data_9FO1
# 
_entry.id   9FO1 
# 
_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   9FO1         pdb_00009fo1 10.2210/pdb9fo1/pdb 
WWPDB D_1292139297 ?            ?                   
# 
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 2025-01-22 
2 'Structure model' 1 1 2025-02-05 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FO1 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              nanna.rhein-knudsen@sb-roscoff.fr 
_pdbx_contact_author.name_first         Nanna 
_pdbx_contact_author.name_last          Rhein-Knudsen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6695-346X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rhein-Knudsen, N.' 1 0000-0001-6695-346X 
'Horn, S.J.'        2 0000-0002-1590-9001 
'Jeudy, A.'         3 0009-0008-8633-3952 
'Czjzek, M.'        4 0000-0002-7483-2841 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'J.Agric.Food Chem.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5118 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            73 
_citation.language                  ? 
_citation.page_first                2044 
_citation.page_last                 2055 
_citation.title                     'Identification and Characterization of a New Thermophilic kappa-Carrageenan Sulfatase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jafc.4c09751 
_citation.pdbx_database_id_PubMed   39797788 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rhein-Knudsen, N.' 1  ? 
primary 'Reyes-Weiss, D.S.' 2  ? 
primary 'Klau, L.J.'        3  ? 
primary 'Jeudy, A.'         4  ? 
primary 'Roret, T.'         5  ? 
primary 'Stokke, R.'        6  ? 
primary 'Eijsink, V.G.H.'   7  ? 
primary 'Aachmann, F.L.'    8  ? 
primary 'Czjzek, M.'        9  ? 
primary 'Horn, S.J.'        10 ? 
# 
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 'k-carrageenan sulfatase S1_16' 52969.078 1  ? ? ? ? 
2 non-polymer syn 'CALCIUM ION'                   40.078    2  ? ? ? ? 
3 non-polymer syn GLYCEROL                        92.094    1  ? ? ? ? 
4 water       nat water                           18.015    26 ? ? ? ? 
# 
_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       
;MGAQRPPDKLNFIIILIDDYGWTDSTCYGSTFYETPNIDRLAREGMRFTNAYAACPVCSPTRASILTGKYPAHLHLTDWI
PGRKQWPTSKLLGAPFYQELPLWETTIAERLKPLGYTTAAMGKWHLGHEPYYPERQGFDINVAGTFRGHPESYFGPFDLP
NFRGWTKNDYLTDRLTDKALQFLEENRQRPFFLYLAHFAVHTPLQAKAEMIAKYERKARGRKLQKNPTYAAMIESMDQGV
GRVMSKLEDLKIADHTVIIFTSDNGGLMYEGSRREPVTSNRPLRAGKGHLYEGGVRVPLIIRWPGVVKPGTTCDVPACSV
DFFPTIEEMAGLRHDPKLALDGVSLTPLLRRKGGFKPRALYWHYPHYSNQGGVPGGAIREGNLKLIEFYEDSHVELYDLS
EDIGERHNLAKEMPDKAAELQAKLKAWRASVRATMPTVNPNYDPARADQGLTGADPAHQLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGAQRPPDKLNFIIILIDDYGWTDSTCYGSTFYETPNIDRLAREGMRFTNAYAACPVCSPTRASILTGKYPAHLHLTDWI
PGRKQWPTSKLLGAPFYQELPLWETTIAERLKPLGYTTAAMGKWHLGHEPYYPERQGFDINVAGTFRGHPESYFGPFDLP
NFRGWTKNDYLTDRLTDKALQFLEENRQRPFFLYLAHFAVHTPLQAKAEMIAKYERKARGRKLQKNPTYAAMIESMDQGV
GRVMSKLEDLKIADHTVIIFTSDNGGLMYEGSRREPVTSNRPLRAGKGHLYEGGVRVPLIIRWPGVVKPGTTCDVPACSV
DFFPTIEEMAGLRHDPKLALDGVSLTPLLRRKGGFKPRALYWHYPHYSNQGGVPGGAIREGNLKLIEFYEDSHVELYDLS
EDIGERHNLAKEMPDKAAELQAKLKAWRASVRATMPTVNPNYDPARADQGLTGADPAHQLEHHHHHH
;
_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 'CALCIUM ION' CA  
3 GLYCEROL      GOL 
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   GLY n 
1 3   ALA n 
1 4   GLN n 
1 5   ARG n 
1 6   PRO n 
1 7   PRO n 
1 8   ASP n 
1 9   LYS n 
1 10  LEU n 
1 11  ASN n 
1 12  PHE n 
1 13  ILE n 
1 14  ILE n 
1 15  ILE n 
1 16  LEU n 
1 17  ILE n 
1 18  ASP n 
1 19  ASP n 
1 20  TYR n 
1 21  GLY n 
1 22  TRP n 
1 23  THR n 
1 24  ASP n 
1 25  SER n 
1 26  THR n 
1 27  CYS n 
1 28  TYR n 
1 29  GLY n 
1 30  SER n 
1 31  THR n 
1 32  PHE n 
1 33  TYR n 
1 34  GLU n 
1 35  THR n 
1 36  PRO n 
1 37  ASN n 
1 38  ILE n 
1 39  ASP n 
1 40  ARG n 
1 41  LEU n 
1 42  ALA n 
1 43  ARG n 
1 44  GLU n 
1 45  GLY n 
1 46  MET n 
1 47  ARG n 
1 48  PHE n 
1 49  THR n 
1 50  ASN n 
1 51  ALA n 
1 52  TYR n 
1 53  ALA n 
1 54  ALA n 
1 55  CYS n 
1 56  PRO n 
1 57  VAL n 
1 58  CYS n 
1 59  SER n 
1 60  PRO n 
1 61  THR n 
1 62  ARG n 
1 63  ALA n 
1 64  SER n 
1 65  ILE n 
1 66  LEU n 
1 67  THR n 
1 68  GLY n 
1 69  LYS n 
1 70  TYR n 
1 71  PRO n 
1 72  ALA n 
1 73  HIS n 
1 74  LEU n 
1 75  HIS n 
1 76  LEU n 
1 77  THR n 
1 78  ASP n 
1 79  TRP n 
1 80  ILE n 
1 81  PRO n 
1 82  GLY n 
1 83  ARG n 
1 84  LYS n 
1 85  GLN n 
1 86  TRP n 
1 87  PRO n 
1 88  THR n 
1 89  SER n 
1 90  LYS n 
1 91  LEU n 
1 92  LEU n 
1 93  GLY n 
1 94  ALA n 
1 95  PRO n 
1 96  PHE n 
1 97  TYR n 
1 98  GLN n 
1 99  GLU n 
1 100 LEU n 
1 101 PRO n 
1 102 LEU n 
1 103 TRP n 
1 104 GLU n 
1 105 THR n 
1 106 THR n 
1 107 ILE n 
1 108 ALA n 
1 109 GLU n 
1 110 ARG n 
1 111 LEU n 
1 112 LYS n 
1 113 PRO n 
1 114 LEU n 
1 115 GLY n 
1 116 TYR n 
1 117 THR n 
1 118 THR n 
1 119 ALA n 
1 120 ALA n 
1 121 MET n 
1 122 GLY n 
1 123 LYS n 
1 124 TRP n 
1 125 HIS n 
1 126 LEU n 
1 127 GLY n 
1 128 HIS n 
1 129 GLU n 
1 130 PRO n 
1 131 TYR n 
1 132 TYR n 
1 133 PRO n 
1 134 GLU n 
1 135 ARG n 
1 136 GLN n 
1 137 GLY n 
1 138 PHE n 
1 139 ASP n 
1 140 ILE n 
1 141 ASN n 
1 142 VAL n 
1 143 ALA n 
1 144 GLY n 
1 145 THR n 
1 146 PHE n 
1 147 ARG n 
1 148 GLY n 
1 149 HIS n 
1 150 PRO n 
1 151 GLU n 
1 152 SER n 
1 153 TYR n 
1 154 PHE n 
1 155 GLY n 
1 156 PRO n 
1 157 PHE n 
1 158 ASP n 
1 159 LEU n 
1 160 PRO n 
1 161 ASN n 
1 162 PHE n 
1 163 ARG n 
1 164 GLY n 
1 165 TRP n 
1 166 THR n 
1 167 LYS n 
1 168 ASN n 
1 169 ASP n 
1 170 TYR n 
1 171 LEU n 
1 172 THR n 
1 173 ASP n 
1 174 ARG n 
1 175 LEU n 
1 176 THR n 
1 177 ASP n 
1 178 LYS n 
1 179 ALA n 
1 180 LEU n 
1 181 GLN n 
1 182 PHE n 
1 183 LEU n 
1 184 GLU n 
1 185 GLU n 
1 186 ASN n 
1 187 ARG n 
1 188 GLN n 
1 189 ARG n 
1 190 PRO n 
1 191 PHE n 
1 192 PHE n 
1 193 LEU n 
1 194 TYR n 
1 195 LEU n 
1 196 ALA n 
1 197 HIS n 
1 198 PHE n 
1 199 ALA n 
1 200 VAL n 
1 201 HIS n 
1 202 THR n 
1 203 PRO n 
1 204 LEU n 
1 205 GLN n 
1 206 ALA n 
1 207 LYS n 
1 208 ALA n 
1 209 GLU n 
1 210 MET n 
1 211 ILE n 
1 212 ALA n 
1 213 LYS n 
1 214 TYR n 
1 215 GLU n 
1 216 ARG n 
1 217 LYS n 
1 218 ALA n 
1 219 ARG n 
1 220 GLY n 
1 221 ARG n 
1 222 LYS n 
1 223 LEU n 
1 224 GLN n 
1 225 LYS n 
1 226 ASN n 
1 227 PRO n 
1 228 THR n 
1 229 TYR n 
1 230 ALA n 
1 231 ALA n 
1 232 MET n 
1 233 ILE n 
1 234 GLU n 
1 235 SER n 
1 236 MET n 
1 237 ASP n 
1 238 GLN n 
1 239 GLY n 
1 240 VAL n 
1 241 GLY n 
1 242 ARG n 
1 243 VAL n 
1 244 MET n 
1 245 SER n 
1 246 LYS n 
1 247 LEU n 
1 248 GLU n 
1 249 ASP n 
1 250 LEU n 
1 251 LYS n 
1 252 ILE n 
1 253 ALA n 
1 254 ASP n 
1 255 HIS n 
1 256 THR n 
1 257 VAL n 
1 258 ILE n 
1 259 ILE n 
1 260 PHE n 
1 261 THR n 
1 262 SER n 
1 263 ASP n 
1 264 ASN n 
1 265 GLY n 
1 266 GLY n 
1 267 LEU n 
1 268 MET n 
1 269 TYR n 
1 270 GLU n 
1 271 GLY n 
1 272 SER n 
1 273 ARG n 
1 274 ARG n 
1 275 GLU n 
1 276 PRO n 
1 277 VAL n 
1 278 THR n 
1 279 SER n 
1 280 ASN n 
1 281 ARG n 
1 282 PRO n 
1 283 LEU n 
1 284 ARG n 
1 285 ALA n 
1 286 GLY n 
1 287 LYS n 
1 288 GLY n 
1 289 HIS n 
1 290 LEU n 
1 291 TYR n 
1 292 GLU n 
1 293 GLY n 
1 294 GLY n 
1 295 VAL n 
1 296 ARG n 
1 297 VAL n 
1 298 PRO n 
1 299 LEU n 
1 300 ILE n 
1 301 ILE n 
1 302 ARG n 
1 303 TRP n 
1 304 PRO n 
1 305 GLY n 
1 306 VAL n 
1 307 VAL n 
1 308 LYS n 
1 309 PRO n 
1 310 GLY n 
1 311 THR n 
1 312 THR n 
1 313 CYS n 
1 314 ASP n 
1 315 VAL n 
1 316 PRO n 
1 317 ALA n 
1 318 CYS n 
1 319 SER n 
1 320 VAL n 
1 321 ASP n 
1 322 PHE n 
1 323 PHE n 
1 324 PRO n 
1 325 THR n 
1 326 ILE n 
1 327 GLU n 
1 328 GLU n 
1 329 MET n 
1 330 ALA n 
1 331 GLY n 
1 332 LEU n 
1 333 ARG n 
1 334 HIS n 
1 335 ASP n 
1 336 PRO n 
1 337 LYS n 
1 338 LEU n 
1 339 ALA n 
1 340 LEU n 
1 341 ASP n 
1 342 GLY n 
1 343 VAL n 
1 344 SER n 
1 345 LEU n 
1 346 THR n 
1 347 PRO n 
1 348 LEU n 
1 349 LEU n 
1 350 ARG n 
1 351 ARG n 
1 352 LYS n 
1 353 GLY n 
1 354 GLY n 
1 355 PHE n 
1 356 LYS n 
1 357 PRO n 
1 358 ARG n 
1 359 ALA n 
1 360 LEU n 
1 361 TYR n 
1 362 TRP n 
1 363 HIS n 
1 364 TYR n 
1 365 PRO n 
1 366 HIS n 
1 367 TYR n 
1 368 SER n 
1 369 ASN n 
1 370 GLN n 
1 371 GLY n 
1 372 GLY n 
1 373 VAL n 
1 374 PRO n 
1 375 GLY n 
1 376 GLY n 
1 377 ALA n 
1 378 ILE n 
1 379 ARG n 
1 380 GLU n 
1 381 GLY n 
1 382 ASN n 
1 383 LEU n 
1 384 LYS n 
1 385 LEU n 
1 386 ILE n 
1 387 GLU n 
1 388 PHE n 
1 389 TYR n 
1 390 GLU n 
1 391 ASP n 
1 392 SER n 
1 393 HIS n 
1 394 VAL n 
1 395 GLU n 
1 396 LEU n 
1 397 TYR n 
1 398 ASP n 
1 399 LEU n 
1 400 SER n 
1 401 GLU n 
1 402 ASP n 
1 403 ILE n 
1 404 GLY n 
1 405 GLU n 
1 406 ARG n 
1 407 HIS n 
1 408 ASN n 
1 409 LEU n 
1 410 ALA n 
1 411 LYS n 
1 412 GLU n 
1 413 MET n 
1 414 PRO n 
1 415 ASP n 
1 416 LYS n 
1 417 ALA n 
1 418 ALA n 
1 419 GLU n 
1 420 LEU n 
1 421 GLN n 
1 422 ALA n 
1 423 LYS n 
1 424 LEU n 
1 425 LYS n 
1 426 ALA n 
1 427 TRP n 
1 428 ARG n 
1 429 ALA n 
1 430 SER n 
1 431 VAL n 
1 432 ARG n 
1 433 ALA n 
1 434 THR n 
1 435 MET n 
1 436 PRO n 
1 437 THR n 
1 438 VAL n 
1 439 ASN n 
1 440 PRO n 
1 441 ASN n 
1 442 TYR n 
1 443 ASP n 
1 444 PRO n 
1 445 ALA n 
1 446 ARG n 
1 447 ALA n 
1 448 ASP n 
1 449 GLN n 
1 450 GLY n 
1 451 LEU n 
1 452 THR n 
1 453 GLY n 
1 454 ALA n 
1 455 ASP n 
1 456 PRO n 
1 457 ALA n 
1 458 HIS n 
1 459 GLN n 
1 460 LEU n 
1 461 GLU n 
1 462 HIS n 
1 463 HIS n 
1 464 HIS n 
1 465 HIS n 
1 466 HIS n 
1 467 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   467 
_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      Bryobacteraceae 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1962910 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CA  non-polymer         . 'CALCIUM ION'   ?                               'Ca 2'           40.078  
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  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLY 2   2   ?   ?   ?   A . n 
A 1 3   ALA 3   3   ?   ?   ?   A . n 
A 1 4   GLN 4   4   ?   ?   ?   A . n 
A 1 5   ARG 5   5   ?   ?   ?   A . n 
A 1 6   PRO 6   6   6   PRO ALA A . n 
A 1 7   PRO 7   7   7   PRO PRO A . n 
A 1 8   ASP 8   8   8   ASP ASP A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  PHE 12  12  12  PHE PHE A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  ILE 14  14  14  ILE ILE A . n 
A 1 15  ILE 15  15  15  ILE ILE A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  TYR 20  20  20  TYR TYR A . n 
A 1 21  GLY 21  21  21  GLY GLY A . n 
A 1 22  TRP 22  22  22  TRP TRP A . n 
A 1 23  THR 23  23  23  THR THR A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  CYS 27  27  27  CYS CYS A . n 
A 1 28  TYR 28  28  28  TYR TYR A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  SER 30  30  30  SER SER A . n 
A 1 31  THR 31  31  31  THR THR A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ARG 43  43  43  ARG ARG A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  MET 46  46  46  MET MET A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  CYS 55  55  55  CYS CYS A . n 
A 1 56  PRO 56  56  56  PRO PRO A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  CYS 58  58  58  CYS CYS A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  TYR 70  70  70  TYR TYR A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  HIS 73  73  73  HIS HIS A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  HIS 75  75  75  HIS HIS A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  TRP 79  79  79  TRP TRP A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  PRO 81  81  81  PRO PRO A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  LYS 84  84  84  LYS LYS A . n 
A 1 85  GLN 85  85  85  GLN GLN A . n 
A 1 86  TRP 86  86  86  TRP TRP A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  PHE 96  96  96  PHE PHE A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 TRP 103 103 103 TRP TRP A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 ARG 110 110 110 ARG ARG A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 MET 121 121 121 MET MET A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 TRP 124 124 124 TRP TRP A . n 
A 1 125 HIS 125 125 125 HIS HIS A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 HIS 128 128 128 HIS HIS A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 TYR 131 131 131 TYR TYR A . n 
A 1 132 TYR 132 132 132 TYR TYR A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 ASN 141 141 141 ASN ASN A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 THR 145 145 145 THR THR A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 ARG 147 147 147 ARG ARG A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 HIS 149 149 149 HIS HIS A . n 
A 1 150 PRO 150 150 150 PRO PRO A . n 
A 1 151 GLU 151 151 151 GLU GLU A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 TYR 153 153 153 TYR TYR A . n 
A 1 154 PHE 154 154 154 PHE PHE A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 PRO 156 156 156 PRO PRO A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 PRO 160 160 160 PRO PRO A . n 
A 1 161 ASN 161 161 161 ASN ASN A . n 
A 1 162 PHE 162 162 162 PHE PHE A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 TRP 165 165 165 TRP TRP A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 ASN 168 168 168 ASN ASN A . n 
A 1 169 ASP 169 169 169 ASP ASP A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 THR 172 172 172 THR THR A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 ARG 174 174 174 ARG ARG A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 LYS 178 178 178 LYS LYS A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 GLN 181 181 181 GLN GLN A . n 
A 1 182 PHE 182 182 182 PHE PHE A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 ARG 187 187 187 ARG ARG A . n 
A 1 188 GLN 188 188 188 GLN GLN A . n 
A 1 189 ARG 189 189 189 ARG ARG A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 PHE 191 191 191 PHE PHE A . n 
A 1 192 PHE 192 192 192 PHE PHE A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 TYR 194 194 194 TYR TYR A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 HIS 197 197 197 HIS HIS A . n 
A 1 198 PHE 198 198 198 PHE PHE A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 HIS 201 201 201 HIS HIS A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 PRO 203 203 203 PRO PRO A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 GLN 205 205 205 GLN GLN A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 GLU 209 209 209 GLU GLU A . n 
A 1 210 MET 210 210 210 MET MET A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 LYS 213 213 213 LYS LYS A . n 
A 1 214 TYR 214 214 214 TYR TYR A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 ARG 216 216 216 ARG ARG A . n 
A 1 217 LYS 217 217 217 LYS LYS A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 ARG 219 219 219 ARG ARG A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 LYS 222 222 222 LYS LYS A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 GLN 224 224 224 GLN GLN A . n 
A 1 225 LYS 225 225 225 LYS LYS A . n 
A 1 226 ASN 226 226 226 ASN ASN A . n 
A 1 227 PRO 227 227 227 PRO PRO A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 TYR 229 229 229 TYR TYR A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 MET 232 232 232 MET MET A . n 
A 1 233 ILE 233 233 233 ILE ILE A . n 
A 1 234 GLU 234 234 234 GLU GLU A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 MET 236 236 236 MET MET A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 GLN 238 238 238 GLN GLN A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 GLY 241 241 241 GLY GLY A . n 
A 1 242 ARG 242 242 242 ARG ARG A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 MET 244 244 244 MET MET A . n 
A 1 245 SER 245 245 245 SER SER A . n 
A 1 246 LYS 246 246 246 LYS LYS A . n 
A 1 247 LEU 247 247 247 LEU LEU A . n 
A 1 248 GLU 248 248 248 GLU GLU A . n 
A 1 249 ASP 249 249 249 ASP ASP A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 HIS 255 255 255 HIS HIS A . n 
A 1 256 THR 256 256 256 THR THR A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 PHE 260 260 260 PHE PHE A . n 
A 1 261 THR 261 261 261 THR THR A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 ASN 264 264 264 ASN ASN A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 MET 268 268 268 MET MET A . n 
A 1 269 TYR 269 269 269 TYR TYR A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 SER 272 272 272 SER SER A . n 
A 1 273 ARG 273 273 273 ARG ARG A . n 
A 1 274 ARG 274 274 274 ARG ARG A . n 
A 1 275 GLU 275 275 275 GLU GLU A . n 
A 1 276 PRO 276 276 276 PRO PRO A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 SER 279 279 279 SER SER A . n 
A 1 280 ASN 280 280 280 ASN ASN A . n 
A 1 281 ARG 281 281 281 ARG ARG A . n 
A 1 282 PRO 282 282 282 PRO PRO A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 ARG 284 284 284 ARG ARG A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 GLY 286 286 286 GLY GLY A . n 
A 1 287 LYS 287 287 287 LYS LYS A . n 
A 1 288 GLY 288 288 288 GLY GLY A . n 
A 1 289 HIS 289 289 289 HIS HIS A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 TYR 291 291 291 TYR TYR A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 GLY 294 294 294 GLY GLY A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 ILE 300 300 300 ILE ILE A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 ARG 302 302 302 ARG ARG A . n 
A 1 303 TRP 303 303 303 TRP TRP A . n 
A 1 304 PRO 304 304 304 PRO PRO A . n 
A 1 305 GLY 305 305 305 GLY GLY A . n 
A 1 306 VAL 306 306 306 VAL VAL A . n 
A 1 307 VAL 307 307 307 VAL VAL A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 PRO 309 309 309 PRO PRO A . n 
A 1 310 GLY 310 310 310 GLY GLY A . n 
A 1 311 THR 311 311 311 THR THR A . n 
A 1 312 THR 312 312 312 THR THR A . n 
A 1 313 CYS 313 313 313 CYS CYS A . n 
A 1 314 ASP 314 314 314 ASP ASP A . n 
A 1 315 VAL 315 315 315 VAL VAL A . n 
A 1 316 PRO 316 316 316 PRO PRO A . n 
A 1 317 ALA 317 317 317 ALA ALA A . n 
A 1 318 CYS 318 318 318 CYS CYS A . n 
A 1 319 SER 319 319 319 SER SER A . n 
A 1 320 VAL 320 320 320 VAL VAL A . n 
A 1 321 ASP 321 321 321 ASP ASP A . n 
A 1 322 PHE 322 322 322 PHE PHE A . n 
A 1 323 PHE 323 323 323 PHE PHE A . n 
A 1 324 PRO 324 324 324 PRO PRO A . n 
A 1 325 THR 325 325 325 THR THR A . n 
A 1 326 ILE 326 326 326 ILE ILE A . n 
A 1 327 GLU 327 327 327 GLU GLU A . n 
A 1 328 GLU 328 328 328 GLU GLU A . n 
A 1 329 MET 329 329 329 MET MET A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 HIS 334 334 334 HIS HIS A . n 
A 1 335 ASP 335 335 335 ASP ASP A . n 
A 1 336 PRO 336 336 336 PRO PRO A . n 
A 1 337 LYS 337 337 337 LYS LYS A . n 
A 1 338 LEU 338 338 338 LEU LEU A . n 
A 1 339 ALA 339 339 339 ALA ALA A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 ASP 341 341 341 ASP ASP A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 VAL 343 343 343 VAL VAL A . n 
A 1 344 SER 344 344 344 SER SER A . n 
A 1 345 LEU 345 345 345 LEU LEU A . n 
A 1 346 THR 346 346 346 THR THR A . n 
A 1 347 PRO 347 347 347 PRO PRO A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 ARG 350 350 350 ARG ARG A . n 
A 1 351 ARG 351 351 351 ARG ARG A . n 
A 1 352 LYS 352 352 352 LYS LYS A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 PHE 355 355 355 PHE PHE A . n 
A 1 356 LYS 356 356 356 LYS LYS A . n 
A 1 357 PRO 357 357 357 PRO PRO A . n 
A 1 358 ARG 358 358 358 ARG ARG A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 TYR 361 361 361 TYR TYR A . n 
A 1 362 TRP 362 362 362 TRP TRP A . n 
A 1 363 HIS 363 363 363 HIS HIS A . n 
A 1 364 TYR 364 364 364 TYR TYR A . n 
A 1 365 PRO 365 365 365 PRO PRO A . n 
A 1 366 HIS 366 366 366 HIS HIS A . n 
A 1 367 TYR 367 367 367 TYR TYR A . n 
A 1 368 SER 368 368 368 SER SER A . n 
A 1 369 ASN 369 369 369 ASN ASN A . n 
A 1 370 GLN 370 370 370 GLN GLN A . n 
A 1 371 GLY 371 371 371 GLY GLY A . n 
A 1 372 GLY 372 372 372 GLY GLY A . n 
A 1 373 VAL 373 373 373 VAL VAL A . n 
A 1 374 PRO 374 374 374 PRO PRO A . n 
A 1 375 GLY 375 375 375 GLY GLY A . n 
A 1 376 GLY 376 376 376 GLY GLY A . n 
A 1 377 ALA 377 377 377 ALA ALA A . n 
A 1 378 ILE 378 378 378 ILE ILE A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 GLU 380 380 380 GLU GLU A . n 
A 1 381 GLY 381 381 381 GLY GLY A . n 
A 1 382 ASN 382 382 382 ASN ASN A . n 
A 1 383 LEU 383 383 383 LEU LEU A . n 
A 1 384 LYS 384 384 384 LYS LYS A . n 
A 1 385 LEU 385 385 385 LEU LEU A . n 
A 1 386 ILE 386 386 386 ILE ILE A . n 
A 1 387 GLU 387 387 387 GLU GLU A . n 
A 1 388 PHE 388 388 388 PHE PHE A . n 
A 1 389 TYR 389 389 389 TYR TYR A . n 
A 1 390 GLU 390 390 390 GLU GLU A . n 
A 1 391 ASP 391 391 391 ASP ASP A . n 
A 1 392 SER 392 392 392 SER SER A . n 
A 1 393 HIS 393 393 393 HIS HIS A . n 
A 1 394 VAL 394 394 394 VAL VAL A . n 
A 1 395 GLU 395 395 395 GLU GLU A . n 
A 1 396 LEU 396 396 396 LEU LEU A . n 
A 1 397 TYR 397 397 397 TYR TYR A . n 
A 1 398 ASP 398 398 398 ASP ASP A . n 
A 1 399 LEU 399 399 399 LEU LEU A . n 
A 1 400 SER 400 400 400 SER SER A . n 
A 1 401 GLU 401 401 401 GLU GLU A . n 
A 1 402 ASP 402 402 402 ASP ASP A . n 
A 1 403 ILE 403 403 403 ILE ILE A . n 
A 1 404 GLY 404 404 404 GLY GLY A . n 
A 1 405 GLU 405 405 405 GLU GLU A . n 
A 1 406 ARG 406 406 406 ARG ARG A . n 
A 1 407 HIS 407 407 407 HIS HIS A . n 
A 1 408 ASN 408 408 408 ASN ASN A . n 
A 1 409 LEU 409 409 409 LEU LEU A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 LYS 411 411 411 LYS LYS A . n 
A 1 412 GLU 412 412 412 GLU GLU A . n 
A 1 413 MET 413 413 413 MET MET A . n 
A 1 414 PRO 414 414 414 PRO PRO A . n 
A 1 415 ASP 415 415 415 ASP ASP A . n 
A 1 416 LYS 416 416 416 LYS LYS A . n 
A 1 417 ALA 417 417 417 ALA ALA A . n 
A 1 418 ALA 418 418 418 ALA ALA A . n 
A 1 419 GLU 419 419 419 GLU GLU A . n 
A 1 420 LEU 420 420 420 LEU LEU A . n 
A 1 421 GLN 421 421 421 GLN GLN A . n 
A 1 422 ALA 422 422 422 ALA ALA A . n 
A 1 423 LYS 423 423 423 LYS LYS A . n 
A 1 424 LEU 424 424 424 LEU LEU A . n 
A 1 425 LYS 425 425 425 LYS LYS A . n 
A 1 426 ALA 426 426 426 ALA ALA A . n 
A 1 427 TRP 427 427 427 TRP TRP A . n 
A 1 428 ARG 428 428 428 ARG ARG A . n 
A 1 429 ALA 429 429 429 ALA ALA A . n 
A 1 430 SER 430 430 430 SER SER A . n 
A 1 431 VAL 431 431 431 VAL VAL A . n 
A 1 432 ARG 432 432 432 ARG ARG A . n 
A 1 433 ALA 433 433 433 ALA ALA A . n 
A 1 434 THR 434 434 434 THR THR A . n 
A 1 435 MET 435 435 435 MET MET A . n 
A 1 436 PRO 436 436 436 PRO PRO A . n 
A 1 437 THR 437 437 437 THR THR A . n 
A 1 438 VAL 438 438 438 VAL VAL A . n 
A 1 439 ASN 439 439 439 ASN ASN A . n 
A 1 440 PRO 440 440 440 PRO PRO A . n 
A 1 441 ASN 441 441 441 ASN ASN A . n 
A 1 442 TYR 442 442 442 TYR TYR A . n 
A 1 443 ASP 443 443 443 ASP ASP A . n 
A 1 444 PRO 444 444 444 PRO PRO A . n 
A 1 445 ALA 445 445 445 ALA ALA A . n 
A 1 446 ARG 446 446 446 ARG ARG A . n 
A 1 447 ALA 447 447 447 ALA ALA A . n 
A 1 448 ASP 448 448 448 ASP ASP A . n 
A 1 449 GLN 449 449 449 GLN GLN A . n 
A 1 450 GLY 450 450 450 GLY GLY A . n 
A 1 451 LEU 451 451 451 LEU LEU A . n 
A 1 452 THR 452 452 452 THR THR A . n 
A 1 453 GLY 453 453 453 GLY GLY A . n 
A 1 454 ALA 454 454 454 ALA ALA A . n 
A 1 455 ASP 455 455 455 ASP ASP A . n 
A 1 456 PRO 456 456 456 PRO PRO A . n 
A 1 457 ALA 457 457 457 ALA ALA A . n 
A 1 458 HIS 458 458 ?   ?   ?   A . n 
A 1 459 GLN 459 459 ?   ?   ?   A . n 
A 1 460 LEU 460 460 ?   ?   ?   A . n 
A 1 461 GLU 461 461 ?   ?   ?   A . n 
A 1 462 HIS 462 462 ?   ?   ?   A . n 
A 1 463 HIS 463 463 ?   ?   ?   A . n 
A 1 464 HIS 464 464 ?   ?   ?   A . n 
A 1 465 HIS 465 465 ?   ?   ?   A . n 
A 1 466 HIS 466 466 ?   ?   ?   A . n 
A 1 467 HIS 467 467 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        GOL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   GOL 
_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 CA  1  501 501 CA  CA  A . 
C 2 CA  1  502 502 CA  CA  A . 
D 3 GOL 1  503 503 GOL GOL A . 
E 4 HOH 1  601 20  HOH HOH A . 
E 4 HOH 2  602 24  HOH HOH A . 
E 4 HOH 3  603 21  HOH HOH A . 
E 4 HOH 4  604 26  HOH HOH A . 
E 4 HOH 5  605 16  HOH HOH A . 
E 4 HOH 6  606 2   HOH HOH A . 
E 4 HOH 7  607 23  HOH HOH A . 
E 4 HOH 8  608 11  HOH HOH A . 
E 4 HOH 9  609 25  HOH HOH A . 
E 4 HOH 10 610 10  HOH HOH A . 
E 4 HOH 11 611 17  HOH HOH A . 
E 4 HOH 12 612 1   HOH HOH A . 
E 4 HOH 13 613 22  HOH HOH A . 
E 4 HOH 14 614 14  HOH HOH A . 
E 4 HOH 15 615 18  HOH HOH A . 
E 4 HOH 16 616 12  HOH HOH A . 
E 4 HOH 17 617 9   HOH HOH A . 
E 4 HOH 18 618 13  HOH HOH A . 
E 4 HOH 19 619 19  HOH HOH A . 
E 4 HOH 20 620 8   HOH HOH A . 
E 4 HOH 21 621 5   HOH HOH A . 
E 4 HOH 22 622 3   HOH HOH A . 
E 4 HOH 23 623 6   HOH HOH A . 
E 4 HOH 24 624 15  HOH HOH A . 
E 4 HOH 25 625 7   HOH HOH A . 
E 4 HOH 26 626 4   HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A PRO 6 ? CG ? A PRO 6 CG 
2 1 Y 1 A PRO 6 ? CD ? A PRO 6 CD 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        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                     9FO1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     206.314 
_cell.length_a_esd                 ? 
_cell.length_b                     206.314 
_cell.length_b_esd                 ? 
_cell.length_c                     206.314 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         9FO1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                199 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 21 3' 
_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                   9FO1 
_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             6.87 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          82.11 
_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              5.0 
_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    '0.1M Sodium citrate pH 5.0, 12% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-02-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.98011 
_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                        'SOLEIL BEAMLINE PROXIMA 2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98011 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 2' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FO1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.11 
_reflns.d_resolution_low                               48.6 
_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                                     26345 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                42.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.132 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.60 
_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                                    3.11 
_reflns_shell.d_res_low                                     3.33 
_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                             4723 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.94 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.53 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.00 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               74.526 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.946 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9FO1 
_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                            3.11 
_refine.ls_d_res_low                             45.89 
_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                     25055 
_refine.ls_number_reflns_R_free                  1270 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16331 
_refine.ls_R_factor_R_free                       0.19249 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16184 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.300 
_refine.pdbx_overall_ESU_R_Free                  0.232 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             11.706 
_refine.overall_SU_ML                            0.183 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.11 
_refine_hist.d_res_low                        45.89 
_refine_hist.number_atoms_solvent             26 
_refine_hist.number_atoms_total               3635 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3601 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         8 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.013  3712  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  3453  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.873  1.658  5041  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.389  1.579  7965  ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 8.189  5.000  451   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 32.354 20.833 204   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 19.233 15.000 598   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 20.442 15.000 31    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.076  0.200  463   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  4191  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  883   ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 7.128  7.496  1807  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 7.019  7.494  1806  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 9.775  11.250 2257  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 9.773  11.254 2258  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.585  8.166  1905  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 8.583  8.165  1906  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 12.025 11.970 2785  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 14.227 14     15711 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 14.227 14     15709 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       3.111 
_refine_ls_shell.d_res_low                        3.191 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             101 
_refine_ls_shell.number_reflns_R_work             1832 
_refine_ls_shell.percent_reflns_obs               99.90 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.338 
_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   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.348 
# 
_struct.entry_id                     9FO1 
_struct.title                        'Family S1_16 sulfatase from metagenomic dataset AMOR' 
_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        9FO1 
_struct_keywords.text            'carrageenan sulfatase, 4S-galactose specific sulfatase, marine metagenome, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9FO1 
_struct_ref.pdbx_db_accession          9FO1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9FO1 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 467 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             9FO1 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  467 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       467 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 380   ? 
1 MORE         -11   ? 
1 'SSA (A^2)'  17600 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 25  ? GLY A 29  ? SER A 25  GLY A 29  5 ? 5  
HELX_P HELX_P2  AA2 THR A 35  ? GLU A 44  ? THR A 35  GLU A 44  1 ? 10 
HELX_P HELX_P3  AA3 VAL A 57  ? GLY A 68  ? VAL A 57  GLY A 68  1 ? 12 
HELX_P HELX_P4  AA4 TYR A 70  ? HIS A 75  ? TYR A 70  HIS A 75  1 ? 6  
HELX_P HELX_P5  AA5 THR A 106 ? LYS A 112 ? THR A 106 LYS A 112 1 ? 7  
HELX_P HELX_P6  AA6 PRO A 113 ? GLY A 115 ? PRO A 113 GLY A 115 5 ? 3  
HELX_P HELX_P7  AA7 TYR A 132 ? GLN A 136 ? TYR A 132 GLN A 136 5 ? 5  
HELX_P HELX_P8  AA8 TYR A 170 ? ASN A 186 ? TYR A 170 ASN A 186 1 ? 17 
HELX_P HELX_P9  AA9 LYS A 207 ? ARG A 219 ? LYS A 207 ARG A 219 1 ? 13 
HELX_P HELX_P10 AB1 ASN A 226 ? LEU A 250 ? ASN A 226 LEU A 250 1 ? 25 
HELX_P HELX_P11 AB2 ILE A 252 ? ASP A 254 ? ILE A 252 ASP A 254 5 ? 3  
HELX_P HELX_P12 AB3 TYR A 291 ? GLY A 294 ? TYR A 291 GLY A 294 5 ? 4  
HELX_P HELX_P13 AB4 ASP A 321 ? ALA A 330 ? ASP A 321 ALA A 330 1 ? 10 
HELX_P HELX_P14 AB5 LEU A 345 ? ARG A 350 ? LEU A 345 ARG A 350 1 ? 6  
HELX_P HELX_P15 AB6 MET A 413 ? VAL A 431 ? MET A 413 VAL A 431 1 ? 19 
HELX_P HELX_P16 AB7 ASP A 443 ? ALA A 447 ? ASP A 443 ALA A 447 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 18  OD1 ? ? ? 1_555 B CA . CA ? ? A ASP 18  A CA 501 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
metalc2  metalc ? ? A ASP 19  OD1 ? ? ? 1_555 B CA . CA ? ? A ASP 19  A CA 501 1_555 ? ? ? ? ? ? ? 2.193 ? ? 
metalc3  metalc ? ? A LEU 102 O   ? ? ? 1_555 C CA . CA ? ? A LEU 102 A CA 502 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc4  metalc ? ? A GLU 104 O   ? ? ? 1_555 C CA . CA ? ? A GLU 104 A CA 502 1_555 ? ? ? ? ? ? ? 2.910 ? ? 
metalc5  metalc ? ? A GLU 109 OE1 ? ? ? 1_555 C CA . CA ? ? A GLU 109 A CA 502 1_555 ? ? ? ? ? ? ? 3.060 ? ? 
metalc6  metalc ? ? A GLU 109 OE2 ? ? ? 1_555 C CA . CA ? ? A GLU 109 A CA 502 1_555 ? ? ? ? ? ? ? 2.306 ? ? 
metalc7  metalc ? ? A GLN 136 OE1 ? ? ? 1_555 C CA . CA ? ? A GLN 136 A CA 502 1_555 ? ? ? ? ? ? ? 2.733 ? ? 
metalc8  metalc ? ? A ASP 263 OD1 ? ? ? 1_555 B CA . CA ? ? A ASP 263 A CA 501 1_555 ? ? ? ? ? ? ? 2.815 ? ? 
metalc9  metalc ? ? A ASP 263 OD2 ? ? ? 1_555 B CA . CA ? ? A ASP 263 A CA 501 1_555 ? ? ? ? ? ? ? 2.163 ? ? 
metalc10 metalc ? ? A ASN 264 OD1 ? ? ? 1_555 B CA . CA ? ? A ASN 264 A CA 501 1_555 ? ? ? ? ? ? ? 2.231 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 18  ? A ASP 18  ? 1_555 CA ? B CA . ? A CA 501 ? 1_555 OD1 ? A ASP 19  ? A ASP 19  ? 1_555 80.5  ? 
2  OD1 ? A ASP 18  ? A ASP 18  ? 1_555 CA ? B CA . ? A CA 501 ? 1_555 OD1 ? A ASP 263 ? A ASP 263 ? 1_555 71.6  ? 
3  OD1 ? A ASP 19  ? A ASP 19  ? 1_555 CA ? B CA . ? A CA 501 ? 1_555 OD1 ? A ASP 263 ? A ASP 263 ? 1_555 100.0 ? 
4  OD1 ? A ASP 18  ? A ASP 18  ? 1_555 CA ? B CA . ? A CA 501 ? 1_555 OD2 ? A ASP 263 ? A ASP 263 ? 1_555 76.2  ? 
5  OD1 ? A ASP 19  ? A ASP 19  ? 1_555 CA ? B CA . ? A CA 501 ? 1_555 OD2 ? A ASP 263 ? A ASP 263 ? 1_555 147.0 ? 
6  OD1 ? A ASP 263 ? A ASP 263 ? 1_555 CA ? B CA . ? A CA 501 ? 1_555 OD2 ? A ASP 263 ? A ASP 263 ? 1_555 50.5  ? 
7  OD1 ? A ASP 18  ? A ASP 18  ? 1_555 CA ? B CA . ? A CA 501 ? 1_555 OD1 ? A ASN 264 ? A ASN 264 ? 1_555 143.1 ? 
8  OD1 ? A ASP 19  ? A ASP 19  ? 1_555 CA ? B CA . ? A CA 501 ? 1_555 OD1 ? A ASN 264 ? A ASN 264 ? 1_555 93.8  ? 
9  OD1 ? A ASP 263 ? A ASP 263 ? 1_555 CA ? B CA . ? A CA 501 ? 1_555 OD1 ? A ASN 264 ? A ASN 264 ? 1_555 73.7  ? 
10 OD2 ? A ASP 263 ? A ASP 263 ? 1_555 CA ? B CA . ? A CA 501 ? 1_555 OD1 ? A ASN 264 ? A ASN 264 ? 1_555 91.1  ? 
11 O   ? A LEU 102 ? A LEU 102 ? 1_555 CA ? C CA . ? A CA 502 ? 1_555 O   ? A GLU 104 ? A GLU 104 ? 1_555 80.4  ? 
12 O   ? A LEU 102 ? A LEU 102 ? 1_555 CA ? C CA . ? A CA 502 ? 1_555 OE1 ? A GLU 109 ? A GLU 109 ? 1_555 139.0 ? 
13 O   ? A GLU 104 ? A GLU 104 ? 1_555 CA ? C CA . ? A CA 502 ? 1_555 OE1 ? A GLU 109 ? A GLU 109 ? 1_555 94.6  ? 
14 O   ? A LEU 102 ? A LEU 102 ? 1_555 CA ? C CA . ? A CA 502 ? 1_555 OE2 ? A GLU 109 ? A GLU 109 ? 1_555 152.9 ? 
15 O   ? A GLU 104 ? A GLU 104 ? 1_555 CA ? C CA . ? A CA 502 ? 1_555 OE2 ? A GLU 109 ? A GLU 109 ? 1_555 72.5  ? 
16 OE1 ? A GLU 109 ? A GLU 109 ? 1_555 CA ? C CA . ? A CA 502 ? 1_555 OE2 ? A GLU 109 ? A GLU 109 ? 1_555 46.2  ? 
17 O   ? A LEU 102 ? A LEU 102 ? 1_555 CA ? C CA . ? A CA 502 ? 1_555 OE1 ? A GLN 136 ? A GLN 136 ? 1_555 91.0  ? 
18 O   ? A GLU 104 ? A GLU 104 ? 1_555 CA ? C CA . ? A CA 502 ? 1_555 OE1 ? A GLN 136 ? A GLN 136 ? 1_555 69.8  ? 
19 OE1 ? A GLU 109 ? A GLU 109 ? 1_555 CA ? C CA . ? A CA 502 ? 1_555 OE1 ? A GLN 136 ? A GLN 136 ? 1_555 125.7 ? 
20 OE2 ? A GLU 109 ? A GLU 109 ? 1_555 CA ? C CA . ? A CA 502 ? 1_555 OE1 ? A GLN 136 ? A GLN 136 ? 1_555 79.9  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ILE 80  A . ? ILE 80  A PRO 81  A ? PRO 81  A 1 1.95  
2 GLY 155 A . ? GLY 155 A PRO 156 A ? PRO 156 A 1 -6.17 
3 ALA 199 A . ? ALA 199 A VAL 200 A ? VAL 200 A 1 18.07 
4 THR 202 A . ? THR 202 A PRO 203 A ? PRO 203 A 1 -0.47 
5 ARG 281 A . ? ARG 281 A PRO 282 A ? PRO 282 A 1 4.09  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? 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 ILE A 140 ? VAL A 142 ? ILE A 140 VAL A 142 
AA1 2 THR A 117 ? GLY A 122 ? THR A 117 GLY A 122 
AA1 3 PHE A 191 ? ALA A 196 ? PHE A 191 ALA A 196 
AA1 4 ASN A 11  ? ILE A 17  ? ASN A 11  ILE A 17  
AA1 5 THR A 256 ? SER A 262 ? THR A 256 SER A 262 
AA1 6 LEU A 299 ? ARG A 302 ? LEU A 299 ARG A 302 
AA1 7 MET A 46  ? PHE A 48  ? MET A 46  PHE A 48  
AA1 8 THR A 312 ? CYS A 313 ? THR A 312 CYS A 313 
AA2 1 ARG A 296 ? VAL A 297 ? ARG A 296 VAL A 297 
AA2 2 ALA A 51  ? TYR A 52  ? ALA A 51  TYR A 52  
AA2 3 ALA A 317 ? CYS A 318 ? ALA A 317 CYS A 318 
AA3 1 LEU A 91  ? LEU A 92  ? LEU A 91  LEU A 92  
AA3 2 THR A 437 ? VAL A 438 ? THR A 437 VAL A 438 
AA4 1 ASP A 158 ? LEU A 159 ? ASP A 158 LEU A 159 
AA4 2 PHE A 162 ? ARG A 163 ? PHE A 162 ARG A 163 
AA5 1 ALA A 359 ? TYR A 364 ? ALA A 359 TYR A 364 
AA5 2 GLY A 375 ? GLU A 380 ? GLY A 375 GLU A 380 
AA5 3 LEU A 383 ? PHE A 388 ? LEU A 383 PHE A 388 
AA5 4 VAL A 394 ? ASP A 398 ? VAL A 394 ASP A 398 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 142 ? O VAL A 142 N GLY A 122 ? N GLY A 122 
AA1 2 3 N ALA A 119 ? N ALA A 119 O TYR A 194 ? O TYR A 194 
AA1 3 4 O LEU A 195 ? O LEU A 195 N ILE A 14  ? N ILE A 14  
AA1 4 5 N ILE A 15  ? N ILE A 15  O ILE A 259 ? O ILE A 259 
AA1 5 6 N PHE A 260 ? N PHE A 260 O ILE A 300 ? O ILE A 300 
AA1 6 7 O LEU A 299 ? O LEU A 299 N PHE A 48  ? N PHE A 48  
AA1 7 8 N ARG A 47  ? N ARG A 47  O CYS A 313 ? O CYS A 313 
AA2 1 2 O VAL A 297 ? O VAL A 297 N ALA A 51  ? N ALA A 51  
AA2 2 3 N TYR A 52  ? N TYR A 52  O ALA A 317 ? O ALA A 317 
AA3 1 2 N LEU A 92  ? N LEU A 92  O THR A 437 ? O THR A 437 
AA4 1 2 N LEU A 159 ? N LEU A 159 O PHE A 162 ? O PHE A 162 
AA5 1 2 N TYR A 364 ? N TYR A 364 O GLY A 375 ? O GLY A 375 
AA5 2 3 N GLY A 376 ? N GLY A 376 O GLU A 387 ? O GLU A 387 
AA5 3 4 N ILE A 386 ? N ILE A 386 O GLU A 395 ? O GLU A 395 
# 
_pdbx_entry_details.entry_id                   9FO1 
_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 NZ A LYS 112 ? ? OD2 A ASP 139 ? ? 1.95 
2 1 NZ A LYS 112 ? ? OD1 A ASP 139 ? ? 2.05 
# 
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 PRO A 7   ? ? -87.30  -137.31 
2  1 ASP A 8   ? ? -150.67 87.74   
3  1 ASN A 50  ? ? -117.55 51.64   
4  1 CYS A 58  ? ? -58.58  -71.94  
5  1 PRO A 113 ? ? -55.96  -6.47   
6  1 TRP A 124 ? ? -95.60  -72.64  
7  1 GLN A 136 ? ? -160.95 30.32   
8  1 ALA A 143 ? ? 79.95   -6.03   
9  1 TRP A 165 ? ? -137.32 -135.60 
10 1 LYS A 167 ? ? -60.91  1.63    
11 1 LYS A 222 ? ? 70.87   -65.18  
12 1 LEU A 223 ? ? -79.69  -118.27 
13 1 MET A 268 ? ? -164.54 88.34   
14 1 TYR A 269 ? ? 97.06   56.86   
15 1 ALA A 285 ? ? 63.84   -140.34 
16 1 ASP A 402 ? ? -162.10 47.46   
17 1 ALA A 454 ? ? -57.52  92.53   
18 1 ASP A 455 ? ? -31.83  119.20  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 GLU A 129 ? ? PRO A 130 ? ? 56.96 
2 1 ASP A 455 ? ? PRO A 456 ? ? 79.44 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     609 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A GLY 2   ? A GLY 2   
3  1 Y 1 A ALA 3   ? A ALA 3   
4  1 Y 1 A GLN 4   ? A GLN 4   
5  1 Y 1 A ARG 5   ? A ARG 5   
6  1 Y 1 A HIS 458 ? A HIS 458 
7  1 Y 1 A GLN 459 ? A GLN 459 
8  1 Y 1 A LEU 460 ? A LEU 460 
9  1 Y 1 A GLU 461 ? A GLU 461 
10 1 Y 1 A HIS 462 ? A HIS 462 
11 1 Y 1 A HIS 463 ? A HIS 463 
12 1 Y 1 A HIS 464 ? A HIS 464 
13 1 Y 1 A HIS 465 ? A HIS 465 
14 1 Y 1 A HIS 466 ? A HIS 466 
15 1 Y 1 A HIS 467 ? A HIS 467 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CA  CA   CA N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
GOL C1   C  N N 138 
GOL O1   O  N N 139 
GOL C2   C  N N 140 
GOL O2   O  N N 141 
GOL C3   C  N N 142 
GOL O3   O  N N 143 
GOL H11  H  N N 144 
GOL H12  H  N N 145 
GOL HO1  H  N N 146 
GOL H2   H  N N 147 
GOL HO2  H  N N 148 
GOL H31  H  N N 149 
GOL H32  H  N N 150 
GOL HO3  H  N N 151 
HIS N    N  N N 152 
HIS CA   C  N S 153 
HIS C    C  N N 154 
HIS O    O  N N 155 
HIS CB   C  N N 156 
HIS CG   C  Y N 157 
HIS ND1  N  Y N 158 
HIS CD2  C  Y N 159 
HIS CE1  C  Y N 160 
HIS NE2  N  Y N 161 
HIS OXT  O  N N 162 
HIS H    H  N N 163 
HIS H2   H  N N 164 
HIS HA   H  N N 165 
HIS HB2  H  N N 166 
HIS HB3  H  N N 167 
HIS HD1  H  N N 168 
HIS HD2  H  N N 169 
HIS HE1  H  N N 170 
HIS HE2  H  N N 171 
HIS HXT  H  N N 172 
HOH O    O  N N 173 
HOH H1   H  N N 174 
HOH H2   H  N N 175 
ILE N    N  N N 176 
ILE CA   C  N S 177 
ILE C    C  N N 178 
ILE O    O  N N 179 
ILE CB   C  N S 180 
ILE CG1  C  N N 181 
ILE CG2  C  N N 182 
ILE CD1  C  N N 183 
ILE OXT  O  N N 184 
ILE H    H  N N 185 
ILE H2   H  N N 186 
ILE HA   H  N N 187 
ILE HB   H  N N 188 
ILE HG12 H  N N 189 
ILE HG13 H  N N 190 
ILE HG21 H  N N 191 
ILE HG22 H  N N 192 
ILE HG23 H  N N 193 
ILE HD11 H  N N 194 
ILE HD12 H  N N 195 
ILE HD13 H  N N 196 
ILE HXT  H  N N 197 
LEU N    N  N N 198 
LEU CA   C  N S 199 
LEU C    C  N N 200 
LEU O    O  N N 201 
LEU CB   C  N N 202 
LEU CG   C  N N 203 
LEU CD1  C  N N 204 
LEU CD2  C  N N 205 
LEU OXT  O  N N 206 
LEU H    H  N N 207 
LEU H2   H  N N 208 
LEU HA   H  N N 209 
LEU HB2  H  N N 210 
LEU HB3  H  N N 211 
LEU HG   H  N N 212 
LEU HD11 H  N N 213 
LEU HD12 H  N N 214 
LEU HD13 H  N N 215 
LEU HD21 H  N N 216 
LEU HD22 H  N N 217 
LEU HD23 H  N N 218 
LEU HXT  H  N N 219 
LYS N    N  N N 220 
LYS CA   C  N S 221 
LYS C    C  N N 222 
LYS O    O  N N 223 
LYS CB   C  N N 224 
LYS CG   C  N N 225 
LYS CD   C  N N 226 
LYS CE   C  N N 227 
LYS NZ   N  N N 228 
LYS OXT  O  N N 229 
LYS H    H  N N 230 
LYS H2   H  N N 231 
LYS HA   H  N N 232 
LYS HB2  H  N N 233 
LYS HB3  H  N N 234 
LYS HG2  H  N N 235 
LYS HG3  H  N N 236 
LYS HD2  H  N N 237 
LYS HD3  H  N N 238 
LYS HE2  H  N N 239 
LYS HE3  H  N N 240 
LYS HZ1  H  N N 241 
LYS HZ2  H  N N 242 
LYS HZ3  H  N N 243 
LYS HXT  H  N N 244 
MET N    N  N N 245 
MET CA   C  N S 246 
MET C    C  N N 247 
MET O    O  N N 248 
MET CB   C  N N 249 
MET CG   C  N N 250 
MET SD   S  N N 251 
MET CE   C  N N 252 
MET OXT  O  N N 253 
MET H    H  N N 254 
MET H2   H  N N 255 
MET HA   H  N N 256 
MET HB2  H  N N 257 
MET HB3  H  N N 258 
MET HG2  H  N N 259 
MET HG3  H  N N 260 
MET HE1  H  N N 261 
MET HE2  H  N N 262 
MET HE3  H  N N 263 
MET HXT  H  N N 264 
PHE N    N  N N 265 
PHE CA   C  N S 266 
PHE C    C  N N 267 
PHE O    O  N N 268 
PHE CB   C  N N 269 
PHE CG   C  Y N 270 
PHE CD1  C  Y N 271 
PHE CD2  C  Y N 272 
PHE CE1  C  Y N 273 
PHE CE2  C  Y N 274 
PHE CZ   C  Y N 275 
PHE OXT  O  N N 276 
PHE H    H  N N 277 
PHE H2   H  N N 278 
PHE HA   H  N N 279 
PHE HB2  H  N N 280 
PHE HB3  H  N N 281 
PHE HD1  H  N N 282 
PHE HD2  H  N N 283 
PHE HE1  H  N N 284 
PHE HE2  H  N N 285 
PHE HZ   H  N N 286 
PHE HXT  H  N N 287 
PRO N    N  N N 288 
PRO CA   C  N S 289 
PRO C    C  N N 290 
PRO O    O  N N 291 
PRO CB   C  N N 292 
PRO CG   C  N N 293 
PRO CD   C  N N 294 
PRO OXT  O  N N 295 
PRO H    H  N N 296 
PRO HA   H  N N 297 
PRO HB2  H  N N 298 
PRO HB3  H  N N 299 
PRO HG2  H  N N 300 
PRO HG3  H  N N 301 
PRO HD2  H  N N 302 
PRO HD3  H  N N 303 
PRO HXT  H  N N 304 
SER N    N  N N 305 
SER CA   C  N S 306 
SER C    C  N N 307 
SER O    O  N N 308 
SER CB   C  N N 309 
SER OG   O  N N 310 
SER OXT  O  N N 311 
SER H    H  N N 312 
SER H2   H  N N 313 
SER HA   H  N N 314 
SER HB2  H  N N 315 
SER HB3  H  N N 316 
SER HG   H  N N 317 
SER HXT  H  N N 318 
THR N    N  N N 319 
THR CA   C  N S 320 
THR C    C  N N 321 
THR O    O  N N 322 
THR CB   C  N R 323 
THR OG1  O  N N 324 
THR CG2  C  N N 325 
THR OXT  O  N N 326 
THR H    H  N N 327 
THR H2   H  N N 328 
THR HA   H  N N 329 
THR HB   H  N N 330 
THR HG1  H  N N 331 
THR HG21 H  N N 332 
THR HG22 H  N N 333 
THR HG23 H  N N 334 
THR HXT  H  N N 335 
TRP N    N  N N 336 
TRP CA   C  N S 337 
TRP C    C  N N 338 
TRP O    O  N N 339 
TRP CB   C  N N 340 
TRP CG   C  Y N 341 
TRP CD1  C  Y N 342 
TRP CD2  C  Y N 343 
TRP NE1  N  Y N 344 
TRP CE2  C  Y N 345 
TRP CE3  C  Y N 346 
TRP CZ2  C  Y N 347 
TRP CZ3  C  Y N 348 
TRP CH2  C  Y N 349 
TRP OXT  O  N N 350 
TRP H    H  N N 351 
TRP H2   H  N N 352 
TRP HA   H  N N 353 
TRP HB2  H  N N 354 
TRP HB3  H  N N 355 
TRP HD1  H  N N 356 
TRP HE1  H  N N 357 
TRP HE3  H  N N 358 
TRP HZ2  H  N N 359 
TRP HZ3  H  N N 360 
TRP HH2  H  N N 361 
TRP HXT  H  N N 362 
TYR N    N  N N 363 
TYR CA   C  N S 364 
TYR C    C  N N 365 
TYR O    O  N N 366 
TYR CB   C  N N 367 
TYR CG   C  Y N 368 
TYR CD1  C  Y N 369 
TYR CD2  C  Y N 370 
TYR CE1  C  Y N 371 
TYR CE2  C  Y N 372 
TYR CZ   C  Y N 373 
TYR OH   O  N N 374 
TYR OXT  O  N N 375 
TYR H    H  N N 376 
TYR H2   H  N N 377 
TYR HA   H  N N 378 
TYR HB2  H  N N 379 
TYR HB3  H  N N 380 
TYR HD1  H  N N 381 
TYR HD2  H  N N 382 
TYR HE1  H  N N 383 
TYR HE2  H  N N 384 
TYR HH   H  N N 385 
TYR HXT  H  N N 386 
VAL N    N  N N 387 
VAL CA   C  N S 388 
VAL C    C  N N 389 
VAL O    O  N N 390 
VAL CB   C  N N 391 
VAL CG1  C  N N 392 
VAL CG2  C  N N 393 
VAL OXT  O  N N 394 
VAL H    H  N N 395 
VAL H2   H  N N 396 
VAL HA   H  N N 397 
VAL HB   H  N N 398 
VAL HG11 H  N N 399 
VAL HG12 H  N N 400 
VAL HG13 H  N N 401 
VAL HG21 H  N N 402 
VAL HG22 H  N N 403 
VAL HG23 H  N N 404 
VAL HXT  H  N N 405 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   'Research Council of Norway' 
_pdbx_audit_support.country                Norway 
_pdbx_audit_support.grant_number           294946 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FO1 
_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]   0.004847 
_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]   0.004847 
_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]   0.004847 
_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  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . PRO A 1 6   ? 53.929  3.208   24.101 1.00 129.88 ? 6   PRO A N   1 
ATOM   2    C  CA  . PRO A 1 6   ? 52.799  3.515   25.009 1.00 140.64 ? 6   PRO A CA  1 
ATOM   3    C  C   . PRO A 1 6   ? 52.058  2.225   25.375 1.00 174.07 ? 6   PRO A C   1 
ATOM   4    O  O   . PRO A 1 6   ? 52.662  1.142   25.257 1.00 157.30 ? 6   PRO A O   1 
ATOM   5    C  CB  . PRO A 1 6   ? 51.875  4.513   24.359 1.00 118.15 ? 6   PRO A CB  1 
ATOM   6    N  N   . PRO A 1 7   ? 50.823  2.234   25.947 1.00 189.29 ? 7   PRO A N   1 
