data_9DC9
# 
_entry.id   9DC9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9DC9         pdb_00009dc9 10.2210/pdb9dc9/pdb 
WWPDB D_1000287834 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-27 
2 'Structure model' 1 1 2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.year'           
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DC9 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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              sethh@gene.com 
_pdbx_contact_author.name_first         Seth 
_pdbx_contact_author.name_last          Harris 
_pdbx_contact_author.name_mi            F 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1728-9771 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Harris, S.F.' 1 0000-0003-1728-9771 
'Wu, P.'       2 ?                   
# 
_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            Bioorg.Med.Chem.Lett. 
_citation.journal_id_ASTM           BMCLE8 
_citation.journal_id_CSD            1127 
_citation.journal_id_ISSN           1464-3405 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            117 
_citation.language                  ? 
_citation.page_first                130026 
_citation.page_last                 130026 
_citation.title                     
'Discovery of potent dihydro-oxazinoquinolinone inhibitors of GuaB for the treatment of tuberculosis.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmcl.2024.130026 
_citation.pdbx_database_id_PubMed   39536836 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhou, Y.'        1  ? 
primary 'Aliagas, I.'     2  ? 
primary 'Wang, S.'        3  ? 
primary 'Li, C.S.'        4  ? 
primary 'Liu, Z.'         5  ? 
primary 'Bowman, C.M.'    6  ? 
primary 'Burdick, D.J.'   7  ? 
primary 'Clark, K.R.'     8  ? 
primary 'Dening, T.J.'    9  ? 
primary 'Flygare, J.'     10 ? 
primary 'Ganti, A.'       11 ? 
primary 'Girgis, H.S.'    12 ? 
primary 'Hanan, E.J.'     13 ? 
primary 'Harris, S.F.'    14 ? 
primary 'Hu, C.'          15 ? 
primary 'Kapadia, S.B.'   16 ? 
primary 'Koehler, M.F.T.' 17 ? 
primary 'Lai, T.'         18 ? 
primary 'Liang, J.'       19 ? 
primary 'Liu, X.'         20 ? 
primary 'Ma, F.'          21 ? 
primary 'Mao, J.'         22 ? 
primary 'Nicolai, J.'     23 ? 
primary 'Sims, J.'        24 ? 
primary 'Unhayaker, S.'   25 ? 
primary 'Wai, J.'         26 ? 
primary 'Wang, X.'        27 ? 
primary 'Wu, P.'          28 ? 
primary 'Xu, Y.'          29 ? 
primary 'Yen, C.W.'       30 ? 
primary 'Zhang, R.'       31 ? 
primary 'Elfert, T.F.'    32 ? 
primary 'Tan, M.W.'       33 ? 
primary 'Kofoed, E.M.'    34 ? 
primary 'Crawford, T.D.'  35 ? 
# 
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 
;Inosine-5'-monophosphate dehydrogenase
;
43453.504 1   1.1.1.205 ? ? ? 
2 non-polymer syn 'INOSINIC ACID'                                                                                    348.206   1   
?         ? ? ? 
3 non-polymer syn '(3P)-3-(4-chloro-1H-imidazol-2-yl)-5-[(1R)-1-{[(3M)-3-(1H-pyrazol-5-yl)phenyl]oxy}ethyl]pyridine' 365.816   1   
?         ? ? ? 
4 water       nat water                                                                                              18.015    267 
?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'IMP dehydrogenase,IMPD,IMPDH,IMPDH2' 
# 
_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       
;MHHHHHHGENLYFQGSSRGMSGLEDSSDLVVSPYVRMGGLTTDPVPTGGDDPHKVAMLGLTFDDVLLLPAASDVVPATAD
TSSQLTKKIRLKVPLVSSAMDTVTESRMAIAMARAGGMGVLHRNLPVAEQAGQVEMVKRSGGLLVGAAVGVGGDAWVRAM
MLVDAGVDVLVVDTAHAHNRLVLDMVGKLKSEVGDRVEVVGGNVATRSAAAALVDAGADAVKVGVGPGSICTTRVVAGVG
APQITAILEAVAACRPAGVPVIADGGLQYSGDIAKALAAGASTAMLGSLLAGTAEAPGELIFVNGKQYKSYRGMGSLGAM
RGRGGATSYSKDRYFADDALSEDKLVPEGIEGRVPFRGPLSSVIHQLTGGLRAAMGYTGSPTIEVLQQAQFVRITPAGLK
ESHPHDVAMTVEAPNYYARGNS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHGENLYFQGSSRGMSGLEDSSDLVVSPYVRMGGLTTDPVPTGGDDPHKVAMLGLTFDDVLLLPAASDVVPATAD
TSSQLTKKIRLKVPLVSSAMDTVTESRMAIAMARAGGMGVLHRNLPVAEQAGQVEMVKRSGGLLVGAAVGVGGDAWVRAM
MLVDAGVDVLVVDTAHAHNRLVLDMVGKLKSEVGDRVEVVGGNVATRSAAAALVDAGADAVKVGVGPGSICTTRVVAGVG
APQITAILEAVAACRPAGVPVIADGGLQYSGDIAKALAAGASTAMLGSLLAGTAEAPGELIFVNGKQYKSYRGMGSLGAM
RGRGGATSYSKDRYFADDALSEDKLVPEGIEGRVPFRGPLSSVIHQLTGGLRAAMGYTGSPTIEVLQQAQFVRITPAGLK
ESHPHDVAMTVEAPNYYARGNS
;
_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 'INOSINIC ACID'                                                                                    IMP   
3 '(3P)-3-(4-chloro-1H-imidazol-2-yl)-5-[(1R)-1-{[(3M)-3-(1H-pyrazol-5-yl)phenyl]oxy}ethyl]pyridine' A1A3K 
4 water                                                                                              HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLY n 
1 9   GLU n 
1 10  ASN n 
1 11  LEU n 
1 12  TYR n 
1 13  PHE n 
1 14  GLN n 
1 15  GLY n 
1 16  SER n 
1 17  SER n 
1 18  ARG n 
1 19  GLY n 
1 20  MET n 
1 21  SER n 
1 22  GLY n 
1 23  LEU n 
1 24  GLU n 
1 25  ASP n 
1 26  SER n 
1 27  SER n 
1 28  ASP n 
1 29  LEU n 
1 30  VAL n 
1 31  VAL n 
1 32  SER n 
1 33  PRO n 
1 34  TYR n 
1 35  VAL n 
1 36  ARG n 
1 37  MET n 
1 38  GLY n 
1 39  GLY n 
1 40  LEU n 
1 41  THR n 
1 42  THR n 
1 43  ASP n 
1 44  PRO n 
1 45  VAL n 
1 46  PRO n 
1 47  THR n 
1 48  GLY n 
1 49  GLY n 
1 50  ASP n 
1 51  ASP n 
1 52  PRO n 
1 53  HIS n 
1 54  LYS n 
1 55  VAL n 
1 56  ALA n 
1 57  MET n 
1 58  LEU n 
1 59  GLY n 
1 60  LEU n 
1 61  THR n 
1 62  PHE n 
1 63  ASP n 
1 64  ASP n 
1 65  VAL n 
1 66  LEU n 
1 67  LEU n 
1 68  LEU n 
1 69  PRO n 
1 70  ALA n 
1 71  ALA n 
1 72  SER n 
1 73  ASP n 
1 74  VAL n 
1 75  VAL n 
1 76  PRO n 
1 77  ALA n 
1 78  THR n 
1 79  ALA n 
1 80  ASP n 
1 81  THR n 
1 82  SER n 
1 83  SER n 
1 84  GLN n 
1 85  LEU n 
1 86  THR n 
1 87  LYS n 
1 88  LYS n 
1 89  ILE n 
1 90  ARG n 
1 91  LEU n 
1 92  LYS n 
1 93  VAL n 
1 94  PRO n 
1 95  LEU n 
1 96  VAL n 
1 97  SER n 
1 98  SER n 
1 99  ALA n 
1 100 MET n 
1 101 ASP n 
1 102 THR n 
1 103 VAL n 
1 104 THR n 
1 105 GLU n 
1 106 SER n 
1 107 ARG n 
1 108 MET n 
1 109 ALA n 
1 110 ILE n 
1 111 ALA n 
1 112 MET n 
1 113 ALA n 
1 114 ARG n 
1 115 ALA n 
1 116 GLY n 
1 117 GLY n 
1 118 MET n 
1 119 GLY n 
1 120 VAL n 
1 121 LEU n 
1 122 HIS n 
1 123 ARG n 
1 124 ASN n 
1 125 LEU n 
1 126 PRO n 
1 127 VAL n 
1 128 ALA n 
1 129 GLU n 
1 130 GLN n 
1 131 ALA n 
1 132 GLY n 
1 133 GLN n 
1 134 VAL n 
1 135 GLU n 
1 136 MET n 
1 137 VAL n 
1 138 LYS n 
1 139 ARG n 
1 140 SER n 
1 141 GLY n 
1 142 GLY n 
1 143 LEU n 
1 144 LEU n 
1 145 VAL n 
1 146 GLY n 
1 147 ALA n 
1 148 ALA n 
1 149 VAL n 
1 150 GLY n 
1 151 VAL n 
1 152 GLY n 
1 153 GLY n 
1 154 ASP n 
1 155 ALA n 
1 156 TRP n 
1 157 VAL n 
1 158 ARG n 
1 159 ALA n 
1 160 MET n 
1 161 MET n 
1 162 LEU n 
1 163 VAL n 
1 164 ASP n 
1 165 ALA n 
1 166 GLY n 
1 167 VAL n 
1 168 ASP n 
1 169 VAL n 
1 170 LEU n 
1 171 VAL n 
1 172 VAL n 
1 173 ASP n 
1 174 THR n 
1 175 ALA n 
1 176 HIS n 
1 177 ALA n 
1 178 HIS n 
1 179 ASN n 
1 180 ARG n 
1 181 LEU n 
1 182 VAL n 
1 183 LEU n 
1 184 ASP n 
1 185 MET n 
1 186 VAL n 
1 187 GLY n 
1 188 LYS n 
1 189 LEU n 
1 190 LYS n 
1 191 SER n 
1 192 GLU n 
1 193 VAL n 
1 194 GLY n 
1 195 ASP n 
1 196 ARG n 
1 197 VAL n 
1 198 GLU n 
1 199 VAL n 
1 200 VAL n 
1 201 GLY n 
1 202 GLY n 
1 203 ASN n 
1 204 VAL n 
1 205 ALA n 
1 206 THR n 
1 207 ARG n 
1 208 SER n 
1 209 ALA n 
1 210 ALA n 
1 211 ALA n 
1 212 ALA n 
1 213 LEU n 
1 214 VAL n 
1 215 ASP n 
1 216 ALA n 
1 217 GLY n 
1 218 ALA n 
1 219 ASP n 
1 220 ALA n 
1 221 VAL n 
1 222 LYS n 
1 223 VAL n 
1 224 GLY n 
1 225 VAL n 
1 226 GLY n 
1 227 PRO n 
1 228 GLY n 
1 229 SER n 
1 230 ILE n 
1 231 CYS n 
1 232 THR n 
1 233 THR n 
1 234 ARG n 
1 235 VAL n 
1 236 VAL n 
1 237 ALA n 
1 238 GLY n 
1 239 VAL n 
1 240 GLY n 
1 241 ALA n 
1 242 PRO n 
1 243 GLN n 
1 244 ILE n 
1 245 THR n 
1 246 ALA n 
1 247 ILE n 
1 248 LEU n 
1 249 GLU n 
1 250 ALA n 
1 251 VAL n 
1 252 ALA n 
1 253 ALA n 
1 254 CYS n 
1 255 ARG n 
1 256 PRO n 
1 257 ALA n 
1 258 GLY n 
1 259 VAL n 
1 260 PRO n 
1 261 VAL n 
1 262 ILE n 
1 263 ALA n 
1 264 ASP n 
1 265 GLY n 
1 266 GLY n 
1 267 LEU n 
1 268 GLN n 
1 269 TYR n 
1 270 SER n 
1 271 GLY n 
1 272 ASP n 
1 273 ILE n 
1 274 ALA n 
1 275 LYS n 
1 276 ALA n 
1 277 LEU n 
1 278 ALA n 
1 279 ALA n 
1 280 GLY n 
1 281 ALA n 
1 282 SER n 
1 283 THR n 
1 284 ALA n 
1 285 MET n 
1 286 LEU n 
1 287 GLY n 
1 288 SER n 
1 289 LEU n 
1 290 LEU n 
1 291 ALA n 
1 292 GLY n 
1 293 THR n 
1 294 ALA n 
1 295 GLU n 
1 296 ALA n 
1 297 PRO n 
1 298 GLY n 
1 299 GLU n 
1 300 LEU n 
1 301 ILE n 
1 302 PHE n 
1 303 VAL n 
1 304 ASN n 
1 305 GLY n 
1 306 LYS n 
1 307 GLN n 
1 308 TYR n 
1 309 LYS n 
1 310 SER n 
1 311 TYR n 
1 312 ARG n 
1 313 GLY n 
1 314 MET n 
1 315 GLY n 
1 316 SER n 
1 317 LEU n 
1 318 GLY n 
1 319 ALA n 
1 320 MET n 
1 321 ARG n 
1 322 GLY n 
1 323 ARG n 
1 324 GLY n 
1 325 GLY n 
1 326 ALA n 
1 327 THR n 
1 328 SER n 
1 329 TYR n 
1 330 SER n 
1 331 LYS n 
1 332 ASP n 
1 333 ARG n 
1 334 TYR n 
1 335 PHE n 
1 336 ALA n 
1 337 ASP n 
1 338 ASP n 
1 339 ALA n 
1 340 LEU n 
1 341 SER n 
1 342 GLU n 
1 343 ASP n 
1 344 LYS n 
1 345 LEU n 
1 346 VAL n 
1 347 PRO n 
1 348 GLU n 
1 349 GLY n 
1 350 ILE n 
1 351 GLU n 
1 352 GLY n 
1 353 ARG n 
1 354 VAL n 
1 355 PRO n 
1 356 PHE n 
1 357 ARG n 
1 358 GLY n 
1 359 PRO n 
1 360 LEU n 
1 361 SER n 
1 362 SER n 
1 363 VAL n 
1 364 ILE n 
1 365 HIS n 
1 366 GLN n 
1 367 LEU n 
1 368 THR n 
1 369 GLY n 
1 370 GLY n 
1 371 LEU n 
1 372 ARG n 
1 373 ALA n 
1 374 ALA n 
1 375 MET n 
1 376 GLY n 
1 377 TYR n 
1 378 THR n 
1 379 GLY n 
1 380 SER n 
1 381 PRO n 
1 382 THR n 
1 383 ILE n 
1 384 GLU n 
1 385 VAL n 
1 386 LEU n 
1 387 GLN n 
1 388 GLN n 
1 389 ALA n 
1 390 GLN n 
1 391 PHE n 
1 392 VAL n 
1 393 ARG n 
1 394 ILE n 
1 395 THR n 
1 396 PRO n 
1 397 ALA n 
1 398 GLY n 
1 399 LEU n 
1 400 LYS n 
1 401 GLU n 
1 402 SER n 
1 403 HIS n 
1 404 PRO n 
1 405 HIS n 
1 406 ASP n 
1 407 VAL n 
1 408 ALA n 
1 409 MET n 
1 410 THR n 
1 411 VAL n 
1 412 GLU n 
1 413 ALA n 
1 414 PRO n 
1 415 ASN n 
1 416 TYR n 
1 417 TYR n 
1 418 ALA n 
1 419 ARG n 
1 420 GLY n 
1 421 ASN n 
1 422 SER 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   142 ? ? 'guaB, guaB2, Rv3411c, MTCY78.17' ? ? ? ? ? ? 'Mycobacterium tuberculosis' 1773 ? ? ? 
? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 143 422 ? ? 'guaB, guaB2, Rv3411c, MTCY78.17' ? ? ? ? ? ? 'Mycobacterium tuberculosis' 1773 ? ? ? 
? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1A3K non-polymer         . '(3P)-3-(4-chloro-1H-imidazol-2-yl)-5-[(1R)-1-{[(3M)-3-(1H-pyrazol-5-yl)phenyl]oxy}ethyl]pyridine' ? 
'C19 H16 Cl N5 O' 365.816 
ALA   'L-peptide linking' y ALANINE                                                                                            ? 
'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                                                                           ? 
'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                         ? 
'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                    ? 
'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                           ? 
'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                          ? 
'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                    ? 
'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                                                            ? 
'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                          ? 
'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                                                              ? 
'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                         ? 
'C6 H13 N O2'     131.173 
IMP   non-polymer         n 'INOSINIC ACID'                                                                                    ? 
'C10 H13 N4 O8 P' 348.206 
LEU   'L-peptide linking' y LEUCINE                                                                                            ? 
'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                                                             ? 
'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                                                         ? 
'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                      ? 
'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                                                            ? 
'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                                                             ? 
'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                                                          ? 
'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                         ? 
'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                           ? 
'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                                                             ? 
'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -14 ?   ?   ?   A . n 
A 1 2   HIS 2   -13 ?   ?   ?   A . n 
A 1 3   HIS 3   -12 ?   ?   ?   A . n 
A 1 4   HIS 4   -11 ?   ?   ?   A . n 
A 1 5   HIS 5   -10 ?   ?   ?   A . n 
A 1 6   HIS 6   -9  ?   ?   ?   A . n 
A 1 7   HIS 7   -8  ?   ?   ?   A . n 
A 1 8   GLY 8   -7  ?   ?   ?   A . n 
A 1 9   GLU 9   -6  ?   ?   ?   A . n 
A 1 10  ASN 10  -5  ?   ?   ?   A . n 
A 1 11  LEU 11  -4  ?   ?   ?   A . n 
A 1 12  TYR 12  -3  ?   ?   ?   A . n 
A 1 13  PHE 13  -2  ?   ?   ?   A . n 
A 1 14  GLN 14  -1  ?   ?   ?   A . n 
A 1 15  GLY 15  0   ?   ?   ?   A . n 
A 1 16  SER 16  1   ?   ?   ?   A . n 
A 1 17  SER 17  2   ?   ?   ?   A . n 
A 1 18  ARG 18  3   ?   ?   ?   A . n 
A 1 19  GLY 19  4   ?   ?   ?   A . n 
A 1 20  MET 20  5   ?   ?   ?   A . n 
A 1 21  SER 21  6   ?   ?   ?   A . n 
A 1 22  GLY 22  7   ?   ?   ?   A . n 
A 1 23  LEU 23  8   ?   ?   ?   A . n 
A 1 24  GLU 24  9   ?   ?   ?   A . n 
A 1 25  ASP 25  10  ?   ?   ?   A . n 
A 1 26  SER 26  11  ?   ?   ?   A . n 
A 1 27  SER 27  12  ?   ?   ?   A . n 
A 1 28  ASP 28  13  ?   ?   ?   A . n 
A 1 29  LEU 29  14  ?   ?   ?   A . n 
A 1 30  VAL 30  15  ?   ?   ?   A . n 
A 1 31  VAL 31  16  ?   ?   ?   A . n 
A 1 32  SER 32  17  ?   ?   ?   A . n 
A 1 33  PRO 33  18  ?   ?   ?   A . n 
A 1 34  TYR 34  19  ?   ?   ?   A . n 
A 1 35  VAL 35  20  ?   ?   ?   A . n 
A 1 36  ARG 36  21  ?   ?   ?   A . n 
A 1 37  MET 37  22  ?   ?   ?   A . n 
A 1 38  GLY 38  23  ?   ?   ?   A . n 
A 1 39  GLY 39  24  ?   ?   ?   A . n 
A 1 40  LEU 40  25  ?   ?   ?   A . n 
A 1 41  THR 41  26  ?   ?   ?   A . n 
A 1 42  THR 42  27  27  THR THR A . n 
A 1 43  ASP 43  28  28  ASP ASP A . n 
A 1 44  PRO 44  29  29  PRO PRO A . n 
A 1 45  VAL 45  30  30  VAL VAL A . n 
A 1 46  PRO 46  31  31  PRO PRO A . n 
A 1 47  THR 47  32  32  THR THR A . n 
A 1 48  GLY 48  33  33  GLY GLY A . n 
A 1 49  GLY 49  34  34  GLY GLY A . n 
A 1 50  ASP 50  35  35  ASP ASP A . n 
A 1 51  ASP 51  36  36  ASP ASP A . n 
A 1 52  PRO 52  37  37  PRO PRO A . n 
A 1 53  HIS 53  38  38  HIS HIS A . n 
A 1 54  LYS 54  39  39  LYS LYS A . n 
A 1 55  VAL 55  40  40  VAL VAL A . n 
A 1 56  ALA 56  41  41  ALA ALA A . n 
A 1 57  MET 57  42  42  MET MET A . n 
A 1 58  LEU 58  43  43  LEU LEU A . n 
A 1 59  GLY 59  44  44  GLY GLY A . n 
A 1 60  LEU 60  45  45  LEU LEU A . n 
A 1 61  THR 61  46  46  THR THR A . n 
A 1 62  PHE 62  47  47  PHE PHE A . n 
A 1 63  ASP 63  48  48  ASP ASP A . n 
A 1 64  ASP 64  49  49  ASP ASP A . n 
A 1 65  VAL 65  50  50  VAL VAL A . n 
A 1 66  LEU 66  51  51  LEU LEU A . n 
A 1 67  LEU 67  52  52  LEU LEU A . n 
A 1 68  LEU 68  53  53  LEU LEU A . n 
A 1 69  PRO 69  54  54  PRO PRO A . n 
A 1 70  ALA 70  55  55  ALA ALA A . n 
A 1 71  ALA 71  56  56  ALA ALA A . n 
A 1 72  SER 72  57  57  SER SER A . n 
A 1 73  ASP 73  58  58  ASP ASP A . n 
A 1 74  VAL 74  59  59  VAL VAL A . n 
A 1 75  VAL 75  60  60  VAL VAL A . n 
A 1 76  PRO 76  61  61  PRO PRO A . n 
A 1 77  ALA 77  62  62  ALA ALA A . n 
A 1 78  THR 78  63  63  THR THR A . n 
A 1 79  ALA 79  64  64  ALA ALA A . n 
A 1 80  ASP 80  65  65  ASP ASP A . n 
A 1 81  THR 81  66  66  THR THR A . n 
A 1 82  SER 82  67  67  SER SER A . n 
A 1 83  SER 83  68  68  SER SER A . n 
A 1 84  GLN 84  69  69  GLN GLN A . n 
A 1 85  LEU 85  70  70  LEU LEU A . n 
A 1 86  THR 86  71  71  THR THR A . n 
A 1 87  LYS 87  72  72  LYS LYS A . n 
A 1 88  LYS 88  73  73  LYS LYS A . n 
A 1 89  ILE 89  74  74  ILE ILE A . n 
A 1 90  ARG 90  75  75  ARG ARG A . n 
A 1 91  LEU 91  76  76  LEU LEU A . n 
A 1 92  LYS 92  77  77  LYS LYS A . n 
A 1 93  VAL 93  78  78  VAL VAL A . n 
A 1 94  PRO 94  79  79  PRO PRO A . n 
A 1 95  LEU 95  80  80  LEU LEU A . n 
A 1 96  VAL 96  81  81  VAL VAL A . n 
A 1 97  SER 97  82  82  SER SER A . n 
A 1 98  SER 98  83  83  SER SER A . n 
A 1 99  ALA 99  84  84  ALA ALA A . n 
A 1 100 MET 100 85  85  MET MET A . n 
A 1 101 ASP 101 86  86  ASP ASP A . n 
A 1 102 THR 102 87  87  THR THR A . n 
A 1 103 VAL 103 88  88  VAL VAL A . n 
A 1 104 THR 104 89  89  THR THR A . n 
A 1 105 GLU 105 90  90  GLU GLU A . n 
A 1 106 SER 106 91  91  SER SER A . n 
A 1 107 ARG 107 92  92  ARG ARG A . n 
A 1 108 MET 108 93  93  MET MET A . n 
A 1 109 ALA 109 94  94  ALA ALA A . n 
A 1 110 ILE 110 95  95  ILE ILE A . n 
A 1 111 ALA 111 96  96  ALA ALA A . n 
A 1 112 MET 112 97  97  MET MET A . n 
A 1 113 ALA 113 98  98  ALA ALA A . n 
A 1 114 ARG 114 99  99  ARG ARG A . n 
A 1 115 ALA 115 100 100 ALA ALA A . n 
A 1 116 GLY 116 101 101 GLY GLY A . n 
A 1 117 GLY 117 102 102 GLY GLY A . n 
A 1 118 MET 118 103 103 MET MET A . n 
A 1 119 GLY 119 104 104 GLY GLY A . n 
A 1 120 VAL 120 105 105 VAL VAL A . n 
A 1 121 LEU 121 106 106 LEU LEU A . n 
A 1 122 HIS 122 107 107 HIS HIS A . n 
A 1 123 ARG 123 108 108 ARG ARG A . n 
A 1 124 ASN 124 109 109 ASN ASN A . n 
A 1 125 LEU 125 110 110 LEU LEU A . n 
A 1 126 PRO 126 111 111 PRO PRO A . n 
A 1 127 VAL 127 112 112 VAL VAL A . n 
A 1 128 ALA 128 113 113 ALA ALA A . n 
A 1 129 GLU 129 114 114 GLU GLU A . n 
A 1 130 GLN 130 115 115 GLN GLN A . n 
A 1 131 ALA 131 116 116 ALA ALA A . n 
A 1 132 GLY 132 117 117 GLY GLY A . n 
A 1 133 GLN 133 118 118 GLN GLN A . n 
A 1 134 VAL 134 119 119 VAL VAL A . n 
A 1 135 GLU 135 120 120 GLU GLU A . n 
A 1 136 MET 136 121 121 MET MET A . n 
A 1 137 VAL 137 122 122 VAL VAL A . n 
A 1 138 LYS 138 123 123 LYS LYS A . n 
A 1 139 ARG 139 124 124 ARG ARG A . n 
A 1 140 SER 140 125 125 SER SER A . n 
A 1 141 GLY 141 126 126 GLY GLY A . n 
A 1 142 GLY 142 127 127 GLY GLY A . n 
A 1 143 LEU 143 253 253 LEU LEU A . n 
A 1 144 LEU 144 254 254 LEU LEU A . n 
A 1 145 VAL 145 255 255 VAL VAL A . n 
A 1 146 GLY 146 256 256 GLY GLY A . n 
A 1 147 ALA 147 257 257 ALA ALA A . n 
A 1 148 ALA 148 258 258 ALA ALA A . n 
A 1 149 VAL 149 259 259 VAL VAL A . n 
A 1 150 GLY 150 260 260 GLY GLY A . n 
A 1 151 VAL 151 261 261 VAL VAL A . n 
A 1 152 GLY 152 262 262 GLY GLY A . n 
A 1 153 GLY 153 263 263 GLY GLY A . n 
A 1 154 ASP 154 264 264 ASP ASP A . n 
A 1 155 ALA 155 265 265 ALA ALA A . n 
A 1 156 TRP 156 266 266 TRP TRP A . n 
A 1 157 VAL 157 267 267 VAL VAL A . n 
A 1 158 ARG 158 268 268 ARG ARG A . n 
A 1 159 ALA 159 269 269 ALA ALA A . n 
A 1 160 MET 160 270 270 MET MET A . n 
A 1 161 MET 161 271 271 MET MET A . n 
A 1 162 LEU 162 272 272 LEU LEU A . n 
A 1 163 VAL 163 273 273 VAL VAL A . n 
A 1 164 ASP 164 274 274 ASP ASP A . n 
A 1 165 ALA 165 275 275 ALA ALA A . n 
A 1 166 GLY 166 276 276 GLY GLY A . n 
A 1 167 VAL 167 277 277 VAL VAL A . n 
A 1 168 ASP 168 278 278 ASP ASP A . n 
A 1 169 VAL 169 279 279 VAL VAL A . n 
A 1 170 LEU 170 280 280 LEU LEU A . n 
A 1 171 VAL 171 281 281 VAL VAL A . n 
A 1 172 VAL 172 282 282 VAL VAL A . n 
A 1 173 ASP 173 283 283 ASP ASP A . n 
A 1 174 THR 174 284 284 THR THR A . n 
A 1 175 ALA 175 285 285 ALA ALA A . n 
A 1 176 HIS 176 286 286 HIS HIS A . n 
A 1 177 ALA 177 287 287 ALA ALA A . n 
A 1 178 HIS 178 288 288 HIS HIS A . n 
A 1 179 ASN 179 289 289 ASN ASN A . n 
A 1 180 ARG 180 290 290 ARG ARG A . n 
A 1 181 LEU 181 291 291 LEU LEU A . n 
A 1 182 VAL 182 292 292 VAL VAL A . n 
A 1 183 LEU 183 293 293 LEU LEU A . n 
A 1 184 ASP 184 294 294 ASP ASP A . n 
A 1 185 MET 185 295 295 MET MET A . n 
A 1 186 VAL 186 296 296 VAL VAL A . n 
A 1 187 GLY 187 297 297 GLY GLY A . n 
A 1 188 LYS 188 298 298 LYS LYS A . n 
A 1 189 LEU 189 299 299 LEU LEU A . n 
A 1 190 LYS 190 300 300 LYS LYS A . n 
A 1 191 SER 191 301 301 SER SER A . n 
A 1 192 GLU 192 302 302 GLU GLU A . n 
A 1 193 VAL 193 303 303 VAL VAL A . n 
A 1 194 GLY 194 304 304 GLY GLY A . n 
A 1 195 ASP 195 305 305 ASP ASP A . n 
A 1 196 ARG 196 306 306 ARG ARG A . n 
A 1 197 VAL 197 307 307 VAL VAL A . n 
A 1 198 GLU 198 308 308 GLU GLU A . n 
A 1 199 VAL 199 309 309 VAL VAL A . n 
A 1 200 VAL 200 310 310 VAL VAL A . n 
A 1 201 GLY 201 311 311 GLY GLY A . n 
A 1 202 GLY 202 312 312 GLY GLY A . n 
A 1 203 ASN 203 313 313 ASN ASN A . n 
A 1 204 VAL 204 314 314 VAL VAL A . n 
A 1 205 ALA 205 315 315 ALA ALA A . n 
A 1 206 THR 206 316 316 THR THR A . n 
A 1 207 ARG 207 317 317 ARG ARG A . n 
A 1 208 SER 208 318 318 SER SER A . n 
A 1 209 ALA 209 319 319 ALA ALA A . n 
A 1 210 ALA 210 320 320 ALA ALA A . n 
A 1 211 ALA 211 321 321 ALA ALA A . n 
A 1 212 ALA 212 322 322 ALA ALA A . n 
A 1 213 LEU 213 323 323 LEU LEU A . n 
A 1 214 VAL 214 324 324 VAL VAL A . n 
A 1 215 ASP 215 325 325 ASP ASP A . n 
A 1 216 ALA 216 326 326 ALA ALA A . n 
A 1 217 GLY 217 327 327 GLY GLY A . n 
A 1 218 ALA 218 328 328 ALA ALA A . n 
A 1 219 ASP 219 329 329 ASP ASP A . n 
A 1 220 ALA 220 330 330 ALA ALA A . n 
A 1 221 VAL 221 331 331 VAL VAL A . n 
A 1 222 LYS 222 332 332 LYS LYS A . n 
A 1 223 VAL 223 333 333 VAL VAL A . n 
A 1 224 GLY 224 334 334 GLY GLY A . n 
A 1 225 VAL 225 335 335 VAL VAL A . n 
A 1 226 GLY 226 336 336 GLY GLY A . n 
A 1 227 PRO 227 337 337 PRO PRO A . n 
A 1 228 GLY 228 338 338 GLY GLY A . n 
A 1 229 SER 229 339 339 SER SER A . n 
A 1 230 ILE 230 340 340 ILE ILE A . n 
A 1 231 CYS 231 341 341 CYS CYS A . n 
A 1 232 THR 232 342 342 THR THR A . n 
A 1 233 THR 233 343 343 THR THR A . n 
A 1 234 ARG 234 344 344 ARG ARG A . n 
A 1 235 VAL 235 345 345 VAL VAL A . n 
A 1 236 VAL 236 346 346 VAL VAL A . n 
A 1 237 ALA 237 347 347 ALA ALA A . n 
A 1 238 GLY 238 348 348 GLY GLY A . n 
A 1 239 VAL 239 349 349 VAL VAL A . n 
A 1 240 GLY 240 350 350 GLY GLY A . n 
A 1 241 ALA 241 351 351 ALA ALA A . n 
A 1 242 PRO 242 352 352 PRO PRO A . n 
A 1 243 GLN 243 353 353 GLN GLN A . n 
A 1 244 ILE 244 354 354 ILE ILE A . n 
A 1 245 THR 245 355 355 THR THR A . n 
A 1 246 ALA 246 356 356 ALA ALA A . n 
A 1 247 ILE 247 357 357 ILE ILE A . n 
A 1 248 LEU 248 358 358 LEU LEU A . n 
A 1 249 GLU 249 359 359 GLU GLU A . n 
A 1 250 ALA 250 360 360 ALA ALA A . n 
A 1 251 VAL 251 361 361 VAL VAL A . n 
A 1 252 ALA 252 362 362 ALA ALA A . n 
A 1 253 ALA 253 363 363 ALA ALA A . n 
A 1 254 CYS 254 364 364 CYS CYS A . n 
A 1 255 ARG 255 365 365 ARG ARG A . n 
A 1 256 PRO 256 366 366 PRO PRO A . n 
A 1 257 ALA 257 367 367 ALA ALA A . n 
A 1 258 GLY 258 368 368 GLY GLY A . n 
A 1 259 VAL 259 369 369 VAL VAL A . n 
A 1 260 PRO 260 370 370 PRO PRO A . n 
A 1 261 VAL 261 371 371 VAL VAL A . n 
A 1 262 ILE 262 372 372 ILE ILE A . n 
A 1 263 ALA 263 373 373 ALA ALA A . n 
A 1 264 ASP 264 374 374 ASP ASP A . n 
A 1 265 GLY 265 375 375 GLY GLY A . n 
A 1 266 GLY 266 376 376 GLY GLY A . n 
A 1 267 LEU 267 377 377 LEU LEU A . n 
A 1 268 GLN 268 378 378 GLN GLN A . n 
A 1 269 TYR 269 379 379 TYR TYR A . n 
A 1 270 SER 270 380 380 SER SER A . n 
A 1 271 GLY 271 381 381 GLY GLY A . n 
A 1 272 ASP 272 382 382 ASP ASP A . n 
A 1 273 ILE 273 383 383 ILE ILE A . n 
A 1 274 ALA 274 384 384 ALA ALA A . n 
A 1 275 LYS 275 385 385 LYS LYS A . n 
A 1 276 ALA 276 386 386 ALA ALA A . n 
A 1 277 LEU 277 387 387 LEU LEU A . n 
A 1 278 ALA 278 388 388 ALA ALA A . n 
A 1 279 ALA 279 389 389 ALA ALA A . n 
A 1 280 GLY 280 390 390 GLY GLY A . n 
A 1 281 ALA 281 391 391 ALA ALA A . n 
A 1 282 SER 282 392 392 SER SER A . n 
A 1 283 THR 283 393 393 THR THR A . n 
A 1 284 ALA 284 394 394 ALA ALA A . n 
A 1 285 MET 285 395 395 MET MET A . n 
A 1 286 LEU 286 396 396 LEU LEU A . n 
A 1 287 GLY 287 397 397 GLY GLY A . n 
A 1 288 SER 288 398 398 SER SER A . n 
A 1 289 LEU 289 399 399 LEU LEU A . n 
A 1 290 LEU 290 400 400 LEU LEU A . n 
A 1 291 ALA 291 401 401 ALA ALA A . n 
A 1 292 GLY 292 402 402 GLY GLY A . n 
A 1 293 THR 293 403 403 THR THR A . n 
A 1 294 ALA 294 404 404 ALA ALA A . n 
A 1 295 GLU 295 405 405 GLU GLU A . n 
A 1 296 ALA 296 406 406 ALA ALA A . n 
A 1 297 PRO 297 407 407 PRO PRO A . n 
A 1 298 GLY 298 408 408 GLY GLY A . n 
A 1 299 GLU 299 409 409 GLU GLU A . n 
A 1 300 LEU 300 410 410 LEU LEU A . n 
A 1 301 ILE 301 411 411 ILE ILE A . n 
A 1 302 PHE 302 412 412 PHE PHE A . n 
A 1 303 VAL 303 413 413 VAL VAL A . n 
A 1 304 ASN 304 414 414 ASN ASN A . n 
A 1 305 GLY 305 415 415 GLY GLY A . n 
A 1 306 LYS 306 416 416 LYS LYS A . n 
A 1 307 GLN 307 417 417 GLN GLN A . n 
A 1 308 TYR 308 418 418 TYR TYR A . n 
A 1 309 LYS 309 419 419 LYS LYS A . n 
A 1 310 SER 310 420 420 SER SER A . n 
A 1 311 TYR 311 421 421 TYR TYR A . n 
A 1 312 ARG 312 422 422 ARG ARG A . n 
A 1 313 GLY 313 423 423 GLY GLY A . n 
A 1 314 MET 314 424 424 MET MET A . n 
A 1 315 GLY 315 425 425 GLY GLY A . n 
A 1 316 SER 316 426 426 SER SER A . n 
A 1 317 LEU 317 427 427 LEU LEU A . n 
A 1 318 GLY 318 428 428 GLY GLY A . n 
A 1 319 ALA 319 429 429 ALA ALA A . n 
A 1 320 MET 320 430 430 MET MET A . n 
A 1 321 ARG 321 431 431 ARG ARG A . n 
A 1 322 GLY 322 432 ?   ?   ?   A . n 
A 1 323 ARG 323 433 ?   ?   ?   A . n 
A 1 324 GLY 324 434 ?   ?   ?   A . n 
A 1 325 GLY 325 435 ?   ?   ?   A . n 
A 1 326 ALA 326 436 ?   ?   ?   A . n 
A 1 327 THR 327 437 ?   ?   ?   A . n 
A 1 328 SER 328 438 ?   ?   ?   A . n 
A 1 329 TYR 329 439 ?   ?   ?   A . n 
A 1 330 SER 330 440 ?   ?   ?   A . n 
A 1 331 LYS 331 441 ?   ?   ?   A . n 
A 1 332 ASP 332 442 ?   ?   ?   A . n 
A 1 333 ARG 333 443 ?   ?   ?   A . n 
A 1 334 TYR 334 444 ?   ?   ?   A . n 
A 1 335 PHE 335 445 ?   ?   ?   A . n 
A 1 336 ALA 336 446 ?   ?   ?   A . n 
A 1 337 ASP 337 447 ?   ?   ?   A . n 
A 1 338 ASP 338 448 ?   ?   ?   A . n 
A 1 339 ALA 339 449 ?   ?   ?   A . n 
A 1 340 LEU 340 450 ?   ?   ?   A . n 
A 1 341 SER 341 451 ?   ?   ?   A . n 
A 1 342 GLU 342 452 ?   ?   ?   A . n 
A 1 343 ASP 343 453 ?   ?   ?   A . n 
A 1 344 LYS 344 454 ?   ?   ?   A . n 
A 1 345 LEU 345 455 455 LEU LEU A . n 
A 1 346 VAL 346 456 456 VAL VAL A . n 
A 1 347 PRO 347 457 457 PRO PRO A . n 
A 1 348 GLU 348 458 458 GLU GLU A . n 
A 1 349 GLY 349 459 459 GLY GLY A . n 
A 1 350 ILE 350 460 460 ILE ILE A . n 
A 1 351 GLU 351 461 461 GLU GLU A . n 
A 1 352 GLY 352 462 462 GLY GLY A . n 
A 1 353 ARG 353 463 463 ARG ARG A . n 
A 1 354 VAL 354 464 464 VAL VAL A . n 
A 1 355 PRO 355 465 465 PRO PRO A . n 
A 1 356 PHE 356 466 466 PHE PHE A . n 
A 1 357 ARG 357 467 467 ARG ARG A . n 
A 1 358 GLY 358 468 468 GLY GLY A . n 
A 1 359 PRO 359 469 469 PRO PRO A . n 
A 1 360 LEU 360 470 470 LEU LEU A . n 
A 1 361 SER 361 471 471 SER SER A . n 
A 1 362 SER 362 472 472 SER SER A . n 
A 1 363 VAL 363 473 473 VAL VAL A . n 
A 1 364 ILE 364 474 474 ILE ILE A . n 
A 1 365 HIS 365 475 475 HIS HIS A . n 
A 1 366 GLN 366 476 476 GLN GLN A . n 
A 1 367 LEU 367 477 477 LEU LEU A . n 
A 1 368 THR 368 478 478 THR THR A . n 
A 1 369 GLY 369 479 479 GLY GLY A . n 
A 1 370 GLY 370 480 480 GLY GLY A . n 
A 1 371 LEU 371 481 481 LEU LEU A . n 
A 1 372 ARG 372 482 482 ARG ARG A . n 
A 1 373 ALA 373 483 483 ALA ALA A . n 
A 1 374 ALA 374 484 484 ALA ALA A . n 
A 1 375 MET 375 485 485 MET MET A . n 
A 1 376 GLY 376 486 486 GLY GLY A . n 
A 1 377 TYR 377 487 487 TYR TYR A . n 
A 1 378 THR 378 488 488 THR THR A . n 
A 1 379 GLY 379 489 489 GLY GLY A . n 
A 1 380 SER 380 490 490 SER SER A . n 
A 1 381 PRO 381 491 491 PRO PRO A . n 
A 1 382 THR 382 492 492 THR THR A . n 
A 1 383 ILE 383 493 493 ILE ILE A . n 
A 1 384 GLU 384 494 494 GLU GLU A . n 
A 1 385 VAL 385 495 495 VAL VAL A . n 
A 1 386 LEU 386 496 496 LEU LEU A . n 
A 1 387 GLN 387 497 497 GLN GLN A . n 
A 1 388 GLN 388 498 498 GLN GLN A . n 
A 1 389 ALA 389 499 499 ALA ALA A . n 
A 1 390 GLN 390 500 500 GLN GLN A . n 
A 1 391 PHE 391 501 501 PHE PHE A . n 
A 1 392 VAL 392 502 502 VAL VAL A . n 
A 1 393 ARG 393 503 503 ARG ARG A . n 
A 1 394 ILE 394 504 504 ILE ILE A . n 
A 1 395 THR 395 505 505 THR THR A . n 
A 1 396 PRO 396 506 506 PRO PRO A . n 
A 1 397 ALA 397 507 507 ALA ALA A . n 
A 1 398 GLY 398 508 508 GLY GLY A . n 
A 1 399 LEU 399 509 509 LEU LEU A . n 
A 1 400 LYS 400 510 510 LYS LYS A . n 
A 1 401 GLU 401 511 511 GLU GLU A . n 
A 1 402 SER 402 512 512 SER SER A . n 
A 1 403 HIS 403 513 513 HIS HIS A . n 
A 1 404 PRO 404 514 514 PRO PRO A . n 
A 1 405 HIS 405 515 515 HIS HIS A . n 
A 1 406 ASP 406 516 516 ASP ASP A . n 
A 1 407 VAL 407 517 517 VAL VAL A . n 
A 1 408 ALA 408 518 518 ALA ALA A . n 
A 1 409 MET 409 519 519 MET MET A . n 
A 1 410 THR 410 520 520 THR THR A . n 
A 1 411 VAL 411 521 521 VAL VAL A . n 
A 1 412 GLU 412 522 522 GLU GLU A . n 
A 1 413 ALA 413 523 523 ALA ALA A . n 
A 1 414 PRO 414 524 524 PRO PRO A . n 
A 1 415 ASN 415 525 525 ASN ASN A . n 
A 1 416 TYR 416 526 ?   ?   ?   A . n 
A 1 417 TYR 417 527 ?   ?   ?   A . n 
A 1 418 ALA 418 528 ?   ?   ?   A . n 
A 1 419 ARG 419 529 ?   ?   ?   A . n 
A 1 420 GLY 420 530 ?   ?   ?   A . n 
A 1 421 ASN 421 531 ?   ?   ?   A . n 
A 1 422 SER 422 532 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A3K 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A3K 
_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 IMP   1   801  801 IMP   IMP A . 
C 3 A1A3K 1   802  1   A1A3K DRG A . 
D 4 HOH   1   901  234 HOH   HOH A . 
D 4 HOH   2   902  142 HOH   HOH A . 
D 4 HOH   3   903  167 HOH   HOH A . 
D 4 HOH   4   904  228 HOH   HOH A . 
D 4 HOH   5   905  181 HOH   HOH A . 
D 4 HOH   6   906  267 HOH   HOH A . 
D 4 HOH   7   907  216 HOH   HOH A . 
D 4 HOH   8   908  275 HOH   HOH A . 
D 4 HOH   9   909  266 HOH   HOH A . 
D 4 HOH   10  910  106 HOH   HOH A . 
D 4 HOH   11  911  125 HOH   HOH A . 
D 4 HOH   12  912  219 HOH   HOH A . 
D 4 HOH   13  913  274 HOH   HOH A . 
D 4 HOH   14  914  135 HOH   HOH A . 
D 4 HOH   15  915  174 HOH   HOH A . 
D 4 HOH   16  916  155 HOH   HOH A . 
D 4 HOH   17  917  257 HOH   HOH A . 
D 4 HOH   18  918  235 HOH   HOH A . 
D 4 HOH   19  919  242 HOH   HOH A . 
D 4 HOH   20  920  238 HOH   HOH A . 
D 4 HOH   21  921  220 HOH   HOH A . 
D 4 HOH   22  922  95  HOH   HOH A . 
D 4 HOH   23  923  279 HOH   HOH A . 
D 4 HOH   24  924  250 HOH   HOH A . 
D 4 HOH   25  925  51  HOH   HOH A . 
D 4 HOH   26  926  93  HOH   HOH A . 
D 4 HOH   27  927  53  HOH   HOH A . 
D 4 HOH   28  928  273 HOH   HOH A . 
D 4 HOH   29  929  258 HOH   HOH A . 
D 4 HOH   30  930  271 HOH   HOH A . 
D 4 HOH   31  931  188 HOH   HOH A . 
D 4 HOH   32  932  33  HOH   HOH A . 
D 4 HOH   33  933  60  HOH   HOH A . 
D 4 HOH   34  934  80  HOH   HOH A . 
D 4 HOH   35  935  165 HOH   HOH A . 
D 4 HOH   36  936  160 HOH   HOH A . 
D 4 HOH   37  937  150 HOH   HOH A . 
D 4 HOH   38  938  177 HOH   HOH A . 
D 4 HOH   39  939  215 HOH   HOH A . 
D 4 HOH   40  940  121 HOH   HOH A . 
D 4 HOH   41  941  14  HOH   HOH A . 
D 4 HOH   42  942  3   HOH   HOH A . 
D 4 HOH   43  943  124 HOH   HOH A . 
D 4 HOH   44  944  32  HOH   HOH A . 
D 4 HOH   45  945  6   HOH   HOH A . 
D 4 HOH   46  946  173 HOH   HOH A . 
D 4 HOH   47  947  26  HOH   HOH A . 
D 4 HOH   48  948  130 HOH   HOH A . 
D 4 HOH   49  949  50  HOH   HOH A . 
D 4 HOH   50  950  28  HOH   HOH A . 
D 4 HOH   51  951  101 HOH   HOH A . 
D 4 HOH   52  952  86  HOH   HOH A . 
D 4 HOH   53  953  5   HOH   HOH A . 
D 4 HOH   54  954  88  HOH   HOH A . 
D 4 HOH   55  955  8   HOH   HOH A . 
D 4 HOH   56  956  7   HOH   HOH A . 
D 4 HOH   57  957  73  HOH   HOH A . 
D 4 HOH   58  958  152 HOH   HOH A . 
D 4 HOH   59  959  114 HOH   HOH A . 
D 4 HOH   60  960  11  HOH   HOH A . 
D 4 HOH   61  961  40  HOH   HOH A . 
D 4 HOH   62  962  34  HOH   HOH A . 
D 4 HOH   63  963  64  HOH   HOH A . 
D 4 HOH   64  964  29  HOH   HOH A . 
D 4 HOH   65  965  270 HOH   HOH A . 
D 4 HOH   66  966  179 HOH   HOH A . 
D 4 HOH   67  967  79  HOH   HOH A . 
D 4 HOH   68  968  12  HOH   HOH A . 
D 4 HOH   69  969  164 HOH   HOH A . 
D 4 HOH   70  970  222 HOH   HOH A . 
D 4 HOH   71  971  37  HOH   HOH A . 
D 4 HOH   72  972  134 HOH   HOH A . 
D 4 HOH   73  973  103 HOH   HOH A . 
D 4 HOH   74  974  1   HOH   HOH A . 
D 4 HOH   75  975  91  HOH   HOH A . 
D 4 HOH   76  976  159 HOH   HOH A . 
D 4 HOH   77  977  66  HOH   HOH A . 
D 4 HOH   78  978  123 HOH   HOH A . 
D 4 HOH   79  979  58  HOH   HOH A . 
D 4 HOH   80  980  27  HOH   HOH A . 
D 4 HOH   81  981  116 HOH   HOH A . 
D 4 HOH   82  982  131 HOH   HOH A . 
D 4 HOH   83  983  18  HOH   HOH A . 
D 4 HOH   84  984  162 HOH   HOH A . 
D 4 HOH   85  985  276 HOH   HOH A . 
D 4 HOH   86  986  261 HOH   HOH A . 
D 4 HOH   87  987  16  HOH   HOH A . 
D 4 HOH   88  988  65  HOH   HOH A . 
D 4 HOH   89  989  9   HOH   HOH A . 
D 4 HOH   90  990  108 HOH   HOH A . 
D 4 HOH   91  991  140 HOH   HOH A . 
D 4 HOH   92  992  71  HOH   HOH A . 
D 4 HOH   93  993  82  HOH   HOH A . 
D 4 HOH   94  994  104 HOH   HOH A . 
D 4 HOH   95  995  59  HOH   HOH A . 
D 4 HOH   96  996  20  HOH   HOH A . 
D 4 HOH   97  997  278 HOH   HOH A . 
D 4 HOH   98  998  36  HOH   HOH A . 
D 4 HOH   99  999  2   HOH   HOH A . 
D 4 HOH   100 1000 260 HOH   HOH A . 
D 4 HOH   101 1001 23  HOH   HOH A . 
D 4 HOH   102 1002 47  HOH   HOH A . 
D 4 HOH   103 1003 52  HOH   HOH A . 
D 4 HOH   104 1004 67  HOH   HOH A . 
D 4 HOH   105 1005 163 HOH   HOH A . 
D 4 HOH   106 1006 63  HOH   HOH A . 
D 4 HOH   107 1007 110 HOH   HOH A . 
D 4 HOH   108 1008 48  HOH   HOH A . 
D 4 HOH   109 1009 175 HOH   HOH A . 
D 4 HOH   110 1010 4   HOH   HOH A . 
D 4 HOH   111 1011 30  HOH   HOH A . 
D 4 HOH   112 1012 19  HOH   HOH A . 
D 4 HOH   113 1013 62  HOH   HOH A . 
D 4 HOH   114 1014 17  HOH   HOH A . 
D 4 HOH   115 1015 54  HOH   HOH A . 
D 4 HOH   116 1016 21  HOH   HOH A . 
D 4 HOH   117 1017 87  HOH   HOH A . 
D 4 HOH   118 1018 15  HOH   HOH A . 
D 4 HOH   119 1019 214 HOH   HOH A . 
D 4 HOH   120 1020 253 HOH   HOH A . 
D 4 HOH   121 1021 107 HOH   HOH A . 
D 4 HOH   122 1022 72  HOH   HOH A . 
D 4 HOH   123 1023 144 HOH   HOH A . 
D 4 HOH   124 1024 61  HOH   HOH A . 
D 4 HOH   125 1025 39  HOH   HOH A . 
D 4 HOH   126 1026 68  HOH   HOH A . 
D 4 HOH   127 1027 75  HOH   HOH A . 
D 4 HOH   128 1028 256 HOH   HOH A . 
D 4 HOH   129 1029 97  HOH   HOH A . 
D 4 HOH   130 1030 94  HOH   HOH A . 
D 4 HOH   131 1031 85  HOH   HOH A . 
D 4 HOH   132 1032 46  HOH   HOH A . 
D 4 HOH   133 1033 38  HOH   HOH A . 
D 4 HOH   134 1034 100 HOH   HOH A . 
D 4 HOH   135 1035 146 HOH   HOH A . 
D 4 HOH   136 1036 44  HOH   HOH A . 
D 4 HOH   137 1037 112 HOH   HOH A . 
D 4 HOH   138 1038 263 HOH   HOH A . 
D 4 HOH   139 1039 139 HOH   HOH A . 
D 4 HOH   140 1040 77  HOH   HOH A . 
D 4 HOH   141 1041 145 HOH   HOH A . 
D 4 HOH   142 1042 57  HOH   HOH A . 
D 4 HOH   143 1043 151 HOH   HOH A . 
D 4 HOH   144 1044 22  HOH   HOH A . 
D 4 HOH   145 1045 70  HOH   HOH A . 
D 4 HOH   146 1046 189 HOH   HOH A . 
D 4 HOH   147 1047 84  HOH   HOH A . 
D 4 HOH   148 1048 227 HOH   HOH A . 
D 4 HOH   149 1049 13  HOH   HOH A . 
D 4 HOH   150 1050 133 HOH   HOH A . 
D 4 HOH   151 1051 190 HOH   HOH A . 
D 4 HOH   152 1052 226 HOH   HOH A . 
D 4 HOH   153 1053 31  HOH   HOH A . 
D 4 HOH   154 1054 178 HOH   HOH A . 
D 4 HOH   155 1055 24  HOH   HOH A . 
D 4 HOH   156 1056 25  HOH   HOH A . 
D 4 HOH   157 1057 43  HOH   HOH A . 
D 4 HOH   158 1058 129 HOH   HOH A . 
D 4 HOH   159 1059 42  HOH   HOH A . 
D 4 HOH   160 1060 171 HOH   HOH A . 
D 4 HOH   161 1061 41  HOH   HOH A . 
D 4 HOH   162 1062 248 HOH   HOH A . 
D 4 HOH   163 1063 182 HOH   HOH A . 
D 4 HOH   164 1064 136 HOH   HOH A . 
D 4 HOH   165 1065 119 HOH   HOH A . 
D 4 HOH   166 1066 294 HOH   HOH A . 
D 4 HOH   167 1067 111 HOH   HOH A . 
D 4 HOH   168 1068 269 HOH   HOH A . 
D 4 HOH   169 1069 239 HOH   HOH A . 
D 4 HOH   170 1070 157 HOH   HOH A . 
D 4 HOH   171 1071 156 HOH   HOH A . 
D 4 HOH   172 1072 78  HOH   HOH A . 
D 4 HOH   173 1073 223 HOH   HOH A . 
D 4 HOH   174 1074 153 HOH   HOH A . 
D 4 HOH   175 1075 76  HOH   HOH A . 
D 4 HOH   176 1076 74  HOH   HOH A . 
D 4 HOH   177 1077 92  HOH   HOH A . 
D 4 HOH   178 1078 236 HOH   HOH A . 
D 4 HOH   179 1079 81  HOH   HOH A . 
D 4 HOH   180 1080 264 HOH   HOH A . 
D 4 HOH   181 1081 280 HOH   HOH A . 
D 4 HOH   182 1082 96  HOH   HOH A . 
D 4 HOH   183 1083 283 HOH   HOH A . 
D 4 HOH   184 1084 10  HOH   HOH A . 
D 4 HOH   185 1085 229 HOH   HOH A . 
D 4 HOH   186 1086 147 HOH   HOH A . 
D 4 HOH   187 1087 35  HOH   HOH A . 
D 4 HOH   188 1088 277 HOH   HOH A . 
D 4 HOH   189 1089 117 HOH   HOH A . 
D 4 HOH   190 1090 90  HOH   HOH A . 
D 4 HOH   191 1091 56  HOH   HOH A . 
D 4 HOH   192 1092 98  HOH   HOH A . 
D 4 HOH   193 1093 113 HOH   HOH A . 
D 4 HOH   194 1094 268 HOH   HOH A . 
D 4 HOH   195 1095 169 HOH   HOH A . 
D 4 HOH   196 1096 287 HOH   HOH A . 
D 4 HOH   197 1097 172 HOH   HOH A . 
D 4 HOH   198 1098 225 HOH   HOH A . 
D 4 HOH   199 1099 55  HOH   HOH A . 
D 4 HOH   200 1100 115 HOH   HOH A . 
D 4 HOH   201 1101 141 HOH   HOH A . 
D 4 HOH   202 1102 259 HOH   HOH A . 
D 4 HOH   203 1103 224 HOH   HOH A . 
D 4 HOH   204 1104 69  HOH   HOH A . 
D 4 HOH   205 1105 217 HOH   HOH A . 
D 4 HOH   206 1106 105 HOH   HOH A . 
D 4 HOH   207 1107 122 HOH   HOH A . 
D 4 HOH   208 1108 262 HOH   HOH A . 
D 4 HOH   209 1109 251 HOH   HOH A . 
D 4 HOH   210 1110 208 HOH   HOH A . 
D 4 HOH   211 1111 286 HOH   HOH A . 
D 4 HOH   212 1112 154 HOH   HOH A . 
D 4 HOH   213 1113 109 HOH   HOH A . 
D 4 HOH   214 1114 265 HOH   HOH A . 
D 4 HOH   215 1115 297 HOH   HOH A . 
D 4 HOH   216 1116 132 HOH   HOH A . 
D 4 HOH   217 1117 284 HOH   HOH A . 
D 4 HOH   218 1118 218 HOH   HOH A . 
D 4 HOH   219 1119 194 HOH   HOH A . 
D 4 HOH   220 1120 240 HOH   HOH A . 
D 4 HOH   221 1121 49  HOH   HOH A . 
D 4 HOH   222 1122 168 HOH   HOH A . 
D 4 HOH   223 1123 161 HOH   HOH A . 
D 4 HOH   224 1124 184 HOH   HOH A . 
D 4 HOH   225 1125 221 HOH   HOH A . 
D 4 HOH   226 1126 282 HOH   HOH A . 
D 4 HOH   227 1127 213 HOH   HOH A . 
D 4 HOH   228 1128 298 HOH   HOH A . 
D 4 HOH   229 1129 237 HOH   HOH A . 
D 4 HOH   230 1130 143 HOH   HOH A . 
D 4 HOH   231 1131 296 HOH   HOH A . 
D 4 HOH   232 1132 83  HOH   HOH A . 
D 4 HOH   233 1133 246 HOH   HOH A . 
D 4 HOH   234 1134 252 HOH   HOH A . 
D 4 HOH   235 1135 118 HOH   HOH A . 
D 4 HOH   236 1136 198 HOH   HOH A . 
D 4 HOH   237 1137 249 HOH   HOH A . 
D 4 HOH   238 1138 290 HOH   HOH A . 
D 4 HOH   239 1139 288 HOH   HOH A . 
D 4 HOH   240 1140 233 HOH   HOH A . 
D 4 HOH   241 1141 289 HOH   HOH A . 
D 4 HOH   242 1142 207 HOH   HOH A . 
D 4 HOH   243 1143 137 HOH   HOH A . 
D 4 HOH   244 1144 230 HOH   HOH A . 
D 4 HOH   245 1145 200 HOH   HOH A . 
D 4 HOH   246 1146 295 HOH   HOH A . 
D 4 HOH   247 1147 232 HOH   HOH A . 
D 4 HOH   248 1148 191 HOH   HOH A . 
D 4 HOH   249 1149 285 HOH   HOH A . 
D 4 HOH   250 1150 120 HOH   HOH A . 
D 4 HOH   251 1151 247 HOH   HOH A . 
D 4 HOH   252 1152 255 HOH   HOH A . 
D 4 HOH   253 1153 128 HOH   HOH A . 
D 4 HOH   254 1154 291 HOH   HOH A . 
D 4 HOH   255 1155 89  HOH   HOH A . 
D 4 HOH   256 1156 102 HOH   HOH A . 
D 4 HOH   257 1157 293 HOH   HOH A . 
D 4 HOH   258 1158 244 HOH   HOH A . 
D 4 HOH   259 1159 127 HOH   HOH A . 
D 4 HOH   260 1160 254 HOH   HOH A . 
D 4 HOH   261 1161 281 HOH   HOH A . 
D 4 HOH   262 1162 243 HOH   HOH A . 
D 4 HOH   263 1163 199 HOH   HOH A . 
D 4 HOH   264 1164 203 HOH   HOH A . 
D 4 HOH   265 1165 292 HOH   HOH A . 
D 4 HOH   266 1166 186 HOH   HOH A . 
D 4 HOH   267 1167 201 HOH   HOH A . 
# 
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  ? ? ? 1.18.2-3874_final 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DC9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     89.749 
_cell.length_a_esd                 ? 
_cell.length_b                     89.749 
_cell.length_b_esd                 ? 
_cell.length_c                     85.963 
_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                         9DC9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                79 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 4' 
_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                   9DC9 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.99 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.25 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_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 Tris pH 8.5, 0.2 M sodium citrate, & 30% PEG400' 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-09-09 
_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   1.18057 
_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                        'CLSI BEAMLINE 08B1-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.18057 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08B1-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DC9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.19 
_reflns.d_resolution_low                               44.87 
_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                                     95597 
_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                           86.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.96 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.059 
_reflns.pdbx_Rpim_I_all                                0.023 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       573257 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.054 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.19 
_reflns_shell.d_res_low                                     1.21 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2306 
_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                               1.4 
_reflns_shell.pdbx_chi_squared                              0.93 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               5.722 
_reflns_shell.pdbx_Rpim_I_all                               3.963 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.01 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  4.115 
_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                                 9DC9 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.60 
_refine.ls_d_res_low                             35.59 
_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                     88300 
_refine.ls_number_reflns_R_free                  4279 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.71 
_refine.ls_percent_reflns_R_free                 4.85 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1668 
_refine.ls_R_factor_R_free                       0.1904 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1656 
_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                          0.01 
_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             1.11 
_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                 21.39 
_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                            0.13 
_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.pdbx_number_atoms_protein        2486 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         49 
_refine_hist.number_atoms_solvent             267 
_refine_hist.number_atoms_total               2802 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        35.59 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  ? 2631 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.887  ? 3592 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.119 ? 948  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.061  ? 432  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 482  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.60 1.62  . . 135 2840 100.00 . . . . 0.2480 . . . . . . . . . . . 0.2786 
'X-RAY DIFFRACTION' 1.62 1.64  . . 146 2750 99.00  . . . . 0.2348 . . . . . . . . . . . 0.2719 
'X-RAY DIFFRACTION' 1.64 1.66  . . 126 2819 99.00  . . . . 0.2199 . . . . . . . . . . . 0.2308 
'X-RAY DIFFRACTION' 1.66 1.68  . . 138 2789 100.00 . . . . 0.2039 . . . . . . . . . . . 0.2431 
'X-RAY DIFFRACTION' 1.68 1.70  . . 74  2887 100.00 . . . . 0.2061 . . . . . . . . . . . 0.2102 
'X-RAY DIFFRACTION' 1.70 1.72  . . 166 2773 100.00 . . . . 0.2061 . . . . . . . . . . . 0.2609 
'X-RAY DIFFRACTION' 1.72 1.75  . . 167 2768 100.00 . . . . 0.2111 . . . . . . . . . . . 0.2701 
'X-RAY DIFFRACTION' 1.75 1.77  . . 124 2860 100.00 . . . . 0.1902 . . . . . . . . . . . 0.2340 
'X-RAY DIFFRACTION' 1.77 1.80  . . 109 2749 100.00 . . . . 0.1775 . . . . . . . . . . . 0.1861 
'X-RAY DIFFRACTION' 1.80 1.83  . . 156 2870 100.00 . . . . 0.1698 . . . . . . . . . . . 0.2305 
'X-RAY DIFFRACTION' 1.83 1.86  . . 142 2774 100.00 . . . . 0.1611 . . . . . . . . . . . 0.2176 
'X-RAY DIFFRACTION' 1.86 1.90  . . 162 2754 100.00 . . . . 0.1717 . . . . . . . . . . . 0.2071 
'X-RAY DIFFRACTION' 1.90 1.93  . . 135 2794 100.00 . . . . 0.1704 . . . . . . . . . . . 0.1909 
'X-RAY DIFFRACTION' 1.93 1.97  . . 142 2832 99.00  . . . . 0.1612 . . . . . . . . . . . 0.1873 
'X-RAY DIFFRACTION' 1.97 2.02  . . 137 2806 100.00 . . . . 0.1585 . . . . . . . . . . . 0.1883 
'X-RAY DIFFRACTION' 2.02 2.06  . . 159 2795 100.00 . . . . 0.1723 . . . . . . . . . . . 0.1929 
'X-RAY DIFFRACTION' 2.06 2.11  . . 136 2784 100.00 . . . . 0.1627 . . . . . . . . . . . 0.1786 
'X-RAY DIFFRACTION' 2.11 2.17  . . 126 2801 100.00 . . . . 0.1587 . . . . . . . . . . . 0.1692 
'X-RAY DIFFRACTION' 2.17 2.24  . . 130 2835 100.00 . . . . 0.1545 . . . . . . . . . . . 0.2205 
'X-RAY DIFFRACTION' 2.24 2.31  . . 122 2842 100.00 . . . . 0.1599 . . . . . . . . . . . 0.1865 
'X-RAY DIFFRACTION' 2.31 2.39  . . 176 2791 100.00 . . . . 0.1589 . . . . . . . . . . . 0.1872 
'X-RAY DIFFRACTION' 2.39 2.49  . . 133 2804 100.00 . . . . 0.1569 . . . . . . . . . . . 0.2180 
'X-RAY DIFFRACTION' 2.49 2.60  . . 160 2778 100.00 . . . . 0.1654 . . . . . . . . . . . 0.2260 
'X-RAY DIFFRACTION' 2.60 2.74  . . 163 2790 100.00 . . . . 0.1753 . . . . . . . . . . . 0.1806 
'X-RAY DIFFRACTION' 2.74 2.91  . . 142 2781 99.00  . . . . 0.1823 . . . . . . . . . . . 0.1990 
'X-RAY DIFFRACTION' 2.91 3.13  . . 138 2761 100.00 . . . . 0.1653 . . . . . . . . . . . 0.1605 
'X-RAY DIFFRACTION' 3.13 3.45  . . 176 2818 100.00 . . . . 0.1640 . . . . . . . . . . . 0.1773 
'X-RAY DIFFRACTION' 3.45 3.94  . . 164 2760 100.00 . . . . 0.1460 . . . . . . . . . . . 0.1870 
'X-RAY DIFFRACTION' 3.94 4.96  . . 161 2810 100.00 . . . . 0.1405 . . . . . . . . . . . 0.1555 
'X-RAY DIFFRACTION' 4.97 35.59 . . 134 2806 100.00 . . . . 0.1750 . . . . . . . . . . . 0.1821 
# 
_struct.entry_id                     9DC9 
_struct.title                        'Mtb GuaB dCBS in complex with inhibitor compound 5' 
_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        9DC9 
_struct_keywords.text            'GuaB, IMPDH, tuberculosis, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
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 IMDH_MYCTU P9WKI7 ? 1 
;SRGMSGLEDSSDLVVSPYVRMGGLTTDPVPTGGDDPHKVAMLGLTFDDVLLLPAASDVVPATADTSSQLTKKIRLKVPLV
SSAMDTVTESRMAIAMARAGGMGVLHRNLPVAEQAGQVEMVKRS
;
2   
2 UNP IMDH_MYCTU P9WKI7 ? 1 
;LLVGAAVGVGGDAWVRAMMLVDAGVDVLVVDTAHAHNRLVLDMVGKLKSEVGDRVEVVGGNVATRSAAAALVDAGADAVK
VGVGPGSICTTRVVAGVGAPQITAILEAVAACRPAGVPVIADGGLQYSGDIAKALAAGASTAMLGSLLAGTAEAPGELIF
VNGKQYKSYRGMGSLGAMRGRGGATSYSKDRYFADDALSEDKLVPEGIEGRVPFRGPLSSVIHQLTGGLRAAMGYTGSPT
IEVLQQAQFVRITPAGLKESHPHDVAMTVEAPNYYAR
;
253 
# 
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 9DC9 A 17  ? 140 ? P9WKI7 2   ? 125 ? 2   125 
2 2 9DC9 A 143 ? 419 ? P9WKI7 253 ? 529 ? 253 529 
# 
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 9DC9 MET A 1   ? UNP P9WKI7 ? ? 'initiating methionine' -14 1  
1 9DC9 HIS A 2   ? UNP P9WKI7 ? ? 'expression tag'        -13 2  
1 9DC9 HIS A 3   ? UNP P9WKI7 ? ? 'expression tag'        -12 3  
1 9DC9 HIS A 4   ? UNP P9WKI7 ? ? 'expression tag'        -11 4  
1 9DC9 HIS A 5   ? UNP P9WKI7 ? ? 'expression tag'        -10 5  
1 9DC9 HIS A 6   ? UNP P9WKI7 ? ? 'expression tag'        -9  6  
1 9DC9 HIS A 7   ? UNP P9WKI7 ? ? 'expression tag'        -8  7  
1 9DC9 GLY A 8   ? UNP P9WKI7 ? ? 'expression tag'        -7  8  
1 9DC9 GLU A 9   ? UNP P9WKI7 ? ? 'expression tag'        -6  9  
1 9DC9 ASN A 10  ? UNP P9WKI7 ? ? 'expression tag'        -5  10 
1 9DC9 LEU A 11  ? UNP P9WKI7 ? ? 'expression tag'        -4  11 
1 9DC9 TYR A 12  ? UNP P9WKI7 ? ? 'expression tag'        -3  12 
1 9DC9 PHE A 13  ? UNP P9WKI7 ? ? 'expression tag'        -2  13 
1 9DC9 GLN A 14  ? UNP P9WKI7 ? ? 'expression tag'        -1  14 
1 9DC9 GLY A 15  ? UNP P9WKI7 ? ? 'expression tag'        0   15 
1 9DC9 SER A 16  ? UNP P9WKI7 ? ? 'expression tag'        1   16 
1 9DC9 GLY A 141 ? UNP P9WKI7 ? ? linker                  126 17 
1 9DC9 GLY A 142 ? UNP P9WKI7 ? ? linker                  127 18 
2 9DC9 GLY A 420 ? UNP P9WKI7 ? ? 'expression tag'        530 19 
2 9DC9 ASN A 421 ? UNP P9WKI7 ? ? 'expression tag'        531 20 
2 9DC9 SER A 422 ? UNP P9WKI7 ? ? 'expression tag'        532 21 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 22510 ? 
