86  ? 1084 VAL   A CA  1 
ATOM   2121 C  C   . VAL   A  1 317 ? 10.179  -66.265 20.129 1.00 64.16  ? 1084 VAL   A C   1 
ATOM   2122 O  O   . VAL   A  1 317 ? 9.307   -65.464 19.775 1.00 60.23  ? 1084 VAL   A O   1 
ATOM   2123 C  CB  . VAL   A  1 317 ? 12.410  -65.701 21.216 1.00 66.00  ? 1084 VAL   A CB  1 
ATOM   2124 C  CG1 . VAL   A  1 317 ? 13.220  -66.916 20.734 1.00 67.99  ? 1084 VAL   A CG1 1 
ATOM   2125 C  CG2 . VAL   A  1 317 ? 12.535  -64.544 20.233 1.00 66.29  ? 1084 VAL   A CG2 1 
ATOM   2126 N  N   . LYS   A  1 318 ? 10.525  -67.309 19.373 1.00 58.60  ? 1085 LYS   A N   1 
ATOM   2127 C  CA  . LYS   A  1 318 ? 9.869   -67.570 18.095 1.00 63.04  ? 1085 LYS   A CA  1 
ATOM   2128 C  C   . LYS   A  1 318 ? 8.350   -67.628 18.235 1.00 52.49  ? 1085 LYS   A C   1 
ATOM   2129 O  O   . LYS   A  1 318 ? 7.628   -67.065 17.405 1.00 49.89  ? 1085 LYS   A O   1 
ATOM   2130 C  CB  . LYS   A  1 318 ? 10.426  -68.857 17.485 1.00 53.68  ? 1085 LYS   A CB  1 
ATOM   2131 C  CG  . LYS   A  1 318 ? 11.891  -68.706 17.134 1.00 50.64  ? 1085 LYS   A CG  1 
ATOM   2132 C  CD  . LYS   A  1 318 ? 12.105  -67.928 15.848 1.00 48.12  ? 1085 LYS   A CD  1 
ATOM   2133 C  CE  . LYS   A  1 318 ? 13.573  -67.976 15.457 1.00 53.31  ? 1085 LYS   A CE  1 
ATOM   2134 N  NZ  . LYS   A  1 318 ? 13.783  -67.669 14.028 1.00 61.99  ? 1085 LYS   A NZ  1 
ATOM   2135 N  N   . GLU   A  1 319 ? 7.840   -68.311 19.268 1.00 47.26  ? 1086 GLU   A N   1 
ATOM   2136 C  CA  . GLU   A  1 319 ? 6.389   -68.370 19.443 1.00 61.63  ? 1086 GLU   A CA  1 
ATOM   2137 C  C   . GLU   A  1 319 ? 5.818   -66.992 19.767 1.00 65.31  ? 1086 GLU   A C   1 
ATOM   2138 O  O   . GLU   A  1 319 ? 4.707   -66.656 19.342 1.00 50.70  ? 1086 GLU   A O   1 
ATOM   2139 C  CB  . GLU   A  1 319 ? 6.003   -69.374 20.536 1.00 53.78  ? 1086 GLU   A CB  1 
ATOM   2140 C  CG  . GLU   A  1 319 ? 5.386   -70.675 20.005 1.00 75.87  ? 1086 GLU   A CG  1 
ATOM   2141 C  CD  . GLU   A  1 319 ? 4.415   -71.329 20.984 1.00 81.32  ? 1086 GLU   A CD  1 
ATOM   2142 O  OE1 . GLU   A  1 319 ? 3.205   -71.032 20.901 1.00 86.47  ? 1086 GLU   A OE1 1 
ATOM   2143 O  OE2 . GLU   A  1 319 ? 4.846   -72.159 21.814 1.00 78.96  ? 1086 GLU   A OE2 1 
ATOM   2144 N  N   . ALA   A  1 320 ? 6.563   -66.185 20.525 1.00 56.03  ? 1087 ALA   A N   1 
ATOM   2145 C  CA  . ALA   A  1 320 ? 6.115   -64.834 20.847 1.00 63.82  ? 1087 ALA   A CA  1 
ATOM   2146 C  C   . ALA   A  1 320 ? 6.129   -63.936 19.617 1.00 59.39  ? 1087 ALA   A C   1 
ATOM   2147 O  O   . ALA   A  1 320 ? 5.207   -63.138 19.415 1.00 56.90  ? 1087 ALA   A O   1 
ATOM   2148 C  CB  . ALA   A  1 320 ? 6.990   -64.244 21.952 1.00 54.46  ? 1087 ALA   A CB  1 
ATOM   2149 N  N   . GLN   A  1 321 ? 7.162   -64.058 18.778 1.00 51.09  ? 1088 GLN   A N   1 
ATOM   2150 C  CA  . GLN   A  1 321 ? 7.231   -63.254 17.562 1.00 51.40  ? 1088 GLN   A CA  1 
ATOM   2151 C  C   . GLN   A  1 321 ? 6.120   -63.606 16.581 1.00 62.40  ? 1088 GLN   A C   1 
ATOM   2152 O  O   . GLN   A  1 321 ? 5.581   -62.721 15.906 1.00 64.93  ? 1088 GLN   A O   1 
ATOM   2153 C  CB  . GLN   A  1 321 ? 8.593   -63.442 16.895 1.00 52.23  ? 1088 GLN   A CB  1 
ATOM   2154 C  CG  . GLN   A  1 321 ? 9.768   -62.919 17.697 1.00 53.77  ? 1088 GLN   A CG  1 
ATOM   2155 C  CD  . GLN   A  1 321 ? 11.100  -63.327 17.099 1.00 69.87  ? 1088 GLN   A CD  1 
ATOM   2156 O  OE1 . GLN   A  1 321 ? 11.405  -64.515 16.991 1.00 70.16  ? 1088 GLN   A OE1 1 
ATOM   2157 N  NE2 . GLN   A  1 321 ? 11.897  -62.344 16.699 1.00 66.08  ? 1088 GLN   A NE2 1 
ATOM   2158 N  N   . ALA   A  1 322 ? 5.767   -64.888 16.478 1.00 48.76  ? 1089 ALA   A N   1 
ATOM   2159 C  CA  . ALA   A  1 322 ? 4.645   -65.265 15.626 1.00 56.82  ? 1089 ALA   A CA  1 
ATOM   2160 C  C   . ALA   A  1 322 ? 3.322   -64.729 16.160 1.00 52.82  ? 1089 ALA   A C   1 
ATOM   2161 O  O   . ALA   A  1 322 ? 2.492   -64.235 15.388 1.00 59.16  ? 1089 ALA   A O   1 
ATOM   2162 C  CB  . ALA   A  1 322 ? 4.585   -66.786 15.483 1.00 47.00  ? 1089 ALA   A CB  1 
ATOM   2163 N  N   . ALA   A  1 323 ? 3.098   -64.839 17.473 1.00 50.54  ? 1090 ALA   A N   1 
ATOM   2164 C  CA  . ALA   A  1 323 ? 1.903   -64.258 18.079 1.00 58.42  ? 1090 ALA   A CA  1 
ATOM   2165 C  C   . ALA   A  1 323 ? 1.801   -62.757 17.838 1.00 60.36  ? 1090 ALA   A C   1 
ATOM   2166 O  O   . ALA   A  1 323 ? 0.705   -62.235 17.597 1.00 57.78  ? 1090 ALA   A O   1 
ATOM   2167 C  CB  . ALA   A  1 323 ? 1.885   -64.553 19.578 1.00 46.27  ? 1090 ALA   A CB  1 
ATOM   2168 N  N   . ALA   A  1 324 ? 2.927   -62.042 17.891 1.00 51.84  ? 1091 ALA   A N   1 
ATOM   2169 C  CA  . ALA   A  1 324 ? 2.856   -60.593 17.745 1.00 66.34  ? 1091 ALA   A CA  1 
ATOM   2170 C  C   . ALA   A  1 324 ? 2.585   -60.177 16.312 1.00 66.33  ? 1091 ALA   A C   1 
ATOM   2171 O  O   . ALA   A  1 324 ? 2.046   -59.092 16.073 1.00 68.00  ? 1091 ALA   A O   1 
ATOM   2172 C  CB  . ALA   A  1 324 ? 4.155   -59.948 18.233 1.00 54.77  ? 1091 ALA   A CB  1 
ATOM   2173 N  N   . GLU   A  1 325 ? 2.979   -61.000 15.345 1.00 62.31  ? 1092 GLU   A N   1 
ATOM   2174 C  CA  . GLU   A  1 325 ? 2.671   -60.680 13.956 1.00 64.75  ? 1092 GLU   A CA  1 
ATOM   2175 C  C   . GLU   A  1 325 ? 1.167   -60.703 13.694 1.00 70.06  ? 1092 GLU   A C   1 
ATOM   2176 O  O   . GLU   A  1 325 ? 0.691   -60.045 12.762 1.00 68.32  ? 1092 GLU   A O   1 
ATOM   2177 C  CB  . GLU   A  1 325 ? 3.458   -61.585 13.021 1.00 67.76  ? 1092 GLU   A CB  1 
ATOM   2178 C  CG  . GLU   A  1 325 ? 3.742   -60.869 11.724 1.00 67.92  ? 1092 GLU   A CG  1 
ATOM   2179 C  CD  . GLU   A  1 325 ? 4.828   -59.778 11.911 1.00 72.73  ? 1092 GLU   A CD  1 
ATOM   2180 O  OE1 . GLU   A  1 325 ? 5.132   -59.371 13.064 1.00 79.72  ? 1092 GLU   A OE1 1 
ATOM   2181 O  OE2 . GLU   A  1 325 ? 5.382   -59.319 10.892 1.00 78.29  ? 1092 GLU   A OE2 1 
ATOM   2182 N  N   . GLN   A  1 326 ? 0.418   -61.486 14.480 1.00 62.99  ? 1093 GLN   A N   1 
ATOM   2183 C  CA  . GLN   A  1 326 ? -1.039  -61.513 14.358 1.00 66.06  ? 1093 GLN   A CA  1 
ATOM   2184 C  C   . GLN   A  1 326 ? -1.631  -60.132 14.601 1.00 74.08  ? 1093 GLN   A C   1 
ATOM   2185 O  O   . GLN   A  1 326 ? -2.706  -59.818 14.077 1.00 65.64  ? 1093 GLN   A O   1 
ATOM   2186 C  CB  . GLN   A  1 326 ? -1.638  -62.529 15.331 1.00 59.47  ? 1093 GLN   A CB  1 
ATOM   2187 C  CG  . GLN   A  1 326 ? -1.048  -63.930 15.229 1.00 71.38  ? 1093 GLN   A CG  1 
ATOM   2188 C  CD  . GLN   A  1 326 ? -1.221  -64.535 13.852 1.00 76.03  ? 1093 GLN   A CD  1 
ATOM   2189 O  OE1 . GLN   A  1 326 ? -0.254  -64.962 13.221 1.00 92.89  ? 1093 GLN   A OE1 1 
ATOM   2190 N  NE2 . GLN   A  1 326 ? -2.461  -64.587 13.383 1.00 65.20  ? 1093 GLN   A NE2 1 
ATOM   2191 N  N   . LEU   A  1 327 ? -0.953  -59.316 15.416 1.00 67.78  ? 1094 LEU   A N   1 
ATOM   2192 C  CA  . LEU   A  1 327 ? -1.384  -57.952 15.704 1.00 64.88  ? 1094 LEU   A CA  1 
ATOM   2193 C  C   . LEU   A  1 327 ? -1.629  -57.161 14.429 1.00 60.31  ? 1094 LEU   A C   1 
ATOM   2194 O  O   . LEU   A  1 327 ? -2.454  -56.242 14.419 1.00 65.40  ? 1094 LEU   A O   1 
ATOM   2195 C  CB  . LEU   A  1 327 ? -0.344  -57.241 16.568 1.00 53.53  ? 1094 LEU   A CB  1 
ATOM   2196 C  CG  . LEU   A  1 327 ? -0.191  -57.775 17.988 1.00 58.34  ? 1094 LEU   A CG  1 
ATOM   2197 C  CD1 . LEU   A  1 327 ? 1.083   -57.258 18.627 1.00 60.95  ? 1094 LEU   A CD1 1 
ATOM   2198 C  CD2 . LEU   A  1 327 ? -1.396  -57.367 18.807 1.00 60.27  ? 1094 LEU   A CD2 1 
ATOM   2199 N  N   . LYS   A  1 328 ? -0.920  -57.495 13.350 1.00 55.83  ? 1095 LYS   A N   1 
ATOM   2200 C  CA  . LYS   A  1 328 ? -1.052  -56.730 12.117 1.00 68.19  ? 1095 LYS   A CA  1 
ATOM   2201 C  C   . LYS   A  1 328 ? -2.445  -56.907 11.523 1.00 70.13  ? 1095 LYS   A C   1 
ATOM   2202 O  O   . LYS   A  1 328 ? -3.009  -55.956 10.969 1.00 64.01  ? 1095 LYS   A O   1 
ATOM   2203 C  CB  . LYS   A  1 328 ? 0.018   -57.163 11.112 1.00 60.92  ? 1095 LYS   A CB  1 
ATOM   2204 C  CG  . LYS   A  1 328 ? 1.422   -56.717 11.485 1.00 62.57  ? 1095 LYS   A CG  1 
ATOM   2205 C  CD  . LYS   A  1 328 ? 2.461   -57.193 10.483 1.00 70.34  ? 1095 LYS   A CD  1 
ATOM   2206 C  CE  . LYS   A  1 328 ? 3.830   -56.613 10.796 1.00 71.70  ? 1095 LYS   A CE  1 
ATOM   2207 N  NZ  . LYS   A  1 328 ? 4.351   -55.721 9.734  1.00 92.20  ? 1095 LYS   A NZ  1 
ATOM   2208 N  N   . THR   A  1 329 ? -3.012  -58.113 11.620 1.00 69.62  ? 1096 THR   A N   1 
ATOM   2209 C  CA  . THR   A  1 329 ? -4.385  -58.313 11.171 1.00 72.35  ? 1096 THR   A CA  1 
ATOM   2210 C  C   . THR   A  1 329 ? -5.351  -57.417 11.947 1.00 65.73  ? 1096 THR   A C   1 
ATOM   2211 O  O   . THR   A  1 329 ? -6.261  -56.822 11.354 1.00 71.44  ? 1096 THR   A O   1 
ATOM   2212 C  CB  . THR   A  1 329 ? -4.762  -59.792 11.315 1.00 71.69  ? 1096 THR   A CB  1 
ATOM   2213 O  OG1 . THR   A  1 329 ? -3.909  -60.576 10.465 1.00 70.80  ? 1096 THR   A OG1 1 
ATOM   2214 C  CG2 . THR   A  1 329 ? -6.207  -60.016 10.924 1.00 58.16  ? 1096 THR   A CG2 1 
ATOM   2215 N  N   . THR   A  1 330 ? -5.170  -57.312 13.276 1.00 58.43  ? 1097 THR   A N   1 
ATOM   2216 C  CA  . THR   A  1 330 ? -6.016  -56.436 14.086 1.00 62.25  ? 1097 THR   A CA  1 
ATOM   2217 C  C   . THR   A  1 330 ? -5.777  -54.978 13.760 1.00 69.55  ? 1097 THR   A C   1 
ATOM   2218 O  O   . THR   A  1 330 ? -6.733  -54.201 13.657 1.00 68.11  ? 1097 THR   A O   1 
ATOM   2219 C  CB  . THR   A  1 330 ? -5.759  -56.666 15.579 1.00 59.29  ? 1097 THR   A CB  1 
ATOM   2220 O  OG1 . THR   A  1 330 ? -5.959  -58.044 15.887 1.00 72.98  ? 1097 THR   A OG1 1 
ATOM   2221 C  CG2 . THR   A  1 330 ? -6.687  -55.806 16.455 1.00 57.58  ? 1097 THR   A CG2 1 
ATOM   2222 N  N   . ARG   A  1 331 ? -4.508  -54.603 13.570 1.00 67.00  ? 1098 ARG   A N   1 
ATOM   2223 C  CA  . ARG   A  1 331 ? -4.171  -53.231 13.210 1.00 71.40  ? 1098 ARG   A CA  1 
ATOM   2224 C  C   . ARG   A  1 331 ? -4.824  -52.833 11.897 1.00 70.43  ? 1098 ARG   A C   1 
ATOM   2225 O  O   . ARG   A  1 331 ? -5.393  -51.742 11.789 1.00 62.56  ? 1098 ARG   A O   1 
ATOM   2226 C  CB  . ARG   A  1 331 ? -2.655  -53.049 13.158 1.00 52.52  ? 1098 ARG   A CB  1 
ATOM   2227 C  CG  . ARG   A  1 331 ? -2.234  -51.633 12.839 1.00 61.63  ? 1098 ARG   A CG  1 
ATOM   2228 C  CD  . ARG   A  1 331 ? -0.871  -51.624 12.199 1.00 63.06  ? 1098 ARG   A CD  1 
ATOM   2229 N  NE  . ARG   A  1 331 ? -0.794  -52.493 11.032 1.00 71.75  ? 1098 ARG   A NE  1 
ATOM   2230 C  CZ  . ARG   A  1 331 ? 0.343   -52.930 10.509 1.00 70.85  ? 1098 ARG   A CZ  1 
ATOM   2231 N  NH1 . ARG   A  1 331 ? 1.514   -52.604 11.032 1.00 65.66  ? 1098 ARG   A NH1 1 
ATOM   2232 N  NH2 . ARG   A  1 331 ? 0.305   -53.721 9.442  1.00 72.87  ? 1098 ARG   A NH2 1 
ATOM   2233 N  N   . ASN   A  1 332 ? -4.783  -53.715 10.893 1.00 68.95  ? 1099 ASN   A N   1 
ATOM   2234 C  CA  . ASN   A  1 332 ? -5.357  -53.365 9.597  1.00 66.19  ? 1099 ASN   A CA  1 
ATOM   2235 C  C   . ASN   A  1 332 ? -6.877  -53.316 9.671  1.00 69.59  ? 1099 ASN   A C   1 
ATOM   2236 O  O   . ASN   A  1 332 ? -7.491  -52.385 9.142  1.00 82.15  ? 1099 ASN   A O   1 
ATOM   2237 C  CB  . ASN   A  1 332 ? -4.894  -54.327 8.499  1.00 63.06  ? 1099 ASN   A CB  1 
ATOM   2238 C  CG  . ASN   A  1 332 ? -3.382  -54.352 8.347  1.00 71.05  ? 1099 ASN   A CG  1 
ATOM   2239 O  OD1 . ASN   A  1 332 ? -2.688  -53.470 8.846  1.00 68.63  ? 1099 ASN   A OD1 1 
ATOM   2240 N  ND2 . ASN   A  1 332 ? -2.862  -55.402 7.713  1.00 70.57  ? 1099 ASN   A ND2 1 
ATOM   2241 N  N   . ALA   A  1 333 ? -7.504  -54.307 10.310 1.00 66.96  ? 1100 ALA   A N   1 
ATOM   2242 C  CA  . ALA   A  1 333 ? -8.963  -54.404 10.296 1.00 61.81  ? 1100 ALA   A CA  1 
ATOM   2243 C  C   . ALA   A  1 333 ? -9.641  -53.419 11.248 1.00 67.17  ? 1100 ALA   A C   1 
ATOM   2244 O  O   . ALA   A  1 333 ? -10.788 -53.019 11.009 1.00 68.92  ? 1100 ALA   A O   1 
ATOM   2245 C  CB  . ALA   A  1 333 ? -9.389  -55.831 10.644 1.00 65.03  ? 1100 ALA   A CB  1 
ATOM   2246 N  N   . TYR   A  1 334 ? -8.971  -53.026 12.327 1.00 71.79  ? 1101 TYR   A N   1 
ATOM   2247 C  CA  . TYR   A  1 334 ? -9.616  -52.216 13.352 1.00 64.45  ? 1101 TYR   A CA  1 
ATOM   2248 C  C   . TYR   A  1 334 ? -8.865  -50.918 13.633 1.00 69.05  ? 1101 TYR   A C   1 
ATOM   2249 O  O   . TYR   A  1 334 ? -9.426  -49.830 13.470 1.00 61.72  ? 1101 TYR   A O   1 
ATOM   2250 C  CB  . TYR   A  1 334 ? -9.775  -53.009 14.652 1.00 65.73  ? 1101 TYR   A CB  1 
ATOM   2251 C  CG  . TYR   A  1 334 ? -10.692 -54.207 14.538 1.00 75.12  ? 1101 TYR   A CG  1 
ATOM   2252 N  N   . ILE   A  1 335 ? -7.608  -51.019 14.080 1.00 64.51  ? 1102 ILE   A N   1 
ATOM   2253 C  CA  . ILE   A  1 335 ? -6.945  -49.870 14.698 1.00 56.56  ? 1102 ILE   A CA  1 
ATOM   2254 C  C   . ILE   A  1 335 ? -6.800  -48.707 13.725 1.00 66.06  ? 1102 ILE   A C   1 
ATOM   2255 O  O   . ILE   A  1 335 ? -7.008  -47.545 14.100 1.00 69.23  ? 1102 ILE   A O   1 
ATOM   2256 C  CB  . ILE   A  1 335 ? -5.579  -50.290 15.278 1.00 57.58  ? 1102 ILE   A CB  1 
ATOM   2257 C  CG1 . ILE   A  1 335 ? -5.712  -51.567 16.112 1.00 63.24  ? 1102 ILE   A CG1 1 
ATOM   2258 C  CG2 . ILE   A  1 335 ? -4.983  -49.154 16.097 1.00 52.62  ? 1102 ILE   A CG2 1 
ATOM   2259 C  CD1 . ILE   A  1 335 ? -6.632  -51.437 17.298 1.00 59.62  ? 1102 ILE   A CD1 1 
ATOM   2260 N  N   . GLN   A  1 336 ? -6.436  -48.978 12.470 1.00 60.82  ? 1103 GLN   A N   1 
ATOM   2261 C  CA  . GLN   A  1 336 ? -6.287  -47.849 11.551 1.00 72.17  ? 1103 GLN   A CA  1 
ATOM   2262 C  C   . GLN   A  1 336 ? -7.638  -47.184 11.282 1.00 68.96  ? 1103 GLN   A C   1 
ATOM   2263 O  O   . GLN   A  1 336 ? -7.700  -45.968 11.058 1.00 61.42  ? 1103 GLN   A O   1 
ATOM   2264 C  CB  . GLN   A  1 336 ? -5.558  -48.244 10.263 1.00 66.22  ? 1103 GLN   A CB  1 
ATOM   2265 C  CG  . GLN   A  1 336 ? -5.957  -47.459 9.025  1.00 91.65  ? 1103 GLN   A CG  1 
ATOM   2266 C  CD  . GLN   A  1 336 ? -5.110  -47.831 7.812  1.00 90.14  ? 1103 GLN   A CD  1 
ATOM   2267 O  OE1 . GLN   A  1 336 ? -3.898  -48.085 7.921  1.00 95.05  ? 1103 GLN   A OE1 1 
ATOM   2268 N  NE2 . GLN   A  1 336 ? -5.752  -47.926 6.664  1.00 92.28  ? 1103 GLN   A NE2 1 
ATOM   2269 N  N   . LYS   A  1 337 ? -8.727  -47.961 11.283 1.00 58.14  ? 1104 LYS   A N   1 
ATOM   2270 C  CA  . LYS   A  1 337 ? -10.042 -47.349 11.103 1.00 67.05  ? 1104 LYS   A CA  1 
ATOM   2271 C  C   . LYS   A  1 337 ? -10.362 -46.410 12.254 1.00 65.62  ? 1104 LYS   A C   1 
ATOM   2272 O  O   . LYS   A  1 337 ? -10.916 -45.325 12.042 1.00 59.98  ? 1104 LYS   A O   1 
ATOM   2273 C  CB  . LYS   A  1 337 ? -11.131 -48.415 10.960 1.00 52.00  ? 1104 LYS   A CB  1 
ATOM   2274 N  N   . TYR   A  1 338 ? -10.013 -46.803 13.478 1.00 60.85  ? 1105 TYR   A N   1 
ATOM   2275 C  CA  . TYR   A  1 338 ? -10.201 -45.918 14.623 1.00 59.36  ? 1105 TYR   A CA  1 
ATOM   2276 C  C   . TYR   A  1 338 ? -9.333  -44.671 14.492 1.00 65.98  ? 1105 TYR   A C   1 
ATOM   2277 O  O   . TYR   A  1 338 ? -9.790  -43.549 14.740 1.00 60.32  ? 1105 TYR   A O   1 
ATOM   2278 C  CB  . TYR   A  1 338 ? -9.869  -46.664 15.918 1.00 51.62  ? 1105 TYR   A CB  1 
ATOM   2279 C  CG  . TYR   A  1 338 ? -9.847  -45.795 17.158 1.00 52.99  ? 1105 TYR   A CG  1 
ATOM   2280 N  N   . LEU   A  1 339 ? -8.064  -44.859 14.126 1.00 59.82  ? 1106 LEU   A N   1 
ATOM   2281 C  CA  . LEU   A  1 339 ? -7.148  -43.739 13.922 1.00 56.04  ? 1106 LEU   A CA  1 
ATOM   2282 C  C   . LEU   A  1 339 ? -7.704  -42.725 12.925 1.00 60.68  ? 1106 LEU   A C   1 
ATOM   2283 O  O   . LEU   A  1 339 ? -7.698  -41.514 13.177 1.00 56.74  ? 1106 LEU   A O   1 
ATOM   2284 C  CB  . LEU   A  1 339 ? -5.801  -44.268 13.439 1.00 61.34  ? 1106 LEU   A CB  1 
ATOM   2285 C  CG  . LEU   A  1 339 ? -4.903  -43.248 12.752 1.00 82.01  ? 1106 LEU   A CG  1 
ATOM   2286 C  CD1 . LEU   A  1 339 ? -4.216  -42.434 13.832 1.00 71.66  ? 1106 LEU   A CD1 1 
ATOM   2287 C  CD2 . LEU   A  1 339 ? -3.905  -43.943 11.837 1.00 75.05  ? 1106 LEU   A CD2 1 
ATOM   2288 N  N   . GLU   A  1 340 ? -8.181  -43.209 11.777 1.00 52.00  ? 219  GLU   A N   1 
ATOM   2289 C  CA  . GLU   A  1 340 ? -8.681  -42.313 10.739 1.00 55.59  ? 219  GLU   A CA  1 
ATOM   2290 C  C   . GLU   A  1 340 ? -9.951  -41.590 11.173 1.00 58.80  ? 219  GLU   A C   1 
ATOM   2291 O  O   . GLU   A  1 340 ? -10.132 -40.407 10.861 1.00 57.75  ? 219  GLU   A O   1 
ATOM   2292 C  CB  . GLU   A  1 340 ? -8.915  -43.110 9.457  1.00 54.84  ? 219  GLU   A CB  1 
ATOM   2293 C  CG  . GLU   A  1 340 ? -7.619  -43.566 8.809  1.00 65.90  ? 219  GLU   A CG  1 
ATOM   2294 C  CD  . GLU   A  1 340 ? -7.827  -44.671 7.798  1.00 77.49  ? 219  GLU   A CD  1 
ATOM   2295 O  OE1 . GLU   A  1 340 ? -8.699  -45.533 8.036  1.00 77.55  ? 219  GLU   A OE1 1 
ATOM   2296 O  OE2 . GLU   A  1 340 ? -7.107  -44.691 6.778  1.00 80.63  ? 219  GLU   A OE2 1 
ATOM   2297 N  N   . ARG   A  1 341 ? -10.837 -42.275 11.901 1.00 50.77  ? 220  ARG   A N   1 
ATOM   2298 C  CA  . ARG   A  1 341 ? -12.055 -41.617 12.362 1.00 50.26  ? 220  ARG   A CA  1 
ATOM   2299 C  C   . ARG   A  1 341 ? -11.748 -40.589 13.444 1.00 54.66  ? 220  ARG   A C   1 
ATOM   2300 O  O   . ARG   A  1 341 ? -12.332 -39.499 13.453 1.00 58.35  ? 220  ARG   A O   1 
ATOM   2301 C  CB  . ARG   A  1 341 ? -13.052 -42.656 12.874 1.00 50.19  ? 220  ARG   A CB  1 
ATOM   2302 N  N   . ALA   A  1 342 ? -10.841 -40.918 14.369 1.00 45.80  ? 221  ALA   A N   1 
ATOM   2303 C  CA  . ALA   A  1 342 ? -10.455 -39.945 15.386 1.00 50.18  ? 221  ALA   A CA  1 