ATOM   7    C  CA  . PRO A 1 7   ? 50.099  0.981   26.214 1.00 160.01 ? 7   PRO A CA  1 
ATOM   8    C  C   . PRO A 1 7   ? 49.255  0.486   25.030 1.00 139.76 ? 7   PRO A C   1 
ATOM   9    O  O   . PRO A 1 7   ? 49.738  0.540   23.914 1.00 144.32 ? 7   PRO A O   1 
ATOM   10   C  CB  . PRO A 1 7   ? 49.167  1.356   27.373 1.00 140.65 ? 7   PRO A CB  1 
ATOM   11   C  CG  . PRO A 1 7   ? 48.799  2.784   27.071 1.00 144.46 ? 7   PRO A CG  1 
ATOM   12   C  CD  . PRO A 1 7   ? 50.071  3.379   26.502 1.00 152.82 ? 7   PRO A CD  1 
ATOM   13   N  N   . ASP A 1 8   ? 48.030  0.021   25.299 1.00 118.09 ? 8   ASP A N   1 
ATOM   14   C  CA  . ASP A 1 8   ? 47.185  -0.553  24.220 1.00 119.63 ? 8   ASP A CA  1 
ATOM   15   C  C   . ASP A 1 8   ? 45.713  -0.324  24.568 1.00 107.41 ? 8   ASP A C   1 
ATOM   16   O  O   . ASP A 1 8   ? 45.115  -1.201  25.208 1.00 131.88 ? 8   ASP A O   1 
ATOM   17   C  CB  . ASP A 1 8   ? 47.517  -2.025  23.974 1.00 110.64 ? 8   ASP A CB  1 
ATOM   18   C  CG  . ASP A 1 8   ? 47.776  -2.343  22.513 1.00 107.67 ? 8   ASP A CG  1 
ATOM   19   O  OD1 . ASP A 1 8   ? 47.685  -1.414  21.689 1.00 95.99  ? 8   ASP A OD1 1 
ATOM   20   O  OD2 . ASP A 1 8   ? 48.065  -3.516  22.213 1.00 103.46 ? 8   ASP A OD2 1 
ATOM   21   N  N   . LYS A 1 9   ? 45.165  0.824   24.175 1.00 93.83  ? 9   LYS A N   1 
ATOM   22   C  CA  . LYS A 1 9   ? 43.718  1.126   24.401 1.00 82.27  ? 9   LYS A CA  1 
ATOM   23   C  C   . LYS A 1 9   ? 42.835  -0.065  24.015 1.00 76.59  ? 9   LYS A C   1 
ATOM   24   O  O   . LYS A 1 9   ? 42.938  -0.603  22.873 1.00 75.56  ? 9   LYS A O   1 
ATOM   25   C  CB  . LYS A 1 9   ? 43.184  2.297   23.573 1.00 81.08  ? 9   LYS A CB  1 
ATOM   26   C  CG  . LYS A 1 9   ? 43.804  3.640   23.886 1.00 87.21  ? 9   LYS A CG  1 
ATOM   27   C  CD  . LYS A 1 9   ? 42.988  4.801   23.419 1.00 86.16  ? 9   LYS A CD  1 
ATOM   28   C  CE  . LYS A 1 9   ? 43.401  6.045   24.166 1.00 91.97  ? 9   LYS A CE  1 
ATOM   29   N  NZ  . LYS A 1 9   ? 43.176  7.245   23.344 1.00 104.58 ? 9   LYS A NZ  1 
ATOM   30   N  N   . LEU A 1 10  ? 41.913  -0.389  24.910 1.00 70.70  ? 10  LEU A N   1 
ATOM   31   C  CA  . LEU A 1 10  ? 41.015  -1.567  24.802 1.00 66.78  ? 10  LEU A CA  1 
ATOM   32   C  C   . LEU A 1 10  ? 39.945  -1.337  23.760 1.00 57.04  ? 10  LEU A C   1 
ATOM   33   O  O   . LEU A 1 10  ? 39.347  -0.279  23.778 1.00 61.08  ? 10  LEU A O   1 
ATOM   34   C  CB  . LEU A 1 10  ? 40.340  -1.798  26.149 1.00 73.30  ? 10  LEU A CB  1 
ATOM   35   C  CG  . LEU A 1 10  ? 41.216  -2.569  27.106 1.00 72.28  ? 10  LEU A CG  1 
ATOM   36   C  CD1 . LEU A 1 10  ? 40.498  -2.791  28.415 1.00 72.27  ? 10  LEU A CD1 1 
ATOM   37   C  CD2 . LEU A 1 10  ? 41.611  -3.869  26.428 1.00 74.05  ? 10  LEU A CD2 1 
ATOM   38   N  N   . ASN A 1 11  ? 39.706  -2.325  22.917 1.00 59.64  ? 11  ASN A N   1 
ATOM   39   C  CA  . ASN A 1 11  ? 38.525  -2.336  22.020 1.00 64.42  ? 11  ASN A CA  1 
ATOM   40   C  C   . ASN A 1 11  ? 37.407  -3.012  22.807 1.00 64.66  ? 11  ASN A C   1 
ATOM   41   O  O   . ASN A 1 11  ? 37.692  -3.629  23.836 1.00 74.10  ? 11  ASN A O   1 
ATOM   42   C  CB  . ASN A 1 11  ? 38.803  -2.993  20.666 1.00 59.78  ? 11  ASN A CB  1 
ATOM   43   C  CG  . ASN A 1 11  ? 40.002  -2.405  19.950 1.00 66.56  ? 11  ASN A CG  1 
ATOM   44   O  OD1 . ASN A 1 11  ? 40.498  -1.318  20.262 1.00 71.18  ? 11  ASN A OD1 1 
ATOM   45   N  ND2 . ASN A 1 11  ? 40.509  -3.143  18.984 1.00 72.62  ? 11  ASN A ND2 1 
ATOM   46   N  N   . PHE A 1 12  ? 36.178  -2.865  22.343 1.00 64.57  ? 12  PHE A N   1 
ATOM   47   C  CA  . PHE A 1 12  ? 34.972  -3.383  23.020 1.00 60.52  ? 12  PHE A CA  1 
ATOM   48   C  C   . PHE A 1 12  ? 33.980  -3.856  21.967 1.00 61.90  ? 12  PHE A C   1 
ATOM   49   O  O   . PHE A 1 12  ? 33.616  -3.107  21.043 1.00 60.81  ? 12  PHE A O   1 
ATOM   50   C  CB  . PHE A 1 12  ? 34.336  -2.303  23.884 1.00 59.15  ? 12  PHE A CB  1 
ATOM   51   C  CG  . PHE A 1 12  ? 35.213  -1.751  24.974 1.00 57.40  ? 12  PHE A CG  1 
ATOM   52   C  CD1 . PHE A 1 12  ? 35.384  -2.444  26.151 1.00 59.74  ? 12  PHE A CD1 1 
ATOM   53   C  CD2 . PHE A 1 12  ? 35.823  -0.521  24.842 1.00 59.29  ? 12  PHE A CD2 1 
ATOM   54   C  CE1 . PHE A 1 12  ? 36.181  -1.933  27.162 1.00 66.72  ? 12  PHE A CE1 1 
ATOM   55   C  CE2 . PHE A 1 12  ? 36.600  -0.002  25.865 1.00 62.66  ? 12  PHE A CE2 1 
ATOM   56   C  CZ  . PHE A 1 12  ? 36.788  -0.712  27.023 1.00 63.17  ? 12  PHE A CZ  1 
ATOM   57   N  N   . ILE A 1 13  ? 33.580  -5.108  22.087 1.00 65.55  ? 13  ILE A N   1 
ATOM   58   C  CA  . ILE A 1 13  ? 32.467  -5.661  21.281 1.00 64.39  ? 13  ILE A CA  1 
ATOM   59   C  C   . ILE A 1 13  ? 31.414  -6.150  22.251 1.00 61.07  ? 13  ILE A C   1 
ATOM   60   O  O   . ILE A 1 13  ? 31.760  -6.927  23.138 1.00 66.54  ? 13  ILE A O   1 
ATOM   61   C  CB  . ILE A 1 13  ? 32.933  -6.793  20.359 1.00 70.65  ? 13  ILE A CB  1 
ATOM   62   C  CG1 . ILE A 1 13  ? 34.048  -6.313  19.422 1.00 71.46  ? 13  ILE A CG1 1 
ATOM   63   C  CG2 . ILE A 1 13  ? 31.722  -7.364  19.622 1.00 67.33  ? 13  ILE A CG2 1 
ATOM   64   C  CD1 . ILE A 1 13  ? 34.516  -7.342  18.403 1.00 73.05  ? 13  ILE A CD1 1 
ATOM   65   N  N   . ILE A 1 14  ? 30.186  -5.691  22.068 1.00 58.81  ? 14  ILE A N   1 
ATOM   66   C  CA  . ILE A 1 14  ? 29.000  -6.281  22.734 1.00 60.03  ? 14  ILE A CA  1 
ATOM   67   C  C   . ILE A 1 14  ? 28.254  -7.098  21.684 1.00 63.67  ? 14  ILE A C   1 
ATOM   68   O  O   . ILE A 1 14  ? 27.749  -6.544  20.696 1.00 59.55  ? 14  ILE A O   1 
ATOM   69   C  CB  . ILE A 1 14  ? 28.112  -5.209  23.377 1.00 60.57  ? 14  ILE A CB  1 
ATOM   70   C  CG1 . ILE A 1 14  ? 28.839  -4.501  24.520 1.00 62.49  ? 14  ILE A CG1 1 
ATOM   71   C  CG2 . ILE A 1 14  ? 26.811  -5.840  23.826 1.00 61.92  ? 14  ILE A CG2 1 
ATOM   72   C  CD1 . ILE A 1 14  ? 27.965  -3.592  25.347 1.00 62.88  ? 14  ILE A CD1 1 
ATOM   73   N  N   . ILE A 1 15  ? 28.217  -8.402  21.881 1.00 70.66  ? 15  ILE A N   1 
ATOM   74   C  CA  . ILE A 1 15  ? 27.434  -9.290  20.995 1.00 67.49  ? 15  ILE A CA  1 
ATOM   75   C  C   . ILE A 1 15  ? 26.125  -9.559  21.721 1.00 69.29  ? 15  ILE A C   1 
ATOM   76   O  O   . ILE A 1 15  ? 26.154  -10.116 22.836 1.00 69.96  ? 15  ILE A O   1 
ATOM   77   C  CB  . ILE A 1 15  ? 28.211  -10.559 20.641 1.00 65.02  ? 15  ILE A CB  1 
ATOM   78   C  CG1 . ILE A 1 15  ? 29.519  -10.229 19.915 1.00 69.36  ? 15  ILE A CG1 1 
ATOM   79   C  CG2 . ILE A 1 15  ? 27.310  -11.455 19.818 1.00 66.41  ? 15  ILE A CG2 1 
ATOM   80   C  CD1 . ILE A 1 15  ? 30.565  -11.344 19.925 1.00 71.10  ? 15  ILE A CD1 1 
ATOM   81   N  N   . LEU A 1 16  ? 25.030  -9.114  21.126 1.00 65.43  ? 16  LEU A N   1 
ATOM   82   C  CA  . LEU A 1 16  ? 23.719  -9.156  21.786 1.00 64.89  ? 16  LEU A CA  1 
ATOM   83   C  C   . LEU A 1 16  ? 22.779  -9.967  20.910 1.00 67.72  ? 16  LEU A C   1 
ATOM   84   O  O   . LEU A 1 16  ? 22.190  -9.416  19.898 1.00 66.07  ? 16  LEU A O   1 
ATOM   85   C  CB  . LEU A 1 16  ? 23.210  -7.736  22.020 1.00 67.75  ? 16  LEU A CB  1 
ATOM   86   C  CG  . LEU A 1 16  ? 21.921  -7.662  22.827 1.00 65.76  ? 16  LEU A CG  1 
ATOM   87   C  CD1 . LEU A 1 16  ? 22.142  -8.248  24.203 1.00 67.04  ? 16  LEU A CD1 1 
ATOM   88   C  CD2 . LEU A 1 16  ? 21.413  -6.239  22.913 1.00 68.92  ? 16  LEU A CD2 1 
ATOM   89   N  N   . ILE A 1 17  ? 22.581  -11.205 21.346 1.00 67.62  ? 17  ILE A N   1 
ATOM   90   C  CA  . ILE A 1 17  ? 21.623  -12.120 20.684 1.00 71.43  ? 17  ILE A CA  1 
ATOM   91   C  C   . ILE A 1 17  ? 20.209  -11.797 21.170 1.00 66.66  ? 17  ILE A C   1 
ATOM   92   O  O   . ILE A 1 17  ? 20.030  -11.469 22.354 1.00 64.18  ? 17  ILE A O   1 
ATOM   93   C  CB  . ILE A 1 17  ? 22.044  -13.569 20.914 1.00 72.60  ? 17  ILE A CB  1 
ATOM   94   C  CG1 . ILE A 1 17  ? 23.549  -13.716 20.721 1.00 75.45  ? 17  ILE A CG1 1 
ATOM   95   C  CG2 . ILE A 1 17  ? 21.263  -14.467 19.970 1.00 83.52  ? 17  ILE A CG2 1 
ATOM   96   C  CD1 . ILE A 1 17  ? 24.028  -13.188 19.375 1.00 85.09  ? 17  ILE A CD1 1 
ATOM   97   N  N   . ASP A 1 18  ? 19.246  -11.876 20.263 1.00 65.45  ? 18  ASP A N   1 
ATOM   98   C  CA  . ASP A 1 18  ? 17.845  -11.490 20.537 1.00 74.43  ? 18  ASP A CA  1 
ATOM   99   C  C   . ASP A 1 18  ? 17.061  -12.704 21.045 1.00 73.04  ? 18  ASP A C   1 
ATOM   100  O  O   . ASP A 1 18  ? 17.053  -13.730 20.342 1.00 81.13  ? 18  ASP A O   1 
ATOM   101  C  CB  . ASP A 1 18  ? 17.209  -10.899 19.284 1.00 76.00  ? 18  ASP A CB  1 
ATOM   102  C  CG  . ASP A 1 18  ? 15.940  -10.136 19.594 1.00 77.77  ? 18  ASP A CG  1 
ATOM   103  O  OD1 . ASP A 1 18  ? 15.645  -9.975  20.821 1.00 60.43  ? 18  ASP A OD1 1 
ATOM   104  O  OD2 . ASP A 1 18  ? 15.280  -9.683  18.599 1.00 92.04  ? 18  ASP A OD2 1 
ATOM   105  N  N   . ASP A 1 19  ? 16.351  -12.566 22.171 1.00 70.51  ? 19  ASP A N   1 
ATOM   106  C  CA  . ASP A 1 19  ? 15.487  -13.671 22.678 1.00 74.11  ? 19  ASP A CA  1 
ATOM   107  C  C   . ASP A 1 19  ? 16.312  -14.957 22.774 1.00 73.60  ? 19  ASP A C   1 
ATOM   108  O  O   . ASP A 1 19  ? 15.823  -16.008 22.316 1.00 70.40  ? 19  ASP A O   1 
ATOM   109  C  CB  . ASP A 1 19  ? 14.232  -13.827 21.816 1.00 75.55  ? 19  ASP A CB  1 
ATOM   110  C  CG  . ASP A 1 19  ? 13.649  -12.494 21.382 1.00 69.32  ? 19  ASP A CG  1 
ATOM   111  O  OD1 . ASP A 1 19  ? 13.646  -11.559 22.209 1.00 63.09  ? 19  ASP A OD1 1 
ATOM   112  O  OD2 . ASP A 1 19  ? 13.211  -12.399 20.221 1.00 74.40  ? 19  ASP A OD2 1 
ATOM   113  N  N   . TYR A 1 20  ? 17.506  -14.869 23.356 1.00 68.45  ? 20  TYR A N   1 
ATOM   114  C  CA  . TYR A 1 20  ? 18.414  -16.033 23.515 1.00 71.95  ? 20  TYR A CA  1 
ATOM   115  C  C   . TYR A 1 20  ? 18.387  -16.484 24.977 1.00 70.35  ? 20  TYR A C   1 
ATOM   116  O  O   . TYR A 1 20  ? 18.927  -15.781 25.845 1.00 69.03  ? 20  TYR A O   1 
ATOM   117  C  CB  . TYR A 1 20  ? 19.837  -15.686 23.061 1.00 70.84  ? 20  TYR A CB  1 
ATOM   118  C  CG  . TYR A 1 20  ? 20.750  -16.871 22.850 1.00 71.52  ? 20  TYR A CG  1 
ATOM   119  C  CD1 . TYR A 1 20  ? 20.366  -17.915 22.015 1.00 76.60  ? 20  TYR A CD1 1 
ATOM   120  C  CD2 . TYR A 1 20  ? 22.000  -16.958 23.457 1.00 71.23  ? 20  TYR A CD2 1 
ATOM   121  C  CE1 . TYR A 1 20  ? 21.180  -19.018 21.800 1.00 72.94  ? 20  TYR A CE1 1 
ATOM   122  C  CE2 . TYR A 1 20  ? 22.835  -18.050 23.242 1.00 72.25  ? 20  TYR A CE2 1 
ATOM   123  C  CZ  . TYR A 1 20  ? 22.419  -19.084 22.412 1.00 76.60  ? 20  TYR A CZ  1 
ATOM   124  O  OH  . TYR A 1 20  ? 23.203  -20.176 22.194 1.00 82.62  ? 20  TYR A OH  1 
ATOM   125  N  N   . GLY A 1 21  ? 17.848  -17.675 25.214 1.00 71.70  ? 21  GLY A N   1 
ATOM   126  C  CA  . GLY A 1 21  ? 17.499  -18.176 26.560 1.00 86.40  ? 21  GLY A CA  1 
ATOM   127  C  C   . GLY A 1 21  ? 18.677  -18.641 27.402 1.00 82.16  ? 21  GLY A C   1 
ATOM   128  O  O   . GLY A 1 21  ? 19.786  -18.956 26.870 1.00 78.05  ? 21  GLY A O   1 
ATOM   129  N  N   . TRP A 1 22  ? 18.444  -18.736 28.705 1.00 77.14  ? 22  TRP A N   1 
ATOM   130  C  CA  . TRP A 1 22  ? 19.545  -19.097 29.633 1.00 78.08  ? 22  TRP A CA  1 
ATOM   131  C  C   . TRP A 1 22  ? 20.184  -20.435 29.280 1.00 79.18  ? 22  TRP A C   1 
ATOM   132  O  O   . TRP A 1 22  ? 21.304  -20.679 29.734 1.00 81.53  ? 22  TRP A O   1 
ATOM   133  C  CB  . TRP A 1 22  ? 19.034  -19.160 31.053 1.00 71.90  ? 22  TRP A CB  1 
ATOM   134  C  CG  . TRP A 1 22  ? 20.111  -19.225 32.081 1.00 66.32  ? 22  TRP A CG  1 
ATOM   135  C  CD1 . TRP A 1 22  ? 21.081  -18.302 32.340 1.00 83.48  ? 22  TRP A CD1 1 
ATOM   136  C  CD2 . TRP A 1 22  ? 20.226  -20.210 33.097 1.00 74.13  ? 22  TRP A CD2 1 
ATOM   137  N  NE1 . TRP A 1 22  ? 21.813  -18.654 33.434 1.00 86.75  ? 22  TRP A NE1 1 
ATOM   138  C  CE2 . TRP A 1 22  ? 21.300  -19.824 33.921 1.00 86.19  ? 22  TRP A CE2 1 
ATOM   139  C  CE3 . TRP A 1 22  ? 19.518  -21.368 33.390 1.00 69.55  ? 22  TRP A CE3 1 
ATOM   140  C  CZ2 . TRP A 1 22  ? 21.692  -20.581 35.013 1.00 84.13  ? 22  TRP A CZ2 1 
ATOM   141  C  CZ3 . TRP A 1 22  ? 19.917  -22.109 34.468 1.00 70.85  ? 22  TRP A CZ3 1 
ATOM   142  C  CH2 . TRP A 1 22  ? 20.985  -21.724 35.263 1.00 72.30  ? 22  TRP A CH2 1 
ATOM   143  N  N   . THR A 1 23  ? 19.431  -21.296 28.601 1.00 95.47  ? 23  THR A N   1 
ATOM   144  C  CA  . THR A 1 23  ? 19.784  -22.716 28.363 1.00 96.16  ? 23  THR A CA  1 
ATOM   145  C  C   . THR A 1 23  ? 19.766  -22.984 26.872 1.00 93.85  ? 23  THR A C   1 
ATOM   146  O  O   . THR A 1 23  ? 19.466  -24.110 26.519 1.00 91.85  ? 23  THR A O   1 
ATOM   147  C  CB  . THR A 1 23  ? 18.784  -23.657 29.040 1.00 95.83  ? 23  THR A CB  1 
ATOM   148  O  OG1 . THR A 1 23  ? 17.505  -23.509 28.412 1.00 85.76  ? 23  THR A OG1 1 
ATOM   149  C  CG2 . THR A 1 23  ? 18.689  -23.386 30.525 1.00 101.54 ? 23  THR A CG2 1 
ATOM   150  N  N   . ASP A 1 24  ? 20.040  -21.976 26.049 1.00 97.22  ? 24  ASP A N   1 
ATOM   151  C  CA  . ASP A 1 24  ? 19.937  -22.113 24.576 1.00 84.69  ? 24  ASP A CA  1 
ATOM   152  C  C   . ASP A 1 24  ? 21.351  -22.220 24.010 1.00 77.75  ? 24  ASP A C   1 
ATOM   153  O  O   . ASP A 1 24  ? 21.514  -22.082 22.811 1.00 78.74  ? 24  ASP A O   1 
ATOM   154  C  CB  . ASP A 1 24  ? 19.113  -20.976 23.966 1.00 91.11  ? 24  ASP A CB  1 
ATOM   155  C  CG  . ASP A 1 24  ? 17.615  -21.050 24.233 1.00 94.35  ? 24  ASP A CG  1 
ATOM   156  O  OD1 . ASP A 1 24  ? 17.175  -21.727 25.241 1.00 86.14  ? 24  ASP A OD1 1 
ATOM   157  O  OD2 . ASP A 1 24  ? 16.893  -20.404 23.436 1.00 76.13  ? 24  ASP A OD2 1 
ATOM   158  N  N   . SER A 1 25  ? 22.346  -22.456 24.854 1.00 83.40  ? 25  SER A N   1 
ATOM   159  C  CA  . SER A 1 25  ? 23.737  -22.732 24.419 1.00 87.25  ? 25  SER A CA  1 
ATOM   160  C  C   . SER A 1 25  ? 24.168  -24.044 25.057 1.00 85.93  ? 25  SER A C   1 
ATOM   161  O  O   . SER A 1 25  ? 23.615  -24.408 26.113 1.00 104.01 ? 25  SER A O   1 
ATOM   162  C  CB  . SER A 1 25  ? 24.677  -21.599 24.775 1.00 90.73  ? 25  SER A CB  1 
ATOM   163  O  OG  . SER A 1 25  ? 24.406  -21.107 26.084 1.00 94.99  ? 25  SER A OG  1 
ATOM   164  N  N   . THR A 1 26  ? 25.134  -24.717 24.456 1.00 92.72  ? 26  THR A N   1 
ATOM   165  C  CA  . THR A 1 26  ? 25.591  -26.040 24.949 1.00 93.06  ? 26  THR A CA  1 
ATOM   166  C  C   . THR A 1 26  ? 26.265  -25.872 26.320 1.00 87.07  ? 26  THR A C   1 
ATOM   167  O  O   . THR A 1 26  ? 25.966  -26.705 27.183 1.00 94.96  ? 26  THR A O   1 
ATOM   168  C  CB  . THR A 1 26  ? 26.455  -26.776 23.918 1.00 81.91  ? 26  THR A CB  1 
ATOM   169  O  OG1 . THR A 1 26  ? 27.638  -26.001 23.749 1.00 93.83  ? 26  THR A OG1 1 
ATOM   170  C  CG2 . THR A 1 26  ? 25.758  -26.996 22.593 1.00 79.76  ? 26  THR A CG2 1 
ATOM   171  N  N   . CYS A 1 27  ? 27.092  -24.841 26.539 1.00 84.43  ? 27  CYS A N   1 
ATOM   172  C  CA  . CYS A 1 27  ? 27.859  -24.656 27.809 1.00 94.76  ? 27  CYS A CA  1 
ATOM   173  C  C   . CYS A 1 27  ? 26.923  -24.153 28.918 1.00 92.96  ? 27  CYS A C   1 
ATOM   174  O  O   . CYS A 1 27  ? 27.410  -23.837 30.020 1.00 80.67  ? 27  CYS A O   1 
ATOM   175  C  CB  . CYS A 1 27  ? 29.007  -23.673 27.636 1.00 96.03  ? 27  CYS A CB  1 
ATOM   176  S  SG  . CYS A 1 27  ? 28.421  -22.112 26.939 1.00 103.36 ? 27  CYS A SG  1 
ATOM   177  N  N   . TYR A 1 28  ? 25.626  -24.041 28.637 1.00 92.12  ? 28  TYR A N   1 
ATOM   178  C  CA  . TYR A 1 28  ? 24.614  -23.638 29.642 1.00 103.89 ? 28  TYR A CA  1 
ATOM   179  C  C   . TYR A 1 28  ? 23.605  -24.763 29.866 1.00 97.43  ? 28  TYR A C   1 
ATOM   180  O  O   . TYR A 1 28  ? 22.591  -24.514 30.542 1.00 108.19 ? 28  TYR A O   1 
ATOM   181  C  CB  . TYR A 1 28  ? 23.908  -22.359 29.198 1.00 114.21 ? 28  TYR A CB  1 
ATOM   182  C  CG  . TYR A 1 28  ? 24.542  -21.103 29.722 1.00 99.27  ? 28  TYR A CG  1 
ATOM   183  C  CD1 . TYR A 1 28  ? 24.547  -20.832 31.075 1.00 88.54  ? 28  TYR A CD1 1 
ATOM   184  C  CD2 . TYR A 1 28  ? 25.128  -20.191 28.864 1.00 95.97  ? 28  TYR A CD2 1 
ATOM   185  C  CE1 . TYR A 1 28  ? 25.111  -19.665 31.555 1.00 93.94  ? 28  TYR A CE1 1 
ATOM   186  C  CE2 . TYR A 1 28  ? 25.707  -19.028 29.334 1.00 88.72  ? 28  TYR A CE2 1 
ATOM   187  C  CZ  . TYR A 1 28  ? 25.691  -18.760 30.685 1.00 80.26  ? 28  TYR A CZ  1 
ATOM   188  O  OH  . TYR A 1 28  ? 26.230  -17.596 31.143 1.00 76.07  ? 28  TYR A OH  1 
ATOM   189  N  N   . GLY A 1 29  ? 23.857  -25.940 29.297 1.00 88.47  ? 29  GLY A N   1 
ATOM   190  C  CA  . GLY A 1 29  ? 23.081  -27.150 29.608 1.00 91.53  ? 29  GLY A CA  1 
ATOM   191  C  C   . GLY A 1 29  ? 22.452  -27.803 28.392 1.00 89.09  ? 29  GLY A C   1 
ATOM   192  O  O   . GLY A 1 29  ? 22.152  -28.993 28.472 1.00 126.08 ? 29  GLY A O   1 
ATOM   193  N  N   . SER A 1 30  ? 22.215  -27.083 27.304 1.00 84.57  ? 30  SER A N   1 
ATOM   194  C  CA  . SER A 1 30  ? 21.446  -27.631 26.163 1.00 85.44  ? 30  SER A CA  1 
ATOM   195  C  C   . SER A 1 30  ? 22.152  -28.868 25.637 1.00 91.07  ? 30  SER A C   1 
ATOM   196  O  O   . SER A 1 30  ? 23.394  -28.909 25.650 1.00 80.39  ? 30  SER A O   1 
ATOM   197  C  CB  . SER A 1 30  ? 21.297  -26.662 25.045 1.00 101.68 ? 30  SER A CB  1 
ATOM   198  O  OG  . SER A 1 30  ? 20.539  -27.251 23.994 1.00 92.35  ? 30  SER A OG  1 
ATOM   199  N  N   . THR A 1 31  ? 21.377  -29.821 25.144 1.00 103.25 ? 31  THR A N   1 
ATOM   200  C  CA  . THR A 1 31  ? 21.923  -31.007 24.435 1.00 97.94  ? 31  THR A CA  1 
ATOM   201  C  C   . THR A 1 31  ? 21.476  -30.979 22.976 1.00 93.59  ? 31  THR A C   1 
ATOM   202  O  O   . THR A 1 31  ? 22.026  -31.772 22.212 1.00 96.77  ? 31  THR A O   1 
ATOM   203  C  CB  . THR A 1 31  ? 21.473  -32.309 25.098 1.00 89.49  ? 31  THR A CB  1 
ATOM   204  O  OG1 . THR A 1 31  ? 20.090  -32.415 24.746 1.00 79.51  ? 31  THR A OG1 1 
ATOM   205  C  CG2 . THR A 1 31  ? 21.712  -32.319 26.594 1.00 81.21  ? 31  THR A CG2 1 
ATOM   206  N  N   . PHE A 1 32  ? 20.492  -30.138 22.632 1.00 90.71  ? 32  PHE A N   1 
ATOM   207  C  CA  . PHE A 1 32  ? 19.932  -30.015 21.261 1.00 91.27  ? 32  PHE A CA  1 
ATOM   208  C  C   . PHE A 1 32  ? 20.825  -29.057 20.481 1.00 91.04  ? 32  PHE A C   1 
ATOM   209  O  O   . PHE A 1 32  ? 21.559  -29.495 19.589 1.00 96.19  ? 32  PHE A O   1 
ATOM   210  C  CB  . PHE A 1 32  ? 18.469  -29.547 21.297 1.00 90.94  ? 32  PHE A CB  1 
ATOM   211  C  CG  . PHE A 1 32  ? 17.704  -29.693 20.007 1.00 94.95  ? 32  PHE A CG  1 
ATOM   212  C  CD1 . PHE A 1 32  ? 17.995  -30.709 19.107 1.00 107.06 ? 32  PHE A CD1 1 
ATOM   213  C  CD2 . PHE A 1 32  ? 16.664  -28.825 19.704 1.00 103.89 ? 32  PHE A CD2 1 
ATOM   214  C  CE1 . PHE A 1 32  ? 17.272  -30.841 17.930 1.00 118.79 ? 32  PHE A CE1 1 
ATOM   215  C  CE2 . PHE A 1 32  ? 15.949  -28.949 18.520 1.00 103.77 ? 32  PHE A CE2 1 
ATOM   216  C  CZ  . PHE A 1 32  ? 16.254  -29.955 17.634 1.00 110.98 ? 32  PHE A CZ  1 
ATOM   217  N  N   . TYR A 1 33  ? 20.790  -27.791 20.877 1.00 96.40  ? 33  TYR A N   1 
ATOM   218  C  CA  . TYR A 1 33  ? 21.449  -26.663 20.189 1.00 87.57  ? 33  TYR A CA  1 
ATOM   219  C  C   . TYR A 1 33  ? 22.940  -26.942 20.205 1.00 95.99  ? 33  TYR A C   1 
ATOM   220  O  O   . TYR A 1 33  ? 23.383  -27.571 21.220 1.00 80.87  ? 33  TYR A O   1 
ATOM   221  C  CB  . TYR A 1 33  ? 21.076  -25.382 20.924 1.00 79.84  ? 33  TYR A CB  1 
ATOM   222  C  CG  . TYR A 1 33  ? 19.590  -25.205 21.073 1.00 71.68  ? 33  TYR A CG  1 
ATOM   223  C  CD1 . TYR A 1 33  ? 18.737  -25.487 20.021 1.00 70.79  ? 33  TYR A CD1 1 
ATOM   224  C  CD2 . TYR A 1 33  ? 19.035  -24.733 22.247 1.00 69.83  ? 33  TYR A CD2 1 
ATOM   225  C  CE1 . TYR A 1 33  ? 17.367  -25.318 20.144 1.00 73.35  ? 33  TYR A CE1 1 
ATOM   226  C  CE2 . TYR A 1 33  ? 17.670  -24.536 22.380 1.00 73.22  ? 33  TYR A CE2 1 
ATOM   227  C  CZ  . TYR A 1 33  ? 16.828  -24.846 21.332 1.00 73.02  ? 33  TYR A CZ  1 
ATOM   228  O  OH  . TYR A 1 33  ? 15.480  -24.670 21.481 1.00 73.09  ? 33  TYR A OH  1 
ATOM   229  N  N   . GLU A 1 34  ? 23.648  -26.518 19.149 1.00 93.95  ? 34  GLU A N   1 
ATOM   230  C  CA  . GLU A 1 34  ? 25.106  -26.780 19.019 1.00 98.40  ? 34  GLU A CA  1 
ATOM   231  C  C   . GLU A 1 34  ? 25.851  -25.457 18.852 1.00 83.67  ? 34  GLU A C   1 
ATOM   232  O  O   . GLU A 1 34  ? 25.783  -24.870 17.743 1.00 86.42  ? 34  GLU A O   1 
ATOM   233  C  CB  . GLU A 1 34  ? 25.370  -27.727 17.850 1.00 116.37 ? 34  GLU A CB  1 
ATOM   234  C  CG  . GLU A 1 34  ? 24.788  -29.126 18.033 1.00 113.44 ? 34  GLU A CG  1 
ATOM   235  C  CD  . GLU A 1 34  ? 24.822  -29.969 16.767 1.00 109.52 ? 34  GLU A CD  1 
ATOM   236  O  OE1 . GLU A 1 34  ? 25.360  -29.480 15.761 1.00 115.44 ? 34  GLU A OE1 1 
ATOM   237  O  OE2 . GLU A 1 34  ? 24.304  -31.100 16.778 1.00 101.96 ? 34  GLU A OE2 1 
ATOM   238  N  N   . THR A 1 35  ? 26.587  -25.048 19.887 1.00 76.21  ? 35  THR A N   1 
ATOM   239  C  CA  . THR A 1 35  ? 27.190  -23.688 19.997 1.00 84.46  ? 35  THR A CA  1 
ATOM   240  C  C   . THR A 1 35  ? 28.682  -23.759 20.324 1.00 86.22  ? 35  THR A C   1 
ATOM   241  O  O   . THR A 1 35  ? 29.143  -23.224 21.341 1.00 72.07  ? 35  THR A O   1 
ATOM   242  C  CB  . THR A 1 35  ? 26.422  -22.837 21.009 1.00 81.05  ? 35  THR A CB  1 
ATOM   243  O  OG1 . THR A 1 35  ? 26.496  -23.409 22.316 1.00 79.80  ? 35  THR A OG1 1 
ATOM   244  C  CG2 . THR A 1 35  ? 24.973  -22.713 20.605 1.00 85.06  ? 35  THR A CG2 1 
ATOM   245  N  N   . PRO A 1 36  ? 29.489  -24.359 19.418 1.00 84.61  ? 36  PRO A N   1 
ATOM   246  C  CA  . PRO A 1 36  ? 30.883  -24.667 19.742 1.00 80.09  ? 36  PRO A CA  1 
ATOM   247  C  C   . PRO A 1 36  ? 31.740  -23.406 19.932 1.00 77.45  ? 36  PRO A C   1 
ATOM   248  O  O   . PRO A 1 36  ? 32.652  -23.396 20.765 1.00 77.81  ? 36  PRO A O   1 
ATOM   249  C  CB  . PRO A 1 36  ? 31.340  -25.522 18.548 1.00 79.63  ? 36  PRO A CB  1 
ATOM   250  C  CG  . PRO A 1 36  ? 30.377  -25.193 17.414 1.00 74.79  ? 36  PRO A CG  1 
ATOM   251  C  CD  . PRO A 1 36  ? 29.082  -24.777 18.059 1.00 74.95  ? 36  PRO A CD  1 
ATOM   252  N  N   . ASN A 1 37  ? 31.442  -22.359 19.168 1.00 77.15  ? 37  ASN A N   1 
ATOM   253  C  CA  . ASN A 1 37  ? 32.223  -21.097 19.230 1.00 82.77  ? 37  ASN A CA  1 
ATOM   254  C  C   . ASN A 1 37  ? 31.943  -20.356 20.526 1.00 88.65  ? 37  ASN A C   1 
ATOM   255  O  O   . ASN A 1 37  ? 32.918  -19.916 21.171 1.00 86.85  ? 37  ASN A O   1 
ATOM   256  C  CB  . ASN A 1 37  ? 31.895  -20.169 18.080 1.00 76.56  ? 37  ASN A CB  1 
ATOM   257  C  CG  . ASN A 1 37  ? 32.506  -20.737 16.839 1.00 70.47  ? 37  ASN A CG  1 
ATOM   258  O  OD1 . ASN A 1 37  ? 33.722  -20.726 16.699 1.00 77.19  ? 37  ASN A OD1 1 
ATOM   259  N  ND2 . ASN A 1 37  ? 31.665  -21.292 15.998 1.00 70.96  ? 37  ASN A ND2 1 
ATOM   260  N  N   . ILE A 1 38  ? 30.661  -20.211 20.861 1.00 80.43  ? 38  ILE A N   1 
ATOM   261  C  CA  . ILE A 1 38  ? 30.233  -19.586 22.139 1.00 77.38  ? 38  ILE A CA  1 
ATOM   262  C  C   . ILE A 1 38  ? 30.886  -20.376 23.274 1.00 84.79  ? 38  ILE A C   1 
ATOM   263  O  O   . ILE A 1 38  ? 31.329  -19.745 24.254 1.00 79.04  ? 38  ILE A O   1 
ATOM   264  C  CB  . ILE A 1 38  ? 28.705  -19.537 22.254 1.00 75.56  ? 38  ILE A CB  1 
ATOM   265  C  CG1 . ILE A 1 38  ? 28.111  -18.650 21.163 1.00 82.00  ? 38  ILE A CG1 1 
ATOM   266  C  CG2 . ILE A 1 38  ? 28.298  -19.048 23.632 1.00 79.77  ? 38  ILE A CG2 1 
ATOM   267  C  CD1 . ILE A 1 38  ? 26.613  -18.748 21.025 1.00 83.19  ? 38  ILE A CD1 1 
ATOM   268  N  N   . ASP A 1 39  ? 30.984  -21.700 23.133 1.00 88.85  ? 39  ASP A N   1 
ATOM   269  C  CA  . ASP A 1 39  ? 31.675  -22.544 24.138 1.00 89.48  ? 39  ASP A CA  1 
ATOM   270  C  C   . ASP A 1 39  ? 33.138  -22.130 24.209 1.00 83.26  ? 39  ASP A C   1 
ATOM   271  O  O   . ASP A 1 39  ? 33.600  -21.946 25.370 1.00 72.31  ? 39  ASP A O   1 
ATOM   272  C  CB  . ASP A 1 39  ? 31.553  -24.028 23.833 1.00 103.81 ? 39  ASP A CB  1 
ATOM   273  C  CG  . ASP A 1 39  ? 30.147  -24.524 24.065 1.00 113.20 ? 39  ASP A CG  1 
ATOM   274  O  OD1 . ASP A 1 39  ? 29.256  -23.681 24.298 1.00 113.06 ? 39  ASP A OD1 1 
ATOM   275  O  OD2 . ASP A 1 39  ? 29.959  -25.740 24.009 1.00 138.80 ? 39  ASP A OD2 1 
ATOM   276  N  N   . ARG A 1 40  ? 33.818  -21.981 23.050 1.00 69.70  ? 40  ARG A N   1 
ATOM   277  C  CA  . ARG A 1 40  ? 35.263  -21.625 23.056 1.00 75.19  ? 40  ARG A CA  1 
ATOM   278  C  C   . ARG A 1 40  ? 35.390  -20.303 23.824 1.00 74.87  ? 40  ARG A C   1 
ATOM   279  O  O   . ARG A 1 40  ? 36.329  -20.169 24.681 1.00 62.14  ? 40  ARG A O   1 
ATOM   280  C  CB  . ARG A 1 40  ? 35.922  -21.604 21.667 1.00 82.05  ? 40  ARG A CB  1 
ATOM   281  C  CG  . ARG A 1 40  ? 37.454  -21.464 21.711 1.00 94.21  ? 40  ARG A CG  1 
ATOM   282  C  CD  . ARG A 1 40  ? 38.189  -21.422 20.376 1.00 101.42 ? 40  ARG A CD  1 
ATOM   283  N  NE  . ARG A 1 40  ? 37.583  -22.435 19.525 1.00 130.26 ? 40  ARG A NE  1 
ATOM   284  C  CZ  . ARG A 1 40  ? 36.680  -22.232 18.548 1.00 129.21 ? 40  ARG A CZ  1 
ATOM   285  N  NH1 . ARG A 1 40  ? 36.267  -21.016 18.210 1.00 125.96 ? 40  ARG A NH1 1 
ATOM   286  N  NH2 . ARG A 1 40  ? 36.197  -23.278 17.893 1.00 123.13 ? 40  ARG A NH2 1 
ATOM   287  N  N   . LEU A 1 41  ? 34.451  -19.383 23.591 1.00 73.23  ? 41  LEU A N   1 
ATOM   288  C  CA  . LEU A 1 41  ? 34.477  -18.057 24.258 1.00 78.07  ? 41  LEU A CA  1 
ATOM   289  C  C   . LEU A 1 41  ? 34.387  -18.254 25.774 1.00 76.81  ? 41  LEU A C   1 
ATOM   290  O  O   . LEU A 1 41  ? 35.118  -17.566 26.523 1.00 61.85  ? 41  LEU A O   1 
ATOM   291  C  CB  . LEU A 1 41  ? 33.328  -17.196 23.736 1.00 77.95  ? 41  LEU A CB  1 
ATOM   292  C  CG  . LEU A 1 41  ? 33.422  -15.716 24.098 1.00 77.72  ? 41  LEU A CG  1 
ATOM   293  C  CD1 . LEU A 1 41  ? 34.645  -15.058 23.464 1.00 82.63  ? 41  LEU A CD1 1 
ATOM   294  C  CD2 . LEU A 1 41  ? 32.162  -15.009 23.662 1.00 83.74  ? 41  LEU A CD2 1 
ATOM   295  N  N   . ALA A 1 42  ? 33.529  -19.174 26.212 1.00 77.61  ? 42  ALA A N   1 
ATOM   296  C  CA  . ALA A 1 42  ? 33.334  -19.460 27.645 1.00 79.22  ? 42  ALA A CA  1 
ATOM   297  C  C   . ALA A 1 42  ? 34.662  -19.980 28.194 1.00 75.43  ? 42  ALA A C   1 
ATOM   298  O  O   . ALA A 1 42  ? 35.050  -19.526 29.293 1.00 66.00  ? 42  ALA A O   1 
ATOM   299  C  CB  . ALA A 1 42  ? 32.180  -20.416 27.840 1.00 84.16  ? 42  ALA A CB  1 
ATOM   300  N  N   . ARG A 1 43  ? 35.334  -20.863 27.432 1.00 79.57  ? 43  ARG A N   1 
ATOM   301  C  CA  . ARG A 1 43  ? 36.595  -21.541 27.861 1.00 80.75  ? 43  ARG A CA  1 
ATOM   302  C  C   . ARG A 1 43  ? 37.687  -20.486 27.951 1.00 73.80  ? 43  ARG A C   1 
ATOM   303  O  O   . ARG A 1 43  ? 38.529  -20.651 28.848 1.00 64.75  ? 43  ARG A O   1 
ATOM   304  C  CB  . ARG A 1 43  ? 37.001  -22.720 26.962 1.00 80.96  ? 43  ARG A CB  1 
ATOM   305  C  CG  . ARG A 1 43  ? 35.955  -23.834 26.921 1.00 86.01  ? 43  ARG A CG  1 
ATOM   306  C  CD  . ARG A 1 43  ? 36.417  -25.111 26.282 1.00 76.62  ? 43  ARG A CD  1 
ATOM   307  N  NE  . ARG A 1 43  ? 37.014  -24.838 24.987 1.00 77.05  ? 43  ARG A NE  1 
ATOM   308  C  CZ  . ARG A 1 43  ? 36.399  -24.982 23.810 1.00 84.61  ? 43  ARG A CZ  1 
ATOM   309  N  NH1 . ARG A 1 43  ? 35.133  -25.383 23.773 1.00 73.89  ? 43  ARG A NH1 1 
ATOM   310  N  NH2 . ARG A 1 43  ? 37.057  -24.686 22.685 1.00 91.43  ? 43  ARG A NH2 1 
ATOM   311  N  N   . GLU A 1 44  ? 37.598  -19.438 27.114 1.00 69.85  ? 44  GLU A N   1 
ATOM   312  C  CA  . GLU A 1 44  ? 38.573  -18.318 27.017 1.00 70.38  ? 44  GLU A CA  1 
ATOM   313  C  C   . GLU A 1 44  ? 38.208  -17.195 28.006 1.00 72.00  ? 44  GLU A C   1 
ATOM   314  O  O   . GLU A 1 44  ? 38.907  -16.151 28.023 1.00 74.28  ? 44  GLU A O   1 
ATOM   315  C  CB  . GLU A 1 44  ? 38.601  -17.783 25.581 1.00 72.45  ? 44  GLU A CB  1 
ATOM   316  C  CG  . GLU A 1 44  ? 39.185  -18.744 24.559 1.00 77.55  ? 44  GLU A CG  1 
ATOM   317  C  CD  . GLU A 1 44  ? 39.130  -18.300 23.105 1.00 85.87  ? 44  GLU A CD  1 
ATOM   318  O  OE1 . GLU A 1 44  ? 38.465  -17.290 22.811 1.00 98.44  ? 44  GLU A OE1 1 
ATOM   319  O  OE2 . GLU A 1 44  ? 39.733  -18.990 22.257 1.00 105.17 ? 44  GLU A OE2 1 
ATOM   320  N  N   . GLY A 1 45  ? 37.152  -17.340 28.808 1.00 67.89  ? 45  GLY A N   1 
ATOM   321  C  CA  . GLY A 1 45  ? 36.685  -16.188 29.602 1.00 76.05  ? 45  GLY A CA  1 
ATOM   322  C  C   . GLY A 1 45  ? 35.927  -16.580 30.847 1.00 75.99  ? 45  GLY A C   1 
ATOM   323  O  O   . GLY A 1 45  ? 36.207  -17.670 31.378 1.00 92.52  ? 45  GLY A O   1 
ATOM   324  N  N   . MET A 1 46  ? 35.027  -15.698 31.309 1.00 69.64  ? 46  MET A N   1 
ATOM   325  C  CA  . MET A 1 46  ? 34.196  -15.894 32.533 1.00 67.86  ? 46  MET A CA  1 
ATOM   326  C  C   . MET A 1 46  ? 32.731  -16.036 32.126 1.00 67.15  ? 46  MET A C   1 
ATOM   327  O  O   . MET A 1 46  ? 32.248  -15.163 31.428 1.00 71.68  ? 46  MET A O   1 
ATOM   328  C  CB  . MET A 1 46  ? 34.340  -14.728 33.512 1.00 62.29  ? 46  MET A CB  1 
ATOM   329  C  CG  . MET A 1 46  ? 33.648  -14.930 34.849 1.00 64.16  ? 46  MET A CG  1 
ATOM   330  S  SD  . MET A 1 46  ? 34.177  -13.707 36.126 1.00 77.80  ? 46  MET A SD  1 
ATOM   331  C  CE  . MET A 1 46  ? 35.869  -14.243 36.374 1.00 73.92  ? 46  MET A CE  1 
ATOM   332  N  N   . ARG A 1 47  ? 32.079  -17.127 32.524 1.00 73.30  ? 47  ARG A N   1 
ATOM   333  C  CA  . ARG A 1 47  ? 30.648  -17.378 32.244 1.00 74.15  ? 47  ARG A CA  1 
ATOM   334  C  C   . ARG A 1 47  ? 29.852  -17.050 33.502 1.00 70.18  ? 47  ARG A C   1 
ATOM   335  O  O   . ARG A 1 47  ? 30.265  -17.454 34.570 1.00 71.71  ? 47  ARG A O   1 
ATOM   336  C  CB  . ARG A 1 47  ? 30.446  -18.824 31.808 1.00 82.90  ? 47  ARG A CB  1 
ATOM   337  C  CG  . ARG A 1 47  ? 29.028  -19.122 31.339 1.00 95.14  ? 47  ARG A CG  1 
ATOM   338  C  CD  . ARG A 1 47  ? 28.883  -20.513 30.730 1.00 102.80 ? 47  ARG A CD  1 
ATOM   339  N  NE  . ARG A 1 47  ? 29.489  -21.416 31.684 1.00 104.10 ? 47  ARG A NE  1 
ATOM   340  C  CZ  . ARG A 1 47  ? 28.865  -21.971 32.708 1.00 88.69  ? 47  ARG A CZ  1 
ATOM   341  N  NH1 . ARG A 1 47  ? 27.560  -21.821 32.891 1.00 75.37  ? 47  ARG A NH1 1 
ATOM   342  N  NH2 . ARG A 1 47  ? 29.581  -22.699 33.540 1.00 106.57 ? 47  ARG A NH2 1 
ATOM   343  N  N   . PHE A 1 48  ? 28.763  -16.305 33.373 1.00 73.21  ? 48  PHE A N   1 
ATOM   344  C  CA  . PHE A 1 48  ? 27.968  -15.825 34.525 1.00 78.28  ? 48  PHE A CA  1 
ATOM   345  C  C   . PHE A 1 48  ? 26.670  -16.637 34.587 1.00 85.78  ? 48  PHE A C   1 
ATOM   346  O  O   . PHE A 1 48  ? 25.806  -16.700 33.626 1.00 76.25  ? 48  PHE A O   1 
ATOM   347  C  CB  . PHE A 1 48  ? 27.710  -14.321 34.430 1.00 83.24  ? 48  PHE A CB  1 
ATOM   348  C  CG  . PHE A 1 48  ? 28.875  -13.402 34.701 1.00 70.01  ? 48  PHE A CG  1 
ATOM   349  C  CD1 . PHE A 1 48  ? 29.894  -13.260 33.789 1.00 67.01  ? 48  PHE A CD1 1 
ATOM   350  C  CD2 . PHE A 1 48  ? 28.913  -12.618 35.842 1.00 70.90  ? 48  PHE A CD2 1 
ATOM   351  C  CE1 . PHE A 1 48  ? 30.936  -12.382 34.044 1.00 73.68  ? 48  PHE A CE1 1 
ATOM   352  C  CE2 . PHE A 1 48  ? 29.963  -11.749 36.099 1.00 60.25  ? 48  PHE A CE2 1 
ATOM   353  C  CZ  . PHE A 1 48  ? 30.973  -11.628 35.197 1.00 65.40  ? 48  PHE A CZ  1 
ATOM   354  N  N   . THR A 1 49  ? 26.493  -17.248 35.746 1.00 91.86  ? 49  THR A N   1 
ATOM   355  C  CA  . THR A 1 49  ? 25.389  -18.196 35.988 1.00 82.59  ? 49  THR A CA  1 
ATOM   356  C  C   . THR A 1 49  ? 24.164  -17.381 36.389 1.00 79.27  ? 49  THR A C   1 
ATOM   357  O  O   . THR A 1 49  ? 23.048  -17.854 36.127 1.00 65.45  ? 49  THR A O   1 
ATOM   358  C  CB  . THR A 1 49  ? 25.843  -19.238 37.011 1.00 80.97  ? 49  THR A CB  1 
ATOM   359  O  OG1 . THR A 1 49  ? 26.374  -18.552 38.143 1.00 79.67  ? 49  THR A OG1 1 
ATOM   360  C  CG2 . THR A 1 49  ? 26.911  -20.153 36.464 1.00 85.27  ? 49  THR A CG2 1 
ATOM   361  N  N   . ASN A 1 50  ? 24.381  -16.209 37.002 1.00 87.22  ? 50  ASN A N   1 
ATOM   362  C  CA  . ASN A 1 50  ? 23.268  -15.365 37.497 1.00 86.92  ? 50  ASN A CA  1 
ATOM   363  C  C   . ASN A 1 50  ? 23.260  -14.023 36.773 1.00 83.90  ? 50  ASN A C   1 
ATOM   364  O  O   . ASN A 1 50  ? 23.145  -12.993 37.430 1.00 77.50  ? 50  ASN A O   1 
ATOM   365  C  CB  . ASN A 1 50  ? 23.320  -15.223 39.013 1.00 90.34  ? 50  ASN A CB  1 
ATOM   366  C  CG  . ASN A 1 50  ? 22.862  -16.496 39.679 1.00 82.10  ? 50  ASN A CG  1 
ATOM   367  O  OD1 . ASN A 1 50  ? 23.344  -17.556 39.318 1.00 82.71  ? 50  ASN A OD1 1 
ATOM   368  N  ND2 . ASN A 1 50  ? 21.880  -16.426 40.563 1.00 79.19  ? 50  ASN A ND2 1 
ATOM   369  N  N   . ALA A 1 51  ? 23.285  -14.049 35.447 1.00 82.60  ? 51  ALA A N   1 
ATOM   370  C  CA  . ALA A 1 51  ? 23.224  -12.809 34.658 1.00 70.65  ? 51  ALA A CA  1 
ATOM   371  C  C   . ALA A 1 51  ? 21.767  -12.551 34.314 1.00 69.79  ? 51  ALA A C   1 
ATOM   372  O  O   . ALA A 1 51  ? 21.053  -13.517 33.929 1.00 66.46  ? 51  ALA A O   1 
ATOM   373  C  CB  . ALA A 1 51  ? 24.057  -12.932 33.423 1.00 78.24  ? 51  ALA A CB  1 
ATOM   374  N  N   . TYR A 1 52  ? 21.372  -11.285 34.410 1.00 63.80  ? 52  TYR A N   1 
ATOM   375  C  CA  . TYR A 1 52  ? 19.996  -10.842 34.110 1.00 64.52  ? 52  TYR A CA  1 
ATOM   376  C  C   . TYR A 1 52  ? 19.944  -9.745  33.048 1.00 64.79  ? 52  TYR A C   1 
ATOM   377  O  O   . TYR A 1 52  ? 20.857  -8.918  32.913 1.00 65.94  ? 52  TYR A O   1 
ATOM   378  C  CB  . TYR A 1 52  ? 19.348  -10.351 35.391 1.00 63.98  ? 52  TYR A CB  1 
ATOM   379  C  CG  . TYR A 1 52  ? 19.075  -11.460 36.357 1.00 69.54  ? 52  TYR A CG  1 
ATOM   380  C  CD1 . TYR A 1 52  ? 17.901  -12.184 36.301 1.00 71.37  ? 52  TYR A CD1 1 
ATOM   381  C  CD2 . TYR A 1 52  ? 20.019  -11.806 37.300 1.00 76.46  ? 52  TYR A CD2 1 
ATOM   382  C  CE1 . TYR A 1 52  ? 17.653  -13.204 37.201 1.00 82.24  ? 52  TYR A CE1 1 
ATOM   383  C  CE2 . TYR A 1 52  ? 19.786  -12.829 38.199 1.00 82.91  ? 52  TYR A CE2 1 
ATOM   384  C  CZ  . TYR A 1 52  ? 18.600  -13.533 38.153 1.00 81.73  ? 52  TYR A CZ  1 
ATOM   385  O  OH  . TYR A 1 52  ? 18.390  -14.541 39.045 1.00 88.81  ? 52  TYR A OH  1 
ATOM   386  N  N   . ALA A 1 53  ? 18.834  -9.745  32.321 1.00 67.39  ? 53  ALA A N   1 
ATOM   387  C  CA  . ALA A 1 53  ? 18.344  -8.624  31.490 1.00 69.56  ? 53  ALA A CA  1 
ATOM   388  C  C   . ALA A 1 53  ? 17.405  -7.779  32.342 1.00 70.86  ? 53  ALA A C   1 
ATOM   389  O  O   . ALA A 1 53  ? 16.610  -8.356  33.105 1.00 71.16  ? 53  ALA A O   1 
ATOM   390  C  CB  . ALA A 1 53  ? 17.628  -9.146  30.279 1.00 70.79  ? 53  ALA A CB  1 
ATOM   391  N  N   . ALA A 1 54  ? 17.454  -6.464  32.180 1.00 73.51  ? 54  ALA A N   1 
ATOM   392  C  CA  . ALA A 1 54  ? 16.791  -5.506  33.095 1.00 72.02  ? 54  ALA A CA  1 
ATOM   393  C  C   . ALA A 1 54  ? 15.283  -5.449  32.845 1.00 64.56  ? 54  ALA A C   1 
ATOM   394  O  O   . ALA A 1 54  ? 14.576  -4.730  33.604 1.00 66.82  ? 54  ALA A O   1 
ATOM   395  C  CB  . ALA A 1 54  ? 17.418  -4.168  32.908 1.00 79.26  ? 54  ALA A CB  1 
ATOM   396  N  N   . CYS A 1 55  ? 14.832  -6.185  31.830 1.00 61.61  ? 55  CYS A N   1 
ATOM   397  C  CA  . CYS A 1 55  ? 13.433  -6.245  31.365 1.00 65.72  ? 55  CYS A CA  1 
ATOM   398  C  C   . CYS A 1 55  ? 13.258  -7.535  30.577 1.00 67.79  ? 55  CYS A C   1 
ATOM   399  O  O   . CYS A 1 55  ? 14.160  -7.937  29.853 1.00 66.70  ? 55  CYS A O   1 
ATOM   400  C  CB  . CYS A 1 55  ? 13.115  -5.037  30.494 1.00 69.03  ? 55  CYS A CB  1 
ATOM   401  S  SG  . CYS A 1 55  ? 11.504  -5.104  29.669 1.00 74.55  ? 55  CYS A SG  1 
ATOM   402  N  N   . PRO A 1 56  ? 12.091  -8.203  30.686 1.00 65.22  ? 56  PRO A N   1 
ATOM   403  C  CA  . PRO A 1 56  ? 11.834  -9.441  29.958 1.00 65.11  ? 56  PRO A CA  1 
ATOM   404  C  C   . PRO A 1 56  ? 11.368  -9.304  28.501 1.00 68.37  ? 56  PRO A C   1 
ATOM   405  O  O   . PRO A 1 56  ? 10.999  -10.311 27.915 1.00 70.42  ? 56  PRO A O   1 
ATOM   406  C  CB  . PRO A 1 56  ? 10.702  -10.036 30.801 1.00 73.82  ? 56  PRO A CB  1 
ATOM   407  C  CG  . PRO A 1 56  ? 9.898   -8.825  31.232 1.00 72.54  ? 56  PRO A CG  1 
ATOM   408  C  CD  . PRO A 1 56  ? 10.967  -7.809  31.547 1.00 68.30  ? 56  PRO A CD  1 
ATOM   409  N  N   . VAL A 1 57  ? 11.391  -8.097  27.939 1.00 70.68  ? 57  VAL A N   1 
ATOM   410  C  CA  . VAL A 1 57  ? 11.168  -7.903  26.477 1.00 72.37  ? 57  VAL A CA  1 
ATOM   411  C  C   . VAL A 1 57  ? 12.234  -6.939  25.928 1.00 72.26  ? 57  VAL A C   1 
ATOM   412  O  O   . VAL A 1 57  ? 12.945  -6.294  26.750 1.00 64.09  ? 57  VAL A O   1 
ATOM   413  C  CB  . VAL A 1 57  ? 9.727   -7.449  26.199 1.00 74.06  ? 57  VAL A CB  1 
ATOM   414  C  CG1 . VAL A 1 57  ? 8.726   -8.488  26.650 1.00 77.99  ? 57  VAL A CG1 1 
ATOM   415  C  CG2 . VAL A 1 57  ? 9.409   -6.135  26.873 1.00 85.70  ? 57  VAL A CG2 1 
ATOM   416  N  N   . CYS A 1 58  ? 12.308  -6.859  24.594 1.00 65.59  ? 58  CYS A N   1 
ATOM   417  C  CA  . CYS A 1 58  ? 13.453  -6.381  23.778 1.00 67.49  ? 58  CYS A CA  1 
ATOM   418  C  C   . CYS A 1 58  ? 13.861  -4.924  24.115 1.00 69.71  ? 58  CYS A C   1 
ATOM   419  O  O   . CYS A 1 58  ? 14.929  -4.730  24.706 1.00 69.48  ? 58  CYS A O   1 
ATOM   420  C  CB  . CYS A 1 58  ? 13.115  -6.516  22.294 1.00 77.12  ? 58  CYS A CB  1 
ATOM   421  S  SG  . CYS A 1 58  ? 12.389  -8.102  21.770 1.00 80.47  ? 58  CYS A SG  1 
ATOM   422  N  N   . SER A 1 59  ? 13.077  -3.912  23.743 1.00 64.53  ? 59  SER A N   1 
ATOM   423  C  CA  . SER A 1 59  ? 13.528  -2.495  23.699 1.00 63.81  ? 59  SER A CA  1 
ATOM   424  C  C   . SER A 1 59  ? 14.158  -2.054  25.021 1.00 62.72  ? 59  SER A C   1 
ATOM   425  O  O   . SER A 1 59  ? 15.287  -1.585  25.047 1.00 64.09  ? 59  SER A O   1 
ATOM   426  C  CB  . SER A 1 59  ? 12.416  -1.572  23.280 1.00 62.30  ? 59  SER A CB  1 
ATOM   427  O  OG  . SER A 1 59  ? 11.977  -1.861  21.951 1.00 58.31  ? 59  SER A OG  1 
ATOM   428  N  N   . PRO A 1 60  ? 13.490  -2.168  26.181 1.00 60.75  ? 60  PRO A N   1 
ATOM   429  C  CA  . PRO A 1 60  ? 14.050  -1.613  27.408 1.00 58.72  ? 60  PRO A CA  1 
ATOM   430  C  C   . PRO A 1 60  ? 15.389  -2.218  27.844 1.00 60.89  ? 60  PRO A C   1 
ATOM   431  O  O   . PRO A 1 60  ? 16.206  -1.527  28.411 1.00 60.76  ? 60  PRO A O   1 
ATOM   432  C  CB  . PRO A 1 60  ? 12.985  -1.921  28.458 1.00 61.47  ? 60  PRO A CB  1 
ATOM   433  C  CG  . PRO A 1 60  ? 11.717  -2.049  27.645 1.00 66.72  ? 60  PRO A CG  1 
ATOM   434  C  CD  . PRO A 1 60  ? 12.170  -2.769  26.392 1.00 63.76  ? 60  PRO A CD  1 
ATOM   435  N  N   . THR A 1 61  ? 15.622  -3.497  27.586 1.00 63.47  ? 61  THR A N   1 
ATOM   436  C  CA  . THR A 1 61  ? 16.922  -4.092  27.971 1.00 61.69  ? 61  THR A CA  1 
ATOM   437  C  C   . THR A 1 61  ? 18.008  -3.411  27.139 1.00 62.79  ? 61  THR A C   1 
ATOM   438  O  O   . THR A 1 61  ? 19.060  -3.067  27.725 1.00 61.91  ? 61  THR A O   1 
ATOM   439  C  CB  . THR A 1 61  ? 16.931  -5.615  27.848 1.00 63.74  ? 61  THR A CB  1 
ATOM   440  O  OG1 . THR A 1 61  ? 15.975  -6.131  28.775 1.00 66.95  ? 61  THR A OG1 1 
ATOM   441  C  CG2 . THR A 1 61  ? 18.291  -6.206  28.153 1.00 70.07  ? 61  THR A CG2 1 
ATOM   442  N  N   . ARG A 1 62  ? 17.742  -3.205  25.844 1.00 65.57  ? 62  ARG A N   1 
ATOM   443  C  CA  . ARG A 1 62  ? 18.687  -2.566  24.890 1.00 62.08  ? 62  ARG A CA  1 
ATOM   444  C  C   . ARG A 1 62  ? 18.930  -1.139  25.392 1.00 60.62  ? 62  ARG A C   1 
ATOM   445  O  O   . ARG A 1 62  ? 20.113  -0.723  25.521 1.00 62.59  ? 62  ARG A O   1 
ATOM   446  C  CB  . ARG A 1 62  ? 18.151  -2.673  23.456 1.00 65.33  ? 62  ARG A CB  1 
ATOM   447  C  CG  . ARG A 1 62  ? 18.050  -4.114  22.980 1.00 67.41  ? 62  ARG A CG  1 
ATOM   448  C  CD  . ARG A 1 62  ? 17.000  -4.476  21.950 1.00 70.12  ? 62  ARG A CD  1 
ATOM   449  N  NE  . ARG A 1 62  ? 17.171  -5.878  21.555 1.00 70.21  ? 62  ARG A NE  1 
ATOM   450  C  CZ  . ARG A 1 62  ? 18.122  -6.316  20.726 1.00 78.34  ? 62  ARG A CZ  1 
ATOM   451  N  NH1 . ARG A 1 62  ? 18.947  -5.435  20.184 1.00 87.84  ? 62  ARG A NH1 1 
ATOM   452  N  NH2 . ARG A 1 62  ? 18.252  -7.607  20.432 1.00 70.51  ? 62  ARG A NH2 1 
ATOM   453  N  N   . ALA A 1 63  ? 17.874  -0.435  25.778 1.00 53.88  ? 63  ALA A N   1 
ATOM   454  C  CA  . ALA A 1 63  ? 18.044  0.898   26.389 1.00 60.61  ? 63  ALA A CA  1 
ATOM   455  C  C   . ALA A 1 63  ? 18.895  0.801   27.675 1.00 53.61  ? 63  ALA A C   1 
ATOM   456  O  O   . ALA A 1 63  ? 19.750  1.660   27.900 1.00 46.36  ? 63  ALA A O   1 
ATOM   457  C  CB  . ALA A 1 63  ? 16.689  1.514   26.608 1.00 65.26  ? 63  ALA A CB  1 
ATOM   458  N  N   . SER A 1 64  ? 18.706  -0.242  28.473 1.00 56.00  ? 64  SER A N   1 
ATOM   459  C  CA  . SER A 1 64  ? 19.452  -0.431  29.740 1.00 62.59  ? 64  SER A CA  1 
ATOM   460  C  C   . SER A 1 64  ? 20.936  -0.542  29.468 1.00 61.74  ? 64  SER A C   1 
ATOM   461  O  O   . SER A 1 64  ? 21.743  0.139   30.160 1.00 67.87  ? 64  SER A O   1 
ATOM   462  C  CB  . SER A 1 64  ? 18.998  -1.614  30.500 1.00 62.46  ? 64  SER A CB  1 
ATOM   463  O  OG  . SER A 1 64  ? 18.320  -1.134  31.636 1.00 82.36  ? 64  SER A OG  1 
ATOM   464  N  N   . ILE A 1 65  ? 21.271  -1.406  28.521 1.00 65.80  ? 65  ILE A N   1 
ATOM   465  C  CA  . ILE A 1 65  ? 22.689  -1.773  28.252 1.00 69.39  ? 65  ILE A CA  1 
ATOM   466  C  C   . ILE A 1 65  ? 23.474  -0.497  27.984 1.00 71.76  ? 65  ILE A C   1 
ATOM   467  O  O   . ILE A 1 65  ? 24.484  -0.261  28.736 1.00 69.45  ? 65  ILE A O   1 
ATOM   468  C  CB  . ILE A 1 65  ? 22.793  -2.738  27.069 1.00 65.01  ? 65  ILE A CB  1 
ATOM   469  C  CG1 . ILE A 1 65  ? 22.377  -4.150  27.469 1.00 62.51  ? 65  ILE A CG1 1 
ATOM   470  C  CG2 . ILE A 1 65  ? 24.194  -2.711  26.491 1.00 70.44  ? 65  ILE A CG2 1 
ATOM   471  C  CD1 . ILE A 1 65  ? 22.227  -5.075  26.293 1.00 66.47  ? 65  ILE A CD1 1 
ATOM   472  N  N   . LEU A 1 66  ? 22.967  0.255   26.989 1.00 60.93  ? 66  LEU A N   1 
ATOM   473  C  CA  . LEU A 1 66  ? 23.588  1.469   26.420 1.00 57.59  ? 66  LEU A CA  1 
ATOM   474  C  C   . LEU A 1 66  ? 23.653  2.597   27.453 1.00 60.22  ? 66  LEU A C   1 
ATOM   475  O  O   . LEU A 1 66  ? 24.569  3.390   27.328 1.00 73.72  ? 66  LEU A O   1 
ATOM   476  C  CB  . LEU A 1 66  ? 22.772  1.925   25.215 1.00 56.92  ? 66  LEU A CB  1 
ATOM   477  C  CG  . LEU A 1 66  ? 22.779  0.988   24.013 1.00 60.36  ? 66  LEU A CG  1 
ATOM   478  C  CD1 . LEU A 1 66  ? 21.983  1.580   22.854 1.00 58.50  ? 66  LEU A CD1 1 
ATOM   479  C  CD2 . LEU A 1 66  ? 24.196  0.680   23.572 1.00 60.84  ? 66  LEU A CD2 1 
ATOM   480  N  N   . THR A 1 67  ? 22.728  2.714   28.413 1.00 57.24  ? 67  THR A N   1 
ATOM   481  C  CA  . THR A 1 67  ? 22.631  3.927   29.278 1.00 58.54  ? 67  THR A CA  1 
ATOM   482  C  C   . THR A 1 67  ? 23.131  3.715   30.701 1.00 58.37  ? 67  THR A C   1 
ATOM   483  O  O   . THR A 1 67  ? 23.459  4.745   31.367 1.00 60.53  ? 67  THR A O   1 
ATOM   484  C  CB  . THR A 1 67  ? 21.192  4.413   29.365 1.00 59.35  ? 67  THR A CB  1 
ATOM   485  O  OG1 . THR A 1 67  ? 20.390  3.360   29.897 1.00 63.77  ? 67  THR A OG1 1 
ATOM   486  C  CG2 . THR A 1 67  ? 20.696  4.834   28.003 1.00 60.76  ? 67  THR A CG2 1 
ATOM   487  N  N   . GLY A 1 68  ? 23.151  2.454   31.131 1.00 61.11  ? 68  GLY A N   1 
ATOM   488  C  CA  . GLY A 1 68  ? 23.482  2.049   32.506 1.00 67.86  ? 68  GLY A CA  1 
ATOM   489  C  C   . GLY A 1 68  ? 22.384  2.427   33.478 1.00 64.91  ? 68  GLY A C   1 
ATOM   490  O  O   . GLY A 1 68  ? 22.669  2.507   34.680 1.00 65.31  ? 68  GLY A O   1 
ATOM   491  N  N   . LYS A 1 69  ? 21.173  2.625   32.969 1.00 60.57  ? 69  LYS A N   1 
ATOM   492  C  CA  . LYS A 1 69  ? 20.003  3.038   33.766 1.00 61.49  ? 69  LYS A CA  1 
ATOM   493  C  C   . LYS A 1 69  ? 18.920  1.964   33.634 1.00 59.31  ? 69  LYS A C   1 
ATOM   494  O  O   . LYS A 1 69  ? 18.801  1.335   32.573 1.00 52.63  ? 69  LYS A O   1 
ATOM   495  C  CB  . LYS A 1 69  ? 19.556  4.415   33.267 1.00 68.68  ? 69  LYS A CB  1 
ATOM   496  C  CG  . LYS A 1 69  ? 20.334  5.591   33.845 1.00 72.68  ? 69  LYS A CG  1 
ATOM   497  C  CD  . LYS A 1 69  ? 20.111  6.860   33.080 1.00 78.91  ? 69  LYS A CD  1 
ATOM   498  C  CE  . LYS A 1 69  ? 19.711  8.008   33.971 1.00 89.63  ? 69  LYS A CE  1 
ATOM   499  N  NZ  . LYS A 1 69  ? 18.427  8.574   33.500 1.00 101.70 ? 69  LYS A NZ  1 
ATOM   500  N  N   . TYR A 1 70  ? 18.130  1.764   34.686 1.00 63.98  ? 70  TYR A N   1 
ATOM   501  C  CA  . TYR A 1 70  ? 17.043  0.751   34.709 1.00 59.54  ? 70  TYR A CA  1 
ATOM   502  C  C   . TYR A 1 70  ? 15.936  1.272   33.816 1.00 58.06  ? 70  TYR A C   1 
ATOM   503  O  O   . TYR A 1 70  ? 15.758  2.474   33.680 1.00 58.89  ? 70  TYR A O   1 
ATOM   504  C  CB  . TYR A 1 70  ? 16.482  0.513   36.112 1.00 58.75  ? 70  TYR A CB  1 
ATOM   505  C  CG  . TYR A 1 70  ? 17.217  -0.423  37.048 1.00 57.11  ? 70  TYR A CG  1 
ATOM   506  C  CD1 . TYR A 1 70  ? 17.498  -1.744  36.712 1.00 53.51  ? 70  TYR A CD1 1 
ATOM   507  C  CD2 . TYR A 1 70  ? 17.501  -0.014  38.347 1.00 59.62  ? 70  TYR A CD2 1 
ATOM   508  C  CE1 . TYR A 1 70  ? 18.108  -2.613  37.615 1.00 57.48  ? 70  TYR A CE1 1 
ATOM   509  C  CE2 . TYR A 1 70  ? 18.094  -0.873  39.260 1.00 68.48  ? 70  TYR A CE2 1 
ATOM   510  C  CZ  . TYR A 1 70  ? 18.398  -2.183  38.905 1.00 61.26  ? 70  TYR A CZ  1 
ATOM   511  O  OH  . TYR A 1 70  ? 18.965  -2.981  39.877 1.00 53.08  ? 70  TYR A OH  1 
ATOM   512  N  N   . PRO A 1 71  ? 15.176  0.385   33.165 1.00 60.64  ? 71  PRO A N   1 
ATOM   513  C  CA  . PRO A 1 71  ? 14.033  0.788   32.355 1.00 69.28  ? 71  PRO A CA  1 
ATOM   514  C  C   . PRO A 1 71  ? 13.032  1.690   33.081 1.00 64.56  ? 71  PRO A C   1 
ATOM   515  O  O   . PRO A 1 71  ? 12.564  2.611   32.441 1.00 60.05  ? 71  PRO A O   1 
ATOM   516  C  CB  . PRO A 1 71  ? 13.412  -0.555  31.974 1.00 63.49  ? 71  PRO A CB  1 
ATOM   517  C  CG  . PRO A 1 71  ? 14.634  -1.376  31.829 1.00 61.21  ? 71  PRO A CG  1 
ATOM   518  C  CD  . PRO A 1 71  ? 15.394  -1.049  33.099 1.00 63.48  ? 71  PRO A CD  1 
ATOM   519  N  N   . ALA A 1 72  ? 12.757  1.439   34.362 1.00 57.40  ? 72  ALA A N   1 
ATOM   520  C  CA  . ALA A 1 72  ? 11.715  2.203   35.075 1.00 62.12  ? 72  ALA A CA  1 
ATOM   521  C  C   . ALA A 1 72  ? 12.179  3.645   35.199 1.00 60.82  ? 72  ALA A C   1 
ATOM   522  O  O   . ALA A 1 72  ? 11.298  4.526   35.194 1.00 70.60  ? 72  ALA A O   1 
ATOM   523  C  CB  . ALA A 1 72  ? 11.452  1.607   36.420 1.00 66.76  ? 72  ALA A CB  1 
ATOM   524  N  N   . HIS A 1 73  ? 13.504  3.813   35.320 1.00 59.24  ? 73  HIS A N   1 
ATOM   525  C  CA  . HIS A 1 73  ? 14.245  5.094   35.498 1.00 62.31  ? 73  HIS A CA  1 