1 MORE         -134  ? 
1 'SSA (A^2)'  47860 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                
'Two tetramers can also stack to produce an octamer in some GuaB examples.' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000  0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -x,-y,z -1.0000000000 0.0000000000  0.0000000000 0.0000000000 0.0000000000  -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_555 -y,x,z  0.0000000000  -1.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 y,-x,z  0.0000000000  1.0000000000  0.0000000000 0.0000000000 -1.0000000000 0.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 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 THR A 61  ? ASP A 63  ? THR A 46  ASP A 48  5 ? 3  
HELX_P HELX_P2  AA2 VAL A 75  ? ALA A 79  ? VAL A 60  ALA A 64  5 ? 5  
HELX_P HELX_P3  AA3 GLU A 105 ? ALA A 115 ? GLU A 90  ALA A 100 1 ? 11 
HELX_P HELX_P4  AA4 PRO A 126 ? ARG A 139 ? PRO A 111 ARG A 124 1 ? 14 
HELX_P HELX_P5  AA5 GLY A 152 ? ALA A 165 ? GLY A 262 ALA A 275 1 ? 14 
HELX_P HELX_P6  AA6 ASN A 179 ? GLY A 194 ? ASN A 289 GLY A 304 1 ? 16 
HELX_P HELX_P7  AA7 THR A 206 ? ALA A 216 ? THR A 316 ALA A 326 1 ? 11 
HELX_P HELX_P8  AA8 THR A 232 ? ALA A 237 ? THR A 342 ALA A 347 1 ? 6  
HELX_P HELX_P9  AA9 PRO A 242 ? ARG A 255 ? PRO A 352 ARG A 365 1 ? 14 
HELX_P HELX_P10 AB1 PRO A 256 ? GLY A 258 ? PRO A 366 GLY A 368 5 ? 3  
HELX_P HELX_P11 AB2 TYR A 269 ? ALA A 279 ? TYR A 379 ALA A 389 1 ? 11 
HELX_P HELX_P12 AB3 GLY A 287 ? GLY A 292 ? GLY A 397 GLY A 402 1 ? 6  
HELX_P HELX_P13 AB4 SER A 316 ? ARG A 321 ? SER A 426 ARG A 431 1 ? 6  
HELX_P HELX_P14 AB5 PRO A 359 ? GLY A 379 ? PRO A 469 GLY A 489 1 ? 21 
HELX_P HELX_P15 AB6 THR A 382 ? GLN A 387 ? THR A 492 GLN A 497 1 ? 6  
HELX_P HELX_P16 AB7 THR A 395 ? GLU A 401 ? THR A 505 GLU A 511 1 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           202 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            312 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   ASN 
_struct_mon_prot_cis.pdbx_label_seq_id_2    203 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    ASN 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     313 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       1.59 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 9 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA3 7 8 ? parallel      
AA3 8 9 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 65  ? LEU A 67  ? VAL A 50  LEU A 52  
AA1 2 PHE A 391 ? ARG A 393 ? PHE A 501 ARG A 503 
AA2 1 SER A 83  ? GLN A 84  ? SER A 68  GLN A 69  
AA2 2 ARG A 90  ? LEU A 91  ? ARG A 75  LEU A 76  
AA3 1 LEU A 95  ? SER A 97  ? LEU A 80  SER A 82  
AA3 2 MET A 118 ? LEU A 121 ? MET A 103 LEU A 106 
AA3 3 GLY A 146 ? VAL A 149 ? GLY A 256 VAL A 259 
AA3 4 VAL A 169 ? ASP A 173 ? VAL A 279 ASP A 283 
AA3 5 GLU A 198 ? VAL A 204 ? GLU A 308 VAL A 314 
AA3 6 ALA A 220 ? VAL A 223 ? ALA A 330 VAL A 333 
AA3 7 VAL A 261 ? ASP A 264 ? VAL A 371 ASP A 374 
AA3 8 THR A 283 ? LEU A 286 ? THR A 393 LEU A 396 
AA3 9 LEU A 95  ? SER A 97  ? LEU A 80  SER A 82  
AA4 1 ILE A 301 ? VAL A 303 ? ILE A 411 VAL A 413 
AA4 2 LYS A 306 ? ARG A 312 ? LYS A 416 ARG A 422 
AA4 3 GLU A 351 ? PRO A 355 ? GLU A 461 PRO A 465 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 66  ? N LEU A 51  O VAL A 392 ? O VAL A 502 
AA2 1 2 N SER A 83  ? N SER A 68  O LEU A 91  ? O LEU A 76  
AA3 1 2 N SER A 97  ? N SER A 82  O MET A 118 ? O MET A 103 
AA3 2 3 N LEU A 121 ? N LEU A 106 O GLY A 146 ? O GLY A 256 
AA3 3 4 N VAL A 149 ? N VAL A 259 O ASP A 173 ? O ASP A 283 
AA3 4 5 N VAL A 172 ? N VAL A 282 O VAL A 200 ? O VAL A 310 
AA3 5 6 N GLY A 201 ? N GLY A 311 O LYS A 222 ? O LYS A 332 
AA3 6 7 N VAL A 223 ? N VAL A 333 O ILE A 262 ? O ILE A 372 
AA3 7 8 N ALA A 263 ? N ALA A 373 O THR A 283 ? O THR A 393 
AA3 8 9 O LEU A 286 ? O LEU A 396 N VAL A 96  ? N VAL A 81  
AA4 1 2 N VAL A 303 ? N VAL A 413 O LYS A 306 ? O LYS A 416 
AA4 2 3 N TYR A 311 ? N TYR A 421 O GLY A 352 ? O GLY A 462 
# 
_pdbx_entry_details.entry_id                   9DC9 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 906  ? ? O A HOH 1077 ? ? 1.83 
2  1 O   A HOH 1110 ? ? O A HOH 1142 ? ? 1.97 
3  1 O   A HOH 993  ? ? O A HOH 1080 ? ? 2.03 
4  1 O   A HOH 1068 ? ? O A HOH 1112 ? ? 2.04 
5  1 O   A HOH 1066 ? ? O A HOH 1102 ? ? 2.09 
6  1 O   A HOH 1060 ? ? O A HOH 1127 ? ? 2.11 
7  1 O   A HOH 1045 ? ? O A HOH 1081 ? ? 2.11 
8  1 NH1 A ARG 365  ? ? O A HOH 901  ? ? 2.14 
9  1 O   A HOH 1100 ? ? O A HOH 1108 ? ? 2.15 
10 1 O   A HOH 990  ? ? O A HOH 1145 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 1090 ? ? 1_555 O A HOH 1118 ? ? 6_555 1.90 
2 1 O A HOH 1098 ? ? 1_555 O A HOH 1144 ? ? 3_555 2.18 
# 
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 VAL A 88  ? ? -130.39 -53.48  
2 1 GLU A 90  ? ? -118.84 -157.49 
3 1 ASN A 109 ? ? -94.71  57.30   
4 1 ALA A 315 ? ? -145.22 13.10   
5 1 PRO A 514 ? ? -28.89  101.95  
6 1 ASP A 516 ? ? 60.47   65.35   
7 1 VAL A 517 ? ? -164.78 98.09   
8 1 ALA A 518 ? ? -41.40  107.95  
# 
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 -14 ? A MET 1   
2  1 Y 1 A HIS -13 ? A HIS 2   
3  1 Y 1 A HIS -12 ? A HIS 3   
4  1 Y 1 A HIS -11 ? A HIS 4   
5  1 Y 1 A HIS -10 ? A HIS 5   
6  1 Y 1 A HIS -9  ? A HIS 6   
7  1 Y 1 A HIS -8  ? A HIS 7   
8  1 Y 1 A GLY -7  ? A GLY 8   
9  1 Y 1 A GLU -6  ? A GLU 9   
10 1 Y 1 A ASN -5  ? A ASN 10  
11 1 Y 1 A LEU -4  ? A LEU 11  
12 1 Y 1 A TYR -3  ? A TYR 12  
13 1 Y 1 A PHE -2  ? A PHE 13  
14 1 Y 1 A GLN -1  ? A GLN 14  
15 1 Y 1 A GLY 0   ? A GLY 15  
16 1 Y 1 A SER 1   ? A SER 16  
17 1 Y 1 A SER 2   ? A SER 17  
18 1 Y 1 A ARG 3   ? A ARG 18  
19 1 Y 1 A GLY 4   ? A GLY 19  
20 1 Y 1 A MET 5   ? A MET 20  
21 1 Y 1 A SER 6   ? A SER 21  
22 1 Y 1 A GLY 7   ? A GLY 22  
23 1 Y 1 A LEU 8   ? A LEU 23  
24 1 Y 1 A GLU 9   ? A GLU 24  
25 1 Y 1 A ASP 10  ? A ASP 25  
26 1 Y 1 A SER 11  ? A SER 26  
27 1 Y 1 A SER 12  ? A SER 27  
28 1 Y 1 A ASP 13  ? A ASP 28  
29 1 Y 1 A LEU 14  ? A LEU 29  
30 1 Y 1 A VAL 15  ? A VAL 30  
31 1 Y 1 A VAL 16  ? A VAL 31  
32 1 Y 1 A SER 17  ? A SER 32  
33 1 Y 1 A PRO 18  ? A PRO 33  
34 1 Y 1 A TYR 19  ? A TYR 34  
35 1 Y 1 A VAL 20  ? A VAL 35  
36 1 Y 1 A ARG 21  ? A ARG 36  
37 1 Y 1 A MET 22  ? A MET 37  
38 1 Y 1 A GLY 23  ? A GLY 38  
39 1 Y 1 A GLY 24  ? A GLY 39  
40 1 Y 1 A LEU 25  ? A LEU 40  
41 1 Y 1 A THR 26  ? A THR 41  
42 1 Y 1 A GLY 432 ? A GLY 322 
43 1 Y 1 A ARG 433 ? A ARG 323 
44 1 Y 1 A GLY 434 ? A GLY 324 
45 1 Y 1 A GLY 435 ? A GLY 325 
46 1 Y 1 A ALA 436 ? A ALA 326 
47 1 Y 1 A THR 437 ? A THR 327 
48 1 Y 1 A SER 438 ? A SER 328 
49 1 Y 1 A TYR 439 ? A TYR 329 
50 1 Y 1 A SER 440 ? A SER 330 
51 1 Y 1 A LYS 441 ? A LYS 331 
52 1 Y 1 A ASP 442 ? A ASP 332 
53 1 Y 1 A ARG 443 ? A ARG 333 
54 1 Y 1 A TYR 444 ? A TYR 334 
55 1 Y 1 A PHE 445 ? A PHE 335 
56 1 Y 1 A ALA 446 ? A ALA 336 
57 1 Y 1 A ASP 447 ? A ASP 337 
58 1 Y 1 A ASP 448 ? A ASP 338 
59 1 Y 1 A ALA 449 ? A ALA 339 
60 1 Y 1 A LEU 450 ? A LEU 340 
61 1 Y 1 A SER 451 ? A SER 341 
62 1 Y 1 A GLU 452 ? A GLU 342 
63 1 Y 1 A ASP 453 ? A ASP 343 
64 1 Y 1 A LYS 454 ? A LYS 344 
65 1 Y 1 A TYR 526 ? A TYR 416 
66 1 Y 1 A TYR 527 ? A TYR 417 
67 1 Y 1 A ALA 528 ? A ALA 418 
68 1 Y 1 A ARG 529 ? A ARG 419 
69 1 Y 1 A GLY 530 ? A GLY 420 
70 1 Y 1 A ASN 531 ? A ASN 421 
71 1 Y 1 A SER 532 ? A SER 422 
# 
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 
A1A3K C4     C  Y N 1   
A1A3K C5     C  Y N 2   
A1A3K C6     C  Y N 3   
A1A3K C8     C  Y N 4   
A1A3K C9     C  Y N 5   
A1A3K C12    C  Y N 6   
A1A3K C13    C  Y N 7   
A1A3K C3     C  Y N 8   
A1A3K C1     C  N N 9   
A1A3K C17    C  Y N 10  
A1A3K C18    C  Y N 11  
A1A3K C19    C  Y N 12  
A1A3K C2     C  N R 13  
A1A3K C20    C  Y N 14  
A1A3K C21    C  Y N 15  
A1A3K C22    C  Y N 16  
A1A3K C23    C  Y N 17  
A1A3K C24    C  Y N 18  
A1A3K C25    C  Y N 19  
A1A3K N10    N  Y N 20  
A1A3K N14    N  Y N 21  
A1A3K N26    N  Y N 22  
A1A3K N27    N  Y N 23  
A1A3K N7     N  Y N 24  
A1A3K O16    O  N N 25  
A1A3K CL15   CL N N 26  
A1A3K H33    H  N N 27  
A1A3K H34    H  N N 28  
A1A3K H35    H  N N 29  
A1A3K H36    H  N N 30  
A1A3K H30    H  N N 31  
A1A3K H29    H  N N 32  
A1A3K H31    H  N N 33  
A1A3K H37    H  N N 34  
A1A3K H38    H  N N 35  
A1A3K H32    H  N N 36  
A1A3K H39    H  N N 37  
A1A3K H40    H  N N 38  
A1A3K H41    H  N N 39  
A1A3K H42    H  N N 40  
A1A3K H11    H  N N 41  
A1A3K H28    H  N N 42  
ALA   N      N  N N 43  
ALA   CA     C  N S 44  
ALA   C      C  N N 45  
ALA   O      O  N N 46  
ALA   CB     C  N N 47  
ALA   OXT    O  N N 48  
ALA   H      H  N N 49  
ALA   H2     H  N N 50  
ALA   HA     H  N N 51  
ALA   HB1    H  N N 52  
ALA   HB2    H  N N 53  
ALA   HB3    H  N N 54  
ALA   HXT    H  N N 55  
ARG   N      N  N N 56  
ARG   CA     C  N S 57  
ARG   C      C  N N 58  
ARG   O      O  N N 59  
ARG   CB     C  N N 60  
ARG   CG     C  N N 61  
ARG   CD     C  N N 62  
ARG   NE     N  N N 63  
ARG   CZ     C  N N 64  
ARG   NH1    N  N N 65  
ARG   NH2    N  N N 66  
ARG   OXT    O  N N 67  
ARG   H      H  N N 68  
ARG   H2     H  N N 69  
ARG   HA     H  N N 70  
ARG   HB2    H  N N 71  
ARG   HB3    H  N N 72  
ARG   HG2    H  N N 73  
ARG   HG3    H  N N 74  
ARG   HD2    H  N N 75  
ARG   HD3    H  N N 76  
ARG   HE     H  N N 77  
ARG   HH11   H  N N 78  
ARG   HH12   H  N N 79  
ARG   HH21   H  N N 80  
ARG   HH22   H  N N 81  
ARG   HXT    H  N N 82  
ASN   N      N  N N 83  
ASN   CA     C  N S 84  
ASN   C      C  N N 85  
ASN   O      O  N N 86  
ASN   CB     C  N N 87  
ASN   CG     C  N N 88  
ASN   OD1    O  N N 89  
ASN   ND2    N  N N 90  
ASN   OXT    O  N N 91  
ASN   H      H  N N 92  
ASN   H2     H  N N 93  
ASN   HA     H  N N 94  
ASN   HB2    H  N N 95  
ASN   HB3    H  N N 96  
ASN   HD21   H  N N 97  
ASN   HD22   H  N N 98  
ASN   HXT    H  N N 99  
ASP   N      N  N N 100 
ASP   CA     C  N S 101 
ASP   C      C  N N 102 
ASP   O      O  N N 103 
ASP   CB     C  N N 104 
ASP   CG     C  N N 105 
ASP   OD1    O  N N 106 
ASP   OD2    O  N N 107 
ASP   OXT    O  N N 108 
ASP   H      H  N N 109 
ASP   H2     H  N N 110 
ASP   HA     H  N N 111 
ASP   HB2    H  N N 112 
ASP   HB3    H  N N 113 
ASP   HD2    H  N N 114 
ASP   HXT    H  N N 115 
CYS   N      N  N N 116 
CYS   CA     C  N R 117 
CYS   C      C  N N 118 
CYS   O      O  N N 119 
CYS   CB     C  N N 120 
CYS   SG     S  N N 121 
CYS   OXT    O  N N 122 
CYS   H      H  N N 123 
CYS   H2     H  N N 124 
CYS   HA     H  N N 125 
CYS   HB2    H  N N 126 
CYS   HB3    H  N N 127 
CYS   HG     H  N N 128 
CYS   HXT    H  N N 129 
GLN   N      N  N N 130 
GLN   CA     C  N S 131 
GLN   C      C  N N 132 
GLN   O      O  N N 133 
GLN   CB     C  N N 134 
GLN   CG     C  N N 135 
GLN   CD     C  N N 136 
GLN   OE1    O  N N 137 
GLN   NE2    N  N N 138 
GLN   OXT    O  N N 139 
GLN   H      H  N N 140 
GLN   H2     H  N N 141 
GLN   HA     H  N N 142 
GLN   HB2    H  N N 143 
GLN   HB3    H  N N 144 
GLN   HG2    H  N N 145 
GLN   HG3    H  N N 146 
GLN   HE21   H  N N 147 
GLN   HE22   H  N N 148 
GLN   HXT    H  N N 149 
GLU   N      N  N N 150 
GLU   CA     C  N S 151 
GLU   C      C  N N 152 
GLU   O      O  N N 153 
GLU   CB     C  N N 154 
GLU   CG     C  N N 155 
GLU   CD     C  N N 156 
GLU   OE1    O  N N 157 
GLU   OE2    O  N N 158 
GLU   OXT    O  N N 159 
GLU   H      H  N N 160 
GLU   H2     H  N N 161 
GLU   HA     H  N N 162 
GLU   HB2    H  N N 163 
GLU   HB3    H  N N 164 
GLU   HG2    H  N N 165 
GLU   HG3    H  N N 166 
GLU   HE2    H  N N 167 
GLU   HXT    H  N N 168 
GLY   N      N  N N 169 
GLY   CA     C  N N 170 
GLY   C      C  N N 171 
GLY   O      O  N N 172 
GLY   OXT    O  N N 173 
GLY   H      H  N N 174 
GLY   H2     H  N N 175 
GLY   HA2    H  N N 176 
GLY   HA3    H  N N 177 
GLY   HXT    H  N N 178 
HIS   N      N  N N 179 
HIS   CA     C  N S 180 
HIS   C      C  N N 181 
HIS   O      O  N N 182 
HIS   CB     C  N N 183 
HIS   CG     C  Y N 184 
HIS   ND1    N  Y N 185 
HIS   CD2    C  Y N 186 
HIS   CE1    C  Y N 187 
HIS   NE2    N  Y N 188 
HIS   OXT    O  N N 189 
HIS   H      H  N N 190 
HIS   H2     H  N N 191 
HIS   HA     H  N N 192 
HIS   HB2    H  N N 193 
HIS   HB3    H  N N 194 
HIS   HD1    H  N N 195 
HIS   HD2    H  N N 196 
HIS   HE1    H  N N 197 
HIS   HE2    H  N N 198 
HIS   HXT    H  N N 199 
HOH   O      O  N N 200 
HOH   H1     H  N N 201 
HOH   H2     H  N N 202 
ILE   N      N  N N 203 
ILE   CA     C  N S 204 
ILE   C      C  N N 205 
ILE   O      O  N N 206 
ILE   CB     C  N S 207 
ILE   CG1    C  N N 208 
ILE   CG2    C  N N 209 
ILE   CD1    C  N N 210 
ILE   OXT    O  N N 211 
ILE   H      H  N N 212 
ILE   H2     H  N N 213 
ILE   HA     H  N N 214 
ILE   HB     H  N N 215 
ILE   HG12   H  N N 216 
ILE   HG13   H  N N 217 
ILE   HG21   H  N N 218 
ILE   HG22   H  N N 219 
ILE   HG23   H  N N 220 
ILE   HD11   H  N N 221 
ILE   HD12   H  N N 222 
ILE   HD13   H  N N 223 
ILE   HXT    H  N N 224 
IMP   P      P  N N 225 
IMP   O1P    O  N N 226 
IMP   O2P    O  N N 227 
IMP   O3P    O  N N 228 
IMP   "O5'"  O  N N 229 
IMP   "C5'"  C  N N 230 
IMP   "C4'"  C  N R 231 
IMP   "O4'"  O  N N 232 
IMP   "C3'"  C  N S 233 
IMP   "O3'"  O  N N 234 
IMP   "C2'"  C  N R 235 
IMP   "O2'"  O  N N 236 
IMP   "C1'"  C  N R 237 
IMP   N9     N  Y N 238 
IMP   C8     C  Y N 239 
IMP   N7     N  Y N 240 
IMP   C5     C  Y N 241 
IMP   C6     C  N N 242 
IMP   O6     O  N N 243 
IMP   N1     N  N N 244 
IMP   C2     C  N N 245 
IMP   N3     N  N N 246 
IMP   C4     C  Y N 247 
IMP   HOP2   H  N N 248 
IMP   HOP3   H  N N 249 
IMP   "H5'1" H  N N 250 
IMP   "H5'2" H  N N 251 
IMP   "H4'"  H  N N 252 
IMP   "H3'"  H  N N 253 
IMP   "HO3'" H  N N 254 
IMP   "H2'"  H  N N 255 
IMP   "HO2'" H  N N 256 
IMP   "H1'"  H  N N 257 
IMP   H8     H  N N 258 
IMP   HN1    H  N N 259 
IMP   H2     H  N N 260 
LEU   N      N  N N 261 
LEU   CA     C  N S 262 
LEU   C      C  N N 263 
LEU   O      O  N N 264 
LEU   CB     C  N N 265 
LEU   CG     C  N N 266 
LEU   CD1    C  N N 267 
LEU   CD2    C  N N 268 
LEU   OXT    O  N N 269 
LEU   H      H  N N 270 
LEU   H2     H  N N 271 
LEU   HA     H  N N 272 
LEU   HB2    H  N N 273 
LEU   HB3    H  N N 274 
LEU   HG     H  N N 275 
LEU   HD11   H  N N 276 
LEU   HD12   H  N N 277 
LEU   HD13   H  N N 278 
LEU   HD21   H  N N 279 
LEU   HD22   H  N N 280 
LEU   HD23   H  N N 281 
LEU   HXT    H  N N 282 
LYS   N      N  N N 283 
LYS   CA     C  N S 284 
LYS   C      C  N N 285 
LYS   O      O  N N 286 
LYS   CB     C  N N 287 
LYS   CG     C  N N 288 
LYS   CD     C  N N 289 
LYS   CE     C  N N 290 
LYS   NZ     N  N N 291 
LYS   OXT    O  N N 292 
LYS   H      H  N N 293 
LYS   H2     H  N N 294 
LYS   HA     H  N N 295 
LYS   HB2    H  N N 296 
LYS   HB3    H  N N 297 
LYS   HG2    H  N N 298 
LYS   HG3    H  N N 299 
LYS   HD2    H  N N 300 
LYS   HD3    H  N N 301 
LYS   HE2    H  N N 302 
LYS   HE3    H  N N 303 
LYS   HZ1    H  N N 304 
LYS   HZ2    H  N N 305 
LYS   HZ3    H  N N 306 
LYS   HXT    H  N N 307 
MET   N      N  N N 308 
MET   CA     C  N S 309 
MET   C      C  N N 310 
MET   O      O  N N 311 
MET   CB     C  N N 312 
MET   CG     C  N N 313 
MET   SD     S  N N 314 
MET   CE     C  N N 315 
MET   OXT    O  N N 316 
MET   H      H  N N 317 
MET   H2     H  N N 318 
MET   HA     H  N N 319 
MET   HB2    H  N N 320 
MET   HB3    H  N N 321 
MET   HG2    H  N N 322 
MET   HG3    H  N N 323 
MET   HE1    H  N N 324 
MET   HE2    H  N N 325 
MET   HE3    H  N N 326 
MET   HXT    H  N N 327 
PHE   N      N  N N 328 
PHE   CA     C  N S 329 
PHE   C      C  N N 330 
PHE   O      O  N N 331 
PHE   CB     C  N N 332 
PHE   CG     C  Y N 333 
PHE   CD1    C  Y N 334 
PHE   CD2    C  Y N 335 
PHE   CE1    C  Y N 336 
PHE   CE2    C  Y N 337 
PHE   CZ     C  Y N 338 
PHE   OXT    O  N N 339 
PHE   H      H  N N 340 
PHE   H2     H  N N 341 
PHE   HA     H  N N 342 
PHE   HB2    H  N N 343 
PHE   HB3    H  N N 344 
PHE   HD1    H  N N 345 
PHE   HD2    H  N N 346 
PHE   HE1    H  N N 347 
PHE   HE2    H  N N 348 
PHE   HZ     H  N N 349 
PHE   HXT    H  N N 350 
PRO   N      N  N N 351 
PRO   CA     C  N S 352 
PRO   C      C  N N 353 
PRO   O      O  N N 354 
PRO   CB     C  N N 355 
PRO   CG     C  N N 356 
PRO   CD     C  N N 357 
PRO   OXT    O  N N 358 
PRO   H      H  N N 359 
PRO   HA     H  N N 360 
PRO   HB2    H  N N 361 
PRO   HB3    H  N N 362 
PRO   HG2    H  N N 363 
PRO   HG3    H  N N 364 
PRO   HD2    H  N N 365 
PRO   HD3    H  N N 366 
PRO   HXT    H  N N 367 
SER   N      N  N N 368 
SER   CA     C  N S 369 
SER   C      C  N N 370 
SER   O      O  N N 371 
SER   CB     C  N N 372 
SER   OG     O  N N 373 
SER   OXT    O  N N 374 
SER   H      H  N N 375 
SER   H2     H  N N 376 
SER   HA     H  N N 377 
SER   HB2    H  N N 378 
SER   HB3    H  N N 379 
SER   HG     H  N N 380 
SER   HXT    H  N N 381 
THR   N      N  N N 382 
THR   CA     C  N S 383 
THR   C      C  N N 384 
THR   O      O  N N 385 
THR   CB     C  N R 386 
THR   OG1    O  N N 387 
THR   CG2    C  N N 388 
THR   OXT    O  N N 389 
THR   H      H  N N 390 
THR   H2     H  N N 391 
THR   HA     H  N N 392 
THR   HB     H  N N 393 
THR   HG1    H  N N 394 
THR   HG21   H  N N 395 
THR   HG22   H  N N 396 
THR   HG23   H  N N 397 
THR   HXT    H  N N 398 
TRP   N      N  N N 399 
TRP   CA     C  N S 400 
TRP   C      C  N N 401 
TRP   O      O  N N 402 
TRP   CB     C  N N 403 
TRP   CG     C  Y N 404 
TRP   CD1    C  Y N 405 
TRP   CD2    C  Y N 406 
TRP   NE1    N  Y N 407 
TRP   CE2    C  Y N 408 
TRP   CE3    C  Y N 409 
TRP   CZ2    C  Y N 410 
TRP   CZ3    C  Y N 411 
TRP   CH2    C  Y N 412 
TRP   OXT    O  N N 413 
TRP   H      H  N N 414 
TRP   H2     H  N N 415 
TRP   HA     H  N N 416 
TRP   HB2    H  N N 417 
TRP   HB3    H  N N 418 
TRP   HD1    H  N N 419 
TRP   HE1    H  N N 420 
TRP   HE3    H  N N 421 
TRP   HZ2    H  N N 422 
TRP   HZ3    H  N N 423 
TRP   HH2    H  N N 424 
TRP   HXT    H  N N 425 
TYR   N      N  N N 426 
TYR   CA     C  N S 427 
TYR   C      C  N N 428 
TYR   O      O  N N 429 
TYR   CB     C  N N 430 
TYR   CG     C  Y N 431 
TYR   CD1    C  Y N 432 
TYR   CD2    C  Y N 433 
TYR   CE1    C  Y N 434 
TYR   CE2    C  Y N 435 
TYR   CZ     C  Y N 436 
TYR   OH     O  N N 437 
TYR   OXT    O  N N 438 
TYR   H      H  N N 439 
TYR   H2     H  N N 440 
TYR   HA     H  N N 441 
TYR   HB2    H  N N 442 
TYR   HB3    H  N N 443 
TYR   HD1    H  N N 444 
TYR   HD2    H  N N 445 
TYR   HE1    H  N N 446 
TYR   HE2    H  N N 447 
TYR   HH     H  N N 448 
TYR   HXT    H  N N 449 
VAL   N      N  N N 450 
VAL   CA     C  N S 451 
VAL   C      C  N N 452 
VAL   O      O  N N 453 
VAL   CB     C  N N 454 
VAL   CG1    C  N N 455 
VAL   CG2    C  N N 456 
VAL   OXT    O  N N 457 
VAL   H      H  N N 458 
VAL   H2     H  N N 459 
VAL   HA     H  N N 460 
VAL   HB     H  N N 461 
VAL   HG11   H  N N 462 
VAL   HG12   H  N N 463 
VAL   HG13   H  N N 464 
VAL   HG21   H  N N 465 
VAL   HG22   H  N N 466 
VAL   HG23   H  N N 467 
VAL   HXT    H  N N 468 
# 
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 
A1A3K CL15  C13    sing N N 1   
A1A3K C13   C12    doub Y N 2   
A1A3K C13   N14    sing Y N 3   
A1A3K C12   N10    sing Y N 4   
A1A3K N14   C9     doub Y N 5   
A1A3K N10   C9     sing Y N 6   
A1A3K C9    C5     sing N N 7   
A1A3K C5    C6     doub Y N 8   
A1A3K C5    C4     sing Y N 9   
A1A3K C6    N7     sing Y N 10  
A1A3K C4    C3     doub Y N 11  
A1A3K N7    C8     doub Y N 12  
A1A3K C19   C20    doub Y N 13  
A1A3K C19   C18    sing Y N 14  
A1A3K C20   C21    sing Y N 15  
A1A3K C18   C17    doub Y N 16  
A1A3K C3    C8     sing Y N 17  
A1A3K C3    C2     sing N N 18  
A1A3K N27   C23    sing Y N 19  
A1A3K N27   N26    sing Y N 20  
A1A3K C21   C23    sing N N 21  
A1A3K C21   C22    doub Y N 22  
A1A3K C17   C22    sing Y N 23  
A1A3K C17   O16    sing N N 24  
A1A3K C23   C24    doub Y N 25  
A1A3K N26   C25    doub Y N 26  
A1A3K O16   C2     sing N N 27  
A1A3K C2    C1     sing N N 28  
A1A3K C24   C25    sing Y N 29  
A1A3K C4    H33    sing N N 30  
A1A3K C6    H34    sing N N 31  
A1A3K C8    H35    sing N N 32  
A1A3K C12   H36    sing N N 33  
A1A3K C1    H30    sing N N 34  
A1A3K C1    H29    sing N N 35  
A1A3K C1    H31    sing N N 36  
A1A3K C18   H37    sing N N 37  
A1A3K C19   H38    sing N N 38  
A1A3K C2    H32    sing N N 39  
A1A3K C20   H39    sing N N 40  
A1A3K C22   H40    sing N N 41  
A1A3K C24   H41    sing N N 42  
A1A3K C25   H42    sing N N 43  
A1A3K N10   H11    sing N N 44  
A1A3K N27   H28    sing N N 45  
ALA   N     CA     sing N N 46  
ALA   N     H      sing N N 47  
ALA   N     H2     sing N N 48  
ALA   CA    C      sing N N 49  
ALA   CA    CB     sing N N 50  
ALA   CA    HA     sing N N 51  
ALA   C     O      doub N N 52  
ALA   C     OXT    sing N N 53  
ALA   CB    HB1    sing N N 54  
ALA   CB    HB2    sing N N 55  
ALA   CB    HB3    sing N N 56  
ALA   OXT   HXT    sing N N 57  
ARG   N     CA     sing N N 58  
ARG   N     H      sing N N 59  
ARG   N     H2     sing N N 60  
ARG   CA    C      sing N N 61  
ARG   CA    CB     sing N N 62  
ARG   CA    HA     sing N N 63  
ARG   C     O      doub N N 64  
ARG   C     OXT    sing N N 65  
ARG   CB    CG     sing N N 66  
ARG   CB    HB2    sing N N 67  
ARG   CB    HB3    sing N N 68  
ARG   CG    CD     sing N N 69  
ARG   CG    HG2    sing N N 70  
ARG   CG    HG3    sing N N 71  
ARG   CD    NE     sing N N 72  
ARG   CD    HD2    sing N N 73  
ARG   CD    HD3    sing N N 74  
ARG   NE    CZ     sing N N 75  
ARG   NE    HE     sing N N 76  
ARG   CZ    NH1    sing N N 77  
ARG   CZ    NH2    doub N N 78  
ARG   NH1   HH11   sing N N 79  
ARG   NH1   HH12   sing N N 80  
ARG   NH2   HH21   sing N N 81  
ARG   NH2   HH22   sing N N 82  
ARG   OXT   HXT    sing N N 83  
ASN   N     CA     sing N N 84  
ASN   N     H      sing N N 85  
ASN   N     H2     sing N N 86  
ASN   CA    C      sing N N 87  
ASN   CA    CB     sing N N 88  
ASN   CA    HA     sing N N 89  
ASN   C     O      doub N N 90  
ASN   C     OXT    sing N N 91  
ASN   CB    CG     sing N N 92  
ASN   CB    HB2    sing N N 93  
ASN   CB    HB3    sing N N 94  
ASN   CG    OD1    doub N N 95  
ASN   CG    ND2    sing N N 96  
ASN   ND2   HD21   sing N N 97  
ASN   ND2   HD22   sing N N 98  
ASN   OXT   HXT    sing N N 99  
ASP   N     CA     sing N N 100 
ASP   N     H      sing N N 101 
ASP   N     H2     sing N N 102 
ASP   CA    C      sing N N 103 
ASP   CA    CB     sing N N 104 
ASP   CA    HA     sing N N 105 
ASP   C     O      doub N N 106 
ASP   C     OXT    sing N N 107 
ASP   CB    CG     sing N N 108 
ASP   CB    HB2    sing N N 109 
ASP   CB    HB3    sing N N 110 
ASP   CG    OD1    doub N N 111 
ASP   CG    OD2    sing N N 112 
ASP   OD2   HD2    sing N N 113 
ASP   OXT   HXT    sing N N 114 
CYS   N     CA     sing N N 115 
CYS   N     H      sing N N 116 
CYS   N     H2     sing N N 117 
CYS   CA    C      sing N N 118 
CYS   CA    CB     sing N N 119 
CYS   CA    HA     sing N N 120 
CYS   C     O      doub N N 121 
CYS   C     OXT    sing N N 122 
CYS   CB    SG     sing N N 123 
CYS   CB    HB2    sing N N 124 
CYS   CB    HB3    sing N N 125 
CYS   SG    HG     sing N N 126 
CYS   OXT   HXT    sing N N 127 
GLN   N     CA     sing N N 128 
GLN   N     H      sing N N 129 
GLN   N     H2     sing N N 130 
GLN   CA    C      sing N N 131 
GLN   CA    CB     sing N N 132 
GLN   CA    HA     sing N N 133 
GLN   C     O      doub N N 134 
GLN   C     OXT    sing N N 135 
GLN   CB    CG     sing N N 136 
GLN   CB    HB2    sing N N 137 
GLN   CB    HB3    sing N N 138 
GLN   CG    CD     sing N N 139 
GLN   CG    HG2    sing N N 140 
GLN   CG    HG3    sing N N 141 
GLN   CD    OE1    doub N N 142 
GLN   CD    NE2    sing N N 143 
GLN   NE2   HE21   sing N N 144 
GLN   NE2   HE22   sing N N 145 
GLN   OXT   HXT    sing N N 146 
GLU   N     CA     sing N N 147 
GLU   N     H      sing N N 148 
GLU   N     H2     sing N N 149 
GLU   CA    C      sing N N 150 
GLU   CA    CB     sing N N 151 
GLU   CA    HA     sing N N 152 
GLU   C     O      doub N N 153 
GLU   C     OXT    sing N N 154 
GLU   CB    CG     sing N N 155 
GLU   CB    HB2    sing N N 156 
GLU   CB    HB3    sing N N 157 
GLU   CG    CD     sing N N 158 
GLU   CG    HG2    sing N N 159 
GLU   CG    HG3    sing N N 160 
GLU   CD    OE1    doub N N 161 
GLU   CD    OE2    sing N N 162 
GLU   OE2   HE2    sing N N 163 
GLU   OXT   HXT    sing N N 164 
GLY   N     CA     sing N N 165 
GLY   N     H      sing N N 166 
GLY   N     H2     sing N N 167 
GLY   CA    C      sing N N 168 
GLY   CA    HA2    sing N N 169 
GLY   CA    HA3    sing N N 170 
GLY   C     O      doub N N 171 
GLY   C     OXT    sing N N 172 
GLY   OXT   HXT    sing N N 173 
HIS   N     CA     sing N N 174 
HIS   N     H      sing N N 175 
HIS   N     H2     sing N N 176 
HIS   CA    C      sing N N 177 
HIS   CA    CB     sing N N 178 
HIS   CA    HA     sing N N 179 
HIS   C     O      doub N N 180 
HIS   C     OXT    sing N N 181 
HIS   CB    CG     sing N N 182 
HIS   CB    HB2    sing N N 183 
HIS   CB    HB3    sing N N 184 
HIS   CG    ND1    sing Y N 185 
HIS   CG    CD2    doub Y N 186 
HIS   ND1   CE1    doub Y N 187 
HIS   ND1   HD1    sing N N 188 
HIS   CD2   NE2    sing Y N 189 
HIS   CD2   HD2    sing N N 190 
HIS   CE1   NE2    sing Y N 191 
HIS   CE1   HE1    sing N N 192 
HIS   NE2   HE2    sing N N 193 
HIS   OXT   HXT    sing N N 194 
HOH   O     H1     sing N N 195 
HOH   O     H2     sing N N 196 
ILE   N     CA     sing N N 197 
ILE   N     H      sing N N 198 
ILE   N     H2     sing N N 199 
ILE   CA    C      sing N N 200 
ILE   CA    CB     sing N N 201 
ILE   CA    HA     sing N N 202 
ILE   C     O      doub N N 203 
ILE   C     OXT    sing N N 204 
ILE   CB    CG1    sing N N 205 
ILE   CB    CG2    sing N N 206 
ILE   CB    HB     sing N N 207 
ILE   CG1   CD1    sing N N 208 
ILE   CG1   HG12   sing N N 209 
ILE   CG1   HG13   sing N N 210 
ILE   CG2   HG21   sing N N 211 
ILE   CG2   HG22   sing N N 212 
ILE   CG2   HG23   sing N N 213 
ILE   CD1   HD11   sing N N 214 
ILE   CD1   HD12   sing N N 215 
ILE   CD1   HD13   sing N N 216 
ILE   OXT   HXT    sing N N 217 
IMP   P     O1P    doub N N 218 
IMP   P     O2P    sing N N 219 
IMP   P     O3P    sing N N 220 
IMP   P     "O5'"  sing N N 221 
IMP   O2P   HOP2   sing N N 222 
IMP   O3P   HOP3   sing N N 223 
IMP   "O5'" "C5'"  sing N N 224 
IMP   "C5'" "C4'"  sing N N 225 
IMP   "C5'" "H5'1" sing N N 226 
IMP   "C5'" "H5'2" sing N N 227 
IMP   "C4'" "O4'"  sing N N 228 
IMP   "C4'" "C3'"  sing N N 229 
IMP   "C4'" "H4'"  sing N N 230 
IMP   "O4'" "C1'"  sing N N 231 
IMP   "C3'" "O3'"  sing N N 232 
IMP   "C3'" "C2'"  sing N N 233 
IMP   "C3'" "H3'"  sing N N 234 
IMP   "O3'" "HO3'" sing N N 235 
IMP   "C2'" "O2'"  sing N N 236 
IMP   "C2'" "C1'"  sing N N 237 
IMP   "C2'" "H2'"  sing N N 238 
IMP   "O2'" "HO2'" sing N N 239 
IMP   "C1'" N9     sing N N 240 
IMP   "C1'" "H1'"  sing N N 241 
IMP   N9    C8     sing Y N 242 
IMP   N9    C4     sing Y N 243 
IMP   C8    N7     doub Y N 244 
IMP   C8    H8     sing N N 245 
IMP   N7    C5     sing Y N 246 
IMP   C5    C6     sing N N 247 
IMP   C5    C4     doub Y N 248 
IMP   C6    O6     doub N N 249 
IMP   C6    N1     sing N N 250 
IMP   N1    C2     sing N N 251 
IMP   N1    HN1    sing N N 252 
IMP   C2    N3     doub N N 253 
IMP   C2    H2     sing N N 254 
IMP   N3    C4     sing N N 255 
LEU   N     CA     sing N N 256 
LEU   N     H      sing N N 257 
LEU   N     H2     sing N N 258 
LEU   CA    C      sing N N 259 
LEU   CA    CB     sing N N 260 
LEU   CA    HA     sing N N 261 
LEU   C     O      doub N N 262 
LEU   C     OXT    sing N N 263 
LEU   CB    CG     sing N N 264 
LEU   CB    HB2    sing N N 265 
LEU   CB    HB3    sing N N 266 
LEU   CG    CD1    sing N N 267 
LEU   CG    CD2    sing N N 268 
LEU   CG    HG     sing N N 269 
LEU   CD1   HD11   sing N N 270 
LEU   CD1   HD12   sing N N 271 
LEU   CD1   HD13   sing N N 272 
LEU   CD2   HD21   sing N N 273 
LEU   CD2   HD22   sing N N 274 
LEU   CD2   HD23   sing N N 275 
LEU   OXT   HXT    sing N N 276 
LYS   N     CA     sing N N 277 
LYS   N     H      sing N N 278 
LYS   N     H2     sing N N 279 
LYS   CA    C      sing N N 280 
LYS   CA    CB     sing N N 281 
LYS   CA    HA     sing N N 282 
LYS   C     O      doub N N 283 
LYS   C     OXT    sing N N 284 
LYS   CB    CG     sing N N 285 
LYS   CB    HB2    sing N N 286 
LYS   CB    HB3    sing N N 287 
LYS   CG    CD     sing N N 288 
LYS   CG    HG2    sing N N 289 
LYS   CG    HG3    sing N N 290 
LYS   CD    CE     sing N N 291 
LYS   CD    HD2    sing N N 292 
LYS   CD    HD3    sing N N 293 
LYS   CE    NZ     sing N N 294 
LYS   CE    HE2    sing N N 295 
LYS   CE    HE3    sing N N 296 
LYS   NZ    HZ1    sing N N 297 
LYS   NZ    HZ2    sing N N 298 
LYS   NZ    HZ3    sing N N 299 
LYS   OXT   HXT    sing N N 300 
MET   N     CA     sing N N 301 
MET   N     H      sing N N 302 
MET   N     H2     sing N N 303 
MET   CA    C      sing N N 304 
MET   CA    CB     sing N N 305 
MET   CA    HA     sing N N 306 
MET   C     O      doub N N 307 
MET   C     OXT    sing N N 308 
MET   CB    CG     sing N N 309 
MET   CB    HB2    sing N N 310 
MET   CB    HB3    sing N N 311 
MET   CG    SD     sing N N 312 
MET   CG    HG2    sing N N 313 
MET   CG    HG3    sing N N 314 
MET   SD    CE     sing N N 315 
MET   CE    HE1    sing N N 316 
MET   CE    HE2    sing N N 317 
MET   CE    HE3    sing N N 318 
MET   OXT   HXT    sing N N 319 
PHE   N     CA     sing N N 320 
PHE   N     H      sing N N 321 
PHE   N     H2     sing N N 322 
PHE   CA    C      sing N N 323 
PHE   CA    CB     sing N N 324 
PHE   CA    HA     sing N N 325 
PHE   C     O      doub N N 326 
PHE   C     OXT    sing N N 327 
PHE   CB    CG     sing N N 328 
PHE   CB    HB2    sing N N 329 
PHE   CB    HB3    sing N N 330 
PHE   CG    CD1    doub Y N 331 
PHE   CG    CD2    sing Y N 332 
PHE   CD1   CE1    sing Y N 333 
PHE   CD1   HD1    sing N N 334 
PHE   CD2   CE2    doub Y N 335 
PHE   CD2   HD2    sing N N 336 
PHE   CE1   CZ     doub Y N 337 
PHE   CE1   HE1    sing N N 338 
PHE   CE2   CZ     sing Y N 339 
PHE   CE2   HE2    sing N N 340 
PHE   CZ    HZ     sing N N 341 
PHE   OXT   HXT    sing N N 342 
PRO   N     CA     sing N N 343 
PRO   N     CD     sing N N 344 
PRO   N     H      sing N N 345 
PRO   CA    C      sing N N 346 
PRO   CA    CB     sing N N 347 
PRO   CA    HA     sing N N 348 
PRO   C     O      doub N N 349 
PRO   C     OXT    sing N N 350 
PRO   CB    CG     sing N N 351 
PRO   CB    HB2    sing N N 352 
PRO   CB    HB3    sing N N 353 
PRO   CG    CD     sing N N 354 
PRO   CG    HG2    sing N N 355 
PRO   CG    HG3    sing N N 356 
PRO   CD    HD2    sing N N 357 
PRO   CD    HD3    sing N N 358 
PRO   OXT   HXT    sing N N 359 
SER   N     CA     sing N N 360 
SER   N     H      sing N N 361 
SER   N     H2     sing N N 362 
SER   CA    C      sing N N 363 
SER   CA    CB     sing N N 364 
SER   CA    HA     sing N N 365 
SER   C     O      doub N N 366 
SER   C     OXT    sing N N 367 
SER   CB    OG     sing N N 368 
SER   CB    HB2    sing N N 369 
SER   CB    HB3    sing N N 370 
SER   OG    HG     sing N N 371 
SER   OXT   HXT    sing N N 372 
THR   N     CA     sing N N 373 
THR   N     H      sing N N 374 
THR   N     H2     sing N N 375 
THR   CA    C      sing N N 376 
THR   CA    CB     sing N N 377 
THR   CA    HA     sing N N 378 
THR   C     O      doub N N 379 
THR   C     OXT    sing N N 380 
THR   CB    OG1    sing N N 381 
THR   CB    CG2    sing N N 382 
THR   CB    HB     sing N N 383 
THR   OG1   HG1    sing N N 384 
THR   CG2   HG21   sing N N 385 
THR   CG2   HG22   sing N N 386 
THR   CG2   HG23   sing N N 387 
THR   OXT   HXT    sing N N 388 
TRP   N     CA     sing N N 389 
TRP   N     H      sing N N 390 
TRP   N     H2     sing N N 391 
TRP   CA    C      sing N N 392 
TRP   CA    CB     sing N N 393 
TRP   CA    HA     sing N N 394 
TRP   C     O      doub N N 395 
TRP   C     OXT    sing N N 396 
TRP   CB    CG     sing N N 397 
TRP   CB    HB2    sing N N 398 
TRP   CB    HB3    sing N N 399 
TRP   CG    CD1    doub Y N 400 
TRP   CG    CD2    sing Y N 401 
TRP   CD1   NE1    sing Y N 402 
TRP   CD1   HD1    sing N N 403 
TRP   CD2   CE2    doub Y N 404 
TRP   CD2   CE3    sing Y N 405 
TRP   NE1   CE2    sing Y N 406 
TRP   NE1   HE1    sing N N 407 
TRP   CE2   CZ2    sing Y N 408 
TRP   CE3   CZ3    doub Y N 409 
TRP   CE3   HE3    sing N N 410 
TRP   CZ2   CH2    doub Y N 411 
TRP   CZ2   HZ2    sing N N 412 
TRP   CZ3   CH2    sing Y N 413 
TRP   CZ3   HZ3    sing N N 414 
TRP   CH2   HH2    sing N N 415 
TRP   OXT   HXT    sing N N 416 
TYR   N     CA     sing N N 417 
TYR   N     H      sing N N 418 
TYR   N     H2     sing N N 419 
TYR   CA    C      sing N N 420 
TYR   CA    CB     sing N N 421 
TYR   CA    HA     sing N N 422 
TYR   C     O      doub N N 423 
TYR   C     OXT    sing N N 424 
TYR   CB    CG     sing N N 425 
TYR   CB    HB2    sing N N 426 
TYR   CB    HB3    sing N N 427 
TYR   CG    CD1    doub Y N 428 
TYR   CG    CD2    sing Y N 429 
TYR   CD1   CE1    sing Y N 430 
TYR   CD1   HD1    sing N N 431 
TYR   CD2   CE2    doub Y N 432 
TYR   CD2   HD2    sing N N 433 
TYR   CE1   CZ     doub Y N 434 
TYR   CE1   HE1    sing N N 435 
TYR   CE2   CZ     sing Y N 436 
TYR   CE2   HE2    sing N N 437 
TYR   CZ    OH     sing N N 438 
TYR   OH    HH     sing N N 439 
TYR   OXT   HXT    sing N N 440 
VAL   N     CA     sing N N 441 
VAL   N     H      sing N N 442 
VAL   N     H2     sing N N 443 
VAL   CA    C      sing N N 444 
VAL   CA    CB     sing N N 445 
VAL   CA    HA     sing N N 446 
VAL   C     O      doub N N 447 
VAL   C     OXT    sing N N 448 
VAL   CB    CG1    sing N N 449 
VAL   CB    CG2    sing N N 450 
VAL   CB    HB     sing N N 451 
VAL   CG1   HG11   sing N N 452 
VAL   CG1   HG12   sing N N 453 
VAL   CG1   HG13   sing N N 454 
VAL   CG2   HG21   sing N N 455 
VAL   CG2   HG22   sing N N 456 
VAL   CG2   HG23   sing N N 457 
VAL   OXT   HXT    sing N N 458 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4IX2 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DC9 
_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]   0.011142 
_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]   0.011142 
_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]   0.011633 
_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  
CL 
H  
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . THR   A 1 42  ? -16.844 6.072   -28.384 1.00 66.06 ?  27   THR   A N     1 
ATOM   2    C  CA    . THR   A 1 42  ? -15.487 6.115   -27.850 1.00 66.98 ?  27   THR   A CA    1 
ATOM   3    C  C     . THR   A 1 42  ? -15.483 5.756   -26.361 1.00 62.67 ?  27   THR   A C     1 
ATOM   4    O  O     . THR   A 1 42  ? -16.329 6.223   -25.598 1.00 55.52 ?  27   THR   A O     1 
ATOM   5    C  CB    . THR   A 1 42  ? -14.847 7.503   -28.058 1.00 62.95 ?  27   THR   A CB    1 
ATOM   6    O  OG1   . THR   A 1 42  ? -13.440 7.431   -27.792 1.00 72.19 ?  27   THR   A OG1   1 
ATOM   7    C  CG2   . THR   A 1 42  ? -15.489 8.536   -27.141 1.00 66.10 ?  27   THR   A CG2   1 
ATOM   8    N  N     . ASP   A 1 43  ? -14.525 4.922   -25.959 1.00 58.42 ?  28   ASP   A N     1 
ATOM   9    C  CA    . ASP   A 1 43  ? -14.502 4.405   -24.599 1.00 53.02 ?  28   ASP   A CA    1 
ATOM   10   C  C     . ASP   A 1 43  ? -14.084 5.491   -23.607 1.00 42.40 ?  28   ASP   A C     1 
ATOM   11   O  O     . ASP   A 1 43  ? -13.359 6.426   -23.961 1.00 43.38 ?  28   ASP   A O     1 
ATOM   12   C  CB    . ASP   A 1 43  ? -13.546 3.221   -24.494 1.00 53.99 ?  28   ASP   A CB    1 
ATOM   13   C  CG    . ASP   A 1 43  ? -13.945 2.070   -25.396 1.00 61.73 ?  28   ASP   A CG    1 
ATOM   14   O  OD1   . ASP   A 1 43  ? -15.059 2.116   -25.958 1.00 54.83 ?  28   ASP   A OD1   1 
ATOM   15   O  OD2   . ASP   A 1 43  ? -13.142 1.124   -25.546 1.00 68.31 -1 28   ASP   A OD2   1 
ATOM   16   N  N     . PRO   A 1 44  ? -14.530 5.390   -22.358 1.00 41.71 ?  29   PRO   A N     1 
ATOM   17   C  CA    . PRO   A 1 44  ? -14.093 6.351   -21.343 1.00 35.77 ?  29   PRO   A CA    1 
ATOM   18   C  C     . PRO   A 1 44  ? -12.635 6.137   -20.976 1.00 34.99 ?  29   PRO   A C     1 
ATOM   19   O  O     . PRO   A 1 44  ? -12.063 5.060   -21.164 1.00 31.74 ?  29   PRO   A O     1 
ATOM   20   C  CB    . PRO   A 1 44  ? -15.006 6.047   -20.152 1.00 31.74 ?  29   PRO   A CB    1 
ATOM   21   C  CG    . PRO   A 1 44  ? -15.323 4.591   -20.305 1.00 37.89 ?  29   PRO   A CG    1 
ATOM   22   C  CD    . PRO   A 1 44  ? -15.436 4.370   -21.799 1.00 39.37 ?  29   PRO   A CD    1 
ATOM   23   N  N     . VAL   A 1 45  ? -12.032 7.193   -20.441 1.00 26.27 ?  30   VAL   A N     1 
ATOM   24   C  CA    . VAL   A 1 45  ? -10.740 7.028   -19.766 1.00 27.68 ?  30   VAL   A CA    1 
ATOM   25   C  C     . VAL   A 1 45  ? -10.905 6.007   -18.639 1.00 24.37 ?  30   VAL   A C     1 
ATOM   26   O  O     . VAL   A 1 45  ? -11.918 6.052   -17.916 1.00 25.20 ?  30   VAL   A O     1 
ATOM   27   C  CB    . VAL   A 1 45  ? -10.250 8.382   -19.221 1.00 26.47 ?  30   VAL   A CB    1 
ATOM   28   C  CG1   . VAL   A 1 45  ? -8.908  8.234   -18.510 1.00 27.03 ?  30   VAL   A CG1   1 
ATOM   29   C  CG2   . VAL   A 1 45  ? -10.160 9.414   -20.347 1.00 26.73 ?  30   VAL   A CG2   1 
ATOM   30   N  N     . PRO   A 1 46  ? -9.966  5.081   -18.425 1.00 27.78 ?  31   PRO   A N     1 
ATOM   31   C  CA    . PRO   A 1 46  ? -10.201 4.026   -17.420 1.00 27.40 ?  31   PRO   A CA    1 
ATOM   32   C  C     . PRO   A 1 46  ? -10.383 4.537   -15.990 1.00 27.37 ?  31   PRO   A C     1 
ATOM   33   O  O     . PRO   A 1 46  ? -11.042 3.854   -15.196 1.00 28.11 ?  31   PRO   A O     1 
ATOM   34   C  CB    . PRO   A 1 46  ? -8.964  3.121   -17.551 1.00 28.94 ?  31   PRO   A CB    1 
ATOM   35   C  CG    . PRO   A 1 46  ? -7.967  3.898   -18.324 1.00 44.37 ?  31   PRO   A CG    1 
ATOM   36   C  CD    . PRO   A 1 46  ? -8.735  4.848   -19.196 1.00 30.94 ?  31   PRO   A CD    1 
ATOM   37   N  N     . THR   A 1 47  ? -9.875  5.724   -15.638 1.00 21.37 ?  32   THR   A N     1 
ATOM   38   C  CA    . THR   A 1 47  ? -10.103 6.297   -14.307 1.00 20.45 ?  32   THR   A CA    1 
ATOM   39   C  C     . THR   A 1 47  ? -11.275 7.283   -14.246 1.00 20.27 ?  32   THR   A C     1 
ATOM   40   O  O     . THR   A 1 47  ? -11.528 7.856   -13.175 1.00 20.03 ?  32   THR   A O     1 
ATOM   41   C  CB    . THR   A 1 47  ? -8.834  7.006   -13.793 1.00 19.54 ?  32   THR   A CB    1 
ATOM   42   O  OG1   . THR   A 1 47  ? -8.322  7.880   -14.806 1.00 20.28 ?  32   THR   A OG1   1 
ATOM   43   C  CG2   . THR   A 1 47  ? -7.741  5.996   -13.405 1.00 22.68 ?  32   THR   A CG2   1 
ATOM   44   N  N     . GLY   A 1 48  ? -11.986 7.509   -15.353 1.00 18.27 ?  33   GLY   A N     1 
ATOM   45   C  CA    . GLY   A 1 48  ? -13.220 8.285   -15.337 1.00 20.21 ?  33   GLY   A CA    1 
ATOM   46   C  C     . GLY   A 1 48  ? -13.286 9.479   -16.272 1.00 21.21 ?  33   GLY   A C     1 
ATOM   47   O  O     . GLY   A 1 48  ? -12.290 10.195  -16.475 1.00 19.82 ?  33   GLY   A O     1 
ATOM   48   N  N     . GLY   A 1 49  ? -14.474 9.729   -16.826 1.00 18.40 ?  34   GLY   A N     1 
ATOM   49   C  CA    . GLY   A 1 49  ? -14.656 10.828  -17.760 1.00 17.75 ?  34   GLY   A CA    1 
ATOM   50   C  C     . GLY   A 1 49  ? -14.093 10.517  -19.137 1.00 21.32 ?  34   GLY   A C     1 
ATOM   51   O  O     . GLY   A 1 49  ? -13.600 9.427   -19.410 1.00 22.74 ?  34   GLY   A O     1 
ATOM   52   N  N     . ASP   A 1 50  ? -14.156 11.522  -20.023 1.00 24.70 ?  35   ASP   A N     1 
ATOM   53   C  CA    . ASP   A 1 50  ? -13.714 11.375  -21.408 1.00 24.69 ?  35   ASP   A CA    1 
ATOM   54   C  C     . ASP   A 1 50  ? -12.463 12.195  -21.740 1.00 31.56 ?  35   ASP   A C     1 
ATOM   55   O  O     . ASP   A 1 50  ? -12.058 12.227  -22.909 1.00 29.43 ?  35   ASP   A O     1 
ATOM   56   C  CB    . ASP   A 1 50  ? -14.847 11.751  -22.376 1.00 28.08 ?  35   ASP   A CB    1 
ATOM   57   C  CG    . ASP   A 1 50  ? -16.034 10.783  -22.317 1.00 26.82 ?  35   ASP   A CG    1 
ATOM   58   O  OD1   . ASP   A 1 50  ? -15.822 9.557   -22.206 1.00 29.36 ?  35   ASP   A OD1   1 
ATOM   59   O  OD2   . ASP   A 1 50  ? -17.178 11.266  -22.392 1.00 29.89 -1 35   ASP   A OD2   1 
ATOM   60   N  N     . ASP   A 1 51  ? -11.825 12.834  -20.743 1.00 23.42 ?  36   ASP   A N     1 
ATOM   61   C  CA    . ASP   A 1 51  ? -10.665 13.700  -20.969 1.00 21.90 ?  36   ASP   A CA    1 
ATOM   62   C  C     . ASP   A 1 51  ? -9.378  13.009  -20.515 1.00 24.50 ?  36   ASP   A C     1 
ATOM   63   O  O     . ASP   A 1 51  ? -9.151  12.878  -19.297 1.00 22.94 ?  36   ASP   A O     1 
ATOM   64   C  CB    . ASP   A 1 51  ? -10.865 15.026  -20.217 1.00 21.29 ?  36   ASP   A CB    1 
ATOM   65   C  CG    . ASP   A 1 51  ? -9.688  15.994  -20.358 1.00 24.63 ?  36   ASP   A CG    1 
ATOM   66   O  OD1   . ASP   A 1 51  ? -8.678  15.677  -21.036 1.00 24.44 ?  36   ASP   A OD1   1 
ATOM   67   O  OD2   . ASP   A 1 51  ? -9.797  17.089  -19.765 1.00 25.96 -1 36   ASP   A OD2   1 
ATOM   68   N  N     . PRO   A 1 52  ? -8.495  12.582  -21.427 1.00 25.86 ?  37   PRO   A N     1 
ATOM   69   C  CA    . PRO   A 1 52  ? -7.281  11.861  -21.005 1.00 23.25 ?  37   PRO   A CA    1 
ATOM   70   C  C     . PRO   A 1 52  ? -6.222  12.725  -20.332 1.00 23.92 ?  37   PRO   A C     1 
ATOM   71   O  O     . PRO   A 1 52  ? -5.204  12.173  -19.882 1.00 28.25 ?  37   PRO   A O     1 
ATOM   72   C  CB    . PRO   A 1 52  ? -6.744  11.283  -22.324 1.00 32.95 ?  37   PRO   A CB    1 
ATOM   73   C  CG    . PRO   A 1 52  ? -7.226  12.230  -23.355 1.00 30.52 ?  37   PRO   A CG    1 
ATOM   74   C  CD    . PRO   A 1 52  ? -8.586  12.692  -22.895 1.00 28.37 ?  37   PRO   A CD    1 
ATOM   75   N  N     . HIS   A 1 53  ? -6.421  14.040  -20.233 1.00 23.41 ?  38   HIS   A N     1 
ATOM   76   C  CA    . HIS   A 1 53  ? -5.466  14.923  -19.573 1.00 23.36 ?  38   HIS   A CA    1 
ATOM   77   C  C     . HIS   A 1 53  ? -5.975  15.481  -18.247 1.00 22.12 ?  38   HIS   A C     1 
ATOM   78   O  O     . HIS   A 1 53  ? -5.253  16.246  -17.603 1.00 21.72 ?  38   HIS   A O     1 
ATOM   79   C  CB    . HIS   A 1 53  ? -5.059  16.055  -20.532 1.00 26.57 ?  38   HIS   A CB    1 
ATOM   80   C  CG    . HIS   A 1 53  ? -4.495  15.551  -21.827 1.00 30.76 ?  38   HIS   A CG    1 
ATOM   81   N  ND1   . HIS   A 1 53  ? -5.184  15.617  -23.020 1.00 41.75 ?  38   HIS   A ND1   1 
ATOM   82   C  CD2   . HIS   A 1 53  ? -3.327  14.923  -22.103 1.00 41.40 ?  38   HIS   A CD2   1 
ATOM   83   C  CE1   . HIS   A 1 53  ? -4.452  15.079  -23.980 1.00 43.57 ?  38   HIS   A CE1   1 
ATOM   84   N  NE2   . HIS   A 1 53  ? -3.324  14.644  -23.450 1.00 38.07 ?  38   HIS   A NE2   1 
ATOM   85   N  N     . LYS   A 1 54  ? -7.174  15.076  -17.795 1.00 20.31 ?  39   LYS   A N     1 
ATOM   86   C  CA    . LYS   A 1 54  ? -7.691  15.536  -16.504 1.00 18.68 ?  39   LYS   A CA    1 
ATOM   87   C  C     . LYS   A 1 54  ? -6.798  15.078  -15.346 1.00 18.22 ?  39   LYS   A C     1 
ATOM   88   O  O     . LYS   A 1 54  ? -6.479  15.867  -14.436 1.00 19.21 ?  39   LYS   A O     1 
ATOM   89   C  CB    . LYS   A 1 54  ? -9.138  15.034  -16.328 1.00 18.21 ?  39   LYS   A CB    1 
ATOM   90   C  CG    . LYS   A 1 54  ? -9.843  15.563  -15.081 1.00 17.39 ?  39   LYS   A CG    1 
ATOM   91   C  CD    . LYS   A 1 54  ? -10.012 17.091  -15.126 1.00 19.54 ?  39   LYS   A CD    1 
ATOM   92   C  CE    . LYS   A 1 54  ? -10.989 17.552  -14.070 1.00 18.35 ?  39   LYS   A CE    1 
ATOM   93   N  NZ    . LYS   A 1 54  ? -11.135 19.055  -14.138 1.00 17.61 ?  39   LYS   A NZ    1 
ATOM   94   N  N     . VAL   A 1 55  ? -6.420  13.798  -15.347 1.00 18.96 ?  40   VAL   A N     1 
ATOM   95   C  CA    . VAL   A 1 55  ? -5.367  13.253  -14.490 1.00 17.72 ?  40   VAL   A CA    1 
ATOM   96   C  C     . VAL   A 1 55  ? -4.110  13.274  -15.356 1.00 22.02 ?  40   VAL   A C     1 
ATOM   97   O  O     . VAL   A 1 55  ? -3.923  12.405  -16.211 1.00 22.56 ?  40   VAL   A O     1 
ATOM   98   C  CB    . VAL   A 1 55  ? -5.717  11.843  -13.995 1.00 19.45 ?  40   VAL   A CB    1 
ATOM   99   C  CG1   . VAL   A 1 55  ? -4.622  11.296  -13.058 1.00 22.98 ?  40   VAL   A CG1   1 
ATOM   100  C  CG2   . VAL   A 1 55  ? -7.079  11.846  -13.292 1.00 20.66 ?  40   VAL   A CG2   1 
ATOM   101  N  N     . ALA   A 1 56  ? -3.256  14.282  -15.155 1.00 19.17 ?  41   ALA   A N     1 
ATOM   102  C  CA    . ALA   A 1 56  ? -2.252  14.654  -16.148 1.00 21.54 ?  41   ALA   A CA    1 
ATOM   103  C  C     . ALA   A 1 56  ? -0.947  13.870  -16.052 1.00 22.60 ?  41   ALA   A C     1 
ATOM   104  O  O     . ALA   A 1 56  ? -0.235  13.758  -17.063 1.00 25.04 ?  41   ALA   A O     1 
ATOM   105  C  CB    . ALA   A 1 56  ? -1.922  16.146  -16.026 1.00 21.56 ?  41   ALA   A CB    1 
ATOM   106  N  N     A MET   A 1 57  ? -0.628  13.330  -14.872 0.50 20.24 ?  42   MET   A N     1 
ATOM   107  N  N     B MET   A 1 57  ? -0.601  13.346  -14.876 0.50 20.26 ?  42   MET   A N     1 
ATOM   108  C  CA    A MET   A 1 57  ? 0.680   12.742  -14.587 0.50 20.25 ?  42   MET   A CA    1 
ATOM   109  C  CA    B MET   A 1 57  ? 0.675   12.660  -14.681 0.50 20.23 ?  42   MET   A CA    1 
