data_8RW7
# 
_entry.id   8RW7 
# 
_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   8RW7         pdb_00008rw7 10.2210/pdb8rw7/pdb 
WWPDB D_1292136154 ?            ?                   
# 
_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                        8RW7 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           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 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Glover, H.'    1 0000-0001-6558-8878 
'Standfuss, J.' 2 0000-0001-8825-386X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                10837 
_citation.page_last                 10837 
_citation.title                     
'Photoswitch dissociation from a G protein-coupled receptor resolved by time-resolved serial crystallography.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-55109-w 
_citation.pdbx_database_id_PubMed   39738009 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Glover, H.'          1  0000-0001-6558-8878 
primary 'Sassmannshausen, T.' 2  ?                   
primary 'Bertrand, Q.'        3  0000-0003-3476-1775 
primary 'Trabuco, M.'         4  0000-0001-9234-8685 
primary 'Slavov, C.'          5  0000-0001-9441-0243 
primary 'Bacchin, A.'         6  ?                   
primary 'Andres, F.'          7  ?                   
primary 'Kondo, Y.'           8  0000-0003-2131-575X 
primary 'Stipp, R.'           9  ?                   
primary 'Wranik, M.'          10 ?                   
primary 'Khusainov, G.'       11 ?                   
primary 'Carrillo, M.'        12 0000-0002-0744-4486 
primary 'Kekilli, D.'         13 ?                   
primary 'Nan, J.'             14 ?                   
primary 'Gonzalez, A.'        15 0000-0001-8858-399X 
primary 'Cheng, R.'           16 0000-0001-7564-1230 
primary 'Neidhart, W.'        17 ?                   
primary 'Weinert, T.'         18 0000-0002-0339-3722 
primary 'Leonarski, F.'       19 ?                   
primary 'Dworkowski, F.'      20 0000-0001-5004-8684 
primary 'Kepa, M.'            21 0000-0002-4045-3990 
primary 'Wachtveitl, J.'      22 0000-0002-8496-8240 
primary 'Hennig, M.'          23 0000-0002-1839-2351 
primary 'Standfuss, J.'       24 0000-0001-8825-386X 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Adenosine receptor A2a,Soluble cytochrome b562'                               49829.039 1   ? ? ? 
;A2A-StaR2-bRIL562 construct (A2A with bRIL insertion), with A277S revert mutation.,A2A-StaR2-bRIL562 construct (A2A with bRIL insertion), with A277S revert mutation.,A2A-StaR2-bRIL562 construct (A2A with bRIL insertion), with A277S revert mutation.
;
2 non-polymer syn '8-[(~{E})-2-(3,4-dimethoxyphenyl)ethenyl]-1,3-diethyl-7~{H}-purine-2,6-dione' 370.402   1   ? ? ? ? 
3 non-polymer syn CHOLESTEROL                                                                    386.654   3   ? ? ? ? 
4 non-polymer syn 'OLEIC ACID'                                                                   282.461   22  ? ? ? ? 
5 non-polymer syn '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate'                               356.540   3   ? ? ? ? 
6 non-polymer syn '(2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate'                               356.540   1   ? ? ? ? 
7 non-polymer syn 'SODIUM ION'                                                                   22.990    1   ? ? ? ? 
8 water       nat water                                                                          18.015    110 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytochrome b-562' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKTIIALSYIFCLVFADYKDDDDGAPPIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADILV
GVLAIPFAITISTGFCAACHGCLFIACFVLVLAQSSIFSLLAIAIDRYIAIAIPLRYNGLVTGTRAAGIIAICWVLSFAI
GLTPMLGWNNCGQPKEGKAHSQGCGEGQVACLFEDVVPMNYMVYFNFFACVLVPLLLMLGVYLRIFAAARRQLADLEDNW
ETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEA
QAAAEQLKTTRNAYIQKYLERARSTLQKEVHAAKSAAIIAGLFALCWLPLHIINCFTFFCPDCSHAPLWLMYLAIVLSHT
NSVVNPFIYAYRIREFRQTFRKIIRSHVLRQQEPFKAAAHHHHHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKTIIALSYIFCLVFADYKDDDDGAPPIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADILV
GVLAIPFAITISTGFCAACHGCLFIACFVLVLAQSSIFSLLAIAIDRYIAIAIPLRYNGLVTGTRAAGIIAICWVLSFAI
GLTPMLGWNNCGQPKEGKAHSQGCGEGQVACLFEDVVPMNYMVYFNFFACVLVPLLLMLGVYLRIFAAARRQLADLEDNW
ETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEA
QAAAEQLKTTRNAYIQKYLERARSTLQKEVHAAKSAAIIAGLFALCWLPLHIINCFTFFCPDCSHAPLWLMYLAIVLSHT
NSVVNPFIYAYRIREFRQTFRKIIRSHVLRQQEPFKAAAHHHHHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '8-[(~{E})-2-(3,4-dimethoxyphenyl)ethenyl]-1,3-diethyl-7~{H}-purine-2,6-dione' A1H3J 
3 CHOLESTEROL                                                                    CLR   
4 'OLEIC ACID'                                                                   OLA   
5 '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate'                               OLC   
6 '(2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate'                               OLB   
7 'SODIUM ION'                                                                   NA    
8 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 
A1H3J non-polymer         . '8-[(~{E})-2-(3,4-dimethoxyphenyl)ethenyl]-1,3-diethyl-7~{H}-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 
OLB   non-polymer         . '(2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate'                               ?                   
'C21 H40 O4'     356.540 
OLC   non-polymer         . '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate'                               1-Oleoyl-R-glycerol 
'C21 H40 O4'     356.540 
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 1058 MET MET A . n 
A 1 292 LYS 292 1059 1059 LYS LYS A . n 
A 1 293 ASP 293 1060 1060 ASP ASP A . n 
A 1 294 PHE 294 1061 1061 PHE PHE A . n 
A 1 295 ARG 295 1062 1062 ARG ARG A . n 
A 1 296 HIS 296 1063 1063 HIS HIS A . n 
A 1 297 GLY 297 1064 1064 GLY GLY A . n 
A 1 298 PHE 298 1065 1065 PHE PHE A . n 
A 1 299 ASP 299 1066 1066 ASP ASP A . n 
A 1 300 ILE 300 1067 1067 ILE ILE A . n 
A 1 301 LEU 301 1068 1068 LEU LEU A . n 
A 1 302 VAL 302 1069 1069 VAL VAL A . n 
A 1 303 GLY 303 1070 1070 GLY GLY A . n 
A 1 304 GLN 304 1071 1071 GLN GLN A . n 
A 1 305 ILE 305 1072 1072 ILE ILE A . n 
A 1 306 ASP 306 1073 1073 ASP ASP A . n 
A 1 307 ASP 307 1074 1074 ASP ASP A . n 
A 1 308 ALA 308 1075 1075 ALA ALA A . n 
A 1 309 LEU 309 1076 1076 LEU LEU A . n 
A 1 310 LYS 310 1077 1077 LYS LYS A . n 
A 1 311 LEU 311 1078 1078 LEU LEU A . n 
A 1 312 ALA 312 1079 1079 ALA ALA A . n 
A 1 313 ASN 313 1080 1080 ASN ASN A . n 
A 1 314 GLU 314 1081 1081 GLU GLU A . n 
A 1 315 GLY 315 1082 1082 GLY GLY A . n 
A 1 316 LYS 316 1083 1083 LYS LYS A . n 
A 1 317 VAL 317 1084 1084 VAL VAL A . n 
A 1 318 LYS 318 1085 1085 LYS LYS A . n 
A 1 319 GLU 319 1086 1086 GLU GLU A . n 
A 1 320 ALA 320 1087 1087 ALA ALA A . n 
A 1 321 GLN 321 1088 1088 GLN GLN A . n 
A 1 322 ALA 322 1089 1089 ALA ALA A . n 
A 1 323 ALA 323 1090 1090 ALA ALA A . n 
A 1 324 ALA 324 1091 1091 ALA ALA A . n 
A 1 325 GLU 325 1092 1092 GLU GLU A . n 
A 1 326 GLN 326 1093 1093 GLN GLN A . n 
A 1 327 LEU 327 1094 1094 LEU LEU A . n 
A 1 328 LYS 328 1095 1095 LYS LYS A . n 
A 1 329 THR 329 1096 1096 THR THR A . n 
A 1 330 THR 330 1097 1097 THR THR A . n 
A 1 331 ARG 331 1098 1098 ARG ARG A . n 
A 1 332 ASN 332 1099 1099 ASN ASN A . n 
A 1 333 ALA 333 1100 1100 ALA ALA A . n 
A 1 334 TYR 334 1101 1101 TYR TYR A . n 
A 1 335 ILE 335 1102 1102 ILE ILE A . n 
A 1 336 GLN 336 1103 1103 GLN GLN A . n 
A 1 337 LYS 337 1104 1104 LYS LYS A . n 
A 1 338 TYR 338 1105 1105 TYR TYR A . n 
A 1 339 LEU 339 1106 1106 LEU LEU A . n 
A 1 340 GLU 340 219  219  GLU GLU A . n 
A 1 341 ARG 341 220  220  ARG ARG A . n 
A 1 342 ALA 342 221  221  ALA ALA A . n 
A 1 343 ARG 343 222  222  ARG ARG A . n 
A 1 344 SER 344 223  223  SER SER A . n 
A 1 345 THR 345 224  224  THR THR A . n 
A 1 346 LEU 346 225  225  LEU LEU A . n 
A 1 347 GLN 347 226  226  GLN GLN A . n 
A 1 348 LYS 348 227  227  LYS LYS A . n 
A 1 349 GLU 349 228  228  GLU GLU A . n 
A 1 350 VAL 350 229  229  VAL VAL A . n 
A 1 351 HIS 351 230  230  HIS HIS A . n 
A 1 352 ALA 352 231  231  ALA ALA A . n 
A 1 353 ALA 353 232  232  ALA ALA A . n 
A 1 354 LYS 354 233  233  LYS LYS A . n 
A 1 355 SER 355 234  234  SER SER A . n 
A 1 356 ALA 356 235  235  ALA ALA A . n 
A 1 357 ALA 357 236  236  ALA ALA A . n 
A 1 358 ILE 358 237  237  ILE ILE A . n 
A 1 359 ILE 359 238  238  ILE ILE A . n 
A 1 360 ALA 360 239  239  ALA ALA A . n 
A 1 361 GLY 361 240  240  GLY GLY A . n 
A 1 362 LEU 362 241  241  LEU LEU A . n 
A 1 363 PHE 363 242  242  PHE PHE A . n 
A 1 364 ALA 364 243  243  ALA ALA A . n 
A 1 365 LEU 365 244  244  LEU LEU A . n 
A 1 366 CYS 366 245  245  CYS CYS A . n 
A 1 367 TRP 367 246  246  TRP TRP A . n 
A 1 368 LEU 368 247  247  LEU LEU A . n 
A 1 369 PRO 369 248  248  PRO PRO A . n 
A 1 370 LEU 370 249  249  LEU LEU A . n 
A 1 371 HIS 371 250  250  HIS HIS A . n 
A 1 372 ILE 372 251  251  ILE ILE A . n 
A 1 373 ILE 373 252  252  ILE ILE A . n 
A 1 374 ASN 374 253  253  ASN ASN A . n 
A 1 375 CYS 375 254  254  CYS CYS A . n 
A 1 376 PHE 376 255  255  PHE PHE A . n 
A 1 377 THR 377 256  256  THR THR A . n 
A 1 378 PHE 378 257  257  PHE PHE A . n 
A 1 379 PHE 379 258  258  PHE PHE A . n 
A 1 380 CYS 380 259  259  CYS CYS A . n 
A 1 381 PRO 381 260  260  PRO PRO A . n 
A 1 382 ASP 382 261  261  ASP ASP A . n 
A 1 383 CYS 383 262  262  CYS CYS A . n 
A 1 384 SER 384 263  263  SER SER A . n 
A 1 385 HIS 385 264  264  HIS HIS A . n 
A 1 386 ALA 386 265  265  ALA ALA A . n 
A 1 387 PRO 387 266  266  PRO PRO A . n 
A 1 388 LEU 388 267  267  LEU LEU A . n 
A 1 389 TRP 389 268  268  TRP TRP A . n 
A 1 390 LEU 390 269  269  LEU LEU A . n 
A 1 391 MET 391 270  270  MET MET A . n 
A 1 392 TYR 392 271  271  TYR TYR A . n 
A 1 393 LEU 393 272  272  LEU LEU A . n 
A 1 394 ALA 394 273  273  ALA ALA A . n 
A 1 395 ILE 395 274  274  ILE ILE A . n 
A 1 396 VAL 396 275  275  VAL VAL A . n 
A 1 397 LEU 397 276  276  LEU LEU A . n 
A 1 398 SER 398 277  277  SER SER A . n 
A 1 399 HIS 399 278  278  HIS HIS A . n 
A 1 400 THR 400 279  279  THR THR A . n 
A 1 401 ASN 401 280  280  ASN ASN A . n 
A 1 402 SER 402 281  281  SER SER A . n 
A 1 403 VAL 403 282  282  VAL VAL A . n 
A 1 404 VAL 404 283  283  VAL VAL A . n 
A 1 405 ASN 405 284  284  ASN ASN A . n 
A 1 406 PRO 406 285  285  PRO PRO A . n 
A 1 407 PHE 407 286  286  PHE PHE A . n 
A 1 408 ILE 408 287  287  ILE ILE A . n 
A 1 409 TYR 409 288  288  TYR TYR A . n 
A 1 410 ALA 410 289  289  ALA ALA A . n 
A 1 411 TYR 411 290  290  TYR TYR A . n 
A 1 412 ARG 412 291  291  ARG ARG A . n 
A 1 413 ILE 413 292  292  ILE ILE A . n 
A 1 414 ARG 414 293  293  ARG ARG A . n 
A 1 415 GLU 415 294  294  GLU GLU A . n 
A 1 416 PHE 416 295  295  PHE PHE A . n 
A 1 417 ARG 417 296  296  ARG ARG A . n 
A 1 418 GLN 418 297  297  GLN GLN A . n 
A 1 419 THR 419 298  298  THR THR A . n 
A 1 420 PHE 420 299  299  PHE PHE A . n 
A 1 421 ARG 421 300  300  ARG ARG A . n 
A 1 422 LYS 422 301  301  LYS LYS A . n 
A 1 423 ILE 423 302  302  ILE ILE A . n 
A 1 424 ILE 424 303  303  ILE ILE A . n 
A 1 425 ARG 425 304  304  ARG ARG A . n 
A 1 426 SER 426 305  305  SER SER A . n 
A 1 427 HIS 427 306  306  HIS HIS A . n 
A 1 428 VAL 428 307  307  VAL VAL 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        A1H3J 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H3J 
_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 A1H3J 1   1201 1201 A1H3J AC3 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  5 OLC   1   1214 1214 OLC   OLC A . 
P  6 OLB   1   1215 1215 OLB   OLB A . 
Q  5 OLC   1   1216 1216 OLC   OLC 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 5 OLC   1   1228 1228 OLC   OLC A . 
DA 4 OLA   1   1229 1229 OLA   OLA A . 
EA 4 OLA   1   1230 1230 OLA   OLA A . 
FA 7 NA    1   1231 1    NA    NA  A . 
GA 8 HOH   1   1301 112  HOH   HOH A . 
GA 8 HOH   2   1302 75   HOH   HOH A . 
GA 8 HOH   3   1303 105  HOH   HOH A . 
GA 8 HOH   4   1304 29   HOH   HOH A . 
GA 8 HOH   5   1305 37   HOH   HOH A . 
GA 8 HOH   6   1306 58   HOH   HOH A . 
GA 8 HOH   7   1307 45   HOH   HOH A . 
GA 8 HOH   8   1308 55   HOH   HOH A . 
GA 8 HOH   9   1309 86   HOH   HOH A . 
GA 8 HOH   10  1310 56   HOH   HOH A . 
GA 8 HOH   11  1311 23   HOH   HOH A . 
GA 8 HOH   12  1312 5    HOH   HOH A . 
GA 8 HOH   13  1313 17   HOH   HOH A . 
GA 8 HOH   14  1314 43   HOH   HOH A . 
GA 8 HOH   15  1315 85   HOH   HOH A . 
GA 8 HOH   16  1316 20   HOH   HOH A . 
GA 8 HOH   17  1317 16   HOH   HOH A . 
GA 8 HOH   18  1318 111  HOH   HOH A . 
GA 8 HOH   19  1319 12   HOH   HOH A . 
GA 8 HOH   20  1320 34   HOH   HOH A . 
GA 8 HOH   21  1321 40   HOH   HOH A . 
GA 8 HOH   22  1322 14   HOH   HOH A . 
GA 8 HOH   23  1323 107  HOH   HOH A . 
GA 8 HOH   24  1324 92   HOH   HOH A . 
GA 8 HOH   25  1325 99   HOH   HOH A . 
GA 8 HOH   26  1326 97   HOH   HOH A . 
GA 8 HOH   27  1327 36   HOH   HOH A . 
GA 8 HOH   28  1328 44   HOH   HOH A . 
GA 8 HOH   29  1329 2    HOH   HOH A . 
GA 8 HOH   30  1330 7    HOH   HOH A . 
GA 8 HOH   31  1331 50   HOH   HOH A . 
GA 8 HOH   32  1332 100  HOH   HOH A . 
GA 8 HOH   33  1333 11   HOH   HOH A . 
GA 8 HOH   34  1334 1    HOH   HOH A . 
GA 8 HOH   35  1335 81   HOH   HOH A . 
GA 8 HOH   36  1336 15   HOH   HOH A . 
GA 8 HOH   37  1337 39   HOH   HOH A . 
GA 8 HOH   38  1338 27   HOH   HOH A . 
GA 8 HOH   39  1339 19   HOH   HOH A . 
GA 8 HOH   40  1340 10   HOH   HOH A . 
GA 8 HOH   41  1341 53   HOH   HOH A . 
GA 8 HOH   42  1342 95   HOH   HOH A . 
GA 8 HOH   43  1343 80   HOH   HOH A . 
GA 8 HOH   44  1344 33   HOH   HOH A . 
GA 8 HOH   45  1345 67   HOH   HOH A . 
GA 8 HOH   46  1346 101  HOH   HOH A . 
GA 8 HOH   47  1347 41   HOH   HOH A . 
GA 8 HOH   48  1348 22   HOH   HOH A . 
GA 8 HOH   49  1349 72   HOH   HOH A . 
GA 8 HOH   50  1350 32   HOH   HOH A . 
GA 8 HOH   51  1351 78   HOH   HOH A . 
GA 8 HOH   52  1352 26   HOH   HOH A . 
GA 8 HOH   53  1353 104  HOH   HOH A . 
GA 8 HOH   54  1354 51   HOH   HOH A . 
GA 8 HOH   55  1355 4    HOH   HOH A . 
GA 8 HOH   56  1356 77   HOH   HOH A . 
GA 8 HOH   57  1357 64   HOH   HOH A . 
GA 8 HOH   58  1358 13   HOH   HOH A . 
GA 8 HOH   59  1359 90   HOH   HOH A . 
GA 8 HOH   60  1360 35   HOH   HOH A . 
GA 8 HOH   61  1361 3    HOH   HOH A . 
GA 8 HOH   62  1362 18   HOH   HOH A . 
GA 8 HOH   63  1363 65   HOH   HOH A . 
GA 8 HOH   64  1364 89   HOH   HOH A . 
GA 8 HOH   65  1365 47   HOH   HOH A . 
GA 8 HOH   66  1366 25   HOH   HOH A . 
GA 8 HOH   67  1367 96   HOH   HOH A . 
GA 8 HOH   68  1368 84   HOH   HOH A . 
GA 8 HOH   69  1369 52   HOH   HOH A . 
GA 8 HOH   70  1370 9    HOH   HOH A . 
GA 8 HOH   71  1371 57   HOH   HOH A . 
GA 8 HOH   72  1372 69   HOH   HOH A . 
GA 8 HOH   73  1373 93   HOH   HOH A . 
GA 8 HOH   74  1374 38   HOH   HOH A . 
GA 8 HOH   75  1375 48   HOH   HOH A . 
GA 8 HOH   76  1376 49   HOH   HOH A . 
GA 8 HOH   77  1377 6    HOH   HOH A . 
GA 8 HOH   78  1378 30   HOH   HOH A . 
GA 8 HOH   79  1379 79   HOH   HOH A . 
GA 8 HOH   80  1380 46   HOH   HOH A . 
GA 8 HOH   81  1381 73   HOH   HOH A . 
GA 8 HOH   82  1382 109  HOH   HOH A . 
GA 8 HOH   83  1383 98   HOH   HOH A . 
GA 8 HOH   84  1384 62   HOH   HOH A . 
GA 8 HOH   85  1385 21   HOH   HOH A . 
GA 8 HOH   86  1386 110  HOH   HOH A . 
GA 8 HOH   87  1387 74   HOH   HOH A . 
GA 8 HOH   88  1388 66   HOH   HOH A . 
GA 8 HOH   89  1389 83   HOH   HOH A . 
GA 8 HOH   90  1390 54   HOH   HOH A . 
GA 8 HOH   91  1391 8    HOH   HOH A . 
GA 8 HOH   92  1392 71   HOH   HOH A . 
GA 8 HOH   93  1393 68   HOH   HOH A . 
GA 8 HOH   94  1394 31   HOH   HOH A . 
GA 8 HOH   95  1395 106  HOH   HOH A . 
GA 8 HOH   96  1396 108  HOH   HOH A . 
GA 8 HOH   97  1397 60   HOH   HOH A . 
GA 8 HOH   98  1398 87   HOH   HOH A . 
GA 8 HOH   99  1399 103  HOH   HOH A . 
GA 8 HOH   100 1400 88   HOH   HOH A . 
GA 8 HOH   101 1401 28   HOH   HOH A . 
GA 8 HOH   102 1402 102  HOH   HOH A . 
GA 8 HOH   103 1403 42   HOH   HOH A . 
GA 8 HOH   104 1404 70   HOH   HOH A . 
GA 8 HOH   105 1405 91   HOH   HOH A . 
GA 8 HOH   106 1406 59   HOH   HOH A . 
GA 8 HOH   107 1407 61   HOH   HOH A . 
GA 8 HOH   108 1408 24   HOH   HOH A . 
GA 8 HOH   109 1409 63   HOH   HOH A . 
GA 8 HOH   110 1410 82   HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ARG 111  ? CD  ? A  ARG 136 CD  
2   1 Y 1 A ARG 111  ? NE  ? A  ARG 136 NE  
3   1 Y 1 A ARG 111  ? CZ  ? A  ARG 136 CZ  
4   1 Y 1 A ARG 111  ? NH1 ? A  ARG 136 NH1 
5   1 Y 1 A ARG 111  ? NH2 ? A  ARG 136 NH2 
6   1 Y 1 A ARG 206  ? CD  ? A  ARG 231 CD  
7   1 Y 1 A ARG 206  ? NE  ? A  ARG 231 NE  
8   1 Y 1 A ARG 206  ? CZ  ? A  ARG 231 CZ  
9   1 Y 1 A ARG 206  ? NH1 ? A  ARG 231 NH1 
10  1 Y 1 A ARG 206  ? NH2 ? A  ARG 231 NH2 
11  1 Y 1 A GLU 1004 ? CG  ? A  GLU 237 CG  
12  1 Y 1 A GLU 1004 ? CD  ? A  GLU 237 CD  
13  1 Y 1 A GLU 1004 ? OE1 ? A  GLU 237 OE1 
14  1 Y 1 A GLU 1004 ? OE2 ? A  GLU 237 OE2 
15  1 Y 1 A ASP 1021 ? CG  ? A  ASP 254 CG  
16  1 Y 1 A ASP 1021 ? OD1 ? A  ASP 254 OD1 
17  1 Y 1 A ASP 1021 ? OD2 ? A  ASP 254 OD2 
18  1 Y 1 A ASP 1028 ? CG  ? A  ASP 261 CG  
19  1 Y 1 A ASP 1028 ? OD1 ? A  ASP 261 OD1 
20  1 Y 1 A ASP 1028 ? OD2 ? A  ASP 261 OD2 
21  1 Y 1 A MET 1058 ? CG  ? A  MET 291 CG  
22  1 Y 1 A MET 1058 ? SD  ? A  MET 291 SD  
23  1 Y 1 A MET 1058 ? CE  ? A  MET 291 CE  
24  1 Y 1 A LYS 1059 ? CG  ? A  LYS 292 CG  
25  1 Y 1 A LYS 1059 ? CD  ? A  LYS 292 CD  
26  1 Y 1 A LYS 1059 ? CE  ? A  LYS 292 CE  
27  1 Y 1 A LYS 1059 ? NZ  ? A  LYS 292 NZ  
28  1 Y 1 A ARG 1062 ? CG  ? A  ARG 295 CG  
29  1 Y 1 A ARG 1062 ? CD  ? A  ARG 295 CD  
30  1 Y 1 A ARG 1062 ? NE  ? A  ARG 295 NE  
31  1 Y 1 A ARG 1062 ? CZ  ? A  ARG 295 CZ  
32  1 Y 1 A ARG 1062 ? NH1 ? A  ARG 295 NH1 
33  1 Y 1 A ARG 1062 ? NH2 ? A  ARG 295 NH2 
34  1 Y 1 A LYS 1077 ? CE  ? A  LYS 310 CE  
35  1 Y 1 A LYS 1077 ? NZ  ? A  LYS 310 NZ  
36  1 Y 1 A LYS 1104 ? CD  ? A  LYS 337 CD  
37  1 Y 1 A LYS 1104 ? CE  ? A  LYS 337 CE  
38  1 Y 1 A LYS 1104 ? NZ  ? A  LYS 337 NZ  
39  1 Y 1 A TYR 1105 ? CD1 ? A  TYR 338 CD1 
40  1 Y 1 A TYR 1105 ? CD2 ? A  TYR 338 CD2 
41  1 Y 1 A TYR 1105 ? CE1 ? A  TYR 338 CE1 
42  1 Y 1 A TYR 1105 ? CE2 ? A  TYR 338 CE2 
43  1 Y 1 A TYR 1105 ? CZ  ? A  TYR 338 CZ  
44  1 Y 1 A TYR 1105 ? OH  ? A  TYR 338 OH  
45  1 Y 1 A ARG 220  ? CG  ? A  ARG 341 CG  
46  1 Y 1 A ARG 220  ? CD  ? A  ARG 341 CD  
47  1 Y 1 A ARG 220  ? NE  ? A  ARG 341 NE  
48  1 Y 1 A ARG 220  ? CZ  ? A  ARG 341 CZ  
49  1 Y 1 A ARG 220  ? NH1 ? A  ARG 341 NH1 
50  1 Y 1 A ARG 220  ? NH2 ? A  ARG 341 NH2 
51  1 N 1 A OLA 1205 ? C1  ? F  OLA 1   C1  
52  1 N 1 A OLA 1205 ? O1  ? F  OLA 1   O1  
53  1 N 1 A OLA 1205 ? O2  ? F  OLA 1   O2  
54  1 N 1 A OLA 1205 ? C2  ? F  OLA 1   C2  
55  1 N 1 A OLA 1205 ? C13 ? F  OLA 1   C13 
56  1 N 1 A OLA 1205 ? C14 ? F  OLA 1   C14 
57  1 N 1 A OLA 1205 ? C15 ? F  OLA 1   C15 
58  1 N 1 A OLA 1205 ? C16 ? F  OLA 1   C16 
59  1 N 1 A OLA 1205 ? C17 ? F  OLA 1   C17 
60  1 N 1 A OLA 1205 ? C18 ? F  OLA 1   C18 
61  1 N 1 A OLA 1206 ? C1  ? G  OLA 1   C1  
62  1 N 1 A OLA 1206 ? O1  ? G  OLA 1   O1  
63  1 N 1 A OLA 1206 ? O2  ? G  OLA 1   O2  
64  1 N 1 A OLA 1206 ? C2  ? G  OLA 1   C2  
65  1 N 1 A OLA 1206 ? C3  ? G  OLA 1   C3  
66  1 N 1 A OLA 1206 ? C4  ? G  OLA 1   C4  
67  1 N 1 A OLA 1206 ? C5  ? G  OLA 1   C5  
68  1 N 1 A OLA 1206 ? C6  ? G  OLA 1   C6  
69  1 N 1 A OLA 1206 ? C18 ? G  OLA 1   C18 
70  1 N 1 A OLA 1207 ? C8  ? H  OLA 1   C8  
71  1 N 1 A OLA 1207 ? C9  ? H  OLA 1   C9  
72  1 N 1 A OLA 1207 ? C10 ? H  OLA 1   C10 
73  1 N 1 A OLA 1207 ? C11 ? H  OLA 1   C11 
74  1 N 1 A OLA 1207 ? C12 ? H  OLA 1   C12 
75  1 N 1 A OLA 1207 ? C13 ? H  OLA 1   C13 
76  1 N 1 A OLA 1207 ? C14 ? H  OLA 1   C14 
77  1 N 1 A OLA 1207 ? C15 ? H  OLA 1   C15 
78  1 N 1 A OLA 1207 ? C16 ? H  OLA 1   C16 
79  1 N 1 A OLA 1207 ? C17 ? H  OLA 1   C17 
80  1 N 1 A OLA 1207 ? C18 ? H  OLA 1   C18 
81  1 N 1 A OLA 1208 ? C17 ? I  OLA 1   C17 
82  1 N 1 A OLA 1208 ? C18 ? I  OLA 1   C18 
83  1 N 1 A OLA 1209 ? C15 ? J  OLA 1   C15 
84  1 N 1 A OLA 1209 ? C16 ? J  OLA 1   C16 
85  1 N 1 A OLA 1209 ? C17 ? J  OLA 1   C17 
86  1 N 1 A OLA 1209 ? C18 ? J  OLA 1   C18 
87  1 N 1 A OLA 1210 ? C11 ? K  OLA 1   C11 
88  1 N 1 A OLA 1210 ? C12 ? K  OLA 1   C12 
89  1 N 1 A OLA 1210 ? C13 ? K  OLA 1   C13 
90  1 N 1 A OLA 1210 ? C14 ? K  OLA 1   C14 
91  1 N 1 A OLA 1210 ? C15 ? K  OLA 1   C15 
92  1 N 1 A OLA 1210 ? C16 ? K  OLA 1   C16 
93  1 N 1 A OLA 1210 ? C17 ? K  OLA 1   C17 
94  1 N 1 A OLA 1210 ? C18 ? K  OLA 1   C18 
95  1 N 1 A OLA 1212 ? C15 ? M  OLA 1   C15 
96  1 N 1 A OLA 1212 ? C16 ? M  OLA 1   C16 
97  1 N 1 A OLA 1212 ? C17 ? M  OLA 1   C17 
98  1 N 1 A OLA 1212 ? C18 ? M  OLA 1   C18 
99  1 N 1 A OLA 1213 ? C15 ? N  OLA 1   C15 
100 1 N 1 A OLA 1213 ? C16 ? N  OLA 1   C16 
101 1 N 1 A OLA 1213 ? C17 ? N  OLA 1   C17 
102 1 N 1 A OLA 1213 ? C18 ? N  OLA 1   C18 
103 1 N 1 A OLC 1214 ? C18 ? O  OLC 1   C18 
104 1 N 1 A OLC 1214 ? C17 ? O  OLC 1   C17 
105 1 N 1 A OLC 1214 ? C16 ? O  OLC 1   C16 
106 1 N 1 A OLC 1214 ? C15 ? O  OLC 1   C15 
107 1 N 1 A OLC 1214 ? C13 ? O  OLC 1   C13 
108 1 N 1 A OLC 1214 ? C14 ? O  OLC 1   C14 
109 1 N 1 A OLB 1215 ? C11 ? P  OLB 1   C11 
110 1 N 1 A OLB 1215 ? C12 ? P  OLB 1   C12 
111 1 N 1 A OLB 1215 ? C13 ? P  OLB 1   C13 
112 1 N 1 A OLB 1215 ? C14 ? P  OLB 1   C14 
113 1 N 1 A OLB 1215 ? C15 ? P  OLB 1   C15 
114 1 N 1 A OLB 1215 ? C16 ? P  OLB 1   C16 
115 1 N 1 A OLB 1215 ? C17 ? P  OLB 1   C17 
116 1 N 1 A OLB 1215 ? C18 ? P  OLB 1   C18 
117 1 N 1 A OLA 1217 ? C11 ? R  OLA 1   C11 
118 1 N 1 A OLA 1217 ? C12 ? R  OLA 1   C12 
119 1 N 1 A OLA 1217 ? C13 ? R  OLA 1   C13 
120 1 N 1 A OLA 1217 ? C14 ? R  OLA 1   C14 
121 1 N 1 A OLA 1217 ? C15 ? R  OLA 1   C15 
122 1 N 1 A OLA 1217 ? C16 ? R  OLA 1   C16 
123 1 N 1 A OLA 1217 ? C17 ? R  OLA 1   C17 
124 1 N 1 A OLA 1217 ? C18 ? R  OLA 1   C18 
125 1 N 1 A OLA 1218 ? C18 ? S  OLA 1   C18 
126 1 N 1 A OLA 1219 ? O1  ? T  OLA 1   O1  
127 1 N 1 A OLA 1219 ? O2  ? T  OLA 1   O2  
128 1 N 1 A OLA 1219 ? C16 ? T  OLA 1   C16 
129 1 N 1 A OLA 1219 ? C17 ? T  OLA 1   C17 
130 1 N 1 A OLA 1219 ? C18 ? T  OLA 1   C18 
131 1 N 1 A OLA 1220 ? C1  ? U  OLA 1   C1  
132 1 N 1 A OLA 1220 ? O1  ? U  OLA 1   O1  
133 1 N 1 A OLA 1220 ? O2  ? U  OLA 1   O2  
134 1 N 1 A OLA 1220 ? C2  ? U  OLA 1   C2  
135 1 N 1 A OLA 1220 ? C3  ? U  OLA 1   C3  
136 1 N 1 A OLA 1220 ? C4  ? U  OLA 1   C4  
137 1 N 1 A OLA 1220 ? C5  ? U  OLA 1   C5  
138 1 N 1 A OLA 1220 ? C6  ? U  OLA 1   C6  
139 1 N 1 A OLA 1220 ? C7  ? U  OLA 1   C7  
140 1 N 1 A OLA 1220 ? C8  ? U  OLA 1   C8  
141 1 N 1 A OLA 1221 ? C14 ? V  OLA 1   C14 
142 1 N 1 A OLA 1221 ? C15 ? V  OLA 1   C15 
143 1 N 1 A OLA 1221 ? C16 ? V  OLA 1   C16 
144 1 N 1 A OLA 1221 ? C17 ? V  OLA 1   C17 
145 1 N 1 A OLA 1221 ? C18 ? V  OLA 1   C18 
146 1 N 1 A OLA 1223 ? C12 ? X  OLA 1   C12 
147 1 N 1 A OLA 1223 ? C13 ? X  OLA 1   C13 
148 1 N 1 A OLA 1223 ? C14 ? X  OLA 1   C14 
149 1 N 1 A OLA 1223 ? C15 ? X  OLA 1   C15 
150 1 N 1 A OLA 1223 ? C16 ? X  OLA 1   C16 
151 1 N 1 A OLA 1223 ? C17 ? X  OLA 1   C17 
152 1 N 1 A OLA 1223 ? C18 ? X  OLA 1   C18 
153 1 N 1 A OLA 1224 ? C13 ? Y  OLA 1   C13 
154 1 N 1 A OLA 1224 ? C14 ? Y  OLA 1   C14 
155 1 N 1 A OLA 1224 ? C15 ? Y  OLA 1   C15 
156 1 N 1 A OLA 1224 ? C16 ? Y  OLA 1   C16 
157 1 N 1 A OLA 1224 ? C17 ? Y  OLA 1   C17 
158 1 N 1 A OLA 1224 ? C18 ? Y  OLA 1   C18 
159 1 N 1 A OLA 1225 ? C12 ? Z  OLA 1   C12 
160 1 N 1 A OLA 1225 ? C13 ? Z  OLA 1   C13 
161 1 N 1 A OLA 1225 ? C14 ? Z  OLA 1   C14 
162 1 N 1 A OLA 1225 ? C15 ? Z  OLA 1   C15 
163 1 N 1 A OLA 1225 ? C16 ? Z  OLA 1   C16 
164 1 N 1 A OLA 1225 ? C17 ? Z  OLA 1   C17 
165 1 N 1 A OLA 1225 ? C18 ? Z  OLA 1   C18 
166 1 N 1 A OLA 1226 ? C12 ? AA OLA 1   C12 
167 1 N 1 A OLA 1226 ? C13 ? AA OLA 1   C13 
168 1 N 1 A OLA 1226 ? C14 ? AA OLA 1   C14 
169 1 N 1 A OLA 1226 ? C15 ? AA OLA 1   C15 
170 1 N 1 A OLA 1226 ? C16 ? AA OLA 1   C16 
171 1 N 1 A OLA 1226 ? C17 ? AA OLA 1   C17 
172 1 N 1 A OLA 1226 ? C18 ? AA OLA 1   C18 
173 1 N 1 A OLA 1227 ? C1  ? BA OLA 1   C1  
174 1 N 1 A OLA 1227 ? O1  ? BA OLA 1   O1  
175 1 N 1 A OLA 1227 ? O2  ? BA OLA 1   O2  
176 1 N 1 A OLA 1227 ? C10 ? BA OLA 1   C10 
177 1 N 1 A OLA 1227 ? C11 ? BA OLA 1   C11 
178 1 N 1 A OLA 1227 ? C12 ? BA OLA 1   C12 
179 1 N 1 A OLA 1227 ? C13 ? BA OLA 1   C13 
180 1 N 1 A OLA 1227 ? C14 ? BA OLA 1   C14 
181 1 N 1 A OLA 1227 ? C15 ? BA OLA 1   C15 
182 1 N 1 A OLA 1227 ? C16 ? BA OLA 1   C16 
183 1 N 1 A OLA 1227 ? C17 ? BA OLA 1   C17 
184 1 N 1 A OLA 1227 ? C18 ? BA OLA 1   C18 
185 1 N 1 A OLC 1228 ? C18 ? CA OLC 1   C18 
186 1 N 1 A OLC 1228 ? C17 ? CA OLC 1   C17 
187 1 N 1 A OLC 1228 ? C11 ? CA OLC 1   C11 
188 1 N 1 A OLC 1228 ? C16 ? CA OLC 1   C16 
189 1 N 1 A OLC 1228 ? C12 ? CA OLC 1   C12 
190 1 N 1 A OLC 1228 ? C15 ? CA OLC 1   C15 
191 1 N 1 A OLC 1228 ? C13 ? CA OLC 1   C13 
192 1 N 1 A OLC 1228 ? C14 ? CA OLC 1   C14 
193 1 N 1 A OLA 1229 ? C10 ? DA OLA 1   C10 
194 1 N 1 A OLA 1229 ? C11 ? DA OLA 1   C11 
195 1 N 1 A OLA 1229 ? C12 ? DA OLA 1   C12 
196 1 N 1 A OLA 1229 ? C13 ? DA OLA 1   C13 
197 1 N 1 A OLA 1229 ? C14 ? DA OLA 1   C14 
198 1 N 1 A OLA 1229 ? C15 ? DA OLA 1   C15 
199 1 N 1 A OLA 1229 ? C16 ? DA OLA 1   C16 
200 1 N 1 A OLA 1229 ? C17 ? DA OLA 1   C17 
201 1 N 1 A OLA 1229 ? C18 ? DA OLA 1   C18 
202 1 N 1 A OLA 1230 ? C12 ? EA OLA 1   C12 
203 1 N 1 A OLA 1230 ? C13 ? EA OLA 1   C13 
204 1 N 1 A OLA 1230 ? C14 ? EA OLA 1   C14 
205 1 N 1 A OLA 1230 ? C15 ? EA OLA 1   C15 
206 1 N 1 A OLA 1230 ? C16 ? EA OLA 1   C16 
207 1 N 1 A OLA 1230 ? C17 ? EA OLA 1   C17 
208 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                     8RW7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     39.519 
_cell.length_a_esd                 ? 
_cell.length_b                     179.697 
_cell.length_b_esd                 ? 
_cell.length_c                     139.927 
_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                         8RW7 
_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                   8RW7 
_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             2.49 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.66 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          '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         2020-08-30 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RW7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.25 
_reflns.d_resolution_low                               44.92 
_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                                     24300 
_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                           99.92 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.25 
_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                                0.044 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.25 
_reflns_shell.d_res_low                                     2.33 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.16 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2405 
_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                               2.0 
_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                               0.046 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.634 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.92 
_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                                 8RW7 
_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                            2.25 
_refine.ls_d_res_low                             44.92 
_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                     24288 
_refine.ls_number_reflns_R_free                  1180 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 4.86 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1880 
_refine.ls_R_factor_R_free                       0.2141 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1867 
_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                 21.27 
_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                            0.23 
_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                       2.25 
_refine_hist.d_res_low                        44.92 
_refine_hist.number_atoms_solvent             110 
_refine_hist.number_atoms_total               3566 
_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        2962 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         494 
_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  ? 3592 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.632  ? 4798 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.480 ? 746  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041  ? 538  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 586  ? 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' 2.25 2.35  . . 131 2857 100.00 . . . . 0.2332 . . . . . . . . . . . 0.2864 
'X-RAY DIFFRACTION' 2.35 2.48  . . 150 2847 100.00 . . . . 0.1986 . . . . . . . . . . . 0.2470 
'X-RAY DIFFRACTION' 2.48 2.63  . . 132 2857 100.00 . . . . 0.1861 . . . . . . . . . . . 0.2297 
'X-RAY DIFFRACTION' 2.63 2.83  . . 150 2857 100.00 . . . . 0.1789 . . . . . . . . . . . 0.2106 
'X-RAY DIFFRACTION' 2.83 3.12  . . 147 2843 100.00 . . . . 0.1877 . . . . . . . . . . . 0.2210 
'X-RAY DIFFRACTION' 3.12 3.57  . . 140 2904 100.00 . . . . 0.1803 . . . . . . . . . . . 0.2096 
'X-RAY DIFFRACTION' 3.57 4.50  . . 180 2889 100.00 . . . . 0.1682 . . . . . . . . . . . 0.1975 
'X-RAY DIFFRACTION' 4.50 44.92 . . 150 3054 100.00 . . . . 0.1947 . . . . . . . . . . . 0.2035 
# 
_struct.entry_id                     8RW7 
_struct.title                        
;Crystal structure of the adenosine A2A receptor in complex with the synthetic photoswitch 'StilSwitch1
;
_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        8RW7 
_struct_keywords.text            
;GPCR, adenosine receptor, synthetic photoswitch, 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 5 ? 
P  N N 6 ? 
Q  N N 5 ? 
R  N N 4 ? 
S  N N 4 ? 
T  N N 4 ? 
U  N N 4 ? 
V  N N 4 ? 
W  N N 4 ? 
X  N N 4 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 4 ? 
BA N N 4 ? 
CA N N 5 ? 
DA N N 4 ? 
EA N N 4 ? 
FA N N 7 ? 
GA N N 8 ? 
# 
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 8RW7 A 27  ? 233 ? P29274 2   ? 208 ? 2    208  
2 2 8RW7 A 234 ? 338 ? P0ABE7 23  ? 127 ? 1001 1105 
3 3 8RW7 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 8RW7 MET A 1   ? UNP P29274 ?   ?   'initiating methionine' -24  1  
1 8RW7 LYS A 2   ? UNP P29274 ?   ?   'expression tag'        -23  2  
1 8RW7 THR A 3   ? UNP P29274 ?   ?   'expression tag'        -22  3  
1 8RW7 ILE A 4   ? UNP P29274 ?   ?   'expression tag'        -21  4  
1 8RW7 ILE A 5   ? UNP P29274 ?   ?   'expression tag'        -20  5  
1 8RW7 ALA A 6   ? UNP P29274 ?   ?   'expression tag'        -19  6  
1 8RW7 LEU A 7   ? UNP P29274 ?   ?   'expression tag'        -18  7  
1 8RW7 SER A 8   ? UNP P29274 ?   ?   'expression tag'        -17  8  
1 8RW7 TYR A 9   ? UNP P29274 ?   ?   'expression tag'        -16  9  
1 8RW7 ILE A 10  ? UNP P29274 ?   ?   'expression tag'        -15  10 
1 8RW7 PHE A 11  ? UNP P29274 ?   ?   'expression tag'        -14  11 
1 8RW7 CYS A 12  ? UNP P29274 ?   ?   'expression tag'        -13  12 
1 8RW7 LEU A 13  ? UNP P29274 ?   ?   'expression tag'        -12  13 
1 8RW7 VAL A 14  ? UNP P29274 ?   ?   'expression tag'        -11  14 
1 8RW7 PHE A 15  ? UNP P29274 ?   ?   'expression tag'        -10  15 
1 8RW7 ALA A 16  ? UNP P29274 ?   ?   'expression tag'        -9   16 
1 8RW7 ASP A 17  ? UNP P29274 ?   ?   'expression tag'        -8   17 
1 8RW7 TYR A 18  ? UNP P29274 ?   ?   'expression tag'        -7   18 
1 8RW7 LYS A 19  ? UNP P29274 ?   ?   'expression tag'        -6   19 
1 8RW7 ASP A 20  ? UNP P29274 ?   ?   'expression tag'        -5   20 
1 8RW7 ASP A 21  ? UNP P29274 ?   ?   'expression tag'        -4   21 
1 8RW7 ASP A 22  ? UNP P29274 ?   ?   'expression tag'        -3   22 
1 8RW7 ASP A 23  ? UNP P29274 ?   ?   'expression tag'        -2   23 
1 8RW7 GLY A 24  ? UNP P29274 ?   ?   'expression tag'        -1   24 
1 8RW7 ALA A 25  ? UNP P29274 ?   ?   'expression tag'        0    25 
1 8RW7 PRO A 26  ? UNP P29274 ?   ?   'expression tag'        1    26 
1 8RW7 LEU A 79  ? UNP P29274 ALA 54  conflict                54   27 
1 8RW7 ALA A 113 ? UNP P29274 THR 88  conflict                88   28 
1 8RW7 ALA A 132 ? UNP P29274 ARG 107 conflict                107  29 
1 8RW7 ALA A 147 ? UNP P29274 LYS 122 conflict                122  30 
1 8RW7 ALA A 179 ? UNP P29274 ASN 154 conflict                154  31 
1 8RW7 ALA A 227 ? UNP P29274 LEU 202 conflict                202  32 
2 8RW7 TRP A 240 ? UNP P0ABE7 MET 29  conflict                1007 33 
2 8RW7 ILE A 335 ? UNP P0ABE7 HIS 124 conflict                1102 34 
2 8RW7 LEU A 339 ? UNP P0ABE7 ?   ?   linker                  1106 35 
3 8RW7 ALA A 356 ? UNP P29274 LEU 235 conflict                235  36 
3 8RW7 ALA A 360 ? UNP P29274 VAL 239 conflict                239  37 
3 8RW7 ALA A 439 ? UNP P29274 ?   ?   'expression tag'        318  38 
3 8RW7 HIS A 440 ? UNP P29274 ?   ?   'expression tag'        319  39 
3 8RW7 HIS A 441 ? UNP P29274 ?   ?   'expression tag'        320  40 
3 8RW7 HIS A 442 ? UNP P29274 ?   ?   'expression tag'        321  41 
3 8RW7 HIS A 443 ? UNP P29274 ?   ?   'expression tag'        322  42 
3 8RW7 HIS A 444 ? UNP P29274 ?   ?   'expression tag'        323  43 
3 8RW7 HIS A 445 ? UNP P29274 ?   ?   'expression tag'        324  44 
3 8RW7 HIS A 446 ? UNP P29274 ?   ?   'expression tag'        325  45 
3 8RW7 HIS A 447 ? UNP P29274 ?   ?   'expression tag'        326  46 
3 8RW7 HIS A 448 ? UNP P29274 ?   ?   'expression tag'        327  47 
3 8RW7 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)' 11550 ? 
1 MORE         56    ? 
1 'SSA (A^2)'  20220 ? 
# 
_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 LYS A 292 ? GLU A 314 ? LYS A 1059 GLU A 1081 1 ? 23 
HELX_P HELX_P15 AB6 LYS A 316 ? TYR A 334 ? LYS A 1083 TYR A 1101 1 ? 19 
HELX_P HELX_P16 AB7 TYR A 334 ? CYS A 380 ? TYR A 1101 CYS A 259  1 ? 47 
HELX_P HELX_P17 AB8 PRO A 387 ? ILE A 413 ? PRO A 266  ILE A 292  1 ? 27 
HELX_P HELX_P18 AB9 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 ? ? ? ? ? ? ? 2.030 ? ? 
disulf3 disulf ? ? A  CYS 102 SG  ? ? ? 1_555 A  CYS 191 SG ? ? A CYS 77   A CYS 166  1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf4 disulf ? ? A  CYS 380 SG  ? ? ? 1_555 A  CYS 383 SG ? ? A CYS 259  A CYS 262  1_555 ? ? ? ? ? ? ? 2.032 ? ? 
metalc1 metalc ? ? A  ASP 77  OD1 ? ? ? 1_555 FA NA  .   NA ? ? A ASP 52   A NA  1231 1_555 ? ? ? ? ? ? ? 2.481 ? ? 
metalc2 metalc ? ? A  SER 116 OG  ? ? ? 1_555 FA NA  .   NA ? ? A SER 91   A NA  1231 1_555 ? ? ? ? ? ? ? 2.625 ? ? 
metalc3 metalc ? ? FA NA  .   NA  ? ? ? 1_555 GA HOH .   O  ? ? A NA  1231 A HOH 1352 1_555 ? ? ? ? ? ? ? 2.517 ? ? 
metalc4 metalc ? ? FA NA  .   NA  ? ? ? 1_555 GA HOH .   O  ? ? A NA  1231 A HOH 1364 1_555 ? ? ? ? ? ? ? 2.372 ? ? 
metalc5 metalc ? ? FA NA  .   NA  ? ? ? 1_555 GA HOH .   O  ? ? A NA  1231 A HOH 1375 1_555 ? ? ? ? ? ? ? 2.609 ? ? 
# 
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_555 122.1 ? 
2  OD1 ? A  ASP 77  ? A ASP 52   ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1352 ? 1_555 105.1 ? 
3  OG  ? A  SER 116 ? A SER 91   ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1352 ? 1_555 127.9 ? 
4  OD1 ? A  ASP 77  ? A ASP 52   ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1364 ? 1_555 85.6  ? 
5  OG  ? A  SER 116 ? A SER 91   ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1364 ? 1_555 109.1 ? 
6  O   ? GA HOH .   ? A HOH 1352 ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1364 ? 1_555 94.1  ? 
7  OD1 ? A  ASP 77  ? A ASP 52   ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1375 ? 1_555 89.4  ? 
8  OG  ? A  SER 116 ? A SER 91   ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1375 ? 1_555 68.2  ? 
9  O   ? GA HOH .   ? A HOH 1352 ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1375 ? 1_555 93.6  ? 
10 O   ? GA HOH .   ? A HOH 1364 ? 1_555 NA ? FA NA . ? A NA 1231 ? 1_555 O  ? GA HOH .   ? A HOH 1375 ? 1_555 171.7 ? 
# 
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                   8RW7 
_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   ? ? -120.64 -50.35 
2 1 VAL A 186  ? ? -120.34 -55.23 
3 1 VAL A 186  ? ? -120.34 -56.01 
4 1 TYR A 1101 ? ? -124.46 -61.15 
5 1 HIS A 306  ? ? -143.97 -74.04 
# 
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 LEU 308  ? A LEU 429 
41 1 Y 1 A ARG 309  ? A ARG 430 
42 1 Y 1 A GLN 310  ? A GLN 431 
43 1 Y 1 A GLN 311  ? A GLN 432 
44 1 Y 1 A GLU 312  ? A GLU 433 
45 1 Y 1 A PRO 313  ? A PRO 434 
46 1 Y 1 A PHE 314  ? A PHE 435 
47 1 Y 1 A LYS 315  ? A LYS 436 
48 1 Y 1 A ALA 316  ? A ALA 437 
49 1 Y 1 A ALA 317  ? A ALA 438 
50 1 Y 1 A ALA 318  ? A ALA 439 
51 1 Y 1 A HIS 319  ? A HIS 440 
52 1 Y 1 A HIS 320  ? A HIS 441 
53 1 Y 1 A HIS 321  ? A HIS 442 
54 1 Y 1 A HIS 322  ? A HIS 443 
55 1 Y 1 A HIS 323  ? A HIS 444 
56 1 Y 1 A HIS 324  ? A HIS 445 
57 1 Y 1 A HIS 325  ? A HIS 446 
58 1 Y 1 A HIS 326  ? A HIS 447 
59 1 Y 1 A HIS 327  ? A HIS 448 
60 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 
A1H3J C1   C  N N 1   
A1H3J C2   C  N N 2   
A1H3J O2   O  N N 3   
A1H3J C3   C  Y N 4   
A1H3J O3   O  N N 5   
A1H3J C4   C  Y N 6   
A1H3J C5   C  N N 7   
A1H3J C7   C  Y N 8   
A1H3J C6   C  N N 9   
A1H3J N    N  N N 10  
A1H3J C    C  N N 11  
A1H3J O    O  N N 12  
A1H3J C10  C  Y N 13  
A1H3J C11  C  N N 14  
A1H3J C12  C  Y N 15  
A1H3J C13  C  N N 16  
A1H3J C14  C  Y N 17  
A1H3J C15  C  Y N 18  
A1H3J C16  C  N N 19  
A1H3J C17  C  N N 20  
A1H3J C18  C  N N 21  
A1H3J C8   C  Y N 22  
A1H3J C9   C  Y N 23  
A1H3J N1   N  Y N 24  
A1H3J N2   N  Y N 25  
A1H3J N3   N  N N 26  
A1H3J O1   O  N N 27  
A1H3J H1   H  N N 28  
A1H3J H2   H  N N 29  
A1H3J H3   H  N N 30  
A1H3J H4   H  N N 31  
A1H3J H5   H  N N 32  
A1H3J H6   H  N N 33  
A1H3J H7   H  N N 34  
A1H3J H8   H  N N 35  
A1H3J H9   H  N N 36  
A1H3J H10  H  N N 37  
A1H3J H11  H  N N 38  
A1H3J H12  H  N N 39  
A1H3J H13  H  N N 40  
A1H3J H14  H  N N 41  
A1H3J H15  H  N N 42  
A1H3J H16  H  N N 43  
A1H3J H17  H  N N 44  
A1H3J H18  H  N N 45  
A1H3J H19  H  N N 46  
A1H3J H20  H  N N 47  
A1H3J H21  H  N N 48  
A1H3J 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 
OLB   C1   C  N N 428 
OLB   C2   C  N N 429 
OLB   C3   C  N N 430 
OLB   C4   C  N N 431 
OLB   C5   C  N N 432 
OLB   O19  O  N N 433 
OLB   O20  O  N N 434 
OLB   C21  C  N N 435 
OLB   C22  C  N S 436 
OLB   O23  O  N N 437 
OLB   C24  C  N N 438 
OLB   O25  O  N N 439 
OLB   C6   C  N N 440 
OLB   C7   C  N N 441 
OLB   C8   C  N N 442 
OLB   C9   C  N N 443 
OLB   C10  C  N N 444 
OLB   C11  C  N N 445 
OLB   H2   H  N N 446 
OLB   H2A  H  N N 447 
OLB   H3   H  N N 448 
OLB   H3A  H  N N 449 
OLB   H4   H  N N 450 
OLB   H4A  H  N N 451 
OLB   H5   H  N N 452 
OLB   H5A  H  N N 453 
OLB   H21  H  N N 454 
OLB   H21A H  N N 455 
OLB   H22  H  N N 456 
OLB   HO23 H  N N 457 
OLB   H24  H  N N 458 
OLB   H24A H  N N 459 
OLB   HO25 H  N N 460 
OLB   H16  H  N N 461 
OLB   H17  H  N N 462 
OLB   H18  H  N N 463 
OLB   H19  H  N N 464 
OLB   H20  H  N N 465 
OLB   H211 H  N N 466 
OLB   H221 H  N N 467 
OLB   H23  H  N N 468 
OLB   H241 H  N N 469 
OLB   H25  H  N N 470 
OLB   C12  C  N N 471 
OLB   H26  H  N N 472 
OLB   C13  C  N N 473 
OLB   H27  H  N N 474 
OLB   C14  C  N N 475 
OLB   H28  H  N N 476 
OLB   H29  H  N N 477 
OLB   H30  H  N N 478 
OLB   H31  H  N N 479 
OLB   C15  C  N N 480 
OLB   C16  C  N N 481 
OLB   H32  H  N N 482 
OLB   H33  H  N N 483 
OLB   H34  H  N N 484 
OLB   H35  H  N N 485 
OLB   C17  C  N N 486 
OLB   C18  C  N N 487 
OLB   H36  H  N N 488 
OLB   H37  H  N N 489 
OLB   H38  H  N N 490 
OLB   H39  H  N N 491 
OLB   H40  H  N N 492 
OLC   C18  C  N N 493 
OLC   C10  C  N N 494 
OLC   C9   C  N N 495 
OLC   C17  C  N N 496 
OLC   C11  C  N N 497 
OLC   C8   C  N N 498 
OLC   C24  C  N N 499 
OLC   C16  C  N N 500 
OLC   C12  C  N N 501 
OLC   C7   C  N N 502 
OLC   C15  C  N N 503 
OLC   C13  C  N N 504 
OLC   C6   C  N N 505 
OLC   C14  C  N N 506 
OLC   C5   C  N N 507 
OLC   C4   C  N N 508 
OLC   C3   C  N N 509 
OLC   C2   C  N N 510 
OLC   C21  C  N N 511 
OLC   C1   C  N N 512 
OLC   C22  C  N R 513 
OLC   O19  O  N N 514 
OLC   O25  O  N N 515 
OLC   O23  O  N N 516 
OLC   O20  O  N N 517 
OLC   H18  H  N N 518 
OLC   H18A H  N N 519 
OLC   H18B H  N N 520 
OLC   H10  H  N N 521 
OLC   H9   H  N N 522 
OLC   H17  H  N N 523 
OLC   H17A H  N N 524 
OLC   H11  H  N N 525 
OLC   H11A H  N N 526 
OLC   H8   H  N N 527 
OLC   H8A  H  N N 528 
OLC   H24  H  N N 529 
OLC   H24A H  N N 530 
OLC   H16  H  N N 531 
OLC   H16A H  N N 532 
OLC   H12  H  N N 533 
OLC   H12A H  N N 534 
OLC   H7   H  N N 535 
OLC   H7A  H  N N 536 
OLC   H15  H  N N 537 
OLC   H15A H  N N 538 
OLC   H13  H  N N 539 
OLC   H13A H  N N 540 
OLC   H6   H  N N 541 
OLC   H6A  H  N N 542 
OLC   H14  H  N N 543 
OLC   H14A H  N N 544 
OLC   H5   H  N N 545 
OLC   H5A  H  N N 546 
OLC   H4   H  N N 547 
OLC   H4A  H  N N 548 
OLC   H3   H  N N 549 
OLC   H3A  H  N N 550 
OLC   H2   H  N N 551 
OLC   H2A  H  N N 552 
OLC   H21  H  N N 553 
OLC   H21A H  N N 554 
OLC   H22  H  N N 555 
OLC   HO25 H  N N 556 
OLC   HO23 H  N N 557 
PHE   N    N  N N 558 
PHE   CA   C  N S 559 
PHE   C    C  N N 560 
PHE   O    O  N N 561 
PHE   CB   C  N N 562 
PHE   CG   C  Y N 563 
PHE   CD1  C  Y N 564 
PHE   CD2  C  Y N 565 
PHE   CE1  C  Y N 566 
PHE   CE2  C  Y N 567 
PHE   CZ   C  Y N 568 
PHE   OXT  O  N N 569 
PHE   H    H  N N 570 
PHE   H2   H  N N 571 
PHE   HA   H  N N 572 
PHE   HB2  H  N N 573 
PHE   HB3  H  N N 574 
PHE   HD1  H  N N 575 
PHE   HD2  H  N N 576 
PHE   HE1  H  N N 577 
PHE   HE2  H  N N 578 
PHE   HZ   H  N N 579 
PHE   HXT  H  N N 580 
PRO   N    N  N N 581 
PRO   CA   C  N S 582 
PRO   C    C  N N 583 
PRO   O    O  N N 584 
PRO   CB   C  N N 585 
PRO   CG   C  N N 586 
PRO   CD   C  N N 587 
PRO   OXT  O  N N 588 
PRO   H    H  N N 589 
PRO   HA   H  N N 590 
PRO   HB2  H  N N 591 
PRO   HB3  H  N N 592 
PRO   HG2  H  N N 593 
PRO   HG3  H  N N 594 
PRO   HD2  H  N N 595 
PRO   HD3  H  N N 596 
PRO   HXT  H  N N 597 
SER   N    N  N N 598 
SER   CA   C  N S 599 
SER   C    C  N N 600 
SER   O    O  N N 601 
SER   CB   C  N N 602 
SER   OG   O  N N 603 
SER   OXT  O  N N 604 
SER   H    H  N N 605 
SER   H2   H  N N 606 
SER   HA   H  N N 607 
SER   HB2  H  N N 608 
SER   HB3  H  N N 609 
SER   HG   H  N N 610 
SER   HXT  H  N N 611 
THR   N    N  N N 612 
THR   CA   C  N S 613 
THR   C    C  N N 614 
THR   O    O  N N 615 
THR   CB   C  N R 616 
THR   OG1  O  N N 617 
THR   CG2  C  N N 618 
THR   OXT  O  N N 619 
THR   H    H  N N 620 
THR   H2   H  N N 621 
THR   HA   H  N N 622 
THR   HB   H  N N 623 
THR   HG1  H  N N 624 
THR   HG21 H  N N 625 
THR   HG22 H  N N 626 
THR   HG23 H  N N 627 
THR   HXT  H  N N 628 
TRP   N    N  N N 629 
TRP   CA   C  N S 630 
TRP   C    C  N N 631 
TRP   O    O  N N 632 
TRP   CB   C  N N 633 
TRP   CG   C  Y N 634 
TRP   CD1  C  Y N 635 
TRP   CD2  C  Y N 636 
TRP   NE1  N  Y N 637 
TRP   CE2  C  Y N 638 
TRP   CE3  C  Y N 639 
TRP   CZ2  C  Y N 640 
TRP   CZ3  C  Y N 641 
TRP   CH2  C  Y N 642 
TRP   OXT  O  N N 643 
TRP   H    H  N N 644 
TRP   H2   H  N N 645 
TRP   HA   H  N N 646 
TRP   HB2  H  N N 647 
TRP   HB3  H  N N 648 
TRP   HD1  H  N N 649 
TRP   HE1  H  N N 650 
TRP   HE3  H  N N 651 
TRP   HZ2  H  N N 652 
TRP   HZ3  H  N N 653 
TRP   HH2  H  N N 654 
TRP   HXT  H  N N 655 
TYR   N    N  N N 656 
TYR   CA   C  N S 657 
TYR   C    C  N N 658 
TYR   O    O  N N 659 
TYR   CB   C  N N 660 
TYR   CG   C  Y N 661 
TYR   CD1  C  Y N 662 
TYR   CD2  C  Y N 663 
TYR   CE1  C  Y N 664 
TYR   CE2  C  Y N 665 
TYR   CZ   C  Y N 666 
TYR   OH   O  N N 667 
TYR   OXT  O  N N 668 
TYR   H    H  N N 669 
TYR   H2   H  N N 670 
TYR   HA   H  N N 671 
TYR   HB2  H  N N 672 
TYR   HB3  H  N N 673 
TYR   HD1  H  N N 674 
TYR   HD2  H  N N 675 
TYR   HE1  H  N N 676 
TYR   HE2  H  N N 677 
TYR   HH   H  N N 678 
TYR   HXT  H  N N 679 
VAL   N    N  N N 680 
VAL   CA   C  N S 681 
VAL   C    C  N N 682 
VAL   O    O  N N 683 
VAL   CB   C  N N 684 
VAL   CG1  C  N N 685 
VAL   CG2  C  N N 686 
VAL   OXT  O  N N 687 
VAL   H    H  N N 688 
VAL   H2   H  N N 689 
VAL   HA   H  N N 690 
VAL   HB   H  N N 691 
VAL   HG11 H  N N 692 
VAL   HG12 H  N N 693 
VAL   HG13 H  N N 694 
VAL   HG21 H  N N 695 
VAL   HG22 H  N N 696 
VAL   HG23 H  N N 697 
VAL   HXT  H  N N 698 
# 
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 
A1H3J C13 O2   sing N N 1   
A1H3J O2  C12  sing N N 2   
A1H3J O1  C11  sing N N 3   
A1H3J O1  C10  sing N N 4   
A1H3J C12 C10  doub Y N 5   
A1H3J C12 C14  sing Y N 6   
A1H3J C10 C9   sing Y N 7   
A1H3J C14 C7   doub Y N 8   
A1H3J C9  C8   doub Y N 9   
A1H3J C7  C8   sing Y N 10  
A1H3J C7  C6   sing N N 11  
A1H3J C6  C5   doub N E 12  
A1H3J C16 C17  sing N N 13  
A1H3J C16 N3   sing N N 14  
A1H3J N2  C4   doub Y N 15  
A1H3J N2  C15  sing Y N 16  
A1H3J C5  C4   sing N N 17  
A1H3J C4  N1   sing Y N 18  
A1H3J N3  C15  sing N N 19  
A1H3J N3  C18  sing N N 20  
A1H3J C15 C3   doub Y N 21  
A1H3J O3  C18  doub N N 22  
A1H3J C18 N    sing N N 23  
A1H3J N1  C3   sing Y N 24  
A1H3J C3  C2   sing N N 25  
A1H3J N   C2   sing N N 26  
A1H3J N   C1   sing N N 27  
A1H3J C2  O    doub N N 28  
A1H3J C   C1   sing N N 29  
A1H3J C1  H1   sing N N 30  
A1H3J C1  H2   sing N N 31  
A1H3J C5  H3   sing N N 32  
A1H3J C6  H4   sing N N 33  
A1H3J C   H5   sing N N 34  
A1H3J C   H6   sing N N 35  
A1H3J C   H7   sing N N 36  
A1H3J C11 H8   sing N N 37  
A1H3J C11 H9   sing N N 38  
A1H3J C11 H10  sing N N 39  
A1H3J C13 H11  sing N N 40  
A1H3J C13 H12  sing N N 41  
A1H3J C13 H13  sing N N 42  
A1H3J C14 H14  sing N N 43  
A1H3J C16 H15  sing N N 44  
A1H3J C16 H16  sing N N 45  
A1H3J C17 H17  sing N N 46  
A1H3J C17 H18  sing N N 47  
A1H3J C17 H19  sing N N 48  
A1H3J C8  H20  sing N N 49  
A1H3J C9  H21  sing N N 50  
A1H3J N1  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 
OLB   C1  O19  doub N N 418 
OLB   C1  O20  sing N N 419 
OLB   C2  C1   sing N N 420 
OLB   C3  C2   sing N N 421 
OLB   C4  C3   sing N N 422 
OLB   C5  C4   sing N N 423 
OLB   C5  C6   sing N N 424 
OLB   O20 C21  sing N N 425 
OLB   C21 C22  sing N N 426 
OLB   C22 C24  sing N N 427 
OLB   O23 C22  sing N N 428 
OLB   C24 O25  sing N N 429 
OLB   C6  C7   sing N N 430 
OLB   C7  C8   sing N N 431 
OLB   C8  C9   sing N N 432 
OLB   C9  C10  doub N Z 433 
OLB   C10 C11  sing N N 434 
OLB   C2  H2   sing N N 435 
OLB   C2  H2A  sing N N 436 
OLB   C3  H3   sing N N 437 
OLB   C3  H3A  sing N N 438 
OLB   C4  H4   sing N N 439 
OLB   C4  H4A  sing N N 440 
OLB   C5  H5   sing N N 441 
OLB   C5  H5A  sing N N 442 
OLB   C21 H21  sing N N 443 
OLB   C21 H21A sing N N 444 
OLB   C22 H22  sing N N 445 
OLB   O23 HO23 sing N N 446 
OLB   C24 H24  sing N N 447 
OLB   C24 H24A sing N N 448 
OLB   O25 HO25 sing N N 449 
OLB   C6  H16  sing N N 450 
OLB   C6  H17  sing N N 451 
OLB   C7  H18  sing N N 452 
OLB   C7  H19  sing N N 453 
OLB   C8  H20  sing N N 454 
OLB   C8  H211 sing N N 455 
OLB   C9  H221 sing N N 456 
OLB   C10 H23  sing N N 457 
OLB   C11 H241 sing N N 458 
OLB   C11 H25  sing N N 459 
OLB   C11 C12  sing N N 460 
OLB   C12 H26  sing N N 461 
OLB   C12 C13  sing N N 462 
OLB   C12 H27  sing N N 463 
OLB   C13 C14  sing N N 464 
OLB   C13 H28  sing N N 465 
OLB   C13 H29  sing N N 466 
OLB   C14 H30  sing N N 467 
OLB   C14 H31  sing N N 468 
OLB   C14 C15  sing N N 469 
OLB   C15 C16  sing N N 470 
OLB   C15 H32  sing N N 471 
OLB   C15 H33  sing N N 472 
OLB   C16 H34  sing N N 473 
OLB   C16 H35  sing N N 474 
OLB   C16 C17  sing N N 475 
OLB   C17 C18  sing N N 476 
OLB   C17 H36  sing N N 477 
OLB   C17 H37  sing N N 478 
OLB   C18 H38  sing N N 479 
OLB   C18 H39  sing N N 480 
OLB   C18 H40  sing N N 481 
OLC   C18 C17  sing N N 482 
OLC   C10 C9   doub N N 483 
OLC   C10 C11  sing N N 484 
OLC   C9  C8   sing N N 485 
OLC   C17 C16  sing N Z 486 
OLC   C11 C12  sing N N 487 
OLC   C8  C7   sing N N 488 
OLC   C24 C22  sing N N 489 
OLC   C24 O25  sing N N 490 
OLC   C16 C15  sing N N 491 
OLC   C12 C13  sing N N 492 
OLC   C7  C6   sing N N 493 
OLC   C15 C14  sing N N 494 
OLC   C13 C14  sing N N 495 
OLC   C6  C5   sing N N 496 
OLC   C5  C4   sing N N 497 
OLC   C4  C3   sing N N 498 
OLC   C3  C2   sing N N 499 
OLC   C2  C1   sing N N 500 
OLC   C21 C22  sing N N 501 
OLC   C21 O20  sing N N 502 
OLC   C1  O19  doub N N 503 
OLC   C1  O20  sing N N 504 
OLC   C22 O23  sing N N 505 
OLC   C18 H18  sing N N 506 
OLC   C18 H18A sing N N 507 
OLC   C18 H18B sing N N 508 
OLC   C10 H10  sing N N 509 
OLC   C9  H9   sing N N 510 
OLC   C17 H17  sing N N 511 
OLC   C17 H17A sing N N 512 
OLC   C11 H11  sing N N 513 
OLC   C11 H11A sing N N 514 
OLC   C8  H8   sing N N 515 
OLC   C8  H8A  sing N N 516 
OLC   C24 H24  sing N N 517 
OLC   C24 H24A sing N N 518 
OLC   C16 H16  sing N N 519 
OLC   C16 H16A sing N N 520 
OLC   C12 H12  sing N N 521 
OLC   C12 H12A sing N N 522 
OLC   C7  H7   sing N N 523 
OLC   C7  H7A  sing N N 524 
OLC   C15 H15  sing N N 525 
OLC   C15 H15A sing N N 526 
OLC   C13 H13  sing N N 527 
OLC   C13 H13A sing N N 528 
OLC   C6  H6   sing N N 529 
OLC   C6  H6A  sing N N 530 
OLC   C14 H14  sing N N 531 
OLC   C14 H14A sing N N 532 
OLC   C5  H5   sing N N 533 
OLC   C5  H5A  sing N N 534 
OLC   C4  H4   sing N N 535 
OLC   C4  H4A  sing N N 536 
OLC   C3  H3   sing N N 537 
OLC   C3  H3A  sing N N 538 
OLC   C2  H2   sing N N 539 
OLC   C2  H2A  sing N N 540 
OLC   C21 H21  sing N N 541 
OLC   C21 H21A sing N N 542 
OLC   C22 H22  sing N N 543 
OLC   O25 HO25 sing N N 544 
OLC   O23 HO23 sing N N 545 