ATOM   526  C  C   . HIS A 1 73  ? 14.311  5.810   34.148 1.00 59.40  ? 73  HIS A C   1 
ATOM   527  O  O   . HIS A 1 73  ? 14.339  7.019   34.149 1.00 67.44  ? 73  HIS A O   1 
ATOM   528  C  CB  . HIS A 1 73  ? 15.655  4.828   36.074 1.00 61.58  ? 73  HIS A CB  1 
ATOM   529  C  CG  . HIS A 1 73  ? 16.406  6.029   36.539 1.00 59.64  ? 73  HIS A CG  1 
ATOM   530  N  ND1 . HIS A 1 73  ? 17.743  5.972   36.863 1.00 59.89  ? 73  HIS A ND1 1 
ATOM   531  C  CD2 . HIS A 1 73  ? 16.011  7.296   36.776 1.00 67.22  ? 73  HIS A CD2 1 
ATOM   532  C  CE1 . HIS A 1 73  ? 18.140  7.147   37.291 1.00 72.17  ? 73  HIS A CE1 1 
ATOM   533  N  NE2 . HIS A 1 73  ? 17.097  7.986   37.234 1.00 74.62  ? 73  HIS A NE2 1 
ATOM   534  N  N   . LEU A 1 74  ? 14.352  5.065   33.047 1.00 56.12  ? 74  LEU A N   1 
ATOM   535  C  CA  . LEU A 1 74  ? 14.385  5.605   31.670 1.00 52.59  ? 74  LEU A CA  1 
ATOM   536  C  C   . LEU A 1 74  ? 12.972  6.010   31.259 1.00 51.77  ? 74  LEU A C   1 
ATOM   537  O  O   . LEU A 1 74  ? 12.841  6.918   30.454 1.00 54.01  ? 74  LEU A O   1 
ATOM   538  C  CB  . LEU A 1 74  ? 14.963  4.543   30.732 1.00 56.36  ? 74  LEU A CB  1 
ATOM   539  C  CG  . LEU A 1 74  ? 16.473  4.311   30.856 1.00 59.45  ? 74  LEU A CG  1 
ATOM   540  C  CD1 . LEU A 1 74  ? 16.952  3.178   29.954 1.00 60.19  ? 74  LEU A CD1 1 
ATOM   541  C  CD2 . LEU A 1 74  ? 17.243  5.574   30.528 1.00 60.76  ? 74  LEU A CD2 1 
ATOM   542  N  N   . HIS A 1 75  ? 11.959  5.383   31.841 1.00 59.35  ? 75  HIS A N   1 
ATOM   543  C  CA  . HIS A 1 75  ? 10.524  5.489   31.452 1.00 64.13  ? 75  HIS A CA  1 
ATOM   544  C  C   . HIS A 1 75  ? 10.371  4.919   30.044 1.00 61.67  ? 75  HIS A C   1 
ATOM   545  O  O   . HIS A 1 75  ? 9.555   5.387   29.292 1.00 73.68  ? 75  HIS A O   1 
ATOM   546  C  CB  . HIS A 1 75  ? 10.001  6.917   31.675 1.00 66.04  ? 75  HIS A CB  1 
ATOM   547  C  CG  . HIS A 1 75  ? 10.085  7.314   33.107 1.00 71.29  ? 75  HIS A CG  1 
ATOM   548  N  ND1 . HIS A 1 75  ? 11.246  7.823   33.676 1.00 65.34  ? 75  HIS A ND1 1 
ATOM   549  C  CD2 . HIS A 1 75  ? 9.193   7.177   34.110 1.00 84.21  ? 75  HIS A CD2 1 
ATOM   550  C  CE1 . HIS A 1 75  ? 11.048  8.015   34.968 1.00 67.23  ? 75  HIS A CE1 1 
ATOM   551  N  NE2 . HIS A 1 75  ? 9.799   7.620   35.254 1.00 79.52  ? 75  HIS A NE2 1 
ATOM   552  N  N   . LEU A 1 76  ? 11.151  3.897   29.738 1.00 70.10  ? 76  LEU A N   1 
ATOM   553  C  CA  . LEU A 1 76  ? 11.005  3.036   28.545 1.00 67.20  ? 76  LEU A CA  1 
ATOM   554  C  C   . LEU A 1 76  ? 10.917  1.572   29.030 1.00 66.18  ? 76  LEU A C   1 
ATOM   555  O  O   . LEU A 1 76  ? 11.944  1.000   29.397 1.00 65.60  ? 76  LEU A O   1 
ATOM   556  C  CB  . LEU A 1 76  ? 12.239  3.369   27.718 1.00 61.47  ? 76  LEU A CB  1 
ATOM   557  C  CG  . LEU A 1 76  ? 12.468  2.556   26.460 1.00 63.68  ? 76  LEU A CG  1 
ATOM   558  C  CD1 . LEU A 1 76  ? 11.183  1.963   25.938 1.00 70.68  ? 76  LEU A CD1 1 
ATOM   559  C  CD2 . LEU A 1 76  ? 13.113  3.450   25.428 1.00 66.90  ? 76  LEU A CD2 1 
ATOM   560  N  N   . THR A 1 77  ? 9.709   1.035   29.193 1.00 63.29  ? 77  THR A N   1 
ATOM   561  C  CA  . THR A 1 77  ? 9.439   -0.103  30.117 1.00 69.91  ? 77  THR A CA  1 
ATOM   562  C  C   . THR A 1 77  ? 8.820   -1.287  29.370 1.00 66.11  ? 77  THR A C   1 
ATOM   563  O  O   . THR A 1 77  ? 8.849   -2.400  29.942 1.00 73.61  ? 77  THR A O   1 
ATOM   564  C  CB  . THR A 1 77  ? 8.565   0.335   31.305 1.00 70.71  ? 77  THR A CB  1 
ATOM   565  O  OG1 . THR A 1 77  ? 7.513   1.137   30.786 1.00 64.79  ? 77  THR A OG1 1 
ATOM   566  C  CG2 . THR A 1 77  ? 9.292   1.153   32.356 1.00 70.75  ? 77  THR A CG2 1 
ATOM   567  N  N   . ASP A 1 78  ? 8.313   -1.071  28.157 1.00 58.90  ? 78  ASP A N   1 
ATOM   568  C  CA  . ASP A 1 78  ? 7.838   -2.156  27.262 1.00 65.14  ? 78  ASP A CA  1 
ATOM   569  C  C   . ASP A 1 78  ? 8.618   -2.104  25.945 1.00 59.94  ? 78  ASP A C   1 
ATOM   570  O  O   . ASP A 1 78  ? 9.270   -1.119  25.672 1.00 52.17  ? 78  ASP A O   1 
ATOM   571  C  CB  . ASP A 1 78  ? 6.333   -2.040  26.998 1.00 71.95  ? 78  ASP A CB  1 
ATOM   572  C  CG  . ASP A 1 78  ? 5.600   -3.343  26.655 1.00 75.65  ? 78  ASP A CG  1 
ATOM   573  O  OD1 . ASP A 1 78  ? 6.257   -4.388  26.438 1.00 69.51  ? 78  ASP A OD1 1 
ATOM   574  O  OD2 . ASP A 1 78  ? 4.354   -3.306  26.585 1.00 83.09  ? 78  ASP A OD2 1 
ATOM   575  N  N   . TRP A 1 79  ? 8.558   -3.167  25.156 1.00 66.14  ? 79  TRP A N   1 
ATOM   576  C  CA  . TRP A 1 79  ? 9.083   -3.175  23.766 1.00 70.13  ? 79  TRP A CA  1 
ATOM   577  C  C   . TRP A 1 79  ? 8.273   -2.143  22.980 1.00 60.64  ? 79  TRP A C   1 
ATOM   578  O  O   . TRP A 1 79  ? 7.074   -2.010  23.211 1.00 56.05  ? 79  TRP A O   1 
ATOM   579  C  CB  . TRP A 1 79  ? 9.061   -4.587  23.129 1.00 74.68  ? 79  TRP A CB  1 
ATOM   580  C  CG  . TRP A 1 79  ? 7.686   -5.156  23.000 1.00 71.22  ? 79  TRP A CG  1 
ATOM   581  C  CD1 . TRP A 1 79  ? 6.944   -5.781  23.955 1.00 80.65  ? 79  TRP A CD1 1 
ATOM   582  C  CD2 . TRP A 1 79  ? 6.838   -5.037  21.865 1.00 66.02  ? 79  TRP A CD2 1 
ATOM   583  N  NE1 . TRP A 1 79  ? 5.691   -6.058  23.489 1.00 79.60  ? 79  TRP A NE1 1 
ATOM   584  C  CE2 . TRP A 1 79  ? 5.606   -5.618  22.204 1.00 70.38  ? 79  TRP A CE2 1 
ATOM   585  C  CE3 . TRP A 1 79  ? 7.003   -4.482  20.607 1.00 73.28  ? 79  TRP A CE3 1 
ATOM   586  C  CZ2 . TRP A 1 79  ? 4.552   -5.694  21.310 1.00 70.84  ? 79  TRP A CZ2 1 
ATOM   587  C  CZ3 . TRP A 1 79  ? 5.964   -4.562  19.718 1.00 75.21  ? 79  TRP A CZ3 1 
ATOM   588  C  CH2 . TRP A 1 79  ? 4.763   -5.168  20.064 1.00 76.07  ? 79  TRP A CH2 1 
ATOM   589  N  N   . ILE A 1 80  ? 8.914   -1.419  22.082 1.00 61.34  ? 80  ILE A N   1 
ATOM   590  C  CA  . ILE A 1 80  ? 8.216   -0.353  21.322 1.00 64.63  ? 80  ILE A CA  1 
ATOM   591  C  C   . ILE A 1 80  ? 7.535   -0.987  20.122 1.00 63.99  ? 80  ILE A C   1 
ATOM   592  O  O   . ILE A 1 80  ? 8.213   -1.660  19.372 1.00 59.30  ? 80  ILE A O   1 
ATOM   593  C  CB  . ILE A 1 80  ? 9.222   0.715   20.910 1.00 64.71  ? 80  ILE A CB  1 
ATOM   594  C  CG1 . ILE A 1 80  ? 9.974   1.190   22.143 1.00 66.21  ? 80  ILE A CG1 1 
ATOM   595  C  CG2 . ILE A 1 80  ? 8.520   1.858   20.187 1.00 69.39  ? 80  ILE A CG2 1 
ATOM   596  C  CD1 . ILE A 1 80  ? 11.169  2.011   21.806 1.00 79.85  ? 80  ILE A CD1 1 
ATOM   597  N  N   . PRO A 1 81  ? 6.233   -0.753  19.840 1.00 64.63  ? 81  PRO A N   1 
ATOM   598  C  CA  . PRO A 1 81  ? 5.371   0.142   20.610 1.00 71.85  ? 81  PRO A CA  1 
ATOM   599  C  C   . PRO A 1 81  ? 4.475   -0.505  21.679 1.00 72.19  ? 81  PRO A C   1 
ATOM   600  O  O   . PRO A 1 81  ? 3.646   0.181   22.252 1.00 77.79  ? 81  PRO A O   1 
ATOM   601  C  CB  . PRO A 1 81  ? 4.486   0.688   19.487 1.00 72.99  ? 81  PRO A CB  1 
ATOM   602  C  CG  . PRO A 1 81  ? 4.218   -0.533  18.671 1.00 71.05  ? 81  PRO A CG  1 
ATOM   603  C  CD  . PRO A 1 81  ? 5.537   -1.276  18.661 1.00 68.75  ? 81  PRO A CD  1 
ATOM   604  N  N   . GLY A 1 82  ? 4.636   -1.797  21.937 1.00 71.87  ? 82  GLY A N   1 
ATOM   605  C  CA  . GLY A 1 82  ? 3.918   -2.435  23.054 1.00 80.37  ? 82  GLY A CA  1 
ATOM   606  C  C   . GLY A 1 82  ? 2.736   -3.244  22.580 1.00 75.13  ? 82  GLY A C   1 
ATOM   607  O  O   . GLY A 1 82  ? 2.225   -2.948  21.501 1.00 70.22  ? 82  GLY A O   1 
ATOM   608  N  N   . ARG A 1 83  ? 2.342   -4.251  23.356 1.00 75.24  ? 83  ARG A N   1 
ATOM   609  C  CA  . ARG A 1 83  ? 1.112   -5.030  23.101 1.00 75.14  ? 83  ARG A CA  1 
ATOM   610  C  C   . ARG A 1 83  ? -0.084  -4.084  22.962 1.00 73.00  ? 83  ARG A C   1 
ATOM   611  O  O   . ARG A 1 83  ? -0.130  -3.102  23.705 1.00 64.69  ? 83  ARG A O   1 
ATOM   612  C  CB  . ARG A 1 83  ? 0.851   -5.996  24.247 1.00 78.23  ? 83  ARG A CB  1 
ATOM   613  C  CG  . ARG A 1 83  ? -0.455  -6.744  24.064 1.00 82.08  ? 83  ARG A CG  1 
ATOM   614  C  CD  . ARG A 1 83  ? -0.563  -7.907  25.008 1.00 85.02  ? 83  ARG A CD  1 
ATOM   615  N  NE  . ARG A 1 83  ? -1.886  -8.487  24.901 1.00 80.15  ? 83  ARG A NE  1 
ATOM   616  C  CZ  . ARG A 1 83  ? -2.238  -9.412  24.040 1.00 69.03  ? 83  ARG A CZ  1 
ATOM   617  N  NH1 . ARG A 1 83  ? -1.358  -9.903  23.195 1.00 69.93  ? 83  ARG A NH1 1 
ATOM   618  N  NH2 . ARG A 1 83  ? -3.477  -9.848  24.037 1.00 77.52  ? 83  ARG A NH2 1 
ATOM   619  N  N   . LYS A 1 84  ? -1.013  -4.376  22.045 1.00 78.71  ? 84  LYS A N   1 
ATOM   620  C  CA  . LYS A 1 84  ? -2.303  -3.642  21.937 1.00 73.97  ? 84  LYS A CA  1 
ATOM   621  C  C   . LYS A 1 84  ? -3.046  -3.844  23.266 1.00 70.11  ? 84  LYS A C   1 
ATOM   622  O  O   . LYS A 1 84  ? -2.926  -4.940  23.813 1.00 80.88  ? 84  LYS A O   1 
ATOM   623  C  CB  . LYS A 1 84  ? -3.120  -4.150  20.743 1.00 75.56  ? 84  LYS A CB  1 
ATOM   624  C  CG  . LYS A 1 84  ? -2.725  -3.633  19.361 1.00 75.89  ? 84  LYS A CG  1 
ATOM   625  C  CD  . LYS A 1 84  ? -2.491  -4.734  18.312 1.00 89.81  ? 84  LYS A CD  1 
ATOM   626  C  CE  . LYS A 1 84  ? -3.731  -5.157  17.548 1.00 103.33 ? 84  LYS A CE  1 
ATOM   627  N  NZ  . LYS A 1 84  ? -3.758  -4.547  16.208 1.00 109.85 ? 84  LYS A NZ  1 
ATOM   628  N  N   . GLN A 1 85  ? -3.729  -2.816  23.780 1.00 65.88  ? 85  GLN A N   1 
ATOM   629  C  CA  . GLN A 1 85  ? -4.572  -2.859  25.012 1.00 71.01  ? 85  GLN A CA  1 
ATOM   630  C  C   . GLN A 1 85  ? -5.760  -3.816  24.836 1.00 79.01  ? 85  GLN A C   1 
ATOM   631  O  O   . GLN A 1 85  ? -6.577  -3.683  23.889 1.00 83.43  ? 85  GLN A O   1 
ATOM   632  C  CB  . GLN A 1 85  ? -5.119  -1.478  25.376 1.00 76.46  ? 85  GLN A CB  1 
ATOM   633  C  CG  . GLN A 1 85  ? -5.958  -1.466  26.648 1.00 70.08  ? 85  GLN A CG  1 
ATOM   634  C  CD  . GLN A 1 85  ? -5.102  -1.417  27.887 1.00 81.34  ? 85  GLN A CD  1 
ATOM   635  O  OE1 . GLN A 1 85  ? -4.201  -0.588  28.014 1.00 95.19  ? 85  GLN A OE1 1 
ATOM   636  N  NE2 . GLN A 1 85  ? -5.365  -2.321  28.812 1.00 86.21  ? 85  GLN A NE2 1 
ATOM   637  N  N   . TRP A 1 86  ? -5.886  -4.764  25.747 1.00 85.46  ? 86  TRP A N   1 
ATOM   638  C  CA  . TRP A 1 86  ? -7.101  -5.599  25.788 1.00 81.32  ? 86  TRP A CA  1 
ATOM   639  C  C   . TRP A 1 86  ? -8.185  -4.671  26.289 1.00 74.63  ? 86  TRP A C   1 
ATOM   640  O  O   . TRP A 1 86  ? -7.938  -3.948  27.231 1.00 71.21  ? 86  TRP A O   1 
ATOM   641  C  CB  . TRP A 1 86  ? -6.903  -6.809  26.695 1.00 90.11  ? 86  TRP A CB  1 
ATOM   642  C  CG  . TRP A 1 86  ? -7.889  -7.900  26.429 1.00 90.49  ? 86  TRP A CG  1 
ATOM   643  C  CD1 . TRP A 1 86  ? -8.903  -8.310  27.240 1.00 79.91  ? 86  TRP A CD1 1 
ATOM   644  C  CD2 . TRP A 1 86  ? -7.962  -8.705  25.243 1.00 90.45  ? 86  TRP A CD2 1 
ATOM   645  N  NE1 . TRP A 1 86  ? -9.577  -9.339  26.647 1.00 82.19  ? 86  TRP A NE1 1 
ATOM   646  C  CE2 . TRP A 1 86  ? -9.030  -9.593  25.422 1.00 77.15  ? 86  TRP A CE2 1 
ATOM   647  C  CE3 . TRP A 1 86  ? -7.249  -8.737  24.044 1.00 101.32 ? 86  TRP A CE3 1 
ATOM   648  C  CZ2 . TRP A 1 86  ? -9.388  -10.514 24.456 1.00 78.44  ? 86  TRP A CZ2 1 
ATOM   649  C  CZ3 . TRP A 1 86  ? -7.603  -9.654  23.089 1.00 96.05  ? 86  TRP A CZ3 1 
ATOM   650  C  CH2 . TRP A 1 86  ? -8.662  -10.523 23.295 1.00 85.00  ? 86  TRP A CH2 1 
ATOM   651  N  N   . PRO A 1 87  ? -9.374  -4.611  25.675 1.00 69.64  ? 87  PRO A N   1 
ATOM   652  C  CA  . PRO A 1 87  ? -10.339 -3.579  26.045 1.00 63.89  ? 87  PRO A CA  1 
ATOM   653  C  C   . PRO A 1 87  ? -10.905 -3.789  27.456 1.00 69.07  ? 87  PRO A C   1 
ATOM   654  O  O   . PRO A 1 87  ? -11.509 -2.871  27.998 1.00 68.44  ? 87  PRO A O   1 
ATOM   655  C  CB  . PRO A 1 87  ? -11.420 -3.726  24.976 1.00 74.09  ? 87  PRO A CB  1 
ATOM   656  C  CG  . PRO A 1 87  ? -11.318 -5.187  24.566 1.00 81.87  ? 87  PRO A CG  1 
ATOM   657  C  CD  . PRO A 1 87  ? -9.843  -5.526  24.628 1.00 76.39  ? 87  PRO A CD  1 
ATOM   658  N  N   . THR A 1 88  ? -10.713 -4.979  28.030 1.00 76.83  ? 88  THR A N   1 
ATOM   659  C  CA  . THR A 1 88  ? -11.481 -5.415  29.225 1.00 79.99  ? 88  THR A CA  1 
ATOM   660  C  C   . THR A 1 88  ? -10.583 -5.996  30.311 1.00 78.46  ? 88  THR A C   1 
ATOM   661  O  O   . THR A 1 88  ? -11.153 -6.540  31.267 1.00 78.53  ? 88  THR A O   1 
ATOM   662  C  CB  . THR A 1 88  ? -12.552 -6.431  28.819 1.00 81.35  ? 88  THR A CB  1 
ATOM   663  O  OG1 . THR A 1 88  ? -11.952 -7.494  28.080 1.00 78.83  ? 88  THR A OG1 1 
ATOM   664  C  CG2 . THR A 1 88  ? -13.621 -5.797  27.964 1.00 83.52  ? 88  THR A CG2 1 
ATOM   665  N  N   . SER A 1 89  ? -9.262  -5.841  30.212 1.00 75.25  ? 89  SER A N   1 
ATOM   666  C  CA  . SER A 1 89  ? -8.318  -6.343  31.243 1.00 76.58  ? 89  SER A CA  1 
ATOM   667  C  C   . SER A 1 89  ? -8.518  -5.554  32.537 1.00 72.68  ? 89  SER A C   1 
ATOM   668  O  O   . SER A 1 89  ? -9.158  -4.478  32.509 1.00 62.03  ? 89  SER A O   1 
ATOM   669  C  CB  . SER A 1 89  ? -6.883  -6.308  30.791 1.00 78.27  ? 89  SER A CB  1 
ATOM   670  O  OG  . SER A 1 89  ? -6.547  -5.040  30.258 1.00 73.87  ? 89  SER A OG  1 
ATOM   671  N  N   . LYS A 1 90  ? -8.013  -6.107  33.638 1.00 71.97  ? 90  LYS A N   1 
ATOM   672  C  CA  . LYS A 1 90  ? -8.101  -5.457  34.961 1.00 80.07  ? 90  LYS A CA  1 
ATOM   673  C  C   . LYS A 1 90  ? -7.363  -4.113  34.881 1.00 78.68  ? 90  LYS A C   1 
ATOM   674  O  O   . LYS A 1 90  ? -7.773  -3.171  35.579 1.00 71.17  ? 90  LYS A O   1 
ATOM   675  C  CB  . LYS A 1 90  ? -7.544  -6.386  36.046 1.00 91.73  ? 90  LYS A CB  1 
ATOM   676  C  CG  . LYS A 1 90  ? -7.628  -5.867  37.484 1.00 109.91 ? 90  LYS A CG  1 
ATOM   677  C  CD  . LYS A 1 90  ? -9.018  -5.398  37.931 1.00 121.71 ? 90  LYS A CD  1 
ATOM   678  C  CE  . LYS A 1 90  ? -9.249  -5.420  39.433 1.00 121.53 ? 90  LYS A CE  1 
ATOM   679  N  NZ  . LYS A 1 90  ? -8.356  -4.474  40.138 1.00 127.27 ? 90  LYS A NZ  1 
ATOM   680  N  N   . LEU A 1 91  ? -6.310  -4.017  34.065 1.00 76.17  ? 91  LEU A N   1 
ATOM   681  C  CA  . LEU A 1 91  ? -5.414  -2.836  34.077 1.00 70.06  ? 91  LEU A CA  1 
ATOM   682  C  C   . LEU A 1 91  ? -5.339  -2.186  32.708 1.00 70.75  ? 91  LEU A C   1 
ATOM   683  O  O   . LEU A 1 91  ? -5.459  -2.884  31.707 1.00 72.48  ? 91  LEU A O   1 
ATOM   684  C  CB  . LEU A 1 91  ? -4.012  -3.259  34.508 1.00 70.07  ? 91  LEU A CB  1 
ATOM   685  C  CG  . LEU A 1 91  ? -3.867  -3.632  35.982 1.00 72.07  ? 91  LEU A CG  1 
ATOM   686  C  CD1 . LEU A 1 91  ? -2.422  -4.011  36.308 1.00 71.91  ? 91  LEU A CD1 1 
ATOM   687  C  CD2 . LEU A 1 91  ? -4.345  -2.499  36.879 1.00 64.92  ? 91  LEU A CD2 1 
ATOM   688  N  N   . LEU A 1 92  ? -5.110  -0.878  32.721 1.00 77.71  ? 92  LEU A N   1 
ATOM   689  C  CA  . LEU A 1 92  ? -4.602  -0.085  31.574 1.00 74.74  ? 92  LEU A CA  1 
ATOM   690  C  C   . LEU A 1 92  ? -3.081  -0.005  31.711 1.00 73.15  ? 92  LEU A C   1 
ATOM   691  O  O   . LEU A 1 92  ? -2.615  0.404   32.800 1.00 67.16  ? 92  LEU A O   1 
ATOM   692  C  CB  . LEU A 1 92  ? -5.193  1.328   31.605 1.00 77.47  ? 92  LEU A CB  1 
ATOM   693  C  CG  . LEU A 1 92  ? -6.666  1.468   31.227 1.00 74.48  ? 92  LEU A CG  1 
ATOM   694  C  CD1 . LEU A 1 92  ? -7.151  2.889   31.523 1.00 81.42  ? 92  LEU A CD1 1 
ATOM   695  C  CD2 . LEU A 1 92  ? -6.888  1.098   29.770 1.00 72.33  ? 92  LEU A CD2 1 
ATOM   696  N  N   . GLY A 1 93  ? -2.360  -0.359  30.643 1.00 74.33  ? 93  GLY A N   1 
ATOM   697  C  CA  . GLY A 1 93  ? -0.892  -0.254  30.544 1.00 71.87  ? 93  GLY A CA  1 
ATOM   698  C  C   . GLY A 1 93  ? -0.412  1.136   30.904 1.00 70.25  ? 93  GLY A C   1 
ATOM   699  O  O   . GLY A 1 93  ? -1.173  2.133   30.764 1.00 74.99  ? 93  GLY A O   1 
ATOM   700  N  N   . ALA A 1 94  ? 0.826   1.250   31.342 1.00 73.45  ? 94  ALA A N   1 
ATOM   701  C  CA  . ALA A 1 94  ? 1.398   2.583   31.602 1.00 78.03  ? 94  ALA A CA  1 
ATOM   702  C  C   . ALA A 1 94  ? 1.919   3.122   30.281 1.00 71.94  ? 94  ALA A C   1 
ATOM   703  O  O   . ALA A 1 94  ? 2.257   2.367   29.367 1.00 75.66  ? 94  ALA A O   1 
ATOM   704  C  CB  . ALA A 1 94  ? 2.452   2.541   32.675 1.00 86.22  ? 94  ALA A CB  1 
ATOM   705  N  N   . PRO A 1 95  ? 1.888   4.453   30.116 1.00 66.34  ? 95  PRO A N   1 
ATOM   706  C  CA  . PRO A 1 95  ? 2.512   5.092   28.973 1.00 63.38  ? 95  PRO A CA  1 
ATOM   707  C  C   . PRO A 1 95  ? 4.035   5.069   29.137 1.00 58.44  ? 95  PRO A C   1 
ATOM   708  O  O   . PRO A 1 95  ? 4.533   5.120   30.256 1.00 54.01  ? 95  PRO A O   1 
ATOM   709  C  CB  . PRO A 1 95  ? 1.985   6.525   29.017 1.00 67.27  ? 95  PRO A CB  1 
ATOM   710  C  CG  . PRO A 1 95  ? 0.836   6.518   30.012 1.00 84.36  ? 95  PRO A CG  1 
ATOM   711  C  CD  . PRO A 1 95  ? 1.189   5.407   30.978 1.00 79.25  ? 95  PRO A CD  1 
ATOM   712  N  N   . PHE A 1 96  ? 4.760   5.027   28.024 1.00 57.17  ? 96  PHE A N   1 
ATOM   713  C  CA  . PHE A 1 96  ? 6.242   5.072   28.047 1.00 60.62  ? 96  PHE A CA  1 
ATOM   714  C  C   . PHE A 1 96  ? 6.791   5.700   26.769 1.00 62.35  ? 96  PHE A C   1 
ATOM   715  O  O   . PHE A 1 96  ? 6.118   5.632   25.723 1.00 73.24  ? 96  PHE A O   1 
ATOM   716  C  CB  . PHE A 1 96  ? 6.789   3.664   28.240 1.00 59.38  ? 96  PHE A CB  1 
ATOM   717  C  CG  . PHE A 1 96  ? 6.410   2.707   27.142 1.00 58.27  ? 96  PHE A CG  1 
ATOM   718  C  CD1 . PHE A 1 96  ? 5.099   2.302   26.974 1.00 60.79  ? 96  PHE A CD1 1 
ATOM   719  C  CD2 . PHE A 1 96  ? 7.376   2.214   26.279 1.00 57.80  ? 96  PHE A CD2 1 
ATOM   720  C  CE1 . PHE A 1 96  ? 4.769   1.424   25.955 1.00 66.68  ? 96  PHE A CE1 1 
ATOM   721  C  CE2 . PHE A 1 96  ? 7.055   1.293   25.300 1.00 54.32  ? 96  PHE A CE2 1 
ATOM   722  C  CZ  . PHE A 1 96  ? 5.752   0.907   25.135 1.00 61.03  ? 96  PHE A CZ  1 
ATOM   723  N  N   . TYR A 1 97  ? 7.990   6.271   26.867 1.00 58.62  ? 97  TYR A N   1 
ATOM   724  C  CA  . TYR A 1 97  ? 8.763   6.798   25.715 1.00 63.36  ? 97  TYR A CA  1 
ATOM   725  C  C   . TYR A 1 97  ? 8.797   5.753   24.594 1.00 61.82  ? 97  TYR A C   1 
ATOM   726  O  O   . TYR A 1 97  ? 9.201   4.599   24.843 1.00 57.52  ? 97  TYR A O   1 
ATOM   727  C  CB  . TYR A 1 97  ? 10.178  7.198   26.143 1.00 62.37  ? 97  TYR A CB  1 
ATOM   728  C  CG  . TYR A 1 97  ? 10.233  8.486   26.917 1.00 60.20  ? 97  TYR A CG  1 
ATOM   729  C  CD1 . TYR A 1 97  ? 9.738   9.645   26.369 1.00 71.91  ? 97  TYR A CD1 1 
ATOM   730  C  CD2 . TYR A 1 97  ? 10.764  8.558   28.185 1.00 60.10  ? 97  TYR A CD2 1 
ATOM   731  C  CE1 . TYR A 1 97  ? 9.758   10.847  27.055 1.00 74.52  ? 97  TYR A CE1 1 
ATOM   732  C  CE2 . TYR A 1 97  ? 10.795  9.748   28.889 1.00 66.08  ? 97  TYR A CE2 1 
ATOM   733  C  CZ  . TYR A 1 97  ? 10.275  10.893  28.328 1.00 66.35  ? 97  TYR A CZ  1 
ATOM   734  O  OH  . TYR A 1 97  ? 10.260  12.073  28.995 1.00 71.71  ? 97  TYR A OH  1 
ATOM   735  N  N   . GLN A 1 98  ? 8.413   6.165   23.384 1.00 59.46  ? 98  GLN A N   1 
ATOM   736  C  CA  . GLN A 1 98  ? 8.423   5.288   22.187 1.00 62.31  ? 98  GLN A CA  1 
ATOM   737  C  C   . GLN A 1 98  ? 9.789   5.374   21.481 1.00 61.02  ? 98  GLN A C   1 
ATOM   738  O  O   . GLN A 1 98  ? 9.878   5.144   20.236 1.00 54.63  ? 98  GLN A O   1 
ATOM   739  C  CB  . GLN A 1 98  ? 7.306   5.725   21.250 1.00 70.79  ? 98  GLN A CB  1 
ATOM   740  C  CG  . GLN A 1 98  ? 5.943   5.753   21.901 1.00 70.48  ? 98  GLN A CG  1 
ATOM   741  C  CD  . GLN A 1 98  ? 5.506   4.346   22.164 1.00 74.57  ? 98  GLN A CD  1 
ATOM   742  O  OE1 . GLN A 1 98  ? 5.385   3.557   21.232 1.00 74.08  ? 98  GLN A OE1 1 
ATOM   743  N  NE2 . GLN A 1 98  ? 5.310   4.039   23.435 1.00 75.19  ? 98  GLN A NE2 1 
ATOM   744  N  N   . GLU A 1 99  ? 10.835  5.681   22.240 1.00 58.75  ? 99  GLU A N   1 
ATOM   745  C  CA  . GLU A 1 99  ? 12.178  5.994   21.703 1.00 63.81  ? 99  GLU A CA  1 
ATOM   746  C  C   . GLU A 1 99  ? 13.141  5.984   22.886 1.00 65.17  ? 99  GLU A C   1 
ATOM   747  O  O   . GLU A 1 99  ? 12.716  6.246   24.000 1.00 60.65  ? 99  GLU A O   1 
ATOM   748  C  CB  . GLU A 1 99  ? 12.201  7.347   20.974 1.00 66.71  ? 99  GLU A CB  1 
ATOM   749  C  CG  . GLU A 1 99  ? 11.683  8.531   21.784 1.00 74.19  ? 99  GLU A CG  1 
ATOM   750  C  CD  . GLU A 1 99  ? 10.252  8.972   21.499 1.00 85.07  ? 99  GLU A CD  1 
ATOM   751  O  OE1 . GLU A 1 99  ? 9.633   8.447   20.546 1.00 86.27  ? 99  GLU A OE1 1 
ATOM   752  O  OE2 . GLU A 1 99  ? 9.769   9.870   22.208 1.00 94.60  ? 99  GLU A OE2 1 
ATOM   753  N  N   . LEU A 1 100 ? 14.398  5.648   22.671 1.00 74.36  ? 100 LEU A N   1 
ATOM   754  C  CA  . LEU A 1 100 ? 15.418  6.033   23.656 1.00 67.51  ? 100 LEU A CA  1 
ATOM   755  C  C   . LEU A 1 100 ? 15.643  7.509   23.380 1.00 70.27  ? 100 LEU A C   1 
ATOM   756  O  O   . LEU A 1 100 ? 16.139  7.844   22.296 1.00 74.19  ? 100 LEU A O   1 
ATOM   757  C  CB  . LEU A 1 100 ? 16.704  5.231   23.470 1.00 69.63  ? 100 LEU A CB  1 
ATOM   758  C  CG  . LEU A 1 100 ? 17.830  5.691   24.393 1.00 65.55  ? 100 LEU A CG  1 
ATOM   759  C  CD1 . LEU A 1 100 ? 17.391  5.656   25.854 1.00 59.51  ? 100 LEU A CD1 1 
ATOM   760  C  CD2 . LEU A 1 100 ? 19.072  4.863   24.175 1.00 61.74  ? 100 LEU A CD2 1 
ATOM   761  N  N   . PRO A 1 101 ? 15.204  8.393   24.307 1.00 60.06  ? 101 PRO A N   1 
ATOM   762  C  CA  . PRO A 1 101 ? 15.444  9.831   24.247 1.00 60.01  ? 101 PRO A CA  1 
ATOM   763  C  C   . PRO A 1 101 ? 16.898  10.221  23.990 1.00 60.62  ? 101 PRO A C   1 
ATOM   764  O  O   . PRO A 1 101 ? 17.830  9.488   24.419 1.00 55.38  ? 101 PRO A O   1 
ATOM   765  C  CB  . PRO A 1 101 ? 15.113  10.297  25.661 1.00 59.10  ? 101 PRO A CB  1 
ATOM   766  C  CG  . PRO A 1 101 ? 14.010  9.381   26.057 1.00 60.84  ? 101 PRO A CG  1 
ATOM   767  C  CD  . PRO A 1 101 ? 14.441  8.043   25.501 1.00 59.90  ? 101 PRO A CD  1 
ATOM   768  N  N   . LEU A 1 102 ? 17.059  11.350  23.304 1.00 56.25  ? 102 LEU A N   1 
ATOM   769  C  CA  . LEU A 1 102 ? 18.409  11.803  22.900 1.00 59.22  ? 102 LEU A CA  1 
ATOM   770  C  C   . LEU A 1 102 ? 19.158  12.376  24.105 1.00 63.32  ? 102 LEU A C   1 
ATOM   771  O  O   . LEU A 1 102 ? 20.402  12.505  24.027 1.00 78.17  ? 102 LEU A O   1 
ATOM   772  C  CB  . LEU A 1 102 ? 18.266  12.838  21.791 1.00 59.15  ? 102 LEU A CB  1 
ATOM   773  C  CG  . LEU A 1 102 ? 17.645  12.294  20.511 1.00 59.60  ? 102 LEU A CG  1 
ATOM   774  C  CD1 . LEU A 1 102 ? 17.703  13.327  19.404 1.00 62.23  ? 102 LEU A CD1 1 
ATOM   775  C  CD2 . LEU A 1 102 ? 18.357  11.040  20.047 1.00 59.41  ? 102 LEU A CD2 1 
ATOM   776  N  N   . TRP A 1 103 ? 18.441  12.733  25.168 1.00 59.41  ? 103 TRP A N   1 
ATOM   777  C  CA  . TRP A 1 103 ? 19.058  13.387  26.344 1.00 58.03  ? 103 TRP A CA  1 
ATOM   778  C  C   . TRP A 1 103 ? 19.711  12.349  27.247 1.00 60.69  ? 103 TRP A C   1 
ATOM   779  O  O   . TRP A 1 103 ? 20.470  12.728  28.152 1.00 63.04  ? 103 TRP A O   1 
ATOM   780  C  CB  . TRP A 1 103 ? 18.041  14.232  27.099 1.00 62.99  ? 103 TRP A CB  1 
ATOM   781  C  CG  . TRP A 1 103 ? 16.811  13.545  27.580 1.00 62.81  ? 103 TRP A CG  1 
ATOM   782  C  CD1 . TRP A 1 103 ? 16.691  12.713  28.652 1.00 67.81  ? 103 TRP A CD1 1 
ATOM   783  C  CD2 . TRP A 1 103 ? 15.492  13.742  27.060 1.00 67.71  ? 103 TRP A CD2 1 
ATOM   784  N  NE1 . TRP A 1 103 ? 15.384  12.331  28.803 1.00 72.64  ? 103 TRP A NE1 1 
ATOM   785  C  CE2 . TRP A 1 103 ? 14.623  12.957  27.847 1.00 74.76  ? 103 TRP A CE2 1 
ATOM   786  C  CE3 . TRP A 1 103 ? 14.969  14.458  25.979 1.00 79.69  ? 103 TRP A CE3 1 
ATOM   787  C  CZ2 . TRP A 1 103 ? 13.254  12.878  27.582 1.00 82.76  ? 103 TRP A CZ2 1 
ATOM   788  C  CZ3 . TRP A 1 103 ? 13.615  14.373  25.713 1.00 98.43  ? 103 TRP A CZ3 1 
ATOM   789  C  CH2 . TRP A 1 103 ? 12.765  13.596  26.511 1.00 91.45  ? 103 TRP A CH2 1 
ATOM   790  N  N   . GLU A 1 104 ? 19.448  11.077  26.985 1.00 65.62  ? 104 GLU A N   1 
ATOM   791  C  CA  . GLU A 1 104 ? 20.158  9.971   27.657 1.00 60.09  ? 104 GLU A CA  1 
ATOM   792  C  C   . GLU A 1 104 ? 21.535  9.835   27.007 1.00 60.96  ? 104 GLU A C   1 
ATOM   793  O  O   . GLU A 1 104 ? 21.640  9.859   25.761 1.00 62.75  ? 104 GLU A O   1 
ATOM   794  C  CB  . GLU A 1 104 ? 19.304  8.707   27.591 1.00 62.89  ? 104 GLU A CB  1 
ATOM   795  C  CG  . GLU A 1 104 ? 18.046  8.778   28.455 1.00 65.70  ? 104 GLU A CG  1 
ATOM   796  C  CD  . GLU A 1 104 ? 18.231  9.038   29.949 1.00 68.46  ? 104 GLU A CD  1 
ATOM   797  O  OE1 . GLU A 1 104 ? 19.368  8.929   30.488 1.00 82.25  ? 104 GLU A OE1 1 
ATOM   798  O  OE2 . GLU A 1 104 ? 17.237  9.370   30.577 1.00 74.00  ? 104 GLU A OE2 1 
ATOM   799  N  N   . THR A 1 105 ? 22.556  9.734   27.843 1.00 62.48  ? 105 THR A N   1 
ATOM   800  C  CA  . THR A 1 105 ? 23.954  9.430   27.461 1.00 61.78  ? 105 THR A CA  1 
ATOM   801  C  C   . THR A 1 105 ? 24.169  7.919   27.289 1.00 60.62  ? 105 THR A C   1 
ATOM   802  O  O   . THR A 1 105 ? 23.912  7.142   28.262 1.00 64.36  ? 105 THR A O   1 
ATOM   803  C  CB  . THR A 1 105 ? 24.863  9.942   28.568 1.00 62.33  ? 105 THR A CB  1 
ATOM   804  O  OG1 . THR A 1 105 ? 24.297  11.202  28.925 1.00 60.75  ? 105 THR A OG1 1 
ATOM   805  C  CG2 . THR A 1 105 ? 26.303  10.007  28.136 1.00 67.53  ? 105 THR A CG2 1 
ATOM   806  N  N   . THR A 1 106 ? 24.647  7.512   26.115 1.00 55.02  ? 106 THR A N   1 
ATOM   807  C  CA  . THR A 1 106 ? 25.005  6.106   25.819 1.00 55.22  ? 106 THR A CA  1 
ATOM   808  C  C   . THR A 1 106 ? 26.499  5.878   26.008 1.00 55.03  ? 106 THR A C   1 
ATOM   809  O  O   . THR A 1 106 ? 27.282  6.824   25.980 1.00 53.89  ? 106 THR A O   1 
ATOM   810  C  CB  . THR A 1 106 ? 24.668  5.701   24.386 1.00 60.34  ? 106 THR A CB  1 
ATOM   811  O  OG1 . THR A 1 106 ? 25.586  6.320   23.481 1.00 55.75  ? 106 THR A OG1 1 
ATOM   812  C  CG2 . THR A 1 106 ? 23.249  6.067   24.024 1.00 64.79  ? 106 THR A CG2 1 
ATOM   813  N  N   . ILE A 1 107 ? 26.877  4.623   26.163 1.00 62.89  ? 107 ILE A N   1 
ATOM   814  C  CA  . ILE A 1 107 ? 28.293  4.248   26.398 1.00 66.51  ? 107 ILE A CA  1 
ATOM   815  C  C   . ILE A 1 107 ? 29.089  4.678   25.165 1.00 63.32  ? 107 ILE A C   1 
ATOM   816  O  O   . ILE A 1 107 ? 30.270  5.021   25.315 1.00 64.99  ? 107 ILE A O   1 
ATOM   817  C  CB  . ILE A 1 107 ? 28.430  2.748   26.728 1.00 67.64  ? 107 ILE A CB  1 
ATOM   818  C  CG1 . ILE A 1 107 ? 29.853  2.425   27.179 1.00 73.57  ? 107 ILE A CG1 1 
ATOM   819  C  CG2 . ILE A 1 107 ? 28.011  1.876   25.566 1.00 62.57  ? 107 ILE A CG2 1 
ATOM   820  C  CD1 . ILE A 1 107 ? 30.259  3.095   28.477 1.00 75.09  ? 107 ILE A CD1 1 
ATOM   821  N  N   . ALA A 1 108 ? 28.450  4.703   23.999 1.00 59.58  ? 108 ALA A N   1 
ATOM   822  C  CA  . ALA A 1 108 ? 29.094  5.147   22.745 1.00 61.65  ? 108 ALA A CA  1 
ATOM   823  C  C   . ALA A 1 108 ? 29.487  6.618   22.882 1.00 59.70  ? 108 ALA A C   1 
ATOM   824  O  O   . ALA A 1 108 ? 30.621  6.933   22.561 1.00 59.06  ? 108 ALA A O   1 
ATOM   825  C  CB  . ALA A 1 108 ? 28.182  4.928   21.565 1.00 63.68  ? 108 ALA A CB  1 
ATOM   826  N  N   . GLU A 1 109 ? 28.568  7.476   23.333 1.00 58.03  ? 109 GLU A N   1 
ATOM   827  C  CA  . GLU A 1 109 ? 28.838  8.928   23.507 1.00 56.54  ? 109 GLU A CA  1 
ATOM   828  C  C   . GLU A 1 109 ? 29.984  9.036   24.510 1.00 53.39  ? 109 GLU A C   1 
ATOM   829  O  O   . GLU A 1 109 ? 30.813  9.899   24.358 1.00 58.10  ? 109 GLU A O   1 
ATOM   830  C  CB  . GLU A 1 109 ? 27.623  9.746   23.984 1.00 62.92  ? 109 GLU A CB  1 
ATOM   831  C  CG  . GLU A 1 109 ? 26.334  9.581   23.164 1.00 73.54  ? 109 GLU A CG  1 
ATOM   832  C  CD  . GLU A 1 109 ? 25.126  10.362  23.672 1.00 84.75  ? 109 GLU A CD  1 
ATOM   833  O  OE1 . GLU A 1 109 ? 25.333  11.521  24.069 1.00 90.29  ? 109 GLU A OE1 1 
ATOM   834  O  OE2 . GLU A 1 109 ? 23.970  9.819   23.683 1.00 95.85  ? 109 GLU A OE2 1 
ATOM   835  N  N   . ARG A 1 110 ? 29.986  8.237   25.572 1.00 53.92  ? 110 ARG A N   1 
ATOM   836  C  CA  . ARG A 1 110 ? 30.998  8.429   26.650 1.00 61.25  ? 110 ARG A CA  1 
ATOM   837  C  C   . ARG A 1 110 ? 32.398  8.096   26.143 1.00 58.59  ? 110 ARG A C   1 
ATOM   838  O  O   . ARG A 1 110 ? 33.353  8.742   26.590 1.00 58.91  ? 110 ARG A O   1 
ATOM   839  C  CB  . ARG A 1 110 ? 30.616  7.574   27.860 1.00 67.87  ? 110 ARG A CB  1 
ATOM   840  C  CG  . ARG A 1 110 ? 31.538  7.728   29.060 1.00 72.33  ? 110 ARG A CG  1 
ATOM   841  C  CD  . ARG A 1 110 ? 31.002  8.705   30.085 1.00 78.23  ? 110 ARG A CD  1 
ATOM   842  N  NE  . ARG A 1 110 ? 32.094  9.402   30.747 1.00 82.03  ? 110 ARG A NE  1 
ATOM   843  C  CZ  . ARG A 1 110 ? 32.348  9.339   32.047 1.00 85.03  ? 110 ARG A CZ  1 
ATOM   844  N  NH1 . ARG A 1 110 ? 31.578  8.612   32.837 1.00 99.20  ? 110 ARG A NH1 1 
ATOM   845  N  NH2 . ARG A 1 110 ? 33.368  10.006  32.553 1.00 88.73  ? 110 ARG A NH2 1 
ATOM   846  N  N   . LEU A 1 111 ? 32.506  7.117   25.261 1.00 59.64  ? 111 LEU A N   1 
ATOM   847  C  CA  . LEU A 1 111 ? 33.802  6.686   24.688 1.00 61.95  ? 111 LEU A CA  1 
ATOM   848  C  C   . LEU A 1 111 ? 34.272  7.647   23.606 1.00 63.76  ? 111 LEU A C   1 
ATOM   849  O  O   . LEU A 1 111 ? 35.459  7.691   23.375 1.00 63.69  ? 111 LEU A O   1 
ATOM   850  C  CB  . LEU A 1 111 ? 33.628  5.305   24.062 1.00 60.31  ? 111 LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 111 ? 33.556  4.164   25.068 1.00 63.03  ? 111 LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 111 ? 33.597  2.842   24.338 1.00 66.88  ? 111 LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 111 ? 34.678  4.250   26.098 1.00 63.98  ? 111 LEU A CD2 1 
ATOM   854  N  N   . LYS A 1 112 ? 33.349  8.205   22.830 1.00 69.99  ? 112 LYS A N   1 
ATOM   855  C  CA  . LYS A 1 112 ? 33.755  9.031   21.663 1.00 65.03  ? 112 LYS A CA  1 
ATOM   856  C  C   . LYS A 1 112 ? 34.924  9.937   22.050 1.00 61.51  ? 112 LYS A C   1 
ATOM   857  O  O   . LYS A 1 112 ? 35.988  9.798   21.434 1.00 57.21  ? 112 LYS A O   1 
ATOM   858  C  CB  . LYS A 1 112 ? 32.558  9.806   21.111 1.00 64.53  ? 112 LYS A CB  1 
ATOM   859  C  CG  . LYS A 1 112 ? 31.562  8.978   20.316 1.00 66.88  ? 112 LYS A CG  1 
ATOM   860  C  CD  . LYS A 1 112 ? 31.700  9.169   18.826 1.00 95.96  ? 112 LYS A CD  1 
ATOM   861  C  CE  . LYS A 1 112 ? 32.627  8.155   18.195 1.00 126.20 ? 112 LYS A CE  1 
ATOM   862  N  NZ  . LYS A 1 112 ? 32.643  8.267   16.718 1.00 130.67 ? 112 LYS A NZ  1 
ATOM   863  N  N   . PRO A 1 113 ? 34.804  10.848  23.031 1.00 58.57  ? 113 PRO A N   1 
ATOM   864  C  CA  . PRO A 1 113 ? 35.916  11.739  23.338 1.00 57.72  ? 113 PRO A CA  1 
ATOM   865  C  C   . PRO A 1 113 ? 37.255  11.068  23.679 1.00 59.54  ? 113 PRO A C   1 
ATOM   866  O  O   . PRO A 1 113 ? 38.192  11.788  23.817 1.00 67.52  ? 113 PRO A O   1 
ATOM   867  C  CB  . PRO A 1 113 ? 35.446  12.491  24.591 1.00 57.64  ? 113 PRO A CB  1 
ATOM   868  C  CG  . PRO A 1 113 ? 34.455  11.559  25.228 1.00 63.31  ? 113 PRO A CG  1 
ATOM   869  C  CD  . PRO A 1 113 ? 33.733  10.970  24.029 1.00 65.38  ? 113 PRO A CD  1 
ATOM   870  N  N   . LEU A 1 114 ? 37.360  9.748   23.817 1.00 61.42  ? 114 LEU A N   1 
ATOM   871  C  CA  . LEU A 1 114 ? 38.698  9.118   24.051 1.00 68.85  ? 114 LEU A CA  1 
ATOM   872  C  C   . LEU A 1 114 ? 39.284  8.586   22.745 1.00 62.99  ? 114 LEU A C   1 
ATOM   873  O  O   . LEU A 1 114 ? 40.195  7.738   22.835 1.00 69.46  ? 114 LEU A O   1 
ATOM   874  C  CB  . LEU A 1 114 ? 38.599  7.961   25.051 1.00 72.95  ? 114 LEU A CB  1 
ATOM   875  C  CG  . LEU A 1 114 ? 38.170  8.324   26.466 1.00 77.78  ? 114 LEU A CG  1 
ATOM   876  C  CD1 . LEU A 1 114 ? 38.087  7.049   27.292 1.00 80.05  ? 114 LEU A CD1 1 
ATOM   877  C  CD2 . LEU A 1 114 ? 39.121  9.343   27.105 1.00 80.98  ? 114 LEU A CD2 1 
ATOM   878  N  N   . GLY A 1 115 ? 38.708  8.976   21.605 1.00 61.99  ? 115 GLY A N   1 
ATOM   879  C  CA  . GLY A 1 115 ? 39.196  8.644   20.252 1.00 64.66  ? 115 GLY A CA  1 
ATOM   880  C  C   . GLY A 1 115 ? 38.556  7.400   19.684 1.00 59.03  ? 115 GLY A C   1 
ATOM   881  O  O   . GLY A 1 115 ? 39.093  6.831   18.732 1.00 76.48  ? 115 GLY A O   1 
ATOM   882  N  N   . TYR A 1 116 ? 37.448  6.959   20.240 1.00 61.67  ? 116 TYR A N   1 
ATOM   883  C  CA  . TYR A 1 116 ? 36.848  5.670   19.827 1.00 63.65  ? 116 TYR A CA  1 
ATOM   884  C  C   . TYR A 1 116 ? 36.033  5.902   18.563 1.00 60.56  ? 116 TYR A C   1 
ATOM   885  O  O   . TYR A 1 116 ? 35.424  6.947   18.408 1.00 66.20  ? 116 TYR A O   1 
ATOM   886  C  CB  . TYR A 1 116 ? 36.012  5.051   20.943 1.00 63.28  ? 116 TYR A CB  1 
ATOM   887  C  CG  . TYR A 1 116 ? 36.845  4.295   21.937 1.00 64.37  ? 116 TYR A CG  1 
ATOM   888  C  CD1 . TYR A 1 116 ? 37.542  4.972   22.922 1.00 64.40  ? 116 TYR A CD1 1 
ATOM   889  C  CD2 . TYR A 1 116 ? 36.968  2.913   21.879 1.00 64.38  ? 116 TYR A CD2 1 
ATOM   890  C  CE1 . TYR A 1 116 ? 38.307  4.292   23.857 1.00 68.44  ? 116 TYR A CE1 1 
ATOM   891  C  CE2 . TYR A 1 116 ? 37.735  2.218   22.804 1.00 61.98  ? 116 TYR A CE2 1 
ATOM   892  C  CZ  . TYR A 1 116 ? 38.410  2.912   23.798 1.00 63.59  ? 116 TYR A CZ  1 
ATOM   893  O  OH  . TYR A 1 116 ? 39.210  2.284   24.707 1.00 60.26  ? 116 TYR A OH  1 
ATOM   894  N  N   . THR A 1 117 ? 36.103  4.933   17.672 1.00 58.16  ? 117 THR A N   1 
ATOM   895  C  CA  . THR A 1 117 ? 35.174  4.764   16.546 1.00 59.47  ? 117 THR A CA  1 
ATOM   896  C  C   . THR A 1 117 ? 34.077  3.836   17.048 1.00 59.22  ? 117 THR A C   1 
ATOM   897  O  O   . THR A 1 117 ? 34.397  2.853   17.699 1.00 69.39  ? 117 THR A O   1 
ATOM   898  C  CB  . THR A 1 117 ? 35.911  4.182   15.340 1.00 62.24  ? 117 THR A CB  1 
ATOM   899  O  OG1 . THR A 1 117 ? 37.152  4.879   15.273 1.00 77.68  ? 117 THR A OG1 1 
ATOM   900  C  CG2 . THR A 1 117 ? 35.154  4.337   14.047 1.00 65.35  ? 117 THR A CG2 1 
ATOM   901  N  N   . THR A 1 118 ? 32.829  4.145   16.748 1.00 58.97  ? 118 THR A N   1 
ATOM   902  C  CA  . THR A 1 118 ? 31.654  3.474   17.335 1.00 58.92  ? 118 THR A CA  1 
ATOM   903  C  C   . THR A 1 118 ? 30.695  3.074   16.221 1.00 58.27  ? 118 THR A C   1 
ATOM   904  O  O   . THR A 1 118 ? 30.434  3.899   15.316 1.00 58.65  ? 118 THR A O   1 
ATOM   905  C  CB  . THR A 1 118 ? 31.018  4.385   18.384 1.00 61.89  ? 118 THR A CB  1 
ATOM   906  O  OG1 . THR A 1 118 ? 30.433  5.519   17.753 1.00 65.26  ? 118 THR A OG1 1 
ATOM   907  C  CG2 . THR A 1 118 ? 32.043  4.883   19.371 1.00 66.67  ? 118 THR A CG2 1 
ATOM   908  N  N   . ALA A 1 119 ? 30.180  1.853   16.299 1.00 56.96  ? 119 ALA A N   1 
ATOM   909  C  CA  . ALA A 1 119 ? 29.190  1.358   15.334 1.00 58.16  ? 119 ALA A CA  1 
ATOM   910  C  C   . ALA A 1 119 ? 28.139  0.515   16.049 1.00 56.39  ? 119 ALA A C   1 
ATOM   911  O  O   . ALA A 1 119 ? 28.464  -0.215  16.995 1.00 50.82  ? 119 ALA A O   1 
ATOM   912  C  CB  . ALA A 1 119 ? 29.904  0.601   14.256 1.00 69.97  ? 119 ALA A CB  1 
ATOM   913  N  N   . ALA A 1 120 ? 26.898  0.701   15.627 1.00 59.24  ? 120 ALA A N   1 
ATOM   914  C  CA  . ALA A 1 120 ? 25.735  -0.124  15.983 1.00 64.76  ? 120 ALA A CA  1 
ATOM   915  C  C   . ALA A 1 120 ? 25.296  -0.872  14.724 1.00 68.51  ? 120 ALA A C   1 
ATOM   916  O  O   . ALA A 1 120 ? 25.004  -0.249  13.683 1.00 69.08  ? 120 ALA A O   1 
ATOM   917  C  CB  . ALA A 1 120 ? 24.631  0.736   16.547 1.00 71.16  ? 120 ALA A CB  1 
ATOM   918  N  N   . MET A 1 121 ? 25.261  -2.190  14.811 1.00 73.93  ? 121 MET A N   1 
ATOM   919  C  CA  . MET A 1 121 ? 24.956  -3.042  13.646 1.00 74.96  ? 121 MET A CA  1 
ATOM   920  C  C   . MET A 1 121 ? 23.962  -4.114  14.066 1.00 72.39  ? 121 MET A C   1 
ATOM   921  O  O   . MET A 1 121 ? 24.268  -4.893  14.984 1.00 70.14  ? 121 MET A O   1 
ATOM   922  C  CB  . MET A 1 121 ? 26.222  -3.705  13.114 1.00 75.92  ? 121 MET A CB  1 
ATOM   923  C  CG  . MET A 1 121 ? 27.282  -2.732  12.684 1.00 74.13  ? 121 MET A CG  1 
ATOM   924  S  SD  . MET A 1 121 ? 28.388  -3.601  11.576 1.00 76.87  ? 121 MET A SD  1 
ATOM   925  C  CE  . MET A 1 121 ? 29.406  -2.272  10.921 1.00 96.81  ? 121 MET A CE  1 
ATOM   926  N  N   . GLY A 1 122 ? 22.812  -4.121  13.406 1.00 74.56  ? 122 GLY A N   1 
ATOM   927  C  CA  . GLY A 1 122 ? 21.750  -5.109  13.621 1.00 68.66  ? 122 GLY A CA  1 
ATOM   928  C  C   . GLY A 1 122 ? 20.536  -4.415  14.174 1.00 65.38  ? 122 GLY A C   1 
ATOM   929  O  O   . GLY A 1 122 ? 20.190  -3.353  13.660 1.00 72.19  ? 122 GLY A O   1 
ATOM   930  N  N   . LYS A 1 123 ? 19.964  -4.974  15.225 1.00 64.12  ? 123 LYS A N   1 
ATOM   931  C  CA  . LYS A 1 123 ? 18.642  -4.584  15.743 1.00 68.39  ? 123 LYS A CA  1 
ATOM   932  C  C   . LYS A 1 123 ? 18.797  -3.339  16.616 1.00 73.72  ? 123 LYS A C   1 
ATOM   933  O  O   . LYS A 1 123 ? 19.555  -3.342  17.642 1.00 68.40  ? 123 LYS A O   1 
ATOM   934  C  CB  . LYS A 1 123 ? 18.021  -5.743  16.526 1.00 76.02  ? 123 LYS A CB  1 
ATOM   935  C  CG  . LYS A 1 123 ? 16.503  -5.699  16.614 1.00 86.58  ? 123 LYS A CG  1 
ATOM   936  C  CD  . LYS A 1 123 ? 15.872  -6.803  17.420 1.00 85.45  ? 123 LYS A CD  1 
ATOM   937  C  CE  . LYS A 1 123 ? 14.999  -6.226  18.513 1.00 91.66  ? 123 LYS A CE  1 
ATOM   938  N  NZ  . LYS A 1 123 ? 14.451  -7.280  19.392 1.00 104.61 ? 123 LYS A NZ  1 
ATOM   939  N  N   . TRP A 1 124 ? 18.039  -2.310  16.273 1.00 71.20  ? 124 TRP A N   1 
ATOM   940  C  CA  . TRP A 1 124 ? 18.066  -1.071  17.081 1.00 74.87  ? 124 TRP A CA  1 
ATOM   941  C  C   . TRP A 1 124 ? 16.915  -1.112  18.083 1.00 68.26  ? 124 TRP A C   1 
ATOM   942  O  O   . TRP A 1 124 ? 17.180  -1.352  19.283 1.00 70.45  ? 124 TRP A O   1 
ATOM   943  C  CB  . TRP A 1 124 ? 18.006  0.146   16.166 1.00 69.29  ? 124 TRP A CB  1 
ATOM   944  C  CG  . TRP A 1 124 ? 18.129  1.438   16.902 1.00 64.64  ? 124 TRP A CG  1 
ATOM   945  C  CD1 . TRP A 1 124 ? 17.239  2.462   16.885 1.00 62.78  ? 124 TRP A CD1 1 
ATOM   946  C  CD2 . TRP A 1 124 ? 19.199  1.843   17.769 1.00 58.58  ? 124 TRP A CD2 1 
ATOM   947  N  NE1 . TRP A 1 124 ? 17.692  3.486   17.660 1.00 62.23  ? 124 TRP A NE1 1 
ATOM   948  C  CE2 . TRP A 1 124 ? 18.897  3.143   18.206 1.00 57.71  ? 124 TRP A CE2 1 
ATOM   949  C  CE3 . TRP A 1 124 ? 20.384  1.245   18.202 1.00 61.16  ? 124 TRP A CE3 1 
ATOM   950  C  CZ2 . TRP A 1 124 ? 19.726  3.855   19.065 1.00 59.41  ? 124 TRP A CZ2 1 
ATOM   951  C  CZ3 . TRP A 1 124 ? 21.195  1.942   19.068 1.00 59.38  ? 124 TRP A CZ3 1 
ATOM   952  C  CH2 . TRP A 1 124 ? 20.867  3.226   19.494 1.00 56.43  ? 124 TRP A CH2 1 
ATOM   953  N  N   . HIS A 1 125 ? 15.710  -0.933  17.551 1.00 58.03  ? 125 HIS A N   1 
ATOM   954  C  CA  . HIS A 1 125 ? 14.423  -1.028  18.259 1.00 55.69  ? 125 HIS A CA  1 
ATOM   955  C  C   . HIS A 1 125 ? 14.377  -0.009  19.387 1.00 58.73  ? 125 HIS A C   1 
ATOM   956  O  O   . HIS A 1 125 ? 13.780  -0.325  20.414 1.00 58.91  ? 125 HIS A O   1 
ATOM   957  C  CB  . HIS A 1 125 ? 14.253  -2.452  18.751 1.00 55.48  ? 125 HIS A CB  1 
ATOM   958  C  CG  . HIS A 1 125 ? 12.836  -2.824  18.983 1.00 56.84  ? 125 HIS A CG  1 
ATOM   959  N  ND1 . HIS A 1 125 ? 12.484  -3.986  19.642 1.00 60.07  ? 125 HIS A ND1 1 
ATOM   960  C  CD2 . HIS A 1 125 ? 11.695  -2.195  18.652 1.00 53.93  ? 125 HIS A CD2 1 
ATOM   961  C  CE1 . HIS A 1 125 ? 11.179  -4.066  19.701 1.00 59.65  ? 125 HIS A CE1 1 
ATOM   962  N  NE2 . HIS A 1 125 ? 10.680  -2.966  19.114 1.00 56.92  ? 125 HIS A NE2 1 
ATOM   963  N  N   . LEU A 1 126 ? 14.961  1.169   19.185 1.00 61.23  ? 126 LEU A N   1 
ATOM   964  C  CA  . LEU A 1 126 ? 14.839  2.280   20.157 1.00 61.13  ? 126 LEU A CA  1 
ATOM   965  C  C   . LEU A 1 126 ? 14.295  3.562   19.494 1.00 64.92  ? 126 LEU A C   1 
ATOM   966  O  O   . LEU A 1 126 ? 14.735  4.686   19.880 1.00 66.48  ? 126 LEU A O   1 
ATOM   967  C  CB  . LEU A 1 126 ? 16.219  2.427   20.781 1.00 63.63  ? 126 LEU A CB  1 
ATOM   968  C  CG  . LEU A 1 126 ? 16.689  1.186   21.534 1.00 63.73  ? 126 LEU A CG  1 
ATOM   969  C  CD1 . LEU A 1 126 ? 18.201  1.167   21.699 1.00 63.19  ? 126 LEU A CD1 1 
ATOM   970  C  CD2 . LEU A 1 126 ? 16.027  1.125   22.893 1.00 67.14  ? 126 LEU A CD2 1 
ATOM   971  N  N   . GLY A 1 127 ? 13.324  3.407   18.582 1.00 66.83  ? 127 GLY A N   1 
ATOM   972  C  CA  . GLY A 1 127 ? 12.515  4.526   18.065 1.00 74.11  ? 127 GLY A CA  1 
ATOM   973  C  C   . GLY A 1 127 ? 12.760  4.757   16.592 1.00 72.02  ? 127 GLY A C   1 
ATOM   974  O  O   . GLY A 1 127 ? 13.596  4.047   16.064 1.00 60.02  ? 127 GLY A O   1 
ATOM   975  N  N   . HIS A 1 128 ? 12.011  5.674   15.958 1.00 76.61  ? 128 HIS A N   1 
ATOM   976  C  CA  . HIS A 1 128 ? 12.176  6.073   14.532 1.00 77.30  ? 128 HIS A CA  1 
ATOM   977  C  C   . HIS A 1 128 ? 13.330  7.064   14.460 1.00 79.87  ? 128 HIS A C   1 
ATOM   978  O  O   . HIS A 1 128 ? 13.791  7.486   15.574 1.00 77.86  ? 128 HIS A O   1 
ATOM   979  C  CB  . HIS A 1 128 ? 10.907  6.722   13.953 1.00 82.50  ? 128 HIS A CB  1 
ATOM   980  C  CG  . HIS A 1 128 ? 9.756   5.792   13.874 1.00 76.86  ? 128 HIS A CG  1 
ATOM   981  N  ND1 . HIS A 1 128 ? 9.097   5.363   15.004 1.00 77.48  ? 128 HIS A ND1 1 
ATOM   982  C  CD2 . HIS A 1 128 ? 9.170   5.190   12.822 1.00 75.98  ? 128 HIS A CD2 1 
ATOM   983  C  CE1 . HIS A 1 128 ? 8.163   4.504   14.661 1.00 72.92  ? 128 HIS A CE1 1 
ATOM   984  N  NE2 . HIS A 1 128 ? 8.187   4.383   13.328 1.00 74.38  ? 128 HIS A NE2 1 
ATOM   985  N  N   . GLU A 1 129 ? 13.786  7.398   13.252 1.00 84.15  ? 129 GLU A N   1 
ATOM   986  C  CA  . GLU A 1 129 ? 14.876  8.386   13.091 1.00 79.84  ? 129 GLU A CA  1 
ATOM   987  C  C   . GLU A 1 129 ? 14.260  9.754   13.287 1.00 79.36  ? 129 GLU A C   1 
ATOM   988  O  O   . GLU A 1 129 ? 13.428  10.137  12.454 1.00 75.51  ? 129 GLU A O   1 
ATOM   989  C  CB  . GLU A 1 129 ? 15.503  8.346   11.700 1.00 80.80  ? 129 GLU A CB  1 
ATOM   990  C  CG  . GLU A 1 129 ? 14.621  7.712   10.646 1.00 97.69  ? 129 GLU A CG  1 
ATOM   991  C  CD  . GLU A 1 129 ? 15.261  7.709   9.270  1.00 118.85 ? 129 GLU A CD  1 
ATOM   992  O  OE1 . GLU A 1 129 ? 14.743  7.011   8.379  1.00 90.16  ? 129 GLU A OE1 1 
ATOM   993  O  OE2 . GLU A 1 129 ? 16.281  8.403   9.097  1.00 124.73 ? 129 GLU A OE2 1 
ATOM   994  N  N   . PRO A 1 130 ? 14.566  10.472  14.376 1.00 71.72  ? 130 PRO A N   1 
ATOM   995  C  CA  . PRO A 1 130 ? 15.917  10.854  14.766 1.00 73.77  ? 130 PRO A CA  1 
ATOM   996  C  C   . PRO A 1 130 ? 16.479  10.092  15.972 1.00 71.16  ? 130 PRO A C   1 
ATOM   997  O  O   . PRO A 1 130 ? 17.565  10.434  16.401 1.00 76.81  ? 130 PRO A O   1 
ATOM   998  C  CB  . PRO A 1 130 ? 15.637  12.285  15.230 1.00 86.78  ? 130 PRO A CB  1 
ATOM   999  C  CG  . PRO A 1 130 ? 14.327  12.154  15.985 1.00 84.73  ? 130 PRO A CG  1 
ATOM   1000 C  CD  . PRO A 1 130 ? 13.571  11.038  15.288 1.00 72.10  ? 130 PRO A CD  1 
ATOM   1001 N  N   . TYR A 1 131 ? 15.752  9.099   16.497 1.00 73.28  ? 131 TYR A N   1 
ATOM   1002 C  CA  . TYR A 1 131 ? 16.251  8.449   17.735 1.00 67.87  ? 131 TYR A CA  1 
ATOM   1003 C  C   . TYR A 1 131 ? 17.093  7.196   17.420 1.00 64.12  ? 131 TYR A C   1 
ATOM   1004 O  O   . TYR A 1 131 ? 17.397  6.431   18.404 1.00 77.55  ? 131 TYR A O   1 
ATOM   1005 C  CB  . TYR A 1 131 ? 15.082  8.242   18.689 1.00 71.09  ? 131 TYR A CB  1 
ATOM   1006 C  CG  . TYR A 1 131 ? 14.154  9.421   18.854 1.00 64.02  ? 131 TYR A CG  1 
ATOM   1007 C  CD1 . TYR A 1 131 ? 14.469  10.538  19.611 1.00 65.57  ? 131 TYR A CD1 1 
ATOM   1008 C  CD2 . TYR A 1 131 ? 12.906  9.383   18.285 1.00 72.08  ? 131 TYR A CD2 1 
ATOM   1009 C  CE1 . TYR A 1 131 ? 13.576  11.596  19.770 1.00 70.81  ? 131 TYR A CE1 1 
ATOM   1010 C  CE2 . TYR A 1 131 ? 12.003  10.420  18.435 1.00 89.13  ? 131 TYR A CE2 1 
ATOM   1011 C  CZ  . TYR A 1 131 ? 12.319  11.540  19.180 1.00 82.40  ? 131 TYR A CZ  1 
ATOM   1012 O  OH  . TYR A 1 131 ? 11.300  12.470  19.265 1.00 89.81  ? 131 TYR A OH  1 
ATOM   1013 N  N   . TYR A 1 132 ? 17.623  7.200   16.184 1.00 59.40  ? 132 TYR A N   1 
ATOM   1014 C  CA  . TYR A 1 132 ? 18.503  6.129   15.660 1.00 56.62  ? 132 TYR A CA  1 
ATOM   1015 C  C   . TYR A 1 132 ? 19.921  6.315   16.191 1.00 58.36  ? 132 TYR A C   1 
ATOM   1016 O  O   . TYR A 1 132 ? 20.165  7.290   16.906 1.00 56.93  ? 132 TYR A O   1 
ATOM   1017 C  CB  . TYR A 1 132 ? 18.497  6.193   14.133 1.00 57.77  ? 132 TYR A CB  1 
ATOM   1018 C  CG  . TYR A 1 132 ? 17.354  5.497   13.441 1.00 55.37  ? 132 TYR A CG  1 
ATOM   1019 C  CD1 . TYR A 1 132 ? 16.219  5.111   14.129 1.00 63.47  ? 132 TYR A CD1 1 
ATOM   1020 C  CD2 . TYR A 1 132 ? 17.408  5.234   12.084 1.00 63.69  ? 132 TYR A CD2 1 
ATOM   1021 C  CE1 . TYR A 1 132 ? 15.170  4.475   13.486 1.00 67.02  ? 132 TYR A CE1 1 
ATOM   1022 C  CE2 . TYR A 1 132 ? 16.369  4.601   11.426 1.00 62.57  ? 132 TYR A CE2 1 
ATOM   1023 C  CZ  . TYR A 1 132 ? 15.243  4.223   12.130 1.00 59.93  ? 132 TYR A CZ  1 
ATOM   1024 O  OH  . TYR A 1 132 ? 14.216  3.599   11.486 1.00 66.80  ? 132 TYR A OH  1 
ATOM   1025 N  N   . PRO A 1 133 ? 20.887  5.444   15.839 1.00 57.64  ? 133 PRO A N   1 
ATOM   1026 C  CA  . PRO A 1 133 ? 22.193  5.448   16.492 1.00 56.48  ? 133 PRO A CA  1 
ATOM   1027 C  C   . PRO A 1 133 ? 23.106  6.609   16.115 1.00 57.33  ? 133 PRO A C   1 
ATOM   1028 O  O   . PRO A 1 133 ? 23.811  7.083   16.961 1.00 52.19  ? 133 PRO A O   1 
ATOM   1029 C  CB  . PRO A 1 133 ? 22.867  4.175   15.981 1.00 60.36  ? 133 PRO A CB  1 
ATOM   1030 C  CG  . PRO A 1 133 ? 21.723  3.264   15.609 1.00 61.61  ? 133 PRO A CG  1 
ATOM   1031 C  CD  . PRO A 1 133 ? 20.657  4.201   15.089 1.00 62.84  ? 133 PRO A CD  1 
ATOM   1032 N  N   . GLU A 1 134 ? 23.091  6.999   14.854 1.00 62.88  ? 134 GLU A N   1 
ATOM   1033 C  CA  . GLU A 1 134 ? 23.983  8.086   14.409 1.00 66.54  ? 134 GLU A CA  1 
ATOM   1034 C  C   . GLU A 1 134 ? 23.771  9.282   15.336 1.00 68.08  ? 134 GLU A C   1 
ATOM   1035 O  O   . GLU A 1 134 ? 24.724  10.045  15.536 1.00 73.11  ? 134 GLU A O   1 
ATOM   1036 C  CB  . GLU A 1 134 ? 23.664  8.399   12.953 1.00 77.56  ? 134 GLU A CB  1 
ATOM   1037 C  CG  . GLU A 1 134 ? 23.364  7.159   12.132 1.00 88.49  ? 134 GLU A CG  1 
ATOM   1038 C  CD  . GLU A 1 134 ? 21.888  6.823   12.034 1.00 105.07 ? 134 GLU A CD  1 
ATOM   1039 O  OE1 . GLU A 1 134 ? 21.096  7.463   12.747 1.00 120.47 ? 134 GLU A OE1 1 
ATOM   1040 O  OE2 . GLU A 1 134 ? 21.535  5.926   11.245 1.00 90.31  ? 134 GLU A OE2 1 
ATOM   1041 N  N   . ARG A 1 135 ? 22.566  9.427   15.885 1.00 65.04  ? 135 ARG A N   1 
ATOM   1042 C  CA  . ARG A 1 135 ? 22.262  10.607  16.740 1.00 67.69  ? 135 ARG A CA  1 
ATOM   1043 C  C   . ARG A 1 135 ? 22.267  10.179  18.202 1.00 70.14  ? 135 ARG A C   1 