ATOM   110  C  C     A MET   A 1 57  ? 0.540   11.716  -13.469 0.50 20.20 ?  42   MET   A C     1 
ATOM   111  C  C     B MET   A 1 57  ? 0.577   11.755  -13.462 0.50 20.20 ?  42   MET   A C     1 
ATOM   112  O  O     A MET   A 1 57  ? -0.447  11.717  -12.728 0.50 19.83 ?  42   MET   A O     1 
ATOM   113  O  O     B MET   A 1 57  ? -0.342  11.884  -12.647 0.50 19.62 ?  42   MET   A O     1 
ATOM   114  C  CB    A MET   A 1 57  ? 1.707   13.810  -14.161 0.50 24.97 ?  42   MET   A CB    1 
ATOM   115  C  CB    B MET   A 1 57  ? 1.842   13.647  -14.499 0.50 24.76 ?  42   MET   A CB    1 
ATOM   116  C  CG    A MET   A 1 57  ? 1.831   15.016  -15.090 0.50 23.48 ?  42   MET   A CG    1 
ATOM   117  C  CG    B MET   A 1 57  ? 2.103   14.586  -15.674 0.50 28.48 ?  42   MET   A CG    1 
ATOM   118  S  SD    A MET   A 1 57  ? 2.997   14.726  -16.442 0.50 30.15 ?  42   MET   A SD    1 
ATOM   119  S  SD    B MET   A 1 57  ? 3.529   15.666  -15.403 0.50 32.75 ?  42   MET   A SD    1 
ATOM   120  C  CE    A MET   A 1 57  ? 4.524   14.592  -15.514 0.50 21.01 ?  42   MET   A CE    1 
ATOM   121  C  CE    B MET   A 1 57  ? 4.722   14.448  -14.879 0.50 21.02 ?  42   MET   A CE    1 
ATOM   122  N  N     . LEU   A 1 58  ? 1.549   10.835  -13.348 1.00 20.18 ?  43   LEU   A N     1 
ATOM   123  C  CA    . LEU   A 1 58  ? 1.716   9.955   -12.182 1.00 19.02 ?  43   LEU   A CA    1 
ATOM   124  C  C     . LEU   A 1 58  ? 2.931   10.456  -11.395 1.00 22.07 ?  43   LEU   A C     1 
ATOM   125  O  O     . LEU   A 1 58  ? 4.066   10.380  -11.889 1.00 21.30 ?  43   LEU   A O     1 
ATOM   126  C  CB    . LEU   A 1 58  ? 1.898   8.491   -12.598 1.00 24.15 ?  43   LEU   A CB    1 
ATOM   127  C  CG    . LEU   A 1 58  ? 2.160   7.494   -11.462 1.00 25.76 ?  43   LEU   A CG    1 
ATOM   128  C  CD1   . LEU   A 1 58  ? 0.961   7.381   -10.519 1.00 25.13 ?  43   LEU   A CD1   1 
ATOM   129  C  CD2   . LEU   A 1 58  ? 2.546   6.119   -12.010 1.00 32.06 ?  43   LEU   A CD2   1 
ATOM   130  N  N     . GLY   A 1 59  ? 2.704   10.973  -10.186 1.00 16.87 ?  44   GLY   A N     1 
ATOM   131  C  CA    . GLY   A 1 59  ? 3.772   11.603  -9.408  1.00 17.63 ?  44   GLY   A CA    1 
ATOM   132  C  C     . GLY   A 1 59  ? 4.503   10.654  -8.463  1.00 17.99 ?  44   GLY   A C     1 
ATOM   133  O  O     . GLY   A 1 59  ? 3.883   10.015  -7.602  1.00 19.68 ?  44   GLY   A O     1 
ATOM   134  N  N     . LEU   A 1 60  ? 5.838   10.615  -8.592  1.00 15.64 ?  45   LEU   A N     1 
ATOM   135  C  CA    . LEU   A 1 60  ? 6.714   9.837   -7.720  1.00 17.13 ?  45   LEU   A CA    1 
ATOM   136  C  C     . LEU   A 1 60  ? 7.343   10.701  -6.622  1.00 15.52 ?  45   LEU   A C     1 
ATOM   137  O  O     . LEU   A 1 60  ? 7.808   11.822  -6.885  1.00 16.26 ?  45   LEU   A O     1 
ATOM   138  C  CB    . LEU   A 1 60  ? 7.843   9.186   -8.542  1.00 16.39 ?  45   LEU   A CB    1 
ATOM   139  C  CG    . LEU   A 1 60  ? 7.420   8.377   -9.777  1.00 17.74 ?  45   LEU   A CG    1 
ATOM   140  C  CD1   . LEU   A 1 60  ? 8.649   7.796   -10.497 1.00 18.29 ?  45   LEU   A CD1   1 
ATOM   141  C  CD2   . LEU   A 1 60  ? 6.464   7.278   -9.382  1.00 18.04 ?  45   LEU   A CD2   1 
ATOM   142  N  N     . THR   A 1 61  ? 7.396   10.160  -5.394  1.00 16.13 ?  46   THR   A N     1 
ATOM   143  C  CA    . THR   A 1 61  ? 8.151   10.765  -4.296  1.00 15.67 ?  46   THR   A CA    1 
ATOM   144  C  C     . THR   A 1 61  ? 9.464   9.993   -4.042  1.00 18.90 ?  46   THR   A C     1 
ATOM   145  O  O     . THR   A 1 61  ? 9.777   9.020   -4.735  1.00 17.19 ?  46   THR   A O     1 
ATOM   146  C  CB    . THR   A 1 61  ? 7.286   10.843  -3.038  1.00 20.62 ?  46   THR   A CB    1 
ATOM   147  O  OG1   . THR   A 1 61  ? 7.942   11.667  -2.060  1.00 27.56 ?  46   THR   A OG1   1 
ATOM   148  C  CG2   . THR   A 1 61  ? 7.005   9.433   -2.482  1.00 21.35 ?  46   THR   A CG2   1 
ATOM   149  N  N     . PHE   A 1 62  ? 10.259  10.450  -3.054  1.00 16.55 ?  47   PHE   A N     1 
ATOM   150  C  CA    . PHE   A 1 62  ? 11.555  9.811   -2.788  1.00 16.91 ?  47   PHE   A CA    1 
ATOM   151  C  C     . PHE   A 1 62  ? 11.400  8.319   -2.485  1.00 17.22 ?  47   PHE   A C     1 
ATOM   152  O  O     . PHE   A 1 62  ? 12.187  7.502   -2.983  1.00 17.94 ?  47   PHE   A O     1 
ATOM   153  C  CB    . PHE   A 1 62  ? 12.294  10.520  -1.634  1.00 18.53 ?  47   PHE   A CB    1 
ATOM   154  C  CG    . PHE   A 1 62  ? 12.642  11.975  -1.911  1.00 17.99 ?  47   PHE   A CG    1 
ATOM   155  C  CD1   . PHE   A 1 62  ? 13.546  12.318  -2.903  1.00 17.83 ?  47   PHE   A CD1   1 
ATOM   156  C  CD2   . PHE   A 1 62  ? 12.079  13.003  -1.146  1.00 20.28 ?  47   PHE   A CD2   1 
ATOM   157  C  CE1   . PHE   A 1 62  ? 13.867  13.657  -3.162  1.00 19.27 ?  47   PHE   A CE1   1 
ATOM   158  C  CE2   . PHE   A 1 62  ? 12.402  14.338  -1.392  1.00 20.99 ?  47   PHE   A CE2   1 
ATOM   159  C  CZ    . PHE   A 1 62  ? 13.295  14.672  -2.400  1.00 21.94 ?  47   PHE   A CZ    1 
ATOM   160  N  N     . ASP   A 1 63  ? 10.387  7.937   -1.691  1.00 18.33 ?  48   ASP   A N     1 
ATOM   161  C  CA    . ASP   A 1 63  ? 10.227  6.526   -1.324  1.00 20.39 ?  48   ASP   A CA    1 
ATOM   162  C  C     . ASP   A 1 63  ? 9.835   5.632   -2.502  1.00 20.69 ?  48   ASP   A C     1 
ATOM   163  O  O     . ASP   A 1 63  ? 9.889   4.402   -2.358  1.00 22.69 ?  48   ASP   A O     1 
ATOM   164  C  CB    . ASP   A 1 63  ? 9.177   6.369   -0.210  1.00 23.36 ?  48   ASP   A CB    1 
ATOM   165  C  CG    . ASP   A 1 63  ? 9.684   6.816   1.164   1.00 29.66 ?  48   ASP   A CG    1 
ATOM   166  O  OD1   . ASP   A 1 63  ? 10.877  7.150   1.311   1.00 29.97 ?  48   ASP   A OD1   1 
ATOM   167  O  OD2   . ASP   A 1 63  ? 8.864   6.843   2.114   1.00 34.94 -1 48   ASP   A OD2   1 
ATOM   168  N  N     . ASP   A 1 64  ? 9.441   6.201   -3.654  1.00 16.31 ?  49   ASP   A N     1 
ATOM   169  C  CA    . ASP   A 1 64  ? 9.060   5.404   -4.820  1.00 16.90 ?  49   ASP   A CA    1 
ATOM   170  C  C     . ASP   A 1 64  ? 10.238  4.890   -5.659  1.00 16.50 ?  49   ASP   A C     1 
ATOM   171  O  O     . ASP   A 1 64  ? 9.994   4.073   -6.561  1.00 19.08 ?  49   ASP   A O     1 
ATOM   172  C  CB    . ASP   A 1 64  ? 8.132   6.217   -5.741  1.00 18.15 ?  49   ASP   A CB    1 
ATOM   173  C  CG    . ASP   A 1 64  ? 6.719   6.373   -5.188  1.00 21.16 ?  49   ASP   A CG    1 
ATOM   174  O  OD1   . ASP   A 1 64  ? 6.059   5.343   -4.892  1.00 22.97 ?  49   ASP   A OD1   1 
ATOM   175  O  OD2   . ASP   A 1 64  ? 6.239   7.528   -5.093  1.00 18.54 -1 49   ASP   A OD2   1 
ATOM   176  N  N     . VAL   A 1 65  ? 11.487  5.349   -5.427  1.00 16.35 ?  50   VAL   A N     1 
ATOM   177  C  CA    . VAL   A 1 65  ? 12.614  5.014   -6.305  1.00 18.04 ?  50   VAL   A CA    1 
ATOM   178  C  C     . VAL   A 1 65  ? 13.866  4.670   -5.498  1.00 17.02 ?  50   VAL   A C     1 
ATOM   179  O  O     . VAL   A 1 65  ? 14.036  5.124   -4.363  1.00 17.27 ?  50   VAL   A O     1 
ATOM   180  C  CB    . VAL   A 1 65  ? 12.942  6.185   -7.281  1.00 16.46 ?  50   VAL   A CB    1 
ATOM   181  C  CG1   . VAL   A 1 65  ? 11.800  6.424   -8.268  1.00 16.91 ?  50   VAL   A CG1   1 
ATOM   182  C  CG2   . VAL   A 1 65  ? 13.266  7.475   -6.512  1.00 17.40 ?  50   VAL   A CG2   1 
ATOM   183  N  N     . LEU   A 1 66  ? 14.757  3.864   -6.103  1.00 15.25 ?  51   LEU   A N     1 
ATOM   184  C  CA    . LEU   A 1 66  ? 16.128  3.655   -5.628  1.00 16.30 ?  51   LEU   A CA    1 
ATOM   185  C  C     . LEU   A 1 66  ? 17.088  3.903   -6.786  1.00 16.04 ?  51   LEU   A C     1 
ATOM   186  O  O     . LEU   A 1 66  ? 16.725  3.709   -7.948  1.00 15.95 ?  51   LEU   A O     1 
ATOM   187  C  CB    . LEU   A 1 66  ? 16.382  2.204   -5.072  1.00 15.44 ?  51   LEU   A CB    1 
ATOM   188  C  CG    . LEU   A 1 66  ? 15.617  1.858   -3.789  1.00 17.20 ?  51   LEU   A CG    1 
ATOM   189  C  CD1   . LEU   A 1 66  ? 15.746  0.331   -3.506  1.00 19.17 ?  51   LEU   A CD1   1 
ATOM   190  C  CD2   . LEU   A 1 66  ? 16.142  2.653   -2.588  1.00 20.04 ?  51   LEU   A CD2   1 
ATOM   191  N  N     . LEU   A 1 67  ? 18.325  4.321   -6.465  1.00 16.11 ?  52   LEU   A N     1 
ATOM   192  C  CA    . LEU   A 1 67  ? 19.402  4.417   -7.464  1.00 15.30 ?  52   LEU   A CA    1 
ATOM   193  C  C     . LEU   A 1 67  ? 20.010  3.049   -7.798  1.00 14.96 ?  52   LEU   A C     1 
ATOM   194  O  O     . LEU   A 1 67  ? 20.372  2.283   -6.900  1.00 16.58 ?  52   LEU   A O     1 
ATOM   195  C  CB    . LEU   A 1 67  ? 20.508  5.355   -6.962  1.00 16.09 ?  52   LEU   A CB    1 
ATOM   196  C  CG    . LEU   A 1 67  ? 20.100  6.833   -6.919  1.00 19.09 ?  52   LEU   A CG    1 
ATOM   197  C  CD1   . LEU   A 1 67  ? 21.056  7.660   -6.049  1.00 18.67 ?  52   LEU   A CD1   1 
ATOM   198  C  CD2   . LEU   A 1 67  ? 20.044  7.375   -8.327  1.00 20.90 ?  52   LEU   A CD2   1 
ATOM   199  N  N     . LEU   A 1 68  ? 20.151  2.760   -9.106  1.00 17.10 ?  53   LEU   A N     1 
ATOM   200  C  CA    . LEU   A 1 68  ? 20.773  1.502   -9.544  1.00 17.57 ?  53   LEU   A CA    1 
ATOM   201  C  C     . LEU   A 1 68  ? 22.299  1.586   -9.460  1.00 16.14 ?  53   LEU   A C     1 
ATOM   202  O  O     . LEU   A 1 68  ? 22.894  2.574   -9.916  1.00 19.70 ?  53   LEU   A O     1 
ATOM   203  C  CB    . LEU   A 1 68  ? 20.348  1.164   -10.982 1.00 17.97 ?  53   LEU   A CB    1 
ATOM   204  C  CG    . LEU   A 1 68  ? 18.919  0.627   -11.163 1.00 18.91 ?  53   LEU   A CG    1 
ATOM   205  C  CD1   . LEU   A 1 68  ? 18.495  0.688   -12.627 1.00 21.69 ?  53   LEU   A CD1   1 
ATOM   206  C  CD2   . LEU   A 1 68  ? 18.842  -0.817  -10.652 1.00 18.23 ?  53   LEU   A CD2   1 
ATOM   207  N  N     . PRO   A 1 69  ? 22.966  0.565   -8.913  1.00 17.76 ?  54   PRO   A N     1 
ATOM   208  C  CA    . PRO   A 1 69  ? 24.435  0.512   -9.004  1.00 17.28 ?  54   PRO   A CA    1 
ATOM   209  C  C     . PRO   A 1 69  ? 24.882  0.454   -10.463 1.00 18.06 ?  54   PRO   A C     1 
ATOM   210  O  O     . PRO   A 1 69  ? 24.161  -0.052  -11.328 1.00 18.55 ?  54   PRO   A O     1 
ATOM   211  C  CB    . PRO   A 1 69  ? 24.803  -0.779  -8.247  1.00 19.98 ?  54   PRO   A CB    1 
ATOM   212  C  CG    . PRO   A 1 69  ? 23.590  -1.125  -7.408  1.00 20.48 ?  54   PRO   A CG    1 
ATOM   213  C  CD    . PRO   A 1 69  ? 22.391  -0.573  -8.169  1.00 18.01 ?  54   PRO   A CD    1 
ATOM   214  N  N     . ALA   A 1 70  ? 26.084  0.995   -10.737 1.00 17.84 ?  55   ALA   A N     1 
ATOM   215  C  CA    . ALA   A 1 70  ? 26.627  1.054   -12.096 1.00 18.14 ?  55   ALA   A CA    1 
ATOM   216  C  C     . ALA   A 1 70  ? 28.146  0.861   -12.063 1.00 20.00 ?  55   ALA   A C     1 
ATOM   217  O  O     . ALA   A 1 70  ? 28.768  0.873   -11.002 1.00 18.44 ?  55   ALA   A O     1 
ATOM   218  C  CB    . ALA   A 1 70  ? 26.275  2.382   -12.790 1.00 20.45 ?  55   ALA   A CB    1 
ATOM   219  N  N     . ALA   A 1 71  ? 28.747  0.678   -13.246 1.00 19.12 ?  56   ALA   A N     1 
ATOM   220  C  CA    . ALA   A 1 71  ? 30.198  0.493   -13.324 1.00 19.14 ?  56   ALA   A CA    1 
ATOM   221  C  C     . ALA   A 1 71  ? 30.921  1.690   -12.710 1.00 20.66 ?  56   ALA   A C     1 
ATOM   222  O  O     . ALA   A 1 71  ? 30.595  2.844   -13.019 1.00 21.01 ?  56   ALA   A O     1 
ATOM   223  C  CB    . ALA   A 1 71  ? 30.612  0.308   -14.782 1.00 20.01 ?  56   ALA   A CB    1 
ATOM   224  N  N     . SER   A 1 72  ? 31.915  1.424   -11.846 1.00 18.13 ?  57   SER   A N     1 
ATOM   225  C  CA    . SER   A 1 72  ? 32.511  2.492   -11.043 1.00 19.30 ?  57   SER   A CA    1 
ATOM   226  C  C     . SER   A 1 72  ? 34.002  2.310   -10.785 1.00 25.15 ?  57   SER   A C     1 
ATOM   227  O  O     . SER   A 1 72  ? 34.455  1.223   -10.418 1.00 27.65 ?  57   SER   A O     1 
ATOM   228  C  CB    . SER   A 1 72  ? 31.796  2.612   -9.691  1.00 19.51 ?  57   SER   A CB    1 
ATOM   229  O  OG    . SER   A 1 72  ? 32.343  3.677   -8.936  1.00 18.82 ?  57   SER   A OG    1 
ATOM   230  N  N     . ASP   A 1 73  ? 34.753  3.410   -10.935 1.00 24.95 ?  58   ASP   A N     1 
ATOM   231  C  CA    . ASP   A 1 73  ? 36.112  3.534   -10.411 1.00 27.32 ?  58   ASP   A CA    1 
ATOM   232  C  C     . ASP   A 1 73  ? 36.174  4.465   -9.198  1.00 31.14 ?  58   ASP   A C     1 
ATOM   233  O  O     . ASP   A 1 73  ? 37.268  4.769   -8.707  1.00 34.80 ?  58   ASP   A O     1 
ATOM   234  C  CB    . ASP   A 1 73  ? 37.063  4.039   -11.503 1.00 31.24 ?  58   ASP   A CB    1 
ATOM   235  C  CG    . ASP   A 1 73  ? 37.303  3.016   -12.596 1.00 47.02 ?  58   ASP   A CG    1 
ATOM   236  O  OD1   . ASP   A 1 73  ? 37.421  1.812   -12.282 1.00 46.79 ?  58   ASP   A OD1   1 
ATOM   237  O  OD2   . ASP   A 1 73  ? 37.370  3.423   -13.777 1.00 52.23 -1 58   ASP   A OD2   1 
ATOM   238  N  N     . VAL   A 1 74  ? 35.025  4.920   -8.707  1.00 21.78 ?  59   VAL   A N     1 
ATOM   239  C  CA    . VAL   A 1 74  ? 34.930  5.912   -7.640  1.00 20.79 ?  59   VAL   A CA    1 
ATOM   240  C  C     . VAL   A 1 74  ? 34.774  5.194   -6.311  1.00 20.72 ?  59   VAL   A C     1 
ATOM   241  O  O     . VAL   A 1 74  ? 33.937  4.293   -6.189  1.00 23.28 ?  59   VAL   A O     1 
ATOM   242  C  CB    . VAL   A 1 74  ? 33.725  6.844   -7.877  1.00 19.10 ?  59   VAL   A CB    1 
ATOM   243  C  CG1   . VAL   A 1 74  ? 33.559  7.845   -6.724  1.00 21.94 ?  59   VAL   A CG1   1 
ATOM   244  C  CG2   . VAL   A 1 74  ? 33.840  7.538   -9.230  1.00 24.24 ?  59   VAL   A CG2   1 
ATOM   245  N  N     . VAL   A 1 75  ? 35.534  5.612   -5.303  1.00 25.71 ?  60   VAL   A N     1 
ATOM   246  C  CA    . VAL   A 1 75  ? 35.267  5.161   -3.937  1.00 30.00 ?  60   VAL   A CA    1 
ATOM   247  C  C     . VAL   A 1 75  ? 34.805  6.363   -3.126  1.00 23.34 ?  60   VAL   A C     1 
ATOM   248  O  O     . VAL   A 1 75  ? 35.094  7.509   -3.504  1.00 26.99 ?  60   VAL   A O     1 
ATOM   249  C  CB    . VAL   A 1 75  ? 36.488  4.492   -3.289  1.00 30.29 ?  60   VAL   A CB    1 
ATOM   250  C  CG1   . VAL   A 1 75  ? 36.819  3.193   -4.021  1.00 35.21 ?  60   VAL   A CG1   1 
ATOM   251  C  CG2   . VAL   A 1 75  ? 37.684  5.449   -3.249  1.00 24.14 ?  60   VAL   A CG2   1 
ATOM   252  N  N     . PRO   A 1 76  ? 34.102  6.157   -2.017  1.00 22.20 ?  61   PRO   A N     1 
ATOM   253  C  CA    . PRO   A 1 76  ? 33.498  7.305   -1.322  1.00 21.27 ?  61   PRO   A CA    1 
ATOM   254  C  C     . PRO   A 1 76  ? 34.500  8.404   -1.004  1.00 20.67 ?  61   PRO   A C     1 
ATOM   255  O  O     . PRO   A 1 76  ? 34.175  9.594   -1.138  1.00 25.05 ?  61   PRO   A O     1 
ATOM   256  C  CB    . PRO   A 1 76  ? 32.903  6.658   -0.066  1.00 25.01 ?  61   PRO   A CB    1 
ATOM   257  C  CG    . PRO   A 1 76  ? 32.510  5.269   -0.541  1.00 25.23 ?  61   PRO   A CG    1 
ATOM   258  C  CD    . PRO   A 1 76  ? 33.657  4.864   -1.455  1.00 24.05 ?  61   PRO   A CD    1 
ATOM   259  N  N     . ALA   A 1 77  ? 35.740  8.030   -0.661  1.00 23.09 ?  62   ALA   A N     1 
ATOM   260  C  CA    . ALA   A 1 77  ? 36.763  9.014   -0.301  1.00 25.91 ?  62   ALA   A CA    1 
ATOM   261  C  C     . ALA   A 1 77  ? 37.209  9.876   -1.481  1.00 24.27 ?  62   ALA   A C     1 
ATOM   262  O  O     . ALA   A 1 77  ? 37.699  10.992  -1.271  1.00 33.46 ?  62   ALA   A O     1 
ATOM   263  C  CB    . ALA   A 1 77  ? 37.975  8.302   0.303   1.00 33.24 ?  62   ALA   A CB    1 
ATOM   264  N  N     . THR   A 1 78  ? 37.099  9.397   -2.714  1.00 28.20 ?  63   THR   A N     1 
ATOM   265  C  CA    . THR   A 1 78  ? 37.612  10.186  -3.829  1.00 26.29 ?  63   THR   A CA    1 
ATOM   266  C  C     . THR   A 1 78  ? 36.532  11.014  -4.522  1.00 31.24 ?  63   THR   A C     1 
ATOM   267  O  O     . THR   A 1 78  ? 36.858  11.801  -5.416  1.00 29.13 ?  63   THR   A O     1 
ATOM   268  C  CB    . THR   A 1 78  ? 38.349  9.301   -4.858  1.00 23.86 ?  63   THR   A CB    1 
ATOM   269  O  OG1   . THR   A 1 78  ? 37.462  8.337   -5.456  1.00 28.89 ?  63   THR   A OG1   1 
ATOM   270  C  CG2   . THR   A 1 78  ? 39.529  8.565   -4.204  1.00 25.69 ?  63   THR   A CG2   1 
ATOM   271  N  N     . ALA   A 1 79  ? 35.266  10.898  -4.109  1.00 22.89 ?  64   ALA   A N     1 
ATOM   272  C  CA    . ALA   A 1 79  ? 34.214  11.684  -4.749  1.00 23.93 ?  64   ALA   A CA    1 
ATOM   273  C  C     . ALA   A 1 79  ? 34.370  13.188  -4.480  1.00 21.84 ?  64   ALA   A C     1 
ATOM   274  O  O     . ALA   A 1 79  ? 34.860  13.610  -3.428  1.00 28.90 ?  64   ALA   A O     1 
ATOM   275  C  CB    . ALA   A 1 79  ? 32.852  11.206  -4.263  1.00 21.84 ?  64   ALA   A CB    1 
ATOM   276  N  N     . ASP   A 1 80  ? 33.929  14.006  -5.457  1.00 18.67 ?  65   ASP   A N     1 
ATOM   277  C  CA    . ASP   A 1 80  ? 33.946  15.471  -5.379  1.00 19.08 ?  65   ASP   A CA    1 
ATOM   278  C  C     . ASP   A 1 80  ? 32.497  15.946  -5.237  1.00 18.05 ?  65   ASP   A C     1 
ATOM   279  O  O     . ASP   A 1 80  ? 31.711  15.819  -6.183  1.00 20.08 ?  65   ASP   A O     1 
ATOM   280  C  CB    . ASP   A 1 80  ? 34.605  16.050  -6.636  1.00 21.46 ?  65   ASP   A CB    1 
ATOM   281  C  CG    . ASP   A 1 80  ? 34.586  17.575  -6.704  1.00 27.63 ?  65   ASP   A CG    1 
ATOM   282  O  OD1   . ASP   A 1 80  ? 33.948  18.254  -5.866  1.00 23.88 ?  65   ASP   A OD1   1 
ATOM   283  O  OD2   . ASP   A 1 80  ? 35.240  18.102  -7.634  1.00 30.66 -1 65   ASP   A OD2   1 
ATOM   284  N  N     . THR   A 1 81  ? 32.142  16.481  -4.060  1.00 19.13 ?  66   THR   A N     1 
ATOM   285  C  CA    . THR   A 1 81  ? 30.749  16.854  -3.773  1.00 17.67 ?  66   THR   A CA    1 
ATOM   286  C  C     . THR   A 1 81  ? 30.384  18.311  -4.144  1.00 19.43 ?  66   THR   A C     1 
ATOM   287  O  O     . THR   A 1 81  ? 29.262  18.737  -3.843  1.00 19.71 ?  66   THR   A O     1 
ATOM   288  C  CB    . THR   A 1 81  ? 30.405  16.617  -2.285  1.00 18.03 ?  66   THR   A CB    1 
ATOM   289  O  OG1   . THR   A 1 81  ? 31.228  17.430  -1.420  1.00 22.24 ?  66   THR   A OG1   1 
ATOM   290  C  CG2   . THR   A 1 81  ? 30.548  15.116  -1.890  1.00 21.66 ?  66   THR   A CG2   1 
ATOM   291  N  N     . SER   A 1 82  ? 31.272  19.083  -4.785  1.00 18.43 ?  67   SER   A N     1 
ATOM   292  C  CA    . SER   A 1 82  ? 30.946  20.485  -5.079  1.00 17.84 ?  67   SER   A CA    1 
ATOM   293  C  C     . SER   A 1 82  ? 29.856  20.618  -6.153  1.00 20.50 ?  67   SER   A C     1 
ATOM   294  O  O     . SER   A 1 82  ? 29.680  19.738  -7.007  1.00 19.69 ?  67   SER   A O     1 
ATOM   295  C  CB    . SER   A 1 82  ? 32.210  21.237  -5.512  1.00 20.29 ?  67   SER   A CB    1 
ATOM   296  O  OG    . SER   A 1 82  ? 32.741  20.734  -6.728  1.00 22.57 ?  67   SER   A OG    1 
ATOM   297  N  N     . SER   A 1 83  ? 29.109  21.734  -6.105  1.00 18.59 ?  68   SER   A N     1 
ATOM   298  C  CA    . SER   A 1 83  ? 27.978  21.920  -7.017  1.00 18.19 ?  68   SER   A CA    1 
ATOM   299  C  C     . SER   A 1 83  ? 27.540  23.383  -7.018  1.00 19.33 ?  68   SER   A C     1 
ATOM   300  O  O     . SER   A 1 83  ? 27.730  24.104  -6.034  1.00 20.94 ?  68   SER   A O     1 
ATOM   301  C  CB    . SER   A 1 83  ? 26.795  21.022  -6.616  1.00 19.36 ?  68   SER   A CB    1 
ATOM   302  O  OG    . SER   A 1 83  ? 25.825  20.946  -7.651  1.00 19.62 ?  68   SER   A OG    1 
ATOM   303  N  N     . GLN   A 1 84  ? 26.899  23.800  -8.114  1.00 19.02 ?  69   GLN   A N     1 
ATOM   304  C  CA    . GLN   A 1 84  ? 26.388  25.171  -8.206  1.00 20.01 ?  69   GLN   A CA    1 
ATOM   305  C  C     . GLN   A 1 84  ? 25.141  25.382  -7.355  1.00 19.70 ?  69   GLN   A C     1 
ATOM   306  O  O     . GLN   A 1 84  ? 24.146  24.657  -7.507  1.00 19.27 ?  69   GLN   A O     1 
ATOM   307  C  CB    . GLN   A 1 84  ? 26.037  25.535  -9.647  1.00 20.27 ?  69   GLN   A CB    1 
ATOM   308  C  CG    . GLN   A 1 84  ? 27.177  25.382  -10.662 1.00 27.42 ?  69   GLN   A CG    1 
ATOM   309  C  CD    . GLN   A 1 84  ? 28.356  26.296  -10.407 1.00 27.01 ?  69   GLN   A CD    1 
ATOM   310  O  OE1   . GLN   A 1 84  ? 29.513  25.867  -10.490 1.00 28.65 ?  69   GLN   A OE1   1 
ATOM   311  N  NE2   . GLN   A 1 84  ? 28.083  27.568  -10.119 1.00 26.88 ?  69   GLN   A NE2   1 
ATOM   312  N  N     . LEU   A 1 85  ? 25.183  26.415  -6.499  1.00 18.54 ?  70   LEU   A N     1 
ATOM   313  C  CA    . LEU   A 1 85  ? 23.966  26.955  -5.881  1.00 16.84 ?  70   LEU   A CA    1 
ATOM   314  C  C     . LEU   A 1 85  ? 23.207  27.860  -6.845  1.00 19.24 ?  70   LEU   A C     1 
ATOM   315  O  O     . LEU   A 1 85  ? 21.979  27.749  -6.980  1.00 19.13 ?  70   LEU   A O     1 
ATOM   316  C  CB    . LEU   A 1 85  ? 24.311  27.726  -4.604  1.00 16.83 ?  70   LEU   A CB    1 
ATOM   317  C  CG    . LEU   A 1 85  ? 23.122  28.372  -3.874  1.00 16.70 ?  70   LEU   A CG    1 
ATOM   318  C  CD1   . LEU   A 1 85  ? 22.203  27.290  -3.278  1.00 19.00 ?  70   LEU   A CD1   1 
ATOM   319  C  CD2   . LEU   A 1 85  ? 23.608  29.365  -2.792  1.00 20.65 ?  70   LEU   A CD2   1 
ATOM   320  N  N     . THR   A 1 86  ? 23.916  28.791  -7.498  1.00 21.50 ?  71   THR   A N     1 
ATOM   321  C  CA    . THR   A 1 86  ? 23.351  29.702  -8.493  1.00 20.21 ?  71   THR   A CA    1 
ATOM   322  C  C     . THR   A 1 86  ? 24.283  29.734  -9.700  1.00 22.10 ?  71   THR   A C     1 
ATOM   323  O  O     . THR   A 1 86  ? 25.337  29.094  -9.707  1.00 20.73 ?  71   THR   A O     1 
ATOM   324  C  CB    . THR   A 1 86  ? 23.168  31.124  -7.932  1.00 21.66 ?  71   THR   A CB    1 
ATOM   325  O  OG1   . THR   A 1 86  ? 24.459  31.722  -7.759  1.00 21.79 ?  71   THR   A OG1   1 
ATOM   326  C  CG2   . THR   A 1 86  ? 22.445  31.119  -6.583  1.00 21.81 ?  71   THR   A CG2   1 
ATOM   327  N  N     . LYS   A 1 87  ? 23.912  30.517  -10.721 1.00 23.35 ?  72   LYS   A N     1 
ATOM   328  C  CA    . LYS   A 1 87  ? 24.781  30.653  -11.894 1.00 26.16 ?  72   LYS   A CA    1 
ATOM   329  C  C     . LYS   A 1 87  ? 26.223  30.980  -11.501 1.00 29.06 ?  72   LYS   A C     1 
ATOM   330  O  O     . LYS   A 1 87  ? 27.167  30.387  -12.042 1.00 30.17 ?  72   LYS   A O     1 
ATOM   331  C  CB    . LYS   A 1 87  ? 24.233  31.725  -12.849 1.00 23.65 ?  72   LYS   A CB    1 
ATOM   332  C  CG    . LYS   A 1 87  ? 22.957  31.317  -13.607 1.00 26.18 ?  72   LYS   A CG    1 
ATOM   333  C  CD    . LYS   A 1 87  ? 22.478  32.434  -14.548 1.00 28.56 ?  72   LYS   A CD    1 
ATOM   334  C  CE    . LYS   A 1 87  ? 21.165  32.057  -15.226 1.00 32.06 ?  72   LYS   A CE    1 
ATOM   335  N  NZ    . LYS   A 1 87  ? 20.567  33.231  -15.954 1.00 40.94 ?  72   LYS   A NZ    1 
ATOM   336  N  N     . LYS   A 1 88  ? 26.425  31.910  -10.559 1.00 23.45 ?  73   LYS   A N     1 
ATOM   337  C  CA    . LYS   A 1 88  ? 27.782  32.355  -10.240 1.00 25.13 ?  73   LYS   A CA    1 
ATOM   338  C  C     . LYS   A 1 88  ? 28.387  31.746  -8.974  1.00 29.83 ?  73   LYS   A C     1 
ATOM   339  O  O     . LYS   A 1 88  ? 29.600  31.884  -8.776  1.00 35.03 ?  73   LYS   A O     1 
ATOM   340  C  CB    . LYS   A 1 88  ? 27.814  33.893  -10.131 1.00 27.48 ?  73   LYS   A CB    1 
ATOM   341  C  CG    . LYS   A 1 88  ? 27.495  34.583  -11.460 1.00 30.57 ?  73   LYS   A CG    1 
ATOM   342  C  CD    . LYS   A 1 88  ? 26.974  36.013  -11.308 1.00 44.65 ?  73   LYS   A CD    1 
ATOM   343  C  CE    . LYS   A 1 88  ? 28.059  36.998  -10.929 1.00 40.88 ?  73   LYS   A CE    1 
ATOM   344  N  NZ    . LYS   A 1 88  ? 27.641  38.433  -11.152 1.00 44.69 ?  73   LYS   A NZ    1 
ATOM   345  N  N     . ILE   A 1 89  ? 27.615  31.079  -8.111  1.00 22.80 ?  74   ILE   A N     1 
ATOM   346  C  CA    . ILE   A 1 89  ? 28.117  30.641  -6.804  1.00 22.63 ?  74   ILE   A CA    1 
ATOM   347  C  C     . ILE   A 1 89  ? 28.170  29.112  -6.754  1.00 24.28 ?  74   ILE   A C     1 
ATOM   348  O  O     . ILE   A 1 89  ? 27.140  28.448  -6.929  1.00 23.04 ?  74   ILE   A O     1 
ATOM   349  C  CB    . ILE   A 1 89  ? 27.254  31.196  -5.659  1.00 21.87 ?  74   ILE   A CB    1 
ATOM   350  C  CG1   . ILE   A 1 89  ? 27.343  32.731  -5.606  1.00 22.84 ?  74   ILE   A CG1   1 
ATOM   351  C  CG2   . ILE   A 1 89  ? 27.679  30.593  -4.329  1.00 23.17 ?  74   ILE   A CG2   1 
ATOM   352  C  CD1   . ILE   A 1 89  ? 26.432  33.343  -4.580  1.00 30.06 ?  74   ILE   A CD1   1 
ATOM   353  N  N     . ARG   A 1 90  ? 29.358  28.556  -6.470  1.00 22.28 ?  75   ARG   A N     1 
ATOM   354  C  CA    . ARG   A 1 90  ? 29.569  27.114  -6.303  1.00 20.30 ?  75   ARG   A CA    1 
ATOM   355  C  C     . ARG   A 1 90  ? 29.902  26.822  -4.841  1.00 23.43 ?  75   ARG   A C     1 
ATOM   356  O  O     . ARG   A 1 90  ? 30.727  27.518  -4.238  1.00 30.23 ?  75   ARG   A O     1 
ATOM   357  C  CB    . ARG   A 1 90  ? 30.700  26.601  -7.216  1.00 23.38 ?  75   ARG   A CB    1 
ATOM   358  C  CG    . ARG   A 1 90  ? 30.749  25.065  -7.382  1.00 22.49 ?  75   ARG   A CG    1 
ATOM   359  C  CD    . ARG   A 1 90  ? 31.849  24.617  -8.378  1.00 26.05 ?  75   ARG   A CD    1 
ATOM   360  N  NE    . ARG   A 1 90  ? 31.912  23.161  -8.573  1.00 27.11 ?  75   ARG   A NE    1 
ATOM   361  C  CZ    . ARG   A 1 90  ? 31.088  22.462  -9.357  1.00 24.97 ?  75   ARG   A CZ    1 
ATOM   362  N  NH1   . ARG   A 1 90  ? 30.111  23.074  -10.031 1.00 27.65 ?  75   ARG   A NH1   1 
ATOM   363  N  NH2   . ARG   A 1 90  ? 31.220  21.145  -9.464  1.00 26.17 ?  75   ARG   A NH2   1 
ATOM   364  N  N     . LEU   A 1 91  ? 29.270  25.795  -4.272  1.00 18.74 ?  76   LEU   A N     1 
ATOM   365  C  CA    . LEU   A 1 91  ? 29.503  25.362  -2.897  1.00 19.11 ?  76   LEU   A CA    1 
ATOM   366  C  C     . LEU   A 1 91  ? 30.363  24.091  -2.856  1.00 20.83 ?  76   LEU   A C     1 
ATOM   367  O  O     . LEU   A 1 91  ? 30.335  23.276  -3.783  1.00 21.08 ?  76   LEU   A O     1 
ATOM   368  C  CB    . LEU   A 1 91  ? 28.163  25.071  -2.192  1.00 18.12 ?  76   LEU   A CB    1 
ATOM   369  C  CG    . LEU   A 1 91  ? 27.111  26.189  -2.070  1.00 17.40 ?  76   LEU   A CG    1 
ATOM   370  C  CD1   . LEU   A 1 91  ? 25.807  25.685  -1.424  1.00 18.72 ?  76   LEU   A CD1   1 
ATOM   371  C  CD2   . LEU   A 1 91  ? 27.682  27.381  -1.294  1.00 22.40 ?  76   LEU   A CD2   1 
ATOM   372  N  N     . LYS   A 1 92  ? 31.111  23.914  -1.755  1.00 20.15 ?  77   LYS   A N     1 
ATOM   373  C  CA    . LYS   A 1 92  ? 31.870  22.678  -1.557  1.00 19.55 ?  77   LYS   A CA    1 
ATOM   374  C  C     . LYS   A 1 92  ? 30.989  21.490  -1.160  1.00 19.39 ?  77   LYS   A C     1 
ATOM   375  O  O     . LYS   A 1 92  ? 31.323  20.338  -1.493  1.00 19.93 ?  77   LYS   A O     1 
ATOM   376  C  CB    . LYS   A 1 92  ? 32.948  22.884  -0.489  1.00 23.47 ?  77   LYS   A CB    1 
ATOM   377  C  CG    . LYS   A 1 92  ? 34.086  23.807  -0.911  1.00 27.64 ?  77   LYS   A CG    1 
ATOM   378  C  CD    . LYS   A 1 92  ? 35.014  24.075  0.262   1.00 39.17 ?  77   LYS   A CD    1 
ATOM   379  C  CE    . LYS   A 1 92  ? 36.161  23.080  0.305   1.00 51.41 ?  77   LYS   A CE    1 
ATOM   380  N  NZ    . LYS   A 1 92  ? 37.138  23.351  -0.791  1.00 60.21 ?  77   LYS   A NZ    1 
ATOM   381  N  N     . VAL   A 1 93  ? 29.891  21.744  -0.444  1.00 19.70 ?  78   VAL   A N     1 
ATOM   382  C  CA    . VAL   A 1 93  ? 28.933  20.726  0.000   1.00 18.34 ?  78   VAL   A CA    1 
ATOM   383  C  C     . VAL   A 1 93  ? 27.569  21.210  -0.491  1.00 16.99 ?  78   VAL   A C     1 
ATOM   384  O  O     . VAL   A 1 93  ? 27.246  22.386  -0.276  1.00 20.02 ?  78   VAL   A O     1 
ATOM   385  C  CB    . VAL   A 1 93  ? 28.981  20.562  1.530   1.00 24.74 ?  78   VAL   A CB    1 
ATOM   386  C  CG1   . VAL   A 1 93  ? 27.813  19.731  2.053   1.00 26.97 ?  78   VAL   A CG1   1 
ATOM   387  C  CG2   . VAL   A 1 93  ? 30.332  19.952  1.954   1.00 23.57 ?  78   VAL   A CG2   1 
ATOM   388  N  N     . PRO   A 1 94  ? 26.748  20.374  -1.187  1.00 17.49 ?  79   PRO   A N     1 
ATOM   389  C  CA    . PRO   A 1 94  ? 25.570  20.895  -1.901  1.00 18.97 ?  79   PRO   A CA    1 
ATOM   390  C  C     . PRO   A 1 94  ? 24.296  20.996  -1.062  1.00 17.91 ?  79   PRO   A C     1 
ATOM   391  O  O     . PRO   A 1 94  ? 23.210  20.525  -1.470  1.00 18.26 ?  79   PRO   A O     1 
ATOM   392  C  CB    . PRO   A 1 94  ? 25.404  19.885  -3.048  1.00 20.18 ?  79   PRO   A CB    1 
ATOM   393  C  CG    . PRO   A 1 94  ? 25.873  18.573  -2.440  1.00 18.83 ?  79   PRO   A CG    1 
ATOM   394  C  CD    . PRO   A 1 94  ? 27.051  18.984  -1.571  1.00 17.58 ?  79   PRO   A CD    1 
ATOM   395  N  N     . LEU   A 1 95  ? 24.399  21.653  0.100   1.00 17.52 ?  80   LEU   A N     1 
ATOM   396  C  CA    . LEU   A 1 95  ? 23.323  21.719  1.089   1.00 20.17 ?  80   LEU   A CA    1 
ATOM   397  C  C     . LEU   A 1 95  ? 23.129  23.137  1.626   1.00 18.24 ?  80   LEU   A C     1 
ATOM   398  O  O     . LEU   A 1 95  ? 24.108  23.855  1.882   1.00 19.16 ?  80   LEU   A O     1 
ATOM   399  C  CB    . LEU   A 1 95  ? 23.625  20.790  2.270   1.00 17.43 ?  80   LEU   A CB    1 
ATOM   400  C  CG    . LEU   A 1 95  ? 23.864  19.312  1.945   1.00 20.16 ?  80   LEU   A CG    1 
ATOM   401  C  CD1   . LEU   A 1 95  ? 24.345  18.542  3.185   1.00 21.25 ?  80   LEU   A CD1   1 
ATOM   402  C  CD2   . LEU   A 1 95  ? 22.580  18.688  1.391   1.00 19.88 ?  80   LEU   A CD2   1 
ATOM   403  N  N     A VAL   A 1 96  ? 21.866  23.546  1.777   0.66 19.23 ?  81   VAL   A N     1 
ATOM   404  N  N     B VAL   A 1 96  ? 21.866  23.509  1.848   0.34 19.22 ?  81   VAL   A N     1 
ATOM   405  C  CA    A VAL   A 1 96  ? 21.535  24.834  2.383   0.66 18.26 ?  81   VAL   A CA    1 
ATOM   406  C  CA    B VAL   A 1 96  ? 21.494  24.834  2.345   0.34 18.30 ?  81   VAL   A CA    1 
ATOM   407  C  C     A VAL   A 1 96  ? 20.450  24.623  3.432   0.66 18.51 ?  81   VAL   A C     1 
ATOM   408  C  C     B VAL   A 1 96  ? 20.384  24.687  3.380   0.34 18.53 ?  81   VAL   A C     1 
ATOM   409  O  O     A VAL   A 1 96  ? 19.643  23.694  3.342   0.66 17.13 ?  81   VAL   A O     1 
ATOM   410  O  O     B VAL   A 1 96  ? 19.466  23.880  3.202   0.34 17.45 ?  81   VAL   A O     1 
ATOM   411  C  CB    A VAL   A 1 96  ? 21.099  25.890  1.336   0.66 24.19 ?  81   VAL   A CB    1 
ATOM   412  C  CB    B VAL   A 1 96  ? 21.044  25.757  1.193   0.34 23.65 ?  81   VAL   A CB    1 
ATOM   413  C  CG1   A VAL   A 1 96  ? 22.198  26.087  0.278   0.66 21.14 ?  81   VAL   A CG1   1 
ATOM   414  C  CG1   B VAL   A 1 96  ? 19.974  25.080  0.360   0.34 23.78 ?  81   VAL   A CG1   1 
ATOM   415  C  CG2   A VAL   A 1 96  ? 19.784  25.518  0.696   0.66 23.48 ?  81   VAL   A CG2   1 
ATOM   416  C  CG2   B VAL   A 1 96  ? 20.541  27.076  1.742   0.34 17.90 ?  81   VAL   A CG2   1 
ATOM   417  N  N     . SER   A 1 97  ? 20.453  25.478  4.456   1.00 19.27 ?  82   SER   A N     1 
ATOM   418  C  CA    . SER   A 1 97  ? 19.461  25.398  5.539   1.00 18.59 ?  82   SER   A CA    1 
ATOM   419  C  C     . SER   A 1 97  ? 18.220  26.252  5.254   1.00 20.21 ?  82   SER   A C     1 
ATOM   420  O  O     . SER   A 1 97  ? 18.323  27.350  4.701   1.00 20.10 ?  82   SER   A O     1 
ATOM   421  C  CB    . SER   A 1 97  ? 20.069  25.813  6.889   1.00 19.68 ?  82   SER   A CB    1 
ATOM   422  O  OG    . SER   A 1 97  ? 20.632  27.127  6.882   1.00 19.64 ?  82   SER   A OG    1 
ATOM   423  N  N     . SER   A 1 98  ? 17.047  25.744  5.672   1.00 18.13 ?  83   SER   A N     1 
ATOM   424  C  CA    . SER   A 1 98  ? 15.758  26.391  5.388   1.00 16.66 ?  83   SER   A CA    1 
ATOM   425  C  C     . SER   A 1 98  ? 15.638  27.766  6.038   1.00 19.83 ?  83   SER   A C     1 
ATOM   426  O  O     . SER   A 1 98  ? 16.158  28.015  7.128   1.00 20.00 ?  83   SER   A O     1 
ATOM   427  C  CB    . SER   A 1 98  ? 14.592  25.513  5.876   1.00 18.34 ?  83   SER   A CB    1 
ATOM   428  O  OG    . SER   A 1 98  ? 14.458  24.325  5.111   1.00 19.37 ?  83   SER   A OG    1 
ATOM   429  N  N     . ALA   A 1 99  ? 14.866  28.641  5.385   1.00 17.57 ?  84   ALA   A N     1 
ATOM   430  C  CA    . ALA   A 1 99  ? 14.649  30.020  5.858   1.00 17.91 ?  84   ALA   A CA    1 
ATOM   431  C  C     . ALA   A 1 99  ? 13.464  30.064  6.827   1.00 18.06 ?  84   ALA   A C     1 
ATOM   432  O  O     . ALA   A 1 99  ? 12.384  30.580  6.526   1.00 22.65 ?  84   ALA   A O     1 
ATOM   433  C  CB    . ALA   A 1 99  ? 14.444  30.943  4.666   1.00 18.90 ?  84   ALA   A CB    1 
ATOM   434  N  N     . MET   A 1 100 ? 13.677  29.498  8.017   1.00 19.04 ?  85   MET   A N     1 
ATOM   435  C  CA    . MET   A 1 100 ? 12.614  29.277  8.992   1.00 17.54 ?  85   MET   A CA    1 
ATOM   436  C  C     . MET   A 1 100 ? 13.068  29.760  10.371  1.00 20.47 ?  85   MET   A C     1 
ATOM   437  O  O     . MET   A 1 100 ? 14.254  29.666  10.708  1.00 20.30 ?  85   MET   A O     1 
ATOM   438  C  CB    . MET   A 1 100 ? 12.216  27.779  9.056   1.00 18.17 ?  85   MET   A CB    1 
ATOM   439  C  CG    . MET   A 1 100 ? 11.695  27.230  7.714   1.00 19.27 ?  85   MET   A CG    1 
ATOM   440  S  SD    . MET   A 1 100 ? 11.392  25.439  7.634   1.00 19.68 ?  85   MET   A SD    1 
ATOM   441  C  CE    . MET   A 1 100 ? 9.932   25.272  8.681   1.00 20.64 ?  85   MET   A CE    1 
ATOM   442  N  N     . ASP   A 1 101 ? 12.120  30.256  11.182  1.00 21.44 ?  86   ASP   A N     1 
ATOM   443  C  CA    . ASP   A 1 101 ? 12.504  30.844  12.469  1.00 19.60 ?  86   ASP   A CA    1 
ATOM   444  C  C     . ASP   A 1 101 ? 12.798  29.800  13.549  1.00 25.35 ?  86   ASP   A C     1 
ATOM   445  O  O     . ASP   A 1 101 ? 13.171  30.178  14.667  1.00 25.65 ?  86   ASP   A O     1 
ATOM   446  C  CB    . ASP   A 1 101 ? 11.463  31.903  12.937  1.00 23.04 ?  86   ASP   A CB    1 
ATOM   447  C  CG    . ASP   A 1 101 ? 10.075  31.342  13.321  1.00 24.63 ?  86   ASP   A CG    1 
ATOM   448  O  OD1   . ASP   A 1 101 ? 9.820   30.121  13.352  1.00 22.75 ?  86   ASP   A OD1   1 
ATOM   449  O  OD2   . ASP   A 1 101 ? 9.190   32.192  13.620  1.00 26.52 -1 86   ASP   A OD2   1 
ATOM   450  N  N     . THR   A 1 102 ? 12.726  28.504  13.227  1.00 22.63 ?  87   THR   A N     1 
ATOM   451  C  CA    . THR   A 1 102 ? 13.253  27.446  14.084  1.00 23.89 ?  87   THR   A CA    1 
ATOM   452  C  C     . THR   A 1 102 ? 14.426  26.708  13.433  1.00 24.70 ?  87   THR   A C     1 
ATOM   453  O  O     . THR   A 1 102 ? 14.807  25.627  13.900  1.00 25.96 ?  87   THR   A O     1 
ATOM   454  C  CB    . THR   A 1 102 ? 12.146  26.462  14.491  1.00 23.24 ?  87   THR   A CB    1 
ATOM   455  O  OG1   . THR   A 1 102 ? 11.447  25.965  13.336  1.00 23.22 ?  87   THR   A OG1   1 
ATOM   456  C  CG2   . THR   A 1 102 ? 11.142  27.149  15.414  1.00 25.48 ?  87   THR   A CG2   1 
ATOM   457  N  N     . VAL   A 1 103 ? 15.030  27.281  12.386  1.00 20.31 ?  88   VAL   A N     1 
ATOM   458  C  CA    . VAL   A 1 103 ? 16.168  26.628  11.728  1.00 20.80 ?  88   VAL   A CA    1 
ATOM   459  C  C     . VAL   A 1 103 ? 17.373  27.557  11.532  1.00 21.03 ?  88   VAL   A C     1 
ATOM   460  O  O     . VAL   A 1 103 ? 18.488  27.195  11.932  1.00 21.35 ?  88   VAL   A O     1 
ATOM   461  C  CB    . VAL   A 1 103 ? 15.757  25.992  10.379  1.00 19.53 ?  88   VAL   A CB    1 
ATOM   462  C  CG1   . VAL   A 1 103 ? 16.953  25.245  9.746   1.00 19.49 ?  88   VAL   A CG1   1 
ATOM   463  C  CG2   . VAL   A 1 103 ? 14.586  25.024  10.559  1.00 20.59 ?  88   VAL   A CG2   1 
ATOM   464  N  N     . THR   A 1 104 ? 17.207  28.740  10.909  1.00 21.39 ?  89   THR   A N     1 
ATOM   465  C  CA    . THR   A 1 104 ? 18.368  29.551  10.503  1.00 19.68 ?  89   THR   A CA    1 
ATOM   466  C  C     . THR   A 1 104 ? 18.320  30.995  11.009  1.00 22.29 ?  89   THR   A C     1 
ATOM   467  O  O     . THR   A 1 104 ? 17.613  31.833  10.436  1.00 22.46 ?  89   THR   A O     1 
ATOM   468  C  CB    . THR   A 1 104 ? 18.536  29.562  8.976   1.00 18.42 ?  89   THR   A CB    1 
ATOM   469  O  OG1   . THR   A 1 104 ? 18.544  28.211  8.475   1.00 19.24 ?  89   THR   A OG1   1 
ATOM   470  C  CG2   . THR   A 1 104 ? 19.859  30.245  8.594   1.00 20.41 ?  89   THR   A CG2   1 
ATOM   471  N  N     . GLU   A 1 105 ? 19.136  31.298  12.034  1.00 21.97 ?  90   GLU   A N     1 
ATOM   472  C  CA    . GLU   A 1 105 ? 19.615  32.659  12.295  1.00 21.63 ?  90   GLU   A CA    1 
ATOM   473  C  C     . GLU   A 1 105 ? 21.144  32.678  12.198  1.00 25.29 ?  90   GLU   A C     1 
ATOM   474  O  O     . GLU   A 1 105 ? 21.729  31.804  11.549  1.00 23.41 ?  90   GLU   A O     1 
ATOM   475  C  CB    . GLU   A 1 105 ? 19.106  33.170  13.651  1.00 23.23 ?  90   GLU   A CB    1 
ATOM   476  C  CG    . GLU   A 1 105 ? 17.587  33.328  13.647  1.00 24.99 ?  90   GLU   A CG    1 
ATOM   477  C  CD    . GLU   A 1 105 ? 16.988  33.893  14.927  1.00 34.84 ?  90   GLU   A CD    1 
ATOM   478  O  OE1   . GLU   A 1 105 ? 17.681  33.934  15.966  1.00 37.13 ?  90   GLU   A OE1   1 
ATOM   479  O  OE2   . GLU   A 1 105 ? 15.795  34.275  14.889  1.00 32.61 -1 90   GLU   A OE2   1 
ATOM   480  N  N     . SER   A 1 106 ? 21.818  33.654  12.825  1.00 27.02 ?  91   SER   A N     1 
ATOM   481  C  CA    . SER   A 1 106 ? 23.234  33.865  12.517  1.00 24.84 ?  91   SER   A CA    1 
ATOM   482  C  C     . SER   A 1 106 ? 24.108  32.655  12.877  1.00 23.61 ?  91   SER   A C     1 
ATOM   483  O  O     . SER   A 1 106 ? 25.051  32.330  12.144  1.00 24.87 ?  91   SER   A O     1 
ATOM   484  C  CB    . SER   A 1 106 ? 23.744  35.140  13.213  1.00 30.24 ?  91   SER   A CB    1 
ATOM   485  O  OG    . SER   A 1 106 ? 23.658  35.028  14.624  1.00 31.20 ?  91   SER   A OG    1 
ATOM   486  N  N     . ARG   A 1 107 ? 23.826  31.970  13.991  1.00 24.77 ?  92   ARG   A N     1 
ATOM   487  C  CA    . ARG   A 1 107 ? 24.702  30.864  14.397  1.00 23.89 ?  92   ARG   A CA    1 
ATOM   488  C  C     . ARG   A 1 107 ? 24.645  29.695  13.415  1.00 25.03 ?  92   ARG   A C     1 
ATOM   489  O  O     . ARG   A 1 107 ? 25.671  29.058  13.139  1.00 25.09 ?  92   ARG   A O     1 
ATOM   490  C  CB    . ARG   A 1 107 ? 24.353  30.387  15.806  1.00 29.03 ?  92   ARG   A CB    1 
ATOM   491  C  CG    . ARG   A 1 107 ? 25.232  31.026  16.877  1.00 45.69 ?  92   ARG   A CG    1 
ATOM   492  C  CD    . ARG   A 1 107 ? 24.844  30.594  18.279  1.00 51.53 ?  92   ARG   A CD    1 
ATOM   493  N  NE    . ARG   A 1 107 ? 24.816  29.143  18.427  1.00 51.72 ?  92   ARG   A NE    1 
ATOM   494  C  CZ    . ARG   A 1 107 ? 24.915  28.518  19.595  1.00 60.17 ?  92   ARG   A CZ    1 
ATOM   495  N  NH1   . ARG   A 1 107 ? 25.063  29.222  20.712  1.00 63.00 ?  92   ARG   A NH1   1 
ATOM   496  N  NH2   . ARG   A 1 107 ? 24.874  27.194  19.650  1.00 52.12 ?  92   ARG   A NH2   1 
ATOM   497  N  N     . MET   A 1 108 ? 23.453  29.386  12.892  1.00 25.28 ?  93   MET   A N     1 
ATOM   498  C  CA    . MET   A 1 108 ? 23.335  28.329  11.888  1.00 21.16 ?  93   MET   A CA    1 
ATOM   499  C  C     . MET   A 1 108 ? 23.990  28.732  10.572  1.00 20.10 ?  93   MET   A C     1 
ATOM   500  O  O     . MET   A 1 108 ? 24.626  27.900  9.907   1.00 22.22 ?  93   MET   A O     1 
ATOM   501  C  CB    . MET   A 1 108 ? 21.851  27.982  11.674  1.00 20.86 ?  93   MET   A CB    1 
ATOM   502  C  CG    . MET   A 1 108 ? 21.559  27.014  10.505  1.00 22.58 ?  93   MET   A CG    1 
ATOM   503  S  SD    . MET   A 1 108 ? 22.132  25.310  10.768  1.00 22.22 ?  93   MET   A SD    1 
ATOM   504  C  CE    . MET   A 1 108 ? 20.966  24.719  11.995  1.00 24.74 ?  93   MET   A CE    1 
ATOM   505  N  N     . ALA   A 1 109 ? 23.843  30.001  10.161  1.00 20.67 ?  94   ALA   A N     1 
ATOM   506  C  CA    . ALA   A 1 109 ? 24.452  30.424  8.903   1.00 20.82 ?  94   ALA   A CA    1 
ATOM   507  C  C     . ALA   A 1 109 ? 25.977  30.355  8.974   1.00 22.29 ?  94   ALA   A C     1 
ATOM   508  O  O     . ALA   A 1 109 ? 26.635  29.962  8.002   1.00 21.60 ?  94   ALA   A O     1 
ATOM   509  C  CB    . ALA   A 1 109 ? 23.981  31.834  8.528   1.00 23.08 ?  94   ALA   A CB    1 
ATOM   510  N  N     . ILE   A 1 110 ? 26.562  30.728  10.118  1.00 24.28 ?  95   ILE   A N     1 
ATOM   511  C  CA    . ILE   A 1 110 ? 28.016  30.648  10.253  1.00 23.10 ?  95   ILE   A CA    1 
ATOM   512  C  C     . ILE   A 1 110 ? 28.480  29.193  10.175  1.00 22.18 ?  95   ILE   A C     1 
ATOM   513  O  O     . ILE   A 1 110 ? 29.446  28.868  9.474   1.00 24.50 ?  95   ILE   A O     1 
ATOM   514  C  CB    . ILE   A 1 110 ? 28.462  31.324  11.565  1.00 24.26 ?  95   ILE   A CB    1 
ATOM   515  C  CG1   . ILE   A 1 110 ? 28.279  32.841  11.476  1.00 25.70 ?  95   ILE   A CG1   1 
ATOM   516  C  CG2   . ILE   A 1 110 ? 29.939  31.018  11.856  1.00 26.62 ?  95   ILE   A CG2   1 
ATOM   517  C  CD1   . ILE   A 1 110 ? 28.331  33.539  12.812  1.00 28.82 ?  95   ILE   A CD1   1 
ATOM   518  N  N     . ALA   A 1 111 ? 27.790  28.295  10.875  1.00 26.97 ?  96   ALA   A N     1 
ATOM   519  C  CA    . ALA   A 1 111 ? 28.200  26.890  10.903  1.00 24.10 ?  96   ALA   A CA    1 
ATOM   520  C  C     . ALA   A 1 111 ? 28.033  26.218  9.540   1.00 24.52 ?  96   ALA   A C     1 
ATOM   521  O  O     . ALA   A 1 111 ? 28.875  25.405  9.136   1.00 23.96 ?  96   ALA   A O     1 
ATOM   522  C  CB    . ALA   A 1 111 ? 27.398  26.150  11.969  1.00 25.95 ?  96   ALA   A CB    1 
ATOM   523  N  N     . MET   A 1 112 ? 26.945  26.532  8.823   1.00 23.03 ?  97   MET   A N     1 
ATOM   524  C  CA    . MET   A 1 112 ? 26.748  25.972  7.485   1.00 20.82 ?  97   MET   A CA    1 
ATOM   525  C  C     . MET   A 1 112 ? 27.849  26.410  6.522   1.00 23.79 ?  97   MET   A C     1 
ATOM   526  O  O     . MET   A 1 112 ? 28.354  25.597  5.740   1.00 22.45 ?  97   MET   A O     1 
ATOM   527  C  CB    . MET   A 1 112 ? 25.373  26.379  6.933   1.00 20.22 ?  97   MET   A CB    1 
ATOM   528  C  CG    . MET   A 1 112 ? 24.174  25.632  7.539   1.00 19.64 ?  97   MET   A CG    1 
ATOM   529  S  SD    . MET   A 1 112 ? 24.111  23.843  7.170   1.00 21.26 ?  97   MET   A SD    1 
ATOM   530  C  CE    . MET   A 1 112 ? 23.999  23.876  5.369   1.00 22.10 ?  97   MET   A CE    1 
ATOM   531  N  N     . ALA   A 1 113 ? 28.221  27.697  6.540   1.00 23.79 ?  98   ALA   A N     1 
ATOM   532  C  CA    . ALA   A 1 113 ? 29.270  28.166  5.641   1.00 20.82 ?  98   ALA   A CA    1 
ATOM   533  C  C     . ALA   A 1 113 ? 30.618  27.534  5.976   1.00 22.13 ?  98   ALA   A C     1 
ATOM   534  O  O     . ALA   A 1 113 ? 31.373  27.163  5.069   1.00 21.93 ?  98   ALA   A O     1 
ATOM   535  C  CB    . ALA   A 1 113 ? 29.384  29.693  5.689   1.00 22.26 ?  98   ALA   A CB    1 
ATOM   536  N  N     . ARG   A 1 114 ? 30.932  27.381  7.268   1.00 23.02 ?  99   ARG   A N     1 
ATOM   537  C  CA    . ARG   A 1 114 ? 32.194  26.739  7.636   1.00 23.83 ?  99   ARG   A CA    1 
ATOM   538  C  C     . ARG   A 1 114 ? 32.217  25.263  7.250   1.00 28.65 ?  99   ARG   A C     1 
ATOM   539  O  O     . ARG   A 1 114 ? 33.294  24.707  6.982   1.00 27.27 ?  99   ARG   A O     1 
ATOM   540  C  CB    . ARG   A 1 114 ? 32.446  26.916  9.133   1.00 24.21 ?  99   ARG   A CB    1 
ATOM   541  C  CG    . ARG   A 1 114 ? 32.807  28.360  9.507   1.00 26.77 ?  99   ARG   A CG    1 
ATOM   542  C  CD    . ARG   A 1 114 ? 32.993  28.526  11.003  1.00 28.83 ?  99   ARG   A CD    1 
ATOM   543  N  NE    . ARG   A 1 114 ? 33.454  29.875  11.325  1.00 34.47 ?  99   ARG   A NE    1 
ATOM   544  C  CZ    . ARG   A 1 114 ? 33.460  30.396  12.549  1.00 42.40 ?  99   ARG   A CZ    1 
ATOM   545  N  NH1   . ARG   A 1 114 ? 33.018  29.685  13.575  1.00 39.12 ?  99   ARG   A NH1   1 
ATOM   546  N  NH2   . ARG   A 1 114 ? 33.902  31.634  12.744  1.00 41.52 ?  99   ARG   A NH2   1 
ATOM   547  N  N     . ALA   A 1 115 ? 31.052  24.615  7.209   1.00 24.00 ?  100  ALA   A N     1 
ATOM   548  C  CA    . ALA   A 1 115 ? 30.945  23.230  6.778   1.00 23.64 ?  100  ALA   A CA    1 
ATOM   549  C  C     . ALA   A 1 115 ? 30.988  23.072  5.262   1.00 25.40 ?  100  ALA   A C     1 
ATOM   550  O  O     . ALA   A 1 115 ? 31.006  21.932  4.778   1.00 26.68 ?  100  ALA   A O     1 
ATOM   551  C  CB    . ALA   A 1 115 ? 29.655  22.614  7.328   1.00 23.52 ?  100  ALA   A CB    1 
ATOM   552  N  N     . GLY   A 1 116 ? 30.990  24.169  4.507   1.00 22.16 ?  101  GLY   A N     1 
ATOM   553  C  CA    . GLY   A 1 116 ? 31.049  24.109  3.062   1.00 22.13 ?  101  GLY   A CA    1 
ATOM   554  C  C     . GLY   A 1 116 ? 29.728  24.332  2.343   1.00 20.07 ?  101  GLY   A C     1 
ATOM   555  O  O     . GLY   A 1 116 ? 29.720  24.335  1.101   1.00 20.07 ?  101  GLY   A O     1 
ATOM   556  N  N     . GLY   A 1 117 ? 28.635  24.560  3.080   1.00 20.70 ?  102  GLY   A N     1 
ATOM   557  C  CA    . GLY   A 1 117 ? 27.317  24.860  2.515   1.00 20.31 ?  102  GLY   A CA    1 
ATOM   558  C  C     . GLY   A 1 117 ? 26.917  26.320  2.697   1.00 19.03 ?  102  GLY   A C     1 
ATOM   559  O  O     . GLY   A 1 117 ? 27.779  27.200  2.629   1.00 19.76 ?  102  GLY   A O     1 
ATOM   560  N  N     . MET   A 1 118 ? 25.631  26.608  2.935   1.00 19.52 ?  103  MET   A N     1 
ATOM   561  C  CA    . MET   A 1 118 ? 25.191  27.989  3.166   1.00 19.60 ?  103  MET   A CA    1 
ATOM   562  C  C     . MET   A 1 118 ? 23.887  27.972  3.953   1.00 19.99 ?  103  MET   A C     1 
ATOM   563  O  O     . MET   A 1 118 ? 23.112  27.014  3.872   1.00 19.93 ?  103  MET   A O     1 
ATOM   564  C  CB    . MET   A 1 118 ? 24.989  28.769  1.846   1.00 19.08 ?  103  MET   A CB    1 
ATOM   565  C  CG    . MET   A 1 118 ? 24.982  30.308  1.989   1.00 19.54 ?  103  MET   A CG    1 
ATOM   566  S  SD    . MET   A 1 118 ? 24.535  31.229  0.491   1.00 21.32 ?  103  MET   A SD    1 
ATOM   567  C  CE    . MET   A 1 118 ? 22.757  30.899  0.431   1.00 21.35 ?  103  MET   A CE    1 
ATOM   568  N  N     . GLY   A 1 119 ? 23.624  29.067  4.675   1.00 21.49 ?  104  GLY   A N     1 
ATOM   569  C  CA    . GLY   A 1 119 ? 22.343  29.279  5.337   1.00 18.64 ?  104  GLY   A CA    1 