PHE   N   CA   sing N N 546 
PHE   N   H    sing N N 547 
PHE   N   H2   sing N N 548 
PHE   CA  C    sing N N 549 
PHE   CA  CB   sing N N 550 
PHE   CA  HA   sing N N 551 
PHE   C   O    doub N N 552 
PHE   C   OXT  sing N N 553 
PHE   CB  CG   sing N N 554 
PHE   CB  HB2  sing N N 555 
PHE   CB  HB3  sing N N 556 
PHE   CG  CD1  doub Y N 557 
PHE   CG  CD2  sing Y N 558 
PHE   CD1 CE1  sing Y N 559 
PHE   CD1 HD1  sing N N 560 
PHE   CD2 CE2  doub Y N 561 
PHE   CD2 HD2  sing N N 562 
PHE   CE1 CZ   doub Y N 563 
PHE   CE1 HE1  sing N N 564 
PHE   CE2 CZ   sing Y N 565 
PHE   CE2 HE2  sing N N 566 
PHE   CZ  HZ   sing N N 567 
PHE   OXT HXT  sing N N 568 
PRO   N   CA   sing N N 569 
PRO   N   CD   sing N N 570 
PRO   N   H    sing N N 571 
PRO   CA  C    sing N N 572 
PRO   CA  CB   sing N N 573 
PRO   CA  HA   sing N N 574 
PRO   C   O    doub N N 575 
PRO   C   OXT  sing N N 576 
PRO   CB  CG   sing N N 577 
PRO   CB  HB2  sing N N 578 
PRO   CB  HB3  sing N N 579 
PRO   CG  CD   sing N N 580 
PRO   CG  HG2  sing N N 581 
PRO   CG  HG3  sing N N 582 
PRO   CD  HD2  sing N N 583 
PRO   CD  HD3  sing N N 584 
PRO   OXT HXT  sing N N 585 
SER   N   CA   sing N N 586 
SER   N   H    sing N N 587 
SER   N   H2   sing N N 588 
SER   CA  C    sing N N 589 
SER   CA  CB   sing N N 590 
SER   CA  HA   sing N N 591 
SER   C   O    doub N N 592 
SER   C   OXT  sing N N 593 
SER   CB  OG   sing N N 594 
SER   CB  HB2  sing N N 595 
SER   CB  HB3  sing N N 596 
SER   OG  HG   sing N N 597 
SER   OXT HXT  sing N N 598 
THR   N   CA   sing N N 599 
THR   N   H    sing N N 600 
THR   N   H2   sing N N 601 
THR   CA  C    sing N N 602 
THR   CA  CB   sing N N 603 
THR   CA  HA   sing N N 604 
THR   C   O    doub N N 605 
THR   C   OXT  sing N N 606 
THR   CB  OG1  sing N N 607 
THR   CB  CG2  sing N N 608 
THR   CB  HB   sing N N 609 
THR   OG1 HG1  sing N N 610 
THR   CG2 HG21 sing N N 611 
THR   CG2 HG22 sing N N 612 
THR   CG2 HG23 sing N N 613 
THR   OXT HXT  sing N N 614 
TRP   N   CA   sing N N 615 
TRP   N   H    sing N N 616 
TRP   N   H2   sing N N 617 
TRP   CA  C    sing N N 618 
TRP   CA  CB   sing N N 619 
TRP   CA  HA   sing N N 620 
TRP   C   O    doub N N 621 
TRP   C   OXT  sing N N 622 
TRP   CB  CG   sing N N 623 
TRP   CB  HB2  sing N N 624 
TRP   CB  HB3  sing N N 625 
TRP   CG  CD1  doub Y N 626 
TRP   CG  CD2  sing Y N 627 
TRP   CD1 NE1  sing Y N 628 
TRP   CD1 HD1  sing N N 629 
TRP   CD2 CE2  doub Y N 630 
TRP   CD2 CE3  sing Y N 631 
TRP   NE1 CE2  sing Y N 632 
TRP   NE1 HE1  sing N N 633 
TRP   CE2 CZ2  sing Y N 634 
TRP   CE3 CZ3  doub Y N 635 
TRP   CE3 HE3  sing N N 636 
TRP   CZ2 CH2  doub Y N 637 
TRP   CZ2 HZ2  sing N N 638 
TRP   CZ3 CH2  sing Y N 639 
TRP   CZ3 HZ3  sing N N 640 
TRP   CH2 HH2  sing N N 641 
TRP   OXT HXT  sing N N 642 
TYR   N   CA   sing N N 643 
TYR   N   H    sing N N 644 
TYR   N   H2   sing N N 645 
TYR   CA  C    sing N N 646 
TYR   CA  CB   sing N N 647 
TYR   CA  HA   sing N N 648 
TYR   C   O    doub N N 649 
TYR   C   OXT  sing N N 650 
TYR   CB  CG   sing N N 651 
TYR   CB  HB2  sing N N 652 
TYR   CB  HB3  sing N N 653 
TYR   CG  CD1  doub Y N 654 
TYR   CG  CD2  sing Y N 655 
TYR   CD1 CE1  sing Y N 656 
TYR   CD1 HD1  sing N N 657 
TYR   CD2 CE2  doub Y N 658 
TYR   CD2 HD2  sing N N 659 
TYR   CE1 CZ   doub Y N 660 
TYR   CE1 HE1  sing N N 661 
TYR   CE2 CZ   sing Y N 662 
TYR   CE2 HE2  sing N N 663 
TYR   CZ  OH   sing N N 664 
TYR   OH  HH   sing N N 665 
TYR   OXT HXT  sing N N 666 
VAL   N   CA   sing N N 667 
VAL   N   H    sing N N 668 
VAL   N   H2   sing N N 669 
VAL   CA  C    sing N N 670 
VAL   CA  CB   sing N N 671 
VAL   CA  HA   sing N N 672 
VAL   C   O    doub N N 673 
VAL   C   OXT  sing N N 674 
VAL   CB  CG1  sing N N 675 
VAL   CB  CG2  sing N N 676 
VAL   CB  HB   sing N N 677 
VAL   CG1 HG11 sing N N 678 
VAL   CG1 HG12 sing N N 679 
VAL   CG1 HG13 sing N N 680 
VAL   CG2 HG21 sing N N 681 
VAL   CG2 HG22 sing N N 682 
VAL   CG2 HG23 sing N N 683 
VAL   OXT HXT  sing N N 684 
# 
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                    8RW7 
_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]   0.025304 
_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]   0.005565 
_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]   0.007147 
_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  ? -22.464 21.973  1.183  1.00 66.21  ? 0    ALA   A N   1 
ATOM   2    C  CA  . ALA   A  1 25  ? -23.554 21.306  0.480  1.00 71.31  ? 0    ALA   A CA  1 
ATOM   3    C  C   . ALA   A  1 25  ? -24.680 20.968  1.451  1.00 64.71  ? 0    ALA   A C   1 
ATOM   4    O  O   . ALA   A  1 25  ? -24.421 20.735  2.634  1.00 66.04  ? 0    ALA   A O   1 
ATOM   5    C  CB  . ALA   A  1 25  ? -23.046 20.051  -0.213 1.00 62.66  ? 0    ALA   A CB  1 
ATOM   6    N  N   . PRO   A  1 26  ? -25.922 20.978  0.967  1.00 63.99  ? 1    PRO   A N   1 
ATOM   7    C  CA  . PRO   A  1 26  ? -27.066 20.679  1.840  1.00 52.98  ? 1    PRO   A CA  1 
ATOM   8    C  C   . PRO   A  1 26  ? -26.878 19.370  2.584  1.00 56.78  ? 1    PRO   A C   1 
ATOM   9    O  O   . PRO   A  1 26  ? -26.563 18.336  1.974  1.00 50.76  ? 1    PRO   A O   1 
ATOM   10   C  CB  . PRO   A  1 26  ? -28.241 20.590  0.855  1.00 52.97  ? 1    PRO   A CB  1 
ATOM   11   C  CG  . PRO   A  1 26  ? -27.843 21.465  -0.278 1.00 53.79  ? 1    PRO   A CG  1 
ATOM   12   C  CD  . PRO   A  1 26  ? -26.344 21.358  -0.393 1.00 54.47  ? 1    PRO   A CD  1 
ATOM   13   N  N   . PRO   A  1 27  ? -27.046 19.381  3.909  1.00 57.23  ? 2    PRO   A N   1 
ATOM   14   C  CA  . PRO   A  1 27  ? -26.770 18.167  4.696  1.00 52.01  ? 2    PRO   A CA  1 
ATOM   15   C  C   . PRO   A  1 27  ? -27.647 16.985  4.322  1.00 48.79  ? 2    PRO   A C   1 
ATOM   16   O  O   . PRO   A  1 27  ? -27.217 15.834  4.473  1.00 38.49  ? 2    PRO   A O   1 
ATOM   17   C  CB  . PRO   A  1 27  ? -27.013 18.620  6.146  1.00 58.76  ? 2    PRO   A CB  1 
ATOM   18   C  CG  . PRO   A  1 27  ? -27.030 20.117  6.100  1.00 65.65  ? 2    PRO   A CG  1 
ATOM   19   C  CD  . PRO   A  1 27  ? -27.532 20.487  4.747  1.00 63.29  ? 2    PRO   A CD  1 
ATOM   20   N  N   . ILE   A  1 28  ? -28.866 17.237  3.835  1.00 40.76  ? 3    ILE   A N   1 
ATOM   21   C  CA  . ILE   A  1 28  ? -29.789 16.158  3.512  1.00 49.86  ? 3    ILE   A CA  1 
ATOM   22   C  C   . ILE   A  1 28  ? -29.268 15.288  2.375  1.00 42.83  ? 3    ILE   A C   1 
ATOM   23   O  O   . ILE   A  1 28  ? -29.753 14.168  2.186  1.00 43.17  ? 3    ILE   A O   1 
ATOM   24   C  CB  . ILE   A  1 28  ? -31.191 16.740  3.194  1.00 35.33  ? 3    ILE   A CB  1 
ATOM   25   C  CG1 . ILE   A  1 28  ? -32.266 15.655  3.289  1.00 54.90  ? 3    ILE   A CG1 1 
ATOM   26   C  CG2 . ILE   A  1 28  ? -31.208 17.370  1.816  1.00 48.84  ? 3    ILE   A CG2 1 
ATOM   27   C  CD1 . ILE   A  1 28  ? -33.600 16.071  2.701  1.00 59.79  ? 3    ILE   A CD1 1 
ATOM   28   N  N   . MET   A  1 29  ? -28.289 15.775  1.610  1.00 35.51  ? 4    MET   A N   1 
ATOM   29   C  CA  . MET   A  1 29  ? -27.774 15.007  0.485  1.00 45.99  ? 4    MET   A CA  1 
ATOM   30   C  C   . MET   A  1 29  ? -26.874 13.887  0.994  1.00 32.61  ? 4    MET   A C   1 
ATOM   31   O  O   . MET   A  1 29  ? -27.100 12.705  0.703  1.00 38.02  ? 4    MET   A O   1 
ATOM   32   C  CB  . MET   A  1 29  ? -27.004 15.915  -0.484 1.00 41.45  ? 4    MET   A CB  1 
ATOM   33   C  CG  . MET   A  1 29  ? -27.852 16.955  -1.210 1.00 40.85  ? 4    MET   A CG  1 
ATOM   34   S  SD  . MET   A  1 29  ? -26.917 17.954  -2.391 1.00 45.03  ? 4    MET   A SD  1 
ATOM   35   C  CE  . MET   A  1 29  ? -26.506 16.724  -3.628 1.00 32.51  ? 4    MET   A CE  1 
ATOM   36   N  N   . GLY   A  1 30  ? -25.836 14.249  1.752  1.00 36.85  ? 5    GLY   A N   1 
ATOM   37   C  CA  . GLY   A  1 30  ? -25.001 13.239  2.384  1.00 32.44  ? 5    GLY   A CA  1 
ATOM   38   C  C   . GLY   A  1 30  ? -25.772 12.394  3.378  1.00 40.82  ? 5    GLY   A C   1 
ATOM   39   O  O   . GLY   A  1 30  ? -25.467 11.214  3.564  1.00 30.50  ? 5    GLY   A O   1 
ATOM   40   N  N   A SER   A  1 31  ? -26.779 12.984  4.029  0.30 28.43  ? 6    SER   A N   1 
ATOM   41   N  N   B SER   A  1 31  ? -26.778 12.985  4.031  0.70 28.11  ? 6    SER   A N   1 
ATOM   42   C  CA  A SER   A  1 31  ? -27.617 12.218  4.946  0.30 34.93  ? 6    SER   A CA  1 
ATOM   43   C  CA  B SER   A  1 31  ? -27.618 12.219  4.945  0.70 35.02  ? 6    SER   A CA  1 
ATOM   44   C  C   A SER   A  1 31  ? -28.432 11.169  4.201  0.30 30.80  ? 6    SER   A C   1 
ATOM   45   C  C   B SER   A  1 31  ? -28.421 11.164  4.196  0.70 30.79  ? 6    SER   A C   1 
ATOM   46   O  O   A SER   A  1 31  ? -28.615 10.051  4.698  0.30 27.59  ? 6    SER   A O   1 
ATOM   47   O  O   B SER   A  1 31  ? -28.586 10.039  4.682  0.70 27.51  ? 6    SER   A O   1 
ATOM   48   C  CB  A SER   A  1 31  ? -28.536 13.159  5.724  0.30 39.01  ? 6    SER   A CB  1 
ATOM   49   C  CB  B SER   A  1 31  ? -28.552 13.156  5.711  0.70 39.06  ? 6    SER   A CB  1 
ATOM   50   O  OG  A SER   A  1 31  ? -29.508 12.435  6.458  0.30 35.94  ? 6    SER   A OG  1 
ATOM   51   O  OG  B SER   A  1 31  ? -27.853 13.877  6.712  0.70 42.46  ? 6    SER   A OG  1 
ATOM   52   N  N   . SER   A  1 32  ? -28.929 11.512  3.009  1.00 26.39  ? 7    SER   A N   1 
ATOM   53   C  CA  . SER   A  1 32  ? -29.695 10.556  2.213  1.00 32.77  ? 7    SER   A CA  1 
ATOM   54   C  C   . SER   A  1 32  ? -28.866 9.325   1.872  1.00 24.15  ? 7    SER   A C   1 
ATOM   55   O  O   . SER   A  1 32  ? -29.364 8.195   1.937  1.00 25.76  ? 7    SER   A O   1 
ATOM   56   C  CB  . SER   A  1 32  ? -30.211 11.226  0.940  1.00 29.10  ? 7    SER   A CB  1 
ATOM   57   O  OG  . SER   A  1 32  ? -31.108 12.279  1.249  1.00 40.31  ? 7    SER   A OG  1 
ATOM   58   N  N   . VAL   A  1 33  ? -27.599 9.524   1.503  1.00 21.11  ? 8    VAL   A N   1 
ATOM   59   C  CA  . VAL   A  1 33  ? -26.729 8.395   1.185  1.00 19.73  ? 8    VAL   A CA  1 
ATOM   60   C  C   . VAL   A  1 33  ? -26.510 7.536   2.424  1.00 35.26  ? 8    VAL   A C   1 
ATOM   61   O  O   . VAL   A  1 33  ? -26.636 6.306   2.380  1.00 21.39  ? 8    VAL   A O   1 
ATOM   62   C  CB  . VAL   A  1 33  ? -25.396 8.895   0.600  1.00 29.93  ? 8    VAL   A CB  1 
ATOM   63   C  CG1 . VAL   A  1 33  ? -24.403 7.751   0.484  1.00 19.76  ? 8    VAL   A CG1 1 
ATOM   64   C  CG2 . VAL   A  1 33  ? -25.627 9.544   -0.752 1.00 26.11  ? 8    VAL   A CG2 1 
ATOM   65   N  N   . TYR   A  1 34  ? -26.156 8.173   3.543  1.00 26.16  ? 9    TYR   A N   1 
ATOM   66   C  CA  . TYR   A  1 34  ? -25.943 7.443   4.789  1.00 24.64  ? 9    TYR   A CA  1 
ATOM   67   C  C   . TYR   A  1 34  ? -27.186 6.652   5.182  1.00 19.96  ? 9    TYR   A C   1 
ATOM   68   O  O   . TYR   A  1 34  ? -27.102 5.464   5.514  1.00 17.73  ? 9    TYR   A O   1 
ATOM   69   C  CB  . TYR   A  1 34  ? -25.554 8.420   5.900  1.00 33.90  ? 9    TYR   A CB  1 
ATOM   70   C  CG  . TYR   A  1 34  ? -25.608 7.833   7.292  1.00 27.33  ? 9    TYR   A CG  1 
ATOM   71   C  CD1 . TYR   A  1 34  ? -24.777 6.782   7.659  1.00 24.84  ? 9    TYR   A CD1 1 
ATOM   72   C  CD2 . TYR   A  1 34  ? -26.498 8.325   8.238  1.00 23.51  ? 9    TYR   A CD2 1 
ATOM   73   C  CE1 . TYR   A  1 34  ? -24.828 6.241   8.930  1.00 21.53  ? 9    TYR   A CE1 1 
ATOM   74   C  CE2 . TYR   A  1 34  ? -26.556 7.791   9.512  1.00 23.08  ? 9    TYR   A CE2 1 
ATOM   75   C  CZ  . TYR   A  1 34  ? -25.720 6.749   9.852  1.00 25.80  ? 9    TYR   A CZ  1 
ATOM   76   O  OH  . TYR   A  1 34  ? -25.770 6.217   11.119 1.00 27.10  ? 9    TYR   A OH  1 
ATOM   77   N  N   . ILE   A  1 35  ? -28.354 7.299   5.143  1.00 22.96  ? 10   ILE   A N   1 
ATOM   78   C  CA  . ILE   A  1 35  ? -29.592 6.650   5.568  1.00 22.21  ? 10   ILE   A CA  1 
ATOM   79   C  C   . ILE   A  1 35  ? -29.954 5.504   4.631  1.00 24.71  ? 10   ILE   A C   1 
ATOM   80   O  O   . ILE   A  1 35  ? -30.380 4.432   5.078  1.00 20.19  ? 10   ILE   A O   1 
ATOM   81   C  CB  . ILE   A  1 35  ? -30.729 7.683   5.678  1.00 24.92  ? 10   ILE   A CB  1 
ATOM   82   C  CG1 . ILE   A  1 35  ? -30.455 8.650   6.832  1.00 29.30  ? 10   ILE   A CG1 1 
ATOM   83   C  CG2 . ILE   A  1 35  ? -32.071 6.993   5.866  1.00 23.49  ? 10   ILE   A CG2 1 
ATOM   84   C  CD1 . ILE   A  1 35  ? -31.455 9.780   6.934  1.00 33.11  ? 10   ILE   A CD1 1 
ATOM   85   N  N   . THR   A  1 36  ? -29.797 5.706   3.320  1.00 21.22  ? 11   THR   A N   1 
ATOM   86   C  CA  . THR   A  1 36  ? -30.126 4.648   2.370  1.00 23.35  ? 11   THR   A CA  1 
ATOM   87   C  C   . THR   A  1 36  ? -29.241 3.427   2.583  1.00 21.58  ? 11   THR   A C   1 
ATOM   88   O  O   . THR   A  1 36  ? -29.720 2.287   2.542  1.00 20.59  ? 11   THR   A O   1 
ATOM   89   C  CB  . THR   A  1 36  ? -29.984 5.163   0.936  1.00 21.43  ? 11   THR   A CB  1 
ATOM   90   O  OG1 . THR   A  1 36  ? -30.816 6.315   0.754  1.00 18.90  ? 11   THR   A OG1 1 
ATOM   91   C  CG2 . THR   A  1 36  ? -30.389 4.089   -0.060 1.00 18.58  ? 11   THR   A CG2 1 
ATOM   92   N  N   . VAL   A  1 37  ? -27.944 3.646   2.808  1.00 20.17  ? 12   VAL   A N   1 
ATOM   93   C  CA  . VAL   A  1 37  ? -27.033 2.535   3.068  1.00 19.91  ? 12   VAL   A CA  1 
ATOM   94   C  C   . VAL   A  1 37  ? -27.425 1.815   4.354  1.00 28.50  ? 12   VAL   A C   1 
ATOM   95   O  O   . VAL   A  1 37  ? -27.436 0.579   4.413  1.00 18.65  ? 12   VAL   A O   1 
ATOM   96   C  CB  . VAL   A  1 37  ? -25.579 3.039   3.116  1.00 18.07  ? 12   VAL   A CB  1 
ATOM   97   C  CG1 . VAL   A  1 37  ? -24.664 1.985   3.721  1.00 14.73  ? 12   VAL   A CG1 1 
ATOM   98   C  CG2 . VAL   A  1 37  ? -25.107 3.425   1.722  1.00 22.37  ? 12   VAL   A CG2 1 
ATOM   99   N  N   . GLU   A  1 38  ? -27.753 2.577   5.403  1.00 17.60  ? 13   GLU   A N   1 
ATOM   100  C  CA  . GLU   A  1 38  ? -28.154 1.971   6.671  1.00 18.24  ? 13   GLU   A CA  1 
ATOM   101  C  C   . GLU   A  1 38  ? -29.392 1.100   6.502  1.00 16.95  ? 13   GLU   A C   1 
ATOM   102  O  O   . GLU   A  1 38  ? -29.457 -0.018  7.026  1.00 23.86  ? 13   GLU   A O   1 
ATOM   103  C  CB  . GLU   A  1 38  ? -28.412 3.062   7.711  1.00 20.06  ? 13   GLU   A CB  1 
ATOM   104  C  CG  . GLU   A  1 38  ? -27.168 3.754   8.233  1.00 22.34  ? 13   GLU   A CG  1 
ATOM   105  C  CD  . GLU   A  1 38  ? -26.503 2.992   9.363  1.00 34.03  ? 13   GLU   A CD  1 
ATOM   106  O  OE1 . GLU   A  1 38  ? -26.180 1.799   9.178  1.00 33.28  ? 13   GLU   A OE1 1 
ATOM   107  O  OE2 . GLU   A  1 38  ? -26.306 3.591   10.441 1.00 28.77  ? 13   GLU   A OE2 1 
ATOM   108  N  N   . LEU   A  1 39  ? -30.394 1.605   5.778  1.00 19.11  ? 14   LEU   A N   1 
ATOM   109  C  CA  . LEU   A  1 39  ? -31.608 0.827   5.551  1.00 18.47  ? 14   LEU   A CA  1 
ATOM   110  C  C   . LEU   A  1 39  ? -31.312 -0.437  4.754  1.00 16.05  ? 14   LEU   A C   1 
ATOM   111  O  O   . LEU   A  1 39  ? -31.877 -1.501  5.034  1.00 20.77  ? 14   LEU   A O   1 
ATOM   112  C  CB  . LEU   A  1 39  ? -32.663 1.685   4.854  1.00 27.14  ? 14   LEU   A CB  1 
ATOM   113  C  CG  . LEU   A  1 39  ? -33.208 2.814   5.733  1.00 25.74  ? 14   LEU   A CG  1 
ATOM   114  C  CD1 . LEU   A  1 39  ? -34.126 3.734   4.943  1.00 30.49  ? 14   LEU   A CD1 1 
ATOM   115  C  CD2 . LEU   A  1 39  ? -33.924 2.245   6.951  1.00 29.28  ? 14   LEU   A CD2 1 
ATOM   116  N  N   . ALA   A  1 40  ? -30.436 -0.339  3.751  1.00 18.60  ? 15   ALA   A N   1 
ATOM   117  C  CA  . ALA   A  1 40  ? -30.032 -1.528  3.007  1.00 18.99  ? 15   ALA   A CA  1 
ATOM   118  C  C   . ALA   A  1 40  ? -29.372 -2.548  3.925  1.00 19.26  ? 15   ALA   A C   1 
ATOM   119  O  O   . ALA   A  1 40  ? -29.628 -3.753  3.814  1.00 20.46  ? 15   ALA   A O   1 
ATOM   120  C  CB  . ALA   A  1 40  ? -29.092 -1.140  1.866  1.00 20.07  ? 15   ALA   A CB  1 
ATOM   121  N  N   . ILE   A  1 41  ? -28.519 -2.084  4.841  1.00 19.92  ? 16   ILE   A N   1 
ATOM   122  C  CA  . ILE   A  1 41  ? -27.859 -2.996  5.769  1.00 19.85  ? 16   ILE   A CA  1 
ATOM   123  C  C   . ILE   A  1 41  ? -28.882 -3.632  6.702  1.00 20.88  ? 16   ILE   A C   1 
ATOM   124  O  O   . ILE   A  1 41  ? -28.806 -4.829  7.008  1.00 19.31  ? 16   ILE   A O   1 
ATOM   125  C  CB  . ILE   A  1 41  ? -26.754 -2.259  6.549  1.00 19.34  ? 16   ILE   A CB  1 
ATOM   126  C  CG1 . ILE   A  1 41  ? -25.619 -1.853  5.607  1.00 22.38  ? 16   ILE   A CG1 1 
ATOM   127  C  CG2 . ILE   A  1 41  ? -26.226 -3.124  7.685  1.00 20.62  ? 16   ILE   A CG2 1 
ATOM   128  C  CD1 . ILE   A  1 41  ? -24.647 -0.868  6.217  1.00 23.65  ? 16   ILE   A CD1 1 
ATOM   129  N  N   . ALA   A  1 42  ? -29.853 -2.841  7.169  1.00 16.81  ? 17   ALA   A N   1 
ATOM   130  C  CA  . ALA   A  1 42  ? -30.863 -3.357  8.088  1.00 17.52  ? 17   ALA   A CA  1 
ATOM   131  C  C   . ALA   A  1 42  ? -31.672 -4.478  7.450  1.00 22.99  ? 17   ALA   A C   1 
ATOM   132  O  O   . ALA   A  1 42  ? -31.962 -5.490  8.099  1.00 26.69  ? 17   ALA   A O   1 
ATOM   133  C  CB  . ALA   A  1 42  ? -31.784 -2.226  8.543  1.00 11.10  ? 17   ALA   A CB  1 
ATOM   134  N  N   . VAL   A  1 43  ? -32.047 -4.315  6.179  1.00 26.00  ? 18   VAL   A N   1 
ATOM   135  C  CA  . VAL   A  1 43  ? -32.801 -5.355  5.483  1.00 22.28  ? 18   VAL   A CA  1 
ATOM   136  C  C   . VAL   A  1 43  ? -31.998 -6.647  5.433  1.00 15.91  ? 18   VAL   A C   1 
ATOM   137  O  O   . VAL   A  1 43  ? -32.511 -7.733  5.730  1.00 19.68  ? 18   VAL   A O   1 
ATOM   138  C  CB  . VAL   A  1 43  ? -33.189 -4.882  4.070  1.00 23.58  ? 18   VAL   A CB  1 
ATOM   139  C  CG1 . VAL   A  1 43  ? -33.803 -6.025  3.276  1.00 19.44  ? 18   VAL   A CG1 1 
ATOM   140  C  CG2 . VAL   A  1 43  ? -34.145 -3.703  4.146  1.00 20.73  ? 18   VAL   A CG2 1 
ATOM   141  N  N   . LEU   A  1 44  ? -30.718 -6.547  5.069  1.00 18.19  ? 19   LEU   A N   1 
ATOM   142  C  CA  . LEU   A  1 44  ? -29.896 -7.742  4.923  1.00 21.72  ? 19   LEU   A CA  1 
ATOM   143  C  C   . LEU   A  1 44  ? -29.628 -8.401  6.271  1.00 23.62  ? 19   LEU   A C   1 
ATOM   144  O  O   . LEU   A  1 44  ? -29.566 -9.633  6.363  1.00 20.84  ? 19   LEU   A O   1 
ATOM   145  C  CB  . LEU   A  1 44  ? -28.582 -7.386  4.230  1.00 13.65  ? 19   LEU   A CB  1 
ATOM   146  C  CG  . LEU   A  1 44  ? -28.692 -6.937  2.770  1.00 28.51  ? 19   LEU   A CG  1 
ATOM   147  C  CD1 . LEU   A  1 44  ? -27.394 -6.293  2.305  1.00 22.30  ? 19   LEU   A CD1 1 
ATOM   148  C  CD2 . LEU   A  1 44  ? -29.071 -8.104  1.870  1.00 29.13  ? 19   LEU   A CD2 1 
ATOM   149  N  N   . ALA   A  1 45  ? -29.457 -7.599  7.324  1.00 23.32  ? 20   ALA   A N   1 
ATOM   150  C  CA  . ALA   A  1 45  ? -29.228 -8.158  8.653  1.00 27.41  ? 20   ALA   A CA  1 
ATOM   151  C  C   . ALA   A  1 45  ? -30.436 -8.949  9.142  1.00 23.70  ? 20   ALA   A C   1 
ATOM   152  O  O   . ALA   A  1 45  ? -30.285 -10.028 9.728  1.00 23.61  ? 20   ALA   A O   1 
ATOM   153  C  CB  . ALA   A  1 45  ? -28.884 -7.043  9.639  1.00 16.70  ? 20   ALA   A CB  1 
ATOM   154  N  N   . ILE   A  1 46  ? -31.641 -8.426  8.915  1.00 21.27  ? 21   ILE   A N   1 
ATOM   155  C  CA  . ILE   A  1 46  ? -32.853 -9.132  9.321  1.00 19.42  ? 21   ILE   A CA  1 
ATOM   156  C  C   . ILE   A  1 46  ? -33.015 -10.429 8.535  1.00 27.01  ? 21   ILE   A C   1 
ATOM   157  O  O   . ILE   A  1 46  ? -33.211 -11.502 9.116  1.00 25.99  ? 21   ILE   A O   1 
ATOM   158  C  CB  . ILE   A  1 46  ? -34.083 -8.219  9.171  1.00 22.25  ? 21   ILE   A CB  1 
ATOM   159  C  CG1 . ILE   A  1 46  ? -33.974 -7.029  10.128 1.00 19.34  ? 21   ILE   A CG1 1 
ATOM   160  C  CG2 . ILE   A  1 46  ? -35.364 -8.997  9.429  1.00 28.06  ? 21   ILE   A CG2 1 
ATOM   161  C  CD1 . ILE   A  1 46  ? -34.939 -5.904  9.823  1.00 18.50  ? 21   ILE   A CD1 1 
ATOM   162  N  N   . LEU   A  1 47  ? -32.929 -10.352 7.204  1.00 23.61  ? 22   LEU   A N   1 
ATOM   163  C  CA  . LEU   A  1 47  ? -33.205 -11.524 6.375  1.00 21.35  ? 22   LEU   A CA  1 
ATOM   164  C  C   . LEU   A  1 47  ? -32.222 -12.653 6.656  1.00 22.96  ? 22   LEU   A C   1 
ATOM   165  O  O   . LEU   A  1 47  ? -32.621 -13.813 6.813  1.00 27.80  ? 22   LEU   A O   1 
ATOM   166  C  CB  . LEU   A  1 47  ? -33.164 -11.143 4.895  1.00 24.83  ? 22   LEU   A CB  1 
ATOM   167  C  CG  . LEU   A  1 47  ? -34.295 -10.266 4.362  1.00 32.24  ? 22   LEU   A CG  1 
ATOM   168  C  CD1 . LEU   A  1 47  ? -34.043 -9.915  2.906  1.00 29.14  ? 22   LEU   A CD1 1 
ATOM   169  C  CD2 . LEU   A  1 47  ? -35.631 -10.971 4.525  1.00 35.37  ? 22   LEU   A CD2 1 
ATOM   170  N  N   . GLY   A  1 48  ? -30.928 -12.336 6.721  1.00 18.98  ? 23   GLY   A N   1 
ATOM   171  C  CA  . GLY   A  1 48  ? -29.938 -13.386 6.890  1.00 20.69  ? 23   GLY   A CA  1 
ATOM   172  C  C   . GLY   A  1 48  ? -30.021 -14.065 8.243  1.00 26.25  ? 23   GLY   A C   1 
ATOM   173  O  O   . GLY   A  1 48  ? -29.894 -15.288 8.344  1.00 24.11  ? 23   GLY   A O   1 
ATOM   174  N  N   . ASN   A  1 49  ? -30.236 -13.284 9.302  1.00 18.00  ? 24   ASN   A N   1 
ATOM   175  C  CA  . ASN   A  1 49  ? -30.228 -13.849 10.645 1.00 27.01  ? 24   ASN   A CA  1 
ATOM   176  C  C   . ASN   A  1 49  ? -31.561 -14.483 11.026 1.00 23.12  ? 24   ASN   A C   1 
ATOM   177  O  O   . ASN   A  1 49  ? -31.583 -15.411 11.843 1.00 21.76  ? 24   ASN   A O   1 
ATOM   178  C  CB  . ASN   A  1 49  ? -29.827 -12.775 11.655 1.00 20.31  ? 24   ASN   A CB  1 
ATOM   179  C  CG  . ASN   A  1 49  ? -28.351 -12.435 11.577 1.00 25.68  ? 24   ASN   A CG  1 
ATOM   180  O  OD1 . ASN   A  1 49  ? -27.498 -13.240 11.950 1.00 24.67  ? 24   ASN   A OD1 1 
ATOM   181  N  ND2 . ASN   A  1 49  ? -28.042 -11.252 11.061 1.00 23.23  ? 24   ASN   A ND2 1 
ATOM   182  N  N   . VAL   A  1 50  ? -32.678 -14.002 10.469 1.00 23.45  ? 25   VAL   A N   1 
ATOM   183  C  CA  . VAL   A  1 50  ? -33.919 -14.769 10.550 1.00 29.50  ? 25   VAL   A CA  1 
ATOM   184  C  C   . VAL   A  1 50  ? -33.728 -16.151 9.939  1.00 27.02  ? 25   VAL   A C   1 
ATOM   185  O  O   . VAL   A  1 50  ? -34.196 -17.159 10.483 1.00 27.66  ? 25   VAL   A O   1 
ATOM   186  C  CB  . VAL   A  1 50  ? -35.071 -14.003 9.873  1.00 31.40  ? 25   VAL   A CB  1 
ATOM   187  C  CG1 . VAL   A  1 50  ? -36.220 -14.943 9.534  1.00 29.86  ? 25   VAL   A CG1 1 
ATOM   188  C  CG2 . VAL   A  1 50  ? -35.562 -12.878 10.774 1.00 25.04  ? 25   VAL   A CG2 1 
ATOM   189  N  N   . LEU   A  1 51  ? -33.027 -16.220 8.805  1.00 25.07  ? 26   LEU   A N   1 
ATOM   190  C  CA  . LEU   A  1 51  ? -32.774 -17.508 8.167  1.00 24.77  ? 26   LEU   A CA  1 
ATOM   191  C  C   . LEU   A  1 51  ? -31.936 -18.411 9.065  1.00 26.80  ? 26   LEU   A C   1 
ATOM   192  O  O   . LEU   A  1 51  ? -32.152 -19.627 9.111  1.00 26.94  ? 26   LEU   A O   1 
ATOM   193  C  CB  . LEU   A  1 51  ? -32.101 -17.297 6.811  1.00 26.85  ? 26   LEU   A CB  1 
ATOM   194  C  CG  . LEU   A  1 51  ? -31.973 -18.530 5.916  1.00 50.85  ? 26   LEU   A CG  1 
ATOM   195  C  CD1 . LEU   A  1 51  ? -33.352 -19.064 5.562  1.00 40.14  ? 26   LEU   A CD1 1 
ATOM   196  C  CD2 . LEU   A  1 51  ? -31.212 -18.176 4.654  1.00 48.96  ? 26   LEU   A CD2 1 
ATOM   197  N  N   . VAL   A  1 52  ? -30.958 -17.833 9.770  1.00 22.98  ? 27   VAL   A N   1 
ATOM   198  C  CA  . VAL   A  1 52  ? -30.170 -18.602 10.731 1.00 21.64  ? 27   VAL   A CA  1 
ATOM   199  C  C   . VAL   A  1 52  ? -31.075 -19.195 11.804 1.00 31.21  ? 27   VAL   A C   1 
ATOM   200  O  O   . VAL   A  1 52  ? -31.008 -20.393 12.105 1.00 25.15  ? 27   VAL   A O   1 
ATOM   201  C  CB  . VAL   A  1 52  ? -29.061 -17.729 11.346 1.00 26.58  ? 27   VAL   A CB  1 
ATOM   202  C  CG1 . VAL   A  1 52  ? -28.487 -18.395 12.592 1.00 18.28  ? 27   VAL   A CG1 1 
ATOM   203  C  CG2 . VAL   A  1 52  ? -27.961 -17.478 10.329 1.00 25.05  ? 27   VAL   A CG2 1 
ATOM   204  N  N   . CYS   A  1 53  ? -31.930 -18.362 12.405 1.00 19.62  ? 28   CYS   A N   1 
ATOM   205  C  CA  . CYS   A  1 53  ? -32.787 -18.843 13.483 1.00 32.86  ? 28   CYS   A CA  1 
ATOM   206  C  C   . CYS   A  1 53  ? -33.762 -19.897 12.975 1.00 34.16  ? 28   CYS   A C   1 
ATOM   207  O  O   . CYS   A  1 53  ? -34.035 -20.887 13.664 1.00 33.35  ? 28   CYS   A O   1 
ATOM   208  C  CB  . CYS   A  1 53  ? -33.545 -17.673 14.110 1.00 33.30  ? 28   CYS   A CB  1 
ATOM   209  S  SG  . CYS   A  1 53  ? -32.499 -16.466 14.954 1.00 31.33  ? 28   CYS   A SG  1 
ATOM   210  N  N   . TRP   A  1 54  ? -34.311 -19.689 11.776 1.00 32.25  ? 29   TRP   A N   1 
ATOM   211  C  CA  . TRP   A  1 54  ? -35.228 -20.663 11.193 1.00 31.47  ? 29   TRP   A CA  1 
ATOM   212  C  C   . TRP   A  1 54  ? -34.543 -22.009 10.991 1.00 32.38  ? 29   TRP   A C   1 
ATOM   213  O  O   . TRP   A  1 54  ? -35.136 -23.063 11.251 1.00 32.88  ? 29   TRP   A O   1 
ATOM   214  C  CB  . TRP   A  1 54  ? -35.805 -20.138 9.879  1.00 31.22  ? 29   TRP   A CB  1 
ATOM   215  C  CG  . TRP   A  1 54  ? -37.204 -19.610 10.028 1.00 54.57  ? 29   TRP   A CG  1 
ATOM   216  C  CD1 . TRP   A  1 54  ? -37.625 -18.329 9.819  1.00 66.49  ? 29   TRP   A CD1 1 
ATOM   217  C  CD2 . TRP   A  1 54  ? -38.364 -20.351 10.433 1.00 69.80  ? 29   TRP   A CD2 1 
ATOM   218  N  NE1 . TRP   A  1 54  ? -38.974 -18.227 10.062 1.00 73.11  ? 29   TRP   A NE1 1 
ATOM   219  C  CE2 . TRP   A  1 54  ? -39.451 -19.454 10.440 1.00 81.71  ? 29   TRP   A CE2 1 
ATOM   220  C  CE3 . TRP   A  1 54  ? -38.590 -21.686 10.787 1.00 68.68  ? 29   TRP   A CE3 1 
ATOM   221  C  CZ2 . TRP   A  1 54  ? -40.742 -19.848 10.787 1.00 62.83  ? 29   TRP   A CZ2 1 
ATOM   222  C  CZ3 . TRP   A  1 54  ? -39.872 -22.074 11.131 1.00 68.60  ? 29   TRP   A CZ3 1 
ATOM   223  C  CH2 . TRP   A  1 54  ? -40.931 -21.159 11.127 1.00 64.13  ? 29   TRP   A CH2 1 
ATOM   224  N  N   . ALA   A  1 55  ? -33.293 -21.989 10.519 1.00 25.74  ? 30   ALA   A N   1 
ATOM   225  C  CA  . ALA   A  1 55  ? -32.551 -23.227 10.297 1.00 27.45  ? 30   ALA   A CA  1 
ATOM   226  C  C   . ALA   A  1 55  ? -32.353 -23.996 11.597 1.00 34.98  ? 30   ALA   A C   1 
ATOM   227  O  O   . ALA   A  1 55  ? -32.541 -25.217 11.641 1.00 28.78  ? 30   ALA   A O   1 
ATOM   228  C  CB  . ALA   A  1 55  ? -31.204 -22.915 9.643  1.00 22.90  ? 30   ALA   A CB  1 
ATOM   229  N  N   . VAL   A  1 56  ? -31.959 -23.303 12.668 1.00 31.20  ? 31   VAL   A N   1 
ATOM   230  C  CA  . VAL   A  1 56  ? -31.751 -23.991 13.940 1.00 21.16  ? 31   VAL   A CA  1 
ATOM   231  C  C   . VAL   A  1 56  ? -33.073 -24.565 14.433 1.00 33.80  ? 31   VAL   A C   1 
ATOM   232  O  O   . VAL   A  1 56  ? -33.132 -25.698 14.925 1.00 25.72  ? 31   VAL   A O   1 
ATOM   233  C  CB  . VAL   A  1 56  ? -31.104 -23.042 14.967 1.00 29.29  ? 31   VAL   A CB  1 
ATOM   234  C  CG1 . VAL   A  1 56  ? -30.926 -23.745 16.304 1.00 27.01  ? 31   VAL   A CG1 1 
ATOM   235  C  CG2 . VAL   A  1 56  ? -29.762 -22.548 14.448 1.00 24.55  ? 31   VAL   A CG2 1 
ATOM   236  N  N   . TRP   A  1 57  ? -34.151 -23.784 14.319 1.00 27.95  ? 32   TRP   A N   1 
ATOM   237  C  CA  . TRP   A  1 57  ? -35.475 -24.259 14.712 1.00 41.66  ? 32   TRP   A CA  1 
ATOM   238  C  C   . TRP   A  1 57  ? -35.904 -25.502 13.938 1.00 39.02  ? 32   TRP   A C   1 
ATOM   239  O  O   . TRP   A  1 57  ? -36.495 -26.422 14.516 1.00 43.80  ? 32   TRP   A O   1 
ATOM   240  C  CB  . TRP   A  1 57  ? -36.502 -23.129 14.559 1.00 38.43  ? 32   TRP   A CB  1 
ATOM   241  C  CG  . TRP   A  1 57  ? -37.915 -23.584 14.786 1.00 57.94  ? 32   TRP   A CG  1 
ATOM   242  C  CD1 . TRP   A  1 57  ? -38.688 -24.252 13.879 1.00 58.72  ? 32   TRP   A CD1 1 
ATOM   243  C  CD2 . TRP   A  1 57  ? -38.678 -23.546 16.003 1.00 52.11  ? 32   TRP   A CD2 1 
ATOM   244  N  NE1 . TRP   A  1 57  ? -39.903 -24.560 14.421 1.00 58.55  ? 32   TRP   A NE1 1 
ATOM   245  C  CE2 . TRP   A  1 57  ? -39.922 -24.152 15.728 1.00 57.90  ? 32   TRP   A CE2 1 
ATOM   246  C  CE3 . TRP   A  1 57  ? -38.445 -23.036 17.284 1.00 73.12  ? 32   TRP   A CE3 1 
ATOM   247  C  CZ2 . TRP   A  1 57  ? -40.927 -24.263 16.684 1.00 65.98  ? 32   TRP   A CZ2 1 
ATOM   248  C  CZ3 . TRP   A  1 57  ? -39.453 -23.147 18.235 1.00 80.46  ? 32   TRP   A CZ3 1 
ATOM   249  C  CH2 . TRP   A  1 57  ? -40.677 -23.756 17.927 1.00 73.77  ? 32   TRP   A CH2 1 
ATOM   250  N  N   . LEU   A  1 58  ? -35.617 -25.560 12.639 1.00 37.96  ? 33   LEU   A N   1 
ATOM   251  C  CA  . LEU   A  1 58  ? -36.174 -26.640 11.831 1.00 46.47  ? 33   LEU   A CA  1 
ATOM   252  C  C   . LEU   A  1 58  ? -35.355 -27.923 11.900 1.00 46.24  ? 33   LEU   A C   1 
ATOM   253  O  O   . LEU   A  1 58  ? -35.929 -29.016 11.860 1.00 52.84  ? 33   LEU   A O   1 
ATOM   254  C  CB  . LEU   A  1 58  ? -36.318 -26.184 10.379 1.00 47.04  ? 33   LEU   A CB  1 
ATOM   255  C  CG  . LEU   A  1 58  ? -37.482 -25.219 10.140 1.00 44.90  ? 33   LEU   A CG  1 
ATOM   256  C  CD1 . LEU   A  1 58  ? -37.568 -24.841 8.674  1.00 59.37  ? 33   LEU   A CD1 1 
ATOM   257  C  CD2 . LEU   A  1 58  ? -38.796 -25.821 10.623 1.00 42.50  ? 33   LEU   A CD2 1 
ATOM   258  N  N   . ASN   A  1 59  ? -34.034 -27.824 12.016 1.00 34.58  ? 34   ASN   A N   1 
ATOM   259  C  CA  . ASN   A  1 59  ? -33.146 -28.971 11.856 1.00 36.06  ? 34   ASN   A CA  1 
ATOM   260  C  C   . ASN   A  1 59  ? -32.603 -29.376 13.223 1.00 46.23  ? 34   ASN   A C   1 
ATOM   261  O  O   . ASN   A  1 59  ? -31.860 -28.615 13.853 1.00 34.88  ? 34   ASN   A O   1 
ATOM   262  C  CB  . ASN   A  1 59  ? -32.017 -28.631 10.883 1.00 38.47  ? 34   ASN   A CB  1 
ATOM   263  C  CG  . ASN   A  1 59  ? -31.147 -29.830 10.543 1.00 43.94  ? 34   ASN   A CG  1 
ATOM   264  O  OD1 . ASN   A  1 59  ? -31.266 -30.898 11.144 1.00 45.51  ? 34   ASN   A OD1 1 
ATOM   265  N  ND2 . ASN   A  1 59  ? -30.264 -29.654 9.566  1.00 29.77  ? 34   ASN   A ND2 1 
ATOM   266  N  N   A SER   A  1 60  ? -32.972 -30.579 13.672 0.61 40.59  ? 35   SER   A N   1 
ATOM   267  N  N   B SER   A  1 60  ? -32.971 -30.578 13.675 0.39 40.59  ? 35   SER   A N   1 
ATOM   268  C  CA  A SER   A  1 60  ? -32.493 -31.085 14.953 0.61 39.38  ? 35   SER   A CA  1 
ATOM   269  C  CA  B SER   A  1 60  ? -32.489 -31.076 14.958 0.39 39.37  ? 35   SER   A CA  1 
ATOM   270  C  C   A SER   A  1 60  ? -30.995 -31.358 14.945 0.61 36.33  ? 35   SER   A C   1 
ATOM   271  C  C   B SER   A  1 60  ? -30.992 -31.355 14.946 0.39 36.41  ? 35   SER   A C   1 
ATOM   272  O  O   A SER   A  1 60  ? -30.382 -31.419 16.016 0.61 41.39  ? 35   SER   A O   1 
ATOM   273  O  O   B SER   A  1 60  ? -30.377 -31.416 16.016 0.39 41.32  ? 35   SER   A O   1 
ATOM   274  C  CB  A SER   A  1 60  ? -33.252 -32.358 15.334 0.61 41.38  ? 35   SER   A CB  1 
ATOM   275  C  CB  B SER   A  1 60  ? -33.251 -32.341 15.354 0.39 41.33  ? 35   SER   A CB  1 
ATOM   276  O  OG  A SER   A  1 60  ? -32.825 -33.460 14.552 0.61 41.50  ? 35   SER   A OG  1 
ATOM   277  O  OG  B SER   A  1 60  ? -34.555 -32.025 15.812 0.39 37.23  ? 35   SER   A OG  1 
ATOM   278  N  N   . ASN   A  1 61  ? -30.394 -31.528 13.764 1.00 27.28  ? 36   ASN   A N   1 
ATOM   279  C  CA  . ASN   A  1 61  ? -28.947 -31.684 13.676 1.00 30.11  ? 36   ASN   A CA  1 
ATOM   280  C  C   . ASN   A  1 61  ? -28.216 -30.392 14.017 1.00 42.17  ? 36   ASN   A C   1 
ATOM   281  O  O   . ASN   A  1 61  ? -27.011 -30.425 14.287 1.00 38.09  ? 36   ASN   A O   1 
ATOM   282  C  CB  . ASN   A  1 61  ? -28.548 -32.158 12.278 1.00 46.16  ? 36   ASN   A CB  1 
ATOM   283  C  CG  . ASN   A  1 61  ? -29.017 -33.570 11.987 1.00 53.07  ? 36   ASN   A CG  1 
ATOM   284  O  OD1 . ASN   A  1 61  ? -29.276 -34.350 12.903 1.00 59.81  ? 36   ASN   A OD1 1 
ATOM   285  N  ND2 . ASN   A  1 61  ? -29.130 -33.905 10.707 1.00 54.86  ? 36   ASN   A ND2 1 
ATOM   286  N  N   . LEU   A  1 62  ? -28.919 -29.261 14.007 1.00 30.55  ? 37   LEU   A N   1 
ATOM   287  C  CA  . LEU   A  1 62  ? -28.351 -27.968 14.357 1.00 38.42  ? 37   LEU   A CA  1 
ATOM   288  C  C   . LEU   A  1 62  ? -28.692 -27.545 15.778 1.00 34.66  ? 37   LEU   A C   1 
ATOM   289  O  O   . LEU   A  1 62  ? -28.275 -26.465 16.205 1.00 32.03  ? 37   LEU   A O   1 
ATOM   290  C  CB  . LEU   A  1 62  ? -28.826 -26.894 13.372 1.00 26.56  ? 37   LEU   A CB  1 
ATOM   291  C  CG  . LEU   A  1 62  ? -28.287 -26.984 11.942 1.00 37.44  ? 37   LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A  1 62  ? -29.035 -26.024 11.027 1.00 28.72  ? 37   LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A  1 62  ? -26.792 -26.707 11.911 1.00 27.97  ? 37   LEU   A CD2 1 
ATOM   294  N  N   . GLN   A  1 63  ? -29.441 -28.363 16.518 1.00 36.65  ? 38   GLN   A N   1 
ATOM   295  C  CA  . GLN   A  1 63  ? -29.890 -28.007 17.864 1.00 36.29  ? 38   GLN   A CA  1 
ATOM   296  C  C   . GLN   A  1 63  ? -28.892 -28.588 18.859 1.00 38.08  ? 38   GLN   A C   1 
ATOM   297  O  O   . GLN   A  1 63  ? -29.029 -29.717 19.333 1.00 45.06  ? 38   GLN   A O   1 
ATOM   298  C  CB  . GLN   A  1 63  ? -31.312 -28.495 18.115 1.00 38.48  ? 38   GLN   A CB  1 
ATOM   299  C  CG  . GLN   A  1 63  ? -32.348 -27.823 17.224 1.00 36.79  ? 38   GLN   A CG  1 
ATOM   300  C  CD  . GLN   A  1 63  ? -33.693 -28.522 17.246 1.00 48.72  ? 38   GLN   A CD  1 
ATOM   301  O  OE1 . GLN   A  1 63  ? -33.901 -29.474 17.997 1.00 47.14  ? 38   GLN   A OE1 1 
ATOM   302  N  NE2 . GLN   A  1 63  ? -34.619 -28.044 16.422 1.00 32.93  ? 38   GLN   A NE2 1 
ATOM   303  N  N   . ASN   A  1 64  ? -27.872 -27.791 19.169 1.00 38.75  ? 39   ASN   A N   1 
ATOM   304  C  CA  . ASN   A  1 64  ? -26.856 -28.112 20.160 1.00 36.36  ? 39   ASN   A CA  1 
ATOM   305  C  C   . ASN   A  1 64  ? -26.518 -26.831 20.910 1.00 39.80  ? 39   ASN   A C   1 
ATOM   306  O  O   . ASN   A  1 64  ? -26.950 -25.739 20.532 1.00 33.82  ? 39   ASN   A O   1 
ATOM   307  C  CB  . ASN   A  1 64  ? -25.608 -28.723 19.511 1.00 27.81  ? 39   ASN   A CB  1 
ATOM   308  C  CG  . ASN   A  1 64  ? -25.123 -27.925 18.316 1.00 50.50  ? 39   ASN   A CG  1 
ATOM   309  O  OD1 . ASN   A  1 64  ? -24.698 -26.778 18.452 1.00 50.88  ? 39   ASN   A OD1 1 
ATOM   310  N  ND2 . ASN   A  1 64  ? -25.192 -28.529 17.135 1.00 41.85  ? 39   ASN   A ND2 1 
ATOM   311  N  N   . VAL   A  1 65  ? -25.753 -26.968 21.996 1.00 34.59  ? 40   VAL   A N   1 
ATOM   312  C  CA  . VAL   A  1 65  ? -25.488 -25.813 22.852 1.00 30.94  ? 40   VAL   A CA  1 
ATOM   313  C  C   . VAL   A  1 65  ? -24.763 -24.716 22.079 1.00 28.83  ? 40   VAL   A C   1 
ATOM   314  O  O   . VAL   A  1 65  ? -25.084 -23.529 22.217 1.00 32.15  ? 40   VAL   A O   1 
ATOM   315  C  CB  . VAL   A  1 65  ? -24.697 -26.242 24.102 1.00 43.45  ? 40   VAL   A CB  1 
ATOM   316  C  CG1 . VAL   A  1 65  ? -24.120 -25.022 24.795 1.00 39.26  ? 40   VAL   A CG1 1 
ATOM   317  C  CG2 . VAL   A  1 65  ? -25.585 -27.037 25.047 1.00 32.89  ? 40   VAL   A CG2 1 
ATOM   318  N  N   . THR   A  1 66  ? -23.770 -25.092 21.265 1.00 25.24  ? 41   THR   A N   1 
ATOM   319  C  CA  . THR   A  1 66  ? -23.025 -24.109 20.477 1.00 33.94  ? 41   THR   A CA  1 
ATOM   320  C  C   . THR   A  1 66  ? -23.953 -23.226 19.655 1.00 30.40  ? 41   THR   A C   1 
ATOM   321  O  O   . THR   A  1 66  ? -23.778 -22.004 19.599 1.00 33.13  ? 41   THR   A O   1 
ATOM   322  C  CB  . THR   A  1 66  ? -22.017 -24.792 19.553 1.00 33.07  ? 41   THR   A CB  1 
ATOM   323  O  OG1 . THR   A  1 66  ? -21.533 -25.989 20.170 1.00 37.31  ? 41   THR   A OG1 1 
ATOM   324  C  CG2 . THR   A  1 66  ? -20.837 -23.859 19.266 1.00 26.80  ? 41   THR   A CG2 1 
ATOM   325  N  N   . ASN   A  1 67  ? -24.956 -23.830 19.019 1.00 26.29  ? 42   ASN   A N   1 
ATOM   326  C  CA  . ASN   A  1 67  ? -25.845 -23.084 18.139 1.00 25.13  ? 42   ASN   A CA  1 
ATOM   327  C  C   . ASN   A  1 67  ? -26.903 -22.293 18.892 1.00 31.15  ? 42   ASN   A C   1 
ATOM   328  O  O   . ASN   A  1 67  ? -27.516 -21.398 18.302 1.00 23.06  ? 42   ASN   A O   1 
ATOM   329  C  CB  . ASN   A  1 67  ? -26.505 -24.036 17.143 1.00 25.51  ? 42   ASN   A CB  1 
ATOM   330  C  CG  . ASN   A  1 67  ? -25.558 -24.457 16.032 1.00 32.21  ? 42   ASN   A CG  1 
ATOM   331  O  OD1 . ASN   A  1 67  ? -24.496 -23.860 15.851 1.00 31.53  ? 42   ASN   A OD1 1 
ATOM   332  N  ND2 . ASN   A  1 67  ? -25.934 -25.491 15.289 1.00 29.22  ? 42   ASN   A ND2 1 
ATOM   333  N  N   . TYR   A  1 68  ? -27.139 -22.597 20.170 1.00 25.28  ? 43   TYR   A N   1 
ATOM   334  C  CA  . TYR   A  1 68  ? -27.986 -21.718 20.969 1.00 31.62  ? 43   TYR   A CA  1 
ATOM   335  C  C   . TYR   A  1 68  ? -27.320 -20.363 21.172 1.00 22.73  ? 43   TYR   A C   1 
ATOM   336  O  O   . TYR   A  1 68  ? -27.995 -19.328 21.178 1.00 22.89  ? 43   TYR   A O   1 
ATOM   337  C  CB  . TYR   A  1 68  ? -28.311 -22.380 22.308 1.00 27.70  ? 43   TYR   A CB  1 
ATOM   338  C  CG  . TYR   A  1 68  ? -28.964 -23.737 22.159 1.00 48.72  ? 43   TYR   A CG  1 
ATOM   339  C  CD1 . TYR   A  1 68  ? -29.751 -24.028 21.052 1.00 44.43  ? 43   TYR   A CD1 1 
ATOM   340  C  CD2 . TYR   A  1 68  ? -28.785 -24.729 23.114 1.00 40.13  ? 43   TYR   A CD2 1 
ATOM   341  C  CE1 . TYR   A  1 68  ? -30.348 -25.262 20.902 1.00 51.90  ? 43   TYR   A CE1 1 
ATOM   342  C  CE2 . TYR   A  1 68  ? -29.377 -25.972 22.971 1.00 48.08  ? 43   TYR   A CE2 1 
ATOM   343  C  CZ  . TYR   A  1 68  ? -30.159 -26.231 21.863 1.00 57.19  ? 43   TYR   A CZ  1 
ATOM   344  O  OH  . TYR   A  1 68  ? -30.755 -27.462 21.714 1.00 51.87  ? 43   TYR   A OH  1 
ATOM   345  N  N   . PHE   A  1 69  ? -25.996 -20.349 21.341 1.00 23.13  ? 44   PHE   A N   1 
ATOM   346  C  CA  . PHE   A  1 69  ? -25.279 -19.078 21.378 1.00 22.14  ? 44   PHE   A CA  1 
ATOM   347  C  C   . PHE   A  1 69  ? -25.270 -18.418 20.003 1.00 19.15  ? 44   PHE   A C   1 
ATOM   348  O  O   . PHE   A  1 69  ? -25.321 -17.188 19.898 1.00 20.06  ? 44   PHE   A O   1 
ATOM   349  C  CB  . PHE   A  1 69  ? -23.856 -19.287 21.894 1.00 16.02  ? 44   PHE   A CB  1 
ATOM   350  C  CG  . PHE   A  1 69  ? -23.792 -19.712 23.334 1.00 28.47  ? 44   PHE   A CG  1 
ATOM   351  C  CD1 . PHE   A  1 69  ? -24.139 -18.830 24.344 1.00 22.66  ? 44   PHE   A CD1 1 
ATOM   352  C  CD2 . PHE   A  1 69  ? -23.386 -20.990 23.678 1.00 26.52  ? 44   PHE   A CD2 1 
ATOM   353  C  CE1 . PHE   A  1 69  ? -24.084 -19.216 25.671 1.00 37.87  ? 44   PHE   A CE1 1 
ATOM   354  C  CE2 . PHE   A  1 69  ? -23.329 -21.381 25.003 1.00 34.08  ? 44   PHE   A CE2 1 
ATOM   355  C  CZ  . PHE   A  1 69  ? -23.678 -20.492 26.000 1.00 26.68  ? 44   PHE   A CZ  1 
ATOM   356  N  N   . VAL   A  1 70  ? -25.185 -19.225 18.942 1.00 19.17  ? 45   VAL   A N   1 
ATOM   357  C  CA  . VAL   A  1 70  ? -25.317 -18.712 17.579 1.00 23.57  ? 45   VAL   A CA  1 
ATOM   358  C  C   . VAL   A  1 70  ? -26.671 -18.039 17.379 1.00 22.34  ? 45   VAL   A C   1 
ATOM   359  O  O   . VAL   A  1 70  ? -26.768 -16.986 16.735 1.00 23.86  ? 45   VAL   A O   1 
ATOM   360  C  CB  . VAL   A  1 70  ? -25.093 -19.845 16.559 1.00 29.33  ? 45   VAL   A CB  1 
ATOM   361  C  CG1 . VAL   A  1 70  ? -25.569 -19.426 15.174 1.00 26.89  ? 45   VAL   A CG1 1 
ATOM   362  C  CG2 . VAL   A  1 70  ? -23.627 -20.248 16.526 1.00 20.90  ? 45   VAL   A CG2 1 
ATOM   363  N  N   . VAL   A  1 71  ? -27.733 -18.619 17.943 1.00 23.01  ? 46   VAL   A N   1 
ATOM   364  C  CA  . VAL   A  1 71  ? -29.057 -18.014 17.821 1.00 13.06  ? 46   VAL   A CA  1 
ATOM   365  C  C   . VAL   A  1 71  ? -29.136 -16.719 18.620 1.00 20.06  ? 46   VAL   A C   1 
ATOM   366  O  O   . VAL   A  1 71  ? -29.681 -15.716 18.142 1.00 23.54  ? 46   VAL   A O   1 
ATOM   367  C  CB  . VAL   A  1 71  ? -30.143 -19.017 18.251 1.00 30.46  ? 46   VAL   A CB  1 
ATOM   368  C  CG1 . VAL   A  1 71  ? -31.474 -18.309 18.448 1.00 27.78  ? 46   VAL   A CG1 1 
ATOM   369  C  CG2 . VAL   A  1 71  ? -30.279 -20.119 17.214 1.00 32.90  ? 46   VAL   A CG2 1 
ATOM   370  N  N   . SER   A  1 72  ? -28.600 -16.714 19.843 1.00 19.59  ? 47   SER   A N   1 
ATOM   371  C  CA  A SER   A  1 72  ? -28.558 -15.479 20.619 0.78 23.98  ? 47   SER   A CA  1 
ATOM   372  C  CA  B SER   A  1 72  ? -28.562 -15.478 20.617 0.22 23.88  ? 47   SER   A CA  1 
ATOM   373  C  C   . SER   A  1 72  ? -27.786 -14.396 19.877 1.00 23.43  ? 47   SER   A C   1 
ATOM   374  O  O   . SER   A  1 72  ? -28.146 -13.214 19.932 1.00 20.02  ? 47   SER   A O   1 
ATOM   375  C  CB  A SER   A  1 72  ? -27.934 -15.740 21.990 0.78 20.52  ? 47   SER   A CB  1 
ATOM   376  C  CB  B SER   A  1 72  ? -27.946 -15.735 21.993 0.22 20.66  ? 47   SER   A CB  1 
ATOM   377  O  OG  A SER   A  1 72  ? -27.839 -14.544 22.743 0.78 18.16  ? 47   SER   A OG  1 
ATOM   378  O  OG  B SER   A  1 72  ? -26.586 -16.115 21.880 0.22 18.68  ? 47   SER   A OG  1 
ATOM   379  N  N   . LEU   A  1 73  ? -26.722 -14.785 19.173 1.00 17.98  ? 48   LEU   A N   1 
ATOM   380  C  CA  . LEU   A  1 73  ? -25.957 -13.835 18.372 1.00 22.91  ? 48   LEU   A CA  1 
ATOM   381  C  C   . LEU   A  1 73  ? -26.766 -13.340 17.179 1.00 19.92  ? 48   LEU   A C   1 
ATOM   382  O  O   . LEU   A  1 73  ? -26.727 -12.150 16.847 1.00 20.54  ? 48   LEU   A O   1 
ATOM   383  C  CB  . LEU   A  1 73  ? -24.657 -14.493 17.908 1.00 20.62  ? 48   LEU   A CB  1 
ATOM   384  C  CG  . LEU   A  1 73  ? -23.631 -13.700 17.099 1.00 33.77  ? 48   LEU   A CG  1 
ATOM   385  C  CD1 . LEU   A  1 73  ? -23.153 -12.480 17.857 1.00 27.33  ? 48   LEU   A CD1 1 
ATOM   386  C  CD2 . LEU   A  1 73  ? -22.456 -14.597 16.738 1.00 29.11  ? 48   LEU   A CD2 1 
ATOM   387  N  N   . ALA   A  1 74  ? -27.512 -14.237 16.528 1.00 17.95  ? 49   ALA   A N   1 
ATOM   388  C  CA  . ALA   A  1 74  ? -28.389 -13.823 15.437 1.00 19.79  ? 49   ALA   A CA  1 
ATOM   389  C  C   . ALA   A  1 74  ? -29.532 -12.939 15.921 1.00 18.70  ? 49   ALA   A C   1 
ATOM   390  O  O   . ALA   A  1 74  ? -29.954 -12.029 15.199 1.00 20.30  ? 49   ALA   A O   1 
ATOM   391  C  CB  . ALA   A  1 74  ? -28.942 -15.052 14.715 1.00 19.71  ? 49   ALA   A CB  1 
ATOM   392  N  N   . ALA   A  1 75  ? -30.046 -13.189 17.128 1.00 19.49  ? 50   ALA   A N   1 
ATOM   393  C  CA  . ALA   A  1 75  ? -31.088 -12.329 17.681 1.00 23.19  ? 50   ALA   A CA  1 
ATOM   394  C  C   . ALA   A  1 75  ? -30.581 -10.907 17.891 1.00 22.05  ? 50   ALA   A C   1 
ATOM   395  O  O   . ALA   A  1 75  ? -31.294 -9.937  17.604 1.00 22.25  ? 50   ALA   A O   1 
ATOM   396  C  CB  . ALA   A  1 75  ? -31.611 -12.914 18.992 1.00 16.45  ? 50   ALA   A CB  1 
ATOM   397  N  N   . ALA   A  1 76  ? -29.354 -10.765 18.400 1.00 20.78  ? 51   ALA   A N   1 
ATOM   398  C  CA  . ALA   A  1 76  ? -28.755 -9.441  18.539 1.00 22.35  ? 51   ALA   A CA  1 
ATOM   399  C  C   . ALA   A  1 76  ? -28.646 -8.740  17.192 1.00 16.85  ? 51   ALA   A C   1 
ATOM   400  O  O   . ALA   A  1 76  ? -28.888 -7.531  17.090 1.00 21.28  ? 51   ALA   A O   1 
ATOM   401  C  CB  . ALA   A  1 76  ? -27.381 -9.554  19.199 1.00 16.19  ? 51   ALA   A CB  1 
ATOM   402  N  N   . ASP   A  1 77  ? -28.282 -9.483  16.144 1.00 18.01  ? 52   ASP   A N   1 
ATOM   403  C  CA  . ASP   A  1 77  ? -28.114 -8.871  14.832 1.00 21.37  ? 52   ASP   A CA  1 
ATOM   404  C  C   . ASP   A  1 77  ? -29.457 -8.514  14.204 1.00 21.29  ? 52   ASP   A C   1 
ATOM   405  O  O   . ASP   A  1 77  ? -29.551 -7.520  13.475 1.00 24.22  ? 52   ASP   A O   1 
ATOM   406  C  CB  . ASP   A  1 77  ? -27.314 -9.801  13.920 1.00 17.99  ? 52   ASP   A CB  1 
ATOM   407  C  CG  . ASP   A  1 77  ? -25.848 -9.869  14.308 1.00 37.23  ? 52   ASP   A CG  1 
ATOM   408  O  OD1 . ASP   A  1 77  ? -25.327 -8.864  14.837 1.00 35.72  ? 52   ASP   A OD1 1 
ATOM   409  O  OD2 . ASP   A  1 77  ? -25.216 -10.924 14.085 1.00 35.94  ? 52   ASP   A OD2 1 
ATOM   410  N  N   . ILE   A  1 78  ? -30.497 -9.313  14.462 1.00 22.09  ? 53   ILE   A N   1 
ATOM   411  C  CA  . ILE   A  1 78  ? -31.844 -8.941  14.035 1.00 21.66  ? 53   ILE   A CA  1 
ATOM   412  C  C   . ILE   A  1 78  ? -32.256 -7.618  14.669 1.00 22.68  ? 53   ILE   A C   1 
ATOM   413  O  O   . ILE   A  1 78  ? -32.844 -6.751  14.011 1.00 21.93  ? 53   ILE   A O   1 
ATOM   414  C  CB  . ILE   A  1 78  ? -32.846 -10.065 14.362 1.00 20.55  ? 53   ILE   A CB  1 
ATOM   415  C  CG1 . ILE   A  1 78  ? -32.586 -11.287 13.479 1.00 27.54  ? 53   ILE   A CG1 1 
ATOM   416  C  CG2 . ILE   A  1 78  ? -34.279 -9.580  14.191 1.00 16.38  ? 53   ILE   A CG2 1 
ATOM   417  C  CD1 . ILE   A  1 78  ? -33.350 -12.523 13.902 1.00 19.74  ? 53   ILE   A CD1 1 
ATOM   418  N  N   . LEU   A  1 79  ? -31.944 -7.436  15.955 1.00 15.08  ? 54   LEU   A N   1 
ATOM   419  C  CA  . LEU   A  1 79  ? -32.300 -6.199  16.641 1.00 18.86  ? 54   LEU   A CA  1 
ATOM   420  C  C   . LEU   A  1 79  ? -31.448 -5.016  16.203 1.00 18.46  ? 54   LEU   A C   1 
ATOM   421  O  O   . LEU   A  1 79  ? -31.883 -3.870  16.358 1.00 17.21  ? 54   LEU   A O   1 
ATOM   422  C  CB  . LEU   A  1 79  ? -32.193 -6.384  18.155 1.00 18.49  ? 54   LEU   A CB  1 
ATOM   423  C  CG  . LEU   A  1 79  ? -33.174 -7.384  18.764 1.00 29.61  ? 54   LEU   A CG  1 
ATOM   424  C  CD1 . LEU   A  1 79  ? -32.858 -7.629  20.228 1.00 24.61  ? 54   LEU   A CD1 1 
ATOM   425  C  CD2 . LEU   A  1 79  ? -34.585 -6.842  18.607 1.00 30.23  ? 54   LEU   A CD2 1 
ATOM   426  N  N   . VAL   A  1 80  ? -30.246 -5.257  15.673 1.00 14.03  ? 55   VAL   A N   1 
ATOM   427  C  CA  . VAL   A  1 80  ? -29.511 -4.177  15.021 1.00 14.68  ? 55   VAL   A CA  1 
ATOM   428  C  C   . VAL   A  1 80  ? -30.301 -3.639  13.835 1.00 18.53  ? 55   VAL   A C   1 
ATOM   429  O  O   . VAL   A  1 80  ? -30.393 -2.423  13.627 1.00 18.10  ? 55   VAL   A O   1 
ATOM   430  C  CB  . VAL   A  1 80  ? -28.111 -4.661  14.597 1.00 18.33  ? 55   VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A  1 80  ? -27.469 -3.666  13.641 1.00 15.27  ? 55   VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A  1 80  ? -27.231 -4.871  15.819 1.00 18.21  ? 55   VAL   A CG2 1 
ATOM   433  N  N   . GLY   A  1 81  ? -30.896 -4.536  13.048 1.00 16.30  ? 56   GLY   A N   1 
ATOM   434  C  CA  . GLY   A  1 81  ? -31.671 -4.099  11.900 1.00 18.78  ? 56   GLY   A CA  1 
ATOM   435  C  C   . GLY   A  1 81  ? -32.983 -3.446  12.292 1.00 18.84  ? 56   GLY   A C   1 
ATOM   436  O  O   . GLY   A  1 81  ? -33.375 -2.424  11.722 1.00 23.45  ? 56   GLY   A O   1 
ATOM   437  N  N   . VAL   A  1 82  ? -33.681 -4.030  13.266 1.00 18.05  ? 57   VAL   A N   1 
ATOM   438  C  CA  . VAL   A  1 82  ? -35.008 -3.551  13.637 1.00 19.92  ? 57   VAL   A CA  1 
ATOM   439  C  C   . VAL   A  1 82  ? -34.930 -2.299  14.507 1.00 23.74  ? 57   VAL   A C   1 
ATOM   440  O  O   . VAL   A  1 82  ? -35.755 -1.389  14.371 1.00 21.31  ? 57   VAL   A O   1 
ATOM   441  C  CB  . VAL   A  1 82  ? -35.791 -4.684  14.328 1.00 26.26  ? 57   VAL   A CB  1 
ATOM   442  C  CG1 . VAL   A  1 82  ? -37.042 -4.149  15.009 1.00 33.75  ? 57   VAL   A CG1 1 
ATOM   443  C  CG2 . VAL   A  1 82  ? -36.152 -5.769  13.321 1.00 22.83  ? 57   VAL   A CG2 1 
ATOM   444  N  N   . LEU   A  1 83  ? -33.949 -2.216  15.406 1.00 19.07  ? 58   LEU   A N   1 
ATOM   445  C  CA  . LEU   A  1 83  ? -33.916 -1.121  16.370 1.00 18.21  ? 58   LEU   A CA  1 
ATOM   446  C  C   . LEU   A  1 83  ? -32.663 -0.263  16.296 1.00 16.50  ? 58   LEU   A C   1 
ATOM   447  O  O   . LEU   A  1 83  ? -32.772 0.968   16.239 1.00 20.81  ? 58   LEU   A O   1 
ATOM   448  C  CB  . LEU   A  1 83  ? -34.079 -1.667  17.799 1.00 23.49  ? 58   LEU   A CB  1 
ATOM   449  C  CG  . LEU   A  1 83  ? -35.445 -2.252  18.157 1.00 28.93  ? 58   LEU   A CG  1 
ATOM   450  C  CD1 . LEU   A  1 83  ? -35.435 -2.824  19.565 1.00 14.06  ? 58   LEU   A CD1 1 
ATOM   451  C  CD2 . LEU   A  1 83  ? -36.510 -1.182  18.027 1.00 28.70  ? 58   LEU   A CD2 1 
ATOM   452  N  N   . ALA   A  1 84  ? -31.470 -0.866  16.306 1.00 15.58  ? 59   ALA   A N   1 
ATOM   453  C  CA  . ALA   A  1 84  ? -30.255 -0.061  16.424 1.00 24.40  ? 59   ALA   A CA  1 
ATOM   454  C  C   . ALA   A  1 84  ? -30.033 0.817   15.198 1.00 20.33  ? 59   ALA   A C   1 
ATOM   455  O  O   . ALA   A  1 84  ? -29.569 1.957   15.323 1.00 18.73  ? 59   ALA   A O   1 
ATOM   456  C  CB  . ALA   A  1 84  ? -29.047 -0.966  16.658 1.00 15.56  ? 59   ALA   A CB  1 
ATOM   457  N  N   . ILE   A  1 85  ? -30.353 0.315   14.011 1.00 15.68  ? 60   ILE   A N   1 
ATOM   458  C  CA  . ILE   A  1 85  ? -30.117 1.083   12.790 1.00 19.43  ? 60   ILE   A CA  1 
ATOM   459  C  C   . ILE   A  1 85  ? -31.153 2.204   12.705 1.00 20.91  ? 60   ILE   A C   1 
ATOM   460  O  O   . ILE   A  1 85  ? -30.780 3.347   12.400 1.00 20.29  ? 60   ILE   A O   1 
ATOM   461  C  CB  . ILE   A  1 85  ? -30.099 0.182   11.544 1.00 18.78  ? 60   ILE   A CB  1 
ATOM   462  C  CG1 . ILE   A  1 85  ? -28.777 -0.589  11.492 1.00 25.02  ? 60   ILE   A CG1 1 
ATOM   463  C  CG2 . ILE   A  1 85  ? -30.281 1.006   10.278 1.00 20.76  ? 60   ILE   A CG2 1 
ATOM   464  C  CD1 . ILE   A  1 85  ? -28.668 -1.560  10.345 1.00 20.35  ? 60   ILE   A CD1 1 
ATOM   465  N  N   . PRO   A  1 86  ? -32.450 1.947   12.945 1.00 18.80  ? 61   PRO   A N   1 
ATOM   466  C  CA  . PRO   A  1 86  ? -33.384 3.079   13.075 1.00 22.25  ? 61   PRO   A CA  1 
ATOM   467  C  C   . PRO   A  1 86  ? -32.962 4.094   14.126 1.00 25.65  ? 61   PRO   A C   1 
ATOM   468  O  O   . PRO   A  1 86  ? -33.135 5.301   13.917 1.00 16.42  ? 61   PRO   A O   1 
ATOM   469  C  CB  . PRO   A  1 86  ? -34.703 2.390   13.445 1.00 21.64  ? 61   PRO   A CB  1 
ATOM   470  C  CG  . PRO   A  1 86  ? -34.626 1.098   12.742 1.00 18.06  ? 61   PRO   A CG  1 
ATOM   471  C  CD  . PRO   A  1 86  ? -33.185 0.667   12.888 1.00 21.21  ? 61   PRO   A CD  1 
ATOM   472  N  N   . PHE   A  1 87  ? -32.417 3.638   15.258 1.00 15.39  ? 62   PHE   A N   1 
ATOM   473  C  CA  . PHE   A  1 87  ? -31.944 4.576   16.272 1.00 20.03  ? 62   PHE   A CA  1 
ATOM   474  C  C   . PHE   A  1 87  ? -30.762 5.389   15.758 1.00 23.02  ? 62   PHE   A C   1 
ATOM   475  O  O   . PHE   A  1 87  ? -30.671 6.596   16.016 1.00 19.09  ? 62   PHE   A O   1 
ATOM   476  C  CB  . PHE   A  1 87  ? -31.554 3.829   17.551 1.00 18.65  ? 62   PHE   A CB  1 
ATOM   477  C  CG  . PHE   A  1 87  ? -32.720 3.260   18.318 1.00 19.10  ? 62   PHE   A CG  1 
ATOM   478  C  CD1 . PHE   A  1 87  ? -34.027 3.469   17.902 1.00 19.95  ? 62   PHE   A CD1 1 
ATOM   479  C  CD2 . PHE   A  1 87  ? -32.500 2.514   19.464 1.00 20.33  ? 62   PHE   A CD2 1 
ATOM   480  C  CE1 . PHE   A  1 87  ? -35.090 2.941   18.617 1.00 21.02  ? 62   PHE   A CE1 1 
ATOM   481  C  CE2 . PHE   A  1 87  ? -33.556 1.986   20.182 1.00 22.02  ? 62   PHE   A CE2 1 