ATOM   1044 O  O   . ARG A 1 135 ? 21.478  10.741  18.972 1.00 65.33  ? 135 ARG A O   1 
ATOM   1045 C  CB  . ARG A 1 135 ? 20.886  11.174  16.391 1.00 59.94  ? 135 ARG A CB  1 
ATOM   1046 C  CG  . ARG A 1 135 ? 20.619  11.307  14.901 1.00 72.92  ? 135 ARG A CG  1 
ATOM   1047 C  CD  . ARG A 1 135 ? 19.934  12.627  14.612 1.00 73.68  ? 135 ARG A CD  1 
ATOM   1048 N  NE  . ARG A 1 135 ? 20.289  13.625  15.609 1.00 61.53  ? 135 ARG A NE  1 
ATOM   1049 C  CZ  . ARG A 1 135 ? 19.428  14.451  16.186 1.00 79.19  ? 135 ARG A CZ  1 
ATOM   1050 N  NH1 . ARG A 1 135 ? 18.147  14.408  15.864 1.00 66.98  ? 135 ARG A NH1 1 
ATOM   1051 N  NH2 . ARG A 1 135 ? 19.850  15.322  17.083 1.00 110.58 ? 135 ARG A NH2 1 
ATOM   1052 N  N   . GLN A 1 136 ? 23.160  9.268   18.573 1.00 68.71  ? 136 GLN A N   1 
ATOM   1053 C  CA  . GLN A 1 136 ? 23.159  8.690   19.927 1.00 62.04  ? 136 GLN A CA  1 
ATOM   1054 C  C   . GLN A 1 136 ? 24.551  8.076   20.164 1.00 63.61  ? 136 GLN A C   1 
ATOM   1055 O  O   . GLN A 1 136 ? 24.671  7.106   20.914 1.00 55.58  ? 136 GLN A O   1 
ATOM   1056 C  CB  . GLN A 1 136 ? 21.942  7.778   19.947 1.00 59.67  ? 136 GLN A CB  1 
ATOM   1057 C  CG  . GLN A 1 136 ? 21.565  7.359   21.331 1.00 67.72  ? 136 GLN A CG  1 
ATOM   1058 C  CD  . GLN A 1 136 ? 20.562  8.291   21.934 1.00 68.07  ? 136 GLN A CD  1 
ATOM   1059 O  OE1 . GLN A 1 136 ? 20.940  9.210   22.672 1.00 60.88  ? 136 GLN A OE1 1 
ATOM   1060 N  NE2 . GLN A 1 136 ? 19.296  8.000   21.639 1.00 67.35  ? 136 GLN A NE2 1 
ATOM   1061 N  N   . GLY A 1 137 ? 25.588  8.649   19.542 1.00 65.72  ? 137 GLY A N   1 
ATOM   1062 C  CA  . GLY A 1 137 ? 26.998  8.355   19.863 1.00 64.49  ? 137 GLY A CA  1 
ATOM   1063 C  C   . GLY A 1 137 ? 27.675  7.461   18.844 1.00 62.53  ? 137 GLY A C   1 
ATOM   1064 O  O   . GLY A 1 137 ? 28.903  7.396   18.855 1.00 73.22  ? 137 GLY A O   1 
ATOM   1065 N  N   . PHE A 1 138 ? 26.923  6.824   17.961 1.00 58.44  ? 138 PHE A N   1 
ATOM   1066 C  CA  . PHE A 1 138 ? 27.484  5.949   16.912 1.00 58.65  ? 138 PHE A CA  1 
ATOM   1067 C  C   . PHE A 1 138 ? 27.818  6.689   15.606 1.00 64.50  ? 138 PHE A C   1 
ATOM   1068 O  O   . PHE A 1 138 ? 27.054  7.584   15.095 1.00 66.69  ? 138 PHE A O   1 
ATOM   1069 C  CB  . PHE A 1 138 ? 26.493  4.831   16.659 1.00 65.11  ? 138 PHE A CB  1 
ATOM   1070 C  CG  . PHE A 1 138 ? 26.344  3.921   17.843 1.00 64.15  ? 138 PHE A CG  1 
ATOM   1071 C  CD1 . PHE A 1 138 ? 27.245  2.900   18.053 1.00 65.39  ? 138 PHE A CD1 1 
ATOM   1072 C  CD2 . PHE A 1 138 ? 25.303  4.086   18.732 1.00 59.72  ? 138 PHE A CD2 1 
ATOM   1073 C  CE1 . PHE A 1 138 ? 27.077  2.033   19.112 1.00 63.73  ? 138 PHE A CE1 1 
ATOM   1074 C  CE2 . PHE A 1 138 ? 25.134  3.211   19.786 1.00 53.44  ? 138 PHE A CE2 1 
ATOM   1075 C  CZ  . PHE A 1 138 ? 26.022  2.193   19.975 1.00 56.17  ? 138 PHE A CZ  1 
ATOM   1076 N  N   . ASP A 1 139 ? 28.953  6.271   15.027 1.00 62.56  ? 139 ASP A N   1 
ATOM   1077 C  CA  . ASP A 1 139 ? 29.505  6.821   13.763 1.00 62.69  ? 139 ASP A CA  1 
ATOM   1078 C  C   . ASP A 1 139 ? 28.829  6.125   12.595 1.00 60.95  ? 139 ASP A C   1 
ATOM   1079 O  O   . ASP A 1 139 ? 28.683  6.752   11.534 1.00 77.50  ? 139 ASP A O   1 
ATOM   1080 C  CB  . ASP A 1 139 ? 31.022  6.679   13.713 1.00 66.20  ? 139 ASP A CB  1 
ATOM   1081 C  CG  . ASP A 1 139 ? 31.711  7.435   14.839 1.00 74.00  ? 139 ASP A CG  1 
ATOM   1082 O  OD1 . ASP A 1 139 ? 31.113  8.398   15.360 1.00 107.25 ? 139 ASP A OD1 1 
ATOM   1083 O  OD2 . ASP A 1 139 ? 32.834  7.058   15.197 1.00 85.00  ? 139 ASP A OD2 1 
ATOM   1084 N  N   . ILE A 1 140 ? 28.454  4.867   12.793 1.00 62.96  ? 140 ILE A N   1 
ATOM   1085 C  CA  . ILE A 1 140 ? 27.927  3.991   11.718 1.00 62.61  ? 140 ILE A CA  1 
ATOM   1086 C  C   . ILE A 1 140 ? 26.687  3.292   12.252 1.00 64.61  ? 140 ILE A C   1 
ATOM   1087 O  O   . ILE A 1 140 ? 26.769  2.714   13.352 1.00 68.90  ? 140 ILE A O   1 
ATOM   1088 C  CB  . ILE A 1 140 ? 28.985  2.968   11.300 1.00 58.97  ? 140 ILE A CB  1 
ATOM   1089 C  CG1 . ILE A 1 140 ? 30.294  3.632   10.865 1.00 71.35  ? 140 ILE A CG1 1 
ATOM   1090 C  CG2 . ILE A 1 140 ? 28.386  2.120   10.220 1.00 64.99  ? 140 ILE A CG2 1 
ATOM   1091 C  CD1 . ILE A 1 140 ? 31.339  2.710   10.275 1.00 82.23  ? 140 ILE A CD1 1 
ATOM   1092 N  N   . ASN A 1 141 ? 25.599  3.326   11.493 1.00 61.25  ? 141 ASN A N   1 
ATOM   1093 C  CA  . ASN A 1 141 ? 24.433  2.441   11.725 1.00 58.73  ? 141 ASN A CA  1 
ATOM   1094 C  C   . ASN A 1 141 ? 24.406  1.450   10.572 1.00 62.58  ? 141 ASN A C   1 
ATOM   1095 O  O   . ASN A 1 141 ? 24.451  1.907   9.395  1.00 72.51  ? 141 ASN A O   1 
ATOM   1096 C  CB  . ASN A 1 141 ? 23.128  3.232   11.818 1.00 65.03  ? 141 ASN A CB  1 
ATOM   1097 C  CG  . ASN A 1 141 ? 21.891  2.360   11.779 1.00 63.60  ? 141 ASN A CG  1 
ATOM   1098 O  OD1 . ASN A 1 141 ? 21.923  1.205   12.214 1.00 58.13  ? 141 ASN A OD1 1 
ATOM   1099 N  ND2 . ASN A 1 141 ? 20.795  2.937   11.295 1.00 64.88  ? 141 ASN A ND2 1 
ATOM   1100 N  N   . VAL A 1 142 ? 24.362  0.152   10.872 1.00 65.47  ? 142 VAL A N   1 
ATOM   1101 C  CA  . VAL A 1 142 ? 24.091  -0.875  9.824  1.00 64.89  ? 142 VAL A CA  1 
ATOM   1102 C  C   . VAL A 1 142 ? 22.876  -1.685  10.242 1.00 66.83  ? 142 VAL A C   1 
ATOM   1103 O  O   . VAL A 1 142 ? 22.942  -2.320  11.305 1.00 74.07  ? 142 VAL A O   1 
ATOM   1104 C  CB  . VAL A 1 142 ? 25.295  -1.777  9.544  1.00 63.82  ? 142 VAL A CB  1 
ATOM   1105 C  CG1 . VAL A 1 142 ? 25.015  -2.667  8.352  1.00 66.31  ? 142 VAL A CG1 1 
ATOM   1106 C  CG2 . VAL A 1 142 ? 26.538  -0.949  9.302  1.00 64.12  ? 142 VAL A CG2 1 
ATOM   1107 N  N   . ALA A 1 143 ? 21.786  -1.526  9.487  1.00 70.05  ? 143 ALA A N   1 
ATOM   1108 C  CA  . ALA A 1 143 ? 20.547  -2.341  9.544  1.00 73.11  ? 143 ALA A CA  1 
ATOM   1109 C  C   . ALA A 1 143 ? 19.587  -1.952  10.699 1.00 70.33  ? 143 ALA A C   1 
ATOM   1110 O  O   . ALA A 1 143 ? 18.438  -2.491  10.738 1.00 67.10  ? 143 ALA A O   1 
ATOM   1111 C  CB  . ALA A 1 143 ? 20.969  -3.784  9.597  1.00 73.38  ? 143 ALA A CB  1 
ATOM   1112 N  N   . GLY A 1 144 ? 19.990  -1.038  11.592 1.00 69.12  ? 144 GLY A N   1 
ATOM   1113 C  CA  . GLY A 1 144 ? 19.132  -0.519  12.674 1.00 69.23  ? 144 GLY A CA  1 
ATOM   1114 C  C   . GLY A 1 144 ? 17.955  0.304   12.166 1.00 63.28  ? 144 GLY A C   1 
ATOM   1115 O  O   . GLY A 1 144 ? 18.168  1.225   11.414 1.00 57.74  ? 144 GLY A O   1 
ATOM   1116 N  N   . THR A 1 145 ? 16.744  -0.009  12.607 1.00 67.48  ? 145 THR A N   1 
ATOM   1117 C  CA  . THR A 1 145 ? 15.528  0.804   12.377 1.00 65.16  ? 145 THR A CA  1 
ATOM   1118 C  C   . THR A 1 145 ? 14.677  0.795   13.643 1.00 65.03  ? 145 THR A C   1 
ATOM   1119 O  O   . THR A 1 145 ? 15.136  0.267   14.664 1.00 70.45  ? 145 THR A O   1 
ATOM   1120 C  CB  . THR A 1 145 ? 14.734  0.263   11.190 1.00 70.09  ? 145 THR A CB  1 
ATOM   1121 O  OG1 . THR A 1 145 ? 14.636  -1.151  11.367 1.00 82.95  ? 145 THR A OG1 1 
ATOM   1122 C  CG2 . THR A 1 145 ? 15.386  0.607   9.871  1.00 75.05  ? 145 THR A CG2 1 
ATOM   1123 N  N   . PHE A 1 146 ? 13.484  1.370   13.579 1.00 65.99  ? 146 PHE A N   1 
ATOM   1124 C  CA  . PHE A 1 146 ? 12.490  1.307   14.676 1.00 71.80  ? 146 PHE A CA  1 
ATOM   1125 C  C   . PHE A 1 146 ? 12.062  -0.140  14.839 1.00 70.87  ? 146 PHE A C   1 
ATOM   1126 O  O   . PHE A 1 146 ? 11.582  -0.481  15.921 1.00 76.86  ? 146 PHE A O   1 
ATOM   1127 C  CB  . PHE A 1 146 ? 11.249  2.124   14.343 1.00 80.94  ? 146 PHE A CB  1 
ATOM   1128 C  CG  . PHE A 1 146 ? 10.653  1.777   13.003 1.00 82.77  ? 146 PHE A CG  1 
ATOM   1129 C  CD1 . PHE A 1 146 ? 9.719   0.763   12.881 1.00 79.75  ? 146 PHE A CD1 1 
ATOM   1130 C  CD2 . PHE A 1 146 ? 11.041  2.456   11.861 1.00 86.67  ? 146 PHE A CD2 1 
ATOM   1131 C  CE1 . PHE A 1 146 ? 9.175   0.443   11.650 1.00 74.37  ? 146 PHE A CE1 1 
ATOM   1132 C  CE2 . PHE A 1 146 ? 10.494  2.131   10.632 1.00 88.29  ? 146 PHE A CE2 1 
ATOM   1133 C  CZ  . PHE A 1 146 ? 9.565   1.125   10.530 1.00 77.42  ? 146 PHE A CZ  1 
ATOM   1134 N  N   . ARG A 1 147 ? 12.232  -0.937  13.780 1.00 64.13  ? 147 ARG A N   1 
ATOM   1135 C  CA  . ARG A 1 147 ? 11.740  -2.333  13.736 1.00 68.22  ? 147 ARG A CA  1 
ATOM   1136 C  C   . ARG A 1 147 ? 12.337  -3.151  14.891 1.00 63.17  ? 147 ARG A C   1 
ATOM   1137 O  O   . ARG A 1 147 ? 13.510  -2.919  15.255 1.00 60.25  ? 147 ARG A O   1 
ATOM   1138 C  CB  . ARG A 1 147 ? 12.067  -2.962  12.379 1.00 75.54  ? 147 ARG A CB  1 
ATOM   1139 C  CG  . ARG A 1 147 ? 11.022  -2.730  11.298 1.00 83.56  ? 147 ARG A CG  1 
ATOM   1140 C  CD  . ARG A 1 147 ? 11.536  -3.152  9.943  1.00 87.77  ? 147 ARG A CD  1 
ATOM   1141 N  NE  . ARG A 1 147 ? 11.976  -1.930  9.296  1.00 90.81  ? 147 ARG A NE  1 
ATOM   1142 C  CZ  . ARG A 1 147 ? 11.368  -1.361  8.272  1.00 90.82  ? 147 ARG A CZ  1 
ATOM   1143 N  NH1 . ARG A 1 147 ? 10.310  -1.969  7.748  1.00 87.11  ? 147 ARG A NH1 1 
ATOM   1144 N  NH2 . ARG A 1 147 ? 11.832  -0.205  7.786  1.00 80.45  ? 147 ARG A NH2 1 
ATOM   1145 N  N   . GLY A 1 148 ? 11.556  -4.112  15.387 1.00 71.76  ? 148 GLY A N   1 
ATOM   1146 C  CA  . GLY A 1 148 ? 11.922  -5.084  16.435 1.00 78.94  ? 148 GLY A CA  1 
ATOM   1147 C  C   . GLY A 1 148 ? 12.083  -6.486  15.882 1.00 78.39  ? 148 GLY A C   1 
ATOM   1148 O  O   . GLY A 1 148 ? 12.319  -7.396  16.660 1.00 107.09 ? 148 GLY A O   1 
ATOM   1149 N  N   . HIS A 1 149 ? 12.006  -6.653  14.571 1.00 82.87  ? 149 HIS A N   1 
ATOM   1150 C  CA  . HIS A 1 149 ? 12.246  -7.953  13.908 1.00 83.07  ? 149 HIS A CA  1 
ATOM   1151 C  C   . HIS A 1 149 ? 12.568  -7.736  12.435 1.00 81.01  ? 149 HIS A C   1 
ATOM   1152 O  O   . HIS A 1 149 ? 12.303  -6.685  11.845 1.00 94.45  ? 149 HIS A O   1 
ATOM   1153 C  CB  . HIS A 1 149 ? 11.032  -8.871  14.122 1.00 90.55  ? 149 HIS A CB  1 
ATOM   1154 C  CG  . HIS A 1 149 ? 9.792   -8.471  13.404 1.00 79.73  ? 149 HIS A CG  1 
ATOM   1155 N  ND1 . HIS A 1 149 ? 8.554   -8.617  13.969 1.00 80.42  ? 149 HIS A ND1 1 
ATOM   1156 C  CD2 . HIS A 1 149 ? 9.599   -7.919  12.191 1.00 85.06  ? 149 HIS A CD2 1 
ATOM   1157 C  CE1 . HIS A 1 149 ? 7.642   -8.207  13.120 1.00 89.69  ? 149 HIS A CE1 1 
ATOM   1158 N  NE2 . HIS A 1 149 ? 8.260   -7.788  12.012 1.00 93.23  ? 149 HIS A NE2 1 
ATOM   1159 N  N   . PRO A 1 150 ? 13.193  -8.737  11.802 1.00 69.22  ? 150 PRO A N   1 
ATOM   1160 C  CA  . PRO A 1 150 ? 13.402  -8.722  10.358 1.00 72.29  ? 150 PRO A CA  1 
ATOM   1161 C  C   . PRO A 1 150 ? 12.183  -9.198  9.576  1.00 71.84  ? 150 PRO A C   1 
ATOM   1162 O  O   . PRO A 1 150 ? 11.546  -10.105 10.050 1.00 75.66  ? 150 PRO A O   1 
ATOM   1163 C  CB  . PRO A 1 150 ? 14.512  -9.751  10.159 1.00 71.79  ? 150 PRO A CB  1 
ATOM   1164 C  CG  . PRO A 1 150 ? 14.362  -10.699 11.322 1.00 77.73  ? 150 PRO A CG  1 
ATOM   1165 C  CD  . PRO A 1 150 ? 13.821  -9.877  12.474 1.00 76.51  ? 150 PRO A CD  1 
ATOM   1166 N  N   . GLU A 1 151 ? 11.881  -8.596  8.430  1.00 72.60  ? 151 GLU A N   1 
ATOM   1167 C  CA  . GLU A 1 151 ? 10.736  -9.099  7.638  1.00 79.34  ? 151 GLU A CA  1 
ATOM   1168 C  C   . GLU A 1 151 ? 11.102  -10.513 7.202  1.00 74.96  ? 151 GLU A C   1 
ATOM   1169 O  O   . GLU A 1 151 ? 10.286  -11.416 7.301  1.00 86.02  ? 151 GLU A O   1 
ATOM   1170 C  CB  . GLU A 1 151 ? 10.340  -8.169  6.496  1.00 89.32  ? 151 GLU A CB  1 
ATOM   1171 C  CG  . GLU A 1 151 ? 9.345   -7.120  6.965  1.00 117.27 ? 151 GLU A CG  1 
ATOM   1172 C  CD  . GLU A 1 151 ? 9.388   -5.807  6.204  1.00 142.19 ? 151 GLU A CD  1 
ATOM   1173 O  OE1 . GLU A 1 151 ? 9.619   -5.855  4.963  1.00 129.34 ? 151 GLU A OE1 1 
ATOM   1174 O  OE2 . GLU A 1 151 ? 9.205   -4.741  6.857  1.00 153.99 ? 151 GLU A OE2 1 
ATOM   1175 N  N   . SER A 1 152 ? 12.325  -10.739 6.795  1.00 76.16  ? 152 SER A N   1 
ATOM   1176 C  CA  . SER A 1 152 ? 12.763  -12.112 6.471  1.00 78.10  ? 152 SER A CA  1 
ATOM   1177 C  C   . SER A 1 152 ? 14.235  -12.178 6.824  1.00 75.50  ? 152 SER A C   1 
ATOM   1178 O  O   . SER A 1 152 ? 14.865  -11.101 6.966  1.00 74.72  ? 152 SER A O   1 
ATOM   1179 C  CB  . SER A 1 152 ? 12.450  -12.501 5.021  1.00 75.35  ? 152 SER A CB  1 
ATOM   1180 O  OG  . SER A 1 152 ? 13.454  -13.334 4.448  1.00 67.29  ? 152 SER A OG  1 
ATOM   1181 N  N   . TYR A 1 153 ? 14.704  -13.397 7.025  1.00 69.09  ? 153 TYR A N   1 
ATOM   1182 C  CA  . TYR A 1 153 ? 16.128  -13.742 7.224  1.00 76.47  ? 153 TYR A CA  1 
ATOM   1183 C  C   . TYR A 1 153 ? 16.805  -13.977 5.853  1.00 71.74  ? 153 TYR A C   1 
ATOM   1184 O  O   . TYR A 1 153 ? 18.033  -14.236 5.803  1.00 71.71  ? 153 TYR A O   1 
ATOM   1185 C  CB  . TYR A 1 153 ? 16.205  -14.939 8.179  1.00 81.06  ? 153 TYR A CB  1 
ATOM   1186 C  CG  . TYR A 1 153 ? 16.101  -14.629 9.651  1.00 71.15  ? 153 TYR A CG  1 
ATOM   1187 C  CD1 . TYR A 1 153 ? 14.881  -14.530 10.291 1.00 70.18  ? 153 TYR A CD1 1 
ATOM   1188 C  CD2 . TYR A 1 153 ? 17.241  -14.466 10.416 1.00 69.70  ? 153 TYR A CD2 1 
ATOM   1189 C  CE1 . TYR A 1 153 ? 14.802  -14.280 11.656 1.00 75.62  ? 153 TYR A CE1 1 
ATOM   1190 C  CE2 . TYR A 1 153 ? 17.179  -14.207 11.773 1.00 68.75  ? 153 TYR A CE2 1 
ATOM   1191 C  CZ  . TYR A 1 153 ? 15.954  -14.108 12.403 1.00 69.47  ? 153 TYR A CZ  1 
ATOM   1192 O  OH  . TYR A 1 153 ? 15.888  -13.868 13.748 1.00 64.57  ? 153 TYR A OH  1 
ATOM   1193 N  N   . PHE A 1 154 ? 16.068  -13.852 4.747  1.00 68.51  ? 154 PHE A N   1 
ATOM   1194 C  CA  . PHE A 1 154 ? 16.643  -13.996 3.385  1.00 72.63  ? 154 PHE A CA  1 
ATOM   1195 C  C   . PHE A 1 154 ? 16.454  -12.696 2.614  1.00 71.76  ? 154 PHE A C   1 
ATOM   1196 O  O   . PHE A 1 154 ? 15.429  -11.977 2.750  1.00 64.42  ? 154 PHE A O   1 
ATOM   1197 C  CB  . PHE A 1 154 ? 16.060  -15.199 2.635  1.00 79.16  ? 154 PHE A CB  1 
ATOM   1198 C  CG  . PHE A 1 154 ? 16.439  -16.505 3.278  1.00 73.70  ? 154 PHE A CG  1 
ATOM   1199 C  CD1 . PHE A 1 154 ? 17.676  -17.081 3.052  1.00 78.63  ? 154 PHE A CD1 1 
ATOM   1200 C  CD2 . PHE A 1 154 ? 15.599  -17.100 4.189  1.00 71.90  ? 154 PHE A CD2 1 
ATOM   1201 C  CE1 . PHE A 1 154 ? 18.055  -18.239 3.709  1.00 79.99  ? 154 PHE A CE1 1 
ATOM   1202 C  CE2 . PHE A 1 154 ? 15.981  -18.256 4.845  1.00 83.75  ? 154 PHE A CE2 1 
ATOM   1203 C  CZ  . PHE A 1 154 ? 17.205  -18.832 4.601  1.00 79.83  ? 154 PHE A CZ  1 
ATOM   1204 N  N   . GLY A 1 155 ? 17.451  -12.413 1.794  1.00 75.55  ? 155 GLY A N   1 
ATOM   1205 C  CA  . GLY A 1 155 ? 17.455  -11.217 0.945  1.00 81.63  ? 155 GLY A CA  1 
ATOM   1206 C  C   . GLY A 1 155 ? 16.325  -11.229 -0.083 1.00 76.15  ? 155 GLY A C   1 
ATOM   1207 O  O   . GLY A 1 155 ? 15.489  -12.119 -0.113 1.00 70.73  ? 155 GLY A O   1 
ATOM   1208 N  N   . PRO A 1 156 ? 16.246  -10.201 -0.941 1.00 80.86  ? 156 PRO A N   1 
ATOM   1209 C  CA  . PRO A 1 156 ? 17.115  -9.028  -0.832 1.00 88.50  ? 156 PRO A CA  1 
ATOM   1210 C  C   . PRO A 1 156 ? 16.783  -8.257  0.456  1.00 85.79  ? 156 PRO A C   1 
ATOM   1211 O  O   . PRO A 1 156 ? 15.710  -8.529  0.996  1.00 74.70  ? 156 PRO A O   1 
ATOM   1212 C  CB  . PRO A 1 156 ? 16.758  -8.229  -2.090 1.00 90.06  ? 156 PRO A CB  1 
ATOM   1213 C  CG  . PRO A 1 156 ? 15.308  -8.588  -2.303 1.00 88.71  ? 156 PRO A CG  1 
ATOM   1214 C  CD  . PRO A 1 156 ? 15.274  -10.081 -2.028 1.00 88.09  ? 156 PRO A CD  1 
ATOM   1215 N  N   . PHE A 1 157 ? 17.684  -7.375  0.924  1.00 76.24  ? 157 PHE A N   1 
ATOM   1216 C  CA  . PHE A 1 157 ? 17.466  -6.534  2.133  1.00 74.40  ? 157 PHE A CA  1 
ATOM   1217 C  C   . PHE A 1 157 ? 17.373  -5.051  1.767  1.00 76.92  ? 157 PHE A C   1 
ATOM   1218 O  O   . PHE A 1 157 ? 17.897  -4.618  0.720  1.00 74.58  ? 157 PHE A O   1 
ATOM   1219 C  CB  . PHE A 1 157 ? 18.568  -6.751  3.159  1.00 67.29  ? 157 PHE A CB  1 
ATOM   1220 C  CG  . PHE A 1 157 ? 18.693  -8.178  3.611  1.00 70.75  ? 157 PHE A CG  1 
ATOM   1221 C  CD1 . PHE A 1 157 ? 17.658  -8.812  4.275  1.00 72.52  ? 157 PHE A CD1 1 
ATOM   1222 C  CD2 . PHE A 1 157 ? 19.854  -8.891  3.376  1.00 75.51  ? 157 PHE A CD2 1 
ATOM   1223 C  CE1 . PHE A 1 157 ? 17.792  -10.123 4.701  1.00 72.75  ? 157 PHE A CE1 1 
ATOM   1224 C  CE2 . PHE A 1 157 ? 19.981  -10.206 3.802  1.00 72.30  ? 157 PHE A CE2 1 
ATOM   1225 C  CZ  . PHE A 1 157 ? 18.945  -10.824 4.447  1.00 68.00  ? 157 PHE A CZ  1 
ATOM   1226 N  N   . ASP A 1 158 ? 16.674  -4.286  2.599  1.00 72.64  ? 158 ASP A N   1 
ATOM   1227 C  CA  . ASP A 1 158 ? 16.494  -2.836  2.357  1.00 78.70  ? 158 ASP A CA  1 
ATOM   1228 C  C   . ASP A 1 158 ? 16.444  -2.136  3.709  1.00 76.10  ? 158 ASP A C   1 
ATOM   1229 O  O   . ASP A 1 158 ? 15.367  -1.680  4.142  1.00 72.11  ? 158 ASP A O   1 
ATOM   1230 C  CB  . ASP A 1 158 ? 15.298  -2.523  1.463  1.00 73.63  ? 158 ASP A CB  1 
ATOM   1231 C  CG  . ASP A 1 158 ? 15.297  -1.077  1.000  1.00 80.61  ? 158 ASP A CG  1 
ATOM   1232 O  OD1 . ASP A 1 158 ? 16.174  -0.269  1.452  1.00 91.59  ? 158 ASP A OD1 1 
ATOM   1233 O  OD2 . ASP A 1 158 ? 14.434  -0.762  0.184  1.00 98.40  ? 158 ASP A OD2 1 
ATOM   1234 N  N   . LEU A 1 159 ? 17.616  -2.047  4.313  1.00 73.55  ? 159 LEU A N   1 
ATOM   1235 C  CA  . LEU A 1 159 ? 17.814  -1.417  5.627  1.00 71.71  ? 159 LEU A CA  1 
ATOM   1236 C  C   . LEU A 1 159 ? 18.985  -0.448  5.544  1.00 71.12  ? 159 LEU A C   1 
ATOM   1237 O  O   . LEU A 1 159 ? 19.805  -0.522  4.632  1.00 77.16  ? 159 LEU A O   1 
ATOM   1238 C  CB  . LEU A 1 159 ? 18.081  -2.544  6.616  1.00 66.97  ? 159 LEU A CB  1 
ATOM   1239 C  CG  . LEU A 1 159 ? 16.867  -3.371  7.023  1.00 62.56  ? 159 LEU A CG  1 
ATOM   1240 C  CD1 . LEU A 1 159 ? 17.324  -4.668  7.636  1.00 64.38  ? 159 LEU A CD1 1 
ATOM   1241 C  CD2 . LEU A 1 159 ? 16.031  -2.635  8.051  1.00 76.83  ? 159 LEU A CD2 1 
ATOM   1242 N  N   . PRO A 1 160 ? 19.086  0.499   6.498  1.00 69.11  ? 160 PRO A N   1 
ATOM   1243 C  CA  . PRO A 1 160 ? 20.156  1.497   6.485  1.00 71.04  ? 160 PRO A CA  1 
ATOM   1244 C  C   . PRO A 1 160 ? 21.567  0.907   6.335  1.00 66.74  ? 160 PRO A C   1 
ATOM   1245 O  O   . PRO A 1 160 ? 21.968  0.150   7.179  1.00 65.75  ? 160 PRO A O   1 
ATOM   1246 C  CB  . PRO A 1 160 ? 19.958  2.217   7.825  1.00 67.44  ? 160 PRO A CB  1 
ATOM   1247 C  CG  . PRO A 1 160 ? 18.465  2.110   8.034  1.00 66.55  ? 160 PRO A CG  1 
ATOM   1248 C  CD  . PRO A 1 160 ? 18.137  0.701   7.601  1.00 67.51  ? 160 PRO A CD  1 
ATOM   1249 N  N   . ASN A 1 161 ? 22.256  1.253   5.242  1.00 62.31  ? 161 ASN A N   1 
ATOM   1250 C  CA  . ASN A 1 161 ? 23.653  0.840   4.987  1.00 63.20  ? 161 ASN A CA  1 
ATOM   1251 C  C   . ASN A 1 161 ? 23.741  -0.683  4.916  1.00 64.62  ? 161 ASN A C   1 
ATOM   1252 O  O   . ASN A 1 161 ? 24.831  -1.239  5.100  1.00 66.01  ? 161 ASN A O   1 
ATOM   1253 C  CB  . ASN A 1 161 ? 24.541  1.371   6.099  1.00 62.31  ? 161 ASN A CB  1 
ATOM   1254 C  CG  . ASN A 1 161 ? 25.270  2.621   5.689  1.00 64.96  ? 161 ASN A CG  1 
ATOM   1255 O  OD1 . ASN A 1 161 ? 25.823  2.721   4.580  1.00 76.80  ? 161 ASN A OD1 1 
ATOM   1256 N  ND2 . ASN A 1 161 ? 25.298  3.554   6.614  1.00 62.93  ? 161 ASN A ND2 1 
ATOM   1257 N  N   . PHE A 1 162 ? 22.603  -1.326  4.716  1.00 66.34  ? 162 PHE A N   1 
ATOM   1258 C  CA  . PHE A 1 162 ? 22.469  -2.793  4.620  1.00 63.29  ? 162 PHE A CA  1 
ATOM   1259 C  C   . PHE A 1 162 ? 21.446  -3.060  3.534  1.00 67.15  ? 162 PHE A C   1 
ATOM   1260 O  O   . PHE A 1 162 ? 20.264  -3.374  3.832  1.00 65.11  ? 162 PHE A O   1 
ATOM   1261 C  CB  . PHE A 1 162 ? 22.001  -3.390  5.940  1.00 62.45  ? 162 PHE A CB  1 
ATOM   1262 C  CG  . PHE A 1 162 ? 22.240  -4.868  6.042  1.00 61.39  ? 162 PHE A CG  1 
ATOM   1263 C  CD1 . PHE A 1 162 ? 23.535  -5.346  6.154  1.00 70.83  ? 162 PHE A CD1 1 
ATOM   1264 C  CD2 . PHE A 1 162 ? 21.193  -5.775  6.026  1.00 62.16  ? 162 PHE A CD2 1 
ATOM   1265 C  CE1 . PHE A 1 162 ? 23.786  -6.706  6.258  1.00 76.01  ? 162 PHE A CE1 1 
ATOM   1266 C  CE2 . PHE A 1 162 ? 21.441  -7.135  6.142  1.00 67.15  ? 162 PHE A CE2 1 
ATOM   1267 C  CZ  . PHE A 1 162 ? 22.737  -7.598  6.263  1.00 74.02  ? 162 PHE A CZ  1 
ATOM   1268 N  N   . ARG A 1 163 ? 21.872  -2.879  2.293  1.00 70.19  ? 163 ARG A N   1 
ATOM   1269 C  CA  . ARG A 1 163 ? 20.886  -2.779  1.201  1.00 73.56  ? 163 ARG A CA  1 
ATOM   1270 C  C   . ARG A 1 163 ? 21.263  -3.739  0.083  1.00 71.83  ? 163 ARG A C   1 
ATOM   1271 O  O   . ARG A 1 163 ? 22.303  -3.514  -0.520 1.00 78.36  ? 163 ARG A O   1 
ATOM   1272 C  CB  . ARG A 1 163 ? 20.829  -1.325  0.752  1.00 77.31  ? 163 ARG A CB  1 
ATOM   1273 C  CG  . ARG A 1 163 ? 19.457  -0.920  0.264  1.00 77.04  ? 163 ARG A CG  1 
ATOM   1274 C  CD  . ARG A 1 163 ? 19.424  0.568   0.031  1.00 78.21  ? 163 ARG A CD  1 
ATOM   1275 N  NE  . ARG A 1 163 ? 19.451  0.836   -1.398 1.00 79.48  ? 163 ARG A NE  1 
ATOM   1276 C  CZ  . ARG A 1 163 ? 18.376  0.831   -2.181 1.00 84.19  ? 163 ARG A CZ  1 
ATOM   1277 N  NH1 . ARG A 1 163 ? 17.187  0.563   -1.672 1.00 89.07  ? 163 ARG A NH1 1 
ATOM   1278 N  NH2 . ARG A 1 163 ? 18.479  1.107   -3.471 1.00 99.91  ? 163 ARG A NH2 1 
ATOM   1279 N  N   . GLY A 1 164 ? 20.471  -4.802  -0.083 1.00 78.20  ? 164 GLY A N   1 
ATOM   1280 C  CA  . GLY A 1 164 ? 20.406  -5.659  -1.276 1.00 83.76  ? 164 GLY A CA  1 
ATOM   1281 C  C   . GLY A 1 164 ? 21.318  -6.854  -1.165 1.00 82.71  ? 164 GLY A C   1 
ATOM   1282 O  O   . GLY A 1 164 ? 22.525  -6.717  -1.257 1.00 120.99 ? 164 GLY A O   1 
ATOM   1283 N  N   . TRP A 1 165 ? 20.779  -8.035  -1.093 1.00 69.81  ? 165 TRP A N   1 
ATOM   1284 C  CA  . TRP A 1 165 ? 21.580  -9.202  -1.515 1.00 68.76  ? 165 TRP A CA  1 
ATOM   1285 C  C   . TRP A 1 165 ? 20.603  -10.053 -2.320 1.00 80.85  ? 165 TRP A C   1 
ATOM   1286 O  O   . TRP A 1 165 ? 19.825  -9.413  -3.029 1.00 94.36  ? 165 TRP A O   1 
ATOM   1287 C  CB  . TRP A 1 165 ? 22.154  -9.836  -0.267 1.00 70.84  ? 165 TRP A CB  1 
ATOM   1288 C  CG  . TRP A 1 165 ? 23.487  -9.347  0.195  1.00 68.25  ? 165 TRP A CG  1 
ATOM   1289 C  CD1 . TRP A 1 165 ? 24.655  -9.969  -0.100 1.00 70.10  ? 165 TRP A CD1 1 
ATOM   1290 C  CD2 . TRP A 1 165 ? 23.827  -8.301  1.139  1.00 71.99  ? 165 TRP A CD2 1 
ATOM   1291 N  NE1 . TRP A 1 165 ? 25.697  -9.376  0.560  1.00 72.17  ? 165 TRP A NE1 1 
ATOM   1292 C  CE2 . TRP A 1 165 ? 25.229  -8.341  1.312  1.00 67.37  ? 165 TRP A CE2 1 
ATOM   1293 C  CE3 . TRP A 1 165 ? 23.129  -7.295  1.815  1.00 75.46  ? 165 TRP A CE3 1 
ATOM   1294 C  CZ2 . TRP A 1 165 ? 25.936  -7.435  2.095  1.00 71.38  ? 165 TRP A CZ2 1 
ATOM   1295 C  CZ3 . TRP A 1 165 ? 23.829  -6.395  2.599  1.00 76.93  ? 165 TRP A CZ3 1 
ATOM   1296 C  CH2 . TRP A 1 165 ? 25.216  -6.449  2.720  1.00 76.51  ? 165 TRP A CH2 1 
ATOM   1297 N  N   . THR A 1 166 ? 20.527  -11.382 -2.158 1.00 79.51  ? 166 THR A N   1 
ATOM   1298 C  CA  . THR A 1 166 ? 19.503  -12.140 -2.946 1.00 81.08  ? 166 THR A CA  1 
ATOM   1299 C  C   . THR A 1 166 ? 18.676  -13.084 -2.055 1.00 80.04  ? 166 THR A C   1 
ATOM   1300 O  O   . THR A 1 166 ? 19.059  -13.268 -0.883 1.00 70.24  ? 166 THR A O   1 
ATOM   1301 C  CB  . THR A 1 166 ? 20.146  -12.900 -4.114 1.00 80.77  ? 166 THR A CB  1 
ATOM   1302 O  OG1 . THR A 1 166 ? 19.165  -13.009 -5.146 1.00 124.02 ? 166 THR A OG1 1 
ATOM   1303 C  CG2 . THR A 1 166 ? 20.635  -14.280 -3.735 1.00 80.01  ? 166 THR A CG2 1 
ATOM   1304 N  N   . LYS A 1 167 ? 17.600  -13.665 -2.588 1.00 80.79  ? 167 LYS A N   1 
ATOM   1305 C  CA  . LYS A 1 167 ? 16.731  -14.568 -1.786 1.00 87.44  ? 167 LYS A CA  1 
ATOM   1306 C  C   . LYS A 1 167 ? 17.542  -15.774 -1.292 1.00 76.64  ? 167 LYS A C   1 
ATOM   1307 O  O   . LYS A 1 167 ? 16.947  -16.643 -0.627 1.00 85.37  ? 167 LYS A O   1 
ATOM   1308 C  CB  . LYS A 1 167 ? 15.538  -15.024 -2.629 1.00 94.18  ? 167 LYS A CB  1 
ATOM   1309 C  CG  . LYS A 1 167 ? 15.767  -14.994 -4.134 1.00 112.02 ? 167 LYS A CG  1 
ATOM   1310 C  CD  . LYS A 1 167 ? 16.699  -16.084 -4.616 1.00 118.86 ? 167 LYS A CD  1 
ATOM   1311 C  CE  . LYS A 1 167 ? 16.277  -17.462 -4.152 1.00 143.14 ? 167 LYS A CE  1 
ATOM   1312 N  NZ  . LYS A 1 167 ? 14.877  -17.764 -4.532 1.00 200.07 ? 167 LYS A NZ  1 
ATOM   1313 N  N   . ASN A 1 168 ? 18.841  -15.823 -1.602 1.00 75.75  ? 168 ASN A N   1 
ATOM   1314 C  CA  . ASN A 1 168 ? 19.695  -16.981 -1.218 1.00 78.57  ? 168 ASN A CA  1 
ATOM   1315 C  C   . ASN A 1 168 ? 20.695  -16.572 -0.152 1.00 78.58  ? 168 ASN A C   1 
ATOM   1316 O  O   . ASN A 1 168 ? 21.528  -17.410 0.177  1.00 77.78  ? 168 ASN A O   1 
ATOM   1317 C  CB  . ASN A 1 168 ? 20.477  -17.547 -2.405 1.00 85.06  ? 168 ASN A CB  1 
ATOM   1318 C  CG  . ASN A 1 168 ? 19.565  -18.253 -3.379 1.00 99.88  ? 168 ASN A CG  1 
ATOM   1319 O  OD1 . ASN A 1 168 ? 19.516  -17.912 -4.554 1.00 116.05 ? 168 ASN A OD1 1 
ATOM   1320 N  ND2 . ASN A 1 168 ? 18.780  -19.192 -2.879 1.00 114.13 ? 168 ASN A ND2 1 
ATOM   1321 N  N   . ASP A 1 169 ? 20.632  -15.330 0.326  1.00 82.15  ? 169 ASP A N   1 
ATOM   1322 C  CA  . ASP A 1 169 ? 21.626  -14.783 1.279  1.00 79.34  ? 169 ASP A CA  1 
ATOM   1323 C  C   . ASP A 1 169 ? 20.950  -14.745 2.651  1.00 77.39  ? 169 ASP A C   1 
ATOM   1324 O  O   . ASP A 1 169 ? 19.807  -14.224 2.745  1.00 69.58  ? 169 ASP A O   1 
ATOM   1325 C  CB  . ASP A 1 169 ? 22.142  -13.434 0.778  1.00 84.73  ? 169 ASP A CB  1 
ATOM   1326 C  CG  . ASP A 1 169 ? 23.065  -13.481 -0.440 1.00 89.10  ? 169 ASP A CG  1 
ATOM   1327 O  OD1 . ASP A 1 169 ? 24.290  -13.579 -0.230 1.00 98.01  ? 169 ASP A OD1 1 
ATOM   1328 O  OD2 . ASP A 1 169 ? 22.570  -13.330 -1.592 1.00 81.84  ? 169 ASP A OD2 1 
ATOM   1329 N  N   . TYR A 1 170 ? 21.586  -15.340 3.660  1.00 74.80  ? 170 TYR A N   1 
ATOM   1330 C  CA  . TYR A 1 170 ? 21.011  -15.410 5.025  1.00 76.49  ? 170 TYR A CA  1 
ATOM   1331 C  C   . TYR A 1 170 ? 21.467  -14.174 5.807  1.00 76.40  ? 170 TYR A C   1 
ATOM   1332 O  O   . TYR A 1 170 ? 22.672  -13.809 5.799  1.00 74.37  ? 170 TYR A O   1 
ATOM   1333 C  CB  . TYR A 1 170 ? 21.375  -16.728 5.711  1.00 81.00  ? 170 TYR A CB  1 
ATOM   1334 C  CG  . TYR A 1 170 ? 20.616  -17.048 6.984  1.00 73.93  ? 170 TYR A CG  1 
ATOM   1335 C  CD1 . TYR A 1 170 ? 19.241  -17.226 6.994  1.00 68.25  ? 170 TYR A CD1 1 
ATOM   1336 C  CD2 . TYR A 1 170 ? 21.292  -17.209 8.189  1.00 78.22  ? 170 TYR A CD2 1 
ATOM   1337 C  CE1 . TYR A 1 170 ? 18.565  -17.548 8.161  1.00 76.28  ? 170 TYR A CE1 1 
ATOM   1338 C  CE2 . TYR A 1 170 ? 20.628  -17.490 9.375  1.00 81.53  ? 170 TYR A CE2 1 
ATOM   1339 C  CZ  . TYR A 1 170 ? 19.258  -17.685 9.353  1.00 81.62  ? 170 TYR A CZ  1 
ATOM   1340 O  OH  . TYR A 1 170 ? 18.591  -17.972 10.508 1.00 82.85  ? 170 TYR A OH  1 
ATOM   1341 N  N   . LEU A 1 171 ? 20.504  -13.548 6.478  1.00 68.41  ? 171 LEU A N   1 
ATOM   1342 C  CA  . LEU A 1 171 ? 20.693  -12.297 7.248  1.00 66.68  ? 171 LEU A CA  1 
ATOM   1343 C  C   . LEU A 1 171 ? 21.856  -12.453 8.225  1.00 63.21  ? 171 LEU A C   1 
ATOM   1344 O  O   . LEU A 1 171 ? 22.747  -11.639 8.201  1.00 65.80  ? 171 LEU A O   1 
ATOM   1345 C  CB  . LEU A 1 171 ? 19.395  -11.978 7.988  1.00 67.10  ? 171 LEU A CB  1 
ATOM   1346 C  CG  . LEU A 1 171 ? 19.412  -10.759 8.907  1.00 68.99  ? 171 LEU A CG  1 
ATOM   1347 C  CD1 . LEU A 1 171 ? 19.977  -9.532  8.212  1.00 69.70  ? 171 LEU A CD1 1 
ATOM   1348 C  CD2 . LEU A 1 171 ? 18.005  -10.476 9.409  1.00 70.57  ? 171 LEU A CD2 1 
ATOM   1349 N  N   . THR A 1 172 ? 21.804  -13.426 9.117  1.00 64.50  ? 172 THR A N   1 
ATOM   1350 C  CA  . THR A 1 172 ? 22.822  -13.588 10.179 1.00 74.05  ? 172 THR A CA  1 
ATOM   1351 C  C   . THR A 1 172 ? 24.224  -13.661 9.547  1.00 74.81  ? 172 THR A C   1 
ATOM   1352 O  O   . THR A 1 172 ? 25.178  -13.116 10.145 1.00 67.70  ? 172 THR A O   1 
ATOM   1353 C  CB  . THR A 1 172 ? 22.463  -14.799 11.033 1.00 77.19  ? 172 THR A CB  1 
ATOM   1354 O  OG1 . THR A 1 172 ? 21.195  -14.473 11.607 1.00 74.84  ? 172 THR A OG1 1 
ATOM   1355 C  CG2 . THR A 1 172 ? 23.513  -15.098 12.077 1.00 81.28  ? 172 THR A CG2 1 
ATOM   1356 N  N   . ASP A 1 173 ? 24.337  -14.288 8.372  1.00 84.84  ? 173 ASP A N   1 
ATOM   1357 C  CA  . ASP A 1 173 ? 25.618  -14.465 7.627  1.00 83.19  ? 173 ASP A CA  1 
ATOM   1358 C  C   . ASP A 1 173 ? 26.071  -13.099 7.117  1.00 70.98  ? 173 ASP A C   1 
ATOM   1359 O  O   . ASP A 1 173 ? 27.185  -12.696 7.457  1.00 77.48  ? 173 ASP A O   1 
ATOM   1360 C  CB  . ASP A 1 173 ? 25.501  -15.466 6.469  1.00 86.03  ? 173 ASP A CB  1 
ATOM   1361 C  CG  . ASP A 1 173 ? 25.324  -16.920 6.893  1.00 97.88  ? 173 ASP A CG  1 
ATOM   1362 O  OD1 . ASP A 1 173 ? 25.404  -17.233 8.136  1.00 94.88  ? 173 ASP A OD1 1 
ATOM   1363 O  OD2 . ASP A 1 173 ? 25.092  -17.730 5.983  1.00 92.95  ? 173 ASP A OD2 1 
ATOM   1364 N  N   . ARG A 1 174 ? 25.215  -12.390 6.384  1.00 65.06  ? 174 ARG A N   1 
ATOM   1365 C  CA  . ARG A 1 174 ? 25.562  -11.088 5.739  1.00 69.35  ? 174 ARG A CA  1 
ATOM   1366 C  C   . ARG A 1 174 ? 25.797  -9.983  6.793  1.00 70.13  ? 174 ARG A C   1 
ATOM   1367 O  O   . ARG A 1 174 ? 26.756  -9.178  6.665  1.00 62.94  ? 174 ARG A O   1 
ATOM   1368 C  CB  . ARG A 1 174 ? 24.448  -10.683 4.773  1.00 74.33  ? 174 ARG A CB  1 
ATOM   1369 C  CG  . ARG A 1 174 ? 24.220  -11.671 3.641  1.00 78.59  ? 174 ARG A CG  1 
ATOM   1370 C  CD  . ARG A 1 174 ? 25.364  -11.625 2.652  1.00 82.36  ? 174 ARG A CD  1 
ATOM   1371 N  NE  . ARG A 1 174 ? 26.443  -12.557 2.913  1.00 87.31  ? 174 ARG A NE  1 
ATOM   1372 C  CZ  . ARG A 1 174 ? 26.429  -13.823 2.542  1.00 82.91  ? 174 ARG A CZ  1 
ATOM   1373 N  NH1 . ARG A 1 174 ? 25.363  -14.311 1.926  1.00 78.45  ? 174 ARG A NH1 1 
ATOM   1374 N  NH2 . ARG A 1 174 ? 27.455  -14.602 2.841  1.00 84.74  ? 174 ARG A NH2 1 
ATOM   1375 N  N   . LEU A 1 175 ? 24.959  -9.909  7.820  1.00 71.54  ? 175 LEU A N   1 
ATOM   1376 C  CA  . LEU A 1 175 ? 25.216  -8.982  8.943  1.00 69.89  ? 175 LEU A CA  1 
ATOM   1377 C  C   . LEU A 1 175 ? 26.638  -9.224  9.451  1.00 65.96  ? 175 LEU A C   1 
ATOM   1378 O  O   . LEU A 1 175 ? 27.360  -8.238  9.668  1.00 73.12  ? 175 LEU A O   1 
ATOM   1379 C  CB  . LEU A 1 175 ? 24.183  -9.199  10.048 1.00 72.59  ? 175 LEU A CB  1 
ATOM   1380 C  CG  . LEU A 1 175 ? 24.343  -8.272  11.247 1.00 74.50  ? 175 LEU A CG  1 
ATOM   1381 C  CD1 . LEU A 1 175 ? 24.250  -6.826  10.819 1.00 83.43  ? 175 LEU A CD1 1 
ATOM   1382 C  CD2 . LEU A 1 175 ? 23.294  -8.553  12.290 1.00 84.61  ? 175 LEU A CD2 1 
ATOM   1383 N  N   . THR A 1 176 ? 27.040  -10.483 9.616  1.00 66.17  ? 176 THR A N   1 
ATOM   1384 C  CA  . THR A 1 176 ? 28.389  -10.810 10.143 1.00 71.82  ? 176 THR A CA  1 
ATOM   1385 C  C   . THR A 1 176 ? 29.451  -10.257 9.173  1.00 69.71  ? 176 THR A C   1 
ATOM   1386 O  O   . THR A 1 176 ? 30.381  -9.581  9.643  1.00 68.30  ? 176 THR A O   1 
ATOM   1387 C  CB  . THR A 1 176 ? 28.539  -12.308 10.432 1.00 74.37  ? 176 THR A CB  1 
ATOM   1388 O  OG1 . THR A 1 176 ? 27.776  -12.681 11.582 1.00 72.24  ? 176 THR A OG1 1 
ATOM   1389 C  CG2 . THR A 1 176 ? 29.986  -12.658 10.674 1.00 79.95  ? 176 THR A CG2 1 
ATOM   1390 N  N   . ASP A 1 177 ? 29.334  -10.521 7.872  1.00 71.20  ? 177 ASP A N   1 
ATOM   1391 C  CA  . ASP A 1 177 ? 30.315  -9.947  6.912  1.00 73.09  ? 177 ASP A CA  1 
ATOM   1392 C  C   . ASP A 1 177 ? 30.464  -8.440  7.150  1.00 68.70  ? 177 ASP A C   1 
ATOM   1393 O  O   . ASP A 1 177 ? 31.615  -7.963  7.181  1.00 67.67  ? 177 ASP A O   1 
ATOM   1394 C  CB  . ASP A 1 177 ? 29.907  -10.229 5.466  1.00 78.48  ? 177 ASP A CB  1 
ATOM   1395 C  CG  . ASP A 1 177 ? 29.231  -11.576 5.283  1.00 84.66  ? 177 ASP A CG  1 
ATOM   1396 O  OD1 . ASP A 1 177 ? 29.607  -12.520 6.000  1.00 85.41  ? 177 ASP A OD1 1 
ATOM   1397 O  OD2 . ASP A 1 177 ? 28.340  -11.669 4.421  1.00 83.36  ? 177 ASP A OD2 1 
ATOM   1398 N  N   . LYS A 1 178 ? 29.352  -7.726  7.327  1.00 64.58  ? 178 LYS A N   1 
ATOM   1399 C  CA  . LYS A 1 178 ? 29.359  -6.245  7.481  1.00 65.77  ? 178 LYS A CA  1 
ATOM   1400 C  C   . LYS A 1 178 ? 30.054  -5.845  8.788  1.00 62.36  ? 178 LYS A C   1 
ATOM   1401 O  O   . LYS A 1 178 ? 30.614  -4.725  8.835  1.00 71.72  ? 178 LYS A O   1 
ATOM   1402 C  CB  . LYS A 1 178 ? 27.941  -5.678  7.363  1.00 64.61  ? 178 LYS A CB  1 
ATOM   1403 C  CG  . LYS A 1 178 ? 27.506  -5.331  5.942  1.00 64.08  ? 178 LYS A CG  1 
ATOM   1404 C  CD  . LYS A 1 178 ? 28.479  -4.289  5.345  1.00 75.42  ? 178 LYS A CD  1 
ATOM   1405 C  CE  . LYS A 1 178 ? 27.945  -3.102  4.560  1.00 74.68  ? 178 LYS A CE  1 
ATOM   1406 N  NZ  . LYS A 1 178 ? 27.816  -3.457  3.125  1.00 79.78  ? 178 LYS A NZ  1 
ATOM   1407 N  N   . ALA A 1 179 ? 30.027  -6.708  9.795  1.00 63.06  ? 179 ALA A N   1 
ATOM   1408 C  CA  . ALA A 1 179 ? 30.677  -6.455  11.100 1.00 68.63  ? 179 ALA A CA  1 
ATOM   1409 C  C   . ALA A 1 179 ? 32.171  -6.701  10.933 1.00 64.57  ? 179 ALA A C   1 
ATOM   1410 O  O   . ALA A 1 179 ? 32.950  -5.875  11.400 1.00 60.98  ? 179 ALA A O   1 
ATOM   1411 C  CB  . ALA A 1 179 ? 30.085  -7.327  12.186 1.00 75.22  ? 179 ALA A CB  1 
ATOM   1412 N  N   . LEU A 1 180 ? 32.532  -7.806  10.281 1.00 65.96  ? 180 LEU A N   1 
ATOM   1413 C  CA  . LEU A 1 180 ? 33.934  -8.074  9.891  1.00 71.99  ? 180 LEU A CA  1 
ATOM   1414 C  C   . LEU A 1 180 ? 34.417  -6.842  9.118  1.00 71.49  ? 180 LEU A C   1 
ATOM   1415 O  O   . LEU A 1 180 ? 35.583  -6.391  9.351  1.00 67.68  ? 180 LEU A O   1 
ATOM   1416 C  CB  . LEU A 1 180 ? 34.053  -9.338  9.025  1.00 79.84  ? 180 LEU A CB  1 
ATOM   1417 C  CG  . LEU A 1 180 ? 33.742  -10.699 9.660  1.00 83.26  ? 180 LEU A CG  1 
ATOM   1418 C  CD1 . LEU A 1 180 ? 34.500  -11.796 8.911  1.00 104.75 ? 180 LEU A CD1 1 
ATOM   1419 C  CD2 . LEU A 1 180 ? 34.063  -10.762 11.149 1.00 74.54  ? 180 LEU A CD2 1 
ATOM   1420 N  N   . GLN A 1 181 ? 33.569  -6.277  8.250  1.00 63.50  ? 181 GLN A N   1 
ATOM   1421 C  CA  . GLN A 1 181 ? 34.003  -5.117  7.422  1.00 66.28  ? 181 GLN A CA  1 
ATOM   1422 C  C   . GLN A 1 181 ? 34.493  -4.013  8.347  1.00 65.36  ? 181 GLN A C   1 
ATOM   1423 O  O   . GLN A 1 181 ? 35.515  -3.396  8.014  1.00 57.60  ? 181 GLN A O   1 
ATOM   1424 C  CB  . GLN A 1 181 ? 32.895  -4.530  6.552  1.00 75.28  ? 181 GLN A CB  1 
ATOM   1425 C  CG  . GLN A 1 181 ? 33.276  -3.248  5.822  1.00 71.75  ? 181 GLN A CG  1 
ATOM   1426 C  CD  . GLN A 1 181 ? 32.159  -2.795  4.913  1.00 79.91  ? 181 GLN A CD  1 
ATOM   1427 O  OE1 . GLN A 1 181 ? 31.009  -2.589  5.350  1.00 75.08  ? 181 GLN A OE1 1 
ATOM   1428 N  NE2 . GLN A 1 181 ? 32.495  -2.665  3.636  1.00 74.26  ? 181 GLN A NE2 1 
ATOM   1429 N  N   . PHE A 1 182 ? 33.745  -3.757  9.425  1.00 70.48  ? 182 PHE A N   1 
ATOM   1430 C  CA  . PHE A 1 182 ? 34.043  -2.704  10.424 1.00 65.30  ? 182 PHE A CA  1 
ATOM   1431 C  C   . PHE A 1 182 ? 35.349  -3.035  11.140 1.00 61.86  ? 182 PHE A C   1 
ATOM   1432 O  O   . PHE A 1 182 ? 36.156  -2.143  11.393 1.00 62.90  ? 182 PHE A O   1 
ATOM   1433 C  CB  . PHE A 1 182 ? 32.902  -2.569  11.423 1.00 71.33  ? 182 PHE A CB  1 
ATOM   1434 C  CG  . PHE A 1 182 ? 33.186  -1.605  12.541 1.00 62.53  ? 182 PHE A CG  1 
ATOM   1435 C  CD1 . PHE A 1 182 ? 32.970  -0.255  12.373 1.00 63.50  ? 182 PHE A CD1 1 
ATOM   1436 C  CD2 . PHE A 1 182 ? 33.665  -2.044  13.756 1.00 65.44  ? 182 PHE A CD2 1 
ATOM   1437 C  CE1 . PHE A 1 182 ? 33.232  0.640   13.397 1.00 66.82  ? 182 PHE A CE1 1 
ATOM   1438 C  CE2 . PHE A 1 182 ? 33.931  -1.147  14.780 1.00 72.29  ? 182 PHE A CE2 1 
ATOM   1439 C  CZ  . PHE A 1 182 ? 33.710  0.195   14.602 1.00 70.27  ? 182 PHE A CZ  1 
ATOM   1440 N  N   . LEU A 1 183 ? 35.559  -4.302  11.467 1.00 67.23  ? 183 LEU A N   1 
ATOM   1441 C  CA  . LEU A 1 183 ? 36.789  -4.723  12.173 1.00 67.69  ? 183 LEU A CA  1 
ATOM   1442 C  C   . LEU A 1 183 ? 37.971  -4.494  11.245 1.00 65.42  ? 183 LEU A C   1 
ATOM   1443 O  O   . LEU A 1 183 ? 38.976  -3.940  11.743 1.00 60.90  ? 183 LEU A O   1 
ATOM   1444 C  CB  . LEU A 1 183 ? 36.630  -6.181  12.589 1.00 71.97  ? 183 LEU A CB  1 
ATOM   1445 C  CG  . LEU A 1 183 ? 35.598  -6.375  13.695 1.00 74.60  ? 183 LEU A CG  1 
ATOM   1446 C  CD1 . LEU A 1 183 ? 35.429  -7.837  14.073 1.00 72.87  ? 183 LEU A CD1 1 
ATOM   1447 C  CD2 . LEU A 1 183 ? 35.998  -5.550  14.908 1.00 75.34  ? 183 LEU A CD2 1 
ATOM   1448 N  N   . GLU A 1 184 ? 37.814  -4.851  9.960  1.00 65.14  ? 184 GLU A N   1 
ATOM   1449 C  CA  . GLU A 1 184 ? 38.880  -4.711  8.924  1.00 73.08  ? 184 GLU A CA  1 
ATOM   1450 C  C   . GLU A 1 184 ? 39.193  -3.214  8.768  1.00 68.84  ? 184 GLU A C   1 
ATOM   1451 O  O   . GLU A 1 184 ? 40.387  -2.863  8.798  1.00 70.26  ? 184 GLU A O   1 
ATOM   1452 C  CB  . GLU A 1 184 ? 38.488  -5.406  7.610  1.00 76.11  ? 184 GLU A CB  1 
ATOM   1453 C  CG  . GLU A 1 184 ? 38.449  -6.935  7.702  1.00 86.20  ? 184 GLU A CG  1 
ATOM   1454 C  CD  . GLU A 1 184 ? 37.557  -7.708  6.722  1.00 89.87  ? 184 GLU A CD  1 
ATOM   1455 O  OE1 . GLU A 1 184 ? 36.991  -7.091  5.800  1.00 88.32  ? 184 GLU A OE1 1 
ATOM   1456 O  OE2 . GLU A 1 184 ? 37.400  -8.948  6.894  1.00 100.60 ? 184 GLU A OE2 1 
ATOM   1457 N  N   . GLU A 1 185 ? 38.163  -2.360  8.663  1.00 63.28  ? 185 GLU A N   1 
ATOM   1458 C  CA  . GLU A 1 185 ? 38.306  -0.893  8.450  1.00 59.52  ? 185 GLU A CA  1 
ATOM   1459 C  C   . GLU A 1 185 ? 39.053  -0.307  9.645  1.00 64.17  ? 185 GLU A C   1 
ATOM   1460 O  O   . GLU A 1 185 ? 40.002  0.421   9.440  1.00 74.02  ? 185 GLU A O   1 
ATOM   1461 C  CB  . GLU A 1 185 ? 36.951  -0.196  8.325  1.00 65.49  ? 185 GLU A CB  1 
ATOM   1462 C  CG  . GLU A 1 185 ? 36.407  -0.040  6.913  1.00 70.83  ? 185 GLU A CG  1 
ATOM   1463 C  CD  . GLU A 1 185 ? 34.890  0.164   6.742  1.00 82.73  ? 185 GLU A CD  1 
ATOM   1464 O  OE1 . GLU A 1 185 ? 34.104  0.344   7.764  1.00 87.28  ? 185 GLU A OE1 1 
ATOM   1465 O  OE2 . GLU A 1 185 ? 34.464  0.132   5.564  1.00 79.18  ? 185 GLU A OE2 1 
ATOM   1466 N  N   . ASN A 1 186 ? 38.664  -0.649  10.865 1.00 66.92  ? 186 ASN A N   1 
ATOM   1467 C  CA  . ASN A 1 186 ? 39.206  0.014   12.077 1.00 72.77  ? 186 ASN A CA  1 
ATOM   1468 C  C   . ASN A 1 186 ? 40.219  -0.880  12.783 1.00 69.01  ? 186 ASN A C   1 
ATOM   1469 O  O   . ASN A 1 186 ? 40.398  -0.702  13.989 1.00 63.21  ? 186 ASN A O   1 
ATOM   1470 C  CB  . ASN A 1 186 ? 38.060  0.391   13.007 1.00 73.99  ? 186 ASN A CB  1 
ATOM   1471 C  CG  . ASN A 1 186 ? 37.130  1.346   12.309 1.00 68.56  ? 186 ASN A CG  1 
ATOM   1472 O  OD1 . ASN A 1 186 ? 37.435  2.517   12.204 1.00 67.80  ? 186 ASN A OD1 1 
ATOM   1473 N  ND2 . ASN A 1 186 ? 36.040  0.844   11.773 1.00 71.24  ? 186 ASN A ND2 1 
ATOM   1474 N  N   . ARG A 1 187 ? 40.827  -1.818  12.065 1.00 72.47  ? 187 ARG A N   1 
ATOM   1475 C  CA  . ARG A 1 187 ? 41.853  -2.738  12.615 1.00 74.89  ? 187 ARG A CA  1 
ATOM   1476 C  C   . ARG A 1 187 ? 42.803  -1.928  13.510 1.00 74.06  ? 187 ARG A C   1 
ATOM   1477 O  O   . ARG A 1 187 ? 43.259  -2.470  14.529 1.00 73.01  ? 187 ARG A O   1 
ATOM   1478 C  CB  . ARG A 1 187 ? 42.599  -3.426  11.469 1.00 83.95  ? 187 ARG A CB  1 
ATOM   1479 C  CG  . ARG A 1 187 ? 43.258  -2.437  10.512 1.00 110.37 ? 187 ARG A CG  1 
ATOM   1480 C  CD  . ARG A 1 187 ? 43.566  -2.956  9.124  1.00 110.40 ? 187 ARG A CD  1 
ATOM   1481 N  NE  . ARG A 1 187 ? 44.321  -4.175  9.318  1.00 123.78 ? 187 ARG A NE  1 
ATOM   1482 C  CZ  . ARG A 1 187 ? 44.253  -5.247  8.542  1.00 141.42 ? 187 ARG A CZ  1 
ATOM   1483 N  NH1 . ARG A 1 187 ? 43.449  -5.275  7.483  1.00 128.60 ? 187 ARG A NH1 1 
ATOM   1484 N  NH2 . ARG A 1 187 ? 45.002  -6.296  8.852  1.00 140.96 ? 187 ARG A NH2 1 
ATOM   1485 N  N   . GLN A 1 188 ? 43.169  -0.707  13.123 1.00 71.30  ? 188 GLN A N   1 
ATOM   1486 C  CA  . GLN A 1 188 ? 44.250  0.004   13.866 1.00 73.84  ? 188 GLN A CA  1 
ATOM   1487 C  C   . GLN A 1 188 ? 43.734  1.039   14.858 1.00 72.50  ? 188 GLN A C   1 
ATOM   1488 O  O   . GLN A 1 188 ? 44.569  1.712   15.478 1.00 72.45  ? 188 GLN A O   1 
ATOM   1489 C  CB  . GLN A 1 188 ? 45.151  0.727   12.871 1.00 83.59  ? 188 GLN A CB  1 
ATOM   1490 C  CG  . GLN A 1 188 ? 45.857  -0.202  11.899 1.00 84.26  ? 188 GLN A CG  1 
ATOM   1491 C  CD  . GLN A 1 188 ? 46.569  0.587   10.830 1.00 88.48  ? 188 GLN A CD  1 
ATOM   1492 O  OE1 . GLN A 1 188 ? 46.090  0.720   9.707  1.00 93.64  ? 188 GLN A OE1 1 
ATOM   1493 N  NE2 . GLN A 1 188 ? 47.721  1.132   11.181 1.00 108.79 ? 188 GLN A NE2 1 
ATOM   1494 N  N   . ARG A 1 189 ? 42.425  1.156   15.011 1.00 81.36  ? 189 ARG A N   1 
ATOM   1495 C  CA  . ARG A 1 189 ? 41.854  2.189   15.884 1.00 75.18  ? 189 ARG A CA  1 
ATOM   1496 C  C   . ARG A 1 189 ? 41.198  1.547   17.080 1.00 78.35  ? 189 ARG A C   1 
ATOM   1497 O  O   . ARG A 1 189 ? 40.845  0.370   17.058 1.00 75.57  ? 189 ARG A O   1 
ATOM   1498 C  CB  . ARG A 1 189 ? 40.835  2.987   15.095 1.00 81.20  ? 189 ARG A CB  1 
ATOM   1499 C  CG  . ARG A 1 189 ? 41.524  3.855   14.062 1.00 91.16  ? 189 ARG A CG  1 
ATOM   1500 C  CD  . ARG A 1 189 ? 40.585  4.922   13.575 1.00 86.90  ? 189 ARG A CD  1 
ATOM   1501 N  NE  . ARG A 1 189 ? 39.952  4.343   12.417 1.00 78.94  ? 189 ARG A NE  1 
ATOM   1502 C  CZ  . ARG A 1 189 ? 40.206  4.691   11.171 1.00 69.87  ? 189 ARG A CZ  1 
ATOM   1503 N  NH1 . ARG A 1 189 ? 41.054  5.661   10.887 1.00 63.28  ? 189 ARG A NH1 1 
ATOM   1504 N  NH2 . ARG A 1 189 ? 39.560  4.088   10.201 1.00 75.72  ? 189 ARG A NH2 1 
ATOM   1505 N  N   . PRO A 1 190 ? 41.065  2.339   18.156 1.00 73.62  ? 190 PRO A N   1 
ATOM   1506 C  CA  . PRO A 1 190 ? 40.228  1.959   19.285 1.00 67.59  ? 190 PRO A CA  1 
ATOM   1507 C  C   . PRO A 1 190 ? 38.753  2.027   18.864 1.00 61.59  ? 190 PRO A C   1 
ATOM   1508 O  O   . PRO A 1 190 ? 38.328  3.052   18.348 1.00 60.35  ? 190 PRO A O   1 
ATOM   1509 C  CB  . PRO A 1 190 ? 40.607  2.997   20.350 1.00 68.66  ? 190 PRO A CB  1 
ATOM   1510 C  CG  . PRO A 1 190 ? 41.053  4.199   19.554 1.00 69.50  ? 190 PRO A CG  1 
ATOM   1511 C  CD  . PRO A 1 190 ? 41.739  3.631   18.334 1.00 68.90  ? 190 PRO A CD  1 
ATOM   1512 N  N   . PHE A 1 191 ? 38.002  0.949   19.072 1.00 58.54  ? 191 PHE A N   1 
ATOM   1513 C  CA  . PHE A 1 191 ? 36.588  0.901   18.633 1.00 63.86  ? 191 PHE A CA  1 
ATOM   1514 C  C   . PHE A 1 191 ? 35.670  0.258   19.669 1.00 64.04  ? 191 PHE A C   1 
ATOM   1515 O  O   . PHE A 1 191 ? 36.088  -0.510  20.537 1.00 63.82  ? 191 PHE A O   1 
ATOM   1516 C  CB  . PHE A 1 191 ? 36.418  0.162   17.304 1.00 65.88  ? 191 PHE A CB  1 
ATOM   1517 C  CG  . PHE A 1 191 ? 36.845  -1.274  17.320 1.00 59.06  ? 191 PHE A CG  1 
ATOM   1518 C  CD1 . PHE A 1 191 ? 35.982  -2.245  17.738 1.00 62.50  ? 191 PHE A CD1 1 
ATOM   1519 C  CD2 . PHE A 1 191 ? 38.113  -1.637  16.919 1.00 69.02  ? 191 PHE A CD2 1 
ATOM   1520 C  CE1 . PHE A 1 191 ? 36.390  -3.564  17.753 1.00 72.92  ? 191 PHE A CE1 1 
ATOM   1521 C  CE2 . PHE A 1 191 ? 38.522  -2.952  16.941 1.00 67.38  ? 191 PHE A CE2 1 
ATOM   1522 C  CZ  . PHE A 1 191 ? 37.655  -3.914  17.356 1.00 68.68  ? 191 PHE A CZ  1 
ATOM   1523 N  N   . PHE A 1 192 ? 34.401  0.601   19.515 1.00 59.59  ? 192 PHE A N   1 
ATOM   1524 C  CA  . PHE A 1 192 ? 33.268  0.015   20.239 1.00 59.27  ? 192 PHE A CA  1 
ATOM   1525 C  C   . PHE A 1 192 ? 32.241  -0.428  19.199 1.00 59.08  ? 192 PHE A C   1 
ATOM   1526 O  O   . PHE A 1 192 ? 31.793  0.384   18.394 1.00 59.07  ? 192 PHE A O   1 
ATOM   1527 C  CB  . PHE A 1 192 ? 32.712  1.015   21.251 1.00 59.72  ? 192 PHE A CB  1 
ATOM   1528 C  CG  . PHE A 1 192 ? 31.361  0.601   21.757 1.00 61.66  ? 192 PHE A CG  1 
ATOM   1529 C  CD1 . PHE A 1 192 ? 31.168  -0.658  22.271 1.00 64.83  ? 192 PHE A CD1 1 
ATOM   1530 C  CD2 . PHE A 1 192 ? 30.275  1.435   21.654 1.00 72.72  ? 192 PHE A CD2 1 
ATOM   1531 C  CE1 . PHE A 1 192 ? 29.925  -1.070  22.701 1.00 69.57  ? 192 PHE A CE1 1 
ATOM   1532 C  CE2 . PHE A 1 192 ? 29.030  1.022   22.082 1.00 73.49  ? 192 PHE A CE2 1 
ATOM   1533 C  CZ  . PHE A 1 192 ? 28.856  -0.233  22.597 1.00 70.72  ? 192 PHE A CZ  1 
ATOM   1534 N  N   . LEU A 1 193 ? 31.893  -1.706  19.220 1.00 59.77  ? 193 LEU A N   1 
ATOM   1535 C  CA  . LEU A 1 193 ? 30.884  -2.284  18.312 1.00 59.06  ? 193 LEU A CA  1 
ATOM   1536 C  C   . LEU A 1 193 ? 29.743  -2.859  19.147 1.00 62.19  ? 193 LEU A C   1 
ATOM   1537 O  O   . LEU A 1 193 ? 29.991  -3.799  19.926 1.00 77.18  ? 193 LEU A O   1 
ATOM   1538 C  CB  . LEU A 1 193 ? 31.563  -3.362  17.467 1.00 61.98  ? 193 LEU A CB  1 
ATOM   1539 C  CG  . LEU A 1 193 ? 30.640  -4.148  16.536 1.00 70.30  ? 193 LEU A CG  1 
ATOM   1540 C  CD1 . LEU A 1 193 ? 30.045  -3.249  15.465 1.00 79.77  ? 193 LEU A CD1 1 
ATOM   1541 C  CD2 . LEU A 1 193 ? 31.365  -5.314  15.874 1.00 75.42  ? 193 LEU A CD2 1 
ATOM   1542 N  N   . TYR A 1 194 ? 28.539  -2.314  18.982 1.00 64.92  ? 194 TYR A N   1 
ATOM   1543 C  CA  . TYR A 1 194 ? 27.259  -2.907  19.466 1.00 62.59  ? 194 TYR A CA  1 
ATOM   1544 C  C   . TYR A 1 194 ? 26.761  -3.801  18.323 1.00 59.90  ? 194 TYR A C   1 
ATOM   1545 O  O   . TYR A 1 194 ? 26.320  -3.283  17.295 1.00 63.22  ? 194 TYR A O   1 
ATOM   1546 C  CB  . TYR A 1 194 ? 26.329  -1.780  19.948 1.00 62.79  ? 194 TYR A CB  1 
ATOM   1547 C  CG  . TYR A 1 194 ? 24.925  -2.118  20.391 1.00 58.94  ? 194 TYR A CG  1 
ATOM   1548 C  CD1 . TYR A 1 194 ? 24.624  -2.538  21.668 1.00 60.46  ? 194 TYR A CD1 1 
ATOM   1549 C  CD2 . TYR A 1 194 ? 23.856  -1.868  19.556 1.00 73.02  ? 194 TYR A CD2 1 
ATOM   1550 C  CE1 . TYR A 1 194 ? 23.313  -2.781  22.074 1.00 62.67  ? 194 TYR A CE1 1 
ATOM   1551 C  CE2 . TYR A 1 194 ? 22.547  -2.121  19.930 1.00 81.11  ? 194 TYR A CE2 1 
ATOM   1552 C  CZ  . TYR A 1 194 ? 22.252  -2.585  21.198 1.00 70.83  ? 194 TYR A CZ  1 
ATOM   1553 O  OH  . TYR A 1 194 ? 20.906  -2.807  21.453 1.00 60.56  ? 194 TYR A OH  1 
ATOM   1554 N  N   . LEU A 1 195 ? 26.922  -5.120  18.456 1.00 64.31  ? 195 LEU A N   1 
ATOM   1555 C  CA  . LEU A 1 195 ? 26.526  -6.122  17.423 1.00 61.26  ? 195 LEU A CA  1 
ATOM   1556 C  C   . LEU A 1 195 ? 25.258  -6.843  17.884 1.00 58.82  ? 195 LEU A C   1 
ATOM   1557 O  O   . LEU A 1 195 ? 25.358  -7.844  18.620 1.00 60.75  ? 195 LEU A O   1 
ATOM   1558 C  CB  . LEU A 1 195 ? 27.677  -7.110  17.198 1.00 62.16  ? 195 LEU A CB  1 
ATOM   1559 C  CG  . LEU A 1 195 ? 27.437  -8.162  16.123 1.00 61.22  ? 195 LEU A CG  1 
ATOM   1560 C  CD1 . LEU A 1 195 ? 26.852  -7.524  14.884 1.00 62.06  ? 195 LEU A CD1 1 
ATOM   1561 C  CD2 . LEU A 1 195 ? 28.719  -8.896  15.788 1.00 66.24  ? 195 LEU A CD2 1 