ATOM   2304 C  C   . ALA   A  1 342 ? -9.802  -38.730 14.745 1.00 52.15  ? 221  ALA   A C   1 
ATOM   2305 O  O   . ALA   A  1 342 ? -10.095 -37.586 15.112 1.00 54.95  ? 221  ALA   A O   1 
ATOM   2306 C  CB  . ALA   A  1 342 ? -9.514  -40.589 16.401 1.00 46.41  ? 221  ALA   A CB  1 
ATOM   2307 N  N   . ARG   A  1 343 ? -8.901  -38.968 13.793 1.00 48.82  ? 222  ARG   A N   1 
ATOM   2308 C  CA  . ARG   A  1 343 ? -8.296  -37.877 13.039 1.00 53.26  ? 222  ARG   A CA  1 
ATOM   2309 C  C   . ARG   A  1 343 ? -9.346  -37.068 12.286 1.00 58.40  ? 222  ARG   A C   1 
ATOM   2310 O  O   . ARG   A  1 343 ? -9.277  -35.835 12.259 1.00 54.29  ? 222  ARG   A O   1 
ATOM   2311 C  CB  . ARG   A  1 343 ? -7.193  -38.432 12.136 1.00 48.84  ? 222  ARG   A CB  1 
ATOM   2312 C  CG  . ARG   A  1 343 ? -6.435  -37.404 11.318 1.00 61.40  ? 222  ARG   A CG  1 
ATOM   2313 C  CD  . ARG   A  1 343 ? -5.361  -38.081 10.470 1.00 75.13  ? 222  ARG   A CD  1 
ATOM   2314 N  NE  . ARG   A  1 343 ? -4.522  -38.939 11.307 1.00 92.21  ? 222  ARG   A NE  1 
ATOM   2315 C  CZ  . ARG   A  1 343 ? -3.679  -39.860 10.859 1.00 92.30  ? 222  ARG   A CZ  1 
ATOM   2316 N  NH1 . ARG   A  1 343 ? -3.537  -40.097 9.566  1.00 81.04  ? 222  ARG   A NH1 1 
ATOM   2317 N  NH2 . ARG   A  1 343 ? -2.935  -40.538 11.729 1.00 84.57  ? 222  ARG   A NH2 1 
ATOM   2318 N  N   . SER   A  1 344 ? -10.325 -37.738 11.670 1.00 55.34  ? 223  SER   A N   1 
ATOM   2319 C  CA  . SER   A  1 344 ? -11.340 -37.010 10.915 1.00 50.99  ? 223  SER   A CA  1 
ATOM   2320 C  C   . SER   A  1 344 ? -12.207 -36.159 11.837 1.00 52.17  ? 223  SER   A C   1 
ATOM   2321 O  O   . SER   A  1 344 ? -12.594 -35.042 11.474 1.00 54.68  ? 223  SER   A O   1 
ATOM   2322 C  CB  . SER   A  1 344 ? -12.211 -37.983 10.118 1.00 51.46  ? 223  SER   A CB  1 
ATOM   2323 O  OG  . SER   A  1 344 ? -13.383 -37.344 9.636  1.00 63.04  ? 223  SER   A OG  1 
ATOM   2324 N  N   . THR   A  1 345 ? -12.492 -36.656 13.044 1.00 43.88  ? 224  THR   A N   1 
ATOM   2325 C  CA  . THR   A  1 345 ? -13.255 -35.885 14.024 1.00 52.20  ? 224  THR   A CA  1 
ATOM   2326 C  C   . THR   A  1 345 ? -12.478 -34.670 14.511 1.00 47.70  ? 224  THR   A C   1 
ATOM   2327 O  O   . THR   A  1 345 ? -13.038 -33.572 14.623 1.00 43.81  ? 224  THR   A O   1 
ATOM   2328 C  CB  . THR   A  1 345 ? -13.652 -36.771 15.206 1.00 44.38  ? 224  THR   A CB  1 
ATOM   2329 O  OG1 . THR   A  1 345 ? -14.583 -37.766 14.763 1.00 59.93  ? 224  THR   A OG1 1 
ATOM   2330 C  CG2 . THR   A  1 345 ? -14.293 -35.943 16.308 1.00 52.16  ? 224  THR   A CG2 1 
ATOM   2331 N  N   . LEU   A  1 346 ? -11.189 -34.848 14.804 1.00 43.47  ? 225  LEU   A N   1 
ATOM   2332 C  CA  . LEU   A  1 346 ? -10.376 -33.721 15.245 1.00 45.93  ? 225  LEU   A CA  1 
ATOM   2333 C  C   . LEU   A  1 346 ? -10.318 -32.649 14.159 1.00 52.58  ? 225  LEU   A C   1 
ATOM   2334 O  O   . LEU   A  1 346 ? -10.392 -31.452 14.454 1.00 46.64  ? 225  LEU   A O   1 
ATOM   2335 C  CB  . LEU   A  1 346 ? -8.977  -34.220 15.610 1.00 51.93  ? 225  LEU   A CB  1 
ATOM   2336 C  CG  . LEU   A  1 346 ? -8.731  -34.517 17.096 1.00 60.49  ? 225  LEU   A CG  1 
ATOM   2337 C  CD1 . LEU   A  1 346 ? -7.467  -35.353 17.274 1.00 48.05  ? 225  LEU   A CD1 1 
ATOM   2338 C  CD2 . LEU   A  1 346 ? -8.698  -33.265 17.964 1.00 60.06  ? 225  LEU   A CD2 1 
ATOM   2339 N  N   . GLN   A  1 347 ? -10.185 -33.063 12.896 1.00 43.77  ? 226  GLN   A N   1 
ATOM   2340 C  CA  . GLN   A  1 347 ? -10.112 -32.116 11.791 1.00 46.63  ? 226  GLN   A CA  1 
ATOM   2341 C  C   . GLN   A  1 347 ? -11.427 -31.354 11.609 1.00 47.46  ? 226  GLN   A C   1 
ATOM   2342 O  O   . GLN   A  1 347 ? -11.426 -30.180 11.220 1.00 42.70  ? 226  GLN   A O   1 
ATOM   2343 C  CB  . GLN   A  1 347 ? -9.715  -32.843 10.511 1.00 45.88  ? 226  GLN   A CB  1 
ATOM   2344 C  CG  . GLN   A  1 347 ? -8.297  -33.409 10.552 1.00 56.69  ? 226  GLN   A CG  1 
ATOM   2345 C  CD  . GLN   A  1 347 ? -7.979  -34.272 9.349  1.00 76.91  ? 226  GLN   A CD  1 
ATOM   2346 O  OE1 . GLN   A  1 347 ? -8.881  -34.720 8.635  1.00 71.73  ? 226  GLN   A OE1 1 
ATOM   2347 N  NE2 . GLN   A  1 347 ? -6.696  -34.509 9.112  1.00 66.09  ? 226  GLN   A NE2 1 
ATOM   2348 N  N   . LYS   A  1 348 ? -12.555 -32.012 11.873 1.00 44.51  ? 227  LYS   A N   1 
ATOM   2349 C  CA  . LYS   A  1 348 ? -13.859 -31.364 11.828 1.00 46.06  ? 227  LYS   A CA  1 
ATOM   2350 C  C   . LYS   A  1 348 ? -13.995 -30.348 12.955 1.00 42.86  ? 227  LYS   A C   1 
ATOM   2351 O  O   . LYS   A  1 348 ? -14.592 -29.279 12.774 1.00 40.96  ? 227  LYS   A O   1 
ATOM   2352 C  CB  . LYS   A  1 348 ? -14.906 -32.459 11.940 1.00 44.42  ? 227  LYS   A CB  1 
ATOM   2353 C  CG  . LYS   A  1 348 ? -15.053 -33.310 10.725 1.00 55.97  ? 227  LYS   A CG  1 
ATOM   2354 C  CD  . LYS   A  1 348 ? -15.660 -34.661 11.084 1.00 69.79  ? 227  LYS   A CD  1 
ATOM   2355 C  CE  . LYS   A  1 348 ? -16.570 -34.607 12.300 1.00 65.96  ? 227  LYS   A CE  1 
ATOM   2356 N  NZ  . LYS   A  1 348 ? -17.072 -35.983 12.586 1.00 83.90  ? 227  LYS   A NZ  1 
ATOM   2357 N  N   . GLU   A  1 349 ? -13.428 -30.664 14.122 1.00 34.40  ? 228  GLU   A N   1 
ATOM   2358 C  CA  . GLU   A  1 349 ? -13.403 -29.720 15.236 1.00 44.58  ? 228  GLU   A CA  1 
ATOM   2359 C  C   . GLU   A  1 349 ? -12.532 -28.508 14.915 1.00 40.77  ? 228  GLU   A C   1 
ATOM   2360 O  O   . GLU   A  1 349 ? -12.899 -27.373 15.241 1.00 44.65  ? 228  GLU   A O   1 
ATOM   2361 C  CB  . GLU   A  1 349 ? -12.920 -30.425 16.502 1.00 44.09  ? 228  GLU   A CB  1 
ATOM   2362 C  CG  . GLU   A  1 349 ? -14.052 -31.032 17.313 1.00 53.20  ? 228  GLU   A CG  1 
ATOM   2363 C  CD  . GLU   A  1 349 ? -13.569 -31.705 18.577 1.00 50.69  ? 228  GLU   A CD  1 
ATOM   2364 O  OE1 . GLU   A  1 349 ? -13.400 -31.005 19.595 1.00 44.26  ? 228  GLU   A OE1 1 
ATOM   2365 O  OE2 . GLU   A  1 349 ? -13.350 -32.935 18.549 1.00 50.97  ? 228  GLU   A OE2 1 
ATOM   2366 N  N   . VAL   A  1 350 ? -11.372 -28.727 14.287 1.00 38.07  ? 229  VAL   A N   1 
ATOM   2367 C  CA  . VAL   A  1 350 ? -10.555 -27.602 13.835 1.00 41.02  ? 229  VAL   A CA  1 
ATOM   2368 C  C   . VAL   A  1 350 ? -11.349 -26.742 12.861 1.00 39.35  ? 229  VAL   A C   1 
ATOM   2369 O  O   . VAL   A  1 350 ? -11.319 -25.507 12.933 1.00 41.41  ? 229  VAL   A O   1 
ATOM   2370 C  CB  . VAL   A  1 350 ? -9.239  -28.106 13.215 1.00 40.53  ? 229  VAL   A CB  1 
ATOM   2371 C  CG1 . VAL   A  1 350 ? -8.444  -26.946 12.634 1.00 37.85  ? 229  VAL   A CG1 1 
ATOM   2372 C  CG2 . VAL   A  1 350 ? -8.420  -28.849 14.254 1.00 41.05  ? 229  VAL   A CG2 1 
ATOM   2373 N  N   . HIS   A  1 351 ? -12.064 -27.379 11.927 1.00 38.81  ? 230  HIS   A N   1 
ATOM   2374 C  CA  . HIS   A  1 351 ? -12.831 -26.621 10.942 1.00 43.47  ? 230  HIS   A CA  1 
ATOM   2375 C  C   . HIS   A  1 351 ? -13.929 -25.802 11.599 1.00 41.56  ? 230  HIS   A C   1 
ATOM   2376 O  O   . HIS   A  1 351 ? -14.162 -24.648 11.222 1.00 36.10  ? 230  HIS   A O   1 
ATOM   2377 C  CB  . HIS   A  1 351 ? -13.450 -27.558 9.907  1.00 49.66  ? 230  HIS   A CB  1 
ATOM   2378 C  CG  . HIS   A  1 351 ? -14.044 -26.845 8.732  1.00 53.73  ? 230  HIS   A CG  1 
ATOM   2379 N  ND1 . HIS   A  1 351 ? -13.343 -26.575 7.576  1.00 58.92  ? 230  HIS   A ND1 1 
ATOM   2380 C  CD2 . HIS   A  1 351 ? -15.288 -26.343 8.542  1.00 53.51  ? 230  HIS   A CD2 1 
ATOM   2381 C  CE1 . HIS   A  1 351 ? -14.130 -25.938 6.726  1.00 57.89  ? 230  HIS   A CE1 1 
ATOM   2382 N  NE2 . HIS   A  1 351 ? -15.315 -25.784 7.289  1.00 60.47  ? 230  HIS   A NE2 1 
ATOM   2383 N  N   . ALA   A  1 352 ? -14.608 -26.376 12.593 1.00 36.84  ? 231  ALA   A N   1 
ATOM   2384 C  CA  . ALA   A  1 352 ? -15.660 -25.633 13.270 1.00 36.75  ? 231  ALA   A CA  1 
ATOM   2385 C  C   . ALA   A  1 352 ? -15.080 -24.516 14.124 1.00 41.10  ? 231  ALA   A C   1 
ATOM   2386 O  O   . ALA   A  1 352 ? -15.659 -23.426 14.206 1.00 36.16  ? 231  ALA   A O   1 
ATOM   2387 C  CB  . ALA   A  1 352 ? -16.507 -26.581 14.117 1.00 33.48  ? 231  ALA   A CB  1 
ATOM   2388 N  N   . ALA   A  1 353 ? -13.935 -24.763 14.767 1.00 34.32  ? 232  ALA   A N   1 
ATOM   2389 C  CA  . ALA   A  1 353 ? -13.300 -23.708 15.548 1.00 33.77  ? 232  ALA   A CA  1 
ATOM   2390 C  C   . ALA   A  1 353 ? -12.782 -22.589 14.655 1.00 41.50  ? 232  ALA   A C   1 
ATOM   2391 O  O   . ALA   A  1 353 ? -12.839 -21.413 15.033 1.00 37.68  ? 232  ALA   A O   1 
ATOM   2392 C  CB  . ALA   A  1 353 ? -12.168 -24.288 16.395 1.00 31.72  ? 232  ALA   A CB  1 
ATOM   2393 N  N   . LYS   A  1 354 ? -12.275 -22.931 13.466 1.00 35.80  ? 233  LYS   A N   1 
ATOM   2394 C  CA  . LYS   A  1 354 ? -11.850 -21.898 12.526 1.00 37.36  ? 233  LYS   A CA  1 
ATOM   2395 C  C   . LYS   A  1 354 ? -13.032 -21.053 12.073 1.00 37.23  ? 233  LYS   A C   1 
ATOM   2396 O  O   . LYS   A  1 354 ? -12.923 -19.826 11.960 1.00 33.63  ? 233  LYS   A O   1 
ATOM   2397 C  CB  . LYS   A  1 354 ? -11.147 -22.531 11.325 1.00 36.52  ? 233  LYS   A CB  1 
ATOM   2398 N  N   . SER   A  1 355 ? -14.171 -21.697 11.802 1.00 34.96  ? 234  SER   A N   1 
ATOM   2399 C  CA  . SER   A  1 355 ? -15.364 -20.961 11.397 1.00 34.99  ? 234  SER   A CA  1 
ATOM   2400 C  C   . SER   A  1 355 ? -15.809 -20.004 12.492 1.00 35.27  ? 234  SER   A C   1 
ATOM   2401 O  O   . SER   A  1 355 ? -16.149 -18.847 12.219 1.00 34.58  ? 234  SER   A O   1 
ATOM   2402 C  CB  . SER   A  1 355 ? -16.486 -21.936 11.042 1.00 33.85  ? 234  SER   A CB  1 
ATOM   2403 O  OG  . SER   A  1 355 ? -16.093 -22.795 9.987  1.00 40.65  ? 234  SER   A OG  1 
ATOM   2404 N  N   . ALA   A  1 356 ? -15.824 -20.477 13.740 1.00 30.40  ? 235  ALA   A N   1 
ATOM   2405 C  CA  . ALA   A  1 356 ? -16.192 -19.622 14.861 1.00 34.42  ? 235  ALA   A CA  1 
ATOM   2406 C  C   . ALA   A  1 356 ? -15.202 -18.475 15.026 1.00 40.55  ? 235  ALA   A C   1 
ATOM   2407 O  O   . ALA   A  1 356 ? -15.598 -17.342 15.325 1.00 30.91  ? 235  ALA   A O   1 
ATOM   2408 C  CB  . ALA   A  1 356 ? -16.284 -20.449 16.142 1.00 35.78  ? 235  ALA   A CB  1 
ATOM   2409 N  N   . ALA   A  1 357 ? -13.907 -18.754 14.845 1.00 30.45  ? 236  ALA   A N   1 
ATOM   2410 C  CA  . ALA   A  1 357 ? -12.896 -17.710 14.976 1.00 35.45  ? 236  ALA   A CA  1 
ATOM   2411 C  C   . ALA   A  1 357 ? -13.038 -16.650 13.889 1.00 28.00  ? 236  ALA   A C   1 
ATOM   2412 O  O   . ALA   A  1 357 ? -12.771 -15.468 14.133 1.00 30.75  ? 236  ALA   A O   1 
ATOM   2413 C  CB  . ALA   A  1 357 ? -11.498 -18.327 14.944 1.00 30.81  ? 236  ALA   A CB  1 
ATOM   2414 N  N   . ILE   A  1 358 ? -13.427 -17.055 12.677 1.00 25.98  ? 237  ILE   A N   1 
ATOM   2415 C  CA  . ILE   A  1 358 ? -13.668 -16.082 11.614 1.00 26.82  ? 237  ILE   A CA  1 
ATOM   2416 C  C   . ILE   A  1 358 ? -14.773 -15.115 12.019 1.00 28.35  ? 237  ILE   A C   1 
ATOM   2417 O  O   . ILE   A  1 358 ? -14.667 -13.901 11.805 1.00 29.66  ? 237  ILE   A O   1 
ATOM   2418 C  CB  . ILE   A  1 358 ? -13.990 -16.796 10.288 1.00 31.28  ? 237  ILE   A CB  1 
ATOM   2419 C  CG1 . ILE   A  1 358 ? -12.751 -17.523 9.760  1.00 32.26  ? 237  ILE   A CG1 1 
ATOM   2420 C  CG2 . ILE   A  1 358 ? -14.517 -15.804 9.255  1.00 27.78  ? 237  ILE   A CG2 1 
ATOM   2421 C  CD1 . ILE   A  1 358 ? -13.044 -18.481 8.620  1.00 31.39  ? 237  ILE   A CD1 1 
ATOM   2422 N  N   . ILE   A  1 359 ? -15.848 -15.640 12.616 1.00 26.08  ? 238  ILE   A N   1 
ATOM   2423 C  CA  . ILE   A  1 359 ? -16.948 -14.796 13.078 1.00 30.84  ? 238  ILE   A CA  1 
ATOM   2424 C  C   . ILE   A  1 359 ? -16.451 -13.794 14.112 1.00 28.78  ? 238  ILE   A C   1 
ATOM   2425 O  O   . ILE   A  1 359 ? -16.772 -12.601 14.054 1.00 26.51  ? 238  ILE   A O   1 
ATOM   2426 C  CB  . ILE   A  1 359 ? -18.086 -15.664 13.645 1.00 31.89  ? 238  ILE   A CB  1 
ATOM   2427 C  CG1 . ILE   A  1 359 ? -18.611 -16.625 12.577 1.00 45.03  ? 238  ILE   A CG1 1 
ATOM   2428 C  CG2 . ILE   A  1 359 ? -19.208 -14.788 14.175 1.00 30.85  ? 238  ILE   A CG2 1 
ATOM   2429 C  CD1 . ILE   A  1 359 ? -19.583 -15.989 11.622 1.00 41.90  ? 238  ILE   A CD1 1 
ATOM   2430 N  N   . ALA   A  1 360 ? -15.665 -14.270 15.081 1.00 28.72  ? 239  ALA   A N   1 
ATOM   2431 C  CA  . ALA   A  1 360 ? -15.109 -13.372 16.088 1.00 29.28  ? 239  ALA   A CA  1 
ATOM   2432 C  C   . ALA   A  1 360 ? -14.157 -12.363 15.460 1.00 26.41  ? 239  ALA   A C   1 
ATOM   2433 O  O   . ALA   A  1 360 ? -14.139 -11.190 15.851 1.00 24.74  ? 239  ALA   A O   1 
ATOM   2434 C  CB  . ALA   A  1 360 ? -14.399 -14.177 17.177 1.00 26.74  ? 239  ALA   A CB  1 
ATOM   2435 N  N   . GLY   A  1 361 ? -13.350 -12.802 14.492 1.00 25.71  ? 240  GLY   A N   1 
ATOM   2436 C  CA  . GLY   A  1 361 ? -12.434 -11.884 13.836 1.00 27.74  ? 240  GLY   A CA  1 
ATOM   2437 C  C   . GLY   A  1 361 ? -13.140 -10.837 12.995 1.00 28.86  ? 240  GLY   A C   1 
ATOM   2438 O  O   . GLY   A  1 361 ? -12.704 -9.685  12.932 1.00 27.45  ? 240  GLY   A O   1 
ATOM   2439 N  N   . LEU   A  1 362 ? -14.249 -11.215 12.348 1.00 24.16  ? 241  LEU   A N   1 
ATOM   2440 C  CA  . LEU   A  1 362 ? -15.011 -10.248 11.563 1.00 23.68  ? 241  LEU   A CA  1 
ATOM   2441 C  C   . LEU   A  1 362 ? -15.703 -9.217  12.444 1.00 24.22  ? 241  LEU   A C   1 
ATOM   2442 O  O   . LEU   A  1 362 ? -15.833 -8.054  12.045 1.00 25.73  ? 241  LEU   A O   1 
ATOM   2443 C  CB  . LEU   A  1 362 ? -16.041 -10.957 10.682 1.00 24.98  ? 241  LEU   A CB  1 
ATOM   2444 C  CG  . LEU   A  1 362 ? -15.497 -11.682 9.451  1.00 31.94  ? 241  LEU   A CG  1 
ATOM   2445 C  CD1 . LEU   A  1 362 ? -16.588 -12.519 8.808  1.00 39.45  ? 241  LEU   A CD1 1 
ATOM   2446 C  CD2 . LEU   A  1 362 ? -14.925 -10.682 8.458  1.00 38.80  ? 241  LEU   A CD2 1 
ATOM   2447 N  N   . PHE   A  1 363 ? -16.160 -9.620  13.632 1.00 23.15  ? 242  PHE   A N   1 
ATOM   2448 C  CA  . PHE   A  1 363 ? -16.684 -8.649  14.586 1.00 22.95  ? 242  PHE   A CA  1 
ATOM   2449 C  C   . PHE   A  1 363 ? -15.624 -7.606  14.921 1.00 22.93  ? 242  PHE   A C   1 
ATOM   2450 O  O   . PHE   A  1 363 ? -15.898 -6.400  14.925 1.00 23.24  ? 242  PHE   A O   1 
ATOM   2451 C  CB  . PHE   A  1 363 ? -17.173 -9.371  15.847 1.00 19.14  ? 242  PHE   A CB  1 
ATOM   2452 C  CG  . PHE   A  1 363 ? -17.751 -8.454  16.892 1.00 22.79  ? 242  PHE   A CG  1 
ATOM   2453 C  CD1 . PHE   A  1 363 ? -16.933 -7.792  17.796 1.00 20.02  ? 242  PHE   A CD1 1 
ATOM   2454 C  CD2 . PHE   A  1 363 ? -19.121 -8.258  16.966 1.00 23.11  ? 242  PHE   A CD2 1 
ATOM   2455 C  CE1 . PHE   A  1 363 ? -17.473 -6.940  18.751 1.00 26.51  ? 242  PHE   A CE1 1 
ATOM   2456 C  CE2 . PHE   A  1 363 ? -19.668 -7.415  17.923 1.00 26.55  ? 242  PHE   A CE2 1 
ATOM   2457 C  CZ  . PHE   A  1 363 ? -18.843 -6.756  18.816 1.00 24.13  ? 242  PHE   A CZ  1 
ATOM   2458 N  N   . ALA   A  1 364 ? -14.401 -8.058  15.213 1.00 23.48  ? 243  ALA   A N   1 
ATOM   2459 C  CA  . ALA   A  1 364 ? -13.323 -7.126  15.529 1.00 27.14  ? 243  ALA   A CA  1 
ATOM   2460 C  C   . ALA   A  1 364 ? -13.017 -6.219  14.343 1.00 20.61  ? 243  ALA   A C   1 
ATOM   2461 O  O   . ALA   A  1 364 ? -12.861 -5.003  14.503 1.00 25.77  ? 243  ALA   A O   1 
ATOM   2462 C  CB  . ALA   A  1 364 ? -12.074 -7.895  15.958 1.00 22.90  ? 243  ALA   A CB  1 
ATOM   2463 N  N   . LEU   A  1 365 ? -12.942 -6.794  13.140 1.00 23.90  ? 244  LEU   A N   1 
ATOM   2464 C  CA  . LEU   A  1 365 ? -12.618 -6.004  11.957 1.00 26.25  ? 244  LEU   A CA  1 
ATOM   2465 C  C   . LEU   A  1 365 ? -13.673 -4.935  11.694 1.00 31.09  ? 244  LEU   A C   1 
ATOM   2466 O  O   . LEU   A  1 365 ? -13.345 -3.816  11.284 1.00 23.46  ? 244  LEU   A O   1 
ATOM   2467 C  CB  . LEU   A  1 365 ? -12.471 -6.922  10.743 1.00 32.32  ? 244  LEU   A CB  1 
ATOM   2468 C  CG  . LEU   A  1 365 ? -12.066 -6.277  9.415  1.00 44.98  ? 244  LEU   A CG  1 
ATOM   2469 C  CD1 . LEU   A  1 365 ? -10.665 -5.696  9.509  1.00 53.42  ? 244  LEU   A CD1 1 
ATOM   2470 C  CD2 . LEU   A  1 365 ? -12.158 -7.282  8.271  1.00 36.75  ? 244  LEU   A CD2 1 
ATOM   2471 N  N   . CYS   A  1 366 ? -14.947 -5.259  11.932 1.00 23.04  ? 245  CYS   A N   1 
ATOM   2472 C  CA  . CYS   A  1 366 ? -16.025 -4.321  11.639 1.00 24.33  ? 245  CYS   A CA  1 
ATOM   2473 C  C   . CYS   A  1 366 ? -16.183 -3.255  12.718 1.00 22.81  ? 245  CYS   A C   1 
ATOM   2474 O  O   . CYS   A  1 366 ? -16.620 -2.140  12.413 1.00 23.39  ? 245  CYS   A O   1 
ATOM   2475 C  CB  . CYS   A  1 366 ? -17.340 -5.077  11.452 1.00 28.34  ? 245  CYS   A CB  1 
ATOM   2476 S  SG  . CYS   A  1 366 ? -17.396 -6.095  9.958  1.00 29.94  ? 245  CYS   A SG  1 
ATOM   2477 N  N   . TRP   A  1 367 ? -15.876 -3.575  13.976 1.00 18.43  ? 246  TRP   A N   1 
ATOM   2478 C  CA  . TRP   A  1 367 ? -16.077 -2.626  15.066 1.00 22.35  ? 246  TRP   A CA  1 
ATOM   2479 C  C   . TRP   A  1 367 ? -14.840 -1.818  15.430 1.00 20.59  ? 246  TRP   A C   1 
ATOM   2480 O  O   . TRP   A  1 367 ? -14.984 -0.711  15.962 1.00 21.05  ? 246  TRP   A O   1 
ATOM   2481 C  CB  . TRP   A  1 367 ? -16.580 -3.350  16.320 1.00 25.79  ? 246  TRP   A CB  1 
ATOM   2482 C  CG  . TRP   A  1 367 ? -18.028 -3.687  16.263 1.00 21.26  ? 246  TRP   A CG  1 
ATOM   2483 C  CD1 . TRP   A  1 367 ? -18.592 -4.866  15.872 1.00 22.07  ? 246  TRP   A CD1 1 
ATOM   2484 C  CD2 . TRP   A  1 367 ? -19.108 -2.829  16.642 1.00 19.64  ? 246  TRP   A CD2 1 
ATOM   2485 N  NE1 . TRP   A  1 367 ? -19.964 -4.787  15.970 1.00 24.33  ? 246  TRP   A NE1 1 
ATOM   2486 C  CE2 . TRP   A  1 367 ? -20.303 -3.545  16.442 1.00 25.53  ? 246  TRP   A CE2 1 