ATOM   482  C  CZ  . PHE   A  1 87  ? -34.853 2.199   19.759 1.00 22.25  ? 62   PHE   A CZ  1 
ATOM   483  N  N   . ALA   A  1 88  ? -29.846 4.742   15.030 1.00 19.71  ? 63   ALA   A N   1 
ATOM   484  C  CA  . ALA   A  1 88  ? -28.685 5.443   14.488 1.00 17.08  ? 63   ALA   A CA  1 
ATOM   485  C  C   . ALA   A  1 88  ? -29.096 6.491   13.460 1.00 15.69  ? 63   ALA   A C   1 
ATOM   486  O  O   . ALA   A  1 88  ? -28.542 7.596   13.433 1.00 18.91  ? 63   ALA   A O   1 
ATOM   487  C  CB  . ALA   A  1 88  ? -27.708 4.442   13.871 1.00 15.87  ? 63   ALA   A CB  1 
ATOM   488  N  N   . ILE   A  1 89  ? -30.053 6.152   12.595 1.00 23.17  ? 64   ILE   A N   1 
ATOM   489  C  CA  . ILE   A  1 89  ? -30.590 7.128   11.649 1.00 24.74  ? 64   ILE   A CA  1 
ATOM   490  C  C   . ILE   A  1 89  ? -31.171 8.321   12.398 1.00 22.36  ? 64   ILE   A C   1 
ATOM   491  O  O   . ILE   A  1 89  ? -30.928 9.481   12.044 1.00 23.49  ? 64   ILE   A O   1 
ATOM   492  C  CB  . ILE   A  1 89  ? -31.638 6.462   10.737 1.00 22.17  ? 64   ILE   A CB  1 
ATOM   493  C  CG1 . ILE   A  1 89  ? -30.966 5.442   9.816  1.00 20.41  ? 64   ILE   A CG1 1 
ATOM   494  C  CG2 . ILE   A  1 89  ? -32.387 7.507   9.921  1.00 19.47  ? 64   ILE   A CG2 1 
ATOM   495  C  CD1 . ILE   A  1 89  ? -31.940 4.549   9.078  1.00 19.06  ? 64   ILE   A CD1 1 
ATOM   496  N  N   . THR   A  1 90  ? -31.960 8.047   13.439 1.00 16.17  ? 65   THR   A N   1 
ATOM   497  C  CA  . THR   A  1 90  ? -32.592 9.115   14.208 1.00 20.02  ? 65   THR   A CA  1 
ATOM   498  C  C   . THR   A  1 90  ? -31.555 10.043  14.833 1.00 25.24  ? 65   THR   A C   1 
ATOM   499  O  O   . THR   A  1 90  ? -31.665 11.271  14.735 1.00 19.28  ? 65   THR   A O   1 
ATOM   500  C  CB  . THR   A  1 90  ? -33.494 8.511   15.285 1.00 29.39  ? 65   THR   A CB  1 
ATOM   501  O  OG1 . THR   A  1 90  ? -34.449 7.638   14.670 1.00 25.76  ? 65   THR   A OG1 1 
ATOM   502  C  CG2 . THR   A  1 90  ? -34.233 9.605   16.028 1.00 24.99  ? 65   THR   A CG2 1 
ATOM   503  N  N   . ILE   A  1 91  ? -30.534 9.475   15.481 1.00 23.88  ? 66   ILE   A N   1 
ATOM   504  C  CA  . ILE   A  1 91  ? -29.555 10.290  16.191 1.00 19.56  ? 66   ILE   A CA  1 
ATOM   505  C  C   . ILE   A  1 91  ? -28.610 11.030  15.257 1.00 25.30  ? 66   ILE   A C   1 
ATOM   506  O  O   . ILE   A  1 91  ? -27.902 11.942  15.699 1.00 28.12  ? 66   ILE   A O   1 
ATOM   507  C  CB  . ILE   A  1 91  ? -28.754 9.424   17.186 1.00 25.40  ? 66   ILE   A CB  1 
ATOM   508  C  CG1 . ILE   A  1 91  ? -28.179 10.296  18.303 1.00 41.36  ? 66   ILE   A CG1 1 
ATOM   509  C  CG2 . ILE   A  1 91  ? -27.650 8.659   16.472 1.00 22.07  ? 66   ILE   A CG2 1 
ATOM   510  C  CD1 . ILE   A  1 91  ? -27.936 9.556   19.587 1.00 31.18  ? 66   ILE   A CD1 1 
ATOM   511  N  N   . SER   A  1 92  ? -28.584 10.673  13.972 1.00 25.48  ? 67   SER   A N   1 
ATOM   512  C  CA  . SER   A  1 92  ? -27.776 11.422  13.018 1.00 22.06  ? 67   SER   A CA  1 
ATOM   513  C  C   . SER   A  1 92  ? -28.410 12.757  12.650 1.00 30.66  ? 67   SER   A C   1 
ATOM   514  O  O   . SER   A  1 92  ? -27.714 13.635  12.128 1.00 27.78  ? 67   SER   A O   1 
ATOM   515  C  CB  . SER   A  1 92  ? -27.539 10.591  11.756 1.00 22.53  ? 67   SER   A CB  1 
ATOM   516  O  OG  . SER   A  1 92  ? -28.684 10.590  10.922 1.00 28.68  ? 67   SER   A OG  1 
ATOM   517  N  N   . THR   A  1 93  ? -29.707 12.932  12.908 1.00 25.94  ? 68   THR   A N   1 
ATOM   518  C  CA  . THR   A  1 93  ? -30.394 14.166  12.551 1.00 35.50  ? 68   THR   A CA  1 
ATOM   519  C  C   . THR   A  1 93  ? -30.230 15.267  13.590 1.00 38.16  ? 68   THR   A C   1 
ATOM   520  O  O   . THR   A  1 93  ? -30.520 16.429  13.284 1.00 36.15  ? 68   THR   A O   1 
ATOM   521  C  CB  . THR   A  1 93  ? -31.887 13.899  12.340 1.00 30.77  ? 68   THR   A CB  1 
ATOM   522  O  OG1 . THR   A  1 93  ? -32.508 13.633  13.604 1.00 23.52  ? 68   THR   A OG1 1 
ATOM   523  C  CG2 . THR   A  1 93  ? -32.091 12.706  11.421 1.00 21.68  ? 68   THR   A CG2 1 
ATOM   524  N  N   . GLY   A  1 94  ? -29.775 14.939  14.798 1.00 33.29  ? 69   GLY   A N   1 
ATOM   525  C  CA  . GLY   A  1 94  ? -29.666 15.936  15.844 1.00 21.31  ? 69   GLY   A CA  1 
ATOM   526  C  C   . GLY   A  1 94  ? -30.977 16.489  16.354 1.00 31.03  ? 69   GLY   A C   1 
ATOM   527  O  O   . GLY   A  1 94  ? -30.997 17.601  16.883 1.00 33.14  ? 69   GLY   A O   1 
ATOM   528  N  N   . PHE   A  1 95  ? -32.073 15.747  16.216 1.00 24.40  ? 70   PHE   A N   1 
ATOM   529  C  CA  . PHE   A  1 95  ? -33.391 16.257  16.569 1.00 28.64  ? 70   PHE   A CA  1 
ATOM   530  C  C   . PHE   A  1 95  ? -33.476 16.586  18.059 1.00 30.89  ? 70   PHE   A C   1 
ATOM   531  O  O   . PHE   A  1 95  ? -32.740 16.043  18.888 1.00 21.94  ? 70   PHE   A O   1 
ATOM   532  C  CB  . PHE   A  1 95  ? -34.469 15.232  16.221 1.00 26.35  ? 70   PHE   A CB  1 
ATOM   533  C  CG  . PHE   A  1 95  ? -34.547 14.094  17.198 1.00 30.86  ? 70   PHE   A CG  1 
ATOM   534  C  CD1 . PHE   A  1 95  ? -33.503 13.191  17.316 1.00 27.63  ? 70   PHE   A CD1 1 
ATOM   535  C  CD2 . PHE   A  1 95  ? -35.654 13.939  18.014 1.00 31.05  ? 70   PHE   A CD2 1 
ATOM   536  C  CE1 . PHE   A  1 95  ? -33.566 12.150  18.221 1.00 26.17  ? 70   PHE   A CE1 1 
ATOM   537  C  CE2 . PHE   A  1 95  ? -35.723 12.899  18.921 1.00 30.20  ? 70   PHE   A CE2 1 
ATOM   538  C  CZ  . PHE   A  1 95  ? -34.678 12.002  19.023 1.00 24.45  ? 70   PHE   A CZ  1 
ATOM   539  N  N   . CYS   A  1 96  ? -34.388 17.499  18.393 1.00 28.02  ? 71   CYS   A N   1 
ATOM   540  C  CA  . CYS   A  1 96  ? -34.575 17.905  19.781 1.00 38.94  ? 71   CYS   A CA  1 
ATOM   541  C  C   . CYS   A  1 96  ? -35.201 16.773  20.589 1.00 33.84  ? 71   CYS   A C   1 
ATOM   542  O  O   . CYS   A  1 96  ? -36.208 16.187  20.179 1.00 30.89  ? 71   CYS   A O   1 
ATOM   543  C  CB  . CYS   A  1 96  ? -35.457 19.151  19.858 1.00 30.04  ? 71   CYS   A CB  1 
ATOM   544  S  SG  . CYS   A  1 96  ? -34.725 20.653  19.167 1.00 38.26  ? 71   CYS   A SG  1 
ATOM   545  N  N   . ALA   A  1 97  ? -34.605 16.467  21.741 1.00 28.77  ? 72   ALA   A N   1 
ATOM   546  C  CA  . ALA   A  1 97  ? -35.058 15.357  22.566 1.00 21.71  ? 72   ALA   A CA  1 
ATOM   547  C  C   . ALA   A  1 97  ? -34.669 15.603  24.017 1.00 26.51  ? 72   ALA   A C   1 
ATOM   548  O  O   . ALA   A  1 97  ? -33.645 16.231  24.299 1.00 34.94  ? 72   ALA   A O   1 
ATOM   549  C  CB  . ALA   A  1 97  ? -34.477 14.023  22.085 1.00 26.88  ? 72   ALA   A CB  1 
ATOM   550  N  N   . ALA   A  1 98  ? -35.505 15.114  24.934 1.00 30.45  ? 73   ALA   A N   1 
ATOM   551  C  CA  . ALA   A  1 98  ? -35.097 14.978  26.328 1.00 31.02  ? 73   ALA   A CA  1 
ATOM   552  C  C   . ALA   A  1 98  ? -33.820 14.150  26.403 1.00 24.36  ? 73   ALA   A C   1 
ATOM   553  O  O   . ALA   A  1 98  ? -33.707 13.110  25.750 1.00 26.57  ? 73   ALA   A O   1 
ATOM   554  C  CB  . ALA   A  1 98  ? -36.210 14.325  27.149 1.00 24.69  ? 73   ALA   A CB  1 
ATOM   555  N  N   . CYS   A  1 99  ? -32.851 14.623  27.193 1.00 31.00  ? 74   CYS   A N   1 
ATOM   556  C  CA  . CYS   A  1 99  ? -31.502 14.068  27.107 1.00 30.88  ? 74   CYS   A CA  1 
ATOM   557  C  C   . CYS   A  1 99  ? -31.458 12.579  27.445 1.00 27.70  ? 74   CYS   A C   1 
ATOM   558  O  O   . CYS   A  1 99  ? -30.719 11.821  26.806 1.00 24.09  ? 74   CYS   A O   1 
ATOM   559  C  CB  . CYS   A  1 99  ? -30.555 14.845  28.021 1.00 38.47  ? 74   CYS   A CB  1 
ATOM   560  S  SG  . CYS   A  1 99  ? -28.822 14.372  27.825 1.00 39.96  ? 74   CYS   A SG  1 
ATOM   561  N  N   . HIS   A  1 100 ? -32.231 12.132  28.440 1.00 22.33  ? 75   HIS   A N   1 
ATOM   562  C  CA  . HIS   A  1 100 ? -32.166 10.713  28.788 1.00 29.04  ? 75   HIS   A CA  1 
ATOM   563  C  C   . HIS   A  1 100 ? -32.888 9.832   27.776 1.00 27.26  ? 75   HIS   A C   1 
ATOM   564  O  O   . HIS   A  1 100 ? -32.509 8.668   27.602 1.00 25.45  ? 75   HIS   A O   1 
ATOM   565  C  CB  . HIS   A  1 100 ? -32.690 10.450  30.203 1.00 28.34  ? 75   HIS   A CB  1 
ATOM   566  C  CG  . HIS   A  1 100 ? -31.792 10.963  31.287 1.00 51.86  ? 75   HIS   A CG  1 
ATOM   567  N  ND1 . HIS   A  1 100 ? -31.847 12.255  31.764 1.00 47.39  ? 75   HIS   A ND1 1 
ATOM   568  C  CD2 . HIS   A  1 100 ? -30.805 10.349  31.982 1.00 41.58  ? 75   HIS   A CD2 1 
ATOM   569  C  CE1 . HIS   A  1 100 ? -30.937 12.412  32.710 1.00 43.65  ? 75   HIS   A CE1 1 
ATOM   570  N  NE2 . HIS   A  1 100 ? -30.291 11.270  32.860 1.00 55.79  ? 75   HIS   A NE2 1 
ATOM   571  N  N   . GLY   A  1 101 ? -33.923 10.341  27.106 1.00 29.55  ? 76   GLY   A N   1 
ATOM   572  C  CA  . GLY   A  1 101 ? -34.460 9.598   25.980 1.00 29.22  ? 76   GLY   A CA  1 
ATOM   573  C  C   . GLY   A  1 101 ? -33.455 9.497   24.851 1.00 23.12  ? 76   GLY   A C   1 
ATOM   574  O  O   . GLY   A  1 101 ? -33.300 8.439   24.235 1.00 27.54  ? 76   GLY   A O   1 
ATOM   575  N  N   . CYS   A  1 102 ? -32.765 10.602  24.561 1.00 18.66  ? 77   CYS   A N   1 
ATOM   576  C  CA  . CYS   A  1 102 ? -31.679 10.580  23.589 1.00 27.39  ? 77   CYS   A CA  1 
ATOM   577  C  C   . CYS   A  1 102 ? -30.600 9.585   24.002 1.00 28.29  ? 77   CYS   A C   1 
ATOM   578  O  O   . CYS   A  1 102 ? -30.011 8.903   23.154 1.00 21.76  ? 77   CYS   A O   1 
ATOM   579  C  CB  . CYS   A  1 102 ? -31.095 11.982  23.430 1.00 25.42  ? 77   CYS   A CB  1 
ATOM   580  S  SG  . CYS   A  1 102 ? -29.697 12.049  22.310 1.00 36.07  ? 77   CYS   A SG  1 
ATOM   581  N  N   A LEU   A  1 103 ? -30.316 9.510   25.306 0.68 22.85  ? 78   LEU   A N   1 
ATOM   582  N  N   B LEU   A  1 103 ? -30.331 9.487   25.306 0.32 22.89  ? 78   LEU   A N   1 
ATOM   583  C  CA  A LEU   A  1 103 ? -29.297 8.596   25.811 0.68 20.67  ? 78   LEU   A CA  1 
ATOM   584  C  CA  B LEU   A  1 103 ? -29.282 8.595   25.788 0.32 20.71  ? 78   LEU   A CA  1 
ATOM   585  C  C   A LEU   A  1 103 ? -29.639 7.150   25.486 0.68 21.51  ? 78   LEU   A C   1 
ATOM   586  C  C   B LEU   A  1 103 ? -29.629 7.134   25.528 0.32 21.54  ? 78   LEU   A C   1 
ATOM   587  O  O   A LEU   A  1 103 ? -28.760 6.363   25.113 0.68 23.58  ? 78   LEU   A O   1 
ATOM   588  O  O   B LEU   A  1 103 ? -28.744 6.322   25.234 0.32 23.37  ? 78   LEU   A O   1 
ATOM   589  C  CB  A LEU   A  1 103 ? -29.150 8.770   27.322 0.68 25.27  ? 78   LEU   A CB  1 
ATOM   590  C  CB  B LEU   A  1 103 ? -29.044 8.835   27.279 0.32 25.17  ? 78   LEU   A CB  1 
ATOM   591  C  CG  A LEU   A  1 103 ? -27.885 9.392   27.905 0.68 27.06  ? 78   LEU   A CG  1 
ATOM   592  C  CG  B LEU   A  1 103 ? -27.776 8.256   27.909 0.32 23.31  ? 78   LEU   A CG  1 
ATOM   593  C  CD1 A LEU   A  1 103 ? -27.940 9.254   29.412 0.68 19.44  ? 78   LEU   A CD1 1 
ATOM   594  C  CD1 B LEU   A  1 103 ? -26.529 8.728   27.177 0.32 23.63  ? 78   LEU   A CD1 1 
ATOM   595  C  CD2 A LEU   A  1 103 ? -26.634 8.734   27.346 0.68 23.98  ? 78   LEU   A CD2 1 
ATOM   596  C  CD2 B LEU   A  1 103 ? -27.714 8.627   29.381 0.32 21.53  ? 78   LEU   A CD2 1 
ATOM   597  N  N   . PHE   A  1 104 ? -30.912 6.779   25.629 1.00 20.10  ? 79   PHE   A N   1 
ATOM   598  C  CA  . PHE   A  1 104 ? -31.314 5.394   25.402 1.00 22.81  ? 79   PHE   A CA  1 
ATOM   599  C  C   . PHE   A  1 104 ? -31.111 4.985   23.948 1.00 17.88  ? 79   PHE   A C   1 
ATOM   600  O  O   . PHE   A  1 104 ? -30.557 3.917   23.667 1.00 20.69  ? 79   PHE   A O   1 
ATOM   601  C  CB  . PHE   A  1 104 ? -32.770 5.188   25.814 1.00 19.64  ? 79   PHE   A CB  1 
ATOM   602  C  CG  . PHE   A  1 104 ? -33.254 3.782   25.610 1.00 23.12  ? 79   PHE   A CG  1 
ATOM   603  C  CD1 . PHE   A  1 104 ? -32.909 2.778   26.499 1.00 21.02  ? 79   PHE   A CD1 1 
ATOM   604  C  CD2 . PHE   A  1 104 ? -34.035 3.460   24.513 1.00 24.85  ? 79   PHE   A CD2 1 
ATOM   605  C  CE1 . PHE   A  1 104 ? -33.348 1.482   26.306 1.00 24.29  ? 79   PHE   A CE1 1 
ATOM   606  C  CE2 . PHE   A  1 104 ? -34.475 2.167   24.313 1.00 24.87  ? 79   PHE   A CE2 1 
ATOM   607  C  CZ  . PHE   A  1 104 ? -34.132 1.177   25.211 1.00 27.92  ? 79   PHE   A CZ  1 
ATOM   608  N  N   . ILE   A  1 105 ? -31.564 5.816   23.005 1.00 22.23  ? 80   ILE   A N   1 
ATOM   609  C  CA  . ILE   A  1 105 ? -31.393 5.460   21.600 1.00 26.93  ? 80   ILE   A CA  1 
ATOM   610  C  C   . ILE   A  1 105 ? -29.921 5.476   21.220 1.00 20.93  ? 80   ILE   A C   1 
ATOM   611  O  O   . ILE   A  1 105 ? -29.506 4.770   20.293 1.00 19.41  ? 80   ILE   A O   1 
ATOM   612  C  CB  . ILE   A  1 105 ? -32.223 6.383   20.687 1.00 21.20  ? 80   ILE   A CB  1 
ATOM   613  C  CG1 . ILE   A  1 105 ? -31.732 7.829   20.761 1.00 26.93  ? 80   ILE   A CG1 1 
ATOM   614  C  CG2 . ILE   A  1 105 ? -33.687 6.308   21.051 1.00 24.54  ? 80   ILE   A CG2 1 
ATOM   615  C  CD1 . ILE   A  1 105 ? -32.362 8.736   19.721 1.00 39.47  ? 80   ILE   A CD1 1 
ATOM   616  N  N   . ALA   A  1 106 ? -29.106 6.264   21.924 1.00 14.28  ? 81   ALA   A N   1 
ATOM   617  C  CA  . ALA   A  1 106 ? -27.672 6.245   21.663 1.00 20.40  ? 81   ALA   A CA  1 
ATOM   618  C  C   . ALA   A  1 106 ? -27.039 4.961   22.178 1.00 22.39  ? 81   ALA   A C   1 
ATOM   619  O  O   . ALA   A  1 106 ? -26.139 4.404   21.538 1.00 19.57  ? 81   ALA   A O   1 
ATOM   620  C  CB  . ALA   A  1 106 ? -27.005 7.462   22.303 1.00 12.78  ? 81   ALA   A CB  1 
ATOM   621  N  N   . CYS   A  1 107 ? -27.493 4.474   23.334 1.00 15.45  ? 82   CYS   A N   1 
ATOM   622  C  CA  . CYS   A  1 107 ? -26.790 3.409   24.033 1.00 23.18  ? 82   CYS   A CA  1 
ATOM   623  C  C   . CYS   A  1 107 ? -27.324 2.015   23.736 1.00 18.25  ? 82   CYS   A C   1 
ATOM   624  O  O   . CYS   A  1 107 ? -26.639 1.038   24.054 1.00 19.55  ? 82   CYS   A O   1 
ATOM   625  C  CB  . CYS   A  1 107 ? -26.844 3.643   25.549 1.00 20.46  ? 82   CYS   A CB  1 
ATOM   626  S  SG  . CYS   A  1 107 ? -25.892 5.066   26.122 1.00 23.11  ? 82   CYS   A SG  1 
ATOM   627  N  N   . PHE   A  1 108 ? -28.526 1.889   23.163 1.00 17.21  ? 83   PHE   A N   1 
ATOM   628  C  CA  . PHE   A  1 108 ? -29.096 0.557   22.977 1.00 16.04  ? 83   PHE   A CA  1 
ATOM   629  C  C   . PHE   A  1 108 ? -28.185 -0.322  22.130 1.00 16.41  ? 83   PHE   A C   1 
ATOM   630  O  O   . PHE   A  1 108 ? -28.097 -1.534  22.357 1.00 17.30  ? 83   PHE   A O   1 
ATOM   631  C  CB  . PHE   A  1 108 ? -30.489 0.633   22.355 1.00 17.78  ? 83   PHE   A CB  1 
ATOM   632  C  CG  . PHE   A  1 108 ? -31.161 -0.709  22.244 1.00 21.86  ? 83   PHE   A CG  1 
ATOM   633  C  CD1 . PHE   A  1 108 ? -31.539 -1.396  23.386 1.00 18.06  ? 83   PHE   A CD1 1 
ATOM   634  C  CD2 . PHE   A  1 108 ? -31.393 -1.294  21.009 1.00 14.69  ? 83   PHE   A CD2 1 
ATOM   635  C  CE1 . PHE   A  1 108 ? -32.148 -2.634  23.304 1.00 20.14  ? 83   PHE   A CE1 1 
ATOM   636  C  CE2 . PHE   A  1 108 ? -32.005 -2.535  20.919 1.00 21.86  ? 83   PHE   A CE2 1 
ATOM   637  C  CZ  . PHE   A  1 108 ? -32.382 -3.204  22.068 1.00 19.83  ? 83   PHE   A CZ  1 
ATOM   638  N  N   . VAL   A  1 109 ? -27.516 0.265   21.132 1.00 18.92  ? 84   VAL   A N   1 
ATOM   639  C  CA  . VAL   A  1 109 ? -26.632 -0.530  20.284 1.00 18.34  ? 84   VAL   A CA  1 
ATOM   640  C  C   . VAL   A  1 109 ? -25.485 -1.111  21.101 1.00 14.06  ? 84   VAL   A C   1 
ATOM   641  O  O   . VAL   A  1 109 ? -24.957 -2.182  20.774 1.00 13.79  ? 84   VAL   A O   1 
ATOM   642  C  CB  . VAL   A  1 109 ? -26.121 0.320   19.100 1.00 22.32  ? 84   VAL   A CB  1 
ATOM   643  C  CG1 . VAL   A  1 109 ? -25.254 1.473   19.592 1.00 15.49  ? 84   VAL   A CG1 1 
ATOM   644  C  CG2 . VAL   A  1 109 ? -25.359 -0.546  18.104 1.00 17.77  ? 84   VAL   A CG2 1 
ATOM   645  N  N   . LEU   A  1 110 ? -25.087 -0.429  22.181 1.00 17.39  ? 85   LEU   A N   1 
ATOM   646  C  CA  . LEU   A  1 110 ? -24.038 -0.963  23.044 1.00 18.99  ? 85   LEU   A CA  1 
ATOM   647  C  C   . LEU   A  1 110 ? -24.495 -2.227  23.761 1.00 14.64  ? 85   LEU   A C   1 
ATOM   648  O  O   . LEU   A  1 110 ? -23.677 -3.109  24.043 1.00 17.72  ? 85   LEU   A O   1 
ATOM   649  C  CB  . LEU   A  1 110 ? -23.589 0.097   24.050 1.00 17.68  ? 85   LEU   A CB  1 
ATOM   650  C  CG  . LEU   A  1 110 ? -23.143 1.432   23.447 1.00 25.26  ? 85   LEU   A CG  1 
ATOM   651  C  CD1 . LEU   A  1 110 ? -22.770 2.422   24.537 1.00 19.99  ? 85   LEU   A CD1 1 
ATOM   652  C  CD2 . LEU   A  1 110 ? -21.975 1.216   22.497 1.00 22.74  ? 85   LEU   A CD2 1 
ATOM   653  N  N   . VAL   A  1 111 ? -25.792 -2.327  24.063 1.00 18.32  ? 86   VAL   A N   1 
ATOM   654  C  CA  . VAL   A  1 111 ? -26.340 -3.554  24.637 1.00 18.38  ? 86   VAL   A CA  1 
ATOM   655  C  C   . VAL   A  1 111 ? -26.197 -4.705  23.651 1.00 16.90  ? 86   VAL   A C   1 
ATOM   656  O  O   . VAL   A  1 111 ? -25.769 -5.809  24.010 1.00 16.69  ? 86   VAL   A O   1 
ATOM   657  C  CB  . VAL   A  1 111 ? -27.808 -3.345  25.051 1.00 20.58  ? 86   VAL   A CB  1 
ATOM   658  C  CG1 . VAL   A  1 111 ? -28.382 -4.631  25.635 1.00 13.99  ? 86   VAL   A CG1 1 
ATOM   659  C  CG2 . VAL   A  1 111 ? -27.923 -2.197  26.043 1.00 11.98  ? 86   VAL   A CG2 1 
ATOM   660  N  N   . LEU   A  1 112 ? -26.553 -4.460  22.388 1.00 11.75  ? 87   LEU   A N   1 
ATOM   661  C  CA  . LEU   A  1 112 ? -26.502 -5.514  21.383 1.00 16.95  ? 87   LEU   A CA  1 
ATOM   662  C  C   . LEU   A  1 112 ? -25.065 -5.932  21.100 1.00 17.41  ? 87   LEU   A C   1 
ATOM   663  O  O   . LEU   A  1 112 ? -24.782 -7.126  20.943 1.00 16.85  ? 87   LEU   A O   1 
ATOM   664  C  CB  . LEU   A  1 112 ? -27.191 -5.047  20.101 1.00 12.38  ? 87   LEU   A CB  1 
ATOM   665  C  CG  . LEU   A  1 112 ? -28.659 -4.631  20.232 1.00 14.92  ? 87   LEU   A CG  1 
ATOM   666  C  CD1 . LEU   A  1 112 ? -29.237 -4.275  18.872 1.00 14.66  ? 87   LEU   A CD1 1 
ATOM   667  C  CD2 . LEU   A  1 112 ? -29.481 -5.725  20.899 1.00 14.36  ? 87   LEU   A CD2 1 
ATOM   668  N  N   . ALA   A  1 113 ? -24.147 -4.965  21.024 1.00 12.59  ? 88   ALA   A N   1 
ATOM   669  C  CA  . ALA   A  1 113 ? -22.740 -5.301  20.834 1.00 20.17  ? 88   ALA   A CA  1 
ATOM   670  C  C   . ALA   A  1 113 ? -22.209 -6.111  22.009 1.00 17.37  ? 88   ALA   A C   1 
ATOM   671  O  O   . ALA   A  1 113 ? -21.437 -7.059  21.821 1.00 15.78  ? 88   ALA   A O   1 
ATOM   672  C  CB  . ALA   A  1 113 ? -21.914 -4.030  20.639 1.00 13.30  ? 88   ALA   A CB  1 
ATOM   673  N  N   . GLN   A  1 114 ? -22.609 -5.752  23.232 1.00 15.72  ? 89   GLN   A N   1 
ATOM   674  C  CA  . GLN   A  1 114 ? -22.106 -6.459  24.404 1.00 17.75  ? 89   GLN   A CA  1 
ATOM   675  C  C   . GLN   A  1 114 ? -22.623 -7.892  24.431 1.00 19.37  ? 89   GLN   A C   1 
ATOM   676  O  O   . GLN   A  1 114 ? -21.877 -8.824  24.753 1.00 20.11  ? 89   GLN   A O   1 
ATOM   677  C  CB  . GLN   A  1 114 ? -22.503 -5.720  25.682 1.00 18.88  ? 89   GLN   A CB  1 
ATOM   678  C  CG  . GLN   A  1 114 ? -21.656 -6.098  26.884 1.00 26.36  ? 89   GLN   A CG  1 
ATOM   679  C  CD  . GLN   A  1 114 ? -20.179 -5.856  26.635 1.00 27.68  ? 89   GLN   A CD  1 
ATOM   680  O  OE1 . GLN   A  1 114 ? -19.790 -4.794  26.148 1.00 26.28  ? 89   GLN   A OE1 1 
ATOM   681  N  NE2 . GLN   A  1 114 ? -19.351 -6.845  26.952 1.00 21.61  ? 89   GLN   A NE2 1 
ATOM   682  N  N   . SER   A  1 115 ? -23.906 -8.080  24.105 1.00 19.45  ? 90   SER   A N   1 
ATOM   683  C  CA  . SER   A  1 115 ? -24.464 -9.425  24.015 1.00 14.81  ? 90   SER   A CA  1 
ATOM   684  C  C   . SER   A  1 115 ? -23.724 -10.254 22.975 1.00 19.63  ? 90   SER   A C   1 
ATOM   685  O  O   . SER   A  1 115 ? -23.470 -11.447 23.186 1.00 20.65  ? 90   SER   A O   1 
ATOM   686  C  CB  . SER   A  1 115 ? -25.954 -9.348  23.682 1.00 21.75  ? 90   SER   A CB  1 
ATOM   687  O  OG  . SER   A  1 115 ? -26.528 -10.640 23.590 1.00 21.22  ? 90   SER   A OG  1 
ATOM   688  N  N   . SER   A  1 116 ? -23.381 -9.641  21.839 1.00 19.39  ? 91   SER   A N   1 
ATOM   689  C  CA  . SER   A  1 116 ? -22.618 -10.347 20.815 1.00 17.23  ? 91   SER   A CA  1 
ATOM   690  C  C   . SER   A  1 116 ? -21.278 -10.821 21.360 1.00 19.78  ? 91   SER   A C   1 
ATOM   691  O  O   . SER   A  1 116 ? -20.849 -11.948 21.087 1.00 17.91  ? 91   SER   A O   1 
ATOM   692  C  CB  . SER   A  1 116 ? -22.412 -9.443  19.599 1.00 14.31  ? 91   SER   A CB  1 
ATOM   693  O  OG  . SER   A  1 116 ? -23.646 -9.150  18.967 1.00 19.38  ? 91   SER   A OG  1 
ATOM   694  N  N   . ILE   A  1 117 ? -20.606 -9.969  22.138 1.00 14.60  ? 92   ILE   A N   1 
ATOM   695  C  CA  . ILE   A  1 117 ? -19.318 -10.335 22.719 1.00 18.57  ? 92   ILE   A CA  1 
ATOM   696  C  C   . ILE   A  1 117 ? -19.471 -11.525 23.656 1.00 18.18  ? 92   ILE   A C   1 
ATOM   697  O  O   . ILE   A  1 117 ? -18.665 -12.464 23.627 1.00 20.22  ? 92   ILE   A O   1 
ATOM   698  C  CB  . ILE   A  1 117 ? -18.704 -9.119  23.437 1.00 24.96  ? 92   ILE   A CB  1 
ATOM   699  C  CG1 . ILE   A  1 117 ? -18.067 -8.172  22.420 1.00 28.64  ? 92   ILE   A CG1 1 
ATOM   700  C  CG2 . ILE   A  1 117 ? -17.694 -9.562  24.476 1.00 15.09  ? 92   ILE   A CG2 1 
ATOM   701  C  CD1 . ILE   A  1 117 ? -17.971 -6.752  22.903 1.00 29.37  ? 92   ILE   A CD1 1 
ATOM   702  N  N   . PHE   A  1 118 ? -20.509 -11.511 24.496 1.00 16.72  ? 93   PHE   A N   1 
ATOM   703  C  CA  . PHE   A  1 118 ? -20.727 -12.624 25.414 1.00 20.58  ? 93   PHE   A CA  1 
ATOM   704  C  C   . PHE   A  1 118 ? -21.000 -13.917 24.655 1.00 20.59  ? 93   PHE   A C   1 
ATOM   705  O  O   . PHE   A  1 118 ? -20.502 -14.984 25.033 1.00 22.76  ? 93   PHE   A O   1 
ATOM   706  C  CB  . PHE   A  1 118 ? -21.887 -12.304 26.357 1.00 22.39  ? 93   PHE   A CB  1 
ATOM   707  C  CG  . PHE   A  1 118 ? -21.535 -11.340 27.456 1.00 25.75  ? 93   PHE   A CG  1 
ATOM   708  C  CD1 . PHE   A  1 118 ? -20.319 -11.426 28.116 1.00 40.14  ? 93   PHE   A CD1 1 
ATOM   709  C  CD2 . PHE   A  1 118 ? -22.425 -10.346 27.829 1.00 20.98  ? 93   PHE   A CD2 1 
ATOM   710  C  CE1 . PHE   A  1 118 ? -19.999 -10.537 29.129 1.00 44.12  ? 93   PHE   A CE1 1 
ATOM   711  C  CE2 . PHE   A  1 118 ? -22.111 -9.455  28.840 1.00 27.67  ? 93   PHE   A CE2 1 
ATOM   712  C  CZ  . PHE   A  1 118 ? -20.897 -9.551  29.490 1.00 24.98  ? 93   PHE   A CZ  1 
ATOM   713  N  N   . SER   A  1 119 ? -21.795 -13.843 23.583 1.00 16.07  ? 94   SER   A N   1 
ATOM   714  C  CA  . SER   A  1 119 ? -22.058 -15.033 22.780 1.00 17.66  ? 94   SER   A CA  1 
ATOM   715  C  C   . SER   A  1 119 ? -20.784 -15.551 22.124 1.00 23.69  ? 94   SER   A C   1 
ATOM   716  O  O   . SER   A  1 119 ? -20.535 -16.762 22.106 1.00 19.55  ? 94   SER   A O   1 
ATOM   717  C  CB  . SER   A  1 119 ? -23.120 -14.731 21.723 1.00 23.00  ? 94   SER   A CB  1 
ATOM   718  O  OG  . SER   A  1 119 ? -24.375 -14.470 22.325 1.00 21.25  ? 94   SER   A OG  1 
ATOM   719  N  N   . LEU   A  1 120 ? -19.967 -14.648 21.574 1.00 16.49  ? 95   LEU   A N   1 
ATOM   720  C  CA  . LEU   A  1 120 ? -18.738 -15.075 20.913 1.00 18.78  ? 95   LEU   A CA  1 
ATOM   721  C  C   . LEU   A  1 120 ? -17.780 -15.717 21.906 1.00 22.48  ? 95   LEU   A C   1 
ATOM   722  O  O   . LEU   A  1 120 ? -17.133 -16.725 21.597 1.00 24.62  ? 95   LEU   A O   1 
ATOM   723  C  CB  . LEU   A  1 120 ? -18.074 -13.887 20.218 1.00 18.71  ? 95   LEU   A CB  1 
ATOM   724  C  CG  . LEU   A  1 120 ? -18.793 -13.336 18.986 1.00 28.20  ? 95   LEU   A CG  1 
ATOM   725  C  CD1 . LEU   A  1 120 ? -18.249 -11.964 18.610 1.00 21.66  ? 95   LEU   A CD1 1 
ATOM   726  C  CD2 . LEU   A  1 120 ? -18.681 -14.305 17.823 1.00 13.63  ? 95   LEU   A CD2 1 
ATOM   727  N  N   . LEU   A  1 121 ? -17.678 -15.145 23.108 1.00 17.47  ? 96   LEU   A N   1 
ATOM   728  C  CA  . LEU   A  1 121 ? -16.824 -15.723 24.139 1.00 24.98  ? 96   LEU   A CA  1 
ATOM   729  C  C   . LEU   A  1 121 ? -17.339 -17.090 24.568 1.00 26.87  ? 96   LEU   A C   1 
ATOM   730  O  O   . LEU   A  1 121 ? -16.555 -18.026 24.769 1.00 26.06  ? 96   LEU   A O   1 
ATOM   731  C  CB  . LEU   A  1 121 ? -16.739 -14.776 25.335 1.00 23.46  ? 96   LEU   A CB  1 
ATOM   732  C  CG  . LEU   A  1 121 ? -15.874 -15.213 26.516 1.00 28.13  ? 96   LEU   A CG  1 
ATOM   733  C  CD1 . LEU   A  1 121 ? -14.464 -15.546 26.060 1.00 22.59  ? 96   LEU   A CD1 1 
ATOM   734  C  CD2 . LEU   A  1 121 ? -15.856 -14.126 27.573 1.00 28.87  ? 96   LEU   A CD2 1 
ATOM   735  N  N   . ALA   A  1 122 ? -18.660 -17.220 24.719 1.00 17.08  ? 97   ALA   A N   1 
ATOM   736  C  CA  . ALA   A  1 122 ? -19.246 -18.499 25.105 1.00 25.17  ? 97   ALA   A CA  1 
ATOM   737  C  C   . ALA   A  1 122 ? -18.976 -19.566 24.052 1.00 28.24  ? 97   ALA   A C   1 
ATOM   738  O  O   . ALA   A  1 122 ? -18.671 -20.716 24.388 1.00 21.24  ? 97   ALA   A O   1 
ATOM   739  C  CB  . ALA   A  1 122 ? -20.746 -18.337 25.341 1.00 19.18  ? 97   ALA   A CB  1 
ATOM   740  N  N   . ILE   A  1 123 ? -19.111 -19.209 22.771 1.00 28.58  ? 98   ILE   A N   1 
ATOM   741  C  CA  . ILE   A  1 123 ? -18.852 -20.168 21.700 1.00 22.85  ? 98   ILE   A CA  1 
ATOM   742  C  C   . ILE   A  1 123 ? -17.410 -20.656 21.760 1.00 21.30  ? 98   ILE   A C   1 
ATOM   743  O  O   . ILE   A  1 123 ? -17.137 -21.852 21.600 1.00 26.97  ? 98   ILE   A O   1 
ATOM   744  C  CB  . ILE   A  1 123 ? -19.185 -19.546 20.331 1.00 21.84  ? 98   ILE   A CB  1 
ATOM   745  C  CG1 . ILE   A  1 123 ? -20.695 -19.360 20.186 1.00 28.57  ? 98   ILE   A CG1 1 
ATOM   746  C  CG2 . ILE   A  1 123 ? -18.637 -20.405 19.200 1.00 19.44  ? 98   ILE   A CG2 1 
ATOM   747  C  CD1 . ILE   A  1 123 ? -21.093 -18.507 19.007 1.00 18.69  ? 98   ILE   A CD1 1 
ATOM   748  N  N   . ALA   A  1 124 ? -16.465 -19.741 21.995 1.00 21.94  ? 99   ALA   A N   1 
ATOM   749  C  CA  . ALA   A  1 124 ? -15.062 -20.131 22.083 1.00 24.18  ? 99   ALA   A CA  1 
ATOM   750  C  C   . ALA   A  1 124 ? -14.840 -21.085 23.249 1.00 28.58  ? 99   ALA   A C   1 
ATOM   751  O  O   . ALA   A  1 124 ? -14.158 -22.107 23.112 1.00 26.11  ? 99   ALA   A O   1 
ATOM   752  C  CB  . ALA   A  1 124 ? -14.178 -18.891 22.222 1.00 13.16  ? 99   ALA   A CB  1 
ATOM   753  N  N   . ILE   A  1 125 ? -15.410 -20.760 24.411 1.00 26.54  ? 100  ILE   A N   1 
ATOM   754  C  CA  . ILE   A  1 125 ? -15.201 -21.585 25.595 1.00 32.88  ? 100  ILE   A CA  1 
ATOM   755  C  C   . ILE   A  1 125 ? -15.845 -22.951 25.401 1.00 32.87  ? 100  ILE   A C   1 
ATOM   756  O  O   . ILE   A  1 125 ? -15.281 -23.982 25.785 1.00 27.39  ? 100  ILE   A O   1 
ATOM   757  C  CB  . ILE   A  1 125 ? -15.753 -20.869 26.842 1.00 24.40  ? 100  ILE   A CB  1 
ATOM   758  C  CG1 . ILE   A  1 125 ? -14.872 -19.674 27.208 1.00 24.92  ? 100  ILE   A CG1 1 
ATOM   759  C  CG2 . ILE   A  1 125 ? -15.865 -21.831 28.019 1.00 23.52  ? 100  ILE   A CG2 1 
ATOM   760  C  CD1 . ILE   A  1 125 ? -15.475 -18.772 28.265 1.00 26.88  ? 100  ILE   A CD1 1 
ATOM   761  N  N   . ASP   A  1 126 ? -17.033 -22.977 24.793 1.00 27.32  ? 101  ASP   A N   1 
ATOM   762  C  CA  . ASP   A  1 126 ? -17.710 -24.236 24.503 1.00 25.69  ? 101  ASP   A CA  1 
ATOM   763  C  C   . ASP   A  1 126 ? -16.850 -25.150 23.638 1.00 26.28  ? 101  ASP   A C   1 
ATOM   764  O  O   . ASP   A  1 126 ? -16.723 -26.348 23.914 1.00 26.00  ? 101  ASP   A O   1 
ATOM   765  C  CB  . ASP   A  1 126 ? -19.043 -23.946 23.812 1.00 28.27  ? 101  ASP   A CB  1 
ATOM   766  C  CG  . ASP   A  1 126 ? -19.760 -25.203 23.368 1.00 29.19  ? 101  ASP   A CG  1 
ATOM   767  O  OD1 . ASP   A  1 126 ? -20.371 -25.870 24.227 1.00 37.88  ? 101  ASP   A OD1 1 
ATOM   768  O  OD2 . ASP   A  1 126 ? -19.729 -25.515 22.158 1.00 37.18  ? 101  ASP   A OD2 1 
ATOM   769  N  N   . ARG   A  1 127 ? -16.257 -24.600 22.577 1.00 21.43  ? 102  ARG   A N   1 
ATOM   770  C  CA  . ARG   A  1 127 ? -15.408 -25.403 21.705 1.00 26.30  ? 102  ARG   A CA  1 
ATOM   771  C  C   . ARG   A  1 127 ? -14.128 -25.852 22.407 1.00 32.80  ? 102  ARG   A C   1 
ATOM   772  O  O   . ARG   A  1 127 ? -13.602 -26.930 22.100 1.00 27.51  ? 102  ARG   A O   1 
ATOM   773  C  CB  . ARG   A  1 127 ? -15.110 -24.620 20.426 1.00 21.53  ? 102  ARG   A CB  1 
ATOM   774  C  CG  . ARG   A  1 127 ? -16.363 -24.291 19.580 1.00 28.99  ? 102  ARG   A CG  1 
ATOM   775  C  CD  . ARG   A  1 127 ? -17.070 -25.530 19.022 1.00 33.54  ? 102  ARG   A CD  1 
ATOM   776  N  NE  . ARG   A  1 127 ? -17.911 -26.211 20.001 1.00 44.88  ? 102  ARG   A NE  1 
ATOM   777  C  CZ  . ARG   A  1 127 ? -18.056 -27.526 20.078 1.00 32.95  ? 102  ARG   A CZ  1 
ATOM   778  N  NH1 . ARG   A  1 127 ? -17.419 -28.339 19.253 1.00 31.89  ? 102  ARG   A NH1 1 
ATOM   779  N  NH2 . ARG   A  1 127 ? -18.871 -28.036 20.997 1.00 35.17  ? 102  ARG   A NH2 1 
ATOM   780  N  N   . TYR   A  1 128 ? -13.607 -25.048 23.339 1.00 21.44  ? 103  TYR   A N   1 
ATOM   781  C  CA  . TYR   A  1 128 ? -12.436 -25.475 24.100 1.00 35.12  ? 103  TYR   A CA  1 
ATOM   782  C  C   . TYR   A  1 128 ? -12.771 -26.654 25.006 1.00 35.23  ? 103  TYR   A C   1 
ATOM   783  O  O   . TYR   A  1 128 ? -11.992 -27.611 25.105 1.00 35.50  ? 103  TYR   A O   1 
ATOM   784  C  CB  . TYR   A  1 128 ? -11.863 -24.317 24.916 1.00 28.61  ? 103  TYR   A CB  1 
ATOM   785  C  CG  . TYR   A  1 128 ? -10.705 -24.742 25.788 1.00 34.31  ? 103  TYR   A CG  1 
ATOM   786  C  CD1 . TYR   A  1 128 ? -9.449  -24.965 25.238 1.00 31.06  ? 103  TYR   A CD1 1 
ATOM   787  C  CD2 . TYR   A  1 128 ? -10.864 -24.930 27.155 1.00 48.39  ? 103  TYR   A CD2 1 
ATOM   788  C  CE1 . TYR   A  1 128 ? -8.383  -25.355 26.022 1.00 45.06  ? 103  TYR   A CE1 1 
ATOM   789  C  CE2 . TYR   A  1 128 ? -9.802  -25.324 27.949 1.00 42.97  ? 103  TYR   A CE2 1 
ATOM   790  C  CZ  . TYR   A  1 128 ? -8.564  -25.533 27.377 1.00 51.48  ? 103  TYR   A CZ  1 
ATOM   791  O  OH  . TYR   A  1 128 ? -7.502  -25.932 28.156 1.00 53.56  ? 103  TYR   A OH  1 
ATOM   792  N  N   . ILE   A  1 129 ? -13.918 -26.594 25.684 1.00 30.80  ? 104  ILE   A N   1 
ATOM   793  C  CA  . ILE   A  1 129 ? -14.351 -27.707 26.524 1.00 31.55  ? 104  ILE   A CA  1 
ATOM   794  C  C   . ILE   A  1 129 ? -14.506 -28.973 25.693 1.00 38.22  ? 104  ILE   A C   1 
ATOM   795  O  O   . ILE   A  1 129 ? -14.133 -30.069 26.129 1.00 37.19  ? 104  ILE   A O   1 
ATOM   796  C  CB  . ILE   A  1 129 ? -15.656 -27.351 27.261 1.00 30.88  ? 104  ILE   A CB  1 
ATOM   797  C  CG1 . ILE   A  1 129 ? -15.456 -26.123 28.154 1.00 24.27  ? 104  ILE   A CG1 1 
ATOM   798  C  CG2 . ILE   A  1 129 ? -16.155 -28.534 28.079 1.00 39.90  ? 104  ILE   A CG2 1 
ATOM   799  C  CD1 . ILE   A  1 129 ? -16.747 -25.536 28.686 1.00 25.25  ? 104  ILE   A CD1 1 
ATOM   800  N  N   . ALA   A  1 130 ? -15.060 -28.846 24.485 1.00 28.62  ? 105  ALA   A N   1 
ATOM   801  C  CA  . ALA   A  1 130 ? -15.286 -30.017 23.645 1.00 29.32  ? 105  ALA   A CA  1 
ATOM   802  C  C   . ALA   A  1 130 ? -13.977 -30.673 23.216 1.00 37.07  ? 105  ALA   A C   1 
ATOM   803  O  O   . ALA   A  1 130 ? -13.902 -31.903 23.112 1.00 50.78  ? 105  ALA   A O   1 
ATOM   804  C  CB  . ALA   A  1 130 ? -16.114 -29.629 22.419 1.00 27.75  ? 105  ALA   A CB  1 
ATOM   805  N  N   . ILE   A  1 131 ? -12.937 -29.881 22.962 1.00 32.41  ? 106  ILE   A N   1 
ATOM   806  C  CA  . ILE   A  1 131 ? -11.667 -30.459 22.529 1.00 36.44  ? 106  ILE   A CA  1 
ATOM   807  C  C   . ILE   A  1 131 ? -10.789 -30.912 23.697 1.00 41.05  ? 106  ILE   A C   1 
ATOM   808  O  O   . ILE   A  1 131 ? -9.985  -31.837 23.538 1.00 36.20  ? 106  ILE   A O   1 
ATOM   809  C  CB  . ILE   A  1 131 ? -10.910 -29.484 21.611 1.00 41.24  ? 106  ILE   A CB  1 
ATOM   810  C  CG1 . ILE   A  1 131 ? -9.847  -30.242 20.814 1.00 41.71  ? 106  ILE   A CG1 1 
ATOM   811  C  CG2 . ILE   A  1 131 ? -10.271 -28.358 22.408 1.00 39.08  ? 106  ILE   A CG2 1 
ATOM   812  C  CD1 . ILE   A  1 131 ? -9.588  -29.668 19.449 1.00 50.26  ? 106  ILE   A CD1 1 
ATOM   813  N  N   . ALA   A  1 132 ? -10.920 -30.296 24.871 1.00 32.08  ? 107  ALA   A N   1 
ATOM   814  C  CA  . ALA   A  1 132 ? -9.975  -30.560 25.947 1.00 43.17  ? 107  ALA   A CA  1 
ATOM   815  C  C   . ALA   A  1 132 ? -10.472 -31.631 26.905 1.00 46.97  ? 107  ALA   A C   1 
ATOM   816  O  O   . ALA   A  1 132 ? -9.660  -32.396 27.443 1.00 47.83  ? 107  ALA   A O   1 
ATOM   817  C  CB  . ALA   A  1 132 ? -9.683  -29.272 26.724 1.00 35.66  ? 107  ALA   A CB  1 
ATOM   818  N  N   . ILE   A  1 133 ? -11.778 -31.685 27.146 1.00 37.13  ? 108  ILE   A N   1 
ATOM   819  C  CA  . ILE   A  1 133 ? -12.398 -32.719 27.972 1.00 38.83  ? 108  ILE   A CA  1 
ATOM   820  C  C   . ILE   A  1 133 ? -13.663 -33.236 27.285 1.00 40.08  ? 108  ILE   A C   1 
ATOM   821  O  O   . ILE   A  1 133 ? -14.774 -33.058 27.811 1.00 41.77  ? 108  ILE   A O   1 
ATOM   822  C  CB  . ILE   A  1 133 ? -12.669 -32.172 29.384 1.00 46.91  ? 108  ILE   A CB  1 
ATOM   823  C  CG1 . ILE   A  1 133 ? -13.257 -30.759 29.290 1.00 43.51  ? 108  ILE   A CG1 1 
ATOM   824  C  CG2 . ILE   A  1 133 ? -11.384 -32.183 30.218 1.00 44.31  ? 108  ILE   A CG2 1 
ATOM   825  C  CD1 . ILE   A  1 133 ? -13.834 -30.225 30.586 1.00 55.14  ? 108  ILE   A CD1 1 
ATOM   826  N  N   . PRO   A  1 134 ? -13.542 -33.882 26.117 1.00 35.42  ? 109  PRO   A N   1 
ATOM   827  C  CA  . PRO   A  1 134 ? -14.740 -34.354 25.395 1.00 40.44  ? 109  PRO   A CA  1 
ATOM   828  C  C   . PRO   A  1 134 ? -15.557 -35.385 26.158 1.00 51.00  ? 109  PRO   A C   1 
ATOM   829  O  O   . PRO   A  1 134 ? -16.747 -35.549 25.860 1.00 44.50  ? 109  PRO   A O   1 
ATOM   830  C  CB  . PRO   A  1 134 ? -14.153 -34.985 24.117 1.00 27.36  ? 109  PRO   A CB  1 
ATOM   831  C  CG  . PRO   A  1 134 ? -12.724 -35.295 24.468 1.00 32.12  ? 109  PRO   A CG  1 
ATOM   832  C  CD  . PRO   A  1 134 ? -12.297 -34.213 25.401 1.00 33.27  ? 109  PRO   A CD  1 
ATOM   833  N  N   . LEU   A  1 135 ? -14.947 -36.092 27.111 1.00 56.45  ? 110  LEU   A N   1 
ATOM   834  C  CA  . LEU   A  1 135 ? -15.633 -37.141 27.843 1.00 60.22  ? 110  LEU   A CA  1 
ATOM   835  C  C   . LEU   A  1 135 ? -16.686 -36.594 28.797 1.00 54.86  ? 110  LEU   A C   1 
ATOM   836  O  O   . LEU   A  1 135 ? -17.656 -37.300 29.099 1.00 58.68  ? 110  LEU   A O   1 
ATOM   837  C  CB  . LEU   A  1 135 ? -14.623 -37.995 28.615 1.00 72.37  ? 110  LEU   A CB  1 
ATOM   838  C  CG  . LEU   A  1 135 ? -13.624 -38.794 27.787 1.00 77.43  ? 110  LEU   A CG  1 
ATOM   839  C  CD1 . LEU   A  1 135 ? -12.691 -39.546 28.729 1.00 69.49  ? 110  LEU   A CD1 1 
ATOM   840  C  CD2 . LEU   A  1 135 ? -14.380 -39.757 26.911 1.00 68.46  ? 110  LEU   A CD2 1 
ATOM   841  N  N   . ARG   A  1 136 ? -16.531 -35.351 29.254 1.00 52.07  ? 111  ARG   A N   1 
ATOM   842  C  CA  . ARG   A  1 136 ? -17.445 -34.717 30.195 1.00 53.80  ? 111  ARG   A CA  1 
ATOM   843  C  C   . ARG   A  1 136 ? -18.179 -33.529 29.583 1.00 57.21  ? 111  ARG   A C   1 
ATOM   844  O  O   . ARG   A  1 136 ? -18.883 -32.812 30.301 1.00 45.08  ? 111  ARG   A O   1 
ATOM   845  C  CB  . ARG   A  1 136 ? -16.677 -34.262 31.438 1.00 54.83  ? 111  ARG   A CB  1 
ATOM   846  C  CG  . ARG   A  1 136 ? -15.634 -35.267 31.897 1.00 59.93  ? 111  ARG   A CG  1 
ATOM   847  N  N   . TYR   A  1 137 ? -18.013 -33.284 28.281 1.00 50.21  ? 112  TYR   A N   1 
ATOM   848  C  CA  . TYR   A  1 137 ? -18.712 -32.168 27.651 1.00 41.83  ? 112  TYR   A CA  1 
ATOM   849  C  C   . TYR   A  1 137 ? -20.223 -32.284 27.842 1.00 46.26  ? 112  TYR   A C   1 
ATOM   850  O  O   . TYR   A  1 137 ? -20.864 -31.373 28.377 1.00 42.30  ? 112  TYR   A O   1 
ATOM   851  C  CB  . TYR   A  1 137 ? -18.336 -32.085 26.170 1.00 29.82  ? 112  TYR   A CB  1 
ATOM   852  C  CG  . TYR   A  1 137 ? -19.116 -31.051 25.386 1.00 40.13  ? 112  TYR   A CG  1 
ATOM   853  C  CD1 . TYR   A  1 137 ? -18.679 -29.732 25.319 1.00 34.22  ? 112  TYR   A CD1 1 
ATOM   854  C  CD2 . TYR   A  1 137 ? -20.273 -31.392 24.701 1.00 36.52  ? 112  TYR   A CD2 1 
ATOM   855  C  CE1 . TYR   A  1 137 ? -19.381 -28.784 24.605 1.00 32.11  ? 112  TYR   A CE1 1 
ATOM   856  C  CE2 . TYR   A  1 137 ? -20.981 -30.451 23.985 1.00 52.75  ? 112  TYR   A CE2 1 
ATOM   857  C  CZ  . TYR   A  1 137 ? -20.530 -29.150 23.940 1.00 37.86  ? 112  TYR   A CZ  1 
ATOM   858  O  OH  . TYR   A  1 137 ? -21.233 -28.209 23.226 1.00 40.42  ? 112  TYR   A OH  1 
ATOM   859  N  N   . ASN   A  1 138 ? -20.812 -33.397 27.396 1.00 48.81  ? 113  ASN   A N   1 
ATOM   860  C  CA  . ASN   A  1 138 ? -22.269 -33.512 27.400 1.00 60.88  ? 113  ASN   A CA  1 
ATOM   861  C  C   . ASN   A  1 138 ? -22.843 -33.437 28.810 1.00 59.89  ? 113  ASN   A C   1 
ATOM   862  O  O   . ASN   A  1 138 ? -23.971 -32.966 28.997 1.00 58.51  ? 113  ASN   A O   1 
ATOM   863  C  CB  . ASN   A  1 138 ? -22.714 -34.797 26.704 1.00 53.20  ? 113  ASN   A CB  1 
ATOM   864  C  CG  . ASN   A  1 138 ? -22.661 -34.687 25.192 1.00 66.97  ? 113  ASN   A CG  1 
ATOM   865  O  OD1 . ASN   A  1 138 ? -22.861 -33.611 24.625 1.00 58.89  ? 113  ASN   A OD1 1 
ATOM   866  N  ND2 . ASN   A  1 138 ? -22.458 -35.817 24.527 1.00 76.65  ? 113  ASN   A ND2 1 
ATOM   867  N  N   . GLY   A  1 139 ? -22.098 -33.912 29.810 1.00 50.26  ? 114  GLY   A N   1 
ATOM   868  C  CA  . GLY   A  1 139 ? -22.567 -33.787 31.178 1.00 48.42  ? 114  GLY   A CA  1 
ATOM   869  C  C   . GLY   A  1 139 ? -22.337 -32.415 31.769 1.00 52.95  ? 114  GLY   A C   1 
ATOM   870  O  O   . GLY   A  1 139 ? -23.053 -32.008 32.689 1.00 55.19  ? 114  GLY   A O   1 
ATOM   871  N  N   . LEU   A  1 140 ? -21.349 -31.681 31.258 1.00 51.37  ? 115  LEU   A N   1 
ATOM   872  C  CA  . LEU   A  1 140 ? -21.035 -30.349 31.762 1.00 53.92  ? 115  LEU   A CA  1 
ATOM   873  C  C   . LEU   A  1 140 ? -21.841 -29.265 31.060 1.00 54.74  ? 115  LEU   A C   1 
ATOM   874  O  O   . LEU   A  1 140 ? -22.331 -28.331 31.705 1.00 50.21  ? 115  LEU   A O   1 
ATOM   875  C  CB  . LEU   A  1 140 ? -19.537 -30.071 31.609 1.00 46.87  ? 115  LEU   A CB  1 
ATOM   876  C  CG  . LEU   A  1 140 ? -19.030 -28.636 31.771 1.00 60.30  ? 115  LEU   A CG  1 
ATOM   877  C  CD1 . LEU   A  1 140 ? -19.422 -28.055 33.124 1.00 60.21  ? 115  LEU   A CD1 1 
ATOM   878  C  CD2 . LEU   A  1 140 ? -17.520 -28.575 31.573 1.00 53.13  ? 115  LEU   A CD2 1 
ATOM   879  N  N   . VAL   A  1 141 ? -21.985 -29.381 29.744 1.00 47.03  ? 116  VAL   A N   1 
ATOM   880  C  CA  . VAL   A  1 141 ? -22.534 -28.334 28.890 1.00 38.19  ? 116  VAL   A CA  1 
ATOM   881  C  C   . VAL   A  1 141 ? -23.902 -28.815 28.417 1.00 38.16  ? 116  VAL   A C   1 
ATOM   882  O  O   . VAL   A  1 141 ? -24.003 -29.622 27.485 1.00 43.20  ? 116  VAL   A O   1 
ATOM   883  C  CB  . VAL   A  1 141 ? -21.600 -28.016 27.715 1.00 46.79  ? 116  VAL   A CB  1 
ATOM   884  C  CG1 . VAL   A  1 141 ? -22.108 -26.823 26.935 1.00 33.58  ? 116  VAL   A CG1 1 
ATOM   885  C  CG2 . VAL   A  1 141 ? -20.183 -27.780 28.207 1.00 43.18  ? 116  VAL   A CG2 1 
ATOM   886  N  N   . THR   A  1 142 ? -24.958 -28.313 29.050 1.00 37.73  ? 117  THR   A N   1 
ATOM   887  C  CA  . THR   A  1 142 ? -26.321 -28.740 28.792 1.00 38.29  ? 117  THR   A CA  1 
ATOM   888  C  C   . THR   A  1 142 ? -27.138 -27.599 28.209 1.00 39.92  ? 117  THR   A C   1 
ATOM   889  O  O   . THR   A  1 142 ? -26.785 -26.424 28.333 1.00 40.83  ? 117  THR   A O   1 
ATOM   890  C  CB  . THR   A  1 142 ? -26.994 -29.211 30.081 1.00 38.51  ? 117  THR   A CB  1 
ATOM   891  O  OG1 . THR   A  1 142 ? -27.165 -28.080 30.955 1.00 45.48  ? 117  THR   A OG1 1 
ATOM   892  C  CG2 . THR   A  1 142 ? -26.159 -30.286 30.762 1.00 41.50  ? 117  THR   A CG2 1 
ATOM   893  N  N   . GLY   A  1 143 ? -28.240 -27.967 27.552 1.00 39.69  ? 118  GLY   A N   1 
ATOM   894  C  CA  . GLY   A  1 143 ? -29.106 -26.961 26.958 1.00 31.14  ? 118  GLY   A CA  1 
ATOM   895  C  C   . GLY   A  1 143 ? -29.697 -26.015 27.985 1.00 41.33  ? 118  GLY   A C   1 
ATOM   896  O  O   . GLY   A  1 143 ? -29.794 -24.809 27.747 1.00 46.65  ? 118  GLY   A O   1 
ATOM   897  N  N   . THR   A  1 144 ? -30.096 -26.552 29.141 1.00 36.35  ? 119  THR   A N   1 
ATOM   898  C  CA  . THR   A  1 144 ? -30.684 -25.720 30.186 1.00 35.75  ? 119  THR   A CA  1 
ATOM   899  C  C   . THR   A  1 144 ? -29.667 -24.745 30.761 1.00 40.78  ? 119  THR   A C   1 
ATOM   900  O  O   . THR   A  1 144 ? -29.999 -23.588 31.042 1.00 44.36  ? 119  THR   A O   1 
ATOM   901  C  CB  . THR   A  1 144 ? -31.259 -26.593 31.303 1.00 47.16  ? 119  THR   A CB  1 
ATOM   902  O  OG1 . THR   A  1 144 ? -32.203 -27.519 30.755 1.00 56.22  ? 119  THR   A OG1 1 
ATOM   903  C  CG2 . THR   A  1 144 ? -31.951 -25.733 32.357 1.00 57.72  ? 119  THR   A CG2 1 
ATOM   904  N  N   . ARG   A  1 145 ? -28.422 -25.189 30.937 1.00 33.90  ? 120  ARG   A N   1 
ATOM   905  C  CA  . ARG   A  1 145 ? -27.385 -24.286 31.426 1.00 43.29  ? 120  ARG   A CA  1 
ATOM   906  C  C   . ARG   A  1 145 ? -27.035 -23.233 30.386 1.00 34.28  ? 120  ARG   A C   1 
ATOM   907  O  O   . ARG   A  1 145 ? -26.792 -22.071 30.732 1.00 41.74  ? 120  ARG   A O   1 
ATOM   908  C  CB  . ARG   A  1 145 ? -26.152 -25.086 31.834 1.00 33.74  ? 120  ARG   A CB  1 
ATOM   909  C  CG  . ARG   A  1 145 ? -26.380 -25.892 33.093 1.00 51.82  ? 120  ARG   A CG  1 
ATOM   910  C  CD  . ARG   A  1 145 ? -25.213 -26.798 33.409 1.00 50.39  ? 120  ARG   A CD  1 
ATOM   911  N  NE  . ARG   A  1 145 ? -25.575 -27.753 34.448 1.00 60.64  ? 120  ARG   A NE  1 
ATOM   912  C  CZ  . ARG   A  1 145 ? -24.875 -28.837 34.748 1.00 59.53  ? 120  ARG   A CZ  1 
ATOM   913  N  NH1 . ARG   A  1 145 ? -23.762 -29.142 34.102 1.00 46.90  ? 120  ARG   A NH1 1 
ATOM   914  N  NH2 . ARG   A  1 145 ? -25.305 -29.639 35.718 1.00 67.41  ? 120  ARG   A NH2 1 
ATOM   915  N  N   . ALA   A  1 146 ? -26.995 -23.617 29.107 1.00 36.50  ? 121  ALA   A N   1 
ATOM   916  C  CA  . ALA   A  1 146 ? -26.760 -22.626 28.066 1.00 32.70  ? 121  ALA   A CA  1 
ATOM   917  C  C   . ALA   A  1 146 ? -27.847 -21.561 28.083 1.00 36.38  ? 121  ALA   A C   1 
ATOM   918  O  O   . ALA   A  1 146 ? -27.555 -20.365 27.970 1.00 32.83  ? 121  ALA   A O   1 
ATOM   919  C  CB  . ALA   A  1 146 ? -26.690 -23.302 26.698 1.00 32.17  ? 121  ALA   A CB  1 
ATOM   920  N  N   . ALA   A  1 147 ? -29.109 -21.976 28.229 1.00 31.14  ? 122  ALA   A N   1 
ATOM   921  C  CA  . ALA   A  1 147 ? -30.200 -21.009 28.206 1.00 35.96  ? 122  ALA   A CA  1 
ATOM   922  C  C   . ALA   A  1 147 ? -30.129 -20.076 29.408 1.00 37.43  ? 122  ALA   A C   1 
ATOM   923  O  O   . ALA   A  1 147 ? -30.441 -18.885 29.296 1.00 31.09  ? 122  ALA   A O   1 
ATOM   924  C  CB  . ALA   A  1 147 ? -31.545 -21.733 28.162 1.00 25.61  ? 122  ALA   A CB  1 
ATOM   925  N  N   . GLY   A  1 148 ? -29.728 -20.601 30.569 1.00 33.05  ? 123  GLY   A N   1 
ATOM   926  C  CA  . GLY   A  1 148 ? -29.537 -19.745 31.728 1.00 26.27  ? 123  GLY   A CA  1 
ATOM   927  C  C   . GLY   A  1 148 ? -28.392 -18.767 31.552 1.00 25.03  ? 123  GLY   A C   1 
ATOM   928  O  O   . GLY   A  1 148 ? -28.505 -17.593 31.914 1.00 25.01  ? 123  GLY   A O   1 
ATOM   929  N  N   . ILE   A  1 149 ? -27.267 -19.242 31.009 1.00 27.33  ? 124  ILE   A N   1 
ATOM   930  C  CA  . ILE   A  1 149 ? -26.132 -18.363 30.739 1.00 32.48  ? 124  ILE   A CA  1 
ATOM   931  C  C   . ILE   A  1 149 ? -26.523 -17.266 29.757 1.00 28.59  ? 124  ILE   A C   1 
ATOM   932  O  O   . ILE   A  1 149 ? -26.179 -16.092 29.945 1.00 29.93  ? 124  ILE   A O   1 
ATOM   933  C  CB  . ILE   A  1 149 ? -24.925 -19.180 30.241 1.00 32.58  ? 124  ILE   A CB  1 
ATOM   934  C  CG1 . ILE   A  1 149 ? -24.397 -20.078 31.364 1.00 30.62  ? 124  ILE   A CG1 1 
ATOM   935  C  CG2 . ILE   A  1 149 ? -23.829 -18.261 29.723 1.00 27.12  ? 124  ILE   A CG2 1 
ATOM   936  C  CD1 . ILE   A  1 149 ? -23.516 -21.214 30.888 1.00 42.13  ? 124  ILE   A CD1 1 
ATOM   937  N  N   . ILE   A  1 150 ? -27.245 -17.631 28.693 1.00 25.67  ? 125  ILE   A N   1 
ATOM   938  C  CA  . ILE   A  1 150 ? -27.685 -16.644 27.710 1.00 32.80  ? 125  ILE   A CA  1 
ATOM   939  C  C   . ILE   A  1 150 ? -28.567 -15.589 28.364 1.00 24.56  ? 125  ILE   A C   1 
ATOM   940  O  O   . ILE   A  1 150 ? -28.423 -14.388 28.101 1.00 21.84  ? 125  ILE   A O   1 
ATOM   941  C  CB  . ILE   A  1 150 ? -28.404 -17.342 26.539 1.00 29.11  ? 125  ILE   A CB  1 
ATOM   942  C  CG1 . ILE   A  1 150 ? -27.412 -18.191 25.740 1.00 24.31  ? 125  ILE   A CG1 1 
ATOM   943  C  CG2 . ILE   A  1 150 ? -29.107 -16.325 25.652 1.00 21.39  ? 125  ILE   A CG2 1 
ATOM   944  C  CD1 . ILE   A  1 150 ? -28.065 -19.160 24.777 1.00 21.36  ? 125  ILE   A CD1 1 
ATOM   945  N  N   . ALA   A  1 151 ? -29.492 -16.016 29.227 1.00 24.44  ? 126  ALA   A N   1 
ATOM   946  C  CA  . ALA   A  1 151 ? -30.340 -15.064 29.937 1.00 26.00  ? 126  ALA   A CA  1 
ATOM   947  C  C   . ALA   A  1 151 ? -29.502 -14.124 30.796 1.00 21.94  ? 126  ALA   A C   1 
ATOM   948  O  O   . ALA   A  1 151 ? -29.714 -12.905 30.796 1.00 23.75  ? 126  ALA   A O   1 
ATOM   949  C  CB  . ALA   A  1 151 ? -31.367 -15.810 30.791 1.00 22.73  ? 126  ALA   A CB  1 
ATOM   950  N  N   . ILE   A  1 152 ? -28.550 -14.682 31.548 1.00 23.33  ? 127  ILE   A N   1 
ATOM   951  C  CA  . ILE   A  1 152 ? -27.685 -13.871 32.402 1.00 25.33  ? 127  ILE   A CA  1 
ATOM   952  C  C   . ILE   A  1 152 ? -26.888 -12.874 31.571 1.00 23.36  ? 127  ILE   A C   1 
ATOM   953  O  O   . ILE   A  1 152 ? -26.754 -11.700 31.940 1.00 22.88  ? 127  ILE   A O   1 
ATOM   954  C  CB  . ILE   A  1 152 ? -26.763 -14.780 33.237 1.00 26.33  ? 127  ILE   A CB  1 
ATOM   955  C  CG1 . ILE   A  1 152 ? -27.567 -15.498 34.322 1.00 33.98  ? 127  ILE   A CG1 1 
ATOM   956  C  CG2 . ILE   A  1 152 ? -25.622 -13.978 33.846 1.00 28.10  ? 127  ILE   A CG2 1 
ATOM   957  C  CD1 . ILE   A  1 152 ? -26.777 -16.548 35.067 1.00 41.79  ? 127  ILE   A CD1 1 
ATOM   958  N  N   . CYS   A  1 153 ? -26.356 -13.321 30.431 1.00 26.13  ? 128  CYS   A N   1 
ATOM   959  C  CA  . CYS   A  1 153 ? -25.525 -12.449 29.605 1.00 26.10  ? 128  CYS   A CA  1 
ATOM   960  C  C   . CYS   A  1 153 ? -26.336 -11.300 29.019 1.00 24.92  ? 128  CYS   A C   1 
ATOM   961  O  O   . CYS   A  1 153 ? -25.822 -10.185 28.873 1.00 19.11  ? 128  CYS   A O   1 
ATOM   962  C  CB  . CYS   A  1 153 ? -24.844 -13.262 28.506 1.00 19.41  ? 128  CYS   A CB  1 
ATOM   963  S  SG  . CYS   A  1 153 ? -23.518 -14.331 29.121 1.00 29.92  ? 128  CYS   A SG  1 
ATOM   964  N  N   . TRP   A  1 154 ? -27.599 -11.552 28.668 1.00 17.26  ? 129  TRP   A N   1 
ATOM   965  C  CA  . TRP   A  1 154 ? -28.445 -10.472 28.169 1.00 22.09  ? 129  TRP   A CA  1 
ATOM   966  C  C   . TRP   A  1 154 ? -28.716 -9.444  29.260 1.00 22.28  ? 129  TRP   A C   1 
ATOM   967  O  O   . TRP   A  1 154 ? -28.738 -8.237  28.990 1.00 17.84  ? 129  TRP   A O   1 
ATOM   968  C  CB  . TRP   A  1 154 ? -29.754 -11.030 27.609 1.00 16.52  ? 129  TRP   A CB  1 
ATOM   969  C  CG  . TRP   A  1 154 ? -29.656 -11.433 26.167 1.00 26.75  ? 129  TRP   A CG  1 
ATOM   970  C  CD1 . TRP   A  1 154 ? -29.501 -12.694 25.671 1.00 22.53  ? 129  TRP   A CD1 1 
ATOM   971  C  CD2 . TRP   A  1 154 ? -29.708 -10.559 25.033 1.00 20.06  ? 129  TRP   A CD2 1 
ATOM   972  N  NE1 . TRP   A  1 154 ? -29.453 -12.659 24.297 1.00 26.88  ? 129  TRP   A NE1 1 
ATOM   973  C  CE2 . TRP   A  1 154 ? -29.578 -11.360 23.881 1.00 23.72  ? 129  TRP   A CE2 1 
ATOM   974  C  CE3 . TRP   A  1 154 ? -29.851 -9.176  24.880 1.00 23.29  ? 129  TRP   A CE3 1 
ATOM   975  C  CZ2 . TRP   A  1 154 ? -29.586 -10.824 22.594 1.00 22.92  ? 129  TRP   A CZ2 1 
ATOM   976  C  CZ3 . TRP   A  1 154 ? -29.860 -8.646  23.603 1.00 22.88  ? 129  TRP   A CZ3 1 
ATOM   977  C  CH2 . TRP   A  1 154 ? -29.728 -9.468  22.476 1.00 23.72  ? 129  TRP   A CH2 1 
ATOM   978  N  N   . VAL   A  1 155 ? -28.934 -9.900  30.495 1.00 20.18  ? 130  VAL   A N   1 
ATOM   979  C  CA  . VAL   A  1 155 ? -29.126 -8.972  31.607 1.00 16.81  ? 130  VAL   A CA  1 
ATOM   980  C  C   . VAL   A  1 155 ? -27.874 -8.128  31.815 1.00 19.80  ? 130  VAL   A C   1 
ATOM   981  O  O   . VAL   A  1 155 ? -27.948 -6.903  31.974 1.00 18.00  ? 130  VAL   A O   1 
ATOM   982  C  CB  . VAL   A  1 155 ? -29.506 -9.738  32.886 1.00 23.89  ? 130  VAL   A CB  1 
ATOM   983  C  CG1 . VAL   A  1 155 ? -29.499 -8.803  34.085 1.00 22.10  ? 130  VAL   A CG1 1 
ATOM   984  C  CG2 . VAL   A  1 155 ? -30.867 -10.395 32.727 1.00 21.84  ? 130  VAL   A CG2 1 
ATOM   985  N  N   . LEU   A  1 156 ? -26.702 -8.770  31.812 1.00 19.93  ? 131  LEU   A N   1 
ATOM   986  C  CA  . LEU   A  1 156 ? -25.457 -8.027  31.983 1.00 17.05  ? 131  LEU   A CA  1 
ATOM   987  C  C   . LEU   A  1 156 ? -25.181 -7.107  30.801 1.00 22.59  ? 131  LEU   A C   1 
ATOM   988  O  O   . LEU   A  1 156 ? -24.547 -6.059  30.970 1.00 26.37  ? 131  LEU   A O   1 
ATOM   989  C  CB  . LEU   A  1 156 ? -24.288 -8.991  32.185 1.00 20.74  ? 131  LEU   A CB  1 
ATOM   990  C  CG  . LEU   A  1 156 ? -24.371 -9.907  33.407 1.00 30.89  ? 131  LEU   A CG  1 
ATOM   991  C  CD1 . LEU   A  1 156 ? -23.313 -10.997 33.335 1.00 25.69  ? 131  LEU   A CD1 1 
ATOM   992  C  CD2 . LEU   A  1 156 ? -24.236 -9.104  34.691 1.00 27.86  ? 131  LEU   A CD2 1 
ATOM   993  N  N   . SER   A  1 157 ? -25.642 -7.477  29.604 1.00 19.21  ? 132  SER   A N   1 
ATOM   994  C  CA  . SER   A  1 157 ? -25.450 -6.614  28.444 1.00 19.27  ? 132  SER   A CA  1 
ATOM   995  C  C   . SER   A  1 157 ? -26.244 -5.324  28.582 1.00 20.41  ? 132  SER   A C   1 
ATOM   996  O  O   . SER   A  1 157 ? -25.775 -4.252  28.180 1.00 19.28  ? 132  SER   A O   1 
ATOM   997  C  CB  . SER   A  1 157 ? -25.848 -7.355  27.169 1.00 19.47  ? 132  SER   A CB  1 
ATOM   998  O  OG  . SER   A  1 157 ? -24.993 -8.461  26.951 1.00 20.66  ? 132  SER   A OG  1 
ATOM   999  N  N   . PHE   A  1 158 ? -27.452 -5.406  29.144 1.00 17.42  ? 133  PHE   A N   1 
ATOM   1000 C  CA  . PHE   A  1 158 ? -28.223 -4.195  29.399 1.00 17.52  ? 133  PHE   A CA  1 
ATOM   1001 C  C   . PHE   A  1 158 ? -27.539 -3.322  30.443 1.00 22.65  ? 133  PHE   A C   1 
ATOM   1002 O  O   . PHE   A  1 158 ? -27.495 -2.095  30.301 1.00 22.92  ? 133  PHE   A O   1 
ATOM   1003 C  CB  . PHE   A  1 158 ? -29.641 -4.561  29.835 1.00 20.11  ? 133  PHE   A CB  1 
ATOM   1004 C  CG  . PHE   A  1 158 ? -30.591 -4.755  28.689 1.00 29.00  ? 133  PHE   A CG  1 
ATOM   1005 C  CD1 . PHE   A  1 158 ? -31.260 -3.677  28.135 1.00 19.63  ? 133  PHE   A CD1 1 
ATOM   1006 C  CD2 . PHE   A  1 158 ? -30.802 -6.015  28.153 1.00 25.47  ? 133  PHE   A CD2 1 
ATOM   1007 C  CE1 . PHE   A  1 158 ? -32.132 -3.852  27.078 1.00 24.79  ? 133  PHE   A CE1 1 
ATOM   1008 C  CE2 . PHE   A  1 158 ? -31.673 -6.198  27.095 1.00 25.17  ? 133  PHE   A CE2 1 