ATOM   1562 N  N   . ALA A 1 196 ? 24.096  -6.330  17.501 1.00 60.35  ? 196 ALA A N   1 
ATOM   1563 C  CA  . ALA A 1 196 ? 22.791  -6.862  17.953 1.00 72.46  ? 196 ALA A CA  1 
ATOM   1564 C  C   . ALA A 1 196 ? 22.222  -7.746  16.861 1.00 71.75  ? 196 ALA A C   1 
ATOM   1565 O  O   . ALA A 1 196 ? 21.643  -7.196  15.914 1.00 78.43  ? 196 ALA A O   1 
ATOM   1566 C  CB  . ALA A 1 196 ? 21.842  -5.740  18.259 1.00 85.89  ? 196 ALA A CB  1 
ATOM   1567 N  N   . HIS A 1 197 ? 22.420  -9.055  16.942 1.00 73.61  ? 197 HIS A N   1 
ATOM   1568 C  CA  . HIS A 1 197 ? 21.905  -9.951  15.876 1.00 76.64  ? 197 HIS A CA  1 
ATOM   1569 C  C   . HIS A 1 197 ? 20.400  -9.807  15.917 1.00 72.04  ? 197 HIS A C   1 
ATOM   1570 O  O   . HIS A 1 197 ? 19.886  -9.468  17.045 1.00 68.89  ? 197 HIS A O   1 
ATOM   1571 C  CB  . HIS A 1 197 ? 22.341  -11.408 16.030 1.00 79.27  ? 197 HIS A CB  1 
ATOM   1572 C  CG  . HIS A 1 197 ? 23.672  -11.667 15.451 1.00 77.90  ? 197 HIS A CG  1 
ATOM   1573 N  ND1 . HIS A 1 197 ? 23.806  -12.012 14.124 1.00 80.69  ? 197 HIS A ND1 1 
ATOM   1574 C  CD2 . HIS A 1 197 ? 24.906  -11.620 16.017 1.00 66.60  ? 197 HIS A CD2 1 
ATOM   1575 C  CE1 . HIS A 1 197 ? 25.109  -12.158 13.891 1.00 91.00  ? 197 HIS A CE1 1 
ATOM   1576 N  NE2 . HIS A 1 197 ? 25.804  -11.922 15.043 1.00 73.66  ? 197 HIS A NE2 1 
ATOM   1577 N  N   . PHE A 1 198 ? 19.764  -10.019 14.763 1.00 70.49  ? 198 PHE A N   1 
ATOM   1578 C  CA  . PHE A 1 198 ? 18.293  -10.145 14.676 1.00 79.20  ? 198 PHE A CA  1 
ATOM   1579 C  C   . PHE A 1 198 ? 17.917  -11.513 15.210 1.00 77.93  ? 198 PHE A C   1 
ATOM   1580 O  O   . PHE A 1 198 ? 16.804  -11.603 15.765 1.00 88.28  ? 198 PHE A O   1 
ATOM   1581 C  CB  . PHE A 1 198 ? 17.795  -9.962  13.251 1.00 83.28  ? 198 PHE A CB  1 
ATOM   1582 C  CG  . PHE A 1 198 ? 18.023  -8.575  12.731 1.00 72.22  ? 198 PHE A CG  1 
ATOM   1583 C  CD1 . PHE A 1 198 ? 17.124  -7.572  13.018 1.00 75.08  ? 198 PHE A CD1 1 
ATOM   1584 C  CD2 . PHE A 1 198 ? 19.145  -8.278  11.994 1.00 70.84  ? 198 PHE A CD2 1 
ATOM   1585 C  CE1 . PHE A 1 198 ? 17.334  -6.287  12.563 1.00 77.01  ? 198 PHE A CE1 1 
ATOM   1586 C  CE2 . PHE A 1 198 ? 19.345  -6.997  11.524 1.00 78.80  ? 198 PHE A CE2 1 
ATOM   1587 C  CZ  . PHE A 1 198 ? 18.438  -6.004  11.806 1.00 83.03  ? 198 PHE A CZ  1 
ATOM   1588 N  N   . ALA A 1 199 ? 18.811  -12.491 15.013 1.00 69.94  ? 199 ALA A N   1 
ATOM   1589 C  CA  . ALA A 1 199 ? 18.702  -13.846 15.589 1.00 69.19  ? 199 ALA A CA  1 
ATOM   1590 C  C   . ALA A 1 199 ? 18.654  -13.704 17.101 1.00 69.17  ? 199 ALA A C   1 
ATOM   1591 O  O   . ALA A 1 199 ? 19.504  -13.040 17.676 1.00 68.95  ? 199 ALA A O   1 
ATOM   1592 C  CB  . ALA A 1 199 ? 19.869  -14.681 15.163 1.00 80.56  ? 199 ALA A CB  1 
ATOM   1593 N  N   . VAL A 1 200 ? 17.683  -14.350 17.751 1.00 71.95  ? 200 VAL A N   1 
ATOM   1594 C  CA  . VAL A 1 200 ? 16.924  -15.449 17.185 1.00 71.60  ? 200 VAL A CA  1 
ATOM   1595 C  C   . VAL A 1 200 ? 15.432  -15.106 17.262 1.00 63.61  ? 200 VAL A C   1 
ATOM   1596 O  O   . VAL A 1 200 ? 14.655  -16.001 17.543 1.00 78.94  ? 200 VAL A O   1 
ATOM   1597 C  CB  . VAL A 1 200 ? 17.272  -16.772 17.915 1.00 75.31  ? 200 VAL A CB  1 
ATOM   1598 C  CG1 . VAL A 1 200 ? 18.687  -17.246 17.617 1.00 74.76  ? 200 VAL A CG1 1 
ATOM   1599 C  CG2 . VAL A 1 200 ? 17.107  -16.681 19.425 1.00 77.75  ? 200 VAL A CG2 1 
ATOM   1600 N  N   . HIS A 1 201 ? 15.044  -13.859 17.018 1.00 67.08  ? 201 HIS A N   1 
ATOM   1601 C  CA  . HIS A 1 201 ? 13.634  -13.375 17.092 1.00 75.89  ? 201 HIS A CA  1 
ATOM   1602 C  C   . HIS A 1 201 ? 12.847  -14.098 16.003 1.00 74.77  ? 201 HIS A C   1 
ATOM   1603 O  O   . HIS A 1 201 ? 13.449  -14.422 14.929 1.00 59.24  ? 201 HIS A O   1 
ATOM   1604 C  CB  . HIS A 1 201 ? 13.540  -11.835 16.916 1.00 82.59  ? 201 HIS A CB  1 
ATOM   1605 C  CG  . HIS A 1 201 ? 12.245  -11.226 17.330 1.00 71.43  ? 201 HIS A CG  1 
ATOM   1606 N  ND1 . HIS A 1 201 ? 11.104  -11.354 16.575 1.00 91.65  ? 201 HIS A ND1 1 
ATOM   1607 C  CD2 . HIS A 1 201 ? 11.906  -10.467 18.396 1.00 80.52  ? 201 HIS A CD2 1 
ATOM   1608 C  CE1 . HIS A 1 201 ? 10.104  -10.710 17.155 1.00 107.75 ? 201 HIS A CE1 1 
ATOM   1609 N  NE2 . HIS A 1 201 ? 10.570  -10.148 18.285 1.00 98.76  ? 201 HIS A NE2 1 
ATOM   1610 N  N   . THR A 1 202 ? 11.555  -14.314 16.245 1.00 72.71  ? 202 THR A N   1 
ATOM   1611 C  CA  . THR A 1 202 ? 10.629  -14.672 15.151 1.00 77.18  ? 202 THR A CA  1 
ATOM   1612 C  C   . THR A 1 202 ? 10.827  -13.650 14.029 1.00 76.68  ? 202 THR A C   1 
ATOM   1613 O  O   . THR A 1 202 ? 11.173  -12.501 14.269 1.00 76.05  ? 202 THR A O   1 
ATOM   1614 C  CB  . THR A 1 202 ? 9.180   -14.786 15.639 1.00 79.12  ? 202 THR A CB  1 
ATOM   1615 O  OG1 . THR A 1 202 ? 8.688   -13.551 16.159 1.00 80.73  ? 202 THR A OG1 1 
ATOM   1616 C  CG2 . THR A 1 202 ? 9.047   -15.876 16.674 1.00 84.72  ? 202 THR A CG2 1 
ATOM   1617 N  N   . PRO A 1 203 ? 10.588  -13.997 12.753 1.00 73.44  ? 203 PRO A N   1 
ATOM   1618 C  CA  . PRO A 1 203 ? 10.145  -15.333 12.342 1.00 76.19  ? 203 PRO A CA  1 
ATOM   1619 C  C   . PRO A 1 203 ? 11.221  -16.422 12.272 1.00 82.33  ? 203 PRO A C   1 
ATOM   1620 O  O   . PRO A 1 203 ? 12.304  -16.111 11.865 1.00 97.06  ? 203 PRO A O   1 
ATOM   1621 C  CB  . PRO A 1 203 ? 9.651   -15.108 10.917 1.00 71.07  ? 203 PRO A CB  1 
ATOM   1622 C  CG  . PRO A 1 203 ? 10.472  -13.940 10.442 1.00 78.10  ? 203 PRO A CG  1 
ATOM   1623 C  CD  . PRO A 1 203 ? 10.610  -13.040 11.648 1.00 77.90  ? 203 PRO A CD  1 
ATOM   1624 N  N   . LEU A 1 204 ? 10.881  -17.659 12.663 1.00 91.00  ? 204 LEU A N   1 
ATOM   1625 C  CA  . LEU A 1 204 ? 11.769  -18.843 12.525 1.00 86.05  ? 204 LEU A CA  1 
ATOM   1626 C  C   . LEU A 1 204 ? 11.999  -19.088 11.033 1.00 77.72  ? 204 LEU A C   1 
ATOM   1627 O  O   . LEU A 1 204 ? 11.052  -19.553 10.385 1.00 90.45  ? 204 LEU A O   1 
ATOM   1628 C  CB  . LEU A 1 204 ? 11.126  -20.084 13.154 1.00 88.18  ? 204 LEU A CB  1 
ATOM   1629 C  CG  . LEU A 1 204 ? 10.887  -20.102 14.664 1.00 87.75  ? 204 LEU A CG  1 
ATOM   1630 C  CD1 . LEU A 1 204 ? 11.933  -19.308 15.420 1.00 78.15  ? 204 LEU A CD1 1 
ATOM   1631 C  CD2 . LEU A 1 204 ? 9.487   -19.602 14.979 1.00 100.73 ? 204 LEU A CD2 1 
ATOM   1632 N  N   . GLN A 1 205 ? 13.179  -18.747 10.508 1.00 70.55  ? 205 GLN A N   1 
ATOM   1633 C  CA  . GLN A 1 205 ? 13.637  -19.135 9.143  1.00 72.51  ? 205 GLN A CA  1 
ATOM   1634 C  C   . GLN A 1 205 ? 15.124  -19.465 9.206  1.00 80.98  ? 205 GLN A C   1 
ATOM   1635 O  O   . GLN A 1 205 ? 15.852  -18.788 9.997  1.00 74.28  ? 205 GLN A O   1 
ATOM   1636 C  CB  . GLN A 1 205 ? 13.441  -18.013 8.135  1.00 68.61  ? 205 GLN A CB  1 
ATOM   1637 C  CG  . GLN A 1 205 ? 12.068  -17.376 8.209  1.00 71.89  ? 205 GLN A CG  1 
ATOM   1638 C  CD  . GLN A 1 205 ? 11.980  -16.099 7.419  1.00 68.38  ? 205 GLN A CD  1 
ATOM   1639 O  OE1 . GLN A 1 205 ? 12.969  -15.500 7.035  1.00 72.11  ? 205 GLN A OE1 1 
ATOM   1640 N  NE2 . GLN A 1 205 ? 10.771  -15.640 7.202  1.00 74.33  ? 205 GLN A NE2 1 
ATOM   1641 N  N   . ALA A 1 206 ? 15.560  -20.456 8.425  1.00 81.46  ? 206 ALA A N   1 
ATOM   1642 C  CA  . ALA A 1 206 ? 16.982  -20.873 8.375  1.00 79.35  ? 206 ALA A CA  1 
ATOM   1643 C  C   . ALA A 1 206 ? 17.263  -21.645 7.077  1.00 82.29  ? 206 ALA A C   1 
ATOM   1644 O  O   . ALA A 1 206 ? 16.307  -21.949 6.329  1.00 86.51  ? 206 ALA A O   1 
ATOM   1645 C  CB  . ALA A 1 206 ? 17.312  -21.666 9.623  1.00 73.66  ? 206 ALA A CB  1 
ATOM   1646 N  N   . LYS A 1 207 ? 18.531  -21.953 6.817  1.00 78.03  ? 207 LYS A N   1 
ATOM   1647 C  CA  . LYS A 1 207 ? 18.956  -22.767 5.652  1.00 94.79  ? 207 LYS A CA  1 
ATOM   1648 C  C   . LYS A 1 207 ? 18.306  -24.159 5.739  1.00 105.19 ? 207 LYS A C   1 
ATOM   1649 O  O   . LYS A 1 207 ? 18.350  -24.755 6.839  1.00 102.26 ? 207 LYS A O   1 
ATOM   1650 C  CB  . LYS A 1 207 ? 20.484  -22.827 5.633  1.00 97.81  ? 207 LYS A CB  1 
ATOM   1651 C  CG  . LYS A 1 207 ? 21.134  -21.469 5.819  1.00 97.54  ? 207 LYS A CG  1 
ATOM   1652 C  CD  . LYS A 1 207 ? 22.478  -21.297 5.173  1.00 95.51  ? 207 LYS A CD  1 
ATOM   1653 C  CE  . LYS A 1 207 ? 23.260  -20.198 5.854  1.00 102.01 ? 207 LYS A CE  1 
ATOM   1654 N  NZ  . LYS A 1 207 ? 24.715  -20.398 5.719  1.00 111.24 ? 207 LYS A NZ  1 
ATOM   1655 N  N   . ALA A 1 208 ? 17.739  -24.663 4.628  1.00 98.73  ? 208 ALA A N   1 
ATOM   1656 C  CA  . ALA A 1 208 ? 17.002  -25.951 4.545  1.00 94.00  ? 208 ALA A CA  1 
ATOM   1657 C  C   . ALA A 1 208 ? 17.886  -27.138 4.995  1.00 99.27  ? 208 ALA A C   1 
ATOM   1658 O  O   . ALA A 1 208 ? 17.446  -27.893 5.878  1.00 94.20  ? 208 ALA A O   1 
ATOM   1659 C  CB  . ALA A 1 208 ? 16.472  -26.132 3.145  1.00 88.35  ? 208 ALA A CB  1 
ATOM   1660 N  N   . GLU A 1 209 ? 19.080  -27.301 4.411  1.00 97.99  ? 209 GLU A N   1 
ATOM   1661 C  CA  . GLU A 1 209 ? 20.101  -28.342 4.747  1.00 96.65  ? 209 GLU A CA  1 
ATOM   1662 C  C   . GLU A 1 209 ? 20.364  -28.333 6.254  1.00 88.42  ? 209 GLU A C   1 
ATOM   1663 O  O   . GLU A 1 209 ? 20.448  -29.399 6.834  1.00 103.51 ? 209 GLU A O   1 
ATOM   1664 C  CB  . GLU A 1 209 ? 21.439  -28.121 4.025  1.00 108.65 ? 209 GLU A CB  1 
ATOM   1665 C  CG  . GLU A 1 209 ? 21.340  -27.284 2.749  1.00 138.20 ? 209 GLU A CG  1 
ATOM   1666 C  CD  . GLU A 1 209 ? 20.996  -25.797 2.922  1.00 147.83 ? 209 GLU A CD  1 
ATOM   1667 O  OE1 . GLU A 1 209 ? 21.874  -25.015 3.377  1.00 121.13 ? 209 GLU A OE1 1 
ATOM   1668 O  OE2 . GLU A 1 209 ? 19.835  -25.406 2.600  1.00 145.27 ? 209 GLU A OE2 1 
ATOM   1669 N  N   . MET A 1 210 ? 20.488  -27.169 6.877  1.00 92.16  ? 210 MET A N   1 
ATOM   1670 C  CA  . MET A 1 210 ? 20.778  -27.081 8.331  1.00 93.63  ? 210 MET A CA  1 
ATOM   1671 C  C   . MET A 1 210 ? 19.535  -27.502 9.137  1.00 95.44  ? 210 MET A C   1 
ATOM   1672 O  O   . MET A 1 210 ? 19.702  -28.222 10.150 1.00 89.94  ? 210 MET A O   1 
ATOM   1673 C  CB  . MET A 1 210 ? 21.203  -25.662 8.709  1.00 97.57  ? 210 MET A CB  1 
ATOM   1674 C  CG  . MET A 1 210 ? 22.103  -25.617 9.927  1.00 102.14 ? 210 MET A CG  1 
ATOM   1675 S  SD  . MET A 1 210 ? 22.842  -23.970 10.197 1.00 108.04 ? 210 MET A SD  1 
ATOM   1676 C  CE  . MET A 1 210 ? 24.058  -23.836 8.883  1.00 110.59 ? 210 MET A CE  1 
ATOM   1677 N  N   . ILE A 1 211 ? 18.331  -27.089 8.717  1.00 88.58  ? 211 ILE A N   1 
ATOM   1678 C  CA  . ILE A 1 211 ? 17.051  -27.524 9.364  1.00 96.49  ? 211 ILE A CA  1 
ATOM   1679 C  C   . ILE A 1 211 ? 17.007  -29.059 9.343  1.00 106.37 ? 211 ILE A C   1 
ATOM   1680 O  O   . ILE A 1 211 ? 16.777  -29.695 10.398 1.00 98.90  ? 211 ILE A O   1 
ATOM   1681 C  CB  . ILE A 1 211 ? 15.803  -26.942 8.663  1.00 94.30  ? 211 ILE A CB  1 
ATOM   1682 C  CG1 . ILE A 1 211 ? 15.638  -25.436 8.870  1.00 102.09 ? 211 ILE A CG1 1 
ATOM   1683 C  CG2 . ILE A 1 211 ? 14.561  -27.690 9.110  1.00 87.39  ? 211 ILE A CG2 1 
ATOM   1684 C  CD1 . ILE A 1 211 ? 14.509  -24.805 8.048  1.00 106.79 ? 211 ILE A CD1 1 
ATOM   1685 N  N   . ALA A 1 212 ? 17.193  -29.649 8.165  1.00 106.24 ? 212 ALA A N   1 
ATOM   1686 C  CA  . ALA A 1 212 ? 17.180  -31.116 7.986  1.00 102.32 ? 212 ALA A CA  1 
ATOM   1687 C  C   . ALA A 1 212 ? 18.033  -31.774 9.092  1.00 97.13  ? 212 ALA A C   1 
ATOM   1688 O  O   . ALA A 1 212 ? 17.538  -32.725 9.733  1.00 84.83  ? 212 ALA A O   1 
ATOM   1689 C  CB  . ALA A 1 212 ? 17.648  -31.450 6.588  1.00 103.89 ? 212 ALA A CB  1 
ATOM   1690 N  N   . LYS A 1 213 ? 19.247  -31.271 9.355  1.00 85.54  ? 213 LYS A N   1 
ATOM   1691 C  CA  . LYS A 1 213 ? 20.155  -31.842 10.385 1.00 87.45  ? 213 LYS A CA  1 
ATOM   1692 C  C   . LYS A 1 213 ? 19.401  -32.008 11.712 1.00 93.90  ? 213 LYS A C   1 
ATOM   1693 O  O   . LYS A 1 213 ? 19.636  -33.013 12.447 1.00 101.30 ? 213 LYS A O   1 
ATOM   1694 C  CB  . LYS A 1 213 ? 21.381  -30.954 10.591 1.00 90.66  ? 213 LYS A CB  1 
ATOM   1695 C  CG  . LYS A 1 213 ? 22.182  -31.245 11.854 1.00 93.44  ? 213 LYS A CG  1 
ATOM   1696 C  CD  . LYS A 1 213 ? 23.180  -30.163 12.141 1.00 99.52  ? 213 LYS A CD  1 
ATOM   1697 C  CE  . LYS A 1 213 ? 24.329  -30.625 13.000 1.00 99.36  ? 213 LYS A CE  1 
ATOM   1698 N  NZ  . LYS A 1 213 ? 25.472  -29.712 12.791 1.00 109.60 ? 213 LYS A NZ  1 
ATOM   1699 N  N   . TYR A 1 214 ? 18.558  -31.040 12.052 1.00 93.80  ? 214 TYR A N   1 
ATOM   1700 C  CA  . TYR A 1 214 ? 18.004  -30.939 13.421 1.00 97.40  ? 214 TYR A CA  1 
ATOM   1701 C  C   . TYR A 1 214 ? 16.647  -31.641 13.483 1.00 93.61  ? 214 TYR A C   1 
ATOM   1702 O  O   . TYR A 1 214 ? 16.270  -31.975 14.611 1.00 98.17  ? 214 TYR A O   1 
ATOM   1703 C  CB  . TYR A 1 214 ? 17.991  -29.479 13.879 1.00 100.08 ? 214 TYR A CB  1 
ATOM   1704 C  CG  . TYR A 1 214 ? 19.342  -28.899 14.238 1.00 95.68  ? 214 TYR A CG  1 
ATOM   1705 C  CD1 . TYR A 1 214 ? 20.027  -29.306 15.376 1.00 97.90  ? 214 TYR A CD1 1 
ATOM   1706 C  CD2 . TYR A 1 214 ? 19.931  -27.915 13.463 1.00 91.59  ? 214 TYR A CD2 1 
ATOM   1707 C  CE1 . TYR A 1 214 ? 21.249  -28.759 15.736 1.00 92.73  ? 214 TYR A CE1 1 
ATOM   1708 C  CE2 . TYR A 1 214 ? 21.158  -27.360 13.809 1.00 95.90  ? 214 TYR A CE2 1 
ATOM   1709 C  CZ  . TYR A 1 214 ? 21.818  -27.776 14.954 1.00 89.15  ? 214 TYR A CZ  1 
ATOM   1710 O  OH  . TYR A 1 214 ? 23.004  -27.228 15.344 1.00 82.94  ? 214 TYR A OH  1 
ATOM   1711 N  N   . GLU A 1 215 ? 15.970  -31.889 12.350 1.00 92.24  ? 215 GLU A N   1 
ATOM   1712 C  CA  . GLU A 1 215 ? 14.766  -32.772 12.323 1.00 93.02  ? 215 GLU A CA  1 
ATOM   1713 C  C   . GLU A 1 215 ? 15.253  -34.190 12.642 1.00 100.75 ? 215 GLU A C   1 
ATOM   1714 O  O   . GLU A 1 215 ? 14.604  -34.847 13.463 1.00 101.06 ? 215 GLU A O   1 
ATOM   1715 C  CB  . GLU A 1 215 ? 14.022  -32.788 10.988 1.00 93.68  ? 215 GLU A CB  1 
ATOM   1716 C  CG  . GLU A 1 215 ? 13.667  -31.423 10.426 1.00 114.56 ? 215 GLU A CG  1 
ATOM   1717 C  CD  . GLU A 1 215 ? 13.345  -31.415 8.932  1.00 129.30 ? 215 GLU A CD  1 
ATOM   1718 O  OE1 . GLU A 1 215 ? 13.846  -32.300 8.214  1.00 139.82 ? 215 GLU A OE1 1 
ATOM   1719 O  OE2 . GLU A 1 215 ? 12.587  -30.526 8.477  1.00 117.29 ? 215 GLU A OE2 1 
ATOM   1720 N  N   . ARG A 1 216 ? 16.382  -34.612 12.067 1.00 104.33 ? 216 ARG A N   1 
ATOM   1721 C  CA  . ARG A 1 216 ? 16.943  -35.957 12.373 1.00 107.88 ? 216 ARG A CA  1 
ATOM   1722 C  C   . ARG A 1 216 ? 17.233  -36.079 13.872 1.00 109.94 ? 216 ARG A C   1 
ATOM   1723 O  O   . ARG A 1 216 ? 17.246  -37.218 14.374 1.00 160.77 ? 216 ARG A O   1 
ATOM   1724 C  CB  . ARG A 1 216 ? 18.236  -36.202 11.591 1.00 116.36 ? 216 ARG A CB  1 
ATOM   1725 C  CG  . ARG A 1 216 ? 18.268  -35.570 10.209 1.00 128.71 ? 216 ARG A CG  1 
ATOM   1726 C  CD  . ARG A 1 216 ? 19.697  -35.362 9.750  1.00 124.36 ? 216 ARG A CD  1 
ATOM   1727 N  NE  . ARG A 1 216 ? 19.806  -34.448 8.623  1.00 124.68 ? 216 ARG A NE  1 
ATOM   1728 C  CZ  . ARG A 1 216 ? 19.539  -34.770 7.364  1.00 123.70 ? 216 ARG A CZ  1 
ATOM   1729 N  NH1 . ARG A 1 216 ? 19.142  -35.995 7.062  1.00 130.16 ? 216 ARG A NH1 1 
ATOM   1730 N  NH2 . ARG A 1 216 ? 19.675  -33.869 6.408  1.00 130.88 ? 216 ARG A NH2 1 
ATOM   1731 N  N   . LYS A 1 217 ? 17.467  -34.956 14.556 1.00 97.06  ? 217 LYS A N   1 
ATOM   1732 C  CA  . LYS A 1 217 ? 17.842  -34.997 15.994 1.00 104.71 ? 217 LYS A CA  1 
ATOM   1733 C  C   . LYS A 1 217 ? 16.635  -34.732 16.900 1.00 109.32 ? 217 LYS A C   1 
ATOM   1734 O  O   . LYS A 1 217 ? 16.789  -34.919 18.115 1.00 94.12  ? 217 LYS A O   1 
ATOM   1735 C  CB  . LYS A 1 217 ? 18.924  -33.955 16.265 1.00 106.63 ? 217 LYS A CB  1 
ATOM   1736 C  CG  . LYS A 1 217 ? 20.336  -34.414 15.917 1.00 122.79 ? 217 LYS A CG  1 
ATOM   1737 C  CD  . LYS A 1 217 ? 21.443  -33.711 16.704 1.00 113.63 ? 217 LYS A CD  1 
ATOM   1738 C  CE  . LYS A 1 217 ? 20.975  -32.868 17.884 1.00 89.79  ? 217 LYS A CE  1 
ATOM   1739 N  NZ  . LYS A 1 217 ? 22.120  -32.172 18.522 1.00 79.66  ? 217 LYS A NZ  1 
ATOM   1740 N  N   . ALA A 1 218 ? 15.501  -34.299 16.335 1.00 120.07 ? 218 ALA A N   1 
ATOM   1741 C  CA  . ALA A 1 218 ? 14.316  -33.805 17.076 1.00 126.60 ? 218 ALA A CA  1 
ATOM   1742 C  C   . ALA A 1 218 ? 13.373  -34.963 17.410 1.00 130.92 ? 218 ALA A C   1 
ATOM   1743 O  O   . ALA A 1 218 ? 12.422  -34.742 18.195 1.00 145.90 ? 218 ALA A O   1 
ATOM   1744 C  CB  . ALA A 1 218 ? 13.608  -32.737 16.269 1.00 131.54 ? 218 ALA A CB  1 
ATOM   1745 N  N   . ARG A 1 219 ? 13.691  -36.149 16.885 1.00 128.36 ? 219 ARG A N   1 
ATOM   1746 C  CA  . ARG A 1 219 ? 12.875  -37.356 17.164 1.00 126.04 ? 219 ARG A CA  1 
ATOM   1747 C  C   . ARG A 1 219 ? 12.819  -37.592 18.673 1.00 125.46 ? 219 ARG A C   1 
ATOM   1748 O  O   . ARG A 1 219 ? 13.890  -37.590 19.311 1.00 92.09  ? 219 ARG A O   1 
ATOM   1749 C  CB  . ARG A 1 219 ? 13.461  -38.571 16.440 1.00 128.02 ? 219 ARG A CB  1 
ATOM   1750 C  CG  . ARG A 1 219 ? 14.870  -38.349 15.913 1.00 130.82 ? 219 ARG A CG  1 
ATOM   1751 C  CD  . ARG A 1 219 ? 15.897  -39.075 16.758 1.00 150.58 ? 219 ARG A CD  1 
ATOM   1752 N  NE  . ARG A 1 219 ? 16.448  -38.239 17.814 1.00 159.26 ? 219 ARG A NE  1 
ATOM   1753 C  CZ  . ARG A 1 219 ? 17.706  -37.819 17.853 1.00 157.19 ? 219 ARG A CZ  1 
ATOM   1754 N  NH1 . ARG A 1 219 ? 18.544  -38.149 16.886 1.00 159.64 ? 219 ARG A NH1 1 
ATOM   1755 N  NH2 . ARG A 1 219 ? 18.121  -37.066 18.855 1.00 152.85 ? 219 ARG A NH2 1 
ATOM   1756 N  N   . GLY A 1 220 ? 11.615  -37.777 19.209 1.00 122.71 ? 220 GLY A N   1 
ATOM   1757 C  CA  . GLY A 1 220 ? 11.406  -38.043 20.655 1.00 108.16 ? 220 GLY A CA  1 
ATOM   1758 C  C   . GLY A 1 220 ? 12.352  -37.232 21.534 1.00 118.86 ? 220 GLY A C   1 
ATOM   1759 O  O   . GLY A 1 220 ? 12.990  -37.808 22.430 1.00 103.01 ? 220 GLY A O   1 
ATOM   1760 N  N   . ARG A 1 221 ? 12.432  -35.921 21.270 1.00 125.89 ? 221 ARG A N   1 
ATOM   1761 C  CA  . ARG A 1 221 ? 13.273  -35.012 22.093 1.00 124.51 ? 221 ARG A CA  1 
ATOM   1762 C  C   . ARG A 1 221 ? 12.415  -34.467 23.236 1.00 118.23 ? 221 ARG A C   1 
ATOM   1763 O  O   . ARG A 1 221 ? 12.988  -34.186 24.307 1.00 101.62 ? 221 ARG A O   1 
ATOM   1764 C  CB  . ARG A 1 221 ? 13.805  -33.862 21.233 1.00 128.71 ? 221 ARG A CB  1 
ATOM   1765 C  CG  . ARG A 1 221 ? 15.216  -34.077 20.708 1.00 117.07 ? 221 ARG A CG  1 
ATOM   1766 C  CD  . ARG A 1 221 ? 16.189  -33.031 21.218 1.00 102.29 ? 221 ARG A CD  1 
ATOM   1767 N  NE  . ARG A 1 221 ? 15.654  -32.292 22.352 1.00 127.57 ? 221 ARG A NE  1 
ATOM   1768 C  CZ  . ARG A 1 221 ? 16.387  -31.777 23.332 1.00 125.02 ? 221 ARG A CZ  1 
ATOM   1769 N  NH1 . ARG A 1 221 ? 17.701  -31.922 23.324 1.00 98.06  ? 221 ARG A NH1 1 
ATOM   1770 N  NH2 . ARG A 1 221 ? 15.803  -31.120 24.318 1.00 134.36 ? 221 ARG A NH2 1 
ATOM   1771 N  N   . LYS A 1 222 ? 11.111  -34.302 23.007 1.00 105.21 ? 222 LYS A N   1 
ATOM   1772 C  CA  . LYS A 1 222 ? 10.179  -33.853 24.078 1.00 120.16 ? 222 LYS A CA  1 
ATOM   1773 C  C   . LYS A 1 222 ? 10.416  -32.385 24.429 1.00 128.29 ? 222 LYS A C   1 
ATOM   1774 O  O   . LYS A 1 222 ? 9.497   -31.579 24.207 1.00 117.61 ? 222 LYS A O   1 
ATOM   1775 C  CB  . LYS A 1 222 ? 10.347  -34.713 25.333 1.00 129.96 ? 222 LYS A CB  1 
ATOM   1776 C  CG  . LYS A 1 222 ? 9.512   -34.286 26.531 1.00 130.68 ? 222 LYS A CG  1 
ATOM   1777 C  CD  . LYS A 1 222 ? 10.352  -33.840 27.706 1.00 141.55 ? 222 LYS A CD  1 
ATOM   1778 C  CE  . LYS A 1 222 ? 9.946   -32.482 28.237 1.00 135.64 ? 222 LYS A CE  1 
ATOM   1779 N  NZ  . LYS A 1 222 ? 9.189   -31.701 27.230 1.00 146.17 ? 222 LYS A NZ  1 
ATOM   1780 N  N   . LEU A 1 223 ? 11.586  -32.057 24.977 1.00 116.58 ? 223 LEU A N   1 
ATOM   1781 C  CA  . LEU A 1 223 ? 11.848  -30.667 25.431 1.00 118.73 ? 223 LEU A CA  1 
ATOM   1782 C  C   . LEU A 1 223 ? 12.214  -29.785 24.235 1.00 121.55 ? 223 LEU A C   1 
ATOM   1783 O  O   . LEU A 1 223 ? 11.362  -29.607 23.359 1.00 156.88 ? 223 LEU A O   1 
ATOM   1784 C  CB  . LEU A 1 223 ? 12.984  -30.702 26.453 1.00 116.37 ? 223 LEU A CB  1 
ATOM   1785 C  CG  . LEU A 1 223 ? 12.771  -29.836 27.693 1.00 121.34 ? 223 LEU A CG  1 
ATOM   1786 C  CD1 . LEU A 1 223 ? 13.825  -28.743 27.774 1.00 122.35 ? 223 LEU A CD1 1 
ATOM   1787 C  CD2 . LEU A 1 223 ? 11.375  -29.235 27.699 1.00 93.08  ? 223 LEU A CD2 1 
ATOM   1788 N  N   . GLN A 1 224 ? 13.422  -29.222 24.227 1.00 102.74 ? 224 GLN A N   1 
ATOM   1789 C  CA  . GLN A 1 224 ? 13.888  -28.379 23.079 1.00 93.46  ? 224 GLN A CA  1 
ATOM   1790 C  C   . GLN A 1 224 ? 13.764  -29.165 21.756 1.00 93.32  ? 224 GLN A C   1 
ATOM   1791 O  O   . GLN A 1 224 ? 14.464  -30.162 21.589 1.00 91.76  ? 224 GLN A O   1 
ATOM   1792 C  CB  . GLN A 1 224 ? 15.341  -27.959 23.264 1.00 102.90 ? 224 GLN A CB  1 
ATOM   1793 C  CG  . GLN A 1 224 ? 15.603  -27.102 24.498 1.00 95.34  ? 224 GLN A CG  1 
ATOM   1794 C  CD  . GLN A 1 224 ? 17.065  -27.138 24.886 1.00 101.14 ? 224 GLN A CD  1 
ATOM   1795 O  OE1 . GLN A 1 224 ? 17.766  -28.165 24.806 1.00 128.08 ? 224 GLN A OE1 1 
ATOM   1796 N  NE2 . GLN A 1 224 ? 17.542  -25.991 25.319 1.00 97.55  ? 224 GLN A NE2 1 
ATOM   1797 N  N   . LYS A 1 225 ? 12.867  -28.764 20.858 1.00 95.56  ? 225 LYS A N   1 
ATOM   1798 C  CA  . LYS A 1 225 ? 12.304  -29.646 19.796 1.00 93.84  ? 225 LYS A CA  1 
ATOM   1799 C  C   . LYS A 1 225 ? 12.344  -28.969 18.430 1.00 93.49  ? 225 LYS A C   1 
ATOM   1800 O  O   . LYS A 1 225 ? 12.017  -29.652 17.458 1.00 105.97 ? 225 LYS A O   1 
ATOM   1801 C  CB  . LYS A 1 225 ? 10.827  -29.997 20.064 1.00 109.16 ? 225 LYS A CB  1 
ATOM   1802 C  CG  . LYS A 1 225 ? 10.572  -31.166 21.020 1.00 132.04 ? 225 LYS A CG  1 
ATOM   1803 C  CD  . LYS A 1 225 ? 9.207   -31.872 20.868 1.00 131.81 ? 225 LYS A CD  1 
ATOM   1804 C  CE  . LYS A 1 225 ? 9.200   -32.995 19.835 1.00 140.83 ? 225 LYS A CE  1 
ATOM   1805 N  NZ  . LYS A 1 225 ? 10.079  -34.154 20.181 1.00 138.60 ? 225 LYS A NZ  1 
ATOM   1806 N  N   . ASN A 1 226 ? 12.624  -27.669 18.347 1.00 102.13 ? 226 ASN A N   1 
ATOM   1807 C  CA  . ASN A 1 226 ? 12.309  -26.888 17.118 1.00 96.35  ? 226 ASN A CA  1 
ATOM   1808 C  C   . ASN A 1 226 ? 13.548  -26.834 16.231 1.00 95.14  ? 226 ASN A C   1 
ATOM   1809 O  O   . ASN A 1 226 ? 14.536  -26.195 16.585 1.00 89.50  ? 226 ASN A O   1 
ATOM   1810 C  CB  . ASN A 1 226 ? 11.767  -25.478 17.376 1.00 84.80  ? 226 ASN A CB  1 
ATOM   1811 C  CG  . ASN A 1 226 ? 11.366  -24.822 16.068 1.00 89.35  ? 226 ASN A CG  1 
ATOM   1812 O  OD1 . ASN A 1 226 ? 12.192  -24.415 15.254 1.00 95.57  ? 226 ASN A OD1 1 
ATOM   1813 N  ND2 . ASN A 1 226 ? 10.081  -24.770 15.806 1.00 97.13  ? 226 ASN A ND2 1 
ATOM   1814 N  N   . PRO A 1 227 ? 13.513  -27.432 15.020 1.00 90.30  ? 227 PRO A N   1 
ATOM   1815 C  CA  . PRO A 1 227 ? 14.717  -27.565 14.212 1.00 89.94  ? 227 PRO A CA  1 
ATOM   1816 C  C   . PRO A 1 227 ? 15.137  -26.203 13.637 1.00 91.81  ? 227 PRO A C   1 
ATOM   1817 O  O   . PRO A 1 227 ? 16.316  -25.799 13.761 1.00 80.43  ? 227 PRO A O   1 
ATOM   1818 C  CB  . PRO A 1 227 ? 14.287  -28.527 13.098 1.00 93.15  ? 227 PRO A CB  1 
ATOM   1819 C  CG  . PRO A 1 227 ? 12.926  -29.041 13.503 1.00 91.58  ? 227 PRO A CG  1 
ATOM   1820 C  CD  . PRO A 1 227 ? 12.324  -27.926 14.316 1.00 88.26  ? 227 PRO A CD  1 
ATOM   1821 N  N   . THR A 1 228 ? 14.176  -25.505 13.029 1.00 79.14  ? 228 THR A N   1 
ATOM   1822 C  CA  . THR A 1 228 ? 14.437  -24.157 12.490 1.00 83.32  ? 228 THR A CA  1 
ATOM   1823 C  C   . THR A 1 228 ? 15.212  -23.336 13.534 1.00 82.49  ? 228 THR A C   1 
ATOM   1824 O  O   . THR A 1 228 ? 16.266  -22.778 13.148 1.00 83.88  ? 228 THR A O   1 
ATOM   1825 C  CB  . THR A 1 228 ? 13.154  -23.475 12.022 1.00 83.15  ? 228 THR A CB  1 
ATOM   1826 O  OG1 . THR A 1 228 ? 12.558  -24.282 11.011 1.00 79.43  ? 228 THR A OG1 1 
ATOM   1827 C  CG2 . THR A 1 228 ? 13.423  -22.102 11.447 1.00 87.36  ? 228 THR A CG2 1 
ATOM   1828 N  N   . TYR A 1 229 ? 14.731  -23.263 14.783 1.00 68.39  ? 229 TYR A N   1 
ATOM   1829 C  CA  . TYR A 1 229 ? 15.376  -22.483 15.877 1.00 70.78  ? 229 TYR A CA  1 
ATOM   1830 C  C   . TYR A 1 229 ? 16.808  -22.965 16.082 1.00 68.91  ? 229 TYR A C   1 
ATOM   1831 O  O   . TYR A 1 229 ? 17.729  -22.150 16.036 1.00 73.06  ? 229 TYR A O   1 
ATOM   1832 C  CB  . TYR A 1 229 ? 14.624  -22.615 17.194 1.00 73.06  ? 229 TYR A CB  1 
ATOM   1833 C  CG  . TYR A 1 229 ? 14.983  -21.655 18.303 1.00 69.23  ? 229 TYR A CG  1 
ATOM   1834 C  CD1 . TYR A 1 229 ? 14.500  -20.364 18.319 1.00 73.89  ? 229 TYR A CD1 1 
ATOM   1835 C  CD2 . TYR A 1 229 ? 15.681  -22.071 19.420 1.00 80.42  ? 229 TYR A CD2 1 
ATOM   1836 C  CE1 . TYR A 1 229 ? 14.752  -19.495 19.374 1.00 80.76  ? 229 TYR A CE1 1 
ATOM   1837 C  CE2 . TYR A 1 229 ? 15.933  -21.227 20.492 1.00 83.42  ? 229 TYR A CE2 1 
ATOM   1838 C  CZ  . TYR A 1 229 ? 15.471  -19.923 20.473 1.00 83.24  ? 229 TYR A CZ  1 
ATOM   1839 O  OH  . TYR A 1 229 ? 15.701  -19.076 21.529 1.00 84.90  ? 229 TYR A OH  1 
ATOM   1840 N  N   . ALA A 1 230 ? 17.000  -24.265 16.250 1.00 76.24  ? 230 ALA A N   1 
ATOM   1841 C  CA  . ALA A 1 230 ? 18.339  -24.856 16.487 1.00 91.44  ? 230 ALA A CA  1 
ATOM   1842 C  C   . ALA A 1 230 ? 19.305  -24.420 15.382 1.00 81.13  ? 230 ALA A C   1 
ATOM   1843 O  O   . ALA A 1 230 ? 20.532  -24.148 15.713 1.00 76.91  ? 230 ALA A O   1 
ATOM   1844 C  CB  . ALA A 1 230 ? 18.254  -26.355 16.557 1.00 105.18 ? 230 ALA A CB  1 
ATOM   1845 N  N   . ALA A 1 231 ? 18.775  -24.356 14.151 1.00 66.85  ? 231 ALA A N   1 
ATOM   1846 C  CA  . ALA A 1 231 ? 19.539  -23.962 12.943 1.00 83.88  ? 231 ALA A CA  1 
ATOM   1847 C  C   . ALA A 1 231 ? 19.888  -22.478 13.033 1.00 85.75  ? 231 ALA A C   1 
ATOM   1848 O  O   . ALA A 1 231 ? 21.039  -22.086 12.734 1.00 84.12  ? 231 ALA A O   1 
ATOM   1849 C  CB  . ALA A 1 231 ? 18.763  -24.263 11.685 1.00 89.12  ? 231 ALA A CB  1 
ATOM   1850 N  N   . MET A 1 232 ? 18.917  -21.672 13.445 1.00 86.57  ? 232 MET A N   1 
ATOM   1851 C  CA  . MET A 1 232 ? 19.146  -20.226 13.663 1.00 78.69  ? 232 MET A CA  1 
ATOM   1852 C  C   . MET A 1 232 ? 20.335  -20.096 14.620 1.00 71.84  ? 232 MET A C   1 
ATOM   1853 O  O   . MET A 1 232 ? 21.258  -19.315 14.333 1.00 75.74  ? 232 MET A O   1 
ATOM   1854 C  CB  . MET A 1 232 ? 17.885  -19.547 14.205 1.00 71.30  ? 232 MET A CB  1 
ATOM   1855 C  CG  . MET A 1 232 ? 16.757  -19.545 13.181 1.00 74.77  ? 232 MET A CG  1 
ATOM   1856 S  SD  . MET A 1 232 ? 15.217  -18.837 13.800 1.00 89.45  ? 232 MET A SD  1 
ATOM   1857 C  CE  . MET A 1 232 ? 15.608  -17.094 13.821 1.00 100.77 ? 232 MET A CE  1 
ATOM   1858 N  N   . ILE A 1 233 ? 20.362  -20.918 15.659 1.00 62.44  ? 233 ILE A N   1 
ATOM   1859 C  CA  . ILE A 1 233 ? 21.410  -20.836 16.705 1.00 71.50  ? 233 ILE A CA  1 
ATOM   1860 C  C   . ILE A 1 233 ? 22.734  -21.273 16.100 1.00 75.01  ? 233 ILE A C   1 
ATOM   1861 O  O   . ILE A 1 233 ? 23.739  -20.583 16.378 1.00 77.84  ? 233 ILE A O   1 
ATOM   1862 C  CB  . ILE A 1 233 ? 21.038  -21.638 17.964 1.00 77.98  ? 233 ILE A CB  1 
ATOM   1863 C  CG1 . ILE A 1 233 ? 19.671  -21.177 18.488 1.00 81.62  ? 233 ILE A CG1 1 
ATOM   1864 C  CG2 . ILE A 1 233 ? 22.137  -21.517 19.016 1.00 71.23  ? 233 ILE A CG2 1 
ATOM   1865 C  CD1 . ILE A 1 233 ? 19.320  -21.625 19.886 1.00 79.86  ? 233 ILE A CD1 1 
ATOM   1866 N  N   . GLU A 1 234 ? 22.751  -22.345 15.309 1.00 77.18  ? 234 GLU A N   1 
ATOM   1867 C  CA  . GLU A 1 234 ? 24.020  -22.741 14.646 1.00 89.55  ? 234 GLU A CA  1 
ATOM   1868 C  C   . GLU A 1 234 ? 24.510  -21.581 13.764 1.00 82.69  ? 234 GLU A C   1 
ATOM   1869 O  O   . GLU A 1 234 ? 25.710  -21.217 13.889 1.00 81.20  ? 234 GLU A O   1 
ATOM   1870 C  CB  . GLU A 1 234 ? 23.877  -24.035 13.854 1.00 101.82 ? 234 GLU A CB  1 
ATOM   1871 C  CG  . GLU A 1 234 ? 25.204  -24.587 13.359 1.00 98.98  ? 234 GLU A CG  1 
ATOM   1872 C  CD  . GLU A 1 234 ? 25.073  -25.933 12.665 1.00 102.12 ? 234 GLU A CD  1 
ATOM   1873 O  OE1 . GLU A 1 234 ? 24.357  -26.803 13.187 1.00 109.95 ? 234 GLU A OE1 1 
ATOM   1874 O  OE2 . GLU A 1 234 ? 25.667  -26.107 11.594 1.00 103.56 ? 234 GLU A OE2 1 
ATOM   1875 N  N   . SER A 1 235 ? 23.644  -20.991 12.929 1.00 75.88  ? 235 SER A N   1 
ATOM   1876 C  CA  . SER A 1 235 ? 24.076  -19.936 11.963 1.00 84.09  ? 235 SER A CA  1 
ATOM   1877 C  C   . SER A 1 235 ? 24.569  -18.709 12.748 1.00 83.81  ? 235 SER A C   1 
ATOM   1878 O  O   . SER A 1 235 ? 25.582  -18.047 12.331 1.00 77.21  ? 235 SER A O   1 
ATOM   1879 C  CB  . SER A 1 235 ? 23.030  -19.600 10.902 1.00 76.22  ? 235 SER A CB  1 
ATOM   1880 O  OG  . SER A 1 235 ? 23.525  -19.949 9.596  1.00 71.96  ? 235 SER A OG  1 
ATOM   1881 N  N   . MET A 1 236 ? 23.924  -18.451 13.884 1.00 74.64  ? 236 MET A N   1 
ATOM   1882 C  CA  . MET A 1 236 ? 24.323  -17.362 14.803 1.00 69.32  ? 236 MET A CA  1 
ATOM   1883 C  C   . MET A 1 236 ? 25.697  -17.698 15.378 1.00 70.24  ? 236 MET A C   1 
ATOM   1884 O  O   . MET A 1 236 ? 26.595  -16.853 15.304 1.00 78.35  ? 236 MET A O   1 
ATOM   1885 C  CB  . MET A 1 236 ? 23.303  -17.204 15.931 1.00 68.24  ? 236 MET A CB  1 
ATOM   1886 C  CG  . MET A 1 236 ? 23.675  -16.138 16.928 1.00 67.23  ? 236 MET A CG  1 
ATOM   1887 S  SD  . MET A 1 236 ? 24.685  -16.756 18.288 1.00 75.52  ? 236 MET A SD  1 
ATOM   1888 C  CE  . MET A 1 236 ? 23.496  -17.757 19.174 1.00 78.57  ? 236 MET A CE  1 
ATOM   1889 N  N   . ASP A 1 237 ? 25.850  -18.898 15.926 1.00 74.82  ? 237 ASP A N   1 
ATOM   1890 C  CA  . ASP A 1 237 ? 27.125  -19.346 16.535 1.00 79.43  ? 237 ASP A CA  1 
ATOM   1891 C  C   . ASP A 1 237 ? 28.261  -19.261 15.498 1.00 84.86  ? 237 ASP A C   1 
ATOM   1892 O  O   . ASP A 1 237 ? 29.379  -18.882 15.913 1.00 77.10  ? 237 ASP A O   1 
ATOM   1893 C  CB  . ASP A 1 237 ? 26.977  -20.740 17.138 1.00 84.53  ? 237 ASP A CB  1 
ATOM   1894 C  CG  . ASP A 1 237 ? 28.274  -21.242 17.746 1.00 92.71  ? 237 ASP A CG  1 
ATOM   1895 O  OD1 . ASP A 1 237 ? 29.080  -21.861 17.001 1.00 90.27  ? 237 ASP A OD1 1 
ATOM   1896 O  OD2 . ASP A 1 237 ? 28.476  -20.992 18.958 1.00 89.25  ? 237 ASP A OD2 1 
ATOM   1897 N  N   . GLN A 1 238 ? 28.013  -19.572 14.212 1.00 82.77  ? 238 GLN A N   1 
ATOM   1898 C  CA  . GLN A 1 238 ? 29.049  -19.435 13.147 1.00 85.98  ? 238 GLN A CA  1 
ATOM   1899 C  C   . GLN A 1 238 ? 29.493  -17.971 13.093 1.00 84.36  ? 238 GLN A C   1 
ATOM   1900 O  O   . GLN A 1 238 ? 30.710  -17.701 13.219 1.00 78.21  ? 238 GLN A O   1 
ATOM   1901 C  CB  . GLN A 1 238 ? 28.549  -19.869 11.772 1.00 95.23  ? 238 GLN A CB  1 
ATOM   1902 C  CG  . GLN A 1 238 ? 28.526  -21.376 11.569 1.00 97.50  ? 238 GLN A CG  1 
ATOM   1903 C  CD  . GLN A 1 238 ? 27.623  -21.813 10.435 1.00 106.84 ? 238 GLN A CD  1 
ATOM   1904 O  OE1 . GLN A 1 238 ? 27.150  -21.027 9.606  1.00 97.66  ? 238 GLN A OE1 1 
ATOM   1905 N  NE2 . GLN A 1 238 ? 27.344  -23.104 10.401 1.00 120.75 ? 238 GLN A NE2 1 
ATOM   1906 N  N   . GLY A 1 239 ? 28.527  -17.058 12.971 1.00 78.81  ? 239 GLY A N   1 
ATOM   1907 C  CA  . GLY A 1 239 ? 28.784  -15.605 12.994 1.00 87.67  ? 239 GLY A CA  1 
ATOM   1908 C  C   . GLY A 1 239 ? 29.657  -15.173 14.170 1.00 77.71  ? 239 GLY A C   1 
ATOM   1909 O  O   . GLY A 1 239 ? 30.431  -14.217 14.036 1.00 88.87  ? 239 GLY A O   1 
ATOM   1910 N  N   . VAL A 1 240 ? 29.530  -15.821 15.314 1.00 69.07  ? 240 VAL A N   1 
ATOM   1911 C  CA  . VAL A 1 240 ? 30.291  -15.430 16.527 1.00 72.89  ? 240 VAL A CA  1 
ATOM   1912 C  C   . VAL A 1 240 ? 31.737  -15.913 16.372 1.00 74.96  ? 240 VAL A C   1 
ATOM   1913 O  O   . VAL A 1 240 ? 32.645  -15.175 16.782 1.00 72.79  ? 240 VAL A O   1 
ATOM   1914 C  CB  . VAL A 1 240 ? 29.600  -15.969 17.794 1.00 73.55  ? 240 VAL A CB  1 
ATOM   1915 C  CG1 . VAL A 1 240 ? 30.479  -15.906 19.039 1.00 75.50  ? 240 VAL A CG1 1 
ATOM   1916 C  CG2 . VAL A 1 240 ? 28.311  -15.221 18.038 1.00 76.39  ? 240 VAL A CG2 1 
ATOM   1917 N  N   . GLY A 1 241 ? 31.949  -17.109 15.819 1.00 77.93  ? 241 GLY A N   1 
ATOM   1918 C  CA  . GLY A 1 241 ? 33.305  -17.637 15.582 1.00 83.39  ? 241 GLY A CA  1 
ATOM   1919 C  C   . GLY A 1 241 ? 34.035  -16.762 14.587 1.00 83.06  ? 241 GLY A C   1 
ATOM   1920 O  O   . GLY A 1 241 ? 35.249  -16.479 14.774 1.00 81.19  ? 241 GLY A O   1 
ATOM   1921 N  N   . ARG A 1 242 ? 33.298  -16.304 13.579 1.00 77.53  ? 242 ARG A N   1 
ATOM   1922 C  CA  . ARG A 1 242 ? 33.879  -15.486 12.490 1.00 76.98  ? 242 ARG A CA  1 
ATOM   1923 C  C   . ARG A 1 242 ? 34.448  -14.204 13.086 1.00 73.00  ? 242 ARG A C   1 
ATOM   1924 O  O   . ARG A 1 242 ? 35.553  -13.803 12.667 1.00 80.15  ? 242 ARG A O   1 
ATOM   1925 C  CB  . ARG A 1 242 ? 32.837  -15.184 11.420 1.00 77.56  ? 242 ARG A CB  1 
ATOM   1926 C  CG  . ARG A 1 242 ? 32.424  -16.409 10.620 1.00 79.39  ? 242 ARG A CG  1 
ATOM   1927 C  CD  . ARG A 1 242 ? 31.484  -16.047 9.498  1.00 76.91  ? 242 ARG A CD  1 
ATOM   1928 N  NE  . ARG A 1 242 ? 32.166  -15.171 8.558  1.00 70.13  ? 242 ARG A NE  1 
ATOM   1929 C  CZ  . ARG A 1 242 ? 31.522  -14.395 7.699  1.00 74.16  ? 242 ARG A CZ  1 
ATOM   1930 N  NH1 . ARG A 1 242 ? 30.199  -14.396 7.674  1.00 78.27  ? 242 ARG A NH1 1 
ATOM   1931 N  NH2 . ARG A 1 242 ? 32.195  -13.630 6.864  1.00 80.60  ? 242 ARG A NH2 1 
ATOM   1932 N  N   . VAL A 1 243 ? 33.714  -13.604 14.019 1.00 66.43  ? 243 VAL A N   1 
ATOM   1933 C  CA  . VAL A 1 243 ? 34.170  -12.393 14.754 1.00 67.34  ? 243 VAL A CA  1 
ATOM   1934 C  C   . VAL A 1 243 ? 35.400  -12.792 15.563 1.00 70.74  ? 243 VAL A C   1 
ATOM   1935 O  O   . VAL A 1 243 ? 36.417  -12.069 15.523 1.00 68.74  ? 243 VAL A O   1 
ATOM   1936 C  CB  . VAL A 1 243 ? 33.088  -11.798 15.678 1.00 67.31  ? 243 VAL A CB  1 
ATOM   1937 C  CG1 . VAL A 1 243 ? 33.685  -10.806 16.670 1.00 66.54  ? 243 VAL A CG1 1 
ATOM   1938 C  CG2 . VAL A 1 243 ? 31.963  -11.142 14.896 1.00 68.75  ? 243 VAL A CG2 1 
ATOM   1939 N  N   . MET A 1 244 ? 35.284  -13.876 16.320 1.00 76.89  ? 244 MET A N   1 
ATOM   1940 C  CA  . MET A 1 244 ? 36.334  -14.254 17.287 1.00 78.74  ? 244 MET A CA  1 
ATOM   1941 C  C   . MET A 1 244 ? 37.620  -14.464 16.486 1.00 75.32  ? 244 MET A C   1 
ATOM   1942 O  O   . MET A 1 244 ? 38.702  -14.002 16.927 1.00 63.58  ? 244 MET A O   1 
ATOM   1943 C  CB  . MET A 1 244 ? 35.942  -15.521 18.044 1.00 88.87  ? 244 MET A CB  1 
ATOM   1944 C  CG  . MET A 1 244 ? 35.091  -15.282 19.278 1.00 90.38  ? 244 MET A CG  1 
ATOM   1945 S  SD  . MET A 1 244 ? 34.394  -16.849 19.888 1.00 101.97 ? 244 MET A SD  1 
ATOM   1946 C  CE  . MET A 1 244 ? 35.843  -17.901 19.880 1.00 109.78 ? 244 MET A CE  1 
ATOM   1947 N  N   . SER A 1 245 ? 37.500  -15.104 15.324 1.00 77.85  ? 245 SER A N   1 
ATOM   1948 C  CA  . SER A 1 245 ? 38.676  -15.551 14.539 1.00 88.89  ? 245 SER A CA  1 
ATOM   1949 C  C   . SER A 1 245 ? 39.202  -14.373 13.707 1.00 80.37  ? 245 SER A C   1 
ATOM   1950 O  O   . SER A 1 245 ? 40.417  -14.290 13.508 1.00 82.50  ? 245 SER A O   1 
ATOM   1951 C  CB  . SER A 1 245 ? 38.354  -16.759 13.710 1.00 89.16  ? 245 SER A CB  1 
ATOM   1952 O  OG  . SER A 1 245 ? 37.928  -16.343 12.432 1.00 96.21  ? 245 SER A OG  1 
ATOM   1953 N  N   . LYS A 1 246 ? 38.340  -13.476 13.241 1.00 71.74  ? 246 LYS A N   1 
ATOM   1954 C  CA  . LYS A 1 246 ? 38.824  -12.229 12.605 1.00 70.59  ? 246 LYS A CA  1 
ATOM   1955 C  C   . LYS A 1 246 ? 39.670  -11.441 13.608 1.00 66.99  ? 246 LYS A C   1 
ATOM   1956 O  O   . LYS A 1 246 ? 40.667  -10.825 13.203 1.00 71.59  ? 246 LYS A O   1 
ATOM   1957 C  CB  . LYS A 1 246 ? 37.699  -11.328 12.098 1.00 72.67  ? 246 LYS A CB  1 
ATOM   1958 C  CG  . LYS A 1 246 ? 38.181  -10.006 11.501 1.00 78.43  ? 246 LYS A CG  1 
ATOM   1959 C  CD  . LYS A 1 246 ? 38.274  -9.949  9.962  1.00 89.03  ? 246 LYS A CD  1 
ATOM   1960 C  CE  . LYS A 1 246 ? 39.299  -10.879 9.356  1.00 97.09  ? 246 LYS A CE  1 
ATOM   1961 N  NZ  . LYS A 1 246 ? 39.131  -10.992 7.895  1.00 110.82 ? 246 LYS A NZ  1 
ATOM   1962 N  N   . LEU A 1 247 ? 39.279  -11.391 14.871 1.00 71.11  ? 247 LEU A N   1 
ATOM   1963 C  CA  . LEU A 1 247 ? 40.087  -10.633 15.857 1.00 74.87  ? 247 LEU A CA  1 
ATOM   1964 C  C   . LEU A 1 247 ? 41.473  -11.285 15.947 1.00 79.57  ? 247 LEU A C   1 
ATOM   1965 O  O   . LEU A 1 247 ? 42.438  -10.576 16.290 1.00 73.45  ? 247 LEU A O   1 
ATOM   1966 C  CB  . LEU A 1 247 ? 39.382  -10.620 17.209 1.00 77.12  ? 247 LEU A CB  1 
ATOM   1967 C  CG  . LEU A 1 247 ? 38.066  -9.858  17.266 1.00 76.89  ? 247 LEU A CG  1 
ATOM   1968 C  CD1 . LEU A 1 247 ? 37.396  -10.076 18.617 1.00 86.93  ? 247 LEU A CD1 1 
ATOM   1969 C  CD2 . LEU A 1 247 ? 38.302  -8.378  17.021 1.00 79.61  ? 247 LEU A CD2 1 
ATOM   1970 N  N   . GLU A 1 248 ? 41.563  -12.588 15.657 1.00 85.39  ? 248 GLU A N   1 
ATOM   1971 C  CA  . GLU A 1 248 ? 42.855  -13.320 15.678 1.00 93.52  ? 248 GLU A CA  1 
ATOM   1972 C  C   . GLU A 1 248 ? 43.691  -12.895 14.461 1.00 83.76  ? 248 GLU A C   1 
ATOM   1973 O  O   . GLU A 1 248 ? 44.875  -12.523 14.672 1.00 71.00  ? 248 GLU A O   1 
ATOM   1974 C  CB  . GLU A 1 248 ? 42.642  -14.838 15.755 1.00 103.20 ? 248 GLU A CB  1 
ATOM   1975 C  CG  . GLU A 1 248 ? 43.895  -15.585 16.192 1.00 112.39 ? 248 GLU A CG  1 
ATOM   1976 C  CD  . GLU A 1 248 ? 44.616  -14.949 17.380 1.00 120.09 ? 248 GLU A CD  1 
ATOM   1977 O  OE1 . GLU A 1 248 ? 43.928  -14.638 18.389 1.00 100.71 ? 248 GLU A OE1 1 
ATOM   1978 O  OE2 . GLU A 1 248 ? 45.859  -14.741 17.299 1.00 115.59 ? 248 GLU A OE2 1 
ATOM   1979 N  N   . ASP A 1 249 ? 43.087  -12.932 13.261 1.00 81.61  ? 249 ASP A N   1 
ATOM   1980 C  CA  . ASP A 1 249 ? 43.725  -12.597 11.955 1.00 78.23  ? 249 ASP A CA  1 
ATOM   1981 C  C   . ASP A 1 249 ? 44.253  -11.169 12.007 1.00 75.02  ? 249 ASP A C   1 
ATOM   1982 O  O   . ASP A 1 249 ? 45.311  -10.935 11.472 1.00 77.26  ? 249 ASP A O   1 
ATOM   1983 C  CB  . ASP A 1 249 ? 42.778  -12.693 10.755 1.00 87.68  ? 249 ASP A CB  1 
ATOM   1984 C  CG  . ASP A 1 249 ? 42.112  -14.054 10.603 1.00 109.22 ? 249 ASP A CG  1 
ATOM   1985 O  OD1 . ASP A 1 249 ? 42.544  -14.991 11.318 1.00 135.24 ? 249 ASP A OD1 1 
ATOM   1986 O  OD2 . ASP A 1 249 ? 41.164  -14.174 9.776  1.00 101.06 ? 249 ASP A OD2 1 
ATOM   1987 N  N   . LEU A 1 250 ? 43.551  -10.258 12.672 1.00 76.78  ? 250 LEU A N   1 
ATOM   1988 C  CA  . LEU A 1 250 ? 43.977  -8.842  12.774 1.00 75.35  ? 250 LEU A CA  1 
ATOM   1989 C  C   . LEU A 1 250 ? 44.953  -8.647  13.943 1.00 69.04  ? 250 LEU A C   1 
ATOM   1990 O  O   . LEU A 1 250 ? 45.446  -7.541  14.090 1.00 70.15  ? 250 LEU A O   1 
ATOM   1991 C  CB  . LEU A 1 250 ? 42.731  -7.968  12.929 1.00 82.25  ? 250 LEU A CB  1 
ATOM   1992 C  CG  . LEU A 1 250 ? 41.731  -8.006  11.770 1.00 83.87  ? 250 LEU A CG  1 
ATOM   1993 C  CD1 . LEU A 1 250 ? 40.564  -7.066  12.024 1.00 85.86  ? 250 LEU A CD1 1 
ATOM   1994 C  CD2 . LEU A 1 250 ? 42.405  -7.633  10.470 1.00 91.23  ? 250 LEU A CD2 1 
ATOM   1995 N  N   . LYS A 1 251 ? 45.239  -9.660  14.751 1.00 70.03  ? 251 LYS A N   1 
ATOM   1996 C  CA  . LYS A 1 251 ? 46.257  -9.534  15.825 1.00 81.46  ? 251 LYS A CA  1 
ATOM   1997 C  C   . LYS A 1 251 ? 45.836  -8.439  16.822 1.00 78.42  ? 251 LYS A C   1 
ATOM   1998 O  O   . LYS A 1 251 ? 46.708  -7.655  17.285 1.00 70.79  ? 251 LYS A O   1 
ATOM   1999 C  CB  . LYS A 1 251 ? 47.626  -9.316  15.157 1.00 94.87  ? 251 LYS A CB  1 
ATOM   2000 C  CG  . LYS A 1 251 ? 48.246  -10.579 14.568 1.00 99.52  ? 251 LYS A CG  1 
ATOM   2001 C  CD  . LYS A 1 251 ? 48.695  -11.557 15.672 1.00 121.88 ? 251 LYS A CD  1 
ATOM   2002 C  CE  . LYS A 1 251 ? 48.086  -12.952 15.644 1.00 122.42 ? 251 LYS A CE  1 
ATOM   2003 N  NZ  . LYS A 1 251 ? 48.565  -13.709 14.468 1.00 143.39 ? 251 LYS A NZ  1 
ATOM   2004 N  N   . ILE A 1 252 ? 44.541  -8.397  17.159 1.00 84.67  ? 252 ILE A N   1 
ATOM   2005 C  CA  . ILE A 1 252 ? 43.973  -7.469  18.188 1.00 83.47  ? 252 ILE A CA  1 
ATOM   2006 C  C   . ILE A 1 252 ? 43.100  -8.208  19.209 1.00 80.64  ? 252 ILE A C   1 
ATOM   2007 O  O   . ILE A 1 252 ? 42.579  -7.523  20.114 1.00 72.24  ? 252 ILE A O   1 
ATOM   2008 C  CB  . ILE A 1 252 ? 43.160  -6.347  17.532 1.00 70.92  ? 252 ILE A CB  1 
ATOM   2009 C  CG1 . ILE A 1 252 ? 41.932  -6.901  16.824 1.00 69.47  ? 252 ILE A CG1 1 
ATOM   2010 C  CG2 . ILE A 1 252 ? 44.027  -5.554  16.594 1.00 83.42  ? 252 ILE A CG2 1 
ATOM   2011 C  CD1 . ILE A 1 252 ? 41.078  -5.838  16.199 1.00 76.95  ? 252 ILE A CD1 1 
ATOM   2012 N  N   . ALA A 1 253 ? 42.916  -9.521  19.093 1.00 73.58  ? 253 ALA A N   1 
ATOM   2013 C  CA  . ALA A 1 253 ? 42.186  -10.297 20.115 1.00 77.83  ? 253 ALA A CA  1 
ATOM   2014 C  C   . ALA A 1 253 ? 42.786  -9.986  21.491 1.00 71.09  ? 253 ALA A C   1 
ATOM   2015 O  O   . ALA A 1 253 ? 42.020  -9.947  22.448 1.00 72.05  ? 253 ALA A O   1 
ATOM   2016 C  CB  . ALA A 1 253 ? 42.239  -11.770 19.809 1.00 91.03  ? 253 ALA A CB  1 
ATOM   2017 N  N   . ASP A 1 254 ? 44.102  -9.788  21.584 1.00 71.81  ? 254 ASP A N   1 
ATOM   2018 C  CA  . ASP A 1 254 ? 44.768  -9.600  22.904 1.00 81.32  ? 254 ASP A CA  1 
ATOM   2019 C  C   . ASP A 1 254 ? 44.199  -8.405  23.674 1.00 74.57  ? 254 ASP A C   1 
ATOM   2020 O  O   . ASP A 1 254 ? 44.203  -8.466  24.919 1.00 72.15  ? 254 ASP A O   1 
ATOM   2021 C  CB  . ASP A 1 254 ? 46.271  -9.396  22.716 1.00 91.52  ? 254 ASP A CB  1 
ATOM   2022 C  CG  . ASP A 1 254 ? 46.588  -8.164  21.886 1.00 99.63  ? 254 ASP A CG  1 
ATOM   2023 O  OD1 . ASP A 1 254 ? 46.138  -8.110  20.723 1.00 102.53 ? 254 ASP A OD1 1 
ATOM   2024 O  OD2 . ASP A 1 254 ? 47.271  -7.264  22.412 1.00 90.97  ? 254 ASP A OD2 1 
ATOM   2025 N  N   . HIS A 1 255 ? 43.730  -7.367  22.981 1.00 78.94  ? 255 HIS A N   1 
ATOM   2026 C  CA  . HIS A 1 255 ? 43.285  -6.112  23.655 1.00 79.73  ? 255 HIS A CA  1 
ATOM   2027 C  C   . HIS A 1 255 ? 41.858  -5.759  23.229 1.00 71.36  ? 255 HIS A C   1 
ATOM   2028 O  O   . HIS A 1 255 ? 41.478  -4.592  23.268 1.00 81.25  ? 255 HIS A O   1 
ATOM   2029 C  CB  . HIS A 1 255 ? 44.299  -4.969  23.449 1.00 82.38  ? 255 HIS A CB  1 
ATOM   2030 C  CG  . HIS A 1 255 ? 44.541  -4.566  22.032 1.00 83.43  ? 255 HIS A CG  1 
ATOM   2031 N  ND1 . HIS A 1 255 ? 45.457  -5.230  21.241 1.00 85.13  ? 255 HIS A ND1 1 
ATOM   2032 C  CD2 . HIS A 1 255 ? 44.040  -3.554  21.285 1.00 85.11  ? 255 HIS A CD2 1 
ATOM   2033 C  CE1 . HIS A 1 255 ? 45.492  -4.665  20.055 1.00 92.79  ? 255 HIS A CE1 1 
ATOM   2034 N  NE2 . HIS A 1 255 ? 44.626  -3.625  20.053 1.00 90.76  ? 255 HIS A NE2 1 
ATOM   2035 N  N   . THR A 1 256 ? 41.071  -6.751  22.875 1.00 65.82  ? 256 THR A N   1 
ATOM   2036 C  CA  . THR A 1 256 ? 39.633  -6.562  22.607 1.00 65.59  ? 256 THR A CA  1 
ATOM   2037 C  C   . THR A 1 256 ? 38.832  -7.318  23.666 1.00 67.69  ? 256 THR A C   1 
ATOM   2038 O  O   . THR A 1 256 ? 38.973  -8.595  23.762 1.00 69.78  ? 256 THR A O   1 
ATOM   2039 C  CB  . THR A 1 256 ? 39.294  -7.016  21.189 1.00 69.36  ? 256 THR A CB  1 
ATOM   2040 O  OG1 . THR A 1 256 ? 39.972  -6.119  20.316 1.00 73.69  ? 256 THR A OG1 1 
ATOM   2041 C  CG2 . THR A 1 256 ? 37.810  -7.013  20.913 1.00 75.95  ? 256 THR A CG2 1 
ATOM   2042 N  N   . VAL A 1 257 ? 37.979  -6.578  24.373 1.00 63.43  ? 257 VAL A N   1 
ATOM   2043 C  CA  . VAL A 1 257 ? 36.976  -7.134  25.325 1.00 61.49  ? 257 VAL A CA  1 
ATOM   2044 C  C   . VAL A 1 257 ? 35.730  -7.559  24.551 1.00 61.20  ? 257 VAL A C   1 
ATOM   2045 O  O   . VAL A 1 257 ? 35.209  -6.751  23.767 1.00 64.75  ? 257 VAL A O   1 
ATOM   2046 C  CB  . VAL A 1 257 ? 36.604  -6.125  26.419 1.00 63.70  ? 257 VAL A CB  1 
ATOM   2047 C  CG1 . VAL A 1 257 ? 35.445  -6.629  27.267 1.00 63.99  ? 257 VAL A CG1 1 
ATOM   2048 C  CG2 . VAL A 1 257 ? 37.815  -5.773  27.275 1.00 69.72  ? 257 VAL A CG2 1 
ATOM   2049 N  N   . ILE A 1 258 ? 35.284  -8.794  24.767 1.00 62.29  ? 258 ILE A N   1 
ATOM   2050 C  CA  . ILE A 1 258 ? 33.992  -9.282  24.228 1.00 61.39  ? 258 ILE A CA  1 
ATOM   2051 C  C   . ILE A 1 258 ? 33.020  -9.468  25.383 1.00 64.22  ? 258 ILE A C   1 
ATOM   2052 O  O   . ILE A 1 258 ? 33.393  -10.034 26.404 1.00 69.28  ? 258 ILE A O   1 
ATOM   2053 C  CB  . ILE A 1 258 ? 34.155  -10.564 23.420 1.00 60.59  ? 258 ILE A CB  1 
ATOM   2054 C  CG1 . ILE A 1 258 ? 35.072  -10.316 22.225 1.00 68.89  ? 258 ILE A CG1 1 
ATOM   2055 C  CG2 . ILE A 1 258 ? 32.777  -11.046 22.998 1.00 63.74  ? 258 ILE A CG2 1 
ATOM   2056 C  CD1 . ILE A 1 258 ? 35.197  -11.494 21.279 1.00 76.55  ? 258 ILE A CD1 1 
ATOM   2057 N  N   . ILE A 1 259 ? 31.811  -8.966  25.196 1.00 65.59  ? 259 ILE A N   1 
ATOM   2058 C  CA  . ILE A 1 259 ? 30.654  -9.177  26.095 1.00 62.34  ? 259 ILE A CA  1 
ATOM   2059 C  C   . ILE A 1 259 ? 29.570  -9.832  25.248 1.00 65.64  ? 259 ILE A C   1 
ATOM   2060 O  O   . ILE A 1 259 ? 29.118  -9.213  24.283 1.00 81.03  ? 259 ILE A O   1 
ATOM   2061 C  CB  . ILE A 1 259 ? 30.213  -7.839  26.693 1.00 62.49  ? 259 ILE A CB  1 
ATOM   2062 C  CG1 . ILE A 1 259 ? 31.310  -7.241  27.567 1.00 66.57  ? 259 ILE A CG1 1 
ATOM   2063 C  CG2 . ILE A 1 259 ? 28.916  -7.993  27.451 1.00 69.28  ? 259 ILE A CG2 1 
ATOM   2064 C  CD1 . ILE A 1 259 ? 30.953  -5.896  28.164 1.00 70.81  ? 259 ILE A CD1 1 
ATOM   2065 N  N   . PHE A 1 260 ? 29.218  -11.067 25.572 1.00 67.87  ? 260 PHE A N   1 
ATOM   2066 C  CA  . PHE A 1 260 ? 28.202  -11.869 24.856 1.00 67.41  ? 260 PHE A CA  1 
ATOM   2067 C  C   . PHE A 1 260 ? 27.039  -12.102 25.797 1.00 67.13  ? 260 PHE A C   1 
ATOM   2068 O  O   . PHE A 1 260 ? 27.272  -12.691 26.869 1.00 71.54  ? 260 PHE A O   1 
ATOM   2069 C  CB  . PHE A 1 260 ? 28.752  -13.235 24.483 1.00 63.95  ? 260 PHE A CB  1 
ATOM   2070 C  CG  . PHE A 1 260 ? 27.729  -14.129 23.852 1.00 58.06  ? 260 PHE A CG  1 
ATOM   2071 C  CD1 . PHE A 1 260 ? 27.553  -14.122 22.486 1.00 62.79  ? 260 PHE A CD1 1 
ATOM   2072 C  CD2 . PHE A 1 260 ? 26.968  -14.989 24.613 1.00 64.33  ? 260 PHE A CD2 1 
ATOM   2073 C  CE1 . PHE A 1 260 ? 26.635  -14.963 21.878 1.00 69.59  ? 260 PHE A CE1 1 
ATOM   2074 C  CE2 . PHE A 1 260 ? 26.048  -15.832 24.013 1.00 72.19  ? 260 PHE A CE2 1 
ATOM   2075 C  CZ  . PHE A 1 260 ? 25.881  -15.817 22.643 1.00 75.05  ? 260 PHE A CZ  1 
ATOM   2076 N  N   . THR A 1 261 ? 25.855  -11.647 25.420 1.00 63.55  ? 261 THR A N   1 
ATOM   2077 C  CA  . THR A 1 261 ? 24.662  -11.738 26.294 1.00 67.54  ? 261 THR A CA  1 
ATOM   2078 C  C   . THR A 1 261 ? 23.412  -11.634 25.431 1.00 66.58  ? 261 THR A C   1 
ATOM   2079 O  O   . THR A 1 261 ? 23.525  -11.745 24.174 1.00 62.47  ? 261 THR A O   1 
ATOM   2080 C  CB  . THR A 1 261 ? 24.685  -10.712 27.443 1.00 66.91  ? 261 THR A CB  1 