ATOM   2487 C  CE3 . TRP   A  1 367 ? -19.179 -1.519  17.127 1.00 23.94  ? 246  TRP   A CE3 1 
ATOM   2488 C  CZ2 . TRP   A  1 367 ? -21.556 -2.996  16.711 1.00 23.39  ? 246  TRP   A CZ2 1 
ATOM   2489 C  CZ3 . TRP   A  1 367 ? -20.423 -0.975  17.391 1.00 25.28  ? 246  TRP   A CZ3 1 
ATOM   2490 C  CH2 . TRP   A  1 367 ? -21.594 -1.712  17.182 1.00 23.55  ? 246  TRP   A CH2 1 
ATOM   2491 N  N   . LEU   A  1 368 ? -13.636 -2.332  15.177 1.00 24.18  ? 247  LEU   A N   1 
ATOM   2492 C  CA  . LEU   A  1 368 ? -12.438 -1.606  15.596 1.00 23.63  ? 247  LEU   A CA  1 
ATOM   2493 C  C   . LEU   A  1 368 ? -12.318 -0.215  14.983 1.00 23.59  ? 247  LEU   A C   1 
ATOM   2494 O  O   . LEU   A  1 368 ? -11.879 0.700   15.702 1.00 24.96  ? 247  LEU   A O   1 
ATOM   2495 C  CB  . LEU   A  1 368 ? -11.176 -2.431  15.306 1.00 24.19  ? 247  LEU   A CB  1 
ATOM   2496 C  CG  . LEU   A  1 368 ? -10.789 -3.435  16.393 1.00 27.19  ? 247  LEU   A CG  1 
ATOM   2497 C  CD1 . LEU   A  1 368 ? -9.748  -4.421  15.883 1.00 31.61  ? 247  LEU   A CD1 1 
ATOM   2498 C  CD2 . LEU   A  1 368 ? -10.271 -2.697  17.620 1.00 25.62  ? 247  LEU   A CD2 1 
ATOM   2499 N  N   . PRO   A  1 369 ? -12.657 0.024   13.706 1.00 25.83  ? 248  PRO   A N   1 
ATOM   2500 C  CA  . PRO   A  1 369 ? -12.465 1.382   13.169 1.00 24.99  ? 248  PRO   A CA  1 
ATOM   2501 C  C   . PRO   A  1 369 ? -13.204 2.447   13.960 1.00 20.84  ? 248  PRO   A C   1 
ATOM   2502 O  O   . PRO   A  1 369 ? -12.626 3.499   14.258 1.00 22.49  ? 248  PRO   A O   1 
ATOM   2503 C  CB  . PRO   A  1 369 ? -12.990 1.249   11.733 1.00 22.66  ? 248  PRO   A CB  1 
ATOM   2504 C  CG  . PRO   A  1 369 ? -12.642 -0.148  11.381 1.00 23.29  ? 248  PRO   A CG  1 
ATOM   2505 C  CD  . PRO   A  1 369 ? -13.028 -0.910  12.624 1.00 19.70  ? 248  PRO   A CD  1 
ATOM   2506 N  N   . LEU   A  1 370 ? -14.470 2.205   14.315 1.00 18.43  ? 249  LEU   A N   1 
ATOM   2507 C  CA  . LEU   A  1 370 ? -15.214 3.191   15.097 1.00 21.14  ? 249  LEU   A CA  1 
ATOM   2508 C  C   . LEU   A  1 370 ? -14.590 3.403   16.470 1.00 19.77  ? 249  LEU   A C   1 
ATOM   2509 O  O   . LEU   A  1 370 ? -14.471 4.543   16.935 1.00 21.10  ? 249  LEU   A O   1 
ATOM   2510 C  CB  . LEU   A  1 370 ? -16.673 2.763   15.238 1.00 16.92  ? 249  LEU   A CB  1 
ATOM   2511 C  CG  . LEU   A  1 370 ? -17.659 3.826   15.736 1.00 24.24  ? 249  LEU   A CG  1 
ATOM   2512 C  CD1 . LEU   A  1 370 ? -17.498 5.153   15.004 1.00 28.55  ? 249  LEU   A CD1 1 
ATOM   2513 C  CD2 . LEU   A  1 370 ? -19.083 3.306   15.600 1.00 20.07  ? 249  LEU   A CD2 1 
ATOM   2514 N  N   . HIS   A  1 371 ? -14.191 2.317   17.136 1.00 19.72  ? 250  HIS   A N   1 
ATOM   2515 C  CA  . HIS   A  1 371 ? -13.530 2.447   18.432 1.00 22.34  ? 250  HIS   A CA  1 
ATOM   2516 C  C   . HIS   A  1 371 ? -12.203 3.186   18.310 1.00 18.83  ? 250  HIS   A C   1 
ATOM   2517 O  O   . HIS   A  1 371 ? -11.874 4.027   19.153 1.00 19.23  ? 250  HIS   A O   1 
ATOM   2518 C  CB  . HIS   A  1 371 ? -13.328 1.070   19.065 1.00 21.77  ? 250  HIS   A CB  1 
ATOM   2519 C  CG  . HIS   A  1 371 ? -14.592 0.453   19.580 1.00 20.40  ? 250  HIS   A CG  1 
ATOM   2520 N  ND1 . HIS   A  1 371 ? -15.289 0.970   20.650 1.00 21.50  ? 250  HIS   A ND1 1 
ATOM   2521 C  CD2 . HIS   A  1 371 ? -15.273 -0.649  19.186 1.00 24.00  ? 250  HIS   A CD2 1 
ATOM   2522 C  CE1 . HIS   A  1 371 ? -16.353 0.222   20.884 1.00 23.43  ? 250  HIS   A CE1 1 
ATOM   2523 N  NE2 . HIS   A  1 371 ? -16.364 -0.769  20.012 1.00 22.48  ? 250  HIS   A NE2 1 
ATOM   2524 N  N   . ILE   A  1 372 ? -11.416 2.866   17.281 1.00 19.17  ? 251  ILE   A N   1 
ATOM   2525 C  CA  . ILE   A  1 372 ? -10.136 3.542   17.085 1.00 20.85  ? 251  ILE   A CA  1 
ATOM   2526 C  C   . ILE   A  1 372 ? -10.345 5.033   16.846 1.00 18.71  ? 251  ILE   A C   1 
ATOM   2527 O  O   . ILE   A  1 372 ? -9.610  5.870   17.383 1.00 20.93  ? 251  ILE   A O   1 
ATOM   2528 C  CB  . ILE   A  1 372 ? -9.347  2.875   15.943 1.00 21.67  ? 251  ILE   A CB  1 
ATOM   2529 C  CG1 . ILE   A  1 372 ? -8.926  1.461   16.356 1.00 20.49  ? 251  ILE   A CG1 1 
ATOM   2530 C  CG2 . ILE   A  1 372 ? -8.139  3.718   15.552 1.00 24.84  ? 251  ILE   A CG2 1 
ATOM   2531 C  CD1 . ILE   A  1 372 ? -8.306  0.650   15.235 1.00 26.10  ? 251  ILE   A CD1 1 
ATOM   2532 N  N   . ILE   A  1 373 ? -11.342 5.391   16.033 1.00 19.20  ? 252  ILE   A N   1 
ATOM   2533 C  CA  . ILE   A  1 373 ? -11.655 6.803   15.832 1.00 19.42  ? 252  ILE   A CA  1 
ATOM   2534 C  C   . ILE   A  1 373 ? -11.989 7.474   17.159 1.00 23.47  ? 252  ILE   A C   1 
ATOM   2535 O  O   . ILE   A  1 373 ? -11.516 8.582   17.445 1.00 22.89  ? 252  ILE   A O   1 
ATOM   2536 C  CB  . ILE   A  1 373 ? -12.804 6.966   14.819 1.00 23.52  ? 252  ILE   A CB  1 
ATOM   2537 C  CG1 . ILE   A  1 373 ? -12.354 6.561   13.416 1.00 22.61  ? 252  ILE   A CG1 1 
ATOM   2538 C  CG2 . ILE   A  1 373 ? -13.318 8.399   14.825 1.00 18.49  ? 252  ILE   A CG2 1 
ATOM   2539 C  CD1 . ILE   A  1 373 ? -13.496 6.440   12.435 1.00 27.98  ? 252  ILE   A CD1 1 
ATOM   2540 N  N   . ASN   A  1 374 ? -12.803 6.816   17.992 1.00 21.54  ? 253  ASN   A N   1 
ATOM   2541 C  CA  . ASN   A  1 374 ? -13.103 7.363   19.313 1.00 19.90  ? 253  ASN   A CA  1 
ATOM   2542 C  C   . ASN   A  1 374 ? -11.833 7.590   20.120 1.00 23.24  ? 253  ASN   A C   1 
ATOM   2543 O  O   . ASN   A  1 374 ? -11.736 8.565   20.874 1.00 19.52  ? 253  ASN   A O   1 
ATOM   2544 C  CB  . ASN   A  1 374 ? -14.057 6.443   20.074 1.00 20.18  ? 253  ASN   A CB  1 
ATOM   2545 C  CG  . ASN   A  1 374 ? -15.467 6.505   19.534 1.00 24.94  ? 253  ASN   A CG  1 
ATOM   2546 O  OD1 . ASN   A  1 374 ? -15.824 7.448   18.836 1.00 24.84  ? 253  ASN   A OD1 1 
ATOM   2547 N  ND2 . ASN   A  1 374 ? -16.283 5.516   19.877 1.00 24.30  ? 253  ASN   A ND2 1 
ATOM   2548 N  N   . CYS   A  1 375 ? -10.849 6.699   19.979 1.00 19.61  ? 254  CYS   A N   1 
ATOM   2549 C  CA  . CYS   A  1 375 ? -9.591  6.887   20.692 1.00 22.80  ? 254  CYS   A CA  1 
ATOM   2550 C  C   . CYS   A  1 375 ? -8.880  8.147   20.214 1.00 18.39  ? 254  CYS   A C   1 
ATOM   2551 O  O   . CYS   A  1 375 ? -8.317  8.895   21.023 1.00 23.24  ? 254  CYS   A O   1 
ATOM   2552 C  CB  . CYS   A  1 375 ? -8.698  5.659   20.516 1.00 20.24  ? 254  CYS   A CB  1 
ATOM   2553 S  SG  . CYS   A  1 375 ? -9.263  4.206   21.435 1.00 22.57  ? 254  CYS   A SG  1 
ATOM   2554 N  N   . PHE   A  1 376 ? -8.889  8.398   18.900 1.00 16.80  ? 255  PHE   A N   1 
ATOM   2555 C  CA  . PHE   A  1 376 ? -8.294  9.631   18.390 1.00 23.06  ? 255  PHE   A CA  1 
ATOM   2556 C  C   . PHE   A  1 376 ? -9.042  10.850  18.913 1.00 26.37  ? 255  PHE   A C   1 
ATOM   2557 O  O   . PHE   A  1 376 ? -8.422  11.838  19.327 1.00 23.65  ? 255  PHE   A O   1 
ATOM   2558 C  CB  . PHE   A  1 376 ? -8.266  9.616   16.862 1.00 24.32  ? 255  PHE   A CB  1 
ATOM   2559 C  CG  . PHE   A  1 376 ? -7.071  8.904   16.296 1.00 19.29  ? 255  PHE   A CG  1 
ATOM   2560 C  CD1 . PHE   A  1 376 ? -5.871  9.572   16.119 1.00 21.41  ? 255  PHE   A CD1 1 
ATOM   2561 C  CD2 . PHE   A  1 376 ? -7.141  7.558   15.970 1.00 22.84  ? 255  PHE   A CD2 1 
ATOM   2562 C  CE1 . PHE   A  1 376 ? -4.766  8.914   15.610 1.00 23.36  ? 255  PHE   A CE1 1 
ATOM   2563 C  CE2 . PHE   A  1 376 ? -6.042  6.895   15.461 1.00 26.13  ? 255  PHE   A CE2 1 
ATOM   2564 C  CZ  . PHE   A  1 376 ? -4.852  7.576   15.282 1.00 24.51  ? 255  PHE   A CZ  1 
ATOM   2565 N  N   . THR   A  1 377 ? -10.378 10.799  18.904 1.00 22.45  ? 256  THR   A N   1 
ATOM   2566 C  CA  . THR   A  1 377 ? -11.161 11.930  19.390 1.00 21.73  ? 256  THR   A CA  1 
ATOM   2567 C  C   . THR   A  1 377 ? -10.836 12.210  20.850 1.00 24.29  ? 256  THR   A C   1 
ATOM   2568 O  O   . THR   A  1 377 ? -10.682 13.369  21.253 1.00 27.22  ? 256  THR   A O   1 
ATOM   2569 C  CB  . THR   A  1 377 ? -12.656 11.640  19.230 1.00 21.19  ? 256  THR   A CB  1 
ATOM   2570 O  OG1 . THR   A  1 377 ? -12.971 11.458  17.843 1.00 24.45  ? 256  THR   A OG1 1 
ATOM   2571 C  CG2 . THR   A  1 377 ? -13.493 12.783  19.797 1.00 20.99  ? 256  THR   A CG2 1 
ATOM   2572 N  N   . PHE   A  1 378 ? -10.695 11.147  21.644 1.00 20.03  ? 257  PHE   A N   1 
ATOM   2573 C  CA  . PHE   A  1 378 ? -10.522 11.257  23.088 1.00 26.22  ? 257  PHE   A CA  1 
ATOM   2574 C  C   . PHE   A  1 378 ? -9.083  11.603  23.457 1.00 28.83  ? 257  PHE   A C   1 
ATOM   2575 O  O   . PHE   A  1 378 ? -8.839  12.531  24.236 1.00 26.09  ? 257  PHE   A O   1 
ATOM   2576 C  CB  . PHE   A  1 378 ? -10.949 9.949   23.757 1.00 21.74  ? 257  PHE   A CB  1 
ATOM   2577 C  CG  . PHE   A  1 378 ? -10.840 9.967   25.253 1.00 24.36  ? 257  PHE   A CG  1 
ATOM   2578 C  CD1 . PHE   A  1 378 ? -11.607 10.841  26.007 1.00 25.98  ? 257  PHE   A CD1 1 
ATOM   2579 C  CD2 . PHE   A  1 378 ? -9.974  9.103   25.905 1.00 26.47  ? 257  PHE   A CD2 1 
ATOM   2580 C  CE1 . PHE   A  1 378 ? -11.510 10.856  27.388 1.00 23.89  ? 257  PHE   A CE1 1 
ATOM   2581 C  CE2 . PHE   A  1 378 ? -9.872  9.111   27.283 1.00 26.12  ? 257  PHE   A CE2 1 
ATOM   2582 C  CZ  . PHE   A  1 378 ? -10.641 9.991   28.027 1.00 33.26  ? 257  PHE   A CZ  1 
ATOM   2583 N  N   . PHE   A  1 379 ? -8.119  10.856  22.912 1.00 21.68  ? 258  PHE   A N   1 
ATOM   2584 C  CA  . PHE   A  1 379 ? -6.723  10.975  23.321 1.00 23.22  ? 258  PHE   A CA  1 
ATOM   2585 C  C   . PHE   A  1 379 ? -5.964  12.089  22.608 1.00 27.44  ? 258  PHE   A C   1 
ATOM   2586 O  O   . PHE   A  1 379 ? -4.900  12.489  23.091 1.00 30.02  ? 258  PHE   A O   1 
ATOM   2587 C  CB  . PHE   A  1 379 ? -5.989  9.646   23.105 1.00 20.77  ? 258  PHE   A CB  1 
ATOM   2588 C  CG  . PHE   A  1 379 ? -6.364  8.571   24.091 1.00 24.70  ? 258  PHE   A CG  1 
ATOM   2589 C  CD1 . PHE   A  1 379 ? -6.293  8.810   25.455 1.00 28.57  ? 258  PHE   A CD1 1 
ATOM   2590 C  CD2 . PHE   A  1 379 ? -6.770  7.319   23.658 1.00 22.33  ? 258  PHE   A CD2 1 
ATOM   2591 C  CE1 . PHE   A  1 379 ? -6.626  7.825   26.367 1.00 30.45  ? 258  PHE   A CE1 1 
ATOM   2592 C  CE2 . PHE   A  1 379 ? -7.105  6.331   24.566 1.00 26.04  ? 258  PHE   A CE2 1 
ATOM   2593 C  CZ  . PHE   A  1 379 ? -7.033  6.586   25.922 1.00 25.54  ? 258  PHE   A CZ  1 
ATOM   2594 N  N   . CYS   A  1 380 ? -6.462  12.593  21.478 1.00 26.70  ? 259  CYS   A N   1 
ATOM   2595 C  CA  . CYS   A  1 380 ? -5.768  13.619  20.699 1.00 30.16  ? 259  CYS   A CA  1 
ATOM   2596 C  C   . CYS   A  1 380 ? -6.659  14.842  20.511 1.00 34.50  ? 259  CYS   A C   1 
ATOM   2597 O  O   . CYS   A  1 380 ? -7.164  15.094  19.409 1.00 31.08  ? 259  CYS   A O   1 
ATOM   2598 C  CB  . CYS   A  1 380 ? -5.297  13.106  19.340 1.00 38.29  ? 259  CYS   A CB  1 
ATOM   2599 S  SG  . CYS   A  1 380 ? -4.103  14.255  18.588 1.00 40.05  ? 259  CYS   A SG  1 
ATOM   2600 N  N   . PRO   A  1 381 ? -6.870  15.631  21.567 1.00 34.81  ? 260  PRO   A N   1 
ATOM   2601 C  CA  . PRO   A  1 381 ? -7.663  16.859  21.407 1.00 40.51  ? 260  PRO   A CA  1 
ATOM   2602 C  C   . PRO   A  1 381 ? -6.979  17.916  20.557 1.00 44.58  ? 260  PRO   A C   1 
ATOM   2603 O  O   . PRO   A  1 381 ? -7.639  18.882  20.154 1.00 48.49  ? 260  PRO   A O   1 
ATOM   2604 C  CB  . PRO   A  1 381 ? -7.853  17.340  22.848 1.00 47.79  ? 260  PRO   A CB  1 
ATOM   2605 C  CG  . PRO   A  1 381 ? -6.654  16.819  23.573 1.00 36.13  ? 260  PRO   A CG  1 
ATOM   2606 C  CD  . PRO   A  1 381 ? -6.344  15.486  22.937 1.00 33.14  ? 260  PRO   A CD  1 
ATOM   2607 N  N   . ASP   A  1 382 ? -5.685  17.771  20.283 1.00 38.40  ? 261  ASP   A N   1 
ATOM   2608 C  CA  . ASP   A  1 382 ? -4.999  18.620  19.322 1.00 41.84  ? 261  ASP   A CA  1 
ATOM   2609 C  C   . ASP   A  1 382 ? -5.204  18.167  17.881 1.00 40.64  ? 261  ASP   A C   1 
ATOM   2610 O  O   . ASP   A  1 382 ? -4.830  18.894  16.952 1.00 37.97  ? 261  ASP   A O   1 
ATOM   2611 C  CB  . ASP   A  1 382 ? -3.510  18.653  19.656 1.00 46.06  ? 261  ASP   A CB  1 
ATOM   2612 C  CG  . ASP   A  1 382 ? -3.234  19.307  20.995 1.00 59.84  ? 261  ASP   A CG  1 
ATOM   2613 O  OD1 . ASP   A  1 382 ? -4.058  20.145  21.420 1.00 68.22  ? 261  ASP   A OD1 1 
ATOM   2614 O  OD2 . ASP   A  1 382 ? -2.171  19.023  21.592 1.00 74.30  ? 261  ASP   A OD2 1 
ATOM   2615 N  N   . CYS   A  1 383 ? -5.751  16.971  17.679 1.00 32.61  ? 262  CYS   A N   1 
ATOM   2616 C  CA  . CYS   A  1 383 ? -6.059  16.462  16.353 1.00 33.45  ? 262  CYS   A CA  1 
ATOM   2617 C  C   . CYS   A  1 383 ? -7.438  16.944  15.936 1.00 37.10  ? 262  CYS   A C   1 
ATOM   2618 O  O   . CYS   A  1 383 ? -8.362  17.005  16.754 1.00 36.46  ? 262  CYS   A O   1 
ATOM   2619 C  CB  . CYS   A  1 383 ? -6.020  14.931  16.316 1.00 38.27  ? 262  CYS   A CB  1 
ATOM   2620 S  SG  . CYS   A  1 383 ? -4.410  14.160  16.585 1.00 43.96  ? 262  CYS   A SG  1 
ATOM   2621 N  N   . SER   A  1 384 ? -7.572  17.296  14.662 1.00 29.04  ? 263  SER   A N   1 
ATOM   2622 C  CA  . SER   A  1 384 ? -8.891  17.594  14.125 1.00 36.46  ? 263  SER   A CA  1 
ATOM   2623 C  C   . SER   A  1 384 ? -9.765  16.349  14.201 1.00 27.27  ? 263  SER   A C   1 
ATOM   2624 O  O   . SER   A  1 384 ? -9.291  15.226  14.008 1.00 31.62  ? 263  SER   A O   1 
ATOM   2625 C  CB  . SER   A  1 384 ? -8.785  18.083  12.680 1.00 41.90  ? 263  SER   A CB  1 
ATOM   2626 O  OG  . SER   A  1 384 ? -8.184  19.364  12.618 1.00 54.12  ? 263  SER   A OG  1 
ATOM   2627 N  N   . HIS   A  1 385 ? -11.043 16.552  14.510 1.00 26.95  ? 264  HIS   A N   1 
ATOM   2628 C  CA  . HIS   A  1 385 ? -11.980 15.438  14.566 1.00 28.52  ? 264  HIS   A CA  1 
ATOM   2629 C  C   . HIS   A  1 385 ? -12.037 14.730  13.218 1.00 28.69  ? 264  HIS   A C   1 
ATOM   2630 O  O   . HIS   A  1 385 ? -11.982 15.368  12.163 1.00 27.92  ? 264  HIS   A O   1 
ATOM   2631 C  CB  . HIS   A  1 385 ? -13.367 15.947  14.964 1.00 26.36  ? 264  HIS   A CB  1 
ATOM   2632 C  CG  . HIS   A  1 385 ? -14.287 14.882  15.478 1.00 25.29  ? 264  HIS   A CG  1 
ATOM   2633 N  ND1 . HIS   A  1 385 ? -14.792 13.882  14.674 1.00 28.72  ? 264  HIS   A ND1 1 
ATOM   2634 C  CD2 . HIS   A  1 385 ? -14.797 14.664  16.713 1.00 27.15  ? 264  HIS   A CD2 1 
ATOM   2635 C  CE1 . HIS   A  1 385 ? -15.575 13.096  15.392 1.00 28.80  ? 264  HIS   A CE1 1 
ATOM   2636 N  NE2 . HIS   A  1 385 ? -15.594 13.548  16.633 1.00 28.69  ? 264  HIS   A NE2 1 
ATOM   2637 N  N   . ALA   A  1 386 ? -12.116 13.401  13.261 1.00 25.51  ? 265  ALA   A N   1 
ATOM   2638 C  CA  . ALA   A  1 386 ? -12.376 12.622  12.059 1.00 23.18  ? 265  ALA   A CA  1 
ATOM   2639 C  C   . ALA   A  1 386 ? -13.545 13.234  11.289 1.00 26.40  ? 265  ALA   A C   1 
ATOM   2640 O  O   . ALA   A  1 386 ? -14.552 13.617  11.900 1.00 25.34  ? 265  ALA   A O   1 
ATOM   2641 C  CB  . ALA   A  1 386 ? -12.679 11.165  12.419 1.00 24.98  ? 265  ALA   A CB  1 
ATOM   2642 N  N   . PRO   A  1 387 ? -13.451 13.348  9.966  1.00 27.79  ? 266  PRO   A N   1 
ATOM   2643 C  CA  . PRO   A  1 387 ? -14.516 14.007  9.201  1.00 33.58  ? 266  PRO   A CA  1 
ATOM   2644 C  C   . PRO   A  1 387 ? -15.810 13.209  9.230  1.00 30.83  ? 266  PRO   A C   1 
ATOM   2645 O  O   . PRO   A  1 387 ? -15.832 12.007  9.502  1.00 24.52  ? 266  PRO   A O   1 
ATOM   2646 C  CB  . PRO   A  1 387 ? -13.946 14.088  7.780  1.00 34.51  ? 266  PRO   A CB  1 
ATOM   2647 C  CG  . PRO   A  1 387 ? -12.901 13.030  7.719  1.00 36.60  ? 266  PRO   A CG  1 
ATOM   2648 C  CD  . PRO   A  1 387 ? -12.345 12.887  9.108  1.00 31.05  ? 266  PRO   A CD  1 
ATOM   2649 N  N   . LEU   A  1 388 ? -16.906 13.912  8.936  1.00 28.97  ? 267  LEU   A N   1 
ATOM   2650 C  CA  . LEU   A  1 388 ? -18.230 13.310  9.055  1.00 30.10  ? 267  LEU   A CA  1 
ATOM   2651 C  C   . LEU   A  1 388 ? -18.375 12.091  8.152  1.00 26.30  ? 267  LEU   A C   1 
ATOM   2652 O  O   . LEU   A  1 388 ? -18.957 11.079  8.561  1.00 26.84  ? 267  LEU   A O   1 
ATOM   2653 C  CB  . LEU   A  1 388 ? -19.311 14.345  8.742  1.00 35.55  ? 267  LEU   A CB  1 
ATOM   2654 C  CG  . LEU   A  1 388 ? -20.761 13.881  8.905  1.00 38.14  ? 267  LEU   A CG  1 
ATOM   2655 C  CD1 . LEU   A  1 388 ? -20.964 13.206  10.250 1.00 37.71  ? 267  LEU   A CD1 1 
ATOM   2656 C  CD2 . LEU   A  1 388 ? -21.719 15.051  8.746  1.00 43.67  ? 267  LEU   A CD2 1 
ATOM   2657 N  N   . TRP   A  1 389 ? -17.845 12.158  6.924  1.00 27.79  ? 268  TRP   A N   1 
ATOM   2658 C  CA  . TRP   A  1 389 ? -17.972 11.020  6.015  1.00 33.45  ? 268  TRP   A CA  1 
ATOM   2659 C  C   . TRP   A  1 389 ? -17.287 9.783   6.578  1.00 27.23  ? 268  TRP   A C   1 
ATOM   2660 O  O   . TRP   A  1 389 ? -17.754 8.659   6.356  1.00 24.65  ? 268  TRP   A O   1 
ATOM   2661 C  CB  . TRP   A  1 389 ? -17.411 11.352  4.629  1.00 28.33  ? 268  TRP   A CB  1 
ATOM   2662 C  CG  . TRP   A  1 389 ? -15.925 11.574  4.560  1.00 30.76  ? 268  TRP   A CG  1 
ATOM   2663 C  CD1 . TRP   A  1 389 ? -15.268 12.768  4.617  1.00 34.16  ? 268  TRP   A CD1 1 
ATOM   2664 C  CD2 . TRP   A  1 389 ? -14.914 10.569  4.396  1.00 32.59  ? 268  TRP   A CD2 1 
ATOM   2665 N  NE1 . TRP   A  1 389 ? -13.912 12.569  4.506  1.00 26.93  ? 268  TRP   A NE1 1 
ATOM   2666 C  CE2 . TRP   A  1 389 ? -13.669 11.228  4.372  1.00 30.83  ? 268  TRP   A CE2 1 
ATOM   2667 C  CE3 . TRP   A  1 389 ? -14.942 9.175   4.276  1.00 27.57  ? 268  TRP   A CE3 1 
ATOM   2668 C  CZ2 . TRP   A  1 389 ? -12.463 10.542  4.231  1.00 33.02  ? 268  TRP   A CZ2 1 