ATOM   1009 C  CZ  . PHE   A  1 158 ? -32.338 -5.114  26.557 1.00 24.93  ? 133  PHE   A CZ  1 
ATOM   1010 N  N   . ALA   A  1 159 ? -27.007 -3.936  31.503 1.00 21.06  ? 134  ALA   A N   1 
ATOM   1011 C  CA  . ALA   A  1 159 ? -26.362 -3.159  32.557 1.00 25.24  ? 134  ALA   A CA  1 
ATOM   1012 C  C   . ALA   A  1 159 ? -25.115 -2.459  32.033 1.00 24.59  ? 134  ALA   A C   1 
ATOM   1013 O  O   . ALA   A  1 159 ? -24.880 -1.283  32.335 1.00 21.34  ? 134  ALA   A O   1 
ATOM   1014 C  CB  . ALA   A  1 159 ? -26.016 -4.062  33.740 1.00 20.68  ? 134  ALA   A CB  1 
ATOM   1015 N  N   . ILE   A  1 160 ? -24.306 -3.168  31.245 1.00 17.49  ? 135  ILE   A N   1 
ATOM   1016 C  CA  . ILE   A  1 160 ? -23.096 -2.574  30.684 1.00 17.98  ? 135  ILE   A CA  1 
ATOM   1017 C  C   . ILE   A  1 160 ? -23.451 -1.510  29.652 1.00 20.63  ? 135  ILE   A C   1 
ATOM   1018 O  O   . ILE   A  1 160 ? -22.941 -0.384  29.697 1.00 14.51  ? 135  ILE   A O   1 
ATOM   1019 C  CB  . ILE   A  1 160 ? -22.197 -3.667  30.081 1.00 21.26  ? 135  ILE   A CB  1 
ATOM   1020 C  CG1 . ILE   A  1 160 ? -21.536 -4.486  31.191 1.00 25.00  ? 135  ILE   A CG1 1 
ATOM   1021 C  CG2 . ILE   A  1 160 ? -21.148 -3.049  29.169 1.00 22.82  ? 135  ILE   A CG2 1 
ATOM   1022 C  CD1 . ILE   A  1 160 ? -20.870 -5.753  30.701 1.00 25.75  ? 135  ILE   A CD1 1 
ATOM   1023 N  N   . GLY   A  1 161 ? -24.330 -1.849  28.707 1.00 19.31  ? 136  GLY   A N   1 
ATOM   1024 C  CA  . GLY   A  1 161 ? -24.620 -0.938  27.613 1.00 13.20  ? 136  GLY   A CA  1 
ATOM   1025 C  C   . GLY   A  1 161 ? -25.415 0.287   28.014 1.00 17.92  ? 136  GLY   A C   1 
ATOM   1026 O  O   . GLY   A  1 161 ? -25.285 1.344   27.390 1.00 18.49  ? 136  GLY   A O   1 
ATOM   1027 N  N   . LEU   A  1 162 ? -26.244 0.176   29.051 1.00 15.75  ? 137  LEU   A N   1 
ATOM   1028 C  CA  . LEU   A  1 162 ? -27.026 1.305   29.537 1.00 21.42  ? 137  LEU   A CA  1 
ATOM   1029 C  C   . LEU   A  1 162 ? -26.418 1.953   30.773 1.00 19.51  ? 137  LEU   A C   1 
ATOM   1030 O  O   . LEU   A  1 162 ? -27.088 2.756   31.430 1.00 18.79  ? 137  LEU   A O   1 
ATOM   1031 C  CB  . LEU   A  1 162 ? -28.466 0.874   29.827 1.00 20.82  ? 137  LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A  1 162 ? -29.242 0.283   28.647 1.00 25.08  ? 137  LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A  1 162 ? -30.664 -0.072  29.058 1.00 26.41  ? 137  LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A  1 162 ? -29.243 1.241   27.464 1.00 20.06  ? 137  LEU   A CD2 1 
ATOM   1035 N  N   . THR   A  1 163 ? -25.181 1.602   31.119 1.00 20.64  ? 138  THR   A N   1 
ATOM   1036 C  CA  . THR   A  1 163 ? -24.487 2.273   32.216 1.00 21.66  ? 138  THR   A CA  1 
ATOM   1037 C  C   . THR   A  1 163 ? -24.519 3.799   32.130 1.00 22.06  ? 138  THR   A C   1 
ATOM   1038 O  O   . THR   A  1 163 ? -24.666 4.441   33.185 1.00 18.96  ? 138  THR   A O   1 
ATOM   1039 C  CB  . THR   A  1 163 ? -23.041 1.755   32.285 1.00 22.11  ? 138  THR   A CB  1 
ATOM   1040 O  OG1 . THR   A  1 163 ? -23.009 0.525   33.019 1.00 19.62  ? 138  THR   A OG1 1 
ATOM   1041 C  CG2 . THR   A  1 163 ? -22.121 2.765   32.961 1.00 17.79  ? 138  THR   A CG2 1 
ATOM   1042 N  N   . PRO   A  1 164 ? -24.412 4.439   30.955 1.00 17.54  ? 139  PRO   A N   1 
ATOM   1043 C  CA  . PRO   A  1 164 ? -24.584 5.901   30.917 1.00 18.47  ? 139  PRO   A CA  1 
ATOM   1044 C  C   . PRO   A  1 164 ? -25.916 6.376   31.468 1.00 20.22  ? 139  PRO   A C   1 
ATOM   1045 O  O   . PRO   A  1 164 ? -25.997 7.497   31.989 1.00 16.39  ? 139  PRO   A O   1 
ATOM   1046 C  CB  . PRO   A  1 164 ? -24.436 6.219   29.423 1.00 15.28  ? 139  PRO   A CB  1 
ATOM   1047 C  CG  . PRO   A  1 164 ? -23.467 5.189   28.970 1.00 16.81  ? 139  PRO   A CG  1 
ATOM   1048 C  CD  . PRO   A  1 164 ? -23.995 3.944   29.629 1.00 17.41  ? 139  PRO   A CD  1 
ATOM   1049 N  N   A MET   A  1 165 ? -26.966 5.557   31.373 0.58 20.50  ? 140  MET   A N   1 
ATOM   1050 N  N   B MET   A  1 165 ? -26.969 5.561   31.367 0.42 20.60  ? 140  MET   A N   1 
ATOM   1051 C  CA  A MET   A  1 165 ? -28.268 5.950   31.899 0.58 22.05  ? 140  MET   A CA  1 
ATOM   1052 C  CA  B MET   A  1 165 ? -28.265 5.951   31.907 0.42 22.06  ? 140  MET   A CA  1 
ATOM   1053 C  C   A MET   A  1 165 ? -28.296 5.974   33.422 0.58 25.31  ? 140  MET   A C   1 
ATOM   1054 C  C   B MET   A  1 165 ? -28.271 5.989   33.428 0.42 25.26  ? 140  MET   A C   1 
ATOM   1055 O  O   A MET   A  1 165 ? -29.213 6.566   34.001 0.58 21.57  ? 140  MET   A O   1 
ATOM   1056 O  O   B MET   A  1 165 ? -29.162 6.611   34.016 0.42 21.72  ? 140  MET   A O   1 
ATOM   1057 C  CB  A MET   A  1 165 ? -29.354 5.011   31.372 0.58 20.56  ? 140  MET   A CB  1 
ATOM   1058 C  CB  B MET   A  1 165 ? -29.353 5.001   31.405 0.42 20.63  ? 140  MET   A CB  1 
ATOM   1059 C  CG  A MET   A  1 165 ? -29.446 4.965   29.855 0.58 23.99  ? 140  MET   A CG  1 
ATOM   1060 C  CG  B MET   A  1 165 ? -29.311 4.748   29.909 0.42 24.42  ? 140  MET   A CG  1 
ATOM   1061 S  SD  A MET   A  1 165 ? -30.971 4.202   29.268 0.58 22.32  ? 140  MET   A SD  1 
ATOM   1062 S  SD  B MET   A  1 165 ? -30.291 5.945   28.987 0.42 20.76  ? 140  MET   A SD  1 
ATOM   1063 C  CE  A MET   A  1 165 ? -32.143 5.532   29.529 0.58 24.39  ? 140  MET   A CE  1 
ATOM   1064 C  CE  B MET   A  1 165 ? -31.941 5.529   29.547 0.42 24.72  ? 140  MET   A CE  1 
ATOM   1065 N  N   A LEU   A  1 166 ? -27.324 5.345   34.081 0.58 22.69  ? 141  LEU   A N   1 
ATOM   1066 N  N   B LEU   A  1 166 ? -27.305 5.341   34.077 0.42 22.74  ? 141  LEU   A N   1 
ATOM   1067 C  CA  A LEU   A  1 166 ? -27.238 5.387   35.535 0.58 25.68  ? 141  LEU   A CA  1 
ATOM   1068 C  CA  B LEU   A  1 166 ? -27.209 5.371   35.530 0.42 25.63  ? 141  LEU   A CA  1 
ATOM   1069 C  C   A LEU   A  1 166 ? -26.542 6.639   36.051 0.58 24.57  ? 141  LEU   A C   1 
ATOM   1070 C  C   B LEU   A  1 166 ? -26.527 6.630   36.050 0.42 24.54  ? 141  LEU   A C   1 
ATOM   1071 O  O   A LEU   A  1 166 ? -26.418 6.801   37.270 0.58 27.27  ? 141  LEU   A O   1 
ATOM   1072 O  O   B LEU   A  1 166 ? -26.400 6.787   37.269 0.42 27.21  ? 141  LEU   A O   1 
ATOM   1073 C  CB  A LEU   A  1 166 ? -26.520 4.140   36.062 0.58 21.70  ? 141  LEU   A CB  1 
ATOM   1074 C  CB  B LEU   A  1 166 ? -26.466 4.129   36.037 0.42 21.75  ? 141  LEU   A CB  1 
ATOM   1075 C  CG  A LEU   A  1 166 ? -27.092 2.785   35.637 0.58 27.95  ? 141  LEU   A CG  1 
ATOM   1076 C  CG  B LEU   A  1 166 ? -27.232 2.802   36.127 0.42 25.80  ? 141  LEU   A CG  1 
ATOM   1077 C  CD1 A LEU   A  1 166 ? -26.416 1.654   36.399 0.58 19.98  ? 141  LEU   A CD1 1 
ATOM   1078 C  CD1 B LEU   A  1 166 ? -28.702 2.951   35.746 0.42 27.70  ? 141  LEU   A CD1 1 
ATOM   1079 C  CD2 A LEU   A  1 166 ? -28.600 2.745   35.839 0.58 27.52  ? 141  LEU   A CD2 1 
ATOM   1080 C  CD2 B LEU   A  1 166 ? -26.562 1.735   35.273 0.42 27.28  ? 141  LEU   A CD2 1 
ATOM   1081 N  N   . GLY   A  1 167 ? -26.085 7.519   35.164 1.00 20.25  ? 142  GLY   A N   1 
ATOM   1082 C  CA  . GLY   A  1 167 ? -25.531 8.796   35.572 1.00 18.44  ? 142  GLY   A CA  1 
ATOM   1083 C  C   . GLY   A  1 167 ? -24.208 9.163   34.931 1.00 23.13  ? 142  GLY   A C   1 
ATOM   1084 O  O   . GLY   A  1 167 ? -23.756 10.305  35.056 1.00 28.10  ? 142  GLY   A O   1 
ATOM   1085 N  N   . TRP   A  1 168 ? -23.572 8.214   34.242 1.00 25.00  ? 143  TRP   A N   1 
ATOM   1086 C  CA  . TRP   A  1 168 ? -22.309 8.480   33.551 1.00 18.48  ? 143  TRP   A CA  1 
ATOM   1087 C  C   . TRP   A  1 168 ? -22.642 9.022   32.163 1.00 14.35  ? 143  TRP   A C   1 
ATOM   1088 O  O   . TRP   A  1 168 ? -22.545 8.331   31.146 1.00 20.79  ? 143  TRP   A O   1 
ATOM   1089 C  CB  . TRP   A  1 168 ? -21.448 7.224   33.488 1.00 17.29  ? 143  TRP   A CB  1 
ATOM   1090 C  CG  . TRP   A  1 168 ? -20.016 7.491   33.110 1.00 23.12  ? 143  TRP   A CG  1 
ATOM   1091 C  CD1 . TRP   A  1 168 ? -19.471 8.691   32.749 1.00 20.58  ? 143  TRP   A CD1 1 
ATOM   1092 C  CD2 . TRP   A  1 168 ? -18.948 6.536   33.064 1.00 19.30  ? 143  TRP   A CD2 1 
ATOM   1093 N  NE1 . TRP   A  1 168 ? -18.132 8.540   32.480 1.00 18.39  ? 143  TRP   A NE1 1 
ATOM   1094 C  CE2 . TRP   A  1 168 ? -17.787 7.227   32.665 1.00 19.92  ? 143  TRP   A CE2 1 
ATOM   1095 C  CE3 . TRP   A  1 168 ? -18.862 5.163   33.318 1.00 16.70  ? 143  TRP   A CE3 1 
ATOM   1096 C  CZ2 . TRP   A  1 168 ? -16.555 6.594   32.515 1.00 17.20  ? 143  TRP   A CZ2 1 
ATOM   1097 C  CZ3 . TRP   A  1 168 ? -17.638 4.536   33.169 1.00 19.35  ? 143  TRP   A CZ3 1 
ATOM   1098 C  CH2 . TRP   A  1 168 ? -16.501 5.251   32.771 1.00 16.10  ? 143  TRP   A CH2 1 
ATOM   1099 N  N   . ASN   A  1 169 ? -23.027 10.294  32.124 1.00 17.92  ? 144  ASN   A N   1 
ATOM   1100 C  CA  . ASN   A  1 169 ? -23.514 10.904  30.896 1.00 23.35  ? 144  ASN   A CA  1 
ATOM   1101 C  C   . ASN   A  1 169 ? -23.255 12.403  30.938 1.00 24.31  ? 144  ASN   A C   1 
ATOM   1102 O  O   . ASN   A  1 169 ? -22.861 12.958  31.966 1.00 27.04  ? 144  ASN   A O   1 
ATOM   1103 C  CB  . ASN   A  1 169 ? -24.996 10.580  30.678 1.00 19.47  ? 144  ASN   A CB  1 
ATOM   1104 C  CG  . ASN   A  1 169 ? -25.896 11.163  31.757 1.00 22.95  ? 144  ASN   A CG  1 
ATOM   1105 O  OD1 . ASN   A  1 169 ? -25.933 12.373  31.975 1.00 26.60  ? 144  ASN   A OD1 1 
ATOM   1106 N  ND2 . ASN   A  1 169 ? -26.628 10.292  32.442 1.00 14.45  ? 144  ASN   A ND2 1 
ATOM   1107 N  N   . ASN   A  1 170 ? -23.484 13.058  29.798 1.00 20.50  ? 145  ASN   A N   1 
ATOM   1108 C  CA  . ASN   A  1 170 ? -23.299 14.498  29.688 1.00 22.25  ? 145  ASN   A CA  1 
ATOM   1109 C  C   . ASN   A  1 170 ? -24.611 15.271  29.757 1.00 22.29  ? 145  ASN   A C   1 
ATOM   1110 O  O   . ASN   A  1 170 ? -24.666 16.418  29.302 1.00 25.95  ? 145  ASN   A O   1 
ATOM   1111 C  CB  . ASN   A  1 170 ? -22.576 14.838  28.385 1.00 19.87  ? 145  ASN   A CB  1 
ATOM   1112 C  CG  . ASN   A  1 170 ? -21.190 14.238  28.311 1.00 32.95  ? 145  ASN   A CG  1 
ATOM   1113 O  OD1 . ASN   A  1 170 ? -20.508 14.094  29.325 1.00 35.87  ? 145  ASN   A OD1 1 
ATOM   1114 N  ND2 . ASN   A  1 170 ? -20.762 13.887  27.103 1.00 35.32  ? 145  ASN   A ND2 1 
ATOM   1115 N  N   . CYS   A  1 171 ? -25.664 14.678  30.324 1.00 19.90  ? 146  CYS   A N   1 
ATOM   1116 C  CA  . CYS   A  1 171 ? -26.944 15.376  30.373 1.00 33.31  ? 146  CYS   A CA  1 
ATOM   1117 C  C   . CYS   A  1 171 ? -26.894 16.540  31.351 1.00 37.29  ? 146  CYS   A C   1 
ATOM   1118 O  O   . CYS   A  1 171 ? -27.651 17.507  31.209 1.00 37.66  ? 146  CYS   A O   1 
ATOM   1119 C  CB  . CYS   A  1 171 ? -28.070 14.410  30.741 1.00 27.96  ? 146  CYS   A CB  1 
ATOM   1120 S  SG  . CYS   A  1 171 ? -28.442 13.210  29.446 1.00 37.23  ? 146  CYS   A SG  1 
ATOM   1121 N  N   . GLY   A  1 172 ? -26.003 16.463  32.341 1.00 33.42  ? 147  GLY   A N   1 
ATOM   1122 C  CA  . GLY   A  1 172 ? -25.795 17.554  33.273 1.00 31.69  ? 147  GLY   A CA  1 
ATOM   1123 C  C   . GLY   A  1 172 ? -25.158 18.781  32.656 1.00 36.00  ? 147  GLY   A C   1 
ATOM   1124 O  O   . GLY   A  1 172 ? -25.257 19.869  33.233 1.00 43.87  ? 147  GLY   A O   1 
ATOM   1125 N  N   . GLN   A  1 173 ? -24.503 18.634  31.502 1.00 39.95  ? 148  GLN   A N   1 
ATOM   1126 C  CA  . GLN   A  1 173 ? -23.806 19.740  30.841 1.00 30.78  ? 148  GLN   A CA  1 
ATOM   1127 C  C   . GLN   A  1 173 ? -24.286 19.889  29.401 1.00 33.17  ? 148  GLN   A C   1 
ATOM   1128 O  O   . GLN   A  1 173 ? -23.513 19.704  28.456 1.00 27.58  ? 148  GLN   A O   1 
ATOM   1129 C  CB  . GLN   A  1 173 ? -22.299 19.496  30.859 1.00 44.67  ? 148  GLN   A CB  1 
ATOM   1130 C  CG  . GLN   A  1 173 ? -21.755 18.923  32.147 1.00 74.49  ? 148  GLN   A CG  1 
ATOM   1131 C  CD  . GLN   A  1 173 ? -20.479 18.128  31.924 1.00 98.69  ? 148  GLN   A CD  1 
ATOM   1132 O  OE1 . GLN   A  1 173 ? -19.601 18.535  31.160 1.00 106.83 ? 148  GLN   A OE1 1 
ATOM   1133 N  NE2 . GLN   A  1 173 ? -20.395 16.963  32.555 1.00 97.54  ? 148  GLN   A NE2 1 
ATOM   1134 N  N   . PRO   A  1 174 ? -25.561 20.222  29.192 1.00 36.93  ? 149  PRO   A N   1 
ATOM   1135 C  CA  . PRO   A  1 174 ? -26.075 20.304  27.820 1.00 25.36  ? 149  PRO   A CA  1 
ATOM   1136 C  C   . PRO   A  1 174 ? -25.393 21.410  27.026 1.00 35.71  ? 149  PRO   A C   1 
ATOM   1137 O  O   . PRO   A  1 174 ? -24.980 22.434  27.574 1.00 34.54  ? 149  PRO   A O   1 
ATOM   1138 C  CB  . PRO   A  1 174 ? -27.565 20.602  28.022 1.00 41.29  ? 149  PRO   A CB  1 
ATOM   1139 C  CG  . PRO   A  1 174 ? -27.611 21.317  29.333 1.00 32.75  ? 149  PRO   A CG  1 
ATOM   1140 C  CD  . PRO   A  1 174 ? -26.575 20.631  30.179 1.00 29.51  ? 149  PRO   A CD  1 
ATOM   1141 N  N   . LYS   A  1 175 ? -25.279 21.194  25.715 1.00 35.95  ? 150  LYS   A N   1 
ATOM   1142 C  CA  . LYS   A  1 175 ? -24.849 22.245  24.792 1.00 41.70  ? 150  LYS   A CA  1 
ATOM   1143 C  C   . LYS   A  1 175 ? -26.039 23.162  24.539 1.00 38.00  ? 150  LYS   A C   1 
ATOM   1144 O  O   . LYS   A  1 175 ? -26.847 22.934  23.637 1.00 34.39  ? 150  LYS   A O   1 
ATOM   1145 C  CB  . LYS   A  1 175 ? -24.310 21.644  23.501 1.00 41.95  ? 150  LYS   A CB  1 
ATOM   1146 C  CG  . LYS   A  1 175 ? -23.055 20.810  23.692 1.00 43.38  ? 150  LYS   A CG  1 
ATOM   1147 C  CD  . LYS   A  1 175 ? -22.274 20.676  22.397 1.00 45.04  ? 150  LYS   A CD  1 
ATOM   1148 C  CE  . LYS   A  1 175 ? -21.161 19.650  22.531 1.00 59.22  ? 150  LYS   A CE  1 
ATOM   1149 N  NZ  . LYS   A  1 175 ? -20.246 19.972  23.659 1.00 53.79  ? 150  LYS   A NZ  1 
ATOM   1150 N  N   . GLU   A  1 176 ? -26.151 24.218  25.346 1.00 47.61  ? 151  GLU   A N   1 
ATOM   1151 C  CA  . GLU   A  1 176 ? -27.324 25.082  25.261 1.00 56.47  ? 151  GLU   A CA  1 
ATOM   1152 C  C   . GLU   A  1 176 ? -27.353 25.894  23.971 1.00 47.18  ? 151  GLU   A C   1 
ATOM   1153 O  O   . GLU   A  1 176 ? -28.435 26.150  23.431 1.00 44.90  ? 151  GLU   A O   1 
ATOM   1154 C  CB  . GLU   A  1 176 ? -27.409 25.994  26.485 1.00 50.08  ? 151  GLU   A CB  1 
ATOM   1155 C  CG  . GLU   A  1 176 ? -28.043 25.332  27.724 1.00 46.68  ? 151  GLU   A CG  1 
ATOM   1156 C  CD  . GLU   A  1 176 ? -29.439 24.731  27.499 1.00 62.69  ? 151  GLU   A CD  1 
ATOM   1157 O  OE1 . GLU   A  1 176 ? -29.996 24.805  26.381 1.00 64.67  ? 151  GLU   A OE1 1 
ATOM   1158 O  OE2 . GLU   A  1 176 ? -29.984 24.157  28.465 1.00 74.79  ? 151  GLU   A OE2 1 
ATOM   1159 N  N   . GLY   A  1 177 ? -26.191 26.299  23.457 1.00 41.54  ? 152  GLY   A N   1 
ATOM   1160 C  CA  . GLY   A  1 177 ? -26.180 27.071  22.225 1.00 50.77  ? 152  GLY   A CA  1 
ATOM   1161 C  C   . GLY   A  1 177 ? -26.667 26.265  21.039 1.00 50.17  ? 152  GLY   A C   1 
ATOM   1162 O  O   . GLY   A  1 177 ? -27.373 26.785  20.170 1.00 51.18  ? 152  GLY   A O   1 
ATOM   1163 N  N   . LYS   A  1 178 ? -26.299 24.984  20.983 1.00 45.58  ? 153  LYS   A N   1 
ATOM   1164 C  CA  . LYS   A  1 178 ? -26.800 24.126  19.916 1.00 42.29  ? 153  LYS   A CA  1 
ATOM   1165 C  C   . LYS   A  1 178 ? -28.293 23.874  20.082 1.00 38.96  ? 153  LYS   A C   1 
ATOM   1166 O  O   . LYS   A  1 178 ? -29.040 23.856  19.097 1.00 33.85  ? 153  LYS   A O   1 
ATOM   1167 C  CB  . LYS   A  1 178 ? -26.030 22.805  19.896 1.00 40.16  ? 153  LYS   A CB  1 
ATOM   1168 C  CG  . LYS   A  1 178 ? -26.260 21.973  18.646 1.00 41.36  ? 153  LYS   A CG  1 
ATOM   1169 C  CD  . LYS   A  1 178 ? -24.951 21.431  18.098 1.00 63.03  ? 153  LYS   A CD  1 
ATOM   1170 C  CE  . LYS   A  1 178 ? -24.264 20.535  19.114 1.00 45.12  ? 153  LYS   A CE  1 
ATOM   1171 N  NZ  . LYS   A  1 178 ? -22.833 20.298  18.779 1.00 53.42  ? 153  LYS   A NZ  1 
ATOM   1172 N  N   . ALA   A  1 179 ? -28.741 23.666  21.323 1.00 30.84  ? 154  ALA   A N   1 
ATOM   1173 C  CA  . ALA   A  1 179 ? -30.165 23.477  21.579 1.00 40.74  ? 154  ALA   A CA  1 
ATOM   1174 C  C   . ALA   A  1 179 ? -30.977 24.713  21.208 1.00 46.86  ? 154  ALA   A C   1 
ATOM   1175 O  O   . ALA   A  1 179 ? -32.042 24.597  20.589 1.00 40.17  ? 154  ALA   A O   1 
ATOM   1176 C  CB  . ALA   A  1 179 ? -30.387 23.111  23.048 1.00 29.74  ? 154  ALA   A CB  1 
ATOM   1177 N  N   . HIS   A  1 180 ? -30.502 25.906  21.584 1.00 41.12  ? 155  HIS   A N   1 
ATOM   1178 C  CA  . HIS   A  1 180 ? -31.248 27.118  21.254 1.00 45.61  ? 155  HIS   A CA  1 
ATOM   1179 C  C   . HIS   A  1 180 ? -31.270 27.369  19.751 1.00 47.71  ? 155  HIS   A C   1 
ATOM   1180 O  O   . HIS   A  1 180 ? -32.279 27.833  19.210 1.00 52.47  ? 155  HIS   A O   1 
ATOM   1181 C  CB  . HIS   A  1 180 ? -30.658 28.323  21.985 1.00 46.81  ? 155  HIS   A CB  1 
ATOM   1182 C  CG  . HIS   A  1 180 ? -30.979 28.361  23.447 1.00 55.32  ? 155  HIS   A CG  1 
ATOM   1183 N  ND1 . HIS   A  1 180 ? -32.265 28.504  23.922 1.00 63.54  ? 155  HIS   A ND1 1 
ATOM   1184 C  CD2 . HIS   A  1 180 ? -30.182 28.294  24.540 1.00 56.91  ? 155  HIS   A CD2 1 
ATOM   1185 C  CE1 . HIS   A  1 180 ? -32.247 28.511  25.243 1.00 66.81  ? 155  HIS   A CE1 1 
ATOM   1186 N  NE2 . HIS   A  1 180 ? -30.995 28.386  25.643 1.00 54.38  ? 155  HIS   A NE2 1 
ATOM   1187 N  N   . SER   A  1 181 ? -30.172 27.060  19.057 1.00 36.51  ? 156  SER   A N   1 
ATOM   1188 C  CA  . SER   A  1 181 ? -30.117 27.318  17.622 1.00 44.88  ? 156  SER   A CA  1 
ATOM   1189 C  C   . SER   A  1 181 ? -31.093 26.422  16.871 1.00 47.15  ? 156  SER   A C   1 
ATOM   1190 O  O   . SER   A  1 181 ? -31.609 26.808  15.814 1.00 49.79  ? 156  SER   A O   1 
ATOM   1191 C  CB  . SER   A  1 181 ? -28.697 27.126  17.093 1.00 44.26  ? 156  SER   A CB  1 
ATOM   1192 O  OG  . SER   A  1 181 ? -28.254 25.794  17.284 1.00 56.58  ? 156  SER   A OG  1 
ATOM   1193 N  N   A GLN   A  1 182 ? -31.356 25.229  17.393 0.65 40.65  ? 157  GLN   A N   1 
ATOM   1194 N  N   B GLN   A  1 182 ? -31.351 25.228  17.398 0.35 40.69  ? 157  GLN   A N   1 
ATOM   1195 C  CA  A GLN   A  1 182 ? -32.283 24.293  16.774 0.65 38.61  ? 157  GLN   A CA  1 
ATOM   1196 C  CA  B GLN   A  1 182 ? -32.271 24.269  16.803 0.35 38.74  ? 157  GLN   A CA  1 
ATOM   1197 C  C   A GLN   A  1 182 ? -33.707 24.444  17.289 0.65 41.79  ? 157  GLN   A C   1 
ATOM   1198 C  C   B GLN   A  1 182 ? -33.702 24.435  17.301 0.35 41.77  ? 157  GLN   A C   1 
ATOM   1199 O  O   A GLN   A  1 182 ? -34.577 23.658  16.900 0.65 42.55  ? 157  GLN   A O   1 
ATOM   1200 O  O   B GLN   A  1 182 ? -34.574 23.654  16.906 0.35 42.53  ? 157  GLN   A O   1 
ATOM   1201 C  CB  A GLN   A  1 182 ? -31.802 22.858  17.000 0.65 37.60  ? 157  GLN   A CB  1 
ATOM   1202 C  CB  B GLN   A  1 182 ? -31.785 22.843  17.085 0.35 37.69  ? 157  GLN   A CB  1 
ATOM   1203 C  CG  A GLN   A  1 182 ? -30.455 22.554  16.369 0.65 39.81  ? 157  GLN   A CG  1 
ATOM   1204 C  CG  B GLN   A  1 182 ? -32.129 21.827  16.009 0.35 42.03  ? 157  GLN   A CG  1 
ATOM   1205 C  CD  A GLN   A  1 182 ? -30.103 21.089  16.465 0.65 44.65  ? 157  GLN   A CD  1 
ATOM   1206 C  CD  B GLN   A  1 182 ? -32.499 20.479  16.593 0.35 42.17  ? 157  GLN   A CD  1 
ATOM   1207 O  OE1 A GLN   A  1 182 ? -30.941 20.267  16.829 0.65 54.93  ? 157  GLN   A OE1 1 
ATOM   1208 O  OE1 B GLN   A  1 182 ? -31.974 20.077  17.630 0.35 43.77  ? 157  GLN   A OE1 1 
ATOM   1209 N  NE2 A GLN   A  1 182 ? -28.860 20.751  16.141 0.65 51.63  ? 157  GLN   A NE2 1 
ATOM   1210 N  NE2 B GLN   A  1 182 ? -33.409 19.774  15.931 0.35 41.25  ? 157  GLN   A NE2 1 
ATOM   1211 N  N   . GLY   A  1 183 ? -33.965 25.425  18.152 1.00 41.56  ? 158  GLY   A N   1 
ATOM   1212 C  CA  . GLY   A  1 183 ? -35.306 25.632  18.661 1.00 34.01  ? 158  GLY   A CA  1 
ATOM   1213 C  C   . GLY   A  1 183 ? -35.777 24.602  19.660 1.00 46.10  ? 158  GLY   A C   1 
ATOM   1214 O  O   . GLY   A  1 183 ? -36.986 24.431  19.834 1.00 57.57  ? 158  GLY   A O   1 
ATOM   1215 N  N   . CYS   A  1 184 ? -34.856 23.908  20.322 1.00 38.46  ? 159  CYS   A N   1 
ATOM   1216 C  CA  . CYS   A  1 184 ? -35.228 22.881  21.284 1.00 39.60  ? 159  CYS   A CA  1 
ATOM   1217 C  C   . CYS   A  1 184 ? -35.935 23.487  22.492 1.00 38.93  ? 159  CYS   A C   1 
ATOM   1218 O  O   . CYS   A  1 184 ? -35.714 24.644  22.861 1.00 49.50  ? 159  CYS   A O   1 
ATOM   1219 C  CB  . CYS   A  1 184 ? -33.997 22.098  21.739 1.00 37.12  ? 159  CYS   A CB  1 
ATOM   1220 S  SG  . CYS   A  1 184 ? -33.210 21.112  20.444 1.00 42.18  ? 159  CYS   A SG  1 
ATOM   1221 N  N   . GLY   A  1 185 ? -36.796 22.679  23.108 1.00 37.78  ? 160  GLY   A N   1 
ATOM   1222 C  CA  . GLY   A  1 185 ? -37.552 23.083  24.272 1.00 39.94  ? 160  GLY   A CA  1 
ATOM   1223 C  C   . GLY   A  1 185 ? -36.744 22.972  25.551 1.00 51.64  ? 160  GLY   A C   1 
ATOM   1224 O  O   . GLY   A  1 185 ? -35.573 22.594  25.559 1.00 53.28  ? 160  GLY   A O   1 
ATOM   1225 N  N   . GLU   A  1 186 ? -37.394 23.319  26.659 1.00 59.05  ? 161  GLU   A N   1 
ATOM   1226 C  CA  . GLU   A  1 186 ? -36.722 23.275  27.949 1.00 46.99  ? 161  GLU   A CA  1 
ATOM   1227 C  C   . GLU   A  1 186 ? -36.474 21.833  28.369 1.00 55.93  ? 161  GLU   A C   1 
ATOM   1228 O  O   . GLU   A  1 186 ? -37.344 20.969  28.228 1.00 57.48  ? 161  GLU   A O   1 
ATOM   1229 C  CB  . GLU   A  1 186 ? -37.580 23.964  29.010 1.00 67.43  ? 161  GLU   A CB  1 
ATOM   1230 C  CG  . GLU   A  1 186 ? -37.346 23.434  30.423 1.00 82.95  ? 161  GLU   A CG  1 
ATOM   1231 C  CD  . GLU   A  1 186 ? -38.355 23.950  31.429 1.00 112.30 ? 161  GLU   A CD  1 
ATOM   1232 O  OE1 . GLU   A  1 186 ? -38.591 23.255  32.441 1.00 111.09 ? 161  GLU   A OE1 1 
ATOM   1233 O  OE2 . GLU   A  1 186 ? -38.927 25.036  31.201 1.00 113.75 ? 161  GLU   A OE2 1 
ATOM   1234 N  N   . GLY   A  1 187 ? -35.274 21.573  28.885 1.00 53.26  ? 162  GLY   A N   1 
ATOM   1235 C  CA  . GLY   A  1 187 ? -34.893 20.218  29.210 1.00 49.46  ? 162  GLY   A CA  1 
ATOM   1236 C  C   . GLY   A  1 187 ? -34.514 19.360  28.026 1.00 50.41  ? 162  GLY   A C   1 
ATOM   1237 O  O   . GLY   A  1 187 ? -34.253 18.164  28.210 1.00 52.81  ? 162  GLY   A O   1 
ATOM   1238 N  N   . GLN   A  1 188 ? -34.469 19.922  26.821 1.00 41.64  ? 163  GLN   A N   1 
ATOM   1239 C  CA  . GLN   A  1 188 ? -34.113 19.174  25.628 1.00 47.75  ? 163  GLN   A CA  1 
ATOM   1240 C  C   . GLN   A  1 188 ? -32.735 19.563  25.111 1.00 43.08  ? 163  GLN   A C   1 
ATOM   1241 O  O   . GLN   A  1 188 ? -32.254 20.678  25.333 1.00 42.05  ? 163  GLN   A O   1 
ATOM   1242 C  CB  . GLN   A  1 188 ? -35.148 19.406  24.524 1.00 39.95  ? 163  GLN   A CB  1 
ATOM   1243 C  CG  . GLN   A  1 188 ? -36.529 18.877  24.850 1.00 34.60  ? 163  GLN   A CG  1 
ATOM   1244 C  CD  . GLN   A  1 188 ? -37.464 18.936  23.662 1.00 43.59  ? 163  GLN   A CD  1 
ATOM   1245 O  OE1 . GLN   A  1 188 ? -37.386 19.852  22.842 1.00 37.12  ? 163  GLN   A OE1 1 
ATOM   1246 N  NE2 . GLN   A  1 188 ? -38.355 17.958  23.560 1.00 44.48  ? 163  GLN   A NE2 1 
ATOM   1247 N  N   . VAL   A  1 189 ? -32.110 18.616  24.414 1.00 32.04  ? 164  VAL   A N   1 
ATOM   1248 C  CA  . VAL   A  1 189 ? -30.837 18.816  23.740 1.00 33.68  ? 164  VAL   A CA  1 
ATOM   1249 C  C   . VAL   A  1 189 ? -30.988 18.388  22.288 1.00 35.58  ? 164  VAL   A C   1 
ATOM   1250 O  O   . VAL   A  1 189 ? -31.899 17.641  21.926 1.00 21.91  ? 164  VAL   A O   1 
ATOM   1251 C  CB  . VAL   A  1 189 ? -29.690 18.029  24.409 1.00 39.37  ? 164  VAL   A CB  1 
ATOM   1252 C  CG1 . VAL   A  1 189 ? -29.495 18.489  25.840 1.00 31.85  ? 164  VAL   A CG1 1 
ATOM   1253 C  CG2 . VAL   A  1 189 ? -29.975 16.536  24.357 1.00 24.80  ? 164  VAL   A CG2 1 
ATOM   1254 N  N   . ALA   A  1 190 ? -30.080 18.879  21.452 1.00 24.39  ? 165  ALA   A N   1 
ATOM   1255 C  CA  . ALA   A  1 190 ? -29.893 18.282  20.137 1.00 30.74  ? 165  ALA   A CA  1 
ATOM   1256 C  C   . ALA   A  1 190 ? -29.337 16.877  20.335 1.00 27.92  ? 165  ALA   A C   1 
ATOM   1257 O  O   . ALA   A  1 190 ? -28.263 16.707  20.921 1.00 30.98  ? 165  ALA   A O   1 
ATOM   1258 C  CB  . ALA   A  1 190 ? -28.951 19.132  19.289 1.00 25.29  ? 165  ALA   A CB  1 
ATOM   1259 N  N   . CYS   A  1 191 ? -30.061 15.869  19.853 1.00 24.42  ? 166  CYS   A N   1 
ATOM   1260 C  CA  . CYS   A  1 191 ? -29.724 14.479  20.158 1.00 28.57  ? 166  CYS   A CA  1 
ATOM   1261 C  C   . CYS   A  1 191 ? -28.604 14.022  19.235 1.00 28.03  ? 166  CYS   A C   1 
ATOM   1262 O  O   . CYS   A  1 191 ? -28.838 13.633  18.088 1.00 31.56  ? 166  CYS   A O   1 
ATOM   1263 C  CB  . CYS   A  1 191 ? -30.944 13.578  20.026 1.00 24.06  ? 166  CYS   A CB  1 
ATOM   1264 S  SG  . CYS   A  1 191 ? -30.594 11.875  20.494 1.00 39.16  ? 166  CYS   A SG  1 
ATOM   1265 N  N   . LEU   A  1 192 ? -27.379 14.071  19.750 1.00 29.33  ? 167  LEU   A N   1 
ATOM   1266 C  CA  . LEU   A  1 192 ? -26.176 13.668  19.038 1.00 24.72  ? 167  LEU   A CA  1 
ATOM   1267 C  C   . LEU   A  1 192 ? -25.360 12.749  19.934 1.00 24.86  ? 167  LEU   A C   1 
ATOM   1268 O  O   . LEU   A  1 192 ? -25.210 13.025  21.129 1.00 21.86  ? 167  LEU   A O   1 
ATOM   1269 C  CB  . LEU   A  1 192 ? -25.349 14.890  18.625 1.00 25.90  ? 167  LEU   A CB  1 
ATOM   1270 C  CG  . LEU   A  1 192 ? -26.009 15.809  17.595 1.00 31.41  ? 167  LEU   A CG  1 
ATOM   1271 C  CD1 . LEU   A  1 192 ? -25.241 17.113  17.464 1.00 31.40  ? 167  LEU   A CD1 1 
ATOM   1272 C  CD2 . LEU   A  1 192 ? -26.119 15.108  16.250 1.00 32.78  ? 167  LEU   A CD2 1 
ATOM   1273 N  N   . PHE   A  1 193 ? -24.870 11.641  19.362 1.00 23.80  ? 168  PHE   A N   1 
ATOM   1274 C  CA  . PHE   A  1 193 ? -24.203 10.606  20.151 1.00 20.75  ? 168  PHE   A CA  1 
ATOM   1275 C  C   . PHE   A  1 193 ? -23.115 11.203  21.037 1.00 21.50  ? 168  PHE   A C   1 
ATOM   1276 O  O   . PHE   A  1 193 ? -23.100 10.982  22.253 1.00 21.71  ? 168  PHE   A O   1 
ATOM   1277 C  CB  . PHE   A  1 193 ? -23.616 9.537   19.225 1.00 19.63  ? 168  PHE   A CB  1 
ATOM   1278 C  CG  . PHE   A  1 193 ? -23.070 8.335   19.952 1.00 22.50  ? 168  PHE   A CG  1 
ATOM   1279 C  CD1 . PHE   A  1 193 ? -21.775 8.337   20.452 1.00 23.63  ? 168  PHE   A CD1 1 
ATOM   1280 C  CD2 . PHE   A  1 193 ? -23.850 7.206   20.135 1.00 15.48  ? 168  PHE   A CD2 1 
ATOM   1281 C  CE1 . PHE   A  1 193 ? -21.271 7.238   21.123 1.00 15.46  ? 168  PHE   A CE1 1 
ATOM   1282 C  CE2 . PHE   A  1 193 ? -23.351 6.102   20.803 1.00 21.68  ? 168  PHE   A CE2 1 
ATOM   1283 C  CZ  . PHE   A  1 193 ? -22.060 6.119   21.298 1.00 19.55  ? 168  PHE   A CZ  1 
ATOM   1284 N  N   . GLU   A  1 194 ? -22.187 11.956  20.442 1.00 15.52  ? 169  GLU   A N   1 
ATOM   1285 C  CA  . GLU   A  1 194 ? -21.040 12.437  21.199 1.00 28.59  ? 169  GLU   A CA  1 
ATOM   1286 C  C   . GLU   A  1 194 ? -21.389 13.605  22.113 1.00 28.68  ? 169  GLU   A C   1 
ATOM   1287 O  O   . GLU   A  1 194 ? -20.550 13.999  22.930 1.00 27.14  ? 169  GLU   A O   1 
ATOM   1288 C  CB  . GLU   A  1 194 ? -19.901 12.854  20.262 1.00 20.36  ? 169  GLU   A CB  1 
ATOM   1289 C  CG  . GLU   A  1 194 ? -19.295 11.720  19.457 1.00 30.30  ? 169  GLU   A CG  1 
ATOM   1290 C  CD  . GLU   A  1 194 ? -18.040 12.145  18.717 1.00 36.46  ? 169  GLU   A CD  1 
ATOM   1291 O  OE1 . GLU   A  1 194 ? -17.563 13.276  18.946 1.00 37.89  ? 169  GLU   A OE1 1 
ATOM   1292 O  OE2 . GLU   A  1 194 ? -17.523 11.343  17.911 1.00 27.19  ? 169  GLU   A OE2 1 
ATOM   1293 N  N   . ASP   A  1 195 ? -22.591 14.171  21.998 1.00 17.43  ? 170  ASP   A N   1 
ATOM   1294 C  CA  . ASP   A  1 195 ? -23.008 15.196  22.949 1.00 23.90  ? 170  ASP   A CA  1 
ATOM   1295 C  C   . ASP   A  1 195 ? -23.542 14.608  24.247 1.00 22.57  ? 170  ASP   A C   1 
ATOM   1296 O  O   . ASP   A  1 195 ? -23.466 15.270  25.286 1.00 22.75  ? 170  ASP   A O   1 
ATOM   1297 C  CB  . ASP   A  1 195 ? -24.063 16.118  22.333 1.00 27.80  ? 170  ASP   A CB  1 
ATOM   1298 C  CG  . ASP   A  1 195 ? -23.501 17.016  21.254 1.00 45.79  ? 170  ASP   A CG  1 
ATOM   1299 O  OD1 . ASP   A  1 195 ? -22.269 16.994  21.037 1.00 40.37  ? 170  ASP   A OD1 1 
ATOM   1300 O  OD2 . ASP   A  1 195 ? -24.306 17.712  20.597 1.00 35.39  ? 170  ASP   A OD2 1 
ATOM   1301 N  N   . VAL   A  1 196 ? -24.075 13.388  24.224 1.00 15.86  ? 171  VAL   A N   1 
ATOM   1302 C  CA  . VAL   A  1 196 ? -24.689 12.810  25.408 1.00 17.35  ? 171  VAL   A CA  1 
ATOM   1303 C  C   . VAL   A  1 196 ? -23.880 11.662  26.008 1.00 18.55  ? 171  VAL   A C   1 
ATOM   1304 O  O   . VAL   A  1 196 ? -23.922 11.468  27.230 1.00 20.51  ? 171  VAL   A O   1 
ATOM   1305 C  CB  . VAL   A  1 196 ? -26.134 12.358  25.108 1.00 25.01  ? 171  VAL   A CB  1 
ATOM   1306 C  CG1 . VAL   A  1 196 ? -26.964 13.539  24.629 1.00 27.54  ? 171  VAL   A CG1 1 
ATOM   1307 C  CG2 . VAL   A  1 196 ? -26.143 11.244  24.075 1.00 18.67  ? 171  VAL   A CG2 1 
ATOM   1308 N  N   . VAL   A  1 197 ? -23.152 10.893  25.205 1.00 21.00  ? 172  VAL   A N   1 
ATOM   1309 C  CA  . VAL   A  1 197 ? -22.383 9.756   25.693 1.00 17.19  ? 172  VAL   A CA  1 
ATOM   1310 C  C   . VAL   A  1 197 ? -20.957 10.227  25.984 1.00 22.59  ? 172  VAL   A C   1 
ATOM   1311 O  O   . VAL   A  1 197 ? -20.302 10.756  25.072 1.00 21.17  ? 172  VAL   A O   1 
ATOM   1312 C  CB  . VAL   A  1 197 ? -22.381 8.597   24.691 1.00 26.12  ? 172  VAL   A CB  1 
ATOM   1313 C  CG1 . VAL   A  1 197 ? -21.696 7.378   25.294 1.00 19.13  ? 172  VAL   A CG1 1 
ATOM   1314 C  CG2 . VAL   A  1 197 ? -23.801 8.258   24.271 1.00 20.15  ? 172  VAL   A CG2 1 
ATOM   1315 N  N   . PRO   A  1 198 ? -20.459 10.071  27.207 1.00 21.93  ? 173  PRO   A N   1 
ATOM   1316 C  CA  . PRO   A  1 198 ? -19.108 10.551  27.517 1.00 25.69  ? 173  PRO   A CA  1 
ATOM   1317 C  C   . PRO   A  1 198 ? -18.061 9.743   26.768 1.00 21.10  ? 173  PRO   A C   1 
ATOM   1318 O  O   . PRO   A  1 198 ? -18.185 8.525   26.611 1.00 17.41  ? 173  PRO   A O   1 
ATOM   1319 C  CB  . PRO   A  1 198 ? -18.992 10.347  29.033 1.00 17.78  ? 173  PRO   A CB  1 
ATOM   1320 C  CG  . PRO   A  1 198 ? -20.394 10.221  29.514 1.00 24.24  ? 173  PRO   A CG  1 
ATOM   1321 C  CD  . PRO   A  1 198 ? -21.138 9.547   28.402 1.00 22.96  ? 173  PRO   A CD  1 
ATOM   1322 N  N   . MET   A  1 199 ? -17.019 10.434  26.307 1.00 18.44  ? 174  MET   A N   1 
ATOM   1323 C  CA  . MET   A  1 199 ? -15.978 9.751   25.548 1.00 18.18  ? 174  MET   A CA  1 
ATOM   1324 C  C   . MET   A  1 199 ? -15.109 8.872   26.441 1.00 17.02  ? 174  MET   A C   1 
ATOM   1325 O  O   . MET   A  1 199 ? -14.560 7.871   25.968 1.00 21.52  ? 174  MET   A O   1 
ATOM   1326 C  CB  . MET   A  1 199 ? -15.120 10.768  24.794 1.00 19.86  ? 174  MET   A CB  1 
ATOM   1327 C  CG  . MET   A  1 199 ? -14.343 10.171  23.630 1.00 30.28  ? 174  MET   A CG  1 
ATOM   1328 S  SD  . MET   A  1 199 ? -15.385 9.318   22.428 1.00 37.05  ? 174  MET   A SD  1 
ATOM   1329 C  CE  . MET   A  1 199 ? -15.889 10.688  21.390 1.00 33.66  ? 174  MET   A CE  1 
ATOM   1330 N  N   . ASN   A  1 200 ? -14.970 9.218   27.726 1.00 14.59  ? 175  ASN   A N   1 
ATOM   1331 C  CA  . ASN   A  1 200 ? -14.196 8.368   28.628 1.00 21.66  ? 175  ASN   A CA  1 
ATOM   1332 C  C   . ASN   A  1 200 ? -14.921 7.054   28.891 1.00 16.48  ? 175  ASN   A C   1 
ATOM   1333 O  O   . ASN   A  1 200 ? -14.280 6.006   29.039 1.00 17.34  ? 175  ASN   A O   1 
ATOM   1334 C  CB  . ASN   A  1 200 ? -13.868 9.092   29.938 1.00 14.86  ? 175  ASN   A CB  1 
ATOM   1335 C  CG  . ASN   A  1 200 ? -15.073 9.743   30.577 1.00 25.83  ? 175  ASN   A CG  1 
ATOM   1336 O  OD1 . ASN   A  1 200 ? -16.218 9.386   30.299 1.00 28.67  ? 175  ASN   A OD1 1 
ATOM   1337 N  ND2 . ASN   A  1 200 ? -14.816 10.694  31.464 1.00 21.23  ? 175  ASN   A ND2 1 
ATOM   1338 N  N   . TYR   A  1 201 ? -16.255 7.089   28.961 1.00 18.14  ? 176  TYR   A N   1 
ATOM   1339 C  CA  . TYR   A  1 201 ? -17.012 5.839   28.973 1.00 15.98  ? 176  TYR   A CA  1 
ATOM   1340 C  C   . TYR   A  1 201 ? -16.716 5.007   27.729 1.00 14.69  ? 176  TYR   A C   1 
ATOM   1341 O  O   . TYR   A  1 201 ? -16.426 3.811   27.830 1.00 13.76  ? 176  TYR   A O   1 
ATOM   1342 C  CB  . TYR   A  1 201 ? -18.510 6.111   29.095 1.00 18.56  ? 176  TYR   A CB  1 
ATOM   1343 C  CG  . TYR   A  1 201 ? -19.347 4.877   28.829 1.00 17.11  ? 176  TYR   A CG  1 
ATOM   1344 C  CD1 . TYR   A  1 201 ? -19.612 3.961   29.841 1.00 20.92  ? 176  TYR   A CD1 1 
ATOM   1345 C  CD2 . TYR   A  1 201 ? -19.853 4.615   27.560 1.00 16.37  ? 176  TYR   A CD2 1 
ATOM   1346 C  CE1 . TYR   A  1 201 ? -20.369 2.832   29.597 1.00 17.51  ? 176  TYR   A CE1 1 
ATOM   1347 C  CE2 . TYR   A  1 201 ? -20.608 3.486   27.308 1.00 15.42  ? 176  TYR   A CE2 1 
ATOM   1348 C  CZ  . TYR   A  1 201 ? -20.862 2.599   28.331 1.00 25.35  ? 176  TYR   A CZ  1 
ATOM   1349 O  OH  . TYR   A  1 201 ? -21.621 1.479   28.085 1.00 23.53  ? 176  TYR   A OH  1 
ATOM   1350 N  N   . MET   A  1 202 ? -16.803 5.617   26.541 1.00 17.63  ? 177  MET   A N   1 
ATOM   1351 C  CA  . MET   A  1 202 ? -16.646 4.852   25.303 1.00 16.72  ? 177  MET   A CA  1 
ATOM   1352 C  C   . MET   A  1 202 ? -15.261 4.246   25.175 1.00 16.00  ? 177  MET   A C   1 
ATOM   1353 O  O   . MET   A  1 202 ? -15.112 3.127   24.668 1.00 20.38  ? 177  MET   A O   1 
ATOM   1354 C  CB  . MET   A  1 202 ? -16.938 5.728   24.095 1.00 10.52  ? 177  MET   A CB  1 
ATOM   1355 C  CG  . MET   A  1 202 ? -18.380 5.999   23.920 1.00 19.53  ? 177  MET   A CG  1 
ATOM   1356 S  SD  . MET   A  1 202 ? -19.255 4.403   23.746 1.00 21.35  ? 177  MET   A SD  1 
ATOM   1357 C  CE  . MET   A  1 202 ? -18.429 3.752   22.272 1.00 25.71  ? 177  MET   A CE  1 
ATOM   1358 N  N   . VAL   A  1 203 ? -14.237 4.950   25.641 1.00 15.21  ? 178  VAL   A N   1 
ATOM   1359 C  CA  . VAL   A  1 203 ? -12.874 4.464   25.467 1.00 18.57  ? 178  VAL   A CA  1 
ATOM   1360 C  C   . VAL   A  1 203 ? -12.456 3.532   26.601 1.00 15.05  ? 178  VAL   A C   1 
ATOM   1361 O  O   . VAL   A  1 203 ? -12.032 2.400   26.356 1.00 16.03  ? 178  VAL   A O   1 
ATOM   1362 C  CB  . VAL   A  1 203 ? -11.905 5.655   25.324 1.00 18.63  ? 178  VAL   A CB  1 
ATOM   1363 C  CG1 . VAL   A  1 203 ? -10.457 5.169   25.338 1.00 13.18  ? 178  VAL   A CG1 1 
ATOM   1364 C  CG2 . VAL   A  1 203 ? -12.202 6.428   24.051 1.00 15.35  ? 178  VAL   A CG2 1 
ATOM   1365 N  N   . TYR   A  1 204 ? -12.561 3.976   27.858 1.00 18.67  ? 179  TYR   A N   1 
ATOM   1366 C  CA  . TYR   A  1 204 ? -12.026 3.178   28.959 1.00 18.97  ? 179  TYR   A CA  1 
ATOM   1367 C  C   . TYR   A  1 204 ? -12.966 2.049   29.346 1.00 20.93  ? 179  TYR   A C   1 
ATOM   1368 O  O   . TYR   A  1 204 ? -12.525 0.910   29.539 1.00 21.73  ? 179  TYR   A O   1 
ATOM   1369 C  CB  . TYR   A  1 204 ? -11.749 4.053   30.180 1.00 16.83  ? 179  TYR   A CB  1 
ATOM   1370 C  CG  . TYR   A  1 204 ? -10.612 5.030   30.028 1.00 23.28  ? 179  TYR   A CG  1 
ATOM   1371 C  CD1 . TYR   A  1 204 ? -9.382  4.621   29.534 1.00 18.80  ? 179  TYR   A CD1 1 
ATOM   1372 C  CD2 . TYR   A  1 204 ? -10.756 6.353   30.419 1.00 21.69  ? 179  TYR   A CD2 1 
ATOM   1373 C  CE1 . TYR   A  1 204 ? -8.333  5.508   29.409 1.00 29.61  ? 179  TYR   A CE1 1 
ATOM   1374 C  CE2 . TYR   A  1 204 ? -9.714  7.248   30.301 1.00 27.81  ? 179  TYR   A CE2 1 
ATOM   1375 C  CZ  . TYR   A  1 204 ? -8.503  6.820   29.795 1.00 29.51  ? 179  TYR   A CZ  1 
ATOM   1376 O  OH  . TYR   A  1 204 ? -7.459  7.707   29.681 1.00 34.54  ? 179  TYR   A OH  1 
ATOM   1377 N  N   . PHE   A  1 205 ? -14.262 2.336   29.447 1.00 21.42  ? 180  PHE   A N   1 
ATOM   1378 C  CA  . PHE   A  1 205 ? -15.205 1.350   29.959 1.00 17.96  ? 180  PHE   A CA  1 
ATOM   1379 C  C   . PHE   A  1 205 ? -15.706 0.442   28.839 1.00 17.54  ? 180  PHE   A C   1 
ATOM   1380 O  O   . PHE   A  1 205 ? -15.574 -0.783  28.920 1.00 25.17  ? 180  PHE   A O   1 
ATOM   1381 C  CB  . PHE   A  1 205 ? -16.370 2.065   30.657 1.00 18.41  ? 180  PHE   A CB  1 
ATOM   1382 C  CG  . PHE   A  1 205 ? -17.274 1.151   31.440 1.00 22.19  ? 180  PHE   A CG  1 
ATOM   1383 C  CD1 . PHE   A  1 205 ? -18.338 0.507   30.829 1.00 12.84  ? 180  PHE   A CD1 1 
ATOM   1384 C  CD2 . PHE   A  1 205 ? -17.068 0.952   32.797 1.00 24.90  ? 180  PHE   A CD2 1 
ATOM   1385 C  CE1 . PHE   A  1 205 ? -19.172 -0.326  31.552 1.00 29.34  ? 180  PHE   A CE1 1 
ATOM   1386 C  CE2 . PHE   A  1 205 ? -17.899 0.120   33.526 1.00 23.18  ? 180  PHE   A CE2 1 
ATOM   1387 C  CZ  . PHE   A  1 205 ? -18.951 -0.520  32.902 1.00 22.94  ? 180  PHE   A CZ  1 
ATOM   1388 N  N   . ASN   A  1 206 ? -16.288 1.029   27.791 1.00 19.62  ? 181  ASN   A N   1 
ATOM   1389 C  CA  . ASN   A  1 206 ? -16.870 0.214   26.730 1.00 20.88  ? 181  ASN   A CA  1 
ATOM   1390 C  C   . ASN   A  1 206 ? -15.790 -0.482  25.907 1.00 24.51  ? 181  ASN   A C   1 
ATOM   1391 O  O   . ASN   A  1 206 ? -15.808 -1.709  25.756 1.00 26.95  ? 181  ASN   A O   1 
ATOM   1392 C  CB  . ASN   A  1 206 ? -17.769 1.061   25.831 1.00 18.65  ? 181  ASN   A CB  1 
ATOM   1393 C  CG  . ASN   A  1 206 ? -18.620 0.211   24.907 1.00 29.01  ? 181  ASN   A CG  1 
ATOM   1394 O  OD1 . ASN   A  1 206 ? -19.658 -0.313  25.311 1.00 27.02  ? 181  ASN   A OD1 1 
ATOM   1395 N  ND2 . ASN   A  1 206 ? -18.171 0.050   23.667 1.00 18.02  ? 181  ASN   A ND2 1 
ATOM   1396 N  N   . PHE   A  1 207 ? -14.831 0.281   25.375 1.00 16.87  ? 182  PHE   A N   1 
ATOM   1397 C  CA  . PHE   A  1 207 ? -13.849 -0.305  24.466 1.00 23.02  ? 182  PHE   A CA  1 
ATOM   1398 C  C   . PHE   A  1 207 ? -12.835 -1.155  25.223 1.00 17.39  ? 182  PHE   A C   1 
ATOM   1399 O  O   . PHE   A  1 207 ? -12.755 -2.372  25.018 1.00 23.74  ? 182  PHE   A O   1 
ATOM   1400 C  CB  . PHE   A  1 207 ? -13.147 0.795   23.663 1.00 15.83  ? 182  PHE   A CB  1 
ATOM   1401 C  CG  . PHE   A  1 207 ? -12.190 0.274   22.623 1.00 24.12  ? 182  PHE   A CG  1 
ATOM   1402 C  CD1 . PHE   A  1 207 ? -12.449 -0.913  21.956 1.00 22.20  ? 182  PHE   A CD1 1 
ATOM   1403 C  CD2 . PHE   A  1 207 ? -11.041 0.979   22.302 1.00 24.46  ? 182  PHE   A CD2 1 
ATOM   1404 C  CE1 . PHE   A  1 207 ? -11.576 -1.392  20.995 1.00 16.79  ? 182  PHE   A CE1 1 
ATOM   1405 C  CE2 . PHE   A  1 207 ? -10.164 0.506   21.341 1.00 29.89  ? 182  PHE   A CE2 1 
ATOM   1406 C  CZ  . PHE   A  1 207 ? -10.432 -0.682  20.688 1.00 22.87  ? 182  PHE   A CZ  1 
ATOM   1407 N  N   . PHE   A  1 208 ? -12.038 -0.530  26.093 1.00 16.24  ? 183  PHE   A N   1 
ATOM   1408 C  CA  . PHE   A  1 208 ? -10.926 -1.247  26.712 1.00 23.05  ? 183  PHE   A CA  1 
ATOM   1409 C  C   . PHE   A  1 208 ? -11.425 -2.400  27.575 1.00 18.91  ? 183  PHE   A C   1 
ATOM   1410 O  O   . PHE   A  1 208 ? -11.018 -3.552  27.390 1.00 22.13  ? 183  PHE   A O   1 
ATOM   1411 C  CB  . PHE   A  1 208 ? -10.074 -0.289  27.548 1.00 19.90  ? 183  PHE   A CB  1 
ATOM   1412 C  CG  . PHE   A  1 208 ? -9.230  0.657   26.736 1.00 18.11  ? 183  PHE   A CG  1 
ATOM   1413 C  CD1 . PHE   A  1 208 ? -9.250  0.627   25.352 1.00 25.72  ? 183  PHE   A CD1 1 
ATOM   1414 C  CD2 . PHE   A  1 208 ? -8.411  1.578   27.368 1.00 29.57  ? 183  PHE   A CD2 1 
ATOM   1415 C  CE1 . PHE   A  1 208 ? -8.467  1.498   24.614 1.00 24.79  ? 183  PHE   A CE1 1 
ATOM   1416 C  CE2 . PHE   A  1 208 ? -7.628  2.450   26.637 1.00 27.12  ? 183  PHE   A CE2 1 
ATOM   1417 C  CZ  . PHE   A  1 208 ? -7.657  2.410   25.258 1.00 21.00  ? 183  PHE   A CZ  1 
ATOM   1418 N  N   . ALA   A  1 209 ? -12.325 -2.108  28.516 1.00 15.79  ? 184  ALA   A N   1 
ATOM   1419 C  CA  . ALA   A  1 209 ? -12.728 -3.117  29.490 1.00 21.46  ? 184  ALA   A CA  1 
ATOM   1420 C  C   . ALA   A  1 209 ? -13.702 -4.129  28.899 1.00 24.40  ? 184  ALA   A C   1 
ATOM   1421 O  O   . ALA   A  1 209 ? -13.541 -5.339  29.090 1.00 22.28  ? 184  ALA   A O   1 
ATOM   1422 C  CB  . ALA   A  1 209 ? -13.343 -2.440  30.716 1.00 18.83  ? 184  ALA   A CB  1 
ATOM   1423 N  N   . CYS   A  1 210 ? -14.721 -3.655  28.183 1.00 16.76  ? 185  CYS   A N   1 
ATOM   1424 C  CA  . CYS   A  1 210 ? -15.840 -4.505  27.800 1.00 27.95  ? 185  CYS   A CA  1 
ATOM   1425 C  C   . CYS   A  1 210 ? -15.718 -5.097  26.401 1.00 18.50  ? 185  CYS   A C   1 
ATOM   1426 O  O   . CYS   A  1 210 ? -16.473 -6.018  26.074 1.00 22.32  ? 185  CYS   A O   1 
ATOM   1427 C  CB  . CYS   A  1 210 ? -17.154 -3.719  27.911 1.00 25.34  ? 185  CYS   A CB  1 
ATOM   1428 S  SG  . CYS   A  1 210 ? -17.609 -3.305  29.612 1.00 32.68  ? 185  CYS   A SG  1 
ATOM   1429 N  N   . VAL   A  1 211 ? -14.798 -4.605  25.573 1.00 19.65  ? 186  VAL   A N   1 
ATOM   1430 C  CA  . VAL   A  1 211 ? -14.675 -5.098  24.205 1.00 21.03  ? 186  VAL   A CA  1 
ATOM   1431 C  C   . VAL   A  1 211 ? -13.284 -5.674  23.978 1.00 27.68  ? 186  VAL   A C   1 
ATOM   1432 O  O   . VAL   A  1 211 ? -13.138 -6.834  23.575 1.00 21.49  ? 186  VAL   A O   1 
ATOM   1433 C  CB  . VAL   A  1 211 ? -14.976 -3.988  23.180 1.00 23.59  ? 186  VAL   A CB  1 
ATOM   1434 C  CG1 . VAL   A  1 211 ? -14.615 -4.451  21.774 1.00 20.08  ? 186  VAL   A CG1 1 
ATOM   1435 C  CG2 . VAL   A  1 211 ? -16.435 -3.567  23.256 1.00 22.95  ? 186  VAL   A CG2 1 
ATOM   1436 N  N   A LEU   A  1 212 ? -12.253 -4.869  24.242 0.45 19.89  ? 187  LEU   A N   1 
ATOM   1437 N  N   B LEU   A  1 212 ? -12.255 -4.860  24.228 0.55 19.86  ? 187  LEU   A N   1 
ATOM   1438 C  CA  A LEU   A  1 212 ? -10.886 -5.295  23.956 0.45 22.66  ? 187  LEU   A CA  1 
ATOM   1439 C  CA  B LEU   A  1 212 ? -10.882 -5.284  23.967 0.55 22.68  ? 187  LEU   A CA  1 
ATOM   1440 C  C   A LEU   A  1 212 ? -10.480 -6.478  24.826 0.45 22.21  ? 187  LEU   A C   1 
ATOM   1441 C  C   B LEU   A  1 212 ? -10.501 -6.484  24.824 0.55 22.21  ? 187  LEU   A C   1 
ATOM   1442 O  O   A LEU   A  1 212 ? -9.920  -7.463  24.331 0.45 21.82  ? 187  LEU   A O   1 
ATOM   1443 O  O   B LEU   A  1 212 ? -9.976  -7.482  24.317 0.55 21.81  ? 187  LEU   A O   1 
ATOM   1444 C  CB  A LEU   A  1 212 ? -9.922  -4.124  24.150 0.45 21.82  ? 187  LEU   A CB  1 
ATOM   1445 C  CB  B LEU   A  1 212 ? -9.920  -4.122  24.219 0.55 21.82  ? 187  LEU   A CB  1 
ATOM   1446 C  CG  A LEU   A  1 212 ? -8.506  -4.335  23.611 0.45 21.02  ? 187  LEU   A CG  1 
ATOM   1447 C  CG  B LEU   A  1 212 ? -9.502  -3.287  23.008 0.55 19.64  ? 187  LEU   A CG  1 
ATOM   1448 C  CD1 A LEU   A  1 212 ? -8.546  -4.836  22.174 0.45 22.96  ? 187  LEU   A CD1 1 
ATOM   1449 C  CD1 B LEU   A  1 212 ? -8.326  -2.386  23.357 0.55 24.18  ? 187  LEU   A CD1 1 
ATOM   1450 C  CD2 A LEU   A  1 212 ? -7.695  -3.052  23.710 0.45 26.38  ? 187  LEU   A CD2 1 
ATOM   1451 C  CD2 B LEU   A  1 212 ? -9.168  -4.177  21.819 0.55 21.75  ? 187  LEU   A CD2 1 
ATOM   1452 N  N   . VAL   A  1 213 ? -10.756 -6.400  26.131 1.00 18.69  ? 188  VAL   A N   1 
ATOM   1453 C  CA  . VAL   A  1 213 ? -10.392 -7.497  27.030 1.00 23.92  ? 188  VAL   A CA  1 
ATOM   1454 C  C   . VAL   A  1 213 ? -11.094 -8.801  26.668 1.00 20.84  ? 188  VAL   A C   1 
ATOM   1455 O  O   . VAL   A  1 213 ? -10.416 -9.837  26.583 1.00 24.86  ? 188  VAL   A O   1 
ATOM   1456 C  CB  . VAL   A  1 213 ? -10.622 -7.079  28.496 1.00 24.61  ? 188  VAL   A CB  1 
ATOM   1457 C  CG1 . VAL   A  1 213 ? -10.562 -8.293  29.410 1.00 25.36  ? 188  VAL   A CG1 1 
ATOM   1458 C  CG2 . VAL   A  1 213 ? -9.590  -6.046  28.919 1.00 18.13  ? 188  VAL   A CG2 1 
ATOM   1459 N  N   . PRO   A  1 214 ? -12.415 -8.835  26.441 1.00 21.13  ? 189  PRO   A N   1 
ATOM   1460 C  CA  . PRO   A  1 214 ? -13.025 -10.101 25.995 1.00 27.09  ? 189  PRO   A CA  1 
ATOM   1461 C  C   . PRO   A  1 214 ? -12.488 -10.615 24.669 1.00 24.81  ? 189  PRO   A C   1 
ATOM   1462 O  O   . PRO   A  1 214 ? -12.316 -11.830 24.514 1.00 19.32  ? 189  PRO   A O   1 
ATOM   1463 C  CB  . PRO   A  1 214 ? -14.514 -9.749  25.895 1.00 25.74  ? 189  PRO   A CB  1 
ATOM   1464 C  CG  . PRO   A  1 214 ? -14.703 -8.650  26.862 1.00 25.61  ? 189  PRO   A CG  1 
ATOM   1465 C  CD  . PRO   A  1 214 ? -13.447 -7.832  26.769 1.00 23.85  ? 189  PRO   A CD  1 
ATOM   1466 N  N   . LEU   A  1 215 ? -12.220 -9.733  23.701 1.00 17.11  ? 190  LEU   A N   1 
ATOM   1467 C  CA  . LEU   A  1 215 ? -11.654 -10.192 22.435 1.00 21.31  ? 190  LEU   A CA  1 
ATOM   1468 C  C   . LEU   A  1 215 ? -10.278 -10.812 22.636 1.00 25.44  ? 190  LEU   A C   1 
ATOM   1469 O  O   . LEU   A  1 215 ? -9.952  -11.832 22.015 1.00 25.74  ? 190  LEU   A O   1 
ATOM   1470 C  CB  . LEU   A  1 215 ? -11.583 -9.038  21.434 1.00 17.22  ? 190  LEU   A CB  1 
ATOM   1471 C  CG  . LEU   A  1 215 ? -12.921 -8.561  20.864 1.00 27.82  ? 190  LEU   A CG  1 
ATOM   1472 C  CD1 . LEU   A  1 215 ? -12.741 -7.291  20.042 1.00 28.32  ? 190  LEU   A CD1 1 
ATOM   1473 C  CD2 . LEU   A  1 215 ? -13.580 -9.656  20.037 1.00 23.28  ? 190  LEU   A CD2 1 
ATOM   1474 N  N   . LEU   A  1 216 ? -9.451  -10.210 23.494 1.00 20.71  ? 191  LEU   A N   1 
ATOM   1475 C  CA  . LEU   A  1 216 ? -8.146  -10.792 23.787 1.00 21.36  ? 191  LEU   A CA  1 
ATOM   1476 C  C   . LEU   A  1 216 ? -8.282  -12.128 24.511 1.00 27.49  ? 191  LEU   A C   1 
ATOM   1477 O  O   . LEU   A  1 216 ? -7.504  -13.056 24.259 1.00 26.36  ? 191  LEU   A O   1 
ATOM   1478 C  CB  . LEU   A  1 216 ? -7.300  -9.810  24.599 1.00 23.01  ? 191  LEU   A CB  1 
ATOM   1479 C  CG  . LEU   A  1 216 ? -6.881  -8.549  23.839 1.00 27.18  ? 191  LEU   A CG  1 
ATOM   1480 C  CD1 . LEU   A  1 216 ? -6.183  -7.553  24.755 1.00 35.19  ? 191  LEU   A CD1 1 
ATOM   1481 C  CD2 . LEU   A  1 216 ? -5.998  -8.903  22.651 1.00 32.31  ? 191  LEU   A CD2 1 
ATOM   1482 N  N   . LEU   A  1 217 ? -9.256  -12.242 25.420 1.00 19.98  ? 192  LEU   A N   1 
ATOM   1483 C  CA  . LEU   A  1 217 ? -9.542  -13.528 26.049 1.00 23.62  ? 192  LEU   A CA  1 
ATOM   1484 C  C   . LEU   A  1 217 ? -9.952  -14.569 25.014 1.00 22.38  ? 192  LEU   A C   1 
ATOM   1485 O  O   . LEU   A  1 217 ? -9.528  -15.728 25.088 1.00 27.59  ? 192  LEU   A O   1 
ATOM   1486 C  CB  . LEU   A  1 217 ? -10.639 -13.371 27.104 1.00 25.20  ? 192  LEU   A CB  1 
ATOM   1487 C  CG  . LEU   A  1 217 ? -10.310 -12.572 28.364 1.00 33.76  ? 192  LEU   A CG  1 
ATOM   1488 C  CD1 . LEU   A  1 217 ? -11.545 -12.428 29.241 1.00 32.39  ? 192  LEU   A CD1 1 
ATOM   1489 C  CD2 . LEU   A  1 217 ? -9.173  -13.221 29.140 1.00 35.93  ? 192  LEU   A CD2 1 
ATOM   1490 N  N   . MET   A  1 218 ? -10.785 -14.176 24.046 1.00 22.62  ? 193  MET   A N   1 
ATOM   1491 C  CA  . MET   A  1 218 ? -11.164 -15.083 22.966 1.00 27.25  ? 193  MET   A CA  1 
ATOM   1492 C  C   . MET   A  1 218 ? -9.937  -15.568 22.209 1.00 21.82  ? 193  MET   A C   1 
ATOM   1493 O  O   . MET   A  1 218 ? -9.811  -16.759 21.902 1.00 25.38  ? 193  MET   A O   1 
ATOM   1494 C  CB  . MET   A  1 218 ? -12.126 -14.386 22.007 1.00 25.81  ? 193  MET   A CB  1 
ATOM   1495 C  CG  . MET   A  1 218 ? -13.552 -14.328 22.488 1.00 38.31  ? 193  MET   A CG  1 
ATOM   1496 S  SD  . MET   A  1 218 ? -14.574 -13.456 21.289 1.00 34.47  ? 193  MET   A SD  1 
ATOM   1497 C  CE  . MET   A  1 218 ? -15.485 -12.337 22.357 1.00 33.69  ? 193  MET   A CE  1 
ATOM   1498 N  N   . LEU   A  1 219 ? -9.032  -14.644 21.877 1.00 25.81  ? 194  LEU   A N   1 
ATOM   1499 C  CA  . LEU   A  1 219 ? -7.799  -15.014 21.193 1.00 28.64  ? 194  LEU   A CA  1 
ATOM   1500 C  C   . LEU   A  1 219 ? -7.027  -16.058 21.989 1.00 24.14  ? 194  LEU   A C   1 
ATOM   1501 O  O   . LEU   A  1 219 ? -6.539  -17.045 21.429 1.00 25.89  ? 194  LEU   A O   1 
ATOM   1502 C  CB  . LEU   A  1 219 ? -6.949  -13.761 20.973 1.00 27.55  ? 194  LEU   A CB  1 
ATOM   1503 C  CG  . LEU   A  1 219 ? -5.557  -13.930 20.362 1.00 33.47  ? 194  LEU   A CG  1 
ATOM   1504 C  CD1 . LEU   A  1 219 ? -5.642  -14.608 19.004 1.00 35.28  ? 194  LEU   A CD1 1 
ATOM   1505 C  CD2 . LEU   A  1 219 ? -4.851  -12.585 20.260 1.00 35.13  ? 194  LEU   A CD2 1 
ATOM   1506 N  N   . GLY   A  1 220 ? -6.908  -15.852 23.302 1.00 26.01  ? 195  GLY   A N   1 
ATOM   1507 C  CA  . GLY   A  1 220 ? -6.229  -16.831 24.134 1.00 25.31  ? 195  GLY   A CA  1 
ATOM   1508 C  C   . GLY   A  1 220 ? -6.909  -18.186 24.142 1.00 28.03  ? 195  GLY   A C   1 
ATOM   1509 O  O   . GLY   A  1 220 ? -6.245  -19.223 24.092 1.00 33.71  ? 195  GLY   A O   1 
ATOM   1510 N  N   . VAL   A  1 221 ? -8.242  -18.198 24.212 1.00 20.64  ? 196  VAL   A N   1 
ATOM   1511 C  CA  . VAL   A  1 221 ? -8.979  -19.460 24.153 1.00 19.40  ? 196  VAL   A CA  1 
ATOM   1512 C  C   . VAL   A  1 221 ? -8.750  -20.166 22.821 1.00 27.31  ? 196  VAL   A C   1 
ATOM   1513 O  O   . VAL   A  1 221 ? -8.502  -21.378 22.778 1.00 27.37  ? 196  VAL   A O   1 
ATOM   1514 C  CB  . VAL   A  1 221 ? -10.478 -19.223 24.409 1.00 21.78  ? 196  VAL   A CB  1 
ATOM   1515 C  CG1 . VAL   A  1 221 ? -11.256 -20.523 24.261 1.00 23.04  ? 196  VAL   A CG1 1 
ATOM   1516 C  CG2 . VAL   A  1 221 ? -10.688 -18.642 25.797 1.00 16.27  ? 196  VAL   A CG2 1 
ATOM   1517 N  N   . TYR   A  1 222 ? -8.835  -19.425 21.713 1.00 24.99  ? 197  TYR   A N   1 
ATOM   1518 C  CA  . TYR   A  1 222 ? -8.627  -20.043 20.407 1.00 29.67  ? 197  TYR   A CA  1 
ATOM   1519 C  C   . TYR   A  1 222 ? -7.207  -20.569 20.257 1.00 34.06  ? 197  TYR   A C   1 
ATOM   1520 O  O   . TYR   A  1 222 ? -6.996  -21.645 19.684 1.00 24.45  ? 197  TYR   A O   1 
ATOM   1521 C  CB  . TYR   A  1 222 ? -8.976  -19.055 19.299 1.00 25.84  ? 197  TYR   A CB  1 
ATOM   1522 C  CG  . TYR   A  1 222 ? -10.463 -18.997 19.062 1.00 27.19  ? 197  TYR   A CG  1 
ATOM   1523 C  CD1 . TYR   A  1 222 ? -11.150 -20.114 18.604 1.00 26.16  ? 197  TYR   A CD1 1 
ATOM   1524 C  CD2 . TYR   A  1 222 ? -11.186 -17.843 19.327 1.00 28.92  ? 197  TYR   A CD2 1 
ATOM   1525 C  CE1 . TYR   A  1 222 ? -12.511 -20.075 18.389 1.00 24.02  ? 197  TYR   A CE1 1 
ATOM   1526 C  CE2 . TYR   A  1 222 ? -12.550 -17.797 19.122 1.00 26.34  ? 197  TYR   A CE2 1 
ATOM   1527 C  CZ  . TYR   A  1 222 ? -13.207 -18.914 18.652 1.00 32.82  ? 197  TYR   A CZ  1 
ATOM   1528 O  OH  . TYR   A  1 222 ? -14.566 -18.868 18.456 1.00 31.90  ? 197  TYR   A OH  1 
ATOM   1529 N  N   . LEU   A  1 223 ? -6.218  -19.824 20.754 1.00 24.79  ? 198  LEU   A N   1 
ATOM   1530 C  CA  . LEU   A  1 223 ? -4.855  -20.343 20.756 1.00 30.90  ? 198  LEU   A CA  1 
ATOM   1531 C  C   . LEU   A  1 223 ? -4.749  -21.649 21.537 1.00 28.17  ? 198  LEU   A C   1 
ATOM   1532 O  O   . LEU   A  1 223 ? -4.093  -22.591 21.085 1.00 31.44  ? 198  LEU   A O   1 
ATOM   1533 C  CB  . LEU   A  1 223 ? -3.897  -19.304 21.319 1.00 26.30  ? 198  LEU   A CB  1 
ATOM   1534 C  CG  . LEU   A  1 223 ? -3.679  -18.078 20.446 1.00 39.73  ? 198  LEU   A CG  1 
ATOM   1535 C  CD1 . LEU   A  1 223 ? -2.800  -17.046 21.139 1.00 27.96  ? 198  LEU   A CD1 1 