ATOM   2081 O  OG1 . THR A 1 261 ? 23.559  -10.923 28.286 1.00 65.75  ? 261 THR A OG1 1 
ATOM   2082 C  CG2 . THR A 1 261 ? 24.585  -9.270  27.015 1.00 66.98  ? 261 THR A CG2 1 
ATOM   2083 N  N   . SER A 1 262 ? 22.276  -11.497 26.112 1.00 61.10  ? 262 SER A N   1 
ATOM   2084 C  CA  . SER A 1 262 ? 20.931  -11.540 25.505 1.00 62.45  ? 262 SER A CA  1 
ATOM   2085 C  C   . SER A 1 262 ? 20.118  -10.365 26.036 1.00 61.31  ? 262 SER A C   1 
ATOM   2086 O  O   . SER A 1 262 ? 20.480  -9.775  27.065 1.00 55.27  ? 262 SER A O   1 
ATOM   2087 C  CB  . SER A 1 262 ? 20.239  -12.852 25.747 1.00 65.55  ? 262 SER A CB  1 
ATOM   2088 O  OG  . SER A 1 262 ? 19.062  -12.924 24.958 1.00 75.43  ? 262 SER A OG  1 
ATOM   2089 N  N   . ASP A 1 263 ? 19.080  -9.977  25.288 1.00 63.34  ? 263 ASP A N   1 
ATOM   2090 C  CA  . ASP A 1 263 ? 18.243  -8.814  25.688 1.00 57.90  ? 263 ASP A CA  1 
ATOM   2091 C  C   . ASP A 1 263 ? 17.079  -9.317  26.544 1.00 58.59  ? 263 ASP A C   1 
ATOM   2092 O  O   . ASP A 1 263 ? 16.402  -8.481  27.167 1.00 66.24  ? 263 ASP A O   1 
ATOM   2093 C  CB  . ASP A 1 263 ? 17.764  -8.027  24.465 1.00 61.32  ? 263 ASP A CB  1 
ATOM   2094 C  CG  . ASP A 1 263 ? 16.833  -8.816  23.562 1.00 58.95  ? 263 ASP A CG  1 
ATOM   2095 O  OD1 . ASP A 1 263 ? 16.939  -10.060 23.548 1.00 52.22  ? 263 ASP A OD1 1 
ATOM   2096 O  OD2 . ASP A 1 263 ? 16.008  -8.179  22.879 1.00 64.46  ? 263 ASP A OD2 1 
ATOM   2097 N  N   . ASN A 1 264 ? 16.855  -10.633 26.557 1.00 67.41  ? 264 ASN A N   1 
ATOM   2098 C  CA  . ASN A 1 264 ? 15.788  -11.227 27.408 1.00 72.78  ? 264 ASN A CA  1 
ATOM   2099 C  C   . ASN A 1 264 ? 15.807  -12.755 27.282 1.00 72.80  ? 264 ASN A C   1 
ATOM   2100 O  O   . ASN A 1 264 ? 16.598  -13.297 26.468 1.00 68.14  ? 264 ASN A O   1 
ATOM   2101 C  CB  . ASN A 1 264 ? 14.408  -10.659 27.062 1.00 66.77  ? 264 ASN A CB  1 
ATOM   2102 C  CG  . ASN A 1 264 ? 14.115  -10.774 25.591 1.00 65.91  ? 264 ASN A CG  1 
ATOM   2103 O  OD1 . ASN A 1 264 ? 14.186  -9.792  24.858 1.00 68.72  ? 264 ASN A OD1 1 
ATOM   2104 N  ND2 . ASN A 1 264 ? 13.830  -11.982 25.149 1.00 73.18  ? 264 ASN A ND2 1 
ATOM   2105 N  N   . GLY A 1 265 ? 14.959  -13.420 28.067 1.00 72.12  ? 265 GLY A N   1 
ATOM   2106 C  CA  . GLY A 1 265 ? 14.898  -14.894 28.125 1.00 86.18  ? 265 GLY A CA  1 
ATOM   2107 C  C   . GLY A 1 265 ? 14.256  -15.473 26.876 1.00 76.18  ? 265 GLY A C   1 
ATOM   2108 O  O   . GLY A 1 265 ? 13.628  -14.698 26.120 1.00 64.04  ? 265 GLY A O   1 
ATOM   2109 N  N   . GLY A 1 266 ? 14.361  -16.790 26.699 1.00 67.21  ? 266 GLY A N   1 
ATOM   2110 C  CA  . GLY A 1 266 ? 13.917  -17.506 25.485 1.00 69.18  ? 266 GLY A CA  1 
ATOM   2111 C  C   . GLY A 1 266 ? 12.419  -17.424 25.236 1.00 66.43  ? 266 GLY A C   1 
ATOM   2112 O  O   . GLY A 1 266 ? 11.629  -17.470 26.190 1.00 67.48  ? 266 GLY A O   1 
ATOM   2113 N  N   . LEU A 1 267 ? 12.025  -17.340 23.970 1.00 71.79  ? 267 LEU A N   1 
ATOM   2114 C  CA  . LEU A 1 267 ? 10.594  -17.356 23.592 1.00 71.52  ? 267 LEU A CA  1 
ATOM   2115 C  C   . LEU A 1 267 ? 10.052  -18.769 23.807 1.00 75.24  ? 267 LEU A C   1 
ATOM   2116 O  O   . LEU A 1 267 ? 10.768  -19.734 23.572 1.00 96.42  ? 267 LEU A O   1 
ATOM   2117 C  CB  . LEU A 1 267 ? 10.452  -16.919 22.130 1.00 77.65  ? 267 LEU A CB  1 
ATOM   2118 C  CG  . LEU A 1 267 ? 9.018   -16.792 21.595 1.00 78.16  ? 267 LEU A CG  1 
ATOM   2119 C  CD1 . LEU A 1 267 ? 8.086   -16.030 22.533 1.00 73.21  ? 267 LEU A CD1 1 
ATOM   2120 C  CD2 . LEU A 1 267 ? 9.012   -16.090 20.243 1.00 92.53  ? 267 LEU A CD2 1 
ATOM   2121 N  N   . MET A 1 268 ? 8.786   -18.843 24.227 1.00 82.96  ? 268 MET A N   1 
ATOM   2122 C  CA  . MET A 1 268 ? 8.115   -20.143 24.474 1.00 69.98  ? 268 MET A CA  1 
ATOM   2123 C  C   . MET A 1 268 ? 6.614   -19.848 24.552 1.00 77.02  ? 268 MET A C   1 
ATOM   2124 O  O   . MET A 1 268 ? 6.156   -19.504 25.659 1.00 96.71  ? 268 MET A O   1 
ATOM   2125 C  CB  . MET A 1 268 ? 8.600   -20.750 25.793 1.00 73.58  ? 268 MET A CB  1 
ATOM   2126 C  CG  . MET A 1 268 ? 7.874   -22.016 26.193 1.00 87.79  ? 268 MET A CG  1 
ATOM   2127 S  SD  . MET A 1 268 ? 8.477   -22.690 27.759 1.00 95.89  ? 268 MET A SD  1 
ATOM   2128 C  CE  . MET A 1 268 ? 7.532   -21.706 28.921 1.00 85.92  ? 268 MET A CE  1 
ATOM   2129 N  N   . TYR A 1 269 ? 5.874   -19.857 23.433 1.00 71.85  ? 269 TYR A N   1 
ATOM   2130 C  CA  . TYR A 1 269 ? 4.390   -19.631 23.418 1.00 102.61 ? 269 TYR A CA  1 
ATOM   2131 C  C   . TYR A 1 269 ? 4.026   -18.173 23.086 1.00 90.35  ? 269 TYR A C   1 
ATOM   2132 O  O   . TYR A 1 269 ? 3.323   -17.542 23.901 1.00 72.28  ? 269 TYR A O   1 
ATOM   2133 C  CB  . TYR A 1 269 ? 3.699   -20.109 24.701 1.00 102.97 ? 269 TYR A CB  1 
ATOM   2134 C  CG  . TYR A 1 269 ? 3.586   -21.607 24.814 1.00 98.68  ? 269 TYR A CG  1 
ATOM   2135 C  CD1 . TYR A 1 269 ? 2.784   -22.327 23.946 1.00 98.94  ? 269 TYR A CD1 1 
ATOM   2136 C  CD2 . TYR A 1 269 ? 4.290   -22.305 25.779 1.00 96.46  ? 269 TYR A CD2 1 
ATOM   2137 C  CE1 . TYR A 1 269 ? 2.675   -23.703 24.041 1.00 94.74  ? 269 TYR A CE1 1 
ATOM   2138 C  CE2 . TYR A 1 269 ? 4.194   -23.682 25.887 1.00 92.44  ? 269 TYR A CE2 1 
ATOM   2139 C  CZ  . TYR A 1 269 ? 3.382   -24.384 25.015 1.00 92.37  ? 269 TYR A CZ  1 
ATOM   2140 O  OH  . TYR A 1 269 ? 3.281   -25.741 25.111 1.00 93.57  ? 269 TYR A OH  1 
ATOM   2141 N  N   . GLU A 1 270 ? 4.477   -17.659 21.944 1.00 90.53  ? 270 GLU A N   1 
ATOM   2142 C  CA  . GLU A 1 270 ? 4.139   -16.315 21.417 1.00 94.59  ? 270 GLU A CA  1 
ATOM   2143 C  C   . GLU A 1 270 ? 2.621   -16.307 21.225 1.00 82.77  ? 270 GLU A C   1 
ATOM   2144 O  O   . GLU A 1 270 ? 2.161   -17.014 20.338 1.00 93.14  ? 270 GLU A O   1 
ATOM   2145 C  CB  . GLU A 1 270 ? 4.948   -16.069 20.126 1.00 108.43 ? 270 GLU A CB  1 
ATOM   2146 C  CG  . GLU A 1 270 ? 4.618   -14.779 19.371 1.00 99.60  ? 270 GLU A CG  1 
ATOM   2147 C  CD  . GLU A 1 270 ? 5.177   -13.496 19.969 1.00 104.38 ? 270 GLU A CD  1 
ATOM   2148 O  OE1 . GLU A 1 270 ? 6.364   -13.164 19.731 1.00 105.24 ? 270 GLU A OE1 1 
ATOM   2149 O  OE2 . GLU A 1 270 ? 4.428   -12.858 20.707 1.00 114.66 ? 270 GLU A OE2 1 
ATOM   2150 N  N   . GLY A 1 271 ? 1.896   -15.632 22.113 1.00 90.63  ? 271 GLY A N   1 
ATOM   2151 C  CA  . GLY A 1 271 ? 0.471   -15.280 21.991 1.00 95.97  ? 271 GLY A CA  1 
ATOM   2152 C  C   . GLY A 1 271 ? -0.393  -16.286 21.258 1.00 95.96  ? 271 GLY A C   1 
ATOM   2153 O  O   . GLY A 1 271 ? -0.624  -16.176 20.040 1.00 131.53 ? 271 GLY A O   1 
ATOM   2154 N  N   . SER A 1 272 ? -0.965  -17.210 21.991 1.00 101.88 ? 272 SER A N   1 
ATOM   2155 C  CA  . SER A 1 272 ? -2.022  -18.157 21.503 1.00 108.12 ? 272 SER A CA  1 
ATOM   2156 C  C   . SER A 1 272 ? -1.492  -19.174 20.489 1.00 98.99  ? 272 SER A C   1 
ATOM   2157 O  O   . SER A 1 272 ? -2.321  -19.798 19.885 1.00 84.42  ? 272 SER A O   1 
ATOM   2158 C  CB  . SER A 1 272 ? -3.230  -17.475 20.878 1.00 84.15  ? 272 SER A CB  1 
ATOM   2159 O  OG  . SER A 1 272 ? -3.661  -16.433 21.718 1.00 123.87 ? 272 SER A OG  1 
ATOM   2160 N  N   . ARG A 1 273 ? -0.169  -19.272 20.341 1.00 109.35 ? 273 ARG A N   1 
ATOM   2161 C  CA  . ARG A 1 273 ? 0.420   -20.310 19.460 1.00 96.15  ? 273 ARG A CA  1 
ATOM   2162 C  C   . ARG A 1 273 ? 0.443   -21.610 20.266 1.00 92.03  ? 273 ARG A C   1 
ATOM   2163 O  O   . ARG A 1 273 ? 0.888   -21.576 21.430 1.00 77.56  ? 273 ARG A O   1 
ATOM   2164 C  CB  . ARG A 1 273 ? 1.806   -19.882 18.969 1.00 117.93 ? 273 ARG A CB  1 
ATOM   2165 C  CG  . ARG A 1 273 ? 1.770   -18.843 17.858 1.00 132.85 ? 273 ARG A CG  1 
ATOM   2166 C  CD  . ARG A 1 273 ? 1.882   -19.474 16.484 1.00 142.91 ? 273 ARG A CD  1 
ATOM   2167 N  NE  . ARG A 1 273 ? 3.260   -19.788 16.136 1.00 150.36 ? 273 ARG A NE  1 
ATOM   2168 C  CZ  . ARG A 1 273 ? 4.145   -18.901 15.695 1.00 144.48 ? 273 ARG A CZ  1 
ATOM   2169 N  NH1 . ARG A 1 273 ? 3.797   -17.635 15.545 1.00 137.21 ? 273 ARG A NH1 1 
ATOM   2170 N  NH2 . ARG A 1 273 ? 5.376   -19.284 15.405 1.00 132.52 ? 273 ARG A NH2 1 
ATOM   2171 N  N   . ARG A 1 274 ? 0.017   -22.730 19.676 1.00 111.33 ? 274 ARG A N   1 
ATOM   2172 C  CA  . ARG A 1 274 ? -0.089  -23.999 20.452 1.00 117.66 ? 274 ARG A CA  1 
ATOM   2173 C  C   . ARG A 1 274 ? 1.295   -24.571 20.793 1.00 94.49  ? 274 ARG A C   1 
ATOM   2174 O  O   . ARG A 1 274 ? 1.381   -25.359 21.751 1.00 82.47  ? 274 ARG A O   1 
ATOM   2175 C  CB  . ARG A 1 274 ? -0.915  -25.035 19.683 1.00 126.87 ? 274 ARG A CB  1 
ATOM   2176 C  CG  . ARG A 1 274 ? -1.715  -25.966 20.583 1.00 136.70 ? 274 ARG A CG  1 
ATOM   2177 C  CD  . ARG A 1 274 ? -2.030  -25.326 21.922 1.00 142.53 ? 274 ARG A CD  1 
ATOM   2178 N  NE  . ARG A 1 274 ? -1.266  -25.907 23.017 1.00 150.97 ? 274 ARG A NE  1 
ATOM   2179 C  CZ  . ARG A 1 274 ? -0.524  -25.210 23.869 1.00 151.30 ? 274 ARG A CZ  1 
ATOM   2180 N  NH1 . ARG A 1 274 ? -0.435  -23.897 23.747 1.00 168.72 ? 274 ARG A NH1 1 
ATOM   2181 N  NH2 . ARG A 1 274 ? 0.138   -25.827 24.831 1.00 144.20 ? 274 ARG A NH2 1 
ATOM   2182 N  N   . GLU A 1 275 ? 2.331   -24.215 20.031 1.00 105.38 ? 275 GLU A N   1 
ATOM   2183 C  CA  . GLU A 1 275 ? 3.685   -24.808 20.264 1.00 104.77 ? 275 GLU A CA  1 
ATOM   2184 C  C   . GLU A 1 275 ? 4.624   -23.777 20.894 1.00 100.04 ? 275 GLU A C   1 
ATOM   2185 O  O   . GLU A 1 275 ? 4.667   -22.619 20.445 1.00 131.31 ? 275 GLU A O   1 
ATOM   2186 C  CB  . GLU A 1 275 ? 4.269   -25.284 18.924 1.00 125.36 ? 275 GLU A CB  1 
ATOM   2187 C  CG  . GLU A 1 275 ? 3.639   -26.545 18.343 1.00 131.24 ? 275 GLU A CG  1 
ATOM   2188 C  CD  . GLU A 1 275 ? 3.336   -27.637 19.358 1.00 134.11 ? 275 GLU A CD  1 
ATOM   2189 O  OE1 . GLU A 1 275 ? 4.266   -28.165 19.994 1.00 121.35 ? 275 GLU A OE1 1 
ATOM   2190 O  OE2 . GLU A 1 275 ? 2.155   -27.930 19.535 1.00 169.88 ? 275 GLU A OE2 1 
ATOM   2191 N  N   . PRO A 1 276 ? 5.444   -24.158 21.906 1.00 92.96  ? 276 PRO A N   1 
ATOM   2192 C  CA  . PRO A 1 276 ? 6.530   -23.300 22.403 1.00 100.25 ? 276 PRO A CA  1 
ATOM   2193 C  C   . PRO A 1 276 ? 7.738   -23.288 21.453 1.00 88.69  ? 276 PRO A C   1 
ATOM   2194 O  O   . PRO A 1 276 ? 7.897   -24.200 20.707 1.00 88.00  ? 276 PRO A O   1 
ATOM   2195 C  CB  . PRO A 1 276 ? 6.959   -23.937 23.734 1.00 85.60  ? 276 PRO A CB  1 
ATOM   2196 C  CG  . PRO A 1 276 ? 6.643   -25.388 23.528 1.00 89.45  ? 276 PRO A CG  1 
ATOM   2197 C  CD  . PRO A 1 276 ? 5.417   -25.439 22.618 1.00 96.14  ? 276 PRO A CD  1 
ATOM   2198 N  N   . VAL A 1 277 ? 8.562   -22.251 21.486 1.00 87.13  ? 277 VAL A N   1 
ATOM   2199 C  CA  . VAL A 1 277 ? 9.705   -22.138 20.534 1.00 82.23  ? 277 VAL A CA  1 
ATOM   2200 C  C   . VAL A 1 277 ? 10.942  -22.825 21.135 1.00 78.34  ? 277 VAL A C   1 
ATOM   2201 O  O   . VAL A 1 277 ? 11.552  -23.690 20.459 1.00 79.22  ? 277 VAL A O   1 
ATOM   2202 C  CB  . VAL A 1 277 ? 9.967   -20.673 20.143 1.00 82.28  ? 277 VAL A CB  1 
ATOM   2203 C  CG1 . VAL A 1 277 ? 11.079  -20.603 19.110 1.00 87.86  ? 277 VAL A CG1 1 
ATOM   2204 C  CG2 . VAL A 1 277 ? 8.698   -19.972 19.638 1.00 86.90  ? 277 VAL A CG2 1 
ATOM   2205 N  N   . THR A 1 278 ? 11.330  -22.440 22.340 1.00 66.08  ? 278 THR A N   1 
ATOM   2206 C  CA  . THR A 1 278 ? 12.356  -23.163 23.126 1.00 79.57  ? 278 THR A CA  1 
ATOM   2207 C  C   . THR A 1 278 ? 11.808  -23.427 24.539 1.00 86.94  ? 278 THR A C   1 
ATOM   2208 O  O   . THR A 1 278 ? 10.612  -23.197 24.799 1.00 76.11  ? 278 THR A O   1 
ATOM   2209 C  CB  . THR A 1 278 ? 13.700  -22.416 23.126 1.00 87.16  ? 278 THR A CB  1 
ATOM   2210 O  OG1 . THR A 1 278 ? 14.745  -23.228 23.684 1.00 86.86  ? 278 THR A OG1 1 
ATOM   2211 C  CG2 . THR A 1 278 ? 13.637  -21.120 23.903 1.00 90.02  ? 278 THR A CG2 1 
ATOM   2212 N  N   . SER A 1 279 ? 12.661  -23.950 25.413 1.00 88.88  ? 279 SER A N   1 
ATOM   2213 C  CA  . SER A 1 279 ? 12.357  -24.195 26.835 1.00 85.97  ? 279 SER A CA  1 
ATOM   2214 C  C   . SER A 1 279 ? 13.544  -23.663 27.621 1.00 85.62  ? 279 SER A C   1 
ATOM   2215 O  O   . SER A 1 279 ? 14.695  -23.697 27.105 1.00 81.63  ? 279 SER A O   1 
ATOM   2216 C  CB  . SER A 1 279 ? 12.098  -25.661 27.109 1.00 109.15 ? 279 SER A CB  1 
ATOM   2217 O  OG  . SER A 1 279 ? 12.075  -25.951 28.509 1.00 111.94 ? 279 SER A OG  1 
ATOM   2218 N  N   . ASN A 1 280 ? 13.245  -23.156 28.805 1.00 83.21  ? 280 ASN A N   1 
ATOM   2219 C  CA  . ASN A 1 280 ? 14.230  -22.542 29.710 1.00 83.60  ? 280 ASN A CA  1 
ATOM   2220 C  C   . ASN A 1 280 ? 14.316  -23.406 30.961 1.00 83.80  ? 280 ASN A C   1 
ATOM   2221 O  O   . ASN A 1 280 ? 14.984  -22.986 31.906 1.00 78.64  ? 280 ASN A O   1 
ATOM   2222 C  CB  . ASN A 1 280 ? 13.840  -21.092 29.971 1.00 95.72  ? 280 ASN A CB  1 
ATOM   2223 C  CG  . ASN A 1 280 ? 13.985  -20.241 28.726 1.00 95.42  ? 280 ASN A CG  1 
ATOM   2224 O  OD1 . ASN A 1 280 ? 15.007  -20.312 28.031 1.00 95.89  ? 280 ASN A OD1 1 
ATOM   2225 N  ND2 . ASN A 1 280 ? 12.951  -19.464 28.434 1.00 79.21  ? 280 ASN A ND2 1 
ATOM   2226 N  N   . ARG A 1 281 ? 13.680  -24.582 30.967 1.00 100.70 ? 281 ARG A N   1 
ATOM   2227 C  CA  . ARG A 1 281 ? 13.826  -25.528 32.103 1.00 95.89  ? 281 ARG A CA  1 
ATOM   2228 C  C   . ARG A 1 281 ? 15.314  -25.577 32.385 1.00 73.88  ? 281 ARG A C   1 
ATOM   2229 O  O   . ARG A 1 281 ? 16.114  -25.581 31.448 1.00 65.03  ? 281 ARG A O   1 
ATOM   2230 C  CB  . ARG A 1 281 ? 13.228  -26.913 31.833 1.00 121.27 ? 281 ARG A CB  1 
ATOM   2231 C  CG  . ARG A 1 281 ? 11.747  -26.982 32.172 1.00 144.56 ? 281 ARG A CG  1 
ATOM   2232 C  CD  . ARG A 1 281 ? 11.214  -28.301 32.716 1.00 145.86 ? 281 ARG A CD  1 
ATOM   2233 N  NE  . ARG A 1 281 ? 9.771   -28.124 32.913 1.00 154.67 ? 281 ARG A NE  1 
ATOM   2234 C  CZ  . ARG A 1 281 ? 8.817   -29.023 32.662 1.00 139.82 ? 281 ARG A CZ  1 
ATOM   2235 N  NH1 . ARG A 1 281 ? 9.127   -30.220 32.194 1.00 152.54 ? 281 ARG A NH1 1 
ATOM   2236 N  NH2 . ARG A 1 281 ? 7.546   -28.714 32.876 1.00 121.69 ? 281 ARG A NH2 1 
ATOM   2237 N  N   . PRO A 1 282 ? 15.724  -25.540 33.669 1.00 69.14  ? 282 PRO A N   1 
ATOM   2238 C  CA  . PRO A 1 282 ? 14.798  -25.542 34.817 1.00 76.27  ? 282 PRO A CA  1 
ATOM   2239 C  C   . PRO A 1 282 ? 13.936  -24.312 35.130 1.00 79.59  ? 282 PRO A C   1 
ATOM   2240 O  O   . PRO A 1 282 ? 13.008  -24.428 35.924 1.00 85.70  ? 282 PRO A O   1 
ATOM   2241 C  CB  . PRO A 1 282 ? 15.731  -25.611 36.034 1.00 73.33  ? 282 PRO A CB  1 
ATOM   2242 C  CG  . PRO A 1 282 ? 17.046  -25.088 35.521 1.00 67.56  ? 282 PRO A CG  1 
ATOM   2243 C  CD  . PRO A 1 282 ? 17.135  -25.542 34.078 1.00 62.51  ? 282 PRO A CD  1 
ATOM   2244 N  N   . LEU A 1 283 ? 14.288  -23.174 34.539 1.00 78.83  ? 283 LEU A N   1 
ATOM   2245 C  CA  . LEU A 1 283 ? 13.705  -21.857 34.889 1.00 79.48  ? 283 LEU A CA  1 
ATOM   2246 C  C   . LEU A 1 283 ? 12.253  -21.805 34.432 1.00 75.66  ? 283 LEU A C   1 
ATOM   2247 O  O   . LEU A 1 283 ? 11.944  -22.338 33.297 1.00 59.27  ? 283 LEU A O   1 
ATOM   2248 C  CB  . LEU A 1 283 ? 14.497  -20.749 34.203 1.00 76.39  ? 283 LEU A CB  1 
ATOM   2249 C  CG  . LEU A 1 283 ? 15.995  -20.772 34.441 1.00 73.42  ? 283 LEU A CG  1 
ATOM   2250 C  CD1 . LEU A 1 283 ? 16.588  -19.569 33.765 1.00 86.10  ? 283 LEU A CD1 1 
ATOM   2251 C  CD2 . LEU A 1 283 ? 16.325  -20.763 35.923 1.00 80.73  ? 283 LEU A CD2 1 
ATOM   2252 N  N   . ARG A 1 284 ? 11.440  -21.109 35.234 1.00 68.59  ? 284 ARG A N   1 
ATOM   2253 C  CA  . ARG A 1 284 ? 9.990   -20.961 34.936 1.00 74.52  ? 284 ARG A CA  1 
ATOM   2254 C  C   . ARG A 1 284 ? 9.782   -20.013 33.756 1.00 66.12  ? 284 ARG A C   1 
ATOM   2255 O  O   . ARG A 1 284 ? 10.364  -18.946 33.771 1.00 75.00  ? 284 ARG A O   1 
ATOM   2256 C  CB  . ARG A 1 284 ? 9.202   -20.460 36.149 1.00 80.71  ? 284 ARG A CB  1 
ATOM   2257 C  CG  . ARG A 1 284 ? 7.689   -20.493 35.967 1.00 71.59  ? 284 ARG A CG  1 
ATOM   2258 C  CD  . ARG A 1 284 ? 7.033   -20.297 37.311 1.00 75.62  ? 284 ARG A CD  1 
ATOM   2259 N  NE  . ARG A 1 284 ? 5.612   -20.052 37.121 1.00 92.89  ? 284 ARG A NE  1 
ATOM   2260 C  CZ  . ARG A 1 284 ? 4.756   -19.759 38.099 1.00 93.15  ? 284 ARG A CZ  1 
ATOM   2261 N  NH1 . ARG A 1 284 ? 5.169   -19.694 39.359 1.00 82.78  ? 284 ARG A NH1 1 
ATOM   2262 N  NH2 . ARG A 1 284 ? 3.481   -19.548 37.807 1.00 97.17  ? 284 ARG A NH2 1 
ATOM   2263 N  N   . ALA A 1 285 ? 8.946   -20.403 32.797 1.00 75.07  ? 285 ALA A N   1 
ATOM   2264 C  CA  . ALA A 1 285 ? 8.425   -19.545 31.711 1.00 78.72  ? 285 ALA A CA  1 
ATOM   2265 C  C   . ALA A 1 285 ? 9.588   -19.083 30.816 1.00 82.67  ? 285 ALA A C   1 
ATOM   2266 O  O   . ALA A 1 285 ? 10.512  -19.938 30.539 1.00 82.43  ? 285 ALA A O   1 
ATOM   2267 C  CB  . ALA A 1 285 ? 7.629   -18.414 32.326 1.00 76.28  ? 285 ALA A CB  1 
ATOM   2268 N  N   . GLY A 1 286 ? 9.541   -17.810 30.380 1.00 77.89  ? 286 GLY A N   1 
ATOM   2269 C  CA  . GLY A 1 286 ? 10.438  -17.224 29.362 1.00 79.43  ? 286 GLY A CA  1 
ATOM   2270 C  C   . GLY A 1 286 ? 10.022  -15.812 28.982 1.00 72.87  ? 286 GLY A C   1 
ATOM   2271 O  O   . GLY A 1 286 ? 9.367   -15.154 29.818 1.00 66.86  ? 286 GLY A O   1 
ATOM   2272 N  N   . LYS A 1 287 ? 10.354  -15.392 27.750 1.00 73.90  ? 287 LYS A N   1 
ATOM   2273 C  CA  . LYS A 1 287 ? 10.284  -13.985 27.270 1.00 71.93  ? 287 LYS A CA  1 
ATOM   2274 C  C   . LYS A 1 287 ? 8.909   -13.479 27.625 1.00 68.75  ? 287 LYS A C   1 
ATOM   2275 O  O   . LYS A 1 287 ? 7.972   -14.221 27.365 1.00 77.29  ? 287 LYS A O   1 
ATOM   2276 C  CB  . LYS A 1 287 ? 10.427  -13.867 25.746 1.00 76.69  ? 287 LYS A CB  1 
ATOM   2277 C  CG  . LYS A 1 287 ? 10.216  -12.473 25.143 1.00 75.39  ? 287 LYS A CG  1 
ATOM   2278 C  CD  . LYS A 1 287 ? 10.472  -12.388 23.622 1.00 75.91  ? 287 LYS A CD  1 
ATOM   2279 C  CE  . LYS A 1 287 ? 10.462  -10.985 23.031 1.00 80.94  ? 287 LYS A CE  1 
ATOM   2280 N  NZ  . LYS A 1 287 ? 9.822   -10.908 21.690 1.00 85.35  ? 287 LYS A NZ  1 
ATOM   2281 N  N   . GLY A 1 288 ? 8.816   -12.290 28.198 1.00 65.35  ? 288 GLY A N   1 
ATOM   2282 C  CA  . GLY A 1 288 ? 7.516   -11.650 28.460 1.00 69.10  ? 288 GLY A CA  1 
ATOM   2283 C  C   . GLY A 1 288 ? 7.048   -11.852 29.890 1.00 69.04  ? 288 GLY A C   1 
ATOM   2284 O  O   . GLY A 1 288 ? 6.011   -11.244 30.254 1.00 72.90  ? 288 GLY A O   1 
ATOM   2285 N  N   . HIS A 1 289 ? 7.800   -12.614 30.692 1.00 66.42  ? 289 HIS A N   1 
ATOM   2286 C  CA  . HIS A 1 289 ? 7.444   -12.936 32.100 1.00 68.35  ? 289 HIS A CA  1 
ATOM   2287 C  C   . HIS A 1 289 ? 8.524   -12.465 33.068 1.00 61.93  ? 289 HIS A C   1 
ATOM   2288 O  O   . HIS A 1 289 ? 9.705   -12.458 32.669 1.00 60.55  ? 289 HIS A O   1 
ATOM   2289 C  CB  . HIS A 1 289 ? 7.235   -14.439 32.240 1.00 77.21  ? 289 HIS A CB  1 
ATOM   2290 C  CG  . HIS A 1 289 ? 6.013   -14.908 31.544 1.00 75.60  ? 289 HIS A CG  1 
ATOM   2291 N  ND1 . HIS A 1 289 ? 4.812   -15.013 32.200 1.00 80.39  ? 289 HIS A ND1 1 
ATOM   2292 C  CD2 . HIS A 1 289 ? 5.800   -15.260 30.258 1.00 74.85  ? 289 HIS A CD2 1 
ATOM   2293 C  CE1 . HIS A 1 289 ? 3.908   -15.463 31.347 1.00 95.12  ? 289 HIS A CE1 1 
ATOM   2294 N  NE2 . HIS A 1 289 ? 4.491   -15.621 30.146 1.00 79.91  ? 289 HIS A NE2 1 
ATOM   2295 N  N   . LEU A 1 290 ? 8.147   -12.162 34.312 1.00 58.51  ? 290 LEU A N   1 
ATOM   2296 C  CA  . LEU A 1 290 ? 9.142   -11.722 35.326 1.00 65.79  ? 290 LEU A CA  1 
ATOM   2297 C  C   . LEU A 1 290 ? 9.758   -12.922 36.061 1.00 66.46  ? 290 LEU A C   1 
ATOM   2298 O  O   . LEU A 1 290 ? 10.669  -12.722 36.890 1.00 64.98  ? 290 LEU A O   1 
ATOM   2299 C  CB  . LEU A 1 290 ? 8.486   -10.729 36.288 1.00 70.67  ? 290 LEU A CB  1 
ATOM   2300 C  CG  . LEU A 1 290 ? 8.434   -9.279  35.805 1.00 73.06  ? 290 LEU A CG  1 
ATOM   2301 C  CD1 . LEU A 1 290 ? 7.997   -8.353  36.919 1.00 77.12  ? 290 LEU A CD1 1 
ATOM   2302 C  CD2 . LEU A 1 290 ? 9.770   -8.823  35.251 1.00 71.39  ? 290 LEU A CD2 1 
ATOM   2303 N  N   . TYR A 1 291 ? 9.319   -14.140 35.770 1.00 71.81  ? 291 TYR A N   1 
ATOM   2304 C  CA  . TYR A 1 291 ? 9.970   -15.363 36.300 1.00 67.62  ? 291 TYR A CA  1 
ATOM   2305 C  C   . TYR A 1 291 ? 11.342  -15.454 35.627 1.00 66.68  ? 291 TYR A C   1 
ATOM   2306 O  O   . TYR A 1 291 ? 11.518  -14.876 34.539 1.00 74.76  ? 291 TYR A O   1 
ATOM   2307 C  CB  . TYR A 1 291 ? 9.096   -16.602 36.074 1.00 67.47  ? 291 TYR A CB  1 
ATOM   2308 C  CG  . TYR A 1 291 ? 7.742   -16.565 36.740 1.00 69.35  ? 291 TYR A CG  1 
ATOM   2309 C  CD1 . TYR A 1 291 ? 7.633   -16.586 38.119 1.00 66.62  ? 291 TYR A CD1 1 
ATOM   2310 C  CD2 . TYR A 1 291 ? 6.572   -16.493 35.994 1.00 73.64  ? 291 TYR A CD2 1 
ATOM   2311 C  CE1 . TYR A 1 291 ? 6.398   -16.546 38.743 1.00 68.87  ? 291 TYR A CE1 1 
ATOM   2312 C  CE2 . TYR A 1 291 ? 5.328   -16.431 36.603 1.00 80.35  ? 291 TYR A CE2 1 
ATOM   2313 C  CZ  . TYR A 1 291 ? 5.244   -16.466 37.985 1.00 75.63  ? 291 TYR A CZ  1 
ATOM   2314 O  OH  . TYR A 1 291 ? 4.032   -16.413 38.611 1.00 73.00  ? 291 TYR A OH  1 
ATOM   2315 N  N   . GLU A 1 292 ? 12.266  -16.183 36.252 1.00 69.53  ? 292 GLU A N   1 
ATOM   2316 C  CA  . GLU A 1 292 ? 13.697  -16.295 35.862 1.00 63.03  ? 292 GLU A CA  1 
ATOM   2317 C  C   . GLU A 1 292 ? 13.806  -16.695 34.384 1.00 62.71  ? 292 GLU A C   1 
ATOM   2318 O  O   . GLU A 1 292 ? 14.798  -16.328 33.753 1.00 69.56  ? 292 GLU A O   1 
ATOM   2319 C  CB  . GLU A 1 292 ? 14.426  -17.256 36.802 1.00 63.42  ? 292 GLU A CB  1 
ATOM   2320 C  CG  . GLU A 1 292 ? 14.486  -16.729 38.227 1.00 65.84  ? 292 GLU A CG  1 
ATOM   2321 C  CD  . GLU A 1 292 ? 15.570  -15.697 38.490 1.00 76.22  ? 292 GLU A CD  1 
ATOM   2322 O  OE1 . GLU A 1 292 ? 16.743  -16.094 38.294 1.00 77.86  ? 292 GLU A OE1 1 
ATOM   2323 O  OE2 . GLU A 1 292 ? 15.259  -14.504 38.918 1.00 84.10  ? 292 GLU A OE2 1 
ATOM   2324 N  N   . GLY A 1 293 ? 12.810  -17.360 33.806 1.00 61.03  ? 293 GLY A N   1 
ATOM   2325 C  CA  . GLY A 1 293 ? 12.893  -17.790 32.396 1.00 69.92  ? 293 GLY A CA  1 
ATOM   2326 C  C   . GLY A 1 293 ? 13.062  -16.614 31.445 1.00 72.70  ? 293 GLY A C   1 
ATOM   2327 O  O   . GLY A 1 293 ? 13.750  -16.785 30.363 1.00 80.11  ? 293 GLY A O   1 
ATOM   2328 N  N   . GLY A 1 294 ? 12.477  -15.477 31.845 1.00 67.47  ? 294 GLY A N   1 
ATOM   2329 C  CA  . GLY A 1 294 ? 12.307  -14.275 31.015 1.00 70.85  ? 294 GLY A CA  1 
ATOM   2330 C  C   . GLY A 1 294 ? 13.366  -13.234 31.301 1.00 70.80  ? 294 GLY A C   1 
ATOM   2331 O  O   . GLY A 1 294 ? 13.436  -12.280 30.550 1.00 81.15  ? 294 GLY A O   1 
ATOM   2332 N  N   . VAL A 1 295 ? 14.185  -13.413 32.328 1.00 65.39  ? 295 VAL A N   1 
ATOM   2333 C  CA  . VAL A 1 295 ? 15.103  -12.342 32.801 1.00 65.15  ? 295 VAL A CA  1 
ATOM   2334 C  C   . VAL A 1 295 ? 16.526  -12.879 32.961 1.00 67.80  ? 295 VAL A C   1 
ATOM   2335 O  O   . VAL A 1 295 ? 17.457  -12.095 32.833 1.00 79.20  ? 295 VAL A O   1 
ATOM   2336 C  CB  . VAL A 1 295 ? 14.552  -11.711 34.089 1.00 68.21  ? 295 VAL A CB  1 
ATOM   2337 C  CG1 . VAL A 1 295 ? 13.377  -10.803 33.789 1.00 71.47  ? 295 VAL A CG1 1 
ATOM   2338 C  CG2 . VAL A 1 295 ? 14.120  -12.754 35.094 1.00 81.60  ? 295 VAL A CG2 1 
ATOM   2339 N  N   . ARG A 1 296 ? 16.708  -14.172 33.200 1.00 72.47  ? 296 ARG A N   1 
ATOM   2340 C  CA  . ARG A 1 296 ? 18.062  -14.755 33.345 1.00 74.82  ? 296 ARG A CA  1 
ATOM   2341 C  C   . ARG A 1 296 ? 18.518  -15.095 31.942 1.00 69.40  ? 296 ARG A C   1 
ATOM   2342 O  O   . ARG A 1 296 ? 17.715  -15.776 31.171 1.00 67.52  ? 296 ARG A O   1 
ATOM   2343 C  CB  . ARG A 1 296 ? 18.065  -15.994 34.244 1.00 90.76  ? 296 ARG A CB  1 
ATOM   2344 C  CG  . ARG A 1 296 ? 19.347  -16.280 35.025 1.00 93.62  ? 296 ARG A CG  1 
ATOM   2345 C  CD  . ARG A 1 296 ? 18.948  -17.170 36.199 1.00 83.87  ? 296 ARG A CD  1 
ATOM   2346 N  NE  . ARG A 1 296 ? 20.026  -17.777 36.936 1.00 77.26  ? 296 ARG A NE  1 
ATOM   2347 C  CZ  . ARG A 1 296 ? 19.914  -18.175 38.192 1.00 89.38  ? 296 ARG A CZ  1 
ATOM   2348 N  NH1 . ARG A 1 296 ? 18.777  -18.042 38.848 1.00 82.52  ? 296 ARG A NH1 1 
ATOM   2349 N  NH2 . ARG A 1 296 ? 20.949  -18.699 38.815 1.00 110.02 ? 296 ARG A NH2 1 
ATOM   2350 N  N   . VAL A 1 297 ? 19.732  -14.626 31.647 1.00 66.77  ? 297 VAL A N   1 
ATOM   2351 C  CA  . VAL A 1 297 ? 20.339  -14.707 30.294 1.00 65.38  ? 297 VAL A CA  1 
ATOM   2352 C  C   . VAL A 1 297 ? 21.778  -15.192 30.402 1.00 62.93  ? 297 VAL A C   1 
ATOM   2353 O  O   . VAL A 1 297 ? 22.403  -15.208 31.490 1.00 64.81  ? 297 VAL A O   1 
ATOM   2354 C  CB  . VAL A 1 297 ? 20.257  -13.345 29.587 1.00 74.22  ? 297 VAL A CB  1 
ATOM   2355 C  CG1 . VAL A 1 297 ? 18.820  -12.971 29.233 1.00 79.75  ? 297 VAL A CG1 1 
ATOM   2356 C  CG2 . VAL A 1 297 ? 20.905  -12.261 30.434 1.00 77.79  ? 297 VAL A CG2 1 
ATOM   2357 N  N   . PRO A 1 298 ? 22.310  -15.633 29.238 1.00 58.80  ? 298 PRO A N   1 
ATOM   2358 C  CA  . PRO A 1 298 ? 23.726  -15.938 29.096 1.00 56.59  ? 298 PRO A CA  1 
ATOM   2359 C  C   . PRO A 1 298 ? 24.566  -14.680 29.271 1.00 59.89  ? 298 PRO A C   1 
ATOM   2360 O  O   . PRO A 1 298 ? 24.154  -13.616 28.875 1.00 65.82  ? 298 PRO A O   1 
ATOM   2361 C  CB  . PRO A 1 298 ? 23.877  -16.373 27.640 1.00 61.81  ? 298 PRO A CB  1 
ATOM   2362 C  CG  . PRO A 1 298 ? 22.487  -16.804 27.232 1.00 69.02  ? 298 PRO A CG  1 
ATOM   2363 C  CD  . PRO A 1 298 ? 21.572  -15.863 27.982 1.00 64.77  ? 298 PRO A CD  1 
ATOM   2364 N  N   . LEU A 1 299 ? 25.740  -14.829 29.843 1.00 61.77  ? 299 LEU A N   1 
ATOM   2365 C  CA  . LEU A 1 299 ? 26.700  -13.711 29.862 1.00 62.38  ? 299 LEU A CA  1 
ATOM   2366 C  C   . LEU A 1 299 ? 28.091  -14.310 29.911 1.00 66.10  ? 299 LEU A C   1 
ATOM   2367 O  O   . LEU A 1 299 ? 28.392  -15.007 30.894 1.00 65.50  ? 299 LEU A O   1 
ATOM   2368 C  CB  . LEU A 1 299 ? 26.447  -12.799 31.061 1.00 60.90  ? 299 LEU A CB  1 
ATOM   2369 C  CG  . LEU A 1 299 ? 27.523  -11.731 31.260 1.00 60.20  ? 299 LEU A CG  1 
ATOM   2370 C  CD1 . LEU A 1 299 ? 27.583  -10.874 30.012 1.00 60.20  ? 299 LEU A CD1 1 
ATOM   2371 C  CD2 . LEU A 1 299 ? 27.286  -10.886 32.515 1.00 57.68  ? 299 LEU A CD2 1 
ATOM   2372 N  N   . ILE A 1 300 ? 28.872  -14.053 28.869 1.00 67.18  ? 300 ILE A N   1 
ATOM   2373 C  CA  . ILE A 1 300 ? 30.289  -14.478 28.799 1.00 68.01  ? 300 ILE A CA  1 
ATOM   2374 C  C   . ILE A 1 300 ? 31.108  -13.236 28.500 1.00 64.72  ? 300 ILE A C   1 
ATOM   2375 O  O   . ILE A 1 300 ? 30.717  -12.493 27.618 1.00 75.78  ? 300 ILE A O   1 
ATOM   2376 C  CB  . ILE A 1 300 ? 30.474  -15.559 27.732 1.00 68.90  ? 300 ILE A CB  1 
ATOM   2377 C  CG1 . ILE A 1 300 ? 29.537  -16.738 27.985 1.00 69.15  ? 300 ILE A CG1 1 
ATOM   2378 C  CG2 . ILE A 1 300 ? 31.933  -15.979 27.664 1.00 74.62  ? 300 ILE A CG2 1 
ATOM   2379 C  CD1 . ILE A 1 300 ? 29.342  -17.630 26.782 1.00 74.54  ? 300 ILE A CD1 1 
ATOM   2380 N  N   . ILE A 1 301 ? 32.213  -13.059 29.201 1.00 62.29  ? 301 ILE A N   1 
ATOM   2381 C  CA  . ILE A 1 301 ? 33.131  -11.914 28.999 1.00 65.53  ? 301 ILE A CA  1 
ATOM   2382 C  C   . ILE A 1 301 ? 34.552  -12.441 28.823 1.00 69.57  ? 301 ILE A C   1 
ATOM   2383 O  O   . ILE A 1 301 ? 35.098  -13.009 29.793 1.00 69.54  ? 301 ILE A O   1 
ATOM   2384 C  CB  . ILE A 1 301 ? 33.011  -10.961 30.188 1.00 67.54  ? 301 ILE A CB  1 
ATOM   2385 C  CG1 . ILE A 1 301 ? 31.596  -10.395 30.250 1.00 69.66  ? 301 ILE A CG1 1 
ATOM   2386 C  CG2 . ILE A 1 301 ? 34.070  -9.878  30.113 1.00 71.11  ? 301 ILE A CG2 1 
ATOM   2387 C  CD1 . ILE A 1 301 ? 31.378  -9.439  31.399 1.00 78.13  ? 301 ILE A CD1 1 
ATOM   2388 N  N   . ARG A 1 302 ? 35.119  -12.254 27.630 1.00 69.13  ? 302 ARG A N   1 
ATOM   2389 C  CA  . ARG A 1 302 ? 36.550  -12.528 27.354 1.00 70.11  ? 302 ARG A CA  1 
ATOM   2390 C  C   . ARG A 1 302 ? 37.272  -11.187 27.512 1.00 68.68  ? 302 ARG A C   1 
ATOM   2391 O  O   . ARG A 1 302 ? 36.848  -10.196 26.913 1.00 73.10  ? 302 ARG A O   1 
ATOM   2392 C  CB  . ARG A 1 302 ? 36.684  -13.245 26.005 1.00 70.08  ? 302 ARG A CB  1 
ATOM   2393 C  CG  . ARG A 1 302 ? 38.005  -13.010 25.286 1.00 80.58  ? 302 ARG A CG  1 
ATOM   2394 C  CD  . ARG A 1 302 ? 38.574  -14.170 24.466 1.00 82.90  ? 302 ARG A CD  1 
ATOM   2395 N  NE  . ARG A 1 302 ? 38.259  -14.289 23.036 1.00 82.52  ? 302 ARG A NE  1 
ATOM   2396 C  CZ  . ARG A 1 302 ? 38.606  -13.424 22.069 1.00 100.32 ? 302 ARG A CZ  1 
ATOM   2397 N  NH1 . ARG A 1 302 ? 39.243  -12.288 22.346 1.00 98.86  ? 302 ARG A NH1 1 
ATOM   2398 N  NH2 . ARG A 1 302 ? 38.283  -13.705 20.812 1.00 91.39  ? 302 ARG A NH2 1 
ATOM   2399 N  N   . TRP A 1 303 ? 38.274  -11.149 28.376 1.00 69.94  ? 303 TRP A N   1 
ATOM   2400 C  CA  . TRP A 1 303 ? 39.136  -9.967  28.606 1.00 64.54  ? 303 TRP A CA  1 
ATOM   2401 C  C   . TRP A 1 303 ? 40.565  -10.481 28.695 1.00 74.34  ? 303 TRP A C   1 
ATOM   2402 O  O   . TRP A 1 303 ? 41.107  -10.685 29.784 1.00 71.87  ? 303 TRP A O   1 
ATOM   2403 C  CB  . TRP A 1 303 ? 38.696  -9.229  29.861 1.00 62.20  ? 303 TRP A CB  1 
ATOM   2404 C  CG  . TRP A 1 303 ? 39.405  -7.933  30.094 1.00 69.27  ? 303 TRP A CG  1 
ATOM   2405 C  CD1 . TRP A 1 303 ? 40.404  -7.360  29.354 1.00 70.78  ? 303 TRP A CD1 1 
ATOM   2406 C  CD2 . TRP A 1 303 ? 39.178  -7.051  31.203 1.00 65.91  ? 303 TRP A CD2 1 
ATOM   2407 N  NE1 . TRP A 1 303 ? 40.812  -6.183  29.933 1.00 69.70  ? 303 TRP A NE1 1 
ATOM   2408 C  CE2 . TRP A 1 303 ? 40.060  -5.963  31.059 1.00 67.74  ? 303 TRP A CE2 1 
ATOM   2409 C  CE3 . TRP A 1 303 ? 38.338  -7.104  32.318 1.00 65.36  ? 303 TRP A CE3 1 
ATOM   2410 C  CZ2 . TRP A 1 303 ? 40.107  -4.931  31.992 1.00 70.56  ? 303 TRP A CZ2 1 
ATOM   2411 C  CZ3 . TRP A 1 303 ? 38.375  -6.077  33.231 1.00 67.58  ? 303 TRP A CZ3 1 
ATOM   2412 C  CH2 . TRP A 1 303 ? 39.243  -5.001  33.063 1.00 67.38  ? 303 TRP A CH2 1 
ATOM   2413 N  N   . PRO A 1 304 ? 41.169  -10.793 27.526 1.00 77.70  ? 304 PRO A N   1 
ATOM   2414 C  CA  . PRO A 1 304 ? 42.439  -11.510 27.474 1.00 69.69  ? 304 PRO A CA  1 
ATOM   2415 C  C   . PRO A 1 304 ? 43.489  -10.831 28.350 1.00 73.04  ? 304 PRO A C   1 
ATOM   2416 O  O   . PRO A 1 304 ? 43.714  -9.640  28.177 1.00 74.36  ? 304 PRO A O   1 
ATOM   2417 C  CB  . PRO A 1 304 ? 42.803  -11.470 25.992 1.00 76.79  ? 304 PRO A CB  1 
ATOM   2418 C  CG  . PRO A 1 304 ? 41.454  -11.464 25.313 1.00 90.15  ? 304 PRO A CG  1 
ATOM   2419 C  CD  . PRO A 1 304 ? 40.616  -10.544 26.183 1.00 88.37  ? 304 PRO A CD  1 
ATOM   2420 N  N   . GLY A 1 305 ? 44.041  -11.607 29.284 1.00 71.13  ? 305 GLY A N   1 
ATOM   2421 C  CA  . GLY A 1 305 ? 45.141  -11.192 30.167 1.00 71.40  ? 305 GLY A CA  1 
ATOM   2422 C  C   . GLY A 1 305 ? 44.635  -10.591 31.464 1.00 77.76  ? 305 GLY A C   1 
ATOM   2423 O  O   . GLY A 1 305 ? 45.469  -10.163 32.254 1.00 89.77  ? 305 GLY A O   1 
ATOM   2424 N  N   . VAL A 1 306 ? 43.324  -10.527 31.690 1.00 82.54  ? 306 VAL A N   1 
ATOM   2425 C  CA  . VAL A 1 306 ? 42.769  -10.029 32.982 1.00 78.90  ? 306 VAL A CA  1 
ATOM   2426 C  C   . VAL A 1 306 ? 41.832  -11.093 33.546 1.00 79.14  ? 306 VAL A C   1 
ATOM   2427 O  O   . VAL A 1 306 ? 41.887  -11.379 34.749 1.00 94.94  ? 306 VAL A O   1 
ATOM   2428 C  CB  . VAL A 1 306 ? 42.049  -8.685  32.799 1.00 74.63  ? 306 VAL A CB  1 
ATOM   2429 C  CG1 . VAL A 1 306 ? 41.471  -8.185  34.111 1.00 83.11  ? 306 VAL A CG1 1 
ATOM   2430 C  CG2 . VAL A 1 306 ? 42.966  -7.642  32.197 1.00 72.29  ? 306 VAL A CG2 1 
ATOM   2431 N  N   . VAL A 1 307 ? 40.977  -11.631 32.697 1.00 77.18  ? 307 VAL A N   1 
ATOM   2432 C  CA  . VAL A 1 307 ? 40.025  -12.688 33.094 1.00 78.54  ? 307 VAL A CA  1 
ATOM   2433 C  C   . VAL A 1 307 ? 40.745  -13.997 32.854 1.00 85.39  ? 307 VAL A C   1 
ATOM   2434 O  O   . VAL A 1 307 ? 41.003  -14.294 31.666 1.00 89.42  ? 307 VAL A O   1 
ATOM   2435 C  CB  . VAL A 1 307 ? 38.741  -12.567 32.268 1.00 82.50  ? 307 VAL A CB  1 
ATOM   2436 C  CG1 . VAL A 1 307 ? 37.960  -13.862 32.186 1.00 87.65  ? 307 VAL A CG1 1 
ATOM   2437 C  CG2 . VAL A 1 307 ? 37.888  -11.443 32.816 1.00 77.63  ? 307 VAL A CG2 1 
ATOM   2438 N  N   . LYS A 1 308 ? 41.094  -14.690 33.943 1.00 87.29  ? 308 LYS A N   1 
ATOM   2439 C  CA  . LYS A 1 308 ? 41.560  -16.102 33.923 1.00 81.31  ? 308 LYS A CA  1 
ATOM   2440 C  C   . LYS A 1 308 ? 40.515  -16.934 33.198 1.00 75.77  ? 308 LYS A C   1 
ATOM   2441 O  O   . LYS A 1 308 ? 39.348  -16.971 33.584 1.00 67.32  ? 308 LYS A O   1 
ATOM   2442 C  CB  . LYS A 1 308 ? 41.744  -16.649 35.334 1.00 95.75  ? 308 LYS A CB  1 
ATOM   2443 C  CG  . LYS A 1 308 ? 42.204  -18.100 35.455 1.00 109.45 ? 308 LYS A CG  1 
ATOM   2444 C  CD  . LYS A 1 308 ? 42.851  -18.356 36.827 1.00 123.20 ? 308 LYS A CD  1 
ATOM   2445 C  CE  . LYS A 1 308 ? 43.479  -19.719 37.011 1.00 113.71 ? 308 LYS A CE  1 
ATOM   2446 N  NZ  . LYS A 1 308 ? 42.421  -20.744 37.087 1.00 123.52 ? 308 LYS A NZ  1 
ATOM   2447 N  N   . PRO A 1 309 ? 40.893  -17.571 32.075 1.00 77.44  ? 309 PRO A N   1 
ATOM   2448 C  CA  . PRO A 1 309 ? 39.936  -18.304 31.256 1.00 74.09  ? 309 PRO A CA  1 
ATOM   2449 C  C   . PRO A 1 309 ? 39.355  -19.519 31.978 1.00 74.24  ? 309 PRO A C   1 
ATOM   2450 O  O   . PRO A 1 309 ? 40.039  -20.107 32.786 1.00 74.32  ? 309 PRO A O   1 
ATOM   2451 C  CB  . PRO A 1 309 ? 40.745  -18.768 30.036 1.00 75.91  ? 309 PRO A CB  1 
ATOM   2452 C  CG  . PRO A 1 309 ? 41.960  -17.858 30.012 1.00 81.52  ? 309 PRO A CG  1 
ATOM   2453 C  CD  . PRO A 1 309 ? 42.233  -17.535 31.470 1.00 83.01  ? 309 PRO A CD  1 
ATOM   2454 N  N   . GLY A 1 310 ? 38.108  -19.843 31.640 1.00 83.36  ? 310 GLY A N   1 
ATOM   2455 C  CA  . GLY A 1 310 ? 37.394  -21.052 32.082 1.00 77.63  ? 310 GLY A CA  1 
ATOM   2456 C  C   . GLY A 1 310 ? 36.671  -20.818 33.384 1.00 78.92  ? 310 GLY A C   1 
ATOM   2457 O  O   . GLY A 1 310 ? 35.939  -21.735 33.774 1.00 97.67  ? 310 GLY A O   1 
ATOM   2458 N  N   . THR A 1 311 ? 36.835  -19.639 34.008 1.00 76.75  ? 311 THR A N   1 
ATOM   2459 C  CA  . THR A 1 311 ? 36.223  -19.287 35.322 1.00 76.68  ? 311 THR A CA  1 
ATOM   2460 C  C   . THR A 1 311 ? 34.720  -19.064 35.166 1.00 77.48  ? 311 THR A C   1 
ATOM   2461 O  O   . THR A 1 311 ? 34.255  -18.907 33.988 1.00 73.07  ? 311 THR A O   1 
ATOM   2462 C  CB  . THR A 1 311 ? 36.857  -18.037 35.920 1.00 74.99  ? 311 THR A CB  1 
ATOM   2463 O  OG1 . THR A 1 311 ? 36.734  -17.025 34.932 1.00 67.04  ? 311 THR A OG1 1 
ATOM   2464 C  CG2 . THR A 1 311 ? 38.313  -18.248 36.247 1.00 87.02  ? 311 THR A CG2 1 
ATOM   2465 N  N   . THR A 1 312 ? 33.978  -19.126 36.281 1.00 71.96  ? 312 THR A N   1 
ATOM   2466 C  CA  . THR A 1 312 ? 32.520  -18.811 36.298 1.00 79.19  ? 312 THR A CA  1 
ATOM   2467 C  C   . THR A 1 312 ? 32.246  -17.853 37.465 1.00 76.44  ? 312 THR A C   1 
ATOM   2468 O  O   . THR A 1 312 ? 33.188  -17.620 38.235 1.00 81.90  ? 312 THR A O   1 
ATOM   2469 C  CB  . THR A 1 312 ? 31.619  -20.060 36.278 1.00 76.87  ? 312 THR A CB  1 
ATOM   2470 O  OG1 . THR A 1 312 ? 31.566  -20.459 37.640 1.00 76.96  ? 312 THR A OG1 1 
ATOM   2471 C  CG2 . THR A 1 312 ? 32.076  -21.197 35.377 1.00 78.47  ? 312 THR A CG2 1 
ATOM   2472 N  N   . CYS A 1 313 ? 31.056  -17.234 37.504 1.00 71.70  ? 313 CYS A N   1 
ATOM   2473 C  CA  . CYS A 1 313 ? 30.662  -16.230 38.516 1.00 70.65  ? 313 CYS A CA  1 
ATOM   2474 C  C   . CYS A 1 313 ? 29.163  -16.363 38.801 1.00 78.43  ? 313 CYS A C   1 
ATOM   2475 O  O   . CYS A 1 313 ? 28.285  -16.174 37.884 1.00 71.06  ? 313 CYS A O   1 
ATOM   2476 C  CB  . CYS A 1 313 ? 31.042  -14.806 38.114 1.00 73.28  ? 313 CYS A CB  1 
ATOM   2477 S  SG  . CYS A 1 313 ? 30.783  -13.574 39.430 1.00 73.39  ? 313 CYS A SG  1 
ATOM   2478 N  N   . ASP A 1 314 ? 28.908  -16.629 40.078 1.00 88.47  ? 314 ASP A N   1 
ATOM   2479 C  CA  . ASP A 1 314 ? 27.574  -16.892 40.662 1.00 87.69  ? 314 ASP A CA  1 
ATOM   2480 C  C   . ASP A 1 314 ? 26.919  -15.584 41.101 1.00 85.07  ? 314 ASP A C   1 
ATOM   2481 O  O   . ASP A 1 314 ? 25.701  -15.634 41.382 1.00 78.26  ? 314 ASP A O   1 
ATOM   2482 C  CB  . ASP A 1 314 ? 27.701  -17.863 41.834 1.00 96.42  ? 314 ASP A CB  1 
ATOM   2483 C  CG  . ASP A 1 314 ? 28.180  -19.232 41.381 1.00 107.98 ? 314 ASP A CG  1 
ATOM   2484 O  OD1 . ASP A 1 314 ? 27.803  -19.671 40.253 1.00 94.73  ? 314 ASP A OD1 1 
ATOM   2485 O  OD2 . ASP A 1 314 ? 28.954  -19.833 42.135 1.00 143.13 ? 314 ASP A OD2 1 
ATOM   2486 N  N   . VAL A 1 315 ? 27.665  -14.470 41.146 1.00 77.85  ? 315 VAL A N   1 
ATOM   2487 C  CA  . VAL A 1 315 ? 27.131  -13.154 41.606 1.00 65.29  ? 315 VAL A CA  1 
ATOM   2488 C  C   . VAL A 1 315 ? 26.154  -12.640 40.556 1.00 73.27  ? 315 VAL A C   1 
ATOM   2489 O  O   . VAL A 1 315 ? 26.453  -12.747 39.345 1.00 65.78  ? 315 VAL A O   1 
ATOM   2490 C  CB  . VAL A 1 315 ? 28.233  -12.120 41.851 1.00 66.05  ? 315 VAL A CB  1 
ATOM   2491 C  CG1 . VAL A 1 315 ? 27.630  -10.772 42.171 1.00 72.72  ? 315 VAL A CG1 1 
ATOM   2492 C  CG2 . VAL A 1 315 ? 29.185  -12.523 42.951 1.00 68.86  ? 315 VAL A CG2 1 
ATOM   2493 N  N   . PRO A 1 316 ? 24.960  -12.131 40.997 1.00 73.66  ? 316 PRO A N   1 
ATOM   2494 C  CA  . PRO A 1 316 ? 23.958  -11.605 40.074 1.00 70.43  ? 316 PRO A CA  1 
ATOM   2495 C  C   . PRO A 1 316 ? 24.462  -10.301 39.415 1.00 72.63  ? 316 PRO A C   1 
ATOM   2496 O  O   . PRO A 1 316 ? 24.943  -9.408  40.108 1.00 66.30  ? 316 PRO A O   1 
ATOM   2497 C  CB  . PRO A 1 316 ? 22.694  -11.487 40.944 1.00 65.53  ? 316 PRO A CB  1 
ATOM   2498 C  CG  . PRO A 1 316 ? 23.205  -11.252 42.344 1.00 68.74  ? 316 PRO A CG  1 
ATOM   2499 C  CD  . PRO A 1 316 ? 24.469  -12.086 42.389 1.00 72.35  ? 316 PRO A CD  1 
ATOM   2500 N  N   . ALA A 1 317 ? 24.391  -10.289 38.081 1.00 69.77  ? 317 ALA A N   1 
ATOM   2501 C  CA  . ALA A 1 317 ? 24.719  -9.193  37.150 1.00 64.14  ? 317 ALA A CA  1 
ATOM   2502 C  C   . ALA A 1 317 ? 23.489  -8.861  36.305 1.00 65.95  ? 317 ALA A C   1 
ATOM   2503 O  O   . ALA A 1 317 ? 22.676  -9.762  36.003 1.00 65.27  ? 317 ALA A O   1 
ATOM   2504 C  CB  . ALA A 1 317 ? 25.836  -9.607  36.237 1.00 65.64  ? 317 ALA A CB  1 
ATOM   2505 N  N   . CYS A 1 318 ? 23.429  -7.620  35.842 1.00 64.50  ? 318 CYS A N   1 
ATOM   2506 C  CA  . CYS A 1 318 ? 22.308  -7.072  35.053 1.00 65.46  ? 318 CYS A CA  1 
ATOM   2507 C  C   . CYS A 1 318 ? 22.844  -6.241  33.881 1.00 66.18  ? 318 CYS A C   1 
ATOM   2508 O  O   . CYS A 1 318 ? 23.996  -5.785  33.930 1.00 69.97  ? 318 CYS A O   1 
ATOM   2509 C  CB  . CYS A 1 318 ? 21.430  -6.249  35.983 1.00 73.40  ? 318 CYS A CB  1 
ATOM   2510 S  SG  . CYS A 1 318 ? 19.784  -5.847  35.332 1.00 82.47  ? 318 CYS A SG  1 
ATOM   2511 N  N   . SER A 1 319 ? 22.006  -6.036  32.874 1.00 68.02  ? 319 SER A N   1 
ATOM   2512 C  CA  . SER A 1 319 ? 22.254  -5.149  31.714 1.00 67.40  ? 319 SER A CA  1 
ATOM   2513 C  C   . SER A 1 319 ? 22.768  -3.781  32.181 1.00 67.35  ? 319 SER A C   1 
ATOM   2514 O  O   . SER A 1 319 ? 23.653  -3.154  31.508 1.00 79.50  ? 319 SER A O   1 
ATOM   2515 C  CB  . SER A 1 319 ? 20.996  -4.991  30.913 1.00 75.69  ? 319 SER A CB  1 
ATOM   2516 O  OG  . SER A 1 319 ? 20.075  -6.037  31.173 1.00 79.88  ? 319 SER A OG  1 
ATOM   2517 N  N   . VAL A 1 320 ? 22.254  -3.279  33.291 1.00 59.57  ? 320 VAL A N   1 
ATOM   2518 C  CA  . VAL A 1 320 ? 22.689  -1.929  33.754 1.00 69.00  ? 320 VAL A CA  1 
ATOM   2519 C  C   . VAL A 1 320 ? 24.189  -1.867  34.070 1.00 64.47  ? 320 VAL A C   1 
ATOM   2520 O  O   . VAL A 1 320 ? 24.723  -0.764  34.174 1.00 69.65  ? 320 VAL A O   1 
ATOM   2521 C  CB  . VAL A 1 320 ? 21.880  -1.486  34.971 1.00 67.10  ? 320 VAL A CB  1 
ATOM   2522 C  CG1 . VAL A 1 320 ? 20.441  -1.267  34.583 1.00 69.13  ? 320 VAL A CG1 1 
ATOM   2523 C  CG2 . VAL A 1 320 ? 22.008  -2.477  36.103 1.00 73.11  ? 320 VAL A CG2 1 
ATOM   2524 N  N   . ASP A 1 321 ? 24.832  -2.995  34.299 1.00 66.77  ? 321 ASP A N   1 
ATOM   2525 C  CA  . ASP A 1 321 ? 26.234  -3.031  34.779 1.00 68.50  ? 321 ASP A CA  1 
ATOM   2526 C  C   . ASP A 1 321 ? 27.232  -2.831  33.631 1.00 71.18  ? 321 ASP A C   1 
ATOM   2527 O  O   . ASP A 1 321 ? 28.430  -2.604  33.938 1.00 63.18  ? 321 ASP A O   1 
ATOM   2528 C  CB  . ASP A 1 321 ? 26.511  -4.364  35.466 1.00 74.13  ? 321 ASP A CB  1 
ATOM   2529 C  CG  . ASP A 1 321 ? 25.640  -4.593  36.680 1.00 67.83  ? 321 ASP A CG  1 
ATOM   2530 O  OD1 . ASP A 1 321 ? 25.506  -3.643  37.494 1.00 61.46  ? 321 ASP A OD1 1 
ATOM   2531 O  OD2 . ASP A 1 321 ? 25.120  -5.715  36.794 1.00 62.29  ? 321 ASP A OD2 1 
ATOM   2532 N  N   . PHE A 1 322 ? 26.813  -2.920  32.364 1.00 72.88  ? 322 PHE A N   1 
ATOM   2533 C  CA  . PHE A 1 322 ? 27.798  -2.929  31.262 1.00 66.52  ? 322 PHE A CA  1 
ATOM   2534 C  C   . PHE A 1 322 ? 28.312  -1.523  31.088 1.00 68.49  ? 322 PHE A C   1 
ATOM   2535 O  O   . PHE A 1 322 ? 29.540  -1.385  30.865 1.00 68.10  ? 322 PHE A O   1 
ATOM   2536 C  CB  . PHE A 1 322 ? 27.228  -3.456  29.956 1.00 70.32  ? 322 PHE A CB  1 
ATOM   2537 C  CG  . PHE A 1 322 ? 26.750  -4.872  30.071 1.00 69.18  ? 322 PHE A CG  1 
ATOM   2538 C  CD1 . PHE A 1 322 ? 27.458  -5.796  30.815 1.00 77.32  ? 322 PHE A CD1 1 
ATOM   2539 C  CD2 . PHE A 1 322 ? 25.584  -5.274  29.456 1.00 73.24  ? 322 PHE A CD2 1 
ATOM   2540 C  CE1 . PHE A 1 322 ? 26.998  -7.095  30.944 1.00 81.27  ? 322 PHE A CE1 1 
ATOM   2541 C  CE2 . PHE A 1 322 ? 25.126  -6.574  29.588 1.00 82.49  ? 322 PHE A CE2 1 
ATOM   2542 C  CZ  . PHE A 1 322 ? 25.835  -7.484  30.324 1.00 77.95  ? 322 PHE A CZ  1 
ATOM   2543 N  N   . PHE A 1 323 ? 27.425  -0.530  31.193 1.00 67.37  ? 323 PHE A N   1 
ATOM   2544 C  CA  . PHE A 1 323 ? 27.879  0.874   30.994 1.00 70.64  ? 323 PHE A CA  1 
ATOM   2545 C  C   . PHE A 1 323 ? 29.077  1.115   31.912 1.00 61.05  ? 323 PHE A C   1 
ATOM   2546 O  O   . PHE A 1 323 ? 30.186  1.340   31.425 1.00 58.66  ? 323 PHE A O   1 
ATOM   2547 C  CB  . PHE A 1 323 ? 26.732  1.879   31.136 1.00 77.89  ? 323 PHE A CB  1 
ATOM   2548 C  CG  . PHE A 1 323 ? 27.050  3.335   30.873 1.00 68.60  ? 323 PHE A CG  1 
ATOM   2549 C  CD1 . PHE A 1 323 ? 27.880  4.057   31.716 1.00 59.92  ? 323 PHE A CD1 1 
ATOM   2550 C  CD2 . PHE A 1 323 ? 26.447  3.997   29.814 1.00 67.62  ? 323 PHE A CD2 1 
ATOM   2551 C  CE1 . PHE A 1 323 ? 28.121  5.398   31.479 1.00 63.19  ? 323 PHE A CE1 1 
ATOM   2552 C  CE2 . PHE A 1 323 ? 26.685  5.341   29.582 1.00 70.74  ? 323 PHE A CE2 1 
ATOM   2553 C  CZ  . PHE A 1 323 ? 27.520  6.042   30.417 1.00 68.46  ? 323 PHE A CZ  1 
ATOM   2554 N  N   . PRO A 1 324 ? 28.919  1.058   33.253 1.00 59.20  ? 324 PRO A N   1 
ATOM   2555 C  CA  . PRO A 1 324 ? 29.980  1.487   34.155 1.00 64.55  ? 324 PRO A CA  1 
ATOM   2556 C  C   . PRO A 1 324 ? 31.157  0.517   34.103 1.00 60.56  ? 324 PRO A C   1 
ATOM   2557 O  O   . PRO A 1 324 ? 32.276  0.951   34.347 1.00 58.40  ? 324 PRO A O   1 
ATOM   2558 C  CB  . PRO A 1 324 ? 29.337  1.514   35.539 1.00 63.32  ? 324 PRO A CB  1 
ATOM   2559 C  CG  . PRO A 1 324 ? 28.198  0.544   35.419 1.00 66.35  ? 324 PRO A CG  1 
ATOM   2560 C  CD  . PRO A 1 324 ? 27.715  0.673   33.996 1.00 67.36  ? 324 PRO A CD  1 
ATOM   2561 N  N   . THR A 1 325 ? 30.884  -0.743  33.776 1.00 56.69  ? 325 THR A N   1 
ATOM   2562 C  CA  . THR A 1 325 ? 31.967  -1.738  33.625 1.00 63.50  ? 325 THR A CA  1 
ATOM   2563 C  C   . THR A 1 325 ? 32.887  -1.220  32.518 1.00 62.65  ? 325 THR A C   1 
ATOM   2564 O  O   . THR A 1 325 ? 34.083  -1.016  32.772 1.00 70.25  ? 325 THR A O   1 
ATOM   2565 C  CB  . THR A 1 325 ? 31.427  -3.148  33.375 1.00 66.38  ? 325 THR A CB  1 
ATOM   2566 O  OG1 . THR A 1 325 ? 30.995  -3.657  34.637 1.00 71.82  ? 325 THR A OG1 1 
ATOM   2567 C  CG2 . THR A 1 325 ? 32.471  -4.062  32.776 1.00 68.47  ? 325 THR A CG2 1 
ATOM   2568 N  N   . ILE A 1 326 ? 32.327  -0.977  31.343 1.00 57.53  ? 326 ILE A N   1 
ATOM   2569 C  CA  . ILE A 1 326 ? 33.127  -0.512  30.188 1.00 56.33  ? 326 ILE A CA  1 
ATOM   2570 C  C   . ILE A 1 326 ? 33.795  0.811   30.560 1.00 58.32  ? 326 ILE A C   1 
ATOM   2571 O  O   . ILE A 1 326 ? 34.972  1.008   30.183 1.00 60.45  ? 326 ILE A O   1 
ATOM   2572 C  CB  . ILE A 1 326 ? 32.264  -0.382  28.932 1.00 54.24  ? 326 ILE A CB  1 
ATOM   2573 C  CG1 . ILE A 1 326 ? 31.829  -1.751  28.421 1.00 58.07  ? 326 ILE A CG1 1 
ATOM   2574 C  CG2 . ILE A 1 326 ? 33.034  0.373   27.869 1.00 54.45  ? 326 ILE A CG2 1 
ATOM   2575 C  CD1 . ILE A 1 326 ? 31.069  -1.698  27.124 1.00 59.86  ? 326 ILE A CD1 1 
ATOM   2576 N  N   . GLU A 1 327 ? 33.050  1.724   31.164 1.00 59.46  ? 327 GLU A N   1 
ATOM   2577 C  CA  . GLU A 1 327 ? 33.596  3.055   31.505 1.00 69.36  ? 327 GLU A CA  1 
ATOM   2578 C  C   . GLU A 1 327 ? 34.897  2.844   32.258 1.00 64.71  ? 327 GLU A C   1 
ATOM   2579 O  O   . GLU A 1 327 ? 35.909  3.445   31.879 1.00 62.49  ? 327 GLU A O   1 
ATOM   2580 C  CB  . GLU A 1 327 ? 32.576  3.738   32.404 1.00 71.99  ? 327 GLU A CB  1 
ATOM   2581 C  CG  . GLU A 1 327 ? 32.674  5.241   32.478 1.00 87.99  ? 327 GLU A CG  1 
ATOM   2582 C  CD  . GLU A 1 327 ? 31.649  5.764   33.464 1.00 94.25  ? 327 GLU A CD  1 
ATOM   2583 O  OE1 . GLU A 1 327 ? 31.900  5.664   34.675 1.00 88.08  ? 327 GLU A OE1 1 
ATOM   2584 O  OE2 . GLU A 1 327 ? 30.592  6.236   33.018 1.00 113.01 ? 327 GLU A OE2 1 
ATOM   2585 N  N   . GLU A 1 328 ? 34.854  1.999   33.277 1.00 71.35  ? 328 GLU A N   1 
ATOM   2586 C  CA  . GLU A 1 328 ? 36.035  1.730   34.129 1.00 74.54  ? 328 GLU A CA  1 
ATOM   2587 C  C   . GLU A 1 328 ? 37.100  0.959   33.343 1.00 62.82  ? 328 GLU A C   1 
ATOM   2588 O  O   . GLU A 1 328 ? 38.258  1.262   33.484 1.00 62.28  ? 328 GLU A O   1 
ATOM   2589 C  CB  . GLU A 1 328 ? 35.677  0.961   35.384 1.00 84.18  ? 328 GLU A CB  1 
ATOM   2590 C  CG  . GLU A 1 328 ? 36.749  1.149   36.419 1.00 98.59  ? 328 GLU A CG  1 
ATOM   2591 C  CD  . GLU A 1 328 ? 36.527  0.351   37.675 1.00 105.88 ? 328 GLU A CD  1 
ATOM   2592 O  OE1 . GLU A 1 328 ? 35.351  0.284   38.127 1.00 86.91  ? 328 GLU A OE1 1 
ATOM   2593 O  OE2 . GLU A 1 328 ? 37.540  -0.189  38.183 1.00 121.67 ? 328 GLU A OE2 1 
ATOM   2594 N  N   . MET A 1 329 ? 36.728  -0.009  32.529 1.00 64.02  ? 329 MET A N   1 
ATOM   2595 C  CA  . MET A 1 329 ? 37.695  -0.763  31.688 1.00 60.02  ? 329 MET A CA  1 
ATOM   2596 C  C   . MET A 1 329 ? 38.477  0.192   30.789 1.00 59.18  ? 329 MET A C   1 
ATOM   2597 O  O   . MET A 1 329 ? 39.540  -0.204  30.369 1.00 66.03  ? 329 MET A O   1 
ATOM   2598 C  CB  . MET A 1 329 ? 36.966  -1.746  30.769 1.00 64.75  ? 329 MET A CB  1 
ATOM   2599 C  CG  . MET A 1 329 ? 36.313  -2.949  31.458 1.00 63.27  ? 329 MET A CG  1 