ATOM   2669 C  CZ3 . TRP   A  1 389 ? -13.744 8.496   4.137  1.00 34.71  ? 268  TRP   A CZ3 1 
ATOM   2670 C  CH2 . TRP   A  1 389 ? -12.522 9.180   4.115  1.00 37.97  ? 268  TRP   A CH2 1 
ATOM   2671 N  N   . LEU   A  1 390 ? -16.190 9.969   7.312  1.00 25.09  ? 269  LEU   A N   1 
ATOM   2672 C  CA  . LEU   A  1 390 ? -15.481 8.833   7.885  1.00 25.65  ? 269  LEU   A CA  1 
ATOM   2673 C  C   . LEU   A  1 390 ? -16.228 8.294   9.095  1.00 21.13  ? 269  LEU   A C   1 
ATOM   2674 O  O   . LEU   A  1 390 ? -16.245 7.079   9.324  1.00 26.52  ? 269  LEU   A O   1 
ATOM   2675 C  CB  . LEU   A  1 390 ? -14.057 9.238   8.271  1.00 25.41  ? 269  LEU   A CB  1 
ATOM   2676 C  CG  . LEU   A  1 390 ? -13.169 8.142   8.857  1.00 26.80  ? 269  LEU   A CG  1 
ATOM   2677 C  CD1 . LEU   A  1 390 ? -12.999 7.008   7.860  1.00 29.28  ? 269  LEU   A CD1 1 
ATOM   2678 C  CD2 . LEU   A  1 390 ? -11.817 8.716   9.258  1.00 22.34  ? 269  LEU   A CD2 1 
ATOM   2679 N  N   . MET   A  1 391 ? -16.823 9.189   9.888  1.00 21.82  ? 270  MET   A N   1 
ATOM   2680 C  CA  . MET   A  1 391 ? -17.696 8.761   10.973 1.00 22.28  ? 270  MET   A CA  1 
ATOM   2681 C  C   . MET   A  1 391 ? -18.786 7.852   10.427 1.00 24.12  ? 270  MET   A C   1 
ATOM   2682 O  O   . MET   A  1 391 ? -19.065 6.787   10.990 1.00 24.54  ? 270  MET   A O   1 
ATOM   2683 C  CB  . MET   A  1 391 ? -18.300 9.962   11.704 1.00 20.36  ? 270  MET   A CB  1 
ATOM   2684 C  CG  . MET   A  1 391 ? -17.263 10.884  12.324 1.00 26.92  ? 270  MET   A CG  1 
ATOM   2685 S  SD  . MET   A  1 391 ? -16.151 10.033  13.462 1.00 25.97  ? 270  MET   A SD  1 
ATOM   2686 C  CE  . MET   A  1 391 ? -17.301 9.367   14.663 1.00 21.68  ? 270  MET   A CE  1 
ATOM   2687 N  N   . TYR   A  1 392 ? -19.411 8.253   9.313  1.00 24.83  ? 271  TYR   A N   1 
ATOM   2688 C  CA  . TYR   A  1 392 ? -20.548 7.487   8.824  1.00 25.24  ? 271  TYR   A CA  1 
ATOM   2689 C  C   . TYR   A  1 392 ? -20.083 6.199   8.167  1.00 23.27  ? 271  TYR   A C   1 
ATOM   2690 O  O   . TYR   A  1 392 ? -20.780 5.182   8.241  1.00 24.97  ? 271  TYR   A O   1 
ATOM   2691 C  CB  . TYR   A  1 392 ? -21.314 8.280   7.759  1.00 27.99  ? 271  TYR   A CB  1 
ATOM   2692 C  CG  . TYR   A  1 392 ? -22.214 9.402   8.216  1.00 31.14  ? 271  TYR   A CG  1 
ATOM   2693 C  CD1 . TYR   A  1 392 ? -22.718 9.457   9.506  1.00 34.48  ? 271  TYR   A CD1 1 
ATOM   2694 C  CD2 . TYR   A  1 392 ? -22.567 10.413  7.329  1.00 40.02  ? 271  TYR   A CD2 1 
ATOM   2695 C  CE1 . TYR   A  1 392 ? -23.547 10.496  9.899  1.00 35.53  ? 271  TYR   A CE1 1 
ATOM   2696 C  CE2 . TYR   A  1 392 ? -23.389 11.448  7.709  1.00 37.63  ? 271  TYR   A CE2 1 
ATOM   2697 C  CZ  . TYR   A  1 392 ? -23.878 11.487  8.994  1.00 41.22  ? 271  TYR   A CZ  1 
ATOM   2698 O  OH  . TYR   A  1 392 ? -24.698 12.527  9.372  1.00 45.03  ? 271  TYR   A OH  1 
ATOM   2699 N  N   . LEU   A  1 393 ? -18.894 6.214   7.554  1.00 19.13  ? 272  LEU   A N   1 
ATOM   2700 C  CA  . LEU   A  1 393 ? -18.299 4.977   7.060  1.00 24.56  ? 272  LEU   A CA  1 
ATOM   2701 C  C   . LEU   A  1 393 ? -18.013 4.002   8.193  1.00 19.82  ? 272  LEU   A C   1 
ATOM   2702 O  O   . LEU   A  1 393 ? -18.247 2.796   8.059  1.00 24.71  ? 272  LEU   A O   1 
ATOM   2703 C  CB  . LEU   A  1 393 ? -17.021 5.289   6.283  1.00 22.69  ? 272  LEU   A CB  1 
ATOM   2704 C  CG  . LEU   A  1 393 ? -16.312 4.086   5.662  1.00 38.03  ? 272  LEU   A CG  1 
ATOM   2705 C  CD1 . LEU   A  1 393 ? -17.211 3.406   4.640  1.00 34.14  ? 272  LEU   A CD1 1 
ATOM   2706 C  CD2 . LEU   A  1 393 ? -15.001 4.520   5.023  1.00 33.03  ? 272  LEU   A CD2 1 
ATOM   2707 N  N   . ALA   A  1 394 ? -17.492 4.504   9.316  1.00 20.94  ? 273  ALA   A N   1 
ATOM   2708 C  CA  . ALA   A  1 394 ? -17.185 3.625   10.439 1.00 21.30  ? 273  ALA   A CA  1 
ATOM   2709 C  C   . ALA   A  1 394 ? -18.449 3.096   11.100 1.00 17.80  ? 273  ALA   A C   1 
ATOM   2710 O  O   . ALA   A  1 394 ? -18.477 1.948   11.558 1.00 18.46  ? 273  ALA   A O   1 
ATOM   2711 C  CB  . ALA   A  1 394 ? -16.321 4.358   11.465 1.00 15.80  ? 273  ALA   A CB  1 
ATOM   2712 N  N   . ILE   A  1 395 ? -19.505 3.910   11.135 1.00 20.45  ? 274  ILE   A N   1 
ATOM   2713 C  CA  . ILE   A  1 395 ? -20.779 3.466   11.692 1.00 22.33  ? 274  ILE   A CA  1 
ATOM   2714 C  C   . ILE   A  1 395 ? -21.400 2.386   10.817 1.00 22.48  ? 274  ILE   A C   1 
ATOM   2715 O  O   . ILE   A  1 395 ? -21.834 1.339   11.311 1.00 22.86  ? 274  ILE   A O   1 
ATOM   2716 C  CB  . ILE   A  1 395 ? -21.725 4.666   11.873 1.00 23.23  ? 274  ILE   A CB  1 
ATOM   2717 C  CG1 . ILE   A  1 395 ? -21.213 5.577   12.990 1.00 19.60  ? 274  ILE   A CG1 1 
ATOM   2718 C  CG2 . ILE   A  1 395 ? -23.149 4.197   12.162 1.00 20.60  ? 274  ILE   A CG2 1 
ATOM   2719 C  CD1 . ILE   A  1 395 ? -21.805 6.972   12.952 1.00 19.95  ? 274  ILE   A CD1 1 
ATOM   2720 N  N   . VAL   A  1 396 ? -21.450 2.620   9.504  1.00 21.61  ? 275  VAL   A N   1 
ATOM   2721 C  CA  A VAL   A  1 396 ? -22.065 1.625   8.631  0.66 22.19  ? 275  VAL   A CA  1 
ATOM   2722 C  CA  B VAL   A  1 396 ? -22.041 1.643   8.595  0.34 22.24  ? 275  VAL   A CA  1 
ATOM   2723 C  C   . VAL   A  1 396 ? -21.241 0.345   8.613  1.00 20.39  ? 275  VAL   A C   1 
ATOM   2724 O  O   . VAL   A  1 396 ? -21.804 -0.754  8.549  1.00 23.53  ? 275  VAL   A O   1 
ATOM   2725 C  CB  A VAL   A  1 396 ? -22.290 2.180   7.208  0.66 27.16  ? 275  VAL   A CB  1 
ATOM   2726 C  CB  B VAL   A  1 396 ? -22.143 2.250   7.183  0.34 26.90  ? 275  VAL   A CB  1 
ATOM   2727 C  CG1 A VAL   A  1 396 ? -23.214 3.395   7.247  0.66 23.86  ? 275  VAL   A CG1 1 
ATOM   2728 C  CG1 B VAL   A  1 396 ? -21.799 1.230   6.117  0.34 23.58  ? 275  VAL   A CG1 1 
ATOM   2729 C  CG2 A VAL   A  1 396 ? -20.977 2.514   6.524  0.66 26.91  ? 275  VAL   A CG2 1 
ATOM   2730 C  CG2 B VAL   A  1 396 ? -23.530 2.834   6.965  0.34 27.81  ? 275  VAL   A CG2 1 
ATOM   2731 N  N   . LEU   A  1 397 ? -19.912 0.450   8.712  1.00 18.74  ? 276  LEU   A N   1 
ATOM   2732 C  CA  . LEU   A  1 397 ? -19.082 -0.750  8.767  1.00 19.69  ? 276  LEU   A CA  1 
ATOM   2733 C  C   . LEU   A  1 397 ? -19.407 -1.593  9.994  1.00 23.16  ? 276  LEU   A C   1 
ATOM   2734 O  O   . LEU   A  1 397 ? -19.522 -2.821  9.900  1.00 22.72  ? 276  LEU   A O   1 
ATOM   2735 C  CB  . LEU   A  1 397 ? -17.603 -0.370  8.760  1.00 19.32  ? 276  LEU   A CB  1 
ATOM   2736 C  CG  . LEU   A  1 397 ? -16.615 -1.532  8.871  1.00 31.15  ? 276  LEU   A CG  1 
ATOM   2737 C  CD1 . LEU   A  1 397 ? -16.767 -2.501  7.702  1.00 29.17  ? 276  LEU   A CD1 1 
ATOM   2738 C  CD2 . LEU   A  1 397 ? -15.191 -1.006  8.950  1.00 32.90  ? 276  LEU   A CD2 1 
ATOM   2739 N  N   . SER   A  1 398 ? -19.553 -0.953  11.157 1.00 18.32  ? 277  SER   A N   1 
ATOM   2740 C  CA  . SER   A  1 398 ? -19.940 -1.694  12.351 1.00 21.42  ? 277  SER   A CA  1 
ATOM   2741 C  C   . SER   A  1 398 ? -21.297 -2.361  12.171 1.00 22.71  ? 277  SER   A C   1 
ATOM   2742 O  O   . SER   A  1 398 ? -21.521 -3.464  12.682 1.00 24.50  ? 277  SER   A O   1 
ATOM   2743 C  CB  . SER   A  1 398 ? -19.947 -0.766  13.569 1.00 20.66  ? 277  SER   A CB  1 
ATOM   2744 O  OG  . SER   A  1 398 ? -21.078 0.087   13.574 1.00 19.83  ? 277  SER   A OG  1 
ATOM   2745 N  N   . HIS   A  1 399 ? -22.200 -1.725  11.420 1.00 20.51  ? 278  HIS   A N   1 
ATOM   2746 C  CA  . HIS   A  1 399 ? -23.515 -2.311  11.188 1.00 22.13  ? 278  HIS   A CA  1 
ATOM   2747 C  C   . HIS   A  1 399 ? -23.455 -3.466  10.194 1.00 20.90  ? 278  HIS   A C   1 
ATOM   2748 O  O   . HIS   A  1 399 ? -24.250 -4.408  10.300 1.00 21.17  ? 278  HIS   A O   1 
ATOM   2749 C  CB  . HIS   A  1 399 ? -24.484 -1.234  10.702 1.00 20.24  ? 278  HIS   A CB  1 
ATOM   2750 C  CG  . HIS   A  1 399 ? -24.803 -0.203  11.739 1.00 25.03  ? 278  HIS   A CG  1 
ATOM   2751 N  ND1 . HIS   A  1 399 ? -25.348 1.024   11.428 1.00 23.81  ? 278  HIS   A ND1 1 
ATOM   2752 C  CD2 . HIS   A  1 399 ? -24.644 -0.215  13.083 1.00 28.19  ? 278  HIS   A CD2 1 
ATOM   2753 C  CE1 . HIS   A  1 399 ? -25.517 1.721   12.538 1.00 28.41  ? 278  HIS   A CE1 1 
ATOM   2754 N  NE2 . HIS   A  1 399 ? -25.097 0.992   13.556 1.00 22.76  ? 278  HIS   A NE2 1 
ATOM   2755 N  N   . THR   A  1 400 ? -22.528 -3.421  9.230  1.00 23.28  ? 279  THR   A N   1 
ATOM   2756 C  CA  . THR   A  1 400 ? -22.407 -4.515  8.271  1.00 27.08  ? 279  THR   A CA  1 
ATOM   2757 C  C   . THR   A  1 400 ? -22.036 -5.828  8.941  1.00 23.64  ? 279  THR   A C   1 
ATOM   2758 O  O   . THR   A  1 400 ? -22.275 -6.893  8.362  1.00 25.48  ? 279  THR   A O   1 
ATOM   2759 C  CB  . THR   A  1 400 ? -21.362 -4.204  7.192  1.00 30.33  ? 279  THR   A CB  1 
ATOM   2760 O  OG1 . THR   A  1 400 ? -20.067 -4.081  7.794  1.00 40.49  ? 279  THR   A OG1 1 
ATOM   2761 C  CG2 . THR   A  1 400 ? -21.705 -2.924  6.447  1.00 19.93  ? 279  THR   A CG2 1 
ATOM   2762 N  N   . ASN   A  1 401 ? -21.445 -5.780  10.138 1.00 24.10  ? 280  ASN   A N   1 
ATOM   2763 C  CA  . ASN   A  1 401 ? -21.142 -7.017  10.847 1.00 25.15  ? 280  ASN   A CA  1 
ATOM   2764 C  C   . ASN   A  1 401 ? -22.400 -7.827  11.115 1.00 24.21  ? 280  ASN   A C   1 
ATOM   2765 O  O   . ASN   A  1 401 ? -22.337 -9.058  11.204 1.00 23.37  ? 280  ASN   A O   1 
ATOM   2766 C  CB  . ASN   A  1 401 ? -20.425 -6.730  12.162 1.00 24.30  ? 280  ASN   A CB  1 
ATOM   2767 C  CG  . ASN   A  1 401 ? -20.015 -8.000  12.877 1.00 33.01  ? 280  ASN   A CG  1 
ATOM   2768 O  OD1 . ASN   A  1 401 ? -19.166 -8.751  12.395 1.00 37.02  ? 280  ASN   A OD1 1 
ATOM   2769 N  ND2 . ASN   A  1 401 ? -20.640 -8.266  14.014 1.00 20.86  ? 280  ASN   A ND2 1 
ATOM   2770 N  N   . SER   A  1 402 ? -23.548 -7.164  11.250 1.00 21.29  ? 281  SER   A N   1 
ATOM   2771 C  CA  . SER   A  1 402 ? -24.782 -7.900  11.480 1.00 27.13  ? 281  SER   A CA  1 
ATOM   2772 C  C   . SER   A  1 402 ? -25.281 -8.606  10.228 1.00 27.03  ? 281  SER   A C   1 
ATOM   2773 O  O   . SER   A  1 402 ? -26.281 -9.328  10.303 1.00 26.08  ? 281  SER   A O   1 
ATOM   2774 C  CB  . SER   A  1 402 ? -25.861 -6.951  12.008 1.00 21.38  ? 281  SER   A CB  1 
ATOM   2775 O  OG  . SER   A  1 402 ? -25.527 -6.472  13.300 1.00 27.64  ? 281  SER   A OG  1 
ATOM   2776 N  N   . VAL   A  1 403 ? -24.613 -8.416  9.090  1.00 28.96  ? 282  VAL   A N   1 
ATOM   2777 C  CA  . VAL   A  1 403 ? -24.977 -9.075  7.841  1.00 23.82  ? 282  VAL   A CA  1 
ATOM   2778 C  C   . VAL   A  1 403 ? -24.144 -10.336 7.624  1.00 35.45  ? 282  VAL   A C   1 
ATOM   2779 O  O   . VAL   A  1 403 ? -24.611 -11.299 7.005  1.00 33.12  ? 282  VAL   A O   1 
ATOM   2780 C  CB  . VAL   A  1 403 ? -24.824 -8.101  6.654  1.00 25.21  ? 282  VAL   A CB  1 
ATOM   2781 C  CG1 . VAL   A  1 403 ? -25.138 -8.792  5.336  1.00 26.61  ? 282  VAL   A CG1 1 
ATOM   2782 C  CG2 . VAL   A  1 403 ? -25.719 -6.886  6.844  1.00 25.51  ? 282  VAL   A CG2 1 
ATOM   2783 N  N   . VAL   A  1 404 ? -22.922 -10.362 8.164  1.00 25.84  ? 283  VAL   A N   1 
ATOM   2784 C  CA  . VAL   A  1 404 ? -21.909 -11.259 7.608  1.00 27.25  ? 283  VAL   A CA  1 
ATOM   2785 C  C   . VAL   A  1 404 ? -22.017 -12.684 8.152  1.00 37.70  ? 283  VAL   A C   1 
ATOM   2786 O  O   . VAL   A  1 404 ? -21.691 -13.638 7.436  1.00 35.15  ? 283  VAL   A O   1 
ATOM   2787 C  CB  . VAL   A  1 404 ? -20.494 -10.692 7.834  1.00 33.32  ? 283  VAL   A CB  1 
ATOM   2788 C  CG1 . VAL   A  1 404 ? -20.348 -9.336  7.166  1.00 39.70  ? 283  VAL   A CG1 1 
ATOM   2789 C  CG2 . VAL   A  1 404 ? -20.170 -10.600 9.320  1.00 38.96  ? 283  VAL   A CG2 1 
ATOM   2790 N  N   . ASN   A  1 405 ? -22.443 -12.865 9.405  1.00 33.76  ? 284  ASN   A N   1 
ATOM   2791 C  CA  . ASN   A  1 405 ? -22.453 -14.209 9.986  1.00 39.08  ? 284  ASN   A CA  1 
ATOM   2792 C  C   . ASN   A  1 405 ? -23.260 -15.222 9.175  1.00 40.06  ? 284  ASN   A C   1 
ATOM   2793 O  O   . ASN   A  1 405 ? -22.754 -16.336 8.954  1.00 36.04  ? 284  ASN   A O   1 
ATOM   2794 C  CB  . ASN   A  1 405 ? -22.954 -14.142 11.434 1.00 35.73  ? 284  ASN   A CB  1 
ATOM   2795 C  CG  . ASN   A  1 405 ? -22.045 -13.318 12.332 1.00 51.07  ? 284  ASN   A CG  1 
ATOM   2796 O  OD1 . ASN   A  1 405 ? -20.946 -12.928 11.935 1.00 38.26  ? 284  ASN   A OD1 1 
ATOM   2797 N  ND2 . ASN   A  1 405 ? -22.508 -13.039 13.546 1.00 48.10  ? 284  ASN   A ND2 1 
ATOM   2798 N  N   . PRO   A  1 406 ? -24.490 -14.932 8.717  1.00 25.77  ? 285  PRO   A N   1 
ATOM   2799 C  CA  . PRO   A  1 406 ? -25.208 -15.920 7.888  1.00 33.70  ? 285  PRO   A CA  1 
ATOM   2800 C  C   . PRO   A  1 406 ? -24.428 -16.420 6.681  1.00 40.25  ? 285  PRO   A C   1 
ATOM   2801 O  O   . PRO   A  1 406 ? -24.569 -17.591 6.307  1.00 45.27  ? 285  PRO   A O   1 
ATOM   2802 C  CB  . PRO   A  1 406 ? -26.474 -15.164 7.467  1.00 30.43  ? 285  PRO   A CB  1 
ATOM   2803 C  CG  . PRO   A  1 406 ? -26.706 -14.207 8.580  1.00 31.01  ? 285  PRO   A CG  1 
ATOM   2804 C  CD  . PRO   A  1 406 ? -25.335 -13.754 8.995  1.00 36.05  ? 285  PRO   A CD  1 
ATOM   2805 N  N   . PHE   A  1 407 ? -23.601 -15.572 6.064  1.00 37.94  ? 286  PHE   A N   1 
ATOM   2806 C  CA  . PHE   A  1 407 ? -22.794 -16.027 4.936  1.00 43.92  ? 286  PHE   A CA  1 
ATOM   2807 C  C   . PHE   A  1 407 ? -21.690 -16.971 5.385  1.00 44.43  ? 286  PHE   A C   1 
ATOM   2808 O  O   . PHE   A  1 407 ? -21.393 -17.956 4.700  1.00 45.16  ? 286  PHE   A O   1 
ATOM   2809 C  CB  . PHE   A  1 407 ? -22.207 -14.834 4.183  1.00 45.45  ? 286  PHE   A CB  1 
ATOM   2810 C  CG  . PHE   A  1 407 ? -23.210 -14.103 3.351  1.00 49.81  ? 286  PHE   A CG  1 
ATOM   2811 C  CD1 . PHE   A  1 407 ? -23.448 -14.489 2.042  1.00 55.65  ? 286  PHE   A CD1 1 
ATOM   2812 C  CD2 . PHE   A  1 407 ? -23.930 -13.045 3.877  1.00 46.96  ? 286  PHE   A CD2 1 
ATOM   2813 C  CE1 . PHE   A  1 407 ? -24.374 -13.827 1.270  1.00 54.28  ? 286  PHE   A CE1 1 
ATOM   2814 C  CE2 . PHE   A  1 407 ? -24.860 -12.380 3.109  1.00 47.87  ? 286  PHE   A CE2 1 
ATOM   2815 C  CZ  . PHE   A  1 407 ? -25.084 -12.773 1.803  1.00 56.04  ? 286  PHE   A CZ  1 
ATOM   2816 N  N   . ILE   A  1 408 ? -21.069 -16.688 6.531  1.00 37.00  ? 287  ILE   A N   1 
ATOM   2817 C  CA  . ILE   A  1 408 ? -20.026 -17.577 7.028  1.00 41.93  ? 287  ILE   A CA  1 
ATOM   2818 C  C   . ILE   A  1 408 ? -20.600 -18.955 7.333  1.00 41.51  ? 287  ILE   A C   1 
ATOM   2819 O  O   . ILE   A  1 408 ? -19.990 -19.978 7.002  1.00 42.47  ? 287  ILE   A O   1 
ATOM   2820 C  CB  . ILE   A  1 408 ? -19.332 -16.959 8.253  1.00 44.92  ? 287  ILE   A CB  1 
ATOM   2821 C  CG1 . ILE   A  1 408 ? -18.836 -15.550 7.925  1.00 34.22  ? 287  ILE   A CG1 1 
ATOM   2822 C  CG2 . ILE   A  1 408 ? -18.176 -17.835 8.707  1.00 44.53  ? 287  ILE   A CG2 1 
ATOM   2823 C  CD1 . ILE   A  1 408 ? -17.811 -15.512 6.809  1.00 40.87  ? 287  ILE   A CD1 1 
ATOM   2824 N  N   . TYR   A  1 409 ? -21.781 -19.011 7.958  1.00 40.61  ? 288  TYR   A N   1 
ATOM   2825 C  CA  . TYR   A  1 409 ? -22.388 -20.312 8.229  1.00 49.62  ? 288  TYR   A CA  1 
ATOM   2826 C  C   . TYR   A  1 409 ? -22.739 -21.032 6.936  1.00 43.99  ? 288  TYR   A C   1 
ATOM   2827 O  O   . TYR   A  1 409 ? -22.518 -22.242 6.809  1.00 50.49  ? 288  TYR   A O   1 
ATOM   2828 C  CB  . TYR   A  1 409 ? -23.651 -20.150 9.073  1.00 39.99  ? 288  TYR   A CB  1 
ATOM   2829 C  CG  . TYR   A  1 409 ? -23.454 -19.429 10.376 1.00 38.38  ? 288  TYR   A CG  1 
ATOM   2830 C  CD1 . TYR   A  1 409 ? -22.384 -19.726 11.207 1.00 48.81  ? 288  TYR   A CD1 1 
ATOM   2831 C  CD2 . TYR   A  1 409 ? -24.348 -18.448 10.779 1.00 36.66  ? 288  TYR   A CD2 1 
ATOM   2832 C  CE1 . TYR   A  1 409 ? -22.216 -19.069 12.412 1.00 47.38  ? 288  TYR   A CE1 1 
ATOM   2833 C  CE2 . TYR   A  1 409 ? -24.184 -17.780 11.970 1.00 35.11  ? 288  TYR   A CE2 1 
ATOM   2834 C  CZ  . TYR   A  1 409 ? -23.120 -18.095 12.786 1.00 44.88  ? 288  TYR   A CZ  1 
ATOM   2835 O  OH  . TYR   A  1 409 ? -22.953 -17.418 13.971 1.00 38.80  ? 288  TYR   A OH  1 
ATOM   2836 N  N   . ALA   A  1 410 ? -23.279 -20.297 5.961  1.00 38.44  ? 289  ALA   A N   1 
ATOM   2837 C  CA  . ALA   A  1 410 ? -23.683 -20.910 4.701  1.00 43.31  ? 289  ALA   A CA  1 
ATOM   2838 C  C   . ALA   A  1 410 ? -22.481 -21.445 3.939  1.00 51.84  ? 289  ALA   A C   1 
ATOM   2839 O  O   . ALA   A  1 410 ? -22.530 -22.546 3.380  1.00 50.50  ? 289  ALA   A O   1 
ATOM   2840 C  CB  . ALA   A  1 410 ? -24.458 -19.903 3.854  1.00 35.95  ? 289  ALA   A CB  1 
ATOM   2841 N  N   . TYR   A  1 411 ? -21.390 -20.685 3.911  1.00 49.34  ? 290  TYR   A N   1 
ATOM   2842 C  CA  . TYR   A  1 411 ? -20.226 -21.089 3.140  1.00 51.92  ? 290  TYR   A CA  1 
ATOM   2843 C  C   . TYR   A  1 411 ? -19.387 -22.128 3.872  1.00 61.45  ? 290  TYR   A C   1 
ATOM   2844 O  O   . TYR   A  1 411 ? -18.631 -22.862 3.226  1.00 56.18  ? 290  TYR   A O   1 
ATOM   2845 C  CB  . TYR   A  1 411 ? -19.354 -19.864 2.835  1.00 57.21  ? 290  TYR   A CB  1 
ATOM   2846 C  CG  . TYR   A  1 411 ? -19.787 -19.027 1.642  1.00 72.87  ? 290  TYR   A CG  1 
ATOM   2847 C  CD1 . TYR   A  1 411 ? -19.603 -19.470 0.337  1.00 82.46  ? 290  TYR   A CD1 1 
ATOM   2848 C  CD2 . TYR   A  1 411 ? -20.359 -17.773 1.831  1.00 79.59  ? 290  TYR   A CD2 1 
ATOM   2849 C  CE1 . TYR   A  1 411 ? -19.995 -18.689 -0.746 1.00 81.32  ? 290  TYR   A CE1 1 
ATOM   2850 C  CE2 . TYR   A  1 411 ? -20.752 -16.992 0.762  1.00 83.81  ? 290  TYR   A CE2 1 
ATOM   2851 C  CZ  . TYR   A  1 411 ? -20.568 -17.451 -0.523 1.00 90.25  ? 290  TYR   A CZ  1 