ATOM   1536 C  CD2 . LEU   A  1 223 ? -3.089  -18.482 19.109 1.00 32.19  ? 198  LEU   A CD2 1 
ATOM   1537 N  N   . ARG   A  1 224 ? -5.378  -21.736 22.714 1.00 29.70  ? 199  ARG   A N   1 
ATOM   1538 C  CA  . ARG   A  1 224 ? -5.337  -23.002 23.451 1.00 28.87  ? 199  ARG   A CA  1 
ATOM   1539 C  C   . ARG   A  1 224 ? -6.079  -24.104 22.692 1.00 33.74  ? 199  ARG   A C   1 
ATOM   1540 O  O   . ARG   A  1 224 ? -5.680  -25.272 22.745 1.00 31.69  ? 199  ARG   A O   1 
ATOM   1541 C  CB  . ARG   A  1 224 ? -5.898  -22.851 24.871 1.00 30.46  ? 199  ARG   A CB  1 
ATOM   1542 C  CG  . ARG   A  1 224 ? -5.094  -21.924 25.862 1.00 36.01  ? 199  ARG   A CG  1 
ATOM   1543 C  CD  . ARG   A  1 224 ? -5.679  -22.013 27.279 1.00 52.34  ? 199  ARG   A CD  1 
ATOM   1544 N  NE  . ARG   A  1 224 ? -5.407  -20.844 28.112 1.00 69.77  ? 199  ARG   A NE  1 
ATOM   1545 C  CZ  . ARG   A  1 224 ? -4.326  -20.746 28.868 1.00 76.33  ? 199  ARG   A CZ  1 
ATOM   1546 N  NH1 . ARG   A  1 224 ? -3.428  -21.720 28.900 1.00 78.71  ? 199  ARG   A NH1 1 
ATOM   1547 N  NH2 . ARG   A  1 224 ? -4.211  -19.729 29.718 1.00 79.70  ? 199  ARG   A NH2 1 
ATOM   1548 N  N   . ILE   A  1 225 ? -7.193  -23.773 22.026 1.00 28.12  ? 200  ILE   A N   1 
ATOM   1549 C  CA  . ILE   A  1 225 ? -7.924  -24.789 21.259 1.00 24.38  ? 200  ILE   A CA  1 
ATOM   1550 C  C   . ILE   A  1 225 ? -7.032  -25.387 20.179 1.00 28.66  ? 200  ILE   A C   1 
ATOM   1551 O  O   . ILE   A  1 225 ? -6.908  -26.612 20.055 1.00 27.85  ? 200  ILE   A O   1 
ATOM   1552 C  CB  . ILE   A  1 225 ? -9.207  -24.196 20.643 1.00 27.11  ? 200  ILE   A CB  1 
ATOM   1553 C  CG1 . ILE   A  1 225 ? -10.248 -23.911 21.723 1.00 34.82  ? 200  ILE   A CG1 1 
ATOM   1554 C  CG2 . ILE   A  1 225 ? -9.780  -25.132 19.573 1.00 20.05  ? 200  ILE   A CG2 1 
ATOM   1555 C  CD1 . ILE   A  1 225 ? -11.419 -23.096 21.230 1.00 20.69  ? 200  ILE   A CD1 1 
ATOM   1556 N  N   . PHE   A  1 226 ? -6.404  -24.530 19.374 1.00 27.07  ? 201  PHE   A N   1 
ATOM   1557 C  CA  . PHE   A  1 226 ? -5.596  -25.016 18.263 1.00 34.31  ? 201  PHE   A CA  1 
ATOM   1558 C  C   . PHE   A  1 226 ? -4.340  -25.731 18.749 1.00 36.92  ? 201  PHE   A C   1 
ATOM   1559 O  O   . PHE   A  1 226 ? -3.902  -26.701 18.121 1.00 36.20  ? 201  PHE   A O   1 
ATOM   1560 C  CB  . PHE   A  1 226 ? -5.234  -23.858 17.334 1.00 28.74  ? 201  PHE   A CB  1 
ATOM   1561 C  CG  . PHE   A  1 226 ? -6.411  -23.280 16.604 1.00 35.93  ? 201  PHE   A CG  1 
ATOM   1562 C  CD1 . PHE   A  1 226 ? -7.265  -24.103 15.890 1.00 25.25  ? 201  PHE   A CD1 1 
ATOM   1563 C  CD2 . PHE   A  1 226 ? -6.662  -21.918 16.623 1.00 35.03  ? 201  PHE   A CD2 1 
ATOM   1564 C  CE1 . PHE   A  1 226 ? -8.353  -23.582 15.213 1.00 33.00  ? 201  PHE   A CE1 1 
ATOM   1565 C  CE2 . PHE   A  1 226 ? -7.749  -21.390 15.948 1.00 32.60  ? 201  PHE   A CE2 1 
ATOM   1566 C  CZ  . PHE   A  1 226 ? -8.594  -22.223 15.242 1.00 32.46  ? 201  PHE   A CZ  1 
ATOM   1567 N  N   . ALA   A  1 227 ? -3.749  -25.272 19.855 1.00 32.70  ? 202  ALA   A N   1 
ATOM   1568 C  CA  . ALA   A  1 227 ? -2.610  -25.983 20.428 1.00 36.02  ? 202  ALA   A CA  1 
ATOM   1569 C  C   . ALA   A  1 227 ? -3.026  -27.347 20.967 1.00 37.41  ? 202  ALA   A C   1 
ATOM   1570 O  O   . ALA   A  1 227 ? -2.282  -28.327 20.835 1.00 43.39  ? 202  ALA   A O   1 
ATOM   1571 C  CB  . ALA   A  1 227 ? -1.965  -25.144 21.531 1.00 21.96  ? 202  ALA   A CB  1 
ATOM   1572 N  N   . ALA   A  1 228 ? -4.208  -27.429 21.579 1.00 33.08  ? 203  ALA   A N   1 
ATOM   1573 C  CA  . ALA   A  1 228 ? -4.695  -28.715 22.067 1.00 30.35  ? 203  ALA   A CA  1 
ATOM   1574 C  C   . ALA   A  1 228 ? -4.981  -29.667 20.914 1.00 46.33  ? 203  ALA   A C   1 
ATOM   1575 O  O   . ALA   A  1 228 ? -4.645  -30.854 20.985 1.00 42.34  ? 203  ALA   A O   1 
ATOM   1576 C  CB  . ALA   A  1 228 ? -5.944  -28.516 22.926 1.00 27.94  ? 203  ALA   A CB  1 
ATOM   1577 N  N   . ALA   A  1 229 ? -5.587  -29.161 19.837 1.00 35.72  ? 204  ALA   A N   1 
ATOM   1578 C  CA  . ALA   A  1 229 ? -5.824  -29.985 18.656 1.00 35.27  ? 204  ALA   A CA  1 
ATOM   1579 C  C   . ALA   A  1 229 ? -4.519  -30.501 18.061 1.00 44.64  ? 204  ALA   A C   1 
ATOM   1580 O  O   . ALA   A  1 229 ? -4.424  -31.674 17.680 1.00 36.64  ? 204  ALA   A O   1 
ATOM   1581 C  CB  . ALA   A  1 229 ? -6.603  -29.188 17.611 1.00 29.60  ? 204  ALA   A CB  1 
ATOM   1582 N  N   A ARG   A  1 230 ? -3.502  -29.642 17.973 0.46 43.39  ? 205  ARG   A N   1 
ATOM   1583 N  N   B ARG   A  1 230 ? -3.504  -29.638 17.976 0.54 43.39  ? 205  ARG   A N   1 
ATOM   1584 C  CA  A ARG   A  1 230 ? -2.235  -30.067 17.384 0.46 46.27  ? 205  ARG   A CA  1 
ATOM   1585 C  CA  B ARG   A  1 230 ? -2.229  -30.043 17.395 0.54 46.23  ? 205  ARG   A CA  1 
ATOM   1586 C  C   A ARG   A  1 230 ? -1.531  -31.096 18.259 0.46 44.53  ? 205  ARG   A C   1 
ATOM   1587 C  C   B ARG   A  1 230 ? -1.535  -31.090 18.259 0.54 44.53  ? 205  ARG   A C   1 
ATOM   1588 O  O   A ARG   A  1 230 ? -0.911  -32.033 17.742 0.46 43.33  ? 205  ARG   A O   1 
ATOM   1589 O  O   B ARG   A  1 230 ? -0.927  -32.031 17.735 0.54 43.30  ? 205  ARG   A O   1 
ATOM   1590 C  CB  A ARG   A  1 230 ? -1.335  -28.856 17.145 0.46 60.93  ? 205  ARG   A CB  1 
ATOM   1591 C  CB  B ARG   A  1 230 ? -1.328  -28.823 17.208 0.54 60.89  ? 205  ARG   A CB  1 
ATOM   1592 C  CG  A ARG   A  1 230 ? -1.734  -28.040 15.930 0.46 59.99  ? 205  ARG   A CG  1 
ATOM   1593 C  CG  B ARG   A  1 230 ? -0.004  -29.132 16.538 0.54 63.40  ? 205  ARG   A CG  1 
ATOM   1594 C  CD  A ARG   A  1 230 ? -0.529  -27.628 15.101 0.46 61.93  ? 205  ARG   A CD  1 
ATOM   1595 C  CD  B ARG   A  1 230 ? 1.161   -28.947 17.491 0.54 64.63  ? 205  ARG   A CD  1 
ATOM   1596 N  NE  A ARG   A  1 230 ? -0.232  -28.565 14.024 0.46 64.68  ? 205  ARG   A NE  1 
ATOM   1597 N  NE  B ARG   A  1 230 ? 1.500   -27.547 17.717 0.54 64.43  ? 205  ARG   A NE  1 
ATOM   1598 C  CZ  A ARG   A  1 230 ? -0.810  -28.545 12.830 0.46 70.53  ? 205  ARG   A CZ  1 
ATOM   1599 C  CZ  B ARG   A  1 230 ? 1.298   -26.904 18.859 0.54 71.54  ? 205  ARG   A CZ  1 
ATOM   1600 N  NH1 A ARG   A  1 230 ? -1.759  -27.672 12.536 0.46 70.67  ? 205  ARG   A NH1 1 
ATOM   1601 N  NH1 B ARG   A  1 230 ? 0.686   -27.483 19.879 0.54 55.87  ? 205  ARG   A NH1 1 
ATOM   1602 N  NH2 A ARG   A  1 230 ? -0.429  -29.426 11.909 0.46 64.63  ? 205  ARG   A NH2 1 
ATOM   1603 N  NH2 B ARG   A  1 230 ? 1.730   -25.653 18.985 0.54 65.68  ? 205  ARG   A NH2 1 
ATOM   1604 N  N   . ARG   A  1 231 ? -1.612  -30.942 19.583 1.00 37.84  ? 206  ARG   A N   1 
ATOM   1605 C  CA  . ARG   A  1 231 ? -0.981  -31.914 20.468 1.00 39.21  ? 206  ARG   A CA  1 
ATOM   1606 C  C   . ARG   A  1 231 ? -1.684  -33.262 20.386 1.00 47.52  ? 206  ARG   A C   1 
ATOM   1607 O  O   . ARG   A  1 231 ? -1.029  -34.311 20.382 1.00 47.80  ? 206  ARG   A O   1 
ATOM   1608 C  CB  . ARG   A  1 231 ? -0.982  -31.394 21.905 1.00 32.28  ? 206  ARG   A CB  1 
ATOM   1609 C  CG  . ARG   A  1 231 ? -0.448  -32.384 22.931 1.00 50.42  ? 206  ARG   A CG  1 
ATOM   1610 N  N   . GLN   A  1 232 ? -3.017  -33.256 20.321 1.00 44.63  ? 207  GLN   A N   1 
ATOM   1611 C  CA  . GLN   A  1 232 ? -3.750  -34.516 20.306 1.00 40.71  ? 207  GLN   A CA  1 
ATOM   1612 C  C   . GLN   A  1 232 ? -3.537  -35.251 18.989 1.00 39.64  ? 207  GLN   A C   1 
ATOM   1613 O  O   . GLN   A  1 232 ? -3.428  -36.483 18.969 1.00 45.07  ? 207  GLN   A O   1 
ATOM   1614 C  CB  . GLN   A  1 232 ? -5.235  -34.261 20.560 1.00 41.16  ? 207  GLN   A CB  1 
ATOM   1615 C  CG  . GLN   A  1 232 ? -5.518  -33.644 21.921 1.00 38.82  ? 207  GLN   A CG  1 
ATOM   1616 C  CD  . GLN   A  1 232 ? -6.997  -33.479 22.199 1.00 49.77  ? 207  GLN   A CD  1 
ATOM   1617 O  OE1 . GLN   A  1 232 ? -7.836  -34.120 21.568 1.00 44.64  ? 207  GLN   A OE1 1 
ATOM   1618 N  NE2 . GLN   A  1 232 ? -7.326  -32.606 23.146 1.00 43.87  ? 207  GLN   A NE2 1 
ATOM   1619 N  N   . LEU   A  1 233 ? -3.484  -34.510 17.878 1.00 41.52  ? 208  LEU   A N   1 
ATOM   1620 C  CA  . LEU   A  1 233 ? -3.194  -35.124 16.587 1.00 37.85  ? 208  LEU   A CA  1 
ATOM   1621 C  C   . LEU   A  1 233 ? -1.782  -35.693 16.548 1.00 56.24  ? 208  LEU   A C   1 
ATOM   1622 O  O   . LEU   A  1 233 ? -1.565  -36.799 16.040 1.00 44.09  ? 208  LEU   A O   1 
ATOM   1623 C  CB  . LEU   A  1 233 ? -3.376  -34.096 15.471 1.00 41.18  ? 208  LEU   A CB  1 
ATOM   1624 C  CG  . LEU   A  1 233 ? -4.797  -33.699 15.078 1.00 59.78  ? 208  LEU   A CG  1 
ATOM   1625 C  CD1 . LEU   A  1 233 ? -4.768  -32.537 14.099 1.00 50.74  ? 208  LEU   A CD1 1 
ATOM   1626 C  CD2 . LEU   A  1 233 ? -5.506  -34.888 14.460 1.00 58.25  ? 208  LEU   A CD2 1 
ATOM   1627 N  N   . ALA   A  1 234 ? -0.809  -34.944 17.073 1.00 44.18  ? 1001 ALA   A N   1 
ATOM   1628 C  CA  . ALA   A  1 234 ? 0.556   -35.452 17.151 1.00 51.05  ? 1001 ALA   A CA  1 
ATOM   1629 C  C   . ALA   A  1 234 ? 0.639   -36.709 18.006 1.00 50.08  ? 1001 ALA   A C   1 
ATOM   1630 O  O   . ALA   A  1 234 ? 1.337   -37.663 17.649 1.00 58.12  ? 1001 ALA   A O   1 
ATOM   1631 C  CB  . ALA   A  1 234 ? 1.486   -34.371 17.700 1.00 41.03  ? 1001 ALA   A CB  1 
ATOM   1632 N  N   . ASP   A  1 235 ? -0.078  -36.733 19.132 1.00 50.12  ? 1002 ASP   A N   1 
ATOM   1633 C  CA  . ASP   A  1 235 ? -0.073  -37.912 19.993 1.00 51.30  ? 1002 ASP   A CA  1 
ATOM   1634 C  C   . ASP   A  1 235 ? -0.673  -39.139 19.315 1.00 57.17  ? 1002 ASP   A C   1 
ATOM   1635 O  O   . ASP   A  1 235 ? -0.184  -40.259 19.511 1.00 59.21  ? 1002 ASP   A O   1 
ATOM   1636 C  CB  . ASP   A  1 235 ? -0.819  -37.627 21.299 1.00 46.66  ? 1002 ASP   A CB  1 
ATOM   1637 C  CG  . ASP   A  1 235 ? -0.097  -36.629 22.182 1.00 62.32  ? 1002 ASP   A CG  1 
ATOM   1638 O  OD1 . ASP   A  1 235 ? 0.961   -36.114 21.765 1.00 76.41  ? 1002 ASP   A OD1 1 
ATOM   1639 O  OD2 . ASP   A  1 235 ? -0.571  -36.391 23.314 1.00 72.59  ? 1002 ASP   A OD2 1 
ATOM   1640 N  N   . LEU   A  1 236 ? -1.733  -38.956 18.520 1.00 50.92  ? 1003 LEU   A N   1 
ATOM   1641 C  CA  . LEU   A  1 236 ? -2.310  -40.090 17.799 1.00 44.69  ? 1003 LEU   A CA  1 
ATOM   1642 C  C   . LEU   A  1 236 ? -1.324  -40.698 16.805 1.00 55.06  ? 1003 LEU   A C   1 
ATOM   1643 O  O   . LEU   A  1 236 ? -1.133  -41.920 16.775 1.00 51.64  ? 1003 LEU   A O   1 
ATOM   1644 C  CB  . LEU   A  1 236 ? -3.585  -39.641 17.086 1.00 47.83  ? 1003 LEU   A CB  1 
ATOM   1645 C  CG  . LEU   A  1 236 ? -4.805  -39.365 17.975 1.00 59.21  ? 1003 LEU   A CG  1 
ATOM   1646 C  CD1 . LEU   A  1 236 ? -5.892  -38.654 17.175 1.00 61.50  ? 1003 LEU   A CD1 1 
ATOM   1647 C  CD2 . LEU   A  1 236 ? -5.346  -40.620 18.667 1.00 59.60  ? 1003 LEU   A CD2 1 
ATOM   1648 N  N   . GLU   A  1 237 ? -0.682  -39.862 15.986 1.00 48.79  ? 1004 GLU   A N   1 
ATOM   1649 C  CA  . GLU   A  1 237 ? 0.260   -40.391 15.004 1.00 62.79  ? 1004 GLU   A CA  1 
ATOM   1650 C  C   . GLU   A  1 237 ? 1.501   -40.948 15.684 1.00 68.06  ? 1004 GLU   A C   1 
ATOM   1651 O  O   . GLU   A  1 237 ? 2.083   -41.935 15.219 1.00 60.11  ? 1004 GLU   A O   1 
ATOM   1652 C  CB  . GLU   A  1 237 ? 0.635   -39.306 13.996 1.00 61.17  ? 1004 GLU   A CB  1 
ATOM   1653 N  N   . ASP   A  1 238 ? 1.907   -40.318 16.787 1.00 57.17  ? 1005 ASP   A N   1 
ATOM   1654 C  CA  . ASP   A  1 238 ? 3.049   -40.769 17.571 1.00 62.51  ? 1005 ASP   A CA  1 
ATOM   1655 C  C   . ASP   A  1 238 ? 2.769   -42.124 18.213 1.00 72.58  ? 1005 ASP   A C   1 
ATOM   1656 O  O   . ASP   A  1 238 ? 3.659   -42.978 18.291 1.00 67.86  ? 1005 ASP   A O   1 
ATOM   1657 C  CB  . ASP   A  1 238 ? 3.407   -39.697 18.602 1.00 64.08  ? 1005 ASP   A CB  1 
ATOM   1658 C  CG  . ASP   A  1 238 ? 4.156   -40.244 19.787 1.00 83.59  ? 1005 ASP   A CG  1 
ATOM   1659 O  OD1 . ASP   A  1 238 ? 3.526   -40.438 20.847 1.00 96.03  ? 1005 ASP   A OD1 1 
ATOM   1660 O  OD2 . ASP   A  1 238 ? 5.379   -40.463 19.663 1.00 105.04 ? 1005 ASP   A OD2 1 
ATOM   1661 N  N   . ASN   A  1 239 ? 1.544   -42.332 18.703 1.00 69.97  ? 1006 ASN   A N   1 
ATOM   1662 C  CA  . ASN   A  1 239 ? 1.191   -43.620 19.295 1.00 55.25  ? 1006 ASN   A CA  1 
ATOM   1663 C  C   . ASN   A  1 239 ? 1.133   -44.712 18.230 1.00 67.82  ? 1006 ASN   A C   1 
ATOM   1664 O  O   . ASN   A  1 239 ? 1.456   -45.873 18.508 1.00 49.44  ? 1006 ASN   A O   1 
ATOM   1665 C  CB  . ASN   A  1 239 ? -0.142  -43.503 20.031 1.00 56.91  ? 1006 ASN   A CB  1 
ATOM   1666 C  CG  . ASN   A  1 239 ? 0.035   -43.204 21.508 1.00 70.05  ? 1006 ASN   A CG  1 
ATOM   1667 O  OD1 . ASN   A  1 239 ? 0.496   -42.124 21.882 1.00 74.38  ? 1006 ASN   A OD1 1 
ATOM   1668 N  ND2 . ASN   A  1 239 ? -0.330  -44.159 22.354 1.00 75.02  ? 1006 ASN   A ND2 1 
ATOM   1669 N  N   . TRP   A  1 240 ? 0.723   -44.346 17.013 1.00 58.97  ? 1007 TRP   A N   1 
ATOM   1670 C  CA  . TRP   A  1 240 ? 0.737   -45.263 15.876 1.00 48.80  ? 1007 TRP   A CA  1 
ATOM   1671 C  C   . TRP   A  1 240 ? 2.156   -45.671 15.532 1.00 61.96  ? 1007 TRP   A C   1 
ATOM   1672 O  O   . TRP   A  1 240 ? 2.435   -46.851 15.287 1.00 55.48  ? 1007 TRP   A O   1 
ATOM   1673 C  CB  . TRP   A  1 240 ? 0.082   -44.588 14.671 1.00 42.21  ? 1007 TRP   A CB  1 
ATOM   1674 C  CG  . TRP   A  1 240 ? 0.066   -45.390 13.403 1.00 47.45  ? 1007 TRP   A CG  1 
ATOM   1675 C  CD1 . TRP   A  1 240 ? 0.803   -45.133 12.281 1.00 38.68  ? 1007 TRP   A CD1 1 
ATOM   1676 C  CD2 . TRP   A  1 240 ? -0.670  -46.587 13.130 1.00 50.43  ? 1007 TRP   A CD2 1 
ATOM   1677 N  NE1 . TRP   A  1 240 ? 0.547   -46.073 11.318 1.00 48.81  ? 1007 TRP   A NE1 1 
ATOM   1678 C  CE2 . TRP   A  1 240 ? -0.351  -46.980 11.814 1.00 58.94  ? 1007 TRP   A CE2 1 
ATOM   1679 C  CE3 . TRP   A  1 240 ? -1.571  -47.363 13.863 1.00 55.29  ? 1007 TRP   A CE3 1 
ATOM   1680 C  CZ2 . TRP   A  1 240 ? -0.902  -48.107 11.219 1.00 64.43  ? 1007 TRP   A CZ2 1 
ATOM   1681 C  CZ3 . TRP   A  1 240 ? -2.122  -48.474 13.268 1.00 60.64  ? 1007 TRP   A CZ3 1 
ATOM   1682 C  CH2 . TRP   A  1 240 ? -1.782  -48.838 11.961 1.00 61.07  ? 1007 TRP   A CH2 1 
ATOM   1683 N  N   . GLU   A  1 241 ? 3.060   -44.697 15.502 1.00 63.87  ? 1008 GLU   A N   1 
ATOM   1684 C  CA  . GLU   A  1 241 ? 4.454   -44.967 15.212 1.00 60.83  ? 1008 GLU   A CA  1 
ATOM   1685 C  C   . GLU   A  1 241 ? 5.091   -45.846 16.290 1.00 62.53  ? 1008 GLU   A C   1 
ATOM   1686 O  O   . GLU   A  1 241 ? 5.822   -46.791 15.970 1.00 54.18  ? 1008 GLU   A O   1 
ATOM   1687 C  CB  . GLU   A  1 241 ? 5.155   -43.601 15.090 1.00 69.96  ? 1008 GLU   A CB  1 
ATOM   1688 C  CG  . GLU   A  1 241 ? 5.949   -43.155 16.333 1.00 85.00  ? 1008 GLU   A CG  1 
ATOM   1689 C  CD  . GLU   A  1 241 ? 6.799   -41.924 16.126 1.00 99.86  ? 1008 GLU   A CD  1 
ATOM   1690 O  OE1 . GLU   A  1 241 ? 7.059   -41.574 14.960 1.00 101.68 ? 1008 GLU   A OE1 1 
ATOM   1691 O  OE2 . GLU   A  1 241 ? 7.205   -41.304 17.138 1.00 98.17  ? 1008 GLU   A OE2 1 
ATOM   1692 N  N   . THR   A  1 242 ? 4.825   -45.558 17.568 1.00 52.14  ? 1009 THR   A N   1 
ATOM   1693 C  CA  . THR   A  1 242 ? 5.363   -46.376 18.650 1.00 54.04  ? 1009 THR   A CA  1 
ATOM   1694 C  C   . THR   A  1 242 ? 4.909   -47.833 18.572 1.00 62.89  ? 1009 THR   A C   1 
ATOM   1695 O  O   . THR   A  1 242 ? 5.703   -48.754 18.806 1.00 55.48  ? 1009 THR   A O   1 
ATOM   1696 C  CB  . THR   A  1 242 ? 4.968   -45.759 19.995 1.00 54.50  ? 1009 THR   A CB  1 
ATOM   1697 O  OG1 . THR   A  1 242 ? 5.668   -44.519 20.184 1.00 73.72  ? 1009 THR   A OG1 1 
ATOM   1698 C  CG2 . THR   A  1 242 ? 5.281   -46.726 21.129 1.00 43.35  ? 1009 THR   A CG2 1 
ATOM   1699 N  N   . LEU   A  1 243 ? 3.635   -48.056 18.235 1.00 53.18  ? 1010 LEU   A N   1 
ATOM   1700 C  CA  . LEU   A  1 243 ? 3.107   -49.412 18.093 1.00 48.51  ? 1010 LEU   A CA  1 
ATOM   1701 C  C   . LEU   A  1 243 ? 3.851   -50.166 16.991 1.00 55.38  ? 1010 LEU   A C   1 
ATOM   1702 O  O   . LEU   A  1 243 ? 4.277   -51.312 17.185 1.00 44.63  ? 1010 LEU   A O   1 
ATOM   1703 C  CB  . LEU   A  1 243 ? 1.592   -49.367 17.844 1.00 45.48  ? 1010 LEU   A CB  1 
ATOM   1704 C  CG  . LEU   A  1 243 ? 0.769   -50.609 17.456 1.00 55.49  ? 1010 LEU   A CG  1 
ATOM   1705 C  CD1 . LEU   A  1 243 ? 0.676   -50.966 15.969 1.00 61.77  ? 1010 LEU   A CD1 1 
ATOM   1706 C  CD2 . LEU   A  1 243 ? 1.152   -51.801 18.340 1.00 51.64  ? 1010 LEU   A CD2 1 
ATOM   1707 N  N   . ASN   A  1 244 ? 4.003   -49.535 15.819 1.00 36.58  ? 1011 ASN   A N   1 
ATOM   1708 C  CA  . ASN   A  1 244 ? 4.604   -50.201 14.661 1.00 43.58  ? 1011 ASN   A CA  1 
ATOM   1709 C  C   . ASN   A  1 244 ? 6.106   -50.364 14.836 1.00 51.07  ? 1011 ASN   A C   1 
ATOM   1710 O  O   . ASN   A  1 244 ? 6.684   -51.359 14.383 1.00 59.26  ? 1011 ASN   A O   1 
ATOM   1711 C  CB  . ASN   A  1 244 ? 4.316   -49.433 13.369 1.00 40.38  ? 1011 ASN   A CB  1 
ATOM   1712 C  CG  . ASN   A  1 244 ? 2.868   -49.531 12.933 1.00 64.31  ? 1011 ASN   A CG  1 
ATOM   1713 O  OD1 . ASN   A  1 244 ? 2.234   -50.577 13.068 1.00 65.72  ? 1011 ASN   A OD1 1 
ATOM   1714 N  ND2 . ASN   A  1 244 ? 2.337   -48.435 12.401 1.00 61.11  ? 1011 ASN   A ND2 1 
ATOM   1715 N  N   . ASP   A  1 245 ? 6.758   -49.388 15.465 1.00 49.83  ? 1012 ASP   A N   1 
ATOM   1716 C  CA  . ASP   A  1 245 ? 8.179   -49.520 15.767 1.00 42.45  ? 1012 ASP   A CA  1 
ATOM   1717 C  C   . ASP   A  1 245 ? 8.406   -50.751 16.632 1.00 52.07  ? 1012 ASP   A C   1 
ATOM   1718 O  O   . ASP   A  1 245 ? 9.303   -51.559 16.365 1.00 50.31  ? 1012 ASP   A O   1 
ATOM   1719 C  CB  . ASP   A  1 245 ? 8.720   -48.265 16.453 1.00 43.90  ? 1012 ASP   A CB  1 
ATOM   1720 C  CG  . ASP   A  1 245 ? 8.752   -47.062 15.532 1.00 69.21  ? 1012 ASP   A CG  1 
ATOM   1721 O  OD1 . ASP   A  1 245 ? 8.776   -45.922 16.044 1.00 75.79  ? 1012 ASP   A OD1 1 
ATOM   1722 O  OD2 . ASP   A  1 245 ? 8.764   -47.257 14.300 1.00 70.38  ? 1012 ASP   A OD2 1 
ATOM   1723 N  N   . ASN   A  1 246 ? 7.607   -50.901 17.690 1.00 45.55  ? 1013 ASN   A N   1 
ATOM   1724 C  CA  . ASN   A  1 246 ? 7.824   -51.997 18.626 1.00 53.29  ? 1013 ASN   A CA  1 
ATOM   1725 C  C   . ASN   A  1 246 ? 7.558   -53.366 17.997 1.00 52.08  ? 1013 ASN   A C   1 
ATOM   1726 O  O   . ASN   A  1 246 ? 8.164   -54.352 18.426 1.00 50.31  ? 1013 ASN   A O   1 
ATOM   1727 C  CB  . ASN   A  1 246 ? 6.939   -51.803 19.858 1.00 46.56  ? 1013 ASN   A CB  1 
ATOM   1728 C  CG  . ASN   A  1 246 ? 7.595   -50.943 20.927 1.00 60.26  ? 1013 ASN   A CG  1 
ATOM   1729 O  OD1 . ASN   A  1 246 ? 8.812   -50.976 21.115 1.00 56.63  ? 1013 ASN   A OD1 1 
ATOM   1730 N  ND2 . ASN   A  1 246 ? 6.782   -50.175 21.644 1.00 58.58  ? 1013 ASN   A ND2 1 
ATOM   1731 N  N   . LEU   A  1 247 ? 6.662   -53.469 17.007 1.00 43.85  ? 1014 LEU   A N   1 
ATOM   1732 C  CA  . LEU   A  1 247 ? 6.544   -54.732 16.270 1.00 45.87  ? 1014 LEU   A CA  1 
ATOM   1733 C  C   . LEU   A  1 247 ? 7.844   -55.088 15.563 1.00 56.44  ? 1014 LEU   A C   1 
ATOM   1734 O  O   . LEU   A  1 247 ? 8.260   -56.252 15.572 1.00 54.85  ? 1014 LEU   A O   1 
ATOM   1735 C  CB  . LEU   A  1 247 ? 5.384   -54.696 15.280 1.00 51.02  ? 1014 LEU   A CB  1 
ATOM   1736 C  CG  . LEU   A  1 247 ? 4.001   -54.932 15.896 1.00 62.18  ? 1014 LEU   A CG  1 
ATOM   1737 C  CD1 . LEU   A  1 247 ? 2.901   -54.720 14.864 1.00 57.04  ? 1014 LEU   A CD1 1 
ATOM   1738 C  CD2 . LEU   A  1 247 ? 3.906   -56.344 16.523 1.00 66.16  ? 1014 LEU   A CD2 1 
ATOM   1739 N  N   . LYS   A  1 248 ? 8.501   -54.102 14.948 1.00 43.51  ? 1015 LYS   A N   1 
ATOM   1740 C  CA  . LYS   A  1 248 ? 9.781   -54.376 14.309 1.00 55.12  ? 1015 LYS   A CA  1 
ATOM   1741 C  C   . LYS   A  1 248 ? 10.809  -54.820 15.336 1.00 46.47  ? 1015 LYS   A C   1 
ATOM   1742 O  O   . LYS   A  1 248 ? 11.605  -55.726 15.072 1.00 54.11  ? 1015 LYS   A O   1 
ATOM   1743 C  CB  . LYS   A  1 248 ? 10.262  -53.161 13.517 1.00 45.10  ? 1015 LYS   A CB  1 
ATOM   1744 C  CG  . LYS   A  1 248 ? 9.342   -52.777 12.364 1.00 58.27  ? 1015 LYS   A CG  1 
ATOM   1745 C  CD  . LYS   A  1 248 ? 9.768   -51.480 11.693 1.00 72.29  ? 1015 LYS   A CD  1 
ATOM   1746 C  CE  . LYS   A  1 248 ? 8.844   -51.136 10.531 1.00 77.99  ? 1015 LYS   A CE  1 
ATOM   1747 N  NZ  . LYS   A  1 248 ? 8.244   -49.782 10.663 1.00 71.76  ? 1015 LYS   A NZ  1 
ATOM   1748 N  N   . VAL   A  1 249 ? 10.813  -54.185 16.508 1.00 43.20  ? 1016 VAL   A N   1 
ATOM   1749 C  CA  . VAL   A  1 249 ? 11.734  -54.592 17.563 1.00 51.29  ? 1016 VAL   A CA  1 
ATOM   1750 C  C   . VAL   A  1 249 ? 11.521  -56.062 17.916 1.00 60.21  ? 1016 VAL   A C   1 
ATOM   1751 O  O   . VAL   A  1 249 ? 12.485  -56.818 18.091 1.00 51.45  ? 1016 VAL   A O   1 
ATOM   1752 C  CB  . VAL   A  1 249 ? 11.565  -53.681 18.795 1.00 41.97  ? 1016 VAL   A CB  1 
ATOM   1753 C  CG1 . VAL   A  1 249 ? 12.335  -54.233 19.987 1.00 38.47  ? 1016 VAL   A CG1 1 
ATOM   1754 C  CG2 . VAL   A  1 249 ? 12.004  -52.262 18.472 1.00 50.27  ? 1016 VAL   A CG2 1 
ATOM   1755 N  N   . ILE   A  1 250 ? 10.258  -56.489 18.033 1.00 55.70  ? 1017 ILE   A N   1 
ATOM   1756 C  CA  . ILE   A  1 250 ? 9.974   -57.883 18.373 1.00 53.48  ? 1017 ILE   A CA  1 
ATOM   1757 C  C   . ILE   A  1 250 ? 10.453  -58.812 17.266 1.00 54.69  ? 1017 ILE   A C   1 
ATOM   1758 O  O   . ILE   A  1 250 ? 11.026  -59.878 17.529 1.00 54.30  ? 1017 ILE   A O   1 
ATOM   1759 C  CB  . ILE   A  1 250 ? 8.468   -58.060 18.646 1.00 45.37  ? 1017 ILE   A CB  1 
ATOM   1760 C  CG1 . ILE   A  1 250 ? 8.076   -57.318 19.926 1.00 44.97  ? 1017 ILE   A CG1 1 
ATOM   1761 C  CG2 . ILE   A  1 250 ? 8.098   -59.520 18.742 1.00 45.02  ? 1017 ILE   A CG2 1 
ATOM   1762 C  CD1 . ILE   A  1 250 ? 6.582   -57.176 20.120 1.00 46.33  ? 1017 ILE   A CD1 1 
ATOM   1763 N  N   . GLU   A  1 251 ? 10.221  -58.419 16.012 1.00 42.46  ? 1018 GLU   A N   1 
ATOM   1764 C  CA  . GLU   A  1 251 ? 10.585  -59.252 14.871 1.00 56.83  ? 1018 GLU   A CA  1 
ATOM   1765 C  C   . GLU   A  1 251 ? 12.087  -59.502 14.808 1.00 63.53  ? 1018 GLU   A C   1 
ATOM   1766 O  O   . GLU   A  1 251 ? 12.522  -60.616 14.501 1.00 67.33  ? 1018 GLU   A O   1 
ATOM   1767 C  CB  . GLU   A  1 251 ? 10.056  -58.618 13.584 1.00 53.95  ? 1018 GLU   A CB  1 
ATOM   1768 C  CG  . GLU   A  1 251 ? 8.546   -58.782 13.450 1.00 60.97  ? 1018 GLU   A CG  1 
ATOM   1769 C  CD  . GLU   A  1 251 ? 7.972   -58.016 12.279 1.00 77.17  ? 1018 GLU   A CD  1 
ATOM   1770 O  OE1 . GLU   A  1 251 ? 6.731   -58.031 12.136 1.00 78.87  ? 1018 GLU   A OE1 1 
ATOM   1771 O  OE2 . GLU   A  1 251 ? 8.744   -57.320 11.578 1.00 76.11  ? 1018 GLU   A OE2 1 
ATOM   1772 N  N   . LYS   A  1 252 ? 12.895  -58.476 15.074 1.00 58.90  ? 1019 LYS   A N   1 
ATOM   1773 C  CA  . LYS   A  1 252 ? 14.345  -58.592 14.988 1.00 59.80  ? 1019 LYS   A CA  1 
ATOM   1774 C  C   . LYS   A  1 252 ? 15.001  -58.717 16.361 1.00 56.18  ? 1019 LYS   A C   1 
ATOM   1775 O  O   . LYS   A  1 252 ? 16.211  -58.498 16.491 1.00 62.12  ? 1019 LYS   A O   1 
ATOM   1776 C  CB  . LYS   A  1 252 ? 14.898  -57.389 14.220 1.00 65.87  ? 1019 LYS   A CB  1 
ATOM   1777 C  CG  . LYS   A  1 252 ? 14.047  -57.080 12.994 1.00 63.65  ? 1019 LYS   A CG  1 
ATOM   1778 C  CD  . LYS   A  1 252 ? 14.524  -55.869 12.217 1.00 62.89  ? 1019 LYS   A CD  1 
ATOM   1779 C  CE  . LYS   A  1 252 ? 13.326  -55.089 11.682 1.00 85.47  ? 1019 LYS   A CE  1 
ATOM   1780 N  NZ  . LYS   A  1 252 ? 13.715  -53.898 10.876 1.00 82.27  ? 1019 LYS   A NZ  1 
ATOM   1781 N  N   . ALA   A  1 253 ? 14.224  -59.076 17.382 1.00 45.55  ? 1020 ALA   A N   1 
ATOM   1782 C  CA  . ALA   A  1 253 ? 14.759  -59.431 18.691 1.00 63.67  ? 1020 ALA   A CA  1 
ATOM   1783 C  C   . ALA   A  1 253 ? 15.503  -60.761 18.628 1.00 73.30  ? 1020 ALA   A C   1 
ATOM   1784 O  O   . ALA   A  1 253 ? 15.239  -61.602 17.766 1.00 60.21  ? 1020 ALA   A O   1 
ATOM   1785 C  CB  . ALA   A  1 253 ? 13.636  -59.509 19.723 1.00 52.28  ? 1020 ALA   A CB  1 
ATOM   1786 N  N   . ASP   A  1 254 ? 16.449  -60.954 19.554 1.00 69.52  ? 1021 ASP   A N   1 
ATOM   1787 C  CA  . ASP   A  1 254 ? 17.208  -62.199 19.584 1.00 79.55  ? 1021 ASP   A CA  1 
ATOM   1788 C  C   . ASP   A  1 254 ? 17.089  -62.997 20.880 1.00 72.53  ? 1021 ASP   A C   1 
ATOM   1789 O  O   . ASP   A  1 254 ? 17.699  -64.067 20.978 1.00 77.51  ? 1021 ASP   A O   1 
ATOM   1790 C  CB  . ASP   A  1 254 ? 18.691  -61.911 19.311 1.00 84.26  ? 1021 ASP   A CB  1 
ATOM   1791 N  N   . ASN   A  1 255 ? 16.341  -62.520 21.875 1.00 72.57  ? 1022 ASN   A N   1 
ATOM   1792 C  CA  . ASN   A  1 255 ? 16.055  -63.323 23.059 1.00 69.47  ? 1022 ASN   A CA  1 
ATOM   1793 C  C   . ASN   A  1 255 ? 14.654  -62.960 23.522 1.00 68.83  ? 1022 ASN   A C   1 
ATOM   1794 O  O   . ASN   A  1 255 ? 14.062  -61.975 23.072 1.00 65.22  ? 1022 ASN   A O   1 
ATOM   1795 C  CB  . ASN   A  1 255 ? 17.044  -63.141 24.223 1.00 58.60  ? 1022 ASN   A CB  1 
ATOM   1796 C  CG  . ASN   A  1 255 ? 17.118  -61.725 24.723 1.00 65.05  ? 1022 ASN   A CG  1 
ATOM   1797 O  OD1 . ASN   A  1 255 ? 17.173  -60.781 23.946 1.00 64.50  ? 1022 ASN   A OD1 1 
ATOM   1798 N  ND2 . ASN   A  1 255 ? 17.106  -61.568 26.044 1.00 79.28  ? 1022 ASN   A ND2 1 
ATOM   1799 N  N   . ALA   A  1 256 ? 14.122  -63.776 24.425 1.00 68.67  ? 1023 ALA   A N   1 
ATOM   1800 C  CA  . ALA   A  1 256 ? 12.758  -63.566 24.885 1.00 56.24  ? 1023 ALA   A CA  1 
ATOM   1801 C  C   . ALA   A  1 256 ? 12.633  -62.273 25.687 1.00 63.35  ? 1023 ALA   A C   1 
ATOM   1802 O  O   . ALA   A  1 256 ? 11.558  -61.663 25.705 1.00 68.12  ? 1023 ALA   A O   1 
ATOM   1803 C  CB  . ALA   A  1 256 ? 12.294  -64.761 25.715 1.00 56.54  ? 1023 ALA   A CB  1 
ATOM   1804 N  N   . ALA   A  1 257 ? 13.709  -61.840 26.354 1.00 63.92  ? 1024 ALA   A N   1 
ATOM   1805 C  CA  . ALA   A  1 257 ? 13.645  -60.626 27.168 1.00 57.95  ? 1024 ALA   A CA  1 
ATOM   1806 C  C   . ALA   A  1 257 ? 13.442  -59.374 26.317 1.00 62.03  ? 1024 ALA   A C   1 
ATOM   1807 O  O   . ALA   A  1 257 ? 12.761  -58.437 26.749 1.00 55.75  ? 1024 ALA   A O   1 
ATOM   1808 C  CB  . ALA   A  1 257 ? 14.901  -60.492 28.028 1.00 56.87  ? 1024 ALA   A CB  1 
ATOM   1809 N  N   . GLN   A  1 258 ? 14.029  -59.324 25.116 1.00 59.67  ? 1025 GLN   A N   1 
ATOM   1810 C  CA  . GLN   A  1 258 ? 13.793  -58.169 24.250 1.00 56.59  ? 1025 GLN   A CA  1 
ATOM   1811 C  C   . GLN   A  1 258 ? 12.340  -58.124 23.803 1.00 56.77  ? 1025 GLN   A C   1 
ATOM   1812 O  O   . GLN   A  1 258 ? 11.733  -57.048 23.745 1.00 55.12  ? 1025 GLN   A O   1 
ATOM   1813 C  CB  . GLN   A  1 258 ? 14.711  -58.185 23.027 1.00 47.88  ? 1025 GLN   A CB  1 
ATOM   1814 C  CG  . GLN   A  1 258 ? 16.186  -57.987 23.303 1.00 66.93  ? 1025 GLN   A CG  1 
ATOM   1815 C  CD  . GLN   A  1 258 ? 17.025  -58.160 22.049 1.00 58.90  ? 1025 GLN   A CD  1 
ATOM   1816 O  OE1 . GLN   A  1 258 ? 16.936  -57.363 21.114 1.00 77.46  ? 1025 GLN   A OE1 1 
ATOM   1817 N  NE2 . GLN   A  1 258 ? 17.837  -59.209 22.020 1.00 78.36  ? 1025 GLN   A NE2 1 
ATOM   1818 N  N   . VAL   A  1 259 ? 11.776  -59.285 23.468 1.00 57.58  ? 1026 VAL   A N   1 
ATOM   1819 C  CA  . VAL   A  1 259 ? 10.358  -59.361 23.133 1.00 55.47  ? 1026 VAL   A CA  1 
ATOM   1820 C  C   . VAL   A  1 259 ? 9.516   -58.876 24.307 1.00 50.15  ? 1026 VAL   A C   1 
ATOM   1821 O  O   . VAL   A  1 259 ? 8.543   -58.134 24.126 1.00 56.41  ? 1026 VAL   A O   1 
ATOM   1822 C  CB  . VAL   A  1 259 ? 9.993   -60.797 22.712 1.00 46.80  ? 1026 VAL   A CB  1 
ATOM   1823 C  CG1 . VAL   A  1 259 ? 8.513   -60.912 22.428 1.00 42.20  ? 1026 VAL   A CG1 1 
ATOM   1824 C  CG2 . VAL   A  1 259 ? 10.804  -61.208 21.494 1.00 43.96  ? 1026 VAL   A CG2 1 
ATOM   1825 N  N   . LYS   A  1 260 ? 9.873   -59.290 25.527 1.00 48.87  ? 1027 LYS   A N   1 
ATOM   1826 C  CA  . LYS   A  1 260 ? 9.111   -58.879 26.703 1.00 49.71  ? 1027 LYS   A CA  1 
ATOM   1827 C  C   . LYS   A  1 260 ? 9.134   -57.365 26.867 1.00 59.16  ? 1027 LYS   A C   1 
ATOM   1828 O  O   . LYS   A  1 260 ? 8.098   -56.741 27.125 1.00 59.50  ? 1027 LYS   A O   1 
ATOM   1829 C  CB  . LYS   A  1 260 ? 9.681   -59.546 27.955 1.00 52.21  ? 1027 LYS   A CB  1 
ATOM   1830 C  CG  . LYS   A  1 260 ? 9.099   -59.005 29.255 1.00 54.15  ? 1027 LYS   A CG  1 
ATOM   1831 C  CD  . LYS   A  1 260 ? 9.671   -59.719 30.467 1.00 55.74  ? 1027 LYS   A CD  1 
ATOM   1832 C  CE  . LYS   A  1 260 ? 8.937   -59.323 31.739 1.00 53.38  ? 1027 LYS   A CE  1 
ATOM   1833 N  NZ  . LYS   A  1 260 ? 9.422   -60.090 32.920 1.00 67.38  ? 1027 LYS   A NZ  1 
ATOM   1834 N  N   . ASP   A  1 261 ? 10.319  -56.761 26.743 1.00 63.74  ? 1028 ASP   A N   1 
ATOM   1835 C  CA  . ASP   A  1 261 ? 10.445  -55.315 26.892 1.00 52.68  ? 1028 ASP   A CA  1 
ATOM   1836 C  C   . ASP   A  1 261 ? 9.511   -54.577 25.940 1.00 51.76  ? 1028 ASP   A C   1 
ATOM   1837 O  O   . ASP   A  1 261 ? 8.777   -53.669 26.350 1.00 56.37  ? 1028 ASP   A O   1 
ATOM   1838 C  CB  . ASP   A  1 261 ? 11.896  -54.890 26.662 1.00 53.56  ? 1028 ASP   A CB  1 
ATOM   1839 N  N   . ALA   A  1 262 ? 9.526   -54.953 24.657 1.00 42.06  ? 1029 ALA   A N   1 
ATOM   1840 C  CA  . ALA   A  1 262 ? 8.706   -54.247 23.678 1.00 52.67  ? 1029 ALA   A CA  1 
ATOM   1841 C  C   . ALA   A  1 262 ? 7.220   -54.504 23.901 1.00 47.78  ? 1029 ALA   A C   1 
ATOM   1842 O  O   . ALA   A  1 262 ? 6.396   -53.604 23.704 1.00 51.28  ? 1029 ALA   A O   1 
ATOM   1843 C  CB  . ALA   A  1 262 ? 9.115   -54.651 22.263 1.00 41.46  ? 1029 ALA   A CB  1 
ATOM   1844 N  N   . LEU   A  1 263 ? 6.856   -55.723 24.307 1.00 41.28  ? 1030 LEU   A N   1 
ATOM   1845 C  CA  . LEU   A  1 263 ? 5.443   -56.024 24.517 1.00 52.77  ? 1030 LEU   A CA  1 
ATOM   1846 C  C   . LEU   A  1 263 ? 4.901   -55.269 25.722 1.00 39.29  ? 1030 LEU   A C   1 
ATOM   1847 O  O   . LEU   A  1 263 ? 3.745   -54.828 25.720 1.00 41.29  ? 1030 LEU   A O   1 
ATOM   1848 C  CB  . LEU   A  1 263 ? 5.224   -57.525 24.688 1.00 38.97  ? 1030 LEU   A CB  1 
ATOM   1849 C  CG  . LEU   A  1 263 ? 5.328   -58.412 23.450 1.00 45.76  ? 1030 LEU   A CG  1 
ATOM   1850 C  CD1 . LEU   A  1 263 ? 5.521   -59.851 23.879 1.00 37.48  ? 1030 LEU   A CD1 1 
ATOM   1851 C  CD2 . LEU   A  1 263 ? 4.095   -58.267 22.572 1.00 37.29  ? 1030 LEU   A CD2 1 
ATOM   1852 N  N   . THR   A  1 264 ? 5.721   -55.128 26.766 1.00 41.75  ? 1031 THR   A N   1 
ATOM   1853 C  CA  . THR   A  1 264 ? 5.322   -54.341 27.926 1.00 51.43  ? 1031 THR   A CA  1 
ATOM   1854 C  C   . THR   A  1 264 ? 5.033   -52.898 27.531 1.00 54.52  ? 1031 THR   A C   1 
ATOM   1855 O  O   . THR   A  1 264 ? 4.078   -52.289 28.029 1.00 49.52  ? 1031 THR   A O   1 
ATOM   1856 C  CB  . THR   A  1 264 ? 6.414   -54.403 28.996 1.00 54.04  ? 1031 THR   A CB  1 
ATOM   1857 O  OG1 . THR   A  1 264 ? 6.578   -55.757 29.434 1.00 50.95  ? 1031 THR   A OG1 1 
ATOM   1858 C  CG2 . THR   A  1 264 ? 6.051   -53.533 30.190 1.00 51.74  ? 1031 THR   A CG2 1 
ATOM   1859 N  N   . LYS   A  1 265 ? 5.839   -52.339 26.624 1.00 41.89  ? 1032 LYS   A N   1 
ATOM   1860 C  CA  . LYS   A  1 265 ? 5.585   -50.986 26.147 1.00 49.73  ? 1032 LYS   A CA  1 
ATOM   1861 C  C   . LYS   A  1 265 ? 4.349   -50.936 25.259 1.00 58.67  ? 1032 LYS   A C   1 
ATOM   1862 O  O   . LYS   A  1 265 ? 3.628   -49.933 25.254 1.00 65.99  ? 1032 LYS   A O   1 
ATOM   1863 C  CB  . LYS   A  1 265 ? 6.788   -50.474 25.356 1.00 55.88  ? 1032 LYS   A CB  1 
ATOM   1864 C  CG  . LYS   A  1 265 ? 8.032   -50.192 26.173 1.00 51.35  ? 1032 LYS   A CG  1 
ATOM   1865 C  CD  . LYS   A  1 265 ? 9.173   -49.787 25.250 1.00 57.98  ? 1032 LYS   A CD  1 
ATOM   1866 C  CE  . LYS   A  1 265 ? 10.385  -49.293 26.019 1.00 67.37  ? 1032 LYS   A CE  1 
ATOM   1867 N  NZ  . LYS   A  1 265 ? 11.495  -48.924 25.094 1.00 80.26  ? 1032 LYS   A NZ  1 
ATOM   1868 N  N   . MET   A  1 266 ? 4.094   -52.008 24.505 1.00 54.18  ? 1033 MET   A N   1 
ATOM   1869 C  CA  . MET   A  1 266 ? 2.894   -52.084 23.686 1.00 53.47  ? 1033 MET   A CA  1 
ATOM   1870 C  C   . MET   A  1 266 ? 1.646   -52.204 24.556 1.00 47.98  ? 1033 MET   A C   1 
ATOM   1871 O  O   . MET   A  1 266 ? 0.603   -51.614 24.243 1.00 50.44  ? 1033 MET   A O   1 
ATOM   1872 C  CB  . MET   A  1 266 ? 3.038   -53.259 22.715 1.00 53.11  ? 1033 MET   A CB  1 
ATOM   1873 C  CG  . MET   A  1 266 ? 4.018   -52.945 21.573 1.00 53.40  ? 1033 MET   A CG  1 
ATOM   1874 S  SD  . MET   A  1 266 ? 4.390   -54.278 20.416 1.00 68.33  ? 1033 MET   A SD  1 
ATOM   1875 C  CE  . MET   A  1 266 ? 2.830   -54.464 19.590 1.00 57.82  ? 1033 MET   A CE  1 
ATOM   1876 N  N   . ARG   A  1 267 ? 1.726   -52.970 25.652 1.00 44.60  ? 1034 ARG   A N   1 
ATOM   1877 C  CA  . ARG   A  1 267 ? 0.542   -53.214 26.478 1.00 53.25  ? 1034 ARG   A CA  1 
ATOM   1878 C  C   . ARG   A  1 267 ? 0.097   -51.954 27.212 1.00 60.89  ? 1034 ARG   A C   1 
ATOM   1879 O  O   . ARG   A  1 267 ? -1.095  -51.630 27.243 1.00 60.05  ? 1034 ARG   A O   1 
ATOM   1880 C  CB  . ARG   A  1 267 ? 0.825   -54.333 27.481 1.00 36.21  ? 1034 ARG   A CB  1 
ATOM   1881 C  CG  . ARG   A  1 267 ? -0.429  -54.877 28.143 1.00 36.46  ? 1034 ARG   A CG  1 
ATOM   1882 C  CD  . ARG   A  1 267 ? -0.105  -55.856 29.258 1.00 44.94  ? 1034 ARG   A CD  1 
ATOM   1883 N  NE  . ARG   A  1 267 ? -1.298  -56.550 29.728 1.00 64.72  ? 1034 ARG   A NE  1 
ATOM   1884 C  CZ  . ARG   A  1 267 ? -2.154  -56.053 30.611 1.00 68.49  ? 1034 ARG   A CZ  1 
ATOM   1885 N  NH1 . ARG   A  1 267 ? -1.980  -54.855 31.142 1.00 79.25  ? 1034 ARG   A NH1 1 
ATOM   1886 N  NH2 . ARG   A  1 267 ? -3.212  -56.776 30.968 1.00 67.21  ? 1034 ARG   A NH2 1 
ATOM   1887 N  N   . ALA   A  1 268 ? 1.048   -51.233 27.818 1.00 55.50  ? 1035 ALA   A N   1 
ATOM   1888 C  CA  . ALA   A  1 268 ? 0.718   -49.971 28.475 1.00 62.39  ? 1035 ALA   A CA  1 
ATOM   1889 C  C   . ALA   A  1 268 ? 0.187   -48.933 27.499 1.00 47.89  ? 1035 ALA   A C   1 
ATOM   1890 O  O   . ALA   A  1 268 ? -0.686  -48.137 27.860 1.00 56.64  ? 1035 ALA   A O   1 
ATOM   1891 C  CB  . ALA   A  1 268 ? 1.946   -49.429 29.208 1.00 50.51  ? 1035 ALA   A CB  1 
ATOM   1892 N  N   . ALA   A  1 269 ? 0.689   -48.925 26.263 1.00 50.95  ? 1036 ALA   A N   1 
ATOM   1893 C  CA  . ALA   A  1 269 ? 0.180   -47.974 25.280 1.00 50.14  ? 1036 ALA   A CA  1 
ATOM   1894 C  C   . ALA   A  1 269 ? -1.214  -48.368 24.813 1.00 69.18  ? 1036 ALA   A C   1 
ATOM   1895 O  O   . ALA   A  1 269 ? -2.067  -47.503 24.583 1.00 74.53  ? 1036 ALA   A O   1 
ATOM   1896 C  CB  . ALA   A  1 269 ? 1.138   -47.874 24.094 1.00 44.25  ? 1036 ALA   A CB  1 
ATOM   1897 N  N   . ALA   A  1 270 ? -1.458  -49.672 24.664 1.00 56.18  ? 1037 ALA   A N   1 
ATOM   1898 C  CA  . ALA   A  1 270 ? -2.767  -50.139 24.227 1.00 51.99  ? 1037 ALA   A CA  1 
ATOM   1899 C  C   . ALA   A  1 270 ? -3.848  -49.756 25.228 1.00 54.19  ? 1037 ALA   A C   1 
ATOM   1900 O  O   . ALA   A  1 270 ? -4.923  -49.279 24.845 1.00 63.30  ? 1037 ALA   A O   1 
ATOM   1901 C  CB  . ALA   A  1 270 ? -2.740  -51.653 24.012 1.00 50.04  ? 1037 ALA   A CB  1 
ATOM   1902 N  N   . LEU   A  1 271 ? -3.588  -49.967 26.522 1.00 60.86  ? 1038 LEU   A N   1 
ATOM   1903 C  CA  . LEU   A  1 271 ? -4.555  -49.532 27.522 1.00 70.56  ? 1038 LEU   A CA  1 
ATOM   1904 C  C   . LEU   A  1 271 ? -4.688  -48.013 27.546 1.00 76.61  ? 1038 LEU   A C   1 
ATOM   1905 O  O   . LEU   A  1 271 ? -5.777  -47.490 27.809 1.00 85.00  ? 1038 LEU   A O   1 
ATOM   1906 C  CB  . LEU   A  1 271 ? -4.119  -50.031 28.901 1.00 65.90  ? 1038 LEU   A CB  1 
ATOM   1907 C  CG  . LEU   A  1 271 ? -3.845  -51.527 29.085 1.00 65.60  ? 1038 LEU   A CG  1 
ATOM   1908 C  CD1 . LEU   A  1 271 ? -3.542  -51.845 30.544 1.00 77.15  ? 1038 LEU   A CD1 1 
ATOM   1909 C  CD2 . LEU   A  1 271 ? -5.004  -52.369 28.582 1.00 78.77  ? 1038 LEU   A CD2 1 
ATOM   1910 N  N   . ASP   A  1 272 ? -3.591  -47.297 27.280 1.00 77.88  ? 1039 ASP   A N   1 
ATOM   1911 C  CA  . ASP   A  1 272 ? -3.622  -45.837 27.237 1.00 80.84  ? 1039 ASP   A CA  1 
ATOM   1912 C  C   . ASP   A  1 272 ? -4.391  -45.317 26.029 1.00 81.98  ? 1039 ASP   A C   1 
ATOM   1913 O  O   . ASP   A  1 272 ? -5.079  -44.293 26.113 1.00 89.68  ? 1039 ASP   A O   1 
ATOM   1914 C  CB  . ASP   A  1 272 ? -2.201  -45.277 27.245 1.00 68.96  ? 1039 ASP   A CB  1 
ATOM   1915 C  CG  . ASP   A  1 272 ? -2.158  -43.818 27.652 1.00 90.23  ? 1039 ASP   A CG  1 
ATOM   1916 O  OD1 . ASP   A  1 272 ? -2.130  -42.950 26.754 1.00 104.70 ? 1039 ASP   A OD1 1 
ATOM   1917 O  OD2 . ASP   A  1 272 ? -2.163  -43.539 28.869 1.00 91.02  ? 1039 ASP   A OD2 1 
ATOM   1918 N  N   . ALA   A  1 273 ? -4.287  -46.018 24.899 1.00 78.53  ? 1040 ALA   A N   1 
ATOM   1919 C  CA  . ALA   A  1 273 ? -5.026  -45.682 23.688 1.00 82.77  ? 1040 ALA   A CA  1 
ATOM   1920 C  C   . ALA   A  1 273 ? -6.484  -46.109 23.723 1.00 86.22  ? 1040 ALA   A C   1 
ATOM   1921 O  O   . ALA   A  1 273 ? -7.271  -45.624 22.903 1.00 78.71  ? 1040 ALA   A O   1 
ATOM   1922 C  CB  . ALA   A  1 273 ? -4.344  -46.309 22.470 1.00 72.69  ? 1040 ALA   A CB  1 
ATOM   1923 N  N   . GLN   A  1 274 ? -6.870  -46.997 24.637 1.00 83.71  ? 1041 GLN   A N   1 
ATOM   1924 C  CA  . GLN   A  1 274 ? -8.277  -47.363 24.708 1.00 85.81  ? 1041 GLN   A CA  1 
ATOM   1925 C  C   . GLN   A  1 274 ? -9.109  -46.301 25.415 1.00 98.61  ? 1041 GLN   A C   1 
ATOM   1926 O  O   . GLN   A  1 274 ? -10.296 -46.146 25.106 1.00 104.80 ? 1041 GLN   A O   1 
ATOM   1927 C  CB  . GLN   A  1 274 ? -8.392  -48.693 25.452 1.00 70.01  ? 1041 GLN   A CB  1 
ATOM   1928 C  CG  . GLN   A  1 274 ? -9.727  -49.393 25.401 1.00 80.13  ? 1041 GLN   A CG  1 
ATOM   1929 C  CD  . GLN   A  1 274 ? -9.648  -50.764 26.047 1.00 88.56  ? 1041 GLN   A CD  1 
ATOM   1930 O  OE1 . GLN   A  1 274 ? -8.749  -51.029 26.847 1.00 79.37  ? 1041 GLN   A OE1 1 
ATOM   1931 N  NE2 . GLN   A  1 274 ? -10.583 -51.640 25.704 1.00 88.12  ? 1041 GLN   A NE2 1 
ATOM   1932 N  N   . LYS   A  1 275 ? -8.514  -45.569 26.351 1.00 89.11  ? 1042 LYS   A N   1 
ATOM   1933 C  CA  . LYS   A  1 275 ? -9.197  -44.489 27.061 1.00 77.15  ? 1042 LYS   A CA  1 
ATOM   1934 C  C   . LYS   A  1 275 ? -9.550  -43.301 26.162 1.00 91.69  ? 1042 LYS   A C   1 
ATOM   1935 O  O   . LYS   A  1 275 ? -10.347 -43.416 25.231 1.00 95.57  ? 1042 LYS   A O   1 
ATOM   1936 C  CB  . LYS   A  1 275 ? -8.367  -44.060 28.269 1.00 80.55  ? 1042 LYS   A CB  1 
ATOM   1937 C  CG  . LYS   A  1 275 ? -8.296  -45.182 29.298 1.00 81.45  ? 1042 LYS   A CG  1 
ATOM   1938 C  CD  . LYS   A  1 275 ? -7.543  -44.811 30.556 1.00 83.37  ? 1042 LYS   A CD  1 
ATOM   1939 C  CE  . LYS   A  1 275 ? -6.205  -45.525 30.594 1.00 97.57  ? 1042 LYS   A CE  1 
ATOM   1940 N  NZ  . LYS   A  1 275 ? -6.386  -46.982 30.865 1.00 91.87  ? 1042 LYS   A NZ  1 
ATOM   1941 N  N   . MET   A  1 291 ? -18.411 -48.274 18.182 1.00 75.85  ? 1058 MET   A N   1 
ATOM   1942 C  CA  . MET   A  1 291 ? -17.795 -48.301 19.503 1.00 88.34  ? 1058 MET   A CA  1 
ATOM   1943 C  C   . MET   A  1 291 ? -17.661 -49.732 20.016 1.00 90.82  ? 1058 MET   A C   1 
ATOM   1944 O  O   . MET   A  1 291 ? -16.767 -50.037 20.806 1.00 86.66  ? 1058 MET   A O   1 
ATOM   1945 C  CB  . MET   A  1 291 ? -18.608 -47.459 20.489 1.00 84.53  ? 1058 MET   A CB  1 
ATOM   1946 N  N   . LYS   A  1 292 ? -18.559 -50.610 19.562 1.00 92.25  ? 1059 LYS   A N   1 
ATOM   1947 C  CA  . LYS   A  1 292 ? -18.496 -52.010 19.969 1.00 93.05  ? 1059 LYS   A CA  1 
ATOM   1948 C  C   . LYS   A  1 292 ? -17.345 -52.729 19.275 1.00 85.41  ? 1059 LYS   A C   1 
ATOM   1949 O  O   . LYS   A  1 292 ? -16.617 -53.504 19.906 1.00 82.39  ? 1059 LYS   A O   1 
ATOM   1950 C  CB  . LYS   A  1 292 ? -19.824 -52.705 19.672 1.00 86.30  ? 1059 LYS   A CB  1 
ATOM   1951 N  N   . ASP   A  1 293 ? -17.167 -52.480 17.976 1.00 77.35  ? 1060 ASP   A N   1 
ATOM   1952 C  CA  . ASP   A  1 293 ? -16.010 -53.003 17.259 1.00 83.90  ? 1060 ASP   A CA  1 
ATOM   1953 C  C   . ASP   A  1 293 ? -14.731 -52.277 17.656 1.00 80.25  ? 1060 ASP   A C   1 
ATOM   1954 O  O   . ASP   A  1 293 ? -13.642 -52.855 17.571 1.00 86.57  ? 1060 ASP   A O   1 
ATOM   1955 C  CB  . ASP   A  1 293 ? -16.240 -52.924 15.750 1.00 73.07  ? 1060 ASP   A CB  1 
ATOM   1956 C  CG  . ASP   A  1 293 ? -17.682 -53.198 15.369 1.00 101.18 ? 1060 ASP   A CG  1 
ATOM   1957 O  OD1 . ASP   A  1 293 ? -18.254 -54.182 15.884 1.00 101.16 ? 1060 ASP   A OD1 1 
ATOM   1958 O  OD2 . ASP   A  1 293 ? -18.240 -52.437 14.553 1.00 111.50 ? 1060 ASP   A OD2 1 
ATOM   1959 N  N   . PHE   A  1 294 ? -14.839 -51.015 18.080 1.00 82.12  ? 1061 PHE   A N   1 
ATOM   1960 C  CA  . PHE   A  1 294 ? -13.696 -50.351 18.699 1.00 73.32  ? 1061 PHE   A CA  1 
ATOM   1961 C  C   . PHE   A  1 294 ? -13.276 -51.101 19.956 1.00 75.38  ? 1061 PHE   A C   1 
ATOM   1962 O  O   . PHE   A  1 294 ? -12.098 -51.438 20.128 1.00 76.55  ? 1061 PHE   A O   1 
ATOM   1963 C  CB  . PHE   A  1 294 ? -14.049 -48.890 19.007 1.00 82.55  ? 1061 PHE   A CB  1 
ATOM   1964 C  CG  . PHE   A  1 294 ? -13.183 -48.245 20.066 1.00 89.67  ? 1061 PHE   A CG  1 
ATOM   1965 C  CD1 . PHE   A  1 294 ? -13.487 -48.361 21.417 1.00 79.68  ? 1061 PHE   A CD1 1 
ATOM   1966 C  CD2 . PHE   A  1 294 ? -12.078 -47.492 19.702 1.00 82.27  ? 1061 PHE   A CD2 1 
ATOM   1967 C  CE1 . PHE   A  1 294 ? -12.692 -47.762 22.377 1.00 90.00  ? 1061 PHE   A CE1 1 
ATOM   1968 C  CE2 . PHE   A  1 294 ? -11.286 -46.885 20.659 1.00 88.53  ? 1061 PHE   A CE2 1 
ATOM   1969 C  CZ  . PHE   A  1 294 ? -11.591 -47.023 21.997 1.00 88.86  ? 1061 PHE   A CZ  1 
ATOM   1970 N  N   . ARG   A  1 295 ? -14.229 -51.364 20.855 1.00 77.93  ? 1062 ARG   A N   1 
ATOM   1971 C  CA  . ARG   A  1 295 ? -13.897 -52.061 22.092 1.00 73.57  ? 1062 ARG   A CA  1 
ATOM   1972 C  C   . ARG   A  1 295 ? -13.426 -53.478 21.791 1.00 68.29  ? 1062 ARG   A C   1 
ATOM   1973 O  O   . ARG   A  1 295 ? -12.504 -53.988 22.439 1.00 59.59  ? 1062 ARG   A O   1 
ATOM   1974 C  CB  . ARG   A  1 295 ? -15.104 -52.078 23.030 1.00 72.25  ? 1062 ARG   A CB  1 
ATOM   1975 N  N   . HIS   A  1 296 ? -14.063 -54.132 20.815 1.00 55.81  ? 1063 HIS   A N   1 
ATOM   1976 C  CA  . HIS   A  1 296 ? -13.658 -55.479 20.425 1.00 68.97  ? 1063 HIS   A CA  1 
ATOM   1977 C  C   . HIS   A  1 296 ? -12.230 -55.489 19.899 1.00 64.05  ? 1063 HIS   A C   1 
ATOM   1978 O  O   . HIS   A  1 296 ? -11.433 -56.363 20.259 1.00 65.58  ? 1063 HIS   A O   1 
ATOM   1979 C  CB  . HIS   A  1 296 ? -14.618 -56.021 19.366 1.00 62.50  ? 1063 HIS   A CB  1 
ATOM   1980 C  CG  . HIS   A  1 296 ? -14.453 -57.482 19.087 1.00 62.91  ? 1063 HIS   A CG  1 
ATOM   1981 N  ND1 . HIS   A  1 296 ? -14.499 -58.440 20.077 1.00 60.59  ? 1063 HIS   A ND1 1 
ATOM   1982 C  CD2 . HIS   A  1 296 ? -14.237 -58.148 17.928 1.00 63.18  ? 1063 HIS   A CD2 1 
ATOM   1983 C  CE1 . HIS   A  1 296 ? -14.322 -59.634 19.539 1.00 54.71  ? 1063 HIS   A CE1 1 
ATOM   1984 N  NE2 . HIS   A  1 296 ? -14.160 -59.485 18.237 1.00 56.25  ? 1063 HIS   A NE2 1 
ATOM   1985 N  N   . GLY   A  1 297 ? -11.893 -54.520 19.044 1.00 51.21  ? 1064 GLY   A N   1 
ATOM   1986 C  CA  . GLY   A  1 297 ? -10.548 -54.447 18.498 1.00 46.71  ? 1064 GLY   A CA  1 
ATOM   1987 C  C   . GLY   A  1 297 ? -9.481  -54.329 19.568 1.00 48.88  ? 1064 GLY   A C   1 
ATOM   1988 O  O   . GLY   A  1 297 ? -8.450  -55.003 19.509 1.00 43.65  ? 1064 GLY   A O   1 
ATOM   1989 N  N   . PHE   A  1 298 ? -9.711  -53.469 20.561 1.00 48.21  ? 1065 PHE   A N   1 
ATOM   1990 C  CA  . PHE   A  1 298 ? -8.735  -53.318 21.633 1.00 55.59  ? 1065 PHE   A CA  1 
ATOM   1991 C  C   . PHE   A  1 298 ? -8.729  -54.524 22.565 1.00 64.53  ? 1065 PHE   A C   1 
ATOM   1992 O  O   . PHE   A  1 298 ? -7.688  -54.839 23.153 1.00 58.26  ? 1065 PHE   A O   1 
ATOM   1993 C  CB  . PHE   A  1 298 ? -9.019  -52.029 22.400 1.00 60.43  ? 1065 PHE   A CB  1 
ATOM   1994 C  CG  . PHE   A  1 298 ? -8.436  -50.809 21.750 1.00 64.18  ? 1065 PHE   A CG  1 
ATOM   1995 C  CD1 . PHE   A  1 298 ? -7.093  -50.503 21.887 1.00 56.69  ? 1065 PHE   A CD1 1 
ATOM   1996 C  CD2 . PHE   A  1 298 ? -9.225  -49.996 20.955 1.00 68.22  ? 1065 PHE   A CD2 1 
ATOM   1997 C  CE1 . PHE   A  1 298 ? -6.558  -49.386 21.273 1.00 65.31  ? 1065 PHE   A CE1 1 
ATOM   1998 C  CE2 . PHE   A  1 298 ? -8.694  -48.885 20.335 1.00 67.31  ? 1065 PHE   A CE2 1 
ATOM   1999 C  CZ  . PHE   A  1 298 ? -7.361  -48.578 20.495 1.00 54.97  ? 1065 PHE   A CZ  1 
ATOM   2000 N  N   . ASP   A  1 299 ? -9.868  -55.203 22.724 1.00 54.52  ? 1066 ASP   A N   1 
ATOM   2001 C  CA  . ASP   A  1 299 ? -9.878  -56.426 23.522 1.00 51.94  ? 1066 ASP   A CA  1 
ATOM   2002 C  C   . ASP   A  1 299 ? -9.013  -57.500 22.874 1.00 45.70  ? 1066 ASP   A C   1 
ATOM   2003 O  O   . ASP   A  1 299 ? -8.250  -58.192 23.560 1.00 58.31  ? 1066 ASP   A O   1 
ATOM   2004 C  CB  . ASP   A  1 299 ? -11.309 -56.924 23.720 1.00 65.24  ? 1066 ASP   A CB  1 
ATOM   2005 C  CG  . ASP   A  1 299 ? -12.040 -56.178 24.821 1.00 73.25  ? 1066 ASP   A CG  1 
ATOM   2006 O  OD1 . ASP   A  1 299 ? -11.370 -55.654 25.737 1.00 83.91  ? 1066 ASP   A OD1 1 
ATOM   2007 O  OD2 . ASP   A  1 299 ? -13.286 -56.112 24.768 1.00 84.09  ? 1066 ASP   A OD2 1 
ATOM   2008 N  N   . ILE   A  1 300 ? -9.135  -57.665 21.554 1.00 39.34  ? 1067 ILE   A N   1 
ATOM   2009 C  CA  . ILE   A  1 300 ? -8.249  -58.571 20.827 1.00 44.55  ? 1067 ILE   A CA  1 
ATOM   2010 C  C   . ILE   A  1 300 ? -6.799  -58.136 20.986 1.00 48.27  ? 1067 ILE   A C   1 
ATOM   2011 O  O   . ILE   A  1 300 ? -5.911  -58.957 21.244 1.00 46.38  ? 1067 ILE   A O   1 
ATOM   2012 C  CB  . ILE   A  1 300 ? -8.653  -58.650 19.343 1.00 36.21  ? 1067 ILE   A CB  1 
ATOM   2013 C  CG1 . ILE   A  1 300 ? -10.138 -58.993 19.205 1.00 54.47  ? 1067 ILE   A CG1 1 
ATOM   2014 C  CG2 . ILE   A  1 300 ? -7.784  -59.656 18.604 1.00 40.10  ? 1067 ILE   A CG2 1 
ATOM   2015 C  CD1 . ILE   A  1 300 ? -10.698 -58.738 17.824 1.00 48.03  ? 1067 ILE   A CD1 1 
ATOM   2016 N  N   . LEU   A  1 301 ? -6.537  -56.835 20.828 1.00 44.79  ? 1068 LEU   A N   1 
ATOM   2017 C  CA  . LEU   A  1 301 ? -5.162  -56.345 20.826 1.00 39.57  ? 1068 LEU   A CA  1 
ATOM   2018 C  C   . LEU   A  1 301 ? -4.481  -56.609 22.162 1.00 36.31  ? 1068 LEU   A C   1 
ATOM   2019 O  O   . LEU   A  1 301 ? -3.376  -57.161 22.212 1.00 40.53  ? 1068 LEU   A O   1 
ATOM   2020 C  CB  . LEU   A  1 301 ? -5.139  -54.852 20.499 1.00 46.99  ? 1068 LEU   A CB  1 
ATOM   2021 C  CG  . LEU   A  1 301 ? -3.751  -54.269 20.228 1.00 35.96  ? 1068 LEU   A CG  1 
ATOM   2022 C  CD1 . LEU   A  1 301 ? -3.223  -54.768 18.894 1.00 39.44  ? 1068 LEU   A CD1 1 
ATOM   2023 C  CD2 . LEU   A  1 301 ? -3.769  -52.750 20.270 1.00 44.82  ? 1068 LEU   A CD2 1 
ATOM   2024 N  N   . VAL   A  1 302 ? -5.125  -56.209 23.260 1.00 39.92  ? 1069 VAL   A N   1 
ATOM   2025 C  CA  . VAL   A  1 302 ? -4.550  -56.423 24.585 1.00 42.25  ? 1069 VAL   A CA  1 
ATOM   2026 C  C   . VAL   A  1 302 ? -4.414  -57.913 24.876 1.00 45.18  ? 1069 VAL   A C   1 
ATOM   2027 O  O   . VAL   A  1 302 ? -3.407  -58.361 25.438 1.00 43.20  ? 1069 VAL   A O   1 
ATOM   2028 C  CB  . VAL   A  1 302 ? -5.395  -55.709 25.657 1.00 43.42  ? 1069 VAL   A CB  1 
ATOM   2029 C  CG1 . VAL   A  1 302 ? -4.857  -56.012 27.048 1.00 44.82  ? 1069 VAL   A CG1 1 
ATOM   2030 C  CG2 . VAL   A  1 302 ? -5.408  -54.211 25.403 1.00 55.79  ? 1069 VAL   A CG2 1 
ATOM   2031 N  N   . GLY   A  1 303 ? -5.421  -58.703 24.498 1.00 37.44  ? 1070 GLY   A N   1 
ATOM   2032 C  CA  . GLY   A  1 303 ? -5.333  -60.139 24.701 1.00 43.66  ? 1070 GLY   A CA  1 
ATOM   2033 C  C   . GLY   A  1 303 ? -4.193  -60.777 23.930 1.00 41.44  ? 1070 GLY   A C   1 
ATOM   2034 O  O   . GLY   A  1 303 ? -3.501  -61.658 24.445 1.00 40.39  ? 1070 GLY   A O   1 
ATOM   2035 N  N   . GLN   A  1 304 ? -3.983  -60.345 22.684 1.00 34.47  ? 1071 GLN   A N   1 
ATOM   2036 C  CA  . GLN   A  1 304 ? -2.892  -60.905 21.892 1.00 45.05  ? 1071 GLN   A CA  1 
ATOM   2037 C  C   . GLN   A  1 304 ? -1.529  -60.467 22.414 1.00 44.69  ? 1071 GLN   A C   1 
ATOM   2038 O  O   . GLN   A  1 304 ? -0.548  -61.207 22.276 1.00 42.55  ? 1071 GLN   A O   1 
ATOM   2039 C  CB  . GLN   A  1 304 ? -3.043  -60.509 20.423 1.00 37.46  ? 1071 GLN   A CB  1 
ATOM   2040 C  CG  . GLN   A  1 304 ? -4.199  -61.174 19.697 1.00 51.32  ? 1071 GLN   A CG  1 
ATOM   2041 C  CD  . GLN   A  1 304 ? -4.384  -60.632 18.293 1.00 44.34  ? 1071 GLN   A CD  1 
ATOM   2042 O  OE1 . GLN   A  1 304 ? -4.192  -59.441 18.046 1.00 46.66  ? 1071 GLN   A OE1 1 
ATOM   2043 N  NE2 . GLN   A  1 304 ? -4.755  -61.506 17.364 1.00 38.02  ? 1071 GLN   A NE2 1 
ATOM   2044 N  N   . ILE   A  1 305 ? -1.448  -59.277 23.015 1.00 40.56  ? 1072 ILE   A N   1 
ATOM   2045 C  CA  . ILE   A  1 305 ? -0.214  -58.853 23.671 1.00 47.14  ? 1072 ILE   A CA  1 
ATOM   2046 C  C   . ILE   A  1 305 ? 0.052   -59.693 24.915 1.00 38.51  ? 1072 ILE   A C   1 
ATOM   2047 O  O   . ILE   A  1 305 ? 1.189   -60.118 25.160 1.00 38.05  ? 1072 ILE   A O   1 
ATOM   2048 C  CB  . ILE   A  1 305 ? -0.273  -57.349 23.993 1.00 39.68  ? 1072 ILE   A CB  1 
ATOM   2049 C  CG1 . ILE   A  1 305 ? -0.256  -56.533 22.699 1.00 38.70  ? 1072 ILE   A CG1 1 
ATOM   2050 C  CG2 . ILE   A  1 305 ? 0.885   -56.947 24.892 1.00 43.22  ? 1072 ILE   A CG2 1 
ATOM   2051 C  CD1 . ILE   A  1 305 ? -0.571  -55.066 22.894 1.00 47.12  ? 1072 ILE   A CD1 1 
ATOM   2052 N  N   . ASP   A  1 306 ? -0.986  -59.948 25.718 1.00 40.29  ? 1073 ASP   A N   1 
ATOM   2053 C  CA  . ASP   A  1 306 ? -0.822  -60.809 26.886 1.00 42.86  ? 1073 ASP   A CA  1 
ATOM   2054 C  C   . ASP   A  1 306 ? -0.410  -62.214 26.470 1.00 46.18  ? 1073 ASP   A C   1 
ATOM   2055 O  O   . ASP   A  1 306 ? 0.428   -62.842 27.128 1.00 44.29  ? 1073 ASP   A O   1 
ATOM   2056 C  CB  . ASP   A  1 306 ? -2.109  -60.848 27.710 1.00 44.26  ? 1073 ASP   A CB  1 
ATOM   2057 C  CG  . ASP   A  1 306 ? -2.429  -59.517 28.351 1.00 58.30  ? 1073 ASP   A CG  1 
ATOM   2058 O  OD1 . ASP   A  1 306 ? -1.495  -58.708 28.537 1.00 52.79  ? 1073 ASP   A OD1 1 
ATOM   2059 O  OD2 . ASP   A  1 306 ? -3.611  -59.284 28.679 1.00 57.73  ? 1073 ASP   A OD2 1 
ATOM   2060 N  N   . ASP   A  1 307 ? -1.005  -62.731 25.389 1.00 37.93  ? 1074 ASP   A N   1 
ATOM   2061 C  CA  . ASP   A  1 307 ? -0.624  -64.049 24.887 1.00 37.22  ? 1074 ASP   A CA  1 
ATOM   2062 C  C   . ASP   A  1 307 ? 0.868   -64.104 24.587 1.00 43.89  ? 1074 ASP   A C   1 
ATOM   2063 O  O   . ASP   A  1 307 ? 1.564   -65.037 25.004 1.00 34.83  ? 1074 ASP   A O   1 