ATOM   570  C  C     . GLY   A 1 119 ? 21.554  30.389  4.661   1.00 18.92 ?  104  GLY   A C     1 
ATOM   571  O  O     . GLY   A 1 119 ? 22.137  31.323  4.088   1.00 20.81 ?  104  GLY   A O     1 
ATOM   572  N  N     . VAL   A 1 120 ? 20.220  30.295  4.728   1.00 17.90 ?  105  VAL   A N     1 
ATOM   573  C  CA    . VAL   A 1 120 ? 19.318  31.366  4.282   1.00 18.52 ?  105  VAL   A CA    1 
ATOM   574  C  C     . VAL   A 1 120 ? 18.580  31.893  5.514   1.00 19.35 ?  105  VAL   A C     1 
ATOM   575  O  O     . VAL   A 1 120 ? 17.746  31.191  6.095   1.00 19.60 ?  105  VAL   A O     1 
ATOM   576  C  CB    . VAL   A 1 120 ? 18.324  30.888  3.200   1.00 18.75 ?  105  VAL   A CB    1 
ATOM   577  C  CG1   . VAL   A 1 120 ? 17.396  32.056  2.758   1.00 17.90 ?  105  VAL   A CG1   1 
ATOM   578  C  CG2   . VAL   A 1 120 ? 19.057  30.285  1.985   1.00 18.47 ?  105  VAL   A CG2   1 
ATOM   579  N  N     . LEU   A 1 121 ? 18.869  33.139  5.912   1.00 18.52 ?  106  LEU   A N     1 
ATOM   580  C  CA    . LEU   A 1 121 ? 18.231  33.727  7.097   1.00 18.71 ?  106  LEU   A CA    1 
ATOM   581  C  C     . LEU   A 1 121 ? 16.729  33.980  6.901   1.00 21.50 ?  106  LEU   A C     1 
ATOM   582  O  O     . LEU   A 1 121 ? 16.302  34.510  5.872   1.00 22.56 ?  106  LEU   A O     1 
ATOM   583  C  CB    . LEU   A 1 121 ? 18.927  35.052  7.446   1.00 19.19 ?  106  LEU   A CB    1 
ATOM   584  C  CG    . LEU   A 1 121 ? 20.421  35.001  7.774   1.00 19.54 ?  106  LEU   A CG    1 
ATOM   585  C  CD1   . LEU   A 1 121 ? 21.050  36.404  7.688   1.00 25.84 ?  106  LEU   A CD1   1 
ATOM   586  C  CD2   . LEU   A 1 121 ? 20.617  34.428  9.160   1.00 23.29 ?  106  LEU   A CD2   1 
ATOM   587  N  N     . HIS   A 1 122 ? 15.924  33.645  7.921   1.00 19.77 ?  107  HIS   A N     1 
ATOM   588  C  CA    . HIS   A 1 122 ? 14.465  33.790  7.834   1.00 19.67 ?  107  HIS   A CA    1 
ATOM   589  C  C     . HIS   A 1 122 ? 14.054  35.266  7.907   1.00 24.12 ?  107  HIS   A C     1 
ATOM   590  O  O     . HIS   A 1 122 ? 14.841  36.143  8.277   1.00 23.95 ?  107  HIS   A O     1 
ATOM   591  C  CB    . HIS   A 1 122 ? 13.762  32.970  8.930   1.00 22.72 ?  107  HIS   A CB    1 
ATOM   592  C  CG    . HIS   A 1 122 ? 13.835  33.567  10.307  1.00 24.87 ?  107  HIS   A CG    1 
ATOM   593  N  ND1   . HIS   A 1 122 ? 12.889  34.449  10.792  1.00 23.06 ?  107  HIS   A ND1   1 
ATOM   594  C  CD2   . HIS   A 1 122 ? 14.726  33.383  11.312  1.00 26.53 ?  107  HIS   A CD2   1 
ATOM   595  C  CE1   . HIS   A 1 122 ? 13.203  34.795  12.029  1.00 23.93 ?  107  HIS   A CE1   1 
ATOM   596  N  NE2   . HIS   A 1 122 ? 14.311  34.156  12.372  1.00 24.20 ?  107  HIS   A NE2   1 
ATOM   597  N  N     . ARG   A 1 123 ? 12.795  35.539  7.540   1.00 22.57 ?  108  ARG   A N     1 
ATOM   598  C  CA    . ARG   A 1 123 ? 12.310  36.915  7.417   1.00 21.95 ?  108  ARG   A CA    1 
ATOM   599  C  C     . ARG   A 1 123 ? 11.161  37.243  8.371   1.00 24.25 ?  108  ARG   A C     1 
ATOM   600  O  O     . ARG   A 1 123 ? 10.442  38.231  8.152   1.00 25.16 ?  108  ARG   A O     1 
ATOM   601  C  CB    . ARG   A 1 123 ? 11.899  37.212  5.970   1.00 21.43 ?  108  ARG   A CB    1 
ATOM   602  C  CG    . ARG   A 1 123 ? 10.729  36.355  5.429   1.00 22.55 ?  108  ARG   A CG    1 
ATOM   603  C  CD    . ARG   A 1 123 ? 10.419  36.739  3.974   1.00 21.40 ?  108  ARG   A CD    1 
ATOM   604  N  NE    . ARG   A 1 123 ? 9.373   35.932  3.329   1.00 21.28 ?  108  ARG   A NE    1 
ATOM   605  C  CZ    . ARG   A 1 123 ? 8.099   36.298  3.230   1.00 26.61 ?  108  ARG   A CZ    1 
ATOM   606  N  NH1   . ARG   A 1 123 ? 7.693   37.445  3.770   1.00 26.04 ?  108  ARG   A NH1   1 
ATOM   607  N  NH2   . ARG   A 1 123 ? 7.220   35.513  2.607   1.00 24.63 ?  108  ARG   A NH2   1 
ATOM   608  N  N     . ASN   A 1 124 ? 10.983  36.467  9.439   1.00 22.27 ?  109  ASN   A N     1 
ATOM   609  C  CA    . ASN   A 1 124 ? 9.923   36.712  10.427  1.00 23.44 ?  109  ASN   A CA    1 
ATOM   610  C  C     . ASN   A 1 124 ? 10.462  37.537  11.602  1.00 27.71 ?  109  ASN   A C     1 
ATOM   611  O  O     . ASN   A 1 124 ? 10.416  37.136  12.770  1.00 31.51 ?  109  ASN   A O     1 
ATOM   612  C  CB    . ASN   A 1 124 ? 9.338   35.381  10.899  1.00 25.97 ?  109  ASN   A CB    1 
ATOM   613  C  CG    . ASN   A 1 124 ? 7.966   35.520  11.525  1.00 30.36 ?  109  ASN   A CG    1 
ATOM   614  O  OD1   . ASN   A 1 124 ? 7.242   36.476  11.256  1.00 32.45 ?  109  ASN   A OD1   1 
ATOM   615  N  ND2   . ASN   A 1 124 ? 7.590   34.546  12.357  1.00 28.29 ?  109  ASN   A ND2   1 
ATOM   616  N  N     . LEU   A 1 125 ? 10.994  38.711  11.266  1.00 27.75 ?  110  LEU   A N     1 
ATOM   617  C  CA    . LEU   A 1 125 ? 11.571  39.627  12.246  1.00 31.68 ?  110  LEU   A CA    1 
ATOM   618  C  C     . LEU   A 1 125 ? 11.785  40.992  11.603  1.00 33.11 ?  110  LEU   A C     1 
ATOM   619  O  O     . LEU   A 1 125 ? 11.715  41.119  10.374  1.00 31.49 ?  110  LEU   A O     1 
ATOM   620  C  CB    . LEU   A 1 125 ? 12.891  39.071  12.801  1.00 30.30 ?  110  LEU   A CB    1 
ATOM   621  C  CG    . LEU   A 1 125 ? 14.165  39.132  11.944  1.00 30.28 ?  110  LEU   A CG    1 
ATOM   622  C  CD1   . LEU   A 1 125 ? 15.342  38.497  12.683  1.00 32.45 ?  110  LEU   A CD1   1 
ATOM   623  C  CD2   . LEU   A 1 125 ? 13.997  38.481  10.568  1.00 27.65 ?  110  LEU   A CD2   1 
ATOM   624  N  N     . PRO   A 1 126 ? 12.046  42.038  12.387  1.00 34.26 ?  111  PRO   A N     1 
ATOM   625  C  CA    . PRO   A 1 126 ? 12.194  43.374  11.797  1.00 32.25 ?  111  PRO   A CA    1 
ATOM   626  C  C     . PRO   A 1 126 ? 13.343  43.444  10.803  1.00 30.52 ?  111  PRO   A C     1 
ATOM   627  O  O     . PRO   A 1 126 ? 14.334  42.714  10.903  1.00 30.85 ?  111  PRO   A O     1 
ATOM   628  C  CB    . PRO   A 1 126 ? 12.456  44.272  13.014  1.00 35.17 ?  111  PRO   A CB    1 
ATOM   629  C  CG    . PRO   A 1 126 ? 11.880  43.532  14.165  1.00 36.51 ?  111  PRO   A CG    1 
ATOM   630  C  CD    . PRO   A 1 126 ? 12.136  42.074  13.854  1.00 35.74 ?  111  PRO   A CD    1 
ATOM   631  N  N     . VAL   A 1 127 ? 13.207  44.366  9.844   1.00 28.05 ?  112  VAL   A N     1 
ATOM   632  C  CA    . VAL   A 1 127 ? 14.238  44.553  8.822   1.00 29.81 ?  112  VAL   A CA    1 
ATOM   633  C  C     . VAL   A 1 127 ? 15.600  44.819  9.465   1.00 28.90 ?  112  VAL   A C     1 
ATOM   634  O  O     . VAL   A 1 127 ? 16.618  44.233  9.076   1.00 26.92 ?  112  VAL   A O     1 
ATOM   635  C  CB    . VAL   A 1 127 ? 13.840  45.692  7.863   1.00 29.31 ?  112  VAL   A CB    1 
ATOM   636  C  CG1   . VAL   A 1 127 ? 15.013  46.080  6.965   1.00 27.66 ?  112  VAL   A CG1   1 
ATOM   637  C  CG2   . VAL   A 1 127 ? 12.628  45.297  7.035   1.00 31.33 ?  112  VAL   A CG2   1 
ATOM   638  N  N     . ALA   A 1 128 ? 15.646  45.729  10.445  1.00 31.00 ?  113  ALA   A N     1 
ATOM   639  C  CA    . ALA   A 1 128 ? 16.928  46.070  11.058  1.00 29.82 ?  113  ALA   A CA    1 
ATOM   640  C  C     . ALA   A 1 128 ? 17.589  44.872  11.726  1.00 27.64 ?  113  ALA   A C     1 
ATOM   641  O  O     . ALA   A 1 128 ? 18.821  44.773  11.727  1.00 32.42 ?  113  ALA   A O     1 
ATOM   642  C  CB    . ALA   A 1 128 ? 16.744  47.200  12.074  1.00 33.50 ?  113  ALA   A CB    1 
ATOM   643  N  N     . GLU   A 1 129 ? 16.800  43.956  12.298  1.00 30.25 ?  114  GLU   A N     1 
ATOM   644  C  CA    . GLU   A 1 129 ? 17.382  42.776  12.934  1.00 33.59 ?  114  GLU   A CA    1 
ATOM   645  C  C     . GLU   A 1 129 ? 17.907  41.788  11.901  1.00 31.07 ?  114  GLU   A C     1 
ATOM   646  O  O     . GLU   A 1 129 ? 18.973  41.197  12.093  1.00 27.93 ?  114  GLU   A O     1 
ATOM   647  C  CB    . GLU   A 1 129 ? 16.362  42.084  13.835  1.00 35.59 ?  114  GLU   A CB    1 
ATOM   648  C  CG    . GLU   A 1 129 ? 16.096  42.774  15.154  1.00 42.79 ?  114  GLU   A CG    1 
ATOM   649  C  CD    . GLU   A 1 129 ? 15.251  41.925  16.087  1.00 48.97 ?  114  GLU   A CD    1 
ATOM   650  O  OE1   . GLU   A 1 129 ? 15.445  40.688  16.119  1.00 51.61 ?  114  GLU   A OE1   1 
ATOM   651  O  OE2   . GLU   A 1 129 ? 14.390  42.498  16.787  1.00 54.69 -1 114  GLU   A OE2   1 
ATOM   652  N  N     . GLN   A 1 130 ? 17.172  41.584  10.802  1.00 30.19 ?  115  GLN   A N     1 
ATOM   653  C  CA    . GLN   A 1 130 ? 17.649  40.660  9.774   1.00 25.36 ?  115  GLN   A CA    1 
ATOM   654  C  C     . GLN   A 1 130 ? 18.940  41.170  9.140   1.00 31.45 ?  115  GLN   A C     1 
ATOM   655  O  O     . GLN   A 1 130 ? 19.876  40.395  8.904   1.00 29.41 ?  115  GLN   A O     1 
ATOM   656  C  CB    . GLN   A 1 130 ? 16.562  40.441  8.708   1.00 24.50 ?  115  GLN   A CB    1 
ATOM   657  C  CG    . GLN   A 1 130 ? 16.815  39.202  7.793   1.00 24.00 ?  115  GLN   A CG    1 
ATOM   658  C  CD    . GLN   A 1 130 ? 15.843  39.132  6.614   1.00 24.68 ?  115  GLN   A CD    1 
ATOM   659  O  OE1   . GLN   A 1 130 ? 15.237  40.139  6.239   1.00 24.97 ?  115  GLN   A OE1   1 
ATOM   660  N  NE2   . GLN   A 1 130 ? 15.707  37.940  6.010   1.00 23.25 ?  115  GLN   A NE2   1 
ATOM   661  N  N     . ALA   A 1 131 ? 19.017  42.482  8.876   1.00 24.24 ?  116  ALA   A N     1 
ATOM   662  C  CA    . ALA   A 1 131 ? 20.235  43.059  8.307   1.00 28.59 ?  116  ALA   A CA    1 
ATOM   663  C  C     . ALA   A 1 131 ? 21.411  42.939  9.274   1.00 25.74 ?  116  ALA   A C     1 
ATOM   664  O  O     . ALA   A 1 131 ? 22.557  42.722  8.853   1.00 27.90 ?  116  ALA   A O     1 
ATOM   665  C  CB    . ALA   A 1 131 ? 19.990  44.526  7.926   1.00 25.91 ?  116  ALA   A CB    1 
ATOM   666  N  N     . GLY   A 1 132 ? 21.146  43.069  10.575  1.00 29.21 ?  117  GLY   A N     1 
ATOM   667  C  CA    . GLY   A 1 132 ? 22.203  42.899  11.563  1.00 31.74 ?  117  GLY   A CA    1 
ATOM   668  C  C     . GLY   A 1 132 ? 22.727  41.479  11.667  1.00 32.45 ?  117  GLY   A C     1 
ATOM   669  O  O     . GLY   A 1 132 ? 23.910  41.268  11.965  1.00 33.69 ?  117  GLY   A O     1 
ATOM   670  N  N     . GLN   A 1 133 ? 21.876  40.488  11.411  1.00 29.97 ?  118  GLN   A N     1 
ATOM   671  C  CA    . GLN   A 1 133 ? 22.359  39.112  11.412  1.00 29.87 ?  118  GLN   A CA    1 
ATOM   672  C  C     . GLN   A 1 133 ? 23.253  38.842  10.212  1.00 28.34 ?  118  GLN   A C     1 
ATOM   673  O  O     . GLN   A 1 133 ? 24.201  38.055  10.319  1.00 29.34 ?  118  GLN   A O     1 
ATOM   674  C  CB    . GLN   A 1 133 ? 21.180  38.140  11.459  1.00 27.68 ?  118  GLN   A CB    1 
ATOM   675  C  CG    . GLN   A 1 133 ? 20.381  38.269  12.738  1.00 32.87 ?  118  GLN   A CG    1 
ATOM   676  C  CD    . GLN   A 1 133 ? 19.598  37.036  13.083  1.00 41.70 ?  118  GLN   A CD    1 
ATOM   677  O  OE1   . GLN   A 1 133 ? 19.765  35.984  12.460  1.00 44.25 ?  118  GLN   A OE1   1 
ATOM   678  N  NE2   . GLN   A 1 133 ? 18.734  37.149  14.088  1.00 40.83 ?  118  GLN   A NE2   1 
ATOM   679  N  N     . VAL   A 1 134 ? 22.981  39.489  9.073   1.00 24.40 ?  119  VAL   A N     1 
ATOM   680  C  CA    . VAL   A 1 134 ? 23.893  39.425  7.936   1.00 25.64 ?  119  VAL   A CA    1 
ATOM   681  C  C     . VAL   A 1 134 ? 25.268  39.963  8.328   1.00 33.16 ?  119  VAL   A C     1 
ATOM   682  O  O     . VAL   A 1 134 ? 26.304  39.382  7.981   1.00 29.21 ?  119  VAL   A O     1 
ATOM   683  C  CB    . VAL   A 1 134 ? 23.308  40.188  6.729   1.00 25.17 ?  119  VAL   A CB    1 
ATOM   684  C  CG1   . VAL   A 1 134 ? 24.345  40.309  5.618   1.00 25.68 ?  119  VAL   A CG1   1 
ATOM   685  C  CG2   . VAL   A 1 134 ? 22.049  39.496  6.184   1.00 23.81 ?  119  VAL   A CG2   1 
ATOM   686  N  N     . GLU   A 1 135 ? 25.305  41.081  9.060   1.00 32.36 ?  120  GLU   A N     1 
ATOM   687  C  CA    . GLU   A 1 135 ? 26.599  41.646  9.443   1.00 34.46 ?  120  GLU   A CA    1 
ATOM   688  C  C     . GLU   A 1 135 ? 27.356  40.721  10.390  1.00 34.21 ?  120  GLU   A C     1 
ATOM   689  O  O     . GLU   A 1 135 ? 28.572  40.545  10.251  1.00 38.34 ?  120  GLU   A O     1 
ATOM   690  C  CB    . GLU   A 1 135 ? 26.416  43.029  10.069  1.00 38.88 ?  120  GLU   A CB    1 
ATOM   691  C  CG    . GLU   A 1 135 ? 25.944  44.088  9.083   1.00 40.53 ?  120  GLU   A CG    1 
ATOM   692  C  CD    . GLU   A 1 135 ? 25.993  45.492  9.663   1.00 59.24 ?  120  GLU   A CD    1 
ATOM   693  O  OE1   . GLU   A 1 135 ? 26.583  45.667  10.754  1.00 58.48 ?  120  GLU   A OE1   1 
ATOM   694  O  OE2   . GLU   A 1 135 ? 25.444  46.419  9.026   1.00 56.70 -1 120  GLU   A OE2   1 
ATOM   695  N  N     . MET   A 1 136 ? 26.659  40.114  11.353  1.00 32.71 ?  121  MET   A N     1 
ATOM   696  C  CA    . MET   A 1 136 ? 27.325  39.182  12.256  1.00 35.70 ?  121  MET   A CA    1 
ATOM   697  C  C     . MET   A 1 136 ? 27.987  38.043  11.489  1.00 37.73 ?  121  MET   A C     1 
ATOM   698  O  O     . MET   A 1 136 ? 29.094  37.613  11.838  1.00 38.00 ?  121  MET   A O     1 
ATOM   699  C  CB    . MET   A 1 136 ? 26.336  38.627  13.275  1.00 42.47 ?  121  MET   A CB    1 
ATOM   700  C  CG    . MET   A 1 136 ? 25.634  39.677  14.101  1.00 43.82 ?  121  MET   A CG    1 
ATOM   701  S  SD    . MET   A 1 136 ? 24.517  38.914  15.286  1.00 63.24 ?  121  MET   A SD    1 
ATOM   702  C  CE    . MET   A 1 136 ? 23.322  40.229  15.519  1.00 57.13 ?  121  MET   A CE    1 
ATOM   703  N  N     . VAL   A 1 137 ? 27.321  37.526  10.451  1.00 33.90 ?  122  VAL   A N     1 
ATOM   704  C  CA    . VAL   A 1 137 ? 27.925  36.452  9.667   1.00 32.11 ?  122  VAL   A CA    1 
ATOM   705  C  C     . VAL   A 1 137 ? 29.161  36.961  8.938   1.00 36.85 ?  122  VAL   A C     1 
ATOM   706  O  O     . VAL   A 1 137 ? 30.193  36.282  8.884   1.00 34.43 ?  122  VAL   A O     1 
ATOM   707  C  CB    . VAL   A 1 137 ? 26.896  35.842  8.692   1.00 29.72 ?  122  VAL   A CB    1 
ATOM   708  C  CG1   . VAL   A 1 137 ? 27.573  34.813  7.790   1.00 30.87 ?  122  VAL   A CG1   1 
ATOM   709  C  CG2   . VAL   A 1 137 ? 25.746  35.212  9.467   1.00 28.58 ?  122  VAL   A CG2   1 
ATOM   710  N  N     . LYS   A 1 138 ? 29.083  38.169  8.375   1.00 37.11 ?  123  LYS   A N     1 
ATOM   711  C  CA    . LYS   A 1 138 ? 30.220  38.722  7.650   1.00 38.35 ?  123  LYS   A CA    1 
ATOM   712  C  C     . LYS   A 1 138 ? 31.391  39.052  8.565   1.00 39.15 ?  123  LYS   A C     1 
ATOM   713  O  O     . LYS   A 1 138 ? 32.535  39.102  8.098   1.00 47.47 ?  123  LYS   A O     1 
ATOM   714  C  CB    . LYS   A 1 138 ? 29.785  39.965  6.874   1.00 37.50 ?  123  LYS   A CB    1 
ATOM   715  C  CG    . LYS   A 1 138 ? 28.939  39.643  5.653   1.00 35.44 ?  123  LYS   A CG    1 
ATOM   716  C  CD    . LYS   A 1 138 ? 29.674  38.668  4.733   1.00 35.21 ?  123  LYS   A CD    1 
ATOM   717  C  CE    . LYS   A 1 138 ? 28.809  38.275  3.543   1.00 32.61 ?  123  LYS   A CE    1 
ATOM   718  N  NZ    . LYS   A 1 138 ? 29.585  37.509  2.519   1.00 31.62 ?  123  LYS   A NZ    1 
ATOM   719  N  N     . ARG   A 1 139 ? 31.142  39.264  9.854   1.00 39.21 ?  124  ARG   A N     1 
ATOM   720  C  CA    . ARG   A 1 139 ? 32.232  39.552  10.777  1.00 40.26 ?  124  ARG   A CA    1 
ATOM   721  C  C     . ARG   A 1 139 ? 32.978  38.302  11.222  1.00 48.25 ?  124  ARG   A C     1 
ATOM   722  O  O     . ARG   A 1 139 ? 34.011  38.425  11.894  1.00 41.04 ?  124  ARG   A O     1 
ATOM   723  C  CB    . ARG   A 1 139 ? 31.687  40.302  11.991  1.00 43.98 ?  124  ARG   A CB    1 
ATOM   724  C  CG    . ARG   A 1 139 ? 31.067  41.644  11.618  1.00 52.93 ?  124  ARG   A CG    1 
ATOM   725  C  CD    . ARG   A 1 139 ? 29.983  42.044  12.596  1.00 56.06 ?  124  ARG   A CD    1 
ATOM   726  N  NE    . ARG   A 1 139 ? 30.538  42.506  13.862  1.00 62.82 ?  124  ARG   A NE    1 
ATOM   727  C  CZ    . ARG   A 1 139 ? 29.860  42.537  15.004  1.00 68.24 ?  124  ARG   A CZ    1 
ATOM   728  N  NH1   . ARG   A 1 139 ? 28.600  42.120  15.041  1.00 62.39 ?  124  ARG   A NH1   1 
ATOM   729  N  NH2   . ARG   A 1 139 ? 30.446  42.979  16.110  1.00 66.56 ?  124  ARG   A NH2   1 
ATOM   730  N  N     . SER   A 1 140 ? 32.494  37.114  10.854  1.00 42.05 ?  125  SER   A N     1 
ATOM   731  C  CA    . SER   A 1 140 ? 33.127  35.850  11.206  1.00 37.98 ?  125  SER   A CA    1 
ATOM   732  C  C     . SER   A 1 140 ? 33.938  35.260  10.056  1.00 41.80 ?  125  SER   A C     1 
ATOM   733  O  O     . SER   A 1 140 ? 34.103  34.038  9.982   1.00 46.22 ?  125  SER   A O     1 
ATOM   734  C  CB    . SER   A 1 140 ? 32.078  34.841  11.675  1.00 42.56 ?  125  SER   A CB    1 
ATOM   735  O  OG    . SER   A 1 140 ? 31.357  35.327  12.794  1.00 48.02 ?  125  SER   A OG    1 
ATOM   736  N  N     . GLY   A 1 141 ? 34.434  36.096  9.147   1.00 41.71 ?  126  GLY   A N     1 
ATOM   737  C  CA    . GLY   A 1 141 ? 35.341  35.617  8.120   1.00 43.69 ?  126  GLY   A CA    1 
ATOM   738  C  C     . GLY   A 1 141 ? 34.922  35.822  6.676   1.00 42.55 ?  126  GLY   A C     1 
ATOM   739  O  O     . GLY   A 1 141 ? 35.462  35.166  5.780   1.00 42.76 ?  126  GLY   A O     1 
ATOM   740  N  N     . GLY   A 1 142 ? 33.988  36.731  6.419   1.00 44.71 ?  127  GLY   A N     1 
ATOM   741  C  CA    . GLY   A 1 142 ? 33.546  36.920  5.043   1.00 48.55 ?  127  GLY   A CA    1 
ATOM   742  C  C     . GLY   A 1 142 ? 32.907  35.681  4.450   1.00 45.86 ?  127  GLY   A C     1 
ATOM   743  O  O     . GLY   A 1 142 ? 33.048  35.417  3.249   1.00 49.00 ?  127  GLY   A O     1 
ATOM   744  N  N     . LEU   A 1 143 ? 32.220  34.906  5.279   1.00 38.73 ?  253  LEU   A N     1 
ATOM   745  C  CA    . LEU   A 1 143 ? 31.522  33.706  4.840   1.00 30.53 ?  253  LEU   A CA    1 
ATOM   746  C  C     . LEU   A 1 143 ? 30.347  34.060  3.925   1.00 28.42 ?  253  LEU   A C     1 
ATOM   747  O  O     . LEU   A 1 143 ? 29.793  35.159  3.997   1.00 30.30 ?  253  LEU   A O     1 
ATOM   748  C  CB    . LEU   A 1 143 ? 31.028  32.951  6.072   1.00 28.83 ?  253  LEU   A CB    1 
ATOM   749  C  CG    . LEU   A 1 143 ? 32.121  32.584  7.084   1.00 32.12 ?  253  LEU   A CG    1 
ATOM   750  C  CD1   . LEU   A 1 143 ? 31.512  32.214  8.432   1.00 30.41 ?  253  LEU   A CD1   1 
ATOM   751  C  CD2   . LEU   A 1 143 ? 32.968  31.436  6.538   1.00 33.00 ?  253  LEU   A CD2   1 
ATOM   752  N  N     . LEU   A 1 144 ? 29.962  33.112  3.060   1.00 28.07 ?  254  LEU   A N     1 
ATOM   753  C  CA    . LEU   A 1 144 ? 28.764  33.274  2.230   1.00 24.51 ?  254  LEU   A CA    1 
ATOM   754  C  C     . LEU   A 1 144 ? 27.491  33.233  3.078   1.00 25.23 ?  254  LEU   A C     1 
ATOM   755  O  O     . LEU   A 1 144 ? 27.402  32.460  4.037   1.00 23.54 ?  254  LEU   A O     1 
ATOM   756  C  CB    . LEU   A 1 144 ? 28.685  32.157  1.183   1.00 26.13 ?  254  LEU   A CB    1 
ATOM   757  C  CG    . LEU   A 1 144 ? 29.619  32.115  -0.020  1.00 30.32 ?  254  LEU   A CG    1 
ATOM   758  C  CD1   . LEU   A 1 144 ? 29.542  30.731  -0.678  1.00 32.80 ?  254  LEU   A CD1   1 
ATOM   759  C  CD2   . LEU   A 1 144 ? 29.236  33.193  -1.010  1.00 31.81 ?  254  LEU   A CD2   1 
ATOM   760  N  N     . VAL   A 1 145 ? 26.482  34.038  2.698   1.00 22.21 ?  255  VAL   A N     1 
ATOM   761  C  CA    . VAL   A 1 145 ? 25.190  34.027  3.393   1.00 22.43 ?  255  VAL   A CA    1 
ATOM   762  C  C     . VAL   A 1 145 ? 24.072  34.483  2.453   1.00 20.66 ?  255  VAL   A C     1 
ATOM   763  O  O     . VAL   A 1 145 ? 24.278  35.313  1.566   1.00 21.61 ?  255  VAL   A O     1 
ATOM   764  C  CB    . VAL   A 1 145 ? 25.220  34.901  4.675   1.00 20.90 ?  255  VAL   A CB    1 
ATOM   765  C  CG1   . VAL   A 1 145 ? 25.367  36.401  4.330   1.00 23.38 ?  255  VAL   A CG1   1 
ATOM   766  C  CG2   . VAL   A 1 145 ? 23.983  34.655  5.528   1.00 22.14 ?  255  VAL   A CG2   1 
ATOM   767  N  N     . GLY   A 1 146 ? 22.873  33.911  2.649   1.00 18.98 ?  256  GLY   A N     1 
ATOM   768  C  CA    . GLY   A 1 146 ? 21.667  34.368  1.986   1.00 18.28 ?  256  GLY   A CA    1 
ATOM   769  C  C     . GLY   A 1 146 ? 20.585  34.831  2.960   1.00 16.61 ?  256  GLY   A C     1 
ATOM   770  O  O     . GLY   A 1 146 ? 20.680  34.630  4.179   1.00 19.46 ?  256  GLY   A O     1 
ATOM   771  N  N     . ALA   A 1 147 ? 19.546  35.471  2.408   1.00 17.27 ?  257  ALA   A N     1 
ATOM   772  C  CA    . ALA   A 1 147 ? 18.433  35.966  3.219   1.00 18.20 ?  257  ALA   A CA    1 
ATOM   773  C  C     . ALA   A 1 147 ? 17.139  36.013  2.405   1.00 17.38 ?  257  ALA   A C     1 
ATOM   774  O  O     . ALA   A 1 147 ? 17.159  36.375  1.225   1.00 18.91 ?  257  ALA   A O     1 
ATOM   775  C  CB    . ALA   A 1 147 ? 18.734  37.367  3.793   1.00 19.05 ?  257  ALA   A CB    1 
ATOM   776  N  N     . ALA   A 1 148 ? 16.022  35.627  3.045   1.00 19.14 ?  258  ALA   A N     1 
ATOM   777  C  CA    . ALA   A 1 148 ? 14.698  35.613  2.417   1.00 17.91 ?  258  ALA   A CA    1 
ATOM   778  C  C     . ALA   A 1 148 ? 14.018  36.985  2.412   1.00 18.12 ?  258  ALA   A C     1 
ATOM   779  O  O     . ALA   A 1 148 ? 14.126  37.757  3.370   1.00 19.68 ?  258  ALA   A O     1 
ATOM   780  C  CB    . ALA   A 1 148 ? 13.784  34.620  3.142   1.00 20.10 ?  258  ALA   A CB    1 
ATOM   781  N  N     . VAL   A 1 149 ? 13.263  37.262  1.337   1.00 18.48 ?  259  VAL   A N     1 
ATOM   782  C  CA    . VAL   A 1 149 ? 12.355  38.413  1.273   1.00 20.84 ?  259  VAL   A CA    1 
ATOM   783  C  C     . VAL   A 1 149 ? 11.042  37.986  0.614   1.00 20.79 ?  259  VAL   A C     1 
ATOM   784  O  O     . VAL   A 1 149 ? 10.984  36.996  -0.122  1.00 21.27 ?  259  VAL   A O     1 
ATOM   785  C  CB    . VAL   A 1 149 ? 12.957  39.621  0.499   1.00 20.97 ?  259  VAL   A CB    1 
ATOM   786  C  CG1   . VAL   A 1 149 ? 14.300  40.057  1.089   1.00 21.12 ?  259  VAL   A CG1   1 
ATOM   787  C  CG2   . VAL   A 1 149 ? 13.091  39.305  -0.991  1.00 19.90 ?  259  VAL   A CG2   1 
ATOM   788  N  N     . GLY   A 1 150 ? 9.966   38.747  0.893   1.00 19.06 ?  260  GLY   A N     1 
ATOM   789  C  CA    . GLY   A 1 150 ? 8.655   38.540  0.279   1.00 21.40 ?  260  GLY   A CA    1 
ATOM   790  C  C     . GLY   A 1 150 ? 8.447   39.336  -0.995  1.00 20.33 ?  260  GLY   A C     1 
ATOM   791  O  O     . GLY   A 1 150 ? 9.386   39.584  -1.763  1.00 20.81 ?  260  GLY   A O     1 
ATOM   792  N  N     . VAL   A 1 151 ? 7.198   39.761  -1.222  1.00 23.01 ?  261  VAL   A N     1 
ATOM   793  C  CA    . VAL   A 1 151 ? 6.830   40.508  -2.423  1.00 24.97 ?  261  VAL   A CA    1 
ATOM   794  C  C     . VAL   A 1 151 ? 6.098   41.788  -2.010  1.00 27.56 ?  261  VAL   A C     1 
ATOM   795  O  O     . VAL   A 1 151 ? 5.237   41.754  -1.125  1.00 30.21 ?  261  VAL   A O     1 
ATOM   796  C  CB    . VAL   A 1 151 ? 5.970   39.641  -3.369  1.00 25.30 ?  261  VAL   A CB    1 
ATOM   797  C  CG1   . VAL   A 1 151 ? 5.443   40.463  -4.541  1.00 28.74 ?  261  VAL   A CG1   1 
ATOM   798  C  CG2   . VAL   A 1 151 ? 6.783   38.439  -3.877  1.00 26.36 ?  261  VAL   A CG2   1 
ATOM   799  N  N     . GLY   A 1 152 ? 6.463   42.917  -2.625  1.00 30.29 ?  262  GLY   A N     1 
ATOM   800  C  CA    . GLY   A 1 152 ? 5.793   44.188  -2.381  1.00 30.97 ?  262  GLY   A CA    1 
ATOM   801  C  C     . GLY   A 1 152 ? 6.744   45.281  -1.915  1.00 31.65 ?  262  GLY   A C     1 
ATOM   802  O  O     . GLY   A 1 152 ? 7.968   45.120  -1.888  1.00 28.89 ?  262  GLY   A O     1 
ATOM   803  N  N     . GLY   A 1 153 ? 6.154   46.418  -1.528  1.00 28.72 ?  263  GLY   A N     1 
ATOM   804  C  CA    . GLY   A 1 153 ? 6.965   47.578  -1.164  1.00 29.60 ?  263  GLY   A CA    1 
ATOM   805  C  C     . GLY   A 1 153 ? 7.811   47.382  0.085   1.00 27.88 ?  263  GLY   A C     1 
ATOM   806  O  O     . GLY   A 1 153 ? 8.989   47.760  0.111   1.00 31.77 ?  263  GLY   A O     1 
ATOM   807  N  N     . ASP   A 1 154 ? 7.231   46.806  1.143   1.00 32.53 ?  264  ASP   A N     1 
ATOM   808  C  CA    . ASP   A 1 154 ? 8.014   46.535  2.351   1.00 30.65 ?  264  ASP   A CA    1 
ATOM   809  C  C     . ASP   A 1 154 ? 9.124   45.516  2.087   1.00 26.44 ?  264  ASP   A C     1 
ATOM   810  O  O     . ASP   A 1 154 ? 10.233  45.639  2.621   1.00 27.07 ?  264  ASP   A O     1 
ATOM   811  C  CB    . ASP   A 1 154 ? 7.109   46.040  3.479   1.00 32.49 ?  264  ASP   A CB    1 
ATOM   812  C  CG    . ASP   A 1 154 ? 6.131   47.100  3.962   1.00 48.27 ?  264  ASP   A CG    1 
ATOM   813  O  OD1   . ASP   A 1 154 ? 6.291   48.283  3.599   1.00 52.09 ?  264  ASP   A OD1   1 
ATOM   814  O  OD2   . ASP   A 1 154 ? 5.194   46.742  4.706   1.00 59.13 -1 264  ASP   A OD2   1 
ATOM   815  N  N     . ALA   A 1 155 ? 8.847   44.499  1.269   1.00 26.49 ?  265  ALA   A N     1 
ATOM   816  C  CA    . ALA   A 1 155 ? 9.890   43.538  0.915   1.00 23.22 ?  265  ALA   A CA    1 
ATOM   817  C  C     . ALA   A 1 155 ? 11.002  44.183  0.092   1.00 23.78 ?  265  ALA   A C     1 
ATOM   818  O  O     . ALA   A 1 155 ? 12.158  43.733  0.146   1.00 23.27 ?  265  ALA   A O     1 
ATOM   819  C  CB    . ALA   A 1 155 ? 9.264   42.358  0.165   1.00 23.31 ?  265  ALA   A CB    1 
ATOM   820  N  N     . TRP   A 1 156 ? 10.685  45.245  -0.659  1.00 24.53 ?  266  TRP   A N     1 
ATOM   821  C  CA    . TRP   A 1 156 ? 11.714  45.952  -1.420  1.00 26.01 ?  266  TRP   A CA    1 
ATOM   822  C  C     . TRP   A 1 156 ? 12.666  46.702  -0.489  1.00 23.63 ?  266  TRP   A C     1 
ATOM   823  O  O     . TRP   A 1 156 ? 13.892  46.622  -0.638  1.00 21.95 ?  266  TRP   A O     1 
ATOM   824  C  CB    . TRP   A 1 156 ? 11.062  46.916  -2.423  1.00 26.27 ?  266  TRP   A CB    1 
ATOM   825  C  CG    . TRP   A 1 156 ? 12.056  47.605  -3.313  1.00 23.66 ?  266  TRP   A CG    1 
ATOM   826  C  CD1   . TRP   A 1 156 ? 12.550  48.882  -3.168  1.00 27.72 ?  266  TRP   A CD1   1 
ATOM   827  C  CD2   . TRP   A 1 156 ? 12.678  47.073  -4.495  1.00 23.25 ?  266  TRP   A CD2   1 
ATOM   828  N  NE1   . TRP   A 1 156 ? 13.441  49.159  -4.176  1.00 27.91 ?  266  TRP   A NE1   1 
ATOM   829  C  CE2   . TRP   A 1 156 ? 13.538  48.069  -5.003  1.00 27.65 ?  266  TRP   A CE2   1 
ATOM   830  C  CE3   . TRP   A 1 156 ? 12.597  45.845  -5.168  1.00 25.97 ?  266  TRP   A CE3   1 
ATOM   831  C  CZ2   . TRP   A 1 156 ? 14.307  47.877  -6.152  1.00 30.10 ?  266  TRP   A CZ2   1 
ATOM   832  C  CZ3   . TRP   A 1 156 ? 13.357  45.659  -6.306  1.00 25.58 ?  266  TRP   A CZ3   1 
ATOM   833  C  CH2   . TRP   A 1 156 ? 14.208  46.664  -6.787  1.00 29.09 ?  266  TRP   A CH2   1 
ATOM   834  N  N     . VAL   A 1 157 ? 12.117  47.435  0.486   1.00 27.50 ?  267  VAL   A N     1 
ATOM   835  C  CA    . VAL   A 1 157 ? 12.953  48.108  1.483   1.00 23.82 ?  267  VAL   A CA    1 
ATOM   836  C  C     . VAL   A 1 157 ? 13.824  47.096  2.224   1.00 23.65 ?  267  VAL   A C     1 
ATOM   837  O  O     . VAL   A 1 157 ? 15.021  47.328  2.454   1.00 27.01 ?  267  VAL   A O     1 
ATOM   838  C  CB    . VAL   A 1 157 ? 12.063  48.918  2.445   1.00 26.65 ?  267  VAL   A CB    1 
ATOM   839  C  CG1   . VAL   A 1 157 ? 12.894  49.537  3.547   1.00 29.50 ?  267  VAL   A CG1   1 
ATOM   840  C  CG2   . VAL   A 1 157 ? 11.333  50.011  1.670   1.00 29.77 ?  267  VAL   A CG2   1 
ATOM   841  N  N     . ARG   A 1 158 ? 13.239  45.951  2.599   1.00 24.26 ?  268  ARG   A N     1 
ATOM   842  C  CA    . ARG   A 1 158 ? 14.016  44.885  3.237   1.00 26.51 ?  268  ARG   A CA    1 
ATOM   843  C  C     . ARG   A 1 158 ? 15.177  44.442  2.351   1.00 23.94 ?  268  ARG   A C     1 
ATOM   844  O  O     . ARG   A 1 158 ? 16.328  44.342  2.807   1.00 23.58 ?  268  ARG   A O     1 
ATOM   845  C  CB    . ARG   A 1 158 ? 13.093  43.701  3.568   1.00 20.61 ?  268  ARG   A CB    1 
ATOM   846  C  CG    . ARG   A 1 158 ? 13.768  42.579  4.386   1.00 22.07 ?  268  ARG   A CG    1 
ATOM   847  C  CD    . ARG   A 1 158 ? 12.793  41.410  4.650   1.00 26.13 ?  268  ARG   A CD    1 
ATOM   848  N  NE    . ARG   A 1 158 ? 11.696  41.770  5.550   1.00 24.74 ?  268  ARG   A NE    1 
ATOM   849  C  CZ    . ARG   A 1 158 ? 11.734  41.626  6.874   1.00 25.64 ?  268  ARG   A CZ    1 
ATOM   850  N  NH1   . ARG   A 1 158 ? 12.822  41.149  7.459   1.00 23.23 ?  268  ARG   A NH1   1 
ATOM   851  N  NH2   . ARG   A 1 158 ? 10.688  41.973  7.617   1.00 26.16 ?  268  ARG   A NH2   1 
ATOM   852  N  N     . ALA   A 1 159 ? 14.895  44.171  1.071   1.00 24.76 ?  269  ALA   A N     1 
ATOM   853  C  CA    . ALA   A 1 159 ? 15.939  43.721  0.155   1.00 19.11 ?  269  ALA   A CA    1 
ATOM   854  C  C     . ALA   A 1 159 ? 17.079  44.731  0.050   1.00 22.69 ?  269  ALA   A C     1 
ATOM   855  O  O     . ALA   A 1 159 ? 18.250  44.346  0.039   1.00 23.28 ?  269  ALA   A O     1 
ATOM   856  C  CB    . ALA   A 1 159 ? 15.348  43.454  -1.226  1.00 22.53 ?  269  ALA   A CB    1 
ATOM   857  N  N     . MET   A 1 160 ? 16.764  46.024  -0.048  1.00 24.02 ?  270  MET   A N     1 
ATOM   858  C  CA    . MET   A 1 160 ? 17.840  47.002  -0.212  1.00 23.62 ?  270  MET   A CA    1 
ATOM   859  C  C     . MET   A 1 160 ? 18.719  47.083  1.035   1.00 23.30 ?  270  MET   A C     1 
ATOM   860  O  O     . MET   A 1 160 ? 19.942  47.227  0.924   1.00 24.91 ?  270  MET   A O     1 
ATOM   861  C  CB    . MET   A 1 160 ? 17.261  48.378  -0.561  1.00 28.06 ?  270  MET   A CB    1 
ATOM   862  C  CG    . MET   A 1 160 ? 16.475  48.460  -1.885  1.00 23.00 ?  270  MET   A CG    1 
ATOM   863  S  SD    . MET   A 1 160 ? 17.389  48.014  -3.371  1.00 27.69 ?  270  MET   A SD    1 
ATOM   864  C  CE    . MET   A 1 160 ? 16.878  46.275  -3.533  1.00 21.56 ?  270  MET   A CE    1 
ATOM   865  N  N     . MET   A 1 161 ? 18.132  46.963  2.231   1.00 23.88 ?  271  MET   A N     1 
ATOM   866  C  CA    . MET   A 1 161 ? 18.946  46.975  3.448   1.00 26.33 ?  271  MET   A CA    1 
ATOM   867  C  C     . MET   A 1 161 ? 19.845  45.742  3.539   1.00 30.56 ?  271  MET   A C     1 
ATOM   868  O  O     . MET   A 1 161 ? 20.998  45.840  3.984   1.00 26.47 ?  271  MET   A O     1 
ATOM   869  C  CB    . MET   A 1 161 ? 18.057  47.081  4.687   1.00 26.67 ?  271  MET   A CB    1 
ATOM   870  C  CG    . MET   A 1 161 ? 17.179  48.329  4.755   1.00 32.08 ?  271  MET   A CG    1 
ATOM   871  S  SD    . MET   A 1 161 ? 18.137  49.836  5.033   1.00 58.25 ?  271  MET   A SD    1 
ATOM   872  C  CE    . MET   A 1 161 ? 18.553  50.303  3.351   1.00 42.72 ?  271  MET   A CE    1 
ATOM   873  N  N     . LEU   A 1 162 ? 19.342  44.572  3.124   1.00 24.86 ?  272  LEU   A N     1 
ATOM   874  C  CA    . LEU   A 1 162 ? 20.173  43.367  3.130   1.00 22.50 ?  272  LEU   A CA    1 
ATOM   875  C  C     . LEU   A 1 162 ? 21.361  43.497  2.179   1.00 22.59 ?  272  LEU   A C     1 
ATOM   876  O  O     . LEU   A 1 162 ? 22.463  43.014  2.478   1.00 25.79 ?  272  LEU   A O     1 
ATOM   877  C  CB    . LEU   A 1 162 ? 19.320  42.141  2.764   1.00 22.32 ?  272  LEU   A CB    1 
ATOM   878  C  CG    . LEU   A 1 162 ? 18.173  41.812  3.734   1.00 22.36 ?  272  LEU   A CG    1 
ATOM   879  C  CD1   . LEU   A 1 162 ? 17.142  40.839  3.105   1.00 20.82 ?  272  LEU   A CD1   1 
ATOM   880  C  CD2   . LEU   A 1 162 ? 18.718  41.235  5.045   1.00 25.20 ?  272  LEU   A CD2   1 
ATOM   881  N  N     . VAL   A 1 163 ? 21.150  44.100  1.004   1.00 23.47 ?  273  VAL   A N     1 
ATOM   882  C  CA    . VAL   A 1 163 ? 22.252  44.291  0.063   1.00 25.28 ?  273  VAL   A CA    1 
ATOM   883  C  C     . VAL   A 1 163 ? 23.298  45.229  0.658   1.00 25.01 ?  273  VAL   A C     1 
ATOM   884  O  O     . VAL   A 1 163 ? 24.506  44.975  0.571   1.00 26.77 ?  273  VAL   A O     1 
ATOM   885  C  CB    . VAL   A 1 163 ? 21.731  44.817  -1.289  1.00 25.40 ?  273  VAL   A CB    1 
ATOM   886  C  CG1   . VAL   A 1 163 ? 22.894  45.266  -2.167  1.00 29.86 ?  273  VAL   A CG1   1 
ATOM   887  C  CG2   . VAL   A 1 163 ? 20.878  43.764  -2.013  1.00 26.08 ?  273  VAL   A CG2   1 
ATOM   888  N  N     . ASP   A 1 164 ? 22.850  46.323  1.278   1.00 28.30 ?  274  ASP   A N     1 
ATOM   889  C  CA    . ASP   A 1 164 ? 23.793  47.247  1.906   1.00 28.92 ?  274  ASP   A CA    1 
ATOM   890  C  C     . ASP   A 1 164 ? 24.600  46.568  3.004   1.00 30.77 ?  274  ASP   A C     1 
ATOM   891  O  O     . ASP   A 1 164 ? 25.749  46.951  3.255   1.00 31.88 ?  274  ASP   A O     1 
ATOM   892  C  CB    . ASP   A 1 164 ? 23.045  48.461  2.466   1.00 30.57 ?  274  ASP   A CB    1 
ATOM   893  C  CG    . ASP   A 1 164 ? 22.648  49.452  1.389   1.00 37.54 ?  274  ASP   A CG    1 
ATOM   894  O  OD1   . ASP   A 1 164 ? 23.106  49.302  0.237   1.00 44.01 ?  274  ASP   A OD1   1 
ATOM   895  O  OD2   . ASP   A 1 164 ? 21.877  50.388  1.699   1.00 45.48 -1 274  ASP   A OD2   1 
ATOM   896  N  N     . ALA   A 1 165 ? 24.032  45.553  3.662   1.00 29.17 ?  275  ALA   A N     1 
ATOM   897  C  CA    . ALA   A 1 165 ? 24.738  44.850  4.727   1.00 28.78 ?  275  ALA   A CA    1 
ATOM   898  C  C     . ALA   A 1 165 ? 25.698  43.777  4.222   1.00 27.34 ?  275  ALA   A C     1 
ATOM   899  O  O     . ALA   A 1 165 ? 26.427  43.197  5.038   1.00 26.97 ?  275  ALA   A O     1 
ATOM   900  C  CB    . ALA   A 1 165 ? 23.740  44.224  5.702   1.00 29.11 ?  275  ALA   A CB    1 
ATOM   901  N  N     . GLY   A 1 166 ? 25.731  43.510  2.918   1.00 26.32 ?  276  GLY   A N     1 
ATOM   902  C  CA    . GLY   A 1 166 ? 26.687  42.593  2.338   1.00 26.16 ?  276  GLY   A CA    1 
ATOM   903  C  C     . GLY   A 1 166 ? 26.177  41.216  1.955   1.00 25.92 ?  276  GLY   A C     1 
ATOM   904  O  O     . GLY   A 1 166 ? 27.001  40.335  1.702   1.00 25.18 ?  276  GLY   A O     1 
ATOM   905  N  N     . VAL   A 1 167 ? 24.859  41.008  1.877   1.00 25.64 ?  277  VAL   A N     1 
ATOM   906  C  CA    . VAL   A 1 167 ? 24.347  39.665  1.589   1.00 20.36 ?  277  VAL   A CA    1 
ATOM   907  C  C     . VAL   A 1 167 ? 24.800  39.222  0.193   1.00 22.05 ?  277  VAL   A C     1 
ATOM   908  O  O     . VAL   A 1 167 ? 24.937  40.034  -0.728  1.00 26.70 ?  277  VAL   A O     1 
ATOM   909  C  CB    . VAL   A 1 167 ? 22.812  39.634  1.727   1.00 21.31 ?  277  VAL   A CB    1 
ATOM   910  C  CG1   . VAL   A 1 167 ? 22.133  40.168  0.491   1.00 23.41 ?  277  VAL   A CG1   1 
ATOM   911  C  CG2   . VAL   A 1 167 ? 22.314  38.196  2.039   1.00 22.59 ?  277  VAL   A CG2   1 
ATOM   912  N  N     . ASP   A 1 168 ? 25.013  37.900  0.028   1.00 20.43 ?  278  ASP   A N     1 
ATOM   913  C  CA    . ASP   A 1 168 ? 25.456  37.340  -1.248  1.00 21.69 ?  278  ASP   A CA    1 
ATOM   914  C  C     . ASP   A 1 168 ? 24.306  36.866  -2.136  1.00 20.12 ?  278  ASP   A C     1 
ATOM   915  O  O     . ASP   A 1 168 ? 24.423  36.921  -3.370  1.00 21.25 ?  278  ASP   A O     1 
ATOM   916  C  CB    . ASP   A 1 168 ? 26.409  36.159  -1.000  1.00 24.60 ?  278  ASP   A CB    1 
ATOM   917  C  CG    . ASP   A 1 168 ? 27.639  36.561  -0.190  1.00 27.75 ?  278  ASP   A CG    1 
ATOM   918  O  OD1   . ASP   A 1 168 ? 28.570  37.152  -0.777  1.00 27.39 ?  278  ASP   A OD1   1 
ATOM   919  O  OD2   . ASP   A 1 168 ? 27.665  36.311  1.035   1.00 24.23 -1 278  ASP   A OD2   1 
ATOM   920  N  N     . VAL   A 1 169 ? 23.215  36.392  -1.531  1.00 20.66 ?  279  VAL   A N     1 
ATOM   921  C  CA    . VAL   A 1 169 ? 22.071  35.809  -2.242  1.00 21.22 ?  279  VAL   A CA    1 
ATOM   922  C  C     . VAL   A 1 169 ? 20.776  36.329  -1.623  1.00 19.84 ?  279  VAL   A C     1 
ATOM   923  O  O     . VAL   A 1 169 ? 20.601  36.264  -0.402  1.00 19.90 ?  279  VAL   A O     1 
ATOM   924  C  CB    . VAL   A 1 169 ? 22.078  34.266  -2.182  1.00 19.35 ?  279  VAL   A CB    1 
ATOM   925  C  CG1   . VAL   A 1 169 ? 20.852  33.684  -2.938  1.00 20.52 ?  279  VAL   A CG1   1 
ATOM   926  C  CG2   . VAL   A 1 169 ? 23.377  33.685  -2.725  1.00 21.01 ?  279  VAL   A CG2   1 
ATOM   927  N  N     . LEU   A 1 170 ? 19.868  36.843  -2.456  1.00 19.54 ?  280  LEU   A N     1 
ATOM   928  C  CA    . LEU   A 1 170 ? 18.496  37.135  -2.042  1.00 19.07 ?  280  LEU   A CA    1 
ATOM   929  C  C     . LEU   A 1 170 ? 17.568  36.015  -2.510  1.00 19.88 ?  280  LEU   A C     1 
ATOM   930  O  O     . LEU   A 1 170 ? 17.649  35.582  -3.659  1.00 20.16 ?  280  LEU   A O     1 
ATOM   931  C  CB    . LEU   A 1 170 ? 18.011  38.469  -2.623  1.00 20.79 ?  280  LEU   A CB    1 
ATOM   932  C  CG    . LEU   A 1 170 ? 18.604  39.781  -2.094  1.00 22.60 ?  280  LEU   A CG    1 
ATOM   933  C  CD1   . LEU   A 1 170 ? 18.160  40.917  -2.997  1.00 22.85 ?  280  LEU   A CD1   1 
ATOM   934  C  CD2   . LEU   A 1 170 ? 18.164  40.042  -0.656  1.00 24.05 ?  280  LEU   A CD2   1 
ATOM   935  N  N     . VAL   A 1 171 ? 16.674  35.554  -1.631  1.00 18.41 ?  281  VAL   A N     1 
ATOM   936  C  CA    . VAL   A 1 171 ? 15.729  34.483  -1.974  1.00 18.22 ?  281  VAL   A CA    1 
ATOM   937  C  C     . VAL   A 1 171 ? 14.320  35.072  -1.912  1.00 16.48 ?  281  VAL   A C     1 
ATOM   938  O  O     . VAL   A 1 171 ? 13.805  35.345  -0.816  1.00 18.05 ?  281  VAL   A O     1 
ATOM   939  C  CB    . VAL   A 1 171 ? 15.877  33.265  -1.044  1.00 18.09 ?  281  VAL   A CB    1 
ATOM   940  C  CG1   . VAL   A 1 171 ? 14.850  32.165  -1.393  1.00 19.68 ?  281  VAL   A CG1   1 
ATOM   941  C  CG2   . VAL   A 1 171 ? 17.311  32.704  -1.079  1.00 19.78 ?  281  VAL   A CG2   1 
ATOM   942  N  N     . VAL   A 1 172 ? 13.691  35.269  -3.078  1.00 16.74 ?  282  VAL   A N     1 
ATOM   943  C  CA    . VAL   A 1 172 ? 12.270  35.627  -3.127  1.00 17.08 ?  282  VAL   A CA    1 
ATOM   944  C  C     . VAL   A 1 172 ? 11.476  34.384  -2.716  1.00 18.99 ?  282  VAL   A C     1 
ATOM   945  O  O     . VAL   A 1 172 ? 11.498  33.367  -3.416  1.00 20.86 ?  282  VAL   A O     1 
ATOM   946  C  CB    . VAL   A 1 172 ? 11.856  36.146  -4.514  1.00 17.78 ?  282  VAL   A CB    1 
ATOM   947  C  CG1   . VAL   A 1 172 ? 10.410  36.608  -4.511  1.00 22.27 ?  282  VAL   A CG1   1 
ATOM   948  C  CG2   . VAL   A 1 172 ? 12.737  37.346  -4.924  1.00 20.64 ?  282  VAL   A CG2   1 
ATOM   949  N  N     . ASP   A 1 173 ? 10.785  34.474  -1.573  1.00 17.98 ?  283  ASP   A N     1 
ATOM   950  C  CA    . ASP   A 1 173 ? 10.371  33.346  -0.721  1.00 19.53 ?  283  ASP   A CA    1 
ATOM   951  C  C     . ASP   A 1 173 ? 8.843   33.344  -0.617  1.00 19.94 ?  283  ASP   A C     1 
ATOM   952  O  O     . ASP   A 1 173 ? 8.288   34.052  0.226   1.00 21.17 ?  283  ASP   A O     1 
ATOM   953  C  CB    . ASP   A 1 173 ? 11.066  33.513  0.653   1.00 21.62 ?  283  ASP   A CB    1 
ATOM   954  C  CG    . ASP   A 1 173 ? 10.529  32.602  1.746   1.00 27.00 ?  283  ASP   A CG    1 
ATOM   955  O  OD1   . ASP   A 1 173 ? 10.381  31.388  1.488   1.00 26.24 ?  283  ASP   A OD1   1 
ATOM   956  O  OD2   . ASP   A 1 173 ? 10.331  33.087  2.898   1.00 21.09 -1 283  ASP   A OD2   1 
ATOM   957  N  N     . THR   A 1 174 ? 8.155   32.533  -1.448  1.00 17.61 ?  284  THR   A N     1 
ATOM   958  C  CA    . THR   A 1 174 ? 6.688   32.533  -1.510  1.00 18.76 ?  284  THR   A CA    1 
ATOM   959  C  C     . THR   A 1 174 ? 6.128   31.109  -1.537  1.00 18.52 ?  284  THR   A C     1 
ATOM   960  O  O     . THR   A 1 174 ? 6.817   30.143  -1.875  1.00 21.77 ?  284  THR   A O     1 
ATOM   961  C  CB    . THR   A 1 174 ? 6.149   33.288  -2.741  1.00 21.06 ?  284  THR   A CB    1 
ATOM   962  O  OG1   . THR   A 1 174 ? 6.376   32.530  -3.937  1.00 21.73 ?  284  THR   A OG1   1 
ATOM   963  C  CG2   . THR   A 1 174 ? 6.822   34.671  -2.877  1.00 20.88 ?  284  THR   A CG2   1 
ATOM   964  N  N     . ALA   A 1 175 ? 4.845   31.002  -1.169  1.00 18.94 ?  285  ALA   A N     1 
ATOM   965  C  CA    . ALA   A 1 175 ? 4.144   29.715  -1.219  1.00 19.07 ?  285  ALA   A CA    1 
ATOM   966  C  C     . ALA   A 1 175 ? 3.796   29.302  -2.650  1.00 21.16 ?  285  ALA   A C     1 
ATOM   967  O  O     . ALA   A 1 175 ? 3.688   28.092  -2.936  1.00 20.55 ?  285  ALA   A O     1 
ATOM   968  C  CB    . ALA   A 1 175 ? 2.872   29.794  -0.367  1.00 21.37 ?  285  ALA   A CB    1 
ATOM   969  N  N     . HIS   A 1 176 ? 3.571   30.273  -3.550  1.00 19.44 ?  286  HIS   A N     1 
ATOM   970  C  CA    . HIS   A 1 176 ? 3.181   30.001  -4.940  1.00 17.82 ?  286  HIS   A CA    1 
ATOM   971  C  C     . HIS   A 1 176 ? 3.844   31.040  -5.850  1.00 19.59 ?  286  HIS   A C     1 
ATOM   972  O  O     . HIS   A 1 176 ? 3.360   32.176  -5.952  1.00 20.54 ?  286  HIS   A O     1 
ATOM   973  C  CB    . HIS   A 1 176 ? 1.655   30.017  -5.066  1.00 18.00 ?  286  HIS   A CB    1 
ATOM   974  C  CG    . HIS   A 1 176 ? 1.140   29.654  -6.427  1.00 20.44 ?  286  HIS   A CG    1 
ATOM   975  N  ND1   . HIS   A 1 176 ? 1.671   28.631  -7.185  1.00 19.82 ?  286  HIS   A ND1   1 
ATOM   976  C  CD2   . HIS   A 1 176 ? 0.115   30.166  -7.150  1.00 17.84 ?  286  HIS   A CD2   1 
ATOM   977  C  CE1   . HIS   A 1 176 ? 1.003   28.537  -8.323  1.00 17.57 ?  286  HIS   A CE1   1 
ATOM   978  N  NE2   . HIS   A 1 176 ? 0.061   29.465  -8.330  1.00 19.18 ?  286  HIS   A NE2   1 
ATOM   979  N  N     . ALA   A 1 177 ? 4.963   30.663  -6.494  1.00 18.35 ?  287  ALA   A N     1 
ATOM   980  C  CA    . ALA   A 1 177 ? 5.726   31.613  -7.313  1.00 16.39 ?  287  ALA   A CA    1 
ATOM   981  C  C     . ALA   A 1 177 ? 5.173   31.806  -8.732  1.00 20.13 ?  287  ALA   A C     1 
ATOM   982  O  O     . ALA   A 1 177 ? 5.654   32.701  -9.440  1.00 20.23 ?  287  ALA   A O     1 
ATOM   983  C  CB    . ALA   A 1 177 ? 7.201   31.186  -7.394  1.00 18.91 ?  287  ALA   A CB    1 
ATOM   984  N  N     . HIS   A 1 178 ? 4.170   31.031  -9.169  1.00 18.98 ?  288  HIS   A N     1 
ATOM   985  C  CA    . HIS   A 1 178 ? 3.655   31.131  -10.548 1.00 17.47 ?  288  HIS   A CA    1 
ATOM   986  C  C     . HIS   A 1 178 ? 2.596   32.240  -10.636 1.00 20.83 ?  288  HIS   A C     1 
ATOM   987  O  O     . HIS   A 1 178 ? 1.403   32.009  -10.887 1.00 21.03 ?  288  HIS   A O     1 
ATOM   988  C  CB    . HIS   A 1 178 ? 3.106   29.776  -11.002 1.00 19.57 ?  288  HIS   A CB    1 
ATOM   989  C  CG    . HIS   A 1 178 ? 3.090   29.572  -12.492 1.00 19.00 ?  288  HIS   A CG    1 
ATOM   990  N  ND1   . HIS   A 1 178 ? 2.676   28.392  -13.078 1.00 19.62 ?  288  HIS   A ND1   1 
ATOM   991  C  CD2   . HIS   A 1 178 ? 3.463   30.383  -13.511 1.00 20.63 ?  288  HIS   A CD2   1 
ATOM   992  C  CE1   . HIS   A 1 178 ? 2.774   28.493  -14.393 1.00 20.68 ?  288  HIS   A CE1   1 
ATOM   993  N  NE2   . HIS   A 1 178 ? 3.247   29.694  -14.682 1.00 21.07 ?  288  HIS   A NE2   1 
ATOM   994  N  N     . ASN   A 1 179 ? 3.071   33.474  -10.458 1.00 21.19 ?  289  ASN   A N     1 
ATOM   995  C  CA    . ASN   A 1 179 ? 2.222   34.646  -10.264 1.00 24.07 ?  289  ASN   A CA    1 
ATOM   996  C  C     . ASN   A 1 179 ? 2.983   35.874  -10.753 1.00 22.97 ?  289  ASN   A C     1 
ATOM   997  O  O     . ASN   A 1 179 ? 4.182   36.000  -10.493 1.00 21.47 ?  289  ASN   A O     1 
ATOM   998  C  CB    . ASN   A 1 179 ? 1.835   34.753  -8.778  1.00 23.25 ?  289  ASN   A CB    1 
ATOM   999  C  CG    . ASN   A 1 179 ? 1.167   36.057  -8.419  1.00 36.35 ?  289  ASN   A CG    1 
ATOM   1000 O  OD1   . ASN   A 1 179 ? 1.827   37.097  -8.311  1.00 33.70 ?  289  ASN   A OD1   1 
ATOM   1001 N  ND2   . ASN   A 1 179 ? -0.139  36.000  -8.165  1.00 31.97 ?  289  ASN   A ND2   1 
ATOM   1002 N  N     . ARG   A 1 180 ? 2.294   36.776  -11.477 1.00 21.89 ?  290  ARG   A N     1 
ATOM   1003 C  CA    . ARG   A 1 180 ? 3.026   37.873  -12.122 1.00 25.85 ?  290  ARG   A CA    1 
ATOM   1004 C  C     . ARG   A 1 180 ? 3.688   38.809  -11.114 1.00 23.45 ?  290  ARG   A C     1 
ATOM   1005 O  O     . ARG   A 1 180 ? 4.749   39.373  -11.406 1.00 23.98 ?  290  ARG   A O     1 
ATOM   1006 C  CB    . ARG   A 1 180 ? 2.107   38.661  -13.064 1.00 31.00 ?  290  ARG   A CB    1 
ATOM   1007 C  CG    . ARG   A 1 180 ? 0.861   39.223  -12.427 1.00 42.66 ?  290  ARG   A CG    1 
ATOM   1008 C  CD    . ARG   A 1 180 ? -0.088  39.745  -13.502 1.00 53.65 ?  290  ARG   A CD    1 
ATOM   1009 N  NE    . ARG   A 1 180 ? -0.180  38.817  -14.628 1.00 58.27 ?  290  ARG   A NE    1 
ATOM   1010 C  CZ    . ARG   A 1 180 ? -1.207  38.757  -15.469 1.00 62.79 ?  290  ARG   A CZ    1 
ATOM   1011 N  NH1   . ARG   A 1 180 ? -1.202  37.879  -16.463 1.00 67.31 ?  290  ARG   A NH1   1 
ATOM   1012 N  NH2   . ARG   A 1 180 ? -2.246  39.566  -15.310 1.00 65.49 ?  290  ARG   A NH2   1 
ATOM   1013 N  N     . LEU   A 1 181 ? 3.102   38.993  -9.930  1.00 25.72 ?  291  LEU   A N     1 
ATOM   1014 C  CA    . LEU   A 1 181 ? 3.743   39.860  -8.943  1.00 24.73 ?  291  LEU   A CA    1 
ATOM   1015 C  C     . LEU   A 1 181 ? 5.073   39.272  -8.457  1.00 24.82 ?  291  LEU   A C     1 
ATOM   1016 O  O     . LEU   A 1 181 ? 6.038   40.012  -8.217  1.00 26.31 ?  291  LEU   A O     1 
ATOM   1017 C  CB    . LEU   A 1 181 ? 2.794   40.110  -7.771  1.00 25.91 ?  291  LEU   A CB    1 
ATOM   1018 C  CG    . LEU   A 1 181 ? 1.532   40.923  -8.083  1.00 31.06 ?  291  LEU   A CG    1 
ATOM   1019 C  CD1   . LEU   A 1 181 ? 0.673   41.075  -6.839  1.00 36.17 ?  291  LEU   A CD1   1 
ATOM   1020 C  CD2   . LEU   A 1 181 ? 1.910   42.292  -8.629  1.00 41.05 ?  291  LEU   A CD2   1 
ATOM   1021 N  N     . VAL   A 1 182 ? 5.151   37.943  -8.323  1.00 22.72 ?  292  VAL   A N     1 
ATOM   1022 C  CA    . VAL   A 1 182 ? 6.404   37.310  -7.896  1.00 21.96 ?  292  VAL   A CA    1 
ATOM   1023 C  C     . VAL   A 1 182 ? 7.459   37.398  -8.994  1.00 22.51 ?  292  VAL   A C     1 
ATOM   1024 O  O     . VAL   A 1 182 ? 8.636   37.671  -8.725  1.00 22.84 ?  292  VAL   A O     1 
ATOM   1025 C  CB    . VAL   A 1 182 ? 6.157   35.846  -7.475  1.00 18.75 ?  292  VAL   A CB    1 
ATOM   1026 C  CG1   . VAL   A 1 182 ? 7.476   35.179  -7.130  1.00 21.65 ?  292  VAL   A CG1   1 
ATOM   1027 C  CG2   . VAL   A 1 182 ? 5.215   35.791  -6.281  1.00 23.57 ?  292  VAL   A CG2   1 
ATOM   1028 N  N     . LEU   A 1 183 ? 7.061   37.147  -10.244 1.00 21.43 ?  293  LEU   A N     1 
ATOM   1029 C  CA    . LEU   A 1 183 ? 7.984   37.253  -11.366 1.00 20.71 ?  293  LEU   A CA    1 