ATOM   2852 O  OH  . TYR   A  1 411 ? -20.962 -16.668 -1.585 1.00 102.56 ? 290  TYR   A OH  1 
ATOM   2853 N  N   . ARG   A  1 412 ? -19.509 -22.212 5.202  1.00 46.81  ? 291  ARG   A N   1 
ATOM   2854 C  CA  . ARG   A  1 412 ? -18.604 -23.014 6.013  1.00 50.58  ? 291  ARG   A CA  1 
ATOM   2855 C  C   . ARG   A  1 412 ? -19.244 -24.185 6.757  1.00 47.46  ? 291  ARG   A C   1 
ATOM   2856 O  O   . ARG   A  1 412 ? -18.504 -25.057 7.226  1.00 48.86  ? 291  ARG   A O   1 
ATOM   2857 C  CB  . ARG   A  1 412 ? -17.889 -22.106 7.026  1.00 44.22  ? 291  ARG   A CB  1 
ATOM   2858 C  CG  . ARG   A  1 412 ? -16.911 -21.153 6.347  1.00 47.53  ? 291  ARG   A CG  1 
ATOM   2859 C  CD  . ARG   A  1 412 ? -15.827 -20.642 7.268  1.00 38.30  ? 291  ARG   A CD  1 
ATOM   2860 N  NE  . ARG   A  1 412 ? -15.159 -21.716 7.988  1.00 51.97  ? 291  ARG   A NE  1 
ATOM   2861 C  CZ  . ARG   A  1 412 ? -13.974 -22.204 7.655  1.00 53.04  ? 291  ARG   A CZ  1 
ATOM   2862 N  NH1 . ARG   A  1 412 ? -13.303 -21.738 6.614  1.00 48.16  ? 291  ARG   A NH1 1 
ATOM   2863 N  NH2 . ARG   A  1 412 ? -13.444 -23.178 8.389  1.00 52.89  ? 291  ARG   A NH2 1 
ATOM   2864 N  N   . ILE   A  1 413 ? -20.571 -24.241 6.887  1.00 47.53  ? 292  ILE   A N   1 
ATOM   2865 C  CA  . ILE   A  1 413 ? -21.244 -25.273 7.683  1.00 48.10  ? 292  ILE   A CA  1 
ATOM   2866 C  C   . ILE   A  1 413 ? -22.297 -25.944 6.812  1.00 45.56  ? 292  ILE   A C   1 
ATOM   2867 O  O   . ILE   A  1 413 ? -23.355 -25.358 6.544  1.00 41.07  ? 292  ILE   A O   1 
ATOM   2868 C  CB  . ILE   A  1 413 ? -21.883 -24.713 8.963  1.00 50.55  ? 292  ILE   A CB  1 
ATOM   2869 C  CG1 . ILE   A  1 413 ? -20.901 -23.817 9.719  1.00 51.24  ? 292  ILE   A CG1 1 
ATOM   2870 C  CG2 . ILE   A  1 413 ? -22.365 -25.852 9.857  1.00 46.64  ? 292  ILE   A CG2 1 
ATOM   2871 C  CD1 . ILE   A  1 413 ? -21.445 -23.295 11.032 1.00 47.12  ? 292  ILE   A CD1 1 
ATOM   2872 N  N   . ARG   A  1 414 ? -22.000 -27.168 6.361  1.00 49.09  ? 293  ARG   A N   1 
ATOM   2873 C  CA  . ARG   A  1 414 ? -22.893 -27.886 5.456  1.00 49.89  ? 293  ARG   A CA  1 
ATOM   2874 C  C   . ARG   A  1 414 ? -24.316 -27.986 5.998  1.00 38.17  ? 293  ARG   A C   1 
ATOM   2875 O  O   . ARG   A  1 414 ? -25.282 -27.793 5.252  1.00 45.73  ? 293  ARG   A O   1 
ATOM   2876 C  CB  . ARG   A  1 414 ? -22.314 -29.272 5.162  1.00 61.81  ? 293  ARG   A CB  1 
ATOM   2877 C  CG  . ARG   A  1 414 ? -22.961 -29.978 3.984  1.00 60.14  ? 293  ARG   A CG  1 
ATOM   2878 C  CD  . ARG   A  1 414 ? -22.085 -31.118 3.485  1.00 60.58  ? 293  ARG   A CD  1 
ATOM   2879 N  N   . GLU   A  1 415 ? -24.471 -28.285 7.293  1.00 45.75  ? 294  GLU   A N   1 
ATOM   2880 C  CA  . GLU   A  1 415 ? -25.816 -28.466 7.837  1.00 52.97  ? 294  GLU   A CA  1 
ATOM   2881 C  C   . GLU   A  1 415 ? -26.623 -27.178 7.752  1.00 44.77  ? 294  GLU   A C   1 
ATOM   2882 O  O   . GLU   A  1 415 ? -27.836 -27.212 7.516  1.00 43.34  ? 294  GLU   A O   1 
ATOM   2883 C  CB  . GLU   A  1 415 ? -25.756 -28.974 9.276  1.00 47.55  ? 294  GLU   A CB  1 
ATOM   2884 C  CG  . GLU   A  1 415 ? -27.073 -29.579 9.753  1.00 59.68  ? 294  GLU   A CG  1 
ATOM   2885 C  CD  . GLU   A  1 415 ? -27.408 -30.883 9.060  1.00 62.09  ? 294  GLU   A CD  1 
ATOM   2886 O  OE1 . GLU   A  1 415 ? -26.480 -31.671 8.784  1.00 71.62  ? 294  GLU   A OE1 1 
ATOM   2887 O  OE2 . GLU   A  1 415 ? -28.605 -31.116 8.784  1.00 61.24  ? 294  GLU   A OE2 1 
ATOM   2888 N  N   . PHE   A  1 416 ? -25.968 -26.031 7.944  1.00 48.16  ? 295  PHE   A N   1 
ATOM   2889 C  CA  . PHE   A  1 416 ? -26.649 -24.759 7.735  1.00 42.59  ? 295  PHE   A CA  1 
ATOM   2890 C  C   . PHE   A  1 416 ? -26.936 -24.560 6.254  1.00 37.04  ? 295  PHE   A C   1 
ATOM   2891 O  O   . PHE   A  1 416 ? -28.068 -24.250 5.864  1.00 43.94  ? 295  PHE   A O   1 
ATOM   2892 C  CB  . PHE   A  1 416 ? -25.803 -23.614 8.292  1.00 39.39  ? 295  PHE   A CB  1 
ATOM   2893 C  CG  . PHE   A  1 416 ? -26.140 -23.250 9.709  1.00 40.18  ? 295  PHE   A CG  1 
ATOM   2894 C  CD1 . PHE   A  1 416 ? -27.364 -22.682 10.021 1.00 33.55  ? 295  PHE   A CD1 1 
ATOM   2895 C  CD2 . PHE   A  1 416 ? -25.241 -23.499 10.734 1.00 39.42  ? 295  PHE   A CD2 1 
ATOM   2896 C  CE1 . PHE   A  1 416 ? -27.679 -22.353 11.326 1.00 35.84  ? 295  PHE   A CE1 1 
ATOM   2897 C  CE2 . PHE   A  1 416 ? -25.551 -23.175 12.042 1.00 39.27  ? 295  PHE   A CE2 1 
ATOM   2898 C  CZ  . PHE   A  1 416 ? -26.771 -22.600 12.338 1.00 38.64  ? 295  PHE   A CZ  1 
ATOM   2899 N  N   . ARG   A  1 417 ? -25.903 -24.714 5.419  1.00 40.71  ? 296  ARG   A N   1 
ATOM   2900 C  CA  . ARG   A  1 417 ? -26.047 -24.497 3.983  1.00 47.17  ? 296  ARG   A CA  1 
ATOM   2901 C  C   . ARG   A  1 417 ? -27.162 -25.360 3.410  1.00 46.13  ? 296  ARG   A C   1 
ATOM   2902 O  O   . ARG   A  1 417 ? -27.961 -24.895 2.588  1.00 46.99  ? 296  ARG   A O   1 
ATOM   2903 C  CB  . ARG   A  1 417 ? -24.720 -24.786 3.283  1.00 44.69  ? 296  ARG   A CB  1 
ATOM   2904 C  CG  . ARG   A  1 417 ? -24.737 -24.615 1.775  1.00 53.69  ? 296  ARG   A CG  1 
ATOM   2905 C  CD  . ARG   A  1 417 ? -23.326 -24.649 1.203  1.00 57.10  ? 296  ARG   A CD  1 
ATOM   2906 N  NE  . ARG   A  1 417 ? -22.657 -25.925 1.426  1.00 54.37  ? 296  ARG   A NE  1 
ATOM   2907 C  CZ  . ARG   A  1 417 ? -21.690 -26.113 2.315  1.00 53.35  ? 296  ARG   A CZ  1 
ATOM   2908 N  NH1 . ARG   A  1 417 ? -21.244 -25.122 3.070  1.00 53.97  ? 296  ARG   A NH1 1 
ATOM   2909 N  NH2 . ARG   A  1 417 ? -21.149 -27.321 2.442  1.00 51.50  ? 296  ARG   A NH2 1 
ATOM   2910 N  N   . GLN   A  1 418 ? -27.240 -26.619 3.847  1.00 43.97  ? 297  GLN   A N   1 
ATOM   2911 C  CA  . GLN   A  1 418 ? -28.274 -27.513 3.341  1.00 47.32  ? 297  GLN   A CA  1 
ATOM   2912 C  C   . GLN   A  1 418 ? -29.643 -27.101 3.860  1.00 45.64  ? 297  GLN   A C   1 
ATOM   2913 O  O   . GLN   A  1 418 ? -30.631 -27.148 3.123  1.00 42.13  ? 297  GLN   A O   1 
ATOM   2914 C  CB  . GLN   A  1 418 ? -27.957 -28.956 3.737  1.00 42.48  ? 297  GLN   A CB  1 
ATOM   2915 C  CG  . GLN   A  1 418 ? -26.752 -29.540 3.018  1.00 54.81  ? 297  GLN   A CG  1 
ATOM   2916 C  CD  . GLN   A  1 418 ? -26.397 -30.932 3.504  1.00 74.32  ? 297  GLN   A CD  1 
ATOM   2917 O  OE1 . GLN   A  1 418 ? -26.777 -31.335 4.604  1.00 67.32  ? 297  GLN   A OE1 1 
ATOM   2918 N  NE2 . GLN   A  1 418 ? -25.654 -31.672 2.689  1.00 58.51  ? 297  GLN   A NE2 1 
ATOM   2919 N  N   . THR   A  1 419 ? -29.711 -26.655 5.115  1.00 41.22  ? 298  THR   A N   1 
ATOM   2920 C  CA  . THR   A  1 419 ? -30.982 -26.208 5.675  1.00 44.96  ? 298  THR   A CA  1 
ATOM   2921 C  C   . THR   A  1 419 ? -31.432 -24.902 5.033  1.00 44.59  ? 298  THR   A C   1 
ATOM   2922 O  O   . THR   A  1 419 ? -32.623 -24.716 4.760  1.00 39.22  ? 298  THR   A O   1 
ATOM   2923 C  CB  . THR   A  1 419 ? -30.862 -26.048 7.191  1.00 42.34  ? 298  THR   A CB  1 
ATOM   2924 O  OG1 . THR   A  1 419 ? -30.297 -27.238 7.754  1.00 45.60  ? 298  THR   A OG1 1 
ATOM   2925 C  CG2 . THR   A  1 419 ? -32.230 -25.806 7.810  1.00 35.28  ? 298  THR   A CG2 1 
ATOM   2926 N  N   . PHE   A  1 420 ? -30.494 -23.978 4.806  1.00 40.59  ? 299  PHE   A N   1 
ATOM   2927 C  CA  . PHE   A  1 420 ? -30.806 -22.762 4.060  1.00 44.76  ? 299  PHE   A CA  1 
ATOM   2928 C  C   . PHE   A  1 420 ? -31.427 -23.079 2.703  1.00 45.17  ? 299  PHE   A C   1 
ATOM   2929 O  O   . PHE   A  1 420 ? -32.445 -22.489 2.323  1.00 42.75  ? 299  PHE   A O   1 
ATOM   2930 C  CB  . PHE   A  1 420 ? -29.544 -21.913 3.884  1.00 42.43  ? 299  PHE   A CB  1 
ATOM   2931 C  CG  . PHE   A  1 420 ? -29.030 -21.307 5.162  1.00 36.90  ? 299  PHE   A CG  1 
ATOM   2932 C  CD1 . PHE   A  1 420 ? -29.804 -21.311 6.311  1.00 31.40  ? 299  PHE   A CD1 1 
ATOM   2933 C  CD2 . PHE   A  1 420 ? -27.778 -20.714 5.205  1.00 37.37  ? 299  PHE   A CD2 1 
ATOM   2934 C  CE1 . PHE   A  1 420 ? -29.334 -20.747 7.482  1.00 42.86  ? 299  PHE   A CE1 1 
ATOM   2935 C  CE2 . PHE   A  1 420 ? -27.303 -20.147 6.373  1.00 40.60  ? 299  PHE   A CE2 1 
ATOM   2936 C  CZ  . PHE   A  1 420 ? -28.083 -20.164 7.513  1.00 35.67  ? 299  PHE   A CZ  1 
ATOM   2937 N  N   . ARG   A  1 421 ? -30.827 -24.009 1.955  1.00 45.29  ? 300  ARG   A N   1 
ATOM   2938 C  CA  . ARG   A  1 421 ? -31.341 -24.321 0.624  1.00 56.52  ? 300  ARG   A CA  1 
ATOM   2939 C  C   . ARG   A  1 421 ? -32.759 -24.877 0.699  1.00 54.97  ? 300  ARG   A C   1 
ATOM   2940 O  O   . ARG   A  1 421 ? -33.623 -24.512 -0.107 1.00 55.97  ? 300  ARG   A O   1 
ATOM   2941 C  CB  . ARG   A  1 421 ? -30.412 -25.303 -0.092 1.00 60.10  ? 300  ARG   A CB  1 
ATOM   2942 C  CG  . ARG   A  1 421 ? -29.132 -24.664 -0.607 1.00 64.94  ? 300  ARG   A CG  1 
ATOM   2943 C  CD  . ARG   A  1 421 ? -28.419 -25.544 -1.626 1.00 73.50  ? 300  ARG   A CD  1 
ATOM   2944 N  NE  . ARG   A  1 421 ? -27.608 -26.581 -0.998 1.00 79.31  ? 300  ARG   A NE  1 
ATOM   2945 C  CZ  . ARG   A  1 421 ? -26.282 -26.581 -0.974 1.00 80.52  ? 300  ARG   A CZ  1 
ATOM   2946 N  NH1 . ARG   A  1 421 ? -25.579 -25.619 -1.551 1.00 69.05  ? 300  ARG   A NH1 1 
ATOM   2947 N  NH2 . ARG   A  1 421 ? -25.644 -27.571 -0.356 1.00 73.36  ? 300  ARG   A NH2 1 
ATOM   2948 N  N   . LYS   A  1 422 ? -33.021 -25.748 1.681  1.00 58.58  ? 301  LYS   A N   1 
ATOM   2949 C  CA  . LYS   A  1 422 ? -34.345 -26.350 1.806  1.00 55.19  ? 301  LYS   A CA  1 
ATOM   2950 C  C   . LYS   A  1 422 ? -35.379 -25.285 2.144  1.00 52.76  ? 301  LYS   A C   1 
ATOM   2951 O  O   . LYS   A  1 422 ? -36.497 -25.297 1.618  1.00 56.73  ? 301  LYS   A O   1 
ATOM   2952 C  CB  . LYS   A  1 422 ? -34.356 -27.398 2.923  1.00 55.86  ? 301  LYS   A CB  1 
ATOM   2953 C  CG  . LYS   A  1 422 ? -33.307 -28.511 2.890  1.00 73.28  ? 301  LYS   A CG  1 
ATOM   2954 C  CD  . LYS   A  1 422 ? -32.725 -28.863 1.533  1.00 75.02  ? 301  LYS   A CD  1 
ATOM   2955 C  CE  . LYS   A  1 422 ? -31.784 -30.055 1.674  1.00 77.50  ? 301  LYS   A CE  1 
ATOM   2956 N  NZ  . LYS   A  1 422 ? -32.503 -31.323 1.917  1.00 77.52  ? 301  LYS   A NZ  1 
ATOM   2957 N  N   . ILE   A  1 423 ? -35.011 -24.342 3.017  1.00 51.28  ? 302  ILE   A N   1 
ATOM   2958 C  CA  . ILE   A  1 423 ? -35.924 -23.264 3.387  1.00 54.71  ? 302  ILE   A CA  1 
ATOM   2959 C  C   . ILE   A  1 423 ? -36.223 -22.385 2.181  1.00 56.45  ? 302  ILE   A C   1 
ATOM   2960 O  O   . ILE   A  1 423 ? -37.379 -22.032 1.918  1.00 60.48  ? 302  ILE   A O   1 
ATOM   2961 C  CB  . ILE   A  1 423 ? -35.342 -22.439 4.551  1.00 48.68  ? 302  ILE   A CB  1 
ATOM   2962 C  CG1 . ILE   A  1 423 ? -35.288 -23.258 5.846  1.00 53.58  ? 302  ILE   A CG1 1 
ATOM   2963 C  CG2 . ILE   A  1 423 ? -36.160 -21.180 4.767  1.00 46.01  ? 302  ILE   A CG2 1 
ATOM   2964 C  CD1 . ILE   A  1 423 ? -34.355 -22.669 6.900  1.00 44.79  ? 302  ILE   A CD1 1 
ATOM   2965 N  N   . ILE   A  1 424 ? -35.184 -22.008 1.434  1.00 50.46  ? 303  ILE   A N   1 
ATOM   2966 C  CA  . ILE   A  1 424 ? -35.393 -21.116 0.299  1.00 67.86  ? 303  ILE   A CA  1 
ATOM   2967 C  C   . ILE   A  1 424 ? -36.195 -21.812 -0.796 1.00 65.69  ? 303  ILE   A C   1 
ATOM   2968 O  O   . ILE   A  1 424 ? -37.190 -21.271 -1.291 1.00 61.00  ? 303  ILE   A O   1 
ATOM   2969 C  CB  . ILE   A  1 424 ? -34.041 -20.600 -0.227 1.00 61.68  ? 303  ILE   A CB  1 
ATOM   2970 C  CG1 . ILE   A  1 424 ? -33.374 -19.710 0.823  1.00 57.17  ? 303  ILE   A CG1 1 
ATOM   2971 C  CG2 . ILE   A  1 424 ? -34.233 -19.829 -1.526 1.00 54.56  ? 303  ILE   A CG2 1 
ATOM   2972 C  CD1 . ILE   A  1 424 ? -31.864 -19.734 0.776  1.00 42.15  ? 303  ILE   A CD1 1 
ATOM   2973 N  N   . ARG   A  1 425 ? -35.775 -23.020 -1.193 1.00 67.33  ? 304  ARG   A N   1 
ATOM   2974 C  CA  . ARG   A  1 425 ? -36.490 -23.743 -2.245 1.00 68.89  ? 304  ARG   A CA  1 
ATOM   2975 C  C   . ARG   A  1 425 ? -37.945 -23.993 -1.869 1.00 72.46  ? 304  ARG   A C   1 
ATOM   2976 O  O   . ARG   A  1 425 ? -38.865 -23.651 -2.620 1.00 86.97  ? 304  ARG   A O   1 
ATOM   2977 C  CB  . ARG   A  1 425 ? -35.804 -25.075 -2.552 1.00 59.45  ? 304  ARG   A CB  1 
ATOM   2978 C  CG  . ARG   A  1 425 ? -34.510 -24.986 -3.338 1.00 68.99  ? 304  ARG   A CG  1 
ATOM   2979 C  CD  . ARG   A  1 425 ? -33.852 -26.357 -3.387 1.00 69.88  ? 304  ARG   A CD  1 
ATOM   2980 N  NE  . ARG   A  1 425 ? -32.520 -26.332 -3.978 1.00 83.59  ? 304  ARG   A NE  1 
ATOM   2981 C  CZ  . ARG   A  1 425 ? -31.674 -27.352 -3.947 1.00 94.59  ? 304  ARG   A CZ  1 
ATOM   2982 N  NH1 . ARG   A  1 425 ? -32.025 -28.526 -3.446 1.00 89.05  ? 304  ARG   A NH1 1 
ATOM   2983 N  NH2 . ARG   A  1 425 ? -30.449 -27.195 -4.439 1.00 85.16  ? 304  ARG   A NH2 1 
ATOM   2984 N  N   . SER   A  1 426 ? -38.169 -24.590 -0.702 1.00 68.38  ? 305  SER   A N   1 
ATOM   2985 C  CA  . SER   A  1 426 ? -39.516 -24.854 -0.208 1.00 73.51  ? 305  SER   A CA  1 
ATOM   2986 C  C   . SER   A  1 426 ? -40.228 -23.578 0.221  1.00 74.54  ? 305  SER   A C   1 
ATOM   2987 O  O   . SER   A  1 426 ? -41.450 -23.562 0.367  1.00 94.23  ? 305  SER   A O   1 
ATOM   2988 C  CB  . SER   A  1 426 ? -39.468 -25.852 0.952  1.00 76.77  ? 305  SER   A CB  1 
ATOM   2989 O  OG  . SER   A  1 426 ? -38.764 -27.026 0.578  1.00 80.70  ? 305  SER   A OG  1 
HETATM 2990 N  N1  . A1H3H B  2 .   ? -22.641 5.573   16.962 1.00 27.01  ? 1201 A1H3H A N1  1 
HETATM 2991 N  N3  . A1H3H B  2 .   ? -21.860 7.814   16.306 1.00 21.16  ? 1201 A1H3H A N3  1 
HETATM 2992 C  C4  . A1H3H B  2 .   ? -25.007 6.000   16.399 1.00 30.45  ? 1201 A1H3H A C4  1 
HETATM 2993 C  C5  . A1H3H B  2 .   ? -21.746 6.627   16.973 1.00 23.06  ? 1201 A1H3H A C5  1 
HETATM 2994 C  C6  . A1H3H B  2 .   ? -20.604 6.550   17.716 1.00 22.01  ? 1201 A1H3H A C6  1 
HETATM 2995 C  C8  . A1H3H B  2 .   ? -20.752 8.473   16.651 1.00 25.50  ? 1201 A1H3H A C8  1 
HETATM 2996 C  C13 . A1H3H B  2 .   ? -21.699 13.872  13.766 1.00 46.82  ? 1201 A1H3H A C13 1 
HETATM 2997 C  C15 . A1H3H B  2 .   ? -19.144 16.440  13.681 1.00 66.57  ? 1201 A1H3H A C15 1 
HETATM 2998 C  C9  . A1H3H B  2 .   ? -20.405 9.814   16.209 1.00 23.91  ? 1201 A1H3H A C9  1 
HETATM 2999 C  C17 . A1H3H B  2 .   ? -19.749 12.567  15.245 1.00 34.15  ? 1201 A1H3H A C17 1 
HETATM 3000 C  C1  . A1H3H B  2 .   ? -21.054 3.260   19.366 1.00 21.56  ? 1201 A1H3H A C1  1 
HETATM 3001 C  C2  . A1H3H B  2 .   ? -22.346 4.396   17.625 1.00 26.47  ? 1201 A1H3H A C2  1 
HETATM 3002 C  C3  . A1H3H B  2 .   ? -23.664 5.523   15.903 1.00 29.93  ? 1201 A1H3H A C3  1 
HETATM 3003 C  C14 . A1H3H B  2 .   ? -20.512 14.532  14.108 1.00 51.68  ? 1201 A1H3H A C14 1 
HETATM 3004 C  C16 . A1H3H B  2 .   ? -19.537 13.876  14.846 1.00 39.32  ? 1201 A1H3H A C16 1 
HETATM 3005 C  C19 . A1H3H B  2 .   ? -20.288 5.440   18.572 1.00 25.77  ? 1201 A1H3H A C19 1 
HETATM 3006 O  O1  . A1H3H B  2 .   ? -20.428 15.822  13.665 1.00 61.73  ? 1201 A1H3H A O1  1 
HETATM 3007 N  N   . A1H3H B  2 .   ? -21.256 4.426   18.485 1.00 22.92  ? 1201 A1H3H A N   1 
HETATM 3008 C  C   . A1H3H B  2 .   ? -20.105 2.238   18.797 1.00 30.63  ? 1201 A1H3H A C   1 
HETATM 3009 O  O   . A1H3H B  2 .   ? -23.006 3.386   17.460 1.00 32.58  ? 1201 A1H3H A O   1 
HETATM 3010 C  C10 . A1H3H B  2 .   ? -21.179 10.531  15.402 1.00 28.55  ? 1201 A1H3H A C10 1 
HETATM 3011 C  C11 . A1H3H B  2 .   ? -20.923 11.892  14.917 1.00 36.15  ? 1201 A1H3H A C11 1 
HETATM 3012 C  C12 . A1H3H B  2 .   ? -21.892 12.560  14.164 1.00 38.08  ? 1201 A1H3H A C12 1 
HETATM 3013 C  C7  . A1H3H B  2 .   ? -18.673 8.175   18.068 1.00 20.89  ? 1201 A1H3H A C7  1 
HETATM 3014 N  N2  . A1H3H B  2 .   ? -19.952 7.751   17.495 1.00 25.37  ? 1201 A1H3H A N2  1 
HETATM 3015 O  O2  . A1H3H B  2 .   ? -22.670 14.514  13.067 1.00 49.23  ? 1201 A1H3H A O2  1 
HETATM 3016 O  O3  . A1H3H B  2 .   ? -19.303 5.313   19.289 1.00 26.40  ? 1201 A1H3H A O3  1 
HETATM 3017 C  C1  . CLR   C  3 .   ? -3.185  8.124   21.065 1.00 24.45  ? 1202 CLR   A C1  1 
HETATM 3018 C  C2  . CLR   C  3 .   ? -3.044  9.644   20.992 1.00 26.20  ? 1202 CLR   A C2  1 
HETATM 3019 C  C3  . CLR   C  3 .   ? -2.015  10.032  19.953 1.00 25.05  ? 1202 CLR   A C3  1 
HETATM 3020 C  C4  . CLR   C  3 .   ? -2.413  9.488   18.592 1.00 28.78  ? 1202 CLR   A C4  1 
HETATM 3021 C  C5  . CLR   C  3 .   ? -2.691  8.003   18.628 1.00 23.90  ? 1202 CLR   A C5  1 
HETATM 3022 C  C6  . CLR   C  3 .   ? -2.147  7.192   17.730 1.00 23.97  ? 1202 CLR   A C6  1 
HETATM 3023 C  C7  . CLR   C  3 .   ? -2.360  5.713   17.667 1.00 29.91  ? 1202 CLR   A C7  1 
HETATM 3024 C  C8  . CLR   C  3 .   ? -3.576  5.267   18.471 1.00 26.03  ? 1202 CLR   A C8  1 
HETATM 3025 C  C9  . CLR   C  3 .   ? -3.575  5.964   19.840 1.00 22.82  ? 1202 CLR   A C9  1 
HETATM 3026 C  C10 . CLR   C  3 .   ? -3.632  7.516   19.726 1.00 28.55  ? 1202 CLR   A C10 1 
HETATM 3027 C  C11 . CLR   C  3 .   ? -4.649  5.402   20.781 1.00 24.04  ? 1202 CLR   A C11 1 
HETATM 3028 C  C12 . CLR   C  3 .   ? -4.635  3.878   20.881 1.00 27.67  ? 1202 CLR   A C12 1 
HETATM 3029 C  C13 . CLR   C  3 .   ? -4.752  3.214   19.503 1.00 34.15  ? 1202 CLR   A C13 1 
HETATM 3030 C  C14 . CLR   C  3 .   ? -3.571  3.746   18.667 1.00 24.70  ? 1202 CLR   A C14 1 
HETATM 3031 C  C15 . CLR   C  3 .   ? -3.556  2.827   17.437 1.00 26.16  ? 1202 CLR   A C15 1 
HETATM 3032 C  C16 . CLR   C  3 .   ? -4.017  1.459   17.976 1.00 29.50  ? 1202 CLR   A C16 1 
HETATM 3033 C  C17 . CLR   C  3 .   ? -4.472  1.693   19.433 1.00 25.61  ? 1202 CLR   A C17 1 
HETATM 3034 C  C18 . CLR   C  3 .   ? -6.102  3.564   18.853 1.00 22.03  ? 1202 CLR   A C18 1 