ATOM   2064 C  CB  . ASP   A  1 307 ? -1.427  -64.381 23.627 1.00 38.33  ? 1074 ASP   A CB  1 
ATOM   2065 C  CG  . ASP   A  1 307 ? -2.900  -64.586 23.903 1.00 53.29  ? 1074 ASP   A CG  1 
ATOM   2066 O  OD1 . ASP   A  1 307 ? -3.272  -64.702 25.090 1.00 52.15  ? 1074 ASP   A OD1 1 
ATOM   2067 O  OD2 . ASP   A  1 307 ? -3.689  -64.600 22.934 1.00 38.50  ? 1074 ASP   A OD2 1 
ATOM   2068 N  N   . ALA   A  1 308 ? 1.378   -63.105 23.863 1.00 38.02  ? 1075 ALA   A N   1 
ATOM   2069 C  CA  . ALA   A  1 308 ? 2.787   -63.099 23.487 1.00 45.21  ? 1075 ALA   A CA  1 
ATOM   2070 C  C   . ALA   A  1 308 ? 3.683   -62.870 24.698 1.00 43.10  ? 1075 ALA   A C   1 
ATOM   2071 O  O   . ALA   A  1 308 ? 4.777   -63.441 24.786 1.00 42.27  ? 1075 ALA   A O   1 
ATOM   2072 C  CB  . ALA   A  1 308 ? 3.036   -62.035 22.419 1.00 33.06  ? 1075 ALA   A CB  1 
ATOM   2073 N  N   . LEU   A  1 309 ? 3.241   -62.026 25.635 1.00 42.00  ? 1076 LEU   A N   1 
ATOM   2074 C  CA  . LEU   A  1 309 ? 4.036   -61.761 26.830 1.00 44.60  ? 1076 LEU   A CA  1 
ATOM   2075 C  C   . LEU   A  1 309 ? 4.188   -63.013 27.682 1.00 44.65  ? 1076 LEU   A C   1 
ATOM   2076 O  O   . LEU   A  1 309 ? 5.238   -63.228 28.300 1.00 40.61  ? 1076 LEU   A O   1 
ATOM   2077 C  CB  . LEU   A  1 309 ? 3.401   -60.636 27.649 1.00 45.57  ? 1076 LEU   A CB  1 
ATOM   2078 C  CG  . LEU   A  1 309 ? 4.079   -59.266 27.587 1.00 59.79  ? 1076 LEU   A CG  1 
ATOM   2079 C  CD1 . LEU   A  1 309 ? 3.226   -58.212 28.276 1.00 46.34  ? 1076 LEU   A CD1 1 
ATOM   2080 C  CD2 . LEU   A  1 309 ? 5.472   -59.320 28.199 1.00 44.01  ? 1076 LEU   A CD2 1 
ATOM   2081 N  N   . LYS   A  1 310 ? 3.149   -63.850 27.733 1.00 42.75  ? 1077 LYS   A N   1 
ATOM   2082 C  CA  . LYS   A  1 310 ? 3.246   -65.088 28.499 1.00 43.63  ? 1077 LYS   A CA  1 
ATOM   2083 C  C   . LYS   A  1 310 ? 4.271   -66.032 27.882 1.00 46.20  ? 1077 LYS   A C   1 
ATOM   2084 O  O   . LYS   A  1 310 ? 5.053   -66.664 28.602 1.00 45.91  ? 1077 LYS   A O   1 
ATOM   2085 C  CB  . LYS   A  1 310 ? 1.873   -65.754 28.587 1.00 31.76  ? 1077 LYS   A CB  1 
ATOM   2086 C  CG  . LYS   A  1 310 ? 1.869   -67.100 29.293 1.00 53.14  ? 1077 LYS   A CG  1 
ATOM   2087 C  CD  . LYS   A  1 310 ? 1.623   -68.236 28.313 1.00 66.79  ? 1077 LYS   A CD  1 
ATOM   2088 N  N   . LEU   A  1 311 ? 4.280   -66.141 26.552 1.00 41.20  ? 1078 LEU   A N   1 
ATOM   2089 C  CA  . LEU   A  1 311 ? 5.279   -66.963 25.876 1.00 43.77  ? 1078 LEU   A CA  1 
ATOM   2090 C  C   . LEU   A  1 311 ? 6.680   -66.400 26.077 1.00 47.77  ? 1078 LEU   A C   1 
ATOM   2091 O  O   . LEU   A  1 311 ? 7.635   -67.154 26.300 1.00 48.03  ? 1078 LEU   A O   1 
ATOM   2092 C  CB  . LEU   A  1 311 ? 4.944   -67.086 24.391 1.00 39.18  ? 1078 LEU   A CB  1 
ATOM   2093 C  CG  . LEU   A  1 311 ? 3.648   -67.846 24.102 1.00 44.25  ? 1078 LEU   A CG  1 
ATOM   2094 C  CD1 . LEU   A  1 311 ? 3.251   -67.723 22.639 1.00 45.51  ? 1078 LEU   A CD1 1 
ATOM   2095 C  CD2 . LEU   A  1 311 ? 3.784   -69.308 24.508 1.00 38.71  ? 1078 LEU   A CD2 1 
ATOM   2096 N  N   . ALA   A  1 312 ? 6.822   -65.075 25.980 1.00 41.54  ? 1079 ALA   A N   1 
ATOM   2097 C  CA  . ALA   A  1 312 ? 8.111   -64.433 26.220 1.00 50.52  ? 1079 ALA   A CA  1 
ATOM   2098 C  C   . ALA   A  1 312 ? 8.648   -64.790 27.601 1.00 56.71  ? 1079 ALA   A C   1 
ATOM   2099 O  O   . ALA   A  1 312 ? 9.820   -65.154 27.749 1.00 62.11  ? 1079 ALA   A O   1 
ATOM   2100 C  CB  . ALA   A  1 312 ? 7.983   -62.918 26.059 1.00 47.18  ? 1079 ALA   A CB  1 
ATOM   2101 N  N   . ASN   A  1 313 ? 7.802   -64.688 28.629 1.00 44.55  ? 1080 ASN   A N   1 
ATOM   2102 C  CA  . ASN   A  1 313 ? 8.240   -64.982 29.989 1.00 57.69  ? 1080 ASN   A CA  1 
ATOM   2103 C  C   . ASN   A  1 313 ? 8.607   -66.450 30.182 1.00 51.71  ? 1080 ASN   A C   1 
ATOM   2104 O  O   . ASN   A  1 313 ? 9.351   -66.768 31.116 1.00 63.06  ? 1080 ASN   A O   1 
ATOM   2105 C  CB  . ASN   A  1 313 ? 7.163   -64.568 30.993 1.00 57.71  ? 1080 ASN   A CB  1 
ATOM   2106 C  CG  . ASN   A  1 313 ? 6.985   -63.063 31.066 1.00 55.25  ? 1080 ASN   A CG  1 
ATOM   2107 O  OD1 . ASN   A  1 313 ? 7.957   -62.310 31.052 1.00 60.32  ? 1080 ASN   A OD1 1 
ATOM   2108 N  ND2 . ASN   A  1 313 ? 5.737   -62.619 31.149 1.00 51.48  ? 1080 ASN   A ND2 1 
ATOM   2109 N  N   . GLU   A  1 314 ? 8.111   -67.349 29.328 1.00 47.65  ? 1081 GLU   A N   1 
ATOM   2110 C  CA  . GLU   A  1 314 ? 8.564   -68.738 29.333 1.00 58.65  ? 1081 GLU   A CA  1 
ATOM   2111 C  C   . GLU   A  1 314 ? 9.829   -68.949 28.511 1.00 58.93  ? 1081 GLU   A C   1 
ATOM   2112 O  O   . GLU   A  1 314 ? 10.278  -70.093 28.381 1.00 69.74  ? 1081 GLU   A O   1 
ATOM   2113 C  CB  . GLU   A  1 314 ? 7.473   -69.688 28.825 1.00 58.64  ? 1081 GLU   A CB  1 
ATOM   2114 C  CG  . GLU   A  1 314 ? 6.243   -69.813 29.716 1.00 50.89  ? 1081 GLU   A CG  1 
ATOM   2115 C  CD  . GLU   A  1 314 ? 5.073   -70.460 28.996 1.00 67.77  ? 1081 GLU   A CD  1 
ATOM   2116 O  OE1 . GLU   A  1 314 ? 5.193   -70.707 27.777 1.00 66.19  ? 1081 GLU   A OE1 1 
ATOM   2117 O  OE2 . GLU   A  1 314 ? 4.042   -70.737 29.644 1.00 82.52  ? 1081 GLU   A OE2 1 
ATOM   2118 N  N   . GLY   A  1 315 ? 10.414  -67.889 27.955 1.00 55.52  ? 1082 GLY   A N   1 
ATOM   2119 C  CA  . GLY   A  1 315 ? 11.605  -68.049 27.144 1.00 55.43  ? 1082 GLY   A CA  1 
ATOM   2120 C  C   . GLY   A  1 315 ? 11.378  -68.654 25.779 1.00 57.17  ? 1082 GLY   A C   1 
ATOM   2121 O  O   . GLY   A  1 315 ? 12.322  -69.169 25.174 1.00 70.14  ? 1082 GLY   A O   1 
ATOM   2122 N  N   . LYS   A  1 316 ? 10.145  -68.611 25.276 1.00 44.98  ? 1083 LYS   A N   1 
ATOM   2123 C  CA  . LYS   A  1 316 ? 9.807   -69.150 23.961 1.00 42.35  ? 1083 LYS   A CA  1 
ATOM   2124 C  C   . LYS   A  1 316 ? 9.777   -67.991 22.970 1.00 52.78  ? 1083 LYS   A C   1 
ATOM   2125 O  O   . LYS   A  1 316 ? 8.736   -67.405 22.676 1.00 51.84  ? 1083 LYS   A O   1 
ATOM   2126 C  CB  . LYS   A  1 316 ? 8.483   -69.906 23.998 1.00 46.11  ? 1083 LYS   A CB  1 
ATOM   2127 C  CG  . LYS   A  1 316 ? 8.391   -70.949 25.094 1.00 45.19  ? 1083 LYS   A CG  1 
ATOM   2128 C  CD  . LYS   A  1 316 ? 7.041   -71.642 25.072 1.00 55.08  ? 1083 LYS   A CD  1 
ATOM   2129 C  CE  . LYS   A  1 316 ? 6.953   -72.710 26.147 1.00 56.77  ? 1083 LYS   A CE  1 
ATOM   2130 N  NZ  . LYS   A  1 316 ? 5.636   -73.404 26.118 1.00 51.62  ? 1083 LYS   A NZ  1 
ATOM   2131 N  N   . VAL   A  1 317 ? 10.960  -67.662 22.453 1.00 41.84  ? 1084 VAL   A N   1 
ATOM   2132 C  CA  . VAL   A  1 317 ? 11.122  -66.460 21.641 1.00 38.62  ? 1084 VAL   A CA  1 
ATOM   2133 C  C   . VAL   A  1 317 ? 10.372  -66.605 20.317 1.00 47.28  ? 1084 VAL   A C   1 
ATOM   2134 O  O   . VAL   A  1 317 ? 9.538   -65.761 19.969 1.00 48.93  ? 1084 VAL   A O   1 
ATOM   2135 C  CB  . VAL   A  1 317 ? 12.616  -66.121 21.452 1.00 52.53  ? 1084 VAL   A CB  1 
ATOM   2136 C  CG1 . VAL   A  1 317 ? 13.392  -67.248 20.765 1.00 56.03  ? 1084 VAL   A CG1 1 
ATOM   2137 C  CG2 . VAL   A  1 317 ? 12.775  -64.807 20.691 1.00 47.14  ? 1084 VAL   A CG2 1 
ATOM   2138 N  N   . LYS   A  1 318 ? 10.677  -67.656 19.548 1.00 44.74  ? 1085 LYS   A N   1 
ATOM   2139 C  CA  . LYS   A  1 318 ? 10.014  -67.866 18.262 1.00 47.63  ? 1085 LYS   A CA  1 
ATOM   2140 C  C   . LYS   A  1 318 ? 8.489   -67.859 18.381 1.00 40.13  ? 1085 LYS   A C   1 
ATOM   2141 O  O   . LYS   A  1 318 ? 7.807   -67.244 17.552 1.00 38.83  ? 1085 LYS   A O   1 
ATOM   2142 C  CB  . LYS   A  1 318 ? 10.511  -69.165 17.624 1.00 50.20  ? 1085 LYS   A CB  1 
ATOM   2143 C  CG  . LYS   A  1 318 ? 11.987  -69.123 17.230 1.00 48.38  ? 1085 LYS   A CG  1 
ATOM   2144 C  CD  . LYS   A  1 318 ? 12.195  -68.341 15.935 1.00 44.44  ? 1085 LYS   A CD  1 
ATOM   2145 C  CE  . LYS   A  1 318 ? 13.621  -68.482 15.419 1.00 44.35  ? 1085 LYS   A CE  1 
ATOM   2146 N  NZ  . LYS   A  1 318 ? 13.729  -68.165 13.966 1.00 62.14  ? 1085 LYS   A NZ  1 
ATOM   2147 N  N   . GLU   A  1 319 ? 7.923   -68.539 19.389 1.00 35.73  ? 1086 GLU   A N   1 
ATOM   2148 C  CA  . GLU   A  1 319 ? 6.463   -68.515 19.520 1.00 43.45  ? 1086 GLU   A CA  1 
ATOM   2149 C  C   . GLU   A  1 319 ? 5.961   -67.121 19.861 1.00 42.32  ? 1086 GLU   A C   1 
ATOM   2150 O  O   . GLU   A  1 319 ? 4.882   -66.720 19.412 1.00 44.70  ? 1086 GLU   A O   1 
ATOM   2151 C  CB  . GLU   A  1 319 ? 5.936   -69.486 20.578 1.00 36.33  ? 1086 GLU   A CB  1 
ATOM   2152 C  CG  . GLU   A  1 319 ? 5.450   -70.828 20.072 1.00 59.14  ? 1086 GLU   A CG  1 
ATOM   2153 C  CD  . GLU   A  1 319 ? 5.058   -71.744 21.215 1.00 69.00  ? 1086 GLU   A CD  1 
ATOM   2154 O  OE1 . GLU   A  1 319 ? 4.109   -71.392 21.955 1.00 73.44  ? 1086 GLU   A OE1 1 
ATOM   2155 O  OE2 . GLU   A  1 319 ? 5.701   -72.795 21.390 1.00 81.56  ? 1086 GLU   A OE2 1 
ATOM   2156 N  N   . ALA   A  1 320 ? 6.725   -66.368 20.653 1.00 34.40  ? 1087 ALA   A N   1 
ATOM   2157 C  CA  . ALA   A  1 320 ? 6.306   -65.014 20.988 1.00 46.66  ? 1087 ALA   A CA  1 
ATOM   2158 C  C   . ALA   A  1 320 ? 6.355   -64.107 19.766 1.00 45.04  ? 1087 ALA   A C   1 
ATOM   2159 O  O   . ALA   A  1 320 ? 5.456   -63.280 19.568 1.00 48.39  ? 1087 ALA   A O   1 
ATOM   2160 C  CB  . ALA   A  1 320 ? 7.182   -64.456 22.109 1.00 37.08  ? 1087 ALA   A CB  1 
ATOM   2161 N  N   . GLN   A  1 321 ? 7.390   -64.241 18.936 1.00 38.79  ? 1088 GLN   A N   1 
ATOM   2162 C  CA  . GLN   A  1 321 ? 7.446   -63.425 17.729 1.00 38.27  ? 1088 GLN   A CA  1 
ATOM   2163 C  C   . GLN   A  1 321 ? 6.322   -63.793 16.767 1.00 50.77  ? 1088 GLN   A C   1 
ATOM   2164 O  O   . GLN   A  1 321 ? 5.749   -62.916 16.109 1.00 53.59  ? 1088 GLN   A O   1 
ATOM   2165 C  CB  . GLN   A  1 321 ? 8.803   -63.593 17.046 1.00 37.94  ? 1088 GLN   A CB  1 
ATOM   2166 C  CG  . GLN   A  1 321 ? 9.982   -63.070 17.846 1.00 44.18  ? 1088 GLN   A CG  1 
ATOM   2167 C  CD  . GLN   A  1 321 ? 11.312  -63.457 17.229 1.00 51.54  ? 1088 GLN   A CD  1 
ATOM   2168 O  OE1 . GLN   A  1 321 ? 11.629  -64.640 17.102 1.00 57.43  ? 1088 GLN   A OE1 1 
ATOM   2169 N  NE2 . GLN   A  1 321 ? 12.094  -62.459 16.835 1.00 47.25  ? 1088 GLN   A NE2 1 
ATOM   2170 N  N   . ALA   A  1 322 ? 5.994   -65.084 16.671 1.00 38.01  ? 1089 ALA   A N   1 
ATOM   2171 C  CA  . ALA   A  1 322 ? 4.860   -65.499 15.850 1.00 44.29  ? 1089 ALA   A CA  1 
ATOM   2172 C  C   . ALA   A  1 322 ? 3.537   -65.007 16.426 1.00 45.71  ? 1089 ALA   A C   1 
ATOM   2173 O  O   . ALA   A  1 322 ? 2.669   -64.533 15.684 1.00 43.69  ? 1089 ALA   A O   1 
ATOM   2174 C  CB  . ALA   A  1 322 ? 4.848   -67.021 15.706 1.00 39.13  ? 1089 ALA   A CB  1 
ATOM   2175 N  N   . ALA   A  1 323 ? 3.359   -65.128 17.746 1.00 39.52  ? 1090 ALA   A N   1 
ATOM   2176 C  CA  . ALA   A  1 323 ? 2.169   -64.585 18.397 1.00 41.33  ? 1090 ALA   A CA  1 
ATOM   2177 C  C   . ALA   A  1 323 ? 2.025   -63.087 18.156 1.00 43.56  ? 1090 ALA   A C   1 
ATOM   2178 O  O   . ALA   A  1 323 ? 0.911   -62.586 17.965 1.00 39.76  ? 1090 ALA   A O   1 
ATOM   2179 C  CB  . ALA   A  1 323 ? 2.209   -64.885 19.895 1.00 33.27  ? 1090 ALA   A CB  1 
ATOM   2180 N  N   . ALA   A  1 324 ? 3.142   -62.356 18.159 1.00 35.72  ? 1091 ALA   A N   1 
ATOM   2181 C  CA  . ALA   A  1 324 ? 3.078   -60.906 18.011 1.00 51.61  ? 1091 ALA   A CA  1 
ATOM   2182 C  C   . ALA   A  1 324 ? 2.742   -60.498 16.583 1.00 52.38  ? 1091 ALA   A C   1 
ATOM   2183 O  O   . ALA   A  1 324 ? 2.204   -59.409 16.362 1.00 51.28  ? 1091 ALA   A O   1 
ATOM   2184 C  CB  . ALA   A  1 324 ? 4.396   -60.272 18.451 1.00 40.05  ? 1091 ALA   A CB  1 
ATOM   2185 N  N   . GLU   A  1 325 ? 3.066   -61.345 15.605 1.00 43.11  ? 1092 GLU   A N   1 
ATOM   2186 C  CA  . GLU   A  1 325 ? 2.701   -61.059 14.222 1.00 54.04  ? 1092 GLU   A CA  1 
ATOM   2187 C  C   . GLU   A  1 325 ? 1.189   -61.026 14.036 1.00 56.54  ? 1092 GLU   A C   1 
ATOM   2188 O  O   . GLU   A  1 325 ? 0.690   -60.343 13.134 1.00 55.83  ? 1092 GLU   A O   1 
ATOM   2189 C  CB  . GLU   A  1 325 ? 3.347   -62.098 13.306 1.00 50.97  ? 1092 GLU   A CB  1 
ATOM   2190 C  CG  . GLU   A  1 325 ? 3.631   -61.643 11.888 1.00 70.96  ? 1092 GLU   A CG  1 
ATOM   2191 C  CD  . GLU   A  1 325 ? 4.824   -60.714 11.799 1.00 71.87  ? 1092 GLU   A CD  1 
ATOM   2192 O  OE1 . GLU   A  1 325 ? 5.804   -60.925 12.543 1.00 86.06  ? 1092 GLU   A OE1 1 
ATOM   2193 O  OE2 . GLU   A  1 325 ? 4.816   -59.825 10.925 1.00 73.82  ? 1092 GLU   A OE2 1 
ATOM   2194 N  N   . GLN   A  1 326 ? 0.447   -61.763 14.869 1.00 43.83  ? 1093 GLN   A N   1 
ATOM   2195 C  CA  . GLN   A  1 326 ? -1.012  -61.723 14.810 1.00 52.10  ? 1093 GLN   A CA  1 
ATOM   2196 C  C   . GLN   A  1 326 ? -1.554  -60.322 15.072 1.00 59.37  ? 1093 GLN   A C   1 
ATOM   2197 O  O   . GLN   A  1 326 ? -2.627  -59.970 14.570 1.00 57.72  ? 1093 GLN   A O   1 
ATOM   2198 C  CB  . GLN   A  1 326 ? -1.605  -62.708 15.816 1.00 52.70  ? 1093 GLN   A CB  1 
ATOM   2199 C  CG  . GLN   A  1 326 ? -2.307  -63.905 15.196 1.00 70.35  ? 1093 GLN   A CG  1 
ATOM   2200 C  CD  . GLN   A  1 326 ? -1.474  -64.584 14.129 1.00 62.93  ? 1093 GLN   A CD  1 
ATOM   2201 O  OE1 . GLN   A  1 326 ? -0.415  -65.143 14.415 1.00 60.20  ? 1093 GLN   A OE1 1 
ATOM   2202 N  NE2 . GLN   A  1 326 ? -1.950  -64.541 12.890 1.00 70.67  ? 1093 GLN   A NE2 1 
ATOM   2203 N  N   . LEU   A  1 327 ? -0.835  -59.525 15.872 1.00 47.74  ? 1094 LEU   A N   1 
ATOM   2204 C  CA  . LEU   A  1 327 ? -1.227  -58.150 16.180 1.00 50.17  ? 1094 LEU   A CA  1 
ATOM   2205 C  C   . LEU   A  1 327 ? -1.475  -57.344 14.916 1.00 52.45  ? 1094 LEU   A C   1 
ATOM   2206 O  O   . LEU   A  1 327 ? -2.285  -56.410 14.911 1.00 56.61  ? 1094 LEU   A O   1 
ATOM   2207 C  CB  . LEU   A  1 327 ? -0.143  -57.482 17.020 1.00 43.33  ? 1094 LEU   A CB  1 
ATOM   2208 C  CG  . LEU   A  1 327 ? 0.001   -58.072 18.427 1.00 45.82  ? 1094 LEU   A CG  1 
ATOM   2209 C  CD1 . LEU   A  1 327 ? 1.299   -57.632 19.075 1.00 41.71  ? 1094 LEU   A CD1 1 
ATOM   2210 C  CD2 . LEU   A  1 327 ? -1.182  -57.680 19.289 1.00 46.48  ? 1094 LEU   A CD2 1 
ATOM   2211 N  N   . LYS   A  1 328 ? -0.780  -57.692 13.834 1.00 46.74  ? 1095 LYS   A N   1 
ATOM   2212 C  CA  . LYS   A  1 328 ? -0.874  -56.930 12.592 1.00 50.86  ? 1095 LYS   A CA  1 
ATOM   2213 C  C   . LYS   A  1 328 ? -2.251  -57.074 11.962 1.00 57.46  ? 1095 LYS   A C   1 
ATOM   2214 O  O   . LYS   A  1 328 ? -2.787  -56.109 11.406 1.00 60.01  ? 1095 LYS   A O   1 
ATOM   2215 C  CB  . LYS   A  1 328 ? 0.213   -57.411 11.637 1.00 58.32  ? 1095 LYS   A CB  1 
ATOM   2216 C  CG  . LYS   A  1 328 ? 1.593   -56.963 12.059 1.00 57.91  ? 1095 LYS   A CG  1 
ATOM   2217 C  CD  . LYS   A  1 328 ? 2.683   -57.517 11.162 1.00 61.98  ? 1095 LYS   A CD  1 
ATOM   2218 C  CE  . LYS   A  1 328 ? 4.049   -56.938 11.548 1.00 68.81  ? 1095 LYS   A CE  1 
ATOM   2219 N  NZ  . LYS   A  1 328 ? 4.602   -55.937 10.575 1.00 80.20  ? 1095 LYS   A NZ  1 
ATOM   2220 N  N   . THR   A  1 329 ? -2.833  -58.276 12.032 1.00 55.75  ? 1096 THR   A N   1 
ATOM   2221 C  CA  . THR   A  1 329 ? -4.199  -58.473 11.557 1.00 55.45  ? 1096 THR   A CA  1 
ATOM   2222 C  C   . THR   A  1 329 ? -5.174  -57.592 12.332 1.00 46.57  ? 1096 THR   A C   1 
ATOM   2223 O  O   . THR   A  1 329 ? -6.082  -56.985 11.750 1.00 55.72  ? 1096 THR   A O   1 
ATOM   2224 C  CB  . THR   A  1 329 ? -4.579  -59.946 11.695 1.00 54.29  ? 1096 THR   A CB  1 
ATOM   2225 O  OG1 . THR   A  1 329 ? -3.727  -60.745 10.864 1.00 69.84  ? 1096 THR   A OG1 1 
ATOM   2226 C  CG2 . THR   A  1 329 ? -6.028  -60.165 11.289 1.00 47.21  ? 1096 THR   A CG2 1 
ATOM   2227 N  N   . THR   A  1 330 ? -4.998  -57.517 13.653 1.00 44.33  ? 1097 THR   A N   1 
ATOM   2228 C  CA  . THR   A  1 330 ? -5.849  -56.663 14.476 1.00 50.50  ? 1097 THR   A CA  1 
ATOM   2229 C  C   . THR   A  1 330 ? -5.606  -55.193 14.167 1.00 51.43  ? 1097 THR   A C   1 
ATOM   2230 O  O   . THR   A  1 330 ? -6.550  -54.396 14.110 1.00 51.57  ? 1097 THR   A O   1 
ATOM   2231 C  CB  . THR   A  1 330 ? -5.602  -56.940 15.961 1.00 39.36  ? 1097 THR   A CB  1 
ATOM   2232 O  OG1 . THR   A  1 330 ? -5.703  -58.345 16.215 1.00 54.85  ? 1097 THR   A OG1 1 
ATOM   2233 C  CG2 . THR   A  1 330 ? -6.619  -56.195 16.820 1.00 30.87  ? 1097 THR   A CG2 1 
ATOM   2234 N  N   . ARG   A  1 331 ? -4.340  -54.822 13.965 1.00 48.12  ? 1098 ARG   A N   1 
ATOM   2235 C  CA  . ARG   A  1 331 ? -3.994  -53.447 13.622 1.00 55.15  ? 1098 ARG   A CA  1 
ATOM   2236 C  C   . ARG   A  1 331 ? -4.666  -53.010 12.324 1.00 56.11  ? 1098 ARG   A C   1 
ATOM   2237 O  O   . ARG   A  1 331 ? -5.197  -51.896 12.237 1.00 56.50  ? 1098 ARG   A O   1 
ATOM   2238 C  CB  . ARG   A  1 331 ? -2.474  -53.320 13.535 1.00 47.82  ? 1098 ARG   A CB  1 
ATOM   2239 C  CG  . ARG   A  1 331 ? -1.969  -51.932 13.247 1.00 51.03  ? 1098 ARG   A CG  1 
ATOM   2240 C  CD  . ARG   A  1 331 ? -0.610  -51.965 12.566 1.00 57.22  ? 1098 ARG   A CD  1 
ATOM   2241 N  NE  . ARG   A  1 331 ? -0.603  -52.783 11.360 1.00 56.29  ? 1098 ARG   A NE  1 
ATOM   2242 C  CZ  . ARG   A  1 331 ? 0.495   -53.253 10.785 1.00 57.29  ? 1098 ARG   A CZ  1 
ATOM   2243 N  NH1 . ARG   A  1 331 ? 1.695   -53.012 11.287 1.00 49.27  ? 1098 ARG   A NH1 1 
ATOM   2244 N  NH2 . ARG   A  1 331 ? 0.387   -53.986 9.681  1.00 63.58  ? 1098 ARG   A NH2 1 
ATOM   2245 N  N   . ASN   A  1 332 ? -4.655  -53.870 11.305 1.00 58.76  ? 1099 ASN   A N   1 
ATOM   2246 C  CA  . ASN   A  1 332 ? -5.230  -53.501 10.014 1.00 56.33  ? 1099 ASN   A CA  1 
ATOM   2247 C  C   . ASN   A  1 332 ? -6.752  -53.430 10.088 1.00 61.35  ? 1099 ASN   A C   1 
ATOM   2248 O  O   . ASN   A  1 332 ? -7.367  -52.484 9.582  1.00 73.89  ? 1099 ASN   A O   1 
ATOM   2249 C  CB  . ASN   A  1 332 ? -4.789  -54.496 8.939  1.00 45.27  ? 1099 ASN   A CB  1 
ATOM   2250 C  CG  . ASN   A  1 332 ? -3.280  -54.569 8.794  1.00 59.72  ? 1099 ASN   A CG  1 
ATOM   2251 O  OD1 . ASN   A  1 332 ? -2.559  -53.663 9.211  1.00 59.41  ? 1099 ASN   A OD1 1 
ATOM   2252 N  ND2 . ASN   A  1 332 ? -2.795  -55.656 8.203  1.00 65.20  ? 1099 ASN   A ND2 1 
ATOM   2253 N  N   . ALA   A  1 333 ? -7.378  -54.429 10.715 1.00 53.06  ? 1100 ALA   A N   1 
ATOM   2254 C  CA  . ALA   A  1 333 ? -8.833  -54.545 10.719 1.00 51.98  ? 1100 ALA   A CA  1 
ATOM   2255 C  C   . ALA   A  1 333 ? -9.501  -53.581 11.694 1.00 57.64  ? 1100 ALA   A C   1 
ATOM   2256 O  O   . ALA   A  1 333 ? -10.654 -53.191 11.476 1.00 69.31  ? 1100 ALA   A O   1 
ATOM   2257 C  CB  . ALA   A  1 333 ? -9.241  -55.982 11.048 1.00 55.16  ? 1100 ALA   A CB  1 
ATOM   2258 N  N   . TYR   A  1 334 ? -8.808  -53.192 12.764 1.00 56.56  ? 1101 TYR   A N   1 
ATOM   2259 C  CA  . TYR   A  1 334 ? -9.398  -52.401 13.841 1.00 53.37  ? 1101 TYR   A CA  1 
ATOM   2260 C  C   . TYR   A  1 334 ? -8.637  -51.110 14.107 1.00 52.46  ? 1101 TYR   A C   1 
ATOM   2261 O  O   . TYR   A  1 334 ? -9.220  -50.028 13.980 1.00 55.49  ? 1101 TYR   A O   1 
ATOM   2262 C  CB  . TYR   A  1 334 ? -9.493  -53.253 15.114 1.00 48.95  ? 1101 TYR   A CB  1 
ATOM   2263 C  CG  . TYR   A  1 334 ? -10.433 -54.426 14.976 1.00 60.93  ? 1101 TYR   A CG  1 
ATOM   2264 C  CD1 . TYR   A  1 334 ? -11.797 -54.264 15.179 1.00 66.06  ? 1101 TYR   A CD1 1 
ATOM   2265 C  CD2 . TYR   A  1 334 ? -9.969  -55.685 14.614 1.00 55.95  ? 1101 TYR   A CD2 1 
ATOM   2266 C  CE1 . TYR   A  1 334 ? -12.671 -55.322 15.047 1.00 72.46  ? 1101 TYR   A CE1 1 
ATOM   2267 C  CE2 . TYR   A  1 334 ? -10.839 -56.754 14.478 1.00 53.79  ? 1101 TYR   A CE2 1 
ATOM   2268 C  CZ  . TYR   A  1 334 ? -12.190 -56.564 14.695 1.00 63.62  ? 1101 TYR   A CZ  1 
ATOM   2269 O  OH  . TYR   A  1 334 ? -13.065 -57.618 14.566 1.00 69.74  ? 1101 TYR   A OH  1 
ATOM   2270 N  N   . ILE   A  1 335 ? -7.360  -51.185 14.491 1.00 50.07  ? 1102 ILE   A N   1 
ATOM   2271 C  CA  . ILE   A  1 335 ? -6.679  -50.027 15.068 1.00 45.01  ? 1102 ILE   A CA  1 
ATOM   2272 C  C   . ILE   A  1 335 ? -6.612  -48.880 14.067 1.00 56.50  ? 1102 ILE   A C   1 
ATOM   2273 O  O   . ILE   A  1 335 ? -6.788  -47.711 14.433 1.00 53.22  ? 1102 ILE   A O   1 
ATOM   2274 C  CB  . ILE   A  1 335 ? -5.283  -50.421 15.585 1.00 51.95  ? 1102 ILE   A CB  1 
ATOM   2275 C  CG1 . ILE   A  1 335 ? -5.373  -51.695 16.427 1.00 54.15  ? 1102 ILE   A CG1 1 
ATOM   2276 C  CG2 . ILE   A  1 335 ? -4.676  -49.286 16.394 1.00 44.64  ? 1102 ILE   A CG2 1 
ATOM   2277 C  CD1 . ILE   A  1 335 ? -6.257  -51.553 17.652 1.00 51.04  ? 1102 ILE   A CD1 1 
ATOM   2278 N  N   . GLN   A  1 336 ? -6.349  -49.185 12.791 1.00 39.11  ? 1103 GLN   A N   1 
ATOM   2279 C  CA  . GLN   A  1 336 ? -6.254  -48.116 11.802 1.00 55.66  ? 1103 GLN   A CA  1 
ATOM   2280 C  C   . GLN   A  1 336 ? -7.586  -47.406 11.616 1.00 45.96  ? 1103 GLN   A C   1 
ATOM   2281 O  O   . GLN   A  1 336 ? -7.613  -46.195 11.372 1.00 41.20  ? 1103 GLN   A O   1 
ATOM   2282 C  CB  . GLN   A  1 336 ? -5.799  -48.678 10.454 1.00 51.30  ? 1103 GLN   A CB  1 
ATOM   2283 C  CG  . GLN   A  1 336 ? -4.400  -48.288 10.039 1.00 62.75  ? 1103 GLN   A CG  1 
ATOM   2284 C  CD  . GLN   A  1 336 ? -4.005  -48.861 8.690  1.00 74.47  ? 1103 GLN   A CD  1 
ATOM   2285 O  OE1 . GLN   A  1 336 ? -4.336  -50.002 8.363  1.00 75.77  ? 1103 GLN   A OE1 1 
ATOM   2286 N  NE2 . GLN   A  1 336 ? -3.284  -48.072 7.903  1.00 79.46  ? 1103 GLN   A NE2 1 
ATOM   2287 N  N   . LYS   A  1 337 ? -8.696  -48.137 11.725 1.00 43.70  ? 1104 LYS   A N   1 
ATOM   2288 C  CA  . LYS   A  1 337 ? -10.005 -47.500 11.636 1.00 45.68  ? 1104 LYS   A CA  1 
ATOM   2289 C  C   . LYS   A  1 337 ? -10.252 -46.544 12.798 1.00 47.43  ? 1104 LYS   A C   1 
ATOM   2290 O  O   . LYS   A  1 337 ? -10.807 -45.457 12.602 1.00 52.92  ? 1104 LYS   A O   1 
ATOM   2291 C  CB  . LYS   A  1 337 ? -11.099 -48.565 11.576 1.00 46.39  ? 1104 LYS   A CB  1 
ATOM   2292 C  CG  . LYS   A  1 337 ? -11.017 -49.471 10.358 1.00 55.47  ? 1104 LYS   A CG  1 
ATOM   2293 N  N   . TYR   A  1 338 ? -9.855  -46.929 14.015 1.00 43.35  ? 1105 TYR   A N   1 
ATOM   2294 C  CA  . TYR   A  1 338 ? -10.003 -46.023 15.151 1.00 45.93  ? 1105 TYR   A CA  1 
ATOM   2295 C  C   . TYR   A  1 338 ? -9.137  -44.779 14.999 1.00 45.30  ? 1105 TYR   A C   1 
ATOM   2296 O  O   . TYR   A  1 338 ? -9.599  -43.655 15.228 1.00 50.62  ? 1105 TYR   A O   1 
ATOM   2297 C  CB  . TYR   A  1 338 ? -9.658  -46.762 16.445 1.00 41.05  ? 1105 TYR   A CB  1 
ATOM   2298 C  CG  . TYR   A  1 338 ? -9.618  -45.878 17.671 1.00 53.14  ? 1105 TYR   A CG  1 
ATOM   2299 N  N   . LEU   A  1 339 ? -7.865  -44.965 14.636 1.00 35.07  ? 1106 LEU   A N   1 
ATOM   2300 C  CA  . LEU   A  1 339 ? -6.969  -43.833 14.409 1.00 40.67  ? 1106 LEU   A CA  1 
ATOM   2301 C  C   . LEU   A  1 339 ? -7.530  -42.863 13.376 1.00 39.77  ? 1106 LEU   A C   1 
ATOM   2302 O  O   . LEU   A  1 339 ? -7.542  -41.646 13.592 1.00 48.98  ? 1106 LEU   A O   1 
ATOM   2303 C  CB  . LEU   A  1 339 ? -5.577  -44.322 14.025 1.00 39.84  ? 1106 LEU   A CB  1 
ATOM   2304 C  CG  . LEU   A  1 339 ? -4.794  -44.568 15.317 1.00 59.56  ? 1106 LEU   A CG  1 
ATOM   2305 C  CD1 . LEU   A  1 339 ? -3.366  -44.892 15.021 1.00 71.58  ? 1106 LEU   A CD1 1 
ATOM   2306 C  CD2 . LEU   A  1 339 ? -4.883  -43.368 16.250 1.00 66.21  ? 1106 LEU   A CD2 1 
ATOM   2307 N  N   . GLU   A  1 340 ? -7.991  -43.387 12.238 1.00 38.71  ? 219  GLU   A N   1 
ATOM   2308 C  CA  . GLU   A  1 340 ? -8.497  -42.523 11.177 1.00 48.50  ? 219  GLU   A CA  1 
ATOM   2309 C  C   . GLU   A  1 340 ? -9.769  -41.807 11.612 1.00 51.06  ? 219  GLU   A C   1 
ATOM   2310 O  O   . GLU   A  1 340 ? -9.983  -40.644 11.253 1.00 43.40  ? 219  GLU   A O   1 
ATOM   2311 C  CB  . GLU   A  1 340 ? -8.722  -43.325 9.896  1.00 34.31  ? 219  GLU   A CB  1 
ATOM   2312 C  CG  . GLU   A  1 340 ? -7.426  -43.772 9.233  1.00 52.50  ? 219  GLU   A CG  1 
ATOM   2313 C  CD  . GLU   A  1 340 ? -7.628  -44.874 8.215  1.00 60.22  ? 219  GLU   A CD  1 
ATOM   2314 O  OE1 . GLU   A  1 340 ? -6.858  -44.920 7.232  1.00 61.21  ? 219  GLU   A OE1 1 
ATOM   2315 O  OE2 . GLU   A  1 340 ? -8.553  -45.693 8.395  1.00 71.80  ? 219  GLU   A OE2 1 
ATOM   2316 N  N   . ARG   A  1 341 ? -10.627 -42.482 12.379 1.00 39.12  ? 220  ARG   A N   1 
ATOM   2317 C  CA  . ARG   A  1 341 ? -11.842 -41.824 12.844 1.00 37.93  ? 220  ARG   A CA  1 
ATOM   2318 C  C   . ARG   A  1 341 ? -11.500 -40.747 13.865 1.00 41.10  ? 220  ARG   A C   1 
ATOM   2319 O  O   . ARG   A  1 341 ? -12.096 -39.663 13.858 1.00 50.08  ? 220  ARG   A O   1 
ATOM   2320 C  CB  . ARG   A  1 341 ? -12.806 -42.851 13.439 1.00 42.70  ? 220  ARG   A CB  1 
ATOM   2321 N  N   . ALA   A  1 342 ? -10.546 -41.030 14.754 1.00 39.00  ? 221  ALA   A N   1 
ATOM   2322 C  CA  . ALA   A  1 342 ? -10.106 -40.022 15.712 1.00 36.51  ? 221  ALA   A CA  1 
ATOM   2323 C  C   . ALA   A  1 342 ? -9.499  -38.824 14.993 1.00 45.42  ? 221  ALA   A C   1 
ATOM   2324 O  O   . ALA   A  1 342 ? -9.768  -37.671 15.350 1.00 42.31  ? 221  ALA   A O   1 
ATOM   2325 C  CB  . ALA   A  1 342 ? -9.102  -40.628 16.691 1.00 40.75  ? 221  ALA   A CB  1 
ATOM   2326 N  N   . ARG   A  1 343 ? -8.664  -39.083 13.983 1.00 40.83  ? 222  ARG   A N   1 
ATOM   2327 C  CA  . ARG   A  1 343 ? -8.107  -38.006 13.172 1.00 43.78  ? 222  ARG   A CA  1 
ATOM   2328 C  C   . ARG   A  1 343 ? -9.201  -37.198 12.482 1.00 47.27  ? 222  ARG   A C   1 
ATOM   2329 O  O   . ARG   A  1 343 ? -9.146  -35.962 12.447 1.00 46.31  ? 222  ARG   A O   1 
ATOM   2330 C  CB  . ARG   A  1 343 ? -7.171  -38.604 12.123 1.00 47.47  ? 222  ARG   A CB  1 
ATOM   2331 C  CG  . ARG   A  1 343 ? -6.442  -37.582 11.267 1.00 58.19  ? 222  ARG   A CG  1 
ATOM   2332 C  CD  . ARG   A  1 343 ? -5.590  -38.268 10.217 1.00 67.19  ? 222  ARG   A CD  1 
ATOM   2333 N  NE  . ARG   A  1 343 ? -4.696  -39.257 10.803 1.00 100.64 ? 222  ARG   A NE  1 
ATOM   2334 C  CZ  . ARG   A  1 343 ? -4.049  -40.190 10.116 1.00 104.19 ? 222  ARG   A CZ  1 
ATOM   2335 N  NH1 . ARG   A  1 343 ? -4.181  -40.299 8.803  1.00 95.37  ? 222  ARG   A NH1 1 
ATOM   2336 N  NH2 . ARG   A  1 343 ? -3.267  -41.048 10.765 1.00 89.47  ? 222  ARG   A NH2 1 
ATOM   2337 N  N   . SER   A  1 344 ? -10.210 -37.878 11.933 1.00 44.47  ? 223  SER   A N   1 
ATOM   2338 C  CA  . SER   A  1 344 ? -11.274 -37.172 11.226 1.00 37.35  ? 223  SER   A CA  1 
ATOM   2339 C  C   . SER   A  1 344 ? -12.107 -36.323 12.178 1.00 41.08  ? 223  SER   A C   1 
ATOM   2340 O  O   . SER   A  1 344 ? -12.550 -35.227 11.816 1.00 47.54  ? 223  SER   A O   1 
ATOM   2341 C  CB  . SER   A  1 344 ? -12.158 -38.170 10.479 1.00 47.22  ? 223  SER   A CB  1 
ATOM   2342 O  OG  . SER   A  1 344 ? -13.365 -37.561 10.057 1.00 63.11  ? 223  SER   A OG  1 
ATOM   2343 N  N   . THR   A  1 345 ? -12.326 -36.812 13.401 1.00 34.88  ? 224  THR   A N   1 
ATOM   2344 C  CA  . THR   A  1 345 ? -13.057 -36.031 14.393 1.00 43.56  ? 224  THR   A CA  1 
ATOM   2345 C  C   . THR   A  1 345 ? -12.276 -34.797 14.831 1.00 39.23  ? 224  THR   A C   1 
ATOM   2346 O  O   . THR   A  1 345 ? -12.841 -33.701 14.928 1.00 37.00  ? 224  THR   A O   1 
ATOM   2347 C  CB  . THR   A  1 345 ? -13.390 -36.910 15.599 1.00 37.53  ? 224  THR   A CB  1 
ATOM   2348 O  OG1 . THR   A  1 345 ? -14.311 -37.934 15.204 1.00 52.24  ? 224  THR   A OG1 1 
ATOM   2349 C  CG2 . THR   A  1 345 ? -14.009 -36.082 16.714 1.00 43.54  ? 224  THR   A CG2 1 
ATOM   2350 N  N   . LEU   A  1 346 ? -10.977 -34.953 15.098 1.00 36.16  ? 225  LEU   A N   1 
ATOM   2351 C  CA  . LEU   A  1 346 ? -10.163 -33.806 15.486 1.00 38.69  ? 225  LEU   A CA  1 
ATOM   2352 C  C   . LEU   A  1 346 ? -10.102 -32.759 14.379 1.00 42.17  ? 225  LEU   A C   1 
ATOM   2353 O  O   . LEU   A  1 346 ? -10.168 -31.555 14.651 1.00 41.25  ? 225  LEU   A O   1 
ATOM   2354 C  CB  . LEU   A  1 346 ? -8.760  -34.272 15.871 1.00 32.08  ? 225  LEU   A CB  1 
ATOM   2355 C  CG  . LEU   A  1 346 ? -8.531  -34.468 17.373 1.00 47.15  ? 225  LEU   A CG  1 
ATOM   2356 C  CD1 . LEU   A  1 346 ? -7.275  -35.283 17.634 1.00 47.84  ? 225  LEU   A CD1 1 
ATOM   2357 C  CD2 . LEU   A  1 346 ? -8.465  -33.129 18.090 1.00 52.78  ? 225  LEU   A CD2 1 
ATOM   2358 N  N   . GLN   A  1 347 ? -9.967  -33.198 13.124 1.00 38.54  ? 226  GLN   A N   1 
ATOM   2359 C  CA  . GLN   A  1 347 ? -9.881  -32.251 12.015 1.00 37.18  ? 226  GLN   A CA  1 
ATOM   2360 C  C   . GLN   A  1 347 ? -11.182 -31.475 11.829 1.00 37.96  ? 226  GLN   A C   1 
ATOM   2361 O  O   . GLN   A  1 347 ? -11.148 -30.298 11.450 1.00 31.49  ? 226  GLN   A O   1 
ATOM   2362 C  CB  . GLN   A  1 347 ? -9.456  -32.981 10.741 1.00 41.91  ? 226  GLN   A CB  1 
ATOM   2363 C  CG  . GLN   A  1 347 ? -8.015  -33.486 10.831 1.00 59.24  ? 226  GLN   A CG  1 
ATOM   2364 C  CD  . GLN   A  1 347 ? -7.612  -34.384 9.679  1.00 70.50  ? 226  GLN   A CD  1 
ATOM   2365 O  OE1 . GLN   A  1 347 ? -8.454  -34.854 8.916  1.00 70.47  ? 226  GLN   A OE1 1 
ATOM   2366 N  NE2 . GLN   A  1 347 ? -6.312  -34.630 9.552  1.00 63.75  ? 226  GLN   A NE2 1 
ATOM   2367 N  N   . LYS   A  1 348 ? -12.331 -32.107 12.087 1.00 32.69  ? 227  LYS   A N   1 
ATOM   2368 C  CA  . LYS   A  1 348 ? -13.602 -31.387 12.033 1.00 41.50  ? 227  LYS   A CA  1 
ATOM   2369 C  C   . LYS   A  1 348 ? -13.701 -30.380 13.168 1.00 38.59  ? 227  LYS   A C   1 
ATOM   2370 O  O   . LYS   A  1 348 ? -14.271 -29.296 13.001 1.00 36.17  ? 227  LYS   A O   1 
ATOM   2371 C  CB  . LYS   A  1 348 ? -14.795 -32.340 12.083 1.00 32.32  ? 227  LYS   A CB  1 
ATOM   2372 C  CG  . LYS   A  1 348 ? -15.012 -33.189 10.849 1.00 45.09  ? 227  LYS   A CG  1 
ATOM   2373 C  CD  . LYS   A  1 348 ? -16.272 -34.030 11.014 1.00 61.03  ? 227  LYS   A CD  1 
ATOM   2374 C  CE  . LYS   A  1 348 ? -17.363 -33.231 11.728 1.00 67.85  ? 227  LYS   A CE  1 
ATOM   2375 N  NZ  . LYS   A  1 348 ? -18.470 -32.818 10.822 1.00 79.38  ? 227  LYS   A NZ  1 
ATOM   2376 N  N   . GLU   A  1 349 ? -13.152 -30.729 14.331 1.00 34.60  ? 228  GLU   A N   1 
ATOM   2377 C  CA  . GLU   A  1 349 ? -13.113 -29.794 15.448 1.00 35.41  ? 228  GLU   A CA  1 
ATOM   2378 C  C   . GLU   A  1 349 ? -12.233 -28.600 15.111 1.00 32.36  ? 228  GLU   A C   1 
ATOM   2379 O  O   . GLU   A  1 349 ? -12.569 -27.461 15.457 1.00 32.34  ? 228  GLU   A O   1 
ATOM   2380 C  CB  . GLU   A  1 349 ? -12.634 -30.512 16.707 1.00 31.20  ? 228  GLU   A CB  1 
ATOM   2381 C  CG  . GLU   A  1 349 ? -13.780 -31.108 17.509 1.00 43.79  ? 228  GLU   A CG  1 
ATOM   2382 C  CD  . GLU   A  1 349 ? -13.320 -31.801 18.771 1.00 49.80  ? 228  GLU   A CD  1 
ATOM   2383 O  OE1 . GLU   A  1 349 ? -13.177 -31.117 19.804 1.00 60.78  ? 228  GLU   A OE1 1 
ATOM   2384 O  OE2 . GLU   A  1 349 ? -13.106 -33.031 18.731 1.00 54.06  ? 228  GLU   A OE2 1 
ATOM   2385 N  N   . VAL   A  1 350 ? -11.094 -28.838 14.457 1.00 31.06  ? 229  VAL   A N   1 
ATOM   2386 C  CA  . VAL   A  1 350 ? -10.287 -27.720 13.979 1.00 30.83  ? 229  VAL   A CA  1 
ATOM   2387 C  C   . VAL   A  1 350 ? -11.121 -26.870 13.027 1.00 33.82  ? 229  VAL   A C   1 
ATOM   2388 O  O   . VAL   A  1 350 ? -11.098 -25.635 13.091 1.00 34.45  ? 229  VAL   A O   1 
ATOM   2389 C  CB  . VAL   A  1 350 ? -8.994  -28.230 13.316 1.00 33.01  ? 229  VAL   A CB  1 
ATOM   2390 C  CG1 . VAL   A  1 350 ? -8.215  -27.076 12.710 1.00 23.85  ? 229  VAL   A CG1 1 
ATOM   2391 C  CG2 . VAL   A  1 350 ? -8.140  -28.978 14.326 1.00 36.46  ? 229  VAL   A CG2 1 
ATOM   2392 N  N   . HIS   A  1 351 ? -11.872 -27.521 12.130 1.00 34.31  ? 230  HIS   A N   1 
ATOM   2393 C  CA  . HIS   A  1 351 ? -12.684 -26.791 11.159 1.00 35.54  ? 230  HIS   A CA  1 
ATOM   2394 C  C   . HIS   A  1 351 ? -13.769 -25.958 11.825 1.00 37.90  ? 230  HIS   A C   1 
ATOM   2395 O  O   . HIS   A  1 351 ? -14.024 -24.820 11.413 1.00 35.32  ? 230  HIS   A O   1 
ATOM   2396 C  CB  . HIS   A  1 351 ? -13.344 -27.764 10.184 1.00 40.51  ? 230  HIS   A CB  1 
ATOM   2397 C  CG  . HIS   A  1 351 ? -14.001 -27.093 9.018  1.00 50.05  ? 230  HIS   A CG  1 
ATOM   2398 N  ND1 . HIS   A  1 351 ? -13.303 -26.559 7.957  1.00 56.72  ? 230  HIS   A ND1 1 
ATOM   2399 C  CD2 . HIS   A  1 351 ? -15.310 -26.849 8.768  1.00 44.41  ? 230  HIS   A CD2 1 
ATOM   2400 C  CE1 . HIS   A  1 351 ? -14.155 -26.027 7.097  1.00 53.49  ? 230  HIS   A CE1 1 
ATOM   2401 N  NE2 . HIS   A  1 351 ? -15.379 -26.190 7.566  1.00 57.59  ? 230  HIS   A NE2 1 
ATOM   2402 N  N   . ALA   A  1 352 ? -14.421 -26.501 12.853 1.00 32.50  ? 231  ALA   A N   1 
ATOM   2403 C  CA  . ALA   A  1 352 ? -15.459 -25.730 13.524 1.00 32.70  ? 231  ALA   A CA  1 
ATOM   2404 C  C   . ALA   A  1 352 ? -14.866 -24.582 14.328 1.00 36.44  ? 231  ALA   A C   1 
ATOM   2405 O  O   . ALA   A  1 352 ? -15.442 -23.489 14.376 1.00 37.23  ? 231  ALA   A O   1 
ATOM   2406 C  CB  . ALA   A  1 352 ? -16.294 -26.643 14.420 1.00 25.94  ? 231  ALA   A CB  1 
ATOM   2407 N  N   . ALA   A  1 353 ? -13.712 -24.808 14.961 1.00 28.02  ? 232  ALA   A N   1 
ATOM   2408 C  CA  . ALA   A  1 353 ? -13.061 -23.732 15.700 1.00 28.51  ? 232  ALA   A CA  1 
ATOM   2409 C  C   . ALA   A  1 353 ? -12.547 -22.635 14.776 1.00 26.70  ? 232  ALA   A C   1 
ATOM   2410 O  O   . ALA   A  1 353 ? -12.591 -21.451 15.132 1.00 34.45  ? 232  ALA   A O   1 
ATOM   2411 C  CB  . ALA   A  1 353 ? -11.920 -24.297 16.545 1.00 22.04  ? 232  ALA   A CB  1 
ATOM   2412 N  N   . LYS   A  1 354 ? -12.051 -22.999 13.589 1.00 27.31  ? 233  LYS   A N   1 
ATOM   2413 C  CA  . LYS   A  1 354 ? -11.630 -21.974 12.638 1.00 27.57  ? 233  LYS   A CA  1 
ATOM   2414 C  C   . LYS   A  1 354 ? -12.807 -21.126 12.176 1.00 32.01  ? 233  LYS   A C   1 
ATOM   2415 O  O   . LYS   A  1 354 ? -12.694 -19.899 12.070 1.00 27.14  ? 233  LYS   A O   1 
ATOM   2416 C  CB  . LYS   A  1 354 ? -10.929 -22.616 11.440 1.00 33.49  ? 233  LYS   A CB  1 
ATOM   2417 C  CG  . LYS   A  1 354 ? -9.553  -23.189 11.753 1.00 50.03  ? 233  LYS   A CG  1 
ATOM   2418 C  CD  . LYS   A  1 354 ? -8.829  -23.624 10.487 1.00 59.29  ? 233  LYS   A CD  1 
ATOM   2419 C  CE  . LYS   A  1 354 ? -7.435  -24.150 10.798 1.00 62.50  ? 233  LYS   A CE  1 
ATOM   2420 N  NZ  . LYS   A  1 354 ? -6.384  -23.105 10.668 1.00 77.27  ? 233  LYS   A NZ  1 
ATOM   2421 N  N   . SER   A  1 355 ? -13.950 -21.762 11.905 1.00 26.94  ? 234  SER   A N   1 
ATOM   2422 C  CA  . SER   A  1 355 ? -15.134 -21.017 11.487 1.00 32.92  ? 234  SER   A CA  1 
ATOM   2423 C  C   . SER   A  1 355 ? -15.589 -20.046 12.569 1.00 28.88  ? 234  SER   A C   1 
ATOM   2424 O  O   . SER   A  1 355 ? -15.918 -18.890 12.280 1.00 31.97  ? 234  SER   A O   1 
ATOM   2425 C  CB  . SER   A  1 355 ? -16.259 -21.984 11.117 1.00 19.07  ? 234  SER   A CB  1 
ATOM   2426 O  OG  . SER   A  1 355 ? -15.861 -22.844 10.063 1.00 27.40  ? 234  SER   A OG  1 
ATOM   2427 N  N   . ALA   A  1 356 ? -15.627 -20.506 13.822 1.00 30.13  ? 235  ALA   A N   1 
ATOM   2428 C  CA  . ALA   A  1 356 ? -16.012 -19.631 14.923 1.00 31.30  ? 235  ALA   A CA  1 
ATOM   2429 C  C   . ALA   A  1 356 ? -15.022 -18.485 15.096 1.00 32.01  ? 235  ALA   A C   1 
ATOM   2430 O  O   . ALA   A  1 356 ? -15.422 -17.346 15.367 1.00 27.72  ? 235  ALA   A O   1 
ATOM   2431 C  CB  . ALA   A  1 356 ? -16.134 -20.440 16.213 1.00 24.71  ? 235  ALA   A CB  1 
ATOM   2432 N  N   . ALA   A  1 357 ? -13.724 -18.769 14.953 1.00 24.45  ? 236  ALA   A N   1 
ATOM   2433 C  CA  . ALA   A  1 357 ? -12.714 -17.724 15.097 1.00 29.99  ? 236  ALA   A CA  1 
ATOM   2434 C  C   . ALA   A  1 357 ? -12.820 -16.680 13.991 1.00 25.81  ? 236  ALA   A C   1 
ATOM   2435 O  O   . ALA   A  1 357 ? -12.576 -15.491 14.230 1.00 20.94  ? 236  ALA   A O   1 
ATOM   2436 C  CB  . ALA   A  1 357 ? -11.318 -18.345 15.117 1.00 22.39  ? 236  ALA   A CB  1 
ATOM   2437 N  N   . ILE   A  1 358 ? -13.173 -17.103 12.773 1.00 21.04  ? 237  ILE   A N   1 
ATOM   2438 C  CA  . ILE   A  1 358 ? -13.375 -16.152 11.682 1.00 21.00  ? 237  ILE   A CA  1 
ATOM   2439 C  C   . ILE   A  1 358 ? -14.484 -15.169 12.031 1.00 25.63  ? 237  ILE   A C   1 
ATOM   2440 O  O   . ILE   A  1 358 ? -14.381 -13.966 11.761 1.00 25.34  ? 237  ILE   A O   1 
ATOM   2441 C  CB  . ILE   A  1 358 ? -13.667 -16.899 10.365 1.00 29.16  ? 237  ILE   A CB  1 
ATOM   2442 C  CG1 . ILE   A  1 358 ? -12.421 -17.649 9.888  1.00 24.61  ? 237  ILE   A CG1 1 
ATOM   2443 C  CG2 . ILE   A  1 358 ? -14.179 -15.943 9.294  1.00 18.09  ? 237  ILE   A CG2 1 
ATOM   2444 C  CD1 . ILE   A  1 358 ? -12.691 -18.630 8.767  1.00 28.30  ? 237  ILE   A CD1 1 
ATOM   2445 N  N   . ILE   A  1 359 ? -15.555 -15.664 12.651 1.00 24.49  ? 238  ILE   A N   1 
ATOM   2446 C  CA  . ILE   A  1 359 ? -16.676 -14.802 13.004 1.00 18.97  ? 238  ILE   A CA  1 
ATOM   2447 C  C   . ILE   A  1 359 ? -16.284 -13.844 14.122 1.00 24.62  ? 238  ILE   A C   1 
ATOM   2448 O  O   . ILE   A  1 359 ? -16.664 -12.666 14.109 1.00 18.79  ? 238  ILE   A O   1 
ATOM   2449 C  CB  . ILE   A  1 359 ? -17.890 -15.669 13.374 1.00 33.01  ? 238  ILE   A CB  1 
ATOM   2450 C  CG1 . ILE   A  1 359 ? -18.572 -16.143 12.093 1.00 32.63  ? 238  ILE   A CG1 1 
ATOM   2451 C  CG2 . ILE   A  1 359 ? -18.862 -14.904 14.256 1.00 19.38  ? 238  ILE   A CG2 1 
ATOM   2452 C  CD1 . ILE   A  1 359 ? -19.502 -17.276 12.301 1.00 42.42  ? 238  ILE   A CD1 1 
ATOM   2453 N  N   . ALA   A  1 360 ? -15.509 -14.324 15.097 1.00 17.48  ? 239  ALA   A N   1 
ATOM   2454 C  CA  . ALA   A  1 360 ? -14.987 -13.429 16.123 1.00 25.75  ? 239  ALA   A CA  1 
ATOM   2455 C  C   . ALA   A  1 360 ? -14.049 -12.393 15.517 1.00 19.78  ? 239  ALA   A C   1 
ATOM   2456 O  O   . ALA   A  1 360 ? -14.064 -11.222 15.914 1.00 21.41  ? 239  ALA   A O   1 
ATOM   2457 C  CB  . ALA   A  1 360 ? -14.272 -14.232 17.210 1.00 24.44  ? 239  ALA   A CB  1 
ATOM   2458 N  N   . GLY   A  1 361 ? -13.222 -12.807 14.554 1.00 24.79  ? 240  GLY   A N   1 
ATOM   2459 C  CA  . GLY   A  1 361 ? -12.318 -11.866 13.913 1.00 18.61  ? 240  GLY   A CA  1 
ATOM   2460 C  C   . GLY   A  1 361 ? -13.040 -10.830 13.072 1.00 23.77  ? 240  GLY   A C   1 
ATOM   2461 O  O   . GLY   A  1 361 ? -12.621 -9.671  13.006 1.00 22.49  ? 240  GLY   A O   1 
ATOM   2462 N  N   . LEU   A  1 362 ? -14.134 -11.230 12.418 1.00 19.04  ? 241  LEU   A N   1 
ATOM   2463 C  CA  . LEU   A  1 362 ? -14.909 -10.273 11.632 1.00 22.51  ? 241  LEU   A CA  1 
ATOM   2464 C  C   . LEU   A  1 362 ? -15.626 -9.263  12.517 1.00 20.39  ? 241  LEU   A C   1 
ATOM   2465 O  O   . LEU   A  1 362 ? -15.783 -8.102  12.122 1.00 23.95  ? 241  LEU   A O   1 
ATOM   2466 C  CB  . LEU   A  1 362 ? -15.906 -11.004 10.734 1.00 21.82  ? 241  LEU   A CB  1 
ATOM   2467 C  CG  . LEU   A  1 362 ? -15.275 -11.687 9.519  1.00 26.23  ? 241  LEU   A CG  1 
ATOM   2468 C  CD1 . LEU   A  1 362 ? -16.282 -12.573 8.806  1.00 30.26  ? 241  LEU   A CD1 1 
ATOM   2469 C  CD2 . LEU   A  1 362 ? -14.701 -10.644 8.571  1.00 32.97  ? 241  LEU   A CD2 1 
ATOM   2470 N  N   . PHE   A  1 363 ? -16.082 -9.682  13.700 1.00 20.15  ? 242  PHE   A N   1 
ATOM   2471 C  CA  . PHE   A  1 363 ? -16.625 -8.723  14.656 1.00 20.10  ? 242  PHE   A CA  1 
ATOM   2472 C  C   . PHE   A  1 363 ? -15.579 -7.672  15.002 1.00 17.49  ? 242  PHE   A C   1 
ATOM   2473 O  O   . PHE   A  1 363 ? -15.865 -6.469  15.011 1.00 16.01  ? 242  PHE   A O   1 
ATOM   2474 C  CB  . PHE   A  1 363 ? -17.113 -9.453  15.911 1.00 20.52  ? 242  PHE   A CB  1 
ATOM   2475 C  CG  . PHE   A  1 363 ? -17.704 -8.547  16.959 1.00 20.39  ? 242  PHE   A CG  1 
ATOM   2476 C  CD1 . PHE   A  1 363 ? -16.896 -7.873  17.863 1.00 21.24  ? 242  PHE   A CD1 1 
ATOM   2477 C  CD2 . PHE   A  1 363 ? -19.077 -8.374  17.040 1.00 17.73  ? 242  PHE   A CD2 1 
ATOM   2478 C  CE1 . PHE   A  1 363 ? -17.446 -7.040  18.822 1.00 26.33  ? 242  PHE   A CE1 1 
ATOM   2479 C  CE2 . PHE   A  1 363 ? -19.632 -7.546  17.997 1.00 22.44  ? 242  PHE   A CE2 1 
ATOM   2480 C  CZ  . PHE   A  1 363 ? -18.815 -6.878  18.889 1.00 18.63  ? 242  PHE   A CZ  1 
ATOM   2481 N  N   . ALA   A  1 364 ? -14.356 -8.116  15.301 1.00 21.13  ? 243  ALA   A N   1 
ATOM   2482 C  CA  . ALA   A  1 364 ? -13.286 -7.180  15.627 1.00 18.70  ? 243  ALA   A CA  1 
ATOM   2483 C  C   . ALA   A  1 364 ? -12.978 -6.270  14.446 1.00 19.31  ? 243  ALA   A C   1 
ATOM   2484 O  O   . ALA   A  1 364 ? -12.796 -5.059  14.615 1.00 21.97  ? 243  ALA   A O   1 
ATOM   2485 C  CB  . ALA   A  1 364 ? -12.035 -7.942  16.063 1.00 22.82  ? 243  ALA   A CB  1 
ATOM   2486 N  N   . LEU   A  1 365 ? -12.926 -6.835  13.237 1.00 20.56  ? 244  LEU   A N   1 
ATOM   2487 C  CA  . LEU   A  1 365 ? -12.595 -6.039  12.060 1.00 24.60  ? 244  LEU   A CA  1 
ATOM   2488 C  C   . LEU   A  1 365 ? -13.648 -4.971  11.796 1.00 26.12  ? 244  LEU   A C   1 
ATOM   2489 O  O   . LEU   A  1 365 ? -13.319 -3.849  11.393 1.00 22.92  ? 244  LEU   A O   1 
ATOM   2490 C  CB  . LEU   A  1 365 ? -12.439 -6.948  10.840 1.00 29.43  ? 244  LEU   A CB  1 
ATOM   2491 C  CG  . LEU   A  1 365 ? -11.766 -6.333  9.613  1.00 45.56  ? 244  LEU   A CG  1 
ATOM   2492 C  CD1 . LEU   A  1 365 ? -10.463 -5.663  10.008 1.00 47.25  ? 244  LEU   A CD1 1 
ATOM   2493 C  CD2 . LEU   A  1 365 ? -11.524 -7.387  8.545  1.00 45.69  ? 244  LEU   A CD2 1 
ATOM   2494 N  N   . CYS   A  1 366 ? -14.921 -5.297  12.022 1.00 21.00  ? 245  CYS   A N   1 
ATOM   2495 C  CA  . CYS   A  1 366 ? -15.992 -4.354  11.723 1.00 20.93  ? 245  CYS   A CA  1 
ATOM   2496 C  C   . CYS   A  1 366 ? -16.140 -3.282  12.797 1.00 20.94  ? 245  CYS   A C   1 
ATOM   2497 O  O   . CYS   A  1 366 ? -16.542 -2.155  12.485 1.00 20.25  ? 245  CYS   A O   1 
ATOM   2498 C  CB  . CYS   A  1 366 ? -17.314 -5.101  11.541 1.00 23.75  ? 245  CYS   A CB  1 
ATOM   2499 S  SG  . CYS   A  1 366 ? -17.392 -6.133  10.057 1.00 32.39  ? 245  CYS   A SG  1 
ATOM   2500 N  N   . TRP   A  1 367 ? -15.832 -3.603  14.054 1.00 18.74  ? 246  TRP   A N   1 
ATOM   2501 C  CA  . TRP   A  1 367 ? -16.023 -2.657  15.148 1.00 20.71  ? 246  TRP   A CA  1 
ATOM   2502 C  C   . TRP   A  1 367 ? -14.780 -1.858  15.508 1.00 19.73  ? 246  TRP   A C   1 
ATOM   2503 O  O   . TRP   A  1 367 ? -14.913 -0.754  16.045 1.00 21.84  ? 246  TRP   A O   1 
ATOM   2504 C  CB  . TRP   A  1 367 ? -16.513 -3.392  16.401 1.00 19.66  ? 246  TRP   A CB  1 
ATOM   2505 C  CG  . TRP   A  1 367 ? -17.959 -3.741  16.363 1.00 19.16  ? 246  TRP   A CG  1 
ATOM   2506 C  CD1 . TRP   A  1 367 ? -18.516 -4.924  15.975 1.00 18.33  ? 246  TRP   A CD1 1 
ATOM   2507 C  CD2 . TRP   A  1 367 ? -19.043 -2.900  16.769 1.00 16.70  ? 246  TRP   A CD2 1 
ATOM   2508 N  NE1 . TRP   A  1 367 ? -19.885 -4.863  16.095 1.00 21.88  ? 246  TRP   A NE1 1 
ATOM   2509 C  CE2 . TRP   A  1 367 ? -20.232 -3.630  16.583 1.00 24.82  ? 246  TRP   A CE2 1 
ATOM   2510 C  CE3 . TRP   A  1 367 ? -19.122 -1.595  17.265 1.00 18.86  ? 246  TRP   A CE3 1 
ATOM   2511 C  CZ2 . TRP   A  1 367 ? -21.486 -3.099  16.877 1.00 22.54  ? 246  TRP   A CZ2 1 
ATOM   2512 C  CZ3 . TRP   A  1 367 ? -20.367 -1.070  17.554 1.00 24.15  ? 246  TRP   A CZ3 1 
ATOM   2513 C  CH2 . TRP   A  1 367 ? -21.532 -1.820  17.359 1.00 23.11  ? 246  TRP   A CH2 1 
ATOM   2514 N  N   . LEU   A  1 368 ? -13.581 -2.379  15.244 1.00 20.83  ? 247  LEU   A N   1 
ATOM   2515 C  CA  . LEU   A  1 368 ? -12.376 -1.666  15.661 1.00 21.83  ? 247  LEU   A CA  1 
ATOM   2516 C  C   . LEU   A  1 368 ? -12.245 -0.270  15.061 1.00 20.08  ? 247  LEU   A C   1 
ATOM   2517 O  O   . LEU   A  1 368 ? -11.805 0.636   15.790 1.00 21.79  ? 247  LEU   A O   1 
ATOM   2518 C  CB  . LEU   A  1 368 ? -11.127 -2.503  15.356 1.00 21.49  ? 247  LEU   A CB  1 
ATOM   2519 C  CG  . LEU   A  1 368 ? -10.755 -3.521  16.437 1.00 26.76  ? 247  LEU   A CG  1 
ATOM   2520 C  CD1 . LEU   A  1 368 ? -9.731  -4.517  15.916 1.00 28.61  ? 247  LEU   A CD1 1 
ATOM   2521 C  CD2 . LEU   A  1 368 ? -10.243 -2.816  17.686 1.00 19.73  ? 247  LEU   A CD2 1 
ATOM   2522 N  N   . PRO   A  1 369 ? -12.581 -0.016  13.785 1.00 21.90  ? 248  PRO   A N   1 
ATOM   2523 C  CA  . PRO   A  1 369 ? -12.382 1.346   13.259 1.00 16.48  ? 248  PRO   A CA  1 
ATOM   2524 C  C   . PRO   A  1 369 ? -13.117 2.412   14.050 1.00 14.27  ? 248  PRO   A C   1 
ATOM   2525 O  O   . PRO   A  1 369 ? -12.535 3.461   14.350 1.00 17.35  ? 248  PRO   A O   1 
ATOM   2526 C  CB  . PRO   A  1 369 ? -12.904 1.230   11.821 1.00 19.06  ? 248  PRO   A CB  1 
ATOM   2527 C  CG  . PRO   A  1 369 ? -12.559 -0.167  11.459 1.00 21.73  ? 248  PRO   A CG  1 
ATOM   2528 C  CD  . PRO   A  1 369 ? -12.951 -0.939  12.695 1.00 18.45  ? 248  PRO   A CD  1 
ATOM   2529 N  N   . LEU   A  1 370 ? -14.384 2.172   14.397 1.00 16.80  ? 249  LEU   A N   1 
ATOM   2530 C  CA  . LEU   A  1 370 ? -15.136 3.151   15.175 1.00 15.80  ? 249  LEU   A CA  1 
ATOM   2531 C  C   . LEU   A  1 370 ? -14.520 3.362   16.552 1.00 17.34  ? 249  LEU   A C   1 
ATOM   2532 O  O   . LEU   A  1 370 ? -14.407 4.500   17.023 1.00 15.31  ? 249  LEU   A O   1 
ATOM   2533 C  CB  . LEU   A  1 370 ? -16.593 2.709   15.304 1.00 17.97  ? 249  LEU   A CB  1 
ATOM   2534 C  CG  . LEU   A  1 370 ? -17.597 3.759   15.786 1.00 27.06  ? 249  LEU   A CG  1 
ATOM   2535 C  CD1 . LEU   A  1 370 ? -17.437 5.074   15.039 1.00 23.37  ? 249  LEU   A CD1 1 
ATOM   2536 C  CD2 . LEU   A  1 370 ? -19.011 3.228   15.634 1.00 18.18  ? 249  LEU   A CD2 1 
ATOM   2537 N  N   . HIS   A  1 371 ? -14.117 2.274   17.215 1.00 16.46  ? 250  HIS   A N   1 
ATOM   2538 C  CA  . HIS   A  1 371 ? -13.463 2.400   18.513 1.00 20.83  ? 250  HIS   A CA  1 
ATOM   2539 C  C   . HIS   A  1 371 ? -12.140 3.148   18.399 1.00 17.28  ? 250  HIS   A C   1 
ATOM   2540 O  O   . HIS   A  1 371 ? -11.824 3.999   19.240 1.00 17.59  ? 250  HIS   A O   1 
ATOM   2541 C  CB  . HIS   A  1 371 ? -13.250 1.018   19.129 1.00 16.79  ? 250  HIS   A CB  1 
ATOM   2542 C  CG  . HIS   A  1 371 ? -14.508 0.376   19.628 1.00 22.95  ? 250  HIS   A CG  1 
ATOM   2543 N  ND1 . HIS   A  1 371 ? -15.220 0.868   20.700 1.00 16.15  ? 250  HIS   A ND1 1 
ATOM   2544 C  CD2 . HIS   A  1 371 ? -15.171 -0.729  19.211 1.00 20.22  ? 250  HIS   A CD2 1 
ATOM   2545 C  CE1 . HIS   A  1 371 ? -16.274 0.100   20.916 1.00 20.06  ? 250  HIS   A CE1 1 
ATOM   2546 N  NE2 . HIS   A  1 371 ? -16.266 -0.877  20.027 1.00 22.90  ? 250  HIS   A NE2 1 
ATOM   2547 N  N   . ILE   A  1 372 ? -11.348 2.834   17.372 1.00 17.05  ? 251  ILE   A N   1 
ATOM   2548 C  CA  . ILE   A  1 372 ? -10.069 3.512   17.177 1.00 13.08  ? 251  ILE   A CA  1 
ATOM   2549 C  C   . ILE   A  1 372 ? -10.278 5.003   16.936 1.00 16.36  ? 251  ILE   A C   1 
ATOM   2550 O  O   . ILE   A  1 372 ? -9.545  5.841   17.477 1.00 20.10  ? 251  ILE   A O   1 
ATOM   2551 C  CB  . ILE   A  1 372 ? -9.283  2.850   16.029 1.00 19.05  ? 251  ILE   A CB  1 
ATOM   2552 C  CG1 . ILE   A  1 372 ? -8.861  1.433   16.428 1.00 14.02  ? 251  ILE   A CG1 1 
ATOM   2553 C  CG2 . ILE   A  1 372 ? -8.071  3.687   15.647 1.00 16.07  ? 251  ILE   A CG2 1 
ATOM   2554 C  CD1 . ILE   A  1 372 ? -8.246  0.638   15.299 1.00 22.99  ? 251  ILE   A CD1 1 
ATOM   2555 N  N   . ILE   A  1 373 ? -11.273 5.360   16.119 1.00 13.07  ? 252  ILE   A N   1 
ATOM   2556 C  CA  . ILE   A  1 373 ? -11.587 6.772   15.910 1.00 12.17  ? 252  ILE   A CA  1 
ATOM   2557 C  C   . ILE   A  1 373 ? -11.931 7.450   17.231 1.00 16.97  ? 252  ILE   A C   1 
ATOM   2558 O  O   . ILE   A  1 373 ? -11.470 8.564   17.509 1.00 19.78  ? 252  ILE   A O   1 
ATOM   2559 C  CB  . ILE   A  1 373 ? -12.723 6.925   14.882 1.00 19.36  ? 252  ILE   A CB  1 
ATOM   2560 C  CG1 . ILE   A  1 373 ? -12.243 6.513   13.490 1.00 14.23  ? 252  ILE   A CG1 1 
ATOM   2561 C  CG2 . ILE   A  1 373 ? -13.239 8.353   14.872 1.00 15.49  ? 252  ILE   A CG2 1 
ATOM   2562 C  CD1 . ILE   A  1 373 ? -13.358 6.375   12.477 1.00 24.03  ? 252  ILE   A CD1 1 
ATOM   2563 N  N   . ASN   A  1 374 ? -12.754 6.800   18.060 1.00 16.56  ? 253  ASN   A N   1 
ATOM   2564 C  CA  . ASN   A  1 374 ? -13.058 7.351   19.378 1.00 15.06  ? 253  ASN   A CA  1 
ATOM   2565 C  C   . ASN   A  1 374 ? -11.790 7.564   20.196 1.00 19.69  ? 253  ASN   A C   1 
ATOM   2566 O  O   . ASN   A  1 374 ? -11.687 8.539   20.950 1.00 17.55  ? 253  ASN   A O   1 
ATOM   2567 C  CB  . ASN   A  1 374 ? -14.042 6.448   20.124 1.00 14.24  ? 253  ASN   A CB  1 
ATOM   2568 C  CG  . ASN   A  1 374 ? -15.453 6.544   19.573 1.00 20.88  ? 253  ASN   A CG  1 
ATOM   2569 O  OD1 . ASN   A  1 374 ? -15.797 7.504   18.880 1.00 21.63  ? 253  ASN   A OD1 1 
ATOM   2570 N  ND2 . ASN   A  1 374 ? -16.282 5.556   19.888 1.00 15.29  ? 253  ASN   A ND2 1 
ATOM   2571 N  N   . CYS   A  1 375 ? -10.813 6.661   20.062 1.00 12.57  ? 254  CYS   A N   1 
ATOM   2572 C  CA  . CYS   A  1 375 ? -9.555  6.826   20.785 1.00 17.96  ? 254  CYS   A CA  1 
ATOM   2573 C  C   . CYS   A  1 375 ? -8.814  8.074   20.323 1.00 13.78  ? 254  CYS   A C   1 
ATOM   2574 O  O   . CYS   A  1 375 ? -8.244  8.804   21.143 1.00 18.84  ? 254  CYS   A O   1 
ATOM   2575 C  CB  . CYS   A  1 375 ? -8.676  5.587   20.610 1.00 16.73  ? 254  CYS   A CB  1 
ATOM   2576 S  SG  . CYS   A  1 375 ? -9.239  4.124   21.509 1.00 19.75  ? 254  CYS   A SG  1 
ATOM   2577 N  N   . PHE   A  1 376 ? -8.805  8.335   19.013 1.00 15.46  ? 255  PHE   A N   1 
ATOM   2578 C  CA  . PHE   A  1 376 ? -8.178  9.555   18.514 1.00 16.88  ? 255  PHE   A CA  1 
ATOM   2579 C  C   . PHE   A  1 376 ? -8.895  10.790  19.041 1.00 21.56  ? 255  PHE   A C   1 
ATOM   2580 O  O   . PHE   A  1 376 ? -8.251  11.766  19.446 1.00 23.08  ? 255  PHE   A O   1 
ATOM   2581 C  CB  . PHE   A  1 376 ? -8.152  9.550   16.987 1.00 18.36  ? 255  PHE   A CB  1 
ATOM   2582 C  CG  . PHE   A  1 376 ? -6.980  8.814   16.406 1.00 20.42  ? 255  PHE   A CG  1 
ATOM   2583 C  CD1 . PHE   A  1 376 ? -5.772  9.462   16.208 1.00 14.97  ? 255  PHE   A CD1 1 
ATOM   2584 C  CD2 . PHE   A  1 376 ? -7.082  7.475   16.063 1.00 18.78  ? 255  PHE   A CD2 1 
ATOM   2585 C  CE1 . PHE   A  1 376 ? -4.688  8.791   15.677 1.00 24.04  ? 255  PHE   A CE1 1 
ATOM   2586 C  CE2 . PHE   A  1 376 ? -6.001  6.798   15.529 1.00 25.09  ? 255  PHE   A CE2 1 
ATOM   2587 C  CZ  . PHE   A  1 376 ? -4.802  7.458   15.336 1.00 27.89  ? 255  PHE   A CZ  1 
ATOM   2588 N  N   . THR   A  1 377 ? -10.230 10.773  19.028 1.00 20.65  ? 256  THR   A N   1 
ATOM   2589 C  CA  . THR   A  1 377 ? -10.990 11.919  19.516 1.00 16.30  ? 256  THR   A CA  1 
ATOM   2590 C  C   . THR   A  1 377 ? -10.671 12.188  20.981 1.00 19.70  ? 256  THR   A C   1 