ATOM   2600 S  SD  . MET A 1 329 ? 35.598  -4.024  30.192 1.00 81.33  ? 329 MET A SD  1 
ATOM   2601 C  CE  . MET A 1 329 ? 35.327  -5.576  31.026 1.00 90.38  ? 329 MET A CE  1 
ATOM   2602 N  N   . ALA A 1 330 ? 37.919  1.353   30.437 1.00 62.42  ? 330 ALA A N   1 
ATOM   2603 C  CA  . ALA A 1 330 ? 38.493  2.331   29.479 1.00 63.44  ? 330 ALA A CA  1 
ATOM   2604 C  C   . ALA A 1 330 ? 39.179  3.490   30.205 1.00 62.88  ? 330 ALA A C   1 
ATOM   2605 O  O   . ALA A 1 330 ? 39.549  4.460   29.534 1.00 66.21  ? 330 ALA A O   1 
ATOM   2606 C  CB  . ALA A 1 330 ? 37.390  2.870   28.611 1.00 72.07  ? 330 ALA A CB  1 
ATOM   2607 N  N   . GLY A 1 331 ? 39.289  3.416   31.533 1.00 70.51  ? 331 GLY A N   1 
ATOM   2608 C  CA  . GLY A 1 331 ? 39.968  4.407   32.399 1.00 67.93  ? 331 GLY A CA  1 
ATOM   2609 C  C   . GLY A 1 331 ? 39.179  5.688   32.482 1.00 67.40  ? 331 GLY A C   1 
ATOM   2610 O  O   . GLY A 1 331 ? 39.730  6.730   32.200 1.00 88.32  ? 331 GLY A O   1 
ATOM   2611 N  N   . LEU A 1 332 ? 37.902  5.600   32.813 1.00 72.73  ? 332 LEU A N   1 
ATOM   2612 C  CA  . LEU A 1 332 ? 37.025  6.781   32.946 1.00 77.77  ? 332 LEU A CA  1 
ATOM   2613 C  C   . LEU A 1 332 ? 36.484  6.908   34.367 1.00 84.54  ? 332 LEU A C   1 
ATOM   2614 O  O   . LEU A 1 332 ? 36.059  5.877   34.983 1.00 92.20  ? 332 LEU A O   1 
ATOM   2615 C  CB  . LEU A 1 332 ? 35.903  6.662   31.923 1.00 82.32  ? 332 LEU A CB  1 
ATOM   2616 C  CG  . LEU A 1 332 ? 36.304  7.123   30.532 1.00 82.09  ? 332 LEU A CG  1 
ATOM   2617 C  CD1 . LEU A 1 332 ? 35.080  7.247   29.621 1.00 83.27  ? 332 LEU A CD1 1 
ATOM   2618 C  CD2 . LEU A 1 332 ? 37.052  8.442   30.656 1.00 88.06  ? 332 LEU A CD2 1 
ATOM   2619 N  N   . ARG A 1 333 ? 36.511  8.143   34.858 1.00 80.11  ? 333 ARG A N   1 
ATOM   2620 C  CA  . ARG A 1 333 ? 35.942  8.477   36.175 1.00 101.99 ? 333 ARG A CA  1 
ATOM   2621 C  C   . ARG A 1 333 ? 34.422  8.463   36.042 1.00 98.53  ? 333 ARG A C   1 
ATOM   2622 O  O   . ARG A 1 333 ? 33.916  9.071   35.100 1.00 96.74  ? 333 ARG A O   1 
ATOM   2623 C  CB  . ARG A 1 333 ? 36.509  9.814   36.654 1.00 118.75 ? 333 ARG A CB  1 
ATOM   2624 C  CG  . ARG A 1 333 ? 37.880  9.671   37.296 1.00 128.28 ? 333 ARG A CG  1 
ATOM   2625 C  CD  . ARG A 1 333 ? 38.110  10.669  38.409 1.00 137.62 ? 333 ARG A CD  1 
ATOM   2626 N  NE  . ARG A 1 333 ? 39.540  10.871  38.568 1.00 153.48 ? 333 ARG A NE  1 
ATOM   2627 C  CZ  . ARG A 1 333 ? 40.098  11.859  39.258 1.00 154.82 ? 333 ARG A CZ  1 
ATOM   2628 N  NH1 . ARG A 1 333 ? 39.335  12.742  39.876 1.00 161.08 ? 333 ARG A NH1 1 
ATOM   2629 N  NH2 . ARG A 1 333 ? 41.416  11.960  39.328 1.00 144.44 ? 333 ARG A NH2 1 
ATOM   2630 N  N   . HIS A 1 334 ? 33.740  7.763   36.953 1.00 106.10 ? 334 HIS A N   1 
ATOM   2631 C  CA  . HIS A 1 334 ? 32.254  7.712   36.927 1.00 119.45 ? 334 HIS A CA  1 
ATOM   2632 C  C   . HIS A 1 334 ? 31.718  9.133   37.113 1.00 110.99 ? 334 HIS A C   1 
ATOM   2633 O  O   . HIS A 1 334 ? 32.036  9.752   38.147 1.00 94.71  ? 334 HIS A O   1 
ATOM   2634 C  CB  . HIS A 1 334 ? 31.744  6.685   37.946 1.00 123.37 ? 334 HIS A CB  1 
ATOM   2635 C  CG  . HIS A 1 334 ? 32.146  5.291   37.595 1.00 148.98 ? 334 HIS A CG  1 
ATOM   2636 N  ND1 . HIS A 1 334 ? 31.224  4.305   37.300 1.00 134.64 ? 334 HIS A ND1 1 
ATOM   2637 C  CD2 . HIS A 1 334 ? 33.364  4.722   37.458 1.00 149.74 ? 334 HIS A CD2 1 
ATOM   2638 C  CE1 . HIS A 1 334 ? 31.857  3.185   37.013 1.00 112.55 ? 334 HIS A CE1 1 
ATOM   2639 N  NE2 . HIS A 1 334 ? 33.171  3.415   37.102 1.00 116.55 ? 334 HIS A NE2 1 
ATOM   2640 N  N   . ASP A 1 335 ? 30.943  9.627   36.146 1.00 111.47 ? 335 ASP A N   1 
ATOM   2641 C  CA  . ASP A 1 335 ? 30.475  11.026  36.191 1.00 109.34 ? 335 ASP A CA  1 
ATOM   2642 C  C   . ASP A 1 335 ? 29.389  11.091  37.259 1.00 122.08 ? 335 ASP A C   1 
ATOM   2643 O  O   . ASP A 1 335 ? 28.413  10.344  37.159 1.00 127.28 ? 335 ASP A O   1 
ATOM   2644 C  CB  . ASP A 1 335 ? 29.998  11.468  34.818 1.00 105.64 ? 335 ASP A CB  1 
ATOM   2645 C  CG  . ASP A 1 335 ? 29.564  12.909  34.860 1.00 113.62 ? 335 ASP A CG  1 
ATOM   2646 O  OD1 . ASP A 1 335 ? 29.625  13.518  35.975 1.00 112.41 ? 335 ASP A OD1 1 
ATOM   2647 O  OD2 . ASP A 1 335 ? 29.182  13.404  33.796 1.00 105.32 ? 335 ASP A OD2 1 
ATOM   2648 N  N   . PRO A 1 336 ? 29.511  11.931  38.322 1.00 123.07 ? 336 PRO A N   1 
ATOM   2649 C  CA  . PRO A 1 336 ? 28.552  11.869  39.429 1.00 113.48 ? 336 PRO A CA  1 
ATOM   2650 C  C   . PRO A 1 336 ? 27.204  12.467  38.989 1.00 115.43 ? 336 PRO A C   1 
ATOM   2651 O  O   . PRO A 1 336 ? 26.211  12.145  39.585 1.00 110.99 ? 336 PRO A O   1 
ATOM   2652 C  CB  . PRO A 1 336 ? 29.214  12.644  40.581 1.00 111.77 ? 336 PRO A CB  1 
ATOM   2653 C  CG  . PRO A 1 336 ? 30.582  13.103  40.038 1.00 115.36 ? 336 PRO A CG  1 
ATOM   2654 C  CD  . PRO A 1 336 ? 30.527  12.982  38.525 1.00 110.26 ? 336 PRO A CD  1 
ATOM   2655 N  N   . LYS A 1 337 ? 27.210  13.274  37.923 1.00 123.60 ? 337 LYS A N   1 
ATOM   2656 C  CA  . LYS A 1 337 ? 26.008  13.906  37.317 1.00 116.02 ? 337 LYS A CA  1 
ATOM   2657 C  C   . LYS A 1 337 ? 25.217  12.853  36.520 1.00 100.02 ? 337 LYS A C   1 
ATOM   2658 O  O   . LYS A 1 337 ? 24.109  13.158  36.148 1.00 91.25  ? 337 LYS A O   1 
ATOM   2659 C  CB  . LYS A 1 337 ? 26.416  15.090  36.420 1.00 126.24 ? 337 LYS A CB  1 
ATOM   2660 C  CG  . LYS A 1 337 ? 27.319  16.151  37.059 1.00 139.34 ? 337 LYS A CG  1 
ATOM   2661 C  CD  . LYS A 1 337 ? 28.681  16.405  36.365 1.00 141.65 ? 337 LYS A CD  1 
ATOM   2662 C  CE  . LYS A 1 337 ? 28.603  16.921  34.939 1.00 134.80 ? 337 LYS A CE  1 
ATOM   2663 N  NZ  . LYS A 1 337 ? 28.362  18.374  34.890 1.00 139.25 ? 337 LYS A NZ  1 
ATOM   2664 N  N   . LEU A 1 338 ? 25.734  11.651  36.252 1.00 94.57  ? 338 LEU A N   1 
ATOM   2665 C  CA  . LEU A 1 338 ? 25.026  10.684  35.362 1.00 91.49  ? 338 LEU A CA  1 
ATOM   2666 C  C   . LEU A 1 338 ? 23.919  9.929   36.108 1.00 99.79  ? 338 LEU A C   1 
ATOM   2667 O  O   . LEU A 1 338 ? 22.869  9.635   35.476 1.00 103.09 ? 338 LEU A O   1 
ATOM   2668 C  CB  . LEU A 1 338 ? 26.015  9.695   34.748 1.00 93.76  ? 338 LEU A CB  1 
ATOM   2669 C  CG  . LEU A 1 338 ? 26.487  10.060  33.338 1.00 102.05 ? 338 LEU A CG  1 
ATOM   2670 C  CD1 . LEU A 1 338 ? 27.672  9.200   32.914 1.00 122.40 ? 338 LEU A CD1 1 
ATOM   2671 C  CD2 . LEU A 1 338 ? 25.364  9.937   32.314 1.00 87.55  ? 338 LEU A CD2 1 
ATOM   2672 N  N   . ALA A 1 339 ? 24.142  9.620   37.389 1.00 95.05  ? 339 ALA A N   1 
ATOM   2673 C  CA  . ALA A 1 339 ? 23.133  8.892   38.195 1.00 92.59  ? 339 ALA A CA  1 
ATOM   2674 C  C   . ALA A 1 339 ? 22.717  7.608   37.469 1.00 79.62  ? 339 ALA A C   1 
ATOM   2675 O  O   . ALA A 1 339 ? 21.552  7.525   37.031 1.00 60.66  ? 339 ALA A O   1 
ATOM   2676 C  CB  . ALA A 1 339 ? 21.947  9.786   38.466 1.00 89.25  ? 339 ALA A CB  1 
ATOM   2677 N  N   . LEU A 1 340 ? 23.637  6.646   37.349 1.00 74.59  ? 340 LEU A N   1 
ATOM   2678 C  CA  . LEU A 1 340 ? 23.317  5.361   36.703 1.00 73.72  ? 340 LEU A CA  1 
ATOM   2679 C  C   . LEU A 1 340 ? 22.842  4.406   37.793 1.00 72.45  ? 340 LEU A C   1 
ATOM   2680 O  O   . LEU A 1 340 ? 22.980  4.744   38.984 1.00 70.19  ? 340 LEU A O   1 
ATOM   2681 C  CB  . LEU A 1 340 ? 24.571  4.830   36.003 1.00 69.98  ? 340 LEU A CB  1 
ATOM   2682 C  CG  . LEU A 1 340 ? 25.319  5.855   35.153 1.00 70.72  ? 340 LEU A CG  1 
ATOM   2683 C  CD1 . LEU A 1 340 ? 26.624  5.277   34.633 1.00 77.46  ? 340 LEU A CD1 1 
ATOM   2684 C  CD2 . LEU A 1 340 ? 24.451  6.342   34.003 1.00 80.67  ? 340 LEU A CD2 1 
ATOM   2685 N  N   . ASP A 1 341 ? 22.307  3.267   37.394 1.00 74.45  ? 341 ASP A N   1 
ATOM   2686 C  CA  . ASP A 1 341 ? 21.775  2.224   38.305 1.00 68.49  ? 341 ASP A CA  1 
ATOM   2687 C  C   . ASP A 1 341 ? 22.743  1.032   38.341 1.00 66.79  ? 341 ASP A C   1 
ATOM   2688 O  O   . ASP A 1 341 ? 22.681  0.291   39.293 1.00 77.01  ? 341 ASP A O   1 
ATOM   2689 C  CB  . ASP A 1 341 ? 20.333  1.875   37.916 1.00 70.19  ? 341 ASP A CB  1 
ATOM   2690 C  CG  . ASP A 1 341 ? 19.395  3.076   37.769 1.00 73.69  ? 341 ASP A CG  1 
ATOM   2691 O  OD1 . ASP A 1 341 ? 19.417  3.984   38.613 1.00 73.37  ? 341 ASP A OD1 1 
ATOM   2692 O  OD2 . ASP A 1 341 ? 18.665  3.121   36.778 1.00 78.64  ? 341 ASP A OD2 1 
ATOM   2693 N  N   . GLY A 1 342 ? 23.651  0.868   37.376 1.00 76.66  ? 342 GLY A N   1 
ATOM   2694 C  CA  . GLY A 1 342 ? 24.569  -0.289  37.342 1.00 66.64  ? 342 GLY A CA  1 
ATOM   2695 C  C   . GLY A 1 342 ? 25.760  -0.077  38.257 1.00 67.46  ? 342 GLY A C   1 
ATOM   2696 O  O   . GLY A 1 342 ? 25.963  1.069   38.699 1.00 65.80  ? 342 GLY A O   1 
ATOM   2697 N  N   . VAL A 1 343 ? 26.531  -1.127  38.540 1.00 61.56  ? 343 VAL A N   1 
ATOM   2698 C  CA  . VAL A 1 343 ? 27.915  -0.994  39.084 1.00 68.99  ? 343 VAL A CA  1 
ATOM   2699 C  C   . VAL A 1 343 ? 28.868  -1.720  38.136 1.00 73.87  ? 343 VAL A C   1 
ATOM   2700 O  O   . VAL A 1 343 ? 28.380  -2.537  37.294 1.00 63.10  ? 343 VAL A O   1 
ATOM   2701 C  CB  . VAL A 1 343 ? 28.031  -1.550  40.505 1.00 68.63  ? 343 VAL A CB  1 
ATOM   2702 C  CG1 . VAL A 1 343 ? 27.134  -0.794  41.462 1.00 74.33  ? 343 VAL A CG1 1 
ATOM   2703 C  CG2 . VAL A 1 343 ? 27.691  -3.021  40.533 1.00 83.68  ? 343 VAL A CG2 1 
ATOM   2704 N  N   . SER A 1 344 ? 30.168  -1.441  38.247 1.00 68.09  ? 344 SER A N   1 
ATOM   2705 C  CA  . SER A 1 344 ? 31.178  -2.126  37.403 1.00 65.61  ? 344 SER A CA  1 
ATOM   2706 C  C   . SER A 1 344 ? 31.387  -3.551  37.925 1.00 65.20  ? 344 SER A C   1 
ATOM   2707 O  O   . SER A 1 344 ? 31.467  -3.741  39.175 1.00 73.31  ? 344 SER A O   1 
ATOM   2708 C  CB  . SER A 1 344 ? 32.467  -1.351  37.328 1.00 67.54  ? 344 SER A CB  1 
ATOM   2709 O  OG  . SER A 1 344 ? 33.589  -2.223  37.207 1.00 65.67  ? 344 SER A OG  1 
ATOM   2710 N  N   . LEU A 1 345 ? 31.506  -4.487  36.990 1.00 62.52  ? 345 LEU A N   1 
ATOM   2711 C  CA  . LEU A 1 345 ? 31.850  -5.910  37.231 1.00 68.53  ? 345 LEU A CA  1 
ATOM   2712 C  C   . LEU A 1 345 ? 33.376  -6.146  37.252 1.00 72.30  ? 345 LEU A C   1 
ATOM   2713 O  O   . LEU A 1 345 ? 33.778  -7.295  37.488 1.00 76.31  ? 345 LEU A O   1 
ATOM   2714 C  CB  . LEU A 1 345 ? 31.230  -6.750  36.114 1.00 67.35  ? 345 LEU A CB  1 
ATOM   2715 C  CG  . LEU A 1 345 ? 29.752  -6.506  35.828 1.00 64.15  ? 345 LEU A CG  1 
ATOM   2716 C  CD1 . LEU A 1 345 ? 29.357  -7.198  34.535 1.00 64.89  ? 345 LEU A CD1 1 
ATOM   2717 C  CD2 . LEU A 1 345 ? 28.876  -6.982  36.963 1.00 60.96  ? 345 LEU A CD2 1 
ATOM   2718 N  N   . THR A 1 346 ? 34.226  -5.143  37.033 1.00 71.48  ? 346 THR A N   1 
ATOM   2719 C  CA  . THR A 1 346 ? 35.694  -5.376  36.998 1.00 75.80  ? 346 THR A CA  1 
ATOM   2720 C  C   . THR A 1 346 ? 36.171  -6.130  38.239 1.00 75.37  ? 346 THR A C   1 
ATOM   2721 O  O   . THR A 1 346 ? 37.066  -6.962  38.106 1.00 89.22  ? 346 THR A O   1 
ATOM   2722 C  CB  . THR A 1 346 ? 36.527  -4.102  36.842 1.00 73.15  ? 346 THR A CB  1 
ATOM   2723 O  OG1 . THR A 1 346 ? 36.220  -3.187  37.883 1.00 75.40  ? 346 THR A OG1 1 
ATOM   2724 C  CG2 . THR A 1 346 ? 36.299  -3.428  35.514 1.00 76.39  ? 346 THR A CG2 1 
ATOM   2725 N  N   . PRO A 1 347 ? 35.643  -5.892  39.466 1.00 73.22  ? 347 PRO A N   1 
ATOM   2726 C  CA  . PRO A 1 347 ? 36.088  -6.651  40.638 1.00 76.28  ? 347 PRO A CA  1 
ATOM   2727 C  C   . PRO A 1 347 ? 35.798  -8.154  40.479 1.00 70.77  ? 347 PRO A C   1 
ATOM   2728 O  O   . PRO A 1 347 ? 36.633  -8.939  40.852 1.00 75.06  ? 347 PRO A O   1 
ATOM   2729 C  CB  . PRO A 1 347 ? 35.308  -6.076  41.836 1.00 73.85  ? 347 PRO A CB  1 
ATOM   2730 C  CG  . PRO A 1 347 ? 34.779  -4.752  41.328 1.00 82.73  ? 347 PRO A CG  1 
ATOM   2731 C  CD  . PRO A 1 347 ? 34.598  -4.921  39.825 1.00 77.05  ? 347 PRO A CD  1 
ATOM   2732 N  N   . LEU A 1 348 ? 34.643  -8.515  39.915 1.00 64.70  ? 348 LEU A N   1 
ATOM   2733 C  CA  . LEU A 1 348 ? 34.271  -9.929  39.667 1.00 64.76  ? 348 LEU A CA  1 
ATOM   2734 C  C   . LEU A 1 348 ? 35.164  -10.507 38.567 1.00 71.28  ? 348 LEU A C   1 
ATOM   2735 O  O   . LEU A 1 348 ? 35.629  -11.623 38.756 1.00 75.58  ? 348 LEU A O   1 
ATOM   2736 C  CB  . LEU A 1 348 ? 32.799  -10.039 39.268 1.00 67.09  ? 348 LEU A CB  1 
ATOM   2737 C  CG  . LEU A 1 348 ? 31.776  -9.423  40.226 1.00 68.38  ? 348 LEU A CG  1 
ATOM   2738 C  CD1 . LEU A 1 348 ? 30.387  -9.553  39.641 1.00 72.74  ? 348 LEU A CD1 1 
ATOM   2739 C  CD2 . LEU A 1 348 ? 31.794  -10.057 41.603 1.00 63.36  ? 348 LEU A CD2 1 
ATOM   2740 N  N   . LEU A 1 349 ? 35.387  -9.775  37.471 1.00 74.71  ? 349 LEU A N   1 
ATOM   2741 C  CA  . LEU A 1 349 ? 36.182  -10.253 36.311 1.00 76.52  ? 349 LEU A CA  1 
ATOM   2742 C  C   . LEU A 1 349 ? 37.639  -10.481 36.738 1.00 85.72  ? 349 LEU A C   1 
ATOM   2743 O  O   . LEU A 1 349 ? 38.277  -11.488 36.270 1.00 82.71  ? 349 LEU A O   1 
ATOM   2744 C  CB  . LEU A 1 349 ? 36.067  -9.218  35.192 1.00 78.27  ? 349 LEU A CB  1 
ATOM   2745 C  CG  . LEU A 1 349 ? 34.672  -9.105  34.585 1.00 81.76  ? 349 LEU A CG  1 
ATOM   2746 C  CD1 . LEU A 1 349 ? 34.598  -7.959  33.616 1.00 80.71  ? 349 LEU A CD1 1 
ATOM   2747 C  CD2 . LEU A 1 349 ? 34.249  -10.392 33.898 1.00 77.57  ? 349 LEU A CD2 1 
ATOM   2748 N  N   . ARG A 1 350 ? 38.145  -9.614  37.620 1.00 81.81  ? 350 ARG A N   1 
ATOM   2749 C  CA  . ARG A 1 350 ? 39.523  -9.733  38.170 1.00 84.39  ? 350 ARG A CA  1 
ATOM   2750 C  C   . ARG A 1 350 ? 39.584  -10.773 39.295 1.00 86.83  ? 350 ARG A C   1 
ATOM   2751 O  O   . ARG A 1 350 ? 40.637  -10.851 39.940 1.00 87.32  ? 350 ARG A O   1 
ATOM   2752 C  CB  . ARG A 1 350 ? 39.996  -8.386  38.714 1.00 85.99  ? 350 ARG A CB  1 
ATOM   2753 C  CG  . ARG A 1 350 ? 40.257  -7.360  37.627 1.00 88.60  ? 350 ARG A CG  1 
ATOM   2754 C  CD  . ARG A 1 350 ? 40.929  -6.125  38.177 1.00 88.81  ? 350 ARG A CD  1 
ATOM   2755 N  NE  . ARG A 1 350 ? 40.822  -5.145  37.125 1.00 93.87  ? 350 ARG A NE  1 
ATOM   2756 C  CZ  . ARG A 1 350 ? 41.704  -4.959  36.166 1.00 89.07  ? 350 ARG A CZ  1 
ATOM   2757 N  NH1 . ARG A 1 350 ? 42.832  -5.642  36.155 1.00 82.26  ? 350 ARG A NH1 1 
ATOM   2758 N  NH2 . ARG A 1 350 ? 41.468  -4.039  35.246 1.00 104.24 ? 350 ARG A NH2 1 
ATOM   2759 N  N   . ARG A 1 351 ? 38.490  -11.490 39.567 1.00 90.21  ? 351 ARG A N   1 
ATOM   2760 C  CA  . ARG A 1 351 ? 38.343  -12.378 40.749 1.00 83.60  ? 351 ARG A CA  1 
ATOM   2761 C  C   . ARG A 1 351 ? 38.961  -11.694 41.981 1.00 78.04  ? 351 ARG A C   1 
ATOM   2762 O  O   . ARG A 1 351 ? 39.591  -12.360 42.749 1.00 91.14  ? 351 ARG A O   1 
ATOM   2763 C  CB  . ARG A 1 351 ? 38.989  -13.729 40.421 1.00 84.15  ? 351 ARG A CB  1 
ATOM   2764 C  CG  . ARG A 1 351 ? 38.172  -14.638 39.512 1.00 87.81  ? 351 ARG A CG  1 
ATOM   2765 C  CD  . ARG A 1 351 ? 38.821  -15.993 39.264 1.00 98.09  ? 351 ARG A CD  1 
ATOM   2766 N  NE  . ARG A 1 351 ? 40.161  -15.759 38.724 1.00 116.02 ? 351 ARG A NE  1 
ATOM   2767 C  CZ  . ARG A 1 351 ? 41.303  -16.092 39.313 1.00 121.61 ? 351 ARG A CZ  1 
ATOM   2768 N  NH1 . ARG A 1 351 ? 41.303  -16.734 40.465 1.00 144.72 ? 351 ARG A NH1 1 
ATOM   2769 N  NH2 . ARG A 1 351 ? 42.453  -15.787 38.740 1.00 127.95 ? 351 ARG A NH2 1 
ATOM   2770 N  N   . LYS A 1 352 ? 38.818  -10.385 42.146 1.00 90.30  ? 352 LYS A N   1 
ATOM   2771 C  CA  . LYS A 1 352 ? 39.191  -9.679  43.395 1.00 89.77  ? 352 LYS A CA  1 
ATOM   2772 C  C   . LYS A 1 352 ? 37.917  -9.403  44.186 1.00 100.73 ? 352 LYS A C   1 
ATOM   2773 O  O   . LYS A 1 352 ? 36.837  -9.917  43.815 1.00 113.22 ? 352 LYS A O   1 
ATOM   2774 C  CB  . LYS A 1 352 ? 39.940  -8.392  43.092 1.00 91.10  ? 352 LYS A CB  1 
ATOM   2775 C  CG  . LYS A 1 352 ? 41.442  -8.585  42.977 1.00 108.45 ? 352 LYS A CG  1 
ATOM   2776 C  CD  . LYS A 1 352 ? 42.108  -7.349  42.409 1.00 140.20 ? 352 LYS A CD  1 
ATOM   2777 C  CE  . LYS A 1 352 ? 41.235  -6.101  42.449 1.00 143.19 ? 352 LYS A CE  1 
ATOM   2778 N  NZ  . LYS A 1 352 ? 41.989  -4.899  42.031 1.00 146.02 ? 352 LYS A NZ  1 
ATOM   2779 N  N   . GLY A 1 353 ? 38.041  -8.677  45.285 1.00 91.45  ? 353 GLY A N   1 
ATOM   2780 C  CA  . GLY A 1 353 ? 36.879  -8.414  46.136 1.00 87.75  ? 353 GLY A CA  1 
ATOM   2781 C  C   . GLY A 1 353 ? 36.474  -6.986  45.949 1.00 87.79  ? 353 GLY A C   1 
ATOM   2782 O  O   . GLY A 1 353 ? 36.968  -6.351  45.023 1.00 93.78  ? 353 GLY A O   1 
ATOM   2783 N  N   . GLY A 1 354 ? 35.646  -6.494  46.850 1.00 99.24  ? 354 GLY A N   1 
ATOM   2784 C  CA  . GLY A 1 354 ? 35.226  -5.092  46.868 1.00 95.65  ? 354 GLY A CA  1 
ATOM   2785 C  C   . GLY A 1 354 ? 33.941  -4.878  46.098 1.00 86.98  ? 354 GLY A C   1 
ATOM   2786 O  O   . GLY A 1 354 ? 33.580  -3.722  45.989 1.00 100.98 ? 354 GLY A O   1 
ATOM   2787 N  N   . PHE A 1 355 ? 33.266  -5.927  45.614 1.00 78.97  ? 355 PHE A N   1 
ATOM   2788 C  CA  . PHE A 1 355 ? 31.970  -5.818  44.892 1.00 77.24  ? 355 PHE A CA  1 
ATOM   2789 C  C   . PHE A 1 355 ? 30.809  -5.809  45.888 1.00 78.93  ? 355 PHE A C   1 
ATOM   2790 O  O   . PHE A 1 355 ? 30.440  -6.870  46.370 1.00 82.24  ? 355 PHE A O   1 
ATOM   2791 C  CB  . PHE A 1 355 ? 31.816  -6.954  43.885 1.00 77.94  ? 355 PHE A CB  1 
ATOM   2792 C  CG  . PHE A 1 355 ? 30.600  -6.826  43.007 1.00 77.90  ? 355 PHE A CG  1 
ATOM   2793 C  CD1 . PHE A 1 355 ? 29.396  -7.380  43.386 1.00 77.35  ? 355 PHE A CD1 1 
ATOM   2794 C  CD2 . PHE A 1 355 ? 30.662  -6.155  41.801 1.00 84.77  ? 355 PHE A CD2 1 
ATOM   2795 C  CE1 . PHE A 1 355 ? 28.272  -7.263  42.589 1.00 78.80  ? 355 PHE A CE1 1 
ATOM   2796 C  CE2 . PHE A 1 355 ? 29.543  -6.060  40.991 1.00 87.24  ? 355 PHE A CE2 1 
ATOM   2797 C  CZ  . PHE A 1 355 ? 28.348  -6.610  41.389 1.00 81.43  ? 355 PHE A CZ  1 
ATOM   2798 N  N   . LYS A 1 356 ? 30.222  -4.642  46.157 1.00 96.91  ? 356 LYS A N   1 
ATOM   2799 C  CA  . LYS A 1 356 ? 29.216  -4.451  47.246 1.00 91.93  ? 356 LYS A CA  1 
ATOM   2800 C  C   . LYS A 1 356 ? 27.990  -5.297  46.888 1.00 86.82  ? 356 LYS A C   1 
ATOM   2801 O  O   . LYS A 1 356 ? 27.584  -5.415  45.718 1.00 88.80  ? 356 LYS A O   1 
ATOM   2802 C  CB  . LYS A 1 356 ? 28.961  -2.953  47.526 1.00 91.14  ? 356 LYS A CB  1 
ATOM   2803 C  CG  . LYS A 1 356 ? 30.224  -2.134  47.826 1.00 105.52 ? 356 LYS A CG  1 
ATOM   2804 C  CD  . LYS A 1 356 ? 30.308  -0.685  47.256 1.00 117.78 ? 356 LYS A CD  1 
ATOM   2805 C  CE  . LYS A 1 356 ? 30.483  0.387   48.311 1.00 119.53 ? 356 LYS A CE  1 
ATOM   2806 N  NZ  . LYS A 1 356 ? 29.189  0.641   48.991 1.00 135.34 ? 356 LYS A NZ  1 
ATOM   2807 N  N   . PRO A 1 357 ? 27.387  -5.947  47.906 1.00 83.62  ? 357 PRO A N   1 
ATOM   2808 C  CA  . PRO A 1 357 ? 26.234  -6.823  47.692 1.00 89.00  ? 357 PRO A CA  1 
ATOM   2809 C  C   . PRO A 1 357 ? 24.999  -5.915  47.568 1.00 87.87  ? 357 PRO A C   1 
ATOM   2810 O  O   . PRO A 1 357 ? 24.957  -4.868  48.198 1.00 74.48  ? 357 PRO A O   1 
ATOM   2811 C  CB  . PRO A 1 357 ? 26.244  -7.663  48.975 1.00 82.82  ? 357 PRO A CB  1 
ATOM   2812 C  CG  . PRO A 1 357 ? 26.668  -6.648  50.031 1.00 79.44  ? 357 PRO A CG  1 
ATOM   2813 C  CD  . PRO A 1 357 ? 27.684  -5.762  49.336 1.00 76.65  ? 357 PRO A CD  1 
ATOM   2814 N  N   . ARG A 1 358 ? 24.015  -6.286  46.761 1.00 80.19  ? 358 ARG A N   1 
ATOM   2815 C  CA  . ARG A 1 358 ? 22.962  -5.312  46.388 1.00 74.14  ? 358 ARG A CA  1 
ATOM   2816 C  C   . ARG A 1 358 ? 21.685  -6.018  45.979 1.00 67.68  ? 358 ARG A C   1 
ATOM   2817 O  O   . ARG A 1 358 ? 21.622  -7.227  46.051 1.00 71.81  ? 358 ARG A O   1 
ATOM   2818 C  CB  . ARG A 1 358 ? 23.467  -4.528  45.186 1.00 80.57  ? 358 ARG A CB  1 
ATOM   2819 C  CG  . ARG A 1 358 ? 23.819  -5.430  44.018 1.00 74.17  ? 358 ARG A CG  1 
ATOM   2820 C  CD  . ARG A 1 358 ? 23.851  -4.707  42.693 1.00 70.86  ? 358 ARG A CD  1 
ATOM   2821 N  NE  . ARG A 1 358 ? 24.303  -5.652  41.681 1.00 81.80  ? 358 ARG A NE  1 
ATOM   2822 C  CZ  . ARG A 1 358 ? 24.452  -5.408  40.382 1.00 68.20  ? 358 ARG A CZ  1 
ATOM   2823 N  NH1 . ARG A 1 358 ? 24.178  -4.215  39.894 1.00 67.41  ? 358 ARG A NH1 1 
ATOM   2824 N  NH2 . ARG A 1 358 ? 24.887  -6.363  39.578 1.00 70.32  ? 358 ARG A NH2 1 
ATOM   2825 N  N   . ALA A 1 359 ? 20.716  -5.259  45.517 1.00 63.40  ? 359 ALA A N   1 
ATOM   2826 C  CA  . ALA A 1 359 ? 19.439  -5.813  45.039 1.00 63.24  ? 359 ALA A CA  1 
ATOM   2827 C  C   . ALA A 1 359 ? 19.285  -5.546  43.546 1.00 60.17  ? 359 ALA A C   1 
ATOM   2828 O  O   . ALA A 1 359 ? 19.792  -4.545  43.046 1.00 66.53  ? 359 ALA A O   1 
ATOM   2829 C  CB  . ALA A 1 359 ? 18.345  -5.172  45.823 1.00 69.65  ? 359 ALA A CB  1 
ATOM   2830 N  N   . LEU A 1 360 ? 18.586  -6.403  42.831 1.00 58.25  ? 360 LEU A N   1 
ATOM   2831 C  CA  . LEU A 1 360 ? 18.218  -6.050  41.447 1.00 64.11  ? 360 LEU A CA  1 
ATOM   2832 C  C   . LEU A 1 360 ? 16.718  -5.777  41.412 1.00 68.28  ? 360 LEU A C   1 
ATOM   2833 O  O   . LEU A 1 360 ? 15.954  -6.334  42.217 1.00 61.75  ? 360 LEU A O   1 
ATOM   2834 C  CB  . LEU A 1 360 ? 18.656  -7.137  40.469 1.00 65.06  ? 360 LEU A CB  1 
ATOM   2835 C  CG  . LEU A 1 360 ? 20.158  -7.404  40.458 1.00 71.10  ? 360 LEU A CG  1 
ATOM   2836 C  CD1 . LEU A 1 360 ? 20.520  -8.453  39.416 1.00 74.22  ? 360 LEU A CD1 1 
ATOM   2837 C  CD2 . LEU A 1 360 ? 20.936  -6.119  40.208 1.00 74.85  ? 360 LEU A CD2 1 
ATOM   2838 N  N   . TYR A 1 361 ? 16.340  -4.886  40.516 1.00 71.13  ? 361 TYR A N   1 
ATOM   2839 C  CA  . TYR A 1 361 ? 14.954  -4.427  40.386 1.00 61.63  ? 361 TYR A CA  1 
ATOM   2840 C  C   . TYR A 1 361 ? 14.516  -4.654  38.946 1.00 63.58  ? 361 TYR A C   1 
ATOM   2841 O  O   . TYR A 1 361 ? 15.366  -4.621  37.976 1.00 71.11  ? 361 TYR A O   1 
ATOM   2842 C  CB  . TYR A 1 361 ? 14.890  -2.989  40.868 1.00 58.63  ? 361 TYR A CB  1 
ATOM   2843 C  CG  . TYR A 1 361 ? 15.379  -2.778  42.280 1.00 58.32  ? 361 TYR A CG  1 
ATOM   2844 C  CD1 . TYR A 1 361 ? 14.523  -2.896  43.366 1.00 62.74  ? 361 TYR A CD1 1 
ATOM   2845 C  CD2 . TYR A 1 361 ? 16.689  -2.417  42.543 1.00 60.51  ? 361 TYR A CD2 1 
ATOM   2846 C  CE1 . TYR A 1 361 ? 14.947  -2.653  44.670 1.00 67.00  ? 361 TYR A CE1 1 
ATOM   2847 C  CE2 . TYR A 1 361 ? 17.137  -2.186  43.843 1.00 65.33  ? 361 TYR A CE2 1 
ATOM   2848 C  CZ  . TYR A 1 361 ? 16.263  -2.286  44.917 1.00 67.19  ? 361 TYR A CZ  1 
ATOM   2849 O  OH  . TYR A 1 361 ? 16.683  -2.027  46.196 1.00 63.70  ? 361 TYR A OH  1 
ATOM   2850 N  N   . TRP A 1 362 ? 13.234  -4.995  38.868 1.00 58.83  ? 362 TRP A N   1 
ATOM   2851 C  CA  . TRP A 1 362 ? 12.416  -5.079  37.639 1.00 59.96  ? 362 TRP A CA  1 
ATOM   2852 C  C   . TRP A 1 362 ? 11.127  -4.289  37.858 1.00 62.56  ? 362 TRP A C   1 
ATOM   2853 O  O   . TRP A 1 362 ? 10.678  -4.191  39.018 1.00 58.12  ? 362 TRP A O   1 
ATOM   2854 C  CB  . TRP A 1 362 ? 12.112  -6.533  37.301 1.00 59.84  ? 362 TRP A CB  1 
ATOM   2855 C  CG  . TRP A 1 362 ? 13.313  -7.289  36.843 1.00 62.89  ? 362 TRP A CG  1 
ATOM   2856 C  CD1 . TRP A 1 362 ? 13.721  -7.485  35.562 1.00 63.68  ? 362 TRP A CD1 1 
ATOM   2857 C  CD2 . TRP A 1 362 ? 14.276  -7.930  37.681 1.00 66.80  ? 362 TRP A CD2 1 
ATOM   2858 N  NE1 . TRP A 1 362 ? 14.890  -8.184  35.550 1.00 67.50  ? 362 TRP A NE1 1 
ATOM   2859 C  CE2 . TRP A 1 362 ? 15.244  -8.478  36.833 1.00 66.61  ? 362 TRP A CE2 1 
ATOM   2860 C  CE3 . TRP A 1 362 ? 14.408  -8.086  39.060 1.00 72.92  ? 362 TRP A CE3 1 
ATOM   2861 C  CZ2 . TRP A 1 362 ? 16.320  -9.198  37.320 1.00 75.06  ? 362 TRP A CZ2 1 
ATOM   2862 C  CZ3 . TRP A 1 362 ? 15.474  -8.800  39.542 1.00 76.48  ? 362 TRP A CZ3 1 
ATOM   2863 C  CH2 . TRP A 1 362 ? 16.409  -9.363  38.678 1.00 76.72  ? 362 TRP A CH2 1 
ATOM   2864 N  N   . HIS A 1 363 ? 10.587  -3.724  36.779 1.00 61.69  ? 363 HIS A N   1 
ATOM   2865 C  CA  . HIS A 1 363 ? 9.268   -3.052  36.767 1.00 59.74  ? 363 HIS A CA  1 
ATOM   2866 C  C   . HIS A 1 363 ? 8.684   -3.109  35.357 1.00 59.99  ? 363 HIS A C   1 
ATOM   2867 O  O   . HIS A 1 363 ? 9.224   -2.464  34.464 1.00 62.99  ? 363 HIS A O   1 
ATOM   2868 C  CB  . HIS A 1 363 ? 9.405   -1.636  37.310 1.00 61.39  ? 363 HIS A CB  1 
ATOM   2869 C  CG  . HIS A 1 363 ? 8.170   -0.827  37.107 1.00 64.18  ? 363 HIS A CG  1 
ATOM   2870 N  ND1 . HIS A 1 363 ? 7.008   -1.140  37.736 1.00 68.05  ? 363 HIS A ND1 1 
ATOM   2871 C  CD2 . HIS A 1 363 ? 7.911   0.277   36.372 1.00 64.90  ? 363 HIS A CD2 1 
ATOM   2872 C  CE1 . HIS A 1 363 ? 6.076   -0.273  37.392 1.00 69.52  ? 363 HIS A CE1 1 
ATOM   2873 N  NE2 . HIS A 1 363 ? 6.603   0.614   36.568 1.00 58.46  ? 363 HIS A NE2 1 
ATOM   2874 N  N   . TYR A 1 364 ? 7.627   -3.896  35.168 1.00 67.86  ? 364 TYR A N   1 
ATOM   2875 C  CA  . TYR A 1 364 ? 7.011   -4.176  33.845 1.00 66.08  ? 364 TYR A CA  1 
ATOM   2876 C  C   . TYR A 1 364 ? 5.518   -3.873  33.932 1.00 62.56  ? 364 TYR A C   1 
ATOM   2877 O  O   . TYR A 1 364 ? 4.730   -4.788  34.099 1.00 69.30  ? 364 TYR A O   1 
ATOM   2878 C  CB  . TYR A 1 364 ? 7.314   -5.610  33.389 1.00 57.61  ? 364 TYR A CB  1 
ATOM   2879 C  CG  . TYR A 1 364 ? 6.858   -5.863  31.973 1.00 61.27  ? 364 TYR A CG  1 
ATOM   2880 C  CD1 . TYR A 1 364 ? 7.504   -5.277  30.898 1.00 65.26  ? 364 TYR A CD1 1 
ATOM   2881 C  CD2 . TYR A 1 364 ? 5.742   -6.629  31.704 1.00 61.17  ? 364 TYR A CD2 1 
ATOM   2882 C  CE1 . TYR A 1 364 ? 7.078   -5.477  29.598 1.00 62.42  ? 364 TYR A CE1 1 
ATOM   2883 C  CE2 . TYR A 1 364 ? 5.303   -6.850  30.416 1.00 63.14  ? 364 TYR A CE2 1 
ATOM   2884 C  CZ  . TYR A 1 364 ? 5.976   -6.273  29.358 1.00 67.00  ? 364 TYR A CZ  1 
ATOM   2885 O  OH  . TYR A 1 364 ? 5.531   -6.460  28.082 1.00 78.60  ? 364 TYR A OH  1 
ATOM   2886 N  N   . PRO A 1 365 ? 5.082   -2.591  33.871 1.00 68.11  ? 365 PRO A N   1 
ATOM   2887 C  CA  . PRO A 1 365 ? 3.669   -2.233  34.020 1.00 67.96  ? 365 PRO A CA  1 
ATOM   2888 C  C   . PRO A 1 365 ? 2.910   -2.401  32.702 1.00 61.08  ? 365 PRO A C   1 
ATOM   2889 O  O   . PRO A 1 365 ? 2.294   -1.458  32.265 1.00 55.50  ? 365 PRO A O   1 
ATOM   2890 C  CB  . PRO A 1 365 ? 3.718   -0.753  34.444 1.00 68.76  ? 365 PRO A CB  1 
ATOM   2891 C  CG  . PRO A 1 365 ? 4.936   -0.226  33.738 1.00 68.12  ? 365 PRO A CG  1 
ATOM   2892 C  CD  . PRO A 1 365 ? 5.913   -1.391  33.682 1.00 74.42  ? 365 PRO A CD  1 
ATOM   2893 N  N   . HIS A 1 366 ? 2.985   -3.596  32.119 1.00 59.41  ? 366 HIS A N   1 
ATOM   2894 C  CA  . HIS A 1 366 ? 2.390   -3.907  30.802 1.00 62.11  ? 366 HIS A CA  1 
ATOM   2895 C  C   . HIS A 1 366 ? 1.873   -5.345  30.777 1.00 66.56  ? 366 HIS A C   1 
ATOM   2896 O  O   . HIS A 1 366 ? 2.284   -6.167  31.621 1.00 71.74  ? 366 HIS A O   1 
ATOM   2897 C  CB  . HIS A 1 366 ? 3.445   -3.644  29.727 1.00 69.57  ? 366 HIS A CB  1 
ATOM   2898 C  CG  . HIS A 1 366 ? 4.069   -2.291  29.813 1.00 70.46  ? 366 HIS A CG  1 
ATOM   2899 N  ND1 . HIS A 1 366 ? 3.444   -1.165  29.309 1.00 70.28  ? 366 HIS A ND1 1 
ATOM   2900 C  CD2 . HIS A 1 366 ? 5.252   -1.891  30.341 1.00 71.78  ? 366 HIS A CD2 1 
ATOM   2901 C  CE1 . HIS A 1 366 ? 4.217   -0.121  29.547 1.00 74.29  ? 366 HIS A CE1 1 
ATOM   2902 N  NE2 . HIS A 1 366 ? 5.344   -0.542  30.173 1.00 66.07  ? 366 HIS A NE2 1 
ATOM   2903 N  N   . TYR A 1 367 ? 0.992   -5.639  29.830 1.00 68.15  ? 367 TYR A N   1 
ATOM   2904 C  CA  . TYR A 1 367 ? 0.685   -7.020  29.395 1.00 66.28  ? 367 TYR A CA  1 
ATOM   2905 C  C   . TYR A 1 367 ? 1.636   -7.363  28.259 1.00 65.34  ? 367 TYR A C   1 
ATOM   2906 O  O   . TYR A 1 367 ? 1.733   -6.527  27.347 1.00 71.81  ? 367 TYR A O   1 
ATOM   2907 C  CB  . TYR A 1 367 ? -0.767  -7.093  28.953 1.00 69.20  ? 367 TYR A CB  1 
ATOM   2908 C  CG  . TYR A 1 367 ? -1.732  -6.885  30.086 1.00 66.14  ? 367 TYR A CG  1 
ATOM   2909 C  CD1 . TYR A 1 367 ? -2.025  -7.923  30.931 1.00 70.15  ? 367 TYR A CD1 1 
ATOM   2910 C  CD2 . TYR A 1 367 ? -2.333  -5.665  30.336 1.00 70.58  ? 367 TYR A CD2 1 
ATOM   2911 C  CE1 . TYR A 1 367 ? -2.894  -7.764  31.994 1.00 76.25  ? 367 TYR A CE1 1 
ATOM   2912 C  CE2 . TYR A 1 367 ? -3.198  -5.480  31.398 1.00 69.51  ? 367 TYR A CE2 1 
ATOM   2913 C  CZ  . TYR A 1 367 ? -3.484  -6.541  32.235 1.00 74.22  ? 367 TYR A CZ  1 
ATOM   2914 O  OH  . TYR A 1 367 ? -4.350  -6.427  33.285 1.00 67.85  ? 367 TYR A OH  1 
ATOM   2915 N  N   . SER A 1 368 ? 2.312   -8.512  28.325 1.00 68.25  ? 368 SER A N   1 
ATOM   2916 C  CA  . SER A 1 368 ? 3.235   -8.997  27.261 1.00 76.52  ? 368 SER A CA  1 
ATOM   2917 C  C   . SER A 1 368 ? 2.475   -9.881  26.273 1.00 73.16  ? 368 SER A C   1 
ATOM   2918 O  O   . SER A 1 368 ? 1.349   -10.359 26.609 1.00 71.96  ? 368 SER A O   1 
ATOM   2919 C  CB  . SER A 1 368 ? 4.428   -9.746  27.803 1.00 78.52  ? 368 SER A CB  1 
ATOM   2920 O  OG  . SER A 1 368 ? 4.130   -11.119 28.003 1.00 80.19  ? 368 SER A OG  1 
ATOM   2921 N  N   . ASN A 1 369 ? 3.098   -10.140 25.125 1.00 64.89  ? 369 ASN A N   1 
ATOM   2922 C  CA  . ASN A 1 369 ? 2.473   -10.999 24.094 1.00 66.44  ? 369 ASN A CA  1 
ATOM   2923 C  C   . ASN A 1 369 ? 2.674   -12.461 24.458 1.00 66.01  ? 369 ASN A C   1 
ATOM   2924 O  O   . ASN A 1 369 ? 2.116   -13.293 23.766 1.00 82.89  ? 369 ASN A O   1 
ATOM   2925 C  CB  . ASN A 1 369 ? 3.035   -10.773 22.697 1.00 69.73  ? 369 ASN A CB  1 
ATOM   2926 C  CG  . ASN A 1 369 ? 2.486   -9.524  22.057 1.00 70.95  ? 369 ASN A CG  1 
ATOM   2927 O  OD1 . ASN A 1 369 ? 1.467   -8.992  22.504 1.00 69.10  ? 369 ASN A OD1 1 
ATOM   2928 N  ND2 . ASN A 1 369 ? 3.178   -9.052  21.031 1.00 81.93  ? 369 ASN A ND2 1 
ATOM   2929 N  N   . GLN A 1 370 ? 3.409   -12.770 25.518 1.00 71.97  ? 370 GLN A N   1 
ATOM   2930 C  CA  . GLN A 1 370 ? 3.886   -14.155 25.755 1.00 82.54  ? 370 GLN A CA  1 
ATOM   2931 C  C   . GLN A 1 370 ? 3.221   -14.724 27.019 1.00 80.62  ? 370 GLN A C   1 
ATOM   2932 O  O   . GLN A 1 370 ? 3.736   -15.740 27.563 1.00 85.50  ? 370 GLN A O   1 
ATOM   2933 C  CB  . GLN A 1 370 ? 5.419   -14.113 25.769 1.00 85.73  ? 370 GLN A CB  1 
ATOM   2934 C  CG  . GLN A 1 370 ? 6.053   -13.701 24.440 1.00 79.80  ? 370 GLN A CG  1 
ATOM   2935 C  CD  . GLN A 1 370 ? 6.348   -12.228 24.266 1.00 81.06  ? 370 GLN A CD  1 
ATOM   2936 O  OE1 . GLN A 1 370 ? 6.206   -11.413 25.185 1.00 80.88  ? 370 GLN A OE1 1 
ATOM   2937 N  NE2 . GLN A 1 370 ? 6.744   -11.875 23.046 1.00 91.35  ? 370 GLN A NE2 1 
ATOM   2938 N  N   . GLY A 1 371 ? 2.139   -14.085 27.479 1.00 77.83  ? 371 GLY A N   1 
ATOM   2939 C  CA  . GLY A 1 371 ? 1.421   -14.553 28.682 1.00 86.01  ? 371 GLY A CA  1 
ATOM   2940 C  C   . GLY A 1 371 ? 1.765   -13.729 29.911 1.00 78.49  ? 371 GLY A C   1 
ATOM   2941 O  O   . GLY A 1 371 ? 1.179   -14.000 30.978 1.00 93.26  ? 371 GLY A O   1 
ATOM   2942 N  N   . GLY A 1 372 ? 2.676   -12.758 29.778 1.00 71.00  ? 372 GLY A N   1 
ATOM   2943 C  CA  . GLY A 1 372 ? 3.120   -11.958 30.937 1.00 71.01  ? 372 GLY A CA  1 
ATOM   2944 C  C   . GLY A 1 372 ? 2.078   -10.948 31.389 1.00 68.60  ? 372 GLY A C   1 
ATOM   2945 O  O   . GLY A 1 372 ? 1.242   -10.549 30.552 1.00 77.64  ? 372 GLY A O   1 
ATOM   2946 N  N   . VAL A 1 373 ? 2.130   -10.541 32.663 1.00 68.32  ? 373 VAL A N   1 
ATOM   2947 C  CA  . VAL A 1 373 ? 1.142   -9.566  33.218 1.00 71.09  ? 373 VAL A CA  1 
ATOM   2948 C  C   . VAL A 1 373 ? 1.890   -8.481  34.001 1.00 64.55  ? 373 VAL A C   1 
ATOM   2949 O  O   . VAL A 1 373 ? 3.040   -8.733  34.411 1.00 64.55  ? 373 VAL A O   1 
ATOM   2950 C  CB  . VAL A 1 373 ? 0.098   -10.272 34.105 1.00 81.08  ? 373 VAL A CB  1 
ATOM   2951 C  CG1 . VAL A 1 373 ? -0.975  -10.958 33.275 1.00 86.39  ? 373 VAL A CG1 1 
ATOM   2952 C  CG2 . VAL A 1 373 ? 0.749   -11.253 35.067 1.00 85.72  ? 373 VAL A CG2 1 
ATOM   2953 N  N   . PRO A 1 374 ? 1.295   -7.288  34.225 1.00 56.47  ? 374 PRO A N   1 
ATOM   2954 C  CA  . PRO A 1 374 ? 1.966   -6.199  34.912 1.00 57.80  ? 374 PRO A CA  1 
ATOM   2955 C  C   . PRO A 1 374 ? 2.390   -6.632  36.310 1.00 58.76  ? 374 PRO A C   1 
ATOM   2956 O  O   . PRO A 1 374 ? 1.535   -7.155  37.076 1.00 66.89  ? 374 PRO A O   1 
ATOM   2957 C  CB  . PRO A 1 374 ? 0.923   -5.073  35.011 1.00 62.67  ? 374 PRO A CB  1 
ATOM   2958 C  CG  . PRO A 1 374 ? -0.066  -5.379  33.900 1.00 62.97  ? 374 PRO A CG  1 
ATOM   2959 C  CD  . PRO A 1 374 ? -0.041  -6.890  33.758 1.00 61.84  ? 374 PRO A CD  1 
ATOM   2960 N  N   . GLY A 1 375 ? 3.672   -6.389  36.584 1.00 59.54  ? 375 GLY A N   1 
ATOM   2961 C  CA  . GLY A 1 375 ? 4.317   -6.680  37.867 1.00 61.01  ? 375 GLY A CA  1 
ATOM   2962 C  C   . GLY A 1 375 ? 5.677   -6.041  37.952 1.00 59.25  ? 375 GLY A C   1 
ATOM   2963 O  O   . GLY A 1 375 ? 6.102   -5.412  36.997 1.00 61.98  ? 375 GLY A O   1 
ATOM   2964 N  N   . GLY A 1 376 ? 6.303   -6.179  39.108 1.00 64.97  ? 376 GLY A N   1 
ATOM   2965 C  CA  . GLY A 1 376 ? 7.701   -5.805  39.362 1.00 69.37  ? 376 GLY A CA  1 
ATOM   2966 C  C   . GLY A 1 376 ? 8.392   -6.922  40.104 1.00 66.17  ? 376 GLY A C   1 
ATOM   2967 O  O   . GLY A 1 376 ? 7.744   -7.944  40.387 1.00 69.16  ? 376 GLY A O   1 
ATOM   2968 N  N   . ALA A 1 377 ? 9.662   -6.754  40.420 1.00 64.62  ? 377 ALA A N   1 
ATOM   2969 C  CA  . ALA A 1 377 ? 10.379  -7.783  41.183 1.00 63.85  ? 377 ALA A CA  1 
ATOM   2970 C  C   . ALA A 1 377 ? 11.666  -7.218  41.759 1.00 60.07  ? 377 ALA A C   1 
ATOM   2971 O  O   . ALA A 1 377 ? 12.234  -6.240  41.228 1.00 65.81  ? 377 ALA A O   1 
ATOM   2972 C  CB  . ALA A 1 377 ? 10.638  -8.983  40.305 1.00 69.76  ? 377 ALA A CB  1 
ATOM   2973 N  N   . ILE A 1 378 ? 12.102  -7.870  42.818 1.00 55.14  ? 378 ILE A N   1 
ATOM   2974 C  CA  . ILE A 1 378 ? 13.377  -7.560  43.495 1.00 59.72  ? 378 ILE A CA  1 
ATOM   2975 C  C   . ILE A 1 378 ? 14.053  -8.887  43.757 1.00 58.48  ? 378 ILE A C   1 
ATOM   2976 O  O   . ILE A 1 378 ? 13.365  -9.849  44.003 1.00 62.90  ? 378 ILE A O   1 
ATOM   2977 C  CB  . ILE A 1 378 ? 13.139  -6.772  44.781 1.00 60.55  ? 378 ILE A CB  1 
ATOM   2978 C  CG1 . ILE A 1 378 ? 14.440  -6.574  45.548 1.00 60.16  ? 378 ILE A CG1 1 
ATOM   2979 C  CG2 . ILE A 1 378 ? 12.077  -7.439  45.638 1.00 65.69  ? 378 ILE A CG2 1 
ATOM   2980 C  CD1 . ILE A 1 378 ? 14.325  -5.522  46.635 1.00 70.10  ? 378 ILE A CD1 1 
ATOM   2981 N  N   . ARG A 1 379 ? 15.358  -8.923  43.602 1.00 64.88  ? 379 ARG A N   1 
ATOM   2982 C  CA  . ARG A 1 379 ? 16.192  -10.094 43.935 1.00 65.23  ? 379 ARG A CA  1 
ATOM   2983 C  C   . ARG A 1 379 ? 17.236  -9.578  44.918 1.00 68.11  ? 379 ARG A C   1 
ATOM   2984 O  O   . ARG A 1 379 ? 17.956  -8.618  44.576 1.00 75.32  ? 379 ARG A O   1 
ATOM   2985 C  CB  . ARG A 1 379 ? 16.761  -10.692 42.646 1.00 72.32  ? 379 ARG A CB  1 
ATOM   2986 C  CG  . ARG A 1 379 ? 18.084  -11.414 42.813 1.00 73.95  ? 379 ARG A CG  1 
ATOM   2987 C  CD  . ARG A 1 379 ? 17.871  -12.786 43.403 1.00 82.09  ? 379 ARG A CD  1 
ATOM   2988 N  NE  . ARG A 1 379 ? 19.131  -13.503 43.486 1.00 77.86  ? 379 ARG A NE  1 
ATOM   2989 C  CZ  . ARG A 1 379 ? 19.677  -14.207 42.502 1.00 66.50  ? 379 ARG A CZ  1 
ATOM   2990 N  NH1 . ARG A 1 379 ? 19.092  -14.346 41.322 1.00 70.26  ? 379 ARG A NH1 1 
ATOM   2991 N  NH2 . ARG A 1 379 ? 20.835  -14.771 42.718 1.00 62.38  ? 379 ARG A NH2 1 
ATOM   2992 N  N   . GLU A 1 380 ? 17.254  -10.124 46.125 1.00 68.98  ? 380 GLU A N   1 
ATOM   2993 C  CA  . GLU A 1 380 ? 18.293  -9.776  47.111 1.00 71.91  ? 380 GLU A CA  1 
ATOM   2994 C  C   . GLU A 1 380 ? 18.937  -11.070 47.600 1.00 73.95  ? 380 GLU A C   1 
ATOM   2995 O  O   . GLU A 1 380 ? 18.212  -11.886 48.148 1.00 74.70  ? 380 GLU A O   1 
ATOM   2996 C  CB  . GLU A 1 380 ? 17.712  -8.943  48.241 1.00 77.16  ? 380 GLU A CB  1 
ATOM   2997 C  CG  . GLU A 1 380 ? 18.828  -8.390  49.092 1.00 96.01  ? 380 GLU A CG  1 
ATOM   2998 C  CD  . GLU A 1 380 ? 18.489  -7.096  49.793 1.00 105.01 ? 380 GLU A CD  1 
ATOM   2999 O  OE1 . GLU A 1 380 ? 17.469  -7.099  50.566 1.00 95.39  ? 380 GLU A OE1 1 
ATOM   3000 O  OE2 . GLU A 1 380 ? 19.242  -6.101  49.554 1.00 109.60 ? 380 GLU A OE2 1 
ATOM   3001 N  N   . GLY A 1 381 ? 20.249  -11.226 47.387 1.00 72.62  ? 381 GLY A N   1 
ATOM   3002 C  CA  . GLY A 1 381 ? 20.993  -12.463 47.662 1.00 75.72  ? 381 GLY A CA  1 
ATOM   3003 C  C   . GLY A 1 381 ? 20.347  -13.620 46.946 1.00 76.77  ? 381 GLY A C   1 
ATOM   3004 O  O   . GLY A 1 381 ? 20.526  -13.722 45.734 1.00 88.99  ? 381 GLY A O   1 
ATOM   3005 N  N   . ASN A 1 382 ? 19.591  -14.441 47.665 1.00 77.99  ? 382 ASN A N   1 
ATOM   3006 C  CA  . ASN A 1 382 ? 19.053  -15.722 47.136 1.00 83.61  ? 382 ASN A CA  1 
ATOM   3007 C  C   . ASN A 1 382 ? 17.544  -15.681 46.949 1.00 79.32  ? 382 ASN A C   1 
ATOM   3008 O  O   . ASN A 1 382 ? 17.027  -16.573 46.247 1.00 65.08  ? 382 ASN A O   1 
ATOM   3009 C  CB  . ASN A 1 382 ? 19.396  -16.883 48.057 1.00 86.19  ? 382 ASN A CB  1 
ATOM   3010 C  CG  . ASN A 1 382 ? 20.755  -17.419 47.705 1.00 86.67  ? 382 ASN A CG  1 
ATOM   3011 O  OD1 . ASN A 1 382 ? 21.506  -16.785 46.968 1.00 94.41  ? 382 ASN A OD1 1 
ATOM   3012 N  ND2 . ASN A 1 382 ? 21.067  -18.585 48.219 1.00 104.39 ? 382 ASN A ND2 1 
ATOM   3013 N  N   . LEU A 1 383 ? 16.890  -14.703 47.564 1.00 80.11  ? 383 LEU A N   1 
ATOM   3014 C  CA  . LEU A 1 383 ? 15.419  -14.570 47.553 1.00 75.55  ? 383 LEU A CA  1 
ATOM   3015 C  C   . LEU A 1 383 ? 15.006  -13.682 46.398 1.00 70.02  ? 383 LEU A C   1 
ATOM   3016 O  O   . LEU A 1 383 ? 15.755  -12.791 46.024 1.00 78.04  ? 383 LEU A O   1 
ATOM   3017 C  CB  . LEU A 1 383 ? 14.977  -13.974 48.883 1.00 77.78  ? 383 LEU A CB  1 
ATOM   3018 C  CG  . LEU A 1 383 ? 15.227  -14.913 50.050 1.00 78.86  ? 383 LEU A CG  1 
ATOM   3019 C  CD1 . LEU A 1 383 ? 14.749  -14.304 51.362 1.00 82.78  ? 383 LEU A CD1 1 
ATOM   3020 C  CD2 . LEU A 1 383 ? 14.557  -16.246 49.760 1.00 75.02  ? 383 LEU A CD2 1 
ATOM   3021 N  N   . LYS A 1 384 ? 13.837  -13.954 45.868 1.00 65.44  ? 384 LYS A N   1 
ATOM   3022 C  CA  . LYS A 1 384 ? 13.258  -13.149 44.792 1.00 66.71  ? 384 LYS A CA  1 
ATOM   3023 C  C   . LYS A 1 384 ? 11.763  -13.010 45.053 1.00 65.40  ? 384 LYS A C   1 
ATOM   3024 O  O   . LYS A 1 384 ? 11.073  -14.036 45.194 1.00 75.21  ? 384 LYS A O   1 
ATOM   3025 C  CB  . LYS A 1 384 ? 13.521  -13.807 43.443 1.00 73.80  ? 384 LYS A CB  1 
ATOM   3026 C  CG  . LYS A 1 384 ? 12.656  -13.242 42.328 1.00 78.58  ? 384 LYS A CG  1 
ATOM   3027 C  CD  . LYS A 1 384 ? 13.192  -13.472 40.953 1.00 75.75  ? 384 LYS A CD  1 
ATOM   3028 C  CE  . LYS A 1 384 ? 12.063  -13.345 39.968 1.00 79.69  ? 384 LYS A CE  1 
ATOM   3029 N  NZ  . LYS A 1 384 ? 12.403  -13.920 38.656 1.00 81.72  ? 384 LYS A NZ  1 
ATOM   3030 N  N   . LEU A 1 385 ? 11.298  -11.772 45.084 1.00 62.43  ? 385 LEU A N   1 
ATOM   3031 C  CA  . LEU A 1 385 ? 9.872   -11.435 45.234 1.00 63.76  ? 385 LEU A CA  1 
ATOM   3032 C  C   . LEU A 1 385 ? 9.342   -10.872 43.912 1.00 60.66  ? 385 LEU A C   1 
ATOM   3033 O  O   . LEU A 1 385 ? 9.979   -10.012 43.314 1.00 62.56  ? 385 LEU A O   1 
ATOM   3034 C  CB  . LEU A 1 385 ? 9.718   -10.445 46.389 1.00 64.09  ? 385 LEU A CB  1 
ATOM   3035 C  CG  . LEU A 1 385 ? 8.266   -10.186 46.778 1.00 72.11  ? 385 LEU A CG  1 
ATOM   3036 C  CD1 . LEU A 1 385 ? 8.108   -10.125 48.283 1.00 80.49  ? 385 LEU A CD1 1 
ATOM   3037 C  CD2 . LEU A 1 385 ? 7.735   -8.919  46.128 1.00 76.98  ? 385 LEU A CD2 1 
ATOM   3038 N  N   . ILE A 1 386 ? 8.202   -11.367 43.473 1.00 60.48  ? 386 ILE A N   1 
ATOM   3039 C  CA  . ILE A 1 386 ? 7.455   -10.789 42.334 1.00 58.94  ? 386 ILE A CA  1 
ATOM   3040 C  C   . ILE A 1 386 ? 6.157   -10.188 42.870 1.00 61.55  ? 386 ILE A C   1 
ATOM   3041 O  O   . ILE A 1 386 ? 5.465   -10.860 43.636 1.00 70.47  ? 386 ILE A O   1 
ATOM   3042 C  CB  . ILE A 1 386 ? 7.205   -11.887 41.304 1.00 56.20  ? 386 ILE A CB  1 
ATOM   3043 C  CG1 . ILE A 1 386 ? 8.526   -12.535 40.899 1.00 57.25  ? 386 ILE A CG1 1 
ATOM   3044 C  CG2 . ILE A 1 386 ? 6.436   -11.320 40.127 1.00 64.08  ? 386 ILE A CG2 1 
ATOM   3045 C  CD1 . ILE A 1 386 ? 8.397   -13.570 39.793 1.00 63.49  ? 386 ILE A CD1 1 
ATOM   3046 N  N   . GLU A 1 387 ? 5.855   -8.953  42.492 1.00 63.68  ? 387 GLU A N   1 
ATOM   3047 C  CA  . GLU A 1 387 ? 4.596   -8.258  42.852 1.00 63.94  ? 387 GLU A CA  1 
ATOM   3048 C  C   . GLU A 1 387 ? 3.756   -8.225  41.590 1.00 60.63  ? 387 GLU A C   1 
ATOM   3049 O  O   . GLU A 1 387 ? 4.265   -7.809  40.570 1.00 69.65  ? 387 GLU A O   1 
ATOM   3050 C  CB  . GLU A 1 387 ? 4.864   -6.847  43.393 1.00 65.25  ? 387 GLU A CB  1 
ATOM   3051 C  CG  . GLU A 1 387 ? 3.600   -6.082  43.751 1.00 74.74  ? 387 GLU A CG  1 
ATOM   3052 C  CD  . GLU A 1 387 ? 3.788   -4.796  44.550 1.00 82.58  ? 387 GLU A CD  1 
ATOM   3053 O  OE1 . GLU A 1 387 ? 4.939   -4.522  44.968 1.00 81.32  ? 387 GLU A OE1 1 
ATOM   3054 O  OE2 . GLU A 1 387 ? 2.775   -4.056  44.744 1.00 83.13  ? 387 GLU A OE2 1 
ATOM   3055 N  N   . PHE A 1 388 ? 2.516   -8.663  41.665 1.00 67.65  ? 388 PHE A N   1 
ATOM   3056 C  CA  . PHE A 1 388 ? 1.581   -8.670  40.516 1.00 69.81  ? 388 PHE A CA  1 
ATOM   3057 C  C   . PHE A 1 388 ? 0.650   -7.485  40.679 1.00 72.59  ? 388 PHE A C   1 
ATOM   3058 O  O   . PHE A 1 388 ? 0.039   -7.362  41.740 1.00 70.82  ? 388 PHE A O   1 
ATOM   3059 C  CB  . PHE A 1 388 ? 0.840   -9.997  40.475 1.00 76.83  ? 388 PHE A CB  1 
ATOM   3060 C  CG  . PHE A 1 388 ? 1.757   -11.140 40.145 1.00 73.71  ? 388 PHE A CG  1 
ATOM   3061 C  CD1 . PHE A 1 388 ? 2.554   -11.709 41.110 1.00 69.03  ? 388 PHE A CD1 1 
ATOM   3062 C  CD2 . PHE A 1 388 ? 1.839   -11.615 38.849 1.00 88.24  ? 388 PHE A CD2 1 
ATOM   3063 C  CE1 . PHE A 1 388 ? 3.407   -12.741 40.776 1.00 78.98  ? 388 PHE A CE1 1 
ATOM   3064 C  CE2 . PHE A 1 388 ? 2.692   -12.650 38.514 1.00 85.05  ? 388 PHE A CE2 1 
ATOM   3065 C  CZ  . PHE A 1 388 ? 3.476   -13.207 39.483 1.00 84.96  ? 388 PHE A CZ  1 
ATOM   3066 N  N   . TYR A 1 389 ? 0.596   -6.612  39.689 1.00 79.15  ? 389 TYR A N   1 
ATOM   3067 C  CA  . TYR A 1 389 ? 0.032   -5.260  39.897 1.00 74.36  ? 389 TYR A CA  1 
ATOM   3068 C  C   . TYR A 1 389 ? -1.486  -5.333  39.827 1.00 72.92  ? 389 TYR A C   1 
ATOM   3069 O  O   . TYR A 1 389 ? -2.112  -4.408  40.396 1.00 68.97  ? 389 TYR A O   1 
ATOM   3070 C  CB  . TYR A 1 389 ? 0.599   -4.275  38.882 1.00 71.04  ? 389 TYR A CB  1 
ATOM   3071 C  CG  . TYR A 1 389 ? 2.035   -3.937  39.127 1.00 64.92  ? 389 TYR A CG  1 
ATOM   3072 C  CD1 . TYR A 1 389 ? 2.573   -3.985  40.396 1.00 77.28  ? 389 TYR A CD1 1 
ATOM   3073 C  CD2 . TYR A 1 389 ? 2.858   -3.571  38.093 1.00 63.70  ? 389 TYR A CD2 1 
ATOM   3074 C  CE1 . TYR A 1 389 ? 3.903   -3.673  40.631 1.00 81.01  ? 389 TYR A CE1 1 
ATOM   3075 C  CE2 . TYR A 1 389 ? 4.191   -3.258  38.311 1.00 72.85  ? 389 TYR A CE2 1 
ATOM   3076 C  CZ  . TYR A 1 389 ? 4.726   -3.297  39.586 1.00 73.25  ? 389 TYR A CZ  1 
ATOM   3077 O  OH  . TYR A 1 389 ? 6.041   -2.963  39.810 1.00 62.39  ? 389 TYR A OH  1 
ATOM   3078 N  N   . GLU A 1 390 ? -2.039  -6.375  39.186 1.00 70.37  ? 390 GLU A N   1 
ATOM   3079 C  CA  . GLU A 1 390 ? -3.515  -6.505  39.024 1.00 71.70  ? 390 GLU A CA  1 
ATOM   3080 C  C   . GLU A 1 390 ? -4.206  -6.548  40.398 1.00 72.55  ? 390 GLU A C   1 
ATOM   3081 O  O   . GLU A 1 390 ? -5.207  -5.848  40.565 1.00 75.40  ? 390 GLU A O   1 
ATOM   3082 C  CB  . GLU A 1 390 ? -3.859  -7.739  38.204 1.00 72.42  ? 390 GLU A CB  1 
ATOM   3083 C  CG  . GLU A 1 390 ? -3.403  -7.655  36.775 1.00 75.80  ? 390 GLU A CG  1 
ATOM   3084 C  CD  . GLU A 1 390 ? -3.977  -8.757  35.902 1.00 84.38  ? 390 GLU A CD  1 
ATOM   3085 O  OE1 . GLU A 1 390 ? -3.564  -9.915  36.102 1.00 93.11  ? 390 GLU A OE1 1 
ATOM   3086 O  OE2 . GLU A 1 390 ? -4.828  -8.458  35.021 1.00 83.64  ? 390 GLU A OE2 1 
ATOM   3087 N  N   . ASP A 1 391 ? -3.679  -7.327  41.347 1.00 79.73  ? 391 ASP A N   1 
ATOM   3088 C  CA  . ASP A 1 391 ? -4.323  -7.632  42.653 1.00 78.92  ? 391 ASP A CA  1 
ATOM   3089 C  C   . ASP A 1 391 ? -3.332  -7.422  43.805 1.00 70.71  ? 391 ASP A C   1 
ATOM   3090 O  O   . ASP A 1 391 ? -3.611  -7.822  44.902 1.00 70.40  ? 391 ASP A O   1 
ATOM   3091 C  CB  . ASP A 1 391 ? -4.890  -9.060  42.630 1.00 84.70  ? 391 ASP A CB  1 
ATOM   3092 C  CG  . ASP A 1 391 ? -3.898  -10.159 42.261 1.00 82.24  ? 391 ASP A CG  1 
ATOM   3093 O  OD1 . ASP A 1 391 ? -2.696  -9.873  42.177 1.00 75.50  ? 391 ASP A OD1 1 
ATOM   3094 O  OD2 . ASP A 1 391 ? -4.342  -11.293 42.050 1.00 90.81  ? 391 ASP A OD2 1 
ATOM   3095 N  N   . SER A 1 392 ? -2.165  -6.860  43.566 1.00 75.68  ? 392 SER A N   1 
ATOM   3096 C  CA  . SER A 1 392 ? -1.161  -6.579  44.622 1.00 74.66  ? 392 SER A CA  1 
ATOM   3097 C  C   . SER A 1 392 ? -0.599  -7.842  45.304 1.00 69.96  ? 392 SER A C   1 
ATOM   3098 O  O   . SER A 1 392 ? 0.191   -7.652  46.240 1.00 56.63  ? 392 SER A O   1 
ATOM   3099 C  CB  . SER A 1 392 ? -1.735  -5.632  45.623 1.00 70.05  ? 392 SER A CB  1 
ATOM   3100 O  OG  . SER A 1 392 ? -1.830  -4.349  45.051 1.00 86.29  ? 392 SER A OG  1 
ATOM   3101 N  N   . HIS A 1 393 ? -0.885  -9.068  44.844 1.00 68.26  ? 393 HIS A N   1 
ATOM   3102 C  CA  . HIS A 1 393 ? -0.381  -10.298 45.522 1.00 70.79  ? 393 HIS A CA  1 
ATOM   3103 C  C   . HIS A 1 393 ? 1.104   -10.465 45.216 1.00 66.33  ? 393 HIS A C   1 
ATOM   3104 O  O   . HIS A 1 393 ? 1.568   -9.934  44.191 1.00 63.76  ? 393 HIS A O   1 
ATOM   3105 C  CB  . HIS A 1 393 ? -1.203  -11.546 45.169 1.00 73.93  ? 393 HIS A CB  1 
ATOM   3106 C  CG  . HIS A 1 393 ? -0.721  -12.356 44.011 1.00 75.67  ? 393 HIS A CG  1 
ATOM   3107 N  ND1 . HIS A 1 393 ? -1.233  -12.178 42.738 1.00 88.34  ? 393 HIS A ND1 1 
ATOM   3108 C  CD2 . HIS A 1 393 ? 0.146   -13.392 43.929 1.00 79.26  ? 393 HIS A CD2 1 
ATOM   3109 C  CE1 . HIS A 1 393 ? -0.691  -13.053 41.912 1.00 87.48  ? 393 HIS A CE1 1 
ATOM   3110 N  NE2 . HIS A 1 393 ? 0.160   -13.814 42.620 1.00 87.23  ? 393 HIS A NE2 1 
ATOM   3111 N  N   . VAL A 1 394 ? 1.831   -11.133 46.107 1.00 65.27  ? 394 VAL A N   1 
ATOM   3112 C  CA  . VAL A 1 394 ? 3.297   -11.320 45.936 1.00 66.18  ? 394 VAL A CA  1 
ATOM   3113 C  C   . VAL A 1 394 ? 3.637   -12.807 46.015 1.00 66.89  ? 394 VAL A C   1 
ATOM   3114 O  O   . VAL A 1 394 ? 2.966   -13.566 46.695 1.00 74.70  ? 394 VAL A O   1 
ATOM   3115 C  CB  . VAL A 1 394 ? 4.133   -10.474 46.918 1.00 65.92  ? 394 VAL A CB  1 
ATOM   3116 C  CG1 . VAL A 1 394 ? 3.874   -8.983  46.754 1.00 73.36  ? 394 VAL A CG1 1 
ATOM   3117 C  CG2 . VAL A 1 394 ? 3.942   -10.875 48.354 1.00 61.46  ? 394 VAL A CG2 1 