HETATM 3035 C  C19 . CLR   C  3 .   ? -5.055  8.009   19.394 1.00 23.45  ? 1202 CLR   A C19 1 
HETATM 3036 C  C20 . CLR   C  3 .   ? -5.570  0.698   19.858 1.00 35.16  ? 1202 CLR   A C20 1 
HETATM 3037 C  C21 . CLR   C  3 .   ? -5.928  0.779   21.340 1.00 27.56  ? 1202 CLR   A C21 1 
HETATM 3038 C  C22 . CLR   C  3 .   ? -5.174  -0.742  19.485 1.00 36.91  ? 1202 CLR   A C22 1 
HETATM 3039 C  C23 . CLR   C  3 .   ? -6.260  -1.780  19.742 1.00 44.53  ? 1202 CLR   A C23 1 
HETATM 3040 C  C24 . CLR   C  3 .   ? -5.750  -3.216  19.759 1.00 46.47  ? 1202 CLR   A C24 1 
HETATM 3041 C  C25 . CLR   C  3 .   ? -5.179  -3.736  18.455 1.00 61.30  ? 1202 CLR   A C25 1 
HETATM 3042 C  C26 . CLR   C  3 .   ? -6.158  -3.548  17.309 1.00 69.29  ? 1202 CLR   A C26 1 
HETATM 3043 C  C27 . CLR   C  3 .   ? -4.785  -5.198  18.582 1.00 57.14  ? 1202 CLR   A C27 1 
HETATM 3044 O  O1  . CLR   C  3 .   ? -1.899  11.455  19.889 1.00 29.01  ? 1202 CLR   A O1  1 
HETATM 3045 C  C1  . CLR   D  3 .   ? -8.306  10.768  13.179 1.00 29.67  ? 1203 CLR   A C1  1 
HETATM 3046 C  C2  . CLR   D  3 .   ? -8.384  12.293  13.173 1.00 30.76  ? 1203 CLR   A C2  1 
HETATM 3047 C  C3  . CLR   D  3 .   ? -7.018  12.893  12.919 1.00 32.73  ? 1203 CLR   A C3  1 
HETATM 3048 C  C4  . CLR   D  3 .   ? -6.471  12.405  11.590 1.00 28.78  ? 1203 CLR   A C4  1 
HETATM 3049 C  C5  . CLR   D  3 .   ? -6.496  10.898  11.472 1.00 32.17  ? 1203 CLR   A C5  1 
HETATM 3050 C  C6  . CLR   D  3 .   ? -5.428  10.238  11.047 1.00 24.27  ? 1203 CLR   A C6  1 
HETATM 3051 C  C7  . CLR   D  3 .   ? -5.345  8.754   10.881 1.00 26.62  ? 1203 CLR   A C7  1 
HETATM 3052 C  C8  . CLR   D  3 .   ? -6.718  8.091   10.864 1.00 29.69  ? 1203 CLR   A C8  1 
HETATM 3053 C  C9  . CLR   D  3 .   ? -7.588  8.675   11.987 1.00 27.57  ? 1203 CLR   A C9  1 
HETATM 3054 C  C10 . CLR   D  3 .   ? -7.808  10.210  11.838 1.00 31.90  ? 1203 CLR   A C10 1 
HETATM 3055 C  C11 . CLR   D  3 .   ? -8.900  7.901   12.168 1.00 30.32  ? 1203 CLR   A C11 1 
HETATM 3056 C  C12 . CLR   D  3 .   ? -8.701  6.391   12.295 1.00 26.20  ? 1203 CLR   A C12 1 
HETATM 3057 C  C13 . CLR   D  3 .   ? -7.927  5.814   11.101 1.00 27.96  ? 1203 CLR   A C13 1 
HETATM 3058 C  C14 . CLR   D  3 .   ? -6.584  6.574   11.052 1.00 29.38  ? 1203 CLR   A C14 1 
HETATM 3059 C  C15 . CLR   D  3 .   ? -5.745  5.764   10.057 1.00 33.72  ? 1203 CLR   A C15 1 
HETATM 3060 C  C16 . CLR   D  3 .   ? -6.182  4.307   10.297 1.00 35.27  ? 1203 CLR   A C16 1 
HETATM 3061 C  C17 . CLR   D  3 .   ? -7.407  4.361   11.236 1.00 29.73  ? 1203 CLR   A C17 1 
HETATM 3062 C  C18 . CLR   D  3 .   ? -8.730  5.999   9.804  1.00 25.60  ? 1203 CLR   A C18 1 
HETATM 3063 C  C19 . CLR   D  3 .   ? -8.840  10.532  10.739 1.00 34.43  ? 1203 CLR   A C19 1 
HETATM 3064 C  C20 . CLR   D  3 .   ? -8.362  3.176   10.995 1.00 32.58  ? 1203 CLR   A C20 1 
HETATM 3065 C  C21 . CLR   D  3 .   ? -9.536  3.127   11.970 1.00 32.94  ? 1203 CLR   A C21 1 
HETATM 3066 C  C22 . CLR   D  3 .   ? -7.573  1.857   11.046 1.00 31.56  ? 1203 CLR   A C22 1 
HETATM 3067 C  C23 . CLR   D  3 .   ? -8.413  0.584   11.035 1.00 33.53  ? 1203 CLR   A C23 1 
HETATM 3068 C  C24 . CLR   D  3 .   ? -7.565  -0.676  11.169 1.00 42.22  ? 1203 CLR   A C24 1 
HETATM 3069 C  C25 . CLR   D  3 .   ? -8.305  -2.004  11.094 1.00 49.19  ? 1203 CLR   A C25 1 
HETATM 3070 C  C26 . CLR   D  3 .   ? -9.035  -2.174  9.777  1.00 49.29  ? 1203 CLR   A C26 1 
HETATM 3071 C  C27 . CLR   D  3 .   ? -9.253  -2.196  12.261 1.00 33.66  ? 1203 CLR   A C27 1 
HETATM 3072 O  O1  . CLR   D  3 .   ? -7.102  14.320  12.910 1.00 33.10  ? 1203 CLR   A O1  1 
HETATM 3073 C  C1  . CLR   E  3 .   ? -38.231 10.702  21.711 1.00 26.52  ? 1204 CLR   A C1  1 
HETATM 3074 C  C2  . CLR   E  3 .   ? -37.874 12.170  21.940 1.00 34.41  ? 1204 CLR   A C2  1 
HETATM 3075 C  C3  . CLR   E  3 .   ? -38.115 12.550  23.384 1.00 32.45  ? 1204 CLR   A C3  1 
HETATM 3076 C  C4  . CLR   E  3 .   ? -37.279 11.674  24.297 1.00 28.15  ? 1204 CLR   A C4  1 
HETATM 3077 C  C5  . CLR   E  3 .   ? -37.532 10.203  24.058 1.00 29.47  ? 1204 CLR   A C5  1 
HETATM 3078 C  C6  . CLR   E  3 .   ? -37.791 9.393   25.073 1.00 29.75  ? 1204 CLR   A C6  1 
HETATM 3079 C  C7  . CLR   E  3 .   ? -38.056 7.925   24.959 1.00 30.93  ? 1204 CLR   A C7  1 
HETATM 3080 C  C8  . CLR   E  3 .   ? -37.681 7.346   23.597 1.00 29.27  ? 1204 CLR   A C8  1 
HETATM 3081 C  C9  . CLR   E  3 .   ? -38.101 8.315   22.482 1.00 25.05  ? 1204 CLR   A C9  1 
HETATM 3082 C  C10 . CLR   E  3 .   ? -37.453 9.725   22.611 1.00 31.07  ? 1204 CLR   A C10 1 
HETATM 3083 C  C11 . CLR   E  3 .   ? -37.909 7.697   21.090 1.00 28.08  ? 1204 CLR   A C11 1 
HETATM 3084 C  C12 . CLR   E  3 .   ? -38.580 6.332   20.946 1.00 23.31  ? 1204 CLR   A C12 1 
HETATM 3085 C  C13 . CLR   E  3 .   ? -38.115 5.337   22.020 1.00 33.61  ? 1204 CLR   A C13 1 
HETATM 3086 C  C14 . CLR   E  3 .   ? -38.391 6.004   23.383 1.00 28.40  ? 1204 CLR   A C14 1 
HETATM 3087 C  C15 . CLR   E  3 .   ? -38.183 4.867   24.388 1.00 32.51  ? 1204 CLR   A C15 1 
HETATM 3088 C  C16 . CLR   E  3 .   ? -38.757 3.639   23.660 1.00 35.33  ? 1204 CLR   A C16 1 
HETATM 3089 C  C17 . CLR   E  3 .   ? -38.952 4.043   22.180 1.00 25.55  ? 1204 CLR   A C17 1 
HETATM 3090 C  C18 . CLR   E  3 .   ? -36.622 5.012   21.843 1.00 27.09  ? 1204 CLR   A C18 1 
HETATM 3091 C  C19 . CLR   E  3 .   ? -35.971 9.711   22.186 1.00 28.42  ? 1204 CLR   A C19 1 
HETATM 3092 C  C20 . CLR   E  3 .   ? -38.716 2.853   21.230 1.00 23.94  ? 1204 CLR   A C20 1 
HETATM 3093 C  C21 . CLR   E  3 .   ? -39.030 3.165   19.768 1.00 30.43  ? 1204 CLR   A C21 1 
HETATM 3094 C  C22 . CLR   E  3 .   ? -39.538 1.644   21.707 1.00 29.61  ? 1204 CLR   A C22 1 
HETATM 3095 C  C23 . CLR   E  3 .   ? -39.421 0.389   20.850 1.00 29.63  ? 1204 CLR   A C23 1 
HETATM 3096 C  C24 . CLR   E  3 .   ? -40.132 -0.811  21.468 1.00 44.31  ? 1204 CLR   A C24 1 
HETATM 3097 C  C25 . CLR   E  3 .   ? -40.027 -2.119  20.701 1.00 61.39  ? 1204 CLR   A C25 1 
HETATM 3098 C  C26 . CLR   E  3 .   ? -40.688 -2.027  19.338 1.00 53.32  ? 1204 CLR   A C26 1 
HETATM 3099 C  C27 . CLR   E  3 .   ? -40.599 -3.282  21.491 1.00 58.16  ? 1204 CLR   A C27 1 
HETATM 3100 O  O1  . CLR   E  3 .   ? -37.795 13.927  23.600 1.00 32.53  ? 1204 CLR   A O1  1 
HETATM 3101 C  C1  . OLA   F  4 .   ? -1.803  12.481  25.697 1.00 50.70  ? 1205 OLA   A C1  1 
HETATM 3102 O  O1  . OLA   F  4 .   ? -0.842  12.250  26.462 1.00 62.24  ? 1205 OLA   A O1  1 
HETATM 3103 O  O2  . OLA   F  4 .   ? -2.157  13.665  25.508 1.00 52.03  ? 1205 OLA   A O2  1 
HETATM 3104 C  C2  . OLA   F  4 .   ? -2.522  11.347  25.005 1.00 43.95  ? 1205 OLA   A C2  1 
HETATM 3105 C  C3  . OLA   F  4 .   ? -2.465  10.088  25.862 1.00 36.61  ? 1205 OLA   A C3  1 
HETATM 3106 C  C4  . OLA   F  4 .   ? -2.290  8.862   24.977 1.00 31.48  ? 1205 OLA   A C4  1 
HETATM 3107 C  C5  . OLA   F  4 .   ? -2.321  7.573   25.787 1.00 40.07  ? 1205 OLA   A C5  1 
HETATM 3108 C  C6  . OLA   F  4 .   ? -3.435  6.659   25.293 1.00 37.56  ? 1205 OLA   A C6  1 
HETATM 3109 C  C7  . OLA   F  4 .   ? -2.852  5.444   24.588 1.00 38.14  ? 1205 OLA   A C7  1 
HETATM 3110 C  C8  . OLA   F  4 .   ? -3.350  4.137   25.191 1.00 37.74  ? 1205 OLA   A C8  1 
HETATM 3111 C  C9  . OLA   F  4 .   ? -3.087  3.041   24.187 1.00 45.26  ? 1205 OLA   A C9  1 
HETATM 3112 C  C10 . OLA   F  4 .   ? -3.759  1.738   24.283 1.00 47.17  ? 1205 OLA   A C10 1 
HETATM 3113 C  C11 . OLA   F  4 .   ? -3.712  0.948   25.567 1.00 54.60  ? 1205 OLA   A C11 1 
HETATM 3114 C  C12 . OLA   F  4 .   ? -4.189  -0.472  25.289 1.00 56.69  ? 1205 OLA   A C12 1 
HETATM 3115 C  C13 . OLA   F  4 .   ? -3.323  -1.123  24.219 1.00 60.28  ? 1205 OLA   A C13 1 
HETATM 3116 C  C14 . OLA   F  4 .   ? -4.037  -2.304  23.572 1.00 73.74  ? 1205 OLA   A C14 1 
HETATM 3117 C  C15 . OLA   F  4 .   ? -4.436  -3.339  24.616 1.00 70.12  ? 1205 OLA   A C15 1 
HETATM 3118 C  C1  . OLA   G  4 .   ? -39.397 14.823  17.499 1.00 54.42  ? 1206 OLA   A C1  1 
HETATM 3119 O  O1  . OLA   G  4 .   ? -38.660 15.058  18.481 1.00 65.58  ? 1206 OLA   A O1  1 
HETATM 3120 O  O2  . OLA   G  4 .   ? -40.368 15.579  17.279 1.00 80.03  ? 1206 OLA   A O2  1 
HETATM 3121 C  C2  . OLA   G  4 .   ? -39.126 13.647  16.591 1.00 49.27  ? 1206 OLA   A C2  1 
HETATM 3122 C  C3  . OLA   G  4 .   ? -38.892 12.391  17.423 1.00 42.94  ? 1206 OLA   A C3  1 
HETATM 3123 C  C4  . OLA   G  4 .   ? -38.209 11.306  16.595 1.00 42.94  ? 1206 OLA   A C4  1 
HETATM 3124 C  C5  . OLA   G  4 .   ? -38.377 9.939   17.250 1.00 40.05  ? 1206 OLA   A C5  1 
HETATM 3125 C  C6  . OLA   G  4 .   ? -37.633 8.852   16.484 1.00 34.02  ? 1206 OLA   A C6  1 
HETATM 3126 C  C7  . OLA   G  4 .   ? -37.205 7.729   17.421 1.00 35.07  ? 1206 OLA   A C7  1 
HETATM 3127 C  C8  . OLA   G  4 .   ? -37.707 6.373   16.940 1.00 49.72  ? 1206 OLA   A C8  1 
HETATM 3128 C  C9  . OLA   G  4 .   ? -36.747 5.825   15.913 1.00 48.33  ? 1206 OLA   A C9  1 
HETATM 3129 C  C10 . OLA   G  4 .   ? -37.174 4.766   14.989 1.00 43.52  ? 1206 OLA   A C10 1 
HETATM 3130 C  C11 . OLA   G  4 .   ? -37.944 3.572   15.495 1.00 49.04  ? 1206 OLA   A C11 1 
HETATM 3131 C  C12 . OLA   G  4 .   ? -38.555 2.846   14.302 1.00 59.53  ? 1206 OLA   A C12 1 
HETATM 3132 C  C13 . OLA   G  4 .   ? -39.509 1.751   14.757 1.00 56.14  ? 1206 OLA   A C13 1 
HETATM 3133 C  C14 . OLA   G  4 .   ? -38.831 0.808   15.742 1.00 54.30  ? 1206 OLA   A C14 1 
HETATM 3134 C  C15 . OLA   G  4 .   ? -39.865 -0.078  16.425 1.00 55.70  ? 1206 OLA   A C15 1 
HETATM 3135 C  C16 . OLA   G  4 .   ? -40.563 -0.999  15.431 1.00 71.10  ? 1206 OLA   A C16 1 
HETATM 3136 C  C17 . OLA   G  4 .   ? -40.274 -2.464  15.739 1.00 61.93  ? 1206 OLA   A C17 1 
HETATM 3137 C  C18 . OLA   G  4 .   ? -40.922 -3.380  14.709 1.00 78.81  ? 1206 OLA   A C18 1 
HETATM 3138 C  C1  . OLA   H  4 .   ? -31.983 -18.265 22.490 1.00 58.36  ? 1207 OLA   A C1  1 
HETATM 3139 O  O1  . OLA   H  4 .   ? -31.042 -18.488 21.699 1.00 68.66  ? 1207 OLA   A O1  1 
HETATM 3140 O  O2  . OLA   H  4 .   ? -32.704 -19.219 22.853 1.00 74.55  ? 1207 OLA   A O2  1 
HETATM 3141 C  C2  . OLA   H  4 .   ? -32.236 -16.867 23.003 1.00 49.82  ? 1207 OLA   A C2  1 
HETATM 3142 C  C3  . OLA   H  4 .   ? -31.943 -15.861 21.898 1.00 52.48  ? 1207 OLA   A C3  1 
HETATM 3143 C  C4  . OLA   H  4 .   ? -32.956 -14.722 21.884 1.00 47.10  ? 1207 OLA   A C4  1 
HETATM 3144 C  C5  . OLA   H  4 .   ? -32.819 -13.859 23.132 1.00 45.63  ? 1207 OLA   A C5  1 
HETATM 3145 C  C6  . OLA   H  4 .   ? -33.800 -12.694 23.104 1.00 53.46  ? 1207 OLA   A C6  1 
HETATM 3146 C  C7  . OLA   H  4 .   ? -33.074 -11.371 23.319 1.00 47.18  ? 1207 OLA   A C7  1 
HETATM 3147 C  C8  . OLA   H  4 .   ? -34.061 -10.224 23.499 1.00 50.32  ? 1207 OLA   A C8  1 
HETATM 3148 C  C9  . OLA   H  4 .   ? -33.337 -9.009  24.029 1.00 45.47  ? 1207 OLA   A C9  1 
HETATM 3149 C  C10 . OLA   H  4 .   ? -34.069 -7.748  24.214 1.00 35.18  ? 1207 OLA   A C10 1 
HETATM 3150 C  C11 . OLA   H  4 .   ? -35.095 -7.332  23.186 1.00 53.42  ? 1207 OLA   A C11 1 
HETATM 3151 C  C12 . OLA   H  4 .   ? -35.625 -5.938  23.503 1.00 49.91  ? 1207 OLA   A C12 1 
HETATM 3152 C  C13 . OLA   H  4 .   ? -36.732 -5.543  22.531 1.00 45.86  ? 1207 OLA   A C13 1 
HETATM 3153 C  C1  . OLA   I  4 .   ? -2.447  16.174  13.580 1.00 80.44  ? 1208 OLA   A C1  1 
HETATM 3154 O  O1  . OLA   I  4 .   ? -2.987  17.298  13.486 1.00 80.03  ? 1208 OLA   A O1  1 
HETATM 3155 O  O2  . OLA   I  4 .   ? -1.291  16.098  14.050 1.00 80.22  ? 1208 OLA   A O2  1 
HETATM 3156 C  C2  . OLA   I  4 .   ? -3.183  14.931  13.134 1.00 53.32  ? 1208 OLA   A C2  1 
HETATM 3157 C  C3  . OLA   I  4 .   ? -2.189  13.825  12.794 1.00 52.28  ? 1208 OLA   A C3  1 
HETATM 3158 C  C4  . OLA   I  4 .   ? -2.479  12.552  13.583 1.00 43.80  ? 1208 OLA   A C4  1 
HETATM 3159 C  C5  . OLA   I  4 .   ? -1.464  11.458  13.269 1.00 42.29  ? 1208 OLA   A C5  1 
HETATM 3160 C  C6  . OLA   I  4 .   ? -1.952  10.100  13.760 1.00 42.05  ? 1208 OLA   A C6  1 
HETATM 3161 C  C7  . OLA   I  4 .   ? -1.326  8.946   12.983 1.00 42.32  ? 1208 OLA   A C7  1 
HETATM 3162 C  C8  . OLA   I  4 .   ? -2.020  7.631   13.322 1.00 45.87  ? 1208 OLA   A C8  1 
HETATM 3163 C  C9  . OLA   I  4 .   ? -1.404  6.493   12.545 1.00 41.02  ? 1208 OLA   A C9  1 
HETATM 3164 C  C10 . OLA   I  4 .   ? -2.171  5.270   12.261 1.00 41.28  ? 1208 OLA   A C10 1 
HETATM 3165 C  C11 . OLA   I  4 .   ? -2.912  4.524   13.348 1.00 44.68  ? 1208 OLA   A C11 1 
HETATM 3166 C  C12 . OLA   I  4 .   ? -3.608  3.319   12.724 1.00 45.64  ? 1208 OLA   A C12 1 
HETATM 3167 C  C13 . OLA   I  4 .   ? -4.080  2.318   13.772 1.00 42.99  ? 1208 OLA   A C13 1 
HETATM 3168 C  C14 . OLA   I  4 .   ? -3.923  0.891   13.258 1.00 45.48  ? 1208 OLA   A C14 1 
HETATM 3169 C  C15 . OLA   I  4 .   ? -4.627  -0.112  14.163 1.00 45.39  ? 1208 OLA   A C15 1 
HETATM 3170 C  C9  . OLA   J  4 .   ? -8.111  -16.980 15.360 1.00 54.89  ? 1209 OLA   A C9  1 
HETATM 3171 C  C10 . OLA   J  4 .   ? -8.250  -15.880 16.326 1.00 52.30  ? 1209 OLA   A C10 1 
HETATM 3172 C  C11 . OLA   J  4 .   ? -9.610  -15.294 16.626 1.00 48.67  ? 1209 OLA   A C11 1 
HETATM 3173 C  C12 . OLA   J  4 .   ? -9.435  -14.078 17.529 1.00 56.88  ? 1209 OLA   A C12 1 
HETATM 3174 C  C13 . OLA   J  4 .   ? -10.767 -13.395 17.811 1.00 39.29  ? 1209 OLA   A C13 1 
HETATM 3175 C  C14 . OLA   J  4 .   ? -10.661 -11.885 17.620 1.00 48.70  ? 1209 OLA   A C14 1 
HETATM 3176 C  C15 . OLA   J  4 .   ? -9.370  -11.333 18.215 1.00 39.16  ? 1209 OLA   A C15 1 
HETATM 3177 C  C16 . OLA   J  4 .   ? -9.361  -9.809  18.190 1.00 44.69  ? 1209 OLA   A C16 1 
HETATM 3178 C  C17 . OLA   J  4 .   ? -8.063  -9.260  18.772 1.00 45.86  ? 1209 OLA   A C17 1 
HETATM 3179 C  C18 . OLA   J  4 .   ? -8.185  -7.775  19.092 1.00 41.72  ? 1209 OLA   A C18 1 
HETATM 3180 C  C1  . OLA   K  4 .   ? -36.312 14.890  12.751 1.00 69.29  ? 1210 OLA   A C1  1 
HETATM 3181 O  O1  . OLA   K  4 .   ? -35.618 15.830  12.307 1.00 67.80  ? 1210 OLA   A O1  1 
HETATM 3182 O  O2  . OLA   K  4 .   ? -37.077 15.103  13.716 1.00 63.43  ? 1210 OLA   A O2  1 
HETATM 3183 C  C2  . OLA   K  4 .   ? -36.235 13.514  12.132 1.00 56.71  ? 1210 OLA   A C2  1 
HETATM 3184 C  C3  . OLA   K  4 .   ? -36.665 12.484  13.170 1.00 55.12  ? 1210 OLA   A C3  1 
HETATM 3185 C  C4  . OLA   K  4 .   ? -35.917 11.167  12.994 1.00 50.27  ? 1210 OLA   A C4  1 
HETATM 3186 C  C5  . OLA   K  4 .   ? -36.513 10.353  11.852 1.00 45.14  ? 1210 OLA   A C5  1 
HETATM 3187 C  C6  . OLA   K  4 .   ? -36.688 8.892   12.251 1.00 37.72  ? 1210 OLA   A C6  1 
HETATM 3188 C  C7  . OLA   K  4 .   ? -35.852 7.968   11.375 1.00 46.27  ? 1210 OLA   A C7  1 
HETATM 3189 C  C8  . OLA   K  4 .   ? -36.475 6.578   11.313 1.00 37.65  ? 1210 OLA   A C8  1 
HETATM 3190 C  C9  . OLA   K  4 .   ? -35.807 5.762   10.232 1.00 49.16  ? 1210 OLA   A C9  1 
HETATM 3191 C  C10 . OLA   K  4 .   ? -36.494 4.580   9.693  1.00 54.92  ? 1210 OLA   A C10 1 
HETATM 3192 C  C11 . OLA   K  4 .   ? -37.462 3.836   10.581 1.00 55.12  ? 1210 OLA   A C11 1 
HETATM 3193 C  C12 . OLA   K  4 .   ? -38.054 2.642   9.843  1.00 60.76  ? 1210 OLA   A C12 1 
HETATM 3194 C  C13 . OLA   K  4 .   ? -39.262 2.105   10.603 1.00 61.22  ? 1210 OLA   A C13 1 
HETATM 3195 C  C14 . OLA   K  4 .   ? -39.287 0.581   10.611 1.00 70.99  ? 1210 OLA   A C14 1 
HETATM 3196 C  C15 . OLA   K  4 .   ? -38.459 0.022   11.762 1.00 52.48  ? 1210 OLA   A C15 1 
HETATM 3197 C  C16 . OLA   K  4 .   ? -38.328 -1.494  11.667 1.00 64.81  ? 1210 OLA   A C16 1 
HETATM 3198 C  C17 . OLA   K  4 .   ? -39.675 -2.153  11.394 1.00 75.23  ? 1210 OLA   A C17 1 
HETATM 3199 C  C18 . OLA   K  4 .   ? -39.531 -3.666  11.281 1.00 58.91  ? 1210 OLA   A C18 1 
HETATM 3200 C  C1  . OLA   L  4 .   ? -34.453 -21.439 18.141 1.00 62.23  ? 1211 OLA   A C1  1 
HETATM 3201 O  O1  . OLA   L  4 .   ? -33.746 -21.332 17.116 1.00 60.52  ? 1211 OLA   A O1  1 
HETATM 3202 O  O2  . OLA   L  4 .   ? -34.461 -22.525 18.763 1.00 69.14  ? 1211 OLA   A O2  1 
HETATM 3203 C  C2  . OLA   L  4 .   ? -35.289 -20.274 18.619 1.00 59.82  ? 1211 OLA   A C2  1 
HETATM 3204 C  C3  . OLA   L  4 .   ? -35.915 -19.576 17.418 1.00 52.28  ? 1211 OLA   A C3  1 
HETATM 3205 C  C4  . OLA   L  4 .   ? -36.269 -18.126 17.733 1.00 65.52  ? 1211 OLA   A C4  1 
HETATM 3206 C  C5  . OLA   L  4 .   ? -35.023 -17.273 17.934 1.00 59.13  ? 1211 OLA   A C5  1 
HETATM 3207 C  C6  . OLA   L  4 .   ? -35.355 -15.977 18.664 1.00 44.58  ? 1211 OLA   A C6  1 
HETATM 3208 C  C7  . OLA   L  4 .   ? -35.525 -14.834 17.671 1.00 52.57  ? 1211 OLA   A C7  1 
HETATM 3209 C  C8  . OLA   L  4 .   ? -35.443 -13.477 18.360 1.00 54.55  ? 1211 OLA   A C8  1 
HETATM 3210 C  C9  . OLA   L  4 .   ? -35.443 -12.389 17.314 1.00 51.20  ? 1211 OLA   A C9  1 
HETATM 3211 C  C10 . OLA   L  4 .   ? -35.196 -10.992 17.699 1.00 54.42  ? 1211 OLA   A C10 1 
HETATM 3212 C  C11 . OLA   L  4 .   ? -35.846 -10.424 18.939 1.00 54.79  ? 1211 OLA   A C11 1 
HETATM 3213 C  C1  . OLA   M  4 .   ? -20.954 13.365  4.320  1.00 66.87  ? 1212 OLA   A C1  1 
HETATM 3214 O  O1  . OLA   M  4 .   ? -20.775 14.137  3.352  1.00 79.84  ? 1212 OLA   A O1  1 
HETATM 3215 O  O2  . OLA   M  4 .   ? -20.476 13.670  5.435  1.00 59.58  ? 1212 OLA   A O2  1 
HETATM 3216 C  C2  . OLA   M  4 .   ? -21.735 12.085  4.145  1.00 61.01  ? 1212 OLA   A C2  1 
HETATM 3217 C  C3  . OLA   M  4 .   ? -21.372 11.452  2.808  1.00 61.79  ? 1212 OLA   A C3  1 