ATOM   2591 O  O   . THR   A  1 377 ? -10.514 13.343  21.395 1.00 23.85  ? 256  THR   A O   1 
ATOM   2592 C  CB  . THR   A  1 377 ? -12.488 11.673  19.328 1.00 24.60  ? 256  THR   A CB  1 
ATOM   2593 O  OG1 . THR   A  1 377 ? -12.779 11.517  17.934 1.00 26.42  ? 256  THR   A OG1 1 
ATOM   2594 C  CG2 . THR   A  1 377 ? -13.295 12.839  19.881 1.00 20.65  ? 256  THR   A CG2 1 
ATOM   2595 N  N   . PHE   A  1 378 ? -10.552 11.122  21.773 1.00 17.70  ? 257  PHE   A N   1 
ATOM   2596 C  CA  . PHE   A  1 378 ? -10.388 11.229  23.218 1.00 23.76  ? 257  PHE   A CA  1 
ATOM   2597 C  C   . PHE   A  1 378 ? -8.947  11.560  23.589 1.00 24.35  ? 257  PHE   A C   1 
ATOM   2598 O  O   . PHE   A  1 378 ? -8.692  12.491  24.361 1.00 23.51  ? 257  PHE   A O   1 
ATOM   2599 C  CB  . PHE   A  1 378 ? -10.833 9.923   23.881 1.00 17.04  ? 257  PHE   A CB  1 
ATOM   2600 C  CG  . PHE   A  1 378 ? -10.739 9.932   25.378 1.00 18.65  ? 257  PHE   A CG  1 
ATOM   2601 C  CD1 . PHE   A  1 378 ? -11.546 10.767  26.135 1.00 19.24  ? 257  PHE   A CD1 1 
ATOM   2602 C  CD2 . PHE   A  1 378 ? -9.850  9.094   26.029 1.00 19.41  ? 257  PHE   A CD2 1 
ATOM   2603 C  CE1 . PHE   A  1 378 ? -11.463 10.770  27.514 1.00 14.81  ? 257  PHE   A CE1 1 
ATOM   2604 C  CE2 . PHE   A  1 378 ? -9.761  9.091   27.407 1.00 21.87  ? 257  PHE   A CE2 1 
ATOM   2605 C  CZ  . PHE   A  1 378 ? -10.569 9.931   28.152 1.00 23.56  ? 257  PHE   A CZ  1 
ATOM   2606 N  N   . PHE   A  1 379 ? -7.991  10.805  23.042 1.00 21.32  ? 258  PHE   A N   1 
ATOM   2607 C  CA  . PHE   A  1 379 ? -6.597  10.915  23.451 1.00 21.09  ? 258  PHE   A CA  1 
ATOM   2608 C  C   . PHE   A  1 379 ? -5.845  12.029  22.734 1.00 25.67  ? 258  PHE   A C   1 
ATOM   2609 O  O   . PHE   A  1 379 ? -4.785  12.444  23.214 1.00 30.69  ? 258  PHE   A O   1 
ATOM   2610 C  CB  . PHE   A  1 379 ? -5.872  9.585   23.221 1.00 15.94  ? 258  PHE   A CB  1 
ATOM   2611 C  CG  . PHE   A  1 379 ? -6.260  8.505   24.192 1.00 18.68  ? 258  PHE   A CG  1 
ATOM   2612 C  CD1 . PHE   A  1 379 ? -6.139  8.707   25.557 1.00 18.19  ? 258  PHE   A CD1 1 
ATOM   2613 C  CD2 . PHE   A  1 379 ? -6.734  7.284   23.740 1.00 14.40  ? 258  PHE   A CD2 1 
ATOM   2614 C  CE1 . PHE   A  1 379 ? -6.491  7.715   26.454 1.00 21.15  ? 258  PHE   A CE1 1 
ATOM   2615 C  CE2 . PHE   A  1 379 ? -7.088  6.288   24.632 1.00 19.30  ? 258  PHE   A CE2 1 
ATOM   2616 C  CZ  . PHE   A  1 379 ? -6.966  6.505   25.991 1.00 21.33  ? 258  PHE   A CZ  1 
ATOM   2617 N  N   . CYS   A  1 380 ? -6.354  12.524  21.604 1.00 29.21  ? 259  CYS   A N   1 
ATOM   2618 C  CA  . CYS   A  1 380 ? -5.676  13.552  20.816 1.00 31.78  ? 259  CYS   A CA  1 
ATOM   2619 C  C   . CYS   A  1 380 ? -6.585  14.762  20.632 1.00 23.80  ? 259  CYS   A C   1 
ATOM   2620 O  O   . CYS   A  1 380 ? -7.100  15.007  19.532 1.00 23.71  ? 259  CYS   A O   1 
ATOM   2621 C  CB  . CYS   A  1 380 ? -5.210  13.033  19.458 1.00 27.03  ? 259  CYS   A CB  1 
ATOM   2622 S  SG  . CYS   A  1 380 ? -4.032  14.176  18.682 1.00 46.10  ? 259  CYS   A SG  1 
ATOM   2623 N  N   . PRO   A  1 381 ? -6.804  15.546  21.691 1.00 31.87  ? 260  PRO   A N   1 
ATOM   2624 C  CA  . PRO   A  1 381 ? -7.609  16.766  21.546 1.00 41.26  ? 260  PRO   A CA  1 
ATOM   2625 C  C   . PRO   A  1 381 ? -6.927  17.823  20.700 1.00 42.41  ? 260  PRO   A C   1 
ATOM   2626 O  O   . PRO   A  1 381 ? -7.585  18.790  20.293 1.00 44.22  ? 260  PRO   A O   1 
ATOM   2627 C  CB  . PRO   A  1 381 ? -7.792  17.241  22.991 1.00 45.49  ? 260  PRO   A CB  1 
ATOM   2628 C  CG  . PRO   A  1 381 ? -6.578  16.735  23.693 1.00 34.74  ? 260  PRO   A CG  1 
ATOM   2629 C  CD  . PRO   A  1 381 ? -6.255  15.409  23.053 1.00 31.60  ? 260  PRO   A CD  1 
ATOM   2630 N  N   . ASP   A  1 382 ? -5.631  17.665  20.430 1.00 35.87  ? 261  ASP   A N   1 
ATOM   2631 C  CA  . ASP   A  1 382 ? -4.917  18.504  19.481 1.00 34.26  ? 261  ASP   A CA  1 
ATOM   2632 C  C   . ASP   A  1 382 ? -5.125  18.071  18.036 1.00 38.54  ? 261  ASP   A C   1 
ATOM   2633 O  O   . ASP   A  1 382 ? -4.760  18.818  17.121 1.00 36.93  ? 261  ASP   A O   1 
ATOM   2634 C  CB  . ASP   A  1 382 ? -3.426  18.470  19.815 1.00 55.44  ? 261  ASP   A CB  1 
ATOM   2635 C  CG  . ASP   A  1 382 ? -3.125  19.063  21.174 1.00 68.68  ? 261  ASP   A CG  1 
ATOM   2636 O  OD1 . ASP   A  1 382 ? -3.923  19.906  21.634 1.00 69.30  ? 261  ASP   A OD1 1 
ATOM   2637 O  OD2 . ASP   A  1 382 ? -2.098  18.683  21.780 1.00 71.45  ? 261  ASP   A OD2 1 
ATOM   2638 N  N   . CYS   A  1 383 ? -5.697  16.890  17.813 1.00 38.96  ? 262  CYS   A N   1 
ATOM   2639 C  CA  . CYS   A  1 383 ? -6.006  16.409  16.475 1.00 36.85  ? 262  CYS   A CA  1 
ATOM   2640 C  C   . CYS   A  1 383 ? -7.373  16.922  16.047 1.00 27.12  ? 262  CYS   A C   1 
ATOM   2641 O  O   . CYS   A  1 383 ? -8.295  17.020  16.863 1.00 33.81  ? 262  CYS   A O   1 
ATOM   2642 C  CB  . CYS   A  1 383 ? -5.988  14.878  16.417 1.00 38.76  ? 262  CYS   A CB  1 
ATOM   2643 S  SG  . CYS   A  1 383 ? -4.384  14.070  16.684 1.00 49.69  ? 262  CYS   A SG  1 
ATOM   2644 N  N   . SER   A  1 384 ? -7.500  17.253  14.765 1.00 30.25  ? 263  SER   A N   1 
ATOM   2645 C  CA  . SER   A  1 384 ? -8.811  17.573  14.221 1.00 32.89  ? 263  SER   A CA  1 
ATOM   2646 C  C   . SER   A  1 384 ? -9.709  16.345  14.296 1.00 31.83  ? 263  SER   A C   1 
ATOM   2647 O  O   . SER   A  1 384 ? -9.255  15.215  14.103 1.00 25.60  ? 263  SER   A O   1 
ATOM   2648 C  CB  . SER   A  1 384 ? -8.690  18.055  12.774 1.00 36.11  ? 263  SER   A CB  1 
ATOM   2649 O  OG  . SER   A  1 384 ? -8.242  19.398  12.718 1.00 49.96  ? 263  SER   A OG  1 
ATOM   2650 N  N   . HIS   A  1 385 ? -10.985 16.569  14.601 1.00 25.94  ? 264  HIS   A N   1 
ATOM   2651 C  CA  . HIS   A  1 385 ? -11.930 15.464  14.676 1.00 26.59  ? 264  HIS   A CA  1 
ATOM   2652 C  C   . HIS   A  1 385 ? -12.008 14.758  13.328 1.00 33.52  ? 264  HIS   A C   1 
ATOM   2653 O  O   . HIS   A  1 385 ? -11.952 15.397  12.274 1.00 22.23  ? 264  HIS   A O   1 
ATOM   2654 C  CB  . HIS   A  1 385 ? -13.310 15.976  15.095 1.00 22.50  ? 264  HIS   A CB  1 
ATOM   2655 C  CG  . HIS   A  1 385 ? -14.218 14.912  15.632 1.00 21.07  ? 264  HIS   A CG  1 
ATOM   2656 N  ND1 . HIS   A  1 385 ? -14.733 13.904  14.845 1.00 28.66  ? 264  HIS   A ND1 1 
ATOM   2657 C  CD2 . HIS   A  1 385 ? -14.706 14.703  16.878 1.00 26.62  ? 264  HIS   A CD2 1 
ATOM   2658 C  CE1 . HIS   A  1 385 ? -15.499 13.119  15.584 1.00 30.17  ? 264  HIS   A CE1 1 
ATOM   2659 N  NE2 . HIS   A  1 385 ? -15.499 13.582  16.821 1.00 30.58  ? 264  HIS   A NE2 1 
ATOM   2660 N  N   . ALA   A  1 386 ? -12.094 13.432  13.371 1.00 22.44  ? 265  ALA   A N   1 
ATOM   2661 C  CA  . ALA   A  1 386 ? -12.370 12.656  12.172 1.00 22.29  ? 265  ALA   A CA  1 
ATOM   2662 C  C   . ALA   A  1 386 ? -13.543 13.269  11.409 1.00 24.29  ? 265  ALA   A C   1 
ATOM   2663 O  O   . ALA   A  1 386 ? -14.548 13.650  12.023 1.00 19.72  ? 265  ALA   A O   1 
ATOM   2664 C  CB  . ALA   A  1 386 ? -12.675 11.200  12.537 1.00 22.96  ? 265  ALA   A CB  1 
ATOM   2665 N  N   . PRO   A  1 387 ? -13.456 13.380  10.086 1.00 24.07  ? 266  PRO   A N   1 
ATOM   2666 C  CA  . PRO   A  1 387 ? -14.527 14.037  9.330  1.00 32.64  ? 266  PRO   A CA  1 
ATOM   2667 C  C   . PRO   A  1 387 ? -15.814 13.230  9.377  1.00 25.44  ? 266  PRO   A C   1 
ATOM   2668 O  O   . PRO   A  1 387 ? -15.821 12.024  9.637  1.00 26.00  ? 266  PRO   A O   1 
ATOM   2669 C  CB  . PRO   A  1 387 ? -13.970 14.115  7.904  1.00 23.29  ? 266  PRO   A CB  1 
ATOM   2670 C  CG  . PRO   A  1 387 ? -12.924 13.057  7.838  1.00 26.12  ? 266  PRO   A CG  1 
ATOM   2671 C  CD  . PRO   A  1 387 ? -12.357 12.918  9.220  1.00 30.25  ? 266  PRO   A CD  1 
ATOM   2672 N  N   . LEU   A  1 388 ? -16.922 13.929  9.118  1.00 28.47  ? 267  LEU   A N   1 
ATOM   2673 C  CA  . LEU   A  1 388 ? -18.240 13.318  9.264  1.00 27.17  ? 267  LEU   A CA  1 
ATOM   2674 C  C   . LEU   A  1 388 ? -18.419 12.137  8.317  1.00 26.95  ? 267  LEU   A C   1 
ATOM   2675 O  O   . LEU   A  1 388 ? -19.037 11.131  8.684  1.00 22.76  ? 267  LEU   A O   1 
ATOM   2676 C  CB  . LEU   A  1 388 ? -19.330 14.365  9.035  1.00 26.60  ? 267  LEU   A CB  1 
ATOM   2677 C  CG  . LEU   A  1 388 ? -20.785 13.900  9.134  1.00 32.30  ? 267  LEU   A CG  1 
ATOM   2678 C  CD1 . LEU   A  1 388 ? -21.044 13.189  10.454 1.00 39.07  ? 267  LEU   A CD1 1 
ATOM   2679 C  CD2 . LEU   A  1 388 ? -21.729 15.080  8.969  1.00 33.72  ? 267  LEU   A CD2 1 
ATOM   2680 N  N   . TRP   A  1 389 ? -17.882 12.235  7.096  1.00 24.75  ? 268  TRP   A N   1 
ATOM   2681 C  CA  . TRP   A  1 389 ? -18.024 11.132  6.150  1.00 28.29  ? 268  TRP   A CA  1 
ATOM   2682 C  C   . TRP   A  1 389 ? -17.329 9.876   6.658  1.00 21.79  ? 268  TRP   A C   1 
ATOM   2683 O  O   . TRP   A  1 389 ? -17.805 8.761   6.414  1.00 18.38  ? 268  TRP   A O   1 
ATOM   2684 C  CB  . TRP   A  1 389 ? -17.486 11.525  4.772  1.00 25.91  ? 268  TRP   A CB  1 
ATOM   2685 C  CG  . TRP   A  1 389 ? -16.005 11.751  4.706  1.00 27.74  ? 268  TRP   A CG  1 
ATOM   2686 C  CD1 . TRP   A  1 389 ? -15.351 12.944  4.812  1.00 28.49  ? 268  TRP   A CD1 1 
ATOM   2687 C  CD2 . TRP   A  1 389 ? -14.994 10.756  4.496  1.00 24.37  ? 268  TRP   A CD2 1 
ATOM   2688 N  NE1 . TRP   A  1 389 ? -13.996 12.753  4.688  1.00 29.11  ? 268  TRP   A NE1 1 
ATOM   2689 C  CE2 . TRP   A  1 389 ? -13.751 11.419  4.494  1.00 26.80  ? 268  TRP   A CE2 1 
ATOM   2690 C  CE3 . TRP   A  1 389 ? -15.020 9.370   4.315  1.00 34.38  ? 268  TRP   A CE3 1 
ATOM   2691 C  CZ2 . TRP   A  1 389 ? -12.545 10.743  4.318  1.00 24.54  ? 268  TRP   A CZ2 1 
ATOM   2692 C  CZ3 . TRP   A  1 389 ? -13.822 8.700   4.141  1.00 26.20  ? 268  TRP   A CZ3 1 
ATOM   2693 C  CH2 . TRP   A  1 389 ? -12.602 9.387   4.144  1.00 31.52  ? 268  TRP   A CH2 1 
ATOM   2694 N  N   . LEU   A  1 390 ? -16.215 10.036  7.378  1.00 17.42  ? 269  LEU   A N   1 
ATOM   2695 C  CA  . LEU   A  1 390 ? -15.489 8.887   7.907  1.00 19.39  ? 269  LEU   A CA  1 
ATOM   2696 C  C   . LEU   A  1 390 ? -16.215 8.317   9.116  1.00 21.93  ? 269  LEU   A C   1 
ATOM   2697 O  O   . LEU   A  1 390 ? -16.238 7.097   9.317  1.00 17.61  ? 269  LEU   A O   1 
ATOM   2698 C  CB  . LEU   A  1 390 ? -14.057 9.272   8.275  1.00 17.44  ? 269  LEU   A CB  1 
ATOM   2699 C  CG  . LEU   A  1 390 ? -13.183 8.133   8.812  1.00 24.93  ? 269  LEU   A CG  1 
ATOM   2700 C  CD1 . LEU   A  1 390 ? -13.040 7.017   7.786  1.00 24.09  ? 269  LEU   A CD1 1 
ATOM   2701 C  CD2 . LEU   A  1 390 ? -11.824 8.652   9.245  1.00 23.42  ? 269  LEU   A CD2 1 
ATOM   2702 N  N   . MET   A  1 391 ? -16.800 9.194   9.934  1.00 17.30  ? 270  MET   A N   1 
ATOM   2703 C  CA  . MET   A  1 391 ? -17.659 8.746   11.025 1.00 13.66  ? 270  MET   A CA  1 
ATOM   2704 C  C   . MET   A  1 391 ? -18.757 7.839   10.492 1.00 24.94  ? 270  MET   A C   1 
ATOM   2705 O  O   . MET   A  1 391 ? -19.025 6.773   11.057 1.00 20.02  ? 270  MET   A O   1 
ATOM   2706 C  CB  . MET   A  1 391 ? -18.233 9.947   11.772 1.00 19.10  ? 270  MET   A CB  1 
ATOM   2707 C  CG  . MET   A  1 391 ? -17.157 10.835  12.372 1.00 15.80  ? 270  MET   A CG  1 
ATOM   2708 S  SD  . MET   A  1 391 ? -16.020 9.985   13.499 1.00 23.43  ? 270  MET   A SD  1 
ATOM   2709 C  CE  . MET   A  1 391 ? -17.119 9.292   14.741 1.00 17.60  ? 270  MET   A CE  1 
ATOM   2710 N  N   . TYR   A  1 392 ? -19.401 8.241   9.392  1.00 19.05  ? 271  TYR   A N   1 
ATOM   2711 C  CA  . TYR   A  1 392 ? -20.544 7.473   8.920  1.00 20.81  ? 271  TYR   A CA  1 
ATOM   2712 C  C   . TYR   A  1 392 ? -20.090 6.184   8.254  1.00 18.83  ? 271  TYR   A C   1 
ATOM   2713 O  O   . TYR   A  1 392 ? -20.796 5.172   8.323  1.00 18.38  ? 271  TYR   A O   1 
ATOM   2714 C  CB  . TYR   A  1 392 ? -21.324 8.266   7.867  1.00 22.96  ? 271  TYR   A CB  1 
ATOM   2715 C  CG  . TYR   A  1 392 ? -22.224 9.393   8.316  1.00 31.42  ? 271  TYR   A CG  1 
ATOM   2716 C  CD1 . TYR   A  1 392 ? -22.803 9.412   9.575  1.00 34.63  ? 271  TYR   A CD1 1 
ATOM   2717 C  CD2 . TYR   A  1 392 ? -22.513 10.439  7.444  1.00 35.13  ? 271  TYR   A CD2 1 
ATOM   2718 C  CE1 . TYR   A  1 392 ? -23.638 10.454  9.958  1.00 37.59  ? 271  TYR   A CE1 1 
ATOM   2719 C  CE2 . TYR   A  1 392 ? -23.338 11.477  7.814  1.00 38.19  ? 271  TYR   A CE2 1 
ATOM   2720 C  CZ  . TYR   A  1 392 ? -23.900 11.482  9.071  1.00 44.73  ? 271  TYR   A CZ  1 
ATOM   2721 O  OH  . TYR   A  1 392 ? -24.722 12.523  9.437  1.00 58.85  ? 271  TYR   A OH  1 
ATOM   2722 N  N   . LEU   A  1 393 ? -18.911 6.192   7.625  1.00 14.18  ? 272  LEU   A N   1 
ATOM   2723 C  CA  . LEU   A  1 393 ? -18.329 4.953   7.117  1.00 21.04  ? 272  LEU   A CA  1 
ATOM   2724 C  C   . LEU   A  1 393 ? -18.036 3.971   8.243  1.00 19.27  ? 272  LEU   A C   1 
ATOM   2725 O  O   . LEU   A  1 393 ? -18.284 2.767   8.111  1.00 19.77  ? 272  LEU   A O   1 
ATOM   2726 C  CB  . LEU   A  1 393 ? -17.063 5.259   6.317  1.00 22.68  ? 272  LEU   A CB  1 
ATOM   2727 C  CG  . LEU   A  1 393 ? -16.376 4.052   5.680  1.00 31.83  ? 272  LEU   A CG  1 
ATOM   2728 C  CD1 . LEU   A  1 393 ? -17.301 3.384   4.677  1.00 32.70  ? 272  LEU   A CD1 1 
ATOM   2729 C  CD2 . LEU   A  1 393 ? -15.080 4.474   5.012  1.00 27.96  ? 272  LEU   A CD2 1 
ATOM   2730 N  N   . ALA   A  1 394 ? -17.505 4.468   9.362  1.00 20.48  ? 273  ALA   A N   1 
ATOM   2731 C  CA  . ALA   A  1 394 ? -17.188 3.590   10.482 1.00 16.90  ? 273  ALA   A CA  1 
ATOM   2732 C  C   . ALA   A  1 394 ? -18.448 3.053   11.143 1.00 16.45  ? 273  ALA   A C   1 
ATOM   2733 O  O   . ALA   A  1 394 ? -18.459 1.914   11.622 1.00 16.59  ? 273  ALA   A O   1 
ATOM   2734 C  CB  . ALA   A  1 394 ? -16.324 4.327   11.504 1.00 14.66  ? 273  ALA   A CB  1 
ATOM   2735 N  N   . ILE   A  1 395 ? -19.512 3.856   11.174 1.00 14.62  ? 274  ILE   A N   1 
ATOM   2736 C  CA  . ILE   A  1 395 ? -20.782 3.399   11.731 1.00 17.36  ? 274  ILE   A CA  1 
ATOM   2737 C  C   . ILE   A  1 395 ? -21.395 2.308   10.861 1.00 15.17  ? 274  ILE   A C   1 
ATOM   2738 O  O   . ILE   A  1 395 ? -21.791 1.249   11.362 1.00 17.19  ? 274  ILE   A O   1 
ATOM   2739 C  CB  . ILE   A  1 395 ? -21.739 4.589   11.913 1.00 20.28  ? 274  ILE   A CB  1 
ATOM   2740 C  CG1 . ILE   A  1 395 ? -21.231 5.499   13.035 1.00 14.50  ? 274  ILE   A CG1 1 
ATOM   2741 C  CG2 . ILE   A  1 395 ? -23.149 4.104   12.203 1.00 21.73  ? 274  ILE   A CG2 1 
ATOM   2742 C  CD1 . ILE   A  1 395 ? -21.824 6.886   13.011 1.00 17.62  ? 274  ILE   A CD1 1 
ATOM   2743 N  N   . VAL   A  1 396 ? -21.486 2.542   9.547  1.00 11.88  ? 275  VAL   A N   1 
ATOM   2744 C  CA  . VAL   A  1 396 ? -22.083 1.527   8.682  1.00 24.21  ? 275  VAL   A CA  1 
ATOM   2745 C  C   . VAL   A  1 396 ? -21.236 0.262   8.671  1.00 16.90  ? 275  VAL   A C   1 
ATOM   2746 O  O   . VAL   A  1 396 ? -21.775 -0.848  8.598  1.00 20.02  ? 275  VAL   A O   1 
ATOM   2747 C  CB  . VAL   A  1 396 ? -22.320 2.071   7.254  1.00 28.44  ? 275  VAL   A CB  1 
ATOM   2748 C  CG1 . VAL   A  1 396 ? -23.131 3.357   7.298  1.00 19.30  ? 275  VAL   A CG1 1 
ATOM   2749 C  CG2 . VAL   A  1 396 ? -21.008 2.282   6.511  1.00 24.66  ? 275  VAL   A CG2 1 
ATOM   2750 N  N   . LEU   A  1 397 ? -19.909 0.398   8.770  1.00 16.31  ? 276  LEU   A N   1 
ATOM   2751 C  CA  A LEU   A  1 397 ? -19.055 -0.785  8.819  0.67 17.91  ? 276  LEU   A CA  1 
ATOM   2752 C  CA  B LEU   A  1 397 ? -19.050 -0.781  8.822  0.33 17.44  ? 276  LEU   A CA  1 
ATOM   2753 C  C   . LEU   A  1 397 ? -19.366 -1.637  10.042 1.00 19.36  ? 276  LEU   A C   1 
ATOM   2754 O  O   . LEU   A  1 397 ? -19.447 -2.867  9.945  1.00 17.50  ? 276  LEU   A O   1 
ATOM   2755 C  CB  A LEU   A  1 397 ? -17.582 -0.379  8.811  0.67 17.97  ? 276  LEU   A CB  1 
ATOM   2756 C  CB  B LEU   A  1 397 ? -17.579 -0.362  8.829  0.33 18.13  ? 276  LEU   A CB  1 
ATOM   2757 C  CG  A LEU   A  1 397 ? -16.598 -1.540  8.984  0.67 17.86  ? 276  LEU   A CG  1 
ATOM   2758 C  CG  B LEU   A  1 397 ? -16.897 -0.193  7.470  0.33 16.13  ? 276  LEU   A CG  1 
ATOM   2759 C  CD1 A LEU   A  1 397 ? -16.748 -2.547  7.852  0.67 16.54  ? 276  LEU   A CD1 1 
ATOM   2760 C  CD1 B LEU   A  1 397 ? -15.751 0.803   7.562  0.33 17.29  ? 276  LEU   A CD1 1 
ATOM   2761 C  CD2 A LEU   A  1 397 ? -15.168 -1.036  9.069  0.67 20.28  ? 276  LEU   A CD2 1 
ATOM   2762 C  CD2 B LEU   A  1 397 ? -16.404 -1.534  6.946  0.33 16.28  ? 276  LEU   A CD2 1 
ATOM   2763 N  N   . SER   A  1 398 ? -19.545 -1.001  11.202 1.00 15.50  ? 277  SER   A N   1 
ATOM   2764 C  CA  . SER   A  1 398 ? -19.911 -1.749  12.398 1.00 21.94  ? 277  SER   A CA  1 
ATOM   2765 C  C   . SER   A  1 398 ? -21.275 -2.407  12.241 1.00 16.49  ? 277  SER   A C   1 
ATOM   2766 O  O   . SER   A  1 398 ? -21.506 -3.495  12.782 1.00 20.68  ? 277  SER   A O   1 
ATOM   2767 C  CB  . SER   A  1 398 ? -19.890 -0.828  13.619 1.00 18.83  ? 277  SER   A CB  1 
ATOM   2768 O  OG  . SER   A  1 398 ? -21.062 -0.035  13.687 1.00 16.84  ? 277  SER   A OG  1 
ATOM   2769 N  N   . HIS   A  1 399 ? -22.183 -1.776  11.491 1.00 15.92  ? 278  HIS   A N   1 
ATOM   2770 C  CA  . HIS   A  1 399 ? -23.487 -2.383  11.244 1.00 15.51  ? 278  HIS   A CA  1 
ATOM   2771 C  C   . HIS   A  1 399 ? -23.400 -3.532  10.247 1.00 17.22  ? 278  HIS   A C   1 
ATOM   2772 O  O   . HIS   A  1 399 ? -24.210 -4.464  10.312 1.00 15.84  ? 278  HIS   A O   1 
ATOM   2773 C  CB  . HIS   A  1 399 ? -24.479 -1.326  10.754 1.00 20.93  ? 278  HIS   A CB  1 
ATOM   2774 C  CG  . HIS   A  1 399 ? -24.838 -0.308  11.791 1.00 20.60  ? 278  HIS   A CG  1 
ATOM   2775 N  ND1 . HIS   A  1 399 ? -25.411 0.906   11.476 1.00 25.81  ? 278  HIS   A ND1 1 
ATOM   2776 C  CD2 . HIS   A  1 399 ? -24.710 -0.325  13.139 1.00 19.59  ? 278  HIS   A CD2 1 
ATOM   2777 C  CE1 . HIS   A  1 399 ? -25.619 1.593   12.586 1.00 28.14  ? 278  HIS   A CE1 1 
ATOM   2778 N  NE2 . HIS   A  1 399 ? -25.202 0.868   13.609 1.00 19.78  ? 278  HIS   A NE2 1 
ATOM   2779 N  N   A THR   A  1 400 ? -22.432 -3.480  9.329  0.50 19.94  ? 279  THR   A N   1 
ATOM   2780 N  N   B THR   A  1 400 ? -22.440 -3.492  9.316  0.50 19.95  ? 279  THR   A N   1 
ATOM   2781 C  CA  A THR   A  1 400 ? -22.240 -4.551  8.358  0.50 20.73  ? 279  THR   A CA  1 
ATOM   2782 C  CA  B THR   A  1 400 ? -22.309 -4.590  8.360  0.50 20.66  ? 279  THR   A CA  1 
ATOM   2783 C  C   A THR   A  1 400 ? -21.929 -5.884  9.030  0.50 20.50  ? 279  THR   A C   1 
ATOM   2784 C  C   B THR   A  1 400 ? -21.931 -5.902  9.030  0.50 20.50  ? 279  THR   A C   1 
ATOM   2785 O  O   A THR   A  1 400 ? -22.199 -6.940  8.446  0.50 21.74  ? 279  THR   A O   1 
ATOM   2786 O  O   B THR   A  1 400 ? -22.123 -6.964  8.428  0.50 21.69  ? 279  THR   A O   1 
ATOM   2787 C  CB  A THR   A  1 400 ? -21.121 -4.159  7.385  0.50 23.07  ? 279  THR   A CB  1 
ATOM   2788 C  CB  B THR   A  1 400 ? -21.272 -4.271  7.279  0.50 22.94  ? 279  THR   A CB  1 
ATOM   2789 O  OG1 A THR   A  1 400 ? -21.430 -2.891  6.791  0.50 17.82  ? 279  THR   A OG1 1 
ATOM   2790 O  OG1 B THR   A  1 400 ? -19.987 -4.071  7.882  0.50 15.99  ? 279  THR   A OG1 1 
ATOM   2791 C  CG2 A THR   A  1 400 ? -20.958 -5.194  6.284  0.50 18.46  ? 279  THR   A CG2 1 
ATOM   2792 C  CG2 B THR   A  1 400 ? -21.672 -3.043  6.478  0.50 17.91  ? 279  THR   A CG2 1 
ATOM   2793 N  N   . ASN   A  1 401 ? -21.390 -5.859  10.252 1.00 18.12  ? 280  ASN   A N   1 
ATOM   2794 C  CA  . ASN   A  1 401 ? -21.092 -7.100  10.960 1.00 24.14  ? 280  ASN   A CA  1 
ATOM   2795 C  C   . ASN   A  1 401 ? -22.350 -7.916  11.216 1.00 22.48  ? 280  ASN   A C   1 
ATOM   2796 O  O   . ASN   A  1 401 ? -22.285 -9.148  11.293 1.00 23.24  ? 280  ASN   A O   1 
ATOM   2797 C  CB  . ASN   A  1 401 ? -20.386 -6.803  12.282 1.00 23.35  ? 280  ASN   A CB  1 
ATOM   2798 C  CG  . ASN   A  1 401 ? -19.974 -8.066  13.013 1.00 29.05  ? 280  ASN   A CG  1 
ATOM   2799 O  OD1 . ASN   A  1 401 ? -20.486 -8.366  14.092 1.00 28.13  ? 280  ASN   A OD1 1 
ATOM   2800 N  ND2 . ASN   A  1 401 ? -19.061 -8.824  12.418 1.00 24.51  ? 280  ASN   A ND2 1 
ATOM   2801 N  N   . SER   A  1 402 ? -23.500 -7.257  11.347 1.00 15.45  ? 281  SER   A N   1 
ATOM   2802 C  CA  . SER   A  1 402 ? -24.735 -7.996  11.563 1.00 30.52  ? 281  SER   A CA  1 
ATOM   2803 C  C   . SER   A  1 402 ? -25.228 -8.692  10.301 1.00 23.38  ? 281  SER   A C   1 
ATOM   2804 O  O   . SER   A  1 402 ? -26.230 -9.412  10.365 1.00 24.93  ? 281  SER   A O   1 
ATOM   2805 C  CB  . SER   A  1 402 ? -25.817 -7.049  12.088 1.00 21.70  ? 281  SER   A CB  1 
ATOM   2806 O  OG  . SER   A  1 402 ? -25.496 -6.574  13.385 1.00 31.69  ? 281  SER   A OG  1 
ATOM   2807 N  N   . VAL   A  1 403 ? -24.559 -8.490  9.166  1.00 24.78  ? 282  VAL   A N   1 
ATOM   2808 C  CA  . VAL   A  1 403 ? -24.921 -9.135  7.908  1.00 25.43  ? 282  VAL   A CA  1 
ATOM   2809 C  C   . VAL   A  1 403 ? -24.087 -10.393 7.675  1.00 26.94  ? 282  VAL   A C   1 
ATOM   2810 O  O   . VAL   A  1 403 ? -24.547 -11.346 7.036  1.00 26.69  ? 282  VAL   A O   1 
ATOM   2811 C  CB  . VAL   A  1 403 ? -24.775 -8.142  6.737  1.00 25.12  ? 282  VAL   A CB  1 
ATOM   2812 C  CG1 . VAL   A  1 403 ? -25.085 -8.809  5.403  1.00 19.29  ? 282  VAL   A CG1 1 
ATOM   2813 C  CG2 . VAL   A  1 403 ? -25.674 -6.933  6.955  1.00 19.55  ? 282  VAL   A CG2 1 
ATOM   2814 N  N   . VAL   A  1 404 ? -22.865 -10.422 8.215  1.00 19.34  ? 283  VAL   A N   1 
ATOM   2815 C  CA  . VAL   A  1 404 ? -21.846 -11.306 7.651  1.00 24.91  ? 283  VAL   A CA  1 
ATOM   2816 C  C   . VAL   A  1 404 ? -21.939 -12.740 8.176  1.00 28.99  ? 283  VAL   A C   1 
ATOM   2817 O  O   . VAL   A  1 404 ? -21.611 -13.682 7.444  1.00 25.87  ? 283  VAL   A O   1 
ATOM   2818 C  CB  . VAL   A  1 404 ? -20.439 -10.730 7.898  1.00 24.98  ? 283  VAL   A CB  1 
ATOM   2819 C  CG1 . VAL   A  1 404 ? -20.300 -9.362  7.254  1.00 29.54  ? 283  VAL   A CG1 1 
ATOM   2820 C  CG2 . VAL   A  1 404 ? -20.129 -10.663 9.388  1.00 20.97  ? 283  VAL   A CG2 1 
ATOM   2821 N  N   . ASN   A  1 405 ? -22.357 -12.942 9.429  1.00 18.98  ? 284  ASN   A N   1 
ATOM   2822 C  CA  . ASN   A  1 405 ? -22.350 -14.293 9.993  1.00 30.10  ? 284  ASN   A CA  1 
ATOM   2823 C  C   . ASN   A  1 405 ? -23.148 -15.307 9.179  1.00 30.02  ? 284  ASN   A C   1 
ATOM   2824 O  O   . ASN   A  1 405 ? -22.637 -16.421 8.965  1.00 31.29  ? 284  ASN   A O   1 
ATOM   2825 C  CB  . ASN   A  1 405 ? -22.824 -14.254 11.450 1.00 21.79  ? 284  ASN   A CB  1 
ATOM   2826 C  CG  . ASN   A  1 405 ? -21.899 -13.447 12.341 1.00 41.42  ? 284  ASN   A CG  1 
ATOM   2827 O  OD1 . ASN   A  1 405 ? -20.811 -13.049 11.925 1.00 30.99  ? 284  ASN   A OD1 1 
ATOM   2828 N  ND2 . ASN   A  1 405 ? -22.324 -13.210 13.576 1.00 40.09  ? 284  ASN   A ND2 1 
ATOM   2829 N  N   . PRO   A  1 406 ? -24.379 -15.028 8.725  1.00 23.59  ? 285  PRO   A N   1 
ATOM   2830 C  CA  . PRO   A  1 406 ? -25.084 -16.020 7.891  1.00 27.47  ? 285  PRO   A CA  1 
ATOM   2831 C  C   . PRO   A  1 406 ? -24.289 -16.499 6.687  1.00 32.30  ? 285  PRO   A C   1 
ATOM   2832 O  O   . PRO   A  1 406 ? -24.417 -17.667 6.295  1.00 30.48  ? 285  PRO   A O   1 
ATOM   2833 C  CB  . PRO   A  1 406 ? -26.355 -15.271 7.468  1.00 19.64  ? 285  PRO   A CB  1 
ATOM   2834 C  CG  . PRO   A  1 406 ? -26.598 -14.322 8.580  1.00 24.30  ? 285  PRO   A CG  1 
ATOM   2835 C  CD  . PRO   A  1 406 ? -25.235 -13.859 9.004  1.00 24.82  ? 285  PRO   A CD  1 
ATOM   2836 N  N   . PHE   A  1 407 ? -23.471 -15.633 6.086  1.00 26.09  ? 286  PHE   A N   1 
ATOM   2837 C  CA  . PHE   A  1 407 ? -22.642 -16.054 4.960  1.00 32.37  ? 286  PHE   A CA  1 
ATOM   2838 C  C   . PHE   A  1 407 ? -21.522 -16.981 5.411  1.00 34.99  ? 286  PHE   A C   1 
ATOM   2839 O  O   . PHE   A  1 407 ? -21.186 -17.943 4.711  1.00 37.50  ? 286  PHE   A O   1 
ATOM   2840 C  CB  . PHE   A  1 407 ? -22.079 -14.835 4.234  1.00 30.51  ? 286  PHE   A CB  1 
ATOM   2841 C  CG  . PHE   A  1 407 ? -23.094 -14.111 3.406  1.00 37.12  ? 286  PHE   A CG  1 
ATOM   2842 C  CD1 . PHE   A  1 407 ? -23.296 -14.457 2.080  1.00 38.07  ? 286  PHE   A CD1 1 
ATOM   2843 C  CD2 . PHE   A  1 407 ? -23.859 -13.096 3.954  1.00 32.77  ? 286  PHE   A CD2 1 
ATOM   2844 C  CE1 . PHE   A  1 407 ? -24.234 -13.797 1.313  1.00 43.87  ? 286  PHE   A CE1 1 
ATOM   2845 C  CE2 . PHE   A  1 407 ? -24.799 -12.433 3.192  1.00 41.95  ? 286  PHE   A CE2 1 
ATOM   2846 C  CZ  . PHE   A  1 407 ? -24.988 -12.785 1.870  1.00 42.85  ? 286  PHE   A CZ  1 
ATOM   2847 N  N   . ILE   A  1 408 ? -20.922 -16.699 6.569  1.00 30.22  ? 287  ILE   A N   1 
ATOM   2848 C  CA  . ILE   A  1 408 ? -19.864 -17.562 7.085  1.00 32.77  ? 287  ILE   A CA  1 
ATOM   2849 C  C   . ILE   A  1 408 ? -20.411 -18.954 7.370  1.00 31.71  ? 287  ILE   A C   1 
ATOM   2850 O  O   . ILE   A  1 408 ? -19.766 -19.964 7.065  1.00 34.42  ? 287  ILE   A O   1 
ATOM   2851 C  CB  . ILE   A  1 408 ? -19.213 -16.930 8.328  1.00 35.88  ? 287  ILE   A CB  1 
ATOM   2852 C  CG1 . ILE   A  1 408 ? -18.752 -15.507 8.008  1.00 29.75  ? 287  ILE   A CG1 1 
ATOM   2853 C  CG2 . ILE   A  1 408 ? -18.035 -17.768 8.795  1.00 30.31  ? 287  ILE   A CG2 1 
ATOM   2854 C  CD1 . ILE   A  1 408 ? -17.709 -15.436 6.910  1.00 37.35  ? 287  ILE   A CD1 1 
ATOM   2855 N  N   . TYR   A  1 409 ? -21.608 -19.034 7.960  1.00 28.85  ? 288  TYR   A N   1 
ATOM   2856 C  CA  . TYR   A  1 409 ? -22.210 -20.338 8.214  1.00 38.74  ? 288  TYR   A CA  1 
ATOM   2857 C  C   . TYR   A  1 409 ? -22.508 -21.065 6.910  1.00 33.13  ? 288  TYR   A C   1 
ATOM   2858 O  O   . TYR   A  1 409 ? -22.293 -22.278 6.804  1.00 31.62  ? 288  TYR   A O   1 
ATOM   2859 C  CB  . TYR   A  1 409 ? -23.501 -20.184 9.022  1.00 25.03  ? 288  TYR   A CB  1 
ATOM   2860 C  CG  . TYR   A  1 409 ? -23.360 -19.469 10.343 1.00 29.64  ? 288  TYR   A CG  1 
ATOM   2861 C  CD1 . TYR   A  1 409 ? -22.326 -19.774 11.213 1.00 38.76  ? 288  TYR   A CD1 1 
ATOM   2862 C  CD2 . TYR   A  1 409 ? -24.258 -18.476 10.713 1.00 32.67  ? 288  TYR   A CD2 1 
ATOM   2863 C  CE1 . TYR   A  1 409 ? -22.208 -19.134 12.428 1.00 40.70  ? 288  TYR   A CE1 1 
ATOM   2864 C  CE2 . TYR   A  1 409 ? -24.135 -17.815 11.918 1.00 25.74  ? 288  TYR   A CE2 1 
ATOM   2865 C  CZ  . TYR   A  1 409 ? -23.107 -18.147 12.772 1.00 38.38  ? 288  TYR   A CZ  1 
ATOM   2866 O  OH  . TYR   A  1 409 ? -22.975 -17.491 13.974 1.00 31.33  ? 288  TYR   A OH  1 
ATOM   2867 N  N   . ALA   A  1 410 ? -23.012 -20.340 5.907  1.00 28.47  ? 289  ALA   A N   1 
ATOM   2868 C  CA  . ALA   A  1 410 ? -23.361 -20.981 4.643  1.00 35.70  ? 289  ALA   A CA  1 
ATOM   2869 C  C   . ALA   A  1 410 ? -22.129 -21.528 3.931  1.00 40.59  ? 289  ALA   A C   1 
ATOM   2870 O  O   . ALA   A  1 410 ? -22.157 -22.647 3.408  1.00 36.77  ? 289  ALA   A O   1 
ATOM   2871 C  CB  . ALA   A  1 410 ? -24.109 -19.995 3.747  1.00 26.54  ? 289  ALA   A CB  1 
ATOM   2872 N  N   . TYR   A  1 411 ? -21.034 -20.766 3.905  1.00 40.93  ? 290  TYR   A N   1 
ATOM   2873 C  CA  . TYR   A  1 411 ? -19.853 -21.217 3.177  1.00 44.27  ? 290  TYR   A CA  1 
ATOM   2874 C  C   . TYR   A  1 411 ? -19.013 -22.222 3.950  1.00 44.80  ? 290  TYR   A C   1 
ATOM   2875 O  O   . TYR   A  1 411 ? -18.247 -22.966 3.328  1.00 39.86  ? 290  TYR   A O   1 
ATOM   2876 C  CB  . TYR   A  1 411 ? -18.953 -20.046 2.771  1.00 39.06  ? 290  TYR   A CB  1 
ATOM   2877 C  CG  . TYR   A  1 411 ? -19.351 -19.347 1.491  1.00 61.58  ? 290  TYR   A CG  1 
ATOM   2878 C  CD1 . TYR   A  1 411 ? -19.152 -19.962 0.259  1.00 73.31  ? 290  TYR   A CD1 1 
ATOM   2879 C  CD2 . TYR   A  1 411 ? -19.863 -18.058 1.504  1.00 60.16  ? 290  TYR   A CD2 1 
ATOM   2880 C  CE1 . TYR   A  1 411 ? -19.487 -19.330 -0.920 1.00 67.96  ? 290  TYR   A CE1 1 
ATOM   2881 C  CE2 . TYR   A  1 411 ? -20.201 -17.414 0.325  1.00 79.64  ? 290  TYR   A CE2 1 
ATOM   2882 C  CZ  . TYR   A  1 411 ? -20.010 -18.057 -0.883 1.00 77.95  ? 290  TYR   A CZ  1 
ATOM   2883 O  OH  . TYR   A  1 411 ? -20.345 -17.431 -2.061 1.00 79.61  ? 290  TYR   A OH  1 
ATOM   2884 N  N   . ARG   A  1 412 ? -19.130 -22.270 5.276  1.00 41.94  ? 291  ARG   A N   1 
ATOM   2885 C  CA  . ARG   A  1 412 ? -18.200 -23.052 6.075  1.00 41.38  ? 291  ARG   A CA  1 
ATOM   2886 C  C   . ARG   A  1 412 ? -18.825 -24.221 6.821  1.00 35.37  ? 291  ARG   A C   1 
ATOM   2887 O  O   . ARG   A  1 412 ? -18.080 -25.095 7.279  1.00 40.40  ? 291  ARG   A O   1 
ATOM   2888 C  CB  . ARG   A  1 412 ? -17.482 -22.146 7.090  1.00 32.75  ? 291  ARG   A CB  1 
ATOM   2889 C  CG  . ARG   A  1 412 ? -16.515 -21.165 6.440  1.00 32.83  ? 291  ARG   A CG  1 
ATOM   2890 C  CD  . ARG   A  1 412 ? -15.439 -20.687 7.399  1.00 33.70  ? 291  ARG   A CD  1 
ATOM   2891 N  NE  . ARG   A  1 412 ? -14.779 -21.793 8.080  1.00 46.85  ? 291  ARG   A NE  1 
ATOM   2892 C  CZ  . ARG   A  1 412 ? -13.586 -22.266 7.747  1.00 52.11  ? 291  ARG   A CZ  1 
ATOM   2893 N  NH1 . ARG   A  1 412 ? -12.895 -21.753 6.742  1.00 40.07  ? 291  ARG   A NH1 1 
ATOM   2894 N  NH2 . ARG   A  1 412 ? -13.073 -23.279 8.440  1.00 43.16  ? 291  ARG   A NH2 1 
ATOM   2895 N  N   . ILE   A  1 413 ? -20.148 -24.277 6.955  1.00 33.63  ? 292  ILE   A N   1 
ATOM   2896 C  CA  . ILE   A  1 413 ? -20.811 -25.310 7.748  1.00 34.95  ? 292  ILE   A CA  1 
ATOM   2897 C  C   . ILE   A  1 413 ? -21.857 -25.955 6.847  1.00 41.69  ? 292  ILE   A C   1 
ATOM   2898 O  O   . ILE   A  1 413 ? -22.913 -25.367 6.584  1.00 33.98  ? 292  ILE   A O   1 
ATOM   2899 C  CB  . ILE   A  1 413 ? -21.446 -24.754 9.027  1.00 30.43  ? 292  ILE   A CB  1 
ATOM   2900 C  CG1 . ILE   A  1 413 ? -20.454 -23.855 9.768  1.00 45.11  ? 292  ILE   A CG1 1 
ATOM   2901 C  CG2 . ILE   A  1 413 ? -21.905 -25.891 9.926  1.00 30.98  ? 292  ILE   A CG2 1 
ATOM   2902 C  CD1 . ILE   A  1 413 ? -20.971 -23.322 11.086 1.00 32.31  ? 292  ILE   A CD1 1 
ATOM   2903 N  N   . ARG   A  1 414 ? -21.554 -27.162 6.363  1.00 34.79  ? 293  ARG   A N   1 
ATOM   2904 C  CA  . ARG   A  1 414 ? -22.428 -27.873 5.431  1.00 41.69  ? 293  ARG   A CA  1 
ATOM   2905 C  C   . ARG   A  1 414 ? -23.854 -28.013 5.956  1.00 32.36  ? 293  ARG   A C   1 
ATOM   2906 O  O   . ARG   A  1 414 ? -24.818 -27.846 5.200  1.00 38.91  ? 293  ARG   A O   1 
ATOM   2907 C  CB  . ARG   A  1 414 ? -21.808 -29.226 5.085  1.00 49.60  ? 293  ARG   A CB  1 
ATOM   2908 C  CG  . ARG   A  1 414 ? -22.539 -30.011 4.012  1.00 55.13  ? 293  ARG   A CG  1 
ATOM   2909 C  CD  . ARG   A  1 414 ? -21.895 -31.375 3.844  1.00 54.51  ? 293  ARG   A CD  1 
ATOM   2910 N  NE  . ARG   A  1 414 ? -20.572 -31.233 3.245  1.00 73.14  ? 293  ARG   A NE  1 
ATOM   2911 C  CZ  . ARG   A  1 414 ? -19.427 -31.402 3.894  1.00 68.62  ? 293  ARG   A CZ  1 
ATOM   2912 N  NH1 . ARG   A  1 414 ? -19.400 -31.728 5.175  1.00 63.31  ? 293  ARG   A NH1 1 
ATOM   2913 N  NH2 . ARG   A  1 414 ? -18.281 -31.224 3.243  1.00 67.70  ? 293  ARG   A NH2 1 
ATOM   2914 N  N   . GLU   A  1 415 ? -24.012 -28.337 7.245  1.00 37.34  ? 294  GLU   A N   1 
ATOM   2915 C  CA  . GLU   A  1 415 ? -25.351 -28.565 7.787  1.00 41.83  ? 294  GLU   A CA  1 
ATOM   2916 C  C   . GLU   A  1 415 ? -26.198 -27.301 7.707  1.00 38.64  ? 294  GLU   A C   1 
ATOM   2917 O  O   . GLU   A  1 415 ? -27.412 -27.371 7.479  1.00 37.56  ? 294  GLU   A O   1 
ATOM   2918 C  CB  . GLU   A  1 415 ? -25.263 -29.067 9.229  1.00 37.76  ? 294  GLU   A CB  1 
ATOM   2919 C  CG  . GLU   A  1 415 ? -26.542 -29.726 9.731  1.00 48.67  ? 294  GLU   A CG  1 
ATOM   2920 C  CD  . GLU   A  1 415 ? -26.831 -31.052 9.053  1.00 68.50  ? 294  GLU   A CD  1 
ATOM   2921 O  OE1 . GLU   A  1 415 ? -25.874 -31.802 8.768  1.00 61.83  ? 294  GLU   A OE1 1 
ATOM   2922 O  OE2 . GLU   A  1 415 ? -28.021 -31.343 8.805  1.00 55.52  ? 294  GLU   A OE2 1 
ATOM   2923 N  N   . PHE   A  1 416 ? -25.578 -26.136 7.899  1.00 38.13  ? 295  PHE   A N   1 
ATOM   2924 C  CA  . PHE   A  1 416 ? -26.290 -24.879 7.697  1.00 36.53  ? 295  PHE   A CA  1 
ATOM   2925 C  C   . PHE   A  1 416 ? -26.596 -24.663 6.218  1.00 28.20  ? 295  PHE   A C   1 
ATOM   2926 O  O   . PHE   A  1 416 ? -27.738 -24.363 5.848  1.00 35.22  ? 295  PHE   A O   1 
ATOM   2927 C  CB  . PHE   A  1 416 ? -25.485 -23.712 8.272  1.00 29.81  ? 295  PHE   A CB  1 
ATOM   2928 C  CG  . PHE   A  1 416 ? -25.853 -23.364 9.691  1.00 30.58  ? 295  PHE   A CG  1 
ATOM   2929 C  CD1 . PHE   A  1 416 ? -27.100 -22.834 9.985  1.00 31.17  ? 295  PHE   A CD1 1 
ATOM   2930 C  CD2 . PHE   A  1 416 ? -24.957 -23.566 10.729 1.00 28.26  ? 295  PHE   A CD2 1 
ATOM   2931 C  CE1 . PHE   A  1 416 ? -27.446 -22.512 11.286 1.00 26.77  ? 295  PHE   A CE1 1 
ATOM   2932 C  CE2 . PHE   A  1 416 ? -25.298 -23.245 12.034 1.00 31.37  ? 295  PHE   A CE2 1 
ATOM   2933 C  CZ  . PHE   A  1 416 ? -26.545 -22.717 12.311 1.00 28.07  ? 295  PHE   A CZ  1 
ATOM   2934 N  N   . ARG   A  1 417 ? -25.575 -24.791 5.364  1.00 26.69  ? 296  ARG   A N   1 
ATOM   2935 C  CA  . ARG   A  1 417 ? -25.735 -24.545 3.932  1.00 33.80  ? 296  ARG   A CA  1 
ATOM   2936 C  C   . ARG   A  1 417 ? -26.860 -25.386 3.346  1.00 37.47  ? 296  ARG   A C   1 
ATOM   2937 O  O   . ARG   A  1 417 ? -27.650 -24.903 2.528  1.00 42.65  ? 296  ARG   A O   1 
ATOM   2938 C  CB  . ARG   A  1 417 ? -24.415 -24.838 3.218  1.00 36.06  ? 296  ARG   A CB  1 
ATOM   2939 C  CG  . ARG   A  1 417 ? -24.427 -24.646 1.715  1.00 40.48  ? 296  ARG   A CG  1 
ATOM   2940 C  CD  . ARG   A  1 417 ? -23.010 -24.685 1.149  1.00 35.52  ? 296  ARG   A CD  1 
ATOM   2941 N  NE  . ARG   A  1 417 ? -22.338 -25.965 1.344  1.00 39.62  ? 296  ARG   A NE  1 
ATOM   2942 C  CZ  . ARG   A  1 417 ? -21.373 -26.171 2.231  1.00 39.70  ? 296  ARG   A CZ  1 
ATOM   2943 N  NH1 . ARG   A  1 417 ? -20.946 -25.203 3.026  1.00 42.17  ? 296  ARG   A NH1 1 
ATOM   2944 N  NH2 . ARG   A  1 417 ? -20.821 -27.378 2.323  1.00 43.26  ? 296  ARG   A NH2 1 
ATOM   2945 N  N   . GLN   A  1 418 ? -26.945 -26.649 3.756  1.00 32.46  ? 297  GLN   A N   1 
ATOM   2946 C  CA  . GLN   A  1 418 ? -27.984 -27.530 3.246  1.00 40.86  ? 297  GLN   A CA  1 
ATOM   2947 C  C   . GLN   A  1 418 ? -29.353 -27.130 3.784  1.00 39.58  ? 297  GLN   A C   1 
ATOM   2948 O  O   . GLN   A  1 418 ? -30.356 -27.211 3.065  1.00 35.29  ? 297  GLN   A O   1 
ATOM   2949 C  CB  . GLN   A  1 418 ? -27.659 -28.980 3.599  1.00 31.25  ? 297  GLN   A CB  1 
ATOM   2950 C  CG  . GLN   A  1 418 ? -26.497 -29.538 2.816  1.00 52.46  ? 297  GLN   A CG  1 
ATOM   2951 C  CD  . GLN   A  1 418 ? -26.072 -30.924 3.268  1.00 64.67  ? 297  GLN   A CD  1 
ATOM   2952 O  OE1 . GLN   A  1 418 ? -25.775 -31.782 2.439  1.00 74.12  ? 297  GLN   A OE1 1 
ATOM   2953 N  NE2 . GLN   A  1 418 ? -25.975 -31.128 4.588  1.00 67.00  ? 297  GLN   A NE2 1 
ATOM   2954 N  N   . THR   A  1 419 ? -29.418 -26.704 5.049  1.00 36.00  ? 298  THR   A N   1 
ATOM   2955 C  CA  . THR   A  1 419 ? -30.691 -26.267 5.616  1.00 32.98  ? 298  THR   A CA  1 
ATOM   2956 C  C   . THR   A  1 419 ? -31.141 -24.951 4.989  1.00 36.17  ? 298  THR   A C   1 
ATOM   2957 O  O   . THR   A  1 419 ? -32.332 -24.763 4.713  1.00 34.27  ? 298  THR   A O   1 
ATOM   2958 C  CB  . THR   A  1 419 ? -30.573 -26.130 7.135  1.00 29.92  ? 298  THR   A CB  1 
ATOM   2959 O  OG1 . THR   A  1 419 ? -30.008 -27.327 7.681  1.00 33.46  ? 298  THR   A OG1 1 
ATOM   2960 C  CG2 . THR   A  1 419 ? -31.943 -25.900 7.754  1.00 28.43  ? 298  THR   A CG2 1 
ATOM   2961 N  N   . PHE   A  1 420 ? -30.203 -24.022 4.777  1.00 32.11  ? 299  PHE   A N   1 
ATOM   2962 C  CA  . PHE   A  1 420 ? -30.516 -22.804 4.035  1.00 43.38  ? 299  PHE   A CA  1 
ATOM   2963 C  C   . PHE   A  1 420 ? -31.119 -23.138 2.676  1.00 43.71  ? 299  PHE   A C   1 
ATOM   2964 O  O   . PHE   A  1 420 ? -32.118 -22.541 2.260  1.00 45.79  ? 299  PHE   A O   1 
ATOM   2965 C  CB  . PHE   A  1 420 ? -29.262 -21.943 3.856  1.00 32.70  ? 299  PHE   A CB  1 
ATOM   2966 C  CG  . PHE   A  1 420 ? -28.743 -21.333 5.130  1.00 43.14  ? 299  PHE   A CG  1 
ATOM   2967 C  CD1 . PHE   A  1 420 ? -29.507 -21.338 6.286  1.00 34.46  ? 299  PHE   A CD1 1 
ATOM   2968 C  CD2 . PHE   A  1 420 ? -27.492 -20.737 5.163  1.00 29.43  ? 299  PHE   A CD2 1 
ATOM   2969 C  CE1 . PHE   A  1 420 ? -29.027 -20.771 7.453  1.00 30.99  ? 299  PHE   A CE1 1 
ATOM   2970 C  CE2 . PHE   A  1 420 ? -27.008 -20.167 6.325  1.00 31.12  ? 299  PHE   A CE2 1 
ATOM   2971 C  CZ  . PHE   A  1 420 ? -27.776 -20.185 7.472  1.00 32.69  ? 299  PHE   A CZ  1 
ATOM   2972 N  N   . ARG   A  1 421 ? -30.520 -24.103 1.973  1.00 43.14  ? 300  ARG   A N   1 
ATOM   2973 C  CA  . ARG   A  1 421 ? -31.005 -24.484 0.650  1.00 49.73  ? 300  ARG   A CA  1 
ATOM   2974 C  C   . ARG   A  1 421 ? -32.444 -24.985 0.712  1.00 43.60  ? 300  ARG   A C   1 
ATOM   2975 O  O   . ARG   A  1 421 ? -33.301 -24.540 -0.059 1.00 36.32  ? 300  ARG   A O   1 
ATOM   2976 C  CB  . ARG   A  1 421 ? -30.092 -25.551 0.046  1.00 51.65  ? 300  ARG   A CB  1 
ATOM   2977 C  CG  . ARG   A  1 421 ? -28.797 -25.020 -0.546 1.00 55.33  ? 300  ARG   A CG  1 
ATOM   2978 C  CD  . ARG   A  1 421 ? -28.387 -25.842 -1.758 1.00 66.01  ? 300  ARG   A CD  1 
ATOM   2979 N  NE  . ARG   A  1 421 ? -27.123 -26.544 -1.565 1.00 74.12  ? 300  ARG   A NE  1 
ATOM   2980 C  CZ  . ARG   A  1 421 ? -25.927 -25.989 -1.705 1.00 78.98  ? 300  ARG   A CZ  1 
ATOM   2981 N  NH1 . ARG   A  1 421 ? -25.790 -24.716 -2.040 1.00 66.02  ? 300  ARG   A NH1 1 
ATOM   2982 N  NH2 . ARG   A  1 421 ? -24.841 -26.731 -1.510 1.00 76.33  ? 300  ARG   A NH2 1 
ATOM   2983 N  N   . LYS   A  1 422 ? -32.726 -25.917 1.627  1.00 43.76  ? 301  LYS   A N   1 
ATOM   2984 C  CA  . LYS   A  1 422 ? -34.068 -26.488 1.709  1.00 50.28  ? 301  LYS   A CA  1 
ATOM   2985 C  C   . LYS   A  1 422 ? -35.105 -25.435 2.081  1.00 50.16  ? 301  LYS   A C   1 
ATOM   2986 O  O   . LYS   A  1 422 ? -36.225 -25.451 1.557  1.00 52.79  ? 301  LYS   A O   1 
ATOM   2987 C  CB  . LYS   A  1 422 ? -34.114 -27.660 2.697  1.00 46.75  ? 301  LYS   A CB  1 
ATOM   2988 C  CG  . LYS   A  1 422 ? -34.813 -27.346 4.016  1.00 59.27  ? 301  LYS   A CG  1 
ATOM   2989 C  CD  . LYS   A  1 422 ? -35.299 -28.576 4.761  1.00 73.31  ? 301  LYS   A CD  1 
ATOM   2990 C  CE  . LYS   A  1 422 ? -36.552 -29.135 4.097  1.00 72.67  ? 301  LYS   A CE  1 
ATOM   2991 N  NZ  . LYS   A  1 422 ? -36.993 -30.427 4.688  1.00 76.60  ? 301  LYS   A NZ  1 
ATOM   2992 N  N   . ILE   A  1 423 ? -34.760 -24.516 2.985  1.00 45.16  ? 302  ILE   A N   1 
ATOM   2993 C  CA  . ILE   A  1 423 ? -35.716 -23.481 3.364  1.00 48.51  ? 302  ILE   A CA  1 
ATOM   2994 C  C   . ILE   A  1 423 ? -36.035 -22.586 2.173  1.00 51.97  ? 302  ILE   A C   1 
ATOM   2995 O  O   . ILE   A  1 423 ? -37.202 -22.286 1.897  1.00 57.31  ? 302  ILE   A O   1 
ATOM   2996 C  CB  . ILE   A  1 423 ? -35.173 -22.660 4.550  1.00 44.53  ? 302  ILE   A CB  1 
ATOM   2997 C  CG1 . ILE   A  1 423 ? -35.105 -23.514 5.818  1.00 48.74  ? 302  ILE   A CG1 1 
ATOM   2998 C  CG2 . ILE   A  1 423 ? -36.043 -21.437 4.796  1.00 38.36  ? 302  ILE   A CG2 1 
ATOM   2999 C  CD1 . ILE   A  1 423 ? -34.207 -22.928 6.894  1.00 37.19  ? 302  ILE   A CD1 1 
ATOM   3000 N  N   . ILE   A  1 424 ? -35.008 -22.144 1.451  1.00 56.05  ? 303  ILE   A N   1 
ATOM   3001 C  CA  . ILE   A  1 424 ? -35.241 -21.239 0.331  1.00 59.47  ? 303  ILE   A CA  1 
ATOM   3002 C  C   . ILE   A  1 424 ? -35.981 -21.946 -0.803 1.00 63.48  ? 303  ILE   A C   1 
ATOM   3003 O  O   . ILE   A  1 424 ? -36.987 -21.441 -1.317 1.00 60.79  ? 303  ILE   A O   1 
ATOM   3004 C  CB  . ILE   A  1 424 ? -33.908 -20.632 -0.146 1.00 55.69  ? 303  ILE   A CB  1 
ATOM   3005 C  CG1 . ILE   A  1 424 ? -33.336 -19.721 0.944  1.00 56.29  ? 303  ILE   A CG1 1 
ATOM   3006 C  CG2 . ILE   A  1 424 ? -34.099 -19.871 -1.447 1.00 58.73  ? 303  ILE   A CG2 1 
ATOM   3007 C  CD1 . ILE   A  1 424 ? -31.825 -19.639 0.966  1.00 40.77  ? 303  ILE   A CD1 1 
ATOM   3008 N  N   . ARG   A  1 425 ? -35.486 -23.116 -1.217 1.00 53.38  ? 304  ARG   A N   1 
ATOM   3009 C  CA  . ARG   A  1 425 ? -36.110 -23.861 -2.308 1.00 66.26  ? 304  ARG   A CA  1 
ATOM   3010 C  C   . ARG   A  1 425 ? -37.563 -24.230 -2.025 1.00 66.47  ? 304  ARG   A C   1 
ATOM   3011 O  O   . ARG   A  1 425 ? -38.459 -23.937 -2.826 1.00 78.72  ? 304  ARG   A O   1 
ATOM   3012 C  CB  . ARG   A  1 425 ? -35.307 -25.128 -2.608 1.00 53.91  ? 304  ARG   A CB  1 
ATOM   3013 C  CG  . ARG   A  1 425 ? -34.006 -24.906 -3.351 1.00 64.52  ? 304  ARG   A CG  1 
ATOM   3014 C  CD  . ARG   A  1 425 ? -33.228 -26.211 -3.427 1.00 69.48  ? 304  ARG   A CD  1 
ATOM   3015 N  NE  . ARG   A  1 425 ? -31.890 -26.044 -3.980 1.00 88.69  ? 304  ARG   A NE  1 
ATOM   3016 C  CZ  . ARG   A  1 425 ? -30.939 -26.967 -3.939 1.00 88.00  ? 304  ARG   A CZ  1 
ATOM   3017 N  NH1 . ARG   A  1 425 ? -31.137 -28.140 -3.360 1.00 83.12  ? 304  ARG   A NH1 1 
ATOM   3018 N  NH2 . ARG   A  1 425 ? -29.778 -26.727 -4.542 1.00 79.86  ? 304  ARG   A NH2 1 
ATOM   3019 N  N   . SER   A  1 426 ? -37.818 -24.878 -0.886 1.00 62.78  ? 305  SER   A N   1 
ATOM   3020 C  CA  . SER   A  1 426 ? -39.167 -25.274 -0.486 1.00 70.73  ? 305  SER   A CA  1 
ATOM   3021 C  C   . SER   A  1 426 ? -40.073 -24.126 -0.069 1.00 73.70  ? 305  SER   A C   1 
ATOM   3022 O  O   . SER   A  1 426 ? -41.202 -24.403 0.351  1.00 91.87  ? 305  SER   A O   1 
ATOM   3023 C  CB  . SER   A  1 426 ? -39.088 -26.294 0.653  1.00 71.46  ? 305  SER   A CB  1 
ATOM   3024 O  OG  . SER   A  1 426 ? -38.260 -27.387 0.297  1.00 73.13  ? 305  SER   A OG  1 
ATOM   3025 N  N   . HIS   A  1 427 ? -39.648 -22.867 -0.155 1.00 72.74  ? 306  HIS   A N   1 
ATOM   3026 C  CA  . HIS   A  1 427 ? -40.528 -21.786 0.276  1.00 85.30  ? 306  HIS   A CA  1 
ATOM   3027 C  C   . HIS   A  1 427 ? -40.374 -20.551 -0.602 1.00 89.60  ? 306  HIS   A C   1 
ATOM   3028 O  O   . HIS   A  1 427 ? -41.250 -20.254 -1.421 1.00 99.85  ? 306  HIS   A O   1 
ATOM   3029 C  CB  . HIS   A  1 427 ? -40.261 -21.431 1.741  1.00 81.22  ? 306  HIS   A CB  1 
ATOM   3030 C  CG  . HIS   A  1 427 ? -40.488 -22.568 2.689  1.00 93.34  ? 306  HIS   A CG  1 
ATOM   3031 N  ND1 . HIS   A  1 427 ? -39.531 -23.528 2.941  1.00 94.10  ? 306  HIS   A ND1 1 
ATOM   3032 C  CD2 . HIS   A  1 427 ? -41.564 -22.905 3.439  1.00 89.68  ? 306  HIS   A CD2 1 
ATOM   3033 C  CE1 . HIS   A  1 427 ? -40.007 -24.405 3.807  1.00 97.33  ? 306  HIS   A CE1 1 
ATOM   3034 N  NE2 . HIS   A  1 427 ? -41.238 -24.049 4.126  1.00 86.19  ? 306  HIS   A NE2 1 
ATOM   3035 N  N   . VAL   A  1 428 ? -39.269 -19.832 -0.431 1.00 68.25  ? 307  VAL   A N   1 
ATOM   3036 C  CA  . VAL   A  1 428 ? -39.011 -18.590 -1.155 1.00 85.06  ? 307  VAL   A CA  1 
ATOM   3037 C  C   . VAL   A  1 428 ? -39.106 -18.784 -2.665 1.00 81.65  ? 307  VAL   A C   1 
ATOM   3038 O  O   . VAL   A  1 428 ? -38.431 -19.641 -3.235 1.00 79.51  ? 307  VAL   A O   1 
ATOM   3039 C  CB  . VAL   A  1 428 ? -37.634 -18.017 -0.778 1.00 71.32  ? 307  VAL   A CB  1 
ATOM   3040 C  CG1 . VAL   A  1 428 ? -37.289 -16.833 -1.667 1.00 84.74  ? 307  VAL   A CG1 1 
ATOM   3041 C  CG2 . VAL   A  1 428 ? -37.610 -17.618 0.689  1.00 81.09  ? 307  VAL   A CG2 1 
HETATM 3042 C  C1  . A1H3J B  2 .   ? -21.021 3.086   19.353 1.00 23.14  ? 1201 A1H3J A C1  1 
HETATM 3043 C  C2  . A1H3J B  2 .   ? -20.358 5.304   18.552 1.00 21.69  ? 1201 A1H3J A C2  1 
HETATM 3044 O  O2  . A1H3J B  2 .   ? -23.091 14.289  13.163 1.00 42.36  ? 1201 A1H3J A O2  1 
HETATM 3045 C  C3  . A1H3J B  2 .   ? -20.709 6.434   17.763 1.00 24.16  ? 1201 A1H3J A C3  1 
HETATM 3046 O  O3  . A1H3J B  2 .   ? -23.070 3.201   17.548 1.00 36.18  ? 1201 A1H3J A O3  1 
HETATM 3047 C  C4  . A1H3J B  2 .   ? -20.891 8.415   16.764 1.00 21.28  ? 1201 A1H3J A C4  1 
HETATM 3048 C  C5  . A1H3J B  2 .   ? -20.634 9.783   16.386 1.00 24.76  ? 1201 A1H3J A C5  1 
HETATM 3049 C  C7  . A1H3J B  2 .   ? -21.058 11.724  14.871 1.00 28.87  ? 1201 A1H3J A C7  1 
HETATM 3050 C  C6  . A1H3J B  2 .   ? -21.115 10.316  15.268 1.00 26.05  ? 1201 A1H3J A C6  1 
HETATM 3051 N  N   . A1H3J B  2 .   ? -21.245 4.228   18.447 1.00 23.31  ? 1201 A1H3J A N   1 
HETATM 3052 C  C   . A1H3J B  2 .   ? -19.963 2.130   18.872 1.00 34.14  ? 1201 A1H3J A C   1 
HETATM 3053 O  O   . A1H3J B  2 .   ? -19.374 5.211   19.277 1.00 24.35  ? 1201 A1H3J A O   1 
HETATM 3054 C  C10 . A1H3J B  2 .   ? -20.975 14.422  14.164 1.00 42.46  ? 1201 A1H3J A C10 1 
HETATM 3055 C  C11 . A1H3J B  2 .   ? -19.929 16.565  14.102 1.00 60.36  ? 1201 A1H3J A C11 1 
HETATM 3056 C  C12 . A1H3J B  2 .   ? -22.095 13.638  13.833 1.00 35.32  ? 1201 A1H3J A C12 1 
HETATM 3057 C  C13 . A1H3J B  2 .   ? -24.242 13.530  12.799 1.00 38.41  ? 1201 A1H3J A C13 1 
HETATM 3058 C  C14 . A1H3J B  2 .   ? -22.130 12.303  14.186 1.00 28.05  ? 1201 A1H3J A C14 1 
HETATM 3059 C  C15 . A1H3J B  2 .   ? -21.812 6.467   16.952 1.00 21.34  ? 1201 A1H3J A C15 1 
HETATM 3060 C  C16 . A1H3J B  2 .   ? -23.790 5.340   16.008 1.00 24.22  ? 1201 A1H3J A C16 1 
HETATM 3061 C  C17 . A1H3J B  2 .   ? -24.993 5.976   16.655 1.00 23.04  ? 1201 A1H3J A C17 1 
HETATM 3062 C  C18 . A1H3J B  2 .   ? -22.361 4.187   17.627 1.00 27.43  ? 1201 A1H3J A C18 1 
HETATM 3063 C  C8  . A1H3J B  2 .   ? -19.955 12.514  15.184 1.00 28.85  ? 1201 A1H3J A C8  1 
HETATM 3064 C  C9  . A1H3J B  2 .   ? -19.907 13.852  14.838 1.00 44.39  ? 1201 A1H3J A C9  1 
HETATM 3065 N  N1  . A1H3J B  2 .   ? -20.128 7.670   17.636 1.00 20.84  ? 1201 A1H3J A N1  1 
HETATM 3066 N  N2  . A1H3J B  2 .   ? -21.914 7.684   16.344 1.00 22.44  ? 1201 A1H3J A N2  1 
HETATM 3067 N  N3  . A1H3J B  2 .   ? -22.612 5.334   16.894 1.00 20.60  ? 1201 A1H3J A N3  1 
HETATM 3068 O  O1  . A1H3J B  2 .   ? -21.040 15.731  13.781 1.00 60.38  ? 1201 A1H3J A O1  1 
HETATM 3069 C  C1  . CLR   C  3 .   ? -38.283 10.609  21.930 1.00 27.47  ? 1202 CLR   A C1  1 
HETATM 3070 C  C2  . CLR   C  3 .   ? -37.988 12.076  22.222 1.00 28.31  ? 1202 CLR   A C2  1 
HETATM 3071 C  C3  . CLR   C  3 .   ? -38.260 12.393  23.677 1.00 26.55  ? 1202 CLR   A C3  1 
HETATM 3072 C  C4  . CLR   C  3 .   ? -37.396 11.496  24.557 1.00 25.62  ? 1202 CLR   A C4  1 
HETATM 3073 C  C5  . CLR   C  3 .   ? -37.630 10.037  24.266 1.00 25.17  ? 1202 CLR   A C5  1 
HETATM 3074 C  C6  . CLR   C  3 .   ? -37.937 9.200   25.255 1.00 30.67  ? 1202 CLR   A C6  1 
HETATM 3075 C  C7  . CLR   C  3 .   ? -38.171 7.734   25.107 1.00 26.17  ? 1202 CLR   A C7  1 
HETATM 3076 C  C8  . CLR   C  3 .   ? -37.807 7.197   23.727 1.00 32.12  ? 1202 CLR   A C8  1 
HETATM 3077 C  C9  . CLR   C  3 .   ? -38.189 8.207   22.634 1.00 28.32  ? 1202 CLR   A C9  1 
HETATM 3078 C  C10 . CLR   C  3 .   ? -37.523 9.597   22.816 1.00 30.68  ? 1202 CLR   A C10 1 
HETATM 3079 C  C11 . CLR   C  3 .   ? -37.975 7.612   21.238 1.00 30.69  ? 1202 CLR   A C11 1 
HETATM 3080 C  C12 . CLR   C  3 .   ? -38.657 6.256   21.044 1.00 24.66  ? 1202 CLR   A C12 1 
HETATM 3081 C  C13 . CLR   C  3 .   ? -38.226 5.238   22.106 1.00 31.28  ? 1202 CLR   A C13 1 
HETATM 3082 C  C14 . CLR   C  3 .   ? -38.533 5.887   23.465 1.00 28.01  ? 1202 CLR   A C14 1 
HETATM 3083 C  C15 . CLR   C  3 .   ? -38.378 4.752   24.466 1.00 32.71  ? 1202 CLR   A C15 1 
HETATM 3084 C  C16 . CLR   C  3 .   ? -38.976 3.550   23.711 1.00 28.95  ? 1202 CLR   A C16 1 
HETATM 3085 C  C17 . CLR   C  3 .   ? -39.056 3.930   22.204 1.00 22.65  ? 1202 CLR   A C17 1 
HETATM 3086 C  C18 . CLR   C  3 .   ? -36.743 4.890   21.974 1.00 22.50  ? 1202 CLR   A C18 1 
HETATM 3087 C  C19 . CLR   C  3 .   ? -36.039 9.579   22.421 1.00 23.72  ? 1202 CLR   A C19 1 
HETATM 3088 C  C20 . CLR   C  3 .   ? -38.709 2.721   21.318 1.00 23.18  ? 1202 CLR   A C20 1 
HETATM 3089 C  C21 . CLR   C  3 .   ? -38.848 2.957   19.815 1.00 31.19  ? 1202 CLR   A C21 1 
HETATM 3090 C  C22 . CLR   C  3 .   ? -39.589 1.539   21.742 1.00 28.52  ? 1202 CLR   A C22 1 
HETATM 3091 C  C23 . CLR   C  3 .   ? -39.514 0.300   20.858 1.00 35.18  ? 1202 CLR   A C23 1 
HETATM 3092 C  C24 . CLR   C  3 .   ? -40.394 -0.815  21.409 1.00 49.95  ? 1202 CLR   A C24 1 
HETATM 3093 C  C25 . CLR   C  3 .   ? -39.975 -2.231  21.013 1.00 67.26  ? 1202 CLR   A C25 1 
HETATM 3094 C  C26 . CLR   C  3 .   ? -40.393 -3.222  22.094 1.00 58.58  ? 1202 CLR   A C26 1 
HETATM 3095 C  C27 . CLR   C  3 .   ? -40.571 -2.649  19.674 1.00 60.64  ? 1202 CLR   A C27 1 
HETATM 3096 O  O1  . CLR   C  3 .   ? -37.997 13.764  23.899 1.00 33.97  ? 1202 CLR   A O1  1 
HETATM 3097 C  C1  . CLR   D  3 .   ? -3.050  8.131   21.150 1.00 22.57  ? 1203 CLR   A C1  1 
HETATM 3098 C  C2  . CLR   D  3 .   ? -2.854  9.642   21.114 1.00 20.66  ? 1203 CLR   A C2  1 
HETATM 3099 C  C3  . CLR   D  3 .   ? -1.886  10.045  20.019 1.00 22.83  ? 1203 CLR   A C3  1 
HETATM 3100 C  C4  . CLR   D  3 .   ? -2.336  9.486   18.670 1.00 21.67  ? 1203 CLR   A C4  1 
HETATM 3101 C  C5  . CLR   D  3 .   ? -2.601  8.003   18.719 1.00 25.18  ? 1203 CLR   A C5  1 
HETATM 3102 C  C6  . CLR   D  3 .   ? -1.977  7.169   17.887 1.00 19.31  ? 1203 CLR   A C6  1 
HETATM 3103 C  C7  . CLR   D  3 .   ? -2.272  5.709   17.766 1.00 21.87  ? 1203 CLR   A C7  1 
HETATM 3104 C  C8  . CLR   D  3 .   ? -3.501  5.287   18.566 1.00 21.40  ? 1203 CLR   A C8  1 
HETATM 3105 C  C9  . CLR   D  3 .   ? -3.486  5.982   19.935 1.00 23.24  ? 1203 CLR   A C9  1 
HETATM 3106 C  C10 . CLR   D  3 .   ? -3.534  7.526   19.816 1.00 26.42  ? 1203 CLR   A C10 1 
HETATM 3107 C  C11 . CLR   D  3 .   ? -4.567  5.428   20.867 1.00 24.27  ? 1203 CLR   A C11 1 
HETATM 3108 C  C12 . CLR   D  3 .   ? -4.563  3.903   20.968 1.00 16.74  ? 1203 CLR   A C12 1 
HETATM 3109 C  C13 . CLR   D  3 .   ? -4.704  3.244   19.593 1.00 25.47  ? 1203 CLR   A C13 1 
HETATM 3110 C  C14 . CLR   D  3 .   ? -3.533  3.777   18.751 1.00 23.22  ? 1203 CLR   A C14 1 
HETATM 3111 C  C15 . CLR   D  3 .   ? -3.524  2.893   17.511 1.00 24.50  ? 1203 CLR   A C15 1 
HETATM 3112 C  C16 . CLR   D  3 .   ? -3.986  1.520   18.041 1.00 28.90  ? 1203 CLR   A C16 1 
HETATM 3113 C  C17 . CLR   D  3 .   ? -4.436  1.718   19.515 1.00 29.52  ? 1203 CLR   A C17 1 
HETATM 3114 C  C18 . CLR   D  3 .   ? -6.063  3.564   18.959 1.00 20.59  ? 1203 CLR   A C18 1 
HETATM 3115 C  C19 . CLR   D  3 .   ? -4.952  8.028   19.500 1.00 15.89  ? 1203 CLR   A C19 1 
HETATM 3116 C  C20 . CLR   D  3 .   ? -5.543  0.726   19.915 1.00 40.09  ? 1203 CLR   A C20 1 
HETATM 3117 C  C21 . CLR   D  3 .   ? -5.858  0.701   21.409 1.00 25.70  ? 1203 CLR   A C21 1 
HETATM 3118 C  C22 . CLR   D  3 .   ? -5.177  -0.692  19.457 1.00 36.51  ? 1203 CLR   A C22 1 