ATOM   1030 C  C     . LEU   A 1 183 ? 8.510   38.682  -11.523 1.00 21.55 ?  293  LEU   A C     1 
ATOM   1031 O  O     . LEU   A 1 183 ? 9.690   38.885  -11.834 1.00 24.42 ?  293  LEU   A O     1 
ATOM   1032 C  CB    . LEU   A 1 183 ? 7.285   36.777  -12.642 1.00 23.28 ?  293  LEU   A CB    1 
ATOM   1033 C  CG    . LEU   A 1 183 ? 6.700   35.364  -12.574 1.00 21.30 ?  293  LEU   A CG    1 
ATOM   1034 C  CD1   . LEU   A 1 183 ? 5.808   35.073  -13.786 1.00 27.20 ?  293  LEU   A CD1   1 
ATOM   1035 C  CD2   . LEU   A 1 183 ? 7.825   34.335  -12.474 1.00 24.51 ?  293  LEU   A CD2   1 
ATOM   1036 N  N     . ASP   A 1 184 ? 7.644   39.683  -11.324 1.00 24.99 ?  294  ASP   A N     1 
ATOM   1037 C  CA    . ASP   A 1 184 ? 8.081   41.086  -11.354 1.00 24.07 ?  294  ASP   A CA    1 
ATOM   1038 C  C     . ASP   A 1 184 ? 9.124   41.376  -10.278 1.00 24.38 ?  294  ASP   A C     1 
ATOM   1039 O  O     . ASP   A 1 184 ? 10.106  42.102  -10.522 1.00 25.94 ?  294  ASP   A O     1 
ATOM   1040 C  CB    . ASP   A 1 184 ? 6.871   42.011  -11.169 1.00 26.76 ?  294  ASP   A CB    1 
ATOM   1041 C  CG    . ASP   A 1 184 ? 6.003   42.111  -12.413 1.00 37.06 ?  294  ASP   A CG    1 
ATOM   1042 O  OD1   . ASP   A 1 184 ? 6.412   41.607  -13.480 1.00 42.73 ?  294  ASP   A OD1   1 
ATOM   1043 O  OD2   . ASP   A 1 184 ? 4.908   42.713  -12.326 1.00 44.47 -1 294  ASP   A OD2   1 
ATOM   1044 N  N     . MET   A 1 185 ? 8.917   40.851  -9.067  1.00 24.17 ?  295  MET   A N     1 
ATOM   1045 C  CA    . MET   A 1 185 ? 9.875   41.084  -7.988  1.00 21.66 ?  295  MET   A CA    1 
ATOM   1046 C  C     . MET   A 1 185 ? 11.254  40.520  -8.343  1.00 24.72 ?  295  MET   A C     1 
ATOM   1047 O  O     . MET   A 1 185 ? 12.279  41.182  -8.147  1.00 24.15 ?  295  MET   A O     1 
ATOM   1048 C  CB    . MET   A 1 185 ? 9.332   40.486  -6.682  1.00 22.13 ?  295  MET   A CB    1 
ATOM   1049 C  CG    . MET   A 1 185 ? 10.160  40.734  -5.430  1.00 21.35 ?  295  MET   A CG    1 
ATOM   1050 S  SD    . MET   A 1 185 ? 9.975   42.454  -4.834  1.00 29.51 ?  295  MET   A SD    1 
ATOM   1051 C  CE    . MET   A 1 185 ? 11.005  42.416  -3.369  1.00 24.49 ?  295  MET   A CE    1 
ATOM   1052 N  N     . VAL   A 1 186 ? 11.301  39.290  -8.872  1.00 24.11 ?  296  VAL   A N     1 
ATOM   1053 C  CA    . VAL   A 1 186 ? 12.574  38.697  -9.291  1.00 21.69 ?  296  VAL   A CA    1 
ATOM   1054 C  C     . VAL   A 1 186 ? 13.258  39.564  -10.349 1.00 24.74 ?  296  VAL   A C     1 
ATOM   1055 O  O     . VAL   A 1 186 ? 14.455  39.885  -10.247 1.00 24.71 ?  296  VAL   A O     1 
ATOM   1056 C  CB    . VAL   A 1 186 ? 12.334  37.260  -9.797  1.00 21.83 ?  296  VAL   A CB    1 
ATOM   1057 C  CG1   . VAL   A 1 186 ? 13.576  36.697  -10.487 1.00 24.72 ?  296  VAL   A CG1   1 
ATOM   1058 C  CG2   . VAL   A 1 186 ? 11.889  36.372  -8.640  1.00 23.95 ?  296  VAL   A CG2   1 
ATOM   1059 N  N     . GLY   A 1 187 ? 12.505  39.969  -11.375 1.00 23.84 ?  297  GLY   A N     1 
ATOM   1060 C  CA    . GLY   A 1 187 ? 13.096  40.734  -12.465 1.00 25.86 ?  297  GLY   A CA    1 
ATOM   1061 C  C     . GLY   A 1 187 ? 13.570  42.115  -12.041 1.00 26.18 ?  297  GLY   A C     1 
ATOM   1062 O  O     . GLY   A 1 187 ? 14.594  42.606  -12.526 1.00 29.19 ?  297  GLY   A O     1 
ATOM   1063 N  N     . LYS   A 1 188 ? 12.828  42.767  -11.147 1.00 23.56 ?  298  LYS   A N     1 
ATOM   1064 C  CA    . LYS   A 1 188 ? 13.218  44.108  -10.705 1.00 24.35 ?  298  LYS   A CA    1 
ATOM   1065 C  C     . LYS   A 1 188 ? 14.468  44.064  -9.824  1.00 28.21 ?  298  LYS   A C     1 
ATOM   1066 O  O     . LYS   A 1 188 ? 15.351  44.930  -9.932  1.00 28.25 ?  298  LYS   A O     1 
ATOM   1067 C  CB    . LYS   A 1 188 ? 12.045  44.766  -9.971  1.00 28.28 ?  298  LYS   A CB    1 
ATOM   1068 C  CG    . LYS   A 1 188 ? 12.319  46.192  -9.510  1.00 42.53 ?  298  LYS   A CG    1 
ATOM   1069 C  CD    . LYS   A 1 188 ? 11.173  46.733  -8.657  1.00 45.16 ?  298  LYS   A CD    1 
ATOM   1070 C  CE    . LYS   A 1 188 ? 11.372  48.212  -8.313  1.00 43.94 ?  298  LYS   A CE    1 
ATOM   1071 N  NZ    . LYS   A 1 188 ? 10.286  48.722  -7.428  1.00 42.13 ?  298  LYS   A NZ    1 
ATOM   1072 N  N     . LEU   A 1 189 ? 14.576  43.055  -8.956  1.00 24.44 ?  299  LEU   A N     1 
ATOM   1073 C  CA    . LEU   A 1 189 ? 15.799  42.881  -8.178  1.00 24.67 ?  299  LEU   A CA    1 
ATOM   1074 C  C     . LEU   A 1 189 ? 16.999  42.653  -9.090  1.00 26.62 ?  299  LEU   A C     1 
ATOM   1075 O  O     . LEU   A 1 189 ? 18.067  43.253  -8.899  1.00 26.48 ?  299  LEU   A O     1 
ATOM   1076 C  CB    . LEU   A 1 189 ? 15.630  41.716  -7.189  1.00 24.36 ?  299  LEU   A CB    1 
ATOM   1077 C  CG    . LEU   A 1 189 ? 14.758  41.939  -5.951  1.00 23.18 ?  299  LEU   A CG    1 
ATOM   1078 C  CD1   . LEU   A 1 189 ? 14.675  40.651  -5.088  1.00 22.38 ?  299  LEU   A CD1   1 
ATOM   1079 C  CD2   . LEU   A 1 189 ? 15.313  43.094  -5.103  1.00 24.76 ?  299  LEU   A CD2   1 
ATOM   1080 N  N     . LYS   A 1 190 ? 16.855  41.767  -10.082 1.00 25.84 ?  300  LYS   A N     1 
ATOM   1081 C  CA    . LYS   A 1 190 ? 17.972  41.496  -10.985 1.00 25.78 ?  300  LYS   A CA    1 
ATOM   1082 C  C     . LYS   A 1 190 ? 18.391  42.759  -11.735 1.00 30.64 ?  300  LYS   A C     1 
ATOM   1083 O  O     . LYS   A 1 190 ? 19.588  43.015  -11.919 1.00 31.32 ?  300  LYS   A O     1 
ATOM   1084 C  CB    . LYS   A 1 190 ? 17.597  40.367  -11.954 1.00 33.75 ?  300  LYS   A CB    1 
ATOM   1085 C  CG    . LYS   A 1 190 ? 18.788  39.635  -12.587 1.00 38.28 ?  300  LYS   A CG    1 
ATOM   1086 C  CD    . LYS   A 1 190 ? 19.663  38.950  -11.540 1.00 29.44 ?  300  LYS   A CD    1 
ATOM   1087 C  CE    . LYS   A 1 190 ? 21.031  38.581  -12.098 1.00 36.89 ?  300  LYS   A CE    1 
ATOM   1088 N  NZ    . LYS   A 1 190 ? 22.018  38.406  -10.989 1.00 29.32 ?  300  LYS   A NZ    1 
ATOM   1089 N  N     . SER   A 1 191 ? 17.421  43.581  -12.144 1.00 28.37 ?  301  SER   A N     1 
ATOM   1090 C  CA    . SER   A 1 191 ? 17.755  44.809  -12.870 1.00 32.44 ?  301  SER   A CA    1 
ATOM   1091 C  C     . SER   A 1 191 ? 18.501  45.810  -11.986 1.00 34.63 ?  301  SER   A C     1 
ATOM   1092 O  O     . SER   A 1 191 ? 19.445  46.466  -12.446 1.00 36.67 ?  301  SER   A O     1 
ATOM   1093 C  CB    . SER   A 1 191 ? 16.484  45.442  -13.438 1.00 33.79 ?  301  SER   A CB    1 
ATOM   1094 O  OG    . SER   A 1 191 ? 15.917  44.622  -14.442 1.00 43.72 ?  301  SER   A OG    1 
ATOM   1095 N  N     . GLU   A 1 192 ? 18.095  45.952  -10.723 1.00 31.08 ?  302  GLU   A N     1 
ATOM   1096 C  CA    . GLU   A 1 192 ? 18.651  47.005  -9.874  1.00 30.55 ?  302  GLU   A CA    1 
ATOM   1097 C  C     . GLU   A 1 192 ? 19.951  46.611  -9.184  1.00 35.14 ?  302  GLU   A C     1 
ATOM   1098 O  O     . GLU   A 1 192 ? 20.877  47.431  -9.108  1.00 32.51 ?  302  GLU   A O     1 
ATOM   1099 C  CB    . GLU   A 1 192 ? 17.634  47.422  -8.811  1.00 33.56 ?  302  GLU   A CB    1 
ATOM   1100 C  CG    . GLU   A 1 192 ? 16.360  48.032  -9.364  1.00 40.66 ?  302  GLU   A CG    1 
ATOM   1101 C  CD    . GLU   A 1 192 ? 16.577  49.413  -9.943  1.00 50.99 ?  302  GLU   A CD    1 
ATOM   1102 O  OE1   . GLU   A 1 192 ? 17.412  50.173  -9.395  1.00 44.13 ?  302  GLU   A OE1   1 
ATOM   1103 O  OE2   . GLU   A 1 192 ? 15.919  49.732  -10.955 1.00 54.43 -1 302  GLU   A OE2   1 
ATOM   1104 N  N     . VAL   A 1 193 ? 20.051  45.380  -8.678  1.00 27.68 ?  303  VAL   A N     1 
ATOM   1105 C  CA    . VAL   A 1 193 ? 21.205  44.994  -7.875  1.00 29.54 ?  303  VAL   A CA    1 
ATOM   1106 C  C     . VAL   A 1 193 ? 21.811  43.691  -8.377  1.00 30.42 ?  303  VAL   A C     1 
ATOM   1107 O  O     . VAL   A 1 193 ? 22.681  43.116  -7.717  1.00 30.58 ?  303  VAL   A O     1 
ATOM   1108 C  CB    . VAL   A 1 193 ? 20.828  44.872  -6.388  1.00 30.44 ?  303  VAL   A CB    1 
ATOM   1109 C  CG1   . VAL   A 1 193 ? 20.392  46.217  -5.828  1.00 33.96 ?  303  VAL   A CG1   1 
ATOM   1110 C  CG2   . VAL   A 1 193 ? 19.721  43.814  -6.197  1.00 33.20 ?  303  VAL   A CG2   1 
ATOM   1111 N  N     . GLY   A 1 194 ? 21.387  43.243  -9.561  1.00 32.59 ?  304  GLY   A N     1 
ATOM   1112 C  CA    . GLY   A 1 194 ? 21.821  41.955  -10.087 1.00 30.67 ?  304  GLY   A CA    1 
ATOM   1113 C  C     . GLY   A 1 194 ? 23.306  41.856  -10.375 1.00 39.47 ?  304  GLY   A C     1 
ATOM   1114 O  O     . GLY   A 1 194 ? 23.824  40.744  -10.523 1.00 36.51 ?  304  GLY   A O     1 
ATOM   1115 N  N     . ASP   A 1 195 ? 24.004  42.992  -10.468 1.00 35.84 ?  305  ASP   A N     1 
ATOM   1116 C  CA    . ASP   A 1 195 ? 25.451  42.963  -10.645 1.00 39.99 ?  305  ASP   A CA    1 
ATOM   1117 C  C     . ASP   A 1 195 ? 26.173  42.598  -9.356  1.00 41.27 ?  305  ASP   A C     1 
ATOM   1118 O  O     . ASP   A 1 195 ? 27.279  42.048  -9.402  1.00 46.19 ?  305  ASP   A O     1 
ATOM   1119 C  CB    . ASP   A 1 195 ? 25.946  44.323  -11.150 1.00 45.60 ?  305  ASP   A CB    1 
ATOM   1120 C  CG    . ASP   A 1 195 ? 25.331  45.493  -10.389 1.00 52.61 ?  305  ASP   A CG    1 
ATOM   1121 O  OD1   . ASP   A 1 195 ? 24.082  45.559  -10.293 1.00 50.93 ?  305  ASP   A OD1   1 
ATOM   1122 O  OD2   . ASP   A 1 195 ? 26.095  46.346  -9.884  1.00 58.56 -1 305  ASP   A OD2   1 
ATOM   1123 N  N     . ARG   A 1 196 ? 25.571  42.900  -8.210  1.00 34.04 ?  306  ARG   A N     1 
ATOM   1124 C  CA    . ARG   A 1 196 ? 26.189  42.675  -6.913  1.00 36.26 ?  306  ARG   A CA    1 
ATOM   1125 C  C     . ARG   A 1 196 ? 25.719  41.398  -6.227  1.00 37.41 ?  306  ARG   A C     1 
ATOM   1126 O  O     . ARG   A 1 196 ? 26.503  40.785  -5.498  1.00 38.50 ?  306  ARG   A O     1 
ATOM   1127 C  CB    . ARG   A 1 196 ? 25.906  43.862  -5.982  1.00 39.57 ?  306  ARG   A CB    1 
ATOM   1128 C  CG    . ARG   A 1 196 ? 26.417  45.210  -6.491  1.00 51.27 ?  306  ARG   A CG    1 
ATOM   1129 C  CD    . ARG   A 1 196 ? 25.890  46.363  -5.642  1.00 51.55 ?  306  ARG   A CD    1 
ATOM   1130 N  NE    . ARG   A 1 196 ? 26.409  46.320  -4.277  1.00 60.74 ?  306  ARG   A NE    1 
ATOM   1131 C  CZ    . ARG   A 1 196 ? 26.104  47.204  -3.331  1.00 55.74 ?  306  ARG   A CZ    1 
ATOM   1132 N  NH1   . ARG   A 1 196 ? 25.276  48.205  -3.599  1.00 56.82 ?  306  ARG   A NH1   1 
ATOM   1133 N  NH2   . ARG   A 1 196 ? 26.627  47.087  -2.116  1.00 51.48 ?  306  ARG   A NH2   1 
ATOM   1134 N  N     A VAL   A 1 197 ? 24.459  40.992  -6.403  0.51 32.20 ?  307  VAL   A N     1 
ATOM   1135 N  N     B VAL   A 1 197 ? 24.485  40.965  -6.494  0.49 32.15 ?  307  VAL   A N     1 
ATOM   1136 C  CA    A VAL   A 1 197 ? 23.903  39.868  -5.655  0.51 28.14 ?  307  VAL   A CA    1 
ATOM   1137 C  CA    B VAL   A 1 197 ? 23.810  39.927  -5.726  0.49 28.24 ?  307  VAL   A CA    1 
ATOM   1138 C  C     A VAL   A 1 197 ? 23.148  38.939  -6.595  0.51 24.14 ?  307  VAL   A C     1 
ATOM   1139 C  C     B VAL   A 1 197 ? 23.192  38.913  -6.681  0.49 24.14 ?  307  VAL   A C     1 
ATOM   1140 O  O     A VAL   A 1 197 ? 22.565  39.372  -7.593  0.51 25.34 ?  307  VAL   A O     1 
ATOM   1141 O  O     B VAL   A 1 197 ? 22.756  39.262  -7.782  0.49 25.65 ?  307  VAL   A O     1 
ATOM   1142 C  CB    A VAL   A 1 197 ? 22.971  40.331  -4.508  0.51 29.47 ?  307  VAL   A CB    1 
ATOM   1143 C  CB    B VAL   A 1 197 ? 22.724  40.548  -4.817  0.49 28.90 ?  307  VAL   A CB    1 
ATOM   1144 C  CG1   A VAL   A 1 197 ? 23.682  41.336  -3.611  0.51 28.55 ?  307  VAL   A CG1   1 
ATOM   1145 C  CG1   B VAL   A 1 197 ? 22.293  39.576  -3.738  0.49 25.34 ?  307  VAL   A CG1   1 
ATOM   1146 C  CG2   A VAL   A 1 197 ? 21.662  40.898  -5.060  0.51 29.56 ?  307  VAL   A CG2   1 
ATOM   1147 C  CG2   B VAL   A 1 197 ? 23.222  41.852  -4.213  0.49 31.64 ?  307  VAL   A CG2   1 
ATOM   1148 N  N     . GLU   A 1 198 ? 23.160  37.647  -6.257  1.00 23.27 ?  308  GLU   A N     1 
ATOM   1149 C  CA    . GLU   A 1 198 ? 22.417  36.617  -6.980  1.00 21.96 ?  308  GLU   A CA    1 
ATOM   1150 C  C     . GLU   A 1 198 ? 20.987  36.531  -6.443  1.00 20.86 ?  308  GLU   A C     1 
ATOM   1151 O  O     . GLU   A 1 198 ? 20.748  36.737  -5.252  1.00 23.11 ?  308  GLU   A O     1 
ATOM   1152 C  CB    . GLU   A 1 198 ? 23.106  35.249  -6.845  1.00 21.10 ?  308  GLU   A CB    1 
ATOM   1153 C  CG    . GLU   A 1 198 ? 24.517  35.188  -7.465  1.00 22.37 ?  308  GLU   A CG    1 
ATOM   1154 C  CD    . GLU   A 1 198 ? 24.484  35.003  -8.966  1.00 24.41 ?  308  GLU   A CD    1 
ATOM   1155 O  OE1   . GLU   A 1 198 ? 24.350  33.851  -9.430  1.00 22.61 ?  308  GLU   A OE1   1 
ATOM   1156 O  OE2   . GLU   A 1 198 ? 24.565  36.019  -9.698  1.00 27.76 -1 308  GLU   A OE2   1 
ATOM   1157 N  N     . VAL   A 1 199 ? 20.035  36.222  -7.330  1.00 18.72 ?  309  VAL   A N     1 
ATOM   1158 C  CA    . VAL   A 1 199 ? 18.599  36.288  -7.017  1.00 19.86 ?  309  VAL   A CA    1 
ATOM   1159 C  C     . VAL   A 1 199 ? 17.940  34.930  -7.314  1.00 20.72 ?  309  VAL   A C     1 
ATOM   1160 O  O     . VAL   A 1 199 ? 17.893  34.500  -8.472  1.00 22.28 ?  309  VAL   A O     1 
ATOM   1161 C  CB    . VAL   A 1 199 ? 17.894  37.411  -7.809  1.00 20.64 ?  309  VAL   A CB    1 
ATOM   1162 C  CG1   . VAL   A 1 199 ? 16.406  37.475  -7.472  1.00 24.11 ?  309  VAL   A CG1   1 
ATOM   1163 C  CG2   . VAL   A 1 199 ? 18.558  38.791  -7.560  1.00 23.13 ?  309  VAL   A CG2   1 
ATOM   1164 N  N     . VAL   A 1 200 ? 17.374  34.281  -6.255  1.00 17.50 ?  310  VAL   A N     1 
ATOM   1165 C  CA    . VAL   A 1 200 ? 16.647  33.005  -6.332  1.00 19.12 ?  310  VAL   A CA    1 
ATOM   1166 C  C     . VAL   A 1 200 ? 15.153  33.275  -6.240  1.00 20.33 ?  310  VAL   A C     1 
ATOM   1167 O  O     . VAL   A 1 200 ? 14.718  34.163  -5.503  1.00 20.01 ?  310  VAL   A O     1 
ATOM   1168 C  CB    . VAL   A 1 200 ? 17.088  32.076  -5.183  1.00 16.37 ?  310  VAL   A CB    1 
ATOM   1169 C  CG1   . VAL   A 1 200 ? 16.300  30.746  -5.177  1.00 20.22 ?  310  VAL   A CG1   1 
ATOM   1170 C  CG2   . VAL   A 1 200 ? 18.586  31.834  -5.243  1.00 22.51 ?  310  VAL   A CG2   1 
ATOM   1171 N  N     . GLY   A 1 201 ? 14.352  32.484  -6.950  1.00 19.08 ?  311  GLY   A N     1 
ATOM   1172 C  CA    . GLY   A 1 201 ? 12.906  32.548  -6.813  1.00 18.00 ?  311  GLY   A CA    1 
ATOM   1173 C  C     . GLY   A 1 201 ? 12.281  31.183  -6.587  1.00 19.03 ?  311  GLY   A C     1 
ATOM   1174 O  O     . GLY   A 1 201 ? 12.759  30.172  -7.094  1.00 18.19 ?  311  GLY   A O     1 
ATOM   1175 N  N     . GLY   A 1 202 ? 11.190  31.169  -5.815  1.00 16.84 ?  312  GLY   A N     1 
ATOM   1176 C  CA    . GLY   A 1 202 ? 10.449  29.935  -5.530  1.00 18.21 ?  312  GLY   A CA    1 
ATOM   1177 C  C     . GLY   A 1 202 ? 9.261   30.238  -4.630  1.00 17.86 ?  312  GLY   A C     1 
ATOM   1178 O  O     . GLY   A 1 202 ? 9.068   31.388  -4.196  1.00 17.67 ?  312  GLY   A O     1 
ATOM   1179 N  N     . ASN   A 1 203 ? 8.437   29.210  -4.350  1.00 17.24 ?  313  ASN   A N     1 
ATOM   1180 C  CA    . ASN   A 1 203 ? 8.615   27.808  -4.820  1.00 16.80 ?  313  ASN   A CA    1 
ATOM   1181 C  C     . ASN   A 1 203 ? 7.665   27.420  -5.971  1.00 15.80 ?  313  ASN   A C     1 
ATOM   1182 O  O     . ASN   A 1 203 ? 6.547   27.956  -6.077  1.00 17.28 ?  313  ASN   A O     1 
ATOM   1183 C  CB    . ASN   A 1 203 ? 8.421   26.808  -3.652  1.00 17.58 ?  313  ASN   A CB    1 
ATOM   1184 C  CG    . ASN   A 1 203 ? 9.663   26.683  -2.770  1.00 18.10 ?  313  ASN   A CG    1 
ATOM   1185 O  OD1   . ASN   A 1 203 ? 10.550  27.541  -2.830  1.00 16.18 ?  313  ASN   A OD1   1 
ATOM   1186 N  ND2   . ASN   A 1 203 ? 9.733   25.622  -1.947  1.00 16.83 ?  313  ASN   A ND2   1 
ATOM   1187 N  N     . VAL   A 1 204 ? 8.119   26.493  -6.824  1.00 16.20 ?  314  VAL   A N     1 
ATOM   1188 C  CA    . VAL   A 1 204 ? 7.346   25.966  -7.953  1.00 16.71 ?  314  VAL   A CA    1 
ATOM   1189 C  C     . VAL   A 1 204 ? 7.333   24.436  -7.910  1.00 18.21 ?  314  VAL   A C     1 
ATOM   1190 O  O     . VAL   A 1 204 ? 8.090   23.800  -7.166  1.00 17.64 ?  314  VAL   A O     1 
ATOM   1191 C  CB    . VAL   A 1 204 ? 7.893   26.454  -9.314  1.00 17.42 ?  314  VAL   A CB    1 
ATOM   1192 C  CG1   . VAL   A 1 204 ? 7.940   28.000  -9.364  1.00 19.44 ?  314  VAL   A CG1   1 
ATOM   1193 C  CG2   . VAL   A 1 204 ? 9.273   25.851  -9.600  1.00 20.27 ?  314  VAL   A CG2   1 
ATOM   1194 N  N     . ALA   A 1 205 ? 6.435   23.839  -8.729  1.00 17.40 ?  315  ALA   A N     1 
ATOM   1195 C  CA    . ALA   A 1 205 ? 6.337   22.381  -8.810  1.00 18.76 ?  315  ALA   A CA    1 
ATOM   1196 C  C     . ALA   A 1 205 ? 5.991   21.864  -10.206 1.00 19.37 ?  315  ALA   A C     1 
ATOM   1197 O  O     . ALA   A 1 205 ? 5.648   20.671  -10.338 1.00 19.54 ?  315  ALA   A O     1 
ATOM   1198 C  CB    . ALA   A 1 205 ? 5.308   21.847  -7.801  1.00 24.53 ?  315  ALA   A CB    1 
ATOM   1199 N  N     . THR   A 1 206 ? 6.074   22.706  -11.243 1.00 17.29 ?  316  THR   A N     1 
ATOM   1200 C  CA    . THR   A 1 206 ? 5.775   22.325  -12.623 1.00 17.24 ?  316  THR   A CA    1 
ATOM   1201 C  C     . THR   A 1 206 ? 6.836   22.884  -13.581 1.00 17.65 ?  316  THR   A C     1 
ATOM   1202 O  O     . THR   A 1 206 ? 7.571   23.830  -13.271 1.00 17.83 ?  316  THR   A O     1 
ATOM   1203 C  CB    . THR   A 1 206 ? 4.391   22.825  -13.085 1.00 17.02 ?  316  THR   A CB    1 
ATOM   1204 O  OG1   . THR   A 1 206 ? 4.415   24.263  -13.190 1.00 18.91 ?  316  THR   A OG1   1 
ATOM   1205 C  CG2   . THR   A 1 206 ? 3.277   22.412  -12.115 1.00 17.55 ?  316  THR   A CG2   1 
ATOM   1206 N  N     . ARG   A 1 207 ? 6.879   22.280  -14.774 1.00 16.68 ?  317  ARG   A N     1 
ATOM   1207 C  CA    . ARG   A 1 207 ? 7.733   22.755  -15.861 1.00 15.88 ?  317  ARG   A CA    1 
ATOM   1208 C  C     . ARG   A 1 207 ? 7.387   24.193  -16.275 1.00 17.48 ?  317  ARG   A C     1 
ATOM   1209 O  O     . ARG   A 1 207 ? 8.283   25.035  -16.443 1.00 18.63 ?  317  ARG   A O     1 
ATOM   1210 C  CB    . ARG   A 1 207 ? 7.611   21.778  -17.046 1.00 20.42 ?  317  ARG   A CB    1 
ATOM   1211 C  CG    . ARG   A 1 207 ? 8.607   22.004  -18.171 1.00 20.88 ?  317  ARG   A CG    1 
ATOM   1212 C  CD    . ARG   A 1 207 ? 8.344   21.085  -19.393 1.00 24.64 ?  317  ARG   A CD    1 
ATOM   1213 N  NE    . ARG   A 1 207 ? 8.359   19.648  -19.091 1.00 21.64 ?  317  ARG   A NE    1 
ATOM   1214 C  CZ    . ARG   A 1 207 ? 8.829   18.715  -19.927 1.00 24.69 ?  317  ARG   A CZ    1 
ATOM   1215 N  NH1   . ARG   A 1 207 ? 9.339   19.071  -21.108 1.00 25.66 ?  317  ARG   A NH1   1 
ATOM   1216 N  NH2   . ARG   A 1 207 ? 8.824   17.426  -19.583 1.00 20.57 ?  317  ARG   A NH2   1 
ATOM   1217 N  N     A SER   A 1 208 ? 6.091   24.498  -16.431 0.65 19.89 ?  318  SER   A N     1 
ATOM   1218 N  N     B SER   A 1 208 ? 6.095   24.496  -16.431 0.35 19.89 ?  318  SER   A N     1 
ATOM   1219 C  CA    A SER   A 1 208 ? 5.693   25.832  -16.891 0.65 20.47 ?  318  SER   A CA    1 
ATOM   1220 C  CA    B SER   A 1 208 ? 5.701   25.832  -16.880 0.35 20.46 ?  318  SER   A CA    1 
ATOM   1221 C  C     A SER   A 1 208 ? 6.044   26.918  -15.871 0.65 19.27 ?  318  SER   A C     1 
ATOM   1222 C  C     B SER   A 1 208 ? 6.082   26.906  -15.864 0.35 19.31 ?  318  SER   A C     1 
ATOM   1223 O  O     A SER   A 1 208 ? 6.467   28.021  -16.252 0.65 19.36 ?  318  SER   A O     1 
ATOM   1224 O  O     B SER   A 1 208 ? 6.541   27.994  -16.241 0.35 19.40 ?  318  SER   A O     1 
ATOM   1225 C  CB    A SER   A 1 208 ? 4.193   25.852  -17.218 0.65 20.57 ?  318  SER   A CB    1 
ATOM   1226 C  CB    B SER   A 1 208 ? 4.198   25.869  -17.160 0.35 20.64 ?  318  SER   A CB    1 
ATOM   1227 O  OG    A SER   A 1 208 ? 3.405   25.541  -16.083 0.65 23.41 ?  318  SER   A OG    1 
ATOM   1228 O  OG    B SER   A 1 208 ? 3.779   27.193  -17.431 0.35 23.95 ?  318  SER   A OG    1 
ATOM   1229 N  N     . ALA   A 1 209 ? 5.891   26.628  -14.570 1.00 19.57 ?  319  ALA   A N     1 
ATOM   1230 C  CA    . ALA   A 1 209 ? 6.265   27.602  -13.539 1.00 18.16 ?  319  ALA   A CA    1 
ATOM   1231 C  C     . ALA   A 1 209 ? 7.779   27.840  -13.509 1.00 18.30 ?  319  ALA   A C     1 
ATOM   1232 O  O     . ALA   A 1 209 ? 8.234   28.984  -13.368 1.00 18.92 ?  319  ALA   A O     1 
ATOM   1233 C  CB    . ALA   A 1 209 ? 5.770   27.130  -12.166 1.00 18.19 ?  319  ALA   A CB    1 
ATOM   1234 N  N     . ALA   A 1 210 ? 8.575   26.769  -13.616 1.00 17.97 ?  320  ALA   A N     1 
ATOM   1235 C  CA    . ALA   A 1 210 ? 10.026  26.936  -13.663 1.00 16.96 ?  320  ALA   A CA    1 
ATOM   1236 C  C     . ALA   A 1 210 ? 10.453  27.751  -14.882 1.00 18.39 ?  320  ALA   A C     1 
ATOM   1237 O  O     . ALA   A 1 210 ? 11.320  28.629  -14.777 1.00 19.48 ?  320  ALA   A O     1 
ATOM   1238 C  CB    . ALA   A 1 210 ? 10.709  25.564  -13.673 1.00 17.13 ?  320  ALA   A CB    1 
ATOM   1239 N  N     . ALA   A 1 211 ? 9.839   27.487  -16.043 1.00 19.92 ?  321  ALA   A N     1 
ATOM   1240 C  CA    . ALA   A 1 211 ? 10.162  28.258  -17.245 1.00 21.77 ?  321  ALA   A CA    1 
ATOM   1241 C  C     . ALA   A 1 211 ? 9.858   29.749  -17.066 1.00 19.74 ?  321  ALA   A C     1 
ATOM   1242 O  O     . ALA   A 1 211 ? 10.620  30.608  -17.538 1.00 22.09 ?  321  ALA   A O     1 
ATOM   1243 C  CB    . ALA   A 1 211 ? 9.397   27.687  -18.437 1.00 21.65 ?  321  ALA   A CB    1 
ATOM   1244 N  N     . ALA   A 1 212 ? 8.760   30.083  -16.372 1.00 18.65 ?  322  ALA   A N     1 
ATOM   1245 C  CA    . ALA   A 1 212 ? 8.436   31.498  -16.164 1.00 18.85 ?  322  ALA   A CA    1 
ATOM   1246 C  C     . ALA   A 1 212 ? 9.480   32.202  -15.302 1.00 23.12 ?  322  ALA   A C     1 
ATOM   1247 O  O     . ALA   A 1 212 ? 9.811   33.370  -15.559 1.00 22.16 ?  322  ALA   A O     1 
ATOM   1248 C  CB    . ALA   A 1 212 ? 7.042   31.638  -15.544 1.00 18.94 ?  322  ALA   A CB    1 
ATOM   1249 N  N     . LEU   A 1 213 ? 10.008  31.518  -14.269 1.00 19.68 ?  323  LEU   A N     1 
ATOM   1250 C  CA    . LEU   A 1 213 ? 11.071  32.106  -13.451 1.00 20.50 ?  323  LEU   A CA    1 
ATOM   1251 C  C     . LEU   A 1 213 ? 12.368  32.254  -14.245 1.00 21.01 ?  323  LEU   A C     1 
ATOM   1252 O  O     . LEU   A 1 213 ? 13.102  33.235  -14.063 1.00 22.34 ?  323  LEU   A O     1 
ATOM   1253 C  CB    . LEU   A 1 213 ? 11.316  31.266  -12.183 1.00 18.65 ?  323  LEU   A CB    1 
ATOM   1254 C  CG    . LEU   A 1 213 ? 10.412  31.563  -10.978 1.00 20.71 ?  323  LEU   A CG    1 
ATOM   1255 C  CD1   . LEU   A 1 213 ? 10.579  30.507  -9.871  1.00 21.09 ?  323  LEU   A CD1   1 
ATOM   1256 C  CD2   . LEU   A 1 213 ? 10.680  32.988  -10.412 1.00 20.87 ?  323  LEU   A CD2   1 
ATOM   1257 N  N     . VAL   A 1 214 ? 12.668  31.297  -15.127 1.00 21.54 ?  324  VAL   A N     1 
ATOM   1258 C  CA    . VAL   A 1 214 ? 13.855  31.416  -15.984 1.00 22.92 ?  324  VAL   A CA    1 
ATOM   1259 C  C     . VAL   A 1 214 ? 13.756  32.666  -16.855 1.00 22.82 ?  324  VAL   A C     1 
ATOM   1260 O  O     . VAL   A 1 214 ? 14.723  33.428  -16.998 1.00 23.73 ?  324  VAL   A O     1 
ATOM   1261 C  CB    . VAL   A 1 214 ? 14.028  30.150  -16.845 1.00 22.78 ?  324  VAL   A CB    1 
ATOM   1262 C  CG1   . VAL   A 1 214 ? 15.093  30.384  -17.922 1.00 24.74 ?  324  VAL   A CG1   1 
ATOM   1263 C  CG2   . VAL   A 1 214 ? 14.400  28.933  -15.977 1.00 22.37 ?  324  VAL   A CG2   1 
ATOM   1264 N  N     . ASP   A 1 215 ? 12.587  32.880  -17.468 1.00 22.03 ?  325  ASP   A N     1 
ATOM   1265 C  CA    . ASP   A 1 215 ? 12.398  34.036  -18.351 1.00 25.83 ?  325  ASP   A CA    1 
ATOM   1266 C  C     . ASP   A 1 215 ? 12.468  35.356  -17.595 1.00 28.20 ?  325  ASP   A C     1 
ATOM   1267 O  O     . ASP   A 1 215 ? 12.835  36.382  -18.179 1.00 28.22 ?  325  ASP   A O     1 
ATOM   1268 C  CB    . ASP   A 1 215 ? 11.065  33.921  -19.081 1.00 27.12 ?  325  ASP   A CB    1 
ATOM   1269 C  CG    . ASP   A 1 215 ? 11.066  32.826  -20.119 1.00 34.19 ?  325  ASP   A CG    1 
ATOM   1270 O  OD1   . ASP   A 1 215 ? 12.167  32.395  -20.527 1.00 38.92 ?  325  ASP   A OD1   1 
ATOM   1271 O  OD2   . ASP   A 1 215 ? 9.967   32.397  -20.528 1.00 42.17 -1 325  ASP   A OD2   1 
ATOM   1272 N  N     . ALA   A 1 216 ? 12.133  35.356  -16.308 1.00 23.67 ?  326  ALA   A N     1 
ATOM   1273 C  CA    . ALA   A 1 216 ? 12.185  36.568  -15.497 1.00 24.72 ?  326  ALA   A CA    1 
ATOM   1274 C  C     . ALA   A 1 216 ? 13.600  36.928  -15.030 1.00 24.25 ?  326  ALA   A C     1 
ATOM   1275 O  O     . ALA   A 1 216 ? 13.783  38.019  -14.470 1.00 28.15 ?  326  ALA   A O     1 
ATOM   1276 C  CB    . ALA   A 1 216 ? 11.254  36.418  -14.287 1.00 24.96 ?  326  ALA   A CB    1 
ATOM   1277 N  N     . GLY   A 1 217 ? 14.587  36.053  -15.245 1.00 19.84 ?  327  GLY   A N     1 
ATOM   1278 C  CA    . GLY   A 1 217 ? 15.980  36.297  -14.896 1.00 21.24 ?  327  GLY   A CA    1 
ATOM   1279 C  C     . GLY   A 1 217 ? 16.523  35.603  -13.657 1.00 22.08 ?  327  GLY   A C     1 
ATOM   1280 O  O     . GLY   A 1 217 ? 17.607  35.974  -13.188 1.00 23.48 ?  327  GLY   A O     1 
ATOM   1281 N  N     . ALA   A 1 218 ? 15.814  34.613  -13.111 1.00 22.22 ?  328  ALA   A N     1 
ATOM   1282 C  CA    . ALA   A 1 218 ? 16.275  33.975  -11.883 1.00 19.01 ?  328  ALA   A CA    1 
ATOM   1283 C  C     . ALA   A 1 218 ? 17.648  33.336  -12.064 1.00 19.34 ?  328  ALA   A C     1 
ATOM   1284 O  O     . ALA   A 1 218 ? 17.941  32.721  -13.098 1.00 21.97 ?  328  ALA   A O     1 
ATOM   1285 C  CB    . ALA   A 1 218 ? 15.261  32.912  -11.431 1.00 18.25 ?  328  ALA   A CB    1 
ATOM   1286 N  N     . ASP   A 1 219 ? 18.481  33.441  -11.021 1.00 17.04 ?  329  ASP   A N     1 
ATOM   1287 C  CA    . ASP   A 1 219 ? 19.797  32.799  -11.003 1.00 19.86 ?  329  ASP   A CA    1 
ATOM   1288 C  C     . ASP   A 1 219 ? 19.755  31.364  -10.469 1.00 22.01 ?  329  ASP   A C     1 
ATOM   1289 O  O     . ASP   A 1 219 ? 20.751  30.634  -10.604 1.00 21.25 ?  329  ASP   A O     1 
ATOM   1290 C  CB    . ASP   A 1 219 ? 20.789  33.634  -10.166 1.00 20.28 ?  329  ASP   A CB    1 
ATOM   1291 C  CG    . ASP   A 1 219 ? 21.114  34.985  -10.804 1.00 24.36 ?  329  ASP   A CG    1 
ATOM   1292 O  OD1   . ASP   A 1 219 ? 21.396  35.028  -12.022 1.00 22.77 ?  329  ASP   A OD1   1 
ATOM   1293 O  OD2   . ASP   A 1 219 ? 21.085  35.998  -10.078 1.00 23.67 -1 329  ASP   A OD2   1 
ATOM   1294 N  N     . ALA   A 1 220 ? 18.639  30.962  -9.847  1.00 18.89 ?  330  ALA   A N     1 
ATOM   1295 C  CA    . ALA   A 1 220 ? 18.324  29.581  -9.473  1.00 17.30 ?  330  ALA   A CA    1 
ATOM   1296 C  C     . ALA   A 1 220 ? 16.820  29.503  -9.212  1.00 17.70 ?  330  ALA   A C     1 
ATOM   1297 O  O     . ALA   A 1 220 ? 16.188  30.517  -8.900  1.00 18.65 ?  330  ALA   A O     1 
ATOM   1298 C  CB    . ALA   A 1 220 ? 19.106  29.139  -8.236  1.00 18.49 ?  330  ALA   A CB    1 
ATOM   1299 N  N     . VAL   A 1 221 ? 16.254  28.290  -9.333  1.00 17.29 ?  331  VAL   A N     1 
ATOM   1300 C  CA    . VAL   A 1 221 ? 14.812  28.030  -9.168  1.00 17.90 ?  331  VAL   A CA    1 
ATOM   1301 C  C     . VAL   A 1 221 ? 14.622  27.015  -8.046  1.00 16.25 ?  331  VAL   A C     1 
ATOM   1302 O  O     . VAL   A 1 221 ? 15.226  25.939  -8.081  1.00 18.16 ?  331  VAL   A O     1 
ATOM   1303 C  CB    . VAL   A 1 221 ? 14.177  27.511  -10.479 1.00 16.95 ?  331  VAL   A CB    1 
ATOM   1304 C  CG1   . VAL   A 1 221 ? 12.743  26.953  -10.266 1.00 17.55 ?  331  VAL   A CG1   1 
ATOM   1305 C  CG2   . VAL   A 1 221 ? 14.142  28.631  -11.529 1.00 18.91 ?  331  VAL   A CG2   1 
ATOM   1306 N  N     . LYS   A 1 222 ? 13.768  27.332  -7.069  1.00 17.73 ?  332  LYS   A N     1 
ATOM   1307 C  CA    . LYS   A 1 222 ? 13.570  26.456  -5.912  1.00 18.12 ?  332  LYS   A CA    1 
ATOM   1308 C  C     . LYS   A 1 222 ? 12.247  25.693  -6.040  1.00 14.87 ?  332  LYS   A C     1 
ATOM   1309 O  O     . LYS   A 1 222 ? 11.199  26.296  -6.291  1.00 17.39 ?  332  LYS   A O     1 
ATOM   1310 C  CB    . LYS   A 1 222 ? 13.629  27.254  -4.599  1.00 15.51 ?  332  LYS   A CB    1 
ATOM   1311 C  CG    . LYS   A 1 222 ? 13.723  26.375  -3.317  1.00 18.22 ?  332  LYS   A CG    1 
ATOM   1312 C  CD    . LYS   A 1 222 ? 14.579  26.998  -2.178  1.00 17.83 ?  332  LYS   A CD    1 
ATOM   1313 C  CE    . LYS   A 1 222 ? 13.974  28.282  -1.584  1.00 16.52 ?  332  LYS   A CE    1 
ATOM   1314 N  NZ    . LYS   A 1 222 ? 12.624  28.059  -0.941  1.00 17.61 ?  332  LYS   A NZ    1 
ATOM   1315 N  N     . VAL   A 1 223 ? 12.305  24.365  -5.858  1.00 15.11 ?  333  VAL   A N     1 
ATOM   1316 C  CA    . VAL   A 1 223 ? 11.201  23.443  -6.164  1.00 14.94 ?  333  VAL   A CA    1 
ATOM   1317 C  C     . VAL   A 1 223 ? 10.664  22.807  -4.883  1.00 16.10 ?  333  VAL   A C     1 
ATOM   1318 O  O     . VAL   A 1 223 ? 11.427  22.228  -4.092  1.00 17.54 ?  333  VAL   A O     1 
ATOM   1319 C  CB    . VAL   A 1 223 ? 11.661  22.344  -7.148  1.00 15.11 ?  333  VAL   A CB    1 
ATOM   1320 C  CG1   . VAL   A 1 223 ? 10.616  21.231  -7.282  1.00 16.16 ?  333  VAL   A CG1   1 
ATOM   1321 C  CG2   . VAL   A 1 223 ? 12.037  22.932  -8.520  1.00 18.76 ?  333  VAL   A CG2   1 
ATOM   1322 N  N     . GLY   A 1 224 ? 9.336   22.843  -4.719  1.00 15.85 ?  334  GLY   A N     1 
ATOM   1323 C  CA    . GLY   A 1 224 ? 8.669   22.182  -3.602  1.00 16.30 ?  334  GLY   A CA    1 
ATOM   1324 C  C     . GLY   A 1 224 ? 7.338   22.816  -3.215  1.00 17.36 ?  334  GLY   A C     1 
ATOM   1325 O  O     . GLY   A 1 224 ? 7.321   23.872  -2.575  1.00 17.96 ?  334  GLY   A O     1 
ATOM   1326 N  N     . VAL   A 1 225 ? 6.214   22.199  -3.611  1.00 16.79 ?  335  VAL   A N     1 
ATOM   1327 C  CA    . VAL   A 1 225 ? 4.868   22.600  -3.152  1.00 16.65 ?  335  VAL   A CA    1 
ATOM   1328 C  C     . VAL   A 1 225 ? 4.188   21.318  -2.667  1.00 18.14 ?  335  VAL   A C     1 
ATOM   1329 O  O     . VAL   A 1 225 ? 3.909   20.413  -3.471  1.00 18.60 ?  335  VAL   A O     1 
ATOM   1330 C  CB    . VAL   A 1 225 ? 4.031   23.283  -4.253  1.00 17.16 ?  335  VAL   A CB    1 
ATOM   1331 C  CG1   . VAL   A 1 225 ? 2.629   23.712  -3.695  1.00 17.54 ?  335  VAL   A CG1   1 
ATOM   1332 C  CG2   . VAL   A 1 225 ? 4.750   24.490  -4.840  1.00 20.70 ?  335  VAL   A CG2   1 
ATOM   1333 N  N     . GLY   A 1 226 ? 3.987   21.204  -1.349  1.00 20.16 ?  336  GLY   A N     1 
ATOM   1334 C  CA    . GLY   A 1 226 ? 3.412   20.000  -0.769  1.00 23.24 ?  336  GLY   A CA    1 
ATOM   1335 C  C     . GLY   A 1 226 ? 4.289   19.075  0.087   1.00 28.41 ?  336  GLY   A C     1 
ATOM   1336 O  O     . GLY   A 1 226 ? 3.775   18.407  0.994   1.00 31.85 ?  336  GLY   A O     1 
ATOM   1337 N  N     . PRO   A 1 227 ? 5.600   18.975  -0.176  1.00 22.30 ?  337  PRO   A N     1 
ATOM   1338 C  CA    . PRO   A 1 227 ? 6.387   17.860  0.384   1.00 21.69 ?  337  PRO   A CA    1 
ATOM   1339 C  C     . PRO   A 1 227 ? 6.970   18.004  1.791   1.00 22.02 ?  337  PRO   A C     1 
ATOM   1340 O  O     . PRO   A 1 227 ? 7.499   17.005  2.316   1.00 23.81 ?  337  PRO   A O     1 
ATOM   1341 C  CB    . PRO   A 1 227 ? 7.538   17.747  -0.627  1.00 25.01 ?  337  PRO   A CB    1 
ATOM   1342 C  CG    . PRO   A 1 227 ? 7.807   19.158  -0.982  1.00 21.90 ?  337  PRO   A CG    1 
ATOM   1343 C  CD    . PRO   A 1 227 ? 6.429   19.810  -1.068  1.00 25.70 ?  337  PRO   A CD    1 
ATOM   1344 N  N     . GLY   A 1 228 ? 6.916   19.179  2.412   1.00 21.62 ?  338  GLY   A N     1 
ATOM   1345 C  CA    . GLY   A 1 228 ? 7.663   19.400  3.642   1.00 21.87 ?  338  GLY   A CA    1 
ATOM   1346 C  C     . GLY   A 1 228 ? 7.090   18.646  4.829   1.00 26.05 ?  338  GLY   A C     1 
ATOM   1347 O  O     . GLY   A 1 228 ? 5.886   18.402  4.925   1.00 25.76 ?  338  GLY   A O     1 
ATOM   1348 N  N     . SER   A 1 229 ? 7.974   18.313  5.777   1.00 21.02 ?  339  SER   A N     1 
ATOM   1349 C  CA    . SER   A 1 229 ? 7.569   17.492  6.922   1.00 21.81 ?  339  SER   A CA    1 
ATOM   1350 C  C     . SER   A 1 229 ? 6.494   18.163  7.771   1.00 28.68 ?  339  SER   A C     1 
ATOM   1351 O  O     . SER   A 1 229 ? 5.660   17.471  8.370   1.00 28.25 ?  339  SER   A O     1 
ATOM   1352 C  CB    . SER   A 1 229 ? 8.785   17.171  7.798   1.00 23.95 ?  339  SER   A CB    1 
ATOM   1353 O  OG    . SER   A 1 229 ? 9.268   18.348  8.432   1.00 24.66 ?  339  SER   A OG    1 
ATOM   1354 N  N     . ILE   A 1 230 ? 6.510   19.496  7.852   1.00 22.52 ?  340  ILE   A N     1 
ATOM   1355 C  CA    . ILE   A 1 230 ? 5.549   20.271  8.636   1.00 23.17 ?  340  ILE   A CA    1 
ATOM   1356 C  C     . ILE   A 1 230 ? 4.456   20.894  7.762   1.00 24.97 ?  340  ILE   A C     1 
ATOM   1357 O  O     . ILE   A 1 230 ? 3.691   21.737  8.245   1.00 25.34 ?  340  ILE   A O     1 
ATOM   1358 C  CB    . ILE   A 1 230 ? 6.256   21.358  9.475   1.00 25.09 ?  340  ILE   A CB    1 
ATOM   1359 C  CG1   . ILE   A 1 230 ? 7.371   22.082  8.693   1.00 22.49 ?  340  ILE   A CG1   1 
ATOM   1360 C  CG2   . ILE   A 1 230 ? 6.866   20.755  10.749  1.00 25.59 ?  340  ILE   A CG2   1 
ATOM   1361 C  CD1   . ILE   A 1 230 ? 6.933   22.804  7.399   1.00 23.93 ?  340  ILE   A CD1   1 
ATOM   1362 N  N     . CYS   A 1 231 ? 4.360   20.496  6.491   1.00 21.56 ?  341  CYS   A N     1 
ATOM   1363 C  CA    . CYS   A 1 231 ? 3.389   21.077  5.564   1.00 24.46 ?  341  CYS   A CA    1 
ATOM   1364 C  C     . CYS   A 1 231 ? 2.015   20.425  5.700   1.00 26.72 ?  341  CYS   A C     1 
ATOM   1365 O  O     . CYS   A 1 231 ? 1.898   19.201  5.811   1.00 25.57 ?  341  CYS   A O     1 
ATOM   1366 C  CB    . CYS   A 1 231 ? 3.891   20.917  4.124   1.00 32.29 ?  341  CYS   A CB    1 
ATOM   1367 S  SG    . CYS   A 1 231 ? 2.752   21.533  2.836   1.00 30.30 ?  341  CYS   A SG    1 
ATOM   1368 N  N     . THR   A 1 232 ? 0.962   21.252  5.693   1.00 22.47 ?  342  THR   A N     1 
ATOM   1369 C  CA    . THR   A 1 232 ? -0.401  20.738  5.599   1.00 20.99 ?  342  THR   A CA    1 
ATOM   1370 C  C     . THR   A 1 232 ? -1.148  21.287  4.388   1.00 20.48 ?  342  THR   A C     1 
ATOM   1371 O  O     . THR   A 1 232 ? -2.364  21.080  4.282   1.00 20.69 ?  342  THR   A O     1 
ATOM   1372 C  CB    . THR   A 1 232 ? -1.185  21.007  6.889   1.00 23.63 ?  342  THR   A CB    1 
ATOM   1373 O  OG1   . THR   A 1 232 ? -1.286  22.414  7.131   1.00 22.49 ?  342  THR   A OG1   1 
ATOM   1374 C  CG2   . THR   A 1 232 ? -0.482  20.338  8.078   1.00 26.63 ?  342  THR   A CG2   1 
ATOM   1375 N  N     . THR   A 1 233 ? -0.444  21.933  3.450   1.00 20.85 ?  343  THR   A N     1 
ATOM   1376 C  CA    . THR   A 1 233 ? -1.059  22.352  2.190   1.00 19.10 ?  343  THR   A CA    1 
ATOM   1377 C  C     . THR   A 1 233 ? -1.786  21.190  1.513   1.00 17.79 ?  343  THR   A C     1 
ATOM   1378 O  O     . THR   A 1 233 ? -2.885  21.369  0.953   1.00 18.49 ?  343  THR   A O     1 
ATOM   1379 C  CB    . THR   A 1 233 ? 0.013   22.936  1.262   1.00 19.03 ?  343  THR   A CB    1 
ATOM   1380 O  OG1   . THR   A 1 233 ? 0.621   24.072  1.895   1.00 19.96 ?  343  THR   A OG1   1 
ATOM   1381 C  CG2   . THR   A 1 233 ? -0.573  23.346  -0.095  1.00 21.43 ?  343  THR   A CG2   1 
ATOM   1382 N  N     . ARG   A 1 234 ? -1.194  19.989  1.558   1.00 19.41 ?  344  ARG   A N     1 
ATOM   1383 C  CA    . ARG   A 1 234 ? -1.797  18.837  0.887   1.00 20.13 ?  344  ARG   A CA    1 
ATOM   1384 C  C     . ARG   A 1 234 ? -3.177  18.496  1.435   1.00 21.37 ?  344  ARG   A C     1 
ATOM   1385 O  O     . ARG   A 1 234 ? -4.052  18.068  0.676   1.00 23.90 ?  344  ARG   A O     1 
ATOM   1386 C  CB    . ARG   A 1 234 ? -0.883  17.608  0.984   1.00 23.16 ?  344  ARG   A CB    1 
ATOM   1387 C  CG    . ARG   A 1 234 ? 0.226   17.647  -0.036  1.00 25.60 ?  344  ARG   A CG    1 
ATOM   1388 C  CD    . ARG   A 1 234 ? 1.098   16.368  -0.136  1.00 36.77 ?  344  ARG   A CD    1 
ATOM   1389 N  NE    . ARG   A 1 234 ? 2.308   16.720  -0.885  1.00 48.55 ?  344  ARG   A NE    1 
ATOM   1390 C  CZ    . ARG   A 1 234 ? 3.105   15.879  -1.541  1.00 46.72 ?  344  ARG   A CZ    1 
ATOM   1391 N  NH1   . ARG   A 1 234 ? 2.846   14.578  -1.578  1.00 45.61 ?  344  ARG   A NH1   1 
ATOM   1392 N  NH2   . ARG   A 1 234 ? 4.176   16.364  -2.170  1.00 41.01 ?  344  ARG   A NH2   1 
ATOM   1393 N  N     A VAL   A 1 235 ? -3.413  18.663  2.736   0.53 20.85 ?  345  VAL   A N     1 
ATOM   1394 N  N     B VAL   A 1 235 ? -3.374  18.649  2.743   0.47 20.83 ?  345  VAL   A N     1 
ATOM   1395 C  CA    A VAL   A 1 235 ? -4.730  18.302  3.262   0.53 22.26 ?  345  VAL   A CA    1 
ATOM   1396 C  CA    B VAL   A 1 235 ? -4.648  18.306  3.374   0.47 22.29 ?  345  VAL   A CA    1 
ATOM   1397 C  C     A VAL   A 1 235 ? -5.640  19.516  3.449   0.53 19.93 ?  345  VAL   A C     1 
ATOM   1398 C  C     B VAL   A 1 235 ? -5.596  19.501  3.435   0.47 19.94 ?  345  VAL   A C     1 
ATOM   1399 O  O     A VAL   A 1 235 ? -6.866  19.380  3.388   0.53 22.85 ?  345  VAL   A O     1 
ATOM   1400 O  O     B VAL   A 1 235 ? -6.807  19.343  3.255   0.47 22.68 ?  345  VAL   A O     1 
ATOM   1401 C  CB    A VAL   A 1 235 ? -4.611  17.503  4.573   0.53 26.82 ?  345  VAL   A CB    1 
ATOM   1402 C  CB    B VAL   A 1 235 ? -4.388  17.713  4.775   0.47 26.76 ?  345  VAL   A CB    1 
ATOM   1403 C  CG1   A VAL   A 1 235 ? -3.981  16.145  4.297   0.53 29.68 ?  345  VAL   A CG1   1 
ATOM   1404 C  CG1   B VAL   A 1 235 ? -5.614  17.863  5.655   0.47 28.35 ?  345  VAL   A CG1   1 
ATOM   1405 C  CG2   A VAL   A 1 235 ? -3.802  18.270  5.586   0.53 19.74 ?  345  VAL   A CG2   1 
ATOM   1406 C  CG2   B VAL   A 1 235 ? -3.995  16.249  4.653   0.47 30.73 ?  345  VAL   A CG2   1 
ATOM   1407 N  N     . VAL   A 1 236 ? -5.068  20.705  3.674   1.00 18.47 ?  346  VAL   A N     1 
ATOM   1408 C  CA    . VAL   A 1 236 ? -5.904  21.904  3.831   1.00 18.04 ?  346  VAL   A CA    1 
ATOM   1409 C  C     . VAL   A 1 236 ? -6.435  22.403  2.487   1.00 19.19 ?  346  VAL   A C     1 
ATOM   1410 O  O     . VAL   A 1 236 ? -7.612  22.784  2.372   1.00 19.63 ?  346  VAL   A O     1 
ATOM   1411 C  CB    . VAL   A 1 236 ? -5.093  23.000  4.558   1.00 20.35 ?  346  VAL   A CB    1 
ATOM   1412 C  CG1   . VAL   A 1 236 ? -5.774  24.376  4.449   1.00 23.40 ?  346  VAL   A CG1   1 
ATOM   1413 C  CG2   . VAL   A 1 236 ? -4.885  22.610  6.009   1.00 22.95 ?  346  VAL   A CG2   1 
ATOM   1414 N  N     . ALA   A 1 237 ? -5.569  22.462  1.469   1.00 18.28 ?  347  ALA   A N     1 
ATOM   1415 C  CA    . ALA   A 1 237 ? -5.947  22.925  0.139   1.00 17.04 ?  347  ALA   A CA    1 
ATOM   1416 C  C     . ALA   A 1 237 ? -6.145  21.783  -0.861  1.00 18.78 ?  347  ALA   A C     1 
ATOM   1417 O  O     . ALA   A 1 237 ? -6.735  22.004  -1.925  1.00 17.92 ?  347  ALA   A O     1 
ATOM   1418 C  CB    . ALA   A 1 237 ? -4.881  23.895  -0.396  1.00 18.67 ?  347  ALA   A CB    1 
ATOM   1419 N  N     . GLY   A 1 238 ? -5.659  20.579  -0.549  1.00 17.41 ?  348  GLY   A N     1 
ATOM   1420 C  CA    . GLY   A 1 238 ? -5.686  19.481  -1.512  1.00 17.43 ?  348  GLY   A CA    1 
ATOM   1421 C  C     . GLY   A 1 238 ? -4.738  19.635  -2.694  1.00 15.89 ?  348  GLY   A C     1 
ATOM   1422 O  O     . GLY   A 1 238 ? -4.977  19.018  -3.753  1.00 16.93 ?  348  GLY   A O     1 
ATOM   1423 N  N     . VAL   A 1 239 ? -3.658  20.418  -2.526  1.00 16.29 ?  349  VAL   A N     1 
ATOM   1424 C  CA    . VAL   A 1 239 ? -2.734  20.844  -3.581  1.00 14.91 ?  349  VAL   A CA    1 
ATOM   1425 C  C     . VAL   A 1 239 ? -1.329  20.307  -3.299  1.00 16.75 ?  349  VAL   A C     1 
ATOM   1426 O  O     . VAL   A 1 239 ? -0.875  20.326  -2.148  1.00 16.79 ?  349  VAL   A O     1 
ATOM   1427 C  CB    . VAL   A 1 239 ? -2.687  22.385  -3.683  1.00 14.90 ?  349  VAL   A CB    1 
ATOM   1428 C  CG1   . VAL   A 1 239 ? -1.498  22.843  -4.562  1.00 17.99 ?  349  VAL   A CG1   1 
ATOM   1429 C  CG2   . VAL   A 1 239 ? -4.029  22.943  -4.185  1.00 15.45 ?  349  VAL   A CG2   1 
ATOM   1430 N  N     . GLY   A 1 240 ? -0.637  19.846  -4.342  1.00 15.38 ?  350  GLY   A N     1 
ATOM   1431 C  CA    . GLY   A 1 240 ? 0.761   19.461  -4.189  1.00 16.96 ?  350  GLY   A CA    1 
ATOM   1432 C  C     . GLY   A 1 240 ? 1.282   18.690  -5.388  1.00 18.48 ?  350  GLY   A C     1 
ATOM   1433 O  O     . GLY   A 1 240 ? 0.553   18.404  -6.347  1.00 17.76 ?  350  GLY   A O     1 
ATOM   1434 N  N     . ALA   A 1 241 ? 2.585   18.336  -5.309  1.00 17.20 ?  351  ALA   A N     1 
ATOM   1435 C  CA    . ALA   A 1 241 ? 3.227   17.547  -6.359  1.00 17.21 ?  351  ALA   A CA    1 
ATOM   1436 C  C     . ALA   A 1 241 ? 4.313   16.654  -5.763  1.00 17.73 ?  351  ALA   A C     1 
ATOM   1437 O  O     . ALA   A 1 241 ? 5.253   17.176  -5.152  1.00 19.34 ?  351  ALA   A O     1 
ATOM   1438 C  CB    . ALA   A 1 241 ? 3.852   18.449  -7.431  1.00 20.49 ?  351  ALA   A CB    1 
ATOM   1439 N  N     . PRO   A 1 242 ? 4.230   15.326  -5.901  1.00 14.84 ?  352  PRO   A N     1 
ATOM   1440 C  CA    . PRO   A 1 242 ? 5.329   14.464  -5.429  1.00 16.56 ?  352  PRO   A CA    1 
ATOM   1441 C  C     . PRO   A 1 242 ? 6.692   14.942  -5.960  1.00 17.68 ?  352  PRO   A C     1 
ATOM   1442 O  O     . PRO   A 1 242 ? 6.837   15.291  -7.133  1.00 16.26 ?  352  PRO   A O     1 
ATOM   1443 C  CB    . PRO   A 1 242 ? 4.933   13.079  -5.958  1.00 15.71 ?  352  PRO   A CB    1 
ATOM   1444 C  CG    . PRO   A 1 242 ? 3.377   13.126  -5.948  1.00 17.04 ?  352  PRO   A CG    1 
ATOM   1445 C  CD    . PRO   A 1 242 ? 3.074   14.546  -6.408  1.00 16.14 ?  352  PRO   A CD    1 
ATOM   1446 N  N     A GLN   A 1 243 ? 7.715   14.911  -5.086  0.70 17.31 ?  353  GLN   A N     1 
ATOM   1447 N  N     B GLN   A 1 243 ? 7.704   14.922  -5.086  0.30 17.32 ?  353  GLN   A N     1 
ATOM   1448 C  CA    A GLN   A 1 243 ? 8.921   15.725  -5.303  0.70 16.44 ?  353  GLN   A CA    1 
ATOM   1449 C  CA    B GLN   A 1 243 ? 8.913   15.709  -5.340  0.30 16.47 ?  353  GLN   A CA    1 
ATOM   1450 C  C     A GLN   A 1 243 ? 9.898   15.172  -6.360  0.70 16.60 ?  353  GLN   A C     1 
ATOM   1451 C  C     B GLN   A 1 243 ? 9.746   15.175  -6.509  0.30 16.73 ?  353  GLN   A C     1 
ATOM   1452 O  O     A GLN   A 1 243 ? 10.621  15.964  -6.981  0.70 15.06 ?  353  GLN   A O     1 
ATOM   1453 O  O     B GLN   A 1 243 ? 10.243  15.967  -7.322  0.30 16.29 ?  353  GLN   A O     1 
ATOM   1454 C  CB    A GLN   A 1 243 ? 9.647   15.922  -3.962  0.70 18.70 ?  353  GLN   A CB    1 
ATOM   1455 C  CB    B GLN   A 1 243 ? 9.763   15.790  -4.071  0.30 18.71 ?  353  GLN   A CB    1 
ATOM   1456 C  CG    A GLN   A 1 243 ? 10.829  16.896  -3.991  0.70 17.49 ?  353  GLN   A CG    1 
ATOM   1457 C  CG    B GLN   A 1 243 ? 9.522   17.050  -3.248  0.30 20.47 ?  353  GLN   A CG    1 
ATOM   1458 C  CD    A GLN   A 1 243 ? 10.411  18.377  -3.994  0.70 19.02 ?  353  GLN   A CD    1 
ATOM   1459 C  CD    B GLN   A 1 243 ? 10.117  18.303  -3.884  0.30 18.55 ?  353  GLN   A CD    1 
ATOM   1460 O  OE1   A GLN   A 1 243 ? 9.375   18.759  -4.555  0.70 16.86 ?  353  GLN   A OE1   1 
ATOM   1461 O  OE1   B GLN   A 1 243 ? 9.800   18.659  -5.025  0.30 16.93 ?  353  GLN   A OE1   1 
ATOM   1462 N  NE2   A GLN   A 1 243 ? 11.231  19.214  -3.363  0.70 20.12 ?  353  GLN   A NE2   1 
ATOM   1463 N  NE2   B GLN   A 1 243 ? 10.988  18.980  -3.141  0.30 19.74 ?  353  GLN   A NE2   1 
ATOM   1464 N  N     . ILE   A 1 244 ? 9.956   13.855  -6.604  1.00 16.91 ?  354  ILE   A N     1 
ATOM   1465 C  CA    . ILE   A 1 244 ? 10.839  13.362  -7.677  1.00 15.94 ?  354  ILE   A CA    1 
ATOM   1466 C  C     . ILE   A 1 244 ? 10.304  13.802  -9.041  1.00 16.42 ?  354  ILE   A C     1 
ATOM   1467 O  O     . ILE   A 1 244 ? 11.054  14.340  -9.868  1.00 16.34 ?  354  ILE   A O     1 
ATOM   1468 C  CB    . ILE   A 1 244 ? 11.052  11.834  -7.591  1.00 15.62 ?  354  ILE   A CB    1 
ATOM   1469 C  CG1   . ILE   A 1 244 ? 11.957  11.474  -6.393  1.00 16.83 ?  354  ILE   A CG1   1 
ATOM   1470 C  CG2   . ILE   A 1 244 ? 11.590  11.240  -8.922  1.00 18.06 ?  354  ILE   A CG2   1 
ATOM   1471 C  CD1   . ILE   A 1 244 ? 13.463  11.809  -6.577  1.00 17.16 ?  354  ILE   A CD1   1 
ATOM   1472 N  N     . THR   A 1 245 ? 8.983   13.679  -9.261  1.00 14.46 ?  355  THR   A N     1 
ATOM   1473 C  CA    . THR   A 1 245 ? 8.384   14.163  -10.512 1.00 14.48 ?  355  THR   A CA    1 
ATOM   1474 C  C     . THR   A 1 245 ? 8.478   15.697  -10.635 1.00 17.23 ?  355  THR   A C     1 
ATOM   1475 O  O     . THR   A 1 245 ? 8.746   16.226  -11.729 1.00 16.81 ?  355  THR   A O     1 
ATOM   1476 C  CB    . THR   A 1 245 ? 6.928   13.677  -10.590 1.00 16.56 ?  355  THR   A CB    1 
ATOM   1477 O  OG1   . THR   A 1 245 ? 6.893   12.240  -10.681 1.00 17.33 ?  355  THR   A OG1   1 
ATOM   1478 C  CG2   . THR   A 1 245 ? 6.192   14.300  -11.787 1.00 17.25 ?  355  THR   A CG2   1 
ATOM   1479 N  N     . ALA   A 1 246 ? 8.277   16.430  -9.528  1.00 16.42 ?  356  ALA   A N     1 
ATOM   1480 C  CA    . ALA   A 1 246 ? 8.406   17.892  -9.575  1.00 15.54 ?  356  ALA   A CA    1 
ATOM   1481 C  C     . ALA   A 1 246 ? 9.821   18.315  -9.987  1.00 17.41 ?  356  ALA   A C     1 
ATOM   1482 O  O     . ALA   A 1 246 ? 9.984   19.244  -10.788 1.00 16.16 ?  356  ALA   A O     1 
ATOM   1483 C  CB    . ALA   A 1 246 ? 8.019   18.499  -8.220  1.00 14.59 ?  356  ALA   A CB    1 
ATOM   1484 N  N     . ILE   A 1 247 ? 10.855  17.635  -9.466  1.00 15.46 ?  357  ILE   A N     1 
ATOM   1485 C  CA    . ILE   A 1 247 ? 12.240  17.948  -9.842  1.00 15.61 ?  357  ILE   A CA    1 
ATOM   1486 C  C     . ILE   A 1 247 ? 12.488  17.613  -11.313 1.00 18.90 ?  357  ILE   A C     1 
ATOM   1487 O  O     . ILE   A 1 247 ? 13.064  18.419  -12.054 1.00 17.57 ?  357  ILE   A O     1 
ATOM   1488 C  CB    . ILE   A 1 247 ? 13.233  17.209  -8.922  1.00 14.29 ?  357  ILE   A CB    1 
ATOM   1489 C  CG1   . ILE   A 1 247 ? 13.142  17.744  -7.481  1.00 15.44 ?  357  ILE   A CG1   1 