HETATM 3218 C  C4  . OLA   M  4 .   ? -21.889 10.022  2.714  1.00 61.47  ? 1212 OLA   A C4  1 
HETATM 3219 C  C5  . OLA   M  4 .   ? -21.219 9.121   3.743  1.00 50.91  ? 1212 OLA   A C5  1 
HETATM 3220 C  C6  . OLA   M  4 .   ? -21.126 7.693   3.219  1.00 49.33  ? 1212 OLA   A C6  1 
HETATM 3221 C  C7  . OLA   M  4 .   ? -22.088 6.765   3.954  1.00 53.37  ? 1212 OLA   A C7  1 
HETATM 3222 C  C8  . OLA   M  4 .   ? -22.029 5.347   3.392  1.00 44.09  ? 1212 OLA   A C8  1 
HETATM 3223 C  C9  . OLA   M  4 .   ? -20.612 5.031   2.980  1.00 56.35  ? 1212 OLA   A C9  1 
HETATM 3224 C  C10 . OLA   M  4 .   ? -20.314 3.939   2.041  1.00 55.92  ? 1212 OLA   A C10 1 
HETATM 3225 C  C11 . OLA   M  4 .   ? -20.783 2.528   2.304  1.00 56.65  ? 1212 OLA   A C11 1 
HETATM 3226 C  C12 . OLA   M  4 .   ? -19.801 1.569   1.638  1.00 68.15  ? 1212 OLA   A C12 1 
HETATM 3227 C  C13 . OLA   M  4 .   ? -20.217 0.103   1.743  1.00 77.66  ? 1212 OLA   A C13 1 
HETATM 3228 C  C14 . OLA   M  4 .   ? -21.015 -0.204  3.002  1.00 61.64  ? 1212 OLA   A C14 1 
HETATM 3229 C  C1  . OLA   N  4 .   ? -34.878 13.784  8.024  1.00 77.14  ? 1213 OLA   A C1  1 
HETATM 3230 O  O1  . OLA   N  4 .   ? -33.691 13.864  7.640  1.00 78.42  ? 1213 OLA   A O1  1 
HETATM 3231 O  O2  . OLA   N  4 .   ? -35.426 14.793  8.519  1.00 82.84  ? 1213 OLA   A O2  1 
HETATM 3232 C  C2  . OLA   N  4 .   ? -35.635 12.485  7.890  1.00 69.11  ? 1213 OLA   A C2  1 
HETATM 3233 C  C3  . OLA   N  4 .   ? -34.698 11.322  8.191  1.00 58.13  ? 1213 OLA   A C3  1 
HETATM 3234 C  C4  . OLA   N  4 .   ? -35.478 10.023  8.357  1.00 59.10  ? 1213 OLA   A C4  1 
HETATM 3235 C  C5  . OLA   N  4 .   ? -35.955 9.500   7.008  1.00 55.85  ? 1213 OLA   A C5  1 
HETATM 3236 C  C6  . OLA   N  4 .   ? -35.771 7.991   6.895  1.00 61.91  ? 1213 OLA   A C6  1 
HETATM 3237 C  C7  . OLA   N  4 .   ? -36.731 7.418   5.858  1.00 63.61  ? 1213 OLA   A C7  1 
HETATM 3238 C  C8  . OLA   N  4 .   ? -36.882 5.907   5.992  1.00 70.36  ? 1213 OLA   A C8  1 
HETATM 3239 C  C9  . OLA   N  4 .   ? -38.020 5.455   5.107  1.00 70.42  ? 1213 OLA   A C9  1 
HETATM 3240 C  C10 . OLA   N  4 .   ? -38.541 4.082   5.187  1.00 78.76  ? 1213 OLA   A C10 1 
HETATM 3241 C  C11 . OLA   N  4 .   ? -37.610 2.902   5.044  1.00 80.39  ? 1213 OLA   A C11 1 
HETATM 3242 C  C1  . OLA   O  4 .   ? -15.917 14.169  1.137  1.00 66.70  ? 1214 OLA   A C1  1 
HETATM 3243 O  O1  . OLA   O  4 .   ? -14.797 14.716  1.036  1.00 81.16  ? 1214 OLA   A O1  1 
HETATM 3244 O  O2  . OLA   O  4 .   ? -16.902 14.858  1.483  1.00 74.14  ? 1214 OLA   A O2  1 
HETATM 3245 C  C2  . OLA   O  4 .   ? -16.079 12.697  0.841  1.00 57.05  ? 1214 OLA   A C2  1 
HETATM 3246 C  C3  . OLA   O  4 .   ? -14.732 11.996  0.983  1.00 58.96  ? 1214 OLA   A C3  1 
HETATM 3247 C  C4  . OLA   O  4 .   ? -14.639 10.772  0.077  1.00 63.03  ? 1214 OLA   A C4  1 
HETATM 3248 C  C5  . OLA   O  4 .   ? -15.126 9.516   0.794  1.00 60.54  ? 1214 OLA   A C5  1 
HETATM 3249 C  C6  . OLA   O  4 .   ? -16.582 9.209   0.461  1.00 58.77  ? 1214 OLA   A C6  1 
HETATM 3250 C  C7  . OLA   O  4 .   ? -17.011 7.835   0.965  1.00 65.38  ? 1214 OLA   A C7  1 
HETATM 3251 C  C8  . OLA   O  4 .   ? -15.987 6.746   0.659  1.00 55.95  ? 1214 OLA   A C8  1 
HETATM 3252 C  C9  . OLA   O  4 .   ? -16.445 5.467   1.320  1.00 67.93  ? 1214 OLA   A C9  1 
HETATM 3253 C  C10 . OLA   O  4 .   ? -15.568 4.289   1.398  1.00 66.10  ? 1214 OLA   A C10 1 
HETATM 3254 C  C11 . OLA   O  4 .   ? -14.946 3.712   0.149  1.00 71.88  ? 1214 OLA   A C11 1 
HETATM 3255 C  C1  . OLA   P  4 .   ? -34.026 9.600   2.887  1.00 68.55  ? 1215 OLA   A C1  1 
HETATM 3256 O  O1  . OLA   P  4 .   ? -33.486 10.728  2.896  1.00 71.43  ? 1215 OLA   A O1  1 
HETATM 3257 O  O2  . OLA   P  4 .   ? -35.164 9.469   3.387  1.00 83.74  ? 1215 OLA   A O2  1 
HETATM 3258 C  C2  . OLA   P  4 .   ? -33.324 8.409   2.278  1.00 57.93  ? 1215 OLA   A C2  1 
HETATM 3259 C  C3  . OLA   P  4 .   ? -33.774 8.247   0.831  1.00 48.60  ? 1215 OLA   A C3  1 
HETATM 3260 C  C4  . OLA   P  4 .   ? -34.908 7.232   0.728  1.00 57.19  ? 1215 OLA   A C4  1 
HETATM 3261 C  C5  . OLA   P  4 .   ? -34.542 5.911   1.393  1.00 49.37  ? 1215 OLA   A C5  1 
HETATM 3262 C  C6  . OLA   P  4 .   ? -35.229 4.744   0.690  1.00 56.36  ? 1215 OLA   A C6  1 
HETATM 3263 C  C7  . OLA   P  4 .   ? -34.224 3.663   0.308  1.00 54.57  ? 1215 OLA   A C7  1 
HETATM 3264 C  C8  . OLA   P  4 .   ? -34.388 2.405   1.154  1.00 64.68  ? 1215 OLA   A C8  1 
HETATM 3265 C  C9  . OLA   P  4 .   ? -33.037 1.754   1.342  1.00 65.40  ? 1215 OLA   A C9  1 
HETATM 3266 C  C10 . OLA   P  4 .   ? -32.921 0.308   1.592  1.00 57.67  ? 1215 OLA   A C10 1 
HETATM 3267 C  C11 . OLA   P  4 .   ? -34.127 -0.506  1.993  1.00 62.53  ? 1215 OLA   A C11 1 
HETATM 3268 C  C1  . OLA   Q  4 .   ? -20.839 -22.772 27.672 1.00 64.12  ? 1216 OLA   A C1  1 
HETATM 3269 O  O1  . OLA   Q  4 .   ? -21.164 -22.771 26.466 1.00 69.65  ? 1216 OLA   A O1  1 
HETATM 3270 O  O2  . OLA   Q  4 .   ? -21.559 -23.384 28.491 1.00 80.86  ? 1216 OLA   A O2  1 
HETATM 3271 C  C2  . OLA   Q  4 .   ? -19.598 -22.045 28.132 1.00 45.97  ? 1216 OLA   A C2  1 
HETATM 3272 C  C3  . OLA   Q  4 .   ? -19.872 -20.551 28.260 1.00 51.06  ? 1216 OLA   A C3  1 
HETATM 3273 C  C4  . OLA   Q  4 .   ? -19.381 -20.027 29.607 1.00 57.07  ? 1216 OLA   A C4  1 
HETATM 3274 C  C5  . OLA   Q  4 .   ? -19.863 -18.606 29.881 1.00 56.62  ? 1216 OLA   A C5  1 
HETATM 3275 C  C6  . OLA   Q  4 .   ? -19.798 -17.735 28.632 1.00 53.23  ? 1216 OLA   A C6  1 
HETATM 3276 C  C7  . OLA   Q  4 .   ? -19.091 -16.410 28.895 1.00 48.74  ? 1216 OLA   A C7  1 
HETATM 3277 C  C8  . OLA   Q  4 .   ? -19.731 -15.663 30.059 1.00 56.66  ? 1216 OLA   A C8  1 
HETATM 3278 C  C1  . OLA   R  4 .   ? -43.772 -24.482 12.679 1.00 70.74  ? 1217 OLA   A C1  1 
HETATM 3279 O  O1  . OLA   R  4 .   ? -43.820 -25.488 11.939 1.00 73.34  ? 1217 OLA   A O1  1 
HETATM 3280 O  O2  . OLA   R  4 .   ? -43.434 -24.624 13.874 1.00 77.13  ? 1217 OLA   A O2  1 
HETATM 3281 C  C2  . OLA   R  4 .   ? -44.113 -23.115 12.135 1.00 60.50  ? 1217 OLA   A C2  1 
HETATM 3282 C  C3  . OLA   R  4 .   ? -44.657 -22.235 13.254 1.00 60.99  ? 1217 OLA   A C3  1 
HETATM 3283 C  C4  . OLA   R  4 .   ? -43.739 -21.051 13.535 1.00 58.13  ? 1217 OLA   A C4  1 
HETATM 3284 C  C5  . OLA   R  4 .   ? -42.777 -21.354 14.678 1.00 66.82  ? 1217 OLA   A C5  1 
HETATM 3285 C  C6  . OLA   R  4 .   ? -41.429 -20.676 14.460 1.00 69.77  ? 1217 OLA   A C6  1 
HETATM 3286 C  C7  . OLA   R  4 .   ? -40.957 -19.949 15.714 1.00 67.41  ? 1217 OLA   A C7  1 
HETATM 3287 C  C8  . OLA   R  4 .   ? -40.069 -18.767 15.343 1.00 71.63  ? 1217 OLA   A C8  1 
HETATM 3288 C  C9  . OLA   R  4 .   ? -38.710 -19.261 14.909 1.00 65.00  ? 1217 OLA   A C9  1 
HETATM 3289 C  C10 . OLA   R  4 .   ? -37.730 -18.297 14.389 1.00 52.71  ? 1217 OLA   A C10 1 
HETATM 3290 C  C11 . OLA   R  4 .   ? -38.118 -17.386 13.248 1.00 59.36  ? 1217 OLA   A C11 1 
HETATM 3291 C  C12 . OLA   R  4 .   ? -37.320 -16.091 13.337 1.00 53.78  ? 1217 OLA   A C12 1 
HETATM 3292 C  C13 . OLA   R  4 .   ? -37.633 -15.367 14.641 1.00 46.29  ? 1217 OLA   A C13 1 
HETATM 3293 C  C14 . OLA   R  4 .   ? -37.320 -13.878 14.552 1.00 54.85  ? 1217 OLA   A C14 1 
HETATM 3294 C  C15 . OLA   R  4 .   ? -38.425 -13.110 13.838 1.00 64.31  ? 1217 OLA   A C15 1 
HETATM 3295 C  C16 . OLA   R  4 .   ? -38.226 -11.608 14.009 1.00 57.53  ? 1217 OLA   A C16 1 
HETATM 3296 C  C17 . OLA   R  4 .   ? -38.706 -10.839 12.784 1.00 61.32  ? 1217 OLA   A C17 1 
HETATM 3297 C  C1  . OLA   S  4 .   ? -35.925 -15.468 4.721  1.00 80.77  ? 1218 OLA   A C1  1 
HETATM 3298 O  O1  . OLA   S  4 .   ? -36.421 -16.508 5.206  1.00 74.88  ? 1218 OLA   A O1  1 
HETATM 3299 O  O2  . OLA   S  4 .   ? -35.529 -14.569 5.494  1.00 76.85  ? 1218 OLA   A O2  1 
HETATM 3300 C  C2  . OLA   S  4 .   ? -35.811 -15.297 3.224  1.00 66.79  ? 1218 OLA   A C2  1 
HETATM 3301 C  C3  . OLA   S  4 .   ? -34.534 -14.537 2.880  1.00 74.18  ? 1218 OLA   A C3  1 
HETATM 3302 C  C4  . OLA   S  4 .   ? -33.540 -15.439 2.156  1.00 71.62  ? 1218 OLA   A C4  1 
HETATM 3303 C  C5  . OLA   S  4 .   ? -32.442 -14.629 1.476  1.00 57.57  ? 1218 OLA   A C5  1 
HETATM 3304 C  C6  . OLA   S  4 .   ? -31.186 -14.555 2.336  1.00 48.66  ? 1218 OLA   A C6  1 
HETATM 3305 C  C7  . OLA   S  4 .   ? -30.920 -13.125 2.787  1.00 47.29  ? 1218 OLA   A C7  1 
HETATM 3306 C  C8  . OLA   S  4 .   ? -29.448 -12.919 3.125  1.00 45.78  ? 1218 OLA   A C8  1 
HETATM 3307 C  C9  . OLA   S  4 .   ? -29.191 -11.444 3.318  1.00 44.26  ? 1218 OLA   A C9  1 
HETATM 3308 C  C10 . OLA   S  4 .   ? -27.824 -10.952 3.528  1.00 47.05  ? 1218 OLA   A C10 1 
HETATM 3309 C  C1  . OLA   T  4 .   ? -27.798 -20.866 39.664 1.00 78.37  ? 1219 OLA   A C1  1 
HETATM 3310 O  O1  . OLA   T  4 .   ? -27.164 -21.879 39.297 1.00 73.82  ? 1219 OLA   A O1  1 
HETATM 3311 O  O2  . OLA   T  4 .   ? -28.902 -21.016 40.232 1.00 71.45  ? 1219 OLA   A O2  1 
HETATM 3312 C  C2  . OLA   T  4 .   ? -27.241 -19.482 39.422 1.00 79.00  ? 1219 OLA   A C2  1 
HETATM 3313 C  C3  . OLA   T  4 .   ? -28.218 -18.437 39.949 1.00 80.97  ? 1219 OLA   A C3  1 
HETATM 3314 C  C4  . OLA   T  4 .   ? -27.870 -17.035 39.458 1.00 59.93  ? 1219 OLA   A C4  1 
HETATM 3315 C  C5  . OLA   T  4 .   ? -26.381 -16.741 39.610 1.00 70.86  ? 1219 OLA   A C5  1 
HETATM 3316 C  C6  . OLA   T  4 .   ? -25.827 -16.133 38.328 1.00 61.53  ? 1219 OLA   A C6  1 
HETATM 3317 C  C7  . OLA   T  4 .   ? -24.561 -15.320 38.569 1.00 56.05  ? 1219 OLA   A C7  1 
HETATM 3318 C  C8  . OLA   T  4 .   ? -24.783 -13.845 38.250 1.00 50.43  ? 1219 OLA   A C8  1 
HETATM 3319 C  C9  . OLA   T  4 .   ? -23.447 -13.163 38.067 1.00 63.29  ? 1219 OLA   A C9  1 
HETATM 3320 C  C10 . OLA   T  4 .   ? -23.196 -11.832 38.642 1.00 70.68  ? 1219 OLA   A C10 1 
HETATM 3321 C  C11 . OLA   T  4 .   ? -24.295 -10.800 38.727 1.00 61.88  ? 1219 OLA   A C11 1 
HETATM 3322 C  C12 . OLA   T  4 .   ? -23.832 -9.630  39.589 1.00 66.58  ? 1219 OLA   A C12 1 
HETATM 3323 C  C13 . OLA   T  4 .   ? -22.703 -8.853  38.921 1.00 65.97  ? 1219 OLA   A C13 1 
HETATM 3324 C  C14 . OLA   T  4 .   ? -23.030 -7.367  38.806 1.00 48.97  ? 1219 OLA   A C14 1 
HETATM 3325 C  C15 . OLA   T  4 .   ? -22.817 -6.887  37.375 1.00 57.38  ? 1219 OLA   A C15 1 
HETATM 3326 C  C16 . OLA   T  4 .   ? -22.353 -5.436  37.320 1.00 55.74  ? 1219 OLA   A C16 1 
HETATM 3327 C  C17 . OLA   T  4 .   ? -22.538 -4.863  35.919 1.00 46.50  ? 1219 OLA   A C17 1 
HETATM 3328 C  C18 . OLA   T  4 .   ? -21.789 -3.546  35.755 1.00 45.93  ? 1219 OLA   A C18 1 
HETATM 3329 C  C6  . OLA   U  4 .   ? -20.321 -12.179 0.561  1.00 72.62  ? 1220 OLA   A C6  1 
HETATM 3330 C  C7  . OLA   U  4 .   ? -21.433 -11.667 1.469  1.00 70.58  ? 1220 OLA   A C7  1 
HETATM 3331 C  C8  . OLA   U  4 .   ? -20.989 -10.447 2.268  1.00 70.26  ? 1220 OLA   A C8  1 
HETATM 3332 C  C9  . OLA   U  4 .   ? -22.177 -9.903  3.022  1.00 61.62  ? 1220 OLA   A C9  1 
HETATM 3333 C  C10 . OLA   U  4 .   ? -22.410 -8.453  3.085  1.00 60.97  ? 1220 OLA   A C10 1 
HETATM 3334 C  C11 . OLA   U  4 .   ? -21.375 -7.530  3.681  1.00 50.95  ? 1220 OLA   A C11 1 
HETATM 3335 C  C12 . OLA   U  4 .   ? -21.585 -6.114  3.155  1.00 59.85  ? 1220 OLA   A C12 1 
HETATM 3336 C  C13 . OLA   U  4 .   ? -23.062 -5.756  3.031  1.00 42.58  ? 1220 OLA   A C13 1 
HETATM 3337 C  C14 . OLA   U  4 .   ? -23.225 -4.272  2.720  1.00 43.82  ? 1220 OLA   A C14 1 
HETATM 3338 C  C15 . OLA   U  4 .   ? -24.608 -3.961  2.161  1.00 47.96  ? 1220 OLA   A C15 1 
HETATM 3339 C  C16 . OLA   U  4 .   ? -24.844 -2.455  2.108  1.00 52.66  ? 1220 OLA   A C16 1 
HETATM 3340 C  C17 . OLA   U  4 .   ? -23.797 -1.756  1.249  1.00 62.97  ? 1220 OLA   A C17 1 
HETATM 3341 C  C1  . OLA   V  4 .   ? -8.775  14.645  8.456  1.00 75.70  ? 1221 OLA   A C1  1 
HETATM 3342 O  O1  . OLA   V  4 .   ? -9.018  15.441  7.523  1.00 78.48  ? 1221 OLA   A O1  1 
HETATM 3343 O  O2  . OLA   V  4 .   ? -9.129  14.943  9.620  1.00 64.52  ? 1221 OLA   A O2  1 
HETATM 3344 C  C2  . OLA   V  4 .   ? -8.056  13.347  8.182  1.00 56.41  ? 1221 OLA   A C2  1 
HETATM 3345 C  C3  . OLA   V  4 .   ? -8.575  12.744  6.884  1.00 54.05  ? 1221 OLA   A C3  1 
HETATM 3346 C  C4  . OLA   V  4 .   ? -9.231  11.396  7.144  1.00 56.98  ? 1221 OLA   A C4  1 
HETATM 3347 C  C5  . OLA   V  4 .   ? -8.945  10.428  6.005  1.00 55.26  ? 1221 OLA   A C5  1 
HETATM 3348 C  C6  . OLA   V  4 .   ? -7.673  9.632   6.286  1.00 56.58  ? 1221 OLA   A C6  1 
HETATM 3349 C  C7  . OLA   V  4 .   ? -7.935  8.457   7.224  1.00 63.22  ? 1221 OLA   A C7  1 
HETATM 3350 C  C8  . OLA   V  4 .   ? -7.942  7.111   6.504  1.00 60.70  ? 1221 OLA   A C8  1 
HETATM 3351 C  C9  . OLA   V  4 .   ? -8.181  7.316   5.031  1.00 73.74  ? 1221 OLA   A C9  1 
HETATM 3352 C  C10 . OLA   V  4 .   ? -9.489  7.003   4.443  1.00 81.94  ? 1221 OLA   A C10 1 
HETATM 3353 C  C11 . OLA   V  4 .   ? -10.179 5.697   4.744  1.00 65.16  ? 1221 OLA   A C11 1 
HETATM 3354 C  C12 . OLA   V  4 .   ? -10.440 5.030   3.401  1.00 68.18  ? 1221 OLA   A C12 1 
HETATM 3355 C  C13 . OLA   V  4 .   ? -11.908 4.688   3.202  1.00 71.26  ? 1221 OLA   A C13 1 
HETATM 3356 C  C14 . OLA   V  4 .   ? -12.028 3.383   2.426  1.00 73.50  ? 1221 OLA   A C14 1 
HETATM 3357 C  C15 . OLA   V  4 .   ? -11.699 2.200   3.328  1.00 74.86  ? 1221 OLA   A C15 1 
HETATM 3358 C  C16 . OLA   V  4 .   ? -11.422 0.946   2.508  1.00 71.97  ? 1221 OLA   A C16 1 
HETATM 3359 C  C10 . OLA   W  4 .   ? -12.035 -3.258  7.269  1.00 52.71  ? 1222 OLA   A C10 1 
HETATM 3360 C  C11 . OLA   W  4 .   ? -11.914 -1.802  7.654  1.00 55.57  ? 1222 OLA   A C11 1 
HETATM 3361 C  C12 . OLA   W  4 .   ? -10.887 -1.127  6.754  1.00 71.20  ? 1222 OLA   A C12 1 
HETATM 3362 C  C13 . OLA   W  4 .   ? -10.563 0.293   7.210  1.00 65.18  ? 1222 OLA   A C13 1 
HETATM 3363 C  C14 . OLA   W  4 .   ? -11.795 1.045   7.701  1.00 58.88  ? 1222 OLA   A C14 1 
HETATM 3364 C  C15 . OLA   W  4 .   ? -11.585 2.550   7.572  1.00 48.94  ? 1222 OLA   A C15 1 
HETATM 3365 C  C16 . OLA   W  4 .   ? -12.573 3.330   8.430  1.00 46.98  ? 1222 OLA   A C16 1 
HETATM 3366 C  C17 . OLA   W  4 .   ? -13.988 2.783   8.283  1.00 41.49  ? 1222 OLA   A C17 1 
HETATM 3367 C  C4  . OLA   X  4 .   ? -32.870 -17.956 26.439 1.00 51.86  ? 1223 OLA   A C4  1 
HETATM 3368 C  C5  . OLA   X  4 .   ? -33.827 -16.899 26.976 1.00 49.91  ? 1223 OLA   A C5  1 
HETATM 3369 C  C6  . OLA   X  4 .   ? -33.137 -15.550 27.154 1.00 57.04  ? 1223 OLA   A C6  1 
HETATM 3370 C  C7  . OLA   X  4 .   ? -34.145 -14.416 27.009 1.00 56.10  ? 1223 OLA   A C7  1 
HETATM 3371 C  C8  . OLA   X  4 .   ? -33.492 -13.039 27.084 1.00 56.40  ? 1223 OLA   A C8  1 
HETATM 3372 C  C9  . OLA   X  4 .   ? -33.183 -12.692 28.523 1.00 64.18  ? 1223 OLA   A C9  1 
HETATM 3373 C  C10 . OLA   X  4 .   ? -33.424 -11.330 29.028 1.00 57.39  ? 1223 OLA   A C10 1 
HETATM 3374 C  C11 . OLA   X  4 .   ? -33.890 -10.244 28.086 1.00 55.24  ? 1223 OLA   A C11 1 
HETATM 3375 C  C12 . OLA   X  4 .   ? -33.423 -8.877  28.575 1.00 55.19  ? 1223 OLA   A C12 1 
HETATM 3376 C  C13 . OLA   X  4 .   ? -33.830 -8.604  30.019 1.00 53.47  ? 1223 OLA   A C13 1 
HETATM 3377 C  C14 . OLA   X  4 .   ? -33.170 -7.327  30.530 1.00 47.12  ? 1223 OLA   A C14 1 
HETATM 3378 C  C15 . OLA   X  4 .   ? -34.195 -6.265  30.914 1.00 60.74  ? 1223 OLA   A C15 1 
HETATM 3379 C  C16 . OLA   X  4 .   ? -33.529 -4.913  31.154 1.00 49.92  ? 1223 OLA   A C16 1 
HETATM 3380 C  C17 . OLA   X  4 .   ? -32.296 -5.034  32.045 1.00 49.33  ? 1223 OLA   A C17 1 
HETATM 3381 C  C18 . OLA   X  4 .   ? -32.674 -5.187  33.513 1.00 68.38  ? 1223 OLA   A C18 1 
HETATM 3382 C  C1  . OLA   Y  4 .   ? -34.851 8.580   33.088 1.00 65.86  ? 1224 OLA   A C1  1 
HETATM 3383 O  O1  . OLA   Y  4 .   ? -34.525 9.787   33.076 1.00 66.66  ? 1224 OLA   A O1  1 
HETATM 3384 O  O2  . OLA   Y  4 .   ? -36.035 8.277   33.348 1.00 75.98  ? 1224 OLA   A O2  1 
HETATM 3385 C  C2  . OLA   Y  4 .   ? -33.823 7.509   32.805 1.00 51.86  ? 1224 OLA   A C2  1 
HETATM 3386 C  C3  . OLA   Y  4 .   ? -34.480 6.243   32.266 1.00 49.53  ? 1224 OLA   A C3  1 
HETATM 3387 C  C4  . OLA   Y  4 .   ? -33.811 5.008   32.861 1.00 50.58  ? 1224 OLA   A C4  1 
HETATM 3388 C  C5  . OLA   Y  4 .   ? -33.843 3.827   31.898 1.00 59.69  ? 1224 OLA   A C5  1 
HETATM 3389 C  C6  . OLA   Y  4 .   ? -33.593 2.516   32.637 1.00 56.38  ? 1224 OLA   A C6  1 
HETATM 3390 C  C7  . OLA   Y  4 .   ? -32.100 2.229   32.745 1.00 46.42  ? 1224 OLA   A C7  1 
HETATM 3391 C  C8  . OLA   Y  4 .   ? -31.838 0.744   32.974 1.00 53.62  ? 1224 OLA   A C8  1 
HETATM 3392 C  C9  . OLA   Y  4 .   ? -30.354 0.514   33.135 1.00 45.41  ? 1224 OLA   A C9  1 
HETATM 3393 C  C10 . OLA   Y  4 .   ? -29.792 -0.839  33.008 1.00 45.23  ? 1224 OLA   A C10 1 
HETATM 3394 C  C11 . OLA   Y  4 .   ? -30.550 -2.034  33.534 1.00 45.69  ? 1224 OLA   A C11 1 
HETATM 3395 C  C1  . OLA   Z  4 .   ? -3.898  9.165   30.327 1.00 68.52  ? 1225 OLA   A C1  1 
HETATM 3396 O  O1  . OLA   Z  4 .   ? -4.750  9.515   29.483 1.00 76.30  ? 1225 OLA   A O1  1 
HETATM 3397 O  O2  . OLA   Z  4 .   ? -3.161  10.039  30.835 1.00 83.38  ? 1225 OLA   A O2  1 
HETATM 3398 C  C2  . OLA   Z  4 .   ? -3.751  7.713   30.719 1.00 56.76  ? 1225 OLA   A C2  1 
HETATM 3399 C  C3  . OLA   Z  4 .   ? -3.406  6.894   29.480 1.00 56.48  ? 1225 OLA   A C3  1 
HETATM 3400 C  C4  . OLA   Z  4 .   ? -4.263  5.638   29.356 1.00 50.56  ? 1225 OLA   A C4  1 