ATOM   3118 N  N   . GLU A 1 395 ? 4.648   -13.194 45.266 1.00 68.82  ? 395 GLU A N   1 
ATOM   3119 C  CA  . GLU A 1 395 ? 5.247   -14.535 45.322 1.00 68.98  ? 395 GLU A CA  1 
ATOM   3120 C  C   . GLU A 1 395 ? 6.695   -14.318 45.711 1.00 69.20  ? 395 GLU A C   1 
ATOM   3121 O  O   . GLU A 1 395 ? 7.264   -13.304 45.307 1.00 78.06  ? 395 GLU A O   1 
ATOM   3122 C  CB  . GLU A 1 395 ? 5.129   -15.259 43.986 1.00 66.15  ? 395 GLU A CB  1 
ATOM   3123 C  CG  . GLU A 1 395 ? 3.691   -15.445 43.530 1.00 72.71  ? 395 GLU A CG  1 
ATOM   3124 C  CD  . GLU A 1 395 ? 3.548   -15.970 42.097 1.00 84.19  ? 395 GLU A CD  1 
ATOM   3125 O  OE1 . GLU A 1 395 ? 4.586   -16.407 41.510 1.00 70.28  ? 395 GLU A OE1 1 
ATOM   3126 O  OE2 . GLU A 1 395 ? 2.398   -15.920 41.544 1.00 85.36  ? 395 GLU A OE2 1 
ATOM   3127 N  N   . LEU A 1 396 ? 7.235   -15.246 46.482 1.00 70.02  ? 396 LEU A N   1 
ATOM   3128 C  CA  . LEU A 1 396 ? 8.621   -15.212 46.980 1.00 62.56  ? 396 LEU A CA  1 
ATOM   3129 C  C   . LEU A 1 396 ? 9.214   -16.598 46.778 1.00 62.98  ? 396 LEU A C   1 
ATOM   3130 O  O   . LEU A 1 396 ? 8.610   -17.553 47.282 1.00 72.61  ? 396 LEU A O   1 
ATOM   3131 C  CB  . LEU A 1 396 ? 8.573   -14.827 48.454 1.00 59.81  ? 396 LEU A CB  1 
ATOM   3132 C  CG  . LEU A 1 396 ? 9.905   -14.884 49.188 1.00 66.79  ? 396 LEU A CG  1 
ATOM   3133 C  CD1 . LEU A 1 396 ? 10.925  -13.969 48.543 1.00 79.42  ? 396 LEU A CD1 1 
ATOM   3134 C  CD2 . LEU A 1 396 ? 9.722   -14.500 50.642 1.00 73.77  ? 396 LEU A CD2 1 
ATOM   3135 N  N   . TYR A 1 397 ? 10.362  -16.682 46.108 1.00 62.56  ? 397 TYR A N   1 
ATOM   3136 C  CA  . TYR A 1 397 ? 11.101  -17.943 45.873 1.00 63.83  ? 397 TYR A CA  1 
ATOM   3137 C  C   . TYR A 1 397 ? 12.523  -17.846 46.417 1.00 65.29  ? 397 TYR A C   1 
ATOM   3138 O  O   . TYR A 1 397 ? 13.029  -16.738 46.582 1.00 54.46  ? 397 TYR A O   1 
ATOM   3139 C  CB  . TYR A 1 397 ? 11.066  -18.252 44.391 1.00 63.90  ? 397 TYR A CB  1 
ATOM   3140 C  CG  . TYR A 1 397 ? 9.660   -18.292 43.867 1.00 69.18  ? 397 TYR A CG  1 
ATOM   3141 C  CD1 . TYR A 1 397 ? 8.902   -19.435 43.994 1.00 80.37  ? 397 TYR A CD1 1 
ATOM   3142 C  CD2 . TYR A 1 397 ? 9.090   -17.197 43.245 1.00 73.09  ? 397 TYR A CD2 1 
ATOM   3143 C  CE1 . TYR A 1 397 ? 7.616   -19.502 43.485 1.00 85.90  ? 397 TYR A CE1 1 
ATOM   3144 C  CE2 . TYR A 1 397 ? 7.804   -17.236 42.744 1.00 74.44  ? 397 TYR A CE2 1 
ATOM   3145 C  CZ  . TYR A 1 397 ? 7.070   -18.401 42.849 1.00 79.50  ? 397 TYR A CZ  1 
ATOM   3146 O  OH  . TYR A 1 397 ? 5.810   -18.455 42.334 1.00 73.37  ? 397 TYR A OH  1 
ATOM   3147 N  N   . ASP A 1 398 ? 13.095  -19.008 46.756 1.00 76.10  ? 398 ASP A N   1 
ATOM   3148 C  CA  . ASP A 1 398 ? 14.530  -19.195 47.104 1.00 75.76  ? 398 ASP A CA  1 
ATOM   3149 C  C   . ASP A 1 398 ? 15.203  -19.893 45.922 1.00 73.97  ? 398 ASP A C   1 
ATOM   3150 O  O   . ASP A 1 398 ? 14.906  -21.063 45.651 1.00 74.55  ? 398 ASP A O   1 
ATOM   3151 C  CB  . ASP A 1 398 ? 14.770  -19.984 48.395 1.00 73.88  ? 398 ASP A CB  1 
ATOM   3152 C  CG  . ASP A 1 398 ? 16.230  -19.905 48.803 1.00 83.35  ? 398 ASP A CG  1 
ATOM   3153 O  OD1 . ASP A 1 398 ? 17.080  -19.824 47.897 1.00 100.78 ? 398 ASP A OD1 1 
ATOM   3154 O  OD2 . ASP A 1 398 ? 16.515  -19.856 50.006 1.00 91.72  ? 398 ASP A OD2 1 
ATOM   3155 N  N   . LEU A 1 399 ? 16.067  -19.174 45.227 1.00 75.52  ? 399 LEU A N   1 
ATOM   3156 C  CA  . LEU A 1 399 ? 16.572  -19.629 43.921 1.00 79.80  ? 399 LEU A CA  1 
ATOM   3157 C  C   . LEU A 1 399 ? 17.746  -20.570 44.147 1.00 79.58  ? 399 LEU A C   1 
ATOM   3158 O  O   . LEU A 1 399 ? 18.123  -21.204 43.147 1.00 90.48  ? 399 LEU A O   1 
ATOM   3159 C  CB  . LEU A 1 399 ? 16.979  -18.419 43.082 1.00 83.63  ? 399 LEU A CB  1 
ATOM   3160 C  CG  . LEU A 1 399 ? 15.855  -17.457 42.706 1.00 75.12  ? 399 LEU A CG  1 
ATOM   3161 C  CD1 . LEU A 1 399 ? 16.431  -16.262 41.986 1.00 85.17  ? 399 LEU A CD1 1 
ATOM   3162 C  CD2 . LEU A 1 399 ? 14.817  -18.124 41.829 1.00 75.51  ? 399 LEU A CD2 1 
ATOM   3163 N  N   . SER A 1 400 ? 18.284  -20.667 45.376 1.00 71.75  ? 400 SER A N   1 
ATOM   3164 C  CA  . SER A 1 400 ? 19.309  -21.697 45.711 1.00 82.05  ? 400 SER A CA  1 
ATOM   3165 C  C   . SER A 1 400 ? 18.629  -23.056 45.865 1.00 81.13  ? 400 SER A C   1 
ATOM   3166 O  O   . SER A 1 400 ? 19.304  -24.056 45.678 1.00 96.05  ? 400 SER A O   1 
ATOM   3167 C  CB  . SER A 1 400 ? 20.090  -21.386 46.933 1.00 82.80  ? 400 SER A CB  1 
ATOM   3168 O  OG  . SER A 1 400 ? 19.208  -21.207 48.022 1.00 96.75  ? 400 SER A OG  1 
ATOM   3169 N  N   . GLU A 1 401 ? 17.333  -23.070 46.159 1.00 84.70  ? 401 GLU A N   1 
ATOM   3170 C  CA  . GLU A 1 401 ? 16.571  -24.300 46.475 1.00 86.43  ? 401 GLU A CA  1 
ATOM   3171 C  C   . GLU A 1 401 ? 15.460  -24.561 45.462 1.00 85.84  ? 401 GLU A C   1 
ATOM   3172 O  O   . GLU A 1 401 ? 14.853  -25.614 45.540 1.00 91.53  ? 401 GLU A O   1 
ATOM   3173 C  CB  . GLU A 1 401 ? 15.992  -24.124 47.867 1.00 89.13  ? 401 GLU A CB  1 
ATOM   3174 C  CG  . GLU A 1 401 ? 17.087  -23.915 48.880 1.00 101.71 ? 401 GLU A CG  1 
ATOM   3175 C  CD  . GLU A 1 401 ? 16.971  -24.862 50.055 1.00 117.91 ? 401 GLU A CD  1 
ATOM   3176 O  OE1 . GLU A 1 401 ? 15.996  -24.713 50.829 1.00 125.43 ? 401 GLU A OE1 1 
ATOM   3177 O  OE2 . GLU A 1 401 ? 17.832  -25.769 50.166 1.00 124.69 ? 401 GLU A OE2 1 
ATOM   3178 N  N   . ASP A 1 402 ? 15.205  -23.636 44.548 1.00 93.92  ? 402 ASP A N   1 
ATOM   3179 C  CA  . ASP A 1 402 ? 13.954  -23.619 43.758 1.00 83.05  ? 402 ASP A CA  1 
ATOM   3180 C  C   . ASP A 1 402 ? 14.170  -22.734 42.530 1.00 81.92  ? 402 ASP A C   1 
ATOM   3181 O  O   . ASP A 1 402 ? 13.329  -21.897 42.260 1.00 79.66  ? 402 ASP A O   1 
ATOM   3182 C  CB  . ASP A 1 402 ? 12.811  -23.145 44.655 1.00 77.48  ? 402 ASP A CB  1 
ATOM   3183 C  CG  . ASP A 1 402 ? 11.470  -23.215 43.967 1.00 80.81  ? 402 ASP A CG  1 
ATOM   3184 O  OD1 . ASP A 1 402 ? 11.350  -24.045 43.042 1.00 77.59  ? 402 ASP A OD1 1 
ATOM   3185 O  OD2 . ASP A 1 402 ? 10.565  -22.441 44.364 1.00 83.58  ? 402 ASP A OD2 1 
ATOM   3186 N  N   . ILE A 1 403 ? 15.274  -22.912 41.811 1.00 81.21  ? 403 ILE A N   1 
ATOM   3187 C  CA  . ILE A 1 403 ? 15.600  -22.064 40.629 1.00 80.28  ? 403 ILE A CA  1 
ATOM   3188 C  C   . ILE A 1 403 ? 14.364  -22.007 39.705 1.00 81.92  ? 403 ILE A C   1 
ATOM   3189 O  O   . ILE A 1 403 ? 14.210  -21.009 38.955 1.00 92.00  ? 403 ILE A O   1 
ATOM   3190 C  CB  . ILE A 1 403 ? 16.876  -22.585 39.925 1.00 85.26  ? 403 ILE A CB  1 
ATOM   3191 C  CG1 . ILE A 1 403 ? 17.704  -21.462 39.295 1.00 92.91  ? 403 ILE A CG1 1 
ATOM   3192 C  CG2 . ILE A 1 403 ? 16.544  -23.642 38.890 1.00 82.76  ? 403 ILE A CG2 1 
ATOM   3193 C  CD1 . ILE A 1 403 ? 19.182  -21.542 39.604 1.00 96.74  ? 403 ILE A CD1 1 
ATOM   3194 N  N   . GLY A 1 404 ? 13.488  -23.018 39.755 1.00 79.27  ? 404 GLY A N   1 
ATOM   3195 C  CA  . GLY A 1 404 ? 12.323  -23.142 38.850 1.00 84.28  ? 404 GLY A CA  1 
ATOM   3196 C  C   . GLY A 1 404 ? 11.076  -22.441 39.374 1.00 85.32  ? 404 GLY A C   1 
ATOM   3197 O  O   . GLY A 1 404 ? 10.019  -22.533 38.703 1.00 78.62  ? 404 GLY A O   1 
ATOM   3198 N  N   . GLU A 1 405 ? 11.172  -21.790 40.542 1.00 83.77  ? 405 GLU A N   1 
ATOM   3199 C  CA  . GLU A 1 405 ? 10.093  -20.972 41.159 1.00 76.96  ? 405 GLU A CA  1 
ATOM   3200 C  C   . GLU A 1 405 ? 8.794   -21.773 41.213 1.00 76.57  ? 405 GLU A C   1 
ATOM   3201 O  O   . GLU A 1 405 ? 7.783   -21.240 40.706 1.00 68.18  ? 405 GLU A O   1 
ATOM   3202 C  CB  . GLU A 1 405 ? 9.861   -19.699 40.347 1.00 92.08  ? 405 GLU A CB  1 
ATOM   3203 C  CG  . GLU A 1 405 ? 10.935  -18.641 40.541 1.00 99.42  ? 405 GLU A CG  1 
ATOM   3204 C  CD  . GLU A 1 405 ? 11.193  -17.780 39.314 1.00 104.15 ? 405 GLU A CD  1 
ATOM   3205 O  OE1 . GLU A 1 405 ? 11.635  -18.374 38.233 1.00 98.75  ? 405 GLU A OE1 1 
ATOM   3206 O  OE2 . GLU A 1 405 ? 10.952  -16.527 39.440 1.00 80.22  ? 405 GLU A OE2 1 
ATOM   3207 N  N   . ARG A 1 406 ? 8.804   -22.923 41.885 1.00 82.08  ? 406 ARG A N   1 
ATOM   3208 C  CA  . ARG A 1 406 ? 7.555   -23.706 42.047 1.00 81.08  ? 406 ARG A CA  1 
ATOM   3209 C  C   . ARG A 1 406 ? 7.032   -23.544 43.477 1.00 80.93  ? 406 ARG A C   1 
ATOM   3210 O  O   . ARG A 1 406 ? 5.805   -23.454 43.642 1.00 73.07  ? 406 ARG A O   1 
ATOM   3211 C  CB  . ARG A 1 406 ? 7.792   -25.176 41.701 1.00 102.83 ? 406 ARG A CB  1 
ATOM   3212 C  CG  . ARG A 1 406 ? 9.052   -25.770 42.311 1.00 119.96 ? 406 ARG A CG  1 
ATOM   3213 C  CD  . ARG A 1 406 ? 9.996   -26.305 41.252 1.00 121.38 ? 406 ARG A CD  1 
ATOM   3214 N  NE  . ARG A 1 406 ? 9.359   -26.436 39.950 1.00 135.72 ? 406 ARG A NE  1 
ATOM   3215 C  CZ  . ARG A 1 406 ? 8.717   -27.520 39.531 1.00 133.77 ? 406 ARG A CZ  1 
ATOM   3216 N  NH1 . ARG A 1 406 ? 8.619   -28.577 40.318 1.00 158.90 ? 406 ARG A NH1 1 
ATOM   3217 N  NH2 . ARG A 1 406 ? 8.171   -27.541 38.329 1.00 134.15 ? 406 ARG A NH2 1 
ATOM   3218 N  N   . HIS A 1 407 ? 7.924   -23.512 44.468 1.00 84.51  ? 407 HIS A N   1 
ATOM   3219 C  CA  . HIS A 1 407 ? 7.445   -23.437 45.887 1.00 90.94  ? 407 HIS A CA  1 
ATOM   3220 C  C   . HIS A 1 407 ? 7.485   -21.979 46.367 1.00 75.04  ? 407 HIS A C   1 
ATOM   3221 O  O   . HIS A 1 407 ? 8.569   -21.503 46.753 1.00 73.71  ? 407 HIS A O   1 
ATOM   3222 C  CB  . HIS A 1 407 ? 8.212   -24.369 46.873 1.00 106.02 ? 407 HIS A CB  1 
ATOM   3223 C  CG  . HIS A 1 407 ? 8.608   -25.686 46.293 1.00 127.13 ? 407 HIS A CG  1 
ATOM   3224 N  ND1 . HIS A 1 407 ? 7.690   -26.533 45.674 1.00 130.12 ? 407 HIS A ND1 1 
ATOM   3225 C  CD2 . HIS A 1 407 ? 9.817   -26.287 46.187 1.00 119.23 ? 407 HIS A CD2 1 
ATOM   3226 C  CE1 . HIS A 1 407 ? 8.319   -27.598 45.201 1.00 115.69 ? 407 HIS A CE1 1 
ATOM   3227 N  NE2 . HIS A 1 407 ? 9.625   -27.469 45.504 1.00 127.06 ? 407 HIS A NE2 1 
ATOM   3228 N  N   . ASN A 1 408 ? 6.318   -21.334 46.402 1.00 62.89  ? 408 ASN A N   1 
ATOM   3229 C  CA  . ASN A 1 408 ? 6.109   -19.934 46.858 1.00 62.84  ? 408 ASN A CA  1 
ATOM   3230 C  C   . ASN A 1 408 ? 6.193   -19.769 48.382 1.00 58.27  ? 408 ASN A C   1 
ATOM   3231 O  O   . ASN A 1 408 ? 5.232   -20.088 49.076 1.00 65.58  ? 408 ASN A O   1 
ATOM   3232 C  CB  . ASN A 1 408 ? 4.733   -19.435 46.415 1.00 63.58  ? 408 ASN A CB  1 
ATOM   3233 C  CG  . ASN A 1 408 ? 4.396   -18.062 46.964 1.00 67.89  ? 408 ASN A CG  1 
ATOM   3234 O  OD1 . ASN A 1 408 ? 5.264   -17.281 47.363 1.00 78.69  ? 408 ASN A OD1 1 
ATOM   3235 N  ND2 . ASN A 1 408 ? 3.123   -17.736 46.955 1.00 67.51  ? 408 ASN A ND2 1 
ATOM   3236 N  N   . LEU A 1 409 ? 7.197   -19.078 48.892 1.00 66.29  ? 409 LEU A N   1 
ATOM   3237 C  CA  . LEU A 1 409 ? 7.428   -18.984 50.363 1.00 73.05  ? 409 LEU A CA  1 
ATOM   3238 C  C   . LEU A 1 409 ? 6.678   -17.799 50.976 1.00 67.93  ? 409 LEU A C   1 
ATOM   3239 O  O   . LEU A 1 409 ? 6.877   -17.538 52.148 1.00 70.56  ? 409 LEU A O   1 
ATOM   3240 C  CB  . LEU A 1 409 ? 8.939   -18.904 50.605 1.00 73.12  ? 409 LEU A CB  1 
ATOM   3241 C  CG  . LEU A 1 409 ? 9.710   -20.034 49.920 1.00 82.37  ? 409 LEU A CG  1 
ATOM   3242 C  CD1 . LEU A 1 409 ? 11.181  -19.704 49.803 1.00 83.65  ? 409 LEU A CD1 1 
ATOM   3243 C  CD2 . LEU A 1 409 ? 9.504   -21.360 50.642 1.00 89.45  ? 409 LEU A CD2 1 
ATOM   3244 N  N   . ALA A 1 410 ? 5.833   -17.105 50.225 1.00 76.73  ? 410 ALA A N   1 
ATOM   3245 C  CA  . ALA A 1 410 ? 5.295   -15.796 50.660 1.00 84.16  ? 410 ALA A CA  1 
ATOM   3246 C  C   . ALA A 1 410 ? 4.465   -15.996 51.930 1.00 78.95  ? 410 ALA A C   1 
ATOM   3247 O  O   . ALA A 1 410 ? 4.520   -15.102 52.799 1.00 60.73  ? 410 ALA A O   1 
ATOM   3248 C  CB  . ALA A 1 410 ? 4.493   -15.149 49.555 1.00 87.71  ? 410 ALA A CB  1 
ATOM   3249 N  N   . LYS A 1 411 ? 3.751   -17.129 52.031 1.00 80.55  ? 411 LYS A N   1 
ATOM   3250 C  CA  . LYS A 1 411 ? 2.869   -17.413 53.192 1.00 77.67  ? 411 LYS A CA  1 
ATOM   3251 C  C   . LYS A 1 411 ? 3.761   -17.897 54.314 1.00 77.36  ? 411 LYS A C   1 
ATOM   3252 O  O   . LYS A 1 411 ? 3.508   -17.493 55.434 1.00 66.46  ? 411 LYS A O   1 
ATOM   3253 C  CB  . LYS A 1 411 ? 1.823   -18.493 52.936 1.00 82.15  ? 411 LYS A CB  1 
ATOM   3254 C  CG  . LYS A 1 411 ? 1.032   -18.346 51.650 1.00 102.24 ? 411 LYS A CG  1 
ATOM   3255 C  CD  . LYS A 1 411 ? -0.384  -17.863 51.808 1.00 107.28 ? 411 LYS A CD  1 
ATOM   3256 C  CE  . LYS A 1 411 ? -1.094  -17.827 50.471 1.00 119.28 ? 411 LYS A CE  1 
ATOM   3257 N  NZ  . LYS A 1 411 ? -2.175  -16.818 50.478 1.00 141.12 ? 411 LYS A NZ  1 
ATOM   3258 N  N   . GLU A 1 412 ? 4.763   -18.719 53.985 1.00 84.50  ? 412 GLU A N   1 
ATOM   3259 C  CA  . GLU A 1 412 ? 5.731   -19.264 54.974 1.00 80.17  ? 412 GLU A CA  1 
ATOM   3260 C  C   . GLU A 1 412 ? 6.595   -18.174 55.609 1.00 72.77  ? 412 GLU A C   1 
ATOM   3261 O  O   . GLU A 1 412 ? 6.840   -18.331 56.769 1.00 80.51  ? 412 GLU A O   1 
ATOM   3262 C  CB  . GLU A 1 412 ? 6.647   -20.319 54.369 1.00 83.59  ? 412 GLU A CB  1 
ATOM   3263 C  CG  . GLU A 1 412 ? 5.871   -21.524 53.894 1.00 104.37 ? 412 GLU A CG  1 
ATOM   3264 C  CD  . GLU A 1 412 ? 6.674   -22.810 53.911 1.00 120.69 ? 412 GLU A CD  1 
ATOM   3265 O  OE1 . GLU A 1 412 ? 7.890   -22.717 54.266 1.00 102.48 ? 412 GLU A OE1 1 
ATOM   3266 O  OE2 . GLU A 1 412 ? 6.080   -23.892 53.560 1.00 122.92 ? 412 GLU A OE2 1 
ATOM   3267 N  N   . MET A 1 413 ? 7.069   -17.145 54.900 1.00 77.63  ? 413 MET A N   1 
ATOM   3268 C  CA  . MET A 1 413 ? 8.014   -16.145 55.472 1.00 77.43  ? 413 MET A CA  1 
ATOM   3269 C  C   . MET A 1 413 ? 7.437   -14.782 55.221 1.00 76.36  ? 413 MET A C   1 
ATOM   3270 O  O   . MET A 1 413 ? 7.948   -14.025 54.424 1.00 92.80  ? 413 MET A O   1 
ATOM   3271 C  CB  . MET A 1 413 ? 9.387   -16.193 54.819 1.00 80.71  ? 413 MET A CB  1 
ATOM   3272 C  CG  . MET A 1 413 ? 9.895   -17.595 54.654 1.00 89.34  ? 413 MET A CG  1 
ATOM   3273 S  SD  . MET A 1 413 ? 11.308  -17.635 53.551 1.00 82.08  ? 413 MET A SD  1 
ATOM   3274 C  CE  . MET A 1 413 ? 12.371  -16.553 54.523 1.00 84.10  ? 413 MET A CE  1 
ATOM   3275 N  N   . PRO A 1 414 ? 6.345   -14.462 55.909 1.00 77.03  ? 414 PRO A N   1 
ATOM   3276 C  CA  . PRO A 1 414 ? 5.490   -13.350 55.510 1.00 79.77  ? 414 PRO A CA  1 
ATOM   3277 C  C   . PRO A 1 414 ? 6.135   -11.981 55.774 1.00 75.11  ? 414 PRO A C   1 
ATOM   3278 O  O   . PRO A 1 414 ? 5.665   -11.009 55.220 1.00 67.91  ? 414 PRO A O   1 
ATOM   3279 C  CB  . PRO A 1 414 ? 4.253   -13.556 56.386 1.00 87.18  ? 414 PRO A CB  1 
ATOM   3280 C  CG  . PRO A 1 414 ? 4.784   -14.268 57.622 1.00 95.03  ? 414 PRO A CG  1 
ATOM   3281 C  CD  . PRO A 1 414 ? 5.950   -15.110 57.158 1.00 83.10  ? 414 PRO A CD  1 
ATOM   3282 N  N   . ASP A 1 415 ? 7.208   -11.962 56.571 1.00 74.78  ? 415 ASP A N   1 
ATOM   3283 C  CA  . ASP A 1 415 ? 7.922   -10.729 56.974 1.00 72.64  ? 415 ASP A CA  1 
ATOM   3284 C  C   . ASP A 1 415 ? 9.059   -10.481 55.988 1.00 74.24  ? 415 ASP A C   1 
ATOM   3285 O  O   . ASP A 1 415 ? 9.274   -9.302  55.698 1.00 75.37  ? 415 ASP A O   1 
ATOM   3286 C  CB  . ASP A 1 415 ? 8.467   -10.822 58.395 1.00 85.83  ? 415 ASP A CB  1 
ATOM   3287 C  CG  . ASP A 1 415 ? 7.491   -11.454 59.367 1.00 90.01  ? 415 ASP A CG  1 
ATOM   3288 O  OD1 . ASP A 1 415 ? 6.694   -10.691 59.914 1.00 81.24  ? 415 ASP A OD1 1 
ATOM   3289 O  OD2 . ASP A 1 415 ? 7.519   -12.718 59.543 1.00 96.83  ? 415 ASP A OD2 1 
ATOM   3290 N  N   . LYS A 1 416 ? 9.723   -11.517 55.490 1.00 68.58  ? 416 LYS A N   1 
ATOM   3291 C  CA  . LYS A 1 416 ? 10.725  -11.253 54.434 1.00 67.19  ? 416 LYS A CA  1 
ATOM   3292 C  C   . LYS A 1 416 ? 9.930   -10.769 53.232 1.00 64.03  ? 416 LYS A C   1 
ATOM   3293 O  O   . LYS A 1 416 ? 10.360  -9.811  52.580 1.00 82.31  ? 416 LYS A O   1 
ATOM   3294 C  CB  . LYS A 1 416 ? 11.520  -12.507 54.084 1.00 67.94  ? 416 LYS A CB  1 
ATOM   3295 C  CG  . LYS A 1 416 ? 12.935  -12.247 53.592 1.00 78.83  ? 416 LYS A CG  1 
ATOM   3296 C  CD  . LYS A 1 416 ? 13.478  -10.912 54.045 1.00 91.66  ? 416 LYS A CD  1 
ATOM   3297 C  CE  . LYS A 1 416 ? 14.984  -10.904 54.188 1.00 92.69  ? 416 LYS A CE  1 
ATOM   3298 N  NZ  . LYS A 1 416 ? 15.592  -9.741  53.499 1.00 100.53 ? 416 LYS A NZ  1 
ATOM   3299 N  N   . ALA A 1 417 ? 8.790   -11.402 52.982 1.00 63.18  ? 417 ALA A N   1 
ATOM   3300 C  CA  . ALA A 1 417 ? 7.921   -10.923 51.886 1.00 70.83  ? 417 ALA A CA  1 
ATOM   3301 C  C   . ALA A 1 417 ? 7.672   -9.427  52.106 1.00 69.43  ? 417 ALA A C   1 
ATOM   3302 O  O   . ALA A 1 417 ? 7.900   -8.635  51.185 1.00 75.13  ? 417 ALA A O   1 
ATOM   3303 C  CB  . ALA A 1 417 ? 6.642   -11.717 51.799 1.00 67.39  ? 417 ALA A CB  1 
ATOM   3304 N  N   . ALA A 1 418 ? 7.241   -9.040  53.297 1.00 68.05  ? 418 ALA A N   1 
ATOM   3305 C  CA  . ALA A 1 418 ? 6.826   -7.650  53.563 1.00 64.95  ? 418 ALA A CA  1 
ATOM   3306 C  C   . ALA A 1 418 ? 8.031   -6.744  53.338 1.00 65.26  ? 418 ALA A C   1 
ATOM   3307 O  O   . ALA A 1 418 ? 7.840   -5.677  52.685 1.00 64.74  ? 418 ALA A O   1 
ATOM   3308 C  CB  . ALA A 1 418 ? 6.261   -7.537  54.948 1.00 59.33  ? 418 ALA A CB  1 
ATOM   3309 N  N   . GLU A 1 419 ? 9.195   -7.180  53.840 1.00 67.77  ? 419 GLU A N   1 
ATOM   3310 C  CA  . GLU A 1 419 ? 10.478  -6.434  53.779 1.00 72.10  ? 419 GLU A CA  1 
ATOM   3311 C  C   . GLU A 1 419 ? 10.784  -6.169  52.305 1.00 68.51  ? 419 GLU A C   1 
ATOM   3312 O  O   . GLU A 1 419 ? 10.972  -4.999  51.935 1.00 78.65  ? 419 GLU A O   1 
ATOM   3313 C  CB  . GLU A 1 419 ? 11.610  -7.211  54.460 1.00 76.70  ? 419 GLU A CB  1 
ATOM   3314 C  CG  . GLU A 1 419 ? 12.829  -6.366  54.764 1.00 84.15  ? 419 GLU A CG  1 
ATOM   3315 C  CD  . GLU A 1 419 ? 14.103  -7.142  55.032 1.00 89.48  ? 419 GLU A CD  1 
ATOM   3316 O  OE1 . GLU A 1 419 ? 14.152  -7.893  56.033 1.00 90.11  ? 419 GLU A OE1 1 
ATOM   3317 O  OE2 . GLU A 1 419 ? 15.039  -6.980  54.230 1.00 114.21 ? 419 GLU A OE2 1 
ATOM   3318 N  N   . LEU A 1 420 ? 10.765  -7.206  51.478 1.00 59.13  ? 420 LEU A N   1 
ATOM   3319 C  CA  . LEU A 1 420 ? 11.233  -7.085  50.082 1.00 59.63  ? 420 LEU A CA  1 
ATOM   3320 C  C   . LEU A 1 420 ? 10.233  -6.239  49.309 1.00 61.77  ? 420 LEU A C   1 
ATOM   3321 O  O   . LEU A 1 420 ? 10.707  -5.279  48.697 1.00 73.21  ? 420 LEU A O   1 
ATOM   3322 C  CB  . LEU A 1 420 ? 11.456  -8.470  49.479 1.00 63.29  ? 420 LEU A CB  1 
ATOM   3323 C  CG  . LEU A 1 420 ? 12.543  -9.273  50.197 1.00 67.60  ? 420 LEU A CG  1 
ATOM   3324 C  CD1 . LEU A 1 420 ? 12.757  -10.618 49.541 1.00 69.97  ? 420 LEU A CD1 1 
ATOM   3325 C  CD2 . LEU A 1 420 ? 13.858  -8.507  50.257 1.00 72.89  ? 420 LEU A CD2 1 
ATOM   3326 N  N   . GLN A 1 421 ? 8.929   -6.538  49.383 1.00 64.40  ? 421 GLN A N   1 
ATOM   3327 C  CA  . GLN A 1 421 ? 7.861   -5.695  48.769 1.00 70.14  ? 421 GLN A CA  1 
ATOM   3328 C  C   . GLN A 1 421 ? 8.171   -4.227  49.130 1.00 63.35  ? 421 GLN A C   1 
ATOM   3329 O  O   . GLN A 1 421 ? 8.154   -3.373  48.236 1.00 67.10  ? 421 GLN A O   1 
ATOM   3330 C  CB  . GLN A 1 421 ? 6.444   -6.148  49.186 1.00 80.39  ? 421 GLN A CB  1 
ATOM   3331 C  CG  . GLN A 1 421 ? 5.275   -5.537  48.400 1.00 82.12  ? 421 GLN A CG  1 
ATOM   3332 C  CD  . GLN A 1 421 ? 4.982   -4.085  48.734 1.00 105.39 ? 421 GLN A CD  1 
ATOM   3333 O  OE1 . GLN A 1 421 ? 5.150   -3.626  49.875 1.00 110.11 ? 421 GLN A OE1 1 
ATOM   3334 N  NE2 . GLN A 1 421 ? 4.530   -3.330  47.736 1.00 106.43 ? 421 GLN A NE2 1 
ATOM   3335 N  N   . ALA A 1 422 ? 8.460   -3.912  50.385 1.00 60.85  ? 422 ALA A N   1 
ATOM   3336 C  CA  . ALA A 1 422 ? 8.658   -2.504  50.798 1.00 64.03  ? 422 ALA A CA  1 
ATOM   3337 C  C   . ALA A 1 422 ? 9.934   -1.951  50.154 1.00 64.68  ? 422 ALA A C   1 
ATOM   3338 O  O   . ALA A 1 422 ? 9.891   -0.795  49.705 1.00 64.34  ? 422 ALA A O   1 
ATOM   3339 C  CB  . ALA A 1 422 ? 8.673   -2.371  52.302 1.00 65.83  ? 422 ALA A CB  1 
ATOM   3340 N  N   . LYS A 1 423 ? 11.016  -2.740  50.115 1.00 65.66  ? 423 LYS A N   1 
ATOM   3341 C  CA  . LYS A 1 423 ? 12.295  -2.324  49.478 1.00 66.44  ? 423 LYS A CA  1 
ATOM   3342 C  C   . LYS A 1 423 ? 11.985  -1.991  48.019 1.00 59.84  ? 423 LYS A C   1 
ATOM   3343 O  O   . LYS A 1 423 ? 12.461  -0.964  47.560 1.00 63.45  ? 423 LYS A O   1 
ATOM   3344 C  CB  . LYS A 1 423 ? 13.411  -3.374  49.602 1.00 76.88  ? 423 LYS A CB  1 
ATOM   3345 C  CG  . LYS A 1 423 ? 14.038  -3.532  51.000 1.00 87.86  ? 423 LYS A CG  1 
ATOM   3346 C  CD  . LYS A 1 423 ? 15.489  -4.052  51.059 1.00 90.28  ? 423 LYS A CD  1 
ATOM   3347 C  CE  . LYS A 1 423 ? 16.327  -3.479  49.923 1.00 109.95 ? 423 LYS A CE  1 
ATOM   3348 N  NZ  . LYS A 1 423 ? 17.786  -3.482  50.198 1.00 123.43 ? 423 LYS A NZ  1 
ATOM   3349 N  N   . LEU A 1 424 ? 11.193  -2.828  47.346 1.00 58.99  ? 424 LEU A N   1 
ATOM   3350 C  CA  . LEU A 1 424 ? 10.815  -2.676  45.909 1.00 58.62  ? 424 LEU A CA  1 
ATOM   3351 C  C   . LEU A 1 424 ? 9.984   -1.404  45.771 1.00 60.58  ? 424 LEU A C   1 
ATOM   3352 O  O   . LEU A 1 424 ? 10.302  -0.625  44.866 1.00 64.91  ? 424 LEU A O   1 
ATOM   3353 C  CB  . LEU A 1 424 ? 10.053  -3.916  45.417 1.00 57.72  ? 424 LEU A CB  1 
ATOM   3354 C  CG  . LEU A 1 424 ? 9.425   -3.877  44.023 1.00 58.79  ? 424 LEU A CG  1 
ATOM   3355 C  CD1 . LEU A 1 424 ? 10.466  -3.771  42.947 1.00 64.97  ? 424 LEU A CD1 1 
ATOM   3356 C  CD2 . LEU A 1 424 ? 8.630   -5.133  43.745 1.00 63.84  ? 424 LEU A CD2 1 
ATOM   3357 N  N   . LYS A 1 425 ? 9.019   -1.174  46.671 1.00 61.48  ? 425 LYS A N   1 
ATOM   3358 C  CA  . LYS A 1 425 ? 8.147   0.030   46.627 1.00 61.61  ? 425 LYS A CA  1 
ATOM   3359 C  C   . LYS A 1 425 ? 9.024   1.273   46.747 1.00 58.10  ? 425 LYS A C   1 
ATOM   3360 O  O   . LYS A 1 425 ? 8.741   2.265   46.023 1.00 58.43  ? 425 LYS A O   1 
ATOM   3361 C  CB  . LYS A 1 425 ? 7.055   0.042   47.701 1.00 67.81  ? 425 LYS A CB  1 
ATOM   3362 C  CG  . LYS A 1 425 ? 5.969   1.097   47.486 1.00 81.68  ? 425 LYS A CG  1 
ATOM   3363 C  CD  . LYS A 1 425 ? 4.649   0.841   48.258 1.00 92.93  ? 425 LYS A CD  1 
ATOM   3364 C  CE  . LYS A 1 425 ? 4.074   2.092   48.917 1.00 105.33 ? 425 LYS A CE  1 
ATOM   3365 N  NZ  . LYS A 1 425 ? 4.395   2.225   50.374 1.00 116.37 ? 425 LYS A NZ  1 
ATOM   3366 N  N   . ALA A 1 426 ? 10.048  1.214   47.599 1.00 55.64  ? 426 ALA A N   1 
ATOM   3367 C  CA  . ALA A 1 426 ? 10.954  2.358   47.852 1.00 60.57  ? 426 ALA A CA  1 
ATOM   3368 C  C   . ALA A 1 426 ? 11.752  2.642   46.584 1.00 61.74  ? 426 ALA A C   1 
ATOM   3369 O  O   . ALA A 1 426 ? 11.883  3.791   46.204 1.00 79.00  ? 426 ALA A O   1 
ATOM   3370 C  CB  . ALA A 1 426 ? 11.862  2.108   49.026 1.00 59.81  ? 426 ALA A CB  1 
ATOM   3371 N  N   . TRP A 1 427 ? 12.238  1.610   45.927 1.00 66.32  ? 427 TRP A N   1 
ATOM   3372 C  CA  . TRP A 1 427 ? 12.948  1.769   44.637 1.00 63.50  ? 427 TRP A CA  1 
ATOM   3373 C  C   . TRP A 1 427 ? 11.977  2.337   43.599 1.00 61.98  ? 427 TRP A C   1 
ATOM   3374 O  O   . TRP A 1 427 ? 12.342  3.297   42.916 1.00 59.52  ? 427 TRP A O   1 
ATOM   3375 C  CB  . TRP A 1 427 ? 13.530  0.435   44.189 1.00 57.44  ? 427 TRP A CB  1 
ATOM   3376 C  CG  . TRP A 1 427 ? 14.070  0.486   42.805 1.00 52.37  ? 427 TRP A CG  1 
ATOM   3377 C  CD1 . TRP A 1 427 ? 15.273  0.990   42.401 1.00 59.77  ? 427 TRP A CD1 1 
ATOM   3378 C  CD2 . TRP A 1 427 ? 13.401  0.061   41.622 1.00 51.31  ? 427 TRP A CD2 1 
ATOM   3379 N  NE1 . TRP A 1 427 ? 15.424  0.880   41.047 1.00 59.30  ? 427 TRP A NE1 1 
ATOM   3380 C  CE2 . TRP A 1 427 ? 14.278  0.310   40.547 1.00 58.33  ? 427 TRP A CE2 1 
ATOM   3381 C  CE3 . TRP A 1 427 ? 12.154  -0.495  41.366 1.00 53.21  ? 427 TRP A CE3 1 
ATOM   3382 C  CZ2 . TRP A 1 427 ? 13.935  -0.014  39.239 1.00 56.39  ? 427 TRP A CZ2 1 
ATOM   3383 C  CZ3 . TRP A 1 427 ? 11.827  -0.836  40.074 1.00 53.60  ? 427 TRP A CZ3 1 
ATOM   3384 C  CH2 . TRP A 1 427 ? 12.708  -0.600  39.028 1.00 55.31  ? 427 TRP A CH2 1 
ATOM   3385 N  N   . ARG A 1 428 ? 10.768  1.789   43.499 1.00 58.08  ? 428 ARG A N   1 
ATOM   3386 C  CA  . ARG A 1 428 ? 9.792   2.304   42.512 1.00 63.17  ? 428 ARG A CA  1 
ATOM   3387 C  C   . ARG A 1 428 ? 9.700   3.831   42.668 1.00 65.78  ? 428 ARG A C   1 
ATOM   3388 O  O   . ARG A 1 428 ? 9.542   4.531   41.665 1.00 80.33  ? 428 ARG A O   1 
ATOM   3389 C  CB  . ARG A 1 428 ? 8.416   1.648   42.645 1.00 62.23  ? 428 ARG A CB  1 
ATOM   3390 C  CG  . ARG A 1 428 ? 8.296   0.310   41.919 1.00 67.88  ? 428 ARG A CG  1 
ATOM   3391 C  CD  . ARG A 1 428 ? 6.859   -0.080  41.561 1.00 74.70  ? 428 ARG A CD  1 
ATOM   3392 N  NE  . ARG A 1 428 ? 6.018   -0.107  42.748 1.00 79.80  ? 428 ARG A NE  1 
ATOM   3393 C  CZ  . ARG A 1 428 ? 5.745   -1.198  43.475 1.00 89.90  ? 428 ARG A CZ  1 
ATOM   3394 N  NH1 . ARG A 1 428 ? 6.164   -2.394  43.106 1.00 86.26  ? 428 ARG A NH1 1 
ATOM   3395 N  NH2 . ARG A 1 428 ? 5.021   -1.091  44.574 1.00 114.89 ? 428 ARG A NH2 1 
ATOM   3396 N  N   . ALA A 1 429 ? 9.777   4.333   43.887 1.00 59.43  ? 429 ALA A N   1 
ATOM   3397 C  CA  . ALA A 1 429 ? 9.599   5.765   44.181 1.00 62.81  ? 429 ALA A CA  1 
ATOM   3398 C  C   . ALA A 1 429 ? 10.869  6.504   43.821 1.00 61.61  ? 429 ALA A C   1 
ATOM   3399 O  O   . ALA A 1 429 ? 10.766  7.633   43.362 1.00 75.09  ? 429 ALA A O   1 
ATOM   3400 C  CB  . ALA A 1 429 ? 9.296   5.971   45.643 1.00 64.88  ? 429 ALA A CB  1 
ATOM   3401 N  N   . SER A 1 430 ? 12.011  5.903   44.132 1.00 64.87  ? 430 SER A N   1 
ATOM   3402 C  CA  . SER A 1 430 ? 13.339  6.514   43.919 1.00 64.52  ? 430 SER A CA  1 
ATOM   3403 C  C   . SER A 1 430 ? 13.407  6.904   42.457 1.00 61.33  ? 430 SER A C   1 
ATOM   3404 O  O   . SER A 1 430 ? 14.027  7.894   42.218 1.00 81.19  ? 430 SER A O   1 
ATOM   3405 C  CB  . SER A 1 430 ? 14.490  5.611   44.297 1.00 73.41  ? 430 SER A CB  1 
ATOM   3406 O  OG  . SER A 1 430 ? 14.738  4.608   43.307 1.00 66.49  ? 430 SER A OG  1 
ATOM   3407 N  N   . VAL A 1 431 ? 12.747  6.174   41.553 1.00 61.53  ? 431 VAL A N   1 
ATOM   3408 C  CA  . VAL A 1 431 ? 12.867  6.375   40.071 1.00 65.85  ? 431 VAL A CA  1 
ATOM   3409 C  C   . VAL A 1 431 ? 11.540  6.858   39.467 1.00 64.38  ? 431 VAL A C   1 
ATOM   3410 O  O   . VAL A 1 431 ? 11.405  6.897   38.216 1.00 56.77  ? 431 VAL A O   1 
ATOM   3411 C  CB  . VAL A 1 431 ? 13.326  5.082   39.368 1.00 64.84  ? 431 VAL A CB  1 
ATOM   3412 C  CG1 . VAL A 1 431 ? 14.646  4.592   39.911 1.00 68.11  ? 431 VAL A CG1 1 
ATOM   3413 C  CG2 . VAL A 1 431 ? 12.280  3.983   39.454 1.00 66.08  ? 431 VAL A CG2 1 
ATOM   3414 N  N   . ARG A 1 432 ? 10.562  7.167   40.305 1.00 70.48  ? 432 ARG A N   1 
ATOM   3415 C  CA  . ARG A 1 432 ? 9.203   7.531   39.833 1.00 71.75  ? 432 ARG A CA  1 
ATOM   3416 C  C   . ARG A 1 432 ? 8.725   6.552   38.762 1.00 62.61  ? 432 ARG A C   1 
ATOM   3417 O  O   . ARG A 1 432 ? 8.356   6.997   37.679 1.00 66.99  ? 432 ARG A O   1 
ATOM   3418 C  CB  . ARG A 1 432 ? 9.252   8.944   39.270 1.00 72.00  ? 432 ARG A CB  1 
ATOM   3419 C  CG  . ARG A 1 432 ? 9.684   9.950   40.314 1.00 84.47  ? 432 ARG A CG  1 
ATOM   3420 C  CD  . ARG A 1 432 ? 9.072   11.277  40.012 1.00 89.12  ? 432 ARG A CD  1 
ATOM   3421 N  NE  . ARG A 1 432 ? 9.862   12.260  40.703 1.00 90.83  ? 432 ARG A NE  1 
ATOM   3422 C  CZ  . ARG A 1 432 ? 9.520   13.519  40.785 1.00 99.00  ? 432 ARG A CZ  1 
ATOM   3423 N  NH1 . ARG A 1 432 ? 8.377   13.935  40.253 1.00 100.88 ? 432 ARG A NH1 1 
ATOM   3424 N  NH2 . ARG A 1 432 ? 10.330  14.349  41.412 1.00 120.93 ? 432 ARG A NH2 1 
ATOM   3425 N  N   . ALA A 1 433 ? 8.756   5.260   39.052 1.00 59.65  ? 433 ALA A N   1 
ATOM   3426 C  CA  . ALA A 1 433 ? 8.216   4.225   38.150 1.00 71.14  ? 433 ALA A CA  1 
ATOM   3427 C  C   . ALA A 1 433 ? 6.769   4.570   37.893 1.00 68.90  ? 433 ALA A C   1 
ATOM   3428 O  O   . ALA A 1 433 ? 6.096   4.857   38.903 1.00 67.78  ? 433 ALA A O   1 
ATOM   3429 C  CB  . ALA A 1 433 ? 8.291   2.874   38.774 1.00 75.59  ? 433 ALA A CB  1 
ATOM   3430 N  N   . THR A 1 434 ? 6.390   4.640   36.611 1.00 71.14  ? 434 THR A N   1 
ATOM   3431 C  CA  . THR A 1 434 ? 4.984   4.900   36.223 1.00 76.38  ? 434 THR A CA  1 
ATOM   3432 C  C   . THR A 1 434 ? 4.206   3.615   36.481 1.00 69.61  ? 434 THR A C   1 
ATOM   3433 O  O   . THR A 1 434 ? 4.698   2.540   36.092 1.00 55.84  ? 434 THR A O   1 
ATOM   3434 C  CB  . THR A 1 434 ? 4.883   5.338   34.757 1.00 79.70  ? 434 THR A CB  1 
ATOM   3435 O  OG1 . THR A 1 434 ? 5.626   6.548   34.606 1.00 52.62  ? 434 THR A OG1 1 
ATOM   3436 C  CG2 . THR A 1 434 ? 3.456   5.555   34.306 1.00 82.05  ? 434 THR A CG2 1 
ATOM   3437 N  N   . MET A 1 435 ? 3.035   3.727   37.095 1.00 74.27  ? 435 MET A N   1 
ATOM   3438 C  CA  . MET A 1 435 ? 2.277   2.521   37.489 1.00 65.71  ? 435 MET A CA  1 
ATOM   3439 C  C   . MET A 1 435 ? 1.101   2.361   36.537 1.00 63.46  ? 435 MET A C   1 
ATOM   3440 O  O   . MET A 1 435 ? 0.639   3.323   35.936 1.00 74.59  ? 435 MET A O   1 
ATOM   3441 C  CB  . MET A 1 435 ? 1.777   2.632   38.930 1.00 61.76  ? 435 MET A CB  1 
ATOM   3442 C  CG  . MET A 1 435 ? 2.889   2.613   39.953 1.00 65.13  ? 435 MET A CG  1 
ATOM   3443 S  SD  . MET A 1 435 ? 3.799   1.073   40.062 1.00 76.83  ? 435 MET A SD  1 
ATOM   3444 C  CE  . MET A 1 435 ? 2.508   -0.042  40.620 1.00 84.59  ? 435 MET A CE  1 
ATOM   3445 N  N   . PRO A 1 436 ? 0.592   1.132   36.350 1.00 58.05  ? 436 PRO A N   1 
ATOM   3446 C  CA  . PRO A 1 436 ? -0.582  0.911   35.525 1.00 59.41  ? 436 PRO A CA  1 
ATOM   3447 C  C   . PRO A 1 436 ? -1.787  1.367   36.337 1.00 63.45  ? 436 PRO A C   1 
ATOM   3448 O  O   . PRO A 1 436 ? -1.588  1.802   37.442 1.00 67.13  ? 436 PRO A O   1 
ATOM   3449 C  CB  . PRO A 1 436 ? -0.560  -0.581  35.267 1.00 59.89  ? 436 PRO A CB  1 
ATOM   3450 C  CG  . PRO A 1 436 ? 0.088   -1.130  36.503 1.00 62.38  ? 436 PRO A CG  1 
ATOM   3451 C  CD  . PRO A 1 436 ? 1.108   -0.106  36.930 1.00 61.16  ? 436 PRO A CD  1 
ATOM   3452 N  N   . THR A 1 437 ? -2.976  1.321   35.746 1.00 68.66  ? 437 THR A N   1 
ATOM   3453 C  CA  . THR A 1 437 ? -4.195  1.946   36.315 1.00 68.56  ? 437 THR A CA  1 
ATOM   3454 C  C   . THR A 1 437 ? -5.339  0.959   36.225 1.00 68.47  ? 437 THR A C   1 
ATOM   3455 O  O   . THR A 1 437 ? -5.363  0.139   35.272 1.00 65.79  ? 437 THR A O   1 
ATOM   3456 C  CB  . THR A 1 437 ? -4.504  3.245   35.571 1.00 78.84  ? 437 THR A CB  1 
ATOM   3457 O  OG1 . THR A 1 437 ? -3.785  4.156   36.403 1.00 68.54  ? 437 THR A OG1 1 
ATOM   3458 C  CG2 . THR A 1 437 ? -5.984  3.571   35.373 1.00 75.18  ? 437 THR A CG2 1 
ATOM   3459 N  N   . VAL A 1 438 ? -6.280  1.064   37.145 1.00 66.23  ? 438 VAL A N   1 
ATOM   3460 C  CA  . VAL A 1 438 ? -7.486  0.201   37.033 1.00 72.28  ? 438 VAL A CA  1 
ATOM   3461 C  C   . VAL A 1 438 ? -8.313  0.617   35.808 1.00 67.56  ? 438 VAL A C   1 
ATOM   3462 O  O   . VAL A 1 438 ? -8.731  1.793   35.705 1.00 69.28  ? 438 VAL A O   1 
ATOM   3463 C  CB  . VAL A 1 438 ? -8.302  0.224   38.324 1.00 76.03  ? 438 VAL A CB  1 
ATOM   3464 C  CG1 . VAL A 1 438 ? -9.470  -0.755  38.213 1.00 82.73  ? 438 VAL A CG1 1 
ATOM   3465 C  CG2 . VAL A 1 438 ? -7.389  -0.054  39.517 1.00 75.94  ? 438 VAL A CG2 1 
ATOM   3466 N  N   . ASN A 1 439 ? -8.532  -0.335  34.904 1.00 66.35  ? 439 ASN A N   1 
ATOM   3467 C  CA  . ASN A 1 439 ? -9.310  -0.132  33.658 1.00 64.40  ? 439 ASN A CA  1 
ATOM   3468 C  C   . ASN A 1 439 ? -10.777 0.047   34.026 1.00 71.22  ? 439 ASN A C   1 
ATOM   3469 O  O   . ASN A 1 439 ? -11.386 -0.853  34.610 1.00 80.60  ? 439 ASN A O   1 
ATOM   3470 C  CB  . ASN A 1 439 ? -9.098  -1.295  32.696 1.00 62.80  ? 439 ASN A CB  1 
ATOM   3471 C  CG  . ASN A 1 439 ? -9.909  -1.154  31.430 1.00 62.80  ? 439 ASN A CG  1 
ATOM   3472 O  OD1 . ASN A 1 439 ? -10.374 -0.064  31.111 1.00 65.32  ? 439 ASN A OD1 1 
ATOM   3473 N  ND2 . ASN A 1 439 ? -10.094 -2.253  30.708 1.00 60.80  ? 439 ASN A ND2 1 
ATOM   3474 N  N   . PRO A 1 440 ? -11.399 1.198   33.684 1.00 76.87  ? 440 PRO A N   1 
ATOM   3475 C  CA  . PRO A 1 440 ? -12.812 1.409   33.961 1.00 78.64  ? 440 PRO A CA  1 
ATOM   3476 C  C   . PRO A 1 440 ? -13.669 0.346   33.272 1.00 79.99  ? 440 PRO A C   1 
ATOM   3477 O  O   . PRO A 1 440 ? -14.703 0.081   33.800 1.00 97.54  ? 440 PRO A O   1 
ATOM   3478 C  CB  . PRO A 1 440 ? -13.128 2.773   33.345 1.00 84.41  ? 440 PRO A CB  1 
ATOM   3479 C  CG  . PRO A 1 440 ? -11.789 3.464   33.245 1.00 86.50  ? 440 PRO A CG  1 
ATOM   3480 C  CD  . PRO A 1 440 ? -10.819 2.341   32.964 1.00 85.29  ? 440 PRO A CD  1 
ATOM   3481 N  N   . ASN A 1 441 ? -13.222 -0.208  32.136 1.00 75.43  ? 441 ASN A N   1 
ATOM   3482 C  CA  . ASN A 1 441 ? -13.993 -1.194  31.327 1.00 79.41  ? 441 ASN A CA  1 
ATOM   3483 C  C   . ASN A 1 441 ? -13.599 -2.624  31.651 1.00 84.95  ? 441 ASN A C   1 
ATOM   3484 O  O   . ASN A 1 441 ? -13.910 -3.512  30.808 1.00 86.90  ? 441 ASN A O   1 
ATOM   3485 C  CB  . ASN A 1 441 ? -13.833 -0.994  29.828 1.00 80.92  ? 441 ASN A CB  1 
ATOM   3486 C  CG  . ASN A 1 441 ? -14.783 0.077   29.367 1.00 102.73 ? 441 ASN A CG  1 
ATOM   3487 O  OD1 . ASN A 1 441 ? -15.090 1.013   30.116 1.00 95.71  ? 441 ASN A OD1 1 
ATOM   3488 N  ND2 . ASN A 1 441 ? -15.286 -0.091  28.161 1.00 131.80 ? 441 ASN A ND2 1 
ATOM   3489 N  N   . TYR A 1 442 ? -12.979 -2.833  32.817 1.00 81.03  ? 442 TYR A N   1 
ATOM   3490 C  CA  . TYR A 1 442 ? -12.654 -4.178  33.329 1.00 77.48  ? 442 TYR A CA  1 
ATOM   3491 C  C   . TYR A 1 442 ? -13.954 -4.962  33.388 1.00 81.30  ? 442 TYR A C   1 
ATOM   3492 O  O   . TYR A 1 442 ? -14.868 -4.458  34.075 1.00 81.50  ? 442 TYR A O   1 
ATOM   3493 C  CB  . TYR A 1 442 ? -12.083 -4.131  34.738 1.00 80.72  ? 442 TYR A CB  1 
ATOM   3494 C  CG  . TYR A 1 442 ? -11.979 -5.495  35.374 1.00 83.11  ? 442 TYR A CG  1 
ATOM   3495 C  CD1 . TYR A 1 442 ? -11.594 -6.599  34.625 1.00 79.91  ? 442 TYR A CD1 1 
ATOM   3496 C  CD2 . TYR A 1 442 ? -12.251 -5.689  36.720 1.00 78.34  ? 442 TYR A CD2 1 
ATOM   3497 C  CE1 . TYR A 1 442 ? -11.481 -7.856  35.193 1.00 77.53  ? 442 TYR A CE1 1 
ATOM   3498 C  CE2 . TYR A 1 442 ? -12.130 -6.943  37.304 1.00 77.51  ? 442 TYR A CE2 1 
ATOM   3499 C  CZ  . TYR A 1 442 ? -11.724 -8.020  36.538 1.00 76.56  ? 442 TYR A CZ  1 
ATOM   3500 O  OH  . TYR A 1 442 ? -11.592 -9.270  37.043 1.00 85.77  ? 442 TYR A OH  1 
ATOM   3501 N  N   . ASP A 1 443 ? -14.025 -6.087  32.671 1.00 80.12  ? 443 ASP A N   1 
ATOM   3502 C  CA  . ASP A 1 443 ? -15.167 -7.039  32.684 1.00 91.43  ? 443 ASP A CA  1 
ATOM   3503 C  C   . ASP A 1 443 ? -14.579 -8.436  32.821 1.00 79.63  ? 443 ASP A C   1 
ATOM   3504 O  O   . ASP A 1 443 ? -14.047 -8.979  31.852 1.00 87.66  ? 443 ASP A O   1 
ATOM   3505 C  CB  . ASP A 1 443 ? -16.064 -6.875  31.444 1.00 112.63 ? 443 ASP A CB  1 
ATOM   3506 C  CG  . ASP A 1 443 ? -17.110 -7.962  31.244 1.00 108.09 ? 443 ASP A CG  1 
ATOM   3507 O  OD1 . ASP A 1 443 ? -17.489 -8.614  32.245 1.00 100.34 ? 443 ASP A OD1 1 
ATOM   3508 O  OD2 . ASP A 1 443 ? -17.526 -8.151  30.086 1.00 105.00 ? 443 ASP A OD2 1 
ATOM   3509 N  N   . PRO A 1 444 ? -14.680 -9.051  34.021 1.00 76.77  ? 444 PRO A N   1 
ATOM   3510 C  CA  . PRO A 1 444 ? -14.005 -10.316 34.319 1.00 74.76  ? 444 PRO A CA  1 
ATOM   3511 C  C   . PRO A 1 444 ? -14.415 -11.433 33.366 1.00 75.65  ? 444 PRO A C   1 
ATOM   3512 O  O   . PRO A 1 444 ? -13.603 -12.294 33.166 1.00 71.20  ? 444 PRO A O   1 
ATOM   3513 C  CB  . PRO A 1 444 ? -14.457 -10.708 35.723 1.00 67.42  ? 444 PRO A CB  1 
ATOM   3514 C  CG  . PRO A 1 444 ? -14.933 -9.403  36.329 1.00 76.74  ? 444 PRO A CG  1 
ATOM   3515 C  CD  . PRO A 1 444 ? -15.451 -8.569  35.172 1.00 76.28  ? 444 PRO A CD  1 
ATOM   3516 N  N   . ALA A 1 445 ? -15.633 -11.373 32.816 1.00 80.14  ? 445 ALA A N   1 
ATOM   3517 C  CA  . ALA A 1 445 ? -16.141 -12.376 31.856 1.00 90.45  ? 445 ALA A CA  1 
ATOM   3518 C  C   . ALA A 1 445 ? -15.193 -12.426 30.675 1.00 89.10  ? 445 ALA A C   1 
ATOM   3519 O  O   . ALA A 1 445 ? -14.748 -13.539 30.334 1.00 90.82  ? 445 ALA A O   1 
ATOM   3520 C  CB  . ALA A 1 445 ? -17.522 -12.040 31.375 1.00 105.38 ? 445 ALA A CB  1 
ATOM   3521 N  N   . ARG A 1 446 ? -14.907 -11.262 30.088 1.00 92.91  ? 446 ARG A N   1 
ATOM   3522 C  CA  . ARG A 1 446 ? -14.211 -11.219 28.780 1.00 108.47 ? 446 ARG A CA  1 
ATOM   3523 C  C   . ARG A 1 446 ? -12.809 -10.644 28.962 1.00 88.95  ? 446 ARG A C   1 
ATOM   3524 O  O   . ARG A 1 446 ? -12.252 -10.141 28.006 1.00 85.03  ? 446 ARG A O   1 
ATOM   3525 C  CB  . ARG A 1 446 ? -15.082 -10.479 27.770 1.00 117.56 ? 446 ARG A CB  1 
ATOM   3526 C  CG  . ARG A 1 446 ? -16.177 -11.334 27.133 1.00 122.16 ? 446 ARG A CG  1 
ATOM   3527 C  CD  . ARG A 1 446 ? -17.119 -10.460 26.330 1.00 123.35 ? 446 ARG A CD  1 
ATOM   3528 N  NE  . ARG A 1 446 ? -17.223 -9.189  27.055 1.00 142.39 ? 446 ARG A NE  1 
ATOM   3529 C  CZ  . ARG A 1 446 ? -17.085 -7.954  26.546 1.00 137.20 ? 446 ARG A CZ  1 
ATOM   3530 N  NH1 . ARG A 1 446 ? -16.866 -7.766  25.251 1.00 144.42 ? 446 ARG A NH1 1 
ATOM   3531 N  NH2 . ARG A 1 446 ? -17.194 -6.902  27.351 1.00 109.82 ? 446 ARG A NH2 1 
ATOM   3532 N  N   . ALA A 1 447 ? -12.238 -10.833 30.139 1.00 82.35  ? 447 ALA A N   1 
ATOM   3533 C  CA  . ALA A 1 447 ? -10.898 -10.341 30.509 1.00 79.75  ? 447 ALA A CA  1 
ATOM   3534 C  C   . ALA A 1 447 ? -9.814  -11.350 30.133 1.00 75.95  ? 447 ALA A C   1 
ATOM   3535 O  O   . ALA A 1 447 ? -8.649  -10.973 30.186 1.00 86.60  ? 447 ALA A O   1 
ATOM   3536 C  CB  . ALA A 1 447 ? -10.859 -10.075 31.984 1.00 85.01  ? 447 ALA A CB  1 
ATOM   3537 N  N   . ASP A 1 448 ? -10.156 -12.591 29.808 1.00 80.94  ? 448 ASP A N   1 
ATOM   3538 C  CA  . ASP A 1 448 ? -9.128  -13.581 29.406 1.00 88.89  ? 448 ASP A CA  1 
ATOM   3539 C  C   . ASP A 1 448 ? -8.711  -13.234 27.977 1.00 86.91  ? 448 ASP A C   1 
ATOM   3540 O  O   . ASP A 1 448 ? -9.573  -13.154 27.092 1.00 88.20  ? 448 ASP A O   1 
ATOM   3541 C  CB  . ASP A 1 448 ? -9.595  -15.031 29.573 1.00 98.67  ? 448 ASP A CB  1 
ATOM   3542 C  CG  . ASP A 1 448 ? -8.511  -16.043 29.247 1.00 96.57  ? 448 ASP A CG  1 
ATOM   3543 O  OD1 . ASP A 1 448 ? -7.348  -15.777 29.570 1.00 125.36 ? 448 ASP A OD1 1 
ATOM   3544 O  OD2 . ASP A 1 448 ? -8.828  -17.065 28.650 1.00 91.16  ? 448 ASP A OD2 1 
ATOM   3545 N  N   . GLN A 1 449 ? -7.422  -13.002 27.785 1.00 95.89  ? 449 GLN A N   1 
ATOM   3546 C  CA  . GLN A 1 449 ? -6.848  -12.594 26.484 1.00 97.40  ? 449 GLN A CA  1 
ATOM   3547 C  C   . GLN A 1 449 ? -6.521  -13.857 25.690 1.00 85.90  ? 449 GLN A C   1 
ATOM   3548 O  O   . GLN A 1 449 ? -6.330  -13.749 24.491 1.00 74.60  ? 449 GLN A O   1 
ATOM   3549 C  CB  . GLN A 1 449 ? -5.631  -11.708 26.737 1.00 104.23 ? 449 GLN A CB  1 
ATOM   3550 C  CG  . GLN A 1 449 ? -5.865  -10.665 27.828 1.00 99.41  ? 449 GLN A CG  1 
ATOM   3551 C  CD  . GLN A 1 449 ? -4.871  -9.538  27.731 1.00 85.47  ? 449 GLN A CD  1 
ATOM   3552 O  OE1 . GLN A 1 449 ? -4.173  -9.424  26.731 1.00 65.79  ? 449 GLN A OE1 1 
ATOM   3553 N  NE2 . GLN A 1 449 ? -4.814  -8.696  28.755 1.00 80.71  ? 449 GLN A NE2 1 
ATOM   3554 N  N   . GLY A 1 450 ? -6.468  -15.007 26.357 1.00 84.46  ? 450 GLY A N   1 
ATOM   3555 C  CA  . GLY A 1 450 ? -6.343  -16.314 25.697 1.00 85.46  ? 450 GLY A CA  1 
ATOM   3556 C  C   . GLY A 1 450 ? -4.964  -16.507 25.106 1.00 81.59  ? 450 GLY A C   1 
ATOM   3557 O  O   . GLY A 1 450 ? -4.848  -17.177 24.049 1.00 70.47  ? 450 GLY A O   1 
ATOM   3558 N  N   . LEU A 1 451 ? -3.942  -15.957 25.757 1.00 84.89  ? 451 LEU A N   1 
ATOM   3559 C  CA  . LEU A 1 451 ? -2.541  -16.220 25.350 1.00 91.85  ? 451 LEU A CA  1 
ATOM   3560 C  C   . LEU A 1 451 ? -2.146  -17.509 26.058 1.00 88.95  ? 451 LEU A C   1 
ATOM   3561 O  O   . LEU A 1 451 ? -2.406  -17.626 27.295 1.00 78.28  ? 451 LEU A O   1 
ATOM   3562 C  CB  . LEU A 1 451 ? -1.616  -15.048 25.710 1.00 104.74 ? 451 LEU A CB  1 
ATOM   3563 C  CG  . LEU A 1 451 ? -2.168  -13.635 25.473 1.00 96.70  ? 451 LEU A CG  1 
ATOM   3564 C  CD1 . LEU A 1 451 ? -1.355  -12.587 26.235 1.00 95.49  ? 451 LEU A CD1 1 
ATOM   3565 C  CD2 . LEU A 1 451 ? -2.226  -13.312 23.983 1.00 86.01  ? 451 LEU A CD2 1 
ATOM   3566 N  N   . THR A 1 452 ? -1.568  -18.442 25.305 1.00 97.33  ? 452 THR A N   1 
ATOM   3567 C  CA  . THR A 1 452 ? -1.210  -19.794 25.804 1.00 95.37  ? 452 THR A CA  1 
ATOM   3568 C  C   . THR A 1 452 ? -0.059  -19.679 26.804 1.00 85.10  ? 452 THR A C   1 
ATOM   3569 O  O   . THR A 1 452 ? 0.199   -20.635 27.448 1.00 81.40  ? 452 THR A O   1 
ATOM   3570 C  CB  . THR A 1 452 ? -0.884  -20.770 24.663 1.00 91.18  ? 452 THR A CB  1 
ATOM   3571 O  OG1 . THR A 1 452 ? 0.114   -20.160 23.859 1.00 95.07  ? 452 THR A OG1 1 
ATOM   3572 C  CG2 . THR A 1 452 ? -2.079  -21.127 23.798 1.00 96.51  ? 452 THR A CG2 1 
ATOM   3573 N  N   . GLY A 1 453 ? 0.620   -18.549 26.924 1.00 92.14  ? 453 GLY A N   1 
ATOM   3574 C  CA  . GLY A 1 453 ? 1.702   -18.435 27.917 1.00 80.75  ? 453 GLY A CA  1 
ATOM   3575 C  C   . GLY A 1 453 ? 1.223   -18.190 29.353 1.00 78.27  ? 453 GLY A C   1 
ATOM   3576 O  O   . GLY A 1 453 ? 2.088   -18.203 30.254 1.00 83.07  ? 453 GLY A O   1 
ATOM   3577 N  N   . ALA A 1 454 ? -0.057  -17.900 29.554 1.00 77.81  ? 454 ALA A N   1 
ATOM   3578 C  CA  . ALA A 1 454 ? -0.517  -17.552 30.915 1.00 91.71  ? 454 ALA A CA  1 
ATOM   3579 C  C   . ALA A 1 454 ? -0.182  -18.699 31.862 1.00 105.85 ? 454 ALA A C   1 
ATOM   3580 O  O   . ALA A 1 454 ? -1.016  -19.604 31.979 1.00 106.99 ? 454 ALA A O   1 
ATOM   3581 C  CB  . ALA A 1 454 ? -1.991  -17.279 30.893 1.00 89.40  ? 454 ALA A CB  1 
ATOM   3582 N  N   . ASP A 1 455 ? 0.981   -18.647 32.516 1.00 126.05 ? 455 ASP A N   1 
ATOM   3583 C  CA  . ASP A 1 455 ? 1.439   -19.753 33.403 1.00 154.93 ? 455 ASP A CA  1 
ATOM   3584 C  C   . ASP A 1 455 ? 0.236   -20.447 34.062 1.00 167.26 ? 455 ASP A C   1 
ATOM   3585 O  O   . ASP A 1 455 ? -0.505  -19.770 34.800 1.00 102.85 ? 455 ASP A O   1 
ATOM   3586 C  CB  . ASP A 1 455 ? 2.469   -19.243 34.415 1.00 115.68 ? 455 ASP A CB  1 
ATOM   3587 C  CG  . ASP A 1 455 ? 3.900   -19.427 33.948 1.00 103.40 ? 455 ASP A CG  1 
ATOM   3588 O  OD1 . ASP A 1 455 ? 4.088   -19.755 32.763 1.00 125.89 ? 455 ASP A OD1 1 
ATOM   3589 O  OD2 . ASP A 1 455 ? 4.810   -19.241 34.771 1.00 114.15 ? 455 ASP A OD2 1 
ATOM   3590 N  N   . PRO A 1 456 ? 0.015   -21.763 33.832 1.00 180.68 ? 456 PRO A N   1 
ATOM   3591 C  CA  . PRO A 1 456 ? 0.754   -22.830 34.520 1.00 172.96 ? 456 PRO A CA  1 
ATOM   3592 C  C   . PRO A 1 456 ? 2.179   -23.025 33.989 1.00 175.58 ? 456 PRO A C   1 
ATOM   3593 O  O   . PRO A 1 456 ? 2.313   -23.443 32.855 1.00 144.99 ? 456 PRO A O   1 
ATOM   3594 C  CB  . PRO A 1 456 ? -0.022  -24.112 34.181 1.00 145.18 ? 456 PRO A CB  1 
ATOM   3595 C  CG  . PRO A 1 456 ? -1.326  -23.631 33.587 1.00 147.01 ? 456 PRO A CG  1 
ATOM   3596 C  CD  . PRO A 1 456 ? -0.982  -22.319 32.920 1.00 139.43 ? 456 PRO A CD  1 
ATOM   3597 N  N   . ALA A 1 457 ? 3.190   -22.741 34.815 1.00 168.92 ? 457 ALA A N   1 
ATOM   3598 C  CA  . ALA A 1 457 ? 4.619   -22.905 34.409 1.00 146.45 ? 457 ALA A CA  1 
ATOM   3599 C  C   . ALA A 1 457 ? 4.715   -22.741 32.873 1.00 135.26 ? 457 ALA A C   1 
ATOM   3600 O  O   . ALA A 1 457 ? 5.644   -22.347 32.143 1.00 82.52  ? 457 ALA A O   1 
ATOM   3601 C  CB  . ALA A 1 457 ? 5.188   -24.227 34.920 1.00 101.37 ? 457 ALA A CB  1 
HETATM 3602 CA CA  . CA  B 2 .   ? 14.327  -9.521  22.648 1.00 55.36  ? 501 CA  A CA  1 
HETATM 3603 CA CA  . CA  C 2 .   ? 22.345  11.433  23.417 1.00 113.43 ? 502 CA  A CA  1 
HETATM 3604 C  C1  . GOL D 3 .   ? 8.037   -8.061  19.351 1.00 96.19  ? 503 GOL A C1  1 
HETATM 3605 O  O1  . GOL D 3 .   ? 9.142   -8.123  20.257 1.00 80.86  ? 503 GOL A O1  1 
HETATM 3606 C  C2  . GOL D 3 .   ? 7.101   -9.257  19.484 1.00 95.72  ? 503 GOL A C2  1 
HETATM 3607 O  O2  . GOL D 3 .   ? 6.440   -9.266  20.753 1.00 83.82  ? 503 GOL A O2  1 
HETATM 3608 C  C3  . GOL D 3 .   ? 6.067   -9.327  18.380 1.00 80.12  ? 503 GOL A C3  1 
HETATM 3609 O  O3  . GOL D 3 .   ? 6.688   -9.131  17.118 1.00 73.58  ? 503 GOL A O3  1 
HETATM 3610 O  O   . HOH E 4 .   ? 19.035  -2.965  20.179 1.00 30.00  ? 601 HOH A O   1 
HETATM 3611 O  O   . HOH E 4 .   ? 17.647  6.227   20.702 1.00 30.00  ? 602 HOH A O   1 
HETATM 3612 O  O   . HOH E 4 .   ? 20.135  -8.570  19.186 1.00 30.00  ? 603 HOH A O   1 
HETATM 3613 O  O   . HOH E 4 .   ? 1.150   -16.739 24.571 1.00 30.00  ? 604 HOH A O   1 
HETATM 3614 O  O   . HOH E 4 .   ? 28.211  -12.007 14.323 1.00 84.33  ? 605 HOH A O   1 
HETATM 3615 O  O   . HOH E 4 .   ? 0.704   -3.130  43.402 1.00 46.66  ? 606 HOH A O   1 
HETATM 3616 O  O   . HOH E 4 .   ? 21.346  -12.137 12.938 1.00 30.00  ? 607 HOH A O   1 
HETATM 3617 O  O   . HOH E 4 .   ? 11.262  -21.592 47.015 1.00 55.87  ? 608 HOH A O   1 
HETATM 3618 O  O   . HOH E 4 .   ? 15.627  15.462  15.473 0.33 30.00  ? 609 HOH A O   1 
HETATM 3619 O  O   . HOH E 4 .   ? 21.399  14.942  23.065 1.00 59.85  ? 610 HOH A O   1 
HETATM 3620 O  O   . HOH E 4 .   ? 20.434  -17.223 12.591 1.00 70.77  ? 611 HOH A O   1 
HETATM 3621 O  O   . HOH E 4 .   ? 20.889  -19.600 41.606 1.00 49.61  ? 612 HOH A O   1 
HETATM 3622 O  O   . HOH E 4 .   ? 15.099  -9.197  15.632 1.00 30.00  ? 613 HOH A O   1 
HETATM 3623 O  O   . HOH E 4 .   ? 9.207   3.615   17.621 1.00 74.30  ? 614 HOH A O   1 
HETATM 3624 O  O   . HOH E 4 .   ? 20.631  -21.513 9.142  1.00 87.08  ? 615 HOH A O   1 
HETATM 3625 O  O   . HOH E 4 .   ? 7.446   -17.694 13.540 1.00 60.45  ? 616 HOH A O   1 
HETATM 3626 O  O   . HOH E 4 .   ? 22.923  13.588  25.786 1.00 44.91  ? 617 HOH A O   1 
HETATM 3627 O  O   . HOH E 4 .   ? 16.187  1.643   4.379  1.00 60.95  ? 618 HOH A O   1 
HETATM 3628 O  O   . HOH E 4 .   ? 4.748   -12.286 35.104 1.00 52.50  ? 619 HOH A O   1 
HETATM 3629 O  O   . HOH E 4 .   ? 15.646  -3.692  55.556 1.00 57.13  ? 620 HOH A O   1 
HETATM 3630 O  O   . HOH E 4 .   ? 20.748  16.105  20.535 1.00 52.21  ? 621 HOH A O   1 
HETATM 3631 O  O   . HOH E 4 .   ? 6.201   10.385  34.290 1.00 35.42  ? 622 HOH A O   1 
HETATM 3632 O  O   . HOH E 4 .   ? 40.595  -23.086 23.151 1.00 51.71  ? 623 HOH A O   1 
HETATM 3633 O  O   . HOH E 4 .   ? 13.773  15.706  29.947 1.00 61.47  ? 624 HOH A O   1 
HETATM 3634 O  O   . HOH E 4 .   ? 45.008  -14.505 34.030 1.00 51.47  ? 625 HOH A O   1 
HETATM 3635 O  O   . HOH E 4 .   ? 7.796   10.084  32.606 1.00 49.08  ? 626 HOH A O   1 
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