ATOM   1490 C  CG2   . ILE   A 1 247 ? 14.689  17.354  -9.459  1.00 16.41 ?  357  ILE   A CG2   1 
ATOM   1491 C  CD1   . ILE   A 1 247 ? 13.839  16.838  -6.427  1.00 17.00 ?  357  ILE   A CD1   1 
ATOM   1492 N  N     . LEU   A 1 248 ? 12.063  16.411  -11.759 1.00 16.62 ?  358  LEU   A N     1 
ATOM   1493 C  CA    . LEU   A 1 248 ? 12.259  16.031  -13.165 1.00 16.52 ?  358  LEU   A CA    1 
ATOM   1494 C  C     . LEU   A 1 248 ? 11.622  17.047  -14.119 1.00 18.89 ?  358  LEU   A C     1 
ATOM   1495 O  O     . LEU   A 1 248 ? 12.220  17.406  -15.148 1.00 18.68 ?  358  LEU   A O     1 
ATOM   1496 C  CB    . LEU   A 1 248 ? 11.696  14.621  -13.423 1.00 17.14 ?  358  LEU   A CB    1 
ATOM   1497 C  CG    . LEU   A 1 248 ? 12.426  13.414  -12.813 1.00 15.51 ?  358  LEU   A CG    1 
ATOM   1498 C  CD1   . LEU   A 1 248 ? 11.550  12.141  -12.875 1.00 18.11 ?  358  LEU   A CD1   1 
ATOM   1499 C  CD2   . LEU   A 1 248 ? 13.817  13.150  -13.450 1.00 17.64 ?  358  LEU   A CD2   1 
ATOM   1500 N  N     . GLU   A 1 249 ? 10.428  17.545  -13.780 1.00 17.18 ?  359  GLU   A N     1 
ATOM   1501 C  CA    . GLU   A 1 249 ? 9.752   18.515  -14.646 1.00 17.42 ?  359  GLU   A CA    1 
ATOM   1502 C  C     . GLU   A 1 249 ? 10.426  19.891  -14.613 1.00 19.21 ?  359  GLU   A C     1 
ATOM   1503 O  O     . GLU   A 1 249 ? 10.603  20.529  -15.669 1.00 18.60 ?  359  GLU   A O     1 
ATOM   1504 C  CB    . GLU   A 1 249 ? 8.269   18.608  -14.249 1.00 16.97 ?  359  GLU   A CB    1 
ATOM   1505 C  CG    . GLU   A 1 249 ? 7.394   17.438  -14.780 1.00 16.14 ?  359  GLU   A CG    1 
ATOM   1506 C  CD    . GLU   A 1 249 ? 7.300   17.461  -16.313 1.00 19.19 ?  359  GLU   A CD    1 
ATOM   1507 O  OE1   . GLU   A 1 249 ? 6.673   18.404  -16.841 1.00 20.37 ?  359  GLU   A OE1   1 
ATOM   1508 O  OE2   . GLU   A 1 249 ? 7.874   16.560  -16.988 1.00 22.15 -1 359  GLU   A OE2   1 
ATOM   1509 N  N     . ALA   A 1 250 ? 10.793  20.386  -13.420 1.00 17.09 ?  360  ALA   A N     1 
ATOM   1510 C  CA    . ALA   A 1 250 ? 11.470  21.685  -13.338 1.00 15.81 ?  360  ALA   A CA    1 
ATOM   1511 C  C     . ALA   A 1 250 ? 12.821  21.663  -14.060 1.00 18.07 ?  360  ALA   A C     1 
ATOM   1512 O  O     . ALA   A 1 250 ? 13.207  22.645  -14.716 1.00 18.21 ?  360  ALA   A O     1 
ATOM   1513 C  CB    . ALA   A 1 250 ? 11.660  22.096  -11.867 1.00 16.92 ?  360  ALA   A CB    1 
ATOM   1514 N  N     . VAL   A 1 251 ? 13.562  20.553  -13.942 1.00 17.56 ?  361  VAL   A N     1 
ATOM   1515 C  CA    . VAL   A 1 251 ? 14.862  20.426  -14.597 1.00 18.03 ?  361  VAL   A CA    1 
ATOM   1516 C  C     . VAL   A 1 251 ? 14.707  20.426  -16.111 1.00 19.37 ?  361  VAL   A C     1 
ATOM   1517 O  O     . VAL   A 1 251 ? 15.563  20.959  -16.828 1.00 19.96 ?  361  VAL   A O     1 
ATOM   1518 C  CB    . VAL   A 1 251 ? 15.565  19.151  -14.085 1.00 18.03 ?  361  VAL   A CB    1 
ATOM   1519 C  CG1   . VAL   A 1 251 ? 16.771  18.798  -14.961 1.00 21.00 ?  361  VAL   A CG1   1 
ATOM   1520 C  CG2   . VAL   A 1 251 ? 16.012  19.342  -12.638 1.00 17.96 ?  361  VAL   A CG2   1 
ATOM   1521 N  N     . ALA   A 1 252 ? 13.600  19.872  -16.626 1.00 18.30 ?  362  ALA   A N     1 
ATOM   1522 C  CA    . ALA   A 1 252 ? 13.383  19.883  -18.072 1.00 19.88 ?  362  ALA   A CA    1 
ATOM   1523 C  C     . ALA   A 1 252 ? 13.331  21.309  -18.630 1.00 23.64 ?  362  ALA   A C     1 
ATOM   1524 O  O     . ALA   A 1 252 ? 13.675  21.524  -19.801 1.00 23.21 ?  362  ALA   A O     1 
ATOM   1525 C  CB    . ALA   A 1 252 ? 12.105  19.110  -18.421 1.00 22.72 ?  362  ALA   A CB    1 
ATOM   1526 N  N     . ALA   A 1 253 ? 12.902  22.292  -17.821 1.00 18.99 ?  363  ALA   A N     1 
ATOM   1527 C  CA    . ALA   A 1 253 ? 12.929  23.701  -18.218 1.00 22.37 ?  363  ALA   A CA    1 
ATOM   1528 C  C     . ALA   A 1 253 ? 14.234  24.412  -17.865 1.00 24.11 ?  363  ALA   A C     1 
ATOM   1529 O  O     . ALA   A 1 253 ? 14.691  25.279  -18.626 1.00 23.71 ?  363  ALA   A O     1 
ATOM   1530 C  CB    . ALA   A 1 253 ? 11.765  24.451  -17.571 1.00 18.89 ?  363  ALA   A CB    1 
ATOM   1531 N  N     . CYS   A 1 254 ? 14.840  24.079  -16.722 1.00 19.59 ?  364  CYS   A N     1 
ATOM   1532 C  CA    . CYS   A 1 254 ? 15.971  24.855  -16.220 1.00 17.93 ?  364  CYS   A CA    1 
ATOM   1533 C  C     . CYS   A 1 254 ? 17.307  24.386  -16.799 1.00 18.33 ?  364  CYS   A C     1 
ATOM   1534 O  O     . CYS   A 1 254 ? 18.169  25.225  -17.090 1.00 22.19 ?  364  CYS   A O     1 
ATOM   1535 C  CB    . CYS   A 1 254 ? 16.007  24.811  -14.685 1.00 17.92 ?  364  CYS   A CB    1 
ATOM   1536 S  SG    . CYS   A 1 254 ? 14.621  25.662  -13.852 1.00 19.10 ?  364  CYS   A SG    1 
ATOM   1537 N  N     . ARG   A 1 255 ? 17.518  23.071  -16.946 1.00 19.12 ?  365  ARG   A N     1 
ATOM   1538 C  CA    . ARG   A 1 255 ? 18.809  22.585  -17.447 1.00 19.96 ?  365  ARG   A CA    1 
ATOM   1539 C  C     . ARG   A 1 255 ? 19.143  23.128  -18.832 1.00 26.62 ?  365  ARG   A C     1 
ATOM   1540 O  O     . ARG   A 1 255 ? 20.288  23.580  -19.026 1.00 25.90 ?  365  ARG   A O     1 
ATOM   1541 C  CB    . ARG   A 1 255 ? 18.836  21.046  -17.441 1.00 23.98 ?  365  ARG   A CB    1 
ATOM   1542 C  CG    . ARG   A 1 255 ? 20.149  20.383  -17.880 1.00 30.36 ?  365  ARG   A CG    1 
ATOM   1543 C  CD    . ARG   A 1 255 ? 19.999  18.855  -17.816 1.00 36.93 ?  365  ARG   A CD    1 
ATOM   1544 N  NE    . ARG   A 1 255 ? 21.259  18.152  -18.050 1.00 52.29 ?  365  ARG   A NE    1 
ATOM   1545 C  CZ    . ARG   A 1 255 ? 22.103  17.784  -17.090 1.00 50.75 ?  365  ARG   A CZ    1 
ATOM   1546 N  NH1   . ARG   A 1 255 ? 21.831  18.057  -15.820 1.00 44.62 ?  365  ARG   A NH1   1 
ATOM   1547 N  NH2   . ARG   A 1 255 ? 23.225  17.142  -17.396 1.00 58.57 ?  365  ARG   A NH2   1 
ATOM   1548 N  N     . PRO   A 1 256 ? 18.231  23.142  -19.808 1.00 24.96 ?  366  PRO   A N     1 
ATOM   1549 C  CA    . PRO   A 1 256 ? 18.586  23.696  -21.125 1.00 25.07 ?  366  PRO   A CA    1 
ATOM   1550 C  C     . PRO   A 1 256 ? 18.969  25.164  -21.087 1.00 26.69 ?  366  PRO   A C     1 
ATOM   1551 O  O     . PRO   A 1 256 ? 19.650  25.626  -22.012 1.00 27.67 ?  366  PRO   A O     1 
ATOM   1552 C  CB    . PRO   A 1 256 ? 17.316  23.472  -21.960 1.00 29.43 ?  366  PRO   A CB    1 
ATOM   1553 C  CG    . PRO   A 1 256 ? 16.609  22.338  -21.274 1.00 30.28 ?  366  PRO   A CG    1 
ATOM   1554 C  CD    . PRO   A 1 256 ? 16.886  22.536  -19.812 1.00 23.96 ?  366  PRO   A CD    1 
ATOM   1555 N  N     . ALA   A 1 257 ? 18.553  25.913  -20.064 1.00 23.51 ?  367  ALA   A N     1 
ATOM   1556 C  CA    . ALA   A 1 257 ? 18.908  27.316  -19.906 1.00 26.17 ?  367  ALA   A CA    1 
ATOM   1557 C  C     . ALA   A 1 257 ? 20.113  27.542  -18.992 1.00 24.44 ?  367  ALA   A C     1 
ATOM   1558 O  O     . ALA   A 1 257 ? 20.504  28.697  -18.784 1.00 26.11 ?  367  ALA   A O     1 
ATOM   1559 C  CB    . ALA   A 1 257 ? 17.701  28.100  -19.374 1.00 24.37 ?  367  ALA   A CB    1 
ATOM   1560 N  N     . GLY   A 1 258 ? 20.703  26.482  -18.436 1.00 25.87 ?  368  GLY   A N     1 
ATOM   1561 C  CA    . GLY   A 1 258 ? 21.833  26.640  -17.529 1.00 24.27 ?  368  GLY   A CA    1 
ATOM   1562 C  C     . GLY   A 1 258 ? 21.508  27.246  -16.174 1.00 27.50 ?  368  GLY   A C     1 
ATOM   1563 O  O     . GLY   A 1 258 ? 22.379  27.896  -15.569 1.00 26.18 ?  368  GLY   A O     1 
ATOM   1564 N  N     . VAL   A 1 259 ? 20.295  27.037  -15.668 1.00 21.38 ?  369  VAL   A N     1 
ATOM   1565 C  CA    . VAL   A 1 259 ? 19.847  27.582  -14.387 1.00 19.34 ?  369  VAL   A CA    1 
ATOM   1566 C  C     . VAL   A 1 259 ? 19.775  26.438  -13.375 1.00 19.10 ?  369  VAL   A C     1 
ATOM   1567 O  O     . VAL   A 1 259 ? 19.015  25.478  -13.594 1.00 19.36 ?  369  VAL   A O     1 
ATOM   1568 C  CB    . VAL   A 1 259 ? 18.483  28.281  -14.513 1.00 19.69 ?  369  VAL   A CB    1 
ATOM   1569 C  CG1   . VAL   A 1 259 ? 17.980  28.727  -13.149 1.00 20.99 ?  369  VAL   A CG1   1 
ATOM   1570 C  CG2   . VAL   A 1 259 ? 18.574  29.460  -15.484 1.00 21.78 ?  369  VAL   A CG2   1 
ATOM   1571 N  N     . PRO   A 1 260 ? 20.506  26.507  -12.256 1.00 16.83 ?  370  PRO   A N     1 
ATOM   1572 C  CA    . PRO   A 1 260 ? 20.449  25.423  -11.250 1.00 17.67 ?  370  PRO   A CA    1 
ATOM   1573 C  C     . PRO   A 1 260 ? 19.106  25.346  -10.520 1.00 17.14 ?  370  PRO   A C     1 
ATOM   1574 O  O     . PRO   A 1 260 ? 18.432  26.359  -10.301 1.00 18.66 ?  370  PRO   A O     1 
ATOM   1575 C  CB    . PRO   A 1 260 ? 21.566  25.785  -10.262 1.00 21.81 ?  370  PRO   A CB    1 
ATOM   1576 C  CG    . PRO   A 1 260 ? 22.459  26.793  -10.985 1.00 26.66 ?  370  PRO   A CG    1 
ATOM   1577 C  CD    . PRO   A 1 260 ? 21.556  27.506  -11.967 1.00 19.84 ?  370  PRO   A CD    1 
ATOM   1578 N  N     . VAL   A 1 261 ? 18.755  24.119  -10.094 1.00 16.77 ?  371  VAL   A N     1 
ATOM   1579 C  CA    . VAL   A 1 261 ? 17.518  23.822  -9.359  1.00 16.78 ?  371  VAL   A CA    1 
ATOM   1580 C  C     . VAL   A 1 261 ? 17.847  23.414  -7.914  1.00 16.94 ?  371  VAL   A C     1 
ATOM   1581 O  O     . VAL   A 1 261 ? 18.693  22.532  -7.688  1.00 17.10 ?  371  VAL   A O     1 
ATOM   1582 C  CB    . VAL   A 1 261 ? 16.719  22.716  -10.067 1.00 16.64 ?  371  VAL   A CB    1 
ATOM   1583 C  CG1   . VAL   A 1 261 ? 15.655  22.103  -9.132  1.00 18.88 ?  371  VAL   A CG1   1 
ATOM   1584 C  CG2   . VAL   A 1 261 ? 16.059  23.269  -11.343 1.00 20.28 ?  371  VAL   A CG2   1 
ATOM   1585 N  N     . ILE   A 1 262 ? 17.167  24.043  -6.941  1.00 16.81 ?  372  ILE   A N     1 
ATOM   1586 C  CA    . ILE   A 1 262 ? 17.292  23.729  -5.506  1.00 16.54 ?  372  ILE   A CA    1 
ATOM   1587 C  C     . ILE   A 1 262 ? 16.096  22.861  -5.098  1.00 17.06 ?  372  ILE   A C     1 
ATOM   1588 O  O     . ILE   A 1 262 ? 14.948  23.308  -5.187  1.00 17.99 ?  372  ILE   A O     1 
ATOM   1589 C  CB    . ILE   A 1 262 ? 17.342  25.016  -4.652  1.00 17.78 ?  372  ILE   A CB    1 
ATOM   1590 C  CG1   . ILE   A 1 262 ? 18.477  25.960  -5.100  1.00 15.27 ?  372  ILE   A CG1   1 
ATOM   1591 C  CG2   . ILE   A 1 262 ? 17.478  24.677  -3.161  1.00 19.63 ?  372  ILE   A CG2   1 
ATOM   1592 C  CD1   . ILE   A 1 262 ? 18.301  27.396  -4.560  1.00 20.03 ?  372  ILE   A CD1   1 
ATOM   1593 N  N     . ALA   A 1 263 ? 16.345  21.627  -4.631  1.00 15.42 ?  373  ALA   A N     1 
ATOM   1594 C  CA    . ALA   A 1 263 ? 15.271  20.718  -4.194  1.00 14.87 ?  373  ALA   A CA    1 
ATOM   1595 C  C     . ALA   A 1 263 ? 14.945  20.999  -2.726  1.00 16.22 ?  373  ALA   A C     1 
ATOM   1596 O  O     . ALA   A 1 263 ? 15.769  20.707  -1.851  1.00 19.37 ?  373  ALA   A O     1 
ATOM   1597 C  CB    . ALA   A 1 263 ? 15.714  19.264  -4.370  1.00 16.63 ?  373  ALA   A CB    1 
ATOM   1598 N  N     . ASP   A 1 264 ? 13.739  21.534  -2.451  1.00 14.95 ?  374  ASP   A N     1 
ATOM   1599 C  CA    . ASP   A 1 264 ? 13.369  22.075  -1.131  1.00 14.96 ?  374  ASP   A CA    1 
ATOM   1600 C  C     . ASP   A 1 264 ? 12.168  21.338  -0.520  1.00 15.31 ?  374  ASP   A C     1 
ATOM   1601 O  O     . ASP   A 1 264 ? 11.023  21.538  -0.956  1.00 17.76 ?  374  ASP   A O     1 
ATOM   1602 C  CB    . ASP   A 1 264 ? 13.063  23.573  -1.279  1.00 15.44 ?  374  ASP   A CB    1 
ATOM   1603 C  CG    . ASP   A 1 264 ? 12.641  24.228  0.023   1.00 16.87 ?  374  ASP   A CG    1 
ATOM   1604 O  OD1   . ASP   A 1 264 ? 12.906  23.648  1.100   1.00 16.59 ?  374  ASP   A OD1   1 
ATOM   1605 O  OD2   . ASP   A 1 264 ? 12.035  25.334  -0.052  1.00 16.88 -1 374  ASP   A OD2   1 
ATOM   1606 N  N     . GLY   A 1 265 ? 12.416  20.500  0.494   1.00 16.54 ?  375  GLY   A N     1 
ATOM   1607 C  CA    . GLY   A 1 265 ? 11.376  19.876  1.299   1.00 16.83 ?  375  GLY   A CA    1 
ATOM   1608 C  C     . GLY   A 1 265 ? 11.258  18.366  1.075   1.00 19.86 ?  375  GLY   A C     1 
ATOM   1609 O  O     . GLY   A 1 265 ? 11.476  17.850  -0.028  1.00 21.60 ?  375  GLY   A O     1 
ATOM   1610 N  N     . GLY   A 1 266 ? 10.867  17.655  2.136   1.00 18.22 ?  376  GLY   A N     1 
ATOM   1611 C  CA    . GLY   A 1 266 ? 10.594  16.219  2.060   1.00 17.28 ?  376  GLY   A CA    1 
ATOM   1612 C  C     . GLY   A 1 266 ? 11.793  15.301  2.245   1.00 22.33 ?  376  GLY   A C     1 
ATOM   1613 O  O     . GLY   A 1 266 ? 11.623  14.065  2.230   1.00 20.80 ?  376  GLY   A O     1 
ATOM   1614 N  N     . LEU   A 1 267 ? 12.994  15.841  2.432   1.00 20.24 ?  377  LEU   A N     1 
ATOM   1615 C  CA    . LEU   A 1 267 ? 14.179  14.994  2.584   1.00 17.44 ?  377  LEU   A CA    1 
ATOM   1616 C  C     . LEU   A 1 267 ? 14.251  14.487  4.025   1.00 20.44 ?  377  LEU   A C     1 
ATOM   1617 O  O     . LEU   A 1 267 ? 14.296  15.283  4.970   1.00 23.53 ?  377  LEU   A O     1 
ATOM   1618 C  CB    . LEU   A 1 267 ? 15.445  15.760  2.195   1.00 20.36 ?  377  LEU   A CB    1 
ATOM   1619 C  CG    . LEU   A 1 267 ? 15.643  15.889  0.671   1.00 20.96 ?  377  LEU   A CG    1 
ATOM   1620 C  CD1   . LEU   A 1 267 ? 15.043  17.171  0.164   1.00 27.72 ?  377  LEU   A CD1   1 
ATOM   1621 C  CD2   . LEU   A 1 267 ? 17.139  15.809  0.294   1.00 29.51 ?  377  LEU   A CD2   1 
ATOM   1622 N  N     . GLN   A 1 268 ? 14.247  13.155  4.201   1.00 20.96 ?  378  GLN   A N     1 
ATOM   1623 C  CA    . GLN   A 1 268 ? 14.205  12.541  5.524   1.00 24.13 ?  378  GLN   A CA    1 
ATOM   1624 C  C     . GLN   A 1 268 ? 15.473  11.789  5.901   1.00 27.22 ?  378  GLN   A C     1 
ATOM   1625 O  O     . GLN   A 1 268 ? 15.738  11.624  7.096   1.00 29.83 ?  378  GLN   A O     1 
ATOM   1626 C  CB    . GLN   A 1 268 ? 13.020  11.560  5.623   1.00 25.55 ?  378  GLN   A CB    1 
ATOM   1627 C  CG    . GLN   A 1 268 ? 11.646  12.191  5.506   1.00 29.25 ?  378  GLN   A CG    1 
ATOM   1628 C  CD    . GLN   A 1 268 ? 10.512  11.177  5.698   1.00 47.67 ?  378  GLN   A CD    1 
ATOM   1629 O  OE1   . GLN   A 1 268 ? 9.766   11.243  6.677   1.00 54.27 ?  378  GLN   A OE1   1 
ATOM   1630 N  NE2   . GLN   A 1 268 ? 10.382  10.238  4.760   1.00 36.35 ?  378  GLN   A NE2   1 
ATOM   1631 N  N     . TYR   A 1 269 ? 16.256  11.339  4.918   1.00 23.09 ?  379  TYR   A N     1 
ATOM   1632 C  CA    . TYR   A 1 269 ? 17.463  10.546  5.136   1.00 23.11 ?  379  TYR   A CA    1 
ATOM   1633 C  C     . TYR   A 1 269 ? 18.561  11.064  4.215   1.00 20.70 ?  379  TYR   A C     1 
ATOM   1634 O  O     . TYR   A 1 269 ? 18.289  11.753  3.231   1.00 20.98 ?  379  TYR   A O     1 
ATOM   1635 C  CB    . TYR   A 1 269 ? 17.230  9.048   4.846   1.00 25.36 ?  379  TYR   A CB    1 
ATOM   1636 C  CG    . TYR   A 1 269 ? 15.907  8.470   5.316   1.00 28.15 ?  379  TYR   A CG    1 
ATOM   1637 C  CD1   . TYR   A 1 269 ? 15.734  8.055   6.628   1.00 37.40 ?  379  TYR   A CD1   1 
ATOM   1638 C  CD2   . TYR   A 1 269 ? 14.846  8.311   4.431   1.00 34.68 ?  379  TYR   A CD2   1 
ATOM   1639 C  CE1   . TYR   A 1 269 ? 14.531  7.509   7.053   1.00 35.78 ?  379  TYR   A CE1   1 
ATOM   1640 C  CE2   . TYR   A 1 269 ? 13.644  7.768   4.844   1.00 37.21 ?  379  TYR   A CE2   1 
ATOM   1641 C  CZ    . TYR   A 1 269 ? 13.491  7.372   6.156   1.00 44.72 ?  379  TYR   A CZ    1 
ATOM   1642 O  OH    . TYR   A 1 269 ? 12.290  6.832   6.566   1.00 57.57 ?  379  TYR   A OH    1 
ATOM   1643 N  N     . SER   A 1 270 ? 19.818  10.715  4.520   1.00 18.77 ?  380  SER   A N     1 
ATOM   1644 C  CA    . SER   A 1 270 ? 20.906  11.127  3.634   1.00 19.46 ?  380  SER   A CA    1 
ATOM   1645 C  C     . SER   A 1 270 ? 20.714  10.593  2.213   1.00 19.29 ?  380  SER   A C     1 
ATOM   1646 O  O     . SER   A 1 270 ? 21.109  11.252  1.243   1.00 18.72 ?  380  SER   A O     1 
ATOM   1647 C  CB    . SER   A 1 270 ? 22.269  10.674  4.201   1.00 20.64 ?  380  SER   A CB    1 
ATOM   1648 O  OG    . SER   A 1 270 ? 22.333  9.250   4.397   1.00 21.25 ?  380  SER   A OG    1 
ATOM   1649 N  N     . GLY   A 1 271 ? 20.119  9.399   2.066   1.00 19.10 ?  381  GLY   A N     1 
ATOM   1650 C  CA    . GLY   A 1 271 ? 19.890  8.849   0.732   1.00 19.60 ?  381  GLY   A CA    1 
ATOM   1651 C  C     . GLY   A 1 271 ? 18.927  9.671   -0.114  1.00 19.82 ?  381  GLY   A C     1 
ATOM   1652 O  O     . GLY   A 1 271 ? 18.987  9.630   -1.354  1.00 18.96 ?  381  GLY   A O     1 
ATOM   1653 N  N     . ASP   A 1 272 ? 18.016  10.412  0.533   1.00 19.85 ?  382  ASP   A N     1 
ATOM   1654 C  CA    . ASP   A 1 272 ? 17.126  11.303  -0.215  1.00 19.05 ?  382  ASP   A CA    1 
ATOM   1655 C  C     . ASP   A 1 272 ? 17.895  12.434  -0.912  1.00 20.00 ?  382  ASP   A C     1 
ATOM   1656 O  O     . ASP   A 1 272 ? 17.473  12.895  -1.984  1.00 20.06 ?  382  ASP   A O     1 
ATOM   1657 C  CB    . ASP   A 1 272 ? 16.044  11.884  0.712   1.00 20.65 ?  382  ASP   A CB    1 
ATOM   1658 C  CG    . ASP   A 1 272 ? 15.088  10.820  1.273   1.00 21.50 ?  382  ASP   A CG    1 
ATOM   1659 O  OD1   . ASP   A 1 272 ? 15.071  9.659   0.792   1.00 22.82 ?  382  ASP   A OD1   1 
ATOM   1660 O  OD2   . ASP   A 1 272 ? 14.289  11.155  2.184   1.00 23.64 -1 382  ASP   A OD2   1 
ATOM   1661 N  N     . ILE   A 1 273 ? 19.011  12.903  -0.328  1.00 18.79 ?  383  ILE   A N     1 
ATOM   1662 C  CA    . ILE   A 1 273 ? 19.845  13.906  -0.999  1.00 16.46 ?  383  ILE   A CA    1 
ATOM   1663 C  C     . ILE   A 1 273 ? 20.375  13.353  -2.320  1.00 18.70 ?  383  ILE   A C     1 
ATOM   1664 O  O     . ILE   A 1 273 ? 20.315  14.020  -3.363  1.00 17.60 ?  383  ILE   A O     1 
ATOM   1665 C  CB    . ILE   A 1 273 ? 21.000  14.360  -0.080  1.00 20.98 ?  383  ILE   A CB    1 
ATOM   1666 C  CG1   . ILE   A 1 273 ? 20.445  14.970  1.216   1.00 22.66 ?  383  ILE   A CG1   1 
ATOM   1667 C  CG2   . ILE   A 1 273 ? 21.927  15.328  -0.823  1.00 21.41 ?  383  ILE   A CG2   1 
ATOM   1668 C  CD1   . ILE   A 1 273 ? 21.520  15.068  2.345   1.00 27.52 ?  383  ILE   A CD1   1 
ATOM   1669 N  N     . ALA   A 1 274 ? 20.891  12.108  -2.302  1.00 16.73 ?  384  ALA   A N     1 
ATOM   1670 C  CA    . ALA   A 1 274 ? 21.407  11.520  -3.537  1.00 18.15 ?  384  ALA   A CA    1 
ATOM   1671 C  C     . ALA   A 1 274 ? 20.306  11.356  -4.590  1.00 15.89 ?  384  ALA   A C     1 
ATOM   1672 O  O     . ALA   A 1 274 ? 20.541  11.613  -5.781  1.00 17.69 ?  384  ALA   A O     1 
ATOM   1673 C  CB    . ALA   A 1 274 ? 22.098  10.174  -3.247  1.00 18.90 ?  384  ALA   A CB    1 
ATOM   1674 N  N     . LYS   A 1 275 ? 19.096  10.958  -4.176  1.00 17.51 ?  385  LYS   A N     1 
ATOM   1675 C  CA    . LYS   A 1 275 ? 17.992  10.820  -5.133  1.00 16.66 ?  385  LYS   A CA    1 
ATOM   1676 C  C     . LYS   A 1 275 ? 17.615  12.174  -5.754  1.00 15.17 ?  385  LYS   A C     1 
ATOM   1677 O  O     . LYS   A 1 275 ? 17.379  12.261  -6.971  1.00 16.22 ?  385  LYS   A O     1 
ATOM   1678 C  CB    . LYS   A 1 275 ? 16.773  10.167  -4.457  1.00 15.97 ?  385  LYS   A CB    1 
ATOM   1679 C  CG    . LYS   A 1 275 ? 17.000  8.743   -3.876  1.00 15.98 ?  385  LYS   A CG    1 
ATOM   1680 C  CD    . LYS   A 1 275 ? 15.712  8.225   -3.137  1.00 16.17 ?  385  LYS   A CD    1 
ATOM   1681 C  CE    . LYS   A 1 275 ? 15.974  6.883   -2.430  1.00 19.45 ?  385  LYS   A CE    1 
ATOM   1682 N  NZ    . LYS   A 1 275 ? 14.710  6.320   -1.824  1.00 19.90 ?  385  LYS   A NZ    1 
ATOM   1683 N  N     . ALA   A 1 276 ? 17.560  13.245  -4.940  1.00 15.92 ?  386  ALA   A N     1 
ATOM   1684 C  CA    . ALA   A 1 276 ? 17.184  14.566  -5.454  1.00 16.43 ?  386  ALA   A CA    1 
ATOM   1685 C  C     . ALA   A 1 276 ? 18.178  15.074  -6.493  1.00 18.63 ?  386  ALA   A C     1 
ATOM   1686 O  O     . ALA   A 1 276 ? 17.775  15.651  -7.516  1.00 17.64 ?  386  ALA   A O     1 
ATOM   1687 C  CB    . ALA   A 1 276 ? 17.089  15.579  -4.307  1.00 16.22 ?  386  ALA   A CB    1 
ATOM   1688 N  N     . LEU   A 1 277 ? 19.486  14.888  -6.237  1.00 17.48 ?  387  LEU   A N     1 
ATOM   1689 C  CA    . LEU   A 1 277 ? 20.503  15.340  -7.186  1.00 16.25 ?  387  LEU   A CA    1 
ATOM   1690 C  C     . LEU   A 1 277 ? 20.525  14.465  -8.443  1.00 18.07 ?  387  LEU   A C     1 
ATOM   1691 O  O     . LEU   A 1 277 ? 20.681  14.981  -9.562  1.00 18.50 ?  387  LEU   A O     1 
ATOM   1692 C  CB    . LEU   A 1 277 ? 21.886  15.377  -6.500  1.00 16.89 ?  387  LEU   A CB    1 
ATOM   1693 C  CG    . LEU   A 1 277 ? 21.964  16.251  -5.242  1.00 17.02 ?  387  LEU   A CG    1 
ATOM   1694 C  CD1   . LEU   A 1 277 ? 23.381  16.223  -4.611  1.00 18.43 ?  387  LEU   A CD1   1 
ATOM   1695 C  CD2   . LEU   A 1 277 ? 21.603  17.705  -5.587  1.00 20.76 ?  387  LEU   A CD2   1 
ATOM   1696 N  N     . ALA   A 1 278 ? 20.301  13.148  -8.297  1.00 15.72 ?  388  ALA   A N     1 
ATOM   1697 C  CA    . ALA   A 1 278 ? 20.207  12.293  -9.483  1.00 16.69 ?  388  ALA   A CA    1 
ATOM   1698 C  C     . ALA   A 1 278 ? 19.010  12.639  -10.364 1.00 17.61 ?  388  ALA   A C     1 
ATOM   1699 O  O     . ALA   A 1 278 ? 19.080  12.469  -11.588 1.00 19.10 ?  388  ALA   A O     1 
ATOM   1700 C  CB    . ALA   A 1 278 ? 20.134  10.808  -9.090  1.00 18.17 ?  388  ALA   A CB    1 
ATOM   1701 N  N     . ALA   A 1 279 ? 17.901  13.119  -9.777  1.00 16.82 ?  389  ALA   A N     1 
ATOM   1702 C  CA    . ALA   A 1 279 ? 16.780  13.592  -10.581 1.00 17.10 ?  389  ALA   A CA    1 
ATOM   1703 C  C     . ALA   A 1 279 ? 17.096  14.881  -11.329 1.00 19.71 ?  389  ALA   A C     1 
ATOM   1704 O  O     . ALA   A 1 279 ? 16.307  15.279  -12.195 1.00 19.86 ?  389  ALA   A O     1 
ATOM   1705 C  CB    . ALA   A 1 279 ? 15.532  13.794  -9.707  1.00 17.05 ?  389  ALA   A CB    1 
ATOM   1706 N  N     . GLY   A 1 280 ? 18.224  15.529  -11.034 1.00 17.18 ?  390  GLY   A N     1 
ATOM   1707 C  CA    . GLY   A 1 280 ? 18.654  16.695  -11.781 1.00 18.00 ?  390  GLY   A CA    1 
ATOM   1708 C  C     . GLY   A 1 280 ? 18.846  17.956  -10.964 1.00 17.32 ?  390  GLY   A C     1 
ATOM   1709 O  O     . GLY   A 1 280 ? 19.364  18.940  -11.521 1.00 17.30 ?  390  GLY   A O     1 
ATOM   1710 N  N     . ALA   A 1 281 ? 18.460  17.997  -9.683  1.00 16.77 ?  391  ALA   A N     1 
ATOM   1711 C  CA    . ALA   A 1 281 ? 18.744  19.164  -8.843  1.00 17.70 ?  391  ALA   A CA    1 
ATOM   1712 C  C     . ALA   A 1 281 ? 20.257  19.332  -8.635  1.00 15.59 ?  391  ALA   A C     1 
ATOM   1713 O  O     . ALA   A 1 281 ? 21.029  18.382  -8.773  1.00 17.01 ?  391  ALA   A O     1 
ATOM   1714 C  CB    . ALA   A 1 281 ? 18.025  19.037  -7.489  1.00 18.27 ?  391  ALA   A CB    1 
ATOM   1715 N  N     . SER   A 1 282 ? 20.679  20.579  -8.332  1.00 16.63 ?  392  SER   A N     1 
ATOM   1716 C  CA    . SER   A 1 282 ? 22.093  20.890  -8.055  1.00 15.40 ?  392  SER   A CA    1 
ATOM   1717 C  C     . SER   A 1 282 ? 22.406  21.075  -6.567  1.00 15.14 ?  392  SER   A C     1 
ATOM   1718 O  O     . SER   A 1 282 ? 23.559  20.856  -6.156  1.00 17.43 ?  392  SER   A O     1 
ATOM   1719 C  CB    . SER   A 1 282 ? 22.510  22.163  -8.829  1.00 18.89 ?  392  SER   A CB    1 
ATOM   1720 O  OG    . SER   A 1 282 ? 22.500  21.926  -10.250 1.00 19.37 ?  392  SER   A OG    1 
ATOM   1721 N  N     . THR   A 1 283 ? 21.421  21.462  -5.742  1.00 16.85 ?  393  THR   A N     1 
ATOM   1722 C  CA    . THR   A 1 283 ? 21.559  21.499  -4.286  1.00 15.01 ?  393  THR   A CA    1 
ATOM   1723 C  C     . THR   A 1 283 ? 20.243  21.052  -3.648  1.00 15.68 ?  393  THR   A C     1 
ATOM   1724 O  O     . THR   A 1 283 ? 19.211  20.939  -4.320  1.00 16.99 ?  393  THR   A O     1 
ATOM   1725 C  CB    . THR   A 1 283 ? 21.942  22.902  -3.760  1.00 16.61 ?  393  THR   A CB    1 
ATOM   1726 O  OG1   . THR   A 1 283 ? 20.962  23.867  -4.178  1.00 17.17 ?  393  THR   A OG1   1 
ATOM   1727 C  CG2   . THR   A 1 283 ? 23.351  23.337  -4.256  1.00 18.34 ?  393  THR   A CG2   1 
ATOM   1728 N  N     . ALA   A 1 284 ? 20.285  20.779  -2.329  1.00 16.39 ?  394  ALA   A N     1 
ATOM   1729 C  CA    . ALA   A 1 284 ? 19.085  20.467  -1.543  1.00 16.13 ?  394  ALA   A CA    1 
ATOM   1730 C  C     . ALA   A 1 284 ? 18.960  21.395  -0.337  1.00 17.65 ?  394  ALA   A C     1 
ATOM   1731 O  O     . ALA   A 1 284 ? 19.967  21.747  0.280   1.00 19.37 ?  394  ALA   A O     1 
ATOM   1732 C  CB    . ALA   A 1 284 ? 19.083  19.011  -1.056  1.00 18.00 ?  394  ALA   A CB    1 
ATOM   1733 N  N     . MET   A 1 285 ? 17.724  21.802  -0.005  1.00 17.28 ?  395  MET   A N     1 
ATOM   1734 C  CA    . MET   A 1 285 ? 17.439  22.633  1.175   1.00 16.90 ?  395  MET   A CA    1 
ATOM   1735 C  C     . MET   A 1 285 ? 16.756  21.788  2.252   1.00 17.91 ?  395  MET   A C     1 
ATOM   1736 O  O     . MET   A 1 285 ? 15.801  21.043  1.957   1.00 17.53 ?  395  MET   A O     1 
ATOM   1737 C  CB    . MET   A 1 285 ? 16.567  23.853  0.804   1.00 17.95 ?  395  MET   A CB    1 
ATOM   1738 C  CG    . MET   A 1 285 ? 16.103  24.706  2.007   1.00 17.89 ?  395  MET   A CG    1 
ATOM   1739 S  SD    . MET   A 1 285 ? 15.205  26.247  1.576   1.00 17.36 ?  395  MET   A SD    1 
ATOM   1740 C  CE    . MET   A 1 285 ? 16.566  27.422  1.390   1.00 16.64 ?  395  MET   A CE    1 
ATOM   1741 N  N     . LEU   A 1 286 ? 17.230  21.917  3.505   1.00 16.93 ?  396  LEU   A N     1 
ATOM   1742 C  CA    . LEU   A 1 286 ? 16.841  21.033  4.610   1.00 16.58 ?  396  LEU   A CA    1 
ATOM   1743 C  C     . LEU   A 1 286 ? 16.261  21.829  5.777   1.00 20.07 ?  396  LEU   A C     1 
ATOM   1744 O  O     . LEU   A 1 286 ? 16.904  22.764  6.281   1.00 19.18 ?  396  LEU   A O     1 
ATOM   1745 C  CB    . LEU   A 1 286 ? 18.046  20.206  5.116   1.00 18.18 ?  396  LEU   A CB    1 
ATOM   1746 C  CG    . LEU   A 1 286 ? 18.921  19.471  4.092   1.00 19.69 ?  396  LEU   A CG    1 
ATOM   1747 C  CD1   . LEU   A 1 286 ? 20.152  18.841  4.757   1.00 25.10 ?  396  LEU   A CD1   1 
ATOM   1748 C  CD2   . LEU   A 1 286 ? 18.086  18.409  3.390   1.00 21.78 ?  396  LEU   A CD2   1 
ATOM   1749 N  N     . GLY   A 1 287 ? 15.070  21.428  6.229   1.00 19.43 ?  397  GLY   A N     1 
ATOM   1750 C  CA    . GLY   A 1 287 ? 14.488  21.947  7.456   1.00 19.31 ?  397  GLY   A CA    1 
ATOM   1751 C  C     . GLY   A 1 287 ? 14.542  20.962  8.614   1.00 22.07 ?  397  GLY   A C     1 
ATOM   1752 O  O     . GLY   A 1 287 ? 15.339  21.145  9.534   1.00 22.64 ?  397  GLY   A O     1 
ATOM   1753 N  N     A SER   A 1 288 ? 13.702  19.921  8.575   0.50 19.60 ?  398  SER   A N     1 
ATOM   1754 N  N     B SER   A 1 288 ? 13.732  19.895  8.563   0.50 19.62 ?  398  SER   A N     1 
ATOM   1755 C  CA    A SER   A 1 288 ? 13.622  18.973  9.688   0.50 21.39 ?  398  SER   A CA    1 
ATOM   1756 C  CA    B SER   A 1 288 ? 13.618  18.982  9.704   0.50 21.39 ?  398  SER   A CA    1 
ATOM   1757 C  C     A SER   A 1 288 ? 14.989  18.399  10.062  0.50 24.11 ?  398  SER   A C     1 
ATOM   1758 C  C     B SER   A 1 288 ? 14.940  18.294  10.054  0.50 24.12 ?  398  SER   A C     1 
ATOM   1759 O  O     A SER   A 1 288 ? 15.318  18.289  11.249  0.50 24.45 ?  398  SER   A O     1 
ATOM   1760 O  O     B SER   A 1 288 ? 15.179  17.981  11.227  0.50 24.03 ?  398  SER   A O     1 
ATOM   1761 C  CB    A SER   A 1 288 ? 12.649  17.844  9.342   0.50 25.86 ?  398  SER   A CB    1 
ATOM   1762 C  CB    B SER   A 1 288 ? 12.541  17.932  9.430   0.50 25.82 ?  398  SER   A CB    1 
ATOM   1763 O  OG    A SER   A 1 288 ? 12.531  16.916  10.409  0.50 28.32 ?  398  SER   A OG    1 
ATOM   1764 O  OG    B SER   A 1 288 ? 13.029  16.901  8.587   0.50 22.77 ?  398  SER   A OG    1 
ATOM   1765 N  N     . LEU   A 1 289 ? 15.797  18.025  9.066   1.00 21.21 ?  399  LEU   A N     1 
ATOM   1766 C  CA    . LEU   A 1 289 ? 17.059  17.336  9.354   1.00 22.80 ?  399  LEU   A CA    1 
ATOM   1767 C  C     . LEU   A 1 289 ? 18.055  18.214  10.104  1.00 24.61 ?  399  LEU   A C     1 
ATOM   1768 O  O     . LEU   A 1 289 ? 18.988  17.679  10.715  1.00 27.95 ?  399  LEU   A O     1 
ATOM   1769 C  CB    . LEU   A 1 289 ? 17.705  16.817  8.061   1.00 19.72 ?  399  LEU   A CB    1 
ATOM   1770 C  CG    . LEU   A 1 289 ? 17.159  15.509  7.455   1.00 24.24 ?  399  LEU   A CG    1 
ATOM   1771 C  CD1   . LEU   A 1 289 ? 17.727  15.267  6.057   1.00 26.67 ?  399  LEU   A CD1   1 
ATOM   1772 C  CD2   . LEU   A 1 289 ? 17.483  14.316  8.346   1.00 36.48 ?  399  LEU   A CD2   1 
ATOM   1773 N  N     . LEU   A 1 290 ? 17.894  19.541  10.064  1.00 20.87 ?  400  LEU   A N     1 
ATOM   1774 C  CA    . LEU   A 1 290 ? 18.794  20.464  10.749  1.00 21.92 ?  400  LEU   A CA    1 
ATOM   1775 C  C     . LEU   A 1 290 ? 18.157  21.158  11.947  1.00 25.76 ?  400  LEU   A C     1 
ATOM   1776 O  O     . LEU   A 1 290 ? 18.884  21.748  12.757  1.00 27.63 ?  400  LEU   A O     1 
ATOM   1777 C  CB    . LEU   A 1 290 ? 19.318  21.535  9.770   1.00 20.29 ?  400  LEU   A CB    1 
ATOM   1778 C  CG    . LEU   A 1 290 ? 20.014  21.056  8.486   1.00 20.49 ?  400  LEU   A CG    1 
ATOM   1779 C  CD1   . LEU   A 1 290 ? 20.491  22.213  7.634   1.00 22.73 ?  400  LEU   A CD1   1 
ATOM   1780 C  CD2   . LEU   A 1 290 ? 21.184  20.115  8.795   1.00 20.97 ?  400  LEU   A CD2   1 
ATOM   1781 N  N     . ALA   A 1 291 ? 16.827  21.106  12.087  1.00 23.87 ?  401  ALA   A N     1 
ATOM   1782 C  CA    . ALA   A 1 291 ? 16.158  21.751  13.212  1.00 23.10 ?  401  ALA   A CA    1 
ATOM   1783 C  C     . ALA   A 1 291 ? 16.526  21.139  14.561  1.00 26.42 ?  401  ALA   A C     1 
ATOM   1784 O  O     . ALA   A 1 291 ? 16.332  21.790  15.595  1.00 33.42 ?  401  ALA   A O     1 
ATOM   1785 C  CB    . ALA   A 1 291 ? 14.638  21.685  13.022  1.00 24.37 ?  401  ALA   A CB    1 
ATOM   1786 N  N     . GLY   A 1 292 ? 17.031  19.915  14.586  1.00 28.65 ?  402  GLY   A N     1 
ATOM   1787 C  CA    . GLY   A 1 292 ? 17.415  19.335  15.859  1.00 34.61 ?  402  GLY   A CA    1 
ATOM   1788 C  C     . GLY   A 1 292 ? 18.792  19.696  16.381  1.00 36.21 ?  402  GLY   A C     1 
ATOM   1789 O  O     . GLY   A 1 292 ? 19.163  19.224  17.460  1.00 35.13 ?  402  GLY   A O     1 
ATOM   1790 N  N     . THR   A 1 293 ? 19.558  20.524  15.677  1.00 24.48 ?  403  THR   A N     1 
ATOM   1791 C  CA    . THR   A 1 293 ? 20.964  20.715  16.009  1.00 24.67 ?  403  THR   A CA    1 
ATOM   1792 C  C     . THR   A 1 293 ? 21.157  21.838  17.024  1.00 27.56 ?  403  THR   A C     1 
ATOM   1793 O  O     . THR   A 1 293 ? 20.284  22.681  17.238  1.00 26.81 ?  403  THR   A O     1 
ATOM   1794 C  CB    . THR   A 1 293 ? 21.793  21.022  14.761  1.00 25.97 ?  403  THR   A CB    1 
ATOM   1795 O  OG1   . THR   A 1 293 ? 21.293  22.217  14.137  1.00 28.73 ?  403  THR   A OG1   1 
ATOM   1796 C  CG2   . THR   A 1 293 ? 21.758  19.841  13.770  1.00 25.53 ?  403  THR   A CG2   1 
ATOM   1797 N  N     . ALA   A 1 294 ? 22.347  21.851  17.630  1.00 25.46 ?  404  ALA   A N     1 
ATOM   1798 C  CA    . ALA   A 1 294 ? 22.653  22.841  18.657  1.00 29.67 ?  404  ALA   A CA    1 
ATOM   1799 C  C     . ALA   A 1 294 ? 22.519  24.260  18.122  1.00 27.16 ?  404  ALA   A C     1 
ATOM   1800 O  O     . ALA   A 1 294 ? 22.101  25.169  18.851  1.00 28.07 ?  404  ALA   A O     1 
ATOM   1801 C  CB    . ALA   A 1 294 ? 24.069  22.615  19.193  1.00 24.63 ?  404  ALA   A CB    1 
ATOM   1802 N  N     . GLU   A 1 295 ? 22.875  24.468  16.852  1.00 25.36 ?  405  GLU   A N     1 
ATOM   1803 C  CA    . GLU   A 1 295 ? 22.930  25.804  16.273  1.00 25.48 ?  405  GLU   A CA    1 
ATOM   1804 C  C     . GLU   A 1 295 ? 21.559  26.348  15.871  1.00 24.37 ?  405  GLU   A C     1 
ATOM   1805 O  O     . GLU   A 1 295 ? 21.433  27.557  15.638  1.00 27.44 ?  405  GLU   A O     1 
ATOM   1806 C  CB    . GLU   A 1 295 ? 23.874  25.795  15.064  1.00 28.55 ?  405  GLU   A CB    1 
ATOM   1807 C  CG    . GLU   A 1 295 ? 25.378  25.746  15.425  1.00 29.71 ?  405  GLU   A CG    1 
ATOM   1808 C  CD    . GLU   A 1 295 ? 25.933  24.338  15.614  1.00 28.86 ?  405  GLU   A CD    1 
ATOM   1809 O  OE1   . GLU   A 1 295 ? 25.151  23.362  15.706  1.00 25.98 ?  405  GLU   A OE1   1 
ATOM   1810 O  OE2   . GLU   A 1 295 ? 27.180  24.207  15.672  1.00 31.49 -1 405  GLU   A OE2   1 
ATOM   1811 N  N     . ALA   A 1 296 ? 20.539  25.501  15.785  1.00 24.57 ?  406  ALA   A N     1 
ATOM   1812 C  CA    . ALA   A 1 296 ? 19.205  25.975  15.428  1.00 23.08 ?  406  ALA   A CA    1 
ATOM   1813 C  C     . ALA   A 1 296 ? 18.642  26.873  16.535  1.00 27.22 ?  406  ALA   A C     1 
ATOM   1814 O  O     . ALA   A 1 296 ? 18.916  26.657  17.716  1.00 30.94 ?  406  ALA   A O     1 
ATOM   1815 C  CB    . ALA   A 1 296 ? 18.275  24.790  15.187  1.00 26.82 ?  406  ALA   A CB    1 
ATOM   1816 N  N     . PRO   A 1 297 ? 17.858  27.897  16.179  1.00 26.08 ?  407  PRO   A N     1 
ATOM   1817 C  CA    . PRO   A 1 297 ? 17.292  28.781  17.208  1.00 30.64 ?  407  PRO   A CA    1 
ATOM   1818 C  C     . PRO   A 1 297 ? 16.335  28.040  18.129  1.00 40.39 ?  407  PRO   A C     1 
ATOM   1819 O  O     . PRO   A 1 297 ? 15.598  27.148  17.705  1.00 38.75 ?  407  PRO   A O     1 
ATOM   1820 C  CB    . PRO   A 1 297 ? 16.550  29.857  16.401  1.00 36.40 ?  407  PRO   A CB    1 
ATOM   1821 C  CG    . PRO   A 1 297 ? 17.028  29.729  14.994  1.00 31.34 ?  407  PRO   A CG    1 
ATOM   1822 C  CD    . PRO   A 1 297 ? 17.517  28.323  14.814  1.00 25.36 ?  407  PRO   A CD    1 
ATOM   1823 N  N     . GLY   A 1 298 ? 16.333  28.437  19.401  1.00 44.90 ?  408  GLY   A N     1 
ATOM   1824 C  CA    . GLY   A 1 298 ? 15.490  27.782  20.383  1.00 48.11 ?  408  GLY   A CA    1 
ATOM   1825 C  C     . GLY   A 1 298 ? 16.267  27.055  21.464  1.00 50.96 ?  408  GLY   A C     1 
ATOM   1826 O  O     . GLY   A 1 298 ? 17.469  26.810  21.316  1.00 43.63 ?  408  GLY   A O     1 
ATOM   1827 N  N     . GLU   A 1 299 ? 15.592  26.708  22.557  1.00 51.61 ?  409  GLU   A N     1 
ATOM   1828 C  CA    . GLU   A 1 299 ? 16.213  26.034  23.688  1.00 51.06 ?  409  GLU   A CA    1 
ATOM   1829 C  C     . GLU   A 1 299 ? 15.927  24.538  23.646  1.00 50.18 ?  409  GLU   A C     1 
ATOM   1830 O  O     . GLU   A 1 299 ? 14.962  24.082  23.028  1.00 47.13 ?  409  GLU   A O     1 
ATOM   1831 C  CB    . GLU   A 1 299 ? 15.704  26.602  25.014  1.00 56.17 ?  409  GLU   A CB    1 
ATOM   1832 C  CG    . GLU   A 1 299 ? 15.554  28.107  25.056  1.00 54.81 ?  409  GLU   A CG    1 
ATOM   1833 C  CD    . GLU   A 1 299 ? 14.522  28.535  26.080  1.00 60.81 ?  409  GLU   A CD    1 
ATOM   1834 O  OE1   . GLU   A 1 299 ? 13.901  27.642  26.700  1.00 61.92 ?  409  GLU   A OE1   1 
ATOM   1835 O  OE2   . GLU   A 1 299 ? 14.325  29.755  26.262  1.00 58.05 -1 409  GLU   A OE2   1 
ATOM   1836 N  N     . LEU   A 1 300 ? 16.772  23.780  24.337  1.00 47.31 ?  410  LEU   A N     1 
ATOM   1837 C  CA    . LEU   A 1 300 ? 16.583  22.340  24.426  1.00 46.77 ?  410  LEU   A CA    1 
ATOM   1838 C  C     . LEU   A 1 300 ? 15.353  22.019  25.273  1.00 50.65 ?  410  LEU   A C     1 
ATOM   1839 O  O     . LEU   A 1 300 ? 14.985  22.768  26.181  1.00 54.89 ?  410  LEU   A O     1 
ATOM   1840 C  CB    . LEU   A 1 300 ? 17.836  21.686  25.013  1.00 48.83 ?  410  LEU   A CB    1 
ATOM   1841 C  CG    . LEU   A 1 300 ? 18.019  20.186  24.788  1.00 49.79 ?  410  LEU   A CG    1 
ATOM   1842 C  CD1   . LEU   A 1 300 ? 17.818  19.839  23.322  1.00 47.33 ?  410  LEU   A CD1   1 
ATOM   1843 C  CD2   . LEU   A 1 300 ? 19.396  19.747  25.253  1.00 48.41 ?  410  LEU   A CD2   1 
ATOM   1844 N  N     . ILE   A 1 301 ? 14.703  20.898  24.955  1.00 52.18 ?  411  ILE   A N     1 
ATOM   1845 C  CA    . ILE   A 1 301 ? 13.505  20.436  25.658  1.00 51.68 ?  411  ILE   A CA    1 
ATOM   1846 C  C     . ILE   A 1 301 ? 13.789  19.048  26.214  1.00 51.47 ?  411  ILE   A C     1 
ATOM   1847 O  O     . ILE   A 1 301 ? 13.821  18.066  25.461  1.00 54.10 ?  411  ILE   A O     1 
ATOM   1848 C  CB    . ILE   A 1 301 ? 12.271  20.412  24.745  1.00 49.02 ?  411  ILE   A CB    1 
ATOM   1849 C  CG1   . ILE   A 1 301 ? 11.817  21.833  24.402  1.00 48.82 ?  411  ILE   A CG1   1 
ATOM   1850 C  CG2   . ILE   A 1 301 ? 11.143  19.628  25.396  1.00 54.79 ?  411  ILE   A CG2   1 
ATOM   1851 C  CD1   . ILE   A 1 301 ? 10.701  21.880  23.373  1.00 48.55 ?  411  ILE   A CD1   1 
ATOM   1852 N  N     . PHE   A 1 302 ? 13.998  18.964  27.530  1.00 62.76 ?  412  PHE   A N     1 
ATOM   1853 C  CA    . PHE   A 1 302 ? 14.159  17.690  28.230  1.00 58.88 ?  412  PHE   A CA    1 
ATOM   1854 C  C     . PHE   A 1 302 ? 12.779  17.221  28.677  1.00 62.45 ?  412  PHE   A C     1 
ATOM   1855 O  O     . PHE   A 1 302 ? 12.166  17.836  29.557  1.00 67.94 ?  412  PHE   A O     1 
ATOM   1856 C  CB    . PHE   A 1 302 ? 15.081  17.834  29.442  1.00 55.52 ?  412  PHE   A CB    1 
ATOM   1857 C  CG    . PHE   A 1 302 ? 16.537  18.074  29.107  1.00 52.81 ?  412  PHE   A CG    1 
ATOM   1858 C  CD1   . PHE   A 1 302 ? 17.492  17.094  29.364  1.00 36.25 ?  412  PHE   A CD1   1 
ATOM   1859 C  CD2   . PHE   A 1 302 ? 16.957  19.286  28.579  1.00 46.60 ?  412  PHE   A CD2   1 
ATOM   1860 C  CE1   . PHE   A 1 302 ? 18.821  17.311  29.089  1.00 46.39 ?  412  PHE   A CE1   1 
ATOM   1861 C  CE2   . PHE   A 1 302 ? 18.296  19.509  28.292  1.00 44.82 ?  412  PHE   A CE2   1 
ATOM   1862 C  CZ    . PHE   A 1 302 ? 19.231  18.520  28.546  1.00 45.84 ?  412  PHE   A CZ    1 
ATOM   1863 N  N     . VAL   A 1 303 ? 12.284  16.139  28.084  1.00 66.27 ?  413  VAL   A N     1 
ATOM   1864 C  CA    . VAL   A 1 303 ? 10.990  15.582  28.465  1.00 70.86 ?  413  VAL   A CA    1 
ATOM   1865 C  C     . VAL   A 1 303 ? 11.089  14.063  28.424  1.00 75.57 ?  413  VAL   A C     1 
ATOM   1866 O  O     . VAL   A 1 303 ? 11.588  13.492  27.448  1.00 75.26 ?  413  VAL   A O     1 
ATOM   1867 C  CB    . VAL   A 1 303 ? 9.846   16.093  27.563  1.00 66.86 ?  413  VAL   A CB    1 
ATOM   1868 C  CG1   . VAL   A 1 303 ? 9.880   15.419  26.203  1.00 67.86 ?  413  VAL   A CG1   1 
ATOM   1869 C  CG2   . VAL   A 1 303 ? 8.499   15.892  28.240  1.00 67.37 ?  413  VAL   A CG2   1 
ATOM   1870 N  N     . ASN   A 1 304 ? 10.630  13.413  29.493  1.00 77.12 ?  414  ASN   A N     1 
ATOM   1871 C  CA    . ASN   A 1 304 ? 10.705  11.959  29.630  1.00 77.03 ?  414  ASN   A CA    1 
ATOM   1872 C  C     . ASN   A 1 304 ? 12.117  11.449  29.344  1.00 77.12 ?  414  ASN   A C     1 
ATOM   1873 O  O     . ASN   A 1 304 ? 12.323  10.493  28.593  1.00 79.99 ?  414  ASN   A O     1 
ATOM   1874 C  CB    . ASN   A 1 304 ? 9.677   11.273  28.732  1.00 81.08 ?  414  ASN   A CB    1 
ATOM   1875 C  CG    . ASN   A 1 304 ? 8.434   10.861  29.490  1.00 88.77 ?  414  ASN   A CG    1 
ATOM   1876 O  OD1   . ASN   A 1 304 ? 8.511   10.437  30.643  1.00 93.07 ?  414  ASN   A OD1   1 
ATOM   1877 N  ND2   . ASN   A 1 304 ? 7.278   10.987  28.849  1.00 96.11 ?  414  ASN   A ND2   1 
ATOM   1878 N  N     . GLY   A 1 305 ? 13.102  12.105  29.961  1.00 71.28 ?  415  GLY   A N     1 
ATOM   1879 C  CA    . GLY   A 1 305 ? 14.491  11.718  29.826  1.00 58.21 ?  415  GLY   A CA    1 
ATOM   1880 C  C     . GLY   A 1 305 ? 15.090  11.904  28.453  1.00 68.10 ?  415  GLY   A C     1 
ATOM   1881 O  O     . GLY   A 1 305 ? 16.318  11.814  28.318  1.00 64.94 ?  415  GLY   A O     1 
ATOM   1882 N  N     . LYS   A 1 306 ? 14.280  12.145  27.429  1.00 74.48 ?  416  LYS   A N     1 
ATOM   1883 C  CA    . LYS   A 1 306 ? 14.774  12.431  26.093  1.00 71.45 ?  416  LYS   A CA    1 
ATOM   1884 C  C     . LYS   A 1 306 ? 14.671  13.929  25.816  1.00 63.03 ?  416  LYS   A C     1 
ATOM   1885 O  O     . LYS   A 1 306 ? 13.984  14.674  26.520  1.00 61.64 ?  416  LYS   A O     1 
ATOM   1886 C  CB    . LYS   A 1 306 ? 14.005  11.613  25.047  1.00 68.86 ?  416  LYS   A CB    1 
ATOM   1887 C  CG    . LYS   A 1 306 ? 14.317  10.122  25.091  1.00 73.42 ?  416  LYS   A CG    1 
ATOM   1888 C  CD    . LYS   A 1 306 ? 13.724  9.384   23.899  1.00 79.43 ?  416  LYS   A CD    1 
ATOM   1889 C  CE    . LYS   A 1 306 ? 14.049  7.896   23.941  1.00 84.53 ?  416  LYS   A CE    1 
ATOM   1890 N  NZ    . LYS   A 1 306 ? 13.484  7.172   22.766  1.00 82.14 ?  416  LYS   A NZ    1 
ATOM   1891 N  N     . GLN   A 1 307 ? 15.374  14.367  24.773  1.00 55.23 ?  417  GLN   A N     1 
ATOM   1892 C  CA    . GLN   A 1 307 ? 15.545  15.781  24.472  1.00 49.91 ?  417  GLN   A CA    1 
ATOM   1893 C  C     . GLN   A 1 307 ? 14.990  16.104  23.090  1.00 41.84 ?  417  GLN   A C     1 
ATOM   1894 O  O     . GLN   A 1 307 ? 15.081  15.290  22.164  1.00 45.25 ?  417  GLN   A O     1 
ATOM   1895 C  CB    . GLN   A 1 307 ? 17.025  16.162  24.544  1.00 43.16 ?  417  GLN   A CB    1 
ATOM   1896 C  CG    . GLN   A 1 307 ? 17.684  15.750  25.852  1.00 43.74 ?  417  GLN   A CG    1 
ATOM   1897 C  CD    . GLN   A 1 307 ? 19.190  15.626  25.738  1.00 41.83 ?  417  GLN   A CD    1 
ATOM   1898 O  OE1   . GLN   A 1 307 ? 19.706  14.931  24.865  1.00 37.73 ?  417  GLN   A OE1   1 
ATOM   1899 N  NE2   . GLN   A 1 307 ? 19.906  16.298  26.629  1.00 42.76 ?  417  GLN   A NE2   1 
ATOM   1900 N  N     . TYR   A 1 308 ? 14.425  17.308  22.959  1.00 45.55 ?  418  TYR   A N     1 
ATOM   1901 C  CA    . TYR   A 1 308 ? 13.808  17.766  21.718  1.00 40.11 ?  418  TYR   A CA    1 
ATOM   1902 C  C     . TYR   A 1 308 ? 14.069  19.257  21.525  1.00 43.64 ?  418  TYR   A C     1 
ATOM   1903 O  O     . TYR   A 1 308 ? 14.547  19.953  22.425  1.00 39.88 ?  418  TYR   A O     1 
ATOM   1904 C  CB    . TYR   A 1 308 ? 12.293  17.513  21.708  1.00 39.55 ?  418  TYR   A CB    1 
ATOM   1905 C  CG    . TYR   A 1 308 ? 11.885  16.082  21.984  1.00 46.74 ?  418  TYR   A CG    1 
ATOM   1906 C  CD1   . TYR   A 1 308 ? 11.824  15.146  20.961  1.00 46.35 ?  418  TYR   A CD1   1 
ATOM   1907 C  CD2   . TYR   A 1 308 ? 11.547  15.673  23.266  1.00 52.54 ?  418  TYR   A CD2   1 
ATOM   1908 C  CE1   . TYR   A 1 308 ? 11.445  13.839  21.211  1.00 50.35 ?  418  TYR   A CE1   1 
ATOM   1909 C  CE2   . TYR   A 1 308 ? 11.169  14.371  23.525  1.00 58.75 ?  418  TYR   A CE2   1 
ATOM   1910 C  CZ    . TYR   A 1 308 ? 11.119  13.458  22.497  1.00 59.33 ?  418  TYR   A CZ    1 
ATOM   1911 O  OH    . TYR   A 1 308 ? 10.742  12.160  22.762  1.00 64.91 ?  418  TYR   A OH    1 
ATOM   1912 N  N     . LYS   A 1 309 ? 13.739  19.750  20.329  1.00 36.19 ?  419  LYS   A N     1 
ATOM   1913 C  CA    . LYS   A 1 309 ? 13.700  21.181  20.055  1.00 31.34 ?  419  LYS   A CA    1 
ATOM   1914 C  C     . LYS   A 1 309 ? 12.476  21.485  19.198  1.00 27.00 ?  419  LYS   A C     1 
ATOM   1915 O  O     . LYS   A 1 309 ? 11.997  20.626  18.455  1.00 33.47 ?  419  LYS   A O     1 
ATOM   1916 C  CB    . LYS   A 1 309 ? 14.980  21.679  19.353  1.00 39.31 ?  419  LYS   A CB    1 
ATOM   1917 C  CG    . LYS   A 1 309 ? 16.215  21.749  20.262  1.00 36.91 ?  419  LYS   A CG    1 
ATOM   1918 C  CD    . LYS   A 1 309 ? 17.436  22.340  19.556  1.00 36.14 ?  419  LYS   A CD    1 
ATOM   1919 C  CE    . LYS   A 1 309 ? 17.342  23.856  19.431  1.00 38.90 ?  419  LYS   A CE    1 
ATOM   1920 N  NZ    . LYS   A 1 309 ? 18.679  24.501  19.280  1.00 37.21 ?  419  LYS   A NZ    1 
ATOM   1921 N  N     . SER   A 1 310 ? 11.976  22.715  19.318  1.00 32.68 ?  420  SER   A N     1 
ATOM   1922 C  CA    . SER   A 1 310 ? 10.789  23.149  18.583  1.00 33.23 ?  420  SER   A CA    1 
ATOM   1923 C  C     . SER   A 1 310 ? 11.065  23.254  17.083  1.00 28.30 ?  420  SER   A C     1 
ATOM   1924 O  O     . SER   A 1 310 ? 12.156  23.658  16.666  1.00 28.12 ?  420  SER   A O     1 
ATOM   1925 C  CB    . SER   A 1 310 ? 10.324  24.500  19.126  1.00 35.36 ?  420  SER   A CB    1 
ATOM   1926 O  OG    . SER   A 1 310 ? 9.303   25.064  18.318  1.00 43.60 ?  420  SER   A OG    1 
ATOM   1927 N  N     . TYR   A 1 311 ? 10.068  22.874  16.272  1.00 24.80 ?  421  TYR   A N     1 
ATOM   1928 C  CA    . TYR   A 1 311 ? 10.121  22.999  14.814  1.00 26.34 ?  421  TYR   A CA    1 
ATOM   1929 C  C     . TYR   A 1 311 ? 8.705   23.269  14.298  1.00 22.46 ?  421  TYR   A C     1 
ATOM   1930 O  O     . TYR   A 1 311 ? 7.788   22.497  14.597  1.00 23.63 ?  421  TYR   A O     1 
ATOM   1931 C  CB    . TYR   A 1 311 ? 10.722  21.728  14.172  1.00 23.28 ?  421  TYR   A CB    1 
ATOM   1932 C  CG    . TYR   A 1 311 ? 10.844  21.789  12.652  1.00 23.86 ?  421  TYR   A CG    1 
ATOM   1933 C  CD1   . TYR   A 1 311 ? 11.435  22.883  12.029  1.00 22.49 ?  421  TYR   A CD1   1 
ATOM   1934 C  CD2   . TYR   A 1 311 ? 10.361  20.753  11.844  1.00 22.38 ?  421  TYR   A CD2   1 
ATOM   1935 C  CE1   . TYR   A 1 311 ? 11.535  22.963  10.637  1.00 20.13 ?  421  TYR   A CE1   1 
ATOM   1936 C  CE2   . TYR   A 1 311 ? 10.457  20.820  10.444  1.00 21.48 ?  421  TYR   A CE2   1 
ATOM   1937 C  CZ    . TYR   A 1 311 ? 11.041  21.936  9.853   1.00 20.51 ?  421  TYR   A CZ    1 
ATOM   1938 O  OH    . TYR   A 1 311 ? 11.139  22.054  8.476   1.00 20.34 ?  421  TYR   A OH    1 
ATOM   1939 N  N     . ARG   A 1 312 ? 8.521   24.360  13.538  1.00 22.31 ?  422  ARG   A N     1 
ATOM   1940 C  CA    . ARG   A 1 312 ? 7.180   24.764  13.100  1.00 22.18 ?  422  ARG   A CA    1 
ATOM   1941 C  C     . ARG   A 1 312 ? 7.201   25.334  11.685  1.00 21.79 ?  422  ARG   A C     1 
ATOM   1942 O  O     . ARG   A 1 312 ? 8.174   25.971  11.268  1.00 21.72 ?  422  ARG   A O     1 
ATOM   1943 C  CB    . ARG   A 1 312 ? 6.572   25.816  14.055  1.00 24.06 ?  422  ARG   A CB    1 
ATOM   1944 C  CG    . ARG   A 1 312 ? 7.222   27.200  13.984  1.00 22.54 ?  422  ARG   A CG    1 
ATOM   1945 C  CD    . ARG   A 1 312 ? 6.651   28.138  15.060  1.00 25.66 ?  422  ARG   A CD    1 
ATOM   1946 N  NE    . ARG   A 1 312 ? 7.230   29.483  15.043  1.00 28.17 ?  422  ARG   A NE    1 
ATOM   1947 C  CZ    . ARG   A 1 312 ? 6.860   30.457  15.874  1.00 31.48 ?  422  ARG   A CZ    1 
ATOM   1948 N  NH1   . ARG   A 1 312 ? 5.916   30.231  16.783  1.00 32.48 ?  422  ARG   A NH1   1 