HETATM 3401 C  C5  . OLA   Z  4 .   ? -3.690  4.486   30.175 1.00 48.63  ? 1225 OLA   A C5  1 
HETATM 3402 C  C6  . OLA   Z  4 .   ? -3.560  3.219   29.333 1.00 67.77  ? 1225 OLA   A C6  1 
HETATM 3403 C  C7  . OLA   Z  4 .   ? -4.711  2.254   29.596 1.00 50.87  ? 1225 OLA   A C7  1 
HETATM 3404 C  C8  . OLA   Z  4 .   ? -4.418  0.845   29.088 1.00 63.23  ? 1225 OLA   A C8  1 
HETATM 3405 C  C9  . OLA   Z  4 .   ? -5.736  0.115   28.975 1.00 72.12  ? 1225 OLA   A C9  1 
HETATM 3406 C  C10 . OLA   Z  4 .   ? -5.855  -1.345  29.110 1.00 82.81  ? 1225 OLA   A C10 1 
HETATM 3407 C  C11 . OLA   Z  4 .   ? -5.855  -2.262  27.909 1.00 69.25  ? 1225 OLA   A C11 1 
HETATM 3408 C  C12 . OLA   Z  4 .   ? -6.524  -3.571  28.314 1.00 70.71  ? 1225 OLA   A C12 1 
HETATM 3409 C  C13 . OLA   Z  4 .   ? -6.238  -4.691  27.321 1.00 68.70  ? 1225 OLA   A C13 1 
HETATM 3410 C  C1  . OLA   AA 4 .   ? -36.440 11.517  29.936 1.00 68.67  ? 1226 OLA   A C1  1 
HETATM 3411 O  O1  . OLA   AA 4 .   ? -36.066 10.987  31.004 1.00 87.24  ? 1226 OLA   A O1  1 
HETATM 3412 O  O2  . OLA   AA 4 .   ? -36.636 12.752  29.909 1.00 80.01  ? 1226 OLA   A O2  1 
HETATM 3413 C  C2  . OLA   AA 4 .   ? -36.642 10.680  28.696 1.00 56.75  ? 1226 OLA   A C2  1 
HETATM 3414 C  C3  . OLA   AA 4 .   ? -36.957 9.239   29.085 1.00 63.57  ? 1226 OLA   A C3  1 
HETATM 3415 C  C4  . OLA   AA 4 .   ? -35.789 8.330   28.720 1.00 53.60  ? 1226 OLA   A C4  1 
HETATM 3416 C  C5  . OLA   AA 4 .   ? -36.257 7.032   28.071 1.00 50.25  ? 1226 OLA   A C5  1 
HETATM 3417 C  C6  . OLA   AA 4 .   ? -37.334 6.355   28.908 1.00 60.76  ? 1226 OLA   A C6  1 
HETATM 3418 C  C7  . OLA   AA 4 .   ? -36.787 5.090   29.557 1.00 71.76  ? 1226 OLA   A C7  1 
HETATM 3419 C  C8  . OLA   AA 4 .   ? -36.320 4.080   28.513 1.00 67.23  ? 1226 OLA   A C8  1 
HETATM 3420 C  C9  . OLA   AA 4 .   ? -37.541 3.568   27.789 1.00 72.44  ? 1226 OLA   A C9  1 
HETATM 3421 C  C10 . OLA   AA 4 .   ? -37.902 2.144   27.826 1.00 68.86  ? 1226 OLA   A C10 1 
HETATM 3422 C  C11 . OLA   AA 4 .   ? -37.433 1.167   26.775 1.00 61.59  ? 1226 OLA   A C11 1 
HETATM 3423 C  C12 . OLA   AA 4 .   ? -38.011 -0.215  27.075 1.00 81.84  ? 1226 OLA   A C12 1 
HETATM 3424 C  C13 . OLA   AA 4 .   ? -39.313 -0.129  27.869 1.00 79.35  ? 1226 OLA   A C13 1 
HETATM 3425 C  C14 . OLA   AA 4 .   ? -39.920 -1.509  28.095 1.00 79.09  ? 1226 OLA   A C14 1 
HETATM 3426 C  C15 . OLA   AA 4 .   ? -40.073 -2.239  26.766 1.00 80.69  ? 1226 OLA   A C15 1 
HETATM 3427 C  C16 . OLA   AA 4 .   ? -40.703 -3.617  26.935 1.00 77.45  ? 1226 OLA   A C16 1 
HETATM 3428 C  C17 . OLA   AA 4 .   ? -40.483 -4.450  25.677 1.00 77.45  ? 1226 OLA   A C17 1 
HETATM 3429 C  C18 . OLA   AA 4 .   ? -41.233 -5.775  25.744 1.00 69.52  ? 1226 OLA   A C18 1 
HETATM 3430 C  C1  . OLA   BA 4 .   ? -28.308 -20.890 34.918 1.00 74.75  ? 1227 OLA   A C1  1 
HETATM 3431 O  O1  . OLA   BA 4 .   ? -27.204 -20.317 35.053 1.00 75.49  ? 1227 OLA   A O1  1 
HETATM 3432 O  O2  . OLA   BA 4 .   ? -28.369 -21.930 34.226 1.00 66.82  ? 1227 OLA   A O2  1 
HETATM 3433 C  C2  . OLA   BA 4 .   ? -29.550 -20.342 35.584 1.00 72.70  ? 1227 OLA   A C2  1 
HETATM 3434 C  C3  . OLA   BA 4 .   ? -29.582 -18.820 35.483 1.00 74.15  ? 1227 OLA   A C3  1 
HETATM 3435 C  C4  . OLA   BA 4 .   ? -31.016 -18.303 35.438 1.00 69.12  ? 1227 OLA   A C4  1 
HETATM 3436 C  C5  . OLA   BA 4 .   ? -31.105 -16.904 36.038 1.00 72.98  ? 1227 OLA   A C5  1 
HETATM 3437 C  C6  . OLA   BA 4 .   ? -31.481 -15.855 34.997 1.00 75.39  ? 1227 OLA   A C6  1 
HETATM 3438 C  C7  . OLA   BA 4 .   ? -31.689 -14.500 35.666 1.00 71.04  ? 1227 OLA   A C7  1 
HETATM 3439 C  C8  . OLA   BA 4 .   ? -30.339 -13.847 35.938 1.00 78.14  ? 1227 OLA   A C8  1 
HETATM 3440 C  C9  . OLA   BA 4 .   ? -30.493 -12.561 36.715 1.00 69.00  ? 1227 OLA   A C9  1 
HETATM 3441 C  C10 . OLA   BA 4 .   ? -29.393 -11.585 36.680 1.00 62.75  ? 1227 OLA   A C10 1 
HETATM 3442 C  C11 . OLA   BA 4 .   ? -28.025 -12.064 36.251 1.00 63.27  ? 1227 OLA   A C11 1 
HETATM 3443 C  C12 . OLA   BA 4 .   ? -26.971 -10.966 36.355 1.00 49.92  ? 1227 OLA   A C12 1 
HETATM 3444 C  C13 . OLA   BA 4 .   ? -27.417 -9.770  37.187 1.00 70.20  ? 1227 OLA   A C13 1 
HETATM 3445 C  C14 . OLA   BA 4 .   ? -26.902 -8.484  36.550 1.00 72.30  ? 1227 OLA   A C14 1 
HETATM 3446 C  C15 . OLA   BA 4 .   ? -26.600 -7.409  37.587 1.00 60.40  ? 1227 OLA   A C15 1 
HETATM 3447 C  C16 . OLA   BA 4 .   ? -26.763 -6.020  36.983 1.00 39.94  ? 1227 OLA   A C16 1 
HETATM 3448 C  C17 . OLA   BA 4 .   ? -28.237 -5.719  36.744 1.00 40.28  ? 1227 OLA   A C17 1 
HETATM 3449 C  C18 . OLA   BA 4 .   ? -28.458 -4.240  36.454 1.00 55.25  ? 1227 OLA   A C18 1 
HETATM 3450 C  C1  . OLA   CA 4 .   ? -31.693 8.388   36.274 1.00 54.46  ? 1228 OLA   A C1  1 
HETATM 3451 O  O1  . OLA   CA 4 .   ? -30.940 9.386   36.234 1.00 55.66  ? 1228 OLA   A O1  1 
HETATM 3452 O  O2  . OLA   CA 4 .   ? -32.931 8.558   36.290 1.00 66.22  ? 1228 OLA   A O2  1 
HETATM 3453 C  C2  . OLA   CA 4 .   ? -31.114 6.996   36.313 1.00 38.64  ? 1228 OLA   A C2  1 
HETATM 3454 C  C3  . OLA   CA 4 .   ? -32.211 5.973   36.062 1.00 37.73  ? 1228 OLA   A C3  1 
HETATM 3455 C  C4  . OLA   CA 4 .   ? -32.128 4.851   37.088 1.00 42.31  ? 1228 OLA   A C4  1 
HETATM 3456 C  C5  . OLA   CA 4 .   ? -31.807 3.526   36.411 1.00 43.63  ? 1228 OLA   A C5  1 
HETATM 3457 C  C6  . OLA   CA 4 .   ? -32.245 2.346   37.267 1.00 51.97  ? 1228 OLA   A C6  1 
HETATM 3458 C  C7  . OLA   CA 4 .   ? -31.049 1.528   37.739 1.00 44.33  ? 1228 OLA   A C7  1 
HETATM 3459 C  C8  . OLA   CA 4 .   ? -31.460 0.080   37.972 1.00 54.13  ? 1228 OLA   A C8  1 
HETATM 3460 C  C9  . OLA   CA 4 .   ? -30.264 -0.749  38.376 1.00 39.51  ? 1228 OLA   A C9  1 
HETATM 3461 C  C10 . OLA   CA 4 .   ? -30.426 -2.191  38.609 1.00 47.56  ? 1228 OLA   A C10 1 
HETATM 3462 C  C3  . OLA   DA 4 .   ? -16.934 -16.286 3.016  1.00 74.45  ? 1229 OLA   A C3  1 
HETATM 3463 C  C4  . OLA   DA 4 .   ? -17.898 -15.112 2.892  1.00 71.09  ? 1229 OLA   A C4  1 
HETATM 3464 C  C5  . OLA   DA 4 .   ? -17.234 -13.820 3.351  1.00 68.81  ? 1229 OLA   A C5  1 
HETATM 3465 C  C6  . OLA   DA 4 .   ? -18.237 -12.913 4.052  1.00 67.28  ? 1229 OLA   A C6  1 
HETATM 3466 C  C7  . OLA   DA 4 .   ? -17.848 -11.450 3.889  1.00 71.14  ? 1229 OLA   A C7  1 
HETATM 3467 C  C8  . OLA   DA 4 .   ? -16.519 -11.140 4.568  1.00 63.16  ? 1229 OLA   A C8  1 
HETATM 3468 C  C9  . OLA   DA 4 .   ? -15.891 -9.961  3.865  1.00 70.94  ? 1229 OLA   A C9  1 
HETATM 3469 C  C10 . OLA   DA 4 .   ? -15.721 -8.692  4.585  1.00 72.49  ? 1229 OLA   A C10 1 
HETATM 3470 C  C11 . OLA   DA 4 .   ? -16.799 -8.255  5.549  1.00 65.91  ? 1229 OLA   A C11 1 
HETATM 3471 C  C12 . OLA   DA 4 .   ? -16.820 -6.735  5.653  1.00 47.56  ? 1229 OLA   A C12 1 
HETATM 3472 C  C1  . OLA   EA 4 .   ? -9.848  -15.231 12.154 1.00 62.74  ? 1230 OLA   A C1  1 
HETATM 3473 C  C2  . OLA   EA 4 .   ? -9.563  -14.080 11.196 1.00 65.16  ? 1230 OLA   A C2  1 
HETATM 3474 C  C3  . OLA   EA 4 .   ? -10.653 -13.956 10.135 1.00 65.03  ? 1230 OLA   A C3  1 
HETATM 3475 C  C4  . OLA   EA 4 .   ? -10.739 -12.536 9.586  1.00 51.05  ? 1230 OLA   A C4  1 
HETATM 3476 C  C5  . OLA   EA 4 .   ? -10.549 -11.506 10.693 1.00 60.87  ? 1230 OLA   A C5  1 
HETATM 3477 C  C6  . OLA   EA 4 .   ? -9.446  -10.549 10.308 1.00 70.09  ? 1230 OLA   A C6  1 
HETATM 3478 C  C7  . OLA   EA 4 .   ? -8.688  -9.843  11.351 1.00 64.79  ? 1230 OLA   A C7  1 
HETATM 3479 C  C8  . OLA   EA 4 .   ? -9.392  -9.325  12.582 1.00 64.52  ? 1230 OLA   A C8  1 
HETATM 3480 C  C9  . OLA   EA 4 .   ? -8.398  -8.575  13.460 1.00 53.18  ? 1230 OLA   A C9  1 
HETATM 3481 NA NA  . NA    FA 5 .   ? -23.331 -9.101  16.225 1.00 43.00  ? 1231 NA    A NA  1 
HETATM 3482 O  O   . HOH   GA 6 .   ? -5.161  17.676  12.845 1.00 54.16  ? 1301 HOH   A O   1 
HETATM 3483 O  O   . HOH   GA 6 .   ? -25.402 14.380  7.180  1.00 55.14  ? 1302 HOH   A O   1 
HETATM 3484 O  O   . HOH   GA 6 .   ? -28.812 9.515   35.073 1.00 46.12  ? 1303 HOH   A O   1 
HETATM 3485 O  O   . HOH   GA 6 .   ? -31.375 14.542  7.995  1.00 66.02  ? 1304 HOH   A O   1 
HETATM 3486 O  O   . HOH   GA 6 .   ? 9.304   -74.931 25.147 1.00 40.92  ? 1305 HOH   A O   1 
HETATM 3487 O  O   . HOH   GA 6 .   ? -12.781 17.592  11.513 1.00 46.14  ? 1306 HOH   A O   1 
HETATM 3488 O  O   . HOH   GA 6 .   ? -33.757 16.538  29.769 1.00 56.91  ? 1307 HOH   A O   1 
HETATM 3489 O  O   . HOH   GA 6 .   ? -22.060 -24.581 30.592 1.00 59.84  ? 1308 HOH   A O   1 
HETATM 3490 O  O   . HOH   GA 6 .   ? -22.024 -6.583  15.228 1.00 33.55  ? 1309 HOH   A O   1 
HETATM 3491 O  O   . HOH   GA 6 .   ? -23.992 -23.742 -1.985 1.00 61.14  ? 1310 HOH   A O   1 
HETATM 3492 O  O   . HOH   GA 6 .   ? -30.745 8.211   32.251 1.00 48.21  ? 1311 HOH   A O   1 
HETATM 3493 O  O   . HOH   GA 6 .   ? -24.759 12.949  11.834 1.00 43.95  ? 1312 HOH   A O   1 
HETATM 3494 O  O   . HOH   GA 6 .   ? -16.322 -17.010 18.874 1.00 30.48  ? 1313 HOH   A O   1 
HETATM 3495 O  O   . HOH   GA 6 .   ? -0.874  -62.611 19.514 1.00 47.58  ? 1314 HOH   A O   1 
HETATM 3496 O  O   . HOH   GA 6 .   ? -23.153 -28.147 21.468 1.00 48.46  ? 1315 HOH   A O   1 
HETATM 3497 O  O   . HOH   GA 6 .   ? -18.217 12.849  23.448 1.00 35.34  ? 1316 HOH   A O   1 
HETATM 3498 O  O   . HOH   GA 6 .   ? -25.140 -7.270  17.720 1.00 53.52  ? 1317 HOH   A O   1 
HETATM 3499 O  O   . HOH   GA 6 .   ? -15.251 10.048  17.674 1.00 22.85  ? 1318 HOH   A O   1 
HETATM 3500 O  O   . HOH   GA 6 .   ? -4.570  -37.715 20.725 1.00 54.46  ? 1319 HOH   A O   1 
HETATM 3501 O  O   . HOH   GA 6 .   ? -23.604 15.109  33.108 1.00 41.65  ? 1320 HOH   A O   1 
HETATM 3502 O  O   . HOH   GA 6 .   ? -19.280 -35.578 26.653 1.00 55.01  ? 1321 HOH   A O   1 
HETATM 3503 O  O   . HOH   GA 6 .   ? 9.297   -70.360 19.866 1.00 59.79  ? 1322 HOH   A O   1 
HETATM 3504 O  O   . HOH   GA 6 .   ? -18.835 -11.486 12.966 1.00 28.72  ? 1323 HOH   A O   1 
HETATM 3505 O  O   . HOH   GA 6 .   ? -16.451 15.191  20.233 1.00 53.83  ? 1324 HOH   A O   1 
HETATM 3506 O  O   . HOH   GA 6 .   ? -26.342 18.377  21.989 1.00 26.84  ? 1325 HOH   A O   1 
HETATM 3507 O  O   . HOH   GA 6 .   ? -28.576 2.575   19.644 1.00 32.35  ? 1326 HOH   A O   1 
HETATM 3508 O  O   . HOH   GA 6 .   ? -23.898 -11.147 11.187 1.00 40.44  ? 1327 HOH   A O   1 
HETATM 3509 O  O   . HOH   GA 6 .   ? -26.250 -12.156 25.538 1.00 34.64  ? 1328 HOH   A O   1 
HETATM 3510 O  O   . HOH   GA 6 .   ? -40.029 15.278  23.117 1.00 51.86  ? 1329 HOH   A O   1 
HETATM 3511 O  O   . HOH   GA 6 .   ? -24.561 16.629  2.102  1.00 50.61  ? 1330 HOH   A O   1 
HETATM 3512 O  O   . HOH   GA 6 .   ? -27.707 3.016   16.953 1.00 23.23  ? 1331 HOH   A O   1 
HETATM 3513 O  O   . HOH   GA 6 .   ? -23.452 -4.922  13.989 1.00 24.03  ? 1332 HOH   A O   1 
HETATM 3514 O  O   . HOH   GA 6 .   ? -1.806  18.561  15.536 1.00 70.38  ? 1333 HOH   A O   1 
HETATM 3515 O  O   . HOH   GA 6 .   ? -25.772 7.710   13.291 1.00 24.34  ? 1334 HOH   A O   1 
HETATM 3516 O  O   . HOH   GA 6 .   ? -25.995 -12.242 21.467 1.00 27.19  ? 1335 HOH   A O   1 
HETATM 3517 O  O   . HOH   GA 6 .   ? -25.768 18.758  24.727 1.00 32.26  ? 1336 HOH   A O   1 
HETATM 3518 O  O   . HOH   GA 6 .   ? -16.684 16.605  8.897  1.00 39.67  ? 1337 HOH   A O   1 
HETATM 3519 O  O   . HOH   GA 6 .   ? -14.580 -27.035 17.331 1.00 38.42  ? 1338 HOH   A O   1 
HETATM 3520 O  O   . HOH   GA 6 .   ? -25.186 2.397   15.867 1.00 23.38  ? 1339 HOH   A O   1 
HETATM 3521 O  O   . HOH   GA 6 .   ? -21.043 -2.668  24.389 1.00 27.06  ? 1340 HOH   A O   1 
HETATM 3522 O  O   . HOH   GA 6 .   ? -16.323 0.598   12.495 1.00 23.45  ? 1341 HOH   A O   1 
HETATM 3523 O  O   . HOH   GA 6 .   ? -27.719 20.669  22.355 1.00 31.45  ? 1342 HOH   A O   1 
HETATM 3524 O  O   . HOH   GA 6 .   ? -15.101 3.497   21.635 1.00 20.48  ? 1343 HOH   A O   1 
HETATM 3525 O  O   . HOH   GA 6 .   ? -19.473 -1.797  22.114 1.00 26.06  ? 1344 HOH   A O   1 
HETATM 3526 O  O   . HOH   GA 6 .   ? -40.159 -15.780 9.088  1.00 71.51  ? 1345 HOH   A O   1 
HETATM 3527 O  O   . HOH   GA 6 .   ? -17.880 -17.506 16.820 1.00 32.09  ? 1346 HOH   A O   1 
HETATM 3528 O  O   . HOH   GA 6 .   ? -25.723 -14.611 24.740 1.00 35.86  ? 1347 HOH   A O   1 
HETATM 3529 O  O   . HOH   GA 6 .   ? -31.383 10.197  38.819 1.00 45.90  ? 1348 HOH   A O   1 
HETATM 3530 O  O   . HOH   GA 6 .   ? 6.189   -75.876 23.859 1.00 34.71  ? 1349 HOH   A O   1 
HETATM 3531 O  O   . HOH   GA 6 .   ? -25.328 -13.626 13.468 1.00 28.95  ? 1350 HOH   A O   1 
HETATM 3532 O  O   . HOH   GA 6 .   ? -25.238 -15.946 14.510 1.00 34.66  ? 1351 HOH   A O   1 
HETATM 3533 O  O   . HOH   GA 6 .   ? -12.840 -33.535 21.210 1.00 51.23  ? 1352 HOH   A O   1 
HETATM 3534 O  O   . HOH   GA 6 .   ? -22.154 13.067  17.723 1.00 27.49  ? 1353 HOH   A O   1 
HETATM 3535 O  O   . HOH   GA 6 .   ? -13.988 -28.173 19.532 1.00 48.26  ? 1354 HOH   A O   1 
HETATM 3536 O  O   . HOH   GA 6 .   ? -27.908 5.561   17.956 1.00 41.67  ? 1355 HOH   A O   1 
HETATM 3537 O  O   . HOH   GA 6 .   ? -21.140 -11.116 15.030 1.00 42.59  ? 1356 HOH   A O   1 
HETATM 3538 O  O   . HOH   GA 6 .   ? -18.853 9.836   22.677 1.00 36.99  ? 1357 HOH   A O   1 
HETATM 3539 O  O   . HOH   GA 6 .   ? -27.393 -11.557 6.683  1.00 42.66  ? 1358 HOH   A O   1 
HETATM 3540 O  O   . HOH   GA 6 .   ? -11.307 12.006  15.635 1.00 23.78  ? 1359 HOH   A O   1 
HETATM 3541 O  O   . HOH   GA 6 .   ? 3.082   -72.845 23.926 1.00 60.09  ? 1360 HOH   A O   1 
HETATM 3542 O  O   . HOH   GA 6 .   ? -10.101 15.271  19.226 1.00 50.44  ? 1361 HOH   A O   1 
HETATM 3543 O  O   . HOH   GA 6 .   ? -22.779 1.334   15.501 1.00 41.75  ? 1362 HOH   A O   1 
HETATM 3544 O  O   . HOH   GA 6 .   ? -18.250 -2.913  19.984 1.00 23.88  ? 1363 HOH   A O   1 
HETATM 3545 O  O   . HOH   GA 6 .   ? -18.408 15.853  18.179 1.00 52.07  ? 1364 HOH   A O   1 
HETATM 3546 O  O   . HOH   GA 6 .   ? -34.072 14.023  30.037 1.00 43.86  ? 1365 HOH   A O   1 
HETATM 3547 O  O   . HOH   GA 6 .   ? -12.067 19.232  14.698 1.00 49.38  ? 1366 HOH   A O   1 
HETATM 3548 O  O   . HOH   GA 6 .   ? -2.306  13.450  21.920 1.00 39.08  ? 1367 HOH   A O   1 
HETATM 3549 O  O   . HOH   GA 6 .   ? -24.607 11.605  16.351 1.00 29.85  ? 1368 HOH   A O   1 
HETATM 3550 O  O   . HOH   GA 6 .   ? -5.542  -31.413 24.557 1.00 54.36  ? 1369 HOH   A O   1 
HETATM 3551 O  O   . HOH   GA 6 .   ? -24.723 13.032  35.621 1.00 49.68  ? 1370 HOH   A O   1 
HETATM 3552 O  O   . HOH   GA 6 .   ? -25.698 16.911  26.597 1.00 33.57  ? 1371 HOH   A O   1 
HETATM 3553 O  O   . HOH   GA 6 .   ? -39.436 16.632  25.355 1.00 54.80  ? 1372 HOH   A O   1 
HETATM 3554 O  O   . HOH   GA 6 .   ? -24.239 9.161   15.252 1.00 27.72  ? 1373 HOH   A O   1 
HETATM 3555 O  O   . HOH   GA 6 .   ? -25.076 -29.559 22.682 1.00 50.67  ? 1374 HOH   A O   1 
HETATM 3556 O  O   . HOH   GA 6 .   ? -26.895 13.834  34.251 1.00 49.70  ? 1375 HOH   A O   1 
HETATM 3557 O  O   . HOH   GA 6 .   ? -4.385  -25.989 25.046 1.00 48.28  ? 1376 HOH   A O   1 
HETATM 3558 O  O   . HOH   GA 6 .   ? -16.298 16.018  12.135 1.00 48.53  ? 1377 HOH   A O   1 
HETATM 3559 O  O   . HOH   GA 6 .   ? -3.499  16.115  21.580 1.00 41.94  ? 1378 HOH   A O   1 
HETATM 3560 O  O   . HOH   GA 6 .   ? -17.864 15.207  5.644  1.00 45.46  ? 1379 HOH   A O   1 
HETATM 3561 O  O   . HOH   GA 6 .   ? -27.949 11.793  34.648 1.00 49.67  ? 1380 HOH   A O   1 
HETATM 3562 O  O   . HOH   GA 6 .   ? -17.275 12.054  32.590 1.00 44.00  ? 1381 HOH   A O   1 
HETATM 3563 O  O   . HOH   GA 6 .   ? -29.940 17.954  29.256 1.00 47.51  ? 1382 HOH   A O   1 
HETATM 3564 O  O   . HOH   GA 6 .   ? -23.147 -15.754 26.460 1.00 43.81  ? 1383 HOH   A O   1 
HETATM 3565 O  O   . HOH   GA 6 .   ? -29.795 15.430  33.673 1.00 46.77  ? 1384 HOH   A O   1 
HETATM 3566 O  O   . HOH   GA 6 .   ? -17.309 13.531  28.912 1.00 46.55  ? 1385 HOH   A O   1 
HETATM 3567 O  O   . HOH   GA 6 .   ? -15.185 12.274  28.270 1.00 28.24  ? 1386 HOH   A O   1 
HETATM 3568 O  O   . HOH   GA 6 .   ? -17.338 13.540  25.989 1.00 35.28  ? 1387 HOH   A O   1 
HETATM 3569 O  O   . HOH   GA 6 .   ? -2.621  16.635  24.485 1.00 60.07  ? 1388 HOH   A O   1 
HETATM 3570 O  O   . HOH   GA 6 .   ? -9.180  13.440  16.665 1.00 30.56  ? 1389 HOH   A O   1 
HETATM 3571 O  O   . HOH   GA 6 .   ? -29.744 16.186  7.819  1.00 60.42  ? 1390 HOH   A O   1 
HETATM 3572 O  O   . HOH   GA 6 .   ? -19.547 12.415  32.870 1.00 47.99  ? 1391 HOH   A O   1 
HETATM 3573 O  O   . HOH   GA 6 .   ? -11.376 10.775  32.015 1.00 53.48  ? 1392 HOH   A O   1 
HETATM 3574 O  O   . HOH   GA 6 .   ? -20.848 12.418  34.745 1.00 53.14  ? 1393 HOH   A O   1 
HETATM 3575 O  O   . HOH   GA 6 .   ? -21.175 15.839  17.836 1.00 46.38  ? 1394 HOH   A O   1 
HETATM 3576 O  O   . HOH   GA 6 .   ? 3.767   -75.479 22.297 1.00 53.14  ? 1395 HOH   A O   1 
HETATM 3577 O  O   . HOH   GA 6 .   ? -14.816 17.070  10.717 1.00 64.83  ? 1396 HOH   A O   1 
HETATM 3578 O  O   . HOH   GA 6 .   ? -11.728 16.722  18.331 1.00 53.33  ? 1397 HOH   A O   1 
HETATM 3579 O  O   . HOH   GA 6 .   ? -31.341 16.415  31.452 1.00 50.76  ? 1398 HOH   A O   1 
HETATM 3580 O  O   . HOH   GA 6 .   ? -16.672 17.207  15.815 1.00 54.79  ? 1399 HOH   A O   1 
HETATM 3581 O  O   . HOH   GA 6 .   ? -20.664 -24.535 32.293 1.00 54.77  ? 1400 HOH   A O   1 
HETATM 3582 O  O   . HOH   GA 6 .   ? 5.709   -75.735 26.296 1.00 42.60  ? 1401 HOH   A O   1 
HETATM 3583 O  O   . HOH   GA 6 .   ? -28.421 15.119  35.389 1.00 69.53  ? 1402 HOH   A O   1 
# 