HETATM 3119 C  C23 . CLR   D  3 .   ? -6.230  -1.743  19.789 1.00 39.34  ? 1203 CLR   A C23 1 
HETATM 3120 C  C24 . CLR   D  3 .   ? -5.618  -3.062  20.248 1.00 47.52  ? 1203 CLR   A C24 1 
HETATM 3121 C  C25 . CLR   D  3 .   ? -5.177  -4.000  19.123 1.00 45.92  ? 1203 CLR   A C25 1 
HETATM 3122 C  C26 . CLR   D  3 .   ? -5.005  -5.418  19.658 1.00 62.48  ? 1203 CLR   A C26 1 
HETATM 3123 C  C27 . CLR   D  3 .   ? -6.152  -3.992  17.949 1.00 55.38  ? 1203 CLR   A C27 1 
HETATM 3124 O  O1  . CLR   D  3 .   ? -1.806  11.456  20.000 1.00 28.23  ? 1203 CLR   A O1  1 
HETATM 3125 C  C1  . CLR   E  3 .   ? -8.209  10.830  13.236 1.00 23.73  ? 1204 CLR   A C1  1 
HETATM 3126 C  C2  . CLR   E  3 .   ? -8.268  12.351  13.259 1.00 29.52  ? 1204 CLR   A C2  1 
HETATM 3127 C  C3  . CLR   E  3 .   ? -6.902  12.949  12.985 1.00 30.82  ? 1204 CLR   A C3  1 
HETATM 3128 C  C4  . CLR   E  3 .   ? -6.349  12.425  11.660 1.00 26.95  ? 1204 CLR   A C4  1 
HETATM 3129 C  C5  . CLR   E  3 .   ? -6.376  10.921  11.574 1.00 31.50  ? 1204 CLR   A C5  1 
HETATM 3130 C  C6  . CLR   E  3 .   ? -5.313  10.242  11.142 1.00 31.21  ? 1204 CLR   A C6  1 
HETATM 3131 C  C7  . CLR   E  3 .   ? -5.265  8.762   10.941 1.00 32.00  ? 1204 CLR   A C7  1 
HETATM 3132 C  C8  . CLR   E  3 .   ? -6.648  8.117   10.955 1.00 32.84  ? 1204 CLR   A C8  1 
HETATM 3133 C  C9  . CLR   E  3 .   ? -7.495  8.727   12.080 1.00 25.68  ? 1204 CLR   A C9  1 
HETATM 3134 C  C10 . CLR   E  3 .   ? -7.698  10.251  11.903 1.00 32.58  ? 1204 CLR   A C10 1 
HETATM 3135 C  C11 . CLR   E  3 .   ? -8.814  7.974   12.273 1.00 24.38  ? 1204 CLR   A C11 1 
HETATM 3136 C  C12 . CLR   E  3 .   ? -8.641  6.460   12.396 1.00 21.72  ? 1204 CLR   A C12 1 
HETATM 3137 C  C13 . CLR   E  3 .   ? -7.893  5.873   11.196 1.00 26.25  ? 1204 CLR   A C13 1 
HETATM 3138 C  C14 . CLR   E  3 .   ? -6.545  6.612   11.151 1.00 37.32  ? 1204 CLR   A C14 1 
HETATM 3139 C  C15 . CLR   E  3 .   ? -5.700  5.809   10.173 1.00 34.68  ? 1204 CLR   A C15 1 
HETATM 3140 C  C16 . CLR   E  3 .   ? -6.146  4.356   10.422 1.00 35.74  ? 1204 CLR   A C16 1 
HETATM 3141 C  C17 . CLR   E  3 .   ? -7.415  4.400   11.319 1.00 34.97  ? 1204 CLR   A C17 1 
HETATM 3142 C  C18 . CLR   E  3 .   ? -8.688  6.064   9.898  1.00 27.89  ? 1204 CLR   A C18 1 
HETATM 3143 C  C19 . CLR   E  3 .   ? -8.700  10.571  10.782 1.00 25.24  ? 1204 CLR   A C19 1 
HETATM 3144 C  C20 . CLR   E  3 .   ? -8.373  3.241   10.989 1.00 28.31  ? 1204 CLR   A C20 1 
HETATM 3145 C  C21 . CLR   E  3 .   ? -9.615  3.178   11.875 1.00 33.23  ? 1204 CLR   A C21 1 
HETATM 3146 C  C22 . CLR   E  3 .   ? -7.620  1.905   11.060 1.00 26.11  ? 1204 CLR   A C22 1 
HETATM 3147 C  C23 . CLR   E  3 .   ? -8.493  0.674   11.288 1.00 34.99  ? 1204 CLR   A C23 1 
HETATM 3148 C  C24 . CLR   E  3 .   ? -7.731  -0.624  11.047 1.00 42.38  ? 1204 CLR   A C24 1 
HETATM 3149 C  C25 . CLR   E  3 .   ? -8.593  -1.888  11.037 1.00 48.80  ? 1204 CLR   A C25 1 
HETATM 3150 C  C26 . CLR   E  3 .   ? -8.915  -2.323  12.463 1.00 31.50  ? 1204 CLR   A C26 1 
HETATM 3151 C  C27 . CLR   E  3 .   ? -7.929  -3.026  10.268 1.00 48.65  ? 1204 CLR   A C27 1 
HETATM 3152 O  O1  . CLR   E  3 .   ? -7.029  14.357  12.982 1.00 36.06  ? 1204 CLR   A O1  1 
HETATM 3153 C  C3  . OLA   F  4 .   ? -17.326 -15.854 2.816  1.00 64.36  ? 1205 OLA   A C3  1 
HETATM 3154 C  C4  . OLA   F  4 .   ? -18.252 -14.778 2.262  1.00 75.71  ? 1205 OLA   A C4  1 
HETATM 3155 C  C5  . OLA   F  4 .   ? -18.576 -13.738 3.327  1.00 70.98  ? 1205 OLA   A C5  1 
HETATM 3156 C  C6  . OLA   F  4 .   ? -17.300 -13.104 3.867  1.00 68.13  ? 1205 OLA   A C6  1 
HETATM 3157 C  C7  . OLA   F  4 .   ? -17.293 -11.600 3.626  1.00 66.11  ? 1205 OLA   A C7  1 
HETATM 3158 C  C8  . OLA   F  4 .   ? -16.374 -10.886 4.609  1.00 63.12  ? 1205 OLA   A C8  1 
HETATM 3159 C  C9  . OLA   F  4 .   ? -15.921 -9.582  3.998  1.00 57.93  ? 1205 OLA   A C9  1 
HETATM 3160 C  C10 . OLA   F  4 .   ? -16.026 -8.349  4.788  1.00 58.67  ? 1205 OLA   A C10 1 
HETATM 3161 C  C11 . OLA   F  4 .   ? -17.374 -7.966  5.351  1.00 55.37  ? 1205 OLA   A C11 1 
HETATM 3162 C  C12 . OLA   F  4 .   ? -17.209 -6.864  6.389  1.00 44.08  ? 1205 OLA   A C12 1 
HETATM 3163 C  C7  . OLA   G  4 .   ? -20.920 -12.860 -0.127 1.00 63.02  ? 1206 OLA   A C7  1 
HETATM 3164 C  C8  . OLA   G  4 .   ? -20.480 -11.550 0.514  1.00 67.11  ? 1206 OLA   A C8  1 
HETATM 3165 C  C9  . OLA   G  4 .   ? -21.456 -11.141 1.609  1.00 63.70  ? 1206 OLA   A C9  1 
HETATM 3166 C  C10 . OLA   G  4 .   ? -20.720 -10.352 2.664  1.00 50.78  ? 1206 OLA   A C10 1 
HETATM 3167 C  C11 . OLA   G  4 .   ? -21.266 -10.279 4.025  1.00 54.36  ? 1206 OLA   A C11 1 
HETATM 3168 C  C12 . OLA   G  4 .   ? -22.739 -7.366  2.766  1.00 51.90  ? 1206 OLA   A C12 1 
HETATM 3169 C  C13 . OLA   G  4 .   ? -23.034 -6.072  3.513  1.00 43.26  ? 1206 OLA   A C13 1 
HETATM 3170 C  C14 . OLA   G  4 .   ? -22.756 -4.851  2.645  1.00 32.71  ? 1206 OLA   A C14 1 
HETATM 3171 C  C15 . OLA   G  4 .   ? -24.038 -4.070  2.384  1.00 42.47  ? 1206 OLA   A C15 1 
HETATM 3172 C  C16 . OLA   G  4 .   ? -23.732 -2.706  1.777  1.00 59.30  ? 1206 OLA   A C16 1 
HETATM 3173 C  C17 . OLA   G  4 .   ? -24.968 -1.815  1.792  1.00 49.57  ? 1206 OLA   A C17 1 
HETATM 3174 C  C1  . OLA   H  4 .   ? -20.327 -22.538 27.920 1.00 49.40  ? 1207 OLA   A C1  1 
HETATM 3175 O  O1  . OLA   H  4 .   ? -19.817 -23.002 26.877 1.00 59.65  ? 1207 OLA   A O1  1 
HETATM 3176 O  O2  . OLA   H  4 .   ? -21.484 -22.890 28.236 1.00 78.25  ? 1207 OLA   A O2  1 
HETATM 3177 C  C2  . OLA   H  4 .   ? -19.559 -21.574 28.792 1.00 39.68  ? 1207 OLA   A C2  1 
HETATM 3178 C  C3  . OLA   H  4 .   ? -20.194 -20.191 28.710 1.00 50.85  ? 1207 OLA   A C3  1 
HETATM 3179 C  C4  . OLA   H  4 .   ? -19.196 -19.106 29.095 1.00 36.96  ? 1207 OLA   A C4  1 
HETATM 3180 C  C5  . OLA   H  4 .   ? -19.900 -17.785 29.386 1.00 36.79  ? 1207 OLA   A C5  1 
HETATM 3181 C  C6  . OLA   H  4 .   ? -18.987 -16.603 29.079 1.00 42.47  ? 1207 OLA   A C6  1 
HETATM 3182 C  C7  . OLA   H  4 .   ? -19.737 -15.283 29.212 1.00 39.73  ? 1207 OLA   A C7  1 
HETATM 3183 C  C1  . OLA   I  4 .   ? -2.301  14.796  13.715 1.00 61.61  ? 1208 OLA   A C1  1 
HETATM 3184 O  O1  . OLA   I  4 .   ? -1.915  15.856  14.255 1.00 72.82  ? 1208 OLA   A O1  1 
HETATM 3185 O  O2  . OLA   I  4 .   ? -3.444  14.755  13.212 1.00 61.34  ? 1208 OLA   A O2  1 
HETATM 3186 C  C2  . OLA   I  4 .   ? -1.394  13.588  13.670 1.00 55.60  ? 1208 OLA   A C2  1 
HETATM 3187 C  C3  . OLA   I  4 .   ? -2.194  12.338  13.321 1.00 38.89  ? 1208 OLA   A C3  1 
HETATM 3188 C  C4  . OLA   I  4 .   ? -1.422  11.079  13.704 1.00 40.71  ? 1208 OLA   A C4  1 
HETATM 3189 C  C5  . OLA   I  4 .   ? -2.001  9.844   13.024 1.00 49.06  ? 1208 OLA   A C5  1 
HETATM 3190 C  C6  . OLA   I  4 .   ? -1.617  8.570   13.768 1.00 47.13  ? 1208 OLA   A C6  1 
HETATM 3191 C  C7  . OLA   I  4 .   ? -1.388  7.411   12.804 1.00 49.78  ? 1208 OLA   A C7  1 
HETATM 3192 C  C8  . OLA   I  4 .   ? -1.865  6.096   13.412 1.00 42.29  ? 1208 OLA   A C8  1 
HETATM 3193 C  C9  . OLA   I  4 .   ? -1.936  5.044   12.330 1.00 50.74  ? 1208 OLA   A C9  1 
HETATM 3194 C  C10 . OLA   I  4 .   ? -2.972  4.000   12.355 1.00 47.94  ? 1208 OLA   A C10 1 
HETATM 3195 C  C11 . OLA   I  4 .   ? -3.257  3.196   13.602 1.00 36.39  ? 1208 OLA   A C11 1 
HETATM 3196 C  C12 . OLA   I  4 .   ? -4.189  2.049   13.226 1.00 43.93  ? 1208 OLA   A C12 1 
HETATM 3197 C  C13 . OLA   I  4 .   ? -4.264  0.986   14.316 1.00 39.62  ? 1208 OLA   A C13 1 
HETATM 3198 C  C14 . OLA   I  4 .   ? -4.344  -0.405  13.696 1.00 52.26  ? 1208 OLA   A C14 1 
HETATM 3199 C  C15 . OLA   I  4 .   ? -5.013  -1.400  14.637 1.00 67.81  ? 1208 OLA   A C15 1 
HETATM 3200 C  C16 . OLA   I  4 .   ? -4.954  -2.813  14.069 1.00 69.57  ? 1208 OLA   A C16 1 
HETATM 3201 C  C1  . OLA   J  4 .   ? -21.222 12.849  3.972  1.00 63.08  ? 1209 OLA   A C1  1 
HETATM 3202 O  O1  . OLA   J  4 .   ? -21.561 13.712  3.134  1.00 78.40  ? 1209 OLA   A O1  1 
HETATM 3203 O  O2  . OLA   J  4 .   ? -21.167 13.170  5.179  1.00 60.30  ? 1209 OLA   A O2  1 
HETATM 3204 C  C2  . OLA   J  4 .   ? -20.880 11.445  3.532  1.00 54.97  ? 1209 OLA   A C2  1 
HETATM 3205 C  C3  . OLA   J  4 .   ? -22.155 10.663  3.239  1.00 47.93  ? 1209 OLA   A C3  1 
HETATM 3206 C  C4  . OLA   J  4 .   ? -22.025 9.220   3.713  1.00 48.77  ? 1209 OLA   A C4  1 
HETATM 3207 C  C5  . OLA   J  4 .   ? -20.757 8.581   3.158  1.00 41.81  ? 1209 OLA   A C5  1 
HETATM 3208 C  C6  . OLA   J  4 .   ? -20.461 7.250   3.840  1.00 49.76  ? 1209 OLA   A C6  1 
HETATM 3209 C  C7  . OLA   J  4 .   ? -21.735 6.443   4.061  1.00 46.15  ? 1209 OLA   A C7  1 
HETATM 3210 C  C8  . OLA   J  4 .   ? -21.544 5.004   3.598  1.00 35.34  ? 1209 OLA   A C8  1 
HETATM 3211 C  C9  . OLA   J  4 .   ? -20.790 4.990   2.290  1.00 47.55  ? 1209 OLA   A C9  1 
HETATM 3212 C  C10 . OLA   J  4 .   ? -20.664 3.731   1.544  1.00 40.95  ? 1209 OLA   A C10 1 
HETATM 3213 C  C11 . OLA   J  4 .   ? -20.588 2.427   2.300  1.00 45.51  ? 1209 OLA   A C11 1 
HETATM 3214 C  C12 . OLA   J  4 .   ? -20.777 1.273   1.324  1.00 44.32  ? 1209 OLA   A C12 1 
HETATM 3215 C  C13 . OLA   J  4 .   ? -21.159 -0.020  2.037  1.00 62.29  ? 1209 OLA   A C13 1 
HETATM 3216 C  C14 . OLA   J  4 .   ? -20.408 -0.187  3.353  1.00 48.61  ? 1209 OLA   A C14 1 
HETATM 3217 C  C1  . OLA   K  4 .   ? -34.191 10.688  2.551  1.00 83.92  ? 1210 OLA   A C1  1 
HETATM 3218 O  O1  . OLA   K  4 .   ? -34.865 11.212  1.638  1.00 86.81  ? 1210 OLA   A O1  1 
HETATM 3219 O  O2  . OLA   K  4 .   ? -34.233 11.184  3.698  1.00 63.95  ? 1210 OLA   A O2  1 
HETATM 3220 C  C2  . OLA   K  4 .   ? -33.335 9.477   2.265  1.00 62.85  ? 1210 OLA   A C2  1 
HETATM 3221 C  C3  . OLA   K  4 .   ? -34.157 8.478   1.459  1.00 58.43  ? 1210 OLA   A C3  1 
HETATM 3222 C  C4  . OLA   K  4 .   ? -34.232 7.126   2.156  1.00 51.05  ? 1210 OLA   A C4  1 
HETATM 3223 C  C5  . OLA   K  4 .   ? -35.377 6.291   1.596  1.00 47.42  ? 1210 OLA   A C5  1 
HETATM 3224 C  C6  . OLA   K  4 .   ? -34.901 5.391   0.464  1.00 37.43  ? 1210 OLA   A C6  1 
HETATM 3225 C  C7  . OLA   K  4 .   ? -34.295 4.104   1.009  1.00 44.80  ? 1210 OLA   A C7  1 
HETATM 3226 C  C8  . OLA   K  4 .   ? -34.652 2.927   0.111  1.00 61.67  ? 1210 OLA   A C8  1 
HETATM 3227 C  C9  . OLA   K  4 .   ? -33.469 1.996   0.020  1.00 60.21  ? 1210 OLA   A C9  1 
HETATM 3228 C  C10 . OLA   K  4 .   ? -33.264 1.205   -1.202 1.00 61.11  ? 1210 OLA   A C10 1 
HETATM 3229 C  C1  . OLA   L  4 .   ? -36.597 14.321  13.116 1.00 62.64  ? 1211 OLA   A C1  1 
HETATM 3230 O  O1  . OLA   L  4 .   ? -36.154 15.488  13.039 1.00 67.10  ? 1211 OLA   A O1  1 
HETATM 3231 O  O2  . OLA   L  4 .   ? -37.637 14.111  13.777 1.00 60.00  ? 1211 OLA   A O2  1 
HETATM 3232 C  C2  . OLA   L  4 .   ? -35.881 13.186  12.422 1.00 61.00  ? 1211 OLA   A C2  1 
HETATM 3233 C  C3  . OLA   L  4 .   ? -36.400 11.848  12.937 1.00 45.15  ? 1211 OLA   A C3  1 
HETATM 3234 C  C4  . OLA   L  4 .   ? -35.848 10.701  12.098 1.00 47.69  ? 1211 OLA   A C4  1 
HETATM 3235 C  C5  . OLA   L  4 .   ? -36.752 9.476   12.174 1.00 41.32  ? 1211 OLA   A C5  1 
HETATM 3236 C  C6  . OLA   L  4 .   ? -36.161 8.294   11.413 1.00 41.54  ? 1211 OLA   A C6  1 
HETATM 3237 C  C7  . OLA   L  4 .   ? -36.553 6.977   12.074 1.00 40.87  ? 1211 OLA   A C7  1 
HETATM 3238 C  C8  . OLA   L  4 .   ? -36.018 5.768   11.314 1.00 46.09  ? 1211 OLA   A C8  1 
HETATM 3239 C  C9  . OLA   L  4 .   ? -36.823 5.583   10.050 1.00 63.96  ? 1211 OLA   A C9  1 
HETATM 3240 C  C10 . OLA   L  4 .   ? -37.487 4.302   9.761  1.00 55.52  ? 1211 OLA   A C10 1 
HETATM 3241 C  C11 . OLA   L  4 .   ? -36.788 2.985   10.004 1.00 61.37  ? 1211 OLA   A C11 1 
HETATM 3242 C  C12 . OLA   L  4 .   ? -37.797 1.848   9.872  1.00 62.02  ? 1211 OLA   A C12 1 
HETATM 3243 C  C13 . OLA   L  4 .   ? -38.840 1.916   10.982 1.00 62.15  ? 1211 OLA   A C13 1 
HETATM 3244 C  C14 . OLA   L  4 .   ? -39.432 0.542   11.277 1.00 67.14  ? 1211 OLA   A C14 1 
HETATM 3245 C  C15 . OLA   L  4 .   ? -38.505 -0.299  12.147 1.00 62.59  ? 1211 OLA   A C15 1 
HETATM 3246 C  C16 . OLA   L  4 .   ? -39.173 -1.614  12.537 1.00 64.98  ? 1211 OLA   A C16 1 
HETATM 3247 C  C17 . OLA   L  4 .   ? -39.178 -2.600  11.374 1.00 70.98  ? 1211 OLA   A C17 1 
HETATM 3248 C  C18 . OLA   L  4 .   ? -40.127 -3.762  11.646 1.00 60.02  ? 1211 OLA   A C18 1 
HETATM 3249 C  C1  . OLA   M  4 .   ? -1.821  12.236  25.782 1.00 51.42  ? 1212 OLA   A C1  1 
HETATM 3250 O  O1  . OLA   M  4 .   ? -2.379  13.354  25.734 1.00 56.02  ? 1212 OLA   A O1  1 
HETATM 3251 O  O2  . OLA   M  4 .   ? -0.786  12.106  26.471 1.00 55.58  ? 1212 OLA   A O2  1 
HETATM 3252 C  C2  . OLA   M  4 .   ? -2.393  11.066  25.016 1.00 39.09  ? 1212 OLA   A C2  1 
HETATM 3253 C  C3  . OLA   M  4 .   ? -2.236  9.779   25.820 1.00 34.93  ? 1212 OLA   A C3  1 
HETATM 3254 C  C4  . OLA   M  4 .   ? -2.392  8.554   24.924 1.00 33.20  ? 1212 OLA   A C4  1 
HETATM 3255 C  C5  . OLA   M  4 .   ? -2.535  7.282   25.754 1.00 28.82  ? 1212 OLA   A C5  1 
HETATM 3256 C  C6  . OLA   M  4 .   ? -3.251  6.169   24.993 1.00 27.63  ? 1212 OLA   A C6  1 
HETATM 3257 C  C7  . OLA   M  4 .   ? -2.803  4.803   25.504 1.00 37.61  ? 1212 OLA   A C7  1 
HETATM 3258 C  C8  . OLA   M  4 .   ? -3.553  3.644   24.853 1.00 35.53  ? 1212 OLA   A C8  1 
HETATM 3259 C  C9  . OLA   M  4 .   ? -2.735  2.386   25.044 1.00 44.71  ? 1212 OLA   A C9  1 
HETATM 3260 C  C10 . OLA   M  4 .   ? -3.145  1.092   24.474 1.00 44.85  ? 1212 OLA   A C10 1 
HETATM 3261 C  C11 . OLA   M  4 .   ? -3.871  0.069   25.318 1.00 51.89  ? 1212 OLA   A C11 1 
HETATM 3262 C  C12 . OLA   M  4 .   ? -4.239  -1.141  24.463 1.00 61.89  ? 1212 OLA   A C12 1 
HETATM 3263 C  C13 . OLA   M  4 .   ? -3.687  -2.436  25.050 1.00 72.60  ? 1212 OLA   A C13 1 
HETATM 3264 C  C14 . OLA   M  4 .   ? -3.884  -3.602  24.088 1.00 59.88  ? 1212 OLA   A C14 1 
HETATM 3265 C  C1  . OLA   N  4 .   ? -40.441 11.106  8.932  1.00 70.13  ? 1213 OLA   A C1  1 
HETATM 3266 O  O1  . OLA   N  4 .   ? -40.902 12.267  8.892  1.00 74.34  ? 1213 OLA   A O1  1 
HETATM 3267 O  O2  . OLA   N  4 .   ? -39.246 10.940  9.259  1.00 57.93  ? 1213 OLA   A O2  1 
HETATM 3268 C  C2  . OLA   N  4 .   ? -41.309 9.921   8.588  1.00 64.73  ? 1213 OLA   A C2  1 
HETATM 3269 C  C3  . OLA   N  4 .   ? -40.841 8.715   9.392  1.00 60.47  ? 1213 OLA   A C3  1 
HETATM 3270 C  C4  . OLA   N  4 .   ? -40.545 7.532   8.479  1.00 59.17  ? 1213 OLA   A C4  1 
HETATM 3271 C  C5  . OLA   N  4 .   ? -41.812 7.037   7.793  1.00 52.50  ? 1213 OLA   A C5  1 
HETATM 3272 C  C6  . OLA   N  4 .   ? -41.647 5.588   7.353  1.00 66.94  ? 1213 OLA   A C6  1 
HETATM 3273 C  C7  . OLA   N  4 .   ? -42.991 4.888   7.212  1.00 67.76  ? 1213 OLA   A C7  1 
HETATM 3274 C  C8  . OLA   N  4 .   ? -42.778 3.400   6.967  1.00 78.77  ? 1213 OLA   A C8  1 
HETATM 3275 C  C9  . OLA   N  4 .   ? -44.021 2.660   7.387  1.00 69.67  ? 1213 OLA   A C9  1 
HETATM 3276 C  C10 . OLA   N  4 .   ? -43.970 1.766   8.550  1.00 68.89  ? 1213 OLA   A C10 1 
HETATM 3277 C  C11 . OLA   N  4 .   ? -42.747 0.929   8.836  1.00 57.35  ? 1213 OLA   A C11 1 
HETATM 3278 C  C12 . OLA   N  4 .   ? -43.094 -0.034  9.965  1.00 67.00  ? 1213 OLA   A C12 1 
HETATM 3279 C  C13 . OLA   N  4 .   ? -42.227 -1.288  9.961  1.00 77.38  ? 1213 OLA   A C13 1 
HETATM 3280 C  C14 . OLA   N  4 .   ? -41.535 -1.520  8.622  1.00 80.40  ? 1213 OLA   A C14 1 
HETATM 3281 C  C10 . OLC   O  5 .   ? -34.139 -9.906  23.196 1.00 52.73  ? 1214 OLC   A C10 1 
HETATM 3282 C  C9  . OLC   O  5 .   ? -33.812 -11.209 23.171 1.00 54.35  ? 1214 OLC   A C9  1 
HETATM 3283 C  C11 . OLC   O  5 .   ? -33.422 -9.129  24.327 1.00 42.03  ? 1214 OLC   A C11 1 
HETATM 3284 C  C8  . OLC   O  5 .   ? -33.047 -12.459 23.691 1.00 45.98  ? 1214 OLC   A C8  1 
HETATM 3285 C  C24 . OLC   O  5 .   ? -31.821 -24.474 24.981 1.00 61.20  ? 1214 OLC   A C24 1 
HETATM 3286 C  C12 . OLC   O  5 .   ? -33.739 -7.613  24.188 1.00 37.94  ? 1214 OLC   A C12 1 
HETATM 3287 C  C7  . OLC   O  5 .   ? -33.136 -13.589 22.631 1.00 38.03  ? 1214 OLC   A C7  1 
HETATM 3288 C  C6  . OLC   O  5 .   ? -32.168 -14.744 23.016 1.00 44.27  ? 1214 OLC   A C6  1 
HETATM 3289 C  C5  . OLC   O  5 .   ? -32.275 -15.886 21.965 1.00 48.63  ? 1214 OLC   A C5  1 
HETATM 3290 C  C4  . OLC   O  5 .   ? -32.633 -17.220 22.682 1.00 50.11  ? 1214 OLC   A C4  1 
HETATM 3291 C  C3  . OLC   O  5 .   ? -31.600 -18.311 22.280 1.00 36.77  ? 1214 OLC   A C3  1 
HETATM 3292 C  C2  . OLC   O  5 .   ? -31.600 -19.452 23.332 1.00 47.24  ? 1214 OLC   A C2  1 
HETATM 3293 C  C21 . OLC   O  5 .   ? -32.664 -22.205 24.307 1.00 64.08  ? 1214 OLC   A C21 1 
HETATM 3294 C  C1  . OLC   O  5 .   ? -31.760 -20.808 22.607 1.00 54.72  ? 1214 OLC   A C1  1 
HETATM 3295 C  C22 . OLC   O  5 .   ? -33.016 -23.695 24.420 1.00 68.72  ? 1214 OLC   A C22 1 
HETATM 3296 O  O19 . OLC   O  5 .   ? -31.964 -20.829 21.436 1.00 67.61  ? 1214 OLC   A O19 1 
HETATM 3297 O  O25 . OLC   O  5 .   ? -32.229 -25.783 25.312 1.00 61.78  ? 1214 OLC   A O25 1 
HETATM 3298 O  O23 . OLC   O  5 .   ? -34.108 -23.852 25.275 1.00 76.84  ? 1214 OLC   A O23 1 
HETATM 3299 O  O20 . OLC   O  5 .   ? -31.661 -22.024 23.325 1.00 72.84  ? 1214 OLC   A O20 1 
HETATM 3300 C  C1  . OLB   P  6 .   ? -3.723  5.548   29.630 1.00 70.03  ? 1215 OLB   A C1  1 
HETATM 3301 C  C2  . OLB   P  6 .   ? -4.233  4.311   30.317 1.00 52.77  ? 1215 OLB   A C2  1 
HETATM 3302 C  C3  . OLB   P  6 .   ? -4.641  3.205   29.358 1.00 61.73  ? 1215 OLB   A C3  1 
HETATM 3303 C  C4  . OLB   P  6 .   ? -4.165  1.837   29.831 1.00 53.54  ? 1215 OLB   A C4  1 
HETATM 3304 C  C5  . OLB   P  6 .   ? -4.938  0.684   29.203 1.00 60.38  ? 1215 OLB   A C5  1 
HETATM 3305 O  O19 . OLB   P  6 .   ? -3.003  5.557   28.663 1.00 78.70  ? 1215 OLB   A O19 1 
HETATM 3306 O  O20 . OLB   P  6 .   ? -4.163  6.657   30.215 1.00 72.26  ? 1215 OLB   A O20 1 
HETATM 3307 C  C21 . OLB   P  6 .   ? -3.290  7.786   30.231 1.00 61.90  ? 1215 OLB   A C21 1 
HETATM 3308 C  C22 . OLB   P  6 .   ? -4.139  9.030   30.426 1.00 67.32  ? 1215 OLB   A C22 1 
HETATM 3309 O  O23 . OLB   P  6 .   ? -3.518  9.969   31.269 1.00 89.45  ? 1215 OLB   A O23 1 
HETATM 3310 C  C24 . OLB   P  6 .   ? -4.495  9.608   29.064 1.00 65.98  ? 1215 OLB   A C24 1 
HETATM 3311 O  O25 . OLB   P  6 .   ? -5.269  10.766  29.252 1.00 81.41  ? 1215 OLB   A O25 1 
HETATM 3312 C  C6  . OLB   P  6 .   ? -4.112  -0.592  29.100 1.00 75.80  ? 1215 OLB   A C6  1 
HETATM 3313 C  C7  . OLB   P  6 .   ? -4.946  -1.856  28.941 1.00 72.89  ? 1215 OLB   A C7  1 
HETATM 3314 C  C8  . OLB   P  6 .   ? -5.937  -1.783  27.778 1.00 54.87  ? 1215 OLB   A C8  1 
HETATM 3315 C  C9  . OLB   P  6 .   ? -6.669  -3.073  27.571 1.00 57.98  ? 1215 OLB   A C9  1 
HETATM 3316 C  C10 . OLB   P  6 .   ? -6.291  -4.111  26.826 1.00 57.32  ? 1215 OLB   A C10 1 
HETATM 3317 C  C18 . OLC   Q  5 .   ? -41.532 -5.067  14.890 1.00 78.23  ? 1216 OLC   A C18 1 
HETATM 3318 C  C10 . OLC   Q  5 .   ? -38.719 3.345   14.589 1.00 56.31  ? 1216 OLC   A C10 1 
HETATM 3319 C  C9  . OLC   Q  5 .   ? -38.053 4.349   15.177 1.00 43.21  ? 1216 OLC   A C9  1 
HETATM 3320 C  C17 . OLC   Q  5 .   ? -40.694 -3.832  15.282 1.00 72.71  ? 1216 OLC   A C17 1 
HETATM 3321 C  C11 . OLC   Q  5 .   ? -38.337 1.978   15.205 1.00 40.26  ? 1216 OLC   A C11 1 
HETATM 3322 C  C8  . OLC   Q  5 .   ? -37.043 4.902   16.219 1.00 31.93  ? 1216 OLC   A C8  1 
HETATM 3323 C  C24 . OLC   Q  5 .   ? -39.550 16.412  20.001 1.00 64.69  ? 1216 OLC   A C24 1 
HETATM 3324 C  C16 . OLC   Q  5 .   ? -41.539 -2.911  16.194 1.00 70.79  ? 1216 OLC   A C16 1 
HETATM 3325 C  C12 . OLC   Q  5 .   ? -39.620 1.116   15.357 1.00 60.79  ? 1216 OLC   A C12 1 
HETATM 3326 C  C7  . OLC   Q  5 .   ? -37.033 6.448   16.129 1.00 49.49  ? 1216 OLC   A C7  1 
HETATM 3327 C  C15 . OLC   Q  5 .   ? -41.160 -1.431  15.935 1.00 72.65  ? 1216 OLC   A C15 1 
HETATM 3328 C  C13 . OLC   Q  5 .   ? -39.579 0.375   16.721 1.00 48.81  ? 1216 OLC   A C13 1 
HETATM 3329 C  C6  . OLC   Q  5 .   ? -37.986 7.036   17.206 1.00 46.13  ? 1216 OLC   A C6  1 
HETATM 3330 C  C14 . OLC   Q  5 .   ? -39.733 -1.151  16.473 1.00 64.14  ? 1216 OLC   A C14 1 
HETATM 3331 C  C5  . OLC   Q  5 .   ? -37.485 8.455   17.584 1.00 39.25  ? 1216 OLC   A C5  1 
HETATM 3332 C  C4  . OLC   Q  5 .   ? -38.184 9.516   16.688 1.00 34.08  ? 1216 OLC   A C4  1 
HETATM 3333 C  C3  . OLC   Q  5 .   ? -38.057 10.893  17.394 1.00 43.07  ? 1216 OLC   A C3  1 
HETATM 3334 C  C2  . OLC   Q  5 .   ? -38.655 12.022  16.515 1.00 54.04  ? 1216 OLC   A C2  1 
HETATM 3335 C  C21 . OLC   Q  5 .   ? -40.167 15.214  17.895 1.00 59.36  ? 1216 OLC   A C21 1 
HETATM 3336 C  C1  . OLC   Q  5 .   ? -39.305 13.059  17.458 1.00 62.25  ? 1216 OLC   A C1  1 
HETATM 3337 C  C22 . OLC   Q  5 .   ? -39.480 16.459  18.471 1.00 75.01  ? 1216 OLC   A C22 1 
HETATM 3338 O  O19 . OLC   Q  5 .   ? -39.872 12.687  18.435 1.00 58.49  ? 1216 OLC   A O19 1 
HETATM 3339 O  O25 . OLC   Q  5 .   ? -39.609 17.725  20.512 1.00 70.04  ? 1216 OLC   A O25 1 
HETATM 3340 O  O23 . OLC   Q  5 .   ? -38.143 16.482  18.068 1.00 63.76  ? 1216 OLC   A O23 1 
HETATM 3341 O  O20 . OLC   Q  5 .   ? -39.226 14.441  17.174 1.00 53.93  ? 1216 OLC   A O20 1 
HETATM 3342 C  C1  . OLA   R  4 .   ? -35.934 -15.595 5.023  1.00 76.46  ? 1217 OLA   A C1  1 
HETATM 3343 O  O1  . OLA   R  4 .   ? -35.725 -16.823 5.126  1.00 75.46  ? 1217 OLA   A O1  1 
HETATM 3344 O  O2  . OLA   R  4 .   ? -36.891 -15.089 5.648  1.00 73.77  ? 1217 OLA   A O2  1 
HETATM 3345 C  C2  . OLA   R  4 .   ? -35.041 -14.737 4.159  1.00 68.67  ? 1217 OLA   A C2  1 
HETATM 3346 C  C3  . OLA   R  4 .   ? -33.790 -15.528 3.796  1.00 72.68  ? 1217 OLA   A C3  1 
HETATM 3347 C  C4  . OLA   R  4 .   ? -33.621 -15.645 2.285  1.00 67.76  ? 1217 OLA   A C4  1 
HETATM 3348 C  C5  . OLA   R  4 .   ? -33.002 -14.381 1.699  1.00 54.74  ? 1217 OLA   A C5  1 
HETATM 3349 C  C6  . OLA   R  4 .   ? -31.481 -14.482 1.657  1.00 54.29  ? 1217 OLA   A C6  1 
HETATM 3350 C  C7  . OLA   R  4 .   ? -30.853 -13.721 2.819  1.00 38.09  ? 1217 OLA   A C7  1 
HETATM 3351 C  C8  . OLA   R  4 .   ? -29.448 -13.240 2.477  1.00 48.43  ? 1217 OLA   A C8  1 
HETATM 3352 C  C9  . OLA   R  4 .   ? -28.970 -12.307 3.564  1.00 33.42  ? 1217 OLA   A C9  1 
HETATM 3353 C  C10 . OLA   R  4 .   ? -27.986 -11.260 3.258  1.00 42.36  ? 1217 OLA   A C10 1 
HETATM 3354 C  C1  . OLA   S  4 .   ? -43.247 -25.017 13.274 1.00 67.78  ? 1218 OLA   A C1  1 
HETATM 3355 O  O1  . OLA   S  4 .   ? -44.094 -25.146 12.363 1.00 66.50  ? 1218 OLA   A O1  1 
HETATM 3356 O  O2  . OLA   S  4 .   ? -42.417 -25.931 13.464 1.00 68.88  ? 1218 OLA   A O2  1 
HETATM 3357 C  C2  . OLA   S  4 .   ? -43.221 -23.781 14.141 1.00 56.45  ? 1218 OLA   A C2  1 
HETATM 3358 C  C3  . OLA   S  4 .   ? -43.972 -22.629 13.485 1.00 54.41  ? 1218 OLA   A C3  1 
HETATM 3359 C  C4  . OLA   S  4 .   ? -43.239 -21.304 13.683 1.00 65.60  ? 1218 OLA   A C4  1 
HETATM 3360 C  C5  . OLA   S  4 .   ? -42.618 -21.194 15.071 1.00 51.85  ? 1218 OLA   A C5  1 
HETATM 3361 C  C6  . OLA   S  4 .   ? -41.116 -20.931 15.005 1.00 70.26  ? 1218 OLA   A C6  1 
HETATM 3362 C  C7  . OLA   S  4 .   ? -40.712 -19.937 16.089 1.00 76.39  ? 1218 OLA   A C7  1 
HETATM 3363 C  C8  . OLA   S  4 .   ? -39.301 -19.384 15.908 1.00 67.62  ? 1218 OLA   A C8  1 
HETATM 3364 C  C9  . OLA   S  4 .   ? -38.904 -19.354 14.451 1.00 72.07  ? 1218 OLA   A C9  1 
HETATM 3365 C  C10 . OLA   S  4 .   ? -37.934 -18.350 13.991 1.00 57.73  ? 1218 OLA   A C10 1 
HETATM 3366 C  C11 . OLA   S  4 .   ? -38.332 -16.892 13.995 1.00 66.86  ? 1218 OLA   A C11 1 
HETATM 3367 C  C12 . OLA   S  4 .   ? -37.099 -16.003 13.892 1.00 50.08  ? 1218 OLA   A C12 1 
HETATM 3368 C  C13 . OLA   S  4 .   ? -37.472 -14.615 13.382 1.00 53.89  ? 1218 OLA   A C13 1 
HETATM 3369 C  C14 . OLA   S  4 .   ? -37.613 -13.601 14.512 1.00 54.88  ? 1218 OLA   A C14 1 
HETATM 3370 C  C15 . OLA   S  4 .   ? -38.220 -12.304 13.989 1.00 58.55  ? 1218 OLA   A C15 1 
HETATM 3371 C  C16 . OLA   S  4 .   ? -37.887 -11.127 14.898 1.00 69.77  ? 1218 OLA   A C16 1 
HETATM 3372 C  C17 . OLA   S  4 .   ? -38.554 -9.849  14.401 1.00 56.73  ? 1218 OLA   A C17 1 
HETATM 3373 C  C1  . OLA   T  4 .   ? -33.401 -18.654 27.050 1.00 56.40  ? 1219 OLA   A C1  1 
HETATM 3374 C  C2  . OLA   T  4 .   ? -33.759 -17.233 27.472 1.00 48.41  ? 1219 OLA   A C2  1 
HETATM 3375 C  C3  . OLA   T  4 .   ? -32.732 -16.233 26.952 1.00 49.26  ? 1219 OLA   A C3  1 
HETATM 3376 C  C4  . OLA   T  4 .   ? -33.407 -14.936 26.522 1.00 51.22  ? 1219 OLA   A C4  1 
HETATM 3377 C  C5  . OLA   T  4 .   ? -33.304 -13.858 27.597 1.00 39.95  ? 1219 OLA   A C5  1 
HETATM 3378 C  C6  . OLA   T  4 .   ? -34.413 -12.859 27.370 1.00 67.15  ? 1219 OLA   A C6  1 
HETATM 3379 C  C7  . OLA   T  4 .   ? -34.233 -11.424 27.639 1.00 62.72  ? 1219 OLA   A C7  1 
HETATM 3380 C  C8  . OLA   T  4 .   ? -33.747 -10.920 28.977 1.00 50.92  ? 1219 OLA   A C8  1 
HETATM 3381 C  C9  . OLA   T  4 .   ? -33.890 -9.401  28.999 1.00 40.48  ? 1219 OLA   A C9  1 
HETATM 3382 C  C10 . OLA   T  4 .   ? -33.329 -8.799  30.281 1.00 50.01  ? 1219 OLA   A C10 1 
HETATM 3383 C  C11 . OLA   T  4 .   ? -33.291 -7.278  30.194 1.00 52.05  ? 1219 OLA   A C11 1 
HETATM 3384 C  C12 . OLA   T  4 .   ? -34.238 -6.621  31.191 1.00 59.34  ? 1219 OLA   A C12 1 
HETATM 3385 C  C13 . OLA   T  4 .   ? -33.545 -5.465  31.903 1.00 52.58  ? 1219 OLA   A C13 1 
HETATM 3386 C  C14 . OLA   T  4 .   ? -32.226 -5.920  32.517 1.00 52.83  ? 1219 OLA   A C14 1 
HETATM 3387 C  C15 . OLA   T  4 .   ? -31.551 -4.784  33.277 1.00 45.33  ? 1219 OLA   A C15 1 
HETATM 3388 C  C9  . OLA   U  4 .   ? -8.436  -16.099 16.021 1.00 44.00  ? 1220 OLA   A C9  1 
HETATM 3389 C  C10 . OLA   U  4 .   ? -8.844  -14.887 16.746 1.00 49.45  ? 1220 OLA   A C10 1 
HETATM 3390 C  C11 . OLA   U  4 .   ? -10.223 -14.803 17.353 1.00 34.56  ? 1220 OLA   A C11 1 
HETATM 3391 C  C12 . OLA   U  4 .   ? -10.310 -13.583 18.264 1.00 40.89  ? 1220 OLA   A C12 1 
HETATM 3392 C  C13 . OLA   U  4 .   ? -10.594 -12.316 17.466 1.00 47.76  ? 1220 OLA   A C13 1 
HETATM 3393 C  C14 . OLA   U  4 .   ? -9.959  -11.090 18.111 1.00 34.17  ? 1220 OLA   A C14 1 
HETATM 3394 C  C15 . OLA   U  4 .   ? -8.699  -10.660 17.370 1.00 51.00  ? 1220 OLA   A C15 1 
HETATM 3395 C  C16 . OLA   U  4 .   ? -8.379  -9.200  17.667 1.00 50.54  ? 1220 OLA   A C16 1 
HETATM 3396 C  C17 . OLA   U  4 .   ? -7.951  -9.019  19.119 1.00 48.02  ? 1220 OLA   A C17 1 
HETATM 3397 C  C18 . OLA   U  4 .   ? -8.085  -7.563  19.549 1.00 52.35  ? 1220 OLA   A C18 1 
HETATM 3398 C  C1  . OLA   V  4 .   ? -8.391  14.059  7.731  1.00 63.16  ? 1221 OLA   A C1  1 
HETATM 3399 O  O1  . OLA   V  4 .   ? -8.755  14.849  6.833  1.00 72.35  ? 1221 OLA   A O1  1 
HETATM 3400 O  O2  . OLA   V  4 .   ? -8.361  14.457  8.916  1.00 63.21  ? 1221 OLA   A O2  1 
HETATM 3401 C  C2  . OLA   V  4 .   ? -7.990  12.645  7.390  1.00 53.27  ? 1221 OLA   A C2  1 
HETATM 3402 C  C3  . OLA   V  4 .   ? -9.228  11.865  6.967  1.00 42.47  ? 1221 OLA   A C3  1 
HETATM 3403 C  C4  . OLA   V  4 .   ? -9.037  11.227  5.596  1.00 53.17  ? 1221 OLA   A C4  1 
HETATM 3404 C  C5  . OLA   V  4 .   ? -9.232  9.716   5.663  1.00 47.84  ? 1221 OLA   A C5  1 
HETATM 3405 C  C6  . OLA   V  4 .   ? -8.659  9.131   6.950  1.00 53.59  ? 1221 OLA   A C6  1 
HETATM 3406 C  C7  . OLA   V  4 .   ? -7.425  8.285   6.661  1.00 50.55  ? 1221 OLA   A C7  1 
HETATM 3407 C  C8  . OLA   V  4 .   ? -7.703  7.344   5.497  1.00 61.37  ? 1221 OLA   A C8  1 
HETATM 3408 C  C9  . OLA   V  4 .   ? -8.525  6.177   5.989  1.00 59.84  ? 1221 OLA   A C9  1 
HETATM 3409 C  C10 . OLA   V  4 .   ? -9.493  5.537   5.087  1.00 64.11  ? 1221 OLA   A C10 1 
HETATM 3410 C  C11 . OLA   V  4 .   ? -10.735 6.292   4.677  1.00 55.84  ? 1221 OLA   A C11 1 
HETATM 3411 C  C12 . OLA   V  4 .   ? -11.256 5.747   3.353  1.00 62.06  ? 1221 OLA   A C12 1 
HETATM 3412 C  C13 . OLA   V  4 .   ? -11.371 4.229   3.391  1.00 55.31  ? 1221 OLA   A C13 1 
HETATM 3413 C  C1  . OLA   W  4 .   ? -28.111 -20.584 39.880 1.00 70.22  ? 1222 OLA   A C1  1 
HETATM 3414 O  O1  . OLA   W  4 .   ? -27.742 -21.730 39.543 1.00 65.32  ? 1222 OLA   A O1  1 
HETATM 3415 O  O2  . OLA   W  4 .   ? -29.163 -20.458 40.543 1.00 80.61  ? 1222 OLA   A O2  1 
HETATM 3416 C  C2  . OLA   W  4 .   ? -27.297 -19.372 39.493 1.00 68.00  ? 1222 OLA   A C2  1 
HETATM 3417 C  C3  . OLA   W  4 .   ? -28.086 -18.103 39.793 1.00 69.70  ? 1222 OLA   A C3  1 
HETATM 3418 C  C4  . OLA   W  4 .   ? -27.672 -16.966 38.865 1.00 63.73  ? 1222 OLA   A C4  1 
HETATM 3419 C  C5  . OLA   W  4 .   ? -26.177 -16.686 38.973 1.00 65.71  ? 1222 OLA   A C5  1 
HETATM 3420 C  C6  . OLA   W  4 .   ? -25.861 -15.241 38.601 1.00 49.68  ? 1222 OLA   A C6  1 
HETATM 3421 C  C7  . OLA   W  4 .   ? -24.417 -15.086 38.134 1.00 52.66  ? 1222 OLA   A C7  1 
HETATM 3422 C  C8  . OLA   W  4 .   ? -24.021 -13.615 38.054 1.00 52.51  ? 1222 OLA   A C8  1 
HETATM 3423 C  C9  . OLA   W  4 .   ? -24.529 -12.900 39.283 1.00 69.57  ? 1222 OLA   A C9  1 
HETATM 3424 C  C10 . OLA   W  4 .   ? -24.752 -11.447 39.292 1.00 61.33  ? 1222 OLA   A C10 1 
HETATM 3425 C  C11 . OLA   W  4 .   ? -23.671 -10.482 38.869 1.00 65.71  ? 1222 OLA   A C11 1 
HETATM 3426 C  C12 . OLA   W  4 .   ? -24.230 -9.065  38.941 1.00 62.46  ? 1222 OLA   A C12 1 
HETATM 3427 C  C13 . OLA   W  4 .   ? -23.335 -8.151  39.767 1.00 44.77  ? 1222 OLA   A C13 1 
HETATM 3428 C  C14 . OLA   W  4 .   ? -22.386 -7.371  38.865 1.00 47.78  ? 1222 OLA   A C14 1 
HETATM 3429 C  C15 . OLA   W  4 .   ? -23.159 -6.402  37.979 1.00 51.77  ? 1222 OLA   A C15 1 
HETATM 3430 C  C16 . OLA   W  4 .   ? -22.228 -5.710  36.992 1.00 46.45  ? 1222 OLA   A C16 1 
HETATM 3431 C  C17 . OLA   W  4 .   ? -22.841 -4.408  36.490 1.00 40.61  ? 1222 OLA   A C17 1 
HETATM 3432 C  C18 . OLA   W  4 .   ? -21.905 -3.704  35.516 1.00 36.68  ? 1222 OLA   A C18 1 
HETATM 3433 C  C1  . OLA   X  4 .   ? -36.894 10.437  29.442 1.00 78.20  ? 1223 OLA   A C1  1 
HETATM 3434 O  O1  . OLA   X  4 .   ? -36.503 11.505  28.923 1.00 64.80  ? 1223 OLA   A O1  1 
HETATM 3435 O  O2  . OLA   X  4 .   ? -37.189 10.427  30.657 1.00 82.83  ? 1223 OLA   A O2  1 
HETATM 3436 C  C2  . OLA   X  4 .   ? -37.019 9.181   28.612 1.00 68.66  ? 1223 OLA   A C2  1 
HETATM 3437 C  C3  . OLA   X  4 .   ? -36.261 8.042   29.285 1.00 64.23  ? 1223 OLA   A C3  1 
HETATM 3438 C  C4  . OLA   X  4 .   ? -37.189 7.211   30.164 1.00 71.56  ? 1223 OLA   A C4  1 
HETATM 3439 C  C5  . OLA   X  4 .   ? -38.224 6.464   29.333 1.00 63.29  ? 1223 OLA   A C5  1 
HETATM 3440 C  C6  . OLA   X  4 .   ? -37.857 4.991   29.200 1.00 67.22  ? 1223 OLA   A C6  1 
HETATM 3441 C  C7  . OLA   X  4 .   ? -39.105 4.120   29.112 1.00 57.58  ? 1223 OLA   A C7  1 
HETATM 3442 C  C8  . OLA   X  4 .   ? -38.732 2.660   28.880 1.00 61.44  ? 1223 OLA   A C8  1 
HETATM 3443 C  C9  . OLA   X  4 .   ? -37.600 2.602   27.881 1.00 54.71  ? 1223 OLA   A C9  1 
HETATM 3444 C  C10 . OLA   X  4 .   ? -37.512 1.507   26.905 1.00 64.05  ? 1223 OLA   A C10 1 
HETATM 3445 C  C11 . OLA   X  4 .   ? -37.930 0.108   27.287 1.00 63.66  ? 1223 OLA   A C11 1 
HETATM 3446 C  C1  . OLA   Y  4 .   ? -34.301 -21.805 17.799 1.00 62.79  ? 1224 OLA   A C1  1 
HETATM 3447 O  O1  . OLA   Y  4 .   ? -33.323 -21.664 17.033 1.00 64.17  ? 1224 OLA   A O1  1 
HETATM 3448 O  O2  . OLA   Y  4 .   ? -34.200 -22.574 18.778 1.00 66.78  ? 1224 OLA   A O2  1 
HETATM 3449 C  C2  . OLA   Y  4 .   ? -35.584 -21.049 17.551 1.00 63.20  ? 1224 OLA   A C2  1 
HETATM 3450 C  C3  . OLA   Y  4 .   ? -35.902 -20.184 18.764 1.00 60.66  ? 1224 OLA   A C3  1 
HETATM 3451 C  C4  . OLA   Y  4 .   ? -35.130 -18.874 18.702 1.00 59.54  ? 1224 OLA   A C4  1 
HETATM 3452 C  C5  . OLA   Y  4 .   ? -35.305 -18.206 17.343 1.00 51.54  ? 1224 OLA   A C5  1 
HETATM 3453 C  C6  . OLA   Y  4 .   ? -35.432 -16.692 17.462 1.00 55.46  ? 1224 OLA   A C6  1 
HETATM 3454 C  C7  . OLA   Y  4 .   ? -34.786 -16.164 18.738 1.00 41.35  ? 1224 OLA   A C7  1 
HETATM 3455 C  C8  . OLA   Y  4 .   ? -35.389 -14.814 19.092 1.00 54.83  ? 1224 OLA   A C8  1 
HETATM 3456 C  C9  . OLA   Y  4 .   ? -35.180 -13.890 17.919 1.00 40.24  ? 1224 OLA   A C9  1 
HETATM 3457 C  C10 . OLA   Y  4 .   ? -35.801 -12.562 17.932 1.00 38.56  ? 1224 OLA   A C10 1 
HETATM 3458 C  C11 . OLA   Y  4 .   ? -34.979 -11.331 17.651 1.00 44.09  ? 1224 OLA   A C11 1 
HETATM 3459 C  C12 . OLA   Y  4 .   ? -35.731 -10.133 18.211 1.00 60.00  ? 1224 OLA   A C12 1 
HETATM 3460 C  C1  . OLA   Z  4 .   ? -15.401 13.088  0.916  1.00 57.91  ? 1225 OLA   A C1  1 
HETATM 3461 O  O1  . OLA   Z  4 .   ? -14.188 13.238  0.652  1.00 52.70  ? 1225 OLA   A O1  1 
HETATM 3462 O  O2  . OLA   Z  4 .   ? -16.101 14.098  1.147  1.00 54.78  ? 1225 OLA   A O2  1 
HETATM 3463 C  C2  . OLA   Z  4 .   ? -16.014 11.708  0.955  1.00 44.52  ? 1225 OLA   A C2  1 
HETATM 3464 C  C3  . OLA   Z  4 .   ? -14.938 10.652  0.725  1.00 45.60  ? 1225 OLA   A C3  1 
HETATM 3465 C  C4  . OLA   Z  4 .   ? -15.548 9.342   0.238  1.00 55.02  ? 1225 OLA   A C4  1 
HETATM 3466 C  C5  . OLA   Z  4 .   ? -16.781 8.988   1.064  1.00 51.84  ? 1225 OLA   A C5  1 
HETATM 3467 C  C6  . OLA   Z  4 .   ? -17.083 7.492   1.087  1.00 59.08  ? 1225 OLA   A C6  1 
HETATM 3468 C  C7  . OLA   Z  4 .   ? -15.840 6.623   0.931  1.00 54.54  ? 1225 OLA   A C7  1 
HETATM 3469 C  C8  . OLA   Z  4 .   ? -16.243 5.193   0.588  1.00 66.11  ? 1225 OLA   A C8  1 
HETATM 3470 C  C9  . OLA   Z  4 .   ? -15.094 4.252   0.864  1.00 56.05  ? 1225 OLA   A C9  1 
HETATM 3471 C  C10 . OLA   Z  4 .   ? -15.154 2.862   0.390  1.00 56.78  ? 1225 OLA   A C10 1 
HETATM 3472 C  C11 . OLA   Z  4 .   ? -16.459 2.101   0.435  1.00 66.52  ? 1225 OLA   A C11 1 
HETATM 3473 C  C1  . OLA   AA 4 .   ? -34.793 9.600   33.443 1.00 75.87  ? 1226 OLA   A C1  1 
HETATM 3474 O  O1  . OLA   AA 4 .   ? -35.990 9.466   33.112 1.00 72.79  ? 1226 OLA   A O1  1 
HETATM 3475 O  O2  . OLA   AA 4 .   ? -34.380 10.728  33.793 1.00 76.55  ? 1226 OLA   A O2  1 
HETATM 3476 C  C2  . OLA   AA 4 .   ? -33.856 8.417   33.438 1.00 67.89  ? 1226 OLA   A C2  1 
HETATM 3477 C  C3  . OLA   AA 4 .   ? -34.329 7.341   32.466 1.00 53.58  ? 1226 OLA   A C3  1 
HETATM 3478 C  C4  . OLA   AA 4 .   ? -34.633 6.052   33.224 1.00 53.87  ? 1226 OLA   A C4  1 
HETATM 3479 C  C5  . OLA   AA 4 .   ? -34.265 4.802   32.432 1.00 49.83  ? 1226 OLA   A C5  1 
HETATM 3480 C  C6  . OLA   AA 4 .   ? -33.679 3.739   33.358 1.00 58.01  ? 1226 OLA   A C6  1 
HETATM 3481 C  C7  . OLA   AA 4 .   ? -32.678 2.836   32.645 1.00 57.55  ? 1226 OLA   A C7  1 
HETATM 3482 C  C8  . OLA   AA 4 .   ? -31.911 1.970   33.641 1.00 58.60  ? 1226 OLA   A C8  1 
HETATM 3483 C  C9  . OLA   AA 4 .   ? -31.406 0.725   32.950 1.00 47.41  ? 1226 OLA   A C9  1 
HETATM 3484 C  C10 . OLA   AA 4 .   ? -30.933 -0.426  33.735 1.00 43.94  ? 1226 OLA   A C10 1 
HETATM 3485 C  C11 . OLA   AA 4 .   ? -29.943 -1.398  33.138 1.00 40.67  ? 1226 OLA   A C11 1 
HETATM 3486 C  C2  . OLA   BA 4 .   ? -37.164 -6.516  27.865 1.00 54.59  ? 1227 OLA   A C2  1 
HETATM 3487 C  C3  . OLA   BA 4 .   ? -36.318 -5.400  28.465 1.00 56.70  ? 1227 OLA   A C3  1 
HETATM 3488 C  C4  . OLA   BA 4 .   ? -36.568 -4.081  27.743 1.00 67.63  ? 1227 OLA   A C4  1 
HETATM 3489 C  C5  . OLA   BA 4 .   ? -35.599 -2.991  28.189 1.00 57.03  ? 1227 OLA   A C5  1 
HETATM 3490 C  C6  . OLA   BA 4 .   ? -35.327 -3.035  29.689 1.00 62.24  ? 1227 OLA   A C6  1 
HETATM 3491 C  C7  . OLA   BA 4 .   ? -34.419 -1.878  30.087 1.00 50.34  ? 1227 OLA   A C7  1 
HETATM 3492 C  C8  . OLA   BA 4 .   ? -35.121 -0.550  29.832 1.00 60.51  ? 1227 OLA   A C8  1 
HETATM 3493 C  C9  . OLA   BA 4 .   ? -34.316 0.578   30.430 1.00 43.11  ? 1227 OLA   A C9  1 
HETATM 3494 C  C10 . OLC   CA 5 .   ? -37.833 4.733   4.703  1.00 54.59  ? 1228 OLC   A C10 1 
HETATM 3495 C  C9  . OLC   CA 5 .   ? -37.201 5.731   5.342  1.00 60.32  ? 1228 OLC   A C9  1 
HETATM 3496 C  C8  . OLC   CA 5 .   ? -36.749 6.474   6.631  1.00 64.86  ? 1228 OLC   A C8  1 
HETATM 3497 C  C24 . OLC   CA 5 .   ? -29.501 16.573  8.104  1.00 64.54  ? 1228 OLC   A C24 1 
HETATM 3498 C  C7  . OLC   CA 5 .   ? -36.697 8.003   6.374  1.00 57.04  ? 1228 OLC   A C7  1 
HETATM 3499 C  C6  . OLC   CA 5 .   ? -35.824 8.679   7.472  1.00 48.46  ? 1228 OLC   A C6  1 
HETATM 3500 C  C5  . OLC   CA 5 .   ? -36.338 10.124  7.728  1.00 58.00  ? 1228 OLC   A C5  1 
HETATM 3501 C  C4  . OLC   CA 5 .   ? -35.216 10.971  8.395  1.00 60.74  ? 1228 OLC   A C4  1 
HETATM 3502 C  C3  . OLC   CA 5 .   ? -34.803 12.118  7.432  1.00 69.28  ? 1228 OLC   A C3  1 
HETATM 3503 C  C2  . OLC   CA 5 .   ? -34.466 13.395  8.247  1.00 57.72  ? 1228 OLC   A C2  1 
HETATM 3504 C  C21 . OLC   CA 5 .   ? -31.150 14.724  8.483  1.00 59.57  ? 1228 OLC   A C21 1 
HETATM 3505 C  C1  . OLC   CA 5 .   ? -33.260 14.111  7.596  1.00 78.97  ? 1228 OLC   A C1  1 
HETATM 3506 C  C22 . OLC   CA 5 .   ? -30.397 15.887  9.143  1.00 67.66  ? 1228 OLC   A C22 1 
HETATM 3507 O  O19 . OLC   CA 5 .   ? -32.961 13.863  6.472  1.00 84.73  ? 1228 OLC   A O19 1 
HETATM 3508 O  O25 . OLC   CA 5 .   ? -30.006 16.326  6.811  1.00 66.03  ? 1228 OLC   A O25 1 
HETATM 3509 O  O23 . OLC   CA 5 .   ? -31.311 16.812  9.650  1.00 80.71  ? 1228 OLC   A O23 1 
HETATM 3510 O  O20 . OLC   CA 5 .   ? -32.516 15.063  8.331  1.00 67.70  ? 1228 OLC   A O20 1 
HETATM 3511 C  C1  . OLA   DA 4 .   ? -30.899 -17.400 35.643 1.00 74.53  ? 1229 OLA   A C1  1 
HETATM 3512 O  O1  . OLA   DA 4 .   ? -31.587 -17.405 34.599 1.00 68.46  ? 1229 OLA   A O1  1 
HETATM 3513 O  O2  . OLA   DA 4 .   ? -30.481 -18.486 36.099 1.00 73.67  ? 1229 OLA   A O2  1 
HETATM 3514 C  C2  . OLA   DA 4 .   ? -30.572 -16.099 36.337 1.00 78.30  ? 1229 OLA   A C2  1 
HETATM 3515 C  C3  . OLA   DA 4 .   ? -31.619 -15.053 35.974 1.00 71.26  ? 1229 OLA   A C3  1 
HETATM 3516 C  C4  . OLA   DA 4 .   ? -30.970 -13.778 35.447 1.00 62.02  ? 1229 OLA   A C4  1 
HETATM 3517 C  C5  . OLA   DA 4 .   ? -30.641 -12.808 36.577 1.00 52.04  ? 1229 OLA   A C5  1 
HETATM 3518 C  C6  . OLA   DA 4 .   ? -29.152 -12.805 36.907 1.00 56.48  ? 1229 OLA   A C6  1 
HETATM 3519 C  C7  . OLA   DA 4 .   ? -28.400 -11.827 36.012 1.00 52.45  ? 1229 OLA   A C7  1 
HETATM 3520 C  C8  . OLA   DA 4 .   ? -27.103 -11.361 36.662 1.00 53.24  ? 1229 OLA   A C8  1 
HETATM 3521 C  C9  . OLA   DA 4 .   ? -27.365 -10.113 37.472 1.00 55.08  ? 1229 OLA   A C9  1 
HETATM 3522 C  C1  . OLA   EA 4 .   ? -31.911 7.838   36.425 1.00 50.16  ? 1230 OLA   A C1  1 
HETATM 3523 O  O1  . OLA   EA 4 .   ? -31.279 8.901   36.239 1.00 57.51  ? 1230 OLA   A O1  1 
HETATM 3524 O  O2  . OLA   EA 4 .   ? -33.159 7.870   36.450 1.00 57.75  ? 1230 OLA   A O2  1 
HETATM 3525 C  C2  . OLA   EA 4 .   ? -31.184 6.531   36.622 1.00 36.77  ? 1230 OLA   A C2  1 
HETATM 3526 C  C3  . OLA   EA 4 .   ? -31.980 5.425   35.946 1.00 42.13  ? 1230 OLA   A C3  1 
HETATM 3527 C  C4  . OLA   EA 4 .   ? -32.716 4.564   36.966 1.00 37.59  ? 1230 OLA   A C4  1 
HETATM 3528 C  C5  . OLA   EA 4 .   ? -31.791 3.532   37.595 1.00 49.18  ? 1230 OLA   A C5  1 
HETATM 3529 C  C6  . OLA   EA 4 .   ? -32.517 2.206   37.783 1.00 50.21  ? 1230 OLA   A C6  1 
HETATM 3530 C  C7  . OLA   EA 4 .   ? -31.603 1.042   37.423 1.00 45.39  ? 1230 OLA   A C7  1 
HETATM 3531 C  C8  . OLA   EA 4 .   ? -31.081 0.346   38.673 1.00 44.91  ? 1230 OLA   A C8  1 
HETATM 3532 C  C9  . OLA   EA 4 .   ? -30.059 -0.689  38.271 1.00 37.35  ? 1230 OLA   A C9  1 
HETATM 3533 C  C10 . OLA   EA 4 .   ? -30.397 -2.115  38.366 1.00 41.04  ? 1230 OLA   A C10 1 
HETATM 3534 C  C11 . OLA   EA 4 .   ? -31.675 -2.536  39.048 1.00 51.74  ? 1230 OLA   A C11 1 
HETATM 3535 NA NA  . NA    FA 7 .   ? -23.472 -8.473  16.437 1.00 41.76  ? 1231 NA    A NA  1 
HETATM 3536 O  O   . HOH   GA 8 .   ? -9.893  15.328  10.410 1.00 44.50  ? 1301 HOH   A O   1 
HETATM 3537 O  O   . HOH   GA 8 .   ? -4.381  -63.902 26.976 1.00 43.94  ? 1302 HOH   A O   1 
HETATM 3538 O  O   . HOH   GA 8 .   ? 7.987   -73.058 21.896 1.00 53.78  ? 1303 HOH   A O   1 
HETATM 3539 O  O   . HOH   GA 8 .   ? -22.802 -28.438 21.454 1.00 40.64  ? 1304 HOH   A O   1 
HETATM 3540 O  O   . HOH   GA 8 .   ? -6.763  12.035  27.862 1.00 53.72  ? 1305 HOH   A O   1 
HETATM 3541 O  O   . HOH   GA 8 .   ? -4.220  -37.771 20.874 1.00 46.47  ? 1306 HOH   A O   1 
HETATM 3542 O  O   . HOH   GA 8 .   ? -13.030 17.456  11.413 1.00 38.60  ? 1307 HOH   A O   1 
HETATM 3543 O  O   . HOH   GA 8 .   ? -0.685  -63.091 19.811 1.00 40.37  ? 1308 HOH   A O   1 
HETATM 3544 O  O   . HOH   GA 8 .   ? 1.741   -46.609 20.902 1.00 52.62  ? 1309 HOH   A O   1 
HETATM 3545 O  O   . HOH   GA 8 .   ? -2.953  -64.751 20.527 1.00 52.89  ? 1310 HOH   A O   1 
HETATM 3546 O  O   . HOH   GA 8 .   ? -18.048 8.643   18.799 1.00 24.05  ? 1311 HOH   A O   1 
HETATM 3547 O  O   . HOH   GA 8 .   ? -18.659 -11.499 13.051 1.00 20.96  ? 1312 HOH   A O   1 
HETATM 3548 O  O   . HOH   GA 8 .   ? -28.752 2.379   19.753 1.00 23.34  ? 1313 HOH   A O   1 
HETATM 3549 O  O   . HOH   GA 8 .   ? -18.323 12.946  23.656 1.00 32.71  ? 1314 HOH   A O   1 
HETATM 3550 O  O   . HOH   GA 8 .   ? -28.751 12.271  8.910  1.00 48.05  ? 1315 HOH   A O   1 
HETATM 3551 O  O   . HOH   GA 8 .   ? -25.455 2.133   15.834 1.00 21.05  ? 1316 HOH   A O   1 
HETATM 3552 O  O   . HOH   GA 8 .   ? -16.241 -16.993 19.002 1.00 21.89  ? 1317 HOH   A O   1 
HETATM 3553 O  O   . HOH   GA 8 .   ? -31.094 7.427   32.430 1.00 51.00  ? 1318 HOH   A O   1 
HETATM 3554 O  O   . HOH   GA 8 .   ? -25.409 -13.453 13.523 1.00 25.46  ? 1319 HOH   A O   1 
HETATM 3555 O  O   . HOH   GA 8 .   ? -19.384 -1.801  22.283 1.00 22.97  ? 1320 HOH   A O   1 
HETATM 3556 O  O   . HOH   GA 8 .   ? -23.823 14.968  33.329 1.00 41.95  ? 1321 HOH   A O   1 
HETATM 3557 O  O   . HOH   GA 8 .   ? -25.053 -16.027 14.634 1.00 27.04  ? 1322 HOH   A O   1 
HETATM 3558 O  O   B HOH   GA 8 .   ? -9.424  14.816  18.312 0.56 26.39  ? 1323 HOH   A O   1 
HETATM 3559 O  O   . HOH   GA 8 .   ? -16.336 15.216  20.244 1.00 41.23  ? 1324 HOH   A O   1 
HETATM 3560 O  O   . HOH   GA 8 .   ? 2.900   -68.256 18.574 1.00 47.20  ? 1325 HOH   A O   1 
HETATM 3561 O  O   . HOH   GA 8 .   ? -19.206 -35.720 26.824 1.00 55.86  ? 1326 HOH   A O   1 
HETATM 3562 O  O   . HOH   GA 8 .   ? -7.641  10.217  30.502 1.00 50.34  ? 1327 HOH   A O   1 
HETATM 3563 O  O   . HOH   GA 8 .   ? -18.916 10.248  22.870 1.00 32.28  ? 1328 HOH   A O   1 
HETATM 3564 O  O   . HOH   GA 8 .   ? -15.048 10.148  17.805 1.00 29.35  ? 1329 HOH   A O   1 
HETATM 3565 O  O   . HOH   GA 8 .   ? -25.963 -12.421 21.704 1.00 23.68  ? 1330 HOH   A O   1 
HETATM 3566 O  O   . HOH   GA 8 .   ? -26.167 -12.340 25.598 1.00 28.67  ? 1331 HOH   A O   1 
HETATM 3567 O  O   . HOH   GA 8 .   ? -21.770 -33.135 22.244 1.00 53.10  ? 1332 HOH   A O   1 
HETATM 3568 O  O   . HOH   GA 8 .   ? -23.505 -4.942  14.087 1.00 22.11  ? 1333 HOH   A O   1 
HETATM 3569 O  O   . HOH   GA 8 .   ? -16.246 0.495   12.586 1.00 20.36  ? 1334 HOH   A O   1 
HETATM 3570 O  O   . HOH   GA 8 .   ? -36.759 18.053  16.402 1.00 47.48  ? 1335 HOH   A O   1 
HETATM 3571 O  O   . HOH   GA 8 .   ? -26.503 18.321  22.135 1.00 23.54  ? 1336 HOH   A O   1 
HETATM 3572 O  O   . HOH   GA 8 .   ? -13.734 -28.237 19.761 1.00 42.22  ? 1337 HOH   A O   1 
HETATM 3573 O  O   . HOH   GA 8 .   ? -27.638 2.852   16.957 1.00 16.94  ? 1338 HOH   A O   1 
HETATM 3574 O  O   . HOH   GA 8 .   ? -14.226 -27.001 17.518 1.00 36.56  ? 1339 HOH   A O   1 
HETATM 3575 O  O   . HOH   GA 8 .   ? -25.798 7.721   13.347 1.00 24.55  ? 1340 HOH   A O   1 
HETATM 3576 O  O   . HOH   GA 8 .   ? -22.839 0.553   15.619 1.00 30.95  ? 1341 HOH   A O   1 
HETATM 3577 O  O   . HOH   GA 8 .   ? 4.044   -47.503 26.348 1.00 52.73  ? 1342 HOH   A O   1 
HETATM 3578 O  O   . HOH   GA 8 .   ? -24.483 16.634  2.258  1.00 40.08  ? 1343 HOH   A O   1 
HETATM 3579 O  O   . HOH   GA 8 .   ? -25.893 18.714  24.813 1.00 32.74  ? 1344 HOH   A O   1 
HETATM 3580 O  O   . HOH   GA 8 .   ? -16.621 16.621  8.997  1.00 32.29  ? 1345 HOH   A O   1 
HETATM 3581 O  O   . HOH   GA 8 .   ? -18.554 15.630  18.030 1.00 43.59  ? 1346 HOH   A O   1 
HETATM 3582 O  O   . HOH   GA 8 .   ? 5.799   -76.074 26.638 1.00 37.76  ? 1347 HOH   A O   1 
HETATM 3583 O  O   . HOH   GA 8 .   ? -2.065  13.153  22.120 1.00 33.71  ? 1348 HOH   A O   1 
HETATM 3584 O  O   . HOH   GA 8 .   ? -32.419 23.317  26.016 1.00 57.38  ? 1349 HOH   A O   1 
HETATM 3585 O  O   . HOH   GA 8 .   ? -10.082 14.582  25.438 1.00 34.27  ? 1350 HOH   A O   1 
HETATM 3586 O  O   . HOH   GA 8 .   ? -25.708 -14.682 24.706 1.00 28.42  ? 1351 HOH   A O   1 
HETATM 3587 O  O   . HOH   GA 8 .   ? -22.112 -6.613  15.424 1.00 29.19  ? 1352 HOH   A O   1 
HETATM 3588 O  O   . HOH   GA 8 .   ? -23.344 -27.477 -3.686 1.00 68.10  ? 1353 HOH   A O   1 
HETATM 3589 O  O   . HOH   GA 8 .   ? -17.754 -17.609 16.851 1.00 33.62  ? 1354 HOH   A O   1 
HETATM 3590 O  O   . HOH   GA 8 .   ? -15.094 3.467   21.696 1.00 21.73  ? 1355 HOH   A O   1 
HETATM 3591 O  O   . HOH   GA 8 .   ? -27.292 -11.564 6.596  1.00 40.44  ? 1356 HOH   A O   1 
HETATM 3592 O  O   . HOH   GA 8 .   ? -10.286 19.272  20.804 1.00 39.88  ? 1357 HOH   A O   1 
HETATM 3593 O  O   . HOH   GA 8 .   ? -11.250 11.973  15.642 1.00 20.07  ? 1358 HOH   A O   1 
HETATM 3594 O  O   . HOH   GA 8 .   ? -11.127 15.086  23.494 1.00 38.41  ? 1359 HOH   A O   1 
HETATM 3595 O  O   . HOH   GA 8 .   ? -27.851 20.737  22.224 1.00 29.74  ? 1360 HOH   A O   1 
HETATM 3596 O  O   . HOH   GA 8 .   ? -24.047 -11.344 11.466 1.00 29.08  ? 1361 HOH   A O   1 
HETATM 3597 O  O   . HOH   GA 8 .   ? -20.879 -2.817  24.365 1.00 24.96  ? 1362 HOH   A O   1 
HETATM 3598 O  O   . HOH   GA 8 .   ? 3.431   -73.183 24.041 1.00 56.98  ? 1363 HOH   A O   1 
HETATM 3599 O  O   . HOH   GA 8 .   ? -22.332 -10.183 15.252 1.00 36.85  ? 1364 HOH   A O   1 
HETATM 3600 O  O   . HOH   GA 8 .   ? -17.179 11.863  32.568 1.00 40.23  ? 1365 HOH   A O   1 
HETATM 3601 O  O   . HOH   GA 8 .   ? -18.209 -2.985  20.096 1.00 23.55  ? 1366 HOH   A O   1 
HETATM 3602 O  O   . HOH   GA 8 .   ? -20.280 -36.115 29.429 1.00 58.27  ? 1367 HOH   A O   1 
HETATM 3603 O  O   . HOH   GA 8 .   ? -25.118 14.643  7.203  1.00 53.89  ? 1368 HOH   A O   1 
HETATM 3604 O  O   . HOH   GA 8 .   ? -28.052 5.332   17.866 1.00 35.18  ? 1369 HOH   A O   1 
HETATM 3605 O  O   . HOH   GA 8 .   ? -17.621 13.264  26.097 1.00 29.95  ? 1370 HOH   A O   1 
HETATM 3606 O  O   . HOH   GA 8 .   ? -3.907  -64.168 18.157 1.00 46.07  ? 1371 HOH   A O   1 
HETATM 3607 O  O   . HOH   GA 8 .   ? -29.960 17.794  29.456 1.00 39.12  ? 1372 HOH   A O   1 
HETATM 3608 O  O   . HOH   GA 8 .   ? -24.925 12.970  34.880 1.00 55.36  ? 1373 HOH   A O   1 
HETATM 3609 O  O   . HOH   GA 8 .   ? -5.185  13.600  26.539 1.00 63.60  ? 1374 HOH   A O   1 
HETATM 3610 O  O   . HOH   GA 8 .   ? -25.008 -6.842  17.774 1.00 35.12  ? 1375 HOH   A O   1 
HETATM 3611 O  O   . HOH   GA 8 .   ? -20.570 -11.612 15.353 1.00 32.14  ? 1376 HOH   A O   1 
HETATM 3612 O  O   . HOH   GA 8 .   ? -22.354 12.925  17.643 1.00 25.59  ? 1377 HOH   A O   1 
HETATM 3613 O  O   . HOH   GA 8 .   ? -24.715 11.372  16.407 1.00 26.71  ? 1378 HOH   A O   1 
HETATM 3614 O  O   . HOH   GA 8 .   ? -5.150  17.161  12.772 1.00 48.15  ? 1379 HOH   A O   1 
HETATM 3615 O  O   . HOH   GA 8 .   ? -11.730 19.471  14.766 1.00 45.97  ? 1380 HOH   A O   1 
HETATM 3616 O  O   . HOH   GA 8 .   ? -4.086  -25.968 25.204 1.00 48.34  ? 1381 HOH   A O   1 
HETATM 3617 O  O   . HOH   GA 8 .   ? -35.210 -31.940 12.011 1.00 50.17  ? 1382 HOH   A O   1 
HETATM 3618 O  O   . HOH   GA 8 .   ? -17.572 13.450  29.067 1.00 42.11  ? 1383 HOH   A O   1 
HETATM 3619 O  O   . HOH   GA 8 .   ? -24.728 -3.933  18.233 1.00 37.22  ? 1384 HOH   A O   1 
HETATM 3620 O  O   . HOH   GA 8 .   ? -24.380 9.060   15.213 1.00 26.57  ? 1385 HOH   A O   1 
HETATM 3621 O  O   . HOH   GA 8 .   ? -33.176 -33.217 10.625 1.00 47.50  ? 1386 HOH   A O   1 
HETATM 3622 O  O   . HOH   GA 8 .   ? -27.958 -31.019 21.901 1.00 52.46  ? 1387 HOH   A O   1 
HETATM 3623 O  O   . HOH   GA 8 .   ? 5.965   -73.588 29.188 1.00 57.60  ? 1388 HOH   A O   1 
HETATM 3624 O  O   . HOH   GA 8 .   ? -23.559 15.136  5.227  1.00 53.05  ? 1389 HOH   A O   1 
HETATM 3625 O  O   . HOH   GA 8 .   ? -3.397  15.867  21.654 1.00 45.08  ? 1390 HOH   A O   1 
HETATM 3626 O  O   . HOH   GA 8 .   ? -15.360 12.234  28.414 1.00 26.90  ? 1391 HOH   A O   1 
HETATM 3627 O  O   . HOH   GA 8 .   ? -32.177 21.913  28.220 1.00 64.78  ? 1392 HOH   A O   1 
HETATM 3628 O  O   . HOH   GA 8 .   ? -17.563 15.205  6.035  1.00 44.90  ? 1393 HOH   A O   1 
HETATM 3629 O  O   . HOH   GA 8 .   ? -9.119  13.314  16.661 1.00 32.07  ? 1394 HOH   A O   1 
HETATM 3630 O  O   A HOH   GA 8 .   ? -10.982 15.884  19.352 0.49 35.31  ? 1395 HOH   A O   1 
HETATM 3631 O  O   . HOH   GA 8 .   ? -16.434 -33.226 21.430 1.00 57.21  ? 1396 HOH   A O   1 
HETATM 3632 O  O   . HOH   GA 8 .   ? -16.401 -32.807 19.068 1.00 61.72  ? 1397 HOH   A O   1 
HETATM 3633 O  O   . HOH   GA 8 .   ? -19.617 12.513  32.659 1.00 44.29  ? 1398 HOH   A O   1 
HETATM 3634 O  O   . HOH   GA 8 .   ? -21.458 15.832  17.995 1.00 43.49  ? 1399 HOH   A O   1 
HETATM 3635 O  O   . HOH   GA 8 .   ? -20.868 12.140  34.585 1.00 41.51  ? 1400 HOH   A O   1 
HETATM 3636 O  O   . HOH   GA 8 .   ? -30.574 20.219  3.774  1.00 44.14  ? 1401 HOH   A O   1 
HETATM 3637 O  O   . HOH   GA 8 .   ? -23.580 -16.088 26.428 1.00 43.88  ? 1402 HOH   A O   1 
HETATM 3638 O  O   . HOH   GA 8 .   ? 6.210   -76.198 23.923 1.00 35.40  ? 1403 HOH   A O   1 
HETATM 3639 O  O   . HOH   GA 8 .   ? -31.218 20.004  28.939 1.00 55.67  ? 1404 HOH   A O   1 
HETATM 3640 O  O   . HOH   GA 8 .   ? 3.830   -75.650 22.795 1.00 45.52  ? 1405 HOH   A O   1 
HETATM 3641 O  O   . HOH   GA 8 .   ? -18.167 -34.513 22.583 1.00 43.95  ? 1406 HOH   A O   1 
HETATM 3642 O  O   . HOH   GA 8 .   ? -18.011 8.374   21.815 1.00 39.65  ? 1407 HOH   A O   1 
HETATM 3643 O  O   . HOH   GA 8 .   ? -31.143 -22.249 -2.791 1.00 32.09  ? 1408 HOH   A O   1 
HETATM 3644 O  O   . HOH   GA 8 .   ? -24.388 -2.827  15.738 1.00 41.21  ? 1409 HOH   A O   1 
HETATM 3645 O  O   . HOH   GA 8 .   ? -23.689 17.686  5.773  1.00 65.13  ? 1410 HOH   A O   1 
# 