ATOM   1949 N  NH2   . ARG   A 1 312 ? 7.416   31.653  15.799  1.00 30.03 ?  422  ARG   A NH2   1 
ATOM   1950 N  N     . GLY   A 1 313 ? 6.103   25.127  10.951  1.00 21.58 ?  423  GLY   A N     1 
ATOM   1951 C  CA    . GLY   A 1 313 ? 5.980   25.747  9.643   1.00 22.69 ?  423  GLY   A CA    1 
ATOM   1952 C  C     . GLY   A 1 313 ? 5.833   27.257  9.736   1.00 22.84 ?  423  GLY   A C     1 
ATOM   1953 O  O     . GLY   A 1 313 ? 5.331   27.802  10.725  1.00 22.09 ?  423  GLY   A O     1 
ATOM   1954 N  N     . MET   A 1 314 ? 6.283   27.955  8.681   1.00 20.65 ?  424  MET   A N     1 
ATOM   1955 C  CA    . MET   A 1 314 ? 6.117   29.408  8.643   1.00 20.91 ?  424  MET   A CA    1 
ATOM   1956 C  C     . MET   A 1 314 ? 4.687   29.825  8.317   1.00 23.35 ?  424  MET   A C     1 
ATOM   1957 O  O     . MET   A 1 314 ? 4.361   31.017  8.447   1.00 24.05 ?  424  MET   A O     1 
ATOM   1958 C  CB    . MET   A 1 314 ? 7.100   30.041  7.644   1.00 21.30 ?  424  MET   A CB    1 
ATOM   1959 C  CG    . MET   A 1 314 ? 8.564   29.809  8.013   1.00 21.01 ?  424  MET   A CG    1 
ATOM   1960 S  SD    . MET   A 1 314 ? 8.986   30.454  9.666   1.00 27.05 ?  424  MET   A SD    1 
ATOM   1961 C  CE    . MET   A 1 314 ? 8.924   32.197  9.353   1.00 34.73 ?  424  MET   A CE    1 
ATOM   1962 N  N     . GLY   A 1 315 ? 3.832   28.872  7.922   1.00 20.65 ?  425  GLY   A N     1 
ATOM   1963 C  CA    . GLY   A 1 315 ? 2.407   29.098  7.752   1.00 21.63 ?  425  GLY   A CA    1 
ATOM   1964 C  C     . GLY   A 1 315 ? 1.585   28.486  8.874   1.00 21.33 ?  425  GLY   A C     1 
ATOM   1965 O  O     . GLY   A 1 315 ? 0.371   28.299  8.724   1.00 22.33 ?  425  GLY   A O     1 
ATOM   1966 N  N     . SER   A 1 316 ? 2.224   28.175  10.005  1.00 22.80 ?  426  SER   A N     1 
ATOM   1967 C  CA    . SER   A 1 316 ? 1.505   27.721  11.191  1.00 22.71 ?  426  SER   A CA    1 
ATOM   1968 C  C     . SER   A 1 316 ? 0.893   28.910  11.936  1.00 23.90 ?  426  SER   A C     1 
ATOM   1969 O  O     . SER   A 1 316 ? 1.283   30.069  11.751  1.00 25.63 ?  426  SER   A O     1 
ATOM   1970 C  CB    . SER   A 1 316 ? 2.431   26.942  12.132  1.00 27.54 ?  426  SER   A CB    1 
ATOM   1971 O  OG    . SER   A 1 316 ? 3.419   27.793  12.696  1.00 25.80 ?  426  SER   A OG    1 
ATOM   1972 N  N     . LEU   A 1 317 ? -0.092  28.610  12.786  1.00 27.45 ?  427  LEU   A N     1 
ATOM   1973 C  CA    . LEU   A 1 317 ? -0.744  29.666  13.556  1.00 30.50 ?  427  LEU   A CA    1 
ATOM   1974 C  C     . LEU   A 1 317 ? 0.273   30.467  14.360  1.00 30.66 ?  427  LEU   A C     1 
ATOM   1975 O  O     . LEU   A 1 317 ? 0.249   31.702  14.359  1.00 35.29 ?  427  LEU   A O     1 
ATOM   1976 C  CB    . LEU   A 1 317 ? -1.802  29.052  14.471  1.00 34.60 ?  427  LEU   A CB    1 
ATOM   1977 C  CG    . LEU   A 1 317 ? -2.962  29.933  14.926  1.00 46.71 ?  427  LEU   A CG    1 
ATOM   1978 C  CD1   . LEU   A 1 317 ? -3.546  30.673  13.746  1.00 44.70 ?  427  LEU   A CD1   1 
ATOM   1979 C  CD2   . LEU   A 1 317 ? -4.021  29.056  15.579  1.00 46.33 ?  427  LEU   A CD2   1 
ATOM   1980 N  N     . GLY   A 1 318 ? 1.194   29.775  15.034  1.00 33.46 ?  428  GLY   A N     1 
ATOM   1981 C  CA    . GLY   A 1 318 ? 2.155   30.460  15.887  1.00 35.85 ?  428  GLY   A CA    1 
ATOM   1982 C  C     . GLY   A 1 318 ? 3.139   31.339  15.135  1.00 35.42 ?  428  GLY   A C     1 
ATOM   1983 O  O     . GLY   A 1 318 ? 3.522   32.407  15.623  1.00 37.26 ?  428  GLY   A O     1 
ATOM   1984 N  N     . ALA   A 1 319 ? 3.590   30.898  13.954  1.00 30.31 ?  429  ALA   A N     1 
ATOM   1985 C  CA    . ALA   A 1 319 ? 4.538   31.709  13.191  1.00 27.69 ?  429  ALA   A CA    1 
ATOM   1986 C  C     . ALA   A 1 319 ? 3.863   32.940  12.598  1.00 35.32 ?  429  ALA   A C     1 
ATOM   1987 O  O     . ALA   A 1 319 ? 4.466   34.020  12.543  1.00 31.50 ?  429  ALA   A O     1 
ATOM   1988 C  CB    . ALA   A 1 319 ? 5.194   30.870  12.089  1.00 28.26 ?  429  ALA   A CB    1 
ATOM   1989 N  N     . MET   A 1 320 ? 2.610   32.805  12.148  1.00 32.99 ?  430  MET   A N     1 
ATOM   1990 C  CA    . MET   A 1 320 ? 1.900   33.957  11.602  1.00 32.56 ?  430  MET   A CA    1 
ATOM   1991 C  C     . MET   A 1 320 ? 1.522   34.956  12.686  1.00 38.40 ?  430  MET   A C     1 
ATOM   1992 O  O     . MET   A 1 320 ? 1.310   36.135  12.379  1.00 42.64 ?  430  MET   A O     1 
ATOM   1993 C  CB    . MET   A 1 320 ? 0.657   33.499  10.826  1.00 30.13 ?  430  MET   A CB    1 
ATOM   1994 C  CG    . MET   A 1 320 ? 1.032   32.746  9.549   1.00 31.23 ?  430  MET   A CG    1 
ATOM   1995 S  SD    . MET   A 1 320 ? -0.312  32.371  8.418   1.00 39.90 ?  430  MET   A SD    1 
ATOM   1996 C  CE    . MET   A 1 320 ? -1.280  31.241  9.410   1.00 28.64 ?  430  MET   A CE    1 
ATOM   1997 N  N     . ARG   A 1 321 ? 1.440   34.516  13.938  1.00 37.95 ?  431  ARG   A N     1 
ATOM   1998 C  CA    . ARG   A 1 321 ? 1.292   35.425  15.071  1.00 50.29 ?  431  ARG   A CA    1 
ATOM   1999 C  C     . ARG   A 1 321 ? 2.645   35.633  15.749  1.00 48.67 ?  431  ARG   A C     1 
ATOM   2000 O  O     . ARG   A 1 321 ? 3.161   36.748  15.805  1.00 61.37 ?  431  ARG   A O     1 
ATOM   2001 C  CB    . ARG   A 1 321 ? 0.274   34.883  16.074  1.00 47.15 ?  431  ARG   A CB    1 
ATOM   2002 C  CG    . ARG   A 1 321 ? -1.125  34.718  15.505  1.00 56.03 ?  431  ARG   A CG    1 
ATOM   2003 C  CD    . ARG   A 1 321 ? -2.075  34.101  16.520  1.00 62.42 ?  431  ARG   A CD    1 
ATOM   2004 N  NE    . ARG   A 1 321 ? -3.447  34.053  16.022  1.00 68.15 ?  431  ARG   A NE    1 
ATOM   2005 C  CZ    . ARG   A 1 321 ? -4.459  33.486  16.672  1.00 71.24 ?  431  ARG   A CZ    1 
ATOM   2006 N  NH1   . ARG   A 1 321 ? -4.254  32.911  17.850  1.00 74.11 ?  431  ARG   A NH1   1 
ATOM   2007 N  NH2   . ARG   A 1 321 ? -5.676  33.490  16.142  1.00 71.15 ?  431  ARG   A NH2   1 
ATOM   2008 N  N     . LEU   A 1 345 ? -5.952  34.254  6.202   1.00 44.80 ?  455  LEU   A N     1 
ATOM   2009 C  CA    . LEU   A 1 345 ? -5.475  32.941  5.768   1.00 32.88 ?  455  LEU   A CA    1 
ATOM   2010 C  C     . LEU   A 1 345 ? -5.627  31.891  6.855   1.00 33.46 ?  455  LEU   A C     1 
ATOM   2011 O  O     . LEU   A 1 345 ? -5.283  32.137  8.008   1.00 40.45 ?  455  LEU   A O     1 
ATOM   2012 C  CB    . LEU   A 1 345 ? -4.003  33.016  5.345   1.00 30.01 ?  455  LEU   A CB    1 
ATOM   2013 C  CG    . LEU   A 1 345 ? -3.688  33.859  4.109   1.00 33.76 ?  455  LEU   A CG    1 
ATOM   2014 C  CD1   . LEU   A 1 345 ? -2.195  33.879  3.848   1.00 37.16 ?  455  LEU   A CD1   1 
ATOM   2015 C  CD2   . LEU   A 1 345 ? -4.429  33.328  2.893   1.00 37.85 ?  455  LEU   A CD2   1 
ATOM   2016 N  N     . VAL   A 1 346 ? -6.112  30.705  6.491   1.00 25.56 ?  456  VAL   A N     1 
ATOM   2017 C  CA    . VAL   A 1 346 ? -6.081  29.582  7.425   1.00 23.99 ?  456  VAL   A CA    1 
ATOM   2018 C  C     . VAL   A 1 346 ? -4.675  28.984  7.396   1.00 21.32 ?  456  VAL   A C     1 
ATOM   2019 O  O     . VAL   A 1 346 ? -3.974  29.093  6.379   1.00 24.43 ?  456  VAL   A O     1 
ATOM   2020 C  CB    . VAL   A 1 346 ? -7.156  28.536  7.090   1.00 26.45 ?  456  VAL   A CB    1 
ATOM   2021 C  CG1   . VAL   A 1 346 ? -8.549  29.164  7.203   1.00 29.46 ?  456  VAL   A CG1   1 
ATOM   2022 C  CG2   . VAL   A 1 346 ? -6.936  27.973  5.697   1.00 28.07 ?  456  VAL   A CG2   1 
ATOM   2023 N  N     . PRO   A 1 347 ? -4.216  28.375  8.482   1.00 23.33 ?  457  PRO   A N     1 
ATOM   2024 C  CA    . PRO   A 1 347 ? -2.855  27.825  8.497   1.00 21.84 ?  457  PRO   A CA    1 
ATOM   2025 C  C     . PRO   A 1 347 ? -2.665  26.693  7.496   1.00 24.25 ?  457  PRO   A C     1 
ATOM   2026 O  O     . PRO   A 1 347 ? -3.578  25.909  7.222   1.00 21.68 ?  457  PRO   A O     1 
ATOM   2027 C  CB    . PRO   A 1 347 ? -2.685  27.315  9.935   1.00 26.35 ?  457  PRO   A CB    1 
ATOM   2028 C  CG    . PRO   A 1 347 ? -3.739  28.064  10.734  1.00 33.36 ?  457  PRO   A CG    1 
ATOM   2029 C  CD    . PRO   A 1 347 ? -4.882  28.275  9.793   1.00 27.98 ?  457  PRO   A CD    1 
ATOM   2030 N  N     . GLU   A 1 348 ? -1.437  26.622  6.953   1.00 20.93 ?  458  GLU   A N     1 
ATOM   2031 C  CA    . GLU   A 1 348 ? -0.987  25.542  6.077   1.00 19.29 ?  458  GLU   A CA    1 
ATOM   2032 C  C     . GLU   A 1 348 ? 0.293   24.894  6.606   1.00 19.58 ?  458  GLU   A C     1 
ATOM   2033 O  O     . GLU   A 1 348 ? 1.065   24.316  5.822   1.00 19.56 ?  458  GLU   A O     1 
ATOM   2034 C  CB    . GLU   A 1 348 ? -0.773  26.045  4.637   1.00 17.62 ?  458  GLU   A CB    1 
ATOM   2035 C  CG    . GLU   A 1 348 ? -2.053  26.528  3.929   1.00 21.06 ?  458  GLU   A CG    1 
ATOM   2036 C  CD    . GLU   A 1 348 ? -1.777  27.028  2.517   1.00 20.39 ?  458  GLU   A CD    1 
ATOM   2037 O  OE1   . GLU   A 1 348 ? -0.951  26.394  1.817   1.00 21.03 ?  458  GLU   A OE1   1 
ATOM   2038 O  OE2   . GLU   A 1 348 ? -2.353  28.070  2.130   1.00 20.81 -1 458  GLU   A OE2   1 
ATOM   2039 N  N     . GLY   A 1 349 ? 0.532   24.979  7.924   1.00 19.41 ?  459  GLY   A N     1 
ATOM   2040 C  CA    . GLY   A 1 349 ? 1.617   24.266  8.577   1.00 21.94 ?  459  GLY   A CA    1 
ATOM   2041 C  C     . GLY   A 1 349 ? 1.273   23.940  10.020  1.00 22.57 ?  459  GLY   A C     1 
ATOM   2042 O  O     . GLY   A 1 349 ? 0.327   24.488  10.587  1.00 25.24 ?  459  GLY   A O     1 
ATOM   2043 N  N     . ILE   A 1 350 ? 2.061   23.034  10.616  1.00 24.42 ?  460  ILE   A N     1 
ATOM   2044 C  CA    . ILE   A 1 350 ? 1.870   22.623  12.009  1.00 30.06 ?  460  ILE   A CA    1 
ATOM   2045 C  C     . ILE   A 1 350 ? 3.033   23.105  12.878  1.00 31.74 ?  460  ILE   A C     1 
ATOM   2046 O  O     . ILE   A 1 350 ? 4.108   23.477  12.392  1.00 27.31 ?  460  ILE   A O     1 
ATOM   2047 C  CB    . ILE   A 1 350 ? 1.707   21.095  12.165  1.00 32.47 ?  460  ILE   A CB    1 
ATOM   2048 C  CG1   . ILE   A 1 350 ? 2.999   20.379  11.757  1.00 33.87 ?  460  ILE   A CG1   1 
ATOM   2049 C  CG2   . ILE   A 1 350 ? 0.509   20.584  11.372  1.00 36.64 ?  460  ILE   A CG2   1 
ATOM   2050 C  CD1   . ILE   A 1 350 ? 3.009   18.887  12.056  1.00 45.73 ?  460  ILE   A CD1   1 
ATOM   2051 N  N     . GLU   A 1 351 ? 2.802   23.078  14.196  1.00 28.42 ?  461  GLU   A N     1 
ATOM   2052 C  CA    . GLU   A 1 351 ? 3.813   23.363  15.209  1.00 26.41 ?  461  GLU   A CA    1 
ATOM   2053 C  C     . GLU   A 1 351 ? 4.104   22.081  15.976  1.00 37.08 ?  461  GLU   A C     1 
ATOM   2054 O  O     . GLU   A 1 351 ? 3.177   21.439  16.481  1.00 35.20 ?  461  GLU   A O     1 
ATOM   2055 C  CB    . GLU   A 1 351 ? 3.340   24.452  16.179  1.00 35.65 ?  461  GLU   A CB    1 
ATOM   2056 C  CG    . GLU   A 1 351 ? 2.839   25.721  15.509  1.00 38.23 ?  461  GLU   A CG    1 
ATOM   2057 C  CD    . GLU   A 1 351 ? 2.073   26.636  16.455  1.00 45.73 ?  461  GLU   A CD    1 
ATOM   2058 O  OE1   . GLU   A 1 351 ? 2.584   26.935  17.557  1.00 51.37 ?  461  GLU   A OE1   1 
ATOM   2059 O  OE2   . GLU   A 1 351 ? 0.954   27.057  16.093  1.00 42.83 -1 461  GLU   A OE2   1 
ATOM   2060 N  N     . GLY   A 1 352 ? 5.379   21.711  16.068  1.00 33.79 ?  462  GLY   A N     1 
ATOM   2061 C  CA    . GLY   A 1 352 ? 5.774   20.456  16.686  1.00 35.65 ?  462  GLY   A CA    1 
ATOM   2062 C  C     . GLY   A 1 352 ? 7.187   20.476  17.239  1.00 30.98 ?  462  GLY   A C     1 
ATOM   2063 O  O     . GLY   A 1 352 ? 7.696   21.526  17.641  1.00 33.79 ?  462  GLY   A O     1 
ATOM   2064 N  N     . ARG   A 1 353 ? 7.815   19.298  17.262  1.00 37.46 ?  463  ARG   A N     1 
ATOM   2065 C  CA    . ARG   A 1 353 ? 9.128   19.116  17.870  1.00 41.27 ?  463  ARG   A CA    1 
ATOM   2066 C  C     . ARG   A 1 353 ? 9.867   17.982  17.167  1.00 40.57 ?  463  ARG   A C     1 
ATOM   2067 O  O     . ARG   A 1 353 ? 9.254   17.090  16.574  1.00 39.72 ?  463  ARG   A O     1 
ATOM   2068 C  CB    . ARG   A 1 353 ? 9.000   18.814  19.367  1.00 43.15 ?  463  ARG   A CB    1 
ATOM   2069 C  CG    . ARG   A 1 353 ? 8.528   17.399  19.649  1.00 53.11 ?  463  ARG   A CG    1 
ATOM   2070 C  CD    . ARG   A 1 353 ? 8.226   17.161  21.120  1.00 59.48 ?  463  ARG   A CD    1 
ATOM   2071 N  NE    . ARG   A 1 353 ? 8.093   15.732  21.401  1.00 67.42 ?  463  ARG   A NE    1 
ATOM   2072 C  CZ    . ARG   A 1 353 ? 7.566   15.229  22.512  1.00 68.51 ?  463  ARG   A CZ    1 
ATOM   2073 N  NH1   . ARG   A 1 353 ? 7.108   16.041  23.457  1.00 69.57 ?  463  ARG   A NH1   1 
ATOM   2074 N  NH2   . ARG   A 1 353 ? 7.493   13.913  22.674  1.00 64.38 ?  463  ARG   A NH2   1 
ATOM   2075 N  N     . VAL   A 1 354 ? 11.198  18.012  17.251  1.00 32.88 ?  464  VAL   A N     1 
ATOM   2076 C  CA    . VAL   A 1 354 ? 12.037  16.958  16.679  1.00 31.51 ?  464  VAL   A CA    1 
ATOM   2077 C  C     . VAL   A 1 354 ? 13.094  16.562  17.703  1.00 31.79 ?  464  VAL   A C     1 
ATOM   2078 O  O     . VAL   A 1 354 ? 13.419  17.337  18.616  1.00 34.56 ?  464  VAL   A O     1 
ATOM   2079 C  CB    . VAL   A 1 354 ? 12.699  17.404  15.354  1.00 36.61 ?  464  VAL   A CB    1 
ATOM   2080 C  CG1   . VAL   A 1 354 ? 11.636  17.705  14.301  1.00 37.82 ?  464  VAL   A CG1   1 
ATOM   2081 C  CG2   . VAL   A 1 354 ? 13.589  18.615  15.584  1.00 32.42 ?  464  VAL   A CG2   1 
ATOM   2082 N  N     . PRO   A 1 355 ? 13.650  15.358  17.583  1.00 33.50 ?  465  PRO   A N     1 
ATOM   2083 C  CA    . PRO   A 1 355 ? 14.666  14.927  18.552  1.00 36.20 ?  465  PRO   A CA    1 
ATOM   2084 C  C     . PRO   A 1 355 ? 15.940  15.752  18.434  1.00 35.55 ?  465  PRO   A C     1 
ATOM   2085 O  O     . PRO   A 1 355 ? 16.326  16.195  17.350  1.00 34.77 ?  465  PRO   A O     1 
ATOM   2086 C  CB    . PRO   A 1 355 ? 14.916  13.460  18.184  1.00 39.63 ?  465  PRO   A CB    1 
ATOM   2087 C  CG    . PRO   A 1 355 ? 14.493  13.344  16.762  1.00 49.95 ?  465  PRO   A CG    1 
ATOM   2088 C  CD    . PRO   A 1 355 ? 13.364  14.321  16.577  1.00 36.88 ?  465  PRO   A CD    1 
ATOM   2089 N  N     . PHE   A 1 356 ? 16.594  15.953  19.579  1.00 36.78 ?  466  PHE   A N     1 
ATOM   2090 C  CA    . PHE   A 1 356 ? 17.866  16.664  19.616  1.00 35.38 ?  466  PHE   A CA    1 
ATOM   2091 C  C     . PHE   A 1 356 ? 18.966  15.829  18.971  1.00 34.15 ?  466  PHE   A C     1 
ATOM   2092 O  O     . PHE   A 1 356 ? 19.084  14.624  19.225  1.00 33.88 ?  466  PHE   A O     1 
ATOM   2093 C  CB    . PHE   A 1 356 ? 18.231  17.005  21.060  1.00 35.45 ?  466  PHE   A CB    1 
ATOM   2094 C  CG    . PHE   A 1 356 ? 19.526  17.751  21.207  1.00 35.31 ?  466  PHE   A CG    1 
ATOM   2095 C  CD1   . PHE   A 1 356 ? 19.643  19.057  20.764  1.00 29.23 ?  466  PHE   A CD1   1 
ATOM   2096 C  CD2   . PHE   A 1 356 ? 20.622  17.151  21.813  1.00 32.76 ?  466  PHE   A CD2   1 
ATOM   2097 C  CE1   . PHE   A 1 356 ? 20.831  19.756  20.909  1.00 34.90 ?  466  PHE   A CE1   1 
ATOM   2098 C  CE2   . PHE   A 1 356 ? 21.808  17.840  21.954  1.00 28.97 ?  466  PHE   A CE2   1 
ATOM   2099 C  CZ    . PHE   A 1 356 ? 21.916  19.140  21.508  1.00 31.15 ?  466  PHE   A CZ    1 
ATOM   2100 N  N     . ARG   A 1 357 ? 19.790  16.481  18.142  1.00 27.97 ?  467  ARG   A N     1 
ATOM   2101 C  CA    . ARG   A 1 357 ? 20.738  15.775  17.288  1.00 34.00 ?  467  ARG   A CA    1 
ATOM   2102 C  C     . ARG   A 1 357 ? 22.202  16.138  17.510  1.00 32.33 ?  467  ARG   A C     1 
ATOM   2103 O  O     . ARG   A 1 357 ? 23.067  15.529  16.873  1.00 34.39 ?  467  ARG   A O     1 
ATOM   2104 C  CB    . ARG   A 1 357 ? 20.388  16.005  15.809  1.00 42.35 ?  467  ARG   A CB    1 
ATOM   2105 C  CG    . ARG   A 1 357 ? 19.269  15.112  15.294  1.00 46.38 ?  467  ARG   A CG    1 
ATOM   2106 C  CD    . ARG   A 1 357 ? 19.772  13.708  14.998  1.00 48.45 ?  467  ARG   A CD    1 
ATOM   2107 N  NE    . ARG   A 1 357 ? 18.729  12.704  15.176  1.00 56.03 ?  467  ARG   A NE    1 
ATOM   2108 C  CZ    . ARG   A 1 357 ? 18.730  11.788  16.141  1.00 65.81 ?  467  ARG   A CZ    1 
ATOM   2109 N  NH1   . ARG   A 1 357 ? 19.728  11.740  17.016  1.00 63.06 ?  467  ARG   A NH1   1 
ATOM   2110 N  NH2   . ARG   A 1 357 ? 17.736  10.913  16.228  1.00 65.40 ?  467  ARG   A NH2   1 
ATOM   2111 N  N     . GLY   A 1 358 ? 22.517  17.108  18.370  1.00 30.59 ?  468  GLY   A N     1 
ATOM   2112 C  CA    . GLY   A 1 358 ? 23.898  17.458  18.628  1.00 27.86 ?  468  GLY   A CA    1 
ATOM   2113 C  C     . GLY   A 1 358 ? 24.421  18.556  17.717  1.00 24.72 ?  468  GLY   A C     1 
ATOM   2114 O  O     . GLY   A 1 358 ? 23.650  19.315  17.125  1.00 25.96 ?  468  GLY   A O     1 
ATOM   2115 N  N     . PRO   A 1 359 ? 25.742  18.655  17.577  1.00 24.21 ?  469  PRO   A N     1 
ATOM   2116 C  CA    . PRO   A 1 359 ? 26.324  19.735  16.768  1.00 24.12 ?  469  PRO   A CA    1 
ATOM   2117 C  C     . PRO   A 1 359 ? 26.055  19.579  15.276  1.00 29.06 ?  469  PRO   A C     1 
ATOM   2118 O  O     . PRO   A 1 359 ? 26.015  18.468  14.735  1.00 26.43 ?  469  PRO   A O     1 
ATOM   2119 C  CB    . PRO   A 1 359 ? 27.827  19.632  17.056  1.00 30.35 ?  469  PRO   A CB    1 
ATOM   2120 C  CG    . PRO   A 1 359 ? 27.963  18.679  18.197  1.00 31.87 ?  469  PRO   A CG    1 
ATOM   2121 C  CD    . PRO   A 1 359 ? 26.767  17.809  18.213  1.00 29.57 ?  469  PRO   A CD    1 
ATOM   2122 N  N     . LEU   A 1 360 ? 25.905  20.730  14.608  1.00 27.62 ?  470  LEU   A N     1 
ATOM   2123 C  CA    . LEU   A 1 360 ? 25.635  20.742  13.172  1.00 28.14 ?  470  LEU   A CA    1 
ATOM   2124 C  C     . LEU   A 1 360 ? 26.760  20.083  12.379  1.00 33.47 ?  470  LEU   A C     1 
ATOM   2125 O  O     . LEU   A 1 360 ? 26.499  19.319  11.440  1.00 27.22 ?  470  LEU   A O     1 
ATOM   2126 C  CB    . LEU   A 1 360 ? 25.419  22.176  12.682  1.00 28.63 ?  470  LEU   A CB    1 
ATOM   2127 C  CG    . LEU   A 1 360 ? 25.288  22.116  11.155  1.00 40.21 ?  470  LEU   A CG    1 
ATOM   2128 C  CD1   . LEU   A 1 360 ? 23.839  21.859  10.707  1.00 26.71 ?  470  LEU   A CD1   1 
ATOM   2129 C  CD2   . LEU   A 1 360 ? 25.877  23.317  10.479  1.00 31.21 ?  470  LEU   A CD2   1 
ATOM   2130 N  N     . SER   A 1 361 ? 28.019  20.377  12.734  1.00 30.02 ?  471  SER   A N     1 
ATOM   2131 C  CA    . SER   A 1 361 ? 29.157  19.814  12.012  1.00 33.30 ?  471  SER   A CA    1 
ATOM   2132 C  C     . SER   A 1 361 ? 29.049  18.302  11.881  1.00 29.75 ?  471  SER   A C     1 
ATOM   2133 O  O     . SER   A 1 361 ? 29.335  17.741  10.815  1.00 30.64 ?  471  SER   A O     1 
ATOM   2134 C  CB    . SER   A 1 361 ? 30.461  20.193  12.721  1.00 35.95 ?  471  SER   A CB    1 
ATOM   2135 O  OG    . SER   A 1 361 ? 30.462  19.684  14.045  1.00 38.34 ?  471  SER   A OG    1 
ATOM   2136 N  N     . SER   A 1 362 ? 28.616  17.624  12.948  1.00 30.88 ?  472  SER   A N     1 
ATOM   2137 C  CA    . SER   A 1 362 ? 28.522  16.169  12.916  1.00 31.96 ?  472  SER   A CA    1 
ATOM   2138 C  C     . SER   A 1 362 ? 27.342  15.682  12.077  1.00 31.62 ?  472  SER   A C     1 
ATOM   2139 O  O     . SER   A 1 362 ? 27.431  14.616  11.451  1.00 30.14 ?  472  SER   A O     1 
ATOM   2140 C  CB    . SER   A 1 362 ? 28.418  15.619  14.338  1.00 40.13 ?  472  SER   A CB    1 
ATOM   2141 O  OG    . SER   A 1 362 ? 29.576  15.943  15.094  1.00 42.01 ?  472  SER   A OG    1 
ATOM   2142 N  N     . VAL   A 1 363 ? 26.227  16.416  12.072  1.00 29.68 ?  473  VAL   A N     1 
ATOM   2143 C  CA    . VAL   A 1 363 ? 25.099  16.040  11.218  1.00 23.81 ?  473  VAL   A CA    1 
ATOM   2144 C  C     . VAL   A 1 363 ? 25.490  16.149  9.748   1.00 22.99 ?  473  VAL   A C     1 
ATOM   2145 O  O     . VAL   A 1 363 ? 25.221  15.241  8.948   1.00 25.52 ?  473  VAL   A O     1 
ATOM   2146 C  CB    . VAL   A 1 363 ? 23.864  16.904  11.534  1.00 24.56 ?  473  VAL   A CB    1 
ATOM   2147 C  CG1   . VAL   A 1 363 ? 22.812  16.720  10.435  1.00 23.40 ?  473  VAL   A CG1   1 
ATOM   2148 C  CG2   . VAL   A 1 363 ? 23.279  16.523  12.887  1.00 29.96 ?  473  VAL   A CG2   1 
ATOM   2149 N  N     . ILE   A 1 364 ? 26.116  17.266  9.369   1.00 22.30 ?  474  ILE   A N     1 
ATOM   2150 C  CA    . ILE   A 1 364 ? 26.533  17.455  7.979   1.00 22.55 ?  474  ILE   A CA    1 
ATOM   2151 C  C     . ILE   A 1 364 ? 27.536  16.379  7.565   1.00 25.06 ?  474  ILE   A C     1 
ATOM   2152 O  O     . ILE   A 1 364 ? 27.511  15.894  6.426   1.00 23.32 ?  474  ILE   A O     1 
ATOM   2153 C  CB    . ILE   A 1 364 ? 27.089  18.880  7.770   1.00 24.74 ?  474  ILE   A CB    1 
ATOM   2154 C  CG1   . ILE   A 1 364 ? 26.003  19.940  8.004   1.00 25.87 ?  474  ILE   A CG1   1 
ATOM   2155 C  CG2   . ILE   A 1 364 ? 27.657  19.042  6.363   1.00 25.60 ?  474  ILE   A CG2   1 
ATOM   2156 C  CD1   . ILE   A 1 364 ? 24.850  19.855  7.014   1.00 26.49 ?  474  ILE   A CD1   1 
ATOM   2157 N  N     . HIS   A 1 365 ? 28.424  15.971  8.480   1.00 25.33 ?  475  HIS   A N     1 
ATOM   2158 C  CA    . HIS   A 1 365 ? 29.380  14.911  8.147   1.00 28.82 ?  475  HIS   A CA    1 
ATOM   2159 C  C     . HIS   A 1 365 ? 28.677  13.611  7.771   1.00 25.44 ?  475  HIS   A C     1 
ATOM   2160 O  O     . HIS   A 1 365 ? 29.077  12.928  6.815   1.00 26.18 ?  475  HIS   A O     1 
ATOM   2161 C  CB    . HIS   A 1 365 ? 30.343  14.673  9.316   1.00 28.02 ?  475  HIS   A CB    1 
ATOM   2162 C  CG    . HIS   A 1 365 ? 31.278  13.523  9.097   1.00 38.73 ?  475  HIS   A CG    1 
ATOM   2163 N  ND1   . HIS   A 1 365 ? 30.993  12.240  9.516   1.00 40.93 ?  475  HIS   A ND1   1 
ATOM   2164 C  CD2   . HIS   A 1 365 ? 32.488  13.458  8.491   1.00 43.41 ?  475  HIS   A CD2   1 
ATOM   2165 C  CE1   . HIS   A 1 365 ? 31.988  11.436  9.183   1.00 41.68 ?  475  HIS   A CE1   1 
ATOM   2166 N  NE2   . HIS   A 1 365 ? 32.908  12.151  8.560   1.00 45.00 ?  475  HIS   A NE2   1 
ATOM   2167 N  N     . GLN   A 1 366 ? 27.630  13.237  8.514   1.00 24.17 ?  476  GLN   A N     1 
ATOM   2168 C  CA    . GLN   A 1 366 ? 26.933  11.992  8.213   1.00 26.80 ?  476  GLN   A CA    1 
ATOM   2169 C  C     . GLN   A 1 366 ? 26.147  12.099  6.909   1.00 24.32 ?  476  GLN   A C     1 
ATOM   2170 O  O     . GLN   A 1 366 ? 26.106  11.145  6.120   1.00 23.37 ?  476  GLN   A O     1 
ATOM   2171 C  CB    . GLN   A 1 366 ? 26.019  11.610  9.379   1.00 30.21 ?  476  GLN   A CB    1 
ATOM   2172 C  CG    . GLN   A 1 366 ? 26.771  11.198  10.644  1.00 38.93 ?  476  GLN   A CG    1 
ATOM   2173 C  CD    . GLN   A 1 366 ? 27.480  9.857   10.493  1.00 47.66 ?  476  GLN   A CD    1 
ATOM   2174 O  OE1   . GLN   A 1 366 ? 26.846  8.835   10.223  1.00 52.79 ?  476  GLN   A OE1   1 
ATOM   2175 N  NE2   . GLN   A 1 366 ? 28.800  9.858   10.657  1.00 43.67 ?  476  GLN   A NE2   1 
ATOM   2176 N  N     . LEU   A 1 367 ? 25.528  13.257  6.657   1.00 22.43 ?  477  LEU   A N     1 
ATOM   2177 C  CA    . LEU   A 1 367 ? 24.771  13.437  5.416   1.00 19.96 ?  477  LEU   A CA    1 
ATOM   2178 C  C     . LEU   A 1 367 ? 25.678  13.389  4.191   1.00 20.90 ?  477  LEU   A C     1 
ATOM   2179 O  O     . LEU   A 1 367 ? 25.350  12.734  3.193   1.00 20.19 ?  477  LEU   A O     1 
ATOM   2180 C  CB    . LEU   A 1 367 ? 24.001  14.764  5.462   1.00 19.65 ?  477  LEU   A CB    1 
ATOM   2181 C  CG    . LEU   A 1 367 ? 22.935  14.926  6.549   1.00 20.33 ?  477  LEU   A CG    1 
ATOM   2182 C  CD1   . LEU   A 1 367 ? 22.336  16.341  6.521   1.00 23.35 ?  477  LEU   A CD1   1 
ATOM   2183 C  CD2   . LEU   A 1 367 ? 21.830  13.904  6.396   1.00 19.45 ?  477  LEU   A CD2   1 
ATOM   2184 N  N     . THR   A 1 368 ? 26.837  14.059  4.242   1.00 19.30 ?  478  THR   A N     1 
ATOM   2185 C  CA    . THR   A 1 368 ? 27.737  14.022  3.091   1.00 18.90 ?  478  THR   A CA    1 
ATOM   2186 C  C     . THR   A 1 368 ? 28.361  12.641  2.916   1.00 20.53 ?  478  THR   A C     1 
ATOM   2187 O  O     . THR   A 1 368 ? 28.652  12.231  1.785   1.00 20.80 ?  478  THR   A O     1 
ATOM   2188 C  CB    . THR   A 1 368 ? 28.837  15.089  3.216   1.00 25.89 ?  478  THR   A CB    1 
ATOM   2189 O  OG1   . THR   A 1 368 ? 29.675  14.801  4.340   1.00 30.40 ?  478  THR   A OG1   1 
ATOM   2190 C  CG2   . THR   A 1 368 ? 28.239  16.486  3.381   1.00 20.55 ?  478  THR   A CG2   1 
ATOM   2191 N  N     . GLY   A 1 369 ? 28.556  11.902  4.009   1.00 19.54 ?  479  GLY   A N     1 
ATOM   2192 C  CA    . GLY   A 1 369 ? 29.067  10.539  3.883   1.00 21.67 ?  479  GLY   A CA    1 
ATOM   2193 C  C     . GLY   A 1 369 ? 28.115  9.611   3.143   1.00 21.36 ?  479  GLY   A C     1 
ATOM   2194 O  O     . GLY   A 1 369 ? 28.545  8.755   2.368   1.00 19.96 ?  479  GLY   A O     1 
ATOM   2195 N  N     . GLY   A 1 370 ? 26.809  9.766   3.369   1.00 18.35 ?  480  GLY   A N     1 
ATOM   2196 C  CA    . GLY   A 1 370 ? 25.842  8.981   2.609   1.00 17.86 ?  480  GLY   A CA    1 
ATOM   2197 C  C     . GLY   A 1 370 ? 25.808  9.352   1.136   1.00 18.80 ?  480  GLY   A C     1 
ATOM   2198 O  O     . GLY   A 1 370 ? 25.713  8.475   0.266   1.00 18.52 ?  480  GLY   A O     1 
ATOM   2199 N  N     . LEU   A 1 371 ? 25.876  10.661  0.835   1.00 16.75 ?  481  LEU   A N     1 
ATOM   2200 C  CA    . LEU   A 1 371 ? 26.019  11.102  -0.552  1.00 16.87 ?  481  LEU   A CA    1 
ATOM   2201 C  C     . LEU   A 1 371 ? 27.267  10.503  -1.201  1.00 18.99 ?  481  LEU   A C     1 
ATOM   2202 O  O     . LEU   A 1 371 ? 27.205  10.010  -2.337  1.00 17.78 ?  481  LEU   A O     1 
ATOM   2203 C  CB    . LEU   A 1 371 ? 26.049  12.638  -0.609  1.00 19.25 ?  481  LEU   A CB    1 
ATOM   2204 C  CG    . LEU   A 1 371 ? 26.298  13.309  -1.968  1.00 17.17 ?  481  LEU   A CG    1 
ATOM   2205 C  CD1   . LEU   A 1 371 ? 25.209  12.941  -2.991  1.00 19.93 ?  481  LEU   A CD1   1 
ATOM   2206 C  CD2   . LEU   A 1 371 ? 26.416  14.832  -1.818  1.00 17.51 ?  481  LEU   A CD2   1 
ATOM   2207 N  N     . ARG   A 1 372 ? 28.405  10.512  -0.494  1.00 17.64 ?  482  ARG   A N     1 
ATOM   2208 C  CA    . ARG   A 1 372 ? 29.633  9.944   -1.064  1.00 18.40 ?  482  ARG   A CA    1 
ATOM   2209 C  C     . ARG   A 1 372 ? 29.480  8.447   -1.357  1.00 18.90 ?  482  ARG   A C     1 
ATOM   2210 O  O     . ARG   A 1 372 ? 29.993  7.954   -2.375  1.00 18.12 ?  482  ARG   A O     1 
ATOM   2211 C  CB    . ARG   A 1 372 ? 30.834  10.203  -0.137  1.00 17.94 ?  482  ARG   A CB    1 
ATOM   2212 C  CG    . ARG   A 1 372 ? 31.319  11.655  -0.081  1.00 20.35 ?  482  ARG   A CG    1 
ATOM   2213 C  CD    . ARG   A 1 372 ? 32.549  11.797  0.860   1.00 21.46 ?  482  ARG   A CD    1 
ATOM   2214 N  NE    . ARG   A 1 372 ? 33.092  13.144  0.753   1.00 27.93 ?  482  ARG   A NE    1 
ATOM   2215 C  CZ    . ARG   A 1 372 ? 33.925  13.521  -0.211  1.00 32.51 ?  482  ARG   A CZ    1 
ATOM   2216 N  NH1   . ARG   A 1 372 ? 34.318  12.641  -1.125  1.00 30.63 ?  482  ARG   A NH1   1 
ATOM   2217 N  NH2   . ARG   A 1 372 ? 34.353  14.776  -0.269  1.00 30.76 ?  482  ARG   A NH2   1 
ATOM   2218 N  N     . ALA   A 1 373 ? 28.771  7.703   -0.487  1.00 16.33 ?  483  ALA   A N     1 
ATOM   2219 C  CA    . ALA   A 1 373 ? 28.512  6.280   -0.750  1.00 16.62 ?  483  ALA   A CA    1 
ATOM   2220 C  C     . ALA   A 1 373 ? 27.713  6.085   -2.042  1.00 18.41 ?  483  ALA   A C     1 
ATOM   2221 O  O     . ALA   A 1 373 ? 28.033  5.208   -2.859  1.00 17.70 ?  483  ALA   A O     1 
ATOM   2222 C  CB    . ALA   A 1 373 ? 27.789  5.630   0.437   1.00 17.46 ?  483  ALA   A CB    1 
ATOM   2223 N  N     . ALA   A 1 374 ? 26.648  6.878   -2.227  1.00 16.34 ?  484  ALA   A N     1 
ATOM   2224 C  CA    . ALA   A 1 374 ? 25.872  6.827   -3.465  1.00 16.08 ?  484  ALA   A CA    1 
ATOM   2225 C  C     . ALA   A 1 374 ? 26.734  7.116   -4.690  1.00 17.15 ?  484  ALA   A C     1 
ATOM   2226 O  O     . ALA   A 1 374 ? 26.551  6.492   -5.743  1.00 17.26 ?  484  ALA   A O     1 
ATOM   2227 C  CB    . ALA   A 1 374 ? 24.718  7.829   -3.409  1.00 15.96 ?  484  ALA   A CB    1 
ATOM   2228 N  N     . MET   A 1 375 ? 27.661  8.082   -4.589  1.00 17.68 ?  485  MET   A N     1 
ATOM   2229 C  CA    . MET   A 1 375 ? 28.521  8.369   -5.737  1.00 16.89 ?  485  MET   A CA    1 
ATOM   2230 C  C     . MET   A 1 375 ? 29.454  7.189   -6.051  1.00 15.65 ?  485  MET   A C     1 
ATOM   2231 O  O     . MET   A 1 375 ? 29.697  6.879   -7.231  1.00 17.57 ?  485  MET   A O     1 
ATOM   2232 C  CB    . MET   A 1 375 ? 29.299  9.672   -5.478  1.00 17.49 ?  485  MET   A CB    1 
ATOM   2233 C  CG    . MET   A 1 375 ? 28.377  10.924  -5.322  1.00 16.51 ?  485  MET   A CG    1 
ATOM   2234 S  SD    . MET   A 1 375 ? 29.207  12.500  -4.917  1.00 17.68 ?  485  MET   A SD    1 
ATOM   2235 C  CE    . MET   A 1 375 ? 29.911  12.914  -6.500  1.00 20.16 ?  485  MET   A CE    1 
ATOM   2236 N  N     . GLY   A 1 376 ? 29.918  6.475   -5.026  1.00 16.96 ?  486  GLY   A N     1 
ATOM   2237 C  CA    . GLY   A 1 376 ? 30.683  5.254   -5.268  1.00 17.34 ?  486  GLY   A CA    1 
ATOM   2238 C  C     . GLY   A 1 376 ? 29.882  4.165   -5.979  1.00 17.16 ?  486  GLY   A C     1 
ATOM   2239 O  O     . GLY   A 1 376 ? 30.365  3.546   -6.933  1.00 16.73 ?  486  GLY   A O     1 
ATOM   2240 N  N     . TYR   A 1 377 ? 28.640  3.922   -5.533  1.00 15.23 ?  487  TYR   A N     1 
ATOM   2241 C  CA    . TYR   A 1 377 ? 27.828  2.858   -6.134  1.00 15.48 ?  487  TYR   A CA    1 
ATOM   2242 C  C     . TYR   A 1 377 ? 27.432  3.165   -7.579  1.00 18.44 ?  487  TYR   A C     1 
ATOM   2243 O  O     . TYR   A 1 377 ? 27.230  2.229   -8.367  1.00 17.69 ?  487  TYR   A O     1 
ATOM   2244 C  CB    . TYR   A 1 377 ? 26.541  2.618   -5.319  1.00 16.19 ?  487  TYR   A CB    1 
ATOM   2245 C  CG    . TYR   A 1 377 ? 26.686  1.844   -4.028  1.00 16.93 ?  487  TYR   A CG    1 
ATOM   2246 C  CD1   . TYR   A 1 377 ? 27.022  0.488   -4.035  1.00 18.41 ?  487  TYR   A CD1   1 
ATOM   2247 C  CD2   . TYR   A 1 377 ? 26.445  2.456   -2.798  1.00 16.67 ?  487  TYR   A CD2   1 
ATOM   2248 C  CE1   . TYR   A 1 377 ? 27.135  -0.233  -2.842  1.00 18.88 ?  487  TYR   A CE1   1 
ATOM   2249 C  CE2   . TYR   A 1 377 ? 26.547  1.749   -1.601  1.00 18.24 ?  487  TYR   A CE2   1 
ATOM   2250 C  CZ    . TYR   A 1 377 ? 26.911  0.399   -1.627  1.00 20.93 ?  487  TYR   A CZ    1 
ATOM   2251 O  OH    . TYR   A 1 377 ? 27.015  -0.332  -0.447  1.00 19.47 ?  487  TYR   A OH    1 
ATOM   2252 N  N     . THR   A 1 378 ? 27.245  4.446   -7.933  1.00 17.33 ?  488  THR   A N     1 
ATOM   2253 C  CA    . THR   A 1 378 ? 26.763  4.840   -9.259  1.00 16.17 ?  488  THR   A CA    1 
ATOM   2254 C  C     . THR   A 1 378 ? 27.893  5.202   -10.223 1.00 17.73 ?  488  THR   A C     1 
ATOM   2255 O  O     . THR   A 1 378 ? 27.621  5.499   -11.390 1.00 19.12 ?  488  THR   A O     1 
ATOM   2256 C  CB    . THR   A 1 378 ? 25.764  6.018   -9.159  1.00 15.96 ?  488  THR   A CB    1 
ATOM   2257 O  OG1   . THR   A 1 378 ? 26.397  7.174   -8.575  1.00 17.18 ?  488  THR   A OG1   1 
ATOM   2258 C  CG2   . THR   A 1 378 ? 24.513  5.639   -8.342  1.00 17.24 ?  488  THR   A CG2   1 
ATOM   2259 N  N     . GLY   A 1 379 ? 29.149  5.156   -9.777  1.00 16.38 ?  489  GLY   A N     1 
ATOM   2260 C  CA    . GLY   A 1 379 ? 30.268  5.553   -10.638 1.00 19.26 ?  489  GLY   A CA    1 
ATOM   2261 C  C     . GLY   A 1 379 ? 30.300  7.028   -11.012 1.00 21.65 ?  489  GLY   A C     1 
ATOM   2262 O  O     . GLY   A 1 379 ? 30.627  7.368   -12.160 1.00 21.18 ?  489  GLY   A O     1 
ATOM   2263 N  N     . SER   A 1 380 ? 29.988  7.914   -10.064 1.00 18.57 ?  490  SER   A N     1 
ATOM   2264 C  CA    . SER   A 1 380 ? 29.859  9.353   -10.310 1.00 18.21 ?  490  SER   A CA    1 
ATOM   2265 C  C     . SER   A 1 380 ? 31.021  10.096  -9.643  1.00 17.99 ?  490  SER   A C     1 
ATOM   2266 O  O     . SER   A 1 380 ? 31.041  10.230  -8.410  1.00 18.27 ?  490  SER   A O     1 
ATOM   2267 C  CB    . SER   A 1 380 ? 28.518  9.865   -9.763  1.00 19.99 ?  490  SER   A CB    1 
ATOM   2268 O  OG    . SER   A 1 380 ? 27.380  9.248   -10.351 1.00 18.59 ?  490  SER   A OG    1 
ATOM   2269 N  N     . PRO   A 1 381 ? 32.032  10.574  -10.388 1.00 19.27 ?  491  PRO   A N     1 
ATOM   2270 C  CA    . PRO   A 1 381 ? 33.142  11.281  -9.722  1.00 22.78 ?  491  PRO   A CA    1 
ATOM   2271 C  C     . PRO   A 1 381 ? 32.793  12.687  -9.278  1.00 20.48 ?  491  PRO   A C     1 
ATOM   2272 O  O     . PRO   A 1 381 ? 33.505  13.241  -8.422  1.00 21.24 ?  491  PRO   A O     1 
ATOM   2273 C  CB    . PRO   A 1 381 ? 34.249  11.306  -10.790 1.00 22.42 ?  491  PRO   A CB    1 
ATOM   2274 C  CG    . PRO   A 1 381 ? 33.537  11.212  -12.096 1.00 23.20 ?  491  PRO   A CG    1 
ATOM   2275 C  CD    . PRO   A 1 381 ? 32.280  10.372  -11.829 1.00 21.52 ?  491  PRO   A CD    1 
ATOM   2276 N  N     . THR   A 1 382 ? 31.713  13.257  -9.821  1.00 20.47 ?  492  THR   A N     1 
ATOM   2277 C  CA    . THR   A 1 382 ? 31.278  14.627  -9.586  1.00 17.46 ?  492  THR   A CA    1 
ATOM   2278 C  C     . THR   A 1 382 ? 29.756  14.637  -9.519  1.00 19.18 ?  492  THR   A C     1 
ATOM   2279 O  O     . THR   A 1 382 ? 29.100  13.669  -9.914  1.00 18.57 ?  492  THR   A O     1 
ATOM   2280 C  CB    . THR   A 1 382 ? 31.739  15.562  -10.707 1.00 20.00 ?  492  THR   A CB    1 
ATOM   2281 O  OG1   . THR   A 1 382 ? 31.150  15.143  -11.947 1.00 21.21 ?  492  THR   A OG1   1 
ATOM   2282 C  CG2   . THR   A 1 382 ? 33.278  15.575  -10.840 1.00 21.44 ?  492  THR   A CG2   1 
ATOM   2283 N  N     . ILE   A 1 383 ? 29.192  15.753  -9.027  1.00 18.23 ?  493  ILE   A N     1 
ATOM   2284 C  CA    . ILE   A 1 383 ? 27.730  15.891  -8.971  1.00 18.02 ?  493  ILE   A CA    1 
ATOM   2285 C  C     . ILE   A 1 383 ? 27.145  15.962  -10.379 1.00 19.75 ?  493  ILE   A C     1 
ATOM   2286 O  O     . ILE   A 1 383 ? 26.045  15.452  -10.627 1.00 19.63 ?  493  ILE   A O     1 
ATOM   2287 C  CB    . ILE   A 1 383 ? 27.308  17.118  -8.129  1.00 18.27 ?  493  ILE   A CB    1 
ATOM   2288 C  CG1   . ILE   A 1 383 ? 27.740  16.973  -6.664  1.00 18.12 ?  493  ILE   A CG1   1 
ATOM   2289 C  CG2   . ILE   A 1 383 ? 25.789  17.339  -8.202  1.00 18.86 ?  493  ILE   A CG2   1 
ATOM   2290 C  CD1   . ILE   A 1 383 ? 27.258  15.710  -5.972  1.00 21.56 ?  493  ILE   A CD1   1 
ATOM   2291 N  N     . GLU   A 1 384 ? 27.863  16.569  -11.328 1.00 20.51 ?  494  GLU   A N     1 
ATOM   2292 C  CA    . GLU   A 1 384 ? 27.368  16.624  -12.703 1.00 22.68 ?  494  GLU   A CA    1 
ATOM   2293 C  C     . GLU   A 1 384 ? 27.195  15.226  -13.313 1.00 22.30 ?  494  GLU   A C     1 
ATOM   2294 O  O     . GLU   A 1 384 ? 26.306  15.028  -14.151 1.00 23.72 ?  494  GLU   A O     1 
ATOM   2295 C  CB    . GLU   A 1 384 ? 28.303  17.484  -13.561 1.00 27.37 ?  494  GLU   A CB    1 
ATOM   2296 C  CG    . GLU   A 1 384 ? 28.178  19.012  -13.311 1.00 29.19 ?  494  GLU   A CG    1 
ATOM   2297 C  CD    . GLU   A 1 384 ? 28.935  19.523  -12.074 1.00 27.23 ?  494  GLU   A CD    1 
ATOM   2298 O  OE1   . GLU   A 1 384 ? 29.837  18.833  -11.567 1.00 25.29 ?  494  GLU   A OE1   1 
ATOM   2299 O  OE2   . GLU   A 1 384 ? 28.637  20.653  -11.615 1.00 30.34 -1 494  GLU   A OE2   1 
ATOM   2300 N  N     . VAL   A 1 385 ? 28.016  14.251  -12.913 1.00 19.75 ?  495  VAL   A N     1 
ATOM   2301 C  CA    . VAL   A 1 385 ? 27.813  12.873  -13.366 1.00 20.22 ?  495  VAL   A CA    1 
ATOM   2302 C  C     . VAL   A 1 385 ? 26.674  12.201  -12.597 1.00 19.88 ?  495  VAL   A C     1 
ATOM   2303 O  O     . VAL   A 1 385 ? 25.909  11.420  -13.173 1.00 21.27 ?  495  VAL   A O     1 
ATOM   2304 C  CB    . VAL   A 1 385 ? 29.125  12.070  -13.255 1.00 21.75 ?  495  VAL   A CB    1 
ATOM   2305 C  CG1   . VAL   A 1 385 ? 28.907  10.599  -13.676 1.00 22.05 ?  495  VAL   A CG1   1 
ATOM   2306 C  CG2   . VAL   A 1 385 ? 30.211  12.714  -14.113 1.00 22.47 ?  495  VAL   A CG2   1 
ATOM   2307 N  N     . LEU   A 1 386 ? 26.538  12.471  -11.290 1.00 18.13 ?  496  LEU   A N     1 
ATOM   2308 C  CA    . LEU   A 1 386 ? 25.411  11.893  -10.536 1.00 18.01 ?  496  LEU   A CA    1 
ATOM   2309 C  C     . LEU   A 1 386 ? 24.056  12.284  -11.135 1.00 18.70 ?  496  LEU   A C     1 
ATOM   2310 O  O     . LEU   A 1 386 ? 23.092  11.496  -11.076 1.00 17.78 ?  496  LEU   A O     1 
ATOM   2311 C  CB    . LEU   A 1 386 ? 25.502  12.315  -9.061  1.00 17.34 ?  496  LEU   A CB    1 
ATOM   2312 C  CG    . LEU   A 1 386 ? 24.426  11.814  -8.078  1.00 16.67 ?  496  LEU   A CG    1 
ATOM   2313 C  CD1   . LEU   A 1 386 ? 24.393  10.289  -7.934  1.00 17.41 ?  496  LEU   A CD1   1 
ATOM   2314 C  CD2   . LEU   A 1 386 ? 24.606  12.473  -6.712  1.00 17.74 ?  496  LEU   A CD2   1 
ATOM   2315 N  N     . GLN   A 1 387 ? 23.960  13.489  -11.717 1.00 19.17 ?  497  GLN   A N     1 
ATOM   2316 C  CA    . GLN   A 1 387 ? 22.735  13.973  -12.351 1.00 18.33 ?  497  GLN   A CA    1 
ATOM   2317 C  C     . GLN   A 1 387 ? 22.329  13.149  -13.569 1.00 18.97 ?  497  GLN   A C     1 
ATOM   2318 O  O     . GLN   A 1 387 ? 21.208  13.334  -14.072 1.00 20.66 ?  497  GLN   A O     1 
ATOM   2319 C  CB    . GLN   A 1 387 ? 22.916  15.464  -12.724 1.00 19.08 ?  497  GLN   A CB    1 
ATOM   2320 C  CG    . GLN   A 1 387 ? 23.042  16.427  -11.516 1.00 17.83 ?  497  GLN   A CG    1 
ATOM   2321 C  CD    . GLN   A 1 387 ? 23.335  17.890  -11.912 1.00 19.73 ?  497  GLN   A CD    1 
ATOM   2322 O  OE1   . GLN   A 1 387 ? 23.944  18.161  -12.966 1.00 21.15 ?  497  GLN   A OE1   1 
ATOM   2323 N  NE2   . GLN   A 1 387 ? 22.923  18.838  -11.055 1.00 19.34 ?  497  GLN   A NE2   1 
ATOM   2324 N  N     . GLN   A 1 388 ? 23.190  12.227  -14.037 1.00 20.41 ?  498  GLN   A N     1 
ATOM   2325 C  CA    . GLN   A 1 388 ? 22.877  11.324  -15.141 1.00 21.14 ?  498  GLN   A CA    1 
ATOM   2326 C  C     . GLN   A 1 388 ? 22.548  9.893   -14.688 1.00 20.95 ?  498  GLN   A C     1 
ATOM   2327 O  O     . GLN   A 1 388 ? 22.349  9.021   -15.542 1.00 22.76 ?  498  GLN   A O     1 
ATOM   2328 C  CB    . GLN   A 1 388 ? 24.059  11.291  -16.133 1.00 23.51 ?  498  GLN   A CB    1 
ATOM   2329 C  CG    . GLN   A 1 388 ? 24.466  12.695  -16.641 1.00 27.81 ?  498  GLN   A CG    1 
ATOM   2330 C  CD    . GLN   A 1 388 ? 25.816  12.715  -17.351 1.00 42.56 ?  498  GLN   A CD    1 
ATOM   2331 O  OE1   . GLN   A 1 388 ? 26.166  11.786  -18.080 1.00 45.15 ?  498  GLN   A OE1   1 
ATOM   2332 N  NE2   . GLN   A 1 388 ? 26.582  13.781  -17.132 1.00 41.73 ?  498  GLN   A NE2   1 
ATOM   2333 N  N     . ALA   A 1 389 ? 22.491  9.621   -13.380 1.00 18.22 ?  499  ALA   A N     1 
ATOM   2334 C  CA    . ALA   A 1 389 ? 22.235  8.262   -12.896 1.00 19.39 ?  499  ALA   A CA    1 
ATOM   2335 C  C     . ALA   A 1 389 ? 20.785  7.825   -13.152 1.00 18.39 ?  499  ALA   A C     1 
ATOM   2336 O  O     . ALA   A 1 389 ? 19.883  8.646   -13.349 1.00 20.82 ?  499  ALA   A O     1 
ATOM   2337 C  CB    . ALA   A 1 389 ? 22.558  8.172   -11.399 1.00 19.34 ?  499  ALA   A CB    1 
ATOM   2338 N  N     . GLN   A 1 390 ? 20.552  6.501   -13.123 1.00 17.73 ?  500  GLN   A N     1 
ATOM   2339 C  CA    . GLN   A 1 390 ? 19.227  5.923   -13.363 1.00 17.83 ?  500  GLN   A CA    1 
ATOM   2340 C  C     . GLN   A 1 390 ? 18.570  5.373   -12.091 1.00 15.18 ?  500  GLN   A C     1 
ATOM   2341 O  O     . GLN   A 1 390 ? 19.256  4.946   -11.156 1.00 17.51 ?  500  GLN   A O     1 
ATOM   2342 C  CB    . GLN   A 1 390 ? 19.307  4.784   -14.395 1.00 18.99 ?  500  GLN   A CB    1 
ATOM   2343 C  CG    . GLN   A 1 390 ? 19.714  5.214   -15.795 1.00 20.90 ?  500  GLN   A CG    1 
ATOM   2344 C  CD    . GLN   A 1 390 ? 19.822  4.031   -16.754 1.00 23.75 ?  500  GLN   A CD    1 
ATOM   2345 O  OE1   . GLN   A 1 390 ? 20.724  3.195   -16.632 1.00 23.28 ?  500  GLN   A OE1   1 
ATOM   2346 N  NE2   . GLN   A 1 390 ? 18.900  3.954   -17.710 1.00 24.30 ?  500  GLN   A NE2   1 
ATOM   2347 N  N     . PHE   A 1 391 ? 17.219  5.362   -12.086 1.00 14.78 ?  501  PHE   A N     1 
ATOM   2348 C  CA    . PHE   A 1 391 ? 16.368  4.822   -11.018 1.00 15.23 ?  501  PHE   A CA    1 
ATOM   2349 C  C     . PHE   A 1 391 ? 15.741  3.468   -11.381 1.00 17.45 ?  501  PHE   A C     1 
ATOM   2350 O  O     . PHE   A 1 391 ? 15.475  3.174   -12.556 1.00 16.83 ?  501  PHE   A O     1 
ATOM   2351 C  CB    . PHE   A 1 391 ? 15.207  5.791   -10.682 1.00 16.45 ?  501  PHE   A CB    1 
ATOM   2352 C  CG    . PHE   A 1 391 ? 15.642  7.162   -10.160 1.00 17.23 ?  501  PHE   A CG    1 
ATOM   2353 C  CD1   . PHE   A 1 391 ? 16.268  7.286   -8.922  1.00 16.80 ?  501  PHE   A CD1   1 
ATOM   2354 C  CD2   . PHE   A 1 391 ? 15.330  8.326   -10.871 1.00 21.04 ?  501  PHE   A CD2   1 
ATOM   2355 C  CE1   . PHE   A 1 391 ? 16.633  8.538   -8.418  1.00 17.40 ?  501  PHE   A CE1   1 
ATOM   2356 C  CE2   . PHE   A 1 391 ? 15.706  9.599   -10.381 1.00 20.20 ?  501  PHE   A CE2   1 
ATOM   2357 C  CZ    . PHE   A 1 391 ? 16.352  9.698   -9.148  1.00 16.73 ?  501  PHE   A CZ    1 
ATOM   2358 N  N     . VAL   A 1 392 ? 15.442  2.663   -10.345 1.00 15.15 ?  502  VAL   A N     1 
ATOM   2359 C  CA    . VAL   A 1 392 ? 14.448  1.586   -10.413 1.00 15.26 ?  502  VAL   A CA    1 
ATOM   2360 C  C     . VAL   A 1 392 ? 13.249  1.979   -9.540  1.00 16.99 ?  502  VAL   A C     1 
ATOM   2361 O  O     . VAL   A 1 392 ? 13.410  2.513   -8.432  1.00 16.91 ?  502  VAL   A O     1 
ATOM   2362 C  CB    . VAL   A 1 392 ? 15.050  0.211   -10.007 1.00 15.66 ?  502  VAL   A CB    1 
ATOM   2363 C  CG1   . VAL   A 1 392 ? 15.719  0.230   -8.623  1.00 18.96 ?  502  VAL   A CG1   1 
ATOM   2364 C  CG2   . VAL   A 1 392 ? 13.981  -0.920  -10.075 1.00 17.93 ?  502  VAL   A CG2   1 
ATOM   2365 N  N     . ARG   A 1 393 ? 12.043  1.772   -10.067 1.00 16.29 ?  503  ARG   A N     1 
ATOM   2366 C  CA    . ARG   A 1 393 ? 10.832  2.044   -9.292  1.00 17.55 ?  503  ARG   A CA    1 
ATOM   2367 C  C     . ARG   A 1 393 ? 10.488  0.866   -8.391  1.00 20.59 ?  503  ARG   A C     1 
ATOM   2368 O  O     . ARG   A 1 393 ? 10.655  -0.293  -8.778  1.00 20.72 ?  503  ARG   A O     1 
ATOM   2369 C  CB    . ARG   A 1 393 ? 9.658   2.322   -10.224 1.00 20.63 ?  503  ARG   A CB    1 
ATOM   2370 C  CG    . ARG   A 1 393 ? 8.428   2.719   -9.439  1.00 27.71 ?  503  ARG   A CG    1 
ATOM   2371 C  CD    . ARG   A 1 393 ? 7.385   3.376   -10.284 1.00 26.37 ?  503  ARG   A CD    1 
ATOM   2372 N  NE    . ARG   A 1 393 ? 6.133   3.368   -9.543  1.00 28.79 ?  503  ARG   A NE    1 
ATOM   2373 C  CZ    . ARG   A 1 393 ? 4.945   3.384   -10.114 1.00 28.54 ?  503  ARG   A CZ    1 
ATOM   2374 N  NH1   . ARG   A 1 393 ? 4.857   3.423   -11.434 1.00 34.51 ?  503  ARG   A NH1   1 
ATOM   2375 N  NH2   . ARG   A 1 393 ? 3.851   3.353   -9.364  1.00 38.02 ?  503  ARG   A NH2   1 
ATOM   2376 N  N     . ILE   A 1 394 ? 9.993   1.151   -7.186  1.00 18.95 ?  504  ILE   A N     1 
ATOM   2377 C  CA    . ILE   A 1 394 ? 9.660   0.059   -6.277  1.00 20.56 ?  504  ILE   A CA    1 
ATOM   2378 C  C     . ILE   A 1 394 ? 8.165   0.084   -5.946  1.00 20.68 ?  504  ILE   A C     1 
ATOM   2379 O  O     . ILE   A 1 394 ? 7.458   1.078   -6.156  1.00 23.57 ?  504  ILE   A O     1 
ATOM   2380 C  CB    . ILE   A 1 394 ? 10.524  0.070   -4.993  1.00 27.99 ?  504  ILE   A CB    1 
ATOM   2381 C  CG1   . ILE   A 1 394 ? 10.234  1.281   -4.123  1.00 30.05 ?  504  ILE   A CG1   1 
ATOM   2382 C  CG2   . ILE   A 1 394 ? 12.043  -0.015  -5.337  1.00 26.28 ?  504  ILE   A CG2   1 
ATOM   2383 C  CD1   . ILE   A 1 394 ? 11.089  1.304   -2.857  1.00 39.34 ?  504  ILE   A CD1   1 
ATOM   2384 N  N     . THR   A 1 395 ? 7.676   -1.054  -5.450  1.00 23.51 ?  505  THR   A N     1 
ATOM   2385 C  CA    . THR   A 1 395 ? 6.284   -1.208  -5.043  1.00 23.80 ?  505  THR   A CA    1 
ATOM   2386 C  C     . THR   A 1 395 ? 6.129   -0.979  -3.546  1.00 23.97 ?  505  THR   A C     1 
ATOM   2387 O  O     . THR   A 1 395 ? 7.113   -0.901  -2.799  1.00 29.93 ?  505  THR   A O     1 
ATOM   2388 C  CB    . THR   A 1 395 ? 5.786   -2.623  -5.384  1.00 27.51 ?  505  THR   A CB    1 
ATOM   2389 O  OG1   . THR   A 1 395 ? 6.430   -3.547  -4.509  1.00 32.14 ?  505  THR   A OG1   1 
ATOM   2390 C  CG2   . THR   A 1 395 ? 6.096   -3.003  -6.817  1.00 28.30 ?  505  THR   A CG2   1 
ATOM   2391 N  N     . PRO   A 1 396 ? 4.887   -0.954  -3.054  1.00 31.49 ?  506  PRO   A N     1 
ATOM   2392 C  CA    . PRO   A 1 396 ? 4.678   -0.831  -1.600  1.00 37.32 ?  506  PRO   A CA    1 
ATOM   2393 C  C     . PRO   A 1 396 ? 5.351   -1.918  -0.783  1.00 43.69 ?  506  PRO   A C     1 
ATOM   2394 O  O     . PRO   A 1 396 ? 5.789   -1.655  0.344   1.00 46.73 ?  506  PRO   A O     1 
ATOM   2395 C  CB    . PRO   A 1 396 ? 3.149   -0.898  -1.474  1.00 29.87 ?  506  PRO   A CB    1 
ATOM   2396 C  CG    . PRO   A 1 396 ? 2.649   -0.382  -2.770  1.00 37.62 ?  506  PRO   A CG    1 
ATOM   2397 C  CD    . PRO   A 1 396 ? 3.621   -0.856  -3.803  1.00 31.90 ?  506  PRO   A CD    1 
ATOM   2398 N  N     . ALA   A 1 397 ? 5.423   -3.147  -1.307  1.00 38.28 ?  507  ALA   A N     1 
ATOM   2399 C  CA    . ALA   A 1 397 ? 6.051   -4.220  -0.547  1.00 38.25 ?  507  ALA   A CA    1 
ATOM   2400 C  C     . ALA   A 1 397 ? 7.545   -3.985  -0.383  1.00 43.22 ?  507  ALA   A C     1 
ATOM   2401 O  O     . ALA   A 1 397 ? 8.146   -4.456  0.588   1.00 48.27 ?  507  ALA   A O     1 
ATOM   2402 C  CB    . ALA   A 1 397 ? 5.795   -5.569  -1.224  1.00 34.63 ?  507  ALA   A CB    1 
ATOM   2403 N  N     . GLY   A 1 398 ? 8.160   -3.251  -1.311  1.00 43.46 ?  508  GLY   A N     1 
ATOM   2404 C  CA    . GLY   A 1 398 ? 9.589   -3.025  -1.231  1.00 47.68 ?  508  GLY   A CA    1 
ATOM   2405 C  C     . GLY   A 1 398 ? 9.996   -1.904  -0.305  1.00 55.25 ?  508  GLY   A C     1 
ATOM   2406 O  O     . GLY   A 1 398 ? 11.147  -1.866  0.139   1.00 56.75 ?  508  GLY   A O     1 
ATOM   2407 N  N     . LEU   A 1 399 ? 9.078   -0.989  -0.002  1.00 55.55 ?  509  LEU   A N     1 
ATOM   2408 C  CA    . LEU   A 1 399 ? 9.419   0.117   0.881   1.00 62.00 ?  509  LEU   A CA    1 
ATOM   2409 C  C     . LEU   A 1 399 ? 9.412   -0.317  2.341   1.00 67.16 ?  509  LEU   A C     1 
ATOM   2410 O  O     . LEU   A 1 399 ? 10.303  0.064   3.108   1.00 67.42 ?  509  LEU   A O     1 
ATOM   2411 C  CB    . LEU   A 1 399 ? 8.451   1.279   0.657   1.00 55.60 ?  509  LEU   A CB    1 
ATOM   2412 C  CG    . LEU   A 1 399 ? 8.841   2.607   1.303   1.00 54.37 ?  509  LEU   A CG    1 
ATOM   2413 C  CD1   . LEU   A 1 399 ? 10.181  3.095   0.751   1.00 45.70 ?  509  LEU   A CD1   1 
ATOM   2414 C  CD2   . LEU   A 1 399 ? 7.740   3.644   1.094   1.00 52.18 ?  509  LEU   A CD2   1 
ATOM   2415 N  N     . LYS   A 1 400 ? 8.425   -1.127  2.737   1.00 64.84 ?  510  LYS   A N     1 
ATOM   2416 C  CA    . LYS   A 1 400 ? 8.308   -1.532  4.134   1.00 70.07 ?  510  LYS   A CA    1 
ATOM   2417 C  C     . LYS   A 1 400 ? 9.573   -2.211  4.644   1.00 75.31 ?  510  LYS   A C     1 
ATOM   2418 O  O     . LYS   A 1 400 ? 9.928   -2.054  5.819   1.00 78.85 ?  510  LYS   A O     1 
ATOM   2419 C  CB    . LYS   A 1 400 ? 7.099   -2.451  4.312   1.00 72.82 ?  510  LYS   A CB    1 
ATOM   2420 C  CG    . LYS   A 1 400 ? 5.887   -1.741  4.896   1.00 79.56 ?  510  LYS   A CG    1 
ATOM   2421 C  CD    . LYS   A 1 400 ? 4.638   -1.971  4.063   1.00 80.81 ?  510  LYS   A CD    1 
ATOM   2422 C  CE    . LYS   A 1 400 ? 3.567   -0.943  4.399   1.00 80.82 ?  510  LYS   A CE    1 
ATOM   2423 N  NZ    . LYS   A 1 400 ? 2.373   -1.071  3.519   1.00 77.22 ?  510  LYS   A NZ    1 
ATOM   2424 N  N     . GLU   A 1 401 ? 10.266  -2.963  3.788   1.00 73.20 ?  511  GLU   A N     1 
ATOM   2425 C  CA    . GLU   A 1 401 ? 11.489  -3.643  4.198   1.00 72.20 ?  511  GLU   A CA    1 
ATOM   2426 C  C     . GLU   A 1 401 ? 12.710  -2.731  4.189   1.00 73.03 ?  511  GLU   A C     1 
ATOM   2427 O  O     . GLU   A 1 401 ? 13.751  -3.117  4.734   1.00 71.42 ?  511  GLU   A O     1 
ATOM   2428 C  CB    . GLU   A 1 401 ? 11.749  -4.851  3.294   1.00 67.93 ?  511  GLU   A CB    1 
ATOM   2429 C  CG    . GLU   A 1 401 ? 11.936  -4.494  1.828   1.00 63.85 ?  511  GLU   A CG    1 
ATOM   2430 C  CD    . GLU   A 1 401 ? 12.100  -5.715  0.940   1.00 56.21 ?  511  GLU   A CD    1 
ATOM   2431 O  OE1   . GLU   A 1 401 ? 12.466  -5.543  -0.243  1.00 49.31 ?  511  GLU   A OE1   1 
ATOM   2432 O  OE2   . GLU   A 1 401 ? 11.860  -6.843  1.422   1.00 63.75 -1 511  GLU   A OE2   1 
ATOM   2433 N  N     . SER   A 1 402 ? 12.609  -1.540  3.591   1.00 74.44 ?  512  SER   A N     1 
ATOM   2434 C  CA    . SER   A 1 402 ? 13.756  -0.638  3.529   1.00 70.67 ?  512  SER   A CA    1 
ATOM   2435 C  C     . SER   A 1 402 ? 14.080  -0.058  4.901   1.00 73.99 ?  512  SER   A C     1 
ATOM   2436 O  O     . SER   A 1 402 ? 15.254  0.044   5.277   1.00 67.69 ?  512  SER   A O     1 
ATOM   2437 C  CB    . SER   A 1 402 ? 13.494  0.477   2.515   1.00 65.72 ?  512  SER   A CB    1 
ATOM   2438 O  OG    . SER   A 1 402 ? 13.301  -0.053  1.212   1.00 63.02 ?  512  SER   A OG    1 
ATOM   2439 N  N     . HIS   A 1 403 ? 13.062  0.333   5.658   1.00 78.57 ?  513  HIS   A N     1 
ATOM   2440 C  CA    . HIS   A 1 403 ? 13.286  0.695   7.051   1.00 85.86 ?  513  HIS   A CA    1 
ATOM   2441 C  C     . HIS   A 1 403 ? 13.592  -0.573  7.841   1.00 85.57 ?  513  HIS   A C     1 
ATOM   2442 O  O     . HIS   A 1 403 ? 12.796  -1.520  7.805   1.00 84.14 ?  513  HIS   A O     1 
ATOM   2443 C  CB    . HIS   A 1 403 ? 12.071  1.416   7.633   1.00 88.53 ?  513  HIS   A CB    1 
ATOM   2444 C  CG    . HIS   A 1 403 ? 12.387  2.769   8.192   1.00 89.61 ?  513  HIS   A CG    1 
ATOM   2445 N  ND1   . HIS   A 1 403 ? 11.696  3.320   9.250   1.00 93.60 ?  513  HIS   A ND1   1 
ATOM   2446 C  CD2   . HIS   A 1 403 ? 13.324  3.682   7.839   1.00 81.50 ?  513  HIS   A CD2   1 
ATOM   2447 C  CE1   . HIS   A 1 403 ? 12.193  4.513   9.525   1.00 89.38 ?  513  HIS   A CE1   1 
ATOM   2448 N  NE2   . HIS   A 1 403 ? 13.182  4.756   8.683   1.00 82.62 ?  513  HIS   A NE2   1 
ATOM   2449 N  N     . PRO   A 1 404 ? 14.719  -0.618  8.587   1.00 87.23 ?  514  PRO   A N     1 
ATOM   2450 C  CA    . PRO   A 1 404 ? 15.255  -1.895  9.094   1.00 81.15 ?  514  PRO   A CA    1 
ATOM   2451 C  C     . PRO   A 1 404 ? 14.211  -2.974  9.341   1.00 85.83 ?  514  PRO   A C     1 
ATOM   2452 O  O     . PRO   A 1 404 ? 13.506  -2.951  10.355  1.00 91.07 ?  514  PRO   A O     1 
ATOM   2453 C  CB    . PRO   A 1 404 ? 15.944  -1.474  10.397  1.00 79.70 ?  514  PRO   A CB    1 
ATOM   2454 C  CG    . PRO   A 1 404 ? 16.430  -0.083  10.105  1.00 79.40 ?  514  PRO   A CG    1 
ATOM   2455 C  CD    . PRO   A 1 404 ? 15.422  0.544   9.162   1.00 86.06 ?  514  PRO   A CD    1 
ATOM   2456 N  N     . HIS   A 1 405 ? 14.112  -3.931  8.417   1.00 82.37 ?  515  HIS   A N     1 
ATOM   2457 C  CA    . HIS   A 1 405 ? 13.007  -4.884  8.407   1.00 81.35 ?  515  HIS   A CA    1 
ATOM   2458 C  C     . HIS   A 1 405 ? 13.359  -6.097  9.266   1.00 80.52 ?  515  HIS   A C     1 
ATOM   2459 O  O     . HIS   A 1 405 ? 14.274  -6.861  8.942   1.00 71.49 ?  515  HIS   A O     1 
ATOM   2460 C  CB    . HIS   A 1 405 ? 12.641  -5.278  6.972   1.00 78.34 ?  515  HIS   A CB    1 
ATOM   2461 C  CG    . HIS   A 1 405 ? 13.533  -6.316  6.356   1.00 70.09 ?  515  HIS   A CG    1 
ATOM   2462 N  ND1   . HIS   A 1 405 ? 13.417  -7.663  6.637   1.00 64.24 ?  515  HIS   A ND1   1 
ATOM   2463 C  CD2   . HIS   A 1 405 ? 14.534  -6.209  5.448   1.00 62.11 ?  515  HIS   A CD2   1 
ATOM   2464 C  CE1   . HIS   A 1 405 ? 14.314  -8.338  5.940   1.00 52.17 ?  515  HIS   A CE1   1 
ATOM   2465 N  NE2   . HIS   A 1 405 ? 15.005  -7.479  5.210   1.00 56.90 ?  515  HIS   A NE2   1 
ATOM   2466 N  N     . ASP   A 1 406 ? 12.651  -6.240  10.387  1.00 85.80 ?  516  ASP   A N     1 
ATOM   2467 C  CA    . ASP   A 1 406 ? 12.583  -7.482  11.159  1.00 85.36 ?  516  ASP   A CA    1 
ATOM   2468 C  C     . ASP   A 1 406 ? 13.957  -7.929  11.670  1.00 84.16 ?  516  ASP   A C     1 
ATOM   2469 O  O     . ASP   A 1 406 ? 14.482  -8.980  11.295  1.00 76.98 ?  516  ASP   A O     1 
ATOM   2470 C  CB    . ASP   A 1 406 ? 11.910  -8.584  10.333  1.00 86.27 ?  516  ASP   A CB    1 
ATOM   2471 C  CG    . ASP   A 1 406 ? 11.680  -9.851  11.132  1.00 88.10 ?  516  ASP   A CG    1 
ATOM   2472 O  OD1   . ASP   A 1 406 ? 12.561  -10.738 11.111  1.00 84.47 ?  516  ASP   A OD1   1 
ATOM   2473 O  OD2   . ASP   A 1 406 ? 10.627  -9.949  11.797  1.00 90.90 -1 516  ASP   A OD2   1 
ATOM   2474 N  N     . VAL   A 1 407 ? 14.520  -7.110  12.560  1.00 81.86 ?  517  VAL   A N     1 
ATOM   2475 C  CA    . VAL   A 1 407 ? 15.672  -7.475  13.385  1.00 74.74 ?  517  VAL   A CA    1 
ATOM   2476 C  C     . VAL   A 1 407 ? 15.782  -6.459  14.514  1.00 74.90 ?  517  VAL   A C     1 
ATOM   2477 O  O     . VAL   A 1 407 ? 16.328  -5.365  14.325  1.00 72.56 ?  517  VAL   A O     1 
ATOM   2478 C  CB    . VAL   A 1 407 ? 16.984  -7.543  12.580  1.00 61.74 ?  517  VAL   A CB    1 
ATOM   2479 C  CG1   . VAL   A 1 407 ? 17.119  -8.884  11.853  1.00 55.53 ?  517  VAL   A CG1   1 
ATOM   2480 C  CG2   . VAL   A 1 407 ? 17.076  -6.375  11.608  1.00 60.88 ?  517  VAL   A CG2   1 
ATOM   2481 N  N     . ALA   A 1 408 ? 15.263  -6.816  15.691  1.00 70.47 ?  518  ALA   A N     1 
ATOM   2482 C  CA    . ALA   A 1 408 ? 15.216  -5.915  16.837  1.00 67.67 ?  518  ALA   A CA    1 
ATOM   2483 C  C     . ALA   A 1 408 ? 16.504  -5.114  16.984  1.00 65.91 ?  518  ALA   A C     1 
ATOM   2484 O  O     . ALA   A 1 408 ? 17.546  -5.662  17.358  1.00 61.79 ?  518  ALA   A O     1 
ATOM   2485 C  CB    . ALA   A 1 408 ? 14.932  -6.703  18.119  1.00 65.16 ?  518  ALA   A CB    1 
ATOM   2486 N  N     . MET   A 1 409 ? 16.440  -3.819  16.680  1.00 69.23 ?  519  MET   A N     1 
ATOM   2487 C  CA    . MET   A 1 409 ? 17.598  -2.949  16.827  1.00 64.97 ?  519  MET   A CA    1 
ATOM   2488 C  C     . MET   A 1 409 ? 17.913  -2.738  18.304  1.00 68.67 ?  519  MET   A C     1 
ATOM   2489 O  O     . MET   A 1 409 ? 17.011  -2.608  19.136  1.00 73.15 ?  519  MET   A O     1 
ATOM   2490 C  CB    . MET   A 1 409 ? 17.338  -1.607  16.142  1.00 72.58 ?  519  MET   A CB    1 
ATOM   2491 C  CG    . MET   A 1 409 ? 18.592  -0.826  15.778  1.00 65.97 ?  519  MET   A CG    1 
ATOM   2492 S  SD    . MET   A 1 409 ? 18.208  0.764   15.015  1.00 80.66 ?  519  MET   A SD    1 
ATOM   2493 C  CE    . MET   A 1 409 ? 16.975  0.280   13.808  1.00 72.57 ?  519  MET   A CE    1 
ATOM   2494 N  N     . THR   A 1 410 ? 19.206  -2.706  18.628  1.00 65.78 ?  520  THR   A N     1 
ATOM   2495 C  CA    . THR   A 1 410 ? 19.631  -2.633  20.021  1.00 69.39 ?  520  THR   A CA    1 
ATOM   2496 C  C     . THR   A 1 410 ? 20.577  -1.463  20.269  1.00 73.54 ?  520  THR   A C     1 
ATOM   2497 O  O     . THR   A 1 410 ? 20.554  -0.865  21.349  1.00 76.57 ?  520  THR   A O     1 
ATOM   2498 C  CB    . THR   A 1 410 ? 20.303  -3.943  20.450  1.00 64.78 ?  520  THR   A CB    1 
ATOM   2499 O  OG1   . THR   A 1 410 ? 21.552  -4.093  19.763  1.00 60.46 ?  520  THR   A OG1   1 
ATOM   2500 C  CG2   . THR   A 1 410 ? 19.409  -5.139  20.134  1.00 61.01 ?  520  THR   A CG2   1 
ATOM   2501 N  N     . VAL   A 1 411 ? 21.412  -1.131  19.288  1.00 70.47 ?  521  VAL   A N     1 
ATOM   2502 C  CA    . VAL   A 1 411 ? 22.428  -0.102  19.458  1.00 73.18 ?  521  VAL   A CA    1 
ATOM   2503 C  C     . VAL   A 1 411 ? 22.069  1.107   18.603  1.00 79.35 ?  521  VAL   A C     1 
ATOM   2504 O  O     . VAL   A 1 411 ? 21.348  1.012   17.602  1.00 77.16 ?  521  VAL   A O     1 
ATOM   2505 C  CB    . VAL   A 1 411 ? 23.843  -0.620  19.115  1.00 68.84 ?  521  VAL   A CB    1 
ATOM   2506 C  CG1   . VAL   A 1 411 ? 24.893  0.419   19.479  1.00 67.45 ?  521  VAL   A CG1   1 
ATOM   2507 C  CG2   . VAL   A 1 411 ? 24.121  -1.936  19.828  1.00 64.34 ?  521  VAL   A CG2   1 
ATOM   2508 N  N     . GLU   A 1 412 ? 22.581  2.264   19.019  1.00 83.51 ?  522  GLU   A N     1 
ATOM   2509 C  CA    . GLU   A 1 412 ? 22.371  3.504   18.283  1.00 85.78 ?  522  GLU   A CA    1 
ATOM   2510 C  C     . GLU   A 1 412 ? 23.121  3.482   16.956  1.00 83.63 ?  522  GLU   A C     1 
ATOM   2511 O  O     . GLU   A 1 412 ? 24.227  2.942   16.857  1.00 80.53 ?  522  GLU   A O     1 
ATOM   2512 C  CB    . GLU   A 1 412 ? 22.835  4.698   19.119  1.00 90.99 ?  522  GLU   A CB    1 
ATOM   2513 C  CG    . GLU   A 1 412 ? 21.791  5.262   20.067  1.00 92.65 ?  522  GLU   A CG    1 
ATOM   2514 C  CD    . GLU   A 1 412 ? 20.734  6.071   19.344  1.00 98.77 ?  522  GLU   A CD    1 
ATOM   2515 O  OE1   . GLU   A 1 412 ? 19.796  5.465   18.783  1.00 99.75 ?  522  GLU   A OE1   1 
ATOM   2516 O  OE2   . GLU   A 1 412 ? 20.850  7.316   19.321  1.00 99.10 -1 522  GLU   A OE2   1 
ATOM   2517 N  N     . ALA   A 1 413 ? 22.509  4.074   15.932  1.00 81.07 ?  523  ALA   A N     1 
ATOM   2518 C  CA    . ALA   A 1 413 ? 23.141  4.264   14.638  1.00 77.70 ?  523  ALA   A CA    1 
ATOM   2519 C  C     . ALA   A 1 413 ? 23.268  5.754   14.352  1.00 78.03 ?  523  ALA   A C     1 
ATOM   2520 O  O     . ALA   A 1 413 ? 22.289  6.496   14.522  1.00 76.81 ?  523  ALA   A O     1 
ATOM   2521 C  CB    . ALA   A 1 413 ? 22.337  3.579   13.520  1.00 71.93 ?  523  ALA   A CB    1 
ATOM   2522 N  N     . PRO   A 1 414 ? 24.440  6.234   13.924  1.00 79.35 ?  524  PRO   A N     1 
ATOM   2523 C  CA    . PRO   A 1 414 ? 24.593  7.683   13.713  1.00 75.63 ?  524  PRO   A CA    1 
ATOM   2524 C  C     . PRO   A 1 414 ? 23.758  8.216   12.562  1.00 75.05 ?  524  PRO   A C     1 
ATOM   2525 O  O     . PRO   A 1 414 ? 23.337  9.380   12.603  1.00 71.64 ?  524  PRO   A O     1 
ATOM   2526 C  CB    . PRO   A 1 414 ? 26.097  7.841   13.446  1.00 70.53 ?  524  PRO   A CB    1 
ATOM   2527 C  CG    . PRO   A 1 414 ? 26.525  6.515   12.903  1.00 66.56 ?  524  PRO   A CG    1 
ATOM   2528 C  CD    . PRO   A 1 414 ? 25.669  5.488   13.599  1.00 70.03 ?  524  PRO   A CD    1 
ATOM   2529 N  N     . ASN   A 1 415 ? 23.498  7.403   11.543  1.00 73.16 ?  525  ASN   A N     1 
ATOM   2530 C  CA    . ASN   A 1 415 ? 22.782  7.861   10.357  1.00 66.73 ?  525  ASN   A CA    1 
ATOM   2531 C  C     . ASN   A 1 415 ? 21.469  7.110   10.139  1.00 65.29 ?  525  ASN   A C     1 
ATOM   2532 O  O     . ASN   A 1 415 ? 20.720  7.410   9.206   1.00 63.59 ?  525  ASN   A O     1 
ATOM   2533 C  CB    . ASN   A 1 415 ? 23.674  7.723   9.120   1.00 55.14 ?  525  ASN   A CB    1 
ATOM   2534 C  CG    . ASN   A 1 415 ? 24.377  6.369   9.040   1.00 53.80 ?  525  ASN   A CG    1 
ATOM   2535 O  OD1   . ASN   A 1 415 ? 24.139  5.473   9.853   1.00 53.85 ?  525  ASN   A OD1   1 
ATOM   2536 N  ND2   . ASN   A 1 415 ? 25.242  6.218   8.047   1.00 29.52 ?  525  ASN   A ND2   1 
HETATM 2537 P  P     . IMP   B 2 .   ? 11.421  19.692  5.528   1.00 18.05 ?  801  IMP   A P     1 
HETATM 2538 O  O1P   . IMP   B 2 .   ? 12.927  19.782  5.307   1.00 21.20 ?  801  IMP   A O1P   1 
HETATM 2539 O  O2P   . IMP   B 2 .   ? 10.746  18.435  4.962   1.00 17.60 ?  801  IMP   A O2P   1 
HETATM 2540 O  O3P   . IMP   B 2 .   ? 11.077  19.881  7.001   1.00 19.74 ?  801  IMP   A O3P   1 
HETATM 2541 O  "O5'" . IMP   B 2 .   ? 10.768  20.927  4.712   1.00 19.12 ?  801  IMP   A "O5'" 1 
HETATM 2542 C  "C5'" . IMP   B 2 .   ? 11.125  22.316  4.939   1.00 17.50 ?  801  IMP   A "C5'" 1 
HETATM 2543 C  "C4'" . IMP   B 2 .   ? 10.506  23.177  3.864   1.00 15.54 ?  801  IMP   A "C4'" 1 
HETATM 2544 O  "O4'" . IMP   B 2 .   ? 9.079   23.267  4.078   1.00 17.53 ?  801  IMP   A "O4'" 1 
HETATM 2545 C  "C3'" . IMP   B 2 .   ? 10.948  24.636  3.833   1.00 15.68 ?  801  IMP   A "C3'" 1 
HETATM 2546 O  "O3'" . IMP   B 2 .   ? 12.253  24.859  3.275   1.00 18.67 ?  801  IMP   A "O3'" 1 
HETATM 2547 C  "C2'" . IMP   B 2 .   ? 9.802   25.299  3.056   1.00 19.64 ?  801  IMP   A "C2'" 1 
HETATM 2548 O  "O2'" . IMP   B 2 .   ? 9.961   25.142  1.647   1.00 19.62 ?  801  IMP   A "O2'" 1 
HETATM 2549 C  "C1'" . IMP   B 2 .   ? 8.588   24.465  3.495   1.00 17.99 ?  801  IMP   A "C1'" 1 
HETATM 2550 N  N9    . IMP   B 2 .   ? 7.684   25.136  4.460   1.00 17.69 ?  801  IMP   A N9    1 
HETATM 2551 C  C8    . IMP   B 2 .   ? 8.033   25.934  5.521   1.00 19.14 ?  801  IMP   A C8    1 
HETATM 2552 N  N7    . IMP   B 2 .   ? 6.992   26.324  6.248   1.00 18.79 ?  801  IMP   A N7    1 
HETATM 2553 C  C5    . IMP   B 2 .   ? 5.898   25.740  5.622   1.00 17.32 ?  801  IMP   A C5    1 
HETATM 2554 C  C6    . IMP   B 2 .   ? 4.479   25.734  5.959   1.00 22.44 ?  801  IMP   A C6    1 
HETATM 2555 O  O6    . IMP   B 2 .   ? 3.938   26.220  6.954   1.00 20.61 ?  801  IMP   A O6    1 
HETATM 2556 N  N1    . IMP   B 2 .   ? 3.735   25.008  5.046   1.00 19.06 ?  801  IMP   A N1    1 
HETATM 2557 C  C2    . IMP   B 2 .   ? 4.248   24.356  3.979   1.00 21.75 ?  801  IMP   A C2    1 
HETATM 2558 N  N3    . IMP   B 2 .   ? 5.520   24.312  3.663   1.00 19.80 ?  801  IMP   A N3    1 
HETATM 2559 C  C4    . IMP   B 2 .   ? 6.307   25.020  4.511   1.00 21.47 ?  801  IMP   A C4    1 
HETATM 2560 C  C4    . A1A3K C 3 .   ? -0.256  30.720  2.299   1.00 21.49 ?  802  A1A3K A C4    1 
HETATM 2561 C  C5    . A1A3K C 3 .   ? -0.398  31.566  1.202   1.00 24.47 ?  802  A1A3K A C5    1 
HETATM 2562 C  C6    . A1A3K C 3 .   ? 0.090   32.874  1.282   1.00 28.94 ?  802  A1A3K A C6    1 
HETATM 2563 C  C8    . A1A3K C 3 .   ? 0.846   32.512  3.427   1.00 29.47 ?  802  A1A3K A C8    1 
HETATM 2564 C  C9    . A1A3K C 3 .   ? -1.082  31.106  -0.031  1.00 23.30 ?  802  A1A3K A C9    1 
HETATM 2565 C  C12   . A1A3K C 3 .   ? -2.298  29.935  -1.450  1.00 19.04 ?  802  A1A3K A C12   1 
HETATM 2566 C  C13   . A1A3K C 3 .   ? -1.791  31.030  -2.084  1.00 19.04 ?  802  A1A3K A C13   1 
HETATM 2567 C  C3    . A1A3K C 3 .   ? 0.380   31.211  3.425   1.00 24.20 ?  802  A1A3K A C3    1 
HETATM 2568 C  C1    . A1A3K C 3 .   ? -0.734  30.194  5.415   1.00 20.88 ?  802  A1A3K A C1    1 
HETATM 2569 C  C17   . A1A3K C 3 .   ? 2.375   28.953  3.842   1.00 22.09 ?  802  A1A3K A C17   1 
HETATM 2570 C  C18   . A1A3K C 3 .   ? 2.706   27.840  3.076   1.00 23.32 ?  802  A1A3K A C18   1 
HETATM 2571 C  C19   . A1A3K C 3 .   ? 3.997   27.679  2.598   1.00 29.73 ?  802  A1A3K A C19   1 
HETATM 2572 C  C2    . A1A3K C 3 .   ? 0.587   30.377  4.654   1.00 19.88 ?  802  A1A3K A C2    1 
HETATM 2573 C  C20   . A1A3K C 3 .   ? 4.960   28.632  2.868   1.00 25.87 ?  802  A1A3K A C20   1 
HETATM 2574 C  C21   . A1A3K C 3 .   ? 4.651   29.758  3.634   1.00 24.90 ?  802  A1A3K A C21   1 
HETATM 2575 C  C22   . A1A3K C 3 .   ? 3.348   29.912  4.108   1.00 26.12 ?  802  A1A3K A C22   1 
HETATM 2576 C  C23   . A1A3K C 3 .   ? 5.650   30.818  3.938   1.00 25.38 ?  802  A1A3K A C23   1 
HETATM 2577 C  C24   . A1A3K C 3 .   ? 5.444   31.915  4.724   1.00 26.41 ?  802  A1A3K A C24   1 
HETATM 2578 C  C25   . A1A3K C 3 .   ? 6.627   32.669  4.749   1.00 35.03 ?  802  A1A3K A C25   1 
HETATM 2579 N  N10   . A1A3K C 3 .   ? -1.848  29.971  -0.147  1.00 18.76 ?  802  A1A3K A N10   1 
HETATM 2580 N  N14   . A1A3K C 3 .   ? -1.063  31.728  -1.198  1.00 22.34 ?  802  A1A3K A N14   1 
HETATM 2581 N  N26   . A1A3K C 3 .   ? 7.520   32.058  4.009   1.00 33.45 ?  802  A1A3K A N26   1 
HETATM 2582 N  N27   . A1A3K C 3 .   ? 6.934   30.895  3.478   1.00 35.57 ?  802  A1A3K A N27   1 
HETATM 2583 N  N7    . A1A3K C 3 .   ? 0.693   33.304  2.375   1.00 32.14 ?  802  A1A3K A N7    1 
HETATM 2584 O  O16   . A1A3K C 3 .   ? 1.099   29.078  4.336   1.00 21.33 ?  802  A1A3K A O16   1 
HETATM 2585 CL CL15  . A1A3K C 3 .   ? -2.046  31.445  -3.755  1.00 21.71 ?  802  A1A3K A CL15  1 
HETATM 2586 H  H33   . A1A3K C 3 .   ? -0.631  29.707  2.272   1.00 25.87 ?  802  A1A3K A H33   1 
HETATM 2587 H  H34   . A1A3K C 3 .   ? -0.029  33.540  0.440   1.00 34.81 ?  802  A1A3K A H34   1 
HETATM 2588 H  H35   . A1A3K C 3 .   ? 1.347   32.892  4.306   1.00 35.45 ?  802  A1A3K A H35   1 
HETATM 2589 H  H36   . A1A3K C 3 .   ? -2.934  29.179  -1.887  1.00 22.94 ?  802  A1A3K A H36   1 
HETATM 2590 H  H30   . A1A3K C 3 .   ? -1.073  31.159  5.793   1.00 25.14 ?  802  A1A3K A H30   1 
HETATM 2591 H  H29   . A1A3K C 3 .   ? -0.581  29.511  6.250   1.00 25.14 ?  802  A1A3K A H29   1 
HETATM 2592 H  H31   . A1A3K C 3 .   ? -1.487  29.784  4.742   1.00 25.14 ?  802  A1A3K A H31   1 
HETATM 2593 H  H37   . A1A3K C 3 .   ? 1.953   27.098  2.854   1.00 28.07 ?  802  A1A3K A H37   1 
HETATM 2594 H  H38   . A1A3K C 3 .   ? 4.251   26.807  2.013   1.00 35.77 ?  802  A1A3K A H38   1 
HETATM 2595 H  H32   . A1A3K C 3 .   ? 1.311   30.909  5.272   1.00 23.93 ?  802  A1A3K A H32   1 
HETATM 2596 H  H39   . A1A3K C 3 .   ? 5.961   28.505  2.484   1.00 31.13 ?  802  A1A3K A H39   1 
HETATM 2597 H  H40   . A1A3K C 3 .   ? 3.091   30.786  4.689   1.00 31.43 ?  802  A1A3K A H40   1 
HETATM 2598 H  H41   . A1A3K C 3 .   ? 4.527   32.160  5.240   1.00 31.77 ?  802  A1A3K A H41   1 
HETATM 2599 H  H42   . A1A3K C 3 .   ? 6.776   33.595  5.286   1.00 42.12 ?  802  A1A3K A H42   1 
HETATM 2600 H  H11   . A1A3K C 3 .   ? -2.036  29.324  0.551   1.00 22.60 ?  802  A1A3K A H11   1 
HETATM 2601 H  H28   . A1A3K C 3 .   ? 7.366   30.258  2.887   1.00 42.77 ?  802  A1A3K A H28   1 
HETATM 2602 O  O     . HOH   D 4 .   ? 20.580  18.509  -14.146 1.00 33.75 ?  901  HOH   A O     1 
HETATM 2603 O  O     . HOH   D 4 .   ? 10.229  18.670  28.869  1.00 51.35 ?  902  HOH   A O     1 
HETATM 2604 O  O     . HOH   D 4 .   ? 21.381  35.546  15.089  1.00 46.23 ?  903  HOH   A O     1 
HETATM 2605 O  O     . HOH   D 4 .   ? 13.324  24.230  27.088  1.00 60.16 ?  904  HOH   A O     1 
HETATM 2606 O  O     . HOH   D 4 .   ? 11.509  13.767  31.697  1.00 65.76 ?  905  HOH   A O     1 
HETATM 2607 O  O     . HOH   D 4 .   ? 22.282  4.718   -10.828 1.00 29.17 ?  906  HOH   A O     1 
HETATM 2608 O  O     . HOH   D 4 .   ? 13.793  25.748  18.507  1.00 50.58 ?  907  HOH   A O     1 
HETATM 2609 O  O     . HOH   D 4 .   ? 11.765  6.234   3.419   1.00 55.26 ?  908  HOH   A O     1 
HETATM 2610 O  O     . HOH   D 4 .   ? 6.752   0.684   2.859   1.00 69.80 ?  909  HOH   A O     1 
HETATM 2611 O  O     . HOH   D 4 .   ? 33.541  18.675  -9.335  1.00 36.78 ?  910  HOH   A O     1 
HETATM 2612 O  O     . HOH   D 4 .   ? 4.869   27.800  17.934  1.00 44.08 ?  911  HOH   A O     1 
HETATM 2613 O  O     . HOH   D 4 .   ? 23.520  47.379  7.802   1.00 54.59 ?  912  HOH   A O     1 
HETATM 2614 O  O     . HOH   D 4 .   ? 22.009  20.552  -15.685 1.00 52.53 ?  913  HOH   A O     1 
HETATM 2615 O  O     . HOH   D 4 .   ? 1.097   24.842  -15.346 1.00 38.37 ?  914  HOH   A O     1 
HETATM 2616 O  O     . HOH   D 4 .   ? 12.030  14.568  8.670   1.00 38.52 ?  915  HOH   A O     1 
HETATM 2617 O  O     . HOH   D 4 .   ? -0.537  25.147  15.327  1.00 49.85 ?  916  HOH   A O     1 
HETATM 2618 O  O     . HOH   D 4 .   ? 16.451  -1.603  3.719   1.00 48.44 ?  917  HOH   A O     1 
HETATM 2619 O  O     . HOH   D 4 .   ? 13.346  24.618  21.091  1.00 40.74 ?  918  HOH   A O     1 
HETATM 2620 O  O     . HOH   D 4 .   ? 11.794  9.886   2.628   1.00 35.21 ?  919  HOH   A O     1 
HETATM 2621 O  O     . HOH   D 4 .   ? 25.052  16.963  -15.579 1.00 43.23 ?  920  HOH   A O     1 
HETATM 2622 O  O     . HOH   D 4 .   ? 12.852  28.656  28.831  1.00 37.05 ?  921  HOH   A O     1 
HETATM 2623 O  O     . HOH   D 4 .   ? 28.900  22.604  14.583  1.00 34.65 ?  922  HOH   A O     1 
HETATM 2624 O  O     . HOH   D 4 .   ? 15.914  42.163  -15.291 1.00 43.94 ?  923  HOH   A O     1 
HETATM 2625 O  O     . HOH   D 4 .   ? 31.688  33.234  -9.557  1.00 46.71 ?  924  HOH   A O     1 
HETATM 2626 O  O     . HOH   D 4 .   ? 6.071   3.186   -6.834  1.00 29.03 ?  925  HOH   A O     1 
HETATM 2627 O  O     . HOH   D 4 .   ? 12.877  -9.226  1.840   1.00 36.06 ?  926  HOH   A O     1 
HETATM 2628 O  O     . HOH   D 4 .   ? 14.782  23.847  16.124  1.00 35.55 ?  927  HOH   A O     1 
HETATM 2629 O  O     . HOH   D 4 .   ? 16.124  -3.338  5.852   1.00 60.49 ?  928  HOH   A O     1 
HETATM 2630 O  O     . HOH   D 4 .   ? 10.289  31.433  5.178   1.00 37.27 ?  929  HOH   A O     1 
HETATM 2631 O  O     . HOH   D 4 .   ? -16.167 0.273   -27.501 1.00 57.96 ?  930  HOH   A O     1 
HETATM 2632 O  O     . HOH   D 4 .   ? 22.230  46.288  -12.051 1.00 50.42 ?  931  HOH   A O     1 
HETATM 2633 O  O     . HOH   D 4 .   ? 38.694  6.306   -7.077  1.00 33.87 ?  932  HOH   A O     1 
HETATM 2634 O  O     . HOH   D 4 .   ? 20.761  9.330   -17.653 1.00 37.61 ?  933  HOH   A O     1 
HETATM 2635 O  O     . HOH   D 4 .   ? 24.178  35.643  -12.305 1.00 30.67 ?  934  HOH   A O     1 
HETATM 2636 O  O     . HOH   D 4 .   ? -17.149 7.404   -23.355 1.00 40.75 ?  935  HOH   A O     1 
HETATM 2637 O  O     . HOH   D 4 .   ? 36.178  20.590  -7.466  1.00 40.81 ?  936  HOH   A O     1 
HETATM 2638 O  O     . HOH   D 4 .   ? 20.119  35.769  -14.252 1.00 30.37 ?  937  HOH   A O     1 
HETATM 2639 O  O     . HOH   D 4 .   ? -7.629  16.665  -23.326 1.00 46.39 ?  938  HOH   A O     1 
HETATM 2640 O  O     . HOH   D 4 .   ? 32.253  18.988  -12.717 1.00 40.29 ?  939  HOH   A O     1 
HETATM 2641 O  O     . HOH   D 4 .   ? 27.657  23.338  18.164  1.00 39.86 ?  940  HOH   A O     1 
HETATM 2642 O  O     . HOH   D 4 .   ? 26.509  21.606  -10.168 1.00 24.96 ?  941  HOH   A O     1 
HETATM 2643 O  O     . HOH   D 4 .   ? 31.177  17.780  -8.100  1.00 19.94 ?  942  HOH   A O     1 
HETATM 2644 O  O     . HOH   D 4 .   ? 36.655  17.102  -9.700  1.00 37.54 ?  943  HOH   A O     1 
HETATM 2645 O  O     . HOH   D 4 .   ? 13.293  7.705   0.242   1.00 22.65 ?  944  HOH   A O     1 
HETATM 2646 O  O     . HOH   D 4 .   ? 9.929   29.809  -0.654  1.00 24.60 ?  945  HOH   A O     1 
HETATM 2647 O  O     . HOH   D 4 .   ? 32.422  13.981  3.243   1.00 47.92 ?  946  HOH   A O     1 
HETATM 2648 O  O     . HOH   D 4 .   ? 10.077  27.849  11.886  1.00 23.12 ?  947  HOH   A O     1 
HETATM 2649 O  O     . HOH   D 4 .   ? 22.428  30.563  -18.334 1.00 36.84 ?  948  HOH   A O     1 
HETATM 2650 O  O     . HOH   D 4 .   ? 22.696  2.854   -14.789 1.00 22.74 ?  949  HOH   A O     1 
HETATM 2651 O  O     . HOH   D 4 .   ? 11.580  15.976  5.792   1.00 23.89 ?  950  HOH   A O     1 
HETATM 2652 O  O     . HOH   D 4 .   ? 25.468  38.567  -9.337  1.00 30.54 ?  951  HOH   A O     1 
HETATM 2653 O  O     . HOH   D 4 .   ? 13.181  2.573   0.482   1.00 52.85 ?  952  HOH   A O     1 
HETATM 2654 O  O     . HOH   D 4 .   ? 5.084   19.982  -15.275 1.00 20.71 ?  953  HOH   A O     1 
HETATM 2655 O  O     . HOH   D 4 .   ? 32.702  16.796  0.792   1.00 44.42 ?  954  HOH   A O     1 
HETATM 2656 O  O     . HOH   D 4 .   ? 3.610   9.307   -4.975  1.00 24.40 ?  955  HOH   A O     1 
HETATM 2657 O  O     . HOH   D 4 .   ? -9.570  10.250  -15.391 1.00 19.02 ?  956  HOH   A O     1 
HETATM 2658 O  O     . HOH   D 4 .   ? 14.732  19.595  -21.442 1.00 36.60 ?  957  HOH   A O     1 
HETATM 2659 O  O     . HOH   D 4 .   ? -17.247 13.843  -21.442 1.00 44.67 ?  958  HOH   A O     1 
HETATM 2660 O  O     . HOH   D 4 .   ? 14.546  15.699  12.633  1.00 43.96 ?  959  HOH   A O     1 
HETATM 2661 O  O     . HOH   D 4 .   ? 6.812   19.666  -5.008  1.00 17.09 ?  960  HOH   A O     1 
HETATM 2662 O  O     . HOH   D 4 .   ? 25.636  30.900  5.467   1.00 21.25 ?  961  HOH   A O     1 
HETATM 2663 O  O     . HOH   D 4 .   ? 20.047  21.769  -11.502 1.00 18.78 ?  962  HOH   A O     1 
HETATM 2664 O  O     . HOH   D 4 .   ? -12.173 17.464  -18.413 1.00 27.06 ?  963  HOH   A O     1 
HETATM 2665 O  O     . HOH   D 4 .   ? 23.034  0.207   -13.835 1.00 21.75 ?  964  HOH   A O     1 
HETATM 2666 O  O     . HOH   D 4 .   ? -12.377 2.337   -20.830 1.00 43.90 ?  965  HOH   A O     1 
HETATM 2667 O  O     . HOH   D 4 .   ? 25.600  15.726  15.776  1.00 41.21 ?  966  HOH   A O     1 
HETATM 2668 O  O     . HOH   D 4 .   ? 7.762   14.737  0.751   1.00 41.59 ?  967  HOH   A O     1 
HETATM 2669 O  O     . HOH   D 4 .   ? 4.180   27.622  -7.779  1.00 23.65 ?  968  HOH   A O     1 
HETATM 2670 O  O     . HOH   D 4 .   ? 29.280  36.857  -3.442  1.00 38.79 ?  969  HOH   A O     1 
HETATM 2671 O  O     . HOH   D 4 .   ? 20.218  34.448  16.965  1.00 47.68 ?  970  HOH   A O     1 
HETATM 2672 O  O     . HOH   D 4 .   ? -4.819  15.413  0.428   1.00 24.43 ?  971  HOH   A O     1 
HETATM 2673 O  O     . HOH   D 4 .   ? 24.404  20.662  -14.079 1.00 38.79 ?  972  HOH   A O     1 
HETATM 2674 O  O     . HOH   D 4 .   ? 17.835  0.279   4.278   1.00 41.96 ?  973  HOH   A O     1 
HETATM 2675 O  O     . HOH   D 4 .   ? 30.510  27.585  2.271   1.00 23.97 ?  974  HOH   A O     1 
HETATM 2676 O  O     . HOH   D 4 .   ? 31.581  19.477  6.001   1.00 36.00 ?  975  HOH   A O     1 
HETATM 2677 O  O     . HOH   D 4 .   ? 32.407  28.162  -2.085  1.00 41.96 ?  976  HOH   A O     1 
HETATM 2678 O  O     . HOH   D 4 .   ? 23.217  2.880   9.306   1.00 31.49 ?  977  HOH   A O     1 
HETATM 2679 O  O     . HOH   D 4 .   ? 4.886   18.641  -18.997 1.00 31.60 ?  978  HOH   A O     1 
HETATM 2680 O  O     . HOH   D 4 .   ? -5.624  7.951   -15.600 1.00 27.74 ?  979  HOH   A O     1 
HETATM 2681 O  O     . HOH   D 4 .   ? 12.741  29.705  1.338   1.00 23.82 ?  980  HOH   A O     1 
HETATM 2682 O  O     . HOH   D 4 .   ? 24.052  38.632  -12.921 1.00 49.58 ?  981  HOH   A O     1 
HETATM 2683 O  O     . HOH   D 4 .   ? 13.619  47.506  11.254  1.00 35.19 ?  982  HOH   A O     1 
HETATM 2684 O  O     . HOH   D 4 .   ? 13.901  18.907  2.815   1.00 20.79 ?  983  HOH   A O     1 
HETATM 2685 O  O     . HOH   D 4 .   ? 22.708  23.151  -17.650 1.00 43.80 ?  984  HOH   A O     1 
HETATM 2686 O  O     . HOH   D 4 .   ? 1.617   28.971  19.251  1.00 54.78 ?  985  HOH   A O     1 
HETATM 2687 O  O     . HOH   D 4 .   ? 12.147  29.619  -20.022 1.00 42.32 ?  986  HOH   A O     1 
HETATM 2688 O  O     . HOH   D 4 .   ? -11.697 12.670  -17.699 1.00 21.72 ?  987  HOH   A O     1 
HETATM 2689 O  O     . HOH   D 4 .   ? 5.886   43.534  0.971   1.00 34.38 ?  988  HOH   A O     1 
HETATM 2690 O  O     . HOH   D 4 .   ? 8.849   22.844  0.290   1.00 19.73 ?  989  HOH   A O     1 
HETATM 2691 O  O     . HOH   D 4 .   ? 30.548  23.982  10.914  1.00 37.22 ?  990  HOH   A O     1 
HETATM 2692 O  O     . HOH   D 4 .   ? 26.812  37.460  -4.781  1.00 30.11 ?  991  HOH   A O     1 
HETATM 2693 O  O     . HOH   D 4 .   ? 13.589  18.260  -1.860  1.00 28.25 ?  992  HOH   A O     1 
HETATM 2694 O  O     . HOH   D 4 .   ? 11.788  33.271  5.899   1.00 33.92 ?  993  HOH   A O     1 
HETATM 2695 O  O     . HOH   D 4 .   ? 25.901  8.590   -13.248 1.00 30.43 ?  994  HOH   A O     1 
HETATM 2696 O  O     . HOH   D 4 .   ? 5.856   29.388  -18.657 1.00 27.94 ?  995  HOH   A O     1 
HETATM 2697 O  O     . HOH   D 4 .   ? 6.918   14.309  -2.054  1.00 23.17 ?  996  HOH   A O     1 
HETATM 2698 O  O     . HOH   D 4 .   ? 12.324  22.945  -21.851 1.00 43.18 ?  997  HOH   A O     1 
HETATM 2699 O  O     . HOH   D 4 .   ? -7.777  11.687  -17.116 1.00 19.73 ?  998  HOH   A O     1 
HETATM 2700 O  O     . HOH   D 4 .   ? 2.473   25.788  -11.786 1.00 19.55 ?  999  HOH   A O     1 
HETATM 2701 O  O     . HOH   D 4 .   ? 25.949  -2.951  -0.740  1.00 31.47 ?  1000 HOH   A O     1 
HETATM 2702 O  O     . HOH   D 4 .   ? -4.340  29.598  3.602   1.00 21.81 ?  1001 HOH   A O     1 
HETATM 2703 O  O     . HOH   D 4 .   ? 24.464  22.871  -12.082 1.00 33.44 ?  1002 HOH   A O     1 
HETATM 2704 O  O     . HOH   D 4 .   ? 19.816  22.778  -14.029 1.00 25.11 ?  1003 HOH   A O     1 
HETATM 2705 O  O     . HOH   D 4 .   ? 8.399   35.323  -17.085 1.00 33.12 ?  1004 HOH   A O     1 
HETATM 2706 O  O     . HOH   D 4 .   ? 29.035  26.373  15.558  1.00 40.31 ?  1005 HOH   A O     1 
HETATM 2707 O  O     . HOH   D 4 .   ? 34.081  19.646  -1.745  1.00 30.20 ?  1006 HOH   A O     1 
HETATM 2708 O  O     . HOH   D 4 .   ? 36.293  12.738  -8.059  1.00 33.31 ?  1007 HOH   A O     1 
HETATM 2709 O  O     . HOH   D 4 .   ? 17.390  33.059  -15.884 1.00 24.78 ?  1008 HOH   A O     1 
HETATM 2710 O  O     . HOH   D 4 .   ? 5.816   42.757  -7.445  1.00 37.45 ?  1009 HOH   A O     1 
HETATM 2711 O  O     . HOH   D 4 .   ? 21.367  24.903  -6.817  1.00 19.31 ?  1010 HOH   A O     1 
HETATM 2712 O  O     . HOH   D 4 .   ? 14.376  16.185  -16.593 1.00 26.17 ?  1011 HOH   A O     1 
HETATM 2713 O  O     . HOH   D 4 .   ? 20.759  30.038  14.359  1.00 25.47 ?  1012 HOH   A O     1 
HETATM 2714 O  O     . HOH   D 4 .   ? -7.699  18.730  -18.690 1.00 30.25 ?  1013 HOH   A O     1 
HETATM 2715 O  O     . HOH   D 4 .   ? -1.098  25.811  12.703  1.00 32.69 ?  1014 HOH   A O     1 
HETATM 2716 O  O     . HOH   D 4 .   ? 8.869   29.069  2.383   1.00 38.28 ?  1015 HOH   A O     1 
HETATM 2717 O  O     . HOH   D 4 .   ? 14.917  17.928  6.252   1.00 22.66 ?  1016 HOH   A O     1 
HETATM 2718 O  O     . HOH   D 4 .   ? 5.040   17.987  -11.197 1.00 25.50 ?  1017 HOH   A O     1 
HETATM 2719 O  O     . HOH   D 4 .   ? 4.242   25.541  -9.545  1.00 18.36 ?  1018 HOH   A O     1 
HETATM 2720 O  O     . HOH   D 4 .   ? 13.663  32.588  16.191  1.00 34.54 ?  1019 HOH   A O     1 
HETATM 2721 O  O     . HOH   D 4 .   ? 37.912  13.870  -1.050  1.00 41.87 ?  1020 HOH   A O     1 
HETATM 2722 O  O     . HOH   D 4 .   ? 9.561   6.960   4.921   1.00 49.37 ?  1021 HOH   A O     1 
HETATM 2723 O  O     . HOH   D 4 .   ? 24.045  8.837   6.695   1.00 32.19 ?  1022 HOH   A O     1 
HETATM 2724 O  O     . HOH   D 4 .   ? 15.048  26.193  -21.351 1.00 43.99 ?  1023 HOH   A O     1 
HETATM 2725 O  O     . HOH   D 4 .   ? 29.231  4.142   -15.220 1.00 33.08 ?  1024 HOH   A O     1 
HETATM 2726 O  O     . HOH   D 4 .   ? 25.298  5.966   -13.059 1.00 23.39 ?  1025 HOH   A O     1 
HETATM 2727 O  O     . HOH   D 4 .   ? 25.634  42.827  -1.076  1.00 31.90 ?  1026 HOH   A O     1 
HETATM 2728 O  O     . HOH   D 4 .   ? 3.509   30.495  -17.457 1.00 32.59 ?  1027 HOH   A O     1 
HETATM 2729 O  O     . HOH   D 4 .   ? 4.013   23.582  0.311   1.00 31.29 ?  1028 HOH   A O     1 
HETATM 2730 O  O     . HOH   D 4 .   ? 20.326  9.781   7.230   1.00 31.44 ?  1029 HOH   A O     1 
HETATM 2731 O  O     . HOH   D 4 .   ? 19.457  15.467  -15.008 1.00 29.58 ?  1030 HOH   A O     1 
HETATM 2732 O  O     . HOH   D 4 .   ? 29.083  6.902   -14.595 1.00 42.34 ?  1031 HOH   A O     1 
HETATM 2733 O  O     . HOH   D 4 .   ? 11.980  30.540  -2.840  1.00 23.07 ?  1032 HOH   A O     1 
HETATM 2734 O  O     . HOH   D 4 .   ? 30.615  6.840   3.147   1.00 24.24 ?  1033 HOH   A O     1 
HETATM 2735 O  O     . HOH   D 4 .   ? -15.358 14.081  -19.269 1.00 31.34 ?  1034 HOH   A O     1 
HETATM 2736 O  O     . HOH   D 4 .   ? 16.884  7.372   1.039   1.00 25.72 ?  1035 HOH   A O     1 
HETATM 2737 O  O     . HOH   D 4 .   ? 16.595  14.915  -15.090 1.00 25.06 ?  1036 HOH   A O     1 
HETATM 2738 O  O     . HOH   D 4 .   ? 12.666  3.688   -1.739  1.00 34.55 ?  1037 HOH   A O     1 
HETATM 2739 O  O     . HOH   D 4 .   ? 3.052   32.806  6.522   1.00 32.41 ?  1038 HOH   A O     1 
HETATM 2740 O  O     . HOH   D 4 .   ? 0.034   22.402  14.905  1.00 45.61 ?  1039 HOH   A O     1 
HETATM 2741 O  O     . HOH   D 4 .   ? 28.179  28.847  14.662  1.00 32.42 ?  1040 HOH   A O     1 
HETATM 2742 O  O     . HOH   D 4 .   ? -11.946 19.658  -16.901 1.00 27.26 ?  1041 HOH   A O     1 
HETATM 2743 O  O     . HOH   D 4 .   ? 31.762  30.256  -6.455  1.00 33.43 ?  1042 HOH   A O     1 
HETATM 2744 O  O     . HOH   D 4 .   ? 21.984  28.549  18.997  1.00 48.67 ?  1043 HOH   A O     1 
HETATM 2745 O  O     . HOH   D 4 .   ? 6.475   21.941  1.470   1.00 24.52 ?  1044 HOH   A O     1 
HETATM 2746 O  O     . HOH   D 4 .   ? 33.436  1.451   -6.808  1.00 24.97 ?  1045 HOH   A O     1 
HETATM 2747 O  O     . HOH   D 4 .   ? 2.726   17.795  8.380   1.00 44.78 ?  1046 HOH   A O     1 
HETATM 2748 O  O     . HOH   D 4 .   ? 31.231  17.188  5.132   1.00 40.13 ?  1047 HOH   A O     1 
HETATM 2749 O  O     . HOH   D 4 .   ? 17.007  36.403  10.275  1.00 35.51 ?  1048 HOH   A O     1 
HETATM 2750 O  O     . HOH   D 4 .   ? 12.688  27.804  3.556   1.00 19.96 ?  1049 HOH   A O     1 
HETATM 2751 O  O     . HOH   D 4 .   ? 21.776  47.672  6.187   1.00 35.94 ?  1050 HOH   A O     1 
HETATM 2752 O  O     . HOH   D 4 .   ? 0.955   33.707  -5.112  1.00 29.88 ?  1051 HOH   A O     1 
HETATM 2753 O  O     . HOH   D 4 .   ? 8.833   49.493  4.552   1.00 46.27 ?  1052 HOH   A O     1 
HETATM 2754 O  O     . HOH   D 4 .   ? 9.177   9.975   0.104   1.00 26.33 ?  1053 HOH   A O     1 
HETATM 2755 O  O     . HOH   D 4 .   ? 5.556   33.700  8.913   1.00 36.46 ?  1054 HOH   A O     1 
HETATM 2756 O  O     . HOH   D 4 .   ? -5.505  10.143  -17.319 1.00 26.00 ?  1055 HOH   A O     1 
HETATM 2757 O  O     . HOH   D 4 .   ? 3.602   33.522  -0.181  1.00 32.20 ?  1056 HOH   A O     1 
HETATM 2758 O  O     . HOH   D 4 .   ? 34.488  16.998  -2.255  1.00 29.77 ?  1057 HOH   A O     1 
HETATM 2759 O  O     . HOH   D 4 .   ? 7.275   31.704  -19.441 1.00 39.27 ?  1058 HOH   A O     1 
HETATM 2760 O  O     . HOH   D 4 .   ? 8.969   39.325  5.796   1.00 24.37 ?  1059 HOH   A O     1 
HETATM 2761 O  O     . HOH   D 4 .   ? 17.100  17.146  13.357  1.00 41.88 ?  1060 HOH   A O     1 
HETATM 2762 O  O     . HOH   D 4 .   ? 9.536   40.576  3.220   1.00 24.22 ?  1061 HOH   A O     1 
HETATM 2763 O  O     . HOH   D 4 .   ? 10.650  45.937  9.897   1.00 42.01 ?  1062 HOH   A O     1 
HETATM 2764 O  O     . HOH   D 4 .   ? 19.569  14.772  11.211  1.00 40.53 ?  1063 HOH   A O     1 
HETATM 2765 O  O     . HOH   D 4 .   ? 3.755   16.388  3.221   1.00 48.84 ?  1064 HOH   A O     1 
HETATM 2766 O  O     . HOH   D 4 .   ? 3.176   46.742  -1.273  1.00 41.74 ?  1065 HOH   A O     1 
HETATM 2767 O  O     . HOH   D 4 .   ? 5.574   26.098  -1.540  1.00 36.37 ?  1066 HOH   A O     1 
HETATM 2768 O  O     . HOH   D 4 .   ? 36.521  9.653   -7.998  1.00 40.05 ?  1067 HOH   A O     1 
HETATM 2769 O  O     . HOH   D 4 .   ? 4.729   37.201  2.362   1.00 50.88 ?  1068 HOH   A O     1 
HETATM 2770 O  O     . HOH   D 4 .   ? 17.805  30.905  20.357  1.00 56.81 ?  1069 HOH   A O     1 
HETATM 2771 O  O     . HOH   D 4 .   ? 23.384  12.405  12.357  1.00 47.79 ?  1070 HOH   A O     1 
HETATM 2772 O  O     . HOH   D 4 .   ? 19.107  31.866  -18.239 1.00 43.15 ?  1071 HOH   A O     1 
HETATM 2773 O  O     . HOH   D 4 .   ? 26.077  34.208  16.286  1.00 42.89 ?  1072 HOH   A O     1 
HETATM 2774 O  O     . HOH   D 4 .   ? 14.165  36.494  16.206  1.00 49.96 ?  1073 HOH   A O     1 
HETATM 2775 O  O     . HOH   D 4 .   ? 14.688  51.944  -4.031  1.00 34.74 ?  1074 HOH   A O     1 
HETATM 2776 O  O     . HOH   D 4 .   ? 31.687  12.638  5.240   1.00 39.25 ?  1075 HOH   A O     1 
HETATM 2777 O  O     . HOH   D 4 .   ? 4.958   38.636  0.543   1.00 36.86 ?  1076 HOH   A O     1 
HETATM 2778 O  O     . HOH   D 4 .   ? 22.865  4.556   -12.555 1.00 25.29 ?  1077 HOH   A O     1 
HETATM 2779 O  O     . HOH   D 4 .   ? 18.618  25.197  26.348  1.00 48.16 ?  1078 HOH   A O     1 
HETATM 2780 O  O     . HOH   D 4 .   ? 4.537   15.656  -9.144  1.00 23.90 ?  1079 HOH   A O     1 
HETATM 2781 O  O     . HOH   D 4 .   ? 10.452  33.547  7.399   1.00 35.80 ?  1080 HOH   A O     1 
HETATM 2782 O  O     . HOH   D 4 .   ? 34.909  1.512   -5.293  1.00 51.59 ?  1081 HOH   A O     1 
HETATM 2783 O  O     . HOH   D 4 .   ? 23.857  6.691   -16.876 1.00 45.81 ?  1082 HOH   A O     1 
HETATM 2784 O  O     . HOH   D 4 .   ? -1.100  34.764  -1.732  1.00 39.21 ?  1083 HOH   A O     1 
HETATM 2785 O  O     . HOH   D 4 .   ? 3.828   22.407  -16.656 1.00 23.72 ?  1084 HOH   A O     1 
HETATM 2786 O  O     . HOH   D 4 .   ? 7.389   2.661   -1.844  1.00 41.34 ?  1085 HOH   A O     1 
HETATM 2787 O  O     . HOH   D 4 .   ? 27.149  0.394   -15.877 1.00 30.29 ?  1086 HOH   A O     1 
HETATM 2788 O  O     . HOH   D 4 .   ? 31.844  26.387  -0.050  1.00 26.27 ?  1087 HOH   A O     1 
HETATM 2789 O  O     . HOH   D 4 .   ? 24.120  47.320  -7.705  1.00 53.71 ?  1088 HOH   A O     1 
HETATM 2790 O  O     . HOH   D 4 .   ? 9.079   43.415  5.295   1.00 34.94 ?  1089 HOH   A O     1 
HETATM 2791 O  O     . HOH   D 4 .   ? 12.571  16.913  32.491  1.00 51.15 ?  1090 HOH   A O     1 
HETATM 2792 O  O     . HOH   D 4 .   ? 33.529  5.751   -12.566 1.00 29.60 ?  1091 HOH   A O     1 
HETATM 2793 O  O     . HOH   D 4 .   ? 31.507  30.439  2.606   1.00 30.19 ?  1092 HOH   A O     1 
HETATM 2794 O  O     . HOH   D 4 .   ? 4.358   45.579  1.173   1.00 42.01 ?  1093 HOH   A O     1 
HETATM 2795 O  O     . HOH   D 4 .   ? -14.447 6.418   -30.571 1.00 69.78 ?  1094 HOH   A O     1 
HETATM 2796 O  O     . HOH   D 4 .   ? 31.133  21.982  16.062  1.00 41.05 ?  1095 HOH   A O     1 
HETATM 2797 O  O     . HOH   D 4 .   ? 38.522  2.100   -7.649  1.00 39.93 ?  1096 HOH   A O     1 
HETATM 2798 O  O     . HOH   D 4 .   ? 0.900   28.333  -17.936 1.00 38.92 ?  1097 HOH   A O     1 
HETATM 2799 O  O     . HOH   D 4 .   ? 1.929   2.432   -11.983 1.00 47.23 ?  1098 HOH   A O     1 
HETATM 2800 O  O     . HOH   D 4 .   ? 21.557  32.163  16.155  1.00 37.69 ?  1099 HOH   A O     1 
HETATM 2801 O  O     . HOH   D 4 .   ? 10.207  34.858  14.949  1.00 38.19 ?  1100 HOH   A O     1 
HETATM 2802 O  O     . HOH   D 4 .   ? 13.636  12.545  9.252   1.00 54.12 ?  1101 HOH   A O     1 
HETATM 2803 O  O     . HOH   D 4 .   ? 6.634   25.378  0.108   1.00 36.53 ?  1102 HOH   A O     1 
HETATM 2804 O  O     . HOH   D 4 .   ? 25.533  25.057  21.881  1.00 49.05 ?  1103 HOH   A O     1 
HETATM 2805 O  O     . HOH   D 4 .   ? 36.612  5.243   0.555   1.00 29.36 ?  1104 HOH   A O     1 
HETATM 2806 O  O     . HOH   D 4 .   ? 18.933  39.732  15.932  1.00 54.59 ?  1105 HOH   A O     1 
HETATM 2807 O  O     . HOH   D 4 .   ? 18.065  1.529   -19.590 1.00 37.72 ?  1106 HOH   A O     1 
HETATM 2808 O  O     . HOH   D 4 .   ? 9.946   21.794  -22.641 1.00 40.82 ?  1107 HOH   A O     1 
HETATM 2809 O  O     . HOH   D 4 .   ? 11.965  36.036  15.330  1.00 52.80 ?  1108 HOH   A O     1 
HETATM 2810 O  O     . HOH   D 4 .   ? 30.964  19.410  8.636   1.00 46.35 ?  1109 HOH   A O     1 
HETATM 2811 O  O     . HOH   D 4 .   ? 6.555   36.499  8.132   1.00 51.37 ?  1110 HOH   A O     1 
HETATM 2812 O  O     . HOH   D 4 .   ? 39.036  0.566   -9.807  1.00 41.72 ?  1111 HOH   A O     1 
HETATM 2813 O  O     . HOH   D 4 .   ? 5.100   39.133  2.914   1.00 42.71 ?  1112 HOH   A O     1 
HETATM 2814 O  O     . HOH   D 4 .   ? 13.816  -10.337 14.129  1.00 56.92 ?  1113 HOH   A O     1 
HETATM 2815 O  O     . HOH   D 4 .   ? 12.654  27.261  -20.227 1.00 39.38 ?  1114 HOH   A O     1 
HETATM 2816 O  O     . HOH   D 4 .   ? 3.666   11.677  -2.832  1.00 36.60 ?  1115 HOH   A O     1 
HETATM 2817 O  O     . HOH   D 4 .   ? 23.365  10.733  7.863   1.00 39.47 ?  1116 HOH   A O     1 
HETATM 2818 O  O     . HOH   D 4 .   ? 2.033   32.898  -2.316  1.00 33.53 ?  1117 HOH   A O     1 
HETATM 2819 O  O     . HOH   D 4 .   ? 31.040  29.379  -10.380 1.00 45.35 ?  1118 HOH   A O     1 
HETATM 2820 O  O     . HOH   D 4 .   ? 18.402  10.878  8.956   1.00 47.59 ?  1119 HOH   A O     1 
HETATM 2821 O  O     . HOH   D 4 .   ? 16.149  33.028  18.804  1.00 54.51 ?  1120 HOH   A O     1 
HETATM 2822 O  O     . HOH   D 4 .   ? 10.237  28.639  4.708   1.00 24.13 ?  1121 HOH   A O     1 
HETATM 2823 O  O     . HOH   D 4 .   ? 30.588  27.225  13.787  1.00 39.84 ?  1122 HOH   A O     1 
HETATM 2824 O  O     . HOH   D 4 .   ? 20.061  -0.180  -17.059 1.00 48.73 ?  1123 HOH   A O     1 
HETATM 2825 O  O     . HOH   D 4 .   ? 3.477   2.067   -6.149  1.00 41.20 ?  1124 HOH   A O     1 
HETATM 2826 O  O     . HOH   D 4 .   ? 11.197  30.579  17.530  1.00 51.04 ?  1125 HOH   A O     1 
HETATM 2827 O  O     . HOH   D 4 .   ? 7.825   27.730  0.460   1.00 42.32 ?  1126 HOH   A O     1 
HETATM 2828 O  O     . HOH   D 4 .   ? 16.551  15.182  13.913  1.00 47.58 ?  1127 HOH   A O     1 
HETATM 2829 O  O     . HOH   D 4 .   ? 7.017   41.839  2.862   1.00 42.71 ?  1128 HOH   A O     1 
HETATM 2830 O  O     . HOH   D 4 .   ? 24.253  20.620  -17.582 1.00 54.52 ?  1129 HOH   A O     1 
HETATM 2831 O  O     . HOH   D 4 .   ? 22.536  12.940  9.858   1.00 40.88 ?  1130 HOH   A O     1 
HETATM 2832 O  O     . HOH   D 4 .   ? 5.119   50.143  0.650   1.00 40.94 ?  1131 HOH   A O     1 
HETATM 2833 O  O     . HOH   D 4 .   ? 33.634  3.455   -15.002 1.00 48.17 ?  1132 HOH   A O     1 
HETATM 2834 O  O     . HOH   D 4 .   ? 19.451  9.834   28.174  1.00 41.05 ?  1133 HOH   A O     1 
HETATM 2835 O  O     . HOH   D 4 .   ? 6.799   24.780  -20.150 1.00 39.99 ?  1134 HOH   A O     1 
HETATM 2836 O  O     . HOH   D 4 .   ? 12.515  3.989   2.688   1.00 54.58 ?  1135 HOH   A O     1 
HETATM 2837 O  O     . HOH   D 4 .   ? 21.593  38.112  16.483  1.00 62.80 ?  1136 HOH   A O     1 
HETATM 2838 O  O     . HOH   D 4 .   ? -0.098  34.645  -14.544 1.00 50.91 ?  1137 HOH   A O     1 
HETATM 2839 O  O     . HOH   D 4 .   ? 23.458  24.371  -13.704 1.00 45.49 ?  1138 HOH   A O     1 
HETATM 2840 O  O     . HOH   D 4 .   ? 19.676  6.270   -20.819 1.00 44.73 ?  1139 HOH   A O     1 
HETATM 2841 O  O     . HOH   D 4 .   ? 3.698   43.803  -5.389  1.00 45.24 ?  1140 HOH   A O     1 
HETATM 2842 O  O     . HOH   D 4 .   ? 32.232  21.798  9.926   1.00 45.71 ?  1141 HOH   A O     1 
HETATM 2843 O  O     . HOH   D 4 .   ? 7.361   34.822  7.487   1.00 40.12 ?  1142 HOH   A O     1 
HETATM 2844 O  O     . HOH   D 4 .   ? 37.483  8.616   -10.171 1.00 50.75 ?  1143 HOH   A O     1 
HETATM 2845 O  O     . HOH   D 4 .   ? 3.184   -0.083  -12.866 1.00 54.29 ?  1144 HOH   A O     1 
HETATM 2846 O  O     . HOH   D 4 .   ? 30.334  24.674  12.960  1.00 47.27 ?  1145 HOH   A O     1 
HETATM 2847 O  O     . HOH   D 4 .   ? 17.015  17.598  -18.831 1.00 45.77 ?  1146 HOH   A O     1 
HETATM 2848 O  O     . HOH   D 4 .   ? 9.879   29.185  18.684  1.00 48.70 ?  1147 HOH   A O     1 
HETATM 2849 O  O     . HOH   D 4 .   ? 0.378   3.369   -7.039  1.00 41.31 ?  1148 HOH   A O     1 
HETATM 2850 O  O     . HOH   D 4 .   ? 2.285   38.072  -4.233  1.00 39.04 ?  1149 HOH   A O     1 
HETATM 2851 O  O     . HOH   D 4 .   ? 27.176  8.072   -16.346 1.00 49.30 ?  1150 HOH   A O     1 
HETATM 2852 O  O     . HOH   D 4 .   ? 32.744  8.606   2.868   1.00 36.01 ?  1151 HOH   A O     1 
HETATM 2853 O  O     . HOH   D 4 .   ? 36.263  14.006  3.487   1.00 52.55 ?  1152 HOH   A O     1 
HETATM 2854 O  O     . HOH   D 4 .   ? 22.268  23.140  -15.106 1.00 41.44 ?  1153 HOH   A O     1 
HETATM 2855 O  O     . HOH   D 4 .   ? 28.366  30.497  23.201  1.00 41.94 ?  1154 HOH   A O     1 
HETATM 2856 O  O     . HOH   D 4 .   ? 3.523   18.550  -13.574 1.00 31.92 ?  1155 HOH   A O     1 
HETATM 2857 O  O     . HOH   D 4 .   ? 3.971   21.643  -19.074 1.00 42.95 ?  1156 HOH   A O     1 
HETATM 2858 O  O     . HOH   D 4 .   ? 24.816  4.526   -15.456 1.00 38.20 ?  1157 HOH   A O     1 
HETATM 2859 O  O     . HOH   D 4 .   ? 27.321  3.381   -16.645 1.00 35.94 ?  1158 HOH   A O     1 
HETATM 2860 O  O     . HOH   D 4 .   ? -12.911 15.278  -16.871 1.00 25.76 ?  1159 HOH   A O     1 
HETATM 2861 O  O     . HOH   D 4 .   ? 15.596  28.752  -22.278 1.00 42.86 ?  1160 HOH   A O     1 
HETATM 2862 O  O     . HOH   D 4 .   ? 9.835   24.436  -20.802 1.00 44.66 ?  1161 HOH   A O     1 
HETATM 2863 O  O     . HOH   D 4 .   ? 1.383   21.262  -15.214 1.00 32.40 ?  1162 HOH   A O     1 
HETATM 2864 O  O     . HOH   D 4 .   ? 30.522  21.937  18.298  1.00 43.02 ?  1163 HOH   A O     1 
HETATM 2865 O  O     . HOH   D 4 .   ? 36.411  2.447   0.035   1.00 37.32 ?  1164 HOH   A O     1 
HETATM 2866 O  O     . HOH   D 4 .   ? 20.359  12.848  10.466  1.00 49.71 ?  1165 HOH   A O     1 
HETATM 2867 O  O     . HOH   D 4 .   ? 2.390   40.421  2.893   1.00 57.33 ?  1166 HOH   A O     1 
HETATM 2868 O  O     . HOH   D 4 .   ? 10.839  49.143  7.208   1.00 57.31 ?  1167 HOH   A O     1 
# 
